data_9DH7
# 
_entry.id   9DH7 
# 
_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   9DH7         pdb_00009dh7 10.2210/pdb9dh7/pdb 
WWPDB D_1000288099 ?            ?                   
EMDB  EMD-46858    ?            ?                   
# 
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 ? 
# 
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' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DH7 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-03 
_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 the motor domain from full-length human dynein-1 in 5mM AMPPNP with 5mM Mg2+' 
_pdbx_database_related.db_id          EMD-46858 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Cryo-EM Reveals the Mechanochemical Cycle of Reactive Full-length Human Dynein-1.' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_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 'Zhang, K.' 2 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     1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytoplasmic dynein heavy chain 1,Dynein heavy chain,cytosolic' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 'MAGNESIUM ION'             MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    SER n 
1 3    GLU n 
1 4    PRO n 
1 5    GLY n 
1 6    GLY n 
1 7    GLY n 
1 8    GLY n 
1 9    GLY n 
1 10   GLU n 
1 11   ASP n 
1 12   GLY n 
1 13   SER n 
1 14   ALA n 
1 15   GLY n 
1 16   LEU n 
1 17   GLU n 
1 18   VAL n 
1 19   SER n 
1 20   ALA n 
1 21   VAL n 
1 22   GLN n 
1 23   ASN n 
1 24   VAL n 
1 25   ALA n 
1 26   ASP n 
1 27   VAL n 
1 28   SER n 
1 29   VAL n 
1 30   LEU n 
1 31   GLN n 
1 32   LYS n 
1 33   HIS n 
1 34   LEU n 
1 35   ARG n 
1 36   LYS n 
1 37   LEU n 
1 38   VAL n 
1 39   PRO n 
1 40   LEU n 
1 41   LEU n 
1 42   LEU n 
1 43   GLU n 
1 44   ASP n 
1 45   GLY n 
1 46   GLY n 
1 47   GLU n 
1 48   ALA n 
1 49   PRO n 
1 50   ALA n 
1 51   ALA n 
1 52   LEU n 
1 53   GLU n 
1 54   ALA n 
1 55   ALA n 
1 56   LEU n 
1 57   GLU n 
1 58   GLU n 
1 59   LYS n 
1 60   SER n 
1 61   ALA n 
1 62   LEU n 
1 63   GLU n 
1 64   GLN n 
1 65   MET n 
1 66   ARG n 
1 67   LYS n 
1 68   PHE n 
1 69   LEU n 
1 70   SER n 
1 71   ASP n 
1 72   PRO n 
1 73   GLN n 
1 74   VAL n 
1 75   HIS n 
1 76   THR n 
1 77   VAL n 
1 78   LEU n 
1 79   VAL n 
1 80   GLU n 
1 81   ARG n 
1 82   SER n 
1 83   THR n 
1 84   LEU n 
1 85   LYS n 
1 86   GLU n 
1 87   ASP n 
1 88   VAL n 
1 89   GLY n 
1 90   ASP n 
1 91   GLU n 
1 92   GLY n 
1 93   GLU n 
1 94   GLU n 
1 95   GLU n 
1 96   LYS n 
1 97   GLU n 
1 98   PHE n 
1 99   ILE n 
1 100  SER n 
1 101  TYR n 
1 102  ASN n 
1 103  ILE n 
1 104  ASN n 
1 105  ILE n 
1 106  ASP n 
1 107  ILE n 
1 108  HIS n 
1 109  TYR n 
1 110  GLY n 
1 111  VAL n 
1 112  LYS n 
1 113  SER n 
1 114  ASN n 
1 115  SER n 
1 116  LEU n 
1 117  ALA n 
1 118  PHE n 
1 119  ILE n 
1 120  LYS n 
1 121  ARG n 
1 122  THR n 
1 123  PRO n 
1 124  VAL n 
1 125  ILE n 
1 126  ASP n 
1 127  ALA n 
1 128  ASP n 
1 129  LYS n 
1 130  PRO n 
1 131  VAL n 
1 132  SER n 
1 133  SER n 
1 134  GLN n 
1 135  LEU n 
1 136  ARG n 
1 137  VAL n 
1 138  LEU n 
1 139  THR n 
1 140  LEU n 
1 141  SER n 
1 142  GLU n 
1 143  ASP n 
1 144  SER n 
1 145  PRO n 
1 146  TYR n 
1 147  GLU n 
1 148  THR n 
1 149  LEU n 
1 150  HIS n 
1 151  SER n 
1 152  PHE n 
1 153  ILE n 
1 154  SER n 
1 155  ASN n 
1 156  ALA n 
1 157  VAL n 
1 158  ALA n 
1 159  PRO n 
1 160  PHE n 
1 161  PHE n 
1 162  LYS n 
1 163  SER n 
1 164  TYR n 
1 165  ILE n 
1 166  ARG n 
1 167  GLU n 
1 168  SER n 
1 169  GLY n 
1 170  LYS n 
1 171  ALA n 
1 172  ASP n 
1 173  ARG n 
1 174  ASP n 
1 175  GLY n 
1 176  ASP n 
1 177  LYS n 
1 178  MET n 
1 179  ALA n 
1 180  PRO n 
1 181  SER n 
1 182  VAL n 
1 183  GLU n 
1 184  LYS n 
1 185  LYS n 
1 186  ILE n 
1 187  ALA n 
1 188  GLU n 
1 189  LEU n 
1 190  GLU n 
1 191  MET n 
1 192  GLY n 
1 193  LEU n 
1 194  LEU n 
1 195  HIS n 
1 196  LEU n 
1 197  GLN n 
1 198  GLN n 
1 199  ASN n 
1 200  ILE n 
1 201  GLU n 
1 202  ILE n 
1 203  PRO n 
1 204  GLU n 
1 205  ILE n 
1 206  SER n 
1 207  LEU n 
1 208  PRO n 
1 209  ILE n 
1 210  HIS n 
1 211  PRO n 
1 212  MET n 
1 213  ILE n 
1 214  THR n 
1 215  ASN n 
1 216  VAL n 
1 217  ALA n 
1 218  LYS n 
1 219  GLN n 
1 220  CYS n 
1 221  TYR n 
1 222  GLU n 
1 223  ARG n 
1 224  GLY n 
1 225  GLU n 
1 226  LYS n 
1 227  PRO n 
1 228  LYS n 
1 229  VAL n 
1 230  THR n 
1 231  ASP n 
1 232  PHE n 
1 233  GLY n 
1 234  ASP n 
1 235  LYS n 
1 236  VAL n 
1 237  GLU n 
1 238  ASP n 
1 239  PRO n 
1 240  THR n 
1 241  PHE n 
1 242  LEU n 
1 243  ASN n 
1 244  GLN n 
1 245  LEU n 
1 246  GLN n 
1 247  SER n 
1 248  GLY n 
1 249  VAL n 
1 250  ASN n 
1 251  ARG n 
1 252  TRP n 
1 253  ILE n 
1 254  ARG n 
1 255  GLU n 
1 256  ILE n 
1 257  GLN n 
1 258  LYS n 
1 259  VAL n 
1 260  THR n 
1 261  LYS n 
1 262  LEU n 
1 263  ASP n 
1 264  ARG n 
1 265  ASP n 
1 266  PRO n 
1 267  ALA n 
1 268  SER n 
1 269  GLY n 
1 270  THR n 
1 271  ALA n 
1 272  LEU n 
1 273  GLN n 
1 274  GLU n 
1 275  ILE n 
1 276  SER n 
1 277  PHE n 
1 278  TRP n 
1 279  LEU n 
1 280  ASN n 
1 281  LEU n 
1 282  GLU n 
1 283  ARG n 
1 284  ALA n 
1 285  LEU n 
1 286  TYR n 
1 287  ARG n 
1 288  ILE n 
1 289  GLN n 
1 290  GLU n 
1 291  LYS n 
1 292  ARG n 
1 293  GLU n 
1 294  SER n 
1 295  PRO n 
1 296  GLU n 
1 297  VAL n 
1 298  LEU n 
1 299  LEU n 
1 300  THR n 
1 301  LEU n 
1 302  ASP n 
1 303  ILE n 
1 304  LEU n 
1 305  LYS n 
1 306  HIS n 
1 307  GLY n 
1 308  LYS n 
1 309  ARG n 
1 310  PHE n 
1 311  HIS n 
1 312  ALA n 
1 313  THR n 
1 314  VAL n 
1 315  SER n 
1 316  PHE n 
1 317  ASP n 
1 318  THR n 
1 319  ASP n 
1 320  THR n 
1 321  GLY n 
1 322  LEU n 
1 323  LYS n 
1 324  GLN n 
1 325  ALA n 
1 326  LEU n 
1 327  GLU n 
1 328  THR n 
1 329  VAL n 
1 330  ASN n 
1 331  ASP n 
1 332  TYR n 
1 333  ASN n 
1 334  PRO n 
1 335  LEU n 
1 336  MET n 
1 337  LYS n 
1 338  ASP n 
1 339  PHE n 
1 340  PRO n 
1 341  LEU n 
1 342  ASN n 
1 343  ASP n 
1 344  LEU n 
1 345  LEU n 
1 346  SER n 
1 347  ALA n 
1 348  THR n 
1 349  GLU n 
1 350  LEU n 
1 351  ASP n 
1 352  LYS n 
1 353  ILE n 
1 354  ARG n 
1 355  GLN n 
1 356  ALA n 
1 357  LEU n 
1 358  VAL n 
1 359  ALA n 
1 360  ILE n 
1 361  PHE n 
1 362  THR n 
1 363  HIS n 
1 364  LEU n 
1 365  ARG n 
1 366  LYS n 
1 367  ILE n 
1 368  ARG n 
1 369  ASN n 
1 370  THR n 
1 371  LYS n 
1 372  TYR n 
1 373  PRO n 
1 374  ILE n 
1 375  GLN n 
1 376  ARG n 
1 377  ALA n 
1 378  LEU n 
1 379  ARG n 
1 380  LEU n 
1 381  VAL n 
1 382  GLU n 
1 383  ALA n 
1 384  ILE n 
1 385  SER n 
1 386  ARG n 
1 387  ASP n 
1 388  LEU n 
1 389  SER n 
1 390  SER n 
1 391  GLN n 
1 392  LEU n 
1 393  LEU n 
1 394  LYS n 
1 395  VAL n 
1 396  LEU n 
1 397  GLY n 
1 398  THR n 
1 399  ARG n 
1 400  LYS n 
1 401  LEU n 
1 402  MET n 
1 403  HIS n 
1 404  VAL n 
1 405  ALA n 
1 406  TYR n 
1 407  GLU n 
1 408  GLU n 
1 409  PHE n 
1 410  GLU n 
1 411  LYS n 
1 412  VAL n 
1 413  MET n 
1 414  VAL n 
1 415  ALA n 
1 416  CYS n 
1 417  PHE n 
1 418  GLU n 
1 419  VAL n 
1 420  PHE n 
1 421  GLN n 
1 422  THR n 
1 423  TRP n 
1 424  ASP n 
1 425  ASP n 
1 426  GLU n 
1 427  TYR n 
1 428  GLU n 
1 429  LYS n 
1 430  LEU n 
1 431  GLN n 
1 432  VAL n 
1 433  LEU n 
1 434  LEU n 
1 435  ARG n 
1 436  ASP n 
1 437  ILE n 
1 438  VAL n 
1 439  LYS n 
1 440  ARG n 
1 441  LYS n 
1 442  ARG n 
1 443  GLU n 
1 444  GLU n 
1 445  ASN n 
1 446  LEU n 
1 447  LYS n 
1 448  MET n 
1 449  VAL n 
1 450  TRP n 
1 451  ARG n 
1 452  ILE n 
1 453  ASN n 
1 454  PRO n 
1 455  ALA n 
1 456  HIS n 
1 457  ARG n 
1 458  LYS n 
1 459  LEU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  LEU n 
1 464  ASP n 
1 465  GLN n 
1 466  MET n 
1 467  ARG n 
1 468  LYS n 
1 469  PHE n 
1 470  ARG n 
1 471  ARG n 
1 472  GLN n 
1 473  HIS n 
1 474  GLU n 
1 475  GLN n 
1 476  LEU n 
1 477  ARG n 
1 478  ALA n 
1 479  VAL n 
1 480  ILE n 
1 481  VAL n 
1 482  ARG n 
1 483  VAL n 
1 484  LEU n 
1 485  ARG n 
1 486  PRO n 
1 487  GLN n 
1 488  VAL n 
1 489  THR n 
1 490  ALA n 
1 491  VAL n 
1 492  ALA n 
1 493  GLN n 
1 494  GLN n 
1 495  ASN n 
1 496  GLN n 
1 497  GLY n 
1 498  GLU n 
1 499  VAL n 
1 500  PRO n 
1 501  GLU n 
1 502  PRO n 
1 503  GLN n 
1 504  ASP n 
1 505  MET n 
1 506  LYS n 
1 507  VAL n 
1 508  ALA n 
1 509  GLU n 
1 510  VAL n 
1 511  LEU n 
1 512  PHE n 
1 513  ASP n 
1 514  ALA n 
1 515  ALA n 
1 516  ASP n 
1 517  ALA n 
1 518  ASN n 
1 519  ALA n 
1 520  ILE n 
1 521  GLU n 
1 522  GLU n 
1 523  VAL n 
1 524  ASN n 
1 525  LEU n 
1 526  ALA n 
1 527  TYR n 
1 528  GLU n 
1 529  ASN n 
1 530  VAL n 
1 531  LYS n 
1 532  GLU n 
1 533  VAL n 
1 534  ASP n 
1 535  GLY n 
1 536  LEU n 
1 537  ASP n 
1 538  VAL n 
1 539  SER n 
1 540  LYS n 
1 541  GLU n 
1 542  GLY n 
1 543  THR n 
1 544  GLU n 
1 545  ALA n 
1 546  TRP n 
1 547  GLU n 
1 548  ALA n 
1 549  ALA n 
1 550  MET n 
1 551  LYS n 
1 552  ARG n 
1 553  TYR n 
1 554  ASP n 
1 555  GLU n 
1 556  ARG n 
1 557  ILE n 
1 558  ASP n 
1 559  ARG n 
1 560  VAL n 
1 561  GLU n 
1 562  THR n 
1 563  ARG n 
1 564  ILE n 
1 565  THR n 
1 566  ALA n 
1 567  ARG n 
1 568  LEU n 
1 569  ARG n 
1 570  ASP n 
1 571  GLN n 
1 572  LEU n 
1 573  GLY n 
1 574  THR n 
1 575  ALA n 
1 576  LYS n 
1 577  ASN n 
1 578  ALA n 
1 579  ASN n 
1 580  GLU n 
1 581  MET n 
1 582  PHE n 
1 583  ARG n 
1 584  ILE n 
1 585  PHE n 
1 586  SER n 
1 587  ARG n 
1 588  PHE n 
1 589  ASN n 
1 590  ALA n 
1 591  LEU n 
1 592  PHE n 
1 593  VAL n 
1 594  ARG n 
1 595  PRO n 
1 596  HIS n 
1 597  ILE n 
1 598  ARG n 
1 599  GLY n 
1 600  ALA n 
1 601  ILE n 
1 602  ARG n 
1 603  GLU n 
1 604  TYR n 
1 605  GLN n 
1 606  THR n 
1 607  GLN n 
1 608  LEU n 
1 609  ILE n 
1 610  GLN n 
1 611  ARG n 
1 612  VAL n 
1 613  LYS n 
1 614  ASP n 
1 615  ASP n 
1 616  ILE n 
1 617  GLU n 
1 618  SER n 
1 619  LEU n 
1 620  HIS n 
1 621  ASP n 
1 622  LYS n 
1 623  PHE n 
1 624  LYS n 
1 625  VAL n 
1 626  GLN n 
1 627  TYR n 
1 628  PRO n 
1 629  GLN n 
1 630  SER n 
1 631  GLN n 
1 632  ALA n 
1 633  CYS n 
1 634  LYS n 
1 635  MET n 
1 636  SER n 
1 637  HIS n 
1 638  VAL n 
1 639  ARG n 
1 640  ASP n 
1 641  LEU n 
1 642  PRO n 
1 643  PRO n 
1 644  VAL n 
1 645  SER n 
1 646  GLY n 
1 647  SER n 
1 648  ILE n 
1 649  ILE n 
1 650  TRP n 
1 651  ALA n 
1 652  LYS n 
1 653  GLN n 
1 654  ILE n 
1 655  ASP n 
1 656  ARG n 
1 657  GLN n 
1 658  LEU n 
1 659  THR n 
1 660  ALA n 
1 661  TYR n 
1 662  MET n 
1 663  LYS n 
1 664  ARG n 
1 665  VAL n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LEU n 
1 670  GLY n 
1 671  LYS n 
1 672  GLY n 
1 673  TRP n 
1 674  GLU n 
1 675  ASN n 
1 676  HIS n 
1 677  VAL n 
1 678  GLU n 
1 679  GLY n 
1 680  GLN n 
1 681  LYS n 
1 682  LEU n 
1 683  LYS n 
1 684  GLN n 
1 685  ASP n 
1 686  GLY n 
1 687  ASP n 
1 688  SER n 
1 689  PHE n 
1 690  ARG n 
1 691  MET n 
1 692  LYS n 
1 693  LEU n 
1 694  ASN n 
1 695  THR n 
1 696  GLN n 
1 697  GLU n 
1 698  ILE n 
1 699  PHE n 
1 700  ASP n 
1 701  ASP n 
1 702  TRP n 
1 703  ALA n 
1 704  ARG n 
1 705  LYS n 
1 706  VAL n 
1 707  GLN n 
1 708  GLN n 
1 709  ARG n 
1 710  ASN n 
1 711  LEU n 
1 712  GLY n 
1 713  VAL n 
1 714  SER n 
1 715  GLY n 
1 716  ARG n 
1 717  ILE n 
1 718  PHE n 
1 719  THR n 
1 720  ILE n 
1 721  GLU n 
1 722  SER n 
1 723  THR n 
1 724  ARG n 
1 725  VAL n 
1 726  ARG n 
1 727  GLY n 
1 728  ARG n 
1 729  THR n 
1 730  GLY n 
1 731  ASN n 
1 732  VAL n 
1 733  LEU n 
1 734  LYS n 
1 735  LEU n 
1 736  LYS n 
1 737  VAL n 
1 738  ASN n 
1 739  PHE n 
1 740  LEU n 
1 741  PRO n 
1 742  GLU n 
1 743  ILE n 
1 744  ILE n 
1 745  THR n 
1 746  LEU n 
1 747  SER n 
1 748  LYS n 
1 749  GLU n 
1 750  VAL n 
1 751  ARG n 
1 752  ASN n 
1 753  LEU n 
1 754  LYS n 
1 755  TRP n 
1 756  LEU n 
1 757  GLY n 
1 758  PHE n 
1 759  ARG n 
1 760  VAL n 
1 761  PRO n 
1 762  LEU n 
1 763  ALA n 
1 764  ILE n 
1 765  VAL n 
1 766  ASN n 
1 767  LYS n 
1 768  ALA n 
1 769  HIS n 
1 770  GLN n 
1 771  ALA n 
1 772  ASN n 
1 773  GLN n 
1 774  LEU n 
1 775  TYR n 
1 776  PRO n 
1 777  PHE n 
1 778  ALA n 
1 779  ILE n 
1 780  SER n 
1 781  LEU n 
1 782  ILE n 
1 783  GLU n 
1 784  SER n 
1 785  VAL n 
1 786  ARG n 
1 787  THR n 
1 788  TYR n 
1 789  GLU n 
1 790  ARG n 
1 791  THR n 
1 792  CYS n 
1 793  GLU n 
1 794  LYS n 
1 795  VAL n 
1 796  GLU n 
1 797  GLU n 
1 798  ARG n 
1 799  ASN n 
1 800  THR n 
1 801  ILE n 
1 802  SER n 
1 803  LEU n 
1 804  LEU n 
1 805  VAL n 
1 806  ALA n 
1 807  GLY n 
1 808  LEU n 
1 809  LYS n 
1 810  LYS n 
1 811  GLU n 
1 812  VAL n 
1 813  GLN n 
1 814  ALA n 
1 815  LEU n 
1 816  ILE n 
1 817  ALA n 
1 818  GLU n 
1 819  GLY n 
1 820  ILE n 
1 821  ALA n 
1 822  LEU n 
1 823  VAL n 
1 824  TRP n 
1 825  GLU n 
1 826  SER n 
1 827  TYR n 
1 828  LYS n 
1 829  LEU n 
1 830  ASP n 
1 831  PRO n 
1 832  TYR n 
1 833  VAL n 
1 834  GLN n 
1 835  ARG n 
1 836  LEU n 
1 837  ALA n 
1 838  GLU n 
1 839  THR n 
1 840  VAL n 
1 841  PHE n 
1 842  ASN n 
1 843  PHE n 
1 844  GLN n 
1 845  GLU n 
1 846  LYS n 
1 847  VAL n 
1 848  ASP n 
1 849  ASP n 
1 850  LEU n 
1 851  LEU n 
1 852  ILE n 
1 853  ILE n 
1 854  GLU n 
1 855  GLU n 
1 856  LYS n 
1 857  ILE n 
1 858  ASP n 
1 859  LEU n 
1 860  GLU n 
1 861  VAL n 
1 862  ARG n 
1 863  SER n 
1 864  LEU n 
1 865  GLU n 
1 866  THR n 
1 867  CYS n 
1 868  MET n 
1 869  TYR n 
1 870  ASP n 
1 871  HIS n 
1 872  LYS n 
1 873  THR n 
1 874  PHE n 
1 875  SER n 
1 876  GLU n 
1 877  ILE n 
1 878  LEU n 
1 879  ASN n 
1 880  ARG n 
1 881  VAL n 
1 882  GLN n 
1 883  LYS n 
1 884  ALA n 
1 885  VAL n 
1 886  ASP n 
1 887  ASP n 
1 888  LEU n 
1 889  ASN n 
1 890  LEU n 
1 891  HIS n 
1 892  SER n 
1 893  TYR n 
1 894  SER n 
1 895  ASN n 
1 896  LEU n 
1 897  PRO n 
1 898  ILE n 
1 899  TRP n 
1 900  VAL n 
1 901  ASN n 
1 902  LYS n 
1 903  LEU n 
1 904  ASP n 
1 905  MET n 
1 906  GLU n 
1 907  ILE n 
1 908  GLU n 
1 909  ARG n 
1 910  ILE n 
1 911  LEU n 
1 912  GLY n 
1 913  VAL n 
1 914  ARG n 
1 915  LEU n 
1 916  GLN n 
1 917  ALA n 
1 918  GLY n 
1 919  LEU n 
1 920  ARG n 
1 921  ALA n 
1 922  TRP n 
1 923  THR n 
1 924  GLN n 
1 925  VAL n 
1 926  LEU n 
1 927  LEU n 
1 928  GLY n 
1 929  GLN n 
1 930  ALA n 
1 931  GLU n 
1 932  ASP n 
1 933  LYS n 
1 934  ALA n 
1 935  GLU n 
1 936  VAL n 
1 937  ASP n 
1 938  MET n 
1 939  ASP n 
1 940  THR n 
1 941  ASP n 
1 942  ALA n 
1 943  PRO n 
1 944  GLN n 
1 945  VAL n 
1 946  SER n 
1 947  HIS n 
1 948  LYS n 
1 949  PRO n 
1 950  GLY n 
1 951  GLY n 
1 952  GLU n 
1 953  PRO n 
1 954  LYS n 
1 955  ILE n 
1 956  LYS n 
1 957  ASN n 
1 958  VAL n 
1 959  VAL n 
1 960  HIS n 
1 961  GLU n 
1 962  LEU n 
1 963  ARG n 
1 964  ILE n 
1 965  THR n 
1 966  ASN n 
1 967  GLN n 
1 968  VAL n 
1 969  ILE n 
1 970  TYR n 
1 971  LEU n 
1 972  ASN n 
1 973  PRO n 
1 974  PRO n 
1 975  ILE n 
1 976  GLU n 
1 977  GLU n 
1 978  CYS n 
1 979  ARG n 
1 980  TYR n 
1 981  LYS n 
1 982  LEU n 
1 983  TYR n 
1 984  GLN n 
1 985  GLU n 
1 986  MET n 
1 987  PHE n 
1 988  ALA n 
1 989  TRP n 
1 990  LYS n 
1 991  MET n 
1 992  VAL n 
1 993  VAL n 
1 994  LEU n 
1 995  SER n 
1 996  LEU n 
1 997  PRO n 
1 998  ARG n 
1 999  ILE n 
1 1000 GLN n 
1 1001 SER n 
1 1002 GLN n 
1 1003 ARG n 
1 1004 TYR n 
1 1005 GLN n 
1 1006 VAL n 
1 1007 GLY n 
1 1008 VAL n 
1 1009 HIS n 
1 1010 TYR n 
1 1011 GLU n 
1 1012 LEU n 
1 1013 THR n 
1 1014 GLU n 
1 1015 GLU n 
1 1016 GLU n 
1 1017 LYS n 
1 1018 PHE n 
1 1019 TYR n 
1 1020 ARG n 
1 1021 ASN n 
1 1022 ALA n 
1 1023 LEU n 
1 1024 THR n 
1 1025 ARG n 
1 1026 MET n 
1 1027 PRO n 
1 1028 ASP n 
1 1029 GLY n 
1 1030 PRO n 
1 1031 VAL n 
1 1032 ALA n 
1 1033 LEU n 
1 1034 GLU n 
1 1035 GLU n 
1 1036 SER n 
1 1037 TYR n 
1 1038 SER n 
1 1039 ALA n 
1 1040 VAL n 
1 1041 MET n 
1 1042 GLY n 
1 1043 ILE n 
1 1044 VAL n 
1 1045 SER n 
1 1046 GLU n 
1 1047 VAL n 
1 1048 GLU n 
1 1049 GLN n 
1 1050 TYR n 
1 1051 VAL n 
1 1052 LYS n 
1 1053 VAL n 
1 1054 TRP n 
1 1055 LEU n 
1 1056 GLN n 
1 1057 TYR n 
1 1058 GLN n 
1 1059 CYS n 
1 1060 LEU n 
1 1061 TRP n 
1 1062 ASP n 
1 1063 MET n 
1 1064 GLN n 
1 1065 ALA n 
1 1066 GLU n 
1 1067 ASN n 
1 1068 ILE n 
1 1069 TYR n 
1 1070 ASN n 
1 1071 ARG n 
1 1072 LEU n 
1 1073 GLY n 
1 1074 GLU n 
1 1075 ASP n 
1 1076 LEU n 
1 1077 ASN n 
1 1078 LYS n 
1 1079 TRP n 
1 1080 GLN n 
1 1081 ALA n 
1 1082 LEU n 
1 1083 LEU n 
1 1084 VAL n 
1 1085 GLN n 
1 1086 ILE n 
1 1087 ARG n 
1 1088 LYS n 
1 1089 ALA n 
1 1090 ARG n 
1 1091 GLY n 
1 1092 THR n 
1 1093 PHE n 
1 1094 ASP n 
1 1095 ASN n 
1 1096 ALA n 
1 1097 GLU n 
1 1098 THR n 
1 1099 LYS n 
1 1100 LYS n 
1 1101 GLU n 
1 1102 PHE n 
1 1103 GLY n 
1 1104 PRO n 
1 1105 VAL n 
1 1106 VAL n 
1 1107 ILE n 
1 1108 ASP n 
1 1109 TYR n 
1 1110 GLY n 
1 1111 LYS n 
1 1112 VAL n 
1 1113 GLN n 
1 1114 SER n 
1 1115 LYS n 
1 1116 VAL n 
1 1117 ASN n 
1 1118 LEU n 
1 1119 LYS n 
1 1120 TYR n 
1 1121 ASP n 
1 1122 SER n 
1 1123 TRP n 
1 1124 HIS n 
1 1125 LYS n 
1 1126 GLU n 
1 1127 VAL n 
1 1128 LEU n 
1 1129 SER n 
1 1130 LYS n 
1 1131 PHE n 
1 1132 GLY n 
1 1133 GLN n 
1 1134 MET n 
1 1135 LEU n 
1 1136 GLY n 
1 1137 SER n 
1 1138 ASN n 
1 1139 MET n 
1 1140 THR n 
1 1141 GLU n 
1 1142 PHE n 
1 1143 HIS n 
1 1144 SER n 
1 1145 GLN n 
1 1146 ILE n 
1 1147 SER n 
1 1148 LYS n 
1 1149 SER n 
1 1150 ARG n 
1 1151 GLN n 
1 1152 GLU n 
1 1153 LEU n 
1 1154 GLU n 
1 1155 GLN n 
1 1156 HIS n 
1 1157 SER n 
1 1158 VAL n 
1 1159 ASP n 
1 1160 THR n 
1 1161 ALA n 
1 1162 SER n 
1 1163 THR n 
1 1164 SER n 
1 1165 ASP n 
1 1166 ALA n 
1 1167 VAL n 
1 1168 THR n 
1 1169 PHE n 
1 1170 ILE n 
1 1171 THR n 
1 1172 TYR n 
1 1173 VAL n 
1 1174 GLN n 
1 1175 SER n 
1 1176 LEU n 
1 1177 LYS n 
1 1178 ARG n 
1 1179 LYS n 
1 1180 ILE n 
1 1181 LYS n 
1 1182 GLN n 
1 1183 PHE n 
1 1184 GLU n 
1 1185 LYS n 
1 1186 GLN n 
1 1187 VAL n 
1 1188 GLU n 
1 1189 LEU n 
1 1190 TYR n 
1 1191 ARG n 
1 1192 ASN n 
1 1193 GLY n 
1 1194 GLN n 
1 1195 ARG n 
1 1196 LEU n 
1 1197 LEU n 
1 1198 GLU n 
1 1199 LYS n 
1 1200 GLN n 
1 1201 ARG n 
1 1202 PHE n 
1 1203 GLN n 
1 1204 PHE n 
1 1205 PRO n 
1 1206 PRO n 
1 1207 SER n 
1 1208 TRP n 
1 1209 LEU n 
1 1210 TYR n 
1 1211 ILE n 
1 1212 ASP n 
1 1213 ASN n 
1 1214 ILE n 
1 1215 GLU n 
1 1216 GLY n 
1 1217 GLU n 
1 1218 TRP n 
1 1219 GLY n 
1 1220 ALA n 
1 1221 PHE n 
1 1222 ASN n 
1 1223 ASP n 
1 1224 ILE n 
1 1225 MET n 
1 1226 ARG n 
1 1227 ARG n 
1 1228 LYS n 
1 1229 ASP n 
1 1230 SER n 
1 1231 ALA n 
1 1232 ILE n 
1 1233 GLN n 
1 1234 GLN n 
1 1235 GLN n 
1 1236 VAL n 
1 1237 ALA n 
1 1238 ASN n 
1 1239 LEU n 
1 1240 GLN n 
1 1241 MET n 
1 1242 LYS n 
1 1243 ILE n 
1 1244 VAL n 
1 1245 GLN n 
1 1246 GLU n 
1 1247 ASP n 
1 1248 ARG n 
1 1249 ALA n 
1 1250 VAL n 
1 1251 GLU n 
1 1252 SER n 
1 1253 ARG n 
1 1254 THR n 
1 1255 THR n 
1 1256 ASP n 
1 1257 LEU n 
1 1258 LEU n 
1 1259 THR n 
1 1260 ASP n 
1 1261 TRP n 
1 1262 GLU n 
1 1263 LYS n 
1 1264 THR n 
1 1265 LYS n 
1 1266 PRO n 
1 1267 VAL n 
1 1268 THR n 
1 1269 GLY n 
1 1270 ASN n 
1 1271 LEU n 
1 1272 ARG n 
1 1273 PRO n 
1 1274 GLU n 
1 1275 GLU n 
1 1276 ALA n 
1 1277 LEU n 
1 1278 GLN n 
1 1279 ALA n 
1 1280 LEU n 
1 1281 THR n 
1 1282 ILE n 
1 1283 TYR n 
1 1284 GLU n 
1 1285 GLY n 
1 1286 LYS n 
1 1287 PHE n 
1 1288 GLY n 
1 1289 ARG n 
1 1290 LEU n 
1 1291 LYS n 
1 1292 ASP n 
1 1293 ASP n 
1 1294 ARG n 
1 1295 GLU n 
1 1296 LYS n 
1 1297 CYS n 
1 1298 ALA n 
1 1299 LYS n 
1 1300 ALA n 
1 1301 LYS n 
1 1302 GLU n 
1 1303 ALA n 
1 1304 LEU n 
1 1305 GLU n 
1 1306 LEU n 
1 1307 THR n 
1 1308 ASP n 
1 1309 THR n 
1 1310 GLY n 
1 1311 LEU n 
1 1312 LEU n 
1 1313 SER n 
1 1314 GLY n 
1 1315 SER n 
1 1316 GLU n 
1 1317 GLU n 
1 1318 ARG n 
1 1319 VAL n 
1 1320 GLN n 
1 1321 VAL n 
1 1322 ALA n 
1 1323 LEU n 
1 1324 GLU n 
1 1325 GLU n 
1 1326 LEU n 
1 1327 GLN n 
1 1328 ASP n 
1 1329 LEU n 
1 1330 LYS n 
1 1331 GLY n 
1 1332 VAL n 
1 1333 TRP n 
1 1334 SER n 
1 1335 GLU n 
1 1336 LEU n 
1 1337 SER n 
1 1338 LYS n 
1 1339 VAL n 
1 1340 TRP n 
1 1341 GLU n 
1 1342 GLN n 
1 1343 ILE n 
1 1344 ASP n 
1 1345 GLN n 
1 1346 MET n 
1 1347 LYS n 
1 1348 GLU n 
1 1349 GLN n 
1 1350 PRO n 
1 1351 TRP n 
1 1352 VAL n 
1 1353 SER n 
1 1354 VAL n 
1 1355 GLN n 
1 1356 PRO n 
1 1357 ARG n 
1 1358 LYS n 
1 1359 LEU n 
1 1360 ARG n 
1 1361 GLN n 
1 1362 ASN n 
1 1363 LEU n 
1 1364 ASP n 
1 1365 ALA n 
1 1366 LEU n 
1 1367 LEU n 
1 1368 ASN n 
1 1369 GLN n 
1 1370 LEU n 
1 1371 LYS n 
1 1372 SER n 
1 1373 PHE n 
1 1374 PRO n 
1 1375 ALA n 
1 1376 ARG n 
1 1377 LEU n 
1 1378 ARG n 
1 1379 GLN n 
1 1380 TYR n 
1 1381 ALA n 
1 1382 SER n 
1 1383 TYR n 
1 1384 GLU n 
1 1385 PHE n 
1 1386 VAL n 
1 1387 GLN n 
1 1388 ARG n 
1 1389 LEU n 
1 1390 LEU n 
1 1391 LYS n 
1 1392 GLY n 
1 1393 TYR n 
1 1394 MET n 
1 1395 LYS n 
1 1396 ILE n 
1 1397 ASN n 
1 1398 MET n 
1 1399 LEU n 
1 1400 VAL n 
1 1401 ILE n 
1 1402 GLU n 
1 1403 LEU n 
1 1404 LYS n 
1 1405 SER n 
1 1406 GLU n 
1 1407 ALA n 
1 1408 LEU n 
1 1409 LYS n 
1 1410 ASP n 
1 1411 ARG n 
1 1412 HIS n 
1 1413 TRP n 
1 1414 LYS n 
1 1415 GLN n 
1 1416 LEU n 
1 1417 MET n 
1 1418 LYS n 
1 1419 ARG n 
1 1420 LEU n 
1 1421 HIS n 
1 1422 VAL n 
1 1423 ASN n 
1 1424 TRP n 
1 1425 VAL n 
1 1426 VAL n 
1 1427 SER n 
1 1428 GLU n 
1 1429 LEU n 
1 1430 THR n 
1 1431 LEU n 
1 1432 GLY n 
1 1433 GLN n 
1 1434 ILE n 
1 1435 TRP n 
1 1436 ASP n 
1 1437 VAL n 
1 1438 ASP n 
1 1439 LEU n 
1 1440 GLN n 
1 1441 LYS n 
1 1442 ASN n 
1 1443 GLU n 
1 1444 ALA n 
1 1445 ILE n 
1 1446 VAL n 
1 1447 LYS n 
1 1448 ASP n 
1 1449 VAL n 
1 1450 LEU n 
1 1451 LEU n 
1 1452 VAL n 
1 1453 ALA n 
1 1454 GLN n 
1 1455 GLY n 
1 1456 GLU n 
1 1457 MET n 
1 1458 ALA n 
1 1459 LEU n 
1 1460 GLU n 
1 1461 GLU n 
1 1462 PHE n 
1 1463 LEU n 
1 1464 LYS n 
1 1465 GLN n 
1 1466 ILE n 
1 1467 ARG n 
1 1468 GLU n 
1 1469 VAL n 
1 1470 TRP n 
1 1471 ASN n 
1 1472 THR n 
1 1473 TYR n 
1 1474 GLU n 
1 1475 LEU n 
1 1476 ASP n 
1 1477 LEU n 
1 1478 VAL n 
1 1479 ASN n 
1 1480 TYR n 
1 1481 GLN n 
1 1482 ASN n 
1 1483 LYS n 
1 1484 CYS n 
1 1485 ARG n 
1 1486 LEU n 
1 1487 ILE n 
1 1488 ARG n 
1 1489 GLY n 
1 1490 TRP n 
1 1491 ASP n 
1 1492 ASP n 
1 1493 LEU n 
1 1494 PHE n 
1 1495 ASN n 
1 1496 LYS n 
1 1497 VAL n 
1 1498 LYS n 
1 1499 GLU n 
1 1500 HIS n 
1 1501 ILE n 
1 1502 ASN n 
1 1503 SER n 
1 1504 VAL n 
1 1505 SER n 
1 1506 ALA n 
1 1507 MET n 
1 1508 LYS n 
1 1509 LEU n 
1 1510 SER n 
1 1511 PRO n 
1 1512 TYR n 
1 1513 TYR n 
1 1514 LYS n 
1 1515 VAL n 
1 1516 PHE n 
1 1517 GLU n 
1 1518 GLU n 
1 1519 ASP n 
1 1520 ALA n 
1 1521 LEU n 
1 1522 SER n 
1 1523 TRP n 
1 1524 GLU n 
1 1525 ASP n 
1 1526 LYS n 
1 1527 LEU n 
1 1528 ASN n 
1 1529 ARG n 
1 1530 ILE n 
1 1531 MET n 
1 1532 ALA n 
1 1533 LEU n 
1 1534 PHE n 
1 1535 ASP n 
1 1536 VAL n 
1 1537 TRP n 
1 1538 ILE n 
1 1539 ASP n 
1 1540 VAL n 
1 1541 GLN n 
1 1542 ARG n 
1 1543 ARG n 
1 1544 TRP n 
1 1545 VAL n 
1 1546 TYR n 
1 1547 LEU n 
1 1548 GLU n 
1 1549 GLY n 
1 1550 ILE n 
1 1551 PHE n 
1 1552 THR n 
1 1553 GLY n 
1 1554 SER n 
1 1555 ALA n 
1 1556 ASP n 
1 1557 ILE n 
1 1558 LYS n 
1 1559 HIS n 
1 1560 LEU n 
1 1561 LEU n 
1 1562 PRO n 
1 1563 VAL n 
1 1564 GLU n 
1 1565 THR n 
1 1566 GLN n 
1 1567 ARG n 
1 1568 PHE n 
1 1569 GLN n 
1 1570 SER n 
1 1571 ILE n 
1 1572 SER n 
1 1573 THR n 
1 1574 GLU n 
1 1575 PHE n 
1 1576 LEU n 
1 1577 ALA n 
1 1578 LEU n 
1 1579 MET n 
1 1580 LYS n 
1 1581 LYS n 
1 1582 VAL n 
1 1583 SER n 
1 1584 LYS n 
1 1585 SER n 
1 1586 PRO n 
1 1587 LEU n 
1 1588 VAL n 
1 1589 MET n 
1 1590 ASP n 
1 1591 VAL n 
1 1592 LEU n 
1 1593 ASN n 
1 1594 ILE n 
1 1595 GLN n 
1 1596 GLY n 
1 1597 VAL n 
1 1598 GLN n 
1 1599 ARG n 
1 1600 SER n 
1 1601 LEU n 
1 1602 GLU n 
1 1603 ARG n 
1 1604 LEU n 
1 1605 ALA n 
1 1606 ASP n 
1 1607 LEU n 
1 1608 LEU n 
1 1609 GLY n 
1 1610 LYS n 
1 1611 ILE n 
1 1612 GLN n 
1 1613 LYS n 
1 1614 ALA n 
1 1615 LEU n 
1 1616 GLY n 
1 1617 GLU n 
1 1618 TYR n 
1 1619 LEU n 
1 1620 GLU n 
1 1621 ARG n 
1 1622 GLU n 
1 1623 ARG n 
1 1624 SER n 
1 1625 SER n 
1 1626 PHE n 
1 1627 PRO n 
1 1628 ARG n 
1 1629 PHE n 
1 1630 TYR n 
1 1631 PHE n 
1 1632 VAL n 
1 1633 GLY n 
1 1634 ASP n 
1 1635 GLU n 
1 1636 ASP n 
1 1637 LEU n 
1 1638 LEU n 
1 1639 GLU n 
1 1640 ILE n 
1 1641 ILE n 
1 1642 GLY n 
1 1643 ASN n 
1 1644 SER n 
1 1645 LYS n 
1 1646 ASN n 
1 1647 VAL n 
1 1648 ALA n 
1 1649 LYS n 
1 1650 LEU n 
1 1651 GLN n 
1 1652 LYS n 
1 1653 HIS n 
1 1654 PHE n 
1 1655 LYS n 
1 1656 LYS n 
1 1657 MET n 
1 1658 PHE n 
1 1659 ALA n 
1 1660 GLY n 
1 1661 VAL n 
1 1662 SER n 
1 1663 SER n 
1 1664 ILE n 
1 1665 ILE n 
1 1666 LEU n 
1 1667 ASN n 
1 1668 GLU n 
1 1669 ASP n 
1 1670 ASN n 
1 1671 SER n 
1 1672 VAL n 
1 1673 VAL n 
1 1674 LEU n 
1 1675 GLY n 
1 1676 ILE n 
1 1677 SER n 
1 1678 SER n 
1 1679 ARG n 
1 1680 GLU n 
1 1681 GLY n 
1 1682 GLU n 
1 1683 GLU n 
1 1684 VAL n 
1 1685 MET n 
1 1686 PHE n 
1 1687 LYS n 
1 1688 THR n 
1 1689 PRO n 
1 1690 VAL n 
1 1691 SER n 
1 1692 ILE n 
1 1693 THR n 
1 1694 GLU n 
1 1695 HIS n 
1 1696 PRO n 
1 1697 LYS n 
1 1698 ILE n 
1 1699 ASN n 
1 1700 GLU n 
1 1701 TRP n 
1 1702 LEU n 
1 1703 THR n 
1 1704 LEU n 
1 1705 VAL n 
1 1706 GLU n 
1 1707 LYS n 
1 1708 GLU n 
1 1709 MET n 
1 1710 ARG n 
1 1711 VAL n 
1 1712 THR n 
1 1713 LEU n 
1 1714 ALA n 
1 1715 LYS n 
1 1716 LEU n 
1 1717 LEU n 
1 1718 ALA n 
1 1719 GLU n 
1 1720 SER n 
1 1721 VAL n 
1 1722 THR n 
1 1723 GLU n 
1 1724 VAL n 
1 1725 GLU n 
1 1726 ILE n 
1 1727 PHE n 
1 1728 GLY n 
1 1729 LYS n 
1 1730 ALA n 
1 1731 THR n 
1 1732 SER n 
1 1733 ILE n 
1 1734 ASP n 
1 1735 PRO n 
1 1736 ASN n 
1 1737 THR n 
1 1738 TYR n 
1 1739 ILE n 
1 1740 THR n 
1 1741 TRP n 
1 1742 ILE n 
1 1743 ASP n 
1 1744 LYS n 
1 1745 TYR n 
1 1746 GLN n 
1 1747 ALA n 
1 1748 GLN n 
1 1749 LEU n 
1 1750 VAL n 
1 1751 VAL n 
1 1752 LEU n 
1 1753 SER n 
1 1754 ALA n 
1 1755 GLN n 
1 1756 ILE n 
1 1757 ALA n 
1 1758 TRP n 
1 1759 SER n 
1 1760 GLU n 
1 1761 ASN n 
1 1762 VAL n 
1 1763 GLU n 
1 1764 THR n 
1 1765 ALA n 
1 1766 LEU n 
1 1767 SER n 
1 1768 SER n 
1 1769 MET n 
1 1770 GLY n 
1 1771 GLY n 
1 1772 GLY n 
1 1773 GLY n 
1 1774 ASP n 
1 1775 ALA n 
1 1776 ALA n 
1 1777 PRO n 
1 1778 LEU n 
1 1779 HIS n 
1 1780 SER n 
1 1781 VAL n 
1 1782 LEU n 
1 1783 SER n 
1 1784 ASN n 
1 1785 VAL n 
1 1786 GLU n 
1 1787 VAL n 
1 1788 THR n 
1 1789 LEU n 
1 1790 ASN n 
1 1791 VAL n 
1 1792 LEU n 
1 1793 ALA n 
1 1794 ASP n 
1 1795 SER n 
1 1796 VAL n 
1 1797 LEU n 
1 1798 MET n 
1 1799 GLU n 
1 1800 GLN n 
1 1801 PRO n 
1 1802 PRO n 
1 1803 LEU n 
1 1804 ARG n 
1 1805 ARG n 
1 1806 ARG n 
1 1807 LYS n 
1 1808 LEU n 
1 1809 GLU n 
1 1810 HIS n 
1 1811 LEU n 
1 1812 ILE n 
1 1813 THR n 
1 1814 GLU n 
1 1815 LEU n 
1 1816 VAL n 
1 1817 HIS n 
1 1818 GLN n 
1 1819 ARG n 
1 1820 ASP n 
1 1821 VAL n 
1 1822 THR n 
1 1823 ARG n 
1 1824 SER n 
1 1825 LEU n 
1 1826 ILE n 
1 1827 LYS n 
1 1828 SER n 
1 1829 LYS n 
1 1830 ILE n 
1 1831 ASP n 
1 1832 ASN n 
1 1833 ALA n 
1 1834 LYS n 
1 1835 SER n 
1 1836 PHE n 
1 1837 GLU n 
1 1838 TRP n 
1 1839 LEU n 
1 1840 SER n 
1 1841 GLN n 
1 1842 MET n 
1 1843 ARG n 
1 1844 PHE n 
1 1845 TYR n 
1 1846 PHE n 
1 1847 ASP n 
1 1848 PRO n 
1 1849 LYS n 
1 1850 GLN n 
1 1851 THR n 
1 1852 ASP n 
1 1853 VAL n 
1 1854 LEU n 
1 1855 GLN n 
1 1856 GLN n 
1 1857 LEU n 
1 1858 SER n 
1 1859 ILE n 
1 1860 GLN n 
1 1861 MET n 
1 1862 ALA n 
1 1863 ASN n 
1 1864 ALA n 
1 1865 LYS n 
1 1866 PHE n 
1 1867 ASN n 
1 1868 TYR n 
1 1869 GLY n 
1 1870 PHE n 
1 1871 GLU n 
1 1872 TYR n 
1 1873 LEU n 
1 1874 GLY n 
1 1875 VAL n 
1 1876 GLN n 
1 1877 ASP n 
1 1878 LYS n 
1 1879 LEU n 
1 1880 VAL n 
1 1881 GLN n 
1 1882 THR n 
1 1883 PRO n 
1 1884 LEU n 
1 1885 THR n 
1 1886 ASP n 
1 1887 ARG n 
1 1888 CYS n 
1 1889 TYR n 
1 1890 LEU n 
1 1891 THR n 
1 1892 MET n 
1 1893 THR n 
1 1894 GLN n 
1 1895 ALA n 
1 1896 LEU n 
1 1897 GLU n 
1 1898 ALA n 
1 1899 ARG n 
1 1900 LEU n 
1 1901 GLY n 
1 1902 GLY n 
1 1903 SER n 
1 1904 PRO n 
1 1905 PHE n 
1 1906 GLY n 
1 1907 PRO n 
1 1908 ALA n 
1 1909 GLY n 
1 1910 THR n 
1 1911 GLY n 
1 1912 LYS n 
1 1913 THR n 
1 1914 GLU n 
1 1915 SER n 
1 1916 VAL n 
1 1917 LYS n 
1 1918 ALA n 
1 1919 LEU n 
1 1920 GLY n 
1 1921 HIS n 
1 1922 GLN n 
1 1923 LEU n 
1 1924 GLY n 
1 1925 ARG n 
1 1926 PHE n 
1 1927 VAL n 
1 1928 LEU n 
1 1929 VAL n 
1 1930 PHE n 
1 1931 ASN n 
1 1932 CYS n 
1 1933 ASP n 
1 1934 GLU n 
1 1935 THR n 
1 1936 PHE n 
1 1937 ASP n 
1 1938 PHE n 
1 1939 GLN n 
1 1940 ALA n 
1 1941 MET n 
1 1942 GLY n 
1 1943 ARG n 
1 1944 ILE n 
1 1945 PHE n 
1 1946 VAL n 
1 1947 GLY n 
1 1948 LEU n 
1 1949 CYS n 
1 1950 GLN n 
1 1951 VAL n 
1 1952 GLY n 
1 1953 ALA n 
1 1954 TRP n 
1 1955 GLY n 
1 1956 CYS n 
1 1957 PHE n 
1 1958 ASP n 
1 1959 GLU n 
1 1960 PHE n 
1 1961 ASN n 
1 1962 ARG n 
1 1963 LEU n 
1 1964 GLU n 
1 1965 GLU n 
1 1966 ARG n 
1 1967 MET n 
1 1968 LEU n 
1 1969 SER n 
1 1970 ALA n 
1 1971 VAL n 
1 1972 SER n 
1 1973 GLN n 
1 1974 GLN n 
1 1975 VAL n 
1 1976 GLN n 
1 1977 CYS n 
1 1978 ILE n 
1 1979 GLN n 
1 1980 GLU n 
1 1981 ALA n 
1 1982 LEU n 
1 1983 ARG n 
1 1984 GLU n 
1 1985 HIS n 
1 1986 SER n 
1 1987 ASN n 
1 1988 PRO n 
1 1989 ASN n 
1 1990 TYR n 
1 1991 ASP n 
1 1992 LYS n 
1 1993 THR n 
1 1994 SER n 
1 1995 ALA n 
1 1996 PRO n 
1 1997 ILE n 
1 1998 THR n 
1 1999 CYS n 
1 2000 GLU n 
1 2001 LEU n 
1 2002 LEU n 
1 2003 ASN n 
1 2004 LYS n 
1 2005 GLN n 
1 2006 VAL n 
1 2007 LYS n 
1 2008 VAL n 
1 2009 SER n 
1 2010 PRO n 
1 2011 ASP n 
1 2012 MET n 
1 2013 ALA n 
1 2014 ILE n 
1 2015 PHE n 
1 2016 ILE n 
1 2017 THR n 
1 2018 MET n 
1 2019 ASN n 
1 2020 PRO n 
1 2021 GLY n 
1 2022 TYR n 
1 2023 ALA n 
1 2024 GLY n 
1 2025 ARG n 
1 2026 SER n 
1 2027 ASN n 
1 2028 LEU n 
1 2029 PRO n 
1 2030 ASP n 
1 2031 ASN n 
1 2032 LEU n 
1 2033 LYS n 
1 2034 LYS n 
1 2035 LEU n 
1 2036 PHE n 
1 2037 ARG n 
1 2038 SER n 
1 2039 LEU n 
1 2040 ALA n 
1 2041 MET n 
1 2042 THR n 
1 2043 LYS n 
1 2044 PRO n 
1 2045 ASP n 
1 2046 ARG n 
1 2047 GLN n 
1 2048 LEU n 
1 2049 ILE n 
1 2050 ALA n 
1 2051 GLN n 
1 2052 VAL n 
1 2053 MET n 
1 2054 LEU n 
1 2055 TYR n 
1 2056 SER n 
1 2057 GLN n 
1 2058 GLY n 
1 2059 PHE n 
1 2060 ARG n 
1 2061 THR n 
1 2062 ALA n 
1 2063 GLU n 
1 2064 VAL n 
1 2065 LEU n 
1 2066 ALA n 
1 2067 ASN n 
1 2068 LYS n 
1 2069 ILE n 
1 2070 VAL n 
1 2071 PRO n 
1 2072 PHE n 
1 2073 PHE n 
1 2074 LYS n 
1 2075 LEU n 
1 2076 CYS n 
1 2077 ASP n 
1 2078 GLU n 
1 2079 GLN n 
1 2080 LEU n 
1 2081 SER n 
1 2082 SER n 
1 2083 GLN n 
1 2084 SER n 
1 2085 HIS n 
1 2086 TYR n 
1 2087 ASP n 
1 2088 PHE n 
1 2089 GLY n 
1 2090 LEU n 
1 2091 ARG n 
1 2092 ALA n 
1 2093 LEU n 
1 2094 LYS n 
1 2095 SER n 
1 2096 VAL n 
1 2097 LEU n 
1 2098 VAL n 
1 2099 SER n 
1 2100 ALA n 
1 2101 GLY n 
1 2102 ASN n 
1 2103 VAL n 
1 2104 LYS n 
1 2105 ARG n 
1 2106 GLU n 
1 2107 ARG n 
1 2108 ILE n 
1 2109 GLN n 
1 2110 LYS n 
1 2111 ILE n 
1 2112 LYS n 
1 2113 ARG n 
1 2114 GLU n 
1 2115 LYS n 
1 2116 GLU n 
1 2117 GLU n 
1 2118 ARG n 
1 2119 GLY n 
1 2120 GLU n 
1 2121 ALA n 
1 2122 VAL n 
1 2123 ASP n 
1 2124 GLU n 
1 2125 GLY n 
1 2126 GLU n 
1 2127 ILE n 
1 2128 ALA n 
1 2129 GLU n 
1 2130 ASN n 
1 2131 LEU n 
1 2132 PRO n 
1 2133 GLU n 
1 2134 GLN n 
1 2135 GLU n 
1 2136 ILE n 
1 2137 LEU n 
1 2138 ILE n 
1 2139 GLN n 
1 2140 SER n 
1 2141 VAL n 
1 2142 CYS n 
1 2143 GLU n 
1 2144 THR n 
1 2145 MET n 
1 2146 VAL n 
1 2147 PRO n 
1 2148 LYS n 
1 2149 LEU n 
1 2150 VAL n 
1 2151 ALA n 
1 2152 GLU n 
1 2153 ASP n 
1 2154 ILE n 
1 2155 PRO n 
1 2156 LEU n 
1 2157 LEU n 
1 2158 PHE n 
1 2159 SER n 
1 2160 LEU n 
1 2161 LEU n 
1 2162 SER n 
1 2163 ASP n 
1 2164 VAL n 
1 2165 PHE n 
1 2166 PRO n 
1 2167 GLY n 
1 2168 VAL n 
1 2169 GLN n 
1 2170 TYR n 
1 2171 HIS n 
1 2172 ARG n 
1 2173 GLY n 
1 2174 GLU n 
1 2175 MET n 
1 2176 THR n 
1 2177 ALA n 
1 2178 LEU n 
1 2179 ARG n 
1 2180 GLU n 
1 2181 GLU n 
1 2182 LEU n 
1 2183 LYS n 
1 2184 LYS n 
1 2185 VAL n 
1 2186 CYS n 
1 2187 GLN n 
1 2188 GLU n 
1 2189 MET n 
1 2190 TYR n 
1 2191 LEU n 
1 2192 THR n 
1 2193 TYR n 
1 2194 GLY n 
1 2195 ASP n 
1 2196 GLY n 
1 2197 GLU n 
1 2198 GLU n 
1 2199 VAL n 
1 2200 GLY n 
1 2201 GLY n 
1 2202 MET n 
1 2203 TRP n 
1 2204 VAL n 
1 2205 GLU n 
1 2206 LYS n 
1 2207 VAL n 
1 2208 LEU n 
1 2209 GLN n 
1 2210 LEU n 
1 2211 TYR n 
1 2212 GLN n 
1 2213 ILE n 
1 2214 THR n 
1 2215 GLN n 
1 2216 ILE n 
1 2217 ASN n 
1 2218 HIS n 
1 2219 GLY n 
1 2220 LEU n 
1 2221 MET n 
1 2222 MET n 
1 2223 VAL n 
1 2224 GLY n 
1 2225 PRO n 
1 2226 SER n 
1 2227 GLY n 
1 2228 SER n 
1 2229 GLY n 
1 2230 LYS n 
1 2231 SER n 
1 2232 MET n 
1 2233 ALA n 
1 2234 TRP n 
1 2235 ARG n 
1 2236 VAL n 
1 2237 LEU n 
1 2238 LEU n 
1 2239 LYS n 
1 2240 ALA n 
1 2241 LEU n 
1 2242 GLU n 
1 2243 ARG n 
1 2244 LEU n 
1 2245 GLU n 
1 2246 GLY n 
1 2247 VAL n 
1 2248 GLU n 
1 2249 GLY n 
1 2250 VAL n 
1 2251 ALA n 
1 2252 HIS n 
1 2253 ILE n 
1 2254 ILE n 
1 2255 ASP n 
1 2256 PRO n 
1 2257 LYS n 
1 2258 ALA n 
1 2259 ILE n 
1 2260 SER n 
1 2261 LYS n 
1 2262 ASP n 
1 2263 HIS n 
1 2264 LEU n 
1 2265 TYR n 
1 2266 GLY n 
1 2267 THR n 
1 2268 LEU n 
1 2269 ASP n 
1 2270 PRO n 
1 2271 ASN n 
1 2272 THR n 
1 2273 ARG n 
1 2274 GLU n 
1 2275 TRP n 
1 2276 THR n 
1 2277 ASP n 
1 2278 GLY n 
1 2279 LEU n 
1 2280 PHE n 
1 2281 THR n 
1 2282 HIS n 
1 2283 VAL n 
1 2284 LEU n 
1 2285 ARG n 
1 2286 LYS n 
1 2287 ILE n 
1 2288 ILE n 
1 2289 ASP n 
1 2290 SER n 
1 2291 VAL n 
1 2292 ARG n 
1 2293 GLY n 
1 2294 GLU n 
1 2295 LEU n 
1 2296 GLN n 
1 2297 LYS n 
1 2298 ARG n 
1 2299 GLN n 
1 2300 TRP n 
1 2301 ILE n 
1 2302 VAL n 
1 2303 PHE n 
1 2304 ASP n 
1 2305 GLY n 
1 2306 ASP n 
1 2307 VAL n 
1 2308 ASP n 
1 2309 PRO n 
1 2310 GLU n 
1 2311 TRP n 
1 2312 VAL n 
1 2313 GLU n 
1 2314 ASN n 
1 2315 LEU n 
1 2316 ASN n 
1 2317 SER n 
1 2318 VAL n 
1 2319 LEU n 
1 2320 ASP n 
1 2321 ASP n 
1 2322 ASN n 
1 2323 LYS n 
1 2324 LEU n 
1 2325 LEU n 
1 2326 THR n 
1 2327 LEU n 
1 2328 PRO n 
1 2329 ASN n 
1 2330 GLY n 
1 2331 GLU n 
1 2332 ARG n 
1 2333 LEU n 
1 2334 SER n 
1 2335 LEU n 
1 2336 PRO n 
1 2337 PRO n 
1 2338 ASN n 
1 2339 VAL n 
1 2340 ARG n 
1 2341 ILE n 
1 2342 MET n 
1 2343 PHE n 
1 2344 GLU n 
1 2345 VAL n 
1 2346 GLN n 
1 2347 ASP n 
1 2348 LEU n 
1 2349 LYS n 
1 2350 TYR n 
1 2351 ALA n 
1 2352 THR n 
1 2353 LEU n 
1 2354 ALA n 
1 2355 THR n 
1 2356 VAL n 
1 2357 SER n 
1 2358 ARG n 
1 2359 CYS n 
1 2360 GLY n 
1 2361 MET n 
1 2362 VAL n 
1 2363 TRP n 
1 2364 PHE n 
1 2365 SER n 
1 2366 GLU n 
1 2367 ASP n 
1 2368 VAL n 
1 2369 LEU n 
1 2370 SER n 
1 2371 THR n 
1 2372 ASP n 
1 2373 MET n 
1 2374 ILE n 
1 2375 PHE n 
1 2376 ASN n 
1 2377 ASN n 
1 2378 PHE n 
1 2379 LEU n 
1 2380 ALA n 
1 2381 ARG n 
1 2382 LEU n 
1 2383 ARG n 
1 2384 SER n 
1 2385 ILE n 
1 2386 PRO n 
1 2387 LEU n 
1 2388 ASP n 
1 2389 GLU n 
1 2390 GLY n 
1 2391 GLU n 
1 2392 ASP n 
1 2393 GLU n 
1 2394 ALA n 
1 2395 GLN n 
1 2396 ARG n 
1 2397 ARG n 
1 2398 ARG n 
1 2399 LYS n 
1 2400 GLY n 
1 2401 LYS n 
1 2402 GLU n 
1 2403 ASP n 
1 2404 GLU n 
1 2405 GLY n 
1 2406 GLU n 
1 2407 GLU n 
1 2408 ALA n 
1 2409 ALA n 
1 2410 SER n 
1 2411 PRO n 
1 2412 MET n 
1 2413 LEU n 
1 2414 GLN n 
1 2415 ILE n 
1 2416 GLN n 
1 2417 ARG n 
1 2418 ASP n 
1 2419 ALA n 
1 2420 ALA n 
1 2421 THR n 
1 2422 ILE n 
1 2423 MET n 
1 2424 GLN n 
1 2425 PRO n 
1 2426 TYR n 
1 2427 PHE n 
1 2428 THR n 
1 2429 SER n 
1 2430 ASN n 
1 2431 GLY n 
1 2432 LEU n 
1 2433 VAL n 
1 2434 THR n 
1 2435 LYS n 
1 2436 ALA n 
1 2437 LEU n 
1 2438 GLU n 
1 2439 HIS n 
1 2440 ALA n 
1 2441 PHE n 
1 2442 GLN n 
1 2443 LEU n 
1 2444 GLU n 
1 2445 HIS n 
1 2446 ILE n 
1 2447 MET n 
1 2448 ASP n 
1 2449 LEU n 
1 2450 THR n 
1 2451 ARG n 
1 2452 LEU n 
1 2453 ARG n 
1 2454 CYS n 
1 2455 LEU n 
1 2456 GLY n 
1 2457 SER n 
1 2458 LEU n 
1 2459 PHE n 
1 2460 SER n 
1 2461 MET n 
1 2462 LEU n 
1 2463 HIS n 
1 2464 GLN n 
1 2465 ALA n 
1 2466 CYS n 
1 2467 ARG n 
1 2468 ASN n 
1 2469 VAL n 
1 2470 ALA n 
1 2471 GLN n 
1 2472 TYR n 
1 2473 ASN n 
1 2474 ALA n 
1 2475 ASN n 
1 2476 HIS n 
1 2477 PRO n 
1 2478 ASP n 
1 2479 PHE n 
1 2480 PRO n 
1 2481 MET n 
1 2482 GLN n 
1 2483 ILE n 
1 2484 GLU n 
1 2485 GLN n 
1 2486 LEU n 
1 2487 GLU n 
1 2488 ARG n 
1 2489 TYR n 
1 2490 ILE n 
1 2491 GLN n 
1 2492 ARG n 
1 2493 TYR n 
1 2494 LEU n 
1 2495 VAL n 
1 2496 TYR n 
1 2497 ALA n 
1 2498 ILE n 
1 2499 LEU n 
1 2500 TRP n 
1 2501 SER n 
1 2502 LEU n 
1 2503 SER n 
1 2504 GLY n 
1 2505 ASP n 
1 2506 SER n 
1 2507 ARG n 
1 2508 LEU n 
1 2509 LYS n 
1 2510 MET n 
1 2511 ARG n 
1 2512 ALA n 
1 2513 GLU n 
1 2514 LEU n 
1 2515 GLY n 
1 2516 GLU n 
1 2517 TYR n 
1 2518 ILE n 
1 2519 ARG n 
1 2520 ARG n 
1 2521 ILE n 
1 2522 THR n 
1 2523 THR n 
1 2524 VAL n 
1 2525 PRO n 
1 2526 LEU n 
1 2527 PRO n 
1 2528 THR n 
1 2529 ALA n 
1 2530 PRO n 
1 2531 ASN n 
1 2532 ILE n 
1 2533 PRO n 
1 2534 ILE n 
1 2535 ILE n 
1 2536 ASP n 
1 2537 TYR n 
1 2538 GLU n 
1 2539 VAL n 
1 2540 SER n 
1 2541 ILE n 
1 2542 SER n 
1 2543 GLY n 
1 2544 GLU n 
1 2545 TRP n 
1 2546 SER n 
1 2547 PRO n 
1 2548 TRP n 
1 2549 GLN n 
1 2550 ALA n 
1 2551 LYS n 
1 2552 VAL n 
1 2553 PRO n 
1 2554 GLN n 
1 2555 ILE n 
1 2556 GLU n 
1 2557 VAL n 
1 2558 GLU n 
1 2559 THR n 
1 2560 HIS n 
1 2561 LYS n 
1 2562 VAL n 
1 2563 ALA n 
1 2564 ALA n 
1 2565 PRO n 
1 2566 ASP n 
1 2567 VAL n 
1 2568 VAL n 
1 2569 VAL n 
1 2570 PRO n 
1 2571 THR n 
1 2572 LEU n 
1 2573 ASP n 
1 2574 THR n 
1 2575 VAL n 
1 2576 ARG n 
1 2577 HIS n 
1 2578 GLU n 
1 2579 ALA n 
1 2580 LEU n 
1 2581 LEU n 
1 2582 TYR n 
1 2583 THR n 
1 2584 TRP n 
1 2585 LEU n 
1 2586 ALA n 
1 2587 GLU n 
1 2588 HIS n 
1 2589 LYS n 
1 2590 PRO n 
1 2591 LEU n 
1 2592 VAL n 
1 2593 LEU n 
1 2594 CYS n 
1 2595 GLY n 
1 2596 PRO n 
1 2597 PRO n 
1 2598 GLY n 
1 2599 SER n 
1 2600 GLY n 
1 2601 LYS n 
1 2602 THR n 
1 2603 MET n 
1 2604 THR n 
1 2605 LEU n 
1 2606 PHE n 
1 2607 SER n 
1 2608 ALA n 
1 2609 LEU n 
1 2610 ARG n 
1 2611 ALA n 
1 2612 LEU n 
1 2613 PRO n 
1 2614 ASP n 
1 2615 MET n 
1 2616 GLU n 
1 2617 VAL n 
1 2618 VAL n 
1 2619 GLY n 
1 2620 LEU n 
1 2621 ASN n 
1 2622 PHE n 
1 2623 SER n 
1 2624 SER n 
1 2625 ALA n 
1 2626 THR n 
1 2627 THR n 
1 2628 PRO n 
1 2629 GLU n 
1 2630 LEU n 
1 2631 LEU n 
1 2632 LEU n 
1 2633 LYS n 
1 2634 THR n 
1 2635 PHE n 
1 2636 ASP n 
1 2637 HIS n 
1 2638 TYR n 
1 2639 CYS n 
1 2640 GLU n 
1 2641 TYR n 
1 2642 ARG n 
1 2643 ARG n 
1 2644 THR n 
1 2645 PRO n 
1 2646 ASN n 
1 2647 GLY n 
1 2648 VAL n 
1 2649 VAL n 
1 2650 LEU n 
1 2651 ALA n 
1 2652 PRO n 
1 2653 VAL n 
1 2654 GLN n 
1 2655 LEU n 
1 2656 GLY n 
1 2657 LYS n 
1 2658 TRP n 
1 2659 LEU n 
1 2660 VAL n 
1 2661 LEU n 
1 2662 PHE n 
1 2663 CYS n 
1 2664 ASP n 
1 2665 GLU n 
1 2666 ILE n 
1 2667 ASN n 
1 2668 LEU n 
1 2669 PRO n 
1 2670 ASP n 
1 2671 MET n 
1 2672 ASP n 
1 2673 LYS n 
1 2674 TYR n 
1 2675 GLY n 
1 2676 THR n 
1 2677 GLN n 
1 2678 ARG n 
1 2679 VAL n 
1 2680 ILE n 
1 2681 SER n 
1 2682 PHE n 
1 2683 ILE n 
1 2684 ARG n 
1 2685 GLN n 
1 2686 MET n 
1 2687 VAL n 
1 2688 GLU n 
1 2689 HIS n 
1 2690 GLY n 
1 2691 GLY n 
1 2692 PHE n 
1 2693 TYR n 
1 2694 ARG n 
1 2695 THR n 
1 2696 SER n 
1 2697 ASP n 
1 2698 GLN n 
1 2699 THR n 
1 2700 TRP n 
1 2701 VAL n 
1 2702 LYS n 
1 2703 LEU n 
1 2704 GLU n 
1 2705 ARG n 
1 2706 ILE n 
1 2707 GLN n 
1 2708 PHE n 
1 2709 VAL n 
1 2710 GLY n 
1 2711 ALA n 
1 2712 CYS n 
1 2713 ASN n 
1 2714 PRO n 
1 2715 PRO n 
1 2716 THR n 
1 2717 ASP n 
1 2718 PRO n 
1 2719 GLY n 
1 2720 ARG n 
1 2721 LYS n 
1 2722 PRO n 
1 2723 LEU n 
1 2724 SER n 
1 2725 HIS n 
1 2726 ARG n 
1 2727 PHE n 
1 2728 LEU n 
1 2729 ARG n 
1 2730 HIS n 
1 2731 VAL n 
1 2732 PRO n 
1 2733 VAL n 
1 2734 VAL n 
1 2735 TYR n 
1 2736 VAL n 
1 2737 ASP n 
1 2738 TYR n 
1 2739 PRO n 
1 2740 GLY n 
1 2741 PRO n 
1 2742 ALA n 
1 2743 SER n 
1 2744 LEU n 
1 2745 THR n 
1 2746 GLN n 
1 2747 ILE n 
1 2748 TYR n 
1 2749 GLY n 
1 2750 THR n 
1 2751 PHE n 
1 2752 ASN n 
1 2753 ARG n 
1 2754 ALA n 
1 2755 MET n 
1 2756 LEU n 
1 2757 ARG n 
1 2758 LEU n 
1 2759 ILE n 
1 2760 PRO n 
1 2761 SER n 
1 2762 LEU n 
1 2763 ARG n 
1 2764 THR n 
1 2765 TYR n 
1 2766 ALA n 
1 2767 GLU n 
1 2768 PRO n 
1 2769 LEU n 
1 2770 THR n 
1 2771 ALA n 
1 2772 ALA n 
1 2773 MET n 
1 2774 VAL n 
1 2775 GLU n 
1 2776 PHE n 
1 2777 TYR n 
1 2778 THR n 
1 2779 MET n 
1 2780 SER n 
1 2781 GLN n 
1 2782 GLU n 
1 2783 ARG n 
1 2784 PHE n 
1 2785 THR n 
1 2786 GLN n 
1 2787 ASP n 
1 2788 THR n 
1 2789 GLN n 
1 2790 PRO n 
1 2791 HIS n 
1 2792 TYR n 
1 2793 ILE n 
1 2794 TYR n 
1 2795 SER n 
1 2796 PRO n 
1 2797 ARG n 
1 2798 GLU n 
1 2799 MET n 
1 2800 THR n 
1 2801 ARG n 
1 2802 TRP n 
1 2803 VAL n 
1 2804 ARG n 
1 2805 GLY n 
1 2806 ILE n 
1 2807 PHE n 
1 2808 GLU n 
1 2809 ALA n 
1 2810 LEU n 
1 2811 ARG n 
1 2812 PRO n 
1 2813 LEU n 
1 2814 GLU n 
1 2815 THR n 
1 2816 LEU n 
1 2817 PRO n 
1 2818 VAL n 
1 2819 GLU n 
1 2820 GLY n 
1 2821 LEU n 
1 2822 ILE n 
1 2823 ARG n 
1 2824 ILE n 
1 2825 TRP n 
1 2826 ALA n 
1 2827 HIS n 
1 2828 GLU n 
1 2829 ALA n 
1 2830 LEU n 
1 2831 ARG n 
1 2832 LEU n 
1 2833 PHE n 
1 2834 GLN n 
1 2835 ASP n 
1 2836 ARG n 
1 2837 LEU n 
1 2838 VAL n 
1 2839 GLU n 
1 2840 ASP n 
1 2841 GLU n 
1 2842 GLU n 
1 2843 ARG n 
1 2844 ARG n 
1 2845 TRP n 
1 2846 THR n 
1 2847 ASP n 
1 2848 GLU n 
1 2849 ASN n 
1 2850 ILE n 
1 2851 ASP n 
1 2852 THR n 
1 2853 VAL n 
1 2854 ALA n 
1 2855 LEU n 
1 2856 LYS n 
1 2857 HIS n 
1 2858 PHE n 
1 2859 PRO n 
1 2860 ASN n 
1 2861 ILE n 
1 2862 ASP n 
1 2863 ARG n 
1 2864 GLU n 
1 2865 LYS n 
1 2866 ALA n 
1 2867 MET n 
1 2868 SER n 
1 2869 ARG n 
1 2870 PRO n 
1 2871 ILE n 
1 2872 LEU n 
1 2873 TYR n 
1 2874 SER n 
1 2875 ASN n 
1 2876 TRP n 
1 2877 LEU n 
1 2878 SER n 
1 2879 LYS n 
1 2880 ASP n 
1 2881 TYR n 
1 2882 ILE n 
1 2883 PRO n 
1 2884 VAL n 
1 2885 ASP n 
1 2886 GLN n 
1 2887 GLU n 
1 2888 GLU n 
1 2889 LEU n 
1 2890 ARG n 
1 2891 ASP n 
1 2892 TYR n 
1 2893 VAL n 
1 2894 LYS n 
1 2895 ALA n 
1 2896 ARG n 
1 2897 LEU n 
1 2898 LYS n 
1 2899 VAL n 
1 2900 PHE n 
1 2901 TYR n 
1 2902 GLU n 
1 2903 GLU n 
1 2904 GLU n 
1 2905 LEU n 
1 2906 ASP n 
1 2907 VAL n 
1 2908 PRO n 
1 2909 LEU n 
1 2910 VAL n 
1 2911 LEU n 
1 2912 PHE n 
1 2913 ASN n 
1 2914 GLU n 
1 2915 VAL n 
1 2916 LEU n 
1 2917 ASP n 
1 2918 HIS n 
1 2919 VAL n 
1 2920 LEU n 
1 2921 ARG n 
1 2922 ILE n 
1 2923 ASP n 
1 2924 ARG n 
1 2925 ILE n 
1 2926 PHE n 
1 2927 ARG n 
1 2928 GLN n 
1 2929 PRO n 
1 2930 GLN n 
1 2931 GLY n 
1 2932 HIS n 
1 2933 LEU n 
1 2934 LEU n 
1 2935 LEU n 
1 2936 ILE n 
1 2937 GLY n 
1 2938 VAL n 
1 2939 SER n 
1 2940 GLY n 
1 2941 ALA n 
1 2942 GLY n 
1 2943 LYS n 
1 2944 THR n 
1 2945 THR n 
1 2946 LEU n 
1 2947 SER n 
1 2948 ARG n 
1 2949 PHE n 
1 2950 VAL n 
1 2951 ALA n 
1 2952 TRP n 
1 2953 MET n 
1 2954 ASN n 
1 2955 GLY n 
1 2956 LEU n 
1 2957 SER n 
1 2958 VAL n 
1 2959 TYR n 
1 2960 GLN n 
1 2961 ILE n 
1 2962 LYS n 
1 2963 VAL n 
1 2964 HIS n 
1 2965 ARG n 
1 2966 LYS n 
1 2967 TYR n 
1 2968 THR n 
1 2969 GLY n 
1 2970 GLU n 
1 2971 ASP n 
1 2972 PHE n 
1 2973 ASP n 
1 2974 GLU n 
1 2975 ASP n 
1 2976 LEU n 
1 2977 ARG n 
1 2978 THR n 
1 2979 VAL n 
1 2980 LEU n 
1 2981 ARG n 
1 2982 ARG n 
1 2983 SER n 
1 2984 GLY n 
1 2985 CYS n 
1 2986 LYS n 
1 2987 ASN n 
1 2988 GLU n 
1 2989 LYS n 
1 2990 ILE n 
1 2991 ALA n 
1 2992 PHE n 
1 2993 ILE n 
1 2994 MET n 
1 2995 ASP n 
1 2996 GLU n 
1 2997 SER n 
1 2998 ASN n 
1 2999 VAL n 
1 3000 LEU n 
1 3001 ASP n 
1 3002 SER n 
1 3003 GLY n 
1 3004 PHE n 
1 3005 LEU n 
1 3006 GLU n 
1 3007 ARG n 
1 3008 MET n 
1 3009 ASN n 
1 3010 THR n 
1 3011 LEU n 
1 3012 LEU n 
1 3013 ALA n 
1 3014 ASN n 
1 3015 GLY n 
1 3016 GLU n 
1 3017 VAL n 
1 3018 PRO n 
1 3019 GLY n 
1 3020 LEU n 
1 3021 PHE n 
1 3022 GLU n 
1 3023 GLY n 
1 3024 ASP n 
1 3025 GLU n 
1 3026 TYR n 
1 3027 ALA n 
1 3028 THR n 
1 3029 LEU n 
1 3030 MET n 
1 3031 THR n 
1 3032 GLN n 
1 3033 CYS n 
1 3034 LYS n 
1 3035 GLU n 
1 3036 GLY n 
1 3037 ALA n 
1 3038 GLN n 
1 3039 LYS n 
1 3040 GLU n 
1 3041 GLY n 
1 3042 LEU n 
1 3043 MET n 
1 3044 LEU n 
1 3045 ASP n 
1 3046 SER n 
1 3047 HIS n 
1 3048 GLU n 
1 3049 GLU n 
1 3050 LEU n 
1 3051 TYR n 
1 3052 LYS n 
1 3053 TRP n 
1 3054 PHE n 
1 3055 THR n 
1 3056 SER n 
1 3057 GLN n 
1 3058 VAL n 
1 3059 ILE n 
1 3060 ARG n 
1 3061 ASN n 
1 3062 LEU n 
1 3063 HIS n 
1 3064 VAL n 
1 3065 VAL n 
1 3066 PHE n 
1 3067 THR n 
1 3068 MET n 
1 3069 ASN n 
1 3070 PRO n 
1 3071 SER n 
1 3072 SER n 
1 3073 GLU n 
1 3074 GLY n 
1 3075 LEU n 
1 3076 LYS n 
1 3077 ASP n 
1 3078 ARG n 
1 3079 ALA n 
1 3080 ALA n 
1 3081 THR n 
1 3082 SER n 
1 3083 PRO n 
1 3084 ALA n 
1 3085 LEU n 
1 3086 PHE n 
1 3087 ASN n 
1 3088 ARG n 
1 3089 CYS n 
1 3090 VAL n 
1 3091 LEU n 
1 3092 ASN n 
1 3093 TRP n 
1 3094 PHE n 
1 3095 GLY n 
1 3096 ASP n 
1 3097 TRP n 
1 3098 SER n 
1 3099 THR n 
1 3100 GLU n 
1 3101 ALA n 
1 3102 LEU n 
1 3103 TYR n 
1 3104 GLN n 
1 3105 VAL n 
1 3106 GLY n 
1 3107 LYS n 
1 3108 GLU n 
1 3109 PHE n 
1 3110 THR n 
1 3111 SER n 
1 3112 LYS n 
1 3113 MET n 
1 3114 ASP n 
1 3115 LEU n 
1 3116 GLU n 
1 3117 LYS n 
1 3118 PRO n 
1 3119 ASN n 
1 3120 TYR n 
1 3121 ILE n 
1 3122 VAL n 
1 3123 PRO n 
1 3124 ASP n 
1 3125 TYR n 
1 3126 MET n 
1 3127 PRO n 
1 3128 VAL n 
1 3129 VAL n 
1 3130 TYR n 
1 3131 ASP n 
1 3132 LYS n 
1 3133 LEU n 
1 3134 PRO n 
1 3135 GLN n 
1 3136 PRO n 
1 3137 PRO n 
1 3138 SER n 
1 3139 HIS n 
1 3140 ARG n 
1 3141 GLU n 
1 3142 ALA n 
1 3143 ILE n 
1 3144 VAL n 
1 3145 ASN n 
1 3146 SER n 
1 3147 CYS n 
1 3148 VAL n 
1 3149 PHE n 
1 3150 VAL n 
1 3151 HIS n 
1 3152 GLN n 
1 3153 THR n 
1 3154 LEU n 
1 3155 HIS n 
1 3156 GLN n 
1 3157 ALA n 
1 3158 ASN n 
1 3159 ALA n 
1 3160 ARG n 
1 3161 LEU n 
1 3162 ALA n 
1 3163 LYS n 
1 3164 ARG n 
1 3165 GLY n 
1 3166 GLY n 
1 3167 ARG n 
1 3168 THR n 
1 3169 MET n 
1 3170 ALA n 
1 3171 ILE n 
1 3172 THR n 
1 3173 PRO n 
1 3174 ARG n 
1 3175 HIS n 
1 3176 TYR n 
1 3177 LEU n 
1 3178 ASP n 
1 3179 PHE n 
1 3180 ILE n 
1 3181 ASN n 
1 3182 HIS n 
1 3183 TYR n 
1 3184 ALA n 
1 3185 ASN n 
1 3186 LEU n 
1 3187 PHE n 
1 3188 HIS n 
1 3189 GLU n 
1 3190 LYS n 
1 3191 ARG n 
1 3192 SER n 
1 3193 GLU n 
1 3194 LEU n 
1 3195 GLU n 
1 3196 GLU n 
1 3197 GLN n 
1 3198 GLN n 
1 3199 MET n 
1 3200 HIS n 
1 3201 LEU n 
1 3202 ASN n 
1 3203 VAL n 
1 3204 GLY n 
1 3205 LEU n 
1 3206 ARG n 
1 3207 LYS n 
1 3208 ILE n 
1 3209 LYS n 
1 3210 GLU n 
1 3211 THR n 
1 3212 VAL n 
1 3213 ASP n 
1 3214 GLN n 
1 3215 VAL n 
1 3216 GLU n 
1 3217 GLU n 
1 3218 LEU n 
1 3219 ARG n 
1 3220 ARG n 
1 3221 ASP n 
1 3222 LEU n 
1 3223 ARG n 
1 3224 ILE n 
1 3225 LYS n 
1 3226 SER n 
1 3227 GLN n 
1 3228 GLU n 
1 3229 LEU n 
1 3230 GLU n 
1 3231 VAL n 
1 3232 LYS n 
1 3233 ASN n 
1 3234 ALA n 
1 3235 ALA n 
1 3236 ALA n 
1 3237 ASN n 
1 3238 ASP n 
1 3239 LYS n 
1 3240 LEU n 
1 3241 LYS n 
1 3242 LYS n 
1 3243 MET n 
1 3244 VAL n 
1 3245 LYS n 
1 3246 ASP n 
1 3247 GLN n 
1 3248 GLN n 
1 3249 GLU n 
1 3250 ALA n 
1 3251 GLU n 
1 3252 LYS n 
1 3253 LYS n 
1 3254 LYS n 
1 3255 VAL n 
1 3256 MET n 
1 3257 SER n 
1 3258 GLN n 
1 3259 GLU n 
1 3260 ILE n 
1 3261 GLN n 
1 3262 GLU n 
1 3263 GLN n 
1 3264 LEU n 
1 3265 HIS n 
1 3266 LYS n 
1 3267 GLN n 
1 3268 GLN n 
1 3269 GLU n 
1 3270 VAL n 
1 3271 ILE n 
1 3272 ALA n 
1 3273 ASP n 
1 3274 LYS n 
1 3275 GLN n 
1 3276 MET n 
1 3277 SER n 
1 3278 VAL n 
1 3279 LYS n 
1 3280 GLU n 
1 3281 ASP n 
1 3282 LEU n 
1 3283 ASP n 
1 3284 LYS n 
1 3285 VAL n 
1 3286 GLU n 
1 3287 PRO n 
1 3288 ALA n 
1 3289 VAL n 
1 3290 ILE n 
1 3291 GLU n 
1 3292 ALA n 
1 3293 GLN n 
1 3294 ASN n 
1 3295 ALA n 
1 3296 VAL n 
1 3297 LYS n 
1 3298 SER n 
1 3299 ILE n 
1 3300 LYS n 
1 3301 LYS n 
1 3302 GLN n 
1 3303 HIS n 
1 3304 LEU n 
1 3305 VAL n 
1 3306 GLU n 
1 3307 VAL n 
1 3308 ARG n 
1 3309 SER n 
1 3310 MET n 
1 3311 ALA n 
1 3312 ASN n 
1 3313 PRO n 
1 3314 PRO n 
1 3315 ALA n 
1 3316 ALA n 
1 3317 VAL n 
1 3318 LYS n 
1 3319 LEU n 
1 3320 ALA n 
1 3321 LEU n 
1 3322 GLU n 
1 3323 SER n 
1 3324 ILE n 
1 3325 CYS n 
1 3326 LEU n 
1 3327 LEU n 
1 3328 LEU n 
1 3329 GLY n 
1 3330 GLU n 
1 3331 SER n 
1 3332 THR n 
1 3333 THR n 
1 3334 ASP n 
1 3335 TRP n 
1 3336 LYS n 
1 3337 GLN n 
1 3338 ILE n 
1 3339 ARG n 
1 3340 SER n 
1 3341 ILE n 
1 3342 ILE n 
1 3343 MET n 
1 3344 ARG n 
1 3345 GLU n 
1 3346 ASN n 
1 3347 PHE n 
1 3348 ILE n 
1 3349 PRO n 
1 3350 THR n 
1 3351 ILE n 
1 3352 VAL n 
1 3353 ASN n 
1 3354 PHE n 
1 3355 SER n 
1 3356 ALA n 
1 3357 GLU n 
1 3358 GLU n 
1 3359 ILE n 
1 3360 SER n 
1 3361 ASP n 
1 3362 ALA n 
1 3363 ILE n 
1 3364 ARG n 
1 3365 GLU n 
1 3366 LYS n 
1 3367 MET n 
1 3368 LYS n 
1 3369 LYS n 
1 3370 ASN n 
1 3371 TYR n 
1 3372 MET n 
1 3373 SER n 
1 3374 ASN n 
1 3375 PRO n 
1 3376 SER n 
1 3377 TYR n 
1 3378 ASN n 
1 3379 TYR n 
1 3380 GLU n 
1 3381 ILE n 
1 3382 VAL n 
1 3383 ASN n 
1 3384 ARG n 
1 3385 ALA n 
1 3386 SER n 
1 3387 LEU n 
1 3388 ALA n 
1 3389 CYS n 
1 3390 GLY n 
1 3391 PRO n 
1 3392 MET n 
1 3393 VAL n 
1 3394 LYS n 
1 3395 TRP n 
1 3396 ALA n 
1 3397 ILE n 
1 3398 ALA n 
1 3399 GLN n 
1 3400 LEU n 
1 3401 ASN n 
1 3402 TYR n 
1 3403 ALA n 
1 3404 ASP n 
1 3405 MET n 
1 3406 LEU n 
1 3407 LYS n 
1 3408 ARG n 
1 3409 VAL n 
1 3410 GLU n 
1 3411 PRO n 
1 3412 LEU n 
1 3413 ARG n 
1 3414 ASN n 
1 3415 GLU n 
1 3416 LEU n 
1 3417 GLN n 
1 3418 LYS n 
1 3419 LEU n 
1 3420 GLU n 
1 3421 ASP n 
1 3422 ASP n 
1 3423 ALA n 
1 3424 LYS n 
1 3425 ASP n 
1 3426 ASN n 
1 3427 GLN n 
1 3428 GLN n 
1 3429 LYS n 
1 3430 ALA n 
1 3431 ASN n 
1 3432 GLU n 
1 3433 VAL n 
1 3434 GLU n 
1 3435 GLN n 
1 3436 MET n 
1 3437 ILE n 
1 3438 ARG n 
1 3439 ASP n 
1 3440 LEU n 
1 3441 GLU n 
1 3442 ALA n 
1 3443 SER n 
1 3444 ILE n 
1 3445 ALA n 
1 3446 ARG n 
1 3447 TYR n 
1 3448 LYS n 
1 3449 GLU n 
1 3450 GLU n 
1 3451 TYR n 
1 3452 ALA n 
1 3453 VAL n 
1 3454 LEU n 
1 3455 ILE n 
1 3456 SER n 
1 3457 GLU n 
1 3458 ALA n 
1 3459 GLN n 
1 3460 ALA n 
1 3461 ILE n 
1 3462 LYS n 
1 3463 ALA n 
1 3464 ASP n 
1 3465 LEU n 
1 3466 ALA n 
1 3467 ALA n 
1 3468 VAL n 
1 3469 GLU n 
1 3470 ALA n 
1 3471 LYS n 
1 3472 VAL n 
1 3473 ASN n 
1 3474 ARG n 
1 3475 SER n 
1 3476 THR n 
1 3477 ALA n 
1 3478 LEU n 
1 3479 LEU n 
1 3480 LYS n 
1 3481 SER n 
1 3482 LEU n 
1 3483 SER n 
1 3484 ALA n 
1 3485 GLU n 
1 3486 ARG n 
1 3487 GLU n 
1 3488 ARG n 
1 3489 TRP n 
1 3490 GLU n 
1 3491 LYS n 
1 3492 THR n 
1 3493 SER n 
1 3494 GLU n 
1 3495 THR n 
1 3496 PHE n 
1 3497 LYS n 
1 3498 ASN n 
1 3499 GLN n 
1 3500 MET n 
1 3501 SER n 
1 3502 THR n 
1 3503 ILE n 
1 3504 ALA n 
1 3505 GLY n 
1 3506 ASP n 
1 3507 CYS n 
1 3508 LEU n 
1 3509 LEU n 
1 3510 SER n 
1 3511 ALA n 
1 3512 ALA n 
1 3513 PHE n 
1 3514 ILE n 
1 3515 ALA n 
1 3516 TYR n 
1 3517 ALA n 
1 3518 GLY n 
1 3519 TYR n 
1 3520 PHE n 
1 3521 ASP n 
1 3522 GLN n 
1 3523 GLN n 
1 3524 MET n 
1 3525 ARG n 
1 3526 GLN n 
1 3527 ASN n 
1 3528 LEU n 
1 3529 PHE n 
1 3530 THR n 
1 3531 THR n 
1 3532 TRP n 
1 3533 SER n 
1 3534 HIS n 
1 3535 HIS n 
1 3536 LEU n 
1 3537 GLN n 
1 3538 GLN n 
1 3539 ALA n 
1 3540 ASN n 
1 3541 ILE n 
1 3542 GLN n 
1 3543 PHE n 
1 3544 ARG n 
1 3545 THR n 
1 3546 ASP n 
1 3547 ILE n 
1 3548 ALA n 
1 3549 ARG n 
1 3550 THR n 
1 3551 GLU n 
1 3552 TYR n 
1 3553 LEU n 
1 3554 SER n 
1 3555 ASN n 
1 3556 ALA n 
1 3557 ASP n 
1 3558 GLU n 
1 3559 ARG n 
1 3560 LEU n 
1 3561 ARG n 
1 3562 TRP n 
1 3563 GLN n 
1 3564 ALA n 
1 3565 SER n 
1 3566 SER n 
1 3567 LEU n 
1 3568 PRO n 
1 3569 ALA n 
1 3570 ASP n 
1 3571 ASP n 
1 3572 LEU n 
1 3573 CYS n 
1 3574 THR n 
1 3575 GLU n 
1 3576 ASN n 
1 3577 ALA n 
1 3578 ILE n 
1 3579 MET n 
1 3580 LEU n 
1 3581 LYS n 
1 3582 ARG n 
1 3583 PHE n 
1 3584 ASN n 
1 3585 ARG n 
1 3586 TYR n 
1 3587 PRO n 
1 3588 LEU n 
1 3589 ILE n 
1 3590 ILE n 
1 3591 ASP n 
1 3592 PRO n 
1 3593 SER n 
1 3594 GLY n 
1 3595 GLN n 
1 3596 ALA n 
1 3597 THR n 
1 3598 GLU n 
1 3599 PHE n 
1 3600 ILE n 
1 3601 MET n 
1 3602 ASN n 
1 3603 GLU n 
1 3604 TYR n 
1 3605 LYS n 
1 3606 ASP n 
1 3607 ARG n 
1 3608 LYS n 
1 3609 ILE n 
1 3610 THR n 
1 3611 ARG n 
1 3612 THR n 
1 3613 SER n 
1 3614 PHE n 
1 3615 LEU n 
1 3616 ASP n 
1 3617 ASP n 
1 3618 ALA n 
1 3619 PHE n 
1 3620 ARG n 
1 3621 LYS n 
1 3622 ASN n 
1 3623 LEU n 
1 3624 GLU n 
1 3625 SER n 
1 3626 ALA n 
1 3627 LEU n 
1 3628 ARG n 
1 3629 PHE n 
1 3630 GLY n 
1 3631 ASN n 
1 3632 PRO n 
1 3633 LEU n 
1 3634 LEU n 
1 3635 VAL n 
1 3636 GLN n 
1 3637 ASP n 
1 3638 VAL n 
1 3639 GLU n 
1 3640 SER n 
1 3641 TYR n 
1 3642 ASP n 
1 3643 PRO n 
1 3644 VAL n 
1 3645 LEU n 
1 3646 ASN n 
1 3647 PRO n 
1 3648 VAL n 
1 3649 LEU n 
1 3650 ASN n 
1 3651 ARG n 
1 3652 GLU n 
1 3653 VAL n 
1 3654 ARG n 
1 3655 ARG n 
1 3656 THR n 
1 3657 GLY n 
1 3658 GLY n 
1 3659 ARG n 
1 3660 VAL n 
1 3661 LEU n 
1 3662 ILE n 
1 3663 THR n 
1 3664 LEU n 
1 3665 GLY n 
1 3666 ASP n 
1 3667 GLN n 
1 3668 ASP n 
1 3669 ILE n 
1 3670 ASP n 
1 3671 LEU n 
1 3672 SER n 
1 3673 PRO n 
1 3674 SER n 
1 3675 PHE n 
1 3676 VAL n 
1 3677 ILE n 
1 3678 PHE n 
1 3679 LEU n 
1 3680 SER n 
1 3681 THR n 
1 3682 ARG n 
1 3683 ASP n 
1 3684 PRO n 
1 3685 THR n 
1 3686 VAL n 
1 3687 GLU n 
1 3688 PHE n 
1 3689 PRO n 
1 3690 PRO n 
1 3691 ASP n 
1 3692 LEU n 
1 3693 CYS n 
1 3694 SER n 
1 3695 ARG n 
1 3696 VAL n 
1 3697 THR n 
1 3698 PHE n 
1 3699 VAL n 
1 3700 ASN n 
1 3701 PHE n 
1 3702 THR n 
1 3703 VAL n 
1 3704 THR n 
1 3705 ARG n 
1 3706 SER n 
1 3707 SER n 
1 3708 LEU n 
1 3709 GLN n 
1 3710 SER n 
1 3711 GLN n 
1 3712 CYS n 
1 3713 LEU n 
1 3714 ASN n 
1 3715 GLU n 
1 3716 VAL n 
1 3717 LEU n 
1 3718 LYS n 
1 3719 ALA n 
1 3720 GLU n 
1 3721 ARG n 
1 3722 PRO n 
1 3723 ASP n 
1 3724 VAL n 
1 3725 ASP n 
1 3726 GLU n 
1 3727 LYS n 
1 3728 ARG n 
1 3729 SER n 
1 3730 ASP n 
1 3731 LEU n 
1 3732 LEU n 
1 3733 LYS n 
1 3734 LEU n 
1 3735 GLN n 
1 3736 GLY n 
1 3737 GLU n 
1 3738 PHE n 
1 3739 GLN n 
1 3740 LEU n 
1 3741 ARG n 
1 3742 LEU n 
1 3743 ARG n 
1 3744 GLN n 
1 3745 LEU n 
1 3746 GLU n 
1 3747 LYS n 
1 3748 SER n 
1 3749 LEU n 
1 3750 LEU n 
1 3751 GLN n 
1 3752 ALA n 
1 3753 LEU n 
1 3754 ASN n 
1 3755 GLU n 
1 3756 VAL n 
1 3757 LYS n 
1 3758 GLY n 
1 3759 ARG n 
1 3760 ILE n 
1 3761 LEU n 
1 3762 ASP n 
1 3763 ASP n 
1 3764 ASP n 
1 3765 THR n 
1 3766 ILE n 
1 3767 ILE n 
1 3768 THR n 
1 3769 THR n 
1 3770 LEU n 
1 3771 GLU n 
1 3772 ASN n 
1 3773 LEU n 
1 3774 LYS n 
1 3775 ARG n 
1 3776 GLU n 
1 3777 ALA n 
1 3778 ALA n 
1 3779 GLU n 
1 3780 VAL n 
1 3781 THR n 
1 3782 ARG n 
1 3783 LYS n 
1 3784 VAL n 
1 3785 GLU n 
1 3786 GLU n 
1 3787 THR n 
1 3788 ASP n 
1 3789 ILE n 
1 3790 VAL n 
1 3791 MET n 
1 3792 GLN n 
1 3793 GLU n 
1 3794 VAL n 
1 3795 GLU n 
1 3796 THR n 
1 3797 VAL n 
1 3798 SER n 
1 3799 GLN n 
1 3800 GLN n 
1 3801 TYR n 
1 3802 LEU n 
1 3803 PRO n 
1 3804 LEU n 
1 3805 SER n 
1 3806 THR n 
1 3807 ALA n 
1 3808 CYS n 
1 3809 SER n 
1 3810 SER n 
1 3811 ILE n 
1 3812 TYR n 
1 3813 PHE n 
1 3814 THR n 
1 3815 MET n 
1 3816 GLU n 
1 3817 SER n 
1 3818 LEU n 
1 3819 LYS n 
1 3820 GLN n 
1 3821 ILE n 
1 3822 HIS n 
1 3823 PHE n 
1 3824 LEU n 
1 3825 TYR n 
1 3826 GLN n 
1 3827 TYR n 
1 3828 SER n 
1 3829 LEU n 
1 3830 GLN n 
1 3831 PHE n 
1 3832 PHE n 
1 3833 LEU n 
1 3834 ASP n 
1 3835 ILE n 
1 3836 TYR n 
1 3837 HIS n 
1 3838 ASN n 
1 3839 VAL n 
1 3840 LEU n 
1 3841 TYR n 
1 3842 GLU n 
1 3843 ASN n 
1 3844 PRO n 
1 3845 ASN n 
1 3846 LEU n 
1 3847 LYS n 
1 3848 GLY n 
1 3849 VAL n 
1 3850 THR n 
1 3851 ASP n 
1 3852 HIS n 
1 3853 THR n 
1 3854 GLN n 
1 3855 ARG n 
1 3856 LEU n 
1 3857 SER n 
1 3858 ILE n 
1 3859 ILE n 
1 3860 THR n 
1 3861 LYS n 
1 3862 ASP n 
1 3863 LEU n 
1 3864 PHE n 
1 3865 GLN n 
1 3866 VAL n 
1 3867 ALA n 
1 3868 PHE n 
1 3869 ASN n 
1 3870 ARG n 
1 3871 VAL n 
1 3872 ALA n 
1 3873 ARG n 
1 3874 GLY n 
1 3875 MET n 
1 3876 LEU n 
1 3877 HIS n 
1 3878 GLN n 
1 3879 ASP n 
1 3880 HIS n 
1 3881 ILE n 
1 3882 THR n 
1 3883 PHE n 
1 3884 ALA n 
1 3885 MET n 
1 3886 LEU n 
1 3887 LEU n 
1 3888 ALA n 
1 3889 ARG n 
1 3890 ILE n 
1 3891 LYS n 
1 3892 LEU n 
1 3893 LYS n 
1 3894 GLY n 
1 3895 THR n 
1 3896 VAL n 
1 3897 GLY n 
1 3898 GLU n 
1 3899 PRO n 
1 3900 THR n 
1 3901 TYR n 
1 3902 ASP n 
1 3903 ALA n 
1 3904 GLU n 
1 3905 PHE n 
1 3906 GLN n 
1 3907 HIS n 
1 3908 PHE n 
1 3909 LEU n 
1 3910 ARG n 
1 3911 GLY n 
1 3912 ASN n 
1 3913 GLU n 
1 3914 ILE n 
1 3915 VAL n 
1 3916 LEU n 
1 3917 SER n 
1 3918 ALA n 
1 3919 GLY n 
1 3920 SER n 
1 3921 THR n 
1 3922 PRO n 
1 3923 ARG n 
1 3924 ILE n 
1 3925 GLN n 
1 3926 GLY n 
1 3927 LEU n 
1 3928 THR n 
1 3929 VAL n 
1 3930 GLU n 
1 3931 GLN n 
1 3932 ALA n 
1 3933 GLU n 
1 3934 ALA n 
1 3935 VAL n 
1 3936 VAL n 
1 3937 ARG n 
1 3938 LEU n 
1 3939 SER n 
1 3940 CYS n 
1 3941 LEU n 
1 3942 PRO n 
1 3943 ALA n 
1 3944 PHE n 
1 3945 LYS n 
1 3946 ASP n 
1 3947 LEU n 
1 3948 ILE n 
1 3949 ALA n 
1 3950 LYS n 
1 3951 VAL n 
1 3952 GLN n 
1 3953 ALA n 
1 3954 ASP n 
1 3955 GLU n 
1 3956 GLN n 
1 3957 PHE n 
1 3958 GLY n 
1 3959 ILE n 
1 3960 TRP n 
1 3961 LEU n 
1 3962 ASP n 
1 3963 SER n 
1 3964 SER n 
1 3965 SER n 
1 3966 PRO n 
1 3967 GLU n 
1 3968 GLN n 
1 3969 THR n 
1 3970 VAL n 
1 3971 PRO n 
1 3972 TYR n 
1 3973 LEU n 
1 3974 TRP n 
1 3975 SER n 
1 3976 GLU n 
1 3977 GLU n 
1 3978 THR n 
1 3979 PRO n 
1 3980 ALA n 
1 3981 THR n 
1 3982 PRO n 
1 3983 ILE n 
1 3984 GLY n 
1 3985 GLN n 
1 3986 ALA n 
1 3987 ILE n 
1 3988 HIS n 
1 3989 ARG n 
1 3990 LEU n 
1 3991 LEU n 
1 3992 LEU n 
1 3993 ILE n 
1 3994 GLN n 
1 3995 ALA n 
1 3996 PHE n 
1 3997 ARG n 
1 3998 PRO n 
1 3999 ASP n 
1 4000 ARG n 
1 4001 LEU n 
1 4002 LEU n 
1 4003 ALA n 
1 4004 MET n 
1 4005 ALA n 
1 4006 HIS n 
1 4007 MET n 
1 4008 PHE n 
1 4009 VAL n 
1 4010 SER n 
1 4011 THR n 
1 4012 ASN n 
1 4013 LEU n 
1 4014 GLY n 
1 4015 GLU n 
1 4016 SER n 
1 4017 PHE n 
1 4018 MET n 
1 4019 SER n 
1 4020 ILE n 
1 4021 MET n 
1 4022 GLU n 
1 4023 GLN n 
1 4024 PRO n 
1 4025 LEU n 
1 4026 ASP n 
1 4027 LEU n 
1 4028 THR n 
1 4029 HIS n 
1 4030 ILE n 
1 4031 VAL n 
1 4032 GLY n 
1 4033 THR n 
1 4034 GLU n 
1 4035 VAL n 
1 4036 LYS n 
1 4037 PRO n 
1 4038 ASN n 
1 4039 THR n 
1 4040 PRO n 
1 4041 VAL n 
1 4042 LEU n 
1 4043 MET n 
1 4044 CYS n 
1 4045 SER n 
1 4046 VAL n 
1 4047 PRO n 
1 4048 GLY n 
1 4049 TYR n 
1 4050 ASP n 
1 4051 ALA n 
1 4052 SER n 
1 4053 GLY n 
1 4054 HIS n 
1 4055 VAL n 
1 4056 GLU n 
1 4057 ASP n 
1 4058 LEU n 
1 4059 ALA n 
1 4060 ALA n 
1 4061 GLU n 
1 4062 GLN n 
1 4063 ASN n 
1 4064 THR n 
1 4065 GLN n 
1 4066 ILE n 
1 4067 THR n 
1 4068 SER n 
1 4069 ILE n 
1 4070 ALA n 
1 4071 ILE n 
1 4072 GLY n 
1 4073 SER n 
1 4074 ALA n 
1 4075 GLU n 
1 4076 GLY n 
1 4077 PHE n 
1 4078 ASN n 
1 4079 GLN n 
1 4080 ALA n 
1 4081 ASP n 
1 4082 LYS n 
1 4083 ALA n 
1 4084 ILE n 
1 4085 ASN n 
1 4086 THR n 
1 4087 ALA n 
1 4088 VAL n 
1 4089 LYS n 
1 4090 SER n 
1 4091 GLY n 
1 4092 ARG n 
1 4093 TRP n 
1 4094 VAL n 
1 4095 MET n 
1 4096 LEU n 
1 4097 LYS n 
1 4098 ASN n 
1 4099 VAL n 
1 4100 HIS n 
1 4101 LEU n 
1 4102 ALA n 
1 4103 PRO n 
1 4104 GLY n 
1 4105 TRP n 
1 4106 LEU n 
1 4107 MET n 
1 4108 GLN n 
1 4109 LEU n 
1 4110 GLU n 
1 4111 LYS n 
1 4112 LYS n 
1 4113 LEU n 
1 4114 HIS n 
1 4115 SER n 
1 4116 LEU n 
1 4117 GLN n 
1 4118 PRO n 
1 4119 HIS n 
1 4120 ALA n 
1 4121 CYS n 
1 4122 PHE n 
1 4123 ARG n 
1 4124 LEU n 
1 4125 PHE n 
1 4126 LEU n 
1 4127 THR n 
1 4128 MET n 
1 4129 GLU n 
1 4130 ILE n 
1 4131 ASN n 
1 4132 PRO n 
1 4133 LYS n 
1 4134 VAL n 
1 4135 PRO n 
1 4136 VAL n 
1 4137 ASN n 
1 4138 LEU n 
1 4139 LEU n 
1 4140 ARG n 
1 4141 ALA n 
1 4142 GLY n 
1 4143 ARG n 
1 4144 ILE n 
1 4145 PHE n 
1 4146 VAL n 
1 4147 PHE n 
1 4148 GLU n 
1 4149 PRO n 
1 4150 PRO n 
1 4151 PRO n 
1 4152 GLY n 
1 4153 VAL n 
1 4154 LYS n 
1 4155 ALA n 
1 4156 ASN n 
1 4157 MET n 
1 4158 LEU n 
1 4159 ARG n 
1 4160 THR n 
1 4161 PHE n 
1 4162 SER n 
1 4163 SER n 
1 4164 ILE n 
1 4165 PRO n 
1 4166 VAL n 
1 4167 SER n 
1 4168 ARG n 
1 4169 ILE n 
1 4170 CYS n 
1 4171 LYS n 
1 4172 SER n 
1 4173 PRO n 
1 4174 ASN n 
1 4175 GLU n 
1 4176 ARG n 
1 4177 ALA n 
1 4178 ARG n 
1 4179 LEU n 
1 4180 TYR n 
1 4181 PHE n 
1 4182 LEU n 
1 4183 LEU n 
1 4184 ALA n 
1 4185 TRP n 
1 4186 PHE n 
1 4187 HIS n 
1 4188 ALA n 
1 4189 ILE n 
1 4190 ILE n 
1 4191 GLN n 
1 4192 GLU n 
1 4193 ARG n 
1 4194 LEU n 
1 4195 ARG n 
1 4196 TYR n 
1 4197 ALA n 
1 4198 PRO n 
1 4199 LEU n 
1 4200 GLY n 
1 4201 TRP n 
1 4202 SER n 
1 4203 LYS n 
1 4204 LYS n 
1 4205 TYR n 
1 4206 GLU n 
1 4207 PHE n 
1 4208 GLY n 
1 4209 GLU n 
1 4210 SER n 
1 4211 ASP n 
1 4212 LEU n 
1 4213 ARG n 
1 4214 SER n 
1 4215 ALA n 
1 4216 CYS n 
1 4217 ASP n 
1 4218 THR n 
1 4219 VAL n 
1 4220 ASP n 
1 4221 THR n 
1 4222 TRP n 
1 4223 LEU n 
1 4224 ASP n 
1 4225 ASP n 
1 4226 THR n 
1 4227 ALA n 
1 4228 LYS n 
1 4229 GLY n 
1 4230 ARG n 
1 4231 GLN n 
1 4232 ASN n 
1 4233 ILE n 
1 4234 SER n 
1 4235 PRO n 
1 4236 ASP n 
1 4237 LYS n 
1 4238 ILE n 
1 4239 PRO n 
1 4240 TRP n 
1 4241 SER n 
1 4242 ALA n 
1 4243 LEU n 
1 4244 LYS n 
1 4245 THR n 
1 4246 LEU n 
1 4247 MET n 
1 4248 ALA n 
1 4249 GLN n 
1 4250 SER n 
1 4251 ILE n 
1 4252 TYR n 
1 4253 GLY n 
1 4254 GLY n 
1 4255 ARG n 
1 4256 VAL n 
1 4257 ASP n 
1 4258 ASN n 
1 4259 GLU n 
1 4260 PHE n 
1 4261 ASP n 
1 4262 GLN n 
1 4263 ARG n 
1 4264 LEU n 
1 4265 LEU n 
1 4266 ASN n 
1 4267 THR n 
1 4268 PHE n 
1 4269 LEU n 
1 4270 GLU n 
1 4271 ARG n 
1 4272 LEU n 
1 4273 PHE n 
1 4274 THR n 
1 4275 THR n 
1 4276 ARG n 
1 4277 SER n 
1 4278 PHE n 
1 4279 ASP n 
1 4280 SER n 
1 4281 GLU n 
1 4282 PHE n 
1 4283 LYS n 
1 4284 LEU n 
1 4285 ALA n 
1 4286 CYS n 
1 4287 LYS n 
1 4288 VAL n 
1 4289 ASP n 
1 4290 GLY n 
1 4291 HIS n 
1 4292 LYS n 
1 4293 ASP n 
1 4294 ILE n 
1 4295 GLN n 
1 4296 MET n 
1 4297 PRO n 
1 4298 ASP n 
1 4299 GLY n 
1 4300 ILE n 
1 4301 ARG n 
1 4302 ARG n 
1 4303 GLU n 
1 4304 GLU n 
1 4305 PHE n 
1 4306 VAL n 
1 4307 GLN n 
1 4308 TRP n 
1 4309 VAL n 
1 4310 GLU n 
1 4311 LEU n 
1 4312 LEU n 
1 4313 PRO n 
1 4314 ASP n 
1 4315 THR n 
1 4316 GLN n 
1 4317 THR n 
1 4318 PRO n 
1 4319 SER n 
1 4320 TRP n 
1 4321 LEU n 
1 4322 GLY n 
1 4323 LEU n 
1 4324 PRO n 
1 4325 ASN n 
1 4326 ASN n 
1 4327 ALA n 
1 4328 GLU n 
1 4329 ARG n 
1 4330 VAL n 
1 4331 LEU n 
1 4332 LEU n 
1 4333 THR n 
1 4334 THR n 
1 4335 GLN n 
1 4336 GLY n 
1 4337 VAL n 
1 4338 ASP n 
1 4339 MET n 
1 4340 ILE n 
1 4341 SER n 
1 4342 LYS n 
1 4343 MET n 
1 4344 LEU n 
1 4345 LYS n 
1 4346 MET n 
1 4347 GLN n 
1 4348 MET n 
1 4349 LEU n 
1 4350 GLU n 
1 4351 ASP n 
1 4352 GLU n 
1 4353 ASP n 
1 4354 ASP n 
1 4355 LEU n 
1 4356 ALA n 
1 4357 TYR n 
1 4358 ALA n 
1 4359 GLU n 
1 4360 THR n 
1 4361 GLU n 
1 4362 LYS n 
1 4363 LYS n 
1 4364 THR n 
1 4365 ARG n 
1 4366 THR n 
1 4367 ASP n 
1 4368 SER n 
1 4369 THR n 
1 4370 SER n 
1 4371 ASP n 
1 4372 GLY n 
1 4373 ARG n 
1 4374 PRO n 
1 4375 ALA n 
1 4376 TRP n 
1 4377 MET n 
1 4378 ARG n 
1 4379 THR n 
1 4380 LEU n 
1 4381 HIS n 
1 4382 THR n 
1 4383 THR n 
1 4384 ALA n 
1 4385 SER n 
1 4386 ASN n 
1 4387 TRP n 
1 4388 LEU n 
1 4389 HIS n 
1 4390 LEU n 
1 4391 ILE n 
1 4392 PRO n 
1 4393 GLN n 
1 4394 THR n 
1 4395 LEU n 
1 4396 SER n 
1 4397 HIS n 
1 4398 LEU n 
1 4399 LYS n 
1 4400 ARG n 
1 4401 THR n 
1 4402 VAL n 
1 4403 GLU n 
1 4404 ASN n 
1 4405 ILE n 
1 4406 LYS n 
1 4407 ASP n 
1 4408 PRO n 
1 4409 LEU n 
1 4410 PHE n 
1 4411 ARG n 
1 4412 PHE n 
1 4413 PHE n 
1 4414 GLU n 
1 4415 ARG n 
1 4416 GLU n 
1 4417 VAL n 
1 4418 LYS n 
1 4419 MET n 
1 4420 GLY n 
1 4421 ALA n 
1 4422 LYS n 
1 4423 LEU n 
1 4424 LEU n 
1 4425 GLN n 
1 4426 ASP n 
1 4427 VAL n 
1 4428 ARG n 
1 4429 GLN n 
1 4430 ASP n 
1 4431 LEU n 
1 4432 ALA n 
1 4433 ASP n 
1 4434 VAL n 
1 4435 VAL n 
1 4436 GLN n 
1 4437 VAL n 
1 4438 CYS n 
1 4439 GLU n 
1 4440 GLY n 
1 4441 LYS n 
1 4442 LYS n 
1 4443 LYS n 
1 4444 GLN n 
1 4445 THR n 
1 4446 ASN n 
1 4447 TYR n 
1 4448 LEU n 
1 4449 ARG n 
1 4450 THR n 
1 4451 LEU n 
1 4452 ILE n 
1 4453 ASN n 
1 4454 GLU n 
1 4455 LEU n 
1 4456 VAL n 
1 4457 LYS n 
1 4458 GLY n 
1 4459 ILE n 
1 4460 LEU n 
1 4461 PRO n 
1 4462 ARG n 
1 4463 SER n 
1 4464 TRP n 
1 4465 SER n 
1 4466 HIS n 
1 4467 TYR n 
1 4468 THR n 
1 4469 VAL n 
1 4470 PRO n 
1 4471 ALA n 
1 4472 GLY n 
1 4473 MET n 
1 4474 THR n 
1 4475 VAL n 
1 4476 ILE n 
1 4477 GLN n 
1 4478 TRP n 
1 4479 VAL n 
1 4480 SER n 
1 4481 ASP n 
1 4482 PHE n 
1 4483 SER n 
1 4484 GLU n 
1 4485 ARG n 
1 4486 ILE n 
1 4487 LYS n 
1 4488 GLN n 
1 4489 LEU n 
1 4490 GLN n 
1 4491 ASN n 
1 4492 ILE n 
1 4493 SER n 
1 4494 LEU n 
1 4495 ALA n 
1 4496 ALA n 
1 4497 ALA n 
1 4498 SER n 
1 4499 GLY n 
1 4500 GLY n 
1 4501 ALA n 
1 4502 LYS n 
1 4503 GLU n 
1 4504 LEU n 
1 4505 LYS n 
1 4506 ASN n 
1 4507 ILE n 
1 4508 HIS n 
1 4509 VAL n 
1 4510 CYS n 
1 4511 LEU n 
1 4512 GLY n 
1 4513 GLY n 
1 4514 LEU n 
1 4515 PHE n 
1 4516 VAL n 
1 4517 PRO n 
1 4518 GLU n 
1 4519 ALA n 
1 4520 TYR n 
1 4521 ILE n 
1 4522 THR n 
1 4523 ALA n 
1 4524 THR n 
1 4525 ARG n 
1 4526 GLN n 
1 4527 TYR n 
1 4528 VAL n 
1 4529 ALA n 
1 4530 GLN n 
1 4531 ALA n 
1 4532 ASN n 
1 4533 SER n 
1 4534 TRP n 
1 4535 SER n 
1 4536 LEU n 
1 4537 GLU n 
1 4538 GLU n 
1 4539 LEU n 
1 4540 CYS n 
1 4541 LEU n 
1 4542 GLU n 
1 4543 VAL n 
1 4544 ASN n 
1 4545 VAL n 
1 4546 THR n 
1 4547 THR n 
1 4548 SER n 
1 4549 GLN n 
1 4550 GLY n 
1 4551 ALA n 
1 4552 THR n 
1 4553 LEU n 
1 4554 ASP n 
1 4555 ALA n 
1 4556 CYS n 
1 4557 SER n 
1 4558 PHE n 
1 4559 GLY n 
1 4560 VAL n 
1 4561 THR n 
1 4562 GLY n 
1 4563 LEU n 
1 4564 LYS n 
1 4565 LEU n 
1 4566 GLN n 
1 4567 GLY n 
1 4568 ALA n 
1 4569 THR n 
1 4570 CYS n 
1 4571 ASN n 
1 4572 ASN n 
1 4573 ASN n 
1 4574 LYS n 
1 4575 LEU n 
1 4576 SER n 
1 4577 LEU n 
1 4578 SER n 
1 4579 ASN n 
1 4580 ALA n 
1 4581 ILE n 
1 4582 SER n 
1 4583 THR n 
1 4584 ALA n 
1 4585 LEU n 
1 4586 PRO n 
1 4587 LEU n 
1 4588 THR n 
1 4589 GLN n 
1 4590 LEU n 
1 4591 ARG n 
1 4592 TRP n 
1 4593 VAL n 
1 4594 LYS n 
1 4595 GLN n 
1 4596 THR n 
1 4597 ASN n 
1 4598 THR n 
1 4599 GLU n 
1 4600 LYS n 
1 4601 LYS n 
1 4602 ALA n 
1 4603 SER n 
1 4604 VAL n 
1 4605 VAL n 
1 4606 THR n 
1 4607 LEU n 
1 4608 PRO n 
1 4609 VAL n 
1 4610 TYR n 
1 4611 LEU n 
1 4612 ASN n 
1 4613 PHE n 
1 4614 THR n 
1 4615 ARG n 
1 4616 ALA n 
1 4617 ASP n 
1 4618 LEU n 
1 4619 ILE n 
1 4620 PHE n 
1 4621 THR n 
1 4622 VAL n 
1 4623 ASP n 
1 4624 PHE n 
1 4625 GLU n 
1 4626 ILE n 
1 4627 ALA n 
1 4628 THR n 
1 4629 LYS n 
1 4630 GLU n 
1 4631 ASP n 
1 4632 PRO n 
1 4633 ARG n 
1 4634 SER n 
1 4635 PHE n 
1 4636 TYR n 
1 4637 GLU n 
1 4638 ARG n 
1 4639 GLY n 
1 4640 VAL n 
1 4641 ALA n 
1 4642 VAL n 
1 4643 LEU n 
1 4644 CYS n 
1 4645 THR n 
1 4646 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   4646 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               'fall armyworm' 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O10 P2' 427.201 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    GLU 3    3    ?    ?   ?   A . n 
A 1 4    PRO 4    4    ?    ?   ?   A . n 
A 1 5    GLY 5    5    ?    ?   ?   A . n 
A 1 6    GLY 6    6    ?    ?   ?   A . n 
A 1 7    GLY 7    7    ?    ?   ?   A . n 
A 1 8    GLY 8    8    ?    ?   ?   A . n 
A 1 9    GLY 9    9    ?    ?   ?   A . n 
A 1 10   GLU 10   10   ?    ?   ?   A . n 
A 1 11   ASP 11   11   ?    ?   ?   A . n 
A 1 12   GLY 12   12   ?    ?   ?   A . n 
A 1 13   SER 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   GLY 15   15   ?    ?   ?   A . n 
A 1 16   LEU 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   SER 19   19   ?    ?   ?   A . n 
A 1 20   ALA 20   20   ?    ?   ?   A . n 
A 1 21   VAL 21   21   ?    ?   ?   A . n 
A 1 22   GLN 22   22   ?    ?   ?   A . n 
A 1 23   ASN 23   23   ?    ?   ?   A . n 
A 1 24   VAL 24   24   ?    ?   ?   A . n 
A 1 25   ALA 25   25   ?    ?   ?   A . n 
A 1 26   ASP 26   26   ?    ?   ?   A . n 
A 1 27   VAL 27   27   ?    ?   ?   A . n 
A 1 28   SER 28   28   ?    ?   ?   A . n 
A 1 29   VAL 29   29   ?    ?   ?   A . n 
A 1 30   LEU 30   30   ?    ?   ?   A . n 
A 1 31   GLN 31   31   ?    ?   ?   A . n 
A 1 32   LYS 32   32   ?    ?   ?   A . n 
A 1 33   HIS 33   33   ?    ?   ?   A . n 
A 1 34   LEU 34   34   ?    ?   ?   A . n 
A 1 35   ARG 35   35   ?    ?   ?   A . n 
A 1 36   LYS 36   36   ?    ?   ?   A . n 
A 1 37   LEU 37   37   ?    ?   ?   A . n 
A 1 38   VAL 38   38   ?    ?   ?   A . n 
A 1 39   PRO 39   39   ?    ?   ?   A . n 
A 1 40   LEU 40   40   ?    ?   ?   A . n 
A 1 41   LEU 41   41   ?    ?   ?   A . n 
A 1 42   LEU 42   42   ?    ?   ?   A . n 
A 1 43   GLU 43   43   ?    ?   ?   A . n 
A 1 44   ASP 44   44   ?    ?   ?   A . n 
A 1 45   GLY 45   45   ?    ?   ?   A . n 
A 1 46   GLY 46   46   ?    ?   ?   A . n 
A 1 47   GLU 47   47   ?    ?   ?   A . n 
A 1 48   ALA 48   48   ?    ?   ?   A . n 
A 1 49   PRO 49   49   ?    ?   ?   A . n 
A 1 50   ALA 50   50   ?    ?   ?   A . n 
A 1 51   ALA 51   51   ?    ?   ?   A . n 
A 1 52   LEU 52   52   ?    ?   ?   A . n 
A 1 53   GLU 53   53   ?    ?   ?   A . n 
A 1 54   ALA 54   54   ?    ?   ?   A . n 
A 1 55   ALA 55   55   ?    ?   ?   A . n 
A 1 56   LEU 56   56   ?    ?   ?   A . n 
A 1 57   GLU 57   57   ?    ?   ?   A . n 
A 1 58   GLU 58   58   ?    ?   ?   A . n 
A 1 59   LYS 59   59   ?    ?   ?   A . n 
A 1 60   SER 60   60   ?    ?   ?   A . n 
A 1 61   ALA 61   61   ?    ?   ?   A . n 
A 1 62   LEU 62   62   ?    ?   ?   A . n 
A 1 63   GLU 63   63   ?    ?   ?   A . n 
A 1 64   GLN 64   64   ?    ?   ?   A . n 
A 1 65   MET 65   65   ?    ?   ?   A . n 
A 1 66   ARG 66   66   ?    ?   ?   A . n 
A 1 67   LYS 67   67   ?    ?   ?   A . n 
A 1 68   PHE 68   68   ?    ?   ?   A . n 
A 1 69   LEU 69   69   ?    ?   ?   A . n 
A 1 70   SER 70   70   ?    ?   ?   A . n 
A 1 71   ASP 71   71   ?    ?   ?   A . n 
A 1 72   PRO 72   72   ?    ?   ?   A . n 
A 1 73   GLN 73   73   ?    ?   ?   A . n 
A 1 74   VAL 74   74   ?    ?   ?   A . n 
A 1 75   HIS 75   75   ?    ?   ?   A . n 
A 1 76   THR 76   76   ?    ?   ?   A . n 
A 1 77   VAL 77   77   ?    ?   ?   A . n 
A 1 78   LEU 78   78   ?    ?   ?   A . n 
A 1 79   VAL 79   79   ?    ?   ?   A . n 
A 1 80   GLU 80   80   ?    ?   ?   A . n 
A 1 81   ARG 81   81   ?    ?   ?   A . n 
A 1 82   SER 82   82   ?    ?   ?   A . n 
A 1 83   THR 83   83   ?    ?   ?   A . n 
A 1 84   LEU 84   84   ?    ?   ?   A . n 
A 1 85   LYS 85   85   ?    ?   ?   A . n 
A 1 86   GLU 86   86   ?    ?   ?   A . n 
A 1 87   ASP 87   87   ?    ?   ?   A . n 
A 1 88   VAL 88   88   ?    ?   ?   A . n 
A 1 89   GLY 89   89   ?    ?   ?   A . n 
A 1 90   ASP 90   90   ?    ?   ?   A . n 
A 1 91   GLU 91   91   ?    ?   ?   A . n 
A 1 92   GLY 92   92   ?    ?   ?   A . n 
A 1 93   GLU 93   93   ?    ?   ?   A . n 
A 1 94   GLU 94   94   ?    ?   ?   A . n 
A 1 95   GLU 95   95   ?    ?   ?   A . n 
A 1 96   LYS 96   96   ?    ?   ?   A . n 
A 1 97   GLU 97   97   ?    ?   ?   A . n 
A 1 98   PHE 98   98   ?    ?   ?   A . n 
A 1 99   ILE 99   99   ?    ?   ?   A . n 
A 1 100  SER 100  100  ?    ?   ?   A . n 
A 1 101  TYR 101  101  ?    ?   ?   A . n 
A 1 102  ASN 102  102  ?    ?   ?   A . n 
A 1 103  ILE 103  103  ?    ?   ?   A . n 
A 1 104  ASN 104  104  ?    ?   ?   A . n 
A 1 105  ILE 105  105  ?    ?   ?   A . n 
A 1 106  ASP 106  106  ?    ?   ?   A . n 
A 1 107  ILE 107  107  ?    ?   ?   A . n 
A 1 108  HIS 108  108  ?    ?   ?   A . n 
A 1 109  TYR 109  109  ?    ?   ?   A . n 
A 1 110  GLY 110  110  ?    ?   ?   A . n 
A 1 111  VAL 111  111  ?    ?   ?   A . n 
A 1 112  LYS 112  112  ?    ?   ?   A . n 
A 1 113  SER 113  113  ?    ?   ?   A . n 
A 1 114  ASN 114  114  ?    ?   ?   A . n 
A 1 115  SER 115  115  ?    ?   ?   A . n 
A 1 116  LEU 116  116  ?    ?   ?   A . n 
A 1 117  ALA 117  117  ?    ?   ?   A . n 
A 1 118  PHE 118  118  ?    ?   ?   A . n 
A 1 119  ILE 119  119  ?    ?   ?   A . n 
A 1 120  LYS 120  120  ?    ?   ?   A . n 
A 1 121  ARG 121  121  ?    ?   ?   A . n 
A 1 122  THR 122  122  ?    ?   ?   A . n 
A 1 123  PRO 123  123  ?    ?   ?   A . n 
A 1 124  VAL 124  124  ?    ?   ?   A . n 
A 1 125  ILE 125  125  ?    ?   ?   A . n 
A 1 126  ASP 126  126  ?    ?   ?   A . n 
A 1 127  ALA 127  127  ?    ?   ?   A . n 
A 1 128  ASP 128  128  ?    ?   ?   A . n 
A 1 129  LYS 129  129  ?    ?   ?   A . n 
A 1 130  PRO 130  130  ?    ?   ?   A . n 
A 1 131  VAL 131  131  ?    ?   ?   A . n 
A 1 132  SER 132  132  ?    ?   ?   A . n 
A 1 133  SER 133  133  ?    ?   ?   A . n 
A 1 134  GLN 134  134  ?    ?   ?   A . n 
A 1 135  LEU 135  135  ?    ?   ?   A . n 
A 1 136  ARG 136  136  ?    ?   ?   A . n 
A 1 137  VAL 137  137  ?    ?   ?   A . n 
A 1 138  LEU 138  138  ?    ?   ?   A . n 
A 1 139  THR 139  139  ?    ?   ?   A . n 
A 1 140  LEU 140  140  ?    ?   ?   A . n 
A 1 141  SER 141  141  ?    ?   ?   A . n 
A 1 142  GLU 142  142  ?    ?   ?   A . n 
A 1 143  ASP 143  143  ?    ?   ?   A . n 
A 1 144  SER 144  144  ?    ?   ?   A . n 
A 1 145  PRO 145  145  ?    ?   ?   A . n 
A 1 146  TYR 146  146  ?    ?   ?   A . n 
A 1 147  GLU 147  147  ?    ?   ?   A . n 
A 1 148  THR 148  148  ?    ?   ?   A . n 
A 1 149  LEU 149  149  ?    ?   ?   A . n 
A 1 150  HIS 150  150  ?    ?   ?   A . n 
A 1 151  SER 151  151  ?    ?   ?   A . n 
A 1 152  PHE 152  152  ?    ?   ?   A . n 
A 1 153  ILE 153  153  ?    ?   ?   A . n 
A 1 154  SER 154  154  ?    ?   ?   A . n 
A 1 155  ASN 155  155  ?    ?   ?   A . n 
A 1 156  ALA 156  156  ?    ?   ?   A . n 
A 1 157  VAL 157  157  ?    ?   ?   A . n 
A 1 158  ALA 158  158  ?    ?   ?   A . n 
A 1 159  PRO 159  159  ?    ?   ?   A . n 
A 1 160  PHE 160  160  ?    ?   ?   A . n 
A 1 161  PHE 161  161  ?    ?   ?   A . n 
A 1 162  LYS 162  162  ?    ?   ?   A . n 
A 1 163  SER 163  163  ?    ?   ?   A . n 
A 1 164  TYR 164  164  ?    ?   ?   A . n 
A 1 165  ILE 165  165  ?    ?   ?   A . n 
A 1 166  ARG 166  166  ?    ?   ?   A . n 
A 1 167  GLU 167  167  ?    ?   ?   A . n 
A 1 168  SER 168  168  ?    ?   ?   A . n 
A 1 169  GLY 169  169  ?    ?   ?   A . n 
A 1 170  LYS 170  170  ?    ?   ?   A . n 
A 1 171  ALA 171  171  ?    ?   ?   A . n 
A 1 172  ASP 172  172  ?    ?   ?   A . n 
A 1 173  ARG 173  173  ?    ?   ?   A . n 
A 1 174  ASP 174  174  ?    ?   ?   A . n 
A 1 175  GLY 175  175  ?    ?   ?   A . n 
A 1 176  ASP 176  176  ?    ?   ?   A . n 
A 1 177  LYS 177  177  ?    ?   ?   A . n 
A 1 178  MET 178  178  ?    ?   ?   A . n 
A 1 179  ALA 179  179  ?    ?   ?   A . n 
A 1 180  PRO 180  180  ?    ?   ?   A . n 
A 1 181  SER 181  181  ?    ?   ?   A . n 
A 1 182  VAL 182  182  ?    ?   ?   A . n 
A 1 183  GLU 183  183  ?    ?   ?   A . n 
A 1 184  LYS 184  184  ?    ?   ?   A . n 
A 1 185  LYS 185  185  ?    ?   ?   A . n 
A 1 186  ILE 186  186  ?    ?   ?   A . n 
A 1 187  ALA 187  187  ?    ?   ?   A . n 
A 1 188  GLU 188  188  ?    ?   ?   A . n 
A 1 189  LEU 189  189  ?    ?   ?   A . n 
A 1 190  GLU 190  190  ?    ?   ?   A . n 
A 1 191  MET 191  191  ?    ?   ?   A . n 
A 1 192  GLY 192  192  ?    ?   ?   A . n 
A 1 193  LEU 193  193  ?    ?   ?   A . n 
A 1 194  LEU 194  194  ?    ?   ?   A . n 
A 1 195  HIS 195  195  ?    ?   ?   A . n 
A 1 196  LEU 196  196  ?    ?   ?   A . n 
A 1 197  GLN 197  197  ?    ?   ?   A . n 
A 1 198  GLN 198  198  ?    ?   ?   A . n 
A 1 199  ASN 199  199  ?    ?   ?   A . n 
A 1 200  ILE 200  200  ?    ?   ?   A . n 
A 1 201  GLU 201  201  ?    ?   ?   A . n 
A 1 202  ILE 202  202  ?    ?   ?   A . n 
A 1 203  PRO 203  203  ?    ?   ?   A . n 
A 1 204  GLU 204  204  ?    ?   ?   A . n 
A 1 205  ILE 205  205  ?    ?   ?   A . n 
A 1 206  SER 206  206  ?    ?   ?   A . n 
A 1 207  LEU 207  207  ?    ?   ?   A . n 
A 1 208  PRO 208  208  ?    ?   ?   A . n 
A 1 209  ILE 209  209  ?    ?   ?   A . n 
A 1 210  HIS 210  210  ?    ?   ?   A . n 
A 1 211  PRO 211  211  ?    ?   ?   A . n 
A 1 212  MET 212  212  ?    ?   ?   A . n 
A 1 213  ILE 213  213  ?    ?   ?   A . n 
A 1 214  THR 214  214  ?    ?   ?   A . n 
A 1 215  ASN 215  215  ?    ?   ?   A . n 
A 1 216  VAL 216  216  ?    ?   ?   A . n 
A 1 217  ALA 217  217  ?    ?   ?   A . n 
A 1 218  LYS 218  218  ?    ?   ?   A . n 
A 1 219  GLN 219  219  ?    ?   ?   A . n 
A 1 220  CYS 220  220  ?    ?   ?   A . n 
A 1 221  TYR 221  221  ?    ?   ?   A . n 
A 1 222  GLU 222  222  ?    ?   ?   A . n 
A 1 223  ARG 223  223  ?    ?   ?   A . n 
A 1 224  GLY 224  224  ?    ?   ?   A . n 
A 1 225  GLU 225  225  ?    ?   ?   A . n 
A 1 226  LYS 226  226  ?    ?   ?   A . n 
A 1 227  PRO 227  227  ?    ?   ?   A . n 
A 1 228  LYS 228  228  ?    ?   ?   A . n 
A 1 229  VAL 229  229  ?    ?   ?   A . n 
A 1 230  THR 230  230  ?    ?   ?   A . n 
A 1 231  ASP 231  231  ?    ?   ?   A . n 
A 1 232  PHE 232  232  ?    ?   ?   A . n 
A 1 233  GLY 233  233  ?    ?   ?   A . n 
A 1 234  ASP 234  234  ?    ?   ?   A . n 
A 1 235  LYS 235  235  ?    ?   ?   A . n 
A 1 236  VAL 236  236  ?    ?   ?   A . n 
A 1 237  GLU 237  237  ?    ?   ?   A . n 
A 1 238  ASP 238  238  ?    ?   ?   A . n 
A 1 239  PRO 239  239  ?    ?   ?   A . n 
A 1 240  THR 240  240  ?    ?   ?   A . n 
A 1 241  PHE 241  241  ?    ?   ?   A . n 
A 1 242  LEU 242  242  ?    ?   ?   A . n 
A 1 243  ASN 243  243  ?    ?   ?   A . n 
A 1 244  GLN 244  244  ?    ?   ?   A . n 
A 1 245  LEU 245  245  ?    ?   ?   A . n 
A 1 246  GLN 246  246  ?    ?   ?   A . n 
A 1 247  SER 247  247  ?    ?   ?   A . n 
A 1 248  GLY 248  248  ?    ?   ?   A . n 
A 1 249  VAL 249  249  ?    ?   ?   A . n 
A 1 250  ASN 250  250  ?    ?   ?   A . n 
A 1 251  ARG 251  251  ?    ?   ?   A . n 
A 1 252  TRP 252  252  ?    ?   ?   A . n 
A 1 253  ILE 253  253  ?    ?   ?   A . n 
A 1 254  ARG 254  254  ?    ?   ?   A . n 
A 1 255  GLU 255  255  ?    ?   ?   A . n 
A 1 256  ILE 256  256  ?    ?   ?   A . n 
A 1 257  GLN 257  257  ?    ?   ?   A . n 
A 1 258  LYS 258  258  ?    ?   ?   A . n 
A 1 259  VAL 259  259  ?    ?   ?   A . n 
A 1 260  THR 260  260  ?    ?   ?   A . n 
A 1 261  LYS 261  261  ?    ?   ?   A . n 
A 1 262  LEU 262  262  ?    ?   ?   A . n 
A 1 263  ASP 263  263  ?    ?   ?   A . n 
A 1 264  ARG 264  264  ?    ?   ?   A . n 
A 1 265  ASP 265  265  ?    ?   ?   A . n 
A 1 266  PRO 266  266  ?    ?   ?   A . n 
A 1 267  ALA 267  267  ?    ?   ?   A . n 
A 1 268  SER 268  268  ?    ?   ?   A . n 
A 1 269  GLY 269  269  ?    ?   ?   A . n 
A 1 270  THR 270  270  ?    ?   ?   A . n 
A 1 271  ALA 271  271  ?    ?   ?   A . n 
A 1 272  LEU 272  272  ?    ?   ?   A . n 
A 1 273  GLN 273  273  ?    ?   ?   A . n 
A 1 274  GLU 274  274  ?    ?   ?   A . n 
A 1 275  ILE 275  275  ?    ?   ?   A . n 
A 1 276  SER 276  276  ?    ?   ?   A . n 
A 1 277  PHE 277  277  ?    ?   ?   A . n 
A 1 278  TRP 278  278  ?    ?   ?   A . n 
A 1 279  LEU 279  279  ?    ?   ?   A . n 
A 1 280  ASN 280  280  ?    ?   ?   A . n 
A 1 281  LEU 281  281  ?    ?   ?   A . n 
A 1 282  GLU 282  282  ?    ?   ?   A . n 
A 1 283  ARG 283  283  ?    ?   ?   A . n 
A 1 284  ALA 284  284  ?    ?   ?   A . n 
A 1 285  LEU 285  285  ?    ?   ?   A . n 
A 1 286  TYR 286  286  ?    ?   ?   A . n 
A 1 287  ARG 287  287  ?    ?   ?   A . n 
A 1 288  ILE 288  288  ?    ?   ?   A . n 
A 1 289  GLN 289  289  ?    ?   ?   A . n 
A 1 290  GLU 290  290  ?    ?   ?   A . n 
A 1 291  LYS 291  291  ?    ?   ?   A . n 
A 1 292  ARG 292  292  ?    ?   ?   A . n 
A 1 293  GLU 293  293  ?    ?   ?   A . n 
A 1 294  SER 294  294  ?    ?   ?   A . n 
A 1 295  PRO 295  295  ?    ?   ?   A . n 
A 1 296  GLU 296  296  ?    ?   ?   A . n 
A 1 297  VAL 297  297  ?    ?   ?   A . n 
A 1 298  LEU 298  298  ?    ?   ?   A . n 
A 1 299  LEU 299  299  ?    ?   ?   A . n 
A 1 300  THR 300  300  ?    ?   ?   A . n 
A 1 301  LEU 301  301  ?    ?   ?   A . n 
A 1 302  ASP 302  302  ?    ?   ?   A . n 
A 1 303  ILE 303  303  ?    ?   ?   A . n 
A 1 304  LEU 304  304  ?    ?   ?   A . n 
A 1 305  LYS 305  305  ?    ?   ?   A . n 
A 1 306  HIS 306  306  ?    ?   ?   A . n 
A 1 307  GLY 307  307  ?    ?   ?   A . n 
A 1 308  LYS 308  308  ?    ?   ?   A . n 
A 1 309  ARG 309  309  ?    ?   ?   A . n 
A 1 310  PHE 310  310  ?    ?   ?   A . n 
A 1 311  HIS 311  311  ?    ?   ?   A . n 
A 1 312  ALA 312  312  ?    ?   ?   A . n 
A 1 313  THR 313  313  ?    ?   ?   A . n 
A 1 314  VAL 314  314  ?    ?   ?   A . n 
A 1 315  SER 315  315  ?    ?   ?   A . n 
A 1 316  PHE 316  316  ?    ?   ?   A . n 
A 1 317  ASP 317  317  ?    ?   ?   A . n 
A 1 318  THR 318  318  ?    ?   ?   A . n 
A 1 319  ASP 319  319  ?    ?   ?   A . n 
A 1 320  THR 320  320  ?    ?   ?   A . n 
A 1 321  GLY 321  321  ?    ?   ?   A . n 
A 1 322  LEU 322  322  ?    ?   ?   A . n 
A 1 323  LYS 323  323  ?    ?   ?   A . n 
A 1 324  GLN 324  324  ?    ?   ?   A . n 
A 1 325  ALA 325  325  ?    ?   ?   A . n 
A 1 326  LEU 326  326  ?    ?   ?   A . n 
A 1 327  GLU 327  327  ?    ?   ?   A . n 
A 1 328  THR 328  328  ?    ?   ?   A . n 
A 1 329  VAL 329  329  ?    ?   ?   A . n 
A 1 330  ASN 330  330  ?    ?   ?   A . n 
A 1 331  ASP 331  331  ?    ?   ?   A . n 
A 1 332  TYR 332  332  ?    ?   ?   A . n 
A 1 333  ASN 333  333  ?    ?   ?   A . n 
A 1 334  PRO 334  334  ?    ?   ?   A . n 
A 1 335  LEU 335  335  ?    ?   ?   A . n 
A 1 336  MET 336  336  ?    ?   ?   A . n 
A 1 337  LYS 337  337  ?    ?   ?   A . n 
A 1 338  ASP 338  338  ?    ?   ?   A . n 
A 1 339  PHE 339  339  ?    ?   ?   A . n 
A 1 340  PRO 340  340  ?    ?   ?   A . n 
A 1 341  LEU 341  341  ?    ?   ?   A . n 
A 1 342  ASN 342  342  ?    ?   ?   A . n 
A 1 343  ASP 343  343  ?    ?   ?   A . n 
A 1 344  LEU 344  344  ?    ?   ?   A . n 
A 1 345  LEU 345  345  ?    ?   ?   A . n 
A 1 346  SER 346  346  ?    ?   ?   A . n 
A 1 347  ALA 347  347  ?    ?   ?   A . n 
A 1 348  THR 348  348  ?    ?   ?   A . n 
A 1 349  GLU 349  349  ?    ?   ?   A . n 
A 1 350  LEU 350  350  ?    ?   ?   A . n 
A 1 351  ASP 351  351  ?    ?   ?   A . n 
A 1 352  LYS 352  352  ?    ?   ?   A . n 
A 1 353  ILE 353  353  ?    ?   ?   A . n 
A 1 354  ARG 354  354  ?    ?   ?   A . n 
A 1 355  GLN 355  355  ?    ?   ?   A . n 
A 1 356  ALA 356  356  ?    ?   ?   A . n 
A 1 357  LEU 357  357  ?    ?   ?   A . n 
A 1 358  VAL 358  358  ?    ?   ?   A . n 
A 1 359  ALA 359  359  ?    ?   ?   A . n 
A 1 360  ILE 360  360  ?    ?   ?   A . n 
A 1 361  PHE 361  361  ?    ?   ?   A . n 
A 1 362  THR 362  362  ?    ?   ?   A . n 
A 1 363  HIS 363  363  ?    ?   ?   A . n 
A 1 364  LEU 364  364  ?    ?   ?   A . n 
A 1 365  ARG 365  365  ?    ?   ?   A . n 
A 1 366  LYS 366  366  ?    ?   ?   A . n 
A 1 367  ILE 367  367  ?    ?   ?   A . n 
A 1 368  ARG 368  368  ?    ?   ?   A . n 
A 1 369  ASN 369  369  ?    ?   ?   A . n 
A 1 370  THR 370  370  ?    ?   ?   A . n 
A 1 371  LYS 371  371  ?    ?   ?   A . n 
A 1 372  TYR 372  372  ?    ?   ?   A . n 
A 1 373  PRO 373  373  ?    ?   ?   A . n 
A 1 374  ILE 374  374  ?    ?   ?   A . n 
A 1 375  GLN 375  375  ?    ?   ?   A . n 
A 1 376  ARG 376  376  ?    ?   ?   A . n 
A 1 377  ALA 377  377  ?    ?   ?   A . n 
A 1 378  LEU 378  378  ?    ?   ?   A . n 
A 1 379  ARG 379  379  ?    ?   ?   A . n 
A 1 380  LEU 380  380  ?    ?   ?   A . n 
A 1 381  VAL 381  381  ?    ?   ?   A . n 
A 1 382  GLU 382  382  ?    ?   ?   A . n 
A 1 383  ALA 383  383  ?    ?   ?   A . n 
A 1 384  ILE 384  384  ?    ?   ?   A . n 
A 1 385  SER 385  385  ?    ?   ?   A . n 
A 1 386  ARG 386  386  ?    ?   ?   A . n 
A 1 387  ASP 387  387  ?    ?   ?   A . n 
A 1 388  LEU 388  388  ?    ?   ?   A . n 
A 1 389  SER 389  389  ?    ?   ?   A . n 
A 1 390  SER 390  390  ?    ?   ?   A . n 
A 1 391  GLN 391  391  ?    ?   ?   A . n 
A 1 392  LEU 392  392  ?    ?   ?   A . n 
A 1 393  LEU 393  393  ?    ?   ?   A . n 
A 1 394  LYS 394  394  ?    ?   ?   A . n 
A 1 395  VAL 395  395  ?    ?   ?   A . n 
A 1 396  LEU 396  396  ?    ?   ?   A . n 
A 1 397  GLY 397  397  ?    ?   ?   A . n 
A 1 398  THR 398  398  ?    ?   ?   A . n 
A 1 399  ARG 399  399  ?    ?   ?   A . n 
A 1 400  LYS 400  400  ?    ?   ?   A . n 
A 1 401  LEU 401  401  ?    ?   ?   A . n 
A 1 402  MET 402  402  ?    ?   ?   A . n 
A 1 403  HIS 403  403  ?    ?   ?   A . n 
A 1 404  VAL 404  404  ?    ?   ?   A . n 
A 1 405  ALA 405  405  ?    ?   ?   A . n 
A 1 406  TYR 406  406  ?    ?   ?   A . n 
A 1 407  GLU 407  407  ?    ?   ?   A . n 
A 1 408  GLU 408  408  ?    ?   ?   A . n 
A 1 409  PHE 409  409  ?    ?   ?   A . n 
A 1 410  GLU 410  410  ?    ?   ?   A . n 
A 1 411  LYS 411  411  ?    ?   ?   A . n 
A 1 412  VAL 412  412  ?    ?   ?   A . n 
A 1 413  MET 413  413  ?    ?   ?   A . n 
A 1 414  VAL 414  414  ?    ?   ?   A . n 
A 1 415  ALA 415  415  ?    ?   ?   A . n 
A 1 416  CYS 416  416  ?    ?   ?   A . n 
A 1 417  PHE 417  417  ?    ?   ?   A . n 
A 1 418  GLU 418  418  ?    ?   ?   A . n 
A 1 419  VAL 419  419  ?    ?   ?   A . n 
A 1 420  PHE 420  420  ?    ?   ?   A . n 
A 1 421  GLN 421  421  ?    ?   ?   A . n 
A 1 422  THR 422  422  ?    ?   ?   A . n 
A 1 423  TRP 423  423  ?    ?   ?   A . n 
A 1 424  ASP 424  424  ?    ?   ?   A . n 
A 1 425  ASP 425  425  ?    ?   ?   A . n 
A 1 426  GLU 426  426  ?    ?   ?   A . n 
A 1 427  TYR 427  427  ?    ?   ?   A . n 
A 1 428  GLU 428  428  ?    ?   ?   A . n 
A 1 429  LYS 429  429  ?    ?   ?   A . n 
A 1 430  LEU 430  430  ?    ?   ?   A . n 
A 1 431  GLN 431  431  ?    ?   ?   A . n 
A 1 432  VAL 432  432  ?    ?   ?   A . n 
A 1 433  LEU 433  433  ?    ?   ?   A . n 
A 1 434  LEU 434  434  ?    ?   ?   A . n 
A 1 435  ARG 435  435  ?    ?   ?   A . n 
A 1 436  ASP 436  436  ?    ?   ?   A . n 
A 1 437  ILE 437  437  ?    ?   ?   A . n 
A 1 438  VAL 438  438  ?    ?   ?   A . n 
A 1 439  LYS 439  439  ?    ?   ?   A . n 
A 1 440  ARG 440  440  ?    ?   ?   A . n 
A 1 441  LYS 441  441  ?    ?   ?   A . n 
A 1 442  ARG 442  442  ?    ?   ?   A . n 
A 1 443  GLU 443  443  ?    ?   ?   A . n 
A 1 444  GLU 444  444  ?    ?   ?   A . n 
A 1 445  ASN 445  445  ?    ?   ?   A . n 
A 1 446  LEU 446  446  ?    ?   ?   A . n 
A 1 447  LYS 447  447  ?    ?   ?   A . n 
A 1 448  MET 448  448  ?    ?   ?   A . n 
A 1 449  VAL 449  449  ?    ?   ?   A . n 
A 1 450  TRP 450  450  ?    ?   ?   A . n 
A 1 451  ARG 451  451  ?    ?   ?   A . n 
A 1 452  ILE 452  452  ?    ?   ?   A . n 
A 1 453  ASN 453  453  ?    ?   ?   A . n 
A 1 454  PRO 454  454  ?    ?   ?   A . n 
A 1 455  ALA 455  455  ?    ?   ?   A . n 
A 1 456  HIS 456  456  ?    ?   ?   A . n 
A 1 457  ARG 457  457  ?    ?   ?   A . n 
A 1 458  LYS 458  458  ?    ?   ?   A . n 
A 1 459  LEU 459  459  ?    ?   ?   A . n 
A 1 460  GLN 460  460  ?    ?   ?   A . n 
A 1 461  ALA 461  461  ?    ?   ?   A . n 
A 1 462  ARG 462  462  ?    ?   ?   A . n 
A 1 463  LEU 463  463  ?    ?   ?   A . n 
A 1 464  ASP 464  464  ?    ?   ?   A . n 
A 1 465  GLN 465  465  ?    ?   ?   A . n 
A 1 466  MET 466  466  ?    ?   ?   A . n 
A 1 467  ARG 467  467  ?    ?   ?   A . n 
A 1 468  LYS 468  468  ?    ?   ?   A . n 
A 1 469  PHE 469  469  ?    ?   ?   A . n 
A 1 470  ARG 470  470  ?    ?   ?   A . n 
A 1 471  ARG 471  471  ?    ?   ?   A . n 
A 1 472  GLN 472  472  ?    ?   ?   A . n 
A 1 473  HIS 473  473  ?    ?   ?   A . n 
A 1 474  GLU 474  474  ?    ?   ?   A . n 
A 1 475  GLN 475  475  ?    ?   ?   A . n 
A 1 476  LEU 476  476  ?    ?   ?   A . n 
A 1 477  ARG 477  477  ?    ?   ?   A . n 
A 1 478  ALA 478  478  ?    ?   ?   A . n 
A 1 479  VAL 479  479  ?    ?   ?   A . n 
A 1 480  ILE 480  480  ?    ?   ?   A . n 
A 1 481  VAL 481  481  ?    ?   ?   A . n 
A 1 482  ARG 482  482  ?    ?   ?   A . n 
A 1 483  VAL 483  483  ?    ?   ?   A . n 
A 1 484  LEU 484  484  ?    ?   ?   A . n 
A 1 485  ARG 485  485  ?    ?   ?   A . n 
A 1 486  PRO 486  486  ?    ?   ?   A . n 
A 1 487  GLN 487  487  ?    ?   ?   A . n 
A 1 488  VAL 488  488  ?    ?   ?   A . n 
A 1 489  THR 489  489  ?    ?   ?   A . n 
A 1 490  ALA 490  490  ?    ?   ?   A . n 
A 1 491  VAL 491  491  ?    ?   ?   A . n 
A 1 492  ALA 492  492  ?    ?   ?   A . n 
A 1 493  GLN 493  493  ?    ?   ?   A . n 
A 1 494  GLN 494  494  ?    ?   ?   A . n 
A 1 495  ASN 495  495  ?    ?   ?   A . n 
A 1 496  GLN 496  496  ?    ?   ?   A . n 
A 1 497  GLY 497  497  ?    ?   ?   A . n 
A 1 498  GLU 498  498  ?    ?   ?   A . n 
A 1 499  VAL 499  499  ?    ?   ?   A . n 
A 1 500  PRO 500  500  ?    ?   ?   A . n 
A 1 501  GLU 501  501  ?    ?   ?   A . n 
A 1 502  PRO 502  502  ?    ?   ?   A . n 
A 1 503  GLN 503  503  ?    ?   ?   A . n 
A 1 504  ASP 504  504  ?    ?   ?   A . n 
A 1 505  MET 505  505  ?    ?   ?   A . n 
A 1 506  LYS 506  506  ?    ?   ?   A . n 
A 1 507  VAL 507  507  ?    ?   ?   A . n 
A 1 508  ALA 508  508  ?    ?   ?   A . n 
A 1 509  GLU 509  509  ?    ?   ?   A . n 
A 1 510  VAL 510  510  ?    ?   ?   A . n 
A 1 511  LEU 511  511  ?    ?   ?   A . n 
A 1 512  PHE 512  512  ?    ?   ?   A . n 
A 1 513  ASP 513  513  ?    ?   ?   A . n 
A 1 514  ALA 514  514  ?    ?   ?   A . n 
A 1 515  ALA 515  515  ?    ?   ?   A . n 
A 1 516  ASP 516  516  ?    ?   ?   A . n 
A 1 517  ALA 517  517  ?    ?   ?   A . n 
A 1 518  ASN 518  518  ?    ?   ?   A . n 
A 1 519  ALA 519  519  ?    ?   ?   A . n 
A 1 520  ILE 520  520  ?    ?   ?   A . n 
A 1 521  GLU 521  521  ?    ?   ?   A . n 
A 1 522  GLU 522  522  ?    ?   ?   A . n 
A 1 523  VAL 523  523  ?    ?   ?   A . n 
A 1 524  ASN 524  524  ?    ?   ?   A . n 
A 1 525  LEU 525  525  ?    ?   ?   A . n 
A 1 526  ALA 526  526  ?    ?   ?   A . n 
A 1 527  TYR 527  527  ?    ?   ?   A . n 
A 1 528  GLU 528  528  ?    ?   ?   A . n 
A 1 529  ASN 529  529  ?    ?   ?   A . n 
A 1 530  VAL 530  530  ?    ?   ?   A . n 
A 1 531  LYS 531  531  ?    ?   ?   A . n 
A 1 532  GLU 532  532  ?    ?   ?   A . n 
A 1 533  VAL 533  533  ?    ?   ?   A . n 
A 1 534  ASP 534  534  ?    ?   ?   A . n 
A 1 535  GLY 535  535  ?    ?   ?   A . n 
A 1 536  LEU 536  536  ?    ?   ?   A . n 
A 1 537  ASP 537  537  ?    ?   ?   A . n 
A 1 538  VAL 538  538  ?    ?   ?   A . n 
A 1 539  SER 539  539  ?    ?   ?   A . n 
A 1 540  LYS 540  540  ?    ?   ?   A . n 
A 1 541  GLU 541  541  ?    ?   ?   A . n 
A 1 542  GLY 542  542  ?    ?   ?   A . n 
A 1 543  THR 543  543  ?    ?   ?   A . n 
A 1 544  GLU 544  544  ?    ?   ?   A . n 
A 1 545  ALA 545  545  ?    ?   ?   A . n 
A 1 546  TRP 546  546  ?    ?   ?   A . n 
A 1 547  GLU 547  547  ?    ?   ?   A . n 
A 1 548  ALA 548  548  ?    ?   ?   A . n 
A 1 549  ALA 549  549  ?    ?   ?   A . n 
A 1 550  MET 550  550  ?    ?   ?   A . n 
A 1 551  LYS 551  551  ?    ?   ?   A . n 
A 1 552  ARG 552  552  ?    ?   ?   A . n 
A 1 553  TYR 553  553  ?    ?   ?   A . n 
A 1 554  ASP 554  554  ?    ?   ?   A . n 
A 1 555  GLU 555  555  ?    ?   ?   A . n 
A 1 556  ARG 556  556  ?    ?   ?   A . n 
A 1 557  ILE 557  557  ?    ?   ?   A . n 
A 1 558  ASP 558  558  ?    ?   ?   A . n 
A 1 559  ARG 559  559  ?    ?   ?   A . n 
A 1 560  VAL 560  560  ?    ?   ?   A . n 
A 1 561  GLU 561  561  ?    ?   ?   A . n 
A 1 562  THR 562  562  ?    ?   ?   A . n 
A 1 563  ARG 563  563  ?    ?   ?   A . n 
A 1 564  ILE 564  564  ?    ?   ?   A . n 
A 1 565  THR 565  565  ?    ?   ?   A . n 
A 1 566  ALA 566  566  ?    ?   ?   A . n 
A 1 567  ARG 567  567  ?    ?   ?   A . n 
A 1 568  LEU 568  568  ?    ?   ?   A . n 
A 1 569  ARG 569  569  ?    ?   ?   A . n 
A 1 570  ASP 570  570  ?    ?   ?   A . n 
A 1 571  GLN 571  571  ?    ?   ?   A . n 
A 1 572  LEU 572  572  ?    ?   ?   A . n 
A 1 573  GLY 573  573  ?    ?   ?   A . n 
A 1 574  THR 574  574  ?    ?   ?   A . n 
A 1 575  ALA 575  575  ?    ?   ?   A . n 
A 1 576  LYS 576  576  ?    ?   ?   A . n 
A 1 577  ASN 577  577  ?    ?   ?   A . n 
A 1 578  ALA 578  578  ?    ?   ?   A . n 
A 1 579  ASN 579  579  ?    ?   ?   A . n 
A 1 580  GLU 580  580  ?    ?   ?   A . n 
A 1 581  MET 581  581  ?    ?   ?   A . n 
A 1 582  PHE 582  582  ?    ?   ?   A . n 
A 1 583  ARG 583  583  ?    ?   ?   A . n 
A 1 584  ILE 584  584  ?    ?   ?   A . n 
A 1 585  PHE 585  585  ?    ?   ?   A . n 
A 1 586  SER 586  586  ?    ?   ?   A . n 
A 1 587  ARG 587  587  ?    ?   ?   A . n 
A 1 588  PHE 588  588  ?    ?   ?   A . n 
A 1 589  ASN 589  589  ?    ?   ?   A . n 
A 1 590  ALA 590  590  ?    ?   ?   A . n 
A 1 591  LEU 591  591  ?    ?   ?   A . n 
A 1 592  PHE 592  592  ?    ?   ?   A . n 
A 1 593  VAL 593  593  ?    ?   ?   A . n 
A 1 594  ARG 594  594  ?    ?   ?   A . n 
A 1 595  PRO 595  595  ?    ?   ?   A . n 
A 1 596  HIS 596  596  ?    ?   ?   A . n 
A 1 597  ILE 597  597  ?    ?   ?   A . n 
A 1 598  ARG 598  598  ?    ?   ?   A . n 
A 1 599  GLY 599  599  ?    ?   ?   A . n 
A 1 600  ALA 600  600  ?    ?   ?   A . n 
A 1 601  ILE 601  601  ?    ?   ?   A . n 
A 1 602  ARG 602  602  ?    ?   ?   A . n 
A 1 603  GLU 603  603  ?    ?   ?   A . n 
A 1 604  TYR 604  604  ?    ?   ?   A . n 
A 1 605  GLN 605  605  ?    ?   ?   A . n 
A 1 606  THR 606  606  ?    ?   ?   A . n 
A 1 607  GLN 607  607  ?    ?   ?   A . n 
A 1 608  LEU 608  608  ?    ?   ?   A . n 
A 1 609  ILE 609  609  ?    ?   ?   A . n 
A 1 610  GLN 610  610  ?    ?   ?   A . n 
A 1 611  ARG 611  611  ?    ?   ?   A . n 
A 1 612  VAL 612  612  ?    ?   ?   A . n 
A 1 613  LYS 613  613  ?    ?   ?   A . n 
A 1 614  ASP 614  614  ?    ?   ?   A . n 
A 1 615  ASP 615  615  ?    ?   ?   A . n 
A 1 616  ILE 616  616  ?    ?   ?   A . n 
A 1 617  GLU 617  617  ?    ?   ?   A . n 
A 1 618  SER 618  618  ?    ?   ?   A . n 
A 1 619  LEU 619  619  ?    ?   ?   A . n 
A 1 620  HIS 620  620  ?    ?   ?   A . n 
A 1 621  ASP 621  621  ?    ?   ?   A . n 
A 1 622  LYS 622  622  ?    ?   ?   A . n 
A 1 623  PHE 623  623  ?    ?   ?   A . n 
A 1 624  LYS 624  624  ?    ?   ?   A . n 
A 1 625  VAL 625  625  ?    ?   ?   A . n 
A 1 626  GLN 626  626  ?    ?   ?   A . n 
A 1 627  TYR 627  627  ?    ?   ?   A . n 
A 1 628  PRO 628  628  ?    ?   ?   A . n 
A 1 629  GLN 629  629  ?    ?   ?   A . n 
A 1 630  SER 630  630  ?    ?   ?   A . n 
A 1 631  GLN 631  631  ?    ?   ?   A . n 
A 1 632  ALA 632  632  ?    ?   ?   A . n 
A 1 633  CYS 633  633  ?    ?   ?   A . n 
A 1 634  LYS 634  634  ?    ?   ?   A . n 
A 1 635  MET 635  635  ?    ?   ?   A . n 
A 1 636  SER 636  636  ?    ?   ?   A . n 
A 1 637  HIS 637  637  ?    ?   ?   A . n 
A 1 638  VAL 638  638  ?    ?   ?   A . n 
A 1 639  ARG 639  639  ?    ?   ?   A . n 
A 1 640  ASP 640  640  ?    ?   ?   A . n 
A 1 641  LEU 641  641  ?    ?   ?   A . n 
A 1 642  PRO 642  642  ?    ?   ?   A . n 
A 1 643  PRO 643  643  ?    ?   ?   A . n 
A 1 644  VAL 644  644  ?    ?   ?   A . n 
A 1 645  SER 645  645  ?    ?   ?   A . n 
A 1 646  GLY 646  646  ?    ?   ?   A . n 
A 1 647  SER 647  647  ?    ?   ?   A . n 
A 1 648  ILE 648  648  ?    ?   ?   A . n 
A 1 649  ILE 649  649  ?    ?   ?   A . n 
A 1 650  TRP 650  650  ?    ?   ?   A . n 
A 1 651  ALA 651  651  ?    ?   ?   A . n 
A 1 652  LYS 652  652  ?    ?   ?   A . n 
A 1 653  GLN 653  653  ?    ?   ?   A . n 
A 1 654  ILE 654  654  ?    ?   ?   A . n 
A 1 655  ASP 655  655  ?    ?   ?   A . n 
A 1 656  ARG 656  656  ?    ?   ?   A . n 
A 1 657  GLN 657  657  ?    ?   ?   A . n 
A 1 658  LEU 658  658  ?    ?   ?   A . n 
A 1 659  THR 659  659  ?    ?   ?   A . n 
A 1 660  ALA 660  660  ?    ?   ?   A . n 
A 1 661  TYR 661  661  ?    ?   ?   A . n 
A 1 662  MET 662  662  ?    ?   ?   A . n 
A 1 663  LYS 663  663  ?    ?   ?   A . n 
A 1 664  ARG 664  664  ?    ?   ?   A . n 
A 1 665  VAL 665  665  ?    ?   ?   A . n 
A 1 666  GLU 666  666  ?    ?   ?   A . n 
A 1 667  ASP 667  667  ?    ?   ?   A . n 
A 1 668  VAL 668  668  ?    ?   ?   A . n 
A 1 669  LEU 669  669  ?    ?   ?   A . n 
A 1 670  GLY 670  670  ?    ?   ?   A . n 
A 1 671  LYS 671  671  ?    ?   ?   A . n 
A 1 672  GLY 672  672  ?    ?   ?   A . n 
A 1 673  TRP 673  673  ?    ?   ?   A . n 
A 1 674  GLU 674  674  ?    ?   ?   A . n 
A 1 675  ASN 675  675  ?    ?   ?   A . n 
A 1 676  HIS 676  676  ?    ?   ?   A . n 
A 1 677  VAL 677  677  ?    ?   ?   A . n 
A 1 678  GLU 678  678  ?    ?   ?   A . n 
A 1 679  GLY 679  679  ?    ?   ?   A . n 
A 1 680  GLN 680  680  ?    ?   ?   A . n 
A 1 681  LYS 681  681  ?    ?   ?   A . n 
A 1 682  LEU 682  682  ?    ?   ?   A . n 
A 1 683  LYS 683  683  ?    ?   ?   A . n 
A 1 684  GLN 684  684  ?    ?   ?   A . n 
A 1 685  ASP 685  685  ?    ?   ?   A . n 
A 1 686  GLY 686  686  ?    ?   ?   A . n 
A 1 687  ASP 687  687  ?    ?   ?   A . n 
A 1 688  SER 688  688  ?    ?   ?   A . n 
A 1 689  PHE 689  689  ?    ?   ?   A . n 
A 1 690  ARG 690  690  ?    ?   ?   A . n 
A 1 691  MET 691  691  ?    ?   ?   A . n 
A 1 692  LYS 692  692  ?    ?   ?   A . n 
A 1 693  LEU 693  693  ?    ?   ?   A . n 
A 1 694  ASN 694  694  ?    ?   ?   A . n 
A 1 695  THR 695  695  ?    ?   ?   A . n 
A 1 696  GLN 696  696  ?    ?   ?   A . n 
A 1 697  GLU 697  697  ?    ?   ?   A . n 
A 1 698  ILE 698  698  ?    ?   ?   A . n 
A 1 699  PHE 699  699  ?    ?   ?   A . n 
A 1 700  ASP 700  700  ?    ?   ?   A . n 
A 1 701  ASP 701  701  ?    ?   ?   A . n 
A 1 702  TRP 702  702  ?    ?   ?   A . n 
A 1 703  ALA 703  703  ?    ?   ?   A . n 
A 1 704  ARG 704  704  ?    ?   ?   A . n 
A 1 705  LYS 705  705  ?    ?   ?   A . n 
A 1 706  VAL 706  706  ?    ?   ?   A . n 
A 1 707  GLN 707  707  ?    ?   ?   A . n 
A 1 708  GLN 708  708  ?    ?   ?   A . n 
A 1 709  ARG 709  709  ?    ?   ?   A . n 
A 1 710  ASN 710  710  ?    ?   ?   A . n 
A 1 711  LEU 711  711  ?    ?   ?   A . n 
A 1 712  GLY 712  712  ?    ?   ?   A . n 
A 1 713  VAL 713  713  ?    ?   ?   A . n 
A 1 714  SER 714  714  ?    ?   ?   A . n 
A 1 715  GLY 715  715  ?    ?   ?   A . n 
A 1 716  ARG 716  716  ?    ?   ?   A . n 
A 1 717  ILE 717  717  ?    ?   ?   A . n 
A 1 718  PHE 718  718  ?    ?   ?   A . n 
A 1 719  THR 719  719  ?    ?   ?   A . n 
A 1 720  ILE 720  720  ?    ?   ?   A . n 
A 1 721  GLU 721  721  ?    ?   ?   A . n 
A 1 722  SER 722  722  ?    ?   ?   A . n 
A 1 723  THR 723  723  ?    ?   ?   A . n 
A 1 724  ARG 724  724  ?    ?   ?   A . n 
A 1 725  VAL 725  725  ?    ?   ?   A . n 
A 1 726  ARG 726  726  ?    ?   ?   A . n 
A 1 727  GLY 727  727  ?    ?   ?   A . n 
A 1 728  ARG 728  728  ?    ?   ?   A . n 
A 1 729  THR 729  729  ?    ?   ?   A . n 
A 1 730  GLY 730  730  ?    ?   ?   A . n 
A 1 731  ASN 731  731  ?    ?   ?   A . n 
A 1 732  VAL 732  732  ?    ?   ?   A . n 
A 1 733  LEU 733  733  ?    ?   ?   A . n 
A 1 734  LYS 734  734  ?    ?   ?   A . n 
A 1 735  LEU 735  735  ?    ?   ?   A . n 
A 1 736  LYS 736  736  ?    ?   ?   A . n 
A 1 737  VAL 737  737  ?    ?   ?   A . n 
A 1 738  ASN 738  738  ?    ?   ?   A . n 
A 1 739  PHE 739  739  ?    ?   ?   A . n 
A 1 740  LEU 740  740  ?    ?   ?   A . n 
A 1 741  PRO 741  741  ?    ?   ?   A . n 
A 1 742  GLU 742  742  ?    ?   ?   A . n 
A 1 743  ILE 743  743  ?    ?   ?   A . n 
A 1 744  ILE 744  744  ?    ?   ?   A . n 
A 1 745  THR 745  745  ?    ?   ?   A . n 
A 1 746  LEU 746  746  ?    ?   ?   A . n 
A 1 747  SER 747  747  ?    ?   ?   A . n 
A 1 748  LYS 748  748  ?    ?   ?   A . n 
A 1 749  GLU 749  749  ?    ?   ?   A . n 
A 1 750  VAL 750  750  ?    ?   ?   A . n 
A 1 751  ARG 751  751  ?    ?   ?   A . n 
A 1 752  ASN 752  752  ?    ?   ?   A . n 
A 1 753  LEU 753  753  ?    ?   ?   A . n 
A 1 754  LYS 754  754  ?    ?   ?   A . n 
A 1 755  TRP 755  755  ?    ?   ?   A . n 
A 1 756  LEU 756  756  ?    ?   ?   A . n 
A 1 757  GLY 757  757  ?    ?   ?   A . n 
A 1 758  PHE 758  758  ?    ?   ?   A . n 
A 1 759  ARG 759  759  ?    ?   ?   A . n 
A 1 760  VAL 760  760  ?    ?   ?   A . n 
A 1 761  PRO 761  761  ?    ?   ?   A . n 
A 1 762  LEU 762  762  ?    ?   ?   A . n 
A 1 763  ALA 763  763  ?    ?   ?   A . n 
A 1 764  ILE 764  764  ?    ?   ?   A . n 
A 1 765  VAL 765  765  ?    ?   ?   A . n 
A 1 766  ASN 766  766  ?    ?   ?   A . n 
A 1 767  LYS 767  767  ?    ?   ?   A . n 
A 1 768  ALA 768  768  ?    ?   ?   A . n 
A 1 769  HIS 769  769  ?    ?   ?   A . n 
A 1 770  GLN 770  770  ?    ?   ?   A . n 
A 1 771  ALA 771  771  ?    ?   ?   A . n 
A 1 772  ASN 772  772  ?    ?   ?   A . n 
A 1 773  GLN 773  773  ?    ?   ?   A . n 
A 1 774  LEU 774  774  ?    ?   ?   A . n 
A 1 775  TYR 775  775  ?    ?   ?   A . n 
A 1 776  PRO 776  776  ?    ?   ?   A . n 
A 1 777  PHE 777  777  ?    ?   ?   A . n 
A 1 778  ALA 778  778  ?    ?   ?   A . n 
A 1 779  ILE 779  779  ?    ?   ?   A . n 
A 1 780  SER 780  780  ?    ?   ?   A . n 
A 1 781  LEU 781  781  ?    ?   ?   A . n 
A 1 782  ILE 782  782  ?    ?   ?   A . n 
A 1 783  GLU 783  783  ?    ?   ?   A . n 
A 1 784  SER 784  784  ?    ?   ?   A . n 
A 1 785  VAL 785  785  ?    ?   ?   A . n 
A 1 786  ARG 786  786  ?    ?   ?   A . n 
A 1 787  THR 787  787  ?    ?   ?   A . n 
A 1 788  TYR 788  788  ?    ?   ?   A . n 
A 1 789  GLU 789  789  ?    ?   ?   A . n 
A 1 790  ARG 790  790  ?    ?   ?   A . n 
A 1 791  THR 791  791  ?    ?   ?   A . n 
A 1 792  CYS 792  792  ?    ?   ?   A . n 
A 1 793  GLU 793  793  ?    ?   ?   A . n 
A 1 794  LYS 794  794  ?    ?   ?   A . n 
A 1 795  VAL 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLU 797  797  ?    ?   ?   A . n 
A 1 798  ARG 798  798  ?    ?   ?   A . n 
A 1 799  ASN 799  799  ?    ?   ?   A . n 
A 1 800  THR 800  800  ?    ?   ?   A . n 
A 1 801  ILE 801  801  ?    ?   ?   A . n 
A 1 802  SER 802  802  ?    ?   ?   A . n 
A 1 803  LEU 803  803  ?    ?   ?   A . n 
A 1 804  LEU 804  804  ?    ?   ?   A . n 
A 1 805  VAL 805  805  ?    ?   ?   A . n 
A 1 806  ALA 806  806  ?    ?   ?   A . n 
A 1 807  GLY 807  807  ?    ?   ?   A . n 
A 1 808  LEU 808  808  ?    ?   ?   A . n 
A 1 809  LYS 809  809  ?    ?   ?   A . n 
A 1 810  LYS 810  810  ?    ?   ?   A . n 
A 1 811  GLU 811  811  ?    ?   ?   A . n 
A 1 812  VAL 812  812  ?    ?   ?   A . n 
A 1 813  GLN 813  813  ?    ?   ?   A . n 
A 1 814  ALA 814  814  ?    ?   ?   A . n 
A 1 815  LEU 815  815  ?    ?   ?   A . n 
A 1 816  ILE 816  816  ?    ?   ?   A . n 
A 1 817  ALA 817  817  ?    ?   ?   A . n 
A 1 818  GLU 818  818  ?    ?   ?   A . n 
A 1 819  GLY 819  819  ?    ?   ?   A . n 
A 1 820  ILE 820  820  ?    ?   ?   A . n 
A 1 821  ALA 821  821  ?    ?   ?   A . n 
A 1 822  LEU 822  822  ?    ?   ?   A . n 
A 1 823  VAL 823  823  ?    ?   ?   A . n 
A 1 824  TRP 824  824  ?    ?   ?   A . n 
A 1 825  GLU 825  825  ?    ?   ?   A . n 
A 1 826  SER 826  826  ?    ?   ?   A . n 
A 1 827  TYR 827  827  ?    ?   ?   A . n 
A 1 828  LYS 828  828  ?    ?   ?   A . n 
A 1 829  LEU 829  829  ?    ?   ?   A . n 
A 1 830  ASP 830  830  ?    ?   ?   A . n 
A 1 831  PRO 831  831  ?    ?   ?   A . n 
A 1 832  TYR 832  832  ?    ?   ?   A . n 
A 1 833  VAL 833  833  ?    ?   ?   A . n 
A 1 834  GLN 834  834  ?    ?   ?   A . n 
A 1 835  ARG 835  835  ?    ?   ?   A . n 
A 1 836  LEU 836  836  ?    ?   ?   A . n 
A 1 837  ALA 837  837  ?    ?   ?   A . n 
A 1 838  GLU 838  838  ?    ?   ?   A . n 
A 1 839  THR 839  839  ?    ?   ?   A . n 
A 1 840  VAL 840  840  ?    ?   ?   A . n 
A 1 841  PHE 841  841  ?    ?   ?   A . n 
A 1 842  ASN 842  842  ?    ?   ?   A . n 
A 1 843  PHE 843  843  ?    ?   ?   A . n 
A 1 844  GLN 844  844  ?    ?   ?   A . n 
A 1 845  GLU 845  845  ?    ?   ?   A . n 
A 1 846  LYS 846  846  ?    ?   ?   A . n 
A 1 847  VAL 847  847  ?    ?   ?   A . n 
A 1 848  ASP 848  848  ?    ?   ?   A . n 
A 1 849  ASP 849  849  ?    ?   ?   A . n 
A 1 850  LEU 850  850  ?    ?   ?   A . n 
A 1 851  LEU 851  851  ?    ?   ?   A . n 
A 1 852  ILE 852  852  ?    ?   ?   A . n 
A 1 853  ILE 853  853  ?    ?   ?   A . n 
A 1 854  GLU 854  854  ?    ?   ?   A . n 
A 1 855  GLU 855  855  ?    ?   ?   A . n 
A 1 856  LYS 856  856  ?    ?   ?   A . n 
A 1 857  ILE 857  857  ?    ?   ?   A . n 
A 1 858  ASP 858  858  ?    ?   ?   A . n 
A 1 859  LEU 859  859  ?    ?   ?   A . n 
A 1 860  GLU 860  860  ?    ?   ?   A . n 
A 1 861  VAL 861  861  ?    ?   ?   A . n 
A 1 862  ARG 862  862  ?    ?   ?   A . n 
A 1 863  SER 863  863  ?    ?   ?   A . n 
A 1 864  LEU 864  864  ?    ?   ?   A . n 
A 1 865  GLU 865  865  ?    ?   ?   A . n 
A 1 866  THR 866  866  ?    ?   ?   A . n 
A 1 867  CYS 867  867  ?    ?   ?   A . n 
A 1 868  MET 868  868  ?    ?   ?   A . n 
A 1 869  TYR 869  869  ?    ?   ?   A . n 
A 1 870  ASP 870  870  ?    ?   ?   A . n 
A 1 871  HIS 871  871  ?    ?   ?   A . n 
A 1 872  LYS 872  872  ?    ?   ?   A . n 
A 1 873  THR 873  873  ?    ?   ?   A . n 
A 1 874  PHE 874  874  ?    ?   ?   A . n 
A 1 875  SER 875  875  ?    ?   ?   A . n 
A 1 876  GLU 876  876  ?    ?   ?   A . n 
A 1 877  ILE 877  877  ?    ?   ?   A . n 
A 1 878  LEU 878  878  ?    ?   ?   A . n 
A 1 879  ASN 879  879  ?    ?   ?   A . n 
A 1 880  ARG 880  880  ?    ?   ?   A . n 
A 1 881  VAL 881  881  ?    ?   ?   A . n 
A 1 882  GLN 882  882  ?    ?   ?   A . n 
A 1 883  LYS 883  883  ?    ?   ?   A . n 
A 1 884  ALA 884  884  ?    ?   ?   A . n 
A 1 885  VAL 885  885  ?    ?   ?   A . n 
A 1 886  ASP 886  886  ?    ?   ?   A . n 
A 1 887  ASP 887  887  ?    ?   ?   A . n 
A 1 888  LEU 888  888  ?    ?   ?   A . n 
A 1 889  ASN 889  889  ?    ?   ?   A . n 
A 1 890  LEU 890  890  ?    ?   ?   A . n 
A 1 891  HIS 891  891  ?    ?   ?   A . n 
A 1 892  SER 892  892  ?    ?   ?   A . n 
A 1 893  TYR 893  893  ?    ?   ?   A . n 
A 1 894  SER 894  894  ?    ?   ?   A . n 
A 1 895  ASN 895  895  ?    ?   ?   A . n 
A 1 896  LEU 896  896  ?    ?   ?   A . n 
A 1 897  PRO 897  897  ?    ?   ?   A . n 
A 1 898  ILE 898  898  ?    ?   ?   A . n 
A 1 899  TRP 899  899  ?    ?   ?   A . n 
A 1 900  VAL 900  900  ?    ?   ?   A . n 
A 1 901  ASN 901  901  ?    ?   ?   A . n 
A 1 902  LYS 902  902  ?    ?   ?   A . n 
A 1 903  LEU 903  903  ?    ?   ?   A . n 
A 1 904  ASP 904  904  ?    ?   ?   A . n 
A 1 905  MET 905  905  ?    ?   ?   A . n 
A 1 906  GLU 906  906  ?    ?   ?   A . n 
A 1 907  ILE 907  907  ?    ?   ?   A . n 
A 1 908  GLU 908  908  ?    ?   ?   A . n 
A 1 909  ARG 909  909  ?    ?   ?   A . n 
A 1 910  ILE 910  910  ?    ?   ?   A . n 
A 1 911  LEU 911  911  ?    ?   ?   A . n 
A 1 912  GLY 912  912  ?    ?   ?   A . n 
A 1 913  VAL 913  913  ?    ?   ?   A . n 
A 1 914  ARG 914  914  ?    ?   ?   A . n 
A 1 915  LEU 915  915  ?    ?   ?   A . n 
A 1 916  GLN 916  916  ?    ?   ?   A . n 
A 1 917  ALA 917  917  ?    ?   ?   A . n 
A 1 918  GLY 918  918  ?    ?   ?   A . n 
A 1 919  LEU 919  919  ?    ?   ?   A . n 
A 1 920  ARG 920  920  ?    ?   ?   A . n 
A 1 921  ALA 921  921  ?    ?   ?   A . n 
A 1 922  TRP 922  922  ?    ?   ?   A . n 
A 1 923  THR 923  923  ?    ?   ?   A . n 
A 1 924  GLN 924  924  ?    ?   ?   A . n 
A 1 925  VAL 925  925  ?    ?   ?   A . n 
A 1 926  LEU 926  926  ?    ?   ?   A . n 
A 1 927  LEU 927  927  ?    ?   ?   A . n 
A 1 928  GLY 928  928  ?    ?   ?   A . n 
A 1 929  GLN 929  929  ?    ?   ?   A . n 
A 1 930  ALA 930  930  ?    ?   ?   A . n 
A 1 931  GLU 931  931  ?    ?   ?   A . n 
A 1 932  ASP 932  932  ?    ?   ?   A . n 
A 1 933  LYS 933  933  ?    ?   ?   A . n 
A 1 934  ALA 934  934  ?    ?   ?   A . n 
A 1 935  GLU 935  935  ?    ?   ?   A . n 
A 1 936  VAL 936  936  ?    ?   ?   A . n 
A 1 937  ASP 937  937  ?    ?   ?   A . n 
A 1 938  MET 938  938  ?    ?   ?   A . n 
A 1 939  ASP 939  939  ?    ?   ?   A . n 
A 1 940  THR 940  940  ?    ?   ?   A . n 
A 1 941  ASP 941  941  ?    ?   ?   A . n 
A 1 942  ALA 942  942  ?    ?   ?   A . n 
A 1 943  PRO 943  943  ?    ?   ?   A . n 
A 1 944  GLN 944  944  ?    ?   ?   A . n 
A 1 945  VAL 945  945  ?    ?   ?   A . n 
A 1 946  SER 946  946  ?    ?   ?   A . n 
A 1 947  HIS 947  947  ?    ?   ?   A . n 
A 1 948  LYS 948  948  ?    ?   ?   A . n 
A 1 949  PRO 949  949  ?    ?   ?   A . n 
A 1 950  GLY 950  950  ?    ?   ?   A . n 
A 1 951  GLY 951  951  ?    ?   ?   A . n 
A 1 952  GLU 952  952  ?    ?   ?   A . n 
A 1 953  PRO 953  953  ?    ?   ?   A . n 
A 1 954  LYS 954  954  ?    ?   ?   A . n 
A 1 955  ILE 955  955  ?    ?   ?   A . n 
A 1 956  LYS 956  956  ?    ?   ?   A . n 
A 1 957  ASN 957  957  ?    ?   ?   A . n 
A 1 958  VAL 958  958  ?    ?   ?   A . n 
A 1 959  VAL 959  959  ?    ?   ?   A . n 
A 1 960  HIS 960  960  ?    ?   ?   A . n 
A 1 961  GLU 961  961  ?    ?   ?   A . n 
A 1 962  LEU 962  962  ?    ?   ?   A . n 
A 1 963  ARG 963  963  ?    ?   ?   A . n 
A 1 964  ILE 964  964  ?    ?   ?   A . n 
A 1 965  THR 965  965  ?    ?   ?   A . n 
A 1 966  ASN 966  966  ?    ?   ?   A . n 
A 1 967  GLN 967  967  ?    ?   ?   A . n 
A 1 968  VAL 968  968  ?    ?   ?   A . n 
A 1 969  ILE 969  969  ?    ?   ?   A . n 
A 1 970  TYR 970  970  ?    ?   ?   A . n 
A 1 971  LEU 971  971  ?    ?   ?   A . n 
A 1 972  ASN 972  972  ?    ?   ?   A . n 
A 1 973  PRO 973  973  ?    ?   ?   A . n 
A 1 974  PRO 974  974  ?    ?   ?   A . n 
A 1 975  ILE 975  975  ?    ?   ?   A . n 
A 1 976  GLU 976  976  ?    ?   ?   A . n 
A 1 977  GLU 977  977  ?    ?   ?   A . n 
A 1 978  CYS 978  978  ?    ?   ?   A . n 
A 1 979  ARG 979  979  ?    ?   ?   A . n 
A 1 980  TYR 980  980  ?    ?   ?   A . n 
A 1 981  LYS 981  981  ?    ?   ?   A . n 
A 1 982  LEU 982  982  ?    ?   ?   A . n 
A 1 983  TYR 983  983  ?    ?   ?   A . n 
A 1 984  GLN 984  984  ?    ?   ?   A . n 
A 1 985  GLU 985  985  ?    ?   ?   A . n 
A 1 986  MET 986  986  ?    ?   ?   A . n 
A 1 987  PHE 987  987  ?    ?   ?   A . n 
A 1 988  ALA 988  988  ?    ?   ?   A . n 
A 1 989  TRP 989  989  ?    ?   ?   A . n 
A 1 990  LYS 990  990  ?    ?   ?   A . n 
A 1 991  MET 991  991  ?    ?   ?   A . n 
A 1 992  VAL 992  992  ?    ?   ?   A . n 
A 1 993  VAL 993  993  ?    ?   ?   A . n 
A 1 994  LEU 994  994  ?    ?   ?   A . n 
A 1 995  SER 995  995  ?    ?   ?   A . n 
A 1 996  LEU 996  996  ?    ?   ?   A . n 
A 1 997  PRO 997  997  ?    ?   ?   A . n 
A 1 998  ARG 998  998  ?    ?   ?   A . n 
A 1 999  ILE 999  999  ?    ?   ?   A . n 
A 1 1000 GLN 1000 1000 ?    ?   ?   A . n 
A 1 1001 SER 1001 1001 ?    ?   ?   A . n 
A 1 1002 GLN 1002 1002 ?    ?   ?   A . n 
A 1 1003 ARG 1003 1003 ?    ?   ?   A . n 
A 1 1004 TYR 1004 1004 ?    ?   ?   A . n 
A 1 1005 GLN 1005 1005 ?    ?   ?   A . n 
A 1 1006 VAL 1006 1006 ?    ?   ?   A . n 
A 1 1007 GLY 1007 1007 ?    ?   ?   A . n 
A 1 1008 VAL 1008 1008 ?    ?   ?   A . n 
A 1 1009 HIS 1009 1009 ?    ?   ?   A . n 
A 1 1010 TYR 1010 1010 ?    ?   ?   A . n 
A 1 1011 GLU 1011 1011 ?    ?   ?   A . n 
A 1 1012 LEU 1012 1012 ?    ?   ?   A . n 
A 1 1013 THR 1013 1013 ?    ?   ?   A . n 
A 1 1014 GLU 1014 1014 ?    ?   ?   A . n 
A 1 1015 GLU 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLU 1016 1016 ?    ?   ?   A . n 
A 1 1017 LYS 1017 1017 ?    ?   ?   A . n 
A 1 1018 PHE 1018 1018 ?    ?   ?   A . n 
A 1 1019 TYR 1019 1019 ?    ?   ?   A . n 
A 1 1020 ARG 1020 1020 ?    ?   ?   A . n 
A 1 1021 ASN 1021 1021 ?    ?   ?   A . n 
A 1 1022 ALA 1022 1022 ?    ?   ?   A . n 
A 1 1023 LEU 1023 1023 ?    ?   ?   A . n 
A 1 1024 THR 1024 1024 ?    ?   ?   A . n 
A 1 1025 ARG 1025 1025 ?    ?   ?   A . n 
A 1 1026 MET 1026 1026 ?    ?   ?   A . n 
A 1 1027 PRO 1027 1027 ?    ?   ?   A . n 
A 1 1028 ASP 1028 1028 ?    ?   ?   A . n 
A 1 1029 GLY 1029 1029 ?    ?   ?   A . n 
A 1 1030 PRO 1030 1030 ?    ?   ?   A . n 
A 1 1031 VAL 1031 1031 ?    ?   ?   A . n 
A 1 1032 ALA 1032 1032 ?    ?   ?   A . n 
A 1 1033 LEU 1033 1033 ?    ?   ?   A . n 
A 1 1034 GLU 1034 1034 ?    ?   ?   A . n 
A 1 1035 GLU 1035 1035 ?    ?   ?   A . n 
A 1 1036 SER 1036 1036 ?    ?   ?   A . n 
A 1 1037 TYR 1037 1037 ?    ?   ?   A . n 
A 1 1038 SER 1038 1038 ?    ?   ?   A . n 
A 1 1039 ALA 1039 1039 ?    ?   ?   A . n 
A 1 1040 VAL 1040 1040 ?    ?   ?   A . n 
A 1 1041 MET 1041 1041 ?    ?   ?   A . n 
A 1 1042 GLY 1042 1042 ?    ?   ?   A . n 
A 1 1043 ILE 1043 1043 ?    ?   ?   A . n 
A 1 1044 VAL 1044 1044 ?    ?   ?   A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   A . n 
A 1 1046 GLU 1046 1046 ?    ?   ?   A . n 
A 1 1047 VAL 1047 1047 ?    ?   ?   A . n 
A 1 1048 GLU 1048 1048 ?    ?   ?   A . n 
A 1 1049 GLN 1049 1049 ?    ?   ?   A . n 
A 1 1050 TYR 1050 1050 ?    ?   ?   A . n 
A 1 1051 VAL 1051 1051 ?    ?   ?   A . n 
A 1 1052 LYS 1052 1052 ?    ?   ?   A . n 
A 1 1053 VAL 1053 1053 ?    ?   ?   A . n 
A 1 1054 TRP 1054 1054 ?    ?   ?   A . n 
A 1 1055 LEU 1055 1055 ?    ?   ?   A . n 
A 1 1056 GLN 1056 1056 ?    ?   ?   A . n 
A 1 1057 TYR 1057 1057 ?    ?   ?   A . n 
A 1 1058 GLN 1058 1058 ?    ?   ?   A . n 
A 1 1059 CYS 1059 1059 ?    ?   ?   A . n 
A 1 1060 LEU 1060 1060 ?    ?   ?   A . n 
A 1 1061 TRP 1061 1061 ?    ?   ?   A . n 
A 1 1062 ASP 1062 1062 ?    ?   ?   A . n 
A 1 1063 MET 1063 1063 ?    ?   ?   A . n 
A 1 1064 GLN 1064 1064 ?    ?   ?   A . n 
A 1 1065 ALA 1065 1065 ?    ?   ?   A . n 
A 1 1066 GLU 1066 1066 ?    ?   ?   A . n 
A 1 1067 ASN 1067 1067 ?    ?   ?   A . n 
A 1 1068 ILE 1068 1068 ?    ?   ?   A . n 
A 1 1069 TYR 1069 1069 ?    ?   ?   A . n 
A 1 1070 ASN 1070 1070 ?    ?   ?   A . n 
A 1 1071 ARG 1071 1071 ?    ?   ?   A . n 
A 1 1072 LEU 1072 1072 ?    ?   ?   A . n 
A 1 1073 GLY 1073 1073 ?    ?   ?   A . n 
A 1 1074 GLU 1074 1074 ?    ?   ?   A . n 
A 1 1075 ASP 1075 1075 ?    ?   ?   A . n 
A 1 1076 LEU 1076 1076 ?    ?   ?   A . n 
A 1 1077 ASN 1077 1077 ?    ?   ?   A . n 
A 1 1078 LYS 1078 1078 ?    ?   ?   A . n 
A 1 1079 TRP 1079 1079 ?    ?   ?   A . n 
A 1 1080 GLN 1080 1080 ?    ?   ?   A . n 
A 1 1081 ALA 1081 1081 ?    ?   ?   A . n 
A 1 1082 LEU 1082 1082 ?    ?   ?   A . n 
A 1 1083 LEU 1083 1083 ?    ?   ?   A . n 
A 1 1084 VAL 1084 1084 ?    ?   ?   A . n 
A 1 1085 GLN 1085 1085 ?    ?   ?   A . n 
A 1 1086 ILE 1086 1086 ?    ?   ?   A . n 
A 1 1087 ARG 1087 1087 ?    ?   ?   A . n 
A 1 1088 LYS 1088 1088 ?    ?   ?   A . n 
A 1 1089 ALA 1089 1089 ?    ?   ?   A . n 
A 1 1090 ARG 1090 1090 ?    ?   ?   A . n 
A 1 1091 GLY 1091 1091 ?    ?   ?   A . n 
A 1 1092 THR 1092 1092 ?    ?   ?   A . n 
A 1 1093 PHE 1093 1093 ?    ?   ?   A . n 
A 1 1094 ASP 1094 1094 ?    ?   ?   A . n 
A 1 1095 ASN 1095 1095 ?    ?   ?   A . n 
A 1 1096 ALA 1096 1096 ?    ?   ?   A . n 
A 1 1097 GLU 1097 1097 ?    ?   ?   A . n 
A 1 1098 THR 1098 1098 ?    ?   ?   A . n 
A 1 1099 LYS 1099 1099 ?    ?   ?   A . n 
A 1 1100 LYS 1100 1100 ?    ?   ?   A . n 
A 1 1101 GLU 1101 1101 ?    ?   ?   A . n 
A 1 1102 PHE 1102 1102 ?    ?   ?   A . n 
A 1 1103 GLY 1103 1103 ?    ?   ?   A . n 
A 1 1104 PRO 1104 1104 ?    ?   ?   A . n 
A 1 1105 VAL 1105 1105 ?    ?   ?   A . n 
A 1 1106 VAL 1106 1106 ?    ?   ?   A . n 
A 1 1107 ILE 1107 1107 ?    ?   ?   A . n 
A 1 1108 ASP 1108 1108 ?    ?   ?   A . n 
A 1 1109 TYR 1109 1109 ?    ?   ?   A . n 
A 1 1110 GLY 1110 1110 ?    ?   ?   A . n 
A 1 1111 LYS 1111 1111 ?    ?   ?   A . n 
A 1 1112 VAL 1112 1112 ?    ?   ?   A . n 
A 1 1113 GLN 1113 1113 ?    ?   ?   A . n 
A 1 1114 SER 1114 1114 ?    ?   ?   A . n 
A 1 1115 LYS 1115 1115 ?    ?   ?   A . n 
A 1 1116 VAL 1116 1116 ?    ?   ?   A . n 
A 1 1117 ASN 1117 1117 ?    ?   ?   A . n 
A 1 1118 LEU 1118 1118 ?    ?   ?   A . n 
A 1 1119 LYS 1119 1119 ?    ?   ?   A . n 
A 1 1120 TYR 1120 1120 ?    ?   ?   A . n 
A 1 1121 ASP 1121 1121 ?    ?   ?   A . n 
A 1 1122 SER 1122 1122 ?    ?   ?   A . n 
A 1 1123 TRP 1123 1123 ?    ?   ?   A . n 
A 1 1124 HIS 1124 1124 ?    ?   ?   A . n 
A 1 1125 LYS 1125 1125 ?    ?   ?   A . n 
A 1 1126 GLU 1126 1126 ?    ?   ?   A . n 
A 1 1127 VAL 1127 1127 ?    ?   ?   A . n 
A 1 1128 LEU 1128 1128 ?    ?   ?   A . n 
A 1 1129 SER 1129 1129 ?    ?   ?   A . n 
A 1 1130 LYS 1130 1130 ?    ?   ?   A . n 
A 1 1131 PHE 1131 1131 ?    ?   ?   A . n 
A 1 1132 GLY 1132 1132 ?    ?   ?   A . n 
A 1 1133 GLN 1133 1133 ?    ?   ?   A . n 
A 1 1134 MET 1134 1134 ?    ?   ?   A . n 
A 1 1135 LEU 1135 1135 ?    ?   ?   A . n 
A 1 1136 GLY 1136 1136 ?    ?   ?   A . n 
A 1 1137 SER 1137 1137 ?    ?   ?   A . n 
A 1 1138 ASN 1138 1138 ?    ?   ?   A . n 
A 1 1139 MET 1139 1139 ?    ?   ?   A . n 
A 1 1140 THR 1140 1140 ?    ?   ?   A . n 
A 1 1141 GLU 1141 1141 ?    ?   ?   A . n 
A 1 1142 PHE 1142 1142 ?    ?   ?   A . n 
A 1 1143 HIS 1143 1143 ?    ?   ?   A . n 
A 1 1144 SER 1144 1144 ?    ?   ?   A . n 
A 1 1145 GLN 1145 1145 ?    ?   ?   A . n 
A 1 1146 ILE 1146 1146 ?    ?   ?   A . n 
A 1 1147 SER 1147 1147 ?    ?   ?   A . n 
A 1 1148 LYS 1148 1148 ?    ?   ?   A . n 
A 1 1149 SER 1149 1149 ?    ?   ?   A . n 
A 1 1150 ARG 1150 1150 ?    ?   ?   A . n 
A 1 1151 GLN 1151 1151 ?    ?   ?   A . n 
A 1 1152 GLU 1152 1152 ?    ?   ?   A . n 
A 1 1153 LEU 1153 1153 ?    ?   ?   A . n 
A 1 1154 GLU 1154 1154 ?    ?   ?   A . n 
A 1 1155 GLN 1155 1155 ?    ?   ?   A . n 
A 1 1156 HIS 1156 1156 ?    ?   ?   A . n 
A 1 1157 SER 1157 1157 ?    ?   ?   A . n 
A 1 1158 VAL 1158 1158 ?    ?   ?   A . n 
A 1 1159 ASP 1159 1159 ?    ?   ?   A . n 
A 1 1160 THR 1160 1160 ?    ?   ?   A . n 
A 1 1161 ALA 1161 1161 ?    ?   ?   A . n 
A 1 1162 SER 1162 1162 ?    ?   ?   A . n 
A 1 1163 THR 1163 1163 ?    ?   ?   A . n 
A 1 1164 SER 1164 1164 ?    ?   ?   A . n 
A 1 1165 ASP 1165 1165 ?    ?   ?   A . n 
A 1 1166 ALA 1166 1166 ?    ?   ?   A . n 
A 1 1167 VAL 1167 1167 ?    ?   ?   A . n 
A 1 1168 THR 1168 1168 ?    ?   ?   A . n 
A 1 1169 PHE 1169 1169 ?    ?   ?   A . n 
A 1 1170 ILE 1170 1170 ?    ?   ?   A . n 
A 1 1171 THR 1171 1171 ?    ?   ?   A . n 
A 1 1172 TYR 1172 1172 ?    ?   ?   A . n 
A 1 1173 VAL 1173 1173 ?    ?   ?   A . n 
A 1 1174 GLN 1174 1174 ?    ?   ?   A . n 
A 1 1175 SER 1175 1175 ?    ?   ?   A . n 
A 1 1176 LEU 1176 1176 ?    ?   ?   A . n 
A 1 1177 LYS 1177 1177 ?    ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?    ?   ?   A . n 
A 1 1179 LYS 1179 1179 ?    ?   ?   A . n 
A 1 1180 ILE 1180 1180 ?    ?   ?   A . n 
A 1 1181 LYS 1181 1181 ?    ?   ?   A . n 
A 1 1182 GLN 1182 1182 ?    ?   ?   A . n 
A 1 1183 PHE 1183 1183 ?    ?   ?   A . n 
A 1 1184 GLU 1184 1184 ?    ?   ?   A . n 
A 1 1185 LYS 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLN 1186 1186 ?    ?   ?   A . n 
A 1 1187 VAL 1187 1187 ?    ?   ?   A . n 
A 1 1188 GLU 1188 1188 ?    ?   ?   A . n 
A 1 1189 LEU 1189 1189 ?    ?   ?   A . n 
A 1 1190 TYR 1190 1190 ?    ?   ?   A . n 
A 1 1191 ARG 1191 1191 ?    ?   ?   A . n 
A 1 1192 ASN 1192 1192 ?    ?   ?   A . n 
A 1 1193 GLY 1193 1193 ?    ?   ?   A . n 
A 1 1194 GLN 1194 1194 ?    ?   ?   A . n 
A 1 1195 ARG 1195 1195 ?    ?   ?   A . n 
A 1 1196 LEU 1196 1196 ?    ?   ?   A . n 
A 1 1197 LEU 1197 1197 ?    ?   ?   A . n 
A 1 1198 GLU 1198 1198 ?    ?   ?   A . n 
A 1 1199 LYS 1199 1199 ?    ?   ?   A . n 
A 1 1200 GLN 1200 1200 ?    ?   ?   A . n 
A 1 1201 ARG 1201 1201 ?    ?   ?   A . n 
A 1 1202 PHE 1202 1202 ?    ?   ?   A . n 
A 1 1203 GLN 1203 1203 ?    ?   ?   A . n 
A 1 1204 PHE 1204 1204 ?    ?   ?   A . n 
A 1 1205 PRO 1205 1205 ?    ?   ?   A . n 
A 1 1206 PRO 1206 1206 ?    ?   ?   A . n 
A 1 1207 SER 1207 1207 ?    ?   ?   A . n 
A 1 1208 TRP 1208 1208 ?    ?   ?   A . n 
A 1 1209 LEU 1209 1209 ?    ?   ?   A . n 
A 1 1210 TYR 1210 1210 ?    ?   ?   A . n 
A 1 1211 ILE 1211 1211 ?    ?   ?   A . n 
A 1 1212 ASP 1212 1212 ?    ?   ?   A . n 
A 1 1213 ASN 1213 1213 ?    ?   ?   A . n 
A 1 1214 ILE 1214 1214 ?    ?   ?   A . n 
A 1 1215 GLU 1215 1215 ?    ?   ?   A . n 
A 1 1216 GLY 1216 1216 ?    ?   ?   A . n 
A 1 1217 GLU 1217 1217 ?    ?   ?   A . n 
A 1 1218 TRP 1218 1218 ?    ?   ?   A . n 
A 1 1219 GLY 1219 1219 ?    ?   ?   A . n 
A 1 1220 ALA 1220 1220 ?    ?   ?   A . n 
A 1 1221 PHE 1221 1221 ?    ?   ?   A . n 
A 1 1222 ASN 1222 1222 ?    ?   ?   A . n 
A 1 1223 ASP 1223 1223 ?    ?   ?   A . n 
A 1 1224 ILE 1224 1224 ?    ?   ?   A . n 
A 1 1225 MET 1225 1225 ?    ?   ?   A . n 
A 1 1226 ARG 1226 1226 ?    ?   ?   A . n 
A 1 1227 ARG 1227 1227 ?    ?   ?   A . n 
A 1 1228 LYS 1228 1228 ?    ?   ?   A . n 
A 1 1229 ASP 1229 1229 ?    ?   ?   A . n 
A 1 1230 SER 1230 1230 ?    ?   ?   A . n 
A 1 1231 ALA 1231 1231 ?    ?   ?   A . n 
A 1 1232 ILE 1232 1232 ?    ?   ?   A . n 
A 1 1233 GLN 1233 1233 ?    ?   ?   A . n 
A 1 1234 GLN 1234 1234 ?    ?   ?   A . n 
A 1 1235 GLN 1235 1235 ?    ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?    ?   ?   A . n 
A 1 1237 ALA 1237 1237 ?    ?   ?   A . n 
A 1 1238 ASN 1238 1238 ?    ?   ?   A . n 
A 1 1239 LEU 1239 1239 ?    ?   ?   A . n 
A 1 1240 GLN 1240 1240 ?    ?   ?   A . n 
A 1 1241 MET 1241 1241 ?    ?   ?   A . n 
A 1 1242 LYS 1242 1242 ?    ?   ?   A . n 
A 1 1243 ILE 1243 1243 ?    ?   ?   A . n 
A 1 1244 VAL 1244 1244 ?    ?   ?   A . n 
A 1 1245 GLN 1245 1245 ?    ?   ?   A . n 
A 1 1246 GLU 1246 1246 ?    ?   ?   A . n 
A 1 1247 ASP 1247 1247 ?    ?   ?   A . n 
A 1 1248 ARG 1248 1248 ?    ?   ?   A . n 
A 1 1249 ALA 1249 1249 ?    ?   ?   A . n 
A 1 1250 VAL 1250 1250 ?    ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?    ?   ?   A . n 
A 1 1252 SER 1252 1252 ?    ?   ?   A . n 
A 1 1253 ARG 1253 1253 ?    ?   ?   A . n 
A 1 1254 THR 1254 1254 ?    ?   ?   A . n 
A 1 1255 THR 1255 1255 ?    ?   ?   A . n 
A 1 1256 ASP 1256 1256 ?    ?   ?   A . n 
A 1 1257 LEU 1257 1257 ?    ?   ?   A . n 
A 1 1258 LEU 1258 1258 ?    ?   ?   A . n 
A 1 1259 THR 1259 1259 ?    ?   ?   A . n 
A 1 1260 ASP 1260 1260 ?    ?   ?   A . n 
A 1 1261 TRP 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLU 1262 1262 ?    ?   ?   A . n 
A 1 1263 LYS 1263 1263 ?    ?   ?   A . n 
A 1 1264 THR 1264 1264 ?    ?   ?   A . n 
A 1 1265 LYS 1265 1265 ?    ?   ?   A . n 
A 1 1266 PRO 1266 1266 ?    ?   ?   A . n 
A 1 1267 VAL 1267 1267 ?    ?   ?   A . n 
A 1 1268 THR 1268 1268 ?    ?   ?   A . n 
A 1 1269 GLY 1269 1269 ?    ?   ?   A . n 
A 1 1270 ASN 1270 1270 ?    ?   ?   A . n 
A 1 1271 LEU 1271 1271 ?    ?   ?   A . n 
A 1 1272 ARG 1272 1272 ?    ?   ?   A . n 
A 1 1273 PRO 1273 1273 ?    ?   ?   A . n 
A 1 1274 GLU 1274 1274 ?    ?   ?   A . n 
A 1 1275 GLU 1275 1275 ?    ?   ?   A . n 
A 1 1276 ALA 1276 1276 ?    ?   ?   A . n 
A 1 1277 LEU 1277 1277 ?    ?   ?   A . n 
A 1 1278 GLN 1278 1278 ?    ?   ?   A . n 
A 1 1279 ALA 1279 1279 ?    ?   ?   A . n 
A 1 1280 LEU 1280 1280 ?    ?   ?   A . n 
A 1 1281 THR 1281 1281 ?    ?   ?   A . n 
A 1 1282 ILE 1282 1282 ?    ?   ?   A . n 
A 1 1283 TYR 1283 1283 ?    ?   ?   A . n 
A 1 1284 GLU 1284 1284 ?    ?   ?   A . n 
A 1 1285 GLY 1285 1285 ?    ?   ?   A . n 
A 1 1286 LYS 1286 1286 ?    ?   ?   A . n 
A 1 1287 PHE 1287 1287 ?    ?   ?   A . n 
A 1 1288 GLY 1288 1288 ?    ?   ?   A . n 
A 1 1289 ARG 1289 1289 ?    ?   ?   A . n 
A 1 1290 LEU 1290 1290 ?    ?   ?   A . n 
A 1 1291 LYS 1291 1291 ?    ?   ?   A . n 
A 1 1292 ASP 1292 1292 ?    ?   ?   A . n 
A 1 1293 ASP 1293 1293 ?    ?   ?   A . n 
A 1 1294 ARG 1294 1294 ?    ?   ?   A . n 
A 1 1295 GLU 1295 1295 ?    ?   ?   A . n 
A 1 1296 LYS 1296 1296 ?    ?   ?   A . n 
A 1 1297 CYS 1297 1297 ?    ?   ?   A . n 
A 1 1298 ALA 1298 1298 ?    ?   ?   A . n 
A 1 1299 LYS 1299 1299 ?    ?   ?   A . n 
A 1 1300 ALA 1300 1300 ?    ?   ?   A . n 
A 1 1301 LYS 1301 1301 ?    ?   ?   A . n 
A 1 1302 GLU 1302 1302 ?    ?   ?   A . n 
A 1 1303 ALA 1303 1303 ?    ?   ?   A . n 
A 1 1304 LEU 1304 1304 ?    ?   ?   A . n 
A 1 1305 GLU 1305 1305 ?    ?   ?   A . n 
A 1 1306 LEU 1306 1306 ?    ?   ?   A . n 
A 1 1307 THR 1307 1307 ?    ?   ?   A . n 
A 1 1308 ASP 1308 1308 ?    ?   ?   A . n 
A 1 1309 THR 1309 1309 ?    ?   ?   A . n 
A 1 1310 GLY 1310 1310 ?    ?   ?   A . n 
A 1 1311 LEU 1311 1311 ?    ?   ?   A . n 
A 1 1312 LEU 1312 1312 ?    ?   ?   A . n 
A 1 1313 SER 1313 1313 ?    ?   ?   A . n 
A 1 1314 GLY 1314 1314 ?    ?   ?   A . n 
A 1 1315 SER 1315 1315 ?    ?   ?   A . n 
A 1 1316 GLU 1316 1316 ?    ?   ?   A . n 
A 1 1317 GLU 1317 1317 ?    ?   ?   A . n 
A 1 1318 ARG 1318 1318 ?    ?   ?   A . n 
A 1 1319 VAL 1319 1319 ?    ?   ?   A . n 
A 1 1320 GLN 1320 1320 ?    ?   ?   A . n 
A 1 1321 VAL 1321 1321 ?    ?   ?   A . n 
A 1 1322 ALA 1322 1322 ?    ?   ?   A . n 
A 1 1323 LEU 1323 1323 ?    ?   ?   A . n 
A 1 1324 GLU 1324 1324 ?    ?   ?   A . n 
A 1 1325 GLU 1325 1325 ?    ?   ?   A . n 
A 1 1326 LEU 1326 1326 ?    ?   ?   A . n 
A 1 1327 GLN 1327 1327 ?    ?   ?   A . n 
A 1 1328 ASP 1328 1328 ?    ?   ?   A . n 
A 1 1329 LEU 1329 1329 ?    ?   ?   A . n 
A 1 1330 LYS 1330 1330 ?    ?   ?   A . n 
A 1 1331 GLY 1331 1331 ?    ?   ?   A . n 
A 1 1332 VAL 1332 1332 ?    ?   ?   A . n 
A 1 1333 TRP 1333 1333 ?    ?   ?   A . n 
A 1 1334 SER 1334 1334 ?    ?   ?   A . n 
A 1 1335 GLU 1335 1335 ?    ?   ?   A . n 
A 1 1336 LEU 1336 1336 ?    ?   ?   A . n 
A 1 1337 SER 1337 1337 ?    ?   ?   A . n 
A 1 1338 LYS 1338 1338 ?    ?   ?   A . n 
A 1 1339 VAL 1339 1339 ?    ?   ?   A . n 
A 1 1340 TRP 1340 1340 ?    ?   ?   A . n 
A 1 1341 GLU 1341 1341 ?    ?   ?   A . n 
A 1 1342 GLN 1342 1342 ?    ?   ?   A . n 
A 1 1343 ILE 1343 1343 ?    ?   ?   A . n 
A 1 1344 ASP 1344 1344 ?    ?   ?   A . n 
A 1 1345 GLN 1345 1345 ?    ?   ?   A . n 
A 1 1346 MET 1346 1346 ?    ?   ?   A . n 
A 1 1347 LYS 1347 1347 ?    ?   ?   A . n 
A 1 1348 GLU 1348 1348 ?    ?   ?   A . n 
A 1 1349 GLN 1349 1349 ?    ?   ?   A . n 
A 1 1350 PRO 1350 1350 ?    ?   ?   A . n 
A 1 1351 TRP 1351 1351 ?    ?   ?   A . n 
A 1 1352 VAL 1352 1352 ?    ?   ?   A . n 
A 1 1353 SER 1353 1353 ?    ?   ?   A . n 
A 1 1354 VAL 1354 1354 ?    ?   ?   A . n 
A 1 1355 GLN 1355 1355 ?    ?   ?   A . n 
A 1 1356 PRO 1356 1356 ?    ?   ?   A . n 
A 1 1357 ARG 1357 1357 ?    ?   ?   A . n 
A 1 1358 LYS 1358 1358 ?    ?   ?   A . n 
A 1 1359 LEU 1359 1359 ?    ?   ?   A . n 
A 1 1360 ARG 1360 1360 ?    ?   ?   A . n 
A 1 1361 GLN 1361 1361 ?    ?   ?   A . n 
A 1 1362 ASN 1362 1362 ?    ?   ?   A . n 
A 1 1363 LEU 1363 1363 ?    ?   ?   A . n 
A 1 1364 ASP 1364 1364 ?    ?   ?   A . n 
A 1 1365 ALA 1365 1365 ?    ?   ?   A . n 
A 1 1366 LEU 1366 1366 ?    ?   ?   A . n 
A 1 1367 LEU 1367 1367 ?    ?   ?   A . n 
A 1 1368 ASN 1368 1368 ?    ?   ?   A . n 
A 1 1369 GLN 1369 1369 ?    ?   ?   A . n 
A 1 1370 LEU 1370 1370 ?    ?   ?   A . n 
A 1 1371 LYS 1371 1371 ?    ?   ?   A . n 
A 1 1372 SER 1372 1372 ?    ?   ?   A . n 
A 1 1373 PHE 1373 1373 ?    ?   ?   A . n 
A 1 1374 PRO 1374 1374 ?    ?   ?   A . n 
A 1 1375 ALA 1375 1375 ?    ?   ?   A . n 
A 1 1376 ARG 1376 1376 ?    ?   ?   A . n 
A 1 1377 LEU 1377 1377 ?    ?   ?   A . n 
A 1 1378 ARG 1378 1378 ?    ?   ?   A . n 
A 1 1379 GLN 1379 1379 ?    ?   ?   A . n 
A 1 1380 TYR 1380 1380 ?    ?   ?   A . n 
A 1 1381 ALA 1381 1381 ?    ?   ?   A . n 
A 1 1382 SER 1382 1382 ?    ?   ?   A . n 
A 1 1383 TYR 1383 1383 ?    ?   ?   A . n 
A 1 1384 GLU 1384 1384 ?    ?   ?   A . n 
A 1 1385 PHE 1385 1385 ?    ?   ?   A . n 
A 1 1386 VAL 1386 1386 ?    ?   ?   A . n 
A 1 1387 GLN 1387 1387 ?    ?   ?   A . n 
A 1 1388 ARG 1388 1388 ?    ?   ?   A . n 
A 1 1389 LEU 1389 1389 ?    ?   ?   A . n 
A 1 1390 LEU 1390 1390 ?    ?   ?   A . n 
A 1 1391 LYS 1391 1391 ?    ?   ?   A . n 
A 1 1392 GLY 1392 1392 ?    ?   ?   A . n 
A 1 1393 TYR 1393 1393 ?    ?   ?   A . n 
A 1 1394 MET 1394 1394 ?    ?   ?   A . n 
A 1 1395 LYS 1395 1395 ?    ?   ?   A . n 
A 1 1396 ILE 1396 1396 ?    ?   ?   A . n 
A 1 1397 ASN 1397 1397 ?    ?   ?   A . n 
A 1 1398 MET 1398 1398 ?    ?   ?   A . n 
A 1 1399 LEU 1399 1399 ?    ?   ?   A . n 
A 1 1400 VAL 1400 1400 ?    ?   ?   A . n 
A 1 1401 ILE 1401 1401 ?    ?   ?   A . n 
A 1 1402 GLU 1402 1402 ?    ?   ?   A . n 
A 1 1403 LEU 1403 1403 ?    ?   ?   A . n 
A 1 1404 LYS 1404 1404 ?    ?   ?   A . n 
A 1 1405 SER 1405 1405 ?    ?   ?   A . n 
A 1 1406 GLU 1406 1406 ?    ?   ?   A . n 
A 1 1407 ALA 1407 1407 ?    ?   ?   A . n 
A 1 1408 LEU 1408 1408 ?    ?   ?   A . n 
A 1 1409 LYS 1409 1409 ?    ?   ?   A . n 
A 1 1410 ASP 1410 1410 ?    ?   ?   A . n 
A 1 1411 ARG 1411 1411 ?    ?   ?   A . n 
A 1 1412 HIS 1412 1412 ?    ?   ?   A . n 
A 1 1413 TRP 1413 1413 ?    ?   ?   A . n 
A 1 1414 LYS 1414 1414 ?    ?   ?   A . n 
A 1 1415 GLN 1415 1415 ?    ?   ?   A . n 
A 1 1416 LEU 1416 1416 ?    ?   ?   A . n 
A 1 1417 MET 1417 1417 ?    ?   ?   A . n 
A 1 1418 LYS 1418 1418 ?    ?   ?   A . n 
A 1 1419 ARG 1419 1419 ?    ?   ?   A . n 
A 1 1420 LEU 1420 1420 ?    ?   ?   A . n 
A 1 1421 HIS 1421 1421 ?    ?   ?   A . n 
A 1 1422 VAL 1422 1422 ?    ?   ?   A . n 
A 1 1423 ASN 1423 1423 ?    ?   ?   A . n 
A 1 1424 TRP 1424 1424 ?    ?   ?   A . n 
A 1 1425 VAL 1425 1425 ?    ?   ?   A . n 
A 1 1426 VAL 1426 1426 ?    ?   ?   A . n 
A 1 1427 SER 1427 1427 ?    ?   ?   A . n 
A 1 1428 GLU 1428 1428 ?    ?   ?   A . n 
A 1 1429 LEU 1429 1429 ?    ?   ?   A . n 
A 1 1430 THR 1430 1430 ?    ?   ?   A . n 
A 1 1431 LEU 1431 1431 ?    ?   ?   A . n 
A 1 1432 GLY 1432 1432 ?    ?   ?   A . n 
A 1 1433 GLN 1433 1433 ?    ?   ?   A . n 
A 1 1434 ILE 1434 1434 ?    ?   ?   A . n 
A 1 1435 TRP 1435 1435 ?    ?   ?   A . n 
A 1 1436 ASP 1436 1436 ?    ?   ?   A . n 
A 1 1437 VAL 1437 1437 ?    ?   ?   A . n 
A 1 1438 ASP 1438 1438 ?    ?   ?   A . n 
A 1 1439 LEU 1439 1439 ?    ?   ?   A . n 
A 1 1440 GLN 1440 1440 ?    ?   ?   A . n 
A 1 1441 LYS 1441 1441 ?    ?   ?   A . n 
A 1 1442 ASN 1442 1442 ?    ?   ?   A . n 
A 1 1443 GLU 1443 1443 ?    ?   ?   A . n 
A 1 1444 ALA 1444 1444 ?    ?   ?   A . n 
A 1 1445 ILE 1445 1445 ?    ?   ?   A . n 
A 1 1446 VAL 1446 1446 ?    ?   ?   A . n 
A 1 1447 LYS 1447 1447 ?    ?   ?   A . n 
A 1 1448 ASP 1448 1448 ?    ?   ?   A . n 
A 1 1449 VAL 1449 1449 ?    ?   ?   A . n 
A 1 1450 LEU 1450 1450 ?    ?   ?   A . n 
A 1 1451 LEU 1451 1451 ?    ?   ?   A . n 
A 1 1452 VAL 1452 1452 ?    ?   ?   A . n 
A 1 1453 ALA 1453 1453 ?    ?   ?   A . n 
A 1 1454 GLN 1454 1454 ?    ?   ?   A . n 
A 1 1455 GLY 1455 1455 ?    ?   ?   A . n 
A 1 1456 GLU 1456 1456 ?    ?   ?   A . n 
A 1 1457 MET 1457 1457 ?    ?   ?   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 ?    ?   ?   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 ?    ?   ?   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 4706 MG  MG  A . 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DH7 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9DH7 
_struct.title                        'State-4 of the motor domain from full-length human dynein-1 in 5mM AMPPNP with 5mM Mg2+' 
_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        9DH7 
_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 ? 
# 
_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              9DH7 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 4646 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q14204 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  4646 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       4646 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 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 SER 2231 OG  ? ? ? 1_555 F MG . MG ? ? A SER 2231 A MG 4705 1_555 ? ? ? ? ? ? ? 1.891 ? ? 
metalc2 metalc ? ? A GLU 2344 OE2 ? ? ? 1_555 F MG . MG ? ? A GLU 2344 A MG 4705 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc3 metalc ? ? C ATP .    O2G ? ? ? 1_555 F MG . MG ? ? A ATP 4702 A MG 4705 1_555 ? ? ? ? ? ? ? 2.142 ? ? 
metalc4 metalc ? ? C ATP .    O2B ? ? ? 1_555 F MG . MG ? ? A ATP 4702 A MG 4705 1_555 ? ? ? ? ? ? ? 2.732 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 78.7  ? 
2 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 156.4 ? 
3 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 84.9  ? 
4 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 74.9  ? 
5 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 72.2  ? 
6 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 84.0  ? 
# 
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                   9DH7 
_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 ? ? -83.00  49.17   
2  1 PHE A 1626 ? ? 52.53   74.21   
3  1 ALA A 1862 ? ? 56.32   -122.27 
4  1 ASN A 2130 ? ? -94.51  53.91   
5  1 LYS A 2673 ? ? -69.29  2.67    
6  1 TYR A 2881 ? ? -90.07  57.63   
7  1 GLU A 2904 ? ? -126.58 -164.33 
8  1 LEU A 2905 ? ? -37.40  127.62  
9  1 GLU A 3842 ? ? 39.91   42.58   
10 1 LEU A 3973 ? ? -95.00  52.18   
11 1 GLU A 4034 ? ? 67.06   -2.62   
12 1 GLU A 4206 ? ? -94.90  56.55   
13 1 LYS A 4287 ? ? 39.71   56.87   
14 1 GLU A 4599 ? ? 58.81   -147.56 
15 1 PHE A 4620 ? ? -161.31 -169.91 
16 1 LYS A 4629 ? ? 70.16   -7.83   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9DH7 
_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                    9DH7 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.4 
_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               20077 
_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, 5 mM MgCl2, 5 mM DTT, 5 mM AMPPNP' 
_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 the motor domain from full-length human dynein-1 in 5mM AMPPNP with 5mM Mg2+' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9DH7 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS GLACIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             3000 
_em_imaging.calibrated_defocus_min          1200 
_em_imaging.calibrated_defocus_max          3000 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           45000 
_em_imaging.calibrated_magnification        45000 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            50 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              9DH7 
_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                9DH7 
_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 GLU 2389 ? A GLU 2389 
1536 1 Y 1 A GLY 2390 ? A GLY 2390 
1537 1 Y 1 A GLU 2391 ? A GLU 2391 
1538 1 Y 1 A ASP 2392 ? A ASP 2392 
1539 1 Y 1 A GLU 2393 ? A GLU 2393 
1540 1 Y 1 A ALA 2394 ? A ALA 2394 
1541 1 Y 1 A GLN 2395 ? A GLN 2395 
1542 1 Y 1 A ARG 2396 ? A ARG 2396 
1543 1 Y 1 A ARG 2397 ? A ARG 2397 
1544 1 Y 1 A ARG 2398 ? A ARG 2398 
1545 1 Y 1 A LYS 2399 ? A LYS 2399 
1546 1 Y 1 A GLY 2400 ? A GLY 2400 
1547 1 Y 1 A LYS 2401 ? A LYS 2401 
1548 1 Y 1 A GLU 2402 ? A GLU 2402 
1549 1 Y 1 A ASP 2403 ? A ASP 2403 
1550 1 Y 1 A GLU 2404 ? A GLU 2404 
1551 1 Y 1 A GLY 2405 ? A GLY 2405 
1552 1 Y 1 A GLU 2406 ? A GLU 2406 
1553 1 Y 1 A GLU 2407 ? A GLU 2407 
1554 1 Y 1 A ALA 2408 ? A ALA 2408 
1555 1 Y 1 A ALA 2409 ? A ALA 2409 
1556 1 Y 1 A LYS 3242 ? A LYS 3242 
1557 1 Y 1 A MET 3243 ? A MET 3243 
1558 1 Y 1 A VAL 3244 ? A VAL 3244 
1559 1 Y 1 A LYS 3245 ? A LYS 3245 
1560 1 Y 1 A ASP 3246 ? A ASP 3246 
1561 1 Y 1 A GLN 3247 ? A GLN 3247 
1562 1 Y 1 A GLN 3248 ? A GLN 3248 
1563 1 Y 1 A GLU 3249 ? A GLU 3249 
1564 1 Y 1 A ALA 3250 ? A ALA 3250 
1565 1 Y 1 A GLU 3251 ? A GLU 3251 
1566 1 Y 1 A LYS 3252 ? A LYS 3252 
1567 1 Y 1 A LYS 3253 ? A LYS 3253 
1568 1 Y 1 A LYS 3254 ? A LYS 3254 
1569 1 Y 1 A VAL 3255 ? A VAL 3255 
1570 1 Y 1 A MET 3256 ? A MET 3256 
1571 1 Y 1 A SER 3257 ? A SER 3257 
1572 1 Y 1 A GLN 3258 ? A GLN 3258 
1573 1 Y 1 A GLU 3259 ? A GLU 3259 
1574 1 Y 1 A ILE 3260 ? A ILE 3260 
1575 1 Y 1 A GLN 3261 ? A GLN 3261 
1576 1 Y 1 A GLU 3262 ? A GLU 3262 
1577 1 Y 1 A GLN 3263 ? A GLN 3263 
1578 1 Y 1 A LEU 3264 ? A LEU 3264 
1579 1 Y 1 A HIS 3265 ? A HIS 3265 
1580 1 Y 1 A LYS 3266 ? A LYS 3266 
1581 1 Y 1 A GLN 3267 ? A GLN 3267 
1582 1 Y 1 A GLN 3268 ? A GLN 3268 
1583 1 Y 1 A GLU 3269 ? A GLU 3269 
1584 1 Y 1 A VAL 3270 ? A VAL 3270 
1585 1 Y 1 A ILE 3271 ? A ILE 3271 
1586 1 Y 1 A ALA 3272 ? A ALA 3272 
1587 1 Y 1 A ASP 3273 ? A ASP 3273 
1588 1 Y 1 A LYS 3274 ? A LYS 3274 
1589 1 Y 1 A GLN 3275 ? A GLN 3275 
1590 1 Y 1 A MET 3276 ? A MET 3276 
1591 1 Y 1 A SER 3277 ? A SER 3277 
1592 1 Y 1 A VAL 3278 ? A VAL 3278 
1593 1 Y 1 A LYS 3279 ? A LYS 3279 
1594 1 Y 1 A GLU 3280 ? A GLU 3280 
1595 1 Y 1 A ASP 3281 ? A ASP 3281 
1596 1 Y 1 A LEU 3282 ? A LEU 3282 
1597 1 Y 1 A ASP 3283 ? A ASP 3283 
1598 1 Y 1 A LYS 3284 ? A LYS 3284 
1599 1 Y 1 A VAL 3285 ? A VAL 3285 
1600 1 Y 1 A GLU 3286 ? A GLU 3286 
1601 1 Y 1 A PRO 3287 ? A PRO 3287 
1602 1 Y 1 A ALA 3288 ? A ALA 3288 
1603 1 Y 1 A VAL 3289 ? A VAL 3289 
1604 1 Y 1 A ILE 3290 ? A ILE 3290 
1605 1 Y 1 A GLU 3291 ? A GLU 3291 
1606 1 Y 1 A ALA 3292 ? A ALA 3292 
1607 1 Y 1 A GLN 3293 ? A GLN 3293 
1608 1 Y 1 A ASN 3294 ? A ASN 3294 
1609 1 Y 1 A ALA 3295 ? A ALA 3295 
1610 1 Y 1 A VAL 3296 ? A VAL 3296 
1611 1 Y 1 A LYS 3297 ? A LYS 3297 
1612 1 Y 1 A SER 3298 ? A SER 3298 
1613 1 Y 1 A ILE 3299 ? A ILE 3299 
1614 1 Y 1 A LYS 3300 ? A LYS 3300 
1615 1 Y 1 A LYS 3301 ? A LYS 3301 
1616 1 Y 1 A GLN 3302 ? A GLN 3302 
1617 1 Y 1 A HIS 3303 ? A HIS 3303 
1618 1 Y 1 A LEU 3304 ? A LEU 3304 
1619 1 Y 1 A VAL 3305 ? A VAL 3305 
1620 1 Y 1 A GLU 3306 ? A GLU 3306 
1621 1 Y 1 A VAL 3307 ? A VAL 3307 
1622 1 Y 1 A ARG 3308 ? A ARG 3308 
1623 1 Y 1 A SER 3309 ? A SER 3309 
1624 1 Y 1 A MET 3310 ? A MET 3310 
1625 1 Y 1 A ALA 3311 ? A ALA 3311 
1626 1 Y 1 A ASN 3312 ? A ASN 3312 
1627 1 Y 1 A PRO 3313 ? A PRO 3313 
1628 1 Y 1 A PRO 3314 ? A PRO 3314 
1629 1 Y 1 A ALA 3315 ? A ALA 3315 
1630 1 Y 1 A ALA 3316 ? A ALA 3316 
1631 1 Y 1 A VAL 3317 ? A VAL 3317 
1632 1 Y 1 A LYS 3318 ? A LYS 3318 
1633 1 Y 1 A LEU 3319 ? A LEU 3319 
1634 1 Y 1 A ALA 3320 ? A ALA 3320 
1635 1 Y 1 A LEU 3321 ? A LEU 3321 
1636 1 Y 1 A GLU 3322 ? A GLU 3322 
1637 1 Y 1 A SER 3323 ? A SER 3323 
1638 1 Y 1 A ILE 3324 ? A ILE 3324 
1639 1 Y 1 A CYS 3325 ? A CYS 3325 
1640 1 Y 1 A LEU 3326 ? A LEU 3326 
1641 1 Y 1 A LEU 3327 ? A LEU 3327 
1642 1 Y 1 A LEU 3328 ? A LEU 3328 
1643 1 Y 1 A GLY 3329 ? A GLY 3329 
1644 1 Y 1 A GLU 3330 ? A GLU 3330 
1645 1 Y 1 A SER 3331 ? A SER 3331 
1646 1 Y 1 A THR 3332 ? A THR 3332 
1647 1 Y 1 A THR 3333 ? A THR 3333 
1648 1 Y 1 A ASP 3334 ? A ASP 3334 
1649 1 Y 1 A TRP 3335 ? A TRP 3335 
1650 1 Y 1 A LYS 3336 ? A LYS 3336 
1651 1 Y 1 A GLN 3337 ? A GLN 3337 
1652 1 Y 1 A ILE 3338 ? A ILE 3338 
1653 1 Y 1 A ARG 3339 ? A ARG 3339 
1654 1 Y 1 A SER 3340 ? A SER 3340 
1655 1 Y 1 A ILE 3341 ? A ILE 3341 
1656 1 Y 1 A ILE 3342 ? A ILE 3342 
1657 1 Y 1 A MET 3343 ? A MET 3343 
1658 1 Y 1 A ARG 3344 ? A ARG 3344 
1659 1 Y 1 A GLU 3345 ? A GLU 3345 
1660 1 Y 1 A ASN 3346 ? A ASN 3346 
1661 1 Y 1 A PHE 3347 ? A PHE 3347 
1662 1 Y 1 A ILE 3348 ? A ILE 3348 
1663 1 Y 1 A PRO 3349 ? A PRO 3349 
1664 1 Y 1 A THR 3350 ? A THR 3350 
1665 1 Y 1 A ILE 3351 ? A ILE 3351 
1666 1 Y 1 A VAL 3352 ? A VAL 3352 
1667 1 Y 1 A ASN 3353 ? A ASN 3353 
1668 1 Y 1 A PHE 3354 ? A PHE 3354 
1669 1 Y 1 A SER 3355 ? A SER 3355 
1670 1 Y 1 A ALA 3356 ? A ALA 3356 
1671 1 Y 1 A GLU 3357 ? A GLU 3357 
1672 1 Y 1 A GLU 3358 ? A GLU 3358 
1673 1 Y 1 A ILE 3359 ? A ILE 3359 
1674 1 Y 1 A SER 3360 ? A SER 3360 
1675 1 Y 1 A ASP 3361 ? A ASP 3361 
1676 1 Y 1 A ALA 3362 ? A ALA 3362 
1677 1 Y 1 A ILE 3363 ? A ILE 3363 
1678 1 Y 1 A ARG 3364 ? A ARG 3364 
1679 1 Y 1 A GLU 3365 ? A GLU 3365 
1680 1 Y 1 A LYS 3366 ? A LYS 3366 
1681 1 Y 1 A MET 3367 ? A MET 3367 
1682 1 Y 1 A LYS 3368 ? A LYS 3368 
1683 1 Y 1 A LYS 3369 ? A LYS 3369 
1684 1 Y 1 A ASN 3370 ? A ASN 3370 
1685 1 Y 1 A TYR 3371 ? A TYR 3371 
1686 1 Y 1 A MET 3372 ? A MET 3372 
1687 1 Y 1 A SER 3373 ? A SER 3373 
1688 1 Y 1 A ASN 3374 ? A ASN 3374 
1689 1 Y 1 A PRO 3375 ? A PRO 3375 
1690 1 Y 1 A SER 3376 ? A SER 3376 
1691 1 Y 1 A TYR 3377 ? A TYR 3377 
1692 1 Y 1 A ASN 3378 ? A ASN 3378 
1693 1 Y 1 A TYR 3379 ? A TYR 3379 
1694 1 Y 1 A GLU 3380 ? A GLU 3380 
1695 1 Y 1 A ILE 3381 ? A ILE 3381 
1696 1 Y 1 A VAL 3382 ? A VAL 3382 
1697 1 Y 1 A ASN 3383 ? A ASN 3383 
1698 1 Y 1 A ARG 3384 ? A ARG 3384 
1699 1 Y 1 A ALA 3385 ? A ALA 3385 
1700 1 Y 1 A SER 3386 ? A SER 3386 
1701 1 Y 1 A LEU 3387 ? A LEU 3387 
1702 1 Y 1 A ALA 3388 ? A ALA 3388 
1703 1 Y 1 A CYS 3389 ? A CYS 3389 
1704 1 Y 1 A GLY 3390 ? A GLY 3390 
1705 1 Y 1 A PRO 3391 ? A PRO 3391 
1706 1 Y 1 A MET 3392 ? A MET 3392 
1707 1 Y 1 A VAL 3393 ? A VAL 3393 
1708 1 Y 1 A LYS 3394 ? A LYS 3394 
1709 1 Y 1 A TRP 3395 ? A TRP 3395 
1710 1 Y 1 A ALA 3396 ? A ALA 3396 
1711 1 Y 1 A ILE 3397 ? A ILE 3397 
1712 1 Y 1 A ALA 3398 ? A ALA 3398 
1713 1 Y 1 A GLN 3399 ? A GLN 3399 
1714 1 Y 1 A LEU 3400 ? A LEU 3400 
1715 1 Y 1 A ASN 3401 ? A ASN 3401 
1716 1 Y 1 A TYR 3402 ? A TYR 3402 
1717 1 Y 1 A ALA 3403 ? A ALA 3403 
1718 1 Y 1 A ASP 3404 ? A ASP 3404 
1719 1 Y 1 A MET 3405 ? A MET 3405 
1720 1 Y 1 A LEU 3406 ? A LEU 3406 
1721 1 Y 1 A LYS 3407 ? A LYS 3407 
1722 1 Y 1 A ARG 3408 ? A ARG 3408 
1723 1 Y 1 A VAL 3409 ? A VAL 3409 
1724 1 Y 1 A GLU 3410 ? A GLU 3410 
1725 1 Y 1 A PRO 3411 ? A PRO 3411 
1726 1 Y 1 A LEU 3412 ? A LEU 3412 
1727 1 Y 1 A ARG 3413 ? A ARG 3413 
1728 1 Y 1 A ASN 3414 ? A ASN 3414 
1729 1 Y 1 A GLU 3415 ? A GLU 3415 
1730 1 Y 1 A LEU 3416 ? A LEU 3416 
1731 1 Y 1 A GLN 3417 ? A GLN 3417 
1732 1 Y 1 A LYS 3418 ? A LYS 3418 
1733 1 Y 1 A LEU 3419 ? A LEU 3419 
1734 1 Y 1 A GLU 3420 ? A GLU 3420 
1735 1 Y 1 A ASP 3421 ? A ASP 3421 
1736 1 Y 1 A ASP 3422 ? A ASP 3422 
1737 1 Y 1 A ALA 3423 ? A ALA 3423 
1738 1 Y 1 A LYS 3424 ? A LYS 3424 
1739 1 Y 1 A ASP 3425 ? A ASP 3425 
1740 1 Y 1 A ASN 3426 ? A ASN 3426 
1741 1 Y 1 A GLN 3427 ? A GLN 3427 
1742 1 Y 1 A GLN 3428 ? A GLN 3428 
1743 1 Y 1 A LYS 3429 ? A LYS 3429 
1744 1 Y 1 A ALA 3430 ? A ALA 3430 
1745 1 Y 1 A ASN 3431 ? A ASN 3431 
1746 1 Y 1 A GLU 3432 ? A GLU 3432 
1747 1 Y 1 A VAL 3433 ? A VAL 3433 
1748 1 Y 1 A GLU 3434 ? A GLU 3434 
1749 1 Y 1 A GLN 3435 ? A GLN 3435 
1750 1 Y 1 A MET 3436 ? A MET 3436 
1751 1 Y 1 A ILE 3437 ? A ILE 3437 
1752 1 Y 1 A ARG 3438 ? A ARG 3438 
1753 1 Y 1 A ASP 3439 ? A ASP 3439 
1754 1 Y 1 A LEU 3440 ? A LEU 3440 
1755 1 Y 1 A GLU 3441 ? A GLU 3441 
1756 1 Y 1 A ALA 3442 ? A ALA 3442 
1757 1 Y 1 A SER 3443 ? A SER 3443 
1758 1 Y 1 A ILE 3444 ? A ILE 3444 
1759 1 Y 1 A ALA 3445 ? A ALA 3445 
1760 1 Y 1 A ARG 3446 ? A ARG 3446 
1761 1 Y 1 A TYR 3447 ? A TYR 3447 
1762 1 Y 1 A LYS 3448 ? A LYS 3448 
1763 1 Y 1 A MET 4348 ? A MET 4348 
1764 1 Y 1 A LEU 4349 ? A LEU 4349 
1765 1 Y 1 A GLU 4350 ? A GLU 4350 
1766 1 Y 1 A ASP 4351 ? A ASP 4351 
1767 1 Y 1 A GLU 4352 ? A GLU 4352 
1768 1 Y 1 A ASP 4353 ? A ASP 4353 
1769 1 Y 1 A ASP 4354 ? A ASP 4354 
1770 1 Y 1 A LEU 4355 ? A LEU 4355 
1771 1 Y 1 A ALA 4356 ? A ALA 4356 
1772 1 Y 1 A TYR 4357 ? A TYR 4357 
1773 1 Y 1 A ALA 4358 ? A ALA 4358 
1774 1 Y 1 A GLU 4359 ? A GLU 4359 
1775 1 Y 1 A THR 4360 ? A THR 4360 
1776 1 Y 1 A GLU 4361 ? A GLU 4361 
1777 1 Y 1 A LYS 4362 ? A LYS 4362 
1778 1 Y 1 A LYS 4363 ? A LYS 4363 
1779 1 Y 1 A THR 4364 ? A THR 4364 
1780 1 Y 1 A ARG 4365 ? A ARG 4365 
1781 1 Y 1 A THR 4366 ? A THR 4366 
1782 1 Y 1 A ASP 4367 ? A ASP 4367 
1783 1 Y 1 A SER 4368 ? A SER 4368 
1784 1 Y 1 A THR 4369 ? A THR 4369 
1785 1 Y 1 A SER 4370 ? A SER 4370 
1786 1 Y 1 A ASP 4371 ? A ASP 4371 
1787 1 Y 1 A GLY 4372 ? A GLY 4372 
1788 1 Y 1 A ARG 4373 ? A ARG 4373 
1789 1 Y 1 A GLU 4646 ? A GLU 4646 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
ATP PG     P  N N 116 
ATP O1G    O  N N 117 
ATP O2G    O  N N 118 
ATP O3G    O  N N 119 
ATP PB     P  N R 120 
ATP O1B    O  N N 121 
ATP O2B    O  N N 122 
ATP O3B    O  N N 123 
ATP PA     P  N R 124 
ATP O1A    O  N N 125 
ATP O2A    O  N N 126 
ATP O3A    O  N N 127 
ATP "O5'"  O  N N 128 
ATP "C5'"  C  N N 129 
ATP "C4'"  C  N R 130 
ATP "O4'"  O  N N 131 
ATP "C3'"  C  N S 132 
ATP "O3'"  O  N N 133 
ATP "C2'"  C  N R 134 
ATP "O2'"  O  N N 135 
ATP "C1'"  C  N R 136 
ATP N9     N  Y N 137 
ATP C8     C  Y N 138 
ATP N7     N  Y N 139 
ATP C5     C  Y N 140 
ATP C6     C  Y N 141 
ATP N6     N  N N 142 
ATP N1     N  Y N 143 
ATP C2     C  Y N 144 
ATP N3     N  Y N 145 
ATP C4     C  Y N 146 
ATP HOG2   H  N N 147 
ATP HOG3   H  N N 148 
ATP HOB2   H  N N 149 
ATP HOA2   H  N N 150 
ATP "H5'1" H  N N 151 
ATP "H5'2" H  N N 152 
ATP "H4'"  H  N N 153 
ATP "H3'"  H  N N 154 
ATP "HO3'" H  N N 155 
ATP "H2'"  H  N N 156 
ATP "HO2'" H  N N 157 
ATP "H1'"  H  N N 158 
ATP H8     H  N N 159 
ATP HN61   H  N N 160 
ATP HN62   H  N N 161 
ATP H2     H  N N 162 
CYS N      N  N N 163 
CYS CA     C  N R 164 
CYS C      C  N N 165 
CYS O      O  N N 166 
CYS CB     C  N N 167 
CYS SG     S  N N 168 
CYS OXT    O  N N 169 
CYS H      H  N N 170 
CYS H2     H  N N 171 
CYS HA     H  N N 172 
CYS HB2    H  N N 173 
CYS HB3    H  N N 174 
CYS HG     H  N N 175 
CYS HXT    H  N N 176 
GLN N      N  N N 177 
GLN CA     C  N S 178 
GLN C      C  N N 179 
GLN O      O  N N 180 
GLN CB     C  N N 181 
GLN CG     C  N N 182 
GLN CD     C  N N 183 
GLN OE1    O  N N 184 
GLN NE2    N  N N 185 
GLN OXT    O  N N 186 
GLN H      H  N N 187 
GLN H2     H  N N 188 
GLN HA     H  N N 189 
GLN HB2    H  N N 190 
GLN HB3    H  N N 191 
GLN HG2    H  N N 192 
GLN HG3    H  N N 193 
GLN HE21   H  N N 194 
GLN HE22   H  N N 195 
GLN HXT    H  N N 196 
GLU N      N  N N 197 
GLU CA     C  N S 198 
GLU C      C  N N 199 
GLU O      O  N N 200 
GLU CB     C  N N 201 
GLU CG     C  N N 202 
GLU CD     C  N N 203 
GLU OE1    O  N N 204 
GLU OE2    O  N N 205 
GLU OXT    O  N N 206 
GLU H      H  N N 207 
GLU H2     H  N N 208 
GLU HA     H  N N 209 
GLU HB2    H  N N 210 
GLU HB3    H  N N 211 
GLU HG2    H  N N 212 
GLU HG3    H  N N 213 
GLU HE2    H  N N 214 
GLU HXT    H  N N 215 
GLY N      N  N N 216 
GLY CA     C  N N 217 
GLY C      C  N N 218 
GLY O      O  N N 219 
GLY OXT    O  N N 220 
GLY H      H  N N 221 
GLY H2     H  N N 222 
GLY HA2    H  N N 223 
GLY HA3    H  N N 224 
GLY HXT    H  N N 225 
HIS N      N  N N 226 
HIS CA     C  N S 227 
HIS C      C  N N 228 
HIS O      O  N N 229 
HIS CB     C  N N 230 
HIS CG     C  Y N 231 
HIS ND1    N  Y N 232 
HIS CD2    C  Y N 233 
HIS CE1    C  Y N 234 
HIS NE2    N  Y N 235 
HIS OXT    O  N N 236 
HIS H      H  N N 237 
HIS H2     H  N N 238 
HIS HA     H  N N 239 
HIS HB2    H  N N 240 
HIS HB3    H  N N 241 
HIS HD1    H  N N 242 
HIS HD2    H  N N 243 
HIS HE1    H  N N 244 
HIS HE2    H  N N 245 
HIS HXT    H  N N 246 
ILE N      N  N N 247 
ILE CA     C  N S 248 
ILE C      C  N N 249 
ILE O      O  N N 250 
ILE CB     C  N S 251 
ILE CG1    C  N N 252 
ILE CG2    C  N N 253 
ILE CD1    C  N N 254 
ILE OXT    O  N N 255 
ILE H      H  N N 256 
ILE H2     H  N N 257 
ILE HA     H  N N 258 
ILE HB     H  N N 259 
ILE HG12   H  N N 260 
ILE HG13   H  N N 261 
ILE HG21   H  N N 262 
ILE HG22   H  N N 263 
ILE HG23   H  N N 264 
ILE HD11   H  N N 265 
ILE HD12   H  N N 266 
ILE HD13   H  N N 267 
ILE HXT    H  N N 268 
LEU N      N  N N 269 
LEU CA     C  N S 270 
LEU C      C  N N 271 
LEU O      O  N N 272 
LEU CB     C  N N 273 
LEU CG     C  N N 274 
LEU CD1    C  N N 275 
LEU CD2    C  N N 276 
LEU OXT    O  N N 277 
LEU H      H  N N 278 
LEU H2     H  N N 279 
LEU HA     H  N N 280 
LEU HB2    H  N N 281 
LEU HB3    H  N N 282 
LEU HG     H  N N 283 
LEU HD11   H  N N 284 
LEU HD12   H  N N 285 
LEU HD13   H  N N 286 
LEU HD21   H  N N 287 
LEU HD22   H  N N 288 
LEU HD23   H  N N 289 
LEU HXT    H  N N 290 
LYS N      N  N N 291 
LYS CA     C  N S 292 
LYS C      C  N N 293 
LYS O      O  N N 294 
LYS CB     C  N N 295 
LYS CG     C  N N 296 
LYS CD     C  N N 297 
LYS CE     C  N N 298 
LYS NZ     N  N N 299 
LYS OXT    O  N N 300 
LYS H      H  N N 301 
LYS H2     H  N N 302 
LYS HA     H  N N 303 
LYS HB2    H  N N 304 
LYS HB3    H  N N 305 
LYS HG2    H  N N 306 
LYS HG3    H  N N 307 
LYS HD2    H  N N 308 
LYS HD3    H  N N 309 
LYS HE2    H  N N 310 
LYS HE3    H  N N 311 
LYS HZ1    H  N N 312 
LYS HZ2    H  N N 313 
LYS HZ3    H  N N 314 
LYS HXT    H  N N 315 
MET N      N  N N 316 
MET CA     C  N S 317 
MET C      C  N N 318 
MET O      O  N N 319 
MET CB     C  N N 320 
MET CG     C  N N 321 
MET SD     S  N N 322 
MET CE     C  N N 323 
MET OXT    O  N N 324 
MET H      H  N N 325 
MET H2     H  N N 326 
MET HA     H  N N 327 
MET HB2    H  N N 328 
MET HB3    H  N N 329 
MET HG2    H  N N 330 
MET HG3    H  N N 331 
MET HE1    H  N N 332 
MET HE2    H  N N 333 
MET HE3    H  N N 334 
MET HXT    H  N N 335 
MG  MG     MG N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TYR N      N  N N 435 
TYR CA     C  N S 436 
TYR C      C  N N 437 
TYR O      O  N N 438 
TYR CB     C  N N 439 
TYR CG     C  Y N 440 
TYR CD1    C  Y N 441 
TYR CD2    C  Y N 442 
TYR CE1    C  Y N 443 
TYR CE2    C  Y N 444 
TYR CZ     C  Y N 445 
TYR OH     O  N N 446 
TYR OXT    O  N N 447 
TYR H      H  N N 448 
TYR H2     H  N N 449 
TYR HA     H  N N 450 
TYR HB2    H  N N 451 
TYR HB3    H  N N 452 
TYR HD1    H  N N 453 
TYR HD2    H  N N 454 
TYR HE1    H  N N 455 
TYR HE2    H  N N 456 
TYR HH     H  N N 457 
TYR HXT    H  N N 458 
VAL N      N  N N 459 
VAL CA     C  N S 460 
VAL C      C  N N 461 
VAL O      O  N N 462 
VAL CB     C  N N 463 
VAL CG1    C  N N 464 
VAL CG2    C  N N 465 
VAL OXT    O  N N 466 
VAL H      H  N N 467 
VAL H2     H  N N 468 
VAL HA     H  N N 469 
VAL HB     H  N N 470 
VAL HG11   H  N N 471 
VAL HG12   H  N N 472 
VAL HG13   H  N N 473 
VAL HG21   H  N N 474 
VAL HG22   H  N N 475 
VAL HG23   H  N N 476 
VAL HXT    H  N N 477 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
ATP PG    O1G    doub N N 114 
ATP PG    O2G    sing N N 115 
ATP PG    O3G    sing N N 116 
ATP PG    O3B    sing N N 117 
ATP O2G   HOG2   sing N N 118 
ATP O3G   HOG3   sing N N 119 
ATP PB    O1B    doub N N 120 
ATP PB    O2B    sing N N 121 
ATP PB    O3B    sing N N 122 
ATP PB    O3A    sing N N 123 
ATP O2B   HOB2   sing N N 124 
ATP PA    O1A    doub N N 125 
ATP PA    O2A    sing N N 126 
ATP PA    O3A    sing N N 127 
ATP PA    "O5'"  sing N N 128 
ATP O2A   HOA2   sing N N 129 
ATP "O5'" "C5'"  sing N N 130 
ATP "C5'" "C4'"  sing N N 131 
ATP "C5'" "H5'1" sing N N 132 
ATP "C5'" "H5'2" sing N N 133 
ATP "C4'" "O4'"  sing N N 134 
ATP "C4'" "C3'"  sing N N 135 
ATP "C4'" "H4'"  sing N N 136 
ATP "O4'" "C1'"  sing N N 137 
ATP "C3'" "O3'"  sing N N 138 
ATP "C3'" "C2'"  sing N N 139 
ATP "C3'" "H3'"  sing N N 140 
ATP "O3'" "HO3'" sing N N 141 
ATP "C2'" "O2'"  sing N N 142 
ATP "C2'" "C1'"  sing N N 143 
ATP "C2'" "H2'"  sing N N 144 
ATP "O2'" "HO2'" sing N N 145 
ATP "C1'" N9     sing N N 146 
ATP "C1'" "H1'"  sing N N 147 
ATP N9    C8     sing Y N 148 
ATP N9    C4     sing Y N 149 
ATP C8    N7     doub Y N 150 
ATP C8    H8     sing N N 151 
ATP N7    C5     sing Y N 152 
ATP C5    C6     sing Y N 153 
ATP C5    C4     doub Y N 154 
ATP C6    N6     sing N N 155 
ATP C6    N1     doub Y N 156 
ATP N6    HN61   sing N N 157 
ATP N6    HN62   sing N N 158 
ATP N1    C2     sing Y N 159 
ATP C2    N3     doub Y N 160 
ATP C2    H2     sing N N 161 
ATP N3    C4     sing Y N 162 
CYS N     CA     sing N N 163 
CYS N     H      sing N N 164 
CYS N     H2     sing N N 165 
CYS CA    C      sing N N 166 
CYS CA    CB     sing N N 167 
CYS CA    HA     sing N N 168 
CYS C     O      doub N N 169 
CYS C     OXT    sing N N 170 
CYS CB    SG     sing N N 171 
CYS CB    HB2    sing N N 172 
CYS CB    HB3    sing N N 173 
CYS SG    HG     sing N N 174 
CYS OXT   HXT    sing N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-09-03 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9DH7 
_em_admin.last_update        2025-04-23 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-4 of the motor domain from full-length human dynein-1 in 5mM AMPPNP with 5mM Mg2+' 
# 
_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' 'R35 GM142959' 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 'R35 GM139483' 2 
# 
_atom_sites.entry_id                    9DH7 
_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 ? 180.435 230.389 236.396 1.00 125.88 ? 1535 ASP A N     1 
ATOM   2     C  CA    . ASP A 1 1535 ? 181.287 229.915 235.311 1.00 129.72 ? 1535 ASP A CA    1 
ATOM   3     C  C     . ASP A 1 1535 ? 180.604 230.099 233.960 1.00 133.85 ? 1535 ASP A C     1 
ATOM   4     O  O     . ASP A 1 1535 ? 181.167 229.766 232.918 1.00 132.16 ? 1535 ASP A O     1 
ATOM   5     C  CB    . ASP A 1 1535 ? 181.651 228.444 235.520 1.00 125.63 ? 1535 ASP A CB    1 
ATOM   6     C  CG    . ASP A 1 1535 ? 182.565 228.233 236.711 1.00 120.78 ? 1535 ASP A CG    1 
ATOM   7     O  OD1   . ASP A 1 1535 ? 183.324 229.164 237.052 1.00 120.30 ? 1535 ASP A OD1   1 
ATOM   8     O  OD2   . ASP A 1 1535 ? 182.526 227.135 237.306 1.00 116.96 ? 1535 ASP A OD2   1 
ATOM   9     N  N     . VAL A 1 1536 ? 179.385 230.633 233.987 1.00 135.86 ? 1536 VAL A N     1 
ATOM   10    C  CA    . VAL A 1 1536 ? 178.598 230.851 232.785 1.00 133.66 ? 1536 VAL A CA    1 
ATOM   11    C  C     . VAL A 1 1536 ? 178.424 232.336 232.489 1.00 136.10 ? 1536 VAL A C     1 
ATOM   12    O  O     . VAL A 1 1536 ? 178.440 232.745 231.326 1.00 135.67 ? 1536 VAL A O     1 
ATOM   13    C  CB    . VAL A 1 1536 ? 177.228 230.145 232.898 1.00 126.15 ? 1536 VAL A CB    1 
ATOM   14    C  CG1   . VAL A 1 1536 ? 176.358 230.449 231.687 1.00 128.22 ? 1536 VAL A CG1   1 
ATOM   15    C  CG2   . VAL A 1 1536 ? 177.417 228.645 233.061 1.00 115.32 ? 1536 VAL A CG2   1 
ATOM   16    N  N     . TRP A 1 1537 ? 178.273 233.160 233.530 1.00 135.52 ? 1537 TRP A N     1 
ATOM   17    C  CA    . TRP A 1 1537 ? 178.019 234.584 233.325 1.00 136.52 ? 1537 TRP A CA    1 
ATOM   18    C  C     . TRP A 1 1537 ? 179.180 235.261 232.606 1.00 138.24 ? 1537 TRP A C     1 
ATOM   19    O  O     . TRP A 1 1537 ? 178.965 236.074 231.700 1.00 138.00 ? 1537 TRP A O     1 
ATOM   20    C  CB    . TRP A 1 1537 ? 177.748 235.265 234.668 1.00 134.02 ? 1537 TRP A CB    1 
ATOM   21    C  CG    . TRP A 1 1537 ? 177.036 236.587 234.563 1.00 138.80 ? 1537 TRP A CG    1 
ATOM   22    C  CD1   . TRP A 1 1537 ? 177.317 237.605 233.697 1.00 135.21 ? 1537 TRP A CD1   1 
ATOM   23    C  CD2   . TRP A 1 1537 ? 175.929 237.032 235.357 1.00 144.38 ? 1537 TRP A CD2   1 
ATOM   24    N  NE1   . TRP A 1 1537 ? 176.453 238.653 233.902 1.00 134.31 ? 1537 TRP A NE1   1 
ATOM   25    C  CE2   . TRP A 1 1537 ? 175.591 238.327 234.914 1.00 142.19 ? 1537 TRP A CE2   1 
ATOM   26    C  CE3   . TRP A 1 1537 ? 175.191 236.461 236.398 1.00 140.70 ? 1537 TRP A CE3   1 
ATOM   27    C  CZ2   . TRP A 1 1537 ? 174.547 239.059 235.477 1.00 139.16 ? 1537 TRP A CZ2   1 
ATOM   28    C  CZ3   . TRP A 1 1537 ? 174.154 237.189 236.955 1.00 136.34 ? 1537 TRP A CZ3   1 
ATOM   29    C  CH2   . TRP A 1 1537 ? 173.843 238.475 236.493 1.00 138.41 ? 1537 TRP A CH2   1 
ATOM   30    N  N     . ILE A 1 1538 ? 180.417 234.941 232.992 1.00 138.04 ? 1538 ILE A N     1 
ATOM   31    C  CA    . ILE A 1 1538 ? 181.574 235.619 232.410 1.00 134.39 ? 1538 ILE A CA    1 
ATOM   32    C  C     . ILE A 1 1538 ? 181.723 235.268 230.932 1.00 136.02 ? 1538 ILE A C     1 
ATOM   33    O  O     . ILE A 1 1538 ? 182.029 236.136 230.102 1.00 132.29 ? 1538 ILE A O     1 
ATOM   34    C  CB    . ILE A 1 1538 ? 182.848 235.296 233.218 1.00 125.12 ? 1538 ILE A CB    1 
ATOM   35    C  CG1   . ILE A 1 1538 ? 184.013 236.179 232.764 1.00 119.75 ? 1538 ILE A CG1   1 
ATOM   36    C  CG2   . ILE A 1 1538 ? 183.201 233.810 233.154 1.00 118.42 ? 1538 ILE A CG2   1 
ATOM   37    C  CD1   . ILE A 1 1538 ? 185.198 236.159 233.705 1.00 106.26 ? 1538 ILE A CD1   1 
ATOM   38    N  N     . ASP A 1 1539 ? 181.500 233.999 230.576 1.00 137.30 ? 1539 ASP A N     1 
ATOM   39    C  CA    . ASP A 1 1539 ? 181.626 233.590 229.180 1.00 134.49 ? 1539 ASP A CA    1 
ATOM   40    C  C     . ASP A 1 1539 ? 180.578 234.275 228.313 1.00 134.44 ? 1539 ASP A C     1 
ATOM   41    O  O     . ASP A 1 1539 ? 180.889 234.796 227.235 1.00 132.18 ? 1539 ASP A O     1 
ATOM   42    C  CB    . ASP A 1 1539 ? 181.508 232.069 229.067 1.00 130.80 ? 1539 ASP A CB    1 
ATOM   43    C  CG    . ASP A 1 1539 ? 182.643 231.343 229.760 1.00 128.88 ? 1539 ASP A CG    1 
ATOM   44    O  OD1   . ASP A 1 1539 ? 183.769 231.882 229.784 1.00 125.14 ? 1539 ASP A OD1   1 
ATOM   45    O  OD2   . ASP A 1 1539 ? 182.409 230.232 230.281 1.00 125.96 ? 1539 ASP A OD2   1 
ATOM   46    N  N     . VAL A 1 1540 ? 179.326 234.292 228.778 1.00 136.58 ? 1540 VAL A N     1 
ATOM   47    C  CA    . VAL A 1 1540 ? 178.260 234.948 228.027 1.00 136.63 ? 1540 VAL A CA    1 
ATOM   48    C  C     . VAL A 1 1540 ? 178.538 236.439 227.907 1.00 137.87 ? 1540 VAL A C     1 
ATOM   49    O  O     . VAL A 1 1540 ? 178.316 237.044 226.852 1.00 138.54 ? 1540 VAL A O     1 
ATOM   50    C  CB    . VAL A 1 1540 ? 176.895 234.678 228.687 1.00 134.63 ? 1540 VAL A CB    1 
ATOM   51    C  CG1   . VAL A 1 1540 ? 175.789 235.416 227.947 1.00 131.63 ? 1540 VAL A CG1   1 
ATOM   52    C  CG2   . VAL A 1 1540 ? 176.611 233.188 228.723 1.00 131.96 ? 1540 VAL A CG2   1 
ATOM   53    N  N     . GLN A 1 1541 ? 179.030 237.054 228.986 1.00 137.66 ? 1541 GLN A N     1 
ATOM   54    C  CA    . GLN A 1 1541 ? 179.341 238.477 228.952 1.00 135.71 ? 1541 GLN A CA    1 
ATOM   55    C  C     . GLN A 1 1541 ? 180.409 238.780 227.908 1.00 137.02 ? 1541 GLN A C     1 
ATOM   56    O  O     . GLN A 1 1541 ? 180.245 239.690 227.087 1.00 137.35 ? 1541 GLN A O     1 
ATOM   57    C  CB    . GLN A 1 1541 ? 179.792 238.946 230.337 1.00 134.35 ? 1541 GLN A CB    1 
ATOM   58    C  CG    . GLN A 1 1541 ? 180.184 240.413 230.401 1.00 128.59 ? 1541 GLN A CG    1 
ATOM   59    C  CD    . GLN A 1 1541 ? 180.517 240.867 231.809 1.00 126.35 ? 1541 GLN A CD    1 
ATOM   60    O  OE1   . GLN A 1 1541 ? 179.654 240.891 232.687 1.00 122.65 ? 1541 GLN A OE1   1 
ATOM   61    N  NE2   . GLN A 1 1541 ? 181.775 241.229 232.032 1.00 123.52 ? 1541 GLN A NE2   1 
ATOM   62    N  N     . ARG A 1 1542 ? 181.506 238.019 227.915 1.00 137.16 ? 1542 ARG A N     1 
ATOM   63    C  CA    . ARG A 1 1542 ? 182.574 238.259 226.948 1.00 136.79 ? 1542 ARG A CA    1 
ATOM   64    C  C     . ARG A 1 1542 ? 182.089 238.026 225.522 1.00 137.01 ? 1542 ARG A C     1 
ATOM   65    O  O     . ARG A 1 1542 ? 182.394 238.815 224.612 1.00 135.05 ? 1542 ARG A O     1 
ATOM   66    C  CB    . ARG A 1 1542 ? 183.777 237.367 227.260 1.00 132.50 ? 1542 ARG A CB    1 
ATOM   67    C  CG    . ARG A 1 1542 ? 184.721 237.162 226.084 1.00 129.18 ? 1542 ARG A CG    1 
ATOM   68    C  CD    . ARG A 1 1542 ? 185.827 236.171 226.415 1.00 130.94 ? 1542 ARG A CD    1 
ATOM   69    N  NE    . ARG A 1 1542 ? 185.330 235.000 227.129 1.00 132.96 ? 1542 ARG A NE    1 
ATOM   70    C  CZ    . ARG A 1 1542 ? 184.738 233.964 226.549 1.00 131.06 ? 1542 ARG A CZ    1 
ATOM   71    N  NH1   . ARG A 1 1542 ? 184.551 233.919 225.240 1.00 129.97 ? 1542 ARG A NH1   1 
ATOM   72    N  NH2   . ARG A 1 1542 ? 184.329 232.946 227.300 1.00 125.91 ? 1542 ARG A NH2   1 
ATOM   73    N  N     . ARG A 1 1543 ? 181.329 236.947 225.307 1.00 136.60 ? 1543 ARG A N     1 
ATOM   74    C  CA    . ARG A 1 1543 ? 180.813 236.652 223.976 1.00 131.61 ? 1543 ARG A CA    1 
ATOM   75    C  C     . ARG A 1 1543 ? 179.927 237.782 223.478 1.00 132.38 ? 1543 ARG A C     1 
ATOM   76    O  O     . ARG A 1 1543 ? 180.065 238.239 222.336 1.00 133.48 ? 1543 ARG A O     1 
ATOM   77    C  CB    . ARG A 1 1543 ? 180.043 235.331 223.992 1.00 127.62 ? 1543 ARG A CB    1 
ATOM   78    C  CG    . ARG A 1 1543 ? 180.911 234.094 224.165 1.00 127.12 ? 1543 ARG A CG    1 
ATOM   79    C  CD    . ARG A 1 1543 ? 180.062 232.877 224.504 1.00 127.87 ? 1543 ARG A CD    1 
ATOM   80    N  NE    . ARG A 1 1543 ? 180.864 231.762 224.992 1.00 125.63 ? 1543 ARG A NE    1 
ATOM   81    C  CZ    . ARG A 1 1543 ? 181.320 230.777 224.230 1.00 122.79 ? 1543 ARG A CZ    1 
ATOM   82    N  NH1   . ARG A 1 1543 ? 181.070 230.735 222.933 1.00 123.15 ? 1543 ARG A NH1   1 
ATOM   83    N  NH2   . ARG A 1 1543 ? 182.044 229.810 224.785 1.00 116.85 ? 1543 ARG A NH2   1 
ATOM   84    N  N     . TRP A 1 1544 ? 179.022 238.264 224.335 1.00 134.63 ? 1544 TRP A N     1 
ATOM   85    C  CA    . TRP A 1 1544 ? 178.133 239.344 223.931 1.00 138.08 ? 1544 TRP A CA    1 
ATOM   86    C  C     . TRP A 1 1544 ? 178.911 240.621 223.656 1.00 136.65 ? 1544 TRP A C     1 
ATOM   87    O  O     . TRP A 1 1544 ? 178.605 241.340 222.702 1.00 134.68 ? 1544 TRP A O     1 
ATOM   88    C  CB    . TRP A 1 1544 ? 177.065 239.587 224.997 1.00 140.75 ? 1544 TRP A CB    1 
ATOM   89    C  CG    . TRP A 1 1544 ? 176.029 240.586 224.569 1.00 142.56 ? 1544 TRP A CG    1 
ATOM   90    C  CD1   . TRP A 1 1544 ? 174.815 240.316 224.008 1.00 140.41 ? 1544 TRP A CD1   1 
ATOM   91    C  CD2   . TRP A 1 1544 ? 176.116 242.015 224.664 1.00 141.36 ? 1544 TRP A CD2   1 
ATOM   92    N  NE1   . TRP A 1 1544 ? 174.143 241.485 223.746 1.00 140.36 ? 1544 TRP A NE1   1 
ATOM   93    C  CE2   . TRP A 1 1544 ? 174.919 242.542 224.139 1.00 139.51 ? 1544 TRP A CE2   1 
ATOM   94    C  CE3   . TRP A 1 1544 ? 177.090 242.900 225.140 1.00 136.62 ? 1544 TRP A CE3   1 
ATOM   95    C  CZ2   . TRP A 1 1544 ? 174.669 243.912 224.080 1.00 133.42 ? 1544 TRP A CZ2   1 
ATOM   96    C  CZ3   . TRP A 1 1544 ? 176.841 244.258 225.079 1.00 133.76 ? 1544 TRP A CZ3   1 
ATOM   97    C  CH2   . TRP A 1 1544 ? 175.639 244.751 224.553 1.00 130.85 ? 1544 TRP A CH2   1 
ATOM   98    N  N     . VAL A 1 1545 ? 179.925 240.920 224.473 1.00 136.07 ? 1545 VAL A N     1 
ATOM   99    C  CA    . VAL A 1 1545 ? 180.701 242.140 224.260 1.00 134.19 ? 1545 VAL A CA    1 
ATOM   100   C  C     . VAL A 1 1545 ? 181.394 242.106 222.904 1.00 134.29 ? 1545 VAL A C     1 
ATOM   101   O  O     . VAL A 1 1545 ? 181.282 243.050 222.109 1.00 129.94 ? 1545 VAL A O     1 
ATOM   102   C  CB    . VAL A 1 1545 ? 181.709 242.357 225.403 1.00 130.40 ? 1545 VAL A CB    1 
ATOM   103   C  CG1   . VAL A 1 1545 ? 182.603 243.543 225.090 1.00 121.97 ? 1545 VAL A CG1   1 
ATOM   104   C  CG2   . VAL A 1 1545 ? 180.976 242.620 226.705 1.00 124.19 ? 1545 VAL A CG2   1 
ATOM   105   N  N     . TYR A 1 1546 ? 182.106 241.013 222.600 1.00 136.22 ? 1546 TYR A N     1 
ATOM   106   C  CA    . TYR A 1 1546 ? 182.847 241.037 221.341 1.00 133.20 ? 1546 TYR A CA    1 
ATOM   107   C  C     . TYR A 1 1546 ? 181.918 240.896 220.140 1.00 131.20 ? 1546 TYR A C     1 
ATOM   108   O  O     . TYR A 1 1546 ? 182.186 241.484 219.084 1.00 127.65 ? 1546 TYR A O     1 
ATOM   109   C  CB    . TYR A 1 1546 ? 183.975 239.989 221.311 1.00 132.95 ? 1546 TYR A CB    1 
ATOM   110   C  CG    . TYR A 1 1546 ? 183.626 238.513 221.398 1.00 132.40 ? 1546 TYR A CG    1 
ATOM   111   C  CD1   . TYR A 1 1546 ? 182.863 237.889 220.420 1.00 131.26 ? 1546 TYR A CD1   1 
ATOM   112   C  CD2   . TYR A 1 1546 ? 184.149 237.723 222.415 1.00 130.54 ? 1546 TYR A CD2   1 
ATOM   113   C  CE1   . TYR A 1 1546 ? 182.574 236.540 220.488 1.00 130.99 ? 1546 TYR A CE1   1 
ATOM   114   C  CE2   . TYR A 1 1546 ? 183.872 236.372 222.488 1.00 130.07 ? 1546 TYR A CE2   1 
ATOM   115   C  CZ    . TYR A 1 1546 ? 183.083 235.787 221.522 1.00 131.14 ? 1546 TYR A CZ    1 
ATOM   116   O  OH    . TYR A 1 1546 ? 182.801 234.441 221.591 1.00 130.52 ? 1546 TYR A OH    1 
ATOM   117   N  N     . LEU A 1 1547 ? 180.799 240.175 220.280 1.00 134.10 ? 1547 LEU A N     1 
ATOM   118   C  CA    . LEU A 1 1547 ? 179.868 240.071 219.161 1.00 132.07 ? 1547 LEU A CA    1 
ATOM   119   C  C     . LEU A 1 1547 ? 179.144 241.389 218.919 1.00 131.91 ? 1547 LEU A C     1 
ATOM   120   O  O     . LEU A 1 1547 ? 178.877 241.750 217.768 1.00 131.29 ? 1547 LEU A O     1 
ATOM   121   C  CB    . LEU A 1 1547 ? 178.874 238.938 219.406 1.00 130.67 ? 1547 LEU A CB    1 
ATOM   122   C  CG    . LEU A 1 1547 ? 179.394 237.549 219.027 1.00 127.85 ? 1547 LEU A CG    1 
ATOM   123   C  CD1   . LEU A 1 1547 ? 178.274 236.531 219.043 1.00 121.14 ? 1547 LEU A CD1   1 
ATOM   124   C  CD2   . LEU A 1 1547 ? 180.074 237.576 217.667 1.00 129.45 ? 1547 LEU A CD2   1 
ATOM   125   N  N     . GLU A 1 1548 ? 178.826 242.128 219.986 1.00 133.13 ? 1548 GLU A N     1 
ATOM   126   C  CA    . GLU A 1 1548 ? 178.245 243.455 219.819 1.00 133.28 ? 1548 GLU A CA    1 
ATOM   127   C  C     . GLU A 1 1548 ? 179.237 244.402 219.165 1.00 133.75 ? 1548 GLU A C     1 
ATOM   128   O  O     . GLU A 1 1548 ? 178.861 245.201 218.300 1.00 130.67 ? 1548 GLU A O     1 
ATOM   129   C  CB    . GLU A 1 1548 ? 177.789 244.004 221.171 1.00 132.20 ? 1548 GLU A CB    1 
ATOM   130   C  CG    . GLU A 1 1548 ? 176.853 245.201 221.068 1.00 127.53 ? 1548 GLU A CG    1 
ATOM   131   C  CD    . GLU A 1 1548 ? 177.591 246.526 221.097 1.00 127.04 ? 1548 GLU A CD    1 
ATOM   132   O  OE1   . GLU A 1 1548 ? 178.790 246.533 221.447 1.00 130.90 ? 1548 GLU A OE1   1 
ATOM   133   O  OE2   . GLU A 1 1548 ? 176.971 247.559 220.769 1.00 119.90 ? 1548 GLU A OE2   1 
ATOM   134   N  N     . GLY A 1 1549 ? 180.509 244.332 219.565 1.00 134.91 ? 1549 GLY A N     1 
ATOM   135   C  CA    . GLY A 1 1549 ? 181.521 245.126 218.891 1.00 134.70 ? 1549 GLY A CA    1 
ATOM   136   C  C     . GLY A 1 1549 ? 181.616 244.804 217.412 1.00 131.72 ? 1549 GLY A C     1 
ATOM   137   O  O     . GLY A 1 1549 ? 181.715 245.704 216.574 1.00 125.06 ? 1549 GLY A O     1 
ATOM   138   N  N     . ILE A 1 1550 ? 181.572 243.513 217.071 1.00 131.34 ? 1550 ILE A N     1 
ATOM   139   C  CA    . ILE A 1 1550 ? 181.632 243.102 215.670 1.00 128.67 ? 1550 ILE A CA    1 
ATOM   140   C  C     . ILE A 1 1550 ? 180.421 243.623 214.903 1.00 129.52 ? 1550 ILE A C     1 
ATOM   141   O  O     . ILE A 1 1550 ? 180.550 244.177 213.804 1.00 126.72 ? 1550 ILE A O     1 
ATOM   142   C  CB    . ILE A 1 1550 ? 181.750 241.570 215.569 1.00 128.36 ? 1550 ILE A CB    1 
ATOM   143   C  CG1   . ILE A 1 1550 ? 183.190 241.128 215.837 1.00 122.60 ? 1550 ILE A CG1   1 
ATOM   144   C  CG2   . ILE A 1 1550 ? 181.266 241.078 214.212 1.00 122.34 ? 1550 ILE A CG2   1 
ATOM   145   C  CD1   . ILE A 1 1550 ? 183.338 239.642 216.086 1.00 111.88 ? 1550 ILE A CD1   1 
ATOM   146   N  N     . PHE A 1 1551 ? 179.224 243.460 215.474 1.00 130.17 ? 1551 PHE A N     1 
ATOM   147   C  CA    . PHE A 1 1551 ? 178.001 243.827 214.768 1.00 126.93 ? 1551 PHE A CA    1 
ATOM   148   C  C     . PHE A 1 1551 ? 177.782 245.333 214.713 1.00 126.01 ? 1551 PHE A C     1 
ATOM   149   O  O     . PHE A 1 1551 ? 177.036 245.804 213.847 1.00 122.71 ? 1551 PHE A O     1 
ATOM   150   C  CB    . PHE A 1 1551 ? 176.794 243.151 215.424 1.00 127.13 ? 1551 PHE A CB    1 
ATOM   151   C  CG    . PHE A 1 1551 ? 176.501 241.779 214.886 1.00 130.83 ? 1551 PHE A CG    1 
ATOM   152   C  CD1   . PHE A 1 1551 ? 175.846 241.620 213.677 1.00 129.64 ? 1551 PHE A CD1   1 
ATOM   153   C  CD2   . PHE A 1 1551 ? 176.878 240.648 215.591 1.00 135.23 ? 1551 PHE A CD2   1 
ATOM   154   C  CE1   . PHE A 1 1551 ? 175.574 240.359 213.178 1.00 129.08 ? 1551 PHE A CE1   1 
ATOM   155   C  CE2   . PHE A 1 1551 ? 176.608 239.383 215.099 1.00 134.77 ? 1551 PHE A CE2   1 
ATOM   156   C  CZ    . PHE A 1 1551 ? 175.956 239.239 213.891 1.00 129.31 ? 1551 PHE A CZ    1 
ATOM   157   N  N     . THR A 1 1552 ? 178.403 246.098 215.609 1.00 127.63 ? 1552 THR A N     1 
ATOM   158   C  CA    . THR A 1 1552 ? 178.258 247.548 215.624 1.00 126.84 ? 1552 THR A CA    1 
ATOM   159   C  C     . THR A 1 1552 ? 179.333 248.259 214.816 1.00 125.48 ? 1552 THR A C     1 
ATOM   160   O  O     . THR A 1 1552 ? 179.033 249.242 214.130 1.00 120.16 ? 1552 THR A O     1 
ATOM   161   C  CB    . THR A 1 1552 ? 178.279 248.068 217.066 1.00 127.59 ? 1552 THR A CB    1 
ATOM   162   O  OG1   . THR A 1 1552 ? 177.459 247.229 217.890 1.00 127.01 ? 1552 THR A OG1   1 
ATOM   163   C  CG2   . THR A 1 1552 ? 177.757 249.496 217.128 1.00 120.46 ? 1552 THR A CG2   1 
ATOM   164   N  N     . GLY A 1 1553 ? 180.581 247.790 214.881 1.00 125.22 ? 1553 GLY A N     1 
ATOM   165   C  CA    . GLY A 1 1553 ? 181.616 248.369 214.039 1.00 121.81 ? 1553 GLY A CA    1 
ATOM   166   C  C     . GLY A 1 1553 ? 181.335 248.163 212.564 1.00 122.18 ? 1553 GLY A C     1 
ATOM   167   O  O     . GLY A 1 1553 ? 181.642 249.026 211.736 1.00 116.49 ? 1553 GLY A O     1 
ATOM   168   N  N     . SER A 1 1554 ? 180.749 247.022 212.216 1.00 125.73 ? 1554 SER A N     1 
ATOM   169   C  CA    . SER A 1 1554 ? 180.353 246.716 210.843 1.00 122.22 ? 1554 SER A CA    1 
ATOM   170   C  C     . SER A 1 1554 ? 178.847 246.940 210.739 1.00 124.44 ? 1554 SER A C     1 
ATOM   171   O  O     . SER A 1 1554 ? 178.046 246.047 211.016 1.00 124.21 ? 1554 SER A O     1 
ATOM   172   C  CB    . SER A 1 1554 ? 180.742 245.291 210.471 1.00 119.71 ? 1554 SER A CB    1 
ATOM   173   O  OG    . SER A 1 1554 ? 180.333 244.373 211.472 1.00 125.18 ? 1554 SER A OG    1 
ATOM   174   N  N     . ALA A 1 1555 ? 178.462 248.153 210.341 1.00 124.63 ? 1555 ALA A N     1 
ATOM   175   C  CA    . ALA A 1 1555 ? 177.050 248.475 210.179 1.00 121.01 ? 1555 ALA A CA    1 
ATOM   176   C  C     . ALA A 1 1555 ? 176.435 247.827 208.945 1.00 120.76 ? 1555 ALA A C     1 
ATOM   177   O  O     . ALA A 1 1555 ? 175.206 247.736 208.863 1.00 120.25 ? 1555 ALA A O     1 
ATOM   178   C  CB    . ALA A 1 1555 ? 176.860 249.992 210.112 1.00 109.33 ? 1555 ALA A CB    1 
ATOM   179   N  N     . ASP A 1 1556 ? 177.253 247.380 207.995 1.00 116.83 ? 1556 ASP A N     1 
ATOM   180   C  CA    . ASP A 1 1556 ? 176.772 246.730 206.784 1.00 116.73 ? 1556 ASP A CA    1 
ATOM   181   C  C     . ASP A 1 1556 ? 176.800 245.211 206.876 1.00 117.40 ? 1556 ASP A C     1 
ATOM   182   O  O     . ASP A 1 1556 ? 176.481 244.538 205.891 1.00 114.61 ? 1556 ASP A O     1 
ATOM   183   C  CB    . ASP A 1 1556 ? 177.599 247.190 205.580 1.00 114.45 ? 1556 ASP A CB    1 
ATOM   184   C  CG    . ASP A 1 1556 ? 177.361 248.646 205.234 1.00 111.43 ? 1556 ASP A CG    1 
ATOM   185   O  OD1   . ASP A 1 1556 ? 176.246 249.146 205.493 1.00 111.60 ? 1556 ASP A OD1   1 
ATOM   186   O  OD2   . ASP A 1 1556 ? 178.291 249.293 204.707 1.00 102.33 ? 1556 ASP A OD2   1 
ATOM   187   N  N     . ILE A 1 1557 ? 177.172 244.653 208.032 1.00 117.59 ? 1557 ILE A N     1 
ATOM   188   C  CA    . ILE A 1 1557 ? 177.234 243.204 208.180 1.00 116.44 ? 1557 ILE A CA    1 
ATOM   189   C  C     . ILE A 1 1557 ? 175.845 242.581 208.207 1.00 119.00 ? 1557 ILE A C     1 
ATOM   190   O  O     . ILE A 1 1557 ? 175.709 241.368 208.006 1.00 117.63 ? 1557 ILE A O     1 
ATOM   191   C  CB    . ILE A 1 1557 ? 178.026 242.831 209.448 1.00 116.61 ? 1557 ILE A CB    1 
ATOM   192   C  CG1   . ILE A 1 1557 ? 178.577 241.408 209.341 1.00 114.07 ? 1557 ILE A CG1   1 
ATOM   193   C  CG2   . ILE A 1 1557 ? 177.154 242.967 210.685 1.00 119.67 ? 1557 ILE A CG2   1 
ATOM   194   C  CD1   . ILE A 1 1557 ? 179.587 241.065 210.413 1.00 112.93 ? 1557 ILE A CD1   1 
ATOM   195   N  N     . LYS A 1 1558 ? 174.803 243.380 208.452 1.00 121.48 ? 1558 LYS A N     1 
ATOM   196   C  CA    . LYS A 1 1558 ? 173.451 242.837 208.500 1.00 123.69 ? 1558 LYS A CA    1 
ATOM   197   C  C     . LYS A 1 1558 ? 172.942 242.461 207.115 1.00 123.07 ? 1558 LYS A C     1 
ATOM   198   O  O     . LYS A 1 1558 ? 172.162 241.510 206.982 1.00 120.34 ? 1558 LYS A O     1 
ATOM   199   C  CB    . LYS A 1 1558 ? 172.505 243.842 209.156 1.00 119.82 ? 1558 LYS A CB    1 
ATOM   200   C  CG    . LYS A 1 1558 ? 172.631 245.261 208.623 1.00 113.73 ? 1558 LYS A CG    1 
ATOM   201   C  CD    . LYS A 1 1558 ? 171.830 246.239 209.466 1.00 110.79 ? 1558 LYS A CD    1 
ATOM   202   C  CE    . LYS A 1 1558 ? 170.424 245.719 209.733 1.00 108.00 ? 1558 LYS A CE    1 
ATOM   203   N  NZ    . LYS A 1 1558 ? 169.670 246.599 210.668 1.00 93.96  ? 1558 LYS A NZ    1 
ATOM   204   N  N     . HIS A 1 1559 ? 173.367 243.188 206.080 1.00 123.73 ? 1559 HIS A N     1 
ATOM   205   C  CA    . HIS A 1 1559 ? 172.887 242.922 204.729 1.00 123.22 ? 1559 HIS A CA    1 
ATOM   206   C  C     . HIS A 1 1559 ? 173.320 241.555 204.217 1.00 124.75 ? 1559 HIS A C     1 
ATOM   207   O  O     . HIS A 1 1559 ? 172.628 240.977 203.372 1.00 125.48 ? 1559 HIS A O     1 
ATOM   208   C  CB    . HIS A 1 1559 ? 173.372 244.018 203.782 1.00 120.01 ? 1559 HIS A CB    1 
ATOM   209   C  CG    . HIS A 1 1559 ? 173.190 245.404 204.320 1.00 121.19 ? 1559 HIS A CG    1 
ATOM   210   N  ND1   . HIS A 1 1559 ? 171.986 245.856 204.815 1.00 117.92 ? 1559 HIS A ND1   1 
ATOM   211   C  CD2   . HIS A 1 1559 ? 174.059 246.435 204.445 1.00 121.17 ? 1559 HIS A CD2   1 
ATOM   212   C  CE1   . HIS A 1 1559 ? 172.120 247.107 205.220 1.00 114.70 ? 1559 HIS A CE1   1 
ATOM   213   N  NE2   . HIS A 1 1559 ? 173.368 247.481 205.007 1.00 118.65 ? 1559 HIS A NE2   1 
ATOM   214   N  N     . LEU A 1 1560 ? 174.442 241.026 204.706 1.00 123.29 ? 1560 LEU A N     1 
ATOM   215   C  CA    . LEU A 1 1560 ? 174.897 239.697 204.331 1.00 120.14 ? 1560 LEU A CA    1 
ATOM   216   C  C     . LEU A 1 1560 ? 174.547 238.632 205.358 1.00 121.33 ? 1560 LEU A C     1 
ATOM   217   O  O     . LEU A 1 1560 ? 174.601 237.441 205.031 1.00 117.84 ? 1560 LEU A O     1 
ATOM   218   C  CB    . LEU A 1 1560 ? 176.417 239.699 204.105 1.00 112.58 ? 1560 LEU A CB    1 
ATOM   219   C  CG    . LEU A 1 1560 ? 176.970 238.639 203.148 1.00 110.44 ? 1560 LEU A CG    1 
ATOM   220   C  CD1   . LEU A 1 1560 ? 176.095 238.515 201.909 1.00 104.41 ? 1560 LEU A CD1   1 
ATOM   221   C  CD2   . LEU A 1 1560 ? 178.407 238.954 202.763 1.00 104.23 ? 1560 LEU A CD2   1 
ATOM   222   N  N     . LEU A 1 1561 ? 174.169 239.022 206.573 1.00 125.07 ? 1561 LEU A N     1 
ATOM   223   C  CA    . LEU A 1 1561 ? 173.883 238.085 207.661 1.00 122.55 ? 1561 LEU A CA    1 
ATOM   224   C  C     . LEU A 1 1561 ? 172.521 238.402 208.271 1.00 123.65 ? 1561 LEU A C     1 
ATOM   225   O  O     . LEU A 1 1561 ? 172.424 238.780 209.442 1.00 122.87 ? 1561 LEU A O     1 
ATOM   226   C  CB    . LEU A 1 1561 ? 174.981 238.155 208.722 1.00 119.87 ? 1561 LEU A CB    1 
ATOM   227   C  CG    . LEU A 1 1561 ? 176.437 237.879 208.340 1.00 110.92 ? 1561 LEU A CG    1 
ATOM   228   C  CD1   . LEU A 1 1561 ? 177.272 237.648 209.589 1.00 103.70 ? 1561 LEU A CD1   1 
ATOM   229   C  CD2   . LEU A 1 1561 ? 176.542 236.688 207.411 1.00 109.68 ? 1561 LEU A CD2   1 
ATOM   230   N  N     . PRO A 1 1562 ? 171.435 238.241 207.503 1.00 125.19 ? 1562 PRO A N     1 
ATOM   231   C  CA    . PRO A 1 1562 ? 170.127 238.739 207.960 1.00 123.19 ? 1562 PRO A CA    1 
ATOM   232   C  C     . PRO A 1 1562 ? 169.519 237.984 209.137 1.00 120.84 ? 1562 PRO A C     1 
ATOM   233   O  O     . PRO A 1 1562 ? 169.127 238.602 210.135 1.00 121.13 ? 1562 PRO A O     1 
ATOM   234   C  CB    . PRO A 1 1562 ? 169.250 238.604 206.708 1.00 123.81 ? 1562 PRO A CB    1 
ATOM   235   C  CG    . PRO A 1 1562 ? 169.871 237.501 205.925 1.00 119.15 ? 1562 PRO A CG    1 
ATOM   236   C  CD    . PRO A 1 1562 ? 171.345 237.524 206.218 1.00 120.15 ? 1562 PRO A CD    1 
ATOM   237   N  N     . VAL A 1 1563 ? 169.420 236.656 209.032 1.00 121.78 ? 1563 VAL A N     1 
ATOM   238   C  CA    . VAL A 1 1563 ? 168.727 235.887 210.062 1.00 122.63 ? 1563 VAL A CA    1 
ATOM   239   C  C     . VAL A 1 1563 ? 169.477 235.962 211.388 1.00 121.37 ? 1563 VAL A C     1 
ATOM   240   O  O     . VAL A 1 1563 ? 168.869 236.146 212.453 1.00 119.68 ? 1563 VAL A O     1 
ATOM   241   C  CB    . VAL A 1 1563 ? 168.497 234.436 209.593 1.00 113.26 ? 1563 VAL A CB    1 
ATOM   242   C  CG1   . VAL A 1 1563 ? 169.812 233.696 209.383 1.00 105.86 ? 1563 VAL A CG1   1 
ATOM   243   C  CG2   . VAL A 1 1563 ? 167.617 233.692 210.587 1.00 110.67 ? 1563 VAL A CG2   1 
ATOM   244   N  N     . GLU A 1 1564 ? 170.805 235.849 211.352 1.00 119.96 ? 1564 GLU A N     1 
ATOM   245   C  CA    . GLU A 1 1564 ? 171.567 236.020 212.579 1.00 117.59 ? 1564 GLU A CA    1 
ATOM   246   C  C     . GLU A 1 1564 ? 171.582 237.470 213.040 1.00 119.68 ? 1564 GLU A C     1 
ATOM   247   O  O     . GLU A 1 1564 ? 171.765 237.716 214.232 1.00 119.05 ? 1564 GLU A O     1 
ATOM   248   C  CB    . GLU A 1 1564 ? 172.993 235.493 212.408 1.00 119.46 ? 1564 GLU A CB    1 
ATOM   249   C  CG    . GLU A 1 1564 ? 173.772 236.124 211.279 1.00 122.38 ? 1564 GLU A CG    1 
ATOM   250   C  CD    . GLU A 1 1564 ? 173.909 235.197 210.089 1.00 120.70 ? 1564 GLU A CD    1 
ATOM   251   O  OE1   . GLU A 1 1564 ? 172.878 234.677 209.615 1.00 119.82 ? 1564 GLU A OE1   1 
ATOM   252   O  OE2   . GLU A 1 1564 ? 175.051 234.977 209.636 1.00 118.20 ? 1564 GLU A OE2   1 
ATOM   253   N  N     . THR A 1 1565 ? 171.366 238.432 212.138 1.00 123.93 ? 1565 THR A N     1 
ATOM   254   C  CA    . THR A 1 1565 ? 171.181 239.812 212.583 1.00 123.27 ? 1565 THR A CA    1 
ATOM   255   C  C     . THR A 1 1565 ? 169.910 239.957 213.409 1.00 123.09 ? 1565 THR A C     1 
ATOM   256   O  O     . THR A 1 1565 ? 169.914 240.619 214.452 1.00 123.12 ? 1565 THR A O     1 
ATOM   257   C  CB    . THR A 1 1565 ? 171.148 240.764 211.387 1.00 121.17 ? 1565 THR A CB    1 
ATOM   258   O  OG1   . THR A 1 1565 ? 172.447 240.817 210.784 1.00 122.51 ? 1565 THR A OG1   1 
ATOM   259   C  CG2   . THR A 1 1565 ? 170.743 242.164 211.827 1.00 115.29 ? 1565 THR A CG2   1 
ATOM   260   N  N     . GLN A 1 1566 ? 168.811 239.341 212.966 1.00 123.36 ? 1566 GLN A N     1 
ATOM   261   C  CA    . GLN A 1 1566 ? 167.585 239.369 213.761 1.00 119.74 ? 1566 GLN A CA    1 
ATOM   262   C  C     . GLN A 1 1566 ? 167.772 238.632 215.083 1.00 121.64 ? 1566 GLN A C     1 
ATOM   263   O  O     . GLN A 1 1566 ? 167.310 239.094 216.138 1.00 120.95 ? 1566 GLN A O     1 
ATOM   264   C  CB    . GLN A 1 1566 ? 166.426 238.765 212.969 1.00 117.60 ? 1566 GLN A CB    1 
ATOM   265   C  CG    . GLN A 1 1566 ? 166.339 239.240 211.528 1.00 121.38 ? 1566 GLN A CG    1 
ATOM   266   C  CD    . GLN A 1 1566 ? 166.295 240.750 211.414 1.00 119.54 ? 1566 GLN A CD    1 
ATOM   267   O  OE1   . GLN A 1 1566 ? 167.176 241.365 210.814 1.00 110.94 ? 1566 GLN A OE1   1 
ATOM   268   N  NE2   . GLN A 1 1566 ? 165.266 241.358 211.993 1.00 116.61 ? 1566 GLN A NE2   1 
ATOM   269   N  N     . ARG A 1 1567 ? 168.451 237.483 215.046 1.00 121.82 ? 1567 ARG A N     1 
ATOM   270   C  CA    . ARG A 1 1567 ? 168.717 236.744 216.277 1.00 119.83 ? 1567 ARG A CA    1 
ATOM   271   C  C     . ARG A 1 1567 ? 169.560 237.570 217.243 1.00 121.70 ? 1567 ARG A C     1 
ATOM   272   O  O     . ARG A 1 1567 ? 169.302 237.579 218.451 1.00 122.68 ? 1567 ARG A O     1 
ATOM   273   C  CB    . ARG A 1 1567 ? 169.405 235.418 215.955 1.00 115.20 ? 1567 ARG A CB    1 
ATOM   274   C  CG    . ARG A 1 1567 ? 168.543 234.452 215.161 1.00 109.55 ? 1567 ARG A CG    1 
ATOM   275   C  CD    . ARG A 1 1567 ? 169.311 233.191 214.800 1.00 110.28 ? 1567 ARG A CD    1 
ATOM   276   N  NE    . ARG A 1 1567 ? 168.629 232.405 213.778 1.00 115.87 ? 1567 ARG A NE    1 
ATOM   277   C  CZ    . ARG A 1 1567 ? 167.578 231.629 214.005 1.00 117.30 ? 1567 ARG A CZ    1 
ATOM   278   N  NH1   . ARG A 1 1567 ? 167.058 231.503 215.215 1.00 118.08 ? 1567 ARG A NH1   1 
ATOM   279   N  NH2   . ARG A 1 1567 ? 167.035 230.960 212.992 1.00 109.90 ? 1567 ARG A NH2   1 
ATOM   280   N  N     . PHE A 1 1568 ? 170.564 238.281 216.728 1.00 122.63 ? 1568 PHE A N     1 
ATOM   281   C  CA    . PHE A 1 1568 ? 171.395 239.111 217.588 1.00 125.64 ? 1568 PHE A CA    1 
ATOM   282   C  C     . PHE A 1 1568 ? 170.645 240.339 218.079 1.00 128.76 ? 1568 PHE A C     1 
ATOM   283   O  O     . PHE A 1 1568 ? 170.944 240.846 219.162 1.00 131.96 ? 1568 PHE A O     1 
ATOM   284   C  CB    . PHE A 1 1568 ? 172.670 239.530 216.860 1.00 128.13 ? 1568 PHE A CB    1 
ATOM   285   C  CG    . PHE A 1 1568 ? 173.693 240.156 217.759 1.00 132.97 ? 1568 PHE A CG    1 
ATOM   286   C  CD1   . PHE A 1 1568 ? 174.284 239.416 218.770 1.00 133.13 ? 1568 PHE A CD1   1 
ATOM   287   C  CD2   . PHE A 1 1568 ? 174.052 241.484 217.608 1.00 131.01 ? 1568 PHE A CD2   1 
ATOM   288   C  CE1   . PHE A 1 1568 ? 175.222 239.985 219.606 1.00 131.66 ? 1568 PHE A CE1   1 
ATOM   289   C  CE2   . PHE A 1 1568 ? 174.991 242.059 218.443 1.00 128.38 ? 1568 PHE A CE2   1 
ATOM   290   C  CZ    . PHE A 1 1568 ? 175.575 241.306 219.444 1.00 131.96 ? 1568 PHE A CZ    1 
ATOM   291   N  N     . GLN A 1 1569 ? 169.682 240.840 217.305 1.00 125.01 ? 1569 GLN A N     1 
ATOM   292   C  CA    . GLN A 1 1569 ? 168.819 241.903 217.812 1.00 123.97 ? 1569 GLN A CA    1 
ATOM   293   C  C     . GLN A 1 1569 ? 168.001 241.414 219.000 1.00 125.40 ? 1569 GLN A C     1 
ATOM   294   O  O     . GLN A 1 1569 ? 167.863 242.119 220.008 1.00 123.87 ? 1569 GLN A O     1 
ATOM   295   C  CB    . GLN A 1 1569 ? 167.903 242.414 216.700 1.00 117.58 ? 1569 GLN A CB    1 
ATOM   296   C  CG    . GLN A 1 1569 ? 166.937 243.498 217.146 1.00 118.99 ? 1569 GLN A CG    1 
ATOM   297   C  CD    . GLN A 1 1569 ? 167.638 244.661 217.818 1.00 117.42 ? 1569 GLN A CD    1 
ATOM   298   O  OE1   . GLN A 1 1569 ? 167.297 245.044 218.937 1.00 116.62 ? 1569 GLN A OE1   1 
ATOM   299   N  NE2   . GLN A 1 1569 ? 168.624 245.232 217.136 1.00 112.26 ? 1569 GLN A NE2   1 
ATOM   300   N  N     . SER A 1 1570 ? 167.461 240.197 218.900 1.00 125.03 ? 1570 SER A N     1 
ATOM   301   C  CA    . SER A 1 1570 ? 166.761 239.607 220.038 1.00 122.34 ? 1570 SER A CA    1 
ATOM   302   C  C     . SER A 1 1570 ? 167.700 239.423 221.227 1.00 127.61 ? 1570 SER A C     1 
ATOM   303   O  O     . SER A 1 1570 ? 167.323 239.680 222.379 1.00 127.94 ? 1570 SER A O     1 
ATOM   304   C  CB    . SER A 1 1570 ? 166.136 238.272 219.633 1.00 116.78 ? 1570 SER A CB    1 
ATOM   305   O  OG    . SER A 1 1570 ? 165.278 238.430 218.517 1.00 113.96 ? 1570 SER A OG    1 
ATOM   306   N  N     . ILE A 1 1571 ? 168.931 238.977 220.963 1.00 129.48 ? 1571 ILE A N     1 
ATOM   307   C  CA    . ILE A 1 1571 ? 169.913 238.795 222.029 1.00 130.48 ? 1571 ILE A CA    1 
ATOM   308   C  C     . ILE A 1 1571 ? 170.241 240.128 222.693 1.00 134.65 ? 1571 ILE A C     1 
ATOM   309   O  O     . ILE A 1 1571 ? 170.386 240.210 223.917 1.00 135.78 ? 1571 ILE A O     1 
ATOM   310   C  CB    . ILE A 1 1571 ? 171.179 238.110 221.478 1.00 130.69 ? 1571 ILE A CB    1 
ATOM   311   C  CG1   . ILE A 1 1571 ? 170.876 236.667 221.077 1.00 126.32 ? 1571 ILE A CG1   1 
ATOM   312   C  CG2   . ILE A 1 1571 ? 172.302 238.145 222.505 1.00 130.23 ? 1571 ILE A CG2   1 
ATOM   313   C  CD1   . ILE A 1 1571 ? 172.065 235.938 220.489 1.00 121.76 ? 1571 ILE A CD1   1 
ATOM   314   N  N     . SER A 1 1572 ? 170.373 241.190 221.895 1.00 133.34 ? 1572 SER A N     1 
ATOM   315   C  CA    . SER A 1 1572 ? 170.659 242.512 222.442 1.00 132.90 ? 1572 SER A CA    1 
ATOM   316   C  C     . SER A 1 1572 ? 169.494 243.030 223.274 1.00 133.44 ? 1572 SER A C     1 
ATOM   317   O  O     . SER A 1 1572 ? 169.703 243.674 224.307 1.00 132.87 ? 1572 SER A O     1 
ATOM   318   C  CB    . SER A 1 1572 ? 170.986 243.488 221.311 1.00 127.53 ? 1572 SER A CB    1 
ATOM   319   O  OG    . SER A 1 1572 ? 172.137 243.074 220.595 1.00 127.11 ? 1572 SER A OG    1 
ATOM   320   N  N     . THR A 1 1573 ? 168.260 242.773 222.832 1.00 133.43 ? 1573 THR A N     1 
ATOM   321   C  CA    . THR A 1 1573 ? 167.103 243.142 223.644 1.00 131.39 ? 1573 THR A CA    1 
ATOM   322   C  C     . THR A 1 1573 ? 167.112 242.401 224.977 1.00 135.76 ? 1573 THR A C     1 
ATOM   323   O  O     . THR A 1 1573 ? 166.844 242.993 226.031 1.00 134.02 ? 1573 THR A O     1 
ATOM   324   C  CB    . THR A 1 1573 ? 165.809 242.856 222.880 1.00 125.65 ? 1573 THR A CB    1 
ATOM   325   O  OG1   . THR A 1 1573 ? 165.917 243.369 221.546 1.00 123.70 ? 1573 THR A OG1   1 
ATOM   326   C  CG2   . THR A 1 1573 ? 164.626 243.511 223.575 1.00 118.23 ? 1573 THR A CG2   1 
ATOM   327   N  N     . GLU A 1 1574 ? 167.433 241.105 224.949 1.00 137.05 ? 1574 GLU A N     1 
ATOM   328   C  CA    . GLU A 1 1574 ? 167.549 240.348 226.192 1.00 134.75 ? 1574 GLU A CA    1 
ATOM   329   C  C     . GLU A 1 1574 ? 168.647 240.918 227.084 1.00 136.39 ? 1574 GLU A C     1 
ATOM   330   O  O     . GLU A 1 1574 ? 168.471 241.035 228.302 1.00 135.05 ? 1574 GLU A O     1 
ATOM   331   C  CB    . GLU A 1 1574 ? 167.820 238.875 225.886 1.00 127.63 ? 1574 GLU A CB    1 
ATOM   332   C  CG    . GLU A 1 1574 ? 166.640 238.138 225.279 1.00 124.63 ? 1574 GLU A CG    1 
ATOM   333   C  CD    . GLU A 1 1574 ? 165.665 237.640 226.327 1.00 121.03 ? 1574 GLU A CD    1 
ATOM   334   O  OE1   . GLU A 1 1574 ? 165.992 236.655 227.021 1.00 118.94 ? 1574 GLU A OE1   1 
ATOM   335   O  OE2   . GLU A 1 1574 ? 164.576 238.234 226.457 1.00 118.58 ? 1574 GLU A OE2   1 
ATOM   336   N  N     . PHE A 1 1575 ? 169.789 241.271 226.494 1.00 137.15 ? 1575 PHE A N     1 
ATOM   337   C  CA    . PHE A 1 1575 ? 170.899 241.828 227.258 1.00 135.80 ? 1575 PHE A CA    1 
ATOM   338   C  C     . PHE A 1 1575 ? 170.514 243.154 227.900 1.00 134.92 ? 1575 PHE A C     1 
ATOM   339   O  O     . PHE A 1 1575 ? 170.875 243.424 229.053 1.00 135.05 ? 1575 PHE A O     1 
ATOM   340   C  CB    . PHE A 1 1575 ? 172.111 241.994 226.342 1.00 134.46 ? 1575 PHE A CB    1 
ATOM   341   C  CG    . PHE A 1 1575 ? 173.429 241.935 227.054 1.00 137.88 ? 1575 PHE A CG    1 
ATOM   342   C  CD1   . PHE A 1 1575 ? 174.046 240.718 227.295 1.00 137.55 ? 1575 PHE A CD1   1 
ATOM   343   C  CD2   . PHE A 1 1575 ? 174.070 243.096 227.449 1.00 135.75 ? 1575 PHE A CD2   1 
ATOM   344   C  CE1   . PHE A 1 1575 ? 175.265 240.660 227.942 1.00 134.50 ? 1575 PHE A CE1   1 
ATOM   345   C  CE2   . PHE A 1 1575 ? 175.290 243.043 228.090 1.00 133.34 ? 1575 PHE A CE2   1 
ATOM   346   C  CZ    . PHE A 1 1575 ? 175.887 241.824 228.340 1.00 133.31 ? 1575 PHE A CZ    1 
ATOM   347   N  N     . LEU A 1 1576 ? 169.781 243.993 227.167 1.00 135.14 ? 1576 LEU A N     1 
ATOM   348   C  CA    . LEU A 1 1576 ? 169.269 245.233 227.742 1.00 134.32 ? 1576 LEU A CA    1 
ATOM   349   C  C     . LEU A 1 1576 ? 168.307 244.947 228.887 1.00 133.29 ? 1576 LEU A C     1 
ATOM   350   O  O     . LEU A 1 1576 ? 168.302 245.661 229.895 1.00 128.35 ? 1576 LEU A O     1 
ATOM   351   C  CB    . LEU A 1 1576 ? 168.585 246.073 226.663 1.00 130.39 ? 1576 LEU A CB    1 
ATOM   352   C  CG    . LEU A 1 1576 ? 169.476 246.649 225.560 1.00 126.80 ? 1576 LEU A CG    1 
ATOM   353   C  CD1   . LEU A 1 1576 ? 168.767 247.787 224.841 1.00 116.28 ? 1576 LEU A CD1   1 
ATOM   354   C  CD2   . LEU A 1 1576 ? 170.810 247.117 226.125 1.00 121.95 ? 1576 LEU A CD2   1 
ATOM   355   N  N     . ALA A 1 1577 ? 167.480 243.907 228.747 1.00 136.26 ? 1577 ALA A N     1 
ATOM   356   C  CA    . ALA A 1 1577 ? 166.583 243.531 229.837 1.00 134.31 ? 1577 ALA A CA    1 
ATOM   357   C  C     . ALA A 1 1577 ? 167.364 243.124 231.084 1.00 134.85 ? 1577 ALA A C     1 
ATOM   358   O  O     . ALA A 1 1577 ? 167.035 243.548 232.199 1.00 132.84 ? 1577 ALA A O     1 
ATOM   359   C  CB    . ALA A 1 1577 ? 165.656 242.401 229.391 1.00 125.35 ? 1577 ALA A CB    1 
ATOM   360   N  N     . LEU A 1 1578 ? 168.405 242.306 230.913 1.00 134.99 ? 1578 LEU A N     1 
ATOM   361   C  CA    . LEU A 1 1578 ? 169.235 241.925 232.057 1.00 132.07 ? 1578 LEU A CA    1 
ATOM   362   C  C     . LEU A 1 1578 ? 169.907 243.138 232.689 1.00 133.97 ? 1578 LEU A C     1 
ATOM   363   O  O     . LEU A 1 1578 ? 169.947 243.262 233.917 1.00 132.28 ? 1578 LEU A O     1 
ATOM   364   C  CB    . LEU A 1 1578 ? 170.281 240.876 231.662 1.00 125.75 ? 1578 LEU A CB    1 
ATOM   365   C  CG    . LEU A 1 1578 ? 169.898 239.390 231.593 1.00 121.03 ? 1578 LEU A CG    1 
ATOM   366   C  CD1   . LEU A 1 1578 ? 169.005 239.026 230.425 1.00 123.90 ? 1578 LEU A CD1   1 
ATOM   367   C  CD2   . LEU A 1 1578 ? 171.160 238.532 231.584 1.00 105.23 ? 1578 LEU A CD2   1 
ATOM   368   N  N     . MET A 1 1579 ? 170.445 244.045 231.872 1.00 136.24 ? 1579 MET A N     1 
ATOM   369   C  CA    . MET A 1 1579 ? 171.092 245.230 232.433 1.00 134.84 ? 1579 MET A CA    1 
ATOM   370   C  C     . MET A 1 1579 ? 170.096 246.138 233.147 1.00 130.50 ? 1579 MET A C     1 
ATOM   371   O  O     . MET A 1 1579 ? 170.448 246.802 234.128 1.00 126.01 ? 1579 MET A O     1 
ATOM   372   C  CB    . MET A 1 1579 ? 171.854 245.993 231.349 1.00 131.78 ? 1579 MET A CB    1 
ATOM   373   C  CG    . MET A 1 1579 ? 173.025 245.213 230.788 1.00 134.31 ? 1579 MET A CG    1 
ATOM   374   S  SD    . MET A 1 1579 ? 174.220 244.963 232.122 1.00 131.63 ? 1579 MET A SD    1 
ATOM   375   C  CE    . MET A 1 1579 ? 175.399 243.850 231.371 1.00 119.81 ? 1579 MET A CE    1 
ATOM   376   N  N     . LYS A 1 1580 ? 168.852 246.185 232.673 1.00 130.31 ? 1580 LYS A N     1 
ATOM   377   C  CA    . LYS A 1 1580 ? 167.844 246.979 233.367 1.00 126.04 ? 1580 LYS A CA    1 
ATOM   378   C  C     . LYS A 1 1580 ? 167.311 246.295 234.619 1.00 129.67 ? 1580 LYS A C     1 
ATOM   379   O  O     . LYS A 1 1580 ? 166.778 246.983 235.497 1.00 127.29 ? 1580 LYS A O     1 
ATOM   380   C  CB    . LYS A 1 1580 ? 166.688 247.306 232.420 1.00 118.64 ? 1580 LYS A CB    1 
ATOM   381   C  CG    . LYS A 1 1580 ? 165.957 248.599 232.758 1.00 110.59 ? 1580 LYS A CG    1 
ATOM   382   C  CD    . LYS A 1 1580 ? 166.907 249.790 232.812 1.00 105.59 ? 1580 LYS A CD    1 
ATOM   383   C  CE    . LYS A 1 1580 ? 167.607 250.019 231.480 1.00 100.09 ? 1580 LYS A CE    1 
ATOM   384   N  NZ    . LYS A 1 1580 ? 168.537 251.181 231.536 1.00 75.20  ? 1580 LYS A NZ    1 
ATOM   385   N  N     . LYS A 1 1581 ? 167.440 244.974 234.728 1.00 133.86 ? 1581 LYS A N     1 
ATOM   386   C  CA    . LYS A 1 1581 ? 166.930 244.253 235.890 1.00 131.81 ? 1581 LYS A CA    1 
ATOM   387   C  C     . LYS A 1 1581 ? 167.964 244.081 236.999 1.00 134.49 ? 1581 LYS A C     1 
ATOM   388   O  O     . LYS A 1 1581 ? 167.651 244.310 238.171 1.00 132.18 ? 1581 LYS A O     1 
ATOM   389   C  CB    . LYS A 1 1581 ? 166.392 242.881 235.464 1.00 126.15 ? 1581 LYS A CB    1 
ATOM   390   C  CG    . LYS A 1 1581 ? 165.113 242.948 234.642 1.00 124.66 ? 1581 LYS A CG    1 
ATOM   391   C  CD    . LYS A 1 1581 ? 164.115 243.921 235.251 1.00 121.49 ? 1581 LYS A CD    1 
ATOM   392   C  CE    . LYS A 1 1581 ? 162.900 244.101 234.358 1.00 111.98 ? 1581 LYS A CE    1 
ATOM   393   N  NZ    . LYS A 1 1581 ? 162.098 242.851 234.253 1.00 107.89 ? 1581 LYS A NZ    1 
ATOM   394   N  N     . VAL A 1 1582 ? 169.193 243.684 236.663 1.00 137.25 ? 1582 VAL A N     1 
ATOM   395   C  CA    . VAL A 1 1582 ? 170.168 243.371 237.706 1.00 138.63 ? 1582 VAL A CA    1 
ATOM   396   C  C     . VAL A 1 1582 ? 170.810 244.638 238.266 1.00 138.99 ? 1582 VAL A C     1 
ATOM   397   O  O     . VAL A 1 1582 ? 171.179 244.679 239.445 1.00 136.19 ? 1582 VAL A O     1 
ATOM   398   C  CB    . VAL A 1 1582 ? 171.231 242.386 237.181 1.00 134.82 ? 1582 VAL A CB    1 
ATOM   399   C  CG1   . VAL A 1 1582 ? 172.088 243.022 236.096 1.00 131.61 ? 1582 VAL A CG1   1 
ATOM   400   C  CG2   . VAL A 1 1582 ? 172.099 241.871 238.320 1.00 126.52 ? 1582 VAL A CG2   1 
ATOM   401   N  N     . SER A 1 1583 ? 170.950 245.688 237.453 1.00 137.74 ? 1583 SER A N     1 
ATOM   402   C  CA    . SER A 1 1583 ? 171.587 246.914 237.915 1.00 134.06 ? 1583 SER A CA    1 
ATOM   403   C  C     . SER A 1 1583 ? 170.742 247.673 238.927 1.00 137.04 ? 1583 SER A C     1 
ATOM   404   O  O     . SER A 1 1583 ? 171.285 248.495 239.674 1.00 134.62 ? 1583 SER A O     1 
ATOM   405   C  CB    . SER A 1 1583 ? 171.908 247.826 236.729 1.00 124.59 ? 1583 SER A CB    1 
ATOM   406   O  OG    . SER A 1 1583 ? 170.768 248.568 236.332 1.00 122.97 ? 1583 SER A OG    1 
ATOM   407   N  N     . LYS A 1 1584 ? 169.430 247.426 238.964 1.00 137.34 ? 1584 LYS A N     1 
ATOM   408   C  CA    . LYS A 1 1584 ? 168.581 248.082 239.953 1.00 133.63 ? 1584 LYS A CA    1 
ATOM   409   C  C     . LYS A 1 1584 ? 168.939 247.640 241.366 1.00 137.01 ? 1584 LYS A C     1 
ATOM   410   O  O     . LYS A 1 1584 ? 168.940 248.452 242.299 1.00 133.09 ? 1584 LYS A O     1 
ATOM   411   C  CB    . LYS A 1 1584 ? 167.110 247.795 239.652 1.00 130.78 ? 1584 LYS A CB    1 
ATOM   412   C  CG    . LYS A 1 1584 ? 166.551 248.598 238.486 1.00 125.90 ? 1584 LYS A CG    1 
ATOM   413   C  CD    . LYS A 1 1584 ? 165.034 248.534 238.444 1.00 121.22 ? 1584 LYS A CD    1 
ATOM   414   C  CE    . LYS A 1 1584 ? 164.548 247.109 238.241 1.00 122.82 ? 1584 LYS A CE    1 
ATOM   415   N  NZ    . LYS A 1 1584 ? 163.067 247.042 238.110 1.00 119.69 ? 1584 LYS A NZ    1 
ATOM   416   N  N     . SER A 1 1585 ? 169.245 246.355 241.545 1.00 139.57 ? 1585 SER A N     1 
ATOM   417   C  CA    . SER A 1 1585 ? 169.628 245.815 242.847 1.00 138.91 ? 1585 SER A CA    1 
ATOM   418   C  C     . SER A 1 1585 ? 171.085 245.374 242.805 1.00 139.85 ? 1585 SER A C     1 
ATOM   419   O  O     . SER A 1 1585 ? 171.392 244.294 242.278 1.00 135.44 ? 1585 SER A O     1 
ATOM   420   C  CB    . SER A 1 1585 ? 168.723 244.640 243.231 1.00 131.40 ? 1585 SER A CB    1 
ATOM   421   O  OG    . SER A 1 1585 ? 167.361 245.026 243.235 1.00 123.07 ? 1585 SER A OG    1 
ATOM   422   N  N     . PRO A 1 1586 ? 172.024 246.165 243.346 1.00 141.41 ? 1586 PRO A N     1 
ATOM   423   C  CA    . PRO A 1 1586 ? 173.451 245.822 243.305 1.00 140.24 ? 1586 PRO A CA    1 
ATOM   424   C  C     . PRO A 1 1586 ? 173.882 244.860 244.412 1.00 140.62 ? 1586 PRO A C     1 
ATOM   425   O  O     . PRO A 1 1586 ? 174.872 245.089 245.109 1.00 139.31 ? 1586 PRO A O     1 
ATOM   426   C  CB    . PRO A 1 1586 ? 174.127 247.189 243.450 1.00 131.15 ? 1586 PRO A CB    1 
ATOM   427   C  CG    . PRO A 1 1586 ? 173.181 247.970 244.302 1.00 127.54 ? 1586 PRO A CG    1 
ATOM   428   C  CD    . PRO A 1 1586 ? 171.788 247.473 243.984 1.00 134.09 ? 1586 PRO A CD    1 
ATOM   429   N  N     . LEU A 1 1587 ? 173.133 243.772 244.572 1.00 140.49 ? 1587 LEU A N     1 
ATOM   430   C  CA    . LEU A 1 1587 ? 173.424 242.762 245.579 1.00 141.43 ? 1587 LEU A CA    1 
ATOM   431   C  C     . LEU A 1 1587 ? 173.350 241.377 244.956 1.00 142.17 ? 1587 LEU A C     1 
ATOM   432   O  O     . LEU A 1 1587 ? 172.440 241.085 244.174 1.00 140.88 ? 1587 LEU A O     1 
ATOM   433   C  CB    . LEU A 1 1587 ? 172.453 242.859 246.762 1.00 138.10 ? 1587 LEU A CB    1 
ATOM   434   C  CG    . LEU A 1 1587 ? 172.947 242.276 248.088 1.00 132.64 ? 1587 LEU A CG    1 
ATOM   435   C  CD1   . LEU A 1 1587 ? 174.345 242.783 248.411 1.00 128.32 ? 1587 LEU A CD1   1 
ATOM   436   C  CD2   . LEU A 1 1587 ? 171.980 242.607 249.212 1.00 121.06 ? 1587 LEU A CD2   1 
ATOM   437   N  N     . VAL A 1 1588 ? 174.318 240.529 245.306 1.00 143.60 ? 1588 VAL A N     1 
ATOM   438   C  CA    . VAL A 1 1588 ? 174.336 239.163 244.791 1.00 144.06 ? 1588 VAL A CA    1 
ATOM   439   C  C     . VAL A 1 1588 ? 173.162 238.362 245.346 1.00 145.20 ? 1588 VAL A C     1 
ATOM   440   O  O     . VAL A 1 1588 ? 172.518 237.590 244.623 1.00 143.57 ? 1588 VAL A O     1 
ATOM   441   C  CB    . VAL A 1 1588 ? 175.694 238.500 245.100 1.00 135.20 ? 1588 VAL A CB    1 
ATOM   442   C  CG1   . VAL A 1 1588 ? 176.009 238.566 246.589 1.00 131.20 ? 1588 VAL A CG1   1 
ATOM   443   C  CG2   . VAL A 1 1588 ? 175.717 237.062 244.612 1.00 126.12 ? 1588 VAL A CG2   1 
ATOM   444   N  N     . MET A 1 1589 ? 172.856 238.536 246.635 1.00 145.66 ? 1589 MET A N     1 
ATOM   445   C  CA    . MET A 1 1589 ? 171.735 237.818 247.234 1.00 142.90 ? 1589 MET A CA    1 
ATOM   446   C  C     . MET A 1 1589 ? 170.407 238.295 246.662 1.00 142.73 ? 1589 MET A C     1 
ATOM   447   O  O     . MET A 1 1589 ? 169.462 237.508 246.532 1.00 136.84 ? 1589 MET A O     1 
ATOM   448   C  CB    . MET A 1 1589 ? 171.758 237.983 248.753 1.00 138.96 ? 1589 MET A CB    1 
ATOM   449   C  CG    . MET A 1 1589 ? 172.965 237.351 249.429 1.00 139.29 ? 1589 MET A CG    1 
ATOM   450   S  SD    . MET A 1 1589 ? 173.014 235.560 249.236 1.00 150.63 ? 1589 MET A SD    1 
ATOM   451   C  CE    . MET A 1 1589 ? 174.629 235.191 249.917 1.00 122.45 ? 1589 MET A CE    1 
ATOM   452   N  N     . ASP A 1 1590 ? 170.316 239.581 246.316 1.00 145.48 ? 1590 ASP A N     1 
ATOM   453   C  CA    . ASP A 1 1590 ? 169.082 240.121 245.758 1.00 144.26 ? 1590 ASP A CA    1 
ATOM   454   C  C     . ASP A 1 1590 ? 168.798 239.604 244.355 1.00 142.78 ? 1590 ASP A C     1 
ATOM   455   O  O     . ASP A 1 1590 ? 167.652 239.687 243.900 1.00 139.43 ? 1590 ASP A O     1 
ATOM   456   C  CB    . ASP A 1 1590 ? 169.138 241.650 245.742 1.00 138.75 ? 1590 ASP A CB    1 
ATOM   457   C  CG    . ASP A 1 1590 ? 168.849 242.259 247.100 1.00 133.96 ? 1590 ASP A CG    1 
ATOM   458   O  OD1   . ASP A 1 1590 ? 168.816 241.506 248.096 1.00 134.02 ? 1590 ASP A OD1   1 
ATOM   459   O  OD2   . ASP A 1 1590 ? 168.654 243.491 247.171 1.00 128.01 ? 1590 ASP A OD2   1 
ATOM   460   N  N     . VAL A 1 1591 ? 169.803 239.075 243.660 1.00 146.24 ? 1591 VAL A N     1 
ATOM   461   C  CA    . VAL A 1 1591 ? 169.622 238.604 242.295 1.00 143.13 ? 1591 VAL A CA    1 
ATOM   462   C  C     . VAL A 1 1591 ? 169.660 237.085 242.176 1.00 142.52 ? 1591 VAL A C     1 
ATOM   463   O  O     . VAL A 1 1591 ? 169.072 236.543 241.227 1.00 140.08 ? 1591 VAL A O     1 
ATOM   464   C  CB    . VAL A 1 1591 ? 170.652 239.243 241.339 1.00 138.03 ? 1591 VAL A CB    1 
ATOM   465   C  CG1   . VAL A 1 1591 ? 170.586 240.758 241.431 1.00 132.21 ? 1591 VAL A CG1   1 
ATOM   466   C  CG2   . VAL A 1 1591 ? 172.055 238.747 241.648 1.00 133.88 ? 1591 VAL A CG2   1 
ATOM   467   N  N     . LEU A 1 1592 ? 170.325 236.377 243.094 1.00 144.53 ? 1592 LEU A N     1 
ATOM   468   C  CA    . LEU A 1 1592 ? 170.261 234.918 243.068 1.00 141.51 ? 1592 LEU A CA    1 
ATOM   469   C  C     . LEU A 1 1592 ? 168.930 234.384 243.584 1.00 141.03 ? 1592 LEU A C     1 
ATOM   470   O  O     . LEU A 1 1592 ? 168.649 233.193 243.412 1.00 138.36 ? 1592 LEU A O     1 
ATOM   471   C  CB    . LEU A 1 1592 ? 171.417 234.307 243.866 1.00 136.10 ? 1592 LEU A CB    1 
ATOM   472   C  CG    . LEU A 1 1592 ? 172.750 234.082 243.141 1.00 132.56 ? 1592 LEU A CG    1 
ATOM   473   C  CD1   . LEU A 1 1592 ? 172.569 233.047 242.042 1.00 125.58 ? 1592 LEU A CD1   1 
ATOM   474   C  CD2   . LEU A 1 1592 ? 173.323 235.361 242.559 1.00 132.96 ? 1592 LEU A CD2   1 
ATOM   475   N  N     . ASN A 1 1593 ? 168.111 235.228 244.208 1.00 141.59 ? 1593 ASN A N     1 
ATOM   476   C  CA    . ASN A 1 1593 ? 166.776 234.827 244.633 1.00 142.99 ? 1593 ASN A CA    1 
ATOM   477   C  C     . ASN A 1 1593 ? 165.739 234.959 243.526 1.00 143.00 ? 1593 ASN A C     1 
ATOM   478   O  O     . ASN A 1 1593 ? 164.625 234.445 243.676 1.00 141.58 ? 1593 ASN A O     1 
ATOM   479   C  CB    . ASN A 1 1593 ? 166.339 235.655 245.847 1.00 140.14 ? 1593 ASN A CB    1 
ATOM   480   C  CG    . ASN A 1 1593 ? 165.166 235.035 246.585 1.00 137.54 ? 1593 ASN A CG    1 
ATOM   481   O  OD1   . ASN A 1 1593 ? 164.907 233.837 246.468 1.00 139.04 ? 1593 ASN A OD1   1 
ATOM   482   N  ND2   . ASN A 1 1593 ? 164.449 235.852 247.349 1.00 127.77 ? 1593 ASN A ND2   1 
ATOM   483   N  N     . ILE A 1 1594 ? 166.075 235.622 242.424 1.00 142.16 ? 1594 ILE A N     1 
ATOM   484   C  CA    . ILE A 1 1594 ? 165.133 235.822 241.329 1.00 141.40 ? 1594 ILE A CA    1 
ATOM   485   C  C     . ILE A 1 1594 ? 165.124 234.584 240.443 1.00 142.42 ? 1594 ILE A C     1 
ATOM   486   O  O     . ILE A 1 1594 ? 166.176 234.126 239.982 1.00 142.44 ? 1594 ILE A O     1 
ATOM   487   C  CB    . ILE A 1 1594 ? 165.496 237.079 240.523 1.00 136.80 ? 1594 ILE A CB    1 
ATOM   488   C  CG1   . ILE A 1 1594 ? 165.549 238.303 241.439 1.00 130.06 ? 1594 ILE A CG1   1 
ATOM   489   C  CG2   . ILE A 1 1594 ? 164.499 237.295 239.393 1.00 130.98 ? 1594 ILE A CG2   1 
ATOM   490   C  CD1   . ILE A 1 1594 ? 165.861 239.596 240.718 1.00 116.01 ? 1594 ILE A CD1   1 
ATOM   491   N  N     . GLN A 1 1595 ? 163.935 234.038 240.206 1.00 140.78 ? 1595 GLN A N     1 
ATOM   492   C  CA    . GLN A 1 1595 ? 163.796 232.865 239.357 1.00 141.18 ? 1595 GLN A CA    1 
ATOM   493   C  C     . GLN A 1 1595 ? 163.872 233.257 237.884 1.00 142.13 ? 1595 GLN A C     1 
ATOM   494   O  O     . GLN A 1 1595 ? 163.700 234.421 237.511 1.00 141.23 ? 1595 GLN A O     1 
ATOM   495   C  CB    . GLN A 1 1595 ? 162.477 232.146 239.642 1.00 135.94 ? 1595 GLN A CB    1 
ATOM   496   C  CG    . GLN A 1 1595 ? 161.257 232.824 239.040 1.00 132.52 ? 1595 GLN A CG    1 
ATOM   497   C  CD    . GLN A 1 1595 ? 160.657 233.866 239.961 1.00 128.36 ? 1595 GLN A CD    1 
ATOM   498   O  OE1   . GLN A 1 1595 ? 160.844 233.820 241.176 1.00 126.62 ? 1595 GLN A OE1   1 
ATOM   499   N  NE2   . GLN A 1 1595 ? 159.931 234.818 239.384 1.00 123.14 ? 1595 GLN A NE2   1 
ATOM   500   N  N     . GLY A 1 1596 ? 164.137 232.261 237.043 1.00 140.42 ? 1596 GLY A N     1 
ATOM   501   C  CA    . GLY A 1 1596 ? 164.247 232.487 235.618 1.00 134.25 ? 1596 GLY A CA    1 
ATOM   502   C  C     . GLY A 1 1596 ? 165.557 233.086 235.163 1.00 136.48 ? 1596 GLY A C     1 
ATOM   503   O  O     . GLY A 1 1596 ? 165.678 233.450 233.987 1.00 134.11 ? 1596 GLY A O     1 
ATOM   504   N  N     . VAL A 1 1597 ? 166.540 233.205 236.051 1.00 139.52 ? 1597 VAL A N     1 
ATOM   505   C  CA    . VAL A 1 1597 ? 167.825 233.800 235.696 1.00 136.30 ? 1597 VAL A CA    1 
ATOM   506   C  C     . VAL A 1 1597 ? 168.781 232.760 235.129 1.00 136.77 ? 1597 VAL A C     1 
ATOM   507   O  O     . VAL A 1 1597 ? 169.396 232.976 234.081 1.00 135.30 ? 1597 VAL A O     1 
ATOM   508   C  CB    . VAL A 1 1597 ? 168.433 234.514 236.922 1.00 134.43 ? 1597 VAL A CB    1 
ATOM   509   C  CG1   . VAL A 1 1597 ? 169.829 235.027 236.600 1.00 125.46 ? 1597 VAL A CG1   1 
ATOM   510   C  CG2   . VAL A 1 1597 ? 167.532 235.654 237.371 1.00 131.49 ? 1597 VAL A CG2   1 
ATOM   511   N  N     . GLN A 1 1598 ? 168.924 231.616 235.804 1.00 137.60 ? 1598 GLN A N     1 
ATOM   512   C  CA    . GLN A 1 1598 ? 169.891 230.615 235.362 1.00 138.55 ? 1598 GLN A CA    1 
ATOM   513   C  C     . GLN A 1 1598 ? 169.439 229.928 234.077 1.00 138.00 ? 1598 GLN A C     1 
ATOM   514   O  O     . GLN A 1 1598 ? 170.261 229.653 233.194 1.00 137.18 ? 1598 GLN A O     1 
ATOM   515   C  CB    . GLN A 1 1598 ? 170.127 229.588 236.468 1.00 130.66 ? 1598 GLN A CB    1 
ATOM   516   C  CG    . GLN A 1 1598 ? 171.162 228.530 236.119 1.00 132.16 ? 1598 GLN A CG    1 
ATOM   517   C  CD    . GLN A 1 1598 ? 172.570 229.089 236.059 1.00 137.47 ? 1598 GLN A CD    1 
ATOM   518   O  OE1   . GLN A 1 1598 ? 173.155 229.217 234.984 1.00 135.82 ? 1598 GLN A OE1   1 
ATOM   519   N  NE2   . GLN A 1 1598 ? 173.123 229.427 237.218 1.00 136.10 ? 1598 GLN A NE2   1 
ATOM   520   N  N     . ARG A 1 1599 ? 168.143 229.634 233.956 1.00 135.90 ? 1599 ARG A N     1 
ATOM   521   C  CA    . ARG A 1 1599 ? 167.636 229.028 232.728 1.00 134.55 ? 1599 ARG A CA    1 
ATOM   522   C  C     . ARG A 1 1599 ? 167.812 229.965 231.539 1.00 136.39 ? 1599 ARG A C     1 
ATOM   523   O  O     . ARG A 1 1599 ? 168.255 229.544 230.461 1.00 133.78 ? 1599 ARG A O     1 
ATOM   524   C  CB    . ARG A 1 1599 ? 166.167 228.646 232.907 1.00 135.70 ? 1599 ARG A CB    1 
ATOM   525   C  CG    . ARG A 1 1599 ? 165.555 227.919 231.721 1.00 132.49 ? 1599 ARG A CG    1 
ATOM   526   C  CD    . ARG A 1 1599 ? 164.113 228.352 231.487 1.00 129.80 ? 1599 ARG A CD    1 
ATOM   527   N  NE    . ARG A 1 1599 ? 163.887 229.754 231.820 1.00 133.69 ? 1599 ARG A NE    1 
ATOM   528   C  CZ    . ARG A 1 1599 ? 164.247 230.775 231.054 1.00 132.15 ? 1599 ARG A CZ    1 
ATOM   529   N  NH1   . ARG A 1 1599 ? 164.848 230.588 229.890 1.00 132.78 ? 1599 ARG A NH1   1 
ATOM   530   N  NH2   . ARG A 1 1599 ? 163.995 232.014 231.464 1.00 127.02 ? 1599 ARG A NH2   1 
ATOM   531   N  N     . SER A 1 1600 ? 167.485 231.247 231.721 1.00 139.17 ? 1600 SER A N     1 
ATOM   532   C  CA    . SER A 1 1600 ? 167.694 232.224 230.659 1.00 136.62 ? 1600 SER A CA    1 
ATOM   533   C  C     . SER A 1 1600 ? 169.174 232.394 230.343 1.00 136.63 ? 1600 SER A C     1 
ATOM   534   O  O     . SER A 1 1600 ? 169.536 232.591 229.181 1.00 134.50 ? 1600 SER A O     1 
ATOM   535   C  CB    . SER A 1 1600 ? 167.076 233.567 231.045 1.00 133.36 ? 1600 SER A CB    1 
ATOM   536   O  OG    . SER A 1 1600 ? 167.633 234.059 232.251 1.00 133.95 ? 1600 SER A OG    1 
ATOM   537   N  N     . LEU A 1 1601 ? 170.038 232.320 231.357 1.00 137.52 ? 1601 LEU A N     1 
ATOM   538   C  CA    . LEU A 1 1601 ? 171.474 232.425 231.117 1.00 135.91 ? 1601 LEU A CA    1 
ATOM   539   C  C     . LEU A 1 1601 ? 171.989 231.243 230.305 1.00 138.27 ? 1601 LEU A C     1 
ATOM   540   O  O     . LEU A 1 1601 ? 172.815 231.416 229.404 1.00 138.49 ? 1601 LEU A O     1 
ATOM   541   C  CB    . LEU A 1 1601 ? 172.219 232.533 232.446 1.00 133.85 ? 1601 LEU A CB    1 
ATOM   542   C  CG    . LEU A 1 1601 ? 173.694 232.930 232.364 1.00 131.63 ? 1601 LEU A CG    1 
ATOM   543   C  CD1   . LEU A 1 1601 ? 173.847 234.270 231.665 1.00 125.43 ? 1601 LEU A CD1   1 
ATOM   544   C  CD2   . LEU A 1 1601 ? 174.318 232.967 233.752 1.00 130.72 ? 1601 LEU A CD2   1 
ATOM   545   N  N     . GLU A 1 1602 ? 171.516 230.032 230.611 1.00 138.49 ? 1602 GLU A N     1 
ATOM   546   C  CA    . GLU A 1 1602 ? 171.910 228.865 229.825 1.00 136.02 ? 1602 GLU A CA    1 
ATOM   547   C  C     . GLU A 1 1602 ? 171.405 228.970 228.391 1.00 134.95 ? 1602 GLU A C     1 
ATOM   548   O  O     . GLU A 1 1602 ? 172.126 228.636 227.439 1.00 132.08 ? 1602 GLU A O     1 
ATOM   549   C  CB    . GLU A 1 1602 ? 171.393 227.586 230.484 1.00 131.50 ? 1602 GLU A CB    1 
ATOM   550   C  CG    . GLU A 1 1602 ? 172.036 227.268 231.823 1.00 131.97 ? 1602 GLU A CG    1 
ATOM   551   C  CD    . GLU A 1 1602 ? 171.445 226.031 232.472 1.00 131.65 ? 1602 GLU A CD    1 
ATOM   552   O  OE1   . GLU A 1 1602 ? 170.414 225.532 231.974 1.00 132.17 ? 1602 GLU A OE1   1 
ATOM   553   O  OE2   . GLU A 1 1602 ? 172.011 225.559 233.480 1.00 127.22 ? 1602 GLU A OE2   1 
ATOM   554   N  N     . ARG A 1 1603 ? 170.162 229.431 228.217 1.00 135.47 ? 1603 ARG A N     1 
ATOM   555   C  CA    . ARG A 1 1603 ? 169.633 229.626 226.870 1.00 136.16 ? 1603 ARG A CA    1 
ATOM   556   C  C     . ARG A 1 1603 ? 170.449 230.662 226.105 1.00 138.61 ? 1603 ARG A C     1 
ATOM   557   O  O     . ARG A 1 1603 ? 170.743 230.482 224.917 1.00 135.03 ? 1603 ARG A O     1 
ATOM   558   C  CB    . ARG A 1 1603 ? 168.163 230.039 226.941 1.00 133.27 ? 1603 ARG A CB    1 
ATOM   559   C  CG    . ARG A 1 1603 ? 167.581 230.515 225.621 1.00 128.71 ? 1603 ARG A CG    1 
ATOM   560   C  CD    . ARG A 1 1603 ? 166.170 231.047 225.803 1.00 128.57 ? 1603 ARG A CD    1 
ATOM   561   N  NE    . ARG A 1 1603 ? 166.145 232.258 226.615 1.00 128.10 ? 1603 ARG A NE    1 
ATOM   562   C  CZ    . ARG A 1 1603 ? 165.061 232.742 227.204 1.00 125.10 ? 1603 ARG A CZ    1 
ATOM   563   N  NH1   . ARG A 1 1603 ? 163.887 232.144 227.090 1.00 118.79 ? 1603 ARG A NH1   1 
ATOM   564   N  NH2   . ARG A 1 1603 ? 165.156 233.855 227.926 1.00 124.28 ? 1603 ARG A NH2   1 
ATOM   565   N  N     . LEU A 1 1604 ? 170.830 231.753 226.775 1.00 141.30 ? 1604 LEU A N     1 
ATOM   566   C  CA    . LEU A 1 1604 ? 171.647 232.779 226.139 1.00 135.35 ? 1604 LEU A CA    1 
ATOM   567   C  C     . LEU A 1 1604 ? 173.028 232.245 225.782 1.00 134.55 ? 1604 LEU A C     1 
ATOM   568   O  O     . LEU A 1 1604 ? 173.583 232.598 224.739 1.00 133.74 ? 1604 LEU A O     1 
ATOM   569   C  CB    . LEU A 1 1604 ? 171.762 233.999 227.053 1.00 131.01 ? 1604 LEU A CB    1 
ATOM   570   C  CG    . LEU A 1 1604 ? 170.605 234.997 226.995 1.00 129.01 ? 1604 LEU A CG    1 
ATOM   571   C  CD1   . LEU A 1 1604 ? 170.768 236.073 228.058 1.00 116.13 ? 1604 LEU A CD1   1 
ATOM   572   C  CD2   . LEU A 1 1604 ? 170.502 235.617 225.611 1.00 123.00 ? 1604 LEU A CD2   1 
ATOM   573   N  N     . ALA A 1 1605 ? 173.605 231.408 226.647 1.00 136.20 ? 1605 ALA A N     1 
ATOM   574   C  CA    . ALA A 1 1605 ? 174.899 230.805 226.341 1.00 132.20 ? 1605 ALA A CA    1 
ATOM   575   C  C     . ALA A 1 1605 ? 174.811 229.916 225.108 1.00 130.60 ? 1605 ALA A C     1 
ATOM   576   O  O     . ALA A 1 1605 ? 175.683 229.968 224.230 1.00 128.22 ? 1605 ALA A O     1 
ATOM   577   C  CB    . ALA A 1 1605 ? 175.404 230.005 227.542 1.00 128.87 ? 1605 ALA A CB    1 
ATOM   578   N  N     . ASP A 1 1606 ? 173.759 229.098 225.023 1.00 131.59 ? 1606 ASP A N     1 
ATOM   579   C  CA    . ASP A 1 1606 ? 173.576 228.260 223.841 1.00 131.33 ? 1606 ASP A CA    1 
ATOM   580   C  C     . ASP A 1 1606 ? 173.374 229.108 222.591 1.00 132.41 ? 1606 ASP A C     1 
ATOM   581   O  O     . ASP A 1 1606 ? 173.925 228.801 221.526 1.00 129.83 ? 1606 ASP A O     1 
ATOM   582   C  CB    . ASP A 1 1606 ? 172.395 227.311 224.046 1.00 129.25 ? 1606 ASP A CB    1 
ATOM   583   C  CG    . ASP A 1 1606 ? 172.676 226.248 225.090 1.00 124.64 ? 1606 ASP A CG    1 
ATOM   584   O  OD1   . ASP A 1 1606 ? 173.849 225.839 225.223 1.00 117.31 ? 1606 ASP A OD1   1 
ATOM   585   O  OD2   . ASP A 1 1606 ? 171.726 225.822 225.779 1.00 125.81 ? 1606 ASP A OD2   1 
ATOM   586   N  N     . LEU A 1 1607 ? 172.587 230.183 222.700 1.00 133.88 ? 1607 LEU A N     1 
ATOM   587   C  CA    . LEU A 1 1607 ? 172.365 231.062 221.556 1.00 133.19 ? 1607 LEU A CA    1 
ATOM   588   C  C     . LEU A 1 1607 ? 173.659 231.728 221.107 1.00 134.92 ? 1607 LEU A C     1 
ATOM   589   O  O     . LEU A 1 1607 ? 173.927 231.834 219.905 1.00 133.10 ? 1607 LEU A O     1 
ATOM   590   C  CB    . LEU A 1 1607 ? 171.313 232.116 221.905 1.00 131.36 ? 1607 LEU A CB    1 
ATOM   591   C  CG    . LEU A 1 1607 ? 169.853 231.661 221.891 1.00 125.25 ? 1607 LEU A CG    1 
ATOM   592   C  CD1   . LEU A 1 1607 ? 168.944 232.761 222.416 1.00 118.10 ? 1607 LEU A CD1   1 
ATOM   593   C  CD2   . LEU A 1 1607 ? 169.436 231.241 220.490 1.00 111.14 ? 1607 LEU A CD2   1 
ATOM   594   N  N     . LEU A 1 1608 ? 174.468 232.193 222.062 1.00 137.07 ? 1608 LEU A N     1 
ATOM   595   C  CA    . LEU A 1 1608 ? 175.744 232.813 221.726 1.00 135.11 ? 1608 LEU A CA    1 
ATOM   596   C  C     . LEU A 1 1608 ? 176.678 231.818 221.052 1.00 132.73 ? 1608 LEU A C     1 
ATOM   597   O  O     . LEU A 1 1608 ? 177.336 232.148 220.059 1.00 130.35 ? 1608 LEU A O     1 
ATOM   598   C  CB    . LEU A 1 1608 ? 176.393 233.395 222.983 1.00 133.64 ? 1608 LEU A CB    1 
ATOM   599   C  CG    . LEU A 1 1608 ? 176.172 234.883 223.279 1.00 131.53 ? 1608 LEU A CG    1 
ATOM   600   C  CD1   . LEU A 1 1608 ? 176.842 235.737 222.222 1.00 123.77 ? 1608 LEU A CD1   1 
ATOM   601   C  CD2   . LEU A 1 1608 ? 174.694 235.229 223.378 1.00 131.16 ? 1608 LEU A CD2   1 
ATOM   602   N  N     . GLY A 1 1609 ? 176.743 230.590 221.571 1.00 131.10 ? 1609 GLY A N     1 
ATOM   603   C  CA    . GLY A 1 1609 ? 177.560 229.576 220.925 1.00 128.38 ? 1609 GLY A CA    1 
ATOM   604   C  C     . GLY A 1 1609 ? 177.103 229.278 219.511 1.00 127.42 ? 1609 GLY A C     1 
ATOM   605   O  O     . GLY A 1 1609 ? 177.920 229.177 218.591 1.00 127.52 ? 1609 GLY A O     1 
ATOM   606   N  N     . LYS A 1 1610 ? 175.787 229.151 219.314 1.00 126.57 ? 1610 LYS A N     1 
ATOM   607   C  CA    . LYS A 1 1610 ? 175.262 228.858 217.985 1.00 125.62 ? 1610 LYS A CA    1 
ATOM   608   C  C     . LYS A 1 1610 ? 175.538 229.998 217.011 1.00 127.99 ? 1610 LYS A C     1 
ATOM   609   O  O     . LYS A 1 1610 ? 175.933 229.756 215.864 1.00 125.70 ? 1610 LYS A O     1 
ATOM   610   C  CB    . LYS A 1 1610 ? 173.762 228.571 218.065 1.00 121.36 ? 1610 LYS A CB    1 
ATOM   611   C  CG    . LYS A 1 1610 ? 173.098 228.337 216.717 1.00 116.61 ? 1610 LYS A CG    1 
ATOM   612   C  CD    . LYS A 1 1610 ? 172.174 229.486 216.347 1.00 117.29 ? 1610 LYS A CD    1 
ATOM   613   C  CE    . LYS A 1 1610 ? 170.957 229.533 217.257 1.00 117.01 ? 1610 LYS A CE    1 
ATOM   614   N  NZ    . LYS A 1 1610 ? 170.066 230.681 216.936 1.00 105.27 ? 1610 LYS A NZ    1 
ATOM   615   N  N     . ILE A 1 1611 ? 175.339 231.246 217.444 1.00 129.49 ? 1611 ILE A N     1 
ATOM   616   C  CA    . ILE A 1 1611 ? 175.558 232.374 216.544 1.00 127.00 ? 1611 ILE A CA    1 
ATOM   617   C  C     . ILE A 1 1611 ? 177.044 232.540 216.240 1.00 124.91 ? 1611 ILE A C     1 
ATOM   618   O  O     . ILE A 1 1611 ? 177.422 232.902 215.119 1.00 121.70 ? 1611 ILE A O     1 
ATOM   619   C  CB    . ILE A 1 1611 ? 174.929 233.661 217.116 1.00 128.43 ? 1611 ILE A CB    1 
ATOM   620   C  CG1   . ILE A 1 1611 ? 174.896 234.758 216.050 1.00 130.67 ? 1611 ILE A CG1   1 
ATOM   621   C  CG2   . ILE A 1 1611 ? 175.661 234.144 218.349 1.00 127.06 ? 1611 ILE A CG2   1 
ATOM   622   C  CD1   . ILE A 1 1611 ? 173.964 235.905 216.382 1.00 123.46 ? 1611 ILE A CD1   1 
ATOM   623   N  N     . GLN A 1 1612 ? 177.914 232.265 217.218 1.00 125.96 ? 1612 GLN A N     1 
ATOM   624   C  CA    . GLN A 1 1612 ? 179.349 232.309 216.954 1.00 122.22 ? 1612 GLN A CA    1 
ATOM   625   C  C     . GLN A 1 1612 ? 179.758 231.232 215.958 1.00 117.58 ? 1612 GLN A C     1 
ATOM   626   O  O     . GLN A 1 1612 ? 180.564 231.485 215.053 1.00 111.51 ? 1612 GLN A O     1 
ATOM   627   C  CB    . GLN A 1 1612 ? 180.130 232.156 218.260 1.00 121.93 ? 1612 GLN A CB    1 
ATOM   628   C  CG    . GLN A 1 1612 ? 181.639 232.252 218.093 1.00 123.08 ? 1612 GLN A CG    1 
ATOM   629   C  CD    . GLN A 1 1612 ? 182.380 232.143 219.411 1.00 126.04 ? 1612 GLN A CD    1 
ATOM   630   O  OE1   . GLN A 1 1612 ? 183.127 233.044 219.793 1.00 131.63 ? 1612 GLN A OE1   1 
ATOM   631   N  NE2   . GLN A 1 1612 ? 182.181 231.033 220.112 1.00 119.51 ? 1612 GLN A NE2   1 
ATOM   632   N  N     . LYS A 1 1613 ? 179.211 230.022 216.106 1.00 117.01 ? 1613 LYS A N     1 
ATOM   633   C  CA    . LYS A 1 1613 ? 179.501 228.961 215.148 1.00 115.54 ? 1613 LYS A CA    1 
ATOM   634   C  C     . LYS A 1 1613 ? 179.004 229.329 213.756 1.00 116.65 ? 1613 LYS A C     1 
ATOM   635   O  O     . LYS A 1 1613 ? 179.687 229.077 212.756 1.00 115.27 ? 1613 LYS A O     1 
ATOM   636   C  CB    . LYS A 1 1613 ? 178.876 227.648 215.618 1.00 109.88 ? 1613 LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 1613 ? 178.896 226.539 214.578 1.00 105.64 ? 1613 LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 1613 ? 179.197 225.193 215.215 1.00 90.06  ? 1613 LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 1613 ? 179.727 224.204 214.189 1.00 81.51  ? 1613 LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 1613 ? 179.544 222.794 214.632 1.00 69.94  ? 1613 LYS A NZ    1 
ATOM   641   N  N     . ALA A 1 1614 ? 177.813 229.926 213.672 1.00 118.61 ? 1614 ALA A N     1 
ATOM   642   C  CA    . ALA A 1 1614 ? 177.285 230.353 212.379 1.00 115.38 ? 1614 ALA A CA    1 
ATOM   643   C  C     . ALA A 1 1614 ? 178.168 231.422 211.748 1.00 113.05 ? 1614 ALA A C     1 
ATOM   644   O  O     . ALA A 1 1614 ? 178.419 231.393 210.538 1.00 109.13 ? 1614 ALA A O     1 
ATOM   645   C  CB    . ALA A 1 1614 ? 175.853 230.862 212.538 1.00 109.80 ? 1614 ALA A CB    1 
ATOM   646   N  N     . LEU A 1 1615 ? 178.647 232.375 212.552 1.00 115.33 ? 1615 LEU A N     1 
ATOM   647   C  CA    . LEU A 1 1615 ? 179.534 233.409 212.028 1.00 113.26 ? 1615 LEU A CA    1 
ATOM   648   C  C     . LEU A 1 1615 ? 180.850 232.810 211.547 1.00 111.40 ? 1615 LEU A C     1 
ATOM   649   O  O     . LEU A 1 1615 ? 181.395 233.232 210.519 1.00 102.17 ? 1615 LEU A O     1 
ATOM   650   C  CB    . LEU A 1 1615 ? 179.776 234.479 213.094 1.00 106.72 ? 1615 LEU A CB    1 
ATOM   651   C  CG    . LEU A 1 1615 ? 180.416 235.800 212.653 1.00 98.77  ? 1615 LEU A CG    1 
ATOM   652   C  CD1   . LEU A 1 1615 ? 179.853 236.951 213.469 1.00 106.25 ? 1615 LEU A CD1   1 
ATOM   653   C  CD2   . LEU A 1 1615 ? 181.929 235.754 212.785 1.00 99.82  ? 1615 LEU A CD2   1 
ATOM   654   N  N     . GLY A 1 1616 ? 181.378 231.828 212.279 1.00 111.20 ? 1616 GLY A N     1 
ATOM   655   C  CA    . GLY A 1 1616 ? 182.590 231.156 211.832 1.00 105.54 ? 1616 GLY A CA    1 
ATOM   656   C  C     . GLY A 1 1616 ? 182.398 230.413 210.524 1.00 102.64 ? 1616 GLY A C     1 
ATOM   657   O  O     . GLY A 1 1616 ? 183.253 230.466 209.635 1.00 96.60  ? 1616 GLY A O     1 
ATOM   658   N  N     . GLU A 1 1617 ? 181.272 229.707 210.388 1.00 107.24 ? 1617 GLU A N     1 
ATOM   659   C  CA    . GLU A 1 1617 ? 180.983 229.019 209.134 1.00 107.02 ? 1617 GLU A CA    1 
ATOM   660   C  C     . GLU A 1 1617 ? 180.809 230.011 207.989 1.00 99.27  ? 1617 GLU A C     1 
ATOM   661   O  O     . GLU A 1 1617 ? 181.228 229.743 206.858 1.00 90.95  ? 1617 GLU A O     1 
ATOM   662   C  CB    . GLU A 1 1617 ? 179.739 228.143 209.281 1.00 101.47 ? 1617 GLU A CB    1 
ATOM   663   C  CG    . GLU A 1 1617 ? 179.838 227.094 210.375 1.00 105.56 ? 1617 GLU A CG    1 
ATOM   664   C  CD    . GLU A 1 1617 ? 181.219 226.476 210.471 1.00 109.49 ? 1617 GLU A CD    1 
ATOM   665   O  OE1   . GLU A 1 1617 ? 181.610 225.740 209.540 1.00 105.91 ? 1617 GLU A OE1   1 
ATOM   666   O  OE2   . GLU A 1 1617 ? 181.914 226.726 211.478 1.00 112.00 ? 1617 GLU A OE2   1 
ATOM   667   N  N     . TYR A 1 1618 ? 180.188 231.158 208.265 1.00 97.61  ? 1618 TYR A N     1 
ATOM   668   C  CA    . TYR A 1 1618 ? 180.051 232.191 207.243 1.00 99.44  ? 1618 TYR A CA    1 
ATOM   669   C  C     . TYR A 1 1618 ? 181.409 232.736 206.819 1.00 93.80  ? 1618 TYR A C     1 
ATOM   670   O  O     . TYR A 1 1618 ? 181.650 232.966 205.627 1.00 86.81  ? 1618 TYR A O     1 
ATOM   671   C  CB    . TYR A 1 1618 ? 179.158 233.318 207.757 1.00 101.10 ? 1618 TYR A CB    1 
ATOM   672   C  CG    . TYR A 1 1618 ? 179.455 234.663 207.139 1.00 98.54  ? 1618 TYR A CG    1 
ATOM   673   C  CD1   . TYR A 1 1618 ? 179.093 234.942 205.829 1.00 94.58  ? 1618 TYR A CD1   1 
ATOM   674   C  CD2   . TYR A 1 1618 ? 180.093 235.656 207.869 1.00 97.14  ? 1618 TYR A CD2   1 
ATOM   675   C  CE1   . TYR A 1 1618 ? 179.363 236.172 205.261 1.00 98.03  ? 1618 TYR A CE1   1 
ATOM   676   C  CE2   . TYR A 1 1618 ? 180.366 236.887 207.312 1.00 97.93  ? 1618 TYR A CE2   1 
ATOM   677   C  CZ    . TYR A 1 1618 ? 179.997 237.141 206.009 1.00 101.17 ? 1618 TYR A CZ    1 
ATOM   678   O  OH    . TYR A 1 1618 ? 180.267 238.368 205.449 1.00 99.57  ? 1618 TYR A OH    1 
ATOM   679   N  N     . LEU A 1 1619 ? 182.305 232.964 207.781 1.00 90.83  ? 1619 LEU A N     1 
ATOM   680   C  CA    . LEU A 1 1619 ? 183.647 233.426 207.439 1.00 88.70  ? 1619 LEU A CA    1 
ATOM   681   C  C     . LEU A 1 1619 ? 184.385 232.386 206.606 1.00 77.90  ? 1619 LEU A C     1 
ATOM   682   O  O     . LEU A 1 1619 ? 185.067 232.729 205.633 1.00 74.87  ? 1619 LEU A O     1 
ATOM   683   C  CB    . LEU A 1 1619 ? 184.432 233.761 208.706 1.00 87.95  ? 1619 LEU A CB    1 
ATOM   684   C  CG    . LEU A 1 1619 ? 184.063 235.071 209.406 1.00 83.23  ? 1619 LEU A CG    1 
ATOM   685   C  CD1   . LEU A 1 1619 ? 184.890 235.261 210.668 1.00 81.87  ? 1619 LEU A CD1   1 
ATOM   686   C  CD2   . LEU A 1 1619 ? 184.234 236.251 208.465 1.00 78.14  ? 1619 LEU A CD2   1 
ATOM   687   N  N     . GLU A 1 1620 ? 184.245 231.109 206.962 1.00 82.33  ? 1620 GLU A N     1 
ATOM   688   C  CA    . GLU A 1 1620 ? 184.850 230.046 206.165 1.00 79.71  ? 1620 GLU A CA    1 
ATOM   689   C  C     . GLU A 1 1620 ? 184.298 230.032 204.744 1.00 74.63  ? 1620 GLU A C     1 
ATOM   690   O  O     . GLU A 1 1620 ? 185.055 229.908 203.772 1.00 68.79  ? 1620 GLU A O     1 
ATOM   691   C  CB    . GLU A 1 1620 ? 184.611 228.696 206.838 1.00 83.35  ? 1620 GLU A CB    1 
ATOM   692   C  CG    . GLU A 1 1620 ? 185.263 227.524 206.131 1.00 80.25  ? 1620 GLU A CG    1 
ATOM   693   C  CD    . GLU A 1 1620 ? 185.042 226.213 206.854 1.00 86.94  ? 1620 GLU A CD    1 
ATOM   694   O  OE1   . GLU A 1 1620 ? 184.362 226.217 207.900 1.00 91.87  ? 1620 GLU A OE1   1 
ATOM   695   O  OE2   . GLU A 1 1620 ? 185.530 225.175 206.361 1.00 81.06  ? 1620 GLU A OE2   1 
ATOM   696   N  N     . ARG A 1 1621 ? 182.977 230.156 204.607 1.00 80.71  ? 1621 ARG A N     1 
ATOM   697   C  CA    . ARG A 1 1621 ? 182.353 230.118 203.288 1.00 75.55  ? 1621 ARG A CA    1 
ATOM   698   C  C     . ARG A 1 1621 ? 182.781 231.307 202.439 1.00 68.72  ? 1621 ARG A C     1 
ATOM   699   O  O     . ARG A 1 1621 ? 183.004 231.170 201.232 1.00 65.29  ? 1621 ARG A O     1 
ATOM   700   C  CB    . ARG A 1 1621 ? 180.832 230.077 203.437 1.00 81.91  ? 1621 ARG A CB    1 
ATOM   701   C  CG    . ARG A 1 1621 ? 180.267 228.677 203.635 1.00 86.72  ? 1621 ARG A CG    1 
ATOM   702   C  CD    . ARG A 1 1621 ? 178.772 228.639 203.363 1.00 87.72  ? 1621 ARG A CD    1 
ATOM   703   N  NE    . ARG A 1 1621 ? 178.082 229.781 203.951 1.00 97.23  ? 1621 ARG A NE    1 
ATOM   704   C  CZ    . ARG A 1 1621 ? 177.779 229.894 205.237 1.00 98.28  ? 1621 ARG A CZ    1 
ATOM   705   N  NH1   . ARG A 1 1621 ? 178.077 228.941 206.104 1.00 102.09 ? 1621 ARG A NH1   1 
ATOM   706   N  NH2   . ARG A 1 1621 ? 177.156 230.989 205.663 1.00 90.50  ? 1621 ARG A NH2   1 
ATOM   707   N  N     . GLU A 1 1622 ? 182.889 232.488 203.051 1.00 71.84  ? 1622 GLU A N     1 
ATOM   708   C  CA    . GLU A 1 1622 ? 183.321 233.662 202.301 1.00 69.26  ? 1622 GLU A CA    1 
ATOM   709   C  C     . GLU A 1 1622 ? 184.811 233.611 201.997 1.00 61.63  ? 1622 GLU A C     1 
ATOM   710   O  O     . GLU A 1 1622 ? 185.270 234.259 201.050 1.00 62.92  ? 1622 GLU A O     1 
ATOM   711   C  CB    . GLU A 1 1622 ? 182.963 234.937 203.067 1.00 79.34  ? 1622 GLU A CB    1 
ATOM   712   C  CG    . GLU A 1 1622 ? 183.291 236.222 202.325 1.00 84.28  ? 1622 GLU A CG    1 
ATOM   713   C  CD    . GLU A 1 1622 ? 182.862 237.453 203.087 1.00 89.76  ? 1622 GLU A CD    1 
ATOM   714   O  OE1   . GLU A 1 1622 ? 182.323 237.296 204.199 1.00 90.88  ? 1622 GLU A OE1   1 
ATOM   715   O  OE2   . GLU A 1 1622 ? 183.061 238.575 202.576 1.00 87.53  ? 1622 GLU A OE2   1 
ATOM   716   N  N     . ARG A 1 1623 ? 185.584 232.858 202.782 1.00 64.46  ? 1623 ARG A N     1 
ATOM   717   C  CA    . ARG A 1 1623 ? 186.973 232.608 202.413 1.00 52.58  ? 1623 ARG A CA    1 
ATOM   718   C  C     . ARG A 1 1623 ? 187.073 231.594 201.282 1.00 54.39  ? 1623 ARG A C     1 
ATOM   719   O  O     . ARG A 1 1623 ? 188.046 231.612 200.520 1.00 50.78  ? 1623 ARG A O     1 
ATOM   720   C  CB    . ARG A 1 1623 ? 187.767 232.131 203.627 1.00 45.26  ? 1623 ARG A CB    1 
ATOM   721   C  CG    . ARG A 1 1623 ? 188.070 233.221 204.640 1.00 47.67  ? 1623 ARG A CG    1 
ATOM   722   C  CD    . ARG A 1 1623 ? 189.534 233.218 205.036 1.00 38.06  ? 1623 ARG A CD    1 
ATOM   723   N  NE    . ARG A 1 1623 ? 189.849 234.282 205.981 1.00 40.15  ? 1623 ARG A NE    1 
ATOM   724   C  CZ    . ARG A 1 1623 ? 189.662 234.197 207.291 1.00 52.07  ? 1623 ARG A CZ    1 
ATOM   725   N  NH1   . ARG A 1 1623 ? 189.165 233.105 207.849 1.00 56.37  ? 1623 ARG A NH1   1 
ATOM   726   N  NH2   . ARG A 1 1623 ? 189.981 235.233 208.061 1.00 53.61  ? 1623 ARG A NH2   1 
ATOM   727   N  N     . SER A 1 1624 ? 186.085 230.701 201.163 1.00 61.17  ? 1624 SER A N     1 
ATOM   728   C  CA    . SER A 1 1624 ? 186.093 229.729 200.073 1.00 56.56  ? 1624 SER A CA    1 
ATOM   729   C  C     . SER A 1 1624 ? 186.039 230.421 198.717 1.00 56.06  ? 1624 SER A C     1 
ATOM   730   O  O     . SER A 1 1624 ? 186.731 230.017 197.776 1.00 56.43  ? 1624 SER A O     1 
ATOM   731   C  CB    . SER A 1 1624 ? 184.923 228.758 200.230 1.00 59.53  ? 1624 SER A CB    1 
ATOM   732   O  OG    . SER A 1 1624 ? 185.068 227.970 201.399 1.00 55.46  ? 1624 SER A OG    1 
ATOM   733   N  N     . SER A 1 1625 ? 185.216 231.458 198.595 1.00 53.33  ? 1625 SER A N     1 
ATOM   734   C  CA    . SER A 1 1625 ? 185.223 232.318 197.420 1.00 53.81  ? 1625 SER A CA    1 
ATOM   735   C  C     . SER A 1 1625 ? 186.256 233.420 197.612 1.00 51.76  ? 1625 SER A C     1 
ATOM   736   O  O     . SER A 1 1625 ? 186.406 233.953 198.713 1.00 48.16  ? 1625 SER A O     1 
ATOM   737   C  CB    . SER A 1 1625 ? 183.839 232.924 197.183 1.00 49.73  ? 1625 SER A CB    1 
ATOM   738   O  OG    . SER A 1 1625 ? 183.607 234.016 198.054 1.00 51.21  ? 1625 SER A OG    1 
ATOM   739   N  N     . PHE A 1 1626 ? 186.964 233.756 196.533 1.00 51.69  ? 1626 PHE A N     1 
ATOM   740   C  CA    . PHE A 1 1626 ? 188.067 234.712 196.592 1.00 45.34  ? 1626 PHE A CA    1 
ATOM   741   C  C     . PHE A 1 1626 ? 189.048 234.294 197.683 1.00 45.06  ? 1626 PHE A C     1 
ATOM   742   O  O     . PHE A 1 1626 ? 189.082 234.907 198.757 1.00 37.63  ? 1626 PHE A O     1 
ATOM   743   C  CB    . PHE A 1 1626 ? 187.559 236.133 196.844 1.00 42.32  ? 1626 PHE A CB    1 
ATOM   744   C  CG    . PHE A 1 1626 ? 188.617 237.186 196.692 1.00 38.89  ? 1626 PHE A CG    1 
ATOM   745   C  CD1   . PHE A 1 1626 ? 189.165 237.459 195.451 1.00 34.43  ? 1626 PHE A CD1   1 
ATOM   746   C  CD2   . PHE A 1 1626 ? 189.076 237.891 197.791 1.00 34.68  ? 1626 PHE A CD2   1 
ATOM   747   C  CE1   . PHE A 1 1626 ? 190.141 238.424 195.307 1.00 32.15  ? 1626 PHE A CE1   1 
ATOM   748   C  CE2   . PHE A 1 1626 ? 190.052 238.856 197.654 1.00 27.37  ? 1626 PHE A CE2   1 
ATOM   749   C  CZ    . PHE A 1 1626 ? 190.585 239.123 196.411 1.00 28.78  ? 1626 PHE A CZ    1 
ATOM   750   N  N     . PRO A 1 1627 ? 189.847 233.249 197.448 1.00 42.08  ? 1627 PRO A N     1 
ATOM   751   C  CA    . PRO A 1 1627 ? 190.671 232.684 198.531 1.00 38.10  ? 1627 PRO A CA    1 
ATOM   752   C  C     . PRO A 1 1627 ? 191.715 233.634 199.100 1.00 34.90  ? 1627 PRO A C     1 
ATOM   753   O  O     . PRO A 1 1627 ? 192.323 233.298 200.125 1.00 38.68  ? 1627 PRO A O     1 
ATOM   754   C  CB    . PRO A 1 1627 ? 191.337 231.471 197.867 1.00 31.76  ? 1627 PRO A CB    1 
ATOM   755   C  CG    . PRO A 1 1627 ? 190.488 231.168 196.671 1.00 32.14  ? 1627 PRO A CG    1 
ATOM   756   C  CD    . PRO A 1 1627 ? 189.989 232.492 196.195 1.00 33.83  ? 1627 PRO A CD    1 
ATOM   757   N  N     . ARG A 1 1628 ? 191.941 234.799 198.485 1.00 29.44  ? 1628 ARG A N     1 
ATOM   758   C  CA    . ARG A 1 1628 ? 192.944 235.728 198.998 1.00 31.54  ? 1628 ARG A CA    1 
ATOM   759   C  C     . ARG A 1 1628 ? 192.647 236.166 200.425 1.00 36.39  ? 1628 ARG A C     1 
ATOM   760   O  O     . ARG A 1 1628 ? 193.571 236.546 201.153 1.00 39.31  ? 1628 ARG A O     1 
ATOM   761   C  CB    . ARG A 1 1628 ? 193.037 236.955 198.090 1.00 33.52  ? 1628 ARG A CB    1 
ATOM   762   C  CG    . ARG A 1 1628 ? 193.233 236.626 196.623 1.00 32.73  ? 1628 ARG A CG    1 
ATOM   763   C  CD    . ARG A 1 1628 ? 194.699 236.517 196.261 1.00 29.82  ? 1628 ARG A CD    1 
ATOM   764   N  NE    . ARG A 1 1628 ? 194.893 236.457 194.817 1.00 32.40  ? 1628 ARG A NE    1 
ATOM   765   C  CZ    . ARG A 1 1628 ? 195.883 237.051 194.169 1.00 25.50  ? 1628 ARG A CZ    1 
ATOM   766   N  NH1   . ARG A 1 1628 ? 196.804 237.753 194.807 1.00 23.71  ? 1628 ARG A NH1   1 
ATOM   767   N  NH2   . ARG A 1 1628 ? 195.954 236.935 192.846 1.00 24.83  ? 1628 ARG A NH2   1 
ATOM   768   N  N     . PHE A 1 1629 ? 191.383 236.089 200.850 1.00 35.60  ? 1629 PHE A N     1 
ATOM   769   C  CA    . PHE A 1 1629 ? 191.005 236.433 202.214 1.00 37.92  ? 1629 PHE A CA    1 
ATOM   770   C  C     . PHE A 1 1629 ? 191.655 235.524 203.247 1.00 39.91  ? 1629 PHE A C     1 
ATOM   771   O  O     . PHE A 1 1629 ? 191.646 235.860 204.434 1.00 40.38  ? 1629 PHE A O     1 
ATOM   772   C  CB    . PHE A 1 1629 ? 189.484 236.379 202.367 1.00 42.82  ? 1629 PHE A CB    1 
ATOM   773   C  CG    . PHE A 1 1629 ? 188.779 237.599 201.852 1.00 47.06  ? 1629 PHE A CG    1 
ATOM   774   C  CD1   . PHE A 1 1629 ? 189.354 238.851 201.972 1.00 48.96  ? 1629 PHE A CD1   1 
ATOM   775   C  CD2   . PHE A 1 1629 ? 187.539 237.491 201.247 1.00 48.97  ? 1629 PHE A CD2   1 
ATOM   776   C  CE1   . PHE A 1 1629 ? 188.704 239.973 201.498 1.00 51.30  ? 1629 PHE A CE1   1 
ATOM   777   C  CE2   . PHE A 1 1629 ? 186.885 238.607 200.772 1.00 51.79  ? 1629 PHE A CE2   1 
ATOM   778   C  CZ    . PHE A 1 1629 ? 187.468 239.850 200.897 1.00 52.44  ? 1629 PHE A CZ    1 
ATOM   779   N  N     . TYR A 1 1630 ? 192.201 234.381 202.831 1.00 35.99  ? 1630 TYR A N     1 
ATOM   780   C  CA    . TYR A 1 1630 ? 192.963 233.546 203.748 1.00 32.60  ? 1630 TYR A CA    1 
ATOM   781   C  C     . TYR A 1 1630 ? 194.255 234.207 204.208 1.00 28.67  ? 1630 TYR A C     1 
ATOM   782   O  O     . TYR A 1 1630 ? 194.860 233.733 205.175 1.00 28.66  ? 1630 TYR A O     1 
ATOM   783   C  CB    . TYR A 1 1630 ? 193.263 232.199 203.091 1.00 26.72  ? 1630 TYR A CB    1 
ATOM   784   C  CG    . TYR A 1 1630 ? 192.115 231.222 203.181 1.00 32.13  ? 1630 TYR A CG    1 
ATOM   785   C  CD1   . TYR A 1 1630 ? 191.378 230.880 202.057 1.00 35.30  ? 1630 TYR A CD1   1 
ATOM   786   C  CD2   . TYR A 1 1630 ? 191.782 230.623 204.388 1.00 32.72  ? 1630 TYR A CD2   1 
ATOM   787   C  CE1   . TYR A 1 1630 ? 190.326 229.991 202.136 1.00 37.76  ? 1630 TYR A CE1   1 
ATOM   788   C  CE2   . TYR A 1 1630 ? 190.736 229.726 204.475 1.00 36.03  ? 1630 TYR A CE2   1 
ATOM   789   C  CZ    . TYR A 1 1630 ? 190.014 229.412 203.344 1.00 38.41  ? 1630 TYR A CZ    1 
ATOM   790   O  OH    . TYR A 1 1630 ? 188.970 228.520 203.421 1.00 43.97  ? 1630 TYR A OH    1 
ATOM   791   N  N     . PHE A 1 1631 ? 194.687 235.286 203.556 1.00 30.26  ? 1631 PHE A N     1 
ATOM   792   C  CA    . PHE A 1 1631 ? 195.877 236.014 203.975 1.00 34.73  ? 1631 PHE A CA    1 
ATOM   793   C  C     . PHE A 1 1631 ? 195.572 237.177 204.912 1.00 39.92  ? 1631 PHE A C     1 
ATOM   794   O  O     . PHE A 1 1631 ? 196.495 237.911 205.277 1.00 36.47  ? 1631 PHE A O     1 
ATOM   795   C  CB    . PHE A 1 1631 ? 196.648 236.526 202.754 1.00 32.55  ? 1631 PHE A CB    1 
ATOM   796   C  CG    . PHE A 1 1631 ? 197.291 235.438 201.944 1.00 26.06  ? 1631 PHE A CG    1 
ATOM   797   C  CD1   . PHE A 1 1631 ? 197.805 234.311 202.562 1.00 21.27  ? 1631 PHE A CD1   1 
ATOM   798   C  CD2   . PHE A 1 1631 ? 197.394 235.548 200.570 1.00 23.07  ? 1631 PHE A CD2   1 
ATOM   799   C  CE1   . PHE A 1 1631 ? 198.400 233.310 201.824 1.00 16.07  ? 1631 PHE A CE1   1 
ATOM   800   C  CE2   . PHE A 1 1631 ? 197.990 234.549 199.828 1.00 18.45  ? 1631 PHE A CE2   1 
ATOM   801   C  CZ    . PHE A 1 1631 ? 198.493 233.430 200.455 1.00 15.56  ? 1631 PHE A CZ    1 
ATOM   802   N  N     . VAL A 1 1632 ? 194.315 237.366 205.305 1.00 42.84  ? 1632 VAL A N     1 
ATOM   803   C  CA    . VAL A 1 1632 ? 193.950 238.402 206.262 1.00 38.37  ? 1632 VAL A CA    1 
ATOM   804   C  C     . VAL A 1 1632 ? 193.287 237.739 207.461 1.00 43.14  ? 1632 VAL A C     1 
ATOM   805   O  O     . VAL A 1 1632 ? 192.707 236.654 207.354 1.00 43.22  ? 1632 VAL A O     1 
ATOM   806   C  CB    . VAL A 1 1632 ? 193.021 239.475 205.646 1.00 41.79  ? 1632 VAL A CB    1 
ATOM   807   C  CG1   . VAL A 1 1632 ? 193.715 240.191 204.502 1.00 44.03  ? 1632 VAL A CG1   1 
ATOM   808   C  CG2   . VAL A 1 1632 ? 191.714 238.861 205.184 1.00 44.50  ? 1632 VAL A CG2   1 
ATOM   809   N  N     . GLY A 1 1633 ? 193.386 238.399 208.610 1.00 52.89  ? 1633 GLY A N     1 
ATOM   810   C  CA    . GLY A 1 1633 ? 192.815 237.865 209.827 1.00 56.24  ? 1633 GLY A CA    1 
ATOM   811   C  C     . GLY A 1 1633 ? 191.302 237.970 209.851 1.00 62.67  ? 1633 GLY A C     1 
ATOM   812   O  O     . GLY A 1 1633 ? 190.671 238.626 209.023 1.00 66.86  ? 1633 GLY A O     1 
ATOM   813   N  N     . ASP A 1 1634 ? 190.710 237.289 210.837 1.00 67.86  ? 1634 ASP A N     1 
ATOM   814   C  CA    . ASP A 1 1634 ? 189.257 237.293 210.967 1.00 69.52  ? 1634 ASP A CA    1 
ATOM   815   C  C     . ASP A 1 1634 ? 188.730 238.691 211.263 1.00 70.47  ? 1634 ASP A C     1 
ATOM   816   O  O     . ASP A 1 1634 ? 187.720 239.114 210.689 1.00 73.28  ? 1634 ASP A O     1 
ATOM   817   C  CB    . ASP A 1 1634 ? 188.824 236.311 212.055 1.00 71.07  ? 1634 ASP A CB    1 
ATOM   818   C  CG    . ASP A 1 1634 ? 189.125 234.872 211.692 1.00 74.42  ? 1634 ASP A CG    1 
ATOM   819   O  OD1   . ASP A 1 1634 ? 189.561 234.627 210.548 1.00 68.82  ? 1634 ASP A OD1   1 
ATOM   820   O  OD2   . ASP A 1 1634 ? 188.925 233.986 212.549 1.00 73.97  ? 1634 ASP A OD2   1 
ATOM   821   N  N     . GLU A 1 1635 ? 189.396 239.423 212.161 1.00 67.82  ? 1635 GLU A N     1 
ATOM   822   C  CA    . GLU A 1 1635 ? 188.983 240.796 212.436 1.00 71.74  ? 1635 GLU A CA    1 
ATOM   823   C  C     . GLU A 1 1635 ? 189.175 241.683 211.210 1.00 72.27  ? 1635 GLU A C     1 
ATOM   824   O  O     . GLU A 1 1635 ? 188.308 242.506 210.888 1.00 72.85  ? 1635 GLU A O     1 
ATOM   825   C  CB    . GLU A 1 1635 ? 189.742 241.343 213.649 1.00 78.21  ? 1635 GLU A CB    1 
ATOM   826   C  CG    . GLU A 1 1635 ? 191.192 241.760 213.406 1.00 81.53  ? 1635 GLU A CG    1 
ATOM   827   C  CD    . GLU A 1 1635 ? 192.160 240.590 213.430 1.00 81.04  ? 1635 GLU A CD    1 
ATOM   828   O  OE1   . GLU A 1 1635 ? 191.856 239.542 212.824 1.00 78.59  ? 1635 GLU A OE1   1 
ATOM   829   O  OE2   . GLU A 1 1635 ? 193.231 240.722 214.060 1.00 86.00  ? 1635 GLU A OE2   1 
ATOM   830   N  N     . ASP A 1 1636 ? 190.287 241.511 210.494 1.00 70.34  ? 1636 ASP A N     1 
ATOM   831   C  CA    . ASP A 1 1636 ? 190.491 242.260 209.260 1.00 64.38  ? 1636 ASP A CA    1 
ATOM   832   C  C     . ASP A 1 1636 ? 189.455 241.877 208.211 1.00 66.35  ? 1636 ASP A C     1 
ATOM   833   O  O     . ASP A 1 1636 ? 188.899 242.748 207.533 1.00 73.62  ? 1636 ASP A O     1 
ATOM   834   C  CB    . ASP A 1 1636 ? 191.905 242.026 208.732 1.00 64.85  ? 1636 ASP A CB    1 
ATOM   835   C  CG    . ASP A 1 1636 ? 192.919 242.967 209.350 1.00 78.02  ? 1636 ASP A CG    1 
ATOM   836   O  OD1   . ASP A 1 1636 ? 192.844 244.184 209.080 1.00 74.54  ? 1636 ASP A OD1   1 
ATOM   837   O  OD2   . ASP A 1 1636 ? 193.788 242.489 210.109 1.00 82.75  ? 1636 ASP A OD2   1 
ATOM   838   N  N     . LEU A 1 1637 ? 189.182 240.577 208.069 1.00 63.93  ? 1637 LEU A N     1 
ATOM   839   C  CA    . LEU A 1 1637 ? 188.182 240.139 207.104 1.00 67.64  ? 1637 LEU A CA    1 
ATOM   840   C  C     . LEU A 1 1637 ? 186.823 240.748 207.419 1.00 73.99  ? 1637 LEU A C     1 
ATOM   841   O  O     . LEU A 1 1637 ? 186.109 241.192 206.514 1.00 71.54  ? 1637 LEU A O     1 
ATOM   842   C  CB    . LEU A 1 1637 ? 188.102 238.612 207.086 1.00 57.21  ? 1637 LEU A CB    1 
ATOM   843   C  CG    . LEU A 1 1637 ? 187.034 237.989 206.188 1.00 52.67  ? 1637 LEU A CG    1 
ATOM   844   C  CD1   . LEU A 1 1637 ? 187.126 238.545 204.779 1.00 55.81  ? 1637 LEU A CD1   1 
ATOM   845   C  CD2   . LEU A 1 1637 ? 187.165 236.476 206.175 1.00 56.00  ? 1637 LEU A CD2   1 
ATOM   846   N  N     . LEU A 1 1638 ? 186.460 240.798 208.702 1.00 73.74  ? 1638 LEU A N     1 
ATOM   847   C  CA    . LEU A 1 1638 ? 185.215 241.446 209.096 1.00 70.51  ? 1638 LEU A CA    1 
ATOM   848   C  C     . LEU A 1 1638 ? 185.256 242.939 208.796 1.00 69.09  ? 1638 LEU A C     1 
ATOM   849   O  O     . LEU A 1 1638 ? 184.228 243.543 208.469 1.00 72.81  ? 1638 LEU A O     1 
ATOM   850   C  CB    . LEU A 1 1638 ? 184.951 241.196 210.579 1.00 73.34  ? 1638 LEU A CB    1 
ATOM   851   C  CG    . LEU A 1 1638 ? 184.342 239.832 210.914 1.00 73.60  ? 1638 LEU A CG    1 
ATOM   852   C  CD1   . LEU A 1 1638 ? 184.072 239.716 212.401 1.00 83.86  ? 1638 LEU A CD1   1 
ATOM   853   C  CD2   . LEU A 1 1638 ? 183.068 239.596 210.118 1.00 79.17  ? 1638 LEU A CD2   1 
ATOM   854   N  N     . GLU A 1 1639 ? 186.437 243.554 208.913 1.00 75.15  ? 1639 GLU A N     1 
ATOM   855   C  CA    . GLU A 1 1639 ? 186.568 244.970 208.584 1.00 72.85  ? 1639 GLU A CA    1 
ATOM   856   C  C     . GLU A 1 1639 ? 186.279 245.228 207.108 1.00 71.21  ? 1639 GLU A C     1 
ATOM   857   O  O     . GLU A 1 1639 ? 185.557 246.171 206.768 1.00 73.98  ? 1639 GLU A O     1 
ATOM   858   C  CB    . GLU A 1 1639 ? 187.964 245.468 208.956 1.00 65.23  ? 1639 GLU A CB    1 
ATOM   859   C  CG    . GLU A 1 1639 ? 188.172 246.956 208.727 1.00 73.49  ? 1639 GLU A CG    1 
ATOM   860   C  CD    . GLU A 1 1639 ? 189.549 247.425 209.153 1.00 77.72  ? 1639 GLU A CD    1 
ATOM   861   O  OE1   . GLU A 1 1639 ? 190.352 246.586 209.609 1.00 75.39  ? 1639 GLU A OE1   1 
ATOM   862   O  OE2   . GLU A 1 1639 ? 189.827 248.637 209.032 1.00 79.42  ? 1639 GLU A OE2   1 
ATOM   863   N  N     . ILE A 1 1640 ? 186.835 244.404 206.215 1.00 72.21  ? 1640 ILE A N     1 
ATOM   864   C  CA    . ILE A 1 1640 ? 186.465 244.532 204.801 1.00 71.12  ? 1640 ILE A CA    1 
ATOM   865   C  C     . ILE A 1 1640 ? 184.991 244.199 204.591 1.00 74.96  ? 1640 ILE A C     1 
ATOM   866   O  O     . ILE A 1 1640 ? 184.315 244.837 203.773 1.00 77.94  ? 1640 ILE A O     1 
ATOM   867   C  CB    . ILE A 1 1640 ? 187.364 243.689 203.859 1.00 69.74  ? 1640 ILE A CB    1 
ATOM   868   C  CG1   . ILE A 1 1640 ? 188.831 244.138 203.871 1.00 63.60  ? 1640 ILE A CG1   1 
ATOM   869   C  CG2   . ILE A 1 1640 ? 186.838 243.715 202.434 1.00 66.31  ? 1640 ILE A CG2   1 
ATOM   870   C  CD1   . ILE A 1 1640 ? 189.703 243.497 204.878 1.00 61.53  ? 1640 ILE A CD1   1 
ATOM   871   N  N     . ILE A 1 1641 ? 184.466 243.219 205.328 1.00 78.41  ? 1641 ILE A N     1 
ATOM   872   C  CA    . ILE A 1 1641 ? 183.078 242.798 205.147 1.00 77.90  ? 1641 ILE A CA    1 
ATOM   873   C  C     . ILE A 1 1641 ? 182.126 243.951 205.441 1.00 80.82  ? 1641 ILE A C     1 
ATOM   874   O  O     . ILE A 1 1641 ? 181.195 244.225 204.673 1.00 79.55  ? 1641 ILE A O     1 
ATOM   875   C  CB    . ILE A 1 1641 ? 182.774 241.581 206.037 1.00 78.87  ? 1641 ILE A CB    1 
ATOM   876   C  CG1   . ILE A 1 1641 ? 183.260 240.293 205.377 1.00 77.50  ? 1641 ILE A CG1   1 
ATOM   877   C  CG2   . ILE A 1 1641 ? 181.286 241.487 206.336 1.00 87.41  ? 1641 ILE A CG2   1 
ATOM   878   C  CD1   . ILE A 1 1641 ? 183.532 239.185 206.366 1.00 79.34  ? 1641 ILE A CD1   1 
ATOM   879   N  N     . GLY A 1 1642 ? 182.346 244.648 206.559 1.00 81.02  ? 1642 GLY A N     1 
ATOM   880   C  CA    . GLY A 1 1642 ? 181.441 245.708 206.963 1.00 84.52  ? 1642 GLY A CA    1 
ATOM   881   C  C     . GLY A 1 1642 ? 181.689 247.046 206.302 1.00 85.85  ? 1642 GLY A C     1 
ATOM   882   O  O     . GLY A 1 1642 ? 180.818 247.919 206.357 1.00 94.51  ? 1642 GLY A O     1 
ATOM   883   N  N     . ASN A 1 1643 ? 182.848 247.226 205.677 1.00 79.40  ? 1643 ASN A N     1 
ATOM   884   C  CA    . ASN A 1 1643 ? 183.209 248.479 205.025 1.00 79.62  ? 1643 ASN A CA    1 
ATOM   885   C  C     . ASN A 1 1643 ? 183.234 248.329 203.507 1.00 77.73  ? 1643 ASN A C     1 
ATOM   886   O  O     . ASN A 1 1643 ? 184.094 248.887 202.825 1.00 83.14  ? 1643 ASN A O     1 
ATOM   887   C  CB    . ASN A 1 1643 ? 184.555 248.989 205.534 1.00 81.73  ? 1643 ASN A CB    1 
ATOM   888   C  CG    . ASN A 1 1643 ? 184.527 249.333 207.012 1.00 82.87  ? 1643 ASN A CG    1 
ATOM   889   O  OD1   . ASN A 1 1643 ? 183.834 250.257 207.435 1.00 86.30  ? 1643 ASN A OD1   1 
ATOM   890   N  ND2   . ASN A 1 1643 ? 185.287 248.587 207.806 1.00 72.88  ? 1643 ASN A ND2   1 
ATOM   891   N  N     . SER A 1 1644 ? 182.289 247.560 202.962 1.00 79.59  ? 1644 SER A N     1 
ATOM   892   C  CA    . SER A 1 1644 ? 182.215 247.406 201.514 1.00 87.81  ? 1644 SER A CA    1 
ATOM   893   C  C     . SER A 1 1644 ? 181.736 248.685 200.837 1.00 90.95  ? 1644 SER A C     1 
ATOM   894   O  O     . SER A 1 1644 ? 182.112 248.955 199.690 1.00 88.04  ? 1644 SER A O     1 
ATOM   895   C  CB    . SER A 1 1644 ? 181.297 246.237 201.156 1.00 80.10  ? 1644 SER A CB    1 
ATOM   896   O  OG    . SER A 1 1644 ? 181.156 246.111 199.752 1.00 77.18  ? 1644 SER A OG    1 
ATOM   897   N  N     . LYS A 1 1645 ? 180.903 249.475 201.521 1.00 86.53  ? 1645 LYS A N     1 
ATOM   898   C  CA    . LYS A 1 1645 ? 180.376 250.697 200.921 1.00 85.53  ? 1645 LYS A CA    1 
ATOM   899   C  C     . LYS A 1 1645 ? 181.482 251.707 200.642 1.00 81.95  ? 1645 LYS A C     1 
ATOM   900   O  O     . LYS A 1 1645 ? 181.523 252.311 199.564 1.00 77.77  ? 1645 LYS A O     1 
ATOM   901   C  CB    . LYS A 1 1645 ? 179.308 251.308 201.828 1.00 92.52  ? 1645 LYS A CB    1 
ATOM   902   C  CG    . LYS A 1 1645 ? 177.901 250.796 201.564 1.00 95.10  ? 1645 LYS A CG    1 
ATOM   903   C  CD    . LYS A 1 1645 ? 176.903 251.389 202.545 1.00 94.39  ? 1645 LYS A CD    1 
ATOM   904   C  CE    . LYS A 1 1645 ? 176.990 252.906 202.577 1.00 92.46  ? 1645 LYS A CE    1 
ATOM   905   N  NZ    . LYS A 1 1645 ? 176.877 253.498 201.215 1.00 92.62  ? 1645 LYS A NZ    1 
ATOM   906   N  N     . ASN A 1 1646 ? 182.388 251.907 201.597 1.00 83.17  ? 1646 ASN A N     1 
ATOM   907   C  CA    . ASN A 1 1646 ? 183.492 252.845 201.445 1.00 80.59  ? 1646 ASN A CA    1 
ATOM   908   C  C     . ASN A 1 1646 ? 184.761 252.075 201.096 1.00 80.11  ? 1646 ASN A C     1 
ATOM   909   O  O     . ASN A 1 1646 ? 185.177 251.179 201.837 1.00 78.96  ? 1646 ASN A O     1 
ATOM   910   C  CB    . ASN A 1 1646 ? 183.684 253.685 202.709 1.00 73.61  ? 1646 ASN A CB    1 
ATOM   911   C  CG    . ASN A 1 1646 ? 184.019 252.849 203.928 1.00 77.07  ? 1646 ASN A CG    1 
ATOM   912   O  OD1   . ASN A 1 1646 ? 183.604 251.696 204.039 1.00 85.16  ? 1646 ASN A OD1   1 
ATOM   913   N  ND2   . ASN A 1 1646 ? 184.777 253.428 204.851 1.00 73.58  ? 1646 ASN A ND2   1 
ATOM   914   N  N     . VAL A 1 1647 ? 185.371 252.425 199.959 1.00 80.74  ? 1647 VAL A N     1 
ATOM   915   C  CA    . VAL A 1 1647 ? 186.547 251.713 199.472 1.00 77.19  ? 1647 VAL A CA    1 
ATOM   916   C  C     . VAL A 1 1647 ? 187.849 252.317 199.971 1.00 74.72  ? 1647 VAL A C     1 
ATOM   917   O  O     . VAL A 1 1647 ? 188.920 251.744 199.726 1.00 70.96  ? 1647 VAL A O     1 
ATOM   918   C  CB    . VAL A 1 1647 ? 186.551 251.674 197.932 1.00 74.44  ? 1647 VAL A CB    1 
ATOM   919   C  CG1   . VAL A 1 1647 ? 185.378 250.854 197.423 1.00 72.19  ? 1647 VAL A CG1   1 
ATOM   920   C  CG2   . VAL A 1 1647 ? 186.493 253.086 197.384 1.00 72.14  ? 1647 VAL A CG2   1 
ATOM   921   N  N     . ALA A 1 1648 ? 187.797 253.463 200.653 1.00 73.73  ? 1648 ALA A N     1 
ATOM   922   C  CA    . ALA A 1 1648 ? 189.020 254.086 201.149 1.00 71.06  ? 1648 ALA A CA    1 
ATOM   923   C  C     . ALA A 1 1648 ? 189.674 253.243 202.236 1.00 66.79  ? 1648 ALA A C     1 
ATOM   924   O  O     . ALA A 1 1648 ? 190.905 253.139 202.292 1.00 63.93  ? 1648 ALA A O     1 
ATOM   925   C  CB    . ALA A 1 1648 ? 188.721 255.493 201.666 1.00 69.01  ? 1648 ALA A CB    1 
ATOM   926   N  N     . LYS A 1 1649 ? 188.870 252.640 203.114 1.00 66.76  ? 1649 LYS A N     1 
ATOM   927   C  CA    . LYS A 1 1649 ? 189.426 251.849 204.208 1.00 69.03  ? 1649 LYS A CA    1 
ATOM   928   C  C     . LYS A 1 1649 ? 190.045 250.550 203.713 1.00 67.51  ? 1649 LYS A C     1 
ATOM   929   O  O     . LYS A 1 1649 ? 190.915 249.984 204.385 1.00 62.99  ? 1649 LYS A O     1 
ATOM   930   C  CB    . LYS A 1 1649 ? 188.344 251.553 205.246 1.00 68.97  ? 1649 LYS A CB    1 
ATOM   931   C  CG    . LYS A 1 1649 ? 188.178 252.634 206.298 1.00 68.74  ? 1649 LYS A CG    1 
ATOM   932   C  CD    . LYS A 1 1649 ? 187.528 252.080 207.555 1.00 75.35  ? 1649 LYS A CD    1 
ATOM   933   C  CE    . LYS A 1 1649 ? 186.897 253.185 208.385 1.00 77.54  ? 1649 LYS A CE    1 
ATOM   934   N  NZ    . LYS A 1 1649 ? 187.791 253.630 209.488 1.00 71.92  ? 1649 LYS A NZ    1 
ATOM   935   N  N     . LEU A 1 1650 ? 189.615 250.062 202.550 1.00 67.08  ? 1650 LEU A N     1 
ATOM   936   C  CA    . LEU A 1 1650 ? 190.103 248.795 202.024 1.00 63.88  ? 1650 LEU A CA    1 
ATOM   937   C  C     . LEU A 1 1650 ? 191.471 248.905 201.366 1.00 59.25  ? 1650 LEU A C     1 
ATOM   938   O  O     . LEU A 1 1650 ? 192.076 247.870 201.063 1.00 59.89  ? 1650 LEU A O     1 
ATOM   939   C  CB    . LEU A 1 1650 ? 189.103 248.227 201.015 1.00 58.99  ? 1650 LEU A CB    1 
ATOM   940   C  CG    . LEU A 1 1650 ? 188.106 247.190 201.527 1.00 62.20  ? 1650 LEU A CG    1 
ATOM   941   C  CD1   . LEU A 1 1650 ? 187.311 247.726 202.708 1.00 65.71  ? 1650 LEU A CD1   1 
ATOM   942   C  CD2   . LEU A 1 1650 ? 187.179 246.774 200.404 1.00 62.14  ? 1650 LEU A CD2   1 
ATOM   943   N  N     . GLN A 1 1651 ? 191.973 250.120 201.143 1.00 56.44  ? 1651 GLN A N     1 
ATOM   944   C  CA    . GLN A 1 1651 ? 193.207 250.297 200.388 1.00 56.20  ? 1651 GLN A CA    1 
ATOM   945   C  C     . GLN A 1 1651 ? 194.446 249.841 201.146 1.00 55.29  ? 1651 GLN A C     1 
ATOM   946   O  O     . GLN A 1 1651 ? 195.518 249.749 200.538 1.00 62.66  ? 1651 GLN A O     1 
ATOM   947   C  CB    . GLN A 1 1651 ? 193.360 251.763 199.979 1.00 49.04  ? 1651 GLN A CB    1 
ATOM   948   C  CG    . GLN A 1 1651 ? 192.247 252.268 199.073 1.00 52.65  ? 1651 GLN A CG    1 
ATOM   949   C  CD    . GLN A 1 1651 ? 192.620 252.220 197.605 1.00 44.70  ? 1651 GLN A CD    1 
ATOM   950   O  OE1   . GLN A 1 1651 ? 193.468 251.430 197.196 1.00 47.62  ? 1651 GLN A OE1   1 
ATOM   951   N  NE2   . GLN A 1 1651 ? 191.984 253.066 196.804 1.00 42.78  ? 1651 GLN A NE2   1 
ATOM   952   N  N     . LYS A 1 1652 ? 194.337 249.559 202.442 1.00 52.92  ? 1652 LYS A N     1 
ATOM   953   C  CA    . LYS A 1 1652 ? 195.474 249.093 203.227 1.00 53.83  ? 1652 LYS A CA    1 
ATOM   954   C  C     . LYS A 1 1652 ? 195.569 247.576 203.296 1.00 53.72  ? 1652 LYS A C     1 
ATOM   955   O  O     . LYS A 1 1652 ? 196.520 247.058 203.888 1.00 53.97  ? 1652 LYS A O     1 
ATOM   956   C  CB    . LYS A 1 1652 ? 195.409 249.666 204.646 1.00 52.69  ? 1652 LYS A CB    1 
ATOM   957   C  CG    . LYS A 1 1652 ? 194.221 249.185 205.459 1.00 50.21  ? 1652 LYS A CG    1 
ATOM   958   C  CD    . LYS A 1 1652 ? 194.239 249.776 206.856 1.00 47.33  ? 1652 LYS A CD    1 
ATOM   959   C  CE    . LYS A 1 1652 ? 193.868 251.249 206.838 1.00 59.12  ? 1652 LYS A CE    1 
ATOM   960   N  NZ    . LYS A 1 1652 ? 193.753 251.810 208.212 1.00 62.18  ? 1652 LYS A NZ    1 
ATOM   961   N  N     . HIS A 1 1653 ? 194.619 246.855 202.707 1.00 53.09  ? 1653 HIS A N     1 
ATOM   962   C  CA    . HIS A 1 1653 ? 194.590 245.401 202.771 1.00 49.26  ? 1653 HIS A CA    1 
ATOM   963   C  C     . HIS A 1 1653 ? 195.082 244.735 201.494 1.00 39.60  ? 1653 HIS A C     1 
ATOM   964   O  O     . HIS A 1 1653 ? 195.304 243.521 201.492 1.00 40.01  ? 1653 HIS A O     1 
ATOM   965   C  CB    . HIS A 1 1653 ? 193.173 244.920 203.090 1.00 50.38  ? 1653 HIS A CB    1 
ATOM   966   C  CG    . HIS A 1 1653 ? 192.607 245.505 204.346 1.00 57.34  ? 1653 HIS A CG    1 
ATOM   967   N  ND1   . HIS A 1 1653 ? 193.147 245.260 205.590 1.00 52.02  ? 1653 HIS A ND1   1 
ATOM   968   C  CD2   . HIS A 1 1653 ? 191.557 246.335 204.549 1.00 63.14  ? 1653 HIS A CD2   1 
ATOM   969   C  CE1   . HIS A 1 1653 ? 192.448 245.906 206.506 1.00 58.82  ? 1653 HIS A CE1   1 
ATOM   970   N  NE2   . HIS A 1 1653 ? 191.477 246.565 205.901 1.00 60.94  ? 1653 HIS A NE2   1 
ATOM   971   N  N     . PHE A 1 1654 ? 195.260 245.493 200.412 1.00 41.91  ? 1654 PHE A N     1 
ATOM   972   C  CA    . PHE A 1 1654 ? 195.715 244.907 199.159 1.00 39.82  ? 1654 PHE A CA    1 
ATOM   973   C  C     . PHE A 1 1654 ? 197.187 244.522 199.181 1.00 38.45  ? 1654 PHE A C     1 
ATOM   974   O  O     . PHE A 1 1654 ? 197.596 243.656 198.401 1.00 37.97  ? 1654 PHE A O     1 
ATOM   975   C  CB    . PHE A 1 1654 ? 195.442 245.870 198.003 1.00 38.40  ? 1654 PHE A CB    1 
ATOM   976   C  CG    . PHE A 1 1654 ? 193.983 246.075 197.726 1.00 39.46  ? 1654 PHE A CG    1 
ATOM   977   C  CD1   . PHE A 1 1654 ? 193.255 245.110 197.053 1.00 37.80  ? 1654 PHE A CD1   1 
ATOM   978   C  CD2   . PHE A 1 1654 ? 193.335 247.218 198.156 1.00 38.91  ? 1654 PHE A CD2   1 
ATOM   979   C  CE1   . PHE A 1 1654 ? 191.912 245.288 196.799 1.00 31.86  ? 1654 PHE A CE1   1 
ATOM   980   C  CE2   . PHE A 1 1654 ? 191.991 247.400 197.907 1.00 40.45  ? 1654 PHE A CE2   1 
ATOM   981   C  CZ    . PHE A 1 1654 ? 191.279 246.432 197.228 1.00 34.47  ? 1654 PHE A CZ    1 
ATOM   982   N  N     . LYS A 1 1655 ? 197.990 245.140 200.050 1.00 43.30  ? 1655 LYS A N     1 
ATOM   983   C  CA    . LYS A 1 1655 ? 199.400 244.776 200.126 1.00 35.62  ? 1655 LYS A CA    1 
ATOM   984   C  C     . LYS A 1 1655 ? 199.588 243.364 200.665 1.00 37.68  ? 1655 LYS A C     1 
ATOM   985   O  O     . LYS A 1 1655 ? 200.571 242.699 200.320 1.00 46.91  ? 1655 LYS A O     1 
ATOM   986   C  CB    . LYS A 1 1655 ? 200.162 245.784 200.987 1.00 29.44  ? 1655 LYS A CB    1 
ATOM   987   C  CG    . LYS A 1 1655 ? 199.635 245.924 202.404 1.00 43.15  ? 1655 LYS A CG    1 
ATOM   988   C  CD    . LYS A 1 1655 ? 200.458 246.925 203.202 1.00 45.67  ? 1655 LYS A CD    1 
ATOM   989   C  CE    . LYS A 1 1655 ? 199.851 247.167 204.575 1.00 46.93  ? 1655 LYS A CE    1 
ATOM   990   N  NZ    . LYS A 1 1655 ? 199.858 245.938 205.416 1.00 49.85  ? 1655 LYS A NZ    1 
ATOM   991   N  N     . LYS A 1 1656 ? 198.671 242.892 201.507 1.00 32.87  ? 1656 LYS A N     1 
ATOM   992   C  CA    . LYS A 1 1656 ? 198.760 241.555 202.076 1.00 34.05  ? 1656 LYS A CA    1 
ATOM   993   C  C     . LYS A 1 1656 ? 197.909 240.530 201.337 1.00 34.98  ? 1656 LYS A C     1 
ATOM   994   O  O     . LYS A 1 1656 ? 197.950 239.348 201.689 1.00 40.23  ? 1656 LYS A O     1 
ATOM   995   C  CB    . LYS A 1 1656 ? 198.372 241.584 203.557 1.00 45.31  ? 1656 LYS A CB    1 
ATOM   996   C  CG    . LYS A 1 1656 ? 196.972 242.095 203.836 1.00 44.10  ? 1656 LYS A CG    1 
ATOM   997   C  CD    . LYS A 1 1656 ? 196.669 242.063 205.323 1.00 42.90  ? 1656 LYS A CD    1 
ATOM   998   C  CE    . LYS A 1 1656 ? 195.760 243.208 205.728 1.00 49.25  ? 1656 LYS A CE    1 
ATOM   999   N  NZ    . LYS A 1 1656 ? 196.498 244.495 205.836 1.00 48.65  ? 1656 LYS A NZ    1 
ATOM   1000  N  N     . MET A 1 1657 ? 197.145 240.945 200.326 1.00 35.82  ? 1657 MET A N     1 
ATOM   1001  C  CA    . MET A 1 1657 ? 196.398 240.012 199.495 1.00 28.73  ? 1657 MET A CA    1 
ATOM   1002  C  C     . MET A 1 1657 ? 196.948 239.883 198.083 1.00 28.79  ? 1657 MET A C     1 
ATOM   1003  O  O     . MET A 1 1657 ? 196.500 238.999 197.344 1.00 33.41  ? 1657 MET A O     1 
ATOM   1004  C  CB    . MET A 1 1657 ? 194.917 240.415 199.409 1.00 31.74  ? 1657 MET A CB    1 
ATOM   1005  C  CG    . MET A 1 1657 ? 194.151 240.312 200.713 1.00 39.00  ? 1657 MET A CG    1 
ATOM   1006  S  SD    . MET A 1 1657 ? 192.411 240.737 200.508 1.00 48.82  ? 1657 MET A SD    1 
ATOM   1007  C  CE    . MET A 1 1657 ? 192.499 242.515 200.331 1.00 52.33  ? 1657 MET A CE    1 
ATOM   1008  N  N     . PHE A 1 1658 ? 197.891 240.733 197.685 1.00 29.68  ? 1658 PHE A N     1 
ATOM   1009  C  CA    . PHE A 1 1658 ? 198.445 240.702 196.341 1.00 22.25  ? 1658 PHE A CA    1 
ATOM   1010  C  C     . PHE A 1 1658 ? 199.949 240.916 196.401 1.00 23.85  ? 1658 PHE A C     1 
ATOM   1011  O  O     . PHE A 1 1658 ? 200.468 241.526 197.338 1.00 23.19  ? 1658 PHE A O     1 
ATOM   1012  C  CB    . PHE A 1 1658 ? 197.796 241.760 195.440 1.00 24.33  ? 1658 PHE A CB    1 
ATOM   1013  C  CG    . PHE A 1 1658 ? 196.343 241.506 195.151 1.00 24.12  ? 1658 PHE A CG    1 
ATOM   1014  C  CD1   . PHE A 1 1658 ? 195.359 241.999 195.990 1.00 26.53  ? 1658 PHE A CD1   1 
ATOM   1015  C  CD2   . PHE A 1 1658 ? 195.962 240.778 194.038 1.00 24.93  ? 1658 PHE A CD2   1 
ATOM   1016  C  CE1   . PHE A 1 1658 ? 194.024 241.767 195.725 1.00 27.71  ? 1658 PHE A CE1   1 
ATOM   1017  C  CE2   . PHE A 1 1658 ? 194.629 240.542 193.769 1.00 25.62  ? 1658 PHE A CE2   1 
ATOM   1018  C  CZ    . PHE A 1 1658 ? 193.658 241.038 194.613 1.00 27.82  ? 1658 PHE A CZ    1 
ATOM   1019  N  N     . ALA A 1 1659 ? 200.643 240.406 195.380 1.00 29.28  ? 1659 ALA A N     1 
ATOM   1020  C  CA    . ALA A 1 1659 ? 202.100 240.487 195.350 1.00 19.72  ? 1659 ALA A CA    1 
ATOM   1021  C  C     . ALA A 1 1659 ? 202.579 241.926 195.212 1.00 25.35  ? 1659 ALA A C     1 
ATOM   1022  O  O     . ALA A 1 1659 ? 203.436 242.381 195.976 1.00 37.15  ? 1659 ALA A O     1 
ATOM   1023  C  CB    . ALA A 1 1659 ? 202.648 239.631 194.209 1.00 16.27  ? 1659 ALA A CB    1 
ATOM   1024  N  N     . GLY A 1 1660 ? 202.038 242.657 194.241 1.00 20.26  ? 1660 GLY A N     1 
ATOM   1025  C  CA    . GLY A 1 1660 ? 202.524 243.993 193.966 1.00 18.96  ? 1660 GLY A CA    1 
ATOM   1026  C  C     . GLY A 1 1660 ? 201.445 245.051 193.898 1.00 28.58  ? 1660 GLY A C     1 
ATOM   1027  O  O     . GLY A 1 1660 ? 201.735 246.216 193.608 1.00 34.52  ? 1660 GLY A O     1 
ATOM   1028  N  N     . VAL A 1 1661 ? 200.199 244.668 194.158 1.00 28.45  ? 1661 VAL A N     1 
ATOM   1029  C  CA    . VAL A 1 1661 ? 199.095 245.623 194.166 1.00 29.18  ? 1661 VAL A CA    1 
ATOM   1030  C  C     . VAL A 1 1661 ? 199.071 246.301 195.531 1.00 33.64  ? 1661 VAL A C     1 
ATOM   1031  O  O     . VAL A 1 1661 ? 198.728 245.679 196.539 1.00 37.29  ? 1661 VAL A O     1 
ATOM   1032  C  CB    . VAL A 1 1661 ? 197.756 244.947 193.858 1.00 30.08  ? 1661 VAL A CB    1 
ATOM   1033  C  CG1   . VAL A 1 1661 ? 196.613 245.935 194.025 1.00 27.97  ? 1661 VAL A CG1   1 
ATOM   1034  C  CG2   . VAL A 1 1661 ? 197.765 244.373 192.454 1.00 24.96  ? 1661 VAL A CG2   1 
ATOM   1035  N  N     . SER A 1 1662 ? 199.449 247.577 195.567 1.00 32.75  ? 1662 SER A N     1 
ATOM   1036  C  CA    . SER A 1 1662 ? 199.424 248.343 196.804 1.00 31.98  ? 1662 SER A CA    1 
ATOM   1037  C  C     . SER A 1 1662 ? 198.124 249.113 196.982 1.00 39.66  ? 1662 SER A C     1 
ATOM   1038  O  O     . SER A 1 1662 ? 197.660 249.277 198.117 1.00 47.66  ? 1662 SER A O     1 
ATOM   1039  C  CB    . SER A 1 1662 ? 200.607 249.313 196.848 1.00 33.55  ? 1662 SER A CB    1 
ATOM   1040  O  OG    . SER A 1 1662 ? 200.667 249.990 198.091 1.00 40.60  ? 1662 SER A OG    1 
ATOM   1041  N  N     . SER A 1 1663 ? 197.528 249.582 195.889 1.00 37.23  ? 1663 SER A N     1 
ATOM   1042  C  CA    . SER A 1 1663 ? 196.274 250.316 195.950 1.00 33.34  ? 1663 SER A CA    1 
ATOM   1043  C  C     . SER A 1 1663 ? 195.505 250.084 194.659 1.00 32.09  ? 1663 SER A C     1 
ATOM   1044  O  O     . SER A 1 1663 ? 196.076 249.713 193.631 1.00 34.91  ? 1663 SER A O     1 
ATOM   1045  C  CB    . SER A 1 1663 ? 196.508 251.813 196.174 1.00 35.46  ? 1663 SER A CB    1 
ATOM   1046  O  OG    . SER A 1 1663 ? 197.235 252.381 195.099 1.00 32.41  ? 1663 SER A OG    1 
ATOM   1047  N  N     . ILE A 1 1664 ? 194.196 250.308 194.724 1.00 36.82  ? 1664 ILE A N     1 
ATOM   1048  C  CA    . ILE A 1 1664 ? 193.309 250.157 193.578 1.00 36.86  ? 1664 ILE A CA    1 
ATOM   1049  C  C     . ILE A 1 1664 ? 192.862 251.543 193.132 1.00 36.45  ? 1664 ILE A C     1 
ATOM   1050  O  O     . ILE A 1 1664 ? 192.414 252.354 193.951 1.00 44.75  ? 1664 ILE A O     1 
ATOM   1051  C  CB    . ILE A 1 1664 ? 192.105 249.256 193.905 1.00 30.58  ? 1664 ILE A CB    1 
ATOM   1052  C  CG1   . ILE A 1 1664 ? 191.447 249.676 195.220 1.00 30.26  ? 1664 ILE A CG1   1 
ATOM   1053  C  CG2   . ILE A 1 1664 ? 192.534 247.800 193.967 1.00 24.87  ? 1664 ILE A CG2   1 
ATOM   1054  C  CD1   . ILE A 1 1664 ? 190.052 249.121 195.405 1.00 36.13  ? 1664 ILE A CD1   1 
ATOM   1055  N  N     . ILE A 1 1665 ? 193.005 251.817 191.841 1.00 31.62  ? 1665 ILE A N     1 
ATOM   1056  C  CA    . ILE A 1 1665 ? 192.646 253.118 191.289 1.00 39.49  ? 1665 ILE A CA    1 
ATOM   1057  C  C     . ILE A 1 1665 ? 191.148 253.147 191.026 1.00 45.96  ? 1665 ILE A C     1 
ATOM   1058  O  O     . ILE A 1 1665 ? 190.598 252.234 190.402 1.00 41.55  ? 1665 ILE A O     1 
ATOM   1059  C  CB    . ILE A 1 1665 ? 193.440 253.400 190.003 1.00 35.47  ? 1665 ILE A CB    1 
ATOM   1060  C  CG1   . ILE A 1 1665 ? 194.946 253.362 190.279 1.00 32.27  ? 1665 ILE A CG1   1 
ATOM   1061  C  CG2   . ILE A 1 1665 ? 193.040 254.741 189.413 1.00 36.64  ? 1665 ILE A CG2   1 
ATOM   1062  C  CD1   . ILE A 1 1665 ? 195.371 254.156 191.493 1.00 34.52  ? 1665 ILE A CD1   1 
ATOM   1063  N  N     . LEU A 1 1666 ? 190.479 254.188 191.516 1.00 52.64  ? 1666 LEU A N     1 
ATOM   1064  C  CA    . LEU A 1 1666 ? 189.054 254.373 191.289 1.00 49.84  ? 1666 LEU A CA    1 
ATOM   1065  C  C     . LEU A 1 1666 ? 188.787 255.794 190.816 1.00 59.11  ? 1666 LEU A C     1 
ATOM   1066  O  O     . LEU A 1 1666 ? 189.588 256.707 191.030 1.00 61.58  ? 1666 LEU A O     1 
ATOM   1067  C  CB    . LEU A 1 1666 ? 188.217 254.086 192.546 1.00 51.36  ? 1666 LEU A CB    1 
ATOM   1068  C  CG    . LEU A 1 1666 ? 187.945 252.625 192.919 1.00 53.99  ? 1666 LEU A CG    1 
ATOM   1069  C  CD1   . LEU A 1 1666 ? 189.183 251.948 193.468 1.00 47.64  ? 1666 LEU A CD1   1 
ATOM   1070  C  CD2   . LEU A 1 1666 ? 186.789 252.514 193.895 1.00 58.43  ? 1666 LEU A CD2   1 
ATOM   1071  N  N     . ASN A 1 1667 ? 187.639 255.966 190.167 1.00 59.14  ? 1667 ASN A N     1 
ATOM   1072  C  CA    . ASN A 1 1667 ? 187.230 257.270 189.674 1.00 59.51  ? 1667 ASN A CA    1 
ATOM   1073  C  C     . ASN A 1 1667 ? 186.734 258.140 190.830 1.00 70.10  ? 1667 ASN A C     1 
ATOM   1074  O  O     . ASN A 1 1667 ? 186.811 257.773 192.006 1.00 67.66  ? 1667 ASN A O     1 
ATOM   1075  C  CB    . ASN A 1 1667 ? 186.155 257.114 188.602 1.00 57.30  ? 1667 ASN A CB    1 
ATOM   1076  C  CG    . ASN A 1 1667 ? 184.953 256.333 189.095 1.00 60.08  ? 1667 ASN A CG    1 
ATOM   1077  O  OD1   . ASN A 1 1667 ? 185.052 255.554 190.041 1.00 56.17  ? 1667 ASN A OD1   1 
ATOM   1078  N  ND2   . ASN A 1 1667 ? 183.812 256.535 188.449 1.00 64.19  ? 1667 ASN A ND2   1 
ATOM   1079  N  N     . GLU A 1 1668 ? 186.215 259.321 190.482 1.00 73.52  ? 1668 GLU A N     1 
ATOM   1080  C  CA    . GLU A 1 1668 ? 185.754 260.256 191.501 1.00 72.49  ? 1668 GLU A CA    1 
ATOM   1081  C  C     . GLU A 1 1668 ? 184.524 259.736 192.235 1.00 71.49  ? 1668 GLU A C     1 
ATOM   1082  O  O     . GLU A 1 1668 ? 184.282 260.115 193.386 1.00 73.08  ? 1668 GLU A O     1 
ATOM   1083  C  CB    . GLU A 1 1668 ? 185.461 261.615 190.868 1.00 67.64  ? 1668 GLU A CB    1 
ATOM   1084  C  CG    . GLU A 1 1668 ? 184.755 261.533 189.526 1.00 76.27  ? 1668 GLU A CG    1 
ATOM   1085  C  CD    . GLU A 1 1668 ? 184.386 262.896 188.977 1.00 84.76  ? 1668 GLU A CD    1 
ATOM   1086  O  OE1   . GLU A 1 1668 ? 184.507 263.891 189.722 1.00 89.17  ? 1668 GLU A OE1   1 
ATOM   1087  O  OE2   . GLU A 1 1668 ? 183.975 262.972 187.800 1.00 82.67  ? 1668 GLU A OE2   1 
ATOM   1088  N  N     . ASP A 1 1669 ? 183.739 258.873 191.593 1.00 66.03  ? 1669 ASP A N     1 
ATOM   1089  C  CA    . ASP A 1 1669 ? 182.540 258.326 192.213 1.00 70.22  ? 1669 ASP A CA    1 
ATOM   1090  C  C     . ASP A 1 1669 ? 182.833 257.174 193.165 1.00 70.70  ? 1669 ASP A C     1 
ATOM   1091  O  O     . ASP A 1 1669 ? 181.953 256.807 193.950 1.00 70.14  ? 1669 ASP A O     1 
ATOM   1092  C  CB    . ASP A 1 1669 ? 181.562 257.855 191.133 1.00 74.47  ? 1669 ASP A CB    1 
ATOM   1093  C  CG    . ASP A 1 1669 ? 180.113 258.068 191.523 1.00 80.27  ? 1669 ASP A CG    1 
ATOM   1094  O  OD1   . ASP A 1 1669 ? 179.819 258.128 192.735 1.00 80.96  ? 1669 ASP A OD1   1 
ATOM   1095  O  OD2   . ASP A 1 1669 ? 179.263 258.171 190.614 1.00 86.56  ? 1669 ASP A OD2   1 
ATOM   1096  N  N     . ASN A 1 1670 ? 184.038 256.603 193.113 1.00 72.07  ? 1670 ASN A N     1 
ATOM   1097  C  CA    . ASN A 1 1670 ? 184.395 255.427 193.909 1.00 64.88  ? 1670 ASN A CA    1 
ATOM   1098  C  C     . ASN A 1 1670 ? 183.412 254.286 193.666 1.00 62.94  ? 1670 ASN A C     1 
ATOM   1099  O  O     . ASN A 1 1670 ? 183.060 253.531 194.574 1.00 64.25  ? 1670 ASN A O     1 
ATOM   1100  C  CB    . ASN A 1 1670 ? 184.480 255.770 195.398 1.00 61.94  ? 1670 ASN A CB    1 
ATOM   1101  C  CG    . ASN A 1 1670 ? 185.650 256.675 195.720 1.00 67.25  ? 1670 ASN A CG    1 
ATOM   1102  O  OD1   . ASN A 1 1670 ? 185.977 257.581 194.954 1.00 69.62  ? 1670 ASN A OD1   1 
ATOM   1103  N  ND2   . ASN A 1 1670 ? 186.292 256.432 196.856 1.00 65.11  ? 1670 ASN A ND2   1 
ATOM   1104  N  N     . SER A 1 1671 ? 182.965 254.160 192.414 1.00 60.76  ? 1671 SER A N     1 
ATOM   1105  C  CA    . SER A 1 1671 ? 181.994 253.150 192.029 1.00 56.68  ? 1671 SER A CA    1 
ATOM   1106  C  C     . SER A 1 1671 ? 182.523 252.131 191.033 1.00 55.73  ? 1671 SER A C     1 
ATOM   1107  O  O     . SER A 1 1671 ? 181.946 251.044 190.930 1.00 57.00  ? 1671 SER A O     1 
ATOM   1108  C  CB    . SER A 1 1671 ? 180.741 253.810 191.431 1.00 65.93  ? 1671 SER A CB    1 
ATOM   1109  O  OG    . SER A 1 1671 ? 181.049 254.485 190.224 1.00 64.31  ? 1671 SER A OG    1 
ATOM   1110  N  N     . VAL A 1 1672 ? 183.587 252.445 190.299 1.00 56.60  ? 1672 VAL A N     1 
ATOM   1111  C  CA    . VAL A 1 1672 ? 184.208 251.515 189.365 1.00 48.32  ? 1672 VAL A CA    1 
ATOM   1112  C  C     . VAL A 1 1672 ? 185.697 251.447 189.670 1.00 48.17  ? 1672 VAL A C     1 
ATOM   1113  O  O     . VAL A 1 1672 ? 186.292 252.429 190.129 1.00 49.63  ? 1672 VAL A O     1 
ATOM   1114  C  CB    . VAL A 1 1672 ? 183.963 251.917 187.894 1.00 45.46  ? 1672 VAL A CB    1 
ATOM   1115  C  CG1   . VAL A 1 1672 ? 182.479 252.109 187.630 1.00 49.48  ? 1672 VAL A CG1   1 
ATOM   1116  C  CG2   . VAL A 1 1672 ? 184.728 253.181 187.546 1.00 47.22  ? 1672 VAL A CG2   1 
ATOM   1117  N  N     . VAL A 1 1673 ? 186.291 250.282 189.440 1.00 49.72  ? 1673 VAL A N     1 
ATOM   1118  C  CA    . VAL A 1 1673 ? 187.717 250.074 189.668 1.00 41.25  ? 1673 VAL A CA    1 
ATOM   1119  C  C     . VAL A 1 1673 ? 188.426 250.202 188.325 1.00 38.96  ? 1673 VAL A C     1 
ATOM   1120  O  O     . VAL A 1 1673 ? 188.366 249.296 187.491 1.00 40.95  ? 1673 VAL A O     1 
ATOM   1121  C  CB    . VAL A 1 1673 ? 187.993 248.714 190.319 1.00 33.82  ? 1673 VAL A CB    1 
ATOM   1122  C  CG1   . VAL A 1 1673 ? 189.478 248.547 190.585 1.00 34.60  ? 1673 VAL A CG1   1 
ATOM   1123  C  CG2   . VAL A 1 1673 ? 187.199 248.574 191.608 1.00 39.34  ? 1673 VAL A CG2   1 
ATOM   1124  N  N     . LEU A 1 1674 ? 189.102 251.333 188.118 1.00 38.57  ? 1674 LEU A N     1 
ATOM   1125  C  CA    . LEU A 1 1674 ? 189.747 251.601 186.840 1.00 38.73  ? 1674 LEU A CA    1 
ATOM   1126  C  C     . LEU A 1 1674 ? 191.023 250.784 186.664 1.00 32.20  ? 1674 LEU A C     1 
ATOM   1127  O  O     . LEU A 1 1674 ? 191.360 250.396 185.542 1.00 33.62  ? 1674 LEU A O     1 
ATOM   1128  C  CB    . LEU A 1 1674 ? 190.050 253.094 186.714 1.00 39.11  ? 1674 LEU A CB    1 
ATOM   1129  C  CG    . LEU A 1 1674 ? 188.843 254.030 186.720 1.00 31.82  ? 1674 LEU A CG    1 
ATOM   1130  C  CD1   . LEU A 1 1674 ? 189.290 255.471 186.545 1.00 39.73  ? 1674 LEU A CD1   1 
ATOM   1131  C  CD2   . LEU A 1 1674 ? 187.862 253.635 185.632 1.00 29.80  ? 1674 LEU A CD2   1 
ATOM   1132  N  N     . GLY A 1 1675 ? 191.742 250.525 187.745 1.00 31.05  ? 1675 GLY A N     1 
ATOM   1133  C  CA    . GLY A 1 1675 ? 192.973 249.773 187.638 1.00 27.17  ? 1675 GLY A CA    1 
ATOM   1134  C  C     . GLY A 1 1675 ? 193.592 249.498 188.988 1.00 29.79  ? 1675 GLY A C     1 
ATOM   1135  O  O     . GLY A 1 1675 ? 192.921 249.540 190.020 1.00 27.65  ? 1675 GLY A O     1 
ATOM   1136  N  N     . ILE A 1 1676 ? 194.893 249.209 188.961 1.00 25.31  ? 1676 ILE A N     1 
ATOM   1137  C  CA    . ILE A 1 1676 ? 195.660 248.900 190.159 1.00 26.31  ? 1676 ILE A CA    1 
ATOM   1138  C  C     . ILE A 1 1676 ? 196.933 249.734 190.158 1.00 26.64  ? 1676 ILE A C     1 
ATOM   1139  O  O     . ILE A 1 1676 ? 197.380 250.227 189.122 1.00 28.18  ? 1676 ILE A O     1 
ATOM   1140  C  CB    . ILE A 1 1676 ? 196.017 247.404 190.261 1.00 24.71  ? 1676 ILE A CB    1 
ATOM   1141  C  CG1   . ILE A 1 1676 ? 196.606 246.920 188.936 1.00 25.82  ? 1676 ILE A CG1   1 
ATOM   1142  C  CG2   . ILE A 1 1676 ? 194.800 246.587 190.657 1.00 19.46  ? 1676 ILE A CG2   1 
ATOM   1143  C  CD1   . ILE A 1 1676 ? 197.096 245.506 188.968 1.00 19.24  ? 1676 ILE A CD1   1 
ATOM   1144  N  N     . SER A 1 1677 ? 197.525 249.873 191.342 1.00 27.04  ? 1677 SER A N     1 
ATOM   1145  C  CA    . SER A 1 1677 ? 198.764 250.616 191.508 1.00 27.79  ? 1677 SER A CA    1 
ATOM   1146  C  C     . SER A 1 1677 ? 199.688 249.852 192.446 1.00 30.81  ? 1677 SER A C     1 
ATOM   1147  O  O     . SER A 1 1677 ? 199.244 249.068 193.287 1.00 34.43  ? 1677 SER A O     1 
ATOM   1148  C  CB    . SER A 1 1677 ? 198.508 252.029 192.046 1.00 29.34  ? 1677 SER A CB    1 
ATOM   1149  O  OG    . SER A 1 1677 ? 199.724 252.714 192.284 1.00 32.03  ? 1677 SER A OG    1 
ATOM   1150  N  N     . SER A 1 1678 ? 200.986 250.092 192.291 1.00 27.66  ? 1678 SER A N     1 
ATOM   1151  C  CA    . SER A 1 1678 ? 202.016 249.445 193.088 1.00 28.28  ? 1678 SER A CA    1 
ATOM   1152  C  C     . SER A 1 1678 ? 202.602 250.436 194.091 1.00 35.99  ? 1678 SER A C     1 
ATOM   1153  O  O     . SER A 1 1678 ? 202.247 251.616 194.121 1.00 43.93  ? 1678 SER A O     1 
ATOM   1154  C  CB    . SER A 1 1678 ? 203.109 248.865 192.188 1.00 31.29  ? 1678 SER A CB    1 
ATOM   1155  O  OG    . SER A 1 1678 ? 203.887 249.894 191.605 1.00 30.19  ? 1678 SER A OG    1 
ATOM   1156  N  N     . ARG A 1 1679 ? 203.513 249.932 194.927 1.00 35.44  ? 1679 ARG A N     1 
ATOM   1157  C  CA    . ARG A 1 1679 ? 204.175 250.785 195.909 1.00 34.97  ? 1679 ARG A CA    1 
ATOM   1158  C  C     . ARG A 1 1679 ? 205.041 251.840 195.233 1.00 36.66  ? 1679 ARG A C     1 
ATOM   1159  O  O     . ARG A 1 1679 ? 205.081 252.995 195.673 1.00 43.49  ? 1679 ARG A O     1 
ATOM   1160  C  CB    . ARG A 1 1679 ? 205.012 249.936 196.867 1.00 30.12  ? 1679 ARG A CB    1 
ATOM   1161  C  CG    . ARG A 1 1679 ? 204.228 248.865 197.609 1.00 38.11  ? 1679 ARG A CG    1 
ATOM   1162  C  CD    . ARG A 1 1679 ? 204.327 247.513 196.912 1.00 47.73  ? 1679 ARG A CD    1 
ATOM   1163  N  NE    . ARG A 1 1679 ? 203.518 246.495 197.573 1.00 54.52  ? 1679 ARG A NE    1 
ATOM   1164  C  CZ    . ARG A 1 1679 ? 203.952 245.711 198.550 1.00 58.12  ? 1679 ARG A CZ    1 
ATOM   1165  N  NH1   . ARG A 1 1679 ? 205.190 245.797 199.007 1.00 59.33  ? 1679 ARG A NH1   1 
ATOM   1166  N  NH2   . ARG A 1 1679 ? 203.124 244.815 199.078 1.00 47.11  ? 1679 ARG A NH2   1 
ATOM   1167  N  N     . GLU A 1 1680 ? 205.739 251.465 194.160 1.00 33.86  ? 1680 GLU A N     1 
ATOM   1168  C  CA    . GLU A 1 1680 ? 206.580 252.406 193.431 1.00 32.35  ? 1680 GLU A CA    1 
ATOM   1169  C  C     . GLU A 1 1680 ? 205.776 253.432 192.647 1.00 28.27  ? 1680 GLU A C     1 
ATOM   1170  O  O     . GLU A 1 1680 ? 206.365 254.380 192.116 1.00 32.28  ? 1680 GLU A O     1 
ATOM   1171  C  CB    . GLU A 1 1680 ? 207.511 251.650 192.482 1.00 32.74  ? 1680 GLU A CB    1 
ATOM   1172  C  CG    . GLU A 1 1680 ? 208.608 250.874 193.186 1.00 34.42  ? 1680 GLU A CG    1 
ATOM   1173  C  CD    . GLU A 1 1680 ? 208.326 249.387 193.238 1.00 34.04  ? 1680 GLU A CD    1 
ATOM   1174  O  OE1   . GLU A 1 1680 ? 207.317 248.952 192.646 1.00 29.01  ? 1680 GLU A OE1   1 
ATOM   1175  O  OE2   . GLU A 1 1680 ? 209.112 248.656 193.876 1.00 33.36  ? 1680 GLU A OE2   1 
ATOM   1176  N  N     . GLY A 1 1681 ? 204.459 253.266 192.555 1.00 26.02  ? 1681 GLY A N     1 
ATOM   1177  C  CA    . GLY A 1 1681 ? 203.613 254.171 191.811 1.00 31.09  ? 1681 GLY A CA    1 
ATOM   1178  C  C     . GLY A 1 1681 ? 203.242 253.691 190.426 1.00 33.69  ? 1681 GLY A C     1 
ATOM   1179  O  O     . GLY A 1 1681 ? 202.335 254.267 189.812 1.00 38.82  ? 1681 GLY A O     1 
ATOM   1180  N  N     . GLU A 1 1682 ? 203.917 252.663 189.916 1.00 31.45  ? 1682 GLU A N     1 
ATOM   1181  C  CA    . GLU A 1 1682 ? 203.547 252.093 188.630 1.00 26.92  ? 1682 GLU A CA    1 
ATOM   1182  C  C     . GLU A 1 1682 ? 202.136 251.525 188.700 1.00 25.37  ? 1682 GLU A C     1 
ATOM   1183  O  O     . GLU A 1 1682 ? 201.776 250.826 189.649 1.00 26.93  ? 1682 GLU A O     1 
ATOM   1184  C  CB    . GLU A 1 1682 ? 204.539 251.003 188.228 1.00 25.94  ? 1682 GLU A CB    1 
ATOM   1185  C  CG    . GLU A 1 1682 ? 204.384 250.514 186.801 1.00 23.81  ? 1682 GLU A CG    1 
ATOM   1186  C  CD    . GLU A 1 1682 ? 205.137 249.226 186.547 1.00 20.95  ? 1682 GLU A CD    1 
ATOM   1187  O  OE1   . GLU A 1 1682 ? 204.692 248.168 187.034 1.00 24.83  ? 1682 GLU A OE1   1 
ATOM   1188  O  OE2   . GLU A 1 1682 ? 206.178 249.271 185.859 1.00 22.81  ? 1682 GLU A OE2   1 
ATOM   1189  N  N     . GLU A 1 1683 ? 201.335 251.830 187.684 1.00 25.24  ? 1683 GLU A N     1 
ATOM   1190  C  CA    . GLU A 1 1683 ? 199.928 251.467 187.679 1.00 29.91  ? 1683 GLU A CA    1 
ATOM   1191  C  C     . GLU A 1 1683 ? 199.590 250.694 186.415 1.00 26.66  ? 1683 GLU A C     1 
ATOM   1192  O  O     . GLU A 1 1683 ? 200.208 250.877 185.364 1.00 29.96  ? 1683 GLU A O     1 
ATOM   1193  C  CB    . GLU A 1 1683 ? 199.029 252.706 187.789 1.00 32.73  ? 1683 GLU A CB    1 
ATOM   1194  C  CG    . GLU A 1 1683 ? 199.109 253.641 186.597 1.00 38.79  ? 1683 GLU A CG    1 
ATOM   1195  C  CD    . GLU A 1 1683 ? 198.257 254.878 186.777 1.00 52.72  ? 1683 GLU A CD    1 
ATOM   1196  O  OE1   . GLU A 1 1683 ? 197.623 255.013 187.844 1.00 58.53  ? 1683 GLU A OE1   1 
ATOM   1197  O  OE2   . GLU A 1 1683 ? 198.222 255.717 185.852 1.00 59.27  ? 1683 GLU A OE2   1 
ATOM   1198  N  N     . VAL A 1 1684 ? 198.600 249.816 186.541 1.00 23.43  ? 1684 VAL A N     1 
ATOM   1199  C  CA    . VAL A 1 1684 ? 198.064 249.046 185.427 1.00 23.00  ? 1684 VAL A CA    1 
ATOM   1200  C  C     . VAL A 1 1684 ? 196.606 249.441 185.262 1.00 26.75  ? 1684 VAL A C     1 
ATOM   1201  O  O     . VAL A 1 1684 ? 195.806 249.288 186.193 1.00 33.02  ? 1684 VAL A O     1 
ATOM   1202  C  CB    . VAL A 1 1684 ? 198.198 247.532 185.656 1.00 24.56  ? 1684 VAL A CB    1 
ATOM   1203  C  CG1   . VAL A 1 1684 ? 197.887 246.776 184.377 1.00 21.40  ? 1684 VAL A CG1   1 
ATOM   1204  C  CG2   . VAL A 1 1684 ? 199.589 247.189 186.160 1.00 24.25  ? 1684 VAL A CG2   1 
ATOM   1205  N  N     . MET A 1 1685 ? 196.263 249.945 184.080 1.00 25.80  ? 1685 MET A N     1 
ATOM   1206  C  CA    . MET A 1 1685 ? 194.910 250.400 183.793 1.00 23.28  ? 1685 MET A CA    1 
ATOM   1207  C  C     . MET A 1 1685 ? 194.114 249.255 183.180 1.00 29.78  ? 1685 MET A C     1 
ATOM   1208  O  O     . MET A 1 1685 ? 194.483 248.732 182.122 1.00 35.60  ? 1685 MET A O     1 
ATOM   1209  C  CB    . MET A 1 1685 ? 194.939 251.606 182.854 1.00 26.88  ? 1685 MET A CB    1 
ATOM   1210  C  CG    . MET A 1 1685 ? 195.481 252.877 183.492 1.00 29.34  ? 1685 MET A CG    1 
ATOM   1211  S  SD    . MET A 1 1685 ? 194.592 253.396 184.975 1.00 53.54  ? 1685 MET A SD    1 
ATOM   1212  C  CE    . MET A 1 1685 ? 192.888 253.214 184.447 1.00 31.62  ? 1685 MET A CE    1 
ATOM   1213  N  N     . PHE A 1 1686 ? 193.025 248.874 183.842 1.00 29.00  ? 1686 PHE A N     1 
ATOM   1214  C  CA    . PHE A 1 1686 ? 192.224 247.744 183.393 1.00 24.23  ? 1686 PHE A CA    1 
ATOM   1215  C  C     . PHE A 1 1686 ? 191.627 248.015 182.018 1.00 29.63  ? 1686 PHE A C     1 
ATOM   1216  O  O     . PHE A 1 1686 ? 191.158 249.120 181.732 1.00 35.94  ? 1686 PHE A O     1 
ATOM   1217  C  CB    . PHE A 1 1686 ? 191.108 247.456 184.396 1.00 27.36  ? 1686 PHE A CB    1 
ATOM   1218  C  CG    . PHE A 1 1686 ? 191.590 246.905 185.705 1.00 28.84  ? 1686 PHE A CG    1 
ATOM   1219  C  CD1   . PHE A 1 1686 ? 192.868 246.392 185.829 1.00 28.84  ? 1686 PHE A CD1   1 
ATOM   1220  C  CD2   . PHE A 1 1686 ? 190.759 246.893 186.812 1.00 27.78  ? 1686 PHE A CD2   1 
ATOM   1221  C  CE1   . PHE A 1 1686 ? 193.310 245.884 187.031 1.00 27.19  ? 1686 PHE A CE1   1 
ATOM   1222  C  CE2   . PHE A 1 1686 ? 191.197 246.385 188.017 1.00 24.86  ? 1686 PHE A CE2   1 
ATOM   1223  C  CZ    . PHE A 1 1686 ? 192.474 245.879 188.126 1.00 24.92  ? 1686 PHE A CZ    1 
ATOM   1224  N  N     . LYS A 1 1687 ? 191.650 246.991 181.163 1.00 33.23  ? 1687 LYS A N     1 
ATOM   1225  C  CA    . LYS A 1 1687 ? 191.019 247.111 179.853 1.00 37.55  ? 1687 LYS A CA    1 
ATOM   1226  C  C     . LYS A 1 1687 ? 189.515 247.316 179.992 1.00 37.22  ? 1687 LYS A C     1 
ATOM   1227  O  O     . LYS A 1 1687 ? 188.927 248.154 179.299 1.00 36.37  ? 1687 LYS A O     1 
ATOM   1228  C  CB    . LYS A 1 1687 ? 191.318 245.872 179.012 1.00 34.91  ? 1687 LYS A CB    1 
ATOM   1229  C  CG    . LYS A 1 1687 ? 192.785 245.705 178.657 1.00 31.34  ? 1687 LYS A CG    1 
ATOM   1230  C  CD    . LYS A 1 1687 ? 193.333 246.936 177.964 1.00 32.48  ? 1687 LYS A CD    1 
ATOM   1231  C  CE    . LYS A 1 1687 ? 194.453 246.570 177.003 1.00 39.83  ? 1687 LYS A CE    1 
ATOM   1232  N  NZ    . LYS A 1 1687 ? 195.508 247.618 176.959 1.00 38.78  ? 1687 LYS A NZ    1 
ATOM   1233  N  N     . THR A 1 1688 ? 188.882 246.559 180.879 1.00 35.77  ? 1688 THR A N     1 
ATOM   1234  C  CA    . THR A 1 1688 ? 187.467 246.731 181.204 1.00 35.36  ? 1688 THR A CA    1 
ATOM   1235  C  C     . THR A 1 1688 ? 187.342 246.974 182.701 1.00 34.54  ? 1688 THR A C     1 
ATOM   1236  O  O     . THR A 1 1688 ? 187.536 246.033 183.494 1.00 36.10  ? 1688 THR A O     1 
ATOM   1237  C  CB    . THR A 1 1688 ? 186.652 245.507 180.788 1.00 34.30  ? 1688 THR A CB    1 
ATOM   1238  O  OG1   . THR A 1 1688 ? 187.327 244.316 181.209 1.00 38.17  ? 1688 THR A OG1   1 
ATOM   1239  C  CG2   . THR A 1 1688 ? 186.478 245.475 179.278 1.00 30.21  ? 1688 THR A CG2   1 
ATOM   1240  N  N     . PRO A 1 1689 ? 187.040 248.196 183.138 1.00 34.07  ? 1689 PRO A N     1 
ATOM   1241  C  CA    . PRO A 1 1689 ? 186.986 248.472 184.578 1.00 39.56  ? 1689 PRO A CA    1 
ATOM   1242  C  C     . PRO A 1 1689 ? 185.893 247.675 185.273 1.00 36.30  ? 1689 PRO A C     1 
ATOM   1243  O  O     . PRO A 1 1689 ? 184.852 247.362 184.691 1.00 33.96  ? 1689 PRO A O     1 
ATOM   1244  C  CB    . PRO A 1 1689 ? 186.709 249.979 184.644 1.00 38.76  ? 1689 PRO A CB    1 
ATOM   1245  C  CG    . PRO A 1 1689 ? 186.142 250.331 183.311 1.00 34.64  ? 1689 PRO A CG    1 
ATOM   1246  C  CD    . PRO A 1 1689 ? 186.765 249.393 182.327 1.00 28.22  ? 1689 PRO A CD    1 
ATOM   1247  N  N     . VAL A 1 1690 ? 186.146 247.344 186.534 1.00 38.29  ? 1690 VAL A N     1 
ATOM   1248  C  CA    . VAL A 1 1690 ? 185.209 246.584 187.352 1.00 43.24  ? 1690 VAL A CA    1 
ATOM   1249  C  C     . VAL A 1 1690 ? 184.262 247.559 188.040 1.00 43.79  ? 1690 VAL A C     1 
ATOM   1250  O  O     . VAL A 1 1690 ? 184.700 248.440 188.786 1.00 43.33  ? 1690 VAL A O     1 
ATOM   1251  C  CB    . VAL A 1 1690 ? 185.947 245.715 188.382 1.00 45.89  ? 1690 VAL A CB    1 
ATOM   1252  C  CG1   . VAL A 1 1690 ? 184.953 245.014 189.293 1.00 39.99  ? 1690 VAL A CG1   1 
ATOM   1253  C  CG2   . VAL A 1 1690 ? 186.843 244.707 187.681 1.00 41.72  ? 1690 VAL A CG2   1 
ATOM   1254  N  N     . SER A 1 1691 ? 182.965 247.392 187.803 1.00 51.19  ? 1691 SER A N     1 
ATOM   1255  C  CA    . SER A 1 1691 ? 181.949 248.268 188.372 1.00 53.85  ? 1691 SER A CA    1 
ATOM   1256  C  C     . SER A 1 1691 ? 181.444 247.680 189.684 1.00 54.06  ? 1691 SER A C     1 
ATOM   1257  O  O     . SER A 1 1691 ? 180.861 246.591 189.700 1.00 51.84  ? 1691 SER A O     1 
ATOM   1258  C  CB    . SER A 1 1691 ? 180.795 248.457 187.388 1.00 51.61  ? 1691 SER A CB    1 
ATOM   1259  O  OG    . SER A 1 1691 ? 180.320 247.207 186.924 1.00 57.23  ? 1691 SER A OG    1 
ATOM   1260  N  N     . ILE A 1 1692 ? 181.671 248.403 190.783 1.00 53.95  ? 1692 ILE A N     1 
ATOM   1261  C  CA    . ILE A 1 1692 ? 181.210 247.941 192.088 1.00 52.37  ? 1692 ILE A CA    1 
ATOM   1262  C  C     . ILE A 1 1692 ? 179.692 248.025 192.188 1.00 59.72  ? 1692 ILE A C     1 
ATOM   1263  O  O     . ILE A 1 1692 ? 179.066 247.235 192.906 1.00 60.28  ? 1692 ILE A O     1 
ATOM   1264  C  CB    . ILE A 1 1692 ? 181.901 248.740 193.208 1.00 47.72  ? 1692 ILE A CB    1 
ATOM   1265  C  CG1   . ILE A 1 1692 ? 183.414 248.747 192.996 1.00 46.41  ? 1692 ILE A CG1   1 
ATOM   1266  C  CG2   . ILE A 1 1692 ? 181.567 248.154 194.571 1.00 46.97  ? 1692 ILE A CG2   1 
ATOM   1267  C  CD1   . ILE A 1 1692 ? 184.177 249.486 194.069 1.00 45.99  ? 1692 ILE A CD1   1 
ATOM   1268  N  N     . THR A 1 1693 ? 179.073 248.979 191.488 1.00 60.66  ? 1693 THR A N     1 
ATOM   1269  C  CA    . THR A 1 1693 ? 177.620 249.102 191.533 1.00 58.26  ? 1693 THR A CA    1 
ATOM   1270  C  C     . THR A 1 1693 ? 176.938 247.866 190.957 1.00 62.58  ? 1693 THR A C     1 
ATOM   1271  O  O     . THR A 1 1693 ? 175.950 247.375 191.518 1.00 67.87  ? 1693 THR A O     1 
ATOM   1272  C  CB    . THR A 1 1693 ? 177.172 250.355 190.782 1.00 61.55  ? 1693 THR A CB    1 
ATOM   1273  O  OG1   . THR A 1 1693 ? 177.568 250.259 189.408 1.00 69.33  ? 1693 THR A OG1   1 
ATOM   1274  C  CG2   . THR A 1 1693 ? 177.795 251.595 191.399 1.00 62.15  ? 1693 THR A CG2   1 
ATOM   1275  N  N     . GLU A 1 1694 ? 177.450 247.346 189.840 1.00 58.97  ? 1694 GLU A N     1 
ATOM   1276  C  CA    . GLU A 1 1694 ? 176.851 246.162 189.234 1.00 58.95  ? 1694 GLU A CA    1 
ATOM   1277  C  C     . GLU A 1 1694 ? 177.133 244.894 190.030 1.00 58.68  ? 1694 GLU A C     1 
ATOM   1278  O  O     . GLU A 1 1694 ? 176.402 243.911 189.877 1.00 62.03  ? 1694 GLU A O     1 
ATOM   1279  C  CB    . GLU A 1 1694 ? 177.344 245.994 187.797 1.00 60.10  ? 1694 GLU A CB    1 
ATOM   1280  C  CG    . GLU A 1 1694 ? 177.069 247.186 186.899 1.00 61.84  ? 1694 GLU A CG    1 
ATOM   1281  C  CD    . GLU A 1 1694 ? 177.235 246.854 185.430 1.00 75.64  ? 1694 GLU A CD    1 
ATOM   1282  O  OE1   . GLU A 1 1694 ? 177.307 245.653 185.097 1.00 79.17  ? 1694 GLU A OE1   1 
ATOM   1283  O  OE2   . GLU A 1 1694 ? 177.293 247.792 184.608 1.00 73.91  ? 1694 GLU A OE2   1 
ATOM   1284  N  N     . HIS A 1 1695 ? 178.171 244.891 190.864 1.00 54.99  ? 1695 HIS A N     1 
ATOM   1285  C  CA    . HIS A 1 1695 ? 178.497 243.757 191.730 1.00 58.96  ? 1695 HIS A CA    1 
ATOM   1286  C  C     . HIS A 1 1695 ? 178.710 244.279 193.144 1.00 63.85  ? 1695 HIS A C     1 
ATOM   1287  O  O     . HIS A 1 1695 ? 179.852 244.442 193.595 1.00 62.22  ? 1695 HIS A O     1 
ATOM   1288  C  CB    . HIS A 1 1695 ? 179.723 243.002 191.216 1.00 53.65  ? 1695 HIS A CB    1 
ATOM   1289  C  CG    . HIS A 1 1695 ? 179.492 242.293 189.918 1.00 62.34  ? 1695 HIS A CG    1 
ATOM   1290  N  ND1   . HIS A 1 1695 ? 179.101 240.973 189.851 1.00 64.69  ? 1695 HIS A ND1   1 
ATOM   1291  C  CD2   . HIS A 1 1695 ? 179.591 242.722 188.638 1.00 62.55  ? 1695 HIS A CD2   1 
ATOM   1292  C  CE1   . HIS A 1 1695 ? 178.972 240.618 188.584 1.00 62.32  ? 1695 HIS A CE1   1 
ATOM   1293  N  NE2   . HIS A 1 1695 ? 179.263 241.661 187.828 1.00 66.60  ? 1695 HIS A NE2   1 
ATOM   1294  N  N     . PRO A 1 1696 ? 177.627 244.572 193.868 1.00 63.75  ? 1696 PRO A N     1 
ATOM   1295  C  CA    . PRO A 1 1696 ? 177.776 245.153 195.214 1.00 59.86  ? 1696 PRO A CA    1 
ATOM   1296  C  C     . PRO A 1 1696 ? 178.532 244.269 196.189 1.00 62.10  ? 1696 PRO A C     1 
ATOM   1297  O  O     . PRO A 1 1696 ? 179.222 244.796 197.072 1.00 63.90  ? 1696 PRO A O     1 
ATOM   1298  C  CB    . PRO A 1 1696 ? 176.324 245.363 195.663 1.00 62.84  ? 1696 PRO A CB    1 
ATOM   1299  C  CG    . PRO A 1 1696 ? 175.547 245.468 194.397 1.00 70.14  ? 1696 PRO A CG    1 
ATOM   1300  C  CD    . PRO A 1 1696 ? 176.220 244.536 193.434 1.00 59.44  ? 1696 PRO A CD    1 
ATOM   1301  N  N     . LYS A 1 1697 ? 178.418 242.949 196.071 1.00 64.17  ? 1697 LYS A N     1 
ATOM   1302  C  CA    . LYS A 1 1697 ? 179.050 242.054 197.031 1.00 61.79  ? 1697 LYS A CA    1 
ATOM   1303  C  C     . LYS A 1 1697 ? 180.567 242.160 196.958 1.00 60.41  ? 1697 LYS A C     1 
ATOM   1304  O  O     . LYS A 1 1697 ? 181.151 242.222 195.872 1.00 58.18  ? 1697 LYS A O     1 
ATOM   1305  C  CB    . LYS A 1 1697 ? 178.605 240.612 196.792 1.00 63.65  ? 1697 LYS A CB    1 
ATOM   1306  C  CG    . LYS A 1 1697 ? 177.195 240.315 197.293 1.00 64.87  ? 1697 LYS A CG    1 
ATOM   1307  C  CD    . LYS A 1 1697 ? 176.886 238.819 197.324 1.00 67.12  ? 1697 LYS A CD    1 
ATOM   1308  C  CE    . LYS A 1 1697 ? 177.422 238.066 196.111 1.00 70.38  ? 1697 LYS A CE    1 
ATOM   1309  N  NZ    . LYS A 1 1697 ? 177.076 238.726 194.820 1.00 73.20  ? 1697 LYS A NZ    1 
ATOM   1310  N  N     . ILE A 1 1698 ? 181.204 242.164 198.132 1.00 60.31  ? 1698 ILE A N     1 
ATOM   1311  C  CA    . ILE A 1 1698 ? 182.643 242.408 198.220 1.00 57.78  ? 1698 ILE A CA    1 
ATOM   1312  C  C     . ILE A 1 1698 ? 183.424 241.322 197.484 1.00 55.97  ? 1698 ILE A C     1 
ATOM   1313  O  O     . ILE A 1 1698 ? 184.331 241.611 196.689 1.00 52.24  ? 1698 ILE A O     1 
ATOM   1314  C  CB    . ILE A 1 1698 ? 183.067 242.532 199.699 1.00 57.35  ? 1698 ILE A CB    1 
ATOM   1315  C  CG1   . ILE A 1 1698 ? 184.487 243.081 199.823 1.00 52.00  ? 1698 ILE A CG1   1 
ATOM   1316  C  CG2   . ILE A 1 1698 ? 182.873 241.231 200.482 1.00 61.97  ? 1698 ILE A CG2   1 
ATOM   1317  C  CD1   . ILE A 1 1698 ? 184.623 244.485 199.349 1.00 56.44  ? 1698 ILE A CD1   1 
ATOM   1318  N  N     . ASN A 1 1699 ? 183.065 240.057 197.716 1.00 55.71  ? 1699 ASN A N     1 
ATOM   1319  C  CA    . ASN A 1 1699 ? 183.820 238.953 197.138 1.00 54.18  ? 1699 ASN A CA    1 
ATOM   1320  C  C     . ASN A 1 1699 ? 183.723 238.950 195.619 1.00 58.19  ? 1699 ASN A C     1 
ATOM   1321  O  O     . ASN A 1 1699 ? 184.717 238.701 194.927 1.00 58.45  ? 1699 ASN A O     1 
ATOM   1322  C  CB    . ASN A 1 1699 ? 183.341 237.624 197.729 1.00 59.10  ? 1699 ASN A CB    1 
ATOM   1323  C  CG    . ASN A 1 1699 ? 181.880 237.325 197.423 1.00 68.02  ? 1699 ASN A CG    1 
ATOM   1324  O  OD1   . ASN A 1 1699 ? 181.221 238.047 196.673 1.00 64.89  ? 1699 ASN A OD1   1 
ATOM   1325  N  ND2   . ASN A 1 1699 ? 181.367 236.249 198.006 1.00 70.77  ? 1699 ASN A ND2   1 
ATOM   1326  N  N     . GLU A 1 1700 ? 182.537 239.242 195.082 1.00 58.05  ? 1700 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1700 ? 182.354 239.191 193.637 1.00 56.05  ? 1700 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1700 ? 183.213 240.229 192.929 1.00 53.97  ? 1700 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1700 ? 183.929 239.904 191.974 1.00 55.56  ? 1700 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1700 ? 180.878 239.373 193.280 1.00 62.78  ? 1700 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1700 ? 180.090 238.072 193.266 1.00 71.53  ? 1700 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1700 ? 178.868 238.138 192.371 1.00 77.51  ? 1700 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1700 ? 178.559 239.235 191.860 1.00 74.07  ? 1700 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1700 ? 178.217 237.090 192.175 1.00 80.63  ? 1700 GLU A OE2   1 
ATOM   1335  N  N     . TRP A 1 1701 ? 183.175 241.487 193.382 1.00 48.84  ? 1701 TRP A N     1 
ATOM   1336  C  CA    . TRP A 1 1701 ? 183.928 242.490 192.638 1.00 44.78  ? 1701 TRP A CA    1 
ATOM   1337  C  C     . TRP A 1 1701 ? 185.416 242.395 192.944 1.00 42.64  ? 1701 TRP A C     1 
ATOM   1338  O  O     . TRP A 1 1701 ? 186.234 242.770 192.102 1.00 44.62  ? 1701 TRP A O     1 
ATOM   1339  C  CB    . TRP A 1 1701 ? 183.411 243.911 192.898 1.00 44.69  ? 1701 TRP A CB    1 
ATOM   1340  C  CG    . TRP A 1 1701 ? 183.654 244.505 194.250 1.00 41.11  ? 1701 TRP A CG    1 
ATOM   1341  C  CD1   . TRP A 1 1701 ? 182.787 244.558 195.297 1.00 49.46  ? 1701 TRP A CD1   1 
ATOM   1342  C  CD2   . TRP A 1 1701 ? 184.828 245.214 194.667 1.00 38.68  ? 1701 TRP A CD2   1 
ATOM   1343  N  NE1   . TRP A 1 1701 ? 183.361 245.220 196.355 1.00 44.06  ? 1701 TRP A NE1   1 
ATOM   1344  C  CE2   . TRP A 1 1701 ? 184.615 245.634 195.991 1.00 40.49  ? 1701 TRP A CE2   1 
ATOM   1345  C  CE3   . TRP A 1 1701 ? 186.047 245.517 194.053 1.00 42.17  ? 1701 TRP A CE3   1 
ATOM   1346  C  CZ2   . TRP A 1 1701 ? 185.573 246.342 196.712 1.00 43.53  ? 1701 TRP A CZ2   1 
ATOM   1347  C  CZ3   . TRP A 1 1701 ? 186.996 246.216 194.771 1.00 35.60  ? 1701 TRP A CZ3   1 
ATOM   1348  C  CH2   . TRP A 1 1701 ? 186.756 246.620 196.086 1.00 43.34  ? 1701 TRP A CH2   1 
ATOM   1349  N  N     . LEU A 1 1702 ? 185.795 241.871 194.114 1.00 45.50  ? 1702 LEU A N     1 
ATOM   1350  C  CA    . LEU A 1 1702 ? 187.213 241.600 194.344 1.00 40.02  ? 1702 LEU A CA    1 
ATOM   1351  C  C     . LEU A 1 1702 ? 187.730 240.511 193.406 1.00 39.06  ? 1702 LEU A C     1 
ATOM   1352  O  O     . LEU A 1 1702 ? 188.827 240.634 192.842 1.00 42.93  ? 1702 LEU A O     1 
ATOM   1353  C  CB    . LEU A 1 1702 ? 187.448 241.214 195.803 1.00 37.49  ? 1702 LEU A CB    1 
ATOM   1354  C  CG    . LEU A 1 1702 ? 187.875 242.369 196.710 1.00 39.39  ? 1702 LEU A CG    1 
ATOM   1355  C  CD1   . LEU A 1 1702 ? 188.202 241.869 198.104 1.00 43.22  ? 1702 LEU A CD1   1 
ATOM   1356  C  CD2   . LEU A 1 1702 ? 189.059 243.105 196.111 1.00 38.84  ? 1702 LEU A CD2   1 
ATOM   1357  N  N     . THR A 1 1703 ? 186.950 239.442 193.222 1.00 36.37  ? 1703 THR A N     1 
ATOM   1358  C  CA    . THR A 1 1703 ? 187.332 238.402 192.272 1.00 38.95  ? 1703 THR A CA    1 
ATOM   1359  C  C     . THR A 1 1703 ? 187.396 238.957 190.856 1.00 37.61  ? 1703 THR A C     1 
ATOM   1360  O  O     . THR A 1 1703 ? 188.300 238.613 190.083 1.00 41.65  ? 1703 THR A O     1 
ATOM   1361  C  CB    . THR A 1 1703 ? 186.346 237.235 192.351 1.00 39.71  ? 1703 THR A CB    1 
ATOM   1362  O  OG1   . THR A 1 1703 ? 186.410 236.640 193.653 1.00 49.93  ? 1703 THR A OG1   1 
ATOM   1363  C  CG2   . THR A 1 1703 ? 186.669 236.181 191.304 1.00 30.89  ? 1703 THR A CG2   1 
ATOM   1364  N  N     . LEU A 1 1704 ? 186.440 239.817 190.497 1.00 38.10  ? 1704 LEU A N     1 
ATOM   1365  C  CA    . LEU A 1 1704 ? 186.468 240.444 189.181 1.00 36.31  ? 1704 LEU A CA    1 
ATOM   1366  C  C     . LEU A 1 1704 ? 187.698 241.327 189.016 1.00 34.80  ? 1704 LEU A C     1 
ATOM   1367  O  O     . LEU A 1 1704 ? 188.292 241.373 187.936 1.00 35.72  ? 1704 LEU A O     1 
ATOM   1368  C  CB    . LEU A 1 1704 ? 185.191 241.249 188.954 1.00 41.86  ? 1704 LEU A CB    1 
ATOM   1369  C  CG    . LEU A 1 1704 ? 183.935 240.417 188.702 1.00 45.92  ? 1704 LEU A CG    1 
ATOM   1370  C  CD1   . LEU A 1 1704 ? 182.705 241.132 189.230 1.00 50.92  ? 1704 LEU A CD1   1 
ATOM   1371  C  CD2   . LEU A 1 1704 ? 183.790 240.104 187.221 1.00 41.07  ? 1704 LEU A CD2   1 
ATOM   1372  N  N     . VAL A 1 1705 ? 188.092 242.037 190.075 1.00 35.29  ? 1705 VAL A N     1 
ATOM   1373  C  CA    . VAL A 1 1705 ? 189.292 242.869 190.018 1.00 34.49  ? 1705 VAL A CA    1 
ATOM   1374  C  C     . VAL A 1 1705 ? 190.526 242.008 189.784 1.00 26.57  ? 1705 VAL A C     1 
ATOM   1375  O  O     . VAL A 1 1705 ? 191.391 242.350 188.972 1.00 27.11  ? 1705 VAL A O     1 
ATOM   1376  C  CB    . VAL A 1 1705 ? 189.419 243.711 191.301 1.00 30.89  ? 1705 VAL A CB    1 
ATOM   1377  C  CG1   . VAL A 1 1705 ? 190.847 244.199 191.484 1.00 25.49  ? 1705 VAL A CG1   1 
ATOM   1378  C  CG2   . VAL A 1 1705 ? 188.465 244.892 191.254 1.00 26.16  ? 1705 VAL A CG2   1 
ATOM   1379  N  N     . GLU A 1 1706 ? 190.629 240.881 190.490 1.00 27.99  ? 1706 GLU A N     1 
ATOM   1380  C  CA    . GLU A 1 1706 ? 191.780 239.998 190.307 1.00 26.16  ? 1706 GLU A CA    1 
ATOM   1381  C  C     . GLU A 1 1706 ? 191.815 239.412 188.897 1.00 26.12  ? 1706 GLU A C     1 
ATOM   1382  O  O     . GLU A 1 1706 ? 192.868 239.377 188.240 1.00 28.32  ? 1706 GLU A O     1 
ATOM   1383  C  CB    . GLU A 1 1706 ? 191.748 238.890 191.360 1.00 25.20  ? 1706 GLU A CB    1 
ATOM   1384  C  CG    . GLU A 1 1706 ? 192.876 237.886 191.251 1.00 31.41  ? 1706 GLU A CG    1 
ATOM   1385  C  CD    . GLU A 1 1706 ? 192.484 236.523 191.781 1.00 38.60  ? 1706 GLU A CD    1 
ATOM   1386  O  OE1   . GLU A 1 1706 ? 191.910 235.728 191.009 1.00 36.20  ? 1706 GLU A OE1   1 
ATOM   1387  O  OE2   . GLU A 1 1706 ? 192.750 236.247 192.969 1.00 35.98  ? 1706 GLU A OE2   1 
ATOM   1388  N  N     . LYS A 1 1707 ? 190.660 238.954 188.406 1.00 21.68  ? 1707 LYS A N     1 
ATOM   1389  C  CA    . LYS A 1 1707 ? 190.592 238.395 187.061 1.00 24.83  ? 1707 LYS A CA    1 
ATOM   1390  C  C     . LYS A 1 1707 ? 190.928 239.444 186.010 1.00 26.03  ? 1707 LYS A C     1 
ATOM   1391  O  O     . LYS A 1 1707 ? 191.619 239.152 185.025 1.00 29.59  ? 1707 LYS A O     1 
ATOM   1392  C  CB    . LYS A 1 1707 ? 189.203 237.811 186.808 1.00 34.26  ? 1707 LYS A CB    1 
ATOM   1393  C  CG    . LYS A 1 1707 ? 189.053 237.126 185.464 1.00 32.37  ? 1707 LYS A CG    1 
ATOM   1394  C  CD    . LYS A 1 1707 ? 187.671 236.526 185.305 1.00 36.58  ? 1707 LYS A CD    1 
ATOM   1395  C  CE    . LYS A 1 1707 ? 187.551 235.763 183.997 1.00 46.79  ? 1707 LYS A CE    1 
ATOM   1396  N  NZ    . LYS A 1 1707 ? 187.616 236.669 182.820 1.00 42.52  ? 1707 LYS A NZ    1 
ATOM   1397  N  N     . GLU A 1 1708 ? 190.436 240.670 186.196 1.00 27.83  ? 1708 GLU A N     1 
ATOM   1398  C  CA    . GLU A 1 1708 ? 190.743 241.739 185.259 1.00 29.36  ? 1708 GLU A CA    1 
ATOM   1399  C  C     . GLU A 1 1708 ? 192.214 242.121 185.321 1.00 24.53  ? 1708 GLU A C     1 
ATOM   1400  O  O     . GLU A 1 1708 ? 192.804 242.447 184.290 1.00 29.33  ? 1708 GLU A O     1 
ATOM   1401  C  CB    . GLU A 1 1708 ? 189.853 242.950 185.529 1.00 31.58  ? 1708 GLU A CB    1 
ATOM   1402  C  CG    . GLU A 1 1708 ? 190.076 244.095 184.563 1.00 31.05  ? 1708 GLU A CG    1 
ATOM   1403  C  CD    . GLU A 1 1708 ? 189.692 243.745 183.137 1.00 38.11  ? 1708 GLU A CD    1 
ATOM   1404  O  OE1   . GLU A 1 1708 ? 188.834 242.858 182.943 1.00 35.33  ? 1708 GLU A OE1   1 
ATOM   1405  O  OE2   . GLU A 1 1708 ? 190.251 244.358 182.205 1.00 42.11  ? 1708 GLU A OE2   1 
ATOM   1406  N  N     . MET A 1 1709 ? 192.816 242.087 186.511 1.00 20.84  ? 1709 MET A N     1 
ATOM   1407  C  CA    . MET A 1 1709 ? 194.263 242.231 186.621 1.00 19.27  ? 1709 MET A CA    1 
ATOM   1408  C  C     . MET A 1 1709 ? 194.976 241.236 185.723 1.00 24.28  ? 1709 MET A C     1 
ATOM   1409  O  O     . MET A 1 1709 ? 195.836 241.610 184.914 1.00 28.94  ? 1709 MET A O     1 
ATOM   1410  C  CB    . MET A 1 1709 ? 194.703 242.023 188.069 1.00 22.05  ? 1709 MET A CB    1 
ATOM   1411  C  CG    . MET A 1 1709 ? 196.194 242.200 188.286 1.00 25.35  ? 1709 MET A CG    1 
ATOM   1412  S  SD    . MET A 1 1709 ? 196.699 241.972 190.002 1.00 39.99  ? 1709 MET A SD    1 
ATOM   1413  C  CE    . MET A 1 1709 ? 196.508 240.200 190.180 1.00 19.85  ? 1709 MET A CE    1 
ATOM   1414  N  N     . ARG A 1 1710 ? 194.622 239.956 185.850 1.00 26.63  ? 1710 ARG A N     1 
ATOM   1415  C  CA    . ARG A 1 1710 ? 195.307 238.933 185.065 1.00 20.82  ? 1710 ARG A CA    1 
ATOM   1416  C  C     . ARG A 1 1710 ? 195.097 239.137 183.567 1.00 20.86  ? 1710 ARG A C     1 
ATOM   1417  O  O     . ARG A 1 1710 ? 196.055 239.075 182.786 1.00 22.12  ? 1710 ARG A O     1 
ATOM   1418  C  CB    . ARG A 1 1710 ? 194.848 237.541 185.493 1.00 21.63  ? 1710 ARG A CB    1 
ATOM   1419  C  CG    . ARG A 1 1710 ? 195.693 236.941 186.601 1.00 18.21  ? 1710 ARG A CG    1 
ATOM   1420  C  CD    . ARG A 1 1710 ? 195.423 235.460 186.764 1.00 23.63  ? 1710 ARG A CD    1 
ATOM   1421  N  NE    . ARG A 1 1710 ? 194.492 235.182 187.848 1.00 28.26  ? 1710 ARG A NE    1 
ATOM   1422  C  CZ    . ARG A 1 1710 ? 194.857 234.788 189.060 1.00 30.88  ? 1710 ARG A CZ    1 
ATOM   1423  N  NH1   . ARG A 1 1710 ? 196.130 234.631 189.381 1.00 27.03  ? 1710 ARG A NH1   1 
ATOM   1424  N  NH2   . ARG A 1 1710 ? 193.921 234.540 189.972 1.00 29.86  ? 1710 ARG A NH2   1 
ATOM   1425  N  N     . VAL A 1 1711 ? 193.855 239.398 183.148 1.00 20.82  ? 1711 VAL A N     1 
ATOM   1426  C  CA    . VAL A 1 1711 ? 193.581 239.499 181.715 1.00 23.91  ? 1711 VAL A CA    1 
ATOM   1427  C  C     . VAL A 1 1711 ? 194.214 240.759 181.128 1.00 22.82  ? 1711 VAL A C     1 
ATOM   1428  O  O     . VAL A 1 1711 ? 194.717 240.744 179.998 1.00 28.90  ? 1711 VAL A O     1 
ATOM   1429  C  CB    . VAL A 1 1711 ? 192.066 239.425 181.436 1.00 23.97  ? 1711 VAL A CB    1 
ATOM   1430  C  CG1   . VAL A 1 1711 ? 191.337 240.611 182.021 1.00 24.39  ? 1711 VAL A CG1   1 
ATOM   1431  C  CG2   . VAL A 1 1711 ? 191.806 239.326 179.940 1.00 31.03  ? 1711 VAL A CG2   1 
ATOM   1432  N  N     . THR A 1 1712 ? 194.205 241.866 181.878 1.00 19.66  ? 1712 THR A N     1 
ATOM   1433  C  CA    . THR A 1 1712 ? 194.844 243.087 181.407 1.00 23.84  ? 1712 THR A CA    1 
ATOM   1434  C  C     . THR A 1 1712 ? 196.351 242.921 181.303 1.00 23.96  ? 1712 THR A C     1 
ATOM   1435  O  O     . THR A 1 1712 ? 196.959 243.400 180.339 1.00 26.25  ? 1712 THR A O     1 
ATOM   1436  C  CB    . THR A 1 1712 ? 194.504 244.252 182.337 1.00 23.87  ? 1712 THR A CB    1 
ATOM   1437  O  OG1   . THR A 1 1712 ? 193.091 244.283 182.570 1.00 28.84  ? 1712 THR A OG1   1 
ATOM   1438  C  CG2   . THR A 1 1712 ? 194.939 245.569 181.720 1.00 24.12  ? 1712 THR A CG2   1 
ATOM   1439  N  N     . LEU A 1 1713 ? 196.969 242.244 182.275 1.00 20.62  ? 1713 LEU A N     1 
ATOM   1440  C  CA    . LEU A 1 1713 ? 198.396 241.969 182.174 1.00 17.35  ? 1713 LEU A CA    1 
ATOM   1441  C  C     . LEU A 1 1713 ? 198.697 241.100 180.961 1.00 17.96  ? 1713 LEU A C     1 
ATOM   1442  O  O     . LEU A 1 1713 ? 199.679 241.337 180.251 1.00 19.09  ? 1713 LEU A O     1 
ATOM   1443  C  CB    . LEU A 1 1713 ? 198.896 241.302 183.455 1.00 19.76  ? 1713 LEU A CB    1 
ATOM   1444  C  CG    . LEU A 1 1713 ? 199.262 242.251 184.598 1.00 18.99  ? 1713 LEU A CG    1 
ATOM   1445  C  CD1   . LEU A 1 1713 ? 199.722 241.472 185.817 1.00 13.63  ? 1713 LEU A CD1   1 
ATOM   1446  C  CD2   . LEU A 1 1713 ? 200.329 243.236 184.152 1.00 20.41  ? 1713 LEU A CD2   1 
ATOM   1447  N  N     . ALA A 1 1714 ? 197.850 240.101 180.696 1.00 20.26  ? 1714 ALA A N     1 
ATOM   1448  C  CA    . ALA A 1 1714 ? 198.059 239.248 179.529 1.00 17.45  ? 1714 ALA A CA    1 
ATOM   1449  C  C     . ALA A 1 1714 ? 197.947 240.038 178.228 1.00 19.37  ? 1714 ALA A C     1 
ATOM   1450  O  O     . ALA A 1 1714 ? 198.774 239.875 177.321 1.00 22.84  ? 1714 ALA A O     1 
ATOM   1451  C  CB    . ALA A 1 1714 ? 197.063 238.090 179.543 1.00 20.18  ? 1714 ALA A CB    1 
ATOM   1452  N  N     . LYS A 1 1715 ? 196.933 240.897 178.117 1.00 19.71  ? 1715 LYS A N     1 
ATOM   1453  C  CA    . LYS A 1 1715 ? 196.755 241.681 176.896 1.00 22.17  ? 1715 LYS A CA    1 
ATOM   1454  C  C     . LYS A 1 1715 ? 197.903 242.663 176.693 1.00 25.75  ? 1715 LYS A C     1 
ATOM   1455  O  O     . LYS A 1 1715 ? 198.412 242.817 175.572 1.00 30.08  ? 1715 LYS A O     1 
ATOM   1456  C  CB    . LYS A 1 1715 ? 195.419 242.418 176.941 1.00 29.52  ? 1715 LYS A CB    1 
ATOM   1457  C  CG    . LYS A 1 1715 ? 194.206 241.510 176.836 1.00 34.67  ? 1715 LYS A CG    1 
ATOM   1458  C  CD    . LYS A 1 1715 ? 192.918 242.290 177.028 1.00 42.19  ? 1715 LYS A CD    1 
ATOM   1459  C  CE    . LYS A 1 1715 ? 192.646 243.198 175.838 1.00 49.85  ? 1715 LYS A CE    1 
ATOM   1460  N  NZ    . LYS A 1 1715 ? 191.332 243.887 175.951 1.00 60.44  ? 1715 LYS A NZ    1 
ATOM   1461  N  N     . LEU A 1 1716 ? 198.322 243.339 177.766 1.00 21.23  ? 1716 LEU A N     1 
ATOM   1462  C  CA    . LEU A 1 1716 ? 199.448 244.259 177.665 1.00 18.02  ? 1716 LEU A CA    1 
ATOM   1463  C  C     . LEU A 1 1716 ? 200.724 243.517 177.293 1.00 20.27  ? 1716 LEU A C     1 
ATOM   1464  O  O     . LEU A 1 1716 ? 201.542 244.026 176.517 1.00 26.44  ? 1716 LEU A O     1 
ATOM   1465  C  CB    . LEU A 1 1716 ? 199.623 245.016 178.979 1.00 20.68  ? 1716 LEU A CB    1 
ATOM   1466  C  CG    . LEU A 1 1716 ? 198.597 246.101 179.302 1.00 18.15  ? 1716 LEU A CG    1 
ATOM   1467  C  CD1   . LEU A 1 1716 ? 198.883 246.708 180.663 1.00 14.26  ? 1716 LEU A CD1   1 
ATOM   1468  C  CD2   . LEU A 1 1716 ? 198.598 247.171 178.228 1.00 19.97  ? 1716 LEU A CD2   1 
ATOM   1469  N  N     . LEU A 1 1717 ? 200.913 242.312 177.835 1.00 19.50  ? 1717 LEU A N     1 
ATOM   1470  C  CA    . LEU A 1 1717 ? 202.068 241.506 177.461 1.00 21.86  ? 1717 LEU A CA    1 
ATOM   1471  C  C     . LEU A 1 1717 ? 202.022 241.145 175.985 1.00 21.95  ? 1717 LEU A C     1 
ATOM   1472  O  O     . LEU A 1 1717 ? 203.052 241.154 175.306 1.00 24.91  ? 1717 LEU A O     1 
ATOM   1473  C  CB    . LEU A 1 1717 ? 202.126 240.242 178.322 1.00 15.88  ? 1717 LEU A CB    1 
ATOM   1474  C  CG    . LEU A 1 1717 ? 202.930 239.059 177.777 1.00 17.93  ? 1717 LEU A CG    1 
ATOM   1475  C  CD1   . LEU A 1 1717 ? 204.408 239.415 177.669 1.00 14.01  ? 1717 LEU A CD1   1 
ATOM   1476  C  CD2   . LEU A 1 1717 ? 202.736 237.817 178.625 1.00 19.88  ? 1717 LEU A CD2   1 
ATOM   1477  N  N     . ALA A 1 1718 ? 200.835 240.814 175.472 1.00 22.36  ? 1718 ALA A N     1 
ATOM   1478  C  CA    . ALA A 1 1718 ? 200.707 240.491 174.054 1.00 23.70  ? 1718 ALA A CA    1 
ATOM   1479  C  C     . ALA A 1 1718 ? 201.088 241.681 173.181 1.00 28.81  ? 1718 ALA A C     1 
ATOM   1480  O  O     . ALA A 1 1718 ? 201.821 241.538 172.193 1.00 30.60  ? 1718 ALA A O     1 
ATOM   1481  C  CB    . ALA A 1 1718 ? 199.283 240.030 173.748 1.00 24.71  ? 1718 ALA A CB    1 
ATOM   1482  N  N     . GLU A 1 1719 ? 200.602 242.874 173.537 1.00 27.28  ? 1719 GLU A N     1 
ATOM   1483  C  CA    . GLU A 1 1719 ? 200.956 244.067 172.769 1.00 23.69  ? 1719 GLU A CA    1 
ATOM   1484  C  C     . GLU A 1 1719 ? 202.454 244.358 172.847 1.00 23.80  ? 1719 GLU A C     1 
ATOM   1485  O  O     . GLU A 1 1719 ? 203.088 244.700 171.835 1.00 27.82  ? 1719 GLU A O     1 
ATOM   1486  C  CB    . GLU A 1 1719 ? 200.149 245.269 173.260 1.00 26.25  ? 1719 GLU A CB    1 
ATOM   1487  C  CG    . GLU A 1 1719 ? 198.648 245.042 173.281 1.00 32.67  ? 1719 GLU A CG    1 
ATOM   1488  C  CD    . GLU A 1 1719 ? 197.903 246.137 174.017 1.00 44.72  ? 1719 GLU A CD    1 
ATOM   1489  O  OE1   . GLU A 1 1719 ? 198.541 247.142 174.393 1.00 42.96  ? 1719 GLU A OE1   1 
ATOM   1490  O  OE2   . GLU A 1 1719 ? 196.679 245.994 174.218 1.00 44.51  ? 1719 GLU A OE2   1 
ATOM   1491  N  N     . SER A 1 1720 ? 203.037 244.225 174.040 1.00 25.03  ? 1720 SER A N     1 
ATOM   1492  C  CA    . SER A 1 1720 ? 204.464 244.476 174.200 1.00 22.99  ? 1720 SER A CA    1 
ATOM   1493  C  C     . SER A 1 1720 ? 205.291 243.472 173.409 1.00 27.64  ? 1720 SER A C     1 
ATOM   1494  O  O     . SER A 1 1720 ? 206.336 243.822 172.851 1.00 32.36  ? 1720 SER A O     1 
ATOM   1495  C  CB    . SER A 1 1720 ? 204.836 244.437 175.681 1.00 21.74  ? 1720 SER A CB    1 
ATOM   1496  O  OG    . SER A 1 1720 ? 206.235 244.571 175.858 1.00 24.72  ? 1720 SER A OG    1 
ATOM   1497  N  N     . VAL A 1 1721 ? 204.844 242.215 173.358 1.00 26.93  ? 1721 VAL A N     1 
ATOM   1498  C  CA    . VAL A 1 1721 ? 205.520 241.209 172.546 1.00 22.76  ? 1721 VAL A CA    1 
ATOM   1499  C  C     . VAL A 1 1721 ? 205.432 241.573 171.072 1.00 29.01  ? 1721 VAL A C     1 
ATOM   1500  O  O     . VAL A 1 1721 ? 206.412 241.454 170.328 1.00 34.56  ? 1721 VAL A O     1 
ATOM   1501  C  CB    . VAL A 1 1721 ? 204.932 239.813 172.822 1.00 24.92  ? 1721 VAL A CB    1 
ATOM   1502  C  CG1   . VAL A 1 1721 ? 205.347 238.833 171.736 1.00 30.49  ? 1721 VAL A CG1   1 
ATOM   1503  C  CG2   . VAL A 1 1721 ? 205.391 239.311 174.174 1.00 20.85  ? 1721 VAL A CG2   1 
ATOM   1504  N  N     . THR A 1 1722 ? 204.257 242.025 170.628 1.00 30.14  ? 1722 THR A N     1 
ATOM   1505  C  CA    . THR A 1 1722 ? 204.106 242.432 169.234 1.00 28.98  ? 1722 THR A CA    1 
ATOM   1506  C  C     . THR A 1 1722 ? 205.077 243.551 168.882 1.00 31.44  ? 1722 THR A C     1 
ATOM   1507  O  O     . THR A 1 1722 ? 205.664 243.556 167.794 1.00 39.57  ? 1722 THR A O     1 
ATOM   1508  C  CB    . THR A 1 1722 ? 202.664 242.865 168.968 1.00 29.69  ? 1722 THR A CB    1 
ATOM   1509  O  OG1   . THR A 1 1722 ? 201.778 241.773 169.236 1.00 34.11  ? 1722 THR A OG1   1 
ATOM   1510  C  CG2   . THR A 1 1722 ? 202.495 243.300 167.522 1.00 26.32  ? 1722 THR A CG2   1 
ATOM   1511  N  N     . GLU A 1 1723 ? 205.266 244.505 169.795 1.00 32.77  ? 1723 GLU A N     1 
ATOM   1512  C  CA    . GLU A 1 1723 ? 206.196 245.601 169.516 1.00 33.20  ? 1723 GLU A CA    1 
ATOM   1513  C  C     . GLU A 1 1723 ? 207.653 245.141 169.568 1.00 37.19  ? 1723 GLU A C     1 
ATOM   1514  O  O     . GLU A 1 1723 ? 208.463 245.511 168.704 1.00 43.21  ? 1723 GLU A O     1 
ATOM   1515  C  CB    . GLU A 1 1723 ? 205.955 246.752 170.492 1.00 34.49  ? 1723 GLU A CB    1 
ATOM   1516  C  CG    . GLU A 1 1723 ? 204.680 247.530 170.212 1.00 36.37  ? 1723 GLU A CG    1 
ATOM   1517  C  CD    . GLU A 1 1723 ? 204.452 248.655 171.200 1.00 45.59  ? 1723 GLU A CD    1 
ATOM   1518  O  OE1   . GLU A 1 1723 ? 205.393 249.443 171.430 1.00 41.02  ? 1723 GLU A OE1   1 
ATOM   1519  O  OE2   . GLU A 1 1723 ? 203.331 248.755 171.741 1.00 42.01  ? 1723 GLU A OE2   1 
ATOM   1520  N  N     . VAL A 1 1724 ? 208.014 244.337 170.573 1.00 36.86  ? 1724 VAL A N     1 
ATOM   1521  C  CA    . VAL A 1 1724 ? 209.404 243.920 170.721 1.00 34.25  ? 1724 VAL A CA    1 
ATOM   1522  C  C     . VAL A 1 1724 ? 209.821 242.965 169.610 1.00 42.67  ? 1724 VAL A C     1 
ATOM   1523  O  O     . VAL A 1 1724 ? 211.013 242.879 169.290 1.00 49.27  ? 1724 VAL A O     1 
ATOM   1524  C  CB    . VAL A 1 1724 ? 209.642 243.299 172.112 1.00 31.35  ? 1724 VAL A CB    1 
ATOM   1525  C  CG1   . VAL A 1 1724 ? 208.993 241.931 172.219 1.00 31.56  ? 1724 VAL A CG1   1 
ATOM   1526  C  CG2   . VAL A 1 1724 ? 211.130 243.226 172.430 1.00 27.94  ? 1724 VAL A CG2   1 
ATOM   1527  N  N     . GLU A 1 1725 ? 208.871 242.246 169.003 1.00 41.36  ? 1725 GLU A N     1 
ATOM   1528  C  CA    . GLU A 1 1725 ? 209.191 241.462 167.815 1.00 39.99  ? 1725 GLU A CA    1 
ATOM   1529  C  C     . GLU A 1 1725 ? 209.651 242.363 166.679 1.00 43.22  ? 1725 GLU A C     1 
ATOM   1530  O  O     . GLU A 1 1725 ? 210.598 242.032 165.956 1.00 46.79  ? 1725 GLU A O     1 
ATOM   1531  C  CB    . GLU A 1 1725 ? 207.981 240.634 167.384 1.00 41.84  ? 1725 GLU A CB    1 
ATOM   1532  C  CG    . GLU A 1 1725 ? 207.672 239.448 168.281 1.00 39.25  ? 1725 GLU A CG    1 
ATOM   1533  C  CD    . GLU A 1 1725 ? 206.746 238.450 167.617 1.00 50.60  ? 1725 GLU A CD    1 
ATOM   1534  O  OE1   . GLU A 1 1725 ? 205.668 238.865 167.141 1.00 46.98  ? 1725 GLU A OE1   1 
ATOM   1535  O  OE2   . GLU A 1 1725 ? 207.095 237.252 167.565 1.00 52.96  ? 1725 GLU A OE2   1 
ATOM   1536  N  N     . ILE A 1 1726 ? 208.986 243.507 166.503 1.00 47.07  ? 1726 ILE A N     1 
ATOM   1537  C  CA    . ILE A 1 1726 ? 209.443 244.490 165.526 1.00 49.54  ? 1726 ILE A CA    1 
ATOM   1538  C  C     . ILE A 1 1726 ? 210.819 245.016 165.913 1.00 47.41  ? 1726 ILE A C     1 
ATOM   1539  O  O     . ILE A 1 1726 ? 211.697 245.188 165.058 1.00 44.53  ? 1726 ILE A O     1 
ATOM   1540  C  CB    . ILE A 1 1726 ? 208.416 245.627 165.387 1.00 38.13  ? 1726 ILE A CB    1 
ATOM   1541  C  CG1   . ILE A 1 1726 ? 207.061 245.069 164.950 1.00 38.20  ? 1726 ILE A CG1   1 
ATOM   1542  C  CG2   . ILE A 1 1726 ? 208.904 246.667 164.394 1.00 42.57  ? 1726 ILE A CG2   1 
ATOM   1543  C  CD1   . ILE A 1 1726 ? 207.092 244.373 163.609 1.00 43.89  ? 1726 ILE A CD1   1 
ATOM   1544  N  N     . PHE A 1 1727 ? 211.031 245.280 167.205 1.00 48.27  ? 1727 PHE A N     1 
ATOM   1545  C  CA    . PHE A 1 1727 ? 212.372 245.647 167.655 1.00 48.64  ? 1727 PHE A CA    1 
ATOM   1546  C  C     . PHE A 1 1727 ? 213.362 244.512 167.429 1.00 48.86  ? 1727 PHE A C     1 
ATOM   1547  O  O     . PHE A 1 1727 ? 214.549 244.753 167.176 1.00 48.86  ? 1727 PHE A O     1 
ATOM   1548  C  CB    . PHE A 1 1727 ? 212.358 246.057 169.126 1.00 44.67  ? 1727 PHE A CB    1 
ATOM   1549  C  CG    . PHE A 1 1727 ? 211.665 247.358 169.380 1.00 41.77  ? 1727 PHE A CG    1 
ATOM   1550  C  CD1   . PHE A 1 1727 ? 211.377 248.221 168.334 1.00 48.15  ? 1727 PHE A CD1   1 
ATOM   1551  C  CD2   . PHE A 1 1727 ? 211.313 247.729 170.662 1.00 33.14  ? 1727 PHE A CD2   1 
ATOM   1552  C  CE1   . PHE A 1 1727 ? 210.744 249.422 168.565 1.00 51.66  ? 1727 PHE A CE1   1 
ATOM   1553  C  CE2   . PHE A 1 1727 ? 210.684 248.927 170.895 1.00 43.35  ? 1727 PHE A CE2   1 
ATOM   1554  C  CZ    . PHE A 1 1727 ? 210.396 249.776 169.847 1.00 51.67  ? 1727 PHE A CZ    1 
ATOM   1555  N  N     . GLY A 1 1728 ? 212.901 243.270 167.519 1.00 53.64  ? 1728 GLY A N     1 
ATOM   1556  C  CA    . GLY A 1 1728 ? 213.722 242.137 167.161 1.00 53.77  ? 1728 GLY A CA    1 
ATOM   1557  C  C     . GLY A 1 1728 ? 213.917 242.063 165.658 1.00 58.08  ? 1728 GLY A C     1 
ATOM   1558  O  O     . GLY A 1 1728 ? 213.376 242.854 164.885 1.00 61.74  ? 1728 GLY A O     1 
ATOM   1559  N  N     . LYS A 1 1729 ? 214.720 241.077 165.246 1.00 52.09  ? 1729 LYS A N     1 
ATOM   1560  C  CA    . LYS A 1 1729 ? 215.090 240.832 163.850 1.00 60.36  ? 1729 LYS A CA    1 
ATOM   1561  C  C     . LYS A 1 1729 ? 215.363 242.126 163.089 1.00 60.72  ? 1729 LYS A C     1 
ATOM   1562  O  O     . LYS A 1 1729 ? 214.947 242.282 161.937 1.00 64.91  ? 1729 LYS A O     1 
ATOM   1563  C  CB    . LYS A 1 1729 ? 214.019 239.992 163.133 1.00 66.09  ? 1729 LYS A CB    1 
ATOM   1564  C  CG    . LYS A 1 1729 ? 212.614 240.582 163.060 1.00 62.42  ? 1729 LYS A CG    1 
ATOM   1565  C  CD    . LYS A 1 1729 ? 211.719 239.791 162.121 1.00 73.40  ? 1729 LYS A CD    1 
ATOM   1566  C  CE    . LYS A 1 1729 ? 210.299 240.335 162.133 1.00 84.34  ? 1729 LYS A CE    1 
ATOM   1567  N  NZ    . LYS A 1 1729 ? 210.043 241.256 160.991 1.00 78.99  ? 1729 LYS A NZ    1 
ATOM   1568  N  N     . ALA A 1 1730 ? 216.076 243.055 163.724 1.00 58.11  ? 1730 ALA A N     1 
ATOM   1569  C  CA    . ALA A 1 1730 ? 216.420 244.335 163.123 1.00 56.08  ? 1730 ALA A CA    1 
ATOM   1570  C  C     . ALA A 1 1730 ? 217.919 244.562 163.240 1.00 57.80  ? 1730 ALA A C     1 
ATOM   1571  O  O     . ALA A 1 1730 ? 218.524 244.253 164.272 1.00 50.68  ? 1730 ALA A O     1 
ATOM   1572  C  CB    . ALA A 1 1730 ? 215.661 245.487 163.790 1.00 44.03  ? 1730 ALA A CB    1 
ATOM   1573  N  N     . THR A 1 1731 ? 218.516 245.093 162.171 1.00 62.11  ? 1731 THR A N     1 
ATOM   1574  C  CA    . THR A 1 1731 ? 219.952 245.354 162.179 1.00 58.44  ? 1731 THR A CA    1 
ATOM   1575  C  C     . THR A 1 1731 ? 220.312 246.455 163.170 1.00 51.89  ? 1731 THR A C     1 
ATOM   1576  O  O     . THR A 1 1731 ? 221.323 246.358 163.873 1.00 57.82  ? 1731 THR A O     1 
ATOM   1577  C  CB    . THR A 1 1731 ? 220.429 245.722 160.776 1.00 60.64  ? 1731 THR A CB    1 
ATOM   1578  O  OG1   . THR A 1 1731 ? 219.825 246.956 160.370 1.00 63.95  ? 1731 THR A OG1   1 
ATOM   1579  C  CG2   . THR A 1 1731 ? 220.058 244.631 159.785 1.00 50.64  ? 1731 THR A CG2   1 
ATOM   1580  N  N     . SER A 1 1732 ? 219.500 247.507 163.241 1.00 44.78  ? 1732 SER A N     1 
ATOM   1581  C  CA    . SER A 1 1732 ? 219.745 248.621 164.141 1.00 48.21  ? 1732 SER A CA    1 
ATOM   1582  C  C     . SER A 1 1732 ? 218.463 248.976 164.879 1.00 49.83  ? 1732 SER A C     1 
ATOM   1583  O  O     . SER A 1 1732 ? 217.356 248.741 164.385 1.00 50.46  ? 1732 SER A O     1 
ATOM   1584  C  CB    . SER A 1 1732 ? 220.272 249.850 163.386 1.00 53.48  ? 1732 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 1732 ? 220.585 250.902 164.281 1.00 56.70  ? 1732 SER A OG    1 
ATOM   1586  N  N     . ILE A 1 1733 ? 218.623 249.544 166.070 1.00 47.32  ? 1733 ILE A N     1 
ATOM   1587  C  CA    . ILE A 1 1733 ? 217.509 249.892 166.943 1.00 43.61  ? 1733 ILE A CA    1 
ATOM   1588  C  C     . ILE A 1 1733 ? 217.557 251.388 167.211 1.00 44.12  ? 1733 ILE A C     1 
ATOM   1589  O  O     . ILE A 1 1733 ? 218.594 251.916 167.629 1.00 44.99  ? 1733 ILE A O     1 
ATOM   1590  C  CB    . ILE A 1 1733 ? 217.555 249.099 168.262 1.00 42.92  ? 1733 ILE A CB    1 
ATOM   1591  C  CG1   . ILE A 1 1733 ? 217.268 247.619 168.004 1.00 36.53  ? 1733 ILE A CG1   1 
ATOM   1592  C  CG2   . ILE A 1 1733 ? 216.571 249.677 169.271 1.00 36.03  ? 1733 ILE A CG2   1 
ATOM   1593  C  CD1   . ILE A 1 1733 ? 216.961 246.826 169.252 1.00 33.73  ? 1733 ILE A CD1   1 
ATOM   1594  N  N     . ASP A 1 1734 ? 216.442 252.066 166.968 1.00 44.46  ? 1734 ASP A N     1 
ATOM   1595  C  CA    . ASP A 1 1734 ? 216.339 253.483 167.284 1.00 44.82  ? 1734 ASP A CA    1 
ATOM   1596  C  C     . ASP A 1 1734 ? 216.184 253.654 168.789 1.00 46.82  ? 1734 ASP A C     1 
ATOM   1597  O  O     . ASP A 1 1734 ? 215.244 253.098 169.369 1.00 43.05  ? 1734 ASP A O     1 
ATOM   1598  C  CB    . ASP A 1 1734 ? 215.155 254.108 166.559 1.00 45.35  ? 1734 ASP A CB    1 
ATOM   1599  C  CG    . ASP A 1 1734 ? 215.156 255.623 166.634 1.00 55.95  ? 1734 ASP A CG    1 
ATOM   1600  O  OD1   . ASP A 1 1734 ? 216.232 256.208 166.876 1.00 54.21  ? 1734 ASP A OD1   1 
ATOM   1601  O  OD2   . ASP A 1 1734 ? 214.079 256.229 166.455 1.00 57.72  ? 1734 ASP A OD2   1 
ATOM   1602  N  N     . PRO A 1 1735 ? 217.075 254.390 169.458 1.00 44.89  ? 1735 PRO A N     1 
ATOM   1603  C  CA    . PRO A 1 1735 ? 216.932 254.562 170.912 1.00 42.86  ? 1735 PRO A CA    1 
ATOM   1604  C  C     . PRO A 1 1735 ? 215.619 255.201 171.327 1.00 43.12  ? 1735 PRO A C     1 
ATOM   1605  O  O     . PRO A 1 1735 ? 215.067 254.829 172.369 1.00 43.99  ? 1735 PRO A O     1 
ATOM   1606  C  CB    . PRO A 1 1735 ? 218.130 255.450 171.276 1.00 40.96  ? 1735 PRO A CB    1 
ATOM   1607  C  CG    . PRO A 1 1735 ? 219.121 255.210 170.192 1.00 37.77  ? 1735 PRO A CG    1 
ATOM   1608  C  CD    . PRO A 1 1735 ? 218.318 254.990 168.948 1.00 39.02  ? 1735 PRO A CD    1 
ATOM   1609  N  N     . ASN A 1 1736 ? 215.096 256.144 170.540 1.00 46.29  ? 1736 ASN A N     1 
ATOM   1610  C  CA    . ASN A 1 1736 ? 213.870 256.837 170.929 1.00 48.99  ? 1736 ASN A CA    1 
ATOM   1611  C  C     . ASN A 1 1736 ? 212.689 255.876 170.989 1.00 39.38  ? 1736 ASN A C     1 
ATOM   1612  O  O     . ASN A 1 1736 ? 211.919 255.880 171.957 1.00 37.06  ? 1736 ASN A O     1 
ATOM   1613  C  CB    . ASN A 1 1736 ? 213.587 257.983 169.958 1.00 53.31  ? 1736 ASN A CB    1 
ATOM   1614  C  CG    . ASN A 1 1736 ? 214.806 258.843 169.703 1.00 50.45  ? 1736 ASN A CG    1 
ATOM   1615  O  OD1   . ASN A 1 1736 ? 215.595 259.107 170.610 1.00 42.10  ? 1736 ASN A OD1   1 
ATOM   1616  N  ND2   . ASN A 1 1736 ? 214.967 259.288 168.462 1.00 57.62  ? 1736 ASN A ND2   1 
ATOM   1617  N  N     . THR A 1 1737 ? 212.533 255.039 169.961 1.00 38.41  ? 1737 THR A N     1 
ATOM   1618  C  CA    . THR A 1 1737 ? 211.429 254.084 169.946 1.00 41.62  ? 1737 THR A CA    1 
ATOM   1619  C  C     . THR A 1 1737 ? 211.573 253.051 171.056 1.00 38.07  ? 1737 THR A C     1 
ATOM   1620  O  O     . THR A 1 1737 ? 210.578 252.653 171.675 1.00 36.14  ? 1737 THR A O     1 
ATOM   1621  C  CB    . THR A 1 1737 ? 211.346 253.399 168.582 1.00 43.25  ? 1737 THR A CB    1 
ATOM   1622  O  OG1   . THR A 1 1737 ? 212.558 252.677 168.334 1.00 53.77  ? 1737 THR A OG1   1 
ATOM   1623  C  CG2   . THR A 1 1737 ? 211.142 254.428 167.484 1.00 41.62  ? 1737 THR A CG2   1 
ATOM   1624  N  N     . TYR A 1 1738 ? 212.802 252.600 171.318 1.00 35.59  ? 1738 TYR A N     1 
ATOM   1625  C  CA    . TYR A 1 1738 ? 213.024 251.637 172.391 1.00 28.94  ? 1738 TYR A CA    1 
ATOM   1626  C  C     . TYR A 1 1738 ? 212.672 252.230 173.751 1.00 29.34  ? 1738 TYR A C     1 
ATOM   1627  O  O     . TYR A 1 1738 ? 212.030 251.569 174.576 1.00 32.57  ? 1738 TYR A O     1 
ATOM   1628  C  CB    . TYR A 1 1738 ? 214.475 251.158 172.370 1.00 28.15  ? 1738 TYR A CB    1 
ATOM   1629  C  CG    . TYR A 1 1738 ? 214.673 249.803 173.005 1.00 26.93  ? 1738 TYR A CG    1 
ATOM   1630  C  CD1   . TYR A 1 1738 ? 214.197 248.652 172.392 1.00 32.42  ? 1738 TYR A CD1   1 
ATOM   1631  C  CD2   . TYR A 1 1738 ? 215.328 249.673 174.219 1.00 21.76  ? 1738 TYR A CD2   1 
ATOM   1632  C  CE1   . TYR A 1 1738 ? 214.373 247.412 172.969 1.00 27.92  ? 1738 TYR A CE1   1 
ATOM   1633  C  CE2   . TYR A 1 1738 ? 215.508 248.438 174.803 1.00 18.87  ? 1738 TYR A CE2   1 
ATOM   1634  C  CZ    . TYR A 1 1738 ? 215.029 247.311 174.176 1.00 20.53  ? 1738 TYR A CZ    1 
ATOM   1635  O  OH    . TYR A 1 1738 ? 215.207 246.078 174.758 1.00 22.92  ? 1738 TYR A OH    1 
ATOM   1636  N  N     . ILE A 1 1739 ? 213.076 253.478 174.002 1.00 22.41  ? 1739 ILE A N     1 
ATOM   1637  C  CA    . ILE A 1 1739 ? 212.738 254.118 175.271 1.00 23.90  ? 1739 ILE A CA    1 
ATOM   1638  C  C     . ILE A 1 1739 ? 211.236 254.352 175.370 1.00 27.99  ? 1739 ILE A C     1 
ATOM   1639  O  O     . ILE A 1 1739 ? 210.645 254.224 176.448 1.00 32.11  ? 1739 ILE A O     1 
ATOM   1640  C  CB    . ILE A 1 1739 ? 213.537 255.423 175.446 1.00 28.59  ? 1739 ILE A CB    1 
ATOM   1641  C  CG1   . ILE A 1 1739 ? 215.039 255.138 175.428 1.00 29.84  ? 1739 ILE A CG1   1 
ATOM   1642  C  CG2   . ILE A 1 1739 ? 213.154 256.120 176.739 1.00 30.58  ? 1739 ILE A CG2   1 
ATOM   1643  C  CD1   . ILE A 1 1739 ? 215.501 254.225 176.538 1.00 27.70  ? 1739 ILE A CD1   1 
ATOM   1644  N  N     . THR A 1 1740 ? 210.593 254.695 174.251 1.00 26.49  ? 1740 THR A N     1 
ATOM   1645  C  CA    . THR A 1 1740 ? 209.143 254.859 174.255 1.00 27.66  ? 1740 THR A CA    1 
ATOM   1646  C  C     . THR A 1 1740 ? 208.445 253.555 174.620 1.00 26.83  ? 1740 THR A C     1 
ATOM   1647  O  O     . THR A 1 1740 ? 207.505 253.548 175.425 1.00 31.30  ? 1740 THR A O     1 
ATOM   1648  C  CB    . THR A 1 1740 ? 208.672 255.359 172.888 1.00 32.97  ? 1740 THR A CB    1 
ATOM   1649  O  OG1   . THR A 1 1740 ? 209.145 256.695 172.678 1.00 27.30  ? 1740 THR A OG1   1 
ATOM   1650  C  CG2   . THR A 1 1740 ? 207.154 255.344 172.802 1.00 31.63  ? 1740 THR A CG2   1 
ATOM   1651  N  N     . TRP A 1 1741 ? 208.900 252.439 174.047 1.00 24.03  ? 1741 TRP A N     1 
ATOM   1652  C  CA    . TRP A 1 1741 ? 208.317 251.142 174.372 1.00 19.93  ? 1741 TRP A CA    1 
ATOM   1653  C  C     . TRP A 1 1741 ? 208.572 250.765 175.826 1.00 22.90  ? 1741 TRP A C     1 
ATOM   1654  O  O     . TRP A 1 1741 ? 207.696 250.194 176.487 1.00 23.98  ? 1741 TRP A O     1 
ATOM   1655  C  CB    . TRP A 1 1741 ? 208.870 250.072 173.435 1.00 21.18  ? 1741 TRP A CB    1 
ATOM   1656  C  CG    . TRP A 1 1741 ? 208.618 248.668 173.891 1.00 25.88  ? 1741 TRP A CG    1 
ATOM   1657  C  CD1   . TRP A 1 1741 ? 207.461 247.960 173.758 1.00 28.43  ? 1741 TRP A CD1   1 
ATOM   1658  C  CD2   . TRP A 1 1741 ? 209.548 247.797 174.546 1.00 22.96  ? 1741 TRP A CD2   1 
ATOM   1659  N  NE1   . TRP A 1 1741 ? 207.610 246.705 174.293 1.00 28.26  ? 1741 TRP A NE1   1 
ATOM   1660  C  CE2   . TRP A 1 1741 ? 208.883 246.580 174.784 1.00 21.18  ? 1741 TRP A CE2   1 
ATOM   1661  C  CE3   . TRP A 1 1741 ? 210.878 247.931 174.956 1.00 23.55  ? 1741 TRP A CE3   1 
ATOM   1662  C  CZ2   . TRP A 1 1741 ? 209.501 245.503 175.413 1.00 23.71  ? 1741 TRP A CZ2   1 
ATOM   1663  C  CZ3   . TRP A 1 1741 ? 211.488 246.862 175.582 1.00 21.81  ? 1741 TRP A CZ3   1 
ATOM   1664  C  CH2   . TRP A 1 1741 ? 210.801 245.663 175.804 1.00 21.58  ? 1741 TRP A CH2   1 
ATOM   1665  N  N     . ILE A 1 1742 ? 209.766 251.067 176.339 1.00 22.69  ? 1742 ILE A N     1 
ATOM   1666  C  CA    . ILE A 1 1742 ? 210.067 250.779 177.739 1.00 21.69  ? 1742 ILE A CA    1 
ATOM   1667  C  C     . ILE A 1 1742 ? 209.144 251.569 178.655 1.00 25.78  ? 1742 ILE A C     1 
ATOM   1668  O  O     . ILE A 1 1742 ? 208.606 251.036 179.634 1.00 27.30  ? 1742 ILE A O     1 
ATOM   1669  C  CB    . ILE A 1 1742 ? 211.549 251.073 178.036 1.00 24.94  ? 1742 ILE A CB    1 
ATOM   1670  C  CG1   . ILE A 1 1742 ? 212.444 250.028 177.373 1.00 28.46  ? 1742 ILE A CG1   1 
ATOM   1671  C  CG2   . ILE A 1 1742 ? 211.800 251.103 179.535 1.00 19.75  ? 1742 ILE A CG2   1 
ATOM   1672  C  CD1   . ILE A 1 1742 ? 213.916 250.355 177.455 1.00 28.78  ? 1742 ILE A CD1   1 
ATOM   1673  N  N     . ASP A 1 1743 ? 208.939 252.852 178.350 1.00 25.16  ? 1743 ASP A N     1 
ATOM   1674  C  CA    . ASP A 1 1743 ? 208.055 253.678 179.165 1.00 25.99  ? 1743 ASP A CA    1 
ATOM   1675  C  C     . ASP A 1 1743 ? 206.603 253.233 179.056 1.00 23.37  ? 1743 ASP A C     1 
ATOM   1676  O  O     . ASP A 1 1743 ? 205.845 253.358 180.026 1.00 22.92  ? 1743 ASP A O     1 
ATOM   1677  C  CB    . ASP A 1 1743 ? 208.186 255.145 178.759 1.00 22.77  ? 1743 ASP A CB    1 
ATOM   1678  C  CG    . ASP A 1 1743 ? 209.367 255.826 179.412 1.00 27.76  ? 1743 ASP A CG    1 
ATOM   1679  O  OD1   . ASP A 1 1743 ? 209.873 255.297 180.424 1.00 35.47  ? 1743 ASP A OD1   1 
ATOM   1680  O  OD2   . ASP A 1 1743 ? 209.791 256.890 178.915 1.00 31.29  ? 1743 ASP A OD2   1 
ATOM   1681  N  N     . LYS A 1 1744 ? 206.198 252.724 177.892 1.00 22.71  ? 1744 LYS A N     1 
ATOM   1682  C  CA    . LYS A 1 1744 ? 204.796 252.375 177.680 1.00 19.85  ? 1744 LYS A CA    1 
ATOM   1683  C  C     . LYS A 1 1744 ? 204.353 251.233 178.588 1.00 22.59  ? 1744 LYS A C     1 
ATOM   1684  O  O     . LYS A 1 1744 ? 203.247 251.267 179.138 1.00 22.11  ? 1744 LYS A O     1 
ATOM   1685  C  CB    . LYS A 1 1744 ? 204.567 252.014 176.214 1.00 17.27  ? 1744 LYS A CB    1 
ATOM   1686  C  CG    . LYS A 1 1744 ? 203.137 251.626 175.882 1.00 19.37  ? 1744 LYS A CG    1 
ATOM   1687  C  CD    . LYS A 1 1744 ? 202.900 251.639 174.382 1.00 28.28  ? 1744 LYS A CD    1 
ATOM   1688  C  CE    . LYS A 1 1744 ? 201.502 251.161 174.039 1.00 28.78  ? 1744 LYS A CE    1 
ATOM   1689  N  NZ    . LYS A 1 1744 ? 200.465 251.863 174.843 1.00 26.05  ? 1744 LYS A NZ    1 
ATOM   1690  N  N     . TYR A 1 1745 ? 205.197 250.223 178.762 1.00 23.02  ? 1745 TYR A N     1 
ATOM   1691  C  CA    . TYR A 1 1745 ? 204.802 248.990 179.424 1.00 15.04  ? 1745 TYR A CA    1 
ATOM   1692  C  C     . TYR A 1 1745 ? 205.466 248.861 180.789 1.00 16.93  ? 1745 TYR A C     1 
ATOM   1693  O  O     . TYR A 1 1745 ? 206.443 249.545 181.101 1.00 23.25  ? 1745 TYR A O     1 
ATOM   1694  C  CB    . TYR A 1 1745 ? 205.143 247.779 178.552 1.00 15.32  ? 1745 TYR A CB    1 
ATOM   1695  C  CG    . TYR A 1 1745 ? 204.370 247.755 177.257 1.00 17.65  ? 1745 TYR A CG    1 
ATOM   1696  C  CD1   . TYR A 1 1745 ? 203.030 247.391 177.232 1.00 18.90  ? 1745 TYR A CD1   1 
ATOM   1697  C  CD2   . TYR A 1 1745 ? 204.974 248.114 176.062 1.00 15.83  ? 1745 TYR A CD2   1 
ATOM   1698  C  CE1   . TYR A 1 1745 ? 202.319 247.378 176.051 1.00 21.00  ? 1745 TYR A CE1   1 
ATOM   1699  C  CE2   . TYR A 1 1745 ? 204.271 248.103 174.876 1.00 22.46  ? 1745 TYR A CE2   1 
ATOM   1700  C  CZ    . TYR A 1 1745 ? 202.943 247.734 174.877 1.00 26.29  ? 1745 TYR A CZ    1 
ATOM   1701  O  OH    . TYR A 1 1745 ? 202.240 247.722 173.695 1.00 30.06  ? 1745 TYR A OH    1 
ATOM   1702  N  N     . GLN A 1 1746 ? 204.913 247.961 181.597 1.00 17.74  ? 1746 GLN A N     1 
ATOM   1703  C  CA    . GLN A 1 1746 ? 205.373 247.753 182.959 1.00 14.65  ? 1746 GLN A CA    1 
ATOM   1704  C  C     . GLN A 1 1746 ? 206.737 247.068 182.976 1.00 14.55  ? 1746 GLN A C     1 
ATOM   1705  O  O     . GLN A 1 1746 ? 207.167 246.451 181.996 1.00 17.50  ? 1746 GLN A O     1 
ATOM   1706  C  CB    . GLN A 1 1746 ? 204.355 246.918 183.737 1.00 13.84  ? 1746 GLN A CB    1 
ATOM   1707  C  CG    . GLN A 1 1746 ? 203.127 247.696 184.191 1.00 21.56  ? 1746 GLN A CG    1 
ATOM   1708  C  CD    . GLN A 1 1746 ? 202.140 247.946 183.067 1.00 20.66  ? 1746 GLN A CD    1 
ATOM   1709  O  OE1   . GLN A 1 1746 ? 202.271 247.394 181.976 1.00 20.05  ? 1746 GLN A OE1   1 
ATOM   1710  N  NE2   . GLN A 1 1746 ? 201.143 248.783 183.330 1.00 16.94  ? 1746 GLN A NE2   1 
ATOM   1711  N  N     . ALA A 1 1747 ? 207.422 247.185 184.117 1.00 15.87  ? 1747 ALA A N     1 
ATOM   1712  C  CA    . ALA A 1 1747 ? 208.758 246.611 184.251 1.00 12.62  ? 1747 ALA A CA    1 
ATOM   1713  C  C     . ALA A 1 1747 ? 208.728 245.094 184.119 1.00 15.03  ? 1747 ALA A C     1 
ATOM   1714  O  O     . ALA A 1 1747 ? 209.646 244.493 183.550 1.00 17.87  ? 1747 ALA A O     1 
ATOM   1715  C  CB    . ALA A 1 1747 ? 209.372 247.022 185.590 1.00 11.63  ? 1747 ALA A CB    1 
ATOM   1716  N  N     . GLN A 1 1748 ? 207.689 244.457 184.660 1.00 14.52  ? 1748 GLN A N     1 
ATOM   1717  C  CA    . GLN A 1 1748 ? 207.507 243.022 184.470 1.00 12.84  ? 1748 GLN A CA    1 
ATOM   1718  C  C     . GLN A 1 1748 ? 207.357 242.678 182.994 1.00 14.69  ? 1748 GLN A C     1 
ATOM   1719  O  O     . GLN A 1 1748 ? 208.018 241.760 182.482 1.00 16.97  ? 1748 GLN A O     1 
ATOM   1720  C  CB    . GLN A 1 1748 ? 206.276 242.569 185.253 1.00 10.32  ? 1748 GLN A CB    1 
ATOM   1721  C  CG    . GLN A 1 1748 ? 205.979 241.088 185.223 1.00 13.46  ? 1748 GLN A CG    1 
ATOM   1722  C  CD    . GLN A 1 1748 ? 204.764 240.740 186.060 1.00 16.42  ? 1748 GLN A CD    1 
ATOM   1723  O  OE1   . GLN A 1 1748 ? 204.123 241.619 186.635 1.00 11.71  ? 1748 GLN A OE1   1 
ATOM   1724  N  NE2   . GLN A 1 1748 ? 204.436 239.457 186.130 1.00 15.57  ? 1748 GLN A NE2   1 
ATOM   1725  N  N     . LEU A 1 1749 ? 206.515 243.432 182.288 1.00 14.54  ? 1749 LEU A N     1 
ATOM   1726  C  CA    . LEU A 1 1749 ? 206.122 243.050 180.940 1.00 13.28  ? 1749 LEU A CA    1 
ATOM   1727  C  C     . LEU A 1 1749 ? 207.231 243.289 179.927 1.00 13.29  ? 1749 LEU A C     1 
ATOM   1728  O  O     . LEU A 1 1749 ? 207.347 242.528 178.965 1.00 18.49  ? 1749 LEU A O     1 
ATOM   1729  C  CB    . LEU A 1 1749 ? 204.858 243.806 180.539 1.00 16.56  ? 1749 LEU A CB    1 
ATOM   1730  C  CG    . LEU A 1 1749 ? 203.642 243.452 181.395 1.00 14.67  ? 1749 LEU A CG    1 
ATOM   1731  C  CD1   . LEU A 1 1749 ? 202.434 244.249 180.959 1.00 17.52  ? 1749 LEU A CD1   1 
ATOM   1732  C  CD2   . LEU A 1 1749 ? 203.359 241.961 181.336 1.00 15.48  ? 1749 LEU A CD2   1 
ATOM   1733  N  N     . VAL A 1 1750 ? 208.049 244.327 180.111 1.00 10.85  ? 1750 VAL A N     1 
ATOM   1734  C  CA    . VAL A 1 1750 ? 209.134 244.565 179.163 1.00 13.65  ? 1750 VAL A CA    1 
ATOM   1735  C  C     . VAL A 1 1750 ? 210.151 243.431 179.220 1.00 11.91  ? 1750 VAL A C     1 
ATOM   1736  O  O     . VAL A 1 1750 ? 210.600 242.929 178.180 1.00 16.67  ? 1750 VAL A O     1 
ATOM   1737  C  CB    . VAL A 1 1750 ? 209.787 245.940 179.409 1.00 14.31  ? 1750 VAL A CB    1 
ATOM   1738  C  CG1   . VAL A 1 1750 ? 208.849 247.054 178.980 1.00 17.20  ? 1750 VAL A CG1   1 
ATOM   1739  C  CG2   . VAL A 1 1750 ? 210.182 246.111 180.862 1.00 13.66  ? 1750 VAL A CG2   1 
ATOM   1740  N  N     . VAL A 1 1751 ? 210.517 242.996 180.427 1.00 8.22   ? 1751 VAL A N     1 
ATOM   1741  C  CA    . VAL A 1 1751 ? 211.445 241.879 180.567 1.00 9.67   ? 1751 VAL A CA    1 
ATOM   1742  C  C     . VAL A 1 1751 ? 210.825 240.598 180.027 1.00 8.72   ? 1751 VAL A C     1 
ATOM   1743  O  O     . VAL A 1 1751 ? 211.489 239.817 179.332 1.00 9.53   ? 1751 VAL A O     1 
ATOM   1744  C  CB    . VAL A 1 1751 ? 211.880 241.727 182.035 1.00 9.91   ? 1751 VAL A CB    1 
ATOM   1745  C  CG1   . VAL A 1 1751 ? 212.921 240.629 182.170 1.00 6.44   ? 1751 VAL A CG1   1 
ATOM   1746  C  CG2   . VAL A 1 1751 ? 212.421 243.044 182.561 1.00 10.58  ? 1751 VAL A CG2   1 
ATOM   1747  N  N     . LEU A 1 1752 ? 209.545 240.360 180.330 1.00 8.76   ? 1752 LEU A N     1 
ATOM   1748  C  CA    . LEU A 1 1752 ? 208.885 239.163 179.819 1.00 8.21   ? 1752 LEU A CA    1 
ATOM   1749  C  C     . LEU A 1 1752 ? 208.859 239.154 178.294 1.00 11.39  ? 1752 LEU A C     1 
ATOM   1750  O  O     . LEU A 1 1752 ? 209.119 238.122 177.665 1.00 12.71  ? 1752 LEU A O     1 
ATOM   1751  C  CB    . LEU A 1 1752 ? 207.469 239.068 180.386 1.00 7.68   ? 1752 LEU A CB    1 
ATOM   1752  C  CG    . LEU A 1 1752 ? 206.826 237.682 180.444 1.00 8.20   ? 1752 LEU A CG    1 
ATOM   1753  C  CD1   . LEU A 1 1752 ? 207.711 236.711 181.203 1.00 6.81   ? 1752 LEU A CD1   1 
ATOM   1754  C  CD2   . LEU A 1 1752 ? 205.458 237.770 181.085 1.00 9.55   ? 1752 LEU A CD2   1 
ATOM   1755  N  N     . SER A 1 1753 ? 208.559 240.301 177.683 1.00 10.07  ? 1753 SER A N     1 
ATOM   1756  C  CA    . SER A 1 1753 ? 208.501 240.390 176.229 1.00 9.90   ? 1753 SER A CA    1 
ATOM   1757  C  C     . SER A 1 1753 ? 209.876 240.207 175.606 1.00 10.94  ? 1753 SER A C     1 
ATOM   1758  O  O     . SER A 1 1753 ? 210.004 239.569 174.556 1.00 10.16  ? 1753 SER A O     1 
ATOM   1759  C  CB    . SER A 1 1753 ? 207.901 241.732 175.816 1.00 14.60  ? 1753 SER A CB    1 
ATOM   1760  O  OG    . SER A 1 1753 ? 206.604 241.889 176.359 1.00 22.79  ? 1753 SER A OG    1 
ATOM   1761  N  N     . ALA A 1 1754 ? 210.914 240.774 176.225 1.00 10.04  ? 1754 ALA A N     1 
ATOM   1762  C  CA    . ALA A 1 1754 ? 212.266 240.565 175.721 1.00 6.14   ? 1754 ALA A CA    1 
ATOM   1763  C  C     . ALA A 1 1754 ? 212.645 239.092 175.771 1.00 9.20   ? 1754 ALA A C     1 
ATOM   1764  O  O     . ALA A 1 1754 ? 213.226 238.557 174.817 1.00 15.99  ? 1754 ALA A O     1 
ATOM   1765  C  CB    . ALA A 1 1754 ? 213.261 241.405 176.519 1.00 6.81   ? 1754 ALA A CB    1 
ATOM   1766  N  N     . GLN A 1 1755 ? 212.311 238.415 176.874 1.00 9.10   ? 1755 GLN A N     1 
ATOM   1767  C  CA    . GLN A 1 1755 ? 212.585 236.985 176.972 1.00 7.96   ? 1755 GLN A CA    1 
ATOM   1768  C  C     . GLN A 1 1755 ? 211.830 236.202 175.906 1.00 8.54   ? 1755 GLN A C     1 
ATOM   1769  O  O     . GLN A 1 1755 ? 212.391 235.300 175.273 1.00 10.62  ? 1755 GLN A O     1 
ATOM   1770  C  CB    . GLN A 1 1755 ? 212.225 236.474 178.366 1.00 5.57   ? 1755 GLN A CB    1 
ATOM   1771  C  CG    . GLN A 1 1755 ? 213.080 237.053 179.472 1.00 5.04   ? 1755 GLN A CG    1 
ATOM   1772  C  CD    . GLN A 1 1755 ? 212.606 236.651 180.850 1.00 5.81   ? 1755 GLN A CD    1 
ATOM   1773  O  OE1   . GLN A 1 1755 ? 211.429 236.794 181.180 1.00 7.18   ? 1755 GLN A OE1   1 
ATOM   1774  N  NE2   . GLN A 1 1755 ? 213.523 236.151 181.668 1.00 5.41   ? 1755 GLN A NE2   1 
ATOM   1775  N  N     . ILE A 1 1756 ? 210.555 236.535 175.689 1.00 7.38   ? 1756 ILE A N     1 
ATOM   1776  C  CA    . ILE A 1 1756 ? 209.758 235.826 174.690 1.00 7.90   ? 1756 ILE A CA    1 
ATOM   1777  C  C     . ILE A 1 1756 ? 210.342 236.025 173.298 1.00 12.39  ? 1756 ILE A C     1 
ATOM   1778  O  O     . ILE A 1 1756 ? 210.470 235.073 172.519 1.00 16.55  ? 1756 ILE A O     1 
ATOM   1779  C  CB    . ILE A 1 1756 ? 208.288 236.282 174.754 1.00 9.23   ? 1756 ILE A CB    1 
ATOM   1780  C  CG1   . ILE A 1 1756 ? 207.640 235.831 176.062 1.00 12.26  ? 1756 ILE A CG1   1 
ATOM   1781  C  CG2   . ILE A 1 1756 ? 207.508 235.741 173.566 1.00 13.43  ? 1756 ILE A CG2   1 
ATOM   1782  C  CD1   . ILE A 1 1756 ? 206.298 236.469 176.323 1.00 13.65  ? 1756 ILE A CD1   1 
ATOM   1783  N  N     . ALA A 1 1757 ? 210.704 237.266 172.964 1.00 9.93   ? 1757 ALA A N     1 
ATOM   1784  C  CA    . ALA A 1 1757 ? 211.250 237.548 171.640 1.00 10.16  ? 1757 ALA A CA    1 
ATOM   1785  C  C     . ALA A 1 1757 ? 212.579 236.839 171.426 1.00 11.99  ? 1757 ALA A C     1 
ATOM   1786  O  O     . ALA A 1 1757 ? 212.822 236.274 170.352 1.00 16.98  ? 1757 ALA A O     1 
ATOM   1787  C  CB    . ALA A 1 1757 ? 211.407 239.056 171.450 1.00 17.03  ? 1757 ALA A CB    1 
ATOM   1788  N  N     . TRP A 1 1758 ? 213.453 236.852 172.435 1.00 10.20  ? 1758 TRP A N     1 
ATOM   1789  C  CA    . TRP A 1 1758 ? 214.733 236.169 172.297 1.00 9.79   ? 1758 TRP A CA    1 
ATOM   1790  C  C     . TRP A 1 1758 ? 214.543 234.664 172.157 1.00 12.36  ? 1758 TRP A C     1 
ATOM   1791  O  O     . TRP A 1 1758 ? 215.220 234.019 171.347 1.00 18.57  ? 1758 TRP A O     1 
ATOM   1792  C  CB    . TRP A 1 1758 ? 215.632 236.492 173.488 1.00 8.06   ? 1758 TRP A CB    1 
ATOM   1793  C  CG    . TRP A 1 1758 ? 216.878 235.673 173.531 1.00 7.19   ? 1758 TRP A CG    1 
ATOM   1794  C  CD1   . TRP A 1 1758 ? 218.003 235.854 172.785 1.00 7.89   ? 1758 TRP A CD1   1 
ATOM   1795  C  CD2   . TRP A 1 1758 ? 217.128 234.541 174.368 1.00 6.19   ? 1758 TRP A CD2   1 
ATOM   1796  N  NE1   . TRP A 1 1758 ? 218.940 234.903 173.104 1.00 7.26   ? 1758 TRP A NE1   1 
ATOM   1797  C  CE2   . TRP A 1 1758 ? 218.426 234.084 174.075 1.00 6.69   ? 1758 TRP A CE2   1 
ATOM   1798  C  CE3   . TRP A 1 1758 ? 216.381 233.868 175.339 1.00 6.90   ? 1758 TRP A CE3   1 
ATOM   1799  C  CZ2   . TRP A 1 1758 ? 218.993 232.988 174.714 1.00 7.05   ? 1758 TRP A CZ2   1 
ATOM   1800  C  CZ3   . TRP A 1 1758 ? 216.944 232.781 175.971 1.00 9.47   ? 1758 TRP A CZ3   1 
ATOM   1801  C  CH2   . TRP A 1 1758 ? 218.236 232.351 175.658 1.00 8.54   ? 1758 TRP A CH2   1 
ATOM   1802  N  N     . SER A 1 1759 ? 213.627 234.086 172.940 1.00 10.04  ? 1759 SER A N     1 
ATOM   1803  C  CA    . SER A 1 1759 ? 213.366 232.655 172.831 1.00 11.63  ? 1759 SER A CA    1 
ATOM   1804  C  C     . SER A 1 1759 ? 212.836 232.299 171.450 1.00 16.07  ? 1759 SER A C     1 
ATOM   1805  O  O     . SER A 1 1759 ? 213.259 231.301 170.854 1.00 18.09  ? 1759 SER A O     1 
ATOM   1806  C  CB    . SER A 1 1759 ? 212.377 232.218 173.912 1.00 10.28  ? 1759 SER A CB    1 
ATOM   1807  O  OG    . SER A 1 1759 ? 212.890 232.471 175.207 1.00 12.37  ? 1759 SER A OG    1 
ATOM   1808  N  N     . GLU A 1 1760 ? 211.915 233.108 170.922 1.00 16.99  ? 1760 GLU A N     1 
ATOM   1809  C  CA    . GLU A 1 1760 ? 211.383 232.851 169.588 1.00 15.34  ? 1760 GLU A CA    1 
ATOM   1810  C  C     . GLU A 1 1760 ? 212.470 232.964 168.526 1.00 18.25  ? 1760 GLU A C     1 
ATOM   1811  O  O     . GLU A 1 1760 ? 212.524 232.150 167.596 1.00 25.67  ? 1760 GLU A O     1 
ATOM   1812  C  CB    . GLU A 1 1760 ? 210.234 233.811 169.289 1.00 18.57  ? 1760 GLU A CB    1 
ATOM   1813  C  CG    . GLU A 1 1760 ? 208.963 233.515 170.071 1.00 29.96  ? 1760 GLU A CG    1 
ATOM   1814  C  CD    . GLU A 1 1760 ? 207.819 234.434 169.694 1.00 54.90  ? 1760 GLU A CD    1 
ATOM   1815  O  OE1   . GLU A 1 1760 ? 208.009 235.668 169.732 1.00 43.15  ? 1760 GLU A OE1   1 
ATOM   1816  O  OE2   . GLU A 1 1760 ? 206.728 233.924 169.361 1.00 60.06  ? 1760 GLU A OE2   1 
ATOM   1817  N  N     . ASN A 1 1761 ? 213.346 233.964 168.647 1.00 19.42  ? 1761 ASN A N     1 
ATOM   1818  C  CA    . ASN A 1 1761 ? 214.423 234.128 167.675 1.00 19.04  ? 1761 ASN A CA    1 
ATOM   1819  C  C     . ASN A 1 1761 ? 215.375 232.938 167.702 1.00 20.13  ? 1761 ASN A C     1 
ATOM   1820  O  O     . ASN A 1 1761 ? 215.767 232.415 166.651 1.00 25.23  ? 1761 ASN A O     1 
ATOM   1821  C  CB    . ASN A 1 1761 ? 215.180 235.428 167.946 1.00 17.70  ? 1761 ASN A CB    1 
ATOM   1822  C  CG    . ASN A 1 1761 ? 214.370 236.656 167.594 1.00 18.75  ? 1761 ASN A CG    1 
ATOM   1823  O  OD1   . ASN A 1 1761 ? 213.197 236.559 167.235 1.00 18.70  ? 1761 ASN A OD1   1 
ATOM   1824  N  ND2   . ASN A 1 1761 ? 214.993 237.823 167.694 1.00 26.39  ? 1761 ASN A ND2   1 
ATOM   1825  N  N     . VAL A 1 1762 ? 215.759 232.494 168.901 1.00 20.05  ? 1762 VAL A N     1 
ATOM   1826  C  CA    . VAL A 1 1762 ? 216.666 231.356 169.009 1.00 20.65  ? 1762 VAL A CA    1 
ATOM   1827  C  C     . VAL A 1 1762 ? 216.005 230.092 168.475 1.00 21.40  ? 1762 VAL A C     1 
ATOM   1828  O  O     . VAL A 1 1762 ? 216.641 229.285 167.788 1.00 26.90  ? 1762 VAL A O     1 
ATOM   1829  C  CB    . VAL A 1 1762 ? 217.141 231.178 170.463 1.00 16.15  ? 1762 VAL A CB    1 
ATOM   1830  C  CG1   . VAL A 1 1762 ? 217.988 229.923 170.592 1.00 13.46  ? 1762 VAL A CG1   1 
ATOM   1831  C  CG2   . VAL A 1 1762 ? 217.927 232.393 170.915 1.00 16.09  ? 1762 VAL A CG2   1 
ATOM   1832  N  N     . GLU A 1 1763 ? 214.718 229.899 168.781 1.00 23.65  ? 1763 GLU A N     1 
ATOM   1833  C  CA    . GLU A 1 1763 ? 214.007 228.725 168.288 1.00 24.78  ? 1763 GLU A CA    1 
ATOM   1834  C  C     . GLU A 1 1763 ? 213.929 228.727 166.767 1.00 32.59  ? 1763 GLU A C     1 
ATOM   1835  O  O     . GLU A 1 1763 ? 214.122 227.688 166.126 1.00 36.07  ? 1763 GLU A O     1 
ATOM   1836  C  CB    . GLU A 1 1763 ? 212.608 228.674 168.903 1.00 20.65  ? 1763 GLU A CB    1 
ATOM   1837  C  CG    . GLU A 1 1763 ? 211.778 227.466 168.504 1.00 36.62  ? 1763 GLU A CG    1 
ATOM   1838  C  CD    . GLU A 1 1763 ? 212.359 226.160 169.009 1.00 46.86  ? 1763 GLU A CD    1 
ATOM   1839  O  OE1   . GLU A 1 1763 ? 213.078 226.180 170.030 1.00 40.37  ? 1763 GLU A OE1   1 
ATOM   1840  O  OE2   . GLU A 1 1763 ? 212.091 225.110 168.387 1.00 55.69  ? 1763 GLU A OE2   1 
ATOM   1841  N  N     . THR A 1 1764 ? 213.652 229.889 166.169 1.00 27.32  ? 1764 THR A N     1 
ATOM   1842  C  CA    . THR A 1 1764 ? 213.602 229.983 164.712 1.00 26.48  ? 1764 THR A CA    1 
ATOM   1843  C  C     . THR A 1 1764 ? 214.967 229.706 164.093 1.00 33.05  ? 1764 THR A C     1 
ATOM   1844  O  O     . THR A 1 1764 ? 215.067 228.996 163.083 1.00 41.03  ? 1764 THR A O     1 
ATOM   1845  C  CB    . THR A 1 1764 ? 213.096 231.362 164.293 1.00 30.78  ? 1764 THR A CB    1 
ATOM   1846  O  OG1   . THR A 1 1764 ? 211.795 231.586 164.851 1.00 30.35  ? 1764 THR A OG1   1 
ATOM   1847  C  CG2   . THR A 1 1764 ? 213.017 231.465 162.777 1.00 38.37  ? 1764 THR A CG2   1 
ATOM   1848  N  N     . ALA A 1 1765 ? 216.029 230.256 164.685 1.00 33.42  ? 1765 ALA A N     1 
ATOM   1849  C  CA    . ALA A 1 1765 ? 217.369 230.011 164.162 1.00 28.43  ? 1765 ALA A CA    1 
ATOM   1850  C  C     . ALA A 1 1765 ? 217.731 228.534 164.242 1.00 33.62  ? 1765 ALA A C     1 
ATOM   1851  O  O     . ALA A 1 1765 ? 218.301 227.974 163.298 1.00 39.99  ? 1765 ALA A O     1 
ATOM   1852  C  CB    . ALA A 1 1765 ? 218.391 230.858 164.920 1.00 28.17  ? 1765 ALA A CB    1 
ATOM   1853  N  N     . LEU A 1 1766 ? 217.401 227.883 165.359 1.00 34.31  ? 1766 LEU A N     1 
ATOM   1854  C  CA    . LEU A 1 1766 ? 217.701 226.463 165.501 1.00 32.03  ? 1766 LEU A CA    1 
ATOM   1855  C  C     . LEU A 1 1766 ? 216.872 225.622 164.536 1.00 35.91  ? 1766 LEU A C     1 
ATOM   1856  O  O     . LEU A 1 1766 ? 217.369 224.635 163.982 1.00 35.66  ? 1766 LEU A O     1 
ATOM   1857  C  CB    . LEU A 1 1766 ? 217.469 226.023 166.946 1.00 26.48  ? 1766 LEU A CB    1 
ATOM   1858  C  CG    . LEU A 1 1766 ? 218.478 226.562 167.961 1.00 23.46  ? 1766 LEU A CG    1 
ATOM   1859  C  CD1   . LEU A 1 1766 ? 218.225 225.982 169.341 1.00 19.30  ? 1766 LEU A CD1   1 
ATOM   1860  C  CD2   . LEU A 1 1766 ? 219.901 226.278 167.513 1.00 27.76  ? 1766 LEU A CD2   1 
ATOM   1861  N  N     . SER A 1 1767 ? 215.610 225.997 164.319 1.00 39.00  ? 1767 SER A N     1 
ATOM   1862  C  CA    . SER A 1 1767 ? 214.786 225.281 163.350 1.00 38.26  ? 1767 SER A CA    1 
ATOM   1863  C  C     . SER A 1 1767 ? 215.357 225.411 161.946 1.00 48.23  ? 1767 SER A C     1 
ATOM   1864  O  O     . SER A 1 1767 ? 215.343 224.449 161.169 1.00 61.79  ? 1767 SER A O     1 
ATOM   1865  C  CB    . SER A 1 1767 ? 213.349 225.799 163.398 1.00 36.09  ? 1767 SER A CB    1 
ATOM   1866  O  OG    . SER A 1 1767 ? 212.796 225.646 164.693 1.00 53.74  ? 1767 SER A OG    1 
ATOM   1867  N  N     . SER A 1 1768 ? 215.856 226.599 161.597 1.00 41.85  ? 1768 SER A N     1 
ATOM   1868  C  CA    . SER A 1 1768 ? 216.507 226.771 160.302 1.00 35.69  ? 1768 SER A CA    1 
ATOM   1869  C  C     . SER A 1 1768 ? 217.778 225.935 160.206 1.00 44.91  ? 1768 SER A C     1 
ATOM   1870  O  O     . SER A 1 1768 ? 218.042 225.310 159.173 1.00 51.00  ? 1768 SER A O     1 
ATOM   1871  C  CB    . SER A 1 1768 ? 216.819 228.247 160.064 1.00 37.55  ? 1768 SER A CB    1 
ATOM   1872  O  OG    . SER A 1 1768 ? 217.787 228.716 160.986 1.00 53.97  ? 1768 SER A OG    1 
ATOM   1873  N  N     . MET A 1 1769 ? 218.574 225.905 161.277 1.00 44.19  ? 1769 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1769 ? 219.859 225.215 161.260 1.00 44.79  ? 1769 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1769 ? 219.734 223.707 161.429 1.00 52.44  ? 1769 MET A C     1 
ATOM   1876  O  O     . MET A 1 1769 ? 220.737 223.000 161.275 1.00 57.75  ? 1769 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1769 ? 220.766 225.775 162.357 1.00 41.15  ? 1769 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1769 ? 221.299 227.161 162.057 1.00 48.19  ? 1769 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1769 ? 222.157 227.937 163.440 1.00 57.93  ? 1769 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1769 ? 222.873 226.513 164.248 1.00 38.81  ? 1769 MET A CE    1 
ATOM   1881  N  N     . GLY A 1 1770 ? 218.545 223.202 161.752 1.00 60.41  ? 1770 GLY A N     1 
ATOM   1882  C  CA    . GLY A 1 1770 ? 218.332 221.777 161.933 1.00 63.19  ? 1770 GLY A CA    1 
ATOM   1883  C  C     . GLY A 1 1770 ? 218.753 220.883 160.782 1.00 74.73  ? 1770 GLY A C     1 
ATOM   1884  O  O     . GLY A 1 1770 ? 218.788 219.658 160.930 1.00 76.65  ? 1770 GLY A O     1 
ATOM   1885  N  N     . GLY A 1 1771 ? 219.071 221.475 159.629 1.00 73.68  ? 1771 GLY A N     1 
ATOM   1886  C  CA    . GLY A 1 1771 ? 219.561 220.691 158.509 1.00 76.85  ? 1771 GLY A CA    1 
ATOM   1887  C  C     . GLY A 1 1771 ? 220.946 220.119 158.719 1.00 83.32  ? 1771 GLY A C     1 
ATOM   1888  O  O     . GLY A 1 1771 ? 221.295 219.120 158.081 1.00 83.88  ? 1771 GLY A O     1 
ATOM   1889  N  N     . GLY A 1 1772 ? 221.741 220.728 159.594 1.00 85.28  ? 1772 GLY A N     1 
ATOM   1890  C  CA    . GLY A 1 1772 ? 223.071 220.232 159.889 1.00 81.31  ? 1772 GLY A CA    1 
ATOM   1891  C  C     . GLY A 1 1772 ? 224.130 220.729 158.926 1.00 86.79  ? 1772 GLY A C     1 
ATOM   1892  O  O     . GLY A 1 1772 ? 223.960 220.634 157.707 1.00 89.84  ? 1772 GLY A O     1 
ATOM   1893  N  N     . GLY A 1 1773 ? 225.228 221.254 159.461 1.00 83.69  ? 1773 GLY A N     1 
ATOM   1894  C  CA    . GLY A 1 1773 ? 226.307 221.749 158.619 1.00 91.15  ? 1773 GLY A CA    1 
ATOM   1895  C  C     . GLY A 1 1773 ? 225.905 222.909 157.734 1.00 96.36  ? 1773 GLY A C     1 
ATOM   1896  O  O     . GLY A 1 1773 ? 226.231 222.918 156.540 1.00 100.17 ? 1773 GLY A O     1 
ATOM   1897  N  N     . ASP A 1 1774 ? 225.201 223.888 158.292 1.00 95.21  ? 1774 ASP A N     1 
ATOM   1898  C  CA    . ASP A 1 1774 ? 224.671 225.010 157.535 1.00 96.34  ? 1774 ASP A CA    1 
ATOM   1899  C  C     . ASP A 1 1774 ? 225.121 226.321 158.165 1.00 94.67  ? 1774 ASP A C     1 
ATOM   1900  O  O     . ASP A 1 1774 ? 225.444 226.377 159.355 1.00 85.51  ? 1774 ASP A O     1 
ATOM   1901  C  CB    . ASP A 1 1774 ? 223.136 224.950 157.473 1.00 93.24  ? 1774 ASP A CB    1 
ATOM   1902  C  CG    . ASP A 1 1774 ? 222.537 226.077 156.658 1.00 100.89 ? 1774 ASP A CG    1 
ATOM   1903  O  OD1   . ASP A 1 1774 ? 222.824 226.154 155.445 1.00 101.03 ? 1774 ASP A OD1   1 
ATOM   1904  O  OD2   . ASP A 1 1774 ? 221.777 226.887 157.229 1.00 95.18  ? 1774 ASP A OD2   1 
ATOM   1905  N  N     . ALA A 1 1775 ? 225.155 227.373 157.347 1.00 95.35  ? 1775 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 1775 ? 225.474 228.702 157.849 1.00 89.29  ? 1775 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 1775 ? 224.503 229.093 158.955 1.00 85.12  ? 1775 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 1775 ? 223.294 228.873 158.851 1.00 79.06  ? 1775 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 1775 ? 225.426 229.725 156.714 1.00 87.15  ? 1775 ALA A CB    1 
ATOM   1910  N  N     . ALA A 1 1776 ? 225.045 229.676 160.021 1.00 76.70  ? 1776 ALA A N     1 
ATOM   1911  C  CA    . ALA A 1 1776 ? 224.283 229.890 161.242 1.00 52.96  ? 1776 ALA A CA    1 
ATOM   1912  C  C     . ALA A 1 1776 ? 223.691 231.292 161.264 1.00 50.83  ? 1776 ALA A C     1 
ATOM   1913  O  O     . ALA A 1 1776 ? 224.449 232.271 161.270 1.00 39.86  ? 1776 ALA A O     1 
ATOM   1914  C  CB    . ALA A 1 1776 ? 225.164 229.683 162.461 1.00 39.21  ? 1776 ALA A CB    1 
ATOM   1915  N  N     . PRO A 1 1777 ? 222.364 231.440 161.266 1.00 49.46  ? 1777 PRO A N     1 
ATOM   1916  C  CA    . PRO A 1 1777 ? 221.758 232.734 161.600 1.00 38.94  ? 1777 PRO A CA    1 
ATOM   1917  C  C     . PRO A 1 1777 ? 221.658 232.991 163.094 1.00 37.29  ? 1777 PRO A C     1 
ATOM   1918  O  O     . PRO A 1 1777 ? 221.081 234.008 163.492 1.00 36.67  ? 1777 PRO A O     1 
ATOM   1919  C  CB    . PRO A 1 1777 ? 220.365 232.628 160.966 1.00 41.89  ? 1777 PRO A CB    1 
ATOM   1920  C  CG    . PRO A 1 1777 ? 220.053 231.180 161.019 1.00 35.06  ? 1777 PRO A CG    1 
ATOM   1921  C  CD    . PRO A 1 1777 ? 221.359 230.458 160.825 1.00 45.82  ? 1777 PRO A CD    1 
ATOM   1922  N  N     . LEU A 1 1778 ? 222.181 232.088 163.927 1.00 34.68  ? 1778 LEU A N     1 
ATOM   1923  C  CA    . LEU A 1 1778 ? 222.224 232.340 165.363 1.00 30.88  ? 1778 LEU A CA    1 
ATOM   1924  C  C     . LEU A 1 1778 ? 223.142 233.516 165.676 1.00 29.49  ? 1778 LEU A C     1 
ATOM   1925  O  O     . LEU A 1 1778 ? 222.939 234.232 166.666 1.00 28.10  ? 1778 LEU A O     1 
ATOM   1926  C  CB    . LEU A 1 1778 ? 222.683 231.076 166.093 1.00 33.85  ? 1778 LEU A CB    1 
ATOM   1927  C  CG    . LEU A 1 1778 ? 222.338 230.927 167.575 1.00 33.21  ? 1778 LEU A CG    1 
ATOM   1928  C  CD1   . LEU A 1 1778 ? 220.833 230.888 167.773 1.00 25.41  ? 1778 LEU A CD1   1 
ATOM   1929  C  CD2   . LEU A 1 1778 ? 222.982 229.672 168.136 1.00 23.60  ? 1778 LEU A CD2   1 
ATOM   1930  N  N     . HIS A 1 1779 ? 224.156 233.730 164.834 1.00 32.40  ? 1779 HIS A N     1 
ATOM   1931  C  CA    . HIS A 1 1779 ? 224.997 234.913 164.963 1.00 29.64  ? 1779 HIS A CA    1 
ATOM   1932  C  C     . HIS A 1 1779 ? 224.180 236.186 164.795 1.00 26.07  ? 1779 HIS A C     1 
ATOM   1933  O  O     . HIS A 1 1779 ? 224.478 237.211 165.416 1.00 25.16  ? 1779 HIS A O     1 
ATOM   1934  C  CB    . HIS A 1 1779 ? 226.131 234.865 163.938 1.00 30.06  ? 1779 HIS A CB    1 
ATOM   1935  C  CG    . HIS A 1 1779 ? 227.056 233.701 164.114 1.00 37.38  ? 1779 HIS A CG    1 
ATOM   1936  N  ND1   . HIS A 1 1779 ? 228.005 233.649 165.113 1.00 40.78  ? 1779 HIS A ND1   1 
ATOM   1937  C  CD2   . HIS A 1 1779 ? 227.179 232.547 163.419 1.00 40.41  ? 1779 HIS A CD2   1 
ATOM   1938  C  CE1   . HIS A 1 1779 ? 228.673 232.513 165.024 1.00 33.20  ? 1779 HIS A CE1   1 
ATOM   1939  N  NE2   . HIS A 1 1779 ? 228.191 231.824 164.005 1.00 33.74  ? 1779 HIS A NE2   1 
ATOM   1940  N  N     . SER A 1 1780 ? 223.142 236.140 163.957 1.00 27.75  ? 1780 SER A N     1 
ATOM   1941  C  CA    . SER A 1 1780 ? 222.256 237.290 163.809 1.00 23.82  ? 1780 SER A CA    1 
ATOM   1942  C  C     . SER A 1 1780 ? 221.515 237.580 165.109 1.00 24.97  ? 1780 SER A C     1 
ATOM   1943  O  O     . SER A 1 1780 ? 221.349 238.741 165.500 1.00 28.69  ? 1780 SER A O     1 
ATOM   1944  C  CB    . SER A 1 1780 ? 221.268 237.051 162.667 1.00 25.64  ? 1780 SER A CB    1 
ATOM   1945  O  OG    . SER A 1 1780 ? 220.200 236.223 163.088 1.00 36.75  ? 1780 SER A OG    1 
ATOM   1946  N  N     . VAL A 1 1781 ? 221.062 236.529 165.793 1.00 28.22  ? 1781 VAL A N     1 
ATOM   1947  C  CA    . VAL A 1 1781 ? 220.409 236.704 167.090 1.00 24.33  ? 1781 VAL A CA    1 
ATOM   1948  C  C     . VAL A 1 1781 ? 221.387 237.294 168.097 1.00 22.27  ? 1781 VAL A C     1 
ATOM   1949  O  O     . VAL A 1 1781 ? 221.045 238.197 168.874 1.00 26.08  ? 1781 VAL A O     1 
ATOM   1950  C  CB    . VAL A 1 1781 ? 219.831 235.365 167.583 1.00 18.22  ? 1781 VAL A CB    1 
ATOM   1951  C  CG1   . VAL A 1 1781 ? 219.023 235.572 168.851 1.00 22.73  ? 1781 VAL A CG1   1 
ATOM   1952  C  CG2   . VAL A 1 1781 ? 218.979 234.728 166.501 1.00 22.45  ? 1781 VAL A CG2   1 
ATOM   1953  N  N     . LEU A 1 1782 ? 222.623 236.790 168.100 1.00 21.32  ? 1782 LEU A N     1 
ATOM   1954  C  CA    . LEU A 1 1782 ? 223.633 237.319 169.012 1.00 19.98  ? 1782 LEU A CA    1 
ATOM   1955  C  C     . LEU A 1 1782 ? 223.898 238.795 168.738 1.00 23.98  ? 1782 LEU A C     1 
ATOM   1956  O  O     . LEU A 1 1782 ? 224.005 239.601 169.668 1.00 24.94  ? 1782 LEU A O     1 
ATOM   1957  C  CB    . LEU A 1 1782 ? 224.923 236.507 168.895 1.00 19.47  ? 1782 LEU A CB    1 
ATOM   1958  C  CG    . LEU A 1 1782 ? 226.106 236.991 169.735 1.00 21.01  ? 1782 LEU A CG    1 
ATOM   1959  C  CD1   . LEU A 1 1782 ? 225.727 237.063 171.205 1.00 23.54  ? 1782 LEU A CD1   1 
ATOM   1960  C  CD2   . LEU A 1 1782 ? 227.310 236.089 169.535 1.00 22.26  ? 1782 LEU A CD2   1 
ATOM   1961  N  N     . SER A 1 1783 ? 223.996 239.168 167.460 1.00 24.52  ? 1783 SER A N     1 
ATOM   1962  C  CA    . SER A 1 1783 ? 224.241 240.564 167.108 1.00 21.95  ? 1783 SER A CA    1 
ATOM   1963  C  C     . SER A 1 1783 ? 223.056 241.447 167.479 1.00 23.17  ? 1783 SER A C     1 
ATOM   1964  O  O     . SER A 1 1783 ? 223.237 242.594 167.903 1.00 27.07  ? 1783 SER A O     1 
ATOM   1965  C  CB    . SER A 1 1783 ? 224.551 240.678 165.615 1.00 25.55  ? 1783 SER A CB    1 
ATOM   1966  O  OG    . SER A 1 1783 ? 225.673 239.883 165.270 1.00 33.12  ? 1783 SER A OG    1 
ATOM   1967  N  N     . ASN A 1 1784 ? 221.834 240.936 167.312 1.00 23.08  ? 1784 ASN A N     1 
ATOM   1968  C  CA    . ASN A 1 1784 ? 220.661 241.679 167.752 1.00 24.84  ? 1784 ASN A CA    1 
ATOM   1969  C  C     . ASN A 1 1784 ? 220.690 241.913 169.256 1.00 24.47  ? 1784 ASN A C     1 
ATOM   1970  O  O     . ASN A 1 1784 ? 220.321 242.997 169.722 1.00 27.99  ? 1784 ASN A O     1 
ATOM   1971  C  CB    . ASN A 1 1784 ? 219.384 240.939 167.357 1.00 24.17  ? 1784 ASN A CB    1 
ATOM   1972  C  CG    . ASN A 1 1784 ? 218.138 241.770 167.581 1.00 30.81  ? 1784 ASN A CG    1 
ATOM   1973  O  OD1   . ASN A 1 1784 ? 217.344 241.491 168.479 1.00 38.79  ? 1784 ASN A OD1   1 
ATOM   1974  N  ND2   . ASN A 1 1784 ? 217.957 242.799 166.762 1.00 33.53  ? 1784 ASN A ND2   1 
ATOM   1975  N  N     . VAL A 1 1785 ? 221.117 240.912 170.025 1.00 21.39  ? 1785 VAL A N     1 
ATOM   1976  C  CA    . VAL A 1 1785 ? 221.276 241.100 171.464 1.00 21.88  ? 1785 VAL A CA    1 
ATOM   1977  C  C     . VAL A 1 1785 ? 222.342 242.154 171.748 1.00 22.31  ? 1785 VAL A C     1 
ATOM   1978  O  O     . VAL A 1 1785 ? 222.175 243.009 172.626 1.00 24.97  ? 1785 VAL A O     1 
ATOM   1979  C  CB    . VAL A 1 1785 ? 221.605 239.762 172.150 1.00 23.02  ? 1785 VAL A CB    1 
ATOM   1980  C  CG1   . VAL A 1 1785 ? 221.875 239.974 173.628 1.00 18.10  ? 1785 VAL A CG1   1 
ATOM   1981  C  CG2   . VAL A 1 1785 ? 220.460 238.781 171.967 1.00 20.69  ? 1785 VAL A CG2   1 
ATOM   1982  N  N     . GLU A 1 1786 ? 223.454 242.105 171.009 1.00 24.21  ? 1786 GLU A N     1 
ATOM   1983  C  CA    . GLU A 1 1786 ? 224.562 243.030 171.251 1.00 21.94  ? 1786 GLU A CA    1 
ATOM   1984  C  C     . GLU A 1 1786 ? 224.156 244.478 170.994 1.00 22.95  ? 1786 GLU A C     1 
ATOM   1985  O  O     . GLU A 1 1786 ? 224.489 245.374 171.778 1.00 25.16  ? 1786 GLU A O     1 
ATOM   1986  C  CB    . GLU A 1 1786 ? 225.765 242.654 170.384 1.00 24.39  ? 1786 GLU A CB    1 
ATOM   1987  C  CG    . GLU A 1 1786 ? 226.366 241.279 170.651 1.00 25.24  ? 1786 GLU A CG    1 
ATOM   1988  C  CD    . GLU A 1 1786 ? 227.178 241.200 171.935 1.00 36.09  ? 1786 GLU A CD    1 
ATOM   1989  O  OE1   . GLU A 1 1786 ? 228.077 240.336 172.007 1.00 31.26  ? 1786 GLU A OE1   1 
ATOM   1990  O  OE2   . GLU A 1 1786 ? 226.936 241.997 172.866 1.00 37.29  ? 1786 GLU A OE2   1 
ATOM   1991  N  N     . VAL A 1 1787 ? 223.453 244.735 169.888 1.00 21.64  ? 1787 VAL A N     1 
ATOM   1992  C  CA    . VAL A 1 1787 ? 223.085 246.115 169.568 1.00 22.60  ? 1787 VAL A CA    1 
ATOM   1993  C  C     . VAL A 1 1787 ? 222.058 246.645 170.564 1.00 28.12  ? 1787 VAL A C     1 
ATOM   1994  O  O     . VAL A 1 1787 ? 222.101 247.818 170.958 1.00 30.73  ? 1787 VAL A O     1 
ATOM   1995  C  CB    . VAL A 1 1787 ? 222.605 246.234 168.107 1.00 22.05  ? 1787 VAL A CB    1 
ATOM   1996  C  CG1   . VAL A 1 1787 ? 223.596 245.565 167.173 1.00 30.67  ? 1787 VAL A CG1   1 
ATOM   1997  C  CG2   . VAL A 1 1787 ? 221.223 245.628 167.920 1.00 21.21  ? 1787 VAL A CG2   1 
ATOM   1998  N  N     . THR A 1 1788 ? 221.132 245.790 171.002 1.00 27.89  ? 1788 THR A N     1 
ATOM   1999  C  CA    . THR A 1 1788 ? 220.168 246.211 172.012 1.00 26.01  ? 1788 THR A CA    1 
ATOM   2000  C  C     . THR A 1 1788 ? 220.867 246.500 173.335 1.00 23.76  ? 1788 THR A C     1 
ATOM   2001  O  O     . THR A 1 1788 ? 220.515 247.450 174.044 1.00 26.85  ? 1788 THR A O     1 
ATOM   2002  C  CB    . THR A 1 1788 ? 219.088 245.144 172.189 1.00 24.71  ? 1788 THR A CB    1 
ATOM   2003  O  OG1   . THR A 1 1788 ? 218.701 244.642 170.905 1.00 29.72  ? 1788 THR A OG1   1 
ATOM   2004  C  CG2   . THR A 1 1788 ? 217.868 245.746 172.859 1.00 20.28  ? 1788 THR A CG2   1 
ATOM   2005  N  N     . LEU A 1 1789 ? 221.870 245.690 173.678 1.00 23.60  ? 1789 LEU A N     1 
ATOM   2006  C  CA    . LEU A 1 1789 ? 222.661 245.957 174.874 1.00 20.75  ? 1789 LEU A CA    1 
ATOM   2007  C  C     . LEU A 1 1789 ? 223.414 247.273 174.752 1.00 22.59  ? 1789 LEU A C     1 
ATOM   2008  O  O     . LEU A 1 1789 ? 223.553 248.007 175.733 1.00 26.67  ? 1789 LEU A O     1 
ATOM   2009  C  CB    . LEU A 1 1789 ? 223.633 244.807 175.132 1.00 13.29  ? 1789 LEU A CB    1 
ATOM   2010  C  CG    . LEU A 1 1789 ? 223.125 243.692 176.045 1.00 13.53  ? 1789 LEU A CG    1 
ATOM   2011  C  CD1   . LEU A 1 1789 ? 224.061 242.498 176.009 1.00 16.88  ? 1789 LEU A CD1   1 
ATOM   2012  C  CD2   . LEU A 1 1789 ? 222.967 244.206 177.464 1.00 14.88  ? 1789 LEU A CD2   1 
ATOM   2013  N  N     . ASN A 1 1790 ? 223.920 247.581 173.557 1.00 26.19  ? 1790 ASN A N     1 
ATOM   2014  C  CA    . ASN A 1 1790 ? 224.595 248.859 173.347 1.00 26.07  ? 1790 ASN A CA    1 
ATOM   2015  C  C     . ASN A 1 1790 ? 223.634 250.023 173.555 1.00 28.48  ? 1790 ASN A C     1 
ATOM   2016  O  O     . ASN A 1 1790 ? 223.977 251.024 174.195 1.00 30.02  ? 1790 ASN A O     1 
ATOM   2017  C  CB    . ASN A 1 1790 ? 225.204 248.908 171.947 1.00 23.81  ? 1790 ASN A CB    1 
ATOM   2018  C  CG    . ASN A 1 1790 ? 226.391 247.984 171.795 1.00 34.50  ? 1790 ASN A CG    1 
ATOM   2019  O  OD1   . ASN A 1 1790 ? 227.137 247.754 172.747 1.00 36.11  ? 1790 ASN A OD1   1 
ATOM   2020  N  ND2   . ASN A 1 1790 ? 226.574 247.448 170.595 1.00 38.48  ? 1790 ASN A ND2   1 
ATOM   2021  N  N     . VAL A 1 1791 ? 222.419 249.905 173.016 1.00 27.94  ? 1791 VAL A N     1 
ATOM   2022  C  CA    . VAL A 1 1791 ? 221.419 250.957 173.200 1.00 23.03  ? 1791 VAL A CA    1 
ATOM   2023  C  C     . VAL A 1 1791 ? 221.089 251.125 174.677 1.00 22.82  ? 1791 VAL A C     1 
ATOM   2024  O  O     . VAL A 1 1791 ? 221.012 252.248 175.192 1.00 28.59  ? 1791 VAL A O     1 
ATOM   2025  C  CB    . VAL A 1 1791 ? 220.158 250.656 172.370 1.00 26.80  ? 1791 VAL A CB    1 
ATOM   2026  C  CG1   . VAL A 1 1791 ? 219.125 251.749 172.573 1.00 23.52  ? 1791 VAL A CG1   1 
ATOM   2027  C  CG2   . VAL A 1 1791 ? 220.511 250.535 170.901 1.00 33.03  ? 1791 VAL A CG2   1 
ATOM   2028  N  N     . LEU A 1 1792 ? 220.893 250.010 175.385 1.00 20.16  ? 1792 LEU A N     1 
ATOM   2029  C  CA    . LEU A 1 1792 ? 220.569 250.083 176.808 1.00 18.10  ? 1792 LEU A CA    1 
ATOM   2030  C  C     . LEU A 1 1792 ? 221.715 250.687 177.613 1.00 20.31  ? 1792 LEU A C     1 
ATOM   2031  O  O     . LEU A 1 1792 ? 221.486 251.485 178.529 1.00 20.79  ? 1792 LEU A O     1 
ATOM   2032  C  CB    . LEU A 1 1792 ? 220.213 248.695 177.339 1.00 21.47  ? 1792 LEU A CB    1 
ATOM   2033  C  CG    . LEU A 1 1792 ? 218.939 248.041 176.806 1.00 19.10  ? 1792 LEU A CG    1 
ATOM   2034  C  CD1   . LEU A 1 1792 ? 218.968 246.543 177.040 1.00 15.27  ? 1792 LEU A CD1   1 
ATOM   2035  C  CD2   . LEU A 1 1792 ? 217.726 248.652 177.473 1.00 11.51  ? 1792 LEU A CD2   1 
ATOM   2036  N  N     . ALA A 1 1793 ? 222.955 250.314 177.291 1.00 21.24  ? 1793 ALA A N     1 
ATOM   2037  C  CA    . ALA A 1 1793 ? 224.108 250.858 177.998 1.00 23.08  ? 1793 ALA A CA    1 
ATOM   2038  C  C     . ALA A 1 1793 ? 224.268 252.348 177.743 1.00 26.60  ? 1793 ALA A C     1 
ATOM   2039  O  O     . ALA A 1 1793 ? 224.661 253.092 178.647 1.00 34.39  ? 1793 ALA A O     1 
ATOM   2040  C  CB    . ALA A 1 1793 ? 225.376 250.108 177.593 1.00 26.15  ? 1793 ALA A CB    1 
ATOM   2041  N  N     . ASP A 1 1794 ? 223.986 252.799 176.521 1.00 25.11  ? 1794 ASP A N     1 
ATOM   2042  C  CA    . ASP A 1 1794 ? 223.962 254.234 176.263 1.00 30.45  ? 1794 ASP A CA    1 
ATOM   2043  C  C     . ASP A 1 1794 ? 222.853 254.918 177.053 1.00 29.11  ? 1794 ASP A C     1 
ATOM   2044  O  O     . ASP A 1 1794 ? 223.031 256.044 177.530 1.00 31.04  ? 1794 ASP A O     1 
ATOM   2045  C  CB    . ASP A 1 1794 ? 223.792 254.501 174.768 1.00 36.30  ? 1794 ASP A CB    1 
ATOM   2046  C  CG    . ASP A 1 1794 ? 225.007 254.092 173.962 1.00 42.16  ? 1794 ASP A CG    1 
ATOM   2047  O  OD1   . ASP A 1 1794 ? 226.011 253.668 174.572 1.00 41.91  ? 1794 ASP A OD1   1 
ATOM   2048  O  OD2   . ASP A 1 1794 ? 224.957 254.194 172.719 1.00 40.44  ? 1794 ASP A OD2   1 
ATOM   2049  N  N     . SER A 1 1795 ? 221.705 254.251 177.195 1.00 26.45  ? 1795 SER A N     1 
ATOM   2050  C  CA    . SER A 1 1795 ? 220.573 254.855 177.891 1.00 23.93  ? 1795 SER A CA    1 
ATOM   2051  C  C     . SER A 1 1795 ? 220.879 255.093 179.365 1.00 25.80  ? 1795 SER A C     1 
ATOM   2052  O  O     . SER A 1 1795 ? 220.523 256.141 179.916 1.00 34.07  ? 1795 SER A O     1 
ATOM   2053  C  CB    . SER A 1 1795 ? 219.338 253.970 177.738 1.00 24.46  ? 1795 SER A CB    1 
ATOM   2054  O  OG    . SER A 1 1795 ? 219.037 253.747 176.372 1.00 24.74  ? 1795 SER A OG    1 
ATOM   2055  N  N     . VAL A 1 1796 ? 221.531 254.134 180.026 1.00 24.50  ? 1796 VAL A N     1 
ATOM   2056  C  CA    . VAL A 1 1796 ? 221.752 254.256 181.462 1.00 23.83  ? 1796 VAL A CA    1 
ATOM   2057  C  C     . VAL A 1 1796 ? 222.842 255.267 181.793 1.00 26.11  ? 1796 VAL A C     1 
ATOM   2058  O  O     . VAL A 1 1796 ? 222.938 255.709 182.943 1.00 28.67  ? 1796 VAL A O     1 
ATOM   2059  C  CB    . VAL A 1 1796 ? 222.084 252.886 182.082 1.00 17.69  ? 1796 VAL A CB    1 
ATOM   2060  C  CG1   . VAL A 1 1796 ? 220.882 251.966 182.001 1.00 17.11  ? 1796 VAL A CG1   1 
ATOM   2061  C  CG2   . VAL A 1 1796 ? 223.284 252.264 181.395 1.00 21.48  ? 1796 VAL A CG2   1 
ATOM   2062  N  N     . LEU A 1 1797 ? 223.675 255.640 180.820 1.00 26.24  ? 1797 LEU A N     1 
ATOM   2063  C  CA    . LEU A 1 1797 ? 224.678 256.672 181.068 1.00 31.47  ? 1797 LEU A CA    1 
ATOM   2064  C  C     . LEU A 1 1797 ? 224.027 258.016 181.365 1.00 33.12  ? 1797 LEU A C     1 
ATOM   2065  O  O     . LEU A 1 1797 ? 224.457 258.733 182.276 1.00 32.08  ? 1797 LEU A O     1 
ATOM   2066  C  CB    . LEU A 1 1797 ? 225.616 256.795 179.871 1.00 33.18  ? 1797 LEU A CB    1 
ATOM   2067  C  CG    . LEU A 1 1797 ? 226.515 255.603 179.559 1.00 33.16  ? 1797 LEU A CG    1 
ATOM   2068  C  CD1   . LEU A 1 1797 ? 227.258 255.861 178.269 1.00 34.34  ? 1797 LEU A CD1   1 
ATOM   2069  C  CD2   . LEU A 1 1797 ? 227.488 255.356 180.697 1.00 29.13  ? 1797 LEU A CD2   1 
ATOM   2070  N  N     . MET A 1 1798 ? 222.995 258.372 180.609 1.00 35.08  ? 1798 MET A N     1 
ATOM   2071  C  CA    . MET A 1 1798 ? 222.323 259.649 180.766 1.00 37.17  ? 1798 MET A CA    1 
ATOM   2072  C  C     . MET A 1 1798 ? 221.278 259.563 181.878 1.00 38.05  ? 1798 MET A C     1 
ATOM   2073  O  O     . MET A 1 1798 ? 220.878 258.479 182.310 1.00 39.93  ? 1798 MET A O     1 
ATOM   2074  C  CB    . MET A 1 1798 ? 221.703 260.081 179.437 1.00 42.65  ? 1798 MET A CB    1 
ATOM   2075  C  CG    . MET A 1 1798 ? 220.601 259.173 178.936 1.00 43.71  ? 1798 MET A CG    1 
ATOM   2076  S  SD    . MET A 1 1798 ? 219.969 259.657 177.318 1.00 71.43  ? 1798 MET A SD    1 
ATOM   2077  C  CE    . MET A 1 1798 ? 221.323 259.155 176.259 1.00 39.59  ? 1798 MET A CE    1 
ATOM   2078  N  N     . GLU A 1 1799 ? 220.837 260.723 182.357 1.00 42.47  ? 1799 GLU A N     1 
ATOM   2079  C  CA    . GLU A 1 1799 ? 219.855 260.777 183.432 1.00 44.84  ? 1799 GLU A CA    1 
ATOM   2080  C  C     . GLU A 1 1799 ? 218.504 260.261 182.952 1.00 46.19  ? 1799 GLU A C     1 
ATOM   2081  O  O     . GLU A 1 1799 ? 218.057 260.572 181.843 1.00 43.80  ? 1799 GLU A O     1 
ATOM   2082  C  CB    . GLU A 1 1799 ? 219.722 262.205 183.964 1.00 57.32  ? 1799 GLU A CB    1 
ATOM   2083  C  CG    . GLU A 1 1799 ? 219.162 263.210 182.967 1.00 68.39  ? 1799 GLU A CG    1 
ATOM   2084  C  CD    . GLU A 1 1799 ? 219.110 264.619 183.523 1.00 75.78  ? 1799 GLU A CD    1 
ATOM   2085  O  OE1   . GLU A 1 1799 ? 219.533 264.817 184.682 1.00 81.71  ? 1799 GLU A OE1   1 
ATOM   2086  O  OE2   . GLU A 1 1799 ? 218.647 265.527 182.803 1.00 75.62  ? 1799 GLU A OE2   1 
ATOM   2087  N  N     . GLN A 1 1800 ? 217.864 259.451 183.790 1.00 39.66  ? 1800 GLN A N     1 
ATOM   2088  C  CA    . GLN A 1 1800 ? 216.604 258.805 183.459 1.00 39.31  ? 1800 GLN A CA    1 
ATOM   2089  C  C     . GLN A 1 1800 ? 215.654 258.903 184.642 1.00 35.35  ? 1800 GLN A C     1 
ATOM   2090  O  O     . GLN A 1 1800 ? 216.097 259.051 185.787 1.00 40.00  ? 1800 GLN A O     1 
ATOM   2091  C  CB    . GLN A 1 1800 ? 216.804 257.325 183.092 1.00 36.44  ? 1800 GLN A CB    1 
ATOM   2092  C  CG    . GLN A 1 1800 ? 217.877 257.062 182.050 1.00 27.33  ? 1800 GLN A CG    1 
ATOM   2093  C  CD    . GLN A 1 1800 ? 217.390 257.317 180.641 1.00 31.94  ? 1800 GLN A CD    1 
ATOM   2094  O  OE1   . GLN A 1 1800 ? 216.239 257.693 180.428 1.00 35.31  ? 1800 GLN A OE1   1 
ATOM   2095  N  NE2   . GLN A 1 1800 ? 218.262 257.097 179.667 1.00 35.59  ? 1800 GLN A NE2   1 
ATOM   2096  N  N     . PRO A 1 1801 ? 214.347 258.832 184.397 1.00 28.99  ? 1801 PRO A N     1 
ATOM   2097  C  CA    . PRO A 1 1801 ? 213.409 258.699 185.505 1.00 29.45  ? 1801 PRO A CA    1 
ATOM   2098  C  C     . PRO A 1 1801 ? 213.674 257.420 186.269 1.00 26.79  ? 1801 PRO A C     1 
ATOM   2099  O  O     . PRO A 1 1801 ? 214.104 256.406 185.686 1.00 30.52  ? 1801 PRO A O     1 
ATOM   2100  C  CB    . PRO A 1 1801 ? 212.041 258.670 184.808 1.00 32.54  ? 1801 PRO A CB    1 
ATOM   2101  C  CG    . PRO A 1 1801 ? 212.266 259.359 183.506 1.00 31.55  ? 1801 PRO A CG    1 
ATOM   2102  C  CD    . PRO A 1 1801 ? 213.663 259.007 183.105 1.00 25.53  ? 1801 PRO A CD    1 
ATOM   2103  N  N     . PRO A 1 1802 ? 213.449 257.421 187.587 1.00 28.26  ? 1802 PRO A N     1 
ATOM   2104  C  CA    . PRO A 1 1802 ? 213.803 256.234 188.387 1.00 29.87  ? 1802 PRO A CA    1 
ATOM   2105  C  C     . PRO A 1 1802 ? 213.133 254.954 187.919 1.00 24.90  ? 1802 PRO A C     1 
ATOM   2106  O  O     . PRO A 1 1802 ? 213.782 253.900 187.880 1.00 24.53  ? 1802 PRO A O     1 
ATOM   2107  C  CB    . PRO A 1 1802 ? 213.355 256.626 189.803 1.00 29.45  ? 1802 PRO A CB    1 
ATOM   2108  C  CG    . PRO A 1 1802 ? 213.308 258.118 189.794 1.00 29.45  ? 1802 PRO A CG    1 
ATOM   2109  C  CD    . PRO A 1 1802 ? 212.890 258.504 188.412 1.00 28.22  ? 1802 PRO A CD    1 
ATOM   2110  N  N     . LEU A 1 1803 ? 211.853 255.016 187.546 1.00 22.81  ? 1803 LEU A N     1 
ATOM   2111  C  CA    . LEU A 1 1803 ? 211.176 253.828 187.034 1.00 21.16  ? 1803 LEU A CA    1 
ATOM   2112  C  C     . LEU A 1 1803 ? 211.799 253.365 185.725 1.00 19.85  ? 1803 LEU A C     1 
ATOM   2113  O  O     . LEU A 1 1803 ? 212.047 252.166 185.535 1.00 21.98  ? 1803 LEU A O     1 
ATOM   2114  C  CB    . LEU A 1 1803 ? 209.688 254.113 186.848 1.00 27.10  ? 1803 LEU A CB    1 
ATOM   2115  C  CG    . LEU A 1 1803 ? 208.781 252.900 186.643 1.00 25.90  ? 1803 LEU A CG    1 
ATOM   2116  C  CD1   . LEU A 1 1803 ? 208.588 252.163 187.955 1.00 19.65  ? 1803 LEU A CD1   1 
ATOM   2117  C  CD2   . LEU A 1 1803 ? 207.444 253.318 186.056 1.00 19.62  ? 1803 LEU A CD2   1 
ATOM   2118  N  N     . ARG A 1 1804 ? 212.063 254.303 184.815 1.00 20.83  ? 1804 ARG A N     1 
ATOM   2119  C  CA    . ARG A 1 1804 ? 212.716 253.951 183.561 1.00 18.67  ? 1804 ARG A CA    1 
ATOM   2120  C  C     . ARG A 1 1804 ? 214.118 253.416 183.805 1.00 18.68  ? 1804 ARG A C     1 
ATOM   2121  O  O     . ARG A 1 1804 ? 214.563 252.496 183.112 1.00 19.10  ? 1804 ARG A O     1 
ATOM   2122  C  CB    . ARG A 1 1804 ? 212.755 255.160 182.628 1.00 21.84  ? 1804 ARG A CB    1 
ATOM   2123  C  CG    . ARG A 1 1804 ? 213.061 254.805 181.186 1.00 24.90  ? 1804 ARG A CG    1 
ATOM   2124  C  CD    . ARG A 1 1804 ? 213.481 256.026 180.391 1.00 29.43  ? 1804 ARG A CD    1 
ATOM   2125  N  NE    . ARG A 1 1804 ? 212.439 257.043 180.363 1.00 32.27  ? 1804 ARG A NE    1 
ATOM   2126  C  CZ    . ARG A 1 1804 ? 212.563 258.225 179.777 1.00 28.91  ? 1804 ARG A CZ    1 
ATOM   2127  N  NH1   . ARG A 1 1804 ? 213.676 258.575 179.156 1.00 31.98  ? 1804 ARG A NH1   1 
ATOM   2128  N  NH2   . ARG A 1 1804 ? 211.542 259.078 179.812 1.00 33.94  ? 1804 ARG A NH2   1 
ATOM   2129  N  N     . ARG A 1 1805 ? 214.832 253.978 184.783 1.00 20.59  ? 1805 ARG A N     1 
ATOM   2130  C  CA    . ARG A 1 1805 ? 216.165 253.475 185.098 1.00 20.37  ? 1805 ARG A CA    1 
ATOM   2131  C  C     . ARG A 1 1805 ? 216.110 252.038 185.599 1.00 19.56  ? 1805 ARG A C     1 
ATOM   2132  O  O     . ARG A 1 1805 ? 216.932 251.205 185.204 1.00 23.46  ? 1805 ARG A O     1 
ATOM   2133  C  CB    . ARG A 1 1805 ? 216.843 254.376 186.127 1.00 23.70  ? 1805 ARG A CB    1 
ATOM   2134  C  CG    . ARG A 1 1805 ? 218.286 253.997 186.403 1.00 25.13  ? 1805 ARG A CG    1 
ATOM   2135  C  CD    . ARG A 1 1805 ? 218.922 254.927 187.414 1.00 32.14  ? 1805 ARG A CD    1 
ATOM   2136  N  NE    . ARG A 1 1805 ? 219.015 256.288 186.898 1.00 50.03  ? 1805 ARG A NE    1 
ATOM   2137  C  CZ    . ARG A 1 1805 ? 219.998 256.732 186.129 1.00 44.11  ? 1805 ARG A CZ    1 
ATOM   2138  N  NH1   . ARG A 1 1805 ? 220.992 255.945 185.752 1.00 26.40  ? 1805 ARG A NH1   1 
ATOM   2139  N  NH2   . ARG A 1 1805 ? 219.982 257.998 185.723 1.00 46.59  ? 1805 ARG A NH2   1 
ATOM   2140  N  N     . ARG A 1 1806 ? 215.149 251.728 186.473 1.00 21.14  ? 1806 ARG A N     1 
ATOM   2141  C  CA    . ARG A 1 1806 ? 215.017 250.356 186.957 1.00 16.63  ? 1806 ARG A CA    1 
ATOM   2142  C  C     . ARG A 1 1806 ? 214.640 249.405 185.828 1.00 12.64  ? 1806 ARG A C     1 
ATOM   2143  O  O     . ARG A 1 1806 ? 215.153 248.280 185.757 1.00 15.67  ? 1806 ARG A O     1 
ATOM   2144  C  CB    . ARG A 1 1806 ? 213.992 250.295 188.086 1.00 16.53  ? 1806 ARG A CB    1 
ATOM   2145  C  CG    . ARG A 1 1806 ? 214.381 251.110 189.302 1.00 17.62  ? 1806 ARG A CG    1 
ATOM   2146  C  CD    . ARG A 1 1806 ? 213.374 250.951 190.418 1.00 19.26  ? 1806 ARG A CD    1 
ATOM   2147  N  NE    . ARG A 1 1806 ? 213.520 249.670 191.096 1.00 23.49  ? 1806 ARG A NE    1 
ATOM   2148  C  CZ    . ARG A 1 1806 ? 212.775 249.277 192.119 1.00 26.15  ? 1806 ARG A CZ    1 
ATOM   2149  N  NH1   . ARG A 1 1806 ? 211.814 250.044 192.608 1.00 23.21  ? 1806 ARG A NH1   1 
ATOM   2150  N  NH2   . ARG A 1 1806 ? 213.000 248.086 192.667 1.00 23.59  ? 1806 ARG A NH2   1 
ATOM   2151  N  N     . LYS A 1 1807 ? 213.747 249.839 184.934 1.00 15.36  ? 1807 LYS A N     1 
ATOM   2152  C  CA    . LYS A 1 1807 ? 213.409 249.020 183.774 1.00 11.97  ? 1807 LYS A CA    1 
ATOM   2153  C  C     . LYS A 1 1807 ? 214.636 248.768 182.905 1.00 12.38  ? 1807 LYS A C     1 
ATOM   2154  O  O     . LYS A 1 1807 ? 214.850 247.647 182.427 1.00 17.05  ? 1807 LYS A O     1 
ATOM   2155  C  CB    . LYS A 1 1807 ? 212.306 249.690 182.958 1.00 11.92  ? 1807 LYS A CB    1 
ATOM   2156  C  CG    . LYS A 1 1807 ? 210.969 249.779 183.664 1.00 13.42  ? 1807 LYS A CG    1 
ATOM   2157  C  CD    . LYS A 1 1807 ? 209.915 250.389 182.758 1.00 12.43  ? 1807 LYS A CD    1 
ATOM   2158  C  CE    . LYS A 1 1807 ? 208.584 250.524 183.471 1.00 16.92  ? 1807 LYS A CE    1 
ATOM   2159  N  NZ    . LYS A 1 1807 ? 207.536 251.073 182.572 1.00 22.34  ? 1807 LYS A NZ    1 
ATOM   2160  N  N     . LEU A 1 1808 ? 215.452 249.802 182.691 1.00 13.10  ? 1808 LEU A N     1 
ATOM   2161  C  CA    . LEU A 1 1808 ? 216.670 249.644 181.904 1.00 13.44  ? 1808 LEU A CA    1 
ATOM   2162  C  C     . LEU A 1 1808 ? 217.636 248.676 182.571 1.00 12.16  ? 1808 LEU A C     1 
ATOM   2163  O  O     . LEU A 1 1808 ? 218.280 247.871 181.892 1.00 15.72  ? 1808 LEU A O     1 
ATOM   2164  C  CB    . LEU A 1 1808 ? 217.342 251.001 181.687 1.00 17.63  ? 1808 LEU A CB    1 
ATOM   2165  C  CG    . LEU A 1 1808 ? 216.651 252.021 180.779 1.00 15.14  ? 1808 LEU A CG    1 
ATOM   2166  C  CD1   . LEU A 1 1808 ? 217.203 253.412 181.030 1.00 15.36  ? 1808 LEU A CD1   1 
ATOM   2167  C  CD2   . LEU A 1 1808 ? 216.813 251.643 179.319 1.00 17.70  ? 1808 LEU A CD2   1 
ATOM   2168  N  N     . GLU A 1 1809 ? 217.764 248.748 183.897 1.00 10.37  ? 1809 GLU A N     1 
ATOM   2169  C  CA    . GLU A 1 1809 ? 218.644 247.819 184.604 1.00 9.49   ? 1809 GLU A CA    1 
ATOM   2170  C  C     . GLU A 1 1809 ? 218.163 246.379 184.461 1.00 11.73  ? 1809 GLU A C     1 
ATOM   2171  O  O     . GLU A 1 1809 ? 218.965 245.468 184.210 1.00 11.94  ? 1809 GLU A O     1 
ATOM   2172  C  CB    . GLU A 1 1809 ? 218.743 248.203 186.079 1.00 11.85  ? 1809 GLU A CB    1 
ATOM   2173  C  CG    . GLU A 1 1809 ? 219.337 249.574 186.327 1.00 17.72  ? 1809 GLU A CG    1 
ATOM   2174  C  CD    . GLU A 1 1809 ? 219.433 249.905 187.801 1.00 34.00  ? 1809 GLU A CD    1 
ATOM   2175  O  OE1   . GLU A 1 1809 ? 218.378 250.119 188.433 1.00 35.15  ? 1809 GLU A OE1   1 
ATOM   2176  O  OE2   . GLU A 1 1809 ? 220.562 249.947 188.328 1.00 38.34  ? 1809 GLU A OE2   1 
ATOM   2177  N  N     . HIS A 1 1810 ? 216.854 246.153 184.620 1.00 10.53  ? 1810 HIS A N     1 
ATOM   2178  C  CA    . HIS A 1 1810 ? 216.323 244.803 184.455 1.00 8.55   ? 1810 HIS A CA    1 
ATOM   2179  C  C     . HIS A 1 1810 ? 216.551 244.293 183.038 1.00 10.03  ? 1810 HIS A C     1 
ATOM   2180  O  O     . HIS A 1 1810 ? 216.939 243.134 182.838 1.00 11.56  ? 1810 HIS A O     1 
ATOM   2181  C  CB    . HIS A 1 1810 ? 214.833 244.764 184.797 1.00 9.06   ? 1810 HIS A CB    1 
ATOM   2182  C  CG    . HIS A 1 1810 ? 214.515 245.207 186.189 1.00 11.09  ? 1810 HIS A CG    1 
ATOM   2183  N  ND1   . HIS A 1 1810 ? 215.289 244.859 187.276 1.00 16.58  ? 1810 HIS A ND1   1 
ATOM   2184  C  CD2   . HIS A 1 1810 ? 213.487 245.938 186.679 1.00 12.51  ? 1810 HIS A CD2   1 
ATOM   2185  C  CE1   . HIS A 1 1810 ? 214.764 245.378 188.372 1.00 14.61  ? 1810 HIS A CE1   1 
ATOM   2186  N  NE2   . HIS A 1 1810 ? 213.669 246.036 188.038 1.00 14.89  ? 1810 HIS A NE2   1 
ATOM   2187  N  N     . LEU A 1 1811 ? 216.319 245.151 182.041 1.00 9.86   ? 1811 LEU A N     1 
ATOM   2188  C  CA    . LEU A 1 1811 ? 216.528 244.746 180.657 1.00 8.77   ? 1811 LEU A CA    1 
ATOM   2189  C  C     . LEU A 1 1811 ? 217.997 244.452 180.384 1.00 9.15   ? 1811 LEU A C     1 
ATOM   2190  O  O     . LEU A 1 1811 ? 218.322 243.500 179.666 1.00 10.63  ? 1811 LEU A O     1 
ATOM   2191  C  CB    . LEU A 1 1811 ? 216.008 245.828 179.713 1.00 8.13   ? 1811 LEU A CB    1 
ATOM   2192  C  CG    . LEU A 1 1811 ? 214.558 245.649 179.260 1.00 8.36   ? 1811 LEU A CG    1 
ATOM   2193  C  CD1   . LEU A 1 1811 ? 214.143 246.769 178.325 1.00 14.18  ? 1811 LEU A CD1   1 
ATOM   2194  C  CD2   . LEU A 1 1811 ? 214.370 244.296 178.601 1.00 8.40   ? 1811 LEU A CD2   1 
ATOM   2195  N  N     . ILE A 1 1812 ? 218.899 245.257 180.949 1.00 8.34   ? 1812 ILE A N     1 
ATOM   2196  C  CA    . ILE A 1 1812 ? 220.328 245.022 180.771 1.00 9.27   ? 1812 ILE A CA    1 
ATOM   2197  C  C     . ILE A 1 1812 ? 220.717 243.674 181.351 1.00 7.59   ? 1812 ILE A C     1 
ATOM   2198  O  O     . ILE A 1 1812 ? 221.439 242.895 180.717 1.00 8.60   ? 1812 ILE A O     1 
ATOM   2199  C  CB    . ILE A 1 1812 ? 221.143 246.166 181.404 1.00 10.61  ? 1812 ILE A CB    1 
ATOM   2200  C  CG1   . ILE A 1 1812 ? 221.120 247.401 180.506 1.00 7.40   ? 1812 ILE A CG1   1 
ATOM   2201  C  CG2   . ILE A 1 1812 ? 222.577 245.730 181.658 1.00 10.11  ? 1812 ILE A CG2   1 
ATOM   2202  C  CD1   . ILE A 1 1812 ? 221.868 248.579 181.073 1.00 9.82   ? 1812 ILE A CD1   1 
ATOM   2203  N  N     . THR A 1 1813 ? 220.238 243.369 182.558 1.00 9.84   ? 1813 THR A N     1 
ATOM   2204  C  CA    . THR A 1 1813 ? 220.552 242.083 183.174 1.00 6.07   ? 1813 THR A CA    1 
ATOM   2205  C  C     . THR A 1 1813 ? 220.035 240.926 182.324 1.00 6.13   ? 1813 THR A C     1 
ATOM   2206  O  O     . THR A 1 1813 ? 220.770 239.966 182.035 1.00 8.07   ? 1813 THR A O     1 
ATOM   2207  C  CB    . THR A 1 1813 ? 219.959 242.023 184.583 1.00 6.12   ? 1813 THR A CB    1 
ATOM   2208  O  OG1   . THR A 1 1813 ? 220.369 243.179 185.322 1.00 9.14   ? 1813 THR A OG1   1 
ATOM   2209  C  CG2   . THR A 1 1813 ? 220.430 240.777 185.308 1.00 7.22   ? 1813 THR A CG2   1 
ATOM   2210  N  N     . GLU A 1 1814 ? 218.774 241.014 181.892 1.00 6.13   ? 1814 GLU A N     1 
ATOM   2211  C  CA    . GLU A 1 1814 ? 218.186 239.923 181.123 1.00 8.16   ? 1814 GLU A CA    1 
ATOM   2212  C  C     . GLU A 1 1814 ? 218.904 239.721 179.794 1.00 8.81   ? 1814 GLU A C     1 
ATOM   2213  O  O     . GLU A 1 1814 ? 219.175 238.585 179.395 1.00 9.69   ? 1814 GLU A O     1 
ATOM   2214  C  CB    . GLU A 1 1814 ? 216.698 240.178 180.892 1.00 10.37  ? 1814 GLU A CB    1 
ATOM   2215  C  CG    . GLU A 1 1814 ? 215.942 238.985 180.314 1.00 10.65  ? 1814 GLU A CG    1 
ATOM   2216  C  CD    . GLU A 1 1814 ? 216.397 237.640 180.872 1.00 20.09  ? 1814 GLU A CD    1 
ATOM   2217  O  OE1   . GLU A 1 1814 ? 216.593 237.521 182.100 1.00 18.76  ? 1814 GLU A OE1   1 
ATOM   2218  O  OE2   . GLU A 1 1814 ? 216.570 236.696 180.071 1.00 16.16  ? 1814 GLU A OE2   1 
ATOM   2219  N  N     . LEU A 1 1815 ? 219.228 240.809 179.094 1.00 7.19   ? 1815 LEU A N     1 
ATOM   2220  C  CA    . LEU A 1 1815 ? 219.882 240.659 177.801 1.00 6.73   ? 1815 LEU A CA    1 
ATOM   2221  C  C     . LEU A 1 1815 ? 221.349 240.275 177.938 1.00 7.74   ? 1815 LEU A C     1 
ATOM   2222  O  O     . LEU A 1 1815 ? 221.902 239.656 177.028 1.00 11.57  ? 1815 LEU A O     1 
ATOM   2223  C  CB    . LEU A 1 1815 ? 219.725 241.928 176.966 1.00 7.58   ? 1815 LEU A CB    1 
ATOM   2224  C  CG    . LEU A 1 1815 ? 218.415 242.046 176.179 1.00 6.56   ? 1815 LEU A CG    1 
ATOM   2225  C  CD1   . LEU A 1 1815 ? 217.179 242.105 177.062 1.00 10.35  ? 1815 LEU A CD1   1 
ATOM   2226  C  CD2   . LEU A 1 1815 ? 218.473 243.251 175.273 1.00 14.35  ? 1815 LEU A CD2   1 
ATOM   2227  N  N     . VAL A 1 1816 ? 221.993 240.605 179.059 1.00 5.82   ? 1816 VAL A N     1 
ATOM   2228  C  CA    . VAL A 1 1816 ? 223.328 240.069 179.311 1.00 6.43   ? 1816 VAL A CA    1 
ATOM   2229  C  C     . VAL A 1 1816 ? 223.260 238.557 179.476 1.00 7.80   ? 1816 VAL A C     1 
ATOM   2230  O  O     . VAL A 1 1816 ? 224.090 237.814 178.929 1.00 10.56  ? 1816 VAL A O     1 
ATOM   2231  C  CB    . VAL A 1 1816 ? 223.960 240.752 180.539 1.00 6.14   ? 1816 VAL A CB    1 
ATOM   2232  C  CG1   . VAL A 1 1816 ? 225.063 239.890 181.125 1.00 6.49   ? 1816 VAL A CG1   1 
ATOM   2233  C  CG2   . VAL A 1 1816 ? 224.505 242.117 180.157 1.00 8.50   ? 1816 VAL A CG2   1 
ATOM   2234  N  N     . HIS A 1 1817 ? 222.259 238.073 180.217 1.00 7.62   ? 1817 HIS A N     1 
ATOM   2235  C  CA    . HIS A 1 1817 ? 222.070 236.629 180.329 1.00 6.61   ? 1817 HIS A CA    1 
ATOM   2236  C  C     . HIS A 1 1817 ? 221.784 236.005 178.966 1.00 9.23   ? 1817 HIS A C     1 
ATOM   2237  O  O     . HIS A 1 1817 ? 222.305 234.929 178.643 1.00 11.83  ? 1817 HIS A O     1 
ATOM   2238  C  CB    . HIS A 1 1817 ? 220.943 236.317 181.311 1.00 7.73   ? 1817 HIS A CB    1 
ATOM   2239  C  CG    . HIS A 1 1817 ? 220.595 234.864 181.385 1.00 7.17   ? 1817 HIS A CG    1 
ATOM   2240  N  ND1   . HIS A 1 1817 ? 221.517 233.895 181.718 1.00 7.20   ? 1817 HIS A ND1   1 
ATOM   2241  C  CD2   . HIS A 1 1817 ? 219.429 234.213 181.167 1.00 6.18   ? 1817 HIS A CD2   1 
ATOM   2242  C  CE1   . HIS A 1 1817 ? 220.934 232.710 181.702 1.00 6.53   ? 1817 HIS A CE1   1 
ATOM   2243  N  NE2   . HIS A 1 1817 ? 219.666 232.875 181.371 1.00 5.49   ? 1817 HIS A NE2   1 
ATOM   2244  N  N     . GLN A 1 1818 ? 220.956 236.668 178.156 1.00 8.80   ? 1818 GLN A N     1 
ATOM   2245  C  CA    . GLN A 1 1818 ? 220.651 236.164 176.819 1.00 6.86   ? 1818 GLN A CA    1 
ATOM   2246  C  C     . GLN A 1 1818 ? 221.900 236.106 175.950 1.00 9.15   ? 1818 GLN A C     1 
ATOM   2247  O  O     . GLN A 1 1818 ? 222.094 235.149 175.192 1.00 10.89  ? 1818 GLN A O     1 
ATOM   2248  C  CB    . GLN A 1 1818 ? 219.588 237.039 176.157 1.00 5.99   ? 1818 GLN A CB    1 
ATOM   2249  C  CG    . GLN A 1 1818 ? 218.215 236.945 176.788 1.00 6.86   ? 1818 GLN A CG    1 
ATOM   2250  C  CD    . GLN A 1 1818 ? 217.236 237.933 176.191 1.00 6.91   ? 1818 GLN A CD    1 
ATOM   2251  O  OE1   . GLN A 1 1818 ? 217.581 238.698 175.290 1.00 6.33   ? 1818 GLN A OE1   1 
ATOM   2252  N  NE2   . GLN A 1 1818 ? 216.007 237.922 176.688 1.00 8.71   ? 1818 GLN A NE2   1 
ATOM   2253  N  N     . ARG A 1 1819 ? 222.751 237.130 176.034 1.00 11.31  ? 1819 ARG A N     1 
ATOM   2254  C  CA    . ARG A 1 1819 ? 223.996 237.139 175.277 1.00 13.77  ? 1819 ARG A CA    1 
ATOM   2255  C  C     . ARG A 1 1819 ? 224.905 235.995 175.704 1.00 13.49  ? 1819 ARG A C     1 
ATOM   2256  O  O     . ARG A 1 1819 ? 225.513 235.328 174.859 1.00 16.49  ? 1819 ARG A O     1 
ATOM   2257  C  CB    . ARG A 1 1819 ? 224.703 238.481 175.458 1.00 12.71  ? 1819 ARG A CB    1 
ATOM   2258  C  CG    . ARG A 1 1819 ? 225.994 238.625 174.675 1.00 15.67  ? 1819 ARG A CG    1 
ATOM   2259  C  CD    . ARG A 1 1819 ? 226.836 239.753 175.238 1.00 18.03  ? 1819 ARG A CD    1 
ATOM   2260  N  NE    . ARG A 1 1819 ? 227.212 239.504 176.624 1.00 17.87  ? 1819 ARG A NE    1 
ATOM   2261  C  CZ    . ARG A 1 1819 ? 227.605 240.442 177.474 1.00 20.74  ? 1819 ARG A CZ    1 
ATOM   2262  N  NH1   . ARG A 1 1819 ? 227.687 241.712 177.112 1.00 20.68  ? 1819 ARG A NH1   1 
ATOM   2263  N  NH2   . ARG A 1 1819 ? 227.923 240.097 178.719 1.00 24.15  ? 1819 ARG A NH2   1 
ATOM   2264  N  N     . ASP A 1 1820 ? 225.010 235.755 177.013 1.00 12.93  ? 1820 ASP A N     1 
ATOM   2265  C  CA    . ASP A 1 1820 ? 225.829 234.643 177.490 1.00 13.30  ? 1820 ASP A CA    1 
ATOM   2266  C  C     . ASP A 1 1820 ? 225.290 233.305 176.991 1.00 13.11  ? 1820 ASP A C     1 
ATOM   2267  O  O     . ASP A 1 1820 ? 226.059 232.443 176.546 1.00 13.78  ? 1820 ASP A O     1 
ATOM   2268  C  CB    . ASP A 1 1820 ? 225.898 234.662 179.017 1.00 14.95  ? 1820 ASP A CB    1 
ATOM   2269  C  CG    . ASP A 1 1820 ? 226.718 235.823 179.549 1.00 28.14  ? 1820 ASP A CG    1 
ATOM   2270  O  OD1   . ASP A 1 1820 ? 227.295 236.570 178.731 1.00 26.85  ? 1820 ASP A OD1   1 
ATOM   2271  O  OD2   . ASP A 1 1820 ? 226.781 235.993 180.785 1.00 24.36  ? 1820 ASP A OD2   1 
ATOM   2272  N  N     . VAL A 1 1821 ? 223.969 233.122 177.044 1.00 15.20  ? 1821 VAL A N     1 
ATOM   2273  C  CA    . VAL A 1 1821 ? 223.377 231.865 176.589 1.00 12.21  ? 1821 VAL A CA    1 
ATOM   2274  C  C     . VAL A 1 1821 ? 223.589 231.681 175.091 1.00 12.37  ? 1821 VAL A C     1 
ATOM   2275  O  O     . VAL A 1 1821 ? 223.898 230.577 174.626 1.00 18.96  ? 1821 VAL A O     1 
ATOM   2276  C  CB    . VAL A 1 1821 ? 221.885 231.809 176.963 1.00 7.74   ? 1821 VAL A CB    1 
ATOM   2277  C  CG1   . VAL A 1 1821 ? 221.218 230.616 176.303 1.00 9.53   ? 1821 VAL A CG1   1 
ATOM   2278  C  CG2   . VAL A 1 1821 ? 221.722 231.737 178.467 1.00 6.89   ? 1821 VAL A CG2   1 
ATOM   2279  N  N     . THR A 1 1822 ? 223.415 232.749 174.311 1.00 10.79  ? 1822 THR A N     1 
ATOM   2280  C  CA    . THR A 1 1822 ? 223.611 232.653 172.869 1.00 12.88  ? 1822 THR A CA    1 
ATOM   2281  C  C     . THR A 1 1822 ? 225.065 232.354 172.529 1.00 18.18  ? 1822 THR A C     1 
ATOM   2282  O  O     . THR A 1 1822 ? 225.346 231.571 171.614 1.00 19.38  ? 1822 THR A O     1 
ATOM   2283  C  CB    . THR A 1 1822 ? 223.153 233.944 172.192 1.00 14.26  ? 1822 THR A CB    1 
ATOM   2284  O  OG1   . THR A 1 1822 ? 221.764 234.157 172.468 1.00 18.59  ? 1822 THR A OG1   1 
ATOM   2285  C  CG2   . THR A 1 1822 ? 223.339 233.848 170.691 1.00 16.69  ? 1822 THR A CG2   1 
ATOM   2286  N  N     . ARG A 1 1823 ? 226.005 232.966 173.254 1.00 17.03  ? 1823 ARG A N     1 
ATOM   2287  C  CA    . ARG A 1 1823 ? 227.415 232.663 173.039 1.00 16.61  ? 1823 ARG A CA    1 
ATOM   2288  C  C     . ARG A 1 1823 ? 227.722 231.209 173.370 1.00 20.03  ? 1823 ARG A C     1 
ATOM   2289  O  O     . ARG A 1 1823 ? 228.487 230.551 172.656 1.00 20.80  ? 1823 ARG A O     1 
ATOM   2290  C  CB    . ARG A 1 1823 ? 228.286 233.600 173.875 1.00 16.22  ? 1823 ARG A CB    1 
ATOM   2291  C  CG    . ARG A 1 1823 ? 228.494 234.969 173.256 1.00 15.83  ? 1823 ARG A CG    1 
ATOM   2292  C  CD    . ARG A 1 1823 ? 229.235 235.895 174.204 1.00 13.72  ? 1823 ARG A CD    1 
ATOM   2293  N  NE    . ARG A 1 1823 ? 229.441 237.218 173.626 1.00 17.00  ? 1823 ARG A NE    1 
ATOM   2294  C  CZ    . ARG A 1 1823 ? 229.818 238.285 174.316 1.00 24.05  ? 1823 ARG A CZ    1 
ATOM   2295  N  NH1   . ARG A 1 1823 ? 230.043 238.222 175.618 1.00 26.64  ? 1823 ARG A NH1   1 
ATOM   2296  N  NH2   . ARG A 1 1823 ? 229.972 239.445 173.685 1.00 21.50  ? 1823 ARG A NH2   1 
ATOM   2297  N  N     . SER A 1 1824 ? 227.141 230.691 174.455 1.00 19.72  ? 1824 SER A N     1 
ATOM   2298  C  CA    . SER A 1 1824 ? 227.339 229.284 174.793 1.00 17.64  ? 1824 SER A CA    1 
ATOM   2299  C  C     . SER A 1 1824 ? 226.767 228.370 173.716 1.00 20.79  ? 1824 SER A C     1 
ATOM   2300  O  O     . SER A 1 1824 ? 227.376 227.354 173.364 1.00 26.03  ? 1824 SER A O     1 
ATOM   2301  C  CB    . SER A 1 1824 ? 226.711 228.972 176.151 1.00 20.21  ? 1824 SER A CB    1 
ATOM   2302  O  OG    . SER A 1 1824 ? 227.354 229.692 177.188 1.00 36.05  ? 1824 SER A OG    1 
ATOM   2303  N  N     . LEU A 1 1825 ? 225.589 228.711 173.189 1.00 18.30  ? 1825 LEU A N     1 
ATOM   2304  C  CA    . LEU A 1 1825 ? 224.999 227.912 172.119 1.00 21.01  ? 1825 LEU A CA    1 
ATOM   2305  C  C     . LEU A 1 1825 ? 225.864 227.936 170.866 1.00 21.13  ? 1825 LEU A C     1 
ATOM   2306  O  O     . LEU A 1 1825 ? 226.055 226.904 170.213 1.00 26.21  ? 1825 LEU A O     1 
ATOM   2307  C  CB    . LEU A 1 1825 ? 223.589 228.413 171.804 1.00 18.27  ? 1825 LEU A CB    1 
ATOM   2308  C  CG    . LEU A 1 1825 ? 222.471 228.044 172.781 1.00 17.10  ? 1825 LEU A CG    1 
ATOM   2309  C  CD1   . LEU A 1 1825 ? 221.118 228.219 172.118 1.00 13.42  ? 1825 LEU A CD1   1 
ATOM   2310  C  CD2   . LEU A 1 1825 ? 222.636 226.622 173.284 1.00 18.61  ? 1825 LEU A CD2   1 
ATOM   2311  N  N     . ILE A 1 1826 ? 226.389 229.110 170.509 1.00 21.95  ? 1826 ILE A N     1 
ATOM   2312  C  CA    . ILE A 1 1826 ? 227.215 229.227 169.311 1.00 19.81  ? 1826 ILE A CA    1 
ATOM   2313  C  C     . ILE A 1 1826 ? 228.517 228.454 169.477 1.00 22.40  ? 1826 ILE A C     1 
ATOM   2314  O  O     . ILE A 1 1826 ? 228.951 227.739 168.564 1.00 26.53  ? 1826 ILE A O     1 
ATOM   2315  C  CB    . ILE A 1 1826 ? 227.471 230.710 168.985 1.00 15.96  ? 1826 ILE A CB    1 
ATOM   2316  C  CG1   . ILE A 1 1826 ? 226.219 231.342 168.376 1.00 19.35  ? 1826 ILE A CG1   1 
ATOM   2317  C  CG2   . ILE A 1 1826 ? 228.659 230.857 168.054 1.00 20.12  ? 1826 ILE A CG2   1 
ATOM   2318  C  CD1   . ILE A 1 1826 ? 226.347 232.821 168.111 1.00 19.65  ? 1826 ILE A CD1   1 
ATOM   2319  N  N     . LYS A 1 1827 ? 229.156 228.577 170.642 1.00 22.50  ? 1827 LYS A N     1 
ATOM   2320  C  CA    . LYS A 1 1827 ? 230.416 227.878 170.876 1.00 21.63  ? 1827 LYS A CA    1 
ATOM   2321  C  C     . LYS A 1 1827 ? 230.226 226.368 170.827 1.00 33.50  ? 1827 LYS A C     1 
ATOM   2322  O  O     . LYS A 1 1827 ? 231.078 225.643 170.300 1.00 40.17  ? 1827 LYS A O     1 
ATOM   2323  C  CB    . LYS A 1 1827 ? 231.005 228.304 172.219 1.00 25.67  ? 1827 LYS A CB    1 
ATOM   2324  C  CG    . LYS A 1 1827 ? 232.335 227.656 172.550 1.00 33.69  ? 1827 LYS A CG    1 
ATOM   2325  C  CD    . LYS A 1 1827 ? 232.847 228.111 173.904 1.00 29.15  ? 1827 LYS A CD    1 
ATOM   2326  C  CE    . LYS A 1 1827 ? 234.295 227.702 174.105 1.00 31.47  ? 1827 LYS A CE    1 
ATOM   2327  N  NZ    . LYS A 1 1827 ? 235.177 228.264 173.044 1.00 27.47  ? 1827 LYS A NZ    1 
ATOM   2328  N  N     . SER A 1 1828 ? 229.112 225.876 171.363 1.00 33.79  ? 1828 SER A N     1 
ATOM   2329  C  CA    . SER A 1 1828 ? 228.817 224.450 171.381 1.00 28.97  ? 1828 SER A CA    1 
ATOM   2330  C  C     . SER A 1 1828 ? 228.358 223.920 170.029 1.00 30.39  ? 1828 SER A C     1 
ATOM   2331  O  O     . SER A 1 1828 ? 228.167 222.706 169.896 1.00 40.13  ? 1828 SER A O     1 
ATOM   2332  C  CB    . SER A 1 1828 ? 227.752 224.151 172.439 1.00 36.76  ? 1828 SER A CB    1 
ATOM   2333  O  OG    . SER A 1 1828 ? 227.422 222.774 172.456 1.00 51.52  ? 1828 SER A OG    1 
ATOM   2334  N  N     . LYS A 1 1829 ? 228.173 224.792 169.036 1.00 30.29  ? 1829 LYS A N     1 
ATOM   2335  C  CA    . LYS A 1 1829 ? 227.728 224.397 167.699 1.00 35.02  ? 1829 LYS A CA    1 
ATOM   2336  C  C     . LYS A 1 1829 ? 226.399 223.647 167.753 1.00 44.14  ? 1829 LYS A C     1 
ATOM   2337  O  O     . LYS A 1 1829 ? 226.217 222.613 167.108 1.00 47.97  ? 1829 LYS A O     1 
ATOM   2338  C  CB    . LYS A 1 1829 ? 228.795 223.566 166.982 1.00 38.37  ? 1829 LYS A CB    1 
ATOM   2339  C  CG    . LYS A 1 1829 ? 230.102 224.303 166.753 1.00 38.38  ? 1829 LYS A CG    1 
ATOM   2340  C  CD    . LYS A 1 1829 ? 231.266 223.336 166.644 1.00 45.38  ? 1829 LYS A CD    1 
ATOM   2341  C  CE    . LYS A 1 1829 ? 231.742 222.895 168.020 1.00 41.89  ? 1829 LYS A CE    1 
ATOM   2342  N  NZ    . LYS A 1 1829 ? 232.559 223.943 168.689 1.00 38.17  ? 1829 LYS A NZ    1 
ATOM   2343  N  N     . ILE A 1 1830 ? 225.461 224.176 168.533 1.00 41.42  ? 1830 ILE A N     1 
ATOM   2344  C  CA    . ILE A 1 1830 ? 224.134 223.582 168.653 1.00 40.78  ? 1830 ILE A CA    1 
ATOM   2345  C  C     . ILE A 1 1830 ? 223.314 223.971 167.431 1.00 42.91  ? 1830 ILE A C     1 
ATOM   2346  O  O     . ILE A 1 1830 ? 223.065 225.157 167.188 1.00 49.60  ? 1830 ILE A O     1 
ATOM   2347  C  CB    . ILE A 1 1830 ? 223.444 224.030 169.948 1.00 31.87  ? 1830 ILE A CB    1 
ATOM   2348  C  CG1   . ILE A 1 1830 ? 224.281 223.622 171.160 1.00 33.62  ? 1830 ILE A CG1   1 
ATOM   2349  C  CG2   . ILE A 1 1830 ? 222.045 223.449 170.036 1.00 34.87  ? 1830 ILE A CG2   1 
ATOM   2350  C  CD1   . ILE A 1 1830 ? 224.478 222.129 171.279 1.00 35.22  ? 1830 ILE A CD1   1 
ATOM   2351  N  N     . ASP A 1 1831 ? 222.886 222.972 166.661 1.00 36.30  ? 1831 ASP A N     1 
ATOM   2352  C  CA    . ASP A 1 1831 ? 222.095 223.204 165.463 1.00 42.83  ? 1831 ASP A CA    1 
ATOM   2353  C  C     . ASP A 1 1831 ? 220.704 222.595 165.539 1.00 44.07  ? 1831 ASP A C     1 
ATOM   2354  O  O     . ASP A 1 1831 ? 219.927 222.745 164.589 1.00 50.17  ? 1831 ASP A O     1 
ATOM   2355  C  CB    . ASP A 1 1831 ? 222.826 222.658 164.229 1.00 51.13  ? 1831 ASP A CB    1 
ATOM   2356  C  CG    . ASP A 1 1831 ? 223.227 221.207 164.384 1.00 53.77  ? 1831 ASP A CG    1 
ATOM   2357  O  OD1   . ASP A 1 1831 ? 223.330 220.739 165.537 1.00 57.10  ? 1831 ASP A OD1   1 
ATOM   2358  O  OD2   . ASP A 1 1831 ? 223.437 220.535 163.354 1.00 57.60  ? 1831 ASP A OD2   1 
ATOM   2359  N  N     . ASN A 1 1832 ? 220.364 221.922 166.632 1.00 38.31  ? 1832 ASN A N     1 
ATOM   2360  C  CA    . ASN A 1 1832 ? 219.066 221.287 166.800 1.00 32.87  ? 1832 ASN A CA    1 
ATOM   2361  C  C     . ASN A 1 1832 ? 218.318 221.967 167.938 1.00 27.78  ? 1832 ASN A C     1 
ATOM   2362  O  O     . ASN A 1 1832 ? 218.884 222.187 169.014 1.00 30.02  ? 1832 ASN A O     1 
ATOM   2363  C  CB    . ASN A 1 1832 ? 219.225 219.791 167.084 1.00 29.96  ? 1832 ASN A CB    1 
ATOM   2364  C  CG    . ASN A 1 1832 ? 217.895 219.087 167.271 1.00 27.66  ? 1832 ASN A CG    1 
ATOM   2365  O  OD1   . ASN A 1 1832 ? 216.856 219.567 166.819 1.00 28.01  ? 1832 ASN A OD1   1 
ATOM   2366  N  ND2   . ASN A 1 1832 ? 217.924 217.942 167.941 1.00 27.68  ? 1832 ASN A ND2   1 
ATOM   2367  N  N     . ALA A 1 1833 ? 217.050 222.301 167.695 1.00 22.99  ? 1833 ALA A N     1 
ATOM   2368  C  CA    . ALA A 1 1833 ? 216.227 222.898 168.738 1.00 18.20  ? 1833 ALA A CA    1 
ATOM   2369  C  C     . ALA A 1 1833 ? 215.889 221.909 169.844 1.00 22.29  ? 1833 ALA A C     1 
ATOM   2370  O  O     . ALA A 1 1833 ? 215.468 222.328 170.926 1.00 26.91  ? 1833 ALA A O     1 
ATOM   2371  C  CB    . ALA A 1 1833 ? 214.942 223.466 168.138 1.00 24.63  ? 1833 ALA A CB    1 
ATOM   2372  N  N     . LYS A 1 1834 ? 216.059 220.612 169.598 1.00 24.72  ? 1834 LYS A N     1 
ATOM   2373  C  CA    . LYS A 1 1834 ? 215.810 219.584 170.599 1.00 19.70  ? 1834 LYS A CA    1 
ATOM   2374  C  C     . LYS A 1 1834 ? 217.065 219.181 171.361 1.00 21.48  ? 1834 LYS A C     1 
ATOM   2375  O  O     . LYS A 1 1834 ? 217.002 218.260 172.180 1.00 22.53  ? 1834 LYS A O     1 
ATOM   2376  C  CB    . LYS A 1 1834 ? 215.185 218.349 169.945 1.00 24.35  ? 1834 LYS A CB    1 
ATOM   2377  C  CG    . LYS A 1 1834 ? 213.829 218.605 169.311 1.00 26.86  ? 1834 LYS A CG    1 
ATOM   2378  C  CD    . LYS A 1 1834 ? 212.800 219.000 170.356 1.00 28.99  ? 1834 LYS A CD    1 
ATOM   2379  C  CE    . LYS A 1 1834 ? 212.431 217.823 171.242 1.00 35.79  ? 1834 LYS A CE    1 
ATOM   2380  N  NZ    . LYS A 1 1834 ? 211.369 218.179 172.222 1.00 30.06  ? 1834 LYS A NZ    1 
ATOM   2381  N  N     . SER A 1 1835 ? 218.195 219.837 171.111 1.00 19.67  ? 1835 SER A N     1 
ATOM   2382  C  CA    . SER A 1 1835 ? 219.405 219.555 171.868 1.00 19.02  ? 1835 SER A CA    1 
ATOM   2383  C  C     . SER A 1 1835 ? 219.261 220.050 173.301 1.00 19.36  ? 1835 SER A C     1 
ATOM   2384  O  O     . SER A 1 1835 ? 218.708 221.125 173.548 1.00 27.04  ? 1835 SER A O     1 
ATOM   2385  C  CB    . SER A 1 1835 ? 220.614 220.212 171.205 1.00 25.01  ? 1835 SER A CB    1 
ATOM   2386  O  OG    . SER A 1 1835 ? 221.751 220.154 172.047 1.00 31.05  ? 1835 SER A OG    1 
ATOM   2387  N  N     . PHE A 1 1836 ? 219.771 219.263 174.250 1.00 19.91  ? 1836 PHE A N     1 
ATOM   2388  C  CA    . PHE A 1 1836 ? 219.604 219.600 175.659 1.00 14.88  ? 1836 PHE A CA    1 
ATOM   2389  C  C     . PHE A 1 1836 ? 220.310 220.889 176.048 1.00 12.10  ? 1836 PHE A C     1 
ATOM   2390  O  O     . PHE A 1 1836 ? 219.952 221.488 177.068 1.00 12.61  ? 1836 PHE A O     1 
ATOM   2391  C  CB    . PHE A 1 1836 ? 220.095 218.458 176.548 1.00 10.55  ? 1836 PHE A CB    1 
ATOM   2392  C  CG    . PHE A 1 1836 ? 219.631 218.567 177.971 1.00 7.23   ? 1836 PHE A CG    1 
ATOM   2393  C  CD1   . PHE A 1 1836 ? 218.297 218.390 178.292 1.00 7.24   ? 1836 PHE A CD1   1 
ATOM   2394  C  CD2   . PHE A 1 1836 ? 220.526 218.855 178.984 1.00 6.48   ? 1836 PHE A CD2   1 
ATOM   2395  C  CE1   . PHE A 1 1836 ? 217.867 218.493 179.599 1.00 7.16   ? 1836 PHE A CE1   1 
ATOM   2396  C  CE2   . PHE A 1 1836 ? 220.099 218.960 180.291 1.00 7.66   ? 1836 PHE A CE2   1 
ATOM   2397  C  CZ    . PHE A 1 1836 ? 218.768 218.777 180.599 1.00 8.44   ? 1836 PHE A CZ    1 
ATOM   2398  N  N     . GLU A 1 1837 ? 221.298 221.334 175.270 1.00 14.77  ? 1837 GLU A N     1 
ATOM   2399  C  CA    . GLU A 1 1837 ? 221.932 222.614 175.563 1.00 18.65  ? 1837 GLU A CA    1 
ATOM   2400  C  C     . GLU A 1 1837 ? 220.951 223.768 175.400 1.00 16.14  ? 1837 GLU A C     1 
ATOM   2401  O  O     . GLU A 1 1837 ? 221.182 224.860 175.932 1.00 14.25  ? 1837 GLU A O     1 
ATOM   2402  C  CB    . GLU A 1 1837 ? 223.151 222.810 174.665 1.00 21.91  ? 1837 GLU A CB    1 
ATOM   2403  C  CG    . GLU A 1 1837 ? 224.347 221.965 175.064 1.00 27.48  ? 1837 GLU A CG    1 
ATOM   2404  C  CD    . GLU A 1 1837 ? 224.329 220.589 174.426 1.00 39.20  ? 1837 GLU A CD    1 
ATOM   2405  O  OE1   . GLU A 1 1837 ? 223.343 220.265 173.731 1.00 30.66  ? 1837 GLU A OE1   1 
ATOM   2406  O  OE2   . GLU A 1 1837 ? 225.303 219.831 174.617 1.00 45.30  ? 1837 GLU A OE2   1 
ATOM   2407  N  N     . TRP A 1 1838 ? 219.857 223.547 174.675 1.00 11.99  ? 1838 TRP A N     1 
ATOM   2408  C  CA    . TRP A 1 1838 ? 218.796 224.534 174.539 1.00 10.39  ? 1838 TRP A CA    1 
ATOM   2409  C  C     . TRP A 1 1838 ? 217.601 224.253 175.437 1.00 12.42  ? 1838 TRP A C     1 
ATOM   2410  O  O     . TRP A 1 1838 ? 216.957 225.198 175.902 1.00 13.45  ? 1838 TRP A O     1 
ATOM   2411  C  CB    . TRP A 1 1838 ? 218.333 224.612 173.080 1.00 10.16  ? 1838 TRP A CB    1 
ATOM   2412  C  CG    . TRP A 1 1838 ? 217.151 225.506 172.855 1.00 10.42  ? 1838 TRP A CG    1 
ATOM   2413  C  CD1   . TRP A 1 1838 ? 215.963 225.160 172.284 1.00 11.49  ? 1838 TRP A CD1   1 
ATOM   2414  C  CD2   . TRP A 1 1838 ? 217.041 226.893 173.197 1.00 9.91   ? 1838 TRP A CD2   1 
ATOM   2415  N  NE1   . TRP A 1 1838 ? 215.121 226.243 172.246 1.00 12.20  ? 1838 TRP A NE1   1 
ATOM   2416  C  CE2   . TRP A 1 1838 ? 215.759 227.320 172.801 1.00 11.67  ? 1838 TRP A CE2   1 
ATOM   2417  C  CE3   . TRP A 1 1838 ? 217.903 227.816 173.799 1.00 8.12   ? 1838 TRP A CE3   1 
ATOM   2418  C  CZ2   . TRP A 1 1838 ? 215.318 228.626 172.988 1.00 14.25  ? 1838 TRP A CZ2   1 
ATOM   2419  C  CZ3   . TRP A 1 1838 ? 217.462 229.110 173.984 1.00 10.12  ? 1838 TRP A CZ3   1 
ATOM   2420  C  CH2   . TRP A 1 1838 ? 216.181 229.504 173.582 1.00 13.04  ? 1838 TRP A CH2   1 
ATOM   2421  N  N     . LEU A 1 1839 ? 217.288 222.980 175.694 1.00 11.42  ? 1839 LEU A N     1 
ATOM   2422  C  CA    . LEU A 1 1839 ? 216.189 222.667 176.602 1.00 10.40  ? 1839 LEU A CA    1 
ATOM   2423  C  C     . LEU A 1 1839 ? 216.566 222.898 178.058 1.00 10.77  ? 1839 LEU A C     1 
ATOM   2424  O  O     . LEU A 1 1839 ? 215.687 223.175 178.882 1.00 15.73  ? 1839 LEU A O     1 
ATOM   2425  C  CB    . LEU A 1 1839 ? 215.707 221.229 176.398 1.00 10.85  ? 1839 LEU A CB    1 
ATOM   2426  C  CG    . LEU A 1 1839 ? 214.807 220.951 175.189 1.00 13.07  ? 1839 LEU A CG    1 
ATOM   2427  C  CD1   . LEU A 1 1839 ? 215.563 221.020 173.885 1.00 17.42  ? 1839 LEU A CD1   1 
ATOM   2428  C  CD2   . LEU A 1 1839 ? 214.121 219.602 175.335 1.00 13.43  ? 1839 LEU A CD2   1 
ATOM   2429  N  N     . SER A 1 1840 ? 217.851 222.797 178.399 1.00 7.53   ? 1840 SER A N     1 
ATOM   2430  C  CA    . SER A 1 1840 ? 218.274 223.100 179.760 1.00 8.06   ? 1840 SER A CA    1 
ATOM   2431  C  C     . SER A 1 1840 ? 218.109 224.572 180.111 1.00 9.66   ? 1840 SER A C     1 
ATOM   2432  O  O     . SER A 1 1840 ? 218.201 224.925 181.290 1.00 9.37   ? 1840 SER A O     1 
ATOM   2433  C  CB    . SER A 1 1840 ? 219.727 222.676 179.973 1.00 9.39   ? 1840 SER A CB    1 
ATOM   2434  O  OG    . SER A 1 1840 ? 220.553 223.133 178.918 1.00 15.45  ? 1840 SER A OG    1 
ATOM   2435  N  N     . GLN A 1 1841 ? 217.875 225.432 179.123 1.00 11.35  ? 1841 GLN A N     1 
ATOM   2436  C  CA    . GLN A 1 1841 ? 217.625 226.840 179.372 1.00 9.85   ? 1841 GLN A CA    1 
ATOM   2437  C  C     . GLN A 1 1841 ? 216.136 227.089 179.593 1.00 8.14   ? 1841 GLN A C     1 
ATOM   2438  O  O     . GLN A 1 1841 ? 215.282 226.261 179.265 1.00 7.75   ? 1841 GLN A O     1 
ATOM   2439  C  CB    . GLN A 1 1841 ? 218.124 227.692 178.205 1.00 7.67   ? 1841 GLN A CB    1 
ATOM   2440  C  CG    . GLN A 1 1841 ? 219.520 227.342 177.725 1.00 7.33   ? 1841 GLN A CG    1 
ATOM   2441  C  CD    . GLN A 1 1841 ? 220.581 227.616 178.766 1.00 10.56  ? 1841 GLN A CD    1 
ATOM   2442  O  OE1   . GLN A 1 1841 ? 220.589 228.671 179.397 1.00 14.56  ? 1841 GLN A OE1   1 
ATOM   2443  N  NE2   . GLN A 1 1841 ? 221.484 226.664 178.954 1.00 12.40  ? 1841 GLN A NE2   1 
ATOM   2444  N  N     . MET A 1 1842 ? 215.834 228.252 180.163 1.00 7.15   ? 1842 MET A N     1 
ATOM   2445  C  CA    . MET A 1 1842 ? 214.453 228.694 180.317 1.00 5.71   ? 1842 MET A CA    1 
ATOM   2446  C  C     . MET A 1 1842 ? 213.977 229.309 179.007 1.00 6.89   ? 1842 MET A C     1 
ATOM   2447  O  O     . MET A 1 1842 ? 214.543 230.304 178.541 1.00 11.54  ? 1842 MET A O     1 
ATOM   2448  C  CB    . MET A 1 1842 ? 214.342 229.698 181.460 1.00 4.75   ? 1842 MET A CB    1 
ATOM   2449  C  CG    . MET A 1 1842 ? 212.931 229.913 181.968 1.00 6.07   ? 1842 MET A CG    1 
ATOM   2450  S  SD    . MET A 1 1842 ? 212.868 230.356 183.712 1.00 16.13  ? 1842 MET A SD    1 
ATOM   2451  C  CE    . MET A 1 1842 ? 212.642 228.750 184.468 1.00 9.19   ? 1842 MET A CE    1 
ATOM   2452  N  N     . ARG A 1 1843 ? 212.942 228.723 178.413 1.00 7.02   ? 1843 ARG A N     1 
ATOM   2453  C  CA    . ARG A 1 1843 ? 212.435 229.146 177.116 1.00 6.18   ? 1843 ARG A CA    1 
ATOM   2454  C  C     . ARG A 1 1843 ? 210.992 229.602 177.261 1.00 8.67   ? 1843 ARG A C     1 
ATOM   2455  O  O     . ARG A 1 1843 ? 210.230 229.044 178.059 1.00 9.88   ? 1843 ARG A O     1 
ATOM   2456  C  CB    . ARG A 1 1843 ? 212.536 228.012 176.092 1.00 8.52   ? 1843 ARG A CB    1 
ATOM   2457  C  CG    . ARG A 1 1843 ? 213.735 227.109 176.312 1.00 7.74   ? 1843 ARG A CG    1 
ATOM   2458  C  CD    . ARG A 1 1843 ? 213.743 225.921 175.369 1.00 8.79   ? 1843 ARG A CD    1 
ATOM   2459  N  NE    . ARG A 1 1843 ? 212.643 224.993 175.605 1.00 11.77  ? 1843 ARG A NE    1 
ATOM   2460  C  CZ    . ARG A 1 1843 ? 212.580 224.135 176.615 1.00 10.44  ? 1843 ARG A CZ    1 
ATOM   2461  N  NH1   . ARG A 1 1843 ? 213.505 224.110 177.560 1.00 8.04   ? 1843 ARG A NH1   1 
ATOM   2462  N  NH2   . ARG A 1 1843 ? 211.561 223.285 176.681 1.00 13.88  ? 1843 ARG A NH2   1 
ATOM   2463  N  N     . PHE A 1 1844 ? 210.622 230.618 176.489 1.00 10.71  ? 1844 PHE A N     1 
ATOM   2464  C  CA    . PHE A 1 1844 ? 209.308 231.239 176.574 1.00 9.57   ? 1844 PHE A CA    1 
ATOM   2465  C  C     . PHE A 1 1844 ? 208.591 231.081 175.243 1.00 13.33  ? 1844 PHE A C     1 
ATOM   2466  O  O     . PHE A 1 1844 ? 209.119 231.473 174.198 1.00 15.91  ? 1844 PHE A O     1 
ATOM   2467  C  CB    . PHE A 1 1844 ? 209.426 232.719 176.950 1.00 7.83   ? 1844 PHE A CB    1 
ATOM   2468  C  CG    . PHE A 1 1844 ? 210.134 232.956 178.255 1.00 7.43   ? 1844 PHE A CG    1 
ATOM   2469  C  CD1   . PHE A 1 1844 ? 211.517 232.906 178.330 1.00 8.11   ? 1844 PHE A CD1   1 
ATOM   2470  C  CD2   . PHE A 1 1844 ? 209.418 233.219 179.406 1.00 6.70   ? 1844 PHE A CD2   1 
ATOM   2471  C  CE1   . PHE A 1 1844 ? 212.166 233.116 179.527 1.00 6.40   ? 1844 PHE A CE1   1 
ATOM   2472  C  CE2   . PHE A 1 1844 ? 210.064 233.431 180.604 1.00 7.17   ? 1844 PHE A CE2   1 
ATOM   2473  C  CZ    . PHE A 1 1844 ? 211.440 233.379 180.664 1.00 6.29   ? 1844 PHE A CZ    1 
ATOM   2474  N  N     . TYR A 1 1845 ? 207.389 230.513 175.286 1.00 18.35  ? 1845 TYR A N     1 
ATOM   2475  C  CA    . TYR A 1 1845 ? 206.591 230.250 174.099 1.00 17.76  ? 1845 TYR A CA    1 
ATOM   2476  C  C     . TYR A 1 1845 ? 205.289 231.027 174.188 1.00 21.55  ? 1845 TYR A C     1 
ATOM   2477  O  O     . TYR A 1 1845 ? 204.560 230.920 175.180 1.00 19.94  ? 1845 TYR A O     1 
ATOM   2478  C  CB    . TYR A 1 1845 ? 206.325 228.753 173.948 1.00 14.60  ? 1845 TYR A CB    1 
ATOM   2479  C  CG    . TYR A 1 1845 ? 207.593 227.946 173.809 1.00 16.05  ? 1845 TYR A CG    1 
ATOM   2480  C  CD1   . TYR A 1 1845 ? 208.346 228.004 172.645 1.00 18.63  ? 1845 TYR A CD1   1 
ATOM   2481  C  CD2   . TYR A 1 1845 ? 208.055 227.155 174.850 1.00 19.74  ? 1845 TYR A CD2   1 
ATOM   2482  C  CE1   . TYR A 1 1845 ? 209.509 227.278 172.513 1.00 21.92  ? 1845 TYR A CE1   1 
ATOM   2483  C  CE2   . TYR A 1 1845 ? 209.222 226.427 174.725 1.00 19.41  ? 1845 TYR A CE2   1 
ATOM   2484  C  CZ    . TYR A 1 1845 ? 209.943 226.493 173.555 1.00 16.55  ? 1845 TYR A CZ    1 
ATOM   2485  O  OH    . TYR A 1 1845 ? 211.106 225.771 173.424 1.00 19.14  ? 1845 TYR A OH    1 
ATOM   2486  N  N     . PHE A 1 1846 ? 205.003 231.807 173.152 1.00 26.92  ? 1846 PHE A N     1 
ATOM   2487  C  CA    . PHE A 1 1846 ? 203.829 232.664 173.104 1.00 30.71  ? 1846 PHE A CA    1 
ATOM   2488  C  C     . PHE A 1 1846 ? 202.943 232.215 171.951 1.00 42.26  ? 1846 PHE A C     1 
ATOM   2489  O  O     . PHE A 1 1846 ? 203.392 232.163 170.802 1.00 48.71  ? 1846 PHE A O     1 
ATOM   2490  C  CB    . PHE A 1 1846 ? 204.240 234.128 172.932 1.00 32.60  ? 1846 PHE A CB    1 
ATOM   2491  C  CG    . PHE A 1 1846 ? 203.190 235.110 173.358 1.00 30.67  ? 1846 PHE A CG    1 
ATOM   2492  C  CD1   . PHE A 1 1846 ? 202.792 236.130 172.513 1.00 30.92  ? 1846 PHE A CD1   1 
ATOM   2493  C  CD2   . PHE A 1 1846 ? 202.615 235.022 174.614 1.00 27.84  ? 1846 PHE A CD2   1 
ATOM   2494  C  CE1   . PHE A 1 1846 ? 201.832 237.037 172.908 1.00 34.92  ? 1846 PHE A CE1   1 
ATOM   2495  C  CE2   . PHE A 1 1846 ? 201.656 235.928 175.015 1.00 29.49  ? 1846 PHE A CE2   1 
ATOM   2496  C  CZ    . PHE A 1 1846 ? 201.263 236.936 174.161 1.00 34.34  ? 1846 PHE A CZ    1 
ATOM   2497  N  N     . ASP A 1 1847 ? 201.687 231.892 172.259 1.00 46.68  ? 1847 ASP A N     1 
ATOM   2498  C  CA    . ASP A 1 1847 ? 200.739 231.358 171.282 1.00 57.29  ? 1847 ASP A CA    1 
ATOM   2499  C  C     . ASP A 1 1847 ? 199.541 232.293 171.201 1.00 63.52  ? 1847 ASP A C     1 
ATOM   2500  O  O     . ASP A 1 1847 ? 198.575 232.145 171.965 1.00 62.32  ? 1847 ASP A O     1 
ATOM   2501  C  CB    . ASP A 1 1847 ? 200.306 229.941 171.655 1.00 63.53  ? 1847 ASP A CB    1 
ATOM   2502  C  CG    . ASP A 1 1847 ? 199.708 229.186 170.484 1.00 68.45  ? 1847 ASP A CG    1 
ATOM   2503  O  OD1   . ASP A 1 1847 ? 198.789 228.371 170.708 1.00 64.18  ? 1847 ASP A OD1   1 
ATOM   2504  O  OD2   . ASP A 1 1847 ? 200.157 229.406 169.339 1.00 72.56  ? 1847 ASP A OD2   1 
ATOM   2505  N  N     . PRO A 1 1848 ? 199.555 233.263 170.283 1.00 69.74  ? 1848 PRO A N     1 
ATOM   2506  C  CA    . PRO A 1 1848 ? 198.410 234.182 170.168 1.00 74.14  ? 1848 PRO A CA    1 
ATOM   2507  C  C     . PRO A 1 1848 ? 197.117 233.497 169.763 1.00 73.72  ? 1848 PRO A C     1 
ATOM   2508  O  O     . PRO A 1 1848 ? 196.041 234.073 169.966 1.00 63.96  ? 1848 PRO A O     1 
ATOM   2509  C  CB    . PRO A 1 1848 ? 198.872 235.186 169.104 1.00 69.73  ? 1848 PRO A CB    1 
ATOM   2510  C  CG    . PRO A 1 1848 ? 199.911 234.456 168.319 1.00 69.20  ? 1848 PRO A CG    1 
ATOM   2511  C  CD    . PRO A 1 1848 ? 200.611 233.566 169.304 1.00 64.85  ? 1848 PRO A CD    1 
ATOM   2512  N  N     . LYS A 1 1849 ? 197.184 232.293 169.195 1.00 69.55  ? 1849 LYS A N     1 
ATOM   2513  C  CA    . LYS A 1 1849 ? 195.987 231.580 168.773 1.00 66.19  ? 1849 LYS A CA    1 
ATOM   2514  C  C     . LYS A 1 1849 ? 195.195 230.998 169.938 1.00 71.26  ? 1849 LYS A C     1 
ATOM   2515  O  O     . LYS A 1 1849 ? 194.061 230.553 169.730 1.00 73.02  ? 1849 LYS A O     1 
ATOM   2516  C  CB    . LYS A 1 1849 ? 196.359 230.460 167.798 1.00 71.80  ? 1849 LYS A CB    1 
ATOM   2517  C  CG    . LYS A 1 1849 ? 197.247 230.914 166.649 1.00 74.49  ? 1849 LYS A CG    1 
ATOM   2518  C  CD    . LYS A 1 1849 ? 196.451 231.675 165.603 1.00 75.50  ? 1849 LYS A CD    1 
ATOM   2519  C  CE    . LYS A 1 1849 ? 197.342 232.627 164.820 1.00 79.46  ? 1849 LYS A CE    1 
ATOM   2520  N  NZ    . LYS A 1 1849 ? 198.390 231.902 164.048 1.00 85.30  ? 1849 LYS A NZ    1 
ATOM   2521  N  N     . GLN A 1 1850 ? 195.755 230.984 171.145 1.00 71.61  ? 1850 GLN A N     1 
ATOM   2522  C  CA    . GLN A 1 1850 ? 195.023 230.489 172.304 1.00 63.50  ? 1850 GLN A CA    1 
ATOM   2523  C  C     . GLN A 1 1850 ? 193.894 231.443 172.668 1.00 62.34  ? 1850 GLN A C     1 
ATOM   2524  O  O     . GLN A 1 1850 ? 194.091 232.660 172.743 1.00 56.79  ? 1850 GLN A O     1 
ATOM   2525  C  CB    . GLN A 1 1850 ? 195.965 230.308 173.493 1.00 54.96  ? 1850 GLN A CB    1 
ATOM   2526  C  CG    . GLN A 1 1850 ? 197.020 229.238 173.293 1.00 63.97  ? 1850 GLN A CG    1 
ATOM   2527  C  CD    . GLN A 1 1850 ? 196.416 227.858 173.107 1.00 68.53  ? 1850 GLN A CD    1 
ATOM   2528  O  OE1   . GLN A 1 1850 ? 196.447 227.296 172.013 1.00 71.12  ? 1850 GLN A OE1   1 
ATOM   2529  N  NE2   . GLN A 1 1850 ? 195.862 227.307 174.180 1.00 50.85  ? 1850 GLN A NE2   1 
ATOM   2530  N  N     . THR A 1 1851 ? 192.702 230.885 172.890 1.00 67.55  ? 1851 THR A N     1 
ATOM   2531  C  CA    . THR A 1 1851 ? 191.572 231.701 173.321 1.00 64.89  ? 1851 THR A CA    1 
ATOM   2532  C  C     . THR A 1 1851 ? 191.794 232.250 174.724 1.00 54.73  ? 1851 THR A C     1 
ATOM   2533  O  O     . THR A 1 1851 ? 191.464 233.409 175.003 1.00 49.27  ? 1851 THR A O     1 
ATOM   2534  C  CB    . THR A 1 1851 ? 190.280 230.886 173.263 1.00 64.51  ? 1851 THR A CB    1 
ATOM   2535  O  OG1   . THR A 1 1851 ? 190.360 229.792 174.186 1.00 60.54  ? 1851 THR A OG1   1 
ATOM   2536  C  CG2   . THR A 1 1851 ? 190.056 230.343 171.860 1.00 58.81  ? 1851 THR A CG2   1 
ATOM   2537  N  N     . ASP A 1 1852 ? 192.346 231.435 175.619 1.00 52.21  ? 1852 ASP A N     1 
ATOM   2538  C  CA    . ASP A 1 1852 ? 192.615 231.858 176.989 1.00 51.17  ? 1852 ASP A CA    1 
ATOM   2539  C  C     . ASP A 1 1852 ? 193.924 232.636 177.018 1.00 52.24  ? 1852 ASP A C     1 
ATOM   2540  O  O     . ASP A 1 1852 ? 194.995 232.075 176.768 1.00 51.83  ? 1852 ASP A O     1 
ATOM   2541  C  CB    . ASP A 1 1852 ? 192.673 230.649 177.918 1.00 43.64  ? 1852 ASP A CB    1 
ATOM   2542  C  CG    . ASP A 1 1852 ? 192.447 231.020 179.369 1.00 52.06  ? 1852 ASP A CG    1 
ATOM   2543  O  OD1   . ASP A 1 1852 ? 192.156 232.204 179.643 1.00 49.49  ? 1852 ASP A OD1   1 
ATOM   2544  O  OD2   . ASP A 1 1852 ? 192.562 230.130 180.237 1.00 51.56  ? 1852 ASP A OD2   1 
ATOM   2545  N  N     . VAL A 1 1853 ? 193.839 233.934 177.323 1.00 53.94  ? 1853 VAL A N     1 
ATOM   2546  C  CA    . VAL A 1 1853 ? 195.038 234.759 177.393 1.00 46.70  ? 1853 VAL A CA    1 
ATOM   2547  C  C     . VAL A 1 1853 ? 195.898 234.371 178.589 1.00 45.88  ? 1853 VAL A C     1 
ATOM   2548  O  O     . VAL A 1 1853 ? 197.104 234.648 178.610 1.00 44.90  ? 1853 VAL A O     1 
ATOM   2549  C  CB    . VAL A 1 1853 ? 194.659 236.251 177.432 1.00 46.89  ? 1853 VAL A CB    1 
ATOM   2550  C  CG1   . VAL A 1 1853 ? 193.927 236.645 176.160 1.00 45.36  ? 1853 VAL A CG1   1 
ATOM   2551  C  CG2   . VAL A 1 1853 ? 193.803 236.545 178.651 1.00 44.17  ? 1853 VAL A CG2   1 
ATOM   2552  N  N     . LEU A 1 1854 ? 195.304 233.739 179.603 1.00 36.21  ? 1854 LEU A N     1 
ATOM   2553  C  CA    . LEU A 1 1854 ? 196.086 233.310 180.757 1.00 34.10  ? 1854 LEU A CA    1 
ATOM   2554  C  C     . LEU A 1 1854 ? 197.016 232.158 180.399 1.00 40.62  ? 1854 LEU A C     1 
ATOM   2555  O  O     . LEU A 1 1854 ? 198.189 232.154 180.790 1.00 49.52  ? 1854 LEU A O     1 
ATOM   2556  C  CB    . LEU A 1 1854 ? 195.156 232.916 181.905 1.00 39.51  ? 1854 LEU A CB    1 
ATOM   2557  C  CG    . LEU A 1 1854 ? 194.205 233.998 182.424 1.00 36.66  ? 1854 LEU A CG    1 
ATOM   2558  C  CD1   . LEU A 1 1854 ? 193.716 233.645 183.819 1.00 29.26  ? 1854 LEU A CD1   1 
ATOM   2559  C  CD2   . LEU A 1 1854 ? 194.874 235.363 182.422 1.00 28.71  ? 1854 LEU A CD2   1 
ATOM   2560  N  N     . GLN A 1 1855 ? 196.517 231.179 179.649 1.00 40.74  ? 1855 GLN A N     1 
ATOM   2561  C  CA    . GLN A 1 1855 ? 197.323 230.060 179.179 1.00 35.13  ? 1855 GLN A CA    1 
ATOM   2562  C  C     . GLN A 1 1855 ? 198.073 230.383 177.895 1.00 32.07  ? 1855 GLN A C     1 
ATOM   2563  O  O     . GLN A 1 1855 ? 198.578 229.469 177.238 1.00 37.86  ? 1855 GLN A O     1 
ATOM   2564  C  CB    . GLN A 1 1855 ? 196.443 228.828 178.965 1.00 34.25  ? 1855 GLN A CB    1 
ATOM   2565  C  CG    . GLN A 1 1855 ? 196.148 228.041 180.225 1.00 36.13  ? 1855 GLN A CG    1 
ATOM   2566  C  CD    . GLN A 1 1855 ? 195.244 226.854 179.963 1.00 51.83  ? 1855 GLN A CD    1 
ATOM   2567  O  OE1   . GLN A 1 1855 ? 194.587 226.777 178.926 1.00 54.33  ? 1855 GLN A OE1   1 
ATOM   2568  N  NE2   . GLN A 1 1855 ? 195.207 225.919 180.906 1.00 55.24  ? 1855 GLN A NE2   1 
ATOM   2569  N  N     . GLN A 1 1856 ? 198.152 231.662 177.524 1.00 33.02  ? 1856 GLN A N     1 
ATOM   2570  C  CA    . GLN A 1 1856 ? 198.739 232.033 176.241 1.00 38.90  ? 1856 GLN A CA    1 
ATOM   2571  C  C     . GLN A 1 1856 ? 200.260 231.924 176.271 1.00 31.73  ? 1856 GLN A C     1 
ATOM   2572  O  O     . GLN A 1 1856 ? 200.891 231.670 175.238 1.00 32.10  ? 1856 GLN A O     1 
ATOM   2573  C  CB    . GLN A 1 1856 ? 198.292 233.447 175.871 1.00 41.93  ? 1856 GLN A CB    1 
ATOM   2574  C  CG    . GLN A 1 1856 ? 198.749 233.940 174.514 1.00 51.47  ? 1856 GLN A CG    1 
ATOM   2575  C  CD    . GLN A 1 1856 ? 198.215 235.324 174.198 1.00 57.09  ? 1856 GLN A CD    1 
ATOM   2576  O  OE1   . GLN A 1 1856 ? 197.528 235.934 175.015 1.00 57.24  ? 1856 GLN A OE1   1 
ATOM   2577  N  NE2   . GLN A 1 1856 ? 198.519 235.821 173.006 1.00 47.38  ? 1856 GLN A NE2   1 
ATOM   2578  N  N     . LEU A 1 1857 ? 200.863 232.100 177.443 1.00 27.06  ? 1857 LEU A N     1 
ATOM   2579  C  CA    . LEU A 1 1857 ? 202.311 232.059 177.600 1.00 16.14  ? 1857 LEU A CA    1 
ATOM   2580  C  C     . LEU A 1 1857 ? 202.719 230.803 178.357 1.00 16.17  ? 1857 LEU A C     1 
ATOM   2581  O  O     . LEU A 1 1857 ? 202.120 230.468 179.384 1.00 17.26  ? 1857 LEU A O     1 
ATOM   2582  C  CB    . LEU A 1 1857 ? 202.810 233.301 178.341 1.00 13.00  ? 1857 LEU A CB    1 
ATOM   2583  C  CG    . LEU A 1 1857 ? 204.279 233.299 178.764 1.00 13.27  ? 1857 LEU A CG    1 
ATOM   2584  C  CD1   . LEU A 1 1857 ? 205.193 233.200 177.555 1.00 14.92  ? 1857 LEU A CD1   1 
ATOM   2585  C  CD2   . LEU A 1 1857 ? 204.603 234.532 179.584 1.00 11.16  ? 1857 LEU A CD2   1 
ATOM   2586  N  N     . SER A 1 1858 ? 203.739 230.114 177.851 1.00 16.23  ? 1858 SER A N     1 
ATOM   2587  C  CA    . SER A 1 1858 ? 204.287 228.927 178.491 1.00 12.21  ? 1858 SER A CA    1 
ATOM   2588  C  C     . SER A 1 1858 ? 205.774 229.128 178.747 1.00 12.71  ? 1858 SER A C     1 
ATOM   2589  O  O     . SER A 1 1858 ? 206.491 229.674 177.905 1.00 15.78  ? 1858 SER A O     1 
ATOM   2590  C  CB    . SER A 1 1858 ? 204.068 227.683 177.626 1.00 10.98  ? 1858 SER A CB    1 
ATOM   2591  O  OG    . SER A 1 1858 ? 204.677 226.545 178.209 1.00 17.93  ? 1858 SER A OG    1 
ATOM   2592  N  N     . ILE A 1 1859 ? 206.233 228.696 179.918 1.00 8.66   ? 1859 ILE A N     1 
ATOM   2593  C  CA    . ILE A 1 1859 ? 207.639 228.776 180.293 1.00 8.20   ? 1859 ILE A CA    1 
ATOM   2594  C  C     . ILE A 1 1859 ? 208.136 227.360 180.533 1.00 9.36   ? 1859 ILE A C     1 
ATOM   2595  O  O     . ILE A 1 1859 ? 207.599 226.644 181.386 1.00 11.90  ? 1859 ILE A O     1 
ATOM   2596  C  CB    . ILE A 1 1859 ? 207.853 229.655 181.535 1.00 11.19  ? 1859 ILE A CB    1 
ATOM   2597  C  CG1   . ILE A 1 1859 ? 207.129 230.992 181.368 1.00 8.95   ? 1859 ILE A CG1   1 
ATOM   2598  C  CG2   . ILE A 1 1859 ? 209.331 229.879 181.779 1.00 9.04   ? 1859 ILE A CG2   1 
ATOM   2599  C  CD1   . ILE A 1 1859 ? 207.167 231.863 182.596 1.00 7.62   ? 1859 ILE A CD1   1 
ATOM   2600  N  N     . GLN A 1 1860 ? 209.161 226.954 179.789 1.00 11.34  ? 1860 GLN A N     1 
ATOM   2601  C  CA    . GLN A 1 1860 ? 209.631 225.577 179.803 1.00 7.40   ? 1860 GLN A CA    1 
ATOM   2602  C  C     . GLN A 1 1860 ? 211.114 225.524 180.139 1.00 9.03   ? 1860 GLN A C     1 
ATOM   2603  O  O     . GLN A 1 1860 ? 211.913 226.278 179.576 1.00 8.26   ? 1860 GLN A O     1 
ATOM   2604  C  CB    . GLN A 1 1860 ? 209.364 224.900 178.457 1.00 9.17   ? 1860 GLN A CB    1 
ATOM   2605  C  CG    . GLN A 1 1860 ? 207.978 225.171 177.899 1.00 11.82  ? 1860 GLN A CG    1 
ATOM   2606  C  CD    . GLN A 1 1860 ? 207.605 224.227 176.779 1.00 19.76  ? 1860 GLN A CD    1 
ATOM   2607  O  OE1   . GLN A 1 1860 ? 208.345 223.298 176.461 1.00 23.60  ? 1860 GLN A OE1   1 
ATOM   2608  N  NE2   . GLN A 1 1860 ? 206.447 224.459 176.173 1.00 20.06  ? 1860 GLN A NE2   1 
ATOM   2609  N  N     . MET A 1 1861 ? 211.470 224.635 181.062 1.00 8.26   ? 1861 MET A N     1 
ATOM   2610  C  CA    . MET A 1 1861 ? 212.861 224.364 181.404 1.00 6.75   ? 1861 MET A CA    1 
ATOM   2611  C  C     . MET A 1 1861 ? 213.037 222.858 181.488 1.00 12.81  ? 1861 MET A C     1 
ATOM   2612  O  O     . MET A 1 1861 ? 212.387 222.207 182.313 1.00 19.81  ? 1861 MET A O     1 
ATOM   2613  C  CB    . MET A 1 1861 ? 213.257 225.030 182.725 1.00 6.73   ? 1861 MET A CB    1 
ATOM   2614  C  CG    . MET A 1 1861 ? 214.756 225.194 182.902 1.00 10.16  ? 1861 MET A CG    1 
ATOM   2615  S  SD    . MET A 1 1861 ? 215.196 226.224 184.310 1.00 14.19  ? 1861 MET A SD    1 
ATOM   2616  C  CE    . MET A 1 1861 ? 216.915 226.566 183.948 1.00 4.51   ? 1861 MET A CE    1 
ATOM   2617  N  N     . ALA A 1 1862 ? 213.914 222.313 180.643 1.00 12.17  ? 1862 ALA A N     1 
ATOM   2618  C  CA    . ALA A 1 1862 ? 214.111 220.867 180.499 1.00 10.64  ? 1862 ALA A CA    1 
ATOM   2619  C  C     . ALA A 1 1862 ? 212.757 220.259 180.153 1.00 13.59  ? 1862 ALA A C     1 
ATOM   2620  O  O     . ALA A 1 1862 ? 212.163 220.664 179.139 1.00 17.20  ? 1862 ALA A O     1 
ATOM   2621  C  CB    . ALA A 1 1862 ? 214.795 220.312 181.750 1.00 8.45   ? 1862 ALA A CB    1 
ATOM   2622  N  N     . ASN A 1 1863 ? 212.234 219.315 180.930 1.00 10.76  ? 1863 ASN A N     1 
ATOM   2623  C  CA    . ASN A 1 1863 ? 210.929 218.729 180.668 1.00 11.76  ? 1863 ASN A CA    1 
ATOM   2624  C  C     . ASN A 1 1863 ? 209.814 219.370 181.482 1.00 13.91  ? 1863 ASN A C     1 
ATOM   2625  O  O     . ASN A 1 1863 ? 208.666 218.929 181.387 1.00 18.96  ? 1863 ASN A O     1 
ATOM   2626  C  CB    . ASN A 1 1863 ? 210.965 217.222 180.938 1.00 14.48  ? 1863 ASN A CB    1 
ATOM   2627  C  CG    . ASN A 1 1863 ? 211.076 216.899 182.413 1.00 14.74  ? 1863 ASN A CG    1 
ATOM   2628  O  OD1   . ASN A 1 1863 ? 212.025 217.305 183.079 1.00 15.53  ? 1863 ASN A OD1   1 
ATOM   2629  N  ND2   . ASN A 1 1863 ? 210.103 216.161 182.928 1.00 20.12  ? 1863 ASN A ND2   1 
ATOM   2630  N  N     . ALA A 1 1864 ? 210.119 220.396 182.271 1.00 11.98  ? 1864 ALA A N     1 
ATOM   2631  C  CA    . ALA A 1 1864 ? 209.132 221.040 183.125 1.00 10.00  ? 1864 ALA A CA    1 
ATOM   2632  C  C     . ALA A 1 1864 ? 208.478 222.200 182.386 1.00 10.73  ? 1864 ALA A C     1 
ATOM   2633  O  O     . ALA A 1 1864 ? 209.167 223.036 181.796 1.00 14.88  ? 1864 ALA A O     1 
ATOM   2634  C  CB    . ALA A 1 1864 ? 209.778 221.535 184.419 1.00 12.45  ? 1864 ALA A CB    1 
ATOM   2635  N  N     . LYS A 1 1865 ? 207.151 222.246 182.424 1.00 12.43  ? 1865 LYS A N     1 
ATOM   2636  C  CA    . LYS A 1 1865 ? 206.379 223.299 181.783 1.00 10.19  ? 1865 LYS A CA    1 
ATOM   2637  C  C     . LYS A 1 1865 ? 205.508 223.998 182.815 1.00 8.51   ? 1865 LYS A C     1 
ATOM   2638  O  O     . LYS A 1 1865 ? 204.955 223.356 183.714 1.00 9.92   ? 1865 LYS A O     1 
ATOM   2639  C  CB    . LYS A 1 1865 ? 205.508 222.743 180.653 1.00 10.27  ? 1865 LYS A CB    1 
ATOM   2640  C  CG    . LYS A 1 1865 ? 206.292 222.061 179.549 1.00 13.53  ? 1865 LYS A CG    1 
ATOM   2641  C  CD    . LYS A 1 1865 ? 205.367 221.442 178.516 1.00 19.61  ? 1865 LYS A CD    1 
ATOM   2642  C  CE    . LYS A 1 1865 ? 206.142 220.587 177.529 1.00 23.50  ? 1865 LYS A CE    1 
ATOM   2643  N  NZ    . LYS A 1 1865 ? 207.036 219.617 178.222 1.00 24.86  ? 1865 LYS A NZ    1 
ATOM   2644  N  N     . PHE A 1 1866 ? 205.396 225.317 182.683 1.00 8.52   ? 1866 PHE A N     1 
ATOM   2645  C  CA    . PHE A 1 1866 ? 204.594 226.127 183.583 1.00 10.25  ? 1866 PHE A CA    1 
ATOM   2646  C  C     . PHE A 1 1866 ? 203.817 227.148 182.769 1.00 10.63  ? 1866 PHE A C     1 
ATOM   2647  O  O     . PHE A 1 1866 ? 204.220 227.536 181.671 1.00 14.57  ? 1866 PHE A O     1 
ATOM   2648  C  CB    . PHE A 1 1866 ? 205.462 226.841 184.629 1.00 8.33   ? 1866 PHE A CB    1 
ATOM   2649  C  CG    . PHE A 1 1866 ? 206.393 225.930 185.371 1.00 7.63   ? 1866 PHE A CG    1 
ATOM   2650  C  CD1   . PHE A 1 1866 ? 205.980 225.285 186.522 1.00 7.65   ? 1866 PHE A CD1   1 
ATOM   2651  C  CD2   . PHE A 1 1866 ? 207.682 225.712 184.913 1.00 8.14   ? 1866 PHE A CD2   1 
ATOM   2652  C  CE1   . PHE A 1 1866 ? 206.833 224.445 187.206 1.00 8.02   ? 1866 PHE A CE1   1 
ATOM   2653  C  CE2   . PHE A 1 1866 ? 208.537 224.872 185.591 1.00 8.36   ? 1866 PHE A CE2   1 
ATOM   2654  C  CZ    . PHE A 1 1866 ? 208.114 224.238 186.738 1.00 7.10   ? 1866 PHE A CZ    1 
ATOM   2655  N  N     . ASN A 1 1867 ? 202.694 227.583 183.327 1.00 10.94  ? 1867 ASN A N     1 
ATOM   2656  C  CA    . ASN A 1 1867 ? 201.903 228.665 182.767 1.00 11.18  ? 1867 ASN A CA    1 
ATOM   2657  C  C     . ASN A 1 1867 ? 202.103 229.910 183.615 1.00 14.38  ? 1867 ASN A C     1 
ATOM   2658  O  O     . ASN A 1 1867 ? 202.092 229.838 184.849 1.00 12.94  ? 1867 ASN A O     1 
ATOM   2659  C  CB    . ASN A 1 1867 ? 200.418 228.298 182.706 1.00 13.83  ? 1867 ASN A CB    1 
ATOM   2660  C  CG    . ASN A 1 1867 ? 200.101 227.346 181.570 1.00 26.43  ? 1867 ASN A CG    1 
ATOM   2661  O  OD1   . ASN A 1 1867 ? 200.602 227.501 180.457 1.00 25.13  ? 1867 ASN A OD1   1 
ATOM   2662  N  ND2   . ASN A 1 1867 ? 199.265 226.353 181.847 1.00 27.52  ? 1867 ASN A ND2   1 
ATOM   2663  N  N     . TYR A 1 1868 ? 202.305 231.045 182.952 1.00 14.53  ? 1868 TYR A N     1 
ATOM   2664  C  CA    . TYR A 1 1868 ? 202.536 232.294 183.663 1.00 8.43   ? 1868 TYR A CA    1 
ATOM   2665  C  C     . TYR A 1 1868 ? 201.330 232.641 184.526 1.00 8.96   ? 1868 TYR A C     1 
ATOM   2666  O  O     . TYR A 1 1868 ? 200.190 232.639 184.052 1.00 12.34  ? 1868 TYR A O     1 
ATOM   2667  C  CB    . TYR A 1 1868 ? 202.823 233.420 182.670 1.00 11.62  ? 1868 TYR A CB    1 
ATOM   2668  C  CG    . TYR A 1 1868 ? 203.548 234.598 183.274 1.00 10.37  ? 1868 TYR A CG    1 
ATOM   2669  C  CD1   . TYR A 1 1868 ? 204.890 234.510 183.610 1.00 6.76   ? 1868 TYR A CD1   1 
ATOM   2670  C  CD2   . TYR A 1 1868 ? 202.892 235.798 183.508 1.00 7.67   ? 1868 TYR A CD2   1 
ATOM   2671  C  CE1   . TYR A 1 1868 ? 205.558 235.579 184.160 1.00 6.44   ? 1868 TYR A CE1   1 
ATOM   2672  C  CE2   . TYR A 1 1868 ? 203.554 236.874 184.059 1.00 6.16   ? 1868 TYR A CE2   1 
ATOM   2673  C  CZ    . TYR A 1 1868 ? 204.888 236.758 184.384 1.00 6.60   ? 1868 TYR A CZ    1 
ATOM   2674  O  OH    . TYR A 1 1868 ? 205.559 237.824 184.933 1.00 9.82   ? 1868 TYR A OH    1 
ATOM   2675  N  N     . GLY A 1 1869 ? 201.587 232.935 185.801 1.00 8.18   ? 1869 GLY A N     1 
ATOM   2676  C  CA    . GLY A 1 1869 ? 200.506 233.223 186.725 1.00 10.61  ? 1869 GLY A CA    1 
ATOM   2677  C  C     . GLY A 1 1869 ? 199.857 234.572 186.514 1.00 12.11  ? 1869 GLY A C     1 
ATOM   2678  O  O     . GLY A 1 1869 ? 198.718 234.773 186.950 1.00 16.97  ? 1869 GLY A O     1 
ATOM   2679  N  N     . PHE A 1 1870 ? 200.555 235.496 185.852 1.00 11.66  ? 1870 PHE A N     1 
ATOM   2680  C  CA    . PHE A 1 1870 ? 200.051 236.841 185.580 1.00 11.60  ? 1870 PHE A CA    1 
ATOM   2681  C  C     . PHE A 1 1870 ? 199.670 237.572 186.861 1.00 10.54  ? 1870 PHE A C     1 
ATOM   2682  O  O     . PHE A 1 1870 ? 198.704 238.337 186.894 1.00 14.06  ? 1870 PHE A O     1 
ATOM   2683  C  CB    . PHE A 1 1870 ? 198.874 236.806 184.602 1.00 13.03  ? 1870 PHE A CB    1 
ATOM   2684  C  CG    . PHE A 1 1870 ? 199.288 236.575 183.183 1.00 12.14  ? 1870 PHE A CG    1 
ATOM   2685  C  CD1   . PHE A 1 1870 ? 200.045 237.516 182.511 1.00 12.18  ? 1870 PHE A CD1   1 
ATOM   2686  C  CD2   . PHE A 1 1870 ? 198.943 235.406 182.528 1.00 16.41  ? 1870 PHE A CD2   1 
ATOM   2687  C  CE1   . PHE A 1 1870 ? 200.436 237.304 181.209 1.00 14.30  ? 1870 PHE A CE1   1 
ATOM   2688  C  CE2   . PHE A 1 1870 ? 199.331 235.190 181.224 1.00 23.65  ? 1870 PHE A CE2   1 
ATOM   2689  C  CZ    . PHE A 1 1870 ? 200.079 236.141 180.563 1.00 15.81  ? 1870 PHE A CZ    1 
ATOM   2690  N  N     . GLU A 1 1871 ? 200.429 237.332 187.925 1.00 13.70  ? 1871 GLU A N     1 
ATOM   2691  C  CA    . GLU A 1 1871 ? 200.282 238.081 189.161 1.00 13.45  ? 1871 GLU A CA    1 
ATOM   2692  C  C     . GLU A 1 1871 ? 201.087 239.368 189.059 1.00 14.47  ? 1871 GLU A C     1 
ATOM   2693  O  O     . GLU A 1 1871 ? 202.268 239.339 188.702 1.00 22.85  ? 1871 GLU A O     1 
ATOM   2694  C  CB    . GLU A 1 1871 ? 200.761 237.241 190.345 1.00 9.90   ? 1871 GLU A CB    1 
ATOM   2695  C  CG    . GLU A 1 1871 ? 200.614 237.902 191.703 1.00 17.59  ? 1871 GLU A CG    1 
ATOM   2696  C  CD    . GLU A 1 1871 ? 199.169 238.125 192.095 1.00 29.81  ? 1871 GLU A CD    1 
ATOM   2697  O  OE1   . GLU A 1 1871 ? 198.296 237.377 191.608 1.00 31.18  ? 1871 GLU A OE1   1 
ATOM   2698  O  OE2   . GLU A 1 1871 ? 198.907 239.049 192.894 1.00 29.38  ? 1871 GLU A OE2   1 
ATOM   2699  N  N     . TYR A 1 1872 ? 200.450 240.496 189.357 1.00 14.57  ? 1872 TYR A N     1 
ATOM   2700  C  CA    . TYR A 1 1872 ? 201.141 241.779 189.294 1.00 14.05  ? 1872 TYR A CA    1 
ATOM   2701  C  C     . TYR A 1 1872 ? 202.189 241.836 190.396 1.00 17.40  ? 1872 TYR A C     1 
ATOM   2702  O  O     . TYR A 1 1872 ? 201.854 241.812 191.585 1.00 21.48  ? 1872 TYR A O     1 
ATOM   2703  C  CB    . TYR A 1 1872 ? 200.154 242.934 189.424 1.00 13.84  ? 1872 TYR A CB    1 
ATOM   2704  C  CG    . TYR A 1 1872 ? 200.800 244.282 189.219 1.00 15.25  ? 1872 TYR A CG    1 
ATOM   2705  C  CD1   . TYR A 1 1872 ? 201.694 244.491 188.178 1.00 18.04  ? 1872 TYR A CD1   1 
ATOM   2706  C  CD2   . TYR A 1 1872 ? 200.538 245.339 190.077 1.00 16.47  ? 1872 TYR A CD2   1 
ATOM   2707  C  CE1   . TYR A 1 1872 ? 202.297 245.714 187.988 1.00 16.47  ? 1872 TYR A CE1   1 
ATOM   2708  C  CE2   . TYR A 1 1872 ? 201.136 246.569 189.895 1.00 20.95  ? 1872 TYR A CE2   1 
ATOM   2709  C  CZ    . TYR A 1 1872 ? 202.015 246.751 188.849 1.00 21.63  ? 1872 TYR A CZ    1 
ATOM   2710  O  OH    . TYR A 1 1872 ? 202.615 247.974 188.663 1.00 25.69  ? 1872 TYR A OH    1 
ATOM   2711  N  N     . LEU A 1 1873 ? 203.457 241.905 190.005 1.00 13.77  ? 1873 LEU A N     1 
ATOM   2712  C  CA    . LEU A 1 1873 ? 204.563 241.916 190.951 1.00 17.07  ? 1873 LEU A CA    1 
ATOM   2713  C  C     . LEU A 1 1873 ? 205.134 243.307 191.182 1.00 16.84  ? 1873 LEU A C     1 
ATOM   2714  O  O     . LEU A 1 1873 ? 206.086 243.447 191.955 1.00 23.34  ? 1873 LEU A O     1 
ATOM   2715  C  CB    . LEU A 1 1873 ? 205.670 240.976 190.469 1.00 17.94  ? 1873 LEU A CB    1 
ATOM   2716  C  CG    . LEU A 1 1873 ? 205.214 239.567 190.096 1.00 11.55  ? 1873 LEU A CG    1 
ATOM   2717  C  CD1   . LEU A 1 1873 ? 206.180 238.937 189.108 1.00 9.84   ? 1873 LEU A CD1   1 
ATOM   2718  C  CD2   . LEU A 1 1873 ? 205.062 238.704 191.333 1.00 12.48  ? 1873 LEU A CD2   1 
ATOM   2719  N  N     . GLY A 1 1874 ? 204.576 244.333 190.546 1.00 15.42  ? 1874 GLY A N     1 
ATOM   2720  C  CA    . GLY A 1 1874 ? 205.133 245.666 190.697 1.00 16.03  ? 1874 GLY A CA    1 
ATOM   2721  C  C     . GLY A 1 1874 ? 206.511 245.756 190.069 1.00 19.77  ? 1874 GLY A C     1 
ATOM   2722  O  O     . GLY A 1 1874 ? 206.770 245.207 188.993 1.00 20.45  ? 1874 GLY A O     1 
ATOM   2723  N  N     . VAL A 1 1875 ? 207.411 246.464 190.747 1.00 17.41  ? 1875 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1875 ? 208.788 246.588 190.286 1.00 13.95  ? 1875 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1875 ? 209.714 245.931 191.299 1.00 16.16  ? 1875 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1875 ? 210.138 246.562 192.274 1.00 18.16  ? 1875 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1875 ? 209.172 248.061 190.057 1.00 16.45  ? 1875 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1875 ? 210.569 248.159 189.466 1.00 14.31  ? 1875 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1875 ? 208.157 248.735 189.153 1.00 16.53  ? 1875 VAL A CG2   1 
ATOM   2730  N  N     . GLN A 1 1876 ? 210.029 244.661 191.079 1.00 23.15  ? 1876 GLN A N     1 
ATOM   2731  C  CA    . GLN A 1 1876 ? 210.946 243.931 191.938 1.00 20.65  ? 1876 GLN A CA    1 
ATOM   2732  C  C     . GLN A 1 1876 ? 212.382 244.136 191.470 1.00 20.98  ? 1876 GLN A C     1 
ATOM   2733  O  O     . GLN A 1 1876 ? 212.640 244.568 190.346 1.00 22.80  ? 1876 GLN A O     1 
ATOM   2734  C  CB    . GLN A 1 1876 ? 210.607 242.440 191.949 1.00 16.46  ? 1876 GLN A CB    1 
ATOM   2735  C  CG    . GLN A 1 1876 ? 209.120 242.135 192.012 1.00 16.89  ? 1876 GLN A CG    1 
ATOM   2736  C  CD    . GLN A 1 1876 ? 208.622 241.955 193.432 1.00 24.38  ? 1876 GLN A CD    1 
ATOM   2737  O  OE1   . GLN A 1 1876 ? 209.380 242.098 194.390 1.00 25.79  ? 1876 GLN A OE1   1 
ATOM   2738  N  NE2   . GLN A 1 1876 ? 207.343 241.633 193.573 1.00 28.73  ? 1876 GLN A NE2   1 
ATOM   2739  N  N     . ASP A 1 1877 ? 213.322 243.818 192.355 1.00 20.64  ? 1877 ASP A N     1 
ATOM   2740  C  CA    . ASP A 1 1877 ? 214.740 243.886 192.033 1.00 18.88  ? 1877 ASP A CA    1 
ATOM   2741  C  C     . ASP A 1 1877 ? 215.167 242.576 191.383 1.00 15.49  ? 1877 ASP A C     1 
ATOM   2742  O  O     . ASP A 1 1877 ? 215.203 241.532 192.043 1.00 15.03  ? 1877 ASP A O     1 
ATOM   2743  C  CB    . ASP A 1 1877 ? 215.571 244.166 193.286 1.00 22.26  ? 1877 ASP A CB    1 
ATOM   2744  C  CG    . ASP A 1 1877 ? 215.881 245.639 193.462 1.00 31.32  ? 1877 ASP A CG    1 
ATOM   2745  O  OD1   . ASP A 1 1877 ? 215.619 246.420 192.522 1.00 26.35  ? 1877 ASP A OD1   1 
ATOM   2746  O  OD2   . ASP A 1 1877 ? 216.387 246.018 194.538 1.00 38.14  ? 1877 ASP A OD2   1 
ATOM   2747  N  N     . LYS A 1 1878 ? 215.496 242.640 190.089 1.00 11.53  ? 1878 LYS A N     1 
ATOM   2748  C  CA    . LYS A 1 1878 ? 215.891 241.423 189.335 1.00 10.41  ? 1878 LYS A CA    1 
ATOM   2749  C  C     . LYS A 1 1878 ? 217.297 240.981 189.756 1.00 12.19  ? 1878 LYS A C     1 
ATOM   2750  O  O     . LYS A 1 1878 ? 218.180 241.855 189.880 1.00 14.13  ? 1878 LYS A O     1 
ATOM   2751  C  CB    . LYS A 1 1878 ? 215.843 241.720 187.833 1.00 9.03   ? 1878 LYS A CB    1 
ATOM   2752  C  CG    . LYS A 1 1878 ? 216.245 240.579 186.911 1.00 14.14  ? 1878 LYS A CG    1 
ATOM   2753  C  CD    . LYS A 1 1878 ? 216.290 240.997 185.446 1.00 12.09  ? 1878 LYS A CD    1 
ATOM   2754  C  CE    . LYS A 1 1878 ? 216.586 239.856 184.526 1.00 12.58  ? 1878 LYS A CE    1 
ATOM   2755  N  NZ    . LYS A 1 1878 ? 215.530 238.843 184.560 1.00 12.36  ? 1878 LYS A NZ    1 
ATOM   2756  N  N     . LEU A 1 1879 ? 217.522 239.673 189.908 1.00 9.67   ? 1879 LEU A N     1 
ATOM   2757  C  CA    . LEU A 1 1879 ? 218.875 239.163 190.255 1.00 4.25   ? 1879 LEU A CA    1 
ATOM   2758  C  C     . LEU A 1 1879 ? 219.698 238.956 188.974 1.00 6.29   ? 1879 LEU A C     1 
ATOM   2759  O  O     . LEU A 1 1879 ? 219.106 239.020 187.877 1.00 8.94   ? 1879 LEU A O     1 
ATOM   2760  C  CB    . LEU A 1 1879 ? 218.752 237.855 191.031 1.00 5.02   ? 1879 LEU A CB    1 
ATOM   2761  C  CG    . LEU A 1 1879 ? 217.987 237.920 192.355 1.00 4.06   ? 1879 LEU A CG    1 
ATOM   2762  C  CD1   . LEU A 1 1879 ? 217.966 236.531 192.959 1.00 3.06   ? 1879 LEU A CD1   1 
ATOM   2763  C  CD2   . LEU A 1 1879 ? 218.639 238.907 193.307 1.00 7.35   ? 1879 LEU A CD2   1 
ATOM   2764  N  N     . VAL A 1 1880 ? 221.005 238.710 189.113 1.00 5.66   ? 1880 VAL A N     1 
ATOM   2765  C  CA    . VAL A 1 1880 ? 221.865 238.413 187.928 1.00 3.11   ? 1880 VAL A CA    1 
ATOM   2766  C  C     . VAL A 1 1880 ? 221.800 236.901 187.677 1.00 4.09   ? 1880 VAL A C     1 
ATOM   2767  O  O     . VAL A 1 1880 ? 222.105 236.139 188.618 1.00 5.01   ? 1880 VAL A O     1 
ATOM   2768  C  CB    . VAL A 1 1880 ? 223.318 238.870 188.151 1.00 3.93   ? 1880 VAL A CB    1 
ATOM   2769  C  CG1   . VAL A 1 1880 ? 224.235 238.424 187.020 1.00 3.94   ? 1880 VAL A CG1   1 
ATOM   2770  C  CG2   . VAL A 1 1880 ? 223.414 240.374 188.376 1.00 4.54   ? 1880 VAL A CG2   1 
ATOM   2771  N  N     . GLN A 1 1881 ? 221.411 236.484 186.470 1.00 5.39   ? 1881 GLN A N     1 
ATOM   2772  C  CA    . GLN A 1 1881 ? 221.244 235.033 186.194 1.00 4.74   ? 1881 GLN A CA    1 
ATOM   2773  C  C     . GLN A 1 1881 ? 222.635 234.393 186.095 1.00 6.35   ? 1881 GLN A C     1 
ATOM   2774  O  O     . GLN A 1 1881 ? 223.147 234.257 184.965 1.00 10.86  ? 1881 GLN A O     1 
ATOM   2775  C  CB    . GLN A 1 1881 ? 220.416 234.798 184.931 1.00 5.41   ? 1881 GLN A CB    1 
ATOM   2776  C  CG    . GLN A 1 1881 ? 219.951 233.355 184.767 1.00 7.38   ? 1881 GLN A CG    1 
ATOM   2777  C  CD    . GLN A 1 1881 ? 218.881 232.952 185.756 1.00 7.73   ? 1881 GLN A CD    1 
ATOM   2778  O  OE1   . GLN A 1 1881 ? 218.382 233.770 186.538 1.00 13.79  ? 1881 GLN A OE1   1 
ATOM   2779  N  NE2   . GLN A 1 1881 ? 218.502 231.682 185.721 1.00 7.89   ? 1881 GLN A NE2   1 
ATOM   2780  N  N     . THR A 1 1882 ? 223.210 234.025 187.245 1.00 5.88   ? 1882 THR A N     1 
ATOM   2781  C  CA    . THR A 1 1882 ? 224.559 233.421 187.284 1.00 5.02   ? 1882 THR A CA    1 
ATOM   2782  C  C     . THR A 1 1882 ? 224.442 231.927 187.082 1.00 6.53   ? 1882 THR A C     1 
ATOM   2783  O  O     . THR A 1 1882 ? 223.323 231.393 187.226 1.00 9.08   ? 1882 THR A O     1 
ATOM   2784  C  CB    . THR A 1 1882 ? 225.198 233.752 188.630 1.00 6.87   ? 1882 THR A CB    1 
ATOM   2785  O  OG1   . THR A 1 1882 ? 224.364 233.122 189.597 1.00 6.79   ? 1882 THR A OG1   1 
ATOM   2786  C  CG2   . THR A 1 1882 ? 225.270 235.246 188.888 1.00 6.42   ? 1882 THR A CG2   1 
ATOM   2787  N  N     . PRO A 1 1883 ? 225.543 231.210 186.769 1.00 6.93   ? 1883 PRO A N     1 
ATOM   2788  C  CA    . PRO A 1 1883 ? 225.488 229.762 186.627 1.00 5.57   ? 1883 PRO A CA    1 
ATOM   2789  C  C     . PRO A 1 1883 ? 224.761 229.088 187.783 1.00 6.65   ? 1883 PRO A C     1 
ATOM   2790  O  O     . PRO A 1 1883 ? 223.984 228.146 187.536 1.00 7.95   ? 1883 PRO A O     1 
ATOM   2791  C  CB    . PRO A 1 1883 ? 226.978 229.402 186.593 1.00 5.34   ? 1883 PRO A CB    1 
ATOM   2792  C  CG    . PRO A 1 1883 ? 227.626 230.599 185.943 1.00 5.51   ? 1883 PRO A CG    1 
ATOM   2793  C  CD    . PRO A 1 1883 ? 226.865 231.770 186.532 1.00 7.90   ? 1883 PRO A CD    1 
ATOM   2794  N  N     . LEU A 1 1884 ? 225.004 229.550 189.013 1.00 5.67   ? 1884 LEU A N     1 
ATOM   2795  C  CA    . LEU A 1 1884 ? 224.337 228.970 190.207 1.00 4.50   ? 1884 LEU A CA    1 
ATOM   2796  C  C     . LEU A 1 1884 ? 222.824 229.223 190.121 1.00 4.82   ? 1884 LEU A C     1 
ATOM   2797  O  O     . LEU A 1 1884 ? 222.052 228.284 190.402 1.00 6.19   ? 1884 LEU A O     1 
ATOM   2798  C  CB    . LEU A 1 1884 ? 224.936 229.575 191.475 1.00 7.17   ? 1884 LEU A CB    1 
ATOM   2799  C  CG    . LEU A 1 1884 ? 224.348 229.078 192.799 1.00 6.30   ? 1884 LEU A CG    1 
ATOM   2800  C  CD1   . LEU A 1 1884 ? 224.443 227.565 192.897 1.00 4.22   ? 1884 LEU A CD1   1 
ATOM   2801  C  CD2   . LEU A 1 1884 ? 225.054 229.731 193.975 1.00 5.31   ? 1884 LEU A CD2   1 
ATOM   2802  N  N     . THR A 1 1885 ? 222.431 230.443 189.749 1.00 6.13   ? 1885 THR A N     1 
ATOM   2803  C  CA    . THR A 1 1885 ? 220.996 230.770 189.628 1.00 4.87   ? 1885 THR A CA    1 
ATOM   2804  C  C     . THR A 1 1885 ? 220.386 229.844 188.602 1.00 5.88   ? 1885 THR A C     1 
ATOM   2805  O  O     . THR A 1 1885 ? 219.288 229.314 188.862 1.00 5.82   ? 1885 THR A O     1 
ATOM   2806  C  CB    . THR A 1 1885 ? 220.831 232.236 189.238 1.00 4.80   ? 1885 THR A CB    1 
ATOM   2807  O  OG1   . THR A 1 1885 ? 221.743 232.952 190.065 1.00 5.23   ? 1885 THR A OG1   1 
ATOM   2808  C  CG2   . THR A 1 1885 ? 219.418 232.740 189.466 1.00 7.24   ? 1885 THR A CG2   1 
ATOM   2809  N  N     . ASP A 1 1886 ? 221.074 229.639 187.477 1.00 5.78   ? 1886 ASP A N     1 
ATOM   2810  C  CA    . ASP A 1 1886 ? 220.569 228.736 186.408 1.00 4.68   ? 1886 ASP A CA    1 
ATOM   2811  C  C     . ASP A 1 1886 ? 220.438 227.324 186.978 1.00 4.21   ? 1886 ASP A C     1 
ATOM   2812  O  O     . ASP A 1 1886 ? 219.382 226.695 186.765 1.00 4.60   ? 1886 ASP A O     1 
ATOM   2813  C  CB    . ASP A 1 1886 ? 221.456 228.795 185.176 1.00 5.97   ? 1886 ASP A CB    1 
ATOM   2814  C  CG    . ASP A 1 1886 ? 221.413 230.108 184.409 1.00 15.52  ? 1886 ASP A CG    1 
ATOM   2815  O  OD1   . ASP A 1 1886 ? 222.469 230.768 184.315 1.00 15.49  ? 1886 ASP A OD1   1 
ATOM   2816  O  OD2   . ASP A 1 1886 ? 220.325 230.454 183.907 1.00 22.17  ? 1886 ASP A OD2   1 
ATOM   2817  N  N     . ARG A 1 1887 ? 221.470 226.848 187.677 1.00 4.18   ? 1887 ARG A N     1 
ATOM   2818  C  CA    . ARG A 1 1887 ? 221.386 225.535 188.306 1.00 4.33   ? 1887 ARG A CA    1 
ATOM   2819  C  C     . ARG A 1 1887 ? 220.231 225.479 189.298 1.00 5.76   ? 1887 ARG A C     1 
ATOM   2820  O  O     . ARG A 1 1887 ? 219.515 224.474 189.376 1.00 5.61   ? 1887 ARG A O     1 
ATOM   2821  C  CB    . ARG A 1 1887 ? 222.713 225.208 188.991 1.00 4.17   ? 1887 ARG A CB    1 
ATOM   2822  C  CG    . ARG A 1 1887 ? 222.842 223.784 189.492 1.00 5.24   ? 1887 ARG A CG    1 
ATOM   2823  C  CD    . ARG A 1 1887 ? 224.115 223.620 190.299 1.00 5.55   ? 1887 ARG A CD    1 
ATOM   2824  N  NE    . ARG A 1 1887 ? 224.270 222.270 190.825 1.00 7.31   ? 1887 ARG A NE    1 
ATOM   2825  C  CZ    . ARG A 1 1887 ? 225.366 221.536 190.692 1.00 6.93   ? 1887 ARG A CZ    1 
ATOM   2826  N  NH1   . ARG A 1 1887 ? 226.430 221.994 190.054 1.00 6.59   ? 1887 ARG A NH1   1 
ATOM   2827  N  NH2   . ARG A 1 1887 ? 225.396 220.314 191.213 1.00 7.40   ? 1887 ARG A NH2   1 
ATOM   2828  N  N     . CYS A 1 1888 ? 220.033 226.558 190.060 1.00 4.59   ? 1888 CYS A N     1 
ATOM   2829  C  CA    . CYS A 1 1888 ? 218.908 226.623 190.985 1.00 3.42   ? 1888 CYS A CA    1 
ATOM   2830  C  C     . CYS A 1 1888 ? 217.581 226.572 190.244 1.00 3.99   ? 1888 CYS A C     1 
ATOM   2831  O  O     . CYS A 1 1888 ? 216.663 225.854 190.653 1.00 4.45   ? 1888 CYS A O     1 
ATOM   2832  C  CB    . CYS A 1 1888 ? 219.000 227.886 191.839 1.00 5.15   ? 1888 CYS A CB    1 
ATOM   2833  S  SG    . CYS A 1 1888 ? 217.687 228.058 193.071 1.00 12.18  ? 1888 CYS A SG    1 
ATOM   2834  N  N     . TYR A 1 1889 ? 217.462 227.330 189.152 1.00 4.55   ? 1889 TYR A N     1 
ATOM   2835  C  CA    . TYR A 1 1889 ? 216.238 227.299 188.359 1.00 3.84   ? 1889 TYR A CA    1 
ATOM   2836  C  C     . TYR A 1 1889 ? 215.958 225.890 187.857 1.00 4.17   ? 1889 TYR A C     1 
ATOM   2837  O  O     . TYR A 1 1889 ? 214.833 225.392 187.969 1.00 4.99   ? 1889 TYR A O     1 
ATOM   2838  C  CB    . TYR A 1 1889 ? 216.342 228.270 187.183 1.00 3.46   ? 1889 TYR A CB    1 
ATOM   2839  C  CG    . TYR A 1 1889 ? 215.952 229.696 187.497 1.00 4.77   ? 1889 TYR A CG    1 
ATOM   2840  C  CD1   . TYR A 1 1889 ? 216.163 230.237 188.757 1.00 4.27   ? 1889 TYR A CD1   1 
ATOM   2841  C  CD2   . TYR A 1 1889 ? 215.368 230.502 186.528 1.00 5.14   ? 1889 TYR A CD2   1 
ATOM   2842  C  CE1   . TYR A 1 1889 ? 215.807 231.540 189.042 1.00 3.51   ? 1889 TYR A CE1   1 
ATOM   2843  C  CE2   . TYR A 1 1889 ? 215.009 231.804 186.804 1.00 6.59   ? 1889 TYR A CE2   1 
ATOM   2844  C  CZ    . TYR A 1 1889 ? 215.231 232.318 188.063 1.00 5.65   ? 1889 TYR A CZ    1 
ATOM   2845  O  OH    . TYR A 1 1889 ? 214.875 233.616 188.341 1.00 6.38   ? 1889 TYR A OH    1 
ATOM   2846  N  N     . LEU A 1 1890 ? 216.983 225.225 187.322 1.00 4.01   ? 1890 LEU A N     1 
ATOM   2847  C  CA    . LEU A 1 1890 ? 216.801 223.876 186.797 1.00 3.13   ? 1890 LEU A CA    1 
ATOM   2848  C  C     . LEU A 1 1890 ? 216.362 222.912 187.894 1.00 4.29   ? 1890 LEU A C     1 
ATOM   2849  O  O     . LEU A 1 1890 ? 215.405 222.148 187.719 1.00 4.70   ? 1890 LEU A O     1 
ATOM   2850  C  CB    . LEU A 1 1890 ? 218.093 223.395 186.139 1.00 2.78   ? 1890 LEU A CB    1 
ATOM   2851  C  CG    . LEU A 1 1890 ? 218.043 222.044 185.425 1.00 3.27   ? 1890 LEU A CG    1 
ATOM   2852  C  CD1   . LEU A 1 1890 ? 217.222 222.138 184.150 1.00 3.74   ? 1890 LEU A CD1   1 
ATOM   2853  C  CD2   . LEU A 1 1890 ? 219.447 221.553 185.124 1.00 4.52   ? 1890 LEU A CD2   1 
ATOM   2854  N  N     . THR A 1 1891 ? 217.042 222.944 189.043 1.00 4.72   ? 1891 THR A N     1 
ATOM   2855  C  CA    . THR A 1 1891 ? 216.723 222.009 190.118 1.00 3.88   ? 1891 THR A CA    1 
ATOM   2856  C  C     . THR A 1 1891 ? 215.326 222.252 190.680 1.00 3.48   ? 1891 THR A C     1 
ATOM   2857  O  O     . THR A 1 1891 ? 214.566 221.302 190.903 1.00 5.16   ? 1891 THR A O     1 
ATOM   2858  C  CB    . THR A 1 1891 ? 217.775 222.104 191.222 1.00 6.09   ? 1891 THR A CB    1 
ATOM   2859  O  OG1   . THR A 1 1891 ? 219.081 221.996 190.646 1.00 6.64   ? 1891 THR A OG1   1 
ATOM   2860  C  CG2   . THR A 1 1891 ? 217.583 220.992 192.242 1.00 3.91   ? 1891 THR A CG2   1 
ATOM   2861  N  N     . MET A 1 1892 ? 214.962 223.516 190.908 1.00 2.88   ? 1892 MET A N     1 
ATOM   2862  C  CA    . MET A 1 1892 ? 213.645 223.797 191.471 1.00 3.60   ? 1892 MET A CA    1 
ATOM   2863  C  C     . MET A 1 1892 ? 212.534 223.512 190.470 1.00 4.37   ? 1892 MET A C     1 
ATOM   2864  O  O     . MET A 1 1892 ? 211.448 223.073 190.859 1.00 4.87   ? 1892 MET A O     1 
ATOM   2865  C  CB    . MET A 1 1892 ? 213.569 225.240 191.972 1.00 3.59   ? 1892 MET A CB    1 
ATOM   2866  C  CG    . MET A 1 1892 ? 214.684 225.681 192.923 1.00 2.95   ? 1892 MET A CG    1 
ATOM   2867  S  SD    . MET A 1 1892 ? 214.637 224.996 194.596 1.00 22.89  ? 1892 MET A SD    1 
ATOM   2868  C  CE    . MET A 1 1892 ? 215.450 223.412 194.398 1.00 4.63   ? 1892 MET A CE    1 
ATOM   2869  N  N     . THR A 1 1893 ? 212.775 223.741 189.177 1.00 4.34   ? 1893 THR A N     1 
ATOM   2870  C  CA    . THR A 1 1893 ? 211.768 223.391 188.182 1.00 3.91   ? 1893 THR A CA    1 
ATOM   2871  C  C     . THR A 1 1893 ? 211.610 221.879 188.067 1.00 4.10   ? 1893 THR A C     1 
ATOM   2872  O  O     . THR A 1 1893 ? 210.494 221.381 187.875 1.00 4.95   ? 1893 THR A O     1 
ATOM   2873  C  CB    . THR A 1 1893 ? 212.124 224.004 186.828 1.00 4.91   ? 1893 THR A CB    1 
ATOM   2874  O  OG1   . THR A 1 1893 ? 213.510 223.772 186.546 1.00 6.74   ? 1893 THR A OG1   1 
ATOM   2875  C  CG2   . THR A 1 1893 ? 211.853 225.499 186.836 1.00 3.25   ? 1893 THR A CG2   1 
ATOM   2876  N  N     . GLN A 1 1894 ? 212.712 221.134 188.185 1.00 4.37   ? 1894 GLN A N     1 
ATOM   2877  C  CA    . GLN A 1 1894 ? 212.615 219.679 188.220 1.00 4.05   ? 1894 GLN A CA    1 
ATOM   2878  C  C     . GLN A 1 1894 ? 211.822 219.213 189.433 1.00 5.20   ? 1894 GLN A C     1 
ATOM   2879  O  O     . GLN A 1 1894 ? 211.020 218.277 189.337 1.00 7.62   ? 1894 GLN A O     1 
ATOM   2880  C  CB    . GLN A 1 1894 ? 214.011 219.057 188.220 1.00 4.23   ? 1894 GLN A CB    1 
ATOM   2881  C  CG    . GLN A 1 1894 ? 214.704 219.083 186.871 1.00 4.01   ? 1894 GLN A CG    1 
ATOM   2882  C  CD    . GLN A 1 1894 ? 213.872 218.443 185.781 1.00 5.95   ? 1894 GLN A CD    1 
ATOM   2883  O  OE1   . GLN A 1 1894 ? 213.618 217.240 185.805 1.00 8.20   ? 1894 GLN A OE1   1 
ATOM   2884  N  NE2   . GLN A 1 1894 ? 213.439 219.247 184.819 1.00 9.70   ? 1894 GLN A NE2   1 
ATOM   2885  N  N     . ALA A 1 1895 ? 212.042 219.850 190.585 1.00 4.98   ? 1895 ALA A N     1 
ATOM   2886  C  CA    . ALA A 1 1895 ? 211.261 219.521 191.773 1.00 4.47   ? 1895 ALA A CA    1 
ATOM   2887  C  C     . ALA A 1 1895 ? 209.784 219.841 191.573 1.00 4.62   ? 1895 ALA A C     1 
ATOM   2888  O  O     . ALA A 1 1895 ? 208.912 219.069 191.986 1.00 7.96   ? 1895 ALA A O     1 
ATOM   2889  C  CB    . ALA A 1 1895 ? 211.810 220.269 192.986 1.00 4.33   ? 1895 ALA A CB    1 
ATOM   2890  N  N     . LEU A 1 1896 ? 209.488 220.981 190.948 1.00 4.90   ? 1896 LEU A N     1 
ATOM   2891  C  CA    . LEU A 1 1896 ? 208.101 221.368 190.713 1.00 4.56   ? 1896 LEU A CA    1 
ATOM   2892  C  C     . LEU A 1 1896 ? 207.405 220.393 189.774 1.00 7.96   ? 1896 LEU A C     1 
ATOM   2893  O  O     . LEU A 1 1896 ? 206.237 220.046 189.984 1.00 12.17  ? 1896 LEU A O     1 
ATOM   2894  C  CB    . LEU A 1 1896 ? 208.042 222.786 190.145 1.00 3.67   ? 1896 LEU A CB    1 
ATOM   2895  C  CG    . LEU A 1 1896 ? 208.380 223.931 191.098 1.00 3.56   ? 1896 LEU A CG    1 
ATOM   2896  C  CD1   . LEU A 1 1896 ? 208.581 225.216 190.318 1.00 5.36   ? 1896 LEU A CD1   1 
ATOM   2897  C  CD2   . LEU A 1 1896 ? 207.294 224.098 192.136 1.00 2.70   ? 1896 LEU A CD2   1 
ATOM   2898  N  N     . GLU A 1 1897 ? 208.102 219.950 188.725 1.00 7.28   ? 1897 GLU A N     1 
ATOM   2899  C  CA    . GLU A 1 1897 ? 207.519 218.969 187.816 1.00 7.58   ? 1897 GLU A CA    1 
ATOM   2900  C  C     . GLU A 1 1897 ? 207.234 217.657 188.536 1.00 10.47  ? 1897 GLU A C     1 
ATOM   2901  O  O     . GLU A 1 1897 ? 206.242 216.979 188.243 1.00 15.79  ? 1897 GLU A O     1 
ATOM   2902  C  CB    . GLU A 1 1897 ? 208.446 218.743 186.621 1.00 10.13  ? 1897 GLU A CB    1 
ATOM   2903  C  CG    . GLU A 1 1897 ? 207.909 217.761 185.593 1.00 12.39  ? 1897 GLU A CG    1 
ATOM   2904  C  CD    . GLU A 1 1897 ? 207.054 218.424 184.532 1.00 26.20  ? 1897 GLU A CD    1 
ATOM   2905  O  OE1   . GLU A 1 1897 ? 206.435 219.470 184.824 1.00 29.33  ? 1897 GLU A OE1   1 
ATOM   2906  O  OE2   . GLU A 1 1897 ? 206.992 217.895 183.403 1.00 29.54  ? 1897 GLU A OE2   1 
ATOM   2907  N  N     . ALA A 1 1898 ? 208.089 217.287 189.487 1.00 9.04   ? 1898 ALA A N     1 
ATOM   2908  C  CA    . ALA A 1 1898 ? 207.866 216.114 190.319 1.00 8.32   ? 1898 ALA A CA    1 
ATOM   2909  C  C     . ALA A 1 1898 ? 206.817 216.347 191.397 1.00 12.51  ? 1898 ALA A C     1 
ATOM   2910  O  O     . ALA A 1 1898 ? 206.547 215.431 192.182 1.00 19.97  ? 1898 ALA A O     1 
ATOM   2911  C  CB    . ALA A 1 1898 ? 209.180 215.671 190.964 1.00 8.00   ? 1898 ALA A CB    1 
ATOM   2912  N  N     . ARG A 1 1899 ? 206.230 217.546 191.453 1.00 10.52  ? 1899 ARG A N     1 
ATOM   2913  C  CA    . ARG A 1 1899 ? 205.203 217.895 192.437 1.00 13.88  ? 1899 ARG A CA    1 
ATOM   2914  C  C     . ARG A 1 1899 ? 205.719 217.722 193.863 1.00 12.20  ? 1899 ARG A C     1 
ATOM   2915  O  O     . ARG A 1 1899 ? 205.002 217.263 194.753 1.00 16.52  ? 1899 ARG A O     1 
ATOM   2916  C  CB    . ARG A 1 1899 ? 203.921 217.088 192.212 1.00 12.97  ? 1899 ARG A CB    1 
ATOM   2917  C  CG    . ARG A 1 1899 ? 202.941 217.752 191.259 1.00 11.74  ? 1899 ARG A CG    1 
ATOM   2918  C  CD    . ARG A 1 1899 ? 203.376 217.562 189.818 1.00 16.96  ? 1899 ARG A CD    1 
ATOM   2919  N  NE    . ARG A 1 1899 ? 202.800 218.560 188.925 1.00 24.66  ? 1899 ARG A NE    1 
ATOM   2920  C  CZ    . ARG A 1 1899 ? 203.024 218.613 187.620 1.00 21.23  ? 1899 ARG A CZ    1 
ATOM   2921  N  NH1   . ARG A 1 1899 ? 203.822 217.745 187.021 1.00 20.09  ? 1899 ARG A NH1   1 
ATOM   2922  N  NH2   . ARG A 1 1899 ? 202.436 219.562 186.898 1.00 17.76  ? 1899 ARG A NH2   1 
ATOM   2923  N  N     . LEU A 1 1900 ? 206.977 218.097 194.078 1.00 6.99   ? 1900 LEU A N     1 
ATOM   2924  C  CA    . LEU A 1 1900 ? 207.588 218.077 195.397 1.00 7.48   ? 1900 LEU A CA    1 
ATOM   2925  C  C     . LEU A 1 1900 ? 208.376 219.365 195.591 1.00 6.51   ? 1900 LEU A C     1 
ATOM   2926  O  O     . LEU A 1 1900 ? 208.771 220.026 194.629 1.00 9.82   ? 1900 LEU A O     1 
ATOM   2927  C  CB    . LEU A 1 1900 ? 208.461 216.824 195.587 1.00 7.99   ? 1900 LEU A CB    1 
ATOM   2928  C  CG    . LEU A 1 1900 ? 209.676 216.542 194.698 1.00 8.03   ? 1900 LEU A CG    1 
ATOM   2929  C  CD1   . LEU A 1 1900 ? 210.918 217.274 195.164 1.00 9.45   ? 1900 LEU A CD1   1 
ATOM   2930  C  CD2   . LEU A 1 1900 ? 209.936 215.048 194.637 1.00 8.66   ? 1900 LEU A CD2   1 
ATOM   2931  N  N     . GLY A 1 1901 ? 208.587 219.722 196.851 1.00 6.10   ? 1901 GLY A N     1 
ATOM   2932  C  CA    . GLY A 1 1901 ? 209.173 221.005 197.176 1.00 4.75   ? 1901 GLY A CA    1 
ATOM   2933  C  C     . GLY A 1 1901 ? 210.655 221.080 196.869 1.00 4.80   ? 1901 GLY A C     1 
ATOM   2934  O  O     . GLY A 1 1901 ? 211.314 220.097 196.537 1.00 6.39   ? 1901 GLY A O     1 
ATOM   2935  N  N     . GLY A 1 1902 ? 211.190 222.289 196.987 1.00 3.37   ? 1902 GLY A N     1 
ATOM   2936  C  CA    . GLY A 1 1902 ? 212.605 222.551 196.761 1.00 2.49   ? 1902 GLY A CA    1 
ATOM   2937  C  C     . GLY A 1 1902 ? 213.274 222.993 198.050 1.00 2.78   ? 1902 GLY A C     1 
ATOM   2938  O  O     . GLY A 1 1902 ? 212.675 223.716 198.851 1.00 4.27   ? 1902 GLY A O     1 
ATOM   2939  N  N     . SER A 1 1903 ? 214.516 222.557 198.244 1.00 3.42   ? 1903 SER A N     1 
ATOM   2940  C  CA    . SER A 1 1903 ? 215.278 222.836 199.460 1.00 2.98   ? 1903 SER A CA    1 
ATOM   2941  C  C     . SER A 1 1903 ? 216.671 223.326 199.084 1.00 3.61   ? 1903 SER A C     1 
ATOM   2942  O  O     . SER A 1 1903 ? 217.623 222.538 199.013 1.00 4.70   ? 1903 SER A O     1 
ATOM   2943  C  CB    . SER A 1 1903 ? 215.356 221.598 200.353 1.00 3.12   ? 1903 SER A CB    1 
ATOM   2944  O  OG    . SER A 1 1903 ? 216.320 221.768 201.375 1.00 8.39   ? 1903 SER A OG    1 
ATOM   2945  N  N     . PRO A 1 1904 ? 216.822 224.621 198.800 1.00 3.83   ? 1904 PRO A N     1 
ATOM   2946  C  CA    . PRO A 1 1904 ? 218.171 225.186 198.651 1.00 3.61   ? 1904 PRO A CA    1 
ATOM   2947  C  C     . PRO A 1 1904 ? 218.806 225.387 200.019 1.00 4.49   ? 1904 PRO A C     1 
ATOM   2948  O  O     . PRO A 1 1904 ? 218.249 226.069 200.883 1.00 6.07   ? 1904 PRO A O     1 
ATOM   2949  C  CB    . PRO A 1 1904 ? 217.922 226.519 197.938 1.00 3.28   ? 1904 PRO A CB    1 
ATOM   2950  C  CG    . PRO A 1 1904 ? 216.520 226.863 198.249 1.00 3.59   ? 1904 PRO A CG    1 
ATOM   2951  C  CD    . PRO A 1 1904 ? 215.773 225.576 198.408 1.00 4.08   ? 1904 PRO A CD    1 
ATOM   2952  N  N     . PHE A 1 1905 ? 219.975 224.771 200.209 1.00 4.51   ? 1905 PHE A N     1 
ATOM   2953  C  CA    . PHE A 1 1905 ? 220.690 224.873 201.508 1.00 4.19   ? 1905 PHE A CA    1 
ATOM   2954  C  C     . PHE A 1 1905 ? 222.092 225.408 201.255 1.00 4.05   ? 1905 PHE A C     1 
ATOM   2955  O  O     . PHE A 1 1905 ? 222.560 225.373 200.097 1.00 3.74   ? 1905 PHE A O     1 
ATOM   2956  C  CB    . PHE A 1 1905 ? 220.731 223.488 202.157 1.00 4.27   ? 1905 PHE A CB    1 
ATOM   2957  C  CG    . PHE A 1 1905 ? 221.418 222.422 201.314 1.00 3.75   ? 1905 PHE A CG    1 
ATOM   2958  C  CD1   . PHE A 1 1905 ? 220.697 221.654 200.407 1.00 3.42   ? 1905 PHE A CD1   1 
ATOM   2959  C  CD2   . PHE A 1 1905 ? 222.784 222.191 201.429 1.00 2.84   ? 1905 PHE A CD2   1 
ATOM   2960  C  CE1   . PHE A 1 1905 ? 221.324 220.685 199.641 1.00 3.75   ? 1905 PHE A CE1   1 
ATOM   2961  C  CE2   . PHE A 1 1905 ? 223.407 221.221 200.660 1.00 3.25   ? 1905 PHE A CE2   1 
ATOM   2962  C  CZ    . PHE A 1 1905 ? 222.677 220.470 199.768 1.00 3.46   ? 1905 PHE A CZ    1 
ATOM   2963  N  N     . GLY A 1 1906 ? 222.751 225.891 202.309 1.00 6.61   ? 1906 GLY A N     1 
ATOM   2964  C  CA    . GLY A 1 1906 ? 224.120 226.420 202.171 1.00 6.45   ? 1906 GLY A CA    1 
ATOM   2965  C  C     . GLY A 1 1906 ? 224.407 227.480 203.211 1.00 5.40   ? 1906 GLY A C     1 
ATOM   2966  O  O     . GLY A 1 1906 ? 223.560 227.677 204.107 1.00 7.49   ? 1906 GLY A O     1 
ATOM   2967  N  N     . PRO A 1 1907 ? 225.566 228.184 203.181 1.00 4.91   ? 1907 PRO A N     1 
ATOM   2968  C  CA    . PRO A 1 1907 ? 225.808 229.261 204.129 1.00 5.91   ? 1907 PRO A CA    1 
ATOM   2969  C  C     . PRO A 1 1907 ? 224.953 230.483 203.836 1.00 8.62   ? 1907 PRO A C     1 
ATOM   2970  O  O     . PRO A 1 1907 ? 224.342 230.561 202.753 1.00 9.98   ? 1907 PRO A O     1 
ATOM   2971  C  CB    . PRO A 1 1907 ? 227.304 229.550 203.957 1.00 5.56   ? 1907 PRO A CB    1 
ATOM   2972  C  CG    . PRO A 1 1907 ? 227.577 229.197 202.516 1.00 6.09   ? 1907 PRO A CG    1 
ATOM   2973  C  CD    . PRO A 1 1907 ? 226.697 227.987 202.266 1.00 4.00   ? 1907 PRO A CD    1 
ATOM   2974  N  N     . ALA A 1 1908 ? 224.910 231.424 204.782 1.00 10.76  ? 1908 ALA A N     1 
ATOM   2975  C  CA    . ALA A 1 1908 ? 224.090 232.645 204.604 1.00 10.57  ? 1908 ALA A CA    1 
ATOM   2976  C  C     . ALA A 1 1908 ? 224.744 233.565 203.575 1.00 7.56   ? 1908 ALA A C     1 
ATOM   2977  O  O     . ALA A 1 1908 ? 225.990 233.617 203.522 1.00 11.60  ? 1908 ALA A O     1 
ATOM   2978  C  CB    . ALA A 1 1908 ? 223.924 233.345 205.930 1.00 11.24  ? 1908 ALA A CB    1 
ATOM   2979  N  N     . GLY A 1 1909 ? 223.931 234.272 202.787 1.00 6.28   ? 1909 GLY A N     1 
ATOM   2980  C  CA    . GLY A 1 1909 ? 224.474 235.228 201.802 1.00 5.61   ? 1909 GLY A CA    1 
ATOM   2981  C  C     . GLY A 1 1909 ? 224.779 234.571 200.470 1.00 6.93   ? 1909 GLY A C     1 
ATOM   2982  O  O     . GLY A 1 1909 ? 225.486 235.196 199.658 1.00 11.54  ? 1909 GLY A O     1 
ATOM   2983  N  N     . THR A 1 1910 ? 224.271 233.357 200.243 1.00 7.13   ? 1910 THR A N     1 
ATOM   2984  C  CA    . THR A 1 1910 ? 224.468 232.687 198.940 1.00 5.61   ? 1910 THR A CA    1 
ATOM   2985  C  C     . THR A 1 1910 ? 223.277 232.968 198.050 1.00 6.21   ? 1910 THR A C     1 
ATOM   2986  O  O     . THR A 1 1910 ? 223.280 232.489 196.897 1.00 11.85  ? 1910 THR A O     1 
ATOM   2987  C  CB    . THR A 1 1910 ? 224.685 231.192 199.158 1.00 5.50   ? 1910 THR A CB    1 
ATOM   2988  O  OG1   . THR A 1 1910 ? 223.640 230.786 200.035 1.00 6.79   ? 1910 THR A OG1   1 
ATOM   2989  C  CG2   . THR A 1 1910 ? 226.030 230.897 199.794 1.00 4.64   ? 1910 THR A CG2   1 
ATOM   2990  N  N     . GLY A 1 1911 ? 222.295 233.723 198.550 1.00 5.71   ? 1911 GLY A N     1 
ATOM   2991  C  CA    . GLY A 1 1911 ? 221.134 234.109 197.724 1.00 5.10   ? 1911 GLY A CA    1 
ATOM   2992  C  C     . GLY A 1 1911 ? 220.166 232.962 197.517 1.00 4.88   ? 1911 GLY A C     1 
ATOM   2993  O  O     . GLY A 1 1911 ? 219.539 232.909 196.440 1.00 7.34   ? 1911 GLY A O     1 
ATOM   2994  N  N     . LYS A 1 1912 ? 220.038 232.077 198.507 1.00 4.07   ? 1912 LYS A N     1 
ATOM   2995  C  CA    . LYS A 1 1912 ? 219.079 230.948 198.408 1.00 3.79   ? 1912 LYS A CA    1 
ATOM   2996  C  C     . LYS A 1 1912 ? 217.648 231.502 198.340 1.00 5.47   ? 1912 LYS A C     1 
ATOM   2997  O  O     . LYS A 1 1912 ? 216.897 231.082 197.436 1.00 8.42   ? 1912 LYS A O     1 
ATOM   2998  C  CB    . LYS A 1 1912 ? 219.255 230.013 199.607 1.00 4.21   ? 1912 LYS A CB    1 
ATOM   2999  C  CG    . LYS A 1 1912 ? 220.647 229.418 199.739 1.00 3.61   ? 1912 LYS A CG    1 
ATOM   3000  C  CD    . LYS A 1 1912 ? 220.805 228.555 200.983 1.00 4.97   ? 1912 LYS A CD    1 
ATOM   3001  C  CE    . LYS A 1 1912 ? 220.564 229.322 202.241 1.00 4.71   ? 1912 LYS A CE    1 
ATOM   3002  N  NZ    . LYS A 1 1912 ? 221.580 230.357 202.444 1.00 4.62   ? 1912 LYS A NZ    1 
ATOM   3003  N  N     . THR A 1 1913 ? 217.295 232.415 199.248 1.00 4.36   ? 1913 THR A N     1 
ATOM   3004  C  CA    . THR A 1 1913 ? 215.919 232.958 199.287 1.00 4.94   ? 1913 THR A CA    1 
ATOM   3005  C  C     . THR A 1 1913 ? 215.656 233.767 198.037 1.00 6.06   ? 1913 THR A C     1 
ATOM   3006  O  O     . THR A 1 1913 ? 214.628 233.514 197.377 1.00 6.97   ? 1913 THR A O     1 
ATOM   3007  C  CB    . THR A 1 1913 ? 215.739 233.807 200.543 1.00 7.11   ? 1913 THR A CB    1 
ATOM   3008  O  OG1   . THR A 1 1913 ? 215.784 232.881 201.623 1.00 18.27  ? 1913 THR A OG1   1 
ATOM   3009  C  CG2   . THR A 1 1913 ? 214.420 234.559 200.551 1.00 10.58  ? 1913 THR A CG2   1 
ATOM   3010  N  N     . GLU A 1 1914 ? 216.548 234.703 197.709 1.00 6.65   ? 1914 GLU A N     1 
ATOM   3011  C  CA    . GLU A 1 1914 ? 216.312 235.593 196.544 1.00 3.90   ? 1914 GLU A CA    1 
ATOM   3012  C  C     . GLU A 1 1914 ? 216.085 234.737 195.291 1.00 3.80   ? 1914 GLU A C     1 
ATOM   3013  O  O     . GLU A 1 1914 ? 215.172 235.068 194.508 1.00 4.96   ? 1914 GLU A O     1 
ATOM   3014  C  CB    . GLU A 1 1914 ? 217.488 236.550 196.359 1.00 9.57   ? 1914 GLU A CB    1 
ATOM   3015  C  CG    . GLU A 1 1914 ? 217.619 237.569 197.487 1.00 14.21  ? 1914 GLU A CG    1 
ATOM   3016  C  CD    . GLU A 1 1914 ? 216.371 238.395 197.737 1.00 17.15  ? 1914 GLU A CD    1 
ATOM   3017  O  OE1   . GLU A 1 1914 ? 215.924 239.089 196.799 1.00 18.17  ? 1914 GLU A OE1   1 
ATOM   3018  O  OE2   . GLU A 1 1914 ? 215.849 238.350 198.871 1.00 14.85  ? 1914 GLU A OE2   1 
ATOM   3019  N  N     . SER A 1 1915 ? 216.874 233.676 195.119 1.00 4.09   ? 1915 SER A N     1 
ATOM   3020  C  CA    . SER A 1 1915 ? 216.766 232.827 193.905 1.00 2.56   ? 1915 SER A CA    1 
ATOM   3021  C  C     . SER A 1 1915 ? 215.369 232.197 193.843 1.00 2.62   ? 1915 SER A C     1 
ATOM   3022  O  O     . SER A 1 1915 ? 214.797 232.135 192.735 1.00 2.93   ? 1915 SER A O     1 
ATOM   3023  C  CB    . SER A 1 1915 ? 217.842 231.775 193.865 1.00 3.21   ? 1915 SER A CB    1 
ATOM   3024  O  OG    . SER A 1 1915 ? 219.122 232.365 193.693 1.00 6.76   ? 1915 SER A OG    1 
ATOM   3025  N  N     . VAL A 1 1916 ? 214.845 231.753 194.988 1.00 3.65   ? 1916 VAL A N     1 
ATOM   3026  C  CA    . VAL A 1 1916 ? 213.492 231.200 195.004 1.00 3.37   ? 1916 VAL A CA    1 
ATOM   3027  C  C     . VAL A 1 1916 ? 212.474 232.272 194.629 1.00 3.69   ? 1916 VAL A C     1 
ATOM   3028  O  O     . VAL A 1 1916 ? 211.565 232.033 193.823 1.00 5.42   ? 1916 VAL A O     1 
ATOM   3029  C  CB    . VAL A 1 1916 ? 213.185 230.573 196.377 1.00 2.93   ? 1916 VAL A CB    1 
ATOM   3030  C  CG1   . VAL A 1 1916 ? 211.709 230.239 196.492 1.00 3.00   ? 1916 VAL A CG1   1 
ATOM   3031  C  CG2   . VAL A 1 1916 ? 214.028 229.331 196.585 1.00 4.20   ? 1916 VAL A CG2   1 
ATOM   3032  N  N     . LYS A 1 1917 ? 212.620 233.472 195.196 1.00 3.26   ? 1917 LYS A N     1 
ATOM   3033  C  CA    . LYS A 1 1917 ? 211.707 234.561 194.862 1.00 3.04   ? 1917 LYS A CA    1 
ATOM   3034  C  C     . LYS A 1 1917 ? 211.828 234.958 193.396 1.00 3.29   ? 1917 LYS A C     1 
ATOM   3035  O  O     . LYS A 1 1917 ? 210.824 235.272 192.747 1.00 6.36   ? 1917 LYS A O     1 
ATOM   3036  C  CB    . LYS A 1 1917 ? 211.970 235.766 195.763 1.00 4.34   ? 1917 LYS A CB    1 
ATOM   3037  C  CG    . LYS A 1 1917 ? 211.485 235.591 197.187 1.00 5.83   ? 1917 LYS A CG    1 
ATOM   3038  C  CD    . LYS A 1 1917 ? 211.281 236.933 197.866 1.00 8.01   ? 1917 LYS A CD    1 
ATOM   3039  C  CE    . LYS A 1 1917 ? 212.523 237.795 197.780 1.00 7.54   ? 1917 LYS A CE    1 
ATOM   3040  N  NZ    . LYS A 1 1917 ? 212.332 239.106 198.461 1.00 11.22  ? 1917 LYS A NZ    1 
ATOM   3041  N  N     . ALA A 1 1918 ? 213.049 234.962 192.860 1.00 2.56   ? 1918 ALA A N     1 
ATOM   3042  C  CA    . ALA A 1 1918 ? 213.255 235.313 191.460 1.00 2.29   ? 1918 ALA A CA    1 
ATOM   3043  C  C     . ALA A 1 1918 ? 212.617 234.290 190.533 1.00 3.09   ? 1918 ALA A C     1 
ATOM   3044  O  O     . ALA A 1 1918 ? 212.023 234.656 189.514 1.00 5.75   ? 1918 ALA A O     1 
ATOM   3045  C  CB    . ALA A 1 1918 ? 214.749 235.442 191.169 1.00 1.56   ? 1918 ALA A CB    1 
ATOM   3046  N  N     . LEU A 1 1919 ? 212.735 233.003 190.863 1.00 2.60   ? 1919 LEU A N     1 
ATOM   3047  C  CA    . LEU A 1 1919 ? 212.070 231.983 190.060 1.00 2.76   ? 1919 LEU A CA    1 
ATOM   3048  C  C     . LEU A 1 1919 ? 210.555 232.115 190.153 1.00 3.51   ? 1919 LEU A C     1 
ATOM   3049  O  O     . LEU A 1 1919 ? 209.849 231.934 189.155 1.00 3.89   ? 1919 LEU A O     1 
ATOM   3050  C  CB    . LEU A 1 1919 ? 212.519 230.589 190.491 1.00 3.32   ? 1919 LEU A CB    1 
ATOM   3051  C  CG    . LEU A 1 1919 ? 211.843 229.445 189.733 1.00 2.73   ? 1919 LEU A CG    1 
ATOM   3052  C  CD1   . LEU A 1 1919 ? 212.137 229.550 188.248 1.00 3.07   ? 1919 LEU A CD1   1 
ATOM   3053  C  CD2   . LEU A 1 1919 ? 212.282 228.102 190.273 1.00 1.91   ? 1919 LEU A CD2   1 
ATOM   3054  N  N     . GLY A 1 1920 ? 210.039 232.426 191.343 1.00 3.95   ? 1920 GLY A N     1 
ATOM   3055  C  CA    . GLY A 1 1920 ? 208.607 232.638 191.479 1.00 3.90   ? 1920 GLY A CA    1 
ATOM   3056  C  C     . GLY A 1 1920 ? 208.110 233.820 190.668 1.00 4.92   ? 1920 GLY A C     1 
ATOM   3057  O  O     . GLY A 1 1920 ? 207.044 233.759 190.051 1.00 6.80   ? 1920 GLY A O     1 
ATOM   3058  N  N     . HIS A 1 1921 ? 208.876 234.914 190.660 1.00 4.75   ? 1921 HIS A N     1 
ATOM   3059  C  CA    . HIS A 1 1921 ? 208.501 236.080 189.870 1.00 4.31   ? 1921 HIS A CA    1 
ATOM   3060  C  C     . HIS A 1 1921 ? 208.658 235.820 188.378 1.00 5.16   ? 1921 HIS A C     1 
ATOM   3061  O  O     . HIS A 1 1921 ? 207.948 236.424 187.567 1.00 7.76   ? 1921 HIS A O     1 
ATOM   3062  C  CB    . HIS A 1 1921 ? 209.334 237.290 190.290 1.00 5.30   ? 1921 HIS A CB    1 
ATOM   3063  C  CG    . HIS A 1 1921 ? 209.154 237.679 191.723 1.00 13.68  ? 1921 HIS A CG    1 
ATOM   3064  N  ND1   . HIS A 1 1921 ? 208.080 237.261 192.479 1.00 14.90  ? 1921 HIS A ND1   1 
ATOM   3065  C  CD2   . HIS A 1 1921 ? 209.917 238.439 192.543 1.00 15.92  ? 1921 HIS A CD2   1 
ATOM   3066  C  CE1   . HIS A 1 1921 ? 208.186 237.752 193.700 1.00 13.61  ? 1921 HIS A CE1   1 
ATOM   3067  N  NE2   . HIS A 1 1921 ? 209.292 238.470 193.766 1.00 19.35  ? 1921 HIS A NE2   1 
ATOM   3068  N  N     . GLN A 1 1922 ? 209.583 234.936 188.000 1.00 4.33   ? 1922 GLN A N     1 
ATOM   3069  C  CA    . GLN A 1 1922 ? 209.744 234.583 186.594 1.00 3.25   ? 1922 GLN A CA    1 
ATOM   3070  C  C     . GLN A 1 1922 ? 208.511 233.877 186.050 1.00 5.05   ? 1922 GLN A C     1 
ATOM   3071  O  O     . GLN A 1 1922 ? 208.148 234.068 184.884 1.00 6.26   ? 1922 GLN A O     1 
ATOM   3072  C  CB    . GLN A 1 1922 ? 210.984 233.710 186.414 1.00 3.47   ? 1922 GLN A CB    1 
ATOM   3073  C  CG    . GLN A 1 1922 ? 211.208 233.225 184.994 1.00 6.41   ? 1922 GLN A CG    1 
ATOM   3074  C  CD    . GLN A 1 1922 ? 211.603 234.338 184.048 1.00 6.46   ? 1922 GLN A CD    1 
ATOM   3075  O  OE1   . GLN A 1 1922 ? 212.780 234.668 183.917 1.00 7.82   ? 1922 GLN A OE1   1 
ATOM   3076  N  NE2   . GLN A 1 1922 ? 210.618 234.924 183.380 1.00 7.57   ? 1922 GLN A NE2   1 
ATOM   3077  N  N     . LEU A 1 1923 ? 207.855 233.063 186.872 1.00 4.76   ? 1923 LEU A N     1 
ATOM   3078  C  CA    . LEU A 1 1923 ? 206.647 232.356 186.479 1.00 4.02   ? 1923 LEU A CA    1 
ATOM   3079  C  C     . LEU A 1 1923 ? 205.378 233.135 186.804 1.00 6.48   ? 1923 LEU A C     1 
ATOM   3080  O  O     . LEU A 1 1923 ? 204.278 232.596 186.651 1.00 8.86   ? 1923 LEU A O     1 
ATOM   3081  C  CB    . LEU A 1 1923 ? 206.601 230.979 187.147 1.00 4.18   ? 1923 LEU A CB    1 
ATOM   3082  C  CG    . LEU A 1 1923 ? 207.862 230.124 187.005 1.00 3.33   ? 1923 LEU A CG    1 
ATOM   3083  C  CD1   . LEU A 1 1923 ? 207.741 228.843 187.807 1.00 3.72   ? 1923 LEU A CD1   1 
ATOM   3084  C  CD2   . LEU A 1 1923 ? 208.144 229.816 185.546 1.00 3.82   ? 1923 LEU A CD2   1 
ATOM   3085  N  N     . GLY A 1 1924 ? 205.507 234.380 187.248 1.00 5.78   ? 1924 GLY A N     1 
ATOM   3086  C  CA    . GLY A 1 1924 ? 204.350 235.183 187.598 1.00 6.12   ? 1924 GLY A CA    1 
ATOM   3087  C  C     . GLY A 1 1924 ? 203.592 234.666 188.800 1.00 8.31   ? 1924 GLY A C     1 
ATOM   3088  O  O     . GLY A 1 1924 ? 202.361 234.776 188.848 1.00 10.24  ? 1924 GLY A O     1 
ATOM   3089  N  N     . ARG A 1 1925 ? 204.298 234.111 189.777 1.00 8.42   ? 1925 ARG A N     1 
ATOM   3090  C  CA    . ARG A 1 1925 ? 203.681 233.540 190.961 1.00 5.63   ? 1925 ARG A CA    1 
ATOM   3091  C  C     . ARG A 1 1925 ? 203.732 234.527 192.119 1.00 7.71   ? 1925 ARG A C     1 
ATOM   3092  O  O     . ARG A 1 1925 ? 204.592 235.408 192.184 1.00 6.31   ? 1925 ARG A O     1 
ATOM   3093  C  CB    . ARG A 1 1925 ? 204.374 232.233 191.356 1.00 4.78   ? 1925 ARG A CB    1 
ATOM   3094  C  CG    . ARG A 1 1925 ? 204.251 231.132 190.321 1.00 4.80   ? 1925 ARG A CG    1 
ATOM   3095  C  CD    . ARG A 1 1925 ? 202.803 230.733 190.111 1.00 7.63   ? 1925 ARG A CD    1 
ATOM   3096  N  NE    . ARG A 1 1925 ? 202.684 229.440 189.450 1.00 9.32   ? 1925 ARG A NE    1 
ATOM   3097  C  CZ    . ARG A 1 1925 ? 202.817 229.248 188.145 1.00 11.90  ? 1925 ARG A CZ    1 
ATOM   3098  N  NH1   . ARG A 1 1925 ? 203.071 230.252 187.323 1.00 10.52  ? 1925 ARG A NH1   1 
ATOM   3099  N  NH2   . ARG A 1 1925 ? 202.693 228.020 187.654 1.00 18.64  ? 1925 ARG A NH2   1 
ATOM   3100  N  N     . PHE A 1 1926 ? 202.785 234.366 193.038 1.00 7.35   ? 1926 PHE A N     1 
ATOM   3101  C  CA    . PHE A 1 1926 ? 202.708 235.174 194.250 1.00 7.24   ? 1926 PHE A CA    1 
ATOM   3102  C  C     . PHE A 1 1926 ? 203.507 234.446 195.326 1.00 8.17   ? 1926 PHE A C     1 
ATOM   3103  O  O     . PHE A 1 1926 ? 203.086 233.404 195.833 1.00 7.72   ? 1926 PHE A O     1 
ATOM   3104  C  CB    . PHE A 1 1926 ? 201.250 235.400 194.641 1.00 8.08   ? 1926 PHE A CB    1 
ATOM   3105  C  CG    . PHE A 1 1926 ? 201.062 236.136 195.938 1.00 10.14  ? 1926 PHE A CG    1 
ATOM   3106  C  CD1   . PHE A 1 1926 ? 201.992 237.061 196.376 1.00 11.31  ? 1926 PHE A CD1   1 
ATOM   3107  C  CD2   . PHE A 1 1926 ? 199.917 235.945 196.690 1.00 11.08  ? 1926 PHE A CD2   1 
ATOM   3108  C  CE1   . PHE A 1 1926 ? 201.805 237.744 197.560 1.00 12.95  ? 1926 PHE A CE1   1 
ATOM   3109  C  CE2   . PHE A 1 1926 ? 199.721 236.632 197.868 1.00 13.56  ? 1926 PHE A CE2   1 
ATOM   3110  C  CZ    . PHE A 1 1926 ? 200.667 237.531 198.304 1.00 14.72  ? 1926 PHE A CZ    1 
ATOM   3111  N  N     . VAL A 1 1927 ? 204.671 234.995 195.661 1.00 7.13   ? 1927 VAL A N     1 
ATOM   3112  C  CA    . VAL A 1 1927 ? 205.601 234.377 196.598 1.00 4.97   ? 1927 VAL A CA    1 
ATOM   3113  C  C     . VAL A 1 1927 ? 205.502 235.098 197.934 1.00 8.19   ? 1927 VAL A C     1 
ATOM   3114  O  O     . VAL A 1 1927 ? 205.625 236.327 197.996 1.00 17.41  ? 1927 VAL A O     1 
ATOM   3115  C  CB    . VAL A 1 1927 ? 207.042 234.416 196.061 1.00 4.56   ? 1927 VAL A CB    1 
ATOM   3116  C  CG1   . VAL A 1 1927 ? 207.970 233.638 196.976 1.00 6.10   ? 1927 VAL A CG1   1 
ATOM   3117  C  CG2   . VAL A 1 1927 ? 207.097 233.867 194.648 1.00 5.15   ? 1927 VAL A CG2   1 
ATOM   3118  N  N     . LEU A 1 1928 ? 205.279 234.335 199.001 1.00 5.82   ? 1928 LEU A N     1 
ATOM   3119  C  CA    . LEU A 1 1928 ? 205.265 234.859 200.361 1.00 6.28   ? 1928 LEU A CA    1 
ATOM   3120  C  C     . LEU A 1 1928 ? 206.409 234.217 201.130 1.00 6.67   ? 1928 LEU A C     1 
ATOM   3121  O  O     . LEU A 1 1928 ? 206.545 232.989 201.134 1.00 8.92   ? 1928 LEU A O     1 
ATOM   3122  C  CB    . LEU A 1 1928 ? 203.930 234.588 201.064 1.00 7.33   ? 1928 LEU A CB    1 
ATOM   3123  C  CG    . LEU A 1 1928 ? 202.637 235.186 200.504 1.00 7.18   ? 1928 LEU A CG    1 
ATOM   3124  C  CD1   . LEU A 1 1928 ? 202.116 234.399 199.312 1.00 7.02   ? 1928 LEU A CD1   1 
ATOM   3125  C  CD2   . LEU A 1 1928 ? 201.579 235.279 201.590 1.00 7.33   ? 1928 LEU A CD2   1 
ATOM   3126  N  N     . VAL A 1 1929 ? 207.224 235.040 201.770 1.00 7.48   ? 1929 VAL A N     1 
ATOM   3127  C  CA    . VAL A 1 1929 ? 208.354 234.562 202.555 1.00 7.38   ? 1929 VAL A CA    1 
ATOM   3128  C  C     . VAL A 1 1929 ? 207.951 234.539 204.023 1.00 8.44   ? 1929 VAL A C     1 
ATOM   3129  O  O     . VAL A 1 1929 ? 207.459 235.538 204.559 1.00 8.92   ? 1929 VAL A O     1 
ATOM   3130  C  CB    . VAL A 1 1929 ? 209.593 235.446 202.335 1.00 9.42   ? 1929 VAL A CB    1 
ATOM   3131  C  CG1   . VAL A 1 1929 ? 210.686 235.081 203.318 1.00 11.93  ? 1929 VAL A CG1   1 
ATOM   3132  C  CG2   . VAL A 1 1929 ? 210.094 235.304 200.910 1.00 6.74   ? 1929 VAL A CG2   1 
ATOM   3133  N  N     . PHE A 1 1930 ? 208.149 233.394 204.668 1.00 8.03   ? 1930 PHE A N     1 
ATOM   3134  C  CA    . PHE A 1 1930 ? 207.830 233.210 206.081 1.00 7.14   ? 1930 PHE A CA    1 
ATOM   3135  C  C     . PHE A 1 1930 ? 209.135 232.941 206.820 1.00 9.17   ? 1930 PHE A C     1 
ATOM   3136  O  O     . PHE A 1 1930 ? 209.743 231.880 206.651 1.00 13.03  ? 1930 PHE A O     1 
ATOM   3137  C  CB    . PHE A 1 1930 ? 206.841 232.065 206.279 1.00 7.77   ? 1930 PHE A CB    1 
ATOM   3138  C  CG    . PHE A 1 1930 ? 205.479 232.334 205.715 1.00 6.56   ? 1930 PHE A CG    1 
ATOM   3139  C  CD1   . PHE A 1 1930 ? 204.562 233.093 206.419 1.00 7.27   ? 1930 PHE A CD1   1 
ATOM   3140  C  CD2   . PHE A 1 1930 ? 205.115 231.825 204.481 1.00 6.28   ? 1930 PHE A CD2   1 
ATOM   3141  C  CE1   . PHE A 1 1930 ? 203.308 233.340 205.901 1.00 8.17   ? 1930 PHE A CE1   1 
ATOM   3142  C  CE2   . PHE A 1 1930 ? 203.864 232.069 203.960 1.00 7.26   ? 1930 PHE A CE2   1 
ATOM   3143  C  CZ    . PHE A 1 1930 ? 202.958 232.827 204.670 1.00 7.49   ? 1930 PHE A CZ    1 
ATOM   3144  N  N     . ASN A 1 1931 ? 209.570 233.902 207.632 1.00 11.05  ? 1931 ASN A N     1 
ATOM   3145  C  CA    . ASN A 1 1931 ? 210.724 233.677 208.489 1.00 7.98   ? 1931 ASN A CA    1 
ATOM   3146  C  C     . ASN A 1 1931 ? 210.310 232.760 209.629 1.00 9.02   ? 1931 ASN A C     1 
ATOM   3147  O  O     . ASN A 1 1931 ? 209.571 233.170 210.529 1.00 11.09  ? 1931 ASN A O     1 
ATOM   3148  C  CB    . ASN A 1 1931 ? 211.278 234.997 209.022 1.00 8.82   ? 1931 ASN A CB    1 
ATOM   3149  C  CG    . ASN A 1 1931 ? 212.611 234.830 209.716 1.00 9.24   ? 1931 ASN A CG    1 
ATOM   3150  O  OD1   . ASN A 1 1931 ? 213.592 234.411 209.105 1.00 13.28  ? 1931 ASN A OD1   1 
ATOM   3151  N  ND2   . ASN A 1 1931 ? 212.654 235.149 210.999 1.00 10.64  ? 1931 ASN A ND2   1 
ATOM   3152  N  N     . CYS A 1 1932 ? 210.780 231.518 209.599 1.00 9.34   ? 1932 CYS A N     1 
ATOM   3153  C  CA    . CYS A 1 1932 ? 210.265 230.494 210.494 1.00 8.95   ? 1932 CYS A CA    1 
ATOM   3154  C  C     . CYS A 1 1932 ? 211.120 230.374 211.748 1.00 8.92   ? 1932 CYS A C     1 
ATOM   3155  O  O     . CYS A 1 1932 ? 212.346 230.499 211.700 1.00 10.85  ? 1932 CYS A O     1 
ATOM   3156  C  CB    . CYS A 1 1932 ? 210.206 229.150 209.771 1.00 12.97  ? 1932 CYS A CB    1 
ATOM   3157  S  SG    . CYS A 1 1932 ? 209.049 229.088 208.389 1.00 24.27  ? 1932 CYS A SG    1 
ATOM   3158  N  N     . ASP A 1 1933 ? 210.456 230.133 212.877 1.00 11.56  ? 1933 ASP A N     1 
ATOM   3159  C  CA    . ASP A 1 1933 ? 211.119 229.850 214.140 1.00 11.42  ? 1933 ASP A CA    1 
ATOM   3160  C  C     . ASP A 1 1933 ? 210.392 228.693 214.814 1.00 18.36  ? 1933 ASP A C     1 
ATOM   3161  O  O     . ASP A 1 1933 ? 209.522 228.050 214.219 1.00 15.86  ? 1933 ASP A O     1 
ATOM   3162  C  CB    . ASP A 1 1933 ? 211.179 231.100 215.030 1.00 12.94  ? 1933 ASP A CB    1 
ATOM   3163  C  CG    . ASP A 1 1933 ? 209.870 231.388 215.735 1.00 18.85  ? 1933 ASP A CG    1 
ATOM   3164  O  OD1   . ASP A 1 1933 ? 209.909 231.949 216.849 1.00 23.73  ? 1933 ASP A OD1   1 
ATOM   3165  O  OD2   . ASP A 1 1933 ? 208.800 231.086 215.167 1.00 20.59  ? 1933 ASP A OD2   1 
ATOM   3166  N  N     . GLU A 1 1934 ? 210.751 228.423 216.071 1.00 20.94  ? 1934 GLU A N     1 
ATOM   3167  C  CA    . GLU A 1 1934 ? 210.162 227.288 216.772 1.00 18.64  ? 1934 GLU A CA    1 
ATOM   3168  C  C     . GLU A 1 1934 ? 208.716 227.538 217.184 1.00 18.43  ? 1934 GLU A C     1 
ATOM   3169  O  O     . GLU A 1 1934 ? 208.032 226.593 217.585 1.00 29.52  ? 1934 GLU A O     1 
ATOM   3170  C  CB    . GLU A 1 1934 ? 211.001 226.922 217.998 1.00 21.77  ? 1934 GLU A CB    1 
ATOM   3171  C  CG    . GLU A 1 1934 ? 210.969 227.934 219.127 1.00 21.79  ? 1934 GLU A CG    1 
ATOM   3172  C  CD    . GLU A 1 1934 ? 211.982 229.047 218.950 1.00 37.41  ? 1934 GLU A CD    1 
ATOM   3173  O  OE1   . GLU A 1 1934 ? 212.503 229.216 217.827 1.00 40.52  ? 1934 GLU A OE1   1 
ATOM   3174  O  OE2   . GLU A 1 1934 ? 212.269 229.744 219.943 1.00 48.80  ? 1934 GLU A OE2   1 
ATOM   3175  N  N     . THR A 1 1935 ? 208.235 228.778 217.098 1.00 15.88  ? 1935 THR A N     1 
ATOM   3176  C  CA    . THR A 1 1935 ? 206.832 229.052 217.374 1.00 15.97  ? 1935 THR A CA    1 
ATOM   3177  C  C     . THR A 1 1935 ? 205.923 228.699 216.205 1.00 18.01  ? 1935 THR A C     1 
ATOM   3178  O  O     . THR A 1 1935 ? 204.698 228.729 216.362 1.00 18.18  ? 1935 THR A O     1 
ATOM   3179  C  CB    . THR A 1 1935 ? 206.634 230.524 217.745 1.00 13.83  ? 1935 THR A CB    1 
ATOM   3180  O  OG1   . THR A 1 1935 ? 206.979 231.353 216.630 1.00 16.83  ? 1935 THR A OG1   1 
ATOM   3181  C  CG2   . THR A 1 1935 ? 207.506 230.892 218.932 1.00 16.74  ? 1935 THR A CG2   1 
ATOM   3182  N  N     . PHE A 1 1936 ? 206.489 228.373 215.043 1.00 18.94  ? 1936 PHE A N     1 
ATOM   3183  C  CA    . PHE A 1 1936 ? 205.715 227.899 213.898 1.00 15.98  ? 1936 PHE A CA    1 
ATOM   3184  C  C     . PHE A 1 1936 ? 205.358 226.439 214.154 1.00 21.83  ? 1936 PHE A C     1 
ATOM   3185  O  O     . PHE A 1 1936 ? 206.002 225.505 213.669 1.00 23.59  ? 1936 PHE A O     1 
ATOM   3186  C  CB    . PHE A 1 1936 ? 206.501 228.073 212.605 1.00 17.11  ? 1936 PHE A CB    1 
ATOM   3187  C  CG    . PHE A 1 1936 ? 206.395 229.447 212.009 1.00 17.41  ? 1936 PHE A CG    1 
ATOM   3188  C  CD1   . PHE A 1 1936 ? 206.870 230.553 212.692 1.00 12.08  ? 1936 PHE A CD1   1 
ATOM   3189  C  CD2   . PHE A 1 1936 ? 205.826 229.632 210.761 1.00 22.49  ? 1936 PHE A CD2   1 
ATOM   3190  C  CE1   . PHE A 1 1936 ? 206.776 231.817 212.145 1.00 10.86  ? 1936 PHE A CE1   1 
ATOM   3191  C  CE2   . PHE A 1 1936 ? 205.729 230.894 210.208 1.00 21.58  ? 1936 PHE A CE2   1 
ATOM   3192  C  CZ    . PHE A 1 1936 ? 206.205 231.988 210.902 1.00 13.11  ? 1936 PHE A CZ    1 
ATOM   3193  N  N     . ASP A 1 1937 ? 204.307 226.244 214.943 1.00 25.17  ? 1937 ASP A N     1 
ATOM   3194  C  CA    . ASP A 1 1937 ? 203.901 224.913 215.370 1.00 13.84  ? 1937 ASP A CA    1 
ATOM   3195  C  C     . ASP A 1 1937 ? 203.059 224.250 214.282 1.00 16.12  ? 1937 ASP A C     1 
ATOM   3196  O  O     . ASP A 1 1937 ? 202.968 224.728 213.148 1.00 18.58  ? 1937 ASP A O     1 
ATOM   3197  C  CB    . ASP A 1 1937 ? 203.159 224.991 216.701 1.00 14.97  ? 1937 ASP A CB    1 
ATOM   3198  C  CG    . ASP A 1 1937 ? 201.846 225.738 216.593 1.00 20.50  ? 1937 ASP A CG    1 
ATOM   3199  O  OD1   . ASP A 1 1937 ? 201.859 226.905 216.153 1.00 24.32  ? 1937 ASP A OD1   1 
ATOM   3200  O  OD2   . ASP A 1 1937 ? 200.801 225.155 216.949 1.00 20.67  ? 1937 ASP A OD2   1 
ATOM   3201  N  N     . PHE A 1 1938 ? 202.434 223.122 214.627 1.00 19.01  ? 1938 PHE A N     1 
ATOM   3202  C  CA    . PHE A 1 1938 ? 201.648 222.368 213.654 1.00 14.95  ? 1938 PHE A CA    1 
ATOM   3203  C  C     . PHE A 1 1938 ? 200.461 223.178 213.147 1.00 15.12  ? 1938 PHE A C     1 
ATOM   3204  O  O     . PHE A 1 1938 ? 200.161 223.170 211.948 1.00 17.34  ? 1938 PHE A O     1 
ATOM   3205  C  CB    . PHE A 1 1938 ? 201.183 221.054 214.283 1.00 18.47  ? 1938 PHE A CB    1 
ATOM   3206  C  CG    . PHE A 1 1938 ? 200.387 220.180 213.356 1.00 20.95  ? 1938 PHE A CG    1 
ATOM   3207  C  CD1   . PHE A 1 1938 ? 201.016 219.434 212.377 1.00 18.47  ? 1938 PHE A CD1   1 
ATOM   3208  C  CD2   . PHE A 1 1938 ? 199.012 220.091 213.479 1.00 21.68  ? 1938 PHE A CD2   1 
ATOM   3209  C  CE1   . PHE A 1 1938 ? 200.289 218.625 211.531 1.00 17.63  ? 1938 PHE A CE1   1 
ATOM   3210  C  CE2   . PHE A 1 1938 ? 198.280 219.284 212.633 1.00 20.34  ? 1938 PHE A CE2   1 
ATOM   3211  C  CZ    . PHE A 1 1938 ? 198.918 218.551 211.658 1.00 20.88  ? 1938 PHE A CZ    1 
ATOM   3212  N  N     . GLN A 1 1939 ? 199.780 223.893 214.044 1.00 16.01  ? 1939 GLN A N     1 
ATOM   3213  C  CA    . GLN A 1 1939 ? 198.572 224.615 213.658 1.00 17.11  ? 1939 GLN A CA    1 
ATOM   3214  C  C     . GLN A 1 1939 ? 198.887 225.817 212.773 1.00 17.96  ? 1939 GLN A C     1 
ATOM   3215  O  O     . GLN A 1 1939 ? 198.192 226.064 211.777 1.00 23.58  ? 1939 GLN A O     1 
ATOM   3216  C  CB    . GLN A 1 1939 ? 197.815 225.051 214.911 1.00 24.77  ? 1939 GLN A CB    1 
ATOM   3217  C  CG    . GLN A 1 1939 ? 197.442 223.906 215.831 1.00 22.32  ? 1939 GLN A CG    1 
ATOM   3218  C  CD    . GLN A 1 1939 ? 196.092 223.314 215.494 1.00 36.39  ? 1939 GLN A CD    1 
ATOM   3219  O  OE1   . GLN A 1 1939 ? 195.084 224.019 215.457 1.00 35.65  ? 1939 GLN A OE1   1 
ATOM   3220  N  NE2   . GLN A 1 1939 ? 196.063 222.011 215.243 1.00 39.15  ? 1939 GLN A NE2   1 
ATOM   3221  N  N     . ALA A 1 1940 ? 199.921 226.584 213.126 1.00 13.41  ? 1940 ALA A N     1 
ATOM   3222  C  CA    . ALA A 1 1940 ? 200.287 227.749 212.326 1.00 14.06  ? 1940 ALA A CA    1 
ATOM   3223  C  C     . ALA A 1 1940 ? 200.733 227.338 210.928 1.00 14.26  ? 1940 ALA A C     1 
ATOM   3224  O  O     . ALA A 1 1940 ? 200.314 227.932 209.926 1.00 13.22  ? 1940 ALA A O     1 
ATOM   3225  C  CB    . ALA A 1 1940 ? 201.387 228.541 213.033 1.00 17.97  ? 1940 ALA A CB    1 
ATOM   3226  N  N     . MET A 1 1941 ? 201.584 226.312 210.844 1.00 13.69  ? 1941 MET A N     1 
ATOM   3227  C  CA    . MET A 1 1941 ? 202.013 225.814 209.543 1.00 10.95  ? 1941 MET A CA    1 
ATOM   3228  C  C     . MET A 1 1941 ? 200.834 225.259 208.759 1.00 11.41  ? 1941 MET A C     1 
ATOM   3229  O  O     . MET A 1 1941 ? 200.759 225.427 207.537 1.00 13.64  ? 1941 MET A O     1 
ATOM   3230  C  CB    . MET A 1 1941 ? 203.097 224.749 209.713 1.00 9.98   ? 1941 MET A CB    1 
ATOM   3231  C  CG    . MET A 1 1941 ? 204.393 225.268 210.315 1.00 13.70  ? 1941 MET A CG    1 
ATOM   3232  S  SD    . MET A 1 1941 ? 205.289 226.379 209.215 1.00 22.35  ? 1941 MET A SD    1 
ATOM   3233  C  CE    . MET A 1 1941 ? 205.518 225.330 207.785 1.00 6.95   ? 1941 MET A CE    1 
ATOM   3234  N  N     . GLY A 1 1942 ? 199.900 224.599 209.445 1.00 11.12  ? 1942 GLY A N     1 
ATOM   3235  C  CA    . GLY A 1 1942 ? 198.726 224.079 208.764 1.00 11.04  ? 1942 GLY A CA    1 
ATOM   3236  C  C     . GLY A 1 1942 ? 197.873 225.172 208.151 1.00 12.75  ? 1942 GLY A C     1 
ATOM   3237  O  O     . GLY A 1 1942 ? 197.412 225.046 207.017 1.00 15.43  ? 1942 GLY A O     1 
ATOM   3238  N  N     . ARG A 1 1943 ? 197.656 226.263 208.889 1.00 12.76  ? 1943 ARG A N     1 
ATOM   3239  C  CA    . ARG A 1 1943 ? 196.853 227.356 208.342 1.00 11.65  ? 1943 ARG A CA    1 
ATOM   3240  C  C     . ARG A 1 1943 ? 197.591 228.099 207.233 1.00 13.41  ? 1943 ARG A C     1 
ATOM   3241  O  O     . ARG A 1 1943 ? 196.969 228.544 206.259 1.00 20.27  ? 1943 ARG A O     1 
ATOM   3242  C  CB    . ARG A 1 1943 ? 196.420 228.304 209.455 1.00 14.75  ? 1943 ARG A CB    1 
ATOM   3243  C  CG    . ARG A 1 1943 ? 195.431 227.655 210.397 1.00 28.12  ? 1943 ARG A CG    1 
ATOM   3244  C  CD    . ARG A 1 1943 ? 194.983 228.568 211.512 1.00 31.54  ? 1943 ARG A CD    1 
ATOM   3245  N  NE    . ARG A 1 1943 ? 194.011 227.889 212.360 1.00 38.99  ? 1943 ARG A NE    1 
ATOM   3246  C  CZ    . ARG A 1 1943 ? 194.326 227.173 213.429 1.00 43.80  ? 1943 ARG A CZ    1 
ATOM   3247  N  NH1   . ARG A 1 1943 ? 195.583 227.009 213.802 1.00 38.53  ? 1943 ARG A NH1   1 
ATOM   3248  N  NH2   . ARG A 1 1943 ? 193.357 226.599 214.135 1.00 47.95  ? 1943 ARG A NH2   1 
ATOM   3249  N  N     . ILE A 1 1944 ? 198.914 228.233 207.348 1.00 11.60  ? 1944 ILE A N     1 
ATOM   3250  C  CA    . ILE A 1 1944 ? 199.683 228.809 206.248 1.00 9.09   ? 1944 ILE A CA    1 
ATOM   3251  C  C     . ILE A 1 1944 ? 199.549 227.943 205.001 1.00 12.83  ? 1944 ILE A C     1 
ATOM   3252  O  O     . ILE A 1 1944 ? 199.355 228.451 203.888 1.00 14.18  ? 1944 ILE A O     1 
ATOM   3253  C  CB    . ILE A 1 1944 ? 201.155 228.993 206.661 1.00 10.14  ? 1944 ILE A CB    1 
ATOM   3254  C  CG1   . ILE A 1 1944 ? 201.281 230.119 207.688 1.00 7.60   ? 1944 ILE A CG1   1 
ATOM   3255  C  CG2   . ILE A 1 1944 ? 202.024 229.283 205.448 1.00 6.38   ? 1944 ILE A CG2   1 
ATOM   3256  C  CD1   . ILE A 1 1944 ? 202.655 230.230 208.303 1.00 6.77   ? 1944 ILE A CD1   1 
ATOM   3257  N  N     . PHE A 1 1945 ? 199.637 226.621 205.170 1.00 10.47  ? 1945 PHE A N     1 
ATOM   3258  C  CA    . PHE A 1 1945 ? 199.472 225.709 204.045 1.00 9.12   ? 1945 PHE A CA    1 
ATOM   3259  C  C     . PHE A 1 1945 ? 198.069 225.794 203.464 1.00 11.17  ? 1945 PHE A C     1 
ATOM   3260  O  O     . PHE A 1 1945 ? 197.888 225.684 202.249 1.00 14.72  ? 1945 PHE A O     1 
ATOM   3261  C  CB    . PHE A 1 1945 ? 199.781 224.279 204.483 1.00 8.68   ? 1945 PHE A CB    1 
ATOM   3262  C  CG    . PHE A 1 1945 ? 201.243 224.003 204.665 1.00 10.84  ? 1945 PHE A CG    1 
ATOM   3263  C  CD1   . PHE A 1 1945 ? 202.189 224.692 203.927 1.00 8.92   ? 1945 PHE A CD1   1 
ATOM   3264  C  CD2   . PHE A 1 1945 ? 201.673 223.058 205.579 1.00 9.07   ? 1945 PHE A CD2   1 
ATOM   3265  C  CE1   . PHE A 1 1945 ? 203.534 224.440 204.094 1.00 7.03   ? 1945 PHE A CE1   1 
ATOM   3266  C  CE2   . PHE A 1 1945 ? 203.016 222.804 205.751 1.00 9.15   ? 1945 PHE A CE2   1 
ATOM   3267  C  CZ    . PHE A 1 1945 ? 203.949 223.495 205.008 1.00 7.29   ? 1945 PHE A CZ    1 
ATOM   3268  N  N     . VAL A 1 1946 ? 197.060 225.969 204.319 1.00 12.45  ? 1946 VAL A N     1 
ATOM   3269  C  CA    . VAL A 1 1946 ? 195.687 226.111 203.839 1.00 10.02  ? 1946 VAL A CA    1 
ATOM   3270  C  C     . VAL A 1 1946 ? 195.560 227.356 202.970 1.00 14.54  ? 1946 VAL A C     1 
ATOM   3271  O  O     . VAL A 1 1946 ? 194.961 227.325 201.887 1.00 17.82  ? 1946 VAL A O     1 
ATOM   3272  C  CB    . VAL A 1 1946 ? 194.708 226.152 205.026 1.00 7.60   ? 1946 VAL A CB    1 
ATOM   3273  C  CG1   . VAL A 1 1946 ? 193.364 226.718 204.593 1.00 15.25  ? 1946 VAL A CG1   1 
ATOM   3274  C  CG2   . VAL A 1 1946 ? 194.537 224.766 205.621 1.00 10.29  ? 1946 VAL A CG2   1 
ATOM   3275  N  N     . GLY A 1 1947 ? 196.126 228.469 203.438 1.00 16.26  ? 1947 GLY A N     1 
ATOM   3276  C  CA    . GLY A 1 1947 ? 196.097 229.689 202.646 1.00 12.65  ? 1947 GLY A CA    1 
ATOM   3277  C  C     . GLY A 1 1947 ? 196.817 229.534 201.321 1.00 13.69  ? 1947 GLY A C     1 
ATOM   3278  O  O     . GLY A 1 1947 ? 196.337 229.990 200.279 1.00 15.52  ? 1947 GLY A O     1 
ATOM   3279  N  N     . LEU A 1 1948 ? 197.982 228.882 201.341 1.00 14.44  ? 1948 LEU A N     1 
ATOM   3280  C  CA    . LEU A 1 1948 ? 198.733 228.671 200.107 1.00 9.66   ? 1948 LEU A CA    1 
ATOM   3281  C  C     . LEU A 1 1948 ? 197.978 227.762 199.143 1.00 11.36  ? 1948 LEU A C     1 
ATOM   3282  O  O     . LEU A 1 1948 ? 197.994 227.986 197.928 1.00 14.37  ? 1948 LEU A O     1 
ATOM   3283  C  CB    . LEU A 1 1948 ? 200.112 228.094 200.421 1.00 11.71  ? 1948 LEU A CB    1 
ATOM   3284  C  CG    . LEU A 1 1948 ? 201.057 228.987 201.224 1.00 7.69   ? 1948 LEU A CG    1 
ATOM   3285  C  CD1   . LEU A 1 1948 ? 202.357 228.262 201.517 1.00 4.96   ? 1948 LEU A CD1   1 
ATOM   3286  C  CD2   . LEU A 1 1948 ? 201.320 230.292 200.495 1.00 6.24   ? 1948 LEU A CD2   1 
ATOM   3287  N  N     . CYS A 1 1949 ? 197.323 226.722 199.666 1.00 14.37  ? 1949 CYS A N     1 
ATOM   3288  C  CA    . CYS A 1 1949 ? 196.526 225.832 198.830 1.00 11.52  ? 1949 CYS A CA    1 
ATOM   3289  C  C     . CYS A 1 1949 ? 195.378 226.584 198.174 1.00 14.61  ? 1949 CYS A C     1 
ATOM   3290  O  O     . CYS A 1 1949 ? 195.160 226.476 196.962 1.00 15.11  ? 1949 CYS A O     1 
ATOM   3291  C  CB    . CYS A 1 1949 ? 195.978 224.674 199.666 1.00 17.25  ? 1949 CYS A CB    1 
ATOM   3292  S  SG    . CYS A 1 1949 ? 197.137 223.362 200.092 1.00 23.98  ? 1949 CYS A SG    1 
ATOM   3293  N  N     . GLN A 1 1950 ? 194.628 227.350 198.967 1.00 15.55  ? 1950 GLN A N     1 
ATOM   3294  C  CA    . GLN A 1 1950 ? 193.462 228.046 198.436 1.00 15.97  ? 1950 GLN A CA    1 
ATOM   3295  C  C     . GLN A 1 1950 ? 193.860 229.123 197.436 1.00 15.00  ? 1950 GLN A C     1 
ATOM   3296  O  O     . GLN A 1 1950 ? 193.297 229.195 196.337 1.00 18.11  ? 1950 GLN A O     1 
ATOM   3297  C  CB    . GLN A 1 1950 ? 192.651 228.642 199.584 1.00 21.16  ? 1950 GLN A CB    1 
ATOM   3298  C  CG    . GLN A 1 1950 ? 192.035 227.609 200.507 1.00 22.70  ? 1950 GLN A CG    1 
ATOM   3299  C  CD    . GLN A 1 1950 ? 191.036 226.721 199.798 1.00 30.58  ? 1950 GLN A CD    1 
ATOM   3300  O  OE1   . GLN A 1 1950 ? 191.288 225.541 199.571 1.00 36.19  ? 1950 GLN A OE1   1 
ATOM   3301  N  NE2   . GLN A 1 1950 ? 189.892 227.289 199.440 1.00 35.27  ? 1950 GLN A NE2   1 
ATOM   3302  N  N     . VAL A 1 1951 ? 194.827 229.970 197.794 1.00 13.84  ? 1951 VAL A N     1 
ATOM   3303  C  CA    . VAL A 1 1951 ? 195.240 231.041 196.894 1.00 13.58  ? 1951 VAL A CA    1 
ATOM   3304  C  C     . VAL A 1 1951 ? 195.992 230.480 195.694 1.00 11.55  ? 1951 VAL A C     1 
ATOM   3305  O  O     . VAL A 1 1951 ? 195.792 230.919 194.557 1.00 9.43   ? 1951 VAL A O     1 
ATOM   3306  C  CB    . VAL A 1 1951 ? 196.080 232.080 197.660 1.00 13.04  ? 1951 VAL A CB    1 
ATOM   3307  C  CG1   . VAL A 1 1951 ? 196.588 233.155 196.717 1.00 13.87  ? 1951 VAL A CG1   1 
ATOM   3308  C  CG2   . VAL A 1 1951 ? 195.258 232.692 198.777 1.00 21.83  ? 1951 VAL A CG2   1 
ATOM   3309  N  N     . GLY A 1 1952 ? 196.856 229.497 195.923 1.00 14.64  ? 1952 GLY A N     1 
ATOM   3310  C  CA    . GLY A 1 1952 ? 197.693 228.973 194.863 1.00 9.89   ? 1952 GLY A CA    1 
ATOM   3311  C  C     . GLY A 1 1952 ? 199.003 229.724 194.789 1.00 9.87   ? 1952 GLY A C     1 
ATOM   3312  O  O     . GLY A 1 1952 ? 199.488 230.053 193.703 1.00 16.56  ? 1952 GLY A O     1 
ATOM   3313  N  N     . ALA A 1 1953 ? 199.582 229.999 195.951 1.00 8.22   ? 1953 ALA A N     1 
ATOM   3314  C  CA    . ALA A 1 1953 ? 200.775 230.818 196.076 1.00 5.99   ? 1953 ALA A CA    1 
ATOM   3315  C  C     . ALA A 1 1953 ? 201.975 229.960 196.451 1.00 8.49   ? 1953 ALA A C     1 
ATOM   3316  O  O     . ALA A 1 1953 ? 201.850 228.788 196.815 1.00 9.12   ? 1953 ALA A O     1 
ATOM   3317  C  CB    . ALA A 1 1953 ? 200.560 231.924 197.114 1.00 7.36   ? 1953 ALA A CB    1 
ATOM   3318  N  N     . TRP A 1 1954 ? 203.152 230.569 196.358 1.00 8.54   ? 1954 TRP A N     1 
ATOM   3319  C  CA    . TRP A 1 1954 ? 204.408 229.918 196.696 1.00 4.96   ? 1954 TRP A CA    1 
ATOM   3320  C  C     . TRP A 1 1954 ? 204.821 230.317 198.104 1.00 5.12   ? 1954 TRP A C     1 
ATOM   3321  O  O     . TRP A 1 1954 ? 204.856 231.508 198.432 1.00 7.14   ? 1954 TRP A O     1 
ATOM   3322  C  CB    . TRP A 1 1954 ? 205.506 230.301 195.703 1.00 4.04   ? 1954 TRP A CB    1 
ATOM   3323  C  CG    . TRP A 1 1954 ? 205.431 229.579 194.398 1.00 4.34   ? 1954 TRP A CG    1 
ATOM   3324  C  CD1   . TRP A 1 1954 ? 204.324 229.035 193.823 1.00 5.62   ? 1954 TRP A CD1   1 
ATOM   3325  C  CD2   . TRP A 1 1954 ? 206.515 229.332 193.496 1.00 4.06   ? 1954 TRP A CD2   1 
ATOM   3326  N  NE1   . TRP A 1 1954 ? 204.650 228.457 192.621 1.00 6.35   ? 1954 TRP A NE1   1 
ATOM   3327  C  CE2   . TRP A 1 1954 ? 205.991 228.627 192.397 1.00 4.76   ? 1954 TRP A CE2   1 
ATOM   3328  C  CE3   . TRP A 1 1954 ? 207.878 229.637 193.513 1.00 3.67   ? 1954 TRP A CE3   1 
ATOM   3329  C  CZ2   . TRP A 1 1954 ? 206.781 228.225 191.326 1.00 4.41   ? 1954 TRP A CZ2   1 
ATOM   3330  C  CZ3   . TRP A 1 1954 ? 208.659 229.235 192.450 1.00 2.72   ? 1954 TRP A CZ3   1 
ATOM   3331  C  CH2   . TRP A 1 1954 ? 208.110 228.539 191.372 1.00 3.11   ? 1954 TRP A CH2   1 
ATOM   3332  N  N     . GLY A 1 1955 ? 205.133 229.325 198.930 1.00 5.23   ? 1955 GLY A N     1 
ATOM   3333  C  CA    . GLY A 1 1955 ? 205.588 229.593 200.277 1.00 4.15   ? 1955 GLY A CA    1 
ATOM   3334  C  C     . GLY A 1 1955 ? 207.064 229.321 200.460 1.00 4.04   ? 1955 GLY A C     1 
ATOM   3335  O  O     . GLY A 1 1955 ? 207.489 228.164 200.491 1.00 5.23   ? 1955 GLY A O     1 
ATOM   3336  N  N     . CYS A 1 1956 ? 207.858 230.381 200.581 1.00 4.48   ? 1956 CYS A N     1 
ATOM   3337  C  CA    . CYS A 1 1956 ? 209.294 230.256 200.812 1.00 4.24   ? 1956 CYS A CA    1 
ATOM   3338  C  C     . CYS A 1 1956 ? 209.526 230.312 202.315 1.00 7.02   ? 1956 CYS A C     1 
ATOM   3339  O  O     . CYS A 1 1956 ? 209.507 231.386 202.920 1.00 10.56  ? 1956 CYS A O     1 
ATOM   3340  C  CB    . CYS A 1 1956 ? 210.059 231.354 200.082 1.00 6.18   ? 1956 CYS A CB    1 
ATOM   3341  S  SG    . CYS A 1 1956 ? 211.852 231.145 200.094 1.00 18.24  ? 1956 CYS A SG    1 
ATOM   3342  N  N     . PHE A 1 1957 ? 209.741 229.147 202.922 1.00 5.59   ? 1957 PHE A N     1 
ATOM   3343  C  CA    . PHE A 1 1957 ? 209.921 229.043 204.369 1.00 5.99   ? 1957 PHE A CA    1 
ATOM   3344  C  C     . PHE A 1 1957 ? 211.409 229.122 204.682 1.00 8.66   ? 1957 PHE A C     1 
ATOM   3345  O  O     . PHE A 1 1957 ? 212.132 228.127 204.642 1.00 10.49  ? 1957 PHE A O     1 
ATOM   3346  C  CB    . PHE A 1 1957 ? 209.291 227.761 204.895 1.00 4.96   ? 1957 PHE A CB    1 
ATOM   3347  C  CG    . PHE A 1 1957 ? 207.809 227.686 204.678 1.00 4.99   ? 1957 PHE A CG    1 
ATOM   3348  C  CD1   . PHE A 1 1957 ? 206.933 228.177 205.629 1.00 4.77   ? 1957 PHE A CD1   1 
ATOM   3349  C  CD2   . PHE A 1 1957 ? 207.288 227.134 203.522 1.00 5.43   ? 1957 PHE A CD2   1 
ATOM   3350  C  CE1   . PHE A 1 1957 ? 205.571 228.116 205.433 1.00 4.66   ? 1957 PHE A CE1   1 
ATOM   3351  C  CE2   . PHE A 1 1957 ? 205.926 227.070 203.321 1.00 4.32   ? 1957 PHE A CE2   1 
ATOM   3352  C  CZ    . PHE A 1 1957 ? 205.068 227.562 204.278 1.00 4.40   ? 1957 PHE A CZ    1 
ATOM   3353  N  N     . ASP A 1 1958 ? 211.870 230.328 204.998 1.00 8.82   ? 1958 ASP A N     1 
ATOM   3354  C  CA    . ASP A 1 1958 ? 213.256 230.546 205.377 1.00 8.99   ? 1958 ASP A CA    1 
ATOM   3355  C  C     . ASP A 1 1958 ? 213.496 230.099 206.813 1.00 12.97  ? 1958 ASP A C     1 
ATOM   3356  O  O     . ASP A 1 1958 ? 212.615 230.199 207.672 1.00 15.42  ? 1958 ASP A O     1 
ATOM   3357  C  CB    . ASP A 1 1958 ? 213.632 232.017 205.221 1.00 15.00  ? 1958 ASP A CB    1 
ATOM   3358  C  CG    . ASP A 1 1958 ? 213.365 232.543 203.831 1.00 22.51  ? 1958 ASP A CG    1 
ATOM   3359  O  OD1   . ASP A 1 1958 ? 212.912 231.759 202.973 1.00 21.58  ? 1958 ASP A OD1   1 
ATOM   3360  O  OD2   . ASP A 1 1958 ? 213.610 233.744 203.598 1.00 27.87  ? 1958 ASP A OD2   1 
ATOM   3361  N  N     . GLU A 1 1959 ? 214.720 229.631 207.071 1.00 13.09  ? 1959 GLU A N     1 
ATOM   3362  C  CA    . GLU A 1 1959 ? 215.082 229.017 208.352 1.00 9.85   ? 1959 GLU A CA    1 
ATOM   3363  C  C     . GLU A 1 1959 ? 214.052 227.975 208.782 1.00 8.57   ? 1959 GLU A C     1 
ATOM   3364  O  O     . GLU A 1 1959 ? 213.475 228.056 209.867 1.00 12.72  ? 1959 GLU A O     1 
ATOM   3365  C  CB    . GLU A 1 1959 ? 215.295 230.059 209.454 1.00 13.06  ? 1959 GLU A CB    1 
ATOM   3366  C  CG    . GLU A 1 1959 ? 216.507 230.967 209.260 1.00 15.97  ? 1959 GLU A CG    1 
ATOM   3367  C  CD    . GLU A 1 1959 ? 216.248 232.140 208.343 1.00 23.54  ? 1959 GLU A CD    1 
ATOM   3368  O  OE1   . GLU A 1 1959 ? 215.099 232.305 207.896 1.00 31.16  ? 1959 GLU A OE1   1 
ATOM   3369  O  OE2   . GLU A 1 1959 ? 217.202 232.895 208.059 1.00 25.02  ? 1959 GLU A OE2   1 
ATOM   3370  N  N     . PHE A 1 1960 ? 213.793 227.003 207.906 1.00 10.18  ? 1960 PHE A N     1 
ATOM   3371  C  CA    . PHE A 1 1960 ? 212.784 225.955 208.221 1.00 8.88   ? 1960 PHE A CA    1 
ATOM   3372  C  C     . PHE A 1 1960 ? 213.328 225.073 209.339 1.00 7.15   ? 1960 PHE A C     1 
ATOM   3373  O  O     . PHE A 1 1960 ? 212.532 224.411 210.038 1.00 10.44  ? 1960 PHE A O     1 
ATOM   3374  C  CB    . PHE A 1 1960 ? 212.465 225.123 206.976 1.00 7.27   ? 1960 PHE A CB    1 
ATOM   3375  C  CG    . PHE A 1 1960 ? 211.285 224.174 207.136 1.00 6.93   ? 1960 PHE A CG    1 
ATOM   3376  C  CD1   . PHE A 1 1960 ? 210.171 224.540 207.885 1.00 8.45   ? 1960 PHE A CD1   1 
ATOM   3377  C  CD2   . PHE A 1 1960 ? 211.302 222.910 206.558 1.00 6.86   ? 1960 PHE A CD2   1 
ATOM   3378  C  CE1   . PHE A 1 1960 ? 209.101 223.673 208.031 1.00 9.39   ? 1960 PHE A CE1   1 
ATOM   3379  C  CE2   . PHE A 1 1960 ? 210.228 222.047 206.709 1.00 5.59   ? 1960 PHE A CE2   1 
ATOM   3380  C  CZ    . PHE A 1 1960 ? 209.132 222.430 207.445 1.00 7.65   ? 1960 PHE A CZ    1 
ATOM   3381  N  N     . ASN A 1 1961 ? 214.652 225.067 209.514 1.00 5.85   ? 1961 ASN A N     1 
ATOM   3382  C  CA    . ASN A 1 1961 ? 215.289 224.197 210.540 1.00 6.97   ? 1961 ASN A CA    1 
ATOM   3383  C  C     . ASN A 1 1961 ? 215.229 224.876 211.914 1.00 8.54   ? 1961 ASN A C     1 
ATOM   3384  O  O     . ASN A 1 1961 ? 215.666 224.248 212.898 1.00 12.58  ? 1961 ASN A O     1 
ATOM   3385  C  CB    . ASN A 1 1961 ? 216.710 223.817 210.136 1.00 8.57   ? 1961 ASN A CB    1 
ATOM   3386  C  CG    . ASN A 1 1961 ? 217.499 224.994 209.616 1.00 9.77   ? 1961 ASN A CG    1 
ATOM   3387  O  OD1   . ASN A 1 1961 ? 216.999 226.124 209.596 1.00 12.82  ? 1961 ASN A OD1   1 
ATOM   3388  N  ND2   . ASN A 1 1961 ? 218.732 224.754 209.194 1.00 8.77   ? 1961 ASN A ND2   1 
ATOM   3389  N  N     . ARG A 1 1962 ? 214.702 226.103 211.979 1.00 8.27   ? 1962 ARG A N     1 
ATOM   3390  C  CA    . ARG A 1 1962 ? 214.560 226.804 213.284 1.00 11.30  ? 1962 ARG A CA    1 
ATOM   3391  C  C     . ARG A 1 1962 ? 213.352 226.224 214.036 1.00 15.34  ? 1962 ARG A C     1 
ATOM   3392  O  O     . ARG A 1 1962 ? 213.173 226.577 215.221 1.00 18.76  ? 1962 ARG A O     1 
ATOM   3393  C  CB    . ARG A 1 1962 ? 214.465 228.321 213.082 1.00 7.89   ? 1962 ARG A CB    1 
ATOM   3394  C  CG    . ARG A 1 1962 ? 215.798 228.925 212.664 1.00 8.37   ? 1962 ARG A CG    1 
ATOM   3395  C  CD    . ARG A 1 1962 ? 215.825 230.442 212.759 1.00 8.24   ? 1962 ARG A CD    1 
ATOM   3396  N  NE    . ARG A 1 1962 ? 215.630 230.926 214.129 1.00 6.36   ? 1962 ARG A NE    1 
ATOM   3397  C  CZ    . ARG A 1 1962 ? 214.665 231.756 214.504 1.00 6.42   ? 1962 ARG A CZ    1 
ATOM   3398  N  NH1   . ARG A 1 1962 ? 213.872 232.299 213.600 1.00 7.48   ? 1962 ARG A NH1   1 
ATOM   3399  N  NH2   . ARG A 1 1962 ? 214.504 232.045 215.783 1.00 6.97   ? 1962 ARG A NH2   1 
ATOM   3400  N  N     . LEU A 1 1963 ? 212.559 225.370 213.380 1.00 11.27  ? 1963 LEU A N     1 
ATOM   3401  C  CA    . LEU A 1 1963 ? 211.444 224.720 214.044 1.00 11.21  ? 1963 LEU A CA    1 
ATOM   3402  C  C     . LEU A 1 1963 ? 211.951 223.602 214.947 1.00 18.28  ? 1963 LEU A C     1 
ATOM   3403  O  O     . LEU A 1 1963 ? 213.096 223.157 214.845 1.00 20.09  ? 1963 LEU A O     1 
ATOM   3404  C  CB    . LEU A 1 1963 ? 210.459 224.142 213.026 1.00 11.26  ? 1963 LEU A CB    1 
ATOM   3405  C  CG    . LEU A 1 1963 ? 209.398 225.029 212.373 1.00 13.73  ? 1963 LEU A CG    1 
ATOM   3406  C  CD1   . LEU A 1 1963 ? 210.029 226.131 211.553 1.00 13.50  ? 1963 LEU A CD1   1 
ATOM   3407  C  CD2   . LEU A 1 1963 ? 208.467 224.190 211.512 1.00 9.71   ? 1963 LEU A CD2   1 
ATOM   3408  N  N     . GLU A 1 1964 ? 211.080 223.150 215.842 1.00 20.34  ? 1964 GLU A N     1 
ATOM   3409  C  CA    . GLU A 1 1964 ? 211.379 221.958 216.620 1.00 15.04  ? 1964 GLU A CA    1 
ATOM   3410  C  C     . GLU A 1 1964 ? 211.361 220.731 215.716 1.00 13.29  ? 1964 GLU A C     1 
ATOM   3411  O  O     . GLU A 1 1964 ? 210.653 220.687 214.707 1.00 14.05  ? 1964 GLU A O     1 
ATOM   3412  C  CB    . GLU A 1 1964 ? 210.374 221.791 217.761 1.00 22.66  ? 1964 GLU A CB    1 
ATOM   3413  C  CG    . GLU A 1 1964 ? 210.132 223.029 218.640 1.00 35.40  ? 1964 GLU A CG    1 
ATOM   3414  C  CD    . GLU A 1 1964 ? 211.376 223.583 219.340 1.00 46.37  ? 1964 GLU A CD    1 
ATOM   3415  O  OE1   . GLU A 1 1964 ? 212.509 223.129 219.076 1.00 34.06  ? 1964 GLU A OE1   1 
ATOM   3416  O  OE2   . GLU A 1 1964 ? 211.207 224.493 220.179 1.00 52.11  ? 1964 GLU A OE2   1 
ATOM   3417  N  N     . GLU A 1 1965 ? 212.159 219.727 216.085 1.00 13.79  ? 1965 GLU A N     1 
ATOM   3418  C  CA    . GLU A 1 1965 ? 212.211 218.505 215.288 1.00 15.46  ? 1965 GLU A CA    1 
ATOM   3419  C  C     . GLU A 1 1965 ? 210.861 217.804 215.267 1.00 13.95  ? 1965 GLU A C     1 
ATOM   3420  O  O     . GLU A 1 1965 ? 210.451 217.258 214.236 1.00 15.75  ? 1965 GLU A O     1 
ATOM   3421  C  CB    . GLU A 1 1965 ? 213.295 217.570 215.823 1.00 14.25  ? 1965 GLU A CB    1 
ATOM   3422  C  CG    . GLU A 1 1965 ? 214.657 218.221 215.963 1.00 22.77  ? 1965 GLU A CG    1 
ATOM   3423  C  CD    . GLU A 1 1965 ? 215.790 217.221 215.877 1.00 37.42  ? 1965 GLU A CD    1 
ATOM   3424  O  OE1   . GLU A 1 1965 ? 216.958 217.624 216.061 1.00 34.03  ? 1965 GLU A OE1   1 
ATOM   3425  O  OE2   . GLU A 1 1965 ? 215.513 216.031 215.621 1.00 40.63  ? 1965 GLU A OE2   1 
ATOM   3426  N  N     . ARG A 1 1966 ? 210.158 217.803 216.399 1.00 10.35  ? 1966 ARG A N     1 
ATOM   3427  C  CA    . ARG A 1 1966 ? 208.836 217.190 216.449 1.00 10.85  ? 1966 ARG A CA    1 
ATOM   3428  C  C     . ARG A 1 1966 ? 207.827 217.982 215.619 1.00 10.43  ? 1966 ARG A C     1 
ATOM   3429  O  O     . ARG A 1 1966 ? 206.963 217.395 214.959 1.00 11.34  ? 1966 ARG A O     1 
ATOM   3430  C  CB    . ARG A 1 1966 ? 208.407 217.032 217.910 1.00 14.15  ? 1966 ARG A CB    1 
ATOM   3431  C  CG    . ARG A 1 1966 ? 208.214 218.311 218.706 1.00 14.38  ? 1966 ARG A CG    1 
ATOM   3432  C  CD    . ARG A 1 1966 ? 207.833 217.962 220.142 1.00 20.20  ? 1966 ARG A CD    1 
ATOM   3433  N  NE    . ARG A 1 1966 ? 207.717 219.133 221.001 1.00 33.46  ? 1966 ARG A NE    1 
ATOM   3434  C  CZ    . ARG A 1 1966 ? 206.603 219.827 221.184 1.00 29.99  ? 1966 ARG A CZ    1 
ATOM   3435  N  NH1   . ARG A 1 1966 ? 205.448 219.424 220.684 1.00 19.34  ? 1966 ARG A NH1   1 
ATOM   3436  N  NH2   . ARG A 1 1966 ? 206.642 220.935 221.919 1.00 20.27  ? 1966 ARG A NH2   1 
ATOM   3437  N  N     . MET A 1 1967 ? 207.949 219.312 215.604 1.00 12.09  ? 1967 MET A N     1 
ATOM   3438  C  CA    . MET A 1 1967 ? 207.171 220.111 214.659 1.00 9.96   ? 1967 MET A CA    1 
ATOM   3439  C  C     . MET A 1 1967 ? 207.542 219.820 213.213 1.00 7.79   ? 1967 MET A C     1 
ATOM   3440  O  O     . MET A 1 1967 ? 206.659 219.797 212.352 1.00 8.43   ? 1967 MET A O     1 
ATOM   3441  C  CB    . MET A 1 1967 ? 207.328 221.601 214.957 1.00 11.20  ? 1967 MET A CB    1 
ATOM   3442  C  CG    . MET A 1 1967 ? 206.830 221.992 216.323 1.00 21.13  ? 1967 MET A CG    1 
ATOM   3443  S  SD    . MET A 1 1967 ? 205.077 221.579 216.405 1.00 21.34  ? 1967 MET A SD    1 
ATOM   3444  C  CE    . MET A 1 1967 ? 205.039 220.485 217.805 1.00 13.62  ? 1967 MET A CE    1 
ATOM   3445  N  N     . LEU A 1 1968 ? 208.826 219.616 212.917 1.00 8.46   ? 1968 LEU A N     1 
ATOM   3446  C  CA    . LEU A 1 1968 ? 209.206 219.259 211.554 1.00 7.33   ? 1968 LEU A CA    1 
ATOM   3447  C  C     . LEU A 1 1968 ? 208.564 217.942 211.139 1.00 7.82   ? 1968 LEU A C     1 
ATOM   3448  O  O     . LEU A 1 1968 ? 208.021 217.824 210.032 1.00 9.59   ? 1968 LEU A O     1 
ATOM   3449  C  CB    . LEU A 1 1968 ? 210.727 219.179 211.437 1.00 8.91   ? 1968 LEU A CB    1 
ATOM   3450  C  CG    . LEU A 1 1968 ? 211.481 220.509 211.456 1.00 9.57   ? 1968 LEU A CG    1 
ATOM   3451  C  CD1   . LEU A 1 1968 ? 212.959 220.284 211.724 1.00 13.47  ? 1968 LEU A CD1   1 
ATOM   3452  C  CD2   . LEU A 1 1968 ? 211.277 221.263 210.154 1.00 6.65   ? 1968 LEU A CD2   1 
ATOM   3453  N  N     . SER A 1 1969 ? 208.594 216.949 212.029 1.00 10.69  ? 1969 SER A N     1 
ATOM   3454  C  CA    . SER A 1 1969 ? 207.952 215.671 211.744 1.00 7.38   ? 1969 SER A CA    1 
ATOM   3455  C  C     . SER A 1 1969 ? 206.451 215.838 211.542 1.00 7.15   ? 1969 SER A C     1 
ATOM   3456  O  O     . SER A 1 1969 ? 205.875 215.254 210.618 1.00 8.31   ? 1969 SER A O     1 
ATOM   3457  C  CB    . SER A 1 1969 ? 208.236 214.682 212.875 1.00 6.49   ? 1969 SER A CB    1 
ATOM   3458  O  OG    . SER A 1 1969 ? 207.617 213.432 212.631 1.00 15.08  ? 1969 SER A OG    1 
ATOM   3459  N  N     . ALA A 1 1970 ? 205.804 216.640 212.391 1.00 7.14   ? 1970 ALA A N     1 
ATOM   3460  C  CA    . ALA A 1 1970 ? 204.365 216.845 212.262 1.00 7.89   ? 1970 ALA A CA    1 
ATOM   3461  C  C     . ALA A 1 1970 ? 204.012 217.542 210.952 1.00 11.60  ? 1970 ALA A C     1 
ATOM   3462  O  O     . ALA A 1 1970 ? 203.027 217.186 210.296 1.00 13.93  ? 1970 ALA A O     1 
ATOM   3463  C  CB    . ALA A 1 1970 ? 203.846 217.646 213.456 1.00 8.51   ? 1970 ALA A CB    1 
ATOM   3464  N  N     . VAL A 1 1971 ? 204.802 218.542 210.559 1.00 9.34   ? 1971 VAL A N     1 
ATOM   3465  C  CA    . VAL A 1 1971 ? 204.535 219.284 209.330 1.00 9.29   ? 1971 VAL A CA    1 
ATOM   3466  C  C     . VAL A 1 1971 ? 204.825 218.423 208.106 1.00 7.88   ? 1971 VAL A C     1 
ATOM   3467  O  O     . VAL A 1 1971 ? 204.256 218.648 207.026 1.00 12.05  ? 1971 VAL A O     1 
ATOM   3468  C  CB    . VAL A 1 1971 ? 205.351 220.593 209.339 1.00 8.50   ? 1971 VAL A CB    1 
ATOM   3469  C  CG1   . VAL A 1 1971 ? 205.353 221.268 207.977 1.00 7.04   ? 1971 VAL A CG1   1 
ATOM   3470  C  CG2   . VAL A 1 1971 ? 204.811 221.540 210.398 1.00 6.52   ? 1971 VAL A CG2   1 
ATOM   3471  N  N     . SER A 1 1972 ? 205.708 217.430 208.250 1.00 8.55   ? 1972 SER A N     1 
ATOM   3472  C  CA    . SER A 1 1972 ? 205.986 216.523 207.140 1.00 9.21   ? 1972 SER A CA    1 
ATOM   3473  C  C     . SER A 1 1972 ? 204.719 215.833 206.652 1.00 10.30  ? 1972 SER A C     1 
ATOM   3474  O  O     . SER A 1 1972 ? 204.564 215.588 205.452 1.00 10.63  ? 1972 SER A O     1 
ATOM   3475  C  CB    . SER A 1 1972 ? 207.029 215.488 207.559 1.00 6.62   ? 1972 SER A CB    1 
ATOM   3476  O  OG    . SER A 1 1972 ? 206.414 214.366 208.164 1.00 9.11   ? 1972 SER A OG    1 
ATOM   3477  N  N     . GLN A 1 1973 ? 203.800 215.512 207.566 1.00 12.19  ? 1973 GLN A N     1 
ATOM   3478  C  CA    . GLN A 1 1973 ? 202.564 214.846 207.166 1.00 11.23  ? 1973 GLN A CA    1 
ATOM   3479  C  C     . GLN A 1 1973 ? 201.700 215.753 206.294 1.00 9.91   ? 1973 GLN A C     1 
ATOM   3480  O  O     . GLN A 1 1973 ? 201.155 215.308 205.276 1.00 10.42  ? 1973 GLN A O     1 
ATOM   3481  C  CB    . GLN A 1 1973 ? 201.798 214.384 208.406 1.00 12.83  ? 1973 GLN A CB    1 
ATOM   3482  C  CG    . GLN A 1 1973 ? 200.639 213.446 208.108 1.00 21.51  ? 1973 GLN A CG    1 
ATOM   3483  C  CD    . GLN A 1 1973 ? 199.972 212.927 209.365 1.00 24.85  ? 1973 GLN A CD    1 
ATOM   3484  O  OE1   . GLN A 1 1973 ? 200.338 213.305 210.477 1.00 30.43  ? 1973 GLN A OE1   1 
ATOM   3485  N  NE2   . GLN A 1 1973 ? 198.984 212.058 209.194 1.00 22.71  ? 1973 GLN A NE2   1 
ATOM   3486  N  N     . GLN A 1 1974 ? 201.574 217.027 206.671 1.00 11.92  ? 1974 GLN A N     1 
ATOM   3487  C  CA    . GLN A 1 1974 ? 200.817 217.970 205.854 1.00 11.36  ? 1974 GLN A CA    1 
ATOM   3488  C  C     . GLN A 1 1974 ? 201.478 218.178 204.498 1.00 10.07  ? 1974 GLN A C     1 
ATOM   3489  O  O     . GLN A 1 1974 ? 200.794 218.257 203.470 1.00 13.79  ? 1974 GLN A O     1 
ATOM   3490  C  CB    . GLN A 1 1974 ? 200.671 219.303 206.585 1.00 10.66  ? 1974 GLN A CB    1 
ATOM   3491  C  CG    . GLN A 1 1974 ? 200.248 219.178 208.035 1.00 11.45  ? 1974 GLN A CG    1 
ATOM   3492  C  CD    . GLN A 1 1974 ? 200.186 220.516 208.741 1.00 18.58  ? 1974 GLN A CD    1 
ATOM   3493  O  OE1   . GLN A 1 1974 ? 199.150 220.898 209.282 1.00 21.59  ? 1974 GLN A OE1   1 
ATOM   3494  N  NE2   . GLN A 1 1974 ? 201.299 221.238 208.739 1.00 16.85  ? 1974 GLN A NE2   1 
ATOM   3495  N  N     . VAL A 1 1975 ? 202.809 218.272 204.478 1.00 8.55   ? 1975 VAL A N     1 
ATOM   3496  C  CA    . VAL A 1 1975 ? 203.518 218.439 203.212 1.00 7.86   ? 1975 VAL A CA    1 
ATOM   3497  C  C     . VAL A 1 1975 ? 203.289 217.232 202.311 1.00 9.27   ? 1975 VAL A C     1 
ATOM   3498  O  O     . VAL A 1 1975 ? 203.059 217.372 201.103 1.00 11.26  ? 1975 VAL A O     1 
ATOM   3499  C  CB    . VAL A 1 1975 ? 205.018 218.685 203.462 1.00 5.73   ? 1975 VAL A CB    1 
ATOM   3500  C  CG1   . VAL A 1 1975 ? 205.770 218.757 202.147 1.00 5.49   ? 1975 VAL A CG1   1 
ATOM   3501  C  CG2   . VAL A 1 1975 ? 205.216 219.965 204.250 1.00 6.46   ? 1975 VAL A CG2   1 
ATOM   3502  N  N     . GLN A 1 1976 ? 203.343 216.028 202.886 1.00 8.49   ? 1976 GLN A N     1 
ATOM   3503  C  CA    . GLN A 1 1976 ? 203.100 214.816 202.113 1.00 9.97   ? 1976 GLN A CA    1 
ATOM   3504  C  C     . GLN A 1 1976 ? 201.680 214.783 201.568 1.00 12.66  ? 1976 GLN A C     1 
ATOM   3505  O  O     . GLN A 1 1976 ? 201.460 214.398 200.413 1.00 16.36  ? 1976 GLN A O     1 
ATOM   3506  C  CB    . GLN A 1 1976 ? 203.376 213.587 202.979 1.00 12.70  ? 1976 GLN A CB    1 
ATOM   3507  C  CG    . GLN A 1 1976 ? 202.828 212.285 202.425 1.00 15.21  ? 1976 GLN A CG    1 
ATOM   3508  C  CD    . GLN A 1 1976 ? 203.704 211.100 202.765 1.00 23.22  ? 1976 GLN A CD    1 
ATOM   3509  O  OE1   . GLN A 1 1976 ? 204.571 211.185 203.632 1.00 25.46  ? 1976 GLN A OE1   1 
ATOM   3510  N  NE2   . GLN A 1 1976 ? 203.480 209.984 202.083 1.00 37.92  ? 1976 GLN A NE2   1 
ATOM   3511  N  N     . CYS A 1 1977 ? 200.699 215.184 202.381 1.00 13.40  ? 1977 CYS A N     1 
ATOM   3512  C  CA    . CYS A 1 1977 ? 199.318 215.212 201.907 1.00 13.21  ? 1977 CYS A CA    1 
ATOM   3513  C  C     . CYS A 1 1977 ? 199.147 216.194 200.754 1.00 13.84  ? 1977 CYS A C     1 
ATOM   3514  O  O     . CYS A 1 1977 ? 198.493 215.881 199.749 1.00 16.32  ? 1977 CYS A O     1 
ATOM   3515  C  CB    . CYS A 1 1977 ? 198.375 215.567 203.057 1.00 13.00  ? 1977 CYS A CB    1 
ATOM   3516  S  SG    . CYS A 1 1977 ? 198.063 214.214 204.211 1.00 52.37  ? 1977 CYS A SG    1 
ATOM   3517  N  N     . ILE A 1 1978 ? 199.738 217.385 200.875 1.00 12.30  ? 1978 ILE A N     1 
ATOM   3518  C  CA    . ILE A 1 1978 ? 199.618 218.382 199.814 1.00 14.61  ? 1978 ILE A CA    1 
ATOM   3519  C  C     . ILE A 1 1978 ? 200.287 217.889 198.538 1.00 13.13  ? 1978 ILE A C     1 
ATOM   3520  O  O     . ILE A 1 1978 ? 199.751 218.052 197.435 1.00 14.88  ? 1978 ILE A O     1 
ATOM   3521  C  CB    . ILE A 1 1978 ? 200.197 219.732 200.273 1.00 12.99  ? 1978 ILE A CB    1 
ATOM   3522  C  CG1   . ILE A 1 1978 ? 199.376 220.300 201.431 1.00 12.00  ? 1978 ILE A CG1   1 
ATOM   3523  C  CG2   . ILE A 1 1978 ? 200.226 220.718 199.120 1.00 11.82  ? 1978 ILE A CG2   1 
ATOM   3524  C  CD1   . ILE A 1 1978 ? 200.030 221.471 202.119 1.00 10.12  ? 1978 ILE A CD1   1 
ATOM   3525  N  N     . GLN A 1 1979 ? 201.469 217.282 198.664 1.00 14.77  ? 1979 GLN A N     1 
ATOM   3526  C  CA    . GLN A 1 1979 ? 202.170 216.786 197.484 1.00 12.36  ? 1979 GLN A CA    1 
ATOM   3527  C  C     . GLN A 1 1979 ? 201.413 215.636 196.828 1.00 18.03  ? 1979 GLN A C     1 
ATOM   3528  O  O     . GLN A 1 1979 ? 201.396 215.523 195.598 1.00 19.18  ? 1979 GLN A O     1 
ATOM   3529  C  CB    . GLN A 1 1979 ? 203.588 216.360 197.856 1.00 14.25  ? 1979 GLN A CB    1 
ATOM   3530  C  CG    . GLN A 1 1979 ? 204.519 217.525 198.131 1.00 9.60   ? 1979 GLN A CG    1 
ATOM   3531  C  CD    . GLN A 1 1979 ? 205.921 217.081 198.475 1.00 9.56   ? 1979 GLN A CD    1 
ATOM   3532  O  OE1   . GLN A 1 1979 ? 206.241 215.895 198.409 1.00 15.00  ? 1979 GLN A OE1   1 
ATOM   3533  N  NE2   . GLN A 1 1979 ? 206.771 218.032 198.841 1.00 9.87   ? 1979 GLN A NE2   1 
ATOM   3534  N  N     . GLU A 1 1980 ? 200.785 214.771 197.628 1.00 21.82  ? 1980 GLU A N     1 
ATOM   3535  C  CA    . GLU A 1 1980 ? 199.968 213.702 197.061 1.00 18.72  ? 1980 GLU A CA    1 
ATOM   3536  C  C     . GLU A 1 1980 ? 198.767 214.270 196.315 1.00 19.90  ? 1980 GLU A C     1 
ATOM   3537  O  O     . GLU A 1 1980 ? 198.405 213.783 195.237 1.00 25.20  ? 1980 GLU A O     1 
ATOM   3538  C  CB    . GLU A 1 1980 ? 199.517 212.748 198.164 1.00 19.62  ? 1980 GLU A CB    1 
ATOM   3539  C  CG    . GLU A 1 1980 ? 198.693 211.569 197.675 1.00 45.13  ? 1980 GLU A CG    1 
ATOM   3540  C  CD    . GLU A 1 1980 ? 199.484 210.631 196.779 1.00 60.34  ? 1980 GLU A CD    1 
ATOM   3541  O  OE1   . GLU A 1 1980 ? 200.725 210.583 196.909 1.00 48.60  ? 1980 GLU A OE1   1 
ATOM   3542  O  OE2   . GLU A 1 1980 ? 198.862 209.941 195.944 1.00 62.60  ? 1980 GLU A OE2   1 
ATOM   3543  N  N     . ALA A 1 1981 ? 198.137 215.306 196.876 1.00 21.77  ? 1981 ALA A N     1 
ATOM   3544  C  CA    . ALA A 1 1981 ? 197.040 215.966 196.175 1.00 24.79  ? 1981 ALA A CA    1 
ATOM   3545  C  C     . ALA A 1 1981 ? 197.513 216.576 194.860 1.00 22.55  ? 1981 ALA A C     1 
ATOM   3546  O  O     . ALA A 1 1981 ? 196.816 216.496 193.842 1.00 33.02  ? 1981 ALA A O     1 
ATOM   3547  C  CB    . ALA A 1 1981 ? 196.412 217.034 197.069 1.00 26.16  ? 1981 ALA A CB    1 
ATOM   3548  N  N     . LEU A 1 1982 ? 198.696 217.193 194.863 1.00 19.73  ? 1982 LEU A N     1 
ATOM   3549  C  CA    . LEU A 1 1982 ? 199.237 217.766 193.633 1.00 18.06  ? 1982 LEU A CA    1 
ATOM   3550  C  C     . LEU A 1 1982 ? 199.520 216.684 192.597 1.00 24.58  ? 1982 LEU A C     1 
ATOM   3551  O  O     . LEU A 1 1982 ? 199.247 216.866 191.404 1.00 28.55  ? 1982 LEU A O     1 
ATOM   3552  C  CB    . LEU A 1 1982 ? 200.507 218.558 193.938 1.00 13.98  ? 1982 LEU A CB    1 
ATOM   3553  C  CG    . LEU A 1 1982 ? 200.325 219.894 194.657 1.00 10.94  ? 1982 LEU A CG    1 
ATOM   3554  C  CD1   . LEU A 1 1982 ? 201.674 220.531 194.927 1.00 12.33  ? 1982 LEU A CD1   1 
ATOM   3555  C  CD2   . LEU A 1 1982 ? 199.447 220.819 193.841 1.00 12.24  ? 1982 LEU A CD2   1 
ATOM   3556  N  N     . ARG A 1 1983 ? 200.077 215.554 193.037 1.00 27.37  ? 1983 ARG A N     1 
ATOM   3557  C  CA    . ARG A 1 1983 ? 200.337 214.446 192.126 1.00 25.31  ? 1983 ARG A CA    1 
ATOM   3558  C  C     . ARG A 1 1983 ? 199.044 213.923 191.519 1.00 36.36  ? 1983 ARG A C     1 
ATOM   3559  O  O     . ARG A 1 1983 ? 198.986 213.629 190.319 1.00 45.45  ? 1983 ARG A O     1 
ATOM   3560  C  CB    . ARG A 1 1983 ? 201.077 213.328 192.860 1.00 19.32  ? 1983 ARG A CB    1 
ATOM   3561  C  CG    . ARG A 1 1983 ? 202.584 213.479 192.861 1.00 21.48  ? 1983 ARG A CG    1 
ATOM   3562  C  CD    . ARG A 1 1983 ? 203.176 212.999 194.172 1.00 26.22  ? 1983 ARG A CD    1 
ATOM   3563  N  NE    . ARG A 1 1983 ? 204.542 213.471 194.357 1.00 28.93  ? 1983 ARG A NE    1 
ATOM   3564  C  CZ    . ARG A 1 1983 ? 205.223 213.364 195.490 1.00 31.80  ? 1983 ARG A CZ    1 
ATOM   3565  N  NH1   . ARG A 1 1983 ? 204.690 212.809 196.566 1.00 27.92  ? 1983 ARG A NH1   1 
ATOM   3566  N  NH2   . ARG A 1 1983 ? 206.468 213.829 195.544 1.00 28.90  ? 1983 ARG A NH2   1 
ATOM   3567  N  N     . GLU A 1 1984 ? 197.994 213.796 192.334 1.00 38.68  ? 1984 GLU A N     1 
ATOM   3568  C  CA    . GLU A 1 1984 ? 196.699 213.386 191.805 1.00 44.93  ? 1984 GLU A CA    1 
ATOM   3569  C  C     . GLU A 1 1984 ? 196.128 214.412 190.833 1.00 46.19  ? 1984 GLU A C     1 
ATOM   3570  O  O     . GLU A 1 1984 ? 195.490 214.029 189.848 1.00 55.31  ? 1984 GLU A O     1 
ATOM   3571  C  CB    . GLU A 1 1984 ? 195.716 213.136 192.949 1.00 48.19  ? 1984 GLU A CB    1 
ATOM   3572  C  CG    . GLU A 1 1984 ? 194.357 212.625 192.499 1.00 64.63  ? 1984 GLU A CG    1 
ATOM   3573  C  CD    . GLU A 1 1984 ? 193.427 212.338 193.660 1.00 75.75  ? 1984 GLU A CD    1 
ATOM   3574  O  OE1   . GLU A 1 1984 ? 193.835 212.559 194.820 1.00 78.75  ? 1984 GLU A OE1   1 
ATOM   3575  O  OE2   . GLU A 1 1984 ? 192.288 211.888 193.414 1.00 68.33  ? 1984 GLU A OE2   1 
ATOM   3576  N  N     . HIS A 1 1985 ? 196.346 215.704 191.092 1.00 47.42  ? 1985 HIS A N     1 
ATOM   3577  C  CA    . HIS A 1 1985 ? 195.924 216.732 190.145 1.00 48.14  ? 1985 HIS A CA    1 
ATOM   3578  C  C     . HIS A 1 1985 ? 196.641 216.583 188.809 1.00 51.92  ? 1985 HIS A C     1 
ATOM   3579  O  O     . HIS A 1 1985 ? 196.022 216.713 187.748 1.00 58.71  ? 1985 HIS A O     1 
ATOM   3580  C  CB    . HIS A 1 1985 ? 196.182 218.123 190.724 1.00 48.60  ? 1985 HIS A CB    1 
ATOM   3581  C  CG    . HIS A 1 1985 ? 195.653 219.236 189.874 1.00 54.53  ? 1985 HIS A CG    1 
ATOM   3582  N  ND1   . HIS A 1 1985 ? 196.368 219.774 188.825 1.00 57.52  ? 1985 HIS A ND1   1 
ATOM   3583  C  CD2   . HIS A 1 1985 ? 194.492 219.930 189.932 1.00 51.75  ? 1985 HIS A CD2   1 
ATOM   3584  C  CE1   . HIS A 1 1985 ? 195.660 220.736 188.262 1.00 56.57  ? 1985 HIS A CE1   1 
ATOM   3585  N  NE2   . HIS A 1 1985 ? 194.518 220.853 188.915 1.00 50.33  ? 1985 HIS A NE2   1 
ATOM   3586  N  N     . SER A 1 1986 ? 197.947 216.310 188.843 1.00 60.29  ? 1986 SER A N     1 
ATOM   3587  C  CA    . SER A 1 1986 ? 198.745 216.241 187.624 1.00 51.87  ? 1986 SER A CA    1 
ATOM   3588  C  C     . SER A 1 1986 ? 198.385 215.058 186.735 1.00 60.15  ? 1986 SER A C     1 
ATOM   3589  O  O     . SER A 1 1986 ? 198.813 215.028 185.577 1.00 66.64  ? 1986 SER A O     1 
ATOM   3590  C  CB    . SER A 1 1986 ? 200.232 216.181 187.978 1.00 37.67  ? 1986 SER A CB    1 
ATOM   3591  O  OG    . SER A 1 1986 ? 200.642 214.850 188.235 1.00 41.58  ? 1986 SER A OG    1 
ATOM   3592  N  N     . ASN A 1 1987 ? 197.625 214.093 187.237 1.00 66.78  ? 1987 ASN A N     1 
ATOM   3593  C  CA    . ASN A 1 1987 ? 197.265 212.932 186.431 1.00 76.28  ? 1987 ASN A CA    1 
ATOM   3594  C  C     . ASN A 1 1987 ? 196.342 213.350 185.291 1.00 88.39  ? 1987 ASN A C     1 
ATOM   3595  O  O     . ASN A 1 1987 ? 195.391 214.108 185.515 1.00 90.42  ? 1987 ASN A O     1 
ATOM   3596  C  CB    . ASN A 1 1987 ? 196.588 211.873 187.296 1.00 71.51  ? 1987 ASN A CB    1 
ATOM   3597  C  CG    . ASN A 1 1987 ? 197.524 211.284 188.330 1.00 67.24  ? 1987 ASN A CG    1 
ATOM   3598  O  OD1   . ASN A 1 1987 ? 197.152 211.101 189.489 1.00 64.51  ? 1987 ASN A OD1   1 
ATOM   3599  N  ND2   . ASN A 1 1987 ? 198.750 210.984 187.918 1.00 70.10  ? 1987 ASN A ND2   1 
ATOM   3600  N  N     . PRO A 1 1988 ? 196.589 212.891 184.060 1.00 91.73  ? 1988 PRO A N     1 
ATOM   3601  C  CA    . PRO A 1 1988 ? 195.711 213.275 182.943 1.00 95.49  ? 1988 PRO A CA    1 
ATOM   3602  C  C     . PRO A 1 1988 ? 194.294 212.744 183.064 1.00 98.68  ? 1988 PRO A C     1 
ATOM   3603  O  O     . PRO A 1 1988 ? 193.391 213.291 182.419 1.00 95.25  ? 1988 PRO A O     1 
ATOM   3604  C  CB    . PRO A 1 1988 ? 196.423 212.687 181.718 1.00 92.17  ? 1988 PRO A CB    1 
ATOM   3605  C  CG    . PRO A 1 1988 ? 197.227 211.554 182.262 1.00 87.49  ? 1988 PRO A CG    1 
ATOM   3606  C  CD    . PRO A 1 1988 ? 197.663 211.977 183.635 1.00 83.94  ? 1988 PRO A CD    1 
ATOM   3607  N  N     . ASN A 1 1989 ? 194.070 211.696 183.861 1.00 98.67  ? 1989 ASN A N     1 
ATOM   3608  C  CA    . ASN A 1 1989 ? 192.731 211.128 183.981 1.00 94.95  ? 1989 ASN A CA    1 
ATOM   3609  C  C     . ASN A 1 1989 ? 191.761 212.118 184.615 1.00 97.52  ? 1989 ASN A C     1 
ATOM   3610  O  O     . ASN A 1 1989 ? 190.562 212.102 184.315 1.00 95.53  ? 1989 ASN A O     1 
ATOM   3611  C  CB    . ASN A 1 1989 ? 192.783 209.832 184.788 1.00 89.42  ? 1989 ASN A CB    1 
ATOM   3612  C  CG    . ASN A 1 1989 ? 193.718 209.924 185.976 1.00 91.39  ? 1989 ASN A CG    1 
ATOM   3613  O  OD1   . ASN A 1 1989 ? 193.513 210.733 186.881 1.00 93.62  ? 1989 ASN A OD1   1 
ATOM   3614  N  ND2   . ASN A 1 1989 ? 194.755 209.092 185.981 1.00 83.69  ? 1989 ASN A ND2   1 
ATOM   3615  N  N     . TYR A 1 1990 ? 192.259 212.982 185.496 1.00 99.04  ? 1990 TYR A N     1 
ATOM   3616  C  CA    . TYR A 1 1990 ? 191.414 213.998 186.107 1.00 98.99  ? 1990 TYR A CA    1 
ATOM   3617  C  C     . TYR A 1 1990 ? 190.969 215.027 185.074 1.00 99.88  ? 1990 TYR A C     1 
ATOM   3618  O  O     . TYR A 1 1990 ? 191.724 215.396 184.170 1.00 98.84  ? 1990 TYR A O     1 
ATOM   3619  C  CB    . TYR A 1 1990 ? 192.155 214.694 187.248 1.00 95.24  ? 1990 TYR A CB    1 
ATOM   3620  C  CG    . TYR A 1 1990 ? 191.454 215.937 187.752 1.00 92.64  ? 1990 TYR A CG    1 
ATOM   3621  C  CD1   . TYR A 1 1990 ? 190.342 215.845 188.578 1.00 94.34  ? 1990 TYR A CD1   1 
ATOM   3622  C  CD2   . TYR A 1 1990 ? 191.897 217.202 187.388 1.00 86.99  ? 1990 TYR A CD2   1 
ATOM   3623  C  CE1   . TYR A 1 1990 ? 189.695 216.980 189.033 1.00 91.94  ? 1990 TYR A CE1   1 
ATOM   3624  C  CE2   . TYR A 1 1990 ? 191.256 218.341 187.836 1.00 92.04  ? 1990 TYR A CE2   1 
ATOM   3625  C  CZ    . TYR A 1 1990 ? 190.155 218.224 188.657 1.00 93.73  ? 1990 TYR A CZ    1 
ATOM   3626  O  OH    . TYR A 1 1990 ? 189.518 219.357 189.108 1.00 87.62  ? 1990 TYR A OH    1 
ATOM   3627  N  N     . ASP A 1 1991 ? 189.730 215.490 185.216 1.00 103.83 ? 1991 ASP A N     1 
ATOM   3628  C  CA    . ASP A 1 1991 ? 189.198 216.587 184.423 1.00 104.12 ? 1991 ASP A CA    1 
ATOM   3629  C  C     . ASP A 1 1991 ? 188.693 217.679 185.356 1.00 101.80 ? 1991 ASP A C     1 
ATOM   3630  O  O     . ASP A 1 1991 ? 188.122 217.395 186.414 1.00 101.07 ? 1991 ASP A O     1 
ATOM   3631  C  CB    . ASP A 1 1991 ? 188.066 216.121 183.499 1.00 106.60 ? 1991 ASP A CB    1 
ATOM   3632  C  CG    . ASP A 1 1991 ? 186.952 215.418 184.249 1.00 107.71 ? 1991 ASP A CG    1 
ATOM   3633  O  OD1   . ASP A 1 1991 ? 187.244 214.444 184.975 1.00 110.42 ? 1991 ASP A OD1   1 
ATOM   3634  O  OD2   . ASP A 1 1991 ? 185.785 215.843 184.115 1.00 99.95  ? 1991 ASP A OD2   1 
ATOM   3635  N  N     . LYS A 1 1992 ? 188.904 218.934 184.953 1.00 101.63 ? 1992 LYS A N     1 
ATOM   3636  C  CA    . LYS A 1 1992 ? 188.540 220.062 185.805 1.00 104.09 ? 1992 LYS A CA    1 
ATOM   3637  C  C     . LYS A 1 1992 ? 187.046 220.119 186.096 1.00 106.31 ? 1992 LYS A C     1 
ATOM   3638  O  O     . LYS A 1 1992 ? 186.642 220.761 187.072 1.00 106.48 ? 1992 LYS A O     1 
ATOM   3639  C  CB    . LYS A 1 1992 ? 188.996 221.375 185.166 1.00 100.28 ? 1992 LYS A CB    1 
ATOM   3640  C  CG    . LYS A 1 1992 ? 190.502 221.493 184.993 1.00 98.14  ? 1992 LYS A CG    1 
ATOM   3641  C  CD    . LYS A 1 1992 ? 190.896 222.881 184.514 1.00 98.07  ? 1992 LYS A CD    1 
ATOM   3642  C  CE    . LYS A 1 1992 ? 190.157 223.261 183.242 1.00 90.80  ? 1992 LYS A CE    1 
ATOM   3643  N  NZ    . LYS A 1 1992 ? 190.481 224.648 182.804 1.00 79.09  ? 1992 LYS A NZ    1 
ATOM   3644  N  N     . THR A 1 1993 ? 186.219 219.470 185.277 1.00 106.22 ? 1993 THR A N     1 
ATOM   3645  C  CA    . THR A 1 1993 ? 184.781 219.447 185.509 1.00 105.17 ? 1993 THR A CA    1 
ATOM   3646  C  C     . THR A 1 1993 ? 184.366 218.452 186.584 1.00 106.70 ? 1993 THR A C     1 
ATOM   3647  O  O     . THR A 1 1993 ? 183.222 218.510 187.048 1.00 102.32 ? 1993 THR A O     1 
ATOM   3648  C  CB    . THR A 1 1993 ? 184.044 219.125 184.208 1.00 103.87 ? 1993 THR A CB    1 
ATOM   3649  O  OG1   . THR A 1 1993 ? 184.484 217.856 183.708 1.00 105.36 ? 1993 THR A OG1   1 
ATOM   3650  C  CG2   . THR A 1 1993 ? 184.317 220.197 183.164 1.00 88.66  ? 1993 THR A CG2   1 
ATOM   3651  N  N     . SER A 1 1994 ? 185.255 217.549 186.990 1.00 106.43 ? 1994 SER A N     1 
ATOM   3652  C  CA    . SER A 1 1994 ? 184.939 216.562 188.014 1.00 99.82  ? 1994 SER A CA    1 
ATOM   3653  C  C     . SER A 1 1994 ? 185.143 217.179 189.398 1.00 100.48 ? 1994 SER A C     1 
ATOM   3654  O  O     . SER A 1 1994 ? 185.292 218.396 189.549 1.00 96.62  ? 1994 SER A O     1 
ATOM   3655  C  CB    . SER A 1 1994 ? 185.776 215.302 187.813 1.00 95.55  ? 1994 SER A CB    1 
ATOM   3656  O  OG    . SER A 1 1994 ? 187.161 215.579 187.914 1.00 95.93  ? 1994 SER A OG    1 
ATOM   3657  N  N     . ALA A 1 1995 ? 185.139 216.339 190.428 1.00 99.91  ? 1995 ALA A N     1 
ATOM   3658  C  CA    . ALA A 1 1995 ? 185.294 216.830 191.788 1.00 92.75  ? 1995 ALA A CA    1 
ATOM   3659  C  C     . ALA A 1 1995 ? 186.671 217.466 191.967 1.00 89.50  ? 1995 ALA A C     1 
ATOM   3660  O  O     . ALA A 1 1995 ? 187.684 216.875 191.573 1.00 88.55  ? 1995 ALA A O     1 
ATOM   3661  C  CB    . ALA A 1 1995 ? 185.108 215.693 192.794 1.00 79.51  ? 1995 ALA A CB    1 
ATOM   3662  N  N     . PRO A 1 1996 ? 186.745 218.665 192.541 1.00 84.84  ? 1996 PRO A N     1 
ATOM   3663  C  CA    . PRO A 1 1996 ? 188.049 219.301 192.755 1.00 78.58  ? 1996 PRO A CA    1 
ATOM   3664  C  C     . PRO A 1 1996 ? 188.906 218.505 193.725 1.00 70.86  ? 1996 PRO A C     1 
ATOM   3665  O  O     . PRO A 1 1996 ? 188.404 217.820 194.619 1.00 68.32  ? 1996 PRO A O     1 
ATOM   3666  C  CB    . PRO A 1 1996 ? 187.683 220.672 193.337 1.00 71.40  ? 1996 PRO A CB    1 
ATOM   3667  C  CG    . PRO A 1 1996 ? 186.294 220.926 192.851 1.00 78.33  ? 1996 PRO A CG    1 
ATOM   3668  C  CD    . PRO A 1 1996 ? 185.630 219.579 192.843 1.00 80.94  ? 1996 PRO A CD    1 
ATOM   3669  N  N     . ILE A 1 1997 ? 190.219 218.602 193.536 1.00 60.65  ? 1997 ILE A N     1 
ATOM   3670  C  CA    . ILE A 1 1997 ? 191.166 217.911 194.403 1.00 53.82  ? 1997 ILE A CA    1 
ATOM   3671  C  C     . ILE A 1 1997 ? 191.208 218.622 195.747 1.00 49.50  ? 1997 ILE A C     1 
ATOM   3672  O  O     . ILE A 1 1997 ? 191.417 219.838 195.813 1.00 42.32  ? 1997 ILE A O     1 
ATOM   3673  C  CB    . ILE A 1 1997 ? 192.565 217.843 193.774 1.00 49.03  ? 1997 ILE A CB    1 
ATOM   3674  C  CG1   . ILE A 1 1997 ? 192.547 217.036 192.474 1.00 55.17  ? 1997 ILE A CG1   1 
ATOM   3675  C  CG2   . ILE A 1 1997 ? 193.559 217.243 194.753 1.00 48.48  ? 1997 ILE A CG2   1 
ATOM   3676  C  CD1   . ILE A 1 1997 ? 192.253 217.848 191.253 1.00 56.03  ? 1997 ILE A CD1   1 
ATOM   3677  N  N     . THR A 1 1998 ? 191.005 217.865 196.821 1.00 45.38  ? 1998 THR A N     1 
ATOM   3678  C  CA    . THR A 1 1998 ? 191.078 218.384 198.176 1.00 40.97  ? 1998 THR A CA    1 
ATOM   3679  C  C     . THR A 1 1998 ? 192.051 217.535 198.978 1.00 37.26  ? 1998 THR A C     1 
ATOM   3680  O  O     . THR A 1 1998 ? 192.276 216.360 198.683 1.00 42.23  ? 1998 THR A O     1 
ATOM   3681  C  CB    . THR A 1 1998 ? 189.704 218.398 198.868 1.00 44.42  ? 1998 THR A CB    1 
ATOM   3682  O  OG1   . THR A 1 1998 ? 189.398 217.087 199.359 1.00 48.07  ? 1998 THR A OG1   1 
ATOM   3683  C  CG2   . THR A 1 1998 ? 188.612 218.843 197.906 1.00 41.87  ? 1998 THR A CG2   1 
ATOM   3684  N  N     . CYS A 1 1999 ? 192.638 218.155 199.996 1.00 33.30  ? 1999 CYS A N     1 
ATOM   3685  C  CA    . CYS A 1 1999 ? 193.545 217.474 200.904 1.00 37.04  ? 1999 CYS A CA    1 
ATOM   3686  C  C     . CYS A 1 1999 ? 193.081 217.691 202.335 1.00 38.60  ? 1999 CYS A C     1 
ATOM   3687  O  O     . CYS A 1 1999 ? 192.415 218.682 202.647 1.00 35.99  ? 1999 CYS A O     1 
ATOM   3688  C  CB    . CYS A 1 1999 ? 194.992 217.964 200.737 1.00 35.55  ? 1999 CYS A CB    1 
ATOM   3689  S  SG    . CYS A 1 1999 ? 195.339 219.566 201.491 1.00 51.49  ? 1999 CYS A SG    1 
ATOM   3690  N  N     . GLU A 1 2000 ? 193.425 216.742 203.200 1.00 34.66  ? 2000 GLU A N     1 
ATOM   3691  C  CA    . GLU A 1 2000 ? 193.071 216.808 204.615 1.00 31.92  ? 2000 GLU A CA    1 
ATOM   3692  C  C     . GLU A 1 2000 ? 194.093 217.695 205.314 1.00 34.76  ? 2000 GLU A C     1 
ATOM   3693  O  O     . GLU A 1 2000 ? 195.216 217.272 205.595 1.00 38.91  ? 2000 GLU A O     1 
ATOM   3694  C  CB    . GLU A 1 2000 ? 193.015 215.408 205.218 1.00 39.73  ? 2000 GLU A CB    1 
ATOM   3695  C  CG    . GLU A 1 2000 ? 192.440 215.336 206.626 1.00 48.24  ? 2000 GLU A CG    1 
ATOM   3696  C  CD    . GLU A 1 2000 ? 193.478 215.604 207.700 1.00 53.81  ? 2000 GLU A CD    1 
ATOM   3697  O  OE1   . GLU A 1 2000 ? 194.668 215.307 207.467 1.00 55.47  ? 2000 GLU A OE1   1 
ATOM   3698  O  OE2   . GLU A 1 2000 ? 193.105 216.106 208.780 1.00 49.94  ? 2000 GLU A OE2   1 
ATOM   3699  N  N     . LEU A 1 2001 ? 193.704 218.940 205.581 1.00 32.60  ? 2001 LEU A N     1 
ATOM   3700  C  CA    . LEU A 1 2001 ? 194.543 219.901 206.284 1.00 27.51  ? 2001 LEU A CA    1 
ATOM   3701  C  C     . LEU A 1 2001 ? 193.792 220.392 207.511 1.00 27.78  ? 2001 LEU A C     1 
ATOM   3702  O  O     . LEU A 1 2001 ? 192.733 221.016 207.382 1.00 25.44  ? 2001 LEU A O     1 
ATOM   3703  C  CB    . LEU A 1 2001 ? 194.917 221.074 205.378 1.00 23.74  ? 2001 LEU A CB    1 
ATOM   3704  C  CG    . LEU A 1 2001 ? 196.292 221.019 204.712 1.00 20.29  ? 2001 LEU A CG    1 
ATOM   3705  C  CD1   . LEU A 1 2001 ? 196.465 222.189 203.759 1.00 13.05  ? 2001 LEU A CD1   1 
ATOM   3706  C  CD2   . LEU A 1 2001 ? 197.391 221.007 205.758 1.00 18.31  ? 2001 LEU A CD2   1 
ATOM   3707  N  N     . LEU A 1 2002 ? 194.345 220.116 208.692 1.00 29.06  ? 2002 LEU A N     1 
ATOM   3708  C  CA    . LEU A 1 2002 ? 193.753 220.529 209.965 1.00 32.11  ? 2002 LEU A CA    1 
ATOM   3709  C  C     . LEU A 1 2002 ? 192.319 220.018 210.099 1.00 34.66  ? 2002 LEU A C     1 
ATOM   3710  O  O     . LEU A 1 2002 ? 191.401 220.759 210.458 1.00 38.66  ? 2002 LEU A O     1 
ATOM   3711  C  CB    . LEU A 1 2002 ? 193.816 222.049 210.129 1.00 34.23  ? 2002 LEU A CB    1 
ATOM   3712  C  CG    . LEU A 1 2002 ? 195.212 222.650 210.305 1.00 23.04  ? 2002 LEU A CG    1 
ATOM   3713  C  CD1   . LEU A 1 2002 ? 195.117 224.075 210.809 1.00 26.30  ? 2002 LEU A CD1   1 
ATOM   3714  C  CD2   . LEU A 1 2002 ? 196.046 221.805 211.250 1.00 24.94  ? 2002 LEU A CD2   1 
ATOM   3715  N  N     . ASN A 1 2003 ? 192.135 218.730 209.796 1.00 34.85  ? 2003 ASN A N     1 
ATOM   3716  C  CA    . ASN A 1 2003 ? 190.840 218.054 209.902 1.00 36.99  ? 2003 ASN A CA    1 
ATOM   3717  C  C     . ASN A 1 2003 ? 189.781 218.704 209.016 1.00 35.82  ? 2003 ASN A C     1 
ATOM   3718  O  O     . ASN A 1 2003 ? 188.596 218.716 209.352 1.00 38.49  ? 2003 ASN A O     1 
ATOM   3719  C  CB    . ASN A 1 2003 ? 190.358 217.992 211.355 1.00 32.01  ? 2003 ASN A CB    1 
ATOM   3720  C  CG    . ASN A 1 2003 ? 191.327 217.257 212.256 1.00 36.96  ? 2003 ASN A CG    1 
ATOM   3721  O  OD1   . ASN A 1 2003 ? 192.108 216.424 211.798 1.00 35.96  ? 2003 ASN A OD1   1 
ATOM   3722  N  ND2   . ASN A 1 2003 ? 191.279 217.559 213.548 1.00 47.78  ? 2003 ASN A ND2   1 
ATOM   3723  N  N     . LYS A 1 2004 ? 190.201 219.251 207.880 1.00 35.41  ? 2004 LYS A N     1 
ATOM   3724  C  CA    . LYS A 1 2004 ? 189.291 219.897 206.948 1.00 32.83  ? 2004 LYS A CA    1 
ATOM   3725  C  C     . LYS A 1 2004 ? 189.725 219.569 205.527 1.00 34.00  ? 2004 LYS A C     1 
ATOM   3726  O  O     . LYS A 1 2004 ? 190.905 219.340 205.256 1.00 36.04  ? 2004 LYS A O     1 
ATOM   3727  C  CB    . LYS A 1 2004 ? 189.258 221.415 207.176 1.00 34.93  ? 2004 LYS A CB    1 
ATOM   3728  C  CG    . LYS A 1 2004 ? 188.307 222.179 206.280 1.00 42.13  ? 2004 LYS A CG    1 
ATOM   3729  C  CD    . LYS A 1 2004 ? 188.254 223.644 206.673 1.00 49.27  ? 2004 LYS A CD    1 
ATOM   3730  C  CE    . LYS A 1 2004 ? 189.525 224.372 206.264 1.00 50.83  ? 2004 LYS A CE    1 
ATOM   3731  N  NZ    . LYS A 1 2004 ? 189.436 225.835 206.538 1.00 59.03  ? 2004 LYS A NZ    1 
ATOM   3732  N  N     . GLN A 1 2005 ? 188.755 219.549 204.616 1.00 35.02  ? 2005 GLN A N     1 
ATOM   3733  C  CA    . GLN A 1 2005 ? 189.024 219.356 203.195 1.00 33.89  ? 2005 GLN A CA    1 
ATOM   3734  C  C     . GLN A 1 2005 ? 189.351 220.714 202.585 1.00 36.05  ? 2005 GLN A C     1 
ATOM   3735  O  O     . GLN A 1 2005 ? 188.505 221.613 202.563 1.00 37.74  ? 2005 GLN A O     1 
ATOM   3736  C  CB    . GLN A 1 2005 ? 187.832 218.710 202.497 1.00 32.25  ? 2005 GLN A CB    1 
ATOM   3737  C  CG    . GLN A 1 2005 ? 187.565 217.278 202.919 1.00 33.20  ? 2005 GLN A CG    1 
ATOM   3738  C  CD    . GLN A 1 2005 ? 188.764 216.375 202.704 1.00 37.14  ? 2005 GLN A CD    1 
ATOM   3739  O  OE1   . GLN A 1 2005 ? 189.262 216.239 201.588 1.00 43.91  ? 2005 GLN A OE1   1 
ATOM   3740  N  NE2   . GLN A 1 2005 ? 189.231 215.751 203.777 1.00 33.79  ? 2005 GLN A NE2   1 
ATOM   3741  N  N     . VAL A 1 2006 ? 190.578 220.862 202.091 1.00 33.43  ? 2006 VAL A N     1 
ATOM   3742  C  CA    . VAL A 1 2006 ? 191.078 222.126 201.567 1.00 26.29  ? 2006 VAL A CA    1 
ATOM   3743  C  C     . VAL A 1 2006 ? 191.433 221.929 200.101 1.00 28.32  ? 2006 VAL A C     1 
ATOM   3744  O  O     . VAL A 1 2006 ? 192.169 220.997 199.757 1.00 35.99  ? 2006 VAL A O     1 
ATOM   3745  C  CB    . VAL A 1 2006 ? 192.295 222.618 202.369 1.00 25.27  ? 2006 VAL A CB    1 
ATOM   3746  C  CG1   . VAL A 1 2006 ? 193.000 223.749 201.639 1.00 22.06  ? 2006 VAL A CG1   1 
ATOM   3747  C  CG2   . VAL A 1 2006 ? 191.872 223.048 203.762 1.00 25.46  ? 2006 VAL A CG2   1 
ATOM   3748  N  N     . LYS A 1 2007 ? 190.902 222.795 199.241 1.00 27.25  ? 2007 LYS A N     1 
ATOM   3749  C  CA    . LYS A 1 2007 ? 191.205 222.719 197.819 1.00 29.09  ? 2007 LYS A CA    1 
ATOM   3750  C  C     . LYS A 1 2007 ? 192.657 223.106 197.570 1.00 25.90  ? 2007 LYS A C     1 
ATOM   3751  O  O     . LYS A 1 2007 ? 193.150 224.096 198.118 1.00 21.41  ? 2007 LYS A O     1 
ATOM   3752  C  CB    . LYS A 1 2007 ? 190.269 223.630 197.027 1.00 24.23  ? 2007 LYS A CB    1 
ATOM   3753  C  CG    . LYS A 1 2007 ? 188.827 223.156 197.007 1.00 31.61  ? 2007 LYS A CG    1 
ATOM   3754  C  CD    . LYS A 1 2007 ? 187.916 224.161 196.327 1.00 34.24  ? 2007 LYS A CD    1 
ATOM   3755  C  CE    . LYS A 1 2007 ? 188.166 224.204 194.831 1.00 36.80  ? 2007 LYS A CE    1 
ATOM   3756  N  NZ    . LYS A 1 2007 ? 187.205 225.097 194.129 1.00 40.71  ? 2007 LYS A NZ    1 
ATOM   3757  N  N     . VAL A 1 2008 ? 193.342 222.327 196.738 1.00 24.23  ? 2008 VAL A N     1 
ATOM   3758  C  CA    . VAL A 1 2008 ? 194.756 222.536 196.444 1.00 17.81  ? 2008 VAL A CA    1 
ATOM   3759  C  C     . VAL A 1 2008 ? 194.876 223.010 195.005 1.00 17.47  ? 2008 VAL A C     1 
ATOM   3760  O  O     . VAL A 1 2008 ? 194.518 222.283 194.069 1.00 24.97  ? 2008 VAL A O     1 
ATOM   3761  C  CB    . VAL A 1 2008 ? 195.576 221.259 196.676 1.00 19.85  ? 2008 VAL A CB    1 
ATOM   3762  C  CG1   . VAL A 1 2008 ? 197.060 221.565 196.601 1.00 18.28  ? 2008 VAL A CG1   1 
ATOM   3763  C  CG2   . VAL A 1 2008 ? 195.221 220.639 198.014 1.00 22.12  ? 2008 VAL A CG2   1 
ATOM   3764  N  N     . SER A 1 2009 ? 195.378 224.226 194.828 1.00 17.45  ? 2009 SER A N     1 
ATOM   3765  C  CA    . SER A 1 2009 ? 195.594 224.752 193.489 1.00 16.06  ? 2009 SER A CA    1 
ATOM   3766  C  C     . SER A 1 2009 ? 196.847 224.130 192.878 1.00 16.98  ? 2009 SER A C     1 
ATOM   3767  O  O     . SER A 1 2009 ? 197.809 223.838 193.595 1.00 20.28  ? 2009 SER A O     1 
ATOM   3768  C  CB    . SER A 1 2009 ? 195.726 226.273 193.531 1.00 14.95  ? 2009 SER A CB    1 
ATOM   3769  O  OG    . SER A 1 2009 ? 196.061 226.799 192.260 1.00 17.94  ? 2009 SER A OG    1 
ATOM   3770  N  N     . PRO A 1 2010 ? 196.866 223.907 191.562 1.00 17.86  ? 2010 PRO A N     1 
ATOM   3771  C  CA    . PRO A 1 2010 ? 198.080 223.369 190.928 1.00 20.78  ? 2010 PRO A CA    1 
ATOM   3772  C  C     . PRO A 1 2010 ? 199.279 224.295 191.017 1.00 19.37  ? 2010 PRO A C     1 
ATOM   3773  O  O     . PRO A 1 2010 ? 200.418 223.821 190.922 1.00 17.63  ? 2010 PRO A O     1 
ATOM   3774  C  CB    . PRO A 1 2010 ? 197.651 223.152 189.472 1.00 21.98  ? 2010 PRO A CB    1 
ATOM   3775  C  CG    . PRO A 1 2010 ? 196.495 224.078 189.276 1.00 25.15  ? 2010 PRO A CG    1 
ATOM   3776  C  CD    . PRO A 1 2010 ? 195.780 224.114 190.590 1.00 21.46  ? 2010 PRO A CD    1 
ATOM   3777  N  N     . ASP A 1 2011 ? 199.066 225.596 191.197 1.00 16.30  ? 2011 ASP A N     1 
ATOM   3778  C  CA    . ASP A 1 2011 ? 200.158 226.560 191.213 1.00 11.42  ? 2011 ASP A CA    1 
ATOM   3779  C  C     . ASP A 1 2011 ? 200.849 226.657 192.565 1.00 12.84  ? 2011 ASP A C     1 
ATOM   3780  O  O     . ASP A 1 2011 ? 201.805 227.429 192.697 1.00 14.65  ? 2011 ASP A O     1 
ATOM   3781  C  CB    . ASP A 1 2011 ? 199.647 227.940 190.795 1.00 11.61  ? 2011 ASP A CB    1 
ATOM   3782  C  CG    . ASP A 1 2011 ? 199.331 228.020 189.315 1.00 26.03  ? 2011 ASP A CG    1 
ATOM   3783  O  OD1   . ASP A 1 2011 ? 199.156 226.957 188.685 1.00 27.91  ? 2011 ASP A OD1   1 
ATOM   3784  O  OD2   . ASP A 1 2011 ? 199.264 229.145 188.778 1.00 35.89  ? 2011 ASP A OD2   1 
ATOM   3785  N  N     . MET A 1 2012 ? 200.393 225.907 193.566 1.00 9.87   ? 2012 MET A N     1 
ATOM   3786  C  CA    . MET A 1 2012 ? 201.049 225.921 194.864 1.00 8.56   ? 2012 MET A CA    1 
ATOM   3787  C  C     . MET A 1 2012 ? 202.455 225.348 194.772 1.00 9.19   ? 2012 MET A C     1 
ATOM   3788  O  O     . MET A 1 2012 ? 202.722 224.419 194.005 1.00 7.85   ? 2012 MET A O     1 
ATOM   3789  C  CB    . MET A 1 2012 ? 200.242 225.119 195.884 1.00 10.24  ? 2012 MET A CB    1 
ATOM   3790  C  CG    . MET A 1 2012 ? 200.847 225.167 197.275 1.00 12.81  ? 2012 MET A CG    1 
ATOM   3791  S  SD    . MET A 1 2012 ? 199.897 224.313 198.528 1.00 49.26  ? 2012 MET A SD    1 
ATOM   3792  C  CE    . MET A 1 2012 ? 200.965 224.505 199.950 1.00 15.77  ? 2012 MET A CE    1 
ATOM   3793  N  N     . ALA A 1 2013 ? 203.358 225.911 195.570 1.00 6.79   ? 2013 ALA A N     1 
ATOM   3794  C  CA    . ALA A 1 2013 ? 204.693 225.365 195.739 1.00 4.25   ? 2013 ALA A CA    1 
ATOM   3795  C  C     . ALA A 1 2013 ? 205.148 225.635 197.163 1.00 4.65   ? 2013 ALA A C     1 
ATOM   3796  O  O     . ALA A 1 2013 ? 204.776 226.644 197.767 1.00 7.58   ? 2013 ALA A O     1 
ATOM   3797  C  CB    . ALA A 1 2013 ? 205.683 225.969 194.739 1.00 4.84   ? 2013 ALA A CB    1 
ATOM   3798  N  N     . ILE A 1 2014 ? 205.949 224.719 197.697 1.00 3.32   ? 2014 ILE A N     1 
ATOM   3799  C  CA    . ILE A 1 2014 ? 206.556 224.870 199.011 1.00 3.17   ? 2014 ILE A CA    1 
ATOM   3800  C  C     . ILE A 1 2014 ? 208.066 224.843 198.837 1.00 3.21   ? 2014 ILE A C     1 
ATOM   3801  O  O     . ILE A 1 2014 ? 208.613 223.900 198.256 1.00 2.93   ? 2014 ILE A O     1 
ATOM   3802  C  CB    . ILE A 1 2014 ? 206.097 223.771 199.988 1.00 3.31   ? 2014 ILE A CB    1 
ATOM   3803  C  CG1   . ILE A 1 2014 ? 204.571 223.726 200.062 1.00 4.13   ? 2014 ILE A CG1   1 
ATOM   3804  C  CG2   . ILE A 1 2014 ? 206.689 224.000 201.368 1.00 3.81   ? 2014 ILE A CG2   1 
ATOM   3805  C  CD1   . ILE A 1 2014 ? 204.032 222.506 200.768 1.00 6.93   ? 2014 ILE A CD1   1 
ATOM   3806  N  N     . PHE A 1 2015 ? 208.734 225.881 199.328 1.00 3.60   ? 2015 PHE A N     1 
ATOM   3807  C  CA    . PHE A 1 2015 ? 210.183 225.975 199.285 1.00 2.56   ? 2015 PHE A CA    1 
ATOM   3808  C  C     . PHE A 1 2015 ? 210.703 226.251 200.685 1.00 2.89   ? 2015 PHE A C     1 
ATOM   3809  O  O     . PHE A 1 2015 ? 210.113 227.039 201.429 1.00 4.72   ? 2015 PHE A O     1 
ATOM   3810  C  CB    . PHE A 1 2015 ? 210.649 227.075 198.328 1.00 3.52   ? 2015 PHE A CB    1 
ATOM   3811  C  CG    . PHE A 1 2015 ? 210.451 226.743 196.880 1.00 2.72   ? 2015 PHE A CG    1 
ATOM   3812  C  CD1   . PHE A 1 2015 ? 209.251 227.012 196.251 1.00 2.95   ? 2015 PHE A CD1   1 
ATOM   3813  C  CD2   . PHE A 1 2015 ? 211.468 226.165 196.145 1.00 2.13   ? 2015 PHE A CD2   1 
ATOM   3814  C  CE1   . PHE A 1 2015 ? 209.070 226.710 194.920 1.00 3.03   ? 2015 PHE A CE1   1 
ATOM   3815  C  CE2   . PHE A 1 2015 ? 211.291 225.861 194.815 1.00 3.22   ? 2015 PHE A CE2   1 
ATOM   3816  C  CZ    . PHE A 1 2015 ? 210.091 226.134 194.202 1.00 3.29   ? 2015 PHE A CZ    1 
ATOM   3817  N  N     . ILE A 1 2016 ? 211.796 225.575 201.046 1.00 3.22   ? 2016 ILE A N     1 
ATOM   3818  C  CA    . ILE A 1 2016 ? 212.375 225.734 202.412 1.00 4.56   ? 2016 ILE A CA    1 
ATOM   3819  C  C     . ILE A 1 2016 ? 213.877 226.028 202.277 1.00 5.64   ? 2016 ILE A C     1 
ATOM   3820  O  O     . ILE A 1 2016 ? 214.615 225.155 201.775 1.00 5.56   ? 2016 ILE A O     1 
ATOM   3821  C  CB    . ILE A 1 2016 ? 212.096 224.482 203.262 1.00 4.15   ? 2016 ILE A CB    1 
ATOM   3822  C  CG1   . ILE A 1 2016 ? 212.568 223.206 202.568 1.00 3.61   ? 2016 ILE A CG1   1 
ATOM   3823  C  CG2   . ILE A 1 2016 ? 210.613 224.401 203.621 1.00 3.37   ? 2016 ILE A CG2   1 
ATOM   3824  C  CD1   . ILE A 1 2016 ? 212.579 221.980 203.461 1.00 4.06   ? 2016 ILE A CD1   1 
ATOM   3825  N  N     . THR A 1 2017 ? 214.304 227.224 202.683 1.00 7.31   ? 2017 THR A N     1 
ATOM   3826  C  CA    . THR A 1 2017 ? 215.738 227.571 202.632 1.00 6.41   ? 2017 THR A CA    1 
ATOM   3827  C  C     . THR A 1 2017 ? 216.302 227.434 204.026 1.00 7.93   ? 2017 THR A C     1 
ATOM   3828  O  O     . THR A 1 2017 ? 215.749 228.071 204.947 1.00 13.02  ? 2017 THR A O     1 
ATOM   3829  C  CB    . THR A 1 2017 ? 215.907 228.985 202.081 1.00 9.15   ? 2017 THR A CB    1 
ATOM   3830  O  OG1   . THR A 1 2017 ? 215.326 229.847 203.053 1.00 13.62  ? 2017 THR A OG1   1 
ATOM   3831  C  CG2   . THR A 1 2017 ? 215.210 229.176 200.746 1.00 8.94   ? 2017 THR A CG2   1 
ATOM   3832  N  N     . MET A 1 2018 ? 217.351 226.626 204.193 1.00 7.42   ? 2018 MET A N     1 
ATOM   3833  C  CA    . MET A 1 2018 ? 217.901 226.376 205.550 1.00 8.86   ? 2018 MET A CA    1 
ATOM   3834  C  C     . MET A 1 2018 ? 219.432 226.482 205.519 1.00 9.05   ? 2018 MET A C     1 
ATOM   3835  O  O     . MET A 1 2018 ? 220.027 226.130 204.479 1.00 7.08   ? 2018 MET A O     1 
ATOM   3836  C  CB    . MET A 1 2018 ? 217.491 224.986 206.046 1.00 10.08  ? 2018 MET A CB    1 
ATOM   3837  C  CG    . MET A 1 2018 ? 217.749 223.876 205.050 1.00 13.38  ? 2018 MET A CG    1 
ATOM   3838  S  SD    . MET A 1 2018 ? 216.888 222.370 205.540 1.00 8.43   ? 2018 MET A SD    1 
ATOM   3839  C  CE    . MET A 1 2018 ? 215.247 223.063 205.782 1.00 5.84   ? 2018 MET A CE    1 
ATOM   3840  N  N     . ASN A 1 2019 ? 220.035 226.959 206.611 1.00 11.76  ? 2019 ASN A N     1 
ATOM   3841  C  CA    . ASN A 1 2019 ? 221.518 227.050 206.693 1.00 10.06  ? 2019 ASN A CA    1 
ATOM   3842  C  C     . ASN A 1 2019 ? 222.036 225.887 207.541 1.00 11.69  ? 2019 ASN A C     1 
ATOM   3843  O  O     . ASN A 1 2019 ? 221.989 225.992 208.784 1.00 14.35  ? 2019 ASN A O     1 
ATOM   3844  C  CB    . ASN A 1 2019 ? 221.974 228.385 207.269 1.00 10.94  ? 2019 ASN A CB    1 
ATOM   3845  C  CG    . ASN A 1 2019 ? 221.527 229.558 206.431 1.00 12.68  ? 2019 ASN A CG    1 
ATOM   3846  O  OD1   . ASN A 1 2019 ? 220.865 229.373 205.404 1.00 22.12  ? 2019 ASN A OD1   1 
ATOM   3847  N  ND2   . ASN A 1 2019 ? 221.874 230.766 206.848 1.00 12.12  ? 2019 ASN A ND2   1 
ATOM   3848  N  N     . PRO A 1 2020 ? 222.521 224.784 206.933 1.00 13.69  ? 2020 PRO A N     1 
ATOM   3849  C  CA    . PRO A 1 2020 ? 222.969 223.632 207.699 1.00 15.49  ? 2020 PRO A CA    1 
ATOM   3850  C  C     . PRO A 1 2020 ? 224.224 223.952 208.496 1.00 20.50  ? 2020 PRO A C     1 
ATOM   3851  O  O     . PRO A 1 2020 ? 225.159 224.544 207.921 1.00 19.65  ? 2020 PRO A O     1 
ATOM   3852  C  CB    . PRO A 1 2020 ? 223.229 222.574 206.615 1.00 13.55  ? 2020 PRO A CB    1 
ATOM   3853  C  CG    . PRO A 1 2020 ? 222.507 223.100 205.395 1.00 13.65  ? 2020 PRO A CG    1 
ATOM   3854  C  CD    . PRO A 1 2020 ? 222.645 224.605 205.502 1.00 12.18  ? 2020 PRO A CD    1 
ATOM   3855  N  N     . GLY A 1 2021 ? 224.254 223.579 209.780 1.00 14.38  ? 2021 GLY A N     1 
ATOM   3856  C  CA    . GLY A 1 2021 ? 225.468 223.774 210.598 1.00 17.21  ? 2021 GLY A CA    1 
ATOM   3857  C  C     . GLY A 1 2021 ? 225.364 224.965 211.530 1.00 16.75  ? 2021 GLY A C     1 
ATOM   3858  O  O     . GLY A 1 2021 ? 226.176 225.038 212.474 1.00 20.64  ? 2021 GLY A O     1 
ATOM   3859  N  N     . TYR A 1 2022 ? 224.408 225.866 211.294 1.00 16.92  ? 2022 TYR A N     1 
ATOM   3860  C  CA    . TYR A 1 2022 ? 224.306 227.102 212.120 1.00 16.94  ? 2022 TYR A CA    1 
ATOM   3861  C  C     . TYR A 1 2022 ? 223.724 226.751 213.492 1.00 22.49  ? 2022 TYR A C     1 
ATOM   3862  O  O     . TYR A 1 2022 ? 223.226 225.620 213.674 1.00 23.29  ? 2022 TYR A O     1 
ATOM   3863  C  CB    . TYR A 1 2022 ? 223.469 228.170 211.409 1.00 13.59  ? 2022 TYR A CB    1 
ATOM   3864  C  CG    . TYR A 1 2022 ? 224.169 228.897 210.268 1.00 18.24  ? 2022 TYR A CG    1 
ATOM   3865  C  CD1   . TYR A 1 2022 ? 223.890 230.230 209.992 1.00 18.33  ? 2022 TYR A CD1   1 
ATOM   3866  C  CD2   . TYR A 1 2022 ? 225.101 228.252 209.465 1.00 15.44  ? 2022 TYR A CD2   1 
ATOM   3867  C  CE1   . TYR A 1 2022 ? 224.522 230.900 208.957 1.00 13.80  ? 2022 TYR A CE1   1 
ATOM   3868  C  CE2   . TYR A 1 2022 ? 225.737 228.910 208.426 1.00 17.03  ? 2022 TYR A CE2   1 
ATOM   3869  C  CZ    . TYR A 1 2022 ? 225.447 230.237 208.171 1.00 16.15  ? 2022 TYR A CZ    1 
ATOM   3870  O  OH    . TYR A 1 2022 ? 226.073 230.889 207.149 1.00 21.65  ? 2022 TYR A OH    1 
ATOM   3871  N  N     . ALA A 1 2023 ? 223.783 227.698 214.435 1.00 23.71  ? 2023 ALA A N     1 
ATOM   3872  C  CA    . ALA A 1 2023 ? 223.249 227.457 215.798 1.00 15.98  ? 2023 ALA A CA    1 
ATOM   3873  C  C     . ALA A 1 2023 ? 221.765 227.822 215.845 1.00 18.06  ? 2023 ALA A C     1 
ATOM   3874  O  O     . ALA A 1 2023 ? 221.345 228.727 215.091 1.00 19.63  ? 2023 ALA A O     1 
ATOM   3875  C  CB    . ALA A 1 2023 ? 224.043 228.252 216.810 1.00 14.10  ? 2023 ALA A CB    1 
ATOM   3876  N  N     . GLY A 1 2024 ? 220.998 227.147 216.706 1.00 23.44  ? 2024 GLY A N     1 
ATOM   3877  C  CA    . GLY A 1 2024 ? 219.548 227.404 216.802 1.00 16.81  ? 2024 GLY A CA    1 
ATOM   3878  C  C     . GLY A 1 2024 ? 218.797 226.649 215.725 1.00 15.84  ? 2024 GLY A C     1 
ATOM   3879  O  O     . GLY A 1 2024 ? 217.573 226.862 215.599 1.00 20.27  ? 2024 GLY A O     1 
ATOM   3880  N  N     . ARG A 1 2025 ? 219.499 225.795 214.974 1.00 15.27  ? 2025 ARG A N     1 
ATOM   3881  C  CA    . ARG A 1 2025 ? 218.866 225.023 213.875 1.00 12.88  ? 2025 ARG A CA    1 
ATOM   3882  C  C     . ARG A 1 2025 ? 218.645 223.573 214.334 1.00 15.08  ? 2025 ARG A C     1 
ATOM   3883  O  O     . ARG A 1 2025 ? 219.482 223.066 215.111 1.00 17.92  ? 2025 ARG A O     1 
ATOM   3884  C  CB    . ARG A 1 2025 ? 219.737 225.077 212.616 1.00 12.58  ? 2025 ARG A CB    1 
ATOM   3885  C  CG    . ARG A 1 2025 ? 219.570 226.325 211.763 1.00 11.28  ? 2025 ARG A CG    1 
ATOM   3886  C  CD    . ARG A 1 2025 ? 219.982 227.612 212.456 1.00 13.23  ? 2025 ARG A CD    1 
ATOM   3887  N  NE    . ARG A 1 2025 ? 219.975 228.734 211.510 1.00 19.36  ? 2025 ARG A NE    1 
ATOM   3888  C  CZ    . ARG A 1 2025 ? 220.327 229.978 211.804 1.00 21.69  ? 2025 ARG A CZ    1 
ATOM   3889  N  NH1   . ARG A 1 2025 ? 220.554 230.322 213.059 1.00 17.51  ? 2025 ARG A NH1   1 
ATOM   3890  N  NH2   . ARG A 1 2025 ? 220.454 230.870 210.839 1.00 15.97  ? 2025 ARG A NH2   1 
ATOM   3891  N  N     . SER A 1 2026 ? 217.565 222.940 213.869 1.00 15.10  ? 2026 SER A N     1 
ATOM   3892  C  CA    . SER A 1 2026 ? 217.250 221.545 214.271 1.00 14.55  ? 2026 SER A CA    1 
ATOM   3893  C  C     . SER A 1 2026 ? 217.609 220.577 213.137 1.00 16.10  ? 2026 SER A C     1 
ATOM   3894  O  O     . SER A 1 2026 ? 218.077 221.052 212.080 1.00 21.75  ? 2026 SER A O     1 
ATOM   3895  C  CB    . SER A 1 2026 ? 215.800 221.408 214.657 1.00 14.85  ? 2026 SER A CB    1 
ATOM   3896  O  OG    . SER A 1 2026 ? 215.467 222.302 215.709 1.00 19.98  ? 2026 SER A OG    1 
ATOM   3897  N  N     . ASN A 1 2027 ? 217.395 219.277 213.351 1.00 19.33  ? 2027 ASN A N     1 
ATOM   3898  C  CA    . ASN A 1 2027 ? 217.695 218.280 212.334 1.00 15.71  ? 2027 ASN A CA    1 
ATOM   3899  C  C     . ASN A 1 2027 ? 216.397 217.831 211.679 1.00 16.93  ? 2027 ASN A C     1 
ATOM   3900  O  O     . ASN A 1 2027 ? 215.438 217.473 212.371 1.00 23.45  ? 2027 ASN A O     1 
ATOM   3901  C  CB    . ASN A 1 2027 ? 218.430 217.081 212.938 1.00 19.18  ? 2027 ASN A CB    1 
ATOM   3902  C  CG    . ASN A 1 2027 ? 219.933 217.199 212.812 1.00 24.76  ? 2027 ASN A CG    1 
ATOM   3903  O  OD1   . ASN A 1 2027 ? 220.445 217.749 211.838 1.00 28.13  ? 2027 ASN A OD1   1 
ATOM   3904  N  ND2   . ASN A 1 2027 ? 220.652 216.680 213.799 1.00 26.93  ? 2027 ASN A ND2   1 
ATOM   3905  N  N     . LEU A 1 2028 ? 216.368 217.860 210.353 1.00 14.03  ? 2028 LEU A N     1 
ATOM   3906  C  CA    . LEU A 1 2028 ? 215.170 217.467 209.630 1.00 9.21   ? 2028 LEU A CA    1 
ATOM   3907  C  C     . LEU A 1 2028 ? 215.019 215.948 209.642 1.00 11.87  ? 2028 LEU A C     1 
ATOM   3908  O  O     . LEU A 1 2028 ? 216.003 215.225 209.461 1.00 14.65  ? 2028 LEU A O     1 
ATOM   3909  C  CB    . LEU A 1 2028 ? 215.225 217.973 208.191 1.00 9.25   ? 2028 LEU A CB    1 
ATOM   3910  C  CG    . LEU A 1 2028 ? 214.492 219.278 207.886 1.00 9.46   ? 2028 LEU A CG    1 
ATOM   3911  C  CD1   . LEU A 1 2028 ? 215.213 220.458 208.511 1.00 6.51   ? 2028 LEU A CD1   1 
ATOM   3912  C  CD2   . LEU A 1 2028 ? 214.357 219.464 206.386 1.00 10.57  ? 2028 LEU A CD2   1 
ATOM   3913  N  N     . PRO A 1 2029 ? 213.811 215.436 209.863 1.00 15.70  ? 2029 PRO A N     1 
ATOM   3914  C  CA    . PRO A 1 2029 ? 213.592 213.992 209.732 1.00 10.34  ? 2029 PRO A CA    1 
ATOM   3915  C  C     . PRO A 1 2029 ? 213.748 213.537 208.290 1.00 11.78  ? 2029 PRO A C     1 
ATOM   3916  O  O     . PRO A 1 2029 ? 213.567 214.309 207.345 1.00 11.61  ? 2029 PRO A O     1 
ATOM   3917  C  CB    . PRO A 1 2029 ? 212.154 213.801 210.227 1.00 8.13   ? 2029 PRO A CB    1 
ATOM   3918  C  CG    . PRO A 1 2029 ? 211.522 215.141 210.107 1.00 9.42   ? 2029 PRO A CG    1 
ATOM   3919  C  CD    . PRO A 1 2029 ? 212.610 216.141 210.338 1.00 11.65  ? 2029 PRO A CD    1 
ATOM   3920  N  N     . ASP A 1 2030 ? 214.099 212.259 208.132 1.00 11.49  ? 2030 ASP A N     1 
ATOM   3921  C  CA    . ASP A 1 2030 ? 214.371 211.716 206.805 1.00 12.33  ? 2030 ASP A CA    1 
ATOM   3922  C  C     . ASP A 1 2030 ? 213.126 211.722 205.925 1.00 13.24  ? 2030 ASP A C     1 
ATOM   3923  O  O     . ASP A 1 2030 ? 213.215 211.982 204.718 1.00 16.47  ? 2030 ASP A O     1 
ATOM   3924  C  CB    . ASP A 1 2030 ? 214.935 210.301 206.927 1.00 19.57  ? 2030 ASP A CB    1 
ATOM   3925  C  CG    . ASP A 1 2030 ? 216.318 210.279 207.544 1.00 27.65  ? 2030 ASP A CG    1 
ATOM   3926  O  OD1   . ASP A 1 2030 ? 216.821 209.175 207.837 1.00 25.58  ? 2030 ASP A OD1   1 
ATOM   3927  O  OD2   . ASP A 1 2030 ? 216.902 211.366 207.737 1.00 29.62  ? 2030 ASP A OD2   1 
ATOM   3928  N  N     . ASN A 1 2031 ? 211.960 211.426 206.503 1.00 10.13  ? 2031 ASN A N     1 
ATOM   3929  C  CA    . ASN A 1 2031 ? 210.729 211.432 205.720 1.00 12.81  ? 2031 ASN A CA    1 
ATOM   3930  C  C     . ASN A 1 2031 ? 210.405 212.823 205.192 1.00 12.48  ? 2031 ASN A C     1 
ATOM   3931  O  O     . ASN A 1 2031 ? 209.925 212.958 204.061 1.00 12.72  ? 2031 ASN A O     1 
ATOM   3932  C  CB    . ASN A 1 2031 ? 209.567 210.896 206.555 1.00 12.20  ? 2031 ASN A CB    1 
ATOM   3933  C  CG    . ASN A 1 2031 ? 209.484 211.545 207.918 1.00 14.72  ? 2031 ASN A CG    1 
ATOM   3934  O  OD1   . ASN A 1 2031 ? 210.372 211.377 208.753 1.00 19.32  ? 2031 ASN A OD1   1 
ATOM   3935  N  ND2   . ASN A 1 2031 ? 208.413 212.291 208.153 1.00 10.85  ? 2031 ASN A ND2   1 
ATOM   3936  N  N     . LEU A 1 2032 ? 210.646 213.861 205.994 1.00 8.53   ? 2032 LEU A N     1 
ATOM   3937  C  CA    . LEU A 1 2032 ? 210.460 215.225 205.513 1.00 6.83   ? 2032 LEU A CA    1 
ATOM   3938  C  C     . LEU A 1 2032 ? 211.489 215.578 204.447 1.00 7.55   ? 2032 LEU A C     1 
ATOM   3939  O  O     . LEU A 1 2032 ? 211.167 216.254 203.464 1.00 7.31   ? 2032 LEU A O     1 
ATOM   3940  C  CB    . LEU A 1 2032 ? 210.535 216.207 206.681 1.00 8.53   ? 2032 LEU A CB    1 
ATOM   3941  C  CG    . LEU A 1 2032 ? 210.475 217.696 206.338 1.00 5.56   ? 2032 LEU A CG    1 
ATOM   3942  C  CD1   . LEU A 1 2032 ? 209.097 218.068 205.821 1.00 4.04   ? 2032 LEU A CD1   1 
ATOM   3943  C  CD2   . LEU A 1 2032 ? 210.845 218.537 207.545 1.00 6.44   ? 2032 LEU A CD2   1 
ATOM   3944  N  N     . LYS A 1 2033 ? 212.734 215.127 204.625 1.00 8.67   ? 2033 LYS A N     1 
ATOM   3945  C  CA    . LYS A 1 2033 ? 213.779 215.429 203.655 1.00 6.32   ? 2033 LYS A CA    1 
ATOM   3946  C  C     . LYS A 1 2033 ? 213.506 214.779 202.306 1.00 7.92   ? 2033 LYS A C     1 
ATOM   3947  O  O     . LYS A 1 2033 ? 213.824 215.363 201.264 1.00 13.16  ? 2033 LYS A O     1 
ATOM   3948  C  CB    . LYS A 1 2033 ? 215.142 214.991 204.192 1.00 5.44   ? 2033 LYS A CB    1 
ATOM   3949  C  CG    . LYS A 1 2033 ? 215.778 216.001 205.132 1.00 8.76   ? 2033 LYS A CG    1 
ATOM   3950  C  CD    . LYS A 1 2033 ? 217.258 215.731 205.342 1.00 8.51   ? 2033 LYS A CD    1 
ATOM   3951  C  CE    . LYS A 1 2033 ? 217.486 214.536 206.245 1.00 14.76  ? 2033 LYS A CE    1 
ATOM   3952  N  NZ    . LYS A 1 2033 ? 218.900 214.453 206.698 1.00 17.14  ? 2033 LYS A NZ    1 
ATOM   3953  N  N     . LYS A 1 2034 ? 212.919 213.582 202.297 1.00 7.57   ? 2034 LYS A N     1 
ATOM   3954  C  CA    . LYS A 1 2034 ? 212.594 212.929 201.035 1.00 8.25   ? 2034 LYS A CA    1 
ATOM   3955  C  C     . LYS A 1 2034 ? 211.489 213.645 200.269 1.00 9.77   ? 2034 LYS A C     1 
ATOM   3956  O  O     . LYS A 1 2034 ? 211.295 213.356 199.083 1.00 17.90  ? 2034 LYS A O     1 
ATOM   3957  C  CB    . LYS A 1 2034 ? 212.194 211.472 201.282 1.00 12.30  ? 2034 LYS A CB    1 
ATOM   3958  C  CG    . LYS A 1 2034 ? 210.699 211.245 201.413 1.00 13.26  ? 2034 LYS A CG    1 
ATOM   3959  C  CD    . LYS A 1 2034 ? 210.394 209.830 201.863 1.00 20.69  ? 2034 LYS A CD    1 
ATOM   3960  C  CE    . LYS A 1 2034 ? 208.896 209.586 201.915 1.00 33.28  ? 2034 LYS A CE    1 
ATOM   3961  N  NZ    . LYS A 1 2034 ? 208.289 209.575 200.556 1.00 40.64  ? 2034 LYS A NZ    1 
ATOM   3962  N  N     . LEU A 1 2035 ? 210.771 214.565 200.907 1.00 6.22   ? 2035 LEU A N     1 
ATOM   3963  C  CA    . LEU A 1 2035 ? 209.712 215.325 200.258 1.00 5.52   ? 2035 LEU A CA    1 
ATOM   3964  C  C     . LEU A 1 2035 ? 210.225 216.553 199.521 1.00 5.98   ? 2035 LEU A C     1 
ATOM   3965  O  O     . LEU A 1 2035 ? 209.432 217.241 198.871 1.00 4.67   ? 2035 LEU A O     1 
ATOM   3966  C  CB    . LEU A 1 2035 ? 208.663 215.753 201.289 1.00 7.68   ? 2035 LEU A CB    1 
ATOM   3967  C  CG    . LEU A 1 2035 ? 207.828 214.652 201.943 1.00 7.88   ? 2035 LEU A CG    1 
ATOM   3968  C  CD1   . LEU A 1 2035 ? 206.902 215.248 202.985 1.00 7.18   ? 2035 LEU A CD1   1 
ATOM   3969  C  CD2   . LEU A 1 2035 ? 207.038 213.886 200.900 1.00 8.06   ? 2035 LEU A CD2   1 
ATOM   3970  N  N     . PHE A 1 2036 ? 211.520 216.847 199.607 1.00 7.73   ? 2036 PHE A N     1 
ATOM   3971  C  CA    . PHE A 1 2036 ? 212.104 218.015 198.969 1.00 3.80   ? 2036 PHE A CA    1 
ATOM   3972  C  C     . PHE A 1 2036 ? 213.317 217.609 198.147 1.00 4.73   ? 2036 PHE A C     1 
ATOM   3973  O  O     . PHE A 1 2036 ? 214.065 216.699 198.514 1.00 7.95   ? 2036 PHE A O     1 
ATOM   3974  C  CB    . PHE A 1 2036 ? 212.517 219.076 200.001 1.00 2.98   ? 2036 PHE A CB    1 
ATOM   3975  C  CG    . PHE A 1 2036 ? 211.367 219.654 200.775 1.00 4.23   ? 2036 PHE A CG    1 
ATOM   3976  C  CD1   . PHE A 1 2036 ? 210.914 219.040 201.929 1.00 4.23   ? 2036 PHE A CD1   1 
ATOM   3977  C  CD2   . PHE A 1 2036 ? 210.743 220.813 200.351 1.00 3.92   ? 2036 PHE A CD2   1 
ATOM   3978  C  CE1   . PHE A 1 2036 ? 209.858 219.567 202.641 1.00 3.12   ? 2036 PHE A CE1   1 
ATOM   3979  C  CE2   . PHE A 1 2036 ? 209.685 221.345 201.060 1.00 4.09   ? 2036 PHE A CE2   1 
ATOM   3980  C  CZ    . PHE A 1 2036 ? 209.244 220.721 202.207 1.00 3.83   ? 2036 PHE A CZ    1 
ATOM   3981  N  N     . ARG A 1 2037 ? 213.499 218.297 197.023 1.00 4.37   ? 2037 ARG A N     1 
ATOM   3982  C  CA    . ARG A 1 2037 ? 214.693 218.164 196.196 1.00 4.65   ? 2037 ARG A CA    1 
ATOM   3983  C  C     . ARG A 1 2037 ? 215.720 219.164 196.712 1.00 3.51   ? 2037 ARG A C     1 
ATOM   3984  O  O     . ARG A 1 2037 ? 215.502 220.376 196.637 1.00 3.10   ? 2037 ARG A O     1 
ATOM   3985  C  CB    . ARG A 1 2037 ? 214.365 218.426 194.729 1.00 5.18   ? 2037 ARG A CB    1 
ATOM   3986  C  CG    . ARG A 1 2037 ? 215.532 218.247 193.779 1.00 8.40   ? 2037 ARG A CG    1 
ATOM   3987  C  CD    . ARG A 1 2037 ? 215.967 216.800 193.716 1.00 8.17   ? 2037 ARG A CD    1 
ATOM   3988  N  NE    . ARG A 1 2037 ? 214.877 215.954 193.248 1.00 13.14  ? 2037 ARG A NE    1 
ATOM   3989  C  CZ    . ARG A 1 2037 ? 214.579 215.756 191.971 1.00 14.88  ? 2037 ARG A CZ    1 
ATOM   3990  N  NH1   . ARG A 1 2037 ? 215.287 216.312 191.002 1.00 10.06  ? 2037 ARG A NH1   1 
ATOM   3991  N  NH2   . ARG A 1 2037 ? 213.542 214.984 191.657 1.00 12.83  ? 2037 ARG A NH2   1 
ATOM   3992  N  N     . SER A 1 2038 ? 216.823 218.663 197.255 1.00 4.91   ? 2038 SER A N     1 
ATOM   3993  C  CA    . SER A 1 2038 ? 217.811 219.542 197.856 1.00 4.31   ? 2038 SER A CA    1 
ATOM   3994  C  C     . SER A 1 2038 ? 218.782 220.070 196.804 1.00 5.48   ? 2038 SER A C     1 
ATOM   3995  O  O     . SER A 1 2038 ? 218.993 219.465 195.750 1.00 9.76   ? 2038 SER A O     1 
ATOM   3996  C  CB    . SER A 1 2038 ? 218.578 218.821 198.963 1.00 3.64   ? 2038 SER A CB    1 
ATOM   3997  O  OG    . SER A 1 2038 ? 219.379 217.778 198.438 1.00 11.63  ? 2038 SER A OG    1 
ATOM   3998  N  N     . LEU A 1 2039 ? 219.371 221.223 197.107 1.00 4.19   ? 2039 LEU A N     1 
ATOM   3999  C  CA    . LEU A 1 2039 ? 220.337 221.848 196.209 1.00 4.30   ? 2039 LEU A CA    1 
ATOM   4000  C  C     . LEU A 1 2039 ? 221.335 222.652 197.024 1.00 4.89   ? 2039 LEU A C     1 
ATOM   4001  O  O     . LEU A 1 2039 ? 220.940 223.510 197.816 1.00 5.29   ? 2039 LEU A O     1 
ATOM   4002  C  CB    . LEU A 1 2039 ? 219.646 222.749 195.194 1.00 6.61   ? 2039 LEU A CB    1 
ATOM   4003  C  CG    . LEU A 1 2039 ? 220.616 223.383 194.199 1.00 5.13   ? 2039 LEU A CG    1 
ATOM   4004  C  CD1   . LEU A 1 2039 ? 221.317 222.334 193.348 1.00 6.01   ? 2039 LEU A CD1   1 
ATOM   4005  C  CD2   . LEU A 1 2039 ? 219.880 224.362 193.343 1.00 4.16   ? 2039 LEU A CD2   1 
ATOM   4006  N  N     . ALA A 1 2040 ? 222.621 222.401 196.800 1.00 4.48   ? 2040 ALA A N     1 
ATOM   4007  C  CA    . ALA A 1 2040 ? 223.685 223.073 197.539 1.00 3.42   ? 2040 ALA A CA    1 
ATOM   4008  C  C     . ALA A 1 2040 ? 224.007 224.391 196.845 1.00 6.31   ? 2040 ALA A C     1 
ATOM   4009  O  O     . ALA A 1 2040 ? 224.514 224.409 195.721 1.00 15.42  ? 2040 ALA A O     1 
ATOM   4010  C  CB    . ALA A 1 2040 ? 224.918 222.183 197.638 1.00 5.94   ? 2040 ALA A CB    1 
ATOM   4011  N  N     . MET A 1 2041 ? 223.700 225.497 197.515 1.00 6.31   ? 2041 MET A N     1 
ATOM   4012  C  CA    . MET A 1 2041 ? 224.086 226.832 197.063 1.00 4.91   ? 2041 MET A CA    1 
ATOM   4013  C  C     . MET A 1 2041 ? 225.128 227.345 198.050 1.00 5.95   ? 2041 MET A C     1 
ATOM   4014  O  O     . MET A 1 2041 ? 224.798 227.896 199.099 1.00 7.37   ? 2041 MET A O     1 
ATOM   4015  C  CB    . MET A 1 2041 ? 222.876 227.754 196.978 1.00 4.98   ? 2041 MET A CB    1 
ATOM   4016  C  CG    . MET A 1 2041 ? 221.945 227.454 195.818 1.00 7.24   ? 2041 MET A CG    1 
ATOM   4017  S  SD    . MET A 1 2041 ? 220.536 228.573 195.752 1.00 22.38  ? 2041 MET A SD    1 
ATOM   4018  C  CE    . MET A 1 2041 ? 221.316 230.058 195.129 1.00 4.51   ? 2041 MET A CE    1 
ATOM   4019  N  N     . THR A 1 2042 ? 226.401 227.156 197.710 1.00 5.93   ? 2042 THR A N     1 
ATOM   4020  C  CA    . THR A 1 2042 ? 227.502 227.485 198.606 1.00 6.40   ? 2042 THR A CA    1 
ATOM   4021  C  C     . THR A 1 2042 ? 228.420 228.567 198.059 1.00 9.69   ? 2042 THR A C     1 
ATOM   4022  O  O     . THR A 1 2042 ? 228.855 229.444 198.812 1.00 16.91  ? 2042 THR A O     1 
ATOM   4023  C  CB    . THR A 1 2042 ? 228.321 226.224 198.918 1.00 7.42   ? 2042 THR A CB    1 
ATOM   4024  O  OG1   . THR A 1 2042 ? 228.815 225.657 197.701 1.00 14.58  ? 2042 THR A OG1   1 
ATOM   4025  C  CG2   . THR A 1 2042 ? 227.460 225.202 199.635 1.00 7.00   ? 2042 THR A CG2   1 
ATOM   4026  N  N     . LYS A 1 2043 ? 228.734 228.529 196.766 1.00 8.28   ? 2043 LYS A N     1 
ATOM   4027  C  CA    . LYS A 1 2043 ? 229.648 229.499 196.171 1.00 9.85   ? 2043 LYS A CA    1 
ATOM   4028  C  C     . LYS A 1 2043 ? 228.928 230.298 195.097 1.00 11.54  ? 2043 LYS A C     1 
ATOM   4029  O  O     . LYS A 1 2043 ? 228.856 229.857 193.939 1.00 14.72  ? 2043 LYS A O     1 
ATOM   4030  C  CB    . LYS A 1 2043 ? 230.873 228.794 195.582 1.00 11.73  ? 2043 LYS A CB    1 
ATOM   4031  C  CG    . LYS A 1 2043 ? 231.996 228.567 196.575 1.00 17.71  ? 2043 LYS A CG    1 
ATOM   4032  C  CD    . LYS A 1 2043 ? 233.347 228.539 195.879 1.00 29.53  ? 2043 LYS A CD    1 
ATOM   4033  C  CE    . LYS A 1 2043 ? 234.477 228.335 196.873 1.00 37.57  ? 2043 LYS A CE    1 
ATOM   4034  N  NZ    . LYS A 1 2043 ? 235.808 228.328 196.205 1.00 35.70  ? 2043 LYS A NZ    1 
ATOM   4035  N  N     . PRO A 1 2044 ? 228.380 231.468 195.418 1.00 11.94  ? 2044 PRO A N     1 
ATOM   4036  C  CA    . PRO A 1 2044 ? 227.769 232.299 194.378 1.00 9.41   ? 2044 PRO A CA    1 
ATOM   4037  C  C     . PRO A 1 2044 ? 228.814 232.848 193.420 1.00 9.12   ? 2044 PRO A C     1 
ATOM   4038  O  O     . PRO A 1 2044 ? 229.968 233.075 193.790 1.00 11.49  ? 2044 PRO A O     1 
ATOM   4039  C  CB    . PRO A 1 2044 ? 227.088 233.414 195.176 1.00 7.37   ? 2044 PRO A CB    1 
ATOM   4040  C  CG    . PRO A 1 2044 ? 227.912 233.534 196.400 1.00 9.55   ? 2044 PRO A CG    1 
ATOM   4041  C  CD    . PRO A 1 2044 ? 228.391 232.142 196.727 1.00 7.81   ? 2044 PRO A CD    1 
ATOM   4042  N  N     . ASP A 1 2045 ? 228.397 233.055 192.171 1.00 10.80  ? 2045 ASP A N     1 
ATOM   4043  C  CA    . ASP A 1 2045 ? 229.285 233.564 191.125 1.00 10.52  ? 2045 ASP A CA    1 
ATOM   4044  C  C     . ASP A 1 2045 ? 229.418 235.071 191.301 1.00 9.37   ? 2045 ASP A C     1 
ATOM   4045  O  O     . ASP A 1 2045 ? 228.774 235.880 190.628 1.00 9.36   ? 2045 ASP A O     1 
ATOM   4046  C  CB    . ASP A 1 2045 ? 228.760 233.190 189.748 1.00 10.26  ? 2045 ASP A CB    1 
ATOM   4047  C  CG    . ASP A 1 2045 ? 228.439 231.719 189.635 1.00 14.06  ? 2045 ASP A CG    1 
ATOM   4048  O  OD1   . ASP A 1 2045 ? 229.371 230.894 189.735 1.00 16.90  ? 2045 ASP A OD1   1 
ATOM   4049  O  OD2   . ASP A 1 2045 ? 227.253 231.379 189.470 1.00 16.44  ? 2045 ASP A OD2   1 
ATOM   4050  N  N     . ARG A 1 2046 ? 230.291 235.442 192.233 1.00 9.28   ? 2046 ARG A N     1 
ATOM   4051  C  CA    . ARG A 1 2046 ? 230.399 236.830 192.661 1.00 10.37  ? 2046 ARG A CA    1 
ATOM   4052  C  C     . ARG A 1 2046 ? 230.919 237.737 191.549 1.00 9.19   ? 2046 ARG A C     1 
ATOM   4053  O  O     . ARG A 1 2046 ? 230.466 238.882 191.422 1.00 9.64   ? 2046 ARG A O     1 
ATOM   4054  C  CB    . ARG A 1 2046 ? 231.292 236.900 193.904 1.00 11.59  ? 2046 ARG A CB    1 
ATOM   4055  C  CG    . ARG A 1 2046 ? 231.383 238.283 194.506 1.00 24.80  ? 2046 ARG A CG    1 
ATOM   4056  C  CD    . ARG A 1 2046 ? 232.235 238.355 195.762 1.00 37.19  ? 2046 ARG A CD    1 
ATOM   4057  N  NE    . ARG A 1 2046 ? 231.686 237.590 196.875 1.00 35.91  ? 2046 ARG A NE    1 
ATOM   4058  C  CZ    . ARG A 1 2046 ? 232.252 236.504 197.382 1.00 29.56  ? 2046 ARG A CZ    1 
ATOM   4059  N  NH1   . ARG A 1 2046 ? 233.369 236.013 196.877 1.00 31.14  ? 2046 ARG A NH1   1 
ATOM   4060  N  NH2   . ARG A 1 2046 ? 231.679 235.892 198.415 1.00 22.14  ? 2046 ARG A NH2   1 
ATOM   4061  N  N     . GLN A 1 2047 ? 231.853 237.246 190.732 1.00 9.20   ? 2047 GLN A N     1 
ATOM   4062  C  CA    . GLN A 1 2047 ? 232.416 238.065 189.666 1.00 7.99   ? 2047 GLN A CA    1 
ATOM   4063  C  C     . GLN A 1 2047 ? 231.351 238.459 188.652 1.00 9.12   ? 2047 GLN A C     1 
ATOM   4064  O  O     . GLN A 1 2047 ? 231.277 239.620 188.234 1.00 10.45  ? 2047 GLN A O     1 
ATOM   4065  C  CB    . GLN A 1 2047 ? 233.557 237.315 188.983 1.00 10.96  ? 2047 GLN A CB    1 
ATOM   4066  C  CG    . GLN A 1 2047 ? 234.551 238.208 188.264 1.00 9.63   ? 2047 GLN A CG    1 
ATOM   4067  C  CD    . GLN A 1 2047 ? 234.234 238.355 186.789 1.00 18.24  ? 2047 GLN A CD    1 
ATOM   4068  O  OE1   . GLN A 1 2047 ? 233.586 237.496 186.194 1.00 19.14  ? 2047 GLN A OE1   1 
ATOM   4069  N  NE2   . GLN A 1 2047 ? 234.698 239.444 186.190 1.00 17.57  ? 2047 GLN A NE2   1 
ATOM   4070  N  N     . LEU A 1 2048 ? 230.518 237.497 188.249 1.00 9.41   ? 2048 LEU A N     1 
ATOM   4071  C  CA    . LEU A 1 2048 ? 229.467 237.780 187.236 1.00 7.92   ? 2048 LEU A CA    1 
ATOM   4072  C  C     . LEU A 1 2048 ? 228.489 238.824 187.799 1.00 8.04   ? 2048 LEU A C     1 
ATOM   4073  O  O     . LEU A 1 2048 ? 228.185 239.798 187.080 1.00 9.44   ? 2048 LEU A O     1 
ATOM   4074  C  CB    . LEU A 1 2048 ? 228.751 236.494 186.830 1.00 7.74   ? 2048 LEU A CB    1 
ATOM   4075  C  CG    . LEU A 1 2048 ? 227.633 236.647 185.793 1.00 6.65   ? 2048 LEU A CG    1 
ATOM   4076  C  CD1   . LEU A 1 2048 ? 228.161 237.303 184.530 1.00 7.44   ? 2048 LEU A CD1   1 
ATOM   4077  C  CD2   . LEU A 1 2048 ? 227.007 235.302 185.474 1.00 6.03   ? 2048 LEU A CD2   1 
ATOM   4078  N  N     . ILE A 1 2049 ? 228.000 238.605 189.022 1.00 6.39   ? 2049 ILE A N     1 
ATOM   4079  C  CA    . ILE A 1 2049 ? 227.053 239.565 189.664 1.00 6.21   ? 2049 ILE A CA    1 
ATOM   4080  C  C     . ILE A 1 2049 ? 227.683 240.962 189.615 1.00 8.81   ? 2049 ILE A C     1 
ATOM   4081  O  O     . ILE A 1 2049 ? 227.050 241.882 189.056 1.00 11.90  ? 2049 ILE A O     1 
ATOM   4082  C  CB    . ILE A 1 2049 ? 226.751 239.139 191.111 1.00 5.91   ? 2049 ILE A CB    1 
ATOM   4083  C  CG1   . ILE A 1 2049 ? 226.100 237.760 191.160 1.00 4.81   ? 2049 ILE A CG1   1 
ATOM   4084  C  CG2   . ILE A 1 2049 ? 225.902 240.189 191.826 1.00 5.47   ? 2049 ILE A CG2   1 
ATOM   4085  C  CD1   . ILE A 1 2049 ? 225.881 237.228 192.563 1.00 3.78   ? 2049 ILE A CD1   1 
ATOM   4086  N  N     . ALA A 1 2050 ? 228.886 241.101 190.167 1.00 8.15   ? 2050 ALA A N     1 
ATOM   4087  C  CA    . ALA A 1 2050 ? 229.571 242.413 190.210 1.00 5.74   ? 2050 ALA A CA    1 
ATOM   4088  C  C     . ALA A 1 2050 ? 229.618 243.010 188.804 1.00 8.85   ? 2050 ALA A C     1 
ATOM   4089  O  O     . ALA A 1 2050 ? 229.249 244.191 188.644 1.00 13.36  ? 2050 ALA A O     1 
ATOM   4090  C  CB    . ALA A 1 2050 ? 230.957 242.249 190.784 1.00 6.51   ? 2050 ALA A CB    1 
ATOM   4091  N  N     . GLN A 1 2051 ? 230.047 242.219 187.816 1.00 8.01   ? 2051 GLN A N     1 
ATOM   4092  C  CA    . GLN A 1 2051 ? 230.173 242.736 186.457 1.00 6.50   ? 2051 GLN A CA    1 
ATOM   4093  C  C     . GLN A 1 2051 ? 228.830 243.219 185.927 1.00 9.65   ? 2051 GLN A C     1 
ATOM   4094  O  O     . GLN A 1 2051 ? 228.719 244.338 185.413 1.00 12.80  ? 2051 GLN A O     1 
ATOM   4095  C  CB    . GLN A 1 2051 ? 230.765 241.660 185.544 1.00 10.53  ? 2051 GLN A CB    1 
ATOM   4096  C  CG    . GLN A 1 2051 ? 231.130 242.129 184.140 1.00 14.66  ? 2051 GLN A CG    1 
ATOM   4097  C  CD    . GLN A 1 2051 ? 229.959 242.079 183.176 1.00 26.78  ? 2051 GLN A CD    1 
ATOM   4098  O  OE1   . GLN A 1 2051 ? 229.058 241.253 183.317 1.00 37.58  ? 2051 GLN A OE1   1 
ATOM   4099  N  NE2   . GLN A 1 2051 ? 229.965 242.970 182.192 1.00 24.91  ? 2051 GLN A NE2   1 
ATOM   4100  N  N     . VAL A 1 2052 ? 227.790 242.393 186.058 1.00 10.20  ? 2052 VAL A N     1 
ATOM   4101  C  CA    . VAL A 1 2052 ? 226.487 242.756 185.509 1.00 7.83   ? 2052 VAL A CA    1 
ATOM   4102  C  C     . VAL A 1 2052 ? 225.901 243.951 186.251 1.00 8.43   ? 2052 VAL A C     1 
ATOM   4103  O  O     . VAL A 1 2052 ? 225.353 244.870 185.632 1.00 12.68  ? 2052 VAL A O     1 
ATOM   4104  C  CB    . VAL A 1 2052 ? 225.536 241.547 185.530 1.00 5.33   ? 2052 VAL A CB    1 
ATOM   4105  C  CG1   . VAL A 1 2052 ? 224.150 241.954 185.060 1.00 3.85   ? 2052 VAL A CG1   1 
ATOM   4106  C  CG2   . VAL A 1 2052 ? 226.081 240.443 184.649 1.00 4.66   ? 2052 VAL A CG2   1 
ATOM   4107  N  N     . MET A 1 2053 ? 226.004 243.965 187.584 1.00 7.94   ? 2053 MET A N     1 
ATOM   4108  C  CA    . MET A 1 2053 ? 225.465 245.090 188.339 1.00 8.66   ? 2053 MET A CA    1 
ATOM   4109  C  C     . MET A 1 2053 ? 226.165 246.392 187.979 1.00 10.11  ? 2053 MET A C     1 
ATOM   4110  O  O     . MET A 1 2053 ? 225.503 247.411 187.757 1.00 13.89  ? 2053 MET A O     1 
ATOM   4111  C  CB    . MET A 1 2053 ? 225.565 244.830 189.840 1.00 10.92  ? 2053 MET A CB    1 
ATOM   4112  C  CG    . MET A 1 2053 ? 224.641 243.745 190.345 1.00 10.46  ? 2053 MET A CG    1 
ATOM   4113  S  SD    . MET A 1 2053 ? 224.600 243.717 192.140 1.00 28.83  ? 2053 MET A SD    1 
ATOM   4114  C  CE    . MET A 1 2053 ? 223.285 244.894 192.437 1.00 23.02  ? 2053 MET A CE    1 
ATOM   4115  N  N     . LEU A 1 2054 ? 227.498 246.383 187.903 1.00 10.19  ? 2054 LEU A N     1 
ATOM   4116  C  CA    . LEU A 1 2054 ? 228.209 247.604 187.543 1.00 9.06   ? 2054 LEU A CA    1 
ATOM   4117  C  C     . LEU A 1 2054 ? 227.893 248.030 186.114 1.00 10.72  ? 2054 LEU A C     1 
ATOM   4118  O  O     . LEU A 1 2054 ? 227.764 249.226 185.834 1.00 11.54  ? 2054 LEU A O     1 
ATOM   4119  C  CB    . LEU A 1 2054 ? 229.711 247.414 187.742 1.00 7.52   ? 2054 LEU A CB    1 
ATOM   4120  C  CG    . LEU A 1 2054 ? 230.146 247.352 189.207 1.00 7.37   ? 2054 LEU A CG    1 
ATOM   4121  C  CD1   . LEU A 1 2054 ? 231.640 247.139 189.321 1.00 11.08  ? 2054 LEU A CD1   1 
ATOM   4122  C  CD2   . LEU A 1 2054 ? 229.728 248.615 189.942 1.00 9.11   ? 2054 LEU A CD2   1 
ATOM   4123  N  N     . TYR A 1 2055 ? 227.754 247.068 185.199 1.00 13.22  ? 2055 TYR A N     1 
ATOM   4124  C  CA    . TYR A 1 2055 ? 227.416 247.403 183.821 1.00 10.10  ? 2055 TYR A CA    1 
ATOM   4125  C  C     . TYR A 1 2055 ? 226.031 248.029 183.729 1.00 10.72  ? 2055 TYR A C     1 
ATOM   4126  O  O     . TYR A 1 2055 ? 225.801 248.933 182.916 1.00 12.47  ? 2055 TYR A O     1 
ATOM   4127  C  CB    . TYR A 1 2055 ? 227.506 246.152 182.948 1.00 9.46   ? 2055 TYR A CB    1 
ATOM   4128  C  CG    . TYR A 1 2055 ? 227.412 246.416 181.464 1.00 10.67  ? 2055 TYR A CG    1 
ATOM   4129  C  CD1   . TYR A 1 2055 ? 228.219 247.367 180.857 1.00 13.24  ? 2055 TYR A CD1   1 
ATOM   4130  C  CD2   . TYR A 1 2055 ? 226.521 245.711 180.671 1.00 8.75   ? 2055 TYR A CD2   1 
ATOM   4131  C  CE1   . TYR A 1 2055 ? 228.138 247.609 179.500 1.00 12.59  ? 2055 TYR A CE1   1 
ATOM   4132  C  CE2   . TYR A 1 2055 ? 226.433 245.946 179.315 1.00 11.61  ? 2055 TYR A CE2   1 
ATOM   4133  C  CZ    . TYR A 1 2055 ? 227.243 246.896 178.734 1.00 14.51  ? 2055 TYR A CZ    1 
ATOM   4134  O  OH    . TYR A 1 2055 ? 227.158 247.132 177.382 1.00 21.02  ? 2055 TYR A OH    1 
ATOM   4135  N  N     . SER A 1 2056 ? 225.091 247.561 184.553 1.00 10.06  ? 2056 SER A N     1 
ATOM   4136  C  CA    . SER A 1 2056 ? 223.736 248.101 184.525 1.00 9.84   ? 2056 SER A CA    1 
ATOM   4137  C  C     . SER A 1 2056 ? 223.650 249.501 185.121 1.00 16.21  ? 2056 SER A C     1 
ATOM   4138  O  O     . SER A 1 2056 ? 222.787 250.281 184.706 1.00 26.19  ? 2056 SER A O     1 
ATOM   4139  C  CB    . SER A 1 2056 ? 222.781 247.165 185.265 1.00 10.06  ? 2056 SER A CB    1 
ATOM   4140  O  OG    . SER A 1 2056 ? 223.131 247.060 186.633 1.00 15.13  ? 2056 SER A OG    1 
ATOM   4141  N  N     . GLN A 1 2057 ? 224.515 249.837 186.075 1.00 15.95  ? 2057 GLN A N     1 
ATOM   4142  C  CA    . GLN A 1 2057 ? 224.532 251.163 186.679 1.00 14.15  ? 2057 GLN A CA    1 
ATOM   4143  C  C     . GLN A 1 2057 ? 225.146 252.223 185.776 1.00 18.54  ? 2057 GLN A C     1 
ATOM   4144  O  O     . GLN A 1 2057 ? 225.085 253.410 186.109 1.00 25.94  ? 2057 GLN A O     1 
ATOM   4145  C  CB    . GLN A 1 2057 ? 225.292 251.137 188.010 1.00 16.40  ? 2057 GLN A CB    1 
ATOM   4146  C  CG    . GLN A 1 2057 ? 224.793 250.114 189.013 1.00 16.59  ? 2057 GLN A CG    1 
ATOM   4147  C  CD    . GLN A 1 2057 ? 223.731 250.669 189.936 1.00 25.00  ? 2057 GLN A CD    1 
ATOM   4148  O  OE1   . GLN A 1 2057 ? 222.725 251.217 189.488 1.00 26.60  ? 2057 GLN A OE1   1 
ATOM   4149  N  NE2   . GLN A 1 2057 ? 223.948 250.527 191.237 1.00 21.53  ? 2057 GLN A NE2   1 
ATOM   4150  N  N     . GLY A 1 2058 ? 225.728 251.830 184.649 1.00 13.93  ? 2058 GLY A N     1 
ATOM   4151  C  CA    . GLY A 1 2058 ? 226.392 252.762 183.767 1.00 16.84  ? 2058 GLY A CA    1 
ATOM   4152  C  C     . GLY A 1 2058 ? 227.891 252.850 183.930 1.00 15.63  ? 2058 GLY A C     1 
ATOM   4153  O  O     . GLY A 1 2058 ? 228.493 253.810 183.438 1.00 26.32  ? 2058 GLY A O     1 
ATOM   4154  N  N     . PHE A 1 2059 ? 228.512 251.888 184.606 1.00 13.21  ? 2059 PHE A N     1 
ATOM   4155  C  CA    . PHE A 1 2059 ? 229.957 251.890 184.801 1.00 15.97  ? 2059 PHE A CA    1 
ATOM   4156  C  C     . PHE A 1 2059 ? 230.630 251.384 183.531 1.00 19.81  ? 2059 PHE A C     1 
ATOM   4157  O  O     . PHE A 1 2059 ? 230.491 250.210 183.174 1.00 22.72  ? 2059 PHE A O     1 
ATOM   4158  C  CB    . PHE A 1 2059 ? 230.342 251.011 185.987 1.00 11.51  ? 2059 PHE A CB    1 
ATOM   4159  C  CG    . PHE A 1 2059 ? 230.173 251.671 187.325 1.00 12.79  ? 2059 PHE A CG    1 
ATOM   4160  C  CD1   . PHE A 1 2059 ? 228.936 251.699 187.947 1.00 11.42  ? 2059 PHE A CD1   1 
ATOM   4161  C  CD2   . PHE A 1 2059 ? 231.254 252.241 187.970 1.00 15.22  ? 2059 PHE A CD2   1 
ATOM   4162  C  CE1   . PHE A 1 2059 ? 228.781 252.295 189.180 1.00 10.76  ? 2059 PHE A CE1   1 
ATOM   4163  C  CE2   . PHE A 1 2059 ? 231.103 252.840 189.205 1.00 14.46  ? 2059 PHE A CE2   1 
ATOM   4164  C  CZ    . PHE A 1 2059 ? 229.865 252.865 189.810 1.00 12.20  ? 2059 PHE A CZ    1 
ATOM   4165  N  N     . ARG A 1 2060 ? 231.355 252.261 182.845 1.00 19.15  ? 2060 ARG A N     1 
ATOM   4166  C  CA    . ARG A 1 2060 ? 232.291 251.797 181.832 1.00 20.59  ? 2060 ARG A CA    1 
ATOM   4167  C  C     . ARG A 1 2060 ? 233.402 250.983 182.483 1.00 21.33  ? 2060 ARG A C     1 
ATOM   4168  O  O     . ARG A 1 2060 ? 233.756 251.194 183.645 1.00 25.57  ? 2060 ARG A O     1 
ATOM   4169  C  CB    . ARG A 1 2060 ? 232.880 252.974 181.056 1.00 25.53  ? 2060 ARG A CB    1 
ATOM   4170  C  CG    . ARG A 1 2060 ? 231.868 253.793 180.274 1.00 27.75  ? 2060 ARG A CG    1 
ATOM   4171  C  CD    . ARG A 1 2060 ? 231.337 252.952 179.122 1.00 43.68  ? 2060 ARG A CD    1 
ATOM   4172  N  NE    . ARG A 1 2060 ? 230.408 253.664 178.253 1.00 51.58  ? 2060 ARG A NE    1 
ATOM   4173  C  CZ    . ARG A 1 2060 ? 229.773 253.106 177.232 1.00 57.18  ? 2060 ARG A CZ    1 
ATOM   4174  N  NH1   . ARG A 1 2060 ? 229.931 251.826 176.937 1.00 69.30  ? 2060 ARG A NH1   1 
ATOM   4175  N  NH2   . ARG A 1 2060 ? 228.972 253.852 176.479 1.00 42.91  ? 2060 ARG A NH2   1 
ATOM   4176  N  N     . THR A 1 2061 ? 233.945 250.039 181.718 1.00 23.49  ? 2061 THR A N     1 
ATOM   4177  C  CA    . THR A 1 2061 ? 234.976 249.124 182.207 1.00 26.82  ? 2061 THR A CA    1 
ATOM   4178  C  C     . THR A 1 2061 ? 234.520 248.424 183.487 1.00 17.75  ? 2061 THR A C     1 
ATOM   4179  O  O     . THR A 1 2061 ? 235.237 248.366 184.487 1.00 16.92  ? 2061 THR A O     1 
ATOM   4180  C  CB    . THR A 1 2061 ? 236.307 249.850 182.424 1.00 35.69  ? 2061 THR A CB    1 
ATOM   4181  O  OG1   . THR A 1 2061 ? 236.173 250.800 183.490 1.00 20.81  ? 2061 THR A OG1   1 
ATOM   4182  C  CG2   . THR A 1 2061 ? 236.735 250.570 181.153 1.00 32.50  ? 2061 THR A CG2   1 
ATOM   4183  N  N     . ALA A 1 2062 ? 233.293 247.902 183.451 1.00 20.80  ? 2062 ALA A N     1 
ATOM   4184  C  CA    . ALA A 1 2062 ? 232.778 247.159 184.595 1.00 15.59  ? 2062 ALA A CA    1 
ATOM   4185  C  C     . ALA A 1 2062 ? 233.504 245.833 184.779 1.00 17.70  ? 2062 ALA A C     1 
ATOM   4186  O  O     . ALA A 1 2062 ? 233.580 245.320 185.901 1.00 21.69  ? 2062 ALA A O     1 
ATOM   4187  C  CB    . ALA A 1 2062 ? 231.277 246.924 184.437 1.00 12.11  ? 2062 ALA A CB    1 
ATOM   4188  N  N     . GLU A 1 2063 ? 234.038 245.266 183.694 1.00 16.79  ? 2063 GLU A N     1 
ATOM   4189  C  CA    . GLU A 1 2063 ? 234.728 243.983 183.790 1.00 18.12  ? 2063 GLU A CA    1 
ATOM   4190  C  C     . GLU A 1 2063 ? 235.968 244.081 184.668 1.00 22.05  ? 2063 GLU A C     1 
ATOM   4191  O  O     . GLU A 1 2063 ? 236.178 243.239 185.550 1.00 27.74  ? 2063 GLU A O     1 
ATOM   4192  C  CB    . GLU A 1 2063 ? 235.100 243.483 182.395 1.00 20.36  ? 2063 GLU A CB    1 
ATOM   4193  C  CG    . GLU A 1 2063 ? 233.911 243.262 181.481 1.00 38.09  ? 2063 GLU A CG    1 
ATOM   4194  C  CD    . GLU A 1 2063 ? 234.280 242.507 180.220 1.00 58.39  ? 2063 GLU A CD    1 
ATOM   4195  O  OE1   . GLU A 1 2063 ? 235.466 242.145 180.069 1.00 66.17  ? 2063 GLU A OE1   1 
ATOM   4196  O  OE2   . GLU A 1 2063 ? 233.385 242.274 179.381 1.00 50.98  ? 2063 GLU A OE2   1 
ATOM   4197  N  N     . VAL A 1 2064 ? 236.804 245.098 184.444 1.00 19.17  ? 2064 VAL A N     1 
ATOM   4198  C  CA    . VAL A 1 2064 ? 238.011 245.245 185.253 1.00 14.44  ? 2064 VAL A CA    1 
ATOM   4199  C  C     . VAL A 1 2064 ? 237.645 245.587 186.691 1.00 14.45  ? 2064 VAL A C     1 
ATOM   4200  O  O     . VAL A 1 2064 ? 238.296 245.127 187.638 1.00 16.55  ? 2064 VAL A O     1 
ATOM   4201  C  CB    . VAL A 1 2064 ? 238.961 246.290 184.634 1.00 16.88  ? 2064 VAL A CB    1 
ATOM   4202  C  CG1   . VAL A 1 2064 ? 239.413 245.843 183.251 1.00 19.53  ? 2064 VAL A CG1   1 
ATOM   4203  C  CG2   . VAL A 1 2064 ? 238.308 247.656 184.562 1.00 13.19  ? 2064 VAL A CG2   1 
ATOM   4204  N  N     . LEU A 1 2065 ? 236.586 246.377 186.881 1.00 13.49  ? 2065 LEU A N     1 
ATOM   4205  C  CA    . LEU A 1 2065 ? 236.142 246.699 188.231 1.00 11.35  ? 2065 LEU A CA    1 
ATOM   4206  C  C     . LEU A 1 2065 ? 235.729 245.445 188.991 1.00 11.93  ? 2065 LEU A C     1 
ATOM   4207  O  O     . LEU A 1 2065 ? 236.094 245.273 190.158 1.00 13.91  ? 2065 LEU A O     1 
ATOM   4208  C  CB    . LEU A 1 2065 ? 234.989 247.700 188.184 1.00 10.83  ? 2065 LEU A CB    1 
ATOM   4209  C  CG    . LEU A 1 2065 ? 235.343 249.135 187.795 1.00 11.92  ? 2065 LEU A CG    1 
ATOM   4210  C  CD1   . LEU A 1 2065 ? 234.129 250.035 187.934 1.00 11.75  ? 2065 LEU A CD1   1 
ATOM   4211  C  CD2   . LEU A 1 2065 ? 236.485 249.642 188.654 1.00 14.07  ? 2065 LEU A CD2   1 
ATOM   4212  N  N     . ALA A 1 2066 ? 234.973 244.555 188.343 1.00 13.48  ? 2066 ALA A N     1 
ATOM   4213  C  CA    . ALA A 1 2066 ? 234.577 243.310 188.994 1.00 11.51  ? 2066 ALA A CA    1 
ATOM   4214  C  C     . ALA A 1 2066 ? 235.783 242.416 189.253 1.00 12.95  ? 2066 ALA A C     1 
ATOM   4215  O  O     . ALA A 1 2066 ? 235.936 241.857 190.349 1.00 11.58  ? 2066 ALA A O     1 
ATOM   4216  C  CB    . ALA A 1 2066 ? 233.541 242.581 188.140 1.00 9.90   ? 2066 ALA A CB    1 
ATOM   4217  N  N     . ASN A 1 2067 ? 236.658 242.276 188.252 1.00 13.95  ? 2067 ASN A N     1 
ATOM   4218  C  CA    . ASN A 1 2067 ? 237.841 241.435 188.389 1.00 12.79  ? 2067 ASN A CA    1 
ATOM   4219  C  C     . ASN A 1 2067 ? 238.818 241.977 189.418 1.00 16.32  ? 2067 ASN A C     1 
ATOM   4220  O  O     . ASN A 1 2067 ? 239.732 241.256 189.826 1.00 20.65  ? 2067 ASN A O     1 
ATOM   4221  C  CB    . ASN A 1 2067 ? 238.540 241.288 187.038 1.00 9.19   ? 2067 ASN A CB    1 
ATOM   4222  C  CG    . ASN A 1 2067 ? 237.712 240.513 186.039 1.00 12.19  ? 2067 ASN A CG    1 
ATOM   4223  O  OD1   . ASN A 1 2067 ? 237.282 239.393 186.310 1.00 15.58  ? 2067 ASN A OD1   1 
ATOM   4224  N  ND2   . ASN A 1 2067 ? 237.483 241.105 184.875 1.00 11.90  ? 2067 ASN A ND2   1 
ATOM   4225  N  N     . LYS A 1 2068 ? 238.668 243.237 189.817 1.00 16.20  ? 2068 LYS A N     1 
ATOM   4226  C  CA    . LYS A 1 2068 ? 239.456 243.777 190.914 1.00 14.62  ? 2068 LYS A CA    1 
ATOM   4227  C  C     . LYS A 1 2068 ? 238.742 243.673 192.255 1.00 12.60  ? 2068 LYS A C     1 
ATOM   4228  O  O     . LYS A 1 2068 ? 239.390 243.409 193.273 1.00 16.36  ? 2068 LYS A O     1 
ATOM   4229  C  CB    . LYS A 1 2068 ? 239.807 245.239 190.633 1.00 14.30  ? 2068 LYS A CB    1 
ATOM   4230  C  CG    . LYS A 1 2068 ? 240.867 245.424 189.564 1.00 15.55  ? 2068 LYS A CG    1 
ATOM   4231  C  CD    . LYS A 1 2068 ? 241.173 246.892 189.337 1.00 15.62  ? 2068 LYS A CD    1 
ATOM   4232  C  CE    . LYS A 1 2068 ? 242.455 247.069 188.548 1.00 20.32  ? 2068 LYS A CE    1 
ATOM   4233  N  NZ    . LYS A 1 2068 ? 243.611 246.418 189.215 1.00 21.77  ? 2068 LYS A NZ    1 
ATOM   4234  N  N     . ILE A 1 2069 ? 237.423 243.848 192.280 1.00 10.80  ? 2069 ILE A N     1 
ATOM   4235  C  CA    . ILE A 1 2069 ? 236.713 243.954 193.548 1.00 11.22  ? 2069 ILE A CA    1 
ATOM   4236  C  C     . ILE A 1 2069 ? 236.328 242.594 194.127 1.00 10.56  ? 2069 ILE A C     1 
ATOM   4237  O  O     . ILE A 1 2069 ? 236.181 242.466 195.346 1.00 11.98  ? 2069 ILE A O     1 
ATOM   4238  C  CB    . ILE A 1 2069 ? 235.478 244.862 193.391 1.00 9.30   ? 2069 ILE A CB    1 
ATOM   4239  C  CG1   . ILE A 1 2069 ? 234.998 245.350 194.759 1.00 11.09  ? 2069 ILE A CG1   1 
ATOM   4240  C  CG2   . ILE A 1 2069 ? 234.357 244.142 192.658 1.00 6.86   ? 2069 ILE A CG2   1 
ATOM   4241  C  CD1   . ILE A 1 2069 ? 236.005 246.207 195.483 1.00 10.57  ? 2069 ILE A CD1   1 
ATOM   4242  N  N     . VAL A 1 2070 ? 236.162 241.568 193.297 1.00 10.13  ? 2070 VAL A N     1 
ATOM   4243  C  CA    . VAL A 1 2070 ? 235.809 240.253 193.831 1.00 10.90  ? 2070 VAL A CA    1 
ATOM   4244  C  C     . VAL A 1 2070 ? 237.052 239.586 194.421 1.00 11.00  ? 2070 VAL A C     1 
ATOM   4245  O  O     . VAL A 1 2070 ? 236.993 239.085 195.560 1.00 11.32  ? 2070 VAL A O     1 
ATOM   4246  C  CB    . VAL A 1 2070 ? 235.129 239.383 192.761 1.00 10.90  ? 2070 VAL A CB    1 
ATOM   4247  C  CG1   . VAL A 1 2070 ? 234.921 237.969 193.275 1.00 9.97   ? 2070 VAL A CG1   1 
ATOM   4248  C  CG2   . VAL A 1 2070 ? 233.811 240.008 192.347 1.00 9.12   ? 2070 VAL A CG2   1 
ATOM   4249  N  N     . PRO A 1 2071 ? 238.191 239.553 193.717 1.00 10.50  ? 2071 PRO A N     1 
ATOM   4250  C  CA    . PRO A 1 2071 ? 239.419 239.089 194.379 1.00 10.13  ? 2071 PRO A CA    1 
ATOM   4251  C  C     . PRO A 1 2071 ? 239.789 239.918 195.591 1.00 13.81  ? 2071 PRO A C     1 
ATOM   4252  O  O     . PRO A 1 2071 ? 240.389 239.385 196.528 1.00 14.75  ? 2071 PRO A O     1 
ATOM   4253  C  CB    . PRO A 1 2071 ? 240.475 239.199 193.273 1.00 7.46   ? 2071 PRO A CB    1 
ATOM   4254  C  CG    . PRO A 1 2071 ? 239.710 239.028 192.034 1.00 8.87   ? 2071 PRO A CG    1 
ATOM   4255  C  CD    . PRO A 1 2071 ? 238.422 239.753 192.274 1.00 10.24  ? 2071 PRO A CD    1 
ATOM   4256  N  N     . PHE A 1 2072 ? 239.454 241.211 195.602 1.00 13.42  ? 2072 PHE A N     1 
ATOM   4257  C  CA    . PHE A 1 2072 ? 239.709 242.020 196.788 1.00 10.46  ? 2072 PHE A CA    1 
ATOM   4258  C  C     . PHE A 1 2072 ? 238.940 241.491 197.990 1.00 12.48  ? 2072 PHE A C     1 
ATOM   4259  O  O     . PHE A 1 2072 ? 239.491 241.385 199.089 1.00 15.31  ? 2072 PHE A O     1 
ATOM   4260  C  CB    . PHE A 1 2072 ? 239.346 243.481 196.525 1.00 11.75  ? 2072 PHE A CB    1 
ATOM   4261  C  CG    . PHE A 1 2072 ? 239.275 244.317 197.770 1.00 12.83  ? 2072 PHE A CG    1 
ATOM   4262  C  CD1   . PHE A 1 2072 ? 240.432 244.724 198.412 1.00 11.53  ? 2072 PHE A CD1   1 
ATOM   4263  C  CD2   . PHE A 1 2072 ? 238.052 244.694 198.299 1.00 13.08  ? 2072 PHE A CD2   1 
ATOM   4264  C  CE1   . PHE A 1 2072 ? 240.370 245.489 199.559 1.00 11.63  ? 2072 PHE A CE1   1 
ATOM   4265  C  CE2   . PHE A 1 2072 ? 237.985 245.459 199.445 1.00 9.78   ? 2072 PHE A CE2   1 
ATOM   4266  C  CZ    . PHE A 1 2072 ? 239.145 245.859 200.074 1.00 11.96  ? 2072 PHE A CZ    1 
ATOM   4267  N  N     . PHE A 1 2073 ? 237.664 241.148 197.801 1.00 11.95  ? 2073 PHE A N     1 
ATOM   4268  C  CA    . PHE A 1 2073 ? 236.884 240.591 198.902 1.00 11.28  ? 2073 PHE A CA    1 
ATOM   4269  C  C     . PHE A 1 2073 ? 237.414 239.225 199.321 1.00 12.25  ? 2073 PHE A C     1 
ATOM   4270  O  O     . PHE A 1 2073 ? 237.462 238.912 200.517 1.00 17.19  ? 2073 PHE A O     1 
ATOM   4271  C  CB    . PHE A 1 2073 ? 235.408 240.504 198.515 1.00 11.66  ? 2073 PHE A CB    1 
ATOM   4272  C  CG    . PHE A 1 2073 ? 234.607 241.708 198.917 1.00 11.53  ? 2073 PHE A CG    1 
ATOM   4273  C  CD1   . PHE A 1 2073 ? 234.643 242.866 198.161 1.00 10.24  ? 2073 PHE A CD1   1 
ATOM   4274  C  CD2   . PHE A 1 2073 ? 233.823 241.684 200.057 1.00 10.47  ? 2073 PHE A CD2   1 
ATOM   4275  C  CE1   . PHE A 1 2073 ? 233.909 243.974 198.530 1.00 9.95   ? 2073 PHE A CE1   1 
ATOM   4276  C  CE2   . PHE A 1 2073 ? 233.088 242.789 200.432 1.00 7.79   ? 2073 PHE A CE2   1 
ATOM   4277  C  CZ    . PHE A 1 2073 ? 233.131 243.936 199.667 1.00 9.38   ? 2073 PHE A CZ    1 
ATOM   4278  N  N     . LYS A 1 2074 ? 237.821 238.399 198.353 1.00 15.24  ? 2074 LYS A N     1 
ATOM   4279  C  CA    . LYS A 1 2074 ? 238.396 237.102 198.703 1.00 14.73  ? 2074 LYS A CA    1 
ATOM   4280  C  C     . LYS A 1 2074 ? 239.667 237.263 199.533 1.00 16.93  ? 2074 LYS A C     1 
ATOM   4281  O  O     . LYS A 1 2074 ? 239.853 236.576 200.548 1.00 18.68  ? 2074 LYS A O     1 
ATOM   4282  C  CB    . LYS A 1 2074 ? 238.682 236.294 197.437 1.00 12.69  ? 2074 LYS A CB    1 
ATOM   4283  C  CG    . LYS A 1 2074 ? 239.377 234.970 197.699 1.00 22.86  ? 2074 LYS A CG    1 
ATOM   4284  C  CD    . LYS A 1 2074 ? 238.824 233.869 196.815 1.00 36.77  ? 2074 LYS A CD    1 
ATOM   4285  C  CE    . LYS A 1 2074 ? 239.144 232.496 197.379 1.00 41.93  ? 2074 LYS A CE    1 
ATOM   4286  N  NZ    . LYS A 1 2074 ? 240.612 232.261 197.468 1.00 49.45  ? 2074 LYS A NZ    1 
ATOM   4287  N  N     . LEU A 1 2075 ? 240.546 238.182 199.131 1.00 14.20  ? 2075 LEU A N     1 
ATOM   4288  C  CA    . LEU A 1 2075 ? 241.793 238.377 199.857 1.00 14.92  ? 2075 LEU A CA    1 
ATOM   4289  C  C     . LEU A 1 2075 ? 241.566 239.084 201.185 1.00 15.91  ? 2075 LEU A C     1 
ATOM   4290  O  O     . LEU A 1 2075 ? 242.376 238.936 202.104 1.00 19.53  ? 2075 LEU A O     1 
ATOM   4291  C  CB    . LEU A 1 2075 ? 242.791 239.154 199.000 1.00 15.58  ? 2075 LEU A CB    1 
ATOM   4292  C  CG    . LEU A 1 2075 ? 243.208 238.484 197.689 1.00 17.82  ? 2075 LEU A CG    1 
ATOM   4293  C  CD1   . LEU A 1 2075 ? 243.821 239.497 196.739 1.00 12.40  ? 2075 LEU A CD1   1 
ATOM   4294  C  CD2   . LEU A 1 2075 ? 244.160 237.323 197.937 1.00 18.62  ? 2075 LEU A CD2   1 
ATOM   4295  N  N     . CYS A 1 2076 ? 240.490 239.862 201.308 1.00 17.63  ? 2076 CYS A N     1 
ATOM   4296  C  CA    . CYS A 1 2076 ? 240.130 240.408 202.612 1.00 15.55  ? 2076 CYS A CA    1 
ATOM   4297  C  C     . CYS A 1 2076 ? 239.651 239.308 203.547 1.00 13.29  ? 2076 CYS A C     1 
ATOM   4298  O  O     . CYS A 1 2076 ? 239.968 239.316 204.742 1.00 12.24  ? 2076 CYS A O     1 
ATOM   4299  C  CB    . CYS A 1 2076 ? 239.058 241.484 202.459 1.00 11.62  ? 2076 CYS A CB    1 
ATOM   4300  S  SG    . CYS A 1 2076 ? 239.699 243.115 202.053 1.00 17.08  ? 2076 CYS A SG    1 
ATOM   4301  N  N     . ASP A 1 2077 ? 238.880 238.354 203.022 1.00 17.05  ? 2077 ASP A N     1 
ATOM   4302  C  CA    . ASP A 1 2077 ? 238.467 237.217 203.836 1.00 18.87  ? 2077 ASP A CA    1 
ATOM   4303  C  C     . ASP A 1 2077 ? 239.671 236.386 204.265 1.00 18.67  ? 2077 ASP A C     1 
ATOM   4304  O  O     . ASP A 1 2077 ? 239.726 235.895 205.398 1.00 21.62  ? 2077 ASP A O     1 
ATOM   4305  C  CB    . ASP A 1 2077 ? 237.463 236.357 203.067 1.00 17.88  ? 2077 ASP A CB    1 
ATOM   4306  C  CG    . ASP A 1 2077 ? 236.579 235.532 203.981 1.00 30.30  ? 2077 ASP A CG    1 
ATOM   4307  O  OD1   . ASP A 1 2077 ? 236.996 235.245 205.122 1.00 30.15  ? 2077 ASP A OD1   1 
ATOM   4308  O  OD2   . ASP A 1 2077 ? 235.462 235.169 203.557 1.00 33.55  ? 2077 ASP A OD2   1 
ATOM   4309  N  N     . GLU A 1 2078 ? 240.649 236.221 203.372 1.00 20.72  ? 2078 GLU A N     1 
ATOM   4310  C  CA    . GLU A 1 2078 ? 241.811 235.397 203.698 1.00 18.17  ? 2078 GLU A CA    1 
ATOM   4311  C  C     . GLU A 1 2078 ? 242.762 236.109 204.658 1.00 17.57  ? 2078 GLU A C     1 
ATOM   4312  O  O     . GLU A 1 2078 ? 243.120 235.566 205.709 1.00 24.21  ? 2078 GLU A O     1 
ATOM   4313  C  CB    . GLU A 1 2078 ? 242.544 234.996 202.417 1.00 19.64  ? 2078 GLU A CB    1 
ATOM   4314  C  CG    . GLU A 1 2078 ? 242.076 233.682 201.824 1.00 29.21  ? 2078 GLU A CG    1 
ATOM   4315  C  CD    . GLU A 1 2078 ? 242.085 233.689 200.310 1.00 44.92  ? 2078 GLU A CD    1 
ATOM   4316  O  OE1   . GLU A 1 2078 ? 242.711 234.595 199.722 1.00 41.55  ? 2078 GLU A OE1   1 
ATOM   4317  O  OE2   . GLU A 1 2078 ? 241.466 232.787 199.709 1.00 53.55  ? 2078 GLU A OE2   1 
ATOM   4318  N  N     . GLN A 1 2079 ? 243.186 237.326 204.310 1.00 17.87  ? 2079 GLN A N     1 
ATOM   4319  C  CA    . GLN A 1 2079 ? 244.283 237.978 205.021 1.00 15.91  ? 2079 GLN A CA    1 
ATOM   4320  C  C     . GLN A 1 2079 ? 243.857 238.505 206.386 1.00 16.83  ? 2079 GLN A C     1 
ATOM   4321  O  O     . GLN A 1 2079 ? 244.605 238.382 207.362 1.00 21.26  ? 2079 GLN A O     1 
ATOM   4322  C  CB    . GLN A 1 2079 ? 244.851 239.112 204.167 1.00 20.04  ? 2079 GLN A CB    1 
ATOM   4323  C  CG    . GLN A 1 2079 ? 246.052 239.817 204.776 1.00 22.19  ? 2079 GLN A CG    1 
ATOM   4324  C  CD    . GLN A 1 2079 ? 247.270 238.923 204.875 1.00 31.55  ? 2079 GLN A CD    1 
ATOM   4325  O  OE1   . GLN A 1 2079 ? 247.567 238.156 203.962 1.00 28.85  ? 2079 GLN A OE1   1 
ATOM   4326  N  NE2   . GLN A 1 2079 ? 247.983 239.016 205.992 1.00 31.44  ? 2079 GLN A NE2   1 
ATOM   4327  N  N     . LEU A 1 2080 ? 242.673 239.105 206.476 1.00 17.49  ? 2080 LEU A N     1 
ATOM   4328  C  CA    . LEU A 1 2080 ? 242.273 239.776 207.706 1.00 15.33  ? 2080 LEU A CA    1 
ATOM   4329  C  C     . LEU A 1 2080 ? 242.069 238.776 208.839 1.00 21.63  ? 2080 LEU A C     1 
ATOM   4330  O  O     . LEU A 1 2080 ? 241.782 237.598 208.619 1.00 22.81  ? 2080 LEU A O     1 
ATOM   4331  C  CB    . LEU A 1 2080 ? 240.993 240.583 207.486 1.00 12.43  ? 2080 LEU A CB    1 
ATOM   4332  C  CG    . LEU A 1 2080 ? 241.084 241.777 206.533 1.00 18.35  ? 2080 LEU A CG    1 
ATOM   4333  C  CD1   . LEU A 1 2080 ? 239.937 242.741 206.770 1.00 11.13  ? 2080 LEU A CD1   1 
ATOM   4334  C  CD2   . LEU A 1 2080 ? 242.411 242.489 206.691 1.00 17.29  ? 2080 LEU A CD2   1 
ATOM   4335  N  N     . SER A 1 2081 ? 242.232 239.265 210.066 1.00 15.31  ? 2081 SER A N     1 
ATOM   4336  C  CA    . SER A 1 2081 ? 242.071 238.428 211.242 1.00 14.26  ? 2081 SER A CA    1 
ATOM   4337  C  C     . SER A 1 2081 ? 240.616 238.000 211.400 1.00 17.22  ? 2081 SER A C     1 
ATOM   4338  O  O     . SER A 1 2081 ? 239.688 238.647 210.906 1.00 19.93  ? 2081 SER A O     1 
ATOM   4339  C  CB    . SER A 1 2081 ? 242.534 239.166 212.497 1.00 16.90  ? 2081 SER A CB    1 
ATOM   4340  O  OG    . SER A 1 2081 ? 241.751 240.326 212.722 1.00 17.35  ? 2081 SER A OG    1 
ATOM   4341  N  N     . SER A 1 2082 ? 240.423 236.889 212.104 1.00 13.70  ? 2082 SER A N     1 
ATOM   4342  C  CA    . SER A 1 2082 ? 239.093 236.327 212.303 1.00 10.78  ? 2082 SER A CA    1 
ATOM   4343  C  C     . SER A 1 2082 ? 238.396 237.080 213.429 1.00 13.88  ? 2082 SER A C     1 
ATOM   4344  O  O     . SER A 1 2082 ? 238.817 237.010 214.588 1.00 21.41  ? 2082 SER A O     1 
ATOM   4345  C  CB    . SER A 1 2082 ? 239.187 234.836 212.611 1.00 20.55  ? 2082 SER A CB    1 
ATOM   4346  O  OG    . SER A 1 2082 ? 239.460 234.092 211.436 1.00 32.51  ? 2082 SER A OG    1 
ATOM   4347  N  N     . GLN A 1 2083 ? 237.335 237.805 213.089 1.00 12.26  ? 2083 GLN A N     1 
ATOM   4348  C  CA    . GLN A 1 2083 ? 236.515 238.506 214.064 1.00 9.36   ? 2083 GLN A CA    1 
ATOM   4349  C  C     . GLN A 1 2083 ? 235.060 238.096 213.895 1.00 11.45  ? 2083 GLN A C     1 
ATOM   4350  O  O     . GLN A 1 2083 ? 234.593 237.846 212.780 1.00 16.19  ? 2083 GLN A O     1 
ATOM   4351  C  CB    . GLN A 1 2083 ? 236.654 240.026 213.927 1.00 7.77   ? 2083 GLN A CB    1 
ATOM   4352  C  CG    . GLN A 1 2083 ? 238.091 240.510 213.849 1.00 9.59   ? 2083 GLN A CG    1 
ATOM   4353  C  CD    . GLN A 1 2083 ? 238.793 240.472 215.188 1.00 8.67   ? 2083 GLN A CD    1 
ATOM   4354  O  OE1   . GLN A 1 2083 ? 238.156 240.374 216.235 1.00 13.28  ? 2083 GLN A OE1   1 
ATOM   4355  N  NE2   . GLN A 1 2083 ? 240.117 240.547 215.164 1.00 13.12  ? 2083 GLN A NE2   1 
ATOM   4356  N  N     . SER A 1 2084 ? 234.347 238.024 215.021 1.00 10.50  ? 2084 SER A N     1 
ATOM   4357  C  CA    . SER A 1 2084 ? 232.967 237.558 215.004 1.00 8.90   ? 2084 SER A CA    1 
ATOM   4358  C  C     . SER A 1 2084 ? 232.038 238.503 214.256 1.00 11.39  ? 2084 SER A C     1 
ATOM   4359  O  O     . SER A 1 2084 ? 230.958 238.080 213.830 1.00 18.68  ? 2084 SER A O     1 
ATOM   4360  C  CB    . SER A 1 2084 ? 232.465 237.359 216.433 1.00 9.92   ? 2084 SER A CB    1 
ATOM   4361  O  OG    . SER A 1 2084 ? 232.409 238.591 217.129 1.00 19.09  ? 2084 SER A OG    1 
ATOM   4362  N  N     . HIS A 1 2085 ? 232.426 239.766 214.086 1.00 9.09   ? 2085 HIS A N     1 
ATOM   4363  C  CA    . HIS A 1 2085 ? 231.614 240.745 213.380 1.00 7.30   ? 2085 HIS A CA    1 
ATOM   4364  C  C     . HIS A 1 2085 ? 232.086 240.980 211.952 1.00 9.19   ? 2085 HIS A C     1 
ATOM   4365  O  O     . HIS A 1 2085 ? 231.645 241.940 211.314 1.00 14.48  ? 2085 HIS A O     1 
ATOM   4366  C  CB    . HIS A 1 2085 ? 231.592 242.068 214.151 1.00 6.88   ? 2085 HIS A CB    1 
ATOM   4367  C  CG    . HIS A 1 2085 ? 232.927 242.738 214.250 1.00 7.18   ? 2085 HIS A CG    1 
ATOM   4368  N  ND1   . HIS A 1 2085 ? 233.938 242.265 215.056 1.00 7.75   ? 2085 HIS A ND1   1 
ATOM   4369  C  CD2   . HIS A 1 2085 ? 233.412 243.851 213.651 1.00 7.03   ? 2085 HIS A CD2   1 
ATOM   4370  C  CE1   . HIS A 1 2085 ? 234.991 243.055 214.946 1.00 7.67   ? 2085 HIS A CE1   1 
ATOM   4371  N  NE2   . HIS A 1 2085 ? 234.698 244.024 214.099 1.00 6.59   ? 2085 HIS A NE2   1 
ATOM   4372  N  N     . TYR A 1 2086 ? 232.968 240.131 211.437 1.00 8.96   ? 2086 TYR A N     1 
ATOM   4373  C  CA    . TYR A 1 2086 ? 233.477 240.274 210.083 1.00 8.69   ? 2086 TYR A CA    1 
ATOM   4374  C  C     . TYR A 1 2086 ? 232.620 239.485 209.104 1.00 11.43  ? 2086 TYR A C     1 
ATOM   4375  O  O     . TYR A 1 2086 ? 232.274 238.328 209.353 1.00 15.56  ? 2086 TYR A O     1 
ATOM   4376  C  CB    . TYR A 1 2086 ? 234.927 239.797 209.995 1.00 9.16   ? 2086 TYR A CB    1 
ATOM   4377  C  CG    . TYR A 1 2086 ? 235.941 240.846 210.374 1.00 8.94   ? 2086 TYR A CG    1 
ATOM   4378  C  CD1   . TYR A 1 2086 ? 235.547 242.045 210.951 1.00 8.62   ? 2086 TYR A CD1   1 
ATOM   4379  C  CD2   . TYR A 1 2086 ? 237.293 240.639 210.155 1.00 8.94   ? 2086 TYR A CD2   1 
ATOM   4380  C  CE1   . TYR A 1 2086 ? 236.472 243.005 211.300 1.00 8.58   ? 2086 TYR A CE1   1 
ATOM   4381  C  CE2   . TYR A 1 2086 ? 238.224 241.592 210.499 1.00 10.06  ? 2086 TYR A CE2   1 
ATOM   4382  C  CZ    . TYR A 1 2086 ? 237.809 242.773 211.072 1.00 9.45   ? 2086 TYR A CZ    1 
ATOM   4383  O  OH    . TYR A 1 2086 ? 238.736 243.726 211.417 1.00 12.19  ? 2086 TYR A OH    1 
ATOM   4384  N  N     . ASP A 1 2087 ? 232.284 240.122 207.986 1.00 12.10  ? 2087 ASP A N     1 
ATOM   4385  C  CA    . ASP A 1 2087 ? 231.537 239.463 206.921 1.00 13.47  ? 2087 ASP A CA    1 
ATOM   4386  C  C     . ASP A 1 2087 ? 231.995 240.029 205.590 1.00 12.24  ? 2087 ASP A C     1 
ATOM   4387  O  O     . ASP A 1 2087 ? 231.783 241.214 205.313 1.00 15.41  ? 2087 ASP A O     1 
ATOM   4388  C  CB    . ASP A 1 2087 ? 230.031 239.656 207.096 1.00 12.15  ? 2087 ASP A CB    1 
ATOM   4389  C  CG    . ASP A 1 2087 ? 229.241 239.141 205.911 1.00 17.60  ? 2087 ASP A CG    1 
ATOM   4390  O  OD1   . ASP A 1 2087 ? 229.212 237.909 205.708 1.00 21.44  ? 2087 ASP A OD1   1 
ATOM   4391  O  OD2   . ASP A 1 2087 ? 228.653 239.966 205.181 1.00 14.83  ? 2087 ASP A OD2   1 
ATOM   4392  N  N     . PHE A 1 2088 ? 232.621 239.189 204.775 1.00 12.98  ? 2088 PHE A N     1 
ATOM   4393  C  CA    . PHE A 1 2088 ? 233.067 239.560 203.438 1.00 11.72  ? 2088 PHE A CA    1 
ATOM   4394  C  C     . PHE A 1 2088 ? 232.428 238.652 202.397 1.00 10.04  ? 2088 PHE A C     1 
ATOM   4395  O  O     . PHE A 1 2088 ? 233.078 238.198 201.455 1.00 13.99  ? 2088 PHE A O     1 
ATOM   4396  C  CB    . PHE A 1 2088 ? 234.588 239.519 203.343 1.00 14.85  ? 2088 PHE A CB    1 
ATOM   4397  C  CG    . PHE A 1 2088 ? 235.276 240.377 204.363 1.00 14.49  ? 2088 PHE A CG    1 
ATOM   4398  C  CD1   . PHE A 1 2088 ? 235.409 241.738 204.161 1.00 13.31  ? 2088 PHE A CD1   1 
ATOM   4399  C  CD2   . PHE A 1 2088 ? 235.779 239.824 205.527 1.00 12.01  ? 2088 PHE A CD2   1 
ATOM   4400  C  CE1   . PHE A 1 2088 ? 236.034 242.531 205.098 1.00 13.26  ? 2088 PHE A CE1   1 
ATOM   4401  C  CE2   . PHE A 1 2088 ? 236.406 240.613 206.469 1.00 10.96  ? 2088 PHE A CE2   1 
ATOM   4402  C  CZ    . PHE A 1 2088 ? 236.532 241.968 206.254 1.00 9.76   ? 2088 PHE A CZ    1 
ATOM   4403  N  N     . GLY A 1 2089 ? 231.120 238.428 202.550 1.00 10.99  ? 2089 GLY A N     1 
ATOM   4404  C  CA    . GLY A 1 2089 ? 230.389 237.558 201.610 1.00 8.03   ? 2089 GLY A CA    1 
ATOM   4405  C  C     . GLY A 1 2089 ? 229.691 238.354 200.525 1.00 8.25   ? 2089 GLY A C     1 
ATOM   4406  O  O     . GLY A 1 2089 ? 230.150 239.475 200.230 1.00 12.23  ? 2089 GLY A O     1 
ATOM   4407  N  N     . LEU A 1 2090 ? 228.648 237.786 199.917 1.00 6.03   ? 2090 LEU A N     1 
ATOM   4408  C  CA    . LEU A 1 2090 ? 227.966 238.476 198.793 1.00 5.63   ? 2090 LEU A CA    1 
ATOM   4409  C  C     . LEU A 1 2090 ? 227.288 239.742 199.335 1.00 5.98   ? 2090 LEU A C     1 
ATOM   4410  O  O     . LEU A 1 2090 ? 227.482 240.818 198.737 1.00 6.56   ? 2090 LEU A O     1 
ATOM   4411  C  CB    . LEU A 1 2090 ? 226.967 237.537 198.120 1.00 6.11   ? 2090 LEU A CB    1 
ATOM   4412  C  CG    . LEU A 1 2090 ? 226.318 238.056 196.835 1.00 5.15   ? 2090 LEU A CG    1 
ATOM   4413  C  CD1   . LEU A 1 2090 ? 227.384 238.528 195.863 1.00 8.63   ? 2090 LEU A CD1   1 
ATOM   4414  C  CD2   . LEU A 1 2090 ? 225.486 236.950 196.214 1.00 5.37   ? 2090 LEU A CD2   1 
ATOM   4415  N  N     . ARG A 1 2091 ? 226.536 239.614 200.430 1.00 6.54   ? 2091 ARG A N     1 
ATOM   4416  C  CA    . ARG A 1 2091 ? 225.810 240.780 200.995 1.00 4.84   ? 2091 ARG A CA    1 
ATOM   4417  C  C     . ARG A 1 2091 ? 226.774 241.972 201.091 1.00 6.74   ? 2091 ARG A C     1 
ATOM   4418  O  O     . ARG A 1 2091 ? 226.382 243.084 200.682 1.00 9.26   ? 2091 ARG A O     1 
ATOM   4419  C  CB    . ARG A 1 2091 ? 225.197 240.422 202.353 1.00 5.28   ? 2091 ARG A CB    1 
ATOM   4420  C  CG    . ARG A 1 2091 ? 224.032 239.451 202.229 1.00 7.55   ? 2091 ARG A CG    1 
ATOM   4421  C  CD    . ARG A 1 2091 ? 223.322 239.213 203.552 1.00 6.50   ? 2091 ARG A CD    1 
ATOM   4422  N  NE    . ARG A 1 2091 ? 222.109 238.407 203.381 1.00 9.64   ? 2091 ARG A NE    1 
ATOM   4423  C  CZ    . ARG A 1 2091 ? 221.900 237.228 203.952 1.00 6.95   ? 2091 ARG A CZ    1 
ATOM   4424  N  NH1   . ARG A 1 2091 ? 222.788 236.734 204.795 1.00 7.76   ? 2091 ARG A NH1   1 
ATOM   4425  N  NH2   . ARG A 1 2091 ? 220.803 236.548 203.678 1.00 6.74   ? 2091 ARG A NH2   1 
ATOM   4426  N  N     . ALA A 1 2092 ? 227.986 241.743 201.602 1.00 7.48   ? 2092 ALA A N     1 
ATOM   4427  C  CA    . ALA A 1 2092 ? 228.983 242.828 201.734 1.00 5.11   ? 2092 ALA A CA    1 
ATOM   4428  C  C     . ALA A 1 2092 ? 229.272 243.430 200.358 1.00 7.46   ? 2092 ALA A C     1 
ATOM   4429  O  O     . ALA A 1 2092 ? 229.228 244.670 200.220 1.00 9.89   ? 2092 ALA A O     1 
ATOM   4430  C  CB    . ALA A 1 2092 ? 230.237 242.280 202.373 1.00 7.03   ? 2092 ALA A CB    1 
ATOM   4431  N  N     . LEU A 1 2093 ? 229.546 242.578 199.366 1.00 8.27   ? 2093 LEU A N     1 
ATOM   4432  C  CA    . LEU A 1 2093 ? 229.826 243.061 197.990 1.00 6.03   ? 2093 LEU A CA    1 
ATOM   4433  C  C     . LEU A 1 2093 ? 228.569 243.751 197.447 1.00 7.99   ? 2093 LEU A C     1 
ATOM   4434  O  O     . LEU A 1 2093 ? 228.703 244.827 196.827 1.00 13.25  ? 2093 LEU A O     1 
ATOM   4435  C  CB    . LEU A 1 2093 ? 230.245 241.899 197.092 1.00 6.63   ? 2093 LEU A CB    1 
ATOM   4436  C  CG    . LEU A 1 2093 ? 230.637 242.277 195.662 1.00 10.78  ? 2093 LEU A CG    1 
ATOM   4437  C  CD1   . LEU A 1 2093 ? 232.144 242.390 195.506 1.00 9.14   ? 2093 LEU A CD1   1 
ATOM   4438  C  CD2   . LEU A 1 2093 ? 230.051 241.319 194.642 1.00 11.21  ? 2093 LEU A CD2   1 
ATOM   4439  N  N     . LYS A 1 2094 ? 227.403 243.132 197.642 1.00 6.08   ? 2094 LYS A N     1 
ATOM   4440  C  CA    . LYS A 1 2094 ? 226.129 243.739 197.183 1.00 7.91   ? 2094 LYS A CA    1 
ATOM   4441  C  C     . LYS A 1 2094 ? 226.052 245.162 197.742 1.00 8.00   ? 2094 LYS A C     1 
ATOM   4442  O  O     . LYS A 1 2094 ? 225.872 246.107 196.947 1.00 13.01  ? 2094 LYS A O     1 
ATOM   4443  C  CB    . LYS A 1 2094 ? 224.938 242.917 197.682 1.00 8.09   ? 2094 LYS A CB    1 
ATOM   4444  C  CG    . LYS A 1 2094 ? 223.565 243.403 197.247 1.00 12.01  ? 2094 LYS A CG    1 
ATOM   4445  C  CD    . LYS A 1 2094 ? 223.199 242.995 195.825 1.00 10.02  ? 2094 LYS A CD    1 
ATOM   4446  C  CE    . LYS A 1 2094 ? 221.821 243.444 195.460 1.00 12.03  ? 2094 LYS A CE    1 
ATOM   4447  N  NZ    . LYS A 1 2094 ? 220.833 243.009 196.450 1.00 16.64  ? 2094 LYS A NZ    1 
ATOM   4448  N  N     . SER A 1 2095 ? 226.199 245.297 199.061 1.00 5.95   ? 2095 SER A N     1 
ATOM   4449  C  CA    . SER A 1 2095 ? 226.100 246.634 199.700 1.00 8.00   ? 2095 SER A CA    1 
ATOM   4450  C  C     . SER A 1 2095 ? 227.130 247.566 199.056 1.00 8.69   ? 2095 SER A C     1 
ATOM   4451  O  O     . SER A 1 2095 ? 226.796 248.744 198.811 1.00 10.71  ? 2095 SER A O     1 
ATOM   4452  C  CB    . SER A 1 2095 ? 226.298 246.542 201.187 1.00 8.32   ? 2095 SER A CB    1 
ATOM   4453  O  OG    . SER A 1 2095 ? 227.609 246.091 201.494 1.00 14.50  ? 2095 SER A OG    1 
ATOM   4454  N  N     . VAL A 1 2096 ? 228.328 247.045 198.786 1.00 8.50   ? 2096 VAL A N     1 
ATOM   4455  C  CA    . VAL A 1 2096 ? 229.382 247.858 198.183 1.00 7.25   ? 2096 VAL A CA    1 
ATOM   4456  C  C     . VAL A 1 2096 ? 228.974 248.313 196.788 1.00 7.81   ? 2096 VAL A C     1 
ATOM   4457  O  O     . VAL A 1 2096 ? 229.176 249.472 196.417 1.00 8.43   ? 2096 VAL A O     1 
ATOM   4458  C  CB    . VAL A 1 2096 ? 230.714 247.083 198.162 1.00 7.84   ? 2096 VAL A CB    1 
ATOM   4459  C  CG1   . VAL A 1 2096 ? 231.678 247.701 197.163 1.00 8.77   ? 2096 VAL A CG1   1 
ATOM   4460  C  CG2   . VAL A 1 2096 ? 231.335 247.058 199.545 1.00 10.48  ? 2096 VAL A CG2   1 
ATOM   4461  N  N     . LEU A 1 2097 ? 228.384 247.415 195.998 1.00 8.73   ? 2097 LEU A N     1 
ATOM   4462  C  CA    . LEU A 1 2097 ? 227.987 247.761 194.635 1.00 8.46   ? 2097 LEU A CA    1 
ATOM   4463  C  C     . LEU A 1 2097 ? 226.843 248.770 194.620 1.00 9.25   ? 2097 LEU A C     1 
ATOM   4464  O  O     . LEU A 1 2097 ? 226.849 249.714 193.818 1.00 13.25  ? 2097 LEU A O     1 
ATOM   4465  C  CB    . LEU A 1 2097 ? 227.599 246.499 193.867 1.00 9.77   ? 2097 LEU A CB    1 
ATOM   4466  C  CG    . LEU A 1 2097 ? 228.688 245.440 193.672 1.00 7.20   ? 2097 LEU A CG    1 
ATOM   4467  C  CD1   . LEU A 1 2097 ? 228.073 244.141 193.186 1.00 8.40   ? 2097 LEU A CD1   1 
ATOM   4468  C  CD2   . LEU A 1 2097 ? 229.765 245.919 192.713 1.00 6.22   ? 2097 LEU A CD2   1 
ATOM   4469  N  N     . VAL A 1 2098 ? 225.845 248.585 195.489 1.00 9.65   ? 2098 VAL A N     1 
ATOM   4470  C  CA    . VAL A 1 2098 ? 224.748 249.548 195.560 1.00 11.88  ? 2098 VAL A CA    1 
ATOM   4471  C  C     . VAL A 1 2098 ? 225.269 250.913 195.996 1.00 12.57  ? 2098 VAL A C     1 
ATOM   4472  O  O     . VAL A 1 2098 ? 224.881 251.952 195.441 1.00 16.18  ? 2098 VAL A O     1 
ATOM   4473  C  CB    . VAL A 1 2098 ? 223.639 249.034 196.497 1.00 11.46  ? 2098 VAL A CB    1 
ATOM   4474  C  CG1   . VAL A 1 2098 ? 222.550 250.082 196.656 1.00 16.66  ? 2098 VAL A CG1   1 
ATOM   4475  C  CG2   . VAL A 1 2098 ? 223.048 247.744 195.958 1.00 7.69   ? 2098 VAL A CG2   1 
ATOM   4476  N  N     . SER A 1 2099 ? 226.162 250.931 196.988 1.00 12.24  ? 2099 SER A N     1 
ATOM   4477  C  CA    . SER A 1 2099 ? 226.757 252.186 197.425 1.00 14.39  ? 2099 SER A CA    1 
ATOM   4478  C  C     . SER A 1 2099 ? 227.588 252.817 196.318 1.00 14.17  ? 2099 SER A C     1 
ATOM   4479  O  O     . SER A 1 2099 ? 227.621 254.042 196.187 1.00 19.65  ? 2099 SER A O     1 
ATOM   4480  C  CB    . SER A 1 2099 ? 227.608 251.953 198.674 1.00 11.66  ? 2099 SER A CB    1 
ATOM   4481  O  OG    . SER A 1 2099 ? 228.432 253.071 198.948 1.00 24.09  ? 2099 SER A OG    1 
ATOM   4482  N  N     . ALA A 1 2100 ? 228.269 252.001 195.512 1.00 12.76  ? 2100 ALA A N     1 
ATOM   4483  C  CA    . ALA A 1 2100 ? 229.052 252.534 194.403 1.00 12.16  ? 2100 ALA A CA    1 
ATOM   4484  C  C     . ALA A 1 2100 ? 228.154 253.188 193.362 1.00 14.39  ? 2100 ALA A C     1 
ATOM   4485  O  O     . ALA A 1 2100 ? 228.478 254.259 192.839 1.00 22.29  ? 2100 ALA A O     1 
ATOM   4486  C  CB    . ALA A 1 2100 ? 229.891 251.427 193.769 1.00 12.44  ? 2100 ALA A CB    1 
ATOM   4487  N  N     . GLY A 1 2101 ? 227.025 252.554 193.046 1.00 12.17  ? 2101 GLY A N     1 
ATOM   4488  C  CA    . GLY A 1 2101 ? 226.076 253.178 192.135 1.00 13.92  ? 2101 GLY A CA    1 
ATOM   4489  C  C     . GLY A 1 2101 ? 225.527 254.487 192.674 1.00 19.94  ? 2101 GLY A C     1 
ATOM   4490  O  O     . GLY A 1 2101 ? 225.435 255.485 191.948 1.00 18.65  ? 2101 GLY A O     1 
ATOM   4491  N  N     . ASN A 1 2102 ? 225.166 254.505 193.961 1.00 18.35  ? 2102 ASN A N     1 
ATOM   4492  C  CA    . ASN A 1 2102 ? 224.670 255.734 194.573 1.00 18.10  ? 2102 ASN A CA    1 
ATOM   4493  C  C     . ASN A 1 2102 ? 225.735 256.826 194.569 1.00 23.65  ? 2102 ASN A C     1 
ATOM   4494  O  O     . ASN A 1 2102 ? 225.436 257.995 194.299 1.00 28.37  ? 2102 ASN A O     1 
ATOM   4495  C  CB    . ASN A 1 2102 ? 224.195 255.455 195.998 1.00 21.72  ? 2102 ASN A CB    1 
ATOM   4496  C  CG    . ASN A 1 2102 ? 222.916 254.642 196.037 1.00 25.68  ? 2102 ASN A CG    1 
ATOM   4497  O  OD1   . ASN A 1 2102 ? 222.273 254.426 195.012 1.00 29.70  ? 2102 ASN A OD1   1 
ATOM   4498  N  ND2   . ASN A 1 2102 ? 222.547 254.183 197.226 1.00 22.54  ? 2102 ASN A ND2   1 
ATOM   4499  N  N     . VAL A 1 2103 ? 226.982 256.460 194.869 1.00 23.95  ? 2103 VAL A N     1 
ATOM   4500  C  CA    . VAL A 1 2103 ? 228.076 257.424 194.878 1.00 22.38  ? 2103 VAL A CA    1 
ATOM   4501  C  C     . VAL A 1 2103 ? 228.325 257.962 193.477 1.00 22.72  ? 2103 VAL A C     1 
ATOM   4502  O  O     . VAL A 1 2103 ? 228.613 259.150 193.300 1.00 30.54  ? 2103 VAL A O     1 
ATOM   4503  C  CB    . VAL A 1 2103 ? 229.342 256.781 195.477 1.00 16.42  ? 2103 VAL A CB    1 
ATOM   4504  C  CG1   . VAL A 1 2103 ? 230.578 257.594 195.129 1.00 15.83  ? 2103 VAL A CG1   1 
ATOM   4505  C  CG2   . VAL A 1 2103 ? 229.203 256.648 196.983 1.00 22.51  ? 2103 VAL A CG2   1 
ATOM   4506  N  N     . LYS A 1 2104 ? 228.227 257.103 192.462 1.00 18.66  ? 2104 LYS A N     1 
ATOM   4507  C  CA    . LYS A 1 2104 ? 228.385 257.569 191.089 1.00 21.70  ? 2104 LYS A CA    1 
ATOM   4508  C  C     . LYS A 1 2104 ? 227.292 258.562 190.722 1.00 25.22  ? 2104 LYS A C     1 
ATOM   4509  O  O     . LYS A 1 2104 ? 227.566 259.595 190.098 1.00 24.55  ? 2104 LYS A O     1 
ATOM   4510  C  CB    . LYS A 1 2104 ? 228.386 256.385 190.123 1.00 18.14  ? 2104 LYS A CB    1 
ATOM   4511  C  CG    . LYS A 1 2104 ? 228.896 256.736 188.737 1.00 18.40  ? 2104 LYS A CG    1 
ATOM   4512  C  CD    . LYS A 1 2104 ? 228.844 255.549 187.792 1.00 13.26  ? 2104 LYS A CD    1 
ATOM   4513  C  CE    . LYS A 1 2104 ? 227.433 255.280 187.311 1.00 17.52  ? 2104 LYS A CE    1 
ATOM   4514  N  NZ    . LYS A 1 2104 ? 226.903 256.406 186.496 1.00 31.35  ? 2104 LYS A NZ    1 
ATOM   4515  N  N     . ARG A 1 2105 ? 226.046 258.273 191.110 1.00 27.86  ? 2105 ARG A N     1 
ATOM   4516  C  CA    . ARG A 1 2105 ? 224.964 259.217 190.836 1.00 23.74  ? 2105 ARG A CA    1 
ATOM   4517  C  C     . ARG A 1 2105 ? 225.198 260.546 191.548 1.00 27.77  ? 2105 ARG A C     1 
ATOM   4518  O  O     . ARG A 1 2105 ? 224.996 261.618 190.963 1.00 35.53  ? 2105 ARG A O     1 
ATOM   4519  C  CB    . ARG A 1 2105 ? 223.618 258.624 191.251 1.00 24.17  ? 2105 ARG A CB    1 
ATOM   4520  C  CG    . ARG A 1 2105 ? 223.171 257.445 190.413 1.00 29.45  ? 2105 ARG A CG    1 
ATOM   4521  C  CD    . ARG A 1 2105 ? 221.830 256.919 190.890 1.00 31.31  ? 2105 ARG A CD    1 
ATOM   4522  N  NE    . ARG A 1 2105 ? 221.366 255.796 190.085 1.00 33.76  ? 2105 ARG A NE    1 
ATOM   4523  C  CZ    . ARG A 1 2105 ? 221.631 254.526 190.354 1.00 37.21  ? 2105 ARG A CZ    1 
ATOM   4524  N  NH1   . ARG A 1 2105 ? 222.340 254.179 191.415 1.00 29.22  ? 2105 ARG A NH1   1 
ATOM   4525  N  NH2   . ARG A 1 2105 ? 221.169 253.579 189.542 1.00 45.73  ? 2105 ARG A NH2   1 
ATOM   4526  N  N     . GLU A 1 2106 ? 225.629 260.493 192.810 1.00 29.50  ? 2106 GLU A N     1 
ATOM   4527  C  CA    . GLU A 1 2106 ? 225.874 261.719 193.564 1.00 31.91  ? 2106 GLU A CA    1 
ATOM   4528  C  C     . GLU A 1 2106 ? 227.024 262.522 192.967 1.00 34.60  ? 2106 GLU A C     1 
ATOM   4529  O  O     . GLU A 1 2106 ? 226.959 263.755 192.907 1.00 41.17  ? 2106 GLU A O     1 
ATOM   4530  C  CB    . GLU A 1 2106 ? 226.153 261.386 195.029 1.00 33.57  ? 2106 GLU A CB    1 
ATOM   4531  C  CG    . GLU A 1 2106 ? 224.954 260.818 195.771 1.00 48.76  ? 2106 GLU A CG    1 
ATOM   4532  C  CD    . GLU A 1 2106 ? 225.268 260.479 197.214 1.00 62.70  ? 2106 GLU A CD    1 
ATOM   4533  O  OE1   . GLU A 1 2106 ? 226.450 260.570 197.604 1.00 62.71  ? 2106 GLU A OE1   1 
ATOM   4534  O  OE2   . GLU A 1 2106 ? 224.331 260.123 197.961 1.00 64.15  ? 2106 GLU A OE2   1 
ATOM   4535  N  N     . ARG A 1 2107 ? 228.086 261.847 192.524 1.00 33.96  ? 2107 ARG A N     1 
ATOM   4536  C  CA    . ARG A 1 2107 ? 229.202 262.545 191.895 1.00 33.13  ? 2107 ARG A CA    1 
ATOM   4537  C  C     . ARG A 1 2107 ? 228.785 263.170 190.571 1.00 37.88  ? 2107 ARG A C     1 
ATOM   4538  O  O     . ARG A 1 2107 ? 229.215 264.282 190.241 1.00 46.71  ? 2107 ARG A O     1 
ATOM   4539  C  CB    . ARG A 1 2107 ? 230.374 261.586 191.691 1.00 32.55  ? 2107 ARG A CB    1 
ATOM   4540  C  CG    . ARG A 1 2107 ? 231.671 262.277 191.313 1.00 41.55  ? 2107 ARG A CG    1 
ATOM   4541  C  CD    . ARG A 1 2107 ? 232.871 261.379 191.553 1.00 33.97  ? 2107 ARG A CD    1 
ATOM   4542  N  NE    . ARG A 1 2107 ? 232.929 260.891 192.925 1.00 30.41  ? 2107 ARG A NE    1 
ATOM   4543  C  CZ    . ARG A 1 2107 ? 233.997 260.327 193.472 1.00 30.06  ? 2107 ARG A CZ    1 
ATOM   4544  N  NH1   . ARG A 1 2107 ? 235.121 260.177 192.793 1.00 30.53  ? 2107 ARG A NH1   1 
ATOM   4545  N  NH2   . ARG A 1 2107 ? 233.935 259.905 194.731 1.00 28.80  ? 2107 ARG A NH2   1 
ATOM   4546  N  N     . ILE A 1 2108 ? 227.951 262.471 189.799 1.00 34.87  ? 2108 ILE A N     1 
ATOM   4547  C  CA    . ILE A 1 2108 ? 227.441 263.041 188.556 1.00 35.66  ? 2108 ILE A CA    1 
ATOM   4548  C  C     . ILE A 1 2108 ? 226.611 264.284 188.847 1.00 42.47  ? 2108 ILE A C     1 
ATOM   4549  O  O     . ILE A 1 2108 ? 226.735 265.305 188.161 1.00 53.51  ? 2108 ILE A O     1 
ATOM   4550  C  CB    . ILE A 1 2108 ? 226.639 261.986 187.772 1.00 32.73  ? 2108 ILE A CB    1 
ATOM   4551  C  CG1   . ILE A 1 2108 ? 227.583 260.956 187.151 1.00 28.01  ? 2108 ILE A CG1   1 
ATOM   4552  C  CG2   . ILE A 1 2108 ? 225.788 262.644 186.699 1.00 34.60  ? 2108 ILE A CG2   1 
ATOM   4553  C  CD1   . ILE A 1 2108 ? 226.873 259.798 186.495 1.00 25.13  ? 2108 ILE A CD1   1 
ATOM   4554  N  N     . GLN A 1 2109 ? 225.762 264.223 189.875 1.00 39.31  ? 2109 GLN A N     1 
ATOM   4555  C  CA    . GLN A 1 2109 ? 224.963 265.390 190.243 1.00 38.88  ? 2109 GLN A CA    1 
ATOM   4556  C  C     . GLN A 1 2109 ? 225.845 266.546 190.706 1.00 52.16  ? 2109 GLN A C     1 
ATOM   4557  O  O     . GLN A 1 2109 ? 225.562 267.713 190.409 1.00 62.84  ? 2109 GLN A O     1 
ATOM   4558  C  CB    . GLN A 1 2109 ? 223.958 265.014 191.332 1.00 38.91  ? 2109 GLN A CB    1 
ATOM   4559  C  CG    . GLN A 1 2109 ? 222.830 264.118 190.852 1.00 48.55  ? 2109 GLN A CG    1 
ATOM   4560  C  CD    . GLN A 1 2109 ? 221.880 264.826 189.908 1.00 56.70  ? 2109 GLN A CD    1 
ATOM   4561  O  OE1   . GLN A 1 2109 ? 222.128 264.907 188.705 1.00 60.84  ? 2109 GLN A OE1   1 
ATOM   4562  N  NE2   . GLN A 1 2109 ? 220.785 265.344 190.451 1.00 56.69  ? 2109 GLN A NE2   1 
ATOM   4563  N  N     . LYS A 1 2110 ? 226.908 266.241 191.455 1.00 53.76  ? 2110 LYS A N     1 
ATOM   4564  C  CA    . LYS A 1 2110 ? 227.816 267.287 191.912 1.00 53.87  ? 2110 LYS A CA    1 
ATOM   4565  C  C     . LYS A 1 2110 ? 228.523 267.954 190.741 1.00 56.50  ? 2110 LYS A C     1 
ATOM   4566  O  O     . LYS A 1 2110 ? 228.633 269.185 190.691 1.00 68.42  ? 2110 LYS A O     1 
ATOM   4567  C  CB    . LYS A 1 2110 ? 228.834 266.706 192.894 1.00 54.00  ? 2110 LYS A CB    1 
ATOM   4568  C  CG    . LYS A 1 2110 ? 229.894 267.697 193.343 1.00 60.02  ? 2110 LYS A CG    1 
ATOM   4569  C  CD    . LYS A 1 2110 ? 231.049 266.994 194.030 1.00 58.09  ? 2110 LYS A CD    1 
ATOM   4570  C  CE    . LYS A 1 2110 ? 231.777 266.069 193.068 1.00 59.36  ? 2110 LYS A CE    1 
ATOM   4571  N  NZ    . LYS A 1 2110 ? 232.378 266.813 191.927 1.00 62.18  ? 2110 LYS A NZ    1 
ATOM   4572  N  N     . ILE A 1 2111 ? 229.007 267.158 189.787 1.00 51.67  ? 2111 ILE A N     1 
ATOM   4573  C  CA    . ILE A 1 2111 ? 229.623 267.729 188.594 1.00 57.44  ? 2111 ILE A CA    1 
ATOM   4574  C  C     . ILE A 1 2111 ? 228.602 268.547 187.812 1.00 61.60  ? 2111 ILE A C     1 
ATOM   4575  O  O     . ILE A 1 2111 ? 228.931 269.596 187.247 1.00 63.87  ? 2111 ILE A O     1 
ATOM   4576  C  CB    . ILE A 1 2111 ? 230.258 266.621 187.731 1.00 55.51  ? 2111 ILE A CB    1 
ATOM   4577  C  CG1   . ILE A 1 2111 ? 231.386 265.931 188.499 1.00 49.57  ? 2111 ILE A CG1   1 
ATOM   4578  C  CG2   . ILE A 1 2111 ? 230.780 267.186 186.420 1.00 53.48  ? 2111 ILE A CG2   1 
ATOM   4579  C  CD1   . ILE A 1 2111 ? 231.895 264.671 187.838 1.00 48.39  ? 2111 ILE A CD1   1 
ATOM   4580  N  N     . LYS A 1 2112 ? 227.347 268.093 187.780 1.00 60.14  ? 2112 LYS A N     1 
ATOM   4581  C  CA    . LYS A 1 2112 ? 226.310 268.835 187.071 1.00 60.86  ? 2112 LYS A CA    1 
ATOM   4582  C  C     . LYS A 1 2112 ? 226.071 270.202 187.700 1.00 65.31  ? 2112 LYS A C     1 
ATOM   4583  O  O     . LYS A 1 2112 ? 226.000 271.213 186.991 1.00 72.64  ? 2112 LYS A O     1 
ATOM   4584  C  CB    . LYS A 1 2112 ? 225.012 268.026 187.043 1.00 59.00  ? 2112 LYS A CB    1 
ATOM   4585  C  CG    . LYS A 1 2112 ? 224.937 267.025 185.906 1.00 64.77  ? 2112 LYS A CG    1 
ATOM   4586  C  CD    . LYS A 1 2112 ? 223.498 266.694 185.554 1.00 68.27  ? 2112 LYS A CD    1 
ATOM   4587  C  CE    . LYS A 1 2112 ? 223.429 265.816 184.316 1.00 68.22  ? 2112 LYS A CE    1 
ATOM   4588  N  NZ    . LYS A 1 2112 ? 222.309 264.837 184.385 1.00 75.03  ? 2112 LYS A NZ    1 
ATOM   4589  N  N     . ARG A 1 2113 ? 225.951 270.261 189.028 1.00 65.42  ? 2113 ARG A N     1 
ATOM   4590  C  CA    . ARG A 1 2113 ? 225.714 271.557 189.662 1.00 67.78  ? 2113 ARG A CA    1 
ATOM   4591  C  C     . ARG A 1 2113 ? 226.947 272.449 189.569 1.00 69.65  ? 2113 ARG A C     1 
ATOM   4592  O  O     . ARG A 1 2113 ? 226.827 273.674 189.432 1.00 74.53  ? 2113 ARG A O     1 
ATOM   4593  C  CB    . ARG A 1 2113 ? 225.267 271.398 191.119 1.00 59.73  ? 2113 ARG A CB    1 
ATOM   4594  C  CG    . ARG A 1 2113 ? 226.275 270.801 192.087 1.00 63.42  ? 2113 ARG A CG    1 
ATOM   4595  C  CD    . ARG A 1 2113 ? 225.675 270.757 193.493 1.00 66.69  ? 2113 ARG A CD    1 
ATOM   4596  N  NE    . ARG A 1 2113 ? 224.515 269.879 193.595 1.00 74.21  ? 2113 ARG A NE    1 
ATOM   4597  C  CZ    . ARG A 1 2113 ? 224.574 268.584 193.869 1.00 68.14  ? 2113 ARG A CZ    1 
ATOM   4598  N  NH1   . ARG A 1 2113 ? 225.716 267.992 194.167 1.00 64.95  ? 2113 ARG A NH1   1 
ATOM   4599  N  NH2   . ARG A 1 2113 ? 223.452 267.870 193.869 1.00 61.57  ? 2113 ARG A NH2   1 
ATOM   4600  N  N     . GLU A 1 2114 ? 228.144 271.857 189.634 1.00 68.65  ? 2114 GLU A N     1 
ATOM   4601  C  CA    . GLU A 1 2114 ? 229.364 272.636 189.452 1.00 74.05  ? 2114 GLU A CA    1 
ATOM   4602  C  C     . GLU A 1 2114 ? 229.431 273.232 188.052 1.00 77.62  ? 2114 GLU A C     1 
ATOM   4603  O  O     . GLU A 1 2114 ? 229.839 274.386 187.878 1.00 78.01  ? 2114 GLU A O     1 
ATOM   4604  C  CB    . GLU A 1 2114 ? 230.585 271.758 189.734 1.00 75.66  ? 2114 GLU A CB    1 
ATOM   4605  C  CG    . GLU A 1 2114 ? 231.910 272.501 189.808 1.00 78.33  ? 2114 GLU A CG    1 
ATOM   4606  C  CD    . GLU A 1 2114 ? 232.528 272.739 188.445 1.00 87.16  ? 2114 GLU A CD    1 
ATOM   4607  O  OE1   . GLU A 1 2114 ? 232.283 271.927 187.529 1.00 84.56  ? 2114 GLU A OE1   1 
ATOM   4608  O  OE2   . GLU A 1 2114 ? 233.262 273.736 188.289 1.00 91.37  ? 2114 GLU A OE2   1 
ATOM   4609  N  N     . LYS A 1 2115 ? 229.044 272.455 187.039 1.00 78.78  ? 2115 LYS A N     1 
ATOM   4610  C  CA    . LYS A 1 2115 ? 228.993 272.974 185.677 1.00 79.23  ? 2115 LYS A CA    1 
ATOM   4611  C  C     . LYS A 1 2115 ? 227.939 274.064 185.545 1.00 78.24  ? 2115 LYS A C     1 
ATOM   4612  O  O     . LYS A 1 2115 ? 228.136 275.046 184.823 1.00 78.73  ? 2115 LYS A O     1 
ATOM   4613  C  CB    . LYS A 1 2115 ? 228.714 271.835 184.696 1.00 75.97  ? 2115 LYS A CB    1 
ATOM   4614  C  CG    . LYS A 1 2115 ? 229.939 271.022 184.313 1.00 74.85  ? 2115 LYS A CG    1 
ATOM   4615  C  CD    . LYS A 1 2115 ? 229.659 270.152 183.098 1.00 78.53  ? 2115 LYS A CD    1 
ATOM   4616  C  CE    . LYS A 1 2115 ? 230.922 269.881 182.302 1.00 77.86  ? 2115 LYS A CE    1 
ATOM   4617  N  NZ    . LYS A 1 2115 ? 231.033 268.447 181.920 1.00 77.65  ? 2115 LYS A NZ    1 
ATOM   4618  N  N     . GLU A 1 2116 ? 226.801 273.897 186.222 1.00 76.73  ? 2116 GLU A N     1 
ATOM   4619  C  CA    . GLU A 1 2116 ? 225.756 274.914 186.164 1.00 75.08  ? 2116 GLU A CA    1 
ATOM   4620  C  C     . GLU A 1 2116 ? 226.225 276.231 186.771 1.00 81.57  ? 2116 GLU A C     1 
ATOM   4621  O  O     . GLU A 1 2116 ? 225.970 277.303 186.211 1.00 81.28  ? 2116 GLU A O     1 
ATOM   4622  C  CB    . GLU A 1 2116 ? 224.497 274.416 186.871 1.00 72.53  ? 2116 GLU A CB    1 
ATOM   4623  C  CG    . GLU A 1 2116 ? 223.327 275.383 186.790 1.00 75.70  ? 2116 GLU A CG    1 
ATOM   4624  C  CD    . GLU A 1 2116 ? 222.076 274.845 187.454 1.00 79.42  ? 2116 GLU A CD    1 
ATOM   4625  O  OE1   . GLU A 1 2116 ? 222.127 273.722 187.998 1.00 79.07  ? 2116 GLU A OE1   1 
ATOM   4626  O  OE2   . GLU A 1 2116 ? 221.043 275.546 187.433 1.00 81.53  ? 2116 GLU A OE2   1 
ATOM   4627  N  N     . GLU A 1 2117 ? 226.912 276.175 187.914 1.00 84.64  ? 2117 GLU A N     1 
ATOM   4628  C  CA    . GLU A 1 2117 ? 227.383 277.400 188.550 1.00 83.78  ? 2117 GLU A CA    1 
ATOM   4629  C  C     . GLU A 1 2117 ? 228.608 277.996 187.866 1.00 85.15  ? 2117 GLU A C     1 
ATOM   4630  O  O     . GLU A 1 2117 ? 228.844 279.201 188.001 1.00 89.82  ? 2117 GLU A O     1 
ATOM   4631  C  CB    . GLU A 1 2117 ? 227.680 277.149 190.034 1.00 89.38  ? 2117 GLU A CB    1 
ATOM   4632  C  CG    . GLU A 1 2117 ? 228.767 276.121 190.323 1.00 91.00  ? 2117 GLU A CG    1 
ATOM   4633  C  CD    . GLU A 1 2117 ? 230.165 276.716 190.332 1.00 96.76  ? 2117 GLU A CD    1 
ATOM   4634  O  OE1   . GLU A 1 2117 ? 230.289 277.949 190.492 1.00 98.19  ? 2117 GLU A OE1   1 
ATOM   4635  O  OE2   . GLU A 1 2117 ? 231.140 275.949 190.186 1.00 92.13  ? 2117 GLU A OE2   1 
ATOM   4636  N  N     . ARG A 1 2118 ? 229.383 277.195 187.137 1.00 86.47  ? 2118 ARG A N     1 
ATOM   4637  C  CA    . ARG A 1 2118 ? 230.563 277.672 186.415 1.00 83.01  ? 2118 ARG A CA    1 
ATOM   4638  C  C     . ARG A 1 2118 ? 230.370 277.322 184.942 1.00 86.69  ? 2118 ARG A C     1 
ATOM   4639  O  O     . ARG A 1 2118 ? 230.585 276.177 184.534 1.00 88.30  ? 2118 ARG A O     1 
ATOM   4640  C  CB    . ARG A 1 2118 ? 231.844 277.058 186.977 1.00 84.83  ? 2118 ARG A CB    1 
ATOM   4641  C  CG    . ARG A 1 2118 ? 233.053 277.170 186.057 1.00 86.26  ? 2118 ARG A CG    1 
ATOM   4642  C  CD    . ARG A 1 2118 ? 234.149 276.199 186.460 1.00 86.52  ? 2118 ARG A CD    1 
ATOM   4643  N  NE    . ARG A 1 2118 ? 235.089 275.954 185.374 1.00 86.52  ? 2118 ARG A NE    1 
ATOM   4644  C  CZ    . ARG A 1 2118 ? 235.207 274.799 184.732 1.00 83.86  ? 2118 ARG A CZ    1 
ATOM   4645  N  NH1   . ARG A 1 2118 ? 234.452 273.757 185.040 1.00 79.34  ? 2118 ARG A NH1   1 
ATOM   4646  N  NH2   . ARG A 1 2118 ? 236.105 274.687 183.758 1.00 78.87  ? 2118 ARG A NH2   1 
ATOM   4647  N  N     . GLY A 1 2119 ? 229.964 278.305 184.148 1.00 80.99  ? 2119 GLY A N     1 
ATOM   4648  C  CA    . GLY A 1 2119 ? 229.686 278.070 182.749 1.00 82.39  ? 2119 GLY A CA    1 
ATOM   4649  C  C     . GLY A 1 2119 ? 228.295 277.504 182.525 1.00 83.22  ? 2119 GLY A C     1 
ATOM   4650  O  O     . GLY A 1 2119 ? 227.470 277.398 183.436 1.00 82.44  ? 2119 GLY A O     1 
ATOM   4651  N  N     . GLU A 1 2120 ? 228.038 277.136 181.267 1.00 86.97  ? 2120 GLU A N     1 
ATOM   4652  C  CA    . GLU A 1 2120 ? 226.735 276.597 180.895 1.00 96.40  ? 2120 GLU A CA    1 
ATOM   4653  C  C     . GLU A 1 2120 ? 226.834 275.366 179.999 1.00 94.58  ? 2120 GLU A C     1 
ATOM   4654  O  O     . GLU A 1 2120 ? 225.801 274.904 179.499 1.00 95.41  ? 2120 GLU A O     1 
ATOM   4655  C  CB    . GLU A 1 2120 ? 225.884 277.669 180.200 1.00 97.19  ? 2120 GLU A CB    1 
ATOM   4656  C  CG    . GLU A 1 2120 ? 225.495 278.837 181.094 1.00 94.86  ? 2120 GLU A CG    1 
ATOM   4657  C  CD    . GLU A 1 2120 ? 224.680 279.885 180.364 1.00 96.69  ? 2120 GLU A CD    1 
ATOM   4658  O  OE1   . GLU A 1 2120 ? 223.545 279.575 179.946 1.00 99.77  ? 2120 GLU A OE1   1 
ATOM   4659  O  OE2   . GLU A 1 2120 ? 225.176 281.021 180.206 1.00 92.87  ? 2120 GLU A OE2   1 
ATOM   4660  N  N     . ALA A 1 2121 ? 228.027 274.823 179.781 1.00 90.95  ? 2121 ALA A N     1 
ATOM   4661  C  CA    . ALA A 1 2121 ? 228.208 273.672 178.906 1.00 85.61  ? 2121 ALA A CA    1 
ATOM   4662  C  C     . ALA A 1 2121 ? 228.136 272.392 179.729 1.00 91.50  ? 2121 ALA A C     1 
ATOM   4663  O  O     . ALA A 1 2121 ? 228.993 272.149 180.586 1.00 93.08  ? 2121 ALA A O     1 
ATOM   4664  C  CB    . ALA A 1 2121 ? 229.540 273.760 178.164 1.00 71.86  ? 2121 ALA A CB    1 
ATOM   4665  N  N     . VAL A 1 2122 ? 227.119 271.575 179.466 1.00 93.74  ? 2122 VAL A N     1 
ATOM   4666  C  CA    . VAL A 1 2122 ? 226.925 270.301 180.145 1.00 87.03  ? 2122 VAL A CA    1 
ATOM   4667  C  C     . VAL A 1 2122 ? 226.813 269.211 179.090 1.00 89.28  ? 2122 VAL A C     1 
ATOM   4668  O  O     . VAL A 1 2122 ? 225.949 269.282 178.207 1.00 90.82  ? 2122 VAL A O     1 
ATOM   4669  C  CB    . VAL A 1 2122 ? 225.678 270.320 181.049 1.00 81.98  ? 2122 VAL A CB    1 
ATOM   4670  C  CG1   . VAL A 1 2122 ? 225.218 268.902 181.355 1.00 74.85  ? 2122 VAL A CG1   1 
ATOM   4671  C  CG2   . VAL A 1 2122 ? 225.964 271.083 182.329 1.00 83.96  ? 2122 VAL A CG2   1 
ATOM   4672  N  N     . ASP A 1 2123 ? 227.684 268.208 179.179 1.00 88.30  ? 2123 ASP A N     1 
ATOM   4673  C  CA    . ASP A 1 2123 ? 227.641 267.056 178.281 1.00 84.35  ? 2123 ASP A CA    1 
ATOM   4674  C  C     . ASP A 1 2123 ? 227.729 265.800 179.135 1.00 82.21  ? 2123 ASP A C     1 
ATOM   4675  O  O     . ASP A 1 2123 ? 228.792 265.490 179.680 1.00 82.46  ? 2123 ASP A O     1 
ATOM   4676  C  CB    . ASP A 1 2123 ? 228.769 267.103 177.252 1.00 84.83  ? 2123 ASP A CB    1 
ATOM   4677  C  CG    . ASP A 1 2123 ? 228.710 265.947 176.271 1.00 87.04  ? 2123 ASP A CG    1 
ATOM   4678  O  OD1   . ASP A 1 2123 ? 227.629 265.716 175.690 1.00 86.59  ? 2123 ASP A OD1   1 
ATOM   4679  O  OD2   . ASP A 1 2123 ? 229.743 265.274 176.076 1.00 84.74  ? 2123 ASP A OD2   1 
ATOM   4680  N  N     . GLU A 1 2124 ? 226.610 265.080 179.247 1.00 77.84  ? 2124 GLU A N     1 
ATOM   4681  C  CA    . GLU A 1 2124 ? 226.557 263.916 180.125 1.00 70.63  ? 2124 GLU A CA    1 
ATOM   4682  C  C     . GLU A 1 2124 ? 227.463 262.797 179.624 1.00 74.90  ? 2124 GLU A C     1 
ATOM   4683  O  O     . GLU A 1 2124 ? 228.021 262.037 180.423 1.00 76.52  ? 2124 GLU A O     1 
ATOM   4684  C  CB    . GLU A 1 2124 ? 225.112 263.433 180.252 1.00 66.84  ? 2124 GLU A CB    1 
ATOM   4685  C  CG    . GLU A 1 2124 ? 224.210 264.413 180.982 1.00 70.00  ? 2124 GLU A CG    1 
ATOM   4686  C  CD    . GLU A 1 2124 ? 222.776 263.940 181.058 1.00 67.32  ? 2124 GLU A CD    1 
ATOM   4687  O  OE1   . GLU A 1 2124 ? 222.460 262.913 180.427 1.00 55.60  ? 2124 GLU A OE1   1 
ATOM   4688  O  OE2   . GLU A 1 2124 ? 221.962 264.594 181.743 1.00 76.67  ? 2124 GLU A OE2   1 
ATOM   4689  N  N     . GLY A 1 2125 ? 227.615 262.676 178.304 1.00 81.18  ? 2125 GLY A N     1 
ATOM   4690  C  CA    . GLY A 1 2125 ? 228.558 261.706 177.769 1.00 77.20  ? 2125 GLY A CA    1 
ATOM   4691  C  C     . GLY A 1 2125 ? 229.986 262.003 178.183 1.00 75.76  ? 2125 GLY A C     1 
ATOM   4692  O  O     . GLY A 1 2125 ? 230.741 261.096 178.546 1.00 76.74  ? 2125 GLY A O     1 
ATOM   4693  N  N     . GLU A 1 2126 ? 230.376 263.280 178.140 1.00 75.66  ? 2126 GLU A N     1 
ATOM   4694  C  CA    . GLU A 1 2126 ? 231.691 263.671 178.632 1.00 78.18  ? 2126 GLU A CA    1 
ATOM   4695  C  C     . GLU A 1 2126 ? 231.825 263.385 180.122 1.00 78.70  ? 2126 GLU A C     1 
ATOM   4696  O  O     . GLU A 1 2126 ? 232.869 262.908 180.578 1.00 80.50  ? 2126 GLU A O     1 
ATOM   4697  C  CB    . GLU A 1 2126 ? 231.943 265.151 178.347 1.00 82.29  ? 2126 GLU A CB    1 
ATOM   4698  C  CG    . GLU A 1 2126 ? 233.125 265.744 179.095 1.00 85.72  ? 2126 GLU A CG    1 
ATOM   4699  C  CD    . GLU A 1 2126 ? 232.971 267.232 179.342 1.00 92.31  ? 2126 GLU A CD    1 
ATOM   4700  O  OE1   . GLU A 1 2126 ? 231.934 267.798 178.937 1.00 92.97  ? 2126 GLU A OE1   1 
ATOM   4701  O  OE2   . GLU A 1 2126 ? 233.885 267.836 179.941 1.00 92.18  ? 2126 GLU A OE2   1 
ATOM   4702  N  N     . ILE A 1 2127 ? 230.768 263.662 180.892 1.00 72.89  ? 2127 ILE A N     1 
ATOM   4703  C  CA    . ILE A 1 2127 ? 230.798 263.407 182.331 1.00 68.94  ? 2127 ILE A CA    1 
ATOM   4704  C  C     . ILE A 1 2127 ? 231.033 261.927 182.602 1.00 68.08  ? 2127 ILE A C     1 
ATOM   4705  O  O     . ILE A 1 2127 ? 231.820 261.557 183.480 1.00 72.09  ? 2127 ILE A O     1 
ATOM   4706  C  CB    . ILE A 1 2127 ? 229.496 263.903 182.987 1.00 64.21  ? 2127 ILE A CB    1 
ATOM   4707  C  CG1   . ILE A 1 2127 ? 229.387 265.423 182.877 1.00 70.40  ? 2127 ILE A CG1   1 
ATOM   4708  C  CG2   . ILE A 1 2127 ? 229.429 263.470 184.443 1.00 52.86  ? 2127 ILE A CG2   1 
ATOM   4709  C  CD1   . ILE A 1 2127 ? 228.071 265.974 183.373 1.00 65.13  ? 2127 ILE A CD1   1 
ATOM   4710  N  N     . ALA A 1 2128 ? 230.353 261.059 181.850 1.00 69.80  ? 2128 ALA A N     1 
ATOM   4711  C  CA    . ALA A 1 2128 ? 230.565 259.625 182.003 1.00 71.04  ? 2128 ALA A CA    1 
ATOM   4712  C  C     . ALA A 1 2128 ? 231.961 259.207 181.556 1.00 67.26  ? 2128 ALA A C     1 
ATOM   4713  O  O     . ALA A 1 2128 ? 232.551 258.298 182.151 1.00 64.80  ? 2128 ALA A O     1 
ATOM   4714  C  CB    . ALA A 1 2128 ? 229.506 258.851 181.219 1.00 70.05  ? 2128 ALA A CB    1 
ATOM   4715  N  N     . GLU A 1 2129 ? 232.501 259.848 180.517 1.00 72.00  ? 2129 GLU A N     1 
ATOM   4716  C  CA    . GLU A 1 2129 ? 233.795 259.433 179.981 1.00 73.80  ? 2129 GLU A CA    1 
ATOM   4717  C  C     . GLU A 1 2129 ? 234.922 259.681 180.977 1.00 70.62  ? 2129 GLU A C     1 
ATOM   4718  O  O     . GLU A 1 2129 ? 235.722 258.781 181.259 1.00 66.21  ? 2129 GLU A O     1 
ATOM   4719  C  CB    . GLU A 1 2129 ? 234.074 260.159 178.664 1.00 81.48  ? 2129 GLU A CB    1 
ATOM   4720  C  CG    . GLU A 1 2129 ? 234.934 259.368 177.691 1.00 88.00  ? 2129 GLU A CG    1 
ATOM   4721  C  CD    . GLU A 1 2129 ? 235.152 260.099 176.381 1.00 94.93  ? 2129 GLU A CD    1 
ATOM   4722  O  OE1   . GLU A 1 2129 ? 234.610 261.212 176.222 1.00 93.79  ? 2129 GLU A OE1   1 
ATOM   4723  O  OE2   . GLU A 1 2129 ? 235.868 259.559 175.510 1.00 94.66  ? 2129 GLU A OE2   1 
ATOM   4724  N  N     . ASN A 1 2130 ? 235.008 260.893 181.515 1.00 69.07  ? 2130 ASN A N     1 
ATOM   4725  C  CA    . ASN A 1 2130 ? 236.087 261.265 182.432 1.00 67.45  ? 2130 ASN A CA    1 
ATOM   4726  C  C     . ASN A 1 2130 ? 235.677 261.080 183.888 1.00 62.18  ? 2130 ASN A C     1 
ATOM   4727  O  O     . ASN A 1 2130 ? 235.783 261.995 184.703 1.00 63.14  ? 2130 ASN A O     1 
ATOM   4728  C  CB    . ASN A 1 2130 ? 236.534 262.698 182.163 1.00 67.05  ? 2130 ASN A CB    1 
ATOM   4729  C  CG    . ASN A 1 2130 ? 235.390 263.698 182.230 1.00 75.31  ? 2130 ASN A CG    1 
ATOM   4730  O  OD1   . ASN A 1 2130 ? 234.338 263.426 182.808 1.00 71.38  ? 2130 ASN A OD1   1 
ATOM   4731  N  ND2   . ASN A 1 2130 ? 235.596 264.867 181.634 1.00 76.24  ? 2130 ASN A ND2   1 
ATOM   4732  N  N     . LEU A 1 2131 ? 235.214 259.882 184.240 1.00 55.40  ? 2131 LEU A N     1 
ATOM   4733  C  CA    . LEU A 1 2131 ? 234.685 259.629 185.571 1.00 47.36  ? 2131 LEU A CA    1 
ATOM   4734  C  C     . LEU A 1 2131 ? 235.547 258.595 186.280 1.00 44.46  ? 2131 LEU A C     1 
ATOM   4735  O  O     . LEU A 1 2131 ? 235.691 257.471 185.778 1.00 45.70  ? 2131 LEU A O     1 
ATOM   4736  C  CB    . LEU A 1 2131 ? 233.237 259.155 185.481 1.00 44.02  ? 2131 LEU A CB    1 
ATOM   4737  C  CG    . LEU A 1 2131 ? 232.470 258.910 186.778 1.00 43.78  ? 2131 LEU A CG    1 
ATOM   4738  C  CD1   . LEU A 1 2131 ? 232.338 260.197 187.570 1.00 39.65  ? 2131 LEU A CD1   1 
ATOM   4739  C  CD2   . LEU A 1 2131 ? 231.101 258.344 186.458 1.00 41.07  ? 2131 LEU A CD2   1 
ATOM   4740  N  N     . PRO A 1 2132 ? 236.136 258.919 187.435 1.00 45.61  ? 2132 PRO A N     1 
ATOM   4741  C  CA    . PRO A 1 2132 ? 237.027 257.974 188.148 1.00 37.41  ? 2132 PRO A CA    1 
ATOM   4742  C  C     . PRO A 1 2132 ? 236.258 256.857 188.853 1.00 30.61  ? 2132 PRO A C     1 
ATOM   4743  O  O     . PRO A 1 2132 ? 235.949 256.903 190.042 1.00 29.60  ? 2132 PRO A O     1 
ATOM   4744  C  CB    . PRO A 1 2132 ? 237.757 258.884 189.139 1.00 35.22  ? 2132 PRO A CB    1 
ATOM   4745  C  CG    . PRO A 1 2132 ? 236.801 259.995 189.401 1.00 30.51  ? 2132 PRO A CG    1 
ATOM   4746  C  CD    . PRO A 1 2132 ? 236.017 260.210 188.136 1.00 38.82  ? 2132 PRO A CD    1 
ATOM   4747  N  N     . GLU A 1 2133 ? 235.933 255.819 188.080 1.00 24.62  ? 2133 GLU A N     1 
ATOM   4748  C  CA    . GLU A 1 2133 ? 235.118 254.724 188.596 1.00 21.08  ? 2133 GLU A CA    1 
ATOM   4749  C  C     . GLU A 1 2133 ? 235.835 253.957 189.699 1.00 20.66  ? 2133 GLU A C     1 
ATOM   4750  O  O     . GLU A 1 2133 ? 235.208 253.547 190.685 1.00 24.17  ? 2133 GLU A O     1 
ATOM   4751  C  CB    . GLU A 1 2133 ? 234.732 253.786 187.455 1.00 25.05  ? 2133 GLU A CB    1 
ATOM   4752  C  CG    . GLU A 1 2133 ? 233.678 254.352 186.527 1.00 29.14  ? 2133 GLU A CG    1 
ATOM   4753  C  CD    . GLU A 1 2133 ? 233.854 253.873 185.106 1.00 32.50  ? 2133 GLU A CD    1 
ATOM   4754  O  OE1   . GLU A 1 2133 ? 234.943 253.350 184.793 1.00 33.51  ? 2133 GLU A OE1   1 
ATOM   4755  O  OE2   . GLU A 1 2133 ? 232.906 254.014 184.305 1.00 34.27  ? 2133 GLU A OE2   1 
ATOM   4756  N  N     . GLN A 1 2134 ? 237.143 253.737 189.547 1.00 18.00  ? 2134 GLN A N     1 
ATOM   4757  C  CA    . GLN A 1 2134 ? 237.893 253.045 190.590 1.00 17.69  ? 2134 GLN A CA    1 
ATOM   4758  C  C     . GLN A 1 2134 ? 237.886 253.843 191.886 1.00 24.48  ? 2134 GLN A C     1 
ATOM   4759  O  O     . GLN A 1 2134 ? 237.794 253.269 192.975 1.00 28.70  ? 2134 GLN A O     1 
ATOM   4760  C  CB    . GLN A 1 2134 ? 239.324 252.778 190.126 1.00 17.61  ? 2134 GLN A CB    1 
ATOM   4761  C  CG    . GLN A 1 2134 ? 239.432 251.718 189.044 1.00 13.66  ? 2134 GLN A CG    1 
ATOM   4762  C  CD    . GLN A 1 2134 ? 240.848 251.218 188.850 1.00 17.66  ? 2134 GLN A CD    1 
ATOM   4763  O  OE1   . GLN A 1 2134 ? 241.772 251.651 189.537 1.00 19.30  ? 2134 GLN A OE1   1 
ATOM   4764  N  NE2   . GLN A 1 2134 ? 241.025 250.297 187.911 1.00 23.94  ? 2134 GLN A NE2   1 
ATOM   4765  N  N     . GLU A 1 2135 ? 237.981 255.170 191.786 1.00 20.80  ? 2135 GLU A N     1 
ATOM   4766  C  CA    . GLU A 1 2135 ? 237.888 256.012 192.974 1.00 18.35  ? 2135 GLU A CA    1 
ATOM   4767  C  C     . GLU A 1 2135 ? 236.520 255.881 193.632 1.00 17.55  ? 2135 GLU A C     1 
ATOM   4768  O  O     . GLU A 1 2135 ? 236.414 255.851 194.865 1.00 21.11  ? 2135 GLU A O     1 
ATOM   4769  C  CB    . GLU A 1 2135 ? 238.179 257.465 192.599 1.00 25.08  ? 2135 GLU A CB    1 
ATOM   4770  C  CG    . GLU A 1 2135 ? 237.857 258.476 193.680 1.00 39.76  ? 2135 GLU A CG    1 
ATOM   4771  C  CD    . GLU A 1 2135 ? 238.191 259.891 193.259 1.00 43.44  ? 2135 GLU A CD    1 
ATOM   4772  O  OE1   . GLU A 1 2135 ? 239.206 260.078 192.555 1.00 41.53  ? 2135 GLU A OE1   1 
ATOM   4773  O  OE2   . GLU A 1 2135 ? 237.437 260.816 193.625 1.00 40.78  ? 2135 GLU A OE2   1 
ATOM   4774  N  N     . ILE A 1 2136 ? 235.461 255.793 192.825 1.00 17.34  ? 2136 ILE A N     1 
ATOM   4775  C  CA    . ILE A 1 2136 ? 234.118 255.593 193.362 1.00 16.12  ? 2136 ILE A CA    1 
ATOM   4776  C  C     . ILE A 1 2136 ? 234.031 254.262 194.099 1.00 18.55  ? 2136 ILE A C     1 
ATOM   4777  O  O     . ILE A 1 2136 ? 233.441 254.171 195.184 1.00 22.52  ? 2136 ILE A O     1 
ATOM   4778  C  CB    . ILE A 1 2136 ? 233.080 255.686 192.227 1.00 16.01  ? 2136 ILE A CB    1 
ATOM   4779  C  CG1   . ILE A 1 2136 ? 232.955 257.130 191.741 1.00 20.10  ? 2136 ILE A CG1   1 
ATOM   4780  C  CG2   . ILE A 1 2136 ? 231.734 255.145 192.678 1.00 17.52  ? 2136 ILE A CG2   1 
ATOM   4781  C  CD1   . ILE A 1 2136 ? 232.245 257.269 190.417 1.00 22.17  ? 2136 ILE A CD1   1 
ATOM   4782  N  N     . LEU A 1 2137 ? 234.617 253.211 193.522 1.00 14.86  ? 2137 LEU A N     1 
ATOM   4783  C  CA    . LEU A 1 2137 ? 234.607 251.906 194.176 1.00 11.88  ? 2137 LEU A CA    1 
ATOM   4784  C  C     . LEU A 1 2137 ? 235.387 251.936 195.487 1.00 13.91  ? 2137 LEU A C     1 
ATOM   4785  O  O     . LEU A 1 2137 ? 234.965 251.333 196.481 1.00 19.19  ? 2137 LEU A O     1 
ATOM   4786  C  CB    . LEU A 1 2137 ? 235.176 250.847 193.231 1.00 18.07  ? 2137 LEU A CB    1 
ATOM   4787  C  CG    . LEU A 1 2137 ? 234.568 249.446 193.319 1.00 17.00  ? 2137 LEU A CG    1 
ATOM   4788  C  CD1   . LEU A 1 2137 ? 233.115 249.472 192.884 1.00 19.50  ? 2137 LEU A CD1   1 
ATOM   4789  C  CD2   . LEU A 1 2137 ? 235.360 248.471 192.469 1.00 12.46  ? 2137 LEU A CD2   1 
ATOM   4790  N  N     . ILE A 1 2138 ? 236.530 252.626 195.505 1.00 16.30  ? 2138 ILE A N     1 
ATOM   4791  C  CA    . ILE A 1 2138 ? 237.302 252.762 196.740 1.00 17.35  ? 2138 ILE A CA    1 
ATOM   4792  C  C     . ILE A 1 2138 ? 236.491 253.496 197.797 1.00 15.47  ? 2138 ILE A C     1 
ATOM   4793  O  O     . ILE A 1 2138 ? 236.494 253.119 198.976 1.00 16.52  ? 2138 ILE A O     1 
ATOM   4794  C  CB    . ILE A 1 2138 ? 238.642 253.473 196.472 1.00 21.48  ? 2138 ILE A CB    1 
ATOM   4795  C  CG1   . ILE A 1 2138 ? 239.475 252.697 195.457 1.00 21.85  ? 2138 ILE A CG1   1 
ATOM   4796  C  CG2   . ILE A 1 2138 ? 239.427 253.643 197.762 1.00 19.29  ? 2138 ILE A CG2   1 
ATOM   4797  C  CD1   . ILE A 1 2138 ? 239.827 251.318 195.917 1.00 25.91  ? 2138 ILE A CD1   1 
ATOM   4798  N  N     . GLN A 1 2139 ? 235.800 254.566 197.399 1.00 14.53  ? 2139 GLN A N     1 
ATOM   4799  C  CA    . GLN A 1 2139 ? 234.970 255.299 198.347 1.00 17.44  ? 2139 GLN A CA    1 
ATOM   4800  C  C     . GLN A 1 2139 ? 233.865 254.415 198.907 1.00 18.65  ? 2139 GLN A C     1 
ATOM   4801  O  O     . GLN A 1 2139 ? 233.587 254.446 200.110 1.00 19.24  ? 2139 GLN A O     1 
ATOM   4802  C  CB    . GLN A 1 2139 ? 234.380 256.541 197.680 1.00 18.18  ? 2139 GLN A CB    1 
ATOM   4803  C  CG    . GLN A 1 2139 ? 233.328 257.247 198.516 1.00 19.67  ? 2139 GLN A CG    1 
ATOM   4804  C  CD    . GLN A 1 2139 ? 232.710 258.425 197.799 1.00 27.50  ? 2139 GLN A CD    1 
ATOM   4805  O  OE1   . GLN A 1 2139 ? 233.335 259.035 196.934 1.00 40.86  ? 2139 GLN A OE1   1 
ATOM   4806  N  NE2   . GLN A 1 2139 ? 231.481 258.762 198.166 1.00 24.58  ? 2139 GLN A NE2   1 
ATOM   4807  N  N     . SER A 1 2140 ? 233.227 253.618 198.048 1.00 21.58  ? 2140 SER A N     1 
ATOM   4808  C  CA    . SER A 1 2140 ? 232.193 252.699 198.515 1.00 12.17  ? 2140 SER A CA    1 
ATOM   4809  C  C     . SER A 1 2140 ? 232.755 251.687 199.506 1.00 10.20  ? 2140 SER A C     1 
ATOM   4810  O  O     . SER A 1 2140 ? 232.154 251.433 200.559 1.00 15.81  ? 2140 SER A O     1 
ATOM   4811  C  CB    . SER A 1 2140 ? 231.560 251.982 197.324 1.00 12.48  ? 2140 SER A CB    1 
ATOM   4812  O  OG    . SER A 1 2140 ? 230.485 251.160 197.735 1.00 25.99  ? 2140 SER A OG    1 
ATOM   4813  N  N     . VAL A 1 2141 ? 233.915 251.109 199.189 1.00 10.03  ? 2141 VAL A N     1 
ATOM   4814  C  CA    . VAL A 1 2141 ? 234.523 250.114 200.068 1.00 10.24  ? 2141 VAL A CA    1 
ATOM   4815  C  C     . VAL A 1 2141 ? 234.860 250.733 201.417 1.00 13.39  ? 2141 VAL A C     1 
ATOM   4816  O  O     . VAL A 1 2141 ? 234.592 250.145 202.472 1.00 12.65  ? 2141 VAL A O     1 
ATOM   4817  C  CB    . VAL A 1 2141 ? 235.766 249.502 199.397 1.00 9.33   ? 2141 VAL A CB    1 
ATOM   4818  C  CG1   . VAL A 1 2141 ? 236.621 248.769 200.419 1.00 9.23   ? 2141 VAL A CG1   1 
ATOM   4819  C  CG2   . VAL A 1 2141 ? 235.355 248.571 198.274 1.00 7.86   ? 2141 VAL A CG2   1 
ATOM   4820  N  N     . CYS A 1 2142 ? 235.444 251.932 201.408 1.00 17.73  ? 2142 CYS A N     1 
ATOM   4821  C  CA    . CYS A 1 2142 ? 235.786 252.596 202.660 1.00 14.26  ? 2142 CYS A CA    1 
ATOM   4822  C  C     . CYS A 1 2142 ? 234.537 252.950 203.459 1.00 16.10  ? 2142 CYS A C     1 
ATOM   4823  O  O     . CYS A 1 2142 ? 234.529 252.839 204.690 1.00 21.71  ? 2142 CYS A O     1 
ATOM   4824  C  CB    . CYS A 1 2142 ? 236.621 253.843 202.380 1.00 14.40  ? 2142 CYS A CB    1 
ATOM   4825  S  SG    . CYS A 1 2142 ? 238.280 253.493 201.759 1.00 30.75  ? 2142 CYS A SG    1 
ATOM   4826  N  N     . GLU A 1 2143 ? 233.472 253.378 202.781 1.00 12.53  ? 2143 GLU A N     1 
ATOM   4827  C  CA    . GLU A 1 2143 ? 232.247 253.735 203.483 1.00 12.02  ? 2143 GLU A CA    1 
ATOM   4828  C  C     . GLU A 1 2143 ? 231.564 252.518 204.087 1.00 14.08  ? 2143 GLU A C     1 
ATOM   4829  O  O     . GLU A 1 2143 ? 230.878 252.641 205.106 1.00 21.97  ? 2143 GLU A O     1 
ATOM   4830  C  CB    . GLU A 1 2143 ? 231.291 254.459 202.537 1.00 16.71  ? 2143 GLU A CB    1 
ATOM   4831  C  CG    . GLU A 1 2143 ? 231.619 255.926 202.321 1.00 27.95  ? 2143 GLU A CG    1 
ATOM   4832  C  CD    . GLU A 1 2143 ? 230.626 256.612 201.407 1.00 39.48  ? 2143 GLU A CD    1 
ATOM   4833  O  OE1   . GLU A 1 2143 ? 229.632 255.964 201.015 1.00 39.46  ? 2143 GLU A OE1   1 
ATOM   4834  O  OE2   . GLU A 1 2143 ? 230.839 257.798 201.076 1.00 38.40  ? 2143 GLU A OE2   1 
ATOM   4835  N  N     . THR A 1 2144 ? 231.731 251.340 203.484 1.00 12.18  ? 2144 THR A N     1 
ATOM   4836  C  CA    . THR A 1 2144 ? 230.998 250.162 203.936 1.00 9.59   ? 2144 THR A CA    1 
ATOM   4837  C  C     . THR A 1 2144 ? 231.865 249.175 204.714 1.00 13.74  ? 2144 THR A C     1 
ATOM   4838  O  O     . THR A 1 2144 ? 231.417 248.629 205.726 1.00 22.16  ? 2144 THR A O     1 
ATOM   4839  C  CB    . THR A 1 2144 ? 230.350 249.469 202.732 1.00 17.93  ? 2144 THR A CB    1 
ATOM   4840  O  OG1   . THR A 1 2144 ? 229.477 250.391 202.069 1.00 20.58  ? 2144 THR A OG1   1 
ATOM   4841  C  CG2   . THR A 1 2144 ? 229.514 248.294 203.188 1.00 18.29  ? 2144 THR A CG2   1 
ATOM   4842  N  N     . MET A 1 2145 ? 233.103 248.935 204.272 1.00 14.50  ? 2145 MET A N     1 
ATOM   4843  C  CA    . MET A 1 2145 ? 233.956 247.942 204.926 1.00 8.73   ? 2145 MET A CA    1 
ATOM   4844  C  C     . MET A 1 2145 ? 234.757 248.523 206.086 1.00 9.34   ? 2145 MET A C     1 
ATOM   4845  O  O     . MET A 1 2145 ? 234.880 247.881 207.134 1.00 10.22  ? 2145 MET A O     1 
ATOM   4846  C  CB    . MET A 1 2145 ? 234.907 247.308 203.909 1.00 9.53   ? 2145 MET A CB    1 
ATOM   4847  C  CG    . MET A 1 2145 ? 234.248 246.469 202.825 1.00 13.39  ? 2145 MET A CG    1 
ATOM   4848  S  SD    . MET A 1 2145 ? 233.366 245.047 203.502 1.00 46.03  ? 2145 MET A SD    1 
ATOM   4849  C  CE    . MET A 1 2145 ? 231.669 245.590 203.431 1.00 14.13  ? 2145 MET A CE    1 
ATOM   4850  N  N     . VAL A 1 2146 ? 235.322 249.722 205.912 1.00 11.65  ? 2146 VAL A N     1 
ATOM   4851  C  CA    . VAL A 1 2146 ? 236.256 250.256 206.911 1.00 8.90   ? 2146 VAL A CA    1 
ATOM   4852  C  C     . VAL A 1 2146 ? 235.653 250.360 208.307 1.00 7.42   ? 2146 VAL A C     1 
ATOM   4853  O  O     . VAL A 1 2146 ? 236.341 250.001 209.274 1.00 10.24  ? 2146 VAL A O     1 
ATOM   4854  C  CB    . VAL A 1 2146 ? 236.855 251.579 206.416 1.00 8.20   ? 2146 VAL A CB    1 
ATOM   4855  C  CG1   . VAL A 1 2146 ? 237.464 252.364 207.567 1.00 9.27   ? 2146 VAL A CG1   1 
ATOM   4856  C  CG2   . VAL A 1 2146 ? 237.899 251.312 205.346 1.00 10.39  ? 2146 VAL A CG2   1 
ATOM   4857  N  N     . PRO A 1 2147 ? 234.412 250.828 208.503 1.00 7.69   ? 2147 PRO A N     1 
ATOM   4858  C  CA    . PRO A 1 2147 ? 233.930 251.037 209.882 1.00 5.02   ? 2147 PRO A CA    1 
ATOM   4859  C  C     . PRO A 1 2147 ? 233.972 249.801 210.766 1.00 5.48   ? 2147 PRO A C     1 
ATOM   4860  O  O     . PRO A 1 2147 ? 234.103 249.939 211.989 1.00 6.63   ? 2147 PRO A O     1 
ATOM   4861  C  CB    . PRO A 1 2147 ? 232.491 251.524 209.673 1.00 3.88   ? 2147 PRO A CB    1 
ATOM   4862  C  CG    . PRO A 1 2147 ? 232.516 252.180 208.362 1.00 5.48   ? 2147 PRO A CG    1 
ATOM   4863  C  CD    . PRO A 1 2147 ? 233.455 251.374 207.522 1.00 7.53   ? 2147 PRO A CD    1 
ATOM   4864  N  N     . LYS A 1 2148 ? 233.854 248.602 210.202 1.00 5.21   ? 2148 LYS A N     1 
ATOM   4865  C  CA    . LYS A 1 2148 ? 233.852 247.387 211.007 1.00 5.08   ? 2148 LYS A CA    1 
ATOM   4866  C  C     . LYS A 1 2148 ? 235.248 246.870 211.324 1.00 7.26   ? 2148 LYS A C     1 
ATOM   4867  O  O     . LYS A 1 2148 ? 235.379 245.950 212.138 1.00 8.79   ? 2148 LYS A O     1 
ATOM   4868  C  CB    . LYS A 1 2148 ? 233.060 246.286 210.298 1.00 7.32   ? 2148 LYS A CB    1 
ATOM   4869  C  CG    . LYS A 1 2148 ? 233.768 245.679 209.103 1.00 7.23   ? 2148 LYS A CG    1 
ATOM   4870  C  CD    . LYS A 1 2148 ? 232.890 244.655 208.411 1.00 12.08  ? 2148 LYS A CD    1 
ATOM   4871  C  CE    . LYS A 1 2148 ? 233.601 244.026 207.232 1.00 9.41   ? 2148 LYS A CE    1 
ATOM   4872  N  NZ    . LYS A 1 2148 ? 232.726 243.058 206.520 1.00 15.57  ? 2148 LYS A NZ    1 
ATOM   4873  N  N     . LEU A 1 2149 ? 236.286 247.431 210.714 1.00 7.11   ? 2149 LEU A N     1 
ATOM   4874  C  CA    . LEU A 1 2149 ? 237.631 246.902 210.886 1.00 7.04   ? 2149 LEU A CA    1 
ATOM   4875  C  C     . LEU A 1 2149 ? 238.172 247.218 212.274 1.00 8.86   ? 2149 LEU A C     1 
ATOM   4876  O  O     . LEU A 1 2149 ? 237.936 248.298 212.822 1.00 16.46  ? 2149 LEU A O     1 
ATOM   4877  C  CB    . LEU A 1 2149 ? 238.564 247.478 209.824 1.00 7.84   ? 2149 LEU A CB    1 
ATOM   4878  C  CG    . LEU A 1 2149 ? 238.245 247.142 208.370 1.00 8.06   ? 2149 LEU A CG    1 
ATOM   4879  C  CD1   . LEU A 1 2149 ? 239.315 247.714 207.463 1.00 8.91   ? 2149 LEU A CD1   1 
ATOM   4880  C  CD2   . LEU A 1 2149 ? 238.115 245.641 208.181 1.00 6.13   ? 2149 LEU A CD2   1 
ATOM   4881  N  N     . VAL A 1 2150 ? 238.908 246.264 212.840 1.00 7.41   ? 2150 VAL A N     1 
ATOM   4882  C  CA    . VAL A 1 2150 ? 239.647 246.490 214.076 1.00 7.58   ? 2150 VAL A CA    1 
ATOM   4883  C  C     . VAL A 1 2150 ? 240.924 247.241 213.728 1.00 11.22  ? 2150 VAL A C     1 
ATOM   4884  O  O     . VAL A 1 2150 ? 241.273 247.376 212.550 1.00 13.99  ? 2150 VAL A O     1 
ATOM   4885  C  CB    . VAL A 1 2150 ? 239.950 245.173 214.812 1.00 7.47   ? 2150 VAL A CB    1 
ATOM   4886  C  CG1   . VAL A 1 2150 ? 238.659 244.497 215.245 1.00 5.31   ? 2150 VAL A CG1   1 
ATOM   4887  C  CG2   . VAL A 1 2150 ? 240.771 244.250 213.932 1.00 9.77   ? 2150 VAL A CG2   1 
ATOM   4888  N  N     . ALA A 1 2151 ? 241.626 247.739 214.749 1.00 13.49  ? 2151 ALA A N     1 
ATOM   4889  C  CA    . ALA A 1 2151 ? 242.792 248.583 214.508 1.00 13.72  ? 2151 ALA A CA    1 
ATOM   4890  C  C     . ALA A 1 2151 ? 243.878 247.840 213.739 1.00 13.80  ? 2151 ALA A C     1 
ATOM   4891  O  O     . ALA A 1 2151 ? 244.500 248.403 212.831 1.00 12.69  ? 2151 ALA A O     1 
ATOM   4892  C  CB    . ALA A 1 2151 ? 243.340 249.108 215.834 1.00 13.71  ? 2151 ALA A CB    1 
ATOM   4893  N  N     . GLU A 1 2152 ? 244.120 246.576 214.087 1.00 16.16  ? 2152 GLU A N     1 
ATOM   4894  C  CA    . GLU A 1 2152 ? 245.200 245.824 213.460 1.00 17.08  ? 2152 GLU A CA    1 
ATOM   4895  C  C     . GLU A 1 2152 ? 244.880 245.415 212.027 1.00 19.51  ? 2152 GLU A C     1 
ATOM   4896  O  O     . GLU A 1 2152 ? 245.789 245.004 211.298 1.00 20.47  ? 2152 GLU A O     1 
ATOM   4897  C  CB    . GLU A 1 2152 ? 245.528 244.585 214.293 1.00 17.76  ? 2152 GLU A CB    1 
ATOM   4898  C  CG    . GLU A 1 2152 ? 244.335 243.679 214.555 1.00 23.87  ? 2152 GLU A CG    1 
ATOM   4899  C  CD    . GLU A 1 2152 ? 243.790 243.821 215.963 1.00 35.07  ? 2152 GLU A CD    1 
ATOM   4900  O  OE1   . GLU A 1 2152 ? 243.716 244.963 216.464 1.00 29.13  ? 2152 GLU A OE1   1 
ATOM   4901  O  OE2   . GLU A 1 2152 ? 243.431 242.790 216.570 1.00 34.17  ? 2152 GLU A OE2   1 
ATOM   4902  N  N     . ASP A 1 2153 ? 243.619 245.513 211.608 1.00 16.32  ? 2153 ASP A N     1 
ATOM   4903  C  CA    . ASP A 1 2153 ? 243.212 245.096 210.272 1.00 13.24  ? 2153 ASP A CA    1 
ATOM   4904  C  C     . ASP A 1 2153 ? 243.041 246.254 209.299 1.00 17.59  ? 2153 ASP A C     1 
ATOM   4905  O  O     . ASP A 1 2153 ? 242.929 246.013 208.093 1.00 24.90  ? 2153 ASP A O     1 
ATOM   4906  C  CB    . ASP A 1 2153 ? 241.907 244.296 210.344 1.00 9.42   ? 2153 ASP A CB    1 
ATOM   4907  C  CG    . ASP A 1 2153 ? 242.116 242.889 210.864 1.00 17.77  ? 2153 ASP A CG    1 
ATOM   4908  O  OD1   . ASP A 1 2153 ? 243.275 242.427 210.885 1.00 25.80  ? 2153 ASP A OD1   1 
ATOM   4909  O  OD2   . ASP A 1 2153 ? 241.123 242.245 211.254 1.00 18.15  ? 2153 ASP A OD2   1 
ATOM   4910  N  N     . ILE A 1 2154 ? 243.006 247.495 209.788 1.00 12.55  ? 2154 ILE A N     1 
ATOM   4911  C  CA    . ILE A 1 2154 ? 242.896 248.644 208.887 1.00 12.74  ? 2154 ILE A CA    1 
ATOM   4912  C  C     . ILE A 1 2154 ? 244.094 248.756 207.950 1.00 17.18  ? 2154 ILE A C     1 
ATOM   4913  O  O     . ILE A 1 2154 ? 243.885 248.919 206.734 1.00 21.39  ? 2154 ILE A O     1 
ATOM   4914  C  CB    . ILE A 1 2154 ? 242.652 249.927 209.700 1.00 14.90  ? 2154 ILE A CB    1 
ATOM   4915  C  CG1   . ILE A 1 2154 ? 241.340 249.822 210.480 1.00 11.36  ? 2154 ILE A CG1   1 
ATOM   4916  C  CG2   . ILE A 1 2154 ? 242.635 251.145 208.793 1.00 17.25  ? 2154 ILE A CG2   1 
ATOM   4917  C  CD1   . ILE A 1 2154 ? 241.025 251.040 211.313 1.00 13.86  ? 2154 ILE A CD1   1 
ATOM   4918  N  N     . PRO A 1 2155 ? 245.350 248.693 208.421 1.00 17.05  ? 2155 PRO A N     1 
ATOM   4919  C  CA    . PRO A 1 2155 ? 246.470 248.762 207.470 1.00 15.89  ? 2155 PRO A CA    1 
ATOM   4920  C  C     . PRO A 1 2155 ? 246.462 247.638 206.453 1.00 18.14  ? 2155 PRO A C     1 
ATOM   4921  O  O     . PRO A 1 2155 ? 246.840 247.855 205.297 1.00 19.10  ? 2155 PRO A O     1 
ATOM   4922  C  CB    . PRO A 1 2155 ? 247.706 248.695 208.378 1.00 13.83  ? 2155 PRO A CB    1 
ATOM   4923  C  CG    . PRO A 1 2155 ? 247.231 249.158 209.698 1.00 14.52  ? 2155 PRO A CG    1 
ATOM   4924  C  CD    . PRO A 1 2155 ? 245.837 248.637 209.812 1.00 16.55  ? 2155 PRO A CD    1 
ATOM   4925  N  N     . LEU A 1 2156 ? 246.037 246.438 206.851 1.00 16.59  ? 2156 LEU A N     1 
ATOM   4926  C  CA    . LEU A 1 2156 ? 245.992 245.321 205.915 1.00 16.11  ? 2156 LEU A CA    1 
ATOM   4927  C  C     . LEU A 1 2156 ? 245.006 245.592 204.785 1.00 16.14  ? 2156 LEU A C     1 
ATOM   4928  O  O     . LEU A 1 2156 ? 245.316 245.378 203.608 1.00 21.39  ? 2156 LEU A O     1 
ATOM   4929  C  CB    . LEU A 1 2156 ? 245.627 244.035 206.652 1.00 17.78  ? 2156 LEU A CB    1 
ATOM   4930  C  CG    . LEU A 1 2156 ? 246.523 243.618 207.816 1.00 16.34  ? 2156 LEU A CG    1 
ATOM   4931  C  CD1   . LEU A 1 2156 ? 246.028 242.317 208.422 1.00 23.94  ? 2156 LEU A CD1   1 
ATOM   4932  C  CD2   . LEU A 1 2156 ? 247.964 243.484 207.356 1.00 14.25  ? 2156 LEU A CD2   1 
ATOM   4933  N  N     . LEU A 1 2157 ? 243.812 246.080 205.126 1.00 12.54  ? 2157 LEU A N     1 
ATOM   4934  C  CA    . LEU A 1 2157 ? 242.817 246.354 204.097 1.00 12.22  ? 2157 LEU A CA    1 
ATOM   4935  C  C     . LEU A 1 2157 ? 243.242 247.520 203.215 1.00 15.23  ? 2157 LEU A C     1 
ATOM   4936  O  O     . LEU A 1 2157 ? 242.995 247.509 202.004 1.00 20.13  ? 2157 LEU A O     1 
ATOM   4937  C  CB    . LEU A 1 2157 ? 241.452 246.622 204.731 1.00 11.86  ? 2157 LEU A CB    1 
ATOM   4938  C  CG    . LEU A 1 2157 ? 240.281 246.762 203.757 1.00 8.54   ? 2157 LEU A CG    1 
ATOM   4939  C  CD1   . LEU A 1 2157 ? 239.074 245.992 204.254 1.00 7.97   ? 2157 LEU A CD1   1 
ATOM   4940  C  CD2   . LEU A 1 2157 ? 239.922 248.224 203.546 1.00 9.87   ? 2157 LEU A CD2   1 
ATOM   4941  N  N     . PHE A 1 2158 ? 243.889 248.533 203.793 1.00 16.46  ? 2158 PHE A N     1 
ATOM   4942  C  CA    . PHE A 1 2158 ? 244.330 249.647 202.960 1.00 18.75  ? 2158 PHE A CA    1 
ATOM   4943  C  C     . PHE A 1 2158 ? 245.484 249.247 202.046 1.00 22.66  ? 2158 PHE A C     1 
ATOM   4944  O  O     . PHE A 1 2158 ? 245.559 249.719 200.905 1.00 30.34  ? 2158 PHE A O     1 
ATOM   4945  C  CB    . PHE A 1 2158 ? 244.701 250.844 203.833 1.00 17.75  ? 2158 PHE A CB    1 
ATOM   4946  C  CG    . PHE A 1 2158 ? 243.535 251.739 204.137 1.00 21.79  ? 2158 PHE A CG    1 
ATOM   4947  C  CD1   . PHE A 1 2158 ? 242.732 252.215 203.116 1.00 20.47  ? 2158 PHE A CD1   1 
ATOM   4948  C  CD2   . PHE A 1 2158 ? 243.232 252.089 205.439 1.00 27.69  ? 2158 PHE A CD2   1 
ATOM   4949  C  CE1   . PHE A 1 2158 ? 241.653 253.032 203.388 1.00 19.03  ? 2158 PHE A CE1   1 
ATOM   4950  C  CE2   . PHE A 1 2158 ? 242.154 252.906 205.716 1.00 32.07  ? 2158 PHE A CE2   1 
ATOM   4951  C  CZ    . PHE A 1 2158 ? 241.364 253.377 204.689 1.00 26.78  ? 2158 PHE A CZ    1 
ATOM   4952  N  N     . SER A 1 2159 ? 246.376 248.366 202.508 1.00 16.03  ? 2159 SER A N     1 
ATOM   4953  C  CA    . SER A 1 2159 ? 247.403 247.823 201.626 1.00 15.81  ? 2159 SER A CA    1 
ATOM   4954  C  C     . SER A 1 2159 ? 246.784 246.975 200.523 1.00 16.09  ? 2159 SER A C     1 
ATOM   4955  O  O     . SER A 1 2159 ? 247.240 247.008 199.374 1.00 18.81  ? 2159 SER A O     1 
ATOM   4956  C  CB    . SER A 1 2159 ? 248.410 247.004 202.432 1.00 18.67  ? 2159 SER A CB    1 
ATOM   4957  O  OG    . SER A 1 2159 ? 249.059 247.805 203.403 1.00 27.38  ? 2159 SER A OG    1 
ATOM   4958  N  N     . LEU A 1 2160 ? 245.747 246.202 200.855 1.00 14.24  ? 2160 LEU A N     1 
ATOM   4959  C  CA    . LEU A 1 2160 ? 245.041 245.432 199.835 1.00 15.07  ? 2160 LEU A CA    1 
ATOM   4960  C  C     . LEU A 1 2160 ? 244.416 246.350 198.793 1.00 19.30  ? 2160 LEU A C     1 
ATOM   4961  O  O     . LEU A 1 2160 ? 244.442 246.052 197.595 1.00 25.66  ? 2160 LEU A O     1 
ATOM   4962  C  CB    . LEU A 1 2160 ? 243.972 244.557 200.489 1.00 15.06  ? 2160 LEU A CB    1 
ATOM   4963  C  CG    . LEU A 1 2160 ? 244.370 243.151 200.944 1.00 16.23  ? 2160 LEU A CG    1 
ATOM   4964  C  CD1   . LEU A 1 2160 ? 243.136 242.323 201.244 1.00 15.05  ? 2160 LEU A CD1   1 
ATOM   4965  C  CD2   . LEU A 1 2160 ? 245.231 242.462 199.910 1.00 14.18  ? 2160 LEU A CD2   1 
ATOM   4966  N  N     . LEU A 1 2161 ? 243.835 247.467 199.237 1.00 18.24  ? 2161 LEU A N     1 
ATOM   4967  C  CA    . LEU A 1 2161 ? 243.298 248.453 198.304 1.00 18.94  ? 2161 LEU A CA    1 
ATOM   4968  C  C     . LEU A 1 2161 ? 244.395 249.035 197.421 1.00 17.93  ? 2161 LEU A C     1 
ATOM   4969  O  O     . LEU A 1 2161 ? 244.216 249.174 196.207 1.00 23.36  ? 2161 LEU A O     1 
ATOM   4970  C  CB    . LEU A 1 2161 ? 242.589 249.569 199.069 1.00 21.39  ? 2161 LEU A CB    1 
ATOM   4971  C  CG    . LEU A 1 2161 ? 241.154 249.338 199.537 1.00 16.68  ? 2161 LEU A CG    1 
ATOM   4972  C  CD1   . LEU A 1 2161 ? 240.549 250.647 200.002 1.00 22.89  ? 2161 LEU A CD1   1 
ATOM   4973  C  CD2   . LEU A 1 2161 ? 240.325 248.750 198.415 1.00 12.22  ? 2161 LEU A CD2   1 
ATOM   4974  N  N     . SER A 1 2162 ? 245.537 249.382 198.017 1.00 20.54  ? 2162 SER A N     1 
ATOM   4975  C  CA    . SER A 1 2162 ? 246.625 249.975 197.246 1.00 24.77  ? 2162 SER A CA    1 
ATOM   4976  C  C     . SER A 1 2162 ? 247.229 248.982 196.260 1.00 18.85  ? 2162 SER A C     1 
ATOM   4977  O  O     . SER A 1 2162 ? 247.783 249.392 195.234 1.00 18.36  ? 2162 SER A O     1 
ATOM   4978  C  CB    . SER A 1 2162 ? 247.702 250.511 198.189 1.00 24.00  ? 2162 SER A CB    1 
ATOM   4979  O  OG    . SER A 1 2162 ? 247.148 251.402 199.138 1.00 26.25  ? 2162 SER A OG    1 
ATOM   4980  N  N     . ASP A 1 2163 ? 247.149 247.684 196.556 1.00 21.86  ? 2163 ASP A N     1 
ATOM   4981  C  CA    . ASP A 1 2163 ? 247.691 246.688 195.637 1.00 20.01  ? 2163 ASP A CA    1 
ATOM   4982  C  C     . ASP A 1 2163 ? 246.699 246.360 194.527 1.00 19.81  ? 2163 ASP A C     1 
ATOM   4983  O  O     . ASP A 1 2163 ? 247.066 246.313 193.347 1.00 25.31  ? 2163 ASP A O     1 
ATOM   4984  C  CB    . ASP A 1 2163 ? 248.081 245.424 196.403 1.00 18.96  ? 2163 ASP A CB    1 
ATOM   4985  C  CG    . ASP A 1 2163 ? 249.170 245.676 197.425 1.00 29.57  ? 2163 ASP A CG    1 
ATOM   4986  O  OD1   . ASP A 1 2163 ? 249.402 244.795 198.278 1.00 34.00  ? 2163 ASP A OD1   1 
ATOM   4987  O  OD2   . ASP A 1 2163 ? 249.795 246.755 197.376 1.00 29.50  ? 2163 ASP A OD2   1 
ATOM   4988  N  N     . VAL A 1 2164 ? 245.435 246.122 194.884 1.00 19.02  ? 2164 VAL A N     1 
ATOM   4989  C  CA    . VAL A 1 2164 ? 244.435 245.760 193.884 1.00 18.31  ? 2164 VAL A CA    1 
ATOM   4990  C  C     . VAL A 1 2164 ? 244.097 246.957 193.004 1.00 20.80  ? 2164 VAL A C     1 
ATOM   4991  O  O     . VAL A 1 2164 ? 243.972 246.829 191.779 1.00 26.52  ? 2164 VAL A O     1 
ATOM   4992  C  CB    . VAL A 1 2164 ? 243.184 245.182 194.569 1.00 20.73  ? 2164 VAL A CB    1 
ATOM   4993  C  CG1   . VAL A 1 2164 ? 242.000 245.214 193.627 1.00 15.08  ? 2164 VAL A CG1   1 
ATOM   4994  C  CG2   . VAL A 1 2164 ? 243.448 243.764 195.046 1.00 20.33  ? 2164 VAL A CG2   1 
ATOM   4995  N  N     . PHE A 1 2165 ? 243.944 248.135 193.605 1.00 21.04  ? 2165 PHE A N     1 
ATOM   4996  C  CA    . PHE A 1 2165 ? 243.701 249.360 192.854 1.00 19.05  ? 2165 PHE A CA    1 
ATOM   4997  C  C     . PHE A 1 2165 ? 244.900 250.289 192.992 1.00 23.19  ? 2165 PHE A C     1 
ATOM   4998  O  O     . PHE A 1 2165 ? 244.868 251.225 193.800 1.00 28.50  ? 2165 PHE A O     1 
ATOM   4999  C  CB    . PHE A 1 2165 ? 242.435 250.068 193.341 1.00 18.68  ? 2165 PHE A CB    1 
ATOM   5000  C  CG    . PHE A 1 2165 ? 241.192 249.231 193.263 1.00 16.42  ? 2165 PHE A CG    1 
ATOM   5001  C  CD1   . PHE A 1 2165 ? 240.406 249.243 192.125 1.00 16.74  ? 2165 PHE A CD1   1 
ATOM   5002  C  CD2   . PHE A 1 2165 ? 240.795 248.451 194.336 1.00 18.36  ? 2165 PHE A CD2   1 
ATOM   5003  C  CE1   . PHE A 1 2165 ? 239.256 248.483 192.052 1.00 18.91  ? 2165 PHE A CE1   1 
ATOM   5004  C  CE2   . PHE A 1 2165 ? 239.644 247.692 194.269 1.00 19.39  ? 2165 PHE A CE2   1 
ATOM   5005  C  CZ    . PHE A 1 2165 ? 238.875 247.706 193.125 1.00 16.05  ? 2165 PHE A CZ    1 
ATOM   5006  N  N     . PRO A 1 2166 ? 245.970 250.072 192.228 1.00 25.29  ? 2166 PRO A N     1 
ATOM   5007  C  CA    . PRO A 1 2166 ? 247.165 250.905 192.388 1.00 25.67  ? 2166 PRO A CA    1 
ATOM   5008  C  C     . PRO A 1 2166 ? 247.012 252.252 191.700 1.00 31.33  ? 2166 PRO A C     1 
ATOM   5009  O  O     . PRO A 1 2166 ? 246.351 252.377 190.666 1.00 34.36  ? 2166 PRO A O     1 
ATOM   5010  C  CB    . PRO A 1 2166 ? 248.262 250.067 191.725 1.00 23.43  ? 2166 PRO A CB    1 
ATOM   5011  C  CG    . PRO A 1 2166 ? 247.541 249.310 190.666 1.00 27.81  ? 2166 PRO A CG    1 
ATOM   5012  C  CD    . PRO A 1 2166 ? 246.141 249.059 191.174 1.00 23.65  ? 2166 PRO A CD    1 
ATOM   5013  N  N     . GLY A 1 2167 ? 247.634 253.268 192.293 1.00 27.81  ? 2167 GLY A N     1 
ATOM   5014  C  CA    . GLY A 1 2167 ? 247.667 254.589 191.706 1.00 34.91  ? 2167 GLY A CA    1 
ATOM   5015  C  C     . GLY A 1 2167 ? 246.431 255.429 191.928 1.00 36.85  ? 2167 GLY A C     1 
ATOM   5016  O  O     . GLY A 1 2167 ? 246.397 256.578 191.469 1.00 46.43  ? 2167 GLY A O     1 
ATOM   5017  N  N     . VAL A 1 2168 ? 245.419 254.905 192.611 1.00 31.70  ? 2168 VAL A N     1 
ATOM   5018  C  CA    . VAL A 1 2168 ? 244.195 255.638 192.900 1.00 35.89  ? 2168 VAL A CA    1 
ATOM   5019  C  C     . VAL A 1 2168 ? 244.040 255.735 194.410 1.00 32.50  ? 2168 VAL A C     1 
ATOM   5020  O  O     . VAL A 1 2168 ? 244.275 254.757 195.131 1.00 24.46  ? 2168 VAL A O     1 
ATOM   5021  C  CB    . VAL A 1 2168 ? 242.964 254.984 192.240 1.00 32.24  ? 2168 VAL A CB    1 
ATOM   5022  C  CG1   . VAL A 1 2168 ? 242.692 253.607 192.815 1.00 26.13  ? 2168 VAL A CG1   1 
ATOM   5023  C  CG2   . VAL A 1 2168 ? 241.740 255.875 192.392 1.00 31.59  ? 2168 VAL A CG2   1 
ATOM   5024  N  N     . GLN A 1 2169 ? 243.690 256.923 194.890 1.00 41.84  ? 2169 GLN A N     1 
ATOM   5025  C  CA    . GLN A 1 2169 ? 243.494 257.171 196.308 1.00 40.98  ? 2169 GLN A CA    1 
ATOM   5026  C  C     . GLN A 1 2169 ? 242.179 257.905 196.520 1.00 46.21  ? 2169 GLN A C     1 
ATOM   5027  O  O     . GLN A 1 2169 ? 241.746 258.697 195.677 1.00 47.98  ? 2169 GLN A O     1 
ATOM   5028  C  CB    . GLN A 1 2169 ? 244.654 257.983 196.903 1.00 44.08  ? 2169 GLN A CB    1 
ATOM   5029  C  CG    . GLN A 1 2169 ? 244.719 259.431 196.438 1.00 54.60  ? 2169 GLN A CG    1 
ATOM   5030  C  CD    . GLN A 1 2169 ? 245.445 259.599 195.116 1.00 61.40  ? 2169 GLN A CD    1 
ATOM   5031  O  OE1   . GLN A 1 2169 ? 245.649 258.637 194.378 1.00 58.64  ? 2169 GLN A OE1   1 
ATOM   5032  N  NE2   . GLN A 1 2169 ? 245.836 260.831 194.810 1.00 63.88  ? 2169 GLN A NE2   1 
ATOM   5033  N  N     . TYR A 1 2170 ? 241.539 257.624 197.649 1.00 43.49  ? 2170 TYR A N     1 
ATOM   5034  C  CA    . TYR A 1 2170 ? 240.298 258.275 198.034 1.00 43.36  ? 2170 TYR A CA    1 
ATOM   5035  C  C     . TYR A 1 2170 ? 240.485 258.966 199.375 1.00 46.12  ? 2170 TYR A C     1 
ATOM   5036  O  O     . TYR A 1 2170 ? 241.040 258.380 200.310 1.00 47.11  ? 2170 TYR A O     1 
ATOM   5037  C  CB    . TYR A 1 2170 ? 239.142 257.275 198.123 1.00 42.97  ? 2170 TYR A CB    1 
ATOM   5038  C  CG    . TYR A 1 2170 ? 237.934 257.836 198.834 1.00 41.69  ? 2170 TYR A CG    1 
ATOM   5039  C  CD1   . TYR A 1 2170 ? 237.511 257.308 200.045 1.00 32.58  ? 2170 TYR A CD1   1 
ATOM   5040  C  CD2   . TYR A 1 2170 ? 237.229 258.908 198.303 1.00 38.21  ? 2170 TYR A CD2   1 
ATOM   5041  C  CE1   . TYR A 1 2170 ? 236.412 257.823 200.704 1.00 38.22  ? 2170 TYR A CE1   1 
ATOM   5042  C  CE2   . TYR A 1 2170 ? 236.131 259.431 198.955 1.00 37.94  ? 2170 TYR A CE2   1 
ATOM   5043  C  CZ    . TYR A 1 2170 ? 235.727 258.886 200.154 1.00 47.39  ? 2170 TYR A CZ    1 
ATOM   5044  O  OH    . TYR A 1 2170 ? 234.629 259.404 200.803 1.00 46.60  ? 2170 TYR A OH    1 
ATOM   5045  N  N     . HIS A 1 2171 ? 240.020 260.206 199.462 1.00 50.42  ? 2171 HIS A N     1 
ATOM   5046  C  CA    . HIS A 1 2171 ? 240.008 260.963 200.704 1.00 48.21  ? 2171 HIS A CA    1 
ATOM   5047  C  C     . HIS A 1 2171 ? 238.564 261.235 201.096 1.00 44.11  ? 2171 HIS A C     1 
ATOM   5048  O  O     . HIS A 1 2171 ? 237.796 261.789 200.303 1.00 44.20  ? 2171 HIS A O     1 
ATOM   5049  C  CB    . HIS A 1 2171 ? 240.786 262.271 200.555 1.00 50.12  ? 2171 HIS A CB    1 
ATOM   5050  C  CG    . HIS A 1 2171 ? 242.030 262.140 199.734 1.00 59.27  ? 2171 HIS A CG    1 
ATOM   5051  N  ND1   . HIS A 1 2171 ? 243.248 261.795 200.278 1.00 61.56  ? 2171 HIS A ND1   1 
ATOM   5052  C  CD2   . HIS A 1 2171 ? 242.243 262.302 198.406 1.00 57.38  ? 2171 HIS A CD2   1 
ATOM   5053  C  CE1   . HIS A 1 2171 ? 244.159 261.752 199.322 1.00 61.98  ? 2171 HIS A CE1   1 
ATOM   5054  N  NE2   . HIS A 1 2171 ? 243.575 262.056 198.177 1.00 58.89  ? 2171 HIS A NE2   1 
ATOM   5055  N  N     . ARG A 1 2172 ? 238.198 260.839 202.311 1.00 42.28  ? 2172 ARG A N     1 
ATOM   5056  C  CA    . ARG A 1 2172 ? 236.827 261.004 202.771 1.00 40.58  ? 2172 ARG A CA    1 
ATOM   5057  C  C     . ARG A 1 2172 ? 236.456 262.479 202.844 1.00 43.47  ? 2172 ARG A C     1 
ATOM   5058  O  O     . ARG A 1 2172 ? 237.226 263.308 203.339 1.00 52.99  ? 2172 ARG A O     1 
ATOM   5059  C  CB    . ARG A 1 2172 ? 236.642 260.347 204.137 1.00 51.76  ? 2172 ARG A CB    1 
ATOM   5060  C  CG    . ARG A 1 2172 ? 236.735 258.831 204.111 1.00 64.23  ? 2172 ARG A CG    1 
ATOM   5061  C  CD    . ARG A 1 2172 ? 236.470 258.248 205.487 1.00 69.83  ? 2172 ARG A CD    1 
ATOM   5062  N  NE    . ARG A 1 2172 ? 237.546 258.563 206.416 1.00 81.83  ? 2172 ARG A NE    1 
ATOM   5063  C  CZ    . ARG A 1 2172 ? 237.418 259.361 207.468 1.00 73.68  ? 2172 ARG A CZ    1 
ATOM   5064  N  NH1   . ARG A 1 2172 ? 236.270 259.954 207.749 1.00 66.44  ? 2172 ARG A NH1   1 
ATOM   5065  N  NH2   . ARG A 1 2172 ? 238.470 259.570 208.255 1.00 57.84  ? 2172 ARG A NH2   1 
ATOM   5066  N  N     . GLY A 1 2173 ? 235.269 262.801 202.341 1.00 45.97  ? 2173 GLY A N     1 
ATOM   5067  C  CA    . GLY A 1 2173 ? 234.796 264.171 202.401 1.00 44.04  ? 2173 GLY A CA    1 
ATOM   5068  C  C     . GLY A 1 2173 ? 234.555 264.607 203.835 1.00 42.89  ? 2173 GLY A C     1 
ATOM   5069  O  O     . GLY A 1 2173 ? 234.219 263.802 204.705 1.00 43.05  ? 2173 GLY A O     1 
ATOM   5070  N  N     . GLU A 1 2174 ? 234.750 265.898 204.083 1.00 46.58  ? 2174 GLU A N     1 
ATOM   5071  C  CA    . GLU A 1 2174 ? 234.531 266.477 205.403 1.00 52.38  ? 2174 GLU A CA    1 
ATOM   5072  C  C     . GLU A 1 2174 ? 233.071 266.898 205.510 1.00 51.04  ? 2174 GLU A C     1 
ATOM   5073  O  O     . GLU A 1 2174 ? 232.678 267.942 204.977 1.00 60.37  ? 2174 GLU A O     1 
ATOM   5074  C  CB    . GLU A 1 2174 ? 235.471 267.657 205.633 1.00 52.90  ? 2174 GLU A CB    1 
ATOM   5075  C  CG    . GLU A 1 2174 ? 236.927 267.257 205.813 1.00 68.71  ? 2174 GLU A CG    1 
ATOM   5076  C  CD    . GLU A 1 2174 ? 237.872 268.440 205.744 1.00 83.29  ? 2174 GLU A CD    1 
ATOM   5077  O  OE1   . GLU A 1 2174 ? 237.402 269.566 205.478 1.00 76.42  ? 2174 GLU A OE1   1 
ATOM   5078  O  OE2   . GLU A 1 2174 ? 239.088 268.244 205.951 1.00 84.52  ? 2174 GLU A OE2   1 
ATOM   5079  N  N     . MET A 1 2175 ? 232.264 266.087 206.194 1.00 35.68  ? 2175 MET A N     1 
ATOM   5080  C  CA    . MET A 1 2175 ? 230.850 266.400 206.404 1.00 39.02  ? 2175 MET A CA    1 
ATOM   5081  C  C     . MET A 1 2175 ? 230.736 267.501 207.458 1.00 33.97  ? 2175 MET A C     1 
ATOM   5082  O  O     . MET A 1 2175 ? 230.361 267.277 208.612 1.00 42.26  ? 2175 MET A O     1 
ATOM   5083  C  CB    . MET A 1 2175 ? 230.071 265.157 206.813 1.00 41.24  ? 2175 MET A CB    1 
ATOM   5084  C  CG    . MET A 1 2175 ? 229.760 264.196 205.677 1.00 40.61  ? 2175 MET A CG    1 
ATOM   5085  S  SD    . MET A 1 2175 ? 231.195 263.273 205.110 1.00 74.21  ? 2175 MET A SD    1 
ATOM   5086  C  CE    . MET A 1 2175 ? 231.397 262.111 206.456 1.00 35.67  ? 2175 MET A CE    1 
ATOM   5087  N  N     . THR A 1 2176 ? 231.071 268.721 207.033 1.00 30.16  ? 2176 THR A N     1 
ATOM   5088  C  CA    . THR A 1 2176 ? 231.074 269.852 207.954 1.00 24.64  ? 2176 THR A CA    1 
ATOM   5089  C  C     . THR A 1 2176 ? 229.681 270.120 208.507 1.00 23.02  ? 2176 THR A C     1 
ATOM   5090  O  O     . THR A 1 2176 ? 229.491 270.161 209.729 1.00 26.90  ? 2176 THR A O     1 
ATOM   5091  C  CB    . THR A 1 2176 ? 231.621 271.097 207.256 1.00 29.97  ? 2176 THR A CB    1 
ATOM   5092  O  OG1   . THR A 1 2176 ? 231.042 271.208 205.951 1.00 34.13  ? 2176 THR A OG1   1 
ATOM   5093  C  CG2   . THR A 1 2176 ? 233.131 271.011 207.124 1.00 31.46  ? 2176 THR A CG2   1 
ATOM   5094  N  N     . ALA A 1 2177 ? 228.685 270.239 207.622 1.00 25.18  ? 2177 ALA A N     1 
ATOM   5095  C  CA    . ALA A 1 2177 ? 227.343 270.636 208.042 1.00 17.66  ? 2177 ALA A CA    1 
ATOM   5096  C  C     . ALA A 1 2177 ? 226.826 269.750 209.167 1.00 21.17  ? 2177 ALA A C     1 
ATOM   5097  O  O     . ALA A 1 2177 ? 226.111 270.221 210.059 1.00 23.22  ? 2177 ALA A O     1 
ATOM   5098  C  CB    . ALA A 1 2177 ? 226.390 270.599 206.849 1.00 16.81  ? 2177 ALA A CB    1 
ATOM   5099  N  N     . LEU A 1 2178 ? 227.177 268.465 209.144 1.00 20.06  ? 2178 LEU A N     1 
ATOM   5100  C  CA    . LEU A 1 2178 ? 226.900 267.607 210.286 1.00 16.85  ? 2178 LEU A CA    1 
ATOM   5101  C  C     . LEU A 1 2178 ? 227.891 267.841 211.420 1.00 18.17  ? 2178 LEU A C     1 
ATOM   5102  O  O     . LEU A 1 2178 ? 227.561 267.592 212.584 1.00 20.73  ? 2178 LEU A O     1 
ATOM   5103  C  CB    . LEU A 1 2178 ? 226.922 266.139 209.856 1.00 16.93  ? 2178 LEU A CB    1 
ATOM   5104  C  CG    . LEU A 1 2178 ? 226.522 265.097 210.903 1.00 10.36  ? 2178 LEU A CG    1 
ATOM   5105  C  CD1   . LEU A 1 2178 ? 225.064 265.265 211.290 1.00 10.87  ? 2178 LEU A CD1   1 
ATOM   5106  C  CD2   . LEU A 1 2178 ? 226.782 263.694 210.392 1.00 6.58   ? 2178 LEU A CD2   1 
ATOM   5107  N  N     . ARG A 1 2179 ? 229.095 268.328 211.109 1.00 20.11  ? 2179 ARG A N     1 
ATOM   5108  C  CA    . ARG A 1 2179 ? 230.123 268.465 212.139 1.00 17.15  ? 2179 ARG A CA    1 
ATOM   5109  C  C     . ARG A 1 2179 ? 229.808 269.597 213.113 1.00 19.01  ? 2179 ARG A C     1 
ATOM   5110  O  O     . ARG A 1 2179 ? 230.038 269.452 214.318 1.00 20.13  ? 2179 ARG A O     1 
ATOM   5111  C  CB    . ARG A 1 2179 ? 231.499 268.663 211.501 1.00 22.56  ? 2179 ARG A CB    1 
ATOM   5112  C  CG    . ARG A 1 2179 ? 232.227 267.366 211.184 1.00 13.87  ? 2179 ARG A CG    1 
ATOM   5113  C  CD    . ARG A 1 2179 ? 233.662 267.634 210.768 1.00 19.32  ? 2179 ARG A CD    1 
ATOM   5114  N  NE    . ARG A 1 2179 ? 234.311 266.454 210.210 1.00 24.35  ? 2179 ARG A NE    1 
ATOM   5115  C  CZ    . ARG A 1 2179 ? 234.999 265.570 210.920 1.00 25.52  ? 2179 ARG A CZ    1 
ATOM   5116  N  NH1   . ARG A 1 2179 ? 235.138 265.693 212.231 1.00 21.84  ? 2179 ARG A NH1   1 
ATOM   5117  N  NH2   . ARG A 1 2179 ? 235.565 264.539 210.300 1.00 21.23  ? 2179 ARG A NH2   1 
ATOM   5118  N  N     . GLU A 1 2180 ? 229.291 270.733 212.629 1.00 19.52  ? 2180 GLU A N     1 
ATOM   5119  C  CA    . GLU A 1 2180 ? 228.899 271.774 213.585 1.00 24.62  ? 2180 GLU A CA    1 
ATOM   5120  C  C     . GLU A 1 2180 ? 227.736 271.314 214.457 1.00 21.47  ? 2180 GLU A C     1 
ATOM   5121  O  O     . GLU A 1 2180 ? 227.673 271.651 215.647 1.00 23.15  ? 2180 GLU A O     1 
ATOM   5122  C  CB    . GLU A 1 2180 ? 228.545 273.107 212.912 1.00 28.49  ? 2180 GLU A CB    1 
ATOM   5123  C  CG    . GLU A 1 2180 ? 229.694 273.856 212.245 1.00 25.52  ? 2180 GLU A CG    1 
ATOM   5124  C  CD    . GLU A 1 2180 ? 229.975 273.388 210.849 1.00 35.18  ? 2180 GLU A CD    1 
ATOM   5125  O  OE1   . GLU A 1 2180 ? 229.219 272.533 210.370 1.00 39.55  ? 2180 GLU A OE1   1 
ATOM   5126  O  OE2   . GLU A 1 2180 ? 230.947 273.871 210.232 1.00 45.74  ? 2180 GLU A OE2   1 
ATOM   5127  N  N     . GLU A 1 2181 ? 226.797 270.559 213.884 1.00 21.11  ? 2181 GLU A N     1 
ATOM   5128  C  CA    . GLU A 1 2181 ? 225.701 270.026 214.686 1.00 19.52  ? 2181 GLU A CA    1 
ATOM   5129  C  C     . GLU A 1 2181 ? 226.216 269.062 215.748 1.00 15.17  ? 2181 GLU A C     1 
ATOM   5130  O  O     . GLU A 1 2181 ? 225.754 269.083 216.896 1.00 17.04  ? 2181 GLU A O     1 
ATOM   5131  C  CB    . GLU A 1 2181 ? 224.675 269.342 213.785 1.00 17.02  ? 2181 GLU A CB    1 
ATOM   5132  C  CG    . GLU A 1 2181 ? 223.674 270.293 213.141 1.00 21.31  ? 2181 GLU A CG    1 
ATOM   5133  C  CD    . GLU A 1 2181 ? 223.189 271.380 214.086 1.00 35.74  ? 2181 GLU A CD    1 
ATOM   5134  O  OE1   . GLU A 1 2181 ? 223.114 272.550 213.655 1.00 36.88  ? 2181 GLU A OE1   1 
ATOM   5135  O  OE2   . GLU A 1 2181 ? 222.859 271.067 215.250 1.00 39.59  ? 2181 GLU A OE2   1 
ATOM   5136  N  N     . LEU A 1 2182 ? 227.178 268.213 215.380 1.00 16.05  ? 2182 LEU A N     1 
ATOM   5137  C  CA    . LEU A 1 2182 ? 227.804 267.328 216.355 1.00 13.84  ? 2182 LEU A CA    1 
ATOM   5138  C  C     . LEU A 1 2182 ? 228.505 268.127 217.445 1.00 14.19  ? 2182 LEU A C     1 
ATOM   5139  O  O     . LEU A 1 2182 ? 228.438 267.770 218.625 1.00 20.01  ? 2182 LEU A O     1 
ATOM   5140  C  CB    . LEU A 1 2182 ? 228.791 266.389 215.660 1.00 10.39  ? 2182 LEU A CB    1 
ATOM   5141  C  CG    . LEU A 1 2182 ? 228.217 265.303 214.747 1.00 8.84   ? 2182 LEU A CG    1 
ATOM   5142  C  CD1   . LEU A 1 2182 ? 229.328 264.460 214.146 1.00 7.04   ? 2182 LEU A CD1   1 
ATOM   5143  C  CD2   . LEU A 1 2182 ? 227.241 264.428 215.505 1.00 8.25   ? 2182 LEU A CD2   1 
ATOM   5144  N  N     . LYS A 1 2183 ? 229.182 269.213 217.065 1.00 14.37  ? 2183 LYS A N     1 
ATOM   5145  C  CA    . LYS A 1 2183 ? 229.831 270.079 218.044 1.00 13.05  ? 2183 LYS A CA    1 
ATOM   5146  C  C     . LYS A 1 2183 ? 228.820 270.637 219.037 1.00 16.08  ? 2183 LYS A C     1 
ATOM   5147  O  O     . LYS A 1 2183 ? 229.039 270.605 220.253 1.00 22.08  ? 2183 LYS A O     1 
ATOM   5148  C  CB    . LYS A 1 2183 ? 230.550 271.223 217.331 1.00 16.21  ? 2183 LYS A CB    1 
ATOM   5149  C  CG    . LYS A 1 2183 ? 231.980 270.931 216.949 1.00 19.22  ? 2183 LYS A CG    1 
ATOM   5150  C  CD    . LYS A 1 2183 ? 232.773 272.210 216.754 1.00 23.96  ? 2183 LYS A CD    1 
ATOM   5151  C  CE    . LYS A 1 2183 ? 233.017 272.913 218.077 1.00 20.83  ? 2183 LYS A CE    1 
ATOM   5152  N  NZ    . LYS A 1 2183 ? 233.846 272.083 218.991 1.00 25.20  ? 2183 LYS A NZ    1 
ATOM   5153  N  N     . LYS A 1 2184 ? 227.707 271.167 218.527 1.00 16.15  ? 2184 LYS A N     1 
ATOM   5154  C  CA    . LYS A 1 2184 ? 226.704 271.764 219.401 1.00 15.80  ? 2184 LYS A CA    1 
ATOM   5155  C  C     . LYS A 1 2184 ? 226.086 270.723 220.326 1.00 14.81  ? 2184 LYS A C     1 
ATOM   5156  O  O     . LYS A 1 2184 ? 225.885 270.982 221.519 1.00 21.65  ? 2184 LYS A O     1 
ATOM   5157  C  CB    . LYS A 1 2184 ? 225.624 272.451 218.567 1.00 20.30  ? 2184 LYS A CB    1 
ATOM   5158  C  CG    . LYS A 1 2184 ? 226.106 273.690 217.835 1.00 22.35  ? 2184 LYS A CG    1 
ATOM   5159  C  CD    . LYS A 1 2184 ? 225.007 274.281 216.974 1.00 36.66  ? 2184 LYS A CD    1 
ATOM   5160  C  CE    . LYS A 1 2184 ? 223.920 274.912 217.828 1.00 46.22  ? 2184 LYS A CE    1 
ATOM   5161  N  NZ    . LYS A 1 2184 ? 224.408 276.121 218.545 1.00 44.76  ? 2184 LYS A NZ    1 
ATOM   5162  N  N     . VAL A 1 2185 ? 225.782 269.536 219.796 1.00 13.05  ? 2185 VAL A N     1 
ATOM   5163  C  CA    . VAL A 1 2185 ? 225.196 268.488 220.624 1.00 14.07  ? 2185 VAL A CA    1 
ATOM   5164  C  C     . VAL A 1 2185 ? 226.183 268.033 221.693 1.00 14.97  ? 2185 VAL A C     1 
ATOM   5165  O  O     . VAL A 1 2185 ? 225.805 267.812 222.850 1.00 16.30  ? 2185 VAL A O     1 
ATOM   5166  C  CB    . VAL A 1 2185 ? 224.718 267.318 219.746 1.00 14.62  ? 2185 VAL A CB    1 
ATOM   5167  C  CG1   . VAL A 1 2185 ? 224.309 266.132 220.605 1.00 10.79  ? 2185 VAL A CG1   1 
ATOM   5168  C  CG2   . VAL A 1 2185 ? 223.558 267.760 218.871 1.00 15.59  ? 2185 VAL A CG2   1 
ATOM   5169  N  N     . CYS A 1 2186 ? 227.461 267.892 221.333 1.00 12.08  ? 2186 CYS A N     1 
ATOM   5170  C  CA    . CYS A 1 2186 ? 228.466 267.486 222.308 1.00 10.26  ? 2186 CYS A CA    1 
ATOM   5171  C  C     . CYS A 1 2186 ? 228.636 268.533 223.400 1.00 16.55  ? 2186 CYS A C     1 
ATOM   5172  O  O     . CYS A 1 2186 ? 228.786 268.190 224.579 1.00 19.25  ? 2186 CYS A O     1 
ATOM   5173  C  CB    . CYS A 1 2186 ? 229.799 267.216 221.610 1.00 11.27  ? 2186 CYS A CB    1 
ATOM   5174  S  SG    . CYS A 1 2186 ? 229.842 265.689 220.649 1.00 21.38  ? 2186 CYS A SG    1 
ATOM   5175  N  N     . GLN A 1 2187 ? 228.624 269.817 223.030 1.00 17.08  ? 2187 GLN A N     1 
ATOM   5176  C  CA    . GLN A 1 2187 ? 228.678 270.868 224.042 1.00 18.30  ? 2187 GLN A CA    1 
ATOM   5177  C  C     . GLN A 1 2187 ? 227.463 270.810 224.956 1.00 18.54  ? 2187 GLN A C     1 
ATOM   5178  O  O     . GLN A 1 2187 ? 227.586 270.970 226.176 1.00 24.52  ? 2187 GLN A O     1 
ATOM   5179  C  CB    . GLN A 1 2187 ? 228.782 272.243 223.381 1.00 25.40  ? 2187 GLN A CB    1 
ATOM   5180  C  CG    . GLN A 1 2187 ? 230.052 272.470 222.582 1.00 34.55  ? 2187 GLN A CG    1 
ATOM   5181  C  CD    . GLN A 1 2187 ? 231.293 272.493 223.452 1.00 45.74  ? 2187 GLN A CD    1 
ATOM   5182  O  OE1   . GLN A 1 2187 ? 231.276 273.026 224.562 1.00 40.34  ? 2187 GLN A OE1   1 
ATOM   5183  N  NE2   . GLN A 1 2187 ? 232.377 271.915 222.952 1.00 49.07  ? 2187 GLN A NE2   1 
ATOM   5184  N  N     . GLU A 1 2188 ? 226.280 270.573 224.389 1.00 15.73  ? 2188 GLU A N     1 
ATOM   5185  C  CA    . GLU A 1 2188 ? 225.073 270.500 225.200 1.00 18.05  ? 2188 GLU A CA    1 
ATOM   5186  C  C     . GLU A 1 2188 ? 224.991 269.220 226.024 1.00 15.95  ? 2188 GLU A C     1 
ATOM   5187  O  O     . GLU A 1 2188 ? 224.312 269.207 227.055 1.00 16.07  ? 2188 GLU A O     1 
ATOM   5188  C  CB    . GLU A 1 2188 ? 223.837 270.627 224.308 1.00 19.30  ? 2188 GLU A CB    1 
ATOM   5189  C  CG    . GLU A 1 2188 ? 222.639 271.251 225.000 1.00 31.90  ? 2188 GLU A CG    1 
ATOM   5190  C  CD    . GLU A 1 2188 ? 221.609 271.772 224.021 1.00 55.43  ? 2188 GLU A CD    1 
ATOM   5191  O  OE1   . GLU A 1 2188 ? 221.837 271.651 222.800 1.00 57.24  ? 2188 GLU A OE1   1 
ATOM   5192  O  OE2   . GLU A 1 2188 ? 220.573 272.308 224.470 1.00 51.72  ? 2188 GLU A OE2   1 
ATOM   5193  N  N     . MET A 1 2189 ? 225.670 268.154 225.603 1.00 17.08  ? 2189 MET A N     1 
ATOM   5194  C  CA    . MET A 1 2189 ? 225.652 266.880 226.312 1.00 10.93  ? 2189 MET A CA    1 
ATOM   5195  C  C     . MET A 1 2189 ? 226.923 266.634 227.117 1.00 10.09  ? 2189 MET A C     1 
ATOM   5196  O  O     . MET A 1 2189 ? 227.160 265.501 227.547 1.00 8.09   ? 2189 MET A O     1 
ATOM   5197  C  CB    . MET A 1 2189 ? 225.420 265.733 225.328 1.00 10.86  ? 2189 MET A CB    1 
ATOM   5198  C  CG    . MET A 1 2189 ? 223.955 265.458 225.037 1.00 11.26  ? 2189 MET A CG    1 
ATOM   5199  S  SD    . MET A 1 2189 ? 223.709 264.217 223.753 1.00 26.07  ? 2189 MET A SD    1 
ATOM   5200  C  CE    . MET A 1 2189 ? 223.983 262.709 224.675 1.00 7.73   ? 2189 MET A CE    1 
ATOM   5201  N  N     . TYR A 1 2190 ? 227.743 267.667 227.328 1.00 12.75  ? 2190 TYR A N     1 
ATOM   5202  C  CA    . TYR A 1 2190 ? 228.970 267.574 228.123 1.00 10.40  ? 2190 TYR A CA    1 
ATOM   5203  C  C     . TYR A 1 2190 ? 229.940 266.537 227.566 1.00 9.40   ? 2190 TYR A C     1 
ATOM   5204  O  O     . TYR A 1 2190 ? 230.639 265.857 228.319 1.00 9.06   ? 2190 TYR A O     1 
ATOM   5205  C  CB    . TYR A 1 2190 ? 228.660 267.274 229.594 1.00 9.73   ? 2190 TYR A CB    1 
ATOM   5206  C  CG    . TYR A 1 2190 ? 227.570 268.143 230.178 1.00 11.46  ? 2190 TYR A CG    1 
ATOM   5207  C  CD1   . TYR A 1 2190 ? 227.720 269.519 230.253 1.00 12.62  ? 2190 TYR A CD1   1 
ATOM   5208  C  CD2   . TYR A 1 2190 ? 226.387 267.586 230.640 1.00 10.00  ? 2190 TYR A CD2   1 
ATOM   5209  C  CE1   . TYR A 1 2190 ? 226.727 270.315 230.780 1.00 14.88  ? 2190 TYR A CE1   1 
ATOM   5210  C  CE2   . TYR A 1 2190 ? 225.388 268.375 231.168 1.00 14.96  ? 2190 TYR A CE2   1 
ATOM   5211  C  CZ    . TYR A 1 2190 ? 225.562 269.739 231.237 1.00 21.82  ? 2190 TYR A CZ    1 
ATOM   5212  O  OH    . TYR A 1 2190 ? 224.568 270.531 231.762 1.00 31.92  ? 2190 TYR A OH    1 
ATOM   5213  N  N     . LEU A 1 2191 ? 229.996 266.410 226.246 1.00 9.82   ? 2191 LEU A N     1 
ATOM   5214  C  CA    . LEU A 1 2191 ? 230.876 265.459 225.587 1.00 7.02   ? 2191 LEU A CA    1 
ATOM   5215  C  C     . LEU A 1 2191 ? 232.035 266.184 224.917 1.00 7.45   ? 2191 LEU A C     1 
ATOM   5216  O  O     . LEU A 1 2191 ? 231.986 267.391 224.666 1.00 11.58  ? 2191 LEU A O     1 
ATOM   5217  C  CB    . LEU A 1 2191 ? 230.109 264.622 224.558 1.00 6.67   ? 2191 LEU A CB    1 
ATOM   5218  C  CG    . LEU A 1 2191 ? 228.963 263.761 225.098 1.00 6.82   ? 2191 LEU A CG    1 
ATOM   5219  C  CD1   . LEU A 1 2191 ? 228.563 262.713 224.082 1.00 6.45   ? 2191 LEU A CD1   1 
ATOM   5220  C  CD2   . LEU A 1 2191 ? 229.344 263.104 226.414 1.00 6.01   ? 2191 LEU A CD2   1 
ATOM   5221  N  N     . THR A 1 2192 ? 233.087 265.424 224.630 1.00 7.11   ? 2192 THR A N     1 
ATOM   5222  C  CA    . THR A 1 2192 ? 234.310 265.950 224.039 1.00 7.77   ? 2192 THR A CA    1 
ATOM   5223  C  C     . THR A 1 2192 ? 234.273 265.730 222.533 1.00 9.59   ? 2192 THR A C     1 
ATOM   5224  O  O     . THR A 1 2192 ? 234.027 264.611 222.070 1.00 11.79  ? 2192 THR A O     1 
ATOM   5225  C  CB    . THR A 1 2192 ? 235.541 265.279 224.649 1.00 7.63   ? 2192 THR A CB    1 
ATOM   5226  O  OG1   . THR A 1 2192 ? 235.622 265.603 226.041 1.00 12.10  ? 2192 THR A OG1   1 
ATOM   5227  C  CG2   . THR A 1 2192 ? 236.806 265.747 223.952 1.00 8.43   ? 2192 THR A CG2   1 
ATOM   5228  N  N     . TYR A 1 2193 ? 234.513 266.795 221.774 1.00 13.81  ? 2193 TYR A N     1 
ATOM   5229  C  CA    . TYR A 1 2193 ? 234.523 266.747 220.321 1.00 10.49  ? 2193 TYR A CA    1 
ATOM   5230  C  C     . TYR A 1 2193 ? 235.929 267.024 219.804 1.00 12.62  ? 2193 TYR A C     1 
ATOM   5231  O  O     . TYR A 1 2193 ? 236.640 267.880 220.340 1.00 19.67  ? 2193 TYR A O     1 
ATOM   5232  C  CB    . TYR A 1 2193 ? 233.535 267.758 219.735 1.00 10.35  ? 2193 TYR A CB    1 
ATOM   5233  C  CG    . TYR A 1 2193 ? 233.523 267.798 218.225 1.00 15.62  ? 2193 TYR A CG    1 
ATOM   5234  C  CD1   . TYR A 1 2193 ? 234.416 268.596 217.525 1.00 17.92  ? 2193 TYR A CD1   1 
ATOM   5235  C  CD2   . TYR A 1 2193 ? 232.621 267.035 217.500 1.00 14.72  ? 2193 TYR A CD2   1 
ATOM   5236  C  CE1   . TYR A 1 2193 ? 234.412 268.632 216.152 1.00 18.11  ? 2193 TYR A CE1   1 
ATOM   5237  C  CE2   . TYR A 1 2193 ? 232.608 267.065 216.124 1.00 13.10  ? 2193 TYR A CE2   1 
ATOM   5238  C  CZ    . TYR A 1 2193 ? 233.508 267.866 215.455 1.00 17.95  ? 2193 TYR A CZ    1 
ATOM   5239  O  OH    . TYR A 1 2193 ? 233.504 267.904 214.082 1.00 32.25  ? 2193 TYR A OH    1 
ATOM   5240  N  N     . GLY A 1 2194 ? 236.319 266.307 218.762 1.00 12.72  ? 2194 GLY A N     1 
ATOM   5241  C  CA    . GLY A 1 2194 ? 237.621 266.510 218.151 1.00 15.37  ? 2194 GLY A CA    1 
ATOM   5242  C  C     . GLY A 1 2194 ? 237.573 266.199 216.675 1.00 18.02  ? 2194 GLY A C     1 
ATOM   5243  O  O     . GLY A 1 2194 ? 236.728 265.427 216.212 1.00 22.24  ? 2194 GLY A O     1 
ATOM   5244  N  N     . ASP A 1 2195 ? 238.484 266.813 215.926 1.00 26.13  ? 2195 ASP A N     1 
ATOM   5245  C  CA    . ASP A 1 2195 ? 238.613 266.588 214.492 1.00 24.18  ? 2195 ASP A CA    1 
ATOM   5246  C  C     . ASP A 1 2195 ? 239.951 265.920 214.208 1.00 25.84  ? 2195 ASP A C     1 
ATOM   5247  O  O     . ASP A 1 2195 ? 241.005 266.466 214.551 1.00 34.70  ? 2195 ASP A O     1 
ATOM   5248  C  CB    . ASP A 1 2195 ? 238.489 267.899 213.719 1.00 27.55  ? 2195 ASP A CB    1 
ATOM   5249  C  CG    . ASP A 1 2195 ? 237.086 268.465 213.757 1.00 33.54  ? 2195 ASP A CG    1 
ATOM   5250  O  OD1   . ASP A 1 2195 ? 236.134 267.667 213.853 1.00 35.71  ? 2195 ASP A OD1   1 
ATOM   5251  O  OD2   . ASP A 1 2195 ? 236.936 269.703 213.701 1.00 36.48  ? 2195 ASP A OD2   1 
ATOM   5252  N  N     . GLY A 1 2196 ? 239.904 264.755 213.566 1.00 25.70  ? 2196 GLY A N     1 
ATOM   5253  C  CA    . GLY A 1 2196 ? 241.117 264.054 213.197 1.00 26.61  ? 2196 GLY A CA    1 
ATOM   5254  C  C     . GLY A 1 2196 ? 241.901 263.505 214.370 1.00 28.29  ? 2196 GLY A C     1 
ATOM   5255  O  O     . GLY A 1 2196 ? 241.478 262.537 215.011 1.00 28.67  ? 2196 GLY A O     1 
ATOM   5256  N  N     . GLU A 1 2197 ? 243.051 264.113 214.655 1.00 30.46  ? 2197 GLU A N     1 
ATOM   5257  C  CA    . GLU A 1 2197 ? 243.981 263.611 215.656 1.00 26.74  ? 2197 GLU A CA    1 
ATOM   5258  C  C     . GLU A 1 2197 ? 243.857 264.304 217.007 1.00 26.46  ? 2197 GLU A C     1 
ATOM   5259  O  O     . GLU A 1 2197 ? 244.670 264.035 217.897 1.00 31.60  ? 2197 GLU A O     1 
ATOM   5260  C  CB    . GLU A 1 2197 ? 245.420 263.741 215.146 1.00 31.17  ? 2197 GLU A CB    1 
ATOM   5261  C  CG    . GLU A 1 2197 ? 245.730 262.858 213.951 1.00 39.37  ? 2197 GLU A CG    1 
ATOM   5262  C  CD    . GLU A 1 2197 ? 245.690 261.386 214.294 1.00 51.42  ? 2197 GLU A CD    1 
ATOM   5263  O  OE1   . GLU A 1 2197 ? 246.020 261.035 215.446 1.00 51.00  ? 2197 GLU A OE1   1 
ATOM   5264  O  OE2   . GLU A 1 2197 ? 245.325 260.576 213.415 1.00 54.40  ? 2197 GLU A OE2   1 
ATOM   5265  N  N     . GLU A 1 2198 ? 242.876 265.186 217.190 1.00 27.29  ? 2198 GLU A N     1 
ATOM   5266  C  CA    . GLU A 1 2198 ? 242.664 265.791 218.496 1.00 25.35  ? 2198 GLU A CA    1 
ATOM   5267  C  C     . GLU A 1 2198 ? 242.017 264.781 219.445 1.00 22.01  ? 2198 GLU A C     1 
ATOM   5268  O  O     . GLU A 1 2198 ? 241.722 263.639 219.083 1.00 19.35  ? 2198 GLU A O     1 
ATOM   5269  C  CB    . GLU A 1 2198 ? 241.803 267.047 218.385 1.00 21.91  ? 2198 GLU A CB    1 
ATOM   5270  C  CG    . GLU A 1 2198 ? 241.986 267.834 217.106 1.00 26.62  ? 2198 GLU A CG    1 
ATOM   5271  C  CD    . GLU A 1 2198 ? 241.154 269.101 217.081 1.00 37.32  ? 2198 GLU A CD    1 
ATOM   5272  O  OE1   . GLU A 1 2198 ? 240.013 269.074 217.589 1.00 31.32  ? 2198 GLU A OE1   1 
ATOM   5273  O  OE2   . GLU A 1 2198 ? 241.635 270.122 216.548 1.00 54.50  ? 2198 GLU A OE2   1 
ATOM   5274  N  N     . VAL A 1 2199 ? 241.797 265.217 220.685 1.00 16.85  ? 2199 VAL A N     1 
ATOM   5275  C  CA    . VAL A 1 2199 ? 241.133 264.372 221.669 1.00 13.86  ? 2199 VAL A CA    1 
ATOM   5276  C  C     . VAL A 1 2199 ? 239.668 264.222 221.289 1.00 15.09  ? 2199 VAL A C     1 
ATOM   5277  O  O     . VAL A 1 2199 ? 238.949 265.213 221.103 1.00 14.92  ? 2199 VAL A O     1 
ATOM   5278  C  CB    . VAL A 1 2199 ? 241.290 264.960 223.077 1.00 18.50  ? 2199 VAL A CB    1 
ATOM   5279  C  CG1   . VAL A 1 2199 ? 240.544 264.110 224.093 1.00 17.50  ? 2199 VAL A CG1   1 
ATOM   5280  C  CG2   . VAL A 1 2199 ? 242.761 265.069 223.445 1.00 18.73  ? 2199 VAL A CG2   1 
ATOM   5281  N  N     . GLY A 1 2200 ? 239.216 262.977 221.173 1.00 14.98  ? 2200 GLY A N     1 
ATOM   5282  C  CA    . GLY A 1 2200 ? 237.865 262.697 220.738 1.00 10.00  ? 2200 GLY A CA    1 
ATOM   5283  C  C     . GLY A 1 2200 ? 237.670 262.641 219.242 1.00 10.57  ? 2200 GLY A C     1 
ATOM   5284  O  O     . GLY A 1 2200 ? 236.530 262.484 218.790 1.00 14.05  ? 2200 GLY A O     1 
ATOM   5285  N  N     . GLY A 1 2201 ? 238.741 262.767 218.457 1.00 11.21  ? 2201 GLY A N     1 
ATOM   5286  C  CA    . GLY A 1 2201 ? 238.597 262.715 217.012 1.00 12.36  ? 2201 GLY A CA    1 
ATOM   5287  C  C     . GLY A 1 2201 ? 238.159 261.354 216.510 1.00 9.60   ? 2201 GLY A C     1 
ATOM   5288  O  O     . GLY A 1 2201 ? 237.338 261.256 215.593 1.00 9.85   ? 2201 GLY A O     1 
ATOM   5289  N  N     . MET A 1 2202 ? 238.703 260.285 217.096 1.00 10.19  ? 2202 MET A N     1 
ATOM   5290  C  CA    . MET A 1 2202 ? 238.312 258.937 216.698 1.00 6.59   ? 2202 MET A CA    1 
ATOM   5291  C  C     . MET A 1 2202 ? 236.838 258.685 216.987 1.00 7.50   ? 2202 MET A C     1 
ATOM   5292  O  O     . MET A 1 2202 ? 236.152 258.005 216.215 1.00 10.39  ? 2202 MET A O     1 
ATOM   5293  C  CB    . MET A 1 2202 ? 239.185 257.908 217.414 1.00 7.62   ? 2202 MET A CB    1 
ATOM   5294  C  CG    . MET A 1 2202 ? 240.645 257.939 216.996 1.00 11.77  ? 2202 MET A CG    1 
ATOM   5295  S  SD    . MET A 1 2202 ? 241.657 256.771 217.922 1.00 47.14  ? 2202 MET A SD    1 
ATOM   5296  C  CE    . MET A 1 2202 ? 241.072 255.215 217.257 1.00 31.85  ? 2202 MET A CE    1 
ATOM   5297  N  N     . TRP A 1 2203 ? 236.334 259.224 218.098 1.00 7.09   ? 2203 TRP A N     1 
ATOM   5298  C  CA    . TRP A 1 2203 ? 234.916 259.090 218.412 1.00 5.52   ? 2203 TRP A CA    1 
ATOM   5299  C  C     . TRP A 1 2203 ? 234.048 259.773 217.361 1.00 5.05   ? 2203 TRP A C     1 
ATOM   5300  O  O     . TRP A 1 2203 ? 233.023 259.226 216.939 1.00 6.87   ? 2203 TRP A O     1 
ATOM   5301  C  CB    . TRP A 1 2203 ? 234.640 259.661 219.801 1.00 6.30   ? 2203 TRP A CB    1 
ATOM   5302  C  CG    . TRP A 1 2203 ? 233.250 259.432 220.281 1.00 3.36   ? 2203 TRP A CG    1 
ATOM   5303  C  CD1   . TRP A 1 2203 ? 232.729 258.268 220.758 1.00 2.05   ? 2203 TRP A CD1   1 
ATOM   5304  C  CD2   . TRP A 1 2203 ? 232.197 260.397 220.335 1.00 3.53   ? 2203 TRP A CD2   1 
ATOM   5305  N  NE1   . TRP A 1 2203 ? 231.414 258.447 221.105 1.00 2.15   ? 2203 TRP A NE1   1 
ATOM   5306  C  CE2   . TRP A 1 2203 ? 231.063 259.747 220.855 1.00 3.19   ? 2203 TRP A CE2   1 
ATOM   5307  C  CE3   . TRP A 1 2203 ? 232.102 261.748 219.995 1.00 4.74   ? 2203 TRP A CE3   1 
ATOM   5308  C  CZ2   . TRP A 1 2203 ? 229.850 260.401 221.043 1.00 3.53   ? 2203 TRP A CZ2   1 
ATOM   5309  C  CZ3   . TRP A 1 2203 ? 230.898 262.394 220.180 1.00 5.49   ? 2203 TRP A CZ3   1 
ATOM   5310  C  CH2   . TRP A 1 2203 ? 229.788 261.721 220.698 1.00 3.97   ? 2203 TRP A CH2   1 
ATOM   5311  N  N     . VAL A 1 2204 ? 234.444 260.968 216.921 1.00 6.08   ? 2204 VAL A N     1 
ATOM   5312  C  CA    . VAL A 1 2204 ? 233.680 261.666 215.892 1.00 6.00   ? 2204 VAL A CA    1 
ATOM   5313  C  C     . VAL A 1 2204 ? 233.766 260.921 214.566 1.00 5.85   ? 2204 VAL A C     1 
ATOM   5314  O  O     . VAL A 1 2204 ? 232.794 260.870 213.801 1.00 7.35   ? 2204 VAL A O     1 
ATOM   5315  C  CB    . VAL A 1 2204 ? 234.162 263.122 215.764 1.00 7.86   ? 2204 VAL A CB    1 
ATOM   5316  C  CG1   . VAL A 1 2204 ? 233.360 263.858 214.705 1.00 12.30  ? 2204 VAL A CG1   1 
ATOM   5317  C  CG2   . VAL A 1 2204 ? 234.053 263.826 217.104 1.00 7.15   ? 2204 VAL A CG2   1 
ATOM   5318  N  N     . GLU A 1 2205 ? 234.928 260.333 214.269 1.00 6.93   ? 2205 GLU A N     1 
ATOM   5319  C  CA    . GLU A 1 2205 ? 235.050 259.505 213.073 1.00 7.08   ? 2205 GLU A CA    1 
ATOM   5320  C  C     . GLU A 1 2205 ? 234.094 258.322 213.133 1.00 6.82   ? 2205 GLU A C     1 
ATOM   5321  O  O     . GLU A 1 2205 ? 233.452 257.980 212.133 1.00 10.13  ? 2205 GLU A O     1 
ATOM   5322  C  CB    . GLU A 1 2205 ? 236.489 259.017 212.913 1.00 6.94   ? 2205 GLU A CB    1 
ATOM   5323  C  CG    . GLU A 1 2205 ? 237.501 260.112 212.632 1.00 18.20  ? 2205 GLU A CG    1 
ATOM   5324  C  CD    . GLU A 1 2205 ? 237.295 260.769 211.284 1.00 30.76  ? 2205 GLU A CD    1 
ATOM   5325  O  OE1   . GLU A 1 2205 ? 236.836 260.079 210.350 1.00 41.21  ? 2205 GLU A OE1   1 
ATOM   5326  O  OE2   . GLU A 1 2205 ? 237.595 261.973 211.157 1.00 34.17  ? 2205 GLU A OE2   1 
ATOM   5327  N  N     . LYS A 1 2206 ? 233.988 257.688 214.301 1.00 5.12   ? 2206 LYS A N     1 
ATOM   5328  C  CA    . LYS A 1 2206 ? 233.054 256.579 214.463 1.00 3.99   ? 2206 LYS A CA    1 
ATOM   5329  C  C     . LYS A 1 2206 ? 231.612 257.047 214.304 1.00 4.56   ? 2206 LYS A C     1 
ATOM   5330  O  O     . LYS A 1 2206 ? 230.779 256.332 213.737 1.00 5.50   ? 2206 LYS A O     1 
ATOM   5331  C  CB    . LYS A 1 2206 ? 233.260 255.919 215.824 1.00 4.23   ? 2206 LYS A CB    1 
ATOM   5332  C  CG    . LYS A 1 2206 ? 234.464 254.998 215.886 1.00 4.51   ? 2206 LYS A CG    1 
ATOM   5333  C  CD    . LYS A 1 2206 ? 234.307 253.812 214.958 1.00 4.36   ? 2206 LYS A CD    1 
ATOM   5334  C  CE    . LYS A 1 2206 ? 235.650 253.365 214.412 1.00 4.26   ? 2206 LYS A CE    1 
ATOM   5335  N  NZ    . LYS A 1 2206 ? 235.521 252.183 213.520 1.00 4.76   ? 2206 LYS A NZ    1 
ATOM   5336  N  N     . VAL A 1 2207 ? 231.296 258.241 214.810 1.00 5.11   ? 2207 VAL A N     1 
ATOM   5337  C  CA    . VAL A 1 2207 ? 229.947 258.784 214.651 1.00 5.46   ? 2207 VAL A CA    1 
ATOM   5338  C  C     . VAL A 1 2207 ? 229.628 259.008 213.177 1.00 6.45   ? 2207 VAL A C     1 
ATOM   5339  O  O     . VAL A 1 2207 ? 228.527 258.692 212.707 1.00 9.62   ? 2207 VAL A O     1 
ATOM   5340  C  CB    . VAL A 1 2207 ? 229.793 260.081 215.468 1.00 5.41   ? 2207 VAL A CB    1 
ATOM   5341  C  CG1   . VAL A 1 2207 ? 228.478 260.765 215.139 1.00 5.87   ? 2207 VAL A CG1   1 
ATOM   5342  C  CG2   . VAL A 1 2207 ? 229.878 259.788 216.954 1.00 3.65   ? 2207 VAL A CG2   1 
ATOM   5343  N  N     . LEU A 1 2208 ? 230.582 259.561 212.427 1.00 5.09   ? 2208 LEU A N     1 
ATOM   5344  C  CA    . LEU A 1 2208 ? 230.372 259.775 210.997 1.00 4.12   ? 2208 LEU A CA    1 
ATOM   5345  C  C     . LEU A 1 2208 ? 230.236 258.452 210.249 1.00 4.23   ? 2208 LEU A C     1 
ATOM   5346  O  O     . LEU A 1 2208 ? 229.423 258.335 209.323 1.00 6.24   ? 2208 LEU A O     1 
ATOM   5347  C  CB    . LEU A 1 2208 ? 231.516 260.608 210.422 1.00 5.38   ? 2208 LEU A CB    1 
ATOM   5348  C  CG    . LEU A 1 2208 ? 231.631 262.030 210.971 1.00 5.81   ? 2208 LEU A CG    1 
ATOM   5349  C  CD1   . LEU A 1 2208 ? 232.780 262.759 210.314 1.00 10.21  ? 2208 LEU A CD1   1 
ATOM   5350  C  CD2   . LEU A 1 2208 ? 230.333 262.785 210.762 1.00 5.05   ? 2208 LEU A CD2   1 
ATOM   5351  N  N     . GLN A 1 2209 ? 231.023 257.447 210.635 1.00 4.89   ? 2209 GLN A N     1 
ATOM   5352  C  CA    . GLN A 1 2209 ? 230.877 256.122 210.040 1.00 5.41   ? 2209 GLN A CA    1 
ATOM   5353  C  C     . GLN A 1 2209 ? 229.497 255.544 210.326 1.00 5.58   ? 2209 GLN A C     1 
ATOM   5354  O  O     . GLN A 1 2209 ? 228.878 254.929 209.450 1.00 7.32   ? 2209 GLN A O     1 
ATOM   5355  C  CB    . GLN A 1 2209 ? 231.964 255.187 210.563 1.00 3.01   ? 2209 GLN A CB    1 
ATOM   5356  C  CG    . GLN A 1 2209 ? 233.360 255.528 210.090 1.00 3.55   ? 2209 GLN A CG    1 
ATOM   5357  C  CD    . GLN A 1 2209 ? 234.417 254.695 210.777 1.00 3.49   ? 2209 GLN A CD    1 
ATOM   5358  O  OE1   . GLN A 1 2209 ? 234.106 253.849 211.612 1.00 6.14   ? 2209 GLN A OE1   1 
ATOM   5359  N  NE2   . GLN A 1 2209 ? 235.675 254.928 210.430 1.00 3.25   ? 2209 GLN A NE2   1 
ATOM   5360  N  N     . LEU A 1 2210 ? 229.006 255.727 211.552 1.00 4.68   ? 2210 LEU A N     1 
ATOM   5361  C  CA    . LEU A 1 2210 ? 227.668 255.262 211.898 1.00 4.81   ? 2210 LEU A CA    1 
ATOM   5362  C  C     . LEU A 1 2210 ? 226.612 255.976 211.067 1.00 5.07   ? 2210 LEU A C     1 
ATOM   5363  O  O     . LEU A 1 2210 ? 225.632 255.361 210.634 1.00 8.16   ? 2210 LEU A O     1 
ATOM   5364  C  CB    . LEU A 1 2210 ? 227.416 255.472 213.391 1.00 5.25   ? 2210 LEU A CB    1 
ATOM   5365  C  CG    . LEU A 1 2210 ? 226.053 255.061 213.945 1.00 5.67   ? 2210 LEU A CG    1 
ATOM   5366  C  CD1   . LEU A 1 2210 ? 225.893 253.555 213.896 1.00 5.67   ? 2210 LEU A CD1   1 
ATOM   5367  C  CD2   . LEU A 1 2210 ? 225.881 255.575 215.362 1.00 5.27   ? 2210 LEU A CD2   1 
ATOM   5368  N  N     . TYR A 1 2211 ? 226.794 257.279 210.838 1.00 5.09   ? 2211 TYR A N     1 
ATOM   5369  C  CA    . TYR A 1 2211 ? 225.871 258.017 209.981 1.00 5.46   ? 2211 TYR A CA    1 
ATOM   5370  C  C     . TYR A 1 2211 ? 225.868 257.461 208.562 1.00 5.74   ? 2211 TYR A C     1 
ATOM   5371  O  O     . TYR A 1 2211 ? 224.802 257.285 207.955 1.00 6.48   ? 2211 TYR A O     1 
ATOM   5372  C  CB    . TYR A 1 2211 ? 226.241 259.499 209.968 1.00 5.46   ? 2211 TYR A CB    1 
ATOM   5373  C  CG    . TYR A 1 2211 ? 225.428 260.314 208.989 1.00 7.19   ? 2211 TYR A CG    1 
ATOM   5374  C  CD1   . TYR A 1 2211 ? 224.044 260.343 209.062 1.00 7.18   ? 2211 TYR A CD1   1 
ATOM   5375  C  CD2   . TYR A 1 2211 ? 226.045 261.040 207.982 1.00 10.14  ? 2211 TYR A CD2   1 
ATOM   5376  C  CE1   . TYR A 1 2211 ? 223.299 261.079 208.167 1.00 8.86   ? 2211 TYR A CE1   1 
ATOM   5377  C  CE2   . TYR A 1 2211 ? 225.309 261.778 207.083 1.00 12.88  ? 2211 TYR A CE2   1 
ATOM   5378  C  CZ    . TYR A 1 2211 ? 223.935 261.795 207.180 1.00 14.53  ? 2211 TYR A CZ    1 
ATOM   5379  O  OH    . TYR A 1 2211 ? 223.196 262.532 206.283 1.00 38.07  ? 2211 TYR A OH    1 
ATOM   5380  N  N     . GLN A 1 2212 ? 227.052 257.181 208.015 1.00 6.02   ? 2212 GLN A N     1 
ATOM   5381  C  CA    . GLN A 1 2212 ? 227.125 256.619 206.669 1.00 6.49   ? 2212 GLN A CA    1 
ATOM   5382  C  C     . GLN A 1 2212 ? 226.455 255.250 206.602 1.00 6.59   ? 2212 GLN A C     1 
ATOM   5383  O  O     . GLN A 1 2212 ? 225.727 254.950 205.646 1.00 8.21   ? 2212 GLN A O     1 
ATOM   5384  C  CB    . GLN A 1 2212 ? 228.582 256.525 206.216 1.00 8.78   ? 2212 GLN A CB    1 
ATOM   5385  C  CG    . GLN A 1 2212 ? 229.279 257.866 206.090 1.00 12.49  ? 2212 GLN A CG    1 
ATOM   5386  C  CD    . GLN A 1 2212 ? 230.686 257.743 205.540 1.00 22.43  ? 2212 GLN A CD    1 
ATOM   5387  O  OE1   . GLN A 1 2212 ? 231.029 258.367 204.537 1.00 27.38  ? 2212 GLN A OE1   1 
ATOM   5388  N  NE2   . GLN A 1 2212 ? 231.508 256.931 206.194 1.00 20.22  ? 2212 GLN A NE2   1 
ATOM   5389  N  N     . ILE A 1 2213 ? 226.685 254.408 207.612 1.00 5.35   ? 2213 ILE A N     1 
ATOM   5390  C  CA    . ILE A 1 2213 ? 226.065 253.085 207.629 1.00 6.34   ? 2213 ILE A CA    1 
ATOM   5391  C  C     . ILE A 1 2213 ? 224.550 253.208 207.737 1.00 7.49   ? 2213 ILE A C     1 
ATOM   5392  O  O     . ILE A 1 2213 ? 223.806 252.444 207.112 1.00 9.35   ? 2213 ILE A O     1 
ATOM   5393  C  CB    . ILE A 1 2213 ? 226.654 252.226 208.764 1.00 8.03   ? 2213 ILE A CB    1 
ATOM   5394  C  CG1   . ILE A 1 2213 ? 228.156 252.026 208.557 1.00 6.99   ? 2213 ILE A CG1   1 
ATOM   5395  C  CG2   . ILE A 1 2213 ? 225.973 250.873 208.818 1.00 7.80   ? 2213 ILE A CG2   1 
ATOM   5396  C  CD1   . ILE A 1 2213 ? 228.502 251.127 207.394 1.00 6.50   ? 2213 ILE A CD1   1 
ATOM   5397  N  N     . THR A 1 2214 ? 224.068 254.174 208.525 1.00 7.64   ? 2214 THR A N     1 
ATOM   5398  C  CA    . THR A 1 2214 ? 222.632 254.438 208.578 1.00 6.28   ? 2214 THR A CA    1 
ATOM   5399  C  C     . THR A 1 2214 ? 222.105 254.825 207.205 1.00 7.92   ? 2214 THR A C     1 
ATOM   5400  O  O     . THR A 1 2214 ? 221.032 254.371 206.789 1.00 9.20   ? 2214 THR A O     1 
ATOM   5401  C  CB    . THR A 1 2214 ? 222.336 255.551 209.588 1.00 7.36   ? 2214 THR A CB    1 
ATOM   5402  O  OG1   . THR A 1 2214 ? 222.495 255.057 210.922 1.00 10.44  ? 2214 THR A OG1   1 
ATOM   5403  C  CG2   . THR A 1 2214 ? 220.915 256.065 209.424 1.00 8.12   ? 2214 THR A CG2   1 
ATOM   5404  N  N     . GLN A 1 2215 ? 222.855 255.659 206.485 1.00 13.55  ? 2215 GLN A N     1 
ATOM   5405  C  CA    . GLN A 1 2215 ? 222.425 256.080 205.155 1.00 11.19  ? 2215 GLN A CA    1 
ATOM   5406  C  C     . GLN A 1 2215 ? 222.387 254.907 204.185 1.00 12.76  ? 2215 GLN A C     1 
ATOM   5407  O  O     . GLN A 1 2215 ? 221.553 254.875 203.272 1.00 13.75  ? 2215 GLN A O     1 
ATOM   5408  C  CB    . GLN A 1 2215 ? 223.351 257.179 204.631 1.00 9.50   ? 2215 GLN A CB    1 
ATOM   5409  C  CG    . GLN A 1 2215 ? 223.174 258.525 205.313 1.00 10.83  ? 2215 GLN A CG    1 
ATOM   5410  C  CD    . GLN A 1 2215 ? 221.904 259.236 204.892 1.00 26.68  ? 2215 GLN A CD    1 
ATOM   5411  O  OE1   . GLN A 1 2215 ? 220.808 258.890 205.334 1.00 29.86  ? 2215 GLN A OE1   1 
ATOM   5412  N  NE2   . GLN A 1 2215 ? 222.044 260.237 204.032 1.00 27.01  ? 2215 GLN A NE2   1 
ATOM   5413  N  N     . ILE A 1 2216 ? 223.282 253.929 204.360 1.00 12.74  ? 2216 ILE A N     1 
ATOM   5414  C  CA    . ILE A 1 2216 ? 223.393 252.833 203.400 1.00 11.72  ? 2216 ILE A CA    1 
ATOM   5415  C  C     . ILE A 1 2216 ? 222.708 251.549 203.868 1.00 8.71   ? 2216 ILE A C     1 
ATOM   5416  O  O     . ILE A 1 2216 ? 222.354 250.711 203.024 1.00 7.06   ? 2216 ILE A O     1 
ATOM   5417  C  CB    . ILE A 1 2216 ? 224.874 252.549 203.059 1.00 10.88  ? 2216 ILE A CB    1 
ATOM   5418  C  CG1   . ILE A 1 2216 ? 224.988 251.638 201.834 1.00 14.35  ? 2216 ILE A CG1   1 
ATOM   5419  C  CG2   . ILE A 1 2216 ? 225.587 251.916 204.240 1.00 11.54  ? 2216 ILE A CG2   1 
ATOM   5420  C  CD1   . ILE A 1 2216 ? 224.487 252.274 200.556 1.00 14.73  ? 2216 ILE A CD1   1 
ATOM   5421  N  N     . ASN A 1 2217 ? 222.484 251.379 205.169 1.00 10.95  ? 2217 ASN A N     1 
ATOM   5422  C  CA    . ASN A 1 2217 ? 221.910 250.150 205.703 1.00 9.84   ? 2217 ASN A CA    1 
ATOM   5423  C  C     . ASN A 1 2217 ? 220.679 250.468 206.537 1.00 8.79   ? 2217 ASN A C     1 
ATOM   5424  O  O     . ASN A 1 2217 ? 220.639 251.483 207.237 1.00 11.61  ? 2217 ASN A O     1 
ATOM   5425  C  CB    . ASN A 1 2217 ? 222.927 249.386 206.563 1.00 7.23   ? 2217 ASN A CB    1 
ATOM   5426  C  CG    . ASN A 1 2217 ? 223.811 248.467 205.747 1.00 12.01  ? 2217 ASN A CG    1 
ATOM   5427  O  OD1   . ASN A 1 2217 ? 225.002 248.726 205.576 1.00 14.29  ? 2217 ASN A OD1   1 
ATOM   5428  N  ND2   . ASN A 1 2217 ? 223.235 247.385 205.244 1.00 10.73  ? 2217 ASN A ND2   1 
ATOM   5429  N  N     . HIS A 1 2218 ? 219.671 249.600 206.452 1.00 7.43   ? 2218 HIS A N     1 
ATOM   5430  C  CA    . HIS A 1 2218 ? 218.513 249.674 207.334 1.00 6.07   ? 2218 HIS A CA    1 
ATOM   5431  C  C     . HIS A 1 2218 ? 218.655 248.776 208.552 1.00 5.59   ? 2218 HIS A C     1 
ATOM   5432  O  O     . HIS A 1 2218 ? 217.790 248.800 209.434 1.00 4.85   ? 2218 HIS A O     1 
ATOM   5433  C  CB    . HIS A 1 2218 ? 217.232 249.315 206.574 1.00 5.51   ? 2218 HIS A CB    1 
ATOM   5434  C  CG    . HIS A 1 2218 ? 217.138 247.872 206.189 1.00 5.42   ? 2218 HIS A CG    1 
ATOM   5435  N  ND1   . HIS A 1 2218 ? 217.942 247.305 205.224 1.00 7.88   ? 2218 HIS A ND1   1 
ATOM   5436  C  CD2   . HIS A 1 2218 ? 216.332 246.882 206.636 1.00 6.28   ? 2218 HIS A CD2   1 
ATOM   5437  C  CE1   . HIS A 1 2218 ? 217.636 246.027 205.095 1.00 7.04   ? 2218 HIS A CE1   1 
ATOM   5438  N  NE2   . HIS A 1 2218 ? 216.664 245.744 205.942 1.00 7.74   ? 2218 HIS A NE2   1 
ATOM   5439  N  N     . GLY A 1 2219 ? 219.721 247.985 208.618 1.00 7.07   ? 2219 GLY A N     1 
ATOM   5440  C  CA    . GLY A 1 2219 ? 220.039 247.219 209.801 1.00 5.35   ? 2219 GLY A CA    1 
ATOM   5441  C  C     . GLY A 1 2219 ? 221.476 247.454 210.213 1.00 6.94   ? 2219 GLY A C     1 
ATOM   5442  O  O     . GLY A 1 2219 ? 222.410 247.128 209.474 1.00 8.57   ? 2219 GLY A O     1 
ATOM   5443  N  N     . LEU A 1 2220 ? 221.664 248.016 211.399 1.00 10.17  ? 2220 LEU A N     1 
ATOM   5444  C  CA    . LEU A 1 2220 ? 222.974 248.446 211.853 1.00 6.16   ? 2220 LEU A CA    1 
ATOM   5445  C  C     . LEU A 1 2220 ? 223.330 247.720 213.136 1.00 8.05   ? 2220 LEU A C     1 
ATOM   5446  O  O     . LEU A 1 2220 ? 222.459 247.196 213.832 1.00 10.11  ? 2220 LEU A O     1 
ATOM   5447  C  CB    . LEU A 1 2220 ? 223.024 249.944 212.123 1.00 4.93   ? 2220 LEU A CB    1 
ATOM   5448  C  CG    . LEU A 1 2220 ? 223.122 250.905 210.946 1.00 8.99   ? 2220 LEU A CG    1 
ATOM   5449  C  CD1   . LEU A 1 2220 ? 221.817 250.978 210.163 1.00 10.31  ? 2220 LEU A CD1   1 
ATOM   5450  C  CD2   . LEU A 1 2220 ? 223.526 252.258 211.453 1.00 11.58  ? 2220 LEU A CD2   1 
ATOM   5451  N  N     . MET A 1 2221 ? 224.624 247.692 213.439 1.00 7.18   ? 2221 MET A N     1 
ATOM   5452  C  CA    . MET A 1 2221 ? 225.087 247.144 214.703 1.00 8.31   ? 2221 MET A CA    1 
ATOM   5453  C  C     . MET A 1 2221 ? 226.372 247.838 215.140 1.00 7.64   ? 2221 MET A C     1 
ATOM   5454  O  O     . MET A 1 2221 ? 227.275 248.067 214.327 1.00 8.51   ? 2221 MET A O     1 
ATOM   5455  C  CB    . MET A 1 2221 ? 225.273 245.633 214.578 1.00 5.40   ? 2221 MET A CB    1 
ATOM   5456  C  CG    . MET A 1 2221 ? 225.637 244.932 215.861 1.00 7.20   ? 2221 MET A CG    1 
ATOM   5457  S  SD    . MET A 1 2221 ? 225.803 243.177 215.564 1.00 39.92  ? 2221 MET A SD    1 
ATOM   5458  C  CE    . MET A 1 2221 ? 224.096 242.711 215.329 1.00 6.62   ? 2221 MET A CE    1 
ATOM   5459  N  N     . MET A 1 2222 ? 226.427 248.196 216.425 1.00 5.76   ? 2222 MET A N     1 
ATOM   5460  C  CA    . MET A 1 2222 ? 227.541 248.924 217.022 1.00 4.44   ? 2222 MET A CA    1 
ATOM   5461  C  C     . MET A 1 2222 ? 228.257 247.968 217.971 1.00 4.82   ? 2222 MET A C     1 
ATOM   5462  O  O     . MET A 1 2222 ? 227.789 247.714 219.083 1.00 5.81   ? 2222 MET A O     1 
ATOM   5463  C  CB    . MET A 1 2222 ? 227.042 250.171 217.744 1.00 4.57   ? 2222 MET A CB    1 
ATOM   5464  C  CG    . MET A 1 2222 ? 226.547 251.252 216.801 1.00 6.46   ? 2222 MET A CG    1 
ATOM   5465  S  SD    . MET A 1 2222 ? 225.802 252.636 217.672 1.00 21.32  ? 2222 MET A SD    1 
ATOM   5466  C  CE    . MET A 1 2222 ? 224.119 252.045 217.816 1.00 8.58   ? 2222 MET A CE    1 
ATOM   5467  N  N     . VAL A 1 2223 ? 229.391 247.444 217.528 1.00 4.06   ? 2223 VAL A N     1 
ATOM   5468  C  CA    . VAL A 1 2223 ? 230.103 246.396 218.245 1.00 4.28   ? 2223 VAL A CA    1 
ATOM   5469  C  C     . VAL A 1 2223 ? 231.348 246.991 218.884 1.00 5.29   ? 2223 VAL A C     1 
ATOM   5470  O  O     . VAL A 1 2223 ? 232.059 247.800 218.279 1.00 6.18   ? 2223 VAL A O     1 
ATOM   5471  C  CB    . VAL A 1 2223 ? 230.461 245.226 217.302 1.00 4.35   ? 2223 VAL A CB    1 
ATOM   5472  C  CG1   . VAL A 1 2223 ? 231.275 244.168 218.033 1.00 4.77   ? 2223 VAL A CG1   1 
ATOM   5473  C  CG2   . VAL A 1 2223 ? 229.198 244.623 216.698 1.00 5.19   ? 2223 VAL A CG2   1 
ATOM   5474  N  N     . GLY A 1 2224 ? 231.604 246.604 220.130 1.00 4.00   ? 2224 GLY A N     1 
ATOM   5475  C  CA    . GLY A 1 2224 ? 232.796 247.021 220.822 1.00 3.04   ? 2224 GLY A CA    1 
ATOM   5476  C  C     . GLY A 1 2224 ? 232.721 246.739 222.306 1.00 5.42   ? 2224 GLY A C     1 
ATOM   5477  O  O     . GLY A 1 2224 ? 231.639 246.549 222.865 1.00 5.78   ? 2224 GLY A O     1 
ATOM   5478  N  N     . PRO A 1 2225 ? 233.872 246.718 222.977 1.00 6.54   ? 2225 PRO A N     1 
ATOM   5479  C  CA    . PRO A 1 2225 ? 233.885 246.434 224.415 1.00 4.27   ? 2225 PRO A CA    1 
ATOM   5480  C  C     . PRO A 1 2225 ? 233.061 247.450 225.190 1.00 4.48   ? 2225 PRO A C     1 
ATOM   5481  O  O     . PRO A 1 2225 ? 232.771 248.550 224.713 1.00 7.06   ? 2225 PRO A O     1 
ATOM   5482  C  CB    . PRO A 1 2225 ? 235.370 246.525 224.785 1.00 5.98   ? 2225 PRO A CB    1 
ATOM   5483  C  CG    . PRO A 1 2225 ? 236.093 246.307 223.504 1.00 6.02   ? 2225 PRO A CG    1 
ATOM   5484  C  CD    . PRO A 1 2225 ? 235.230 246.898 222.439 1.00 5.51   ? 2225 PRO A CD    1 
ATOM   5485  N  N     . SER A 1 2226 ? 232.673 247.059 226.402 1.00 4.47   ? 2226 SER A N     1 
ATOM   5486  C  CA    . SER A 1 2226 ? 231.808 247.903 227.214 1.00 4.85   ? 2226 SER A CA    1 
ATOM   5487  C  C     . SER A 1 2226 ? 232.459 249.256 227.464 1.00 4.12   ? 2226 SER A C     1 
ATOM   5488  O  O     . SER A 1 2226 ? 233.653 249.348 227.757 1.00 7.79   ? 2226 SER A O     1 
ATOM   5489  C  CB    . SER A 1 2226 ? 231.486 247.221 228.543 1.00 5.07   ? 2226 SER A CB    1 
ATOM   5490  O  OG    . SER A 1 2226 ? 230.455 247.910 229.229 1.00 4.51   ? 2226 SER A OG    1 
ATOM   5491  N  N     . GLY A 1 2227 ? 231.660 250.309 227.348 1.00 3.27   ? 2227 GLY A N     1 
ATOM   5492  C  CA    . GLY A 1 2227 ? 232.164 251.656 227.515 1.00 3.01   ? 2227 GLY A CA    1 
ATOM   5493  C  C     . GLY A 1 2227 ? 233.130 252.120 226.448 1.00 3.75   ? 2227 GLY A C     1 
ATOM   5494  O  O     . GLY A 1 2227 ? 234.164 252.715 226.770 1.00 7.04   ? 2227 GLY A O     1 
ATOM   5495  N  N     . SER A 1 2228 ? 232.820 251.855 225.181 1.00 4.67   ? 2228 SER A N     1 
ATOM   5496  C  CA    . SER A 1 2228 ? 233.594 252.371 224.063 1.00 4.45   ? 2228 SER A CA    1 
ATOM   5497  C  C     . SER A 1 2228 ? 232.929 253.576 223.409 1.00 3.63   ? 2228 SER A C     1 
ATOM   5498  O  O     . SER A 1 2228 ? 233.382 254.025 222.352 1.00 6.90   ? 2228 SER A O     1 
ATOM   5499  C  CB    . SER A 1 2228 ? 233.829 251.267 223.030 1.00 5.25   ? 2228 SER A CB    1 
ATOM   5500  O  OG    . SER A 1 2228 ? 232.644 250.532 222.786 1.00 5.02   ? 2228 SER A OG    1 
ATOM   5501  N  N     . GLY A 1 2229 ? 231.869 254.109 224.011 1.00 2.33   ? 2229 GLY A N     1 
ATOM   5502  C  CA    . GLY A 1 2229 ? 231.220 255.296 223.499 1.00 3.20   ? 2229 GLY A CA    1 
ATOM   5503  C  C     . GLY A 1 2229 ? 230.118 255.063 222.493 1.00 3.47   ? 2229 GLY A C     1 
ATOM   5504  O  O     . GLY A 1 2229 ? 229.759 255.997 221.769 1.00 7.10   ? 2229 GLY A O     1 
ATOM   5505  N  N     . LYS A 1 2230 ? 229.568 253.851 222.423 1.00 1.85   ? 2230 LYS A N     1 
ATOM   5506  C  CA    . LYS A 1 2230 ? 228.555 253.539 221.419 1.00 1.57   ? 2230 LYS A CA    1 
ATOM   5507  C  C     . LYS A 1 2230 ? 227.248 254.274 221.690 1.00 3.06   ? 2230 LYS A C     1 
ATOM   5508  O  O     . LYS A 1 2230 ? 226.655 254.872 220.779 1.00 5.76   ? 2230 LYS A O     1 
ATOM   5509  C  CB    . LYS A 1 2230 ? 228.319 252.031 221.380 1.00 4.07   ? 2230 LYS A CB    1 
ATOM   5510  C  CG    . LYS A 1 2230 ? 229.579 251.205 221.212 1.00 2.47   ? 2230 LYS A CG    1 
ATOM   5511  C  CD    . LYS A 1 2230 ? 229.302 249.736 221.453 1.00 3.08   ? 2230 LYS A CD    1 
ATOM   5512  C  CE    . LYS A 1 2230 ? 228.782 249.509 222.861 1.00 3.39   ? 2230 LYS A CE    1 
ATOM   5513  N  NZ    . LYS A 1 2230 ? 228.759 248.073 223.238 1.00 3.59   ? 2230 LYS A NZ    1 
ATOM   5514  N  N     . SER A 1 2231 ? 226.769 254.218 222.937 1.00 2.91   ? 2231 SER A N     1 
ATOM   5515  C  CA    . SER A 1 2231 ? 225.484 254.823 223.271 1.00 2.44   ? 2231 SER A CA    1 
ATOM   5516  C  C     . SER A 1 2231 ? 225.508 256.323 223.032 1.00 2.87   ? 2231 SER A C     1 
ATOM   5517  O  O     . SER A 1 2231 ? 224.601 256.881 222.400 1.00 3.23   ? 2231 SER A O     1 
ATOM   5518  C  CB    . SER A 1 2231 ? 225.120 254.519 224.723 1.00 2.39   ? 2231 SER A CB    1 
ATOM   5519  O  OG    . SER A 1 2231 ? 225.002 253.127 224.944 1.00 3.23   ? 2231 SER A OG    1 
ATOM   5520  N  N     . MET A 1 2232 ? 226.544 256.992 223.538 1.00 3.13   ? 2232 MET A N     1 
ATOM   5521  C  CA    . MET A 1 2232 ? 226.686 258.421 223.299 1.00 3.09   ? 2232 MET A CA    1 
ATOM   5522  C  C     . MET A 1 2232 ? 226.813 258.712 221.814 1.00 3.21   ? 2232 MET A C     1 
ATOM   5523  O  O     . MET A 1 2232 ? 226.271 259.708 221.326 1.00 4.99   ? 2232 MET A O     1 
ATOM   5524  C  CB    . MET A 1 2232 ? 227.888 258.967 224.065 1.00 2.82   ? 2232 MET A CB    1 
ATOM   5525  C  CG    . MET A 1 2232 ? 227.767 259.030 225.597 1.00 2.92   ? 2232 MET A CG    1 
ATOM   5526  S  SD    . MET A 1 2232 ? 226.351 259.895 226.335 1.00 14.44  ? 2232 MET A SD    1 
ATOM   5527  C  CE    . MET A 1 2232 ? 225.011 258.713 226.200 1.00 4.08   ? 2232 MET A CE    1 
ATOM   5528  N  N     . ALA A 1 2233 ? 227.501 257.840 221.076 1.00 3.00   ? 2233 ALA A N     1 
ATOM   5529  C  CA    . ALA A 1 2233 ? 227.652 258.043 219.640 1.00 2.40   ? 2233 ALA A CA    1 
ATOM   5530  C  C     . ALA A 1 2233 ? 226.299 258.090 218.945 1.00 3.11   ? 2233 ALA A C     1 
ATOM   5531  O  O     . ALA A 1 2233 ? 225.992 259.052 218.232 1.00 4.31   ? 2233 ALA A O     1 
ATOM   5532  C  CB    . ALA A 1 2233 ? 228.523 256.942 219.039 1.00 1.97   ? 2233 ALA A CB    1 
ATOM   5533  N  N     . TRP A 1 2234 ? 225.461 257.073 219.160 1.00 3.33   ? 2234 TRP A N     1 
ATOM   5534  C  CA    . TRP A 1 2234 ? 224.202 257.058 218.420 1.00 2.48   ? 2234 TRP A CA    1 
ATOM   5535  C  C     . TRP A 1 2234 ? 223.217 258.095 218.953 1.00 3.31   ? 2234 TRP A C     1 
ATOM   5536  O  O     . TRP A 1 2234 ? 222.445 258.660 218.171 1.00 4.71   ? 2234 TRP A O     1 
ATOM   5537  C  CB    . TRP A 1 2234 ? 223.588 255.651 218.397 1.00 2.56   ? 2234 TRP A CB    1 
ATOM   5538  C  CG    . TRP A 1 2234 ? 223.002 255.139 219.675 1.00 2.53   ? 2234 TRP A CG    1 
ATOM   5539  C  CD1   . TRP A 1 2234 ? 223.573 254.247 220.530 1.00 2.44   ? 2234 TRP A CD1   1 
ATOM   5540  C  CD2   . TRP A 1 2234 ? 221.713 255.447 220.218 1.00 2.75   ? 2234 TRP A CD2   1 
ATOM   5541  N  NE1   . TRP A 1 2234 ? 222.734 253.997 221.585 1.00 3.34   ? 2234 TRP A NE1   1 
ATOM   5542  C  CE2   . TRP A 1 2234 ? 221.585 254.723 221.418 1.00 2.78   ? 2234 TRP A CE2   1 
ATOM   5543  C  CE3   . TRP A 1 2234 ? 220.662 256.275 219.817 1.00 2.68   ? 2234 TRP A CE3   1 
ATOM   5544  C  CZ2   . TRP A 1 2234 ? 220.450 254.800 222.216 1.00 2.53   ? 2234 TRP A CZ2   1 
ATOM   5545  C  CZ3   . TRP A 1 2234 ? 219.540 256.351 220.610 1.00 2.68   ? 2234 TRP A CZ3   1 
ATOM   5546  C  CH2   . TRP A 1 2234 ? 219.441 255.618 221.796 1.00 3.44   ? 2234 TRP A CH2   1 
ATOM   5547  N  N     . ARG A 1 2235 ? 223.248 258.397 220.254 1.00 3.21   ? 2235 ARG A N     1 
ATOM   5548  C  CA    . ARG A 1 2235 ? 222.374 259.447 220.771 1.00 2.91   ? 2235 ARG A CA    1 
ATOM   5549  C  C     . ARG A 1 2235 ? 222.750 260.812 220.203 1.00 4.62   ? 2235 ARG A C     1 
ATOM   5550  O  O     . ARG A 1 2235 ? 221.877 261.595 219.797 1.00 8.76   ? 2235 ARG A O     1 
ATOM   5551  C  CB    . ARG A 1 2235 ? 222.428 259.467 222.298 1.00 3.18   ? 2235 ARG A CB    1 
ATOM   5552  C  CG    . ARG A 1 2235 ? 221.739 258.290 222.956 1.00 3.21   ? 2235 ARG A CG    1 
ATOM   5553  C  CD    . ARG A 1 2235 ? 221.929 258.346 224.456 1.00 5.62   ? 2235 ARG A CD    1 
ATOM   5554  N  NE    . ARG A 1 2235 ? 221.407 257.166 225.132 1.00 10.88  ? 2235 ARG A NE    1 
ATOM   5555  C  CZ    . ARG A 1 2235 ? 220.122 256.947 225.371 1.00 11.14  ? 2235 ARG A CZ    1 
ATOM   5556  N  NH1   . ARG A 1 2235 ? 219.189 257.798 224.977 1.00 6.73   ? 2235 ARG A NH1   1 
ATOM   5557  N  NH2   . ARG A 1 2235 ? 219.764 255.849 226.028 1.00 11.76  ? 2235 ARG A NH2   1 
ATOM   5558  N  N     . VAL A 1 2236 ? 224.049 261.118 220.168 1.00 3.68   ? 2236 VAL A N     1 
ATOM   5559  C  CA    . VAL A 1 2236 ? 224.509 262.386 219.619 1.00 3.63   ? 2236 VAL A CA    1 
ATOM   5560  C  C     . VAL A 1 2236 ? 224.202 262.459 218.132 1.00 6.22   ? 2236 VAL A C     1 
ATOM   5561  O  O     . VAL A 1 2236 ? 223.813 263.513 217.617 1.00 9.91   ? 2236 VAL A O     1 
ATOM   5562  C  CB    . VAL A 1 2236 ? 226.010 262.575 219.907 1.00 4.75   ? 2236 VAL A CB    1 
ATOM   5563  C  CG1   . VAL A 1 2236 ? 226.611 263.629 218.997 1.00 11.37  ? 2236 VAL A CG1   1 
ATOM   5564  C  CG2   . VAL A 1 2236 ? 226.217 262.955 221.359 1.00 5.31   ? 2236 VAL A CG2   1 
ATOM   5565  N  N     . LEU A 1 2237 ? 224.364 261.341 217.417 1.00 5.83   ? 2237 LEU A N     1 
ATOM   5566  C  CA    . LEU A 1 2237 ? 224.009 261.322 216.004 1.00 4.38   ? 2237 LEU A CA    1 
ATOM   5567  C  C     . LEU A 1 2237 ? 222.526 261.603 215.806 1.00 4.57   ? 2237 LEU A C     1 
ATOM   5568  O  O     . LEU A 1 2237 ? 222.148 262.354 214.902 1.00 6.92   ? 2237 LEU A O     1 
ATOM   5569  C  CB    . LEU A 1 2237 ? 224.389 259.979 215.380 1.00 4.34   ? 2237 LEU A CB    1 
ATOM   5570  C  CG    . LEU A 1 2237 ? 224.083 259.841 213.889 1.00 6.02   ? 2237 LEU A CG    1 
ATOM   5571  C  CD1   . LEU A 1 2237 ? 224.821 260.901 213.093 1.00 4.97   ? 2237 LEU A CD1   1 
ATOM   5572  C  CD2   . LEU A 1 2237 ? 224.442 258.454 213.393 1.00 5.08   ? 2237 LEU A CD2   1 
ATOM   5573  N  N     . LEU A 1 2238 ? 221.672 261.011 216.643 1.00 4.26   ? 2238 LEU A N     1 
ATOM   5574  C  CA    . LEU A 1 2238 ? 220.236 261.242 216.524 1.00 5.64   ? 2238 LEU A CA    1 
ATOM   5575  C  C     . LEU A 1 2238 ? 219.893 262.710 216.758 1.00 8.71   ? 2238 LEU A C     1 
ATOM   5576  O  O     . LEU A 1 2238 ? 219.135 263.315 215.988 1.00 11.32  ? 2238 LEU A O     1 
ATOM   5577  C  CB    . LEU A 1 2238 ? 219.486 260.346 217.510 1.00 4.03   ? 2238 LEU A CB    1 
ATOM   5578  C  CG    . LEU A 1 2238 ? 217.981 260.163 217.310 1.00 4.63   ? 2238 LEU A CG    1 
ATOM   5579  C  CD1   . LEU A 1 2238 ? 217.688 259.593 215.936 1.00 3.97   ? 2238 LEU A CD1   1 
ATOM   5580  C  CD2   . LEU A 1 2238 ? 217.406 259.273 218.394 1.00 4.79   ? 2238 LEU A CD2   1 
ATOM   5581  N  N     . LYS A 1 2239 ? 220.458 263.304 217.813 1.00 7.67   ? 2239 LYS A N     1 
ATOM   5582  C  CA    . LYS A 1 2239 ? 220.173 264.709 218.098 1.00 8.00   ? 2239 LYS A CA    1 
ATOM   5583  C  C     . LYS A 1 2239 ? 220.697 265.623 216.992 1.00 12.97  ? 2239 LYS A C     1 
ATOM   5584  O  O     . LYS A 1 2239 ? 220.017 266.578 216.590 1.00 16.38  ? 2239 LYS A O     1 
ATOM   5585  C  CB    . LYS A 1 2239 ? 220.764 265.105 219.450 1.00 13.18  ? 2239 LYS A CB    1 
ATOM   5586  C  CG    . LYS A 1 2239 ? 220.162 264.355 220.624 1.00 20.12  ? 2239 LYS A CG    1 
ATOM   5587  C  CD    . LYS A 1 2239 ? 220.420 265.072 221.936 1.00 19.65  ? 2239 LYS A CD    1 
ATOM   5588  C  CE    . LYS A 1 2239 ? 219.838 264.295 223.104 1.00 23.45  ? 2239 LYS A CE    1 
ATOM   5589  N  NZ    . LYS A 1 2239 ? 219.804 265.104 224.352 1.00 33.74  ? 2239 LYS A NZ    1 
ATOM   5590  N  N     . ALA A 1 2240 ? 221.901 265.345 216.485 1.00 11.61  ? 2240 ALA A N     1 
ATOM   5591  C  CA    . ALA A 1 2240 ? 222.465 266.163 215.419 1.00 10.87  ? 2240 ALA A CA    1 
ATOM   5592  C  C     . ALA A 1 2240 ? 221.650 266.046 214.139 1.00 11.67  ? 2240 ALA A C     1 
ATOM   5593  O  O     . ALA A 1 2240 ? 221.448 267.039 213.433 1.00 15.65  ? 2240 ALA A O     1 
ATOM   5594  C  CB    . ALA A 1 2240 ? 223.917 265.770 215.168 1.00 12.31  ? 2240 ALA A CB    1 
ATOM   5595  N  N     . LEU A 1 2241 ? 221.181 264.840 213.815 1.00 12.43  ? 2241 LEU A N     1 
ATOM   5596  C  CA    . LEU A 1 2241 ? 220.339 264.674 212.636 1.00 12.03  ? 2241 LEU A CA    1 
ATOM   5597  C  C     . LEU A 1 2241 ? 219.014 265.403 212.805 1.00 12.23  ? 2241 LEU A C     1 
ATOM   5598  O  O     . LEU A 1 2241 ? 218.490 265.977 211.844 1.00 14.25  ? 2241 LEU A O     1 
ATOM   5599  C  CB    . LEU A 1 2241 ? 220.108 263.191 212.355 1.00 8.31   ? 2241 LEU A CB    1 
ATOM   5600  C  CG    . LEU A 1 2241 ? 221.295 262.454 211.733 1.00 7.18   ? 2241 LEU A CG    1 
ATOM   5601  C  CD1   . LEU A 1 2241 ? 220.892 261.059 211.295 1.00 12.41  ? 2241 LEU A CD1   1 
ATOM   5602  C  CD2   . LEU A 1 2241 ? 221.857 263.248 210.569 1.00 8.45   ? 2241 LEU A CD2   1 
ATOM   5603  N  N     . GLU A 1 2242 ? 218.457 265.390 214.018 1.00 16.33  ? 2242 GLU A N     1 
ATOM   5604  C  CA    . GLU A 1 2242 ? 217.230 266.139 214.266 1.00 17.92  ? 2242 GLU A CA    1 
ATOM   5605  C  C     . GLU A 1 2242 ? 217.449 267.634 214.073 1.00 19.60  ? 2242 GLU A C     1 
ATOM   5606  O  O     . GLU A 1 2242 ? 216.601 268.324 213.495 1.00 24.48  ? 2242 GLU A O     1 
ATOM   5607  C  CB    . GLU A 1 2242 ? 216.709 265.851 215.672 1.00 17.42  ? 2242 GLU A CB    1 
ATOM   5608  C  CG    . GLU A 1 2242 ? 215.447 266.617 216.026 1.00 24.49  ? 2242 GLU A CG    1 
ATOM   5609  C  CD    . GLU A 1 2242 ? 215.001 266.380 217.454 1.00 40.68  ? 2242 GLU A CD    1 
ATOM   5610  O  OE1   . GLU A 1 2242 ? 215.318 265.307 218.007 1.00 42.15  ? 2242 GLU A OE1   1 
ATOM   5611  O  OE2   . GLU A 1 2242 ? 214.333 267.269 218.024 1.00 45.27  ? 2242 GLU A OE2   1 
ATOM   5612  N  N     . ARG A 1 2243 ? 218.582 268.154 214.544 1.00 22.06  ? 2243 ARG A N     1 
ATOM   5613  C  CA    . ARG A 1 2243 ? 218.843 269.583 214.418 1.00 20.35  ? 2243 ARG A CA    1 
ATOM   5614  C  C     . ARG A 1 2243 ? 219.347 269.989 213.038 1.00 20.51  ? 2243 ARG A C     1 
ATOM   5615  O  O     . ARG A 1 2243 ? 219.329 271.182 212.721 1.00 32.57  ? 2243 ARG A O     1 
ATOM   5616  C  CB    . ARG A 1 2243 ? 219.844 270.034 215.482 1.00 18.02  ? 2243 ARG A CB    1 
ATOM   5617  C  CG    . ARG A 1 2243 ? 219.243 270.170 216.867 1.00 25.92  ? 2243 ARG A CG    1 
ATOM   5618  C  CD    . ARG A 1 2243 ? 220.169 270.921 217.807 1.00 33.96  ? 2243 ARG A CD    1 
ATOM   5619  N  NE    . ARG A 1 2243 ? 220.295 270.253 219.096 1.00 35.89  ? 2243 ARG A NE    1 
ATOM   5620  C  CZ    . ARG A 1 2243 ? 221.169 270.592 220.032 1.00 40.43  ? 2243 ARG A CZ    1 
ATOM   5621  N  NH1   . ARG A 1 2243 ? 222.015 271.594 219.858 1.00 41.75  ? 2243 ARG A NH1   1 
ATOM   5622  N  NH2   . ARG A 1 2243 ? 221.195 269.911 221.173 1.00 42.88  ? 2243 ARG A NH2   1 
ATOM   5623  N  N     . LEU A 1 2244 ? 219.794 269.042 212.216 1.00 17.45  ? 2244 LEU A N     1 
ATOM   5624  C  CA    . LEU A 1 2244 ? 220.288 269.343 210.877 1.00 15.67  ? 2244 LEU A CA    1 
ATOM   5625  C  C     . LEU A 1 2244 ? 219.225 269.161 209.800 1.00 19.31  ? 2244 LEU A C     1 
ATOM   5626  O  O     . LEU A 1 2244 ? 219.010 270.061 208.984 1.00 20.85  ? 2244 LEU A O     1 
ATOM   5627  C  CB    . LEU A 1 2244 ? 221.506 268.467 210.561 1.00 17.01  ? 2244 LEU A CB    1 
ATOM   5628  C  CG    . LEU A 1 2244 ? 222.044 268.514 209.130 1.00 22.92  ? 2244 LEU A CG    1 
ATOM   5629  C  CD1   . LEU A 1 2244 ? 222.980 269.695 208.945 1.00 16.66  ? 2244 LEU A CD1   1 
ATOM   5630  C  CD2   . LEU A 1 2244 ? 222.747 267.214 208.776 1.00 19.94  ? 2244 LEU A CD2   1 
ATOM   5631  N  N     . GLU A 1 2245 ? 218.557 268.008 209.774 1.00 25.61  ? 2245 GLU A N     1 
ATOM   5632  C  CA    . GLU A 1 2245 ? 217.533 267.742 208.773 1.00 23.20  ? 2245 GLU A CA    1 
ATOM   5633  C  C     . GLU A 1 2245 ? 216.156 268.249 209.173 1.00 19.24  ? 2245 GLU A C     1 
ATOM   5634  O  O     . GLU A 1 2245 ? 215.271 268.332 208.315 1.00 27.29  ? 2245 GLU A O     1 
ATOM   5635  C  CB    . GLU A 1 2245 ? 217.445 266.240 208.493 1.00 26.84  ? 2245 GLU A CB    1 
ATOM   5636  C  CG    . GLU A 1 2245 ? 218.766 265.597 208.118 1.00 22.54  ? 2245 GLU A CG    1 
ATOM   5637  C  CD    . GLU A 1 2245 ? 218.640 264.103 207.911 1.00 27.81  ? 2245 GLU A CD    1 
ATOM   5638  O  OE1   . GLU A 1 2245 ? 217.495 263.611 207.839 1.00 30.44  ? 2245 GLU A OE1   1 
ATOM   5639  O  OE2   . GLU A 1 2245 ? 219.683 263.423 207.821 1.00 32.82  ? 2245 GLU A OE2   1 
ATOM   5640  N  N     . GLY A 1 2246 ? 215.952 268.585 210.443 1.00 19.12  ? 2246 GLY A N     1 
ATOM   5641  C  CA    . GLY A 1 2246 ? 214.655 269.014 210.914 1.00 20.30  ? 2246 GLY A CA    1 
ATOM   5642  C  C     . GLY A 1 2246 ? 213.677 267.899 211.202 1.00 24.64  ? 2246 GLY A C     1 
ATOM   5643  O  O     . GLY A 1 2246 ? 212.534 268.185 211.583 1.00 28.56  ? 2246 GLY A O     1 
ATOM   5644  N  N     . VAL A 1 2247 ? 214.079 266.645 211.034 1.00 24.81  ? 2247 VAL A N     1 
ATOM   5645  C  CA    . VAL A 1 2247 ? 213.213 265.502 211.300 1.00 22.61  ? 2247 VAL A CA    1 
ATOM   5646  C  C     . VAL A 1 2247 ? 213.463 265.037 212.728 1.00 23.39  ? 2247 VAL A C     1 
ATOM   5647  O  O     . VAL A 1 2247 ? 214.593 264.697 213.091 1.00 27.31  ? 2247 VAL A O     1 
ATOM   5648  C  CB    . VAL A 1 2247 ? 213.466 264.367 210.297 1.00 22.49  ? 2247 VAL A CB    1 
ATOM   5649  C  CG1   . VAL A 1 2247 ? 212.376 263.315 210.399 1.00 23.54  ? 2247 VAL A CG1   1 
ATOM   5650  C  CG2   . VAL A 1 2247 ? 213.546 264.920 208.885 1.00 22.81  ? 2247 VAL A CG2   1 
ATOM   5651  N  N     . GLU A 1 2248 ? 212.407 265.021 213.538 1.00 24.14  ? 2248 GLU A N     1 
ATOM   5652  C  CA    . GLU A 1 2248 ? 212.549 264.634 214.934 1.00 25.45  ? 2248 GLU A CA    1 
ATOM   5653  C  C     . GLU A 1 2248 ? 212.881 263.152 215.049 1.00 22.45  ? 2248 GLU A C     1 
ATOM   5654  O  O     . GLU A 1 2248 ? 212.267 262.305 214.394 1.00 28.80  ? 2248 GLU A O     1 
ATOM   5655  C  CB    . GLU A 1 2248 ? 211.269 264.962 215.705 1.00 26.35  ? 2248 GLU A CB    1 
ATOM   5656  C  CG    . GLU A 1 2248 ? 211.145 264.253 217.043 1.00 35.79  ? 2248 GLU A CG    1 
ATOM   5657  C  CD    . GLU A 1 2248 ? 209.707 264.085 217.485 1.00 51.03  ? 2248 GLU A CD    1 
ATOM   5658  O  OE1   . GLU A 1 2248 ? 208.809 264.641 216.821 1.00 48.78  ? 2248 GLU A OE1   1 
ATOM   5659  O  OE2   . GLU A 1 2248 ? 209.474 263.392 218.497 1.00 55.35  ? 2248 GLU A OE2   1 
ATOM   5660  N  N     . GLY A 1 2249 ? 213.864 262.841 215.889 1.00 16.74  ? 2249 GLY A N     1 
ATOM   5661  C  CA    . GLY A 1 2249 ? 214.313 261.474 216.058 1.00 13.04  ? 2249 GLY A CA    1 
ATOM   5662  C  C     . GLY A 1 2249 ? 213.808 260.824 217.329 1.00 13.27  ? 2249 GLY A C     1 
ATOM   5663  O  O     . GLY A 1 2249 ? 214.007 261.350 218.428 1.00 15.62  ? 2249 GLY A O     1 
ATOM   5664  N  N     . VAL A 1 2250 ? 213.152 259.676 217.188 1.00 14.89  ? 2250 VAL A N     1 
ATOM   5665  C  CA    . VAL A 1 2250 ? 212.612 258.924 218.313 1.00 10.65  ? 2250 VAL A CA    1 
ATOM   5666  C  C     . VAL A 1 2250 ? 213.337 257.589 218.384 1.00 12.03  ? 2250 VAL A C     1 
ATOM   5667  O  O     . VAL A 1 2250 ? 213.413 256.863 217.385 1.00 12.67  ? 2250 VAL A O     1 
ATOM   5668  C  CB    . VAL A 1 2250 ? 211.095 258.709 218.182 1.00 11.03  ? 2250 VAL A CB    1 
ATOM   5669  C  CG1   . VAL A 1 2250 ? 210.535 258.119 219.464 1.00 10.40  ? 2250 VAL A CG1   1 
ATOM   5670  C  CG2   . VAL A 1 2250 ? 210.401 260.017 217.840 1.00 23.36  ? 2250 VAL A CG2   1 
ATOM   5671  N  N     . ALA A 1 2251 ? 213.858 257.266 219.564 1.00 8.86   ? 2251 ALA A N     1 
ATOM   5672  C  CA    . ALA A 1 2251 ? 214.598 256.035 219.790 1.00 7.02   ? 2251 ALA A CA    1 
ATOM   5673  C  C     . ALA A 1 2251 ? 213.851 255.167 220.791 1.00 7.90   ? 2251 ALA A C     1 
ATOM   5674  O  O     . ALA A 1 2251 ? 213.487 255.633 221.875 1.00 10.54  ? 2251 ALA A O     1 
ATOM   5675  C  CB    . ALA A 1 2251 ? 216.012 256.328 220.297 1.00 4.92   ? 2251 ALA A CB    1 
ATOM   5676  N  N     . HIS A 1 2252 ? 213.623 253.911 220.421 1.00 6.82   ? 2252 HIS A N     1 
ATOM   5677  C  CA    . HIS A 1 2252 ? 213.036 252.910 221.304 1.00 5.38   ? 2252 HIS A CA    1 
ATOM   5678  C  C     . HIS A 1 2252 ? 214.129 251.915 221.669 1.00 6.66   ? 2252 HIS A C     1 
ATOM   5679  O  O     . HIS A 1 2252 ? 214.590 251.152 220.815 1.00 6.84   ? 2252 HIS A O     1 
ATOM   5680  C  CB    . HIS A 1 2252 ? 211.852 252.212 220.639 1.00 4.83   ? 2252 HIS A CB    1 
ATOM   5681  C  CG    . HIS A 1 2252 ? 210.869 253.152 220.017 1.00 8.70   ? 2252 HIS A CG    1 
ATOM   5682  N  ND1   . HIS A 1 2252 ? 209.782 253.651 220.702 1.00 7.31   ? 2252 HIS A ND1   1 
ATOM   5683  C  CD2   . HIS A 1 2252 ? 210.806 253.683 218.773 1.00 10.13  ? 2252 HIS A CD2   1 
ATOM   5684  C  CE1   . HIS A 1 2252 ? 209.094 254.450 219.907 1.00 6.66   ? 2252 HIS A CE1   1 
ATOM   5685  N  NE2   . HIS A 1 2252 ? 209.694 254.487 218.731 1.00 7.15   ? 2252 HIS A NE2   1 
ATOM   5686  N  N     . ILE A 1 2253 ? 214.541 251.924 222.932 1.00 5.60   ? 2253 ILE A N     1 
ATOM   5687  C  CA    . ILE A 1 2253 ? 215.611 251.063 223.421 1.00 4.77   ? 2253 ILE A CA    1 
ATOM   5688  C  C     . ILE A 1 2253 ? 214.990 249.845 224.083 1.00 6.50   ? 2253 ILE A C     1 
ATOM   5689  O  O     . ILE A 1 2253 ? 214.133 249.975 224.965 1.00 11.20  ? 2253 ILE A O     1 
ATOM   5690  C  CB    . ILE A 1 2253 ? 216.526 251.816 224.399 1.00 4.17   ? 2253 ILE A CB    1 
ATOM   5691  C  CG1   . ILE A 1 2253 ? 216.819 253.216 223.865 1.00 4.34   ? 2253 ILE A CG1   1 
ATOM   5692  C  CG2   . ILE A 1 2253 ? 217.815 251.045 224.619 1.00 5.13   ? 2253 ILE A CG2   1 
ATOM   5693  C  CD1   . ILE A 1 2253 ? 217.267 254.179 224.921 1.00 6.05   ? 2253 ILE A CD1   1 
ATOM   5694  N  N     . ILE A 1 2254 ? 215.417 248.659 223.657 1.00 4.46   ? 2254 ILE A N     1 
ATOM   5695  C  CA    . ILE A 1 2254 ? 214.884 247.400 224.156 1.00 5.49   ? 2254 ILE A CA    1 
ATOM   5696  C  C     . ILE A 1 2254 ? 216.050 246.520 224.579 1.00 7.08   ? 2254 ILE A C     1 
ATOM   5697  O  O     . ILE A 1 2254 ? 217.041 246.406 223.851 1.00 9.67   ? 2254 ILE A O     1 
ATOM   5698  C  CB    . ILE A 1 2254 ? 214.026 246.683 223.096 1.00 5.41   ? 2254 ILE A CB    1 
ATOM   5699  C  CG1   . ILE A 1 2254 ? 212.809 247.533 222.724 1.00 7.53   ? 2254 ILE A CG1   1 
ATOM   5700  C  CG2   . ILE A 1 2254 ? 213.601 245.308 223.583 1.00 5.47   ? 2254 ILE A CG2   1 
ATOM   5701  C  CD1   . ILE A 1 2254 ? 212.074 247.044 221.499 1.00 5.99   ? 2254 ILE A CD1   1 
ATOM   5702  N  N     . ASP A 1 2255 ? 215.939 245.915 225.758 1.00 8.91   ? 2255 ASP A N     1 
ATOM   5703  C  CA    . ASP A 1 2255 ? 216.865 244.864 226.150 1.00 7.96   ? 2255 ASP A CA    1 
ATOM   5704  C  C     . ASP A 1 2255 ? 216.248 243.520 225.782 1.00 7.76   ? 2255 ASP A C     1 
ATOM   5705  O  O     . ASP A 1 2255 ? 215.378 243.015 226.501 1.00 6.57   ? 2255 ASP A O     1 
ATOM   5706  C  CB    . ASP A 1 2255 ? 217.182 244.931 227.643 1.00 7.42   ? 2255 ASP A CB    1 
ATOM   5707  C  CG    . ASP A 1 2255 ? 218.545 244.355 227.974 1.00 10.39  ? 2255 ASP A CG    1 
ATOM   5708  O  OD1   . ASP A 1 2255 ? 218.849 243.239 227.503 1.00 7.86   ? 2255 ASP A OD1   1 
ATOM   5709  O  OD2   . ASP A 1 2255 ? 219.312 245.016 228.703 1.00 11.56  ? 2255 ASP A OD2   1 
ATOM   5710  N  N     . PRO A 1 2256 ? 216.659 242.926 224.660 1.00 7.31   ? 2256 PRO A N     1 
ATOM   5711  C  CA    . PRO A 1 2256 ? 216.004 241.692 224.198 1.00 6.25   ? 2256 PRO A CA    1 
ATOM   5712  C  C     . PRO A 1 2256 ? 216.131 240.528 225.161 1.00 6.75   ? 2256 PRO A C     1 
ATOM   5713  O  O     . PRO A 1 2256 ? 215.215 239.699 225.238 1.00 8.93   ? 2256 PRO A O     1 
ATOM   5714  C  CB    . PRO A 1 2256 ? 216.717 241.405 222.869 1.00 5.03   ? 2256 PRO A CB    1 
ATOM   5715  C  CG    . PRO A 1 2256 ? 218.048 242.060 223.020 1.00 5.32   ? 2256 PRO A CG    1 
ATOM   5716  C  CD    . PRO A 1 2256 ? 217.795 243.304 223.804 1.00 5.75   ? 2256 PRO A CD    1 
ATOM   5717  N  N     . LYS A 1 2257 ? 217.238 240.429 225.892 1.00 7.68   ? 2257 LYS A N     1 
ATOM   5718  C  CA    . LYS A 1 2257 ? 217.456 239.314 226.800 1.00 5.19   ? 2257 LYS A CA    1 
ATOM   5719  C  C     . LYS A 1 2257 ? 217.037 239.611 228.232 1.00 5.69   ? 2257 LYS A C     1 
ATOM   5720  O  O     . LYS A 1 2257 ? 217.169 238.734 229.091 1.00 9.14   ? 2257 LYS A O     1 
ATOM   5721  C  CB    . LYS A 1 2257 ? 218.928 238.894 226.769 1.00 5.87   ? 2257 LYS A CB    1 
ATOM   5722  C  CG    . LYS A 1 2257 ? 219.438 238.594 225.373 1.00 4.40   ? 2257 LYS A CG    1 
ATOM   5723  C  CD    . LYS A 1 2257 ? 219.261 237.128 225.033 1.00 5.93   ? 2257 LYS A CD    1 
ATOM   5724  C  CE    . LYS A 1 2257 ? 220.394 236.298 225.596 1.00 5.76   ? 2257 LYS A CE    1 
ATOM   5725  N  NZ    . LYS A 1 2257 ? 220.165 234.843 225.421 1.00 5.29   ? 2257 LYS A NZ    1 
ATOM   5726  N  N     . ALA A 1 2258 ? 216.543 240.816 228.514 1.00 5.47   ? 2258 ALA A N     1 
ATOM   5727  C  CA    . ALA A 1 2258 ? 215.961 241.103 229.817 1.00 5.17   ? 2258 ALA A CA    1 
ATOM   5728  C  C     . ALA A 1 2258 ? 214.544 240.568 229.949 1.00 6.83   ? 2258 ALA A C     1 
ATOM   5729  O  O     . ALA A 1 2258 ? 214.000 240.560 231.057 1.00 10.64  ? 2258 ALA A O     1 
ATOM   5730  C  CB    . ALA A 1 2258 ? 215.967 242.609 230.085 1.00 4.48   ? 2258 ALA A CB    1 
ATOM   5731  N  N     . ILE A 1 2259 ? 213.941 240.127 228.847 1.00 6.17   ? 2259 ILE A N     1 
ATOM   5732  C  CA    . ILE A 1 2259 ? 212.593 239.585 228.829 1.00 6.05   ? 2259 ILE A CA    1 
ATOM   5733  C  C     . ILE A 1 2259 ? 212.608 238.291 228.031 1.00 7.21   ? 2259 ILE A C     1 
ATOM   5734  O  O     . ILE A 1 2259 ? 213.548 238.003 227.286 1.00 8.70   ? 2259 ILE A O     1 
ATOM   5735  C  CB    . ILE A 1 2259 ? 211.576 240.579 228.229 1.00 6.32   ? 2259 ILE A CB    1 
ATOM   5736  C  CG1   . ILE A 1 2259 ? 212.045 241.046 226.850 1.00 5.87   ? 2259 ILE A CG1   1 
ATOM   5737  C  CG2   . ILE A 1 2259 ? 211.376 241.765 229.157 1.00 4.86   ? 2259 ILE A CG2   1 
ATOM   5738  C  CD1   . ILE A 1 2259 ? 211.173 242.116 226.234 1.00 7.29   ? 2259 ILE A CD1   1 
ATOM   5739  N  N     . SER A 1 2260 ? 211.555 237.499 228.205 1.00 7.96   ? 2260 SER A N     1 
ATOM   5740  C  CA    . SER A 1 2260 ? 211.408 236.284 227.419 1.00 5.54   ? 2260 SER A CA    1 
ATOM   5741  C  C     . SER A 1 2260 ? 211.110 236.629 225.965 1.00 9.84   ? 2260 SER A C     1 
ATOM   5742  O  O     . SER A 1 2260 ? 210.568 237.692 225.654 1.00 12.10  ? 2260 SER A O     1 
ATOM   5743  C  CB    . SER A 1 2260 ? 210.297 235.405 227.990 1.00 6.32   ? 2260 SER A CB    1 
ATOM   5744  O  OG    . SER A 1 2260 ? 209.025 235.988 227.776 1.00 9.90   ? 2260 SER A OG    1 
ATOM   5745  N  N     . LYS A 1 2261 ? 211.484 235.715 225.066 1.00 10.49  ? 2261 LYS A N     1 
ATOM   5746  C  CA    . LYS A 1 2261 ? 211.243 235.939 223.644 1.00 6.29   ? 2261 LYS A CA    1 
ATOM   5747  C  C     . LYS A 1 2261 ? 209.755 236.057 223.345 1.00 7.72   ? 2261 LYS A C     1 
ATOM   5748  O  O     . LYS A 1 2261 ? 209.362 236.749 222.399 1.00 8.84   ? 2261 LYS A O     1 
ATOM   5749  C  CB    . LYS A 1 2261 ? 211.867 234.813 222.821 1.00 5.90   ? 2261 LYS A CB    1 
ATOM   5750  C  CG    . LYS A 1 2261 ? 211.892 235.083 221.330 1.00 9.66   ? 2261 LYS A CG    1 
ATOM   5751  C  CD    . LYS A 1 2261 ? 212.642 234.000 220.581 1.00 9.03   ? 2261 LYS A CD    1 
ATOM   5752  C  CE    . LYS A 1 2261 ? 211.749 232.804 220.326 1.00 19.46  ? 2261 LYS A CE    1 
ATOM   5753  N  NZ    . LYS A 1 2261 ? 211.261 232.760 218.919 1.00 27.73  ? 2261 LYS A NZ    1 
ATOM   5754  N  N     . ASP A 1 2262 ? 208.916 235.389 224.140 1.00 9.41   ? 2262 ASP A N     1 
ATOM   5755  C  CA    . ASP A 1 2262 ? 207.473 235.542 223.990 1.00 9.73   ? 2262 ASP A CA    1 
ATOM   5756  C  C     . ASP A 1 2262 ? 207.042 236.974 224.276 1.00 9.25   ? 2262 ASP A C     1 
ATOM   5757  O  O     . ASP A 1 2262 ? 206.167 237.516 223.590 1.00 11.96  ? 2262 ASP A O     1 
ATOM   5758  C  CB    . ASP A 1 2262 ? 206.746 234.564 224.912 1.00 12.94  ? 2262 ASP A CB    1 
ATOM   5759  C  CG    . ASP A 1 2262 ? 206.917 233.123 224.483 1.00 27.85  ? 2262 ASP A CG    1 
ATOM   5760  O  OD1   . ASP A 1 2262 ? 207.083 232.880 223.269 1.00 37.37  ? 2262 ASP A OD1   1 
ATOM   5761  O  OD2   . ASP A 1 2262 ? 206.882 232.230 225.355 1.00 29.56  ? 2262 ASP A OD2   1 
ATOM   5762  N  N     . HIS A 1 2263 ? 207.641 237.602 225.287 1.00 7.25   ? 2263 HIS A N     1 
ATOM   5763  C  CA    . HIS A 1 2263 ? 207.356 239.000 225.577 1.00 6.48   ? 2263 HIS A CA    1 
ATOM   5764  C  C     . HIS A 1 2263 ? 208.010 239.949 224.584 1.00 6.37   ? 2263 HIS A C     1 
ATOM   5765  O  O     . HIS A 1 2263 ? 207.618 241.118 224.514 1.00 8.24   ? 2263 HIS A O     1 
ATOM   5766  C  CB    . HIS A 1 2263 ? 207.814 239.348 226.994 1.00 7.47   ? 2263 HIS A CB    1 
ATOM   5767  C  CG    . HIS A 1 2263 ? 206.963 238.748 228.069 1.00 6.77   ? 2263 HIS A CG    1 
ATOM   5768  N  ND1   . HIS A 1 2263 ? 205.588 238.711 227.995 1.00 6.63   ? 2263 HIS A ND1   1 
ATOM   5769  C  CD2   . HIS A 1 2263 ? 207.292 238.166 229.246 1.00 6.33   ? 2263 HIS A CD2   1 
ATOM   5770  C  CE1   . HIS A 1 2263 ? 205.106 238.129 229.077 1.00 6.12   ? 2263 HIS A CE1   1 
ATOM   5771  N  NE2   . HIS A 1 2263 ? 206.119 237.790 229.852 1.00 8.98   ? 2263 HIS A NE2   1 
ATOM   5772  N  N     . LEU A 1 2264 ? 208.992 239.477 223.817 1.00 6.98   ? 2264 LEU A N     1 
ATOM   5773  C  CA    . LEU A 1 2264 ? 209.693 240.315 222.855 1.00 5.15   ? 2264 LEU A CA    1 
ATOM   5774  C  C     . LEU A 1 2264 ? 209.010 240.334 221.494 1.00 6.73   ? 2264 LEU A C     1 
ATOM   5775  O  O     . LEU A 1 2264 ? 208.904 241.396 220.871 1.00 8.30   ? 2264 LEU A O     1 
ATOM   5776  C  CB    . LEU A 1 2264 ? 211.139 239.837 222.702 1.00 4.96   ? 2264 LEU A CB    1 
ATOM   5777  C  CG    . LEU A 1 2264 ? 212.006 240.543 221.659 1.00 3.60   ? 2264 LEU A CG    1 
ATOM   5778  C  CD1   . LEU A 1 2264 ? 212.188 242.007 222.017 1.00 4.55   ? 2264 LEU A CD1   1 
ATOM   5779  C  CD2   . LEU A 1 2264 ? 213.349 239.851 221.521 1.00 4.58   ? 2264 LEU A CD2   1 
ATOM   5780  N  N     . TYR A 1 2265 ? 208.542 239.182 221.016 1.00 8.13   ? 2265 TYR A N     1 
ATOM   5781  C  CA    . TYR A 1 2265 ? 207.922 239.091 219.700 1.00 7.30   ? 2265 TYR A CA    1 
ATOM   5782  C  C     . TYR A 1 2265 ? 206.419 238.883 219.738 1.00 8.48   ? 2265 TYR A C     1 
ATOM   5783  O  O     . TYR A 1 2265 ? 205.725 239.346 218.834 1.00 10.97  ? 2265 TYR A O     1 
ATOM   5784  C  CB    . TYR A 1 2265 ? 208.555 237.954 218.889 1.00 4.77   ? 2265 TYR A CB    1 
ATOM   5785  C  CG    . TYR A 1 2265 ? 209.967 238.245 218.449 1.00 4.68   ? 2265 TYR A CG    1 
ATOM   5786  C  CD1   . TYR A 1 2265 ? 210.233 239.247 217.528 1.00 4.53   ? 2265 TYR A CD1   1 
ATOM   5787  C  CD2   . TYR A 1 2265 ? 211.034 237.523 218.957 1.00 5.62   ? 2265 TYR A CD2   1 
ATOM   5788  C  CE1   . TYR A 1 2265 ? 211.522 239.519 217.125 1.00 4.19   ? 2265 TYR A CE1   1 
ATOM   5789  C  CE2   . TYR A 1 2265 ? 212.326 237.787 218.560 1.00 4.79   ? 2265 TYR A CE2   1 
ATOM   5790  C  CZ    . TYR A 1 2265 ? 212.565 238.786 217.645 1.00 4.71   ? 2265 TYR A CZ    1 
ATOM   5791  O  OH    . TYR A 1 2265 ? 213.853 239.051 217.244 1.00 9.16   ? 2265 TYR A OH    1 
ATOM   5792  N  N     . GLY A 1 2266 ? 205.900 238.202 220.751 1.00 6.76   ? 2266 GLY A N     1 
ATOM   5793  C  CA    . GLY A 1 2266 ? 204.477 237.959 220.871 1.00 8.53   ? 2266 GLY A CA    1 
ATOM   5794  C  C     . GLY A 1 2266 ? 204.170 236.488 221.066 1.00 11.83  ? 2266 GLY A C     1 
ATOM   5795  O  O     . GLY A 1 2266 ? 205.008 235.609 220.875 1.00 16.39  ? 2266 GLY A O     1 
ATOM   5796  N  N     . THR A 1 2267 ? 202.923 236.241 221.451 1.00 13.03  ? 2267 THR A N     1 
ATOM   5797  C  CA    . THR A 1 2267 ? 202.436 234.900 221.737 1.00 15.33  ? 2267 THR A CA    1 
ATOM   5798  C  C     . THR A 1 2267 ? 201.197 234.602 220.909 1.00 15.12  ? 2267 THR A C     1 
ATOM   5799  O  O     . THR A 1 2267 ? 200.360 235.481 220.680 1.00 16.64  ? 2267 THR A O     1 
ATOM   5800  C  CB    . THR A 1 2267 ? 202.103 234.725 223.225 1.00 19.82  ? 2267 THR A CB    1 
ATOM   5801  O  OG1   . THR A 1 2267 ? 201.066 235.642 223.597 1.00 26.67  ? 2267 THR A OG1   1 
ATOM   5802  C  CG2   . THR A 1 2267 ? 203.324 234.979 224.081 1.00 16.70  ? 2267 THR A CG2   1 
ATOM   5803  N  N     . LEU A 1 2268 ? 201.087 233.358 220.459 1.00 18.45  ? 2268 LEU A N     1 
ATOM   5804  C  CA    . LEU A 1 2268 ? 199.886 232.852 219.811 1.00 26.32  ? 2268 LEU A CA    1 
ATOM   5805  C  C     . LEU A 1 2268 ? 199.209 231.882 220.767 1.00 30.47  ? 2268 LEU A C     1 
ATOM   5806  O  O     . LEU A 1 2268 ? 199.826 230.903 221.200 1.00 26.11  ? 2268 LEU A O     1 
ATOM   5807  C  CB    . LEU A 1 2268 ? 200.217 232.173 218.483 1.00 23.04  ? 2268 LEU A CB    1 
ATOM   5808  C  CG    . LEU A 1 2268 ? 199.031 231.877 217.566 1.00 24.51  ? 2268 LEU A CG    1 
ATOM   5809  C  CD1   . LEU A 1 2268 ? 198.250 233.145 217.279 1.00 22.31  ? 2268 LEU A CD1   1 
ATOM   5810  C  CD2   . LEU A 1 2268 ? 199.505 231.239 216.272 1.00 25.19  ? 2268 LEU A CD2   1 
ATOM   5811  N  N     . ASP A 1 2269 ? 197.956 232.157 221.095 1.00 35.71  ? 2269 ASP A N     1 
ATOM   5812  C  CA    . ASP A 1 2269 ? 197.231 231.342 222.062 1.00 38.26  ? 2269 ASP A CA    1 
ATOM   5813  C  C     . ASP A 1 2269 ? 196.960 229.969 221.461 1.00 46.13  ? 2269 ASP A C     1 
ATOM   5814  O  O     . ASP A 1 2269 ? 196.282 229.878 220.428 1.00 44.42  ? 2269 ASP A O     1 
ATOM   5815  C  CB    . ASP A 1 2269 ? 195.925 232.037 222.442 1.00 38.34  ? 2269 ASP A CB    1 
ATOM   5816  C  CG    . ASP A 1 2269 ? 195.219 231.377 223.610 1.00 44.41  ? 2269 ASP A CG    1 
ATOM   5817  O  OD1   . ASP A 1 2269 ? 195.716 230.357 224.125 1.00 54.24  ? 2269 ASP A OD1   1 
ATOM   5818  O  OD2   . ASP A 1 2269 ? 194.155 231.888 224.015 1.00 52.05  ? 2269 ASP A OD2   1 
ATOM   5819  N  N     . PRO A 1 2270 ? 197.462 228.883 222.058 1.00 42.31  ? 2270 PRO A N     1 
ATOM   5820  C  CA    . PRO A 1 2270 ? 197.214 227.553 221.481 1.00 45.14  ? 2270 PRO A CA    1 
ATOM   5821  C  C     . PRO A 1 2270 ? 195.755 227.144 221.498 1.00 53.76  ? 2270 PRO A C     1 
ATOM   5822  O  O     . PRO A 1 2270 ? 195.378 226.229 220.754 1.00 53.08  ? 2270 PRO A O     1 
ATOM   5823  C  CB    . PRO A 1 2270 ? 198.067 226.625 222.356 1.00 43.25  ? 2270 PRO A CB    1 
ATOM   5824  C  CG    . PRO A 1 2270 ? 198.228 227.360 223.643 1.00 40.01  ? 2270 PRO A CG    1 
ATOM   5825  C  CD    . PRO A 1 2270 ? 198.280 228.815 223.280 1.00 36.78  ? 2270 PRO A CD    1 
ATOM   5826  N  N     . ASN A 1 2271 ? 194.923 227.786 222.316 1.00 53.01  ? 2271 ASN A N     1 
ATOM   5827  C  CA    . ASN A 1 2271 ? 193.516 227.416 222.427 1.00 49.40  ? 2271 ASN A CA    1 
ATOM   5828  C  C     . ASN A 1 2271 ? 192.632 228.270 221.521 1.00 51.83  ? 2271 ASN A C     1 
ATOM   5829  O  O     . ASN A 1 2271 ? 191.890 227.739 220.688 1.00 47.02  ? 2271 ASN A O     1 
ATOM   5830  C  CB    . ASN A 1 2271 ? 193.064 227.532 223.887 1.00 53.57  ? 2271 ASN A CB    1 
ATOM   5831  C  CG    . ASN A 1 2271 ? 194.061 226.925 224.852 1.00 59.67  ? 2271 ASN A CG    1 
ATOM   5832  O  OD1   . ASN A 1 2271 ? 194.434 227.542 225.849 1.00 57.92  ? 2271 ASN A OD1   1 
ATOM   5833  N  ND2   . ASN A 1 2271 ? 194.500 225.706 224.561 1.00 60.90  ? 2271 ASN A ND2   1 
ATOM   5834  N  N     . THR A 1 2272 ? 192.706 229.591 221.668 1.00 51.91  ? 2272 THR A N     1 
ATOM   5835  C  CA    . THR A 1 2272 ? 191.803 230.504 220.978 1.00 45.99  ? 2272 THR A CA    1 
ATOM   5836  C  C     . THR A 1 2272 ? 192.402 231.125 219.724 1.00 45.74  ? 2272 THR A C     1 
ATOM   5837  O  O     . THR A 1 2272 ? 191.722 231.921 219.067 1.00 49.19  ? 2272 THR A O     1 
ATOM   5838  C  CB    . THR A 1 2272 ? 191.357 231.618 221.928 1.00 44.82  ? 2272 THR A CB    1 
ATOM   5839  O  OG1   . THR A 1 2272 ? 192.471 232.467 222.229 1.00 39.07  ? 2272 THR A OG1   1 
ATOM   5840  C  CG2   . THR A 1 2272 ? 190.810 231.029 223.219 1.00 46.98  ? 2272 THR A CG2   1 
ATOM   5841  N  N     . ARG A 1 2273 ? 193.646 230.787 219.377 1.00 45.49  ? 2273 ARG A N     1 
ATOM   5842  C  CA    . ARG A 1 2273 ? 194.307 231.331 218.187 1.00 41.33  ? 2273 ARG A CA    1 
ATOM   5843  C  C     . ARG A 1 2273 ? 194.333 232.858 218.212 1.00 39.26  ? 2273 ARG A C     1 
ATOM   5844  O  O     . ARG A 1 2273 ? 194.171 233.522 217.186 1.00 41.51  ? 2273 ARG A O     1 
ATOM   5845  C  CB    . ARG A 1 2273 ? 193.642 230.822 216.909 1.00 39.43  ? 2273 ARG A CB    1 
ATOM   5846  C  CG    . ARG A 1 2273 ? 193.854 229.347 216.632 1.00 37.49  ? 2273 ARG A CG    1 
ATOM   5847  C  CD    . ARG A 1 2273 ? 195.286 229.061 216.217 1.00 33.35  ? 2273 ARG A CD    1 
ATOM   5848  N  NE    . ARG A 1 2273 ? 196.037 228.333 217.231 1.00 37.74  ? 2273 ARG A NE    1 
ATOM   5849  C  CZ    . ARG A 1 2273 ? 197.306 227.972 217.102 1.00 32.77  ? 2273 ARG A CZ    1 
ATOM   5850  N  NH1   . ARG A 1 2273 ? 197.992 228.243 216.003 1.00 23.22  ? 2273 ARG A NH1   1 
ATOM   5851  N  NH2   . ARG A 1 2273 ? 197.901 227.319 218.095 1.00 30.87  ? 2273 ARG A NH2   1 
ATOM   5852  N  N     . GLU A 1 2274 ? 194.539 233.420 219.398 1.00 38.18  ? 2274 GLU A N     1 
ATOM   5853  C  CA    . GLU A 1 2274 ? 194.561 234.863 219.589 1.00 33.32  ? 2274 GLU A CA    1 
ATOM   5854  C  C     . GLU A 1 2274 ? 196.005 235.321 219.744 1.00 34.90  ? 2274 GLU A C     1 
ATOM   5855  O  O     . GLU A 1 2274 ? 196.769 234.728 220.514 1.00 32.06  ? 2274 GLU A O     1 
ATOM   5856  C  CB    . GLU A 1 2274 ? 193.727 235.258 220.810 1.00 36.46  ? 2274 GLU A CB    1 
ATOM   5857  C  CG    . GLU A 1 2274 ? 193.483 236.754 220.975 1.00 41.97  ? 2274 GLU A CG    1 
ATOM   5858  C  CD    . GLU A 1 2274 ? 194.626 237.473 221.664 1.00 51.20  ? 2274 GLU A CD    1 
ATOM   5859  O  OE1   . GLU A 1 2274 ? 195.329 236.837 222.477 1.00 46.30  ? 2274 GLU A OE1   1 
ATOM   5860  O  OE2   . GLU A 1 2274 ? 194.816 238.678 221.398 1.00 48.14  ? 2274 GLU A OE2   1 
ATOM   5861  N  N     . TRP A 1 2275 ? 196.375 236.367 219.013 1.00 28.36  ? 2275 TRP A N     1 
ATOM   5862  C  CA    . TRP A 1 2275 ? 197.744 236.863 218.983 1.00 21.70  ? 2275 TRP A CA    1 
ATOM   5863  C  C     . TRP A 1 2275 ? 197.887 238.042 219.936 1.00 22.20  ? 2275 TRP A C     1 
ATOM   5864  O  O     . TRP A 1 2275 ? 197.150 239.028 219.827 1.00 28.21  ? 2275 TRP A O     1 
ATOM   5865  C  CB    . TRP A 1 2275 ? 198.145 237.274 217.565 1.00 18.11  ? 2275 TRP A CB    1 
ATOM   5866  C  CG    . TRP A 1 2275 ? 199.490 237.932 217.492 1.00 16.89  ? 2275 TRP A CG    1 
ATOM   5867  C  CD1   . TRP A 1 2275 ? 199.743 239.267 217.372 1.00 12.77  ? 2275 TRP A CD1   1 
ATOM   5868  C  CD2   . TRP A 1 2275 ? 200.767 237.286 217.543 1.00 16.35  ? 2275 TRP A CD2   1 
ATOM   5869  N  NE1   . TRP A 1 2275 ? 201.096 239.492 217.342 1.00 10.36  ? 2275 TRP A NE1   1 
ATOM   5870  C  CE2   . TRP A 1 2275 ? 201.748 238.292 217.447 1.00 13.44  ? 2275 TRP A CE2   1 
ATOM   5871  C  CE3   . TRP A 1 2275 ? 201.176 235.955 217.657 1.00 14.10  ? 2275 TRP A CE3   1 
ATOM   5872  C  CZ2   . TRP A 1 2275 ? 203.111 238.009 217.463 1.00 12.60  ? 2275 TRP A CZ2   1 
ATOM   5873  C  CZ3   . TRP A 1 2275 ? 202.530 235.676 217.672 1.00 11.30  ? 2275 TRP A CZ3   1 
ATOM   5874  C  CH2   . TRP A 1 2275 ? 203.480 236.697 217.575 1.00 10.30  ? 2275 TRP A CH2   1 
ATOM   5875  N  N     . THR A 1 2276 ? 198.836 237.939 220.862 1.00 17.98  ? 2276 THR A N     1 
ATOM   5876  C  CA    . THR A 1 2276 ? 199.204 239.033 221.748 1.00 17.45  ? 2276 THR A CA    1 
ATOM   5877  C  C     . THR A 1 2276 ? 200.569 239.545 221.314 1.00 16.52  ? 2276 THR A C     1 
ATOM   5878  O  O     . THR A 1 2276 ? 201.531 238.772 221.251 1.00 18.30  ? 2276 THR A O     1 
ATOM   5879  C  CB    . THR A 1 2276 ? 199.238 238.578 223.209 1.00 21.95  ? 2276 THR A CB    1 
ATOM   5880  O  OG1   . THR A 1 2276 ? 197.935 238.135 223.604 1.00 41.44  ? 2276 THR A OG1   1 
ATOM   5881  C  CG2   . THR A 1 2276 ? 199.675 239.720 224.111 1.00 13.24  ? 2276 THR A CG2   1 
ATOM   5882  N  N     . ASP A 1 2277 ? 200.649 240.837 221.011 1.00 11.97  ? 2277 ASP A N     1 
ATOM   5883  C  CA    . ASP A 1 2277 ? 201.889 241.414 220.511 1.00 9.79   ? 2277 ASP A CA    1 
ATOM   5884  C  C     . ASP A 1 2277 ? 202.961 241.439 221.594 1.00 10.15  ? 2277 ASP A C     1 
ATOM   5885  O  O     . ASP A 1 2277 ? 202.675 241.589 222.785 1.00 10.15  ? 2277 ASP A O     1 
ATOM   5886  C  CB    . ASP A 1 2277 ? 201.651 242.832 219.993 1.00 10.66  ? 2277 ASP A CB    1 
ATOM   5887  C  CG    . ASP A 1 2277 ? 201.214 242.859 218.545 1.00 10.36  ? 2277 ASP A CG    1 
ATOM   5888  O  OD1   . ASP A 1 2277 ? 201.564 241.923 217.799 1.00 15.50  ? 2277 ASP A OD1   1 
ATOM   5889  O  OD2   . ASP A 1 2277 ? 200.526 243.821 218.149 1.00 12.50  ? 2277 ASP A OD2   1 
ATOM   5890  N  N     . GLY A 1 2278 ? 204.209 241.288 221.162 1.00 8.95   ? 2278 GLY A N     1 
ATOM   5891  C  CA    . GLY A 1 2278 ? 205.351 241.454 222.034 1.00 6.59   ? 2278 GLY A CA    1 
ATOM   5892  C  C     . GLY A 1 2278 ? 205.758 242.910 222.112 1.00 7.32   ? 2278 GLY A C     1 
ATOM   5893  O  O     . GLY A 1 2278 ? 204.992 243.816 221.781 1.00 9.99   ? 2278 GLY A O     1 
ATOM   5894  N  N     . LEU A 1 2279 ? 206.994 243.135 222.553 1.00 7.31   ? 2279 LEU A N     1 
ATOM   5895  C  CA    . LEU A 1 2279 ? 207.492 244.500 222.695 1.00 5.61   ? 2279 LEU A CA    1 
ATOM   5896  C  C     . LEU A 1 2279 ? 207.909 245.080 221.348 1.00 6.47   ? 2279 LEU A C     1 
ATOM   5897  O  O     . LEU A 1 2279 ? 207.410 246.133 220.928 1.00 9.31   ? 2279 LEU A O     1 
ATOM   5898  C  CB    . LEU A 1 2279 ? 208.660 244.524 223.684 1.00 5.22   ? 2279 LEU A CB    1 
ATOM   5899  C  CG    . LEU A 1 2279 ? 209.294 245.881 223.985 1.00 6.42   ? 2279 LEU A CG    1 
ATOM   5900  C  CD1   . LEU A 1 2279 ? 208.234 246.905 224.353 1.00 6.61   ? 2279 LEU A CD1   1 
ATOM   5901  C  CD2   . LEU A 1 2279 ? 210.310 245.737 225.099 1.00 7.70   ? 2279 LEU A CD2   1 
ATOM   5902  N  N     . PHE A 1 2280 ? 208.828 244.401 220.657 1.00 5.68   ? 2280 PHE A N     1 
ATOM   5903  C  CA    . PHE A 1 2280 ? 209.268 244.872 219.348 1.00 5.91   ? 2280 PHE A CA    1 
ATOM   5904  C  C     . PHE A 1 2280 ? 208.113 244.891 218.357 1.00 6.20   ? 2280 PHE A C     1 
ATOM   5905  O  O     . PHE A 1 2280 ? 207.992 245.822 217.551 1.00 8.22   ? 2280 PHE A O     1 
ATOM   5906  C  CB    . PHE A 1 2280 ? 210.404 243.994 218.823 1.00 5.94   ? 2280 PHE A CB    1 
ATOM   5907  C  CG    . PHE A 1 2280 ? 210.774 244.276 217.396 1.00 5.73   ? 2280 PHE A CG    1 
ATOM   5908  C  CD1   . PHE A 1 2280 ? 211.462 245.430 217.060 1.00 4.34   ? 2280 PHE A CD1   1 
ATOM   5909  C  CD2   . PHE A 1 2280 ? 210.419 243.398 216.388 1.00 4.96   ? 2280 PHE A CD2   1 
ATOM   5910  C  CE1   . PHE A 1 2280 ? 211.797 245.693 215.748 1.00 4.43   ? 2280 PHE A CE1   1 
ATOM   5911  C  CE2   . PHE A 1 2280 ? 210.749 243.660 215.073 1.00 4.17   ? 2280 PHE A CE2   1 
ATOM   5912  C  CZ    . PHE A 1 2280 ? 211.441 244.808 214.754 1.00 5.02   ? 2280 PHE A CZ    1 
ATOM   5913  N  N     . THR A 1 2281 ? 207.261 243.865 218.394 1.00 5.25   ? 2281 THR A N     1 
ATOM   5914  C  CA    . THR A 1 2281 ? 206.109 243.829 217.502 1.00 5.01   ? 2281 THR A CA    1 
ATOM   5915  C  C     . THR A 1 2281 ? 205.169 244.996 217.773 1.00 6.71   ? 2281 THR A C     1 
ATOM   5916  O  O     . THR A 1 2281 ? 204.667 245.626 216.836 1.00 7.69   ? 2281 THR A O     1 
ATOM   5917  C  CB    . THR A 1 2281 ? 205.370 242.499 217.650 1.00 7.75   ? 2281 THR A CB    1 
ATOM   5918  O  OG1   . THR A 1 2281 ? 206.319 241.431 217.734 1.00 12.77  ? 2281 THR A OG1   1 
ATOM   5919  C  CG2   . THR A 1 2281 ? 204.465 242.260 216.455 1.00 6.83   ? 2281 THR A CG2   1 
ATOM   5920  N  N     . HIS A 1 2282 ? 204.926 245.303 219.050 1.00 6.35   ? 2282 HIS A N     1 
ATOM   5921  C  CA    . HIS A 1 2282 ? 204.065 246.433 219.390 1.00 8.23   ? 2282 HIS A CA    1 
ATOM   5922  C  C     . HIS A 1 2282 ? 204.659 247.746 218.900 1.00 8.07   ? 2282 HIS A C     1 
ATOM   5923  O  O     . HIS A 1 2282 ? 203.948 248.581 218.329 1.00 8.86   ? 2282 HIS A O     1 
ATOM   5924  C  CB    . HIS A 1 2282 ? 203.833 246.478 220.901 1.00 11.07  ? 2282 HIS A CB    1 
ATOM   5925  C  CG    . HIS A 1 2282 ? 203.282 247.778 221.395 1.00 14.22  ? 2282 HIS A CG    1 
ATOM   5926  N  ND1   . HIS A 1 2282 ? 201.940 248.083 221.348 1.00 13.63  ? 2282 HIS A ND1   1 
ATOM   5927  C  CD2   . HIS A 1 2282 ? 203.890 248.849 221.958 1.00 15.38  ? 2282 HIS A CD2   1 
ATOM   5928  C  CE1   . HIS A 1 2282 ? 201.745 249.286 221.855 1.00 17.79  ? 2282 HIS A CE1   1 
ATOM   5929  N  NE2   . HIS A 1 2282 ? 202.913 249.773 222.231 1.00 20.48  ? 2282 HIS A NE2   1 
ATOM   5930  N  N     . VAL A 1 2283 ? 205.963 247.944 219.104 1.00 8.02   ? 2283 VAL A N     1 
ATOM   5931  C  CA    . VAL A 1 2283 ? 206.602 249.187 218.676 1.00 8.06   ? 2283 VAL A CA    1 
ATOM   5932  C  C     . VAL A 1 2283 ? 206.533 249.326 217.159 1.00 7.98   ? 2283 VAL A C     1 
ATOM   5933  O  O     . VAL A 1 2283 ? 206.179 250.387 216.627 1.00 12.51  ? 2283 VAL A O     1 
ATOM   5934  C  CB    . VAL A 1 2283 ? 208.054 249.248 219.183 1.00 7.00   ? 2283 VAL A CB    1 
ATOM   5935  C  CG1   . VAL A 1 2283 ? 208.821 250.360 218.484 1.00 7.46   ? 2283 VAL A CG1   1 
ATOM   5936  C  CG2   . VAL A 1 2283 ? 208.081 249.444 220.689 1.00 4.86   ? 2283 VAL A CG2   1 
ATOM   5937  N  N     . LEU A 1 2284 ? 206.860 248.250 216.439 1.00 6.51   ? 2284 LEU A N     1 
ATOM   5938  C  CA    . LEU A 1 2284 ? 206.847 248.299 214.981 1.00 8.02   ? 2284 LEU A CA    1 
ATOM   5939  C  C     . LEU A 1 2284 ? 205.441 248.533 214.445 1.00 8.68   ? 2284 LEU A C     1 
ATOM   5940  O  O     . LEU A 1 2284 ? 205.253 249.308 213.501 1.00 9.58   ? 2284 LEU A O     1 
ATOM   5941  C  CB    . LEU A 1 2284 ? 207.432 247.007 214.409 1.00 6.81   ? 2284 LEU A CB    1 
ATOM   5942  C  CG    . LEU A 1 2284 ? 207.708 246.999 212.906 1.00 7.87   ? 2284 LEU A CG    1 
ATOM   5943  C  CD1   . LEU A 1 2284 ? 208.788 248.008 212.554 1.00 7.44   ? 2284 LEU A CD1   1 
ATOM   5944  C  CD2   . LEU A 1 2284 ? 208.094 245.606 212.436 1.00 6.45   ? 2284 LEU A CD2   1 
ATOM   5945  N  N     . ARG A 1 2285 ? 204.441 247.869 215.029 1.00 8.28   ? 2285 ARG A N     1 
ATOM   5946  C  CA    . ARG A 1 2285 ? 203.066 248.059 214.582 1.00 8.25   ? 2285 ARG A CA    1 
ATOM   5947  C  C     . ARG A 1 2285 ? 202.585 249.477 214.858 1.00 11.36  ? 2285 ARG A C     1 
ATOM   5948  O  O     . ARG A 1 2285 ? 201.880 250.070 214.032 1.00 14.61  ? 2285 ARG A O     1 
ATOM   5949  C  CB    . ARG A 1 2285 ? 202.153 247.033 215.253 1.00 8.44   ? 2285 ARG A CB    1 
ATOM   5950  C  CG    . ARG A 1 2285 ? 200.721 247.061 214.763 1.00 10.50  ? 2285 ARG A CG    1 
ATOM   5951  C  CD    . ARG A 1 2285 ? 199.842 246.139 215.587 1.00 11.13  ? 2285 ARG A CD    1 
ATOM   5952  N  NE    . ARG A 1 2285 ? 200.366 244.781 215.643 1.00 9.39   ? 2285 ARG A NE    1 
ATOM   5953  C  CZ    . ARG A 1 2285 ? 200.236 243.886 214.673 1.00 11.91  ? 2285 ARG A CZ    1 
ATOM   5954  N  NH1   . ARG A 1 2285 ? 199.601 244.172 213.548 1.00 12.70  ? 2285 ARG A NH1   1 
ATOM   5955  N  NH2   . ARG A 1 2285 ? 200.752 242.672 214.838 1.00 12.48  ? 2285 ARG A NH2   1 
ATOM   5956  N  N     . LYS A 1 2286 ? 202.951 250.038 216.014 1.00 13.13  ? 2286 LYS A N     1 
ATOM   5957  C  CA    . LYS A 1 2286 ? 202.587 251.418 216.310 1.00 11.53  ? 2286 LYS A CA    1 
ATOM   5958  C  C     . LYS A 1 2286 ? 203.228 252.378 215.316 1.00 13.85  ? 2286 LYS A C     1 
ATOM   5959  O  O     . LYS A 1 2286 ? 202.591 253.338 214.869 1.00 19.38  ? 2286 LYS A O     1 
ATOM   5960  C  CB    . LYS A 1 2286 ? 202.988 251.770 217.742 1.00 12.56  ? 2286 LYS A CB    1 
ATOM   5961  C  CG    . LYS A 1 2286 ? 203.239 253.248 217.978 1.00 22.48  ? 2286 LYS A CG    1 
ATOM   5962  C  CD    . LYS A 1 2286 ? 203.482 253.538 219.450 1.00 28.42  ? 2286 LYS A CD    1 
ATOM   5963  C  CE    . LYS A 1 2286 ? 202.260 253.194 220.284 1.00 31.47  ? 2286 LYS A CE    1 
ATOM   5964  N  NZ    . LYS A 1 2286 ? 201.054 253.936 219.822 1.00 32.00  ? 2286 LYS A NZ    1 
ATOM   5965  N  N     . ILE A 1 2287 ? 204.492 252.134 214.958 1.00 12.28  ? 2287 ILE A N     1 
ATOM   5966  C  CA    . ILE A 1 2287 ? 205.151 252.976 213.962 1.00 11.93  ? 2287 ILE A CA    1 
ATOM   5967  C  C     . ILE A 1 2287 ? 204.453 252.854 212.612 1.00 13.58  ? 2287 ILE A C     1 
ATOM   5968  O  O     . ILE A 1 2287 ? 204.227 253.856 211.921 1.00 17.16  ? 2287 ILE A O     1 
ATOM   5969  C  CB    . ILE A 1 2287 ? 206.645 252.618 213.862 1.00 12.61  ? 2287 ILE A CB    1 
ATOM   5970  C  CG1   . ILE A 1 2287 ? 207.376 253.005 215.149 1.00 9.10   ? 2287 ILE A CG1   1 
ATOM   5971  C  CG2   . ILE A 1 2287 ? 207.280 253.308 212.667 1.00 10.29  ? 2287 ILE A CG2   1 
ATOM   5972  C  CD1   . ILE A 1 2287 ? 208.818 252.559 215.185 1.00 5.38   ? 2287 ILE A CD1   1 
ATOM   5973  N  N     . ILE A 1 2288 ? 204.100 251.629 212.217 1.00 14.43  ? 2288 ILE A N     1 
ATOM   5974  C  CA    . ILE A 1 2288 ? 203.471 251.411 210.917 1.00 11.88  ? 2288 ILE A CA    1 
ATOM   5975  C  C     . ILE A 1 2288 ? 202.109 252.092 210.851 1.00 16.26  ? 2288 ILE A C     1 
ATOM   5976  O  O     . ILE A 1 2288 ? 201.764 252.721 209.843 1.00 20.69  ? 2288 ILE A O     1 
ATOM   5977  C  CB    . ILE A 1 2288 ? 203.367 249.903 210.623 1.00 8.74   ? 2288 ILE A CB    1 
ATOM   5978  C  CG1   . ILE A 1 2288 ? 204.751 249.321 210.336 1.00 11.35  ? 2288 ILE A CG1   1 
ATOM   5979  C  CG2   . ILE A 1 2288 ? 202.430 249.643 209.458 1.00 10.26  ? 2288 ILE A CG2   1 
ATOM   5980  C  CD1   . ILE A 1 2288 ? 204.824 247.820 210.483 1.00 10.47  ? 2288 ILE A CD1   1 
ATOM   5981  N  N     . ASP A 1 2289 ? 201.313 251.977 211.916 1.00 15.16  ? 2289 ASP A N     1 
ATOM   5982  C  CA    . ASP A 1 2289 ? 200.006 252.627 211.933 1.00 15.83  ? 2289 ASP A CA    1 
ATOM   5983  C  C     . ASP A 1 2289 ? 200.144 254.142 211.852 1.00 20.82  ? 2289 ASP A C     1 
ATOM   5984  O  O     . ASP A 1 2289 ? 199.388 254.804 211.131 1.00 24.39  ? 2289 ASP A O     1 
ATOM   5985  C  CB    . ASP A 1 2289 ? 199.234 252.220 213.187 1.00 19.56  ? 2289 ASP A CB    1 
ATOM   5986  C  CG    . ASP A 1 2289 ? 198.969 250.729 213.249 1.00 30.54  ? 2289 ASP A CG    1 
ATOM   5987  O  OD1   . ASP A 1 2289 ? 199.329 250.018 212.288 1.00 24.62  ? 2289 ASP A OD1   1 
ATOM   5988  O  OD2   . ASP A 1 2289 ? 198.399 250.267 214.259 1.00 40.41  ? 2289 ASP A OD2   1 
ATOM   5989  N  N     . SER A 1 2290 ? 201.107 254.705 212.584 1.00 22.83  ? 2290 SER A N     1 
ATOM   5990  C  CA    . SER A 1 2290 ? 201.423 256.134 212.534 1.00 26.45  ? 2290 SER A CA    1 
ATOM   5991  C  C     . SER A 1 2290 ? 200.193 256.993 212.824 1.00 30.81  ? 2290 SER A C     1 
ATOM   5992  O  O     . SER A 1 2290 ? 199.879 257.938 212.097 1.00 36.34  ? 2290 SER A O     1 
ATOM   5993  C  CB    . SER A 1 2290 ? 202.047 256.509 211.190 1.00 22.78  ? 2290 SER A CB    1 
ATOM   5994  O  OG    . SER A 1 2290 ? 202.113 257.915 211.035 1.00 30.64  ? 2290 SER A OG    1 
ATOM   5995  N  N     . VAL A 1 2291 ? 199.488 256.650 213.903 1.00 30.99  ? 2291 VAL A N     1 
ATOM   5996  C  CA    . VAL A 1 2291 ? 198.341 257.447 214.323 1.00 32.36  ? 2291 VAL A CA    1 
ATOM   5997  C  C     . VAL A 1 2291 ? 198.785 258.857 214.690 1.00 38.74  ? 2291 VAL A C     1 
ATOM   5998  O  O     . VAL A 1 2291 ? 198.137 259.846 214.326 1.00 36.30  ? 2291 VAL A O     1 
ATOM   5999  C  CB    . VAL A 1 2291 ? 197.610 256.755 215.488 1.00 29.70  ? 2291 VAL A CB    1 
ATOM   6000  C  CG1   . VAL A 1 2291 ? 196.713 257.739 216.222 1.00 31.53  ? 2291 VAL A CG1   1 
ATOM   6001  C  CG2   . VAL A 1 2291 ? 196.805 255.572 214.977 1.00 22.33  ? 2291 VAL A CG2   1 
ATOM   6002  N  N     . ARG A 1 2292 ? 199.907 258.973 215.399 1.00 39.99  ? 2292 ARG A N     1 
ATOM   6003  C  CA    . ARG A 1 2292 ? 200.442 260.256 215.846 1.00 39.94  ? 2292 ARG A CA    1 
ATOM   6004  C  C     . ARG A 1 2292 ? 201.614 260.718 214.989 1.00 36.05  ? 2292 ARG A C     1 
ATOM   6005  O  O     . ARG A 1 2292 ? 202.566 261.315 215.497 1.00 40.79  ? 2292 ARG A O     1 
ATOM   6006  C  CB    . ARG A 1 2292 ? 200.851 260.169 217.312 1.00 39.07  ? 2292 ARG A CB    1 
ATOM   6007  C  CG    . ARG A 1 2292 ? 199.687 259.991 218.271 1.00 39.05  ? 2292 ARG A CG    1 
ATOM   6008  C  CD    . ARG A 1 2292 ? 200.168 259.909 219.708 1.00 51.51  ? 2292 ARG A CD    1 
ATOM   6009  N  NE    . ARG A 1 2292 ? 199.069 259.717 220.645 1.00 70.06  ? 2292 ARG A NE    1 
ATOM   6010  C  CZ    . ARG A 1 2292 ? 199.219 259.559 221.953 1.00 67.74  ? 2292 ARG A CZ    1 
ATOM   6011  N  NH1   . ARG A 1 2292 ? 200.416 259.563 222.516 1.00 59.34  ? 2292 ARG A NH1   1 
ATOM   6012  N  NH2   . ARG A 1 2292 ? 198.141 259.391 222.715 1.00 61.78  ? 2292 ARG A NH2   1 
ATOM   6013  N  N     . GLY A 1 2293 ? 201.566 260.457 213.687 1.00 35.63  ? 2293 GLY A N     1 
ATOM   6014  C  CA    . GLY A 1 2293 ? 202.623 260.883 212.785 1.00 31.88  ? 2293 GLY A CA    1 
ATOM   6015  C  C     . GLY A 1 2293 ? 203.961 260.207 213.002 1.00 30.74  ? 2293 GLY A C     1 
ATOM   6016  O  O     . GLY A 1 2293 ? 205.000 260.877 212.973 1.00 28.44  ? 2293 GLY A O     1 
ATOM   6017  N  N     . GLU A 1 2294 ? 203.962 258.890 213.220 1.00 34.93  ? 2294 GLU A N     1 
ATOM   6018  C  CA    . GLU A 1 2294 ? 205.211 258.178 213.466 1.00 27.34  ? 2294 GLU A CA    1 
ATOM   6019  C  C     . GLU A 1 2294 ? 206.042 258.021 212.198 1.00 26.19  ? 2294 GLU A C     1 
ATOM   6020  O  O     . GLU A 1 2294 ? 207.276 258.039 212.266 1.00 25.28  ? 2294 GLU A O     1 
ATOM   6021  C  CB    . GLU A 1 2294 ? 204.919 256.810 214.081 1.00 21.30  ? 2294 GLU A CB    1 
ATOM   6022  C  CG    . GLU A 1 2294 ? 204.903 256.807 215.599 1.00 31.35  ? 2294 GLU A CG    1 
ATOM   6023  C  CD    . GLU A 1 2294 ? 203.521 257.053 216.169 1.00 41.04  ? 2294 GLU A CD    1 
ATOM   6024  O  OE1   . GLU A 1 2294 ? 202.587 257.309 215.381 1.00 37.80  ? 2294 GLU A OE1   1 
ATOM   6025  O  OE2   . GLU A 1 2294 ? 203.366 256.987 217.407 1.00 43.86  ? 2294 GLU A OE2   1 
ATOM   6026  N  N     . LEU A 1 2295 ? 205.396 257.863 211.040 1.00 23.61  ? 2295 LEU A N     1 
ATOM   6027  C  CA    . LEU A 1 2295 ? 206.125 257.681 209.790 1.00 17.72  ? 2295 LEU A CA    1 
ATOM   6028  C  C     . LEU A 1 2295 ? 206.874 258.930 209.351 1.00 19.48  ? 2295 LEU A C     1 
ATOM   6029  O  O     . LEU A 1 2295 ? 207.751 258.832 208.487 1.00 18.83  ? 2295 LEU A O     1 
ATOM   6030  C  CB    . LEU A 1 2295 ? 205.170 257.245 208.677 1.00 16.80  ? 2295 LEU A CB    1 
ATOM   6031  C  CG    . LEU A 1 2295 ? 204.585 255.837 208.783 1.00 15.90  ? 2295 LEU A CG    1 
ATOM   6032  C  CD1   . LEU A 1 2295 ? 203.379 255.687 207.872 1.00 19.61  ? 2295 LEU A CD1   1 
ATOM   6033  C  CD2   . LEU A 1 2295 ? 205.637 254.799 208.458 1.00 12.64  ? 2295 LEU A CD2   1 
ATOM   6034  N  N     . GLN A 1 2296 ? 206.555 260.088 209.917 1.00 23.30  ? 2296 GLN A N     1 
ATOM   6035  C  CA    . GLN A 1 2296 ? 207.230 261.333 209.582 1.00 20.99  ? 2296 GLN A CA    1 
ATOM   6036  C  C     . GLN A 1 2296 ? 208.437 261.596 210.468 1.00 21.80  ? 2296 GLN A C     1 
ATOM   6037  O  O     . GLN A 1 2296 ? 209.074 262.645 210.333 1.00 29.43  ? 2296 GLN A O     1 
ATOM   6038  C  CB    . GLN A 1 2296 ? 206.247 262.504 209.681 1.00 23.78  ? 2296 GLN A CB    1 
ATOM   6039  C  CG    . GLN A 1 2296 ? 205.316 262.632 208.485 1.00 23.17  ? 2296 GLN A CG    1 
ATOM   6040  C  CD    . GLN A 1 2296 ? 204.226 261.578 208.482 1.00 28.47  ? 2296 GLN A CD    1 
ATOM   6041  O  OE1   . GLN A 1 2296 ? 204.144 260.755 207.571 1.00 33.14  ? 2296 GLN A OE1   1 
ATOM   6042  N  NE2   . GLN A 1 2296 ? 203.380 261.597 209.506 1.00 25.54  ? 2296 GLN A NE2   1 
ATOM   6043  N  N     . LYS A 1 2297 ? 208.765 260.670 211.363 1.00 24.11  ? 2297 LYS A N     1 
ATOM   6044  C  CA    . LYS A 1 2297 ? 209.863 260.815 212.304 1.00 19.63  ? 2297 LYS A CA    1 
ATOM   6045  C  C     . LYS A 1 2297 ? 210.915 259.752 212.026 1.00 15.40  ? 2297 LYS A C     1 
ATOM   6046  O  O     . LYS A 1 2297 ? 210.604 258.662 211.540 1.00 16.22  ? 2297 LYS A O     1 
ATOM   6047  C  CB    . LYS A 1 2297 ? 209.364 260.683 213.748 1.00 19.44  ? 2297 LYS A CB    1 
ATOM   6048  C  CG    . LYS A 1 2297 ? 208.111 261.486 214.037 1.00 23.86  ? 2297 LYS A CG    1 
ATOM   6049  C  CD    . LYS A 1 2297 ? 207.994 261.830 215.509 1.00 32.08  ? 2297 LYS A CD    1 
ATOM   6050  C  CE    . LYS A 1 2297 ? 206.536 261.816 215.950 1.00 44.04  ? 2297 LYS A CE    1 
ATOM   6051  N  NZ    . LYS A 1 2297 ? 206.387 261.551 217.405 1.00 39.72  ? 2297 LYS A NZ    1 
ATOM   6052  N  N     . ARG A 1 2298 ? 212.166 260.077 212.338 1.00 13.89  ? 2298 ARG A N     1 
ATOM   6053  C  CA    . ARG A 1 2298 ? 213.257 259.114 212.231 1.00 9.67   ? 2298 ARG A CA    1 
ATOM   6054  C  C     . ARG A 1 2298 ? 213.176 258.164 213.418 1.00 13.36  ? 2298 ARG A C     1 
ATOM   6055  O  O     . ARG A 1 2298 ? 213.498 258.540 214.549 1.00 18.23  ? 2298 ARG A O     1 
ATOM   6056  C  CB    . ARG A 1 2298 ? 214.601 259.834 212.180 1.00 7.41   ? 2298 ARG A CB    1 
ATOM   6057  C  CG    . ARG A 1 2298 ? 215.802 258.946 212.448 1.00 5.67   ? 2298 ARG A CG    1 
ATOM   6058  C  CD    . ARG A 1 2298 ? 217.105 259.719 212.320 1.00 5.58   ? 2298 ARG A CD    1 
ATOM   6059  N  NE    . ARG A 1 2298 ? 217.455 259.989 210.931 1.00 4.60   ? 2298 ARG A NE    1 
ATOM   6060  C  CZ    . ARG A 1 2298 ? 217.271 261.153 210.322 1.00 5.88   ? 2298 ARG A CZ    1 
ATOM   6061  N  NH1   . ARG A 1 2298 ? 216.732 262.185 210.949 1.00 12.47  ? 2298 ARG A NH1   1 
ATOM   6062  N  NH2   . ARG A 1 2298 ? 217.635 261.282 209.051 1.00 5.78   ? 2298 ARG A NH2   1 
ATOM   6063  N  N     . GLN A 1 2299 ? 212.741 256.932 213.168 1.00 10.65  ? 2299 GLN A N     1 
ATOM   6064  C  CA    . GLN A 1 2299 ? 212.527 255.945 214.218 1.00 7.90   ? 2299 GLN A CA    1 
ATOM   6065  C  C     . GLN A 1 2299 ? 213.717 254.998 214.272 1.00 8.73   ? 2299 GLN A C     1 
ATOM   6066  O  O     . GLN A 1 2299 ? 214.069 254.379 213.263 1.00 7.74   ? 2299 GLN A O     1 
ATOM   6067  C  CB    . GLN A 1 2299 ? 211.233 255.169 213.976 1.00 6.77   ? 2299 GLN A CB    1 
ATOM   6068  C  CG    . GLN A 1 2299 ? 210.014 256.044 213.758 1.00 7.20   ? 2299 GLN A CG    1 
ATOM   6069  C  CD    . GLN A 1 2299 ? 209.319 256.405 215.052 1.00 9.66   ? 2299 GLN A CD    1 
ATOM   6070  O  OE1   . GLN A 1 2299 ? 209.751 256.010 216.132 1.00 13.41  ? 2299 GLN A OE1   1 
ATOM   6071  N  NE2   . GLN A 1 2299 ? 208.234 257.161 214.950 1.00 15.75  ? 2299 GLN A NE2   1 
ATOM   6072  N  N     . TRP A 1 2300 ? 214.331 254.884 215.446 1.00 11.09  ? 2300 TRP A N     1 
ATOM   6073  C  CA    . TRP A 1 2300 ? 215.474 254.003 215.658 1.00 5.77   ? 2300 TRP A CA    1 
ATOM   6074  C  C     . TRP A 1 2300 ? 215.130 253.021 216.770 1.00 6.65   ? 2300 TRP A C     1 
ATOM   6075  O  O     . TRP A 1 2300 ? 215.007 253.414 217.934 1.00 9.66   ? 2300 TRP A O     1 
ATOM   6076  C  CB    . TRP A 1 2300 ? 216.730 254.801 216.007 1.00 5.04   ? 2300 TRP A CB    1 
ATOM   6077  C  CG    . TRP A 1 2300 ? 217.375 255.473 214.836 1.00 4.32   ? 2300 TRP A CG    1 
ATOM   6078  C  CD1   . TRP A 1 2300 ? 216.909 255.517 213.557 1.00 5.02   ? 2300 TRP A CD1   1 
ATOM   6079  C  CD2   . TRP A 1 2300 ? 218.613 256.191 214.836 1.00 3.82   ? 2300 TRP A CD2   1 
ATOM   6080  N  NE1   . TRP A 1 2300 ? 217.777 256.223 212.761 1.00 5.02   ? 2300 TRP A NE1   1 
ATOM   6081  C  CE2   . TRP A 1 2300 ? 218.832 256.647 213.523 1.00 5.40   ? 2300 TRP A CE2   1 
ATOM   6082  C  CE3   . TRP A 1 2300 ? 219.557 256.496 215.821 1.00 3.38   ? 2300 TRP A CE3   1 
ATOM   6083  C  CZ2   . TRP A 1 2300 ? 219.954 257.389 213.169 1.00 5.01   ? 2300 TRP A CZ2   1 
ATOM   6084  C  CZ3   . TRP A 1 2300 ? 220.669 257.233 215.467 1.00 3.61   ? 2300 TRP A CZ3   1 
ATOM   6085  C  CH2   . TRP A 1 2300 ? 220.858 257.672 214.153 1.00 4.46   ? 2300 TRP A CH2   1 
ATOM   6086  N  N     . ILE A 1 2301 ? 214.979 251.751 216.415 1.00 4.06   ? 2301 ILE A N     1 
ATOM   6087  C  CA    . ILE A 1 2301 ? 214.753 250.687 217.384 1.00 3.73   ? 2301 ILE A CA    1 
ATOM   6088  C  C     . ILE A 1 2301 ? 216.108 250.075 217.709 1.00 5.20   ? 2301 ILE A C     1 
ATOM   6089  O  O     . ILE A 1 2301 ? 216.692 249.363 216.887 1.00 7.89   ? 2301 ILE A O     1 
ATOM   6090  C  CB    . ILE A 1 2301 ? 213.774 249.632 216.852 1.00 2.93   ? 2301 ILE A CB    1 
ATOM   6091  C  CG1   . ILE A 1 2301 ? 212.450 250.285 216.456 1.00 4.17   ? 2301 ILE A CG1   1 
ATOM   6092  C  CG2   . ILE A 1 2301 ? 213.548 248.549 217.892 1.00 3.04   ? 2301 ILE A CG2   1 
ATOM   6093  C  CD1   . ILE A 1 2301 ? 211.429 249.313 215.915 1.00 4.17   ? 2301 ILE A CD1   1 
ATOM   6094  N  N     . VAL A 1 2302 ? 216.611 250.353 218.908 1.00 2.87   ? 2302 VAL A N     1 
ATOM   6095  C  CA    . VAL A 1 2302 ? 217.914 249.875 219.350 1.00 2.66   ? 2302 VAL A CA    1 
ATOM   6096  C  C     . VAL A 1 2302 ? 217.710 248.657 220.236 1.00 3.42   ? 2302 VAL A C     1 
ATOM   6097  O  O     . VAL A 1 2302 ? 216.856 248.668 221.133 1.00 5.03   ? 2302 VAL A O     1 
ATOM   6098  C  CB    . VAL A 1 2302 ? 218.690 250.973 220.095 1.00 3.54   ? 2302 VAL A CB    1 
ATOM   6099  C  CG1   . VAL A 1 2302 ? 220.151 250.584 220.239 1.00 3.16   ? 2302 VAL A CG1   1 
ATOM   6100  C  CG2   . VAL A 1 2302 ? 218.558 252.302 219.367 1.00 4.53   ? 2302 VAL A CG2   1 
ATOM   6101  N  N     . PHE A 1 2303 ? 218.472 247.601 219.972 1.00 3.75   ? 2303 PHE A N     1 
ATOM   6102  C  CA    . PHE A 1 2303 ? 218.497 246.396 220.795 1.00 2.72   ? 2303 PHE A CA    1 
ATOM   6103  C  C     . PHE A 1 2303 ? 219.786 246.444 221.609 1.00 4.39   ? 2303 PHE A C     1 
ATOM   6104  O  O     . PHE A 1 2303 ? 220.845 246.015 221.149 1.00 6.52   ? 2303 PHE A O     1 
ATOM   6105  C  CB    . PHE A 1 2303 ? 218.421 245.133 219.944 1.00 3.50   ? 2303 PHE A CB    1 
ATOM   6106  C  CG    . PHE A 1 2303 ? 217.052 244.846 219.396 1.00 3.71   ? 2303 PHE A CG    1 
ATOM   6107  C  CD1   . PHE A 1 2303 ? 216.042 244.390 220.222 1.00 4.06   ? 2303 PHE A CD1   1 
ATOM   6108  C  CD2   . PHE A 1 2303 ? 216.785 245.009 218.050 1.00 3.34   ? 2303 PHE A CD2   1 
ATOM   6109  C  CE1   . PHE A 1 2303 ? 214.787 244.119 219.718 1.00 3.94   ? 2303 PHE A CE1   1 
ATOM   6110  C  CE2   . PHE A 1 2303 ? 215.532 244.738 217.541 1.00 4.14   ? 2303 PHE A CE2   1 
ATOM   6111  C  CZ    . PHE A 1 2303 ? 214.533 244.292 218.376 1.00 3.25   ? 2303 PHE A CZ    1 
ATOM   6112  N  N     . ASP A 1 2304 ? 219.690 246.971 222.826 1.00 5.47   ? 2304 ASP A N     1 
ATOM   6113  C  CA    . ASP A 1 2304 ? 220.853 247.130 223.699 1.00 5.29   ? 2304 ASP A CA    1 
ATOM   6114  C  C     . ASP A 1 2304 ? 220.920 245.921 224.622 1.00 8.22   ? 2304 ASP A C     1 
ATOM   6115  O  O     . ASP A 1 2304 ? 220.388 245.926 225.732 1.00 12.65  ? 2304 ASP A O     1 
ATOM   6116  C  CB    . ASP A 1 2304 ? 220.765 248.436 224.478 1.00 7.25   ? 2304 ASP A CB    1 
ATOM   6117  C  CG    . ASP A 1 2304 ? 222.064 248.789 225.174 1.00 10.84  ? 2304 ASP A CG    1 
ATOM   6118  O  OD1   . ASP A 1 2304 ? 223.045 248.032 225.028 1.00 11.00  ? 2304 ASP A OD1   1 
ATOM   6119  O  OD2   . ASP A 1 2304 ? 222.103 249.824 225.870 1.00 13.31  ? 2304 ASP A OD2   1 
ATOM   6120  N  N     . GLY A 1 2305 ? 221.582 244.870 224.156 1.00 6.41   ? 2305 GLY A N     1 
ATOM   6121  C  CA    . GLY A 1 2305 ? 221.701 243.658 224.944 1.00 7.76   ? 2305 GLY A CA    1 
ATOM   6122  C  C     . GLY A 1 2305 ? 222.459 242.604 224.172 1.00 7.40   ? 2305 GLY A C     1 
ATOM   6123  O  O     . GLY A 1 2305 ? 222.973 242.847 223.077 1.00 8.73   ? 2305 GLY A O     1 
ATOM   6124  N  N     . ASP A 1 2306 ? 222.525 241.418 224.768 1.00 7.47   ? 2306 ASP A N     1 
ATOM   6125  C  CA    . ASP A 1 2306 ? 223.211 240.299 224.139 1.00 6.15   ? 2306 ASP A CA    1 
ATOM   6126  C  C     . ASP A 1 2306 ? 222.424 239.785 222.938 1.00 7.59   ? 2306 ASP A C     1 
ATOM   6127  O  O     . ASP A 1 2306 ? 221.194 239.850 222.895 1.00 10.15  ? 2306 ASP A O     1 
ATOM   6128  C  CB    . ASP A 1 2306 ? 223.422 239.170 225.145 1.00 7.44   ? 2306 ASP A CB    1 
ATOM   6129  C  CG    . ASP A 1 2306 ? 224.422 239.532 226.221 1.00 14.42  ? 2306 ASP A CG    1 
ATOM   6130  O  OD1   . ASP A 1 2306 ? 225.330 240.339 225.941 1.00 34.20  ? 2306 ASP A OD1   1 
ATOM   6131  O  OD2   . ASP A 1 2306 ? 224.300 239.009 227.348 1.00 15.23  ? 2306 ASP A OD2   1 
ATOM   6132  N  N     . VAL A 1 2307 ? 223.156 239.266 221.956 1.00 5.67   ? 2307 VAL A N     1 
ATOM   6133  C  CA    . VAL A 1 2307 ? 222.583 238.751 220.719 1.00 5.08   ? 2307 VAL A CA    1 
ATOM   6134  C  C     . VAL A 1 2307 ? 222.888 237.262 220.641 1.00 8.33   ? 2307 VAL A C     1 
ATOM   6135  O  O     . VAL A 1 2307 ? 224.056 236.859 220.704 1.00 15.67  ? 2307 VAL A O     1 
ATOM   6136  C  CB    . VAL A 1 2307 ? 223.133 239.488 219.488 1.00 4.62   ? 2307 VAL A CB    1 
ATOM   6137  C  CG1   . VAL A 1 2307 ? 222.911 238.667 218.231 1.00 7.72   ? 2307 VAL A CG1   1 
ATOM   6138  C  CG2   . VAL A 1 2307 ? 222.482 240.852 219.352 1.00 3.98   ? 2307 VAL A CG2   1 
ATOM   6139  N  N     . ASP A 1 2308 ? 221.847 236.451 220.509 1.00 9.65   ? 2308 ASP A N     1 
ATOM   6140  C  CA    . ASP A 1 2308 ? 221.974 235.023 220.274 1.00 9.49   ? 2308 ASP A CA    1 
ATOM   6141  C  C     . ASP A 1 2308 ? 220.999 234.611 219.182 1.00 10.09  ? 2308 ASP A C     1 
ATOM   6142  O  O     . ASP A 1 2308 ? 220.002 235.299 218.941 1.00 10.70  ? 2308 ASP A O     1 
ATOM   6143  C  CB    . ASP A 1 2308 ? 221.744 234.212 221.564 1.00 7.80   ? 2308 ASP A CB    1 
ATOM   6144  C  CG    . ASP A 1 2308 ? 220.334 234.344 222.136 1.00 9.93   ? 2308 ASP A CG    1 
ATOM   6145  O  OD1   . ASP A 1 2308 ? 219.403 234.798 221.450 1.00 12.30  ? 2308 ASP A OD1   1 
ATOM   6146  O  OD2   . ASP A 1 2308 ? 220.153 233.974 223.313 1.00 12.74  ? 2308 ASP A OD2   1 
ATOM   6147  N  N     . PRO A 1 2309 ? 221.264 233.497 218.490 1.00 8.96   ? 2309 PRO A N     1 
ATOM   6148  C  CA    . PRO A 1 2309 ? 220.394 233.108 217.368 1.00 8.04   ? 2309 PRO A CA    1 
ATOM   6149  C  C     . PRO A 1 2309 ? 218.958 232.809 217.764 1.00 8.70   ? 2309 PRO A C     1 
ATOM   6150  O  O     . PRO A 1 2309 ? 218.094 232.764 216.880 1.00 7.57   ? 2309 PRO A O     1 
ATOM   6151  C  CB    . PRO A 1 2309 ? 221.084 231.859 216.803 1.00 10.93  ? 2309 PRO A CB    1 
ATOM   6152  C  CG    . PRO A 1 2309 ? 221.959 231.366 217.902 1.00 12.07  ? 2309 PRO A CG    1 
ATOM   6153  C  CD    . PRO A 1 2309 ? 222.409 232.584 218.637 1.00 8.16   ? 2309 PRO A CD    1 
ATOM   6154  N  N     . GLU A 1 2310 ? 218.672 232.595 219.050 1.00 11.88  ? 2310 GLU A N     1 
ATOM   6155  C  CA    . GLU A 1 2310 ? 217.308 232.278 219.457 1.00 10.93  ? 2310 GLU A CA    1 
ATOM   6156  C  C     . GLU A 1 2310 ? 216.350 233.431 219.179 1.00 11.96  ? 2310 GLU A C     1 
ATOM   6157  O  O     . GLU A 1 2310 ? 215.230 233.209 218.704 1.00 21.87  ? 2310 GLU A O     1 
ATOM   6158  C  CB    . GLU A 1 2310 ? 217.276 231.900 220.935 1.00 16.73  ? 2310 GLU A CB    1 
ATOM   6159  C  CG    . GLU A 1 2310 ? 217.984 230.597 221.252 1.00 24.96  ? 2310 GLU A CG    1 
ATOM   6160  C  CD    . GLU A 1 2310 ? 217.234 229.388 220.734 1.00 36.63  ? 2310 GLU A CD    1 
ATOM   6161  O  OE1   . GLU A 1 2310 ? 215.987 229.386 220.809 1.00 41.92  ? 2310 GLU A OE1   1 
ATOM   6162  O  OE2   . GLU A 1 2310 ? 217.889 228.441 220.251 1.00 34.72  ? 2310 GLU A OE2   1 
ATOM   6163  N  N     . TRP A 1 2311 ? 216.761 234.668 219.465 1.00 7.98   ? 2311 TRP A N     1 
ATOM   6164  C  CA    . TRP A 1 2311 ? 215.864 235.805 219.297 1.00 6.06   ? 2311 TRP A CA    1 
ATOM   6165  C  C     . TRP A 1 2311 ? 216.175 236.660 218.077 1.00 5.30   ? 2311 TRP A C     1 
ATOM   6166  O  O     . TRP A 1 2311 ? 215.246 237.200 217.469 1.00 7.18   ? 2311 TRP A O     1 
ATOM   6167  C  CB    . TRP A 1 2311 ? 215.872 236.691 220.556 1.00 4.53   ? 2311 TRP A CB    1 
ATOM   6168  C  CG    . TRP A 1 2311 ? 217.064 237.603 220.693 1.00 4.70   ? 2311 TRP A CG    1 
ATOM   6169  C  CD1   . TRP A 1 2311 ? 218.182 237.375 221.434 1.00 4.17   ? 2311 TRP A CD1   1 
ATOM   6170  C  CD2   . TRP A 1 2311 ? 217.240 238.892 220.092 1.00 6.11   ? 2311 TRP A CD2   1 
ATOM   6171  N  NE1   . TRP A 1 2311 ? 219.052 238.428 221.319 1.00 4.54   ? 2311 TRP A NE1   1 
ATOM   6172  C  CE2   . TRP A 1 2311 ? 218.497 239.375 220.500 1.00 3.71   ? 2311 TRP A CE2   1 
ATOM   6173  C  CE3   . TRP A 1 2311 ? 216.462 239.681 219.240 1.00 3.33   ? 2311 TRP A CE3   1 
ATOM   6174  C  CZ2   . TRP A 1 2311 ? 218.992 240.605 220.089 1.00 3.01   ? 2311 TRP A CZ2   1 
ATOM   6175  C  CZ3   . TRP A 1 2311 ? 216.956 240.901 218.833 1.00 2.78   ? 2311 TRP A CZ3   1 
ATOM   6176  C  CH2   . TRP A 1 2311 ? 218.207 241.353 219.260 1.00 3.42   ? 2311 TRP A CH2   1 
ATOM   6177  N  N     . VAL A 1 2312 ? 217.445 236.800 217.691 1.00 5.10   ? 2312 VAL A N     1 
ATOM   6178  C  CA    . VAL A 1 2312 ? 217.771 237.742 216.624 1.00 4.47   ? 2312 VAL A CA    1 
ATOM   6179  C  C     . VAL A 1 2312 ? 217.455 237.175 215.244 1.00 7.01   ? 2312 VAL A C     1 
ATOM   6180  O  O     . VAL A 1 2312 ? 217.208 237.946 214.309 1.00 9.23   ? 2312 VAL A O     1 
ATOM   6181  C  CB    . VAL A 1 2312 ? 219.247 238.174 216.704 1.00 3.61   ? 2312 VAL A CB    1 
ATOM   6182  C  CG1   . VAL A 1 2312 ? 220.176 237.013 216.397 1.00 6.14   ? 2312 VAL A CG1   1 
ATOM   6183  C  CG2   . VAL A 1 2312 ? 219.519 239.371 215.803 1.00 3.15   ? 2312 VAL A CG2   1 
ATOM   6184  N  N     . GLU A 1 2313 ? 217.437 235.849 215.089 1.00 5.77   ? 2313 GLU A N     1 
ATOM   6185  C  CA    . GLU A 1 2313 ? 217.121 235.261 213.794 1.00 5.34   ? 2313 GLU A CA    1 
ATOM   6186  C  C     . GLU A 1 2313 ? 215.686 235.535 213.369 1.00 7.21   ? 2313 GLU A C     1 
ATOM   6187  O  O     . GLU A 1 2313 ? 215.399 235.526 212.166 1.00 10.11  ? 2313 GLU A O     1 
ATOM   6188  C  CB    . GLU A 1 2313 ? 217.382 233.756 213.820 1.00 7.14   ? 2313 GLU A CB    1 
ATOM   6189  C  CG    . GLU A 1 2313 ? 218.851 233.391 213.899 1.00 10.47  ? 2313 GLU A CG    1 
ATOM   6190  C  CD    . GLU A 1 2313 ? 219.503 233.310 212.539 1.00 18.01  ? 2313 GLU A CD    1 
ATOM   6191  O  OE1   . GLU A 1 2313 ? 218.850 232.818 211.596 1.00 20.85  ? 2313 GLU A OE1   1 
ATOM   6192  O  OE2   . GLU A 1 2313 ? 220.669 233.736 212.411 1.00 19.85  ? 2313 GLU A OE2   1 
ATOM   6193  N  N     . ASN A 1 2314 ? 214.786 235.803 214.317 1.00 7.31   ? 2314 ASN A N     1 
ATOM   6194  C  CA    . ASN A 1 2314 ? 213.436 236.226 213.967 1.00 4.65   ? 2314 ASN A CA    1 
ATOM   6195  C  C     . ASN A 1 2314 ? 213.427 237.522 213.175 1.00 6.89   ? 2314 ASN A C     1 
ATOM   6196  O  O     . ASN A 1 2314 ? 212.428 237.820 212.513 1.00 13.95  ? 2314 ASN A O     1 
ATOM   6197  C  CB    . ASN A 1 2314 ? 212.584 236.397 215.225 1.00 5.73   ? 2314 ASN A CB    1 
ATOM   6198  C  CG    . ASN A 1 2314 ? 212.127 235.077 215.809 1.00 8.36   ? 2314 ASN A CG    1 
ATOM   6199  O  OD1   . ASN A 1 2314 ? 212.932 234.184 216.061 1.00 10.11  ? 2314 ASN A OD1   1 
ATOM   6200  N  ND2   . ASN A 1 2314 ? 210.826 234.953 216.032 1.00 6.09   ? 2314 ASN A ND2   1 
ATOM   6201  N  N     . LEU A 1 2315 ? 214.508 238.296 213.230 1.00 7.24   ? 2315 LEU A N     1 
ATOM   6202  C  CA    . LEU A 1 2315 ? 214.643 239.532 212.479 1.00 6.01   ? 2315 LEU A CA    1 
ATOM   6203  C  C     . LEU A 1 2315 ? 215.316 239.328 211.130 1.00 6.64   ? 2315 LEU A C     1 
ATOM   6204  O  O     . LEU A 1 2315 ? 215.589 240.313 210.437 1.00 9.43   ? 2315 LEU A O     1 
ATOM   6205  C  CB    . LEU A 1 2315 ? 215.432 240.558 213.293 1.00 5.71   ? 2315 LEU A CB    1 
ATOM   6206  C  CG    . LEU A 1 2315 ? 214.881 240.935 214.666 1.00 5.79   ? 2315 LEU A CG    1 
ATOM   6207  C  CD1   . LEU A 1 2315 ? 215.821 241.903 215.359 1.00 5.14   ? 2315 LEU A CD1   1 
ATOM   6208  C  CD2   . LEU A 1 2315 ? 213.494 241.532 214.535 1.00 5.75   ? 2315 LEU A CD2   1 
ATOM   6209  N  N     . ASN A 1 2316 ? 215.601 238.078 210.747 1.00 6.13   ? 2316 ASN A N     1 
ATOM   6210  C  CA    . ASN A 1 2316 ? 216.321 237.835 209.499 1.00 7.27   ? 2316 ASN A CA    1 
ATOM   6211  C  C     . ASN A 1 2316 ? 215.589 238.443 208.311 1.00 7.24   ? 2316 ASN A C     1 
ATOM   6212  O  O     . ASN A 1 2316 ? 216.158 239.246 207.562 1.00 10.49  ? 2316 ASN A O     1 
ATOM   6213  C  CB    . ASN A 1 2316 ? 216.526 236.334 209.294 1.00 7.36   ? 2316 ASN A CB    1 
ATOM   6214  C  CG    . ASN A 1 2316 ? 217.717 235.797 210.061 1.00 5.56   ? 2316 ASN A CG    1 
ATOM   6215  O  OD1   . ASN A 1 2316 ? 218.391 236.532 210.782 1.00 7.46   ? 2316 ASN A OD1   1 
ATOM   6216  N  ND2   . ASN A 1 2316 ? 217.985 234.509 209.905 1.00 6.67   ? 2316 ASN A ND2   1 
ATOM   6217  N  N     . SER A 1 2317 ? 214.306 238.108 208.150 1.00 7.57   ? 2317 SER A N     1 
ATOM   6218  C  CA    . SER A 1 2317 ? 213.523 238.699 207.071 1.00 7.26   ? 2317 SER A CA    1 
ATOM   6219  C  C     . SER A 1 2317 ? 213.399 240.207 207.239 1.00 7.14   ? 2317 SER A C     1 
ATOM   6220  O  O     . SER A 1 2317 ? 213.232 240.931 206.252 1.00 9.42   ? 2317 SER A O     1 
ATOM   6221  C  CB    . SER A 1 2317 ? 212.140 238.055 207.009 1.00 8.74   ? 2317 SER A CB    1 
ATOM   6222  O  OG    . SER A 1 2317 ? 211.497 238.105 208.269 1.00 12.22  ? 2317 SER A OG    1 
ATOM   6223  N  N     . VAL A 1 2318 ? 213.474 240.694 208.479 1.00 8.55   ? 2318 VAL A N     1 
ATOM   6224  C  CA    . VAL A 1 2318 ? 213.480 242.133 208.716 1.00 7.82   ? 2318 VAL A CA    1 
ATOM   6225  C  C     . VAL A 1 2318 ? 214.766 242.752 208.183 1.00 8.93   ? 2318 VAL A C     1 
ATOM   6226  O  O     . VAL A 1 2318 ? 214.755 243.841 207.598 1.00 13.30  ? 2318 VAL A O     1 
ATOM   6227  C  CB    . VAL A 1 2318 ? 213.291 242.429 210.214 1.00 5.99   ? 2318 VAL A CB    1 
ATOM   6228  C  CG1   . VAL A 1 2318 ? 213.282 243.929 210.465 1.00 4.89   ? 2318 VAL A CG1   1 
ATOM   6229  C  CG2   . VAL A 1 2318 ? 212.012 241.791 210.721 1.00 5.13   ? 2318 VAL A CG2   1 
ATOM   6230  N  N     . LEU A 1 2319 ? 215.904 242.110 208.462 1.00 8.76   ? 2319 LEU A N     1 
ATOM   6231  C  CA    . LEU A 1 2319 ? 217.211 242.719 208.093 1.00 8.12   ? 2319 LEU A CA    1 
ATOM   6232  C  C     . LEU A 1 2319 ? 217.631 242.300 206.679 1.00 10.30  ? 2319 LEU A C     1 
ATOM   6233  O  O     . LEU A 1 2319 ? 218.783 242.588 206.297 1.00 18.42  ? 2319 LEU A O     1 
ATOM   6234  C  CB    . LEU A 1 2319 ? 218.239 242.291 209.140 1.00 10.82  ? 2319 LEU A CB    1 
ATOM   6235  C  CG    . LEU A 1 2319 ? 217.849 242.551 210.598 1.00 9.43   ? 2319 LEU A CG    1 
ATOM   6236  C  CD1   . LEU A 1 2319 ? 218.860 241.936 211.547 1.00 9.28   ? 2319 LEU A CD1   1 
ATOM   6237  C  CD2   . LEU A 1 2319 ? 217.701 244.038 210.860 1.00 7.51   ? 2319 LEU A CD2   1 
ATOM   6238  N  N     . ASP A 1 2320 ? 216.721 241.660 205.942 1.00 11.68  ? 2320 ASP A N     1 
ATOM   6239  C  CA    . ASP A 1 2320 ? 217.014 241.231 204.549 1.00 9.54   ? 2320 ASP A CA    1 
ATOM   6240  C  C     . ASP A 1 2320 ? 216.307 242.175 203.575 1.00 12.51  ? 2320 ASP A C     1 
ATOM   6241  O  O     . ASP A 1 2320 ? 215.679 243.150 204.040 1.00 13.45  ? 2320 ASP A O     1 
ATOM   6242  C  CB    . ASP A 1 2320 ? 216.593 239.790 204.319 1.00 10.58  ? 2320 ASP A CB    1 
ATOM   6243  C  CG    . ASP A 1 2320 ? 217.727 238.779 204.245 1.00 19.38  ? 2320 ASP A CG    1 
ATOM   6244  O  OD1   . ASP A 1 2320 ? 218.899 239.209 204.279 1.00 26.91  ? 2320 ASP A OD1   1 
ATOM   6245  O  OD2   . ASP A 1 2320 ? 217.427 237.570 204.174 1.00 20.98  ? 2320 ASP A OD2   1 
ATOM   6246  N  N     . ASP A 1 2321 ? 216.402 241.890 202.276 1.00 15.19  ? 2321 ASP A N     1 
ATOM   6247  C  CA    . ASP A 1 2321 ? 215.711 242.723 201.256 1.00 16.85  ? 2321 ASP A CA    1 
ATOM   6248  C  C     . ASP A 1 2321 ? 214.208 242.694 201.539 1.00 16.20  ? 2321 ASP A C     1 
ATOM   6249  O  O     . ASP A 1 2321 ? 213.519 243.674 201.185 1.00 17.44  ? 2321 ASP A O     1 
ATOM   6250  C  CB    . ASP A 1 2321 ? 216.029 242.239 199.851 1.00 23.26  ? 2321 ASP A CB    1 
ATOM   6251  C  CG    . ASP A 1 2321 ? 217.493 241.919 199.580 1.00 38.20  ? 2321 ASP A CG    1 
ATOM   6252  O  OD1   . ASP A 1 2321 ? 217.801 241.500 198.445 1.00 29.47  ? 2321 ASP A OD1   1 
ATOM   6253  O  OD2   . ASP A 1 2321 ? 218.312 242.089 200.507 1.00 37.24  ? 2321 ASP A OD2   1 
ATOM   6254  N  N     . ASN A 1 2322 ? 213.722 241.617 202.162 1.00 14.64  ? 2322 ASN A N     1 
ATOM   6255  C  CA    . ASN A 1 2322 ? 212.263 241.466 202.416 1.00 12.09  ? 2322 ASN A CA    1 
ATOM   6256  C  C     . ASN A 1 2322 ? 211.759 242.604 203.305 1.00 11.64  ? 2322 ASN A C     1 
ATOM   6257  O  O     . ASN A 1 2322 ? 210.579 242.982 203.157 1.00 16.24  ? 2322 ASN A O     1 
ATOM   6258  C  CB    . ASN A 1 2322 ? 211.954 240.113 203.046 1.00 10.32  ? 2322 ASN A CB    1 
ATOM   6259  C  CG    . ASN A 1 2322 ? 212.714 238.992 202.379 1.00 14.61  ? 2322 ASN A CG    1 
ATOM   6260  O  OD1   . ASN A 1 2322 ? 212.550 238.759 201.177 1.00 20.18  ? 2322 ASN A OD1   1 
ATOM   6261  N  ND2   . ASN A 1 2322 ? 213.547 238.292 203.135 1.00 11.83  ? 2322 ASN A ND2   1 
ATOM   6262  N  N     . LYS A 1 2323 ? 212.611 243.130 204.188 1.00 11.85  ? 2323 LYS A N     1 
ATOM   6263  C  CA    . LYS A 1 2323 ? 212.186 244.168 205.128 1.00 10.12  ? 2323 LYS A CA    1 
ATOM   6264  C  C     . LYS A 1 2323 ? 210.790 243.869 205.664 1.00 7.72   ? 2323 LYS A C     1 
ATOM   6265  O  O     . LYS A 1 2323 ? 209.890 244.710 205.654 1.00 11.45  ? 2323 LYS A O     1 
ATOM   6266  C  CB    . LYS A 1 2323 ? 212.245 245.554 204.488 1.00 9.23   ? 2323 LYS A CB    1 
ATOM   6267  C  CG    . LYS A 1 2323 ? 213.644 246.005 204.119 1.00 8.36   ? 2323 LYS A CG    1 
ATOM   6268  C  CD    . LYS A 1 2323 ? 213.630 247.400 203.521 1.00 8.15   ? 2323 LYS A CD    1 
ATOM   6269  C  CE    . LYS A 1 2323 ? 214.841 247.632 202.636 1.00 11.64  ? 2323 LYS A CE    1 
ATOM   6270  N  NZ    . LYS A 1 2323 ? 215.438 248.975 202.859 1.00 9.42   ? 2323 LYS A NZ    1 
ATOM   6271  N  N     . LEU A 1 2324 ? 210.615 242.637 206.134 1.00 6.22   ? 2324 LEU A N     1 
ATOM   6272  C  CA    . LEU A 1 2324 ? 209.312 242.146 206.554 1.00 7.87   ? 2324 LEU A CA    1 
ATOM   6273  C  C     . LEU A 1 2324 ? 209.461 241.327 207.825 1.00 8.31   ? 2324 LEU A C     1 
ATOM   6274  O  O     . LEU A 1 2324 ? 210.366 240.496 207.928 1.00 12.43  ? 2324 LEU A O     1 
ATOM   6275  C  CB    . LEU A 1 2324 ? 208.673 241.298 205.450 1.00 7.40   ? 2324 LEU A CB    1 
ATOM   6276  C  CG    . LEU A 1 2324 ? 207.161 241.093 205.485 1.00 9.55   ? 2324 LEU A CG    1 
ATOM   6277  C  CD1   . LEU A 1 2324 ? 206.441 242.346 205.030 1.00 10.75  ? 2324 LEU A CD1   1 
ATOM   6278  C  CD2   . LEU A 1 2324 ? 206.789 239.920 204.605 1.00 9.26   ? 2324 LEU A CD2   1 
ATOM   6279  N  N     . LEU A 1 2325 ? 208.577 241.565 208.787 1.00 5.92   ? 2325 LEU A N     1 
ATOM   6280  C  CA    . LEU A 1 2325 ? 208.492 240.762 209.999 1.00 6.39   ? 2325 LEU A CA    1 
ATOM   6281  C  C     . LEU A 1 2325 ? 207.304 239.822 209.860 1.00 8.79   ? 2325 LEU A C     1 
ATOM   6282  O  O     . LEU A 1 2325 ? 206.161 240.278 209.732 1.00 13.61  ? 2325 LEU A O     1 
ATOM   6283  C  CB    . LEU A 1 2325 ? 208.341 241.645 211.237 1.00 6.90   ? 2325 LEU A CB    1 
ATOM   6284  C  CG    . LEU A 1 2325 ? 208.156 240.915 212.568 1.00 4.96   ? 2325 LEU A CG    1 
ATOM   6285  C  CD1   . LEU A 1 2325 ? 209.469 240.312 213.033 1.00 3.80   ? 2325 LEU A CD1   1 
ATOM   6286  C  CD2   . LEU A 1 2325 ? 207.587 241.846 213.623 1.00 7.18   ? 2325 LEU A CD2   1 
ATOM   6287  N  N     . THR A 1 2326 ? 207.576 238.523 209.871 1.00 7.59   ? 2326 THR A N     1 
ATOM   6288  C  CA    . THR A 1 2326 ? 206.551 237.501 209.717 1.00 10.21  ? 2326 THR A CA    1 
ATOM   6289  C  C     . THR A 1 2326 ? 206.279 236.848 211.064 1.00 9.14   ? 2326 THR A C     1 
ATOM   6290  O  O     . THR A 1 2326 ? 207.210 236.422 211.755 1.00 7.64   ? 2326 THR A O     1 
ATOM   6291  C  CB    . THR A 1 2326 ? 206.974 236.444 208.694 1.00 9.17   ? 2326 THR A CB    1 
ATOM   6292  O  OG1   . THR A 1 2326 ? 207.919 235.549 209.292 1.00 8.34   ? 2326 THR A OG1   1 
ATOM   6293  C  CG2   . THR A 1 2326 ? 207.604 237.100 207.477 1.00 6.20   ? 2326 THR A CG2   1 
ATOM   6294  N  N     . LEU A 1 2327 ? 205.009 236.776 211.432 1.00 9.28   ? 2327 LEU A N     1 
ATOM   6295  C  CA    . LEU A 1 2327 ? 204.573 236.189 212.684 1.00 10.08  ? 2327 LEU A CA    1 
ATOM   6296  C  C     . LEU A 1 2327 ? 203.898 234.847 212.434 1.00 11.57  ? 2327 LEU A C     1 
ATOM   6297  O  O     . LEU A 1 2327 ? 203.386 234.592 211.340 1.00 16.01  ? 2327 LEU A O     1 
ATOM   6298  C  CB    . LEU A 1 2327 ? 203.608 237.135 213.411 1.00 11.83  ? 2327 LEU A CB    1 
ATOM   6299  C  CG    . LEU A 1 2327 ? 204.132 238.555 213.636 1.00 9.00   ? 2327 LEU A CG    1 
ATOM   6300  C  CD1   . LEU A 1 2327 ? 203.015 239.476 214.092 1.00 10.99  ? 2327 LEU A CD1   1 
ATOM   6301  C  CD2   . LEU A 1 2327 ? 205.277 238.552 214.635 1.00 7.49   ? 2327 LEU A CD2   1 
ATOM   6302  N  N     . PRO A 1 2328 ? 203.893 233.953 213.428 1.00 9.98   ? 2328 PRO A N     1 
ATOM   6303  C  CA    . PRO A 1 2328 ? 203.282 232.630 213.215 1.00 12.77  ? 2328 PRO A CA    1 
ATOM   6304  C  C     . PRO A 1 2328 ? 201.809 232.687 212.850 1.00 15.90  ? 2328 PRO A C     1 
ATOM   6305  O  O     . PRO A 1 2328 ? 201.313 231.771 212.183 1.00 17.86  ? 2328 PRO A O     1 
ATOM   6306  C  CB    . PRO A 1 2328 ? 203.504 231.919 214.558 1.00 12.06  ? 2328 PRO A CB    1 
ATOM   6307  C  CG    . PRO A 1 2328 ? 203.842 232.998 215.532 1.00 11.88  ? 2328 PRO A CG    1 
ATOM   6308  C  CD    . PRO A 1 2328 ? 204.534 234.056 214.747 1.00 8.94   ? 2328 PRO A CD    1 
ATOM   6309  N  N     . ASN A 1 2329 ? 201.093 233.732 213.257 1.00 12.53  ? 2329 ASN A N     1 
ATOM   6310  C  CA    . ASN A 1 2329 ? 199.677 233.865 212.937 1.00 10.21  ? 2329 ASN A CA    1 
ATOM   6311  C  C     . ASN A 1 2329 ? 199.429 234.314 211.502 1.00 15.19  ? 2329 ASN A C     1 
ATOM   6312  O  O     . ASN A 1 2329 ? 198.291 234.656 211.164 1.00 15.27  ? 2329 ASN A O     1 
ATOM   6313  C  CB    . ASN A 1 2329 ? 199.008 234.836 213.914 1.00 15.47  ? 2329 ASN A CB    1 
ATOM   6314  C  CG    . ASN A 1 2329 ? 199.312 236.285 213.598 1.00 17.54  ? 2329 ASN A CG    1 
ATOM   6315  O  OD1   . ASN A 1 2329 ? 200.451 236.644 213.306 1.00 14.70  ? 2329 ASN A OD1   1 
ATOM   6316  N  ND2   . ASN A 1 2329 ? 198.289 237.129 213.660 1.00 19.37  ? 2329 ASN A ND2   1 
ATOM   6317  N  N     . GLY A 1 2330 ? 200.457 234.317 210.654 1.00 15.15  ? 2330 GLY A N     1 
ATOM   6318  C  CA    . GLY A 1 2330 ? 200.310 234.682 209.263 1.00 11.29  ? 2330 GLY A CA    1 
ATOM   6319  C  C     . GLY A 1 2330 ? 200.390 236.162 208.972 1.00 14.09  ? 2330 GLY A C     1 
ATOM   6320  O  O     . GLY A 1 2330 ? 200.332 236.549 207.799 1.00 17.33  ? 2330 GLY A O     1 
ATOM   6321  N  N     . GLU A 1 2331 ? 200.524 237.000 209.994 1.00 16.22  ? 2331 GLU A N     1 
ATOM   6322  C  CA    . GLU A 1 2331 ? 200.603 238.438 209.790 1.00 16.02  ? 2331 GLU A CA    1 
ATOM   6323  C  C     . GLU A 1 2331 ? 202.012 238.836 209.369 1.00 13.34  ? 2331 GLU A C     1 
ATOM   6324  O  O     . GLU A 1 2331 ? 203.003 238.319 209.892 1.00 14.90  ? 2331 GLU A O     1 
ATOM   6325  C  CB    . GLU A 1 2331 ? 200.204 239.175 211.067 1.00 19.12  ? 2331 GLU A CB    1 
ATOM   6326  C  CG    . GLU A 1 2331 ? 199.923 240.652 210.878 1.00 24.75  ? 2331 GLU A CG    1 
ATOM   6327  C  CD    . GLU A 1 2331 ? 199.115 241.233 212.018 1.00 39.71  ? 2331 GLU A CD    1 
ATOM   6328  O  OE1   . GLU A 1 2331 ? 199.054 240.592 213.089 1.00 36.08  ? 2331 GLU A OE1   1 
ATOM   6329  O  OE2   . GLU A 1 2331 ? 198.539 242.328 211.845 1.00 46.41  ? 2331 GLU A OE2   1 
ATOM   6330  N  N     . ARG A 1 2332 ? 202.093 239.754 208.410 1.00 15.23  ? 2332 ARG A N     1 
ATOM   6331  C  CA    . ARG A 1 2332 ? 203.364 240.258 207.909 1.00 12.80  ? 2332 ARG A CA    1 
ATOM   6332  C  C     . ARG A 1 2332 ? 203.363 241.775 207.993 1.00 12.04  ? 2332 ARG A C     1 
ATOM   6333  O  O     . ARG A 1 2332 ? 202.465 242.428 207.453 1.00 12.02  ? 2332 ARG A O     1 
ATOM   6334  C  CB    . ARG A 1 2332 ? 203.612 239.807 206.466 1.00 10.27  ? 2332 ARG A CB    1 
ATOM   6335  C  CG    . ARG A 1 2332 ? 203.348 238.333 206.227 1.00 12.88  ? 2332 ARG A CG    1 
ATOM   6336  C  CD    . ARG A 1 2332 ? 202.740 238.097 204.858 1.00 11.74  ? 2332 ARG A CD    1 
ATOM   6337  N  NE    . ARG A 1 2332 ? 203.725 238.244 203.793 1.00 12.47  ? 2332 ARG A NE    1 
ATOM   6338  C  CZ    . ARG A 1 2332 ? 204.677 237.363 203.524 1.00 11.31  ? 2332 ARG A CZ    1 
ATOM   6339  N  NH1   . ARG A 1 2332 ? 204.799 236.242 204.216 1.00 7.56   ? 2332 ARG A NH1   1 
ATOM   6340  N  NH2   . ARG A 1 2332 ? 205.530 237.612 202.534 1.00 11.88  ? 2332 ARG A NH2   1 
ATOM   6341  N  N     . LEU A 1 2333 ? 204.370 242.331 208.661 1.00 9.97   ? 2333 LEU A N     1 
ATOM   6342  C  CA    . LEU A 1 2333 ? 204.500 243.772 208.838 1.00 7.81   ? 2333 LEU A CA    1 
ATOM   6343  C  C     . LEU A 1 2333 ? 205.711 244.259 208.057 1.00 9.28   ? 2333 LEU A C     1 
ATOM   6344  O  O     . LEU A 1 2333 ? 206.824 243.775 208.272 1.00 13.37  ? 2333 LEU A O     1 
ATOM   6345  C  CB    . LEU A 1 2333 ? 204.635 244.135 210.316 1.00 10.31  ? 2333 LEU A CB    1 
ATOM   6346  C  CG    . LEU A 1 2333 ? 203.459 243.794 211.235 1.00 10.13  ? 2333 LEU A CG    1 
ATOM   6347  C  CD1   . LEU A 1 2333 ? 203.680 242.457 211.917 1.00 15.57  ? 2333 LEU A CD1   1 
ATOM   6348  C  CD2   . LEU A 1 2333 ? 203.254 244.889 212.263 1.00 8.75   ? 2333 LEU A CD2   1 
ATOM   6349  N  N     . SER A 1 2334 ? 205.496 245.216 207.160 1.00 10.98  ? 2334 SER A N     1 
ATOM   6350  C  CA    . SER A 1 2334 ? 206.584 245.749 206.354 1.00 8.95   ? 2334 SER A CA    1 
ATOM   6351  C  C     . SER A 1 2334 ? 207.344 246.821 207.123 1.00 10.14  ? 2334 SER A C     1 
ATOM   6352  O  O     . SER A 1 2334 ? 206.748 247.655 207.808 1.00 11.79  ? 2334 SER A O     1 
ATOM   6353  C  CB    . SER A 1 2334 ? 206.047 246.323 205.043 1.00 9.89   ? 2334 SER A CB    1 
ATOM   6354  O  OG    . SER A 1 2334 ? 207.094 246.870 204.261 1.00 16.52  ? 2334 SER A OG    1 
ATOM   6355  N  N     . LEU A 1 2335 ? 208.667 246.792 207.007 1.00 9.61   ? 2335 LEU A N     1 
ATOM   6356  C  CA    . LEU A 1 2335 ? 209.506 247.765 207.695 1.00 7.33   ? 2335 LEU A CA    1 
ATOM   6357  C  C     . LEU A 1 2335 ? 209.433 249.110 206.983 1.00 8.70   ? 2335 LEU A C     1 
ATOM   6358  O  O     . LEU A 1 2335 ? 209.759 249.188 205.793 1.00 9.83   ? 2335 LEU A O     1 
ATOM   6359  C  CB    . LEU A 1 2335 ? 210.949 247.281 207.754 1.00 6.15   ? 2335 LEU A CB    1 
ATOM   6360  C  CG    . LEU A 1 2335 ? 211.856 247.996 208.754 1.00 7.08   ? 2335 LEU A CG    1 
ATOM   6361  C  CD1   . LEU A 1 2335 ? 211.583 247.512 210.165 1.00 11.06  ? 2335 LEU A CD1   1 
ATOM   6362  C  CD2   . LEU A 1 2335 ? 213.318 247.796 208.396 1.00 8.28   ? 2335 LEU A CD2   1 
ATOM   6363  N  N     . PRO A 1 2336 ? 209.011 250.180 207.660 1.00 8.00   ? 2336 PRO A N     1 
ATOM   6364  C  CA    . PRO A 1 2336 ? 208.940 251.479 206.997 1.00 6.44   ? 2336 PRO A CA    1 
ATOM   6365  C  C     . PRO A 1 2336 ? 210.326 251.994 206.654 1.00 8.54   ? 2336 PRO A C     1 
ATOM   6366  O  O     . PRO A 1 2336 ? 211.310 251.674 207.342 1.00 10.47  ? 2336 PRO A O     1 
ATOM   6367  C  CB    . PRO A 1 2336 ? 208.253 252.374 208.045 1.00 7.58   ? 2336 PRO A CB    1 
ATOM   6368  C  CG    . PRO A 1 2336 ? 207.576 251.426 208.978 1.00 9.08   ? 2336 PRO A CG    1 
ATOM   6369  C  CD    . PRO A 1 2336 ? 208.456 250.223 209.022 1.00 10.60  ? 2336 PRO A CD    1 
ATOM   6370  N  N     . PRO A 1 2337 ? 210.453 252.799 205.595 1.00 8.98   ? 2337 PRO A N     1 
ATOM   6371  C  CA    . PRO A 1 2337 ? 211.784 253.290 205.197 1.00 10.46  ? 2337 PRO A CA    1 
ATOM   6372  C  C     . PRO A 1 2337 ? 212.440 254.210 206.214 1.00 8.54   ? 2337 PRO A C     1 
ATOM   6373  O  O     . PRO A 1 2337 ? 213.659 254.405 206.143 1.00 9.99   ? 2337 PRO A O     1 
ATOM   6374  C  CB    . PRO A 1 2337 ? 211.508 254.026 203.879 1.00 5.82   ? 2337 PRO A CB    1 
ATOM   6375  C  CG    . PRO A 1 2337 ? 210.061 254.376 203.937 1.00 10.16  ? 2337 PRO A CG    1 
ATOM   6376  C  CD    . PRO A 1 2337 ? 209.395 253.266 204.686 1.00 7.38   ? 2337 PRO A CD    1 
ATOM   6377  N  N     . ASN A 1 2338 ? 211.685 254.785 207.144 1.00 7.14   ? 2338 ASN A N     1 
ATOM   6378  C  CA    . ASN A 1 2338 ? 212.240 255.702 208.132 1.00 8.73   ? 2338 ASN A CA    1 
ATOM   6379  C  C     . ASN A 1 2338 ? 212.700 255.001 209.401 1.00 9.84   ? 2338 ASN A C     1 
ATOM   6380  O  O     . ASN A 1 2338 ? 213.130 255.675 210.343 1.00 9.42   ? 2338 ASN A O     1 
ATOM   6381  C  CB    . ASN A 1 2338 ? 211.210 256.779 208.489 1.00 10.84  ? 2338 ASN A CB    1 
ATOM   6382  C  CG    . ASN A 1 2338 ? 210.023 256.222 209.246 1.00 10.61  ? 2338 ASN A CG    1 
ATOM   6383  O  OD1   . ASN A 1 2338 ? 209.386 255.268 208.807 1.00 12.64  ? 2338 ASN A OD1   1 
ATOM   6384  N  ND2   . ASN A 1 2338 ? 209.718 256.820 210.390 1.00 11.03  ? 2338 ASN A ND2   1 
ATOM   6385  N  N     . VAL A 1 2339 ? 212.625 253.674 209.453 1.00 9.52   ? 2339 VAL A N     1 
ATOM   6386  C  CA    . VAL A 1 2339 ? 212.963 252.907 210.644 1.00 5.82   ? 2339 VAL A CA    1 
ATOM   6387  C  C     . VAL A 1 2339 ? 214.306 252.225 210.429 1.00 6.61   ? 2339 VAL A C     1 
ATOM   6388  O  O     . VAL A 1 2339 ? 214.536 251.602 209.385 1.00 10.59  ? 2339 VAL A O     1 
ATOM   6389  C  CB    . VAL A 1 2339 ? 211.871 251.877 210.970 1.00 5.90   ? 2339 VAL A CB    1 
ATOM   6390  C  CG1   . VAL A 1 2339 ? 212.230 251.104 212.228 1.00 7.31   ? 2339 VAL A CG1   1 
ATOM   6391  C  CG2   . VAL A 1 2339 ? 210.531 252.568 211.130 1.00 6.56   ? 2339 VAL A CG2   1 
ATOM   6392  N  N     . ARG A 1 2340 ? 215.195 252.348 211.412 1.00 5.99   ? 2340 ARG A N     1 
ATOM   6393  C  CA    . ARG A 1 2340 ? 216.478 251.663 211.412 1.00 4.61   ? 2340 ARG A CA    1 
ATOM   6394  C  C     . ARG A 1 2340 ? 216.523 250.701 212.590 1.00 5.09   ? 2340 ARG A C     1 
ATOM   6395  O  O     . ARG A 1 2340 ? 216.242 251.093 213.725 1.00 9.59   ? 2340 ARG A O     1 
ATOM   6396  C  CB    . ARG A 1 2340 ? 217.642 252.653 211.500 1.00 4.80   ? 2340 ARG A CB    1 
ATOM   6397  C  CG    . ARG A 1 2340 ? 217.721 253.628 210.345 1.00 4.38   ? 2340 ARG A CG    1 
ATOM   6398  C  CD    . ARG A 1 2340 ? 218.247 252.956 209.091 1.00 4.18   ? 2340 ARG A CD    1 
ATOM   6399  N  NE    . ARG A 1 2340 ? 218.368 253.895 207.982 1.00 4.81   ? 2340 ARG A NE    1 
ATOM   6400  C  CZ    . ARG A 1 2340 ? 217.346 254.365 207.283 1.00 6.32   ? 2340 ARG A CZ    1 
ATOM   6401  N  NH1   . ARG A 1 2340 ? 216.100 254.019 207.559 1.00 8.02   ? 2340 ARG A NH1   1 
ATOM   6402  N  NH2   . ARG A 1 2340 ? 217.579 255.208 206.281 1.00 8.33   ? 2340 ARG A NH2   1 
ATOM   6403  N  N     . ILE A 1 2341 ? 216.877 249.449 212.317 1.00 5.65   ? 2341 ILE A N     1 
ATOM   6404  C  CA    . ILE A 1 2341 ? 217.025 248.438 213.356 1.00 3.69   ? 2341 ILE A CA    1 
ATOM   6405  C  C     . ILE A 1 2341 ? 218.492 248.412 213.765 1.00 4.66   ? 2341 ILE A C     1 
ATOM   6406  O  O     . ILE A 1 2341 ? 219.363 248.070 212.962 1.00 6.28   ? 2341 ILE A O     1 
ATOM   6407  C  CB    . ILE A 1 2341 ? 216.553 247.061 212.875 1.00 4.31   ? 2341 ILE A CB    1 
ATOM   6408  C  CG1   . ILE A 1 2341 ? 215.143 247.155 212.292 1.00 5.53   ? 2341 ILE A CG1   1 
ATOM   6409  C  CG2   . ILE A 1 2341 ? 216.590 246.058 214.013 1.00 5.07   ? 2341 ILE A CG2   1 
ATOM   6410  C  CD1   . ILE A 1 2341 ? 214.089 247.536 213.300 1.00 5.65   ? 2341 ILE A CD1   1 
ATOM   6411  N  N     . MET A 1 2342 ? 218.767 248.771 215.014 1.00 6.03   ? 2342 MET A N     1 
ATOM   6412  C  CA    . MET A 1 2342 ? 220.127 248.892 215.513 1.00 3.63   ? 2342 MET A CA    1 
ATOM   6413  C  C     . MET A 1 2342 ? 220.346 247.960 216.695 1.00 3.72   ? 2342 MET A C     1 
ATOM   6414  O  O     . MET A 1 2342 ? 219.433 247.698 217.482 1.00 3.72   ? 2342 MET A O     1 
ATOM   6415  C  CB    . MET A 1 2342 ? 220.440 250.333 215.927 1.00 3.41   ? 2342 MET A CB    1 
ATOM   6416  C  CG    . MET A 1 2342 ? 220.682 251.268 214.761 1.00 5.69   ? 2342 MET A CG    1 
ATOM   6417  S  SD    . MET A 1 2342 ? 220.829 252.991 215.264 1.00 23.65  ? 2342 MET A SD    1 
ATOM   6418  C  CE    . MET A 1 2342 ? 220.897 253.793 213.666 1.00 8.22   ? 2342 MET A CE    1 
ATOM   6419  N  N     . PHE A 1 2343 ? 221.571 247.454 216.804 1.00 4.25   ? 2343 PHE A N     1 
ATOM   6420  C  CA    . PHE A 1 2343 ? 221.989 246.622 217.923 1.00 3.28   ? 2343 PHE A CA    1 
ATOM   6421  C  C     . PHE A 1 2343 ? 223.225 247.239 218.556 1.00 4.74   ? 2343 PHE A C     1 
ATOM   6422  O  O     . PHE A 1 2343 ? 224.189 247.565 217.856 1.00 7.58   ? 2343 PHE A O     1 
ATOM   6423  C  CB    . PHE A 1 2343 ? 222.290 245.183 217.483 1.00 3.35   ? 2343 PHE A CB    1 
ATOM   6424  C  CG    . PHE A 1 2343 ? 221.204 244.553 216.658 1.00 3.38   ? 2343 PHE A CG    1 
ATOM   6425  C  CD1   . PHE A 1 2343 ? 221.089 244.826 215.306 1.00 5.07   ? 2343 PHE A CD1   1 
ATOM   6426  C  CD2   . PHE A 1 2343 ? 220.302 243.679 217.235 1.00 2.90   ? 2343 PHE A CD2   1 
ATOM   6427  C  CE1   . PHE A 1 2343 ? 220.093 244.247 214.551 1.00 4.43   ? 2343 PHE A CE1   1 
ATOM   6428  C  CE2   . PHE A 1 2343 ? 219.305 243.096 216.483 1.00 3.61   ? 2343 PHE A CE2   1 
ATOM   6429  C  CZ    . PHE A 1 2343 ? 219.201 243.380 215.140 1.00 4.18   ? 2343 PHE A CZ    1 
ATOM   6430  N  N     . GLU A 1 2344 ? 223.195 247.400 219.873 1.00 3.72   ? 2344 GLU A N     1 
ATOM   6431  C  CA    . GLU A 1 2344 ? 224.342 247.874 220.640 1.00 2.42   ? 2344 GLU A CA    1 
ATOM   6432  C  C     . GLU A 1 2344 ? 224.798 246.714 221.516 1.00 3.14   ? 2344 GLU A C     1 
ATOM   6433  O  O     . GLU A 1 2344 ? 224.153 246.387 222.516 1.00 4.99   ? 2344 GLU A O     1 
ATOM   6434  C  CB    . GLU A 1 2344 ? 223.985 249.103 221.466 1.00 4.86   ? 2344 GLU A CB    1 
ATOM   6435  C  CG    . GLU A 1 2344 ? 225.184 249.803 222.072 1.00 4.54   ? 2344 GLU A CG    1 
ATOM   6436  C  CD    . GLU A 1 2344 ? 224.794 250.782 223.150 1.00 5.24   ? 2344 GLU A CD    1 
ATOM   6437  O  OE1   . GLU A 1 2344 ? 223.857 251.573 222.920 1.00 10.16  ? 2344 GLU A OE1   1 
ATOM   6438  O  OE2   . GLU A 1 2344 ? 225.425 250.770 224.225 1.00 5.03   ? 2344 GLU A OE2   1 
ATOM   6439  N  N     . VAL A 1 2345 ? 225.908 246.091 221.133 1.00 3.87   ? 2345 VAL A N     1 
ATOM   6440  C  CA    . VAL A 1 2345 ? 226.389 244.878 221.775 1.00 2.97   ? 2345 VAL A CA    1 
ATOM   6441  C  C     . VAL A 1 2345 ? 227.853 245.065 222.143 1.00 3.78   ? 2345 VAL A C     1 
ATOM   6442  O  O     . VAL A 1 2345 ? 228.537 245.962 221.644 1.00 5.11   ? 2345 VAL A O     1 
ATOM   6443  C  CB    . VAL A 1 2345 ? 226.214 243.638 220.875 1.00 3.52   ? 2345 VAL A CB    1 
ATOM   6444  C  CG1   . VAL A 1 2345 ? 224.757 243.450 220.501 1.00 3.65   ? 2345 VAL A CG1   1 
ATOM   6445  C  CG2   . VAL A 1 2345 ? 227.077 243.760 219.631 1.00 3.53   ? 2345 VAL A CG2   1 
ATOM   6446  N  N     . GLN A 1 2346 ? 228.330 244.202 223.038 1.00 5.18   ? 2346 GLN A N     1 
ATOM   6447  C  CA    . GLN A 1 2346 ? 229.738 244.185 223.399 1.00 4.78   ? 2346 GLN A CA    1 
ATOM   6448  C  C     . GLN A 1 2346 ? 230.528 243.104 222.676 1.00 7.81   ? 2346 GLN A C     1 
ATOM   6449  O  O     . GLN A 1 2346 ? 231.761 243.183 222.634 1.00 7.98   ? 2346 GLN A O     1 
ATOM   6450  C  CB    . GLN A 1 2346 ? 229.900 244.019 224.915 1.00 4.68   ? 2346 GLN A CB    1 
ATOM   6451  C  CG    . GLN A 1 2346 ? 229.845 242.589 225.417 1.00 6.13   ? 2346 GLN A CG    1 
ATOM   6452  C  CD    . GLN A 1 2346 ? 229.823 242.512 226.929 1.00 8.75   ? 2346 GLN A CD    1 
ATOM   6453  O  OE1   . GLN A 1 2346 ? 230.390 243.363 227.613 1.00 8.22   ? 2346 GLN A OE1   1 
ATOM   6454  N  NE2   . GLN A 1 2346 ? 229.162 241.492 227.461 1.00 13.82  ? 2346 GLN A NE2   1 
ATOM   6455  N  N     . ASP A 1 2347 ? 229.853 242.108 222.107 1.00 7.22   ? 2347 ASP A N     1 
ATOM   6456  C  CA    . ASP A 1 2347 ? 230.518 241.073 221.329 1.00 7.06   ? 2347 ASP A CA    1 
ATOM   6457  C  C     . ASP A 1 2347 ? 229.481 240.371 220.469 1.00 8.82   ? 2347 ASP A C     1 
ATOM   6458  O  O     . ASP A 1 2347 ? 228.275 240.577 220.625 1.00 6.95   ? 2347 ASP A O     1 
ATOM   6459  C  CB    . ASP A 1 2347 ? 231.251 240.065 222.223 1.00 5.73   ? 2347 ASP A CB    1 
ATOM   6460  C  CG    . ASP A 1 2347 ? 230.326 239.367 223.204 1.00 11.80  ? 2347 ASP A CG    1 
ATOM   6461  O  OD1   . ASP A 1 2347 ? 229.521 238.515 222.774 1.00 18.60  ? 2347 ASP A OD1   1 
ATOM   6462  O  OD2   . ASP A 1 2347 ? 230.418 239.659 224.414 1.00 13.21  ? 2347 ASP A OD2   1 
ATOM   6463  N  N     . LEU A 1 2348 ? 229.971 239.538 219.558 1.00 9.29   ? 2348 LEU A N     1 
ATOM   6464  C  CA    . LEU A 1 2348 ? 229.134 238.715 218.697 1.00 8.52   ? 2348 LEU A CA    1 
ATOM   6465  C  C     . LEU A 1 2348 ? 229.630 237.279 218.682 1.00 11.26  ? 2348 LEU A C     1 
ATOM   6466  O  O     . LEU A 1 2348 ? 229.560 236.592 217.661 1.00 19.02  ? 2348 LEU A O     1 
ATOM   6467  C  CB    . LEU A 1 2348 ? 229.086 239.273 217.276 1.00 8.80   ? 2348 LEU A CB    1 
ATOM   6468  C  CG    . LEU A 1 2348 ? 228.278 240.549 217.040 1.00 7.36   ? 2348 LEU A CG    1 
ATOM   6469  C  CD1   . LEU A 1 2348 ? 228.520 241.088 215.648 1.00 9.34   ? 2348 LEU A CD1   1 
ATOM   6470  C  CD2   . LEU A 1 2348 ? 226.803 240.286 217.251 1.00 5.14   ? 2348 LEU A CD2   1 
ATOM   6471  N  N     . LYS A 1 2349 ? 230.139 236.792 219.815 1.00 10.54  ? 2349 LYS A N     1 
ATOM   6472  C  CA    . LYS A 1 2349 ? 230.702 235.447 219.816 1.00 16.37  ? 2349 LYS A CA    1 
ATOM   6473  C  C     . LYS A 1 2349 ? 229.636 234.362 219.769 1.00 10.06  ? 2349 LYS A C     1 
ATOM   6474  O  O     . LYS A 1 2349 ? 229.985 233.187 219.613 1.00 13.06  ? 2349 LYS A O     1 
ATOM   6475  C  CB    . LYS A 1 2349 ? 231.595 235.237 221.038 1.00 18.03  ? 2349 LYS A CB    1 
ATOM   6476  C  CG    . LYS A 1 2349 ? 230.839 235.085 222.335 1.00 17.14  ? 2349 LYS A CG    1 
ATOM   6477  C  CD    . LYS A 1 2349 ? 231.782 234.953 223.518 1.00 23.43  ? 2349 LYS A CD    1 
ATOM   6478  C  CE    . LYS A 1 2349 ? 232.737 233.781 223.350 1.00 29.02  ? 2349 LYS A CE    1 
ATOM   6479  N  NZ    . LYS A 1 2349 ? 232.026 232.475 223.297 1.00 26.70  ? 2349 LYS A NZ    1 
ATOM   6480  N  N     . TYR A 1 2350 ? 228.358 234.713 219.911 1.00 10.69  ? 2350 TYR A N     1 
ATOM   6481  C  CA    . TYR A 1 2350 ? 227.282 233.737 219.830 1.00 7.85   ? 2350 TYR A CA    1 
ATOM   6482  C  C     . TYR A 1 2350 ? 226.352 233.955 218.646 1.00 12.97  ? 2350 TYR A C     1 
ATOM   6483  O  O     . TYR A 1 2350 ? 225.568 233.056 218.326 1.00 18.46  ? 2350 TYR A O     1 
ATOM   6484  C  CB    . TYR A 1 2350 ? 226.466 233.735 221.130 1.00 8.41   ? 2350 TYR A CB    1 
ATOM   6485  C  CG    . TYR A 1 2350 ? 227.231 233.158 222.297 1.00 10.86  ? 2350 TYR A CG    1 
ATOM   6486  C  CD1   . TYR A 1 2350 ? 227.513 231.802 222.362 1.00 10.26  ? 2350 TYR A CD1   1 
ATOM   6487  C  CD2   . TYR A 1 2350 ? 227.686 233.971 223.323 1.00 10.46  ? 2350 TYR A CD2   1 
ATOM   6488  C  CE1   . TYR A 1 2350 ? 228.221 231.271 223.419 1.00 14.35  ? 2350 TYR A CE1   1 
ATOM   6489  C  CE2   . TYR A 1 2350 ? 228.397 233.449 224.384 1.00 11.62  ? 2350 TYR A CE2   1 
ATOM   6490  C  CZ    . TYR A 1 2350 ? 228.659 232.099 224.428 1.00 18.51  ? 2350 TYR A CZ    1 
ATOM   6491  O  OH    . TYR A 1 2350 ? 229.363 231.570 225.484 1.00 28.76  ? 2350 TYR A OH    1 
ATOM   6492  N  N     . ALA A 1 2351 ? 226.417 235.109 217.991 1.00 14.56  ? 2351 ALA A N     1 
ATOM   6493  C  CA    . ALA A 1 2351 ? 225.614 235.341 216.799 1.00 8.40   ? 2351 ALA A CA    1 
ATOM   6494  C  C     . ALA A 1 2351 ? 226.146 234.526 215.628 1.00 8.20   ? 2351 ALA A C     1 
ATOM   6495  O  O     . ALA A 1 2351 ? 227.359 234.395 215.439 1.00 10.34  ? 2351 ALA A O     1 
ATOM   6496  C  CB    . ALA A 1 2351 ? 225.605 236.825 216.441 1.00 8.73   ? 2351 ALA A CB    1 
ATOM   6497  N  N     . THR A 1 2352 ? 225.230 233.975 214.840 1.00 9.78   ? 2352 THR A N     1 
ATOM   6498  C  CA    . THR A 1 2352 ? 225.606 233.236 213.648 1.00 7.49   ? 2352 THR A CA    1 
ATOM   6499  C  C     . THR A 1 2352 ? 225.941 234.197 212.511 1.00 7.09   ? 2352 THR A C     1 
ATOM   6500  O  O     . THR A 1 2352 ? 225.669 235.400 212.572 1.00 7.45   ? 2352 THR A O     1 
ATOM   6501  C  CB    . THR A 1 2352 ? 224.486 232.285 213.229 1.00 9.37   ? 2352 THR A CB    1 
ATOM   6502  O  OG1   . THR A 1 2352 ? 223.272 233.024 213.045 1.00 12.99  ? 2352 THR A OG1   1 
ATOM   6503  C  CG2   . THR A 1 2352 ? 224.268 231.220 214.289 1.00 12.07  ? 2352 THR A CG2   1 
ATOM   6504  N  N     . LEU A 1 2353 ? 226.519 233.655 211.434 1.00 10.31  ? 2353 LEU A N     1 
ATOM   6505  C  CA    . LEU A 1 2353 ? 226.882 234.500 210.264 1.00 9.69   ? 2353 LEU A CA    1 
ATOM   6506  C  C     . LEU A 1 2353 ? 225.605 235.060 209.618 1.00 9.00   ? 2353 LEU A C     1 
ATOM   6507  O  O     . LEU A 1 2353 ? 225.679 236.151 209.011 1.00 11.82  ? 2353 LEU A O     1 
ATOM   6508  C  CB    . LEU A 1 2353 ? 227.697 233.689 209.258 1.00 11.70  ? 2353 LEU A CB    1 
ATOM   6509  C  CG    . LEU A 1 2353 ? 228.005 234.390 207.932 1.00 17.04  ? 2353 LEU A CG    1 
ATOM   6510  C  CD1   . LEU A 1 2353 ? 228.839 235.640 208.157 1.00 16.50  ? 2353 LEU A CD1   1 
ATOM   6511  C  CD2   . LEU A 1 2353 ? 228.692 233.449 206.959 1.00 17.60  ? 2353 LEU A CD2   1 
ATOM   6512  N  N     . ALA A 1 2354 ? 224.483 234.349 209.750 1.00 8.68   ? 2354 ALA A N     1 
ATOM   6513  C  CA    . ALA A 1 2354 ? 223.216 234.795 209.123 1.00 7.95   ? 2354 ALA A CA    1 
ATOM   6514  C  C     . ALA A 1 2354 ? 222.889 236.211 209.594 1.00 7.21   ? 2354 ALA A C     1 
ATOM   6515  O  O     . ALA A 1 2354 ? 222.447 237.035 208.768 1.00 7.89   ? 2354 ALA A O     1 
ATOM   6516  C  CB    . ALA A 1 2354 ? 222.104 233.832 209.467 1.00 10.21  ? 2354 ALA A CB    1 
ATOM   6517  N  N     . THR A 1 2355 ? 223.108 236.486 210.881 1.00 8.11   ? 2355 THR A N     1 
ATOM   6518  C  CA    . THR A 1 2355 ? 222.811 237.820 211.442 1.00 7.54   ? 2355 THR A CA    1 
ATOM   6519  C  C     . THR A 1 2355 ? 223.939 238.767 211.097 1.00 8.48   ? 2355 THR A C     1 
ATOM   6520  O  O     . THR A 1 2355 ? 223.644 239.927 210.737 1.00 8.19   ? 2355 THR A O     1 
ATOM   6521  C  CB    . THR A 1 2355 ? 222.621 237.699 212.952 1.00 7.21   ? 2355 THR A CB    1 
ATOM   6522  O  OG1   . THR A 1 2355 ? 221.484 236.858 213.117 1.00 8.97   ? 2355 THR A OG1   1 
ATOM   6523  C  CG2   . THR A 1 2355 ? 222.378 239.040 213.617 1.00 6.28   ? 2355 THR A CG2   1 
ATOM   6524  N  N     . VAL A 1 2356 ? 225.187 238.302 211.192 1.00 8.54   ? 2356 VAL A N     1 
ATOM   6525  C  CA    . VAL A 1 2356 ? 226.326 239.185 210.958 1.00 7.53   ? 2356 VAL A CA    1 
ATOM   6526  C  C     . VAL A 1 2356 ? 226.290 239.747 209.542 1.00 10.49  ? 2356 VAL A C     1 
ATOM   6527  O  O     . VAL A 1 2356 ? 226.545 240.937 209.322 1.00 12.41  ? 2356 VAL A O     1 
ATOM   6528  C  CB    . VAL A 1 2356 ? 227.642 238.438 211.243 1.00 9.48   ? 2356 VAL A CB    1 
ATOM   6529  C  CG1   . VAL A 1 2356 ? 228.833 239.209 210.697 1.00 10.83  ? 2356 VAL A CG1   1 
ATOM   6530  C  CG2   . VAL A 1 2356 ? 227.795 238.193 212.734 1.00 8.54   ? 2356 VAL A CG2   1 
ATOM   6531  N  N     . SER A 1 2357 ? 225.937 238.893 208.577 1.00 7.50   ? 2357 SER A N     1 
ATOM   6532  C  CA    . SER A 1 2357 ? 225.937 239.306 207.148 1.00 5.42   ? 2357 SER A CA    1 
ATOM   6533  C  C     . SER A 1 2357 ? 224.794 240.280 206.835 1.00 7.92   ? 2357 SER A C     1 
ATOM   6534  O  O     . SER A 1 2357 ? 224.918 241.014 205.833 1.00 10.63  ? 2357 SER A O     1 
ATOM   6535  C  CB    . SER A 1 2357 ? 225.852 238.095 206.262 1.00 9.22   ? 2357 SER A CB    1 
ATOM   6536  O  OG    . SER A 1 2357 ? 224.667 237.358 206.526 1.00 10.87  ? 2357 SER A OG    1 
ATOM   6537  N  N     . ARG A 1 2358 ? 223.729 240.284 207.640 1.00 8.47   ? 2358 ARG A N     1 
ATOM   6538  C  CA    . ARG A 1 2358 ? 222.547 241.128 207.320 1.00 6.66   ? 2358 ARG A CA    1 
ATOM   6539  C  C     . ARG A 1 2358 ? 222.630 242.488 208.028 1.00 11.70  ? 2358 ARG A C     1 
ATOM   6540  O  O     . ARG A 1 2358 ? 221.584 243.165 208.106 1.00 16.36  ? 2358 ARG A O     1 
ATOM   6541  C  CB    . ARG A 1 2358 ? 221.252 240.441 207.767 1.00 9.59   ? 2358 ARG A CB    1 
ATOM   6542  C  CG    . ARG A 1 2358 ? 220.803 239.212 206.991 1.00 6.27   ? 2358 ARG A CG    1 
ATOM   6543  C  CD    . ARG A 1 2358 ? 219.559 238.636 207.650 1.00 7.09   ? 2358 ARG A CD    1 
ATOM   6544  N  NE    . ARG A 1 2358 ? 218.902 237.557 206.903 1.00 7.33   ? 2358 ARG A NE    1 
ATOM   6545  C  CZ    . ARG A 1 2358 ? 219.422 236.367 206.627 1.00 6.06   ? 2358 ARG A CZ    1 
ATOM   6546  N  NH1   . ARG A 1 2358 ? 220.604 236.026 207.107 1.00 8.46   ? 2358 ARG A NH1   1 
ATOM   6547  N  NH2   . ARG A 1 2358 ? 218.749 235.516 205.874 1.00 6.27   ? 2358 ARG A NH2   1 
ATOM   6548  N  N     . CYS A 1 2359 ? 223.807 242.881 208.522 1.00 11.22  ? 2359 CYS A N     1 
ATOM   6549  C  CA    . CYS A 1 2359 ? 223.885 244.147 209.298 1.00 7.74   ? 2359 CYS A CA    1 
ATOM   6550  C  C     . CYS A 1 2359 ? 225.188 244.902 209.021 1.00 10.70  ? 2359 CYS A C     1 
ATOM   6551  O  O     . CYS A 1 2359 ? 226.238 244.236 208.889 1.00 14.28  ? 2359 CYS A O     1 
ATOM   6552  C  CB    . CYS A 1 2359 ? 223.811 243.874 210.796 1.00 8.96   ? 2359 CYS A CB    1 
ATOM   6553  S  SG    . CYS A 1 2359 ? 222.167 243.377 211.372 1.00 22.81  ? 2359 CYS A SG    1 
ATOM   6554  N  N     . GLY A 1 2360 ? 225.121 246.234 208.929 1.00 8.32   ? 2360 GLY A N     1 
ATOM   6555  C  CA    . GLY A 1 2360 ? 226.321 247.040 208.782 1.00 4.19   ? 2360 GLY A CA    1 
ATOM   6556  C  C     . GLY A 1 2360 ? 226.965 247.256 210.137 1.00 4.33   ? 2360 GLY A C     1 
ATOM   6557  O  O     . GLY A 1 2360 ? 226.318 247.724 211.079 1.00 9.74   ? 2360 GLY A O     1 
ATOM   6558  N  N     . MET A 1 2361 ? 228.245 246.919 210.239 1.00 3.64   ? 2361 MET A N     1 
ATOM   6559  C  CA    . MET A 1 2361 ? 228.944 246.908 211.515 1.00 5.15   ? 2361 MET A CA    1 
ATOM   6560  C  C     . MET A 1 2361 ? 229.807 248.150 211.675 1.00 4.13   ? 2361 MET A C     1 
ATOM   6561  O  O     . MET A 1 2361 ? 230.536 248.538 210.759 1.00 5.07   ? 2361 MET A O     1 
ATOM   6562  C  CB    . MET A 1 2361 ? 229.815 245.657 211.646 1.00 6.48   ? 2361 MET A CB    1 
ATOM   6563  C  CG    . MET A 1 2361 ? 229.078 244.366 211.373 1.00 8.31   ? 2361 MET A CG    1 
ATOM   6564  S  SD    . MET A 1 2361 ? 227.871 244.006 212.656 1.00 15.55  ? 2361 MET A SD    1 
ATOM   6565  C  CE    . MET A 1 2361 ? 227.587 242.267 212.366 1.00 8.54   ? 2361 MET A CE    1 
ATOM   6566  N  N     . VAL A 1 2362 ? 229.714 248.772 212.847 1.00 4.21   ? 2362 VAL A N     1 
ATOM   6567  C  CA    . VAL A 1 2362 ? 230.622 249.838 213.251 1.00 4.66   ? 2362 VAL A CA    1 
ATOM   6568  C  C     . VAL A 1 2362 ? 231.328 249.374 214.516 1.00 6.31   ? 2362 VAL A C     1 
ATOM   6569  O  O     . VAL A 1 2362 ? 230.678 249.128 215.540 1.00 8.62   ? 2362 VAL A O     1 
ATOM   6570  C  CB    . VAL A 1 2362 ? 229.887 251.168 213.482 1.00 5.93   ? 2362 VAL A CB    1 
ATOM   6571  C  CG1   . VAL A 1 2362 ? 230.887 252.296 213.656 1.00 5.98   ? 2362 VAL A CG1   1 
ATOM   6572  C  CG2   . VAL A 1 2362 ? 228.948 251.462 212.328 1.00 6.06   ? 2362 VAL A CG2   1 
ATOM   6573  N  N     . TRP A 1 2363 ? 232.651 249.257 214.447 1.00 4.30   ? 2363 TRP A N     1 
ATOM   6574  C  CA    . TRP A 1 2363 ? 233.448 248.703 215.535 1.00 3.82   ? 2363 TRP A CA    1 
ATOM   6575  C  C     . TRP A 1 2363 ? 233.957 249.833 216.419 1.00 5.12   ? 2363 TRP A C     1 
ATOM   6576  O  O     . TRP A 1 2363 ? 234.627 250.751 215.938 1.00 9.15   ? 2363 TRP A O     1 
ATOM   6577  C  CB    . TRP A 1 2363 ? 234.614 247.879 214.993 1.00 4.14   ? 2363 TRP A CB    1 
ATOM   6578  C  CG    . TRP A 1 2363 ? 235.635 247.545 216.032 1.00 4.17   ? 2363 TRP A CG    1 
ATOM   6579  C  CD1   . TRP A 1 2363 ? 236.867 248.107 216.179 1.00 4.13   ? 2363 TRP A CD1   1 
ATOM   6580  C  CD2   . TRP A 1 2363 ? 235.509 246.578 217.080 1.00 4.16   ? 2363 TRP A CD2   1 
ATOM   6581  N  NE1   . TRP A 1 2363 ? 237.519 247.549 217.250 1.00 3.94   ? 2363 TRP A NE1   1 
ATOM   6582  C  CE2   . TRP A 1 2363 ? 236.706 246.607 217.820 1.00 3.22   ? 2363 TRP A CE2   1 
ATOM   6583  C  CE3   . TRP A 1 2363 ? 234.501 245.689 217.462 1.00 4.63   ? 2363 TRP A CE3   1 
ATOM   6584  C  CZ2   . TRP A 1 2363 ? 236.922 245.782 218.920 1.00 2.70   ? 2363 TRP A CZ2   1 
ATOM   6585  C  CZ3   . TRP A 1 2363 ? 234.718 244.871 218.554 1.00 4.17   ? 2363 TRP A CZ3   1 
ATOM   6586  C  CH2   . TRP A 1 2363 ? 235.918 244.923 219.269 1.00 3.68   ? 2363 TRP A CH2   1 
ATOM   6587  N  N     . PHE A 1 2364 ? 233.647 249.758 217.709 1.00 3.11   ? 2364 PHE A N     1 
ATOM   6588  C  CA    . PHE A 1 2364 ? 234.066 250.751 218.693 1.00 3.42   ? 2364 PHE A CA    1 
ATOM   6589  C  C     . PHE A 1 2364 ? 235.115 250.111 219.595 1.00 5.56   ? 2364 PHE A C     1 
ATOM   6590  O  O     . PHE A 1 2364 ? 234.775 249.379 220.527 1.00 6.94   ? 2364 PHE A O     1 
ATOM   6591  C  CB    . PHE A 1 2364 ? 232.881 251.247 219.516 1.00 3.51   ? 2364 PHE A CB    1 
ATOM   6592  C  CG    . PHE A 1 2364 ? 231.917 252.107 218.756 1.00 3.87   ? 2364 PHE A CG    1 
ATOM   6593  C  CD1   . PHE A 1 2364 ? 230.960 251.539 217.933 1.00 4.53   ? 2364 PHE A CD1   1 
ATOM   6594  C  CD2   . PHE A 1 2364 ? 231.946 253.482 218.886 1.00 2.64   ? 2364 PHE A CD2   1 
ATOM   6595  C  CE1   . PHE A 1 2364 ? 230.066 252.327 217.245 1.00 3.19   ? 2364 PHE A CE1   1 
ATOM   6596  C  CE2   . PHE A 1 2364 ? 231.054 254.273 218.200 1.00 2.22   ? 2364 PHE A CE2   1 
ATOM   6597  C  CZ    . PHE A 1 2364 ? 230.114 253.696 217.379 1.00 2.88   ? 2364 PHE A CZ    1 
ATOM   6598  N  N     . SER A 1 2365 ? 236.386 250.389 219.329 1.00 6.00   ? 2365 SER A N     1 
ATOM   6599  C  CA    . SER A 1 2365 ? 237.426 249.931 220.235 1.00 6.21   ? 2365 SER A CA    1 
ATOM   6600  C  C     . SER A 1 2365 ? 237.441 250.790 221.497 1.00 12.86  ? 2365 SER A C     1 
ATOM   6601  O  O     . SER A 1 2365 ? 236.917 251.907 221.527 1.00 12.23  ? 2365 SER A O     1 
ATOM   6602  C  CB    . SER A 1 2365 ? 238.793 249.970 219.554 1.00 8.43   ? 2365 SER A CB    1 
ATOM   6603  O  OG    . SER A 1 2365 ? 239.060 251.253 219.020 1.00 21.41  ? 2365 SER A OG    1 
ATOM   6604  N  N     . GLU A 1 2366 ? 238.049 250.251 222.555 1.00 17.66  ? 2366 GLU A N     1 
ATOM   6605  C  CA    . GLU A 1 2366 ? 238.203 251.021 223.783 1.00 15.87  ? 2366 GLU A CA    1 
ATOM   6606  C  C     . GLU A 1 2366 ? 239.093 252.237 223.584 1.00 19.93  ? 2366 GLU A C     1 
ATOM   6607  O  O     . GLU A 1 2366 ? 238.997 253.197 224.356 1.00 21.16  ? 2366 GLU A O     1 
ATOM   6608  C  CB    . GLU A 1 2366 ? 238.771 250.140 224.896 1.00 15.87  ? 2366 GLU A CB    1 
ATOM   6609  C  CG    . GLU A 1 2366 ? 237.720 249.388 225.693 1.00 25.88  ? 2366 GLU A CG    1 
ATOM   6610  C  CD    . GLU A 1 2366 ? 238.281 248.774 226.961 1.00 37.39  ? 2366 GLU A CD    1 
ATOM   6611  O  OE1   . GLU A 1 2366 ? 238.711 249.537 227.852 1.00 26.84  ? 2366 GLU A OE1   1 
ATOM   6612  O  OE2   . GLU A 1 2366 ? 238.294 247.529 227.065 1.00 31.09  ? 2366 GLU A OE2   1 
ATOM   6613  N  N     . ASP A 1 2367 ? 239.958 252.219 222.571 1.00 21.07  ? 2367 ASP A N     1 
ATOM   6614  C  CA    . ASP A 1 2367 ? 240.797 253.363 222.252 1.00 16.91  ? 2367 ASP A CA    1 
ATOM   6615  C  C     . ASP A 1 2367 ? 240.020 254.509 221.621 1.00 18.58  ? 2367 ASP A C     1 
ATOM   6616  O  O     . ASP A 1 2367 ? 240.525 255.636 221.594 1.00 20.25  ? 2367 ASP A O     1 
ATOM   6617  C  CB    . ASP A 1 2367 ? 241.929 252.931 221.318 1.00 22.79  ? 2367 ASP A CB    1 
ATOM   6618  C  CG    . ASP A 1 2367 ? 242.828 251.885 221.943 1.00 41.53  ? 2367 ASP A CG    1 
ATOM   6619  O  OD1   . ASP A 1 2367 ? 242.681 250.693 221.603 1.00 51.28  ? 2367 ASP A OD1   1 
ATOM   6620  O  OD2   . ASP A 1 2367 ? 243.682 252.255 222.776 1.00 47.67  ? 2367 ASP A OD2   1 
ATOM   6621  N  N     . VAL A 1 2368 ? 238.816 254.246 221.107 1.00 16.28  ? 2368 VAL A N     1 
ATOM   6622  C  CA    . VAL A 1 2368 ? 237.993 255.312 220.542 1.00 12.24  ? 2368 VAL A CA    1 
ATOM   6623  C  C     . VAL A 1 2368 ? 237.626 256.322 221.621 1.00 11.32  ? 2368 VAL A C     1 
ATOM   6624  O  O     . VAL A 1 2368 ? 237.711 257.538 221.416 1.00 13.77  ? 2368 VAL A O     1 
ATOM   6625  C  CB    . VAL A 1 2368 ? 236.741 254.718 219.870 1.00 9.76   ? 2368 VAL A CB    1 
ATOM   6626  C  CG1   . VAL A 1 2368 ? 235.680 255.784 219.677 1.00 10.19  ? 2368 VAL A CG1   1 
ATOM   6627  C  CG2   . VAL A 1 2368 ? 237.106 254.081 218.543 1.00 11.41  ? 2368 VAL A CG2   1 
ATOM   6628  N  N     . LEU A 1 2369 ? 237.223 255.831 222.789 1.00 12.26  ? 2369 LEU A N     1 
ATOM   6629  C  CA    . LEU A 1 2369 ? 236.900 256.675 223.936 1.00 9.29   ? 2369 LEU A CA    1 
ATOM   6630  C  C     . LEU A 1 2369 ? 238.107 256.691 224.865 1.00 8.34   ? 2369 LEU A C     1 
ATOM   6631  O  O     . LEU A 1 2369 ? 238.358 255.729 225.594 1.00 11.36  ? 2369 LEU A O     1 
ATOM   6632  C  CB    . LEU A 1 2369 ? 235.652 256.163 224.648 1.00 7.87   ? 2369 LEU A CB    1 
ATOM   6633  C  CG    . LEU A 1 2369 ? 235.259 256.912 225.920 1.00 10.36  ? 2369 LEU A CG    1 
ATOM   6634  C  CD1   . LEU A 1 2369 ? 234.489 258.171 225.579 1.00 9.77   ? 2369 LEU A CD1   1 
ATOM   6635  C  CD2   . LEU A 1 2369 ? 234.442 256.013 226.830 1.00 5.89   ? 2369 LEU A CD2   1 
ATOM   6636  N  N     . SER A 1 2370 ? 238.857 257.787 224.836 1.00 8.49   ? 2370 SER A N     1 
ATOM   6637  C  CA    . SER A 1 2370 ? 240.028 257.912 225.687 1.00 9.55   ? 2370 SER A CA    1 
ATOM   6638  C  C     . SER A 1 2370 ? 239.620 258.284 227.109 1.00 9.49   ? 2370 SER A C     1 
ATOM   6639  O  O     . SER A 1 2370 ? 238.515 258.771 227.365 1.00 9.85   ? 2370 SER A O     1 
ATOM   6640  C  CB    . SER A 1 2370 ? 240.994 258.955 225.128 1.00 13.01  ? 2370 SER A CB    1 
ATOM   6641  O  OG    . SER A 1 2370 ? 240.363 260.213 224.980 1.00 12.47  ? 2370 SER A OG    1 
ATOM   6642  N  N     . THR A 1 2371 ? 240.538 258.039 228.044 1.00 10.70  ? 2371 THR A N     1 
ATOM   6643  C  CA    . THR A 1 2371 ? 240.280 258.356 229.444 1.00 10.40  ? 2371 THR A CA    1 
ATOM   6644  C  C     . THR A 1 2371 ? 240.173 259.862 229.662 1.00 10.29  ? 2371 THR A C     1 
ATOM   6645  O  O     . THR A 1 2371 ? 239.405 260.314 230.523 1.00 12.92  ? 2371 THR A O     1 
ATOM   6646  C  CB    . THR A 1 2371 ? 241.384 257.755 230.315 1.00 8.67   ? 2371 THR A CB    1 
ATOM   6647  O  OG1   . THR A 1 2371 ? 241.419 256.335 230.123 1.00 13.58  ? 2371 THR A OG1   1 
ATOM   6648  C  CG2   . THR A 1 2371 ? 241.119 258.025 231.773 1.00 12.17  ? 2371 THR A CG2   1 
ATOM   6649  N  N     . ASP A 1 2372 ? 240.922 260.649 228.884 1.00 10.36  ? 2372 ASP A N     1 
ATOM   6650  C  CA    . ASP A 1 2372 ? 240.811 262.101 228.958 1.00 11.22  ? 2372 ASP A CA    1 
ATOM   6651  C  C     . ASP A 1 2372 ? 239.398 262.562 228.634 1.00 11.99  ? 2372 ASP A C     1 
ATOM   6652  O  O     . ASP A 1 2372 ? 238.900 263.527 229.225 1.00 12.33  ? 2372 ASP A O     1 
ATOM   6653  C  CB    . ASP A 1 2372 ? 241.811 262.750 228.002 1.00 20.20  ? 2372 ASP A CB    1 
ATOM   6654  C  CG    . ASP A 1 2372 ? 243.245 262.561 228.442 1.00 43.71  ? 2372 ASP A CG    1 
ATOM   6655  O  OD1   . ASP A 1 2372 ? 243.485 262.450 229.662 1.00 55.39  ? 2372 ASP A OD1   1 
ATOM   6656  O  OD2   . ASP A 1 2372 ? 244.134 262.522 227.566 1.00 48.35  ? 2372 ASP A OD2   1 
ATOM   6657  N  N     . MET A 1 2373 ? 238.738 261.889 227.688 1.00 10.76  ? 2373 MET A N     1 
ATOM   6658  C  CA    . MET A 1 2373 ? 237.360 262.226 227.351 1.00 7.42   ? 2373 MET A CA    1 
ATOM   6659  C  C     . MET A 1 2373 ? 236.435 262.016 228.542 1.00 10.03  ? 2373 MET A C     1 
ATOM   6660  O  O     . MET A 1 2373 ? 235.572 262.853 228.826 1.00 13.85  ? 2373 MET A O     1 
ATOM   6661  C  CB    . MET A 1 2373 ? 236.905 261.378 226.166 1.00 9.94   ? 2373 MET A CB    1 
ATOM   6662  C  CG    . MET A 1 2373 ? 237.571 261.728 224.853 1.00 10.22  ? 2373 MET A CG    1 
ATOM   6663  S  SD    . MET A 1 2373 ? 237.118 260.582 223.542 1.00 11.97  ? 2373 MET A SD    1 
ATOM   6664  C  CE    . MET A 1 2373 ? 235.526 261.224 223.063 1.00 6.34   ? 2373 MET A CE    1 
ATOM   6665  N  N     . ILE A 1 2374 ? 236.605 260.898 229.250 1.00 11.03  ? 2374 ILE A N     1 
ATOM   6666  C  CA    . ILE A 1 2374 ? 235.778 260.614 230.419 1.00 7.77   ? 2374 ILE A CA    1 
ATOM   6667  C  C     . ILE A 1 2374 ? 236.042 261.636 231.516 1.00 8.51   ? 2374 ILE A C     1 
ATOM   6668  O  O     . ILE A 1 2374 ? 235.114 262.099 232.192 1.00 10.37  ? 2374 ILE A O     1 
ATOM   6669  C  CB    . ILE A 1 2374 ? 236.028 259.176 230.906 1.00 7.15   ? 2374 ILE A CB    1 
ATOM   6670  C  CG1   . ILE A 1 2374 ? 236.006 258.211 229.722 1.00 8.88   ? 2374 ILE A CG1   1 
ATOM   6671  C  CG2   . ILE A 1 2374 ? 234.986 258.774 231.932 1.00 11.56  ? 2374 ILE A CG2   1 
ATOM   6672  C  CD1   . ILE A 1 2374 ? 236.472 256.820 230.057 1.00 9.06   ? 2374 ILE A CD1   1 
ATOM   6673  N  N     . PHE A 1 2375 ? 237.311 262.001 231.709 1.00 9.13   ? 2375 PHE A N     1 
ATOM   6674  C  CA    . PHE A 1 2375 ? 237.640 263.023 232.699 1.00 9.39   ? 2375 PHE A CA    1 
ATOM   6675  C  C     . PHE A 1 2375 ? 237.004 264.362 232.344 1.00 12.34  ? 2375 PHE A C     1 
ATOM   6676  O  O     . PHE A 1 2375 ? 236.464 265.054 233.216 1.00 15.47  ? 2375 PHE A O     1 
ATOM   6677  C  CB    . PHE A 1 2375 ? 239.155 263.166 232.822 1.00 9.07   ? 2375 PHE A CB    1 
ATOM   6678  C  CG    . PHE A 1 2375 ? 239.824 261.986 233.463 1.00 9.38   ? 2375 PHE A CG    1 
ATOM   6679  C  CD1   . PHE A 1 2375 ? 239.086 261.050 234.164 1.00 10.51  ? 2375 PHE A CD1   1 
ATOM   6680  C  CD2   . PHE A 1 2375 ? 241.194 261.820 233.374 1.00 10.56  ? 2375 PHE A CD2   1 
ATOM   6681  C  CE1   . PHE A 1 2375 ? 239.700 259.969 234.756 1.00 10.58  ? 2375 PHE A CE1   1 
ATOM   6682  C  CE2   . PHE A 1 2375 ? 241.812 260.742 233.967 1.00 12.43  ? 2375 PHE A CE2   1 
ATOM   6683  C  CZ    . PHE A 1 2375 ? 241.064 259.817 234.660 1.00 11.38  ? 2375 PHE A CZ    1 
ATOM   6684  N  N     . ASN A 1 2376 ? 237.060 264.743 231.066 1.00 11.00  ? 2376 ASN A N     1 
ATOM   6685  C  CA    . ASN A 1 2376 ? 236.444 265.993 230.634 1.00 8.29   ? 2376 ASN A CA    1 
ATOM   6686  C  C     . ASN A 1 2376 ? 234.939 265.966 230.849 1.00 9.56   ? 2376 ASN A C     1 
ATOM   6687  O  O     . ASN A 1 2376 ? 234.353 266.958 231.296 1.00 12.66  ? 2376 ASN A O     1 
ATOM   6688  C  CB    . ASN A 1 2376 ? 236.767 266.257 229.163 1.00 7.78   ? 2376 ASN A CB    1 
ATOM   6689  C  CG    . ASN A 1 2376 ? 238.228 266.579 228.936 1.00 11.39  ? 2376 ASN A CG    1 
ATOM   6690  O  OD1   . ASN A 1 2376 ? 238.995 266.738 229.885 1.00 20.64  ? 2376 ASN A OD1   1 
ATOM   6691  N  ND2   . ASN A 1 2376 ? 238.623 266.677 227.674 1.00 9.30   ? 2376 ASN A ND2   1 
ATOM   6692  N  N     . ASN A 1 2377 ? 234.294 264.841 230.529 1.00 9.24   ? 2377 ASN A N     1 
ATOM   6693  C  CA    . ASN A 1 2377 ? 232.855 264.727 230.745 1.00 7.91   ? 2377 ASN A CA    1 
ATOM   6694  C  C     . ASN A 1 2377 ? 232.509 264.861 232.221 1.00 8.45   ? 2377 ASN A C     1 
ATOM   6695  O  O     . ASN A 1 2377 ? 231.572 265.582 232.585 1.00 10.09  ? 2377 ASN A O     1 
ATOM   6696  C  CB    . ASN A 1 2377 ? 232.345 263.395 230.193 1.00 6.56   ? 2377 ASN A CB    1 
ATOM   6697  C  CG    . ASN A 1 2377 ? 230.877 263.163 230.490 1.00 6.60   ? 2377 ASN A CG    1 
ATOM   6698  O  OD1   . ASN A 1 2377 ? 230.514 262.207 231.174 1.00 7.04   ? 2377 ASN A OD1   1 
ATOM   6699  N  ND2   . ASN A 1 2377 ? 230.023 264.037 229.975 1.00 8.99   ? 2377 ASN A ND2   1 
ATOM   6700  N  N     . PHE A 1 2378 ? 233.268 264.184 233.087 1.00 10.14  ? 2378 PHE A N     1 
ATOM   6701  C  CA    . PHE A 1 2378 ? 233.010 264.261 234.521 1.00 7.54   ? 2378 PHE A CA    1 
ATOM   6702  C  C     . PHE A 1 2378 ? 233.183 265.685 235.034 1.00 7.82   ? 2378 PHE A C     1 
ATOM   6703  O  O     . PHE A 1 2378 ? 232.353 266.186 235.800 1.00 8.52   ? 2378 PHE A O     1 
ATOM   6704  C  CB    . PHE A 1 2378 ? 233.935 263.301 235.268 1.00 5.91   ? 2378 PHE A CB    1 
ATOM   6705  C  CG    . PHE A 1 2378 ? 234.100 263.629 236.725 1.00 6.90   ? 2378 PHE A CG    1 
ATOM   6706  C  CD1   . PHE A 1 2378 ? 233.038 263.499 237.603 1.00 8.12   ? 2378 PHE A CD1   1 
ATOM   6707  C  CD2   . PHE A 1 2378 ? 235.318 264.070 237.215 1.00 5.79   ? 2378 PHE A CD2   1 
ATOM   6708  C  CE1   . PHE A 1 2378 ? 233.188 263.801 238.941 1.00 5.94   ? 2378 PHE A CE1   1 
ATOM   6709  C  CE2   . PHE A 1 2378 ? 235.472 264.373 238.552 1.00 5.42   ? 2378 PHE A CE2   1 
ATOM   6710  C  CZ    . PHE A 1 2378 ? 234.405 264.239 239.415 1.00 5.30   ? 2378 PHE A CZ    1 
ATOM   6711  N  N     . LEU A 1 2379 ? 234.258 266.356 234.613 1.00 7.86   ? 2379 LEU A N     1 
ATOM   6712  C  CA    . LEU A 1 2379 ? 234.508 267.713 235.089 1.00 7.84   ? 2379 LEU A CA    1 
ATOM   6713  C  C     . LEU A 1 2379 ? 233.457 268.690 234.573 1.00 9.85   ? 2379 LEU A C     1 
ATOM   6714  O  O     . LEU A 1 2379 ? 233.025 269.585 235.308 1.00 12.82  ? 2379 LEU A O     1 
ATOM   6715  C  CB    . LEU A 1 2379 ? 235.912 268.158 234.683 1.00 9.38   ? 2379 LEU A CB    1 
ATOM   6716  C  CG    . LEU A 1 2379 ? 237.047 267.442 235.419 1.00 8.29   ? 2379 LEU A CG    1 
ATOM   6717  C  CD1   . LEU A 1 2379 ? 238.395 267.818 234.835 1.00 10.73  ? 2379 LEU A CD1   1 
ATOM   6718  C  CD2   . LEU A 1 2379 ? 237.000 267.747 236.907 1.00 8.54   ? 2379 LEU A CD2   1 
ATOM   6719  N  N     . ALA A 1 2380 ? 233.032 268.535 233.316 1.00 8.15   ? 2380 ALA A N     1 
ATOM   6720  C  CA    . ALA A 1 2380 ? 231.991 269.404 232.778 1.00 8.87   ? 2380 ALA A CA    1 
ATOM   6721  C  C     . ALA A 1 2380 ? 230.673 269.206 233.514 1.00 10.72  ? 2380 ALA A C     1 
ATOM   6722  O  O     . ALA A 1 2380 ? 229.985 270.179 233.843 1.00 14.58  ? 2380 ALA A O     1 
ATOM   6723  C  CB    . ALA A 1 2380 ? 231.815 269.148 231.282 1.00 8.40   ? 2380 ALA A CB    1 
ATOM   6724  N  N     . ARG A 1 2381 ? 230.307 267.950 233.787 1.00 9.89   ? 2381 ARG A N     1 
ATOM   6725  C  CA    . ARG A 1 2381 ? 229.086 267.690 234.541 1.00 10.52  ? 2381 ARG A CA    1 
ATOM   6726  C  C     . ARG A 1 2381 ? 229.180 268.256 235.952 1.00 12.90  ? 2381 ARG A C     1 
ATOM   6727  O  O     . ARG A 1 2381 ? 228.202 268.799 236.478 1.00 15.93  ? 2381 ARG A O     1 
ATOM   6728  C  CB    . ARG A 1 2381 ? 228.804 266.190 234.581 1.00 11.07  ? 2381 ARG A CB    1 
ATOM   6729  C  CG    . ARG A 1 2381 ? 228.442 265.593 233.236 1.00 10.79  ? 2381 ARG A CG    1 
ATOM   6730  C  CD    . ARG A 1 2381 ? 228.192 264.101 233.345 1.00 12.98  ? 2381 ARG A CD    1 
ATOM   6731  N  NE    . ARG A 1 2381 ? 227.119 263.801 234.284 1.00 18.63  ? 2381 ARG A NE    1 
ATOM   6732  C  CZ    . ARG A 1 2381 ? 225.827 263.906 234.003 1.00 19.36  ? 2381 ARG A CZ    1 
ATOM   6733  N  NH1   . ARG A 1 2381 ? 225.410 264.297 232.812 1.00 15.06  ? 2381 ARG A NH1   1 
ATOM   6734  N  NH2   . ARG A 1 2381 ? 224.934 263.613 234.942 1.00 27.56  ? 2381 ARG A NH2   1 
ATOM   6735  N  N     . LEU A 1 2382 ? 230.351 268.134 236.584 1.00 11.69  ? 2382 LEU A N     1 
ATOM   6736  C  CA    . LEU A 1 2382 ? 230.533 268.684 237.922 1.00 11.74  ? 2382 LEU A CA    1 
ATOM   6737  C  C     . LEU A 1 2382 ? 230.401 270.201 237.923 1.00 14.01  ? 2382 LEU A C     1 
ATOM   6738  O  O     . LEU A 1 2382 ? 229.785 270.778 238.826 1.00 16.76  ? 2382 LEU A O     1 
ATOM   6739  C  CB    . LEU A 1 2382 ? 231.894 268.261 238.477 1.00 11.48  ? 2382 LEU A CB    1 
ATOM   6740  C  CG    . LEU A 1 2382 ? 232.149 268.509 239.964 1.00 11.60  ? 2382 LEU A CG    1 
ATOM   6741  C  CD1   . LEU A 1 2382 ? 231.214 267.670 240.816 1.00 13.13  ? 2382 LEU A CD1   1 
ATOM   6742  C  CD2   . LEU A 1 2382 ? 233.597 268.210 240.302 1.00 12.07  ? 2382 LEU A CD2   1 
ATOM   6743  N  N     . ARG A 1 2383 ? 230.975 270.865 236.917 1.00 13.19  ? 2383 ARG A N     1 
ATOM   6744  C  CA    . ARG A 1 2383 ? 230.919 272.321 236.859 1.00 13.80  ? 2383 ARG A CA    1 
ATOM   6745  C  C     . ARG A 1 2383 ? 229.553 272.843 236.435 1.00 14.72  ? 2383 ARG A C     1 
ATOM   6746  O  O     . ARG A 1 2383 ? 229.227 273.995 236.737 1.00 15.56  ? 2383 ARG A O     1 
ATOM   6747  C  CB    . ARG A 1 2383 ? 231.987 272.855 235.906 1.00 10.97  ? 2383 ARG A CB    1 
ATOM   6748  C  CG    . ARG A 1 2383 ? 233.399 272.772 236.448 1.00 12.50  ? 2383 ARG A CG    1 
ATOM   6749  C  CD    . ARG A 1 2383 ? 234.408 273.186 235.398 1.00 12.61  ? 2383 ARG A CD    1 
ATOM   6750  N  NE    . ARG A 1 2383 ? 235.735 273.390 235.965 1.00 17.57  ? 2383 ARG A NE    1 
ATOM   6751  C  CZ    . ARG A 1 2383 ? 236.827 272.759 235.559 1.00 19.95  ? 2383 ARG A CZ    1 
ATOM   6752  N  NH1   . ARG A 1 2383 ? 236.785 271.857 234.593 1.00 11.91  ? 2383 ARG A NH1   1 
ATOM   6753  N  NH2   . ARG A 1 2383 ? 237.991 273.039 236.137 1.00 19.36  ? 2383 ARG A NH2   1 
ATOM   6754  N  N     . SER A 1 2384 ? 228.751 272.036 235.741 1.00 15.61  ? 2384 SER A N     1 
ATOM   6755  C  CA    . SER A 1 2384 ? 227.472 272.506 235.219 1.00 16.56  ? 2384 SER A CA    1 
ATOM   6756  C  C     . SER A 1 2384 ? 226.277 272.028 236.035 1.00 19.62  ? 2384 SER A C     1 
ATOM   6757  O  O     . SER A 1 2384 ? 225.393 272.826 236.359 1.00 21.76  ? 2384 SER A O     1 
ATOM   6758  C  CB    . SER A 1 2384 ? 227.314 272.065 233.760 1.00 17.80  ? 2384 SER A CB    1 
ATOM   6759  O  OG    . SER A 1 2384 ? 226.289 272.800 233.113 1.00 24.31  ? 2384 SER A OG    1 
ATOM   6760  N  N     . ILE A 1 2385 ? 226.226 270.745 236.372 1.00 18.57  ? 2385 ILE A N     1 
ATOM   6761  C  CA    . ILE A 1 2385 ? 225.052 270.141 236.992 1.00 18.63  ? 2385 ILE A CA    1 
ATOM   6762  C  C     . ILE A 1 2385 ? 225.204 270.240 238.507 1.00 22.77  ? 2385 ILE A C     1 
ATOM   6763  O  O     . ILE A 1 2385 ? 226.183 269.705 239.053 1.00 26.64  ? 2385 ILE A O     1 
ATOM   6764  C  CB    . ILE A 1 2385 ? 224.876 268.684 236.556 1.00 15.45  ? 2385 ILE A CB    1 
ATOM   6765  C  CG1   . ILE A 1 2385 ? 224.751 268.598 235.034 1.00 20.14  ? 2385 ILE A CG1   1 
ATOM   6766  C  CG2   . ILE A 1 2385 ? 223.662 268.073 237.230 1.00 15.55  ? 2385 ILE A CG2   1 
ATOM   6767  C  CD1   . ILE A 1 2385 ? 224.563 267.193 234.516 1.00 20.24  ? 2385 ILE A CD1   1 
ATOM   6768  N  N     . PRO A 1 2386 ? 224.289 270.903 239.211 1.00 21.99  ? 2386 PRO A N     1 
ATOM   6769  C  CA    . PRO A 1 2386 ? 224.335 270.889 240.676 1.00 23.12  ? 2386 PRO A CA    1 
ATOM   6770  C  C     . PRO A 1 2386 ? 224.035 269.503 241.227 1.00 23.51  ? 2386 PRO A C     1 
ATOM   6771  O  O     . PRO A 1 2386 ? 223.280 268.724 240.641 1.00 27.92  ? 2386 PRO A O     1 
ATOM   6772  C  CB    . PRO A 1 2386 ? 223.249 271.896 241.081 1.00 24.45  ? 2386 PRO A CB    1 
ATOM   6773  C  CG    . PRO A 1 2386 ? 222.896 272.639 239.829 1.00 22.32  ? 2386 PRO A CG    1 
ATOM   6774  C  CD    . PRO A 1 2386 ? 223.170 271.708 238.700 1.00 22.43  ? 2386 PRO A CD    1 
ATOM   6775  N  N     . LEU A 1 2387 ? 224.638 269.203 242.378 1.00 22.19  ? 2387 LEU A N     1 
ATOM   6776  C  CA    . LEU A 1 2387 ? 224.460 267.887 242.980 1.00 22.82  ? 2387 LEU A CA    1 
ATOM   6777  C  C     . LEU A 1 2387 ? 223.191 267.815 243.822 1.00 30.86  ? 2387 LEU A C     1 
ATOM   6778  O  O     . LEU A 1 2387 ? 222.569 266.752 243.920 1.00 32.86  ? 2387 LEU A O     1 
ATOM   6779  C  CB    . LEU A 1 2387 ? 225.682 267.528 243.823 1.00 17.83  ? 2387 LEU A CB    1 
ATOM   6780  C  CG    . LEU A 1 2387 ? 226.878 266.975 243.047 1.00 13.51  ? 2387 LEU A CG    1 
ATOM   6781  C  CD1   . LEU A 1 2387 ? 228.021 266.645 243.986 1.00 16.89  ? 2387 LEU A CD1   1 
ATOM   6782  C  CD2   . LEU A 1 2387 ? 226.474 265.755 242.238 1.00 12.95  ? 2387 LEU A CD2   1 
ATOM   6783  N  N     . ASP A 1 2388 ? 222.798 268.929 244.443 1.00 35.13  ? 2388 ASP A N     1 
ATOM   6784  C  CA    . ASP A 1 2388 ? 221.606 268.922 245.286 1.00 33.93  ? 2388 ASP A CA    1 
ATOM   6785  C  C     . ASP A 1 2388 ? 220.337 268.754 244.460 1.00 42.54  ? 2388 ASP A C     1 
ATOM   6786  O  O     . ASP A 1 2388 ? 219.391 268.086 244.895 1.00 50.50  ? 2388 ASP A O     1 
ATOM   6787  C  CB    . ASP A 1 2388 ? 221.545 270.202 246.119 1.00 31.28  ? 2388 ASP A CB    1 
ATOM   6788  C  CG    . ASP A 1 2388 ? 221.824 271.443 245.300 1.00 41.26  ? 2388 ASP A CG    1 
ATOM   6789  O  OD1   . ASP A 1 2388 ? 222.176 271.304 244.111 1.00 44.65  ? 2388 ASP A OD1   1 
ATOM   6790  O  OD2   . ASP A 1 2388 ? 221.690 272.557 245.845 1.00 54.37  ? 2388 ASP A OD2   1 
ATOM   6791  N  N     . SER A 1 2410 ? 223.746 279.220 243.039 1.00 37.26  ? 2410 SER A N     1 
ATOM   6792  C  CA    . SER A 1 2410 ? 223.663 278.106 243.975 1.00 34.97  ? 2410 SER A CA    1 
ATOM   6793  C  C     . SER A 1 2410 ? 225.011 277.843 244.634 1.00 30.94  ? 2410 SER A C     1 
ATOM   6794  O  O     . SER A 1 2410 ? 226.009 277.636 243.945 1.00 31.91  ? 2410 SER A O     1 
ATOM   6795  C  CB    . SER A 1 2410 ? 223.172 276.844 243.265 1.00 28.57  ? 2410 SER A CB    1 
ATOM   6796  O  OG    . SER A 1 2410 ? 223.142 275.739 244.152 1.00 35.73  ? 2410 SER A OG    1 
ATOM   6797  N  N     . PRO A 1 2411 ? 225.041 277.865 245.969 1.00 33.29  ? 2411 PRO A N     1 
ATOM   6798  C  CA    . PRO A 1 2411 ? 226.299 277.568 246.676 1.00 33.60  ? 2411 PRO A CA    1 
ATOM   6799  C  C     . PRO A 1 2411 ? 226.833 276.178 246.393 1.00 30.59  ? 2411 PRO A C     1 
ATOM   6800  O  O     . PRO A 1 2411 ? 228.056 275.985 246.362 1.00 34.83  ? 2411 PRO A O     1 
ATOM   6801  C  CB    . PRO A 1 2411 ? 225.918 277.741 248.153 1.00 32.35  ? 2411 PRO A CB    1 
ATOM   6802  C  CG    . PRO A 1 2411 ? 224.435 277.561 248.189 1.00 27.47  ? 2411 PRO A CG    1 
ATOM   6803  C  CD    . PRO A 1 2411 ? 223.927 278.118 246.898 1.00 31.52  ? 2411 PRO A CD    1 
ATOM   6804  N  N     . MET A 1 2412 ? 225.949 275.198 246.186 1.00 24.83  ? 2412 MET A N     1 
ATOM   6805  C  CA    . MET A 1 2412 ? 226.400 273.850 245.858 1.00 25.94  ? 2412 MET A CA    1 
ATOM   6806  C  C     . MET A 1 2412 ? 227.156 273.833 244.536 1.00 26.19  ? 2412 MET A C     1 
ATOM   6807  O  O     . MET A 1 2412 ? 228.195 273.174 244.412 1.00 26.16  ? 2412 MET A O     1 
ATOM   6808  C  CB    . MET A 1 2412 ? 225.205 272.898 245.806 1.00 28.39  ? 2412 MET A CB    1 
ATOM   6809  C  CG    . MET A 1 2412 ? 225.584 271.441 245.628 1.00 29.62  ? 2412 MET A CG    1 
ATOM   6810  S  SD    . MET A 1 2412 ? 226.478 270.815 247.060 1.00 39.85  ? 2412 MET A SD    1 
ATOM   6811  C  CE    . MET A 1 2412 ? 227.381 269.449 246.341 1.00 25.50  ? 2412 MET A CE    1 
ATOM   6812  N  N     . LEU A 1 2413 ? 226.648 274.558 243.536 1.00 27.03  ? 2413 LEU A N     1 
ATOM   6813  C  CA    . LEU A 1 2413 ? 227.339 274.636 242.254 1.00 21.47  ? 2413 LEU A CA    1 
ATOM   6814  C  C     . LEU A 1 2413 ? 228.684 275.336 242.395 1.00 22.32  ? 2413 LEU A C     1 
ATOM   6815  O  O     . LEU A 1 2413 ? 229.657 274.957 241.736 1.00 29.49  ? 2413 LEU A O     1 
ATOM   6816  C  CB    . LEU A 1 2413 ? 226.462 275.350 241.227 1.00 26.65  ? 2413 LEU A CB    1 
ATOM   6817  C  CG    . LEU A 1 2413 ? 226.789 275.087 239.756 1.00 23.52  ? 2413 LEU A CG    1 
ATOM   6818  C  CD1   . LEU A 1 2413 ? 226.800 273.597 239.472 1.00 21.79  ? 2413 LEU A CD1   1 
ATOM   6819  C  CD2   . LEU A 1 2413 ? 225.798 275.797 238.851 1.00 20.67  ? 2413 LEU A CD2   1 
ATOM   6820  N  N     . GLN A 1 2414 ? 228.758 276.362 243.247 1.00 25.79  ? 2414 GLN A N     1 
ATOM   6821  C  CA    . GLN A 1 2414 ? 230.035 277.026 243.492 1.00 28.78  ? 2414 GLN A CA    1 
ATOM   6822  C  C     . GLN A 1 2414 ? 231.039 276.073 244.128 1.00 28.42  ? 2414 GLN A C     1 
ATOM   6823  O  O     . GLN A 1 2414 ? 232.218 276.053 243.747 1.00 24.02  ? 2414 GLN A O     1 
ATOM   6824  C  CB    . GLN A 1 2414 ? 229.826 278.255 244.376 1.00 23.85  ? 2414 GLN A CB    1 
ATOM   6825  C  CG    . GLN A 1 2414 ? 231.068 279.113 244.551 1.00 25.57  ? 2414 GLN A CG    1 
ATOM   6826  C  CD    . GLN A 1 2414 ? 231.683 279.521 243.228 1.00 32.50  ? 2414 GLN A CD    1 
ATOM   6827  O  OE1   . GLN A 1 2414 ? 230.988 279.983 242.324 1.00 33.46  ? 2414 GLN A OE1   1 
ATOM   6828  N  NE2   . GLN A 1 2414 ? 232.994 279.356 243.110 1.00 37.02  ? 2414 GLN A NE2   1 
ATOM   6829  N  N     . ILE A 1 2415 ? 230.593 275.277 245.101 1.00 27.03  ? 2415 ILE A N     1 
ATOM   6830  C  CA    . ILE A 1 2415 ? 231.479 274.298 245.726 1.00 25.20  ? 2415 ILE A CA    1 
ATOM   6831  C  C     . ILE A 1 2415 ? 231.946 273.276 244.699 1.00 24.25  ? 2415 ILE A C     1 
ATOM   6832  O  O     . ILE A 1 2415 ? 233.125 272.899 244.666 1.00 25.84  ? 2415 ILE A O     1 
ATOM   6833  C  CB    . ILE A 1 2415 ? 230.776 273.622 246.918 1.00 26.87  ? 2415 ILE A CB    1 
ATOM   6834  C  CG1   . ILE A 1 2415 ? 230.563 274.624 248.052 1.00 22.55  ? 2415 ILE A CG1   1 
ATOM   6835  C  CG2   . ILE A 1 2415 ? 231.581 272.429 247.407 1.00 22.41  ? 2415 ILE A CG2   1 
ATOM   6836  C  CD1   . ILE A 1 2415 ? 229.626 274.129 249.127 1.00 20.21  ? 2415 ILE A CD1   1 
ATOM   6837  N  N     . GLN A 1 2416 ? 231.029 272.811 243.847 1.00 23.62  ? 2416 GLN A N     1 
ATOM   6838  C  CA    . GLN A 1 2416 ? 231.397 271.852 242.811 1.00 18.10  ? 2416 GLN A CA    1 
ATOM   6839  C  C     . GLN A 1 2416 ? 232.423 272.441 241.851 1.00 22.20  ? 2416 GLN A C     1 
ATOM   6840  O  O     . GLN A 1 2416 ? 233.383 271.766 241.469 1.00 24.88  ? 2416 GLN A O     1 
ATOM   6841  C  CB    . GLN A 1 2416 ? 230.152 271.399 242.051 1.00 18.47  ? 2416 GLN A CB    1 
ATOM   6842  C  CG    . GLN A 1 2416 ? 229.249 270.468 242.833 1.00 16.39  ? 2416 GLN A CG    1 
ATOM   6843  C  CD    . GLN A 1 2416 ? 227.903 270.276 242.166 1.00 18.62  ? 2416 GLN A CD    1 
ATOM   6844  O  OE1   . GLN A 1 2416 ? 226.860 270.372 242.809 1.00 22.47  ? 2416 GLN A OE1   1 
ATOM   6845  N  NE2   . GLN A 1 2416 ? 227.920 270.005 240.868 1.00 18.26  ? 2416 GLN A NE2   1 
ATOM   6846  N  N     . ARG A 1 2417 ? 232.231 273.699 241.446 1.00 26.26  ? 2417 ARG A N     1 
ATOM   6847  C  CA    . ARG A 1 2417 ? 233.171 274.339 240.529 1.00 19.17  ? 2417 ARG A CA    1 
ATOM   6848  C  C     . ARG A 1 2417 ? 234.541 274.512 241.170 1.00 19.41  ? 2417 ARG A C     1 
ATOM   6849  O  O     . ARG A 1 2417 ? 235.571 274.284 240.522 1.00 23.97  ? 2417 ARG A O     1 
ATOM   6850  C  CB    . ARG A 1 2417 ? 232.618 275.687 240.069 1.00 17.06  ? 2417 ARG A CB    1 
ATOM   6851  C  CG    . ARG A 1 2417 ? 231.450 275.575 239.107 1.00 14.03  ? 2417 ARG A CG    1 
ATOM   6852  C  CD    . ARG A 1 2417 ? 231.121 276.915 238.483 1.00 16.97  ? 2417 ARG A CD    1 
ATOM   6853  N  NE    . ARG A 1 2417 ? 230.111 276.792 237.440 1.00 19.48  ? 2417 ARG A NE    1 
ATOM   6854  C  CZ    . ARG A 1 2417 ? 228.904 277.339 237.497 1.00 23.12  ? 2417 ARG A CZ    1 
ATOM   6855  N  NH1   . ARG A 1 2417 ? 228.520 278.056 238.540 1.00 18.68  ? 2417 ARG A NH1   1 
ATOM   6856  N  NH2   . ARG A 1 2417 ? 228.063 277.161 236.483 1.00 23.64  ? 2417 ARG A NH2   1 
ATOM   6857  N  N     . ASP A 1 2418 ? 234.577 274.917 242.442 1.00 21.66  ? 2418 ASP A N     1 
ATOM   6858  C  CA    . ASP A 1 2418 ? 235.854 275.045 243.135 1.00 19.51  ? 2418 ASP A CA    1 
ATOM   6859  C  C     . ASP A 1 2418 ? 236.558 273.699 243.245 1.00 20.79  ? 2418 ASP A C     1 
ATOM   6860  O  O     . ASP A 1 2418 ? 237.770 273.602 243.018 1.00 20.31  ? 2418 ASP A O     1 
ATOM   6861  C  CB    . ASP A 1 2418 ? 235.642 275.657 244.519 1.00 25.90  ? 2418 ASP A CB    1 
ATOM   6862  C  CG    . ASP A 1 2418 ? 235.272 277.124 244.457 1.00 37.71  ? 2418 ASP A CG    1 
ATOM   6863  O  OD1   . ASP A 1 2418 ? 234.710 277.555 243.429 1.00 39.16  ? 2418 ASP A OD1   1 
ATOM   6864  O  OD2   . ASP A 1 2418 ? 235.543 277.848 245.436 1.00 40.92  ? 2418 ASP A OD2   1 
ATOM   6865  N  N     . ALA A 1 2419 ? 235.811 272.646 243.582 1.00 21.38  ? 2419 ALA A N     1 
ATOM   6866  C  CA    . ALA A 1 2419 ? 236.406 271.317 243.679 1.00 16.34  ? 2419 ALA A CA    1 
ATOM   6867  C  C     . ALA A 1 2419 ? 236.922 270.844 242.327 1.00 18.74  ? 2419 ALA A C     1 
ATOM   6868  O  O     . ALA A 1 2419 ? 237.984 270.217 242.246 1.00 18.14  ? 2419 ALA A O     1 
ATOM   6869  C  CB    . ALA A 1 2419 ? 235.392 270.326 244.246 1.00 19.43  ? 2419 ALA A CB    1 
ATOM   6870  N  N     . ALA A 1 2420 ? 236.176 271.124 241.255 1.00 20.45  ? 2420 ALA A N     1 
ATOM   6871  C  CA    . ALA A 1 2420 ? 236.628 270.757 239.917 1.00 16.14  ? 2420 ALA A CA    1 
ATOM   6872  C  C     . ALA A 1 2420 ? 237.907 271.494 239.550 1.00 18.33  ? 2420 ALA A C     1 
ATOM   6873  O  O     . ALA A 1 2420 ? 238.826 270.907 238.966 1.00 22.46  ? 2420 ALA A O     1 
ATOM   6874  C  CB    . ALA A 1 2420 ? 235.531 271.046 238.895 1.00 13.72  ? 2420 ALA A CB    1 
ATOM   6875  N  N     . THR A 1 2421 ? 237.987 272.782 239.888 1.00 18.65  ? 2421 THR A N     1 
ATOM   6876  C  CA    . THR A 1 2421 ? 239.215 273.534 239.648 1.00 18.59  ? 2421 THR A CA    1 
ATOM   6877  C  C     . THR A 1 2421 ? 240.383 272.948 240.429 1.00 18.34  ? 2421 THR A C     1 
ATOM   6878  O  O     . THR A 1 2421 ? 241.507 272.888 239.917 1.00 18.31  ? 2421 THR A O     1 
ATOM   6879  C  CB    . THR A 1 2421 ? 239.015 275.003 240.018 1.00 23.75  ? 2421 THR A CB    1 
ATOM   6880  O  OG1   . THR A 1 2421 ? 237.858 275.516 239.345 1.00 24.34  ? 2421 THR A OG1   1 
ATOM   6881  C  CG2   . THR A 1 2421 ? 240.230 275.825 239.617 1.00 27.23  ? 2421 THR A CG2   1 
ATOM   6882  N  N     . ILE A 1 2422 ? 240.136 272.512 241.665 1.00 21.40  ? 2422 ILE A N     1 
ATOM   6883  C  CA    . ILE A 1 2422 ? 241.208 271.940 242.476 1.00 18.98  ? 2422 ILE A CA    1 
ATOM   6884  C  C     . ILE A 1 2422 ? 241.669 270.602 241.909 1.00 18.72  ? 2422 ILE A C     1 
ATOM   6885  O  O     . ILE A 1 2422 ? 242.871 270.314 241.868 1.00 18.44  ? 2422 ILE A O     1 
ATOM   6886  C  CB    . ILE A 1 2422 ? 240.753 271.814 243.941 1.00 19.34  ? 2422 ILE A CB    1 
ATOM   6887  C  CG1   . ILE A 1 2422 ? 240.466 273.196 244.523 1.00 19.47  ? 2422 ILE A CG1   1 
ATOM   6888  C  CG2   . ILE A 1 2422 ? 241.809 271.102 244.772 1.00 23.82  ? 2422 ILE A CG2   1 
ATOM   6889  C  CD1   . ILE A 1 2422 ? 239.773 273.158 245.857 1.00 21.36  ? 2422 ILE A CD1   1 
ATOM   6890  N  N     . MET A 1 2423 ? 240.731 269.762 241.465 1.00 18.63  ? 2423 MET A N     1 
ATOM   6891  C  CA    . MET A 1 2423 ? 241.093 268.422 241.014 1.00 19.80  ? 2423 MET A CA    1 
ATOM   6892  C  C     . MET A 1 2423 ? 241.435 268.354 239.531 1.00 19.60  ? 2423 MET A C     1 
ATOM   6893  O  O     . MET A 1 2423 ? 241.777 267.270 239.046 1.00 21.49  ? 2423 MET A O     1 
ATOM   6894  C  CB    . MET A 1 2423 ? 239.970 267.423 241.317 1.00 16.26  ? 2423 MET A CB    1 
ATOM   6895  C  CG    . MET A 1 2423 ? 238.670 267.675 240.575 1.00 19.77  ? 2423 MET A CG    1 
ATOM   6896  S  SD    . MET A 1 2423 ? 237.366 266.525 241.053 1.00 24.96  ? 2423 MET A SD    1 
ATOM   6897  C  CE    . MET A 1 2423 ? 236.942 267.131 242.682 1.00 14.83  ? 2423 MET A CE    1 
ATOM   6898  N  N     . GLN A 1 2424 ? 241.338 269.465 238.802 1.00 18.13  ? 2424 GLN A N     1 
ATOM   6899  C  CA    . GLN A 1 2424 ? 241.730 269.482 237.393 1.00 16.66  ? 2424 GLN A CA    1 
ATOM   6900  C  C     . GLN A 1 2424 ? 243.156 269.005 237.132 1.00 19.61  ? 2424 GLN A C     1 
ATOM   6901  O  O     . GLN A 1 2424 ? 243.349 268.212 236.196 1.00 18.43  ? 2424 GLN A O     1 
ATOM   6902  C  CB    . GLN A 1 2424 ? 241.513 270.896 236.834 1.00 17.09  ? 2424 GLN A CB    1 
ATOM   6903  C  CG    . GLN A 1 2424 ? 242.016 271.088 235.415 1.00 19.84  ? 2424 GLN A CG    1 
ATOM   6904  C  CD    . GLN A 1 2424 ? 241.243 270.263 234.409 1.00 20.06  ? 2424 GLN A CD    1 
ATOM   6905  O  OE1   . GLN A 1 2424 ? 240.076 270.536 234.132 1.00 19.85  ? 2424 GLN A OE1   1 
ATOM   6906  N  NE2   . GLN A 1 2424 ? 241.890 269.245 233.857 1.00 19.95  ? 2424 GLN A NE2   1 
ATOM   6907  N  N     . PRO A 1 2425 ? 244.184 269.429 237.883 1.00 19.14  ? 2425 PRO A N     1 
ATOM   6908  C  CA    . PRO A 1 2425 ? 245.548 268.985 237.547 1.00 16.76  ? 2425 PRO A CA    1 
ATOM   6909  C  C     . PRO A 1 2425 ? 245.751 267.481 237.614 1.00 16.99  ? 2425 PRO A C     1 
ATOM   6910  O  O     . PRO A 1 2425 ? 246.653 266.961 236.946 1.00 17.45  ? 2425 PRO A O     1 
ATOM   6911  C  CB    . PRO A 1 2425 ? 246.417 269.709 238.586 1.00 13.20  ? 2425 PRO A CB    1 
ATOM   6912  C  CG    . PRO A 1 2425 ? 245.624 270.887 238.981 1.00 17.61  ? 2425 PRO A CG    1 
ATOM   6913  C  CD    . PRO A 1 2425 ? 244.200 270.437 238.959 1.00 16.77  ? 2425 PRO A CD    1 
ATOM   6914  N  N     . TYR A 1 2426 ? 244.953 266.766 238.402 1.00 18.82  ? 2426 TYR A N     1 
ATOM   6915  C  CA    . TYR A 1 2426 ? 245.122 265.327 238.552 1.00 18.10  ? 2426 TYR A CA    1 
ATOM   6916  C  C     . TYR A 1 2426 ? 244.342 264.516 237.526 1.00 18.30  ? 2426 TYR A C     1 
ATOM   6917  O  O     . TYR A 1 2426 ? 244.564 263.306 237.422 1.00 20.18  ? 2426 TYR A O     1 
ATOM   6918  C  CB    . TYR A 1 2426 ? 244.708 264.895 239.961 1.00 16.40  ? 2426 TYR A CB    1 
ATOM   6919  C  CG    . TYR A 1 2426 ? 245.374 265.695 241.053 1.00 16.85  ? 2426 TYR A CG    1 
ATOM   6920  C  CD1   . TYR A 1 2426 ? 246.687 265.438 241.425 1.00 13.09  ? 2426 TYR A CD1   1 
ATOM   6921  C  CD2   . TYR A 1 2426 ? 244.696 266.713 241.707 1.00 15.54  ? 2426 TYR A CD2   1 
ATOM   6922  C  CE1   . TYR A 1 2426 ? 247.302 266.170 242.419 1.00 16.11  ? 2426 TYR A CE1   1 
ATOM   6923  C  CE2   . TYR A 1 2426 ? 245.304 267.449 242.704 1.00 16.95  ? 2426 TYR A CE2   1 
ATOM   6924  C  CZ    . TYR A 1 2426 ? 246.605 267.173 243.055 1.00 18.74  ? 2426 TYR A CZ    1 
ATOM   6925  O  OH    . TYR A 1 2426 ? 247.216 267.903 244.047 1.00 30.86  ? 2426 TYR A OH    1 
ATOM   6926  N  N     . PHE A 1 2427 ? 243.449 265.147 236.764 1.00 18.81  ? 2427 PHE A N     1 
ATOM   6927  C  CA    . PHE A 1 2427 ? 242.626 264.458 235.780 1.00 13.20  ? 2427 PHE A CA    1 
ATOM   6928  C  C     . PHE A 1 2427 ? 243.090 264.720 234.352 1.00 18.84  ? 2427 PHE A C     1 
ATOM   6929  O  O     . PHE A 1 2427 ? 242.266 264.809 233.436 1.00 25.77  ? 2427 PHE A O     1 
ATOM   6930  C  CB    . PHE A 1 2427 ? 241.162 264.859 235.946 1.00 12.81  ? 2427 PHE A CB    1 
ATOM   6931  C  CG    . PHE A 1 2427 ? 240.450 264.116 237.036 1.00 13.33  ? 2427 PHE A CG    1 
ATOM   6932  C  CD1   . PHE A 1 2427 ? 240.235 262.754 236.936 1.00 11.84  ? 2427 PHE A CD1   1 
ATOM   6933  C  CD2   . PHE A 1 2427 ? 239.996 264.779 238.162 1.00 11.31  ? 2427 PHE A CD2   1 
ATOM   6934  C  CE1   . PHE A 1 2427 ? 239.578 262.067 237.936 1.00 10.67  ? 2427 PHE A CE1   1 
ATOM   6935  C  CE2   . PHE A 1 2427 ? 239.340 264.098 239.165 1.00 10.68  ? 2427 PHE A CE2   1 
ATOM   6936  C  CZ    . PHE A 1 2427 ? 239.131 262.741 239.051 1.00 10.78  ? 2427 PHE A CZ    1 
ATOM   6937  N  N     . THR A 1 2428 ? 244.395 264.847 234.146 1.00 21.26  ? 2428 THR A N     1 
ATOM   6938  C  CA    . THR A 1 2428 ? 244.966 265.100 232.835 1.00 28.15  ? 2428 THR A CA    1 
ATOM   6939  C  C     . THR A 1 2428 ? 245.690 263.859 232.330 1.00 33.95  ? 2428 THR A C     1 
ATOM   6940  O  O     . THR A 1 2428 ? 245.937 262.909 233.077 1.00 41.60  ? 2428 THR A O     1 
ATOM   6941  C  CB    . THR A 1 2428 ? 245.935 266.286 232.879 1.00 26.90  ? 2428 THR A CB    1 
ATOM   6942  O  OG1   . THR A 1 2428 ? 247.106 265.921 233.620 1.00 22.59  ? 2428 THR A OG1   1 
ATOM   6943  C  CG2   . THR A 1 2428 ? 245.276 267.484 233.543 1.00 22.60  ? 2428 THR A CG2   1 
ATOM   6944  N  N     . SER A 1 2429 ? 246.015 263.876 231.039 1.00 31.07  ? 2429 SER A N     1 
ATOM   6945  C  CA    . SER A 1 2429 ? 246.791 262.792 230.454 1.00 35.21  ? 2429 SER A CA    1 
ATOM   6946  C  C     . SER A 1 2429 ? 248.137 262.674 231.155 1.00 47.19  ? 2429 SER A C     1 
ATOM   6947  O  O     . SER A 1 2429 ? 248.795 263.678 231.444 1.00 48.26  ? 2429 SER A O     1 
ATOM   6948  C  CB    . SER A 1 2429 ? 246.992 263.031 228.957 1.00 43.62  ? 2429 SER A CB    1 
ATOM   6949  O  OG    . SER A 1 2429 ? 247.782 264.185 228.729 1.00 53.38  ? 2429 SER A OG    1 
ATOM   6950  N  N     . ASN A 1 2430 ? 248.544 261.434 231.429 1.00 38.74  ? 2430 ASN A N     1 
ATOM   6951  C  CA    . ASN A 1 2430 ? 249.733 261.136 232.224 1.00 40.64  ? 2430 ASN A CA    1 
ATOM   6952  C  C     . ASN A 1 2430 ? 249.675 261.825 233.587 1.00 45.40  ? 2430 ASN A C     1 
ATOM   6953  O  O     . ASN A 1 2430 ? 250.680 262.357 234.071 1.00 46.91  ? 2430 ASN A O     1 
ATOM   6954  C  CB    . ASN A 1 2430 ? 251.015 261.517 231.467 1.00 54.54  ? 2430 ASN A CB    1 
ATOM   6955  C  CG    . ASN A 1 2430 ? 252.278 260.973 232.120 1.00 60.85  ? 2430 ASN A CG    1 
ATOM   6956  O  OD1   . ASN A 1 2430 ? 252.226 260.311 233.156 1.00 60.47  ? 2430 ASN A OD1   1 
ATOM   6957  N  ND2   . ASN A 1 2430 ? 253.424 261.257 231.511 1.00 63.12  ? 2430 ASN A ND2   1 
ATOM   6958  N  N     . GLY A 1 2431 ? 248.497 261.853 234.201 1.00 41.26  ? 2431 GLY A N     1 
ATOM   6959  C  CA    . GLY A 1 2431 ? 248.311 262.443 235.509 1.00 29.03  ? 2431 GLY A CA    1 
ATOM   6960  C  C     . GLY A 1 2431 ? 248.322 261.406 236.610 1.00 26.87  ? 2431 GLY A C     1 
ATOM   6961  O  O     . GLY A 1 2431 ? 248.749 260.264 236.425 1.00 27.51  ? 2431 GLY A O     1 
ATOM   6962  N  N     . LEU A 1 2432 ? 247.845 261.820 237.785 1.00 25.33  ? 2432 LEU A N     1 
ATOM   6963  C  CA    . LEU A 1 2432 ? 247.799 260.909 238.924 1.00 16.05  ? 2432 LEU A CA    1 
ATOM   6964  C  C     . LEU A 1 2432 ? 246.774 259.804 238.701 1.00 20.18  ? 2432 LEU A C     1 
ATOM   6965  O  O     . LEU A 1 2432 ? 247.072 258.618 238.892 1.00 23.18  ? 2432 LEU A O     1 
ATOM   6966  C  CB    . LEU A 1 2432 ? 247.484 261.688 240.201 1.00 13.53  ? 2432 LEU A CB    1 
ATOM   6967  C  CG    . LEU A 1 2432 ? 247.060 260.873 241.422 1.00 20.74  ? 2432 LEU A CG    1 
ATOM   6968  C  CD1   . LEU A 1 2432 ? 248.223 260.053 241.955 1.00 19.65  ? 2432 LEU A CD1   1 
ATOM   6969  C  CD2   . LEU A 1 2432 ? 246.502 261.782 242.502 1.00 27.76  ? 2432 LEU A CD2   1 
ATOM   6970  N  N     . VAL A 1 2433 ? 245.562 260.173 238.283 1.00 17.45  ? 2433 VAL A N     1 
ATOM   6971  C  CA    . VAL A 1 2433 ? 244.493 259.192 238.123 1.00 12.63  ? 2433 VAL A CA    1 
ATOM   6972  C  C     . VAL A 1 2433 ? 244.817 258.217 236.999 1.00 14.29  ? 2433 VAL A C     1 
ATOM   6973  O  O     . VAL A 1 2433 ? 244.565 257.013 237.118 1.00 17.68  ? 2433 VAL A O     1 
ATOM   6974  C  CB    . VAL A 1 2433 ? 243.147 259.901 237.888 1.00 13.27  ? 2433 VAL A CB    1 
ATOM   6975  C  CG1   . VAL A 1 2433 ? 242.014 258.891 237.882 1.00 11.99  ? 2433 VAL A CG1   1 
ATOM   6976  C  CG2   . VAL A 1 2433 ? 242.912 260.955 238.954 1.00 14.56  ? 2433 VAL A CG2   1 
ATOM   6977  N  N     . THR A 1 2434 ? 245.370 258.713 235.891 1.00 21.24  ? 2434 THR A N     1 
ATOM   6978  C  CA    . THR A 1 2434 ? 245.667 257.842 234.758 1.00 17.75  ? 2434 THR A CA    1 
ATOM   6979  C  C     . THR A 1 2434 ? 246.736 256.815 235.113 1.00 16.80  ? 2434 THR A C     1 
ATOM   6980  O  O     . THR A 1 2434 ? 246.584 255.620 234.826 1.00 17.07  ? 2434 THR A O     1 
ATOM   6981  C  CB    . THR A 1 2434 ? 246.102 258.679 233.555 1.00 19.43  ? 2434 THR A CB    1 
ATOM   6982  O  OG1   . THR A 1 2434 ? 245.114 259.682 233.289 1.00 24.23  ? 2434 THR A OG1   1 
ATOM   6983  C  CG2   . THR A 1 2434 ? 246.264 257.800 232.326 1.00 21.32  ? 2434 THR A CG2   1 
ATOM   6984  N  N     . LYS A 1 2435 ? 247.829 257.261 235.736 1.00 16.96  ? 2435 LYS A N     1 
ATOM   6985  C  CA    . LYS A 1 2435 ? 248.881 256.333 236.139 1.00 17.94  ? 2435 LYS A CA    1 
ATOM   6986  C  C     . LYS A 1 2435 ? 248.384 255.366 237.205 1.00 16.22  ? 2435 LYS A C     1 
ATOM   6987  O  O     . LYS A 1 2435 ? 248.744 254.182 237.195 1.00 17.23  ? 2435 LYS A O     1 
ATOM   6988  C  CB    . LYS A 1 2435 ? 250.105 257.103 236.631 1.00 21.61  ? 2435 LYS A CB    1 
ATOM   6989  C  CG    . LYS A 1 2435 ? 250.764 257.956 235.561 1.00 30.32  ? 2435 LYS A CG    1 
ATOM   6990  C  CD    . LYS A 1 2435 ? 251.817 258.880 236.149 1.00 32.07  ? 2435 LYS A CD    1 
ATOM   6991  C  CE    . LYS A 1 2435 ? 253.131 258.158 236.366 1.00 33.51  ? 2435 LYS A CE    1 
ATOM   6992  N  NZ    . LYS A 1 2435 ? 254.201 259.093 236.804 1.00 43.97  ? 2435 LYS A NZ    1 
ATOM   6993  N  N     . ALA A 1 2436 ? 247.555 255.850 238.132 1.00 18.48  ? 2436 ALA A N     1 
ATOM   6994  C  CA    . ALA A 1 2436 ? 246.982 254.967 239.142 1.00 13.15  ? 2436 ALA A CA    1 
ATOM   6995  C  C     . ALA A 1 2436 ? 246.116 253.890 238.505 1.00 13.82  ? 2436 ALA A C     1 
ATOM   6996  O  O     . ALA A 1 2436 ? 246.173 252.724 238.905 1.00 18.41  ? 2436 ALA A O     1 
ATOM   6997  C  CB    . ALA A 1 2436 ? 246.175 255.780 240.152 1.00 12.85  ? 2436 ALA A CB    1 
ATOM   6998  N  N     . LEU A 1 2437 ? 245.301 254.262 237.515 1.00 12.23  ? 2437 LEU A N     1 
ATOM   6999  C  CA    . LEU A 1 2437 ? 244.463 253.284 236.827 1.00 10.89  ? 2437 LEU A CA    1 
ATOM   7000  C  C     . LEU A 1 2437 ? 245.307 252.283 236.049 1.00 11.98  ? 2437 LEU A C     1 
ATOM   7001  O  O     . LEU A 1 2437 ? 245.020 251.077 236.054 1.00 15.76  ? 2437 LEU A O     1 
ATOM   7002  C  CB    . LEU A 1 2437 ? 243.484 254.007 235.901 1.00 10.42  ? 2437 LEU A CB    1 
ATOM   7003  C  CG    . LEU A 1 2437 ? 242.425 253.183 235.171 1.00 10.80  ? 2437 LEU A CG    1 
ATOM   7004  C  CD1   . LEU A 1 2437 ? 241.405 252.629 236.148 1.00 13.81  ? 2437 LEU A CD1   1 
ATOM   7005  C  CD2   . LEU A 1 2437 ? 241.747 254.029 234.110 1.00 12.92  ? 2437 LEU A CD2   1 
ATOM   7006  N  N     . GLU A 1 2438 ? 246.358 252.765 235.382 1.00 16.23  ? 2438 GLU A N     1 
ATOM   7007  C  CA    . GLU A 1 2438 ? 247.244 251.870 234.646 1.00 16.69  ? 2438 GLU A CA    1 
ATOM   7008  C  C     . GLU A 1 2438 ? 247.909 250.870 235.580 1.00 15.11  ? 2438 GLU A C     1 
ATOM   7009  O  O     . GLU A 1 2438 ? 248.038 249.686 235.245 1.00 15.22  ? 2438 GLU A O     1 
ATOM   7010  C  CB    . GLU A 1 2438 ? 248.294 252.681 233.888 1.00 20.80  ? 2438 GLU A CB    1 
ATOM   7011  C  CG    . GLU A 1 2438 ? 249.111 251.869 232.896 1.00 34.91  ? 2438 GLU A CG    1 
ATOM   7012  C  CD    . GLU A 1 2438 ? 248.401 251.685 231.570 1.00 55.33  ? 2438 GLU A CD    1 
ATOM   7013  O  OE1   . GLU A 1 2438 ? 248.807 250.793 230.796 1.00 58.64  ? 2438 GLU A OE1   1 
ATOM   7014  O  OE2   . GLU A 1 2438 ? 247.436 252.433 231.300 1.00 51.45  ? 2438 GLU A OE2   1 
ATOM   7015  N  N     . HIS A 1 2439 ? 248.340 251.325 236.758 1.00 15.04  ? 2439 HIS A N     1 
ATOM   7016  C  CA    . HIS A 1 2439 ? 248.952 250.414 237.719 1.00 16.47  ? 2439 HIS A CA    1 
ATOM   7017  C  C     . HIS A 1 2439 ? 247.927 249.444 238.296 1.00 17.60  ? 2439 HIS A C     1 
ATOM   7018  O  O     . HIS A 1 2439 ? 248.224 248.259 238.482 1.00 18.41  ? 2439 HIS A O     1 
ATOM   7019  C  CB    . HIS A 1 2439 ? 249.628 251.203 238.836 1.00 16.75  ? 2439 HIS A CB    1 
ATOM   7020  C  CG    . HIS A 1 2439 ? 250.425 250.354 239.775 1.00 24.58  ? 2439 HIS A CG    1 
ATOM   7021  N  ND1   . HIS A 1 2439 ? 251.655 249.832 239.442 1.00 23.51  ? 2439 HIS A ND1   1 
ATOM   7022  C  CD2   . HIS A 1 2439 ? 250.165 249.930 241.035 1.00 28.11  ? 2439 HIS A CD2   1 
ATOM   7023  C  CE1   . HIS A 1 2439 ? 252.121 249.125 240.456 1.00 28.94  ? 2439 HIS A CE1   1 
ATOM   7024  N  NE2   . HIS A 1 2439 ? 251.236 249.169 241.435 1.00 28.51  ? 2439 HIS A NE2   1 
ATOM   7025  N  N     . ALA A 1 2440 ? 246.720 249.931 238.591 1.00 17.87  ? 2440 ALA A N     1 
ATOM   7026  C  CA    . ALA A 1 2440 ? 245.687 249.078 239.166 1.00 13.54  ? 2440 ALA A CA    1 
ATOM   7027  C  C     . ALA A 1 2440 ? 245.250 247.994 238.195 1.00 12.97  ? 2440 ALA A C     1 
ATOM   7028  O  O     . ALA A 1 2440 ? 244.833 246.913 238.624 1.00 17.22  ? 2440 ALA A O     1 
ATOM   7029  C  CB    . ALA A 1 2440 ? 244.489 249.921 239.598 1.00 13.27  ? 2440 ALA A CB    1 
ATOM   7030  N  N     . PHE A 1 2441 ? 245.332 248.258 236.889 1.00 14.36  ? 2441 PHE A N     1 
ATOM   7031  C  CA    . PHE A 1 2441 ? 245.023 247.213 235.920 1.00 14.51  ? 2441 PHE A CA    1 
ATOM   7032  C  C     . PHE A 1 2441 ? 246.013 246.057 235.985 1.00 16.44  ? 2441 PHE A C     1 
ATOM   7033  O  O     . PHE A 1 2441 ? 245.732 244.983 235.443 1.00 12.94  ? 2441 PHE A O     1 
ATOM   7034  C  CB    . PHE A 1 2441 ? 244.987 247.789 234.506 1.00 13.93  ? 2441 PHE A CB    1 
ATOM   7035  C  CG    . PHE A 1 2441 ? 243.609 248.149 234.036 1.00 16.71  ? 2441 PHE A CG    1 
ATOM   7036  C  CD1   . PHE A 1 2441 ? 242.746 247.173 233.574 1.00 17.75  ? 2441 PHE A CD1   1 
ATOM   7037  C  CD2   . PHE A 1 2441 ? 243.180 249.464 234.048 1.00 14.04  ? 2441 PHE A CD2   1 
ATOM   7038  C  CE1   . PHE A 1 2441 ? 241.476 247.499 233.139 1.00 17.55  ? 2441 PHE A CE1   1 
ATOM   7039  C  CE2   . PHE A 1 2441 ? 241.913 249.797 233.613 1.00 17.53  ? 2441 PHE A CE2   1 
ATOM   7040  C  CZ    . PHE A 1 2441 ? 241.061 248.813 233.158 1.00 15.95  ? 2441 PHE A CZ    1 
ATOM   7041  N  N     . GLN A 1 2442 ? 247.163 246.249 236.629 1.00 20.35  ? 2442 GLN A N     1 
ATOM   7042  C  CA    . GLN A 1 2442 ? 248.161 245.202 236.790 1.00 14.95  ? 2442 GLN A CA    1 
ATOM   7043  C  C     . GLN A 1 2442 ? 248.015 244.435 238.097 1.00 16.54  ? 2442 GLN A C     1 
ATOM   7044  O  O     . GLN A 1 2442 ? 248.817 243.533 238.361 1.00 18.62  ? 2442 GLN A O     1 
ATOM   7045  C  CB    . GLN A 1 2442 ? 249.569 245.799 236.701 1.00 18.42  ? 2442 GLN A CB    1 
ATOM   7046  C  CG    . GLN A 1 2442 ? 249.917 246.370 235.336 1.00 23.88  ? 2442 GLN A CG    1 
ATOM   7047  C  CD    . GLN A 1 2442 ? 249.577 245.421 234.203 1.00 26.30  ? 2442 GLN A CD    1 
ATOM   7048  O  OE1   . GLN A 1 2442 ? 250.017 244.272 234.188 1.00 26.80  ? 2442 GLN A OE1   1 
ATOM   7049  N  NE2   . GLN A 1 2442 ? 248.791 245.899 233.246 1.00 21.55  ? 2442 GLN A NE2   1 
ATOM   7050  N  N     . LEU A 1 2443 ? 247.026 244.768 238.921 1.00 18.69  ? 2443 LEU A N     1 
ATOM   7051  C  CA    . LEU A 1 2443 ? 246.806 244.083 240.182 1.00 15.33  ? 2443 LEU A CA    1 
ATOM   7052  C  C     . LEU A 1 2443 ? 245.782 242.963 240.009 1.00 17.21  ? 2443 LEU A C     1 
ATOM   7053  O  O     . LEU A 1 2443 ? 245.213 242.763 238.933 1.00 19.02  ? 2443 LEU A O     1 
ATOM   7054  C  CB    . LEU A 1 2443 ? 246.358 245.070 241.258 1.00 15.08  ? 2443 LEU A CB    1 
ATOM   7055  C  CG    . LEU A 1 2443 ? 247.248 246.290 241.498 1.00 17.08  ? 2443 LEU A CG    1 
ATOM   7056  C  CD1   . LEU A 1 2443 ? 246.648 247.178 242.575 1.00 15.50  ? 2443 LEU A CD1   1 
ATOM   7057  C  CD2   . LEU A 1 2443 ? 248.653 245.860 241.878 1.00 21.07  ? 2443 LEU A CD2   1 
ATOM   7058  N  N     . GLU A 1 2444 ? 245.542 242.222 241.086 1.00 13.77  ? 2444 GLU A N     1 
ATOM   7059  C  CA    . GLU A 1 2444 ? 244.577 241.131 241.102 1.00 13.14  ? 2444 GLU A CA    1 
ATOM   7060  C  C     . GLU A 1 2444 ? 243.332 241.593 241.843 1.00 15.83  ? 2444 GLU A C     1 
ATOM   7061  O  O     . GLU A 1 2444 ? 243.424 242.089 242.971 1.00 16.06  ? 2444 GLU A O     1 
ATOM   7062  C  CB    . GLU A 1 2444 ? 245.169 239.884 241.757 1.00 15.57  ? 2444 GLU A CB    1 
ATOM   7063  C  CG    . GLU A 1 2444 ? 246.300 239.251 240.967 1.00 27.08  ? 2444 GLU A CG    1 
ATOM   7064  C  CD    . GLU A 1 2444 ? 246.879 238.029 241.650 1.00 55.09  ? 2444 GLU A CD    1 
ATOM   7065  O  OE1   . GLU A 1 2444 ? 246.484 237.745 242.800 1.00 58.30  ? 2444 GLU A OE1   1 
ATOM   7066  O  OE2   . GLU A 1 2444 ? 247.731 237.353 241.037 1.00 60.48  ? 2444 GLU A OE2   1 
ATOM   7067  N  N     . HIS A 1 2445 ? 242.175 241.431 241.211 1.00 11.26  ? 2445 HIS A N     1 
ATOM   7068  C  CA    . HIS A 1 2445 ? 240.906 241.866 241.769 1.00 8.80   ? 2445 HIS A CA    1 
ATOM   7069  C  C     . HIS A 1 2445 ? 239.945 240.688 241.834 1.00 9.18   ? 2445 HIS A C     1 
ATOM   7070  O  O     . HIS A 1 2445 ? 240.055 239.732 241.061 1.00 12.22  ? 2445 HIS A O     1 
ATOM   7071  C  CB    . HIS A 1 2445 ? 240.297 243.000 240.936 1.00 9.37   ? 2445 HIS A CB    1 
ATOM   7072  C  CG    . HIS A 1 2445 ? 241.239 244.137 240.684 1.00 11.33  ? 2445 HIS A CG    1 
ATOM   7073  N  ND1   . HIS A 1 2445 ? 241.491 245.117 241.618 1.00 13.97  ? 2445 HIS A ND1   1 
ATOM   7074  C  CD2   . HIS A 1 2445 ? 241.994 244.445 239.603 1.00 9.80   ? 2445 HIS A CD2   1 
ATOM   7075  C  CE1   . HIS A 1 2445 ? 242.358 245.982 241.123 1.00 11.82  ? 2445 HIS A CE1   1 
ATOM   7076  N  NE2   . HIS A 1 2445 ? 242.679 245.596 239.903 1.00 10.05  ? 2445 HIS A NE2   1 
ATOM   7077  N  N     . ILE A 1 2446 ? 238.997 240.764 242.772 1.00 7.44   ? 2446 ILE A N     1 
ATOM   7078  C  CA    . ILE A 1 2446 ? 238.031 239.686 242.942 1.00 7.27   ? 2446 ILE A CA    1 
ATOM   7079  C  C     . ILE A 1 2446 ? 237.129 239.545 241.721 1.00 9.08   ? 2446 ILE A C     1 
ATOM   7080  O  O     . ILE A 1 2446 ? 236.542 238.479 241.509 1.00 11.22  ? 2446 ILE A O     1 
ATOM   7081  C  CB    . ILE A 1 2446 ? 237.207 239.905 244.226 1.00 7.58   ? 2446 ILE A CB    1 
ATOM   7082  C  CG1   . ILE A 1 2446 ? 236.696 238.570 244.769 1.00 8.24   ? 2446 ILE A CG1   1 
ATOM   7083  C  CG2   . ILE A 1 2446 ? 236.054 240.865 243.979 1.00 8.34   ? 2446 ILE A CG2   1 
ATOM   7084  C  CD1   . ILE A 1 2446 ? 237.795 237.578 245.073 1.00 7.88   ? 2446 ILE A CD1   1 
ATOM   7085  N  N     . MET A 1 2447 ? 237.006 240.592 240.910 1.00 8.51   ? 2447 MET A N     1 
ATOM   7086  C  CA    . MET A 1 2447 ? 236.281 240.532 239.652 1.00 6.98   ? 2447 MET A CA    1 
ATOM   7087  C  C     . MET A 1 2447 ? 237.119 241.177 238.559 1.00 9.76   ? 2447 MET A C     1 
ATOM   7088  O  O     . MET A 1 2447 ? 238.122 241.840 238.828 1.00 10.90  ? 2447 MET A O     1 
ATOM   7089  C  CB    . MET A 1 2447 ? 234.919 241.229 239.738 1.00 9.26   ? 2447 MET A CB    1 
ATOM   7090  C  CG    . MET A 1 2447 ? 233.924 240.540 240.642 1.00 7.90   ? 2447 MET A CG    1 
ATOM   7091  S  SD    . MET A 1 2447 ? 232.362 241.426 240.686 1.00 27.83  ? 2447 MET A SD    1 
ATOM   7092  C  CE    . MET A 1 2447 ? 231.471 240.444 241.877 1.00 15.13  ? 2447 MET A CE    1 
ATOM   7093  N  N     . ASP A 1 2448 ? 236.695 240.965 237.316 1.00 14.19  ? 2448 ASP A N     1 
ATOM   7094  C  CA    . ASP A 1 2448 ? 237.373 241.580 236.185 1.00 11.47  ? 2448 ASP A CA    1 
ATOM   7095  C  C     . ASP A 1 2448 ? 237.301 243.097 236.297 1.00 13.33  ? 2448 ASP A C     1 
ATOM   7096  O  O     . ASP A 1 2448 ? 236.232 243.667 236.529 1.00 17.09  ? 2448 ASP A O     1 
ATOM   7097  C  CB    . ASP A 1 2448 ? 236.744 241.113 234.874 1.00 9.63   ? 2448 ASP A CB    1 
ATOM   7098  C  CG    . ASP A 1 2448 ? 237.233 239.743 234.450 1.00 24.49  ? 2448 ASP A CG    1 
ATOM   7099  O  OD1   . ASP A 1 2448 ? 237.018 239.372 233.279 1.00 29.52  ? 2448 ASP A OD1   1 
ATOM   7100  O  OD2   . ASP A 1 2448 ? 237.834 239.039 235.288 1.00 33.91  ? 2448 ASP A OD2   1 
ATOM   7101  N  N     . LEU A 1 2449 ? 238.446 243.750 236.130 1.00 11.81  ? 2449 LEU A N     1 
ATOM   7102  C  CA    . LEU A 1 2449 ? 238.538 245.193 236.285 1.00 10.16  ? 2449 LEU A CA    1 
ATOM   7103  C  C     . LEU A 1 2449 ? 238.265 245.881 234.956 1.00 14.13  ? 2449 LEU A C     1 
ATOM   7104  O  O     . LEU A 1 2449 ? 238.920 245.591 233.950 1.00 14.60  ? 2449 LEU A O     1 
ATOM   7105  C  CB    . LEU A 1 2449 ? 239.914 245.597 236.809 1.00 12.49  ? 2449 LEU A CB    1 
ATOM   7106  C  CG    . LEU A 1 2449 ? 239.984 246.987 237.440 1.00 12.16  ? 2449 LEU A CG    1 
ATOM   7107  C  CD1   . LEU A 1 2449 ? 239.453 246.950 238.862 1.00 14.22  ? 2449 LEU A CD1   1 
ATOM   7108  C  CD2   . LEU A 1 2449 ? 241.403 247.528 237.405 1.00 11.96  ? 2449 LEU A CD2   1 
ATOM   7109  N  N     . THR A 1 2450 ? 237.299 246.792 234.960 1.00 15.66  ? 2450 THR A N     1 
ATOM   7110  C  CA    . THR A 1 2450 ? 237.003 247.634 233.813 1.00 12.99  ? 2450 THR A CA    1 
ATOM   7111  C  C     . THR A 1 2450 ? 237.243 249.087 234.194 1.00 11.27  ? 2450 THR A C     1 
ATOM   7112  O  O     . THR A 1 2450 ? 237.113 249.469 235.361 1.00 13.89  ? 2450 THR A O     1 
ATOM   7113  C  CB    . THR A 1 2450 ? 235.561 247.449 233.327 1.00 12.76  ? 2450 THR A CB    1 
ATOM   7114  O  OG1   . THR A 1 2450 ? 234.650 247.844 234.360 1.00 21.11  ? 2450 THR A OG1   1 
ATOM   7115  C  CG2   . THR A 1 2450 ? 235.308 245.999 232.955 1.00 12.43  ? 2450 THR A CG2   1 
ATOM   7116  N  N     . ARG A 1 2451 ? 237.606 249.890 233.194 1.00 10.28  ? 2451 ARG A N     1 
ATOM   7117  C  CA    . ARG A 1 2451 ? 237.968 251.278 233.454 1.00 10.43  ? 2451 ARG A CA    1 
ATOM   7118  C  C     . ARG A 1 2451 ? 236.793 252.067 234.019 1.00 10.11  ? 2451 ARG A C     1 
ATOM   7119  O  O     . ARG A 1 2451 ? 236.952 252.826 234.984 1.00 12.67  ? 2451 ARG A O     1 
ATOM   7120  C  CB    . ARG A 1 2451 ? 238.490 251.919 232.168 1.00 11.48  ? 2451 ARG A CB    1 
ATOM   7121  C  CG    . ARG A 1 2451 ? 238.617 253.425 232.216 1.00 11.23  ? 2451 ARG A CG    1 
ATOM   7122  C  CD    . ARG A 1 2451 ? 239.010 253.974 230.858 1.00 16.19  ? 2451 ARG A CD    1 
ATOM   7123  N  NE    . ARG A 1 2451 ? 238.079 253.571 229.811 1.00 18.67  ? 2451 ARG A NE    1 
ATOM   7124  C  CZ    . ARG A 1 2451 ? 238.173 253.945 228.542 1.00 11.43  ? 2451 ARG A CZ    1 
ATOM   7125  N  NH1   . ARG A 1 2451 ? 239.150 254.731 228.125 1.00 8.61   ? 2451 ARG A NH1   1 
ATOM   7126  N  NH2   . ARG A 1 2451 ? 237.263 253.520 227.670 1.00 9.06   ? 2451 ARG A NH2   1 
ATOM   7127  N  N     . LEU A 1 2452 ? 235.599 251.884 233.451 1.00 9.17   ? 2452 LEU A N     1 
ATOM   7128  C  CA    . LEU A 1 2452 ? 234.475 252.720 233.857 1.00 7.58   ? 2452 LEU A CA    1 
ATOM   7129  C  C     . LEU A 1 2452 ? 233.938 252.352 235.231 1.00 7.31   ? 2452 LEU A C     1 
ATOM   7130  O  O     . LEU A 1 2452 ? 233.371 253.212 235.904 1.00 9.95   ? 2452 LEU A O     1 
ATOM   7131  C  CB    . LEU A 1 2452 ? 233.350 252.670 232.829 1.00 8.11   ? 2452 LEU A CB    1 
ATOM   7132  C  CG    . LEU A 1 2452 ? 233.686 253.312 231.488 1.00 6.59   ? 2452 LEU A CG    1 
ATOM   7133  C  CD1   . LEU A 1 2452 ? 232.540 253.102 230.549 1.00 6.38   ? 2452 LEU A CD1   1 
ATOM   7134  C  CD2   . LEU A 1 2452 ? 233.965 254.789 231.666 1.00 7.60   ? 2452 LEU A CD2   1 
ATOM   7135  N  N     . ARG A 1 2453 ? 234.100 251.105 235.676 1.00 8.37   ? 2453 ARG A N     1 
ATOM   7136  C  CA    . ARG A 1 2453 ? 233.687 250.778 237.038 1.00 8.06   ? 2453 ARG A CA    1 
ATOM   7137  C  C     . ARG A 1 2453 ? 234.471 251.605 238.050 1.00 9.14   ? 2453 ARG A C     1 
ATOM   7138  O  O     . ARG A 1 2453 ? 233.888 252.286 238.907 1.00 9.86   ? 2453 ARG A O     1 
ATOM   7139  C  CB    . ARG A 1 2453 ? 233.868 249.284 237.305 1.00 7.06   ? 2453 ARG A CB    1 
ATOM   7140  C  CG    . ARG A 1 2453 ? 233.755 248.920 238.775 1.00 8.50   ? 2453 ARG A CG    1 
ATOM   7141  C  CD    . ARG A 1 2453 ? 233.448 247.448 238.977 1.00 5.97   ? 2453 ARG A CD    1 
ATOM   7142  N  NE    . ARG A 1 2453 ? 234.563 246.585 238.611 1.00 10.43  ? 2453 ARG A NE    1 
ATOM   7143  C  CZ    . ARG A 1 2453 ? 235.477 246.148 239.466 1.00 9.17   ? 2453 ARG A CZ    1 
ATOM   7144  N  NH1   . ARG A 1 2453 ? 235.453 246.497 240.741 1.00 5.93   ? 2453 ARG A NH1   1 
ATOM   7145  N  NH2   . ARG A 1 2453 ? 236.439 245.340 239.030 1.00 10.09  ? 2453 ARG A NH2   1 
ATOM   7146  N  N     . CYS A 1 2454 ? 235.801 251.584 237.938 1.00 11.03  ? 2454 CYS A N     1 
ATOM   7147  C  CA    . CYS A 1 2454 ? 236.639 252.375 238.831 1.00 9.59   ? 2454 CYS A CA    1 
ATOM   7148  C  C     . CYS A 1 2454 ? 236.374 253.864 238.662 1.00 9.58   ? 2454 CYS A C     1 
ATOM   7149  O  O     . CYS A 1 2454 ? 236.324 254.609 239.648 1.00 9.18   ? 2454 CYS A O     1 
ATOM   7150  C  CB    . CYS A 1 2454 ? 238.115 252.070 238.573 1.00 7.99   ? 2454 CYS A CB    1 
ATOM   7151  S  SG    . CYS A 1 2454 ? 238.488 250.330 238.307 1.00 39.60  ? 2454 CYS A SG    1 
ATOM   7152  N  N     . LEU A 1 2455 ? 236.214 254.320 237.416 1.00 8.39   ? 2455 LEU A N     1 
ATOM   7153  C  CA    . LEU A 1 2455 ? 236.003 255.745 237.184 1.00 6.35   ? 2455 LEU A CA    1 
ATOM   7154  C  C     . LEU A 1 2455 ? 234.684 256.222 237.781 1.00 6.23   ? 2455 LEU A C     1 
ATOM   7155  O  O     . LEU A 1 2455 ? 234.633 257.286 238.404 1.00 11.13  ? 2455 LEU A O     1 
ATOM   7156  C  CB    . LEU A 1 2455 ? 236.070 256.048 235.689 1.00 9.04   ? 2455 LEU A CB    1 
ATOM   7157  C  CG    . LEU A 1 2455 ? 237.474 256.005 235.080 1.00 7.52   ? 2455 LEU A CG    1 
ATOM   7158  C  CD1   . LEU A 1 2455 ? 237.509 256.732 233.749 1.00 10.53  ? 2455 LEU A CD1   1 
ATOM   7159  C  CD2   . LEU A 1 2455 ? 238.497 256.594 236.038 1.00 6.53   ? 2455 LEU A CD2   1 
ATOM   7160  N  N     . GLY A 1 2456 ? 233.610 255.450 237.610 1.00 4.63   ? 2456 GLY A N     1 
ATOM   7161  C  CA    . GLY A 1 2456 ? 232.338 255.826 238.200 1.00 6.21   ? 2456 GLY A CA    1 
ATOM   7162  C  C     . GLY A 1 2456 ? 232.364 255.779 239.712 1.00 7.43   ? 2456 GLY A C     1 
ATOM   7163  O  O     . GLY A 1 2456 ? 231.767 256.631 240.379 1.00 9.23   ? 2456 GLY A O     1 
ATOM   7164  N  N     . SER A 1 2457 ? 233.061 254.790 240.280 1.00 8.39   ? 2457 SER A N     1 
ATOM   7165  C  CA    . SER A 1 2457 ? 233.240 254.763 241.726 1.00 5.97   ? 2457 SER A CA    1 
ATOM   7166  C  C     . SER A 1 2457 ? 233.937 256.029 242.206 1.00 8.85   ? 2457 SER A C     1 
ATOM   7167  O  O     . SER A 1 2457 ? 233.488 256.683 243.156 1.00 12.50  ? 2457 SER A O     1 
ATOM   7168  C  CB    . SER A 1 2457 ? 234.041 253.526 242.126 1.00 5.81   ? 2457 SER A CB    1 
ATOM   7169  O  OG    . SER A 1 2457 ? 233.527 252.368 241.499 1.00 13.93  ? 2457 SER A OG    1 
ATOM   7170  N  N     . LEU A 1 2458 ? 235.026 256.405 241.531 1.00 6.10   ? 2458 LEU A N     1 
ATOM   7171  C  CA    . LEU A 1 2458 ? 235.775 257.597 241.914 1.00 5.18   ? 2458 LEU A CA    1 
ATOM   7172  C  C     . LEU A 1 2458 ? 234.922 258.852 241.784 1.00 8.00   ? 2458 LEU A C     1 
ATOM   7173  O  O     . LEU A 1 2458 ? 234.959 259.730 242.654 1.00 10.63  ? 2458 LEU A O     1 
ATOM   7174  C  CB    . LEU A 1 2458 ? 237.039 257.704 241.059 1.00 6.24   ? 2458 LEU A CB    1 
ATOM   7175  C  CG    . LEU A 1 2458 ? 237.836 259.008 241.071 1.00 7.17   ? 2458 LEU A CG    1 
ATOM   7176  C  CD1   . LEU A 1 2458 ? 238.436 259.255 242.440 1.00 8.88   ? 2458 LEU A CD1   1 
ATOM   7177  C  CD2   . LEU A 1 2458 ? 238.923 258.963 240.017 1.00 7.71   ? 2458 LEU A CD2   1 
ATOM   7178  N  N     . PHE A 1 2459 ? 234.144 258.952 240.705 1.00 6.45   ? 2459 PHE A N     1 
ATOM   7179  C  CA    . PHE A 1 2459 ? 233.299 260.125 240.503 1.00 7.09   ? 2459 PHE A CA    1 
ATOM   7180  C  C     . PHE A 1 2459 ? 232.226 260.224 241.580 1.00 8.96   ? 2459 PHE A C     1 
ATOM   7181  O  O     . PHE A 1 2459 ? 231.933 261.319 242.076 1.00 11.71  ? 2459 PHE A O     1 
ATOM   7182  C  CB    . PHE A 1 2459 ? 232.666 260.081 239.112 1.00 5.76   ? 2459 PHE A CB    1 
ATOM   7183  C  CG    . PHE A 1 2459 ? 233.664 260.078 237.988 1.00 5.12   ? 2459 PHE A CG    1 
ATOM   7184  C  CD1   . PHE A 1 2459 ? 234.942 260.577 238.173 1.00 4.50   ? 2459 PHE A CD1   1 
ATOM   7185  C  CD2   . PHE A 1 2459 ? 233.327 259.564 236.748 1.00 4.94   ? 2459 PHE A CD2   1 
ATOM   7186  C  CE1   . PHE A 1 2459 ? 235.860 260.569 237.144 1.00 5.33   ? 2459 PHE A CE1   1 
ATOM   7187  C  CE2   . PHE A 1 2459 ? 234.241 259.553 235.715 1.00 4.09   ? 2459 PHE A CE2   1 
ATOM   7188  C  CZ    . PHE A 1 2459 ? 235.508 260.057 235.913 1.00 5.24   ? 2459 PHE A CZ    1 
ATOM   7189  N  N     . SER A 1 2460 ? 231.627 259.092 241.955 1.00 7.20   ? 2460 SER A N     1 
ATOM   7190  C  CA    . SER A 1 2460 ? 230.634 259.103 243.022 1.00 6.11   ? 2460 SER A CA    1 
ATOM   7191  C  C     . SER A 1 2460 ? 231.254 259.515 244.351 1.00 12.07  ? 2460 SER A C     1 
ATOM   7192  O  O     . SER A 1 2460 ? 230.650 260.276 245.118 1.00 12.39  ? 2460 SER A O     1 
ATOM   7193  C  CB    . SER A 1 2460 ? 229.973 257.731 243.137 1.00 8.01   ? 2460 SER A CB    1 
ATOM   7194  O  OG    . SER A 1 2460 ? 229.250 257.419 241.960 1.00 11.66  ? 2460 SER A OG    1 
ATOM   7195  N  N     . MET A 1 2461 ? 232.462 259.029 244.644 1.00 9.55   ? 2461 MET A N     1 
ATOM   7196  C  CA    . MET A 1 2461 ? 233.113 259.429 245.889 1.00 8.19   ? 2461 MET A CA    1 
ATOM   7197  C  C     . MET A 1 2461 ? 233.477 260.911 245.878 1.00 8.65   ? 2461 MET A C     1 
ATOM   7198  O  O     . MET A 1 2461 ? 233.413 261.577 246.915 1.00 14.19  ? 2461 MET A O     1 
ATOM   7199  C  CB    . MET A 1 2461 ? 234.346 258.563 246.155 1.00 10.31  ? 2461 MET A CB    1 
ATOM   7200  C  CG    . MET A 1 2461 ? 234.084 257.070 246.043 1.00 7.16   ? 2461 MET A CG    1 
ATOM   7201  S  SD    . MET A 1 2461 ? 235.376 256.049 246.764 1.00 8.84   ? 2461 MET A SD    1 
ATOM   7202  C  CE    . MET A 1 2461 ? 235.714 256.966 248.258 1.00 10.63  ? 2461 MET A CE    1 
ATOM   7203  N  N     . LEU A 1 2462 ? 233.851 261.454 244.718 1.00 8.90   ? 2462 LEU A N     1 
ATOM   7204  C  CA    . LEU A 1 2462 ? 234.131 262.886 244.645 1.00 8.71   ? 2462 LEU A CA    1 
ATOM   7205  C  C     . LEU A 1 2462 ? 232.858 263.712 244.815 1.00 10.26  ? 2462 LEU A C     1 
ATOM   7206  O  O     . LEU A 1 2462 ? 232.881 264.783 245.436 1.00 14.06  ? 2462 LEU A O     1 
ATOM   7207  C  CB    . LEU A 1 2462 ? 234.828 263.222 243.328 1.00 6.73   ? 2462 LEU A CB    1 
ATOM   7208  C  CG    . LEU A 1 2462 ? 236.211 262.589 243.153 1.00 7.72   ? 2462 LEU A CG    1 
ATOM   7209  C  CD1   . LEU A 1 2462 ? 236.780 262.892 241.779 1.00 7.82   ? 2462 LEU A CD1   1 
ATOM   7210  C  CD2   . LEU A 1 2462 ? 237.159 263.051 244.247 1.00 8.26   ? 2462 LEU A CD2   1 
ATOM   7211  N  N     . HIS A 1 2463 ? 231.738 263.232 244.271 1.00 8.63   ? 2463 HIS A N     1 
ATOM   7212  C  CA    . HIS A 1 2463 ? 230.458 263.886 244.528 1.00 11.87  ? 2463 HIS A CA    1 
ATOM   7213  C  C     . HIS A 1 2463 ? 230.124 263.861 246.014 1.00 13.83  ? 2463 HIS A C     1 
ATOM   7214  O  O     . HIS A 1 2463 ? 229.618 264.846 246.566 1.00 15.38  ? 2463 HIS A O     1 
ATOM   7215  C  CB    . HIS A 1 2463 ? 229.348 263.215 243.719 1.00 11.10  ? 2463 HIS A CB    1 
ATOM   7216  C  CG    . HIS A 1 2463 ? 229.424 263.481 242.249 1.00 10.92  ? 2463 HIS A CG    1 
ATOM   7217  N  ND1   . HIS A 1 2463 ? 228.675 262.780 241.329 1.00 9.42   ? 2463 HIS A ND1   1 
ATOM   7218  C  CD2   . HIS A 1 2463 ? 230.154 264.372 241.540 1.00 13.53  ? 2463 HIS A CD2   1 
ATOM   7219  C  CE1   . HIS A 1 2463 ? 228.944 263.227 240.115 1.00 15.95  ? 2463 HIS A CE1   1 
ATOM   7220  N  NE2   . HIS A 1 2463 ? 229.838 264.193 240.215 1.00 17.86  ? 2463 HIS A NE2   1 
ATOM   7221  N  N     . GLN A 1 2464 ? 230.399 262.736 246.675 1.00 16.81  ? 2464 GLN A N     1 
ATOM   7222  C  CA    . GLN A 1 2464 ? 230.200 262.657 248.118 1.00 16.98  ? 2464 GLN A CA    1 
ATOM   7223  C  C     . GLN A 1 2464 ? 231.106 263.633 248.857 1.00 17.27  ? 2464 GLN A C     1 
ATOM   7224  O  O     . GLN A 1 2464 ? 230.708 264.211 249.872 1.00 23.15  ? 2464 GLN A O     1 
ATOM   7225  C  CB    . GLN A 1 2464 ? 230.437 261.229 248.606 1.00 17.79  ? 2464 GLN A CB    1 
ATOM   7226  C  CG    . GLN A 1 2464 ? 230.005 260.987 250.042 1.00 20.05  ? 2464 GLN A CG    1 
ATOM   7227  C  CD    . GLN A 1 2464 ? 228.581 261.430 250.308 1.00 26.80  ? 2464 GLN A CD    1 
ATOM   7228  O  OE1   . GLN A 1 2464 ? 227.667 261.117 249.546 1.00 23.61  ? 2464 GLN A OE1   1 
ATOM   7229  N  NE2   . GLN A 1 2464 ? 228.385 262.165 251.396 1.00 25.30  ? 2464 GLN A NE2   1 
ATOM   7230  N  N     . ALA A 1 2465 ? 232.336 263.818 248.374 1.00 13.04  ? 2465 ALA A N     1 
ATOM   7231  C  CA    . ALA A 1 2465 ? 233.233 264.798 248.985 1.00 13.25  ? 2465 ALA A CA    1 
ATOM   7232  C  C     . ALA A 1 2465 ? 232.682 266.213 248.851 1.00 13.91  ? 2465 ALA A C     1 
ATOM   7233  O  O     . ALA A 1 2465 ? 232.753 267.015 249.792 1.00 17.73  ? 2465 ALA A O     1 
ATOM   7234  C  CB    . ALA A 1 2465 ? 234.619 264.705 248.353 1.00 12.79  ? 2465 ALA A CB    1 
ATOM   7235  N  N     . CYS A 1 2466 ? 232.140 266.543 247.677 1.00 14.45  ? 2466 CYS A N     1 
ATOM   7236  C  CA    . CYS A 1 2466 ? 231.516 267.851 247.498 1.00 17.32  ? 2466 CYS A CA    1 
ATOM   7237  C  C     . CYS A 1 2466 ? 230.321 268.019 248.429 1.00 18.30  ? 2466 CYS A C     1 
ATOM   7238  O  O     . CYS A 1 2466 ? 230.116 269.096 249.006 1.00 18.93  ? 2466 CYS A O     1 
ATOM   7239  C  CB    . CYS A 1 2466 ? 231.097 268.039 246.040 1.00 15.93  ? 2466 CYS A CB    1 
ATOM   7240  S  SG    . CYS A 1 2466 ? 232.474 268.111 244.876 1.00 25.70  ? 2466 CYS A SG    1 
ATOM   7241  N  N     . ARG A 1 2467 ? 229.521 266.963 248.591 1.00 15.22  ? 2467 ARG A N     1 
ATOM   7242  C  CA    . ARG A 1 2467 ? 228.401 267.025 249.525 1.00 20.47  ? 2467 ARG A CA    1 
ATOM   7243  C  C     . ARG A 1 2467 ? 228.886 267.185 250.962 1.00 21.86  ? 2467 ARG A C     1 
ATOM   7244  O  O     . ARG A 1 2467 ? 228.237 267.850 251.774 1.00 25.70  ? 2467 ARG A O     1 
ATOM   7245  C  CB    . ARG A 1 2467 ? 227.529 265.779 249.387 1.00 18.28  ? 2467 ARG A CB    1 
ATOM   7246  C  CG    . ARG A 1 2467 ? 226.685 265.761 248.126 1.00 19.23  ? 2467 ARG A CG    1 
ATOM   7247  C  CD    . ARG A 1 2467 ? 225.855 264.497 248.042 1.00 24.65  ? 2467 ARG A CD    1 
ATOM   7248  N  NE    . ARG A 1 2467 ? 225.321 264.280 246.704 1.00 29.01  ? 2467 ARG A NE    1 
ATOM   7249  C  CZ    . ARG A 1 2467 ? 224.205 264.829 246.243 1.00 31.77  ? 2467 ARG A CZ    1 
ATOM   7250  N  NH1   . ARG A 1 2467 ? 223.477 265.643 246.989 1.00 29.31  ? 2467 ARG A NH1   1 
ATOM   7251  N  NH2   . ARG A 1 2467 ? 223.809 264.550 245.005 1.00 28.24  ? 2467 ARG A NH2   1 
ATOM   7252  N  N     . ASN A 1 2468 ? 230.022 266.569 251.295 1.00 16.74  ? 2468 ASN A N     1 
ATOM   7253  C  CA    . ASN A 1 2468 ? 230.608 266.746 252.620 1.00 17.98  ? 2468 ASN A CA    1 
ATOM   7254  C  C     . ASN A 1 2468 ? 231.017 268.194 252.847 1.00 20.26  ? 2468 ASN A C     1 
ATOM   7255  O  O     . ASN A 1 2468 ? 230.803 268.748 253.932 1.00 28.36  ? 2468 ASN A O     1 
ATOM   7256  C  CB    . ASN A 1 2468 ? 231.811 265.820 252.792 1.00 18.31  ? 2468 ASN A CB    1 
ATOM   7257  C  CG    . ASN A 1 2468 ? 231.421 264.358 252.823 1.00 19.13  ? 2468 ASN A CG    1 
ATOM   7258  O  OD1   . ASN A 1 2468 ? 230.240 264.019 252.831 1.00 29.30  ? 2468 ASN A OD1   1 
ATOM   7259  N  ND2   . ASN A 1 2468 ? 232.417 263.482 252.835 1.00 16.85  ? 2468 ASN A ND2   1 
ATOM   7260  N  N     . VAL A 1 2469 ? 231.618 268.821 251.835 1.00 19.61  ? 2469 VAL A N     1 
ATOM   7261  C  CA    . VAL A 1 2469 ? 231.980 270.233 251.948 1.00 22.99  ? 2469 VAL A CA    1 
ATOM   7262  C  C     . VAL A 1 2469 ? 230.730 271.090 252.117 1.00 24.12  ? 2469 VAL A C     1 
ATOM   7263  O  O     . VAL A 1 2469 ? 230.710 272.043 252.908 1.00 27.14  ? 2469 VAL A O     1 
ATOM   7264  C  CB    . VAL A 1 2469 ? 232.813 270.674 250.732 1.00 22.22  ? 2469 VAL A CB    1 
ATOM   7265  C  CG1   . VAL A 1 2469 ? 233.115 272.161 250.807 1.00 23.89  ? 2469 VAL A CG1   1 
ATOM   7266  C  CG2   . VAL A 1 2469 ? 234.098 269.875 250.661 1.00 18.40  ? 2469 VAL A CG2   1 
ATOM   7267  N  N     . ALA A 1 2470 ? 229.670 270.767 251.373 1.00 24.60  ? 2470 ALA A N     1 
ATOM   7268  C  CA    . ALA A 1 2470 ? 228.417 271.506 251.512 1.00 22.05  ? 2470 ALA A CA    1 
ATOM   7269  C  C     . ALA A 1 2470 ? 227.837 271.354 252.913 1.00 28.56  ? 2470 ALA A C     1 
ATOM   7270  O  O     . ALA A 1 2470 ? 227.333 272.323 253.495 1.00 33.55  ? 2470 ALA A O     1 
ATOM   7271  C  CB    . ALA A 1 2470 ? 227.412 271.036 250.464 1.00 17.72  ? 2470 ALA A CB    1 
ATOM   7272  N  N     . GLN A 1 2471 ? 227.888 270.142 253.467 1.00 35.34  ? 2471 GLN A N     1 
ATOM   7273  C  CA    . GLN A 1 2471 ? 227.401 269.919 254.825 1.00 34.47  ? 2471 GLN A CA    1 
ATOM   7274  C  C     . GLN A 1 2471 ? 228.241 270.680 255.842 1.00 34.04  ? 2471 GLN A C     1 
ATOM   7275  O  O     . GLN A 1 2471 ? 227.706 271.205 256.825 1.00 43.50  ? 2471 GLN A O     1 
ATOM   7276  C  CB    . GLN A 1 2471 ? 227.394 268.425 255.145 1.00 37.80  ? 2471 GLN A CB    1 
ATOM   7277  C  CG    . GLN A 1 2471 ? 226.680 268.074 256.440 1.00 42.39  ? 2471 GLN A CG    1 
ATOM   7278  C  CD    . GLN A 1 2471 ? 226.462 266.583 256.602 1.00 54.04  ? 2471 GLN A CD    1 
ATOM   7279  O  OE1   . GLN A 1 2471 ? 227.263 265.773 256.137 1.00 54.01  ? 2471 GLN A OE1   1 
ATOM   7280  N  NE2   . GLN A 1 2471 ? 225.375 266.214 257.267 1.00 56.68  ? 2471 GLN A NE2   1 
ATOM   7281  N  N     . TYR A 1 2472 ? 229.558 270.736 255.633 1.00 30.23  ? 2472 TYR A N     1 
ATOM   7282  C  CA    . TYR A 1 2472 ? 230.411 271.532 256.510 1.00 31.44  ? 2472 TYR A CA    1 
ATOM   7283  C  C     . TYR A 1 2472 ? 230.030 273.004 256.455 1.00 30.01  ? 2472 TYR A C     1 
ATOM   7284  O  O     . TYR A 1 2472 ? 229.973 273.679 257.489 1.00 35.31  ? 2472 TYR A O     1 
ATOM   7285  C  CB    . TYR A 1 2472 ? 231.878 271.351 256.125 1.00 34.52  ? 2472 TYR A CB    1 
ATOM   7286  C  CG    . TYR A 1 2472 ? 232.841 272.109 257.008 1.00 37.80  ? 2472 TYR A CG    1 
ATOM   7287  C  CD1   . TYR A 1 2472 ? 233.147 271.659 258.284 1.00 43.14  ? 2472 TYR A CD1   1 
ATOM   7288  C  CD2   . TYR A 1 2472 ? 233.440 273.282 256.569 1.00 37.00  ? 2472 TYR A CD2   1 
ATOM   7289  C  CE1   . TYR A 1 2472 ? 234.026 272.348 259.095 1.00 43.19  ? 2472 TYR A CE1   1 
ATOM   7290  C  CE2   . TYR A 1 2472 ? 234.320 273.979 257.373 1.00 39.70  ? 2472 TYR A CE2   1 
ATOM   7291  C  CZ    . TYR A 1 2472 ? 234.608 273.508 258.635 1.00 44.96  ? 2472 TYR A CZ    1 
ATOM   7292  O  OH    . TYR A 1 2472 ? 235.485 274.199 259.442 1.00 50.95  ? 2472 TYR A OH    1 
ATOM   7293  N  N     . ASN A 1 2473 ? 229.774 273.520 255.251 1.00 36.02  ? 2473 ASN A N     1 
ATOM   7294  C  CA    . ASN A 1 2473 ? 229.376 274.918 255.114 1.00 34.31  ? 2473 ASN A CA    1 
ATOM   7295  C  C     . ASN A 1 2473 ? 228.034 275.180 255.786 1.00 33.23  ? 2473 ASN A C     1 
ATOM   7296  O  O     . ASN A 1 2473 ? 227.836 276.228 256.411 1.00 34.08  ? 2473 ASN A O     1 
ATOM   7297  C  CB    . ASN A 1 2473 ? 229.321 275.307 253.638 1.00 30.63  ? 2473 ASN A CB    1 
ATOM   7298  C  CG    . ASN A 1 2473 ? 230.684 275.651 253.080 1.00 36.84  ? 2473 ASN A CG    1 
ATOM   7299  O  OD1   . ASN A 1 2473 ? 231.681 275.641 253.799 1.00 38.80  ? 2473 ASN A OD1   1 
ATOM   7300  N  ND2   . ASN A 1 2473 ? 230.733 275.963 251.791 1.00 44.19  ? 2473 ASN A ND2   1 
ATOM   7301  N  N     . ALA A 1 2474 ? 227.094 274.242 255.658 1.00 34.86  ? 2474 ALA A N     1 
ATOM   7302  C  CA    . ALA A 1 2474 ? 225.796 274.397 256.308 1.00 36.97  ? 2474 ALA A CA    1 
ATOM   7303  C  C     . ALA A 1 2474 ? 225.926 274.352 257.826 1.00 40.05  ? 2474 ALA A C     1 
ATOM   7304  O  O     . ALA A 1 2474 ? 225.241 275.097 258.536 1.00 42.88  ? 2474 ALA A O     1 
ATOM   7305  C  CB    . ALA A 1 2474 ? 224.830 273.321 255.817 1.00 30.63  ? 2474 ALA A CB    1 
ATOM   7306  N  N     . ASN A 1 2475 ? 226.796 273.481 258.341 1.00 38.80  ? 2475 ASN A N     1 
ATOM   7307  C  CA    . ASN A 1 2475 ? 226.992 273.369 259.781 1.00 40.24  ? 2475 ASN A CA    1 
ATOM   7308  C  C     . ASN A 1 2475 ? 227.698 274.584 260.369 1.00 43.08  ? 2475 ASN A C     1 
ATOM   7309  O  O     . ASN A 1 2475 ? 227.568 274.838 261.571 1.00 45.25  ? 2475 ASN A O     1 
ATOM   7310  C  CB    . ASN A 1 2475 ? 227.792 272.107 260.106 1.00 43.56  ? 2475 ASN A CB    1 
ATOM   7311  C  CG    . ASN A 1 2475 ? 226.912 270.887 260.282 1.00 52.07  ? 2475 ASN A CG    1 
ATOM   7312  O  OD1   . ASN A 1 2475 ? 225.704 271.001 260.492 1.00 58.85  ? 2475 ASN A OD1   1 
ATOM   7313  N  ND2   . ASN A 1 2475 ? 227.514 269.707 260.197 1.00 44.37  ? 2475 ASN A ND2   1 
ATOM   7314  N  N     . HIS A 1 2476 ? 228.436 275.336 259.555 1.00 42.88  ? 2476 HIS A N     1 
ATOM   7315  C  CA    . HIS A 1 2476 ? 229.208 276.490 260.012 1.00 44.49  ? 2476 HIS A CA    1 
ATOM   7316  C  C     . HIS A 1 2476 ? 228.815 277.706 259.182 1.00 54.28  ? 2476 HIS A C     1 
ATOM   7317  O  O     . HIS A 1 2476 ? 229.571 278.152 258.312 1.00 58.38  ? 2476 HIS A O     1 
ATOM   7318  C  CB    . HIS A 1 2476 ? 230.711 276.227 259.905 1.00 41.17  ? 2476 HIS A CB    1 
ATOM   7319  C  CG    . HIS A 1 2476 ? 231.218 275.188 260.856 1.00 47.08  ? 2476 HIS A CG    1 
ATOM   7320  N  ND1   . HIS A 1 2476 ? 230.646 273.940 260.975 1.00 42.32  ? 2476 HIS A ND1   1 
ATOM   7321  C  CD2   . HIS A 1 2476 ? 232.258 275.208 261.725 1.00 46.54  ? 2476 HIS A CD2   1 
ATOM   7322  C  CE1   . HIS A 1 2476 ? 231.304 273.240 261.881 1.00 43.28  ? 2476 HIS A CE1   1 
ATOM   7323  N  NE2   . HIS A 1 2476 ? 232.287 273.987 262.351 1.00 45.18  ? 2476 HIS A NE2   1 
ATOM   7324  N  N     . PRO A 1 2477 ? 227.623 278.261 259.420 1.00 52.93  ? 2477 PRO A N     1 
ATOM   7325  C  CA    . PRO A 1 2477 ? 227.203 279.439 258.646 1.00 52.86  ? 2477 PRO A CA    1 
ATOM   7326  C  C     . PRO A 1 2477 ? 228.115 280.638 258.831 1.00 63.77  ? 2477 PRO A C     1 
ATOM   7327  O  O     . PRO A 1 2477 ? 228.284 281.429 257.894 1.00 64.98  ? 2477 PRO A O     1 
ATOM   7328  C  CB    . PRO A 1 2477 ? 225.786 279.719 259.172 1.00 54.76  ? 2477 PRO A CB    1 
ATOM   7329  C  CG    . PRO A 1 2477 ? 225.365 278.457 259.871 1.00 52.29  ? 2477 PRO A CG    1 
ATOM   7330  C  CD    . PRO A 1 2477 ? 226.619 277.874 260.424 1.00 45.68  ? 2477 PRO A CD    1 
ATOM   7331  N  N     . ASP A 1 2478 ? 228.707 280.799 260.016 1.00 63.47  ? 2478 ASP A N     1 
ATOM   7332  C  CA    . ASP A 1 2478 ? 229.561 281.954 260.268 1.00 73.69  ? 2478 ASP A CA    1 
ATOM   7333  C  C     . ASP A 1 2478 ? 230.910 281.814 259.573 1.00 72.35  ? 2478 ASP A C     1 
ATOM   7334  O  O     . ASP A 1 2478 ? 231.468 282.803 259.083 1.00 70.75  ? 2478 ASP A O     1 
ATOM   7335  C  CB    . ASP A 1 2478 ? 229.749 282.141 261.774 1.00 82.20  ? 2478 ASP A CB    1 
ATOM   7336  C  CG    . ASP A 1 2478 ? 230.319 283.503 262.131 1.00 91.16  ? 2478 ASP A CG    1 
ATOM   7337  O  OD1   . ASP A 1 2478 ? 230.508 284.334 261.218 1.00 86.19  ? 2478 ASP A OD1   1 
ATOM   7338  O  OD2   . ASP A 1 2478 ? 230.575 283.742 263.329 1.00 96.85  ? 2478 ASP A OD2   1 
ATOM   7339  N  N     . PHE A 1 2479 ? 231.450 280.598 259.515 1.00 67.51  ? 2479 PHE A N     1 
ATOM   7340  C  CA    . PHE A 1 2479 ? 232.788 280.346 258.980 1.00 63.03  ? 2479 PHE A CA    1 
ATOM   7341  C  C     . PHE A 1 2479 ? 232.715 279.270 257.907 1.00 63.91  ? 2479 PHE A C     1 
ATOM   7342  O  O     . PHE A 1 2479 ? 232.963 278.086 258.178 1.00 62.03  ? 2479 PHE A O     1 
ATOM   7343  C  CB    . PHE A 1 2479 ? 233.759 279.947 260.091 1.00 67.11  ? 2479 PHE A CB    1 
ATOM   7344  C  CG    . PHE A 1 2479 ? 234.148 281.081 260.992 1.00 69.47  ? 2479 PHE A CG    1 
ATOM   7345  C  CD1   . PHE A 1 2479 ? 234.914 282.129 260.512 1.00 68.73  ? 2479 PHE A CD1   1 
ATOM   7346  C  CD2   . PHE A 1 2479 ? 233.747 281.102 262.316 1.00 74.06  ? 2479 PHE A CD2   1 
ATOM   7347  C  CE1   . PHE A 1 2479 ? 235.273 283.178 261.337 1.00 74.98  ? 2479 PHE A CE1   1 
ATOM   7348  C  CE2   . PHE A 1 2479 ? 234.104 282.147 263.146 1.00 74.69  ? 2479 PHE A CE2   1 
ATOM   7349  C  CZ    . PHE A 1 2479 ? 234.868 283.186 262.655 1.00 79.11  ? 2479 PHE A CZ    1 
ATOM   7350  N  N     . PRO A 1 2480 ? 232.378 279.644 256.675 1.00 60.83  ? 2480 PRO A N     1 
ATOM   7351  C  CA    . PRO A 1 2480 ? 232.393 278.672 255.579 1.00 55.16  ? 2480 PRO A CA    1 
ATOM   7352  C  C     . PRO A 1 2480 ? 233.810 278.219 255.263 1.00 51.95  ? 2480 PRO A C     1 
ATOM   7353  O  O     . PRO A 1 2480 ? 234.792 278.918 255.525 1.00 55.13  ? 2480 PRO A O     1 
ATOM   7354  C  CB    . PRO A 1 2480 ? 231.782 279.447 254.408 1.00 50.35  ? 2480 PRO A CB    1 
ATOM   7355  C  CG    . PRO A 1 2480 ? 232.091 280.872 254.712 1.00 57.84  ? 2480 PRO A CG    1 
ATOM   7356  C  CD    . PRO A 1 2480 ? 232.028 280.997 256.212 1.00 59.13  ? 2480 PRO A CD    1 
ATOM   7357  N  N     . MET A 1 2481 ? 233.903 277.016 254.702 1.00 43.62  ? 2481 MET A N     1 
ATOM   7358  C  CA    . MET A 1 2481 ? 235.200 276.441 254.370 1.00 41.39  ? 2481 MET A CA    1 
ATOM   7359  C  C     . MET A 1 2481 ? 235.928 277.314 253.357 1.00 46.10  ? 2481 MET A C     1 
ATOM   7360  O  O     . MET A 1 2481 ? 235.351 277.734 252.349 1.00 49.57  ? 2481 MET A O     1 
ATOM   7361  C  CB    . MET A 1 2481 ? 235.021 275.026 253.824 1.00 34.37  ? 2481 MET A CB    1 
ATOM   7362  C  CG    . MET A 1 2481 ? 236.313 274.243 253.703 1.00 33.76  ? 2481 MET A CG    1 
ATOM   7363  S  SD    . MET A 1 2481 ? 236.118 272.732 252.745 1.00 44.41  ? 2481 MET A SD    1 
ATOM   7364  C  CE    . MET A 1 2481 ? 235.786 271.549 254.046 1.00 34.31  ? 2481 MET A CE    1 
ATOM   7365  N  N     . GLN A 1 2482 ? 237.200 277.587 253.628 1.00 47.54  ? 2482 GLN A N     1 
ATOM   7366  C  CA    . GLN A 1 2482 ? 237.990 278.469 252.785 1.00 48.88  ? 2482 GLN A CA    1 
ATOM   7367  C  C     . GLN A 1 2482 ? 238.689 277.677 251.683 1.00 43.31  ? 2482 GLN A C     1 
ATOM   7368  O  O     . GLN A 1 2482 ? 238.630 276.446 251.629 1.00 42.90  ? 2482 GLN A O     1 
ATOM   7369  C  CB    . GLN A 1 2482 ? 239.008 279.241 253.627 1.00 50.03  ? 2482 GLN A CB    1 
ATOM   7370  C  CG    . GLN A 1 2482 ? 238.423 280.073 254.781 1.00 52.57  ? 2482 GLN A CG    1 
ATOM   7371  C  CD    . GLN A 1 2482 ? 237.239 280.965 254.407 1.00 53.30  ? 2482 GLN A CD    1 
ATOM   7372  O  OE1   . GLN A 1 2482 ? 236.925 281.171 253.234 1.00 50.74  ? 2482 GLN A OE1   1 
ATOM   7373  N  NE2   . GLN A 1 2482 ? 236.572 281.497 255.425 1.00 52.63  ? 2482 GLN A NE2   1 
ATOM   7374  N  N     . ILE A 1 2483 ? 239.361 278.408 250.792 1.00 43.99  ? 2483 ILE A N     1 
ATOM   7375  C  CA    . ILE A 1 2483 ? 239.938 277.788 249.604 1.00 41.12  ? 2483 ILE A CA    1 
ATOM   7376  C  C     . ILE A 1 2483 ? 241.103 276.869 249.961 1.00 41.92  ? 2483 ILE A C     1 
ATOM   7377  O  O     . ILE A 1 2483 ? 241.300 275.835 249.315 1.00 40.11  ? 2483 ILE A O     1 
ATOM   7378  C  CB    . ILE A 1 2483 ? 240.345 278.868 248.583 1.00 43.16  ? 2483 ILE A CB    1 
ATOM   7379  C  CG1   . ILE A 1 2483 ? 240.653 278.233 247.225 1.00 48.07  ? 2483 ILE A CG1   1 
ATOM   7380  C  CG2   . ILE A 1 2483 ? 241.522 279.697 249.087 1.00 44.66  ? 2483 ILE A CG2   1 
ATOM   7381  C  CD1   . ILE A 1 2483 ? 239.447 277.604 246.562 1.00 35.54  ? 2483 ILE A CD1   1 
ATOM   7382  N  N     . GLU A 1 2484 ? 241.887 277.213 250.985 1.00 39.07  ? 2484 GLU A N     1 
ATOM   7383  C  CA    . GLU A 1 2484 ? 243.032 276.380 251.351 1.00 40.66  ? 2484 GLU A CA    1 
ATOM   7384  C  C     . GLU A 1 2484 ? 242.581 275.079 252.005 1.00 42.77  ? 2484 GLU A C     1 
ATOM   7385  O  O     . GLU A 1 2484 ? 243.080 273.993 251.671 1.00 40.03  ? 2484 GLU A O     1 
ATOM   7386  C  CB    . GLU A 1 2484 ? 243.962 277.160 252.280 1.00 42.08  ? 2484 GLU A CB    1 
ATOM   7387  C  CG    . GLU A 1 2484 ? 244.648 278.342 251.613 1.00 56.47  ? 2484 GLU A CG    1 
ATOM   7388  C  CD    . GLU A 1 2484 ? 245.548 279.108 252.562 1.00 70.15  ? 2484 GLU A CD    1 
ATOM   7389  O  OE1   . GLU A 1 2484 ? 245.544 278.794 253.770 1.00 71.04  ? 2484 GLU A OE1   1 
ATOM   7390  O  OE2   . GLU A 1 2484 ? 246.261 280.023 252.099 1.00 67.31  ? 2484 GLU A OE2   1 
ATOM   7391  N  N     . GLN A 1 2485 ? 241.636 275.170 252.944 1.00 44.33  ? 2485 GLN A N     1 
ATOM   7392  C  CA    . GLN A 1 2485 ? 241.088 273.969 253.562 1.00 39.11  ? 2485 GLN A CA    1 
ATOM   7393  C  C     . GLN A 1 2485 ? 240.387 273.101 252.529 1.00 38.52  ? 2485 GLN A C     1 
ATOM   7394  O  O     . GLN A 1 2485 ? 240.527 271.872 252.538 1.00 41.31  ? 2485 GLN A O     1 
ATOM   7395  C  CB    . GLN A 1 2485 ? 240.122 274.350 254.683 1.00 33.78  ? 2485 GLN A CB    1 
ATOM   7396  C  CG    . GLN A 1 2485 ? 239.796 273.216 255.636 1.00 40.11  ? 2485 GLN A CG    1 
ATOM   7397  C  CD    . GLN A 1 2485 ? 238.621 273.535 256.537 1.00 41.97  ? 2485 GLN A CD    1 
ATOM   7398  O  OE1   . GLN A 1 2485 ? 237.749 272.696 256.759 1.00 36.42  ? 2485 GLN A OE1   1 
ATOM   7399  N  NE2   . GLN A 1 2485 ? 238.589 274.757 257.055 1.00 40.31  ? 2485 GLN A NE2   1 
ATOM   7400  N  N     . LEU A 1 2486 ? 239.634 273.728 251.622 1.00 35.25  ? 2486 LEU A N     1 
ATOM   7401  C  CA    . LEU A 1 2486 ? 238.972 272.981 250.561 1.00 31.88  ? 2486 LEU A CA    1 
ATOM   7402  C  C     . LEU A 1 2486 ? 239.988 272.288 249.666 1.00 28.40  ? 2486 LEU A C     1 
ATOM   7403  O  O     . LEU A 1 2486 ? 239.787 271.138 249.267 1.00 30.11  ? 2486 LEU A O     1 
ATOM   7404  C  CB    . LEU A 1 2486 ? 238.077 273.910 249.742 1.00 26.74  ? 2486 LEU A CB    1 
ATOM   7405  C  CG    . LEU A 1 2486 ? 237.335 273.277 248.565 1.00 24.98  ? 2486 LEU A CG    1 
ATOM   7406  C  CD1   . LEU A 1 2486 ? 236.464 272.131 249.041 1.00 29.40  ? 2486 LEU A CD1   1 
ATOM   7407  C  CD2   . LEU A 1 2486 ? 236.505 274.313 247.831 1.00 27.41  ? 2486 LEU A CD2   1 
ATOM   7408  N  N     . GLU A 1 2487 ? 241.089 272.968 249.345 1.00 27.38  ? 2487 GLU A N     1 
ATOM   7409  C  CA    . GLU A 1 2487 ? 242.109 272.370 248.491 1.00 31.14  ? 2487 GLU A CA    1 
ATOM   7410  C  C     . GLU A 1 2487 ? 242.738 271.155 249.158 1.00 28.52  ? 2487 GLU A C     1 
ATOM   7411  O  O     . GLU A 1 2487 ? 242.872 270.091 248.539 1.00 30.38  ? 2487 GLU A O     1 
ATOM   7412  C  CB    . GLU A 1 2487 ? 243.173 273.411 248.145 1.00 32.09  ? 2487 GLU A CB    1 
ATOM   7413  C  CG    . GLU A 1 2487 ? 244.414 272.839 247.490 1.00 31.79  ? 2487 GLU A CG    1 
ATOM   7414  C  CD    . GLU A 1 2487 ? 245.141 273.861 246.643 1.00 52.80  ? 2487 GLU A CD    1 
ATOM   7415  O  OE1   . GLU A 1 2487 ? 244.518 274.879 246.274 1.00 47.20  ? 2487 GLU A OE1   1 
ATOM   7416  O  OE2   . GLU A 1 2487 ? 246.336 273.648 246.346 1.00 58.06  ? 2487 GLU A OE2   1 
ATOM   7417  N  N     . ARG A 1 2488 ? 243.126 271.294 250.429 1.00 32.27  ? 2488 ARG A N     1 
ATOM   7418  C  CA    . ARG A 1 2488 ? 243.728 270.169 251.139 1.00 25.22  ? 2488 ARG A CA    1 
ATOM   7419  C  C     . ARG A 1 2488 ? 242.756 268.999 251.233 1.00 26.63  ? 2488 ARG A C     1 
ATOM   7420  O  O     . ARG A 1 2488 ? 243.122 267.844 250.965 1.00 25.65  ? 2488 ARG A O     1 
ATOM   7421  C  CB    . ARG A 1 2488 ? 244.178 270.603 252.533 1.00 28.40  ? 2488 ARG A CB    1 
ATOM   7422  C  CG    . ARG A 1 2488 ? 245.344 271.572 252.548 1.00 40.43  ? 2488 ARG A CG    1 
ATOM   7423  C  CD    . ARG A 1 2488 ? 245.857 271.782 253.963 1.00 39.31  ? 2488 ARG A CD    1 
ATOM   7424  N  NE    . ARG A 1 2488 ? 244.856 272.403 254.823 1.00 45.83  ? 2488 ARG A NE    1 
ATOM   7425  C  CZ    . ARG A 1 2488 ? 244.692 273.711 254.958 1.00 51.55  ? 2488 ARG A CZ    1 
ATOM   7426  N  NH1   . ARG A 1 2488 ? 245.456 274.575 254.309 1.00 50.20  ? 2488 ARG A NH1   1 
ATOM   7427  N  NH2   . ARG A 1 2488 ? 243.740 274.165 255.768 1.00 42.42  ? 2488 ARG A NH2   1 
ATOM   7428  N  N     . TYR A 1 2489 ? 241.503 269.287 251.597 1.00 25.45  ? 2489 TYR A N     1 
ATOM   7429  C  CA    . TYR A 1 2489 ? 240.511 268.229 251.733 1.00 17.74  ? 2489 TYR A CA    1 
ATOM   7430  C  C     . TYR A 1 2489 ? 240.264 267.533 250.403 1.00 18.62  ? 2489 TYR A C     1 
ATOM   7431  O  O     . TYR A 1 2489 ? 240.194 266.302 250.347 1.00 19.87  ? 2489 TYR A O     1 
ATOM   7432  C  CB    . TYR A 1 2489 ? 239.206 268.798 252.285 1.00 16.09  ? 2489 TYR A CB    1 
ATOM   7433  C  CG    . TYR A 1 2489 ? 238.096 267.777 252.370 1.00 21.66  ? 2489 TYR A CG    1 
ATOM   7434  C  CD1   . TYR A 1 2489 ? 238.215 266.664 253.190 1.00 24.04  ? 2489 TYR A CD1   1 
ATOM   7435  C  CD2   . TYR A 1 2489 ? 236.936 267.917 251.622 1.00 18.36  ? 2489 TYR A CD2   1 
ATOM   7436  C  CE1   . TYR A 1 2489 ? 237.207 265.724 253.270 1.00 18.12  ? 2489 TYR A CE1   1 
ATOM   7437  C  CE2   . TYR A 1 2489 ? 235.925 266.983 251.695 1.00 16.96  ? 2489 TYR A CE2   1 
ATOM   7438  C  CZ    . TYR A 1 2489 ? 236.066 265.888 252.520 1.00 20.85  ? 2489 TYR A CZ    1 
ATOM   7439  O  OH    . TYR A 1 2489 ? 235.059 264.954 252.596 1.00 26.58  ? 2489 TYR A OH    1 
ATOM   7440  N  N     . ILE A 1 2490 ? 240.147 268.301 249.319 1.00 18.38  ? 2490 ILE A N     1 
ATOM   7441  C  CA    . ILE A 1 2490 ? 239.846 267.712 248.020 1.00 14.80  ? 2490 ILE A CA    1 
ATOM   7442  C  C     . ILE A 1 2490 ? 241.010 266.862 247.534 1.00 15.28  ? 2490 ILE A C     1 
ATOM   7443  O  O     . ILE A 1 2490 ? 240.805 265.768 247.003 1.00 15.25  ? 2490 ILE A O     1 
ATOM   7444  C  CB    . ILE A 1 2490 ? 239.468 268.808 247.008 1.00 19.09  ? 2490 ILE A CB    1 
ATOM   7445  C  CG1   . ILE A 1 2490 ? 238.061 269.331 247.297 1.00 17.18  ? 2490 ILE A CG1   1 
ATOM   7446  C  CG2   . ILE A 1 2490 ? 239.537 268.277 245.584 1.00 15.29  ? 2490 ILE A CG2   1 
ATOM   7447  C  CD1   . ILE A 1 2490 ? 237.006 268.252 247.358 1.00 15.68  ? 2490 ILE A CD1   1 
ATOM   7448  N  N     . GLN A 1 2491 ? 242.248 267.328 247.719 1.00 14.69  ? 2491 GLN A N     1 
ATOM   7449  C  CA    . GLN A 1 2491 ? 243.394 266.537 247.277 1.00 13.02  ? 2491 GLN A CA    1 
ATOM   7450  C  C     . GLN A 1 2491 ? 243.502 265.231 248.060 1.00 16.57  ? 2491 GLN A C     1 
ATOM   7451  O  O     . GLN A 1 2491 ? 243.660 264.145 247.474 1.00 18.50  ? 2491 GLN A O     1 
ATOM   7452  C  CB    . GLN A 1 2491 ? 244.681 267.353 247.410 1.00 16.43  ? 2491 GLN A CB    1 
ATOM   7453  C  CG    . GLN A 1 2491 ? 244.802 268.489 246.410 1.00 19.99  ? 2491 GLN A CG    1 
ATOM   7454  C  CD    . GLN A 1 2491 ? 246.068 269.296 246.599 1.00 26.98  ? 2491 GLN A CD    1 
ATOM   7455  O  OE1   . GLN A 1 2491 ? 246.852 269.037 247.511 1.00 30.82  ? 2491 GLN A OE1   1 
ATOM   7456  N  NE2   . GLN A 1 2491 ? 246.275 270.284 245.737 1.00 29.37  ? 2491 GLN A NE2   1 
ATOM   7457  N  N     . ARG A 1 2492 ? 243.413 265.314 249.391 1.00 16.77  ? 2492 ARG A N     1 
ATOM   7458  C  CA    . ARG A 1 2492 ? 243.527 264.103 250.197 1.00 15.12  ? 2492 ARG A CA    1 
ATOM   7459  C  C     . ARG A 1 2492 ? 242.378 263.143 249.914 1.00 12.92  ? 2492 ARG A C     1 
ATOM   7460  O  O     . ARG A 1 2492 ? 242.584 261.927 249.818 1.00 13.72  ? 2492 ARG A O     1 
ATOM   7461  C  CB    . ARG A 1 2492 ? 243.587 264.465 251.680 1.00 20.66  ? 2492 ARG A CB    1 
ATOM   7462  C  CG    . ARG A 1 2492 ? 244.905 265.088 252.105 1.00 20.96  ? 2492 ARG A CG    1 
ATOM   7463  C  CD    . ARG A 1 2492 ? 244.745 265.898 253.378 1.00 30.67  ? 2492 ARG A CD    1 
ATOM   7464  N  NE    . ARG A 1 2492 ? 246.018 266.398 253.882 1.00 32.98  ? 2492 ARG A NE    1 
ATOM   7465  C  CZ    . ARG A 1 2492 ? 246.699 267.402 253.346 1.00 31.53  ? 2492 ARG A CZ    1 
ATOM   7466  N  NH1   . ARG A 1 2492 ? 246.261 268.037 252.272 1.00 32.13  ? 2492 ARG A NH1   1 
ATOM   7467  N  NH2   . ARG A 1 2492 ? 247.846 267.778 253.902 1.00 34.91  ? 2492 ARG A NH2   1 
ATOM   7468  N  N     . TYR A 1 2493 ? 241.161 263.671 249.760 1.00 11.30  ? 2493 TYR A N     1 
ATOM   7469  C  CA    . TYR A 1 2493 ? 240.024 262.815 249.458 1.00 12.08  ? 2493 TYR A CA    1 
ATOM   7470  C  C     . TYR A 1 2493 ? 240.125 262.227 248.062 1.00 10.86  ? 2493 TYR A C     1 
ATOM   7471  O  O     . TYR A 1 2493 ? 239.630 261.126 247.826 1.00 13.25  ? 2493 TYR A O     1 
ATOM   7472  C  CB    . TYR A 1 2493 ? 238.718 263.594 249.609 1.00 12.87  ? 2493 TYR A CB    1 
ATOM   7473  C  CG    . TYR A 1 2493 ? 237.509 262.710 249.802 1.00 10.19  ? 2493 TYR A CG    1 
ATOM   7474  C  CD1   . TYR A 1 2493 ? 236.877 262.116 248.720 1.00 8.43   ? 2493 TYR A CD1   1 
ATOM   7475  C  CD2   . TYR A 1 2493 ? 236.999 262.469 251.069 1.00 13.14  ? 2493 TYR A CD2   1 
ATOM   7476  C  CE1   . TYR A 1 2493 ? 235.777 261.307 248.892 1.00 10.65  ? 2493 TYR A CE1   1 
ATOM   7477  C  CE2   . TYR A 1 2493 ? 235.895 261.663 251.251 1.00 16.15  ? 2493 TYR A CE2   1 
ATOM   7478  C  CZ    . TYR A 1 2493 ? 235.288 261.084 250.159 1.00 16.75  ? 2493 TYR A CZ    1 
ATOM   7479  O  OH    . TYR A 1 2493 ? 234.188 260.279 250.335 1.00 16.85  ? 2493 TYR A OH    1 
ATOM   7480  N  N     . LEU A 1 2494 ? 240.748 262.939 247.122 1.00 11.64  ? 2494 LEU A N     1 
ATOM   7481  C  CA    . LEU A 1 2494 ? 240.973 262.368 245.802 1.00 10.71  ? 2494 LEU A CA    1 
ATOM   7482  C  C     . LEU A 1 2494 ? 241.910 261.175 245.884 1.00 10.00  ? 2494 LEU A C     1 
ATOM   7483  O  O     . LEU A 1 2494 ? 241.661 260.138 245.258 1.00 11.27  ? 2494 LEU A O     1 
ATOM   7484  C  CB    . LEU A 1 2494 ? 241.528 263.432 244.858 1.00 12.11  ? 2494 LEU A CB    1 
ATOM   7485  C  CG    . LEU A 1 2494 ? 241.932 262.976 243.457 1.00 13.32  ? 2494 LEU A CG    1 
ATOM   7486  C  CD1   . LEU A 1 2494 ? 240.775 262.287 242.755 1.00 12.26  ? 2494 LEU A CD1   1 
ATOM   7487  C  CD2   . LEU A 1 2494 ? 242.409 264.163 242.651 1.00 14.16  ? 2494 LEU A CD2   1 
ATOM   7488  N  N     . VAL A 1 2495 ? 242.984 261.293 246.667 1.00 10.72  ? 2495 VAL A N     1 
ATOM   7489  C  CA    . VAL A 1 2495 ? 243.870 260.144 246.859 1.00 10.21  ? 2495 VAL A CA    1 
ATOM   7490  C  C     . VAL A 1 2495 ? 243.115 258.988 247.511 1.00 10.83  ? 2495 VAL A C     1 
ATOM   7491  O  O     . VAL A 1 2495 ? 243.219 257.828 247.082 1.00 10.12  ? 2495 VAL A O     1 
ATOM   7492  C  CB    . VAL A 1 2495 ? 245.106 260.549 247.680 1.00 12.64  ? 2495 VAL A CB    1 
ATOM   7493  C  CG1   . VAL A 1 2495 ? 245.928 259.322 248.042 1.00 13.63  ? 2495 VAL A CG1   1 
ATOM   7494  C  CG2   . VAL A 1 2495 ? 245.949 261.545 246.906 1.00 14.44  ? 2495 VAL A CG2   1 
ATOM   7495  N  N     . TYR A 1 2496 ? 242.332 259.292 248.549 1.00 13.23  ? 2496 TYR A N     1 
ATOM   7496  C  CA    . TYR A 1 2496 ? 241.569 258.269 249.261 1.00 11.11  ? 2496 TYR A CA    1 
ATOM   7497  C  C     . TYR A 1 2496 ? 240.568 257.574 248.342 1.00 10.81  ? 2496 TYR A C     1 
ATOM   7498  O  O     . TYR A 1 2496 ? 240.433 256.343 248.365 1.00 11.25  ? 2496 TYR A O     1 
ATOM   7499  C  CB    . TYR A 1 2496 ? 240.877 258.927 250.460 1.00 9.29   ? 2496 TYR A CB    1 
ATOM   7500  C  CG    . TYR A 1 2496 ? 239.701 258.194 251.064 1.00 13.78  ? 2496 TYR A CG    1 
ATOM   7501  C  CD1   . TYR A 1 2496 ? 238.405 258.461 250.644 1.00 12.33  ? 2496 TYR A CD1   1 
ATOM   7502  C  CD2   . TYR A 1 2496 ? 239.880 257.275 252.086 1.00 15.72  ? 2496 TYR A CD2   1 
ATOM   7503  C  CE1   . TYR A 1 2496 ? 237.325 257.813 251.204 1.00 12.16  ? 2496 TYR A CE1   1 
ATOM   7504  C  CE2   . TYR A 1 2496 ? 238.805 256.622 252.656 1.00 14.39  ? 2496 TYR A CE2   1 
ATOM   7505  C  CZ    . TYR A 1 2496 ? 237.530 256.894 252.208 1.00 15.16  ? 2496 TYR A CZ    1 
ATOM   7506  O  OH    . TYR A 1 2496 ? 236.452 256.248 252.766 1.00 19.12  ? 2496 TYR A OH    1 
ATOM   7507  N  N     . ALA A 1 2497 ? 239.872 258.349 247.509 1.00 10.31  ? 2497 ALA A N     1 
ATOM   7508  C  CA    . ALA A 1 2497 ? 238.874 257.789 246.609 1.00 10.37  ? 2497 ALA A CA    1 
ATOM   7509  C  C     . ALA A 1 2497 ? 239.523 256.985 245.493 1.00 10.06  ? 2497 ALA A C     1 
ATOM   7510  O  O     . ALA A 1 2497 ? 238.977 255.964 245.067 1.00 12.24  ? 2497 ALA A O     1 
ATOM   7511  C  CB    . ALA A 1 2497 ? 238.004 258.905 246.034 1.00 12.70  ? 2497 ALA A CB    1 
ATOM   7512  N  N     . ILE A 1 2498 ? 240.688 257.422 245.008 1.00 9.39   ? 2498 ILE A N     1 
ATOM   7513  C  CA    . ILE A 1 2498 ? 241.422 256.618 244.038 1.00 8.66   ? 2498 ILE A CA    1 
ATOM   7514  C  C     . ILE A 1 2498 ? 241.779 255.270 244.644 1.00 8.79   ? 2498 ILE A C     1 
ATOM   7515  O  O     . ILE A 1 2498 ? 241.589 254.218 244.019 1.00 9.53   ? 2498 ILE A O     1 
ATOM   7516  C  CB    . ILE A 1 2498 ? 242.677 257.369 243.556 1.00 8.99   ? 2498 ILE A CB    1 
ATOM   7517  C  CG1   . ILE A 1 2498 ? 242.297 258.507 242.610 1.00 11.33  ? 2498 ILE A CG1   1 
ATOM   7518  C  CG2   . ILE A 1 2498 ? 243.636 256.418 242.863 1.00 11.24  ? 2498 ILE A CG2   1 
ATOM   7519  C  CD1   . ILE A 1 2498 ? 243.468 259.372 242.216 1.00 12.64  ? 2498 ILE A CD1   1 
ATOM   7520  N  N     . LEU A 1 2499 ? 242.274 255.279 245.883 1.00 10.27  ? 2499 LEU A N     1 
ATOM   7521  C  CA    . LEU A 1 2499 ? 242.645 254.030 246.539 1.00 8.42   ? 2499 LEU A CA    1 
ATOM   7522  C  C     . LEU A 1 2499 ? 241.442 253.109 246.701 1.00 9.62   ? 2499 LEU A C     1 
ATOM   7523  O  O     . LEU A 1 2499 ? 241.529 251.904 246.441 1.00 11.21  ? 2499 LEU A O     1 
ATOM   7524  C  CB    . LEU A 1 2499 ? 243.283 254.318 247.895 1.00 10.83  ? 2499 LEU A CB    1 
ATOM   7525  C  CG    . LEU A 1 2499 ? 244.799 254.482 247.870 1.00 18.04  ? 2499 LEU A CG    1 
ATOM   7526  C  CD1   . LEU A 1 2499 ? 245.299 254.853 249.245 1.00 20.32  ? 2499 LEU A CD1   1 
ATOM   7527  C  CD2   . LEU A 1 2499 ? 245.455 253.205 247.377 1.00 19.35  ? 2499 LEU A CD2   1 
ATOM   7528  N  N     . TRP A 1 2500 ? 240.306 253.658 247.131 1.00 9.72   ? 2500 TRP A N     1 
ATOM   7529  C  CA    . TRP A 1 2500 ? 239.150 252.809 247.402 1.00 9.23   ? 2500 TRP A CA    1 
ATOM   7530  C  C     . TRP A 1 2500 ? 238.369 252.434 246.150 1.00 8.40   ? 2500 TRP A C     1 
ATOM   7531  O  O     . TRP A 1 2500 ? 237.577 251.488 246.195 1.00 11.68  ? 2500 TRP A O     1 
ATOM   7532  C  CB    . TRP A 1 2500 ? 238.220 253.489 248.406 1.00 9.50   ? 2500 TRP A CB    1 
ATOM   7533  C  CG    . TRP A 1 2500 ? 238.558 253.146 249.817 1.00 9.58   ? 2500 TRP A CG    1 
ATOM   7534  C  CD1   . TRP A 1 2500 ? 238.983 254.002 250.783 1.00 10.74  ? 2500 TRP A CD1   1 
ATOM   7535  C  CD2   . TRP A 1 2500 ? 238.516 251.847 250.419 1.00 13.29  ? 2500 TRP A CD2   1 
ATOM   7536  N  NE1   . TRP A 1 2500 ? 239.203 253.323 251.956 1.00 14.62  ? 2500 TRP A NE1   1 
ATOM   7537  C  CE2   . TRP A 1 2500 ? 238.923 251.997 251.758 1.00 13.95  ? 2500 TRP A CE2   1 
ATOM   7538  C  CE3   . TRP A 1 2500 ? 238.169 250.574 249.958 1.00 10.05  ? 2500 TRP A CE3   1 
ATOM   7539  C  CZ2   . TRP A 1 2500 ? 238.995 250.924 252.641 1.00 14.46  ? 2500 TRP A CZ2   1 
ATOM   7540  C  CZ3   . TRP A 1 2500 ? 238.241 249.510 250.836 1.00 12.74  ? 2500 TRP A CZ3   1 
ATOM   7541  C  CH2   . TRP A 1 2500 ? 238.650 249.691 252.162 1.00 15.11  ? 2500 TRP A CH2   1 
ATOM   7542  N  N     . SER A 1 2501 ? 238.571 253.138 245.038 1.00 8.88   ? 2501 SER A N     1 
ATOM   7543  C  CA    . SER A 1 2501 ? 237.856 252.830 243.808 1.00 7.59   ? 2501 SER A CA    1 
ATOM   7544  C  C     . SER A 1 2501 ? 238.659 251.924 242.888 1.00 8.14   ? 2501 SER A C     1 
ATOM   7545  O  O     . SER A 1 2501 ? 238.079 251.154 242.117 1.00 10.79  ? 2501 SER A O     1 
ATOM   7546  C  CB    . SER A 1 2501 ? 237.496 254.122 243.074 1.00 7.64   ? 2501 SER A CB    1 
ATOM   7547  O  OG    . SER A 1 2501 ? 236.714 254.969 243.895 1.00 11.51  ? 2501 SER A OG    1 
ATOM   7548  N  N     . LEU A 1 2502 ? 239.984 252.007 242.950 1.00 6.74   ? 2502 LEU A N     1 
ATOM   7549  C  CA    . LEU A 1 2502 ? 240.841 251.209 242.090 1.00 7.17   ? 2502 LEU A CA    1 
ATOM   7550  C  C     . LEU A 1 2502 ? 241.334 249.932 242.754 1.00 8.29   ? 2502 LEU A C     1 
ATOM   7551  O  O     . LEU A 1 2502 ? 241.899 249.074 242.067 1.00 15.59  ? 2502 LEU A O     1 
ATOM   7552  C  CB    . LEU A 1 2502 ? 242.034 252.053 241.630 1.00 12.21  ? 2502 LEU A CB    1 
ATOM   7553  C  CG    . LEU A 1 2502 ? 241.789 253.047 240.491 1.00 6.84   ? 2502 LEU A CG    1 
ATOM   7554  C  CD1   . LEU A 1 2502 ? 240.923 254.223 240.904 1.00 10.51  ? 2502 LEU A CD1   1 
ATOM   7555  C  CD2   . LEU A 1 2502 ? 243.122 253.558 240.037 1.00 10.17  ? 2502 LEU A CD2   1 
ATOM   7556  N  N     . SER A 1 2503 ? 241.134 249.781 244.067 1.00 9.03   ? 2503 SER A N     1 
ATOM   7557  C  CA    . SER A 1 2503 ? 241.550 248.567 244.759 1.00 6.97   ? 2503 SER A CA    1 
ATOM   7558  C  C     . SER A 1 2503 ? 240.522 248.104 245.786 1.00 6.79   ? 2503 SER A C     1 
ATOM   7559  O  O     . SER A 1 2503 ? 240.851 247.286 246.652 1.00 8.14   ? 2503 SER A O     1 
ATOM   7560  C  CB    . SER A 1 2503 ? 242.903 248.765 245.449 1.00 7.70   ? 2503 SER A CB    1 
ATOM   7561  O  OG    . SER A 1 2503 ? 242.782 249.613 246.575 1.00 10.57  ? 2503 SER A OG    1 
ATOM   7562  N  N     . GLY A 1 2504 ? 239.285 248.600 245.713 1.00 5.78   ? 2504 GLY A N     1 
ATOM   7563  C  CA    . GLY A 1 2504 ? 238.279 248.193 246.677 1.00 6.93   ? 2504 GLY A CA    1 
ATOM   7564  C  C     . GLY A 1 2504 ? 237.841 246.753 246.516 1.00 7.40   ? 2504 GLY A C     1 
ATOM   7565  O  O     . GLY A 1 2504 ? 237.338 246.145 247.464 1.00 8.36   ? 2504 GLY A O     1 
ATOM   7566  N  N     . ASP A 1 2505 ? 238.026 246.187 245.323 1.00 8.09   ? 2505 ASP A N     1 
ATOM   7567  C  CA    . ASP A 1 2505 ? 237.657 244.807 245.035 1.00 8.28   ? 2505 ASP A CA    1 
ATOM   7568  C  C     . ASP A 1 2505 ? 238.849 243.862 245.112 1.00 8.01   ? 2505 ASP A C     1 
ATOM   7569  O  O     . ASP A 1 2505 ? 238.826 242.781 244.516 1.00 11.45  ? 2505 ASP A O     1 
ATOM   7570  C  CB    . ASP A 1 2505 ? 237.002 244.714 243.659 1.00 9.80   ? 2505 ASP A CB    1 
ATOM   7571  C  CG    . ASP A 1 2505 ? 237.842 245.351 242.570 1.00 15.75  ? 2505 ASP A CG    1 
ATOM   7572  O  OD1   . ASP A 1 2505 ? 238.724 246.171 242.900 1.00 13.98  ? 2505 ASP A OD1   1 
ATOM   7573  O  OD2   . ASP A 1 2505 ? 237.623 245.027 241.384 1.00 19.26  ? 2505 ASP A OD2   1 
ATOM   7574  N  N     . SER A 1 2506 ? 239.896 244.246 245.836 1.00 8.33   ? 2506 SER A N     1 
ATOM   7575  C  CA    . SER A 1 2506 ? 241.117 243.464 245.909 1.00 12.20  ? 2506 SER A CA    1 
ATOM   7576  C  C     . SER A 1 2506 ? 241.457 243.165 247.363 1.00 11.35  ? 2506 SER A C     1 
ATOM   7577  O  O     . SER A 1 2506 ? 240.881 243.740 248.290 1.00 13.47  ? 2506 SER A O     1 
ATOM   7578  C  CB    . SER A 1 2506 ? 242.286 244.190 245.233 1.00 12.68  ? 2506 SER A CB    1 
ATOM   7579  O  OG    . SER A 1 2506 ? 242.350 245.542 245.642 1.00 11.71  ? 2506 SER A OG    1 
ATOM   7580  N  N     . ARG A 1 2507 ? 242.405 242.252 247.548 1.00 13.79  ? 2507 ARG A N     1 
ATOM   7581  C  CA    . ARG A 1 2507 ? 242.824 241.850 248.881 1.00 11.24  ? 2507 ARG A CA    1 
ATOM   7582  C  C     . ARG A 1 2507 ? 243.711 242.925 249.508 1.00 15.22  ? 2507 ARG A C     1 
ATOM   7583  O  O     . ARG A 1 2507 ? 243.996 243.966 248.913 1.00 21.78  ? 2507 ARG A O     1 
ATOM   7584  C  CB    . ARG A 1 2507 ? 243.539 240.502 248.826 1.00 11.27  ? 2507 ARG A CB    1 
ATOM   7585  C  CG    . ARG A 1 2507 ? 242.881 239.502 247.895 1.00 15.92  ? 2507 ARG A CG    1 
ATOM   7586  C  CD    . ARG A 1 2507 ? 243.757 238.287 247.667 1.00 28.08  ? 2507 ARG A CD    1 
ATOM   7587  N  NE    . ARG A 1 2507 ? 245.175 238.622 247.654 1.00 32.23  ? 2507 ARG A NE    1 
ATOM   7588  C  CZ    . ARG A 1 2507 ? 246.147 237.741 247.466 1.00 45.39  ? 2507 ARG A CZ    1 
ATOM   7589  N  NH1   . ARG A 1 2507 ? 245.890 236.457 247.279 1.00 41.30  ? 2507 ARG A NH1   1 
ATOM   7590  N  NH2   . ARG A 1 2507 ? 247.409 238.158 247.466 1.00 42.12  ? 2507 ARG A NH2   1 
ATOM   7591  N  N     . LEU A 1 2508 ? 244.146 242.658 250.740 1.00 15.80  ? 2508 LEU A N     1 
ATOM   7592  C  CA    . LEU A 1 2508 ? 244.914 243.646 251.493 1.00 20.67  ? 2508 LEU A CA    1 
ATOM   7593  C  C     . LEU A 1 2508 ? 246.256 243.936 250.834 1.00 21.72  ? 2508 LEU A C     1 
ATOM   7594  O  O     . LEU A 1 2508 ? 246.700 245.091 250.799 1.00 18.71  ? 2508 LEU A O     1 
ATOM   7595  C  CB    . LEU A 1 2508 ? 245.115 243.162 252.929 1.00 23.93  ? 2508 LEU A CB    1 
ATOM   7596  C  CG    . LEU A 1 2508 ? 245.455 244.229 253.968 1.00 29.71  ? 2508 LEU A CG    1 
ATOM   7597  C  CD1   . LEU A 1 2508 ? 244.191 244.909 254.466 1.00 30.74  ? 2508 LEU A CD1   1 
ATOM   7598  C  CD2   . LEU A 1 2508 ? 246.224 243.613 255.124 1.00 26.06  ? 2508 LEU A CD2   1 
ATOM   7599  N  N     . LYS A 1 2509 ? 246.925 242.903 250.319 1.00 20.28  ? 2509 LYS A N     1 
ATOM   7600  C  CA    . LYS A 1 2509 ? 248.253 243.101 249.747 1.00 21.27  ? 2509 LYS A CA    1 
ATOM   7601  C  C     . LYS A 1 2509 ? 248.184 243.924 248.465 1.00 27.92  ? 2509 LYS A C     1 
ATOM   7602  O  O     . LYS A 1 2509 ? 249.052 244.769 248.215 1.00 34.13  ? 2509 LYS A O     1 
ATOM   7603  C  CB    . LYS A 1 2509 ? 248.924 241.746 249.514 1.00 31.15  ? 2509 LYS A CB    1 
ATOM   7604  C  CG    . LYS A 1 2509 ? 250.336 241.817 248.956 1.00 47.04  ? 2509 LYS A CG    1 
ATOM   7605  C  CD    . LYS A 1 2509 ? 250.971 240.433 248.904 1.00 46.89  ? 2509 LYS A CD    1 
ATOM   7606  C  CE    . LYS A 1 2509 ? 250.369 239.555 247.824 1.00 45.63  ? 2509 LYS A CE    1 
ATOM   7607  N  NZ    . LYS A 1 2509 ? 250.708 240.044 246.465 1.00 56.39  ? 2509 LYS A NZ    1 
ATOM   7608  N  N     . MET A 1 2510 ? 247.148 243.708 247.650 1.00 25.63  ? 2510 MET A N     1 
ATOM   7609  C  CA    . MET A 1 2510 ? 246.937 244.552 246.476 1.00 20.10  ? 2510 MET A CA    1 
ATOM   7610  C  C     . MET A 1 2510 ? 246.663 246.001 246.857 1.00 17.91  ? 2510 MET A C     1 
ATOM   7611  O  O     . MET A 1 2510 ? 247.177 246.921 246.208 1.00 20.32  ? 2510 MET A O     1 
ATOM   7612  C  CB    . MET A 1 2510 ? 245.781 244.006 245.639 1.00 19.12  ? 2510 MET A CB    1 
ATOM   7613  C  CG    . MET A 1 2510 ? 246.022 242.645 245.010 1.00 21.05  ? 2510 MET A CG    1 
ATOM   7614  S  SD    . MET A 1 2510 ? 247.403 242.639 243.851 1.00 41.43  ? 2510 MET A SD    1 
ATOM   7615  C  CE    . MET A 1 2510 ? 248.680 241.877 244.840 1.00 39.41  ? 2510 MET A CE    1 
ATOM   7616  N  N     . ARG A 1 2511 ? 245.850 246.222 247.891 1.00 14.96  ? 2511 ARG A N     1 
ATOM   7617  C  CA    . ARG A 1 2511 ? 245.578 247.583 248.341 1.00 16.58  ? 2511 ARG A CA    1 
ATOM   7618  C  C     . ARG A 1 2511 ? 246.852 248.262 248.825 1.00 19.86  ? 2511 ARG A C     1 
ATOM   7619  O  O     . ARG A 1 2511 ? 247.094 249.437 248.522 1.00 22.37  ? 2511 ARG A O     1 
ATOM   7620  C  CB    . ARG A 1 2511 ? 244.524 247.564 249.447 1.00 13.03  ? 2511 ARG A CB    1 
ATOM   7621  C  CG    . ARG A 1 2511 ? 243.159 247.083 248.991 1.00 8.45   ? 2511 ARG A CG    1 
ATOM   7622  C  CD    . ARG A 1 2511 ? 242.194 246.997 250.155 1.00 9.02   ? 2511 ARG A CD    1 
ATOM   7623  N  NE    . ARG A 1 2511 ? 240.873 246.542 249.739 1.00 7.84   ? 2511 ARG A NE    1 
ATOM   7624  C  CZ    . ARG A 1 2511 ? 239.843 246.385 250.559 1.00 8.27   ? 2511 ARG A CZ    1 
ATOM   7625  N  NH1   . ARG A 1 2511 ? 239.946 246.641 251.853 1.00 9.90   ? 2511 ARG A NH1   1 
ATOM   7626  N  NH2   . ARG A 1 2511 ? 238.682 245.963 250.070 1.00 7.22   ? 2511 ARG A NH2   1 
ATOM   7627  N  N     . ALA A 1 2512 ? 247.682 247.529 249.569 1.00 19.64  ? 2512 ALA A N     1 
ATOM   7628  C  CA    . ALA A 1 2512 ? 248.954 248.078 250.024 1.00 19.14  ? 2512 ALA A CA    1 
ATOM   7629  C  C     . ALA A 1 2512 ? 249.873 248.389 248.850 1.00 21.97  ? 2512 ALA A C     1 
ATOM   7630  O  O     . ALA A 1 2512 ? 250.566 249.412 248.851 1.00 24.76  ? 2512 ALA A O     1 
ATOM   7631  C  CB    . ALA A 1 2512 ? 249.626 247.106 250.992 1.00 22.44  ? 2512 ALA A CB    1 
ATOM   7632  N  N     . GLU A 1 2513 ? 249.899 247.515 247.843 1.00 21.19  ? 2513 GLU A N     1 
ATOM   7633  C  CA    . GLU A 1 2513 ? 250.732 247.758 246.668 1.00 22.27  ? 2513 GLU A CA    1 
ATOM   7634  C  C     . GLU A 1 2513 ? 250.290 249.017 245.932 1.00 24.85  ? 2513 GLU A C     1 
ATOM   7635  O  O     . GLU A 1 2513 ? 251.122 249.838 245.524 1.00 30.07  ? 2513 GLU A O     1 
ATOM   7636  C  CB    . GLU A 1 2513 ? 250.687 246.546 245.739 1.00 23.97  ? 2513 GLU A CB    1 
ATOM   7637  C  CG    . GLU A 1 2513 ? 251.923 246.382 244.875 1.00 37.33  ? 2513 GLU A CG    1 
ATOM   7638  C  CD    . GLU A 1 2513 ? 251.838 245.176 243.962 1.00 52.81  ? 2513 GLU A CD    1 
ATOM   7639  O  OE1   . GLU A 1 2513 ? 251.161 244.195 244.333 1.00 53.43  ? 2513 GLU A OE1   1 
ATOM   7640  O  OE2   . GLU A 1 2513 ? 252.450 245.209 242.874 1.00 54.29  ? 2513 GLU A OE2   1 
ATOM   7641  N  N     . LEU A 1 2514 ? 248.978 249.183 245.751 1.00 20.79  ? 2514 LEU A N     1 
ATOM   7642  C  CA    . LEU A 1 2514 ? 248.479 250.380 245.080 1.00 21.44  ? 2514 LEU A CA    1 
ATOM   7643  C  C     . LEU A 1 2514 ? 248.777 251.630 245.896 1.00 23.95  ? 2514 LEU A C     1 
ATOM   7644  O  O     . LEU A 1 2514 ? 249.130 252.677 245.338 1.00 25.68  ? 2514 LEU A O     1 
ATOM   7645  C  CB    . LEU A 1 2514 ? 246.979 250.259 244.813 1.00 18.92  ? 2514 LEU A CB    1 
ATOM   7646  C  CG    . LEU A 1 2514 ? 246.392 251.442 244.040 1.00 16.71  ? 2514 LEU A CG    1 
ATOM   7647  C  CD1   . LEU A 1 2514 ? 246.915 251.457 242.615 1.00 19.16  ? 2514 LEU A CD1   1 
ATOM   7648  C  CD2   . LEU A 1 2514 ? 244.877 251.418 244.056 1.00 13.03  ? 2514 LEU A CD2   1 
ATOM   7649  N  N     . GLY A 1 2515 ? 248.636 251.544 247.221 1.00 21.64  ? 2515 GLY A N     1 
ATOM   7650  C  CA    . GLY A 1 2515 ? 248.984 252.675 248.064 1.00 23.30  ? 2515 GLY A CA    1 
ATOM   7651  C  C     . GLY A 1 2515 ? 250.449 253.049 247.962 1.00 23.53  ? 2515 GLY A C     1 
ATOM   7652  O  O     . GLY A 1 2515 ? 250.796 254.231 247.906 1.00 27.96  ? 2515 GLY A O     1 
ATOM   7653  N  N     . GLU A 1 2516 ? 251.331 252.047 247.936 1.00 23.79  ? 2516 GLU A N     1 
ATOM   7654  C  CA    . GLU A 1 2516 ? 252.757 252.320 247.791 1.00 25.93  ? 2516 GLU A CA    1 
ATOM   7655  C  C     . GLU A 1 2516 ? 253.066 252.957 246.443 1.00 27.11  ? 2516 GLU A C     1 
ATOM   7656  O  O     . GLU A 1 2516 ? 253.861 253.902 246.363 1.00 31.65  ? 2516 GLU A O     1 
ATOM   7657  C  CB    . GLU A 1 2516 ? 253.562 251.032 247.975 1.00 24.07  ? 2516 GLU A CB    1 
ATOM   7658  C  CG    . GLU A 1 2516 ? 253.530 250.470 249.387 1.00 28.76  ? 2516 GLU A CG    1 
ATOM   7659  C  CD    . GLU A 1 2516 ? 254.535 251.134 250.311 1.00 46.01  ? 2516 GLU A CD    1 
ATOM   7660  O  OE1   . GLU A 1 2516 ? 254.465 252.368 250.492 1.00 37.09  ? 2516 GLU A OE1   1 
ATOM   7661  O  OE2   . GLU A 1 2516 ? 255.400 250.418 250.860 1.00 48.08  ? 2516 GLU A OE2   1 
ATOM   7662  N  N     . TYR A 1 2517 ? 252.449 252.457 245.371 1.00 20.74  ? 2517 TYR A N     1 
ATOM   7663  C  CA    . TYR A 1 2517 ? 252.666 253.059 244.058 1.00 21.54  ? 2517 TYR A CA    1 
ATOM   7664  C  C     . TYR A 1 2517 ? 252.193 254.507 244.032 1.00 26.67  ? 2517 TYR A C     1 
ATOM   7665  O  O     . TYR A 1 2517 ? 252.891 255.392 243.515 1.00 34.47  ? 2517 TYR A O     1 
ATOM   7666  C  CB    . TYR A 1 2517 ? 251.957 252.248 242.975 1.00 25.11  ? 2517 TYR A CB    1 
ATOM   7667  C  CG    . TYR A 1 2517 ? 252.080 252.852 241.594 1.00 28.63  ? 2517 TYR A CG    1 
ATOM   7668  C  CD1   . TYR A 1 2517 ? 253.222 252.659 240.832 1.00 26.90  ? 2517 TYR A CD1   1 
ATOM   7669  C  CD2   . TYR A 1 2517 ? 251.055 253.616 241.054 1.00 27.25  ? 2517 TYR A CD2   1 
ATOM   7670  C  CE1   . TYR A 1 2517 ? 253.339 253.210 239.571 1.00 31.95  ? 2517 TYR A CE1   1 
ATOM   7671  C  CE2   . TYR A 1 2517 ? 251.165 254.170 239.796 1.00 24.51  ? 2517 TYR A CE2   1 
ATOM   7672  C  CZ    . TYR A 1 2517 ? 252.308 253.964 239.059 1.00 26.64  ? 2517 TYR A CZ    1 
ATOM   7673  O  OH    . TYR A 1 2517 ? 252.419 254.514 237.804 1.00 28.68  ? 2517 TYR A OH    1 
ATOM   7674  N  N     . ILE A 1 2518 ? 251.011 254.771 244.593 1.00 24.46  ? 2518 ILE A N     1 
ATOM   7675  C  CA    . ILE A 1 2518 ? 250.502 256.136 244.635 1.00 23.37  ? 2518 ILE A CA    1 
ATOM   7676  C  C     . ILE A 1 2518 ? 251.448 257.025 245.428 1.00 24.91  ? 2518 ILE A C     1 
ATOM   7677  O  O     . ILE A 1 2518 ? 251.801 258.125 244.988 1.00 33.20  ? 2518 ILE A O     1 
ATOM   7678  C  CB    . ILE A 1 2518 ? 249.075 256.158 245.214 1.00 22.54  ? 2518 ILE A CB    1 
ATOM   7679  C  CG1   . ILE A 1 2518 ? 248.075 255.661 244.172 1.00 20.22  ? 2518 ILE A CG1   1 
ATOM   7680  C  CG2   . ILE A 1 2518 ? 248.704 257.558 245.675 1.00 22.00  ? 2518 ILE A CG2   1 
ATOM   7681  C  CD1   . ILE A 1 2518 ? 246.664 255.559 244.686 1.00 16.45  ? 2518 ILE A CD1   1 
ATOM   7682  N  N     . ARG A 1 2519 ? 251.904 256.547 246.587 1.00 26.41  ? 2519 ARG A N     1 
ATOM   7683  C  CA    . ARG A 1 2519 ? 252.855 257.308 247.391 1.00 28.03  ? 2519 ARG A CA    1 
ATOM   7684  C  C     . ARG A 1 2519 ? 254.117 257.621 246.602 1.00 31.74  ? 2519 ARG A C     1 
ATOM   7685  O  O     . ARG A 1 2519 ? 254.680 258.714 246.722 1.00 32.59  ? 2519 ARG A O     1 
ATOM   7686  C  CB    . ARG A 1 2519 ? 253.197 256.534 248.663 1.00 25.71  ? 2519 ARG A CB    1 
ATOM   7687  C  CG    . ARG A 1 2519 ? 254.115 257.276 249.614 1.00 32.26  ? 2519 ARG A CG    1 
ATOM   7688  C  CD    . ARG A 1 2519 ? 254.499 256.408 250.799 1.00 35.36  ? 2519 ARG A CD    1 
ATOM   7689  N  NE    . ARG A 1 2519 ? 253.437 256.347 251.797 1.00 36.78  ? 2519 ARG A NE    1 
ATOM   7690  C  CZ    . ARG A 1 2519 ? 253.202 257.289 252.697 1.00 37.91  ? 2519 ARG A CZ    1 
ATOM   7691  N  NH1   . ARG A 1 2519 ? 253.934 258.389 252.754 1.00 33.40  ? 2519 ARG A NH1   1 
ATOM   7692  N  NH2   . ARG A 1 2519 ? 252.207 257.125 253.564 1.00 38.50  ? 2519 ARG A NH2   1 
ATOM   7693  N  N     . ARG A 1 2520 ? 254.578 256.668 245.792 1.00 34.69  ? 2520 ARG A N     1 
ATOM   7694  C  CA    . ARG A 1 2520 ? 255.764 256.909 244.978 1.00 31.32  ? 2520 ARG A CA    1 
ATOM   7695  C  C     . ARG A 1 2520 ? 255.508 257.979 243.923 1.00 34.32  ? 2520 ARG A C     1 
ATOM   7696  O  O     . ARG A 1 2520 ? 256.379 258.818 243.664 1.00 37.84  ? 2520 ARG A O     1 
ATOM   7697  C  CB    . ARG A 1 2520 ? 256.231 255.609 244.327 1.00 25.88  ? 2520 ARG A CB    1 
ATOM   7698  C  CG    . ARG A 1 2520 ? 257.228 254.829 245.171 1.00 29.03  ? 2520 ARG A CG    1 
ATOM   7699  C  CD    . ARG A 1 2520 ? 258.184 253.999 244.319 1.00 35.79  ? 2520 ARG A CD    1 
ATOM   7700  N  NE    . ARG A 1 2520 ? 257.568 253.463 243.109 1.00 38.23  ? 2520 ARG A NE    1 
ATOM   7701  C  CZ    . ARG A 1 2520 ? 256.646 252.510 243.087 1.00 36.06  ? 2520 ARG A CZ    1 
ATOM   7702  N  NH1   . ARG A 1 2520 ? 256.201 251.948 244.199 1.00 30.53  ? 2520 ARG A NH1   1 
ATOM   7703  N  NH2   . ARG A 1 2520 ? 256.162 252.105 241.917 1.00 34.40  ? 2520 ARG A NH2   1 
ATOM   7704  N  N     . ILE A 1 2521 ? 254.326 257.976 243.305 1.00 34.12  ? 2521 ILE A N     1 
ATOM   7705  C  CA    . ILE A 1 2521 ? 254.076 258.886 242.190 1.00 30.11  ? 2521 ILE A CA    1 
ATOM   7706  C  C     . ILE A 1 2521 ? 253.384 260.192 242.585 1.00 31.90  ? 2521 ILE A C     1 
ATOM   7707  O  O     . ILE A 1 2521 ? 253.502 261.181 241.846 1.00 39.17  ? 2521 ILE A O     1 
ATOM   7708  C  CB    . ILE A 1 2521 ? 253.267 258.195 241.073 1.00 28.46  ? 2521 ILE A CB    1 
ATOM   7709  C  CG1   . ILE A 1 2521 ? 251.776 258.178 241.413 1.00 30.86  ? 2521 ILE A CG1   1 
ATOM   7710  C  CG2   . ILE A 1 2521 ? 253.794 256.792 240.819 1.00 33.23  ? 2521 ILE A CG2   1 
ATOM   7711  C  CD1   . ILE A 1 2521 ? 250.910 257.577 240.334 1.00 28.19  ? 2521 ILE A CD1   1 
ATOM   7712  N  N     . THR A 1 2522 ? 252.672 260.233 243.707 1.00 31.54  ? 2522 THR A N     1 
ATOM   7713  C  CA    . THR A 1 2522 ? 251.861 261.410 243.976 1.00 35.77  ? 2522 THR A CA    1 
ATOM   7714  C  C     . THR A 1 2522 ? 252.708 262.535 244.563 1.00 40.38  ? 2522 THR A C     1 
ATOM   7715  O  O     . THR A 1 2522 ? 253.845 262.342 245.001 1.00 44.48  ? 2522 THR A O     1 
ATOM   7716  C  CB    . THR A 1 2522 ? 250.712 261.093 244.931 1.00 39.22  ? 2522 THR A CB    1 
ATOM   7717  O  OG1   . THR A 1 2522 ? 249.848 262.231 245.021 1.00 43.45  ? 2522 THR A OG1   1 
ATOM   7718  C  CG2   . THR A 1 2522 ? 251.250 260.811 246.322 1.00 35.14  ? 2522 THR A CG2   1 
ATOM   7719  N  N     . THR A 1 2523 ? 252.127 263.735 244.558 1.00 36.10  ? 2523 THR A N     1 
ATOM   7720  C  CA    . THR A 1 2523 ? 252.689 264.887 245.244 1.00 37.02  ? 2523 THR A CA    1 
ATOM   7721  C  C     . THR A 1 2523 ? 251.780 265.398 246.352 1.00 41.50  ? 2523 THR A C     1 
ATOM   7722  O  O     . THR A 1 2523 ? 252.152 266.344 247.054 1.00 45.37  ? 2523 THR A O     1 
ATOM   7723  C  CB    . THR A 1 2523 ? 252.975 266.021 244.249 1.00 40.54  ? 2523 THR A CB    1 
ATOM   7724  O  OG1   . THR A 1 2523 ? 253.829 266.994 244.861 1.00 50.00  ? 2523 THR A OG1   1 
ATOM   7725  C  CG2   . THR A 1 2523 ? 251.681 266.688 243.808 1.00 37.72  ? 2523 THR A CG2   1 
ATOM   7726  N  N     . VAL A 1 2524 ? 250.606 264.804 246.522 1.00 35.35  ? 2524 VAL A N     1 
ATOM   7727  C  CA    . VAL A 1 2524 ? 249.693 265.191 247.603 1.00 35.71  ? 2524 VAL A CA    1 
ATOM   7728  C  C     . VAL A 1 2524 ? 250.320 264.822 248.942 1.00 38.32  ? 2524 VAL A C     1 
ATOM   7729  O  O     . VAL A 1 2524 ? 250.928 263.742 249.057 1.00 35.98  ? 2524 VAL A O     1 
ATOM   7730  C  CB    . VAL A 1 2524 ? 248.337 264.504 247.419 1.00 29.78  ? 2524 VAL A CB    1 
ATOM   7731  C  CG1   . VAL A 1 2524 ? 247.329 265.007 248.439 1.00 26.72  ? 2524 VAL A CG1   1 
ATOM   7732  C  CG2   . VAL A 1 2524 ? 247.823 264.719 246.005 1.00 24.53  ? 2524 VAL A CG2   1 
ATOM   7733  N  N     . PRO A 1 2525 ? 250.226 265.671 249.964 1.00 33.84  ? 2525 PRO A N     1 
ATOM   7734  C  CA    . PRO A 1 2525 ? 250.725 265.285 251.293 1.00 32.07  ? 2525 PRO A CA    1 
ATOM   7735  C  C     . PRO A 1 2525 ? 250.019 264.036 251.799 1.00 37.44  ? 2525 PRO A C     1 
ATOM   7736  O  O     . PRO A 1 2525 ? 248.789 263.955 251.810 1.00 37.99  ? 2525 PRO A O     1 
ATOM   7737  C  CB    . PRO A 1 2525 ? 250.412 266.511 252.158 1.00 28.92  ? 2525 PRO A CB    1 
ATOM   7738  C  CG    . PRO A 1 2525 ? 250.343 267.642 251.193 1.00 35.01  ? 2525 PRO A CG    1 
ATOM   7739  C  CD    . PRO A 1 2525 ? 249.768 267.071 249.933 1.00 35.27  ? 2525 PRO A CD    1 
ATOM   7740  N  N     . LEU A 1 2526 ? 250.812 263.063 252.222 1.00 37.53  ? 2526 LEU A N     1 
ATOM   7741  C  CA    . LEU A 1 2526 ? 250.345 261.751 252.631 1.00 29.77  ? 2526 LEU A CA    1 
ATOM   7742  C  C     . LEU A 1 2526 ? 250.706 261.479 254.084 1.00 33.25  ? 2526 LEU A C     1 
ATOM   7743  O  O     . LEU A 1 2526 ? 251.582 262.141 254.650 1.00 41.48  ? 2526 LEU A O     1 
ATOM   7744  C  CB    . LEU A 1 2526 ? 250.962 260.671 251.733 1.00 34.83  ? 2526 LEU A CB    1 
ATOM   7745  C  CG    . LEU A 1 2526 ? 250.389 260.572 250.320 1.00 35.80  ? 2526 LEU A CG    1 
ATOM   7746  C  CD1   . LEU A 1 2526 ? 250.894 259.322 249.644 1.00 31.16  ? 2526 LEU A CD1   1 
ATOM   7747  C  CD2   . LEU A 1 2526 ? 248.871 260.581 250.353 1.00 31.63  ? 2526 LEU A CD2   1 
ATOM   7748  N  N     . PRO A 1 2527 ? 250.032 260.527 254.731 1.00 36.58  ? 2527 PRO A N     1 
ATOM   7749  C  CA    . PRO A 1 2527 ? 250.412 260.167 256.104 1.00 34.02  ? 2527 PRO A CA    1 
ATOM   7750  C  C     . PRO A 1 2527 ? 251.857 259.696 256.167 1.00 36.43  ? 2527 PRO A C     1 
ATOM   7751  O  O     . PRO A 1 2527 ? 252.344 258.997 255.277 1.00 39.70  ? 2527 PRO A O     1 
ATOM   7752  C  CB    . PRO A 1 2527 ? 249.434 259.043 256.457 1.00 32.90  ? 2527 PRO A CB    1 
ATOM   7753  C  CG    . PRO A 1 2527 ? 248.256 259.288 255.583 1.00 24.73  ? 2527 PRO A CG    1 
ATOM   7754  C  CD    . PRO A 1 2527 ? 248.802 259.837 254.303 1.00 30.23  ? 2527 PRO A CD    1 
ATOM   7755  N  N     . THR A 1 2528 ? 252.538 260.081 257.244 1.00 40.34  ? 2528 THR A N     1 
ATOM   7756  C  CA    . THR A 1 2528 ? 253.981 259.917 257.363 1.00 47.98  ? 2528 THR A CA    1 
ATOM   7757  C  C     . THR A 1 2528 ? 254.385 258.664 258.130 1.00 52.13  ? 2528 THR A C     1 
ATOM   7758  O  O     . THR A 1 2528 ? 255.561 258.522 258.478 1.00 56.69  ? 2528 THR A O     1 
ATOM   7759  C  CB    . THR A 1 2528 ? 254.594 261.149 258.029 1.00 48.69  ? 2528 THR A CB    1 
ATOM   7760  O  OG1   . THR A 1 2528 ? 254.052 261.298 259.347 1.00 55.61  ? 2528 THR A OG1   1 
ATOM   7761  C  CG2   . THR A 1 2528 ? 254.289 262.398 257.219 1.00 41.04  ? 2528 THR A CG2   1 
ATOM   7762  N  N     . ALA A 1 2529 ? 253.453 257.762 258.408 1.00 52.52  ? 2529 ALA A N     1 
ATOM   7763  C  CA    . ALA A 1 2529 ? 253.796 256.552 259.146 1.00 61.05  ? 2529 ALA A CA    1 
ATOM   7764  C  C     . ALA A 1 2529 ? 254.714 255.669 258.308 1.00 66.86  ? 2529 ALA A C     1 
ATOM   7765  O  O     . ALA A 1 2529 ? 254.418 255.412 257.135 1.00 66.30  ? 2529 ALA A O     1 
ATOM   7766  C  CB    . ALA A 1 2529 ? 252.542 255.781 259.537 1.00 53.77  ? 2529 ALA A CB    1 
ATOM   7767  N  N     . PRO A 1 2530 ? 255.833 255.199 258.863 1.00 62.34  ? 2530 PRO A N     1 
ATOM   7768  C  CA    . PRO A 1 2530 ? 256.754 254.369 258.069 1.00 66.20  ? 2530 PRO A CA    1 
ATOM   7769  C  C     . PRO A 1 2530 ? 256.150 253.060 257.589 1.00 65.59  ? 2530 PRO A C     1 
ATOM   7770  O  O     . PRO A 1 2530 ? 256.541 252.566 256.524 1.00 62.23  ? 2530 PRO A O     1 
ATOM   7771  C  CB    . PRO A 1 2530 ? 257.926 254.127 259.032 1.00 66.98  ? 2530 PRO A CB    1 
ATOM   7772  C  CG    . PRO A 1 2530 ? 257.372 254.384 260.396 1.00 68.45  ? 2530 PRO A CG    1 
ATOM   7773  C  CD    . PRO A 1 2530 ? 256.326 255.437 260.229 1.00 58.18  ? 2530 PRO A CD    1 
ATOM   7774  N  N     . ASN A 1 2531 ? 255.214 252.476 258.339 1.00 63.95  ? 2531 ASN A N     1 
ATOM   7775  C  CA    . ASN A 1 2531 ? 254.711 251.144 258.034 1.00 62.65  ? 2531 ASN A CA    1 
ATOM   7776  C  C     . ASN A 1 2531 ? 253.206 251.055 257.819 1.00 53.77  ? 2531 ASN A C     1 
ATOM   7777  O  O     . ASN A 1 2531 ? 252.755 250.094 257.187 1.00 46.25  ? 2531 ASN A O     1 
ATOM   7778  C  CB    . ASN A 1 2531 ? 255.119 250.158 259.143 1.00 64.07  ? 2531 ASN A CB    1 
ATOM   7779  C  CG    . ASN A 1 2531 ? 254.510 250.499 260.494 1.00 73.37  ? 2531 ASN A CG    1 
ATOM   7780  O  OD1   . ASN A 1 2531 ? 253.681 251.400 260.615 1.00 73.03  ? 2531 ASN A OD1   1 
ATOM   7781  N  ND2   . ASN A 1 2531 ? 254.927 249.772 261.525 1.00 73.80  ? 2531 ASN A ND2   1 
ATOM   7782  N  N     . ILE A 1 2532 ? 252.425 252.004 258.315 1.00 50.97  ? 2532 ILE A N     1 
ATOM   7783  C  CA    . ILE A 1 2532 ? 250.970 251.937 258.159 1.00 41.44  ? 2532 ILE A CA    1 
ATOM   7784  C  C     . ILE A 1 2532 ? 250.613 252.302 256.720 1.00 36.87  ? 2532 ILE A C     1 
ATOM   7785  O  O     . ILE A 1 2532 ? 251.011 253.378 256.246 1.00 42.84  ? 2532 ILE A O     1 
ATOM   7786  C  CB    . ILE A 1 2532 ? 250.279 252.868 259.147 1.00 42.51  ? 2532 ILE A CB    1 
ATOM   7787  C  CG1   . ILE A 1 2532 ? 250.574 252.437 260.583 1.00 51.33  ? 2532 ILE A CG1   1 
ATOM   7788  C  CG2   . ILE A 1 2532 ? 248.781 252.865 258.910 1.00 29.91  ? 2532 ILE A CG2   1 
ATOM   7789  C  CD1   . ILE A 1 2532 ? 250.145 253.450 261.620 1.00 43.68  ? 2532 ILE A CD1   1 
ATOM   7790  N  N     . PRO A 1 2533 ? 249.884 251.452 256.002 1.00 29.20  ? 2533 PRO A N     1 
ATOM   7791  C  CA    . PRO A 1 2533 ? 249.484 251.792 254.633 1.00 26.18  ? 2533 PRO A CA    1 
ATOM   7792  C  C     . PRO A 1 2533 ? 248.468 252.925 254.608 1.00 24.06  ? 2533 PRO A C     1 
ATOM   7793  O  O     . PRO A 1 2533 ? 247.775 253.206 255.589 1.00 33.55  ? 2533 PRO A O     1 
ATOM   7794  C  CB    . PRO A 1 2533 ? 248.878 250.490 254.102 1.00 22.36  ? 2533 PRO A CB    1 
ATOM   7795  C  CG    . PRO A 1 2533 ? 248.447 249.755 255.313 1.00 18.61  ? 2533 PRO A CG    1 
ATOM   7796  C  CD    . PRO A 1 2533 ? 249.428 250.107 256.392 1.00 28.34  ? 2533 PRO A CD    1 
ATOM   7797  N  N     . ILE A 1 2534 ? 248.396 253.586 253.451 1.00 19.13  ? 2534 ILE A N     1 
ATOM   7798  C  CA    . ILE A 1 2534 ? 247.515 254.739 253.294 1.00 21.78  ? 2534 ILE A CA    1 
ATOM   7799  C  C     . ILE A 1 2534 ? 246.055 254.323 253.400 1.00 20.15  ? 2534 ILE A C     1 
ATOM   7800  O  O     . ILE A 1 2534 ? 245.200 255.117 253.814 1.00 18.77  ? 2534 ILE A O     1 
ATOM   7801  C  CB    . ILE A 1 2534 ? 247.808 255.447 251.955 1.00 13.88  ? 2534 ILE A CB    1 
ATOM   7802  C  CG1   . ILE A 1 2534 ? 249.277 255.855 251.887 1.00 24.42  ? 2534 ILE A CG1   1 
ATOM   7803  C  CG2   . ILE A 1 2534 ? 246.954 256.689 251.805 1.00 11.40  ? 2534 ILE A CG2   1 
ATOM   7804  C  CD1   . ILE A 1 2534 ? 249.790 256.018 250.480 1.00 28.82  ? 2534 ILE A CD1   1 
ATOM   7805  N  N     . ILE A 1 2535 ? 245.743 253.074 253.048 1.00 19.07  ? 2535 ILE A N     1 
ATOM   7806  C  CA    . ILE A 1 2535 ? 244.376 252.577 253.099 1.00 20.45  ? 2535 ILE A CA    1 
ATOM   7807  C  C     . ILE A 1 2535 ? 243.807 252.561 254.511 1.00 19.85  ? 2535 ILE A C     1 
ATOM   7808  O  O     . ILE A 1 2535 ? 242.592 252.422 254.679 1.00 17.62  ? 2535 ILE A O     1 
ATOM   7809  C  CB    . ILE A 1 2535 ? 244.303 251.166 252.471 1.00 21.00  ? 2535 ILE A CB    1 
ATOM   7810  C  CG1   . ILE A 1 2535 ? 242.925 250.922 251.852 1.00 23.21  ? 2535 ILE A CG1   1 
ATOM   7811  C  CG2   . ILE A 1 2535 ? 244.635 250.096 253.501 1.00 16.01  ? 2535 ILE A CG2   1 
ATOM   7812  C  CD1   . ILE A 1 2535 ? 242.673 251.713 250.590 1.00 17.14  ? 2535 ILE A CD1   1 
ATOM   7813  N  N     . ASP A 1 2536 ? 244.649 252.713 255.531 1.00 19.07  ? 2536 ASP A N     1 
ATOM   7814  C  CA    . ASP A 1 2536 ? 244.198 252.720 256.915 1.00 17.15  ? 2536 ASP A CA    1 
ATOM   7815  C  C     . ASP A 1 2536 ? 243.829 254.111 257.410 1.00 21.51  ? 2536 ASP A C     1 
ATOM   7816  O  O     . ASP A 1 2536 ? 243.513 254.266 258.595 1.00 25.20  ? 2536 ASP A O     1 
ATOM   7817  C  CB    . ASP A 1 2536 ? 245.273 252.123 257.827 1.00 18.61  ? 2536 ASP A CB    1 
ATOM   7818  C  CG    . ASP A 1 2536 ? 245.461 250.638 257.609 1.00 28.98  ? 2536 ASP A CG    1 
ATOM   7819  O  OD1   . ASP A 1 2536 ? 244.487 249.966 257.214 1.00 38.42  ? 2536 ASP A OD1   1 
ATOM   7820  O  OD2   . ASP A 1 2536 ? 246.576 250.137 257.857 1.00 30.55  ? 2536 ASP A OD2   1 
ATOM   7821  N  N     . TYR A 1 2537 ? 243.865 255.119 256.546 1.00 17.09  ? 2537 TYR A N     1 
ATOM   7822  C  CA    . TYR A 1 2537 ? 243.542 256.487 256.916 1.00 15.26  ? 2537 TYR A CA    1 
ATOM   7823  C  C     . TYR A 1 2537 ? 242.295 256.963 256.188 1.00 17.15  ? 2537 TYR A C     1 
ATOM   7824  O  O     . TYR A 1 2537 ? 241.945 256.463 255.115 1.00 23.34  ? 2537 TYR A O     1 
ATOM   7825  C  CB    . TYR A 1 2537 ? 244.697 257.440 256.597 1.00 23.15  ? 2537 TYR A CB    1 
ATOM   7826  C  CG    . TYR A 1 2537 ? 245.978 257.133 257.325 1.00 23.73  ? 2537 TYR A CG    1 
ATOM   7827  C  CD1   . TYR A 1 2537 ? 246.889 256.221 256.813 1.00 20.74  ? 2537 TYR A CD1   1 
ATOM   7828  C  CD2   . TYR A 1 2537 ? 246.283 257.765 258.520 1.00 19.67  ? 2537 TYR A CD2   1 
ATOM   7829  C  CE1   . TYR A 1 2537 ? 248.061 255.945 257.475 1.00 24.48  ? 2537 TYR A CE1   1 
ATOM   7830  C  CE2   . TYR A 1 2537 ? 247.451 257.495 259.189 1.00 23.00  ? 2537 TYR A CE2   1 
ATOM   7831  C  CZ    . TYR A 1 2537 ? 248.337 256.584 258.662 1.00 34.89  ? 2537 TYR A CZ    1 
ATOM   7832  O  OH    . TYR A 1 2537 ? 249.505 256.313 259.329 1.00 43.23  ? 2537 TYR A OH    1 
ATOM   7833  N  N     . GLU A 1 2538 ? 241.628 257.939 256.790 1.00 19.76  ? 2538 GLU A N     1 
ATOM   7834  C  CA    . GLU A 1 2538 ? 240.532 258.669 256.182 1.00 16.28  ? 2538 GLU A CA    1 
ATOM   7835  C  C     . GLU A 1 2538 ? 240.881 260.150 256.151 1.00 22.66  ? 2538 GLU A C     1 
ATOM   7836  O  O     . GLU A 1 2538 ? 241.873 260.593 256.735 1.00 26.47  ? 2538 GLU A O     1 
ATOM   7837  C  CB    . GLU A 1 2538 ? 239.222 258.437 256.943 1.00 14.24  ? 2538 GLU A CB    1 
ATOM   7838  C  CG    . GLU A 1 2538 ? 239.255 258.887 258.391 1.00 19.84  ? 2538 GLU A CG    1 
ATOM   7839  C  CD    . GLU A 1 2538 ? 237.886 259.279 258.908 1.00 29.95  ? 2538 GLU A CD    1 
ATOM   7840  O  OE1   . GLU A 1 2538 ? 236.955 259.416 258.088 1.00 24.31  ? 2538 GLU A OE1   1 
ATOM   7841  O  OE2   . GLU A 1 2538 ? 237.739 259.445 260.136 1.00 38.48  ? 2538 GLU A OE2   1 
ATOM   7842  N  N     . VAL A 1 2539 ? 240.056 260.917 255.452 1.00 19.41  ? 2539 VAL A N     1 
ATOM   7843  C  CA    . VAL A 1 2539 ? 240.259 262.351 255.299 1.00 15.58  ? 2539 VAL A CA    1 
ATOM   7844  C  C     . VAL A 1 2539 ? 239.209 263.057 256.142 1.00 23.23  ? 2539 VAL A C     1 
ATOM   7845  O  O     . VAL A 1 2539 ? 238.004 262.922 255.895 1.00 24.42  ? 2539 VAL A O     1 
ATOM   7846  C  CB    . VAL A 1 2539 ? 240.178 262.786 253.830 1.00 18.40  ? 2539 VAL A CB    1 
ATOM   7847  C  CG1   . VAL A 1 2539 ? 240.631 264.225 253.686 1.00 19.95  ? 2539 VAL A CG1   1 
ATOM   7848  C  CG2   . VAL A 1 2539 ? 241.016 261.867 252.961 1.00 14.57  ? 2539 VAL A CG2   1 
ATOM   7849  N  N     . SER A 1 2540 ? 239.663 263.803 257.145 1.00 24.03  ? 2540 SER A N     1 
ATOM   7850  C  CA    . SER A 1 2540 ? 238.751 264.603 257.944 1.00 21.86  ? 2540 SER A CA    1 
ATOM   7851  C  C     . SER A 1 2540 ? 238.280 265.813 257.151 1.00 26.43  ? 2540 SER A C     1 
ATOM   7852  O  O     . SER A 1 2540 ? 238.941 266.267 256.214 1.00 28.17  ? 2540 SER A O     1 
ATOM   7853  C  CB    . SER A 1 2540 ? 239.427 265.056 259.238 1.00 24.99  ? 2540 SER A CB    1 
ATOM   7854  O  OG    . SER A 1 2540 ? 240.698 265.623 258.975 1.00 34.25  ? 2540 SER A OG    1 
ATOM   7855  N  N     . ILE A 1 2541 ? 237.113 266.337 257.533 1.00 27.57  ? 2541 ILE A N     1 
ATOM   7856  C  CA    . ILE A 1 2541 ? 236.579 267.514 256.863 1.00 19.30  ? 2541 ILE A CA    1 
ATOM   7857  C  C     . ILE A 1 2541 ? 237.479 268.723 257.079 1.00 26.30  ? 2541 ILE A C     1 
ATOM   7858  O  O     . ILE A 1 2541 ? 237.434 269.677 256.292 1.00 35.42  ? 2541 ILE A O     1 
ATOM   7859  C  CB    . ILE A 1 2541 ? 235.140 267.787 257.340 1.00 22.75  ? 2541 ILE A CB    1 
ATOM   7860  C  CG1   . ILE A 1 2541 ? 234.455 268.808 256.431 1.00 30.78  ? 2541 ILE A CG1   1 
ATOM   7861  C  CG2   . ILE A 1 2541 ? 235.133 268.261 258.784 1.00 30.99  ? 2541 ILE A CG2   1 
ATOM   7862  C  CD1   . ILE A 1 2541 ? 234.232 268.310 255.020 1.00 23.19  ? 2541 ILE A CD1   1 
ATOM   7863  N  N     . SER A 1 2542 ? 238.313 268.704 258.120 1.00 24.77  ? 2542 SER A N     1 
ATOM   7864  C  CA    . SER A 1 2542 ? 239.287 269.763 258.343 1.00 31.78  ? 2542 SER A CA    1 
ATOM   7865  C  C     . SER A 1 2542 ? 240.432 269.731 257.339 1.00 33.98  ? 2542 SER A C     1 
ATOM   7866  O  O     . SER A 1 2542 ? 241.231 270.674 257.309 1.00 41.53  ? 2542 SER A O     1 
ATOM   7867  C  CB    . SER A 1 2542 ? 239.849 269.668 259.762 1.00 34.36  ? 2542 SER A CB    1 
ATOM   7868  O  OG    . SER A 1 2542 ? 240.747 268.580 259.880 1.00 32.52  ? 2542 SER A OG    1 
ATOM   7869  N  N     . GLY A 1 2543 ? 240.539 268.680 256.531 1.00 27.04  ? 2543 GLY A N     1 
ATOM   7870  C  CA    . GLY A 1 2543 ? 241.573 268.608 255.522 1.00 28.78  ? 2543 GLY A CA    1 
ATOM   7871  C  C     . GLY A 1 2543 ? 242.861 267.956 255.962 1.00 32.05  ? 2543 GLY A C     1 
ATOM   7872  O  O     . GLY A 1 2543 ? 243.928 268.309 255.446 1.00 33.39  ? 2543 GLY A O     1 
ATOM   7873  N  N     . GLU A 1 2544 ? 242.802 267.016 256.899 1.00 29.34  ? 2544 GLU A N     1 
ATOM   7874  C  CA    . GLU A 1 2544 ? 243.985 266.329 257.393 1.00 29.88  ? 2544 GLU A CA    1 
ATOM   7875  C  C     . GLU A 1 2544 ? 243.724 264.831 257.440 1.00 29.66  ? 2544 GLU A C     1 
ATOM   7876  O  O     . GLU A 1 2544 ? 242.600 264.388 257.689 1.00 30.91  ? 2544 GLU A O     1 
ATOM   7877  C  CB    . GLU A 1 2544 ? 244.385 266.844 258.786 1.00 36.86  ? 2544 GLU A CB    1 
ATOM   7878  C  CG    . GLU A 1 2544 ? 245.641 266.207 259.359 1.00 44.53  ? 2544 GLU A CG    1 
ATOM   7879  C  CD    . GLU A 1 2544 ? 246.883 266.536 258.555 1.00 46.45  ? 2544 GLU A CD    1 
ATOM   7880  O  OE1   . GLU A 1 2544 ? 246.901 267.591 257.886 1.00 44.54  ? 2544 GLU A OE1   1 
ATOM   7881  O  OE2   . GLU A 1 2544 ? 247.841 265.735 258.588 1.00 43.81  ? 2544 GLU A OE2   1 
ATOM   7882  N  N     . TRP A 1 2545 ? 244.774 264.054 257.187 1.00 31.07  ? 2545 TRP A N     1 
ATOM   7883  C  CA    . TRP A 1 2545 ? 244.681 262.606 257.301 1.00 28.04  ? 2545 TRP A CA    1 
ATOM   7884  C  C     . TRP A 1 2545 ? 244.479 262.212 258.760 1.00 30.75  ? 2545 TRP A C     1 
ATOM   7885  O  O     . TRP A 1 2545 ? 245.140 262.745 259.655 1.00 34.52  ? 2545 TRP A O     1 
ATOM   7886  C  CB    . TRP A 1 2545 ? 245.946 261.944 256.756 1.00 28.04  ? 2545 TRP A CB    1 
ATOM   7887  C  CG    . TRP A 1 2545 ? 246.107 262.028 255.271 1.00 23.31  ? 2545 TRP A CG    1 
ATOM   7888  C  CD1   . TRP A 1 2545 ? 246.962 262.840 254.588 1.00 27.16  ? 2545 TRP A CD1   1 
ATOM   7889  C  CD2   . TRP A 1 2545 ? 245.399 261.271 254.283 1.00 23.53  ? 2545 TRP A CD2   1 
ATOM   7890  N  NE1   . TRP A 1 2545 ? 246.834 262.634 253.237 1.00 27.21  ? 2545 TRP A NE1   1 
ATOM   7891  C  CE2   . TRP A 1 2545 ? 245.879 261.675 253.024 1.00 21.73  ? 2545 TRP A CE2   1 
ATOM   7892  C  CE3   . TRP A 1 2545 ? 244.405 260.288 254.343 1.00 24.49  ? 2545 TRP A CE3   1 
ATOM   7893  C  CZ2   . TRP A 1 2545 ? 245.401 261.135 251.834 1.00 18.33  ? 2545 TRP A CZ2   1 
ATOM   7894  C  CZ3   . TRP A 1 2545 ? 243.933 259.753 253.160 1.00 19.88  ? 2545 TRP A CZ3   1 
ATOM   7895  C  CH2   . TRP A 1 2545 ? 244.429 260.177 251.923 1.00 16.29  ? 2545 TRP A CH2   1 
ATOM   7896  N  N     . SER A 1 2546 ? 243.565 261.272 259.000 1.00 26.58  ? 2546 SER A N     1 
ATOM   7897  C  CA    . SER A 1 2546 ? 243.322 260.759 260.339 1.00 22.89  ? 2546 SER A CA    1 
ATOM   7898  C  C     . SER A 1 2546 ? 243.261 259.239 260.275 1.00 23.99  ? 2546 SER A C     1 
ATOM   7899  O  O     . SER A 1 2546 ? 242.572 258.684 259.405 1.00 26.42  ? 2546 SER A O     1 
ATOM   7900  C  CB    . SER A 1 2546 ? 242.022 261.325 260.923 1.00 28.32  ? 2546 SER A CB    1 
ATOM   7901  O  OG    . SER A 1 2546 ? 240.951 261.191 260.006 1.00 35.58  ? 2546 SER A OG    1 
ATOM   7902  N  N     . PRO A 1 2547 ? 243.954 258.530 261.164 1.00 29.94  ? 2547 PRO A N     1 
ATOM   7903  C  CA    . PRO A 1 2547 ? 243.902 257.066 261.131 1.00 27.37  ? 2547 PRO A CA    1 
ATOM   7904  C  C     . PRO A 1 2547 ? 242.503 256.551 261.436 1.00 24.97  ? 2547 PRO A C     1 
ATOM   7905  O  O     . PRO A 1 2547 ? 241.760 257.132 262.231 1.00 24.99  ? 2547 PRO A O     1 
ATOM   7906  C  CB    . PRO A 1 2547 ? 244.903 256.649 262.214 1.00 22.36  ? 2547 PRO A CB    1 
ATOM   7907  C  CG    . PRO A 1 2547 ? 244.975 257.820 263.130 1.00 21.80  ? 2547 PRO A CG    1 
ATOM   7908  C  CD    . PRO A 1 2547 ? 244.785 259.033 262.270 1.00 21.53  ? 2547 PRO A CD    1 
ATOM   7909  N  N     . TRP A 1 2548 ? 242.145 255.444 260.782 1.00 21.33  ? 2548 TRP A N     1 
ATOM   7910  C  CA    . TRP A 1 2548 ? 240.845 254.824 261.012 1.00 21.46  ? 2548 TRP A CA    1 
ATOM   7911  C  C     . TRP A 1 2548 ? 240.724 254.226 262.406 1.00 21.40  ? 2548 TRP A C     1 
ATOM   7912  O  O     . TRP A 1 2548 ? 239.604 254.033 262.888 1.00 22.15  ? 2548 TRP A O     1 
ATOM   7913  C  CB    . TRP A 1 2548 ? 240.583 253.741 259.966 1.00 20.52  ? 2548 TRP A CB    1 
ATOM   7914  C  CG    . TRP A 1 2548 ? 239.883 254.231 258.740 1.00 15.52  ? 2548 TRP A CG    1 
ATOM   7915  C  CD1   . TRP A 1 2548 ? 240.352 254.197 257.460 1.00 14.12  ? 2548 TRP A CD1   1 
ATOM   7916  C  CD2   . TRP A 1 2548 ? 238.575 254.808 258.673 1.00 14.69  ? 2548 TRP A CD2   1 
ATOM   7917  N  NE1   . TRP A 1 2548 ? 239.421 254.725 256.602 1.00 15.44  ? 2548 TRP A NE1   1 
ATOM   7918  C  CE2   . TRP A 1 2548 ? 238.321 255.107 257.322 1.00 14.02  ? 2548 TRP A CE2   1 
ATOM   7919  C  CE3   . TRP A 1 2548 ? 237.597 255.105 259.625 1.00 14.07  ? 2548 TRP A CE3   1 
ATOM   7920  C  CZ2   . TRP A 1 2548 ? 237.129 255.689 256.900 1.00 12.67  ? 2548 TRP A CZ2   1 
ATOM   7921  C  CZ3   . TRP A 1 2548 ? 236.418 255.682 259.204 1.00 13.78  ? 2548 TRP A CZ3   1 
ATOM   7922  C  CH2   . TRP A 1 2548 ? 236.194 255.969 257.855 1.00 12.48  ? 2548 TRP A CH2   1 
ATOM   7923  N  N     . GLN A 1 2549 ? 241.849 253.935 263.063 1.00 26.53  ? 2549 GLN A N     1 
ATOM   7924  C  CA    . GLN A 1 2549 ? 241.809 253.352 264.397 1.00 27.61  ? 2549 GLN A CA    1 
ATOM   7925  C  C     . GLN A 1 2549 ? 241.144 254.273 265.411 1.00 26.98  ? 2549 GLN A C     1 
ATOM   7926  O  O     . GLN A 1 2549 ? 240.617 253.788 266.419 1.00 33.71  ? 2549 GLN A O     1 
ATOM   7927  C  CB    . GLN A 1 2549 ? 243.225 253.003 264.856 1.00 21.85  ? 2549 GLN A CB    1 
ATOM   7928  C  CG    . GLN A 1 2549 ? 243.281 251.916 265.912 1.00 26.96  ? 2549 GLN A CG    1 
ATOM   7929  C  CD    . GLN A 1 2549 ? 242.879 250.559 265.373 1.00 24.92  ? 2549 GLN A CD    1 
ATOM   7930  O  OE1   . GLN A 1 2549 ? 241.903 249.963 265.825 1.00 26.41  ? 2549 GLN A OE1   1 
ATOM   7931  N  NE2   . GLN A 1 2549 ? 243.632 250.063 264.400 1.00 22.86  ? 2549 GLN A NE2   1 
ATOM   7932  N  N     . ALA A 1 2550 ? 241.156 255.586 265.171 1.00 22.13  ? 2550 ALA A N     1 
ATOM   7933  C  CA    . ALA A 1 2550 ? 240.462 256.504 266.066 1.00 25.21  ? 2550 ALA A CA    1 
ATOM   7934  C  C     . ALA A 1 2550 ? 238.953 256.303 266.015 1.00 24.24  ? 2550 ALA A C     1 
ATOM   7935  O  O     . ALA A 1 2550 ? 238.253 256.632 266.978 1.00 26.67  ? 2550 ALA A O     1 
ATOM   7936  C  CB    . ALA A 1 2550 ? 240.820 257.948 265.719 1.00 25.69  ? 2550 ALA A CB    1 
ATOM   7937  N  N     . LYS A 1 2551 ? 238.438 255.772 264.909 1.00 24.47  ? 2551 LYS A N     1 
ATOM   7938  C  CA    . LYS A 1 2551 ? 237.024 255.445 264.784 1.00 17.36  ? 2551 LYS A CA    1 
ATOM   7939  C  C     . LYS A 1 2551 ? 236.701 254.043 265.273 1.00 23.98  ? 2551 LYS A C     1 
ATOM   7940  O  O     . LYS A 1 2551 ? 235.541 253.626 265.191 1.00 29.73  ? 2551 LYS A O     1 
ATOM   7941  C  CB    . LYS A 1 2551 ? 236.570 255.593 263.330 1.00 19.14  ? 2551 LYS A CB    1 
ATOM   7942  C  CG    . LYS A 1 2551 ? 236.710 256.993 262.769 1.00 24.11  ? 2551 LYS A CG    1 
ATOM   7943  C  CD    . LYS A 1 2551 ? 235.744 257.948 263.443 1.00 22.72  ? 2551 LYS A CD    1 
ATOM   7944  C  CE    . LYS A 1 2551 ? 235.723 259.288 262.739 1.00 24.73  ? 2551 LYS A CE    1 
ATOM   7945  N  NZ    . LYS A 1 2551 ? 235.117 259.171 261.383 1.00 24.13  ? 2551 LYS A NZ    1 
ATOM   7946  N  N     . VAL A 1 2552 ? 237.690 253.309 265.771 1.00 26.39  ? 2552 VAL A N     1 
ATOM   7947  C  CA    . VAL A 1 2552 ? 237.487 251.947 266.255 1.00 25.48  ? 2552 VAL A CA    1 
ATOM   7948  C  C     . VAL A 1 2552 ? 237.699 251.935 267.763 1.00 27.56  ? 2552 VAL A C     1 
ATOM   7949  O  O     . VAL A 1 2552 ? 238.831 251.737 268.228 1.00 31.79  ? 2552 VAL A O     1 
ATOM   7950  C  CB    . VAL A 1 2552 ? 238.431 250.959 265.553 1.00 24.93  ? 2552 VAL A CB    1 
ATOM   7951  C  CG1   . VAL A 1 2552 ? 238.175 249.540 266.036 1.00 23.02  ? 2552 VAL A CG1   1 
ATOM   7952  C  CG2   . VAL A 1 2552 ? 238.277 251.054 264.049 1.00 19.76  ? 2552 VAL A CG2   1 
ATOM   7953  N  N     . PRO A 1 2553 ? 236.660 252.155 268.560 1.00 30.29  ? 2553 PRO A N     1 
ATOM   7954  C  CA    . PRO A 1 2553 ? 236.809 252.096 270.014 1.00 30.74  ? 2553 PRO A CA    1 
ATOM   7955  C  C     . PRO A 1 2553 ? 236.521 250.710 270.563 1.00 37.14  ? 2553 PRO A C     1 
ATOM   7956  O  O     . PRO A 1 2553 ? 235.656 249.979 270.077 1.00 43.30  ? 2553 PRO A O     1 
ATOM   7957  C  CB    . PRO A 1 2553 ? 235.760 253.105 270.500 1.00 39.21  ? 2553 PRO A CB    1 
ATOM   7958  C  CG    . PRO A 1 2553 ? 234.668 253.009 269.472 1.00 39.04  ? 2553 PRO A CG    1 
ATOM   7959  C  CD    . PRO A 1 2553 ? 235.302 252.573 268.165 1.00 30.07  ? 2553 PRO A CD    1 
ATOM   7960  N  N     . GLN A 1 2554 ? 237.276 250.351 271.597 1.00 40.20  ? 2554 GLN A N     1 
ATOM   7961  C  CA    . GLN A 1 2554 ? 237.041 249.095 272.299 1.00 33.98  ? 2554 GLN A CA    1 
ATOM   7962  C  C     . GLN A 1 2554 ? 235.744 249.212 273.089 1.00 33.27  ? 2554 GLN A C     1 
ATOM   7963  O  O     . GLN A 1 2554 ? 235.701 249.872 274.132 1.00 41.73  ? 2554 GLN A O     1 
ATOM   7964  C  CB    . GLN A 1 2554 ? 238.216 248.766 273.212 1.00 34.61  ? 2554 GLN A CB    1 
ATOM   7965  C  CG    . GLN A 1 2554 ? 238.095 247.427 273.919 1.00 40.75  ? 2554 GLN A CG    1 
ATOM   7966  C  CD    . GLN A 1 2554 ? 239.306 247.108 274.771 1.00 55.18  ? 2554 GLN A CD    1 
ATOM   7967  O  OE1   . GLN A 1 2554 ? 240.237 247.907 274.871 1.00 68.76  ? 2554 GLN A OE1   1 
ATOM   7968  N  NE2   . GLN A 1 2554 ? 239.301 245.935 275.393 1.00 51.97  ? 2554 GLN A NE2   1 
ATOM   7969  N  N     . ILE A 1 2555 ? 234.687 248.579 272.595 1.00 30.16  ? 2555 ILE A N     1 
ATOM   7970  C  CA    . ILE A 1 2555 ? 233.376 248.667 273.210 1.00 33.21  ? 2555 ILE A CA    1 
ATOM   7971  C  C     . ILE A 1 2555 ? 233.184 247.481 274.142 1.00 33.67  ? 2555 ILE A C     1 
ATOM   7972  O  O     . ILE A 1 2555 ? 233.904 246.480 274.083 1.00 35.48  ? 2555 ILE A O     1 
ATOM   7973  C  CB    . ILE A 1 2555 ? 232.244 248.721 272.158 1.00 36.85  ? 2555 ILE A CB    1 
ATOM   7974  C  CG1   . ILE A 1 2555 ? 232.178 247.405 271.381 1.00 29.74  ? 2555 ILE A CG1   1 
ATOM   7975  C  CG2   . ILE A 1 2555 ? 232.448 249.896 271.214 1.00 31.29  ? 2555 ILE A CG2   1 
ATOM   7976  C  CD1   . ILE A 1 2555 ? 230.897 247.220 270.604 1.00 25.30  ? 2555 ILE A CD1   1 
ATOM   7977  N  N     . GLU A 1 2556 ? 232.197 247.598 275.024 1.00 34.72  ? 2556 GLU A N     1 
ATOM   7978  C  CA    . GLU A 1 2556 ? 231.789 246.518 275.918 1.00 33.35  ? 2556 GLU A CA    1 
ATOM   7979  C  C     . GLU A 1 2556 ? 230.332 246.199 275.608 1.00 34.43  ? 2556 GLU A C     1 
ATOM   7980  O  O     . GLU A 1 2556 ? 229.426 246.925 276.030 1.00 38.39  ? 2556 GLU A O     1 
ATOM   7981  C  CB    . GLU A 1 2556 ? 231.981 246.905 277.381 1.00 30.96  ? 2556 GLU A CB    1 
ATOM   7982  C  CG    . GLU A 1 2556 ? 233.403 247.299 277.746 1.00 40.32  ? 2556 GLU A CG    1 
ATOM   7983  C  CD    . GLU A 1 2556 ? 234.299 246.102 278.002 1.00 44.53  ? 2556 GLU A CD    1 
ATOM   7984  O  OE1   . GLU A 1 2556 ? 234.531 245.312 277.063 1.00 45.38  ? 2556 GLU A OE1   1 
ATOM   7985  O  OE2   . GLU A 1 2556 ? 234.773 245.951 279.149 1.00 47.35  ? 2556 GLU A OE2   1 
ATOM   7986  N  N     . VAL A 1 2557 ? 230.109 245.116 274.863 1.00 32.49  ? 2557 VAL A N     1 
ATOM   7987  C  CA    . VAL A 1 2557 ? 228.757 244.715 274.500 1.00 28.12  ? 2557 VAL A CA    1 
ATOM   7988  C  C     . VAL A 1 2557 ? 227.989 244.324 275.755 1.00 36.31  ? 2557 VAL A C     1 
ATOM   7989  O  O     . VAL A 1 2557 ? 228.549 243.745 276.695 1.00 37.48  ? 2557 VAL A O     1 
ATOM   7990  C  CB    . VAL A 1 2557 ? 228.798 243.560 273.485 1.00 25.84  ? 2557 VAL A CB    1 
ATOM   7991  C  CG1   . VAL A 1 2557 ? 227.400 243.242 272.974 1.00 29.25  ? 2557 VAL A CG1   1 
ATOM   7992  C  CG2   . VAL A 1 2557 ? 229.722 243.903 272.333 1.00 30.33  ? 2557 VAL A CG2   1 
ATOM   7993  N  N     . GLU A 1 2558 ? 226.699 244.652 275.779 1.00 38.25  ? 2558 GLU A N     1 
ATOM   7994  C  CA    . GLU A 1 2558 ? 225.856 244.281 276.904 1.00 33.27  ? 2558 GLU A CA    1 
ATOM   7995  C  C     . GLU A 1 2558 ? 225.772 242.764 277.027 1.00 33.34  ? 2558 GLU A C     1 
ATOM   7996  O  O     . GLU A 1 2558 ? 225.859 242.031 276.038 1.00 38.55  ? 2558 GLU A O     1 
ATOM   7997  C  CB    . GLU A 1 2558 ? 224.455 244.875 276.745 1.00 42.52  ? 2558 GLU A CB    1 
ATOM   7998  C  CG    . GLU A 1 2558 ? 224.398 246.394 276.835 1.00 50.60  ? 2558 GLU A CG    1 
ATOM   7999  C  CD    . GLU A 1 2558 ? 224.747 247.081 275.528 1.00 59.17  ? 2558 GLU A CD    1 
ATOM   8000  O  OE1   . GLU A 1 2558 ? 224.976 246.375 274.524 1.00 61.18  ? 2558 GLU A OE1   1 
ATOM   8001  O  OE2   . GLU A 1 2558 ? 224.792 248.329 275.507 1.00 49.09  ? 2558 GLU A OE2   1 
ATOM   8002  N  N     . THR A 1 2559 ? 225.607 242.295 278.266 1.00 36.92  ? 2559 THR A N     1 
ATOM   8003  C  CA    . THR A 1 2559 ? 225.625 240.859 278.528 1.00 36.94  ? 2559 THR A CA    1 
ATOM   8004  C  C     . THR A 1 2559 ? 224.483 240.146 277.814 1.00 31.64  ? 2559 THR A C     1 
ATOM   8005  O  O     . THR A 1 2559 ? 224.668 239.049 277.274 1.00 36.74  ? 2559 THR A O     1 
ATOM   8006  C  CB    . THR A 1 2559 ? 225.561 240.603 280.034 1.00 37.54  ? 2559 THR A CB    1 
ATOM   8007  O  OG1   . THR A 1 2559 ? 226.691 241.211 280.671 1.00 39.29  ? 2559 THR A OG1   1 
ATOM   8008  C  CG2   . THR A 1 2559 ? 225.573 239.116 280.322 1.00 37.95  ? 2559 THR A CG2   1 
ATOM   8009  N  N     . HIS A 1 2560 ? 223.299 240.751 277.791 1.00 31.10  ? 2560 HIS A N     1 
ATOM   8010  C  CA    . HIS A 1 2560 ? 222.157 240.137 277.126 1.00 32.63  ? 2560 HIS A CA    1 
ATOM   8011  C  C     . HIS A 1 2560 ? 222.220 240.248 275.609 1.00 33.86  ? 2560 HIS A C     1 
ATOM   8012  O  O     . HIS A 1 2560 ? 221.393 239.636 274.926 1.00 38.64  ? 2560 HIS A O     1 
ATOM   8013  C  CB    . HIS A 1 2560 ? 220.857 240.762 277.635 1.00 33.17  ? 2560 HIS A CB    1 
ATOM   8014  C  CG    . HIS A 1 2560 ? 220.444 241.989 276.885 1.00 42.48  ? 2560 HIS A CG    1 
ATOM   8015  N  ND1   . HIS A 1 2560 ? 220.919 243.245 277.197 1.00 42.24  ? 2560 HIS A ND1   1 
ATOM   8016  C  CD2   . HIS A 1 2560 ? 219.600 242.155 275.840 1.00 43.00  ? 2560 HIS A CD2   1 
ATOM   8017  C  CE1   . HIS A 1 2560 ? 220.387 244.131 276.374 1.00 46.73  ? 2560 HIS A CE1   1 
ATOM   8018  N  NE2   . HIS A 1 2560 ? 219.584 243.496 275.540 1.00 52.00  ? 2560 HIS A NE2   1 
ATOM   8019  N  N     . LYS A 1 2561 ? 223.172 241.009 275.067 1.00 33.25  ? 2561 LYS A N     1 
ATOM   8020  C  CA    . LYS A 1 2561 ? 223.300 241.216 273.629 1.00 32.10  ? 2561 LYS A CA    1 
ATOM   8021  C  C     . LYS A 1 2561 ? 224.514 240.496 273.053 1.00 33.03  ? 2561 LYS A C     1 
ATOM   8022  O  O     . LYS A 1 2561 ? 225.105 240.951 272.071 1.00 37.19  ? 2561 LYS A O     1 
ATOM   8023  C  CB    . LYS A 1 2561 ? 223.370 242.709 273.313 1.00 36.68  ? 2561 LYS A CB    1 
ATOM   8024  C  CG    . LYS A 1 2561 ? 222.027 243.347 273.001 1.00 42.41  ? 2561 LYS A CG    1 
ATOM   8025  C  CD    . LYS A 1 2561 ? 222.196 244.565 272.106 1.00 51.00  ? 2561 LYS A CD    1 
ATOM   8026  C  CE    . LYS A 1 2561 ? 221.037 244.702 271.130 1.00 46.90  ? 2561 LYS A CE    1 
ATOM   8027  N  NZ    . LYS A 1 2561 ? 221.330 245.691 270.056 1.00 30.11  ? 2561 LYS A NZ    1 
ATOM   8028  N  N     . VAL A 1 2562 ? 224.891 239.368 273.645 1.00 31.75  ? 2562 VAL A N     1 
ATOM   8029  C  CA    . VAL A 1 2562 ? 226.078 238.635 273.219 1.00 28.33  ? 2562 VAL A CA    1 
ATOM   8030  C  C     . VAL A 1 2562 ? 225.772 237.912 271.913 1.00 33.61  ? 2562 VAL A C     1 
ATOM   8031  O  O     . VAL A 1 2562 ? 224.826 237.121 271.837 1.00 33.04  ? 2562 VAL A O     1 
ATOM   8032  C  CB    . VAL A 1 2562 ? 226.534 237.648 274.302 1.00 28.13  ? 2562 VAL A CB    1 
ATOM   8033  C  CG1   . VAL A 1 2562 ? 227.517 236.650 273.725 1.00 26.72  ? 2562 VAL A CG1   1 
ATOM   8034  C  CG2   . VAL A 1 2562 ? 227.160 238.391 275.462 1.00 25.85  ? 2562 VAL A CG2   1 
ATOM   8035  N  N     . ALA A 1 2563 ? 226.576 238.187 270.884 1.00 32.76  ? 2563 ALA A N     1 
ATOM   8036  C  CA    . ALA A 1 2563 ? 226.464 237.540 269.576 1.00 28.73  ? 2563 ALA A CA    1 
ATOM   8037  C  C     . ALA A 1 2563 ? 225.073 237.707 268.970 1.00 36.50  ? 2563 ALA A C     1 
ATOM   8038  O  O     . ALA A 1 2563 ? 224.577 236.814 268.279 1.00 35.32  ? 2563 ALA A O     1 
ATOM   8039  C  CB    . ALA A 1 2563 ? 226.839 236.058 269.654 1.00 22.01  ? 2563 ALA A CB    1 
ATOM   8040  N  N     . ALA A 1 2564 ? 224.438 238.847 269.222 1.00 39.68  ? 2564 ALA A N     1 
ATOM   8041  C  CA    . ALA A 1 2564 ? 223.141 239.123 268.630 1.00 37.21  ? 2564 ALA A CA    1 
ATOM   8042  C  C     . ALA A 1 2564 ? 223.297 239.389 267.132 1.00 39.45  ? 2564 ALA A C     1 
ATOM   8043  O  O     . ALA A 1 2564 ? 224.368 239.795 266.675 1.00 40.68  ? 2564 ALA A O     1 
ATOM   8044  C  CB    . ALA A 1 2564 ? 222.486 240.320 269.315 1.00 36.84  ? 2564 ALA A CB    1 
ATOM   8045  N  N     . PRO A 1 2565 ? 222.244 239.152 266.343 1.00 41.56  ? 2565 PRO A N     1 
ATOM   8046  C  CA    . PRO A 1 2565 ? 222.368 239.342 264.887 1.00 43.10  ? 2565 PRO A CA    1 
ATOM   8047  C  C     . PRO A 1 2565 ? 222.722 240.761 264.470 1.00 35.24  ? 2565 PRO A C     1 
ATOM   8048  O  O     . PRO A 1 2565 ? 223.415 240.939 263.460 1.00 37.24  ? 2565 PRO A O     1 
ATOM   8049  C  CB    . PRO A 1 2565 ? 220.986 238.926 264.361 1.00 40.82  ? 2565 PRO A CB    1 
ATOM   8050  C  CG    . PRO A 1 2565 ? 220.076 239.009 265.539 1.00 40.03  ? 2565 PRO A CG    1 
ATOM   8051  C  CD    . PRO A 1 2565 ? 220.916 238.639 266.718 1.00 44.92  ? 2565 PRO A CD    1 
ATOM   8052  N  N     . ASP A 1 2566 ? 222.309 241.770 265.237 1.00 37.35  ? 2566 ASP A N     1 
ATOM   8053  C  CA    . ASP A 1 2566 ? 222.557 243.168 264.779 1.00 37.83  ? 2566 ASP A CA    1 
ATOM   8054  C  C     . ASP A 1 2566 ? 223.631 243.834 265.649 1.00 31.53  ? 2566 ASP A C     1 
ATOM   8055  O  O     . ASP A 1 2566 ? 223.649 245.081 265.714 1.00 25.59  ? 2566 ASP A O     1 
ATOM   8056  C  CB    . ASP A 1 2566 ? 221.268 243.973 264.725 1.00 44.87  ? 2566 ASP A CB    1 
ATOM   8057  C  CG    . ASP A 1 2566 ? 220.239 243.474 263.722 1.00 47.08  ? 2566 ASP A CG    1 
ATOM   8058  O  OD1   . ASP A 1 2566 ? 220.564 243.446 262.518 1.00 41.33  ? 2566 ASP A OD1   1 
ATOM   8059  O  OD2   . ASP A 1 2566 ? 219.125 243.112 264.155 1.00 57.16  ? 2566 ASP A OD2   1 
ATOM   8060  N  N     . VAL A 1 2567 ? 224.496 243.033 266.280 1.00 34.96  ? 2567 VAL A N     1 
ATOM   8061  C  CA    . VAL A 1 2567 ? 225.587 243.592 267.135 1.00 32.02  ? 2567 VAL A CA    1 
ATOM   8062  C  C     . VAL A 1 2567 ? 226.919 243.438 266.386 1.00 22.73  ? 2567 VAL A C     1 
ATOM   8063  O  O     . VAL A 1 2567 ? 227.313 242.287 266.109 1.00 26.03  ? 2567 VAL A O     1 
ATOM   8064  C  CB    . VAL A 1 2567 ? 225.648 242.935 268.527 1.00 28.28  ? 2567 VAL A CB    1 
ATOM   8065  C  CG1   . VAL A 1 2567 ? 226.896 243.353 269.294 1.00 23.60  ? 2567 VAL A CG1   1 
ATOM   8066  C  CG2   . VAL A 1 2567 ? 224.395 243.223 269.343 1.00 27.40  ? 2567 VAL A CG2   1 
ATOM   8067  N  N     . VAL A 1 2568 ? 227.575 244.559 266.076 1.00 17.38  ? 2568 VAL A N     1 
ATOM   8068  C  CA    . VAL A 1 2568 ? 228.863 244.516 265.324 1.00 14.66  ? 2568 VAL A CA    1 
ATOM   8069  C  C     . VAL A 1 2568 ? 229.981 245.038 266.236 1.00 16.75  ? 2568 VAL A C     1 
ATOM   8070  O  O     . VAL A 1 2568 ? 229.805 246.126 266.821 1.00 20.76  ? 2568 VAL A O     1 
ATOM   8071  C  CB    . VAL A 1 2568 ? 228.787 245.338 264.023 1.00 14.15  ? 2568 VAL A CB    1 
ATOM   8072  C  CG1   . VAL A 1 2568 ? 230.073 245.234 263.213 1.00 11.69  ? 2568 VAL A CG1   1 
ATOM   8073  C  CG2   . VAL A 1 2568 ? 227.582 244.949 263.176 1.00 18.12  ? 2568 VAL A CG2   1 
ATOM   8074  N  N     . VAL A 1 2569 ? 231.077 244.287 266.356 1.00 13.69  ? 2569 VAL A N     1 
ATOM   8075  C  CA    . VAL A 1 2569 ? 232.242 244.771 267.153 1.00 11.38  ? 2569 VAL A CA    1 
ATOM   8076  C  C     . VAL A 1 2569 ? 233.071 245.667 266.223 1.00 16.31  ? 2569 VAL A C     1 
ATOM   8077  O  O     . VAL A 1 2569 ? 233.629 245.140 265.240 1.00 22.54  ? 2569 VAL A O     1 
ATOM   8078  C  CB    . VAL A 1 2569 ? 233.084 243.620 267.733 1.00 10.39  ? 2569 VAL A CB    1 
ATOM   8079  C  CG1   . VAL A 1 2569 ? 234.323 244.133 268.458 1.00 10.42  ? 2569 VAL A CG1   1 
ATOM   8080  C  CG2   . VAL A 1 2569 ? 232.258 242.720 268.644 1.00 13.29  ? 2569 VAL A CG2   1 
ATOM   8081  N  N     . PRO A 1 2570 ? 233.161 246.988 266.478 1.00 14.66  ? 2570 PRO A N     1 
ATOM   8082  C  CA    . PRO A 1 2570 ? 233.866 247.881 265.570 1.00 16.78  ? 2570 PRO A CA    1 
ATOM   8083  C  C     . PRO A 1 2570 ? 235.277 247.405 265.270 1.00 18.05  ? 2570 PRO A C     1 
ATOM   8084  O  O     . PRO A 1 2570 ? 236.042 247.153 266.219 1.00 22.63  ? 2570 PRO A O     1 
ATOM   8085  C  CB    . PRO A 1 2570 ? 233.849 249.227 266.319 1.00 22.82  ? 2570 PRO A CB    1 
ATOM   8086  C  CG    . PRO A 1 2570 ? 233.520 248.860 267.749 1.00 19.28  ? 2570 PRO A CG    1 
ATOM   8087  C  CD    . PRO A 1 2570 ? 232.602 247.658 267.635 1.00 17.69  ? 2570 PRO A CD    1 
ATOM   8088  N  N     . THR A 1 2571 ? 235.615 247.286 263.984 1.00 15.48  ? 2571 THR A N     1 
ATOM   8089  C  CA    . THR A 1 2571 ? 236.982 246.889 263.579 1.00 16.34  ? 2571 THR A CA    1 
ATOM   8090  C  C     . THR A 1 2571 ? 237.411 247.783 262.435 1.00 20.56  ? 2571 THR A C     1 
ATOM   8091  O  O     . THR A 1 2571 ? 236.542 248.491 261.885 1.00 23.06  ? 2571 THR A O     1 
ATOM   8092  C  CB    . THR A 1 2571 ? 237.017 245.410 263.194 1.00 15.97  ? 2571 THR A CB    1 
ATOM   8093  O  OG1   . THR A 1 2571 ? 236.072 245.268 262.138 1.00 21.60  ? 2571 THR A OG1   1 
ATOM   8094  C  CG2   . THR A 1 2571 ? 236.650 244.497 264.350 1.00 19.97  ? 2571 THR A CG2   1 
ATOM   8095  N  N     . LEU A 1 2572 ? 238.699 247.766 262.086 1.00 19.73  ? 2572 LEU A N     1 
ATOM   8096  C  CA    . LEU A 1 2572 ? 239.219 248.652 261.012 1.00 17.55  ? 2572 LEU A CA    1 
ATOM   8097  C  C     . LEU A 1 2572 ? 238.414 248.421 259.725 1.00 18.27  ? 2572 LEU A C     1 
ATOM   8098  O  O     . LEU A 1 2572 ? 237.953 249.416 259.127 1.00 21.75  ? 2572 LEU A O     1 
ATOM   8099  C  CB    . LEU A 1 2572 ? 240.704 248.370 260.797 1.00 19.98  ? 2572 LEU A CB    1 
ATOM   8100  C  CG    . LEU A 1 2572 ? 241.353 249.043 259.584 1.00 21.26  ? 2572 LEU A CG    1 
ATOM   8101  C  CD1   . LEU A 1 2572 ? 241.449 250.543 259.782 1.00 21.32  ? 2572 LEU A CD1   1 
ATOM   8102  C  CD2   . LEU A 1 2572 ? 242.724 248.447 259.327 1.00 25.68  ? 2572 LEU A CD2   1 
ATOM   8103  N  N     . ASP A 1 2573 ? 238.246 247.160 259.324 1.00 16.97  ? 2573 ASP A N     1 
ATOM   8104  C  CA    . ASP A 1 2573 ? 237.524 246.848 258.060 1.00 18.31  ? 2573 ASP A CA    1 
ATOM   8105  C  C     . ASP A 1 2573 ? 236.062 247.277 258.206 1.00 18.61  ? 2573 ASP A C     1 
ATOM   8106  O  O     . ASP A 1 2573 ? 235.497 247.801 257.223 1.00 20.87  ? 2573 ASP A O     1 
ATOM   8107  C  CB    . ASP A 1 2573 ? 237.701 245.387 257.680 1.00 17.95  ? 2573 ASP A CB    1 
ATOM   8108  C  CG    . ASP A 1 2573 ? 239.147 244.937 257.533 1.00 29.99  ? 2573 ASP A CG    1 
ATOM   8109  O  OD1   . ASP A 1 2573 ? 239.518 244.506 256.422 1.00 32.98  ? 2573 ASP A OD1   1 
ATOM   8110  O  OD2   . ASP A 1 2573 ? 239.893 245.028 258.532 1.00 29.36  ? 2573 ASP A OD2   1 
ATOM   8111  N  N     . THR A 1 2574 ? 235.484 247.078 259.393 1.00 16.77  ? 2574 THR A N     1 
ATOM   8112  C  CA    . THR A 1 2574 ? 234.082 247.468 259.636 1.00 13.36  ? 2574 THR A CA    1 
ATOM   8113  C  C     . THR A 1 2574 ? 233.932 248.958 259.426 1.00 14.86  ? 2574 THR A C     1 
ATOM   8114  O  O     . THR A 1 2574 ? 233.000 249.354 258.703 1.00 18.58  ? 2574 THR A O     1 
ATOM   8115  C  CB    . THR A 1 2574 ? 233.689 247.056 261.054 1.00 17.46  ? 2574 THR A CB    1 
ATOM   8116  O  OG1   . THR A 1 2574 ? 233.666 245.633 261.036 1.00 22.15  ? 2574 THR A OG1   1 
ATOM   8117  C  CG2   . THR A 1 2574 ? 232.327 247.586 261.462 1.00 18.86  ? 2574 THR A CG2   1 
ATOM   8118  N  N     . VAL A 1 2575 ? 234.824 249.763 260.009 1.00 15.52  ? 2575 VAL A N     1 
ATOM   8119  C  CA    . VAL A 1 2575 ? 234.685 251.249 259.923 1.00 12.46  ? 2575 VAL A CA    1 
ATOM   8120  C  C     . VAL A 1 2575 ? 235.041 251.720 258.502 1.00 13.09  ? 2575 VAL A C     1 
ATOM   8121  O  O     . VAL A 1 2575 ? 234.432 252.711 258.048 1.00 13.39  ? 2575 VAL A O     1 
ATOM   8122  C  CB    . VAL A 1 2575 ? 235.531 251.971 260.992 1.00 12.95  ? 2575 VAL A CB    1 
ATOM   8123  C  CG1   . VAL A 1 2575 ? 235.137 251.550 262.402 1.00 14.81  ? 2575 VAL A CG1   1 
ATOM   8124  C  CG2   . VAL A 1 2575 ? 237.026 251.775 260.770 1.00 14.39  ? 2575 VAL A CG2   1 
ATOM   8125  N  N     . ARG A 1 2576 ? 235.976 251.039 257.827 1.00 13.64  ? 2576 ARG A N     1 
ATOM   8126  C  CA    . ARG A 1 2576 ? 236.327 251.419 256.461 1.00 10.06  ? 2576 ARG A CA    1 
ATOM   8127  C  C     . ARG A 1 2576 ? 235.215 251.052 255.485 1.00 10.56  ? 2576 ARG A C     1 
ATOM   8128  O  O     . ARG A 1 2576 ? 234.782 251.883 254.673 1.00 14.27  ? 2576 ARG A O     1 
ATOM   8129  C  CB    . ARG A 1 2576 ? 237.638 250.749 256.048 1.00 13.50  ? 2576 ARG A CB    1 
ATOM   8130  C  CG    . ARG A 1 2576 ? 238.860 251.296 256.747 1.00 16.40  ? 2576 ARG A CG    1 
ATOM   8131  C  CD    . ARG A 1 2576 ? 240.136 250.687 256.196 1.00 17.84  ? 2576 ARG A CD    1 
ATOM   8132  N  NE    . ARG A 1 2576 ? 239.998 249.263 255.925 1.00 16.73  ? 2576 ARG A NE    1 
ATOM   8133  C  CZ    . ARG A 1 2576 ? 241.016 248.416 255.859 1.00 23.84  ? 2576 ARG A CZ    1 
ATOM   8134  N  NH1   . ARG A 1 2576 ? 242.262 248.817 256.041 1.00 13.42  ? 2576 ARG A NH1   1 
ATOM   8135  N  NH2   . ARG A 1 2576 ? 240.775 247.133 255.604 1.00 31.75  ? 2576 ARG A NH2   1 
ATOM   8136  N  N     . HIS A 1 2577 ? 234.736 249.807 255.554 1.00 11.21  ? 2577 HIS A N     1 
ATOM   8137  C  CA    . HIS A 1 2577 ? 233.673 249.374 254.660 1.00 9.73   ? 2577 HIS A CA    1 
ATOM   8138  C  C     . HIS A 1 2577 ? 232.373 250.108 254.941 1.00 9.51   ? 2577 HIS A C     1 
ATOM   8139  O  O     . HIS A 1 2577 ? 231.622 250.398 254.008 1.00 9.36   ? 2577 HIS A O     1 
ATOM   8140  C  CB    . HIS A 1 2577 ? 233.474 247.864 254.777 1.00 8.66   ? 2577 HIS A CB    1 
ATOM   8141  C  CG    . HIS A 1 2577 ? 234.662 247.065 254.342 1.00 7.90   ? 2577 HIS A CG    1 
ATOM   8142  N  ND1   . HIS A 1 2577 ? 234.765 245.708 254.554 1.00 12.71  ? 2577 HIS A ND1   1 
ATOM   8143  C  CD2   . HIS A 1 2577 ? 235.798 247.432 253.705 1.00 8.30   ? 2577 HIS A CD2   1 
ATOM   8144  C  CE1   . HIS A 1 2577 ? 235.913 245.273 254.066 1.00 13.34  ? 2577 HIS A CE1   1 
ATOM   8145  N  NE2   . HIS A 1 2577 ? 236.559 246.300 253.545 1.00 11.82  ? 2577 HIS A NE2   1 
ATOM   8146  N  N     . GLU A 1 2578 ? 232.094 250.426 256.207 1.00 11.18  ? 2578 GLU A N     1 
ATOM   8147  C  CA    . GLU A 1 2578 ? 230.896 251.192 256.527 1.00 9.34   ? 2578 GLU A CA    1 
ATOM   8148  C  C     . GLU A 1 2578 ? 230.942 252.569 255.883 1.00 11.64  ? 2578 GLU A C     1 
ATOM   8149  O  O     . GLU A 1 2578 ? 229.956 253.016 255.286 1.00 14.35  ? 2578 GLU A O     1 
ATOM   8150  C  CB    . GLU A 1 2578 ? 230.745 251.314 258.042 1.00 12.47  ? 2578 GLU A CB    1 
ATOM   8151  C  CG    . GLU A 1 2578 ? 230.085 250.119 258.708 1.00 16.90  ? 2578 GLU A CG    1 
ATOM   8152  C  CD    . GLU A 1 2578 ? 230.214 250.153 260.218 1.00 32.17  ? 2578 GLU A CD    1 
ATOM   8153  O  OE1   . GLU A 1 2578 ? 229.556 249.337 260.894 1.00 25.34  ? 2578 GLU A OE1   1 
ATOM   8154  O  OE2   . GLU A 1 2578 ? 230.976 250.999 260.732 1.00 31.43  ? 2578 GLU A OE2   1 
ATOM   8155  N  N     . ALA A 1 2579 ? 232.085 253.252 255.980 1.00 11.06  ? 2579 ALA A N     1 
ATOM   8156  C  CA    . ALA A 1 2579 ? 232.215 254.563 255.353 1.00 8.29   ? 2579 ALA A CA    1 
ATOM   8157  C  C     . ALA A 1 2579 ? 232.090 254.471 253.838 1.00 12.14  ? 2579 ALA A C     1 
ATOM   8158  O  O     . ALA A 1 2579 ? 231.408 255.294 253.214 1.00 16.64  ? 2579 ALA A O     1 
ATOM   8159  C  CB    . ALA A 1 2579 ? 233.546 255.201 255.741 1.00 7.00   ? 2579 ALA A CB    1 
ATOM   8160  N  N     . LEU A 1 2580 ? 232.740 253.476 253.228 1.00 11.04  ? 2580 LEU A N     1 
ATOM   8161  C  CA    . LEU A 1 2580 ? 232.669 253.335 251.777 1.00 9.89   ? 2580 LEU A CA    1 
ATOM   8162  C  C     . LEU A 1 2580 ? 231.245 253.045 251.314 1.00 12.15  ? 2580 LEU A C     1 
ATOM   8163  O  O     . LEU A 1 2580 ? 230.772 253.621 250.324 1.00 16.14  ? 2580 LEU A O     1 
ATOM   8164  C  CB    . LEU A 1 2580 ? 233.623 252.236 251.316 1.00 8.77   ? 2580 LEU A CB    1 
ATOM   8165  C  CG    . LEU A 1 2580 ? 233.805 252.065 249.810 1.00 8.62   ? 2580 LEU A CG    1 
ATOM   8166  C  CD1   . LEU A 1 2580 ? 234.476 253.286 249.209 1.00 9.75   ? 2580 LEU A CD1   1 
ATOM   8167  C  CD2   . LEU A 1 2580 ? 234.614 250.816 249.524 1.00 10.22  ? 2580 LEU A CD2   1 
ATOM   8168  N  N     . LEU A 1 2581 ? 230.544 252.155 252.020 1.00 10.76  ? 2581 LEU A N     1 
ATOM   8169  C  CA    . LEU A 1 2581 ? 229.170 251.836 251.653 1.00 9.12   ? 2581 LEU A CA    1 
ATOM   8170  C  C     . LEU A 1 2581 ? 228.251 253.026 251.867 1.00 12.00  ? 2581 LEU A C     1 
ATOM   8171  O  O     . LEU A 1 2581 ? 227.327 253.242 251.081 1.00 12.79  ? 2581 LEU A O     1 
ATOM   8172  C  CB    . LEU A 1 2581 ? 228.673 250.625 252.441 1.00 10.30  ? 2581 LEU A CB    1 
ATOM   8173  C  CG    . LEU A 1 2581 ? 229.336 249.282 252.130 1.00 8.87   ? 2581 LEU A CG    1 
ATOM   8174  C  CD1   . LEU A 1 2581 ? 228.717 248.176 252.965 1.00 7.76   ? 2581 LEU A CD1   1 
ATOM   8175  C  CD2   . LEU A 1 2581 ? 229.233 248.966 250.651 1.00 10.16  ? 2581 LEU A CD2   1 
ATOM   8176  N  N     . TYR A 1 2582 ? 228.475 253.809 252.926 1.00 13.25  ? 2582 TYR A N     1 
ATOM   8177  C  CA    . TYR A 1 2582 ? 227.680 255.017 253.117 1.00 11.37  ? 2582 TYR A CA    1 
ATOM   8178  C  C     . TYR A 1 2582 ? 227.903 255.992 251.969 1.00 12.87  ? 2582 TYR A C     1 
ATOM   8179  O  O     . TYR A 1 2582 ? 226.948 256.588 251.455 1.00 15.54  ? 2582 TYR A O     1 
ATOM   8180  C  CB    . TYR A 1 2582 ? 228.019 255.658 254.466 1.00 10.19  ? 2582 TYR A CB    1 
ATOM   8181  C  CG    . TYR A 1 2582 ? 227.182 256.866 254.848 1.00 16.99  ? 2582 TYR A CG    1 
ATOM   8182  C  CD1   . TYR A 1 2582 ? 226.302 256.807 255.918 1.00 22.04  ? 2582 TYR A CD1   1 
ATOM   8183  C  CD2   . TYR A 1 2582 ? 227.309 258.078 254.177 1.00 20.30  ? 2582 TYR A CD2   1 
ATOM   8184  C  CE1   . TYR A 1 2582 ? 225.543 257.899 256.282 1.00 22.95  ? 2582 TYR A CE1   1 
ATOM   8185  C  CE2   . TYR A 1 2582 ? 226.552 259.175 254.532 1.00 22.39  ? 2582 TYR A CE2   1 
ATOM   8186  C  CZ    . TYR A 1 2582 ? 225.673 259.082 255.587 1.00 26.98  ? 2582 TYR A CZ    1 
ATOM   8187  O  OH    . TYR A 1 2582 ? 224.923 260.178 255.948 1.00 43.61  ? 2582 TYR A OH    1 
ATOM   8188  N  N     . THR A 1 2583 ? 229.158 256.155 251.546 1.00 15.29  ? 2583 THR A N     1 
ATOM   8189  C  CA    . THR A 1 2583 ? 229.453 257.040 250.425 1.00 12.03  ? 2583 THR A CA    1 
ATOM   8190  C  C     . THR A 1 2583 ? 228.749 256.576 249.156 1.00 13.56  ? 2583 THR A C     1 
ATOM   8191  O  O     . THR A 1 2583 ? 228.147 257.384 248.439 1.00 18.84  ? 2583 THR A O     1 
ATOM   8192  C  CB    . THR A 1 2583 ? 230.964 257.114 250.202 1.00 14.26  ? 2583 THR A CB    1 
ATOM   8193  O  OG1   . THR A 1 2583 ? 231.561 257.927 251.220 1.00 25.76  ? 2583 THR A OG1   1 
ATOM   8194  C  CG2   . THR A 1 2583 ? 231.285 257.700 248.836 1.00 14.45  ? 2583 THR A CG2   1 
ATOM   8195  N  N     . TRP A 1 2584 ? 228.800 255.273 248.870 1.00 13.72  ? 2584 TRP A N     1 
ATOM   8196  C  CA    . TRP A 1 2584 ? 228.191 254.779 247.638 1.00 9.30   ? 2584 TRP A CA    1 
ATOM   8197  C  C     . TRP A 1 2584 ? 226.668 254.781 247.706 1.00 10.63  ? 2584 TRP A C     1 
ATOM   8198  O  O     . TRP A 1 2584 ? 226.006 255.007 246.687 1.00 14.55  ? 2584 TRP A O     1 
ATOM   8199  C  CB    . TRP A 1 2584 ? 228.708 253.379 247.319 1.00 8.85   ? 2584 TRP A CB    1 
ATOM   8200  C  CG    . TRP A 1 2584 ? 230.088 253.370 246.749 1.00 11.29  ? 2584 TRP A CG    1 
ATOM   8201  C  CD1   . TRP A 1 2584 ? 230.740 254.413 246.165 1.00 10.15  ? 2584 TRP A CD1   1 
ATOM   8202  C  CD2   . TRP A 1 2584 ? 230.990 252.259 246.708 1.00 13.36  ? 2584 TRP A CD2   1 
ATOM   8203  N  NE1   . TRP A 1 2584 ? 231.993 254.024 245.762 1.00 8.75   ? 2584 TRP A NE1   1 
ATOM   8204  C  CE2   . TRP A 1 2584 ? 232.171 252.705 246.084 1.00 10.07  ? 2584 TRP A CE2   1 
ATOM   8205  C  CE3   . TRP A 1 2584 ? 230.915 250.931 247.138 1.00 7.47   ? 2584 TRP A CE3   1 
ATOM   8206  C  CZ2   . TRP A 1 2584 ? 233.266 251.873 245.882 1.00 10.50  ? 2584 TRP A CZ2   1 
ATOM   8207  C  CZ3   . TRP A 1 2584 ? 232.000 250.106 246.934 1.00 8.09   ? 2584 TRP A CZ3   1 
ATOM   8208  C  CH2   . TRP A 1 2584 ? 233.161 250.579 246.310 1.00 11.83  ? 2584 TRP A CH2   1 
ATOM   8209  N  N     . LEU A 1 2585 ? 226.093 254.531 248.883 1.00 12.70  ? 2585 LEU A N     1 
ATOM   8210  C  CA    . LEU A 1 2585 ? 224.644 254.477 249.029 1.00 10.78  ? 2585 LEU A CA    1 
ATOM   8211  C  C     . LEU A 1 2585 ? 224.013 255.860 249.041 1.00 13.59  ? 2585 LEU A C     1 
ATOM   8212  O  O     . LEU A 1 2585 ? 222.899 256.028 248.536 1.00 17.26  ? 2585 LEU A O     1 
ATOM   8213  C  CB    . LEU A 1 2585 ? 224.275 253.728 250.312 1.00 9.42   ? 2585 LEU A CB    1 
ATOM   8214  C  CG    . LEU A 1 2585 ? 224.394 252.203 250.313 1.00 12.55  ? 2585 LEU A CG    1 
ATOM   8215  C  CD1   . LEU A 1 2585 ? 224.469 251.681 251.736 1.00 12.63  ? 2585 LEU A CD1   1 
ATOM   8216  C  CD2   . LEU A 1 2585 ? 223.223 251.576 249.582 1.00 12.85  ? 2585 LEU A CD2   1 
ATOM   8217  N  N     . ALA A 1 2586 ? 224.699 256.853 249.614 1.00 13.01  ? 2586 ALA A N     1 
ATOM   8218  C  CA    . ALA A 1 2586 ? 224.143 258.202 249.662 1.00 14.03  ? 2586 ALA A CA    1 
ATOM   8219  C  C     . ALA A 1 2586 ? 223.900 258.761 248.267 1.00 14.74  ? 2586 ALA A C     1 
ATOM   8220  O  O     . ALA A 1 2586 ? 222.995 259.580 248.075 1.00 15.87  ? 2586 ALA A O     1 
ATOM   8221  C  CB    . ALA A 1 2586 ? 225.072 259.123 250.452 1.00 18.79  ? 2586 ALA A CB    1 
ATOM   8222  N  N     . GLU A 1 2587 ? 224.689 258.332 247.285 1.00 13.06  ? 2587 GLU A N     1 
ATOM   8223  C  CA    . GLU A 1 2587 ? 224.490 258.717 245.896 1.00 15.35  ? 2587 GLU A CA    1 
ATOM   8224  C  C     . GLU A 1 2587 ? 223.488 257.827 245.176 1.00 13.88  ? 2587 GLU A C     1 
ATOM   8225  O  O     . GLU A 1 2587 ? 223.225 258.052 243.991 1.00 16.72  ? 2587 GLU A O     1 
ATOM   8226  C  CB    . GLU A 1 2587 ? 225.823 258.689 245.143 1.00 17.19  ? 2587 GLU A CB    1 
ATOM   8227  C  CG    . GLU A 1 2587 ? 226.896 259.583 245.734 1.00 24.64  ? 2587 GLU A CG    1 
ATOM   8228  C  CD    . GLU A 1 2587 ? 226.504 261.046 245.727 1.00 37.22  ? 2587 GLU A CD    1 
ATOM   8229  O  OE1   . GLU A 1 2587 ? 226.013 261.527 244.684 1.00 32.77  ? 2587 GLU A OE1   1 
ATOM   8230  O  OE2   . GLU A 1 2587 ? 226.690 261.715 246.763 1.00 30.26  ? 2587 GLU A OE2   1 
ATOM   8231  N  N     . HIS A 1 2588 ? 222.938 256.822 245.860 1.00 11.49  ? 2588 HIS A N     1 
ATOM   8232  C  CA    . HIS A 1 2588 ? 222.027 255.835 245.282 1.00 10.12  ? 2588 HIS A CA    1 
ATOM   8233  C  C     . HIS A 1 2588 ? 222.681 255.038 244.160 1.00 10.24  ? 2588 HIS A C     1 
ATOM   8234  O  O     . HIS A 1 2588 ? 221.989 254.455 243.321 1.00 9.55   ? 2588 HIS A O     1 
ATOM   8235  C  CB    . HIS A 1 2588 ? 220.732 256.489 244.788 1.00 10.47  ? 2588 HIS A CB    1 
ATOM   8236  C  CG    . HIS A 1 2588 ? 220.154 257.481 245.749 1.00 10.26  ? 2588 HIS A CG    1 
ATOM   8237  N  ND1   . HIS A 1 2588 ? 219.917 257.182 247.072 1.00 11.01  ? 2588 HIS A ND1   1 
ATOM   8238  C  CD2   . HIS A 1 2588 ? 219.771 258.768 245.579 1.00 11.80  ? 2588 HIS A CD2   1 
ATOM   8239  C  CE1   . HIS A 1 2588 ? 219.408 258.241 247.676 1.00 11.88  ? 2588 HIS A CE1   1 
ATOM   8240  N  NE2   . HIS A 1 2588 ? 219.309 259.216 246.792 1.00 12.62  ? 2588 HIS A NE2   1 
ATOM   8241  N  N     . LYS A 1 2589 ? 224.005 255.003 244.139 1.00 11.86  ? 2589 LYS A N     1 
ATOM   8242  C  CA    . LYS A 1 2589 ? 224.736 254.241 243.137 1.00 8.99   ? 2589 LYS A CA    1 
ATOM   8243  C  C     . LYS A 1 2589 ? 224.712 252.761 243.498 1.00 7.77   ? 2589 LYS A C     1 
ATOM   8244  O  O     . LYS A 1 2589 ? 225.078 252.399 244.621 1.00 9.55   ? 2589 LYS A O     1 
ATOM   8245  C  CB    . LYS A 1 2589 ? 226.176 254.738 243.044 1.00 8.68   ? 2589 LYS A CB    1 
ATOM   8246  C  CG    . LYS A 1 2589 ? 227.077 253.915 242.143 1.00 10.94  ? 2589 LYS A CG    1 
ATOM   8247  C  CD    . LYS A 1 2589 ? 227.414 254.663 240.867 1.00 8.84   ? 2589 LYS A CD    1 
ATOM   8248  C  CE    . LYS A 1 2589 ? 228.678 254.114 240.228 1.00 11.04  ? 2589 LYS A CE    1 
ATOM   8249  N  NZ    . LYS A 1 2589 ? 228.868 254.619 238.841 1.00 15.29  ? 2589 LYS A NZ    1 
ATOM   8250  N  N     . PRO A 1 2590 ? 224.278 251.884 242.593 1.00 7.15   ? 2590 PRO A N     1 
ATOM   8251  C  CA    . PRO A 1 2590 ? 224.264 250.452 242.908 1.00 6.56   ? 2590 PRO A CA    1 
ATOM   8252  C  C     . PRO A 1 2590 ? 225.668 249.935 243.180 1.00 9.52   ? 2590 PRO A C     1 
ATOM   8253  O  O     . PRO A 1 2590 ? 226.633 250.341 242.534 1.00 10.84  ? 2590 PRO A O     1 
ATOM   8254  C  CB    . PRO A 1 2590 ? 223.659 249.819 241.651 1.00 5.80   ? 2590 PRO A CB    1 
ATOM   8255  C  CG    . PRO A 1 2590 ? 223.924 250.806 240.566 1.00 7.41   ? 2590 PRO A CG    1 
ATOM   8256  C  CD    . PRO A 1 2590 ? 223.834 252.154 241.215 1.00 9.13   ? 2590 PRO A CD    1 
ATOM   8257  N  N     . LEU A 1 2591 ? 225.772 249.025 244.145 1.00 7.36   ? 2591 LEU A N     1 
ATOM   8258  C  CA    . LEU A 1 2591 ? 227.060 248.503 244.577 1.00 5.23   ? 2591 LEU A CA    1 
ATOM   8259  C  C     . LEU A 1 2591 ? 226.945 247.002 244.785 1.00 6.89   ? 2591 LEU A C     1 
ATOM   8260  O  O     . LEU A 1 2591 ? 225.854 246.463 244.982 1.00 9.10   ? 2591 LEU A O     1 
ATOM   8261  C  CB    . LEU A 1 2591 ? 227.547 249.203 245.857 1.00 8.66   ? 2591 LEU A CB    1 
ATOM   8262  C  CG    . LEU A 1 2591 ? 226.723 249.109 247.148 1.00 5.70   ? 2591 LEU A CG    1 
ATOM   8263  C  CD1   . LEU A 1 2591 ? 227.026 247.844 247.937 1.00 6.82   ? 2591 LEU A CD1   1 
ATOM   8264  C  CD2   . LEU A 1 2591 ? 226.928 250.336 248.015 1.00 5.97   ? 2591 LEU A CD2   1 
ATOM   8265  N  N     . VAL A 1 2592 ? 228.093 246.329 244.732 1.00 7.12   ? 2592 VAL A N     1 
ATOM   8266  C  CA    . VAL A 1 2592 ? 228.174 244.886 244.918 1.00 5.14   ? 2592 VAL A CA    1 
ATOM   8267  C  C     . VAL A 1 2592 ? 229.251 244.590 245.953 1.00 5.88   ? 2592 VAL A C     1 
ATOM   8268  O  O     . VAL A 1 2592 ? 230.369 245.108 245.859 1.00 6.52   ? 2592 VAL A O     1 
ATOM   8269  C  CB    . VAL A 1 2592 ? 228.474 244.155 243.594 1.00 4.22   ? 2592 VAL A CB    1 
ATOM   8270  C  CG1   . VAL A 1 2592 ? 228.864 242.713 243.854 1.00 5.33   ? 2592 VAL A CG1   1 
ATOM   8271  C  CG2   . VAL A 1 2592 ? 227.271 244.221 242.672 1.00 5.33   ? 2592 VAL A CG2   1 
ATOM   8272  N  N     . LEU A 1 2593 ? 228.906 243.765 246.938 1.00 6.30   ? 2593 LEU A N     1 
ATOM   8273  C  CA    . LEU A 1 2593 ? 229.848 243.269 247.931 1.00 4.47   ? 2593 LEU A CA    1 
ATOM   8274  C  C     . LEU A 1 2593 ? 230.225 241.838 247.575 1.00 5.14   ? 2593 LEU A C     1 
ATOM   8275  O  O     . LEU A 1 2593 ? 229.363 240.953 247.546 1.00 6.10   ? 2593 LEU A O     1 
ATOM   8276  C  CB    . LEU A 1 2593 ? 229.251 243.328 249.337 1.00 5.31   ? 2593 LEU A CB    1 
ATOM   8277  C  CG    . LEU A 1 2593 ? 228.784 244.682 249.866 1.00 6.02   ? 2593 LEU A CG    1 
ATOM   8278  C  CD1   . LEU A 1 2593 ? 227.269 244.762 249.846 1.00 5.55   ? 2593 LEU A CD1   1 
ATOM   8279  C  CD2   . LEU A 1 2593 ? 229.315 244.917 251.264 1.00 5.37   ? 2593 LEU A CD2   1 
ATOM   8280  N  N     . CYS A 1 2594 ? 231.508 241.612 247.318 1.00 6.66   ? 2594 CYS A N     1 
ATOM   8281  C  CA    . CYS A 1 2594 ? 232.016 240.293 246.981 1.00 5.18   ? 2594 CYS A CA    1 
ATOM   8282  C  C     . CYS A 1 2594 ? 232.921 239.786 248.095 1.00 6.29   ? 2594 CYS A C     1 
ATOM   8283  O  O     . CYS A 1 2594 ? 233.692 240.546 248.688 1.00 9.25   ? 2594 CYS A O     1 
ATOM   8284  C  CB    . CYS A 1 2594 ? 232.783 240.318 245.658 1.00 5.73   ? 2594 CYS A CB    1 
ATOM   8285  S  SG    . CYS A 1 2594 ? 232.853 238.725 244.815 1.00 15.98  ? 2594 CYS A SG    1 
ATOM   8286  N  N     . GLY A 1 2595 ? 232.804 238.494 248.401 1.00 5.42   ? 2595 GLY A N     1 
ATOM   8287  C  CA    . GLY A 1 2595 ? 233.661 237.909 249.446 1.00 5.21   ? 2595 GLY A CA    1 
ATOM   8288  C  C     . GLY A 1 2595 ? 233.215 236.514 249.818 1.00 6.10   ? 2595 GLY A C     1 
ATOM   8289  O  O     . GLY A 1 2595 ? 232.130 236.093 249.369 1.00 7.78   ? 2595 GLY A O     1 
ATOM   8290  N  N     . PRO A 1 2596 ? 234.000 235.781 250.636 1.00 6.82   ? 2596 PRO A N     1 
ATOM   8291  C  CA    . PRO A 1 2596 ? 233.659 234.416 250.999 1.00 6.23   ? 2596 PRO A CA    1 
ATOM   8292  C  C     . PRO A 1 2596 ? 232.394 234.398 251.843 1.00 6.66   ? 2596 PRO A C     1 
ATOM   8293  O  O     . PRO A 1 2596 ? 232.098 235.392 252.531 1.00 7.92   ? 2596 PRO A O     1 
ATOM   8294  C  CB    . PRO A 1 2596 ? 234.891 233.942 251.781 1.00 5.71   ? 2596 PRO A CB    1 
ATOM   8295  C  CG    . PRO A 1 2596 ? 235.970 234.945 251.444 1.00 6.57   ? 2596 PRO A CG    1 
ATOM   8296  C  CD    . PRO A 1 2596 ? 235.231 236.250 251.239 1.00 6.90   ? 2596 PRO A CD    1 
ATOM   8297  N  N     . PRO A 1 2597 ? 231.571 233.320 251.817 1.00 7.97   ? 2597 PRO A N     1 
ATOM   8298  C  CA    . PRO A 1 2597 ? 230.311 233.331 252.548 1.00 8.26   ? 2597 PRO A CA    1 
ATOM   8299  C  C     . PRO A 1 2597 ? 230.538 233.505 254.039 1.00 7.28   ? 2597 PRO A C     1 
ATOM   8300  O  O     . PRO A 1 2597 ? 231.381 232.795 254.611 1.00 12.58  ? 2597 PRO A O     1 
ATOM   8301  C  CB    . PRO A 1 2597 ? 229.675 231.973 252.215 1.00 6.40   ? 2597 PRO A CB    1 
ATOM   8302  C  CG    . PRO A 1 2597 ? 230.842 231.106 251.813 1.00 4.98   ? 2597 PRO A CG    1 
ATOM   8303  C  CD    . PRO A 1 2597 ? 231.787 232.054 251.105 1.00 6.84   ? 2597 PRO A CD    1 
ATOM   8304  N  N     . GLY A 1 2598 ? 229.792 234.422 254.658 1.00 5.93   ? 2598 GLY A N     1 
ATOM   8305  C  CA    . GLY A 1 2598 ? 229.931 234.661 256.107 1.00 6.78   ? 2598 GLY A CA    1 
ATOM   8306  C  C     . GLY A 1 2598 ? 231.032 235.661 256.384 1.00 9.00   ? 2598 GLY A C     1 
ATOM   8307  O  O     . GLY A 1 2598 ? 231.435 235.789 257.556 1.00 12.58  ? 2598 GLY A O     1 
ATOM   8308  N  N     . SER A 1 2599 ? 231.505 236.348 255.342 1.00 8.13   ? 2599 SER A N     1 
ATOM   8309  C  CA    . SER A 1 2599 ? 232.591 237.353 255.509 1.00 6.41   ? 2599 SER A CA    1 
ATOM   8310  C  C     . SER A 1 2599 ? 232.063 238.591 256.252 1.00 7.95   ? 2599 SER A C     1 
ATOM   8311  O  O     . SER A 1 2599 ? 232.885 239.300 256.867 1.00 7.50   ? 2599 SER A O     1 
ATOM   8312  C  CB    . SER A 1 2599 ? 233.199 237.728 254.185 1.00 5.60   ? 2599 SER A CB    1 
ATOM   8313  O  OG    . SER A 1 2599 ? 232.215 238.254 253.305 1.00 6.93   ? 2599 SER A OG    1 
ATOM   8314  N  N     . GLY A 1 2600 ? 230.752 238.837 256.192 1.00 8.44   ? 2600 GLY A N     1 
ATOM   8315  C  CA    . GLY A 1 2600 ? 230.154 239.981 256.906 1.00 6.51   ? 2600 GLY A CA    1 
ATOM   8316  C  C     . GLY A 1 2600 ? 229.586 241.012 255.952 1.00 6.28   ? 2600 GLY A C     1 
ATOM   8317  O  O     . GLY A 1 2600 ? 229.362 242.157 256.390 1.00 8.28   ? 2600 GLY A O     1 
ATOM   8318  N  N     . LYS A 1 2601 ? 229.358 240.627 254.695 1.00 6.65   ? 2601 LYS A N     1 
ATOM   8319  C  CA    . LYS A 1 2601 ? 228.834 241.573 253.676 1.00 5.50   ? 2601 LYS A CA    1 
ATOM   8320  C  C     . LYS A 1 2601 ? 227.455 242.082 254.120 1.00 6.53   ? 2601 LYS A C     1 
ATOM   8321  O  O     . LYS A 1 2601 ? 227.266 243.316 254.153 1.00 10.49  ? 2601 LYS A O     1 
ATOM   8322  C  CB    . LYS A 1 2601 ? 228.783 240.876 252.312 1.00 4.41   ? 2601 LYS A CB    1 
ATOM   8323  C  CG    . LYS A 1 2601 ? 230.129 240.372 251.807 1.00 4.21   ? 2601 LYS A CG    1 
ATOM   8324  C  CD    . LYS A 1 2601 ? 230.049 239.610 250.490 1.00 4.64   ? 2601 LYS A CD    1 
ATOM   8325  C  CE    . LYS A 1 2601 ? 229.306 238.317 250.614 1.00 5.42   ? 2601 LYS A CE    1 
ATOM   8326  N  NZ    . LYS A 1 2601 ? 229.993 237.388 251.515 1.00 5.99   ? 2601 LYS A NZ    1 
ATOM   8327  N  N     . THR A 1 2602 ? 226.544 241.170 254.469 1.00 7.28   ? 2602 THR A N     1 
ATOM   8328  C  CA    . THR A 1 2602 ? 225.186 241.560 254.912 1.00 5.81   ? 2602 THR A CA    1 
ATOM   8329  C  C     . THR A 1 2602 ? 225.293 242.371 256.184 1.00 7.45   ? 2602 THR A C     1 
ATOM   8330  O  O     . THR A 1 2602 ? 224.581 243.394 256.294 1.00 9.14   ? 2602 THR A O     1 
ATOM   8331  C  CB    . THR A 1 2602 ? 224.335 240.307 255.105 1.00 4.84   ? 2602 THR A CB    1 
ATOM   8332  O  OG1   . THR A 1 2602 ? 224.373 239.632 253.852 1.00 12.17  ? 2602 THR A OG1   1 
ATOM   8333  C  CG2   . THR A 1 2602 ? 222.901 240.628 255.480 1.00 6.81   ? 2602 THR A CG2   1 
ATOM   8334  N  N     . MET A 1 2603 ? 226.153 241.945 257.112 1.00 7.20   ? 2603 MET A N     1 
ATOM   8335  C  CA    . MET A 1 2603 ? 226.325 242.659 258.403 1.00 5.27   ? 2603 MET A CA    1 
ATOM   8336  C  C     . MET A 1 2603 ? 226.833 244.083 258.137 1.00 5.99   ? 2603 MET A C     1 
ATOM   8337  O  O     . MET A 1 2603 ? 226.291 245.028 258.747 1.00 10.29  ? 2603 MET A O     1 
ATOM   8338  C  CB    . MET A 1 2603 ? 227.337 241.930 259.292 1.00 6.10   ? 2603 MET A CB    1 
ATOM   8339  C  CG    . MET A 1 2603 ? 227.681 242.673 260.564 1.00 11.34  ? 2603 MET A CG    1 
ATOM   8340  S  SD    . MET A 1 2603 ? 229.210 242.075 261.312 1.00 9.00   ? 2603 MET A SD    1 
ATOM   8341  C  CE    . MET A 1 2603 ? 230.377 242.420 259.990 1.00 6.38   ? 2603 MET A CE    1 
ATOM   8342  N  N     . THR A 1 2604 ? 227.831 244.222 257.263 1.00 6.33   ? 2604 THR A N     1 
ATOM   8343  C  CA    . THR A 1 2604 ? 228.393 245.553 256.951 1.00 6.37   ? 2604 THR A CA    1 
ATOM   8344  C  C     . THR A 1 2604 ? 227.323 246.391 256.289 1.00 7.33   ? 2604 THR A C     1 
ATOM   8345  O  O     . THR A 1 2604 ? 227.198 247.580 256.650 1.00 8.95   ? 2604 THR A O     1 
ATOM   8346  C  CB    . THR A 1 2604 ? 229.628 245.401 256.065 1.00 5.41   ? 2604 THR A CB    1 
ATOM   8347  O  OG1   . THR A 1 2604 ? 230.493 244.531 256.789 1.00 6.31   ? 2604 THR A OG1   1 
ATOM   8348  C  CG2   . THR A 1 2604 ? 230.321 246.725 255.801 1.00 5.82   ? 2604 THR A CG2   1 
ATOM   8349  N  N     . LEU A 1 2605 ? 226.570 245.805 255.354 1.00 6.92   ? 2605 LEU A N     1 
ATOM   8350  C  CA    . LEU A 1 2605 ? 225.575 246.594 254.639 1.00 6.77   ? 2605 LEU A CA    1 
ATOM   8351  C  C     . LEU A 1 2605 ? 224.478 247.080 255.578 1.00 9.64   ? 2605 LEU A C     1 
ATOM   8352  O  O     . LEU A 1 2605 ? 224.052 248.238 255.496 1.00 11.80  ? 2605 LEU A O     1 
ATOM   8353  C  CB    . LEU A 1 2605 ? 224.975 245.783 253.493 1.00 7.05   ? 2605 LEU A CB    1 
ATOM   8354  C  CG    . LEU A 1 2605 ? 223.814 246.473 252.777 1.00 6.47   ? 2605 LEU A CG    1 
ATOM   8355  C  CD1   . LEU A 1 2605 ? 224.335 247.517 251.803 1.00 8.41   ? 2605 LEU A CD1   1 
ATOM   8356  C  CD2   . LEU A 1 2605 ? 222.938 245.462 252.066 1.00 6.48   ? 2605 LEU A CD2   1 
ATOM   8357  N  N     . PHE A 1 2606 ? 224.006 246.212 256.476 1.00 10.20  ? 2606 PHE A N     1 
ATOM   8358  C  CA    . PHE A 1 2606 ? 222.986 246.631 257.433 1.00 8.89   ? 2606 PHE A CA    1 
ATOM   8359  C  C     . PHE A 1 2606 ? 223.532 247.669 258.406 1.00 9.69   ? 2606 PHE A C     1 
ATOM   8360  O  O     . PHE A 1 2606 ? 222.829 248.622 258.765 1.00 11.89  ? 2606 PHE A O     1 
ATOM   8361  C  CB    . PHE A 1 2606 ? 222.434 245.419 258.184 1.00 10.15  ? 2606 PHE A CB    1 
ATOM   8362  C  CG    . PHE A 1 2606 ? 221.562 244.529 257.343 1.00 11.57  ? 2606 PHE A CG    1 
ATOM   8363  C  CD1   . PHE A 1 2606 ? 221.085 243.331 257.847 1.00 17.55  ? 2606 PHE A CD1   1 
ATOM   8364  C  CD2   . PHE A 1 2606 ? 221.208 244.893 256.055 1.00 10.58  ? 2606 PHE A CD2   1 
ATOM   8365  C  CE1   . PHE A 1 2606 ? 220.280 242.512 257.079 1.00 21.01  ? 2606 PHE A CE1   1 
ATOM   8366  C  CE2   . PHE A 1 2606 ? 220.405 244.078 255.284 1.00 10.01  ? 2606 PHE A CE2   1 
ATOM   8367  C  CZ    . PHE A 1 2606 ? 219.940 242.888 255.795 1.00 16.90  ? 2606 PHE A CZ    1 
ATOM   8368  N  N     . SER A 1 2607 ? 224.786 247.508 258.836 1.00 8.98   ? 2607 SER A N     1 
ATOM   8369  C  CA    . SER A 1 2607 ? 225.397 248.496 259.718 1.00 9.09   ? 2607 SER A CA    1 
ATOM   8370  C  C     . SER A 1 2607 ? 225.501 249.854 259.036 1.00 14.46  ? 2607 SER A C     1 
ATOM   8371  O  O     . SER A 1 2607 ? 225.248 250.892 259.659 1.00 15.63  ? 2607 SER A O     1 
ATOM   8372  C  CB    . SER A 1 2607 ? 226.773 248.008 260.166 1.00 10.33  ? 2607 SER A CB    1 
ATOM   8373  O  OG    . SER A 1 2607 ? 227.349 248.892 261.110 1.00 18.58  ? 2607 SER A OG    1 
ATOM   8374  N  N     . ALA A 1 2608 ? 225.880 249.867 257.756 1.00 13.79  ? 2608 ALA A N     1 
ATOM   8375  C  CA    . ALA A 1 2608 ? 225.952 251.121 257.016 1.00 10.05  ? 2608 ALA A CA    1 
ATOM   8376  C  C     . ALA A 1 2608 ? 224.569 251.727 256.810 1.00 10.02  ? 2608 ALA A C     1 
ATOM   8377  O  O     . ALA A 1 2608 ? 224.395 252.945 256.924 1.00 13.68  ? 2608 ALA A O     1 
ATOM   8378  C  CB    . ALA A 1 2608 ? 226.648 250.900 255.674 1.00 11.36  ? 2608 ALA A CB    1 
ATOM   8379  N  N     . LEU A 1 2609 ? 223.572 250.893 256.505 1.00 9.13   ? 2609 LEU A N     1 
ATOM   8380  C  CA    . LEU A 1 2609 ? 222.219 251.390 256.288 1.00 12.20  ? 2609 LEU A CA    1 
ATOM   8381  C  C     . LEU A 1 2609 ? 221.580 251.900 257.570 1.00 14.98  ? 2609 LEU A C     1 
ATOM   8382  O  O     . LEU A 1 2609 ? 220.650 252.709 257.502 1.00 19.55  ? 2609 LEU A O     1 
ATOM   8383  C  CB    . LEU A 1 2609 ? 221.350 250.293 255.673 1.00 11.67  ? 2609 LEU A CB    1 
ATOM   8384  C  CG    . LEU A 1 2609 ? 221.443 250.146 254.154 1.00 9.65   ? 2609 LEU A CG    1 
ATOM   8385  C  CD1   . LEU A 1 2609 ? 220.611 248.968 253.677 1.00 9.69   ? 2609 LEU A CD1   1 
ATOM   8386  C  CD2   . LEU A 1 2609 ? 221.009 251.427 253.466 1.00 11.47  ? 2609 LEU A CD2   1 
ATOM   8387  N  N     . ARG A 1 2610 ? 222.048 251.438 258.730 1.00 16.79  ? 2610 ARG A N     1 
ATOM   8388  C  CA    . ARG A 1 2610 ? 221.560 251.988 259.990 1.00 17.04  ? 2610 ARG A CA    1 
ATOM   8389  C  C     . ARG A 1 2610 ? 221.872 253.474 260.109 1.00 19.69  ? 2610 ARG A C     1 
ATOM   8390  O  O     . ARG A 1 2610 ? 221.152 254.207 260.796 1.00 25.05  ? 2610 ARG A O     1 
ATOM   8391  C  CB    . ARG A 1 2610 ? 222.166 251.221 261.165 1.00 17.83  ? 2610 ARG A CB    1 
ATOM   8392  C  CG    . ARG A 1 2610 ? 221.344 250.026 261.612 1.00 19.19  ? 2610 ARG A CG    1 
ATOM   8393  C  CD    . ARG A 1 2610 ? 221.822 249.501 262.960 1.00 22.42  ? 2610 ARG A CD    1 
ATOM   8394  N  NE    . ARG A 1 2610 ? 222.730 248.364 262.844 1.00 24.29  ? 2610 ARG A NE    1 
ATOM   8395  C  CZ    . ARG A 1 2610 ? 222.438 247.204 262.267 1.00 22.70  ? 2610 ARG A CZ    1 
ATOM   8396  N  NH1   . ARG A 1 2610 ? 221.232 246.952 261.783 1.00 17.63  ? 2610 ARG A NH1   1 
ATOM   8397  N  NH2   . ARG A 1 2610 ? 223.376 246.266 262.190 1.00 21.26  ? 2610 ARG A NH2   1 
ATOM   8398  N  N     . ALA A 1 2611 ? 222.932 253.936 259.446 1.00 20.64  ? 2611 ALA A N     1 
ATOM   8399  C  CA    . ALA A 1 2611 ? 223.275 255.351 259.427 1.00 21.74  ? 2611 ALA A CA    1 
ATOM   8400  C  C     . ALA A 1 2611 ? 222.460 256.143 258.414 1.00 24.04  ? 2611 ALA A C     1 
ATOM   8401  O  O     . ALA A 1 2611 ? 222.592 257.371 258.361 1.00 27.56  ? 2611 ALA A O     1 
ATOM   8402  C  CB    . ALA A 1 2611 ? 224.767 255.527 259.135 1.00 21.32  ? 2611 ALA A CB    1 
ATOM   8403  N  N     . LEU A 1 2612 ? 221.636 255.478 257.611 1.00 20.73  ? 2612 LEU A N     1 
ATOM   8404  C  CA    . LEU A 1 2612 ? 220.761 256.140 256.645 1.00 24.50  ? 2612 LEU A CA    1 
ATOM   8405  C  C     . LEU A 1 2612 ? 219.317 255.813 256.998 1.00 34.05  ? 2612 LEU A C     1 
ATOM   8406  O  O     . LEU A 1 2612 ? 218.798 254.759 256.588 1.00 36.12  ? 2612 LEU A O     1 
ATOM   8407  C  CB    . LEU A 1 2612 ? 221.085 255.694 255.221 1.00 23.71  ? 2612 LEU A CB    1 
ATOM   8408  C  CG    . LEU A 1 2612 ? 222.431 256.158 254.658 1.00 23.62  ? 2612 LEU A CG    1 
ATOM   8409  C  CD1   . LEU A 1 2612 ? 222.902 255.234 253.551 1.00 14.16  ? 2612 LEU A CD1   1 
ATOM   8410  C  CD2   . LEU A 1 2612 ? 222.332 257.588 254.155 1.00 21.67  ? 2612 LEU A CD2   1 
ATOM   8411  N  N     . PRO A 1 2613 ? 218.629 256.673 257.754 1.00 36.32  ? 2613 PRO A N     1 
ATOM   8412  C  CA    . PRO A 1 2613 ? 217.266 256.343 258.198 1.00 38.85  ? 2613 PRO A CA    1 
ATOM   8413  C  C     . PRO A 1 2613 ? 216.211 256.461 257.114 1.00 33.50  ? 2613 PRO A C     1 
ATOM   8414  O  O     . PRO A 1 2613 ? 215.087 255.983 257.319 1.00 30.88  ? 2613 PRO A O     1 
ATOM   8415  C  CB    . PRO A 1 2613 ? 217.000 257.356 259.325 1.00 38.92  ? 2613 PRO A CB    1 
ATOM   8416  C  CG    . PRO A 1 2613 ? 218.071 258.389 259.232 1.00 32.01  ? 2613 PRO A CG    1 
ATOM   8417  C  CD    . PRO A 1 2613 ? 219.080 257.999 258.205 1.00 25.15  ? 2613 PRO A CD    1 
ATOM   8418  N  N     . ASP A 1 2614 ? 216.528 257.071 255.976 1.00 34.89  ? 2614 ASP A N     1 
ATOM   8419  C  CA    . ASP A 1 2614 ? 215.568 257.273 254.900 1.00 35.40  ? 2614 ASP A CA    1 
ATOM   8420  C  C     . ASP A 1 2614 ? 215.535 256.116 253.911 1.00 33.04  ? 2614 ASP A C     1 
ATOM   8421  O  O     . ASP A 1 2614 ? 214.836 256.206 252.897 1.00 29.80  ? 2614 ASP A O     1 
ATOM   8422  C  CB    . ASP A 1 2614 ? 215.875 258.578 254.161 1.00 37.50  ? 2614 ASP A CB    1 
ATOM   8423  C  CG    . ASP A 1 2614 ? 215.416 259.802 254.926 1.00 49.70  ? 2614 ASP A CG    1 
ATOM   8424  O  OD1   . ASP A 1 2614 ? 214.602 259.647 255.862 1.00 50.13  ? 2614 ASP A OD1   1 
ATOM   8425  O  OD2   . ASP A 1 2614 ? 215.864 260.917 254.591 1.00 46.18  ? 2614 ASP A OD2   1 
ATOM   8426  N  N     . MET A 1 2615 ? 216.270 255.040 254.175 1.00 31.15  ? 2615 MET A N     1 
ATOM   8427  C  CA    . MET A 1 2615 ? 216.343 253.896 253.278 1.00 23.86  ? 2615 MET A CA    1 
ATOM   8428  C  C     . MET A 1 2615 ? 215.764 252.667 253.964 1.00 28.54  ? 2615 MET A C     1 
ATOM   8429  O  O     . MET A 1 2615 ? 216.106 252.372 255.113 1.00 34.85  ? 2615 MET A O     1 
ATOM   8430  C  CB    . MET A 1 2615 ? 217.786 253.633 252.843 1.00 18.28  ? 2615 MET A CB    1 
ATOM   8431  C  CG    . MET A 1 2615 ? 218.361 254.726 251.964 1.00 23.15  ? 2615 MET A CG    1 
ATOM   8432  S  SD    . MET A 1 2615 ? 220.060 254.423 251.459 1.00 28.67  ? 2615 MET A SD    1 
ATOM   8433  C  CE    . MET A 1 2615 ? 220.399 255.928 250.553 1.00 15.92  ? 2615 MET A CE    1 
ATOM   8434  N  N     . GLU A 1 2616 ? 214.889 251.959 253.256 1.00 23.71  ? 2616 GLU A N     1 
ATOM   8435  C  CA    . GLU A 1 2616 ? 214.310 250.708 253.725 1.00 24.88  ? 2616 GLU A CA    1 
ATOM   8436  C  C     . GLU A 1 2616 ? 214.826 249.571 252.855 1.00 19.44  ? 2616 GLU A C     1 
ATOM   8437  O  O     . GLU A 1 2616 ? 214.713 249.626 251.627 1.00 20.24  ? 2616 GLU A O     1 
ATOM   8438  C  CB    . GLU A 1 2616 ? 212.781 250.756 253.685 1.00 26.20  ? 2616 GLU A CB    1 
ATOM   8439  C  CG    . GLU A 1 2616 ? 212.158 251.752 254.651 1.00 40.31  ? 2616 GLU A CG    1 
ATOM   8440  C  CD    . GLU A 1 2616 ? 212.372 251.373 256.103 1.00 54.34  ? 2616 GLU A CD    1 
ATOM   8441  O  OE1   . GLU A 1 2616 ? 212.435 250.163 256.402 1.00 51.41  ? 2616 GLU A OE1   1 
ATOM   8442  O  OE2   . GLU A 1 2616 ? 212.477 252.288 256.947 1.00 57.16  ? 2616 GLU A OE2   1 
ATOM   8443  N  N     . VAL A 1 2617 ? 215.386 248.549 253.488 1.00 19.28  ? 2617 VAL A N     1 
ATOM   8444  C  CA    . VAL A 1 2617 ? 216.016 247.446 252.773 1.00 12.20  ? 2617 VAL A CA    1 
ATOM   8445  C  C     . VAL A 1 2617 ? 215.025 246.301 252.617 1.00 11.86  ? 2617 VAL A C     1 
ATOM   8446  O  O     . VAL A 1 2617 ? 214.217 246.021 253.512 1.00 15.77  ? 2617 VAL A O     1 
ATOM   8447  C  CB    . VAL A 1 2617 ? 217.305 246.995 253.491 1.00 11.70  ? 2617 VAL A CB    1 
ATOM   8448  C  CG1   . VAL A 1 2617 ? 216.988 246.255 254.781 1.00 16.25  ? 2617 VAL A CG1   1 
ATOM   8449  C  CG2   . VAL A 1 2617 ? 218.153 246.130 252.572 1.00 11.70  ? 2617 VAL A CG2   1 
ATOM   8450  N  N     . VAL A 1 2618 ? 215.064 245.657 251.454 1.00 13.10  ? 2618 VAL A N     1 
ATOM   8451  C  CA    . VAL A 1 2618 ? 214.221 244.511 251.138 1.00 12.94  ? 2618 VAL A CA    1 
ATOM   8452  C  C     . VAL A 1 2618 ? 215.126 243.406 250.617 1.00 11.05  ? 2618 VAL A C     1 
ATOM   8453  O  O     . VAL A 1 2618 ? 215.855 243.608 249.640 1.00 14.61  ? 2618 VAL A O     1 
ATOM   8454  C  CB    . VAL A 1 2618 ? 213.138 244.860 250.103 1.00 11.16  ? 2618 VAL A CB    1 
ATOM   8455  C  CG1   . VAL A 1 2618 ? 212.592 243.598 249.458 1.00 13.04  ? 2618 VAL A CG1   1 
ATOM   8456  C  CG2   . VAL A 1 2618 ? 212.024 245.654 250.753 1.00 12.03  ? 2618 VAL A CG2   1 
ATOM   8457  N  N     . GLY A 1 2619 ? 215.073 242.242 251.258 1.00 10.25  ? 2619 GLY A N     1 
ATOM   8458  C  CA    . GLY A 1 2619 ? 215.957 241.151 250.904 1.00 7.58   ? 2619 GLY A CA    1 
ATOM   8459  C  C     . GLY A 1 2619 ? 215.415 240.220 249.840 1.00 11.37  ? 2619 GLY A C     1 
ATOM   8460  O  O     . GLY A 1 2619 ? 214.322 239.663 249.984 1.00 17.80  ? 2619 GLY A O     1 
ATOM   8461  N  N     . LEU A 1 2620 ? 216.174 240.050 248.763 1.00 11.84  ? 2620 LEU A N     1 
ATOM   8462  C  CA    . LEU A 1 2620 ? 215.898 239.073 247.722 1.00 9.93   ? 2620 LEU A CA    1 
ATOM   8463  C  C     . LEU A 1 2620 ? 217.058 238.092 247.686 1.00 12.96  ? 2620 LEU A C     1 
ATOM   8464  O  O     . LEU A 1 2620 ? 218.221 238.504 247.691 1.00 18.58  ? 2620 LEU A O     1 
ATOM   8465  C  CB    . LEU A 1 2620 ? 215.728 239.746 246.357 1.00 10.83  ? 2620 LEU A CB    1 
ATOM   8466  C  CG    . LEU A 1 2620 ? 214.442 240.522 246.076 1.00 15.57  ? 2620 LEU A CG    1 
ATOM   8467  C  CD1   . LEU A 1 2620 ? 214.555 241.954 246.569 1.00 10.36  ? 2620 LEU A CD1   1 
ATOM   8468  C  CD2   . LEU A 1 2620 ? 214.129 240.492 244.591 1.00 15.34  ? 2620 LEU A CD2   1 
ATOM   8469  N  N     . ASN A 1 2621 ? 216.747 236.805 247.659 1.00 13.90  ? 2621 ASN A N     1 
ATOM   8470  C  CA    . ASN A 1 2621 ? 217.760 235.754 247.659 1.00 10.77  ? 2621 ASN A CA    1 
ATOM   8471  C  C     . ASN A 1 2621 ? 217.749 235.080 246.295 1.00 15.12  ? 2621 ASN A C     1 
ATOM   8472  O  O     . ASN A 1 2621 ? 216.865 234.274 245.995 1.00 22.25  ? 2621 ASN A O     1 
ATOM   8473  C  CB    . ASN A 1 2621 ? 217.506 234.760 248.785 1.00 14.54  ? 2621 ASN A CB    1 
ATOM   8474  C  CG    . ASN A 1 2621 ? 217.344 235.440 250.120 1.00 20.41  ? 2621 ASN A CG    1 
ATOM   8475  O  OD1   . ASN A 1 2621 ? 218.324 235.726 250.807 1.00 17.81  ? 2621 ASN A OD1   1 
ATOM   8476  N  ND2   . ASN A 1 2621 ? 216.103 235.720 250.490 1.00 18.29  ? 2621 ASN A ND2   1 
ATOM   8477  N  N     . PHE A 1 2622 ? 218.730 235.422 245.471 1.00 13.45  ? 2622 PHE A N     1 
ATOM   8478  C  CA    . PHE A 1 2622 ? 218.833 234.846 244.144 1.00 9.65   ? 2622 PHE A CA    1 
ATOM   8479  C  C     . PHE A 1 2622 ? 219.358 233.418 244.227 1.00 10.80  ? 2622 PHE A C     1 
ATOM   8480  O  O     . PHE A 1 2622 ? 220.038 233.035 245.182 1.00 16.79  ? 2622 PHE A O     1 
ATOM   8481  C  CB    . PHE A 1 2622 ? 219.759 235.683 243.260 1.00 10.61  ? 2622 PHE A CB    1 
ATOM   8482  C  CG    . PHE A 1 2622 ? 219.167 236.992 242.809 1.00 7.96   ? 2622 PHE A CG    1 
ATOM   8483  C  CD1   . PHE A 1 2622 ? 217.982 237.467 243.342 1.00 9.18   ? 2622 PHE A CD1   1 
ATOM   8484  C  CD2   . PHE A 1 2622 ? 219.811 237.750 241.848 1.00 6.93   ? 2622 PHE A CD2   1 
ATOM   8485  C  CE1   . PHE A 1 2622 ? 217.454 238.669 242.924 1.00 9.02   ? 2622 PHE A CE1   1 
ATOM   8486  C  CE2   . PHE A 1 2622 ? 219.285 238.951 241.426 1.00 6.69   ? 2622 PHE A CE2   1 
ATOM   8487  C  CZ    . PHE A 1 2622 ? 218.107 239.412 241.965 1.00 6.05   ? 2622 PHE A CZ    1 
ATOM   8488  N  N     . SER A 1 2623 ? 219.031 232.630 243.208 1.00 12.92  ? 2623 SER A N     1 
ATOM   8489  C  CA    . SER A 1 2623 ? 219.538 231.275 243.070 1.00 11.77  ? 2623 SER A CA    1 
ATOM   8490  C  C     . SER A 1 2623 ? 219.767 231.005 241.591 1.00 13.60  ? 2623 SER A C     1 
ATOM   8491  O  O     . SER A 1 2623 ? 219.670 231.907 240.756 1.00 13.87  ? 2623 SER A O     1 
ATOM   8492  C  CB    . SER A 1 2623 ? 218.578 230.255 243.691 1.00 14.68  ? 2623 SER A CB    1 
ATOM   8493  O  OG    . SER A 1 2623 ? 217.317 230.292 243.052 1.00 14.00  ? 2623 SER A OG    1 
ATOM   8494  N  N     . SER A 1 2624 ? 220.064 229.746 241.263 1.00 15.75  ? 2624 SER A N     1 
ATOM   8495  C  CA    . SER A 1 2624 ? 220.368 229.393 239.880 1.00 11.26  ? 2624 SER A CA    1 
ATOM   8496  C  C     . SER A 1 2624 ? 219.194 229.642 238.943 1.00 13.41  ? 2624 SER A C     1 
ATOM   8497  O  O     . SER A 1 2624 ? 219.411 230.037 237.793 1.00 17.72  ? 2624 SER A O     1 
ATOM   8498  C  CB    . SER A 1 2624 ? 220.802 227.930 239.791 1.00 13.50  ? 2624 SER A CB    1 
ATOM   8499  O  OG    . SER A 1 2624 ? 219.716 227.055 240.032 1.00 25.05  ? 2624 SER A OG    1 
ATOM   8500  N  N     . ALA A 1 2625 ? 217.962 229.426 239.402 1.00 11.64  ? 2625 ALA A N     1 
ATOM   8501  C  CA    . ALA A 1 2625 ? 216.779 229.625 238.579 1.00 13.73  ? 2625 ALA A CA    1 
ATOM   8502  C  C     . ALA A 1 2625 ? 216.076 230.943 238.878 1.00 18.01  ? 2625 ALA A C     1 
ATOM   8503  O  O     . ALA A 1 2625 ? 214.870 231.067 238.636 1.00 17.05  ? 2625 ALA A O     1 
ATOM   8504  C  CB    . ALA A 1 2625 ? 215.812 228.454 238.748 1.00 19.49  ? 2625 ALA A CB    1 
ATOM   8505  N  N     . THR A 1 2626 ? 216.799 231.927 239.406 1.00 21.32  ? 2626 THR A N     1 
ATOM   8506  C  CA    . THR A 1 2626 ? 216.219 233.242 239.639 1.00 12.32  ? 2626 THR A CA    1 
ATOM   8507  C  C     . THR A 1 2626 ? 216.034 233.978 238.319 1.00 11.18  ? 2626 THR A C     1 
ATOM   8508  O  O     . THR A 1 2626 ? 216.955 234.053 237.500 1.00 15.95  ? 2626 THR A O     1 
ATOM   8509  C  CB    . THR A 1 2626 ? 217.105 234.054 240.580 1.00 8.06   ? 2626 THR A CB    1 
ATOM   8510  O  OG1   . THR A 1 2626 ? 217.234 233.362 241.826 1.00 13.67  ? 2626 THR A OG1   1 
ATOM   8511  C  CG2   . THR A 1 2626 ? 216.503 235.425 240.828 1.00 8.16   ? 2626 THR A CG2   1 
ATOM   8512  N  N     . THR A 1 2627 ? 214.844 234.519 238.117 1.00 15.04  ? 2627 THR A N     1 
ATOM   8513  C  CA    . THR A 1 2627 ? 214.456 235.244 236.919 1.00 13.75  ? 2627 THR A CA    1 
ATOM   8514  C  C     . THR A 1 2627 ? 213.809 236.556 237.332 1.00 12.25  ? 2627 THR A C     1 
ATOM   8515  O  O     . THR A 1 2627 ? 213.382 236.709 238.482 1.00 14.88  ? 2627 THR A O     1 
ATOM   8516  C  CB    . THR A 1 2627 ? 213.489 234.414 236.059 1.00 15.55  ? 2627 THR A CB    1 
ATOM   8517  O  OG1   . THR A 1 2627 ? 212.213 234.338 236.706 1.00 15.80  ? 2627 THR A OG1   1 
ATOM   8518  C  CG2   . THR A 1 2627 ? 214.027 233.010 235.827 1.00 23.29  ? 2627 THR A CG2   1 
ATOM   8519  N  N     . PRO A 1 2628 ? 213.736 237.544 236.417 1.00 10.65  ? 2628 PRO A N     1 
ATOM   8520  C  CA    . PRO A 1 2628 ? 213.216 238.871 236.789 1.00 11.29  ? 2628 PRO A CA    1 
ATOM   8521  C  C     . PRO A 1 2628 ? 211.824 238.893 237.413 1.00 12.92  ? 2628 PRO A C     1 
ATOM   8522  O  O     . PRO A 1 2628 ? 211.424 239.922 237.968 1.00 11.72  ? 2628 PRO A O     1 
ATOM   8523  C  CB    . PRO A 1 2628 ? 213.219 239.624 235.455 1.00 7.00   ? 2628 PRO A CB    1 
ATOM   8524  C  CG    . PRO A 1 2628 ? 214.319 239.006 234.687 1.00 7.42   ? 2628 PRO A CG    1 
ATOM   8525  C  CD    . PRO A 1 2628 ? 214.359 237.557 235.080 1.00 9.39   ? 2628 PRO A CD    1 
ATOM   8526  N  N     . GLU A 1 2629 ? 211.070 237.794 237.328 1.00 13.62  ? 2629 GLU A N     1 
ATOM   8527  C  CA    . GLU A 1 2629 ? 209.751 237.773 237.954 1.00 14.22  ? 2629 GLU A CA    1 
ATOM   8528  C  C     . GLU A 1 2629 ? 209.846 237.870 239.473 1.00 13.73  ? 2629 GLU A C     1 
ATOM   8529  O  O     . GLU A 1 2629 ? 208.916 238.353 240.123 1.00 15.89  ? 2629 GLU A O     1 
ATOM   8530  C  CB    . GLU A 1 2629 ? 208.972 236.527 237.533 1.00 19.04  ? 2629 GLU A CB    1 
ATOM   8531  C  CG    . GLU A 1 2629 ? 208.580 236.506 236.057 1.00 35.30  ? 2629 GLU A CG    1 
ATOM   8532  C  CD    . GLU A 1 2629 ? 209.688 236.024 235.153 1.00 36.20  ? 2629 GLU A CD    1 
ATOM   8533  O  OE1   . GLU A 1 2629 ? 210.748 235.645 235.680 1.00 32.07  ? 2629 GLU A OE1   1 
ATOM   8534  O  OE2   . GLU A 1 2629 ? 209.500 236.023 233.920 1.00 38.49  ? 2629 GLU A OE2   1 
ATOM   8535  N  N     . LEU A 1 2630 ? 210.963 237.434 240.059 1.00 11.61  ? 2630 LEU A N     1 
ATOM   8536  C  CA    . LEU A 1 2630 ? 211.173 237.672 241.485 1.00 9.88   ? 2630 LEU A CA    1 
ATOM   8537  C  C     . LEU A 1 2630 ? 211.243 239.165 241.781 1.00 14.65  ? 2630 LEU A C     1 
ATOM   8538  O  O     . LEU A 1 2630 ? 210.618 239.655 242.732 1.00 15.86  ? 2630 LEU A O     1 
ATOM   8539  C  CB    . LEU A 1 2630 ? 212.448 236.968 241.949 1.00 12.17  ? 2630 LEU A CB    1 
ATOM   8540  C  CG    . LEU A 1 2630 ? 212.787 237.027 243.439 1.00 9.91   ? 2630 LEU A CG    1 
ATOM   8541  C  CD1   . LEU A 1 2630 ? 212.034 235.951 244.202 1.00 8.62   ? 2630 LEU A CD1   1 
ATOM   8542  C  CD2   . LEU A 1 2630 ? 214.282 236.884 243.651 1.00 9.85   ? 2630 LEU A CD2   1 
ATOM   8543  N  N     . LEU A 1 2631 ? 211.983 239.908 240.953 1.00 15.99  ? 2631 LEU A N     1 
ATOM   8544  C  CA    . LEU A 1 2631 ? 212.045 241.358 241.099 1.00 11.62  ? 2631 LEU A CA    1 
ATOM   8545  C  C     . LEU A 1 2631 ? 210.673 241.983 240.891 1.00 10.76  ? 2631 LEU A C     1 
ATOM   8546  O  O     . LEU A 1 2631 ? 210.303 242.935 241.587 1.00 10.95  ? 2631 LEU A O     1 
ATOM   8547  C  CB    . LEU A 1 2631 ? 213.049 241.943 240.105 1.00 9.99   ? 2631 LEU A CB    1 
ATOM   8548  C  CG    . LEU A 1 2631 ? 214.546 241.950 240.434 1.00 9.95   ? 2631 LEU A CG    1 
ATOM   8549  C  CD1   . LEU A 1 2631 ? 214.838 242.814 241.644 1.00 8.40   ? 2631 LEU A CD1   1 
ATOM   8550  C  CD2   . LEU A 1 2631 ? 215.081 240.542 240.632 1.00 12.92  ? 2631 LEU A CD2   1 
ATOM   8551  N  N     . LEU A 1 2632 ? 209.911 241.468 239.926 1.00 12.57  ? 2632 LEU A N     1 
ATOM   8552  C  CA    . LEU A 1 2632 ? 208.585 242.012 239.655 1.00 11.92  ? 2632 LEU A CA    1 
ATOM   8553  C  C     . LEU A 1 2632 ? 207.632 241.766 240.821 1.00 16.49  ? 2632 LEU A C     1 
ATOM   8554  O  O     . LEU A 1 2632 ? 206.825 242.636 241.163 1.00 20.32  ? 2632 LEU A O     1 
ATOM   8555  C  CB    . LEU A 1 2632 ? 208.034 241.414 238.363 1.00 11.95  ? 2632 LEU A CB    1 
ATOM   8556  C  CG    . LEU A 1 2632 ? 208.807 241.816 237.105 1.00 9.04   ? 2632 LEU A CG    1 
ATOM   8557  C  CD1   . LEU A 1 2632 ? 208.248 241.121 235.875 1.00 12.84  ? 2632 LEU A CD1   1 
ATOM   8558  C  CD2   . LEU A 1 2632 ? 208.791 243.325 236.928 1.00 8.36   ? 2632 LEU A CD2   1 
ATOM   8559  N  N     . LYS A 1 2633 ? 207.707 240.586 241.441 1.00 13.99  ? 2633 LYS A N     1 
ATOM   8560  C  CA    . LYS A 1 2633 ? 206.899 240.315 242.626 1.00 13.41  ? 2633 LYS A CA    1 
ATOM   8561  C  C     . LYS A 1 2633 ? 207.295 241.225 243.779 1.00 17.11  ? 2633 LYS A C     1 
ATOM   8562  O  O     . LYS A 1 2633 ? 206.432 241.721 244.515 1.00 23.35  ? 2633 LYS A O     1 
ATOM   8563  C  CB    . LYS A 1 2633 ? 207.035 238.848 243.036 1.00 15.86  ? 2633 LYS A CB    1 
ATOM   8564  C  CG    . LYS A 1 2633 ? 206.499 237.860 242.017 1.00 18.79  ? 2633 LYS A CG    1 
ATOM   8565  C  CD    . LYS A 1 2633 ? 204.984 237.850 241.986 1.00 30.59  ? 2633 LYS A CD    1 
ATOM   8566  C  CE    . LYS A 1 2633 ? 204.473 236.860 240.955 1.00 32.96  ? 2633 LYS A CE    1 
ATOM   8567  N  NZ    . LYS A 1 2633 ? 205.243 235.587 240.994 1.00 30.61  ? 2633 LYS A NZ    1 
ATOM   8568  N  N     . THR A 1 2634 ? 208.598 241.455 243.956 1.00 19.54  ? 2634 THR A N     1 
ATOM   8569  C  CA    . THR A 1 2634 ? 209.042 242.378 244.996 1.00 16.25  ? 2634 THR A CA    1 
ATOM   8570  C  C     . THR A 1 2634 ? 208.520 243.788 244.738 1.00 15.60  ? 2634 THR A C     1 
ATOM   8571  O  O     . THR A 1 2634 ? 208.084 244.479 245.667 1.00 21.47  ? 2634 THR A O     1 
ATOM   8572  C  CB    . THR A 1 2634 ? 210.567 242.375 245.087 1.00 15.51  ? 2634 THR A CB    1 
ATOM   8573  O  OG1   . THR A 1 2634 ? 211.017 241.078 245.501 1.00 17.23  ? 2634 THR A OG1   1 
ATOM   8574  C  CG2   . THR A 1 2634 ? 211.048 243.409 246.090 1.00 15.18  ? 2634 THR A CG2   1 
ATOM   8575  N  N     . PHE A 1 2635 ? 208.548 244.227 243.477 1.00 14.88  ? 2635 PHE A N     1 
ATOM   8576  C  CA    . PHE A 1 2635 ? 208.006 245.536 243.129 1.00 14.80  ? 2635 PHE A CA    1 
ATOM   8577  C  C     . PHE A 1 2635 ? 206.510 245.605 243.396 1.00 18.48  ? 2635 PHE A C     1 
ATOM   8578  O  O     . PHE A 1 2635 ? 206.008 246.616 243.899 1.00 22.33  ? 2635 PHE A O     1 
ATOM   8579  C  CB    . PHE A 1 2635 ? 208.301 245.853 241.663 1.00 12.15  ? 2635 PHE A CB    1 
ATOM   8580  C  CG    . PHE A 1 2635 ? 209.745 246.147 241.383 1.00 12.03  ? 2635 PHE A CG    1 
ATOM   8581  C  CD1   . PHE A 1 2635 ? 210.569 246.652 242.373 1.00 13.05  ? 2635 PHE A CD1   1 
ATOM   8582  C  CD2   . PHE A 1 2635 ? 210.280 245.916 240.127 1.00 13.22  ? 2635 PHE A CD2   1 
ATOM   8583  C  CE1   . PHE A 1 2635 ? 211.896 246.923 242.116 1.00 11.18  ? 2635 PHE A CE1   1 
ATOM   8584  C  CE2   . PHE A 1 2635 ? 211.608 246.185 239.865 1.00 10.56  ? 2635 PHE A CE2   1 
ATOM   8585  C  CZ    . PHE A 1 2635 ? 212.417 246.688 240.861 1.00 9.38   ? 2635 PHE A CZ    1 
ATOM   8586  N  N     . ASP A 1 2636 ? 205.777 244.542 243.058 1.00 18.29  ? 2636 ASP A N     1 
ATOM   8587  C  CA    . ASP A 1 2636 ? 204.340 244.525 243.306 1.00 17.62  ? 2636 ASP A CA    1 
ATOM   8588  C  C     . ASP A 1 2636 ? 204.037 244.601 244.796 1.00 24.27  ? 2636 ASP A C     1 
ATOM   8589  O  O     . ASP A 1 2636 ? 203.083 245.270 245.211 1.00 30.63  ? 2636 ASP A O     1 
ATOM   8590  C  CB    . ASP A 1 2636 ? 203.713 243.269 242.699 1.00 19.28  ? 2636 ASP A CB    1 
ATOM   8591  C  CG    . ASP A 1 2636 ? 203.720 243.288 241.184 1.00 42.28  ? 2636 ASP A CG    1 
ATOM   8592  O  OD1   . ASP A 1 2636 ? 203.669 244.391 240.602 1.00 47.78  ? 2636 ASP A OD1   1 
ATOM   8593  O  OD2   . ASP A 1 2636 ? 203.774 242.199 240.575 1.00 40.74  ? 2636 ASP A OD2   1 
ATOM   8594  N  N     . HIS A 1 2637 ? 204.836 243.917 245.616 1.00 22.72  ? 2637 HIS A N     1 
ATOM   8595  C  CA    . HIS A 1 2637 ? 204.577 243.913 247.052 1.00 17.78  ? 2637 HIS A CA    1 
ATOM   8596  C  C     . HIS A 1 2637 ? 204.958 245.238 247.701 1.00 19.05  ? 2637 HIS A C     1 
ATOM   8597  O  O     . HIS A 1 2637 ? 204.236 245.737 248.572 1.00 24.05  ? 2637 HIS A O     1 
ATOM   8598  C  CB    . HIS A 1 2637 ? 205.326 242.759 247.717 1.00 19.78  ? 2637 HIS A CB    1 
ATOM   8599  C  CG    . HIS A 1 2637 ? 204.925 242.524 249.140 1.00 26.10  ? 2637 HIS A CG    1 
ATOM   8600  N  ND1   . HIS A 1 2637 ? 205.322 243.348 250.170 1.00 25.28  ? 2637 HIS A ND1   1 
ATOM   8601  C  CD2   . HIS A 1 2637 ? 204.157 241.562 249.702 1.00 31.42  ? 2637 HIS A CD2   1 
ATOM   8602  C  CE1   . HIS A 1 2637 ? 204.817 242.902 251.307 1.00 31.95  ? 2637 HIS A CE1   1 
ATOM   8603  N  NE2   . HIS A 1 2637 ? 204.108 241.819 251.050 1.00 37.11  ? 2637 HIS A NE2   1 
ATOM   8604  N  N     . TYR A 1 2638 ? 206.088 245.825 247.302 1.00 17.55  ? 2638 TYR A N     1 
ATOM   8605  C  CA    . TYR A 1 2638 ? 206.631 246.976 248.013 1.00 14.67  ? 2638 TYR A CA    1 
ATOM   8606  C  C     . TYR A 1 2638 ? 206.448 248.300 247.287 1.00 18.06  ? 2638 TYR A C     1 
ATOM   8607  O  O     . TYR A 1 2638 ? 206.617 249.354 247.910 1.00 15.63  ? 2638 TYR A O     1 
ATOM   8608  C  CB    . TYR A 1 2638 ? 208.125 246.769 248.289 1.00 11.47  ? 2638 TYR A CB    1 
ATOM   8609  C  CG    . TYR A 1 2638 ? 208.410 245.753 249.368 1.00 13.95  ? 2638 TYR A CG    1 
ATOM   8610  C  CD1   . TYR A 1 2638 ? 208.386 246.110 250.709 1.00 13.30  ? 2638 TYR A CD1   1 
ATOM   8611  C  CD2   . TYR A 1 2638 ? 208.701 244.435 249.048 1.00 13.96  ? 2638 TYR A CD2   1 
ATOM   8612  C  CE1   . TYR A 1 2638 ? 208.645 245.185 251.698 1.00 16.75  ? 2638 TYR A CE1   1 
ATOM   8613  C  CE2   . TYR A 1 2638 ? 208.961 243.503 250.030 1.00 17.39  ? 2638 TYR A CE2   1 
ATOM   8614  C  CZ    . TYR A 1 2638 ? 208.931 243.883 251.353 1.00 19.78  ? 2638 TYR A CZ    1 
ATOM   8615  O  OH    . TYR A 1 2638 ? 209.191 242.957 252.335 1.00 22.15  ? 2638 TYR A OH    1 
ATOM   8616  N  N     . CYS A 1 2639 ? 206.114 248.283 246.001 1.00 20.25  ? 2639 CYS A N     1 
ATOM   8617  C  CA    . CYS A 1 2639 ? 206.019 249.502 245.213 1.00 15.33  ? 2639 CYS A CA    1 
ATOM   8618  C  C     . CYS A 1 2639 ? 204.690 249.536 244.474 1.00 20.50  ? 2639 CYS A C     1 
ATOM   8619  O  O     . CYS A 1 2639 ? 203.922 248.571 244.474 1.00 18.43  ? 2639 CYS A O     1 
ATOM   8620  C  CB    . CYS A 1 2639 ? 207.180 249.619 244.218 1.00 16.15  ? 2639 CYS A CB    1 
ATOM   8621  S  SG    . CYS A 1 2639 ? 208.803 249.272 244.916 1.00 21.20  ? 2639 CYS A SG    1 
ATOM   8622  N  N     . GLU A 1 2640 ? 204.430 250.673 243.836 1.00 22.77  ? 2640 GLU A N     1 
ATOM   8623  C  CA    . GLU A 1 2640 ? 203.222 250.878 243.055 1.00 18.09  ? 2640 GLU A CA    1 
ATOM   8624  C  C     . GLU A 1 2640 ? 203.557 251.672 241.801 1.00 21.85  ? 2640 GLU A C     1 
ATOM   8625  O  O     . GLU A 1 2640 ? 204.522 252.444 241.769 1.00 23.04  ? 2640 GLU A O     1 
ATOM   8626  C  CB    . GLU A 1 2640 ? 202.141 251.599 243.870 1.00 20.71  ? 2640 GLU A CB    1 
ATOM   8627  C  CG    . GLU A 1 2640 ? 202.503 253.021 244.259 1.00 35.20  ? 2640 GLU A CG    1 
ATOM   8628  C  CD    . GLU A 1 2640 ? 201.443 253.681 245.116 1.00 46.54  ? 2640 GLU A CD    1 
ATOM   8629  O  OE1   . GLU A 1 2640 ? 200.431 253.018 245.428 1.00 43.68  ? 2640 GLU A OE1   1 
ATOM   8630  O  OE2   . GLU A 1 2640 ? 201.623 254.862 245.479 1.00 44.15  ? 2640 GLU A OE2   1 
ATOM   8631  N  N     . TYR A 1 2641 ? 202.741 251.467 240.769 1.00 23.34  ? 2641 TYR A N     1 
ATOM   8632  C  CA    . TYR A 1 2641 ? 202.859 252.173 239.501 1.00 19.65  ? 2641 TYR A CA    1 
ATOM   8633  C  C     . TYR A 1 2641 ? 201.829 253.293 239.457 1.00 20.41  ? 2641 TYR A C     1 
ATOM   8634  O  O     . TYR A 1 2641 ? 200.657 253.074 239.781 1.00 26.04  ? 2641 TYR A O     1 
ATOM   8635  C  CB    . TYR A 1 2641 ? 202.637 251.233 238.312 1.00 18.05  ? 2641 TYR A CB    1 
ATOM   8636  C  CG    . TYR A 1 2641 ? 203.468 249.968 238.296 1.00 18.15  ? 2641 TYR A CG    1 
ATOM   8637  C  CD1   . TYR A 1 2641 ? 203.159 248.894 239.119 1.00 23.63  ? 2641 TYR A CD1   1 
ATOM   8638  C  CD2   . TYR A 1 2641 ? 204.546 249.839 237.433 1.00 17.73  ? 2641 TYR A CD2   1 
ATOM   8639  C  CE1   . TYR A 1 2641 ? 203.911 247.736 239.095 1.00 28.64  ? 2641 TYR A CE1   1 
ATOM   8640  C  CE2   . TYR A 1 2641 ? 205.303 248.686 237.401 1.00 17.31  ? 2641 TYR A CE2   1 
ATOM   8641  C  CZ    . TYR A 1 2641 ? 204.982 247.637 238.234 1.00 24.84  ? 2641 TYR A CZ    1 
ATOM   8642  O  OH    . TYR A 1 2641 ? 205.734 246.485 238.209 1.00 25.00  ? 2641 TYR A OH    1 
ATOM   8643  N  N     . ARG A 1 2642 ? 202.263 254.484 239.054 1.00 20.57  ? 2642 ARG A N     1 
ATOM   8644  C  CA    . ARG A 1 2642 ? 201.360 255.610 238.863 1.00 20.86  ? 2642 ARG A CA    1 
ATOM   8645  C  C     . ARG A 1 2642 ? 201.621 256.245 237.506 1.00 26.74  ? 2642 ARG A C     1 
ATOM   8646  O  O     . ARG A 1 2642 ? 202.765 256.316 237.051 1.00 25.09  ? 2642 ARG A O     1 
ATOM   8647  C  CB    . ARG A 1 2642 ? 201.508 256.655 239.982 1.00 21.57  ? 2642 ARG A CB    1 
ATOM   8648  C  CG    . ARG A 1 2642 ? 202.832 257.395 239.995 1.00 29.67  ? 2642 ARG A CG    1 
ATOM   8649  C  CD    . ARG A 1 2642 ? 202.825 258.511 241.026 1.00 35.27  ? 2642 ARG A CD    1 
ATOM   8650  N  NE    . ARG A 1 2642 ? 204.152 259.082 241.221 1.00 47.64  ? 2642 ARG A NE    1 
ATOM   8651  C  CZ    . ARG A 1 2642 ? 205.071 258.578 242.033 1.00 47.60  ? 2642 ARG A CZ    1 
ATOM   8652  N  NH1   . ARG A 1 2642 ? 204.837 257.492 242.752 1.00 40.72  ? 2642 ARG A NH1   1 
ATOM   8653  N  NH2   . ARG A 1 2642 ? 206.252 259.179 242.128 1.00 42.53  ? 2642 ARG A NH2   1 
ATOM   8654  N  N     . ARG A 1 2643 ? 200.551 256.702 236.858 1.00 32.30  ? 2643 ARG A N     1 
ATOM   8655  C  CA    . ARG A 1 2643 ? 200.645 257.273 235.515 1.00 29.23  ? 2643 ARG A CA    1 
ATOM   8656  C  C     . ARG A 1 2643 ? 200.815 258.782 235.626 1.00 28.98  ? 2643 ARG A C     1 
ATOM   8657  O  O     . ARG A 1 2643 ? 199.850 259.546 235.582 1.00 36.70  ? 2643 ARG A O     1 
ATOM   8658  C  CB    . ARG A 1 2643 ? 199.422 256.909 234.685 1.00 35.54  ? 2643 ARG A CB    1 
ATOM   8659  C  CG    . ARG A 1 2643 ? 199.675 256.929 233.186 1.00 37.59  ? 2643 ARG A CG    1 
ATOM   8660  C  CD    . ARG A 1 2643 ? 198.576 256.216 232.417 1.00 40.86  ? 2643 ARG A CD    1 
ATOM   8661  N  NE    . ARG A 1 2643 ? 198.943 254.845 232.079 1.00 48.70  ? 2643 ARG A NE    1 
ATOM   8662  C  CZ    . ARG A 1 2643 ? 199.805 254.511 231.128 1.00 53.60  ? 2643 ARG A CZ    1 
ATOM   8663  N  NH1   . ARG A 1 2643 ? 200.418 255.426 230.395 1.00 44.71  ? 2643 ARG A NH1   1 
ATOM   8664  N  NH2   . ARG A 1 2643 ? 200.060 253.224 230.906 1.00 50.51  ? 2643 ARG A NH2   1 
ATOM   8665  N  N     . THR A 1 2644 ? 202.064 259.217 235.770 1.00 29.30  ? 2644 THR A N     1 
ATOM   8666  C  CA    . THR A 1 2644 ? 202.374 260.630 235.719 1.00 34.60  ? 2644 THR A CA    1 
ATOM   8667  C  C     . THR A 1 2644 ? 202.273 261.119 234.276 1.00 39.61  ? 2644 THR A C     1 
ATOM   8668  O  O     . THR A 1 2644 ? 202.276 260.316 233.340 1.00 40.44  ? 2644 THR A O     1 
ATOM   8669  C  CB    . THR A 1 2644 ? 203.774 260.884 236.274 1.00 36.90  ? 2644 THR A CB    1 
ATOM   8670  O  OG1   . THR A 1 2644 ? 204.751 260.531 235.287 1.00 33.79  ? 2644 THR A OG1   1 
ATOM   8671  C  CG2   . THR A 1 2644 ? 204.006 260.053 237.524 1.00 36.11  ? 2644 THR A CG2   1 
ATOM   8672  N  N     . PRO A 1 2645 ? 202.167 262.436 234.067 1.00 42.66  ? 2645 PRO A N     1 
ATOM   8673  C  CA    . PRO A 1 2645 ? 202.100 262.944 232.686 1.00 44.59  ? 2645 PRO A CA    1 
ATOM   8674  C  C     . PRO A 1 2645 ? 203.286 262.542 231.825 1.00 42.28  ? 2645 PRO A C     1 
ATOM   8675  O  O     . PRO A 1 2645 ? 203.152 262.482 230.597 1.00 43.92  ? 2645 PRO A O     1 
ATOM   8676  C  CB    . PRO A 1 2645 ? 202.035 264.464 232.882 1.00 41.23  ? 2645 PRO A CB    1 
ATOM   8677  C  CG    . PRO A 1 2645 ? 201.384 264.632 234.206 1.00 42.85  ? 2645 PRO A CG    1 
ATOM   8678  C  CD    . PRO A 1 2645 ? 201.860 263.486 235.055 1.00 39.92  ? 2645 PRO A CD    1 
ATOM   8679  N  N     . ASN A 1 2646 ? 204.441 262.263 232.426 1.00 39.22  ? 2646 ASN A N     1 
ATOM   8680  C  CA    . ASN A 1 2646 ? 205.613 261.841 231.670 1.00 39.22  ? 2646 ASN A CA    1 
ATOM   8681  C  C     . ASN A 1 2646 ? 205.643 260.345 231.389 1.00 40.12  ? 2646 ASN A C     1 
ATOM   8682  O  O     . ASN A 1 2646 ? 206.511 259.893 230.633 1.00 35.14  ? 2646 ASN A O     1 
ATOM   8683  C  CB    . ASN A 1 2646 ? 206.892 262.243 232.412 1.00 39.97  ? 2646 ASN A CB    1 
ATOM   8684  C  CG    . ASN A 1 2646 ? 207.130 263.737 232.390 1.00 46.92  ? 2646 ASN A CG    1 
ATOM   8685  O  OD1   . ASN A 1 2646 ? 206.863 264.404 231.390 1.00 49.56  ? 2646 ASN A OD1   1 
ATOM   8686  N  ND2   . ASN A 1 2646 ? 207.639 264.271 233.492 1.00 49.37  ? 2646 ASN A ND2   1 
ATOM   8687  N  N     . GLY A 1 2647 ? 204.734 259.569 231.967 1.00 31.46  ? 2647 GLY A N     1 
ATOM   8688  C  CA    . GLY A 1 2647 ? 204.679 258.145 231.735 1.00 21.88  ? 2647 GLY A CA    1 
ATOM   8689  C  C     . GLY A 1 2647 ? 204.398 257.405 233.022 1.00 23.91  ? 2647 GLY A C     1 
ATOM   8690  O  O     . GLY A 1 2647 ? 204.001 257.990 234.027 1.00 31.00  ? 2647 GLY A O     1 
ATOM   8691  N  N     . VAL A 1 2648 ? 204.605 256.094 232.990 1.00 23.86  ? 2648 VAL A N     1 
ATOM   8692  C  CA    . VAL A 1 2648 ? 204.369 255.258 234.162 1.00 18.28  ? 2648 VAL A CA    1 
ATOM   8693  C  C     . VAL A 1 2648 ? 205.621 255.253 235.029 1.00 17.83  ? 2648 VAL A C     1 
ATOM   8694  O  O     . VAL A 1 2648 ? 206.727 254.992 234.544 1.00 20.00  ? 2648 VAL A O     1 
ATOM   8695  C  CB    . VAL A 1 2648 ? 203.971 253.834 233.747 1.00 19.60  ? 2648 VAL A CB    1 
ATOM   8696  C  CG1   . VAL A 1 2648 ? 203.855 252.938 234.969 1.00 18.19  ? 2648 VAL A CG1   1 
ATOM   8697  C  CG2   . VAL A 1 2648 ? 202.665 253.857 232.982 1.00 26.90  ? 2648 VAL A CG2   1 
ATOM   8698  N  N     . VAL A 1 2649 ? 205.447 255.544 236.315 1.00 19.08  ? 2649 VAL A N     1 
ATOM   8699  C  CA    . VAL A 1 2649 ? 206.538 255.599 237.277 1.00 19.27  ? 2649 VAL A CA    1 
ATOM   8700  C  C     . VAL A 1 2649 ? 206.264 254.579 238.373 1.00 18.26  ? 2649 VAL A C     1 
ATOM   8701  O  O     . VAL A 1 2649 ? 205.172 254.564 238.954 1.00 18.49  ? 2649 VAL A O     1 
ATOM   8702  C  CB    . VAL A 1 2649 ? 206.702 257.010 237.870 1.00 20.92  ? 2649 VAL A CB    1 
ATOM   8703  C  CG1   . VAL A 1 2649 ? 207.669 256.987 239.039 1.00 20.17  ? 2649 VAL A CG1   1 
ATOM   8704  C  CG2   . VAL A 1 2649 ? 207.178 257.978 236.802 1.00 24.31  ? 2649 VAL A CG2   1 
ATOM   8705  N  N     . LEU A 1 2650 ? 207.249 253.730 238.643 1.00 16.51  ? 2650 LEU A N     1 
ATOM   8706  C  CA    . LEU A 1 2650 ? 207.184 252.756 239.724 1.00 15.54  ? 2650 LEU A CA    1 
ATOM   8707  C  C     . LEU A 1 2650 ? 207.964 253.299 240.913 1.00 17.18  ? 2650 LEU A C     1 
ATOM   8708  O  O     . LEU A 1 2650 ? 209.172 253.543 240.809 1.00 15.31  ? 2650 LEU A O     1 
ATOM   8709  C  CB    . LEU A 1 2650 ? 207.749 251.408 239.283 1.00 15.11  ? 2650 LEU A CB    1 
ATOM   8710  C  CG    . LEU A 1 2650 ? 207.789 250.305 240.340 1.00 17.26  ? 2650 LEU A CG    1 
ATOM   8711  C  CD1   . LEU A 1 2650 ? 206.388 249.828 240.673 1.00 18.48  ? 2650 LEU A CD1   1 
ATOM   8712  C  CD2   . LEU A 1 2650 ? 208.652 249.149 239.869 1.00 15.33  ? 2650 LEU A CD2   1 
ATOM   8713  N  N     . ALA A 1 2651 ? 207.277 253.485 242.037 1.00 18.47  ? 2651 ALA A N     1 
ATOM   8714  C  CA    . ALA A 1 2651 ? 207.889 254.063 243.223 1.00 14.07  ? 2651 ALA A CA    1 
ATOM   8715  C  C     . ALA A 1 2651 ? 207.432 253.303 244.457 1.00 21.61  ? 2651 ALA A C     1 
ATOM   8716  O  O     . ALA A 1 2651 ? 206.337 252.732 244.464 1.00 23.07  ? 2651 ALA A O     1 
ATOM   8717  C  CB    . ALA A 1 2651 ? 207.533 255.552 243.368 1.00 17.68  ? 2651 ALA A CB    1 
ATOM   8718  N  N     . PRO A 1 2652 ? 208.243 253.284 245.516 1.00 20.70  ? 2652 PRO A N     1 
ATOM   8719  C  CA    . PRO A 1 2652 ? 207.842 252.578 246.737 1.00 20.21  ? 2652 PRO A CA    1 
ATOM   8720  C  C     . PRO A 1 2652 ? 206.578 253.171 247.342 1.00 25.48  ? 2652 PRO A C     1 
ATOM   8721  O  O     . PRO A 1 2652 ? 206.302 254.365 247.214 1.00 26.52  ? 2652 PRO A O     1 
ATOM   8722  C  CB    . PRO A 1 2652 ? 209.045 252.762 247.668 1.00 17.74  ? 2652 PRO A CB    1 
ATOM   8723  C  CG    . PRO A 1 2652 ? 210.185 253.064 246.769 1.00 17.94  ? 2652 PRO A CG    1 
ATOM   8724  C  CD    . PRO A 1 2652 ? 209.609 253.821 245.617 1.00 18.10  ? 2652 PRO A CD    1 
ATOM   8725  N  N     . VAL A 1 2653 ? 205.802 252.308 248.001 1.00 30.30  ? 2653 VAL A N     1 
ATOM   8726  C  CA    . VAL A 1 2653 ? 204.570 252.754 248.648 1.00 25.96  ? 2653 VAL A CA    1 
ATOM   8727  C  C     . VAL A 1 2653 ? 204.879 253.766 249.742 1.00 28.20  ? 2653 VAL A C     1 
ATOM   8728  O  O     . VAL A 1 2653 ? 204.198 254.790 249.872 1.00 25.99  ? 2653 VAL A O     1 
ATOM   8729  C  CB    . VAL A 1 2653 ? 203.789 251.545 249.198 1.00 27.70  ? 2653 VAL A CB    1 
ATOM   8730  C  CG1   . VAL A 1 2653 ? 202.561 252.009 249.964 1.00 40.37  ? 2653 VAL A CG1   1 
ATOM   8731  C  CG2   . VAL A 1 2653 ? 203.394 250.612 248.066 1.00 21.05  ? 2653 VAL A CG2   1 
ATOM   8732  N  N     . GLN A 1 2654 ? 205.909 253.501 250.543 1.00 30.60  ? 2654 GLN A N     1 
ATOM   8733  C  CA    . GLN A 1 2654 ? 206.313 254.415 251.606 1.00 33.06  ? 2654 GLN A CA    1 
ATOM   8734  C  C     . GLN A 1 2654 ? 206.896 255.681 250.990 1.00 28.06  ? 2654 GLN A C     1 
ATOM   8735  O  O     . GLN A 1 2654 ? 207.998 255.658 250.435 1.00 29.14  ? 2654 GLN A O     1 
ATOM   8736  C  CB    . GLN A 1 2654 ? 207.330 253.742 252.523 1.00 32.30  ? 2654 GLN A CB    1 
ATOM   8737  C  CG    . GLN A 1 2654 ? 206.909 252.377 253.035 1.00 36.51  ? 2654 GLN A CG    1 
ATOM   8738  C  CD    . GLN A 1 2654 ? 207.845 251.844 254.101 1.00 50.37  ? 2654 GLN A CD    1 
ATOM   8739  O  OE1   . GLN A 1 2654 ? 208.067 252.487 255.128 1.00 53.37  ? 2654 GLN A OE1   1 
ATOM   8740  N  NE2   . GLN A 1 2654 ? 208.403 250.663 253.864 1.00 52.64  ? 2654 GLN A NE2   1 
ATOM   8741  N  N     . LEU A 1 2655 ? 206.160 256.786 251.085 1.00 26.91  ? 2655 LEU A N     1 
ATOM   8742  C  CA    . LEU A 1 2655 ? 206.654 258.055 250.569 1.00 30.84  ? 2655 LEU A CA    1 
ATOM   8743  C  C     . LEU A 1 2655 ? 207.846 258.535 251.387 1.00 33.69  ? 2655 LEU A C     1 
ATOM   8744  O  O     . LEU A 1 2655 ? 207.919 258.317 252.599 1.00 33.07  ? 2655 LEU A O     1 
ATOM   8745  C  CB    . LEU A 1 2655 ? 205.551 259.114 250.584 1.00 33.23  ? 2655 LEU A CB    1 
ATOM   8746  C  CG    . LEU A 1 2655 ? 204.472 259.090 249.496 1.00 36.07  ? 2655 LEU A CG    1 
ATOM   8747  C  CD1   . LEU A 1 2655 ? 203.507 257.929 249.674 1.00 35.47  ? 2655 LEU A CD1   1 
ATOM   8748  C  CD2   . LEU A 1 2655 ? 203.721 260.413 249.467 1.00 33.50  ? 2655 LEU A CD2   1 
ATOM   8749  N  N     . GLY A 1 2656 ? 208.788 259.189 250.711 1.00 28.77  ? 2656 GLY A N     1 
ATOM   8750  C  CA    . GLY A 1 2656 ? 209.948 259.751 251.368 1.00 25.15  ? 2656 GLY A CA    1 
ATOM   8751  C  C     . GLY A 1 2656 ? 211.044 258.767 251.699 1.00 28.64  ? 2656 GLY A C     1 
ATOM   8752  O  O     . GLY A 1 2656 ? 212.043 259.164 252.312 1.00 34.76  ? 2656 GLY A O     1 
ATOM   8753  N  N     . LYS A 1 2657 ? 210.901 257.503 251.316 1.00 27.22  ? 2657 LYS A N     1 
ATOM   8754  C  CA    . LYS A 1 2657 ? 211.877 256.471 251.627 1.00 27.22  ? 2657 LYS A CA    1 
ATOM   8755  C  C     . LYS A 1 2657 ? 212.429 255.874 250.342 1.00 21.94  ? 2657 LYS A C     1 
ATOM   8756  O  O     . LYS A 1 2657 ? 211.698 255.690 249.365 1.00 22.54  ? 2657 LYS A O     1 
ATOM   8757  C  CB    . LYS A 1 2657 ? 211.259 255.368 252.493 1.00 27.87  ? 2657 LYS A CB    1 
ATOM   8758  C  CG    . LYS A 1 2657 ? 210.485 255.883 253.692 1.00 33.42  ? 2657 LYS A CG    1 
ATOM   8759  C  CD    . LYS A 1 2657 ? 211.381 255.993 254.912 1.00 34.50  ? 2657 LYS A CD    1 
ATOM   8760  C  CE    . LYS A 1 2657 ? 210.586 256.369 256.150 1.00 37.32  ? 2657 LYS A CE    1 
ATOM   8761  N  NZ    . LYS A 1 2657 ? 211.279 257.415 256.951 1.00 41.40  ? 2657 LYS A NZ    1 
ATOM   8762  N  N     . TRP A 1 2658 ? 213.723 255.574 250.353 1.00 18.05  ? 2658 TRP A N     1 
ATOM   8763  C  CA    . TRP A 1 2658 ? 214.393 254.920 249.240 1.00 12.87  ? 2658 TRP A CA    1 
ATOM   8764  C  C     . TRP A 1 2658 ? 214.430 253.420 249.488 1.00 18.04  ? 2658 TRP A C     1 
ATOM   8765  O  O     . TRP A 1 2658 ? 214.898 252.971 250.540 1.00 28.96  ? 2658 TRP A O     1 
ATOM   8766  C  CB    . TRP A 1 2658 ? 215.811 255.465 249.060 1.00 14.53  ? 2658 TRP A CB    1 
ATOM   8767  C  CG    . TRP A 1 2658 ? 215.873 256.667 248.176 1.00 12.00  ? 2658 TRP A CG    1 
ATOM   8768  C  CD1   . TRP A 1 2658 ? 215.568 257.951 248.514 1.00 8.89   ? 2658 TRP A CD1   1 
ATOM   8769  C  CD2   . TRP A 1 2658 ? 216.266 256.697 246.800 1.00 11.37  ? 2658 TRP A CD2   1 
ATOM   8770  N  NE1   . TRP A 1 2658 ? 215.744 258.779 247.435 1.00 10.63  ? 2658 TRP A NE1   1 
ATOM   8771  C  CE2   . TRP A 1 2658 ? 216.173 258.033 246.370 1.00 12.39  ? 2658 TRP A CE2   1 
ATOM   8772  C  CE3   . TRP A 1 2658 ? 216.688 255.723 245.892 1.00 10.01  ? 2658 TRP A CE3   1 
ATOM   8773  C  CZ2   . TRP A 1 2658 ? 216.484 258.421 245.070 1.00 11.10  ? 2658 TRP A CZ2   1 
ATOM   8774  C  CZ3   . TRP A 1 2658 ? 216.996 256.109 244.603 1.00 11.91  ? 2658 TRP A CZ3   1 
ATOM   8775  C  CH2   . TRP A 1 2658 ? 216.893 257.445 244.204 1.00 12.89  ? 2658 TRP A CH2   1 
ATOM   8776  N  N     . LEU A 1 2659 ? 213.940 252.649 248.524 1.00 14.24  ? 2659 LEU A N     1 
ATOM   8777  C  CA    . LEU A 1 2659 ? 213.885 251.199 248.651 1.00 11.64  ? 2659 LEU A CA    1 
ATOM   8778  C  C     . LEU A 1 2659 ? 215.188 250.601 248.137 1.00 14.62  ? 2659 LEU A C     1 
ATOM   8779  O  O     . LEU A 1 2659 ? 215.551 250.796 246.972 1.00 15.68  ? 2659 LEU A O     1 
ATOM   8780  C  CB    . LEU A 1 2659 ? 212.695 250.631 247.882 1.00 12.47  ? 2659 LEU A CB    1 
ATOM   8781  C  CG    . LEU A 1 2659 ? 212.349 249.185 248.233 1.00 18.26  ? 2659 LEU A CG    1 
ATOM   8782  C  CD1   . LEU A 1 2659 ? 211.829 249.108 249.657 1.00 17.11  ? 2659 LEU A CD1   1 
ATOM   8783  C  CD2   . LEU A 1 2659 ? 211.340 248.618 247.261 1.00 14.29  ? 2659 LEU A CD2   1 
ATOM   8784  N  N     . VAL A 1 2660 ? 215.886 249.876 249.003 1.00 15.27  ? 2660 VAL A N     1 
ATOM   8785  C  CA    . VAL A 1 2660 ? 217.153 249.237 248.672 1.00 13.63  ? 2660 VAL A CA    1 
ATOM   8786  C  C     . VAL A 1 2660 ? 216.881 247.751 248.498 1.00 10.95  ? 2660 VAL A C     1 
ATOM   8787  O  O     . VAL A 1 2660 ? 216.656 247.033 249.479 1.00 15.24  ? 2660 VAL A O     1 
ATOM   8788  C  CB    . VAL A 1 2660 ? 218.216 249.482 249.751 1.00 9.32   ? 2660 VAL A CB    1 
ATOM   8789  C  CG1   . VAL A 1 2660 ? 219.512 248.801 249.377 1.00 11.20  ? 2660 VAL A CG1   1 
ATOM   8790  C  CG2   . VAL A 1 2660 ? 218.433 250.971 249.954 1.00 14.81  ? 2660 VAL A CG2   1 
ATOM   8791  N  N     . LEU A 1 2661 ? 216.909 247.281 247.255 1.00 9.98   ? 2661 LEU A N     1 
ATOM   8792  C  CA    . LEU A 1 2661 ? 216.713 245.865 246.967 1.00 8.88   ? 2661 LEU A CA    1 
ATOM   8793  C  C     . LEU A 1 2661 ? 218.053 245.153 247.094 1.00 10.41  ? 2661 LEU A C     1 
ATOM   8794  O  O     . LEU A 1 2661 ? 218.913 245.271 246.216 1.00 10.94  ? 2661 LEU A O     1 
ATOM   8795  C  CB    . LEU A 1 2661 ? 216.113 245.675 245.577 1.00 8.25   ? 2661 LEU A CB    1 
ATOM   8796  C  CG    . LEU A 1 2661 ? 214.600 245.885 245.461 1.00 9.91   ? 2661 LEU A CG    1 
ATOM   8797  C  CD1   . LEU A 1 2661 ? 214.250 247.359 245.351 1.00 15.87  ? 2661 LEU A CD1   1 
ATOM   8798  C  CD2   . LEU A 1 2661 ? 214.036 245.110 244.289 1.00 10.29  ? 2661 LEU A CD2   1 
ATOM   8799  N  N     . PHE A 1 2662 ? 218.232 244.415 248.187 1.00 8.88   ? 2662 PHE A N     1 
ATOM   8800  C  CA    . PHE A 1 2662 ? 219.485 243.734 248.490 1.00 9.03   ? 2662 PHE A CA    1 
ATOM   8801  C  C     . PHE A 1 2662 ? 219.410 242.299 247.985 1.00 10.23  ? 2662 PHE A C     1 
ATOM   8802  O  O     . PHE A 1 2662 ? 218.641 241.491 248.511 1.00 11.79  ? 2662 PHE A O     1 
ATOM   8803  C  CB    . PHE A 1 2662 ? 219.764 243.768 249.990 1.00 8.68   ? 2662 PHE A CB    1 
ATOM   8804  C  CG    . PHE A 1 2662 ? 220.947 242.947 250.402 1.00 8.95   ? 2662 PHE A CG    1 
ATOM   8805  C  CD1   . PHE A 1 2662 ? 222.136 243.022 249.700 1.00 8.21   ? 2662 PHE A CD1   1 
ATOM   8806  C  CD2   . PHE A 1 2662 ? 220.866 242.090 251.483 1.00 5.81   ? 2662 PHE A CD2   1 
ATOM   8807  C  CE1   . PHE A 1 2662 ? 223.222 242.265 250.077 1.00 9.16   ? 2662 PHE A CE1   1 
ATOM   8808  C  CE2   . PHE A 1 2662 ? 221.951 241.330 251.862 1.00 5.72   ? 2662 PHE A CE2   1 
ATOM   8809  C  CZ    . PHE A 1 2662 ? 223.130 241.417 251.159 1.00 7.04   ? 2662 PHE A CZ    1 
ATOM   8810  N  N     . CYS A 1 2663 ? 220.224 241.979 246.981 1.00 10.87  ? 2663 CYS A N     1 
ATOM   8811  C  CA    . CYS A 1 2663 ? 220.275 240.638 246.415 1.00 10.22  ? 2663 CYS A CA    1 
ATOM   8812  C  C     . CYS A 1 2663 ? 221.389 239.846 247.094 1.00 13.85  ? 2663 CYS A C     1 
ATOM   8813  O  O     . CYS A 1 2663 ? 222.541 240.289 247.127 1.00 14.29  ? 2663 CYS A O     1 
ATOM   8814  C  CB    . CYS A 1 2663 ? 220.494 240.702 244.905 1.00 10.43  ? 2663 CYS A CB    1 
ATOM   8815  S  SG    . CYS A 1 2663 ? 219.497 241.960 244.072 1.00 16.42  ? 2663 CYS A SG    1 
ATOM   8816  N  N     . ASP A 1 2664 ? 221.039 238.675 247.635 1.00 16.41  ? 2664 ASP A N     1 
ATOM   8817  C  CA    . ASP A 1 2664 ? 221.983 237.925 248.459 1.00 14.91  ? 2664 ASP A CA    1 
ATOM   8818  C  C     . ASP A 1 2664 ? 223.082 237.274 247.627 1.00 20.57  ? 2664 ASP A C     1 
ATOM   8819  O  O     . ASP A 1 2664 ? 224.256 237.309 248.014 1.00 24.86  ? 2664 ASP A O     1 
ATOM   8820  C  CB    . ASP A 1 2664 ? 221.244 236.864 249.273 1.00 23.91  ? 2664 ASP A CB    1 
ATOM   8821  C  CG    . ASP A 1 2664 ? 222.093 236.299 250.396 1.00 35.36  ? 2664 ASP A CG    1 
ATOM   8822  O  OD1   . ASP A 1 2664 ? 223.123 236.920 250.732 1.00 30.54  ? 2664 ASP A OD1   1 
ATOM   8823  O  OD2   . ASP A 1 2664 ? 221.733 235.233 250.936 1.00 31.57  ? 2664 ASP A OD2   1 
ATOM   8824  N  N     . GLU A 1 2665 ? 222.725 236.642 246.505 1.00 12.47  ? 2665 GLU A N     1 
ATOM   8825  C  CA    . GLU A 1 2665 ? 223.683 235.902 245.672 1.00 10.59  ? 2665 GLU A CA    1 
ATOM   8826  C  C     . GLU A 1 2665 ? 223.480 236.323 244.218 1.00 11.43  ? 2665 GLU A C     1 
ATOM   8827  O  O     . GLU A 1 2665 ? 222.802 235.640 243.451 1.00 15.95  ? 2665 GLU A O     1 
ATOM   8828  C  CB    . GLU A 1 2665 ? 223.509 234.397 245.855 1.00 13.56  ? 2665 GLU A CB    1 
ATOM   8829  C  CG    . GLU A 1 2665 ? 223.604 233.920 247.294 1.00 19.80  ? 2665 GLU A CG    1 
ATOM   8830  C  CD    . GLU A 1 2665 ? 224.998 233.465 247.671 1.00 22.05  ? 2665 GLU A CD    1 
ATOM   8831  O  OE1   . GLU A 1 2665 ? 225.870 233.402 246.779 1.00 24.59  ? 2665 GLU A OE1   1 
ATOM   8832  O  OE2   . GLU A 1 2665 ? 225.224 233.173 248.863 1.00 25.99  ? 2665 GLU A OE2   1 
ATOM   8833  N  N     . ILE A 1 2666 ? 224.116 237.428 243.828 1.00 10.09  ? 2666 ILE A N     1 
ATOM   8834  C  CA    . ILE A 1 2666 ? 223.818 238.032 242.533 1.00 6.32   ? 2666 ILE A CA    1 
ATOM   8835  C  C     . ILE A 1 2666 ? 224.451 237.283 241.364 1.00 6.76   ? 2666 ILE A C     1 
ATOM   8836  O  O     . ILE A 1 2666 ? 224.038 237.490 240.216 1.00 10.44  ? 2666 ILE A O     1 
ATOM   8837  C  CB    . ILE A 1 2666 ? 224.252 239.507 242.531 1.00 9.12   ? 2666 ILE A CB    1 
ATOM   8838  C  CG1   . ILE A 1 2666 ? 223.397 240.317 241.551 1.00 9.51   ? 2666 ILE A CG1   1 
ATOM   8839  C  CG2   . ILE A 1 2666 ? 225.731 239.639 242.207 1.00 7.28   ? 2666 ILE A CG2   1 
ATOM   8840  C  CD1   . ILE A 1 2666 ? 223.474 241.808 241.766 1.00 8.53   ? 2666 ILE A CD1   1 
ATOM   8841  N  N     . ASN A 1 2667 ? 225.429 236.412 241.610 1.00 8.21   ? 2667 ASN A N     1 
ATOM   8842  C  CA    . ASN A 1 2667 ? 226.110 235.696 240.538 1.00 6.56   ? 2667 ASN A CA    1 
ATOM   8843  C  C     . ASN A 1 2667 ? 225.687 234.234 240.430 1.00 8.64   ? 2667 ASN A C     1 
ATOM   8844  O  O     . ASN A 1 2667 ? 226.280 233.485 239.648 1.00 8.25   ? 2667 ASN A O     1 
ATOM   8845  C  CB    . ASN A 1 2667 ? 227.627 235.793 240.714 1.00 6.53   ? 2667 ASN A CB    1 
ATOM   8846  C  CG    . ASN A 1 2667 ? 228.090 235.333 242.079 1.00 7.11   ? 2667 ASN A CG    1 
ATOM   8847  O  OD1   . ASN A 1 2667 ? 227.284 234.967 242.932 1.00 11.41  ? 2667 ASN A OD1   1 
ATOM   8848  N  ND2   . ASN A 1 2667 ? 229.399 235.349 242.294 1.00 4.67   ? 2667 ASN A ND2   1 
ATOM   8849  N  N     . LEU A 1 2668 ? 224.682 233.811 241.190 1.00 9.81   ? 2668 LEU A N     1 
ATOM   8850  C  CA    . LEU A 1 2668 ? 224.147 232.455 241.114 1.00 9.44   ? 2668 LEU A CA    1 
ATOM   8851  C  C     . LEU A 1 2668 ? 223.241 232.173 239.914 1.00 10.15  ? 2668 LEU A C     1 
ATOM   8852  O  O     . LEU A 1 2668 ? 223.259 231.041 239.415 1.00 12.09  ? 2668 LEU A O     1 
ATOM   8853  C  CB    . LEU A 1 2668 ? 223.390 232.103 242.397 1.00 10.63  ? 2668 LEU A CB    1 
ATOM   8854  C  CG    . LEU A 1 2668 ? 224.221 231.441 243.494 1.00 10.16  ? 2668 LEU A CG    1 
ATOM   8855  C  CD1   . LEU A 1 2668 ? 223.348 231.081 244.673 1.00 17.25  ? 2668 LEU A CD1   1 
ATOM   8856  C  CD2   . LEU A 1 2668 ? 224.910 230.207 242.953 1.00 11.12  ? 2668 LEU A CD2   1 
ATOM   8857  N  N     . PRO A 1 2669 ? 222.418 233.119 239.439 1.00 9.56   ? 2669 PRO A N     1 
ATOM   8858  C  CA    . PRO A 1 2669 ? 221.486 232.792 238.351 1.00 8.31   ? 2669 PRO A CA    1 
ATOM   8859  C  C     . PRO A 1 2669 ? 222.181 232.172 237.148 1.00 9.62   ? 2669 PRO A C     1 
ATOM   8860  O  O     . PRO A 1 2669 ? 223.265 232.594 236.739 1.00 15.63  ? 2669 PRO A O     1 
ATOM   8861  C  CB    . PRO A 1 2669 ? 220.868 234.148 238.004 1.00 8.21   ? 2669 PRO A CB    1 
ATOM   8862  C  CG    . PRO A 1 2669 ? 220.857 234.860 239.284 1.00 13.12  ? 2669 PRO A CG    1 
ATOM   8863  C  CD    . PRO A 1 2669 ? 222.114 234.451 239.998 1.00 11.14  ? 2669 PRO A CD    1 
ATOM   8864  N  N     . ASP A 1 2670 ? 221.540 231.149 236.590 1.00 9.55   ? 2670 ASP A N     1 
ATOM   8865  C  CA    . ASP A 1 2670 ? 222.146 230.355 235.533 1.00 12.15  ? 2670 ASP A CA    1 
ATOM   8866  C  C     . ASP A 1 2670 ? 222.304 231.164 234.254 1.00 15.12  ? 2670 ASP A C     1 
ATOM   8867  O  O     . ASP A 1 2670 ? 221.413 231.921 233.860 1.00 13.43  ? 2670 ASP A O     1 
ATOM   8868  C  CB    . ASP A 1 2670 ? 221.299 229.115 235.254 1.00 14.45  ? 2670 ASP A CB    1 
ATOM   8869  C  CG    . ASP A 1 2670 ? 221.740 227.913 236.058 1.00 30.59  ? 2670 ASP A CG    1 
ATOM   8870  O  OD1   . ASP A 1 2670 ? 222.952 227.791 236.333 1.00 31.26  ? 2670 ASP A OD1   1 
ATOM   8871  O  OD2   . ASP A 1 2670 ? 220.873 227.085 236.410 1.00 35.72  ? 2670 ASP A OD2   1 
ATOM   8872  N  N     . MET A 1 2671 ? 223.450 230.996 233.604 1.00 13.20  ? 2671 MET A N     1 
ATOM   8873  C  CA    . MET A 1 2671 ? 223.638 231.512 232.259 1.00 9.63   ? 2671 MET A CA    1 
ATOM   8874  C  C     . MET A 1 2671 ? 223.062 230.530 231.251 1.00 9.37   ? 2671 MET A C     1 
ATOM   8875  O  O     . MET A 1 2671 ? 223.185 229.312 231.409 1.00 13.30  ? 2671 MET A O     1 
ATOM   8876  C  CB    . MET A 1 2671 ? 225.121 231.744 231.970 1.00 8.37   ? 2671 MET A CB    1 
ATOM   8877  C  CG    . MET A 1 2671 ? 225.737 232.893 232.736 1.00 10.52  ? 2671 MET A CG    1 
ATOM   8878  S  SD    . MET A 1 2671 ? 227.278 233.459 232.002 1.00 24.07  ? 2671 MET A SD    1 
ATOM   8879  C  CE    . MET A 1 2671 ? 227.522 234.994 232.885 1.00 15.42  ? 2671 MET A CE    1 
ATOM   8880  N  N     . ASP A 1 2672 ? 222.428 231.063 230.211 1.00 8.78   ? 2672 ASP A N     1 
ATOM   8881  C  CA    . ASP A 1 2672 ? 221.964 230.221 229.123 1.00 9.03   ? 2672 ASP A CA    1 
ATOM   8882  C  C     . ASP A 1 2672 ? 223.163 229.728 228.314 1.00 11.42  ? 2672 ASP A C     1 
ATOM   8883  O  O     . ASP A 1 2672 ? 224.323 230.016 228.626 1.00 11.78  ? 2672 ASP A O     1 
ATOM   8884  C  CB    . ASP A 1 2672 ? 220.970 230.982 228.250 1.00 10.36  ? 2672 ASP A CB    1 
ATOM   8885  C  CG    . ASP A 1 2672 ? 221.531 232.290 227.727 1.00 10.75  ? 2672 ASP A CG    1 
ATOM   8886  O  OD1   . ASP A 1 2672 ? 222.577 232.739 228.236 1.00 10.77  ? 2672 ASP A OD1   1 
ATOM   8887  O  OD2   . ASP A 1 2672 ? 220.922 232.871 226.808 1.00 15.77  ? 2672 ASP A OD2   1 
ATOM   8888  N  N     . LYS A 1 2673 ? 222.886 228.977 227.250 1.00 10.79  ? 2673 LYS A N     1 
ATOM   8889  C  CA    . LYS A 1 2673 ? 223.975 228.476 226.419 1.00 12.12  ? 2673 LYS A CA    1 
ATOM   8890  C  C     . LYS A 1 2673 ? 224.675 229.577 225.634 1.00 10.50  ? 2673 LYS A C     1 
ATOM   8891  O  O     . LYS A 1 2673 ? 225.585 229.273 224.855 1.00 11.25  ? 2673 LYS A O     1 
ATOM   8892  C  CB    . LYS A 1 2673 ? 223.459 227.399 225.464 1.00 14.95  ? 2673 LYS A CB    1 
ATOM   8893  C  CG    . LYS A 1 2673 ? 222.501 227.906 224.411 1.00 12.38  ? 2673 LYS A CG    1 
ATOM   8894  C  CD    . LYS A 1 2673 ? 222.116 226.809 223.435 1.00 15.70  ? 2673 LYS A CD    1 
ATOM   8895  C  CE    . LYS A 1 2673 ? 221.092 225.865 224.034 1.00 17.50  ? 2673 LYS A CE    1 
ATOM   8896  N  NZ    . LYS A 1 2673 ? 219.773 226.530 224.219 1.00 24.41  ? 2673 LYS A NZ    1 
ATOM   8897  N  N     . TYR A 1 2674 ? 224.279 230.839 225.818 1.00 11.55  ? 2674 TYR A N     1 
ATOM   8898  C  CA    . TYR A 1 2674 ? 224.909 231.971 225.151 1.00 8.95   ? 2674 TYR A CA    1 
ATOM   8899  C  C     . TYR A 1 2674 ? 225.499 232.966 226.145 1.00 11.16  ? 2674 TYR A C     1 
ATOM   8900  O  O     . TYR A 1 2674 ? 225.718 234.129 225.796 1.00 13.68  ? 2674 TYR A O     1 
ATOM   8901  C  CB    . TYR A 1 2674 ? 223.905 232.666 224.232 1.00 7.56   ? 2674 TYR A CB    1 
ATOM   8902  C  CG    . TYR A 1 2674 ? 223.160 231.716 223.328 1.00 10.26  ? 2674 TYR A CG    1 
ATOM   8903  C  CD1   . TYR A 1 2674 ? 223.782 231.142 222.230 1.00 11.85  ? 2674 TYR A CD1   1 
ATOM   8904  C  CD2   . TYR A 1 2674 ? 221.833 231.391 223.572 1.00 8.83   ? 2674 TYR A CD2   1 
ATOM   8905  C  CE1   . TYR A 1 2674 ? 223.105 230.272 221.400 1.00 11.72  ? 2674 TYR A CE1   1 
ATOM   8906  C  CE2   . TYR A 1 2674 ? 221.146 230.529 222.746 1.00 11.53  ? 2674 TYR A CE2   1 
ATOM   8907  C  CZ    . TYR A 1 2674 ? 221.788 229.969 221.663 1.00 15.89  ? 2674 TYR A CZ    1 
ATOM   8908  O  OH    . TYR A 1 2674 ? 221.110 229.103 220.837 1.00 27.79  ? 2674 TYR A OH    1 
ATOM   8909  N  N     . GLY A 1 2675 ? 225.756 232.534 227.376 1.00 11.42  ? 2675 GLY A N     1 
ATOM   8910  C  CA    . GLY A 1 2675 ? 226.429 233.360 228.360 1.00 11.26  ? 2675 GLY A CA    1 
ATOM   8911  C  C     . GLY A 1 2675 ? 225.684 234.608 228.786 1.00 9.42   ? 2675 GLY A C     1 
ATOM   8912  O  O     . GLY A 1 2675 ? 226.272 235.691 228.852 1.00 9.17   ? 2675 GLY A O     1 
ATOM   8913  N  N     . THR A 1 2676 ? 224.394 234.478 229.082 1.00 8.93   ? 2676 THR A N     1 
ATOM   8914  C  CA    . THR A 1 2676 ? 223.591 235.614 229.514 1.00 7.35   ? 2676 THR A CA    1 
ATOM   8915  C  C     . THR A 1 2676 ? 222.709 235.206 230.682 1.00 6.76   ? 2676 THR A C     1 
ATOM   8916  O  O     . THR A 1 2676 ? 222.039 234.171 230.626 1.00 9.35   ? 2676 THR A O     1 
ATOM   8917  C  CB    . THR A 1 2676 ? 222.727 236.151 228.366 1.00 7.06   ? 2676 THR A CB    1 
ATOM   8918  O  OG1   . THR A 1 2676 ? 223.554 236.847 227.429 1.00 12.54  ? 2676 THR A OG1   1 
ATOM   8919  C  CG2   . THR A 1 2676 ? 221.664 237.102 228.890 1.00 5.17   ? 2676 THR A CG2   1 
ATOM   8920  N  N     . GLN A 1 2677 ? 222.718 236.015 231.738 1.00 7.53   ? 2677 GLN A N     1 
ATOM   8921  C  CA    . GLN A 1 2677 ? 221.775 235.886 232.838 1.00 5.66   ? 2677 GLN A CA    1 
ATOM   8922  C  C     . GLN A 1 2677 ? 220.669 236.915 232.642 1.00 5.50   ? 2677 GLN A C     1 
ATOM   8923  O  O     . GLN A 1 2677 ? 220.944 238.118 232.578 1.00 8.93   ? 2677 GLN A O     1 
ATOM   8924  C  CB    . GLN A 1 2677 ? 222.467 236.085 234.185 1.00 4.85   ? 2677 GLN A CB    1 
ATOM   8925  C  CG    . GLN A 1 2677 ? 223.499 235.027 234.508 1.00 7.22   ? 2677 GLN A CG    1 
ATOM   8926  C  CD    . GLN A 1 2677 ? 224.600 235.545 235.403 1.00 9.34   ? 2677 GLN A CD    1 
ATOM   8927  O  OE1   . GLN A 1 2677 ? 225.245 236.547 235.097 1.00 15.17  ? 2677 GLN A OE1   1 
ATOM   8928  N  NE2   . GLN A 1 2677 ? 224.827 234.862 236.519 1.00 8.33   ? 2677 GLN A NE2   1 
ATOM   8929  N  N     . ARG A 1 2678 ? 219.426 236.441 232.545 1.00 4.90   ? 2678 ARG A N     1 
ATOM   8930  C  CA    . ARG A 1 2678 ? 218.316 237.338 232.242 1.00 4.97   ? 2678 ARG A CA    1 
ATOM   8931  C  C     . ARG A 1 2678 ? 218.101 238.363 233.348 1.00 5.61   ? 2678 ARG A C     1 
ATOM   8932  O  O     . ARG A 1 2678 ? 217.852 239.540 233.069 1.00 6.76   ? 2678 ARG A O     1 
ATOM   8933  C  CB    . ARG A 1 2678 ? 217.039 236.533 232.001 1.00 3.95   ? 2678 ARG A CB    1 
ATOM   8934  C  CG    . ARG A 1 2678 ? 215.837 237.389 231.648 1.00 5.10   ? 2678 ARG A CG    1 
ATOM   8935  C  CD    . ARG A 1 2678 ? 214.588 236.553 231.464 1.00 5.45   ? 2678 ARG A CD    1 
ATOM   8936  N  NE    . ARG A 1 2678 ? 214.726 235.611 230.362 1.00 8.66   ? 2678 ARG A NE    1 
ATOM   8937  C  CZ    . ARG A 1 2678 ? 213.851 234.657 230.079 1.00 7.03   ? 2678 ARG A CZ    1 
ATOM   8938  N  NH1   . ARG A 1 2678 ? 212.753 234.493 230.796 1.00 6.64   ? 2678 ARG A NH1   1 
ATOM   8939  N  NH2   . ARG A 1 2678 ? 214.083 233.850 229.049 1.00 5.41   ? 2678 ARG A NH2   1 
ATOM   8940  N  N     . VAL A 1 2679 ? 218.187 237.938 234.610 1.00 5.55   ? 2679 VAL A N     1 
ATOM   8941  C  CA    . VAL A 1 2679 ? 217.963 238.864 235.716 1.00 5.64   ? 2679 VAL A CA    1 
ATOM   8942  C  C     . VAL A 1 2679 ? 219.079 239.902 235.782 1.00 6.49   ? 2679 VAL A C     1 
ATOM   8943  O  O     . VAL A 1 2679 ? 218.843 241.067 236.127 1.00 8.33   ? 2679 VAL A O     1 
ATOM   8944  C  CB    . VAL A 1 2679 ? 217.810 238.091 237.041 1.00 5.71   ? 2679 VAL A CB    1 
ATOM   8945  C  CG1   . VAL A 1 2679 ? 219.033 237.241 237.316 1.00 5.93   ? 2679 VAL A CG1   1 
ATOM   8946  C  CG2   . VAL A 1 2679 ? 217.538 239.044 238.194 1.00 4.62   ? 2679 VAL A CG2   1 
ATOM   8947  N  N     . ILE A 1 2680 ? 220.309 239.504 235.453 1.00 4.42   ? 2680 ILE A N     1 
ATOM   8948  C  CA    . ILE A 1 2680 ? 221.413 240.457 235.433 1.00 4.04   ? 2680 ILE A CA    1 
ATOM   8949  C  C     . ILE A 1 2680 ? 221.195 241.502 234.347 1.00 6.03   ? 2680 ILE A C     1 
ATOM   8950  O  O     . ILE A 1 2680 ? 221.436 242.696 234.560 1.00 7.96   ? 2680 ILE A O     1 
ATOM   8951  C  CB    . ILE A 1 2680 ? 222.751 239.719 235.260 1.00 5.44   ? 2680 ILE A CB    1 
ATOM   8952  C  CG1   . ILE A 1 2680 ? 223.025 238.836 236.476 1.00 8.10   ? 2680 ILE A CG1   1 
ATOM   8953  C  CG2   . ILE A 1 2680 ? 223.887 240.706 235.060 1.00 4.61   ? 2680 ILE A CG2   1 
ATOM   8954  C  CD1   . ILE A 1 2680 ? 223.038 239.592 237.783 1.00 6.93   ? 2680 ILE A CD1   1 
ATOM   8955  N  N     . SER A 1 2681 ? 220.728 241.077 233.171 1.00 6.67   ? 2681 SER A N     1 
ATOM   8956  C  CA    . SER A 1 2681 ? 220.396 242.032 232.118 1.00 4.35   ? 2681 SER A CA    1 
ATOM   8957  C  C     . SER A 1 2681 ? 219.244 242.936 232.537 1.00 5.14   ? 2681 SER A C     1 
ATOM   8958  O  O     . SER A 1 2681 ? 219.230 244.127 232.209 1.00 9.50   ? 2681 SER A O     1 
ATOM   8959  C  CB    . SER A 1 2681 ? 220.053 241.292 230.827 1.00 5.42   ? 2681 SER A CB    1 
ATOM   8960  O  OG    . SER A 1 2681 ? 221.201 240.679 230.271 1.00 11.03  ? 2681 SER A OG    1 
ATOM   8961  N  N     . PHE A 1 2682 ? 218.270 242.386 233.263 1.00 5.48   ? 2682 PHE A N     1 
ATOM   8962  C  CA    . PHE A 1 2682 ? 217.148 243.181 233.751 1.00 5.02   ? 2682 PHE A CA    1 
ATOM   8963  C  C     . PHE A 1 2682 ? 217.626 244.270 234.706 1.00 6.94   ? 2682 PHE A C     1 
ATOM   8964  O  O     . PHE A 1 2682 ? 217.209 245.431 234.612 1.00 5.93   ? 2682 PHE A O     1 
ATOM   8965  C  CB    . PHE A 1 2682 ? 216.139 242.258 234.434 1.00 3.91   ? 2682 PHE A CB    1 
ATOM   8966  C  CG    . PHE A 1 2682 ? 214.843 242.921 234.789 1.00 6.80   ? 2682 PHE A CG    1 
ATOM   8967  C  CD1   . PHE A 1 2682 ? 214.043 243.470 233.804 1.00 6.91   ? 2682 PHE A CD1   1 
ATOM   8968  C  CD2   . PHE A 1 2682 ? 214.418 242.985 236.104 1.00 5.62   ? 2682 PHE A CD2   1 
ATOM   8969  C  CE1   . PHE A 1 2682 ? 212.844 244.072 234.127 1.00 7.59   ? 2682 PHE A CE1   1 
ATOM   8970  C  CE2   . PHE A 1 2682 ? 213.225 243.592 236.432 1.00 5.70   ? 2682 PHE A CE2   1 
ATOM   8971  C  CZ    . PHE A 1 2682 ? 212.437 244.137 235.444 1.00 6.48   ? 2682 PHE A CZ    1 
ATOM   8972  N  N     . ILE A 1 2683 ? 218.517 243.909 235.631 1.00 5.52   ? 2683 ILE A N     1 
ATOM   8973  C  CA    . ILE A 1 2683 ? 219.054 244.883 236.576 1.00 5.17   ? 2683 ILE A CA    1 
ATOM   8974  C  C     . ILE A 1 2683 ? 219.911 245.914 235.854 1.00 5.99   ? 2683 ILE A C     1 
ATOM   8975  O  O     . ILE A 1 2683 ? 219.872 247.109 236.173 1.00 9.49   ? 2683 ILE A O     1 
ATOM   8976  C  CB    . ILE A 1 2683 ? 219.840 244.169 237.691 1.00 7.15   ? 2683 ILE A CB    1 
ATOM   8977  C  CG1   . ILE A 1 2683 ? 218.913 243.259 238.498 1.00 6.46   ? 2683 ILE A CG1   1 
ATOM   8978  C  CG2   . ILE A 1 2683 ? 220.513 245.177 238.608 1.00 4.20   ? 2683 ILE A CG2   1 
ATOM   8979  C  CD1   . ILE A 1 2683 ? 219.625 242.438 239.545 1.00 6.48   ? 2683 ILE A CD1   1 
ATOM   8980  N  N     . ARG A 1 2684 ? 220.698 245.473 234.870 1.00 5.03   ? 2684 ARG A N     1 
ATOM   8981  C  CA    . ARG A 1 2684 ? 221.508 246.406 234.096 1.00 5.85   ? 2684 ARG A CA    1 
ATOM   8982  C  C     . ARG A 1 2684 ? 220.630 247.398 233.348 1.00 7.02   ? 2684 ARG A C     1 
ATOM   8983  O  O     . ARG A 1 2684 ? 220.972 248.581 233.242 1.00 9.53   ? 2684 ARG A O     1 
ATOM   8984  C  CB    . ARG A 1 2684 ? 222.410 245.635 233.133 1.00 5.21   ? 2684 ARG A CB    1 
ATOM   8985  C  CG    . ARG A 1 2684 ? 223.388 246.494 232.352 1.00 4.00   ? 2684 ARG A CG    1 
ATOM   8986  C  CD    . ARG A 1 2684 ? 223.044 246.524 230.878 1.00 5.98   ? 2684 ARG A CD    1 
ATOM   8987  N  NE    . ARG A 1 2684 ? 223.896 247.447 230.141 1.00 8.32   ? 2684 ARG A NE    1 
ATOM   8988  C  CZ    . ARG A 1 2684 ? 223.748 247.743 228.858 1.00 6.23   ? 2684 ARG A CZ    1 
ATOM   8989  N  NH1   . ARG A 1 2684 ? 222.794 247.190 228.129 1.00 6.26   ? 2684 ARG A NH1   1 
ATOM   8990  N  NH2   . ARG A 1 2684 ? 224.580 248.609 228.292 1.00 8.21   ? 2684 ARG A NH2   1 
ATOM   8991  N  N     . GLN A 1 2685 ? 219.499 246.933 232.815 1.00 6.02   ? 2685 GLN A N     1 
ATOM   8992  C  CA    . GLN A 1 2685 ? 218.562 247.845 232.169 1.00 5.85   ? 2685 GLN A CA    1 
ATOM   8993  C  C     . GLN A 1 2685 ? 217.953 248.818 233.172 1.00 7.14   ? 2685 GLN A C     1 
ATOM   8994  O  O     . GLN A 1 2685 ? 217.834 250.014 232.884 1.00 8.22   ? 2685 GLN A O     1 
ATOM   8995  C  CB    . GLN A 1 2685 ? 217.472 247.056 231.449 1.00 5.01   ? 2685 GLN A CB    1 
ATOM   8996  C  CG    . GLN A 1 2685 ? 216.312 247.909 230.970 1.00 4.51   ? 2685 GLN A CG    1 
ATOM   8997  C  CD    . GLN A 1 2685 ? 215.297 247.119 230.179 1.00 5.56   ? 2685 GLN A CD    1 
ATOM   8998  O  OE1   . GLN A 1 2685 ? 214.772 246.113 230.649 1.00 5.35   ? 2685 GLN A OE1   1 
ATOM   8999  N  NE2   . GLN A 1 2685 ? 215.020 247.568 228.962 1.00 7.41   ? 2685 GLN A NE2   1 
ATOM   9000  N  N     . MET A 1 2686 ? 217.559 248.332 234.354 1.00 7.33   ? 2686 MET A N     1 
ATOM   9001  C  CA    . MET A 1 2686 ? 216.976 249.237 235.342 1.00 6.55   ? 2686 MET A CA    1 
ATOM   9002  C  C     . MET A 1 2686 ? 217.982 250.254 235.859 1.00 6.70   ? 2686 MET A C     1 
ATOM   9003  O  O     . MET A 1 2686 ? 217.579 251.328 236.313 1.00 7.63   ? 2686 MET A O     1 
ATOM   9004  C  CB    . MET A 1 2686 ? 216.393 248.477 236.536 1.00 6.00   ? 2686 MET A CB    1 
ATOM   9005  C  CG    . MET A 1 2686 ? 215.189 247.608 236.229 1.00 7.40   ? 2686 MET A CG    1 
ATOM   9006  S  SD    . MET A 1 2686 ? 214.546 246.826 237.722 1.00 23.67  ? 2686 MET A SD    1 
ATOM   9007  C  CE    . MET A 1 2686 ? 215.782 245.572 238.029 1.00 6.13   ? 2686 MET A CE    1 
ATOM   9008  N  N     . VAL A 1 2687 ? 219.271 249.941 235.811 1.00 7.08   ? 2687 VAL A N     1 
ATOM   9009  C  CA    . VAL A 1 2687 ? 220.288 250.858 236.317 1.00 6.64   ? 2687 VAL A CA    1 
ATOM   9010  C  C     . VAL A 1 2687 ? 220.739 251.842 235.246 1.00 9.17   ? 2687 VAL A C     1 
ATOM   9011  O  O     . VAL A 1 2687 ? 220.765 253.053 235.473 1.00 16.38  ? 2687 VAL A O     1 
ATOM   9012  C  CB    . VAL A 1 2687 ? 221.478 250.057 236.886 1.00 6.41   ? 2687 VAL A CB    1 
ATOM   9013  C  CG1   . VAL A 1 2687 ? 222.677 250.965 237.088 1.00 11.05  ? 2687 VAL A CG1   1 
ATOM   9014  C  CG2   . VAL A 1 2687 ? 221.087 249.389 238.193 1.00 6.64   ? 2687 VAL A CG2   1 
ATOM   9015  N  N     . GLU A 1 2688 ? 221.097 251.342 234.061 1.00 9.67   ? 2688 GLU A N     1 
ATOM   9016  C  CA    . GLU A 1 2688 ? 221.669 252.205 233.033 1.00 7.73   ? 2688 GLU A CA    1 
ATOM   9017  C  C     . GLU A 1 2688 ? 220.591 253.043 232.350 1.00 7.36   ? 2688 GLU A C     1 
ATOM   9018  O  O     . GLU A 1 2688 ? 220.831 254.201 231.986 1.00 15.55  ? 2688 GLU A O     1 
ATOM   9019  C  CB    . GLU A 1 2688 ? 222.450 251.356 232.025 1.00 8.30   ? 2688 GLU A CB    1 
ATOM   9020  C  CG    . GLU A 1 2688 ? 223.303 252.135 231.024 1.00 11.12  ? 2688 GLU A CG    1 
ATOM   9021  C  CD    . GLU A 1 2688 ? 222.528 252.619 229.823 1.00 22.45  ? 2688 GLU A CD    1 
ATOM   9022  O  OE1   . GLU A 1 2688 ? 221.543 251.954 229.461 1.00 24.55  ? 2688 GLU A OE1   1 
ATOM   9023  O  OE2   . GLU A 1 2688 ? 222.903 253.660 229.244 1.00 26.26  ? 2688 GLU A OE2   1 
ATOM   9024  N  N     . HIS A 1 2689 ? 219.399 252.479 232.166 1.00 7.02   ? 2689 HIS A N     1 
ATOM   9025  C  CA    . HIS A 1 2689 ? 218.278 253.202 231.574 1.00 7.59   ? 2689 HIS A CA    1 
ATOM   9026  C  C     . HIS A 1 2689 ? 217.298 253.750 232.602 1.00 10.18  ? 2689 HIS A C     1 
ATOM   9027  O  O     . HIS A 1 2689 ? 216.388 254.495 232.228 1.00 13.66  ? 2689 HIS A O     1 
ATOM   9028  C  CB    . HIS A 1 2689 ? 217.531 252.306 230.582 1.00 6.97   ? 2689 HIS A CB    1 
ATOM   9029  C  CG    . HIS A 1 2689 ? 218.363 251.866 229.419 1.00 8.50   ? 2689 HIS A CG    1 
ATOM   9030  N  ND1   . HIS A 1 2689 ? 218.660 250.544 229.173 1.00 9.99   ? 2689 HIS A ND1   1 
ATOM   9031  C  CD2   . HIS A 1 2689 ? 218.939 252.574 228.420 1.00 9.17   ? 2689 HIS A CD2   1 
ATOM   9032  C  CE1   . HIS A 1 2689 ? 219.398 250.457 228.081 1.00 13.64  ? 2689 HIS A CE1   1 
ATOM   9033  N  NE2   . HIS A 1 2689 ? 219.585 251.675 227.607 1.00 10.16  ? 2689 HIS A NE2   1 
ATOM   9034  N  N     . GLY A 1 2690 ? 217.458 253.410 233.877 1.00 8.45   ? 2690 GLY A N     1 
ATOM   9035  C  CA    . GLY A 1 2690 ? 216.567 253.928 234.903 1.00 6.65   ? 2690 GLY A CA    1 
ATOM   9036  C  C     . GLY A 1 2690 ? 215.132 253.466 234.772 1.00 7.30   ? 2690 GLY A C     1 
ATOM   9037  O  O     . GLY A 1 2690 ? 214.206 254.248 235.025 1.00 10.11  ? 2690 GLY A O     1 
ATOM   9038  N  N     . GLY A 1 2691 ? 214.924 252.218 234.391 1.00 7.51   ? 2691 GLY A N     1 
ATOM   9039  C  CA    . GLY A 1 2691 ? 213.582 251.698 234.234 1.00 8.03   ? 2691 GLY A CA    1 
ATOM   9040  C  C     . GLY A 1 2691 ? 213.594 250.400 233.457 1.00 8.35   ? 2691 GLY A C     1 
ATOM   9041  O  O     . GLY A 1 2691 ? 214.642 249.889 233.063 1.00 8.33   ? 2691 GLY A O     1 
ATOM   9042  N  N     . PHE A 1 2692 ? 212.390 249.879 233.241 1.00 8.59   ? 2692 PHE A N     1 
ATOM   9043  C  CA    . PHE A 1 2692 ? 212.213 248.618 232.529 1.00 6.45   ? 2692 PHE A CA    1 
ATOM   9044  C  C     . PHE A 1 2692 ? 210.940 248.703 231.696 1.00 9.13   ? 2692 PHE A C     1 
ATOM   9045  O  O     . PHE A 1 2692 ? 210.353 249.775 231.527 1.00 11.23  ? 2692 PHE A O     1 
ATOM   9046  C  CB    . PHE A 1 2692 ? 212.185 247.434 233.507 1.00 6.11   ? 2692 PHE A CB    1 
ATOM   9047  C  CG    . PHE A 1 2692 ? 211.056 247.486 234.495 1.00 8.04   ? 2692 PHE A CG    1 
ATOM   9048  C  CD1   . PHE A 1 2692 ? 211.183 248.194 235.676 1.00 8.85   ? 2692 PHE A CD1   1 
ATOM   9049  C  CD2   . PHE A 1 2692 ? 209.868 246.823 234.243 1.00 7.24   ? 2692 PHE A CD2   1 
ATOM   9050  C  CE1   . PHE A 1 2692 ? 210.147 248.241 236.584 1.00 11.39  ? 2692 PHE A CE1   1 
ATOM   9051  C  CE2   . PHE A 1 2692 ? 208.830 246.869 235.147 1.00 7.97   ? 2692 PHE A CE2   1 
ATOM   9052  C  CZ    . PHE A 1 2692 ? 208.969 247.579 236.319 1.00 12.27  ? 2692 PHE A CZ    1 
ATOM   9053  N  N     . TYR A 1 2693 ? 210.514 247.561 231.163 1.00 8.73   ? 2693 TYR A N     1 
ATOM   9054  C  CA    . TYR A 1 2693 ? 209.318 247.474 230.334 1.00 8.38   ? 2693 TYR A CA    1 
ATOM   9055  C  C     . TYR A 1 2693 ? 208.301 246.574 231.018 1.00 11.74  ? 2693 TYR A C     1 
ATOM   9056  O  O     . TYR A 1 2693 ? 208.607 245.424 231.347 1.00 15.72  ? 2693 TYR A O     1 
ATOM   9057  C  CB    . TYR A 1 2693 ? 209.653 246.930 228.942 1.00 7.71   ? 2693 TYR A CB    1 
ATOM   9058  C  CG    . TYR A 1 2693 ? 209.961 247.994 227.915 1.00 7.57   ? 2693 TYR A CG    1 
ATOM   9059  C  CD1   . TYR A 1 2693 ? 208.962 248.818 227.420 1.00 7.02   ? 2693 TYR A CD1   1 
ATOM   9060  C  CD2   . TYR A 1 2693 ? 211.250 248.165 227.434 1.00 8.93   ? 2693 TYR A CD2   1 
ATOM   9061  C  CE1   . TYR A 1 2693 ? 209.239 249.787 226.481 1.00 7.10   ? 2693 TYR A CE1   1 
ATOM   9062  C  CE2   . TYR A 1 2693 ? 211.536 249.131 226.492 1.00 6.76   ? 2693 TYR A CE2   1 
ATOM   9063  C  CZ    . TYR A 1 2693 ? 210.529 249.939 226.020 1.00 7.31   ? 2693 TYR A CZ    1 
ATOM   9064  O  OH    . TYR A 1 2693 ? 210.811 250.904 225.082 1.00 18.07  ? 2693 TYR A OH    1 
ATOM   9065  N  N     . ARG A 1 2694 ? 207.098 247.099 231.233 1.00 9.09   ? 2694 ARG A N     1 
ATOM   9066  C  CA    . ARG A 1 2694 ? 205.973 246.291 231.679 1.00 11.68  ? 2694 ARG A CA    1 
ATOM   9067  C  C     . ARG A 1 2694 ? 205.394 245.562 230.475 1.00 15.11  ? 2694 ARG A C     1 
ATOM   9068  O  O     . ARG A 1 2694 ? 204.961 246.200 229.504 1.00 19.66  ? 2694 ARG A O     1 
ATOM   9069  C  CB    . ARG A 1 2694 ? 204.918 247.167 232.347 1.00 18.15  ? 2694 ARG A CB    1 
ATOM   9070  C  CG    . ARG A 1 2694 ? 203.810 246.393 233.038 1.00 18.19  ? 2694 ARG A CG    1 
ATOM   9071  C  CD    . ARG A 1 2694 ? 202.943 247.312 233.880 1.00 20.23  ? 2694 ARG A CD    1 
ATOM   9072  N  NE    . ARG A 1 2694 ? 202.426 248.434 233.108 1.00 19.61  ? 2694 ARG A NE    1 
ATOM   9073  C  CZ    . ARG A 1 2694 ? 201.687 249.413 233.612 1.00 20.92  ? 2694 ARG A CZ    1 
ATOM   9074  N  NH1   . ARG A 1 2694 ? 201.371 249.446 234.896 1.00 15.26  ? 2694 ARG A NH1   1 
ATOM   9075  N  NH2   . ARG A 1 2694 ? 201.255 250.380 232.810 1.00 25.21  ? 2694 ARG A NH2   1 
ATOM   9076  N  N     . THR A 1 2695 ? 205.400 244.231 230.538 1.00 13.86  ? 2695 THR A N     1 
ATOM   9077  C  CA    . THR A 1 2695 ? 204.992 243.388 229.424 1.00 15.19  ? 2695 THR A CA    1 
ATOM   9078  C  C     . THR A 1 2695 ? 203.490 243.153 229.370 1.00 17.67  ? 2695 THR A C     1 
ATOM   9079  O  O     . THR A 1 2695 ? 203.016 242.520 228.421 1.00 26.29  ? 2695 THR A O     1 
ATOM   9080  C  CB    . THR A 1 2695 ? 205.710 242.037 229.495 1.00 13.39  ? 2695 THR A CB    1 
ATOM   9081  O  OG1   . THR A 1 2695 ? 205.360 241.372 230.714 1.00 15.56  ? 2695 THR A OG1   1 
ATOM   9082  C  CG2   . THR A 1 2695 ? 207.217 242.235 229.452 1.00 10.17  ? 2695 THR A CG2   1 
ATOM   9083  N  N     . SER A 1 2696 ? 202.735 243.625 230.363 1.00 18.68  ? 2696 SER A N     1 
ATOM   9084  C  CA    . SER A 1 2696 ? 201.283 243.527 230.281 1.00 17.97  ? 2696 SER A CA    1 
ATOM   9085  C  C     . SER A 1 2696 ? 200.747 244.365 229.129 1.00 20.17  ? 2696 SER A C     1 
ATOM   9086  O  O     . SER A 1 2696 ? 199.841 243.935 228.405 1.00 24.99  ? 2696 SER A O     1 
ATOM   9087  C  CB    . SER A 1 2696 ? 200.651 243.961 231.603 1.00 19.62  ? 2696 SER A CB    1 
ATOM   9088  O  OG    . SER A 1 2696 ? 200.430 245.359 231.629 1.00 19.20  ? 2696 SER A OG    1 
ATOM   9089  N  N     . ASP A 1 2697 ? 201.298 245.566 228.943 1.00 16.65  ? 2697 ASP A N     1 
ATOM   9090  C  CA    . ASP A 1 2697 ? 200.875 246.460 227.875 1.00 17.21  ? 2697 ASP A CA    1 
ATOM   9091  C  C     . ASP A 1 2697 ? 202.051 247.051 227.109 1.00 18.87  ? 2697 ASP A C     1 
ATOM   9092  O  O     . ASP A 1 2697 ? 201.855 247.996 226.336 1.00 19.54  ? 2697 ASP A O     1 
ATOM   9093  C  CB    . ASP A 1 2697 ? 200.001 247.587 228.438 1.00 21.45  ? 2697 ASP A CB    1 
ATOM   9094  C  CG    . ASP A 1 2697 ? 200.728 248.425 229.465 1.00 24.38  ? 2697 ASP A CG    1 
ATOM   9095  O  OD1   . ASP A 1 2697 ? 201.449 247.847 230.305 1.00 23.26  ? 2697 ASP A OD1   1 
ATOM   9096  O  OD2   . ASP A 1 2697 ? 200.575 249.664 229.439 1.00 30.06  ? 2697 ASP A OD2   1 
ATOM   9097  N  N     . GLN A 1 2698 ? 203.261 246.521 227.304 1.00 18.55  ? 2698 GLN A N     1 
ATOM   9098  C  CA    . GLN A 1 2698 ? 204.464 247.002 226.623 1.00 17.34  ? 2698 GLN A CA    1 
ATOM   9099  C  C     . GLN A 1 2698 ? 204.691 248.489 226.889 1.00 14.76  ? 2698 GLN A C     1 
ATOM   9100  O  O     . GLN A 1 2698 ? 204.814 249.297 225.967 1.00 17.40  ? 2698 GLN A O     1 
ATOM   9101  C  CB    . GLN A 1 2698 ? 204.400 246.724 225.117 1.00 14.15  ? 2698 GLN A CB    1 
ATOM   9102  C  CG    . GLN A 1 2698 ? 204.583 245.270 224.720 1.00 11.57  ? 2698 GLN A CG    1 
ATOM   9103  C  CD    . GLN A 1 2698 ? 203.412 244.396 225.113 1.00 14.72  ? 2698 GLN A CD    1 
ATOM   9104  O  OE1   . GLN A 1 2698 ? 203.563 243.445 225.876 1.00 21.46  ? 2698 GLN A OE1   1 
ATOM   9105  N  NE2   . GLN A 1 2698 ? 202.235 244.710 224.588 1.00 16.90  ? 2698 GLN A NE2   1 
ATOM   9106  N  N     . THR A 1 2699 ? 204.748 248.852 228.167 1.00 14.96  ? 2699 THR A N     1 
ATOM   9107  C  CA    . THR A 1 2699 ? 204.868 250.250 228.566 1.00 14.73  ? 2699 THR A CA    1 
ATOM   9108  C  C     . THR A 1 2699 ? 206.169 250.467 229.323 1.00 15.00  ? 2699 THR A C     1 
ATOM   9109  O  O     . THR A 1 2699 ? 206.502 249.694 230.224 1.00 17.27  ? 2699 THR A O     1 
ATOM   9110  C  CB    . THR A 1 2699 ? 203.676 250.679 229.427 1.00 18.03  ? 2699 THR A CB    1 
ATOM   9111  O  OG1   . THR A 1 2699 ? 202.493 250.715 228.622 1.00 27.45  ? 2699 THR A OG1   1 
ATOM   9112  C  CG2   . THR A 1 2699 ? 203.909 252.058 230.019 1.00 16.81  ? 2699 THR A CG2   1 
ATOM   9113  N  N     . TRP A 1 2700 ? 206.902 251.515 228.960 1.00 10.00  ? 2700 TRP A N     1 
ATOM   9114  C  CA    . TRP A 1 2700 ? 208.129 251.844 229.673 1.00 8.78   ? 2700 TRP A CA    1 
ATOM   9115  C  C     . TRP A 1 2700 ? 207.792 252.381 231.060 1.00 13.60  ? 2700 TRP A C     1 
ATOM   9116  O  O     . TRP A 1 2700 ? 207.069 253.375 231.191 1.00 15.44  ? 2700 TRP A O     1 
ATOM   9117  C  CB    . TRP A 1 2700 ? 208.949 252.863 228.888 1.00 9.42   ? 2700 TRP A CB    1 
ATOM   9118  C  CG    . TRP A 1 2700 ? 210.193 253.283 229.602 1.00 7.55   ? 2700 TRP A CG    1 
ATOM   9119  C  CD1   . TRP A 1 2700 ? 210.398 254.450 230.275 1.00 8.99   ? 2700 TRP A CD1   1 
ATOM   9120  C  CD2   . TRP A 1 2700 ? 211.406 252.531 229.724 1.00 8.39   ? 2700 TRP A CD2   1 
ATOM   9121  N  NE1   . TRP A 1 2700 ? 211.664 254.475 230.805 1.00 11.55  ? 2700 TRP A NE1   1 
ATOM   9122  C  CE2   . TRP A 1 2700 ? 212.304 253.308 230.481 1.00 11.84  ? 2700 TRP A CE2   1 
ATOM   9123  C  CE3   . TRP A 1 2700 ? 211.821 251.279 229.263 1.00 6.01   ? 2700 TRP A CE3   1 
ATOM   9124  C  CZ2   . TRP A 1 2700 ? 213.590 252.874 230.787 1.00 8.44   ? 2700 TRP A CZ2   1 
ATOM   9125  C  CZ3   . TRP A 1 2700 ? 213.096 250.850 229.571 1.00 6.18   ? 2700 TRP A CZ3   1 
ATOM   9126  C  CH2   . TRP A 1 2700 ? 213.965 251.645 230.324 1.00 7.48   ? 2700 TRP A CH2   1 
ATOM   9127  N  N     . VAL A 1 2701 ? 208.316 251.727 232.091 1.00 12.46  ? 2701 VAL A N     1 
ATOM   9128  C  CA    . VAL A 1 2701 ? 208.122 252.127 233.478 1.00 11.05  ? 2701 VAL A CA    1 
ATOM   9129  C  C     . VAL A 1 2701 ? 209.447 252.667 233.994 1.00 12.98  ? 2701 VAL A C     1 
ATOM   9130  O  O     . VAL A 1 2701 ? 210.482 251.997 233.890 1.00 13.40  ? 2701 VAL A O     1 
ATOM   9131  C  CB    . VAL A 1 2701 ? 207.631 250.959 234.345 1.00 11.38  ? 2701 VAL A CB    1 
ATOM   9132  C  CG1   . VAL A 1 2701 ? 207.122 251.471 235.676 1.00 13.12  ? 2701 VAL A CG1   1 
ATOM   9133  C  CG2   . VAL A 1 2701 ? 206.548 250.182 233.620 1.00 14.56  ? 2701 VAL A CG2   1 
ATOM   9134  N  N     . LYS A 1 2702 ? 209.413 253.877 234.543 1.00 11.28  ? 2702 LYS A N     1 
ATOM   9135  C  CA    . LYS A 1 2702 ? 210.598 254.535 235.077 1.00 11.08  ? 2702 LYS A CA    1 
ATOM   9136  C  C     . LYS A 1 2702 ? 210.656 254.340 236.586 1.00 12.54  ? 2702 LYS A C     1 
ATOM   9137  O  O     . LYS A 1 2702 ? 209.661 254.563 237.283 1.00 16.83  ? 2702 LYS A O     1 
ATOM   9138  C  CB    . LYS A 1 2702 ? 210.590 256.025 234.733 1.00 11.96  ? 2702 LYS A CB    1 
ATOM   9139  C  CG    . LYS A 1 2702 ? 211.809 256.781 235.222 1.00 13.95  ? 2702 LYS A CG    1 
ATOM   9140  C  CD    . LYS A 1 2702 ? 211.798 258.214 234.726 1.00 20.24  ? 2702 LYS A CD    1 
ATOM   9141  C  CE    . LYS A 1 2702 ? 210.728 259.030 235.432 1.00 25.95  ? 2702 LYS A CE    1 
ATOM   9142  N  NZ    . LYS A 1 2702 ? 211.045 259.236 236.870 1.00 22.96  ? 2702 LYS A NZ    1 
ATOM   9143  N  N     . LEU A 1 2703 ? 211.815 253.921 237.082 1.00 10.23  ? 2703 LEU A N     1 
ATOM   9144  C  CA    . LEU A 1 2703 ? 211.994 253.701 238.509 1.00 10.37  ? 2703 LEU A CA    1 
ATOM   9145  C  C     . LEU A 1 2703 ? 212.190 255.023 239.237 1.00 14.32  ? 2703 LEU A C     1 
ATOM   9146  O  O     . LEU A 1 2703 ? 212.874 255.925 238.744 1.00 15.34  ? 2703 LEU A O     1 
ATOM   9147  C  CB    . LEU A 1 2703 ? 213.196 252.791 238.763 1.00 9.99   ? 2703 LEU A CB    1 
ATOM   9148  C  CG    . LEU A 1 2703 ? 213.110 251.355 238.248 1.00 9.20   ? 2703 LEU A CG    1 
ATOM   9149  C  CD1   . LEU A 1 2703 ? 214.177 250.502 238.903 1.00 9.40   ? 2703 LEU A CD1   1 
ATOM   9150  C  CD2   . LEU A 1 2703 ? 211.733 250.780 238.510 1.00 13.23  ? 2703 LEU A CD2   1 
ATOM   9151  N  N     . GLU A 1 2704 ? 211.587 255.136 240.419 1.00 14.55  ? 2704 GLU A N     1 
ATOM   9152  C  CA    . GLU A 1 2704 ? 211.790 256.296 241.275 1.00 16.59  ? 2704 GLU A CA    1 
ATOM   9153  C  C     . GLU A 1 2704 ? 212.037 255.818 242.696 1.00 16.14  ? 2704 GLU A C     1 
ATOM   9154  O  O     . GLU A 1 2704 ? 211.326 254.936 243.186 1.00 23.98  ? 2704 GLU A O     1 
ATOM   9155  C  CB    . GLU A 1 2704 ? 210.585 257.241 241.236 1.00 18.85  ? 2704 GLU A CB    1 
ATOM   9156  C  CG    . GLU A 1 2704 ? 210.780 258.523 242.030 1.00 27.74  ? 2704 GLU A CG    1 
ATOM   9157  C  CD    . GLU A 1 2704 ? 209.472 259.128 242.502 1.00 44.60  ? 2704 GLU A CD    1 
ATOM   9158  O  OE1   . GLU A 1 2704 ? 209.255 259.196 243.730 1.00 41.12  ? 2704 GLU A OE1   1 
ATOM   9159  O  OE2   . GLU A 1 2704 ? 208.660 259.536 241.645 1.00 47.44  ? 2704 GLU A OE2   1 
ATOM   9160  N  N     . ARG A 1 2705 ? 213.049 256.397 243.346 1.00 11.38  ? 2705 ARG A N     1 
ATOM   9161  C  CA    . ARG A 1 2705 ? 213.381 256.092 244.739 1.00 11.66  ? 2705 ARG A CA    1 
ATOM   9162  C  C     . ARG A 1 2705 ? 213.642 254.601 244.943 1.00 13.36  ? 2705 ARG A C     1 
ATOM   9163  O  O     . ARG A 1 2705 ? 213.277 254.023 245.968 1.00 15.80  ? 2705 ARG A O     1 
ATOM   9164  C  CB    . ARG A 1 2705 ? 212.288 256.587 245.688 1.00 13.15  ? 2705 ARG A CB    1 
ATOM   9165  C  CG    . ARG A 1 2705 ? 212.335 258.079 245.962 1.00 10.42  ? 2705 ARG A CG    1 
ATOM   9166  C  CD    . ARG A 1 2705 ? 211.261 258.498 246.951 1.00 11.30  ? 2705 ARG A CD    1 
ATOM   9167  N  NE    . ARG A 1 2705 ? 209.920 258.209 246.460 1.00 18.58  ? 2705 ARG A NE    1 
ATOM   9168  C  CZ    . ARG A 1 2705 ? 209.073 257.372 247.044 1.00 21.60  ? 2705 ARG A CZ    1 
ATOM   9169  N  NH1   . ARG A 1 2705 ? 209.393 256.725 248.152 1.00 17.97  ? 2705 ARG A NH1   1 
ATOM   9170  N  NH2   . ARG A 1 2705 ? 207.874 257.180 246.502 1.00 24.11  ? 2705 ARG A NH2   1 
ATOM   9171  N  N     . ILE A 1 2706 ? 214.283 253.972 243.960 1.00 14.14  ? 2706 ILE A N     1 
ATOM   9172  C  CA    . ILE A 1 2706 ? 214.632 252.558 244.017 1.00 10.71  ? 2706 ILE A CA    1 
ATOM   9173  C  C     . ILE A 1 2706 ? 216.101 252.410 243.650 1.00 13.83  ? 2706 ILE A C     1 
ATOM   9174  O  O     . ILE A 1 2706 ? 216.537 252.907 242.606 1.00 17.62  ? 2706 ILE A O     1 
ATOM   9175  C  CB    . ILE A 1 2706 ? 213.754 251.710 243.076 1.00 10.80  ? 2706 ILE A CB    1 
ATOM   9176  C  CG1   . ILE A 1 2706 ? 212.316 251.647 243.595 1.00 10.84  ? 2706 ILE A CG1   1 
ATOM   9177  C  CG2   . ILE A 1 2706 ? 214.328 250.312 242.927 1.00 9.27   ? 2706 ILE A CG2   1 
ATOM   9178  C  CD1   . ILE A 1 2706 ? 211.330 251.107 242.588 1.00 10.80  ? 2706 ILE A CD1   1 
ATOM   9179  N  N     . GLN A 1 2707 ? 216.860 251.729 244.504 1.00 11.80  ? 2707 GLN A N     1 
ATOM   9180  C  CA    . GLN A 1 2707 ? 218.259 251.434 244.248 1.00 8.32   ? 2707 GLN A CA    1 
ATOM   9181  C  C     . GLN A 1 2707 ? 218.534 249.978 244.593 1.00 8.28   ? 2707 GLN A C     1 
ATOM   9182  O  O     . GLN A 1 2707 ? 217.799 249.350 245.359 1.00 9.11   ? 2707 GLN A O     1 
ATOM   9183  C  CB    . GLN A 1 2707 ? 219.186 252.359 245.045 1.00 8.29   ? 2707 GLN A CB    1 
ATOM   9184  C  CG    . GLN A 1 2707 ? 218.899 252.394 246.531 1.00 10.29  ? 2707 GLN A CG    1 
ATOM   9185  C  CD    . GLN A 1 2707 ? 219.937 253.180 247.299 1.00 11.09  ? 2707 GLN A CD    1 
ATOM   9186  O  OE1   . GLN A 1 2707 ? 219.615 254.158 247.969 1.00 12.98  ? 2707 GLN A OE1   1 
ATOM   9187  N  NE2   . GLN A 1 2707 ? 221.191 252.762 247.199 1.00 13.51  ? 2707 GLN A NE2   1 
ATOM   9188  N  N     . PHE A 1 2708 ? 219.603 249.442 244.014 1.00 7.06   ? 2708 PHE A N     1 
ATOM   9189  C  CA    . PHE A 1 2708 ? 219.931 248.030 244.124 1.00 6.91   ? 2708 PHE A CA    1 
ATOM   9190  C  C     . PHE A 1 2708 ? 221.291 247.842 244.781 1.00 7.76   ? 2708 PHE A C     1 
ATOM   9191  O  O     . PHE A 1 2708 ? 222.242 248.569 244.485 1.00 9.17   ? 2708 PHE A O     1 
ATOM   9192  C  CB    . PHE A 1 2708 ? 219.923 247.351 242.750 1.00 7.58   ? 2708 PHE A CB    1 
ATOM   9193  C  CG    . PHE A 1 2708 ? 218.700 247.649 241.935 1.00 9.47   ? 2708 PHE A CG    1 
ATOM   9194  C  CD1   . PHE A 1 2708 ? 217.559 246.878 242.074 1.00 8.66   ? 2708 PHE A CD1   1 
ATOM   9195  C  CD2   . PHE A 1 2708 ? 218.685 248.702 241.038 1.00 11.03  ? 2708 PHE A CD2   1 
ATOM   9196  C  CE1   . PHE A 1 2708 ? 216.430 247.148 241.331 1.00 12.11  ? 2708 PHE A CE1   1 
ATOM   9197  C  CE2   . PHE A 1 2708 ? 217.559 248.978 240.293 1.00 9.40   ? 2708 PHE A CE2   1 
ATOM   9198  C  CZ    . PHE A 1 2708 ? 216.430 248.200 240.439 1.00 11.61  ? 2708 PHE A CZ    1 
ATOM   9199  N  N     . VAL A 1 2709 ? 221.365 246.864 245.678 1.00 8.53   ? 2709 VAL A N     1 
ATOM   9200  C  CA    . VAL A 1 2709 ? 222.611 246.425 246.289 1.00 6.22   ? 2709 VAL A CA    1 
ATOM   9201  C  C     . VAL A 1 2709 ? 222.711 244.921 246.091 1.00 9.35   ? 2709 VAL A C     1 
ATOM   9202  O  O     . VAL A 1 2709 ? 221.744 244.195 246.342 1.00 7.16   ? 2709 VAL A O     1 
ATOM   9203  C  CB    . VAL A 1 2709 ? 222.681 246.784 247.786 1.00 6.07   ? 2709 VAL A CB    1 
ATOM   9204  C  CG1   . VAL A 1 2709 ? 223.849 246.076 248.449 1.00 7.32   ? 2709 VAL A CG1   1 
ATOM   9205  C  CG2   . VAL A 1 2709 ? 222.805 248.283 247.963 1.00 9.23   ? 2709 VAL A CG2   1 
ATOM   9206  N  N     . GLY A 1 2710 ? 223.864 244.455 245.628 1.00 7.30   ? 2710 GLY A N     1 
ATOM   9207  C  CA    . GLY A 1 2710 ? 224.088 243.042 245.405 1.00 4.94   ? 2710 GLY A CA    1 
ATOM   9208  C  C     . GLY A 1 2710 ? 225.185 242.514 246.308 1.00 5.83   ? 2710 GLY A C     1 
ATOM   9209  O  O     . GLY A 1 2710 ? 226.096 243.244 246.696 1.00 8.59   ? 2710 GLY A O     1 
ATOM   9210  N  N     . ALA A 1 2711 ? 225.077 241.238 246.654 1.00 8.64   ? 2711 ALA A N     1 
ATOM   9211  C  CA    . ALA A 1 2711 ? 226.127 240.529 247.366 1.00 5.68   ? 2711 ALA A CA    1 
ATOM   9212  C  C     . ALA A 1 2711 ? 226.385 239.215 246.650 1.00 9.33   ? 2711 ALA A C     1 
ATOM   9213  O  O     . ALA A 1 2711 ? 225.482 238.640 246.038 1.00 10.75  ? 2711 ALA A O     1 
ATOM   9214  C  CB    . ALA A 1 2711 ? 225.759 240.269 248.829 1.00 4.34   ? 2711 ALA A CB    1 
ATOM   9215  N  N     . CYS A 1 2712 ? 227.630 238.755 246.707 1.00 7.46   ? 2712 CYS A N     1 
ATOM   9216  C  CA    . CYS A 1 2712 ? 227.968 237.520 246.016 1.00 5.64   ? 2712 CYS A CA    1 
ATOM   9217  C  C     . CYS A 1 2712 ? 229.286 236.975 246.538 1.00 6.40   ? 2712 CYS A C     1 
ATOM   9218  O  O     . CYS A 1 2712 ? 230.105 237.702 247.104 1.00 6.55   ? 2712 CYS A O     1 
ATOM   9219  C  CB    . CYS A 1 2712 ? 228.046 237.731 244.502 1.00 5.89   ? 2712 CYS A CB    1 
ATOM   9220  S  SG    . CYS A 1 2712 ? 229.073 239.120 244.004 1.00 11.03  ? 2712 CYS A SG    1 
ATOM   9221  N  N     . ASN A 1 2713 ? 229.466 235.676 246.345 1.00 6.18   ? 2713 ASN A N     1 
ATOM   9222  C  CA    . ASN A 1 2713 ? 230.745 235.026 246.542 1.00 4.65   ? 2713 ASN A CA    1 
ATOM   9223  C  C     . ASN A 1 2713 ? 231.639 235.285 245.333 1.00 6.24   ? 2713 ASN A C     1 
ATOM   9224  O  O     . ASN A 1 2713 ? 231.154 235.686 244.273 1.00 7.87   ? 2713 ASN A O     1 
ATOM   9225  C  CB    . ASN A 1 2713 ? 230.539 233.529 246.753 1.00 8.27   ? 2713 ASN A CB    1 
ATOM   9226  C  CG    . ASN A 1 2713 ? 229.793 233.219 248.035 1.00 6.83   ? 2713 ASN A CG    1 
ATOM   9227  O  OD1   . ASN A 1 2713 ? 229.456 234.117 248.806 1.00 7.15   ? 2713 ASN A OD1   1 
ATOM   9228  N  ND2   . ASN A 1 2713 ? 229.529 231.941 248.271 1.00 5.66   ? 2713 ASN A ND2   1 
ATOM   9229  N  N     . PRO A 1 2714 ? 232.949 235.086 245.468 1.00 9.37   ? 2714 PRO A N     1 
ATOM   9230  C  CA    . PRO A 1 2714 ? 233.851 235.298 244.331 1.00 8.79   ? 2714 PRO A CA    1 
ATOM   9231  C  C     . PRO A 1 2714 ? 233.445 234.446 243.142 1.00 6.32   ? 2714 PRO A C     1 
ATOM   9232  O  O     . PRO A 1 2714 ? 233.001 233.302 243.310 1.00 7.39   ? 2714 PRO A O     1 
ATOM   9233  C  CB    . PRO A 1 2714 ? 235.218 234.870 244.883 1.00 7.55   ? 2714 PRO A CB    1 
ATOM   9234  C  CG    . PRO A 1 2714 ? 235.116 235.133 246.336 1.00 6.96   ? 2714 PRO A CG    1 
ATOM   9235  C  CD    . PRO A 1 2714 ? 233.694 234.832 246.714 1.00 7.03   ? 2714 PRO A CD    1 
ATOM   9236  N  N     . PRO A 1 2715 ? 233.569 234.978 241.923 1.00 8.42   ? 2715 PRO A N     1 
ATOM   9237  C  CA    . PRO A 1 2715 ? 233.111 234.226 240.742 1.00 7.57   ? 2715 PRO A CA    1 
ATOM   9238  C  C     . PRO A 1 2715 ? 233.866 232.931 240.511 1.00 8.62   ? 2715 PRO A C     1 
ATOM   9239  O  O     . PRO A 1 2715 ? 233.368 232.066 239.781 1.00 11.86  ? 2715 PRO A O     1 
ATOM   9240  C  CB    . PRO A 1 2715 ? 233.325 235.217 239.590 1.00 6.41   ? 2715 PRO A CB    1 
ATOM   9241  C  CG    . PRO A 1 2715 ? 234.358 236.165 240.087 1.00 7.00   ? 2715 PRO A CG    1 
ATOM   9242  C  CD    . PRO A 1 2715 ? 234.133 236.289 241.562 1.00 8.24   ? 2715 PRO A CD    1 
ATOM   9243  N  N     . THR A 1 2716 ? 235.051 232.772 241.098 1.00 7.89   ? 2716 THR A N     1 
ATOM   9244  C  CA    . THR A 1 2716 ? 235.791 231.522 240.996 1.00 8.24   ? 2716 THR A CA    1 
ATOM   9245  C  C     . THR A 1 2716 ? 235.210 230.416 241.865 1.00 8.19   ? 2716 THR A C     1 
ATOM   9246  O  O     . THR A 1 2716 ? 235.607 229.257 241.708 1.00 11.47  ? 2716 THR A O     1 
ATOM   9247  C  CB    . THR A 1 2716 ? 237.257 231.751 241.371 1.00 9.59   ? 2716 THR A CB    1 
ATOM   9248  O  OG1   . THR A 1 2716 ? 237.344 232.136 242.747 1.00 12.21  ? 2716 THR A OG1   1 
ATOM   9249  C  CG2   . THR A 1 2716 ? 237.860 232.844 240.505 1.00 6.44   ? 2716 THR A CG2   1 
ATOM   9250  N  N     . ASP A 1 2717 ? 234.292 230.741 242.770 1.00 8.86   ? 2717 ASP A N     1 
ATOM   9251  C  CA    . ASP A 1 2717 ? 233.678 229.730 243.613 1.00 8.64   ? 2717 ASP A CA    1 
ATOM   9252  C  C     . ASP A 1 2717 ? 232.729 228.861 242.788 1.00 8.61   ? 2717 ASP A C     1 
ATOM   9253  O  O     . ASP A 1 2717 ? 232.155 229.324 241.799 1.00 8.45   ? 2717 ASP A O     1 
ATOM   9254  C  CB    . ASP A 1 2717 ? 232.922 230.387 244.763 1.00 9.63   ? 2717 ASP A CB    1 
ATOM   9255  C  CG    . ASP A 1 2717 ? 233.847 230.919 245.837 1.00 13.28  ? 2717 ASP A CG    1 
ATOM   9256  O  OD1   . ASP A 1 2717 ? 235.074 230.935 245.606 1.00 11.13  ? 2717 ASP A OD1   1 
ATOM   9257  O  OD2   . ASP A 1 2717 ? 233.349 231.320 246.909 1.00 15.40  ? 2717 ASP A OD2   1 
ATOM   9258  N  N     . PRO A 1 2718 ? 232.555 227.594 243.168 1.00 11.29  ? 2718 PRO A N     1 
ATOM   9259  C  CA    . PRO A 1 2718 ? 231.681 226.709 242.388 1.00 8.15   ? 2718 PRO A CA    1 
ATOM   9260  C  C     . PRO A 1 2718 ? 230.243 227.203 242.384 1.00 7.10   ? 2718 PRO A C     1 
ATOM   9261  O  O     . PRO A 1 2718 ? 229.716 227.658 243.400 1.00 9.21   ? 2718 PRO A O     1 
ATOM   9262  C  CB    . PRO A 1 2718 ? 231.813 225.358 243.101 1.00 6.55   ? 2718 PRO A CB    1 
ATOM   9263  C  CG    . PRO A 1 2718 ? 232.310 225.686 244.463 1.00 9.54   ? 2718 PRO A CG    1 
ATOM   9264  C  CD    . PRO A 1 2718 ? 233.166 226.901 244.314 1.00 12.46  ? 2718 PRO A CD    1 
ATOM   9265  N  N     . GLY A 1 2719 ? 229.607 227.102 241.219 1.00 7.31   ? 2719 GLY A N     1 
ATOM   9266  C  CA    . GLY A 1 2719 ? 228.246 227.558 241.045 1.00 6.71   ? 2719 GLY A CA    1 
ATOM   9267  C  C     . GLY A 1 2719 ? 228.093 229.038 240.781 1.00 8.41   ? 2719 GLY A C     1 
ATOM   9268  O  O     . GLY A 1 2719 ? 226.964 229.496 240.566 1.00 10.77  ? 2719 GLY A O     1 
ATOM   9269  N  N     . ARG A 1 2720 ? 229.183 229.799 240.781 1.00 8.58   ? 2720 ARG A N     1 
ATOM   9270  C  CA    . ARG A 1 2720 ? 229.144 231.243 240.594 1.00 7.57   ? 2720 ARG A CA    1 
ATOM   9271  C  C     . ARG A 1 2720 ? 229.684 231.588 239.214 1.00 7.18   ? 2720 ARG A C     1 
ATOM   9272  O  O     . ARG A 1 2720 ? 230.712 231.048 238.793 1.00 9.46   ? 2720 ARG A O     1 
ATOM   9273  C  CB    . ARG A 1 2720 ? 229.958 231.959 241.674 1.00 8.06   ? 2720 ARG A CB    1 
ATOM   9274  C  CG    . ARG A 1 2720 ? 229.680 231.484 243.091 1.00 6.84   ? 2720 ARG A CG    1 
ATOM   9275  C  CD    . ARG A 1 2720 ? 228.210 231.607 243.439 1.00 7.92   ? 2720 ARG A CD    1 
ATOM   9276  N  NE    . ARG A 1 2720 ? 227.958 231.379 244.856 1.00 15.83  ? 2720 ARG A NE    1 
ATOM   9277  C  CZ    . ARG A 1 2720 ? 227.862 230.183 245.420 1.00 10.11  ? 2720 ARG A CZ    1 
ATOM   9278  N  NH1   . ARG A 1 2720 ? 228.001 229.072 244.716 1.00 6.79   ? 2720 ARG A NH1   1 
ATOM   9279  N  NH2   . ARG A 1 2720 ? 227.621 230.098 246.725 1.00 7.96   ? 2720 ARG A NH2   1 
ATOM   9280  N  N     . LYS A 1 2721 ? 228.990 232.482 238.515 1.00 6.26   ? 2721 LYS A N     1 
ATOM   9281  C  CA    . LYS A 1 2721 ? 229.392 232.899 237.184 1.00 7.32   ? 2721 LYS A CA    1 
ATOM   9282  C  C     . LYS A 1 2721 ? 229.900 234.335 237.203 1.00 8.67   ? 2721 LYS A C     1 
ATOM   9283  O  O     . LYS A 1 2721 ? 229.392 235.159 237.971 1.00 8.89   ? 2721 LYS A O     1 
ATOM   9284  C  CB    . LYS A 1 2721 ? 228.223 232.790 236.197 1.00 7.73   ? 2721 LYS A CB    1 
ATOM   9285  C  CG    . LYS A 1 2721 ? 228.061 231.420 235.567 1.00 9.82   ? 2721 LYS A CG    1 
ATOM   9286  C  CD    . LYS A 1 2721 ? 227.404 230.440 236.523 1.00 10.81  ? 2721 LYS A CD    1 
ATOM   9287  C  CE    . LYS A 1 2721 ? 226.076 230.966 237.032 1.00 9.72   ? 2721 LYS A CE    1 
ATOM   9288  N  NZ    . LYS A 1 2721 ? 225.427 230.005 237.964 1.00 10.33  ? 2721 LYS A NZ    1 
ATOM   9289  N  N     . PRO A 1 2722 ? 230.900 234.661 236.386 1.00 7.33   ? 2722 PRO A N     1 
ATOM   9290  C  CA    . PRO A 1 2722 ? 231.362 236.052 236.313 1.00 6.43   ? 2722 PRO A CA    1 
ATOM   9291  C  C     . PRO A 1 2722 ? 230.268 236.972 235.796 1.00 8.14   ? 2722 PRO A C     1 
ATOM   9292  O  O     . PRO A 1 2722 ? 229.483 236.606 234.919 1.00 7.45   ? 2722 PRO A O     1 
ATOM   9293  C  CB    . PRO A 1 2722 ? 232.550 235.983 235.347 1.00 4.12   ? 2722 PRO A CB    1 
ATOM   9294  C  CG    . PRO A 1 2722 ? 232.337 234.736 234.566 1.00 6.43   ? 2722 PRO A CG    1 
ATOM   9295  C  CD    . PRO A 1 2722 ? 231.665 233.776 235.494 1.00 6.60   ? 2722 PRO A CD    1 
ATOM   9296  N  N     . LEU A 1 2723 ? 230.222 238.178 236.349 1.00 6.10   ? 2723 LEU A N     1 
ATOM   9297  C  CA    . LEU A 1 2723 ? 229.205 239.145 235.972 1.00 4.48   ? 2723 LEU A CA    1 
ATOM   9298  C  C     . LEU A 1 2723 ? 229.561 239.809 234.648 1.00 5.87   ? 2723 LEU A C     1 
ATOM   9299  O  O     . LEU A 1 2723 ? 230.732 239.917 234.276 1.00 13.18  ? 2723 LEU A O     1 
ATOM   9300  C  CB    . LEU A 1 2723 ? 229.039 240.200 237.064 1.00 5.94   ? 2723 LEU A CB    1 
ATOM   9301  C  CG    . LEU A 1 2723 ? 228.314 239.731 238.328 1.00 6.08   ? 2723 LEU A CG    1 
ATOM   9302  C  CD1   . LEU A 1 2723 ? 228.497 240.724 239.464 1.00 6.24   ? 2723 LEU A CD1   1 
ATOM   9303  C  CD2   . LEU A 1 2723 ? 226.839 239.504 238.044 1.00 5.22   ? 2723 LEU A CD2   1 
ATOM   9304  N  N     . SER A 1 2724 ? 228.528 240.248 233.932 1.00 4.42   ? 2724 SER A N     1 
ATOM   9305  C  CA    . SER A 1 2724 ? 228.731 240.907 232.649 1.00 3.69   ? 2724 SER A CA    1 
ATOM   9306  C  C     . SER A 1 2724 ? 229.474 242.224 232.832 1.00 5.56   ? 2724 SER A C     1 
ATOM   9307  O  O     . SER A 1 2724 ? 229.292 242.936 233.823 1.00 6.33   ? 2724 SER A O     1 
ATOM   9308  C  CB    . SER A 1 2724 ? 227.388 241.152 231.962 1.00 4.53   ? 2724 SER A CB    1 
ATOM   9309  O  OG    . SER A 1 2724 ? 227.554 241.876 230.755 1.00 5.62   ? 2724 SER A OG    1 
ATOM   9310  N  N     . HIS A 1 2725 ? 230.328 242.545 231.857 1.00 5.25   ? 2725 HIS A N     1 
ATOM   9311  C  CA    . HIS A 1 2725 ? 231.087 243.787 231.925 1.00 5.92   ? 2725 HIS A CA    1 
ATOM   9312  C  C     . HIS A 1 2725 ? 230.181 245.004 231.788 1.00 5.69   ? 2725 HIS A C     1 
ATOM   9313  O  O     . HIS A 1 2725 ? 230.461 246.053 232.379 1.00 6.51   ? 2725 HIS A O     1 
ATOM   9314  C  CB    . HIS A 1 2725 ? 232.167 243.801 230.846 1.00 9.01   ? 2725 HIS A CB    1 
ATOM   9315  C  CG    . HIS A 1 2725 ? 233.405 243.049 231.226 1.00 8.69   ? 2725 HIS A CG    1 
ATOM   9316  N  ND1   . HIS A 1 2725 ? 234.510 242.971 230.406 1.00 16.17  ? 2725 HIS A ND1   1 
ATOM   9317  C  CD2   . HIS A 1 2725 ? 233.706 242.330 232.332 1.00 9.06   ? 2725 HIS A CD2   1 
ATOM   9318  C  CE1   . HIS A 1 2725 ? 235.441 242.243 230.995 1.00 13.71  ? 2725 HIS A CE1   1 
ATOM   9319  N  NE2   . HIS A 1 2725 ? 234.979 241.841 232.165 1.00 12.07  ? 2725 HIS A NE2   1 
ATOM   9320  N  N     . ARG A 1 2726 ? 229.102 244.890 231.012 1.00 5.09   ? 2726 ARG A N     1 
ATOM   9321  C  CA    . ARG A 1 2726 ? 228.143 245.982 230.905 1.00 3.76   ? 2726 ARG A CA    1 
ATOM   9322  C  C     . ARG A 1 2726 ? 227.356 246.183 232.191 1.00 5.50   ? 2726 ARG A C     1 
ATOM   9323  O  O     . ARG A 1 2726 ? 226.839 247.281 232.421 1.00 9.90   ? 2726 ARG A O     1 
ATOM   9324  C  CB    . ARG A 1 2726 ? 227.194 245.734 229.733 1.00 3.48   ? 2726 ARG A CB    1 
ATOM   9325  C  CG    . ARG A 1 2726 ? 227.910 245.503 228.412 1.00 3.81   ? 2726 ARG A CG    1 
ATOM   9326  C  CD    . ARG A 1 2726 ? 226.939 245.249 227.280 1.00 4.06   ? 2726 ARG A CD    1 
ATOM   9327  N  NE    . ARG A 1 2726 ? 226.616 246.470 226.552 1.00 4.55   ? 2726 ARG A NE    1 
ATOM   9328  C  CZ    . ARG A 1 2726 ? 225.754 246.536 225.549 1.00 3.83   ? 2726 ARG A CZ    1 
ATOM   9329  N  NH1   . ARG A 1 2726 ? 225.113 245.465 225.115 1.00 4.94   ? 2726 ARG A NH1   1 
ATOM   9330  N  NH2   . ARG A 1 2726 ? 225.530 247.709 224.963 1.00 3.49   ? 2726 ARG A NH2   1 
ATOM   9331  N  N     . PHE A 1 2727 ? 227.248 245.151 233.031 1.00 4.66   ? 2727 PHE A N     1 
ATOM   9332  C  CA    . PHE A 1 2727 ? 226.626 245.320 234.338 1.00 3.65   ? 2727 PHE A CA    1 
ATOM   9333  C  C     . PHE A 1 2727 ? 227.620 245.851 235.362 1.00 5.29   ? 2727 PHE A C     1 
ATOM   9334  O  O     . PHE A 1 2727 ? 227.285 246.742 236.151 1.00 5.04   ? 2727 PHE A O     1 
ATOM   9335  C  CB    . PHE A 1 2727 ? 226.030 243.993 234.813 1.00 4.14   ? 2727 PHE A CB    1 
ATOM   9336  C  CG    . PHE A 1 2727 ? 225.581 244.010 236.246 1.00 5.90   ? 2727 PHE A CG    1 
ATOM   9337  C  CD1   . PHE A 1 2727 ? 224.386 244.610 236.603 1.00 6.43   ? 2727 PHE A CD1   1 
ATOM   9338  C  CD2   . PHE A 1 2727 ? 226.352 243.428 237.237 1.00 4.28   ? 2727 PHE A CD2   1 
ATOM   9339  C  CE1   . PHE A 1 2727 ? 223.972 244.629 237.918 1.00 5.03   ? 2727 PHE A CE1   1 
ATOM   9340  C  CE2   . PHE A 1 2727 ? 225.942 243.445 238.553 1.00 4.62   ? 2727 PHE A CE2   1 
ATOM   9341  C  CZ    . PHE A 1 2727 ? 224.750 244.045 238.894 1.00 3.93   ? 2727 PHE A CZ    1 
ATOM   9342  N  N     . LEU A 1 2728 ? 228.845 245.321 235.361 1.00 6.04   ? 2728 LEU A N     1 
ATOM   9343  C  CA    . LEU A 1 2728 ? 229.855 245.748 236.319 1.00 4.57   ? 2728 LEU A CA    1 
ATOM   9344  C  C     . LEU A 1 2728 ? 230.309 247.182 236.086 1.00 5.81   ? 2728 LEU A C     1 
ATOM   9345  O  O     . LEU A 1 2728 ? 230.949 247.767 236.965 1.00 8.13   ? 2728 LEU A O     1 
ATOM   9346  C  CB    . LEU A 1 2728 ? 231.059 244.807 236.268 1.00 5.74   ? 2728 LEU A CB    1 
ATOM   9347  C  CG    . LEU A 1 2728 ? 230.915 243.479 237.013 1.00 5.37   ? 2728 LEU A CG    1 
ATOM   9348  C  CD1   . LEU A 1 2728 ? 232.203 242.677 236.941 1.00 6.59   ? 2728 LEU A CD1   1 
ATOM   9349  C  CD2   . LEU A 1 2728 ? 230.511 243.715 238.457 1.00 5.37   ? 2728 LEU A CD2   1 
ATOM   9350  N  N     . ARG A 1 2729 ? 229.996 247.757 234.924 1.00 6.50   ? 2729 ARG A N     1 
ATOM   9351  C  CA    . ARG A 1 2729 ? 230.386 249.133 234.644 1.00 5.25   ? 2729 ARG A CA    1 
ATOM   9352  C  C     . ARG A 1 2729 ? 229.719 250.113 235.599 1.00 5.00   ? 2729 ARG A C     1 
ATOM   9353  O  O     . ARG A 1 2729 ? 230.318 251.131 235.964 1.00 6.69   ? 2729 ARG A O     1 
ATOM   9354  C  CB    . ARG A 1 2729 ? 230.052 249.476 233.190 1.00 4.36   ? 2729 ARG A CB    1 
ATOM   9355  C  CG    . ARG A 1 2729 ? 229.861 250.953 232.908 1.00 4.66   ? 2729 ARG A CG    1 
ATOM   9356  C  CD    . ARG A 1 2729 ? 229.571 251.202 231.439 1.00 5.32   ? 2729 ARG A CD    1 
ATOM   9357  N  NE    . ARG A 1 2729 ? 229.259 252.602 231.181 1.00 4.77   ? 2729 ARG A NE    1 
ATOM   9358  C  CZ    . ARG A 1 2729 ? 228.166 253.027 230.565 1.00 4.15   ? 2729 ARG A CZ    1 
ATOM   9359  N  NH1   . ARG A 1 2729 ? 227.263 252.182 230.095 1.00 5.21   ? 2729 ARG A NH1   1 
ATOM   9360  N  NH2   . ARG A 1 2729 ? 227.975 254.334 230.411 1.00 5.27   ? 2729 ARG A NH2   1 
ATOM   9361  N  N     . HIS A 1 2730 ? 228.494 249.819 236.031 1.00 5.60   ? 2730 HIS A N     1 
ATOM   9362  C  CA    . HIS A 1 2730 ? 227.725 250.737 236.855 1.00 4.09   ? 2730 HIS A CA    1 
ATOM   9363  C  C     . HIS A 1 2730 ? 227.752 250.401 238.339 1.00 6.24   ? 2730 HIS A C     1 
ATOM   9364  O  O     . HIS A 1 2730 ? 227.293 251.216 239.145 1.00 9.39   ? 2730 HIS A O     1 
ATOM   9365  C  CB    . HIS A 1 2730 ? 226.269 250.777 236.379 1.00 3.60   ? 2730 HIS A CB    1 
ATOM   9366  C  CG    . HIS A 1 2730 ? 226.125 250.970 234.904 1.00 6.51   ? 2730 HIS A CG    1 
ATOM   9367  N  ND1   . HIS A 1 2730 ? 226.202 249.928 234.006 1.00 6.30   ? 2730 HIS A ND1   1 
ATOM   9368  C  CD2   . HIS A 1 2730 ? 225.918 252.087 234.168 1.00 5.96   ? 2730 HIS A CD2   1 
ATOM   9369  C  CE1   . HIS A 1 2730 ? 226.044 250.393 232.780 1.00 6.23   ? 2730 HIS A CE1   1 
ATOM   9370  N  NE2   . HIS A 1 2730 ? 225.872 251.700 232.851 1.00 7.46   ? 2730 HIS A NE2   1 
ATOM   9371  N  N     . VAL A 1 2731 ? 228.263 249.237 238.723 1.00 6.57   ? 2731 VAL A N     1 
ATOM   9372  C  CA    . VAL A 1 2731 ? 228.259 248.820 240.120 1.00 6.89   ? 2731 VAL A CA    1 
ATOM   9373  C  C     . VAL A 1 2731 ? 229.707 248.761 240.610 1.00 6.62   ? 2731 VAL A C     1 
ATOM   9374  O  O     . VAL A 1 2731 ? 230.499 247.939 240.129 1.00 7.14   ? 2731 VAL A O     1 
ATOM   9375  C  CB    . VAL A 1 2731 ? 227.523 247.485 240.317 1.00 6.31   ? 2731 VAL A CB    1 
ATOM   9376  C  CG1   . VAL A 1 2731 ? 226.070 247.639 239.916 1.00 6.75   ? 2731 VAL A CG1   1 
ATOM   9377  C  CG2   . VAL A 1 2731 ? 228.133 246.374 239.482 1.00 6.17   ? 2731 VAL A CG2   1 
ATOM   9378  N  N     . PRO A 1 2732 ? 230.114 249.649 241.517 1.00 6.45   ? 2732 PRO A N     1 
ATOM   9379  C  CA    . PRO A 1 2732 ? 231.386 249.447 242.217 1.00 5.53   ? 2732 PRO A CA    1 
ATOM   9380  C  C     . PRO A 1 2732 ? 231.351 248.174 243.046 1.00 6.80   ? 2732 PRO A C     1 
ATOM   9381  O  O     . PRO A 1 2732 ? 230.329 247.825 243.640 1.00 8.36   ? 2732 PRO A O     1 
ATOM   9382  C  CB    . PRO A 1 2732 ? 231.508 250.693 243.103 1.00 5.58   ? 2732 PRO A CB    1 
ATOM   9383  C  CG    . PRO A 1 2732 ? 230.149 251.309 243.118 1.00 7.51   ? 2732 PRO A CG    1 
ATOM   9384  C  CD    . PRO A 1 2732 ? 229.539 250.969 241.804 1.00 7.39   ? 2732 PRO A CD    1 
ATOM   9385  N  N     . VAL A 1 2733 ? 232.490 247.490 243.098 1.00 5.54   ? 2733 VAL A N     1 
ATOM   9386  C  CA    . VAL A 1 2733 ? 232.625 246.228 243.814 1.00 4.76   ? 2733 VAL A CA    1 
ATOM   9387  C  C     . VAL A 1 2733 ? 233.565 246.440 244.990 1.00 6.62   ? 2733 VAL A C     1 
ATOM   9388  O  O     . VAL A 1 2733 ? 234.672 246.964 244.823 1.00 7.03   ? 2733 VAL A O     1 
ATOM   9389  C  CB    . VAL A 1 2733 ? 233.142 245.110 242.892 1.00 5.02   ? 2733 VAL A CB    1 
ATOM   9390  C  CG1   . VAL A 1 2733 ? 233.313 243.819 243.672 1.00 5.54   ? 2733 VAL A CG1   1 
ATOM   9391  C  CG2   . VAL A 1 2733 ? 232.193 244.910 241.722 1.00 6.45   ? 2733 VAL A CG2   1 
ATOM   9392  N  N     . VAL A 1 2734 ? 233.121 246.038 246.177 1.00 6.92   ? 2734 VAL A N     1 
ATOM   9393  C  CA    . VAL A 1 2734 ? 233.938 246.083 247.383 1.00 4.90   ? 2734 VAL A CA    1 
ATOM   9394  C  C     . VAL A 1 2734 ? 234.174 244.655 247.854 1.00 4.79   ? 2734 VAL A C     1 
ATOM   9395  O  O     . VAL A 1 2734 ? 233.235 243.854 247.932 1.00 6.36   ? 2734 VAL A O     1 
ATOM   9396  C  CB    . VAL A 1 2734 ? 233.294 246.952 248.483 1.00 5.36   ? 2734 VAL A CB    1 
ATOM   9397  C  CG1   . VAL A 1 2734 ? 231.980 246.360 248.970 1.00 9.61   ? 2734 VAL A CG1   1 
ATOM   9398  C  CG2   . VAL A 1 2734 ? 234.256 247.129 249.645 1.00 5.50   ? 2734 VAL A CG2   1 
ATOM   9399  N  N     . TYR A 1 2735 ? 235.432 244.330 248.135 1.00 7.04   ? 2735 TYR A N     1 
ATOM   9400  C  CA    . TYR A 1 2735 ? 235.814 242.986 248.554 1.00 6.85   ? 2735 TYR A CA    1 
ATOM   9401  C  C     . TYR A 1 2735 ? 235.887 242.943 250.075 1.00 9.41   ? 2735 TYR A C     1 
ATOM   9402  O  O     . TYR A 1 2735 ? 236.768 243.560 250.681 1.00 13.02  ? 2735 TYR A O     1 
ATOM   9403  C  CB    . TYR A 1 2735 ? 237.148 242.581 247.935 1.00 6.27   ? 2735 TYR A CB    1 
ATOM   9404  C  CG    . TYR A 1 2735 ? 237.607 241.201 248.345 1.00 8.91   ? 2735 TYR A CG    1 
ATOM   9405  C  CD1   . TYR A 1 2735 ? 236.850 240.078 248.045 1.00 8.54   ? 2735 TYR A CD1   1 
ATOM   9406  C  CD2   . TYR A 1 2735 ? 238.794 241.023 249.041 1.00 10.69  ? 2735 TYR A CD2   1 
ATOM   9407  C  CE1   . TYR A 1 2735 ? 237.265 238.817 248.422 1.00 10.08  ? 2735 TYR A CE1   1 
ATOM   9408  C  CE2   . TYR A 1 2735 ? 239.217 239.766 249.423 1.00 9.37   ? 2735 TYR A CE2   1 
ATOM   9409  C  CZ    . TYR A 1 2735 ? 238.448 238.666 249.111 1.00 11.47  ? 2735 TYR A CZ    1 
ATOM   9410  O  OH    . TYR A 1 2735 ? 238.866 237.411 249.489 1.00 14.11  ? 2735 TYR A OH    1 
ATOM   9411  N  N     . VAL A 1 2736 ? 234.964 242.213 250.688 1.00 8.15   ? 2736 VAL A N     1 
ATOM   9412  C  CA    . VAL A 1 2736 ? 234.972 241.976 252.125 1.00 8.69   ? 2736 VAL A CA    1 
ATOM   9413  C  C     . VAL A 1 2736 ? 235.581 240.600 252.349 1.00 7.74   ? 2736 VAL A C     1 
ATOM   9414  O  O     . VAL A 1 2736 ? 234.983 239.579 251.994 1.00 9.41   ? 2736 VAL A O     1 
ATOM   9415  C  CB    . VAL A 1 2736 ? 233.564 242.077 252.726 1.00 8.16   ? 2736 VAL A CB    1 
ATOM   9416  C  CG1   . VAL A 1 2736 ? 233.631 242.036 254.241 1.00 6.16   ? 2736 VAL A CG1   1 
ATOM   9417  C  CG2   . VAL A 1 2736 ? 232.881 243.348 252.254 1.00 9.53   ? 2736 VAL A CG2   1 
ATOM   9418  N  N     . ASP A 1 2737 ? 236.773 240.571 252.929 1.00 6.82   ? 2737 ASP A N     1 
ATOM   9419  C  CA    . ASP A 1 2737 ? 237.473 239.327 253.195 1.00 8.55   ? 2737 ASP A CA    1 
ATOM   9420  C  C     . ASP A 1 2737 ? 237.144 238.820 254.595 1.00 8.71   ? 2737 ASP A C     1 
ATOM   9421  O  O     . ASP A 1 2737 ? 236.529 239.511 255.409 1.00 9.73   ? 2737 ASP A O     1 
ATOM   9422  C  CB    . ASP A 1 2737 ? 238.981 239.521 253.034 1.00 11.47  ? 2737 ASP A CB    1 
ATOM   9423  C  CG    . ASP A 1 2737 ? 239.713 238.222 252.763 1.00 12.30  ? 2737 ASP A CG    1 
ATOM   9424  O  OD1   . ASP A 1 2737 ? 239.054 237.162 252.732 1.00 11.06  ? 2737 ASP A OD1   1 
ATOM   9425  O  OD2   . ASP A 1 2737 ? 240.947 238.262 252.580 1.00 12.94  ? 2737 ASP A OD2   1 
ATOM   9426  N  N     . TYR A 1 2738 ? 237.531 237.575 254.880 1.00 10.11  ? 2738 TYR A N     1 
ATOM   9427  C  CA    . TYR A 1 2738 ? 237.285 237.000 256.231 1.00 7.31   ? 2738 TYR A CA    1 
ATOM   9428  C  C     . TYR A 1 2738 ? 238.121 237.765 257.249 1.00 8.42   ? 2738 TYR A C     1 
ATOM   9429  O  O     . TYR A 1 2738 ? 239.292 238.084 256.955 1.00 8.59   ? 2738 TYR A O     1 
ATOM   9430  C  CB    . TYR A 1 2738 ? 237.623 235.508 256.269 1.00 5.04   ? 2738 TYR A CB    1 
ATOM   9431  C  CG    . TYR A 1 2738 ? 236.554 234.564 255.736 1.00 5.92   ? 2738 TYR A CG    1 
ATOM   9432  C  CD1   . TYR A 1 2738 ? 235.204 234.876 255.827 1.00 7.24   ? 2738 TYR A CD1   1 
ATOM   9433  C  CD2   . TYR A 1 2738 ? 236.902 233.352 255.153 1.00 5.46   ? 2738 TYR A CD2   1 
ATOM   9434  C  CE1   . TYR A 1 2738 ? 234.231 234.015 255.348 1.00 6.52   ? 2738 TYR A CE1   1 
ATOM   9435  C  CE2   . TYR A 1 2738 ? 235.939 232.482 254.671 1.00 5.49   ? 2738 TYR A CE2   1 
ATOM   9436  C  CZ    . TYR A 1 2738 ? 234.601 232.815 254.769 1.00 6.51   ? 2738 TYR A CZ    1 
ATOM   9437  O  OH    . TYR A 1 2738 ? 233.658 231.954 254.289 1.00 10.47  ? 2738 TYR A OH    1 
ATOM   9438  N  N     . PRO A 1 2739 ? 237.580 238.084 258.444 1.00 7.06   ? 2739 PRO A N     1 
ATOM   9439  C  CA    . PRO A 1 2739 ? 238.371 238.736 259.477 1.00 7.99   ? 2739 PRO A CA    1 
ATOM   9440  C  C     . PRO A 1 2739 ? 239.612 237.915 259.788 1.00 12.20  ? 2739 PRO A C     1 
ATOM   9441  O  O     . PRO A 1 2739 ? 239.521 236.672 259.839 1.00 15.99  ? 2739 PRO A O     1 
ATOM   9442  C  CB    . PRO A 1 2739 ? 237.404 238.804 260.664 1.00 9.05   ? 2739 PRO A CB    1 
ATOM   9443  C  CG    . PRO A 1 2739 ? 236.035 238.769 260.025 1.00 6.28   ? 2739 PRO A CG    1 
ATOM   9444  C  CD    . PRO A 1 2739 ? 236.197 237.857 258.822 1.00 6.16   ? 2739 PRO A CD    1 
ATOM   9445  N  N     . GLY A 1 2740 ? 240.751 238.585 259.983 1.00 14.65  ? 2740 GLY A N     1 
ATOM   9446  C  CA    . GLY A 1 2740 ? 242.018 237.882 260.265 1.00 13.96  ? 2740 GLY A CA    1 
ATOM   9447  C  C     . GLY A 1 2740 ? 242.121 237.497 261.726 1.00 18.49  ? 2740 GLY A C     1 
ATOM   9448  O  O     . GLY A 1 2740 ? 241.218 237.877 262.500 1.00 19.59  ? 2740 GLY A O     1 
ATOM   9449  N  N     . PRO A 1 2741 ? 243.168 236.759 262.156 1.00 19.20  ? 2741 PRO A N     1 
ATOM   9450  C  CA    . PRO A 1 2741 ? 243.254 236.279 263.545 1.00 15.82  ? 2741 PRO A CA    1 
ATOM   9451  C  C     . PRO A 1 2741 ? 243.188 237.394 264.574 1.00 18.85  ? 2741 PRO A C     1 
ATOM   9452  O  O     . PRO A 1 2741 ? 242.577 237.213 265.633 1.00 18.27  ? 2741 PRO A O     1 
ATOM   9453  C  CB    . PRO A 1 2741 ? 244.605 235.550 263.576 1.00 16.23  ? 2741 PRO A CB    1 
ATOM   9454  C  CG    . PRO A 1 2741 ? 244.864 235.174 262.156 1.00 21.71  ? 2741 PRO A CG    1 
ATOM   9455  C  CD    . PRO A 1 2741 ? 244.294 236.287 261.334 1.00 18.68  ? 2741 PRO A CD    1 
ATOM   9456  N  N     . ALA A 1 2742 ? 243.788 238.551 264.287 1.00 17.03  ? 2742 ALA A N     1 
ATOM   9457  C  CA    . ALA A 1 2742 ? 243.728 239.667 265.226 1.00 15.20  ? 2742 ALA A CA    1 
ATOM   9458  C  C     . ALA A 1 2742 ? 242.320 240.247 265.308 1.00 15.81  ? 2742 ALA A C     1 
ATOM   9459  O  O     . ALA A 1 2742 ? 241.805 240.501 266.404 1.00 16.93  ? 2742 ALA A O     1 
ATOM   9460  C  CB    . ALA A 1 2742 ? 244.733 240.745 264.820 1.00 18.04  ? 2742 ALA A CB    1 
ATOM   9461  N  N     . SER A 1 2743 ? 241.684 240.472 264.157 1.00 17.47  ? 2743 SER A N     1 
ATOM   9462  C  CA    . SER A 1 2743 ? 240.328 241.012 264.154 1.00 15.43  ? 2743 SER A CA    1 
ATOM   9463  C  C     . SER A 1 2743 ? 239.337 240.028 264.763 1.00 17.99  ? 2743 SER A C     1 
ATOM   9464  O  O     . SER A 1 2743 ? 238.453 240.423 265.536 1.00 19.89  ? 2743 SER A O     1 
ATOM   9465  C  CB    . SER A 1 2743 ? 239.917 241.381 262.728 1.00 15.94  ? 2743 SER A CB    1 
ATOM   9466  O  OG    . SER A 1 2743 ? 238.592 241.880 262.692 1.00 32.17  ? 2743 SER A OG    1 
ATOM   9467  N  N     . LEU A 1 2744 ? 239.464 238.743 264.420 1.00 16.65  ? 2744 LEU A N     1 
ATOM   9468  C  CA    . LEU A 1 2744 ? 238.615 237.726 265.030 1.00 14.86  ? 2744 LEU A CA    1 
ATOM   9469  C  C     . LEU A 1 2744 ? 238.828 237.679 266.534 1.00 12.99  ? 2744 LEU A C     1 
ATOM   9470  O  O     . LEU A 1 2744 ? 237.865 237.571 267.304 1.00 16.12  ? 2744 LEU A O     1 
ATOM   9471  C  CB    . LEU A 1 2744 ? 238.906 236.359 264.412 1.00 15.15  ? 2744 LEU A CB    1 
ATOM   9472  C  CG    . LEU A 1 2744 ? 238.355 236.062 263.019 1.00 13.82  ? 2744 LEU A CG    1 
ATOM   9473  C  CD1   . LEU A 1 2744 ? 238.864 234.719 262.542 1.00 10.97  ? 2744 LEU A CD1   1 
ATOM   9474  C  CD2   . LEU A 1 2744 ? 236.839 236.095 263.014 1.00 13.73  ? 2744 LEU A CD2   1 
ATOM   9475  N  N     . THR A 1 2745 ? 240.087 237.761 266.967 1.00 15.03  ? 2745 THR A N     1 
ATOM   9476  C  CA    . THR A 1 2745 ? 240.386 237.767 268.391 1.00 13.02  ? 2745 THR A CA    1 
ATOM   9477  C  C     . THR A 1 2745 ? 239.727 238.950 269.079 1.00 12.50  ? 2745 THR A C     1 
ATOM   9478  O  O     . THR A 1 2745 ? 239.124 238.794 270.139 1.00 18.22  ? 2745 THR A O     1 
ATOM   9479  C  CB    . THR A 1 2745 ? 241.898 237.790 268.612 1.00 11.64  ? 2745 THR A CB    1 
ATOM   9480  O  OG1   . THR A 1 2745 ? 242.491 236.652 267.976 1.00 22.31  ? 2745 THR A OG1   1 
ATOM   9481  C  CG2   . THR A 1 2745 ? 242.220 237.754 270.095 1.00 10.35  ? 2745 THR A CG2   1 
ATOM   9482  N  N     . GLN A 1 2746 ? 239.760 240.114 268.428 1.00 14.36  ? 2746 GLN A N     1 
ATOM   9483  C  CA    . GLN A 1 2746 ? 239.107 241.324 268.991 1.00 18.85  ? 2746 GLN A CA    1 
ATOM   9484  C  C     . GLN A 1 2746 ? 237.581 241.139 269.030 1.00 14.99  ? 2746 GLN A C     1 
ATOM   9485  O  O     . GLN A 1 2746 ? 236.996 241.316 270.121 1.00 16.18  ? 2746 GLN A O     1 
ATOM   9486  C  CB    . GLN A 1 2746 ? 239.467 242.546 268.146 1.00 21.84  ? 2746 GLN A CB    1 
ATOM   9487  C  CG    . GLN A 1 2746 ? 238.839 243.845 268.641 1.00 35.13  ? 2746 GLN A CG    1 
ATOM   9488  C  CD    . GLN A 1 2746 ? 239.057 245.010 267.701 1.00 39.78  ? 2746 GLN A CD    1 
ATOM   9489  O  OE1   . GLN A 1 2746 ? 238.106 245.632 267.214 1.00 27.29  ? 2746 GLN A OE1   1 
ATOM   9490  N  NE2   . GLN A 1 2746 ? 240.318 245.319 267.437 1.00 43.34  ? 2746 GLN A NE2   1 
ATOM   9491  N  N     . ILE A 1 2747 ? 236.965 240.787 267.897 1.00 14.02  ? 2747 ILE A N     1 
ATOM   9492  C  CA    . ILE A 1 2747 ? 235.475 240.669 267.824 1.00 12.95  ? 2747 ILE A CA    1 
ATOM   9493  C  C     . ILE A 1 2747 ? 234.973 239.626 268.833 1.00 12.20  ? 2747 ILE A C     1 
ATOM   9494  O  O     . ILE A 1 2747 ? 234.106 239.979 269.666 1.00 14.38  ? 2747 ILE A O     1 
ATOM   9495  C  CB    . ILE A 1 2747 ? 235.036 240.292 266.398 1.00 10.37  ? 2747 ILE A CB    1 
ATOM   9496  C  CG1   . ILE A 1 2747 ? 235.527 241.306 265.367 1.00 17.27  ? 2747 ILE A CG1   1 
ATOM   9497  C  CG2   . ILE A 1 2747 ? 233.522 240.096 266.324 1.00 10.99  ? 2747 ILE A CG2   1 
ATOM   9498  C  CD1   . ILE A 1 2747 ? 235.461 240.807 263.934 1.00 12.85  ? 2747 ILE A CD1   1 
ATOM   9499  N  N     . TYR A 1 2748 ? 235.486 238.398 268.770 1.00 10.52  ? 2748 TYR A N     1 
ATOM   9500  C  CA    . TYR A 1 2748 ? 234.943 237.333 269.658 1.00 11.50  ? 2748 TYR A CA    1 
ATOM   9501  C  C     . TYR A 1 2748 ? 235.498 237.510 271.074 1.00 13.45  ? 2748 TYR A C     1 
ATOM   9502  O  O     . TYR A 1 2748 ? 234.822 237.085 272.031 1.00 17.55  ? 2748 TYR A O     1 
ATOM   9503  C  CB    . TYR A 1 2748 ? 235.180 235.978 268.983 1.00 13.34  ? 2748 TYR A CB    1 
ATOM   9504  C  CG    . TYR A 1 2748 ? 234.342 235.868 267.718 1.00 11.33  ? 2748 TYR A CG    1 
ATOM   9505  C  CD1   . TYR A 1 2748 ? 233.017 235.458 267.777 1.00 8.78   ? 2748 TYR A CD1   1 
ATOM   9506  C  CD2   . TYR A 1 2748 ? 234.863 236.207 266.476 1.00 9.89   ? 2748 TYR A CD2   1 
ATOM   9507  C  CE1   . TYR A 1 2748 ? 232.238 235.375 266.636 1.00 9.90   ? 2748 TYR A CE1   1 
ATOM   9508  C  CE2   . TYR A 1 2748 ? 234.094 236.124 265.327 1.00 11.57  ? 2748 TYR A CE2   1 
ATOM   9509  C  CZ    . TYR A 1 2748 ? 232.779 235.706 265.408 1.00 11.83  ? 2748 TYR A CZ    1 
ATOM   9510  O  OH    . TYR A 1 2748 ? 232.015 235.621 264.283 1.00 12.97  ? 2748 TYR A OH    1 
ATOM   9511  N  N     . GLY A 1 2749 ? 236.672 238.131 271.215 1.00 10.98  ? 2749 GLY A N     1 
ATOM   9512  C  CA    . GLY A 1 2749 ? 237.173 238.404 272.574 1.00 11.45  ? 2749 GLY A CA    1 
ATOM   9513  C  C     . GLY A 1 2749 ? 236.181 239.287 273.300 1.00 14.27  ? 2749 GLY A C     1 
ATOM   9514  O  O     . GLY A 1 2749 ? 235.927 239.036 274.496 1.00 18.27  ? 2749 GLY A O     1 
ATOM   9515  N  N     . THR A 1 2750 ? 235.623 240.275 272.597 1.00 12.82  ? 2750 THR A N     1 
ATOM   9516  C  CA    . THR A 1 2750 ? 234.634 241.191 273.199 1.00 15.16  ? 2750 THR A CA    1 
ATOM   9517  C  C     . THR A 1 2750 ? 233.394 240.407 273.559 1.00 17.71  ? 2750 THR A C     1 
ATOM   9518  O  O     . THR A 1 2750 ? 232.878 240.598 274.679 1.00 22.30  ? 2750 THR A O     1 
ATOM   9519  C  CB    . THR A 1 2750 ? 234.321 242.309 272.207 1.00 14.58  ? 2750 THR A CB    1 
ATOM   9520  O  OG1   . THR A 1 2750 ? 235.574 242.924 271.926 1.00 15.02  ? 2750 THR A OG1   1 
ATOM   9521  C  CG2   . THR A 1 2750 ? 233.348 243.331 272.768 1.00 21.12  ? 2750 THR A CG2   1 
ATOM   9522  N  N     . PHE A 1 2751 ? 232.928 239.552 272.645 1.00 17.26  ? 2751 PHE A N     1 
ATOM   9523  C  CA    . PHE A 1 2751 ? 231.688 238.763 272.885 1.00 13.85  ? 2751 PHE A CA    1 
ATOM   9524  C  C     . PHE A 1 2751 ? 231.909 237.817 274.062 1.00 15.60  ? 2751 PHE A C     1 
ATOM   9525  O  O     . PHE A 1 2751 ? 230.970 237.605 274.856 1.00 18.50  ? 2751 PHE A O     1 
ATOM   9526  C  CB    . PHE A 1 2751 ? 231.299 238.025 271.602 1.00 16.42  ? 2751 PHE A CB    1 
ATOM   9527  C  CG    . PHE A 1 2751 ? 230.485 238.858 270.621 1.00 14.50  ? 2751 PHE A CG    1 
ATOM   9528  C  CD1   . PHE A 1 2751 ? 229.620 239.847 271.075 1.00 15.36  ? 2751 PHE A CD1   1 
ATOM   9529  C  CD2   . PHE A 1 2751 ? 230.587 238.649 269.251 1.00 15.49  ? 2751 PHE A CD2   1 
ATOM   9530  C  CE1   . PHE A 1 2751 ? 228.878 240.602 270.182 1.00 19.70  ? 2751 PHE A CE1   1 
ATOM   9531  C  CE2   . PHE A 1 2751 ? 229.842 239.410 268.363 1.00 19.92  ? 2751 PHE A CE2   1 
ATOM   9532  C  CZ    . PHE A 1 2751 ? 228.992 240.384 268.829 1.00 19.76  ? 2751 PHE A CZ    1 
ATOM   9533  N  N     . ASN A 1 2752 ? 233.118 237.263 274.177 1.00 13.72  ? 2752 ASN A N     1 
ATOM   9534  C  CA    . ASN A 1 2752 ? 233.408 236.283 275.261 1.00 12.79  ? 2752 ASN A CA    1 
ATOM   9535  C  C     . ASN A 1 2752 ? 233.416 237.013 276.609 1.00 16.25  ? 2752 ASN A C     1 
ATOM   9536  O  O     . ASN A 1 2752 ? 232.812 236.483 277.564 1.00 20.27  ? 2752 ASN A O     1 
ATOM   9537  C  CB    . ASN A 1 2752 ? 234.684 235.495 274.979 1.00 10.09  ? 2752 ASN A CB    1 
ATOM   9538  C  CG    . ASN A 1 2752 ? 234.469 234.438 273.921 1.00 11.41  ? 2752 ASN A CG    1 
ATOM   9539  O  OD1   . ASN A 1 2752 ? 233.362 234.303 273.393 1.00 13.72  ? 2752 ASN A OD1   1 
ATOM   9540  N  ND2   . ASN A 1 2752 ? 235.507 233.680 273.602 1.00 17.24  ? 2752 ASN A ND2   1 
ATOM   9541  N  N     . ARG A 1 2753 ? 234.067 238.177 276.683 1.00 16.92  ? 2753 ARG A N     1 
ATOM   9542  C  CA    . ARG A 1 2753 ? 234.070 238.953 277.918 1.00 17.16  ? 2753 ARG A CA    1 
ATOM   9543  C  C     . ARG A 1 2753 ? 232.650 239.293 278.346 1.00 19.40  ? 2753 ARG A C     1 
ATOM   9544  O  O     . ARG A 1 2753 ? 232.282 239.131 279.518 1.00 22.82  ? 2753 ARG A O     1 
ATOM   9545  C  CB    . ARG A 1 2753 ? 234.900 240.222 277.729 1.00 19.28  ? 2753 ARG A CB    1 
ATOM   9546  C  CG    . ARG A 1 2753 ? 236.392 240.020 277.930 1.00 25.99  ? 2753 ARG A CG    1 
ATOM   9547  C  CD    . ARG A 1 2753 ? 237.107 241.344 278.130 1.00 26.80  ? 2753 ARG A CD    1 
ATOM   9548  N  NE    . ARG A 1 2753 ? 236.492 242.415 277.357 1.00 27.55  ? 2753 ARG A NE    1 
ATOM   9549  C  CZ    . ARG A 1 2753 ? 236.853 242.752 276.126 1.00 26.98  ? 2753 ARG A CZ    1 
ATOM   9550  N  NH1   . ARG A 1 2753 ? 237.822 242.114 275.491 1.00 13.02  ? 2753 ARG A NH1   1 
ATOM   9551  N  NH2   . ARG A 1 2753 ? 236.223 243.751 275.514 1.00 27.83  ? 2753 ARG A NH2   1 
ATOM   9552  N  N     . ALA A 1 2754 ? 231.824 239.739 277.396 1.00 17.10  ? 2754 ALA A N     1 
ATOM   9553  C  CA    . ALA A 1 2754 ? 230.436 240.045 277.726 1.00 19.65  ? 2754 ALA A CA    1 
ATOM   9554  C  C     . ALA A 1 2754 ? 229.696 238.799 278.199 1.00 27.59  ? 2754 ALA A C     1 
ATOM   9555  O  O     . ALA A 1 2754 ? 228.868 238.867 279.117 1.00 31.61  ? 2754 ALA A O     1 
ATOM   9556  C  CB    . ALA A 1 2754 ? 229.735 240.666 276.519 1.00 21.92  ? 2754 ALA A CB    1 
ATOM   9557  N  N     . MET A 1 2755 ? 229.982 237.650 277.584 1.00 24.17  ? 2755 MET A N     1 
ATOM   9558  C  CA    . MET A 1 2755 ? 229.343 236.399 277.979 1.00 18.45  ? 2755 MET A CA    1 
ATOM   9559  C  C     . MET A 1 2755 ? 229.787 235.957 279.369 1.00 24.32  ? 2755 MET A C     1 
ATOM   9560  O  O     . MET A 1 2755 ? 228.957 235.615 280.218 1.00 32.67  ? 2755 MET A O     1 
ATOM   9561  C  CB    . MET A 1 2755 ? 229.662 235.321 276.945 1.00 20.76  ? 2755 MET A CB    1 
ATOM   9562  C  CG    . MET A 1 2755 ? 229.022 233.975 277.199 1.00 18.82  ? 2755 MET A CG    1 
ATOM   9563  S  SD    . MET A 1 2755 ? 229.462 232.816 275.893 1.00 33.08  ? 2755 MET A SD    1 
ATOM   9564  C  CE    . MET A 1 2755 ? 231.185 232.527 276.282 1.00 21.82  ? 2755 MET A CE    1 
ATOM   9565  N  N     . LEU A 1 2756 ? 231.096 235.958 279.619 1.00 23.56  ? 2756 LEU A N     1 
ATOM   9566  C  CA    . LEU A 1 2756 ? 231.644 235.473 280.876 1.00 24.38  ? 2756 LEU A CA    1 
ATOM   9567  C  C     . LEU A 1 2756 ? 231.436 236.451 282.020 1.00 32.60  ? 2756 LEU A C     1 
ATOM   9568  O  O     . LEU A 1 2756 ? 231.711 236.096 283.170 1.00 37.26  ? 2756 LEU A O     1 
ATOM   9569  C  CB    . LEU A 1 2756 ? 233.133 235.169 280.711 1.00 23.34  ? 2756 LEU A CB    1 
ATOM   9570  C  CG    . LEU A 1 2756 ? 233.455 233.896 279.924 1.00 26.68  ? 2756 LEU A CG    1 
ATOM   9571  C  CD1   . LEU A 1 2756 ? 234.887 233.456 280.165 1.00 29.60  ? 2756 LEU A CD1   1 
ATOM   9572  C  CD2   . LEU A 1 2756 ? 232.485 232.779 280.271 1.00 26.30  ? 2756 LEU A CD2   1 
ATOM   9573  N  N     . ARG A 1 2757 ? 230.970 237.669 281.736 1.00 37.69  ? 2757 ARG A N     1 
ATOM   9574  C  CA    . ARG A 1 2757 ? 230.527 238.544 282.815 1.00 33.48  ? 2757 ARG A CA    1 
ATOM   9575  C  C     . ARG A 1 2757 ? 229.363 237.945 283.595 1.00 35.66  ? 2757 ARG A C     1 
ATOM   9576  O  O     . ARG A 1 2757 ? 229.102 238.375 284.723 1.00 42.44  ? 2757 ARG A O     1 
ATOM   9577  C  CB    . ARG A 1 2757 ? 230.139 239.911 282.253 1.00 30.31  ? 2757 ARG A CB    1 
ATOM   9578  C  CG    . ARG A 1 2757 ? 231.294 240.895 282.182 1.00 29.40  ? 2757 ARG A CG    1 
ATOM   9579  C  CD    . ARG A 1 2757 ? 230.797 242.325 282.121 1.00 32.13  ? 2757 ARG A CD    1 
ATOM   9580  N  NE    . ARG A 1 2757 ? 229.850 242.521 281.031 1.00 36.93  ? 2757 ARG A NE    1 
ATOM   9581  C  CZ    . ARG A 1 2757 ? 230.106 243.220 279.933 1.00 37.21  ? 2757 ARG A CZ    1 
ATOM   9582  N  NH1   . ARG A 1 2757 ? 231.281 243.797 279.741 1.00 35.10  ? 2757 ARG A NH1   1 
ATOM   9583  N  NH2   . ARG A 1 2757 ? 229.162 243.339 279.005 1.00 36.31  ? 2757 ARG A NH2   1 
ATOM   9584  N  N     . LEU A 1 2758 ? 228.657 236.967 283.018 1.00 37.18  ? 2758 LEU A N     1 
ATOM   9585  C  CA    . LEU A 1 2758 ? 227.584 236.288 283.739 1.00 43.49  ? 2758 LEU A CA    1 
ATOM   9586  C  C     . LEU A 1 2758 ? 228.115 235.575 284.977 1.00 42.65  ? 2758 LEU A C     1 
ATOM   9587  O  O     . LEU A 1 2758 ? 227.512 235.642 286.054 1.00 49.62  ? 2758 LEU A O     1 
ATOM   9588  C  CB    . LEU A 1 2758 ? 226.880 235.292 282.818 1.00 41.40  ? 2758 LEU A CB    1 
ATOM   9589  C  CG    . LEU A 1 2758 ? 225.845 235.838 281.836 1.00 38.28  ? 2758 LEU A CG    1 
ATOM   9590  C  CD1   . LEU A 1 2758 ? 225.553 234.812 280.755 1.00 35.68  ? 2758 LEU A CD1   1 
ATOM   9591  C  CD2   . LEU A 1 2758 ? 224.571 236.227 282.566 1.00 39.03  ? 2758 LEU A CD2   1 
ATOM   9592  N  N     . ILE A 1 2759 ? 229.239 234.879 284.838 1.00 38.72  ? 2759 ILE A N     1 
ATOM   9593  C  CA    . ILE A 1 2759 ? 229.843 234.144 285.947 1.00 41.60  ? 2759 ILE A CA    1 
ATOM   9594  C  C     . ILE A 1 2759 ? 231.154 234.822 286.324 1.00 45.02  ? 2759 ILE A C     1 
ATOM   9595  O  O     . ILE A 1 2759 ? 232.156 234.668 285.610 1.00 47.05  ? 2759 ILE A O     1 
ATOM   9596  C  CB    . ILE A 1 2759 ? 230.061 232.668 285.583 1.00 42.23  ? 2759 ILE A CB    1 
ATOM   9597  C  CG1   . ILE A 1 2759 ? 228.810 232.096 284.916 1.00 38.65  ? 2759 ILE A CG1   1 
ATOM   9598  C  CG2   . ILE A 1 2759 ? 230.424 231.863 286.819 1.00 45.39  ? 2759 ILE A CG2   1 
ATOM   9599  C  CD1   . ILE A 1 2759 ? 228.869 230.606 284.675 1.00 32.42  ? 2759 ILE A CD1   1 
ATOM   9600  N  N     . PRO A 1 2760 ? 231.193 235.582 287.422 1.00 47.39  ? 2760 PRO A N     1 
ATOM   9601  C  CA    . PRO A 1 2760 ? 232.434 236.300 287.770 1.00 49.43  ? 2760 PRO A CA    1 
ATOM   9602  C  C     . PRO A 1 2760 ? 233.633 235.388 287.958 1.00 47.48  ? 2760 PRO A C     1 
ATOM   9603  O  O     . PRO A 1 2760 ? 234.751 235.756 287.573 1.00 45.58  ? 2760 PRO A O     1 
ATOM   9604  C  CB    . PRO A 1 2760 ? 232.073 237.030 289.072 1.00 48.53  ? 2760 PRO A CB    1 
ATOM   9605  C  CG    . PRO A 1 2760 ? 230.592 237.012 289.163 1.00 54.95  ? 2760 PRO A CG    1 
ATOM   9606  C  CD    . PRO A 1 2760 ? 230.070 235.898 288.319 1.00 46.59  ? 2760 PRO A CD    1 
ATOM   9607  N  N     . SER A 1 2761 ? 233.431 234.197 288.528 1.00 41.54  ? 2761 SER A N     1 
ATOM   9608  C  CA    . SER A 1 2761 ? 234.542 233.290 288.782 1.00 36.95  ? 2761 SER A CA    1 
ATOM   9609  C  C     . SER A 1 2761 ? 235.224 232.831 287.499 1.00 40.67  ? 2761 SER A C     1 
ATOM   9610  O  O     . SER A 1 2761 ? 236.379 232.397 287.546 1.00 37.96  ? 2761 SER A O     1 
ATOM   9611  C  CB    . SER A 1 2761 ? 234.056 232.077 289.576 1.00 45.78  ? 2761 SER A CB    1 
ATOM   9612  O  OG    . SER A 1 2761 ? 233.154 231.296 288.811 1.00 49.34  ? 2761 SER A OG    1 
ATOM   9613  N  N     . LEU A 1 2762 ? 234.537 232.909 286.362 1.00 41.67  ? 2762 LEU A N     1 
ATOM   9614  C  CA    . LEU A 1 2762 ? 235.111 232.557 285.072 1.00 35.48  ? 2762 LEU A CA    1 
ATOM   9615  C  C     . LEU A 1 2762 ? 235.604 233.768 284.293 1.00 38.41  ? 2762 LEU A C     1 
ATOM   9616  O  O     . LEU A 1 2762 ? 236.076 233.607 283.163 1.00 38.56  ? 2762 LEU A O     1 
ATOM   9617  C  CB    . LEU A 1 2762 ? 234.088 231.790 284.231 1.00 36.95  ? 2762 LEU A CB    1 
ATOM   9618  C  CG    . LEU A 1 2762 ? 233.781 230.354 284.657 1.00 37.75  ? 2762 LEU A CG    1 
ATOM   9619  C  CD1   . LEU A 1 2762 ? 232.705 229.753 283.769 1.00 25.57  ? 2762 LEU A CD1   1 
ATOM   9620  C  CD2   . LEU A 1 2762 ? 235.043 229.510 284.621 1.00 32.98  ? 2762 LEU A CD2   1 
ATOM   9621  N  N     . ARG A 1 2763 ? 235.521 234.970 284.873 1.00 41.48  ? 2763 ARG A N     1 
ATOM   9622  C  CA    . ARG A 1 2763 ? 235.825 236.185 284.122 1.00 38.68  ? 2763 ARG A CA    1 
ATOM   9623  C  C     . ARG A 1 2763 ? 237.260 236.202 283.613 1.00 37.58  ? 2763 ARG A C     1 
ATOM   9624  O  O     . ARG A 1 2763 ? 237.549 236.843 282.597 1.00 43.26  ? 2763 ARG A O     1 
ATOM   9625  C  CB    . ARG A 1 2763 ? 235.562 237.416 284.986 1.00 38.81  ? 2763 ARG A CB    1 
ATOM   9626  C  CG    . ARG A 1 2763 ? 234.312 238.188 284.607 1.00 40.12  ? 2763 ARG A CG    1 
ATOM   9627  C  CD    . ARG A 1 2763 ? 234.404 239.632 285.069 1.00 56.88  ? 2763 ARG A CD    1 
ATOM   9628  N  NE    . ARG A 1 2763 ? 234.133 239.769 286.495 1.00 62.41  ? 2763 ARG A NE    1 
ATOM   9629  C  CZ    . ARG A 1 2763 ? 232.972 240.160 287.003 1.00 60.10  ? 2763 ARG A CZ    1 
ATOM   9630  N  NH1   . ARG A 1 2763 ? 231.943 240.459 286.226 1.00 55.84  ? 2763 ARG A NH1   1 
ATOM   9631  N  NH2   . ARG A 1 2763 ? 232.839 240.252 288.322 1.00 56.61  ? 2763 ARG A NH2   1 
ATOM   9632  N  N     . THR A 1 2764 ? 238.168 235.507 284.295 1.00 38.24  ? 2764 THR A N     1 
ATOM   9633  C  CA    . THR A 1 2764 ? 239.567 235.495 283.890 1.00 34.42  ? 2764 THR A CA    1 
ATOM   9634  C  C     . THR A 1 2764 ? 239.851 234.528 282.750 1.00 29.76  ? 2764 THR A C     1 
ATOM   9635  O  O     . THR A 1 2764 ? 240.984 234.497 282.258 1.00 31.93  ? 2764 THR A O     1 
ATOM   9636  C  CB    . THR A 1 2764 ? 240.460 235.147 285.084 1.00 34.32  ? 2764 THR A CB    1 
ATOM   9637  O  OG1   . THR A 1 2764 ? 241.835 235.306 284.717 1.00 40.24  ? 2764 THR A OG1   1 
ATOM   9638  C  CG2   . THR A 1 2764 ? 240.223 233.713 285.523 1.00 27.82  ? 2764 THR A CG2   1 
ATOM   9639  N  N     . TYR A 1 2765 ? 238.866 233.742 282.319 1.00 29.38  ? 2765 TYR A N     1 
ATOM   9640  C  CA    . TYR A 1 2765 ? 239.066 232.769 281.255 1.00 25.14  ? 2765 TYR A CA    1 
ATOM   9641  C  C     . TYR A 1 2765 ? 238.593 233.267 279.897 1.00 27.31  ? 2765 TYR A C     1 
ATOM   9642  O  O     . TYR A 1 2765 ? 238.576 232.490 278.938 1.00 27.12  ? 2765 TYR A O     1 
ATOM   9643  C  CB    . TYR A 1 2765 ? 238.365 231.453 281.598 1.00 24.73  ? 2765 TYR A CB    1 
ATOM   9644  C  CG    . TYR A 1 2765 ? 238.962 230.736 282.785 1.00 23.82  ? 2765 TYR A CG    1 
ATOM   9645  C  CD1   . TYR A 1 2765 ? 240.004 229.837 282.621 1.00 22.24  ? 2765 TYR A CD1   1 
ATOM   9646  C  CD2   . TYR A 1 2765 ? 238.474 230.947 284.066 1.00 27.39  ? 2765 TYR A CD2   1 
ATOM   9647  C  CE1   . TYR A 1 2765 ? 240.552 229.178 283.699 1.00 20.43  ? 2765 TYR A CE1   1 
ATOM   9648  C  CE2   . TYR A 1 2765 ? 239.015 230.291 285.150 1.00 26.91  ? 2765 TYR A CE2   1 
ATOM   9649  C  CZ    . TYR A 1 2765 ? 240.053 229.406 284.961 1.00 21.26  ? 2765 TYR A CZ    1 
ATOM   9650  O  OH    . TYR A 1 2765 ? 240.597 228.747 286.039 1.00 31.76  ? 2765 TYR A OH    1 
ATOM   9651  N  N     . ALA A 1 2766 ? 238.201 234.539 279.790 1.00 28.15  ? 2766 ALA A N     1 
ATOM   9652  C  CA    . ALA A 1 2766 ? 237.749 235.065 278.506 1.00 20.20  ? 2766 ALA A CA    1 
ATOM   9653  C  C     . ALA A 1 2766 ? 238.878 235.086 277.483 1.00 22.22  ? 2766 ALA A C     1 
ATOM   9654  O  O     . ALA A 1 2766 ? 238.682 234.695 276.327 1.00 21.90  ? 2766 ALA A O     1 
ATOM   9655  C  CB    . ALA A 1 2766 ? 237.165 236.463 278.690 1.00 24.86  ? 2766 ALA A CB    1 
ATOM   9656  N  N     . GLU A 1 2767 ? 240.063 235.544 277.886 1.00 24.00  ? 2767 GLU A N     1 
ATOM   9657  C  CA    . GLU A 1 2767 ? 241.183 235.620 276.950 1.00 25.27  ? 2767 GLU A CA    1 
ATOM   9658  C  C     . GLU A 1 2767 ? 241.633 234.254 276.443 1.00 23.10  ? 2767 GLU A C     1 
ATOM   9659  O  O     . GLU A 1 2767 ? 241.824 234.111 275.222 1.00 18.66  ? 2767 GLU A O     1 
ATOM   9660  C  CB    . GLU A 1 2767 ? 242.339 236.394 277.592 1.00 24.35  ? 2767 GLU A CB    1 
ATOM   9661  C  CG    . GLU A 1 2767 ? 243.526 236.600 276.669 1.00 38.64  ? 2767 GLU A CG    1 
ATOM   9662  C  CD    . GLU A 1 2767 ? 244.634 237.410 277.310 1.00 64.96  ? 2767 GLU A CD    1 
ATOM   9663  O  OE1   . GLU A 1 2767 ? 244.483 237.797 278.488 1.00 65.70  ? 2767 GLU A OE1   1 
ATOM   9664  O  OE2   . GLU A 1 2767 ? 245.655 237.660 276.637 1.00 79.25  ? 2767 GLU A OE2   1 
ATOM   9665  N  N     . PRO A 1 2768 ? 241.830 233.228 277.281 1.00 23.23  ? 2768 PRO A N     1 
ATOM   9666  C  CA    . PRO A 1 2768 ? 242.229 231.927 276.717 1.00 22.30  ? 2768 PRO A CA    1 
ATOM   9667  C  C     . PRO A 1 2768 ? 241.129 231.262 275.910 1.00 16.90  ? 2768 PRO A C     1 
ATOM   9668  O  O     . PRO A 1 2768 ? 241.404 230.735 274.824 1.00 17.03  ? 2768 PRO A O     1 
ATOM   9669  C  CB    . PRO A 1 2768 ? 242.606 231.107 277.958 1.00 23.05  ? 2768 PRO A CB    1 
ATOM   9670  C  CG    . PRO A 1 2768 ? 241.852 231.734 279.065 1.00 21.83  ? 2768 PRO A CG    1 
ATOM   9671  C  CD    . PRO A 1 2768 ? 241.821 233.195 278.756 1.00 20.23  ? 2768 PRO A CD    1 
ATOM   9672  N  N     . LEU A 1 2769 ? 239.888 231.284 276.406 1.00 14.62  ? 2769 LEU A N     1 
ATOM   9673  C  CA    . LEU A 1 2769 ? 238.782 230.645 275.699 1.00 15.93  ? 2769 LEU A CA    1 
ATOM   9674  C  C     . LEU A 1 2769 ? 238.660 231.175 274.278 1.00 14.79  ? 2769 LEU A C     1 
ATOM   9675  O  O     . LEU A 1 2769 ? 238.589 230.402 273.315 1.00 15.61  ? 2769 LEU A O     1 
ATOM   9676  C  CB    . LEU A 1 2769 ? 237.479 230.863 276.468 1.00 15.93  ? 2769 LEU A CB    1 
ATOM   9677  C  CG    . LEU A 1 2769 ? 236.196 230.295 275.857 1.00 15.33  ? 2769 LEU A CG    1 
ATOM   9678  C  CD1   . LEU A 1 2769 ? 236.069 228.814 276.168 1.00 15.92  ? 2769 LEU A CD1   1 
ATOM   9679  C  CD2   . LEU A 1 2769 ? 234.980 231.057 276.357 1.00 9.91   ? 2769 LEU A CD2   1 
ATOM   9680  N  N     . THR A 1 2770 ? 238.664 232.503 274.129 1.00 13.72  ? 2770 THR A N     1 
ATOM   9681  C  CA    . THR A 1 2770 ? 238.638 233.110 272.803 1.00 11.25  ? 2770 THR A CA    1 
ATOM   9682  C  C     . THR A 1 2770 ? 239.755 232.557 271.932 1.00 9.76   ? 2770 THR A C     1 
ATOM   9683  O  O     . THR A 1 2770 ? 239.534 232.192 270.771 1.00 10.77  ? 2770 THR A O     1 
ATOM   9684  C  CB    . THR A 1 2770 ? 238.755 234.631 272.920 1.00 11.75  ? 2770 THR A CB    1 
ATOM   9685  O  OG1   . THR A 1 2770 ? 237.689 235.134 273.734 1.00 11.31  ? 2770 THR A OG1   1 
ATOM   9686  C  CG2   . THR A 1 2770 ? 238.689 235.277 271.548 1.00 10.97  ? 2770 THR A CG2   1 
ATOM   9687  N  N     . ALA A 1 2771 ? 240.965 232.460 272.490 1.00 10.56  ? 2771 ALA A N     1 
ATOM   9688  C  CA    . ALA A 1 2771 ? 242.076 231.886 271.742 1.00 10.58  ? 2771 ALA A CA    1 
ATOM   9689  C  C     . ALA A 1 2771 ? 241.757 230.458 271.323 1.00 11.61  ? 2771 ALA A C     1 
ATOM   9690  O  O     . ALA A 1 2771 ? 241.937 230.084 270.158 1.00 12.19  ? 2771 ALA A O     1 
ATOM   9691  C  CB    . ALA A 1 2771 ? 243.355 231.938 272.576 1.00 10.43  ? 2771 ALA A CB    1 
ATOM   9692  N  N     . ALA A 1 2772 ? 241.236 229.656 272.257 1.00 14.16  ? 2772 ALA A N     1 
ATOM   9693  C  CA    . ALA A 1 2772 ? 240.817 228.304 271.909 1.00 12.77  ? 2772 ALA A CA    1 
ATOM   9694  C  C     . ALA A 1 2772 ? 239.724 228.329 270.855 1.00 13.28  ? 2772 ALA A C     1 
ATOM   9695  O  O     . ALA A 1 2772 ? 239.663 227.438 269.998 1.00 16.08  ? 2772 ALA A O     1 
ATOM   9696  C  CB    . ALA A 1 2772 ? 240.341 227.564 273.158 1.00 11.50  ? 2772 ALA A CB    1 
ATOM   9697  N  N     . MET A 1 2773 ? 238.856 229.340 270.899 1.00 13.57  ? 2773 MET A N     1 
ATOM   9698  C  CA    . MET A 1 2773 ? 237.879 229.527 269.836 1.00 9.06   ? 2773 MET A CA    1 
ATOM   9699  C  C     . MET A 1 2773 ? 238.564 229.847 268.514 1.00 12.37  ? 2773 MET A C     1 
ATOM   9700  O  O     . MET A 1 2773 ? 238.203 229.295 267.470 1.00 14.16  ? 2773 MET A O     1 
ATOM   9701  C  CB    . MET A 1 2773 ? 236.913 230.647 270.214 1.00 9.66   ? 2773 MET A CB    1 
ATOM   9702  C  CG    . MET A 1 2773 ? 235.783 230.239 271.138 1.00 9.92   ? 2773 MET A CG    1 
ATOM   9703  S  SD    . MET A 1 2773 ? 234.293 231.184 270.781 1.00 30.03  ? 2773 MET A SD    1 
ATOM   9704  C  CE    . MET A 1 2773 ? 233.096 230.326 271.789 1.00 12.86  ? 2773 MET A CE    1 
ATOM   9705  N  N     . VAL A 1 2774 ? 239.560 230.737 268.544 1.00 14.43  ? 2774 VAL A N     1 
ATOM   9706  C  CA    . VAL A 1 2774 ? 240.141 231.237 267.303 1.00 12.38  ? 2774 VAL A CA    1 
ATOM   9707  C  C     . VAL A 1 2774 ? 241.000 230.172 266.638 1.00 14.47  ? 2774 VAL A C     1 
ATOM   9708  O  O     . VAL A 1 2774 ? 240.925 229.969 265.419 1.00 19.99  ? 2774 VAL A O     1 
ATOM   9709  C  CB    . VAL A 1 2774 ? 240.938 232.527 267.573 1.00 12.59  ? 2774 VAL A CB    1 
ATOM   9710  C  CG1   . VAL A 1 2774 ? 241.848 232.851 266.397 1.00 13.35  ? 2774 VAL A CG1   1 
ATOM   9711  C  CG2   . VAL A 1 2774 ? 239.992 233.682 267.850 1.00 13.18  ? 2774 VAL A CG2   1 
ATOM   9712  N  N     . GLU A 1 2775 ? 241.824 229.473 267.419 1.00 14.23  ? 2775 GLU A N     1 
ATOM   9713  C  CA    . GLU A 1 2775 ? 242.759 228.516 266.837 1.00 15.00  ? 2775 GLU A CA    1 
ATOM   9714  C  C     . GLU A 1 2775 ? 242.027 227.367 266.157 1.00 16.07  ? 2775 GLU A C     1 
ATOM   9715  O  O     . GLU A 1 2775 ? 242.250 227.090 264.972 1.00 20.25  ? 2775 GLU A O     1 
ATOM   9716  C  CB    . GLU A 1 2775 ? 243.702 227.985 267.916 1.00 19.28  ? 2775 GLU A CB    1 
ATOM   9717  C  CG    . GLU A 1 2775 ? 244.420 226.704 267.528 1.00 22.44  ? 2775 GLU A CG    1 
ATOM   9718  C  CD    . GLU A 1 2775 ? 245.581 226.386 268.443 1.00 33.41  ? 2775 GLU A CD    1 
ATOM   9719  O  OE1   . GLU A 1 2775 ? 245.419 226.510 269.675 1.00 33.26  ? 2775 GLU A OE1   1 
ATOM   9720  O  OE2   . GLU A 1 2775 ? 246.655 226.011 267.931 1.00 44.86  ? 2775 GLU A OE2   1 
ATOM   9721  N  N     . PHE A 1 2776 ? 241.116 226.712 266.882 1.00 14.04  ? 2776 PHE A N     1 
ATOM   9722  C  CA    . PHE A 1 2776 ? 240.445 225.537 266.335 1.00 13.06  ? 2776 PHE A CA    1 
ATOM   9723  C  C     . PHE A 1 2776 ? 239.669 225.891 265.075 1.00 14.25  ? 2776 PHE A C     1 
ATOM   9724  O  O     . PHE A 1 2776 ? 239.780 225.207 264.051 1.00 17.56  ? 2776 PHE A O     1 
ATOM   9725  C  CB    . PHE A 1 2776 ? 239.516 224.920 267.381 1.00 13.41  ? 2776 PHE A CB    1 
ATOM   9726  C  CG    . PHE A 1 2776 ? 238.748 223.737 266.873 1.00 14.90  ? 2776 PHE A CG    1 
ATOM   9727  C  CD1   . PHE A 1 2776 ? 239.411 222.611 266.417 1.00 18.81  ? 2776 PHE A CD1   1 
ATOM   9728  C  CD2   . PHE A 1 2776 ? 237.367 223.757 266.826 1.00 16.09  ? 2776 PHE A CD2   1 
ATOM   9729  C  CE1   . PHE A 1 2776 ? 238.712 221.524 265.939 1.00 21.16  ? 2776 PHE A CE1   1 
ATOM   9730  C  CE2   . PHE A 1 2776 ? 236.662 222.673 266.347 1.00 12.76  ? 2776 PHE A CE2   1 
ATOM   9731  C  CZ    . PHE A 1 2776 ? 237.335 221.557 265.902 1.00 13.04  ? 2776 PHE A CZ    1 
ATOM   9732  N  N     . TYR A 1 2777 ? 238.903 226.986 265.125 1.00 14.24  ? 2777 TYR A N     1 
ATOM   9733  C  CA    . TYR A 1 2777 ? 238.175 227.443 263.948 1.00 13.11  ? 2777 TYR A CA    1 
ATOM   9734  C  C     . TYR A 1 2777 ? 239.115 227.637 262.770 1.00 14.19  ? 2777 TYR A C     1 
ATOM   9735  O  O     . TYR A 1 2777 ? 238.768 227.319 261.626 1.00 18.22  ? 2777 TYR A O     1 
ATOM   9736  C  CB    . TYR A 1 2777 ? 237.441 228.749 264.254 1.00 11.41  ? 2777 TYR A CB    1 
ATOM   9737  C  CG    . TYR A 1 2777 ? 237.195 229.605 263.032 1.00 13.10  ? 2777 TYR A CG    1 
ATOM   9738  C  CD1   . TYR A 1 2777 ? 236.176 229.298 262.141 1.00 12.37  ? 2777 TYR A CD1   1 
ATOM   9739  C  CD2   . TYR A 1 2777 ? 237.995 230.706 262.756 1.00 14.01  ? 2777 TYR A CD2   1 
ATOM   9740  C  CE1   . TYR A 1 2777 ? 235.950 230.071 261.023 1.00 10.09  ? 2777 TYR A CE1   1 
ATOM   9741  C  CE2   . TYR A 1 2777 ? 237.776 231.484 261.637 1.00 10.00  ? 2777 TYR A CE2   1 
ATOM   9742  C  CZ    . TYR A 1 2777 ? 236.752 231.162 260.775 1.00 9.99   ? 2777 TYR A CZ    1 
ATOM   9743  O  OH    . TYR A 1 2777 ? 236.531 231.935 259.658 1.00 11.88  ? 2777 TYR A OH    1 
ATOM   9744  N  N     . THR A 1 2778 ? 240.314 228.164 263.030 1.00 12.76  ? 2778 THR A N     1 
ATOM   9745  C  CA    . THR A 1 2778 ? 241.300 228.292 261.966 1.00 13.35  ? 2778 THR A CA    1 
ATOM   9746  C  C     . THR A 1 2778 ? 241.692 226.921 261.434 1.00 16.90  ? 2778 THR A C     1 
ATOM   9747  O  O     . THR A 1 2778 ? 241.631 226.669 260.224 1.00 21.31  ? 2778 THR A O     1 
ATOM   9748  C  CB    . THR A 1 2778 ? 242.528 229.045 262.475 1.00 18.17  ? 2778 THR A CB    1 
ATOM   9749  O  OG1   . THR A 1 2778 ? 242.118 230.282 263.071 1.00 17.40  ? 2778 THR A OG1   1 
ATOM   9750  C  CG2   . THR A 1 2778 ? 243.489 229.331 261.333 1.00 18.68  ? 2778 THR A CG2   1 
ATOM   9751  N  N     . MET A 1 2779 ? 242.046 226.004 262.340 1.00 16.42  ? 2779 MET A N     1 
ATOM   9752  C  CA    . MET A 1 2779 ? 242.553 224.700 261.925 1.00 13.02  ? 2779 MET A CA    1 
ATOM   9753  C  C     . MET A 1 2779 ? 241.539 223.978 261.050 1.00 14.65  ? 2779 MET A C     1 
ATOM   9754  O  O     . MET A 1 2779 ? 241.859 223.543 259.937 1.00 20.94  ? 2779 MET A O     1 
ATOM   9755  C  CB    . MET A 1 2779 ? 242.898 223.865 263.157 1.00 17.82  ? 2779 MET A CB    1 
ATOM   9756  C  CG    . MET A 1 2779 ? 244.062 224.410 263.964 1.00 23.84  ? 2779 MET A CG    1 
ATOM   9757  S  SD    . MET A 1 2779 ? 244.383 223.447 265.452 1.00 39.33  ? 2779 MET A SD    1 
ATOM   9758  C  CE    . MET A 1 2779 ? 245.040 221.945 264.739 1.00 22.65  ? 2779 MET A CE    1 
ATOM   9759  N  N     . SER A 1 2780 ? 240.295 223.886 261.523 1.00 13.34  ? 2780 SER A N     1 
ATOM   9760  C  CA    . SER A 1 2780 ? 239.243 223.264 260.727 1.00 12.74  ? 2780 SER A CA    1 
ATOM   9761  C  C     . SER A 1 2780 ? 239.107 223.952 259.377 1.00 13.05  ? 2780 SER A C     1 
ATOM   9762  O  O     . SER A 1 2780 ? 238.983 223.285 258.343 1.00 13.12  ? 2780 SER A O     1 
ATOM   9763  C  CB    . SER A 1 2780 ? 237.920 223.306 261.487 1.00 12.27  ? 2780 SER A CB    1 
ATOM   9764  O  OG    . SER A 1 2780 ? 238.023 222.627 262.725 1.00 22.70  ? 2780 SER A OG    1 
ATOM   9765  N  N     . GLN A 1 2781 ? 239.163 225.288 259.363 1.00 12.09  ? 2781 GLN A N     1 
ATOM   9766  C  CA    . GLN A 1 2781 ? 239.045 226.012 258.104 1.00 11.68  ? 2781 GLN A CA    1 
ATOM   9767  C  C     . GLN A 1 2781 ? 240.144 225.611 257.135 1.00 14.47  ? 2781 GLN A C     1 
ATOM   9768  O  O     . GLN A 1 2781 ? 239.912 225.552 255.922 1.00 17.31  ? 2781 GLN A O     1 
ATOM   9769  C  CB    . GLN A 1 2781 ? 239.075 227.519 258.358 1.00 10.48  ? 2781 GLN A CB    1 
ATOM   9770  C  CG    . GLN A 1 2781 ? 238.465 228.344 257.239 1.00 9.21   ? 2781 GLN A CG    1 
ATOM   9771  C  CD    . GLN A 1 2781 ? 238.591 229.832 257.480 1.00 20.23  ? 2781 GLN A CD    1 
ATOM   9772  O  OE1   . GLN A 1 2781 ? 237.656 230.594 257.240 1.00 18.00  ? 2781 GLN A OE1   1 
ATOM   9773  N  NE2   . GLN A 1 2781 ? 239.754 230.255 257.959 1.00 27.12  ? 2781 GLN A NE2   1 
ATOM   9774  N  N     . GLU A 1 2782 ? 241.342 225.327 257.646 1.00 12.89  ? 2782 GLU A N     1 
ATOM   9775  C  CA    . GLU A 1 2782 ? 242.399 224.819 256.783 1.00 15.28  ? 2782 GLU A CA    1 
ATOM   9776  C  C     . GLU A 1 2782 ? 242.194 223.343 256.468 1.00 17.00  ? 2782 GLU A C     1 
ATOM   9777  O  O     . GLU A 1 2782 ? 242.482 222.898 255.351 1.00 15.42  ? 2782 GLU A O     1 
ATOM   9778  C  CB    . GLU A 1 2782 ? 243.763 225.048 257.435 1.00 18.88  ? 2782 GLU A CB    1 
ATOM   9779  C  CG    . GLU A 1 2782 ? 244.945 224.589 256.593 1.00 31.87  ? 2782 GLU A CG    1 
ATOM   9780  C  CD    . GLU A 1 2782 ? 245.097 225.380 255.308 1.00 42.21  ? 2782 GLU A CD    1 
ATOM   9781  O  OE1   . GLU A 1 2782 ? 244.649 226.545 255.264 1.00 44.75  ? 2782 GLU A OE1   1 
ATOM   9782  O  OE2   . GLU A 1 2782 ? 245.662 224.832 254.338 1.00 48.17  ? 2782 GLU A OE2   1 
ATOM   9783  N  N     . ARG A 1 2783 ? 241.690 222.571 257.434 1.00 17.04  ? 2783 ARG A N     1 
ATOM   9784  C  CA    . ARG A 1 2783 ? 241.626 221.124 257.261 1.00 13.54  ? 2783 ARG A CA    1 
ATOM   9785  C  C     . ARG A 1 2783 ? 240.507 220.724 256.307 1.00 15.45  ? 2783 ARG A C     1 
ATOM   9786  O  O     . ARG A 1 2783 ? 240.699 219.874 255.432 1.00 14.16  ? 2783 ARG A O     1 
ATOM   9787  C  CB    . ARG A 1 2783 ? 241.445 220.443 258.617 1.00 12.73  ? 2783 ARG A CB    1 
ATOM   9788  C  CG    . ARG A 1 2783 ? 241.194 218.952 258.522 1.00 17.54  ? 2783 ARG A CG    1 
ATOM   9789  C  CD    . ARG A 1 2783 ? 242.443 218.211 258.072 1.00 18.85  ? 2783 ARG A CD    1 
ATOM   9790  N  NE    . ARG A 1 2783 ? 242.348 216.779 258.323 1.00 27.59  ? 2783 ARG A NE    1 
ATOM   9791  C  CZ    . ARG A 1 2783 ? 241.627 215.936 257.596 1.00 31.25  ? 2783 ARG A CZ    1 
ATOM   9792  N  NH1   . ARG A 1 2783 ? 240.938 216.346 256.543 1.00 26.80  ? 2783 ARG A NH1   1 
ATOM   9793  N  NH2   . ARG A 1 2783 ? 241.597 214.650 257.932 1.00 33.80  ? 2783 ARG A NH2   1 
ATOM   9794  N  N     . PHE A 1 2784 ? 239.333 221.327 256.459 1.00 15.92  ? 2784 PHE A N     1 
ATOM   9795  C  CA    . PHE A 1 2784 ? 238.161 220.988 255.660 1.00 12.42  ? 2784 PHE A CA    1 
ATOM   9796  C  C     . PHE A 1 2784 ? 237.852 222.156 254.736 1.00 17.24  ? 2784 PHE A C     1 
ATOM   9797  O  O     . PHE A 1 2784 ? 237.473 223.237 255.197 1.00 21.41  ? 2784 PHE A O     1 
ATOM   9798  C  CB    . PHE A 1 2784 ? 236.968 220.659 256.555 1.00 12.67  ? 2784 PHE A CB    1 
ATOM   9799  C  CG    . PHE A 1 2784 ? 237.297 219.717 257.675 1.00 12.65  ? 2784 PHE A CG    1 
ATOM   9800  C  CD1   . PHE A 1 2784 ? 237.668 218.410 257.409 1.00 12.81  ? 2784 PHE A CD1   1 
ATOM   9801  C  CD2   . PHE A 1 2784 ? 237.238 220.136 258.992 1.00 13.44  ? 2784 PHE A CD2   1 
ATOM   9802  C  CE1   . PHE A 1 2784 ? 237.973 217.541 258.434 1.00 14.36  ? 2784 PHE A CE1   1 
ATOM   9803  C  CE2   . PHE A 1 2784 ? 237.541 219.272 260.021 1.00 13.54  ? 2784 PHE A CE2   1 
ATOM   9804  C  CZ    . PHE A 1 2784 ? 237.908 217.971 259.742 1.00 17.63  ? 2784 PHE A CZ    1 
ATOM   9805  N  N     . THR A 1 2785 ? 238.015 221.936 253.438 1.00 19.76  ? 2785 THR A N     1 
ATOM   9806  C  CA    . THR A 1 2785 ? 237.784 222.952 252.425 1.00 17.72  ? 2785 THR A CA    1 
ATOM   9807  C  C     . THR A 1 2785 ? 236.697 222.483 251.467 1.00 17.85  ? 2785 THR A C     1 
ATOM   9808  O  O     . THR A 1 2785 ? 236.259 221.330 251.500 1.00 19.78  ? 2785 THR A O     1 
ATOM   9809  C  CB    . THR A 1 2785 ? 239.072 223.267 251.653 1.00 23.48  ? 2785 THR A CB    1 
ATOM   9810  O  OG1   . THR A 1 2785 ? 239.482 222.111 250.913 1.00 30.59  ? 2785 THR A OG1   1 
ATOM   9811  C  CG2   . THR A 1 2785 ? 240.183 223.665 252.612 1.00 17.29  ? 2785 THR A CG2   1 
ATOM   9812  N  N     . GLN A 1 2786 ? 236.266 223.398 250.599 1.00 22.36  ? 2786 GLN A N     1 
ATOM   9813  C  CA    . GLN A 1 2786 ? 235.255 223.072 249.602 1.00 22.15  ? 2786 GLN A CA    1 
ATOM   9814  C  C     . GLN A 1 2786 ? 235.764 222.095 248.551 1.00 24.01  ? 2786 GLN A C     1 
ATOM   9815  O  O     . GLN A 1 2786 ? 234.955 221.561 247.784 1.00 24.31  ? 2786 GLN A O     1 
ATOM   9816  C  CB    . GLN A 1 2786 ? 234.756 224.351 248.929 1.00 18.34  ? 2786 GLN A CB    1 
ATOM   9817  C  CG    . GLN A 1 2786 ? 233.307 224.291 248.482 1.00 21.51  ? 2786 GLN A CG    1 
ATOM   9818  C  CD    . GLN A 1 2786 ? 232.800 225.622 247.965 1.00 28.95  ? 2786 GLN A CD    1 
ATOM   9819  O  OE1   . GLN A 1 2786 ? 233.564 226.574 247.813 1.00 36.91  ? 2786 GLN A OE1   1 
ATOM   9820  N  NE2   . GLN A 1 2786 ? 231.502 225.694 247.695 1.00 31.91  ? 2786 GLN A NE2   1 
ATOM   9821  N  N     . ASP A 1 2787 ? 237.075 221.854 248.493 1.00 24.08  ? 2787 ASP A N     1 
ATOM   9822  C  CA    . ASP A 1 2787 ? 237.611 220.870 247.560 1.00 25.55  ? 2787 ASP A CA    1 
ATOM   9823  C  C     . ASP A 1 2787 ? 237.132 219.464 247.902 1.00 25.91  ? 2787 ASP A C     1 
ATOM   9824  O  O     . ASP A 1 2787 ? 236.839 218.668 247.004 1.00 29.27  ? 2787 ASP A O     1 
ATOM   9825  C  CB    . ASP A 1 2787 ? 239.138 220.932 247.554 1.00 30.39  ? 2787 ASP A CB    1 
ATOM   9826  C  CG    . ASP A 1 2787 ? 239.683 221.750 246.399 1.00 54.66  ? 2787 ASP A CG    1 
ATOM   9827  O  OD1   . ASP A 1 2787 ? 238.880 222.188 245.548 1.00 51.69  ? 2787 ASP A OD1   1 
ATOM   9828  O  OD2   . ASP A 1 2787 ? 240.913 221.953 246.339 1.00 65.47  ? 2787 ASP A OD2   1 
ATOM   9829  N  N     . THR A 1 2788 ? 237.054 219.138 249.194 1.00 26.17  ? 2788 THR A N     1 
ATOM   9830  C  CA    . THR A 1 2788 ? 236.591 217.815 249.602 1.00 20.85  ? 2788 THR A CA    1 
ATOM   9831  C  C     . THR A 1 2788 ? 235.084 217.679 249.417 1.00 17.58  ? 2788 THR A C     1 
ATOM   9832  O  O     . THR A 1 2788 ? 234.613 216.845 248.636 1.00 15.98  ? 2788 THR A O     1 
ATOM   9833  C  CB    . THR A 1 2788 ? 236.981 217.547 251.056 1.00 21.10  ? 2788 THR A CB    1 
ATOM   9834  O  OG1   . THR A 1 2788 ? 238.349 217.919 251.262 1.00 32.57  ? 2788 THR A OG1   1 
ATOM   9835  C  CG2   . THR A 1 2788 ? 236.805 216.075 251.392 1.00 22.60  ? 2788 THR A CG2   1 
ATOM   9836  N  N     . GLN A 1 2789 ? 234.311 218.494 250.129 1.00 18.85  ? 2789 GLN A N     1 
ATOM   9837  C  CA    . GLN A 1 2789 ? 232.861 218.478 250.036 1.00 17.83  ? 2789 GLN A CA    1 
ATOM   9838  C  C     . GLN A 1 2789 ? 232.337 219.892 249.844 1.00 17.56  ? 2789 GLN A C     1 
ATOM   9839  O  O     . GLN A 1 2789 ? 232.923 220.851 250.355 1.00 18.50  ? 2789 GLN A O     1 
ATOM   9840  C  CB    . GLN A 1 2789 ? 232.230 217.859 251.292 1.00 12.01  ? 2789 GLN A CB    1 
ATOM   9841  C  CG    . GLN A 1 2789 ? 232.778 216.489 251.648 1.00 13.84  ? 2789 GLN A CG    1 
ATOM   9842  C  CD    . GLN A 1 2789 ? 232.112 215.369 250.874 1.00 14.00  ? 2789 GLN A CD    1 
ATOM   9843  O  OE1   . GLN A 1 2789 ? 231.041 215.548 250.298 1.00 13.54  ? 2789 GLN A OE1   1 
ATOM   9844  N  NE2   . GLN A 1 2789 ? 232.750 214.207 250.853 1.00 15.40  ? 2789 GLN A NE2   1 
ATOM   9845  N  N     . PRO A 1 2790 ? 231.235 220.049 249.107 1.00 20.17  ? 2790 PRO A N     1 
ATOM   9846  C  CA    . PRO A 1 2790 ? 230.714 221.402 248.848 1.00 19.87  ? 2790 PRO A CA    1 
ATOM   9847  C  C     . PRO A 1 2790 ? 230.310 222.160 250.098 1.00 17.88  ? 2790 PRO A C     1 
ATOM   9848  O  O     . PRO A 1 2790 ? 230.435 223.391 250.131 1.00 16.80  ? 2790 PRO A O     1 
ATOM   9849  C  CB    . PRO A 1 2790 ? 229.508 221.140 247.934 1.00 23.90  ? 2790 PRO A CB    1 
ATOM   9850  C  CG    . PRO A 1 2790 ? 229.128 219.723 248.198 1.00 22.82  ? 2790 PRO A CG    1 
ATOM   9851  C  CD    . PRO A 1 2790 ? 230.415 219.011 248.461 1.00 19.23  ? 2790 PRO A CD    1 
ATOM   9852  N  N     . HIS A 1 2791 ? 229.828 221.472 251.129 1.00 20.07  ? 2791 HIS A N     1 
ATOM   9853  C  CA    . HIS A 1 2791 ? 229.320 222.125 252.327 1.00 13.49  ? 2791 HIS A CA    1 
ATOM   9854  C  C     . HIS A 1 2791 ? 230.401 222.421 253.357 1.00 12.07  ? 2791 HIS A C     1 
ATOM   9855  O  O     . HIS A 1 2791 ? 230.093 223.000 254.403 1.00 17.73  ? 2791 HIS A O     1 
ATOM   9856  C  CB    . HIS A 1 2791 ? 228.221 221.270 252.967 1.00 11.48  ? 2791 HIS A CB    1 
ATOM   9857  C  CG    . HIS A 1 2791 ? 228.656 219.876 253.294 1.00 13.99  ? 2791 HIS A CG    1 
ATOM   9858  N  ND1   . HIS A 1 2791 ? 228.745 218.882 252.345 1.00 16.16  ? 2791 HIS A ND1   1 
ATOM   9859  C  CD2   . HIS A 1 2791 ? 229.021 219.308 254.468 1.00 13.02  ? 2791 HIS A CD2   1 
ATOM   9860  C  CE1   . HIS A 1 2791 ? 229.150 217.763 252.918 1.00 16.71  ? 2791 HIS A CE1   1 
ATOM   9861  N  NE2   . HIS A 1 2791 ? 229.326 217.995 254.206 1.00 14.93  ? 2791 HIS A NE2   1 
ATOM   9862  N  N     . TYR A 1 2792 ? 231.654 222.049 253.095 1.00 10.22  ? 2792 TYR A N     1 
ATOM   9863  C  CA    . TYR A 1 2792 ? 232.748 222.301 254.034 1.00 11.59  ? 2792 TYR A CA    1 
ATOM   9864  C  C     . TYR A 1 2792 ? 233.151 223.775 253.962 1.00 15.15  ? 2792 TYR A C     1 
ATOM   9865  O  O     . TYR A 1 2792 ? 234.218 224.148 253.473 1.00 19.81  ? 2792 TYR A O     1 
ATOM   9866  C  CB    . TYR A 1 2792 ? 233.931 221.390 253.742 1.00 12.81  ? 2792 TYR A CB    1 
ATOM   9867  C  CG    . TYR A 1 2792 ? 233.758 219.962 254.203 1.00 14.87  ? 2792 TYR A CG    1 
ATOM   9868  C  CD1   . TYR A 1 2792 ? 232.603 219.554 254.857 1.00 15.12  ? 2792 TYR A CD1   1 
ATOM   9869  C  CD2   . TYR A 1 2792 ? 234.754 219.023 253.988 1.00 15.32  ? 2792 TYR A CD2   1 
ATOM   9870  C  CE1   . TYR A 1 2792 ? 232.446 218.249 255.277 1.00 13.69  ? 2792 TYR A CE1   1 
ATOM   9871  C  CE2   . TYR A 1 2792 ? 234.606 217.718 254.405 1.00 17.41  ? 2792 TYR A CE2   1 
ATOM   9872  C  CZ    . TYR A 1 2792 ? 233.452 217.336 255.047 1.00 16.42  ? 2792 TYR A CZ    1 
ATOM   9873  O  OH    . TYR A 1 2792 ? 233.305 216.034 255.464 1.00 19.73  ? 2792 TYR A OH    1 
ATOM   9874  N  N     . ILE A 1 2793 ? 232.261 224.621 254.469 1.00 13.72  ? 2793 ILE A N     1 
ATOM   9875  C  CA    . ILE A 1 2793 ? 232.461 226.065 254.491 1.00 11.41  ? 2793 ILE A CA    1 
ATOM   9876  C  C     . ILE A 1 2793 ? 232.460 226.512 255.944 1.00 9.33   ? 2793 ILE A C     1 
ATOM   9877  O  O     . ILE A 1 2793 ? 231.491 226.266 256.673 1.00 11.16  ? 2793 ILE A O     1 
ATOM   9878  C  CB    . ILE A 1 2793 ? 231.379 226.805 253.690 1.00 12.27  ? 2793 ILE A CB    1 
ATOM   9879  C  CG1   . ILE A 1 2793 ? 231.443 226.410 252.215 1.00 12.97  ? 2793 ILE A CG1   1 
ATOM   9880  C  CG2   . ILE A 1 2793 ? 231.536 228.308 253.849 1.00 11.21  ? 2793 ILE A CG2   1 
ATOM   9881  C  CD1   . ILE A 1 2793 ? 230.261 226.888 251.408 1.00 18.51  ? 2793 ILE A CD1   1 
ATOM   9882  N  N     . TYR A 1 2794 ? 233.538 227.165 256.362 1.00 7.98   ? 2794 TYR A N     1 
ATOM   9883  C  CA    . TYR A 1 2794 ? 233.676 227.664 257.722 1.00 8.14   ? 2794 TYR A CA    1 
ATOM   9884  C  C     . TYR A 1 2794 ? 233.940 229.159 257.681 1.00 9.69   ? 2794 TYR A C     1 
ATOM   9885  O  O     . TYR A 1 2794 ? 234.809 229.623 256.934 1.00 11.73  ? 2794 TYR A O     1 
ATOM   9886  C  CB    . TYR A 1 2794 ? 234.794 226.930 258.463 1.00 9.00   ? 2794 TYR A CB    1 
ATOM   9887  C  CG    . TYR A 1 2794 ? 234.507 225.460 258.643 1.00 12.31  ? 2794 TYR A CG    1 
ATOM   9888  C  CD1   . TYR A 1 2794 ? 233.564 225.028 259.564 1.00 14.47  ? 2794 TYR A CD1   1 
ATOM   9889  C  CD2   . TYR A 1 2794 ? 235.165 224.505 257.884 1.00 15.03  ? 2794 TYR A CD2   1 
ATOM   9890  C  CE1   . TYR A 1 2794 ? 233.291 223.688 259.730 1.00 13.23  ? 2794 TYR A CE1   1 
ATOM   9891  C  CE2   . TYR A 1 2794 ? 234.899 223.160 258.044 1.00 13.96  ? 2794 TYR A CE2   1 
ATOM   9892  C  CZ    . TYR A 1 2794 ? 233.961 222.758 258.969 1.00 15.95  ? 2794 TYR A CZ    1 
ATOM   9893  O  OH    . TYR A 1 2794 ? 233.691 221.419 259.133 1.00 28.81  ? 2794 TYR A OH    1 
ATOM   9894  N  N     . SER A 1 2795 ? 233.172 229.908 258.475 1.00 8.40   ? 2795 SER A N     1 
ATOM   9895  C  CA    . SER A 1 2795 ? 233.295 231.386 258.466 1.00 7.83   ? 2795 SER A CA    1 
ATOM   9896  C  C     . SER A 1 2795 ? 233.069 231.919 259.884 1.00 10.16  ? 2795 SER A C     1 
ATOM   9897  O  O     . SER A 1 2795 ? 232.660 231.124 260.753 1.00 9.42   ? 2795 SER A O     1 
ATOM   9898  C  CB    . SER A 1 2795 ? 232.305 231.972 257.509 1.00 9.11   ? 2795 SER A CB    1 
ATOM   9899  O  OG    . SER A 1 2795 ? 230.980 231.636 257.892 1.00 14.20  ? 2795 SER A OG    1 
ATOM   9900  N  N     . PRO A 1 2796 ? 233.291 233.222 260.162 1.00 8.58   ? 2796 PRO A N     1 
ATOM   9901  C  CA    . PRO A 1 2796 ? 233.002 233.766 261.480 1.00 8.57   ? 2796 PRO A CA    1 
ATOM   9902  C  C     . PRO A 1 2796 ? 231.584 233.443 261.927 1.00 8.58   ? 2796 PRO A C     1 
ATOM   9903  O  O     . PRO A 1 2796 ? 231.305 233.498 263.139 1.00 12.33  ? 2796 PRO A O     1 
ATOM   9904  C  CB    . PRO A 1 2796 ? 233.213 235.266 261.262 1.00 9.35   ? 2796 PRO A CB    1 
ATOM   9905  C  CG    . PRO A 1 2796 ? 234.261 235.327 260.182 1.00 8.19   ? 2796 PRO A CG    1 
ATOM   9906  C  CD    . PRO A 1 2796 ? 233.879 234.193 259.252 1.00 5.90   ? 2796 PRO A CD    1 
ATOM   9907  N  N     . ARG A 1 2797 ? 230.702 233.119 260.978 1.00 9.05   ? 2797 ARG A N     1 
ATOM   9908  C  CA    . ARG A 1 2797 ? 229.292 232.794 261.314 1.00 8.99   ? 2797 ARG A CA    1 
ATOM   9909  C  C     . ARG A 1 2797 ? 229.271 231.589 262.267 1.00 11.76  ? 2797 ARG A C     1 
ATOM   9910  O  O     . ARG A 1 2797 ? 228.496 231.623 263.245 1.00 12.78  ? 2797 ARG A O     1 
ATOM   9911  C  CB    . ARG A 1 2797 ? 228.497 232.535 260.031 1.00 7.40   ? 2797 ARG A CB    1 
ATOM   9912  C  CG    . ARG A 1 2797 ? 226.986 232.584 260.201 1.00 10.38  ? 2797 ARG A CG    1 
ATOM   9913  C  CD    . ARG A 1 2797 ? 226.327 233.187 258.972 1.00 8.98   ? 2797 ARG A CD    1 
ATOM   9914  N  NE    . ARG A 1 2797 ? 226.782 232.548 257.733 1.00 15.44  ? 2797 ARG A NE    1 
ATOM   9915  C  CZ    . ARG A 1 2797 ? 226.385 232.901 256.517 1.00 20.66  ? 2797 ARG A CZ    1 
ATOM   9916  N  NH1   . ARG A 1 2797 ? 225.494 233.864 256.369 1.00 11.59  ? 2797 ARG A NH1   1 
ATOM   9917  N  NH2   . ARG A 1 2797 ? 226.883 232.292 255.456 1.00 20.19  ? 2797 ARG A NH2   1 
ATOM   9918  N  N     . GLU A 1 2798 ? 230.104 230.578 262.002 1.00 12.84  ? 2798 GLU A N     1 
ATOM   9919  C  CA    . GLU A 1 2798 ? 230.186 229.405 262.910 1.00 8.98   ? 2798 GLU A CA    1 
ATOM   9920  C  C     . GLU A 1 2798 ? 230.604 229.891 264.303 1.00 8.78   ? 2798 GLU A C     1 
ATOM   9921  O  O     . GLU A 1 2798 ? 229.960 229.489 265.291 1.00 12.25  ? 2798 GLU A O     1 
ATOM   9922  C  CB    . GLU A 1 2798 ? 231.201 228.376 262.414 1.00 12.19  ? 2798 GLU A CB    1 
ATOM   9923  C  CG    . GLU A 1 2798 ? 231.183 228.180 260.901 1.00 15.18  ? 2798 GLU A CG    1 
ATOM   9924  C  CD    . GLU A 1 2798 ? 229.989 227.426 260.348 1.00 20.37  ? 2798 GLU A CD    1 
ATOM   9925  O  OE1   . GLU A 1 2798 ? 229.131 226.986 261.141 1.00 30.83  ? 2798 GLU A OE1   1 
ATOM   9926  O  OE2   . GLU A 1 2798 ? 229.919 227.278 259.110 1.00 18.03  ? 2798 GLU A OE2   1 
ATOM   9927  N  N     . MET A 1 2799 ? 231.636 230.734 264.371 1.00 10.15  ? 2799 MET A N     1 
ATOM   9928  C  CA    . MET A 1 2799 ? 232.135 231.230 265.679 1.00 11.40  ? 2799 MET A CA    1 
ATOM   9929  C  C     . MET A 1 2799 ? 231.035 232.050 266.370 1.00 9.04   ? 2799 MET A C     1 
ATOM   9930  O  O     . MET A 1 2799 ? 230.917 231.956 267.608 1.00 13.18  ? 2799 MET A O     1 
ATOM   9931  C  CB    . MET A 1 2799 ? 233.388 232.092 265.502 1.00 10.18  ? 2799 MET A CB    1 
ATOM   9932  C  CG    . MET A 1 2799 ? 234.583 231.336 264.964 1.00 11.30  ? 2799 MET A CG    1 
ATOM   9933  S  SD    . MET A 1 2799 ? 236.101 232.293 265.141 1.00 46.36  ? 2799 MET A SD    1 
ATOM   9934  C  CE    . MET A 1 2799 ? 236.129 232.527 266.924 1.00 13.54  ? 2799 MET A CE    1 
ATOM   9935  N  N     . THR A 1 2800 ? 230.266 232.826 265.602 1.00 7.31   ? 2800 THR A N     1 
ATOM   9936  C  CA    . THR A 1 2800 ? 229.159 233.605 266.196 1.00 8.49   ? 2800 THR A CA    1 
ATOM   9937  C  C     . THR A 1 2800 ? 228.198 232.638 266.846 1.00 10.23  ? 2800 THR A C     1 
ATOM   9938  O  O     . THR A 1 2800 ? 227.810 232.879 268.008 1.00 12.81  ? 2800 THR A O     1 
ATOM   9939  C  CB    . THR A 1 2800 ? 228.470 234.440 265.120 1.00 7.57   ? 2800 THR A CB    1 
ATOM   9940  O  OG1   . THR A 1 2800 ? 229.509 235.192 264.503 1.00 11.41  ? 2800 THR A OG1   1 
ATOM   9941  C  CG2   . THR A 1 2800 ? 227.421 235.374 265.696 1.00 7.26   ? 2800 THR A CG2   1 
ATOM   9942  N  N     . ARG A 1 2801 ? 227.836 231.568 266.132 1.00 11.27  ? 2801 ARG A N     1 
ATOM   9943  C  CA    . ARG A 1 2801 ? 226.931 230.537 266.699 1.00 9.94   ? 2801 ARG A CA    1 
ATOM   9944  C  C     . ARG A 1 2801 ? 227.595 229.944 267.947 1.00 11.15  ? 2801 ARG A C     1 
ATOM   9945  O  O     . ARG A 1 2801 ? 226.893 229.758 268.962 1.00 18.30  ? 2801 ARG A O     1 
ATOM   9946  C  CB    . ARG A 1 2801 ? 226.659 229.461 265.645 1.00 10.90  ? 2801 ARG A CB    1 
ATOM   9947  C  CG    . ARG A 1 2801 ? 225.337 228.725 265.801 1.00 18.00  ? 2801 ARG A CG    1 
ATOM   9948  C  CD    . ARG A 1 2801 ? 225.050 227.889 264.565 1.00 31.38  ? 2801 ARG A CD    1 
ATOM   9949  N  NE    . ARG A 1 2801 ? 225.208 228.677 263.338 1.00 39.61  ? 2801 ARG A NE    1 
ATOM   9950  C  CZ    . ARG A 1 2801 ? 226.070 228.397 262.368 1.00 41.67  ? 2801 ARG A CZ    1 
ATOM   9951  N  NH1   . ARG A 1 2801 ? 226.650 227.212 262.321 1.00 27.79  ? 2801 ARG A NH1   1 
ATOM   9952  N  NH2   . ARG A 1 2801 ? 226.347 229.303 261.448 1.00 47.00  ? 2801 ARG A NH2   1 
ATOM   9953  N  N     . TRP A 1 2802 ? 228.900 229.672 267.872 1.00 7.01   ? 2802 TRP A N     1 
ATOM   9954  C  CA    . TRP A 1 2802 ? 229.619 229.132 269.025 1.00 8.24   ? 2802 TRP A CA    1 
ATOM   9955  C  C     . TRP A 1 2802 ? 229.398 229.984 270.266 1.00 9.59   ? 2802 TRP A C     1 
ATOM   9956  O  O     . TRP A 1 2802 ? 229.004 229.479 271.328 1.00 14.21  ? 2802 TRP A O     1 
ATOM   9957  C  CB    . TRP A 1 2802 ? 231.112 229.073 268.697 1.00 10.31  ? 2802 TRP A CB    1 
ATOM   9958  C  CG    . TRP A 1 2802 ? 231.899 228.023 269.409 1.00 9.82   ? 2802 TRP A CG    1 
ATOM   9959  C  CD1   . TRP A 1 2802 ? 231.544 227.356 270.539 1.00 9.20   ? 2802 TRP A CD1   1 
ATOM   9960  C  CD2   . TRP A 1 2802 ? 233.203 227.553 269.055 1.00 8.05   ? 2802 TRP A CD2   1 
ATOM   9961  N  NE1   . TRP A 1 2802 ? 232.537 226.482 270.902 1.00 8.68   ? 2802 TRP A NE1   1 
ATOM   9962  C  CE2   . TRP A 1 2802 ? 233.569 226.586 270.007 1.00 7.62   ? 2802 TRP A CE2   1 
ATOM   9963  C  CE3   . TRP A 1 2802 ? 234.094 227.851 268.020 1.00 11.17  ? 2802 TRP A CE3   1 
ATOM   9964  C  CZ2   . TRP A 1 2802 ? 234.784 225.913 269.954 1.00 8.97   ? 2802 TRP A CZ2   1 
ATOM   9965  C  CZ3   . TRP A 1 2802 ? 235.299 227.181 267.970 1.00 11.32  ? 2802 TRP A CZ3   1 
ATOM   9966  C  CH2   . TRP A 1 2802 ? 235.634 226.223 268.931 1.00 10.23  ? 2802 TRP A CH2   1 
ATOM   9967  N  N     . VAL A 1 2803 ? 229.663 231.285 270.147 1.00 12.29  ? 2803 VAL A N     1 
ATOM   9968  C  CA    . VAL A 1 2803 ? 229.519 232.185 271.285 1.00 12.24  ? 2803 VAL A CA    1 
ATOM   9969  C  C     . VAL A 1 2803 ? 228.067 232.228 271.738 1.00 11.47  ? 2803 VAL A C     1 
ATOM   9970  O  O     . VAL A 1 2803 ? 227.776 232.212 272.939 1.00 14.55  ? 2803 VAL A O     1 
ATOM   9971  C  CB    . VAL A 1 2803 ? 230.051 233.586 270.930 1.00 11.91  ? 2803 VAL A CB    1 
ATOM   9972  C  CG1   . VAL A 1 2803 ? 229.914 234.520 272.114 1.00 11.51  ? 2803 VAL A CG1   1 
ATOM   9973  C  CG2   . VAL A 1 2803 ? 231.500 233.502 270.494 1.00 12.73  ? 2803 VAL A CG2   1 
ATOM   9974  N  N     . ARG A 1 2804 ? 227.134 232.264 270.785 1.00 10.80  ? 2804 ARG A N     1 
ATOM   9975  C  CA    . ARG A 1 2804 ? 225.715 232.303 271.125 1.00 14.78  ? 2804 ARG A CA    1 
ATOM   9976  C  C     . ARG A 1 2804 ? 225.279 231.041 271.864 1.00 14.91  ? 2804 ARG A C     1 
ATOM   9977  O  O     . ARG A 1 2804 ? 224.526 231.116 272.842 1.00 18.97  ? 2804 ARG A O     1 
ATOM   9978  C  CB    . ARG A 1 2804 ? 224.891 232.509 269.855 1.00 17.53  ? 2804 ARG A CB    1 
ATOM   9979  C  CG    . ARG A 1 2804 ? 223.397 232.594 270.079 1.00 22.63  ? 2804 ARG A CG    1 
ATOM   9980  C  CD    . ARG A 1 2804 ? 223.014 233.833 270.864 1.00 38.78  ? 2804 ARG A CD    1 
ATOM   9981  N  NE    . ARG A 1 2804 ? 221.570 233.930 271.037 1.00 44.81  ? 2804 ARG A NE    1 
ATOM   9982  C  CZ    . ARG A 1 2804 ? 220.967 234.817 271.818 1.00 42.83  ? 2804 ARG A CZ    1 
ATOM   9983  N  NH1   . ARG A 1 2804 ? 221.655 235.706 272.513 1.00 37.10  ? 2804 ARG A NH1   1 
ATOM   9984  N  NH2   . ARG A 1 2804 ? 219.639 234.808 271.903 1.00 44.89  ? 2804 ARG A NH2   1 
ATOM   9985  N  N     . GLY A 1 2805 ? 225.741 229.872 271.414 1.00 11.89  ? 2805 GLY A N     1 
ATOM   9986  C  CA    . GLY A 1 2805 ? 225.378 228.634 272.082 1.00 10.43  ? 2805 GLY A CA    1 
ATOM   9987  C  C     . GLY A 1 2805 ? 225.948 228.531 273.482 1.00 13.50  ? 2805 GLY A C     1 
ATOM   9988  O  O     . GLY A 1 2805 ? 225.253 228.115 274.417 1.00 20.18  ? 2805 GLY A O     1 
ATOM   9989  N  N     . ILE A 1 2806 ? 227.219 228.904 273.653 1.00 12.73  ? 2806 ILE A N     1 
ATOM   9990  C  CA    . ILE A 1 2806 ? 227.796 228.894 274.995 1.00 12.24  ? 2806 ILE A CA    1 
ATOM   9991  C  C     . ILE A 1 2806 ? 227.077 229.897 275.889 1.00 14.54  ? 2806 ILE A C     1 
ATOM   9992  O  O     . ILE A 1 2806 ? 226.867 229.649 277.083 1.00 16.07  ? 2806 ILE A O     1 
ATOM   9993  C  CB    . ILE A 1 2806 ? 229.312 229.158 274.940 1.00 10.07  ? 2806 ILE A CB    1 
ATOM   9994  C  CG1   . ILE A 1 2806 ? 229.998 228.101 274.076 1.00 12.61  ? 2806 ILE A CG1   1 
ATOM   9995  C  CG2   . ILE A 1 2806 ? 229.906 229.140 276.337 1.00 7.78   ? 2806 ILE A CG2   1 
ATOM   9996  C  CD1   . ILE A 1 2806 ? 231.503 228.168 274.115 1.00 12.30  ? 2806 ILE A CD1   1 
ATOM   9997  N  N     . PHE A 1 2807 ? 226.669 231.037 275.327 1.00 15.49  ? 2807 PHE A N     1 
ATOM   9998  C  CA    . PHE A 1 2807 ? 225.934 232.026 276.107 1.00 15.25  ? 2807 PHE A CA    1 
ATOM   9999  C  C     . PHE A 1 2807 ? 224.576 231.495 276.546 1.00 18.65  ? 2807 PHE A C     1 
ATOM   10000 O  O     . PHE A 1 2807 ? 224.152 231.722 277.686 1.00 24.79  ? 2807 PHE A O     1 
ATOM   10001 C  CB    . PHE A 1 2807 ? 225.781 233.312 275.296 1.00 19.08  ? 2807 PHE A CB    1 
ATOM   10002 C  CG    . PHE A 1 2807 ? 224.869 234.320 275.926 1.00 24.38  ? 2807 PHE A CG    1 
ATOM   10003 C  CD1   . PHE A 1 2807 ? 225.265 235.023 277.049 1.00 23.76  ? 2807 PHE A CD1   1 
ATOM   10004 C  CD2   . PHE A 1 2807 ? 223.623 234.578 275.384 1.00 25.28  ? 2807 PHE A CD2   1 
ATOM   10005 C  CE1   . PHE A 1 2807 ? 224.430 235.953 277.624 1.00 30.02  ? 2807 PHE A CE1   1 
ATOM   10006 C  CE2   . PHE A 1 2807 ? 222.787 235.509 275.955 1.00 25.66  ? 2807 PHE A CE2   1 
ATOM   10007 C  CZ    . PHE A 1 2807 ? 223.189 236.198 277.078 1.00 26.80  ? 2807 PHE A CZ    1 
ATOM   10008 N  N     . GLU A 1 2808 ? 223.868 230.796 275.653 1.00 17.72  ? 2808 GLU A N     1 
ATOM   10009 C  CA    . GLU A 1 2808 ? 222.607 230.179 276.054 1.00 20.47  ? 2808 GLU A CA    1 
ATOM   10010 C  C     . GLU A 1 2808 ? 222.828 229.137 277.140 1.00 22.44  ? 2808 GLU A C     1 
ATOM   10011 O  O     . GLU A 1 2808 ? 222.037 229.039 278.086 1.00 24.11  ? 2808 GLU A O     1 
ATOM   10012 C  CB    . GLU A 1 2808 ? 221.895 229.545 274.858 1.00 20.93  ? 2808 GLU A CB    1 
ATOM   10013 C  CG    . GLU A 1 2808 ? 221.539 230.485 273.724 1.00 28.46  ? 2808 GLU A CG    1 
ATOM   10014 C  CD    . GLU A 1 2808 ? 221.543 229.787 272.380 1.00 42.40  ? 2808 GLU A CD    1 
ATOM   10015 O  OE1   . GLU A 1 2808 ? 221.551 230.479 271.343 1.00 43.62  ? 2808 GLU A OE1   1 
ATOM   10016 O  OE2   . GLU A 1 2808 ? 221.534 228.537 272.360 1.00 35.44  ? 2808 GLU A OE2   1 
ATOM   10017 N  N     . ALA A 1 2809 ? 223.894 228.343 277.018 1.00 21.70  ? 2809 ALA A N     1 
ATOM   10018 C  CA    . ALA A 1 2809 ? 224.198 227.359 278.052 1.00 17.98  ? 2809 ALA A CA    1 
ATOM   10019 C  C     . ALA A 1 2809 ? 224.511 228.031 279.384 1.00 22.34  ? 2809 ALA A C     1 
ATOM   10020 O  O     . ALA A 1 2809 ? 224.209 227.480 280.449 1.00 29.81  ? 2809 ALA A O     1 
ATOM   10021 C  CB    . ALA A 1 2809 ? 225.362 226.478 277.608 1.00 15.26  ? 2809 ALA A CB    1 
ATOM   10022 N  N     . LEU A 1 2810 ? 225.119 229.216 279.346 1.00 22.77  ? 2810 LEU A N     1 
ATOM   10023 C  CA    . LEU A 1 2810 ? 225.540 229.896 280.565 1.00 19.96  ? 2810 LEU A CA    1 
ATOM   10024 C  C     . LEU A 1 2810 ? 224.484 230.828 281.148 1.00 24.99  ? 2810 LEU A C     1 
ATOM   10025 O  O     . LEU A 1 2810 ? 224.670 231.308 282.270 1.00 30.56  ? 2810 LEU A O     1 
ATOM   10026 C  CB    . LEU A 1 2810 ? 226.820 230.694 280.301 1.00 21.34  ? 2810 LEU A CB    1 
ATOM   10027 C  CG    . LEU A 1 2810 ? 228.099 229.881 280.113 1.00 15.33  ? 2810 LEU A CG    1 
ATOM   10028 C  CD1   . LEU A 1 2810 ? 229.320 230.784 280.124 1.00 20.97  ? 2810 LEU A CD1   1 
ATOM   10029 C  CD2   . LEU A 1 2810 ? 228.204 228.825 281.186 1.00 19.64  ? 2810 LEU A CD2   1 
ATOM   10030 N  N     . ARG A 1 2811 ? 223.398 231.105 280.425 1.00 28.32  ? 2811 ARG A N     1 
ATOM   10031 C  CA    . ARG A 1 2811 ? 222.388 232.027 280.944 1.00 30.74  ? 2811 ARG A CA    1 
ATOM   10032 C  C     . ARG A 1 2811 ? 221.779 231.586 282.271 1.00 32.30  ? 2811 ARG A C     1 
ATOM   10033 O  O     . ARG A 1 2811 ? 221.771 232.395 283.214 1.00 36.09  ? 2811 ARG A O     1 
ATOM   10034 C  CB    . ARG A 1 2811 ? 221.292 232.258 279.897 1.00 29.54  ? 2811 ARG A CB    1 
ATOM   10035 C  CG    . ARG A 1 2811 ? 221.529 233.421 278.953 1.00 26.63  ? 2811 ARG A CG    1 
ATOM   10036 C  CD    . ARG A 1 2811 ? 220.311 233.619 278.048 1.00 35.71  ? 2811 ARG A CD    1 
ATOM   10037 N  NE    . ARG A 1 2811 ? 220.163 234.982 277.547 1.00 47.73  ? 2811 ARG A NE    1 
ATOM   10038 C  CZ    . ARG A 1 2811 ? 220.017 236.066 278.301 1.00 45.60  ? 2811 ARG A CZ    1 
ATOM   10039 N  NH1   . ARG A 1 2811 ? 219.934 235.988 279.620 1.00 43.03  ? 2811 ARG A NH1   1 
ATOM   10040 N  NH2   . ARG A 1 2811 ? 219.937 237.257 277.717 1.00 30.73  ? 2811 ARG A NH2   1 
ATOM   10041 N  N     . PRO A 1 2812 ? 221.263 230.359 282.430 1.00 34.24  ? 2812 PRO A N     1 
ATOM   10042 C  CA    . PRO A 1 2812 ? 220.564 230.035 283.681 1.00 32.42  ? 2812 PRO A CA    1 
ATOM   10043 C  C     . PRO A 1 2812 ? 221.480 229.675 284.838 1.00 35.07  ? 2812 PRO A C     1 
ATOM   10044 O  O     . PRO A 1 2812 ? 221.044 229.770 285.993 1.00 43.04  ? 2812 PRO A O     1 
ATOM   10045 C  CB    . PRO A 1 2812 ? 219.687 228.841 283.290 1.00 35.36  ? 2812 PRO A CB    1 
ATOM   10046 C  CG    . PRO A 1 2812 ? 220.467 228.160 282.235 1.00 32.55  ? 2812 PRO A CG    1 
ATOM   10047 C  CD    . PRO A 1 2812 ? 221.204 229.233 281.476 1.00 29.00  ? 2812 PRO A CD    1 
ATOM   10048 N  N     . LEU A 1 2813 ? 222.719 229.269 284.575 1.00 33.16  ? 2813 LEU A N     1 
ATOM   10049 C  CA    . LEU A 1 2813 ? 223.590 228.782 285.635 1.00 34.99  ? 2813 LEU A CA    1 
ATOM   10050 C  C     . LEU A 1 2813 ? 224.015 229.920 286.554 1.00 40.92  ? 2813 LEU A C     1 
ATOM   10051 O  O     . LEU A 1 2813 ? 224.455 230.976 286.092 1.00 43.15  ? 2813 LEU A O     1 
ATOM   10052 C  CB    . LEU A 1 2813 ? 224.820 228.103 285.037 1.00 35.03  ? 2813 LEU A CB    1 
ATOM   10053 C  CG    . LEU A 1 2813 ? 224.582 227.129 283.882 1.00 28.09  ? 2813 LEU A CG    1 
ATOM   10054 C  CD1   . LEU A 1 2813 ? 225.896 226.514 283.431 1.00 22.64  ? 2813 LEU A CD1   1 
ATOM   10055 C  CD2   . LEU A 1 2813 ? 223.593 226.047 284.283 1.00 33.08  ? 2813 LEU A CD2   1 
ATOM   10056 N  N     . GLU A 1 2814 ? 223.880 229.701 287.864 1.00 40.33  ? 2814 GLU A N     1 
ATOM   10057 C  CA    . GLU A 1 2814 ? 224.352 230.679 288.837 1.00 46.67  ? 2814 GLU A CA    1 
ATOM   10058 C  C     . GLU A 1 2814 ? 225.866 230.634 288.999 1.00 44.90  ? 2814 GLU A C     1 
ATOM   10059 O  O     . GLU A 1 2814 ? 226.479 231.657 289.324 1.00 42.70  ? 2814 GLU A O     1 
ATOM   10060 C  CB    . GLU A 1 2814 ? 223.665 230.455 290.187 1.00 50.72  ? 2814 GLU A CB    1 
ATOM   10061 C  CG    . GLU A 1 2814 ? 224.101 229.194 290.917 1.00 53.80  ? 2814 GLU A CG    1 
ATOM   10062 C  CD    . GLU A 1 2814 ? 223.054 228.694 291.891 1.00 66.10  ? 2814 GLU A CD    1 
ATOM   10063 O  OE1   . GLU A 1 2814 ? 222.568 229.500 292.710 1.00 61.00  ? 2814 GLU A OE1   1 
ATOM   10064 O  OE2   . GLU A 1 2814 ? 222.717 227.491 291.838 1.00 74.22  ? 2814 GLU A OE2   1 
ATOM   10065 N  N     . THR A 1 2815 ? 226.474 229.471 288.785 1.00 45.47  ? 2815 THR A N     1 
ATOM   10066 C  CA    . THR A 1 2815 ? 227.920 229.318 288.852 1.00 40.99  ? 2815 THR A CA    1 
ATOM   10067 C  C     . THR A 1 2815 ? 228.301 228.063 288.083 1.00 37.84  ? 2815 THR A C     1 
ATOM   10068 O  O     . THR A 1 2815 ? 227.457 227.207 287.802 1.00 37.64  ? 2815 THR A O     1 
ATOM   10069 C  CB    . THR A 1 2815 ? 228.421 229.241 290.298 1.00 44.17  ? 2815 THR A CB    1 
ATOM   10070 O  OG1   . THR A 1 2815 ? 229.842 229.418 290.324 1.00 43.85  ? 2815 THR A OG1   1 
ATOM   10071 C  CG2   . THR A 1 2815 ? 228.068 227.896 290.916 1.00 34.39  ? 2815 THR A CG2   1 
ATOM   10072 N  N     . LEU A 1 2816 ? 229.586 227.966 287.743 1.00 36.31  ? 2816 LEU A N     1 
ATOM   10073 C  CA    . LEU A 1 2816 ? 230.083 226.822 286.990 1.00 29.24  ? 2816 LEU A CA    1 
ATOM   10074 C  C     . LEU A 1 2816 ? 231.606 226.796 287.038 1.00 29.68  ? 2816 LEU A C     1 
ATOM   10075 O  O     . LEU A 1 2816 ? 232.249 227.837 286.850 1.00 36.02  ? 2816 LEU A O     1 
ATOM   10076 C  CB    . LEU A 1 2816 ? 229.595 226.886 285.541 1.00 26.16  ? 2816 LEU A CB    1 
ATOM   10077 C  CG    . LEU A 1 2816 ? 230.283 225.986 284.515 1.00 29.62  ? 2816 LEU A CG    1 
ATOM   10078 C  CD1   . LEU A 1 2816 ? 229.761 224.565 284.636 1.00 30.42  ? 2816 LEU A CD1   1 
ATOM   10079 C  CD2   . LEU A 1 2816 ? 230.083 226.512 283.111 1.00 27.44  ? 2816 LEU A CD2   1 
ATOM   10080 N  N     . PRO A 1 2817 ? 232.220 225.642 287.288 1.00 31.40  ? 2817 PRO A N     1 
ATOM   10081 C  CA    . PRO A 1 2817 ? 233.685 225.563 287.267 1.00 26.89  ? 2817 PRO A CA    1 
ATOM   10082 C  C     . PRO A 1 2817 ? 234.227 225.680 285.849 1.00 29.87  ? 2817 PRO A C     1 
ATOM   10083 O  O     . PRO A 1 2817 ? 233.491 225.676 284.861 1.00 32.35  ? 2817 PRO A O     1 
ATOM   10084 C  CB    . PRO A 1 2817 ? 233.977 224.187 287.869 1.00 28.85  ? 2817 PRO A CB    1 
ATOM   10085 C  CG    . PRO A 1 2817 ? 232.751 223.391 287.591 1.00 30.28  ? 2817 PRO A CG    1 
ATOM   10086 C  CD    . PRO A 1 2817 ? 231.602 224.358 287.659 1.00 27.25  ? 2817 PRO A CD    1 
ATOM   10087 N  N     . VAL A 1 2818 ? 235.554 225.791 285.766 1.00 33.50  ? 2818 VAL A N     1 
ATOM   10088 C  CA    . VAL A 1 2818 ? 236.206 225.941 284.467 1.00 28.23  ? 2818 VAL A CA    1 
ATOM   10089 C  C     . VAL A 1 2818 ? 236.025 224.684 283.625 1.00 30.71  ? 2818 VAL A C     1 
ATOM   10090 O  O     . VAL A 1 2818 ? 235.882 224.756 282.398 1.00 29.98  ? 2818 VAL A O     1 
ATOM   10091 C  CB    . VAL A 1 2818 ? 237.694 226.297 284.657 1.00 22.56  ? 2818 VAL A CB    1 
ATOM   10092 C  CG1   . VAL A 1 2818 ? 238.382 225.278 285.552 1.00 22.74  ? 2818 VAL A CG1   1 
ATOM   10093 C  CG2   . VAL A 1 2818 ? 238.397 226.398 283.311 1.00 24.70  ? 2818 VAL A CG2   1 
ATOM   10094 N  N     . GLU A 1 2819 ? 236.025 223.514 284.267 1.00 31.79  ? 2819 GLU A N     1 
ATOM   10095 C  CA    . GLU A 1 2819 ? 235.880 222.264 283.530 1.00 29.44  ? 2819 GLU A CA    1 
ATOM   10096 C  C     . GLU A 1 2819 ? 234.530 222.188 282.828 1.00 29.83  ? 2819 GLU A C     1 
ATOM   10097 O  O     . GLU A 1 2819 ? 234.441 221.724 281.686 1.00 22.25  ? 2819 GLU A O     1 
ATOM   10098 C  CB    . GLU A 1 2819 ? 236.072 221.078 284.473 1.00 36.97  ? 2819 GLU A CB    1 
ATOM   10099 C  CG    . GLU A 1 2819 ? 237.507 220.894 284.934 1.00 38.86  ? 2819 GLU A CG    1 
ATOM   10100 C  CD    . GLU A 1 2819 ? 237.791 221.605 286.243 1.00 46.77  ? 2819 GLU A CD    1 
ATOM   10101 O  OE1   . GLU A 1 2819 ? 236.831 222.087 286.879 1.00 46.76  ? 2819 GLU A OE1   1 
ATOM   10102 O  OE2   . GLU A 1 2819 ? 238.976 221.686 286.633 1.00 47.68  ? 2819 GLU A OE2   1 
ATOM   10103 N  N     . GLY A 1 2820 ? 233.467 222.649 283.490 1.00 29.83  ? 2820 GLY A N     1 
ATOM   10104 C  CA    . GLY A 1 2820 ? 232.166 222.679 282.844 1.00 23.38  ? 2820 GLY A CA    1 
ATOM   10105 C  C     . GLY A 1 2820 ? 232.115 223.642 281.671 1.00 23.52  ? 2820 GLY A C     1 
ATOM   10106 O  O     . GLY A 1 2820 ? 231.483 223.359 280.650 1.00 24.40  ? 2820 GLY A O     1 
ATOM   10107 N  N     . LEU A 1 2821 ? 232.772 224.796 281.806 1.00 24.74  ? 2821 LEU A N     1 
ATOM   10108 C  CA    . LEU A 1 2821 ? 232.846 225.738 280.692 1.00 18.80  ? 2821 LEU A CA    1 
ATOM   10109 C  C     . LEU A 1 2821 ? 233.586 225.129 279.509 1.00 15.93  ? 2821 LEU A C     1 
ATOM   10110 O  O     . LEU A 1 2821 ? 233.172 225.292 278.355 1.00 21.16  ? 2821 LEU A O     1 
ATOM   10111 C  CB    . LEU A 1 2821 ? 233.523 227.032 281.144 1.00 20.78  ? 2821 LEU A CB    1 
ATOM   10112 C  CG    . LEU A 1 2821 ? 233.942 228.015 280.048 1.00 19.84  ? 2821 LEU A CG    1 
ATOM   10113 C  CD1   . LEU A 1 2821 ? 232.766 228.866 279.598 1.00 13.37  ? 2821 LEU A CD1   1 
ATOM   10114 C  CD2   . LEU A 1 2821 ? 235.092 228.890 280.518 1.00 14.61  ? 2821 LEU A CD2   1 
ATOM   10115 N  N     . ILE A 1 2822 ? 234.681 224.417 279.777 1.00 14.31  ? 2822 ILE A N     1 
ATOM   10116 C  CA    . ILE A 1 2822 ? 235.421 223.759 278.705 1.00 17.63  ? 2822 ILE A CA    1 
ATOM   10117 C  C     . ILE A 1 2822 ? 234.575 222.661 278.074 1.00 18.17  ? 2822 ILE A C     1 
ATOM   10118 O  O     . ILE A 1 2822 ? 234.631 222.431 276.861 1.00 22.01  ? 2822 ILE A O     1 
ATOM   10119 C  CB    . ILE A 1 2822 ? 236.760 223.218 279.239 1.00 21.75  ? 2822 ILE A CB    1 
ATOM   10120 C  CG1   . ILE A 1 2822 ? 237.634 224.369 279.728 1.00 18.00  ? 2822 ILE A CG1   1 
ATOM   10121 C  CG2   . ILE A 1 2822 ? 237.497 222.450 278.162 1.00 18.75  ? 2822 ILE A CG2   1 
ATOM   10122 C  CD1   . ILE A 1 2822 ? 238.842 223.917 280.501 1.00 27.21  ? 2822 ILE A CD1   1 
ATOM   10123 N  N     . ARG A 1 2823 ? 233.778 221.963 278.888 1.00 16.31  ? 2823 ARG A N     1 
ATOM   10124 C  CA    . ARG A 1 2823 ? 232.872 220.954 278.352 1.00 16.69  ? 2823 ARG A CA    1 
ATOM   10125 C  C     . ARG A 1 2823 ? 231.835 221.576 277.426 1.00 14.51  ? 2823 ARG A C     1 
ATOM   10126 O  O     . ARG A 1 2823 ? 231.531 221.023 276.364 1.00 17.34  ? 2823 ARG A O     1 
ATOM   10127 C  CB    . ARG A 1 2823 ? 232.188 220.203 279.493 1.00 18.63  ? 2823 ARG A CB    1 
ATOM   10128 C  CG    . ARG A 1 2823 ? 231.607 218.863 279.083 1.00 16.11  ? 2823 ARG A CG    1 
ATOM   10129 C  CD    . ARG A 1 2823 ? 231.305 217.987 280.284 1.00 19.08  ? 2823 ARG A CD    1 
ATOM   10130 N  NE    . ARG A 1 2823 ? 230.627 216.757 279.892 1.00 24.31  ? 2823 ARG A NE    1 
ATOM   10131 C  CZ    . ARG A 1 2823 ? 231.222 215.723 279.316 1.00 21.75  ? 2823 ARG A CZ    1 
ATOM   10132 N  NH1   . ARG A 1 2823 ? 232.521 215.721 279.070 1.00 27.71  ? 2823 ARG A NH1   1 
ATOM   10133 N  NH2   . ARG A 1 2823 ? 230.495 214.663 278.977 1.00 26.10  ? 2823 ARG A NH2   1 
ATOM   10134 N  N     . ILE A 1 2824 ? 231.274 222.721 277.815 1.00 14.42  ? 2824 ILE A N     1 
ATOM   10135 C  CA    . ILE A 1 2824 ? 230.321 223.416 276.951 1.00 15.25  ? 2824 ILE A CA    1 
ATOM   10136 C  C     . ILE A 1 2824 ? 230.999 223.851 275.658 1.00 13.46  ? 2824 ILE A C     1 
ATOM   10137 O  O     . ILE A 1 2824 ? 230.431 223.731 274.563 1.00 18.77  ? 2824 ILE A O     1 
ATOM   10138 C  CB    . ILE A 1 2824 ? 229.696 224.611 277.693 1.00 13.11  ? 2824 ILE A CB    1 
ATOM   10139 C  CG1   . ILE A 1 2824 ? 228.897 224.130 278.905 1.00 18.26  ? 2824 ILE A CG1   1 
ATOM   10140 C  CG2   . ILE A 1 2824 ? 228.804 225.413 276.761 1.00 10.03  ? 2824 ILE A CG2   1 
ATOM   10141 C  CD1   . ILE A 1 2824 ? 228.469 225.243 279.833 1.00 22.18  ? 2824 ILE A CD1   1 
ATOM   10142 N  N     . TRP A 1 2825 ? 232.225 224.369 275.768 1.00 11.58  ? 2825 TRP A N     1 
ATOM   10143 C  CA    . TRP A 1 2825 ? 232.983 224.786 274.595 1.00 10.63  ? 2825 TRP A CA    1 
ATOM   10144 C  C     . TRP A 1 2825 ? 233.197 223.620 273.638 1.00 12.38  ? 2825 TRP A C     1 
ATOM   10145 O  O     . TRP A 1 2825 ? 232.978 223.743 272.426 1.00 11.74  ? 2825 TRP A O     1 
ATOM   10146 C  CB    . TRP A 1 2825 ? 234.317 225.383 275.054 1.00 9.91   ? 2825 TRP A CB    1 
ATOM   10147 C  CG    . TRP A 1 2825 ? 235.305 225.698 273.975 1.00 11.85  ? 2825 TRP A CG    1 
ATOM   10148 C  CD1   . TRP A 1 2825 ? 235.432 226.878 273.305 1.00 10.06  ? 2825 TRP A CD1   1 
ATOM   10149 C  CD2   . TRP A 1 2825 ? 236.332 224.837 273.472 1.00 11.04  ? 2825 TRP A CD2   1 
ATOM   10150 N  NE1   . TRP A 1 2825 ? 236.464 226.800 272.404 1.00 11.34  ? 2825 TRP A NE1   1 
ATOM   10151 C  CE2   . TRP A 1 2825 ? 237.032 225.558 272.485 1.00 11.44  ? 2825 TRP A CE2   1 
ATOM   10152 C  CE3   . TRP A 1 2825 ? 236.722 223.525 273.751 1.00 13.75  ? 2825 TRP A CE3   1 
ATOM   10153 C  CZ2   . TRP A 1 2825 ? 238.098 225.010 271.777 1.00 14.85  ? 2825 TRP A CZ2   1 
ATOM   10154 C  CZ3   . TRP A 1 2825 ? 237.780 222.983 273.046 1.00 15.96  ? 2825 TRP A CZ3   1 
ATOM   10155 C  CH2   . TRP A 1 2825 ? 238.456 223.724 272.072 1.00 17.95  ? 2825 TRP A CH2   1 
ATOM   10156 N  N     . ALA A 1 2826 ? 233.597 222.466 274.174 1.00 12.56  ? 2826 ALA A N     1 
ATOM   10157 C  CA    . ALA A 1 2826 ? 233.828 221.287 273.346 1.00 11.99  ? 2826 ALA A CA    1 
ATOM   10158 C  C     . ALA A 1 2826 ? 232.533 220.765 272.737 1.00 12.60  ? 2826 ALA A C     1 
ATOM   10159 O  O     . ALA A 1 2826 ? 232.518 220.329 271.581 1.00 12.23  ? 2826 ALA A O     1 
ATOM   10160 C  CB    . ALA A 1 2826 ? 234.512 220.197 274.166 1.00 17.93  ? 2826 ALA A CB    1 
ATOM   10161 N  N     . HIS A 1 2827 ? 231.439 220.786 273.501 1.00 10.19  ? 2827 HIS A N     1 
ATOM   10162 C  CA    . HIS A 1 2827 ? 230.159 220.332 272.969 1.00 9.67   ? 2827 HIS A CA    1 
ATOM   10163 C  C     . HIS A 1 2827 ? 229.706 221.206 271.809 1.00 12.59  ? 2827 HIS A C     1 
ATOM   10164 O  O     . HIS A 1 2827 ? 229.237 220.699 270.784 1.00 13.13  ? 2827 HIS A O     1 
ATOM   10165 C  CB    . HIS A 1 2827 ? 229.105 220.325 274.075 1.00 12.19  ? 2827 HIS A CB    1 
ATOM   10166 C  CG    . HIS A 1 2827 ? 227.732 219.971 273.598 1.00 11.98  ? 2827 HIS A CG    1 
ATOM   10167 N  ND1   . HIS A 1 2827 ? 227.379 218.691 273.226 1.00 14.26  ? 2827 HIS A ND1   1 
ATOM   10168 C  CD2   . HIS A 1 2827 ? 226.624 220.731 273.424 1.00 12.54  ? 2827 HIS A CD2   1 
ATOM   10169 C  CE1   . HIS A 1 2827 ? 226.114 218.678 272.849 1.00 15.19  ? 2827 HIS A CE1   1 
ATOM   10170 N  NE2   . HIS A 1 2827 ? 225.633 219.903 272.958 1.00 15.10  ? 2827 HIS A NE2   1 
ATOM   10171 N  N     . GLU A 1 2828 ? 229.840 222.526 271.953 1.00 13.79  ? 2828 GLU A N     1 
ATOM   10172 C  CA    . GLU A 1 2828 ? 229.455 223.419 270.865 1.00 9.80   ? 2828 GLU A CA    1 
ATOM   10173 C  C     . GLU A 1 2828 ? 230.379 223.255 269.666 1.00 10.70  ? 2828 GLU A C     1 
ATOM   10174 O  O     . GLU A 1 2828 ? 229.927 223.319 268.515 1.00 14.69  ? 2828 GLU A O     1 
ATOM   10175 C  CB    . GLU A 1 2828 ? 229.440 224.866 271.356 1.00 11.14  ? 2828 GLU A CB    1 
ATOM   10176 C  CG    . GLU A 1 2828 ? 228.395 225.192 272.437 1.00 14.29  ? 2828 GLU A CG    1 
ATOM   10177 C  CD    . GLU A 1 2828 ? 226.963 224.758 272.116 1.00 25.66  ? 2828 GLU A CD    1 
ATOM   10178 O  OE1   . GLU A 1 2828 ? 226.100 224.905 273.006 1.00 32.11  ? 2828 GLU A OE1   1 
ATOM   10179 O  OE2   . GLU A 1 2828 ? 226.669 224.328 270.981 1.00 21.56  ? 2828 GLU A OE2   1 
ATOM   10180 N  N     . ALA A 1 2829 ? 231.672 223.026 269.909 1.00 8.33   ? 2829 ALA A N     1 
ATOM   10181 C  CA    . ALA A 1 2829 ? 232.586 222.745 268.808 1.00 8.15   ? 2829 ALA A CA    1 
ATOM   10182 C  C     . ALA A 1 2829 ? 232.176 221.480 268.066 1.00 13.42  ? 2829 ALA A C     1 
ATOM   10183 O  O     . ALA A 1 2829 ? 232.248 221.423 266.833 1.00 18.47  ? 2829 ALA A O     1 
ATOM   10184 C  CB    . ALA A 1 2829 ? 234.016 222.618 269.329 1.00 10.74  ? 2829 ALA A CB    1 
ATOM   10185 N  N     . LEU A 1 2830 ? 231.760 220.449 268.803 1.00 12.70  ? 2830 LEU A N     1 
ATOM   10186 C  CA    . LEU A 1 2830 ? 231.284 219.225 268.168 1.00 8.25   ? 2830 LEU A CA    1 
ATOM   10187 C  C     . LEU A 1 2830 ? 230.024 219.480 267.353 1.00 9.80   ? 2830 LEU A C     1 
ATOM   10188 O  O     . LEU A 1 2830 ? 229.890 218.983 266.229 1.00 12.75  ? 2830 LEU A O     1 
ATOM   10189 C  CB    . LEU A 1 2830 ? 231.026 218.154 269.225 1.00 11.62  ? 2830 LEU A CB    1 
ATOM   10190 C  CG    . LEU A 1 2830 ? 232.270 217.513 269.837 1.00 13.76  ? 2830 LEU A CG    1 
ATOM   10191 C  CD1   . LEU A 1 2830 ? 231.897 216.600 270.994 1.00 11.25  ? 2830 LEU A CD1   1 
ATOM   10192 C  CD2   . LEU A 1 2830 ? 233.034 216.754 268.774 1.00 13.67  ? 2830 LEU A CD2   1 
ATOM   10193 N  N     . ARG A 1 2831 ? 229.086 220.252 267.902 1.00 12.82  ? 2831 ARG A N     1 
ATOM   10194 C  CA    . ARG A 1 2831 ? 227.834 220.507 267.199 1.00 10.81  ? 2831 ARG A CA    1 
ATOM   10195 C  C     . ARG A 1 2831 ? 228.016 221.425 265.998 1.00 9.82   ? 2831 ARG A C     1 
ATOM   10196 O  O     . ARG A 1 2831 ? 227.155 221.441 265.112 1.00 11.87  ? 2831 ARG A O     1 
ATOM   10197 C  CB    . ARG A 1 2831 ? 226.797 221.101 268.153 1.00 11.44  ? 2831 ARG A CB    1 
ATOM   10198 C  CG    . ARG A 1 2831 ? 226.461 220.206 269.335 1.00 11.01  ? 2831 ARG A CG    1 
ATOM   10199 C  CD    . ARG A 1 2831 ? 225.548 219.050 268.941 1.00 10.47  ? 2831 ARG A CD    1 
ATOM   10200 N  NE    . ARG A 1 2831 ? 226.282 217.958 268.310 1.00 11.17  ? 2831 ARG A NE    1 
ATOM   10201 C  CZ    . ARG A 1 2831 ? 227.107 217.137 268.945 1.00 10.77  ? 2831 ARG A CZ    1 
ATOM   10202 N  NH1   . ARG A 1 2831 ? 227.321 217.239 270.245 1.00 8.32   ? 2831 ARG A NH1   1 
ATOM   10203 N  NH2   . ARG A 1 2831 ? 227.736 216.190 268.255 1.00 13.66  ? 2831 ARG A NH2   1 
ATOM   10204 N  N     . LEU A 1 2832 ? 229.106 222.186 265.948 1.00 9.56   ? 2832 LEU A N     1 
ATOM   10205 C  CA    . LEU A 1 2832 ? 229.360 223.091 264.835 1.00 8.01   ? 2832 LEU A CA    1 
ATOM   10206 C  C     . LEU A 1 2832 ? 230.245 222.494 263.752 1.00 9.72   ? 2832 LEU A C     1 
ATOM   10207 O  O     . LEU A 1 2832 ? 229.912 222.588 262.567 1.00 15.90  ? 2832 LEU A O     1 
ATOM   10208 C  CB    . LEU A 1 2832 ? 230.005 224.380 265.345 1.00 9.87   ? 2832 LEU A CB    1 
ATOM   10209 C  CG    . LEU A 1 2832 ? 229.090 225.307 266.135 1.00 10.76  ? 2832 LEU A CG    1 
ATOM   10210 C  CD1   . LEU A 1 2832 ? 229.884 226.489 266.616 1.00 12.19  ? 2832 LEU A CD1   1 
ATOM   10211 C  CD2   . LEU A 1 2832 ? 227.929 225.754 265.280 1.00 11.85  ? 2832 LEU A CD2   1 
ATOM   10212 N  N     . PHE A 1 2833 ? 231.370 221.887 264.127 1.00 8.69   ? 2833 PHE A N     1 
ATOM   10213 C  CA    . PHE A 1 2833 ? 232.382 221.479 263.165 1.00 11.27  ? 2833 PHE A CA    1 
ATOM   10214 C  C     . PHE A 1 2833 ? 232.343 219.997 262.819 1.00 14.04  ? 2833 PHE A C     1 
ATOM   10215 O  O     . PHE A 1 2833 ? 232.946 219.600 261.816 1.00 16.16  ? 2833 PHE A O     1 
ATOM   10216 C  CB    . PHE A 1 2833 ? 233.778 221.825 263.697 1.00 11.57  ? 2833 PHE A CB    1 
ATOM   10217 C  CG    . PHE A 1 2833 ? 233.998 223.296 263.906 1.00 11.15  ? 2833 PHE A CG    1 
ATOM   10218 C  CD1   . PHE A 1 2833 ? 234.506 224.083 262.890 1.00 9.43   ? 2833 PHE A CD1   1 
ATOM   10219 C  CD2   . PHE A 1 2833 ? 233.692 223.891 265.117 1.00 9.05   ? 2833 PHE A CD2   1 
ATOM   10220 C  CE1   . PHE A 1 2833 ? 234.708 225.435 263.078 1.00 10.53  ? 2833 PHE A CE1   1 
ATOM   10221 C  CE2   . PHE A 1 2833 ? 233.891 225.240 265.311 1.00 8.46   ? 2833 PHE A CE2   1 
ATOM   10222 C  CZ    . PHE A 1 2833 ? 234.400 226.012 264.290 1.00 13.17  ? 2833 PHE A CZ    1 
ATOM   10223 N  N     . GLN A 1 2834 ? 231.656 219.173 263.609 1.00 12.75  ? 2834 GLN A N     1 
ATOM   10224 C  CA    . GLN A 1 2834 ? 231.676 217.733 263.398 1.00 11.20  ? 2834 GLN A CA    1 
ATOM   10225 C  C     . GLN A 1 2834 ? 230.381 217.179 262.819 1.00 13.53  ? 2834 GLN A C     1 
ATOM   10226 O  O     . GLN A 1 2834 ? 230.404 216.097 262.225 1.00 18.38  ? 2834 GLN A O     1 
ATOM   10227 C  CB    . GLN A 1 2834 ? 231.978 217.009 264.715 1.00 10.63  ? 2834 GLN A CB    1 
ATOM   10228 C  CG    . GLN A 1 2834 ? 232.549 215.620 264.528 1.00 12.68  ? 2834 GLN A CG    1 
ATOM   10229 C  CD    . GLN A 1 2834 ? 232.607 214.830 265.814 1.00 17.92  ? 2834 GLN A CD    1 
ATOM   10230 O  OE1   . GLN A 1 2834 ? 231.601 214.672 266.504 1.00 24.65  ? 2834 GLN A OE1   1 
ATOM   10231 N  NE2   . GLN A 1 2834 ? 233.786 214.317 266.138 1.00 17.27  ? 2834 GLN A NE2   1 
ATOM   10232 N  N     . ASP A 1 2835 ? 229.262 217.890 262.972 1.00 11.95  ? 2835 ASP A N     1 
ATOM   10233 C  CA    . ASP A 1 2835 ? 227.976 217.344 262.547 1.00 9.49   ? 2835 ASP A CA    1 
ATOM   10234 C  C     . ASP A 1 2835 ? 227.894 217.210 261.031 1.00 12.03  ? 2835 ASP A C     1 
ATOM   10235 O  O     . ASP A 1 2835 ? 227.264 216.279 260.519 1.00 16.31  ? 2835 ASP A O     1 
ATOM   10236 C  CB    . ASP A 1 2835 ? 226.839 218.218 263.071 1.00 13.26  ? 2835 ASP A CB    1 
ATOM   10237 C  CG    . ASP A 1 2835 ? 226.581 218.009 264.548 1.00 22.48  ? 2835 ASP A CG    1 
ATOM   10238 O  OD1   . ASP A 1 2835 ? 227.357 217.272 265.188 1.00 19.98  ? 2835 ASP A OD1   1 
ATOM   10239 O  OD2   . ASP A 1 2835 ? 225.600 218.581 265.069 1.00 20.98  ? 2835 ASP A OD2   1 
ATOM   10240 N  N     . ARG A 1 2836 ? 228.517 218.131 260.298 1.00 13.02  ? 2836 ARG A N     1 
ATOM   10241 C  CA    . ARG A 1 2836 ? 228.451 218.115 258.843 1.00 11.88  ? 2836 ARG A CA    1 
ATOM   10242 C  C     . ARG A 1 2836 ? 229.504 217.222 258.203 1.00 14.46  ? 2836 ARG A C     1 
ATOM   10243 O  O     . ARG A 1 2836 ? 229.443 217.000 256.988 1.00 20.37  ? 2836 ARG A O     1 
ATOM   10244 C  CB    . ARG A 1 2836 ? 228.595 219.536 258.297 1.00 16.28  ? 2836 ARG A CB    1 
ATOM   10245 C  CG    . ARG A 1 2836 ? 230.030 220.024 258.231 1.00 16.40  ? 2836 ARG A CG    1 
ATOM   10246 C  CD    . ARG A 1 2836 ? 230.099 221.445 257.716 1.00 16.44  ? 2836 ARG A CD    1 
ATOM   10247 N  NE    . ARG A 1 2836 ? 229.709 222.407 258.738 1.00 19.73  ? 2836 ARG A NE    1 
ATOM   10248 C  CZ    . ARG A 1 2836 ? 229.569 223.708 258.527 1.00 13.99  ? 2836 ARG A CZ    1 
ATOM   10249 N  NH1   . ARG A 1 2836 ? 229.780 224.240 257.335 1.00 15.02  ? 2836 ARG A NH1   1 
ATOM   10250 N  NH2   . ARG A 1 2836 ? 229.207 224.494 259.536 1.00 12.44  ? 2836 ARG A NH2   1 
ATOM   10251 N  N     . LEU A 1 2837 ? 230.457 216.712 258.975 1.00 13.59  ? 2837 LEU A N     1 
ATOM   10252 C  CA    . LEU A 1 2837 ? 231.522 215.894 258.413 1.00 13.50  ? 2837 LEU A CA    1 
ATOM   10253 C  C     . LEU A 1 2837 ? 230.974 214.572 257.889 1.00 13.46  ? 2837 LEU A C     1 
ATOM   10254 O  O     . LEU A 1 2837 ? 230.058 213.985 258.470 1.00 17.12  ? 2837 LEU A O     1 
ATOM   10255 C  CB    . LEU A 1 2837 ? 232.601 215.643 259.461 1.00 15.91  ? 2837 LEU A CB    1 
ATOM   10256 C  CG    . LEU A 1 2837 ? 233.343 216.897 259.923 1.00 12.49  ? 2837 LEU A CG    1 
ATOM   10257 C  CD1   . LEU A 1 2837 ? 234.447 216.529 260.886 1.00 11.11  ? 2837 LEU A CD1   1 
ATOM   10258 C  CD2   . LEU A 1 2837 ? 233.905 217.654 258.730 1.00 11.01  ? 2837 LEU A CD2   1 
ATOM   10259 N  N     . VAL A 1 2838 ? 231.549 214.103 256.784 1.00 15.29  ? 2838 VAL A N     1 
ATOM   10260 C  CA    . VAL A 1 2838 ? 231.065 212.908 256.102 1.00 15.83  ? 2838 VAL A CA    1 
ATOM   10261 C  C     . VAL A 1 2838 ? 231.838 211.681 256.566 1.00 18.74  ? 2838 VAL A C     1 
ATOM   10262 O  O     . VAL A 1 2838 ? 231.244 210.684 256.990 1.00 20.53  ? 2838 VAL A O     1 
ATOM   10263 C  CB    . VAL A 1 2838 ? 231.167 213.070 254.574 1.00 11.99  ? 2838 VAL A CB    1 
ATOM   10264 C  CG1   . VAL A 1 2838 ? 230.557 211.872 253.872 1.00 11.91  ? 2838 VAL A CG1   1 
ATOM   10265 C  CG2   . VAL A 1 2838 ? 230.488 214.354 254.132 1.00 12.14  ? 2838 VAL A CG2   1 
ATOM   10266 N  N     . GLU A 1 2839 ? 233.163 211.742 256.488 1.00 20.15  ? 2839 GLU A N     1 
ATOM   10267 C  CA    . GLU A 1 2839 ? 233.992 210.580 256.769 1.00 20.50  ? 2839 GLU A CA    1 
ATOM   10268 C  C     . GLU A 1 2839 ? 234.266 210.436 258.262 1.00 24.29  ? 2839 GLU A C     1 
ATOM   10269 O  O     . GLU A 1 2839 ? 234.238 211.409 259.020 1.00 26.03  ? 2839 GLU A O     1 
ATOM   10270 C  CB    . GLU A 1 2839 ? 235.313 210.669 256.006 1.00 24.26  ? 2839 GLU A CB    1 
ATOM   10271 C  CG    . GLU A 1 2839 ? 235.166 211.154 254.574 1.00 25.03  ? 2839 GLU A CG    1 
ATOM   10272 C  CD    . GLU A 1 2839 ? 234.674 210.070 253.637 1.00 30.82  ? 2839 GLU A CD    1 
ATOM   10273 O  OE1   . GLU A 1 2839 ? 234.590 208.901 254.067 1.00 32.89  ? 2839 GLU A OE1   1 
ATOM   10274 O  OE2   . GLU A 1 2839 ? 234.374 210.386 252.468 1.00 34.24  ? 2839 GLU A OE2   1 
ATOM   10275 N  N     . ASP A 1 2840 ? 234.531 209.194 258.676 1.00 29.84  ? 2840 ASP A N     1 
ATOM   10276 C  CA    . ASP A 1 2840 ? 234.855 208.918 260.072 1.00 25.90  ? 2840 ASP A CA    1 
ATOM   10277 C  C     . ASP A 1 2840 ? 236.184 209.539 260.478 1.00 30.51  ? 2840 ASP A C     1 
ATOM   10278 O  O     . ASP A 1 2840 ? 236.317 210.033 261.605 1.00 29.88  ? 2840 ASP A O     1 
ATOM   10279 C  CB    . ASP A 1 2840 ? 234.893 207.408 260.312 1.00 37.83  ? 2840 ASP A CB    1 
ATOM   10280 C  CG    . ASP A 1 2840 ? 233.525 206.765 260.214 1.00 53.74  ? 2840 ASP A CG    1 
ATOM   10281 O  OD1   . ASP A 1 2840 ? 232.523 207.447 260.510 1.00 56.33  ? 2840 ASP A OD1   1 
ATOM   10282 O  OD2   . ASP A 1 2840 ? 233.451 205.576 259.840 1.00 54.87  ? 2840 ASP A OD2   1 
ATOM   10283 N  N     . GLU A 1 2841 ? 237.179 209.508 259.588 1.00 30.22  ? 2841 GLU A N     1 
ATOM   10284 C  CA    . GLU A 1 2841 ? 238.493 210.046 259.927 1.00 32.22  ? 2841 GLU A CA    1 
ATOM   10285 C  C     . GLU A 1 2841 ? 238.440 211.547 260.164 1.00 32.24  ? 2841 GLU A C     1 
ATOM   10286 O  O     . GLU A 1 2841 ? 239.177 212.063 261.011 1.00 36.52  ? 2841 GLU A O     1 
ATOM   10287 C  CB    . GLU A 1 2841 ? 239.503 209.702 258.830 1.00 35.30  ? 2841 GLU A CB    1 
ATOM   10288 C  CG    . GLU A 1 2841 ? 239.167 210.256 257.455 1.00 41.20  ? 2841 GLU A CG    1 
ATOM   10289 C  CD    . GLU A 1 2841 ? 239.852 211.580 257.175 1.00 50.33  ? 2841 GLU A CD    1 
ATOM   10290 O  OE1   . GLU A 1 2841 ? 240.830 211.906 257.880 1.00 47.62  ? 2841 GLU A OE1   1 
ATOM   10291 O  OE2   . GLU A 1 2841 ? 239.414 212.294 256.248 1.00 44.25  ? 2841 GLU A OE2   1 
ATOM   10292 N  N     . GLU A 1 2842 ? 237.572 212.261 259.443 1.00 29.80  ? 2842 GLU A N     1 
ATOM   10293 C  CA    . GLU A 1 2842 ? 237.406 213.688 259.691 1.00 25.76  ? 2842 GLU A CA    1 
ATOM   10294 C  C     . GLU A 1 2842 ? 236.871 213.944 261.095 1.00 20.96  ? 2842 GLU A C     1 
ATOM   10295 O  O     . GLU A 1 2842 ? 237.341 214.850 261.793 1.00 25.31  ? 2842 GLU A O     1 
ATOM   10296 C  CB    . GLU A 1 2842 ? 236.475 214.292 258.640 1.00 21.29  ? 2842 GLU A CB    1 
ATOM   10297 C  CG    . GLU A 1 2842 ? 237.071 214.334 257.244 1.00 21.50  ? 2842 GLU A CG    1 
ATOM   10298 C  CD    . GLU A 1 2842 ? 236.023 214.529 256.169 1.00 32.94  ? 2842 GLU A CD    1 
ATOM   10299 O  OE1   . GLU A 1 2842 ? 234.823 214.564 256.507 1.00 31.83  ? 2842 GLU A OE1   1 
ATOM   10300 O  OE2   . GLU A 1 2842 ? 236.402 214.649 254.985 1.00 37.88  ? 2842 GLU A OE2   1 
ATOM   10301 N  N     . ARG A 1 2843 ? 235.894 213.147 261.530 1.00 15.71  ? 2843 ARG A N     1 
ATOM   10302 C  CA    . ARG A 1 2843 ? 235.344 213.324 262.869 1.00 18.21  ? 2843 ARG A CA    1 
ATOM   10303 C  C     . ARG A 1 2843 ? 236.356 212.934 263.942 1.00 24.86  ? 2843 ARG A C     1 
ATOM   10304 O  O     . ARG A 1 2843 ? 236.413 213.562 265.008 1.00 25.54  ? 2843 ARG A O     1 
ATOM   10305 C  CB    . ARG A 1 2843 ? 234.049 212.522 263.010 1.00 20.04  ? 2843 ARG A CB    1 
ATOM   10306 C  CG    . ARG A 1 2843 ? 232.912 213.079 262.165 1.00 15.72  ? 2843 ARG A CG    1 
ATOM   10307 C  CD    . ARG A 1 2843 ? 231.577 212.424 262.477 1.00 18.84  ? 2843 ARG A CD    1 
ATOM   10308 N  NE    . ARG A 1 2843 ? 231.541 211.007 262.145 1.00 23.31  ? 2843 ARG A NE    1 
ATOM   10309 C  CZ    . ARG A 1 2843 ? 231.187 210.530 260.959 1.00 31.36  ? 2843 ARG A CZ    1 
ATOM   10310 N  NH1   . ARG A 1 2843 ? 230.846 211.333 259.966 1.00 20.64  ? 2843 ARG A NH1   1 
ATOM   10311 N  NH2   . ARG A 1 2843 ? 231.169 209.215 260.767 1.00 34.88  ? 2843 ARG A NH2   1 
ATOM   10312 N  N     . ARG A 1 2844 ? 237.166 211.906 263.680 1.00 27.28  ? 2844 ARG A N     1 
ATOM   10313 C  CA    . ARG A 1 2844 ? 238.237 211.558 264.609 1.00 25.09  ? 2844 ARG A CA    1 
ATOM   10314 C  C     . ARG A 1 2844 ? 239.253 212.689 264.723 1.00 24.01  ? 2844 ARG A C     1 
ATOM   10315 O  O     . ARG A 1 2844 ? 239.713 213.017 265.826 1.00 25.28  ? 2844 ARG A O     1 
ATOM   10316 C  CB    . ARG A 1 2844 ? 238.920 210.266 264.162 1.00 30.79  ? 2844 ARG A CB    1 
ATOM   10317 C  CG    . ARG A 1 2844 ? 239.388 209.381 265.305 1.00 34.81  ? 2844 ARG A CG    1 
ATOM   10318 C  CD    . ARG A 1 2844 ? 240.150 208.153 264.815 1.00 34.70  ? 2844 ARG A CD    1 
ATOM   10319 N  NE    . ARG A 1 2844 ? 241.121 208.461 263.771 1.00 49.49  ? 2844 ARG A NE    1 
ATOM   10320 C  CZ    . ARG A 1 2844 ? 240.924 208.256 262.476 1.00 54.33  ? 2844 ARG A CZ    1 
ATOM   10321 N  NH1   . ARG A 1 2844 ? 239.799 207.727 262.022 1.00 42.24  ? 2844 ARG A NH1   1 
ATOM   10322 N  NH2   . ARG A 1 2844 ? 241.881 208.589 261.613 1.00 44.59  ? 2844 ARG A NH2   1 
ATOM   10323 N  N     . TRP A 1 2845 ? 239.614 213.293 263.588 1.00 21.79  ? 2845 TRP A N     1 
ATOM   10324 C  CA    . TRP A 1 2845 ? 240.483 214.465 263.592 1.00 21.95  ? 2845 TRP A CA    1 
ATOM   10325 C  C     . TRP A 1 2845 ? 239.876 215.591 264.412 1.00 21.32  ? 2845 TRP A C     1 
ATOM   10326 O  O     . TRP A 1 2845 ? 240.573 216.247 265.198 1.00 24.17  ? 2845 TRP A O     1 
ATOM   10327 C  CB    . TRP A 1 2845 ? 240.731 214.919 262.152 1.00 23.97  ? 2845 TRP A CB    1 
ATOM   10328 C  CG    . TRP A 1 2845 ? 241.637 216.106 261.996 1.00 26.83  ? 2845 TRP A CG    1 
ATOM   10329 C  CD1   . TRP A 1 2845 ? 242.964 216.087 261.691 1.00 23.71  ? 2845 TRP A CD1   1 
ATOM   10330 C  CD2   . TRP A 1 2845 ? 241.271 217.489 262.107 1.00 25.99  ? 2845 TRP A CD2   1 
ATOM   10331 N  NE1   . TRP A 1 2845 ? 243.452 217.368 261.618 1.00 23.17  ? 2845 TRP A NE1   1 
ATOM   10332 C  CE2   . TRP A 1 2845 ? 242.432 218.247 261.867 1.00 21.36  ? 2845 TRP A CE2   1 
ATOM   10333 C  CE3   . TRP A 1 2845 ? 240.077 218.157 262.391 1.00 22.41  ? 2845 TRP A CE3   1 
ATOM   10334 C  CZ2   . TRP A 1 2845 ? 242.432 219.641 261.904 1.00 24.65  ? 2845 TRP A CZ2   1 
ATOM   10335 C  CZ3   . TRP A 1 2845 ? 240.081 219.538 262.429 1.00 16.45  ? 2845 TRP A CZ3   1 
ATOM   10336 C  CH2   . TRP A 1 2845 ? 241.250 220.265 262.188 1.00 21.02  ? 2845 TRP A CH2   1 
ATOM   10337 N  N     . THR A 1 2846 ? 238.576 215.833 264.235 1.00 20.83  ? 2846 THR A N     1 
ATOM   10338 C  CA    . THR A 1 2846 ? 237.909 216.893 264.982 1.00 18.83  ? 2846 THR A CA    1 
ATOM   10339 C  C     . THR A 1 2846 ? 237.969 216.635 266.481 1.00 22.98  ? 2846 THR A C     1 
ATOM   10340 O  O     . THR A 1 2846 ? 238.300 217.537 267.256 1.00 31.96  ? 2846 THR A O     1 
ATOM   10341 C  CB    . THR A 1 2846 ? 236.461 217.031 264.515 1.00 16.45  ? 2846 THR A CB    1 
ATOM   10342 O  OG1   . THR A 1 2846 ? 236.442 217.417 263.138 1.00 18.04  ? 2846 THR A OG1   1 
ATOM   10343 C  CG2   . THR A 1 2846 ? 235.732 218.082 265.332 1.00 19.63  ? 2846 THR A CG2   1 
ATOM   10344 N  N     . ASP A 1 2847 ? 237.677 215.403 266.907 1.00 20.47  ? 2847 ASP A N     1 
ATOM   10345 C  CA    . ASP A 1 2847 ? 237.748 215.074 268.330 1.00 24.30  ? 2847 ASP A CA    1 
ATOM   10346 C  C     . ASP A 1 2847 ? 239.156 215.277 268.873 1.00 31.68  ? 2847 ASP A C     1 
ATOM   10347 O  O     . ASP A 1 2847 ? 239.356 215.941 269.904 1.00 33.33  ? 2847 ASP A O     1 
ATOM   10348 C  CB    . ASP A 1 2847 ? 237.305 213.629 268.561 1.00 26.01  ? 2847 ASP A CB    1 
ATOM   10349 C  CG    . ASP A 1 2847 ? 235.832 213.420 268.312 1.00 36.24  ? 2847 ASP A CG    1 
ATOM   10350 O  OD1   . ASP A 1 2847 ? 235.056 214.376 268.501 1.00 39.65  ? 2847 ASP A OD1   1 
ATOM   10351 O  OD2   . ASP A 1 2847 ? 235.448 212.296 267.928 1.00 45.96  ? 2847 ASP A OD2   1 
ATOM   10352 N  N     . GLU A 1 2848 ? 240.150 214.708 268.185 1.00 29.89  ? 2848 GLU A N     1 
ATOM   10353 C  CA    . GLU A 1 2848 ? 241.516 214.757 268.686 1.00 28.77  ? 2848 GLU A CA    1 
ATOM   10354 C  C     . GLU A 1 2848 ? 242.016 216.189 268.779 1.00 32.02  ? 2848 GLU A C     1 
ATOM   10355 O  O     . GLU A 1 2848 ? 242.645 216.570 269.772 1.00 35.91  ? 2848 GLU A O     1 
ATOM   10356 C  CB    . GLU A 1 2848 ? 242.433 213.921 267.794 1.00 29.90  ? 2848 GLU A CB    1 
ATOM   10357 C  CG    . GLU A 1 2848 ? 243.877 213.866 268.267 1.00 44.87  ? 2848 GLU A CG    1 
ATOM   10358 C  CD    . GLU A 1 2848 ? 244.030 213.158 269.602 1.00 51.21  ? 2848 GLU A CD    1 
ATOM   10359 O  OE1   . GLU A 1 2848 ? 243.178 212.306 269.930 1.00 40.98  ? 2848 GLU A OE1   1 
ATOM   10360 O  OE2   . GLU A 1 2848 ? 245.005 213.456 270.324 1.00 56.78  ? 2848 GLU A OE2   1 
ATOM   10361 N  N     . ASN A 1 2849 ? 241.731 217.011 267.769 1.00 32.31  ? 2849 ASN A N     1 
ATOM   10362 C  CA    . ASN A 1 2849 ? 242.246 218.372 267.809 1.00 27.25  ? 2849 ASN A CA    1 
ATOM   10363 C  C     . ASN A 1 2849 ? 241.417 219.287 268.700 1.00 25.23  ? 2849 ASN A C     1 
ATOM   10364 O  O     . ASN A 1 2849 ? 241.949 220.277 269.206 1.00 30.86  ? 2849 ASN A O     1 
ATOM   10365 C  CB    . ASN A 1 2849 ? 242.369 218.934 266.396 1.00 25.18  ? 2849 ASN A CB    1 
ATOM   10366 C  CG    . ASN A 1 2849 ? 243.626 218.451 265.703 1.00 32.41  ? 2849 ASN A CG    1 
ATOM   10367 O  OD1   . ASN A 1 2849 ? 244.421 217.713 266.285 1.00 37.20  ? 2849 ASN A OD1   1 
ATOM   10368 N  ND2   . ASN A 1 2849 ? 243.829 218.886 264.472 1.00 34.05  ? 2849 ASN A ND2   1 
ATOM   10369 N  N     . ILE A 1 2850 ? 240.143 218.970 268.946 1.00 26.23  ? 2850 ILE A N     1 
ATOM   10370 C  CA    . ILE A 1 2850 ? 239.412 219.672 269.996 1.00 27.22  ? 2850 ILE A CA    1 
ATOM   10371 C  C     . ILE A 1 2850 ? 240.085 219.436 271.339 1.00 28.60  ? 2850 ILE A C     1 
ATOM   10372 O  O     . ILE A 1 2850 ? 240.332 220.375 272.108 1.00 33.96  ? 2850 ILE A O     1 
ATOM   10373 C  CB    . ILE A 1 2850 ? 237.937 219.231 270.019 1.00 22.92  ? 2850 ILE A CB    1 
ATOM   10374 C  CG1   . ILE A 1 2850 ? 237.142 219.956 268.936 1.00 23.67  ? 2850 ILE A CG1   1 
ATOM   10375 C  CG2   . ILE A 1 2850 ? 237.323 219.482 271.386 1.00 25.90  ? 2850 ILE A CG2   1 
ATOM   10376 C  CD1   . ILE A 1 2850 ? 235.749 219.411 268.743 1.00 21.02  ? 2850 ILE A CD1   1 
ATOM   10377 N  N     . ASP A 1 2851 ? 240.418 218.174 271.625 1.00 32.86  ? 2851 ASP A N     1 
ATOM   10378 C  CA    . ASP A 1 2851 ? 241.132 217.871 272.863 1.00 33.80  ? 2851 ASP A CA    1 
ATOM   10379 C  C     . ASP A 1 2851 ? 242.481 218.580 272.905 1.00 32.04  ? 2851 ASP A C     1 
ATOM   10380 O  O     . ASP A 1 2851 ? 242.865 219.140 273.939 1.00 29.54  ? 2851 ASP A O     1 
ATOM   10381 C  CB    . ASP A 1 2851 ? 241.316 216.361 273.007 1.00 37.58  ? 2851 ASP A CB    1 
ATOM   10382 C  CG    . ASP A 1 2851 ? 239.999 215.620 273.100 1.00 48.09  ? 2851 ASP A CG    1 
ATOM   10383 O  OD1   . ASP A 1 2851 ? 238.953 216.282 273.256 1.00 49.11  ? 2851 ASP A OD1   1 
ATOM   10384 O  OD2   . ASP A 1 2851 ? 240.009 214.372 273.019 1.00 52.38  ? 2851 ASP A OD2   1 
ATOM   10385 N  N     . THR A 1 2852 ? 243.208 218.568 271.786 1.00 30.09  ? 2852 THR A N     1 
ATOM   10386 C  CA    . THR A 1 2852 ? 244.537 219.173 271.744 1.00 25.12  ? 2852 THR A CA    1 
ATOM   10387 C  C     . THR A 1 2852 ? 244.471 220.675 271.993 1.00 27.79  ? 2852 THR A C     1 
ATOM   10388 O  O     . THR A 1 2852 ? 245.255 221.219 272.779 1.00 34.89  ? 2852 THR A O     1 
ATOM   10389 C  CB    . THR A 1 2852 ? 245.197 218.883 270.396 1.00 26.01  ? 2852 THR A CB    1 
ATOM   10390 O  OG1   . THR A 1 2852 ? 245.129 217.478 270.123 1.00 23.19  ? 2852 THR A OG1   1 
ATOM   10391 C  CG2   . THR A 1 2852 ? 246.651 219.321 270.412 1.00 28.62  ? 2852 THR A CG2   1 
ATOM   10392 N  N     . VAL A 1 2853 ? 243.538 221.363 271.332 1.00 29.37  ? 2853 VAL A N     1 
ATOM   10393 C  CA    . VAL A 1 2853 ? 243.397 222.804 271.509 1.00 26.75  ? 2853 VAL A CA    1 
ATOM   10394 C  C     . VAL A 1 2853 ? 242.975 223.130 272.935 1.00 26.83  ? 2853 VAL A C     1 
ATOM   10395 O  O     . VAL A 1 2853 ? 243.511 224.057 273.559 1.00 30.74  ? 2853 VAL A O     1 
ATOM   10396 C  CB    . VAL A 1 2853 ? 242.408 223.369 270.473 1.00 25.01  ? 2853 VAL A CB    1 
ATOM   10397 C  CG1   . VAL A 1 2853 ? 241.974 224.775 270.857 1.00 22.50  ? 2853 VAL A CG1   1 
ATOM   10398 C  CG2   . VAL A 1 2853 ? 243.032 223.360 269.085 1.00 21.75  ? 2853 VAL A CG2   1 
ATOM   10399 N  N     . ALA A 1 2854 ? 242.017 222.372 273.479 1.00 25.26  ? 2854 ALA A N     1 
ATOM   10400 C  CA    . ALA A 1 2854 ? 241.562 222.634 274.838 1.00 25.95  ? 2854 ALA A CA    1 
ATOM   10401 C  C     . ALA A 1 2854 ? 242.688 222.442 275.845 1.00 31.80  ? 2854 ALA A C     1 
ATOM   10402 O  O     . ALA A 1 2854 ? 242.828 223.231 276.786 1.00 34.30  ? 2854 ALA A O     1 
ATOM   10403 C  CB    . ALA A 1 2854 ? 240.379 221.729 275.179 1.00 23.88  ? 2854 ALA A CB    1 
ATOM   10404 N  N     . LEU A 1 2855 ? 243.505 221.402 275.664 1.00 32.08  ? 2855 LEU A N     1 
ATOM   10405 C  CA    . LEU A 1 2855 ? 244.616 221.182 276.582 1.00 35.70  ? 2855 LEU A CA    1 
ATOM   10406 C  C     . LEU A 1 2855 ? 245.709 222.227 276.403 1.00 38.40  ? 2855 LEU A C     1 
ATOM   10407 O  O     . LEU A 1 2855 ? 246.361 222.612 277.380 1.00 42.10  ? 2855 LEU A O     1 
ATOM   10408 C  CB    . LEU A 1 2855 ? 245.185 219.777 276.399 1.00 37.86  ? 2855 LEU A CB    1 
ATOM   10409 C  CG    . LEU A 1 2855 ? 244.617 218.707 277.333 1.00 42.65  ? 2855 LEU A CG    1 
ATOM   10410 C  CD1   . LEU A 1 2855 ? 244.960 219.039 278.776 1.00 47.46  ? 2855 LEU A CD1   1 
ATOM   10411 C  CD2   . LEU A 1 2855 ? 243.114 218.558 277.154 1.00 47.94  ? 2855 LEU A CD2   1 
ATOM   10412 N  N     . LYS A 1 2856 ? 245.929 222.691 275.171 1.00 29.53  ? 2856 LYS A N     1 
ATOM   10413 C  CA    . LYS A 1 2856 ? 246.930 223.724 274.934 1.00 29.73  ? 2856 LYS A CA    1 
ATOM   10414 C  C     . LYS A 1 2856 ? 246.541 225.034 275.606 1.00 29.62  ? 2856 LYS A C     1 
ATOM   10415 O  O     . LYS A 1 2856 ? 247.375 225.689 276.242 1.00 32.73  ? 2856 LYS A O     1 
ATOM   10416 C  CB    . LYS A 1 2856 ? 247.126 223.924 273.430 1.00 27.92  ? 2856 LYS A CB    1 
ATOM   10417 C  CG    . LYS A 1 2856 ? 247.890 225.183 273.062 1.00 30.73  ? 2856 LYS A CG    1 
ATOM   10418 C  CD    . LYS A 1 2856 ? 248.020 225.323 271.556 1.00 34.32  ? 2856 LYS A CD    1 
ATOM   10419 C  CE    . LYS A 1 2856 ? 248.787 226.582 271.184 1.00 36.28  ? 2856 LYS A CE    1 
ATOM   10420 N  NZ    . LYS A 1 2856 ? 248.878 226.762 269.711 1.00 32.57  ? 2856 LYS A NZ    1 
ATOM   10421 N  N     . HIS A 1 2857 ? 245.278 225.433 275.481 1.00 28.62  ? 2857 HIS A N     1 
ATOM   10422 C  CA    . HIS A 1 2857 ? 244.851 226.720 276.016 1.00 27.43  ? 2857 HIS A CA    1 
ATOM   10423 C  C     . HIS A 1 2857 ? 244.364 226.650 277.458 1.00 28.67  ? 2857 HIS A C     1 
ATOM   10424 O  O     . HIS A 1 2857 ? 244.223 227.698 278.096 1.00 24.45  ? 2857 HIS A O     1 
ATOM   10425 C  CB    . HIS A 1 2857 ? 243.761 227.320 275.127 1.00 23.84  ? 2857 HIS A CB    1 
ATOM   10426 C  CG    . HIS A 1 2857 ? 244.253 227.731 273.774 1.00 18.58  ? 2857 HIS A CG    1 
ATOM   10427 N  ND1   . HIS A 1 2857 ? 245.007 228.866 273.572 1.00 19.73  ? 2857 HIS A ND1   1 
ATOM   10428 C  CD2   . HIS A 1 2857 ? 244.112 227.152 272.560 1.00 22.59  ? 2857 HIS A CD2   1 
ATOM   10429 C  CE1   . HIS A 1 2857 ? 245.304 228.972 272.289 1.00 24.01  ? 2857 HIS A CE1   1 
ATOM   10430 N  NE2   . HIS A 1 2857 ? 244.772 227.945 271.652 1.00 25.28  ? 2857 HIS A NE2   1 
ATOM   10431 N  N     . PHE A 1 2858 ? 244.110 225.454 277.987 1.00 29.52  ? 2858 PHE A N     1 
ATOM   10432 C  CA    . PHE A 1 2858 ? 243.717 225.262 279.383 1.00 30.00  ? 2858 PHE A CA    1 
ATOM   10433 C  C     . PHE A 1 2858 ? 244.591 224.166 279.979 1.00 40.96  ? 2858 PHE A C     1 
ATOM   10434 O  O     . PHE A 1 2858 ? 244.181 223.001 280.059 1.00 45.81  ? 2858 PHE A O     1 
ATOM   10435 C  CB    . PHE A 1 2858 ? 242.231 224.924 279.503 1.00 26.87  ? 2858 PHE A CB    1 
ATOM   10436 C  CG    . PHE A 1 2858 ? 241.319 226.046 279.097 1.00 25.63  ? 2858 PHE A CG    1 
ATOM   10437 C  CD1   . PHE A 1 2858 ? 240.972 226.232 277.770 1.00 24.74  ? 2858 PHE A CD1   1 
ATOM   10438 C  CD2   . PHE A 1 2858 ? 240.805 226.914 280.045 1.00 22.44  ? 2858 PHE A CD2   1 
ATOM   10439 C  CE1   . PHE A 1 2858 ? 240.136 227.263 277.397 1.00 16.76  ? 2858 PHE A CE1   1 
ATOM   10440 C  CE2   . PHE A 1 2858 ? 239.967 227.946 279.676 1.00 21.46  ? 2858 PHE A CE2   1 
ATOM   10441 C  CZ    . PHE A 1 2858 ? 239.632 228.120 278.351 1.00 18.55  ? 2858 PHE A CZ    1 
ATOM   10442 N  N     . PRO A 1 2859 ? 245.811 224.505 280.400 1.00 44.53  ? 2859 PRO A N     1 
ATOM   10443 C  CA    . PRO A 1 2859 ? 246.746 223.474 280.874 1.00 41.74  ? 2859 PRO A CA    1 
ATOM   10444 C  C     . PRO A 1 2859 ? 246.330 222.810 282.178 1.00 49.96  ? 2859 PRO A C     1 
ATOM   10445 O  O     . PRO A 1 2859 ? 246.307 221.578 282.271 1.00 55.96  ? 2859 PRO A O     1 
ATOM   10446 C  CB    . PRO A 1 2859 ? 248.063 224.247 281.046 1.00 45.36  ? 2859 PRO A CB    1 
ATOM   10447 C  CG    . PRO A 1 2859 ? 247.870 225.539 280.303 1.00 39.67  ? 2859 PRO A CG    1 
ATOM   10448 C  CD    . PRO A 1 2859 ? 246.417 225.844 280.406 1.00 34.91  ? 2859 PRO A CD    1 
ATOM   10449 N  N     . ASN A 1 2860 ? 246.005 223.610 283.193 1.00 45.83  ? 2860 ASN A N     1 
ATOM   10450 C  CA    . ASN A 1 2860 ? 245.783 223.095 284.546 1.00 48.55  ? 2860 ASN A CA    1 
ATOM   10451 C  C     . ASN A 1 2860 ? 244.296 222.808 284.765 1.00 48.57  ? 2860 ASN A C     1 
ATOM   10452 O  O     . ASN A 1 2860 ? 243.592 223.491 285.509 1.00 49.84  ? 2860 ASN A O     1 
ATOM   10453 C  CB    . ASN A 1 2860 ? 246.321 224.077 285.579 1.00 53.00  ? 2860 ASN A CB    1 
ATOM   10454 C  CG    . ASN A 1 2860 ? 247.702 224.591 285.226 1.00 54.82  ? 2860 ASN A CG    1 
ATOM   10455 O  OD1   . ASN A 1 2860 ? 248.638 223.814 285.043 1.00 56.42  ? 2860 ASN A OD1   1 
ATOM   10456 N  ND2   . ASN A 1 2860 ? 247.837 225.908 285.129 1.00 55.84  ? 2860 ASN A ND2   1 
ATOM   10457 N  N     . ILE A 1 2861 ? 243.824 221.757 284.094 1.00 49.56  ? 2861 ILE A N     1 
ATOM   10458 C  CA    . ILE A 1 2861 ? 242.430 221.345 284.157 1.00 53.03  ? 2861 ILE A CA    1 
ATOM   10459 C  C     . ILE A 1 2861 ? 242.366 219.835 284.349 1.00 57.15  ? 2861 ILE A C     1 
ATOM   10460 O  O     . ILE A 1 2861 ? 243.348 219.116 284.160 1.00 64.96  ? 2861 ILE A O     1 
ATOM   10461 C  CB    . ILE A 1 2861 ? 241.637 221.753 282.897 1.00 48.55  ? 2861 ILE A CB    1 
ATOM   10462 C  CG1   . ILE A 1 2861 ? 242.222 221.067 281.661 1.00 50.36  ? 2861 ILE A CG1   1 
ATOM   10463 C  CG2   . ILE A 1 2861 ? 241.627 223.263 282.735 1.00 41.51  ? 2861 ILE A CG2   1 
ATOM   10464 C  CD1   . ILE A 1 2861 ? 241.376 221.215 280.417 1.00 45.29  ? 2861 ILE A CD1   1 
ATOM   10465 N  N     . ASP A 1 2862 ? 241.184 219.363 284.737 1.00 51.93  ? 2862 ASP A N     1 
ATOM   10466 C  CA    . ASP A 1 2862 ? 240.902 217.935 284.834 1.00 58.71  ? 2862 ASP A CA    1 
ATOM   10467 C  C     . ASP A 1 2862 ? 240.429 217.450 283.469 1.00 56.10  ? 2862 ASP A C     1 
ATOM   10468 O  O     . ASP A 1 2862 ? 239.326 217.792 283.028 1.00 60.49  ? 2862 ASP A O     1 
ATOM   10469 C  CB    . ASP A 1 2862 ? 239.858 217.665 285.914 1.00 61.54  ? 2862 ASP A CB    1 
ATOM   10470 C  CG    . ASP A 1 2862 ? 239.750 216.195 286.264 1.00 63.56  ? 2862 ASP A CG    1 
ATOM   10471 O  OD1   . ASP A 1 2862 ? 240.547 215.393 285.735 1.00 56.26  ? 2862 ASP A OD1   1 
ATOM   10472 O  OD2   . ASP A 1 2862 ? 238.867 215.843 287.074 1.00 69.00  ? 2862 ASP A OD2   1 
ATOM   10473 N  N     . ARG A 1 2863 ? 241.267 216.659 282.796 1.00 51.05  ? 2863 ARG A N     1 
ATOM   10474 C  CA    . ARG A 1 2863 ? 240.958 216.236 281.433 1.00 51.43  ? 2863 ARG A CA    1 
ATOM   10475 C  C     . ARG A 1 2863 ? 239.708 215.366 281.382 1.00 57.93  ? 2863 ARG A C     1 
ATOM   10476 O  O     . ARG A 1 2863 ? 238.853 215.550 280.508 1.00 53.83  ? 2863 ARG A O     1 
ATOM   10477 C  CB    . ARG A 1 2863 ? 242.150 215.489 280.837 1.00 54.32  ? 2863 ARG A CB    1 
ATOM   10478 C  CG    . ARG A 1 2863 ? 242.438 215.829 279.386 1.00 53.50  ? 2863 ARG A CG    1 
ATOM   10479 C  CD    . ARG A 1 2863 ? 243.678 215.107 278.885 1.00 56.51  ? 2863 ARG A CD    1 
ATOM   10480 N  NE    . ARG A 1 2863 ? 244.906 215.762 279.318 1.00 61.04  ? 2863 ARG A NE    1 
ATOM   10481 C  CZ    . ARG A 1 2863 ? 246.087 215.604 278.735 1.00 63.69  ? 2863 ARG A CZ    1 
ATOM   10482 N  NH1   . ARG A 1 2863 ? 246.239 214.811 277.688 1.00 66.45  ? 2863 ARG A NH1   1 
ATOM   10483 N  NH2   . ARG A 1 2863 ? 247.140 216.259 279.215 1.00 52.98  ? 2863 ARG A NH2   1 
ATOM   10484 N  N     . GLU A 1 2864 ? 239.581 214.416 282.308 1.00 62.58  ? 2864 GLU A N     1 
ATOM   10485 C  CA    . GLU A 1 2864 ? 238.458 213.485 282.256 1.00 58.50  ? 2864 GLU A CA    1 
ATOM   10486 C  C     . GLU A 1 2864 ? 237.143 214.173 282.602 1.00 54.49  ? 2864 GLU A C     1 
ATOM   10487 O  O     . GLU A 1 2864 ? 236.125 213.942 281.938 1.00 58.67  ? 2864 GLU A O     1 
ATOM   10488 C  CB    . GLU A 1 2864 ? 238.708 212.306 283.195 1.00 57.09  ? 2864 GLU A CB    1 
ATOM   10489 C  CG    . GLU A 1 2864 ? 237.843 211.090 282.900 1.00 60.92  ? 2864 GLU A CG    1 
ATOM   10490 C  CD    . GLU A 1 2864 ? 238.108 210.499 281.528 1.00 64.77  ? 2864 GLU A CD    1 
ATOM   10491 O  OE1   . GLU A 1 2864 ? 239.250 210.609 281.037 1.00 65.34  ? 2864 GLU A OE1   1 
ATOM   10492 O  OE2   . GLU A 1 2864 ? 237.170 209.923 280.938 1.00 58.66  ? 2864 GLU A OE2   1 
ATOM   10493 N  N     . LYS A 1 2865 ? 237.143 215.019 283.632 1.00 55.80  ? 2865 LYS A N     1 
ATOM   10494 C  CA    . LYS A 1 2865 ? 235.916 215.690 284.047 1.00 56.41  ? 2865 LYS A CA    1 
ATOM   10495 C  C     . LYS A 1 2865 ? 235.365 216.610 282.966 1.00 54.50  ? 2865 LYS A C     1 
ATOM   10496 O  O     . LYS A 1 2865 ? 234.149 216.818 282.906 1.00 52.35  ? 2865 LYS A O     1 
ATOM   10497 C  CB    . LYS A 1 2865 ? 236.162 216.480 285.333 1.00 51.69  ? 2865 LYS A CB    1 
ATOM   10498 C  CG    . LYS A 1 2865 ? 234.903 217.020 285.991 1.00 52.50  ? 2865 LYS A CG    1 
ATOM   10499 C  CD    . LYS A 1 2865 ? 235.074 217.131 287.498 1.00 60.74  ? 2865 LYS A CD    1 
ATOM   10500 C  CE    . LYS A 1 2865 ? 234.018 218.034 288.109 1.00 62.75  ? 2865 LYS A CE    1 
ATOM   10501 N  NZ    . LYS A 1 2865 ? 233.875 219.307 287.349 1.00 50.73  ? 2865 LYS A NZ    1 
ATOM   10502 N  N     . ALA A 1 2866 ? 236.227 217.159 282.107 1.00 52.62  ? 2866 ALA A N     1 
ATOM   10503 C  CA    . ALA A 1 2866 ? 235.794 218.054 281.046 1.00 41.84  ? 2866 ALA A CA    1 
ATOM   10504 C  C     . ALA A 1 2866 ? 235.653 217.384 279.687 1.00 41.00  ? 2866 ALA A C     1 
ATOM   10505 O  O     . ALA A 1 2866 ? 234.975 217.938 278.818 1.00 38.53  ? 2866 ALA A O     1 
ATOM   10506 C  CB    . ALA A 1 2866 ? 236.770 219.232 280.912 1.00 34.27  ? 2866 ALA A CB    1 
ATOM   10507 N  N     . MET A 1 2867 ? 236.264 216.220 279.483 1.00 46.29  ? 2867 MET A N     1 
ATOM   10508 C  CA    . MET A 1 2867 ? 236.303 215.580 278.172 1.00 42.52  ? 2867 MET A CA    1 
ATOM   10509 C  C     . MET A 1 2867 ? 235.900 214.116 278.254 1.00 48.93  ? 2867 MET A C     1 
ATOM   10510 O  O     . MET A 1 2867 ? 236.524 213.248 277.637 1.00 54.31  ? 2867 MET A O     1 
ATOM   10511 C  CB    . MET A 1 2867 ? 237.686 215.712 277.542 1.00 45.13  ? 2867 MET A CB    1 
ATOM   10512 C  CG    . MET A 1 2867 ? 238.096 217.135 277.215 1.00 47.19  ? 2867 MET A CG    1 
ATOM   10513 S  SD    . MET A 1 2867 ? 237.032 217.879 275.968 1.00 69.86  ? 2867 MET A SD    1 
ATOM   10514 C  CE    . MET A 1 2867 ? 237.624 219.562 275.998 1.00 42.65  ? 2867 MET A CE    1 
ATOM   10515 N  N     . SER A 1 2868 ? 234.856 213.808 279.017 1.00 42.36  ? 2868 SER A N     1 
ATOM   10516 C  CA    . SER A 1 2868 ? 234.245 212.491 278.920 1.00 38.40  ? 2868 SER A CA    1 
ATOM   10517 C  C     . SER A 1 2868 ? 233.626 212.341 277.537 1.00 39.21  ? 2868 SER A C     1 
ATOM   10518 O  O     . SER A 1 2868 ? 232.701 213.077 277.186 1.00 38.15  ? 2868 SER A O     1 
ATOM   10519 C  CB    . SER A 1 2868 ? 233.189 212.307 280.008 1.00 45.89  ? 2868 SER A CB    1 
ATOM   10520 O  OG    . SER A 1 2868 ? 233.750 212.484 281.298 1.00 46.29  ? 2868 SER A OG    1 
ATOM   10521 N  N     . ARG A 1 2869 ? 234.136 211.386 276.762 1.00 43.39  ? 2869 ARG A N     1 
ATOM   10522 C  CA    . ARG A 1 2869 ? 233.871 211.358 275.324 1.00 46.39  ? 2869 ARG A CA    1 
ATOM   10523 C  C     . ARG A 1 2869 ? 232.393 211.415 274.952 1.00 48.32  ? 2869 ARG A C     1 
ATOM   10524 O  O     . ARG A 1 2869 ? 232.063 212.124 273.986 1.00 51.74  ? 2869 ARG A O     1 
ATOM   10525 C  CB    . ARG A 1 2869 ? 234.542 210.128 274.699 1.00 56.11  ? 2869 ARG A CB    1 
ATOM   10526 C  CG    . ARG A 1 2869 ? 235.986 210.367 274.275 1.00 59.04  ? 2869 ARG A CG    1 
ATOM   10527 C  CD    . ARG A 1 2869 ? 236.087 211.457 273.212 1.00 60.51  ? 2869 ARG A CD    1 
ATOM   10528 N  NE    . ARG A 1 2869 ? 236.425 212.756 273.784 1.00 58.23  ? 2869 ARG A NE    1 
ATOM   10529 C  CZ    . ARG A 1 2869 ? 236.144 213.924 273.220 1.00 51.89  ? 2869 ARG A CZ    1 
ATOM   10530 N  NH1   . ARG A 1 2869 ? 235.505 213.998 272.064 1.00 42.33  ? 2869 ARG A NH1   1 
ATOM   10531 N  NH2   . ARG A 1 2869 ? 236.515 215.045 273.832 1.00 46.47  ? 2869 ARG A NH2   1 
ATOM   10532 N  N     . PRO A 1 2870 ? 231.466 210.722 275.630 1.00 42.26  ? 2870 PRO A N     1 
ATOM   10533 C  CA    . PRO A 1 2870 ? 230.045 210.967 275.345 1.00 36.34  ? 2870 PRO A CA    1 
ATOM   10534 C  C     . PRO A 1 2870 ? 229.592 212.325 275.860 1.00 32.05  ? 2870 PRO A C     1 
ATOM   10535 O  O     . PRO A 1 2870 ? 228.920 212.412 276.892 1.00 40.01  ? 2870 PRO A O     1 
ATOM   10536 C  CB    . PRO A 1 2870 ? 229.330 209.819 276.071 1.00 29.97  ? 2870 PRO A CB    1 
ATOM   10537 C  CG    . PRO A 1 2870 ? 230.383 208.796 276.319 1.00 41.25  ? 2870 PRO A CG    1 
ATOM   10538 C  CD    . PRO A 1 2870 ? 231.642 209.569 276.528 1.00 38.24  ? 2870 PRO A CD    1 
ATOM   10539 N  N     . ILE A 1 2871 ? 229.960 213.392 275.152 1.00 22.87  ? 2871 ILE A N     1 
ATOM   10540 C  CA    . ILE A 1 2871 ? 229.592 214.753 275.542 1.00 21.69  ? 2871 ILE A CA    1 
ATOM   10541 C  C     . ILE A 1 2871 ? 228.157 214.983 275.074 1.00 18.17  ? 2871 ILE A C     1 
ATOM   10542 O  O     . ILE A 1 2871 ? 227.908 215.208 273.890 1.00 15.61  ? 2871 ILE A O     1 
ATOM   10543 C  CB    . ILE A 1 2871 ? 230.547 215.797 274.961 1.00 23.00  ? 2871 ILE A CB    1 
ATOM   10544 C  CG1   . ILE A 1 2871 ? 232.000 215.403 275.224 1.00 24.07  ? 2871 ILE A CG1   1 
ATOM   10545 C  CG2   . ILE A 1 2871 ? 230.258 217.163 275.557 1.00 15.08  ? 2871 ILE A CG2   1 
ATOM   10546 C  CD1   . ILE A 1 2871 ? 232.998 216.479 274.866 1.00 21.26  ? 2871 ILE A CD1   1 
ATOM   10547 N  N     . LEU A 1 2872 ? 227.209 214.929 276.006 1.00 17.18  ? 2872 LEU A N     1 
ATOM   10548 C  CA    . LEU A 1 2872 ? 225.798 215.102 275.697 1.00 14.36  ? 2872 LEU A CA    1 
ATOM   10549 C  C     . LEU A 1 2872 ? 225.208 216.180 276.591 1.00 15.40  ? 2872 LEU A C     1 
ATOM   10550 O  O     . LEU A 1 2872 ? 225.455 216.200 277.800 1.00 15.28  ? 2872 LEU A O     1 
ATOM   10551 C  CB    . LEU A 1 2872 ? 225.022 213.794 275.881 1.00 17.27  ? 2872 LEU A CB    1 
ATOM   10552 C  CG    . LEU A 1 2872 ? 225.430 212.619 274.995 1.00 18.85  ? 2872 LEU A CG    1 
ATOM   10553 C  CD1   . LEU A 1 2872 ? 224.640 211.377 275.369 1.00 20.10  ? 2872 LEU A CD1   1 
ATOM   10554 C  CD2   . LEU A 1 2872 ? 225.239 212.960 273.527 1.00 14.36  ? 2872 LEU A CD2   1 
ATOM   10555 N  N     . TYR A 1 2873 ? 224.429 217.074 275.988 1.00 18.09  ? 2873 TYR A N     1 
ATOM   10556 C  CA    . TYR A 1 2873 ? 223.735 218.132 276.703 1.00 13.82  ? 2873 TYR A CA    1 
ATOM   10557 C  C     . TYR A 1 2873 ? 222.262 218.100 276.329 1.00 14.13  ? 2873 TYR A C     1 
ATOM   10558 O  O     . TYR A 1 2873 ? 221.917 217.928 275.156 1.00 19.05  ? 2873 TYR A O     1 
ATOM   10559 C  CB    . TYR A 1 2873 ? 224.320 219.512 276.379 1.00 14.35  ? 2873 TYR A CB    1 
ATOM   10560 C  CG    . TYR A 1 2873 ? 225.540 219.884 277.186 1.00 11.16  ? 2873 TYR A CG    1 
ATOM   10561 C  CD1   . TYR A 1 2873 ? 226.751 219.239 276.989 1.00 12.83  ? 2873 TYR A CD1   1 
ATOM   10562 C  CD2   . TYR A 1 2873 ? 225.480 220.886 278.144 1.00 11.61  ? 2873 TYR A CD2   1 
ATOM   10563 C  CE1   . TYR A 1 2873 ? 227.868 219.580 277.724 1.00 14.07  ? 2873 TYR A CE1   1 
ATOM   10564 C  CE2   . TYR A 1 2873 ? 226.592 221.233 278.883 1.00 15.32  ? 2873 TYR A CE2   1 
ATOM   10565 C  CZ    . TYR A 1 2873 ? 227.784 220.577 278.670 1.00 18.17  ? 2873 TYR A CZ    1 
ATOM   10566 O  OH    . TYR A 1 2873 ? 228.894 220.917 279.404 1.00 16.84  ? 2873 TYR A OH    1 
ATOM   10567 N  N     . SER A 1 2874 ? 221.396 218.266 277.324 1.00 16.01  ? 2874 SER A N     1 
ATOM   10568 C  CA    . SER A 1 2874 ? 219.964 218.266 277.070 1.00 15.79  ? 2874 SER A CA    1 
ATOM   10569 C  C     . SER A 1 2874 ? 219.256 219.024 278.181 1.00 16.63  ? 2874 SER A C     1 
ATOM   10570 O  O     . SER A 1 2874 ? 219.762 219.127 279.301 1.00 22.67  ? 2874 SER A O     1 
ATOM   10571 C  CB    . SER A 1 2874 ? 219.412 216.840 276.966 1.00 16.62  ? 2874 SER A CB    1 
ATOM   10572 O  OG    . SER A 1 2874 ? 218.044 216.851 276.600 1.00 17.57  ? 2874 SER A OG    1 
ATOM   10573 N  N     . ASN A 1 2875 ? 218.080 219.555 277.851 1.00 16.21  ? 2875 ASN A N     1 
ATOM   10574 C  CA    . ASN A 1 2875 ? 217.197 220.190 278.820 1.00 20.39  ? 2875 ASN A CA    1 
ATOM   10575 C  C     . ASN A 1 2875 ? 215.902 219.401 278.994 1.00 22.43  ? 2875 ASN A C     1 
ATOM   10576 O  O     . ASN A 1 2875 ? 214.856 219.970 279.311 1.00 25.74  ? 2875 ASN A O     1 
ATOM   10577 C  CB    . ASN A 1 2875 ? 216.892 221.630 278.412 1.00 23.55  ? 2875 ASN A CB    1 
ATOM   10578 C  CG    . ASN A 1 2875 ? 216.294 221.730 277.023 1.00 24.86  ? 2875 ASN A CG    1 
ATOM   10579 O  OD1   . ASN A 1 2875 ? 216.155 220.731 276.320 1.00 28.30  ? 2875 ASN A OD1   1 
ATOM   10580 N  ND2   . ASN A 1 2875 ? 215.935 222.942 276.623 1.00 32.54  ? 2875 ASN A ND2   1 
ATOM   10581 N  N     . TRP A 1 2876 ? 215.961 218.090 278.772 1.00 23.45  ? 2876 TRP A N     1 
ATOM   10582 C  CA    . TRP A 1 2876 ? 214.791 217.232 278.897 1.00 22.07  ? 2876 TRP A CA    1 
ATOM   10583 C  C     . TRP A 1 2876 ? 214.628 216.711 280.319 1.00 25.94  ? 2876 TRP A C     1 
ATOM   10584 O  O     . TRP A 1 2876 ? 213.521 216.721 280.866 1.00 35.87  ? 2876 TRP A O     1 
ATOM   10585 C  CB    . TRP A 1 2876 ? 214.892 216.062 277.914 1.00 20.07  ? 2876 TRP A CB    1 
ATOM   10586 C  CG    . TRP A 1 2876 ? 214.538 216.421 276.507 1.00 19.17  ? 2876 TRP A CG    1 
ATOM   10587 C  CD1   . TRP A 1 2876 ? 213.866 217.530 276.088 1.00 19.09  ? 2876 TRP A CD1   1 
ATOM   10588 C  CD2   . TRP A 1 2876 ? 214.829 215.660 275.330 1.00 19.52  ? 2876 TRP A CD2   1 
ATOM   10589 N  NE1   . TRP A 1 2876 ? 213.724 217.510 274.723 1.00 16.85  ? 2876 TRP A NE1   1 
ATOM   10590 C  CE2   . TRP A 1 2876 ? 214.306 216.371 274.234 1.00 18.33  ? 2876 TRP A CE2   1 
ATOM   10591 C  CE3   . TRP A 1 2876 ? 215.482 214.446 275.097 1.00 16.73  ? 2876 TRP A CE3   1 
ATOM   10592 C  CZ2   . TRP A 1 2876 ? 214.417 215.910 272.924 1.00 17.10  ? 2876 TRP A CZ2   1 
ATOM   10593 C  CZ3   . TRP A 1 2876 ? 215.591 213.992 273.798 1.00 16.82  ? 2876 TRP A CZ3   1 
ATOM   10594 C  CH2   . TRP A 1 2876 ? 215.061 214.722 272.728 1.00 17.05  ? 2876 TRP A CH2   1 
ATOM   10595 N  N     . LEU A 1 2877 ? 215.721 216.250 280.926 1.00 22.54  ? 2877 LEU A N     1 
ATOM   10596 C  CA    . LEU A 1 2877 ? 215.650 215.729 282.286 1.00 23.78  ? 2877 LEU A CA    1 
ATOM   10597 C  C     . LEU A 1 2877 ? 215.427 216.845 283.297 1.00 30.80  ? 2877 LEU A C     1 
ATOM   10598 O  O     . LEU A 1 2877 ? 214.671 216.675 284.261 1.00 36.79  ? 2877 LEU A O     1 
ATOM   10599 C  CB    . LEU A 1 2877 ? 216.924 214.951 282.614 1.00 21.02  ? 2877 LEU A CB    1 
ATOM   10600 C  CG    . LEU A 1 2877 ? 216.936 213.459 282.270 1.00 22.96  ? 2877 LEU A CG    1 
ATOM   10601 C  CD1   . LEU A 1 2877 ? 216.963 213.236 280.767 1.00 22.06  ? 2877 LEU A CD1   1 
ATOM   10602 C  CD2   . LEU A 1 2877 ? 218.121 212.779 282.929 1.00 28.79  ? 2877 LEU A CD2   1 
ATOM   10603 N  N     . SER A 1 2878 ? 216.070 217.991 283.097 1.00 28.89  ? 2878 SER A N     1 
ATOM   10604 C  CA    . SER A 1 2878 ? 215.984 219.118 284.014 1.00 29.86  ? 2878 SER A CA    1 
ATOM   10605 C  C     . SER A 1 2878 ? 215.518 220.352 283.253 1.00 36.97  ? 2878 SER A C     1 
ATOM   10606 O  O     . SER A 1 2878 ? 215.336 220.326 282.033 1.00 39.97  ? 2878 SER A O     1 
ATOM   10607 C  CB    . SER A 1 2878 ? 217.332 219.373 284.699 1.00 30.02  ? 2878 SER A CB    1 
ATOM   10608 O  OG    . SER A 1 2878 ? 218.278 219.878 283.777 1.00 37.90  ? 2878 SER A OG    1 
ATOM   10609 N  N     . LYS A 1 2879 ? 215.316 221.447 283.988 1.00 37.64  ? 2879 LYS A N     1 
ATOM   10610 C  CA    . LYS A 1 2879 ? 214.857 222.685 283.369 1.00 35.95  ? 2879 LYS A CA    1 
ATOM   10611 C  C     . LYS A 1 2879 ? 215.966 223.388 282.598 1.00 35.26  ? 2879 LYS A C     1 
ATOM   10612 O  O     . LYS A 1 2879 ? 215.683 224.091 281.621 1.00 41.79  ? 2879 LYS A O     1 
ATOM   10613 C  CB    . LYS A 1 2879 ? 214.284 223.624 284.432 1.00 37.70  ? 2879 LYS A CB    1 
ATOM   10614 C  CG    . LYS A 1 2879 ? 215.132 223.729 285.686 1.00 42.20  ? 2879 LYS A CG    1 
ATOM   10615 C  CD    . LYS A 1 2879 ? 214.938 225.068 286.375 1.00 46.58  ? 2879 LYS A CD    1 
ATOM   10616 C  CE    . LYS A 1 2879 ? 215.809 225.181 287.614 1.00 54.17  ? 2879 LYS A CE    1 
ATOM   10617 N  NZ    . LYS A 1 2879 ? 216.149 226.596 287.924 1.00 54.09  ? 2879 LYS A NZ    1 
ATOM   10618 N  N     . ASP A 1 2880 ? 217.215 223.216 283.012 1.00 34.11  ? 2880 ASP A N     1 
ATOM   10619 C  CA    . ASP A 1 2880 ? 218.344 223.883 282.386 1.00 32.00  ? 2880 ASP A CA    1 
ATOM   10620 C  C     . ASP A 1 2880 ? 219.015 222.970 281.365 1.00 25.89  ? 2880 ASP A C     1 
ATOM   10621 O  O     . ASP A 1 2880 ? 218.763 221.766 281.302 1.00 29.56  ? 2880 ASP A O     1 
ATOM   10622 C  CB    . ASP A 1 2880 ? 219.357 224.332 283.444 1.00 33.37  ? 2880 ASP A CB    1 
ATOM   10623 C  CG    . ASP A 1 2880 ? 218.878 225.532 284.232 1.00 41.50  ? 2880 ASP A CG    1 
ATOM   10624 O  OD1   . ASP A 1 2880 ? 217.825 226.099 283.872 1.00 40.43  ? 2880 ASP A OD1   1 
ATOM   10625 O  OD2   . ASP A 1 2880 ? 219.556 225.910 285.209 1.00 48.50  ? 2880 ASP A OD2   1 
ATOM   10626 N  N     . TYR A 1 2881 ? 219.886 223.570 280.559 1.00 25.25  ? 2881 TYR A N     1 
ATOM   10627 C  CA    . TYR A 1 2881 ? 220.621 222.851 279.520 1.00 18.44  ? 2881 TYR A CA    1 
ATOM   10628 C  C     . TYR A 1 2881 ? 221.943 222.317 280.076 1.00 20.73  ? 2881 TYR A C     1 
ATOM   10629 O  O     . TYR A 1 2881 ? 223.033 222.617 279.591 1.00 26.86  ? 2881 TYR A O     1 
ATOM   10630 C  CB    . TYR A 1 2881 ? 220.844 223.758 278.316 1.00 21.49  ? 2881 TYR A CB    1 
ATOM   10631 C  CG    . TYR A 1 2881 ? 221.340 223.044 277.083 1.00 19.37  ? 2881 TYR A CG    1 
ATOM   10632 C  CD1   . TYR A 1 2881 ? 220.562 222.085 276.453 1.00 16.50  ? 2881 TYR A CD1   1 
ATOM   10633 C  CD2   . TYR A 1 2881 ? 222.587 223.333 276.546 1.00 17.02  ? 2881 TYR A CD2   1 
ATOM   10634 C  CE1   . TYR A 1 2881 ? 221.012 221.432 275.326 1.00 14.45  ? 2881 TYR A CE1   1 
ATOM   10635 C  CE2   . TYR A 1 2881 ? 223.045 222.687 275.420 1.00 17.19  ? 2881 TYR A CE2   1 
ATOM   10636 C  CZ    . TYR A 1 2881 ? 222.253 221.738 274.813 1.00 14.62  ? 2881 TYR A CZ    1 
ATOM   10637 O  OH    . TYR A 1 2881 ? 222.708 221.089 273.692 1.00 12.24  ? 2881 TYR A OH    1 
ATOM   10638 N  N     . ILE A 1 2882 ? 221.821 221.513 281.125 1.00 20.18  ? 2882 ILE A N     1 
ATOM   10639 C  CA    . ILE A 1 2882 ? 222.971 220.911 281.795 1.00 16.48  ? 2882 ILE A CA    1 
ATOM   10640 C  C     . ILE A 1 2882 ? 223.367 219.645 281.042 1.00 18.50  ? 2882 ILE A C     1 
ATOM   10641 O  O     . ILE A 1 2882 ? 222.558 219.116 280.266 1.00 19.82  ? 2882 ILE A O     1 
ATOM   10642 C  CB    . ILE A 1 2882 ? 222.658 220.610 283.269 1.00 19.75  ? 2882 ILE A CB    1 
ATOM   10643 C  CG1   . ILE A 1 2882 ? 221.519 219.596 283.376 1.00 15.07  ? 2882 ILE A CG1   1 
ATOM   10644 C  CG2   . ILE A 1 2882 ? 222.309 221.891 284.007 1.00 27.64  ? 2882 ILE A CG2   1 
ATOM   10645 C  CD1   . ILE A 1 2882 ? 221.307 219.067 284.772 1.00 25.45  ? 2882 ILE A CD1   1 
ATOM   10646 N  N     . PRO A 1 2883 ? 224.588 219.138 281.215 1.00 17.84  ? 2883 PRO A N     1 
ATOM   10647 C  CA    . PRO A 1 2883 ? 224.944 217.862 280.583 1.00 16.18  ? 2883 PRO A CA    1 
ATOM   10648 C  C     . PRO A 1 2883 ? 224.086 216.724 281.116 1.00 16.89  ? 2883 PRO A C     1 
ATOM   10649 O  O     . PRO A 1 2883 ? 223.654 216.727 282.270 1.00 16.92  ? 2883 PRO A O     1 
ATOM   10650 C  CB    . PRO A 1 2883 ? 226.420 217.676 280.956 1.00 14.55  ? 2883 PRO A CB    1 
ATOM   10651 C  CG    . PRO A 1 2883 ? 226.638 218.569 282.129 1.00 13.38  ? 2883 PRO A CG    1 
ATOM   10652 C  CD    . PRO A 1 2883 ? 225.733 219.735 281.921 1.00 12.39  ? 2883 PRO A CD    1 
ATOM   10653 N  N     . VAL A 1 2884 ? 223.840 215.741 280.254 1.00 18.54  ? 2884 VAL A N     1 
ATOM   10654 C  CA    . VAL A 1 2884 ? 222.987 214.605 280.575 1.00 16.07  ? 2884 VAL A CA    1 
ATOM   10655 C  C     . VAL A 1 2884 ? 223.798 213.324 280.431 1.00 20.13  ? 2884 VAL A C     1 
ATOM   10656 O  O     . VAL A 1 2884 ? 224.696 213.235 279.587 1.00 22.03  ? 2884 VAL A O     1 
ATOM   10657 C  CB    . VAL A 1 2884 ? 221.725 214.573 279.684 1.00 14.75  ? 2884 VAL A CB    1 
ATOM   10658 C  CG1   . VAL A 1 2884 ? 222.050 214.084 278.281 1.00 14.21  ? 2884 VAL A CG1   1 
ATOM   10659 C  CG2   . VAL A 1 2884 ? 220.649 213.708 280.318 1.00 19.59  ? 2884 VAL A CG2   1 
ATOM   10660 N  N     . ASP A 1 2885 ? 223.504 212.350 281.287 1.00 25.00  ? 2885 ASP A N     1 
ATOM   10661 C  CA    . ASP A 1 2885 ? 224.136 211.045 281.188 1.00 25.70  ? 2885 ASP A CA    1 
ATOM   10662 C  C     . ASP A 1 2885 ? 223.482 210.228 280.079 1.00 24.53  ? 2885 ASP A C     1 
ATOM   10663 O  O     . ASP A 1 2885 ? 222.286 210.356 279.806 1.00 22.28  ? 2885 ASP A O     1 
ATOM   10664 C  CB    . ASP A 1 2885 ? 224.043 210.306 282.525 1.00 28.18  ? 2885 ASP A CB    1 
ATOM   10665 C  CG    . ASP A 1 2885 ? 224.358 208.829 282.401 1.00 34.16  ? 2885 ASP A CG    1 
ATOM   10666 O  OD1   . ASP A 1 2885 ? 225.461 208.494 281.923 1.00 42.98  ? 2885 ASP A OD1   1 
ATOM   10667 O  OD2   . ASP A 1 2885 ? 223.506 208.002 282.783 1.00 33.00  ? 2885 ASP A OD2   1 
ATOM   10668 N  N     . GLN A 1 2886 ? 224.287 209.383 279.429 1.00 27.81  ? 2886 GLN A N     1 
ATOM   10669 C  CA    . GLN A 1 2886 ? 223.791 208.607 278.298 1.00 21.95  ? 2886 GLN A CA    1 
ATOM   10670 C  C     . GLN A 1 2886 ? 222.707 207.622 278.722 1.00 27.50  ? 2886 GLN A C     1 
ATOM   10671 O  O     . GLN A 1 2886 ? 221.720 207.434 278.003 1.00 26.95  ? 2886 GLN A O     1 
ATOM   10672 C  CB    . GLN A 1 2886 ? 224.948 207.874 277.620 1.00 17.45  ? 2886 GLN A CB    1 
ATOM   10673 C  CG    . GLN A 1 2886 ? 224.591 207.264 276.275 1.00 19.08  ? 2886 GLN A CG    1 
ATOM   10674 C  CD    . GLN A 1 2886 ? 225.810 206.934 275.441 1.00 20.31  ? 2886 GLN A CD    1 
ATOM   10675 O  OE1   . GLN A 1 2886 ? 226.663 206.148 275.849 1.00 28.11  ? 2886 GLN A OE1   1 
ATOM   10676 N  NE2   . GLN A 1 2886 ? 225.900 207.537 274.262 1.00 20.42  ? 2886 GLN A NE2   1 
ATOM   10677 N  N     . GLU A 1 2887 ? 222.868 206.986 279.884 1.00 27.89  ? 2887 GLU A N     1 
ATOM   10678 C  CA    . GLU A 1 2887 ? 221.904 205.974 280.309 1.00 27.06  ? 2887 GLU A CA    1 
ATOM   10679 C  C     . GLU A 1 2887 ? 220.579 206.600 280.734 1.00 27.56  ? 2887 GLU A C     1 
ATOM   10680 O  O     . GLU A 1 2887 ? 219.507 206.107 280.361 1.00 34.71  ? 2887 GLU A O     1 
ATOM   10681 C  CB    . GLU A 1 2887 ? 222.494 205.133 281.439 1.00 28.97  ? 2887 GLU A CB    1 
ATOM   10682 C  CG    . GLU A 1 2887 ? 223.742 204.363 281.038 1.00 33.61  ? 2887 GLU A CG    1 
ATOM   10683 C  CD    . GLU A 1 2887 ? 223.563 203.606 279.735 1.00 41.74  ? 2887 GLU A CD    1 
ATOM   10684 O  OE1   . GLU A 1 2887 ? 222.562 202.871 279.604 1.00 36.88  ? 2887 GLU A OE1   1 
ATOM   10685 O  OE2   . GLU A 1 2887 ? 224.424 203.747 278.840 1.00 36.64  ? 2887 GLU A OE2   1 
ATOM   10686 N  N     . GLU A 1 2888 ? 220.629 207.678 281.520 1.00 25.59  ? 2888 GLU A N     1 
ATOM   10687 C  CA    . GLU A 1 2888 ? 219.397 208.360 281.904 1.00 27.53  ? 2888 GLU A CA    1 
ATOM   10688 C  C     . GLU A 1 2888 ? 218.693 208.940 280.686 1.00 28.19  ? 2888 GLU A C     1 
ATOM   10689 O  O     . GLU A 1 2888 ? 217.459 208.899 280.592 1.00 29.80  ? 2888 GLU A O     1 
ATOM   10690 C  CB    . GLU A 1 2888 ? 219.697 209.455 282.928 1.00 25.59  ? 2888 GLU A CB    1 
ATOM   10691 C  CG    . GLU A 1 2888 ? 220.752 209.074 283.947 1.00 32.67  ? 2888 GLU A CG    1 
ATOM   10692 C  CD    . GLU A 1 2888 ? 220.896 210.101 285.050 1.00 60.12  ? 2888 GLU A CD    1 
ATOM   10693 O  OE1   . GLU A 1 2888 ? 220.302 211.193 284.928 1.00 63.29  ? 2888 GLU A OE1   1 
ATOM   10694 O  OE2   . GLU A 1 2888 ? 221.604 209.817 286.040 1.00 58.02  ? 2888 GLU A OE2   1 
ATOM   10695 N  N     . LEU A 1 2889 ? 219.462 209.485 279.742 1.00 21.58  ? 2889 LEU A N     1 
ATOM   10696 C  CA    . LEU A 1 2889 ? 218.871 209.977 278.504 1.00 22.35  ? 2889 LEU A CA    1 
ATOM   10697 C  C     . LEU A 1 2889 ? 218.213 208.846 277.727 1.00 25.75  ? 2889 LEU A C     1 
ATOM   10698 O  O     . LEU A 1 2889 ? 217.126 209.020 277.169 1.00 23.19  ? 2889 LEU A O     1 
ATOM   10699 C  CB    . LEU A 1 2889 ? 219.933 210.672 277.653 1.00 17.52  ? 2889 LEU A CB    1 
ATOM   10700 C  CG    . LEU A 1 2889 ? 219.522 211.044 276.228 1.00 18.93  ? 2889 LEU A CG    1 
ATOM   10701 C  CD1   . LEU A 1 2889 ? 218.516 212.180 276.246 1.00 15.41  ? 2889 LEU A CD1   1 
ATOM   10702 C  CD2   . LEU A 1 2889 ? 220.738 211.411 275.395 1.00 20.07  ? 2889 LEU A CD2   1 
ATOM   10703 N  N     . ARG A 1 2890 ? 218.856 207.677 277.684 1.00 26.46  ? 2890 ARG A N     1 
ATOM   10704 C  CA    . ARG A 1 2890 ? 218.271 206.535 276.990 1.00 23.89  ? 2890 ARG A CA    1 
ATOM   10705 C  C     . ARG A 1 2890 ? 216.963 206.102 277.638 1.00 26.20  ? 2890 ARG A C     1 
ATOM   10706 O  O     . ARG A 1 2890 ? 215.987 205.805 276.941 1.00 31.33  ? 2890 ARG A O     1 
ATOM   10707 C  CB    . ARG A 1 2890 ? 219.262 205.374 276.956 1.00 25.92  ? 2890 ARG A CB    1 
ATOM   10708 C  CG    . ARG A 1 2890 ? 218.873 204.257 276.002 1.00 25.53  ? 2890 ARG A CG    1 
ATOM   10709 C  CD    . ARG A 1 2890 ? 219.660 202.992 276.287 1.00 24.02  ? 2890 ARG A CD    1 
ATOM   10710 N  NE    . ARG A 1 2890 ? 221.098 203.234 276.284 1.00 27.89  ? 2890 ARG A NE    1 
ATOM   10711 C  CZ    . ARG A 1 2890 ? 221.845 203.282 275.190 1.00 33.93  ? 2890 ARG A CZ    1 
ATOM   10712 N  NH1   . ARG A 1 2890 ? 221.324 203.102 273.988 1.00 28.59  ? 2890 ARG A NH1   1 
ATOM   10713 N  NH2   . ARG A 1 2890 ? 223.151 203.514 275.306 1.00 28.87  ? 2890 ARG A NH2   1 
ATOM   10714 N  N     . ASP A 1 2891 ? 216.922 206.057 278.972 1.00 24.19  ? 2891 ASP A N     1 
ATOM   10715 C  CA    . ASP A 1 2891 ? 215.683 205.685 279.655 1.00 26.19  ? 2891 ASP A CA    1 
ATOM   10716 C  C     . ASP A 1 2891 ? 214.577 206.703 279.395 1.00 26.73  ? 2891 ASP A C     1 
ATOM   10717 O  O     . ASP A 1 2891 ? 213.419 206.330 279.146 1.00 27.03  ? 2891 ASP A O     1 
ATOM   10718 C  CB    . ASP A 1 2891 ? 215.924 205.531 281.156 1.00 31.68  ? 2891 ASP A CB    1 
ATOM   10719 C  CG    . ASP A 1 2891 ? 217.165 204.721 281.467 1.00 43.03  ? 2891 ASP A CG    1 
ATOM   10720 O  OD1   . ASP A 1 2891 ? 217.473 203.783 280.702 1.00 41.41  ? 2891 ASP A OD1   1 
ATOM   10721 O  OD2   . ASP A 1 2891 ? 217.834 205.021 282.479 1.00 40.67  ? 2891 ASP A OD2   1 
ATOM   10722 N  N     . TYR A 1 2892 ? 214.912 207.995 279.453 1.00 26.47  ? 2892 TYR A N     1 
ATOM   10723 C  CA    . TYR A 1 2892 ? 213.908 209.023 279.198 1.00 24.97  ? 2892 TYR A CA    1 
ATOM   10724 C  C     . TYR A 1 2892 ? 213.387 208.936 277.769 1.00 24.80  ? 2892 TYR A C     1 
ATOM   10725 O  O     . TYR A 1 2892 ? 212.179 209.065 277.533 1.00 24.99  ? 2892 TYR A O     1 
ATOM   10726 C  CB    . TYR A 1 2892 ? 214.491 210.407 279.477 1.00 22.40  ? 2892 TYR A CB    1 
ATOM   10727 C  CG    . TYR A 1 2892 ? 213.526 211.538 279.208 1.00 22.45  ? 2892 TYR A CG    1 
ATOM   10728 C  CD1   . TYR A 1 2892 ? 212.553 211.878 280.135 1.00 25.16  ? 2892 TYR A CD1   1 
ATOM   10729 C  CD2   . TYR A 1 2892 ? 213.588 212.263 278.027 1.00 23.13  ? 2892 TYR A CD2   1 
ATOM   10730 C  CE1   . TYR A 1 2892 ? 211.667 212.909 279.895 1.00 25.50  ? 2892 TYR A CE1   1 
ATOM   10731 C  CE2   . TYR A 1 2892 ? 212.705 213.295 277.777 1.00 24.35  ? 2892 TYR A CE2   1 
ATOM   10732 C  CZ    . TYR A 1 2892 ? 211.748 213.613 278.715 1.00 23.73  ? 2892 TYR A CZ    1 
ATOM   10733 O  OH    . TYR A 1 2892 ? 210.867 214.640 278.474 1.00 30.25  ? 2892 TYR A OH    1 
ATOM   10734 N  N     . VAL A 1 2893 ? 214.281 208.708 276.805 1.00 23.51  ? 2893 VAL A N     1 
ATOM   10735 C  CA    . VAL A 1 2893 ? 213.858 208.580 275.416 1.00 24.47  ? 2893 VAL A CA    1 
ATOM   10736 C  C     . VAL A 1 2893 ? 213.007 207.331 275.230 1.00 26.52  ? 2893 VAL A C     1 
ATOM   10737 O  O     . VAL A 1 2893 ? 212.060 207.329 274.444 1.00 31.59  ? 2893 VAL A O     1 
ATOM   10738 C  CB    . VAL A 1 2893 ? 215.078 208.590 274.476 1.00 28.37  ? 2893 VAL A CB    1 
ATOM   10739 C  CG1   . VAL A 1 2893 ? 214.661 208.272 273.050 1.00 24.28  ? 2893 VAL A CG1   1 
ATOM   10740 C  CG2   . VAL A 1 2893 ? 215.763 209.944 274.518 1.00 25.77  ? 2893 VAL A CG2   1 
ATOM   10741 N  N     . LYS A 1 2894 ? 213.319 206.253 275.953 1.00 26.21  ? 2894 LYS A N     1 
ATOM   10742 C  CA    . LYS A 1 2894 ? 212.506 205.044 275.866 1.00 25.13  ? 2894 LYS A CA    1 
ATOM   10743 C  C     . LYS A 1 2894 ? 211.086 205.298 276.365 1.00 24.50  ? 2894 LYS A C     1 
ATOM   10744 O  O     . LYS A 1 2894 ? 210.105 204.888 275.730 1.00 27.77  ? 2894 LYS A O     1 
ATOM   10745 C  CB    . LYS A 1 2894 ? 213.167 203.916 276.661 1.00 27.08  ? 2894 LYS A CB    1 
ATOM   10746 C  CG    . LYS A 1 2894 ? 212.430 202.589 276.599 1.00 32.12  ? 2894 LYS A CG    1 
ATOM   10747 C  CD    . LYS A 1 2894 ? 212.372 202.054 275.179 1.00 34.00  ? 2894 LYS A CD    1 
ATOM   10748 C  CE    . LYS A 1 2894 ? 213.757 201.704 274.663 1.00 30.36  ? 2894 LYS A CE    1 
ATOM   10749 N  NZ    . LYS A 1 2894 ? 214.338 200.536 275.381 1.00 27.21  ? 2894 LYS A NZ    1 
ATOM   10750 N  N     . ALA A 1 2895 ? 210.958 205.982 277.503 1.00 25.95  ? 2895 ALA A N     1 
ATOM   10751 C  CA    . ALA A 1 2895 ? 209.629 206.300 278.025 1.00 25.88  ? 2895 ALA A CA    1 
ATOM   10752 C  C     . ALA A 1 2895 ? 208.869 207.220 277.073 1.00 25.76  ? 2895 ALA A C     1 
ATOM   10753 O  O     . ALA A 1 2895 ? 207.679 207.006 276.785 1.00 28.23  ? 2895 ALA A O     1 
ATOM   10754 C  CB    . ALA A 1 2895 ? 209.748 206.933 279.410 1.00 23.18  ? 2895 ALA A CB    1 
ATOM   10755 N  N     . ARG A 1 2896 ? 209.547 208.253 276.565 1.00 25.39  ? 2896 ARG A N     1 
ATOM   10756 C  CA    . ARG A 1 2896 ? 208.896 209.169 275.637 1.00 26.38  ? 2896 ARG A CA    1 
ATOM   10757 C  C     . ARG A 1 2896 ? 208.528 208.475 274.334 1.00 25.60  ? 2896 ARG A C     1 
ATOM   10758 O  O     . ARG A 1 2896 ? 207.522 208.827 273.719 1.00 23.10  ? 2896 ARG A O     1 
ATOM   10759 C  CB    . ARG A 1 2896 ? 209.790 210.378 275.366 1.00 25.93  ? 2896 ARG A CB    1 
ATOM   10760 C  CG    . ARG A 1 2896 ? 210.078 211.231 276.592 1.00 26.72  ? 2896 ARG A CG    1 
ATOM   10761 C  CD    . ARG A 1 2896 ? 208.851 211.392 277.473 1.00 23.51  ? 2896 ARG A CD    1 
ATOM   10762 N  NE    . ARG A 1 2896 ? 207.829 212.226 276.853 1.00 21.22  ? 2896 ARG A NE    1 
ATOM   10763 C  CZ    . ARG A 1 2896 ? 206.553 212.232 277.211 1.00 25.82  ? 2896 ARG A CZ    1 
ATOM   10764 N  NH1   . ARG A 1 2896 ? 206.103 211.451 278.179 1.00 19.97  ? 2896 ARG A NH1   1 
ATOM   10765 N  NH2   . ARG A 1 2896 ? 205.706 213.042 276.583 1.00 30.49  ? 2896 ARG A NH2   1 
ATOM   10766 N  N     . LEU A 1 2897 ? 209.311 207.482 273.907 1.00 23.83  ? 2897 LEU A N     1 
ATOM   10767 C  CA    . LEU A 1 2897 ? 208.963 206.711 272.720 1.00 22.12  ? 2897 LEU A CA    1 
ATOM   10768 C  C     . LEU A 1 2897 ? 207.768 205.807 272.965 1.00 26.91  ? 2897 LEU A C     1 
ATOM   10769 O  O     . LEU A 1 2897 ? 206.970 205.588 272.053 1.00 27.59  ? 2897 LEU A O     1 
ATOM   10770 C  CB    . LEU A 1 2897 ? 210.156 205.881 272.250 1.00 18.04  ? 2897 LEU A CB    1 
ATOM   10771 C  CG    . LEU A 1 2897 ? 211.184 206.583 271.369 1.00 25.64  ? 2897 LEU A CG    1 
ATOM   10772 C  CD1   . LEU A 1 2897 ? 212.316 205.635 271.046 1.00 25.05  ? 2897 LEU A CD1   1 
ATOM   10773 C  CD2   . LEU A 1 2897 ? 210.524 207.066 270.093 1.00 24.01  ? 2897 LEU A CD2   1 
ATOM   10774 N  N     . LYS A 1 2898 ? 207.634 205.260 274.173 1.00 26.68  ? 2898 LYS A N     1 
ATOM   10775 C  CA    . LYS A 1 2898 ? 206.418 204.522 274.501 1.00 27.27  ? 2898 LYS A CA    1 
ATOM   10776 C  C     . LYS A 1 2898 ? 205.195 205.426 274.392 1.00 25.95  ? 2898 LYS A C     1 
ATOM   10777 O  O     . LYS A 1 2898 ? 204.181 205.064 273.774 1.00 29.61  ? 2898 LYS A O     1 
ATOM   10778 C  CB    . LYS A 1 2898 ? 206.530 203.928 275.903 1.00 27.18  ? 2898 LYS A CB    1 
ATOM   10779 C  CG    . LYS A 1 2898 ? 205.337 203.088 276.313 1.00 32.22  ? 2898 LYS A CG    1 
ATOM   10780 C  CD    . LYS A 1 2898 ? 205.338 202.826 277.806 1.00 33.65  ? 2898 LYS A CD    1 
ATOM   10781 C  CE    . LYS A 1 2898 ? 203.933 202.916 278.373 1.00 35.77  ? 2898 LYS A CE    1 
ATOM   10782 N  NZ    . LYS A 1 2898 ? 203.402 204.305 278.295 1.00 32.25  ? 2898 LYS A NZ    1 
ATOM   10783 N  N     . VAL A 1 2899 ? 205.286 206.626 274.969 1.00 27.80  ? 2899 VAL A N     1 
ATOM   10784 C  CA    . VAL A 1 2899 ? 204.176 207.575 274.869 1.00 28.28  ? 2899 VAL A CA    1 
ATOM   10785 C  C     . VAL A 1 2899 ? 203.943 207.975 273.414 1.00 27.99  ? 2899 VAL A C     1 
ATOM   10786 O  O     . VAL A 1 2899 ? 202.800 208.162 272.980 1.00 28.26  ? 2899 VAL A O     1 
ATOM   10787 C  CB    . VAL A 1 2899 ? 204.436 208.801 275.763 1.00 28.88  ? 2899 VAL A CB    1 
ATOM   10788 C  CG1   . VAL A 1 2899 ? 203.233 209.730 275.752 1.00 24.80  ? 2899 VAL A CG1   1 
ATOM   10789 C  CG2   . VAL A 1 2899 ? 204.760 208.359 277.180 1.00 24.55  ? 2899 VAL A CG2   1 
ATOM   10790 N  N     . PHE A 1 2900 ? 205.025 208.112 272.645 1.00 29.78  ? 2900 PHE A N     1 
ATOM   10791 C  CA    . PHE A 1 2900 ? 204.931 208.464 271.232 1.00 21.52  ? 2900 PHE A CA    1 
ATOM   10792 C  C     . PHE A 1 2900 ? 204.211 207.381 270.440 1.00 25.20  ? 2900 PHE A C     1 
ATOM   10793 O  O     . PHE A 1 2900 ? 203.379 207.680 269.579 1.00 27.70  ? 2900 PHE A O     1 
ATOM   10794 C  CB    . PHE A 1 2900 ? 206.342 208.699 270.688 1.00 19.95  ? 2900 PHE A CB    1 
ATOM   10795 C  CG    . PHE A 1 2900 ? 206.392 209.154 269.258 1.00 18.42  ? 2900 PHE A CG    1 
ATOM   10796 C  CD1   . PHE A 1 2900 ? 205.916 210.400 268.895 1.00 13.85  ? 2900 PHE A CD1   1 
ATOM   10797 C  CD2   . PHE A 1 2900 ? 206.945 208.342 268.281 1.00 20.29  ? 2900 PHE A CD2   1 
ATOM   10798 C  CE1   . PHE A 1 2900 ? 205.979 210.822 267.582 1.00 13.91  ? 2900 PHE A CE1   1 
ATOM   10799 C  CE2   . PHE A 1 2900 ? 207.004 208.759 266.966 1.00 15.11  ? 2900 PHE A CE2   1 
ATOM   10800 C  CZ    . PHE A 1 2900 ? 206.520 209.998 266.617 1.00 13.14  ? 2900 PHE A CZ    1 
ATOM   10801 N  N     . TYR A 1 2901 ? 204.523 206.113 270.717 1.00 29.74  ? 2901 TYR A N     1 
ATOM   10802 C  CA    . TYR A 1 2901 ? 203.819 205.010 270.075 1.00 24.96  ? 2901 TYR A CA    1 
ATOM   10803 C  C     . TYR A 1 2901 ? 202.342 205.035 270.426 1.00 28.58  ? 2901 TYR A C     1 
ATOM   10804 O  O     . TYR A 1 2901 ? 201.484 204.831 269.559 1.00 34.89  ? 2901 TYR A O     1 
ATOM   10805 C  CB    . TYR A 1 2901 ? 204.425 203.670 270.493 1.00 26.18  ? 2901 TYR A CB    1 
ATOM   10806 C  CG    . TYR A 1 2901 ? 205.899 203.509 270.202 1.00 23.63  ? 2901 TYR A CG    1 
ATOM   10807 C  CD1   . TYR A 1 2901 ? 206.509 204.208 269.171 1.00 25.92  ? 2901 TYR A CD1   1 
ATOM   10808 C  CD2   . TYR A 1 2901 ? 206.681 202.655 270.966 1.00 22.05  ? 2901 TYR A CD2   1 
ATOM   10809 C  CE1   . TYR A 1 2901 ? 207.857 204.059 268.910 1.00 28.82  ? 2901 TYR A CE1   1 
ATOM   10810 C  CE2   . TYR A 1 2901 ? 208.027 202.501 270.714 1.00 24.05  ? 2901 TYR A CE2   1 
ATOM   10811 C  CZ    . TYR A 1 2901 ? 208.610 203.203 269.685 1.00 25.80  ? 2901 TYR A CZ    1 
ATOM   10812 O  OH    . TYR A 1 2901 ? 209.953 203.051 269.432 1.00 29.24  ? 2901 TYR A OH    1 
ATOM   10813 N  N     . GLU A 1 2902 ? 202.024 205.282 271.700 1.00 33.87  ? 2902 GLU A N     1 
ATOM   10814 C  CA    . GLU A 1 2902 ? 200.624 205.302 272.113 1.00 28.40  ? 2902 GLU A CA    1 
ATOM   10815 C  C     . GLU A 1 2902 ? 199.857 206.441 271.447 1.00 28.52  ? 2902 GLU A C     1 
ATOM   10816 O  O     . GLU A 1 2902 ? 198.716 206.255 271.007 1.00 36.17  ? 2902 GLU A O     1 
ATOM   10817 C  CB    . GLU A 1 2902 ? 200.526 205.406 273.633 1.00 35.86  ? 2902 GLU A CB    1 
ATOM   10818 C  CG    . GLU A 1 2902 ? 201.032 204.177 274.367 1.00 37.79  ? 2902 GLU A CG    1 
ATOM   10819 C  CD    . GLU A 1 2902 ? 200.983 204.340 275.872 1.00 45.45  ? 2902 GLU A CD    1 
ATOM   10820 O  OE1   . GLU A 1 2902 ? 200.655 205.450 276.341 1.00 47.36  ? 2902 GLU A OE1   1 
ATOM   10821 O  OE2   . GLU A 1 2902 ? 201.266 203.355 276.585 1.00 44.86  ? 2902 GLU A OE2   1 
ATOM   10822 N  N     . GLU A 1 2903 ? 200.467 207.623 271.355 1.00 32.12  ? 2903 GLU A N     1 
ATOM   10823 C  CA    . GLU A 1 2903 ? 199.769 208.815 270.883 1.00 36.53  ? 2903 GLU A CA    1 
ATOM   10824 C  C     . GLU A 1 2903 ? 199.995 209.094 269.403 1.00 35.04  ? 2903 GLU A C     1 
ATOM   10825 O  O     . GLU A 1 2903 ? 199.094 209.591 268.720 1.00 37.36  ? 2903 GLU A O     1 
ATOM   10826 C  CB    . GLU A 1 2903 ? 200.208 210.033 271.700 1.00 35.14  ? 2903 GLU A CB    1 
ATOM   10827 C  CG    . GLU A 1 2903 ? 199.960 209.912 273.192 1.00 42.26  ? 2903 GLU A CG    1 
ATOM   10828 C  CD    . GLU A 1 2903 ? 199.579 211.237 273.820 1.00 58.88  ? 2903 GLU A CD    1 
ATOM   10829 O  OE1   . GLU A 1 2903 ? 200.297 212.232 273.588 1.00 49.29  ? 2903 GLU A OE1   1 
ATOM   10830 O  OE2   . GLU A 1 2903 ? 198.563 211.285 274.543 1.00 64.64  ? 2903 GLU A OE2   1 
ATOM   10831 N  N     . GLU A 1 2904 ? 201.183 208.789 268.896 1.00 35.07  ? 2904 GLU A N     1 
ATOM   10832 C  CA    . GLU A 1 2904 ? 201.567 209.119 267.530 1.00 32.85  ? 2904 GLU A CA    1 
ATOM   10833 C  C     . GLU A 1 2904 ? 202.046 207.836 266.856 1.00 32.98  ? 2904 GLU A C     1 
ATOM   10834 O  O     . GLU A 1 2904 ? 201.772 206.725 267.325 1.00 41.92  ? 2904 GLU A O     1 
ATOM   10835 C  CB    . GLU A 1 2904 ? 202.628 210.226 267.506 1.00 34.05  ? 2904 GLU A CB    1 
ATOM   10836 C  CG    . GLU A 1 2904 ? 202.215 211.516 268.188 1.00 34.96  ? 2904 GLU A CG    1 
ATOM   10837 C  CD    . GLU A 1 2904 ? 201.318 212.372 267.320 1.00 41.25  ? 2904 GLU A CD    1 
ATOM   10838 O  OE1   . GLU A 1 2904 ? 201.738 212.724 266.198 1.00 38.36  ? 2904 GLU A OE1   1 
ATOM   10839 O  OE2   . GLU A 1 2904 ? 200.197 212.698 267.760 1.00 49.36  ? 2904 GLU A OE2   1 
ATOM   10840 N  N     . LEU A 1 2905 ? 202.734 207.999 265.725 1.00 29.21  ? 2905 LEU A N     1 
ATOM   10841 C  CA    . LEU A 1 2905 ? 203.244 206.904 264.906 1.00 31.95  ? 2905 LEU A CA    1 
ATOM   10842 C  C     . LEU A 1 2905 ? 203.744 205.739 265.752 1.00 33.21  ? 2905 LEU A C     1 
ATOM   10843 O  O     . LEU A 1 2905 ? 204.562 205.917 266.657 1.00 28.87  ? 2905 LEU A O     1 
ATOM   10844 C  CB    . LEU A 1 2905 ? 204.377 207.427 264.023 1.00 30.52  ? 2905 LEU A CB    1 
ATOM   10845 C  CG    . LEU A 1 2905 ? 204.557 206.747 262.674 1.00 28.96  ? 2905 LEU A CG    1 
ATOM   10846 C  CD1   . LEU A 1 2905 ? 203.320 207.009 261.844 1.00 34.45  ? 2905 LEU A CD1   1 
ATOM   10847 C  CD2   . LEU A 1 2905 ? 205.800 207.271 261.977 1.00 26.44  ? 2905 LEU A CD2   1 
ATOM   10848 N  N     . ASP A 1 2906 ? 203.245 204.542 265.443 1.00 32.33  ? 2906 ASP A N     1 
ATOM   10849 C  CA    . ASP A 1 2906 ? 203.476 203.356 266.255 1.00 29.90  ? 2906 ASP A CA    1 
ATOM   10850 C  C     . ASP A 1 2906 ? 204.500 202.424 265.608 1.00 32.87  ? 2906 ASP A C     1 
ATOM   10851 O  O     . ASP A 1 2906 ? 204.311 201.204 265.597 1.00 37.22  ? 2906 ASP A O     1 
ATOM   10852 C  CB    . ASP A 1 2906 ? 202.144 202.633 266.501 1.00 35.27  ? 2906 ASP A CB    1 
ATOM   10853 C  CG    . ASP A 1 2906 ? 202.210 201.602 267.633 1.00 38.78  ? 2906 ASP A CG    1 
ATOM   10854 O  OD1   . ASP A 1 2906 ? 203.276 201.012 267.900 1.00 30.91  ? 2906 ASP A OD1   1 
ATOM   10855 O  OD2   . ASP A 1 2906 ? 201.159 201.381 268.269 1.00 50.67  ? 2906 ASP A OD2   1 
ATOM   10856 N  N     . VAL A 1 2907 ? 205.548 202.977 265.010 1.00 32.32  ? 2907 VAL A N     1 
ATOM   10857 C  CA    . VAL A 1 2907 ? 206.627 202.154 264.472 1.00 29.66  ? 2907 VAL A CA    1 
ATOM   10858 C  C     . VAL A 1 2907 ? 207.672 201.966 265.567 1.00 31.64  ? 2907 VAL A C     1 
ATOM   10859 O  O     . VAL A 1 2907 ? 208.230 202.948 266.076 1.00 33.54  ? 2907 VAL A O     1 
ATOM   10860 C  CB    . VAL A 1 2907 ? 207.213 202.762 263.184 1.00 29.47  ? 2907 VAL A CB    1 
ATOM   10861 C  CG1   . VAL A 1 2907 ? 206.142 202.828 262.110 1.00 33.57  ? 2907 VAL A CG1   1 
ATOM   10862 C  CG2   . VAL A 1 2907 ? 207.761 204.161 263.424 1.00 28.12  ? 2907 VAL A CG2   1 
ATOM   10863 N  N     . PRO A 1 2908 ? 207.929 200.733 265.999 1.00 31.14  ? 2908 PRO A N     1 
ATOM   10864 C  CA    . PRO A 1 2908 ? 208.926 200.517 267.051 1.00 25.07  ? 2908 PRO A CA    1 
ATOM   10865 C  C     . PRO A 1 2908 ? 210.318 200.899 266.579 1.00 26.85  ? 2908 PRO A C     1 
ATOM   10866 O  O     . PRO A 1 2908 ? 210.676 200.725 265.411 1.00 32.95  ? 2908 PRO A O     1 
ATOM   10867 C  CB    . PRO A 1 2908 ? 208.827 199.016 267.341 1.00 28.66  ? 2908 PRO A CB    1 
ATOM   10868 C  CG    . PRO A 1 2908 ? 207.530 198.578 266.725 1.00 33.65  ? 2908 PRO A CG    1 
ATOM   10869 C  CD    . PRO A 1 2908 ? 207.316 199.473 265.554 1.00 31.61  ? 2908 PRO A CD    1 
ATOM   10870 N  N     . LEU A 1 2909 ? 211.110 201.424 267.508 1.00 20.93  ? 2909 LEU A N     1 
ATOM   10871 C  CA    . LEU A 1 2909 ? 212.454 201.890 267.211 1.00 19.65  ? 2909 LEU A CA    1 
ATOM   10872 C  C     . LEU A 1 2909 ? 213.449 201.242 268.158 1.00 25.45  ? 2909 LEU A C     1 
ATOM   10873 O  O     . LEU A 1 2909 ? 213.138 200.956 269.317 1.00 31.41  ? 2909 LEU A O     1 
ATOM   10874 C  CB    . LEU A 1 2909 ? 212.560 203.418 267.320 1.00 19.51  ? 2909 LEU A CB    1 
ATOM   10875 C  CG    . LEU A 1 2909 ? 211.574 204.250 266.499 1.00 18.94  ? 2909 LEU A CG    1 
ATOM   10876 C  CD1   . LEU A 1 2909 ? 211.855 205.731 266.688 1.00 24.62  ? 2909 LEU A CD1   1 
ATOM   10877 C  CD2   . LEU A 1 2909 ? 211.638 203.874 265.031 1.00 16.35  ? 2909 LEU A CD2   1 
ATOM   10878 N  N     . VAL A 1 2910 ? 214.655 201.013 267.649 1.00 24.09  ? 2910 VAL A N     1 
ATOM   10879 C  CA    . VAL A 1 2910 ? 215.760 200.486 268.439 1.00 22.67  ? 2910 VAL A CA    1 
ATOM   10880 C  C     . VAL A 1 2910 ? 216.667 201.653 268.799 1.00 23.51  ? 2910 VAL A C     1 
ATOM   10881 O  O     . VAL A 1 2910 ? 217.120 202.393 267.917 1.00 22.49  ? 2910 VAL A O     1 
ATOM   10882 C  CB    . VAL A 1 2910 ? 216.532 199.399 267.676 1.00 15.58  ? 2910 VAL A CB    1 
ATOM   10883 C  CG1   . VAL A 1 2910 ? 217.672 198.868 268.525 1.00 14.97  ? 2910 VAL A CG1   1 
ATOM   10884 C  CG2   . VAL A 1 2910 ? 215.596 198.275 267.263 1.00 17.25  ? 2910 VAL A CG2   1 
ATOM   10885 N  N     . LEU A 1 2911 ? 216.928 201.823 270.090 1.00 18.99  ? 2911 LEU A N     1 
ATOM   10886 C  CA    . LEU A 1 2911 ? 217.743 202.927 270.570 1.00 18.80  ? 2911 LEU A CA    1 
ATOM   10887 C  C     . LEU A 1 2911 ? 219.206 202.515 270.644 1.00 28.31  ? 2911 LEU A C     1 
ATOM   10888 O  O     . LEU A 1 2911 ? 219.552 201.543 271.321 1.00 42.02  ? 2911 LEU A O     1 
ATOM   10889 C  CB    . LEU A 1 2911 ? 217.265 203.398 271.942 1.00 21.46  ? 2911 LEU A CB    1 
ATOM   10890 C  CG    . LEU A 1 2911 ? 215.921 204.118 271.987 1.00 23.60  ? 2911 LEU A CG    1 
ATOM   10891 C  CD1   . LEU A 1 2911 ? 215.718 204.762 273.343 1.00 23.51  ? 2911 LEU A CD1   1 
ATOM   10892 C  CD2   . LEU A 1 2911 ? 215.860 205.159 270.885 1.00 24.81  ? 2911 LEU A CD2   1 
ATOM   10893 N  N     . PHE A 1 2912 ? 220.056 203.255 269.939 1.00 21.24  ? 2912 PHE A N     1 
ATOM   10894 C  CA    . PHE A 1 2912 ? 221.498 203.176 270.100 1.00 19.99  ? 2912 PHE A CA    1 
ATOM   10895 C  C     . PHE A 1 2912 ? 222.029 204.591 270.303 1.00 18.43  ? 2912 PHE A C     1 
ATOM   10896 O  O     . PHE A 1 2912 ? 221.271 205.564 270.312 1.00 23.06  ? 2912 PHE A O     1 
ATOM   10897 C  CB    . PHE A 1 2912 ? 222.177 202.475 268.912 1.00 16.08  ? 2912 PHE A CB    1 
ATOM   10898 C  CG    . PHE A 1 2912 ? 221.635 202.866 267.563 1.00 15.42  ? 2912 PHE A CG    1 
ATOM   10899 C  CD1   . PHE A 1 2912 ? 220.475 202.294 267.070 1.00 14.11  ? 2912 PHE A CD1   1 
ATOM   10900 C  CD2   . PHE A 1 2912 ? 222.302 203.788 266.777 1.00 15.96  ? 2912 PHE A CD2   1 
ATOM   10901 C  CE1   . PHE A 1 2912 ? 219.986 202.647 265.826 1.00 14.10  ? 2912 PHE A CE1   1 
ATOM   10902 C  CE2   . PHE A 1 2912 ? 221.816 204.144 265.534 1.00 11.01  ? 2912 PHE A CE2   1 
ATOM   10903 C  CZ    . PHE A 1 2912 ? 220.659 203.571 265.058 1.00 9.76   ? 2912 PHE A CZ    1 
ATOM   10904 N  N     . ASN A 1 2913 ? 223.348 204.700 270.477 1.00 16.42  ? 2913 ASN A N     1 
ATOM   10905 C  CA    . ASN A 1 2913 ? 223.942 205.982 270.842 1.00 19.80  ? 2913 ASN A CA    1 
ATOM   10906 C  C     . ASN A 1 2913 ? 223.722 207.032 269.758 1.00 24.29  ? 2913 ASN A C     1 
ATOM   10907 O  O     . ASN A 1 2913 ? 223.467 208.207 270.060 1.00 26.81  ? 2913 ASN A O     1 
ATOM   10908 C  CB    . ASN A 1 2913 ? 225.432 205.798 271.126 1.00 23.59  ? 2913 ASN A CB    1 
ATOM   10909 C  CG    . ASN A 1 2913 ? 225.697 204.711 272.148 1.00 21.52  ? 2913 ASN A CG    1 
ATOM   10910 O  OD1   . ASN A 1 2913 ? 224.767 204.114 272.690 1.00 14.67  ? 2913 ASN A OD1   1 
ATOM   10911 N  ND2   . ASN A 1 2913 ? 226.969 204.447 272.416 1.00 23.81  ? 2913 ASN A ND2   1 
ATOM   10912 N  N     . GLU A 1 2914 ? 223.814 206.628 268.490 1.00 19.53  ? 2914 GLU A N     1 
ATOM   10913 C  CA    . GLU A 1 2914 ? 223.636 207.577 267.396 1.00 17.82  ? 2914 GLU A CA    1 
ATOM   10914 C  C     . GLU A 1 2914 ? 222.228 208.159 267.391 1.00 18.41  ? 2914 GLU A C     1 
ATOM   10915 O  O     . GLU A 1 2914 ? 222.039 209.334 267.061 1.00 22.20  ? 2914 GLU A O     1 
ATOM   10916 C  CB    . GLU A 1 2914 ? 223.951 206.904 266.062 1.00 19.21  ? 2914 GLU A CB    1 
ATOM   10917 C  CG    . GLU A 1 2914 ? 225.401 206.475 265.918 1.00 23.69  ? 2914 GLU A CG    1 
ATOM   10918 C  CD    . GLU A 1 2914 ? 225.849 206.401 264.472 1.00 35.07  ? 2914 GLU A CD    1 
ATOM   10919 O  OE1   . GLU A 1 2914 ? 225.008 206.089 263.600 1.00 33.90  ? 2914 GLU A OE1   1 
ATOM   10920 O  OE2   . GLU A 1 2914 ? 227.043 206.651 264.206 1.00 32.20  ? 2914 GLU A OE2   1 
ATOM   10921 N  N     . VAL A 1 2915 ? 221.225 207.354 267.754 1.00 15.65  ? 2915 VAL A N     1 
ATOM   10922 C  CA    . VAL A 1 2915 ? 219.860 207.869 267.839 1.00 16.18  ? 2915 VAL A CA    1 
ATOM   10923 C  C     . VAL A 1 2915 ? 219.766 208.961 268.894 1.00 14.45  ? 2915 VAL A C     1 
ATOM   10924 O  O     . VAL A 1 2915 ? 219.140 210.005 268.675 1.00 15.19  ? 2915 VAL A O     1 
ATOM   10925 C  CB    . VAL A 1 2915 ? 218.867 206.727 268.126 1.00 15.05  ? 2915 VAL A CB    1 
ATOM   10926 C  CG1   . VAL A 1 2915 ? 217.472 207.286 268.337 1.00 16.10  ? 2915 VAL A CG1   1 
ATOM   10927 C  CG2   . VAL A 1 2915 ? 218.857 205.746 266.985 1.00 13.57  ? 2915 VAL A CG2   1 
ATOM   10928 N  N     . LEU A 1 2916 ? 220.373 208.732 270.061 1.00 13.75  ? 2916 LEU A N     1 
ATOM   10929 C  CA    . LEU A 1 2916 ? 220.344 209.739 271.115 1.00 15.65  ? 2916 LEU A CA    1 
ATOM   10930 C  C     . LEU A 1 2916 ? 221.047 211.015 270.672 1.00 15.82  ? 2916 LEU A C     1 
ATOM   10931 O  O     . LEU A 1 2916 ? 220.538 212.123 270.891 1.00 14.36  ? 2916 LEU A O     1 
ATOM   10932 C  CB    . LEU A 1 2916 ? 220.982 209.179 272.385 1.00 20.64  ? 2916 LEU A CB    1 
ATOM   10933 C  CG    . LEU A 1 2916 ? 220.363 207.886 272.920 1.00 16.52  ? 2916 LEU A CG    1 
ATOM   10934 C  CD1   . LEU A 1 2916 ? 221.017 207.470 274.226 1.00 17.07  ? 2916 LEU A CD1   1 
ATOM   10935 C  CD2   . LEU A 1 2916 ? 218.863 208.047 273.101 1.00 15.51  ? 2916 LEU A CD2   1 
ATOM   10936 N  N     . ASP A 1 2917 ? 222.207 210.881 270.026 1.00 19.74  ? 2917 ASP A N     1 
ATOM   10937 C  CA    . ASP A 1 2917 ? 222.912 212.062 269.538 1.00 15.53  ? 2917 ASP A CA    1 
ATOM   10938 C  C     . ASP A 1 2917 ? 222.073 212.824 268.517 1.00 16.07  ? 2917 ASP A C     1 
ATOM   10939 O  O     . ASP A 1 2917 ? 221.983 214.058 268.571 1.00 27.15  ? 2917 ASP A O     1 
ATOM   10940 C  CB    . ASP A 1 2917 ? 224.255 211.658 268.933 1.00 17.53  ? 2917 ASP A CB    1 
ATOM   10941 C  CG    . ASP A 1 2917 ? 225.073 210.787 269.862 1.00 33.55  ? 2917 ASP A CG    1 
ATOM   10942 O  OD1   . ASP A 1 2917 ? 224.729 210.711 271.060 1.00 39.42  ? 2917 ASP A OD1   1 
ATOM   10943 O  OD2   . ASP A 1 2917 ? 226.059 210.177 269.397 1.00 38.14  ? 2917 ASP A OD2   1 
ATOM   10944 N  N     . HIS A 1 2918 ? 221.439 212.105 267.591 1.00 12.69  ? 2918 HIS A N     1 
ATOM   10945 C  CA    . HIS A 1 2918 ? 220.654 212.760 266.551 1.00 13.17  ? 2918 HIS A CA    1 
ATOM   10946 C  C     . HIS A 1 2918 ? 219.429 213.459 267.127 1.00 14.21  ? 2918 HIS A C     1 
ATOM   10947 O  O     . HIS A 1 2918 ? 219.103 214.579 266.718 1.00 24.85  ? 2918 HIS A O     1 
ATOM   10948 C  CB    . HIS A 1 2918 ? 220.245 211.743 265.487 1.00 16.95  ? 2918 HIS A CB    1 
ATOM   10949 C  CG    . HIS A 1 2918 ? 221.398 211.195 264.704 1.00 17.20  ? 2918 HIS A CG    1 
ATOM   10950 N  ND1   . HIS A 1 2918 ? 221.305 210.052 263.941 1.00 15.48  ? 2918 HIS A ND1   1 
ATOM   10951 C  CD2   . HIS A 1 2918 ? 222.673 211.633 264.572 1.00 16.42  ? 2918 HIS A CD2   1 
ATOM   10952 C  CE1   . HIS A 1 2918 ? 222.470 209.811 263.369 1.00 22.03  ? 2918 HIS A CE1   1 
ATOM   10953 N  NE2   . HIS A 1 2918 ? 223.318 210.755 263.736 1.00 19.71  ? 2918 HIS A NE2   1 
ATOM   10954 N  N     . VAL A 1 2919 ? 218.728 212.816 268.064 1.00 13.59  ? 2919 VAL A N     1 
ATOM   10955 C  CA    . VAL A 1 2919 ? 217.556 213.460 268.646 1.00 12.47  ? 2919 VAL A CA    1 
ATOM   10956 C  C     . VAL A 1 2919 ? 217.972 214.671 269.470 1.00 10.86  ? 2919 VAL A C     1 
ATOM   10957 O  O     . VAL A 1 2919 ? 217.265 215.684 269.500 1.00 12.93  ? 2919 VAL A O     1 
ATOM   10958 C  CB    . VAL A 1 2919 ? 216.710 212.461 269.463 1.00 13.10  ? 2919 VAL A CB    1 
ATOM   10959 C  CG1   . VAL A 1 2919 ? 216.252 211.308 268.585 1.00 12.07  ? 2919 VAL A CG1   1 
ATOM   10960 C  CG2   . VAL A 1 2919 ? 217.457 211.952 270.679 1.00 10.26  ? 2919 VAL A CG2   1 
ATOM   10961 N  N     . LEU A 1 2920 ? 219.131 214.602 270.134 1.00 10.45  ? 2920 LEU A N     1 
ATOM   10962 C  CA    . LEU A 1 2920 ? 219.629 215.774 270.847 1.00 9.68   ? 2920 LEU A CA    1 
ATOM   10963 C  C     . LEU A 1 2920 ? 219.927 216.920 269.887 1.00 12.29  ? 2920 LEU A C     1 
ATOM   10964 O  O     . LEU A 1 2920 ? 219.590 218.076 270.167 1.00 12.22  ? 2920 LEU A O     1 
ATOM   10965 C  CB    . LEU A 1 2920 ? 220.872 215.410 271.656 1.00 8.74   ? 2920 LEU A CB    1 
ATOM   10966 C  CG    . LEU A 1 2920 ? 220.620 214.636 272.949 1.00 9.16   ? 2920 LEU A CG    1 
ATOM   10967 C  CD1   . LEU A 1 2920 ? 221.862 214.626 273.819 1.00 10.71  ? 2920 LEU A CD1   1 
ATOM   10968 C  CD2   . LEU A 1 2920 ? 219.437 215.217 273.702 1.00 9.26   ? 2920 LEU A CD2   1 
ATOM   10969 N  N     . ARG A 1 2921 ? 220.551 216.620 268.744 1.00 11.23  ? 2921 ARG A N     1 
ATOM   10970 C  CA    . ARG A 1 2921 ? 220.833 217.664 267.762 1.00 11.61  ? 2921 ARG A CA    1 
ATOM   10971 C  C     . ARG A 1 2921 ? 219.549 218.277 267.212 1.00 15.02  ? 2921 ARG A C     1 
ATOM   10972 O  O     . ARG A 1 2921 ? 219.446 219.504 267.057 1.00 22.78  ? 2921 ARG A O     1 
ATOM   10973 C  CB    . ARG A 1 2921 ? 221.683 217.095 266.626 1.00 12.18  ? 2921 ARG A CB    1 
ATOM   10974 C  CG    . ARG A 1 2921 ? 223.049 216.600 267.062 1.00 13.52  ? 2921 ARG A CG    1 
ATOM   10975 C  CD    . ARG A 1 2921 ? 223.791 215.938 265.918 1.00 12.83  ? 2921 ARG A CD    1 
ATOM   10976 N  NE    . ARG A 1 2921 ? 224.790 214.993 266.398 1.00 14.62  ? 2921 ARG A NE    1 
ATOM   10977 C  CZ    . ARG A 1 2921 ? 225.547 214.240 265.612 1.00 21.02  ? 2921 ARG A CZ    1 
ATOM   10978 N  NH1   . ARG A 1 2921 ? 225.446 214.299 264.295 1.00 19.91  ? 2921 ARG A NH1   1 
ATOM   10979 N  NH2   . ARG A 1 2921 ? 226.427 213.408 266.162 1.00 18.95  ? 2921 ARG A NH2   1 
ATOM   10980 N  N     . ILE A 1 2922 ? 218.556 217.439 266.912 1.00 9.15   ? 2922 ILE A N     1 
ATOM   10981 C  CA    . ILE A 1 2922 ? 217.303 217.946 266.365 1.00 10.60  ? 2922 ILE A CA    1 
ATOM   10982 C  C     . ILE A 1 2922 ? 216.570 218.791 267.402 1.00 12.93  ? 2922 ILE A C     1 
ATOM   10983 O  O     . ILE A 1 2922 ? 215.969 219.822 267.072 1.00 13.80  ? 2922 ILE A O     1 
ATOM   10984 C  CB    . ILE A 1 2922 ? 216.439 216.779 265.853 1.00 14.17  ? 2922 ILE A CB    1 
ATOM   10985 C  CG1   . ILE A 1 2922 ? 217.149 216.059 264.707 1.00 11.46  ? 2922 ILE A CG1   1 
ATOM   10986 C  CG2   . ILE A 1 2922 ? 215.102 217.283 265.362 1.00 10.98  ? 2922 ILE A CG2   1 
ATOM   10987 C  CD1   . ILE A 1 2922 ? 216.456 214.794 264.262 1.00 9.39   ? 2922 ILE A CD1   1 
ATOM   10988 N  N     . ASP A 1 2923 ? 216.612 218.375 268.672 1.00 13.16  ? 2923 ASP A N     1 
ATOM   10989 C  CA    . ASP A 1 2923 ? 216.020 219.179 269.738 1.00 13.08  ? 2923 ASP A CA    1 
ATOM   10990 C  C     . ASP A 1 2923 ? 216.746 220.507 269.891 1.00 15.40  ? 2923 ASP A C     1 
ATOM   10991 O  O     . ASP A 1 2923 ? 216.124 221.534 270.185 1.00 18.37  ? 2923 ASP A O     1 
ATOM   10992 C  CB    . ASP A 1 2923 ? 216.042 218.399 271.051 1.00 13.97  ? 2923 ASP A CB    1 
ATOM   10993 C  CG    . ASP A 1 2923 ? 215.491 219.199 272.213 1.00 22.47  ? 2923 ASP A CG    1 
ATOM   10994 O  OD1   . ASP A 1 2923 ? 214.392 219.771 272.077 1.00 24.93  ? 2923 ASP A OD1   1 
ATOM   10995 O  OD2   . ASP A 1 2923 ? 216.160 219.256 273.267 1.00 23.13  ? 2923 ASP A OD2   1 
ATOM   10996 N  N     . ARG A 1 2924 ? 218.068 220.502 269.711 1.00 15.87  ? 2924 ARG A N     1 
ATOM   10997 C  CA    . ARG A 1 2924 ? 218.830 221.744 269.722 1.00 12.50  ? 2924 ARG A CA    1 
ATOM   10998 C  C     . ARG A 1 2924 ? 218.343 222.688 268.633 1.00 14.28  ? 2924 ARG A C     1 
ATOM   10999 O  O     . ARG A 1 2924 ? 218.153 223.887 268.868 1.00 18.11  ? 2924 ARG A O     1 
ATOM   11000 C  CB    . ARG A 1 2924 ? 220.317 221.441 269.534 1.00 12.39  ? 2924 ARG A CB    1 
ATOM   11001 C  CG    . ARG A 1 2924 ? 221.081 221.206 270.813 1.00 19.24  ? 2924 ARG A CG    1 
ATOM   11002 C  CD    . ARG A 1 2924 ? 222.567 221.094 270.536 1.00 18.48  ? 2924 ARG A CD    1 
ATOM   11003 N  NE    . ARG A 1 2924 ? 222.989 221.967 269.449 1.00 14.86  ? 2924 ARG A NE    1 
ATOM   11004 C  CZ    . ARG A 1 2924 ? 223.677 223.088 269.613 1.00 19.46  ? 2924 ARG A CZ    1 
ATOM   11005 N  NH1   . ARG A 1 2924 ? 224.031 223.511 270.816 1.00 17.27  ? 2924 ARG A NH1   1 
ATOM   11006 N  NH2   . ARG A 1 2924 ? 224.021 223.801 268.545 1.00 23.52  ? 2924 ARG A NH2   1 
ATOM   11007 N  N     . ILE A 1 2925 ? 218.136 222.159 267.428 1.00 16.13  ? 2925 ILE A N     1 
ATOM   11008 C  CA    . ILE A 1 2925 ? 217.758 223.019 266.309 1.00 16.05  ? 2925 ILE A CA    1 
ATOM   11009 C  C     . ILE A 1 2925 ? 216.329 223.535 266.465 1.00 13.27  ? 2925 ILE A C     1 
ATOM   11010 O  O     . ILE A 1 2925 ? 216.056 224.714 266.208 1.00 17.41  ? 2925 ILE A O     1 
ATOM   11011 C  CB    . ILE A 1 2925 ? 217.962 222.288 264.972 1.00 17.41  ? 2925 ILE A CB    1 
ATOM   11012 C  CG1   . ILE A 1 2925 ? 219.415 221.833 264.845 1.00 17.37  ? 2925 ILE A CG1   1 
ATOM   11013 C  CG2   . ILE A 1 2925 ? 217.593 223.197 263.813 1.00 11.12  ? 2925 ILE A CG2   1 
ATOM   11014 C  CD1   . ILE A 1 2925 ? 220.428 222.915 265.149 1.00 16.60  ? 2925 ILE A CD1   1 
ATOM   11015 N  N     . PHE A 1 2926 ? 215.394 222.676 266.888 1.00 13.94  ? 2926 PHE A N     1 
ATOM   11016 C  CA    . PHE A 1 2926 ? 214.005 223.111 267.030 1.00 14.84  ? 2926 PHE A CA    1 
ATOM   11017 C  C     . PHE A 1 2926 ? 213.812 224.169 268.109 1.00 19.82  ? 2926 PHE A C     1 
ATOM   11018 O  O     . PHE A 1 2926 ? 212.765 224.824 268.130 1.00 19.05  ? 2926 PHE A O     1 
ATOM   11019 C  CB    . PHE A 1 2926 ? 213.080 221.930 267.335 1.00 15.62  ? 2926 PHE A CB    1 
ATOM   11020 C  CG    . PHE A 1 2926 ? 212.862 221.006 266.174 1.00 14.32  ? 2926 PHE A CG    1 
ATOM   11021 C  CD1   . PHE A 1 2926 ? 213.205 221.389 264.890 1.00 17.21  ? 2926 PHE A CD1   1 
ATOM   11022 C  CD2   . PHE A 1 2926 ? 212.280 219.765 266.365 1.00 11.43  ? 2926 PHE A CD2   1 
ATOM   11023 C  CE1   . PHE A 1 2926 ? 212.992 220.542 263.822 1.00 18.29  ? 2926 PHE A CE1   1 
ATOM   11024 C  CE2   . PHE A 1 2926 ? 212.062 218.918 265.300 1.00 9.90   ? 2926 PHE A CE2   1 
ATOM   11025 C  CZ    . PHE A 1 2926 ? 212.419 219.305 264.028 1.00 11.73  ? 2926 PHE A CZ    1 
ATOM   11026 N  N     . ARG A 1 2927 ? 214.783 224.351 269.002 1.00 23.37  ? 2927 ARG A N     1 
ATOM   11027 C  CA    . ARG A 1 2927 ? 214.664 225.301 270.100 1.00 17.65  ? 2927 ARG A CA    1 
ATOM   11028 C  C     . ARG A 1 2927 ? 215.230 226.676 269.737 1.00 17.68  ? 2927 ARG A C     1 
ATOM   11029 O  O     . ARG A 1 2927 ? 215.310 227.568 270.589 1.00 21.36  ? 2927 ARG A O     1 
ATOM   11030 C  CB    . ARG A 1 2927 ? 215.340 224.712 271.344 1.00 21.73  ? 2927 ARG A CB    1 
ATOM   11031 C  CG    . ARG A 1 2927 ? 215.209 225.498 272.640 1.00 29.77  ? 2927 ARG A CG    1 
ATOM   11032 C  CD    . ARG A 1 2927 ? 215.866 224.755 273.790 1.00 31.13  ? 2927 ARG A CD    1 
ATOM   11033 N  NE    . ARG A 1 2927 ? 217.305 224.622 273.604 1.00 35.21  ? 2927 ARG A NE    1 
ATOM   11034 C  CZ    . ARG A 1 2927 ? 217.931 223.470 273.407 1.00 28.10  ? 2927 ARG A CZ    1 
ATOM   11035 N  NH1   . ARG A 1 2927 ? 217.271 222.325 273.365 1.00 21.54  ? 2927 ARG A NH1   1 
ATOM   11036 N  NH2   . ARG A 1 2927 ? 219.251 223.467 273.246 1.00 22.65  ? 2927 ARG A NH2   1 
ATOM   11037 N  N     . GLN A 1 2928 ? 215.583 226.881 268.472 1.00 20.76  ? 2928 GLN A N     1 
ATOM   11038 C  CA    . GLN A 1 2928 ? 216.178 228.121 268.004 1.00 15.61  ? 2928 GLN A CA    1 
ATOM   11039 C  C     . GLN A 1 2928 ? 215.228 228.838 267.059 1.00 20.17  ? 2928 GLN A C     1 
ATOM   11040 O  O     . GLN A 1 2928 ? 214.471 228.194 266.326 1.00 18.24  ? 2928 GLN A O     1 
ATOM   11041 C  CB    . GLN A 1 2928 ? 217.505 227.855 267.279 1.00 12.33  ? 2928 GLN A CB    1 
ATOM   11042 C  CG    . GLN A 1 2928 ? 218.704 227.729 268.197 1.00 20.96  ? 2928 GLN A CG    1 
ATOM   11043 C  CD    . GLN A 1 2928 ? 219.815 226.901 267.585 1.00 29.17  ? 2928 GLN A CD    1 
ATOM   11044 O  OE1   . GLN A 1 2928 ? 220.143 227.056 266.409 1.00 31.06  ? 2928 GLN A OE1   1 
ATOM   11045 N  NE2   . GLN A 1 2928 ? 220.398 226.012 268.380 1.00 28.12  ? 2928 GLN A NE2   1 
ATOM   11046 N  N     . PRO A 1 2929 ? 215.242 230.171 267.057 1.00 24.11  ? 2929 PRO A N     1 
ATOM   11047 C  CA    . PRO A 1 2929 ? 214.420 230.909 266.092 1.00 15.65  ? 2929 PRO A CA    1 
ATOM   11048 C  C     . PRO A 1 2929 ? 214.941 230.724 264.676 1.00 14.93  ? 2929 PRO A C     1 
ATOM   11049 O  O     . PRO A 1 2929 ? 216.149 230.744 264.432 1.00 16.34  ? 2929 PRO A O     1 
ATOM   11050 C  CB    . PRO A 1 2929 ? 214.553 232.364 266.552 1.00 18.97  ? 2929 PRO A CB    1 
ATOM   11051 C  CG    . PRO A 1 2929 ? 215.866 232.411 267.246 1.00 18.04  ? 2929 PRO A CG    1 
ATOM   11052 C  CD    . PRO A 1 2929 ? 216.030 231.073 267.915 1.00 22.76  ? 2929 PRO A CD    1 
ATOM   11053 N  N     . GLN A 1 2930 ? 214.006 230.550 263.740 1.00 20.01  ? 2930 GLN A N     1 
ATOM   11054 C  CA    . GLN A 1 2930 ? 214.332 230.306 262.333 1.00 14.01  ? 2930 GLN A CA    1 
ATOM   11055 C  C     . GLN A 1 2930 ? 215.263 229.104 262.188 1.00 12.05  ? 2930 GLN A C     1 
ATOM   11056 O  O     . GLN A 1 2930 ? 216.157 229.085 261.339 1.00 7.78   ? 2930 GLN A O     1 
ATOM   11057 C  CB    . GLN A 1 2930 ? 214.936 231.550 261.681 1.00 9.86   ? 2930 GLN A CB    1 
ATOM   11058 C  CG    . GLN A 1 2930 ? 214.526 231.751 260.235 1.00 14.47  ? 2930 GLN A CG    1 
ATOM   11059 C  CD    . GLN A 1 2930 ? 215.145 232.987 259.623 1.00 16.69  ? 2930 GLN A CD    1 
ATOM   11060 O  OE1   . GLN A 1 2930 ? 215.815 233.761 260.304 1.00 18.11  ? 2930 GLN A OE1   1 
ATOM   11061 N  NE2   . GLN A 1 2930 ? 214.924 233.181 258.329 1.00 20.64  ? 2930 GLN A NE2   1 
ATOM   11062 N  N     . GLY A 1 2931 ? 215.047 228.092 263.023 1.00 13.39  ? 2931 GLY A N     1 
ATOM   11063 C  CA    . GLY A 1 2931 ? 215.894 226.918 263.035 1.00 7.91   ? 2931 GLY A CA    1 
ATOM   11064 C  C     . GLY A 1 2931 ? 215.476 225.875 262.024 1.00 11.08  ? 2931 GLY A C     1 
ATOM   11065 O  O     . GLY A 1 2931 ? 214.490 225.161 262.225 1.00 12.82  ? 2931 GLY A O     1 
ATOM   11066 N  N     . HIS A 1 2932 ? 216.220 225.780 260.929 1.00 14.35  ? 2932 HIS A N     1 
ATOM   11067 C  CA    . HIS A 1 2932 ? 215.931 224.847 259.855 1.00 8.92   ? 2932 HIS A CA    1 
ATOM   11068 C  C     . HIS A 1 2932 ? 217.007 223.771 259.798 1.00 9.02   ? 2932 HIS A C     1 
ATOM   11069 O  O     . HIS A 1 2932 ? 218.180 224.027 260.074 1.00 11.43  ? 2932 HIS A O     1 
ATOM   11070 C  CB    . HIS A 1 2932 ? 215.843 225.571 258.510 1.00 9.37   ? 2932 HIS A CB    1 
ATOM   11071 C  CG    . HIS A 1 2932 ? 214.945 226.768 258.530 1.00 9.46   ? 2932 HIS A CG    1 
ATOM   11072 N  ND1   . HIS A 1 2932 ? 213.623 226.700 258.910 1.00 9.12   ? 2932 HIS A ND1   1 
ATOM   11073 C  CD2   . HIS A 1 2932 ? 215.181 228.065 258.222 1.00 11.77  ? 2932 HIS A CD2   1 
ATOM   11074 C  CE1   . HIS A 1 2932 ? 213.082 227.903 258.831 1.00 11.96  ? 2932 HIS A CE1   1 
ATOM   11075 N  NE2   . HIS A 1 2932 ? 214.007 228.749 258.416 1.00 11.62  ? 2932 HIS A NE2   1 
ATOM   11076 N  N     . LEU A 1 2933 ? 216.593 222.562 259.433 1.00 10.34  ? 2933 LEU A N     1 
ATOM   11077 C  CA    . LEU A 1 2933 ? 217.469 221.401 259.418 1.00 8.37   ? 2933 LEU A CA    1 
ATOM   11078 C  C     . LEU A 1 2933 ? 217.683 220.895 258.000 1.00 9.27   ? 2933 LEU A C     1 
ATOM   11079 O  O     . LEU A 1 2933 ? 216.820 221.040 257.130 1.00 12.40  ? 2933 LEU A O     1 
ATOM   11080 C  CB    . LEU A 1 2933 ? 216.895 220.270 260.275 1.00 7.43   ? 2933 LEU A CB    1 
ATOM   11081 C  CG    . LEU A 1 2933 ? 217.349 220.207 261.730 1.00 8.44   ? 2933 LEU A CG    1 
ATOM   11082 C  CD1   . LEU A 1 2933 ? 216.751 218.993 262.412 1.00 12.63  ? 2933 LEU A CD1   1 
ATOM   11083 C  CD2   . LEU A 1 2933 ? 218.862 220.162 261.787 1.00 14.44  ? 2933 LEU A CD2   1 
ATOM   11084 N  N     . LEU A 1 2934 ? 218.850 220.293 257.780 1.00 9.48   ? 2934 LEU A N     1 
ATOM   11085 C  CA    . LEU A 1 2934 ? 219.145 219.562 256.550 1.00 9.76   ? 2934 LEU A CA    1 
ATOM   11086 C  C     . LEU A 1 2934 ? 219.789 218.246 256.974 1.00 12.33  ? 2934 LEU A C     1 
ATOM   11087 O  O     . LEU A 1 2934 ? 220.996 218.194 257.226 1.00 13.42  ? 2934 LEU A O     1 
ATOM   11088 C  CB    . LEU A 1 2934 ? 220.052 220.356 255.619 1.00 9.64   ? 2934 LEU A CB    1 
ATOM   11089 C  CG    . LEU A 1 2934 ? 220.452 219.657 254.317 1.00 10.47  ? 2934 LEU A CG    1 
ATOM   11090 C  CD1   . LEU A 1 2934 ? 219.226 219.163 253.570 1.00 14.64  ? 2934 LEU A CD1   1 
ATOM   11091 C  CD2   . LEU A 1 2934 ? 221.272 220.582 253.439 1.00 13.34  ? 2934 LEU A CD2   1 
ATOM   11092 N  N     . LEU A 1 2935 ? 218.979 217.197 257.074 1.00 12.56  ? 2935 LEU A N     1 
ATOM   11093 C  CA    . LEU A 1 2935 ? 219.464 215.875 257.449 1.00 10.99  ? 2935 LEU A CA    1 
ATOM   11094 C  C     . LEU A 1 2935 ? 219.817 215.101 256.186 1.00 10.17  ? 2935 LEU A C     1 
ATOM   11095 O  O     . LEU A 1 2935 ? 218.936 214.773 255.386 1.00 14.37  ? 2935 LEU A O     1 
ATOM   11096 C  CB    . LEU A 1 2935 ? 218.417 215.120 258.265 1.00 10.64  ? 2935 LEU A CB    1 
ATOM   11097 C  CG    . LEU A 1 2935 ? 217.766 215.869 259.427 1.00 12.60  ? 2935 LEU A CG    1 
ATOM   11098 C  CD1   . LEU A 1 2935 ? 216.804 214.956 260.165 1.00 10.49  ? 2935 LEU A CD1   1 
ATOM   11099 C  CD2   . LEU A 1 2935 ? 218.821 216.414 260.373 1.00 12.44  ? 2935 LEU A CD2   1 
ATOM   11100 N  N     . ILE A 1 2936 ? 221.101 214.806 256.013 1.00 12.51  ? 2936 ILE A N     1 
ATOM   11101 C  CA    . ILE A 1 2936 ? 221.594 214.104 254.834 1.00 12.82  ? 2936 ILE A CA    1 
ATOM   11102 C  C     . ILE A 1 2936 ? 222.008 212.705 255.260 1.00 13.74  ? 2936 ILE A C     1 
ATOM   11103 O  O     . ILE A 1 2936 ? 222.904 212.544 256.097 1.00 14.71  ? 2936 ILE A O     1 
ATOM   11104 C  CB    . ILE A 1 2936 ? 222.762 214.854 254.178 1.00 11.19  ? 2936 ILE A CB    1 
ATOM   11105 C  CG1   . ILE A 1 2936 ? 222.341 216.286 253.845 1.00 11.14  ? 2936 ILE A CG1   1 
ATOM   11106 C  CG2   . ILE A 1 2936 ? 223.226 214.126 252.930 1.00 12.04  ? 2936 ILE A CG2   1 
ATOM   11107 C  CD1   . ILE A 1 2936 ? 223.455 217.132 253.303 1.00 17.97  ? 2936 ILE A CD1   1 
ATOM   11108 N  N     . GLY A 1 2937 ? 221.363 211.698 254.687 1.00 11.38  ? 2937 GLY A N     1 
ATOM   11109 C  CA    . GLY A 1 2937 ? 221.664 210.324 255.041 1.00 12.91  ? 2937 GLY A CA    1 
ATOM   11110 C  C     . GLY A 1 2937 ? 220.905 209.371 254.147 1.00 13.57  ? 2937 GLY A C     1 
ATOM   11111 O  O     . GLY A 1 2937 ? 220.056 209.773 253.345 1.00 15.43  ? 2937 GLY A O     1 
ATOM   11112 N  N     . VAL A 1 2938 ? 221.230 208.087 254.301 1.00 14.52  ? 2938 VAL A N     1 
ATOM   11113 C  CA    . VAL A 1 2938 ? 220.601 207.047 253.499 1.00 12.68  ? 2938 VAL A CA    1 
ATOM   11114 C  C     . VAL A 1 2938 ? 219.124 206.933 253.858 1.00 15.93  ? 2938 VAL A C     1 
ATOM   11115 O  O     . VAL A 1 2938 ? 218.713 207.184 254.999 1.00 16.38  ? 2938 VAL A O     1 
ATOM   11116 C  CB    . VAL A 1 2938 ? 221.332 205.708 253.701 1.00 11.63  ? 2938 VAL A CB    1 
ATOM   11117 C  CG1   . VAL A 1 2938 ? 220.902 204.694 252.656 1.00 15.38  ? 2938 VAL A CG1   1 
ATOM   11118 C  CG2   . VAL A 1 2938 ? 222.831 205.921 253.638 1.00 12.18  ? 2938 VAL A CG2   1 
ATOM   11119 N  N     . SER A 1 2939 ? 218.314 206.561 252.869 1.00 12.50  ? 2939 SER A N     1 
ATOM   11120 C  CA    . SER A 1 2939 ? 216.890 206.371 253.101 1.00 10.96  ? 2939 SER A CA    1 
ATOM   11121 C  C     . SER A 1 2939 ? 216.658 205.207 254.056 1.00 13.11  ? 2939 SER A C     1 
ATOM   11122 O  O     . SER A 1 2939 ? 217.405 204.227 254.071 1.00 15.63  ? 2939 SER A O     1 
ATOM   11123 C  CB    . SER A 1 2939 ? 216.164 206.120 251.779 1.00 15.38  ? 2939 SER A CB    1 
ATOM   11124 O  OG    . SER A 1 2939 ? 216.206 207.265 250.946 1.00 24.63  ? 2939 SER A OG    1 
ATOM   11125 N  N     . GLY A 1 2940 ? 215.613 205.329 254.867 1.00 12.59  ? 2940 GLY A N     1 
ATOM   11126 C  CA    . GLY A 1 2940 ? 215.314 204.317 255.855 1.00 10.39  ? 2940 GLY A CA    1 
ATOM   11127 C  C     . GLY A 1 2940 ? 216.197 204.337 257.079 1.00 12.51  ? 2940 GLY A C     1 
ATOM   11128 O  O     . GLY A 1 2940 ? 216.210 203.355 257.830 1.00 15.32  ? 2940 GLY A O     1 
ATOM   11129 N  N     . ALA A 1 2941 ? 216.944 205.415 257.302 1.00 11.91  ? 2941 ALA A N     1 
ATOM   11130 C  CA    . ALA A 1 2941 ? 217.802 205.539 258.471 1.00 11.43  ? 2941 ALA A CA    1 
ATOM   11131 C  C     . ALA A 1 2941 ? 217.086 206.148 259.668 1.00 14.40  ? 2941 ALA A C     1 
ATOM   11132 O  O     . ALA A 1 2941 ? 217.668 206.205 260.756 1.00 14.84  ? 2941 ALA A O     1 
ATOM   11133 C  CB    . ALA A 1 2941 ? 219.037 206.377 258.132 1.00 12.66  ? 2941 ALA A CB    1 
ATOM   11134 N  N     . GLY A 1 2942 ? 215.845 206.594 259.499 1.00 12.62  ? 2942 GLY A N     1 
ATOM   11135 C  CA    . GLY A 1 2942 ? 215.091 207.159 260.597 1.00 11.38  ? 2942 GLY A CA    1 
ATOM   11136 C  C     . GLY A 1 2942 ? 215.094 208.665 260.688 1.00 11.52  ? 2942 GLY A C     1 
ATOM   11137 O  O     . GLY A 1 2942 ? 214.707 209.203 261.731 1.00 13.39  ? 2942 GLY A O     1 
ATOM   11138 N  N     . LYS A 1 2943 ? 215.515 209.368 259.635 1.00 10.05  ? 2943 LYS A N     1 
ATOM   11139 C  CA    . LYS A 1 2943 ? 215.550 210.827 259.682 1.00 8.92   ? 2943 LYS A CA    1 
ATOM   11140 C  C     . LYS A 1 2943 ? 214.156 211.404 259.904 1.00 9.12   ? 2943 LYS A C     1 
ATOM   11141 O  O     . LYS A 1 2943 ? 213.945 212.215 260.813 1.00 11.35  ? 2943 LYS A O     1 
ATOM   11142 C  CB    . LYS A 1 2943 ? 216.159 211.378 258.394 1.00 9.42   ? 2943 LYS A CB    1 
ATOM   11143 C  CG    . LYS A 1 2943 ? 217.533 210.822 258.068 1.00 9.84   ? 2943 LYS A CG    1 
ATOM   11144 C  CD    . LYS A 1 2943 ? 218.187 211.602 256.942 1.00 10.70  ? 2943 LYS A CD    1 
ATOM   11145 C  CE    . LYS A 1 2943 ? 217.429 211.433 255.638 1.00 9.60   ? 2943 LYS A CE    1 
ATOM   11146 N  NZ    . LYS A 1 2943 ? 217.613 210.076 255.061 1.00 12.25  ? 2943 LYS A NZ    1 
ATOM   11147 N  N     . THR A 1 2944 ? 213.190 210.990 259.082 1.00 9.24   ? 2944 THR A N     1 
ATOM   11148 C  CA    . THR A 1 2944 ? 211.829 211.496 259.225 1.00 8.40   ? 2944 THR A CA    1 
ATOM   11149 C  C     . THR A 1 2944 ? 211.214 211.072 260.552 1.00 8.90   ? 2944 THR A C     1 
ATOM   11150 O  O     . THR A 1 2944 ? 210.544 211.872 261.215 1.00 10.23  ? 2944 THR A O     1 
ATOM   11151 C  CB    . THR A 1 2944 ? 210.965 211.018 258.058 1.00 5.92   ? 2944 THR A CB    1 
ATOM   11152 O  OG1   . THR A 1 2944 ? 211.596 211.365 256.821 1.00 7.65   ? 2944 THR A OG1   1 
ATOM   11153 C  CG2   . THR A 1 2944 ? 209.588 211.656 258.113 1.00 6.02   ? 2944 THR A CG2   1 
ATOM   11154 N  N     . THR A 1 2945 ? 211.432 209.820 260.958 1.00 8.30   ? 2945 THR A N     1 
ATOM   11155 C  CA    . THR A 1 2945 ? 210.854 209.335 262.208 1.00 9.42   ? 2945 THR A CA    1 
ATOM   11156 C  C     . THR A 1 2945 ? 211.425 210.085 263.405 1.00 9.86   ? 2945 THR A C     1 
ATOM   11157 O  O     . THR A 1 2945 ? 210.683 210.505 264.301 1.00 16.04  ? 2945 THR A O     1 
ATOM   11158 C  CB    . THR A 1 2945 ? 211.092 207.832 262.346 1.00 16.21  ? 2945 THR A CB    1 
ATOM   11159 O  OG1   . THR A 1 2945 ? 210.546 207.155 261.207 1.00 18.24  ? 2945 THR A OG1   1 
ATOM   11160 C  CG2   . THR A 1 2945 ? 210.430 207.299 263.606 1.00 11.10  ? 2945 THR A CG2   1 
ATOM   11161 N  N     . LEU A 1 2946 ? 212.748 210.266 263.437 1.00 7.92   ? 2946 LEU A N     1 
ATOM   11162 C  CA    . LEU A 1 2946 ? 213.363 211.000 264.537 1.00 6.87   ? 2946 LEU A CA    1 
ATOM   11163 C  C     . LEU A 1 2946 ? 212.927 212.459 264.541 1.00 8.91   ? 2946 LEU A C     1 
ATOM   11164 O  O     . LEU A 1 2946 ? 212.690 213.038 265.607 1.00 11.11  ? 2946 LEU A O     1 
ATOM   11165 C  CB    . LEU A 1 2946 ? 214.886 210.893 264.460 1.00 7.50   ? 2946 LEU A CB    1 
ATOM   11166 C  CG    . LEU A 1 2946 ? 215.508 209.538 264.801 1.00 7.54   ? 2946 LEU A CG    1 
ATOM   11167 C  CD1   . LEU A 1 2946 ? 217.006 209.678 264.996 1.00 11.41  ? 2946 LEU A CD1   1 
ATOM   11168 C  CD2   . LEU A 1 2946 ? 214.859 208.931 266.035 1.00 7.14   ? 2946 LEU A CD2   1 
ATOM   11169 N  N     . SER A 1 2947 ? 212.817 213.070 263.358 1.00 10.12  ? 2947 SER A N     1 
ATOM   11170 C  CA    . SER A 1 2947 ? 212.348 214.450 263.283 1.00 7.57   ? 2947 SER A CA    1 
ATOM   11171 C  C     . SER A 1 2947 ? 210.931 214.580 263.825 1.00 8.38   ? 2947 SER A C     1 
ATOM   11172 O  O     . SER A 1 2947 ? 210.639 215.496 264.602 1.00 12.84  ? 2947 SER A O     1 
ATOM   11173 C  CB    . SER A 1 2947 ? 212.420 214.949 261.841 1.00 7.27   ? 2947 SER A CB    1 
ATOM   11174 O  OG    . SER A 1 2947 ? 213.696 214.703 261.282 1.00 8.97   ? 2947 SER A OG    1 
ATOM   11175 N  N     . ARG A 1 2948 ? 210.041 213.665 263.436 1.00 8.27   ? 2948 ARG A N     1 
ATOM   11176 C  CA    . ARG A 1 2948 ? 208.672 213.695 263.941 1.00 8.53   ? 2948 ARG A CA    1 
ATOM   11177 C  C     . ARG A 1 2948 ? 208.631 213.476 265.446 1.00 9.53   ? 2948 ARG A C     1 
ATOM   11178 O  O     . ARG A 1 2948 ? 207.863 214.133 266.156 1.00 12.61  ? 2948 ARG A O     1 
ATOM   11179 C  CB    . ARG A 1 2948 ? 207.824 212.643 263.226 1.00 6.86   ? 2948 ARG A CB    1 
ATOM   11180 C  CG    . ARG A 1 2948 ? 207.582 212.934 261.761 1.00 9.70   ? 2948 ARG A CG    1 
ATOM   11181 C  CD    . ARG A 1 2948 ? 206.788 211.822 261.105 1.00 15.30  ? 2948 ARG A CD    1 
ATOM   11182 N  NE    . ARG A 1 2948 ? 205.413 211.776 261.582 1.00 23.77  ? 2948 ARG A NE    1 
ATOM   11183 C  CZ    . ARG A 1 2948 ? 204.440 211.095 260.994 1.00 26.36  ? 2948 ARG A CZ    1 
ATOM   11184 N  NH1   . ARG A 1 2948 ? 204.657 210.390 259.895 1.00 24.59  ? 2948 ARG A NH1   1 
ATOM   11185 N  NH2   . ARG A 1 2948 ? 203.220 211.117 261.522 1.00 26.47  ? 2948 ARG A NH2   1 
ATOM   11186 N  N     . PHE A 1 2949 ? 209.451 212.552 265.951 1.00 7.32   ? 2949 PHE A N     1 
ATOM   11187 C  CA    . PHE A 1 2949 ? 209.467 212.271 267.383 1.00 9.78   ? 2949 PHE A CA    1 
ATOM   11188 C  C     . PHE A 1 2949 ? 209.932 213.489 268.175 1.00 12.94  ? 2949 PHE A C     1 
ATOM   11189 O  O     . PHE A 1 2949 ? 209.327 213.855 269.191 1.00 13.02  ? 2949 PHE A O     1 
ATOM   11190 C  CB    . PHE A 1 2949 ? 210.364 211.061 267.649 1.00 10.89  ? 2949 PHE A CB    1 
ATOM   11191 C  CG    . PHE A 1 2949 ? 210.607 210.783 269.102 1.00 11.88  ? 2949 PHE A CG    1 
ATOM   11192 C  CD1   . PHE A 1 2949 ? 209.549 210.571 269.968 1.00 12.74  ? 2949 PHE A CD1   1 
ATOM   11193 C  CD2   . PHE A 1 2949 ? 211.896 210.708 269.599 1.00 11.69  ? 2949 PHE A CD2   1 
ATOM   11194 C  CE1   . PHE A 1 2949 ? 209.770 210.306 271.301 1.00 13.65  ? 2949 PHE A CE1   1 
ATOM   11195 C  CE2   . PHE A 1 2949 ? 212.123 210.440 270.932 1.00 16.07  ? 2949 PHE A CE2   1 
ATOM   11196 C  CZ    . PHE A 1 2949 ? 211.057 210.236 271.784 1.00 16.46  ? 2949 PHE A CZ    1 
ATOM   11197 N  N     . VAL A 1 2950 ? 210.998 214.144 267.710 1.00 12.67  ? 2950 VAL A N     1 
ATOM   11198 C  CA    . VAL A 1 2950 ? 211.509 215.315 268.414 1.00 11.14  ? 2950 VAL A CA    1 
ATOM   11199 C  C     . VAL A 1 2950 ? 210.526 216.475 268.312 1.00 13.03  ? 2950 VAL A C     1 
ATOM   11200 O  O     . VAL A 1 2950 ? 210.340 217.233 269.271 1.00 20.12  ? 2950 VAL A O     1 
ATOM   11201 C  CB    . VAL A 1 2950 ? 212.901 215.696 267.882 1.00 11.43  ? 2950 VAL A CB    1 
ATOM   11202 C  CG1   . VAL A 1 2950 ? 213.396 216.959 268.557 1.00 12.50  ? 2950 VAL A CG1   1 
ATOM   11203 C  CG2   . VAL A 1 2950 ? 213.880 214.560 268.116 1.00 10.63  ? 2950 VAL A CG2   1 
ATOM   11204 N  N     . ALA A 1 2951 ? 209.875 216.632 267.156 1.00 8.81   ? 2951 ALA A N     1 
ATOM   11205 C  CA    . ALA A 1 2951 ? 208.861 217.671 267.019 1.00 9.65   ? 2951 ALA A CA    1 
ATOM   11206 C  C     . ALA A 1 2951 ? 207.697 217.427 267.968 1.00 13.00  ? 2951 ALA A C     1 
ATOM   11207 O  O     . ALA A 1 2951 ? 207.146 218.371 268.546 1.00 16.05  ? 2951 ALA A O     1 
ATOM   11208 C  CB    . ALA A 1 2951 ? 208.371 217.739 265.573 1.00 9.77   ? 2951 ALA A CB    1 
ATOM   11209 N  N     . TRP A 1 2952 ? 207.304 216.163 268.136 1.00 14.75  ? 2952 TRP A N     1 
ATOM   11210 C  CA    . TRP A 1 2952 ? 206.250 215.834 269.088 1.00 13.54  ? 2952 TRP A CA    1 
ATOM   11211 C  C     . TRP A 1 2952 ? 206.684 216.134 270.517 1.00 12.56  ? 2952 TRP A C     1 
ATOM   11212 O  O     . TRP A 1 2952 ? 205.881 216.610 271.328 1.00 16.44  ? 2952 TRP A O     1 
ATOM   11213 C  CB    . TRP A 1 2952 ? 205.851 214.366 268.941 1.00 15.27  ? 2952 TRP A CB    1 
ATOM   11214 C  CG    . TRP A 1 2952 ? 204.977 213.872 270.045 1.00 15.45  ? 2952 TRP A CG    1 
ATOM   11215 C  CD1   . TRP A 1 2952 ? 203.625 214.017 270.147 1.00 17.71  ? 2952 TRP A CD1   1 
ATOM   11216 C  CD2   . TRP A 1 2952 ? 205.393 213.152 271.209 1.00 14.77  ? 2952 TRP A CD2   1 
ATOM   11217 N  NE1   . TRP A 1 2952 ? 203.173 213.431 271.304 1.00 22.05  ? 2952 TRP A NE1   1 
ATOM   11218 C  CE2   . TRP A 1 2952 ? 204.240 212.894 271.974 1.00 17.29  ? 2952 TRP A CE2   1 
ATOM   11219 C  CE3   . TRP A 1 2952 ? 206.629 212.703 271.680 1.00 13.02  ? 2952 TRP A CE3   1 
ATOM   11220 C  CZ2   . TRP A 1 2952 ? 204.286 212.205 273.182 1.00 21.03  ? 2952 TRP A CZ2   1 
ATOM   11221 C  CZ3   . TRP A 1 2952 ? 206.672 212.020 272.878 1.00 17.90  ? 2952 TRP A CZ3   1 
ATOM   11222 C  CH2   . TRP A 1 2952 ? 205.510 211.777 273.615 1.00 21.50  ? 2952 TRP A CH2   1 
ATOM   11223 N  N     . MET A 1 2953 ? 207.948 215.859 270.849 1.00 12.52  ? 2953 MET A N     1 
ATOM   11224 C  CA    . MET A 1 2953 ? 208.425 216.156 272.197 1.00 14.10  ? 2953 MET A CA    1 
ATOM   11225 C  C     . MET A 1 2953 ? 208.453 217.657 272.457 1.00 16.08  ? 2953 MET A C     1 
ATOM   11226 O  O     . MET A 1 2953 ? 208.212 218.103 273.585 1.00 19.32  ? 2953 MET A O     1 
ATOM   11227 C  CB    . MET A 1 2953 ? 209.814 215.560 272.422 1.00 14.41  ? 2953 MET A CB    1 
ATOM   11228 C  CG    . MET A 1 2953 ? 209.857 214.050 272.429 1.00 16.32  ? 2953 MET A CG    1 
ATOM   11229 S  SD    . MET A 1 2953 ? 211.542 213.453 272.624 1.00 36.78  ? 2953 MET A SD    1 
ATOM   11230 C  CE    . MET A 1 2953 ? 211.846 213.900 274.330 1.00 22.85  ? 2953 MET A CE    1 
ATOM   11231 N  N     . ASN A 1 2954 ? 208.756 218.448 271.433 1.00 16.56  ? 2954 ASN A N     1 
ATOM   11232 C  CA    . ASN A 1 2954 ? 208.837 219.895 271.569 1.00 16.21  ? 2954 ASN A CA    1 
ATOM   11233 C  C     . ASN A 1 2954 ? 207.523 220.597 271.263 1.00 17.29  ? 2954 ASN A C     1 
ATOM   11234 O  O     . ASN A 1 2954 ? 207.488 221.832 271.237 1.00 25.69  ? 2954 ASN A O     1 
ATOM   11235 C  CB    . ASN A 1 2954 ? 209.941 220.447 270.664 1.00 14.60  ? 2954 ASN A CB    1 
ATOM   11236 C  CG    . ASN A 1 2954 ? 211.327 220.125 271.179 1.00 18.25  ? 2954 ASN A CG    1 
ATOM   11237 O  OD1   . ASN A 1 2954 ? 211.661 220.430 272.323 1.00 19.79  ? 2954 ASN A OD1   1 
ATOM   11238 N  ND2   . ASN A 1 2954 ? 212.143 219.508 270.336 1.00 20.63  ? 2954 ASN A ND2   1 
ATOM   11239 N  N     . GLY A 1 2955 ? 206.449 219.851 271.020 1.00 16.20  ? 2955 GLY A N     1 
ATOM   11240 C  CA    . GLY A 1 2955 ? 205.152 220.440 270.773 1.00 14.01  ? 2955 GLY A CA    1 
ATOM   11241 C  C     . GLY A 1 2955 ? 204.919 220.930 269.363 1.00 17.25  ? 2955 GLY A C     1 
ATOM   11242 O  O     . GLY A 1 2955 ? 203.842 221.475 269.089 1.00 22.18  ? 2955 GLY A O     1 
ATOM   11243 N  N     . LEU A 1 2956 ? 205.882 220.764 268.461 1.00 15.12  ? 2956 LEU A N     1 
ATOM   11244 C  CA    . LEU A 1 2956 ? 205.693 221.199 267.087 1.00 13.45  ? 2956 LEU A CA    1 
ATOM   11245 C  C     . LEU A 1 2956 ? 204.698 220.295 266.369 1.00 14.77  ? 2956 LEU A C     1 
ATOM   11246 O  O     . LEU A 1 2956 ? 204.613 219.092 266.633 1.00 19.38  ? 2956 LEU A O     1 
ATOM   11247 C  CB    . LEU A 1 2956 ? 207.022 221.207 266.330 1.00 13.16  ? 2956 LEU A CB    1 
ATOM   11248 C  CG    . LEU A 1 2956 ? 208.277 221.766 267.003 1.00 13.79  ? 2956 LEU A CG    1 
ATOM   11249 C  CD1   . LEU A 1 2956 ? 209.399 221.881 265.988 1.00 14.42  ? 2956 LEU A CD1   1 
ATOM   11250 C  CD2   . LEU A 1 2956 ? 208.012 223.109 267.652 1.00 15.29  ? 2956 LEU A CD2   1 
ATOM   11251 N  N     . SER A 1 2957 ? 203.939 220.887 265.454 1.00 14.98  ? 2957 SER A N     1 
ATOM   11252 C  CA    . SER A 1 2957 ? 202.989 220.160 264.625 1.00 14.96  ? 2957 SER A CA    1 
ATOM   11253 C  C     . SER A 1 2957 ? 203.685 219.752 263.334 1.00 14.58  ? 2957 SER A C     1 
ATOM   11254 O  O     . SER A 1 2957 ? 204.217 220.604 262.618 1.00 16.46  ? 2957 SER A O     1 
ATOM   11255 C  CB    . SER A 1 2957 ? 201.759 221.019 264.328 1.00 15.12  ? 2957 SER A CB    1 
ATOM   11256 O  OG    . SER A 1 2957 ? 200.843 220.332 263.495 1.00 24.83  ? 2957 SER A OG    1 
ATOM   11257 N  N     . VAL A 1 2958 ? 203.696 218.457 263.047 1.00 13.53  ? 2958 VAL A N     1 
ATOM   11258 C  CA    . VAL A 1 2958 ? 204.397 217.946 261.875 1.00 13.61  ? 2958 VAL A CA    1 
ATOM   11259 C  C     . VAL A 1 2958 ? 203.529 218.150 260.642 1.00 11.69  ? 2958 VAL A C     1 
ATOM   11260 O  O     . VAL A 1 2958 ? 202.352 217.772 260.625 1.00 14.80  ? 2958 VAL A O     1 
ATOM   11261 C  CB    . VAL A 1 2958 ? 204.761 216.465 262.061 1.00 12.98  ? 2958 VAL A CB    1 
ATOM   11262 C  CG1   . VAL A 1 2958 ? 205.316 215.888 260.770 1.00 11.02  ? 2958 VAL A CG1   1 
ATOM   11263 C  CG2   . VAL A 1 2958 ? 205.764 216.307 263.189 1.00 12.01  ? 2958 VAL A CG2   1 
ATOM   11264 N  N     . TYR A 1 2959 ? 204.105 218.758 259.608 1.00 14.70  ? 2959 TYR A N     1 
ATOM   11265 C  CA    . TYR A 1 2959 ? 203.431 218.952 258.330 1.00 13.38  ? 2959 TYR A CA    1 
ATOM   11266 C  C     . TYR A 1 2959 ? 204.293 218.370 257.221 1.00 16.82  ? 2959 TYR A C     1 
ATOM   11267 O  O     . TYR A 1 2959 ? 205.451 218.765 257.058 1.00 18.25  ? 2959 TYR A O     1 
ATOM   11268 C  CB    . TYR A 1 2959 ? 203.148 220.434 258.070 1.00 14.75  ? 2959 TYR A CB    1 
ATOM   11269 C  CG    . TYR A 1 2959 ? 202.236 220.685 256.889 1.00 19.09  ? 2959 TYR A CG    1 
ATOM   11270 C  CD1   . TYR A 1 2959 ? 202.729 220.675 255.590 1.00 22.83  ? 2959 TYR A CD1   1 
ATOM   11271 C  CD2   . TYR A 1 2959 ? 200.882 220.924 257.071 1.00 20.44  ? 2959 TYR A CD2   1 
ATOM   11272 C  CE1   . TYR A 1 2959 ? 201.900 220.898 254.509 1.00 23.44  ? 2959 TYR A CE1   1 
ATOM   11273 C  CE2   . TYR A 1 2959 ? 200.047 221.151 255.996 1.00 25.79  ? 2959 TYR A CE2   1 
ATOM   11274 C  CZ    . TYR A 1 2959 ? 200.561 221.137 254.717 1.00 25.78  ? 2959 TYR A CZ    1 
ATOM   11275 O  OH    . TYR A 1 2959 ? 199.733 221.360 253.641 1.00 31.32  ? 2959 TYR A OH    1 
ATOM   11276 N  N     . GLN A 1 2960 ? 203.722 217.442 256.457 1.00 19.50  ? 2960 GLN A N     1 
ATOM   11277 C  CA    . GLN A 1 2960 ? 204.373 216.874 255.286 1.00 19.43  ? 2960 GLN A CA    1 
ATOM   11278 C  C     . GLN A 1 2960 ? 203.443 217.027 254.094 1.00 21.59  ? 2960 GLN A C     1 
ATOM   11279 O  O     . GLN A 1 2960 ? 202.255 216.702 254.188 1.00 33.00  ? 2960 GLN A O     1 
ATOM   11280 C  CB    . GLN A 1 2960 ? 204.723 215.397 255.498 1.00 23.66  ? 2960 GLN A CB    1 
ATOM   11281 C  CG    . GLN A 1 2960 ? 205.439 215.103 256.804 1.00 21.54  ? 2960 GLN A CG    1 
ATOM   11282 C  CD    . GLN A 1 2960 ? 205.608 213.619 257.051 1.00 24.79  ? 2960 GLN A CD    1 
ATOM   11283 O  OE1   . GLN A 1 2960 ? 205.139 213.090 258.058 1.00 28.62  ? 2960 GLN A OE1   1 
ATOM   11284 N  NE2   . GLN A 1 2960 ? 206.277 212.938 256.130 1.00 17.09  ? 2960 GLN A NE2   1 
ATOM   11285 N  N     . ILE A 1 2961 ? 203.977 217.529 252.982 1.00 23.96  ? 2961 ILE A N     1 
ATOM   11286 C  CA    . ILE A 1 2961 ? 203.173 217.671 251.775 1.00 30.04  ? 2961 ILE A CA    1 
ATOM   11287 C  C     . ILE A 1 2961 ? 202.933 216.297 251.165 1.00 33.03  ? 2961 ILE A C     1 
ATOM   11288 O  O     . ILE A 1 2961 ? 203.852 215.477 251.052 1.00 29.73  ? 2961 ILE A O     1 
ATOM   11289 C  CB    . ILE A 1 2961 ? 203.851 218.622 250.776 1.00 28.00  ? 2961 ILE A CB    1 
ATOM   11290 C  CG1   . ILE A 1 2961 ? 205.288 218.185 250.493 1.00 23.80  ? 2961 ILE A CG1   1 
ATOM   11291 C  CG2   . ILE A 1 2961 ? 203.814 220.048 251.292 1.00 25.17  ? 2961 ILE A CG2   1 
ATOM   11292 C  CD1   . ILE A 1 2961 ? 205.920 218.907 249.327 1.00 35.31  ? 2961 ILE A CD1   1 
ATOM   11293 N  N     . LYS A 1 2962 ? 201.685 216.034 250.787 1.00 37.29  ? 2962 LYS A N     1 
ATOM   11294 C  CA    . LYS A 1 2962 ? 201.300 214.749 250.207 1.00 37.06  ? 2962 LYS A CA    1 
ATOM   11295 C  C     . LYS A 1 2962 ? 201.426 214.864 248.693 1.00 40.59  ? 2962 LYS A C     1 
ATOM   11296 O  O     . LYS A 1 2962 ? 200.515 215.319 248.002 1.00 42.49  ? 2962 LYS A O     1 
ATOM   11297 C  CB    . LYS A 1 2962 ? 199.890 214.368 250.640 1.00 40.62  ? 2962 LYS A CB    1 
ATOM   11298 C  CG    . LYS A 1 2962 ? 199.761 214.097 252.133 1.00 44.83  ? 2962 LYS A CG    1 
ATOM   11299 C  CD    . LYS A 1 2962 ? 201.013 213.440 252.696 1.00 44.99  ? 2962 LYS A CD    1 
ATOM   11300 C  CE    . LYS A 1 2962 ? 200.804 212.988 254.128 1.00 46.60  ? 2962 LYS A CE    1 
ATOM   11301 N  NZ    . LYS A 1 2962 ? 200.449 214.127 255.018 1.00 43.68  ? 2962 LYS A NZ    1 
ATOM   11302 N  N     . VAL A 1 2963 ? 202.574 214.443 248.176 1.00 41.01  ? 2963 VAL A N     1 
ATOM   11303 C  CA    . VAL A 1 2963 ? 202.878 214.581 246.757 1.00 38.81  ? 2963 VAL A CA    1 
ATOM   11304 C  C     . VAL A 1 2963 ? 202.343 213.369 246.008 1.00 43.89  ? 2963 VAL A C     1 
ATOM   11305 O  O     . VAL A 1 2963 ? 202.504 212.226 246.453 1.00 44.38  ? 2963 VAL A O     1 
ATOM   11306 C  CB    . VAL A 1 2963 ? 204.391 214.745 246.543 1.00 34.86  ? 2963 VAL A CB    1 
ATOM   11307 C  CG1   . VAL A 1 2963 ? 204.720 214.784 245.060 1.00 38.93  ? 2963 VAL A CG1   1 
ATOM   11308 C  CG2   . VAL A 1 2963 ? 204.890 215.998 247.237 1.00 37.11  ? 2963 VAL A CG2   1 
ATOM   11309 N  N     . HIS A 1 2964 ? 201.694 213.615 244.871 1.00 42.21  ? 2964 HIS A N     1 
ATOM   11310 C  CA    . HIS A 1 2964 ? 201.226 212.538 244.009 1.00 44.65  ? 2964 HIS A CA    1 
ATOM   11311 C  C     . HIS A 1 2964 ? 201.640 212.795 242.565 1.00 48.59  ? 2964 HIS A C     1 
ATOM   11312 O  O     . HIS A 1 2964 ? 202.424 213.711 242.294 1.00 46.54  ? 2964 HIS A O     1 
ATOM   11313 C  CB    . HIS A 1 2964 ? 199.707 212.378 244.118 1.00 40.63  ? 2964 HIS A CB    1 
ATOM   11314 C  CG    . HIS A 1 2964 ? 198.955 213.670 244.056 1.00 43.68  ? 2964 HIS A CG    1 
ATOM   11315 N  ND1   . HIS A 1 2964 ? 198.838 214.409 242.900 1.00 40.73  ? 2964 HIS A ND1   1 
ATOM   11316 C  CD2   . HIS A 1 2964 ? 198.275 214.351 245.008 1.00 45.15  ? 2964 HIS A CD2   1 
ATOM   11317 C  CE1   . HIS A 1 2964 ? 198.122 215.492 243.142 1.00 41.88  ? 2964 HIS A CE1   1 
ATOM   11318 N  NE2   . HIS A 1 2964 ? 197.767 215.481 244.414 1.00 46.26  ? 2964 HIS A NE2   1 
ATOM   11319 N  N     . ARG A 1 2965 ? 201.131 211.985 241.636 1.00 48.73  ? 2965 ARG A N     1 
ATOM   11320 C  CA    . ARG A 1 2965 ? 201.508 212.134 240.232 1.00 48.94  ? 2965 ARG A CA    1 
ATOM   11321 C  C     . ARG A 1 2965 ? 201.035 213.465 239.661 1.00 54.94  ? 2965 ARG A C     1 
ATOM   11322 O  O     . ARG A 1 2965 ? 201.758 214.107 238.890 1.00 54.10  ? 2965 ARG A O     1 
ATOM   11323 C  CB    . ARG A 1 2965 ? 200.947 210.974 239.415 1.00 57.79  ? 2965 ARG A CB    1 
ATOM   11324 C  CG    . ARG A 1 2965 ? 201.290 211.038 237.938 1.00 71.79  ? 2965 ARG A CG    1 
ATOM   11325 C  CD    . ARG A 1 2965 ? 200.737 209.829 237.216 1.00 69.22  ? 2965 ARG A CD    1 
ATOM   11326 N  NE    . ARG A 1 2965 ? 201.270 208.600 237.784 1.00 63.60  ? 2965 ARG A NE    1 
ATOM   11327 C  CZ    . ARG A 1 2965 ? 200.601 207.459 237.861 1.00 63.75  ? 2965 ARG A CZ    1 
ATOM   11328 N  NH1   . ARG A 1 2965 ? 199.362 207.353 237.408 1.00 66.08  ? 2965 ARG A NH1   1 
ATOM   11329 N  NH2   . ARG A 1 2965 ? 201.186 206.401 238.412 1.00 62.15  ? 2965 ARG A NH2   1 
ATOM   11330 N  N     . LYS A 1 2966 ? 199.830 213.895 240.022 1.00 54.92  ? 2966 LYS A N     1 
ATOM   11331 C  CA    . LYS A 1 2966 ? 199.261 215.134 239.515 1.00 51.06  ? 2966 LYS A CA    1 
ATOM   11332 C  C     . LYS A 1 2966 ? 199.679 216.351 240.330 1.00 48.51  ? 2966 LYS A C     1 
ATOM   11333 O  O     . LYS A 1 2966 ? 199.154 217.446 240.099 1.00 40.60  ? 2966 LYS A O     1 
ATOM   11334 C  CB    . LYS A 1 2966 ? 197.734 215.034 239.473 1.00 55.51  ? 2966 LYS A CB    1 
ATOM   11335 C  CG    . LYS A 1 2966 ? 197.211 214.027 238.463 1.00 52.03  ? 2966 LYS A CG    1 
ATOM   11336 C  CD    . LYS A 1 2966 ? 195.698 214.089 238.352 1.00 55.73  ? 2966 LYS A CD    1 
ATOM   11337 C  CE    . LYS A 1 2966 ? 195.030 213.472 239.569 1.00 62.10  ? 2966 LYS A CE    1 
ATOM   11338 N  NZ    . LYS A 1 2966 ? 193.549 213.425 239.428 1.00 55.88  ? 2966 LYS A NZ    1 
ATOM   11339 N  N     . TYR A 1 2967 ? 200.594 216.182 241.282 1.00 50.11  ? 2967 TYR A N     1 
ATOM   11340 C  CA    . TYR A 1 2967 ? 201.086 217.308 242.066 1.00 41.49  ? 2967 TYR A CA    1 
ATOM   11341 C  C     . TYR A 1 2967 ? 201.812 218.300 241.168 1.00 41.75  ? 2967 TYR A C     1 
ATOM   11342 O  O     . TYR A 1 2967 ? 202.657 217.917 240.353 1.00 48.64  ? 2967 TYR A O     1 
ATOM   11343 C  CB    . TYR A 1 2967 ? 202.017 216.810 243.169 1.00 43.38  ? 2967 TYR A CB    1 
ATOM   11344 C  CG    . TYR A 1 2967 ? 202.021 217.665 244.413 1.00 43.30  ? 2967 TYR A CG    1 
ATOM   11345 C  CD1   . TYR A 1 2967 ? 201.005 217.562 245.354 1.00 36.64  ? 2967 TYR A CD1   1 
ATOM   11346 C  CD2   . TYR A 1 2967 ? 203.045 218.572 244.651 1.00 42.42  ? 2967 TYR A CD2   1 
ATOM   11347 C  CE1   . TYR A 1 2967 ? 201.009 218.340 246.493 1.00 34.64  ? 2967 TYR A CE1   1 
ATOM   11348 C  CE2   . TYR A 1 2967 ? 203.056 219.353 245.785 1.00 36.88  ? 2967 TYR A CE2   1 
ATOM   11349 C  CZ    . TYR A 1 2967 ? 202.036 219.234 246.704 1.00 36.16  ? 2967 TYR A CZ    1 
ATOM   11350 O  OH    . TYR A 1 2967 ? 202.047 220.012 247.835 1.00 39.36  ? 2967 TYR A OH    1 
ATOM   11351 N  N     . THR A 1 2968 ? 201.484 219.579 241.322 1.00 42.42  ? 2968 THR A N     1 
ATOM   11352 C  CA    . THR A 1 2968 ? 202.042 220.643 240.501 1.00 41.74  ? 2968 THR A CA    1 
ATOM   11353 C  C     . THR A 1 2968 ? 202.544 221.764 241.401 1.00 41.19  ? 2968 THR A C     1 
ATOM   11354 O  O     . THR A 1 2968 ? 202.503 221.673 242.632 1.00 38.52  ? 2968 THR A O     1 
ATOM   11355 C  CB    . THR A 1 2968 ? 201.005 221.177 239.504 1.00 40.77  ? 2968 THR A CB    1 
ATOM   11356 O  OG1   . THR A 1 2968 ? 199.830 221.592 240.210 1.00 38.76  ? 2968 THR A OG1   1 
ATOM   11357 C  CG2   . THR A 1 2968 ? 200.633 220.105 238.490 1.00 45.01  ? 2968 THR A CG2   1 
ATOM   11358 N  N     . GLY A 1 2969 ? 203.031 222.834 240.770 1.00 43.64  ? 2969 GLY A N     1 
ATOM   11359 C  CA    . GLY A 1 2969 ? 203.485 223.989 241.523 1.00 39.88  ? 2969 GLY A CA    1 
ATOM   11360 C  C     . GLY A 1 2969 ? 202.373 224.686 242.277 1.00 33.39  ? 2969 GLY A C     1 
ATOM   11361 O  O     . GLY A 1 2969 ? 202.602 225.235 243.358 1.00 34.27  ? 2969 GLY A O     1 
ATOM   11362 N  N     . GLU A 1 2970 ? 201.159 224.685 241.720 1.00 41.93  ? 2970 GLU A N     1 
ATOM   11363 C  CA    . GLU A 1 2970 ? 200.032 225.318 242.396 1.00 41.03  ? 2970 GLU A CA    1 
ATOM   11364 C  C     . GLU A 1 2970 ? 199.687 224.595 243.694 1.00 36.92  ? 2970 GLU A C     1 
ATOM   11365 O  O     . GLU A 1 2970 ? 199.349 225.236 244.695 1.00 38.14  ? 2970 GLU A O     1 
ATOM   11366 C  CB    . GLU A 1 2970 ? 198.822 225.363 241.465 1.00 41.02  ? 2970 GLU A CB    1 
ATOM   11367 C  CG    . GLU A 1 2970 ? 199.014 226.259 240.255 1.00 55.68  ? 2970 GLU A CG    1 
ATOM   11368 C  CD    . GLU A 1 2970 ? 199.130 227.723 240.626 1.00 72.01  ? 2970 GLU A CD    1 
ATOM   11369 O  OE1   . GLU A 1 2970 ? 198.505 228.135 241.627 1.00 73.10  ? 2970 GLU A OE1   1 
ATOM   11370 O  OE2   . GLU A 1 2970 ? 199.847 228.463 239.921 1.00 77.01  ? 2970 GLU A OE2   1 
ATOM   11371 N  N     . ASP A 1 2971 ? 199.755 223.263 243.691 1.00 35.78  ? 2971 ASP A N     1 
ATOM   11372 C  CA    . ASP A 1 2971 ? 199.503 222.509 244.915 1.00 35.97  ? 2971 ASP A CA    1 
ATOM   11373 C  C     . ASP A 1 2971 ? 200.540 222.836 245.983 1.00 34.65  ? 2971 ASP A C     1 
ATOM   11374 O  O     . ASP A 1 2971 ? 200.203 222.988 247.164 1.00 36.16  ? 2971 ASP A O     1 
ATOM   11375 C  CB    . ASP A 1 2971 ? 199.499 221.012 244.612 1.00 44.70  ? 2971 ASP A CB    1 
ATOM   11376 C  CG    . ASP A 1 2971 ? 198.310 220.590 243.777 1.00 45.69  ? 2971 ASP A CG    1 
ATOM   11377 O  OD1   . ASP A 1 2971 ? 197.250 221.242 243.878 1.00 51.71  ? 2971 ASP A OD1   1 
ATOM   11378 O  OD2   . ASP A 1 2971 ? 198.436 219.607 243.017 1.00 43.30  ? 2971 ASP A OD2   1 
ATOM   11379 N  N     . PHE A 1 2972 ? 201.807 222.950 245.582 1.00 34.49  ? 2972 PHE A N     1 
ATOM   11380 C  CA    . PHE A 1 2972 ? 202.851 223.320 246.529 1.00 33.87  ? 2972 PHE A CA    1 
ATOM   11381 C  C     . PHE A 1 2972 ? 202.636 224.728 247.062 1.00 33.53  ? 2972 PHE A C     1 
ATOM   11382 O  O     . PHE A 1 2972 ? 202.854 224.988 248.250 1.00 33.69  ? 2972 PHE A O     1 
ATOM   11383 C  CB    . PHE A 1 2972 ? 204.222 223.210 245.872 1.00 28.28  ? 2972 PHE A CB    1 
ATOM   11384 C  CG    . PHE A 1 2972 ? 205.361 223.475 246.808 1.00 32.89  ? 2972 PHE A CG    1 
ATOM   11385 C  CD1   . PHE A 1 2972 ? 205.492 222.746 247.976 1.00 28.04  ? 2972 PHE A CD1   1 
ATOM   11386 C  CD2   . PHE A 1 2972 ? 206.302 224.450 246.522 1.00 35.20  ? 2972 PHE A CD2   1 
ATOM   11387 C  CE1   . PHE A 1 2972 ? 206.536 222.985 248.841 1.00 28.91  ? 2972 PHE A CE1   1 
ATOM   11388 C  CE2   . PHE A 1 2972 ? 207.351 224.691 247.383 1.00 29.29  ? 2972 PHE A CE2   1 
ATOM   11389 C  CZ    . PHE A 1 2972 ? 207.467 223.958 248.544 1.00 33.55  ? 2972 PHE A CZ    1 
ATOM   11390 N  N     . ASP A 1 2973 ? 202.223 225.655 246.197 1.00 30.83  ? 2973 ASP A N     1 
ATOM   11391 C  CA    . ASP A 1 2973 ? 201.941 227.012 246.650 1.00 30.59  ? 2973 ASP A CA    1 
ATOM   11392 C  C     . ASP A 1 2973 ? 200.788 227.032 247.644 1.00 30.28  ? 2973 ASP A C     1 
ATOM   11393 O  O     . ASP A 1 2973 ? 200.829 227.761 248.640 1.00 34.20  ? 2973 ASP A O     1 
ATOM   11394 C  CB    . ASP A 1 2973 ? 201.637 227.912 245.452 1.00 34.85  ? 2973 ASP A CB    1 
ATOM   11395 C  CG    . ASP A 1 2973 ? 202.847 228.132 244.567 1.00 41.70  ? 2973 ASP A CG    1 
ATOM   11396 O  OD1   . ASP A 1 2973 ? 203.894 227.501 244.817 1.00 42.91  ? 2973 ASP A OD1   1 
ATOM   11397 O  OD2   . ASP A 1 2973 ? 202.753 228.939 243.618 1.00 43.58  ? 2973 ASP A OD2   1 
ATOM   11398 N  N     . GLU A 1 2974 ? 199.746 226.237 247.387 1.00 28.54  ? 2974 GLU A N     1 
ATOM   11399 C  CA    . GLU A 1 2974 ? 198.619 226.171 248.313 1.00 29.39  ? 2974 GLU A CA    1 
ATOM   11400 C  C     . GLU A 1 2974 ? 199.038 225.582 249.656 1.00 33.84  ? 2974 GLU A C     1 
ATOM   11401 O  O     . GLU A 1 2974 ? 198.636 226.084 250.713 1.00 32.86  ? 2974 GLU A O     1 
ATOM   11402 C  CB    . GLU A 1 2974 ? 197.483 225.356 247.698 1.00 32.49  ? 2974 GLU A CB    1 
ATOM   11403 C  CG    . GLU A 1 2974 ? 196.158 225.499 248.424 1.00 40.77  ? 2974 GLU A CG    1 
ATOM   11404 C  CD    . GLU A 1 2974 ? 195.847 226.937 248.786 1.00 49.05  ? 2974 GLU A CD    1 
ATOM   11405 O  OE1   . GLU A 1 2974 ? 195.717 227.770 247.865 1.00 51.72  ? 2974 GLU A OE1   1 
ATOM   11406 O  OE2   . GLU A 1 2974 ? 195.733 227.235 249.994 1.00 46.43  ? 2974 GLU A OE2   1 
ATOM   11407 N  N     . ASP A 1 2975 ? 199.845 224.519 249.636 1.00 36.20  ? 2975 ASP A N     1 
ATOM   11408 C  CA    . ASP A 1 2975 ? 200.339 223.952 250.889 1.00 30.64  ? 2975 ASP A CA    1 
ATOM   11409 C  C     . ASP A 1 2975 ? 201.217 224.946 251.636 1.00 30.98  ? 2975 ASP A C     1 
ATOM   11410 O  O     . ASP A 1 2975 ? 201.141 225.055 252.866 1.00 30.17  ? 2975 ASP A O     1 
ATOM   11411 C  CB    . ASP A 1 2975 ? 201.102 222.655 250.618 1.00 35.51  ? 2975 ASP A CB    1 
ATOM   11412 C  CG    . ASP A 1 2975 ? 200.196 221.535 250.152 1.00 49.67  ? 2975 ASP A CG    1 
ATOM   11413 O  OD1   . ASP A 1 2975 ? 199.008 221.530 250.537 1.00 54.20  ? 2975 ASP A OD1   1 
ATOM   11414 O  OD2   . ASP A 1 2975 ? 200.671 220.656 249.405 1.00 51.09  ? 2975 ASP A OD2   1 
ATOM   11415 N  N     . LEU A 1 2976 ? 202.064 225.678 250.907 1.00 30.09  ? 2976 LEU A N     1 
ATOM   11416 C  CA    . LEU A 1 2976 ? 202.895 226.701 251.531 1.00 25.92  ? 2976 LEU A CA    1 
ATOM   11417 C  C     . LEU A 1 2976 ? 202.041 227.782 252.173 1.00 25.17  ? 2976 LEU A C     1 
ATOM   11418 O  O     . LEU A 1 2976 ? 202.336 228.239 253.281 1.00 28.60  ? 2976 LEU A O     1 
ATOM   11419 C  CB    . LEU A 1 2976 ? 203.835 227.313 250.493 1.00 25.00  ? 2976 LEU A CB    1 
ATOM   11420 C  CG    . LEU A 1 2976 ? 205.174 226.613 250.269 1.00 25.08  ? 2976 LEU A CG    1 
ATOM   11421 C  CD1   . LEU A 1 2976 ? 206.008 227.390 249.268 1.00 24.33  ? 2976 LEU A CD1   1 
ATOM   11422 C  CD2   . LEU A 1 2976 ? 205.921 226.450 251.580 1.00 29.83  ? 2976 LEU A CD2   1 
ATOM   11423 N  N     . ARG A 1 2977 ? 200.979 228.208 251.485 1.00 26.42  ? 2977 ARG A N     1 
ATOM   11424 C  CA    . ARG A 1 2977 ? 200.067 229.189 252.061 1.00 30.33  ? 2977 ARG A CA    1 
ATOM   11425 C  C     . ARG A 1 2977 ? 199.411 228.648 253.321 1.00 28.44  ? 2977 ARG A C     1 
ATOM   11426 O  O     . ARG A 1 2977 ? 199.254 229.374 254.307 1.00 30.95  ? 2977 ARG A O     1 
ATOM   11427 C  CB    . ARG A 1 2977 ? 199.007 229.586 251.035 1.00 29.58  ? 2977 ARG A CB    1 
ATOM   11428 C  CG    . ARG A 1 2977 ? 199.524 230.471 249.920 1.00 24.83  ? 2977 ARG A CG    1 
ATOM   11429 C  CD    . ARG A 1 2977 ? 198.416 230.825 248.950 1.00 29.87  ? 2977 ARG A CD    1 
ATOM   11430 N  NE    . ARG A 1 2977 ? 198.904 230.877 247.578 1.00 35.57  ? 2977 ARG A NE    1 
ATOM   11431 C  CZ    . ARG A 1 2977 ? 198.440 230.121 246.593 1.00 37.86  ? 2977 ARG A CZ    1 
ATOM   11432 N  NH1   . ARG A 1 2977 ? 197.466 229.250 246.792 1.00 37.15  ? 2977 ARG A NH1   1 
ATOM   11433 N  NH2   . ARG A 1 2977 ? 198.969 230.242 245.379 1.00 42.50  ? 2977 ARG A NH2   1 
ATOM   11434 N  N     . THR A 1 2978 ? 199.021 227.371 253.308 1.00 30.19  ? 2978 THR A N     1 
ATOM   11435 C  CA    . THR A 1 2978 ? 198.420 226.765 254.492 1.00 27.71  ? 2978 THR A CA    1 
ATOM   11436 C  C     . THR A 1 2978 ? 199.384 226.789 255.673 1.00 26.42  ? 2978 THR A C     1 
ATOM   11437 O  O     . THR A 1 2978 ? 199.020 227.205 256.781 1.00 29.13  ? 2978 THR A O     1 
ATOM   11438 C  CB    . THR A 1 2978 ? 197.989 225.330 254.184 1.00 29.29  ? 2978 THR A CB    1 
ATOM   11439 O  OG1   . THR A 1 2978 ? 197.366 225.281 252.894 1.00 32.64  ? 2978 THR A OG1   1 
ATOM   11440 C  CG2   . THR A 1 2978 ? 197.009 224.830 255.234 1.00 33.28  ? 2978 THR A CG2   1 
ATOM   11441 N  N     . VAL A 1 2979 ? 200.626 226.353 255.449 1.00 27.41  ? 2979 VAL A N     1 
ATOM   11442 C  CA    . VAL A 1 2979 ? 201.609 226.319 256.533 1.00 24.76  ? 2979 VAL A CA    1 
ATOM   11443 C  C     . VAL A 1 2979 ? 201.922 227.726 257.026 1.00 25.42  ? 2979 VAL A C     1 
ATOM   11444 O  O     . VAL A 1 2979 ? 202.052 227.959 258.234 1.00 26.99  ? 2979 VAL A O     1 
ATOM   11445 C  CB    . VAL A 1 2979 ? 202.887 225.581 256.093 1.00 25.94  ? 2979 VAL A CB    1 
ATOM   11446 C  CG1   . VAL A 1 2979 ? 203.770 225.304 257.294 1.00 26.51  ? 2979 VAL A CG1   1 
ATOM   11447 C  CG2   . VAL A 1 2979 ? 202.536 224.271 255.430 1.00 26.34  ? 2979 VAL A CG2   1 
ATOM   11448 N  N     . LEU A 1 2980 ? 202.066 228.681 256.105 1.00 26.07  ? 2980 LEU A N     1 
ATOM   11449 C  CA    . LEU A 1 2980 ? 202.366 230.053 256.506 1.00 22.79  ? 2980 LEU A CA    1 
ATOM   11450 C  C     . LEU A 1 2980 ? 201.220 230.660 257.301 1.00 27.44  ? 2980 LEU A C     1 
ATOM   11451 O  O     . LEU A 1 2980 ? 201.452 231.364 258.289 1.00 34.76  ? 2980 LEU A O     1 
ATOM   11452 C  CB    . LEU A 1 2980 ? 202.684 230.905 255.278 1.00 23.14  ? 2980 LEU A CB    1 
ATOM   11453 C  CG    . LEU A 1 2980 ? 204.017 230.628 254.576 1.00 24.50  ? 2980 LEU A CG    1 
ATOM   11454 C  CD1   . LEU A 1 2980 ? 204.448 231.823 253.746 1.00 30.94  ? 2980 LEU A CD1   1 
ATOM   11455 C  CD2   . LEU A 1 2980 ? 205.095 230.253 255.577 1.00 24.68  ? 2980 LEU A CD2   1 
ATOM   11456 N  N     . ARG A 1 2981 ? 199.977 230.403 256.889 1.00 26.65  ? 2981 ARG A N     1 
ATOM   11457 C  CA    . ARG A 1 2981 ? 198.831 230.889 257.648 1.00 27.17  ? 2981 ARG A CA    1 
ATOM   11458 C  C     . ARG A 1 2981 ? 198.792 230.266 259.036 1.00 26.60  ? 2981 ARG A C     1 
ATOM   11459 O  O     . ARG A 1 2981 ? 198.503 230.949 260.025 1.00 30.59  ? 2981 ARG A O     1 
ATOM   11460 C  CB    . ARG A 1 2981 ? 197.536 230.590 256.894 1.00 26.41  ? 2981 ARG A CB    1 
ATOM   11461 C  CG    . ARG A 1 2981 ? 197.099 231.684 255.936 1.00 36.32  ? 2981 ARG A CG    1 
ATOM   11462 C  CD    . ARG A 1 2981 ? 195.744 231.373 255.321 1.00 32.20  ? 2981 ARG A CD    1 
ATOM   11463 N  NE    . ARG A 1 2981 ? 195.796 230.270 254.371 1.00 35.06  ? 2981 ARG A NE    1 
ATOM   11464 C  CZ    . ARG A 1 2981 ? 195.844 230.419 253.054 1.00 43.07  ? 2981 ARG A CZ    1 
ATOM   11465 N  NH1   . ARG A 1 2981 ? 195.861 231.619 252.496 1.00 40.29  ? 2981 ARG A NH1   1 
ATOM   11466 N  NH2   . ARG A 1 2981 ? 195.874 229.339 252.279 1.00 45.07  ? 2981 ARG A NH2   1 
ATOM   11467 N  N     . ARG A 1 2982 ? 199.083 228.968 259.132 1.00 25.26  ? 2982 ARG A N     1 
ATOM   11468 C  CA    . ARG A 1 2982 ? 199.007 228.297 260.423 1.00 24.62  ? 2982 ARG A CA    1 
ATOM   11469 C  C     . ARG A 1 2982 ? 200.109 228.767 261.366 1.00 26.26  ? 2982 ARG A C     1 
ATOM   11470 O  O     . ARG A 1 2982 ? 199.872 228.938 262.568 1.00 29.43  ? 2982 ARG A O     1 
ATOM   11471 C  CB    . ARG A 1 2982 ? 199.070 226.785 260.231 1.00 25.23  ? 2982 ARG A CB    1 
ATOM   11472 C  CG    . ARG A 1 2982 ? 197.788 226.176 259.695 1.00 24.12  ? 2982 ARG A CG    1 
ATOM   11473 C  CD    . ARG A 1 2982 ? 197.936 224.680 259.508 1.00 28.14  ? 2982 ARG A CD    1 
ATOM   11474 N  NE    . ARG A 1 2982 ? 198.334 224.019 260.745 1.00 21.86  ? 2982 ARG A NE    1 
ATOM   11475 C  CZ    . ARG A 1 2982 ? 198.726 222.755 260.824 1.00 23.53  ? 2982 ARG A CZ    1 
ATOM   11476 N  NH1   . ARG A 1 2982 ? 198.790 221.983 259.752 1.00 26.29  ? 2982 ARG A NH1   1 
ATOM   11477 N  NH2   . ARG A 1 2982 ? 199.063 222.253 262.007 1.00 23.72  ? 2982 ARG A NH2   1 
ATOM   11478 N  N     . SER A 1 2983 ? 201.318 228.980 260.848 1.00 27.49  ? 2983 SER A N     1 
ATOM   11479 C  CA    . SER A 1 2983 ? 202.457 229.319 261.691 1.00 25.56  ? 2983 SER A CA    1 
ATOM   11480 C  C     . SER A 1 2983 ? 202.683 230.818 261.841 1.00 27.01  ? 2983 SER A C     1 
ATOM   11481 O  O     . SER A 1 2983 ? 203.531 231.219 262.644 1.00 28.51  ? 2983 SER A O     1 
ATOM   11482 C  CB    . SER A 1 2983 ? 203.732 228.671 261.140 1.00 23.56  ? 2983 SER A CB    1 
ATOM   11483 O  OG    . SER A 1 2983 ? 203.992 229.099 259.815 1.00 27.79  ? 2983 SER A OG    1 
ATOM   11484 N  N     . GLY A 1 2984 ? 201.954 231.650 261.104 1.00 25.41  ? 2984 GLY A N     1 
ATOM   11485 C  CA    . GLY A 1 2984 ? 202.156 233.081 261.175 1.00 24.41  ? 2984 GLY A CA    1 
ATOM   11486 C  C     . GLY A 1 2984 ? 200.941 233.835 261.665 1.00 35.46  ? 2984 GLY A C     1 
ATOM   11487 O  O     . GLY A 1 2984 ? 201.065 234.921 262.240 1.00 42.24  ? 2984 GLY A O     1 
ATOM   11488 N  N     . CYS A 1 2985 ? 199.756 233.272 261.440 1.00 33.64  ? 2985 CYS A N     1 
ATOM   11489 C  CA    . CYS A 1 2985 ? 198.513 233.882 261.892 1.00 30.96  ? 2985 CYS A CA    1 
ATOM   11490 C  C     . CYS A 1 2985 ? 197.945 233.224 263.139 1.00 33.00  ? 2985 CYS A C     1 
ATOM   11491 O  O     . CYS A 1 2985 ? 197.367 233.917 263.982 1.00 38.59  ? 2985 CYS A O     1 
ATOM   11492 C  CB    . CYS A 1 2985 ? 197.461 233.831 260.780 1.00 30.22  ? 2985 CYS A CB    1 
ATOM   11493 S  SG    . CYS A 1 2985 ? 197.984 234.561 259.214 1.00 50.46  ? 2985 CYS A SG    1 
ATOM   11494 N  N     . LYS A 1 2986 ? 198.092 231.909 263.274 1.00 31.65  ? 2986 LYS A N     1 
ATOM   11495 C  CA    . LYS A 1 2986 ? 197.564 231.174 264.414 1.00 29.78  ? 2986 LYS A CA    1 
ATOM   11496 C  C     . LYS A 1 2986 ? 198.606 230.928 265.495 1.00 32.21  ? 2986 LYS A C     1 
ATOM   11497 O  O     . LYS A 1 2986 ? 198.282 230.312 266.516 1.00 34.61  ? 2986 LYS A O     1 
ATOM   11498 C  CB    . LYS A 1 2986 ? 196.974 229.835 263.954 1.00 27.82  ? 2986 LYS A CB    1 
ATOM   11499 C  CG    . LYS A 1 2986 ? 196.103 229.898 262.699 1.00 30.12  ? 2986 LYS A CG    1 
ATOM   11500 C  CD    . LYS A 1 2986 ? 195.162 231.098 262.698 1.00 33.33  ? 2986 LYS A CD    1 
ATOM   11501 C  CE    . LYS A 1 2986 ? 194.627 231.373 261.303 1.00 40.01  ? 2986 LYS A CE    1 
ATOM   11502 N  NZ    . LYS A 1 2986 ? 193.423 232.249 261.327 1.00 40.02  ? 2986 LYS A NZ    1 
ATOM   11503 N  N     . ASN A 1 2987 ? 199.840 231.401 265.301 1.00 30.39  ? 2987 ASN A N     1 
ATOM   11504 C  CA    . ASN A 1 2987 ? 200.923 231.236 266.274 1.00 28.16  ? 2987 ASN A CA    1 
ATOM   11505 C  C     . ASN A 1 2987 ? 201.136 229.767 266.632 1.00 33.70  ? 2987 ASN A C     1 
ATOM   11506 O  O     . ASN A 1 2987 ? 201.280 229.407 267.801 1.00 30.66  ? 2987 ASN A O     1 
ATOM   11507 C  CB    . ASN A 1 2987 ? 200.668 232.070 267.532 1.00 25.53  ? 2987 ASN A CB    1 
ATOM   11508 C  CG    . ASN A 1 2987 ? 201.932 232.323 268.326 1.00 28.33  ? 2987 ASN A CG    1 
ATOM   11509 O  OD1   . ASN A 1 2987 ? 202.945 232.753 267.779 1.00 30.55  ? 2987 ASN A OD1   1 
ATOM   11510 N  ND2   . ASN A 1 2987 ? 201.878 232.055 269.625 1.00 26.37  ? 2987 ASN A ND2   1 
ATOM   11511 N  N     . GLU A 1 2988 ? 201.155 228.910 265.617 1.00 30.57  ? 2988 GLU A N     1 
ATOM   11512 C  CA    . GLU A 1 2988 ? 201.332 227.476 265.800 1.00 25.31  ? 2988 GLU A CA    1 
ATOM   11513 C  C     . GLU A 1 2988 ? 202.724 227.085 265.323 1.00 25.04  ? 2988 GLU A C     1 
ATOM   11514 O  O     . GLU A 1 2988 ? 203.066 227.300 264.157 1.00 25.60  ? 2988 GLU A O     1 
ATOM   11515 C  CB    . GLU A 1 2988 ? 200.262 226.693 265.042 1.00 25.14  ? 2988 GLU A CB    1 
ATOM   11516 C  CG    . GLU A 1 2988 ? 200.442 225.186 265.089 1.00 28.43  ? 2988 GLU A CG    1 
ATOM   11517 C  CD    . GLU A 1 2988 ? 199.427 224.454 264.236 1.00 38.30  ? 2988 GLU A CD    1 
ATOM   11518 O  OE1   . GLU A 1 2988 ? 199.175 223.261 264.499 1.00 36.26  ? 2988 GLU A OE1   1 
ATOM   11519 O  OE2   . GLU A 1 2988 ? 198.879 225.072 263.298 1.00 34.51  ? 2988 GLU A OE2   1 
ATOM   11520 N  N     . LYS A 1 2989 ? 203.519 226.514 266.224 1.00 24.94  ? 2989 LYS A N     1 
ATOM   11521 C  CA    . LYS A 1 2989 ? 204.848 226.043 265.862 1.00 19.21  ? 2989 LYS A CA    1 
ATOM   11522 C  C     . LYS A 1 2989 ? 204.724 224.800 264.990 1.00 18.43  ? 2989 LYS A C     1 
ATOM   11523 O  O     . LYS A 1 2989 ? 204.122 223.804 265.400 1.00 22.74  ? 2989 LYS A O     1 
ATOM   11524 C  CB    . LYS A 1 2989 ? 205.663 225.745 267.117 1.00 15.86  ? 2989 LYS A CB    1 
ATOM   11525 C  CG    . LYS A 1 2989 ? 205.837 226.936 268.039 1.00 20.86  ? 2989 LYS A CG    1 
ATOM   11526 C  CD    . LYS A 1 2989 ? 206.739 226.593 269.211 1.00 24.41  ? 2989 LYS A CD    1 
ATOM   11527 C  CE    . LYS A 1 2989 ? 206.199 225.409 269.994 1.00 32.88  ? 2989 LYS A CE    1 
ATOM   11528 N  NZ    . LYS A 1 2989 ? 207.106 225.023 271.111 1.00 29.68  ? 2989 LYS A NZ    1 
ATOM   11529 N  N     . ILE A 1 2990 ? 205.295 224.858 263.789 1.00 16.58  ? 2990 ILE A N     1 
ATOM   11530 C  CA    . ILE A 1 2990 ? 205.112 223.818 262.785 1.00 13.32  ? 2990 ILE A CA    1 
ATOM   11531 C  C     . ILE A 1 2990 ? 206.474 223.346 262.300 1.00 13.33  ? 2990 ILE A C     1 
ATOM   11532 O  O     . ILE A 1 2990 ? 207.304 224.158 261.875 1.00 14.37  ? 2990 ILE A O     1 
ATOM   11533 C  CB    . ILE A 1 2990 ? 204.266 224.319 261.601 1.00 14.49  ? 2990 ILE A CB    1 
ATOM   11534 C  CG1   . ILE A 1 2990 ? 202.799 224.442 262.011 1.00 17.22  ? 2990 ILE A CG1   1 
ATOM   11535 C  CG2   . ILE A 1 2990 ? 204.417 223.390 260.405 1.00 11.92  ? 2990 ILE A CG2   1 
ATOM   11536 C  CD1   . ILE A 1 2990 ? 201.867 224.697 260.857 1.00 20.88  ? 2990 ILE A CD1   1 
ATOM   11537 N  N     . ALA A 1 2991 ? 206.689 222.033 262.352 1.00 14.16  ? 2991 ALA A N     1 
ATOM   11538 C  CA    . ALA A 1 2991 ? 207.847 221.390 261.739 1.00 12.67  ? 2991 ALA A CA    1 
ATOM   11539 C  C     . ALA A 1 2991 ? 207.427 220.909 260.356 1.00 12.23  ? 2991 ALA A C     1 
ATOM   11540 O  O     . ALA A 1 2991 ? 206.709 219.915 260.218 1.00 10.55  ? 2991 ALA A O     1 
ATOM   11541 C  CB    . ALA A 1 2991 ? 208.354 220.245 262.607 1.00 9.11   ? 2991 ALA A CB    1 
ATOM   11542 N  N     . PHE A 1 2992 ? 207.862 221.632 259.331 1.00 12.45  ? 2992 PHE A N     1 
ATOM   11543 C  CA    . PHE A 1 2992 ? 207.574 221.303 257.938 1.00 11.55  ? 2992 PHE A CA    1 
ATOM   11544 C  C     . PHE A 1 2992 ? 208.663 220.346 257.471 1.00 15.43  ? 2992 PHE A C     1 
ATOM   11545 O  O     . PHE A 1 2992 ? 209.800 220.752 257.227 1.00 17.73  ? 2992 PHE A O     1 
ATOM   11546 C  CB    . PHE A 1 2992 ? 207.528 222.573 257.097 1.00 11.80  ? 2992 PHE A CB    1 
ATOM   11547 C  CG    . PHE A 1 2992 ? 207.087 222.361 255.673 1.00 14.86  ? 2992 PHE A CG    1 
ATOM   11548 C  CD1   . PHE A 1 2992 ? 206.566 221.149 255.257 1.00 20.54  ? 2992 PHE A CD1   1 
ATOM   11549 C  CD2   . PHE A 1 2992 ? 207.202 223.385 254.751 1.00 14.12  ? 2992 PHE A CD2   1 
ATOM   11550 C  CE1   . PHE A 1 2992 ? 206.166 220.966 253.949 1.00 24.86  ? 2992 PHE A CE1   1 
ATOM   11551 C  CE2   . PHE A 1 2992 ? 206.804 223.207 253.444 1.00 16.26  ? 2992 PHE A CE2   1 
ATOM   11552 C  CZ    . PHE A 1 2992 ? 206.286 221.997 253.044 1.00 25.96  ? 2992 PHE A CZ    1 
ATOM   11553 N  N     . ILE A 1 2993 ? 208.319 219.068 257.351 1.00 14.23  ? 2993 ILE A N     1 
ATOM   11554 C  CA    . ILE A 1 2993 ? 209.277 218.041 256.963 1.00 11.04  ? 2993 ILE A CA    1 
ATOM   11555 C  C     . ILE A 1 2993 ? 209.139 217.788 255.468 1.00 15.97  ? 2993 ILE A C     1 
ATOM   11556 O  O     . ILE A 1 2993 ? 208.067 217.407 254.989 1.00 21.66  ? 2993 ILE A O     1 
ATOM   11557 C  CB    . ILE A 1 2993 ? 209.064 216.750 257.767 1.00 11.55  ? 2993 ILE A CB    1 
ATOM   11558 C  CG1   . ILE A 1 2993 ? 209.172 217.042 259.264 1.00 9.87   ? 2993 ILE A CG1   1 
ATOM   11559 C  CG2   . ILE A 1 2993 ? 210.071 215.692 257.352 1.00 17.67  ? 2993 ILE A CG2   1 
ATOM   11560 C  CD1   . ILE A 1 2993 ? 209.184 215.809 260.129 1.00 9.49   ? 2993 ILE A CD1   1 
ATOM   11561 N  N     . MET A 1 2994 ? 210.225 218.001 254.732 1.00 15.84  ? 2994 MET A N     1 
ATOM   11562 C  CA    . MET A 1 2994 ? 210.242 217.863 253.286 1.00 17.05  ? 2994 MET A CA    1 
ATOM   11563 C  C     . MET A 1 2994 ? 211.373 216.930 252.883 1.00 23.64  ? 2994 MET A C     1 
ATOM   11564 O  O     . MET A 1 2994 ? 212.486 217.029 253.407 1.00 28.36  ? 2994 MET A O     1 
ATOM   11565 C  CB    . MET A 1 2994 ? 210.419 219.223 252.607 1.00 17.06  ? 2994 MET A CB    1 
ATOM   11566 C  CG    . MET A 1 2994 ? 210.327 219.187 251.096 1.00 35.57  ? 2994 MET A CG    1 
ATOM   11567 S  SD    . MET A 1 2994 ? 210.536 220.827 250.384 1.00 64.45  ? 2994 MET A SD    1 
ATOM   11568 C  CE    . MET A 1 2994 ? 208.988 221.583 250.853 1.00 32.21  ? 2994 MET A CE    1 
ATOM   11569 N  N     . ASP A 1 2995 ? 211.085 216.031 251.950 1.00 27.81  ? 2995 ASP A N     1 
ATOM   11570 C  CA    . ASP A 1 2995 ? 212.062 215.084 251.442 1.00 26.73  ? 2995 ASP A CA    1 
ATOM   11571 C  C     . ASP A 1 2995 ? 212.442 215.460 250.016 1.00 32.29  ? 2995 ASP A C     1 
ATOM   11572 O  O     . ASP A 1 2995 ? 211.667 216.088 249.289 1.00 38.63  ? 2995 ASP A O     1 
ATOM   11573 C  CB    . ASP A 1 2995 ? 211.513 213.653 251.500 1.00 28.50  ? 2995 ASP A CB    1 
ATOM   11574 C  CG    . ASP A 1 2995 ? 212.462 212.636 250.900 1.00 38.34  ? 2995 ASP A CG    1 
ATOM   11575 O  OD1   . ASP A 1 2995 ? 213.472 212.303 251.554 1.00 35.08  ? 2995 ASP A OD1   1 
ATOM   11576 O  OD2   . ASP A 1 2995 ? 212.197 212.165 249.777 1.00 40.66  ? 2995 ASP A OD2   1 
ATOM   11577 N  N     . GLU A 1 2996 ? 213.662 215.081 249.625 1.00 31.06  ? 2996 GLU A N     1 
ATOM   11578 C  CA    . GLU A 1 2996 ? 214.163 215.443 248.304 1.00 33.17  ? 2996 GLU A CA    1 
ATOM   11579 C  C     . GLU A 1 2996 ? 213.305 214.859 247.190 1.00 32.36  ? 2996 GLU A C     1 
ATOM   11580 O  O     . GLU A 1 2996 ? 213.248 215.424 246.092 1.00 35.98  ? 2996 GLU A O     1 
ATOM   11581 C  CB    . GLU A 1 2996 ? 215.615 214.991 248.154 1.00 40.45  ? 2996 GLU A CB    1 
ATOM   11582 C  CG    . GLU A 1 2996 ? 215.819 213.492 248.307 1.00 39.28  ? 2996 GLU A CG    1 
ATOM   11583 C  CD    . GLU A 1 2996 ? 217.048 212.998 247.577 1.00 35.47  ? 2996 GLU A CD    1 
ATOM   11584 O  OE1   . GLU A 1 2996 ? 217.741 213.826 246.949 1.00 40.90  ? 2996 GLU A OE1   1 
ATOM   11585 O  OE2   . GLU A 1 2996 ? 217.320 211.781 247.625 1.00 32.22  ? 2996 GLU A OE2   1 
ATOM   11586 N  N     . SER A 1 2997 ? 212.632 213.736 247.445 1.00 37.72  ? 2997 SER A N     1 
ATOM   11587 C  CA    . SER A 1 2997 ? 211.753 213.148 246.442 1.00 41.02  ? 2997 SER A CA    1 
ATOM   11588 C  C     . SER A 1 2997 ? 210.442 213.908 246.290 1.00 41.76  ? 2997 SER A C     1 
ATOM   11589 O  O     . SER A 1 2997 ? 209.756 213.730 245.279 1.00 49.10  ? 2997 SER A O     1 
ATOM   11590 C  CB    . SER A 1 2997 ? 211.461 211.687 246.785 1.00 40.12  ? 2997 SER A CB    1 
ATOM   11591 O  OG    . SER A 1 2997 ? 210.827 211.576 248.047 1.00 43.90  ? 2997 SER A OG    1 
ATOM   11592 N  N     . ASN A 1 2998 ? 210.083 214.747 247.262 1.00 38.07  ? 2998 ASN A N     1 
ATOM   11593 C  CA    . ASN A 1 2998 ? 208.888 215.572 247.153 1.00 36.93  ? 2998 ASN A CA    1 
ATOM   11594 C  C     . ASN A 1 2998 ? 209.037 216.696 246.138 1.00 40.76  ? 2998 ASN A C     1 
ATOM   11595 O  O     . ASN A 1 2998 ? 208.042 217.354 245.817 1.00 48.45  ? 2998 ASN A O     1 
ATOM   11596 C  CB    . ASN A 1 2998 ? 208.530 216.168 248.517 1.00 35.12  ? 2998 ASN A CB    1 
ATOM   11597 C  CG    . ASN A 1 2998 ? 208.142 215.114 249.528 1.00 40.12  ? 2998 ASN A CG    1 
ATOM   11598 O  OD1   . ASN A 1 2998 ? 208.120 213.922 249.223 1.00 40.40  ? 2998 ASN A OD1   1 
ATOM   11599 N  ND2   . ASN A 1 2998 ? 207.832 215.548 250.744 1.00 31.02  ? 2998 ASN A ND2   1 
ATOM   11600 N  N     . VAL A 1 2999 ? 210.245 216.927 245.630 1.00 41.94  ? 2999 VAL A N     1 
ATOM   11601 C  CA    . VAL A 1 2999 ? 210.512 218.014 244.690 1.00 43.00  ? 2999 VAL A CA    1 
ATOM   11602 C  C     . VAL A 1 2999 ? 210.267 217.483 243.280 1.00 51.01  ? 2999 VAL A C     1 
ATOM   11603 O  O     . VAL A 1 2999 ? 210.811 216.450 242.887 1.00 55.57  ? 2999 VAL A O     1 
ATOM   11604 C  CB    . VAL A 1 2999 ? 211.931 218.560 244.846 1.00 43.83  ? 2999 VAL A CB    1 
ATOM   11605 C  CG1   . VAL A 1 2999 ? 212.315 219.365 243.619 1.00 48.89  ? 2999 VAL A CG1   1 
ATOM   11606 C  CG2   . VAL A 1 2999 ? 212.032 219.404 246.106 1.00 36.77  ? 2999 VAL A CG2   1 
ATOM   11607 N  N     . LEU A 1 3000 ? 209.446 218.196 242.512 1.00 47.31  ? 3000 LEU A N     1 
ATOM   11608 C  CA    . LEU A 1 3000 ? 209.160 217.846 241.128 1.00 50.45  ? 3000 LEU A CA    1 
ATOM   11609 C  C     . LEU A 1 3000 ? 209.573 218.934 240.146 1.00 58.51  ? 3000 LEU A C     1 
ATOM   11610 O  O     . LEU A 1 3000 ? 209.463 218.729 238.933 1.00 63.83  ? 3000 LEU A O     1 
ATOM   11611 C  CB    . LEU A 1 3000 ? 207.668 217.543 240.965 1.00 48.96  ? 3000 LEU A CB    1 
ATOM   11612 C  CG    . LEU A 1 3000 ? 207.054 216.640 242.035 1.00 56.02  ? 3000 LEU A CG    1 
ATOM   11613 C  CD1   . LEU A 1 3000 ? 205.536 216.674 241.959 1.00 54.72  ? 3000 LEU A CD1   1 
ATOM   11614 C  CD2   . LEU A 1 3000 ? 207.568 215.216 241.897 1.00 53.14  ? 3000 LEU A CD2   1 
ATOM   11615 N  N     . ASP A 1 3001 ? 210.047 220.077 240.636 1.00 54.90  ? 3001 ASP A N     1 
ATOM   11616 C  CA    . ASP A 1 3001 ? 210.377 221.212 239.787 1.00 56.49  ? 3001 ASP A CA    1 
ATOM   11617 C  C     . ASP A 1 3001 ? 211.315 222.131 240.557 1.00 50.85  ? 3001 ASP A C     1 
ATOM   11618 O  O     . ASP A 1 3001 ? 211.445 222.032 241.780 1.00 44.20  ? 3001 ASP A O     1 
ATOM   11619 C  CB    . ASP A 1 3001 ? 209.114 221.962 239.346 1.00 54.10  ? 3001 ASP A CB    1 
ATOM   11620 C  CG    . ASP A 1 3001 ? 209.389 223.008 238.279 1.00 61.66  ? 3001 ASP A CG    1 
ATOM   11621 O  OD1   . ASP A 1 3001 ? 210.564 223.180 237.892 1.00 65.75  ? 3001 ASP A OD1   1 
ATOM   11622 O  OD2   . ASP A 1 3001 ? 208.425 223.661 237.829 1.00 65.56  ? 3001 ASP A OD2   1 
ATOM   11623 N  N     . SER A 1 3002 ? 211.977 223.026 239.819 1.00 48.70  ? 3002 SER A N     1 
ATOM   11624 C  CA    . SER A 1 3002 ? 212.859 224.002 240.448 1.00 50.85  ? 3002 SER A CA    1 
ATOM   11625 C  C     . SER A 1 3002 ? 212.089 225.090 241.186 1.00 45.14  ? 3002 SER A C     1 
ATOM   11626 O  O     . SER A 1 3002 ? 212.663 225.755 242.055 1.00 48.19  ? 3002 SER A O     1 
ATOM   11627 C  CB    . SER A 1 3002 ? 213.778 224.633 239.401 1.00 48.85  ? 3002 SER A CB    1 
ATOM   11628 O  OG    . SER A 1 3002 ? 214.652 225.576 239.996 1.00 43.27  ? 3002 SER A OG    1 
ATOM   11629 N  N     . GLY A 1 3003 ? 210.812 225.293 240.855 1.00 37.37  ? 3003 GLY A N     1 
ATOM   11630 C  CA    . GLY A 1 3003 ? 210.014 226.265 241.585 1.00 33.61  ? 3003 GLY A CA    1 
ATOM   11631 C  C     . GLY A 1 3003 ? 209.842 225.890 243.043 1.00 36.84  ? 3003 GLY A C     1 
ATOM   11632 O  O     . GLY A 1 3003 ? 209.761 226.762 243.914 1.00 43.07  ? 3003 GLY A O     1 
ATOM   11633 N  N     . PHE A 1 3004 ? 209.777 224.587 243.326 1.00 34.94  ? 3004 PHE A N     1 
ATOM   11634 C  CA    . PHE A 1 3004 ? 209.811 224.109 244.703 1.00 35.97  ? 3004 PHE A CA    1 
ATOM   11635 C  C     . PHE A 1 3004 ? 211.012 224.684 245.439 1.00 34.64  ? 3004 PHE A C     1 
ATOM   11636 O  O     . PHE A 1 3004 ? 210.875 225.280 246.514 1.00 35.12  ? 3004 PHE A O     1 
ATOM   11637 C  CB    . PHE A 1 3004 ? 209.874 222.580 244.715 1.00 43.59  ? 3004 PHE A CB    1 
ATOM   11638 C  CG    . PHE A 1 3004 ? 208.634 221.906 244.199 1.00 41.89  ? 3004 PHE A CG    1 
ATOM   11639 C  CD1   . PHE A 1 3004 ? 207.538 221.712 245.016 1.00 36.49  ? 3004 PHE A CD1   1 
ATOM   11640 C  CD2   . PHE A 1 3004 ? 208.557 221.493 242.884 1.00 49.96  ? 3004 PHE A CD2   1 
ATOM   11641 C  CE1   . PHE A 1 3004 ? 206.404 221.086 244.536 1.00 40.46  ? 3004 PHE A CE1   1 
ATOM   11642 C  CE2   . PHE A 1 3004 ? 207.422 220.877 242.398 1.00 52.88  ? 3004 PHE A CE2   1 
ATOM   11643 C  CZ    . PHE A 1 3004 ? 206.344 220.675 243.225 1.00 48.69  ? 3004 PHE A CZ    1 
ATOM   11644 N  N     . LEU A 1 3005 ? 212.202 224.531 244.852 1.00 37.97  ? 3005 LEU A N     1 
ATOM   11645 C  CA    . LEU A 1 3005 ? 213.416 225.024 245.489 1.00 34.82  ? 3005 LEU A CA    1 
ATOM   11646 C  C     . LEU A 1 3005 ? 213.444 226.541 245.560 1.00 31.56  ? 3005 LEU A C     1 
ATOM   11647 O  O     . LEU A 1 3005 ? 213.949 227.091 246.537 1.00 35.31  ? 3005 LEU A O     1 
ATOM   11648 C  CB    . LEU A 1 3005 ? 214.660 224.511 244.764 1.00 42.05  ? 3005 LEU A CB    1 
ATOM   11649 C  CG    . LEU A 1 3005 ? 215.181 223.115 245.119 1.00 42.29  ? 3005 LEU A CG    1 
ATOM   11650 C  CD1   . LEU A 1 3005 ? 215.622 223.054 246.573 1.00 36.10  ? 3005 LEU A CD1   1 
ATOM   11651 C  CD2   . LEU A 1 3005 ? 214.160 222.046 244.831 1.00 38.79  ? 3005 LEU A CD2   1 
ATOM   11652 N  N     . GLU A 1 3006 ? 212.919 227.233 244.548 1.00 29.58  ? 3006 GLU A N     1 
ATOM   11653 C  CA    . GLU A 1 3006 ? 212.878 228.693 244.602 1.00 26.12  ? 3006 GLU A CA    1 
ATOM   11654 C  C     . GLU A 1 3006 ? 212.038 229.179 245.775 1.00 28.05  ? 3006 GLU A C     1 
ATOM   11655 O  O     . GLU A 1 3006 ? 212.485 230.015 246.578 1.00 28.50  ? 3006 GLU A O     1 
ATOM   11656 C  CB    . GLU A 1 3006 ? 212.335 229.248 243.285 1.00 25.41  ? 3006 GLU A CB    1 
ATOM   11657 C  CG    . GLU A 1 3006 ? 213.242 229.000 242.100 1.00 36.58  ? 3006 GLU A CG    1 
ATOM   11658 C  CD    . GLU A 1 3006 ? 214.542 229.764 242.214 1.00 43.25  ? 3006 GLU A CD    1 
ATOM   11659 O  OE1   . GLU A 1 3006 ? 214.534 230.868 242.797 1.00 36.67  ? 3006 GLU A OE1   1 
ATOM   11660 O  OE2   . GLU A 1 3006 ? 215.581 229.254 241.747 1.00 39.56  ? 3006 GLU A OE2   1 
ATOM   11661 N  N     . ARG A 1 3007 ? 210.815 228.658 245.897 1.00 27.43  ? 3007 ARG A N     1 
ATOM   11662 C  CA    . ARG A 1 3007 ? 209.940 229.083 246.981 1.00 26.51  ? 3007 ARG A CA    1 
ATOM   11663 C  C     . ARG A 1 3007 ? 210.514 228.689 248.336 1.00 25.78  ? 3007 ARG A C     1 
ATOM   11664 O  O     . ARG A 1 3007 ? 210.469 229.476 249.290 1.00 25.08  ? 3007 ARG A O     1 
ATOM   11665 C  CB    . ARG A 1 3007 ? 208.542 228.499 246.783 1.00 27.61  ? 3007 ARG A CB    1 
ATOM   11666 C  CG    . ARG A 1 3007 ? 207.890 228.948 245.485 1.00 22.49  ? 3007 ARG A CG    1 
ATOM   11667 C  CD    . ARG A 1 3007 ? 207.563 230.430 245.527 1.00 32.80  ? 3007 ARG A CD    1 
ATOM   11668 N  NE    . ARG A 1 3007 ? 206.952 230.900 244.290 1.00 48.69  ? 3007 ARG A NE    1 
ATOM   11669 C  CZ    . ARG A 1 3007 ? 205.647 230.915 244.055 1.00 45.32  ? 3007 ARG A CZ    1 
ATOM   11670 N  NH1   . ARG A 1 3007 ? 204.778 230.505 244.961 1.00 37.35  ? 3007 ARG A NH1   1 
ATOM   11671 N  NH2   . ARG A 1 3007 ? 205.205 231.359 242.882 1.00 48.51  ? 3007 ARG A NH2   1 
ATOM   11672 N  N     . MET A 1 3008 ? 211.079 227.482 248.434 1.00 28.29  ? 3008 MET A N     1 
ATOM   11673 C  CA    . MET A 1 3008 ? 211.661 227.047 249.699 1.00 23.77  ? 3008 MET A CA    1 
ATOM   11674 C  C     . MET A 1 3008 ? 212.880 227.883 250.064 1.00 24.52  ? 3008 MET A C     1 
ATOM   11675 O  O     . MET A 1 3008 ? 213.093 228.192 251.237 1.00 28.68  ? 3008 MET A O     1 
ATOM   11676 C  CB    . MET A 1 3008 ? 212.020 225.565 249.631 1.00 24.35  ? 3008 MET A CB    1 
ATOM   11677 C  CG    . MET A 1 3008 ? 210.820 224.644 249.741 1.00 27.21  ? 3008 MET A CG    1 
ATOM   11678 S  SD    . MET A 1 3008 ? 209.688 225.128 251.059 1.00 39.35  ? 3008 MET A SD    1 
ATOM   11679 C  CE    . MET A 1 3008 ? 210.714 224.872 252.503 1.00 26.50  ? 3008 MET A CE    1 
ATOM   11680 N  N     . ASN A 1 3009 ? 213.690 228.257 249.072 1.00 26.98  ? 3009 ASN A N     1 
ATOM   11681 C  CA    . ASN A 1 3009 ? 214.854 229.100 249.319 1.00 20.98  ? 3009 ASN A CA    1 
ATOM   11682 C  C     . ASN A 1 3009 ? 214.431 230.458 249.859 1.00 21.20  ? 3009 ASN A C     1 
ATOM   11683 O  O     . ASN A 1 3009 ? 214.984 230.950 250.852 1.00 21.72  ? 3009 ASN A O     1 
ATOM   11684 C  CB    . ASN A 1 3009 ? 215.649 229.251 248.019 1.00 20.65  ? 3009 ASN A CB    1 
ATOM   11685 C  CG    . ASN A 1 3009 ? 216.952 229.996 248.204 1.00 28.14  ? 3009 ASN A CG    1 
ATOM   11686 O  OD1   . ASN A 1 3009 ? 217.897 229.477 248.794 1.00 24.14  ? 3009 ASN A OD1   1 
ATOM   11687 N  ND2   . ASN A 1 3009 ? 217.016 231.217 247.686 1.00 24.52  ? 3009 ASN A ND2   1 
ATOM   11688 N  N     . THR A 1 3010 ? 213.428 231.069 249.222 1.00 29.79  ? 3010 THR A N     1 
ATOM   11689 C  CA    . THR A 1 3010 ? 212.938 232.359 249.698 1.00 25.71  ? 3010 THR A CA    1 
ATOM   11690 C  C     . THR A 1 3010 ? 212.373 232.248 251.110 1.00 22.40  ? 3010 THR A C     1 
ATOM   11691 O  O     . THR A 1 3010 ? 212.641 233.105 251.962 1.00 25.16  ? 3010 THR A O     1 
ATOM   11692 C  CB    . THR A 1 3010 ? 211.882 232.909 248.740 1.00 27.28  ? 3010 THR A CB    1 
ATOM   11693 O  OG1   . THR A 1 3010 ? 212.320 232.728 247.388 1.00 25.10  ? 3010 THR A OG1   1 
ATOM   11694 C  CG2   . THR A 1 3010 ? 211.656 234.388 248.996 1.00 25.33  ? 3010 THR A CG2   1 
ATOM   11695 N  N     . LEU A 1 3011 ? 211.599 231.193 251.383 1.00 21.64  ? 3011 LEU A N     1 
ATOM   11696 C  CA    . LEU A 1 3011 ? 211.011 231.031 252.709 1.00 20.39  ? 3011 LEU A CA    1 
ATOM   11697 C  C     . LEU A 1 3011 ? 212.077 230.785 253.771 1.00 20.87  ? 3011 LEU A C     1 
ATOM   11698 O  O     . LEU A 1 3011 ? 211.988 231.317 254.883 1.00 20.47  ? 3011 LEU A O     1 
ATOM   11699 C  CB    . LEU A 1 3011 ? 209.992 229.892 252.696 1.00 19.67  ? 3011 LEU A CB    1 
ATOM   11700 C  CG    . LEU A 1 3011 ? 209.468 229.424 254.055 1.00 20.61  ? 3011 LEU A CG    1 
ATOM   11701 C  CD1   . LEU A 1 3011 ? 208.683 230.533 254.731 1.00 19.33  ? 3011 LEU A CD1   1 
ATOM   11702 C  CD2   . LEU A 1 3011 ? 208.612 228.180 253.900 1.00 24.39  ? 3011 LEU A CD2   1 
ATOM   11703 N  N     . LEU A 1 3012 ? 213.088 229.973 253.453 1.00 19.38  ? 3012 LEU A N     1 
ATOM   11704 C  CA    . LEU A 1 3012 ? 214.152 229.699 254.412 1.00 16.89  ? 3012 LEU A CA    1 
ATOM   11705 C  C     . LEU A 1 3012 ? 214.958 230.952 254.717 1.00 20.97  ? 3012 LEU A C     1 
ATOM   11706 O  O     . LEU A 1 3012 ? 215.320 231.199 255.873 1.00 20.91  ? 3012 LEU A O     1 
ATOM   11707 C  CB    . LEU A 1 3012 ? 215.069 228.597 253.881 1.00 16.32  ? 3012 LEU A CB    1 
ATOM   11708 C  CG    . LEU A 1 3012 ? 214.507 227.178 253.816 1.00 13.19  ? 3012 LEU A CG    1 
ATOM   11709 C  CD1   . LEU A 1 3012 ? 215.489 226.243 253.134 1.00 14.27  ? 3012 LEU A CD1   1 
ATOM   11710 C  CD2   . LEU A 1 3012 ? 214.168 226.680 255.199 1.00 17.12  ? 3012 LEU A CD2   1 
ATOM   11711 N  N     . ALA A 1 3013 ? 215.257 231.754 253.695 1.00 18.47  ? 3013 ALA A N     1 
ATOM   11712 C  CA    . ALA A 1 3013 ? 216.134 232.897 253.911 1.00 16.69  ? 3013 ALA A CA    1 
ATOM   11713 C  C     . ALA A 1 3013 ? 215.400 234.068 254.557 1.00 22.54  ? 3013 ALA A C     1 
ATOM   11714 O  O     . ALA A 1 3013 ? 215.899 234.663 255.518 1.00 24.83  ? 3013 ALA A O     1 
ATOM   11715 C  CB    . ALA A 1 3013 ? 216.774 233.319 252.593 1.00 19.48  ? 3013 ALA A CB    1 
ATOM   11716 N  N     . ASN A 1 3014 ? 214.213 234.414 254.054 1.00 25.34  ? 3014 ASN A N     1 
ATOM   11717 C  CA    . ASN A 1 3014 ? 213.510 235.593 254.544 1.00 22.81  ? 3014 ASN A CA    1 
ATOM   11718 C  C     . ASN A 1 3014 ? 212.349 235.278 255.475 1.00 27.87  ? 3014 ASN A C     1 
ATOM   11719 O  O     . ASN A 1 3014 ? 211.963 236.145 256.265 1.00 29.99  ? 3014 ASN A O     1 
ATOM   11720 C  CB    . ASN A 1 3014 ? 212.982 236.432 253.373 1.00 22.63  ? 3014 ASN A CB    1 
ATOM   11721 C  CG    . ASN A 1 3014 ? 214.090 236.990 252.508 1.00 28.79  ? 3014 ASN A CG    1 
ATOM   11722 O  OD1   . ASN A 1 3014 ? 214.222 236.631 251.339 1.00 29.16  ? 3014 ASN A OD1   1 
ATOM   11723 N  ND2   . ASN A 1 3014 ? 214.897 237.876 253.080 1.00 22.33  ? 3014 ASN A ND2   1 
ATOM   11724 N  N     . GLY A 1 3015 ? 211.785 234.076 255.408 1.00 26.42  ? 3015 GLY A N     1 
ATOM   11725 C  CA    . GLY A 1 3015 ? 210.591 233.783 256.169 1.00 24.19  ? 3015 GLY A CA    1 
ATOM   11726 C  C     . GLY A 1 3015 ? 209.299 234.162 255.487 1.00 25.61  ? 3015 GLY A C     1 
ATOM   11727 O  O     . GLY A 1 3015 ? 208.241 234.096 256.119 1.00 29.05  ? 3015 GLY A O     1 
ATOM   11728 N  N     . GLU A 1 3016 ? 209.354 234.564 254.220 1.00 28.77  ? 3016 GLU A N     1 
ATOM   11729 C  CA    . GLU A 1 3016 ? 208.171 234.941 253.459 1.00 29.63  ? 3016 GLU A CA    1 
ATOM   11730 C  C     . GLU A 1 3016 ? 208.478 234.821 251.975 1.00 34.16  ? 3016 GLU A C     1 
ATOM   11731 O  O     . GLU A 1 3016 ? 209.629 234.978 251.561 1.00 36.75  ? 3016 GLU A O     1 
ATOM   11732 C  CB    . GLU A 1 3016 ? 207.724 236.367 253.809 1.00 29.23  ? 3016 GLU A CB    1 
ATOM   11733 C  CG    . GLU A 1 3016 ? 208.755 237.453 253.507 1.00 29.63  ? 3016 GLU A CG    1 
ATOM   11734 C  CD    . GLU A 1 3016 ? 208.703 237.955 252.079 1.00 44.33  ? 3016 GLU A CD    1 
ATOM   11735 O  OE1   . GLU A 1 3016 ? 207.666 237.763 251.413 1.00 48.91  ? 3016 GLU A OE1   1 
ATOM   11736 O  OE2   . GLU A 1 3016 ? 209.706 238.540 251.619 1.00 43.62  ? 3016 GLU A OE2   1 
ATOM   11737 N  N     . VAL A 1 3017 ? 207.448 234.539 251.189 1.00 34.38  ? 3017 VAL A N     1 
ATOM   11738 C  CA    . VAL A 1 3017 ? 207.537 234.527 249.732 1.00 35.79  ? 3017 VAL A CA    1 
ATOM   11739 C  C     . VAL A 1 3017 ? 206.813 235.766 249.215 1.00 39.78  ? 3017 VAL A C     1 
ATOM   11740 O  O     . VAL A 1 3017 ? 205.615 235.925 249.493 1.00 39.08  ? 3017 VAL A O     1 
ATOM   11741 C  CB    . VAL A 1 3017 ? 206.937 233.246 249.136 1.00 33.63  ? 3017 VAL A CB    1 
ATOM   11742 C  CG1   . VAL A 1 3017 ? 206.949 233.317 247.619 1.00 33.79  ? 3017 VAL A CG1   1 
ATOM   11743 C  CG2   . VAL A 1 3017 ? 207.702 232.027 249.623 1.00 25.11  ? 3017 VAL A CG2   1 
ATOM   11744 N  N     . PRO A 1 3018 ? 207.488 236.661 248.486 1.00 38.34  ? 3018 PRO A N     1 
ATOM   11745 C  CA    . PRO A 1 3018 ? 206.847 237.937 248.121 1.00 43.42  ? 3018 PRO A CA    1 
ATOM   11746 C  C     . PRO A 1 3018 ? 205.600 237.787 247.266 1.00 45.02  ? 3018 PRO A C     1 
ATOM   11747 O  O     . PRO A 1 3018 ? 204.662 238.580 247.408 1.00 50.15  ? 3018 PRO A O     1 
ATOM   11748 C  CB    . PRO A 1 3018 ? 207.965 238.680 247.377 1.00 41.20  ? 3018 PRO A CB    1 
ATOM   11749 C  CG    . PRO A 1 3018 ? 208.831 237.598 246.827 1.00 36.48  ? 3018 PRO A CG    1 
ATOM   11750 C  CD    . PRO A 1 3018 ? 208.801 236.490 247.840 1.00 36.54  ? 3018 PRO A CD    1 
ATOM   11751 N  N     . GLY A 1 3019 ? 205.558 236.796 246.380 1.00 33.51  ? 3019 GLY A N     1 
ATOM   11752 C  CA    . GLY A 1 3019 ? 204.425 236.591 245.504 1.00 35.22  ? 3019 GLY A CA    1 
ATOM   11753 C  C     . GLY A 1 3019 ? 203.485 235.467 245.888 1.00 41.97  ? 3019 GLY A C     1 
ATOM   11754 O  O     . GLY A 1 3019 ? 202.596 235.132 245.098 1.00 43.25  ? 3019 GLY A O     1 
ATOM   11755 N  N     . LEU A 1 3020 ? 203.649 234.872 247.071 1.00 34.19  ? 3020 LEU A N     1 
ATOM   11756 C  CA    . LEU A 1 3020 ? 202.803 233.747 247.455 1.00 33.02  ? 3020 LEU A CA    1 
ATOM   11757 C  C     . LEU A 1 3020 ? 201.364 234.189 247.691 1.00 37.67  ? 3020 LEU A C     1 
ATOM   11758 O  O     . LEU A 1 3020 ? 200.419 233.537 247.233 1.00 35.02  ? 3020 LEU A O     1 
ATOM   11759 C  CB    . LEU A 1 3020 ? 203.369 233.066 248.700 1.00 28.54  ? 3020 LEU A CB    1 
ATOM   11760 C  CG    . LEU A 1 3020 ? 202.873 231.646 248.968 1.00 28.96  ? 3020 LEU A CG    1 
ATOM   11761 C  CD1   . LEU A 1 3020 ? 203.376 230.696 247.900 1.00 31.80  ? 3020 LEU A CD1   1 
ATOM   11762 C  CD2   . LEU A 1 3020 ? 203.305 231.179 250.346 1.00 22.19  ? 3020 LEU A CD2   1 
ATOM   11763 N  N     . PHE A 1 3021 ? 201.179 235.294 248.404 1.00 38.62  ? 3021 PHE A N     1 
ATOM   11764 C  CA    . PHE A 1 3021 ? 199.852 235.819 248.715 1.00 36.93  ? 3021 PHE A CA    1 
ATOM   11765 C  C     . PHE A 1 3021 ? 199.592 237.016 247.807 1.00 48.99  ? 3021 PHE A C     1 
ATOM   11766 O  O     . PHE A 1 3021 ? 200.053 238.127 248.079 1.00 47.94  ? 3021 PHE A O     1 
ATOM   11767 C  CB    . PHE A 1 3021 ? 199.752 236.203 250.186 1.00 34.83  ? 3021 PHE A CB    1 
ATOM   11768 C  CG    . PHE A 1 3021 ? 199.994 235.060 251.130 1.00 34.70  ? 3021 PHE A CG    1 
ATOM   11769 C  CD1   . PHE A 1 3021 ? 201.275 234.749 251.548 1.00 29.82  ? 3021 PHE A CD1   1 
ATOM   11770 C  CD2   . PHE A 1 3021 ? 198.938 234.305 251.609 1.00 36.83  ? 3021 PHE A CD2   1 
ATOM   11771 C  CE1   . PHE A 1 3021 ? 201.499 233.704 252.420 1.00 27.02  ? 3021 PHE A CE1   1 
ATOM   11772 C  CE2   . PHE A 1 3021 ? 199.157 233.258 252.482 1.00 34.61  ? 3021 PHE A CE2   1 
ATOM   11773 C  CZ    . PHE A 1 3021 ? 200.440 232.959 252.888 1.00 29.30  ? 3021 PHE A CZ    1 
ATOM   11774 N  N     . GLU A 1 3022 ? 198.854 236.786 246.724 1.00 52.23  ? 3022 GLU A N     1 
ATOM   11775 C  CA    . GLU A 1 3022 ? 198.501 237.846 245.790 1.00 54.20  ? 3022 GLU A CA    1 
ATOM   11776 C  C     . GLU A 1 3022 ? 197.046 237.684 245.379 1.00 52.72  ? 3022 GLU A C     1 
ATOM   11777 O  O     . GLU A 1 3022 ? 196.621 236.584 245.018 1.00 47.82  ? 3022 GLU A O     1 
ATOM   11778 C  CB    . GLU A 1 3022 ? 199.410 237.827 244.556 1.00 54.63  ? 3022 GLU A CB    1 
ATOM   11779 C  CG    . GLU A 1 3022 ? 199.125 238.937 243.555 1.00 68.71  ? 3022 GLU A CG    1 
ATOM   11780 C  CD    . GLU A 1 3022 ? 199.407 240.320 244.112 1.00 69.52  ? 3022 GLU A CD    1 
ATOM   11781 O  OE1   . GLU A 1 3022 ? 200.246 240.436 245.029 1.00 77.75  ? 3022 GLU A OE1   1 
ATOM   11782 O  OE2   . GLU A 1 3022 ? 198.786 241.291 243.633 1.00 70.05  ? 3022 GLU A OE2   1 
ATOM   11783 N  N     . GLY A 1 3023 ? 196.294 238.779 245.433 1.00 51.49  ? 3023 GLY A N     1 
ATOM   11784 C  CA    . GLY A 1 3023 ? 194.888 238.754 245.081 1.00 48.31  ? 3023 GLY A CA    1 
ATOM   11785 C  C     . GLY A 1 3023 ? 193.981 238.657 246.288 1.00 43.70  ? 3023 GLY A C     1 
ATOM   11786 O  O     . GLY A 1 3023 ? 194.251 239.271 247.325 1.00 42.51  ? 3023 GLY A O     1 
ATOM   11787 N  N     . ASP A 1 3024 ? 192.893 237.892 246.165 1.00 52.11  ? 3024 ASP A N     1 
ATOM   11788 C  CA    . ASP A 1 3024 ? 192.008 237.673 247.305 1.00 54.66  ? 3024 ASP A CA    1 
ATOM   11789 C  C     . ASP A 1 3024 ? 192.725 236.937 248.427 1.00 48.92  ? 3024 ASP A C     1 
ATOM   11790 O  O     . ASP A 1 3024 ? 192.378 237.104 249.603 1.00 48.06  ? 3024 ASP A O     1 
ATOM   11791 C  CB    . ASP A 1 3024 ? 190.770 236.894 246.865 1.00 59.99  ? 3024 ASP A CB    1 
ATOM   11792 C  CG    . ASP A 1 3024 ? 191.105 235.738 245.944 1.00 63.90  ? 3024 ASP A CG    1 
ATOM   11793 O  OD1   . ASP A 1 3024 ? 192.278 235.631 245.526 1.00 60.02  ? 3024 ASP A OD1   1 
ATOM   11794 O  OD2   . ASP A 1 3024 ? 190.199 234.936 245.637 1.00 73.16  ? 3024 ASP A OD2   1 
ATOM   11795 N  N     . GLU A 1 3025 ? 193.722 236.120 248.081 1.00 47.63  ? 3025 GLU A N     1 
ATOM   11796 C  CA    . GLU A 1 3025 ? 194.507 235.432 249.098 1.00 47.84  ? 3025 GLU A CA    1 
ATOM   11797 C  C     . GLU A 1 3025 ? 195.237 236.425 249.993 1.00 43.98  ? 3025 GLU A C     1 
ATOM   11798 O  O     . GLU A 1 3025 ? 195.315 236.229 251.210 1.00 45.78  ? 3025 GLU A O     1 
ATOM   11799 C  CB    . GLU A 1 3025 ? 195.497 234.471 248.439 1.00 50.35  ? 3025 GLU A CB    1 
ATOM   11800 C  CG    . GLU A 1 3025 ? 194.852 233.419 247.550 1.00 51.15  ? 3025 GLU A CG    1 
ATOM   11801 C  CD    . GLU A 1 3025 ? 194.239 232.277 248.341 1.00 59.65  ? 3025 GLU A CD    1 
ATOM   11802 O  OE1   . GLU A 1 3025 ? 194.454 232.217 249.571 1.00 57.63  ? 3025 GLU A OE1   1 
ATOM   11803 O  OE2   . GLU A 1 3025 ? 193.543 231.438 247.733 1.00 49.88  ? 3025 GLU A OE2   1 
ATOM   11804 N  N     . TYR A 1 3026 ? 195.782 237.496 249.409 1.00 38.77  ? 3026 TYR A N     1 
ATOM   11805 C  CA    . TYR A 1 3026 ? 196.467 238.501 250.218 1.00 36.79  ? 3026 TYR A CA    1 
ATOM   11806 C  C     . TYR A 1 3026 ? 195.502 239.199 251.167 1.00 39.90  ? 3026 TYR A C     1 
ATOM   11807 O  O     . TYR A 1 3026 ? 195.848 239.477 252.319 1.00 38.75  ? 3026 TYR A O     1 
ATOM   11808 C  CB    . TYR A 1 3026 ? 197.166 239.522 249.323 1.00 36.14  ? 3026 TYR A CB    1 
ATOM   11809 C  CG    . TYR A 1 3026 ? 198.092 240.446 250.084 1.00 32.78  ? 3026 TYR A CG    1 
ATOM   11810 C  CD1   . TYR A 1 3026 ? 199.225 239.953 250.718 1.00 33.16  ? 3026 TYR A CD1   1 
ATOM   11811 C  CD2   . TYR A 1 3026 ? 197.827 241.806 250.179 1.00 35.47  ? 3026 TYR A CD2   1 
ATOM   11812 C  CE1   . TYR A 1 3026 ? 200.072 240.788 251.418 1.00 31.96  ? 3026 TYR A CE1   1 
ATOM   11813 C  CE2   . TYR A 1 3026 ? 198.670 242.649 250.879 1.00 35.56  ? 3026 TYR A CE2   1 
ATOM   11814 C  CZ    . TYR A 1 3026 ? 199.791 242.133 251.497 1.00 34.11  ? 3026 TYR A CZ    1 
ATOM   11815 O  OH    . TYR A 1 3026 ? 200.635 242.964 252.194 1.00 38.99  ? 3026 TYR A OH    1 
ATOM   11816 N  N     . ALA A 1 3027 ? 194.288 239.501 250.699 1.00 42.80  ? 3027 ALA A N     1 
ATOM   11817 C  CA    . ALA A 1 3027 ? 193.299 240.134 251.567 1.00 38.36  ? 3027 ALA A CA    1 
ATOM   11818 C  C     . ALA A 1 3027 ? 192.886 239.208 252.707 1.00 38.29  ? 3027 ALA A C     1 
ATOM   11819 O  O     . ALA A 1 3027 ? 192.758 239.646 253.858 1.00 45.09  ? 3027 ALA A O     1 
ATOM   11820 C  CB    . ALA A 1 3027 ? 192.081 240.560 250.749 1.00 42.39  ? 3027 ALA A CB    1 
ATOM   11821 N  N     . THR A 1 3028 ? 192.674 237.925 252.406 1.00 37.00  ? 3028 THR A N     1 
ATOM   11822 C  CA    . THR A 1 3028 ? 192.349 236.964 253.458 1.00 39.94  ? 3028 THR A CA    1 
ATOM   11823 C  C     . THR A 1 3028 ? 193.494 236.837 254.456 1.00 42.25  ? 3028 THR A C     1 
ATOM   11824 O  O     . THR A 1 3028 ? 193.269 236.753 255.672 1.00 43.67  ? 3028 THR A O     1 
ATOM   11825 C  CB    . THR A 1 3028 ? 192.017 235.606 252.840 1.00 40.52  ? 3028 THR A CB    1 
ATOM   11826 O  OG1   . THR A 1 3028 ? 190.892 235.739 251.963 1.00 40.82  ? 3028 THR A OG1   1 
ATOM   11827 C  CG2   . THR A 1 3028 ? 191.682 234.592 253.924 1.00 44.75  ? 3028 THR A CG2   1 
ATOM   11828 N  N     . LEU A 1 3029 ? 194.732 236.818 253.956 1.00 40.31  ? 3029 LEU A N     1 
ATOM   11829 C  CA    . LEU A 1 3029 ? 195.895 236.754 254.832 1.00 41.65  ? 3029 LEU A CA    1 
ATOM   11830 C  C     . LEU A 1 3029 ? 195.978 237.982 255.725 1.00 42.02  ? 3029 LEU A C     1 
ATOM   11831 O  O     . LEU A 1 3029 ? 196.291 237.871 256.912 1.00 45.33  ? 3029 LEU A O     1 
ATOM   11832 C  CB    . LEU A 1 3029 ? 197.170 236.610 254.000 1.00 39.61  ? 3029 LEU A CB    1 
ATOM   11833 C  CG    . LEU A 1 3029 ? 198.499 236.744 254.749 1.00 33.87  ? 3029 LEU A CG    1 
ATOM   11834 C  CD1   . LEU A 1 3029 ? 198.835 235.460 255.489 1.00 31.31  ? 3029 LEU A CD1   1 
ATOM   11835 C  CD2   . LEU A 1 3029 ? 199.623 237.136 253.805 1.00 28.93  ? 3029 LEU A CD2   1 
ATOM   11836 N  N     . MET A 1 3030 ? 195.703 239.165 255.169 1.00 41.41  ? 3030 MET A N     1 
ATOM   11837 C  CA    . MET A 1 3030 ? 195.708 240.383 255.974 1.00 40.26  ? 3030 MET A CA    1 
ATOM   11838 C  C     . MET A 1 3030 ? 194.632 240.336 257.049 1.00 37.87  ? 3030 MET A C     1 
ATOM   11839 O  O     . MET A 1 3030 ? 194.866 240.748 258.191 1.00 42.11  ? 3030 MET A O     1 
ATOM   11840 C  CB    . MET A 1 3030 ? 195.519 241.605 255.076 1.00 40.14  ? 3030 MET A CB    1 
ATOM   11841 C  CG    . MET A 1 3030 ? 196.779 242.114 254.372 1.00 37.55  ? 3030 MET A CG    1 
ATOM   11842 S  SD    . MET A 1 3030 ? 198.282 242.143 255.374 1.00 50.27  ? 3030 MET A SD    1 
ATOM   11843 C  CE    . MET A 1 3030 ? 199.040 240.574 254.953 1.00 40.51  ? 3030 MET A CE    1 
ATOM   11844 N  N     . THR A 1 3031 ? 193.445 239.833 256.703 1.00 38.66  ? 3031 THR A N     1 
ATOM   11845 C  CA    . THR A 1 3031 ? 192.375 239.716 257.690 1.00 43.30  ? 3031 THR A CA    1 
ATOM   11846 C  C     . THR A 1 3031 ? 192.783 238.795 258.834 1.00 41.68  ? 3031 THR A C     1 
ATOM   11847 O  O     . THR A 1 3031 ? 192.646 239.145 260.015 1.00 41.23  ? 3031 THR A O     1 
ATOM   11848 C  CB    . THR A 1 3031 ? 191.101 239.207 257.018 1.00 43.51  ? 3031 THR A CB    1 
ATOM   11849 O  OG1   . THR A 1 3031 ? 190.884 239.921 255.795 1.00 42.62  ? 3031 THR A OG1   1 
ATOM   11850 C  CG2   . THR A 1 3031 ? 189.902 239.404 257.931 1.00 40.45  ? 3031 THR A CG2   1 
ATOM   11851 N  N     . GLN A 1 3032 ? 193.302 237.611 258.499 1.00 42.68  ? 3032 GLN A N     1 
ATOM   11852 C  CA    . GLN A 1 3032 ? 193.715 236.677 259.541 1.00 39.97  ? 3032 GLN A CA    1 
ATOM   11853 C  C     . GLN A 1 3032 ? 194.889 237.215 260.350 1.00 40.72  ? 3032 GLN A C     1 
ATOM   11854 O  O     . GLN A 1 3032 ? 194.974 236.963 261.555 1.00 41.81  ? 3032 GLN A O     1 
ATOM   11855 C  CB    . GLN A 1 3032 ? 194.070 235.320 258.941 1.00 41.21  ? 3032 GLN A CB    1 
ATOM   11856 C  CG    . GLN A 1 3032 ? 192.897 234.576 258.335 1.00 49.47  ? 3032 GLN A CG    1 
ATOM   11857 C  CD    . GLN A 1 3032 ? 193.312 233.247 257.745 1.00 59.86  ? 3032 GLN A CD    1 
ATOM   11858 O  OE1   . GLN A 1 3032 ? 194.493 232.908 257.730 1.00 58.19  ? 3032 GLN A OE1   1 
ATOM   11859 N  NE2   . GLN A 1 3032 ? 192.341 232.483 257.260 1.00 63.29  ? 3032 GLN A NE2   1 
ATOM   11860 N  N     . CYS A 1 3033 ? 195.803 237.949 259.713 1.00 39.24  ? 3033 CYS A N     1 
ATOM   11861 C  CA    . CYS A 1 3033 ? 196.928 238.529 260.436 1.00 40.50  ? 3033 CYS A CA    1 
ATOM   11862 C  C     . CYS A 1 3033 ? 196.462 239.594 261.418 1.00 40.29  ? 3033 CYS A C     1 
ATOM   11863 O  O     . CYS A 1 3033 ? 196.980 239.682 262.536 1.00 42.43  ? 3033 CYS A O     1 
ATOM   11864 C  CB    . CYS A 1 3033 ? 197.941 239.113 259.453 1.00 46.27  ? 3033 CYS A CB    1 
ATOM   11865 S  SG    . CYS A 1 3033 ? 198.919 237.891 258.558 1.00 65.58  ? 3033 CYS A SG    1 
ATOM   11866 N  N     . LYS A 1 3034 ? 195.498 240.422 261.012 1.00 40.23  ? 3034 LYS A N     1 
ATOM   11867 C  CA    . LYS A 1 3034 ? 194.937 241.401 261.936 1.00 42.79  ? 3034 LYS A CA    1 
ATOM   11868 C  C     . LYS A 1 3034 ? 194.249 240.710 263.105 1.00 50.55  ? 3034 LYS A C     1 
ATOM   11869 O  O     . LYS A 1 3034 ? 194.390 241.135 264.259 1.00 48.29  ? 3034 LYS A O     1 
ATOM   11870 C  CB    . LYS A 1 3034 ? 193.960 242.320 261.206 1.00 43.47  ? 3034 LYS A CB    1 
ATOM   11871 C  CG    . LYS A 1 3034 ? 193.777 243.674 261.871 1.00 42.77  ? 3034 LYS A CG    1 
ATOM   11872 C  CD    . LYS A 1 3034 ? 192.504 244.357 261.399 1.00 38.91  ? 3034 LYS A CD    1 
ATOM   11873 C  CE    . LYS A 1 3034 ? 192.225 245.616 262.200 1.00 44.20  ? 3034 LYS A CE    1 
ATOM   11874 N  NZ    . LYS A 1 3034 ? 193.163 246.716 261.837 1.00 50.09  ? 3034 LYS A NZ    1 
ATOM   11875 N  N     . GLU A 1 3035 ? 193.507 239.634 262.827 1.00 46.78  ? 3035 GLU A N     1 
ATOM   11876 C  CA    . GLU A 1 3035 ? 192.876 238.883 263.908 1.00 49.90  ? 3035 GLU A CA    1 
ATOM   11877 C  C     . GLU A 1 3035 ? 193.917 238.302 264.862 1.00 53.40  ? 3035 GLU A C     1 
ATOM   11878 O  O     . GLU A 1 3035 ? 193.756 238.368 266.087 1.00 59.17  ? 3035 GLU A O     1 
ATOM   11879 C  CB    . GLU A 1 3035 ? 191.996 237.775 263.330 1.00 52.30  ? 3035 GLU A CB    1 
ATOM   11880 C  CG    . GLU A 1 3035 ? 191.257 236.959 264.375 1.00 64.41  ? 3035 GLU A CG    1 
ATOM   11881 C  CD    . GLU A 1 3035 ? 190.239 237.780 265.146 1.00 75.36  ? 3035 GLU A CD    1 
ATOM   11882 O  OE1   . GLU A 1 3035 ? 189.746 238.791 264.604 1.00 73.60  ? 3035 GLU A OE1   1 
ATOM   11883 O  OE2   . GLU A 1 3035 ? 189.933 237.413 266.300 1.00 76.56  ? 3035 GLU A OE2   1 
ATOM   11884 N  N     . GLY A 1 3036 ? 194.996 237.739 264.318 1.00 44.61  ? 3036 GLY A N     1 
ATOM   11885 C  CA    . GLY A 1 3036 ? 196.031 237.170 265.164 1.00 44.69  ? 3036 GLY A CA    1 
ATOM   11886 C  C     . GLY A 1 3036 ? 196.760 238.214 265.988 1.00 49.71  ? 3036 GLY A C     1 
ATOM   11887 O  O     . GLY A 1 3036 ? 197.094 237.974 267.152 1.00 48.47  ? 3036 GLY A O     1 
ATOM   11888 N  N     . ALA A 1 3037 ? 197.030 239.378 265.395 1.00 49.89  ? 3037 ALA A N     1 
ATOM   11889 C  CA    . ALA A 1 3037 ? 197.669 240.458 266.139 1.00 51.04  ? 3037 ALA A CA    1 
ATOM   11890 C  C     . ALA A 1 3037 ? 196.762 240.970 267.249 1.00 60.00  ? 3037 ALA A C     1 
ATOM   11891 O  O     . ALA A 1 3037 ? 197.231 241.288 268.348 1.00 61.41  ? 3037 ALA A O     1 
ATOM   11892 C  CB    . ALA A 1 3037 ? 198.060 241.592 265.192 1.00 51.35  ? 3037 ALA A CB    1 
ATOM   11893 N  N     . GLN A 1 3038 ? 195.456 241.062 266.979 1.00 61.13  ? 3038 GLN A N     1 
ATOM   11894 C  CA    . GLN A 1 3038 ? 194.513 241.431 268.031 1.00 62.97  ? 3038 GLN A CA    1 
ATOM   11895 C  C     . GLN A 1 3038 ? 194.513 240.396 269.148 1.00 62.74  ? 3038 GLN A C     1 
ATOM   11896 O  O     . GLN A 1 3038 ? 194.443 240.748 270.331 1.00 66.41  ? 3038 GLN A O     1 
ATOM   11897 C  CB    . GLN A 1 3038 ? 193.110 241.590 267.445 1.00 66.01  ? 3038 GLN A CB    1 
ATOM   11898 C  CG    . GLN A 1 3038 ? 192.820 242.973 266.889 1.00 71.83  ? 3038 GLN A CG    1 
ATOM   11899 C  CD    . GLN A 1 3038 ? 191.572 242.999 266.029 1.00 73.52  ? 3038 GLN A CD    1 
ATOM   11900 O  OE1   . GLN A 1 3038 ? 190.728 242.106 266.111 1.00 73.00  ? 3038 GLN A OE1   1 
ATOM   11901 N  NE2   . GLN A 1 3038 ? 191.448 244.027 265.196 1.00 66.18  ? 3038 GLN A NE2   1 
ATOM   11902 N  N     . LYS A 1 3039 ? 194.583 239.112 268.788 1.00 59.73  ? 3039 LYS A N     1 
ATOM   11903 C  CA    . LYS A 1 3039 ? 194.677 238.060 269.796 1.00 56.82  ? 3039 LYS A CA    1 
ATOM   11904 C  C     . LYS A 1 3039 ? 195.940 238.209 270.635 1.00 59.66  ? 3039 LYS A C     1 
ATOM   11905 O  O     . LYS A 1 3039 ? 195.903 238.052 271.862 1.00 60.97  ? 3039 LYS A O     1 
ATOM   11906 C  CB    . LYS A 1 3039 ? 194.643 236.689 269.121 1.00 52.84  ? 3039 LYS A CB    1 
ATOM   11907 C  CG    . LYS A 1 3039 ? 194.733 235.516 270.080 1.00 50.99  ? 3039 LYS A CG    1 
ATOM   11908 C  CD    . LYS A 1 3039 ? 193.716 234.441 269.737 1.00 54.68  ? 3039 LYS A CD    1 
ATOM   11909 C  CE    . LYS A 1 3039 ? 193.809 233.267 270.699 1.00 57.12  ? 3039 LYS A CE    1 
ATOM   11910 N  NZ    . LYS A 1 3039 ? 192.721 232.277 270.476 1.00 54.55  ? 3039 LYS A NZ    1 
ATOM   11911 N  N     . GLU A 1 3040 ? 197.070 238.511 269.992 1.00 65.71  ? 3040 GLU A N     1 
ATOM   11912 C  CA    . GLU A 1 3040 ? 198.327 238.665 270.716 1.00 62.10  ? 3040 GLU A CA    1 
ATOM   11913 C  C     . GLU A 1 3040 ? 198.312 239.898 271.613 1.00 66.92  ? 3040 GLU A C     1 
ATOM   11914 O  O     . GLU A 1 3040 ? 198.968 239.910 272.660 1.00 70.80  ? 3040 GLU A O     1 
ATOM   11915 C  CB    . GLU A 1 3040 ? 199.490 238.737 269.726 1.00 58.76  ? 3040 GLU A CB    1 
ATOM   11916 C  CG    . GLU A 1 3040 ? 200.851 238.995 270.357 1.00 60.80  ? 3040 GLU A CG    1 
ATOM   11917 C  CD    . GLU A 1 3040 ? 201.999 238.712 269.406 1.00 63.29  ? 3040 GLU A CD    1 
ATOM   11918 O  OE1   . GLU A 1 3040 ? 202.010 237.626 268.790 1.00 50.34  ? 3040 GLU A OE1   1 
ATOM   11919 O  OE2   . GLU A 1 3040 ? 202.891 239.575 269.277 1.00 62.52  ? 3040 GLU A OE2   1 
ATOM   11920 N  N     . GLY A 1 3041 ? 197.564 240.929 271.233 1.00 64.09  ? 3041 GLY A N     1 
ATOM   11921 C  CA    . GLY A 1 3041 ? 197.520 242.166 271.981 1.00 61.48  ? 3041 GLY A CA    1 
ATOM   11922 C  C     . GLY A 1 3041 ? 198.139 243.363 271.292 1.00 65.14  ? 3041 GLY A C     1 
ATOM   11923 O  O     . GLY A 1 3041 ? 198.381 244.378 271.954 1.00 69.84  ? 3041 GLY A O     1 
ATOM   11924 N  N     . LEU A 1 3042 ? 198.404 243.280 269.991 1.00 65.35  ? 3042 LEU A N     1 
ATOM   11925 C  CA    . LEU A 1 3042 ? 199.012 244.364 269.233 1.00 64.97  ? 3042 LEU A CA    1 
ATOM   11926 C  C     . LEU A 1 3042 ? 197.998 244.919 268.244 1.00 68.45  ? 3042 LEU A C     1 
ATOM   11927 O  O     . LEU A 1 3042 ? 197.412 244.163 267.461 1.00 68.09  ? 3042 LEU A O     1 
ATOM   11928 C  CB    . LEU A 1 3042 ? 200.262 243.882 268.494 1.00 61.27  ? 3042 LEU A CB    1 
ATOM   11929 C  CG    . LEU A 1 3042 ? 201.315 243.175 269.346 1.00 66.00  ? 3042 LEU A CG    1 
ATOM   11930 C  CD1   . LEU A 1 3042 ? 202.518 242.785 268.500 1.00 55.83  ? 3042 LEU A CD1   1 
ATOM   11931 C  CD2   . LEU A 1 3042 ? 201.738 244.051 270.515 1.00 67.60  ? 3042 LEU A CD2   1 
ATOM   11932 N  N     . MET A 1 3043 ? 197.798 246.232 268.279 1.00 71.41  ? 3043 MET A N     1 
ATOM   11933 C  CA    . MET A 1 3043 ? 196.861 246.910 267.388 1.00 69.52  ? 3043 MET A CA    1 
ATOM   11934 C  C     . MET A 1 3043 ? 197.651 247.463 266.209 1.00 67.86  ? 3043 MET A C     1 
ATOM   11935 O  O     . MET A 1 3043 ? 198.342 248.478 266.329 1.00 65.12  ? 3043 MET A O     1 
ATOM   11936 C  CB    . MET A 1 3043 ? 196.106 248.010 268.125 1.00 75.40  ? 3043 MET A CB    1 
ATOM   11937 C  CG    . MET A 1 3043 ? 195.107 247.494 269.146 1.00 83.92  ? 3043 MET A CG    1 
ATOM   11938 S  SD    . MET A 1 3043 ? 193.942 246.318 268.432 1.00 97.46  ? 3043 MET A SD    1 
ATOM   11939 C  CE    . MET A 1 3043 ? 192.935 247.408 267.429 1.00 86.18  ? 3043 MET A CE    1 
ATOM   11940 N  N     . LEU A 1 3044 ? 197.551 246.789 265.067 1.00 61.63  ? 3044 LEU A N     1 
ATOM   11941 C  CA    . LEU A 1 3044 ? 198.246 247.185 263.852 1.00 61.44  ? 3044 LEU A CA    1 
ATOM   11942 C  C     . LEU A 1 3044 ? 197.222 247.548 262.786 1.00 63.50  ? 3044 LEU A C     1 
ATOM   11943 O  O     . LEU A 1 3044 ? 196.226 246.841 262.604 1.00 58.40  ? 3044 LEU A O     1 
ATOM   11944 C  CB    . LEU A 1 3044 ? 199.159 246.061 263.356 1.00 56.28  ? 3044 LEU A CB    1 
ATOM   11945 C  CG    . LEU A 1 3044 ? 200.358 245.750 264.256 1.00 53.73  ? 3044 LEU A CG    1 
ATOM   11946 C  CD1   . LEU A 1 3044 ? 200.683 244.266 264.215 1.00 56.62  ? 3044 LEU A CD1   1 
ATOM   11947 C  CD2   . LEU A 1 3044 ? 201.573 246.584 263.881 1.00 50.07  ? 3044 LEU A CD2   1 
ATOM   11948 N  N     . ASP A 1 3045 ? 197.464 248.656 262.086 1.00 67.28  ? 3045 ASP A N     1 
ATOM   11949 C  CA    . ASP A 1 3045 ? 196.497 249.201 261.140 1.00 68.52  ? 3045 ASP A CA    1 
ATOM   11950 C  C     . ASP A 1 3045 ? 196.905 248.997 259.685 1.00 64.10  ? 3045 ASP A C     1 
ATOM   11951 O  O     . ASP A 1 3045 ? 196.113 248.481 258.891 1.00 57.17  ? 3045 ASP A O     1 
ATOM   11952 C  CB    . ASP A 1 3045 ? 196.253 250.690 261.441 1.00 68.42  ? 3045 ASP A CB    1 
ATOM   11953 C  CG    . ASP A 1 3045 ? 197.501 251.545 261.277 1.00 75.80  ? 3045 ASP A CG    1 
ATOM   11954 O  OD1   . ASP A 1 3045 ? 198.579 250.996 260.969 1.00 76.86  ? 3045 ASP A OD1   1 
ATOM   11955 O  OD2   . ASP A 1 3045 ? 197.399 252.776 261.453 1.00 76.69  ? 3045 ASP A OD2   1 
ATOM   11956 N  N     . SER A 1 3046 ? 198.120 249.384 259.308 1.00 65.14  ? 3046 SER A N     1 
ATOM   11957 C  CA    . SER A 1 3046 ? 198.512 249.323 257.910 1.00 57.50  ? 3046 SER A CA    1 
ATOM   11958 C  C     . SER A 1 3046 ? 198.929 247.907 257.525 1.00 54.56  ? 3046 SER A C     1 
ATOM   11959 O  O     . SER A 1 3046 ? 199.246 247.067 258.371 1.00 59.22  ? 3046 SER A O     1 
ATOM   11960 C  CB    . SER A 1 3046 ? 199.648 250.304 257.618 1.00 60.43  ? 3046 SER A CB    1 
ATOM   11961 O  OG    . SER A 1 3046 ? 200.823 249.960 258.327 1.00 59.63  ? 3046 SER A OG    1 
ATOM   11962 N  N     . HIS A 1 3047 ? 198.918 247.648 256.216 1.00 52.52  ? 3047 HIS A N     1 
ATOM   11963 C  CA    . HIS A 1 3047 ? 199.243 246.316 255.722 1.00 44.25  ? 3047 HIS A CA    1 
ATOM   11964 C  C     . HIS A 1 3047 ? 200.740 246.035 255.786 1.00 49.51  ? 3047 HIS A C     1 
ATOM   11965 O  O     . HIS A 1 3047 ? 201.141 244.873 255.897 1.00 51.84  ? 3047 HIS A O     1 
ATOM   11966 C  CB    . HIS A 1 3047 ? 198.729 246.147 254.293 1.00 44.37  ? 3047 HIS A CB    1 
ATOM   11967 C  CG    . HIS A 1 3047 ? 197.251 245.930 254.203 1.00 49.28  ? 3047 HIS A CG    1 
ATOM   11968 N  ND1   . HIS A 1 3047 ? 196.592 245.777 253.003 1.00 46.00  ? 3047 HIS A ND1   1 
ATOM   11969 C  CD2   . HIS A 1 3047 ? 196.303 245.837 255.167 1.00 48.99  ? 3047 HIS A CD2   1 
ATOM   11970 C  CE1   . HIS A 1 3047 ? 195.303 245.598 253.230 1.00 47.93  ? 3047 HIS A CE1   1 
ATOM   11971 N  NE2   . HIS A 1 3047 ? 195.101 245.632 254.534 1.00 47.32  ? 3047 HIS A NE2   1 
ATOM   11972 N  N     . GLU A 1 3048 ? 201.577 247.073 255.715 1.00 54.67  ? 3048 GLU A N     1 
ATOM   11973 C  CA    . GLU A 1 3048 ? 203.022 246.859 255.743 1.00 49.19  ? 3048 GLU A CA    1 
ATOM   11974 C  C     . GLU A 1 3048 ? 203.482 246.339 257.102 1.00 46.84  ? 3048 GLU A C     1 
ATOM   11975 O  O     . GLU A 1 3048 ? 204.188 245.326 257.185 1.00 45.68  ? 3048 GLU A O     1 
ATOM   11976 C  CB    . GLU A 1 3048 ? 203.750 248.155 255.386 1.00 53.14  ? 3048 GLU A CB    1 
ATOM   11977 C  CG    . GLU A 1 3048 ? 203.545 248.613 253.950 1.00 63.54  ? 3048 GLU A CG    1 
ATOM   11978 C  CD    . GLU A 1 3048 ? 202.252 249.380 253.757 1.00 75.06  ? 3048 GLU A CD    1 
ATOM   11979 O  OE1   . GLU A 1 3048 ? 201.541 249.613 254.755 1.00 65.79  ? 3048 GLU A OE1   1 
ATOM   11980 O  OE2   . GLU A 1 3048 ? 201.944 249.747 252.604 1.00 90.46  ? 3048 GLU A OE2   1 
ATOM   11981 N  N     . GLU A 1 3049 ? 203.080 247.012 258.183 1.00 47.67  ? 3049 GLU A N     1 
ATOM   11982 C  CA    . GLU A 1 3049 ? 203.487 246.572 259.514 1.00 46.98  ? 3049 GLU A CA    1 
ATOM   11983 C  C     . GLU A 1 3049 ? 202.842 245.240 259.873 1.00 43.19  ? 3049 GLU A C     1 
ATOM   11984 O  O     . GLU A 1 3049 ? 203.451 244.408 260.556 1.00 38.85  ? 3049 GLU A O     1 
ATOM   11985 C  CB    . GLU A 1 3049 ? 203.140 247.640 260.552 1.00 46.73  ? 3049 GLU A CB    1 
ATOM   11986 C  CG    . GLU A 1 3049 ? 201.663 247.998 260.610 1.00 55.62  ? 3049 GLU A CG    1 
ATOM   11987 C  CD    . GLU A 1 3049 ? 201.395 249.266 261.398 1.00 65.45  ? 3049 GLU A CD    1 
ATOM   11988 O  OE1   . GLU A 1 3049 ? 200.511 249.244 262.281 1.00 66.90  ? 3049 GLU A OE1   1 
ATOM   11989 O  OE2   . GLU A 1 3049 ? 202.066 250.285 261.135 1.00 71.02  ? 3049 GLU A OE2   1 
ATOM   11990 N  N     . LEU A 1 3050 ? 201.606 245.022 259.420 1.00 39.89  ? 3050 LEU A N     1 
ATOM   11991 C  CA    . LEU A 1 3050 ? 200.939 243.751 259.667 1.00 41.49  ? 3050 LEU A CA    1 
ATOM   11992 C  C     . LEU A 1 3050 ? 201.656 242.611 258.950 1.00 35.41  ? 3050 LEU A C     1 
ATOM   11993 O  O     . LEU A 1 3050 ? 201.816 241.517 259.504 1.00 35.79  ? 3050 LEU A O     1 
ATOM   11994 C  CB    . LEU A 1 3050 ? 199.480 243.849 259.224 1.00 44.88  ? 3050 LEU A CB    1 
ATOM   11995 C  CG    . LEU A 1 3050 ? 198.562 242.655 259.451 1.00 45.39  ? 3050 LEU A CG    1 
ATOM   11996 C  CD1   . LEU A 1 3050 ? 198.435 242.381 260.938 1.00 43.95  ? 3050 LEU A CD1   1 
ATOM   11997 C  CD2   . LEU A 1 3050 ? 197.202 242.921 258.834 1.00 43.94  ? 3050 LEU A CD2   1 
ATOM   11998 N  N     . TYR A 1 3051 ? 202.107 242.856 257.717 1.00 35.62  ? 3051 TYR A N     1 
ATOM   11999 C  CA    . TYR A 1 3051 ? 202.882 241.855 256.992 1.00 32.71  ? 3051 TYR A CA    1 
ATOM   12000 C  C     . TYR A 1 3051 ? 204.229 241.615 257.660 1.00 31.07  ? 3051 TYR A C     1 
ATOM   12001 O  O     . TYR A 1 3051 ? 204.734 240.488 257.666 1.00 33.35  ? 3051 TYR A O     1 
ATOM   12002 C  CB    . TYR A 1 3051 ? 203.067 242.295 255.541 1.00 36.03  ? 3051 TYR A CB    1 
ATOM   12003 C  CG    . TYR A 1 3051 ? 203.774 241.286 254.667 1.00 35.15  ? 3051 TYR A CG    1 
ATOM   12004 C  CD1   . TYR A 1 3051 ? 205.126 241.413 254.379 1.00 35.09  ? 3051 TYR A CD1   1 
ATOM   12005 C  CD2   . TYR A 1 3051 ? 203.084 240.214 254.119 1.00 26.99  ? 3051 TYR A CD2   1 
ATOM   12006 C  CE1   . TYR A 1 3051 ? 205.773 240.493 253.577 1.00 31.97  ? 3051 TYR A CE1   1 
ATOM   12007 C  CE2   . TYR A 1 3051 ? 203.722 239.291 253.317 1.00 29.39  ? 3051 TYR A CE2   1 
ATOM   12008 C  CZ    . TYR A 1 3051 ? 205.065 239.435 253.049 1.00 35.51  ? 3051 TYR A CZ    1 
ATOM   12009 O  OH    . TYR A 1 3051 ? 205.700 238.517 252.248 1.00 42.35  ? 3051 TYR A OH    1 
ATOM   12010 N  N     . LYS A 1 3052 ? 204.829 242.666 258.226 1.00 31.82  ? 3052 LYS A N     1 
ATOM   12011 C  CA    . LYS A 1 3052 ? 206.056 242.484 258.998 1.00 30.03  ? 3052 LYS A CA    1 
ATOM   12012 C  C     . LYS A 1 3052 ? 205.818 241.597 260.214 1.00 28.44  ? 3052 LYS A C     1 
ATOM   12013 O  O     . LYS A 1 3052 ? 206.641 240.731 260.533 1.00 28.82  ? 3052 LYS A O     1 
ATOM   12014 C  CB    . LYS A 1 3052 ? 206.615 243.839 259.428 1.00 31.19  ? 3052 LYS A CB    1 
ATOM   12015 C  CG    . LYS A 1 3052 ? 207.093 244.712 258.285 1.00 34.03  ? 3052 LYS A CG    1 
ATOM   12016 C  CD    . LYS A 1 3052 ? 207.718 245.994 258.801 1.00 38.25  ? 3052 LYS A CD    1 
ATOM   12017 C  CE    . LYS A 1 3052 ? 209.230 245.873 258.878 1.00 41.08  ? 3052 LYS A CE    1 
ATOM   12018 N  NZ    . LYS A 1 3052 ? 209.886 246.359 257.635 1.00 37.77  ? 3052 LYS A NZ    1 
ATOM   12019 N  N     . TRP A 1 3053 ? 204.700 241.807 260.913 1.00 28.68  ? 3053 TRP A N     1 
ATOM   12020 C  CA    . TRP A 1 3053 ? 204.362 240.953 262.048 1.00 26.22  ? 3053 TRP A CA    1 
ATOM   12021 C  C     . TRP A 1 3053 ? 204.140 239.512 261.605 1.00 26.07  ? 3053 TRP A C     1 
ATOM   12022 O  O     . TRP A 1 3053 ? 204.552 238.569 262.291 1.00 30.18  ? 3053 TRP A O     1 
ATOM   12023 C  CB    . TRP A 1 3053 ? 203.123 241.490 262.764 1.00 31.62  ? 3053 TRP A CB    1 
ATOM   12024 C  CG    . TRP A 1 3053 ? 202.662 240.626 263.900 1.00 31.09  ? 3053 TRP A CG    1 
ATOM   12025 C  CD1   . TRP A 1 3053 ? 203.125 240.641 265.182 1.00 30.25  ? 3053 TRP A CD1   1 
ATOM   12026 C  CD2   . TRP A 1 3053 ? 201.646 239.617 263.853 1.00 29.60  ? 3053 TRP A CD2   1 
ATOM   12027 N  NE1   . TRP A 1 3053 ? 202.462 239.706 265.936 1.00 27.27  ? 3053 TRP A NE1   1 
ATOM   12028 C  CE2   . TRP A 1 3053 ? 201.547 239.064 265.144 1.00 30.63  ? 3053 TRP A CE2   1 
ATOM   12029 C  CE3   . TRP A 1 3053 ? 200.810 239.129 262.845 1.00 31.70  ? 3053 TRP A CE3   1 
ATOM   12030 C  CZ2   . TRP A 1 3053 ? 200.647 238.049 265.453 1.00 35.54  ? 3053 TRP A CZ2   1 
ATOM   12031 C  CZ3   . TRP A 1 3053 ? 199.918 238.122 263.154 1.00 35.63  ? 3053 TRP A CZ3   1 
ATOM   12032 C  CH2   . TRP A 1 3053 ? 199.843 237.592 264.446 1.00 37.54  ? 3053 TRP A CH2   1 
ATOM   12033 N  N     . PHE A 1 3054 ? 203.479 239.325 260.460 1.00 26.07  ? 3054 PHE A N     1 
ATOM   12034 C  CA    . PHE A 1 3054 ? 203.290 237.983 259.919 1.00 25.79  ? 3054 PHE A CA    1 
ATOM   12035 C  C     . PHE A 1 3054 ? 204.626 237.319 259.607 1.00 22.48  ? 3054 PHE A C     1 
ATOM   12036 O  O     . PHE A 1 3054 ? 204.826 236.135 259.905 1.00 26.50  ? 3054 PHE A O     1 
ATOM   12037 C  CB    . PHE A 1 3054 ? 202.417 238.052 258.666 1.00 26.22  ? 3054 PHE A CB    1 
ATOM   12038 C  CG    . PHE A 1 3054 ? 202.342 236.763 257.903 1.00 28.11  ? 3054 PHE A CG    1 
ATOM   12039 C  CD1   . PHE A 1 3054 ? 201.656 235.676 258.415 1.00 26.72  ? 3054 PHE A CD1   1 
ATOM   12040 C  CD2   . PHE A 1 3054 ? 202.943 236.642 256.662 1.00 28.34  ? 3054 PHE A CD2   1 
ATOM   12041 C  CE1   . PHE A 1 3054 ? 201.582 234.493 257.711 1.00 22.36  ? 3054 PHE A CE1   1 
ATOM   12042 C  CE2   . PHE A 1 3054 ? 202.872 235.461 255.954 1.00 23.15  ? 3054 PHE A CE2   1 
ATOM   12043 C  CZ    . PHE A 1 3054 ? 202.190 234.385 256.480 1.00 21.87  ? 3054 PHE A CZ    1 
ATOM   12044 N  N     . THR A 1 3055 ? 205.551 238.068 259.006 1.00 25.67  ? 3055 THR A N     1 
ATOM   12045 C  CA    . THR A 1 3055 ? 206.871 237.523 258.701 1.00 25.15  ? 3055 THR A CA    1 
ATOM   12046 C  C     . THR A 1 3055 ? 207.616 237.148 259.976 1.00 21.74  ? 3055 THR A C     1 
ATOM   12047 O  O     . THR A 1 3055 ? 208.263 236.097 260.040 1.00 20.21  ? 3055 THR A O     1 
ATOM   12048 C  CB    . THR A 1 3055 ? 207.679 238.529 257.881 1.00 24.04  ? 3055 THR A CB    1 
ATOM   12049 O  OG1   . THR A 1 3055 ? 207.035 238.743 256.620 1.00 31.18  ? 3055 THR A OG1   1 
ATOM   12050 C  CG2   . THR A 1 3055 ? 209.088 238.017 257.635 1.00 22.00  ? 3055 THR A CG2   1 
ATOM   12051 N  N     . SER A 1 3056 ? 207.534 237.997 261.003 1.00 19.11  ? 3056 SER A N     1 
ATOM   12052 C  CA    . SER A 1 3056 ? 208.186 237.686 262.271 1.00 18.86  ? 3056 SER A CA    1 
ATOM   12053 C  C     . SER A 1 3056 ? 207.596 236.430 262.899 1.00 19.88  ? 3056 SER A C     1 
ATOM   12054 O  O     . SER A 1 3056 ? 208.330 235.590 263.434 1.00 21.47  ? 3056 SER A O     1 
ATOM   12055 C  CB    . SER A 1 3056 ? 208.069 238.872 263.227 1.00 18.33  ? 3056 SER A CB    1 
ATOM   12056 O  OG    . SER A 1 3056 ? 206.739 239.032 263.685 1.00 26.22  ? 3056 SER A OG    1 
ATOM   12057 N  N     . GLN A 1 3057 ? 206.271 236.283 262.841 1.00 22.53  ? 3057 GLN A N     1 
ATOM   12058 C  CA    . GLN A 1 3057 ? 205.633 235.087 263.380 1.00 23.44  ? 3057 GLN A CA    1 
ATOM   12059 C  C     . GLN A 1 3057 ? 206.073 233.837 262.628 1.00 21.80  ? 3057 GLN A C     1 
ATOM   12060 O  O     . GLN A 1 3057 ? 206.369 232.804 263.243 1.00 24.91  ? 3057 GLN A O     1 
ATOM   12061 C  CB    . GLN A 1 3057 ? 204.113 235.237 263.325 1.00 26.47  ? 3057 GLN A CB    1 
ATOM   12062 C  CG    . GLN A 1 3057 ? 203.543 236.158 264.388 1.00 28.23  ? 3057 GLN A CG    1 
ATOM   12063 C  CD    . GLN A 1 3057 ? 203.652 235.574 265.779 1.00 28.35  ? 3057 GLN A CD    1 
ATOM   12064 O  OE1   . GLN A 1 3057 ? 204.499 235.983 266.572 1.00 31.46  ? 3057 GLN A OE1   1 
ATOM   12065 N  NE2   . GLN A 1 3057 ? 202.795 234.609 266.083 1.00 33.11  ? 3057 GLN A NE2   1 
ATOM   12066 N  N     . VAL A 1 3058 ? 206.130 233.911 261.296 1.00 20.15  ? 3058 VAL A N     1 
ATOM   12067 C  CA    . VAL A 1 3058 ? 206.580 232.767 260.508 1.00 19.31  ? 3058 VAL A CA    1 
ATOM   12068 C  C     . VAL A 1 3058 ? 208.022 232.416 260.851 1.00 21.94  ? 3058 VAL A C     1 
ATOM   12069 O  O     . VAL A 1 3058 ? 208.374 231.239 260.991 1.00 25.01  ? 3058 VAL A O     1 
ATOM   12070 C  CB    . VAL A 1 3058 ? 206.411 233.048 259.003 1.00 18.81  ? 3058 VAL A CB    1 
ATOM   12071 C  CG1   . VAL A 1 3058 ? 206.982 231.902 258.191 1.00 21.28  ? 3058 VAL A CG1   1 
ATOM   12072 C  CG2   . VAL A 1 3058 ? 204.948 233.247 258.665 1.00 20.80  ? 3058 VAL A CG2   1 
ATOM   12073 N  N     . ILE A 1 3059 ? 208.878 233.430 260.989 1.00 25.44  ? 3059 ILE A N     1 
ATOM   12074 C  CA    . ILE A 1 3059 ? 210.279 233.189 261.314 1.00 19.28  ? 3059 ILE A CA    1 
ATOM   12075 C  C     . ILE A 1 3059 ? 210.400 232.518 262.676 1.00 21.03  ? 3059 ILE A C     1 
ATOM   12076 O  O     . ILE A 1 3059 ? 211.179 231.575 262.856 1.00 30.02  ? 3059 ILE A O     1 
ATOM   12077 C  CB    . ILE A 1 3059 ? 211.071 234.509 261.257 1.00 19.63  ? 3059 ILE A CB    1 
ATOM   12078 C  CG1   . ILE A 1 3059 ? 211.437 234.846 259.811 1.00 22.73  ? 3059 ILE A CG1   1 
ATOM   12079 C  CG2   . ILE A 1 3059 ? 212.321 234.430 262.118 1.00 14.50  ? 3059 ILE A CG2   1 
ATOM   12080 C  CD1   . ILE A 1 3059 ? 212.255 236.106 259.667 1.00 18.37  ? 3059 ILE A CD1   1 
ATOM   12081 N  N     . ARG A 1 3060 ? 209.621 232.985 263.652 1.00 24.42  ? 3060 ARG A N     1 
ATOM   12082 C  CA    . ARG A 1 3060 ? 209.727 232.446 265.003 1.00 21.18  ? 3060 ARG A CA    1 
ATOM   12083 C  C     . ARG A 1 3060 ? 209.135 231.044 265.110 1.00 21.56  ? 3060 ARG A C     1 
ATOM   12084 O  O     . ARG A 1 3060 ? 209.601 230.243 265.927 1.00 27.16  ? 3060 ARG A O     1 
ATOM   12085 C  CB    . ARG A 1 3060 ? 209.046 233.394 265.988 1.00 21.40  ? 3060 ARG A CB    1 
ATOM   12086 C  CG    . ARG A 1 3060 ? 209.174 232.995 267.444 1.00 24.16  ? 3060 ARG A CG    1 
ATOM   12087 C  CD    . ARG A 1 3060 ? 208.908 234.188 268.360 1.00 31.84  ? 3060 ARG A CD    1 
ATOM   12088 N  NE    . ARG A 1 3060 ? 207.516 234.628 268.377 1.00 36.37  ? 3060 ARG A NE    1 
ATOM   12089 C  CZ    . ARG A 1 3060 ? 206.459 233.857 268.611 1.00 39.51  ? 3060 ARG A CZ    1 
ATOM   12090 N  NH1   . ARG A 1 3060 ? 206.586 232.581 268.941 1.00 36.87  ? 3060 ARG A NH1   1 
ATOM   12091 N  NH2   . ARG A 1 3060 ? 205.242 234.387 268.534 1.00 42.64  ? 3060 ARG A NH2   1 
ATOM   12092 N  N     . ASN A 1 3061 ? 208.129 230.720 264.299 1.00 21.42  ? 3061 ASN A N     1 
ATOM   12093 C  CA    . ASN A 1 3061 ? 207.392 229.471 264.465 1.00 16.71  ? 3061 ASN A CA    1 
ATOM   12094 C  C     . ASN A 1 3061 ? 207.851 228.355 263.533 1.00 18.44  ? 3061 ASN A C     1 
ATOM   12095 O  O     . ASN A 1 3061 ? 208.103 227.237 263.990 1.00 24.25  ? 3061 ASN A O     1 
ATOM   12096 C  CB    . ASN A 1 3061 ? 205.893 229.722 264.265 1.00 21.38  ? 3061 ASN A CB    1 
ATOM   12097 C  CG    . ASN A 1 3061 ? 205.259 230.435 265.441 1.00 24.09  ? 3061 ASN A CG    1 
ATOM   12098 O  OD1   . ASN A 1 3061 ? 205.576 230.156 266.596 1.00 24.89  ? 3061 ASN A OD1   1 
ATOM   12099 N  ND2   . ASN A 1 3061 ? 204.355 231.362 265.150 1.00 26.91  ? 3061 ASN A ND2   1 
ATOM   12100 N  N     . LEU A 1 3062 ? 207.962 228.629 262.236 1.00 14.68  ? 3062 LEU A N     1 
ATOM   12101 C  CA    . LEU A 1 3062 ? 208.161 227.572 261.250 1.00 12.64  ? 3062 LEU A CA    1 
ATOM   12102 C  C     . LEU A 1 3062 ? 209.589 227.040 261.292 1.00 18.65  ? 3062 LEU A C     1 
ATOM   12103 O  O     . LEU A 1 3062 ? 210.551 227.813 261.227 1.00 22.97  ? 3062 LEU A O     1 
ATOM   12104 C  CB    . LEU A 1 3062 ? 207.837 228.094 259.851 1.00 15.03  ? 3062 LEU A CB    1 
ATOM   12105 C  CG    . LEU A 1 3062 ? 207.867 227.086 258.701 1.00 15.28  ? 3062 LEU A CG    1 
ATOM   12106 C  CD1   . LEU A 1 3062 ? 207.048 225.858 259.048 1.00 16.06  ? 3062 LEU A CD1   1 
ATOM   12107 C  CD2   . LEU A 1 3062 ? 207.362 227.722 257.421 1.00 13.11  ? 3062 LEU A CD2   1 
ATOM   12108 N  N     . HIS A 1 3063 ? 209.725 225.718 261.392 1.00 13.45  ? 3063 HIS A N     1 
ATOM   12109 C  CA    . HIS A 1 3063 ? 211.013 225.038 261.319 1.00 10.99  ? 3063 HIS A CA    1 
ATOM   12110 C  C     . HIS A 1 3063 ? 210.962 224.042 260.171 1.00 10.12  ? 3063 HIS A C     1 
ATOM   12111 O  O     . HIS A 1 3063 ? 210.147 223.118 260.191 1.00 13.67  ? 3063 HIS A O     1 
ATOM   12112 C  CB    . HIS A 1 3063 ? 211.337 224.317 262.631 1.00 8.88   ? 3063 HIS A CB    1 
ATOM   12113 C  CG    . HIS A 1 3063 ? 211.356 225.211 263.829 1.00 9.76   ? 3063 HIS A CG    1 
ATOM   12114 N  ND1   . HIS A 1 3063 ? 210.268 225.367 264.659 1.00 11.46  ? 3063 HIS A ND1   1 
ATOM   12115 C  CD2   . HIS A 1 3063 ? 212.341 225.980 264.351 1.00 12.46  ? 3063 HIS A CD2   1 
ATOM   12116 C  CE1   . HIS A 1 3063 ? 210.576 226.203 265.634 1.00 13.88  ? 3063 HIS A CE1   1 
ATOM   12117 N  NE2   . HIS A 1 3063 ? 211.829 226.589 265.471 1.00 15.32  ? 3063 HIS A NE2   1 
ATOM   12118 N  N     . VAL A 1 3064 ? 211.839 224.213 259.189 1.00 9.24   ? 3064 VAL A N     1 
ATOM   12119 C  CA    . VAL A 1 3064 ? 211.853 223.373 257.994 1.00 8.68   ? 3064 VAL A CA    1 
ATOM   12120 C  C     . VAL A 1 3064 ? 212.943 222.321 258.140 1.00 10.86  ? 3064 VAL A C     1 
ATOM   12121 O  O     . VAL A 1 3064 ? 214.111 222.653 258.375 1.00 13.75  ? 3064 VAL A O     1 
ATOM   12122 C  CB    . VAL A 1 3064 ? 212.066 224.214 256.725 1.00 8.79   ? 3064 VAL A CB    1 
ATOM   12123 C  CG1   . VAL A 1 3064 ? 212.193 223.315 255.508 1.00 9.74   ? 3064 VAL A CG1   1 
ATOM   12124 C  CG2   . VAL A 1 3064 ? 210.928 225.201 256.548 1.00 11.45  ? 3064 VAL A CG2   1 
ATOM   12125 N  N     . VAL A 1 3065 ? 212.565 221.055 257.998 1.00 11.40  ? 3065 VAL A N     1 
ATOM   12126 C  CA    . VAL A 1 3065 ? 213.493 219.932 258.072 1.00 9.60   ? 3065 VAL A CA    1 
ATOM   12127 C  C     . VAL A 1 3065 ? 213.561 219.305 256.688 1.00 10.76  ? 3065 VAL A C     1 
ATOM   12128 O  O     . VAL A 1 3065 ? 212.599 218.671 256.236 1.00 15.68  ? 3065 VAL A O     1 
ATOM   12129 C  CB    . VAL A 1 3065 ? 213.064 218.901 259.123 1.00 10.49  ? 3065 VAL A CB    1 
ATOM   12130 C  CG1   . VAL A 1 3065 ? 214.168 217.884 259.342 1.00 11.07  ? 3065 VAL A CG1   1 
ATOM   12131 C  CG2   . VAL A 1 3065 ? 212.703 219.590 260.425 1.00 9.83   ? 3065 VAL A CG2   1 
ATOM   12132 N  N     . PHE A 1 3066 ? 214.700 219.459 256.023 1.00 11.89  ? 3066 PHE A N     1 
ATOM   12133 C  CA    . PHE A 1 3066 ? 214.912 218.924 254.686 1.00 10.43  ? 3066 PHE A CA    1 
ATOM   12134 C  C     . PHE A 1 3066 ? 215.744 217.653 254.786 1.00 14.14  ? 3066 PHE A C     1 
ATOM   12135 O  O     . PHE A 1 3066 ? 216.828 217.661 255.378 1.00 16.98  ? 3066 PHE A O     1 
ATOM   12136 C  CB    . PHE A 1 3066 ? 215.602 219.958 253.796 1.00 15.05  ? 3066 PHE A CB    1 
ATOM   12137 C  CG    . PHE A 1 3066 ? 215.317 219.786 252.334 1.00 22.57  ? 3066 PHE A CG    1 
ATOM   12138 C  CD1   . PHE A 1 3066 ? 216.105 218.958 251.554 1.00 25.44  ? 3066 PHE A CD1   1 
ATOM   12139 C  CD2   . PHE A 1 3066 ? 214.258 220.450 251.739 1.00 19.37  ? 3066 PHE A CD2   1 
ATOM   12140 C  CE1   . PHE A 1 3066 ? 215.846 218.797 250.208 1.00 28.10  ? 3066 PHE A CE1   1 
ATOM   12141 C  CE2   . PHE A 1 3066 ? 213.993 220.291 250.395 1.00 30.27  ? 3066 PHE A CE2   1 
ATOM   12142 C  CZ    . PHE A 1 3066 ? 214.788 219.464 249.627 1.00 35.39  ? 3066 PHE A CZ    1 
ATOM   12143 N  N     . THR A 1 3067 ? 215.236 216.565 254.216 1.00 14.07  ? 3067 THR A N     1 
ATOM   12144 C  CA    . THR A 1 3067 ? 215.912 215.274 254.231 1.00 15.26  ? 3067 THR A CA    1 
ATOM   12145 C  C     . THR A 1 3067 ? 216.262 214.868 252.807 1.00 21.26  ? 3067 THR A C     1 
ATOM   12146 O  O     . THR A 1 3067 ? 215.424 214.975 251.905 1.00 29.76  ? 3067 THR A O     1 
ATOM   12147 C  CB    . THR A 1 3067 ? 215.039 214.201 254.887 1.00 14.80  ? 3067 THR A CB    1 
ATOM   12148 O  OG1   . THR A 1 3067 ? 213.862 213.992 254.100 1.00 22.03  ? 3067 THR A OG1   1 
ATOM   12149 C  CG2   . THR A 1 3067 ? 214.639 214.624 256.291 1.00 12.40  ? 3067 THR A CG2   1 
ATOM   12150 N  N     . MET A 1 3068 ? 217.495 214.407 252.606 1.00 16.66  ? 3068 MET A N     1 
ATOM   12151 C  CA    . MET A 1 3068 ? 217.944 214.010 251.282 1.00 22.26  ? 3068 MET A CA    1 
ATOM   12152 C  C     . MET A 1 3068 ? 218.999 212.918 251.397 1.00 20.11  ? 3068 MET A C     1 
ATOM   12153 O  O     . MET A 1 3068 ? 219.723 212.834 252.392 1.00 17.37  ? 3068 MET A O     1 
ATOM   12154 C  CB    . MET A 1 3068 ? 218.499 215.206 250.500 1.00 23.94  ? 3068 MET A CB    1 
ATOM   12155 C  CG    . MET A 1 3068 ? 219.799 215.762 251.049 1.00 21.71  ? 3068 MET A CG    1 
ATOM   12156 S  SD    . MET A 1 3068 ? 220.178 217.396 250.396 1.00 48.94  ? 3068 MET A SD    1 
ATOM   12157 C  CE    . MET A 1 3068 ? 220.100 217.075 248.638 1.00 30.75  ? 3068 MET A CE    1 
ATOM   12158 N  N     . ASN A 1 3069 ? 219.072 212.081 250.364 1.00 20.37  ? 3069 ASN A N     1 
ATOM   12159 C  CA    . ASN A 1 3069 ? 220.096 211.054 250.303 1.00 18.40  ? 3069 ASN A CA    1 
ATOM   12160 C  C     . ASN A 1 3069 ? 221.451 211.675 249.966 1.00 25.59  ? 3069 ASN A C     1 
ATOM   12161 O  O     . ASN A 1 3069 ? 221.521 212.696 249.278 1.00 29.92  ? 3069 ASN A O     1 
ATOM   12162 C  CB    . ASN A 1 3069 ? 219.736 209.996 249.263 1.00 19.75  ? 3069 ASN A CB    1 
ATOM   12163 C  CG    . ASN A 1 3069 ? 218.472 209.240 249.615 1.00 24.07  ? 3069 ASN A CG    1 
ATOM   12164 O  OD1   . ASN A 1 3069 ? 218.418 208.515 250.606 1.00 28.13  ? 3069 ASN A OD1   1 
ATOM   12165 N  ND2   . ASN A 1 3069 ? 217.441 209.413 248.802 1.00 28.10  ? 3069 ASN A ND2   1 
ATOM   12166 N  N     . PRO A 1 3070 ? 222.547 211.070 250.435 1.00 26.44  ? 3070 PRO A N     1 
ATOM   12167 C  CA    . PRO A 1 3070 ? 223.886 211.653 250.214 1.00 24.03  ? 3070 PRO A CA    1 
ATOM   12168 C  C     . PRO A 1 3070 ? 224.455 211.371 248.825 1.00 30.02  ? 3070 PRO A C     1 
ATOM   12169 O  O     . PRO A 1 3070 ? 225.224 210.441 248.589 1.00 38.55  ? 3070 PRO A O     1 
ATOM   12170 C  CB    . PRO A 1 3070 ? 224.717 210.997 251.318 1.00 20.56  ? 3070 PRO A CB    1 
ATOM   12171 C  CG    . PRO A 1 3070 ? 224.085 209.666 251.508 1.00 20.79  ? 3070 PRO A CG    1 
ATOM   12172 C  CD    . PRO A 1 3070 ? 222.614 209.824 251.218 1.00 23.04  ? 3070 PRO A CD    1 
ATOM   12173 N  N     . SER A 1 3071 ? 224.060 212.202 247.868 1.00 34.14  ? 3071 SER A N     1 
ATOM   12174 C  CA    . SER A 1 3071 ? 224.599 212.133 246.519 1.00 42.86  ? 3071 SER A CA    1 
ATOM   12175 C  C     . SER A 1 3071 ? 225.777 213.088 246.372 1.00 48.82  ? 3071 SER A C     1 
ATOM   12176 O  O     . SER A 1 3071 ? 225.781 214.192 246.923 1.00 46.05  ? 3071 SER A O     1 
ATOM   12177 C  CB    . SER A 1 3071 ? 223.524 212.467 245.484 1.00 40.79  ? 3071 SER A CB    1 
ATOM   12178 O  OG    . SER A 1 3071 ? 224.057 212.441 244.172 1.00 36.95  ? 3071 SER A OG    1 
ATOM   12179 N  N     . SER A 1 3072 ? 226.784 212.647 245.617 1.00 50.95  ? 3072 SER A N     1 
ATOM   12180 C  CA    . SER A 1 3072 ? 227.972 213.469 245.409 1.00 53.23  ? 3072 SER A CA    1 
ATOM   12181 C  C     . SER A 1 3072 ? 227.646 214.700 244.572 1.00 51.57  ? 3072 SER A C     1 
ATOM   12182 O  O     . SER A 1 3072 ? 227.842 215.839 245.011 1.00 53.03  ? 3072 SER A O     1 
ATOM   12183 C  CB    . SER A 1 3072 ? 229.074 212.639 244.750 1.00 55.88  ? 3072 SER A CB    1 
ATOM   12184 O  OG    . SER A 1 3072 ? 229.369 211.484 245.516 1.00 53.01  ? 3072 SER A OG    1 
ATOM   12185 N  N     . GLU A 1 3073 ? 227.148 214.489 243.353 1.00 47.55  ? 3073 GLU A N     1 
ATOM   12186 C  CA    . GLU A 1 3073 ? 226.794 215.608 242.487 1.00 49.00  ? 3073 GLU A CA    1 
ATOM   12187 C  C     . GLU A 1 3073 ? 225.476 216.256 242.892 1.00 45.75  ? 3073 GLU A C     1 
ATOM   12188 O  O     . GLU A 1 3073 ? 225.255 217.437 242.598 1.00 49.34  ? 3073 GLU A O     1 
ATOM   12189 C  CB    . GLU A 1 3073 ? 226.732 215.145 241.030 1.00 56.89  ? 3073 GLU A CB    1 
ATOM   12190 C  CG    . GLU A 1 3073 ? 225.475 214.369 240.671 1.00 58.26  ? 3073 GLU A CG    1 
ATOM   12191 C  CD    . GLU A 1 3073 ? 225.658 212.871 240.811 1.00 63.44  ? 3073 GLU A CD    1 
ATOM   12192 O  OE1   . GLU A 1 3073 ? 226.722 212.443 241.307 1.00 55.25  ? 3073 GLU A OE1   1 
ATOM   12193 O  OE2   . GLU A 1 3073 ? 224.737 212.119 240.426 1.00 71.15  ? 3073 GLU A OE2   1 
ATOM   12194 N  N     . GLY A 1 3074 ? 224.592 215.507 243.555 1.00 43.32  ? 3074 GLY A N     1 
ATOM   12195 C  CA    . GLY A 1 3074 ? 223.319 216.076 243.967 1.00 42.12  ? 3074 GLY A CA    1 
ATOM   12196 C  C     . GLY A 1 3074 ? 223.480 217.198 244.973 1.00 41.23  ? 3074 GLY A C     1 
ATOM   12197 O  O     . GLY A 1 3074 ? 222.802 218.224 244.889 1.00 42.66  ? 3074 GLY A O     1 
ATOM   12198 N  N     . LEU A 1 3075 ? 224.382 217.019 245.940 1.00 36.20  ? 3075 LEU A N     1 
ATOM   12199 C  CA    . LEU A 1 3075 ? 224.633 218.071 246.919 1.00 36.23  ? 3075 LEU A CA    1 
ATOM   12200 C  C     . LEU A 1 3075 ? 225.242 219.302 246.261 1.00 41.20  ? 3075 LEU A C     1 
ATOM   12201 O  O     . LEU A 1 3075 ? 224.894 220.436 246.611 1.00 42.26  ? 3075 LEU A O     1 
ATOM   12202 C  CB    . LEU A 1 3075 ? 225.540 217.546 248.028 1.00 34.72  ? 3075 LEU A CB    1 
ATOM   12203 C  CG    . LEU A 1 3075 ? 225.239 218.116 249.410 1.00 31.25  ? 3075 LEU A CG    1 
ATOM   12204 C  CD1   . LEU A 1 3075 ? 223.816 217.778 249.803 1.00 27.66  ? 3075 LEU A CD1   1 
ATOM   12205 C  CD2   . LEU A 1 3075 ? 226.221 217.577 250.431 1.00 26.91  ? 3075 LEU A CD2   1 
ATOM   12206 N  N     . LYS A 1 3076 ? 226.152 219.100 245.305 1.00 39.20  ? 3076 LYS A N     1 
ATOM   12207 C  CA    . LYS A 1 3076 ? 226.724 220.230 244.581 1.00 33.90  ? 3076 LYS A CA    1 
ATOM   12208 C  C     . LYS A 1 3076 ? 225.653 220.979 243.798 1.00 35.92  ? 3076 LYS A C     1 
ATOM   12209 O  O     . LYS A 1 3076 ? 225.656 222.215 243.752 1.00 44.86  ? 3076 LYS A O     1 
ATOM   12210 C  CB    . LYS A 1 3076 ? 227.834 219.748 243.648 1.00 29.87  ? 3076 LYS A CB    1 
ATOM   12211 C  CG    . LYS A 1 3076 ? 228.959 219.005 244.350 1.00 31.78  ? 3076 LYS A CG    1 
ATOM   12212 C  CD    . LYS A 1 3076 ? 230.244 219.056 243.541 1.00 31.73  ? 3076 LYS A CD    1 
ATOM   12213 C  CE    . LYS A 1 3076 ? 231.074 217.801 243.746 1.00 32.19  ? 3076 LYS A CE    1 
ATOM   12214 N  NZ    . LYS A 1 3076 ? 231.970 217.911 244.929 1.00 41.23  ? 3076 LYS A NZ    1 
ATOM   12215 N  N     . ASP A 1 3077 ? 224.732 220.247 243.169 1.00 31.08  ? 3077 ASP A N     1 
ATOM   12216 C  CA    . ASP A 1 3077 ? 223.648 220.893 242.436 1.00 38.78  ? 3077 ASP A CA    1 
ATOM   12217 C  C     . ASP A 1 3077 ? 222.726 221.665 243.373 1.00 40.16  ? 3077 ASP A C     1 
ATOM   12218 O  O     . ASP A 1 3077 ? 222.294 222.779 243.051 1.00 39.36  ? 3077 ASP A O     1 
ATOM   12219 C  CB    . ASP A 1 3077 ? 222.860 219.852 241.641 1.00 48.90  ? 3077 ASP A CB    1 
ATOM   12220 C  CG    . ASP A 1 3077 ? 223.659 219.266 240.494 1.00 59.42  ? 3077 ASP A CG    1 
ATOM   12221 O  OD1   . ASP A 1 3077 ? 224.537 219.973 239.956 1.00 57.15  ? 3077 ASP A OD1   1 
ATOM   12222 O  OD2   . ASP A 1 3077 ? 223.410 218.098 240.129 1.00 57.08  ? 3077 ASP A OD2   1 
ATOM   12223 N  N     . ARG A 1 3078 ? 222.410 221.087 244.535 1.00 43.71  ? 3078 ARG A N     1 
ATOM   12224 C  CA    . ARG A 1 3078 ? 221.558 221.779 245.498 1.00 39.62  ? 3078 ARG A CA    1 
ATOM   12225 C  C     . ARG A 1 3078 ? 222.244 223.007 246.081 1.00 37.12  ? 3078 ARG A C     1 
ATOM   12226 O  O     . ARG A 1 3078 ? 221.568 223.975 246.446 1.00 32.40  ? 3078 ARG A O     1 
ATOM   12227 C  CB    . ARG A 1 3078 ? 221.145 220.828 246.620 1.00 39.26  ? 3078 ARG A CB    1 
ATOM   12228 C  CG    . ARG A 1 3078 ? 220.289 219.661 246.175 1.00 37.55  ? 3078 ARG A CG    1 
ATOM   12229 C  CD    . ARG A 1 3078 ? 218.907 220.111 245.742 1.00 34.71  ? 3078 ARG A CD    1 
ATOM   12230 N  NE    . ARG A 1 3078 ? 218.051 218.976 245.422 1.00 51.80  ? 3078 ARG A NE    1 
ATOM   12231 C  CZ    . ARG A 1 3078 ? 217.934 218.444 244.213 1.00 58.27  ? 3078 ARG A CZ    1 
ATOM   12232 N  NH1   . ARG A 1 3078 ? 218.608 218.921 243.179 1.00 52.60  ? 3078 ARG A NH1   1 
ATOM   12233 N  NH2   . ARG A 1 3078 ? 217.122 217.405 244.037 1.00 53.82  ? 3078 ARG A NH2   1 
ATOM   12234 N  N     . ALA A 1 3079 ? 223.575 222.986 246.183 1.00 36.52  ? 3079 ALA A N     1 
ATOM   12235 C  CA    . ALA A 1 3079 ? 224.298 224.139 246.704 1.00 33.33  ? 3079 ALA A CA    1 
ATOM   12236 C  C     . ALA A 1 3079 ? 224.117 225.376 245.835 1.00 38.88  ? 3079 ALA A C     1 
ATOM   12237 O  O     . ALA A 1 3079 ? 224.252 226.497 246.338 1.00 33.84  ? 3079 ALA A O     1 
ATOM   12238 C  CB    . ALA A 1 3079 ? 225.785 223.810 246.841 1.00 28.78  ? 3079 ALA A CB    1 
ATOM   12239 N  N     . ALA A 1 3080 ? 223.809 225.201 244.553 1.00 37.02  ? 3080 ALA A N     1 
ATOM   12240 C  CA    . ALA A 1 3080 ? 223.515 226.309 243.654 1.00 34.96  ? 3080 ALA A CA    1 
ATOM   12241 C  C     . ALA A 1 3080 ? 222.028 226.547 243.464 1.00 29.35  ? 3080 ALA A C     1 
ATOM   12242 O  O     . ALA A 1 3080 ? 221.598 227.699 243.390 1.00 28.59  ? 3080 ALA A O     1 
ATOM   12243 C  CB    . ALA A 1 3080 ? 224.164 226.067 242.286 1.00 33.02  ? 3080 ALA A CB    1 
ATOM   12244 N  N     . THR A 1 3081 ? 221.227 225.482 243.382 1.00 30.81  ? 3081 THR A N     1 
ATOM   12245 C  CA    . THR A 1 3081 ? 219.788 225.655 243.212 1.00 31.69  ? 3081 THR A CA    1 
ATOM   12246 C  C     . THR A 1 3081 ? 219.154 226.289 244.445 1.00 34.89  ? 3081 THR A C     1 
ATOM   12247 O  O     . THR A 1 3081 ? 218.266 227.141 244.324 1.00 40.10  ? 3081 THR A O     1 
ATOM   12248 C  CB    . THR A 1 3081 ? 219.132 224.310 242.899 1.00 36.63  ? 3081 THR A CB    1 
ATOM   12249 O  OG1   . THR A 1 3081 ? 219.737 223.742 241.731 1.00 33.92  ? 3081 THR A OG1   1 
ATOM   12250 C  CG2   . THR A 1 3081 ? 217.644 224.487 242.649 1.00 34.70  ? 3081 THR A CG2   1 
ATOM   12251 N  N     . SER A 1 3082 ? 219.586 225.885 245.638 1.00 31.96  ? 3082 SER A N     1 
ATOM   12252 C  CA    . SER A 1 3082 ? 219.069 226.421 246.898 1.00 26.64  ? 3082 SER A CA    1 
ATOM   12253 C  C     . SER A 1 3082 ? 220.239 226.775 247.805 1.00 26.09  ? 3082 SER A C     1 
ATOM   12254 O  O     . SER A 1 3082 ? 220.666 225.961 248.635 1.00 25.04  ? 3082 SER A O     1 
ATOM   12255 C  CB    . SER A 1 3082 ? 218.128 225.427 247.579 1.00 28.66  ? 3082 SER A CB    1 
ATOM   12256 O  OG    . SER A 1 3082 ? 217.480 226.020 248.690 1.00 24.81  ? 3082 SER A OG    1 
ATOM   12257 N  N     . PRO A 1 3083 ? 220.793 227.981 247.664 1.00 20.95  ? 3083 PRO A N     1 
ATOM   12258 C  CA    . PRO A 1 3083 ? 221.894 228.382 248.558 1.00 20.16  ? 3083 PRO A CA    1 
ATOM   12259 C  C     . PRO A 1 3083 ? 221.506 228.412 250.028 1.00 17.15  ? 3083 PRO A C     1 
ATOM   12260 O  O     . PRO A 1 3083 ? 222.336 228.086 250.885 1.00 23.09  ? 3083 PRO A O     1 
ATOM   12261 C  CB    . PRO A 1 3083 ? 222.272 229.775 248.034 1.00 17.50  ? 3083 PRO A CB    1 
ATOM   12262 C  CG    . PRO A 1 3083 ? 221.048 230.262 247.337 1.00 20.59  ? 3083 PRO A CG    1 
ATOM   12263 C  CD    . PRO A 1 3083 ? 220.433 229.047 246.717 1.00 17.40  ? 3083 PRO A CD    1 
ATOM   12264 N  N     . ALA A 1 3084 ? 220.263 228.784 250.346 1.00 14.40  ? 3084 ALA A N     1 
ATOM   12265 C  CA    . ALA A 1 3084 ? 219.843 228.859 251.740 1.00 15.91  ? 3084 ALA A CA    1 
ATOM   12266 C  C     . ALA A 1 3084 ? 219.844 227.499 252.422 1.00 19.83  ? 3084 ALA A C     1 
ATOM   12267 O  O     . ALA A 1 3084 ? 219.902 227.437 253.655 1.00 18.93  ? 3084 ALA A O     1 
ATOM   12268 C  CB    . ALA A 1 3084 ? 218.456 229.489 251.848 1.00 17.85  ? 3084 ALA A CB    1 
ATOM   12269 N  N     . LEU A 1 3085 ? 219.784 226.409 251.655 1.00 20.00  ? 3085 LEU A N     1 
ATOM   12270 C  CA    . LEU A 1 3085 ? 219.893 225.083 252.248 1.00 15.91  ? 3085 LEU A CA    1 
ATOM   12271 C  C     . LEU A 1 3085 ? 221.268 224.836 252.850 1.00 15.54  ? 3085 LEU A C     1 
ATOM   12272 O  O     . LEU A 1 3085 ? 221.436 223.869 253.600 1.00 23.16  ? 3085 LEU A O     1 
ATOM   12273 C  CB    . LEU A 1 3085 ? 219.584 224.011 251.203 1.00 18.44  ? 3085 LEU A CB    1 
ATOM   12274 C  CG    . LEU A 1 3085 ? 218.149 223.488 251.146 1.00 14.92  ? 3085 LEU A CG    1 
ATOM   12275 C  CD1   . LEU A 1 3085 ? 218.038 222.359 250.137 1.00 14.29  ? 3085 LEU A CD1   1 
ATOM   12276 C  CD2   . LEU A 1 3085 ? 217.689 223.028 252.517 1.00 14.58  ? 3085 LEU A CD2   1 
ATOM   12277 N  N     . PHE A 1 3086 ? 222.253 225.680 252.540 1.00 15.99  ? 3086 PHE A N     1 
ATOM   12278 C  CA    . PHE A 1 3086 ? 223.606 225.493 253.034 1.00 20.77  ? 3086 PHE A CA    1 
ATOM   12279 C  C     . PHE A 1 3086 ? 224.137 226.665 253.846 1.00 20.31  ? 3086 PHE A C     1 
ATOM   12280 O  O     . PHE A 1 3086 ? 225.223 226.547 254.424 1.00 24.06  ? 3086 PHE A O     1 
ATOM   12281 C  CB    . PHE A 1 3086 ? 224.560 225.209 251.865 1.00 15.44  ? 3086 PHE A CB    1 
ATOM   12282 C  CG    . PHE A 1 3086 ? 224.329 223.876 251.216 1.00 20.01  ? 3086 PHE A CG    1 
ATOM   12283 C  CD1   . PHE A 1 3086 ? 223.321 223.712 250.283 1.00 22.13  ? 3086 PHE A CD1   1 
ATOM   12284 C  CD2   . PHE A 1 3086 ? 225.106 222.783 251.554 1.00 25.22  ? 3086 PHE A CD2   1 
ATOM   12285 C  CE1   . PHE A 1 3086 ? 223.099 222.485 249.692 1.00 27.30  ? 3086 PHE A CE1   1 
ATOM   12286 C  CE2   . PHE A 1 3086 ? 224.889 221.555 250.965 1.00 25.37  ? 3086 PHE A CE2   1 
ATOM   12287 C  CZ    . PHE A 1 3086 ? 223.883 221.407 250.034 1.00 28.05  ? 3086 PHE A CZ    1 
ATOM   12288 N  N     . ASN A 1 3087 ? 223.369 227.756 253.927 1.00 17.65  ? 3087 ASN A N     1 
ATOM   12289 C  CA    . ASN A 1 3087 ? 223.796 228.918 254.759 1.00 19.31  ? 3087 ASN A CA    1 
ATOM   12290 C  C     . ASN A 1 3087 ? 222.725 229.235 255.810 1.00 17.82  ? 3087 ASN A C     1 
ATOM   12291 O  O     . ASN A 1 3087 ? 223.077 229.844 256.841 1.00 22.96  ? 3087 ASN A O     1 
ATOM   12292 C  CB    . ASN A 1 3087 ? 224.162 230.124 253.898 1.00 22.48  ? 3087 ASN A CB    1 
ATOM   12293 C  CG    . ASN A 1 3087 ? 223.070 230.507 252.929 1.00 24.65  ? 3087 ASN A CG    1 
ATOM   12294 O  OD1   . ASN A 1 3087 ? 221.963 230.863 253.345 1.00 25.32  ? 3087 ASN A OD1   1 
ATOM   12295 N  ND2   . ASN A 1 3087 ? 223.365 230.458 251.639 1.00 27.56  ? 3087 ASN A ND2   1 
ATOM   12296 N  N     . ARG A 1 3088 ? 221.475 228.840 255.564 1.00 13.94  ? 3088 ARG A N     1 
ATOM   12297 C  CA    . ARG A 1 3088 ? 220.399 229.095 256.509 1.00 15.40  ? 3088 ARG A CA    1 
ATOM   12298 C  C     . ARG A 1 3088 ? 219.962 227.857 257.276 1.00 12.73  ? 3088 ARG A C     1 
ATOM   12299 O  O     . ARG A 1 3088 ? 219.254 227.991 258.277 1.00 14.16  ? 3088 ARG A O     1 
ATOM   12300 C  CB    . ARG A 1 3088 ? 219.178 229.684 255.789 1.00 19.32  ? 3088 ARG A CB    1 
ATOM   12301 C  CG    . ARG A 1 3088 ? 219.396 231.061 255.190 1.00 17.76  ? 3088 ARG A CG    1 
ATOM   12302 C  CD    . ARG A 1 3088 ? 219.784 232.073 256.251 1.00 18.58  ? 3088 ARG A CD    1 
ATOM   12303 N  NE    . ARG A 1 3088 ? 219.431 233.435 255.864 1.00 35.48  ? 3088 ARG A NE    1 
ATOM   12304 C  CZ    . ARG A 1 3088 ? 220.074 234.149 254.950 1.00 39.57  ? 3088 ARG A CZ    1 
ATOM   12305 N  NH1   . ARG A 1 3088 ? 221.124 233.667 254.307 1.00 28.71  ? 3088 ARG A NH1   1 
ATOM   12306 N  NH2   . ARG A 1 3088 ? 219.650 235.379 254.673 1.00 30.39  ? 3088 ARG A NH2   1 
ATOM   12307 N  N     . CYS A 1 3089 ? 220.361 226.669 256.835 1.00 16.18  ? 3089 CYS A N     1 
ATOM   12308 C  CA    . CYS A 1 3089 ? 219.989 225.420 257.483 1.00 12.93  ? 3089 CYS A CA    1 
ATOM   12309 C  C     . CYS A 1 3089 ? 221.200 224.813 258.176 1.00 11.62  ? 3089 CYS A C     1 
ATOM   12310 O  O     . CYS A 1 3089 ? 222.326 224.907 257.677 1.00 15.94  ? 3089 CYS A O     1 
ATOM   12311 C  CB    . CYS A 1 3089 ? 219.424 224.422 256.470 1.00 8.40   ? 3089 CYS A CB    1 
ATOM   12312 S  SG    . CYS A 1 3089 ? 217.881 224.921 255.683 1.00 22.01  ? 3089 CYS A SG    1 
ATOM   12313 N  N     . VAL A 1 3090 ? 220.966 224.198 259.330 1.00 12.96  ? 3090 VAL A N     1 
ATOM   12314 C  CA    . VAL A 1 3090 ? 222.001 223.437 260.018 1.00 10.35  ? 3090 VAL A CA    1 
ATOM   12315 C  C     . VAL A 1 3090 ? 222.083 222.063 259.367 1.00 12.37  ? 3090 VAL A C     1 
ATOM   12316 O  O     . VAL A 1 3090 ? 221.083 221.341 259.293 1.00 17.66  ? 3090 VAL A O     1 
ATOM   12317 C  CB    . VAL A 1 3090 ? 221.704 223.325 261.518 1.00 8.00   ? 3090 VAL A CB    1 
ATOM   12318 C  CG1   . VAL A 1 3090 ? 222.642 222.326 262.171 1.00 9.95   ? 3090 VAL A CG1   1 
ATOM   12319 C  CG2   . VAL A 1 3090 ? 221.819 224.684 262.181 1.00 15.05  ? 3090 VAL A CG2   1 
ATOM   12320 N  N     . LEU A 1 3091 ? 223.268 221.703 258.885 1.00 9.36   ? 3091 LEU A N     1 
ATOM   12321 C  CA    . LEU A 1 3091 ? 223.463 220.460 258.154 1.00 8.44   ? 3091 LEU A CA    1 
ATOM   12322 C  C     . LEU A 1 3091 ? 223.909 219.368 259.119 1.00 15.54  ? 3091 LEU A C     1 
ATOM   12323 O  O     . LEU A 1 3091 ? 224.900 219.535 259.838 1.00 16.84  ? 3091 LEU A O     1 
ATOM   12324 C  CB    . LEU A 1 3091 ? 224.488 220.649 257.037 1.00 9.00   ? 3091 LEU A CB    1 
ATOM   12325 C  CG    . LEU A 1 3091 ? 224.539 219.601 255.924 1.00 9.79   ? 3091 LEU A CG    1 
ATOM   12326 C  CD1   . LEU A 1 3091 ? 224.938 220.253 254.614 1.00 11.67  ? 3091 LEU A CD1   1 
ATOM   12327 C  CD2   . LEU A 1 3091 ? 225.500 218.477 256.268 1.00 13.53  ? 3091 LEU A CD2   1 
ATOM   12328 N  N     . ASN A 1 3092 ? 223.178 218.256 259.133 1.00 18.04  ? 3092 ASN A N     1 
ATOM   12329 C  CA    . ASN A 1 3092 ? 223.517 217.095 259.946 1.00 12.65  ? 3092 ASN A CA    1 
ATOM   12330 C  C     . ASN A 1 3092 ? 223.700 215.900 259.024 1.00 16.00  ? 3092 ASN A C     1 
ATOM   12331 O  O     . ASN A 1 3092 ? 222.758 215.495 258.331 1.00 16.44  ? 3092 ASN A O     1 
ATOM   12332 C  CB    . ASN A 1 3092 ? 222.435 216.815 260.990 1.00 13.37  ? 3092 ASN A CB    1 
ATOM   12333 C  CG    . ASN A 1 3092 ? 222.537 217.728 262.192 1.00 23.72  ? 3092 ASN A CG    1 
ATOM   12334 O  OD1   . ASN A 1 3092 ? 223.588 218.313 262.454 1.00 27.12  ? 3092 ASN A OD1   1 
ATOM   12335 N  ND2   . ASN A 1 3092 ? 221.444 217.856 262.932 1.00 25.12  ? 3092 ASN A ND2   1 
ATOM   12336 N  N     . TRP A 1 3093 ? 224.904 215.334 259.025 1.00 15.72  ? 3093 TRP A N     1 
ATOM   12337 C  CA    . TRP A 1 3093 ? 225.231 214.188 258.180 1.00 13.35  ? 3093 TRP A CA    1 
ATOM   12338 C  C     . TRP A 1 3093 ? 224.994 212.916 258.981 1.00 16.71  ? 3093 TRP A C     1 
ATOM   12339 O  O     . TRP A 1 3093 ? 225.860 212.448 259.720 1.00 22.30  ? 3093 TRP A O     1 
ATOM   12340 C  CB    . TRP A 1 3093 ? 226.665 214.275 257.678 1.00 12.50  ? 3093 TRP A CB    1 
ATOM   12341 C  CG    . TRP A 1 3093 ? 226.899 213.485 256.436 1.00 13.13  ? 3093 TRP A CG    1 
ATOM   12342 C  CD1   . TRP A 1 3093 ? 227.179 212.154 256.352 1.00 11.89  ? 3093 TRP A CD1   1 
ATOM   12343 C  CD2   . TRP A 1 3093 ? 226.858 213.973 255.092 1.00 13.74  ? 3093 TRP A CD2   1 
ATOM   12344 N  NE1   . TRP A 1 3093 ? 227.323 211.784 255.038 1.00 10.57  ? 3093 TRP A NE1   1 
ATOM   12345 C  CE2   . TRP A 1 3093 ? 227.131 212.884 254.244 1.00 10.31  ? 3093 TRP A CE2   1 
ATOM   12346 C  CE3   . TRP A 1 3093 ? 226.625 215.228 254.522 1.00 12.95  ? 3093 TRP A CE3   1 
ATOM   12347 C  CZ2   . TRP A 1 3093 ? 227.174 213.009 252.860 1.00 12.98  ? 3093 TRP A CZ2   1 
ATOM   12348 C  CZ3   . TRP A 1 3093 ? 226.665 215.350 253.149 1.00 12.33  ? 3093 TRP A CZ3   1 
ATOM   12349 C  CH2   . TRP A 1 3093 ? 226.938 214.248 252.332 1.00 14.40  ? 3093 TRP A CH2   1 
ATOM   12350 N  N     . PHE A 1 3094 ? 223.796 212.352 258.832 1.00 14.65  ? 3094 PHE A N     1 
ATOM   12351 C  CA    . PHE A 1 3094 ? 223.504 211.076 259.472 1.00 11.76  ? 3094 PHE A CA    1 
ATOM   12352 C  C     . PHE A 1 3094 ? 224.190 209.934 258.733 1.00 14.97  ? 3094 PHE A C     1 
ATOM   12353 O  O     . PHE A 1 3094 ? 224.726 209.013 259.360 1.00 21.67  ? 3094 PHE A O     1 
ATOM   12354 C  CB    . PHE A 1 3094 ? 221.992 210.851 259.529 1.00 16.44  ? 3094 PHE A CB    1 
ATOM   12355 C  CG    . PHE A 1 3094 ? 221.274 211.736 260.512 1.00 17.48  ? 3094 PHE A CG    1 
ATOM   12356 C  CD1   . PHE A 1 3094 ? 221.960 212.678 261.260 1.00 20.11  ? 3094 PHE A CD1   1 
ATOM   12357 C  CD2   . PHE A 1 3094 ? 219.905 211.627 260.681 1.00 17.48  ? 3094 PHE A CD2   1 
ATOM   12358 C  CE1   . PHE A 1 3094 ? 221.294 213.491 262.156 1.00 18.14  ? 3094 PHE A CE1   1 
ATOM   12359 C  CE2   . PHE A 1 3094 ? 219.235 212.435 261.577 1.00 19.63  ? 3094 PHE A CE2   1 
ATOM   12360 C  CZ    . PHE A 1 3094 ? 219.930 213.368 262.315 1.00 19.62  ? 3094 PHE A CZ    1 
ATOM   12361 N  N     . GLY A 1 3095 ? 224.190 209.985 257.403 1.00 11.35  ? 3095 GLY A N     1 
ATOM   12362 C  CA    . GLY A 1 3095 ? 224.801 208.964 256.579 1.00 9.17   ? 3095 GLY A CA    1 
ATOM   12363 C  C     . GLY A 1 3095 ? 224.097 207.629 256.724 1.00 16.67  ? 3095 GLY A C     1 
ATOM   12364 O  O     . GLY A 1 3095 ? 222.883 207.546 256.940 1.00 18.98  ? 3095 GLY A O     1 
ATOM   12365 N  N     . ASP A 1 3096 ? 224.875 206.562 256.589 1.00 18.13  ? 3096 ASP A N     1 
ATOM   12366 C  CA    . ASP A 1 3096 ? 224.398 205.218 256.869 1.00 13.03  ? 3096 ASP A CA    1 
ATOM   12367 C  C     . ASP A 1 3096 ? 224.678 204.864 258.324 1.00 13.01  ? 3096 ASP A C     1 
ATOM   12368 O  O     . ASP A 1 3096 ? 225.472 205.514 259.006 1.00 17.82  ? 3096 ASP A O     1 
ATOM   12369 C  CB    . ASP A 1 3096 ? 225.063 204.201 255.939 1.00 19.31  ? 3096 ASP A CB    1 
ATOM   12370 C  CG    . ASP A 1 3096 ? 224.246 202.931 255.781 1.00 27.18  ? 3096 ASP A CG    1 
ATOM   12371 O  OD1   . ASP A 1 3096 ? 223.838 202.347 256.808 1.00 23.46  ? 3096 ASP A OD1   1 
ATOM   12372 O  OD2   . ASP A 1 3096 ? 224.012 202.512 254.628 1.00 33.94  ? 3096 ASP A OD2   1 
ATOM   12373 N  N     . TRP A 1 3097 ? 224.004 203.821 258.799 1.00 13.11  ? 3097 TRP A N     1 
ATOM   12374 C  CA    . TRP A 1 3097 ? 224.259 203.328 260.143 1.00 11.14  ? 3097 TRP A CA    1 
ATOM   12375 C  C     . TRP A 1 3097 ? 225.679 202.789 260.230 1.00 19.27  ? 3097 TRP A C     1 
ATOM   12376 O  O     . TRP A 1 3097 ? 226.120 202.026 259.364 1.00 19.11  ? 3097 TRP A O     1 
ATOM   12377 C  CB    . TRP A 1 3097 ? 223.253 202.244 260.517 1.00 8.71   ? 3097 TRP A CB    1 
ATOM   12378 C  CG    . TRP A 1 3097 ? 221.888 202.772 260.810 1.00 10.32  ? 3097 TRP A CG    1 
ATOM   12379 C  CD1   . TRP A 1 3097 ? 221.456 204.054 260.651 1.00 8.65   ? 3097 TRP A CD1   1 
ATOM   12380 C  CD2   . TRP A 1 3097 ? 220.774 202.032 261.319 1.00 10.40  ? 3097 TRP A CD2   1 
ATOM   12381 N  NE1   . TRP A 1 3097 ? 220.140 204.158 261.026 1.00 9.80   ? 3097 TRP A NE1   1 
ATOM   12382 C  CE2   . TRP A 1 3097 ? 219.697 202.931 261.440 1.00 9.84   ? 3097 TRP A CE2   1 
ATOM   12383 C  CE3   . TRP A 1 3097 ? 220.580 200.696 261.680 1.00 9.76   ? 3097 TRP A CE3   1 
ATOM   12384 C  CZ2   . TRP A 1 3097 ? 218.448 202.537 261.907 1.00 11.12  ? 3097 TRP A CZ2   1 
ATOM   12385 C  CZ3   . TRP A 1 3097 ? 219.340 200.309 262.144 1.00 10.80  ? 3097 TRP A CZ3   1 
ATOM   12386 C  CH2   . TRP A 1 3097 ? 218.290 201.225 262.253 1.00 11.79  ? 3097 TRP A CH2   1 
ATOM   12387 N  N     . SER A 1 3098 ? 226.397 203.188 261.274 1.00 22.57  ? 3098 SER A N     1 
ATOM   12388 C  CA    . SER A 1 3098 ? 227.774 202.760 261.438 1.00 15.98  ? 3098 SER A CA    1 
ATOM   12389 C  C     . SER A 1 3098 ? 227.831 201.282 261.819 1.00 17.66  ? 3098 SER A C     1 
ATOM   12390 O  O     . SER A 1 3098 ? 226.814 200.632 262.074 1.00 19.18  ? 3098 SER A O     1 
ATOM   12391 C  CB    . SER A 1 3098 ? 228.475 203.607 262.498 1.00 17.54  ? 3098 SER A CB    1 
ATOM   12392 O  OG    . SER A 1 3098 ? 227.790 203.542 263.735 1.00 15.36  ? 3098 SER A OG    1 
ATOM   12393 N  N     . THR A 1 3099 ? 229.054 200.750 261.848 1.00 16.38  ? 3099 THR A N     1 
ATOM   12394 C  CA    . THR A 1 3099 ? 229.249 199.386 262.325 1.00 15.76  ? 3099 THR A CA    1 
ATOM   12395 C  C     . THR A 1 3099 ? 228.795 199.250 263.772 1.00 16.82  ? 3099 THR A C     1 
ATOM   12396 O  O     . THR A 1 3099 ? 228.170 198.251 264.146 1.00 19.69  ? 3099 THR A O     1 
ATOM   12397 C  CB    . THR A 1 3099 ? 230.716 198.985 262.181 1.00 20.20  ? 3099 THR A CB    1 
ATOM   12398 O  OG1   . THR A 1 3099 ? 231.154 199.252 260.843 1.00 26.47  ? 3099 THR A OG1   1 
ATOM   12399 C  CG2   . THR A 1 3099 ? 230.900 197.509 262.482 1.00 19.17  ? 3099 THR A CG2   1 
ATOM   12400 N  N     . GLU A 1 3100 ? 229.096 200.253 264.599 1.00 17.11  ? 3100 GLU A N     1 
ATOM   12401 C  CA    . GLU A 1 3100 ? 228.626 200.246 265.980 1.00 16.10  ? 3100 GLU A CA    1 
ATOM   12402 C  C     . GLU A 1 3100 ? 227.106 200.284 266.045 1.00 13.70  ? 3100 GLU A C     1 
ATOM   12403 O  O     . GLU A 1 3100 ? 226.497 199.595 266.870 1.00 13.35  ? 3100 GLU A O     1 
ATOM   12404 C  CB    . GLU A 1 3100 ? 229.224 201.428 266.743 1.00 22.57  ? 3100 GLU A CB    1 
ATOM   12405 C  CG    . GLU A 1 3100 ? 228.761 201.533 268.185 1.00 28.07  ? 3100 GLU A CG    1 
ATOM   12406 C  CD    . GLU A 1 3100 ? 228.854 202.945 268.724 1.00 37.41  ? 3100 GLU A CD    1 
ATOM   12407 O  OE1   . GLU A 1 3100 ? 228.913 203.889 267.909 1.00 40.01  ? 3100 GLU A OE1   1 
ATOM   12408 O  OE2   . GLU A 1 3100 ? 228.866 203.112 269.962 1.00 35.26  ? 3100 GLU A OE2   1 
ATOM   12409 N  N     . ALA A 1 3101 ? 226.475 201.092 265.188 1.00 15.24  ? 3101 ALA A N     1 
ATOM   12410 C  CA    . ALA A 1 3101 ? 225.017 201.167 265.180 1.00 13.25  ? 3101 ALA A CA    1 
ATOM   12411 C  C     . ALA A 1 3101 ? 224.395 199.832 264.794 1.00 14.71  ? 3101 ALA A C     1 
ATOM   12412 O  O     . ALA A 1 3101 ? 223.434 199.380 265.429 1.00 15.97  ? 3101 ALA A O     1 
ATOM   12413 C  CB    . ALA A 1 3101 ? 224.556 202.269 264.228 1.00 16.09  ? 3101 ALA A CB    1 
ATOM   12414 N  N     . LEU A 1 3102 ? 224.931 199.186 263.755 1.00 15.60  ? 3102 LEU A N     1 
ATOM   12415 C  CA    . LEU A 1 3102 ? 224.431 197.875 263.356 1.00 9.77   ? 3102 LEU A CA    1 
ATOM   12416 C  C     . LEU A 1 3102 ? 224.630 196.853 264.464 1.00 10.03  ? 3102 LEU A C     1 
ATOM   12417 O  O     . LEU A 1 3102 ? 223.738 196.041 264.740 1.00 13.47  ? 3102 LEU A O     1 
ATOM   12418 C  CB    . LEU A 1 3102 ? 225.129 197.413 262.078 1.00 11.72  ? 3102 LEU A CB    1 
ATOM   12419 C  CG    . LEU A 1 3102 ? 224.913 198.235 260.808 1.00 11.55  ? 3102 LEU A CG    1 
ATOM   12420 C  CD1   . LEU A 1 3102 ? 225.799 197.710 259.694 1.00 12.44  ? 3102 LEU A CD1   1 
ATOM   12421 C  CD2   . LEU A 1 3102 ? 223.454 198.200 260.389 1.00 9.65   ? 3102 LEU A CD2   1 
ATOM   12422 N  N     . TYR A 1 3103 ? 225.796 196.878 265.112 1.00 10.55  ? 3103 TYR A N     1 
ATOM   12423 C  CA    . TYR A 1 3103 ? 226.065 195.939 266.195 1.00 14.38  ? 3103 TYR A CA    1 
ATOM   12424 C  C     . TYR A 1 3103 ? 225.098 196.141 267.354 1.00 12.92  ? 3103 TYR A C     1 
ATOM   12425 O  O     . TYR A 1 3103 ? 224.578 195.170 267.915 1.00 19.36  ? 3103 TYR A O     1 
ATOM   12426 C  CB    . TYR A 1 3103 ? 227.512 196.092 266.662 1.00 17.08  ? 3103 TYR A CB    1 
ATOM   12427 C  CG    . TYR A 1 3103 ? 227.937 195.085 267.703 1.00 22.64  ? 3103 TYR A CG    1 
ATOM   12428 C  CD1   . TYR A 1 3103 ? 228.462 193.856 267.332 1.00 23.62  ? 3103 TYR A CD1   1 
ATOM   12429 C  CD2   . TYR A 1 3103 ? 227.823 195.366 269.056 1.00 23.22  ? 3103 TYR A CD2   1 
ATOM   12430 C  CE1   . TYR A 1 3103 ? 228.851 192.931 268.277 1.00 23.56  ? 3103 TYR A CE1   1 
ATOM   12431 C  CE2   . TYR A 1 3103 ? 228.212 194.450 270.007 1.00 27.27  ? 3103 TYR A CE2   1 
ATOM   12432 C  CZ    . TYR A 1 3103 ? 228.725 193.235 269.614 1.00 30.68  ? 3103 TYR A CZ    1 
ATOM   12433 O  OH    . TYR A 1 3103 ? 229.114 192.319 270.563 1.00 44.43  ? 3103 TYR A OH    1 
ATOM   12434 N  N     . GLN A 1 3104 ? 224.845 197.397 267.727 1.00 12.46  ? 3104 GLN A N     1 
ATOM   12435 C  CA    . GLN A 1 3104 ? 223.921 197.676 268.820 1.00 14.27  ? 3104 GLN A CA    1 
ATOM   12436 C  C     . GLN A 1 3104 ? 222.500 197.262 268.465 1.00 13.48  ? 3104 GLN A C     1 
ATOM   12437 O  O     . GLN A 1 3104 ? 221.790 196.691 269.302 1.00 15.22  ? 3104 GLN A O     1 
ATOM   12438 C  CB    . GLN A 1 3104 ? 223.975 199.158 269.184 1.00 14.40  ? 3104 GLN A CB    1 
ATOM   12439 C  CG    . GLN A 1 3104 ? 225.290 199.589 269.804 1.00 16.13  ? 3104 GLN A CG    1 
ATOM   12440 C  CD    . GLN A 1 3104 ? 225.228 200.981 270.389 1.00 22.30  ? 3104 GLN A CD    1 
ATOM   12441 O  OE1   . GLN A 1 3104 ? 225.943 201.881 269.951 1.00 24.40  ? 3104 GLN A OE1   1 
ATOM   12442 N  NE2   . GLN A 1 3104 ? 224.369 201.168 271.383 1.00 21.59  ? 3104 GLN A NE2   1 
ATOM   12443 N  N     . VAL A 1 3105 ? 222.068 197.540 267.233 1.00 12.62  ? 3105 VAL A N     1 
ATOM   12444 C  CA    . VAL A 1 3105 ? 220.728 197.140 266.807 1.00 10.95  ? 3105 VAL A CA    1 
ATOM   12445 C  C     . VAL A 1 3105 ? 220.593 195.625 266.852 1.00 16.34  ? 3105 VAL A C     1 
ATOM   12446 O  O     . VAL A 1 3105 ? 219.590 195.087 267.337 1.00 21.39  ? 3105 VAL A O     1 
ATOM   12447 C  CB    . VAL A 1 3105 ? 220.425 197.693 265.402 1.00 10.26  ? 3105 VAL A CB    1 
ATOM   12448 C  CG1   . VAL A 1 3105 ? 219.249 196.959 264.783 1.00 14.61  ? 3105 VAL A CG1   1 
ATOM   12449 C  CG2   . VAL A 1 3105 ? 220.144 199.174 265.471 1.00 11.84  ? 3105 VAL A CG2   1 
ATOM   12450 N  N     . GLY A 1 3106 ? 221.605 194.916 266.350 1.00 15.22  ? 3106 GLY A N     1 
ATOM   12451 C  CA    . GLY A 1 3106 ? 221.564 193.466 266.380 1.00 15.63  ? 3106 GLY A CA    1 
ATOM   12452 C  C     . GLY A 1 3106 ? 221.528 192.912 267.789 1.00 19.90  ? 3106 GLY A C     1 
ATOM   12453 O  O     . GLY A 1 3106 ? 220.735 192.019 268.094 1.00 22.81  ? 3106 GLY A O     1 
ATOM   12454 N  N     . LYS A 1 3107 ? 222.377 193.437 268.675 1.00 17.39  ? 3107 LYS A N     1 
ATOM   12455 C  CA    . LYS A 1 3107 ? 222.397 192.943 270.047 1.00 18.08  ? 3107 LYS A CA    1 
ATOM   12456 C  C     . LYS A 1 3107 ? 221.071 193.213 270.748 1.00 20.70  ? 3107 LYS A C     1 
ATOM   12457 O  O     . LYS A 1 3107 ? 220.571 192.368 271.499 1.00 26.40  ? 3107 LYS A O     1 
ATOM   12458 C  CB    . LYS A 1 3107 ? 223.558 193.566 270.822 1.00 18.24  ? 3107 LYS A CB    1 
ATOM   12459 C  CG    . LYS A 1 3107 ? 223.716 192.994 272.224 1.00 24.79  ? 3107 LYS A CG    1 
ATOM   12460 C  CD    . LYS A 1 3107 ? 224.832 193.672 272.993 1.00 29.23  ? 3107 LYS A CD    1 
ATOM   12461 C  CE    . LYS A 1 3107 ? 226.192 193.235 272.482 1.00 32.95  ? 3107 LYS A CE    1 
ATOM   12462 N  NZ    . LYS A 1 3107 ? 227.304 193.797 273.296 1.00 25.13  ? 3107 LYS A NZ    1 
ATOM   12463 N  N     . GLU A 1 3108 ? 220.485 194.390 270.516 1.00 19.99  ? 3108 GLU A N     1 
ATOM   12464 C  CA    . GLU A 1 3108 ? 219.214 194.713 271.155 1.00 25.69  ? 3108 GLU A CA    1 
ATOM   12465 C  C     . GLU A 1 3108 ? 218.083 193.836 270.630 1.00 29.49  ? 3108 GLU A C     1 
ATOM   12466 O  O     . GLU A 1 3108 ? 217.260 193.342 271.410 1.00 28.86  ? 3108 GLU A O     1 
ATOM   12467 C  CB    . GLU A 1 3108 ? 218.883 196.190 270.948 1.00 26.10  ? 3108 GLU A CB    1 
ATOM   12468 C  CG    . GLU A 1 3108 ? 217.569 196.618 271.576 1.00 32.72  ? 3108 GLU A CG    1 
ATOM   12469 C  CD    . GLU A 1 3108 ? 217.634 196.647 273.089 1.00 39.44  ? 3108 GLU A CD    1 
ATOM   12470 O  OE1   . GLU A 1 3108 ? 218.524 197.332 273.632 1.00 34.43  ? 3108 GLU A OE1   1 
ATOM   12471 O  OE2   . GLU A 1 3108 ? 216.795 195.982 273.733 1.00 34.14  ? 3108 GLU A OE2   1 
ATOM   12472 N  N     . PHE A 1 3109 ? 218.025 193.626 269.314 1.00 29.63  ? 3109 PHE A N     1 
ATOM   12473 C  CA    . PHE A 1 3109 ? 216.900 192.905 268.731 1.00 29.74  ? 3109 PHE A CA    1 
ATOM   12474 C  C     . PHE A 1 3109 ? 217.011 191.402 268.971 1.00 32.00  ? 3109 PHE A C     1 
ATOM   12475 O  O     . PHE A 1 3109 ? 216.001 190.747 269.250 1.00 35.53  ? 3109 PHE A O     1 
ATOM   12476 C  CB    . PHE A 1 3109 ? 216.813 193.233 267.235 1.00 24.85  ? 3109 PHE A CB    1 
ATOM   12477 C  CG    . PHE A 1 3109 ? 215.514 192.827 266.575 1.00 30.50  ? 3109 PHE A CG    1 
ATOM   12478 C  CD1   . PHE A 1 3109 ? 215.106 191.504 266.516 1.00 33.15  ? 3109 PHE A CD1   1 
ATOM   12479 C  CD2   . PHE A 1 3109 ? 214.701 193.793 266.007 1.00 22.40  ? 3109 PHE A CD2   1 
ATOM   12480 C  CE1   . PHE A 1 3109 ? 213.918 191.156 265.906 1.00 32.50  ? 3109 PHE A CE1   1 
ATOM   12481 C  CE2   . PHE A 1 3109 ? 213.513 193.448 265.395 1.00 24.05  ? 3109 PHE A CE2   1 
ATOM   12482 C  CZ    . PHE A 1 3109 ? 213.122 192.128 265.346 1.00 28.89  ? 3109 PHE A CZ    1 
ATOM   12483 N  N     . THR A 1 3110 ? 218.219 190.846 268.895 1.00 26.59  ? 3110 THR A N     1 
ATOM   12484 C  CA    . THR A 1 3110 ? 218.442 189.417 269.072 1.00 24.92  ? 3110 THR A CA    1 
ATOM   12485 C  C     . THR A 1 3110 ? 218.607 189.008 270.529 1.00 30.49  ? 3110 THR A C     1 
ATOM   12486 O  O     . THR A 1 3110 ? 218.849 187.828 270.801 1.00 36.63  ? 3110 THR A O     1 
ATOM   12487 C  CB    . THR A 1 3110 ? 219.675 188.968 268.277 1.00 28.70  ? 3110 THR A CB    1 
ATOM   12488 O  OG1   . THR A 1 3110 ? 220.866 189.456 268.907 1.00 25.87  ? 3110 THR A OG1   1 
ATOM   12489 C  CG2   . THR A 1 3110 ? 219.604 189.458 266.838 1.00 25.50  ? 3110 THR A CG2   1 
ATOM   12490 N  N     . SER A 1 3111 ? 218.491 189.948 271.469 1.00 31.94  ? 3111 SER A N     1 
ATOM   12491 C  CA    . SER A 1 3111 ? 218.591 189.596 272.881 1.00 37.44  ? 3111 SER A CA    1 
ATOM   12492 C  C     . SER A 1 3111 ? 217.456 188.688 273.332 1.00 39.70  ? 3111 SER A C     1 
ATOM   12493 O  O     . SER A 1 3111 ? 217.603 187.976 274.330 1.00 34.71  ? 3111 SER A O     1 
ATOM   12494 C  CB    . SER A 1 3111 ? 218.610 190.862 273.736 1.00 33.19  ? 3111 SER A CB    1 
ATOM   12495 O  OG    . SER A 1 3111 ? 217.515 191.703 273.418 1.00 32.71  ? 3111 SER A OG    1 
ATOM   12496 N  N     . LYS A 1 3112 ? 216.326 188.700 272.622 1.00 42.41  ? 3112 LYS A N     1 
ATOM   12497 C  CA    . LYS A 1 3112 ? 215.183 187.884 273.013 1.00 37.10  ? 3112 LYS A CA    1 
ATOM   12498 C  C     . LYS A 1 3112 ? 215.387 186.410 272.684 1.00 41.33  ? 3112 LYS A C     1 
ATOM   12499 O  O     . LYS A 1 3112 ? 214.764 185.551 273.316 1.00 42.31  ? 3112 LYS A O     1 
ATOM   12500 C  CB    . LYS A 1 3112 ? 213.902 188.394 272.344 1.00 42.20  ? 3112 LYS A CB    1 
ATOM   12501 C  CG    . LYS A 1 3112 ? 213.750 189.918 272.221 1.00 47.01  ? 3112 LYS A CG    1 
ATOM   12502 C  CD    . LYS A 1 3112 ? 214.213 190.676 273.465 1.00 46.47  ? 3112 LYS A CD    1 
ATOM   12503 C  CE    . LYS A 1 3112 ? 213.601 192.067 273.528 1.00 49.63  ? 3112 LYS A CE    1 
ATOM   12504 N  NZ    . LYS A 1 3112 ? 213.713 192.785 272.227 1.00 47.86  ? 3112 LYS A NZ    1 
ATOM   12505 N  N     . MET A 1 3113 ? 216.238 186.099 271.710 1.00 39.68  ? 3113 MET A N     1 
ATOM   12506 C  CA    . MET A 1 3113 ? 216.467 184.713 271.337 1.00 35.09  ? 3113 MET A CA    1 
ATOM   12507 C  C     . MET A 1 3113 ? 217.437 184.041 272.306 1.00 47.44  ? 3113 MET A C     1 
ATOM   12508 O  O     . MET A 1 3113 ? 218.093 184.683 273.131 1.00 53.22  ? 3113 MET A O     1 
ATOM   12509 C  CB    . MET A 1 3113 ? 217.007 184.614 269.913 1.00 36.32  ? 3113 MET A CB    1 
ATOM   12510 C  CG    . MET A 1 3113 ? 216.030 185.043 268.840 1.00 44.94  ? 3113 MET A CG    1 
ATOM   12511 S  SD    . MET A 1 3113 ? 216.723 184.828 267.193 1.00 58.52  ? 3113 MET A SD    1 
ATOM   12512 C  CE    . MET A 1 3113 ? 217.887 186.176 267.123 1.00 23.20  ? 3113 MET A CE    1 
ATOM   12513 N  N     . ASP A 1 3114 ? 217.523 182.717 272.190 1.00 47.21  ? 3114 ASP A N     1 
ATOM   12514 C  CA    . ASP A 1 3114 ? 218.417 181.901 273.008 1.00 46.23  ? 3114 ASP A CA    1 
ATOM   12515 C  C     . ASP A 1 3114 ? 219.677 181.638 272.189 1.00 46.21  ? 3114 ASP A C     1 
ATOM   12516 O  O     . ASP A 1 3114 ? 219.829 180.589 271.565 1.00 48.83  ? 3114 ASP A O     1 
ATOM   12517 C  CB    . ASP A 1 3114 ? 217.733 180.606 273.428 1.00 55.23  ? 3114 ASP A CB    1 
ATOM   12518 C  CG    . ASP A 1 3114 ? 218.534 179.823 274.454 1.00 60.50  ? 3114 ASP A CG    1 
ATOM   12519 O  OD1   . ASP A 1 3114 ? 219.641 180.270 274.822 1.00 55.74  ? 3114 ASP A OD1   1 
ATOM   12520 O  OD2   . ASP A 1 3114 ? 218.052 178.757 274.892 1.00 61.91  ? 3114 ASP A OD2   1 
ATOM   12521 N  N     . LEU A 1 3115 ? 220.588 182.608 272.195 1.00 46.76  ? 3115 LEU A N     1 
ATOM   12522 C  CA    . LEU A 1 3115 ? 221.862 182.493 271.502 1.00 43.89  ? 3115 LEU A CA    1 
ATOM   12523 C  C     . LEU A 1 3115 ? 222.997 182.090 272.434 1.00 44.43  ? 3115 LEU A C     1 
ATOM   12524 O  O     . LEU A 1 3115 ? 224.162 182.124 272.027 1.00 41.64  ? 3115 LEU A O     1 
ATOM   12525 C  CB    . LEU A 1 3115 ? 222.206 183.809 270.804 1.00 42.20  ? 3115 LEU A CB    1 
ATOM   12526 C  CG    . LEU A 1 3115 ? 221.291 184.233 269.656 1.00 40.58  ? 3115 LEU A CG    1 
ATOM   12527 C  CD1   . LEU A 1 3115 ? 221.669 185.616 269.155 1.00 31.19  ? 3115 LEU A CD1   1 
ATOM   12528 C  CD2   . LEU A 1 3115 ? 221.352 183.219 268.528 1.00 36.18  ? 3115 LEU A CD2   1 
ATOM   12529 N  N     . GLU A 1 3116 ? 222.686 181.709 273.669 1.00 52.42  ? 3116 GLU A N     1 
ATOM   12530 C  CA    . GLU A 1 3116 ? 223.708 181.359 274.648 1.00 55.19  ? 3116 GLU A CA    1 
ATOM   12531 C  C     . GLU A 1 3116 ? 224.187 179.938 274.381 1.00 54.64  ? 3116 GLU A C     1 
ATOM   12532 O  O     . GLU A 1 3116 ? 223.430 178.976 274.546 1.00 56.85  ? 3116 GLU A O     1 
ATOM   12533 C  CB    . GLU A 1 3116 ? 223.155 181.499 276.063 1.00 54.06  ? 3116 GLU A CB    1 
ATOM   12534 C  CG    . GLU A 1 3116 ? 222.399 182.796 276.303 1.00 54.67  ? 3116 GLU A CG    1 
ATOM   12535 C  CD    . GLU A 1 3116 ? 223.319 183.978 276.542 1.00 60.77  ? 3116 GLU A CD    1 
ATOM   12536 O  OE1   . GLU A 1 3116 ? 224.538 183.762 276.709 1.00 68.89  ? 3116 GLU A OE1   1 
ATOM   12537 O  OE2   . GLU A 1 3116 ? 222.824 185.123 276.563 1.00 60.95  ? 3116 GLU A OE2   1 
ATOM   12538 N  N     . LYS A 1 3117 ? 225.444 179.806 273.966 1.00 53.15  ? 3117 LYS A N     1 
ATOM   12539 C  CA    . LYS A 1 3117 ? 226.059 178.506 273.703 1.00 54.25  ? 3117 LYS A CA    1 
ATOM   12540 C  C     . LYS A 1 3117 ? 227.279 178.350 274.599 1.00 57.62  ? 3117 LYS A C     1 
ATOM   12541 O  O     . LYS A 1 3117 ? 228.374 178.828 274.249 1.00 53.24  ? 3117 LYS A O     1 
ATOM   12542 C  CB    . LYS A 1 3117 ? 226.445 178.373 272.231 1.00 47.90  ? 3117 LYS A CB    1 
ATOM   12543 C  CG    . LYS A 1 3117 ? 226.971 177.003 271.849 1.00 54.37  ? 3117 LYS A CG    1 
ATOM   12544 C  CD    . LYS A 1 3117 ? 227.391 176.958 270.391 1.00 49.27  ? 3117 LYS A CD    1 
ATOM   12545 C  CE    . LYS A 1 3117 ? 226.181 176.940 269.472 1.00 48.36  ? 3117 LYS A CE    1 
ATOM   12546 N  NZ    . LYS A 1 3117 ? 226.572 176.777 268.045 1.00 41.94  ? 3117 LYS A NZ    1 
ATOM   12547 N  N     . PRO A 1 3118 ? 227.143 177.713 275.763 1.00 60.54  ? 3118 PRO A N     1 
ATOM   12548 C  CA    . PRO A 1 3118 ? 228.304 177.553 276.655 1.00 61.01  ? 3118 PRO A CA    1 
ATOM   12549 C  C     . PRO A 1 3118 ? 229.441 176.753 276.044 1.00 64.23  ? 3118 PRO A C     1 
ATOM   12550 O  O     . PRO A 1 3118 ? 230.597 176.943 276.443 1.00 62.82  ? 3118 PRO A O     1 
ATOM   12551 C  CB    . PRO A 1 3118 ? 227.714 176.841 277.880 1.00 56.97  ? 3118 PRO A CB    1 
ATOM   12552 C  CG    . PRO A 1 3118 ? 226.247 177.115 277.817 1.00 50.80  ? 3118 PRO A CG    1 
ATOM   12553 C  CD    . PRO A 1 3118 ? 225.909 177.179 276.360 1.00 54.91  ? 3118 PRO A CD    1 
ATOM   12554 N  N     . ASN A 1 3119 ? 229.156 175.874 275.088 1.00 65.48  ? 3119 ASN A N     1 
ATOM   12555 C  CA    . ASN A 1 3119 ? 230.179 175.059 274.449 1.00 69.13  ? 3119 ASN A CA    1 
ATOM   12556 C  C     . ASN A 1 3119 ? 230.878 175.776 273.303 1.00 67.52  ? 3119 ASN A C     1 
ATOM   12557 O  O     . ASN A 1 3119 ? 231.722 175.170 272.636 1.00 71.84  ? 3119 ASN A O     1 
ATOM   12558 C  CB    . ASN A 1 3119 ? 229.569 173.750 273.938 1.00 70.03  ? 3119 ASN A CB    1 
ATOM   12559 C  CG    . ASN A 1 3119 ? 229.205 172.799 275.060 1.00 77.03  ? 3119 ASN A CG    1 
ATOM   12560 O  OD1   . ASN A 1 3119 ? 229.967 172.625 276.011 1.00 82.56  ? 3119 ASN A OD1   1 
ATOM   12561 N  ND2   . ASN A 1 3119 ? 228.037 172.178 274.954 1.00 78.87  ? 3119 ASN A ND2   1 
ATOM   12562 N  N     . TYR A 1 3120 ? 230.540 177.040 273.052 1.00 62.92  ? 3120 TYR A N     1 
ATOM   12563 C  CA    . TYR A 1 3120 ? 231.180 177.787 271.978 1.00 62.80  ? 3120 TYR A CA    1 
ATOM   12564 C  C     . TYR A 1 3120 ? 232.665 177.963 272.262 1.00 57.23  ? 3120 TYR A C     1 
ATOM   12565 O  O     . TYR A 1 3120 ? 233.062 178.297 273.382 1.00 60.15  ? 3120 TYR A O     1 
ATOM   12566 C  CB    . TYR A 1 3120 ? 230.508 179.150 271.812 1.00 50.38  ? 3120 TYR A CB    1 
ATOM   12567 C  CG    . TYR A 1 3120 ? 231.157 180.025 270.767 1.00 44.28  ? 3120 TYR A CG    1 
ATOM   12568 C  CD1   . TYR A 1 3120 ? 231.100 179.688 269.421 1.00 44.21  ? 3120 TYR A CD1   1 
ATOM   12569 C  CD2   . TYR A 1 3120 ? 231.833 181.184 271.124 1.00 46.36  ? 3120 TYR A CD2   1 
ATOM   12570 C  CE1   . TYR A 1 3120 ? 231.693 180.482 268.462 1.00 39.87  ? 3120 TYR A CE1   1 
ATOM   12571 C  CE2   . TYR A 1 3120 ? 232.430 181.984 270.170 1.00 46.09  ? 3120 TYR A CE2   1 
ATOM   12572 C  CZ    . TYR A 1 3120 ? 232.356 181.627 268.840 1.00 44.86  ? 3120 TYR A CZ    1 
ATOM   12573 O  OH    . TYR A 1 3120 ? 232.946 182.416 267.883 1.00 45.96  ? 3120 TYR A OH    1 
ATOM   12574 N  N     . ILE A 1 3121 ? 233.487 177.735 271.242 1.00 51.31  ? 3121 ILE A N     1 
ATOM   12575 C  CA    . ILE A 1 3121 ? 234.934 177.880 271.337 1.00 54.09  ? 3121 ILE A CA    1 
ATOM   12576 C  C     . ILE A 1 3121 ? 235.356 178.986 270.383 1.00 54.25  ? 3121 ILE A C     1 
ATOM   12577 O  O     . ILE A 1 3121 ? 235.147 178.877 269.169 1.00 59.54  ? 3121 ILE A O     1 
ATOM   12578 C  CB    . ILE A 1 3121 ? 235.665 176.567 271.014 1.00 60.09  ? 3121 ILE A CB    1 
ATOM   12579 C  CG1   . ILE A 1 3121 ? 235.372 175.516 272.085 1.00 59.11  ? 3121 ILE A CG1   1 
ATOM   12580 C  CG2   . ILE A 1 3121 ? 237.161 176.804 270.883 1.00 60.97  ? 3121 ILE A CG2   1 
ATOM   12581 C  CD1   . ILE A 1 3121 ? 235.765 175.944 273.480 1.00 60.35  ? 3121 ILE A CD1   1 
ATOM   12582 N  N     . VAL A 1 3122 ? 235.947 180.040 270.928 1.00 49.89  ? 3122 VAL A N     1 
ATOM   12583 C  CA    . VAL A 1 3122 ? 236.387 181.167 270.098 1.00 49.53  ? 3122 VAL A CA    1 
ATOM   12584 C  C     . VAL A 1 3122 ? 237.536 180.711 269.206 1.00 56.98  ? 3122 VAL A C     1 
ATOM   12585 O  O     . VAL A 1 3122 ? 238.499 180.101 269.704 1.00 64.21  ? 3122 VAL A O     1 
ATOM   12586 C  CB    . VAL A 1 3122 ? 236.807 182.344 270.979 1.00 54.62  ? 3122 VAL A CB    1 
ATOM   12587 C  CG1   . VAL A 1 3122 ? 237.259 183.517 270.123 1.00 50.69  ? 3122 VAL A CG1   1 
ATOM   12588 C  CG2   . VAL A 1 3122 ? 235.660 182.757 271.889 1.00 50.66  ? 3122 VAL A CG2   1 
ATOM   12589 N  N     . PRO A 1 3123 ? 237.487 180.972 267.902 1.00 56.54  ? 3123 PRO A N     1 
ATOM   12590 C  CA    . PRO A 1 3123 ? 238.593 180.574 267.030 1.00 63.31  ? 3123 PRO A CA    1 
ATOM   12591 C  C     . PRO A 1 3123 ? 239.861 181.355 267.342 1.00 64.30  ? 3123 PRO A C     1 
ATOM   12592 O  O     . PRO A 1 3123 ? 239.846 182.375 268.035 1.00 62.00  ? 3123 PRO A O     1 
ATOM   12593 C  CB    . PRO A 1 3123 ? 238.074 180.900 265.624 1.00 59.66  ? 3123 PRO A CB    1 
ATOM   12594 C  CG    . PRO A 1 3123 ? 237.039 181.951 265.843 1.00 53.89  ? 3123 PRO A CG    1 
ATOM   12595 C  CD    . PRO A 1 3123 ? 236.391 181.603 267.150 1.00 52.20  ? 3123 PRO A CD    1 
ATOM   12596 N  N     . ASP A 1 3124 ? 240.976 180.844 266.817 1.00 71.67  ? 3124 ASP A N     1 
ATOM   12597 C  CA    . ASP A 1 3124 ? 242.263 181.497 267.036 1.00 71.26  ? 3124 ASP A CA    1 
ATOM   12598 C  C     . ASP A 1 3124 ? 242.275 182.907 266.459 1.00 72.71  ? 3124 ASP A C     1 
ATOM   12599 O  O     . ASP A 1 3124 ? 242.831 183.830 267.066 1.00 71.60  ? 3124 ASP A O     1 
ATOM   12600 C  CB    . ASP A 1 3124 ? 243.387 180.643 266.446 1.00 75.77  ? 3124 ASP A CB    1 
ATOM   12601 C  CG    . ASP A 1 3124 ? 243.255 180.443 264.945 1.00 79.07  ? 3124 ASP A CG    1 
ATOM   12602 O  OD1   . ASP A 1 3124 ? 242.265 180.920 264.354 1.00 72.34  ? 3124 ASP A OD1   1 
ATOM   12603 O  OD2   . ASP A 1 3124 ? 244.150 179.800 264.356 1.00 88.93  ? 3124 ASP A OD2   1 
ATOM   12604 N  N     . TYR A 1 3125 ? 241.668 183.095 265.290 1.00 74.04  ? 3125 TYR A N     1 
ATOM   12605 C  CA    . TYR A 1 3125 ? 241.481 184.415 264.705 1.00 72.09  ? 3125 TYR A CA    1 
ATOM   12606 C  C     . TYR A 1 3125 ? 239.989 184.646 264.499 1.00 73.29  ? 3125 TYR A C     1 
ATOM   12607 O  O     . TYR A 1 3125 ? 239.315 183.831 263.861 1.00 67.86  ? 3125 TYR A O     1 
ATOM   12608 C  CB    . TYR A 1 3125 ? 242.228 184.550 263.380 1.00 65.77  ? 3125 TYR A CB    1 
ATOM   12609 C  CG    . TYR A 1 3125 ? 241.670 185.639 262.493 1.00 72.69  ? 3125 TYR A CG    1 
ATOM   12610 C  CD1   . TYR A 1 3125 ? 241.846 186.979 262.814 1.00 69.56  ? 3125 TYR A CD1   1 
ATOM   12611 C  CD2   . TYR A 1 3125 ? 240.955 185.331 261.344 1.00 74.54  ? 3125 TYR A CD2   1 
ATOM   12612 C  CE1   . TYR A 1 3125 ? 241.334 187.980 262.013 1.00 73.32  ? 3125 TYR A CE1   1 
ATOM   12613 C  CE2   . TYR A 1 3125 ? 240.438 186.326 260.536 1.00 73.72  ? 3125 TYR A CE2   1 
ATOM   12614 C  CZ    . TYR A 1 3125 ? 240.630 187.648 260.874 1.00 77.97  ? 3125 TYR A CZ    1 
ATOM   12615 O  OH    . TYR A 1 3125 ? 240.117 188.640 260.070 1.00 73.94  ? 3125 TYR A OH    1 
ATOM   12616 N  N     . MET A 1 3126 ? 239.481 185.753 265.039 1.00 74.72  ? 3126 MET A N     1 
ATOM   12617 C  CA    . MET A 1 3126 ? 238.084 186.118 264.872 1.00 66.83  ? 3126 MET A CA    1 
ATOM   12618 C  C     . MET A 1 3126 ? 237.952 187.140 263.758 1.00 62.07  ? 3126 MET A C     1 
ATOM   12619 O  O     . MET A 1 3126 ? 238.661 188.158 263.780 1.00 60.50  ? 3126 MET A O     1 
ATOM   12620 C  CB    . MET A 1 3126 ? 237.512 186.679 266.169 1.00 60.96  ? 3126 MET A CB    1 
ATOM   12621 C  CG    . MET A 1 3126 ? 236.025 186.988 266.100 1.00 58.81  ? 3126 MET A CG    1 
ATOM   12622 S  SD    . MET A 1 3126 ? 235.004 185.518 265.885 1.00 66.56  ? 3126 MET A SD    1 
ATOM   12623 C  CE    . MET A 1 3126 ? 234.932 184.909 267.564 1.00 48.75  ? 3126 MET A CE    1 
ATOM   12624 N  N     . PRO A 1 3127 ? 237.079 186.922 262.772 1.00 58.70  ? 3127 PRO A N     1 
ATOM   12625 C  CA    . PRO A 1 3127 ? 236.872 187.941 261.735 1.00 59.47  ? 3127 PRO A CA    1 
ATOM   12626 C  C     . PRO A 1 3127 ? 236.147 189.148 262.301 1.00 57.31  ? 3127 PRO A C     1 
ATOM   12627 O  O     . PRO A 1 3127 ? 234.951 189.341 262.056 1.00 55.20  ? 3127 PRO A O     1 
ATOM   12628 C  CB    . PRO A 1 3127 ? 236.026 187.218 260.678 1.00 53.41  ? 3127 PRO A CB    1 
ATOM   12629 C  CG    . PRO A 1 3127 ? 236.047 185.768 261.053 1.00 52.95  ? 3127 PRO A CG    1 
ATOM   12630 C  CD    . PRO A 1 3127 ? 236.296 185.703 262.521 1.00 49.21  ? 3127 PRO A CD    1 
ATOM   12631 N  N     . VAL A 1 3128 ? 236.869 189.966 263.062 1.00 56.85  ? 3128 VAL A N     1 
ATOM   12632 C  CA    . VAL A 1 3128 ? 236.253 191.058 263.807 1.00 48.01  ? 3128 VAL A CA    1 
ATOM   12633 C  C     . VAL A 1 3128 ? 235.794 192.136 262.835 1.00 47.31  ? 3128 VAL A C     1 
ATOM   12634 O  O     . VAL A 1 3128 ? 236.587 192.663 262.046 1.00 45.47  ? 3128 VAL A O     1 
ATOM   12635 C  CB    . VAL A 1 3128 ? 237.228 191.623 264.847 1.00 55.87  ? 3128 VAL A CB    1 
ATOM   12636 C  CG1   . VAL A 1 3128 ? 236.668 192.890 265.467 1.00 48.63  ? 3128 VAL A CG1   1 
ATOM   12637 C  CG2   . VAL A 1 3128 ? 237.520 190.582 265.919 1.00 51.00  ? 3128 VAL A CG2   1 
ATOM   12638 N  N     . VAL A 1 3129 ? 234.507 192.465 262.888 1.00 46.31  ? 3129 VAL A N     1 
ATOM   12639 C  CA    . VAL A 1 3129 ? 233.941 193.539 262.085 1.00 39.99  ? 3129 VAL A CA    1 
ATOM   12640 C  C     . VAL A 1 3129 ? 233.712 194.794 262.917 1.00 33.29  ? 3129 VAL A C     1 
ATOM   12641 O  O     . VAL A 1 3129 ? 234.031 195.899 262.479 1.00 36.79  ? 3129 VAL A O     1 
ATOM   12642 C  CB    . VAL A 1 3129 ? 232.634 193.068 261.413 1.00 29.03  ? 3129 VAL A CB    1 
ATOM   12643 C  CG1   . VAL A 1 3129 ? 232.095 194.140 260.485 1.00 30.99  ? 3129 VAL A CG1   1 
ATOM   12644 C  CG2   . VAL A 1 3129 ? 232.872 191.775 260.657 1.00 29.57  ? 3129 VAL A CG2   1 
ATOM   12645 N  N     . TYR A 1 3130 ? 233.164 194.637 264.117 1.00 30.29  ? 3130 TYR A N     1 
ATOM   12646 C  CA    . TYR A 1 3130 ? 232.980 195.743 265.047 1.00 36.28  ? 3130 TYR A CA    1 
ATOM   12647 C  C     . TYR A 1 3130 ? 234.267 195.896 265.850 1.00 49.00  ? 3130 TYR A C     1 
ATOM   12648 O  O     . TYR A 1 3130 ? 234.632 195.005 266.623 1.00 54.06  ? 3130 TYR A O     1 
ATOM   12649 C  CB    . TYR A 1 3130 ? 231.783 195.487 265.958 1.00 31.89  ? 3130 TYR A CB    1 
ATOM   12650 C  CG    . TYR A 1 3130 ? 231.540 196.566 266.987 1.00 31.18  ? 3130 TYR A CG    1 
ATOM   12651 C  CD1   . TYR A 1 3130 ? 231.739 197.904 266.680 1.00 28.12  ? 3130 TYR A CD1   1 
ATOM   12652 C  CD2   . TYR A 1 3130 ? 231.106 196.244 268.264 1.00 39.80  ? 3130 TYR A CD2   1 
ATOM   12653 C  CE1   . TYR A 1 3130 ? 231.515 198.890 267.617 1.00 32.50  ? 3130 TYR A CE1   1 
ATOM   12654 C  CE2   . TYR A 1 3130 ? 230.878 197.226 269.209 1.00 37.46  ? 3130 TYR A CE2   1 
ATOM   12655 C  CZ    . TYR A 1 3130 ? 231.083 198.547 268.878 1.00 34.35  ? 3130 TYR A CZ    1 
ATOM   12656 O  OH    . TYR A 1 3130 ? 230.858 199.528 269.815 1.00 44.23  ? 3130 TYR A OH    1 
ATOM   12657 N  N     . ASP A 1 3131 ? 234.950 197.032 265.671 1.00 47.51  ? 3131 ASP A N     1 
ATOM   12658 C  CA    . ASP A 1 3131 ? 236.271 197.207 266.264 1.00 45.20  ? 3131 ASP A CA    1 
ATOM   12659 C  C     . ASP A 1 3131 ? 236.232 197.134 267.784 1.00 42.09  ? 3131 ASP A C     1 
ATOM   12660 O  O     . ASP A 1 3131 ? 237.212 196.714 268.409 1.00 45.25  ? 3131 ASP A O     1 
ATOM   12661 C  CB    . ASP A 1 3131 ? 236.872 198.537 265.812 1.00 52.19  ? 3131 ASP A CB    1 
ATOM   12662 C  CG    . ASP A 1 3131 ? 237.224 198.546 264.338 1.00 60.48  ? 3131 ASP A CG    1 
ATOM   12663 O  OD1   . ASP A 1 3131 ? 237.536 197.466 263.794 1.00 60.60  ? 3131 ASP A OD1   1 
ATOM   12664 O  OD2   . ASP A 1 3131 ? 237.191 199.633 263.724 1.00 68.15  ? 3131 ASP A OD2   1 
ATOM   12665 N  N     . LYS A 1 3132 ? 235.118 197.530 268.396 1.00 40.52  ? 3132 LYS A N     1 
ATOM   12666 C  CA    . LYS A 1 3132 ? 234.971 197.491 269.843 1.00 44.83  ? 3132 LYS A CA    1 
ATOM   12667 C  C     . LYS A 1 3132 ? 234.326 196.198 270.334 1.00 43.08  ? 3132 LYS A C     1 
ATOM   12668 O  O     . LYS A 1 3132 ? 233.741 196.183 271.424 1.00 45.22  ? 3132 LYS A O     1 
ATOM   12669 C  CB    . LYS A 1 3132 ? 234.166 198.700 270.324 1.00 41.14  ? 3132 LYS A CB    1 
ATOM   12670 C  CG    . LYS A 1 3132 ? 234.803 200.036 269.986 1.00 49.78  ? 3132 LYS A CG    1 
ATOM   12671 C  CD    . LYS A 1 3132 ? 236.117 200.221 270.726 1.00 63.81  ? 3132 LYS A CD    1 
ATOM   12672 C  CE    . LYS A 1 3132 ? 236.673 201.621 270.523 1.00 68.88  ? 3132 LYS A CE    1 
ATOM   12673 N  NZ    . LYS A 1 3132 ? 237.128 201.839 269.122 1.00 67.35  ? 3132 LYS A NZ    1 
ATOM   12674 N  N     . LEU A 1 3133 ? 234.410 195.126 269.555 1.00 39.04  ? 3133 LEU A N     1 
ATOM   12675 C  CA    . LEU A 1 3133 ? 233.905 193.840 270.008 1.00 44.54  ? 3133 LEU A CA    1 
ATOM   12676 C  C     . LEU A 1 3133 ? 234.745 193.337 271.181 1.00 49.88  ? 3133 LEU A C     1 
ATOM   12677 O  O     . LEU A 1 3133 ? 235.972 193.488 271.175 1.00 54.30  ? 3133 LEU A O     1 
ATOM   12678 C  CB    . LEU A 1 3133 ? 233.932 192.825 268.865 1.00 41.84  ? 3133 LEU A CB    1 
ATOM   12679 C  CG    . LEU A 1 3133 ? 233.467 191.395 269.146 1.00 43.27  ? 3133 LEU A CG    1 
ATOM   12680 C  CD1   . LEU A 1 3133 ? 231.952 191.302 269.122 1.00 36.12  ? 3133 LEU A CD1   1 
ATOM   12681 C  CD2   . LEU A 1 3133 ? 234.078 190.434 268.140 1.00 48.11  ? 3133 LEU A CD2   1 
ATOM   12682 N  N     . PRO A 1 3134 ? 234.118 192.758 272.205 1.00 44.64  ? 3134 PRO A N     1 
ATOM   12683 C  CA    . PRO A 1 3134 ? 234.886 192.249 273.347 1.00 52.47  ? 3134 PRO A CA    1 
ATOM   12684 C  C     . PRO A 1 3134 ? 235.905 191.201 272.918 1.00 60.61  ? 3134 PRO A C     1 
ATOM   12685 O  O     . PRO A 1 3134 ? 235.641 190.368 272.049 1.00 54.58  ? 3134 PRO A O     1 
ATOM   12686 C  CB    . PRO A 1 3134 ? 233.808 191.651 274.256 1.00 50.67  ? 3134 PRO A CB    1 
ATOM   12687 C  CG    . PRO A 1 3134 ? 232.579 192.428 273.924 1.00 48.98  ? 3134 PRO A CG    1 
ATOM   12688 C  CD    . PRO A 1 3134 ? 232.666 192.711 272.451 1.00 43.24  ? 3134 PRO A CD    1 
ATOM   12689 N  N     . GLN A 1 3135 ? 237.083 191.260 273.543 1.00 68.03  ? 3135 GLN A N     1 
ATOM   12690 C  CA    . GLN A 1 3135 ? 238.181 190.377 273.152 1.00 65.73  ? 3135 GLN A CA    1 
ATOM   12691 C  C     . GLN A 1 3135 ? 237.863 188.899 273.350 1.00 67.53  ? 3135 GLN A C     1 
ATOM   12692 O  O     . GLN A 1 3135 ? 238.206 188.100 272.462 1.00 74.87  ? 3135 GLN A O     1 
ATOM   12693 C  CB    . GLN A 1 3135 ? 239.459 190.784 273.894 1.00 77.10  ? 3135 GLN A CB    1 
ATOM   12694 C  CG    . GLN A 1 3135 ? 239.691 192.287 273.972 1.00 84.00  ? 3135 GLN A CG    1 
ATOM   12695 C  CD    . GLN A 1 3135 ? 239.671 192.958 272.612 1.00 88.78  ? 3135 GLN A CD    1 
ATOM   12696 O  OE1   . GLN A 1 3135 ? 240.244 192.452 271.648 1.00 89.58  ? 3135 GLN A OE1   1 
ATOM   12697 N  NE2   . GLN A 1 3135 ? 239.012 194.108 272.532 1.00 82.01  ? 3135 GLN A NE2   1 
ATOM   12698 N  N     . PRO A 1 3136 ? 237.306 188.453 274.477 1.00 68.72  ? 3136 PRO A N     1 
ATOM   12699 C  CA    . PRO A 1 3136 ? 236.773 187.087 274.549 1.00 63.83  ? 3136 PRO A CA    1 
ATOM   12700 C  C     . PRO A 1 3136 ? 235.294 187.055 274.204 1.00 64.78  ? 3136 PRO A C     1 
ATOM   12701 O  O     . PRO A 1 3136 ? 234.445 187.013 275.107 1.00 67.93  ? 3136 PRO A O     1 
ATOM   12702 C  CB    . PRO A 1 3136 ? 237.015 186.694 276.012 1.00 66.43  ? 3136 PRO A CB    1 
ATOM   12703 C  CG    . PRO A 1 3136 ? 236.964 187.995 276.762 1.00 68.70  ? 3136 PRO A CG    1 
ATOM   12704 C  CD    . PRO A 1 3136 ? 237.209 189.128 275.786 1.00 69.58  ? 3136 PRO A CD    1 
ATOM   12705 N  N     . PRO A 1 3137 ? 234.936 187.076 272.919 1.00 61.87  ? 3137 PRO A N     1 
ATOM   12706 C  CA    . PRO A 1 3137 ? 233.523 187.234 272.564 1.00 50.22  ? 3137 PRO A CA    1 
ATOM   12707 C  C     . PRO A 1 3137 ? 232.722 185.980 272.867 1.00 43.73  ? 3137 PRO A C     1 
ATOM   12708 O  O     . PRO A 1 3137 ? 233.219 184.858 272.754 1.00 51.46  ? 3137 PRO A O     1 
ATOM   12709 C  CB    . PRO A 1 3137 ? 233.571 187.518 271.062 1.00 46.72  ? 3137 PRO A CB    1 
ATOM   12710 C  CG    . PRO A 1 3137 ? 234.764 186.769 270.598 1.00 50.29  ? 3137 PRO A CG    1 
ATOM   12711 C  CD    . PRO A 1 3137 ? 235.733 186.652 271.756 1.00 60.28  ? 3137 PRO A CD    1 
ATOM   12712 N  N     . SER A 1 3138 ? 231.466 186.183 273.253 1.00 39.85  ? 3138 SER A N     1 
ATOM   12713 C  CA    . SER A 1 3138 ? 230.555 185.074 273.478 1.00 39.13  ? 3138 SER A CA    1 
ATOM   12714 C  C     . SER A 1 3138 ? 229.936 184.636 272.153 1.00 42.02  ? 3138 SER A C     1 
ATOM   12715 O  O     . SER A 1 3138 ? 230.239 185.172 271.084 1.00 44.59  ? 3138 SER A O     1 
ATOM   12716 C  CB    . SER A 1 3138 ? 229.481 185.468 274.489 1.00 37.00  ? 3138 SER A CB    1 
ATOM   12717 O  OG    . SER A 1 3138 ? 228.784 186.625 274.063 1.00 37.52  ? 3138 SER A OG    1 
ATOM   12718 N  N     . HIS A 1 3139 ? 229.057 183.634 272.224 1.00 39.63  ? 3139 HIS A N     1 
ATOM   12719 C  CA    . HIS A 1 3139 ? 228.365 183.179 271.022 1.00 36.85  ? 3139 HIS A CA    1 
ATOM   12720 C  C     . HIS A 1 3139 ? 227.450 184.262 270.467 1.00 35.33  ? 3139 HIS A C     1 
ATOM   12721 O  O     . HIS A 1 3139 ? 227.397 184.475 269.251 1.00 31.51  ? 3139 HIS A O     1 
ATOM   12722 C  CB    . HIS A 1 3139 ? 227.572 181.907 271.325 1.00 37.23  ? 3139 HIS A CB    1 
ATOM   12723 C  CG    . HIS A 1 3139 ? 227.040 181.225 270.105 1.00 38.40  ? 3139 HIS A CG    1 
ATOM   12724 N  ND1   . HIS A 1 3139 ? 225.703 180.934 269.939 1.00 37.38  ? 3139 HIS A ND1   1 
ATOM   12725 C  CD2   . HIS A 1 3139 ? 227.663 180.777 268.990 1.00 36.46  ? 3139 HIS A CD2   1 
ATOM   12726 C  CE1   . HIS A 1 3139 ? 225.525 180.336 268.775 1.00 39.66  ? 3139 HIS A CE1   1 
ATOM   12727 N  NE2   . HIS A 1 3139 ? 226.699 180.229 268.179 1.00 38.01  ? 3139 HIS A NE2   1 
ATOM   12728 N  N     . ARG A 1 3140 ? 226.722 184.957 271.344 1.00 33.19  ? 3140 ARG A N     1 
ATOM   12729 C  CA    . ARG A 1 3140 ? 225.796 185.994 270.898 1.00 27.62  ? 3140 ARG A CA    1 
ATOM   12730 C  C     . ARG A 1 3140 ? 226.531 187.132 270.202 1.00 28.95  ? 3140 ARG A C     1 
ATOM   12731 O  O     . ARG A 1 3140 ? 226.082 187.630 269.161 1.00 31.20  ? 3140 ARG A O     1 
ATOM   12732 C  CB    . ARG A 1 3140 ? 224.998 186.516 272.092 1.00 27.01  ? 3140 ARG A CB    1 
ATOM   12733 C  CG    . ARG A 1 3140 ? 223.775 187.334 271.730 1.00 33.31  ? 3140 ARG A CG    1 
ATOM   12734 C  CD    . ARG A 1 3140 ? 223.087 187.857 272.980 1.00 31.86  ? 3140 ARG A CD    1 
ATOM   12735 N  NE    . ARG A 1 3140 ? 222.437 186.790 273.729 1.00 29.03  ? 3140 ARG A NE    1 
ATOM   12736 C  CZ    . ARG A 1 3140 ? 221.232 186.308 273.454 1.00 38.21  ? 3140 ARG A CZ    1 
ATOM   12737 N  NH1   . ARG A 1 3140 ? 220.510 186.781 272.452 1.00 41.16  ? 3140 ARG A NH1   1 
ATOM   12738 N  NH2   . ARG A 1 3140 ? 220.739 185.326 274.203 1.00 47.27  ? 3140 ARG A NH2   1 
ATOM   12739 N  N     . GLU A 1 3141 ? 227.665 187.557 270.762 1.00 29.55  ? 3141 GLU A N     1 
ATOM   12740 C  CA    . GLU A 1 3141 ? 228.442 188.623 270.141 1.00 28.15  ? 3141 GLU A CA    1 
ATOM   12741 C  C     . GLU A 1 3141 ? 228.994 188.186 268.792 1.00 26.07  ? 3141 GLU A C     1 
ATOM   12742 O  O     . GLU A 1 3141 ? 229.037 188.982 267.847 1.00 27.08  ? 3141 GLU A O     1 
ATOM   12743 C  CB    . GLU A 1 3141 ? 229.567 189.062 271.074 1.00 35.18  ? 3141 GLU A CB    1 
ATOM   12744 C  CG    . GLU A 1 3141 ? 229.077 189.588 272.412 1.00 43.45  ? 3141 GLU A CG    1 
ATOM   12745 C  CD    . GLU A 1 3141 ? 230.204 189.826 273.393 1.00 49.16  ? 3141 GLU A CD    1 
ATOM   12746 O  OE1   . GLU A 1 3141 ? 231.369 189.569 273.031 1.00 49.80  ? 3141 GLU A OE1   1 
ATOM   12747 O  OE2   . GLU A 1 3141 ? 229.923 190.268 274.526 1.00 48.86  ? 3141 GLU A OE2   1 
ATOM   12748 N  N     . ALA A 1 3142 ? 229.416 186.925 268.679 1.00 28.86  ? 3142 ALA A N     1 
ATOM   12749 C  CA    . ALA A 1 3142 ? 229.861 186.407 267.390 1.00 27.00  ? 3142 ALA A CA    1 
ATOM   12750 C  C     . ALA A 1 3142 ? 228.725 186.408 266.374 1.00 21.40  ? 3142 ALA A C     1 
ATOM   12751 O  O     . ALA A 1 3142 ? 228.932 186.742 265.202 1.00 19.35  ? 3142 ALA A O     1 
ATOM   12752 C  CB    . ALA A 1 3142 ? 230.431 184.999 267.559 1.00 30.26  ? 3142 ALA A CB    1 
ATOM   12753 N  N     . ILE A 1 3143 ? 227.518 186.039 266.807 1.00 21.56  ? 3143 ILE A N     1 
ATOM   12754 C  CA    . ILE A 1 3143 ? 226.361 186.055 265.913 1.00 18.04  ? 3143 ILE A CA    1 
ATOM   12755 C  C     . ILE A 1 3143 ? 226.084 187.470 265.423 1.00 19.06  ? 3143 ILE A C     1 
ATOM   12756 O  O     . ILE A 1 3143 ? 225.829 187.695 264.231 1.00 17.09  ? 3143 ILE A O     1 
ATOM   12757 C  CB    . ILE A 1 3143 ? 225.131 185.455 266.622 1.00 21.79  ? 3143 ILE A CB    1 
ATOM   12758 C  CG1   . ILE A 1 3143 ? 225.337 183.965 266.904 1.00 24.50  ? 3143 ILE A CG1   1 
ATOM   12759 C  CG2   . ILE A 1 3143 ? 223.880 185.667 265.790 1.00 22.48  ? 3143 ILE A CG2   1 
ATOM   12760 C  CD1   . ILE A 1 3143 ? 225.684 183.151 265.685 1.00 21.78  ? 3143 ILE A CD1   1 
ATOM   12761 N  N     . VAL A 1 3144 ? 226.131 188.447 266.329 1.00 19.60  ? 3144 VAL A N     1 
ATOM   12762 C  CA    . VAL A 1 3144 ? 225.851 189.828 265.939 1.00 16.46  ? 3144 VAL A CA    1 
ATOM   12763 C  C     . VAL A 1 3144 ? 226.939 190.353 265.007 1.00 18.38  ? 3144 VAL A C     1 
ATOM   12764 O  O     . VAL A 1 3144 ? 226.655 191.078 264.043 1.00 22.73  ? 3144 VAL A O     1 
ATOM   12765 C  CB    . VAL A 1 3144 ? 225.685 190.713 267.186 1.00 18.05  ? 3144 VAL A CB    1 
ATOM   12766 C  CG1   . VAL A 1 3144 ? 225.461 192.160 266.784 1.00 20.35  ? 3144 VAL A CG1   1 
ATOM   12767 C  CG2   . VAL A 1 3144 ? 224.531 190.215 268.037 1.00 15.44  ? 3144 VAL A CG2   1 
ATOM   12768 N  N     . ASN A 1 3145 ? 228.197 189.998 265.275 1.00 18.21  ? 3145 ASN A N     1 
ATOM   12769 C  CA    . ASN A 1 3145 ? 229.288 190.390 264.388 1.00 16.52  ? 3145 ASN A CA    1 
ATOM   12770 C  C     . ASN A 1 3145 ? 229.105 189.788 263.001 1.00 19.17  ? 3145 ASN A C     1 
ATOM   12771 O  O     . ASN A 1 3145 ? 229.362 190.450 261.986 1.00 20.70  ? 3145 ASN A O     1 
ATOM   12772 C  CB    . ASN A 1 3145 ? 230.624 189.960 264.993 1.00 25.51  ? 3145 ASN A CB    1 
ATOM   12773 C  CG    . ASN A 1 3145 ? 231.814 190.585 264.292 1.00 34.13  ? 3145 ASN A CG    1 
ATOM   12774 O  OD1   . ASN A 1 3145 ? 232.011 191.797 264.342 1.00 39.34  ? 3145 ASN A OD1   1 
ATOM   12775 N  ND2   . ASN A 1 3145 ? 232.614 189.757 263.635 1.00 30.05  ? 3145 ASN A ND2   1 
ATOM   12776 N  N     . SER A 1 3146 ? 228.662 188.531 262.938 1.00 22.27  ? 3146 SER A N     1 
ATOM   12777 C  CA    . SER A 1 3146 ? 228.389 187.903 261.651 1.00 17.55  ? 3146 SER A CA    1 
ATOM   12778 C  C     . SER A 1 3146 ? 227.246 188.602 260.926 1.00 19.48  ? 3146 SER A C     1 
ATOM   12779 O  O     . SER A 1 3146 ? 227.282 188.752 259.702 1.00 21.29  ? 3146 SER A O     1 
ATOM   12780 C  CB    . SER A 1 3146 ? 228.074 186.423 261.852 1.00 19.49  ? 3146 SER A CB    1 
ATOM   12781 O  OG    . SER A 1 3146 ? 229.200 185.742 262.376 1.00 25.92  ? 3146 SER A OG    1 
ATOM   12782 N  N     . CYS A 1 3147 ? 226.218 189.027 261.664 1.00 14.93  ? 3147 CYS A N     1 
ATOM   12783 C  CA    . CYS A 1 3147 ? 225.129 189.782 261.047 1.00 9.75   ? 3147 CYS A CA    1 
ATOM   12784 C  C     . CYS A 1 3147 ? 225.631 191.098 260.461 1.00 12.65  ? 3147 CYS A C     1 
ATOM   12785 O  O     . CYS A 1 3147 ? 225.243 191.487 259.350 1.00 15.94  ? 3147 CYS A O     1 
ATOM   12786 C  CB    . CYS A 1 3147 ? 224.026 190.043 262.073 1.00 13.57  ? 3147 CYS A CB    1 
ATOM   12787 S  SG    . CYS A 1 3147 ? 223.154 188.569 262.649 1.00 18.28  ? 3147 CYS A SG    1 
ATOM   12788 N  N     . VAL A 1 3148 ? 226.496 191.799 261.197 1.00 13.34  ? 3148 VAL A N     1 
ATOM   12789 C  CA    . VAL A 1 3148 ? 227.058 193.050 260.695 1.00 12.49  ? 3148 VAL A CA    1 
ATOM   12790 C  C     . VAL A 1 3148 ? 227.891 192.797 259.444 1.00 11.54  ? 3148 VAL A C     1 
ATOM   12791 O  O     . VAL A 1 3148 ? 227.821 193.555 258.464 1.00 15.44  ? 3148 VAL A O     1 
ATOM   12792 C  CB    . VAL A 1 3148 ? 227.879 193.749 261.795 1.00 12.21  ? 3148 VAL A CB    1 
ATOM   12793 C  CG1   . VAL A 1 3148 ? 228.556 194.990 261.244 1.00 15.73  ? 3148 VAL A CG1   1 
ATOM   12794 C  CG2   . VAL A 1 3148 ? 226.987 194.113 262.967 1.00 11.78  ? 3148 VAL A CG2   1 
ATOM   12795 N  N     . PHE A 1 3149 ? 228.692 191.728 259.454 1.00 11.89  ? 3149 PHE A N     1 
ATOM   12796 C  CA    . PHE A 1 3149 ? 229.471 191.387 258.269 1.00 15.09  ? 3149 PHE A CA    1 
ATOM   12797 C  C     . PHE A 1 3149 ? 228.562 191.064 257.092 1.00 12.19  ? 3149 PHE A C     1 
ATOM   12798 O  O     . PHE A 1 3149 ? 228.868 191.416 255.949 1.00 12.52  ? 3149 PHE A O     1 
ATOM   12799 C  CB    . PHE A 1 3149 ? 230.397 190.205 258.546 1.00 13.73  ? 3149 PHE A CB    1 
ATOM   12800 C  CG    . PHE A 1 3149 ? 231.078 189.682 257.312 1.00 12.59  ? 3149 PHE A CG    1 
ATOM   12801 C  CD1   . PHE A 1 3149 ? 232.184 190.330 256.794 1.00 14.59  ? 3149 PHE A CD1   1 
ATOM   12802 C  CD2   . PHE A 1 3149 ? 230.589 188.570 256.648 1.00 12.90  ? 3149 PHE A CD2   1 
ATOM   12803 C  CE1   . PHE A 1 3149 ? 232.805 189.866 255.652 1.00 17.21  ? 3149 PHE A CE1   1 
ATOM   12804 C  CE2   . PHE A 1 3149 ? 231.206 188.104 255.505 1.00 15.28  ? 3149 PHE A CE2   1 
ATOM   12805 C  CZ    . PHE A 1 3149 ? 232.315 188.752 255.008 1.00 17.32  ? 3149 PHE A CZ    1 
ATOM   12806 N  N     . VAL A 1 3150 ? 227.451 190.374 257.352 1.00 10.67  ? 3150 VAL A N     1 
ATOM   12807 C  CA    . VAL A 1 3150 ? 226.501 190.058 256.290 1.00 10.65  ? 3150 VAL A CA    1 
ATOM   12808 C  C     . VAL A 1 3150 ? 225.951 191.338 255.681 1.00 13.95  ? 3150 VAL A C     1 
ATOM   12809 O  O     . VAL A 1 3150 ? 225.828 191.459 254.456 1.00 16.56  ? 3150 VAL A O     1 
ATOM   12810 C  CB    . VAL A 1 3150 ? 225.376 189.155 256.832 1.00 10.95  ? 3150 VAL A CB    1 
ATOM   12811 C  CG1   . VAL A 1 3150 ? 224.159 189.210 255.922 1.00 9.47   ? 3150 VAL A CG1   1 
ATOM   12812 C  CG2   . VAL A 1 3150 ? 225.867 187.726 256.982 1.00 14.35  ? 3150 VAL A CG2   1 
ATOM   12813 N  N     . HIS A 1 3151 ? 225.617 192.316 256.525 1.00 12.57  ? 3151 HIS A N     1 
ATOM   12814 C  CA    . HIS A 1 3151 ? 225.123 193.587 256.000 1.00 10.15  ? 3151 HIS A CA    1 
ATOM   12815 C  C     . HIS A 1 3151 ? 226.176 194.288 255.147 1.00 12.02  ? 3151 HIS A C     1 
ATOM   12816 O  O     . HIS A 1 3151 ? 225.866 194.795 254.062 1.00 14.78  ? 3151 HIS A O     1 
ATOM   12817 C  CB    . HIS A 1 3151 ? 224.672 194.502 257.136 1.00 8.13   ? 3151 HIS A CB    1 
ATOM   12818 C  CG    . HIS A 1 3151 ? 224.022 195.764 256.660 1.00 8.19   ? 3151 HIS A CG    1 
ATOM   12819 N  ND1   . HIS A 1 3151 ? 222.723 195.807 256.206 1.00 8.80   ? 3151 HIS A ND1   1 
ATOM   12820 C  CD2   . HIS A 1 3151 ? 224.500 197.026 256.550 1.00 10.13  ? 3151 HIS A CD2   1 
ATOM   12821 C  CE1   . HIS A 1 3151 ? 222.425 197.041 255.845 1.00 8.31   ? 3151 HIS A CE1   1 
ATOM   12822 N  NE2   . HIS A 1 3151 ? 223.486 197.801 256.044 1.00 11.32  ? 3151 HIS A NE2   1 
ATOM   12823 N  N     . GLN A 1 3152 ? 227.426 194.328 255.615 1.00 14.56  ? 3152 GLN A N     1 
ATOM   12824 C  CA    . GLN A 1 3152 ? 228.465 195.018 254.849 1.00 15.24  ? 3152 GLN A CA    1 
ATOM   12825 C  C     . GLN A 1 3152 ? 228.830 194.262 253.575 1.00 18.00  ? 3152 GLN A C     1 
ATOM   12826 O  O     . GLN A 1 3152 ? 229.334 194.861 252.610 1.00 19.11  ? 3152 GLN A O     1 
ATOM   12827 C  CB    . GLN A 1 3152 ? 229.699 195.236 255.721 1.00 18.28  ? 3152 GLN A CB    1 
ATOM   12828 C  CG    . GLN A 1 3152 ? 229.390 195.879 257.062 1.00 15.65  ? 3152 GLN A CG    1 
ATOM   12829 C  CD    . GLN A 1 3152 ? 230.607 196.508 257.703 1.00 22.46  ? 3152 GLN A CD    1 
ATOM   12830 O  OE1   . GLN A 1 3152 ? 231.692 195.927 257.704 1.00 35.23  ? 3152 GLN A OE1   1 
ATOM   12831 N  NE2   . GLN A 1 3152 ? 230.433 197.700 258.261 1.00 20.24  ? 3152 GLN A NE2   1 
ATOM   12832 N  N     . THR A 1 3153 ? 228.581 192.952 253.552 1.00 19.29  ? 3153 THR A N     1 
ATOM   12833 C  CA    . THR A 1 3153 ? 228.817 192.168 252.348 1.00 14.51  ? 3153 THR A CA    1 
ATOM   12834 C  C     . THR A 1 3153 ? 227.940 192.643 251.201 1.00 14.75  ? 3153 THR A C     1 
ATOM   12835 O  O     . THR A 1 3153 ? 228.360 192.595 250.044 1.00 21.19  ? 3153 THR A O     1 
ATOM   12836 C  CB    . THR A 1 3153 ? 228.572 190.687 252.631 1.00 15.27  ? 3153 THR A CB    1 
ATOM   12837 O  OG1   . THR A 1 3153 ? 229.337 190.289 253.775 1.00 18.82  ? 3153 THR A OG1   1 
ATOM   12838 C  CG2   . THR A 1 3153 ? 228.986 189.836 251.443 1.00 23.12  ? 3153 THR A CG2   1 
ATOM   12839 N  N     . LEU A 1 3154 ? 226.729 193.113 251.499 1.00 15.90  ? 3154 LEU A N     1 
ATOM   12840 C  CA    . LEU A 1 3154 ? 225.866 193.635 250.444 1.00 14.11  ? 3154 LEU A CA    1 
ATOM   12841 C  C     . LEU A 1 3154 ? 226.409 194.940 249.878 1.00 17.59  ? 3154 LEU A C     1 
ATOM   12842 O  O     . LEU A 1 3154 ? 226.288 195.193 248.676 1.00 23.54  ? 3154 LEU A O     1 
ATOM   12843 C  CB    . LEU A 1 3154 ? 224.441 193.821 250.960 1.00 10.11  ? 3154 LEU A CB    1 
ATOM   12844 C  CG    . LEU A 1 3154 ? 223.532 192.589 250.921 1.00 8.68   ? 3154 LEU A CG    1 
ATOM   12845 C  CD1   . LEU A 1 3154 ? 223.314 192.154 249.485 1.00 9.11   ? 3154 LEU A CD1   1 
ATOM   12846 C  CD2   . LEU A 1 3154 ? 224.070 191.437 251.752 1.00 10.44  ? 3154 LEU A CD2   1 
ATOM   12847 N  N     . HIS A 1 3155 ? 227.002 195.786 250.723 1.00 20.59  ? 3155 HIS A N     1 
ATOM   12848 C  CA    . HIS A 1 3155 ? 227.659 196.983 250.208 1.00 21.18  ? 3155 HIS A CA    1 
ATOM   12849 C  C     . HIS A 1 3155 ? 228.825 196.618 249.301 1.00 18.77  ? 3155 HIS A C     1 
ATOM   12850 O  O     . HIS A 1 3155 ? 228.988 197.194 248.218 1.00 20.56  ? 3155 HIS A O     1 
ATOM   12851 C  CB    . HIS A 1 3155 ? 228.133 197.863 251.365 1.00 17.26  ? 3155 HIS A CB    1 
ATOM   12852 C  CG    . HIS A 1 3155 ? 227.023 198.574 252.074 1.00 21.46  ? 3155 HIS A CG    1 
ATOM   12853 N  ND1   . HIS A 1 3155 ? 226.730 198.358 253.402 1.00 23.49  ? 3155 HIS A ND1   1 
ATOM   12854 C  CD2   . HIS A 1 3155 ? 226.136 199.499 251.638 1.00 21.11  ? 3155 HIS A CD2   1 
ATOM   12855 C  CE1   . HIS A 1 3155 ? 225.709 199.119 253.755 1.00 25.78  ? 3155 HIS A CE1   1 
ATOM   12856 N  NE2   . HIS A 1 3155 ? 225.330 199.821 252.702 1.00 20.85  ? 3155 HIS A NE2   1 
ATOM   12857 N  N     . GLN A 1 3156 ? 229.642 195.649 249.724 1.00 25.78  ? 3156 GLN A N     1 
ATOM   12858 C  CA    . GLN A 1 3156 ? 230.741 195.194 248.874 1.00 23.92  ? 3156 GLN A CA    1 
ATOM   12859 C  C     . GLN A 1 3156 ? 230.218 194.625 247.559 1.00 23.58  ? 3156 GLN A C     1 
ATOM   12860 O  O     . GLN A 1 3156 ? 230.785 194.878 246.487 1.00 26.56  ? 3156 GLN A O     1 
ATOM   12861 C  CB    . GLN A 1 3156 ? 231.580 194.151 249.611 1.00 23.91  ? 3156 GLN A CB    1 
ATOM   12862 C  CG    . GLN A 1 3156 ? 232.207 194.652 250.899 1.00 26.70  ? 3156 GLN A CG    1 
ATOM   12863 C  CD    . GLN A 1 3156 ? 232.579 193.523 251.841 1.00 39.52  ? 3156 GLN A CD    1 
ATOM   12864 O  OE1   . GLN A 1 3156 ? 232.576 193.689 253.060 1.00 38.19  ? 3156 GLN A OE1   1 
ATOM   12865 N  NE2   . GLN A 1 3156 ? 232.901 192.364 251.277 1.00 33.78  ? 3156 GLN A NE2   1 
ATOM   12866 N  N     . ALA A 1 3157 ? 229.131 193.858 247.626 1.00 25.17  ? 3157 ALA A N     1 
ATOM   12867 C  CA    . ALA A 1 3157 ? 228.525 193.275 246.435 1.00 23.44  ? 3157 ALA A CA    1 
ATOM   12868 C  C     . ALA A 1 3157 ? 228.018 194.348 245.483 1.00 27.63  ? 3157 ALA A C     1 
ATOM   12869 O  O     . ALA A 1 3157 ? 228.231 194.260 244.269 1.00 33.99  ? 3157 ALA A O     1 
ATOM   12870 C  CB    . ALA A 1 3157 ? 227.384 192.349 246.847 1.00 18.15  ? 3157 ALA A CB    1 
ATOM   12871 N  N     . ASN A 1 3158 ? 227.329 195.357 246.015 1.00 25.72  ? 3158 ASN A N     1 
ATOM   12872 C  CA    . ASN A 1 3158 ? 226.825 196.431 245.172 1.00 23.85  ? 3158 ASN A CA    1 
ATOM   12873 C  C     . ASN A 1 3158 ? 227.970 197.208 244.544 1.00 30.83  ? 3158 ASN A C     1 
ATOM   12874 O  O     . ASN A 1 3158 ? 227.877 197.625 243.386 1.00 36.28  ? 3158 ASN A O     1 
ATOM   12875 C  CB    . ASN A 1 3158 ? 225.919 197.355 245.982 1.00 24.71  ? 3158 ASN A CB    1 
ATOM   12876 C  CG    . ASN A 1 3158 ? 224.486 196.879 246.006 1.00 23.06  ? 3158 ASN A CG    1 
ATOM   12877 O  OD1   . ASN A 1 3158 ? 223.643 197.380 245.266 1.00 23.45  ? 3158 ASN A OD1   1 
ATOM   12878 N  ND2   . ASN A 1 3158 ? 224.202 195.898 246.853 1.00 19.87  ? 3158 ASN A ND2   1 
ATOM   12879 N  N     . ALA A 1 3159 ? 229.064 197.400 245.284 1.00 35.82  ? 3159 ALA A N     1 
ATOM   12880 C  CA    . ALA A 1 3159 ? 230.248 198.010 244.690 1.00 29.99  ? 3159 ALA A CA    1 
ATOM   12881 C  C     . ALA A 1 3159 ? 230.784 197.165 243.540 1.00 31.65  ? 3159 ALA A C     1 
ATOM   12882 O  O     . ALA A 1 3159 ? 231.160 197.698 242.489 1.00 37.33  ? 3159 ALA A O     1 
ATOM   12883 C  CB    . ALA A 1 3159 ? 231.327 198.215 245.754 1.00 22.38  ? 3159 ALA A CB    1 
ATOM   12884 N  N     . ARG A 1 3160 ? 230.826 195.843 243.723 1.00 29.46  ? 3160 ARG A N     1 
ATOM   12885 C  CA    . ARG A 1 3160 ? 231.336 194.968 242.670 1.00 33.51  ? 3160 ARG A CA    1 
ATOM   12886 C  C     . ARG A 1 3160 ? 230.455 195.011 241.423 1.00 41.21  ? 3160 ARG A C     1 
ATOM   12887 O  O     . ARG A 1 3160 ? 230.966 195.060 240.298 1.00 45.51  ? 3160 ARG A O     1 
ATOM   12888 C  CB    . ARG A 1 3160 ? 231.481 193.541 243.198 1.00 37.43  ? 3160 ARG A CB    1 
ATOM   12889 C  CG    . ARG A 1 3160 ? 231.818 192.510 242.133 1.00 42.05  ? 3160 ARG A CG    1 
ATOM   12890 C  CD    . ARG A 1 3160 ? 231.835 191.103 242.709 1.00 51.14  ? 3160 ARG A CD    1 
ATOM   12891 N  NE    . ARG A 1 3160 ? 230.943 190.960 243.853 1.00 49.23  ? 3160 ARG A NE    1 
ATOM   12892 C  CZ    . ARG A 1 3160 ? 231.242 190.272 244.947 1.00 50.51  ? 3160 ARG A CZ    1 
ATOM   12893 N  NH1   . ARG A 1 3160 ? 232.398 189.641 245.072 1.00 62.11  ? 3160 ARG A NH1   1 
ATOM   12894 N  NH2   . ARG A 1 3160 ? 230.362 190.221 245.942 1.00 37.40  ? 3160 ARG A NH2   1 
ATOM   12895 N  N     . LEU A 1 3161 ? 229.130 194.985 241.596 1.00 39.32  ? 3161 LEU A N     1 
ATOM   12896 C  CA    . LEU A 1 3161 ? 228.243 195.154 240.441 1.00 37.24  ? 3161 LEU A CA    1 
ATOM   12897 C  C     . LEU A 1 3161 ? 228.391 196.535 239.813 1.00 39.10  ? 3161 LEU A C     1 
ATOM   12898 O  O     . LEU A 1 3161 ? 228.261 196.682 238.593 1.00 43.23  ? 3161 LEU A O     1 
ATOM   12899 C  CB    . LEU A 1 3161 ? 226.779 194.896 240.812 1.00 38.56  ? 3161 LEU A CB    1 
ATOM   12900 C  CG    . LEU A 1 3161 ? 226.224 193.473 240.966 1.00 42.07  ? 3161 LEU A CG    1 
ATOM   12901 C  CD1   . LEU A 1 3161 ? 226.707 192.737 242.196 1.00 41.00  ? 3161 LEU A CD1   1 
ATOM   12902 C  CD2   . LEU A 1 3161 ? 224.702 193.516 240.933 1.00 40.96  ? 3161 LEU A CD2   1 
ATOM   12903 N  N     . ALA A 1 3162 ? 228.646 197.562 240.627 1.00 35.39  ? 3162 ALA A N     1 
ATOM   12904 C  CA    . ALA A 1 3162 ? 228.854 198.899 240.080 1.00 39.07  ? 3162 ALA A CA    1 
ATOM   12905 C  C     . ALA A 1 3162 ? 230.093 198.944 239.198 1.00 48.21  ? 3162 ALA A C     1 
ATOM   12906 O  O     . ALA A 1 3162 ? 230.084 199.567 238.129 1.00 47.00  ? 3162 ALA A O     1 
ATOM   12907 C  CB    . ALA A 1 3162 ? 228.964 199.918 241.214 1.00 32.50  ? 3162 ALA A CB    1 
ATOM   12908 N  N     . LYS A 1 3163 ? 231.173 198.287 239.628 1.00 48.18  ? 3163 LYS A N     1 
ATOM   12909 C  CA    . LYS A 1 3163 ? 232.393 198.270 238.832 1.00 44.33  ? 3163 LYS A CA    1 
ATOM   12910 C  C     . LYS A 1 3163 ? 232.245 197.438 237.565 1.00 47.62  ? 3163 LYS A C     1 
ATOM   12911 O  O     . LYS A 1 3163 ? 233.026 197.622 236.626 1.00 54.27  ? 3163 LYS A O     1 
ATOM   12912 C  CB    . LYS A 1 3163 ? 233.565 197.751 239.667 1.00 43.80  ? 3163 LYS A CB    1 
ATOM   12913 C  CG    . LYS A 1 3163 ? 233.783 198.497 240.976 1.00 44.95  ? 3163 LYS A CG    1 
ATOM   12914 C  CD    . LYS A 1 3163 ? 233.661 200.003 240.794 1.00 43.96  ? 3163 LYS A CD    1 
ATOM   12915 C  CE    . LYS A 1 3163 ? 233.202 200.679 242.076 1.00 41.47  ? 3163 LYS A CE    1 
ATOM   12916 N  NZ    . LYS A 1 3163 ? 234.033 200.288 243.249 1.00 33.92  ? 3163 LYS A NZ    1 
ATOM   12917 N  N     . ARG A 1 3164 ? 231.272 196.529 237.517 1.00 47.65  ? 3164 ARG A N     1 
ATOM   12918 C  CA    . ARG A 1 3164 ? 231.006 195.740 236.323 1.00 45.87  ? 3164 ARG A CA    1 
ATOM   12919 C  C     . ARG A 1 3164 ? 229.907 196.335 235.451 1.00 48.04  ? 3164 ARG A C     1 
ATOM   12920 O  O     . ARG A 1 3164 ? 229.553 195.736 234.431 1.00 44.62  ? 3164 ARG A O     1 
ATOM   12921 C  CB    . ARG A 1 3164 ? 230.642 194.300 236.701 1.00 46.71  ? 3164 ARG A CB    1 
ATOM   12922 C  CG    . ARG A 1 3164 ? 231.794 193.505 237.296 1.00 46.07  ? 3164 ARG A CG    1 
ATOM   12923 C  CD    . ARG A 1 3164 ? 231.397 192.063 237.576 1.00 53.35  ? 3164 ARG A CD    1 
ATOM   12924 N  NE    . ARG A 1 3164 ? 230.435 191.937 238.664 1.00 61.45  ? 3164 ARG A NE    1 
ATOM   12925 C  CZ    . ARG A 1 3164 ? 229.183 191.528 238.508 1.00 59.96  ? 3164 ARG A CZ    1 
ATOM   12926 N  NH1   . ARG A 1 3164 ? 228.699 191.219 237.316 1.00 58.02  ? 3164 ARG A NH1   1 
ATOM   12927 N  NH2   . ARG A 1 3164 ? 228.397 191.423 239.576 1.00 59.90  ? 3164 ARG A NH2   1 
ATOM   12928 N  N     . GLY A 1 3165 ? 229.355 197.486 235.828 1.00 46.85  ? 3165 GLY A N     1 
ATOM   12929 C  CA    . GLY A 1 3165 ? 228.376 198.151 234.993 1.00 45.80  ? 3165 GLY A CA    1 
ATOM   12930 C  C     . GLY A 1 3165 ? 226.961 197.632 235.097 1.00 53.02  ? 3165 GLY A C     1 
ATOM   12931 O  O     . GLY A 1 3165 ? 226.159 197.875 234.190 1.00 52.40  ? 3165 GLY A O     1 
ATOM   12932 N  N     . GLY A 1 3166 ? 226.625 196.920 236.173 1.00 57.54  ? 3166 GLY A N     1 
ATOM   12933 C  CA    . GLY A 1 3166 ? 225.286 196.415 236.370 1.00 47.65  ? 3166 GLY A CA    1 
ATOM   12934 C  C     . GLY A 1 3166 ? 224.455 197.309 237.272 1.00 38.33  ? 3166 GLY A C     1 
ATOM   12935 O  O     . GLY A 1 3166 ? 224.980 198.121 238.029 1.00 39.20  ? 3166 GLY A O     1 
ATOM   12936 N  N     . ARG A 1 3167 ? 223.137 197.147 237.178 1.00 40.14  ? 3167 ARG A N     1 
ATOM   12937 C  CA    . ARG A 1 3167 ? 222.228 197.912 238.023 1.00 39.23  ? 3167 ARG A CA    1 
ATOM   12938 C  C     . ARG A 1 3167 ? 222.369 197.473 239.475 1.00 38.07  ? 3167 ARG A C     1 
ATOM   12939 O  O     . ARG A 1 3167 ? 222.431 196.276 239.770 1.00 39.21  ? 3167 ARG A O     1 
ATOM   12940 C  CB    . ARG A 1 3167 ? 220.781 197.737 237.562 1.00 41.52  ? 3167 ARG A CB    1 
ATOM   12941 C  CG    . ARG A 1 3167 ? 220.406 198.520 236.312 1.00 51.08  ? 3167 ARG A CG    1 
ATOM   12942 C  CD    . ARG A 1 3167 ? 220.771 197.770 235.041 1.00 55.42  ? 3167 ARG A CD    1 
ATOM   12943 N  NE    . ARG A 1 3167 ? 220.209 198.408 233.856 1.00 59.62  ? 3167 ARG A NE    1 
ATOM   12944 C  CZ    . ARG A 1 3167 ? 220.850 199.298 233.112 1.00 61.68  ? 3167 ARG A CZ    1 
ATOM   12945 N  NH1   . ARG A 1 3167 ? 222.081 199.685 233.403 1.00 62.96  ? 3167 ARG A NH1   1 
ATOM   12946 N  NH2   . ARG A 1 3167 ? 220.240 199.813 232.048 1.00 55.97  ? 3167 ARG A NH2   1 
ATOM   12947 N  N     . THR A 1 3168 ? 222.421 198.446 240.379 1.00 33.80  ? 3168 THR A N     1 
ATOM   12948 C  CA    . THR A 1 3168 ? 222.558 198.193 241.805 1.00 25.49  ? 3168 THR A CA    1 
ATOM   12949 C  C     . THR A 1 3168 ? 221.433 198.886 242.560 1.00 21.92  ? 3168 THR A C     1 
ATOM   12950 O  O     . THR A 1 3168 ? 221.083 200.030 242.257 1.00 26.10  ? 3168 THR A O     1 
ATOM   12951 C  CB    . THR A 1 3168 ? 223.911 198.680 242.333 1.00 28.22  ? 3168 THR A CB    1 
ATOM   12952 O  OG1   . THR A 1 3168 ? 224.022 200.094 242.142 1.00 40.95  ? 3168 THR A OG1   1 
ATOM   12953 C  CG2   . THR A 1 3168 ? 225.047 197.987 241.605 1.00 33.69  ? 3168 THR A CG2   1 
ATOM   12954 N  N     . MET A 1 3169 ? 220.872 198.187 243.540 1.00 21.09  ? 3169 MET A N     1 
ATOM   12955 C  CA    . MET A 1 3169 ? 219.842 198.738 244.406 1.00 19.36  ? 3169 MET A CA    1 
ATOM   12956 C  C     . MET A 1 3169 ? 220.446 199.102 245.755 1.00 15.40  ? 3169 MET A C     1 
ATOM   12957 O  O     . MET A 1 3169 ? 221.279 198.368 246.294 1.00 14.87  ? 3169 MET A O     1 
ATOM   12958 C  CB    . MET A 1 3169 ? 218.691 197.746 244.592 1.00 20.68  ? 3169 MET A CB    1 
ATOM   12959 C  CG    . MET A 1 3169 ? 217.940 197.432 243.311 1.00 22.73  ? 3169 MET A CG    1 
ATOM   12960 S  SD    . MET A 1 3169 ? 217.209 198.908 242.576 1.00 35.08  ? 3169 MET A SD    1 
ATOM   12961 C  CE    . MET A 1 3169 ? 217.164 198.453 240.848 1.00 18.53  ? 3169 MET A CE    1 
ATOM   12962 N  N     . ALA A 1 3170 ? 220.024 200.243 246.293 1.00 14.84  ? 3170 ALA A N     1 
ATOM   12963 C  CA    . ALA A 1 3170 ? 220.595 200.747 247.532 1.00 13.99  ? 3170 ALA A CA    1 
ATOM   12964 C  C     . ALA A 1 3170 ? 220.301 199.807 248.693 1.00 15.41  ? 3170 ALA A C     1 
ATOM   12965 O  O     . ALA A 1 3170 ? 219.194 199.278 248.823 1.00 19.63  ? 3170 ALA A O     1 
ATOM   12966 C  CB    . ALA A 1 3170 ? 220.047 202.140 247.836 1.00 12.88  ? 3170 ALA A CB    1 
ATOM   12967 N  N     . ILE A 1 3171 ? 221.304 199.599 249.540 1.00 10.63  ? 3171 ILE A N     1 
ATOM   12968 C  CA    . ILE A 1 3171 ? 221.172 198.784 250.740 1.00 10.70  ? 3171 ILE A CA    1 
ATOM   12969 C  C     . ILE A 1 3171 ? 221.018 199.725 251.925 1.00 11.24  ? 3171 ILE A C     1 
ATOM   12970 O  O     . ILE A 1 3171 ? 221.931 200.497 252.239 1.00 17.30  ? 3171 ILE A O     1 
ATOM   12971 C  CB    . ILE A 1 3171 ? 222.378 197.850 250.923 1.00 12.72  ? 3171 ILE A CB    1 
ATOM   12972 C  CG1   . ILE A 1 3171 ? 222.594 197.006 249.667 1.00 11.30  ? 3171 ILE A CG1   1 
ATOM   12973 C  CG2   . ILE A 1 3171 ? 222.178 196.961 252.139 1.00 12.71  ? 3171 ILE A CG2   1 
ATOM   12974 C  CD1   . ILE A 1 3171 ? 221.454 196.067 249.353 1.00 7.74   ? 3171 ILE A CD1   1 
ATOM   12975 N  N     . THR A 1 3172 ? 219.872 199.659 252.580 1.00 12.84  ? 3172 THR A N     1 
ATOM   12976 C  CA    . THR A 1 3172 ? 219.479 200.574 253.634 1.00 11.62  ? 3172 THR A CA    1 
ATOM   12977 C  C     . THR A 1 3172 ? 219.481 199.881 254.990 1.00 8.63   ? 3172 THR A C     1 
ATOM   12978 O  O     . THR A 1 3172 ? 219.540 198.651 255.076 1.00 10.01  ? 3172 THR A O     1 
ATOM   12979 C  CB    . THR A 1 3172 ? 218.086 201.142 253.338 1.00 11.34  ? 3172 THR A CB    1 
ATOM   12980 O  OG1   . THR A 1 3172 ? 217.096 200.133 253.571 1.00 13.74  ? 3172 THR A OG1   1 
ATOM   12981 C  CG2   . THR A 1 3172 ? 217.999 201.602 251.892 1.00 11.58  ? 3172 THR A CG2   1 
ATOM   12982 N  N     . PRO A 1 3173 ? 219.436 200.649 256.084 1.00 8.86   ? 3173 PRO A N     1 
ATOM   12983 C  CA    . PRO A 1 3173 ? 219.246 200.025 257.402 1.00 7.84   ? 3173 PRO A CA    1 
ATOM   12984 C  C     . PRO A 1 3173 ? 217.946 199.249 257.519 1.00 7.31   ? 3173 PRO A C     1 
ATOM   12985 O  O     . PRO A 1 3173 ? 217.847 198.360 258.374 1.00 9.51   ? 3173 PRO A O     1 
ATOM   12986 C  CB    . PRO A 1 3173 ? 219.275 201.222 258.360 1.00 8.85   ? 3173 PRO A CB    1 
ATOM   12987 C  CG    . PRO A 1 3173 ? 220.098 202.236 257.655 1.00 7.54   ? 3173 PRO A CG    1 
ATOM   12988 C  CD    . PRO A 1 3173 ? 219.778 202.079 256.199 1.00 11.11  ? 3173 PRO A CD    1 
ATOM   12989 N  N     . ARG A 1 3174 ? 216.945 199.561 256.693 1.00 8.68   ? 3174 ARG A N     1 
ATOM   12990 C  CA    . ARG A 1 3174 ? 215.730 198.756 256.665 1.00 8.83   ? 3174 ARG A CA    1 
ATOM   12991 C  C     . ARG A 1 3174 ? 216.020 197.331 256.217 1.00 8.20   ? 3174 ARG A C     1 
ATOM   12992 O  O     . ARG A 1 3174 ? 215.361 196.391 256.675 1.00 10.77  ? 3174 ARG A O     1 
ATOM   12993 C  CB    . ARG A 1 3174 ? 214.693 199.408 255.750 1.00 10.52  ? 3174 ARG A CB    1 
ATOM   12994 C  CG    . ARG A 1 3174 ? 214.145 200.720 256.282 1.00 10.32  ? 3174 ARG A CG    1 
ATOM   12995 C  CD    . ARG A 1 3174 ? 212.813 201.063 255.645 1.00 11.21  ? 3174 ARG A CD    1 
ATOM   12996 N  NE    . ARG A 1 3174 ? 211.729 200.238 256.160 1.00 11.54  ? 3174 ARG A NE    1 
ATOM   12997 C  CZ    . ARG A 1 3174 ? 210.451 200.406 255.851 1.00 14.67  ? 3174 ARG A CZ    1 
ATOM   12998 N  NH1   . ARG A 1 3174 ? 210.060 201.362 255.025 1.00 14.05  ? 3174 ARG A NH1   1 
ATOM   12999 N  NH2   . ARG A 1 3174 ? 209.542 199.592 256.380 1.00 16.71  ? 3174 ARG A NH2   1 
ATOM   13000 N  N     . HIS A 1 3175 ? 217.004 197.151 255.332 1.00 8.11   ? 3175 HIS A N     1 
ATOM   13001 C  CA    . HIS A 1 3175 ? 217.438 195.805 254.972 1.00 8.96   ? 3175 HIS A CA    1 
ATOM   13002 C  C     . HIS A 1 3175 ? 217.959 195.058 256.192 1.00 8.87   ? 3175 HIS A C     1 
ATOM   13003 O  O     . HIS A 1 3175 ? 217.633 193.885 256.401 1.00 11.45  ? 3175 HIS A O     1 
ATOM   13004 C  CB    . HIS A 1 3175 ? 218.522 195.871 253.896 1.00 9.37   ? 3175 HIS A CB    1 
ATOM   13005 C  CG    . HIS A 1 3175 ? 218.024 196.301 252.554 1.00 8.27   ? 3175 HIS A CG    1 
ATOM   13006 N  ND1   . HIS A 1 3175 ? 217.442 197.531 252.335 1.00 10.98  ? 3175 HIS A ND1   1 
ATOM   13007 C  CD2   . HIS A 1 3175 ? 218.031 195.670 251.357 1.00 9.62   ? 3175 HIS A CD2   1 
ATOM   13008 C  CE1   . HIS A 1 3175 ? 217.108 197.636 251.062 1.00 12.56  ? 3175 HIS A CE1   1 
ATOM   13009 N  NE2   . HIS A 1 3175 ? 217.454 196.521 250.447 1.00 12.04  ? 3175 HIS A NE2   1 
ATOM   13010 N  N     . TYR A 1 3176 ? 218.775 195.729 257.010 1.00 7.23   ? 3176 TYR A N     1 
ATOM   13011 C  CA    . TYR A 1 3176 ? 219.290 195.108 258.224 1.00 7.09   ? 3176 TYR A CA    1 
ATOM   13012 C  C     . TYR A 1 3176 ? 218.164 194.775 259.192 1.00 8.19   ? 3176 TYR A C     1 
ATOM   13013 O  O     . TYR A 1 3176 ? 218.167 193.708 259.820 1.00 10.33  ? 3176 TYR A O     1 
ATOM   13014 C  CB    . TYR A 1 3176 ? 220.310 196.033 258.885 1.00 8.14   ? 3176 TYR A CB    1 
ATOM   13015 C  CG    . TYR A 1 3176 ? 221.090 195.394 260.010 1.00 8.57   ? 3176 TYR A CG    1 
ATOM   13016 C  CD1   . TYR A 1 3176 ? 222.085 194.465 259.746 1.00 8.75   ? 3176 TYR A CD1   1 
ATOM   13017 C  CD2   . TYR A 1 3176 ? 220.830 195.717 261.334 1.00 7.37   ? 3176 TYR A CD2   1 
ATOM   13018 C  CE1   . TYR A 1 3176 ? 222.801 193.878 260.768 1.00 10.67  ? 3176 TYR A CE1   1 
ATOM   13019 C  CE2   . TYR A 1 3176 ? 221.540 195.135 262.362 1.00 7.80   ? 3176 TYR A CE2   1 
ATOM   13020 C  CZ    . TYR A 1 3176 ? 222.524 194.217 262.073 1.00 12.05  ? 3176 TYR A CZ    1 
ATOM   13021 O  OH    . TYR A 1 3176 ? 223.238 193.631 263.093 1.00 17.28  ? 3176 TYR A OH    1 
ATOM   13022 N  N     . LEU A 1 3177 ? 217.197 195.683 259.337 1.00 7.33   ? 3177 LEU A N     1 
ATOM   13023 C  CA    . LEU A 1 3177 ? 216.074 195.426 260.233 1.00 8.98   ? 3177 LEU A CA    1 
ATOM   13024 C  C     . LEU A 1 3177 ? 215.258 194.228 259.763 1.00 10.02  ? 3177 LEU A C     1 
ATOM   13025 O  O     . LEU A 1 3177 ? 214.851 193.389 260.575 1.00 17.08  ? 3177 LEU A O     1 
ATOM   13026 C  CB    . LEU A 1 3177 ? 215.199 196.673 260.347 1.00 8.99   ? 3177 LEU A CB    1 
ATOM   13027 C  CG    . LEU A 1 3177 ? 215.883 197.895 260.962 1.00 10.30  ? 3177 LEU A CG    1 
ATOM   13028 C  CD1   . LEU A 1 3177 ? 215.107 199.165 260.656 1.00 11.72  ? 3177 LEU A CD1   1 
ATOM   13029 C  CD2   . LEU A 1 3177 ? 216.052 197.716 262.460 1.00 8.32   ? 3177 LEU A CD2   1 
ATOM   13030 N  N     . ASP A 1 3178 ? 215.018 194.125 258.452 1.00 9.45   ? 3178 ASP A N     1 
ATOM   13031 C  CA    . ASP A 1 3178 ? 214.330 192.954 257.917 1.00 10.00  ? 3178 ASP A CA    1 
ATOM   13032 C  C     . ASP A 1 3178 ? 215.134 191.687 258.157 1.00 11.21  ? 3178 ASP A C     1 
ATOM   13033 O  O     . ASP A 1 3178 ? 214.568 190.637 258.475 1.00 13.56  ? 3178 ASP A O     1 
ATOM   13034 C  CB    . ASP A 1 3178 ? 214.066 193.119 256.424 1.00 11.16  ? 3178 ASP A CB    1 
ATOM   13035 C  CG    . ASP A 1 3178 ? 213.044 194.182 256.126 1.00 26.92  ? 3178 ASP A CG    1 
ATOM   13036 O  OD1   . ASP A 1 3178 ? 212.154 194.417 256.969 1.00 34.14  ? 3178 ASP A OD1   1 
ATOM   13037 O  OD2   . ASP A 1 3178 ? 213.130 194.774 255.035 1.00 35.31  ? 3178 ASP A OD2   1 
ATOM   13038 N  N     . PHE A 1 3179 ? 216.455 191.760 257.983 1.00 9.45   ? 3179 PHE A N     1 
ATOM   13039 C  CA    . PHE A 1 3179 ? 217.292 190.584 258.188 1.00 7.19   ? 3179 PHE A CA    1 
ATOM   13040 C  C     . PHE A 1 3179 ? 217.201 190.099 259.628 1.00 11.72  ? 3179 PHE A C     1 
ATOM   13041 O  O     . PHE A 1 3179 ? 217.040 188.900 259.878 1.00 16.01  ? 3179 PHE A O     1 
ATOM   13042 C  CB    . PHE A 1 3179 ? 218.737 190.911 257.800 1.00 8.22   ? 3179 PHE A CB    1 
ATOM   13043 C  CG    . PHE A 1 3179 ? 219.756 189.925 258.305 1.00 9.32   ? 3179 PHE A CG    1 
ATOM   13044 C  CD1   . PHE A 1 3179 ? 219.571 188.563 258.143 1.00 11.48  ? 3179 PHE A CD1   1 
ATOM   13045 C  CD2   . PHE A 1 3179 ? 220.917 190.365 258.916 1.00 9.88   ? 3179 PHE A CD2   1 
ATOM   13046 C  CE1   . PHE A 1 3179 ? 220.510 187.662 258.600 1.00 12.78  ? 3179 PHE A CE1   1 
ATOM   13047 C  CE2   . PHE A 1 3179 ? 221.860 189.467 259.370 1.00 12.31  ? 3179 PHE A CE2   1 
ATOM   13048 C  CZ    . PHE A 1 3179 ? 221.655 188.113 259.211 1.00 12.53  ? 3179 PHE A CZ    1 
ATOM   13049 N  N     . ILE A 1 3180 ? 217.262 191.022 260.589 1.00 13.30  ? 3180 ILE A N     1 
ATOM   13050 C  CA    . ILE A 1 3180 ? 217.196 190.626 261.994 1.00 11.63  ? 3180 ILE A CA    1 
ATOM   13051 C  C     . ILE A 1 3180 ? 215.802 190.115 262.350 1.00 11.69  ? 3180 ILE A C     1 
ATOM   13052 O  O     . ILE A 1 3180 ? 215.656 189.154 263.117 1.00 16.11  ? 3180 ILE A O     1 
ATOM   13053 C  CB    . ILE A 1 3180 ? 217.630 191.789 262.904 1.00 14.41  ? 3180 ILE A CB    1 
ATOM   13054 C  CG1   . ILE A 1 3180 ? 218.974 192.352 262.446 1.00 10.76  ? 3180 ILE A CG1   1 
ATOM   13055 C  CG2   . ILE A 1 3180 ? 217.759 191.317 264.332 1.00 19.45  ? 3180 ILE A CG2   1 
ATOM   13056 C  CD1   . ILE A 1 3180 ? 220.101 191.348 262.482 1.00 11.07  ? 3180 ILE A CD1   1 
ATOM   13057 N  N     . ASN A 1 3181 ? 214.755 190.745 261.807 1.00 13.65  ? 3181 ASN A N     1 
ATOM   13058 C  CA    . ASN A 1 3181 ? 213.397 190.272 262.064 1.00 16.93  ? 3181 ASN A CA    1 
ATOM   13059 C  C     . ASN A 1 3181 ? 213.189 188.866 261.514 1.00 16.95  ? 3181 ASN A C     1 
ATOM   13060 O  O     . ASN A 1 3181 ? 212.613 188.002 262.189 1.00 19.18  ? 3181 ASN A O     1 
ATOM   13061 C  CB    . ASN A 1 3181 ? 212.384 191.244 261.454 1.00 17.37  ? 3181 ASN A CB    1 
ATOM   13062 C  CG    . ASN A 1 3181 ? 211.059 191.246 262.189 1.00 27.75  ? 3181 ASN A CG    1 
ATOM   13063 O  OD1   . ASN A 1 3181 ? 210.220 190.369 261.986 1.00 30.75  ? 3181 ASN A OD1   1 
ATOM   13064 N  ND2   . ASN A 1 3181 ? 210.860 192.244 263.043 1.00 28.31  ? 3181 ASN A ND2   1 
ATOM   13065 N  N     . HIS A 1 3182 ? 213.663 188.617 260.289 1.00 15.02  ? 3182 HIS A N     1 
ATOM   13066 C  CA    . HIS A 1 3182 ? 213.589 187.281 259.713 1.00 11.69  ? 3182 HIS A CA    1 
ATOM   13067 C  C     . HIS A 1 3182 ? 214.394 186.288 260.536 1.00 15.20  ? 3182 HIS A C     1 
ATOM   13068 O  O     . HIS A 1 3182 ? 213.976 185.141 260.714 1.00 23.40  ? 3182 HIS A O     1 
ATOM   13069 C  CB    . HIS A 1 3182 ? 214.089 187.296 258.269 1.00 10.94  ? 3182 HIS A CB    1 
ATOM   13070 C  CG    . HIS A 1 3182 ? 213.109 187.862 257.289 1.00 11.44  ? 3182 HIS A CG    1 
ATOM   13071 N  ND1   . HIS A 1 3182 ? 213.481 188.718 256.276 1.00 9.21   ? 3182 HIS A ND1   1 
ATOM   13072 C  CD2   . HIS A 1 3182 ? 211.773 187.686 257.161 1.00 14.93  ? 3182 HIS A CD2   1 
ATOM   13073 C  CE1   . HIS A 1 3182 ? 212.415 189.049 255.569 1.00 12.53  ? 3182 HIS A CE1   1 
ATOM   13074 N  NE2   . HIS A 1 3182 ? 211.367 188.437 256.086 1.00 15.37  ? 3182 HIS A NE2   1 
ATOM   13075 N  N     . TYR A 1 3183 ? 215.555 186.709 261.038 1.00 12.18  ? 3183 TYR A N     1 
ATOM   13076 C  CA    . TYR A 1 3183 ? 216.366 185.828 261.870 1.00 14.02  ? 3183 TYR A CA    1 
ATOM   13077 C  C     . TYR A 1 3183 ? 215.597 185.407 263.115 1.00 19.07  ? 3183 TYR A C     1 
ATOM   13078 O  O     . TYR A 1 3183 ? 215.533 184.217 263.446 1.00 27.27  ? 3183 TYR A O     1 
ATOM   13079 C  CB    . TYR A 1 3183 ? 217.667 186.537 262.249 1.00 15.38  ? 3183 TYR A CB    1 
ATOM   13080 C  CG    . TYR A 1 3183 ? 218.713 185.670 262.917 1.00 18.16  ? 3183 TYR A CG    1 
ATOM   13081 C  CD1   . TYR A 1 3183 ? 218.562 184.293 263.005 1.00 19.06  ? 3183 TYR A CD1   1 
ATOM   13082 C  CD2   . TYR A 1 3183 ? 219.849 186.237 263.471 1.00 20.71  ? 3183 TYR A CD2   1 
ATOM   13083 C  CE1   . TYR A 1 3183 ? 219.516 183.509 263.617 1.00 22.23  ? 3183 TYR A CE1   1 
ATOM   13084 C  CE2   . TYR A 1 3183 ? 220.807 185.461 264.084 1.00 23.09  ? 3183 TYR A CE2   1 
ATOM   13085 C  CZ    . TYR A 1 3183 ? 220.638 184.099 264.154 1.00 24.40  ? 3183 TYR A CZ    1 
ATOM   13086 O  OH    . TYR A 1 3183 ? 221.594 183.324 264.766 1.00 30.36  ? 3183 TYR A OH    1 
ATOM   13087 N  N     . ALA A 1 3184 ? 214.986 186.370 263.804 1.00 18.09  ? 3184 ALA A N     1 
ATOM   13088 C  CA    . ALA A 1 3184 ? 214.234 186.051 265.014 1.00 20.25  ? 3184 ALA A CA    1 
ATOM   13089 C  C     . ALA A 1 3184 ? 213.058 185.132 264.704 1.00 20.98  ? 3184 ALA A C     1 
ATOM   13090 O  O     . ALA A 1 3184 ? 212.839 184.123 265.393 1.00 28.73  ? 3184 ALA A O     1 
ATOM   13091 C  CB    . ALA A 1 3184 ? 213.754 187.336 265.686 1.00 23.04  ? 3184 ALA A CB    1 
ATOM   13092 N  N     . ASN A 1 3185 ? 212.296 185.458 263.655 1.00 21.45  ? 3185 ASN A N     1 
ATOM   13093 C  CA    . ASN A 1 3185 ? 211.123 184.660 263.313 1.00 19.17  ? 3185 ASN A CA    1 
ATOM   13094 C  C     . ASN A 1 3185 ? 211.515 183.237 262.937 1.00 23.47  ? 3185 ASN A C     1 
ATOM   13095 O  O     . ASN A 1 3185 ? 210.902 182.268 263.402 1.00 28.47  ? 3185 ASN A O     1 
ATOM   13096 C  CB    . ASN A 1 3185 ? 210.354 185.324 262.172 1.00 14.57  ? 3185 ASN A CB    1 
ATOM   13097 C  CG    . ASN A 1 3185 ? 209.807 186.681 262.551 1.00 18.71  ? 3185 ASN A CG    1 
ATOM   13098 O  OD1   . ASN A 1 3185 ? 209.805 187.059 263.722 1.00 25.15  ? 3185 ASN A OD1   1 
ATOM   13099 N  ND2   . ASN A 1 3185 ? 209.339 187.427 261.558 1.00 19.42  ? 3185 ASN A ND2   1 
ATOM   13100 N  N     . LEU A 1 3186 ? 212.537 183.092 262.091 1.00 23.11  ? 3186 LEU A N     1 
ATOM   13101 C  CA    . LEU A 1 3186 ? 212.970 181.770 261.659 1.00 25.67  ? 3186 LEU A CA    1 
ATOM   13102 C  C     . LEU A 1 3186 ? 213.522 180.964 262.823 1.00 27.37  ? 3186 LEU A C     1 
ATOM   13103 O  O     . LEU A 1 3186 ? 213.250 179.764 262.933 1.00 32.09  ? 3186 LEU A O     1 
ATOM   13104 C  CB    . LEU A 1 3186 ? 214.011 181.895 260.550 1.00 19.03  ? 3186 LEU A CB    1 
ATOM   13105 C  CG    . LEU A 1 3186 ? 213.456 182.133 259.146 1.00 19.40  ? 3186 LEU A CG    1 
ATOM   13106 C  CD1   . LEU A 1 3186 ? 214.584 182.401 258.167 1.00 21.21  ? 3186 LEU A CD1   1 
ATOM   13107 C  CD2   . LEU A 1 3186 ? 212.615 180.952 258.697 1.00 24.94  ? 3186 LEU A CD2   1 
ATOM   13108 N  N     . PHE A 1 3187 ? 214.301 181.600 263.700 1.00 26.62  ? 3187 PHE A N     1 
ATOM   13109 C  CA    . PHE A 1 3187 ? 214.818 180.906 264.873 1.00 27.45  ? 3187 PHE A CA    1 
ATOM   13110 C  C     . PHE A 1 3187 ? 213.680 180.360 265.722 1.00 29.23  ? 3187 PHE A C     1 
ATOM   13111 O  O     . PHE A 1 3187 ? 213.671 179.176 266.081 1.00 35.37  ? 3187 PHE A O     1 
ATOM   13112 C  CB    . PHE A 1 3187 ? 215.694 181.857 265.688 1.00 30.04  ? 3187 PHE A CB    1 
ATOM   13113 C  CG    . PHE A 1 3187 ? 216.637 181.165 266.628 1.00 31.05  ? 3187 PHE A CG    1 
ATOM   13114 C  CD1   . PHE A 1 3187 ? 217.864 180.702 266.184 1.00 31.54  ? 3187 PHE A CD1   1 
ATOM   13115 C  CD2   . PHE A 1 3187 ? 216.303 180.990 267.958 1.00 28.77  ? 3187 PHE A CD2   1 
ATOM   13116 C  CE1   . PHE A 1 3187 ? 218.734 180.071 267.049 1.00 31.38  ? 3187 PHE A CE1   1 
ATOM   13117 C  CE2   . PHE A 1 3187 ? 217.168 180.360 268.827 1.00 33.86  ? 3187 PHE A CE2   1 
ATOM   13118 C  CZ    . PHE A 1 3187 ? 218.385 179.900 268.372 1.00 36.32  ? 3187 PHE A CZ    1 
ATOM   13119 N  N     . HIS A 1 3188 ? 212.697 181.209 266.037 1.00 30.71  ? 3188 HIS A N     1 
ATOM   13120 C  CA    . HIS A 1 3188 ? 211.587 180.761 266.872 1.00 37.15  ? 3188 HIS A CA    1 
ATOM   13121 C  C     . HIS A 1 3188 ? 210.801 179.642 266.198 1.00 39.03  ? 3188 HIS A C     1 
ATOM   13122 O  O     . HIS A 1 3188 ? 210.469 178.633 266.835 1.00 43.23  ? 3188 HIS A O     1 
ATOM   13123 C  CB    . HIS A 1 3188 ? 210.671 181.937 267.204 1.00 35.68  ? 3188 HIS A CB    1 
ATOM   13124 C  CG    . HIS A 1 3188 ? 209.650 181.627 268.253 1.00 56.35  ? 3188 HIS A CG    1 
ATOM   13125 N  ND1   . HIS A 1 3188 ? 209.930 181.677 269.602 1.00 61.39  ? 3188 HIS A ND1   1 
ATOM   13126 C  CD2   . HIS A 1 3188 ? 208.350 181.260 268.153 1.00 60.66  ? 3188 HIS A CD2   1 
ATOM   13127 C  CE1   . HIS A 1 3188 ? 208.848 181.355 270.287 1.00 63.68  ? 3188 HIS A CE1   1 
ATOM   13128 N  NE2   . HIS A 1 3188 ? 207.875 181.097 269.432 1.00 66.85  ? 3188 HIS A NE2   1 
ATOM   13129 N  N     . GLU A 1 3189 ? 210.510 179.795 264.903 1.00 38.31  ? 3189 GLU A N     1 
ATOM   13130 C  CA    . GLU A 1 3189 ? 209.723 178.793 264.190 1.00 36.88  ? 3189 GLU A CA    1 
ATOM   13131 C  C     . GLU A 1 3189 ? 210.448 177.452 264.139 1.00 39.45  ? 3189 GLU A C     1 
ATOM   13132 O  O     . GLU A 1 3189 ? 209.846 176.397 264.380 1.00 44.19  ? 3189 GLU A O     1 
ATOM   13133 C  CB    . GLU A 1 3189 ? 209.408 179.296 262.781 1.00 32.08  ? 3189 GLU A CB    1 
ATOM   13134 C  CG    . GLU A 1 3189 ? 209.014 178.211 261.796 1.00 44.83  ? 3189 GLU A CG    1 
ATOM   13135 C  CD    . GLU A 1 3189 ? 209.066 178.682 260.356 1.00 47.05  ? 3189 GLU A CD    1 
ATOM   13136 O  OE1   . GLU A 1 3189 ? 208.352 179.650 260.018 1.00 41.19  ? 3189 GLU A OE1   1 
ATOM   13137 O  OE2   . GLU A 1 3189 ? 209.821 178.087 259.560 1.00 48.64  ? 3189 GLU A OE2   1 
ATOM   13138 N  N     . LYS A 1 3190 ? 211.749 177.473 263.833 1.00 36.85  ? 3190 LYS A N     1 
ATOM   13139 C  CA    . LYS A 1 3190 ? 212.508 176.233 263.740 1.00 35.16  ? 3190 LYS A CA    1 
ATOM   13140 C  C     . LYS A 1 3190 ? 212.616 175.552 265.096 1.00 39.96  ? 3190 LYS A C     1 
ATOM   13141 O  O     . LYS A 1 3190 ? 212.412 174.334 265.200 1.00 52.83  ? 3190 LYS A O     1 
ATOM   13142 C  CB    . LYS A 1 3190 ? 213.897 176.512 263.164 1.00 35.85  ? 3190 LYS A CB    1 
ATOM   13143 C  CG    . LYS A 1 3190 ? 213.884 176.969 261.715 1.00 36.53  ? 3190 LYS A CG    1 
ATOM   13144 C  CD    . LYS A 1 3190 ? 213.242 175.944 260.808 1.00 36.12  ? 3190 LYS A CD    1 
ATOM   13145 C  CE    . LYS A 1 3190 ? 213.250 176.397 259.357 1.00 35.11  ? 3190 LYS A CE    1 
ATOM   13146 N  NZ    . LYS A 1 3190 ? 212.808 175.315 258.438 1.00 31.53  ? 3190 LYS A NZ    1 
ATOM   13147 N  N     . ARG A 1 3191 ? 212.922 176.319 266.148 1.00 41.32  ? 3191 ARG A N     1 
ATOM   13148 C  CA    . ARG A 1 3191 ? 212.964 175.748 267.490 1.00 46.60  ? 3191 ARG A CA    1 
ATOM   13149 C  C     . ARG A 1 3191 ? 211.638 175.091 267.846 1.00 47.51  ? 3191 ARG A C     1 
ATOM   13150 O  O     . ARG A 1 3191 ? 211.607 173.939 268.296 1.00 54.49  ? 3191 ARG A O     1 
ATOM   13151 C  CB    . ARG A 1 3191 ? 213.316 176.824 268.519 1.00 49.18  ? 3191 ARG A CB    1 
ATOM   13152 C  CG    . ARG A 1 3191 ? 214.705 177.418 268.385 1.00 41.01  ? 3191 ARG A CG    1 
ATOM   13153 C  CD    . ARG A 1 3191 ? 215.770 176.401 268.746 1.00 46.95  ? 3191 ARG A CD    1 
ATOM   13154 N  NE    . ARG A 1 3191 ? 215.634 175.948 270.126 1.00 50.49  ? 3191 ARG A NE    1 
ATOM   13155 C  CZ    . ARG A 1 3191 ? 216.161 176.569 271.173 1.00 48.87  ? 3191 ARG A CZ    1 
ATOM   13156 N  NH1   . ARG A 1 3191 ? 216.866 177.679 271.036 1.00 49.81  ? 3191 ARG A NH1   1 
ATOM   13157 N  NH2   . ARG A 1 3191 ? 215.973 176.062 272.388 1.00 42.12  ? 3191 ARG A NH2   1 
ATOM   13158 N  N     . SER A 1 3192 ? 210.529 175.801 267.631 1.00 43.59  ? 3192 SER A N     1 
ATOM   13159 C  CA    . SER A 1 3192 ? 209.225 175.268 268.010 1.00 48.64  ? 3192 SER A CA    1 
ATOM   13160 C  C     . SER A 1 3192 ? 208.905 173.989 267.244 1.00 51.05  ? 3192 SER A C     1 
ATOM   13161 O  O     . SER A 1 3192 ? 208.523 172.970 267.841 1.00 60.10  ? 3192 SER A O     1 
ATOM   13162 C  CB    . SER A 1 3192 ? 208.144 176.321 267.776 1.00 51.58  ? 3192 SER A CB    1 
ATOM   13163 O  OG    . SER A 1 3192 ? 208.355 177.462 268.589 1.00 54.99  ? 3192 SER A OG    1 
ATOM   13164 N  N     . GLU A 1 3193 ? 209.058 174.020 265.916 1.00 48.46  ? 3193 GLU A N     1 
ATOM   13165 C  CA    . GLU A 1 3193 ? 208.657 172.863 265.126 1.00 53.10  ? 3193 GLU A CA    1 
ATOM   13166 C  C     . GLU A 1 3193 ? 209.537 171.658 265.430 1.00 56.39  ? 3193 GLU A C     1 
ATOM   13167 O  O     . GLU A 1 3193 ? 209.041 170.529 265.521 1.00 62.53  ? 3193 GLU A O     1 
ATOM   13168 C  CB    . GLU A 1 3193 ? 208.678 173.179 263.629 1.00 50.11  ? 3193 GLU A CB    1 
ATOM   13169 C  CG    . GLU A 1 3193 ? 210.044 173.417 263.017 1.00 48.36  ? 3193 GLU A CG    1 
ATOM   13170 C  CD    . GLU A 1 3193 ? 209.954 173.743 261.541 1.00 55.32  ? 3193 GLU A CD    1 
ATOM   13171 O  OE1   . GLU A 1 3193 ? 208.825 173.828 261.016 1.00 61.15  ? 3193 GLU A OE1   1 
ATOM   13172 O  OE2   . GLU A 1 3193 ? 211.011 173.875 260.894 1.00 50.23  ? 3193 GLU A OE2   1 
ATOM   13173 N  N     . LEU A 1 3194 ? 210.843 171.872 265.621 1.00 50.89  ? 3194 LEU A N     1 
ATOM   13174 C  CA    . LEU A 1 3194 ? 211.709 170.721 265.836 1.00 56.07  ? 3194 LEU A CA    1 
ATOM   13175 C  C     . LEU A 1 3194 ? 211.544 170.183 267.252 1.00 58.72  ? 3194 LEU A C     1 
ATOM   13176 O  O     . LEU A 1 3194 ? 211.692 168.979 267.482 1.00 70.61  ? 3194 LEU A O     1 
ATOM   13177 C  CB    . LEU A 1 3194 ? 213.163 171.092 265.541 1.00 57.11  ? 3194 LEU A CB    1 
ATOM   13178 C  CG    . LEU A 1 3194 ? 214.172 169.942 265.416 1.00 61.21  ? 3194 LEU A CG    1 
ATOM   13179 C  CD1   . LEU A 1 3194 ? 215.321 170.377 264.521 1.00 67.38  ? 3194 LEU A CD1   1 
ATOM   13180 C  CD2   . LEU A 1 3194 ? 214.696 169.423 266.736 1.00 61.31  ? 3194 LEU A CD2   1 
ATOM   13181 N  N     . GLU A 1 3195 ? 211.215 171.051 268.215 1.00 56.55  ? 3195 GLU A N     1 
ATOM   13182 C  CA    . GLU A 1 3195 ? 210.885 170.568 269.550 1.00 63.21  ? 3195 GLU A CA    1 
ATOM   13183 C  C     . GLU A 1 3195 ? 209.629 169.704 269.525 1.00 66.91  ? 3195 GLU A C     1 
ATOM   13184 O  O     . GLU A 1 3195 ? 209.584 168.642 270.160 1.00 67.82  ? 3195 GLU A O     1 
ATOM   13185 C  CB    . GLU A 1 3195 ? 210.703 171.748 270.505 1.00 65.57  ? 3195 GLU A CB    1 
ATOM   13186 C  CG    . GLU A 1 3195 ? 212.004 172.313 271.051 1.00 70.09  ? 3195 GLU A CG    1 
ATOM   13187 C  CD    . GLU A 1 3195 ? 211.801 173.618 271.796 1.00 73.75  ? 3195 GLU A CD    1 
ATOM   13188 O  OE1   . GLU A 1 3195 ? 210.634 173.990 272.039 1.00 80.47  ? 3195 GLU A OE1   1 
ATOM   13189 O  OE2   . GLU A 1 3195 ? 212.808 174.273 272.137 1.00 70.27  ? 3195 GLU A OE2   1 
ATOM   13190 N  N     . GLU A 1 3196 ? 208.602 170.138 268.787 1.00 66.45  ? 3196 GLU A N     1 
ATOM   13191 C  CA    . GLU A 1 3196 ? 207.403 169.313 268.650 1.00 67.62  ? 3196 GLU A CA    1 
ATOM   13192 C  C     . GLU A 1 3196 ? 207.728 167.988 267.970 1.00 67.79  ? 3196 GLU A C     1 
ATOM   13193 O  O     . GLU A 1 3196 ? 207.229 166.927 268.373 1.00 73.00  ? 3196 GLU A O     1 
ATOM   13194 C  CB    . GLU A 1 3196 ? 206.328 170.069 267.869 1.00 68.44  ? 3196 GLU A CB    1 
ATOM   13195 C  CG    . GLU A 1 3196 ? 205.787 171.300 268.580 1.00 73.76  ? 3196 GLU A CG    1 
ATOM   13196 C  CD    . GLU A 1 3196 ? 205.013 170.956 269.837 1.00 86.00  ? 3196 GLU A CD    1 
ATOM   13197 O  OE1   . GLU A 1 3196 ? 204.383 169.878 269.877 1.00 87.06  ? 3196 GLU A OE1   1 
ATOM   13198 O  OE2   . GLU A 1 3196 ? 205.033 171.765 270.789 1.00 86.03  ? 3196 GLU A OE2   1 
ATOM   13199 N  N     . GLN A 1 3197 ? 208.570 168.034 266.935 1.00 68.40  ? 3197 GLN A N     1 
ATOM   13200 C  CA    . GLN A 1 3197 ? 208.995 166.814 266.258 1.00 65.57  ? 3197 GLN A CA    1 
ATOM   13201 C  C     . GLN A 1 3197 ? 209.677 165.855 267.225 1.00 69.55  ? 3197 GLN A C     1 
ATOM   13202 O  O     . GLN A 1 3197 ? 209.319 164.673 267.291 1.00 81.56  ? 3197 GLN A O     1 
ATOM   13203 C  CB    . GLN A 1 3197 ? 209.932 167.164 265.103 1.00 67.00  ? 3197 GLN A CB    1 
ATOM   13204 C  CG    . GLN A 1 3197 ? 210.436 165.968 264.317 1.00 74.22  ? 3197 GLN A CG    1 
ATOM   13205 C  CD    . GLN A 1 3197 ? 211.352 166.365 263.179 1.00 70.66  ? 3197 GLN A CD    1 
ATOM   13206 O  OE1   . GLN A 1 3197 ? 211.615 167.548 262.962 1.00 71.86  ? 3197 GLN A OE1   1 
ATOM   13207 N  NE2   . GLN A 1 3197 ? 211.846 165.377 262.444 1.00 63.00  ? 3197 GLN A NE2   1 
ATOM   13208 N  N     . GLN A 1 3198 ? 210.649 166.348 267.992 1.00 66.58  ? 3198 GLN A N     1 
ATOM   13209 C  CA    . GLN A 1 3198 ? 211.360 165.489 268.932 1.00 71.25  ? 3198 GLN A CA    1 
ATOM   13210 C  C     . GLN A 1 3198 ? 210.420 164.928 269.991 1.00 72.46  ? 3198 GLN A C     1 
ATOM   13211 O  O     . GLN A 1 3198 ? 210.561 163.771 270.394 1.00 75.99  ? 3198 GLN A O     1 
ATOM   13212 C  CB    . GLN A 1 3198 ? 212.516 166.248 269.582 1.00 71.38  ? 3198 GLN A CB    1 
ATOM   13213 C  CG    . GLN A 1 3198 ? 213.331 165.399 270.545 1.00 72.36  ? 3198 GLN A CG    1 
ATOM   13214 C  CD    . GLN A 1 3198 ? 214.526 164.731 269.893 1.00 71.60  ? 3198 GLN A CD    1 
ATOM   13215 O  OE1   . GLN A 1 3198 ? 214.581 164.581 268.674 1.00 74.51  ? 3198 GLN A OE1   1 
ATOM   13216 N  NE2   . GLN A 1 3198 ? 215.481 164.306 270.709 1.00 62.75  ? 3198 GLN A NE2   1 
ATOM   13217 N  N     . MET A 1 3199 ? 209.456 165.729 270.451 1.00 75.12  ? 3199 MET A N     1 
ATOM   13218 C  CA    . MET A 1 3199 ? 208.471 165.214 271.399 1.00 75.62  ? 3199 MET A CA    1 
ATOM   13219 C  C     . MET A 1 3199 ? 207.698 164.047 270.798 1.00 82.29  ? 3199 MET A C     1 
ATOM   13220 O  O     . MET A 1 3199 ? 207.499 163.009 271.449 1.00 86.24  ? 3199 MET A O     1 
ATOM   13221 C  CB    . MET A 1 3199 ? 207.517 166.330 271.822 1.00 71.53  ? 3199 MET A CB    1 
ATOM   13222 C  CG    . MET A 1 3199 ? 206.501 165.911 272.870 1.00 78.86  ? 3199 MET A CG    1 
ATOM   13223 S  SD    . MET A 1 3199 ? 205.453 167.274 273.414 1.00 110.59 ? 3199 MET A SD    1 
ATOM   13224 C  CE    . MET A 1 3199 ? 204.342 166.419 274.528 1.00 79.91  ? 3199 MET A CE    1 
ATOM   13225 N  N     . HIS A 1 3200 ? 207.263 164.196 269.543 1.00 76.23  ? 3200 HIS A N     1 
ATOM   13226 C  CA    . HIS A 1 3200 ? 206.524 163.121 268.886 1.00 74.51  ? 3200 HIS A CA    1 
ATOM   13227 C  C     . HIS A 1 3200 ? 207.379 161.866 268.745 1.00 75.00  ? 3200 HIS A C     1 
ATOM   13228 O  O     . HIS A 1 3200 ? 206.911 160.753 269.016 1.00 79.91  ? 3200 HIS A O     1 
ATOM   13229 C  CB    . HIS A 1 3200 ? 206.020 163.587 267.522 1.00 68.39  ? 3200 HIS A CB    1 
ATOM   13230 C  CG    . HIS A 1 3200 ? 204.982 164.662 267.598 1.00 66.81  ? 3200 HIS A CG    1 
ATOM   13231 N  ND1   . HIS A 1 3200 ? 204.411 165.061 268.787 1.00 72.48  ? 3200 HIS A ND1   1 
ATOM   13232 C  CD2   . HIS A 1 3200 ? 204.415 165.424 266.634 1.00 65.27  ? 3200 HIS A CD2   1 
ATOM   13233 C  CE1   . HIS A 1 3200 ? 203.534 166.020 268.552 1.00 71.81  ? 3200 HIS A CE1   1 
ATOM   13234 N  NE2   . HIS A 1 3200 ? 203.518 166.260 267.252 1.00 71.59  ? 3200 HIS A NE2   1 
ATOM   13235 N  N     . LEU A 1 3201 ? 208.636 162.024 268.327 1.00 72.78  ? 3201 LEU A N     1 
ATOM   13236 C  CA    . LEU A 1 3201 ? 209.514 160.861 268.199 1.00 77.29  ? 3201 LEU A CA    1 
ATOM   13237 C  C     . LEU A 1 3201 ? 209.770 160.182 269.540 1.00 81.10  ? 3201 LEU A C     1 
ATOM   13238 O  O     . LEU A 1 3201 ? 209.762 158.949 269.620 1.00 86.10  ? 3201 LEU A O     1 
ATOM   13239 C  CB    . LEU A 1 3201 ? 210.831 161.238 267.523 1.00 75.86  ? 3201 LEU A CB    1 
ATOM   13240 C  CG    . LEU A 1 3201 ? 210.855 161.368 265.994 1.00 79.95  ? 3201 LEU A CG    1 
ATOM   13241 C  CD1   . LEU A 1 3201 ? 210.130 162.564 265.436 1.00 71.28  ? 3201 LEU A CD1   1 
ATOM   13242 C  CD2   . LEU A 1 3201 ? 212.300 161.402 265.556 1.00 81.31  ? 3201 LEU A CD2   1 
ATOM   13243 N  N     . ASN A 1 3202 ? 210.007 160.955 270.603 1.00 80.65  ? 3202 ASN A N     1 
ATOM   13244 C  CA    . ASN A 1 3202 ? 210.241 160.331 271.903 1.00 84.43  ? 3202 ASN A CA    1 
ATOM   13245 C  C     . ASN A 1 3202 ? 209.013 159.573 272.389 1.00 86.21  ? 3202 ASN A C     1 
ATOM   13246 O  O     . ASN A 1 3202 ? 209.134 158.445 272.886 1.00 91.80  ? 3202 ASN A O     1 
ATOM   13247 C  CB    . ASN A 1 3202 ? 210.680 161.361 272.946 1.00 86.40  ? 3202 ASN A CB    1 
ATOM   13248 C  CG    . ASN A 1 3202 ? 212.037 161.961 272.642 1.00 84.46  ? 3202 ASN A CG    1 
ATOM   13249 O  OD1   . ASN A 1 3202 ? 212.162 163.156 272.390 1.00 82.82  ? 3202 ASN A OD1   1 
ATOM   13250 N  ND2   . ASN A 1 3202 ? 213.068 161.125 272.667 1.00 80.87  ? 3202 ASN A ND2   1 
ATOM   13251 N  N     . VAL A 1 3203 ? 207.820 160.157 272.249 1.00 83.18  ? 3203 VAL A N     1 
ATOM   13252 C  CA    . VAL A 1 3203 ? 206.627 159.464 272.731 1.00 83.04  ? 3203 VAL A CA    1 
ATOM   13253 C  C     . VAL A 1 3203 ? 206.359 158.218 271.891 1.00 86.14  ? 3203 VAL A C     1 
ATOM   13254 O  O     . VAL A 1 3203 ? 205.966 157.168 272.416 1.00 93.59  ? 3203 VAL A O     1 
ATOM   13255 C  CB    . VAL A 1 3203 ? 205.415 160.417 272.779 1.00 77.77  ? 3203 VAL A CB    1 
ATOM   13256 C  CG1   . VAL A 1 3203 ? 204.984 160.856 271.396 1.00 78.60  ? 3203 VAL A CG1   1 
ATOM   13257 C  CG2   . VAL A 1 3203 ? 204.255 159.759 273.512 1.00 76.89  ? 3203 VAL A CG2   1 
ATOM   13258 N  N     . GLY A 1 3204 ? 206.609 158.296 270.579 1.00 87.28  ? 3204 GLY A N     1 
ATOM   13259 C  CA    . GLY A 1 3204 ? 206.428 157.124 269.735 1.00 92.56  ? 3204 GLY A CA    1 
ATOM   13260 C  C     . GLY A 1 3204 ? 207.399 156.006 270.063 1.00 93.15  ? 3204 GLY A C     1 
ATOM   13261 O  O     . GLY A 1 3204 ? 207.014 154.833 270.127 1.00 98.78  ? 3204 GLY A O     1 
ATOM   13262 N  N     . LEU A 1 3205 ? 208.674 156.350 270.270 1.00 85.65  ? 3205 LEU A N     1 
ATOM   13263 C  CA    . LEU A 1 3205 ? 209.657 155.338 270.642 1.00 89.93  ? 3205 LEU A CA    1 
ATOM   13264 C  C     . LEU A 1 3205 ? 209.323 154.724 271.995 1.00 94.86  ? 3205 LEU A C     1 
ATOM   13265 O  O     . LEU A 1 3205 ? 209.492 153.517 272.192 1.00 95.84  ? 3205 LEU A O     1 
ATOM   13266 C  CB    . LEU A 1 3205 ? 211.063 155.941 270.658 1.00 88.60  ? 3205 LEU A CB    1 
ATOM   13267 C  CG    . LEU A 1 3205 ? 211.649 156.408 269.323 1.00 84.34  ? 3205 LEU A CG    1 
ATOM   13268 C  CD1   . LEU A 1 3205 ? 212.983 157.106 269.538 1.00 80.49  ? 3205 LEU A CD1   1 
ATOM   13269 C  CD2   . LEU A 1 3205 ? 211.796 155.254 268.347 1.00 87.52  ? 3205 LEU A CD2   1 
ATOM   13270 N  N     . ARG A 1 3206 ? 208.848 155.540 272.940 1.00 98.81  ? 3206 ARG A N     1 
ATOM   13271 C  CA    . ARG A 1 3206 ? 208.441 155.007 274.235 1.00 99.81  ? 3206 ARG A CA    1 
ATOM   13272 C  C     . ARG A 1 3206 ? 207.282 154.028 274.087 1.00 102.89 ? 3206 ARG A C     1 
ATOM   13273 O  O     . ARG A 1 3206 ? 207.278 152.959 274.710 1.00 107.83 ? 3206 ARG A O     1 
ATOM   13274 C  CB    . ARG A 1 3206 ? 208.066 156.155 275.174 1.00 98.69  ? 3206 ARG A CB    1 
ATOM   13275 C  CG    . ARG A 1 3206 ? 207.064 155.789 276.256 1.00 98.44  ? 3206 ARG A CG    1 
ATOM   13276 C  CD    . ARG A 1 3206 ? 207.063 156.827 277.364 1.00 90.64  ? 3206 ARG A CD    1 
ATOM   13277 N  NE    . ARG A 1 3206 ? 206.424 158.067 276.940 1.00 90.83  ? 3206 ARG A NE    1 
ATOM   13278 C  CZ    . ARG A 1 3206 ? 207.066 159.209 276.734 1.00 88.73  ? 3206 ARG A CZ    1 
ATOM   13279 N  NH1   . ARG A 1 3206 ? 208.375 159.305 276.897 1.00 87.64  ? 3206 ARG A NH1   1 
ATOM   13280 N  NH2   . ARG A 1 3206 ? 206.378 160.280 276.352 1.00 85.14  ? 3206 ARG A NH2   1 
ATOM   13281 N  N     . LYS A 1 3207 ? 206.295 154.372 273.254 1.00 100.19 ? 3207 LYS A N     1 
ATOM   13282 C  CA    . LYS A 1 3207 ? 205.165 153.472 273.044 1.00 101.06 ? 3207 LYS A CA    1 
ATOM   13283 C  C     . LYS A 1 3207 ? 205.608 152.162 272.404 1.00 102.58 ? 3207 LYS A C     1 
ATOM   13284 O  O     . LYS A 1 3207 ? 205.158 151.081 272.805 1.00 105.96 ? 3207 LYS A O     1 
ATOM   13285 C  CB    . LYS A 1 3207 ? 204.100 154.157 272.189 1.00 97.79  ? 3207 LYS A CB    1 
ATOM   13286 C  CG    . LYS A 1 3207 ? 203.442 155.350 272.865 1.00 97.70  ? 3207 LYS A CG    1 
ATOM   13287 C  CD    . LYS A 1 3207 ? 202.315 154.917 273.782 1.00 94.21  ? 3207 LYS A CD    1 
ATOM   13288 C  CE    . LYS A 1 3207 ? 201.593 156.116 274.373 1.00 95.92  ? 3207 LYS A CE    1 
ATOM   13289 N  NZ    . LYS A 1 3207 ? 200.898 156.923 273.332 1.00 99.67  ? 3207 LYS A NZ    1 
ATOM   13290 N  N     . ILE A 1 3208 ? 206.497 152.233 271.410 1.00 102.98 ? 3208 ILE A N     1 
ATOM   13291 C  CA    . ILE A 1 3208 ? 206.935 151.012 270.737 1.00 103.33 ? 3208 ILE A CA    1 
ATOM   13292 C  C     . ILE A 1 3208 ? 207.791 150.157 271.672 1.00 108.47 ? 3208 ILE A C     1 
ATOM   13293 O  O     . ILE A 1 3208 ? 207.724 148.922 271.640 1.00 112.91 ? 3208 ILE A O     1 
ATOM   13294 C  CB    . ILE A 1 3208 ? 207.669 151.352 269.426 1.00 99.76  ? 3208 ILE A CB    1 
ATOM   13295 C  CG1   . ILE A 1 3208 ? 206.731 152.103 268.480 1.00 98.99  ? 3208 ILE A CG1   1 
ATOM   13296 C  CG2   . ILE A 1 3208 ? 208.136 150.083 268.734 1.00 99.80  ? 3208 ILE A CG2   1 
ATOM   13297 C  CD1   . ILE A 1 3208 ? 207.294 152.306 267.092 1.00 93.03  ? 3208 ILE A CD1   1 
ATOM   13298 N  N     . LYS A 1 3209 ? 208.604 150.793 272.520 1.00 106.96 ? 3209 LYS A N     1 
ATOM   13299 C  CA    . LYS A 1 3209 ? 209.378 150.044 273.509 1.00 105.14 ? 3209 LYS A CA    1 
ATOM   13300 C  C     . LYS A 1 3209 ? 208.464 149.355 274.515 1.00 109.25 ? 3209 LYS A C     1 
ATOM   13301 O  O     . LYS A 1 3209 ? 208.709 148.204 274.910 1.00 109.13 ? 3209 LYS A O     1 
ATOM   13302 C  CB    . LYS A 1 3209 ? 210.355 150.977 274.223 1.00 102.62 ? 3209 LYS A CB    1 
ATOM   13303 C  CG    . LYS A 1 3209 ? 211.488 150.269 274.944 1.00 98.18  ? 3209 LYS A CG    1 
ATOM   13304 C  CD    . LYS A 1 3209 ? 212.720 150.162 274.061 1.00 94.43  ? 3209 LYS A CD    1 
ATOM   13305 C  CE    . LYS A 1 3209 ? 213.973 149.934 274.890 1.00 84.49  ? 3209 LYS A CE    1 
ATOM   13306 N  NZ    . LYS A 1 3209 ? 215.023 149.213 274.121 1.00 74.17  ? 3209 LYS A NZ    1 
ATOM   13307 N  N     . GLU A 1 3210 ? 207.410 150.049 274.950 1.00 109.34 ? 3210 GLU A N     1 
ATOM   13308 C  CA    . GLU A 1 3210 ? 206.417 149.419 275.813 1.00 111.10 ? 3210 GLU A CA    1 
ATOM   13309 C  C     . GLU A 1 3210 ? 205.774 148.227 275.119 1.00 116.00 ? 3210 GLU A C     1 
ATOM   13310 O  O     . GLU A 1 3210 ? 205.547 147.184 275.741 1.00 117.08 ? 3210 GLU A O     1 
ATOM   13311 C  CB    . GLU A 1 3210 ? 205.356 150.441 276.224 1.00 106.35 ? 3210 GLU A CB    1 
ATOM   13312 C  CG    . GLU A 1 3210 ? 204.700 150.156 277.564 1.00 110.83 ? 3210 GLU A CG    1 
ATOM   13313 C  CD    . GLU A 1 3210 ? 203.988 151.369 278.133 1.00 118.70 ? 3210 GLU A CD    1 
ATOM   13314 O  OE1   . GLU A 1 3210 ? 203.807 152.357 277.390 1.00 113.15 ? 3210 GLU A OE1   1 
ATOM   13315 O  OE2   . GLU A 1 3210 ? 203.608 151.334 279.321 1.00 119.93 ? 3210 GLU A OE2   1 
ATOM   13316 N  N     . THR A 1 3211 ? 205.480 148.364 273.823 1.00 115.66 ? 3211 THR A N     1 
ATOM   13317 C  CA    . THR A 1 3211 ? 204.924 147.250 273.061 1.00 113.84 ? 3211 THR A CA    1 
ATOM   13318 C  C     . THR A 1 3211 ? 205.888 146.067 273.021 1.00 114.42 ? 3211 THR A C     1 
ATOM   13319 O  O     . THR A 1 3211 ? 205.469 144.911 273.143 1.00 118.20 ? 3211 THR A O     1 
ATOM   13320 C  CB    . THR A 1 3211 ? 204.577 147.709 271.644 1.00 110.31 ? 3211 THR A CB    1 
ATOM   13321 O  OG1   . THR A 1 3211 ? 203.602 148.758 271.705 1.00 107.60 ? 3211 THR A OG1   1 
ATOM   13322 C  CG2   . THR A 1 3211 ? 204.028 146.557 270.817 1.00 105.66 ? 3211 THR A CG2   1 
ATOM   13323 N  N     . VAL A 1 3212 ? 207.182 146.338 272.843 1.00 112.34 ? 3212 VAL A N     1 
ATOM   13324 C  CA    . VAL A 1 3212 ? 208.176 145.266 272.814 1.00 110.88 ? 3212 VAL A CA    1 
ATOM   13325 C  C     . VAL A 1 3212 ? 208.227 144.542 274.156 1.00 113.71 ? 3212 VAL A C     1 
ATOM   13326 O  O     . VAL A 1 3212 ? 208.258 143.304 274.215 1.00 112.82 ? 3212 VAL A O     1 
ATOM   13327 C  CB    . VAL A 1 3212 ? 209.553 145.829 272.419 1.00 102.23 ? 3212 VAL A CB    1 
ATOM   13328 C  CG1   . VAL A 1 3212 ? 210.661 144.863 272.816 1.00 93.23  ? 3212 VAL A CG1   1 
ATOM   13329 C  CG2   . VAL A 1 3212 ? 209.603 146.119 270.928 1.00 100.86 ? 3212 VAL A CG2   1 
ATOM   13330 N  N     . ASP A 1 3213 ? 208.235 145.298 275.256 1.00 117.84 ? 3213 ASP A N     1 
ATOM   13331 C  CA    . ASP A 1 3213 ? 208.209 144.666 276.573 1.00 118.75 ? 3213 ASP A CA    1 
ATOM   13332 C  C     . ASP A 1 3213 ? 206.940 143.845 276.766 1.00 118.80 ? 3213 ASP A C     1 
ATOM   13333 O  O     . ASP A 1 3213 ? 206.984 142.742 277.336 1.00 120.93 ? 3213 ASP A O     1 
ATOM   13334 C  CB    . ASP A 1 3213 ? 208.333 145.724 277.669 1.00 122.17 ? 3213 ASP A CB    1 
ATOM   13335 C  CG    . ASP A 1 3213 ? 209.775 146.053 278.001 1.00 124.61 ? 3213 ASP A CG    1 
ATOM   13336 O  OD1   . ASP A 1 3213 ? 210.627 145.144 277.918 1.00 120.66 ? 3213 ASP A OD1   1 
ATOM   13337 O  OD2   . ASP A 1 3213 ? 210.056 147.220 278.345 1.00 122.48 ? 3213 ASP A OD2   1 
ATOM   13338 N  N     . GLN A 1 3214 ? 205.805 144.365 276.294 1.00 119.17 ? 3214 GLN A N     1 
ATOM   13339 C  CA    . GLN A 1 3214 ? 204.546 143.638 276.394 1.00 119.85 ? 3214 GLN A CA    1 
ATOM   13340 C  C     . GLN A 1 3214 ? 204.609 142.319 275.639 1.00 119.71 ? 3214 GLN A C     1 
ATOM   13341 O  O     . GLN A 1 3214 ? 204.176 141.286 276.155 1.00 122.16 ? 3214 GLN A O     1 
ATOM   13342 C  CB    . GLN A 1 3214 ? 203.401 144.503 275.865 1.00 117.04 ? 3214 GLN A CB    1 
ATOM   13343 C  CG    . GLN A 1 3214 ? 202.992 145.633 276.795 1.00 115.05 ? 3214 GLN A CG    1 
ATOM   13344 C  CD    . GLN A 1 3214 ? 202.788 145.170 278.222 1.00 118.63 ? 3214 GLN A CD    1 
ATOM   13345 O  OE1   . GLN A 1 3214 ? 201.998 144.263 278.482 1.00 122.80 ? 3214 GLN A OE1   1 
ATOM   13346 N  NE2   . GLN A 1 3214 ? 203.505 145.786 279.154 1.00 109.95 ? 3214 GLN A NE2   1 
ATOM   13347 N  N     . VAL A 1 3215 ? 205.148 142.328 274.418 1.00 118.30 ? 3215 VAL A N     1 
ATOM   13348 C  CA    . VAL A 1 3215 ? 205.197 141.082 273.658 1.00 115.92 ? 3215 VAL A CA    1 
ATOM   13349 C  C     . VAL A 1 3215 ? 206.172 140.104 274.297 1.00 118.36 ? 3215 VAL A C     1 
ATOM   13350 O  O     . VAL A 1 3215 ? 205.952 138.889 274.256 1.00 116.09 ? 3215 VAL A O     1 
ATOM   13351 C  CB    . VAL A 1 3215 ? 205.534 141.331 272.173 1.00 112.86 ? 3215 VAL A CB    1 
ATOM   13352 C  CG1   . VAL A 1 3215 ? 204.616 142.385 271.587 1.00 110.22 ? 3215 VAL A CG1   1 
ATOM   13353 C  CG2   . VAL A 1 3215 ? 206.993 141.693 271.980 1.00 109.89 ? 3215 VAL A CG2   1 
ATOM   13354 N  N     . GLU A 1 3216 ? 207.252 140.601 274.909 1.00 120.32 ? 3216 GLU A N     1 
ATOM   13355 C  CA    . GLU A 1 3216 ? 208.165 139.703 275.614 1.00 120.49 ? 3216 GLU A CA    1 
ATOM   13356 C  C     . GLU A 1 3216 ? 207.460 139.012 276.779 1.00 123.85 ? 3216 GLU A C     1 
ATOM   13357 O  O     . GLU A 1 3216 ? 207.559 137.786 276.951 1.00 125.05 ? 3216 GLU A O     1 
ATOM   13358 C  CB    . GLU A 1 3216 ? 209.388 140.481 276.104 1.00 121.66 ? 3216 GLU A CB    1 
ATOM   13359 C  CG    . GLU A 1 3216 ? 210.528 139.608 276.612 1.00 121.85 ? 3216 GLU A CG    1 
ATOM   13360 C  CD    . GLU A 1 3216 ? 210.405 139.281 278.088 1.00 122.22 ? 3216 GLU A CD    1 
ATOM   13361 O  OE1   . GLU A 1 3216 ? 209.814 140.090 278.832 1.00 123.70 ? 3216 GLU A OE1   1 
ATOM   13362 O  OE2   . GLU A 1 3216 ? 210.899 138.211 278.504 1.00 112.47 ? 3216 GLU A OE2   1 
ATOM   13363 N  N     . GLU A 1 3217 ? 206.723 139.783 277.585 1.00 124.21 ? 3217 GLU A N     1 
ATOM   13364 C  CA    . GLU A 1 3217 ? 206.054 139.165 278.725 1.00 124.06 ? 3217 GLU A CA    1 
ATOM   13365 C  C     . GLU A 1 3217 ? 204.899 138.272 278.280 1.00 124.65 ? 3217 GLU A C     1 
ATOM   13366 O  O     . GLU A 1 3217 ? 204.605 137.272 278.942 1.00 124.30 ? 3217 GLU A O     1 
ATOM   13367 C  CB    . GLU A 1 3217 ? 205.573 140.222 279.722 1.00 121.26 ? 3217 GLU A CB    1 
ATOM   13368 C  CG    . GLU A 1 3217 ? 204.293 140.941 279.354 1.00 119.69 ? 3217 GLU A CG    1 
ATOM   13369 C  CD    . GLU A 1 3217 ? 203.892 141.956 280.402 1.00 118.34 ? 3217 GLU A CD    1 
ATOM   13370 O  OE1   . GLU A 1 3217 ? 204.711 142.236 281.303 1.00 118.56 ? 3217 GLU A OE1   1 
ATOM   13371 O  OE2   . GLU A 1 3217 ? 202.751 142.458 280.345 1.00 117.58 ? 3217 GLU A OE2   1 
ATOM   13372 N  N     . LEU A 1 3218 ? 204.256 138.589 277.152 1.00 124.94 ? 3218 LEU A N     1 
ATOM   13373 C  CA    . LEU A 1 3218 ? 203.231 137.696 276.617 1.00 123.53 ? 3218 LEU A CA    1 
ATOM   13374 C  C     . LEU A 1 3218 ? 203.834 136.413 276.056 1.00 123.39 ? 3218 LEU A C     1 
ATOM   13375 O  O     . LEU A 1 3218 ? 203.199 135.360 276.113 1.00 124.16 ? 3218 LEU A O     1 
ATOM   13376 C  CB    . LEU A 1 3218 ? 202.384 138.407 275.559 1.00 118.70 ? 3218 LEU A CB    1 
ATOM   13377 C  CG    . LEU A 1 3218 ? 201.150 139.199 276.014 1.00 112.63 ? 3218 LEU A CG    1 
ATOM   13378 C  CD1   . LEU A 1 3218 ? 200.129 138.242 276.604 1.00 104.09 ? 3218 LEU A CD1   1 
ATOM   13379 C  CD2   . LEU A 1 3218 ? 201.467 140.286 277.024 1.00 113.96 ? 3218 LEU A CD2   1 
ATOM   13380 N  N     . ARG A 1 3219 ? 205.050 136.472 275.508 1.00 122.47 ? 3219 ARG A N     1 
ATOM   13381 C  CA    . ARG A 1 3219 ? 205.721 135.237 275.106 1.00 122.60 ? 3219 ARG A CA    1 
ATOM   13382 C  C     . ARG A 1 3219 ? 206.040 134.370 276.319 1.00 123.12 ? 3219 ARG A C     1 
ATOM   13383 O  O     . ARG A 1 3219 ? 205.852 133.143 276.291 1.00 121.10 ? 3219 ARG A O     1 
ATOM   13384 C  CB    . ARG A 1 3219 ? 206.995 135.552 274.321 1.00 117.67 ? 3219 ARG A CB    1 
ATOM   13385 C  CG    . ARG A 1 3219 ? 206.786 135.679 272.822 1.00 114.20 ? 3219 ARG A CG    1 
ATOM   13386 C  CD    . ARG A 1 3219 ? 208.073 135.407 272.057 1.00 112.08 ? 3219 ARG A CD    1 
ATOM   13387 N  NE    . ARG A 1 3219 ? 209.211 136.136 272.602 1.00 115.13 ? 3219 ARG A NE    1 
ATOM   13388 C  CZ    . ARG A 1 3219 ? 209.833 137.128 271.979 1.00 110.60 ? 3219 ARG A CZ    1 
ATOM   13389 N  NH1   . ARG A 1 3219 ? 209.455 137.536 270.779 1.00 103.58 ? 3219 ARG A NH1   1 
ATOM   13390 N  NH2   . ARG A 1 3219 ? 210.863 137.725 272.574 1.00 108.16 ? 3219 ARG A NH2   1 
ATOM   13391 N  N     . ARG A 1 3220 ? 206.521 134.994 277.397 1.00 123.25 ? 3220 ARG A N     1 
ATOM   13392 C  CA    . ARG A 1 3220 ? 206.755 134.241 278.628 1.00 124.10 ? 3220 ARG A CA    1 
ATOM   13393 C  C     . ARG A 1 3220 ? 205.458 133.632 279.154 1.00 126.32 ? 3220 ARG A C     1 
ATOM   13394 O  O     . ARG A 1 3220 ? 205.426 132.464 279.567 1.00 128.31 ? 3220 ARG A O     1 
ATOM   13395 C  CB    . ARG A 1 3220 ? 207.399 135.144 279.681 1.00 122.98 ? 3220 ARG A CB    1 
ATOM   13396 C  CG    . ARG A 1 3220 ? 207.358 134.586 281.094 1.00 120.29 ? 3220 ARG A CG    1 
ATOM   13397 C  CD    . ARG A 1 3220 ? 207.262 135.700 282.122 1.00 118.64 ? 3220 ARG A CD    1 
ATOM   13398 N  NE    . ARG A 1 3220 ? 206.185 136.634 281.816 1.00 124.39 ? 3220 ARG A NE    1 
ATOM   13399 C  CZ    . ARG A 1 3220 ? 204.912 136.441 282.135 1.00 125.31 ? 3220 ARG A CZ    1 
ATOM   13400 N  NH1   . ARG A 1 3220 ? 204.518 135.353 282.775 1.00 124.22 ? 3220 ARG A NH1   1 
ATOM   13401 N  NH2   . ARG A 1 3220 ? 204.014 137.363 281.804 1.00 123.88 ? 3220 ARG A NH2   1 
ATOM   13402 N  N     . ASP A 1 3221 ? 204.370 134.407 279.126 1.00 125.59 ? 3221 ASP A N     1 
ATOM   13403 C  CA    . ASP A 1 3221 ? 203.074 133.893 279.551 1.00 126.13 ? 3221 ASP A CA    1 
ATOM   13404 C  C     . ASP A 1 3221 ? 202.584 132.774 278.641 1.00 128.37 ? 3221 ASP A C     1 
ATOM   13405 O  O     . ASP A 1 3221 ? 201.928 131.844 279.113 1.00 125.52 ? 3221 ASP A O     1 
ATOM   13406 C  CB    . ASP A 1 3221 ? 202.049 135.027 279.598 1.00 122.46 ? 3221 ASP A CB    1 
ATOM   13407 C  CG    . ASP A 1 3221 ? 200.747 134.609 280.257 1.00 124.13 ? 3221 ASP A CG    1 
ATOM   13408 O  OD1   . ASP A 1 3221 ? 199.859 134.091 279.548 1.00 128.46 ? 3221 ASP A OD1   1 
ATOM   13409 O  OD2   . ASP A 1 3221 ? 200.614 134.798 281.483 1.00 117.28 ? 3221 ASP A OD2   1 
ATOM   13410 N  N     . LEU A 1 3222 ? 202.877 132.851 277.342 1.00 129.58 ? 3222 LEU A N     1 
ATOM   13411 C  CA    . LEU A 1 3222 ? 202.511 131.777 276.425 1.00 126.79 ? 3222 LEU A CA    1 
ATOM   13412 C  C     . LEU A 1 3222 ? 203.242 130.489 276.772 1.00 129.61 ? 3222 LEU A C     1 
ATOM   13413 O  O     . LEU A 1 3222 ? 202.651 129.404 276.750 1.00 130.64 ? 3222 LEU A O     1 
ATOM   13414 C  CB    . LEU A 1 3222 ? 202.814 132.192 274.986 1.00 122.98 ? 3222 LEU A CB    1 
ATOM   13415 C  CG    . LEU A 1 3222 ? 202.572 131.144 273.898 1.00 117.70 ? 3222 LEU A CG    1 
ATOM   13416 C  CD1   . LEU A 1 3222 ? 201.087 130.881 273.719 1.00 118.23 ? 3222 LEU A CD1   1 
ATOM   13417 C  CD2   . LEU A 1 3222 ? 203.205 131.574 272.583 1.00 110.87 ? 3222 LEU A CD2   1 
ATOM   13418 N  N     . ARG A 1 3223 ? 204.534 130.590 277.096 1.00 129.21 ? 3223 ARG A N     1 
ATOM   13419 C  CA    . ARG A 1 3223 ? 205.265 129.404 277.536 1.00 126.53 ? 3223 ARG A CA    1 
ATOM   13420 C  C     . ARG A 1 3223 ? 204.673 128.843 278.826 1.00 127.34 ? 3223 ARG A C     1 
ATOM   13421 O  O     . ARG A 1 3223 ? 204.530 127.620 278.981 1.00 126.64 ? 3223 ARG A O     1 
ATOM   13422 C  CB    . ARG A 1 3223 ? 206.746 129.735 277.723 1.00 123.49 ? 3223 ARG A CB    1 
ATOM   13423 C  CG    . ARG A 1 3223 ? 207.602 128.539 278.109 1.00 122.09 ? 3223 ARG A CG    1 
ATOM   13424 C  CD    . ARG A 1 3223 ? 208.915 128.974 278.741 1.00 120.56 ? 3223 ARG A CD    1 
ATOM   13425 N  NE    . ARG A 1 3223 ? 208.741 130.112 279.635 1.00 126.37 ? 3223 ARG A NE    1 
ATOM   13426 C  CZ    . ARG A 1 3223 ? 208.337 130.019 280.894 1.00 125.14 ? 3223 ARG A CZ    1 
ATOM   13427 N  NH1   . ARG A 1 3223 ? 208.055 128.850 281.446 1.00 118.77 ? 3223 ARG A NH1   1 
ATOM   13428 N  NH2   . ARG A 1 3223 ? 208.214 131.128 281.620 1.00 123.28 ? 3223 ARG A NH2   1 
ATOM   13429 N  N     . ILE A 1 3224 ? 204.313 129.727 279.760 1.00 127.10 ? 3224 ILE A N     1 
ATOM   13430 C  CA    . ILE A 1 3224 ? 203.713 129.282 281.018 1.00 126.29 ? 3224 ILE A CA    1 
ATOM   13431 C  C     . ILE A 1 3224 ? 202.384 128.577 280.760 1.00 127.82 ? 3224 ILE A C     1 
ATOM   13432 O  O     . ILE A 1 3224 ? 202.094 127.530 281.355 1.00 127.08 ? 3224 ILE A O     1 
ATOM   13433 C  CB    . ILE A 1 3224 ? 203.547 130.474 281.981 1.00 122.26 ? 3224 ILE A CB    1 
ATOM   13434 C  CG1   . ILE A 1 3224 ? 204.908 130.909 282.526 1.00 118.35 ? 3224 ILE A CG1   1 
ATOM   13435 C  CG2   . ILE A 1 3224 ? 202.604 130.120 283.121 1.00 113.49 ? 3224 ILE A CG2   1 
ATOM   13436 C  CD1   . ILE A 1 3224 ? 204.835 132.061 283.502 1.00 112.58 ? 3224 ILE A CD1   1 
ATOM   13437 N  N     . LYS A 1 3225 ? 201.558 129.138 279.875 1.00 128.44 ? 3225 LYS A N     1 
ATOM   13438 C  CA    . LYS A 1 3225 ? 200.275 128.521 279.548 1.00 127.59 ? 3225 LYS A CA    1 
ATOM   13439 C  C     . LYS A 1 3225 ? 200.465 127.183 278.847 1.00 130.39 ? 3225 LYS A C     1 
ATOM   13440 O  O     . LYS A 1 3225 ? 199.674 126.259 279.052 1.00 131.23 ? 3225 LYS A O     1 
ATOM   13441 C  CB    . LYS A 1 3225 ? 199.433 129.463 278.687 1.00 124.59 ? 3225 LYS A CB    1 
ATOM   13442 C  CG    . LYS A 1 3225 ? 199.060 130.774 279.358 1.00 127.16 ? 3225 LYS A CG    1 
ATOM   13443 C  CD    . LYS A 1 3225 ? 198.213 130.544 280.598 1.00 128.98 ? 3225 LYS A CD    1 
ATOM   13444 C  CE    . LYS A 1 3225 ? 196.849 129.981 280.233 1.00 128.29 ? 3225 LYS A CE    1 
ATOM   13445 N  NZ    . LYS A 1 3225 ? 196.045 130.946 279.433 1.00 126.95 ? 3225 LYS A NZ    1 
ATOM   13446 N  N     . SER A 1 3226 ? 201.491 127.064 278.003 1.00 130.15 ? 3226 SER A N     1 
ATOM   13447 C  CA    . SER A 1 3226 ? 201.775 125.776 277.376 1.00 129.37 ? 3226 SER A CA    1 
ATOM   13448 C  C     . SER A 1 3226 ? 202.145 124.729 278.420 1.00 131.36 ? 3226 SER A C     1 
ATOM   13449 O  O     . SER A 1 3226 ? 201.672 123.585 278.363 1.00 128.65 ? 3226 SER A O     1 
ATOM   13450 C  CB    . SER A 1 3226 ? 202.895 125.926 276.346 1.00 123.18 ? 3226 SER A CB    1 
ATOM   13451 O  OG    . SER A 1 3226 ? 204.130 126.213 276.976 1.00 122.61 ? 3226 SER A OG    1 
ATOM   13452 N  N     . GLN A 1 3227 ? 202.985 125.106 279.388 1.00 130.45 ? 3227 GLN A N     1 
ATOM   13453 C  CA    . GLN A 1 3227 ? 203.329 124.179 280.464 1.00 126.33 ? 3227 GLN A CA    1 
ATOM   13454 C  C     . GLN A 1 3227 ? 202.093 123.790 281.270 1.00 130.07 ? 3227 GLN A C     1 
ATOM   13455 O  O     . GLN A 1 3227 ? 201.908 122.614 281.616 1.00 129.90 ? 3227 GLN A O     1 
ATOM   13456 C  CB    . GLN A 1 3227 ? 204.392 124.799 281.371 1.00 122.73 ? 3227 GLN A CB    1 
ATOM   13457 C  CG    . GLN A 1 3227 ? 204.828 123.908 282.525 1.00 118.84 ? 3227 GLN A CG    1 
ATOM   13458 C  CD    . GLN A 1 3227 ? 204.093 124.220 283.814 1.00 118.23 ? 3227 GLN A CD    1 
ATOM   13459 O  OE1   . GLN A 1 3227 ? 203.337 125.188 283.893 1.00 121.74 ? 3227 GLN A OE1   1 
ATOM   13460 N  NE2   . GLN A 1 3227 ? 204.310 123.397 284.834 1.00 111.92 ? 3227 GLN A NE2   1 
ATOM   13461 N  N     . GLU A 1 3228 ? 201.237 124.768 281.579 1.00 129.42 ? 3228 GLU A N     1 
ATOM   13462 C  CA    . GLU A 1 3228 ? 200.019 124.484 282.333 1.00 128.25 ? 3228 GLU A CA    1 
ATOM   13463 C  C     . GLU A 1 3228 ? 199.090 123.559 281.556 1.00 131.31 ? 3228 GLU A C     1 
ATOM   13464 O  O     . GLU A 1 3228 ? 198.478 122.655 282.135 1.00 130.32 ? 3228 GLU A O     1 
ATOM   13465 C  CB    . GLU A 1 3228 ? 199.309 125.789 282.689 1.00 125.79 ? 3228 GLU A CB    1 
ATOM   13466 C  CG    . GLU A 1 3228 ? 197.947 125.602 283.338 1.00 127.47 ? 3228 GLU A CG    1 
ATOM   13467 C  CD    . GLU A 1 3228 ? 197.087 126.848 283.257 1.00 130.78 ? 3228 GLU A CD    1 
ATOM   13468 O  OE1   . GLU A 1 3228 ? 197.509 127.819 282.594 1.00 129.33 ? 3228 GLU A OE1   1 
ATOM   13469 O  OE2   . GLU A 1 3228 ? 195.991 126.857 283.855 1.00 132.41 ? 3228 GLU A OE2   1 
ATOM   13470 N  N     . LEU A 1 3229 ? 198.966 123.779 280.246 1.00 132.74 ? 3229 LEU A N     1 
ATOM   13471 C  CA    . LEU A 1 3229 ? 198.135 122.913 279.416 1.00 131.90 ? 3229 LEU A CA    1 
ATOM   13472 C  C     . LEU A 1 3229 ? 198.674 121.492 279.389 1.00 132.93 ? 3229 LEU A C     1 
ATOM   13473 O  O     . LEU A 1 3229 ? 197.904 120.526 279.453 1.00 132.50 ? 3229 LEU A O     1 
ATOM   13474 C  CB    . LEU A 1 3229 ? 198.047 123.477 277.998 1.00 129.05 ? 3229 LEU A CB    1 
ATOM   13475 C  CG    . LEU A 1 3229 ? 197.292 122.627 276.975 1.00 126.70 ? 3229 LEU A CG    1 
ATOM   13476 C  CD1   . LEU A 1 3229 ? 195.891 122.306 277.470 1.00 128.33 ? 3229 LEU A CD1   1 
ATOM   13477 C  CD2   . LEU A 1 3229 ? 197.249 123.328 275.626 1.00 123.48 ? 3229 LEU A CD2   1 
ATOM   13478 N  N     . GLU A 1 3230 ? 199.998 121.340 279.282 1.00 132.21 ? 3230 GLU A N     1 
ATOM   13479 C  CA    . GLU A 1 3230 ? 200.583 120.003 279.327 1.00 129.55 ? 3230 GLU A CA    1 
ATOM   13480 C  C     . GLU A 1 3230 ? 200.296 119.326 280.660 1.00 132.96 ? 3230 GLU A C     1 
ATOM   13481 O  O     . GLU A 1 3230 ? 199.924 118.146 280.700 1.00 132.02 ? 3230 GLU A O     1 
ATOM   13482 C  CB    . GLU A 1 3230 ? 202.088 120.072 279.071 1.00 122.56 ? 3230 GLU A CB    1 
ATOM   13483 C  CG    . GLU A 1 3230 ? 202.460 120.284 277.616 1.00 118.25 ? 3230 GLU A CG    1 
ATOM   13484 C  CD    . GLU A 1 3230 ? 203.956 120.382 277.408 1.00 116.00 ? 3230 GLU A CD    1 
ATOM   13485 O  OE1   . GLU A 1 3230 ? 204.706 120.221 278.394 1.00 114.42 ? 3230 GLU A OE1   1 
ATOM   13486 O  OE2   . GLU A 1 3230 ? 204.384 120.616 276.258 1.00 114.71 ? 3230 GLU A OE2   1 
ATOM   13487 N  N     . VAL A 1 3231 ? 200.443 120.062 281.764 1.00 133.87 ? 3231 VAL A N     1 
ATOM   13488 C  CA    . VAL A 1 3231 ? 200.161 119.488 283.078 1.00 132.90 ? 3231 VAL A CA    1 
ATOM   13489 C  C     . VAL A 1 3231 ? 198.701 119.055 283.166 1.00 134.36 ? 3231 VAL A C     1 
ATOM   13490 O  O     . VAL A 1 3231 ? 198.387 117.946 283.615 1.00 133.28 ? 3231 VAL A O     1 
ATOM   13491 C  CB    . VAL A 1 3231 ? 200.521 120.490 284.190 1.00 125.40 ? 3231 VAL A CB    1 
ATOM   13492 C  CG1   . VAL A 1 3231 ? 199.898 120.069 285.512 1.00 119.53 ? 3231 VAL A CG1   1 
ATOM   13493 C  CG2   . VAL A 1 3231 ? 202.031 120.615 284.323 1.00 115.57 ? 3231 VAL A CG2   1 
ATOM   13494 N  N     . LYS A 1 3232 ? 197.790 119.922 282.717 1.00 135.04 ? 3232 LYS A N     1 
ATOM   13495 C  CA    . LYS A 1 3232 ? 196.363 119.632 282.811 1.00 130.80 ? 3232 LYS A CA    1 
ATOM   13496 C  C     . LYS A 1 3232 ? 195.985 118.416 281.973 1.00 132.00 ? 3232 LYS A C     1 
ATOM   13497 O  O     . LYS A 1 3232 ? 195.241 117.541 282.431 1.00 131.27 ? 3232 LYS A O     1 
ATOM   13498 C  CB    . LYS A 1 3232 ? 195.550 120.853 282.382 1.00 126.98 ? 3232 LYS A CB    1 
ATOM   13499 C  CG    . LYS A 1 3232 ? 195.583 122.007 283.370 1.00 123.59 ? 3232 LYS A CG    1 
ATOM   13500 C  CD    . LYS A 1 3232 ? 194.537 121.833 284.459 1.00 117.74 ? 3232 LYS A CD    1 
ATOM   13501 C  CE    . LYS A 1 3232 ? 194.257 123.145 285.172 1.00 114.44 ? 3232 LYS A CE    1 
ATOM   13502 N  NZ    . LYS A 1 3232 ? 193.073 123.050 286.070 1.00 114.25 ? 3232 LYS A NZ    1 
ATOM   13503 N  N     . ASN A 1 3233 ? 196.488 118.341 280.737 1.00 134.02 ? 3233 ASN A N     1 
ATOM   13504 C  CA    . ASN A 1 3233 ? 196.095 117.232 279.873 1.00 134.59 ? 3233 ASN A CA    1 
ATOM   13505 C  C     . ASN A 1 3233 ? 196.717 115.922 280.342 1.00 137.15 ? 3233 ASN A C     1 
ATOM   13506 O  O     . ASN A 1 3233 ? 196.078 114.866 280.266 1.00 136.50 ? 3233 ASN A O     1 
ATOM   13507 C  CB    . ASN A 1 3233 ? 196.434 117.543 278.406 1.00 133.35 ? 3233 ASN A CB    1 
ATOM   13508 C  CG    . ASN A 1 3233 ? 197.932 117.575 278.110 1.00 132.73 ? 3233 ASN A CG    1 
ATOM   13509 O  OD1   . ASN A 1 3233 ? 198.733 116.884 278.736 1.00 135.27 ? 3233 ASN A OD1   1 
ATOM   13510 N  ND2   . ASN A 1 3233 ? 198.311 118.395 277.136 1.00 124.29 ? 3233 ASN A ND2   1 
ATOM   13511 N  N     . ALA A 1 3234 ? 197.955 115.968 280.849 1.00 137.86 ? 3234 ALA A N     1 
ATOM   13512 C  CA    . ALA A 1 3234 ? 198.553 114.766 281.420 1.00 133.67 ? 3234 ALA A CA    1 
ATOM   13513 C  C     . ALA A 1 3234 ? 197.766 114.284 282.631 1.00 135.49 ? 3234 ALA A C     1 
ATOM   13514 O  O     . ALA A 1 3234 ? 197.516 113.080 282.780 1.00 133.65 ? 3234 ALA A O     1 
ATOM   13515 C  CB    . ALA A 1 3234 ? 200.011 115.031 281.795 1.00 123.38 ? 3234 ALA A CB    1 
ATOM   13516 N  N     . ALA A 1 3235 ? 197.356 115.209 283.505 1.00 136.20 ? 3235 ALA A N     1 
ATOM   13517 C  CA    . ALA A 1 3235 ? 196.562 114.825 284.667 1.00 130.93 ? 3235 ALA A CA    1 
ATOM   13518 C  C     . ALA A 1 3235 ? 195.220 114.235 284.251 1.00 133.92 ? 3235 ALA A C     1 
ATOM   13519 O  O     . ALA A 1 3235 ? 194.769 113.236 284.824 1.00 132.21 ? 3235 ALA A O     1 
ATOM   13520 C  CB    . ALA A 1 3235 ? 196.358 116.030 285.586 1.00 119.30 ? 3235 ALA A CB    1 
ATOM   13521 N  N     . ALA A 1 3236 ? 194.565 114.842 283.258 1.00 136.27 ? 3236 ALA A N     1 
ATOM   13522 C  CA    . ALA A 1 3236 ? 193.283 114.325 282.792 1.00 134.73 ? 3236 ALA A CA    1 
ATOM   13523 C  C     . ALA A 1 3236 ? 193.432 112.932 282.192 1.00 134.58 ? 3236 ALA A C     1 
ATOM   13524 O  O     . ALA A 1 3236 ? 192.608 112.045 282.452 1.00 131.13 ? 3236 ALA A O     1 
ATOM   13525 C  CB    . ALA A 1 3236 ? 192.668 115.286 281.774 1.00 129.07 ? 3236 ALA A CB    1 
ATOM   13526 N  N     . ASN A 1 3237 ? 194.477 112.719 281.389 1.00 135.76 ? 3237 ASN A N     1 
ATOM   13527 C  CA    . ASN A 1 3237 ? 194.700 111.402 280.800 1.00 134.09 ? 3237 ASN A CA    1 
ATOM   13528 C  C     . ASN A 1 3237 ? 194.998 110.362 281.870 1.00 134.58 ? 3237 ASN A C     1 
ATOM   13529 O  O     . ASN A 1 3237 ? 194.526 109.222 281.786 1.00 130.90 ? 3237 ASN A O     1 
ATOM   13530 C  CB    . ASN A 1 3237 ? 195.838 111.470 279.780 1.00 128.53 ? 3237 ASN A CB    1 
ATOM   13531 C  CG    . ASN A 1 3237 ? 195.492 112.326 278.578 1.00 125.84 ? 3237 ASN A CG    1 
ATOM   13532 O  OD1   . ASN A 1 3237 ? 194.488 113.039 278.577 1.00 127.05 ? 3237 ASN A OD1   1 
ATOM   13533 N  ND2   . ASN A 1 3237 ? 196.324 112.260 277.545 1.00 119.26 ? 3237 ASN A ND2   1 
ATOM   13534 N  N     . ASP A 1 3238 ? 195.789 110.730 282.883 1.00 136.96 ? 3238 ASP A N     1 
ATOM   13535 C  CA    . ASP A 1 3238 ? 196.074 109.799 283.970 1.00 134.78 ? 3238 ASP A CA    1 
ATOM   13536 C  C     . ASP A 1 3238 ? 194.814 109.462 284.759 1.00 134.80 ? 3238 ASP A C     1 
ATOM   13537 O  O     . ASP A 1 3238 ? 194.605 108.303 285.139 1.00 131.32 ? 3238 ASP A O     1 
ATOM   13538 C  CB    . ASP A 1 3238 ? 197.146 110.380 284.890 1.00 131.62 ? 3238 ASP A CB    1 
ATOM   13539 C  CG    . ASP A 1 3238 ? 198.546 110.207 284.334 1.00 129.89 ? 3238 ASP A CG    1 
ATOM   13540 O  OD1   . ASP A 1 3238 ? 198.691 109.565 283.273 1.00 130.61 ? 3238 ASP A OD1   1 
ATOM   13541 O  OD2   . ASP A 1 3238 ? 199.502 110.714 284.959 1.00 125.15 ? 3238 ASP A OD2   1 
ATOM   13542 N  N     . LYS A 1 3239 ? 193.965 110.460 285.018 1.00 136.26 ? 3239 LYS A N     1 
ATOM   13543 C  CA    . LYS A 1 3239 ? 192.743 110.215 285.776 1.00 134.50 ? 3239 LYS A CA    1 
ATOM   13544 C  C     . LYS A 1 3239 ? 191.737 109.390 284.984 1.00 134.35 ? 3239 LYS A C     1 
ATOM   13545 O  O     . LYS A 1 3239 ? 190.986 108.604 285.571 1.00 133.51 ? 3239 LYS A O     1 
ATOM   13546 C  CB    . LYS A 1 3239 ? 192.117 111.541 286.208 1.00 131.55 ? 3239 LYS A CB    1 
ATOM   13547 C  CG    . LYS A 1 3239 ? 192.758 112.157 287.442 1.00 125.62 ? 3239 LYS A CG    1 
ATOM   13548 C  CD    . LYS A 1 3239 ? 191.837 113.176 288.093 1.00 120.99 ? 3239 LYS A CD    1 
ATOM   13549 C  CE    . LYS A 1 3239 ? 192.505 113.839 289.287 1.00 114.78 ? 3239 LYS A CE    1 
ATOM   13550 N  NZ    . LYS A 1 3239 ? 191.622 114.855 289.924 1.00 113.89 ? 3239 LYS A NZ    1 
ATOM   13551 N  N     . LEU A 1 3240 ? 191.701 109.558 283.659 1.00 134.09 ? 3240 LEU A N     1 
ATOM   13552 C  CA    . LEU A 1 3240 ? 190.761 108.796 282.842 1.00 132.17 ? 3240 LEU A CA    1 
ATOM   13553 C  C     . LEU A 1 3240 ? 191.046 107.301 282.895 1.00 132.60 ? 3240 LEU A C     1 
ATOM   13554 O  O     . LEU A 1 3240 ? 190.127 106.489 282.739 1.00 128.82 ? 3240 LEU A O     1 
ATOM   13555 C  CB    . LEU A 1 3240 ? 190.798 109.291 281.396 1.00 128.13 ? 3240 LEU A CB    1 
ATOM   13556 C  CG    . LEU A 1 3240 ? 190.016 110.571 281.094 1.00 126.70 ? 3240 LEU A CG    1 
ATOM   13557 C  CD1   . LEU A 1 3240 ? 190.404 111.128 279.734 1.00 120.02 ? 3240 LEU A CD1   1 
ATOM   13558 C  CD2   . LEU A 1 3240 ? 188.520 110.310 281.162 1.00 124.01 ? 3240 LEU A CD2   1 
ATOM   13559 N  N     . LYS A 1 3241 ? 192.306 106.917 283.111 1.00 135.40 ? 3241 LYS A N     1 
ATOM   13560 C  CA    . LYS A 1 3241 ? 192.661 105.503 283.158 1.00 133.80 ? 3241 LYS A CA    1 
ATOM   13561 C  C     . LYS A 1 3241 ? 192.106 104.800 284.391 1.00 131.10 ? 3241 LYS A C     1 
ATOM   13562 O  O     . LYS A 1 3241 ? 192.057 103.567 284.414 1.00 121.46 ? 3241 LYS A O     1 
ATOM   13563 C  CB    . LYS A 1 3241 ? 194.181 105.341 283.107 1.00 127.73 ? 3241 LYS A CB    1 
ATOM   13564 C  CG    . LYS A 1 3241 ? 194.782 105.591 281.734 1.00 120.44 ? 3241 LYS A CG    1 
ATOM   13565 C  CD    . LYS A 1 3241 ? 196.216 106.086 281.840 1.00 120.33 ? 3241 LYS A CD    1 
ATOM   13566 C  CE    . LYS A 1 3241 ? 196.669 106.740 280.545 1.00 119.29 ? 3241 LYS A CE    1 
ATOM   13567 N  NZ    . LYS A 1 3241 ? 197.995 107.402 280.692 1.00 113.24 ? 3241 LYS A NZ    1 
ATOM   13568 N  N     . GLU A 1 3449 ? 181.867 112.506 285.665 1.00 126.46 ? 3449 GLU A N     1 
ATOM   13569 C  CA    . GLU A 1 3449 ? 181.521 113.895 285.945 1.00 132.27 ? 3449 GLU A CA    1 
ATOM   13570 C  C     . GLU A 1 3449 ? 182.773 114.745 286.128 1.00 138.46 ? 3449 GLU A C     1 
ATOM   13571 O  O     . GLU A 1 3449 ? 182.937 115.774 285.472 1.00 136.85 ? 3449 GLU A O     1 
ATOM   13572 C  CB    . GLU A 1 3449 ? 180.637 113.987 287.189 1.00 128.60 ? 3449 GLU A CB    1 
ATOM   13573 C  CG    . GLU A 1 3449 ? 179.482 112.999 287.208 1.00 125.47 ? 3449 GLU A CG    1 
ATOM   13574 C  CD    . GLU A 1 3449 ? 178.701 113.042 288.505 1.00 120.92 ? 3449 GLU A CD    1 
ATOM   13575 O  OE1   . GLU A 1 3449 ? 178.987 113.922 289.344 1.00 120.59 ? 3449 GLU A OE1   1 
ATOM   13576 O  OE2   . GLU A 1 3449 ? 177.800 112.196 288.686 1.00 117.80 ? 3449 GLU A OE2   1 
ATOM   13577 N  N     . GLU A 1 3450 ? 183.652 114.310 287.034 1.00 141.25 ? 3450 GLU A N     1 
ATOM   13578 C  CA    . GLU A 1 3450 ? 184.884 115.049 287.285 1.00 138.37 ? 3450 GLU A CA    1 
ATOM   13579 C  C     . GLU A 1 3450 ? 185.776 115.073 286.050 1.00 139.36 ? 3450 GLU A C     1 
ATOM   13580 O  O     . GLU A 1 3450 ? 186.232 116.143 285.624 1.00 136.08 ? 3450 GLU A O     1 
ATOM   13581 C  CB    . GLU A 1 3450 ? 185.627 114.438 288.475 1.00 132.71 ? 3450 GLU A CB    1 
ATOM   13582 C  CG    . GLU A 1 3450 ? 186.778 115.282 288.996 1.00 132.02 ? 3450 GLU A CG    1 
ATOM   13583 C  CD    . GLU A 1 3450 ? 187.370 114.730 290.277 1.00 126.55 ? 3450 GLU A CD    1 
ATOM   13584 O  OE1   . GLU A 1 3450 ? 186.865 113.700 290.772 1.00 123.31 ? 3450 GLU A OE1   1 
ATOM   13585 O  OE2   . GLU A 1 3450 ? 188.340 115.326 290.791 1.00 121.09 ? 3450 GLU A OE2   1 
ATOM   13586 N  N     . TYR A 1 3451 ? 186.024 113.905 285.451 1.00 141.53 ? 3451 TYR A N     1 
ATOM   13587 C  CA    . TYR A 1 3451 ? 186.866 113.841 284.261 1.00 139.26 ? 3451 TYR A CA    1 
ATOM   13588 C  C     . TYR A 1 3451 ? 186.302 114.687 283.128 1.00 139.80 ? 3451 TYR A C     1 
ATOM   13589 O  O     . TYR A 1 3451 ? 187.067 115.253 282.339 1.00 138.53 ? 3451 TYR A O     1 
ATOM   13590 C  CB    . TYR A 1 3451 ? 187.034 112.389 283.814 1.00 135.20 ? 3451 TYR A CB    1 
ATOM   13591 C  CG    . TYR A 1 3451 ? 187.345 111.429 284.942 1.00 134.81 ? 3451 TYR A CG    1 
ATOM   13592 C  CD1   . TYR A 1 3451 ? 188.363 111.700 285.848 1.00 133.17 ? 3451 TYR A CD1   1 
ATOM   13593 C  CD2   . TYR A 1 3451 ? 186.623 110.254 285.099 1.00 130.38 ? 3451 TYR A CD2   1 
ATOM   13594 C  CE1   . TYR A 1 3451 ? 188.650 110.826 286.881 1.00 132.01 ? 3451 TYR A CE1   1 
ATOM   13595 C  CE2   . TYR A 1 3451 ? 186.904 109.373 286.129 1.00 125.86 ? 3451 TYR A CE2   1 
ATOM   13596 C  CZ    . TYR A 1 3451 ? 187.919 109.666 287.017 1.00 128.76 ? 3451 TYR A CZ    1 
ATOM   13597 O  OH    . TYR A 1 3451 ? 188.203 108.794 288.043 1.00 118.86 ? 3451 TYR A OH    1 
ATOM   13598 N  N     . ALA A 1 3452 ? 184.974 114.792 283.035 1.00 140.41 ? 3452 ALA A N     1 
ATOM   13599 C  CA    . ALA A 1 3452 ? 184.373 115.694 282.060 1.00 137.55 ? 3452 ALA A CA    1 
ATOM   13600 C  C     . ALA A 1 3452 ? 184.760 117.141 282.342 1.00 138.39 ? 3452 ALA A C     1 
ATOM   13601 O  O     . ALA A 1 3452 ? 185.062 117.903 281.416 1.00 137.44 ? 3452 ALA A O     1 
ATOM   13602 C  CB    . ALA A 1 3452 ? 182.853 115.532 282.059 1.00 129.79 ? 3452 ALA A CB    1 
ATOM   13603 N  N     . VAL A 1 3453 ? 184.767 117.534 283.618 1.00 138.94 ? 3453 VAL A N     1 
ATOM   13604 C  CA    . VAL A 1 3453 ? 185.176 118.888 283.975 1.00 136.50 ? 3453 VAL A CA    1 
ATOM   13605 C  C     . VAL A 1 3453 ? 186.637 119.118 283.607 1.00 135.97 ? 3453 VAL A C     1 
ATOM   13606 O  O     . VAL A 1 3453 ? 186.997 120.171 283.063 1.00 135.02 ? 3453 VAL A O     1 
ATOM   13607 C  CB    . VAL A 1 3453 ? 184.919 119.147 285.471 1.00 130.49 ? 3453 VAL A CB    1 
ATOM   13608 C  CG1   . VAL A 1 3453 ? 185.476 120.502 285.883 1.00 121.60 ? 3453 VAL A CG1   1 
ATOM   13609 C  CG2   . VAL A 1 3453 ? 183.431 119.062 285.775 1.00 124.61 ? 3453 VAL A CG2   1 
ATOM   13610 N  N     . LEU A 1 3454 ? 187.500 118.141 283.895 1.00 135.64 ? 3454 LEU A N     1 
ATOM   13611 C  CA    . LEU A 1 3454 ? 188.916 118.287 283.557 1.00 134.81 ? 3454 LEU A CA    1 
ATOM   13612 C  C     . LEU A 1 3454 ? 189.128 118.404 282.052 1.00 137.58 ? 3454 LEU A C     1 
ATOM   13613 O  O     . LEU A 1 3454 ? 189.914 119.239 281.594 1.00 137.32 ? 3454 LEU A O     1 
ATOM   13614 C  CB    . LEU A 1 3454 ? 189.738 117.130 284.132 1.00 131.74 ? 3454 LEU A CB    1 
ATOM   13615 C  CG    . LEU A 1 3454 ? 190.155 117.176 285.610 1.00 127.47 ? 3454 LEU A CG    1 
ATOM   13616 C  CD1   . LEU A 1 3454 ? 189.006 116.958 286.572 1.00 127.82 ? 3454 LEU A CD1   1 
ATOM   13617 C  CD2   . LEU A 1 3454 ? 191.269 116.169 285.871 1.00 119.34 ? 3454 LEU A CD2   1 
ATOM   13618 N  N     . ILE A 1 3455 ? 188.438 117.578 281.259 1.00 138.79 ? 3455 ILE A N     1 
ATOM   13619 C  CA    . ILE A 1 3455 ? 188.648 117.656 279.814 1.00 136.56 ? 3455 ILE A CA    1 
ATOM   13620 C  C     . ILE A 1 3455 ? 188.064 118.948 279.246 1.00 136.52 ? 3455 ILE A C     1 
ATOM   13621 O  O     . ILE A 1 3455 ? 188.637 119.538 278.321 1.00 134.49 ? 3455 ILE A O     1 
ATOM   13622 C  CB    . ILE A 1 3455 ? 188.092 116.408 279.097 1.00 133.34 ? 3455 ILE A CB    1 
ATOM   13623 C  CG1   . ILE A 1 3455 ? 186.579 116.285 279.273 1.00 131.41 ? 3455 ILE A CG1   1 
ATOM   13624 C  CG2   . ILE A 1 3455 ? 188.802 115.152 279.588 1.00 129.71 ? 3455 ILE A CG2   1 
ATOM   13625 C  CD1   . ILE A 1 3455 ? 186.014 114.960 278.803 1.00 122.35 ? 3455 ILE A CD1   1 
ATOM   13626 N  N     . SER A 1 3456 ? 186.933 119.419 279.782 1.00 137.83 ? 3456 SER A N     1 
ATOM   13627 C  CA    . SER A 1 3456 ? 186.381 120.692 279.330 1.00 134.57 ? 3456 SER A CA    1 
ATOM   13628 C  C     . SER A 1 3456 ? 187.319 121.849 279.658 1.00 135.46 ? 3456 SER A C     1 
ATOM   13629 O  O     . SER A 1 3456 ? 187.527 122.743 278.827 1.00 131.20 ? 3456 SER A O     1 
ATOM   13630 C  CB    . SER A 1 3456 ? 185.005 120.920 279.953 1.00 128.35 ? 3456 SER A CB    1 
ATOM   13631 O  OG    . SER A 1 3456 ? 185.111 121.192 281.340 1.00 129.98 ? 3456 SER A OG    1 
ATOM   13632 N  N     . GLU A 1 3457 ? 187.901 121.848 280.861 1.00 136.72 ? 3457 GLU A N     1 
ATOM   13633 C  CA    . GLU A 1 3457 ? 188.847 122.900 281.208 1.00 135.18 ? 3457 GLU A CA    1 
ATOM   13634 C  C     . GLU A 1 3457 ? 190.125 122.791 280.385 1.00 138.75 ? 3457 GLU A C     1 
ATOM   13635 O  O     . GLU A 1 3457 ? 190.733 123.814 280.055 1.00 138.25 ? 3457 GLU A O     1 
ATOM   13636 C  CB    . GLU A 1 3457 ? 189.148 122.871 282.710 1.00 131.48 ? 3457 GLU A CB    1 
ATOM   13637 C  CG    . GLU A 1 3457 ? 190.312 121.988 283.130 1.00 130.42 ? 3457 GLU A CG    1 
ATOM   13638 C  CD    . GLU A 1 3457 ? 190.407 121.828 284.634 1.00 125.84 ? 3457 GLU A CD    1 
ATOM   13639 O  OE1   . GLU A 1 3457 ? 189.548 122.388 285.347 1.00 123.40 ? 3457 GLU A OE1   1 
ATOM   13640 O  OE2   . GLU A 1 3457 ? 191.341 121.143 285.103 1.00 121.89 ? 3457 GLU A OE2   1 
ATOM   13641 N  N     . ALA A 1 3458 ? 190.535 121.572 280.023 1.00 139.50 ? 3458 ALA A N     1 
ATOM   13642 C  CA    . ALA A 1 3458 ? 191.684 121.412 279.139 1.00 137.26 ? 3458 ALA A CA    1 
ATOM   13643 C  C     . ALA A 1 3458 ? 191.397 121.987 277.758 1.00 137.44 ? 3458 ALA A C     1 
ATOM   13644 O  O     . ALA A 1 3458 ? 192.260 122.635 277.155 1.00 135.90 ? 3458 ALA A O     1 
ATOM   13645 C  CB    . ALA A 1 3458 ? 192.072 119.937 279.040 1.00 126.35 ? 3458 ALA A CB    1 
ATOM   13646 N  N     . GLN A 1 3459 ? 190.189 121.757 277.239 1.00 137.48 ? 3459 GLN A N     1 
ATOM   13647 C  CA    . GLN A 1 3459 ? 189.808 122.349 275.958 1.00 133.39 ? 3459 GLN A CA    1 
ATOM   13648 C  C     . GLN A 1 3459 ? 189.776 123.871 276.041 1.00 134.97 ? 3459 GLN A C     1 
ATOM   13649 O  O     . GLN A 1 3459 ? 190.208 124.565 275.109 1.00 132.62 ? 3459 GLN A O     1 
ATOM   13650 C  CB    . GLN A 1 3459 ? 188.450 121.804 275.515 1.00 128.77 ? 3459 GLN A CB    1 
ATOM   13651 C  CG    . GLN A 1 3459 ? 188.098 122.108 274.069 1.00 120.23 ? 3459 GLN A CG    1 
ATOM   13652 C  CD    . GLN A 1 3459 ? 186.776 121.497 273.654 1.00 114.29 ? 3459 GLN A CD    1 
ATOM   13653 O  OE1   . GLN A 1 3459 ? 186.554 120.297 273.821 1.00 117.40 ? 3459 GLN A OE1   1 
ATOM   13654 N  NE2   . GLN A 1 3459 ? 185.888 122.319 273.107 1.00 102.96 ? 3459 GLN A NE2   1 
ATOM   13655 N  N     . ALA A 1 3460 ? 189.260 124.409 277.150 1.00 136.80 ? 3460 ALA A N     1 
ATOM   13656 C  CA    . ALA A 1 3460 ? 189.253 125.857 277.334 1.00 133.08 ? 3460 ALA A CA    1 
ATOM   13657 C  C     . ALA A 1 3460 ? 190.671 126.414 277.380 1.00 133.55 ? 3460 ALA A C     1 
ATOM   13658 O  O     . ALA A 1 3460 ? 190.951 127.473 276.805 1.00 131.20 ? 3460 ALA A O     1 
ATOM   13659 C  CB    . ALA A 1 3460 ? 188.490 126.221 278.607 1.00 124.73 ? 3460 ALA A CB    1 
ATOM   13660 N  N     . ILE A 1 3461 ? 191.581 125.714 278.062 1.00 134.15 ? 3461 ILE A N     1 
ATOM   13661 C  CA    . ILE A 1 3461 ? 192.974 126.146 278.112 1.00 134.38 ? 3461 ILE A CA    1 
ATOM   13662 C  C     . ILE A 1 3461 ? 193.608 126.068 276.729 1.00 135.39 ? 3461 ILE A C     1 
ATOM   13663 O  O     . ILE A 1 3461 ? 194.421 126.921 276.360 1.00 133.48 ? 3461 ILE A O     1 
ATOM   13664 C  CB    . ILE A 1 3461 ? 193.753 125.317 279.151 1.00 133.10 ? 3461 ILE A CB    1 
ATOM   13665 C  CG1   . ILE A 1 3461 ? 193.241 125.611 280.562 1.00 129.10 ? 3461 ILE A CG1   1 
ATOM   13666 C  CG2   . ILE A 1 3461 ? 195.245 125.607 279.069 1.00 129.47 ? 3461 ILE A CG2   1 
ATOM   13667 C  CD1   . ILE A 1 3461 ? 193.291 127.075 280.939 1.00 122.33 ? 3461 ILE A CD1   1 
ATOM   13668 N  N     . LYS A 1 3462 ? 193.252 125.049 275.943 1.00 136.65 ? 3462 LYS A N     1 
ATOM   13669 C  CA    . LYS A 1 3462 ? 193.752 124.958 274.573 1.00 133.22 ? 3462 LYS A CA    1 
ATOM   13670 C  C     . LYS A 1 3462 ? 193.301 126.157 273.749 1.00 132.36 ? 3462 LYS A C     1 
ATOM   13671 O  O     . LYS A 1 3462 ? 194.094 126.755 273.008 1.00 129.00 ? 3462 LYS A O     1 
ATOM   13672 C  CB    . LYS A 1 3462 ? 193.276 123.659 273.921 1.00 129.23 ? 3462 LYS A CB    1 
ATOM   13673 C  CG    . LYS A 1 3462 ? 193.961 122.403 274.427 1.00 128.45 ? 3462 LYS A CG    1 
ATOM   13674 C  CD    . LYS A 1 3462 ? 193.232 121.153 273.960 1.00 124.90 ? 3462 LYS A CD    1 
ATOM   13675 C  CE    . LYS A 1 3462 ? 193.830 119.901 274.579 1.00 119.44 ? 3462 LYS A CE    1 
ATOM   13676 N  NZ    . LYS A 1 3462 ? 193.676 119.887 276.060 1.00 120.25 ? 3462 LYS A NZ    1 
ATOM   13677 N  N     . ALA A 1 3463 ? 192.022 126.523 273.864 1.00 132.70 ? 3463 ALA A N     1 
ATOM   13678 C  CA    . ALA A 1 3463 ? 191.514 127.681 273.134 1.00 128.19 ? 3463 ALA A CA    1 
ATOM   13679 C  C     . ALA A 1 3463 ? 192.205 128.965 273.585 1.00 131.21 ? 3463 ALA A C     1 
ATOM   13680 O  O     . ALA A 1 3463 ? 192.561 129.814 272.757 1.00 127.50 ? 3463 ALA A O     1 
ATOM   13681 C  CB    . ALA A 1 3463 ? 190.001 127.793 273.313 1.00 119.50 ? 3463 ALA A CB    1 
ATOM   13682 N  N     . ASP A 1 3464 ? 192.400 129.120 274.897 1.00 133.93 ? 3464 ASP A N     1 
ATOM   13683 C  CA    . ASP A 1 3464 ? 193.083 130.303 275.412 1.00 132.02 ? 3464 ASP A CA    1 
ATOM   13684 C  C     . ASP A 1 3464 ? 194.521 130.370 274.913 1.00 133.46 ? 3464 ASP A C     1 
ATOM   13685 O  O     . ASP A 1 3464 ? 195.009 131.445 274.550 1.00 133.21 ? 3464 ASP A O     1 
ATOM   13686 C  CB    . ASP A 1 3464 ? 193.044 130.305 276.941 1.00 130.60 ? 3464 ASP A CB    1 
ATOM   13687 C  CG    . ASP A 1 3464 ? 193.406 131.654 277.532 1.00 133.12 ? 3464 ASP A CG    1 
ATOM   13688 O  OD1   . ASP A 1 3464 ? 193.526 132.631 276.764 1.00 135.17 ? 3464 ASP A OD1   1 
ATOM   13689 O  OD2   . ASP A 1 3464 ? 193.571 131.736 278.768 1.00 129.41 ? 3464 ASP A OD2   1 
ATOM   13690 N  N     . LEU A 1 3465 ? 195.214 129.230 274.889 1.00 133.16 ? 3465 LEU A N     1 
ATOM   13691 C  CA    . LEU A 1 3465 ? 196.583 129.192 274.386 1.00 131.72 ? 3465 LEU A CA    1 
ATOM   13692 C  C     . LEU A 1 3465 ? 196.635 129.548 272.907 1.00 130.50 ? 3465 LEU A C     1 
ATOM   13693 O  O     . LEU A 1 3465 ? 197.538 130.269 272.465 1.00 127.56 ? 3465 LEU A O     1 
ATOM   13694 C  CB    . LEU A 1 3465 ? 197.188 127.810 274.626 1.00 130.19 ? 3465 LEU A CB    1 
ATOM   13695 C  CG    . LEU A 1 3465 ? 198.639 127.600 274.190 1.00 124.76 ? 3465 LEU A CG    1 
ATOM   13696 C  CD1   . LEU A 1 3465 ? 199.590 127.972 275.316 1.00 121.77 ? 3465 LEU A CD1   1 
ATOM   13697 C  CD2   . LEU A 1 3465 ? 198.864 126.164 273.745 1.00 117.24 ? 3465 LEU A CD2   1 
ATOM   13698 N  N     . ALA A 1 3466 ? 195.682 129.040 272.122 1.00 130.23 ? 3466 ALA A N     1 
ATOM   13699 C  CA    . ALA A 1 3466 ? 195.633 129.384 270.705 1.00 125.97 ? 3466 ALA A CA    1 
ATOM   13700 C  C     . ALA A 1 3466 ? 195.416 130.878 270.510 1.00 128.20 ? 3466 ALA A C     1 
ATOM   13701 O  O     . ALA A 1 3466 ? 196.087 131.509 269.684 1.00 125.80 ? 3466 ALA A O     1 
ATOM   13702 C  CB    . ALA A 1 3466 ? 194.535 128.583 270.007 1.00 117.74 ? 3466 ALA A CB    1 
ATOM   13703 N  N     . ALA A 1 3467 ? 194.489 131.466 271.270 1.00 129.82 ? 3467 ALA A N     1 
ATOM   13704 C  CA    . ALA A 1 3467 ? 194.255 132.904 271.165 1.00 125.73 ? 3467 ALA A CA    1 
ATOM   13705 C  C     . ALA A 1 3467 ? 195.492 133.695 271.576 1.00 127.25 ? 3467 ALA A C     1 
ATOM   13706 O  O     . ALA A 1 3467 ? 195.848 134.689 270.928 1.00 123.24 ? 3467 ALA A O     1 
ATOM   13707 C  CB    . ALA A 1 3467 ? 193.052 133.305 272.017 1.00 115.74 ? 3467 ALA A CB    1 
ATOM   13708 N  N     . VAL A 1 3468 ? 196.165 133.262 272.644 1.00 131.11 ? 3468 VAL A N     1 
ATOM   13709 C  CA    . VAL A 1 3468 ? 197.348 133.969 273.124 1.00 131.41 ? 3468 VAL A CA    1 
ATOM   13710 C  C     . VAL A 1 3468 ? 198.465 133.916 272.090 1.00 127.40 ? 3468 VAL A C     1 
ATOM   13711 O  O     . VAL A 1 3468 ? 199.126 134.925 271.819 1.00 125.37 ? 3468 VAL A O     1 
ATOM   13712 C  CB    . VAL A 1 3468 ? 197.799 133.395 274.482 1.00 130.41 ? 3468 VAL A CB    1 
ATOM   13713 C  CG1   . VAL A 1 3468 ? 199.227 133.816 274.794 1.00 126.57 ? 3468 VAL A CG1   1 
ATOM   13714 C  CG2   . VAL A 1 3468 ? 196.858 133.851 275.586 1.00 122.45 ? 3468 VAL A CG2   1 
ATOM   13715 N  N     . GLU A 1 3469 ? 198.695 132.743 271.490 1.00 124.96 ? 3469 GLU A N     1 
ATOM   13716 C  CA    . GLU A 1 3469 ? 199.761 132.644 270.498 1.00 122.31 ? 3469 GLU A CA    1 
ATOM   13717 C  C     . GLU A 1 3469 ? 199.408 133.393 269.218 1.00 120.05 ? 3469 GLU A C     1 
ATOM   13718 O  O     . GLU A 1 3469 ? 200.298 133.957 268.572 1.00 115.98 ? 3469 GLU A O     1 
ATOM   13719 C  CB    . GLU A 1 3469 ? 200.093 131.179 270.200 1.00 120.57 ? 3469 GLU A CB    1 
ATOM   13720 C  CG    . GLU A 1 3469 ? 198.989 130.378 269.540 1.00 120.33 ? 3469 GLU A CG    1 
ATOM   13721 C  CD    . GLU A 1 3469 ? 199.318 128.900 269.455 1.00 114.76 ? 3469 GLU A CD    1 
ATOM   13722 O  OE1   . GLU A 1 3469 ? 200.339 128.555 268.823 1.00 108.35 ? 3469 GLU A OE1   1 
ATOM   13723 O  OE2   . GLU A 1 3469 ? 198.561 128.085 270.021 1.00 114.70 ? 3469 GLU A OE2   1 
ATOM   13724 N  N     . ALA A 1 3470 ? 198.126 133.430 268.843 1.00 120.93 ? 3470 ALA A N     1 
ATOM   13725 C  CA    . ALA A 1 3470 ? 197.724 134.248 267.705 1.00 118.21 ? 3470 ALA A CA    1 
ATOM   13726 C  C     . ALA A 1 3470 ? 197.986 135.726 267.973 1.00 116.67 ? 3470 ALA A C     1 
ATOM   13727 O  O     . ALA A 1 3470 ? 198.497 136.444 267.104 1.00 110.99 ? 3470 ALA A O     1 
ATOM   13728 C  CB    . ALA A 1 3470 ? 196.249 134.012 267.381 1.00 111.89 ? 3470 ALA A CB    1 
ATOM   13729 N  N     . LYS A 1 3471 ? 197.651 136.194 269.179 1.00 118.23 ? 3471 LYS A N     1 
ATOM   13730 C  CA    . LYS A 1 3471 ? 197.926 137.582 269.539 1.00 112.86 ? 3471 LYS A CA    1 
ATOM   13731 C  C     . LYS A 1 3471 ? 199.424 137.862 269.547 1.00 113.65 ? 3471 LYS A C     1 
ATOM   13732 O  O     . LYS A 1 3471 ? 199.867 138.931 269.108 1.00 113.52 ? 3471 LYS A O     1 
ATOM   13733 C  CB    . LYS A 1 3471 ? 197.306 137.898 270.900 1.00 110.29 ? 3471 LYS A CB    1 
ATOM   13734 C  CG    . LYS A 1 3471 ? 197.868 139.138 271.578 1.00 109.83 ? 3471 LYS A CG    1 
ATOM   13735 C  CD    . LYS A 1 3471 ? 197.105 139.462 272.853 1.00 108.28 ? 3471 LYS A CD    1 
ATOM   13736 C  CE    . LYS A 1 3471 ? 195.725 140.017 272.544 1.00 105.78 ? 3471 LYS A CE    1 
ATOM   13737 N  NZ    . LYS A 1 3471 ? 195.049 140.532 273.767 1.00 100.79 ? 3471 LYS A NZ    1 
ATOM   13738 N  N     . VAL A 1 3472 ? 200.219 136.912 270.044 1.00 113.37 ? 3472 VAL A N     1 
ATOM   13739 C  CA    . VAL A 1 3472 ? 201.670 137.081 270.071 1.00 111.65 ? 3472 VAL A CA    1 
ATOM   13740 C  C     . VAL A 1 3472 ? 202.222 137.191 268.655 1.00 113.34 ? 3472 VAL A C     1 
ATOM   13741 O  O     . VAL A 1 3472 ? 203.069 138.045 268.370 1.00 113.90 ? 3472 VAL A O     1 
ATOM   13742 C  CB    . VAL A 1 3472 ? 202.327 135.927 270.849 1.00 112.48 ? 3472 VAL A CB    1 
ATOM   13743 C  CG1   . VAL A 1 3472 ? 203.819 135.868 270.562 1.00 103.73 ? 3472 VAL A CG1   1 
ATOM   13744 C  CG2   . VAL A 1 3472 ? 202.083 136.088 272.341 1.00 117.23 ? 3472 VAL A CG2   1 
ATOM   13745 N  N     . ASN A 1 3473 ? 201.754 136.330 267.749 1.00 116.04 ? 3473 ASN A N     1 
ATOM   13746 C  CA    . ASN A 1 3473 ? 202.206 136.396 266.362 1.00 110.85 ? 3473 ASN A CA    1 
ATOM   13747 C  C     . ASN A 1 3473 ? 201.795 137.711 265.709 1.00 106.01 ? 3473 ASN A C     1 
ATOM   13748 O  O     . ASN A 1 3473 ? 202.572 138.309 264.956 1.00 101.62 ? 3473 ASN A O     1 
ATOM   13749 C  CB    . ASN A 1 3473 ? 201.656 135.208 265.575 1.00 108.27 ? 3473 ASN A CB    1 
ATOM   13750 C  CG    . ASN A 1 3473 ? 202.387 133.918 265.886 1.00 110.94 ? 3473 ASN A CG    1 
ATOM   13751 O  OD1   . ASN A 1 3473 ? 203.366 133.910 266.632 1.00 113.01 ? 3473 ASN A OD1   1 
ATOM   13752 N  ND2   . ASN A 1 3473 ? 201.913 132.816 265.316 1.00 107.55 ? 3473 ASN A ND2   1 
ATOM   13753 N  N     . ARG A 1 3474 ? 200.573 138.175 265.984 1.00 103.80 ? 3474 ARG A N     1 
ATOM   13754 C  CA    . ARG A 1 3474 ? 200.120 139.447 265.427 1.00 100.84 ? 3474 ARG A CA    1 
ATOM   13755 C  C     . ARG A 1 3474 ? 200.982 140.603 265.924 1.00 105.53 ? 3474 ARG A C     1 
ATOM   13756 O  O     . ARG A 1 3474 ? 201.365 141.487 265.145 1.00 106.00 ? 3474 ARG A O     1 
ATOM   13757 C  CB    . ARG A 1 3474 ? 198.651 139.670 265.787 1.00 98.33  ? 3474 ARG A CB    1 
ATOM   13758 C  CG    . ARG A 1 3474 ? 197.929 140.699 264.935 1.00 91.17  ? 3474 ARG A CG    1 
ATOM   13759 C  CD    . ARG A 1 3474 ? 196.576 141.035 265.541 1.00 87.32  ? 3474 ARG A CD    1 
ATOM   13760 N  NE    . ARG A 1 3474 ? 195.891 142.100 264.820 1.00 93.16  ? 3474 ARG A NE    1 
ATOM   13761 C  CZ    . ARG A 1 3474 ? 195.175 141.920 263.718 1.00 98.54  ? 3474 ARG A CZ    1 
ATOM   13762 N  NH1   . ARG A 1 3474 ? 195.024 140.722 263.178 1.00 100.05 ? 3474 ARG A NH1   1 
ATOM   13763 N  NH2   . ARG A 1 3474 ? 194.594 142.970 263.144 1.00 99.19  ? 3474 ARG A NH2   1 
ATOM   13764 N  N     . SER A 1 3475 ? 201.307 140.606 267.217 1.00 106.94 ? 3475 SER A N     1 
ATOM   13765 C  CA    . SER A 1 3475 ? 202.143 141.668 267.769 1.00 104.79 ? 3475 SER A CA    1 
ATOM   13766 C  C     . SER A 1 3475 ? 203.568 141.593 267.229 1.00 103.35 ? 3475 SER A C     1 
ATOM   13767 O  O     . SER A 1 3475 ? 204.210 142.627 267.002 1.00 101.72 ? 3475 SER A O     1 
ATOM   13768 C  CB    . SER A 1 3475 ? 202.133 141.590 269.294 1.00 108.14 ? 3475 SER A CB    1 
ATOM   13769 O  OG    . SER A 1 3475 ? 202.416 140.275 269.738 1.00 108.36 ? 3475 SER A OG    1 
ATOM   13770 N  N     . THR A 1 3476 ? 204.085 140.380 267.022 1.00 104.76 ? 3476 THR A N     1 
ATOM   13771 C  CA    . THR A 1 3476 ? 205.405 140.234 266.418 1.00 100.51 ? 3476 THR A CA    1 
ATOM   13772 C  C     . THR A 1 3476 ? 205.413 140.752 264.986 1.00 103.72 ? 3476 THR A C     1 
ATOM   13773 O  O     . THR A 1 3476 ? 206.390 141.371 264.548 1.00 103.56 ? 3476 THR A O     1 
ATOM   13774 C  CB    . THR A 1 3476 ? 205.849 138.773 266.464 1.00 99.01  ? 3476 THR A CB    1 
ATOM   13775 O  OG1   . THR A 1 3476 ? 205.595 138.235 267.769 1.00 100.39 ? 3476 THR A OG1   1 
ATOM   13776 C  CG2   . THR A 1 3476 ? 207.335 138.659 266.158 1.00 92.77  ? 3476 THR A CG2   1 
ATOM   13777 N  N     . ALA A 1 3477 ? 204.336 140.500 264.238 1.00 101.46 ? 3477 ALA A N     1 
ATOM   13778 C  CA    . ALA A 1 3477 ? 204.217 141.069 262.899 1.00 98.81  ? 3477 ALA A CA    1 
ATOM   13779 C  C     . ALA A 1 3477 ? 204.173 142.590 262.956 1.00 100.69 ? 3477 ALA A C     1 
ATOM   13780 O  O     . ALA A 1 3477 ? 204.769 143.272 262.113 1.00 96.78  ? 3477 ALA A O     1 
ATOM   13781 C  CB    . ALA A 1 3477 ? 202.975 140.519 262.200 1.00 93.81  ? 3477 ALA A CB    1 
ATOM   13782 N  N     . LEU A 1 3478 ? 203.463 143.139 263.946 1.00 104.44 ? 3478 LEU A N     1 
ATOM   13783 C  CA    . LEU A 1 3478 ? 203.466 144.584 264.158 1.00 98.30  ? 3478 LEU A CA    1 
ATOM   13784 C  C     . LEU A 1 3478 ? 204.882 145.104 264.366 1.00 96.27  ? 3478 LEU A C     1 
ATOM   13785 O  O     . LEU A 1 3478 ? 205.280 146.114 263.775 1.00 93.92  ? 3478 LEU A O     1 
ATOM   13786 C  CB    . LEU A 1 3478 ? 202.600 144.942 265.364 1.00 100.69 ? 3478 LEU A CB    1 
ATOM   13787 C  CG    . LEU A 1 3478 ? 201.107 145.195 265.188 1.00 106.89 ? 3478 LEU A CG    1 
ATOM   13788 C  CD1   . LEU A 1 3478 ? 200.502 145.459 266.551 1.00 106.69 ? 3478 LEU A CD1   1 
ATOM   13789 C  CD2   . LEU A 1 3478 ? 200.856 146.364 264.250 1.00 101.05 ? 3478 LEU A CD2   1 
ATOM   13790 N  N     . LEU A 1 3479 ? 205.653 144.431 265.222 1.00 99.34  ? 3479 LEU A N     1 
ATOM   13791 C  CA    . LEU A 1 3479 ? 207.016 144.875 265.499 1.00 96.52  ? 3479 LEU A CA    1 
ATOM   13792 C  C     . LEU A 1 3479 ? 207.903 144.763 264.265 1.00 93.93  ? 3479 LEU A C     1 
ATOM   13793 O  O     . LEU A 1 3479 ? 208.751 145.628 264.021 1.00 94.59  ? 3479 LEU A O     1 
ATOM   13794 C  CB    . LEU A 1 3479 ? 207.612 144.075 266.656 1.00 96.25  ? 3479 LEU A CB    1 
ATOM   13795 C  CG    . LEU A 1 3479 ? 206.963 144.284 268.023 1.00 99.89  ? 3479 LEU A CG    1 
ATOM   13796 C  CD1   . LEU A 1 3479 ? 207.735 143.517 269.071 1.00 98.61  ? 3479 LEU A CD1   1 
ATOM   13797 C  CD2   . LEU A 1 3479 ? 206.896 145.762 268.372 1.00 100.17 ? 3479 LEU A CD2   1 
ATOM   13798 N  N     . LYS A 1 3480 ? 207.736 143.696 263.484 1.00 95.81  ? 3480 LYS A N     1 
ATOM   13799 C  CA    . LYS A 1 3480 ? 208.507 143.563 262.252 1.00 97.42  ? 3480 LYS A CA    1 
ATOM   13800 C  C     . LYS A 1 3480 ? 208.173 144.684 261.274 1.00 96.13  ? 3480 LYS A C     1 
ATOM   13801 O  O     . LYS A 1 3480 ? 209.064 145.227 260.611 1.00 86.52  ? 3480 LYS A O     1 
ATOM   13802 C  CB    . LYS A 1 3480 ? 208.257 142.196 261.616 1.00 99.49  ? 3480 LYS A CB    1 
ATOM   13803 C  CG    . LYS A 1 3480 ? 208.836 141.033 262.407 1.00 99.72  ? 3480 LYS A CG    1 
ATOM   13804 C  CD    . LYS A 1 3480 ? 208.758 139.734 261.622 1.00 98.94  ? 3480 LYS A CD    1 
ATOM   13805 C  CE    . LYS A 1 3480 ? 207.326 139.237 261.518 1.00 95.94  ? 3480 LYS A CE    1 
ATOM   13806 N  NZ    . LYS A 1 3480 ? 206.844 138.668 262.806 1.00 93.95  ? 3480 LYS A NZ    1 
ATOM   13807 N  N     . SER A 1 3481 ? 206.891 145.043 261.172 1.00 97.54  ? 3481 SER A N     1 
ATOM   13808 C  CA    . SER A 1 3481 ? 206.499 146.145 260.299 1.00 93.45  ? 3481 SER A CA    1 
ATOM   13809 C  C     . SER A 1 3481 ? 207.030 147.479 260.813 1.00 94.16  ? 3481 SER A C     1 
ATOM   13810 O  O     . SER A 1 3481 ? 207.375 148.363 260.020 1.00 91.86  ? 3481 SER A O     1 
ATOM   13811 C  CB    . SER A 1 3481 ? 204.978 146.191 260.164 1.00 91.20  ? 3481 SER A CB    1 
ATOM   13812 O  OG    . SER A 1 3481 ? 204.466 144.944 259.729 1.00 96.75  ? 3481 SER A OG    1 
ATOM   13813 N  N     . LEU A 1 3482 ? 207.095 147.645 262.131 1.00 94.35  ? 3482 LEU A N     1 
ATOM   13814 C  CA    . LEU A 1 3482 ? 207.508 148.901 262.741 1.00 91.22  ? 3482 LEU A CA    1 
ATOM   13815 C  C     . LEU A 1 3482 ? 209.007 148.989 262.996 1.00 93.13  ? 3482 LEU A C     1 
ATOM   13816 O  O     . LEU A 1 3482 ? 209.463 149.993 263.547 1.00 98.02  ? 3482 LEU A O     1 
ATOM   13817 C  CB    . LEU A 1 3482 ? 206.755 149.116 264.059 1.00 85.13  ? 3482 LEU A CB    1 
ATOM   13818 C  CG    . LEU A 1 3482 ? 205.277 149.497 263.950 1.00 81.59  ? 3482 LEU A CG    1 
ATOM   13819 C  CD1   . LEU A 1 3482 ? 204.726 149.883 265.312 1.00 83.77  ? 3482 LEU A CD1   1 
ATOM   13820 C  CD2   . LEU A 1 3482 ? 205.085 150.627 262.953 1.00 86.05  ? 3482 LEU A CD2   1 
ATOM   13821 N  N     . SER A 1 3483 ? 209.774 147.954 262.650 1.00 92.27  ? 3483 SER A N     1 
ATOM   13822 C  CA    . SER A 1 3483 ? 211.224 148.022 262.821 1.00 91.28  ? 3483 SER A CA    1 
ATOM   13823 C  C     . SER A 1 3483 ? 211.839 149.128 261.969 1.00 96.01  ? 3483 SER A C     1 
ATOM   13824 O  O     . SER A 1 3483 ? 212.801 149.785 262.388 1.00 95.88  ? 3483 SER A O     1 
ATOM   13825 C  CB    . SER A 1 3483 ? 211.854 146.671 262.481 1.00 89.44  ? 3483 SER A CB    1 
ATOM   13826 O  OG    . SER A 1 3483 ? 213.265 146.722 262.605 1.00 87.66  ? 3483 SER A OG    1 
ATOM   13827 N  N     . ALA A 1 3484 ? 211.310 149.335 260.759 1.00 93.03  ? 3484 ALA A N     1 
ATOM   13828 C  CA    . ALA A 1 3484 ? 211.804 150.422 259.918 1.00 92.90  ? 3484 ALA A CA    1 
ATOM   13829 C  C     . ALA A 1 3484 ? 211.554 151.777 260.566 1.00 95.69  ? 3484 ALA A C     1 
ATOM   13830 O  O     . ALA A 1 3484 ? 212.428 152.653 260.557 1.00 94.02  ? 3484 ALA A O     1 
ATOM   13831 C  CB    . ALA A 1 3484 ? 211.151 150.355 258.538 1.00 88.90  ? 3484 ALA A CB    1 
ATOM   13832 N  N     . GLU A 1 3485 ? 210.360 151.970 261.132 1.00 96.21  ? 3485 GLU A N     1 
ATOM   13833 C  CA    . GLU A 1 3485 ? 210.078 153.205 261.853 1.00 91.06  ? 3485 GLU A CA    1 
ATOM   13834 C  C     . GLU A 1 3485 ? 210.984 153.348 263.068 1.00 92.89  ? 3485 GLU A C     1 
ATOM   13835 O  O     . GLU A 1 3485 ? 211.494 154.438 263.342 1.00 97.40  ? 3485 GLU A O     1 
ATOM   13836 C  CB    . GLU A 1 3485 ? 208.605 153.248 262.259 1.00 93.70  ? 3485 GLU A CB    1 
ATOM   13837 C  CG    . GLU A 1 3485 ? 207.665 153.619 261.121 1.00 95.22  ? 3485 GLU A CG    1 
ATOM   13838 C  CD    . GLU A 1 3485 ? 207.234 152.422 260.295 1.00 99.11  ? 3485 GLU A CD    1 
ATOM   13839 O  OE1   . GLU A 1 3485 ? 207.685 151.298 260.593 1.00 98.53  ? 3485 GLU A OE1   1 
ATOM   13840 O  OE2   . GLU A 1 3485 ? 206.443 152.607 259.346 1.00 100.34 ? 3485 GLU A OE2   1 
ATOM   13841 N  N     . ARG A 1 3486 ? 211.190 152.256 263.809 1.00 95.11  ? 3486 ARG A N     1 
ATOM   13842 C  CA    . ARG A 1 3486 ? 212.168 152.240 264.897 1.00 93.42  ? 3486 ARG A CA    1 
ATOM   13843 C  C     . ARG A 1 3486 ? 213.511 152.800 264.451 1.00 95.05  ? 3486 ARG A C     1 
ATOM   13844 O  O     . ARG A 1 3486 ? 214.014 153.769 265.030 1.00 96.03  ? 3486 ARG A O     1 
ATOM   13845 C  CB    . ARG A 1 3486 ? 212.338 150.813 265.426 1.00 90.05  ? 3486 ARG A CB    1 
ATOM   13846 C  CG    . ARG A 1 3486 ? 213.458 150.652 266.457 1.00 94.29  ? 3486 ARG A CG    1 
ATOM   13847 C  CD    . ARG A 1 3486 ? 213.255 151.365 267.786 1.00 102.70 ? 3486 ARG A CD    1 
ATOM   13848 N  NE    . ARG A 1 3486 ? 212.172 150.811 268.588 1.00 104.91 ? 3486 ARG A NE    1 
ATOM   13849 C  CZ    . ARG A 1 3486 ? 211.692 151.382 269.684 1.00 106.55 ? 3486 ARG A CZ    1 
ATOM   13850 N  NH1   . ARG A 1 3486 ? 212.145 152.548 270.112 1.00 105.24 ? 3486 ARG A NH1   1 
ATOM   13851 N  NH2   . ARG A 1 3486 ? 210.750 150.757 270.383 1.00 102.36 ? 3486 ARG A NH2   1 
ATOM   13852 N  N     . GLU A 1 3487 ? 214.115 152.190 263.427 1.00 97.17  ? 3487 GLU A N     1 
ATOM   13853 C  CA    . GLU A 1 3487 ? 215.470 152.584 263.046 1.00 91.60  ? 3487 GLU A CA    1 
ATOM   13854 C  C     . GLU A 1 3487 ? 215.506 154.007 262.498 1.00 90.00  ? 3487 GLU A C     1 
ATOM   13855 O  O     . GLU A 1 3487 ? 216.414 154.780 262.833 1.00 91.98  ? 3487 GLU A O     1 
ATOM   13856 C  CB    . GLU A 1 3487 ? 216.055 151.593 262.036 1.00 89.16  ? 3487 GLU A CB    1 
ATOM   13857 C  CG    . GLU A 1 3487 ? 215.186 151.307 260.830 1.00 93.24  ? 3487 GLU A CG    1 
ATOM   13858 C  CD    . GLU A 1 3487 ? 215.462 149.945 260.224 1.00 95.77  ? 3487 GLU A CD    1 
ATOM   13859 O  OE1   . GLU A 1 3487 ? 216.194 149.151 260.851 1.00 97.32  ? 3487 GLU A OE1   1 
ATOM   13860 O  OE2   . GLU A 1 3487 ? 214.946 149.669 259.121 1.00 95.32  ? 3487 GLU A OE2   1 
ATOM   13861 N  N     . ARG A 1 3488 ? 214.526 154.384 261.669 1.00 87.73  ? 3488 ARG A N     1 
ATOM   13862 C  CA    . ARG A 1 3488 ? 214.525 155.732 261.107 1.00 90.25  ? 3488 ARG A CA    1 
ATOM   13863 C  C     . ARG A 1 3488 ? 214.355 156.786 262.195 1.00 91.16  ? 3488 ARG A C     1 
ATOM   13864 O  O     . ARG A 1 3488 ? 215.060 157.805 262.200 1.00 92.13  ? 3488 ARG A O     1 
ATOM   13865 C  CB    . ARG A 1 3488 ? 213.424 155.868 260.056 1.00 88.54  ? 3488 ARG A CB    1 
ATOM   13866 C  CG    . ARG A 1 3488 ? 213.321 157.260 259.458 1.00 85.06  ? 3488 ARG A CG    1 
ATOM   13867 C  CD    . ARG A 1 3488 ? 212.031 157.448 258.678 1.00 85.73  ? 3488 ARG A CD    1 
ATOM   13868 N  NE    . ARG A 1 3488 ? 211.559 156.205 258.081 1.00 92.21  ? 3488 ARG A NE    1 
ATOM   13869 C  CZ    . ARG A 1 3488 ? 210.345 156.031 257.579 1.00 87.09  ? 3488 ARG A CZ    1 
ATOM   13870 N  NH1   . ARG A 1 3488 ? 209.450 157.004 257.582 1.00 77.33  ? 3488 ARG A NH1   1 
ATOM   13871 N  NH2   . ARG A 1 3488 ? 210.021 154.850 257.059 1.00 86.94  ? 3488 ARG A NH2   1 
ATOM   13872 N  N     . TRP A 1 3489 ? 213.432 156.555 263.132 1.00 88.30  ? 3489 TRP A N     1 
ATOM   13873 C  CA    . TRP A 1 3489 ? 213.201 157.520 264.198 1.00 88.12  ? 3489 TRP A CA    1 
ATOM   13874 C  C     . TRP A 1 3489 ? 214.391 157.593 265.142 1.00 91.40  ? 3489 TRP A C     1 
ATOM   13875 O  O     . TRP A 1 3489 ? 214.731 158.676 265.626 1.00 94.67  ? 3489 TRP A O     1 
ATOM   13876 C  CB    . TRP A 1 3489 ? 211.923 157.163 264.951 1.00 84.48  ? 3489 TRP A CB    1 
ATOM   13877 C  CG    . TRP A 1 3489 ? 210.701 157.254 264.096 1.00 85.87  ? 3489 TRP A CG    1 
ATOM   13878 C  CD1   . TRP A 1 3489 ? 210.574 157.932 262.920 1.00 85.63  ? 3489 TRP A CD1   1 
ATOM   13879 C  CD2   . TRP A 1 3489 ? 209.431 156.639 264.343 1.00 87.56  ? 3489 TRP A CD2   1 
ATOM   13880 N  NE1   . TRP A 1 3489 ? 209.304 157.784 262.420 1.00 82.78  ? 3489 TRP A NE1   1 
ATOM   13881 C  CE2   . TRP A 1 3489 ? 208.582 156.994 263.276 1.00 86.39  ? 3489 TRP A CE2   1 
ATOM   13882 C  CE3   . TRP A 1 3489 ? 208.930 155.826 265.362 1.00 85.58  ? 3489 TRP A CE3   1 
ATOM   13883 C  CZ2   . TRP A 1 3489 ? 207.262 156.563 263.200 1.00 86.80  ? 3489 TRP A CZ2   1 
ATOM   13884 C  CZ3   . TRP A 1 3489 ? 207.619 155.401 265.285 1.00 88.52  ? 3489 TRP A CZ3   1 
ATOM   13885 C  CH2   . TRP A 1 3489 ? 206.800 155.770 264.211 1.00 89.62  ? 3489 TRP A CH2   1 
ATOM   13886 N  N     . GLU A 1 3490 ? 215.040 156.459 265.412 1.00 92.65  ? 3490 GLU A N     1 
ATOM   13887 C  CA    . GLU A 1 3490 ? 216.248 156.486 266.229 1.00 90.58  ? 3490 GLU A CA    1 
ATOM   13888 C  C     . GLU A 1 3490 ? 217.352 157.286 265.550 1.00 90.54  ? 3490 GLU A C     1 
ATOM   13889 O  O     . GLU A 1 3490 ? 218.042 158.080 266.200 1.00 90.04  ? 3490 GLU A O     1 
ATOM   13890 C  CB    . GLU A 1 3490 ? 216.720 155.063 266.521 1.00 90.78  ? 3490 GLU A CB    1 
ATOM   13891 C  CG    . GLU A 1 3490 ? 215.961 154.374 267.642 1.00 93.72  ? 3490 GLU A CG    1 
ATOM   13892 C  CD    . GLU A 1 3490 ? 216.390 152.932 267.835 1.00 101.50 ? 3490 GLU A CD    1 
ATOM   13893 O  OE1   . GLU A 1 3490 ? 216.433 152.185 266.835 1.00 103.79 ? 3490 GLU A OE1   1 
ATOM   13894 O  OE2   . GLU A 1 3490 ? 216.684 152.546 268.985 1.00 97.79  ? 3490 GLU A OE2   1 
ATOM   13895 N  N     . LYS A 1 3491 ? 217.530 157.098 264.238 1.00 90.19  ? 3491 LYS A N     1 
ATOM   13896 C  CA    . LYS A 1 3491 ? 218.547 157.857 263.518 1.00 92.21  ? 3491 LYS A CA    1 
ATOM   13897 C  C     . LYS A 1 3491 ? 218.247 159.352 263.542 1.00 93.12  ? 3491 LYS A C     1 
ATOM   13898 O  O     . LYS A 1 3491 ? 219.146 160.169 263.764 1.00 91.47  ? 3491 LYS A O     1 
ATOM   13899 C  CB    . LYS A 1 3491 ? 218.661 157.357 262.078 1.00 89.19  ? 3491 LYS A CB    1 
ATOM   13900 C  CG    . LYS A 1 3491 ? 219.323 155.998 261.941 1.00 94.04  ? 3491 LYS A CG    1 
ATOM   13901 C  CD    . LYS A 1 3491 ? 220.650 155.960 262.682 1.00 89.22  ? 3491 LYS A CD    1 
ATOM   13902 C  CE    . LYS A 1 3491 ? 221.118 154.532 262.906 1.00 92.27  ? 3491 LYS A CE    1 
ATOM   13903 N  NZ    . LYS A 1 3491 ? 220.209 153.785 263.817 1.00 91.17  ? 3491 LYS A NZ    1 
ATOM   13904 N  N     . THR A 1 3492 ? 216.987 159.727 263.313 1.00 94.97  ? 3492 THR A N     1 
ATOM   13905 C  CA    . THR A 1 3492 ? 216.637 161.145 263.301 1.00 88.91  ? 3492 THR A CA    1 
ATOM   13906 C  C     . THR A 1 3492 ? 216.743 161.766 264.691 1.00 88.81  ? 3492 THR A C     1 
ATOM   13907 O  O     . THR A 1 3492 ? 217.171 162.918 264.827 1.00 90.56  ? 3492 THR A O     1 
ATOM   13908 C  CB    . THR A 1 3492 ? 215.237 161.337 262.719 1.00 85.59  ? 3492 THR A CB    1 
ATOM   13909 O  OG1   . THR A 1 3492 ? 214.306 160.526 263.441 1.00 92.09  ? 3492 THR A OG1   1 
ATOM   13910 C  CG2   . THR A 1 3492 ? 215.212 160.953 261.248 1.00 80.89  ? 3492 THR A CG2   1 
ATOM   13911 N  N     . SER A 1 3493 ? 216.357 161.027 265.734 1.00 87.77  ? 3493 SER A N     1 
ATOM   13912 C  CA    . SER A 1 3493 ? 216.452 161.540 267.096 1.00 83.46  ? 3493 SER A CA    1 
ATOM   13913 C  C     . SER A 1 3493 ? 217.885 161.574 267.608 1.00 85.86  ? 3493 SER A C     1 
ATOM   13914 O  O     . SER A 1 3493 ? 218.179 162.333 268.536 1.00 84.94  ? 3493 SER A O     1 
ATOM   13915 C  CB    . SER A 1 3493 ? 215.585 160.698 268.033 1.00 82.87  ? 3493 SER A CB    1 
ATOM   13916 O  OG    . SER A 1 3493 ? 215.758 161.089 269.384 1.00 85.50  ? 3493 SER A OG    1 
ATOM   13917 N  N     . GLU A 1 3494 ? 218.776 160.762 267.034 1.00 90.48  ? 3494 GLU A N     1 
ATOM   13918 C  CA    . GLU A 1 3494 ? 220.179 160.804 267.432 1.00 92.03  ? 3494 GLU A CA    1 
ATOM   13919 C  C     . GLU A 1 3494 ? 220.826 162.133 267.069 1.00 91.23  ? 3494 GLU A C     1 
ATOM   13920 O  O     . GLU A 1 3494 ? 221.759 162.574 267.750 1.00 92.26  ? 3494 GLU A O     1 
ATOM   13921 C  CB    . GLU A 1 3494 ? 220.939 159.646 266.784 1.00 95.25  ? 3494 GLU A CB    1 
ATOM   13922 C  CG    . GLU A 1 3494 ? 222.362 159.465 267.287 1.00 97.85  ? 3494 GLU A CG    1 
ATOM   13923 C  CD    . GLU A 1 3494 ? 223.395 159.990 266.308 1.00 103.09 ? 3494 GLU A CD    1 
ATOM   13924 O  OE1   . GLU A 1 3494 ? 223.041 160.208 265.129 1.00 99.16  ? 3494 GLU A OE1   1 
ATOM   13925 O  OE2   . GLU A 1 3494 ? 224.559 160.185 266.716 1.00 106.77 ? 3494 GLU A OE2   1 
ATOM   13926 N  N     . THR A 1 3495 ? 220.344 162.785 266.014 1.00 92.98  ? 3495 THR A N     1 
ATOM   13927 C  CA    . THR A 1 3495 ? 220.911 164.037 265.532 1.00 93.46  ? 3495 THR A CA    1 
ATOM   13928 C  C     . THR A 1 3495 ? 220.240 165.267 266.132 1.00 89.03  ? 3495 THR A C     1 
ATOM   13929 O  O     . THR A 1 3495 ? 220.585 166.388 265.746 1.00 88.75  ? 3495 THR A O     1 
ATOM   13930 C  CB    . THR A 1 3495 ? 220.823 164.099 264.005 1.00 87.44  ? 3495 THR A CB    1 
ATOM   13931 O  OG1   . THR A 1 3495 ? 219.447 164.149 263.605 1.00 77.48  ? 3495 THR A OG1   1 
ATOM   13932 C  CG2   . THR A 1 3495 ? 221.481 162.875 263.385 1.00 85.41  ? 3495 THR A CG2   1 
ATOM   13933 N  N     . PHE A 1 3496 ? 219.300 165.084 267.065 1.00 82.37  ? 3496 PHE A N     1 
ATOM   13934 C  CA    . PHE A 1 3496 ? 218.558 166.211 267.626 1.00 78.70  ? 3496 PHE A CA    1 
ATOM   13935 C  C     . PHE A 1 3496 ? 219.494 167.302 268.131 1.00 82.94  ? 3496 PHE A C     1 
ATOM   13936 O  O     . PHE A 1 3496 ? 219.320 168.485 267.815 1.00 81.92  ? 3496 PHE A O     1 
ATOM   13937 C  CB    . PHE A 1 3496 ? 217.651 165.718 268.752 1.00 79.12  ? 3496 PHE A CB    1 
ATOM   13938 C  CG    . PHE A 1 3496 ? 217.173 166.805 269.672 1.00 76.65  ? 3496 PHE A CG    1 
ATOM   13939 C  CD1   . PHE A 1 3496 ? 216.128 167.633 269.303 1.00 70.93  ? 3496 PHE A CD1   1 
ATOM   13940 C  CD2   . PHE A 1 3496 ? 217.762 166.991 270.912 1.00 70.77  ? 3496 PHE A CD2   1 
ATOM   13941 C  CE1   . PHE A 1 3496 ? 215.683 168.631 270.147 1.00 66.72  ? 3496 PHE A CE1   1 
ATOM   13942 C  CE2   . PHE A 1 3496 ? 217.322 167.987 271.760 1.00 69.31  ? 3496 PHE A CE2   1 
ATOM   13943 C  CZ    . PHE A 1 3496 ? 216.281 168.808 271.377 1.00 69.81  ? 3496 PHE A CZ    1 
ATOM   13944 N  N     . LYS A 1 3497 ? 220.505 166.918 268.913 1.00 82.97  ? 3497 LYS A N     1 
ATOM   13945 C  CA    . LYS A 1 3497 ? 221.474 167.894 269.398 1.00 75.49  ? 3497 LYS A CA    1 
ATOM   13946 C  C     . LYS A 1 3497 ? 222.271 168.495 268.247 1.00 75.53  ? 3497 LYS A C     1 
ATOM   13947 O  O     . LYS A 1 3497 ? 222.687 169.658 268.310 1.00 78.84  ? 3497 LYS A O     1 
ATOM   13948 C  CB    . LYS A 1 3497 ? 222.407 167.240 270.416 1.00 76.07  ? 3497 LYS A CB    1 
ATOM   13949 C  CG    . LYS A 1 3497 ? 221.779 167.026 271.783 1.00 70.91  ? 3497 LYS A CG    1 
ATOM   13950 C  CD    . LYS A 1 3497 ? 222.749 166.349 272.735 1.00 69.05  ? 3497 LYS A CD    1 
ATOM   13951 C  CE    . LYS A 1 3497 ? 224.087 167.070 272.760 1.00 70.53  ? 3497 LYS A CE    1 
ATOM   13952 N  NZ    . LYS A 1 3497 ? 223.939 168.488 273.186 1.00 57.56  ? 3497 LYS A NZ    1 
ATOM   13953 N  N     . ASN A 1 3498 ? 222.493 167.718 267.183 1.00 76.70  ? 3498 ASN A N     1 
ATOM   13954 C  CA    . ASN A 1 3498 ? 223.207 168.247 266.025 1.00 82.12  ? 3498 ASN A CA    1 
ATOM   13955 C  C     . ASN A 1 3498 ? 222.428 169.377 265.363 1.00 80.64  ? 3498 ASN A C     1 
ATOM   13956 O  O     . ASN A 1 3498 ? 223.010 170.402 264.991 1.00 81.24  ? 3498 ASN A O     1 
ATOM   13957 C  CB    . ASN A 1 3498 ? 223.496 167.127 265.024 1.00 87.27  ? 3498 ASN A CB    1 
ATOM   13958 C  CG    . ASN A 1 3498 ? 224.121 167.639 263.744 1.00 86.86  ? 3498 ASN A CG    1 
ATOM   13959 O  OD1   . ASN A 1 3498 ? 223.580 167.445 262.655 1.00 86.08  ? 3498 ASN A OD1   1 
ATOM   13960 N  ND2   . ASN A 1 3498 ? 225.266 168.300 263.867 1.00 82.30  ? 3498 ASN A ND2   1 
ATOM   13961 N  N     . GLN A 1 3499 ? 221.110 169.211 265.200 1.00 78.42  ? 3499 GLN A N     1 
ATOM   13962 C  CA    . GLN A 1 3499 ? 220.303 170.329 264.718 1.00 76.45  ? 3499 GLN A CA    1 
ATOM   13963 C  C     . GLN A 1 3499 ? 220.294 171.479 265.718 1.00 69.33  ? 3499 GLN A C     1 
ATOM   13964 O  O     . GLN A 1 3499 ? 220.401 172.644 265.324 1.00 62.02  ? 3499 GLN A O     1 
ATOM   13965 C  CB    . GLN A 1 3499 ? 218.873 169.890 264.390 1.00 75.34  ? 3499 GLN A CB    1 
ATOM   13966 C  CG    . GLN A 1 3499 ? 218.700 169.110 263.080 1.00 78.75  ? 3499 GLN A CG    1 
ATOM   13967 C  CD    . GLN A 1 3499 ? 219.249 167.702 263.114 1.00 89.31  ? 3499 GLN A CD    1 
ATOM   13968 O  OE1   . GLN A 1 3499 ? 218.797 166.869 263.897 1.00 91.04  ? 3499 GLN A OE1   1 
ATOM   13969 N  NE2   . GLN A 1 3499 ? 220.225 167.423 262.257 1.00 93.90  ? 3499 GLN A NE2   1 
ATOM   13970 N  N     . MET A 1 3500 ? 220.176 171.174 267.018 1.00 72.68  ? 3500 MET A N     1 
ATOM   13971 C  CA    . MET A 1 3500 ? 220.256 172.225 268.036 1.00 66.74  ? 3500 MET A CA    1 
ATOM   13972 C  C     . MET A 1 3500 ? 221.500 173.085 267.866 1.00 63.39  ? 3500 MET A C     1 
ATOM   13973 O  O     . MET A 1 3500 ? 221.437 174.311 268.010 1.00 63.46  ? 3500 MET A O     1 
ATOM   13974 C  CB    . MET A 1 3500 ? 220.235 171.615 269.440 1.00 73.81  ? 3500 MET A CB    1 
ATOM   13975 C  CG    . MET A 1 3500 ? 218.948 170.921 269.845 1.00 75.57  ? 3500 MET A CG    1 
ATOM   13976 S  SD    . MET A 1 3500 ? 217.555 172.065 269.872 1.00 67.22  ? 3500 MET A SD    1 
ATOM   13977 C  CE    . MET A 1 3500 ? 216.735 171.656 268.345 1.00 64.49  ? 3500 MET A CE    1 
ATOM   13978 N  N     . SER A 1 3501 ? 222.638 172.464 267.559 1.00 66.05  ? 3501 SER A N     1 
ATOM   13979 C  CA    . SER A 1 3501 ? 223.887 173.212 267.491 1.00 64.79  ? 3501 SER A CA    1 
ATOM   13980 C  C     . SER A 1 3501 ? 223.974 174.078 266.239 1.00 59.46  ? 3501 SER A C     1 
ATOM   13981 O  O     . SER A 1 3501 ? 224.851 174.945 266.154 1.00 59.76  ? 3501 SER A O     1 
ATOM   13982 C  CB    . SER A 1 3501 ? 225.076 172.253 267.553 1.00 67.60  ? 3501 SER A CB    1 
ATOM   13983 O  OG    . SER A 1 3501 ? 226.269 172.889 267.129 1.00 66.16  ? 3501 SER A OG    1 
ATOM   13984 N  N     . THR A 1 3502 ? 223.089 173.870 265.265 1.00 54.69  ? 3502 THR A N     1 
ATOM   13985 C  CA    . THR A 1 3502 ? 223.215 174.513 263.963 1.00 50.43  ? 3502 THR A CA    1 
ATOM   13986 C  C     . THR A 1 3502 ? 222.043 175.422 263.608 1.00 39.33  ? 3502 THR A C     1 
ATOM   13987 O  O     . THR A 1 3502 ? 222.042 176.005 262.521 1.00 40.81  ? 3502 THR A O     1 
ATOM   13988 C  CB    . THR A 1 3502 ? 223.392 173.456 262.870 1.00 54.00  ? 3502 THR A CB    1 
ATOM   13989 O  OG1   . THR A 1 3502 ? 222.295 172.536 262.911 1.00 57.37  ? 3502 THR A OG1   1 
ATOM   13990 C  CG2   . THR A 1 3502 ? 224.694 172.696 263.069 1.00 50.54  ? 3502 THR A CG2   1 
ATOM   13991 N  N     . ILE A 1 3503 ? 221.047 175.561 264.488 1.00 38.96  ? 3503 ILE A N     1 
ATOM   13992 C  CA    . ILE A 1 3503 ? 219.900 176.400 264.151 1.00 33.17  ? 3503 ILE A CA    1 
ATOM   13993 C  C     . ILE A 1 3503 ? 220.298 177.865 264.037 1.00 29.53  ? 3503 ILE A C     1 
ATOM   13994 O  O     . ILE A 1 3503 ? 219.775 178.588 263.182 1.00 28.83  ? 3503 ILE A O     1 
ATOM   13995 C  CB    . ILE A 1 3503 ? 218.756 176.202 265.164 1.00 36.04  ? 3503 ILE A CB    1 
ATOM   13996 C  CG1   . ILE A 1 3503 ? 218.246 174.766 265.109 1.00 45.12  ? 3503 ILE A CG1   1 
ATOM   13997 C  CG2   . ILE A 1 3503 ? 217.613 177.167 264.901 1.00 34.37  ? 3503 ILE A CG2   1 
ATOM   13998 C  CD1   . ILE A 1 3503 ? 217.314 174.413 266.227 1.00 49.23  ? 3503 ILE A CD1   1 
ATOM   13999 N  N     . ALA A 1 3504 ? 221.227 178.331 264.873 1.00 33.27  ? 3504 ALA A N     1 
ATOM   14000 C  CA    . ALA A 1 3504 ? 221.617 179.737 264.827 1.00 27.68  ? 3504 ALA A CA    1 
ATOM   14001 C  C     . ALA A 1 3504 ? 222.202 180.105 263.469 1.00 28.17  ? 3504 ALA A C     1 
ATOM   14002 O  O     . ALA A 1 3504 ? 221.738 181.048 262.816 1.00 29.93  ? 3504 ALA A O     1 
ATOM   14003 C  CB    . ALA A 1 3504 ? 222.613 180.040 265.945 1.00 27.90  ? 3504 ALA A CB    1 
ATOM   14004 N  N     . GLY A 1 3505 ? 223.204 179.351 263.012 1.00 29.51  ? 3505 GLY A N     1 
ATOM   14005 C  CA    . GLY A 1 3505 ? 223.823 179.657 261.732 1.00 29.57  ? 3505 GLY A CA    1 
ATOM   14006 C  C     . GLY A 1 3505 ? 222.893 179.433 260.554 1.00 22.13  ? 3505 GLY A C     1 
ATOM   14007 O  O     . GLY A 1 3505 ? 222.869 180.231 259.613 1.00 22.87  ? 3505 GLY A O     1 
ATOM   14008 N  N     . ASP A 1 3506 ? 222.125 178.342 260.585 1.00 22.67  ? 3506 ASP A N     1 
ATOM   14009 C  CA    . ASP A 1 3506 ? 221.199 178.053 259.494 1.00 24.63  ? 3506 ASP A CA    1 
ATOM   14010 C  C     . ASP A 1 3506 ? 220.154 179.152 259.363 1.00 24.25  ? 3506 ASP A C     1 
ATOM   14011 O  O     . ASP A 1 3506 ? 219.862 179.623 258.258 1.00 22.94  ? 3506 ASP A O     1 
ATOM   14012 C  CB    . ASP A 1 3506 ? 220.527 176.700 259.724 1.00 26.70  ? 3506 ASP A CB    1 
ATOM   14013 C  CG    . ASP A 1 3506 ? 221.334 175.544 259.169 1.00 46.40  ? 3506 ASP A CG    1 
ATOM   14014 O  OD1   . ASP A 1 3506 ? 222.543 175.727 258.916 1.00 47.59  ? 3506 ASP A OD1   1 
ATOM   14015 O  OD2   . ASP A 1 3506 ? 220.760 174.451 258.986 1.00 56.45  ? 3506 ASP A OD2   1 
ATOM   14016 N  N     . CYS A 1 3507 ? 219.589 179.584 260.492 1.00 22.61  ? 3507 CYS A N     1 
ATOM   14017 C  CA    . CYS A 1 3507 ? 218.588 180.641 260.466 1.00 18.48  ? 3507 CYS A CA    1 
ATOM   14018 C  C     . CYS A 1 3507 ? 219.202 181.973 260.063 1.00 21.40  ? 3507 CYS A C     1 
ATOM   14019 O  O     . CYS A 1 3507 ? 218.563 182.762 259.359 1.00 21.81  ? 3507 CYS A O     1 
ATOM   14020 C  CB    . CYS A 1 3507 ? 217.905 180.748 261.828 1.00 24.06  ? 3507 CYS A CB    1 
ATOM   14021 S  SG    . CYS A 1 3507 ? 216.775 179.388 262.188 1.00 41.84  ? 3507 CYS A SG    1 
ATOM   14022 N  N     . LEU A 1 3508 ? 220.438 182.245 260.490 1.00 19.71  ? 3508 LEU A N     1 
ATOM   14023 C  CA    . LEU A 1 3508 ? 221.112 183.466 260.062 1.00 15.37  ? 3508 LEU A CA    1 
ATOM   14024 C  C     . LEU A 1 3508 ? 221.282 183.488 258.549 1.00 14.39  ? 3508 LEU A C     1 
ATOM   14025 O  O     . LEU A 1 3508 ? 220.982 184.491 257.891 1.00 18.56  ? 3508 LEU A O     1 
ATOM   14026 C  CB    . LEU A 1 3508 ? 222.465 183.586 260.771 1.00 17.75  ? 3508 LEU A CB    1 
ATOM   14027 C  CG    . LEU A 1 3508 ? 223.299 184.865 260.641 1.00 17.69  ? 3508 LEU A CG    1 
ATOM   14028 C  CD1   . LEU A 1 3508 ? 224.171 185.035 261.869 1.00 16.32  ? 3508 LEU A CD1   1 
ATOM   14029 C  CD2   . LEU A 1 3508 ? 224.168 184.852 259.393 1.00 17.04  ? 3508 LEU A CD2   1 
ATOM   14030 N  N     . LEU A 1 3509 ? 221.754 182.377 257.977 1.00 14.35  ? 3509 LEU A N     1 
ATOM   14031 C  CA    . LEU A 1 3509 ? 221.940 182.307 256.532 1.00 12.28  ? 3509 LEU A CA    1 
ATOM   14032 C  C     . LEU A 1 3509 ? 220.613 182.435 255.797 1.00 14.55  ? 3509 LEU A C     1 
ATOM   14033 O  O     . LEU A 1 3509 ? 220.518 183.147 254.788 1.00 16.43  ? 3509 LEU A O     1 
ATOM   14034 C  CB    . LEU A 1 3509 ? 222.634 180.998 256.157 1.00 14.21  ? 3509 LEU A CB    1 
ATOM   14035 C  CG    . LEU A 1 3509 ? 224.081 180.829 256.619 1.00 16.65  ? 3509 LEU A CG    1 
ATOM   14036 C  CD1   . LEU A 1 3509 ? 224.701 179.593 255.993 1.00 22.25  ? 3509 LEU A CD1   1 
ATOM   14037 C  CD2   . LEU A 1 3509 ? 224.893 182.063 256.284 1.00 16.22  ? 3509 LEU A CD2   1 
ATOM   14038 N  N     . SER A 1 3510 ? 219.576 181.753 256.287 1.00 12.83  ? 3510 SER A N     1 
ATOM   14039 C  CA    . SER A 1 3510 ? 218.272 181.819 255.635 1.00 12.71  ? 3510 SER A CA    1 
ATOM   14040 C  C     . SER A 1 3510 ? 217.700 183.229 255.679 1.00 14.87  ? 3510 SER A C     1 
ATOM   14041 O  O     . SER A 1 3510 ? 217.165 183.720 254.678 1.00 21.16  ? 3510 SER A O     1 
ATOM   14042 C  CB    . SER A 1 3510 ? 217.314 180.827 256.292 1.00 16.41  ? 3510 SER A CB    1 
ATOM   14043 O  OG    . SER A 1 3510 ? 217.902 179.542 256.383 1.00 18.14  ? 3510 SER A OG    1 
ATOM   14044 N  N     . ALA A 1 3511 ? 217.807 183.898 256.829 1.00 13.26  ? 3511 ALA A N     1 
ATOM   14045 C  CA    . ALA A 1 3511 ? 217.308 185.262 256.946 1.00 11.21  ? 3511 ALA A CA    1 
ATOM   14046 C  C     . ALA A 1 3511 ? 218.084 186.213 256.047 1.00 13.03  ? 3511 ALA A C     1 
ATOM   14047 O  O     . ALA A 1 3511 ? 217.498 187.102 255.419 1.00 15.90  ? 3511 ALA A O     1 
ATOM   14048 C  CB    . ALA A 1 3511 ? 217.380 185.721 258.399 1.00 13.71  ? 3511 ALA A CB    1 
ATOM   14049 N  N     . ALA A 1 3512 ? 219.408 186.046 255.978 1.00 10.86  ? 3512 ALA A N     1 
ATOM   14050 C  CA    . ALA A 1 3512 ? 220.207 186.884 255.091 1.00 10.10  ? 3512 ALA A CA    1 
ATOM   14051 C  C     . ALA A 1 3512 ? 219.795 186.691 253.641 1.00 11.96  ? 3512 ALA A C     1 
ATOM   14052 O  O     . ALA A 1 3512 ? 219.657 187.665 252.890 1.00 14.61  ? 3512 ALA A O     1 
ATOM   14053 C  CB    . ALA A 1 3512 ? 221.691 186.576 255.277 1.00 11.60  ? 3512 ALA A CB    1 
ATOM   14054 N  N     . PHE A 1 3513 ? 219.579 185.439 253.230 1.00 12.18  ? 3513 PHE A N     1 
ATOM   14055 C  CA    . PHE A 1 3513 ? 219.160 185.180 251.858 1.00 13.42  ? 3513 PHE A CA    1 
ATOM   14056 C  C     . PHE A 1 3513 ? 217.787 185.776 251.576 1.00 13.26  ? 3513 PHE A C     1 
ATOM   14057 O  O     . PHE A 1 3513 ? 217.555 186.333 250.497 1.00 16.63  ? 3513 PHE A O     1 
ATOM   14058 C  CB    . PHE A 1 3513 ? 219.161 183.679 251.577 1.00 12.35  ? 3513 PHE A CB    1 
ATOM   14059 C  CG    . PHE A 1 3513 ? 219.031 183.344 250.122 1.00 12.12  ? 3513 PHE A CG    1 
ATOM   14060 C  CD1   . PHE A 1 3513 ? 220.131 183.406 249.284 1.00 11.18  ? 3513 PHE A CD1   1 
ATOM   14061 C  CD2   . PHE A 1 3513 ? 217.806 182.988 249.587 1.00 9.04   ? 3513 PHE A CD2   1 
ATOM   14062 C  CE1   . PHE A 1 3513 ? 220.014 183.110 247.945 1.00 11.60  ? 3513 PHE A CE1   1 
ATOM   14063 C  CE2   . PHE A 1 3513 ? 217.684 182.690 248.249 1.00 11.44  ? 3513 PHE A CE2   1 
ATOM   14064 C  CZ    . PHE A 1 3513 ? 218.789 182.752 247.426 1.00 13.31  ? 3513 PHE A CZ    1 
ATOM   14065 N  N     . ILE A 1 3514 ? 216.860 185.662 252.530 1.00 9.89   ? 3514 ILE A N     1 
ATOM   14066 C  CA    . ILE A 1 3514 ? 215.518 186.204 252.323 1.00 12.71  ? 3514 ILE A CA    1 
ATOM   14067 C  C     . ILE A 1 3514 ? 215.560 187.721 252.203 1.00 16.14  ? 3514 ILE A C     1 
ATOM   14068 O  O     . ILE A 1 3514 ? 214.926 188.306 251.317 1.00 20.80  ? 3514 ILE A O     1 
ATOM   14069 C  CB    . ILE A 1 3514 ? 214.577 185.758 253.457 1.00 13.83  ? 3514 ILE A CB    1 
ATOM   14070 C  CG1   . ILE A 1 3514 ? 214.350 184.250 253.416 1.00 18.26  ? 3514 ILE A CG1   1 
ATOM   14071 C  CG2   . ILE A 1 3514 ? 213.248 186.480 253.356 1.00 13.32  ? 3514 ILE A CG2   1 
ATOM   14072 C  CD1   . ILE A 1 3514 ? 213.522 183.738 254.572 1.00 19.32  ? 3514 ILE A CD1   1 
ATOM   14073 N  N     . ALA A 1 3515 ? 216.309 188.384 253.083 1.00 15.37  ? 3515 ALA A N     1 
ATOM   14074 C  CA    . ALA A 1 3515 ? 216.258 189.835 253.177 1.00 10.89  ? 3515 ALA A CA    1 
ATOM   14075 C  C     . ALA A 1 3515 ? 217.250 190.552 252.271 1.00 10.92  ? 3515 ALA A C     1 
ATOM   14076 O  O     . ALA A 1 3515 ? 217.170 191.779 252.152 1.00 13.21  ? 3515 ALA A O     1 
ATOM   14077 C  CB    . ALA A 1 3515 ? 216.496 190.275 254.625 1.00 9.22   ? 3515 ALA A CB    1 
ATOM   14078 N  N     . TYR A 1 3516 ? 218.172 189.843 251.629 1.00 8.48   ? 3516 TYR A N     1 
ATOM   14079 C  CA    . TYR A 1 3516 ? 219.184 190.527 250.832 1.00 7.54   ? 3516 TYR A CA    1 
ATOM   14080 C  C     . TYR A 1 3516 ? 219.257 190.060 249.388 1.00 9.85   ? 3516 TYR A C     1 
ATOM   14081 O  O     . TYR A 1 3516 ? 219.459 190.883 248.493 1.00 12.97  ? 3516 TYR A O     1 
ATOM   14082 C  CB    . TYR A 1 3516 ? 220.563 190.358 251.480 1.00 7.76   ? 3516 TYR A CB    1 
ATOM   14083 C  CG    . TYR A 1 3516 ? 220.750 191.141 252.759 1.00 10.83  ? 3516 TYR A CG    1 
ATOM   14084 C  CD1   . TYR A 1 3516 ? 220.649 192.524 252.773 1.00 9.69   ? 3516 TYR A CD1   1 
ATOM   14085 C  CD2   . TYR A 1 3516 ? 221.044 190.495 253.950 1.00 10.74  ? 3516 TYR A CD2   1 
ATOM   14086 C  CE1   . TYR A 1 3516 ? 220.829 193.241 253.937 1.00 7.47   ? 3516 TYR A CE1   1 
ATOM   14087 C  CE2   . TYR A 1 3516 ? 221.222 191.204 255.120 1.00 12.68  ? 3516 TYR A CE2   1 
ATOM   14088 C  CZ    . TYR A 1 3516 ? 221.114 192.576 255.107 1.00 8.84   ? 3516 TYR A CZ    1 
ATOM   14089 O  OH    . TYR A 1 3516 ? 221.292 193.285 256.271 1.00 10.26  ? 3516 TYR A OH    1 
ATOM   14090 N  N     . ALA A 1 3517 ? 219.092 188.766 249.131 1.00 11.82  ? 3517 ALA A N     1 
ATOM   14091 C  CA    . ALA A 1 3517 ? 219.404 188.182 247.834 1.00 9.70   ? 3517 ALA A CA    1 
ATOM   14092 C  C     . ALA A 1 3517 ? 218.250 188.252 246.842 1.00 9.79   ? 3517 ALA A C     1 
ATOM   14093 O  O     . ALA A 1 3517 ? 218.327 187.627 245.780 1.00 13.73  ? 3517 ALA A O     1 
ATOM   14094 C  CB    . ALA A 1 3517 ? 219.843 186.728 248.008 1.00 10.40  ? 3517 ALA A CB    1 
ATOM   14095 N  N     . GLY A 1 3518 ? 217.190 188.997 247.156 1.00 10.11  ? 3518 GLY A N     1 
ATOM   14096 C  CA    . GLY A 1 3518 ? 216.025 189.005 246.286 1.00 7.98   ? 3518 GLY A CA    1 
ATOM   14097 C  C     . GLY A 1 3518 ? 216.291 189.620 244.925 1.00 7.94   ? 3518 GLY A C     1 
ATOM   14098 O  O     . GLY A 1 3518 ? 215.839 189.099 243.902 1.00 10.14  ? 3518 GLY A O     1 
ATOM   14099 N  N     . TYR A 1 3519 ? 217.021 190.735 244.891 1.00 11.13  ? 3519 TYR A N     1 
ATOM   14100 C  CA    . TYR A 1 3519 ? 217.234 191.449 243.638 1.00 8.39   ? 3519 TYR A CA    1 
ATOM   14101 C  C     . TYR A 1 3519 ? 218.263 190.767 242.742 1.00 11.03  ? 3519 TYR A C     1 
ATOM   14102 O  O     . TYR A 1 3519 ? 218.209 190.917 241.517 1.00 10.08  ? 3519 TYR A O     1 
ATOM   14103 C  CB    . TYR A 1 3519 ? 217.666 192.887 243.921 1.00 9.18   ? 3519 TYR A CB    1 
ATOM   14104 C  CG    . TYR A 1 3519 ? 217.916 193.698 242.672 1.00 15.58  ? 3519 TYR A CG    1 
ATOM   14105 C  CD1   . TYR A 1 3519 ? 216.859 194.170 241.907 1.00 15.27  ? 3519 TYR A CD1   1 
ATOM   14106 C  CD2   . TYR A 1 3519 ? 219.207 193.984 242.252 1.00 16.77  ? 3519 TYR A CD2   1 
ATOM   14107 C  CE1   . TYR A 1 3519 ? 217.080 194.904 240.764 1.00 16.17  ? 3519 TYR A CE1   1 
ATOM   14108 C  CE2   . TYR A 1 3519 ? 219.437 194.719 241.109 1.00 18.46  ? 3519 TYR A CE2   1 
ATOM   14109 C  CZ    . TYR A 1 3519 ? 218.370 195.175 240.369 1.00 17.74  ? 3519 TYR A CZ    1 
ATOM   14110 O  OH    . TYR A 1 3519 ? 218.594 195.910 239.229 1.00 28.85  ? 3519 TYR A OH    1 
ATOM   14111 N  N     . PHE A 1 3520 ? 219.196 190.022 243.324 1.00 15.35  ? 3520 PHE A N     1 
ATOM   14112 C  CA    . PHE A 1 3520 ? 220.311 189.475 242.571 1.00 13.09  ? 3520 PHE A CA    1 
ATOM   14113 C  C     . PHE A 1 3520 ? 219.905 188.207 241.823 1.00 14.47  ? 3520 PHE A C     1 
ATOM   14114 O  O     . PHE A 1 3520 ? 218.911 187.552 242.143 1.00 10.75  ? 3520 PHE A O     1 
ATOM   14115 C  CB    . PHE A 1 3520 ? 221.485 189.190 243.506 1.00 13.37  ? 3520 PHE A CB    1 
ATOM   14116 C  CG    . PHE A 1 3520 ? 221.883 190.368 244.344 1.00 15.67  ? 3520 PHE A CG    1 
ATOM   14117 C  CD1   . PHE A 1 3520 ? 222.769 191.314 243.858 1.00 20.89  ? 3520 PHE A CD1   1 
ATOM   14118 C  CD2   . PHE A 1 3520 ? 221.359 190.540 245.613 1.00 15.75  ? 3520 PHE A CD2   1 
ATOM   14119 C  CE1   . PHE A 1 3520 ? 223.134 192.400 244.625 1.00 15.97  ? 3520 PHE A CE1   1 
ATOM   14120 C  CE2   . PHE A 1 3520 ? 221.718 191.626 246.384 1.00 15.58  ? 3520 PHE A CE2   1 
ATOM   14121 C  CZ    . PHE A 1 3520 ? 222.607 192.557 245.889 1.00 17.24  ? 3520 PHE A CZ    1 
ATOM   14122 N  N     . ASP A 1 3521 ? 220.695 187.872 240.805 1.00 21.26  ? 3521 ASP A N     1 
ATOM   14123 C  CA    . ASP A 1 3521 ? 220.466 186.679 240.006 1.00 14.74  ? 3521 ASP A CA    1 
ATOM   14124 C  C     . ASP A 1 3521 ? 221.126 185.467 240.660 1.00 18.19  ? 3521 ASP A C     1 
ATOM   14125 O  O     . ASP A 1 3521 ? 221.673 185.544 241.764 1.00 20.75  ? 3521 ASP A O     1 
ATOM   14126 C  CB    . ASP A 1 3521 ? 220.962 186.897 238.578 1.00 12.65  ? 3521 ASP A CB    1 
ATOM   14127 C  CG    . ASP A 1 3521 ? 222.417 187.308 238.521 1.00 27.15  ? 3521 ASP A CG    1 
ATOM   14128 O  OD1   . ASP A 1 3521 ? 223.036 187.477 239.590 1.00 30.12  ? 3521 ASP A OD1   1 
ATOM   14129 O  OD2   . ASP A 1 3521 ? 222.944 187.472 237.400 1.00 34.79  ? 3521 ASP A OD2   1 
ATOM   14130 N  N     . GLN A 1 3522 ? 221.085 184.330 239.961 1.00 18.85  ? 3522 GLN A N     1 
ATOM   14131 C  CA    . GLN A 1 3522 ? 221.462 183.055 240.570 1.00 20.08  ? 3522 GLN A CA    1 
ATOM   14132 C  C     . GLN A 1 3522 ? 222.911 183.059 241.045 1.00 21.75  ? 3522 GLN A C     1 
ATOM   14133 O  O     . GLN A 1 3522 ? 223.197 182.737 242.204 1.00 22.98  ? 3522 GLN A O     1 
ATOM   14134 C  CB    . GLN A 1 3522 ? 221.244 181.914 239.578 1.00 20.14  ? 3522 GLN A CB    1 
ATOM   14135 C  CG    . GLN A 1 3522 ? 221.530 180.546 240.164 1.00 20.82  ? 3522 GLN A CG    1 
ATOM   14136 C  CD    . GLN A 1 3522 ? 221.260 179.424 239.189 1.00 31.74  ? 3522 GLN A CD    1 
ATOM   14137 O  OE1   . GLN A 1 3522 ? 220.888 179.660 238.042 1.00 34.40  ? 3522 GLN A OE1   1 
ATOM   14138 N  NE2   . GLN A 1 3522 ? 221.445 178.190 239.642 1.00 38.33  ? 3522 GLN A NE2   1 
ATOM   14139 N  N     . GLN A 1 3523 ? 223.841 183.411 240.155 1.00 23.03  ? 3523 GLN A N     1 
ATOM   14140 C  CA    . GLN A 1 3523 ? 225.256 183.325 240.503 1.00 23.39  ? 3523 GLN A CA    1 
ATOM   14141 C  C     . GLN A 1 3523 ? 225.615 184.302 241.613 1.00 21.56  ? 3523 GLN A C     1 
ATOM   14142 O  O     . GLN A 1 3523 ? 226.426 183.984 242.490 1.00 23.25  ? 3523 GLN A O     1 
ATOM   14143 C  CB    . GLN A 1 3523 ? 226.122 183.552 239.259 1.00 23.72  ? 3523 GLN A CB    1 
ATOM   14144 C  CG    . GLN A 1 3523 ? 226.109 184.966 238.707 1.00 35.70  ? 3523 GLN A CG    1 
ATOM   14145 C  CD    . GLN A 1 3523 ? 224.935 185.213 237.779 1.00 38.86  ? 3523 GLN A CD    1 
ATOM   14146 O  OE1   . GLN A 1 3523 ? 223.965 184.455 237.770 1.00 33.08  ? 3523 GLN A OE1   1 
ATOM   14147 N  NE2   . GLN A 1 3523 ? 225.019 186.276 236.987 1.00 34.75  ? 3523 GLN A NE2   1 
ATOM   14148 N  N     . MET A 1 3524 ? 224.997 185.482 241.617 1.00 20.91  ? 3524 MET A N     1 
ATOM   14149 C  CA    . MET A 1 3524 ? 225.308 186.452 242.658 1.00 18.73  ? 3524 MET A CA    1 
ATOM   14150 C  C     . MET A 1 3524 ? 224.714 186.046 244.002 1.00 16.91  ? 3524 MET A C     1 
ATOM   14151 O  O     . MET A 1 3524 ? 225.345 186.250 245.046 1.00 15.46  ? 3524 MET A O     1 
ATOM   14152 C  CB    . MET A 1 3524 ? 224.807 187.837 242.253 1.00 19.03  ? 3524 MET A CB    1 
ATOM   14153 C  CG    . MET A 1 3524 ? 225.250 188.899 243.212 1.00 30.98  ? 3524 MET A CG    1 
ATOM   14154 S  SD    . MET A 1 3524 ? 227.041 189.012 243.089 1.00 46.56  ? 3524 MET A SD    1 
ATOM   14155 C  CE    . MET A 1 3524 ? 227.430 189.696 244.683 1.00 32.09  ? 3524 MET A CE    1 
ATOM   14156 N  N     . ARG A 1 3525 ? 223.511 185.464 243.992 1.00 16.84  ? 3525 ARG A N     1 
ATOM   14157 C  CA    . ARG A 1 3525 ? 222.939 184.899 245.210 1.00 11.78  ? 3525 ARG A CA    1 
ATOM   14158 C  C     . ARG A 1 3525 ? 223.836 183.803 245.768 1.00 14.02  ? 3525 ARG A C     1 
ATOM   14159 O  O     . ARG A 1 3525 ? 224.078 183.732 246.981 1.00 18.24  ? 3525 ARG A O     1 
ATOM   14160 C  CB    . ARG A 1 3525 ? 221.545 184.343 244.918 1.00 10.98  ? 3525 ARG A CB    1 
ATOM   14161 C  CG    . ARG A 1 3525 ? 220.472 185.382 244.659 1.00 8.67   ? 3525 ARG A CG    1 
ATOM   14162 C  CD    . ARG A 1 3525 ? 219.113 184.716 244.538 1.00 8.01   ? 3525 ARG A CD    1 
ATOM   14163 N  NE    . ARG A 1 3525 ? 218.110 185.593 243.948 1.00 7.55   ? 3525 ARG A NE    1 
ATOM   14164 C  CZ    . ARG A 1 3525 ? 216.812 185.326 243.910 1.00 5.68   ? 3525 ARG A CZ    1 
ATOM   14165 N  NH1   . ARG A 1 3525 ? 216.323 184.207 244.416 1.00 7.21   ? 3525 ARG A NH1   1 
ATOM   14166 N  NH2   . ARG A 1 3525 ? 215.985 186.201 243.347 1.00 7.95   ? 3525 ARG A NH2   1 
ATOM   14167 N  N     . GLN A 1 3526 ? 224.338 182.934 244.888 1.00 15.30  ? 3526 GLN A N     1 
ATOM   14168 C  CA    . GLN A 1 3526 ? 225.239 181.875 245.325 1.00 15.20  ? 3526 GLN A CA    1 
ATOM   14169 C  C     . GLN A 1 3526 ? 226.525 182.450 245.902 1.00 17.73  ? 3526 GLN A C     1 
ATOM   14170 O  O     . GLN A 1 3526 ? 227.040 181.947 246.905 1.00 20.91  ? 3526 GLN A O     1 
ATOM   14171 C  CB    . GLN A 1 3526 ? 225.544 180.934 244.160 1.00 16.23  ? 3526 GLN A CB    1 
ATOM   14172 C  CG    . GLN A 1 3526 ? 226.297 179.677 244.554 1.00 13.77  ? 3526 GLN A CG    1 
ATOM   14173 C  CD    . GLN A 1 3526 ? 225.540 178.837 245.563 1.00 23.55  ? 3526 GLN A CD    1 
ATOM   14174 O  OE1   . GLN A 1 3526 ? 225.696 179.009 246.771 1.00 27.74  ? 3526 GLN A OE1   1 
ATOM   14175 N  NE2   . GLN A 1 3526 ? 224.710 177.926 245.071 1.00 24.10  ? 3526 GLN A NE2   1 
ATOM   14176 N  N     . ASN A 1 3527 ? 227.063 183.500 245.276 1.00 15.11  ? 3527 ASN A N     1 
ATOM   14177 C  CA    . ASN A 1 3527 ? 228.278 184.125 245.789 1.00 14.36  ? 3527 ASN A CA    1 
ATOM   14178 C  C     . ASN A 1 3527 ? 228.056 184.727 247.170 1.00 15.04  ? 3527 ASN A C     1 
ATOM   14179 O  O     . ASN A 1 3527 ? 228.902 184.584 248.061 1.00 21.66  ? 3527 ASN A O     1 
ATOM   14180 C  CB    . ASN A 1 3527 ? 228.769 185.195 244.814 1.00 21.91  ? 3527 ASN A CB    1 
ATOM   14181 C  CG    . ASN A 1 3527 ? 229.442 184.606 243.593 1.00 31.21  ? 3527 ASN A CG    1 
ATOM   14182 O  OD1   . ASN A 1 3527 ? 229.618 183.392 243.491 1.00 29.80  ? 3527 ASN A OD1   1 
ATOM   14183 N  ND2   . ASN A 1 3527 ? 229.822 185.465 242.657 1.00 29.25  ? 3527 ASN A ND2   1 
ATOM   14184 N  N     . LEU A 1 3528 ? 226.923 185.408 247.366 1.00 14.50  ? 3528 LEU A N     1 
ATOM   14185 C  CA    . LEU A 1 3528 ? 226.621 185.975 248.677 1.00 9.85   ? 3528 LEU A CA    1 
ATOM   14186 C  C     . LEU A 1 3528 ? 226.472 184.885 249.731 1.00 12.23  ? 3528 LEU A C     1 
ATOM   14187 O  O     . LEU A 1 3528 ? 226.994 185.011 250.849 1.00 15.52  ? 3528 LEU A O     1 
ATOM   14188 C  CB    . LEU A 1 3528 ? 225.353 186.825 248.604 1.00 8.37   ? 3528 LEU A CB    1 
ATOM   14189 C  CG    . LEU A 1 3528 ? 225.486 188.204 247.961 1.00 10.55  ? 3528 LEU A CG    1 
ATOM   14190 C  CD1   . LEU A 1 3528 ? 224.125 188.862 247.820 1.00 10.51  ? 3528 LEU A CD1   1 
ATOM   14191 C  CD2   . LEU A 1 3528 ? 226.420 189.080 248.778 1.00 9.95   ? 3528 LEU A CD2   1 
ATOM   14192 N  N     . PHE A 1 3529 ? 225.765 183.803 249.393 1.00 12.99  ? 3529 PHE A N     1 
ATOM   14193 C  CA    . PHE A 1 3529 ? 225.608 182.705 250.339 1.00 14.70  ? 3529 PHE A CA    1 
ATOM   14194 C  C     . PHE A 1 3529 ? 226.951 182.070 250.672 1.00 15.91  ? 3529 PHE A C     1 
ATOM   14195 O  O     . PHE A 1 3529 ? 227.212 181.725 251.829 1.00 17.25  ? 3529 PHE A O     1 
ATOM   14196 C  CB    . PHE A 1 3529 ? 224.641 181.660 249.782 1.00 16.06  ? 3529 PHE A CB    1 
ATOM   14197 C  CG    . PHE A 1 3529 ? 223.969 180.837 250.841 1.00 14.40  ? 3529 PHE A CG    1 
ATOM   14198 C  CD1   . PHE A 1 3529 ? 222.828 181.297 251.475 1.00 14.43  ? 3529 PHE A CD1   1 
ATOM   14199 C  CD2   . PHE A 1 3529 ? 224.478 179.602 251.205 1.00 15.65  ? 3529 PHE A CD2   1 
ATOM   14200 C  CE1   . PHE A 1 3529 ? 222.206 180.544 252.449 1.00 14.14  ? 3529 PHE A CE1   1 
ATOM   14201 C  CE2   . PHE A 1 3529 ? 223.861 178.843 252.180 1.00 16.30  ? 3529 PHE A CE2   1 
ATOM   14202 C  CZ    . PHE A 1 3529 ? 222.724 179.314 252.802 1.00 16.85  ? 3529 PHE A CZ    1 
ATOM   14203 N  N     . THR A 1 3530 ? 227.816 181.910 249.668 1.00 16.16  ? 3530 THR A N     1 
ATOM   14204 C  CA    . THR A 1 3530 ? 229.141 181.349 249.905 1.00 17.79  ? 3530 THR A CA    1 
ATOM   14205 C  C     . THR A 1 3530 ? 229.966 182.246 250.816 1.00 16.84  ? 3530 THR A C     1 
ATOM   14206 O  O     . THR A 1 3530 ? 230.669 181.758 251.706 1.00 17.54  ? 3530 THR A O     1 
ATOM   14207 C  CB    . THR A 1 3530 ? 229.861 181.129 248.575 1.00 19.23  ? 3530 THR A CB    1 
ATOM   14208 O  OG1   . THR A 1 3530 ? 229.016 180.385 247.689 1.00 24.37  ? 3530 THR A OG1   1 
ATOM   14209 C  CG2   . THR A 1 3530 ? 231.156 180.363 248.791 1.00 18.83  ? 3530 THR A CG2   1 
ATOM   14210 N  N     . THR A 1 3531 ? 229.881 183.560 250.599 1.00 15.33  ? 3531 THR A N     1 
ATOM   14211 C  CA    . THR A 1 3531 ? 230.653 184.519 251.418 1.00 14.00  ? 3531 THR A CA    1 
ATOM   14212 C  C     . THR A 1 3531 ? 230.208 184.423 252.863 1.00 15.46  ? 3531 THR A C     1 
ATOM   14213 O  O     . THR A 1 3531 ? 231.076 184.209 253.736 1.00 20.86  ? 3531 THR A O     1 
ATOM   14214 C  CB    . THR A 1 3531 ? 230.466 185.929 250.861 1.00 15.41  ? 3531 THR A CB    1 
ATOM   14215 O  OG1   . THR A 1 3531 ? 230.930 185.863 249.516 1.00 13.82  ? 3531 THR A OG1   1 
ATOM   14216 C  CG2   . THR A 1 3531 ? 231.255 186.970 251.636 1.00 16.04  ? 3531 THR A CG2   1 
ATOM   14217 N  N     . TRP A 1 3532 ? 228.904 184.569 253.114 1.00 13.55  ? 3532 TRP A N     1 
ATOM   14218 C  CA    . TRP A 1 3532 ? 228.379 184.537 254.501 1.00 14.83  ? 3532 TRP A CA    1 
ATOM   14219 C  C     . TRP A 1 3532 ? 228.732 183.200 255.150 1.00 16.19  ? 3532 TRP A C     1 
ATOM   14220 O  O     . TRP A 1 3532 ? 229.165 183.197 256.323 1.00 18.74  ? 3532 TRP A O     1 
ATOM   14221 C  CB    . TRP A 1 3532 ? 226.860 184.756 254.501 1.00 12.88  ? 3532 TRP A CB    1 
ATOM   14222 C  CG    . TRP A 1 3532 ? 226.409 185.999 253.783 1.00 11.46  ? 3532 TRP A CG    1 
ATOM   14223 C  CD1   . TRP A 1 3532 ? 227.075 187.185 253.682 1.00 12.99  ? 3532 TRP A CD1   1 
ATOM   14224 C  CD2   . TRP A 1 3532 ? 225.174 186.170 253.053 1.00 9.86   ? 3532 TRP A CD2   1 
ATOM   14225 N  NE1   . TRP A 1 3532 ? 226.343 188.080 252.949 1.00 11.88  ? 3532 TRP A NE1   1 
ATOM   14226 C  CE2   . TRP A 1 3532 ? 225.175 187.488 252.548 1.00 10.19  ? 3532 TRP A CE2   1 
ATOM   14227 C  CE3   . TRP A 1 3532 ? 224.078 185.345 252.780 1.00 8.86   ? 3532 TRP A CE3   1 
ATOM   14228 C  CZ2   . TRP A 1 3532 ? 224.122 187.992 251.789 1.00 8.53   ? 3532 TRP A CZ2   1 
ATOM   14229 C  CZ3   . TRP A 1 3532 ? 223.039 185.845 252.028 1.00 10.19  ? 3532 TRP A CZ3   1 
ATOM   14230 C  CH2   . TRP A 1 3532 ? 223.062 187.151 251.541 1.00 8.40   ? 3532 TRP A CH2   1 
ATOM   14231 N  N     . SER A 1 3533 ? 228.562 182.102 254.410 1.00 18.59  ? 3533 SER A N     1 
ATOM   14232 C  CA    . SER A 1 3533 ? 228.834 180.749 254.962 1.00 21.76  ? 3533 SER A CA    1 
ATOM   14233 C  C     . SER A 1 3533 ? 230.295 180.655 255.420 1.00 23.77  ? 3533 SER A C     1 
ATOM   14234 O  O     . SER A 1 3533 ? 230.536 180.142 256.534 1.00 21.43  ? 3533 SER A O     1 
ATOM   14235 C  CB    . SER A 1 3533 ? 228.512 179.684 253.946 1.00 21.56  ? 3533 SER A CB    1 
ATOM   14236 O  OG    . SER A 1 3533 ? 227.151 179.754 253.546 1.00 23.72  ? 3533 SER A OG    1 
ATOM   14237 N  N     . HIS A 1 3534 ? 231.225 181.138 254.593 1.00 24.35  ? 3534 HIS A N     1 
ATOM   14238 C  CA    . HIS A 1 3534 ? 232.670 181.082 254.941 1.00 25.15  ? 3534 HIS A CA    1 
ATOM   14239 C  C     . HIS A 1 3534 ? 232.913 181.883 256.224 1.00 28.26  ? 3534 HIS A C     1 
ATOM   14240 O  O     . HIS A 1 3534 ? 233.637 181.397 257.118 1.00 32.02  ? 3534 HIS A O     1 
ATOM   14241 C  CB    . HIS A 1 3534 ? 233.523 181.598 253.778 1.00 27.46  ? 3534 HIS A CB    1 
ATOM   14242 C  CG    . HIS A 1 3534 ? 234.961 181.784 254.129 1.00 45.22  ? 3534 HIS A CG    1 
ATOM   14243 N  ND1   . HIS A 1 3534 ? 235.757 182.745 253.542 1.00 51.42  ? 3534 HIS A ND1   1 
ATOM   14244 C  CD2   . HIS A 1 3534 ? 235.743 181.143 255.008 1.00 45.46  ? 3534 HIS A CD2   1 
ATOM   14245 C  CE1   . HIS A 1 3534 ? 236.976 182.675 254.055 1.00 53.47  ? 3534 HIS A CE1   1 
ATOM   14246 N  NE2   . HIS A 1 3534 ? 236.990 181.710 254.948 1.00 50.76  ? 3534 HIS A NE2   1 
ATOM   14247 N  N     . HIS A 1 3535 ? 232.318 183.074 256.313 1.00 26.58  ? 3535 HIS A N     1 
ATOM   14248 C  CA    . HIS A 1 3535 ? 232.523 183.938 257.508 1.00 20.96  ? 3535 HIS A CA    1 
ATOM   14249 C  C     . HIS A 1 3535 ? 232.055 183.190 258.758 1.00 20.52  ? 3535 HIS A C     1 
ATOM   14250 O  O     . HIS A 1 3535 ? 232.771 183.210 259.780 1.00 28.56  ? 3535 HIS A O     1 
ATOM   14251 C  CB    . HIS A 1 3535 ? 231.788 185.272 257.343 1.00 18.68  ? 3535 HIS A CB    1 
ATOM   14252 C  CG    . HIS A 1 3535 ? 231.945 186.185 258.513 1.00 20.34  ? 3535 HIS A CG    1 
ATOM   14253 N  ND1   . HIS A 1 3535 ? 231.083 186.181 259.588 1.00 16.81  ? 3535 HIS A ND1   1 
ATOM   14254 C  CD2   . HIS A 1 3535 ? 232.861 187.123 258.777 1.00 20.53  ? 3535 HIS A CD2   1 
ATOM   14255 C  CE1   . HIS A 1 3535 ? 231.476 187.091 260.465 1.00 19.97  ? 3535 HIS A CE1   1 
ATOM   14256 N  NE2   . HIS A 1 3535 ? 232.554 187.677 259.992 1.00 23.18  ? 3535 HIS A NE2   1 
ATOM   14257 N  N     . LEU A 1 3536 ? 230.889 182.546 258.676 1.00 19.32  ? 3536 LEU A N     1 
ATOM   14258 C  CA    . LEU A 1 3536 ? 230.361 181.773 259.830 1.00 20.17  ? 3536 LEU A CA    1 
ATOM   14259 C  C     . LEU A 1 3536 ? 231.366 180.666 260.177 1.00 26.09  ? 3536 LEU A C     1 
ATOM   14260 O  O     . LEU A 1 3536 ? 231.656 180.485 261.378 1.00 28.08  ? 3536 LEU A O     1 
ATOM   14261 C  CB    . LEU A 1 3536 ? 228.985 181.200 259.494 1.00 24.24  ? 3536 LEU A CB    1 
ATOM   14262 C  CG    . LEU A 1 3536 ? 227.868 182.223 259.269 1.00 16.80  ? 3536 LEU A CG    1 
ATOM   14263 C  CD1   . LEU A 1 3536 ? 226.509 181.551 259.350 1.00 21.76  ? 3536 LEU A CD1   1 
ATOM   14264 C  CD2   . LEU A 1 3536 ? 227.965 183.356 260.273 1.00 17.46  ? 3536 LEU A CD2   1 
ATOM   14265 N  N     . GLN A 1 3537 ? 231.874 179.960 259.164 1.00 31.28  ? 3537 GLN A N     1 
ATOM   14266 C  CA    . GLN A 1 3537 ? 232.900 178.912 259.399 1.00 28.05  ? 3537 GLN A CA    1 
ATOM   14267 C  C     . GLN A 1 3537 ? 234.123 179.558 260.059 1.00 30.09  ? 3537 GLN A C     1 
ATOM   14268 O  O     . GLN A 1 3537 ? 234.590 179.030 261.090 1.00 39.63  ? 3537 GLN A O     1 
ATOM   14269 C  CB    . GLN A 1 3537 ? 233.340 178.264 258.088 1.00 27.69  ? 3537 GLN A CB    1 
ATOM   14270 C  CG    . GLN A 1 3537 ? 232.261 177.434 257.405 1.00 35.40  ? 3537 GLN A CG    1 
ATOM   14271 C  CD    . GLN A 1 3537 ? 232.738 176.781 256.127 1.00 31.64  ? 3537 GLN A CD    1 
ATOM   14272 O  OE1   . GLN A 1 3537 ? 233.892 176.941 255.715 1.00 27.66  ? 3537 GLN A OE1   1 
ATOM   14273 N  NE2   . GLN A 1 3537 ? 231.850 176.036 255.485 1.00 32.27  ? 3537 GLN A NE2   1 
ATOM   14274 N  N     . GLN A 1 3538 ? 234.615 180.657 259.482 1.00 29.07  ? 3538 GLN A N     1 
ATOM   14275 C  CA    . GLN A 1 3538 ? 235.798 181.307 260.025 1.00 29.71  ? 3538 GLN A CA    1 
ATOM   14276 C  C     . GLN A 1 3538 ? 235.583 181.798 261.451 1.00 33.81  ? 3538 GLN A C     1 
ATOM   14277 O  O     . GLN A 1 3538 ? 236.560 182.063 262.157 1.00 46.12  ? 3538 GLN A O     1 
ATOM   14278 C  CB    . GLN A 1 3538 ? 236.196 182.464 259.108 1.00 33.15  ? 3538 GLN A CB    1 
ATOM   14279 C  CG    . GLN A 1 3538 ? 237.605 182.983 259.287 1.00 41.07  ? 3538 GLN A CG    1 
ATOM   14280 C  CD    . GLN A 1 3538 ? 237.995 183.943 258.184 1.00 49.18  ? 3538 GLN A CD    1 
ATOM   14281 O  OE1   . GLN A 1 3538 ? 237.251 184.135 257.223 1.00 43.49  ? 3538 GLN A OE1   1 
ATOM   14282 N  NE2   . GLN A 1 3538 ? 239.171 184.542 258.308 1.00 61.74  ? 3538 GLN A NE2   1 
ATOM   14283 N  N     . ALA A 1 3539 ? 234.331 181.915 261.890 1.00 31.74  ? 3539 ALA A N     1 
ATOM   14284 C  CA    . ALA A 1 3539 ? 234.003 182.327 263.247 1.00 33.71  ? 3539 ALA A CA    1 
ATOM   14285 C  C     . ALA A 1 3539 ? 233.519 181.171 264.110 1.00 33.01  ? 3539 ALA A C     1 
ATOM   14286 O  O     . ALA A 1 3539 ? 233.016 181.407 265.213 1.00 36.75  ? 3539 ALA A O     1 
ATOM   14287 C  CB    . ALA A 1 3539 ? 232.950 183.436 263.222 1.00 35.96  ? 3539 ALA A CB    1 
ATOM   14288 N  N     . ASN A 1 3540 ? 233.661 179.932 263.634 1.00 31.39  ? 3540 ASN A N     1 
ATOM   14289 C  CA    . ASN A 1 3540 ? 233.239 178.737 264.371 1.00 34.15  ? 3540 ASN A CA    1 
ATOM   14290 C  C     . ASN A 1 3540 ? 231.755 178.786 264.725 1.00 30.88  ? 3540 ASN A C     1 
ATOM   14291 O  O     . ASN A 1 3540 ? 231.357 178.498 265.855 1.00 33.82  ? 3540 ASN A O     1 
ATOM   14292 C  CB    . ASN A 1 3540 ? 234.089 178.526 265.625 1.00 39.47  ? 3540 ASN A CB    1 
ATOM   14293 C  CG    . ASN A 1 3540 ? 235.472 178.004 265.307 1.00 48.15  ? 3540 ASN A CG    1 
ATOM   14294 O  OD1   . ASN A 1 3540 ? 235.963 178.155 264.189 1.00 44.32  ? 3540 ASN A OD1   1 
ATOM   14295 N  ND2   . ASN A 1 3540 ? 236.110 177.384 266.292 1.00 54.61  ? 3540 ASN A ND2   1 
ATOM   14296 N  N     . ILE A 1 3541 ? 230.929 179.151 263.752 1.00 31.24  ? 3541 ILE A N     1 
ATOM   14297 C  CA    . ILE A 1 3541 ? 229.480 179.126 263.894 1.00 32.08  ? 3541 ILE A CA    1 
ATOM   14298 C  C     . ILE A 1 3541 ? 228.960 177.915 263.135 1.00 36.98  ? 3541 ILE A C     1 
ATOM   14299 O  O     . ILE A 1 3541 ? 229.138 177.814 261.914 1.00 36.28  ? 3541 ILE A O     1 
ATOM   14300 C  CB    . ILE A 1 3541 ? 228.843 180.425 263.381 1.00 26.96  ? 3541 ILE A CB    1 
ATOM   14301 C  CG1   . ILE A 1 3541 ? 229.244 181.593 264.279 1.00 27.64  ? 3541 ILE A CG1   1 
ATOM   14302 C  CG2   . ILE A 1 3541 ? 227.331 180.288 263.324 1.00 24.68  ? 3541 ILE A CG2   1 
ATOM   14303 C  CD1   . ILE A 1 3541 ? 228.746 182.927 263.800 1.00 25.76  ? 3541 ILE A CD1   1 
ATOM   14304 N  N     . GLN A 1 3542 ? 228.320 176.996 263.852 1.00 37.52  ? 3542 GLN A N     1 
ATOM   14305 C  CA    . GLN A 1 3542 ? 227.893 175.735 263.262 1.00 39.68  ? 3542 GLN A CA    1 
ATOM   14306 C  C     . GLN A 1 3542 ? 226.682 175.947 262.364 1.00 46.70  ? 3542 GLN A C     1 
ATOM   14307 O  O     . GLN A 1 3542 ? 225.688 176.555 262.777 1.00 43.42  ? 3542 GLN A O     1 
ATOM   14308 C  CB    . GLN A 1 3542 ? 227.564 174.721 264.357 1.00 42.49  ? 3542 GLN A CB    1 
ATOM   14309 C  CG    . GLN A 1 3542 ? 228.761 174.285 265.186 1.00 48.68  ? 3542 GLN A CG    1 
ATOM   14310 C  CD    . GLN A 1 3542 ? 229.927 173.828 264.335 1.00 51.00  ? 3542 GLN A CD    1 
ATOM   14311 O  OE1   . GLN A 1 3542 ? 229.887 172.756 263.730 1.00 47.19  ? 3542 GLN A OE1   1 
ATOM   14312 N  NE2   . GLN A 1 3542 ? 230.979 174.639 264.285 1.00 48.38  ? 3542 GLN A NE2   1 
ATOM   14313 N  N     . PHE A 1 3543 ? 226.768 175.442 261.136 1.00 42.54  ? 3543 PHE A N     1 
ATOM   14314 C  CA    . PHE A 1 3543 ? 225.641 175.453 260.215 1.00 37.13  ? 3543 PHE A CA    1 
ATOM   14315 C  C     . PHE A 1 3543 ? 225.718 174.211 259.341 1.00 46.98  ? 3543 PHE A C     1 
ATOM   14316 O  O     . PHE A 1 3543 ? 226.795 173.651 259.116 1.00 51.68  ? 3543 PHE A O     1 
ATOM   14317 C  CB    . PHE A 1 3543 ? 225.612 176.731 259.365 1.00 32.30  ? 3543 PHE A CB    1 
ATOM   14318 C  CG    . PHE A 1 3543 ? 226.795 176.886 258.454 1.00 36.57  ? 3543 PHE A CG    1 
ATOM   14319 C  CD1   . PHE A 1 3543 ? 227.967 177.460 258.913 1.00 31.91  ? 3543 PHE A CD1   1 
ATOM   14320 C  CD2   . PHE A 1 3543 ? 226.731 176.474 257.133 1.00 42.16  ? 3543 PHE A CD2   1 
ATOM   14321 C  CE1   . PHE A 1 3543 ? 229.055 177.610 258.077 1.00 30.15  ? 3543 PHE A CE1   1 
ATOM   14322 C  CE2   . PHE A 1 3543 ? 227.816 176.622 256.294 1.00 33.50  ? 3543 PHE A CE2   1 
ATOM   14323 C  CZ    . PHE A 1 3543 ? 228.979 177.190 256.767 1.00 30.05  ? 3543 PHE A CZ    1 
ATOM   14324 N  N     . ARG A 1 3544 ? 224.558 173.785 258.849 1.00 51.49  ? 3544 ARG A N     1 
ATOM   14325 C  CA    . ARG A 1 3544 ? 224.437 172.551 258.080 1.00 54.81  ? 3544 ARG A CA    1 
ATOM   14326 C  C     . ARG A 1 3544 ? 224.570 172.876 256.596 1.00 54.92  ? 3544 ARG A C     1 
ATOM   14327 O  O     . ARG A 1 3544 ? 223.660 173.453 255.992 1.00 63.38  ? 3544 ARG A O     1 
ATOM   14328 C  CB    . ARG A 1 3544 ? 223.111 171.865 258.399 1.00 50.63  ? 3544 ARG A CB    1 
ATOM   14329 C  CG    . ARG A 1 3544 ? 223.067 171.331 259.823 1.00 56.49  ? 3544 ARG A CG    1 
ATOM   14330 C  CD    . ARG A 1 3544 ? 221.785 170.586 260.148 1.00 70.71  ? 3544 ARG A CD    1 
ATOM   14331 N  NE    . ARG A 1 3544 ? 220.639 171.486 260.203 1.00 69.84  ? 3544 ARG A NE    1 
ATOM   14332 C  CZ    . ARG A 1 3544 ? 219.630 171.470 259.344 1.00 61.63  ? 3544 ARG A CZ    1 
ATOM   14333 N  NH1   . ARG A 1 3544 ? 219.557 170.570 258.380 1.00 65.36  ? 3544 ARG A NH1   1 
ATOM   14334 N  NH2   . ARG A 1 3544 ? 218.659 172.371 259.467 1.00 54.82  ? 3544 ARG A NH2   1 
ATOM   14335 N  N     . THR A 1 3545 ? 225.711 172.502 256.011 1.00 58.36  ? 3545 THR A N     1 
ATOM   14336 C  CA    . THR A 1 3545 ? 226.027 172.882 254.637 1.00 65.64  ? 3545 THR A CA    1 
ATOM   14337 C  C     . THR A 1 3545 ? 225.264 172.054 253.609 1.00 64.05  ? 3545 THR A C     1 
ATOM   14338 O  O     . THR A 1 3545 ? 224.903 172.577 252.548 1.00 60.60  ? 3545 THR A O     1 
ATOM   14339 C  CB    . THR A 1 3545 ? 227.534 172.751 254.398 1.00 59.68  ? 3545 THR A CB    1 
ATOM   14340 O  OG1   . THR A 1 3545 ? 228.243 173.508 255.388 1.00 55.13  ? 3545 THR A OG1   1 
ATOM   14341 C  CG2   . THR A 1 3545 ? 227.911 173.271 253.020 1.00 55.67  ? 3545 THR A CG2   1 
ATOM   14342 N  N     . ASP A 1 3546 ? 225.002 170.778 253.901 1.00 67.51  ? 3546 ASP A N     1 
ATOM   14343 C  CA    . ASP A 1 3546 ? 224.408 169.893 252.904 1.00 70.99  ? 3546 ASP A CA    1 
ATOM   14344 C  C     . ASP A 1 3546 ? 223.004 170.331 252.504 1.00 75.38  ? 3546 ASP A C     1 
ATOM   14345 O  O     . ASP A 1 3546 ? 222.622 170.185 251.337 1.00 78.16  ? 3546 ASP A O     1 
ATOM   14346 C  CB    . ASP A 1 3546 ? 224.385 168.456 253.427 1.00 71.88  ? 3546 ASP A CB    1 
ATOM   14347 C  CG    . ASP A 1 3546 ? 223.668 168.329 254.758 1.00 75.43  ? 3546 ASP A CG    1 
ATOM   14348 O  OD1   . ASP A 1 3546 ? 223.289 169.369 255.337 1.00 74.04  ? 3546 ASP A OD1   1 
ATOM   14349 O  OD2   . ASP A 1 3546 ? 223.482 167.186 255.225 1.00 81.56  ? 3546 ASP A OD2   1 
ATOM   14350 N  N     . ILE A 1 3547 ? 222.225 170.864 253.447 1.00 72.48  ? 3547 ILE A N     1 
ATOM   14351 C  CA    . ILE A 1 3547 ? 220.844 171.233 253.152 1.00 64.21  ? 3547 ILE A CA    1 
ATOM   14352 C  C     . ILE A 1 3547 ? 220.805 172.459 252.243 1.00 59.25  ? 3547 ILE A C     1 
ATOM   14353 O  O     . ILE A 1 3547 ? 221.615 173.388 252.352 1.00 52.87  ? 3547 ILE A O     1 
ATOM   14354 C  CB    . ILE A 1 3547 ? 220.067 171.474 254.455 1.00 65.18  ? 3547 ILE A CB    1 
ATOM   14355 C  CG1   . ILE A 1 3547 ? 220.088 170.211 255.313 1.00 72.87  ? 3547 ILE A CG1   1 
ATOM   14356 C  CG2   . ILE A 1 3547 ? 218.630 171.888 254.173 1.00 53.38  ? 3547 ILE A CG2   1 
ATOM   14357 C  CD1   . ILE A 1 3547 ? 219.442 169.011 254.654 1.00 74.50  ? 3547 ILE A CD1   1 
ATOM   14358 N  N     . ALA A 1 3548 ? 219.844 172.453 251.323 1.00 51.49  ? 3548 ALA A N     1 
ATOM   14359 C  CA    . ALA A 1 3548 ? 219.620 173.550 250.396 1.00 42.54  ? 3548 ALA A CA    1 
ATOM   14360 C  C     . ALA A 1 3548 ? 218.672 174.571 251.010 1.00 38.62  ? 3548 ALA A C     1 
ATOM   14361 O  O     . ALA A 1 3548 ? 217.906 174.260 251.926 1.00 40.21  ? 3548 ALA A O     1 
ATOM   14362 C  CB    . ALA A 1 3548 ? 219.050 173.045 249.068 1.00 43.35  ? 3548 ALA A CB    1 
ATOM   14363 N  N     . ARG A 1 3549 ? 218.740 175.801 250.496 1.00 29.22  ? 3549 ARG A N     1 
ATOM   14364 C  CA    . ARG A 1 3549 ? 217.912 176.878 251.029 1.00 26.13  ? 3549 ARG A CA    1 
ATOM   14365 C  C     . ARG A 1 3549 ? 216.429 176.598 250.818 1.00 27.65  ? 3549 ARG A C     1 
ATOM   14366 O  O     . ARG A 1 3549 ? 215.612 176.819 251.721 1.00 31.47  ? 3549 ARG A O     1 
ATOM   14367 C  CB    . ARG A 1 3549 ? 218.298 178.203 250.371 1.00 22.58  ? 3549 ARG A CB    1 
ATOM   14368 C  CG    . ARG A 1 3549 ? 219.789 178.379 250.163 1.00 19.05  ? 3549 ARG A CG    1 
ATOM   14369 C  CD    . ARG A 1 3549 ? 220.113 179.787 249.705 1.00 16.71  ? 3549 ARG A CD    1 
ATOM   14370 N  NE    . ARG A 1 3549 ? 220.101 179.913 248.253 1.00 14.28  ? 3549 ARG A NE    1 
ATOM   14371 C  CZ    . ARG A 1 3549 ? 221.155 179.713 247.474 1.00 16.39  ? 3549 ARG A CZ    1 
ATOM   14372 N  NH1   . ARG A 1 3549 ? 222.325 179.351 247.974 1.00 15.64  ? 3549 ARG A NH1   1 
ATOM   14373 N  NH2   . ARG A 1 3549 ? 221.032 179.880 246.160 1.00 14.45  ? 3549 ARG A NH2   1 
ATOM   14374 N  N     . THR A 1 3550 ? 216.063 176.118 249.628 1.00 31.73  ? 3550 THR A N     1 
ATOM   14375 C  CA    . THR A 1 3550 ? 214.656 175.899 249.310 1.00 31.07  ? 3550 THR A CA    1 
ATOM   14376 C  C     . THR A 1 3550 ? 214.045 174.822 250.197 1.00 28.86  ? 3550 THR A C     1 
ATOM   14377 O  O     . THR A 1 3550 ? 212.908 174.962 250.659 1.00 25.30  ? 3550 THR A O     1 
ATOM   14378 C  CB    . THR A 1 3550 ? 214.508 175.523 247.836 1.00 27.70  ? 3550 THR A CB    1 
ATOM   14379 O  OG1   . THR A 1 3550 ? 215.487 174.535 247.494 1.00 40.14  ? 3550 THR A OG1   1 
ATOM   14380 C  CG2   . THR A 1 3550 ? 214.718 176.742 246.960 1.00 21.82  ? 3550 THR A CG2   1 
ATOM   14381 N  N     . GLU A 1 3551 ? 214.784 173.737 250.438 1.00 30.37  ? 3551 GLU A N     1 
ATOM   14382 C  CA    . GLU A 1 3551 ? 214.274 172.670 251.290 1.00 34.00  ? 3551 GLU A CA    1 
ATOM   14383 C  C     . GLU A 1 3551 ? 214.137 173.124 252.737 1.00 34.10  ? 3551 GLU A C     1 
ATOM   14384 O  O     . GLU A 1 3551 ? 213.211 172.697 253.435 1.00 33.85  ? 3551 GLU A O     1 
ATOM   14385 C  CB    . GLU A 1 3551 ? 215.190 171.449 251.201 1.00 40.61  ? 3551 GLU A CB    1 
ATOM   14386 C  CG    . GLU A 1 3551 ? 214.837 170.469 250.086 1.00 40.66  ? 3551 GLU A CG    1 
ATOM   14387 C  CD    . GLU A 1 3551 ? 213.680 169.549 250.439 1.00 49.39  ? 3551 GLU A CD    1 
ATOM   14388 O  OE1   . GLU A 1 3551 ? 213.513 168.521 249.751 1.00 56.59  ? 3551 GLU A OE1   1 
ATOM   14389 O  OE2   . GLU A 1 3551 ? 212.939 169.845 251.401 1.00 47.36  ? 3551 GLU A OE2   1 
ATOM   14390 N  N     . TYR A 1 3552 ? 215.045 173.981 253.206 1.00 34.61  ? 3552 TYR A N     1 
ATOM   14391 C  CA    . TYR A 1 3552 ? 215.001 174.433 254.591 1.00 26.75  ? 3552 TYR A CA    1 
ATOM   14392 C  C     . TYR A 1 3552 ? 213.925 175.487 254.823 1.00 21.98  ? 3552 TYR A C     1 
ATOM   14393 O  O     . TYR A 1 3552 ? 213.338 175.532 255.908 1.00 25.83  ? 3552 TYR A O     1 
ATOM   14394 C  CB    . TYR A 1 3552 ? 216.366 174.980 255.005 1.00 26.73  ? 3552 TYR A CB    1 
ATOM   14395 C  CG    . TYR A 1 3552 ? 216.470 175.323 256.471 1.00 27.46  ? 3552 TYR A CG    1 
ATOM   14396 C  CD1   . TYR A 1 3552 ? 216.259 174.356 257.444 1.00 34.81  ? 3552 TYR A CD1   1 
ATOM   14397 C  CD2   . TYR A 1 3552 ? 216.784 176.609 256.884 1.00 29.29  ? 3552 TYR A CD2   1 
ATOM   14398 C  CE1   . TYR A 1 3552 ? 216.355 174.661 258.786 1.00 37.00  ? 3552 TYR A CE1   1 
ATOM   14399 C  CE2   . TYR A 1 3552 ? 216.882 176.924 258.224 1.00 29.65  ? 3552 TYR A CE2   1 
ATOM   14400 C  CZ    . TYR A 1 3552 ? 216.667 175.947 259.171 1.00 35.86  ? 3552 TYR A CZ    1 
ATOM   14401 O  OH    . TYR A 1 3552 ? 216.763 176.255 260.507 1.00 43.25  ? 3552 TYR A OH    1 
ATOM   14402 N  N     . LEU A 1 3553 ? 213.655 176.334 253.833 1.00 23.14  ? 3553 LEU A N     1 
ATOM   14403 C  CA    . LEU A 1 3553 ? 212.733 177.448 254.009 1.00 21.78  ? 3553 LEU A CA    1 
ATOM   14404 C  C     . LEU A 1 3553 ? 211.311 177.139 253.558 1.00 27.83  ? 3553 LEU A C     1 
ATOM   14405 O  O     . LEU A 1 3553 ? 210.460 178.033 253.597 1.00 26.02  ? 3553 LEU A O     1 
ATOM   14406 C  CB    . LEU A 1 3553 ? 213.253 178.678 253.262 1.00 21.57  ? 3553 LEU A CB    1 
ATOM   14407 C  CG    . LEU A 1 3553 ? 214.377 179.452 253.954 1.00 20.52  ? 3553 LEU A CG    1 
ATOM   14408 C  CD1   . LEU A 1 3553 ? 214.959 180.502 253.027 1.00 17.43  ? 3553 LEU A CD1   1 
ATOM   14409 C  CD2   . LEU A 1 3553 ? 213.869 180.087 255.235 1.00 18.73  ? 3553 LEU A CD2   1 
ATOM   14410 N  N     . SER A 1 3554 ? 211.030 175.909 253.134 1.00 29.42  ? 3554 SER A N     1 
ATOM   14411 C  CA    . SER A 1 3554 ? 209.684 175.534 252.722 1.00 25.50  ? 3554 SER A CA    1 
ATOM   14412 C  C     . SER A 1 3554 ? 209.532 174.027 252.854 1.00 32.42  ? 3554 SER A C     1 
ATOM   14413 O  O     . SER A 1 3554 ? 210.519 173.291 252.927 1.00 35.49  ? 3554 SER A O     1 
ATOM   14414 C  CB    . SER A 1 3554 ? 209.390 175.983 251.287 1.00 24.89  ? 3554 SER A CB    1 
ATOM   14415 O  OG    . SER A 1 3554 ? 210.287 175.380 250.375 1.00 27.52  ? 3554 SER A OG    1 
ATOM   14416 N  N     . ASN A 1 3555 ? 208.281 173.577 252.887 1.00 31.02  ? 3555 ASN A N     1 
ATOM   14417 C  CA    . ASN A 1 3555 ? 207.975 172.159 252.972 1.00 26.17  ? 3555 ASN A CA    1 
ATOM   14418 C  C     . ASN A 1 3555 ? 207.445 171.660 251.629 1.00 34.59  ? 3555 ASN A C     1 
ATOM   14419 O  O     . ASN A 1 3555 ? 207.238 172.427 250.686 1.00 35.55  ? 3555 ASN A O     1 
ATOM   14420 C  CB    . ASN A 1 3555 ? 206.982 171.885 254.104 1.00 28.20  ? 3555 ASN A CB    1 
ATOM   14421 C  CG    . ASN A 1 3555 ? 205.829 172.866 254.123 1.00 30.40  ? 3555 ASN A CG    1 
ATOM   14422 O  OD1   . ASN A 1 3555 ? 204.929 172.795 253.289 1.00 33.74  ? 3555 ASN A OD1   1 
ATOM   14423 N  ND2   . ASN A 1 3555 ? 205.851 173.787 255.077 1.00 31.58  ? 3555 ASN A ND2   1 
ATOM   14424 N  N     . ALA A 1 3556 ? 207.226 170.347 251.548 1.00 37.40  ? 3556 ALA A N     1 
ATOM   14425 C  CA    . ALA A 1 3556 ? 206.862 169.729 250.278 1.00 36.77  ? 3556 ALA A CA    1 
ATOM   14426 C  C     . ALA A 1 3556 ? 205.431 170.061 249.861 1.00 36.35  ? 3556 ALA A C     1 
ATOM   14427 O  O     . ALA A 1 3556 ? 205.169 170.272 248.672 1.00 38.35  ? 3556 ALA A O     1 
ATOM   14428 C  CB    . ALA A 1 3556 ? 207.059 168.217 250.359 1.00 42.08  ? 3556 ALA A CB    1 
ATOM   14429 N  N     . ASP A 1 3557 ? 204.494 170.095 250.812 1.00 31.39  ? 3557 ASP A N     1 
ATOM   14430 C  CA    . ASP A 1 3557 ? 203.111 170.432 250.474 1.00 37.79  ? 3557 ASP A CA    1 
ATOM   14431 C  C     . ASP A 1 3557 ? 203.005 171.855 249.943 1.00 39.68  ? 3557 ASP A C     1 
ATOM   14432 O  O     . ASP A 1 3557 ? 202.267 172.121 248.987 1.00 37.51  ? 3557 ASP A O     1 
ATOM   14433 C  CB    . ASP A 1 3557 ? 202.210 170.252 251.696 1.00 41.55  ? 3557 ASP A CB    1 
ATOM   14434 C  CG    . ASP A 1 3557 ? 202.290 168.857 252.278 1.00 53.30  ? 3557 ASP A CG    1 
ATOM   14435 O  OD1   . ASP A 1 3557 ? 203.056 168.033 251.740 1.00 57.86  ? 3557 ASP A OD1   1 
ATOM   14436 O  OD2   . ASP A 1 3557 ? 201.587 168.584 253.273 1.00 56.04  ? 3557 ASP A OD2   1 
ATOM   14437 N  N     . GLU A 1 3558 ? 203.733 172.785 250.562 1.00 34.12  ? 3558 GLU A N     1 
ATOM   14438 C  CA    . GLU A 1 3558 ? 203.765 174.166 250.095 1.00 30.92  ? 3558 GLU A CA    1 
ATOM   14439 C  C     . GLU A 1 3558 ? 204.349 174.266 248.690 1.00 29.90  ? 3558 GLU A C     1 
ATOM   14440 O  O     . GLU A 1 3558 ? 203.837 175.020 247.854 1.00 29.89  ? 3558 GLU A O     1 
ATOM   14441 C  CB    . GLU A 1 3558 ? 204.566 174.996 251.099 1.00 32.83  ? 3558 GLU A CB    1 
ATOM   14442 C  CG    . GLU A 1 3558 ? 204.978 176.384 250.684 1.00 31.92  ? 3558 GLU A CG    1 
ATOM   14443 C  CD    . GLU A 1 3558 ? 205.471 177.184 251.876 1.00 39.80  ? 3558 GLU A CD    1 
ATOM   14444 O  OE1   . GLU A 1 3558 ? 205.390 176.664 253.008 1.00 38.26  ? 3558 GLU A OE1   1 
ATOM   14445 O  OE2   . GLU A 1 3558 ? 205.944 178.320 251.690 1.00 47.20  ? 3558 GLU A OE2   1 
ATOM   14446 N  N     . ARG A 1 3559 ? 205.404 173.498 248.411 1.00 32.50  ? 3559 ARG A N     1 
ATOM   14447 C  CA    . ARG A 1 3559 ? 205.982 173.475 247.072 1.00 25.19  ? 3559 ARG A CA    1 
ATOM   14448 C  C     . ARG A 1 3559 ? 205.005 172.897 246.053 1.00 30.97  ? 3559 ARG A C     1 
ATOM   14449 O  O     . ARG A 1 3559 ? 204.930 173.375 244.917 1.00 33.94  ? 3559 ARG A O     1 
ATOM   14450 C  CB    . ARG A 1 3559 ? 207.285 172.681 247.091 1.00 24.90  ? 3559 ARG A CB    1 
ATOM   14451 C  CG    . ARG A 1 3559 ? 208.511 173.534 247.344 1.00 24.90  ? 3559 ARG A CG    1 
ATOM   14452 C  CD    . ARG A 1 3559 ? 209.775 172.707 247.298 1.00 26.12  ? 3559 ARG A CD    1 
ATOM   14453 N  NE    . ARG A 1 3559 ? 210.319 172.517 248.636 1.00 27.80  ? 3559 ARG A NE    1 
ATOM   14454 C  CZ    . ARG A 1 3559 ? 210.579 171.337 249.180 1.00 33.20  ? 3559 ARG A CZ    1 
ATOM   14455 N  NH1   . ARG A 1 3559 ? 210.360 170.211 248.523 1.00 34.66  ? 3559 ARG A NH1   1 
ATOM   14456 N  NH2   . ARG A 1 3559 ? 211.065 171.286 250.416 1.00 30.82  ? 3559 ARG A NH2   1 
ATOM   14457 N  N     . LEU A 1 3560 ? 204.254 171.861 246.437 1.00 34.35  ? 3560 LEU A N     1 
ATOM   14458 C  CA    . LEU A 1 3560 ? 203.244 171.311 245.536 1.00 33.97  ? 3560 LEU A CA    1 
ATOM   14459 C  C     . LEU A 1 3560 ? 202.138 172.322 245.263 1.00 30.69  ? 3560 LEU A C     1 
ATOM   14460 O  O     . LEU A 1 3560 ? 201.644 172.426 244.134 1.00 34.36  ? 3560 LEU A O     1 
ATOM   14461 C  CB    . LEU A 1 3560 ? 202.662 170.021 246.115 1.00 32.03  ? 3560 LEU A CB    1 
ATOM   14462 C  CG    . LEU A 1 3560 ? 203.618 168.834 246.232 1.00 35.46  ? 3560 LEU A CG    1 
ATOM   14463 C  CD1   . LEU A 1 3560 ? 202.946 167.675 246.947 1.00 43.22  ? 3560 LEU A CD1   1 
ATOM   14464 C  CD2   . LEU A 1 3560 ? 204.108 168.409 244.858 1.00 39.17  ? 3560 LEU A CD2   1 
ATOM   14465 N  N     . ARG A 1 3561 ? 201.724 173.066 246.291 1.00 27.47  ? 3561 ARG A N     1 
ATOM   14466 C  CA    . ARG A 1 3561 ? 200.743 174.125 246.084 1.00 28.23  ? 3561 ARG A CA    1 
ATOM   14467 C  C     . ARG A 1 3561 ? 201.274 175.183 245.127 1.00 35.78  ? 3561 ARG A C     1 
ATOM   14468 O  O     . ARG A 1 3561 ? 200.543 175.668 244.253 1.00 40.59  ? 3561 ARG A O     1 
ATOM   14469 C  CB    . ARG A 1 3561 ? 200.366 174.759 247.422 1.00 32.23  ? 3561 ARG A CB    1 
ATOM   14470 C  CG    . ARG A 1 3561 ? 199.507 173.882 248.312 1.00 40.30  ? 3561 ARG A CG    1 
ATOM   14471 C  CD    . ARG A 1 3561 ? 198.772 174.710 249.351 1.00 43.57  ? 3561 ARG A CD    1 
ATOM   14472 N  NE    . ARG A 1 3561 ? 199.691 175.394 250.255 1.00 45.19  ? 3561 ARG A NE    1 
ATOM   14473 C  CZ    . ARG A 1 3561 ? 200.028 176.673 250.160 1.00 50.77  ? 3561 ARG A CZ    1 
ATOM   14474 N  NH1   . ARG A 1 3561 ? 199.537 177.448 249.208 1.00 41.04  ? 3561 ARG A NH1   1 
ATOM   14475 N  NH2   . ARG A 1 3561 ? 200.881 177.185 251.042 1.00 53.59  ? 3561 ARG A NH2   1 
ATOM   14476 N  N     . TRP A 1 3562 ? 202.546 175.555 245.279 1.00 32.91  ? 3562 TRP A N     1 
ATOM   14477 C  CA    . TRP A 1 3562 ? 203.155 176.501 244.350 1.00 26.39  ? 3562 TRP A CA    1 
ATOM   14478 C  C     . TRP A 1 3562 ? 203.164 175.950 242.929 1.00 35.13  ? 3562 TRP A C     1 
ATOM   14479 O  O     . TRP A 1 3562 ? 202.877 176.676 241.971 1.00 37.33  ? 3562 TRP A O     1 
ATOM   14480 C  CB    . TRP A 1 3562 ? 204.574 176.838 244.799 1.00 26.22  ? 3562 TRP A CB    1 
ATOM   14481 C  CG    . TRP A 1 3562 ? 204.629 177.710 246.004 1.00 25.06  ? 3562 TRP A CG    1 
ATOM   14482 C  CD1   . TRP A 1 3562 ? 203.631 178.498 246.491 1.00 22.70  ? 3562 TRP A CD1   1 
ATOM   14483 C  CD2   . TRP A 1 3562 ? 205.750 177.898 246.872 1.00 22.33  ? 3562 TRP A CD2   1 
ATOM   14484 N  NE1   . TRP A 1 3562 ? 204.057 179.158 247.616 1.00 21.16  ? 3562 TRP A NE1   1 
ATOM   14485 C  CE2   . TRP A 1 3562 ? 205.356 178.808 247.869 1.00 19.84  ? 3562 TRP A CE2   1 
ATOM   14486 C  CE3   . TRP A 1 3562 ? 207.049 177.382 246.904 1.00 17.40  ? 3562 TRP A CE3   1 
ATOM   14487 C  CZ2   . TRP A 1 3562 ? 206.215 179.218 248.881 1.00 21.14  ? 3562 TRP A CZ2   1 
ATOM   14488 C  CZ3   . TRP A 1 3562 ? 207.895 177.787 247.913 1.00 18.24  ? 3562 TRP A CZ3   1 
ATOM   14489 C  CH2   . TRP A 1 3562 ? 207.476 178.692 248.889 1.00 19.77  ? 3562 TRP A CH2   1 
ATOM   14490 N  N     . GLN A 1 3563 ? 203.497 174.666 242.779 1.00 35.23  ? 3563 GLN A N     1 
ATOM   14491 C  CA    . GLN A 1 3563 ? 203.470 174.030 241.466 1.00 34.88  ? 3563 GLN A CA    1 
ATOM   14492 C  C     . GLN A 1 3563 ? 202.077 174.098 240.856 1.00 33.11  ? 3563 GLN A C     1 
ATOM   14493 O  O     . GLN A 1 3563 ? 201.924 174.389 239.665 1.00 30.59  ? 3563 GLN A O     1 
ATOM   14494 C  CB    . GLN A 1 3563 ? 203.926 172.571 241.583 1.00 32.81  ? 3563 GLN A CB    1 
ATOM   14495 C  CG    . GLN A 1 3563 ? 205.421 172.326 241.849 1.00 36.09  ? 3563 GLN A CG    1 
ATOM   14496 C  CD    . GLN A 1 3563 ? 206.376 173.245 241.094 1.00 40.94  ? 3563 GLN A CD    1 
ATOM   14497 O  OE1   . GLN A 1 3563 ? 206.050 173.788 240.041 1.00 37.99  ? 3563 GLN A OE1   1 
ATOM   14498 N  NE2   . GLN A 1 3563 ? 207.572 173.419 241.645 1.00 41.35  ? 3563 GLN A NE2   1 
ATOM   14499 N  N     . ALA A 1 3564 ? 201.050 173.827 241.662 1.00 34.66  ? 3564 ALA A N     1 
ATOM   14500 C  CA    . ALA A 1 3564 ? 199.674 173.930 241.194 1.00 33.11  ? 3564 ALA A CA    1 
ATOM   14501 C  C     . ALA A 1 3564 ? 199.285 175.362 240.854 1.00 34.17  ? 3564 ALA A C     1 
ATOM   14502 O  O     . ALA A 1 3564 ? 198.406 175.568 240.010 1.00 31.51  ? 3564 ALA A O     1 
ATOM   14503 C  CB    . ALA A 1 3564 ? 198.717 173.366 242.243 1.00 32.00  ? 3564 ALA A CB    1 
ATOM   14504 N  N     . SER A 1 3565 ? 199.917 176.352 241.487 1.00 39.70  ? 3565 SER A N     1 
ATOM   14505 C  CA    . SER A 1 3565 ? 199.632 177.757 241.226 1.00 33.61  ? 3565 SER A CA    1 
ATOM   14506 C  C     . SER A 1 3565 ? 200.442 178.317 240.062 1.00 30.86  ? 3565 SER A C     1 
ATOM   14507 O  O     . SER A 1 3565 ? 200.652 179.535 239.988 1.00 30.54  ? 3565 SER A O     1 
ATOM   14508 C  CB    . SER A 1 3565 ? 199.872 178.586 242.489 1.00 31.54  ? 3565 SER A CB    1 
ATOM   14509 O  OG    . SER A 1 3565 ? 198.971 178.217 243.517 1.00 33.50  ? 3565 SER A OG    1 
ATOM   14510 N  N     . SER A 1 3566 ? 200.910 177.452 239.158 1.00 32.47  ? 3566 SER A N     1 
ATOM   14511 C  CA    . SER A 1 3566 ? 201.616 177.859 237.941 1.00 31.95  ? 3566 SER A CA    1 
ATOM   14512 C  C     . SER A 1 3566 ? 202.924 178.582 238.263 1.00 29.46  ? 3566 SER A C     1 
ATOM   14513 O  O     . SER A 1 3566 ? 203.192 179.680 237.774 1.00 32.18  ? 3566 SER A O     1 
ATOM   14514 C  CB    . SER A 1 3566 ? 200.721 178.719 237.045 1.00 36.78  ? 3566 SER A CB    1 
ATOM   14515 O  OG    . SER A 1 3566 ? 200.791 180.085 237.416 1.00 41.67  ? 3566 SER A OG    1 
ATOM   14516 N  N     . LEU A 1 3567 ? 203.745 177.948 239.096 1.00 30.86  ? 3567 LEU A N     1 
ATOM   14517 C  CA    . LEU A 1 3567 ? 205.079 178.440 239.397 1.00 29.38  ? 3567 LEU A CA    1 
ATOM   14518 C  C     . LEU A 1 3567 ? 206.114 177.510 238.791 1.00 32.48  ? 3567 LEU A C     1 
ATOM   14519 O  O     . LEU A 1 3567 ? 206.046 176.295 239.016 1.00 37.96  ? 3567 LEU A O     1 
ATOM   14520 C  CB    . LEU A 1 3567 ? 205.300 178.547 240.910 1.00 26.66  ? 3567 LEU A CB    1 
ATOM   14521 C  CG    . LEU A 1 3567 ? 206.659 179.100 241.348 1.00 25.16  ? 3567 LEU A CG    1 
ATOM   14522 C  CD1   . LEU A 1 3567 ? 206.674 180.619 241.294 1.00 20.11  ? 3567 LEU A CD1   1 
ATOM   14523 C  CD2   . LEU A 1 3567 ? 207.021 178.608 242.739 1.00 24.12  ? 3567 LEU A CD2   1 
ATOM   14524 N  N     . PRO A 1 3568 ? 207.064 178.024 238.009 1.00 32.16  ? 3568 PRO A N     1 
ATOM   14525 C  CA    . PRO A 1 3568 ? 208.082 177.148 237.419 1.00 29.00  ? 3568 PRO A CA    1 
ATOM   14526 C  C     . PRO A 1 3568 ? 208.903 176.441 238.488 1.00 30.46  ? 3568 PRO A C     1 
ATOM   14527 O  O     . PRO A 1 3568 ? 209.155 176.976 239.569 1.00 35.71  ? 3568 PRO A O     1 
ATOM   14528 C  CB    . PRO A 1 3568 ? 208.945 178.106 236.587 1.00 27.95  ? 3568 PRO A CB    1 
ATOM   14529 C  CG    . PRO A 1 3568 ? 208.546 179.481 236.997 1.00 26.62  ? 3568 PRO A CG    1 
ATOM   14530 C  CD    . PRO A 1 3568 ? 207.155 179.406 237.515 1.00 32.81  ? 3568 PRO A CD    1 
ATOM   14531 N  N     . ALA A 1 3569 ? 209.320 175.216 238.167 1.00 30.22  ? 3569 ALA A N     1 
ATOM   14532 C  CA    . ALA A 1 3569 ? 210.018 174.344 239.104 1.00 30.53  ? 3569 ALA A CA    1 
ATOM   14533 C  C     . ALA A 1 3569 ? 211.478 174.728 239.314 1.00 34.12  ? 3569 ALA A C     1 
ATOM   14534 O  O     . ALA A 1 3569 ? 212.219 173.959 239.935 1.00 40.24  ? 3569 ALA A O     1 
ATOM   14535 C  CB    . ALA A 1 3569 ? 209.932 172.892 238.628 1.00 24.85  ? 3569 ALA A CB    1 
ATOM   14536 N  N     . ASP A 1 3570 ? 211.904 175.885 238.818 1.00 29.26  ? 3570 ASP A N     1 
ATOM   14537 C  CA    . ASP A 1 3570 ? 213.278 176.326 238.996 1.00 27.83  ? 3570 ASP A CA    1 
ATOM   14538 C  C     . ASP A 1 3570 ? 213.550 176.664 240.460 1.00 26.20  ? 3570 ASP A C     1 
ATOM   14539 O  O     . ASP A 1 3570 ? 212.670 177.131 241.187 1.00 26.27  ? 3570 ASP A O     1 
ATOM   14540 C  CB    . ASP A 1 3570 ? 213.556 177.537 238.104 1.00 29.10  ? 3570 ASP A CB    1 
ATOM   14541 C  CG    . ASP A 1 3570 ? 214.891 178.184 238.391 1.00 28.12  ? 3570 ASP A CG    1 
ATOM   14542 O  OD1   . ASP A 1 3570 ? 215.922 177.480 238.336 1.00 31.67  ? 3570 ASP A OD1   1 
ATOM   14543 O  OD2   . ASP A 1 3570 ? 214.912 179.401 238.659 1.00 21.39  ? 3570 ASP A OD2   1 
ATOM   14544 N  N     . ASP A 1 3571 ? 214.787 176.403 240.892 1.00 28.04  ? 3571 ASP A N     1 
ATOM   14545 C  CA    . ASP A 1 3571 ? 215.163 176.656 242.282 1.00 24.65  ? 3571 ASP A CA    1 
ATOM   14546 C  C     . ASP A 1 3571 ? 215.087 178.139 242.624 1.00 20.78  ? 3571 ASP A C     1 
ATOM   14547 O  O     . ASP A 1 3571 ? 214.628 178.507 243.712 1.00 21.94  ? 3571 ASP A O     1 
ATOM   14548 C  CB    . ASP A 1 3571 ? 216.569 176.121 242.552 1.00 31.29  ? 3571 ASP A CB    1 
ATOM   14549 C  CG    . ASP A 1 3571 ? 216.633 174.607 242.524 1.00 49.17  ? 3571 ASP A CG    1 
ATOM   14550 O  OD1   . ASP A 1 3571 ? 215.614 173.960 242.846 1.00 49.09  ? 3571 ASP A OD1   1 
ATOM   14551 O  OD2   . ASP A 1 3571 ? 217.703 174.063 242.178 1.00 56.85  ? 3571 ASP A OD2   1 
ATOM   14552 N  N     . LEU A 1 3572 ? 215.545 179.004 241.716 1.00 20.59  ? 3572 LEU A N     1 
ATOM   14553 C  CA    . LEU A 1 3572 ? 215.483 180.440 241.971 1.00 14.56  ? 3572 LEU A CA    1 
ATOM   14554 C  C     . LEU A 1 3572 ? 214.040 180.910 242.093 1.00 17.55  ? 3572 LEU A C     1 
ATOM   14555 O  O     . LEU A 1 3572 ? 213.731 181.789 242.904 1.00 20.65  ? 3572 LEU A O     1 
ATOM   14556 C  CB    . LEU A 1 3572 ? 216.227 181.201 240.870 1.00 12.65  ? 3572 LEU A CB    1 
ATOM   14557 C  CG    . LEU A 1 3572 ? 216.458 182.709 240.997 1.00 14.01  ? 3572 LEU A CG    1 
ATOM   14558 C  CD1   . LEU A 1 3572 ? 217.710 183.104 240.239 1.00 14.08  ? 3572 LEU A CD1   1 
ATOM   14559 C  CD2   . LEU A 1 3572 ? 215.276 183.500 240.461 1.00 10.20  ? 3572 LEU A CD2   1 
ATOM   14560 N  N     . CYS A 1 3573 ? 213.137 180.329 241.302 1.00 16.85  ? 3573 CYS A N     1 
ATOM   14561 C  CA    . CYS A 1 3573 ? 211.726 180.670 241.435 1.00 17.23  ? 3573 CYS A CA    1 
ATOM   14562 C  C     . CYS A 1 3573 ? 211.151 180.183 242.759 1.00 17.21  ? 3573 CYS A C     1 
ATOM   14563 O  O     . CYS A 1 3573 ? 210.292 180.852 243.342 1.00 19.46  ? 3573 CYS A O     1 
ATOM   14564 C  CB    . CYS A 1 3573 ? 210.937 180.102 240.258 1.00 23.17  ? 3573 CYS A CB    1 
ATOM   14565 S  SG    . CYS A 1 3573 ? 211.033 181.129 238.775 1.00 44.86  ? 3573 CYS A SG    1 
ATOM   14566 N  N     . THR A 1 3574 ? 211.609 179.030 243.252 1.00 18.15  ? 3574 THR A N     1 
ATOM   14567 C  CA    . THR A 1 3574 ? 211.184 178.579 244.573 1.00 15.08  ? 3574 THR A CA    1 
ATOM   14568 C  C     . THR A 1 3574 ? 211.680 179.527 245.659 1.00 14.89  ? 3574 THR A C     1 
ATOM   14569 O  O     . THR A 1 3574 ? 210.949 179.833 246.609 1.00 16.62  ? 3574 THR A O     1 
ATOM   14570 C  CB    . THR A 1 3574 ? 211.682 177.156 244.832 1.00 15.39  ? 3574 THR A CB    1 
ATOM   14571 O  OG1   . THR A 1 3574 ? 211.187 176.283 243.810 1.00 24.04  ? 3574 THR A OG1   1 
ATOM   14572 C  CG2   . THR A 1 3574 ? 211.189 176.662 246.181 1.00 18.41  ? 3574 THR A CG2   1 
ATOM   14573 N  N     . GLU A 1 3575 ? 212.920 180.005 245.533 1.00 14.11  ? 3575 GLU A N     1 
ATOM   14574 C  CA    . GLU A 1 3575 ? 213.427 181.005 246.469 1.00 13.66  ? 3575 GLU A CA    1 
ATOM   14575 C  C     . GLU A 1 3575 ? 212.599 182.282 246.406 1.00 13.40  ? 3575 GLU A C     1 
ATOM   14576 O  O     . GLU A 1 3575 ? 212.291 182.888 247.440 1.00 14.67  ? 3575 GLU A O     1 
ATOM   14577 C  CB    . GLU A 1 3575 ? 214.893 181.314 246.166 1.00 14.44  ? 3575 GLU A CB    1 
ATOM   14578 C  CG    . GLU A 1 3575 ? 215.849 180.167 246.430 1.00 18.52  ? 3575 GLU A CG    1 
ATOM   14579 C  CD    . GLU A 1 3575 ? 217.160 180.328 245.687 1.00 17.60  ? 3575 GLU A CD    1 
ATOM   14580 O  OE1   . GLU A 1 3575 ? 217.288 181.292 244.905 1.00 13.52  ? 3575 GLU A OE1   1 
ATOM   14581 O  OE2   . GLU A 1 3575 ? 218.064 179.490 245.884 1.00 22.17  ? 3575 GLU A OE2   1 
ATOM   14582 N  N     . ASN A 1 3576 ? 212.233 182.704 245.195 1.00 14.35  ? 3576 ASN A N     1 
ATOM   14583 C  CA    . ASN A 1 3576 ? 211.400 183.889 245.036 1.00 12.49  ? 3576 ASN A CA    1 
ATOM   14584 C  C     . ASN A 1 3576 ? 210.037 183.699 245.692 1.00 12.80  ? 3576 ASN A C     1 
ATOM   14585 O  O     . ASN A 1 3576 ? 209.513 184.621 246.321 1.00 15.02  ? 3576 ASN A O     1 
ATOM   14586 C  CB    . ASN A 1 3576 ? 211.242 184.223 243.554 1.00 11.30  ? 3576 ASN A CB    1 
ATOM   14587 C  CG    . ASN A 1 3576 ? 212.477 184.876 242.968 1.00 10.17  ? 3576 ASN A CG    1 
ATOM   14588 O  OD1   . ASN A 1 3576 ? 213.382 185.281 243.694 1.00 12.27  ? 3576 ASN A OD1   1 
ATOM   14589 N  ND2   . ASN A 1 3576 ? 212.514 184.988 241.649 1.00 10.03  ? 3576 ASN A ND2   1 
ATOM   14590 N  N     . ALA A 1 3577 ? 209.446 182.512 245.547 1.00 12.78  ? 3577 ALA A N     1 
ATOM   14591 C  CA    . ALA A 1 3577 ? 208.178 182.228 246.213 1.00 13.74  ? 3577 ALA A CA    1 
ATOM   14592 C  C     . ALA A 1 3577 ? 208.328 182.236 247.730 1.00 14.15  ? 3577 ALA A C     1 
ATOM   14593 O  O     . ALA A 1 3577 ? 207.435 182.716 248.442 1.00 17.82  ? 3577 ALA A O     1 
ATOM   14594 C  CB    . ALA A 1 3577 ? 207.622 180.887 245.737 1.00 14.46  ? 3577 ALA A CB    1 
ATOM   14595 N  N     . ILE A 1 3578 ? 209.442 181.708 248.236 1.00 14.72  ? 3578 ILE A N     1 
ATOM   14596 C  CA    . ILE A 1 3578 ? 209.715 181.756 249.671 1.00 12.46  ? 3578 ILE A CA    1 
ATOM   14597 C  C     . ILE A 1 3578 ? 209.770 183.201 250.151 1.00 17.08  ? 3578 ILE A C     1 
ATOM   14598 O  O     . ILE A 1 3578 ? 209.202 183.549 251.192 1.00 21.25  ? 3578 ILE A O     1 
ATOM   14599 C  CB    . ILE A 1 3578 ? 211.019 181.001 249.989 1.00 11.78  ? 3578 ILE A CB    1 
ATOM   14600 C  CG1   . ILE A 1 3578 ? 210.815 179.494 249.838 1.00 12.83  ? 3578 ILE A CG1   1 
ATOM   14601 C  CG2   . ILE A 1 3578 ? 211.506 181.335 251.388 1.00 15.97  ? 3578 ILE A CG2   1 
ATOM   14602 C  CD1   . ILE A 1 3578 ? 212.100 178.701 249.829 1.00 13.03  ? 3578 ILE A CD1   1 
ATOM   14603 N  N     . MET A 1 3579 ? 210.456 184.064 249.397 1.00 13.95  ? 3579 MET A N     1 
ATOM   14604 C  CA    . MET A 1 3579 ? 210.488 185.483 249.744 1.00 10.92  ? 3579 MET A CA    1 
ATOM   14605 C  C     . MET A 1 3579 ? 209.098 186.106 249.672 1.00 12.47  ? 3579 MET A C     1 
ATOM   14606 O  O     . MET A 1 3579 ? 208.732 186.920 250.527 1.00 16.06  ? 3579 MET A O     1 
ATOM   14607 C  CB    . MET A 1 3579 ? 211.460 186.230 248.832 1.00 9.45   ? 3579 MET A CB    1 
ATOM   14608 C  CG    . MET A 1 3579 ? 212.842 185.614 248.761 1.00 8.76   ? 3579 MET A CG    1 
ATOM   14609 S  SD    . MET A 1 3579 ? 213.943 186.513 247.659 1.00 24.96  ? 3579 MET A SD    1 
ATOM   14610 C  CE    . MET A 1 3579 ? 215.444 185.550 247.814 1.00 7.79   ? 3579 MET A CE    1 
ATOM   14611 N  N     . LEU A 1 3580 ? 208.313 185.743 248.657 1.00 13.23  ? 3580 LEU A N     1 
ATOM   14612 C  CA    . LEU A 1 3580 ? 206.953 186.248 248.515 1.00 11.40  ? 3580 LEU A CA    1 
ATOM   14613 C  C     . LEU A 1 3580 ? 206.027 185.769 249.622 1.00 14.18  ? 3580 LEU A C     1 
ATOM   14614 O  O     . LEU A 1 3580 ? 204.960 186.363 249.809 1.00 17.77  ? 3580 LEU A O     1 
ATOM   14615 C  CB    . LEU A 1 3580 ? 206.376 185.849 247.156 1.00 10.28  ? 3580 LEU A CB    1 
ATOM   14616 C  CG    . LEU A 1 3580 ? 207.004 186.510 245.931 1.00 9.94   ? 3580 LEU A CG    1 
ATOM   14617 C  CD1   . LEU A 1 3580 ? 206.470 185.885 244.657 1.00 12.04  ? 3580 LEU A CD1   1 
ATOM   14618 C  CD2   . LEU A 1 3580 ? 206.738 188.004 245.944 1.00 10.15  ? 3580 LEU A CD2   1 
ATOM   14619 N  N     . LYS A 1 3581 ? 206.387 184.708 250.338 1.00 14.75  ? 3581 LYS A N     1 
ATOM   14620 C  CA    . LYS A 1 3581 ? 205.661 184.338 251.546 1.00 14.26  ? 3581 LYS A CA    1 
ATOM   14621 C  C     . LYS A 1 3581 ? 206.266 184.943 252.805 1.00 20.12  ? 3581 LYS A C     1 
ATOM   14622 O  O     . LYS A 1 3581 ? 205.543 185.537 253.611 1.00 23.21  ? 3581 LYS A O     1 
ATOM   14623 C  CB    . LYS A 1 3581 ? 205.604 182.817 251.704 1.00 16.59  ? 3581 LYS A CB    1 
ATOM   14624 C  CG    . LYS A 1 3581 ? 204.781 182.384 252.905 1.00 26.91  ? 3581 LYS A CG    1 
ATOM   14625 C  CD    . LYS A 1 3581 ? 204.684 180.878 253.026 1.00 34.54  ? 3581 LYS A CD    1 
ATOM   14626 C  CE    . LYS A 1 3581 ? 203.777 180.484 254.180 1.00 48.29  ? 3581 LYS A CE    1 
ATOM   14627 N  NZ    . LYS A 1 3581 ? 204.365 180.853 255.496 1.00 54.74  ? 3581 LYS A NZ    1 
ATOM   14628 N  N     . ARG A 1 3582 ? 207.577 184.808 252.988 1.00 20.17  ? 3582 ARG A N     1 
ATOM   14629 C  CA    . ARG A 1 3582 ? 208.273 185.290 254.180 1.00 13.49  ? 3582 ARG A CA    1 
ATOM   14630 C  C     . ARG A 1 3582 ? 208.883 186.651 253.859 1.00 20.93  ? 3582 ARG A C     1 
ATOM   14631 O  O     . ARG A 1 3582 ? 210.053 186.753 253.491 1.00 35.63  ? 3582 ARG A O     1 
ATOM   14632 C  CB    . ARG A 1 3582 ? 209.343 184.297 254.614 1.00 18.21  ? 3582 ARG A CB    1 
ATOM   14633 C  CG    . ARG A 1 3582 ? 208.817 182.931 254.998 1.00 22.32  ? 3582 ARG A CG    1 
ATOM   14634 C  CD    . ARG A 1 3582 ? 209.959 182.001 255.359 1.00 21.12  ? 3582 ARG A CD    1 
ATOM   14635 N  NE    . ARG A 1 3582 ? 209.486 180.663 255.688 1.00 30.94  ? 3582 ARG A NE    1 
ATOM   14636 C  CZ    . ARG A 1 3582 ? 209.082 180.288 256.893 1.00 39.11  ? 3582 ARG A CZ    1 
ATOM   14637 N  NH1   . ARG A 1 3582 ? 209.074 181.132 257.912 1.00 38.42  ? 3582 ARG A NH1   1 
ATOM   14638 N  NH2   . ARG A 1 3582 ? 208.673 179.037 257.080 1.00 46.78  ? 3582 ARG A NH2   1 
ATOM   14639 N  N     . PHE A 1 3583 ? 208.084 187.705 253.999 1.00 15.74  ? 3583 PHE A N     1 
ATOM   14640 C  CA    . PHE A 1 3583 ? 208.557 189.062 253.768 1.00 17.11  ? 3583 PHE A CA    1 
ATOM   14641 C  C     . PHE A 1 3583 ? 208.102 189.966 254.903 1.00 20.68  ? 3583 PHE A C     1 
ATOM   14642 O  O     . PHE A 1 3583 ? 207.007 189.793 255.444 1.00 28.59  ? 3583 PHE A O     1 
ATOM   14643 C  CB    . PHE A 1 3583 ? 208.058 189.615 252.421 1.00 16.29  ? 3583 PHE A CB    1 
ATOM   14644 C  CG    . PHE A 1 3583 ? 206.561 189.716 252.315 1.00 19.44  ? 3583 PHE A CG    1 
ATOM   14645 C  CD1   . PHE A 1 3583 ? 205.902 190.871 252.704 1.00 16.82  ? 3583 PHE A CD1   1 
ATOM   14646 C  CD2   . PHE A 1 3583 ? 205.814 188.664 251.816 1.00 20.68  ? 3583 PHE A CD2   1 
ATOM   14647 C  CE1   . PHE A 1 3583 ? 204.531 190.971 252.608 1.00 15.68  ? 3583 PHE A CE1   1 
ATOM   14648 C  CE2   . PHE A 1 3583 ? 204.439 188.761 251.717 1.00 21.81  ? 3583 PHE A CE2   1 
ATOM   14649 C  CZ    . PHE A 1 3583 ? 203.799 189.916 252.113 1.00 17.39  ? 3583 PHE A CZ    1 
ATOM   14650 N  N     . ASN A 1 3584 ? 208.955 190.925 255.263 1.00 18.71  ? 3584 ASN A N     1 
ATOM   14651 C  CA    . ASN A 1 3584 ? 208.612 191.963 256.227 1.00 16.71  ? 3584 ASN A CA    1 
ATOM   14652 C  C     . ASN A 1 3584 ? 208.140 193.240 255.545 1.00 21.00  ? 3584 ASN A C     1 
ATOM   14653 O  O     . ASN A 1 3584 ? 207.100 193.792 255.914 1.00 35.39  ? 3584 ASN A O     1 
ATOM   14654 C  CB    . ASN A 1 3584 ? 209.808 192.264 257.137 1.00 15.70  ? 3584 ASN A CB    1 
ATOM   14655 C  CG    . ASN A 1 3584 ? 210.255 191.053 257.925 1.00 23.90  ? 3584 ASN A CG    1 
ATOM   14656 O  OD1   . ASN A 1 3584 ? 211.432 190.697 257.920 1.00 25.13  ? 3584 ASN A OD1   1 
ATOM   14657 N  ND2   . ASN A 1 3584 ? 209.313 190.404 258.598 1.00 24.09  ? 3584 ASN A ND2   1 
ATOM   14658 N  N     . ARG A 1 3585 ? 208.886 193.725 254.556 1.00 12.57  ? 3585 ARG A N     1 
ATOM   14659 C  CA    . ARG A 1 3585 ? 208.404 194.791 253.692 1.00 12.83  ? 3585 ARG A CA    1 
ATOM   14660 C  C     . ARG A 1 3585 ? 207.668 194.197 252.501 1.00 16.24  ? 3585 ARG A C     1 
ATOM   14661 O  O     . ARG A 1 3585 ? 207.935 193.070 252.077 1.00 21.62  ? 3585 ARG A O     1 
ATOM   14662 C  CB    . ARG A 1 3585 ? 209.545 195.686 253.202 1.00 16.32  ? 3585 ARG A CB    1 
ATOM   14663 C  CG    . ARG A 1 3585 ? 210.240 196.472 254.292 1.00 14.58  ? 3585 ARG A CG    1 
ATOM   14664 C  CD    . ARG A 1 3585 ? 211.542 197.070 253.798 1.00 12.87  ? 3585 ARG A CD    1 
ATOM   14665 N  NE    . ARG A 1 3585 ? 212.458 196.066 253.277 1.00 13.29  ? 3585 ARG A NE    1 
ATOM   14666 C  CZ    . ARG A 1 3585 ? 213.498 196.336 252.500 1.00 13.00  ? 3585 ARG A CZ    1 
ATOM   14667 N  NH1   . ARG A 1 3585 ? 213.779 197.573 252.129 1.00 12.12  ? 3585 ARG A NH1   1 
ATOM   14668 N  NH2   . ARG A 1 3585 ? 214.274 195.341 252.086 1.00 13.01  ? 3585 ARG A NH2   1 
ATOM   14669 N  N     . TYR A 1 3586 ? 206.734 194.968 251.967 1.00 14.50  ? 3586 TYR A N     1 
ATOM   14670 C  CA    . TYR A 1 3586 ? 205.930 194.502 250.847 1.00 10.18  ? 3586 TYR A CA    1 
ATOM   14671 C  C     . TYR A 1 3586 ? 206.821 194.228 249.641 1.00 12.54  ? 3586 TYR A C     1 
ATOM   14672 O  O     . TYR A 1 3586 ? 207.692 195.045 249.322 1.00 11.47  ? 3586 TYR A O     1 
ATOM   14673 C  CB    . TYR A 1 3586 ? 204.864 195.529 250.495 1.00 13.92  ? 3586 TYR A CB    1 
ATOM   14674 C  CG    . TYR A 1 3586 ? 203.804 195.666 251.557 1.00 19.39  ? 3586 TYR A CG    1 
ATOM   14675 C  CD1   . TYR A 1 3586 ? 203.068 194.567 251.980 1.00 19.01  ? 3586 TYR A CD1   1 
ATOM   14676 C  CD2   . TYR A 1 3586 ? 203.552 196.892 252.156 1.00 21.57  ? 3586 TYR A CD2   1 
ATOM   14677 C  CE1   . TYR A 1 3586 ? 202.110 194.684 252.963 1.00 21.41  ? 3586 TYR A CE1   1 
ATOM   14678 C  CE2   . TYR A 1 3586 ? 202.593 197.018 253.139 1.00 28.21  ? 3586 TYR A CE2   1 
ATOM   14679 C  CZ    . TYR A 1 3586 ? 201.864 195.909 253.534 1.00 32.80  ? 3586 TYR A CZ    1 
ATOM   14680 O  OH    . TYR A 1 3586 ? 200.909 196.028 254.511 1.00 36.39  ? 3586 TYR A OH    1 
ATOM   14681 N  N     . PRO A 1 3587 ? 206.643 193.104 248.957 1.00 11.88  ? 3587 PRO A N     1 
ATOM   14682 C  CA    . PRO A 1 3587 ? 207.576 192.739 247.890 1.00 10.43  ? 3587 PRO A CA    1 
ATOM   14683 C  C     . PRO A 1 3587 ? 207.398 193.589 246.642 1.00 10.31  ? 3587 PRO A C     1 
ATOM   14684 O  O     . PRO A 1 3587 ? 206.304 194.066 246.331 1.00 12.02  ? 3587 PRO A O     1 
ATOM   14685 C  CB    . PRO A 1 3587 ? 207.239 191.269 247.607 1.00 8.00   ? 3587 PRO A CB    1 
ATOM   14686 C  CG    . PRO A 1 3587 ? 206.276 190.849 248.682 1.00 9.54   ? 3587 PRO A CG    1 
ATOM   14687 C  CD    . PRO A 1 3587 ? 205.601 192.085 249.150 1.00 9.49   ? 3587 PRO A CD    1 
ATOM   14688 N  N     . LEU A 1 3588 ? 208.500 193.765 245.921 1.00 9.20   ? 3588 LEU A N     1 
ATOM   14689 C  CA    . LEU A 1 3588 ? 208.492 194.310 244.571 1.00 9.06   ? 3588 LEU A CA    1 
ATOM   14690 C  C     . LEU A 1 3588 ? 208.919 193.196 243.627 1.00 13.15  ? 3588 LEU A C     1 
ATOM   14691 O  O     . LEU A 1 3588 ? 209.994 192.612 243.800 1.00 14.64  ? 3588 LEU A O     1 
ATOM   14692 C  CB    . LEU A 1 3588 ? 209.422 195.518 244.453 1.00 10.87  ? 3588 LEU A CB    1 
ATOM   14693 C  CG    . LEU A 1 3588 ? 209.223 196.431 243.239 1.00 12.36  ? 3588 LEU A CG    1 
ATOM   14694 C  CD1   . LEU A 1 3588 ? 209.526 197.872 243.606 1.00 16.54  ? 3588 LEU A CD1   1 
ATOM   14695 C  CD2   . LEU A 1 3588 ? 210.082 195.992 242.066 1.00 16.13  ? 3588 LEU A CD2   1 
ATOM   14696 N  N     . ILE A 1 3589 ? 208.080 192.900 242.638 1.00 13.34  ? 3589 ILE A N     1 
ATOM   14697 C  CA    . ILE A 1 3589 ? 208.287 191.772 241.739 1.00 12.40  ? 3589 ILE A CA    1 
ATOM   14698 C  C     . ILE A 1 3589 ? 208.831 192.284 240.414 1.00 14.91  ? 3589 ILE A C     1 
ATOM   14699 O  O     . ILE A 1 3589 ? 208.282 193.223 239.827 1.00 16.81  ? 3589 ILE A O     1 
ATOM   14700 C  CB    . ILE A 1 3589 ? 206.983 190.983 241.531 1.00 13.26  ? 3589 ILE A CB    1 
ATOM   14701 C  CG1   . ILE A 1 3589 ? 206.381 190.586 242.880 1.00 15.63  ? 3589 ILE A CG1   1 
ATOM   14702 C  CG2   . ILE A 1 3589 ? 207.236 189.758 240.674 1.00 15.38  ? 3589 ILE A CG2   1 
ATOM   14703 C  CD1   . ILE A 1 3589 ? 204.902 190.290 242.823 1.00 18.52  ? 3589 ILE A CD1   1 
ATOM   14704 N  N     . ILE A 1 3590 ? 209.915 191.669 239.947 1.00 14.41  ? 3590 ILE A N     1 
ATOM   14705 C  CA    . ILE A 1 3590 ? 210.486 191.996 238.646 1.00 17.17  ? 3590 ILE A CA    1 
ATOM   14706 C  C     . ILE A 1 3590 ? 210.395 190.773 237.744 1.00 20.82  ? 3590 ILE A C     1 
ATOM   14707 O  O     . ILE A 1 3590 ? 211.285 189.918 237.754 1.00 23.14  ? 3590 ILE A O     1 
ATOM   14708 C  CB    . ILE A 1 3590 ? 211.942 192.477 238.777 1.00 14.55  ? 3590 ILE A CB    1 
ATOM   14709 C  CG1   . ILE A 1 3590 ? 212.073 193.485 239.920 1.00 13.82  ? 3590 ILE A CG1   1 
ATOM   14710 C  CG2   . ILE A 1 3590 ? 212.429 193.079 237.468 1.00 19.08  ? 3590 ILE A CG2   1 
ATOM   14711 C  CD1   . ILE A 1 3590 ? 213.482 193.983 240.136 1.00 14.27  ? 3590 ILE A CD1   1 
ATOM   14712 N  N     . ASP A 1 3591 ? 209.319 190.679 236.964 1.00 21.38  ? 3591 ASP A N     1 
ATOM   14713 C  CA    . ASP A 1 3591 ? 209.138 189.582 236.017 1.00 23.86  ? 3591 ASP A CA    1 
ATOM   14714 C  C     . ASP A 1 3591 ? 208.924 190.104 234.600 1.00 23.27  ? 3591 ASP A C     1 
ATOM   14715 O  O     . ASP A 1 3591 ? 207.890 190.742 234.321 1.00 26.18  ? 3591 ASP A O     1 
ATOM   14716 C  CB    . ASP A 1 3591 ? 208.009 188.638 236.469 1.00 23.13  ? 3591 ASP A CB    1 
ATOM   14717 C  CG    . ASP A 1 3591 ? 206.635 189.310 236.557 1.00 37.35  ? 3591 ASP A CG    1 
ATOM   14718 O  OD1   . ASP A 1 3591 ? 206.501 190.526 236.327 1.00 40.50  ? 3591 ASP A OD1   1 
ATOM   14719 O  OD2   . ASP A 1 3591 ? 205.658 188.590 236.850 1.00 40.52  ? 3591 ASP A OD2   1 
ATOM   14720 N  N     . PRO A 1 3592 ? 209.861 189.886 233.684 1.00 21.95  ? 3592 PRO A N     1 
ATOM   14721 C  CA    . PRO A 1 3592 ? 209.619 190.275 232.290 1.00 22.14  ? 3592 PRO A CA    1 
ATOM   14722 C  C     . PRO A 1 3592 ? 208.712 189.287 231.575 1.00 22.28  ? 3592 PRO A C     1 
ATOM   14723 O  O     . PRO A 1 3592 ? 207.984 189.655 230.650 1.00 26.38  ? 3592 PRO A O     1 
ATOM   14724 C  CB    . PRO A 1 3592 ? 211.028 190.302 231.687 1.00 22.52  ? 3592 PRO A CB    1 
ATOM   14725 C  CG    . PRO A 1 3592 ? 211.790 189.315 232.496 1.00 23.27  ? 3592 PRO A CG    1 
ATOM   14726 C  CD    . PRO A 1 3592 ? 211.222 189.362 233.890 1.00 16.83  ? 3592 PRO A CD    1 
ATOM   14727 N  N     . SER A 1 3593 ? 208.745 188.024 232.006 1.00 24.94  ? 3593 SER A N     1 
ATOM   14728 C  CA    . SER A 1 3593 ? 207.884 187.007 231.416 1.00 24.86  ? 3593 SER A CA    1 
ATOM   14729 C  C     . SER A 1 3593 ? 206.443 187.121 231.898 1.00 26.13  ? 3593 SER A C     1 
ATOM   14730 O  O     . SER A 1 3593 ? 205.523 186.706 231.187 1.00 33.28  ? 3593 SER A O     1 
ATOM   14731 C  CB    . SER A 1 3593 ? 208.432 185.613 231.724 1.00 26.57  ? 3593 SER A CB    1 
ATOM   14732 O  OG    . SER A 1 3593 ? 208.372 185.338 233.112 1.00 28.60  ? 3593 SER A OG    1 
ATOM   14733 N  N     . GLY A 1 3594 ? 206.228 187.670 233.090 1.00 27.61  ? 3594 GLY A N     1 
ATOM   14734 C  CA    . GLY A 1 3594 ? 204.897 187.808 233.641 1.00 25.90  ? 3594 GLY A CA    1 
ATOM   14735 C  C     . GLY A 1 3594 ? 204.368 186.590 234.364 1.00 27.94  ? 3594 GLY A C     1 
ATOM   14736 O  O     . GLY A 1 3594 ? 203.202 186.595 234.777 1.00 33.94  ? 3594 GLY A O     1 
ATOM   14737 N  N     . GLN A 1 3595 ? 205.183 185.546 234.528 1.00 24.77  ? 3595 GLN A N     1 
ATOM   14738 C  CA    . GLN A 1 3595 ? 204.721 184.341 235.209 1.00 24.30  ? 3595 GLN A CA    1 
ATOM   14739 C  C     . GLN A 1 3595 ? 204.460 184.601 236.686 1.00 27.36  ? 3595 GLN A C     1 
ATOM   14740 O  O     . GLN A 1 3595 ? 203.541 184.016 237.274 1.00 34.26  ? 3595 GLN A O     1 
ATOM   14741 C  CB    . GLN A 1 3595 ? 205.745 183.221 235.039 1.00 29.66  ? 3595 GLN A CB    1 
ATOM   14742 C  CG    . GLN A 1 3595 ? 205.674 182.510 233.700 1.00 34.97  ? 3595 GLN A CG    1 
ATOM   14743 C  CD    . GLN A 1 3595 ? 206.645 181.351 233.611 1.00 46.24  ? 3595 GLN A CD    1 
ATOM   14744 O  OE1   . GLN A 1 3595 ? 207.858 181.534 233.711 1.00 47.90  ? 3595 GLN A OE1   1 
ATOM   14745 N  NE2   . GLN A 1 3595 ? 206.116 180.149 233.422 1.00 46.52  ? 3595 GLN A NE2   1 
ATOM   14746 N  N     . ALA A 1 3596 ? 205.264 185.468 237.307 1.00 24.54  ? 3596 ALA A N     1 
ATOM   14747 C  CA    . ALA A 1 3596 ? 205.105 185.737 238.732 1.00 19.48  ? 3596 ALA A CA    1 
ATOM   14748 C  C     . ALA A 1 3596 ? 203.777 186.423 239.023 1.00 24.87  ? 3596 ALA A C     1 
ATOM   14749 O  O     . ALA A 1 3596 ? 203.167 186.189 240.072 1.00 26.45  ? 3596 ALA A O     1 
ATOM   14750 C  CB    . ALA A 1 3596 ? 206.270 186.583 239.238 1.00 18.16  ? 3596 ALA A CB    1 
ATOM   14751 N  N     . THR A 1 3597 ? 203.317 187.284 238.113 1.00 28.39  ? 3597 THR A N     1 
ATOM   14752 C  CA    . THR A 1 3597 ? 202.015 187.919 238.288 1.00 30.03  ? 3597 THR A CA    1 
ATOM   14753 C  C     . THR A 1 3597 ? 200.900 186.879 238.314 1.00 37.28  ? 3597 THR A C     1 
ATOM   14754 O  O     . THR A 1 3597 ? 200.009 186.923 239.173 1.00 42.12  ? 3597 THR A O     1 
ATOM   14755 C  CB    . THR A 1 3597 ? 201.779 188.938 237.173 1.00 30.41  ? 3597 THR A CB    1 
ATOM   14756 O  OG1   . THR A 1 3597 ? 202.674 190.044 237.342 1.00 34.46  ? 3597 THR A OG1   1 
ATOM   14757 C  CG2   . THR A 1 3597 ? 200.346 189.443 237.197 1.00 39.78  ? 3597 THR A CG2   1 
ATOM   14758 N  N     . GLU A 1 3598 ? 200.949 185.919 237.388 1.00 35.90  ? 3598 GLU A N     1 
ATOM   14759 C  CA    . GLU A 1 3598 ? 199.955 184.852 237.374 1.00 35.13  ? 3598 GLU A CA    1 
ATOM   14760 C  C     . GLU A 1 3598 ? 200.057 183.987 238.624 1.00 33.05  ? 3598 GLU A C     1 
ATOM   14761 O  O     . GLU A 1 3598 ? 199.036 183.559 239.175 1.00 33.26  ? 3598 GLU A O     1 
ATOM   14762 C  CB    . GLU A 1 3598 ? 200.114 184.001 236.116 1.00 42.57  ? 3598 GLU A CB    1 
ATOM   14763 C  CG    . GLU A 1 3598 ? 199.781 184.731 234.826 1.00 56.02  ? 3598 GLU A CG    1 
ATOM   14764 C  CD    . GLU A 1 3598 ? 199.969 183.862 233.598 1.00 81.77  ? 3598 GLU A CD    1 
ATOM   14765 O  OE1   . GLU A 1 3598 ? 200.477 182.730 233.739 1.00 76.99  ? 3598 GLU A OE1   1 
ATOM   14766 O  OE2   . GLU A 1 3598 ? 199.604 184.310 232.489 1.00 94.98  ? 3598 GLU A OE2   1 
ATOM   14767 N  N     . PHE A 1 3599 ? 201.280 183.712 239.081 1.00 31.54  ? 3599 PHE A N     1 
ATOM   14768 C  CA    . PHE A 1 3599 ? 201.456 182.920 240.295 1.00 27.57  ? 3599 PHE A CA    1 
ATOM   14769 C  C     . PHE A 1 3599 ? 200.855 183.627 241.503 1.00 27.19  ? 3599 PHE A C     1 
ATOM   14770 O  O     . PHE A 1 3599 ? 200.182 183.001 242.330 1.00 31.20  ? 3599 PHE A O     1 
ATOM   14771 C  CB    . PHE A 1 3599 ? 202.941 182.633 240.517 1.00 21.55  ? 3599 PHE A CB    1 
ATOM   14772 C  CG    . PHE A 1 3599 ? 203.287 182.251 241.928 1.00 23.02  ? 3599 PHE A CG    1 
ATOM   14773 C  CD1   . PHE A 1 3599 ? 203.047 180.969 242.390 1.00 24.34  ? 3599 PHE A CD1   1 
ATOM   14774 C  CD2   . PHE A 1 3599 ? 203.861 183.169 242.790 1.00 24.09  ? 3599 PHE A CD2   1 
ATOM   14775 C  CE1   . PHE A 1 3599 ? 203.369 180.611 243.683 1.00 21.50  ? 3599 PHE A CE1   1 
ATOM   14776 C  CE2   . PHE A 1 3599 ? 204.183 182.817 244.085 1.00 20.41  ? 3599 PHE A CE2   1 
ATOM   14777 C  CZ    . PHE A 1 3599 ? 203.936 181.536 244.532 1.00 19.97  ? 3599 PHE A CZ    1 
ATOM   14778 N  N     . ILE A 1 3600 ? 201.085 184.937 241.617 1.00 27.02  ? 3600 ILE A N     1 
ATOM   14779 C  CA    . ILE A 1 3600 ? 200.512 185.710 242.715 1.00 30.25  ? 3600 ILE A CA    1 
ATOM   14780 C  C     . ILE A 1 3600 ? 198.992 185.711 242.630 1.00 28.09  ? 3600 ILE A C     1 
ATOM   14781 O  O     . ILE A 1 3600 ? 198.300 185.555 243.642 1.00 31.25  ? 3600 ILE A O     1 
ATOM   14782 C  CB    . ILE A 1 3600 ? 201.086 187.141 242.712 1.00 28.79  ? 3600 ILE A CB    1 
ATOM   14783 C  CG1   . ILE A 1 3600 ? 202.501 187.154 243.291 1.00 23.94  ? 3600 ILE A CG1   1 
ATOM   14784 C  CG2   . ILE A 1 3600 ? 200.192 188.086 243.497 1.00 24.08  ? 3600 ILE A CG2   1 
ATOM   14785 C  CD1   . ILE A 1 3600 ? 202.570 186.755 244.747 1.00 19.38  ? 3600 ILE A CD1   1 
ATOM   14786 N  N     . MET A 1 3601 ? 198.448 185.883 241.424 1.00 31.86  ? 3601 MET A N     1 
ATOM   14787 C  CA    . MET A 1 3601 ? 196.997 185.891 241.262 1.00 30.73  ? 3601 MET A CA    1 
ATOM   14788 C  C     . MET A 1 3601 ? 196.384 184.549 241.642 1.00 34.68  ? 3601 MET A C     1 
ATOM   14789 O  O     . MET A 1 3601 ? 195.319 184.499 242.267 1.00 35.66  ? 3601 MET A O     1 
ATOM   14790 C  CB    . MET A 1 3601 ? 196.632 186.262 239.828 1.00 28.70  ? 3601 MET A CB    1 
ATOM   14791 C  CG    . MET A 1 3601 ? 196.859 187.721 239.526 1.00 33.92  ? 3601 MET A CG    1 
ATOM   14792 S  SD    . MET A 1 3601 ? 195.631 188.732 240.365 1.00 41.75  ? 3601 MET A SD    1 
ATOM   14793 C  CE    . MET A 1 3601 ? 195.783 190.252 239.451 1.00 46.24  ? 3601 MET A CE    1 
ATOM   14794 N  N     . ASN A 1 3602 ? 197.033 183.449 241.259 1.00 32.55  ? 3602 ASN A N     1 
ATOM   14795 C  CA    . ASN A 1 3602 ? 196.529 182.130 241.623 1.00 28.79  ? 3602 ASN A CA    1 
ATOM   14796 C  C     . ASN A 1 3602 ? 196.629 181.893 243.124 1.00 28.37  ? 3602 ASN A C     1 
ATOM   14797 O  O     . ASN A 1 3602 ? 195.724 181.301 243.726 1.00 28.98  ? 3602 ASN A O     1 
ATOM   14798 C  CB    . ASN A 1 3602 ? 197.287 181.048 240.856 1.00 31.85  ? 3602 ASN A CB    1 
ATOM   14799 C  CG    . ASN A 1 3602 ? 197.130 181.182 239.355 1.00 32.70  ? 3602 ASN A CG    1 
ATOM   14800 O  OD1   . ASN A 1 3602 ? 196.060 181.531 238.860 1.00 34.72  ? 3602 ASN A OD1   1 
ATOM   14801 N  ND2   . ASN A 1 3602 ? 198.201 180.903 238.622 1.00 32.76  ? 3602 ASN A ND2   1 
ATOM   14802 N  N     . GLU A 1 3603 ? 197.720 182.343 243.747 1.00 30.03  ? 3603 GLU A N     1 
ATOM   14803 C  CA    . GLU A 1 3603 ? 197.912 182.102 245.174 1.00 29.28  ? 3603 GLU A CA    1 
ATOM   14804 C  C     . GLU A 1 3603 ? 196.886 182.850 246.015 1.00 29.24  ? 3603 GLU A C     1 
ATOM   14805 O  O     . GLU A 1 3603 ? 196.403 182.327 247.026 1.00 36.05  ? 3603 GLU A O     1 
ATOM   14806 C  CB    . GLU A 1 3603 ? 199.328 182.493 245.588 1.00 26.58  ? 3603 GLU A CB    1 
ATOM   14807 C  CG    . GLU A 1 3603 ? 200.380 181.480 245.192 1.00 27.98  ? 3603 GLU A CG    1 
ATOM   14808 C  CD    . GLU A 1 3603 ? 200.633 180.455 246.277 1.00 36.71  ? 3603 GLU A CD    1 
ATOM   14809 O  OE1   . GLU A 1 3603 ? 200.781 180.855 247.451 1.00 44.51  ? 3603 GLU A OE1   1 
ATOM   14810 O  OE2   . GLU A 1 3603 ? 200.682 179.249 245.957 1.00 38.94  ? 3603 GLU A OE2   1 
ATOM   14811 N  N     . TYR A 1 3604 ? 196.543 184.075 245.621 1.00 32.89  ? 3604 TYR A N     1 
ATOM   14812 C  CA    . TYR A 1 3604 ? 195.621 184.907 246.382 1.00 35.71  ? 3604 TYR A CA    1 
ATOM   14813 C  C     . TYR A 1 3604 ? 194.242 184.991 245.738 1.00 38.88  ? 3604 TYR A C     1 
ATOM   14814 O  O     . TYR A 1 3604 ? 193.502 185.945 245.996 1.00 45.95  ? 3604 TYR A O     1 
ATOM   14815 C  CB    . TYR A 1 3604 ? 196.212 186.304 246.571 1.00 33.87  ? 3604 TYR A CB    1 
ATOM   14816 C  CG    . TYR A 1 3604 ? 197.367 186.345 247.545 1.00 31.28  ? 3604 TYR A CG    1 
ATOM   14817 C  CD1   . TYR A 1 3604 ? 198.638 185.942 247.161 1.00 25.51  ? 3604 TYR A CD1   1 
ATOM   14818 C  CD2   . TYR A 1 3604 ? 197.185 186.784 248.849 1.00 33.91  ? 3604 TYR A CD2   1 
ATOM   14819 C  CE1   . TYR A 1 3604 ? 199.694 185.975 248.048 1.00 23.77  ? 3604 TYR A CE1   1 
ATOM   14820 C  CE2   . TYR A 1 3604 ? 198.237 186.822 249.741 1.00 33.22  ? 3604 TYR A CE2   1 
ATOM   14821 C  CZ    . TYR A 1 3604 ? 199.489 186.416 249.336 1.00 30.59  ? 3604 TYR A CZ    1 
ATOM   14822 O  OH    . TYR A 1 3604 ? 200.540 186.451 250.221 1.00 39.07  ? 3604 TYR A OH    1 
ATOM   14823 N  N     . LYS A 1 3605 ? 193.885 184.013 244.903 1.00 40.74  ? 3605 LYS A N     1 
ATOM   14824 C  CA    . LYS A 1 3605 ? 192.566 184.019 244.278 1.00 39.34  ? 3605 LYS A CA    1 
ATOM   14825 C  C     . LYS A 1 3605 ? 191.468 183.791 245.308 1.00 40.23  ? 3605 LYS A C     1 
ATOM   14826 O  O     . LYS A 1 3605 ? 190.366 184.339 245.184 1.00 45.91  ? 3605 LYS A O     1 
ATOM   14827 C  CB    . LYS A 1 3605 ? 192.504 182.961 243.178 1.00 35.52  ? 3605 LYS A CB    1 
ATOM   14828 C  CG    . LYS A 1 3605 ? 191.216 182.972 242.376 1.00 38.35  ? 3605 LYS A CG    1 
ATOM   14829 C  CD    . LYS A 1 3605 ? 191.199 181.855 241.348 1.00 45.11  ? 3605 LYS A CD    1 
ATOM   14830 C  CE    . LYS A 1 3605 ? 192.134 182.164 240.189 1.00 48.87  ? 3605 LYS A CE    1 
ATOM   14831 N  NZ    . LYS A 1 3605 ? 192.044 181.135 239.115 1.00 58.86  ? 3605 LYS A NZ    1 
ATOM   14832 N  N     . ASP A 1 3606 ? 191.748 182.981 246.331 1.00 40.21  ? 3606 ASP A N     1 
ATOM   14833 C  CA    . ASP A 1 3606 ? 190.750 182.709 247.360 1.00 44.29  ? 3606 ASP A CA    1 
ATOM   14834 C  C     . ASP A 1 3606 ? 190.392 183.973 248.129 1.00 50.56  ? 3606 ASP A C     1 
ATOM   14835 O  O     . ASP A 1 3606 ? 189.230 184.166 248.506 1.00 55.99  ? 3606 ASP A O     1 
ATOM   14836 C  CB    . ASP A 1 3606 ? 191.271 181.625 248.308 1.00 56.45  ? 3606 ASP A CB    1 
ATOM   14837 C  CG    . ASP A 1 3606 ? 190.203 181.100 249.257 1.00 71.68  ? 3606 ASP A CG    1 
ATOM   14838 O  OD1   . ASP A 1 3606 ? 189.051 181.577 249.208 1.00 70.44  ? 3606 ASP A OD1   1 
ATOM   14839 O  OD2   . ASP A 1 3606 ? 190.524 180.199 250.060 1.00 80.70  ? 3606 ASP A OD2   1 
ATOM   14840 N  N     . ARG A 1 3607 ? 191.365 184.852 248.354 1.00 50.75  ? 3607 ARG A N     1 
ATOM   14841 C  CA    . ARG A 1 3607 ? 191.151 186.100 249.073 1.00 45.80  ? 3607 ARG A CA    1 
ATOM   14842 C  C     . ARG A 1 3607 ? 190.728 187.244 248.159 1.00 44.04  ? 3607 ARG A C     1 
ATOM   14843 O  O     . ARG A 1 3607 ? 190.675 188.392 248.612 1.00 54.16  ? 3607 ARG A O     1 
ATOM   14844 C  CB    . ARG A 1 3607 ? 192.416 186.488 249.838 1.00 44.70  ? 3607 ARG A CB    1 
ATOM   14845 C  CG    . ARG A 1 3607 ? 192.413 186.060 251.295 1.00 45.68  ? 3607 ARG A CG    1 
ATOM   14846 C  CD    . ARG A 1 3607 ? 192.793 184.596 251.437 1.00 48.53  ? 3607 ARG A CD    1 
ATOM   14847 N  NE    . ARG A 1 3607 ? 194.130 184.317 250.926 1.00 52.21  ? 3607 ARG A NE    1 
ATOM   14848 C  CZ    . ARG A 1 3607 ? 195.257 184.706 251.508 1.00 47.86  ? 3607 ARG A CZ    1 
ATOM   14849 N  NH1   . ARG A 1 3607 ? 195.252 185.387 252.642 1.00 38.95  ? 3607 ARG A NH1   1 
ATOM   14850 N  NH2   . ARG A 1 3607 ? 196.420 184.397 250.941 1.00 42.70  ? 3607 ARG A NH2   1 
ATOM   14851 N  N     . LYS A 1 3608 ? 190.436 186.957 246.889 1.00 38.40  ? 3608 LYS A N     1 
ATOM   14852 C  CA    . LYS A 1 3608 ? 189.971 187.950 245.920 1.00 47.51  ? 3608 LYS A CA    1 
ATOM   14853 C  C     . LYS A 1 3608 ? 190.990 189.079 245.740 1.00 46.13  ? 3608 LYS A C     1 
ATOM   14854 O  O     . LYS A 1 3608 ? 190.726 190.248 246.021 1.00 46.31  ? 3608 LYS A O     1 
ATOM   14855 C  CB    . LYS A 1 3608 ? 188.597 188.505 246.319 1.00 53.43  ? 3608 LYS A CB    1 
ATOM   14856 C  CG    . LYS A 1 3608 ? 187.515 187.447 246.479 1.00 57.90  ? 3608 LYS A CG    1 
ATOM   14857 C  CD    . LYS A 1 3608 ? 187.094 186.864 245.134 1.00 58.08  ? 3608 LYS A CD    1 
ATOM   14858 C  CE    . LYS A 1 3608 ? 186.911 187.951 244.082 1.00 51.77  ? 3608 LYS A CE    1 
ATOM   14859 N  NZ    . LYS A 1 3608 ? 186.952 187.403 242.698 1.00 52.50  ? 3608 LYS A NZ    1 
ATOM   14860 N  N     . ILE A 1 3609 ? 192.173 188.699 245.256 1.00 41.97  ? 3609 ILE A N     1 
ATOM   14861 C  CA    . ILE A 1 3609 ? 193.181 189.684 244.885 1.00 36.46  ? 3609 ILE A CA    1 
ATOM   14862 C  C     . ILE A 1 3609 ? 192.768 190.365 243.587 1.00 33.64  ? 3609 ILE A C     1 
ATOM   14863 O  O     . ILE A 1 3609 ? 192.171 189.745 242.697 1.00 40.65  ? 3609 ILE A O     1 
ATOM   14864 C  CB    . ILE A 1 3609 ? 194.564 189.017 244.773 1.00 34.14  ? 3609 ILE A CB    1 
ATOM   14865 C  CG1   . ILE A 1 3609 ? 195.665 190.071 244.636 1.00 35.18  ? 3609 ILE A CG1   1 
ATOM   14866 C  CG2   . ILE A 1 3609 ? 194.596 188.008 243.637 1.00 36.76  ? 3609 ILE A CG2   1 
ATOM   14867 C  CD1   . ILE A 1 3609 ? 197.056 189.527 244.840 1.00 35.33  ? 3609 ILE A CD1   1 
ATOM   14868 N  N     . THR A 1 3610 ? 193.070 191.657 243.478 1.00 30.00  ? 3610 THR A N     1 
ATOM   14869 C  CA    . THR A 1 3610 ? 192.590 192.489 242.383 1.00 33.97  ? 3610 THR A CA    1 
ATOM   14870 C  C     . THR A 1 3610 ? 193.764 193.089 241.622 1.00 37.28  ? 3610 THR A C     1 
ATOM   14871 O  O     . THR A 1 3610 ? 194.756 193.508 242.228 1.00 37.27  ? 3610 THR A O     1 
ATOM   14872 C  CB    . THR A 1 3610 ? 191.679 193.601 242.909 1.00 35.78  ? 3610 THR A CB    1 
ATOM   14873 O  OG1   . THR A 1 3610 ? 190.666 193.032 243.745 1.00 38.95  ? 3610 THR A OG1   1 
ATOM   14874 C  CG2   . THR A 1 3610 ? 191.016 194.342 241.759 1.00 35.57  ? 3610 THR A CG2   1 
ATOM   14875 N  N     . ARG A 1 3611 ? 193.648 193.127 240.296 1.00 42.24  ? 3611 ARG A N     1 
ATOM   14876 C  CA    . ARG A 1 3611 ? 194.661 193.760 239.465 1.00 36.96  ? 3611 ARG A CA    1 
ATOM   14877 C  C     . ARG A 1 3611 ? 194.466 195.271 239.441 1.00 38.47  ? 3611 ARG A C     1 
ATOM   14878 O  O     . ARG A 1 3611 ? 193.339 195.768 239.365 1.00 37.33  ? 3611 ARG A O     1 
ATOM   14879 C  CB    . ARG A 1 3611 ? 194.608 193.205 238.041 1.00 48.66  ? 3611 ARG A CB    1 
ATOM   14880 C  CG    . ARG A 1 3611 ? 195.518 193.919 237.055 1.00 51.11  ? 3611 ARG A CG    1 
ATOM   14881 C  CD    . ARG A 1 3611 ? 196.896 193.283 237.021 1.00 53.12  ? 3611 ARG A CD    1 
ATOM   14882 N  NE    . ARG A 1 3611 ? 196.832 191.844 236.804 1.00 51.98  ? 3611 ARG A NE    1 
ATOM   14883 C  CZ    . ARG A 1 3611 ? 197.196 191.238 235.682 1.00 60.58  ? 3611 ARG A CZ    1 
ATOM   14884 N  NH1   . ARG A 1 3611 ? 197.666 191.919 234.651 1.00 62.69  ? 3611 ARG A NH1   1 
ATOM   14885 N  NH2   . ARG A 1 3611 ? 197.086 189.916 235.593 1.00 59.43  ? 3611 ARG A NH2   1 
ATOM   14886 N  N     . THR A 1 3612 ? 195.576 195.999 239.509 1.00 39.41  ? 3612 THR A N     1 
ATOM   14887 C  CA    . THR A 1 3612 ? 195.558 197.453 239.485 1.00 34.71  ? 3612 THR A CA    1 
ATOM   14888 C  C     . THR A 1 3612 ? 196.889 197.916 238.907 1.00 34.78  ? 3612 THR A C     1 
ATOM   14889 O  O     . THR A 1 3612 ? 197.866 197.166 238.877 1.00 46.00  ? 3612 THR A O     1 
ATOM   14890 C  CB    . THR A 1 3612 ? 195.298 198.016 240.892 1.00 42.55  ? 3612 THR A CB    1 
ATOM   14891 O  OG1   . THR A 1 3612 ? 194.044 197.521 241.375 1.00 53.29  ? 3612 THR A OG1   1 
ATOM   14892 C  CG2   . THR A 1 3612 ? 195.227 199.533 240.888 1.00 40.28  ? 3612 THR A CG2   1 
ATOM   14893 N  N     . SER A 1 3613 ? 196.912 199.148 238.404 1.00 34.09  ? 3613 SER A N     1 
ATOM   14894 C  CA    . SER A 1 3613 ? 198.142 199.766 237.933 1.00 36.83  ? 3613 SER A CA    1 
ATOM   14895 C  C     . SER A 1 3613 ? 198.207 201.196 238.449 1.00 42.42  ? 3613 SER A C     1 
ATOM   14896 O  O     . SER A 1 3613 ? 197.176 201.844 238.643 1.00 48.14  ? 3613 SER A O     1 
ATOM   14897 C  CB    . SER A 1 3613 ? 198.235 199.750 236.403 1.00 40.89  ? 3613 SER A CB    1 
ATOM   14898 O  OG    . SER A 1 3613 ? 199.377 200.456 235.955 1.00 42.50  ? 3613 SER A OG    1 
ATOM   14899 N  N     . PHE A 1 3614 ? 199.432 201.679 238.675 1.00 45.67  ? 3614 PHE A N     1 
ATOM   14900 C  CA    . PHE A 1 3614 ? 199.604 203.066 239.096 1.00 41.42  ? 3614 PHE A CA    1 
ATOM   14901 C  C     . PHE A 1 3614 ? 199.061 204.036 238.055 1.00 46.35  ? 3614 PHE A C     1 
ATOM   14902 O  O     . PHE A 1 3614 ? 198.547 205.103 238.408 1.00 51.66  ? 3614 PHE A O     1 
ATOM   14903 C  CB    . PHE A 1 3614 ? 201.081 203.367 239.367 1.00 43.38  ? 3614 PHE A CB    1 
ATOM   14904 C  CG    . PHE A 1 3614 ? 201.556 202.935 240.726 1.00 42.18  ? 3614 PHE A CG    1 
ATOM   14905 C  CD1   . PHE A 1 3614 ? 201.157 203.615 241.862 1.00 42.36  ? 3614 PHE A CD1   1 
ATOM   14906 C  CD2   . PHE A 1 3614 ? 202.444 201.884 240.862 1.00 35.28  ? 3614 PHE A CD2   1 
ATOM   14907 C  CE1   . PHE A 1 3614 ? 201.603 203.225 243.109 1.00 36.66  ? 3614 PHE A CE1   1 
ATOM   14908 C  CE2   . PHE A 1 3614 ? 202.891 201.492 242.104 1.00 33.37  ? 3614 PHE A CE2   1 
ATOM   14909 C  CZ    . PHE A 1 3614 ? 202.471 202.163 243.227 1.00 35.70  ? 3614 PHE A CZ    1 
ATOM   14910 N  N     . LEU A 1 3615 ? 199.166 203.686 236.771 1.00 44.71  ? 3615 LEU A N     1 
ATOM   14911 C  CA    . LEU A 1 3615 ? 198.646 204.543 235.714 1.00 46.42  ? 3615 LEU A CA    1 
ATOM   14912 C  C     . LEU A 1 3615 ? 197.124 204.563 235.676 1.00 52.77  ? 3615 LEU A C     1 
ATOM   14913 O  O     . LEU A 1 3615 ? 196.544 205.502 235.120 1.00 61.38  ? 3615 LEU A O     1 
ATOM   14914 C  CB    . LEU A 1 3615 ? 199.195 204.094 234.360 1.00 48.43  ? 3615 LEU A CB    1 
ATOM   14915 C  CG    . LEU A 1 3615 ? 200.717 204.111 234.222 1.00 48.63  ? 3615 LEU A CG    1 
ATOM   14916 C  CD1   . LEU A 1 3615 ? 201.135 203.703 232.820 1.00 42.09  ? 3615 LEU A CD1   1 
ATOM   14917 C  CD2   . LEU A 1 3615 ? 201.255 205.489 234.560 1.00 46.89  ? 3615 LEU A CD2   1 
ATOM   14918 N  N     . ASP A 1 3616 ? 196.468 203.554 236.244 1.00 49.95  ? 3616 ASP A N     1 
ATOM   14919 C  CA    . ASP A 1 3616 ? 195.013 203.526 236.260 1.00 55.05  ? 3616 ASP A CA    1 
ATOM   14920 C  C     . ASP A 1 3616 ? 194.467 204.667 237.109 1.00 60.66  ? 3616 ASP A C     1 
ATOM   14921 O  O     . ASP A 1 3616 ? 194.971 204.952 238.199 1.00 64.40  ? 3616 ASP A O     1 
ATOM   14922 C  CB    . ASP A 1 3616 ? 194.516 202.186 236.804 1.00 48.05  ? 3616 ASP A CB    1 
ATOM   14923 C  CG    . ASP A 1 3616 ? 194.518 201.096 235.754 1.00 54.34  ? 3616 ASP A CG    1 
ATOM   14924 O  OD1   . ASP A 1 3616 ? 194.959 201.364 234.617 1.00 62.24  ? 3616 ASP A OD1   1 
ATOM   14925 O  OD2   . ASP A 1 3616 ? 194.081 199.969 236.066 1.00 49.81  ? 3616 ASP A OD2   1 
ATOM   14926 N  N     . ASP A 1 3617 ? 193.424 205.325 236.598 1.00 57.56  ? 3617 ASP A N     1 
ATOM   14927 C  CA    . ASP A 1 3617 ? 192.801 206.411 237.346 1.00 62.26  ? 3617 ASP A CA    1 
ATOM   14928 C  C     . ASP A 1 3617 ? 192.053 205.894 238.567 1.00 63.08  ? 3617 ASP A C     1 
ATOM   14929 O  O     . ASP A 1 3617 ? 191.791 206.659 239.502 1.00 69.94  ? 3617 ASP A O     1 
ATOM   14930 C  CB    . ASP A 1 3617 ? 191.856 207.200 236.440 1.00 71.69  ? 3617 ASP A CB    1 
ATOM   14931 C  CG    . ASP A 1 3617 ? 190.907 206.307 235.668 1.00 78.69  ? 3617 ASP A CG    1 
ATOM   14932 O  OD1   . ASP A 1 3617 ? 191.076 205.070 235.722 1.00 79.78  ? 3617 ASP A OD1   1 
ATOM   14933 O  OD2   . ASP A 1 3617 ? 189.992 206.841 235.007 1.00 79.01  ? 3617 ASP A OD2   1 
ATOM   14934 N  N     . ALA A 1 3618 ? 191.703 204.610 238.580 1.00 57.62  ? 3618 ALA A N     1 
ATOM   14935 C  CA    . ALA A 1 3618 ? 190.977 204.014 239.693 1.00 56.79  ? 3618 ALA A CA    1 
ATOM   14936 C  C     . ALA A 1 3618 ? 191.893 203.422 240.754 1.00 52.76  ? 3618 ALA A C     1 
ATOM   14937 O  O     . ALA A 1 3618 ? 191.394 202.806 241.701 1.00 51.86  ? 3618 ALA A O     1 
ATOM   14938 C  CB    . ALA A 1 3618 ? 190.024 202.933 239.178 1.00 46.55  ? 3618 ALA A CB    1 
ATOM   14939 N  N     . PHE A 1 3619 ? 193.211 203.600 240.624 1.00 53.48  ? 3619 PHE A N     1 
ATOM   14940 C  CA    . PHE A 1 3619 ? 194.146 202.965 241.548 1.00 52.75  ? 3619 PHE A CA    1 
ATOM   14941 C  C     . PHE A 1 3619 ? 193.924 203.439 242.979 1.00 51.06  ? 3619 PHE A C     1 
ATOM   14942 O  O     . PHE A 1 3619 ? 194.022 202.647 243.923 1.00 45.26  ? 3619 PHE A O     1 
ATOM   14943 C  CB    . PHE A 1 3619 ? 195.583 203.237 241.106 1.00 44.60  ? 3619 PHE A CB    1 
ATOM   14944 C  CG    . PHE A 1 3619 ? 196.580 203.206 242.229 1.00 44.21  ? 3619 PHE A CG    1 
ATOM   14945 C  CD1   . PHE A 1 3619 ? 196.897 202.015 242.861 1.00 43.82  ? 3619 PHE A CD1   1 
ATOM   14946 C  CD2   . PHE A 1 3619 ? 197.202 204.368 242.651 1.00 40.50  ? 3619 PHE A CD2   1 
ATOM   14947 C  CE1   . PHE A 1 3619 ? 197.812 201.985 243.894 1.00 41.16  ? 3619 PHE A CE1   1 
ATOM   14948 C  CE2   . PHE A 1 3619 ? 198.118 204.343 243.683 1.00 43.34  ? 3619 PHE A CE2   1 
ATOM   14949 C  CZ    . PHE A 1 3619 ? 198.422 203.148 244.305 1.00 41.25  ? 3619 PHE A CZ    1 
ATOM   14950 N  N     . ARG A 1 3620 ? 193.631 204.728 243.159 1.00 55.19  ? 3620 ARG A N     1 
ATOM   14951 C  CA    . ARG A 1 3620 ? 193.392 205.250 244.501 1.00 49.24  ? 3620 ARG A CA    1 
ATOM   14952 C  C     . ARG A 1 3620 ? 192.208 204.554 245.160 1.00 47.56  ? 3620 ARG A C     1 
ATOM   14953 O  O     . ARG A 1 3620 ? 192.284 204.154 246.328 1.00 47.32  ? 3620 ARG A O     1 
ATOM   14954 C  CB    . ARG A 1 3620 ? 193.164 206.759 244.439 1.00 52.41  ? 3620 ARG A CB    1 
ATOM   14955 C  CG    . ARG A 1 3620 ? 194.353 207.546 243.909 1.00 53.46  ? 3620 ARG A CG    1 
ATOM   14956 C  CD    . ARG A 1 3620 ? 195.360 207.936 244.997 1.00 54.53  ? 3620 ARG A CD    1 
ATOM   14957 N  NE    . ARG A 1 3620 ? 194.762 208.632 246.131 1.00 56.99  ? 3620 ARG A NE    1 
ATOM   14958 C  CZ    . ARG A 1 3620 ? 194.309 208.043 247.232 1.00 58.28  ? 3620 ARG A CZ    1 
ATOM   14959 N  NH1   . ARG A 1 3620 ? 194.391 206.734 247.400 1.00 56.97  ? 3620 ARG A NH1   1 
ATOM   14960 N  NH2   . ARG A 1 3620 ? 193.767 208.790 248.191 1.00 52.79  ? 3620 ARG A NH2   1 
ATOM   14961 N  N     . LYS A 1 3621 ? 191.112 204.381 244.421 1.00 51.64  ? 3621 LYS A N     1 
ATOM   14962 C  CA    . LYS A 1 3621 ? 189.929 203.743 244.989 1.00 48.77  ? 3621 LYS A CA    1 
ATOM   14963 C  C     . LYS A 1 3621 ? 190.154 202.260 245.252 1.00 41.40  ? 3621 LYS A C     1 
ATOM   14964 O  O     . LYS A 1 3621 ? 189.698 201.737 246.275 1.00 43.42  ? 3621 LYS A O     1 
ATOM   14965 C  CB    . LYS A 1 3621 ? 188.726 203.950 244.068 1.00 55.71  ? 3621 LYS A CB    1 
ATOM   14966 C  CG    . LYS A 1 3621 ? 188.292 205.405 243.932 1.00 58.81  ? 3621 LYS A CG    1 
ATOM   14967 C  CD    . LYS A 1 3621 ? 187.732 205.970 245.236 1.00 64.49  ? 3621 LYS A CD    1 
ATOM   14968 C  CE    . LYS A 1 3621 ? 186.810 204.989 245.949 1.00 70.89  ? 3621 LYS A CE    1 
ATOM   14969 N  NZ    . LYS A 1 3621 ? 186.068 205.637 247.067 1.00 70.19  ? 3621 LYS A NZ    1 
ATOM   14970 N  N     . ASN A 1 3622 ? 190.848 201.565 244.346 1.00 43.72  ? 3622 ASN A N     1 
ATOM   14971 C  CA    . ASN A 1 3622 ? 191.164 200.160 244.588 1.00 44.50  ? 3622 ASN A CA    1 
ATOM   14972 C  C     . ASN A 1 3622 ? 192.035 200.000 245.827 1.00 45.50  ? 3622 ASN A C     1 
ATOM   14973 O  O     . ASN A 1 3622 ? 191.805 199.101 246.644 1.00 44.58  ? 3622 ASN A O     1 
ATOM   14974 C  CB    . ASN A 1 3622 ? 191.850 199.542 243.369 1.00 42.53  ? 3622 ASN A CB    1 
ATOM   14975 C  CG    . ASN A 1 3622 ? 190.958 199.516 242.145 1.00 49.07  ? 3622 ASN A CG    1 
ATOM   14976 O  OD1   . ASN A 1 3622 ? 191.232 200.180 241.147 1.00 55.21  ? 3622 ASN A OD1   1 
ATOM   14977 N  ND2   . ASN A 1 3622 ? 189.879 198.746 242.218 1.00 42.21  ? 3622 ASN A ND2   1 
ATOM   14978 N  N     . LEU A 1 3623 ? 193.036 200.868 245.985 1.00 44.97  ? 3623 LEU A N     1 
ATOM   14979 C  CA    . LEU A 1 3623 ? 193.897 200.806 247.161 1.00 38.52  ? 3623 LEU A CA    1 
ATOM   14980 C  C     . LEU A 1 3623 ? 193.110 201.096 248.434 1.00 38.34  ? 3623 LEU A C     1 
ATOM   14981 O  O     . LEU A 1 3623 ? 193.284 200.420 249.455 1.00 40.51  ? 3623 LEU A O     1 
ATOM   14982 C  CB    . LEU A 1 3623 ? 195.061 201.784 247.001 1.00 35.24  ? 3623 LEU A CB    1 
ATOM   14983 C  CG    . LEU A 1 3623 ? 195.853 202.156 248.252 1.00 35.58  ? 3623 LEU A CG    1 
ATOM   14984 C  CD1   . LEU A 1 3623 ? 196.765 201.014 248.664 1.00 36.93  ? 3623 LEU A CD1   1 
ATOM   14985 C  CD2   . LEU A 1 3623 ? 196.657 203.422 248.009 1.00 31.97  ? 3623 LEU A CD2   1 
ATOM   14986 N  N     . GLU A 1 3624 ? 192.230 202.100 248.387 1.00 41.01  ? 3624 GLU A N     1 
ATOM   14987 C  CA    . GLU A 1 3624 ? 191.414 202.429 249.551 1.00 45.73  ? 3624 GLU A CA    1 
ATOM   14988 C  C     . GLU A 1 3624 ? 190.519 201.260 249.943 1.00 44.17  ? 3624 GLU A C     1 
ATOM   14989 O  O     . GLU A 1 3624 ? 190.407 200.917 251.127 1.00 41.97  ? 3624 GLU A O     1 
ATOM   14990 C  CB    . GLU A 1 3624 ? 190.577 203.677 249.266 1.00 43.04  ? 3624 GLU A CB    1 
ATOM   14991 C  CG    . GLU A 1 3624 ? 189.745 204.152 250.445 1.00 54.88  ? 3624 GLU A CG    1 
ATOM   14992 C  CD    . GLU A 1 3624 ? 188.969 205.419 250.139 1.00 65.25  ? 3624 GLU A CD    1 
ATOM   14993 O  OE1   . GLU A 1 3624 ? 189.064 205.915 248.997 1.00 68.47  ? 3624 GLU A OE1   1 
ATOM   14994 O  OE2   . GLU A 1 3624 ? 188.260 205.917 251.039 1.00 60.77  ? 3624 GLU A OE2   1 
ATOM   14995 N  N     . SER A 1 3625 ? 189.873 200.633 248.957 1.00 41.29  ? 3625 SER A N     1 
ATOM   14996 C  CA    . SER A 1 3625 ? 189.011 199.492 249.244 1.00 40.28  ? 3625 SER A CA    1 
ATOM   14997 C  C     . SER A 1 3625 ? 189.814 198.321 249.792 1.00 45.00  ? 3625 SER A C     1 
ATOM   14998 O  O     . SER A 1 3625 ? 189.364 197.627 250.712 1.00 44.70  ? 3625 SER A O     1 
ATOM   14999 C  CB    . SER A 1 3625 ? 188.249 199.079 247.986 1.00 40.86  ? 3625 SER A CB    1 
ATOM   15000 O  OG    . SER A 1 3625 ? 189.095 199.094 246.852 1.00 41.96  ? 3625 SER A OG    1 
ATOM   15001 N  N     . ALA A 1 3626 ? 191.003 198.079 249.234 1.00 44.96  ? 3626 ALA A N     1 
ATOM   15002 C  CA    . ALA A 1 3626 ? 191.845 196.996 249.725 1.00 34.06  ? 3626 ALA A CA    1 
ATOM   15003 C  C     . ALA A 1 3626 ? 192.267 197.225 251.168 1.00 31.67  ? 3626 ALA A C     1 
ATOM   15004 O  O     . ALA A 1 3626 ? 192.280 196.282 251.966 1.00 32.98  ? 3626 ALA A O     1 
ATOM   15005 C  CB    . ALA A 1 3626 ? 193.073 196.837 248.829 1.00 35.54  ? 3626 ALA A CB    1 
ATOM   15006 N  N     . LEU A 1 3627 ? 192.618 198.462 251.523 1.00 36.03  ? 3627 LEU A N     1 
ATOM   15007 C  CA    . LEU A 1 3627 ? 192.979 198.744 252.908 1.00 33.59  ? 3627 LEU A CA    1 
ATOM   15008 C  C     . LEU A 1 3627 ? 191.777 198.629 253.838 1.00 40.73  ? 3627 LEU A C     1 
ATOM   15009 O  O     . LEU A 1 3627 ? 191.903 198.106 254.950 1.00 47.31  ? 3627 LEU A O     1 
ATOM   15010 C  CB    . LEU A 1 3627 ? 193.606 200.133 253.029 1.00 34.38  ? 3627 LEU A CB    1 
ATOM   15011 C  CG    . LEU A 1 3627 ? 194.892 200.392 252.245 1.00 32.32  ? 3627 LEU A CG    1 
ATOM   15012 C  CD1   . LEU A 1 3627 ? 194.921 201.827 251.771 1.00 33.78  ? 3627 LEU A CD1   1 
ATOM   15013 C  CD2   . LEU A 1 3627 ? 196.115 200.082 253.082 1.00 27.63  ? 3627 LEU A CD2   1 
ATOM   15014 N  N     . ARG A 1 3628 ? 190.609 199.112 253.407 1.00 43.55  ? 3628 ARG A N     1 
ATOM   15015 C  CA    . ARG A 1 3628 ? 189.437 199.091 254.278 1.00 37.60  ? 3628 ARG A CA    1 
ATOM   15016 C  C     . ARG A 1 3628 ? 188.949 197.668 254.521 1.00 43.02  ? 3628 ARG A C     1 
ATOM   15017 O  O     . ARG A 1 3628 ? 188.669 197.285 255.663 1.00 44.02  ? 3628 ARG A O     1 
ATOM   15018 C  CB    . ARG A 1 3628 ? 188.319 199.946 253.678 1.00 42.90  ? 3628 ARG A CB    1 
ATOM   15019 C  CG    . ARG A 1 3628 ? 188.546 201.440 253.814 1.00 51.84  ? 3628 ARG A CG    1 
ATOM   15020 C  CD    . ARG A 1 3628 ? 187.254 202.229 253.683 1.00 47.80  ? 3628 ARG A CD    1 
ATOM   15021 N  NE    . ARG A 1 3628 ? 187.508 203.621 253.334 1.00 58.03  ? 3628 ARG A NE    1 
ATOM   15022 C  CZ    . ARG A 1 3628 ? 187.707 204.593 254.215 1.00 67.03  ? 3628 ARG A CZ    1 
ATOM   15023 N  NH1   . ARG A 1 3628 ? 187.695 204.360 255.516 1.00 60.57  ? 3628 ARG A NH1   1 
ATOM   15024 N  NH2   . ARG A 1 3628 ? 187.925 205.829 253.777 1.00 65.27  ? 3628 ARG A NH2   1 
ATOM   15025 N  N     . PHE A 1 3629 ? 188.840 196.870 253.462 1.00 42.21  ? 3629 PHE A N     1 
ATOM   15026 C  CA    . PHE A 1 3629 ? 188.292 195.524 253.566 1.00 38.76  ? 3629 PHE A CA    1 
ATOM   15027 C  C     . PHE A 1 3629 ? 189.360 194.456 253.754 1.00 39.73  ? 3629 PHE A C     1 
ATOM   15028 O  O     . PHE A 1 3629 ? 189.018 193.272 253.841 1.00 45.30  ? 3629 PHE A O     1 
ATOM   15029 C  CB    . PHE A 1 3629 ? 187.452 195.195 252.325 1.00 46.29  ? 3629 PHE A CB    1 
ATOM   15030 C  CG    . PHE A 1 3629 ? 186.458 196.263 251.957 1.00 49.25  ? 3629 PHE A CG    1 
ATOM   15031 C  CD1   . PHE A 1 3629 ? 185.851 197.038 252.934 1.00 44.23  ? 3629 PHE A CD1   1 
ATOM   15032 C  CD2   . PHE A 1 3629 ? 186.133 196.494 250.631 1.00 51.14  ? 3629 PHE A CD2   1 
ATOM   15033 C  CE1   . PHE A 1 3629 ? 184.943 198.018 252.595 1.00 48.96  ? 3629 PHE A CE1   1 
ATOM   15034 C  CE2   . PHE A 1 3629 ? 185.224 197.474 250.286 1.00 51.79  ? 3629 PHE A CE2   1 
ATOM   15035 C  CZ    . PHE A 1 3629 ? 184.628 198.237 251.269 1.00 56.81  ? 3629 PHE A CZ    1 
ATOM   15036 N  N     . GLY A 1 3630 ? 190.630 194.837 253.824 1.00 36.09  ? 3630 GLY A N     1 
ATOM   15037 C  CA    . GLY A 1 3630 ? 191.694 193.863 254.000 1.00 36.07  ? 3630 GLY A CA    1 
ATOM   15038 C  C     . GLY A 1 3630 ? 191.849 192.901 252.843 1.00 37.80  ? 3630 GLY A C     1 
ATOM   15039 O  O     . GLY A 1 3630 ? 192.024 191.696 253.063 1.00 43.47  ? 3630 GLY A O     1 
ATOM   15040 N  N     . ASN A 1 3631 ? 191.790 193.401 251.614 1.00 32.64  ? 3631 ASN A N     1 
ATOM   15041 C  CA    . ASN A 1 3631 ? 191.903 192.478 250.495 1.00 34.28  ? 3631 ASN A CA    1 
ATOM   15042 C  C     . ASN A 1 3631 ? 193.274 192.590 249.840 1.00 39.58  ? 3631 ASN A C     1 
ATOM   15043 O  O     . ASN A 1 3631 ? 193.836 193.688 249.763 1.00 34.67  ? 3631 ASN A O     1 
ATOM   15044 C  CB    . ASN A 1 3631 ? 190.821 192.759 249.453 1.00 39.91  ? 3631 ASN A CB    1 
ATOM   15045 C  CG    . ASN A 1 3631 ? 189.423 192.637 250.020 1.00 40.42  ? 3631 ASN A CG    1 
ATOM   15046 O  OD1   . ASN A 1 3631 ? 189.167 191.821 250.904 1.00 41.50  ? 3631 ASN A OD1   1 
ATOM   15047 N  ND2   . ASN A 1 3631 ? 188.506 193.452 249.512 1.00 39.30  ? 3631 ASN A ND2   1 
ATOM   15048 N  N     . PRO A 1 3632 ? 193.831 191.473 249.376 1.00 41.57  ? 3632 PRO A N     1 
ATOM   15049 C  CA    . PRO A 1 3632 ? 195.109 191.533 248.659 1.00 30.03  ? 3632 PRO A CA    1 
ATOM   15050 C  C     . PRO A 1 3632 ? 194.997 192.379 247.401 1.00 31.15  ? 3632 PRO A C     1 
ATOM   15051 O  O     . PRO A 1 3632 ? 193.978 192.365 246.707 1.00 37.43  ? 3632 PRO A O     1 
ATOM   15052 C  CB    . PRO A 1 3632 ? 195.397 190.065 248.328 1.00 36.35  ? 3632 PRO A CB    1 
ATOM   15053 C  CG    . PRO A 1 3632 ? 194.646 189.297 249.360 1.00 39.34  ? 3632 PRO A CG    1 
ATOM   15054 C  CD    . PRO A 1 3632 ? 193.394 190.086 249.610 1.00 40.89  ? 3632 PRO A CD    1 
ATOM   15055 N  N     . LEU A 1 3633 ? 196.061 193.122 247.110 1.00 30.98  ? 3633 LEU A N     1 
ATOM   15056 C  CA    . LEU A 1 3633 ? 196.103 194.025 245.971 1.00 27.10  ? 3633 LEU A CA    1 
ATOM   15057 C  C     . LEU A 1 3633 ? 197.435 193.874 245.252 1.00 26.06  ? 3633 LEU A C     1 
ATOM   15058 O  O     . LEU A 1 3633 ? 198.484 193.756 245.890 1.00 28.40  ? 3633 LEU A O     1 
ATOM   15059 C  CB    . LEU A 1 3633 ? 195.901 195.479 246.417 1.00 23.23  ? 3633 LEU A CB    1 
ATOM   15060 C  CG    . LEU A 1 3633 ? 196.088 196.580 245.373 1.00 33.01  ? 3633 LEU A CG    1 
ATOM   15061 C  CD1   . LEU A 1 3633 ? 194.963 196.552 244.353 1.00 30.58  ? 3633 LEU A CD1   1 
ATOM   15062 C  CD2   . LEU A 1 3633 ? 196.173 197.942 246.042 1.00 29.03  ? 3633 LEU A CD2   1 
ATOM   15063 N  N     . LEU A 1 3634 ? 197.388 193.873 243.923 1.00 23.28  ? 3634 LEU A N     1 
ATOM   15064 C  CA    . LEU A 1 3634 ? 198.585 193.789 243.094 1.00 21.15  ? 3634 LEU A CA    1 
ATOM   15065 C  C     . LEU A 1 3634 ? 198.590 194.964 242.132 1.00 25.96  ? 3634 LEU A C     1 
ATOM   15066 O  O     . LEU A 1 3634 ? 197.585 195.221 241.461 1.00 37.98  ? 3634 LEU A O     1 
ATOM   15067 C  CB    . LEU A 1 3634 ? 198.638 192.462 242.330 1.00 22.70  ? 3634 LEU A CB    1 
ATOM   15068 C  CG    . LEU A 1 3634 ? 199.679 192.355 241.214 1.00 23.04  ? 3634 LEU A CG    1 
ATOM   15069 C  CD1   . LEU A 1 3634 ? 201.044 192.015 241.780 1.00 20.02  ? 3634 LEU A CD1   1 
ATOM   15070 C  CD2   . LEU A 1 3634 ? 199.257 191.322 240.187 1.00 25.90  ? 3634 LEU A CD2   1 
ATOM   15071 N  N     . VAL A 1 3635 ? 199.712 195.676 242.067 1.00 19.62  ? 3635 VAL A N     1 
ATOM   15072 C  CA    . VAL A 1 3635 ? 199.876 196.819 241.176 1.00 23.80  ? 3635 VAL A CA    1 
ATOM   15073 C  C     . VAL A 1 3635 ? 201.024 196.511 240.225 1.00 29.16  ? 3635 VAL A C     1 
ATOM   15074 O  O     . VAL A 1 3635 ? 202.108 196.111 240.664 1.00 32.21  ? 3635 VAL A O     1 
ATOM   15075 C  CB    . VAL A 1 3635 ? 200.128 198.117 241.961 1.00 28.92  ? 3635 VAL A CB    1 
ATOM   15076 C  CG1   . VAL A 1 3635 ? 200.370 199.257 241.005 1.00 37.60  ? 3635 VAL A CG1   1 
ATOM   15077 C  CG2   . VAL A 1 3635 ? 198.954 198.424 242.874 1.00 25.50  ? 3635 VAL A CG2   1 
ATOM   15078 N  N     . GLN A 1 3636 ? 200.789 196.700 238.926 1.00 29.51  ? 3636 GLN A N     1 
ATOM   15079 C  CA    . GLN A 1 3636 ? 201.632 196.097 237.901 1.00 32.60  ? 3636 GLN A CA    1 
ATOM   15080 C  C     . GLN A 1 3636 ? 202.589 197.061 237.207 1.00 33.54  ? 3636 GLN A C     1 
ATOM   15081 O  O     . GLN A 1 3636 ? 203.405 196.606 236.399 1.00 37.01  ? 3636 GLN A O     1 
ATOM   15082 C  CB    . GLN A 1 3636 ? 200.760 195.415 236.839 1.00 35.21  ? 3636 GLN A CB    1 
ATOM   15083 C  CG    . GLN A 1 3636 ? 199.891 196.367 236.043 1.00 39.91  ? 3636 GLN A CG    1 
ATOM   15084 C  CD    . GLN A 1 3636 ? 199.010 195.650 235.044 1.00 49.98  ? 3636 GLN A CD    1 
ATOM   15085 O  OE1   . GLN A 1 3636 ? 199.081 194.429 234.903 1.00 51.38  ? 3636 GLN A OE1   1 
ATOM   15086 N  NE2   . GLN A 1 3636 ? 198.177 196.406 234.339 1.00 55.40  ? 3636 GLN A NE2   1 
ATOM   15087 N  N     . ASP A 1 3637 ? 202.525 198.366 237.484 1.00 31.84  ? 3637 ASP A N     1 
ATOM   15088 C  CA    . ASP A 1 3637 ? 203.402 199.338 236.818 1.00 35.18  ? 3637 ASP A CA    1 
ATOM   15089 C  C     . ASP A 1 3637 ? 204.056 200.217 237.885 1.00 39.22  ? 3637 ASP A C     1 
ATOM   15090 O  O     . ASP A 1 3637 ? 203.595 201.325 238.159 1.00 45.86  ? 3637 ASP A O     1 
ATOM   15091 C  CB    . ASP A 1 3637 ? 202.619 200.167 235.796 1.00 41.31  ? 3637 ASP A CB    1 
ATOM   15092 C  CG    . ASP A 1 3637 ? 202.303 199.390 234.531 1.00 48.16  ? 3637 ASP A CG    1 
ATOM   15093 O  OD1   . ASP A 1 3637 ? 201.236 198.746 234.479 1.00 46.37  ? 3637 ASP A OD1   1 
ATOM   15094 O  OD2   . ASP A 1 3637 ? 203.117 199.421 233.587 1.00 52.96  ? 3637 ASP A OD2   1 
ATOM   15095 N  N     . VAL A 1 3638 ? 205.161 199.728 238.457 1.00 34.26  ? 3638 VAL A N     1 
ATOM   15096 C  CA    . VAL A 1 3638 ? 205.808 200.416 239.573 1.00 26.65  ? 3638 VAL A CA    1 
ATOM   15097 C  C     . VAL A 1 3638 ? 206.769 201.501 239.103 1.00 35.76  ? 3638 VAL A C     1 
ATOM   15098 O  O     . VAL A 1 3638 ? 207.189 202.341 239.914 1.00 41.23  ? 3638 VAL A O     1 
ATOM   15099 C  CB    . VAL A 1 3638 ? 206.536 199.389 240.468 1.00 22.08  ? 3638 VAL A CB    1 
ATOM   15100 C  CG1   . VAL A 1 3638 ? 207.677 198.737 239.714 1.00 22.73  ? 3638 VAL A CG1   1 
ATOM   15101 C  CG2   . VAL A 1 3638 ? 206.997 200.004 241.789 1.00 28.30  ? 3638 VAL A CG2   1 
ATOM   15102 N  N     . GLU A 1 3639 ? 207.112 201.529 237.813 1.00 37.54  ? 3639 GLU A N     1 
ATOM   15103 C  CA    . GLU A 1 3639 ? 207.937 202.595 237.257 1.00 33.67  ? 3639 GLU A CA    1 
ATOM   15104 C  C     . GLU A 1 3639 ? 207.303 203.968 237.431 1.00 34.04  ? 3639 GLU A C     1 
ATOM   15105 O  O     . GLU A 1 3639 ? 208.018 204.975 237.387 1.00 45.73  ? 3639 GLU A O     1 
ATOM   15106 C  CB    . GLU A 1 3639 ? 208.187 202.337 235.771 1.00 36.13  ? 3639 GLU A CB    1 
ATOM   15107 C  CG    . GLU A 1 3639 ? 206.938 202.497 234.924 1.00 45.94  ? 3639 GLU A CG    1 
ATOM   15108 C  CD    . GLU A 1 3639 ? 206.091 201.244 234.884 1.00 49.94  ? 3639 GLU A CD    1 
ATOM   15109 O  OE1   . GLU A 1 3639 ? 206.297 200.352 235.733 1.00 49.67  ? 3639 GLU A OE1   1 
ATOM   15110 O  OE2   . GLU A 1 3639 ? 205.197 201.164 234.021 1.00 50.98  ? 3639 GLU A OE2   1 
ATOM   15111 N  N     . SER A 1 3640 ? 205.989 204.026 237.625 1.00 30.14  ? 3640 SER A N     1 
ATOM   15112 C  CA    . SER A 1 3640 ? 205.258 205.255 237.901 1.00 36.57  ? 3640 SER A CA    1 
ATOM   15113 C  C     . SER A 1 3640 ? 204.699 205.225 239.319 1.00 36.21  ? 3640 SER A C     1 
ATOM   15114 O  O     . SER A 1 3640 ? 203.536 205.553 239.558 1.00 37.96  ? 3640 SER A O     1 
ATOM   15115 C  CB    . SER A 1 3640 ? 204.142 205.464 236.883 1.00 46.75  ? 3640 SER A CB    1 
ATOM   15116 O  OG    . SER A 1 3640 ? 203.097 204.527 237.077 1.00 47.50  ? 3640 SER A OG    1 
ATOM   15117 N  N     . TYR A 1 3641 ? 205.535 204.798 240.265 1.00 35.96  ? 3641 TYR A N     1 
ATOM   15118 C  CA    . TYR A 1 3641 ? 205.124 204.656 241.654 1.00 33.70  ? 3641 TYR A CA    1 
ATOM   15119 C  C     . TYR A 1 3641 ? 204.569 205.967 242.196 1.00 34.12  ? 3641 TYR A C     1 
ATOM   15120 O  O     . TYR A 1 3641 ? 205.198 207.022 242.073 1.00 38.11  ? 3641 TYR A O     1 
ATOM   15121 C  CB    . TYR A 1 3641 ? 206.314 204.195 242.494 1.00 30.15  ? 3641 TYR A CB    1 
ATOM   15122 C  CG    . TYR A 1 3641 ? 206.117 204.306 243.988 1.00 28.32  ? 3641 TYR A CG    1 
ATOM   15123 C  CD1   . TYR A 1 3641 ? 205.314 203.405 244.671 1.00 26.92  ? 3641 TYR A CD1   1 
ATOM   15124 C  CD2   . TYR A 1 3641 ? 206.746 205.306 244.717 1.00 25.53  ? 3641 TYR A CD2   1 
ATOM   15125 C  CE1   . TYR A 1 3641 ? 205.137 203.501 246.036 1.00 29.87  ? 3641 TYR A CE1   1 
ATOM   15126 C  CE2   . TYR A 1 3641 ? 206.574 205.411 246.081 1.00 23.56  ? 3641 TYR A CE2   1 
ATOM   15127 C  CZ    . TYR A 1 3641 ? 205.770 204.507 246.735 1.00 26.76  ? 3641 TYR A CZ    1 
ATOM   15128 O  OH    . TYR A 1 3641 ? 205.595 204.606 248.095 1.00 27.75  ? 3641 TYR A OH    1 
ATOM   15129 N  N     . ASP A 1 3642 ? 203.384 205.894 242.796 1.00 32.61  ? 3642 ASP A N     1 
ATOM   15130 C  CA    . ASP A 1 3642 ? 202.739 207.068 243.361 1.00 33.71  ? 3642 ASP A CA    1 
ATOM   15131 C  C     . ASP A 1 3642 ? 203.109 207.173 244.834 1.00 34.17  ? 3642 ASP A C     1 
ATOM   15132 O  O     . ASP A 1 3642 ? 202.943 206.193 245.571 1.00 34.85  ? 3642 ASP A O     1 
ATOM   15133 C  CB    . ASP A 1 3642 ? 201.230 206.981 243.202 1.00 38.26  ? 3642 ASP A CB    1 
ATOM   15134 C  CG    . ASP A 1 3642 ? 200.527 208.290 243.525 1.00 46.85  ? 3642 ASP A CG    1 
ATOM   15135 O  OD1   . ASP A 1 3642 ? 199.873 208.846 242.618 1.00 47.37  ? 3642 ASP A OD1   1 
ATOM   15136 O  OD2   . ASP A 1 3642 ? 200.633 208.773 244.671 1.00 43.86  ? 3642 ASP A OD2   1 
ATOM   15137 N  N     . PRO A 1 3643 ? 203.614 208.318 245.303 1.00 33.29  ? 3643 PRO A N     1 
ATOM   15138 C  CA    . PRO A 1 3643 ? 204.047 208.416 246.707 1.00 26.61  ? 3643 PRO A CA    1 
ATOM   15139 C  C     . PRO A 1 3643 ? 202.926 208.240 247.725 1.00 25.85  ? 3643 PRO A C     1 
ATOM   15140 O  O     . PRO A 1 3643 ? 203.214 208.229 248.927 1.00 25.10  ? 3643 PRO A O     1 
ATOM   15141 C  CB    . PRO A 1 3643 ? 204.655 209.823 246.792 1.00 26.89  ? 3643 PRO A CB    1 
ATOM   15142 C  CG    . PRO A 1 3643 ? 204.992 210.180 245.378 1.00 33.64  ? 3643 PRO A CG    1 
ATOM   15143 C  CD    . PRO A 1 3643 ? 203.930 209.537 244.543 1.00 36.26  ? 3643 PRO A CD    1 
ATOM   15144 N  N     . VAL A 1 3644 ? 201.671 208.090 247.289 1.00 27.13  ? 3644 VAL A N     1 
ATOM   15145 C  CA    . VAL A 1 3644 ? 200.570 207.887 248.225 1.00 30.49  ? 3644 VAL A CA    1 
ATOM   15146 C  C     . VAL A 1 3644 ? 200.781 206.626 249.048 1.00 28.79  ? 3644 VAL A C     1 
ATOM   15147 O  O     . VAL A 1 3644 ? 200.281 206.526 250.173 1.00 29.38  ? 3644 VAL A O     1 
ATOM   15148 C  CB    . VAL A 1 3644 ? 199.223 207.838 247.467 1.00 34.80  ? 3644 VAL A CB    1 
ATOM   15149 C  CG1   . VAL A 1 3644 ? 199.191 206.665 246.495 1.00 38.39  ? 3644 VAL A CG1   1 
ATOM   15150 C  CG2   . VAL A 1 3644 ? 198.046 207.784 248.434 1.00 34.73  ? 3644 VAL A CG2   1 
ATOM   15151 N  N     . LEU A 1 3645 ? 201.538 205.667 248.525 1.00 30.17  ? 3645 LEU A N     1 
ATOM   15152 C  CA    . LEU A 1 3645 ? 201.820 204.419 249.215 1.00 25.22  ? 3645 LEU A CA    1 
ATOM   15153 C  C     . LEU A 1 3645 ? 202.938 204.542 250.240 1.00 21.99  ? 3645 LEU A C     1 
ATOM   15154 O  O     . LEU A 1 3645 ? 203.232 203.559 250.929 1.00 20.72  ? 3645 LEU A O     1 
ATOM   15155 C  CB    . LEU A 1 3645 ? 202.179 203.332 248.198 1.00 26.49  ? 3645 LEU A CB    1 
ATOM   15156 C  CG    . LEU A 1 3645 ? 201.019 202.516 247.633 1.00 29.00  ? 3645 LEU A CG    1 
ATOM   15157 C  CD1   . LEU A 1 3645 ? 201.515 201.575 246.554 1.00 27.91  ? 3645 LEU A CD1   1 
ATOM   15158 C  CD2   . LEU A 1 3645 ? 200.318 201.748 248.736 1.00 24.49  ? 3645 LEU A CD2   1 
ATOM   15159 N  N     . ASN A 1 3646 ? 203.573 205.711 250.355 1.00 22.47  ? 3646 ASN A N     1 
ATOM   15160 C  CA    . ASN A 1 3646 ? 204.682 205.857 251.298 1.00 20.43  ? 3646 ASN A CA    1 
ATOM   15161 C  C     . ASN A 1 3646 ? 204.283 205.543 252.734 1.00 23.71  ? 3646 ASN A C     1 
ATOM   15162 O  O     . ASN A 1 3646 ? 205.006 204.777 253.394 1.00 28.09  ? 3646 ASN A O     1 
ATOM   15163 C  CB    . ASN A 1 3646 ? 205.288 207.261 251.179 1.00 18.26  ? 3646 ASN A CB    1 
ATOM   15164 C  CG    . ASN A 1 3646 ? 206.100 207.440 249.915 1.00 18.17  ? 3646 ASN A CG    1 
ATOM   15165 O  OD1   . ASN A 1 3646 ? 206.197 206.531 249.092 1.00 26.08  ? 3646 ASN A OD1   1 
ATOM   15166 N  ND2   . ASN A 1 3646 ? 206.695 208.616 249.756 1.00 16.69  ? 3646 ASN A ND2   1 
ATOM   15167 N  N     . PRO A 1 3647 ? 203.188 206.080 253.287 1.00 22.13  ? 3647 PRO A N     1 
ATOM   15168 C  CA    . PRO A 1 3647 ? 202.776 205.631 254.627 1.00 20.92  ? 3647 PRO A CA    1 
ATOM   15169 C  C     . PRO A 1 3647 ? 202.415 204.158 254.682 1.00 22.98  ? 3647 PRO A C     1 
ATOM   15170 O  O     . PRO A 1 3647 ? 202.631 203.515 255.717 1.00 24.40  ? 3647 PRO A O     1 
ATOM   15171 C  CB    . PRO A 1 3647 ? 201.567 206.525 254.941 1.00 24.70  ? 3647 PRO A CB    1 
ATOM   15172 C  CG    . PRO A 1 3647 ? 201.080 206.982 253.616 1.00 26.90  ? 3647 PRO A CG    1 
ATOM   15173 C  CD    . PRO A 1 3647 ? 202.305 207.149 252.787 1.00 21.46  ? 3647 PRO A CD    1 
ATOM   15174 N  N     . VAL A 1 3648 ? 201.864 203.605 253.600 1.00 22.01  ? 3648 VAL A N     1 
ATOM   15175 C  CA    . VAL A 1 3648 ? 201.465 202.201 253.600 1.00 20.09  ? 3648 VAL A CA    1 
ATOM   15176 C  C     . VAL A 1 3648 ? 202.686 201.292 253.609 1.00 17.73  ? 3648 VAL A C     1 
ATOM   15177 O  O     . VAL A 1 3648 ? 202.734 200.301 254.348 1.00 19.75  ? 3648 VAL A O     1 
ATOM   15178 C  CB    . VAL A 1 3648 ? 200.547 201.909 252.399 1.00 24.09  ? 3648 VAL A CB    1 
ATOM   15179 C  CG1   . VAL A 1 3648 ? 200.148 200.443 252.378 1.00 23.62  ? 3648 VAL A CG1   1 
ATOM   15180 C  CG2   . VAL A 1 3648 ? 199.318 202.800 252.445 1.00 26.71  ? 3648 VAL A CG2   1 
ATOM   15181 N  N     . LEU A 1 3649 ? 203.689 201.608 252.789 1.00 22.71  ? 3649 LEU A N     1 
ATOM   15182 C  CA    . LEU A 1 3649 ? 204.884 200.771 252.727 1.00 17.20  ? 3649 LEU A CA    1 
ATOM   15183 C  C     . LEU A 1 3649 ? 205.671 200.832 254.029 1.00 20.11  ? 3649 LEU A C     1 
ATOM   15184 O  O     . LEU A 1 3649 ? 206.297 199.843 254.429 1.00 25.46  ? 3649 LEU A O     1 
ATOM   15185 C  CB    . LEU A 1 3649 ? 205.756 201.191 251.545 1.00 16.11  ? 3649 LEU A CB    1 
ATOM   15186 C  CG    . LEU A 1 3649 ? 205.142 201.011 250.153 1.00 16.74  ? 3649 LEU A CG    1 
ATOM   15187 C  CD1   . LEU A 1 3649 ? 206.177 201.256 249.069 1.00 19.22  ? 3649 LEU A CD1   1 
ATOM   15188 C  CD2   . LEU A 1 3649 ? 204.530 199.629 250.009 1.00 18.05  ? 3649 LEU A CD2   1 
ATOM   15189 N  N     . ASN A 1 3650 ? 205.660 201.983 254.703 1.00 20.95  ? 3650 ASN A N     1 
ATOM   15190 C  CA    . ASN A 1 3650 ? 206.364 202.136 255.970 1.00 19.90  ? 3650 ASN A CA    1 
ATOM   15191 C  C     . ASN A 1 3650 ? 205.559 201.650 257.166 1.00 20.89  ? 3650 ASN A C     1 
ATOM   15192 O  O     . ASN A 1 3650 ? 206.079 201.683 258.288 1.00 22.70  ? 3650 ASN A O     1 
ATOM   15193 C  CB    . ASN A 1 3650 ? 206.747 203.600 256.192 1.00 22.30  ? 3650 ASN A CB    1 
ATOM   15194 C  CG    . ASN A 1 3650 ? 207.629 204.147 255.092 1.00 22.44  ? 3650 ASN A CG    1 
ATOM   15195 O  OD1   . ASN A 1 3650 ? 208.635 203.540 254.730 1.00 30.03  ? 3650 ASN A OD1   1 
ATOM   15196 N  ND2   . ASN A 1 3650 ? 207.262 205.306 254.561 1.00 19.37  ? 3650 ASN A ND2   1 
ATOM   15197 N  N     . ARG A 1 3651 ? 204.316 201.207 256.957 1.00 20.21  ? 3651 ARG A N     1 
ATOM   15198 C  CA    . ARG A 1 3651 ? 203.426 200.807 258.048 1.00 23.20  ? 3651 ARG A CA    1 
ATOM   15199 C  C     . ARG A 1 3651 ? 203.232 201.944 259.049 1.00 25.42  ? 3651 ARG A C     1 
ATOM   15200 O  O     . ARG A 1 3651 ? 203.174 201.724 260.261 1.00 28.59  ? 3651 ARG A O     1 
ATOM   15201 C  CB    . ARG A 1 3651 ? 203.932 199.545 258.756 1.00 30.59  ? 3651 ARG A CB    1 
ATOM   15202 C  CG    . ARG A 1 3651 ? 204.044 198.299 257.881 1.00 35.44  ? 3651 ARG A CG    1 
ATOM   15203 C  CD    . ARG A 1 3651 ? 202.672 197.789 257.460 1.00 47.23  ? 3651 ARG A CD    1 
ATOM   15204 N  NE    . ARG A 1 3651 ? 202.749 196.605 256.616 1.00 59.96  ? 3651 ARG A NE    1 
ATOM   15205 C  CZ    . ARG A 1 3651 ? 202.749 195.360 257.074 1.00 54.65  ? 3651 ARG A CZ    1 
ATOM   15206 N  NH1   . ARG A 1 3651 ? 202.708 195.100 258.369 1.00 45.53  ? 3651 ARG A NH1   1 
ATOM   15207 N  NH2   . ARG A 1 3651 ? 202.786 194.351 256.210 1.00 52.54  ? 3651 ARG A NH2   1 
ATOM   15208 N  N     . GLU A 1 3652 ? 203.127 203.173 258.541 1.00 25.59  ? 3652 GLU A N     1 
ATOM   15209 C  CA    . GLU A 1 3652 ? 202.900 204.345 259.386 1.00 24.53  ? 3652 GLU A CA    1 
ATOM   15210 C  C     . GLU A 1 3652 ? 201.440 204.353 259.830 1.00 27.63  ? 3652 GLU A C     1 
ATOM   15211 O  O     . GLU A 1 3652 ? 200.586 205.062 259.290 1.00 31.11  ? 3652 GLU A O     1 
ATOM   15212 C  CB    . GLU A 1 3652 ? 203.277 205.626 258.650 1.00 26.39  ? 3652 GLU A CB    1 
ATOM   15213 C  CG    . GLU A 1 3652 ? 204.768 205.815 258.452 1.00 24.28  ? 3652 GLU A CG    1 
ATOM   15214 C  CD    . GLU A 1 3652 ? 205.090 206.792 257.340 1.00 34.44  ? 3652 GLU A CD    1 
ATOM   15215 O  OE1   . GLU A 1 3652 ? 204.189 207.554 256.933 1.00 43.61  ? 3652 GLU A OE1   1 
ATOM   15216 O  OE2   . GLU A 1 3652 ? 206.253 206.812 256.886 1.00 40.97  ? 3652 GLU A OE2   1 
ATOM   15217 N  N     . VAL A 1 3653 ? 201.159 203.556 260.856 1.00 29.79  ? 3653 VAL A N     1 
ATOM   15218 C  CA    . VAL A 1 3653 ? 199.808 203.358 261.366 1.00 36.53  ? 3653 VAL A CA    1 
ATOM   15219 C  C     . VAL A 1 3653 ? 199.744 203.859 262.800 1.00 39.38  ? 3653 VAL A C     1 
ATOM   15220 O  O     . VAL A 1 3653 ? 200.683 203.666 263.582 1.00 38.11  ? 3653 VAL A O     1 
ATOM   15221 C  CB    . VAL A 1 3653 ? 199.383 201.879 261.278 1.00 34.19  ? 3653 VAL A CB    1 
ATOM   15222 C  CG1   . VAL A 1 3653 ? 199.114 201.498 259.835 1.00 30.50  ? 3653 VAL A CG1   1 
ATOM   15223 C  CG2   . VAL A 1 3653 ? 200.450 200.980 261.879 1.00 27.28  ? 3653 VAL A CG2   1 
ATOM   15224 N  N     . ARG A 1 3654 ? 198.641 204.519 263.139 1.00 45.92  ? 3654 ARG A N     1 
ATOM   15225 C  CA    . ARG A 1 3654 ? 198.402 205.033 264.479 1.00 48.84  ? 3654 ARG A CA    1 
ATOM   15226 C  C     . ARG A 1 3654 ? 197.235 204.276 265.100 1.00 45.23  ? 3654 ARG A C     1 
ATOM   15227 O  O     . ARG A 1 3654 ? 196.162 204.179 264.497 1.00 49.70  ? 3654 ARG A O     1 
ATOM   15228 C  CB    . ARG A 1 3654 ? 198.118 206.537 264.441 1.00 44.60  ? 3654 ARG A CB    1 
ATOM   15229 C  CG    . ARG A 1 3654 ? 197.953 207.186 265.804 1.00 44.94  ? 3654 ARG A CG    1 
ATOM   15230 C  CD    . ARG A 1 3654 ? 196.827 208.204 265.786 1.00 49.91  ? 3654 ARG A CD    1 
ATOM   15231 N  NE    . ARG A 1 3654 ? 197.071 209.258 264.809 1.00 60.75  ? 3654 ARG A NE    1 
ATOM   15232 C  CZ    . ARG A 1 3654 ? 196.189 209.659 263.904 1.00 61.82  ? 3654 ARG A CZ    1 
ATOM   15233 N  NH1   . ARG A 1 3654 ? 194.990 209.106 263.816 1.00 61.90  ? 3654 ARG A NH1   1 
ATOM   15234 N  NH2   . ARG A 1 3654 ? 196.520 210.634 263.063 1.00 53.58  ? 3654 ARG A NH2   1 
ATOM   15235 N  N     . ARG A 1 3655 ? 197.448 203.735 266.296 1.00 47.75  ? 3655 ARG A N     1 
ATOM   15236 C  CA    . ARG A 1 3655 ? 196.459 202.890 266.964 1.00 54.84  ? 3655 ARG A CA    1 
ATOM   15237 C  C     . ARG A 1 3655 ? 195.760 203.724 268.033 1.00 62.75  ? 3655 ARG A C     1 
ATOM   15238 O  O     . ARG A 1 3655 ? 196.255 203.878 269.150 1.00 56.32  ? 3655 ARG A O     1 
ATOM   15239 C  CB    . ARG A 1 3655 ? 197.120 201.652 267.557 1.00 46.62  ? 3655 ARG A CB    1 
ATOM   15240 C  CG    . ARG A 1 3655 ? 197.781 200.759 266.524 1.00 45.61  ? 3655 ARG A CG    1 
ATOM   15241 C  CD    . ARG A 1 3655 ? 198.459 199.564 267.168 1.00 47.87  ? 3655 ARG A CD    1 
ATOM   15242 N  NE    . ARG A 1 3655 ? 198.436 198.399 266.292 1.00 54.93  ? 3655 ARG A NE    1 
ATOM   15243 C  CZ    . ARG A 1 3655 ? 199.412 198.073 265.456 1.00 56.73  ? 3655 ARG A CZ    1 
ATOM   15244 N  NH1   . ARG A 1 3655 ? 200.513 198.800 265.361 1.00 55.93  ? 3655 ARG A NH1   1 
ATOM   15245 N  NH2   . ARG A 1 3655 ? 199.281 196.989 264.698 1.00 55.51  ? 3655 ARG A NH2   1 
ATOM   15246 N  N     . THR A 1 3656 ? 194.595 204.264 267.685 1.00 65.93  ? 3656 THR A N     1 
ATOM   15247 C  CA    . THR A 1 3656 ? 193.802 205.076 268.599 1.00 71.22  ? 3656 THR A CA    1 
ATOM   15248 C  C     . THR A 1 3656 ? 192.529 204.316 268.944 1.00 71.79  ? 3656 THR A C     1 
ATOM   15249 O  O     . THR A 1 3656 ? 191.732 203.999 268.054 1.00 70.43  ? 3656 THR A O     1 
ATOM   15250 C  CB    . THR A 1 3656 ? 193.469 206.435 267.984 1.00 65.87  ? 3656 THR A CB    1 
ATOM   15251 O  OG1   . THR A 1 3656 ? 194.655 207.236 267.928 1.00 56.87  ? 3656 THR A OG1   1 
ATOM   15252 C  CG2   . THR A 1 3656 ? 192.419 207.156 268.818 1.00 65.81  ? 3656 THR A CG2   1 
ATOM   15253 N  N     . GLY A 1 3657 ? 192.339 204.040 270.231 1.00 68.73  ? 3657 GLY A N     1 
ATOM   15254 C  CA    . GLY A 1 3657 ? 191.201 203.237 270.643 1.00 75.92  ? 3657 GLY A CA    1 
ATOM   15255 C  C     . GLY A 1 3657 ? 191.243 201.879 269.973 1.00 74.86  ? 3657 GLY A C     1 
ATOM   15256 O  O     . GLY A 1 3657 ? 192.264 201.182 269.991 1.00 72.75  ? 3657 GLY A O     1 
ATOM   15257 N  N     . GLY A 1 3658 ? 190.125 201.495 269.371 1.00 70.72  ? 3658 GLY A N     1 
ATOM   15258 C  CA    . GLY A 1 3658 ? 190.037 200.280 268.593 1.00 71.65  ? 3658 GLY A CA    1 
ATOM   15259 C  C     . GLY A 1 3658 ? 190.305 200.449 267.115 1.00 71.63  ? 3658 GLY A C     1 
ATOM   15260 O  O     . GLY A 1 3658 ? 190.086 199.508 266.347 1.00 63.38  ? 3658 GLY A O     1 
ATOM   15261 N  N     . ARG A 1 3659 ? 190.777 201.618 266.690 1.00 72.65  ? 3659 ARG A N     1 
ATOM   15262 C  CA    . ARG A 1 3659 ? 190.973 201.926 265.279 1.00 66.40  ? 3659 ARG A CA    1 
ATOM   15263 C  C     . ARG A 1 3659 ? 192.462 202.006 264.971 1.00 67.44  ? 3659 ARG A C     1 
ATOM   15264 O  O     . ARG A 1 3659 ? 193.189 202.796 265.587 1.00 70.27  ? 3659 ARG A O     1 
ATOM   15265 C  CB    . ARG A 1 3659 ? 190.284 203.238 264.905 1.00 65.53  ? 3659 ARG A CB    1 
ATOM   15266 C  CG    . ARG A 1 3659 ? 188.805 203.288 265.240 1.00 62.67  ? 3659 ARG A CG    1 
ATOM   15267 C  CD    . ARG A 1 3659 ? 188.278 204.713 265.171 1.00 58.82  ? 3659 ARG A CD    1 
ATOM   15268 N  NE    . ARG A 1 3659 ? 188.443 205.296 263.845 1.00 61.22  ? 3659 ARG A NE    1 
ATOM   15269 C  CZ    . ARG A 1 3659 ? 188.288 206.584 263.570 1.00 65.07  ? 3659 ARG A CZ    1 
ATOM   15270 N  NH1   . ARG A 1 3659 ? 187.966 207.458 264.510 1.00 70.93  ? 3659 ARG A NH1   1 
ATOM   15271 N  NH2   . ARG A 1 3659 ? 188.458 207.006 262.321 1.00 62.53  ? 3659 ARG A NH2   1 
ATOM   15272 N  N     . VAL A 1 3660 ? 192.907 201.200 264.012 1.00 58.71  ? 3660 VAL A N     1 
ATOM   15273 C  CA    . VAL A 1 3660 ? 194.254 201.287 263.461 1.00 49.90  ? 3660 VAL A CA    1 
ATOM   15274 C  C     . VAL A 1 3660 ? 194.127 202.105 262.182 1.00 48.70  ? 3660 VAL A C     1 
ATOM   15275 O  O     . VAL A 1 3660 ? 193.625 201.619 261.165 1.00 50.49  ? 3660 VAL A O     1 
ATOM   15276 C  CB    . VAL A 1 3660 ? 194.853 199.902 263.202 1.00 47.48  ? 3660 VAL A CB    1 
ATOM   15277 C  CG1   . VAL A 1 3660 ? 196.084 200.008 262.310 1.00 49.40  ? 3660 VAL A CG1   1 
ATOM   15278 C  CG2   . VAL A 1 3660 ? 195.189 199.212 264.514 1.00 46.40  ? 3660 VAL A CG2   1 
ATOM   15279 N  N     . LEU A 1 3661 ? 194.566 203.359 262.228 1.00 51.59  ? 3661 LEU A N     1 
ATOM   15280 C  CA    . LEU A 1 3661 ? 194.355 204.298 261.137 1.00 49.56  ? 3661 LEU A CA    1 
ATOM   15281 C  C     . LEU A 1 3661 ? 195.646 204.544 260.372 1.00 46.61  ? 3661 LEU A C     1 
ATOM   15282 O  O     . LEU A 1 3661 ? 196.735 204.569 260.953 1.00 51.30  ? 3661 LEU A O     1 
ATOM   15283 C  CB    . LEU A 1 3661 ? 193.803 205.623 261.663 1.00 54.74  ? 3661 LEU A CB    1 
ATOM   15284 C  CG    . LEU A 1 3661 ? 192.588 205.521 262.585 1.00 56.16  ? 3661 LEU A CG    1 
ATOM   15285 C  CD1   . LEU A 1 3661 ? 192.494 206.743 263.483 1.00 57.10  ? 3661 LEU A CD1   1 
ATOM   15286 C  CD2   . LEU A 1 3661 ? 191.321 205.354 261.765 1.00 55.37  ? 3661 LEU A CD2   1 
ATOM   15287 N  N     . ILE A 1 3662 ? 195.512 204.727 259.063 1.00 45.81  ? 3662 ILE A N     1 
ATOM   15288 C  CA    . ILE A 1 3662 ? 196.615 205.087 258.184 1.00 42.85  ? 3662 ILE A CA    1 
ATOM   15289 C  C     . ILE A 1 3662 ? 196.182 206.292 257.360 1.00 51.01  ? 3662 ILE A C     1 
ATOM   15290 O  O     . ILE A 1 3662 ? 195.019 206.390 256.950 1.00 59.62  ? 3662 ILE A O     1 
ATOM   15291 C  CB    . ILE A 1 3662 ? 197.037 203.904 257.284 1.00 39.75  ? 3662 ILE A CB    1 
ATOM   15292 C  CG1   . ILE A 1 3662 ? 198.306 204.243 256.501 1.00 41.88  ? 3662 ILE A CG1   1 
ATOM   15293 C  CG2   . ILE A 1 3662 ? 195.906 203.488 256.351 1.00 45.25  ? 3662 ILE A CG2   1 
ATOM   15294 C  CD1   . ILE A 1 3662 ? 199.191 203.049 256.255 1.00 31.72  ? 3662 ILE A CD1   1 
ATOM   15295 N  N     . THR A 1 3663 ? 197.103 207.226 257.142 1.00 50.31  ? 3663 THR A N     1 
ATOM   15296 C  CA    . THR A 1 3663 ? 196.785 208.504 256.514 1.00 54.86  ? 3663 THR A CA    1 
ATOM   15297 C  C     . THR A 1 3663 ? 197.205 208.473 255.049 1.00 53.89  ? 3663 THR A C     1 
ATOM   15298 O  O     . THR A 1 3663 ? 198.401 208.455 254.739 1.00 63.52  ? 3663 THR A O     1 
ATOM   15299 C  CB    . THR A 1 3663 ? 197.470 209.652 257.252 1.00 64.41  ? 3663 THR A CB    1 
ATOM   15300 O  OG1   . THR A 1 3663 ? 196.957 209.737 258.588 1.00 64.99  ? 3663 THR A OG1   1 
ATOM   15301 C  CG2   . THR A 1 3663 ? 197.214 210.970 256.537 1.00 67.19  ? 3663 THR A CG2   1 
ATOM   15302 N  N     . LEU A 1 3664 ? 196.222 208.473 254.149 1.00 59.35  ? 3664 LEU A N     1 
ATOM   15303 C  CA    . LEU A 1 3664 ? 196.461 208.611 252.716 1.00 62.25  ? 3664 LEU A CA    1 
ATOM   15304 C  C     . LEU A 1 3664 ? 196.056 210.022 252.310 1.00 66.27  ? 3664 LEU A C     1 
ATOM   15305 O  O     . LEU A 1 3664 ? 194.879 210.385 252.400 1.00 74.24  ? 3664 LEU A O     1 
ATOM   15306 C  CB    . LEU A 1 3664 ? 195.677 207.577 251.913 1.00 56.74  ? 3664 LEU A CB    1 
ATOM   15307 C  CG    . LEU A 1 3664 ? 196.094 206.114 252.008 1.00 53.43  ? 3664 LEU A CG    1 
ATOM   15308 C  CD1   . LEU A 1 3664 ? 195.253 205.288 251.056 1.00 43.91  ? 3664 LEU A CD1   1 
ATOM   15309 C  CD2   . LEU A 1 3664 ? 197.566 205.959 251.702 1.00 57.26  ? 3664 LEU A CD2   1 
ATOM   15310 N  N     . GLY A 1 3665 ? 197.026 210.808 251.850 1.00 64.39  ? 3665 GLY A N     1 
ATOM   15311 C  CA    . GLY A 1 3665 ? 196.758 212.187 251.503 1.00 68.94  ? 3665 GLY A CA    1 
ATOM   15312 C  C     . GLY A 1 3665 ? 196.218 212.970 252.682 1.00 78.60  ? 3665 GLY A C     1 
ATOM   15313 O  O     . GLY A 1 3665 ? 196.948 213.266 253.631 1.00 78.02  ? 3665 GLY A O     1 
ATOM   15314 N  N     . ASP A 1 3666 ? 194.927 213.303 252.631 1.00 78.24  ? 3666 ASP A N     1 
ATOM   15315 C  CA    . ASP A 1 3666 ? 194.258 214.016 253.711 1.00 84.75  ? 3666 ASP A CA    1 
ATOM   15316 C  C     . ASP A 1 3666 ? 193.114 213.207 254.311 1.00 82.29  ? 3666 ASP A C     1 
ATOM   15317 O  O     . ASP A 1 3666 ? 192.172 213.786 254.863 1.00 85.48  ? 3666 ASP A O     1 
ATOM   15318 C  CB    . ASP A 1 3666 ? 193.749 215.372 253.217 1.00 86.48  ? 3666 ASP A CB    1 
ATOM   15319 C  CG    . ASP A 1 3666 ? 192.792 215.244 252.046 1.00 86.53  ? 3666 ASP A CG    1 
ATOM   15320 O  OD1   . ASP A 1 3666 ? 192.744 214.159 251.430 1.00 81.35  ? 3666 ASP A OD1   1 
ATOM   15321 O  OD2   . ASP A 1 3666 ? 192.088 216.229 251.743 1.00 86.20  ? 3666 ASP A OD2   1 
ATOM   15322 N  N     . GLN A 1 3667 ? 193.170 211.880 254.214 1.00 76.52  ? 3667 GLN A N     1 
ATOM   15323 C  CA    . GLN A 1 3667 ? 192.094 211.017 254.686 1.00 73.37  ? 3667 GLN A CA    1 
ATOM   15324 C  C     . GLN A 1 3667 ? 192.659 209.926 255.583 1.00 68.76  ? 3667 GLN A C     1 
ATOM   15325 O  O     . GLN A 1 3667 ? 193.680 209.312 255.258 1.00 70.72  ? 3667 GLN A O     1 
ATOM   15326 C  CB    . GLN A 1 3667 ? 191.336 210.393 253.510 1.00 73.12  ? 3667 GLN A CB    1 
ATOM   15327 C  CG    . GLN A 1 3667 ? 189.927 209.938 253.850 1.00 75.84  ? 3667 GLN A CG    1 
ATOM   15328 C  CD    . GLN A 1 3667 ? 189.324 209.063 252.772 1.00 74.65  ? 3667 GLN A CD    1 
ATOM   15329 O  OE1   . GLN A 1 3667 ? 188.666 208.064 253.062 1.00 72.57  ? 3667 GLN A OE1   1 
ATOM   15330 N  NE2   . GLN A 1 3667 ? 189.543 209.436 251.516 1.00 68.70  ? 3667 GLN A NE2   1 
ATOM   15331 N  N     . ASP A 1 3668 ? 191.984 209.677 256.703 1.00 70.67  ? 3668 ASP A N     1 
ATOM   15332 C  CA    . ASP A 1 3668 ? 192.356 208.596 257.607 1.00 67.17  ? 3668 ASP A CA    1 
ATOM   15333 C  C     . ASP A 1 3668 ? 191.492 207.374 257.321 1.00 66.40  ? 3668 ASP A C     1 
ATOM   15334 O  O     . ASP A 1 3668 ? 190.263 207.474 257.268 1.00 67.41  ? 3668 ASP A O     1 
ATOM   15335 C  CB    . ASP A 1 3668 ? 192.200 209.030 259.065 1.00 66.10  ? 3668 ASP A CB    1 
ATOM   15336 C  CG    . ASP A 1 3668 ? 193.216 210.076 259.472 1.00 70.54  ? 3668 ASP A CG    1 
ATOM   15337 O  OD1   . ASP A 1 3668 ? 194.326 210.081 258.901 1.00 74.21  ? 3668 ASP A OD1   1 
ATOM   15338 O  OD2   . ASP A 1 3668 ? 192.904 210.895 260.361 1.00 73.32  ? 3668 ASP A OD2   1 
ATOM   15339 N  N     . ILE A 1 3669 ? 192.139 206.226 257.141 1.00 57.23  ? 3669 ILE A N     1 
ATOM   15340 C  CA    . ILE A 1 3669 ? 191.480 204.987 256.750 1.00 53.29  ? 3669 ILE A CA    1 
ATOM   15341 C  C     . ILE A 1 3669 ? 191.786 203.927 257.797 1.00 50.99  ? 3669 ILE A C     1 
ATOM   15342 O  O     . ILE A 1 3669 ? 192.948 203.740 258.174 1.00 51.17  ? 3669 ILE A O     1 
ATOM   15343 C  CB    . ILE A 1 3669 ? 191.935 204.524 255.355 1.00 50.24  ? 3669 ILE A CB    1 
ATOM   15344 C  CG1   . ILE A 1 3669 ? 191.536 205.550 254.296 1.00 55.80  ? 3669 ILE A CG1   1 
ATOM   15345 C  CG2   . ILE A 1 3669 ? 191.372 203.154 255.033 1.00 49.95  ? 3669 ILE A CG2   1 
ATOM   15346 C  CD1   . ILE A 1 3669 ? 192.163 205.302 252.949 1.00 53.47  ? 3669 ILE A CD1   1 
ATOM   15347 N  N     . ASP A 1 3670 ? 190.747 203.239 258.264 1.00 50.45  ? 3670 ASP A N     1 
ATOM   15348 C  CA    . ASP A 1 3670 ? 190.918 202.165 259.237 1.00 52.72  ? 3670 ASP A CA    1 
ATOM   15349 C  C     . ASP A 1 3670 ? 191.566 200.966 258.555 1.00 60.05  ? 3670 ASP A C     1 
ATOM   15350 O  O     . ASP A 1 3670 ? 190.928 200.275 257.755 1.00 58.13  ? 3670 ASP A O     1 
ATOM   15351 C  CB    . ASP A 1 3670 ? 189.572 201.787 259.847 1.00 54.78  ? 3670 ASP A CB    1 
ATOM   15352 C  CG    . ASP A 1 3670 ? 189.710 201.151 261.216 1.00 62.44  ? 3670 ASP A CG    1 
ATOM   15353 O  OD1   . ASP A 1 3670 ? 190.474 200.172 261.349 1.00 55.77  ? 3670 ASP A OD1   1 
ATOM   15354 O  OD2   . ASP A 1 3670 ? 189.054 201.632 262.164 1.00 70.84  ? 3670 ASP A OD2   1 
ATOM   15355 N  N     . LEU A 1 3671 ? 192.836 200.721 258.869 1.00 56.86  ? 3671 LEU A N     1 
ATOM   15356 C  CA    . LEU A 1 3671 ? 193.554 199.603 258.275 1.00 45.90  ? 3671 LEU A CA    1 
ATOM   15357 C  C     . LEU A 1 3671 ? 193.012 198.275 258.786 1.00 48.66  ? 3671 LEU A C     1 
ATOM   15358 O  O     . LEU A 1 3671 ? 192.608 198.152 259.946 1.00 47.27  ? 3671 LEU A O     1 
ATOM   15359 C  CB    . LEU A 1 3671 ? 195.047 199.711 258.585 1.00 45.12  ? 3671 LEU A CB    1 
ATOM   15360 C  CG    . LEU A 1 3671 ? 195.962 198.662 257.952 1.00 42.57  ? 3671 LEU A CG    1 
ATOM   15361 C  CD1   . LEU A 1 3671 ? 196.191 198.962 256.484 1.00 40.37  ? 3671 LEU A CD1   1 
ATOM   15362 C  CD2   . LEU A 1 3671 ? 197.281 198.576 258.699 1.00 37.04  ? 3671 LEU A CD2   1 
ATOM   15363 N  N     . SER A 1 3672 ? 193.005 197.272 257.905 1.00 47.90  ? 3672 SER A N     1 
ATOM   15364 C  CA    . SER A 1 3672 ? 192.640 195.913 258.261 1.00 43.29  ? 3672 SER A CA    1 
ATOM   15365 C  C     . SER A 1 3672 ? 193.864 195.008 258.207 1.00 41.40  ? 3672 SER A C     1 
ATOM   15366 O  O     . SER A 1 3672 ? 194.672 195.117 257.279 1.00 47.04  ? 3672 SER A O     1 
ATOM   15367 C  CB    . SER A 1 3672 ? 191.560 195.366 257.322 1.00 42.87  ? 3672 SER A CB    1 
ATOM   15368 O  OG    . SER A 1 3672 ? 191.187 194.049 257.685 1.00 47.12  ? 3672 SER A OG    1 
ATOM   15369 N  N     . PRO A 1 3673 ? 194.033 194.112 259.183 1.00 38.58  ? 3673 PRO A N     1 
ATOM   15370 C  CA    . PRO A 1 3673 ? 195.238 193.266 259.202 1.00 43.20  ? 3673 PRO A CA    1 
ATOM   15371 C  C     . PRO A 1 3673 ? 195.347 192.324 258.016 1.00 41.54  ? 3673 PRO A C     1 
ATOM   15372 O  O     . PRO A 1 3673 ? 196.446 191.830 257.737 1.00 37.04  ? 3673 PRO A O     1 
ATOM   15373 C  CB    . PRO A 1 3673 ? 195.104 192.493 260.521 1.00 35.35  ? 3673 PRO A CB    1 
ATOM   15374 C  CG    . PRO A 1 3673 ? 193.646 192.516 260.828 1.00 38.97  ? 3673 PRO A CG    1 
ATOM   15375 C  CD    . PRO A 1 3673 ? 193.135 193.827 260.314 1.00 38.24  ? 3673 PRO A CD    1 
ATOM   15376 N  N     . SER A 1 3674 ? 194.252 192.058 257.311 1.00 42.49  ? 3674 SER A N     1 
ATOM   15377 C  CA    . SER A 1 3674 ? 194.272 191.138 256.180 1.00 39.38  ? 3674 SER A CA    1 
ATOM   15378 C  C     . SER A 1 3674 ? 194.754 191.791 254.893 1.00 38.58  ? 3674 SER A C     1 
ATOM   15379 O  O     . SER A 1 3674 ? 194.859 191.103 253.873 1.00 37.56  ? 3674 SER A O     1 
ATOM   15380 C  CB    . SER A 1 3674 ? 192.877 190.544 255.969 1.00 44.42  ? 3674 SER A CB    1 
ATOM   15381 O  OG    . SER A 1 3674 ? 192.484 189.762 257.082 1.00 49.76  ? 3674 SER A OG    1 
ATOM   15382 N  N     . PHE A 1 3675 ? 195.042 193.089 254.912 1.00 39.54  ? 3675 PHE A N     1 
ATOM   15383 C  CA    . PHE A 1 3675 ? 195.523 193.768 253.718 1.00 31.18  ? 3675 PHE A CA    1 
ATOM   15384 C  C     . PHE A 1 3675 ? 196.956 193.360 253.402 1.00 27.93  ? 3675 PHE A C     1 
ATOM   15385 O  O     . PHE A 1 3675 ? 197.792 193.208 254.297 1.00 29.72  ? 3675 PHE A O     1 
ATOM   15386 C  CB    . PHE A 1 3675 ? 195.441 195.284 253.900 1.00 25.92  ? 3675 PHE A CB    1 
ATOM   15387 C  CG    . PHE A 1 3675 ? 196.265 196.060 252.911 1.00 25.76  ? 3675 PHE A CG    1 
ATOM   15388 C  CD1   . PHE A 1 3675 ? 195.812 196.262 251.621 1.00 26.36  ? 3675 PHE A CD1   1 
ATOM   15389 C  CD2   . PHE A 1 3675 ? 197.494 196.587 253.273 1.00 24.31  ? 3675 PHE A CD2   1 
ATOM   15390 C  CE1   . PHE A 1 3675 ? 196.566 196.973 250.710 1.00 24.99  ? 3675 PHE A CE1   1 
ATOM   15391 C  CE2   . PHE A 1 3675 ? 198.254 197.296 252.366 1.00 23.44  ? 3675 PHE A CE2   1 
ATOM   15392 C  CZ    . PHE A 1 3675 ? 197.788 197.491 251.083 1.00 24.75  ? 3675 PHE A CZ    1 
ATOM   15393 N  N     . VAL A 1 3676 ? 197.235 193.183 252.114 1.00 27.19  ? 3676 VAL A N     1 
ATOM   15394 C  CA    . VAL A 1 3676 ? 198.588 192.941 251.625 1.00 24.68  ? 3676 VAL A CA    1 
ATOM   15395 C  C     . VAL A 1 3676 ? 198.667 193.478 250.203 1.00 25.48  ? 3676 VAL A C     1 
ATOM   15396 O  O     . VAL A 1 3676 ? 197.696 193.402 249.445 1.00 29.79  ? 3676 VAL A O     1 
ATOM   15397 C  CB    . VAL A 1 3676 ? 198.963 191.443 251.706 1.00 20.98  ? 3676 VAL A CB    1 
ATOM   15398 C  CG1   . VAL A 1 3676 ? 198.094 190.613 250.775 1.00 27.61  ? 3676 VAL A CG1   1 
ATOM   15399 C  CG2   . VAL A 1 3676 ? 200.438 191.241 251.398 1.00 21.47  ? 3676 VAL A CG2   1 
ATOM   15400 N  N     . ILE A 1 3677 ? 199.816 194.045 249.848 1.00 20.85  ? 3677 ILE A N     1 
ATOM   15401 C  CA    . ILE A 1 3677 ? 200.005 194.671 248.546 1.00 19.80  ? 3677 ILE A CA    1 
ATOM   15402 C  C     . ILE A 1 3677 ? 201.275 194.128 247.907 1.00 20.82  ? 3677 ILE A C     1 
ATOM   15403 O  O     . ILE A 1 3677 ? 202.299 193.954 248.578 1.00 21.94  ? 3677 ILE A O     1 
ATOM   15404 C  CB    . ILE A 1 3677 ? 200.053 196.212 248.655 1.00 21.28  ? 3677 ILE A CB    1 
ATOM   15405 C  CG1   . ILE A 1 3677 ? 200.274 196.849 247.283 1.00 23.52  ? 3677 ILE A CG1   1 
ATOM   15406 C  CG2   . ILE A 1 3677 ? 201.117 196.658 249.639 1.00 21.67  ? 3677 ILE A CG2   1 
ATOM   15407 C  CD1   . ILE A 1 3677 ? 199.976 198.323 247.249 1.00 26.61  ? 3677 ILE A CD1   1 
ATOM   15408 N  N     . PHE A 1 3678 ? 201.197 193.837 246.611 1.00 20.76  ? 3678 PHE A N     1 
ATOM   15409 C  CA    . PHE A 1 3678 ? 202.332 193.376 245.825 1.00 12.75  ? 3678 PHE A CA    1 
ATOM   15410 C  C     . PHE A 1 3678 ? 202.592 194.362 244.696 1.00 13.79  ? 3678 PHE A C     1 
ATOM   15411 O  O     . PHE A 1 3678 ? 201.661 194.761 243.990 1.00 16.15  ? 3678 PHE A O     1 
ATOM   15412 C  CB    . PHE A 1 3678 ? 202.083 191.978 245.253 1.00 12.48  ? 3678 PHE A CB    1 
ATOM   15413 C  CG    . PHE A 1 3678 ? 201.894 190.918 246.297 1.00 16.27  ? 3678 PHE A CG    1 
ATOM   15414 C  CD1   . PHE A 1 3678 ? 200.642 190.665 246.831 1.00 17.95  ? 3678 PHE A CD1   1 
ATOM   15415 C  CD2   . PHE A 1 3678 ? 202.970 190.168 246.740 1.00 14.63  ? 3678 PHE A CD2   1 
ATOM   15416 C  CE1   . PHE A 1 3678 ? 200.470 189.690 247.790 1.00 19.23  ? 3678 PHE A CE1   1 
ATOM   15417 C  CE2   . PHE A 1 3678 ? 202.802 189.192 247.699 1.00 13.52  ? 3678 PHE A CE2   1 
ATOM   15418 C  CZ    . PHE A 1 3678 ? 201.551 188.953 248.225 1.00 16.72  ? 3678 PHE A CZ    1 
ATOM   15419 N  N     . LEU A 1 3679 ? 203.850 194.752 244.533 1.00 15.51  ? 3679 LEU A N     1 
ATOM   15420 C  CA    . LEU A 1 3679 ? 204.271 195.609 243.434 1.00 12.19  ? 3679 LEU A CA    1 
ATOM   15421 C  C     . LEU A 1 3679 ? 205.020 194.768 242.410 1.00 12.81  ? 3679 LEU A C     1 
ATOM   15422 O  O     . LEU A 1 3679 ? 205.911 193.993 242.771 1.00 17.24  ? 3679 LEU A O     1 
ATOM   15423 C  CB    . LEU A 1 3679 ? 205.156 196.752 243.933 1.00 13.37  ? 3679 LEU A CB    1 
ATOM   15424 C  CG    . LEU A 1 3679 ? 204.646 197.525 245.152 1.00 15.85  ? 3679 LEU A CG    1 
ATOM   15425 C  CD1   . LEU A 1 3679 ? 205.618 198.628 245.527 1.00 17.82  ? 3679 LEU A CD1   1 
ATOM   15426 C  CD2   . LEU A 1 3679 ? 203.261 198.094 244.891 1.00 16.19  ? 3679 LEU A CD2   1 
ATOM   15427 N  N     . SER A 1 3680 ? 204.652 194.912 241.141 1.00 16.43  ? 3680 SER A N     1 
ATOM   15428 C  CA    . SER A 1 3680 ? 205.247 194.122 240.076 1.00 17.91  ? 3680 SER A CA    1 
ATOM   15429 C  C     . SER A 1 3680 ? 205.642 195.024 238.916 1.00 18.81  ? 3680 SER A C     1 
ATOM   15430 O  O     . SER A 1 3680 ? 205.088 196.110 238.731 1.00 18.18  ? 3680 SER A O     1 
ATOM   15431 C  CB    . SER A 1 3680 ? 204.295 193.022 239.588 1.00 20.32  ? 3680 SER A CB    1 
ATOM   15432 O  OG    . SER A 1 3680 ? 203.071 193.564 239.131 1.00 18.55  ? 3680 SER A OG    1 
ATOM   15433 N  N     . THR A 1 3681 ? 206.622 194.561 238.143 1.00 21.98  ? 3681 THR A N     1 
ATOM   15434 C  CA    . THR A 1 3681 ? 207.085 195.273 236.964 1.00 19.00  ? 3681 THR A CA    1 
ATOM   15435 C  C     . THR A 1 3681 ? 207.529 194.261 235.922 1.00 21.29  ? 3681 THR A C     1 
ATOM   15436 O  O     . THR A 1 3681 ? 207.799 193.098 236.231 1.00 27.13  ? 3681 THR A O     1 
ATOM   15437 C  CB    . THR A 1 3681 ? 208.233 196.238 237.289 1.00 21.22  ? 3681 THR A CB    1 
ATOM   15438 O  OG1   . THR A 1 3681 ? 208.394 197.172 236.215 1.00 22.76  ? 3681 THR A OG1   1 
ATOM   15439 C  CG2   . THR A 1 3681 ? 209.534 195.481 237.492 1.00 21.52  ? 3681 THR A CG2   1 
ATOM   15440 N  N     . ARG A 1 3682 ? 207.591 194.717 234.674 1.00 20.64  ? 3682 ARG A N     1 
ATOM   15441 C  CA    . ARG A 1 3682 ? 208.035 193.888 233.564 1.00 16.88  ? 3682 ARG A CA    1 
ATOM   15442 C  C     . ARG A 1 3682 ? 209.360 194.352 232.978 1.00 22.77  ? 3682 ARG A C     1 
ATOM   15443 O  O     . ARG A 1 3682 ? 209.918 193.661 232.120 1.00 28.80  ? 3682 ARG A O     1 
ATOM   15444 C  CB    . ARG A 1 3682 ? 206.965 193.855 232.469 1.00 18.64  ? 3682 ARG A CB    1 
ATOM   15445 C  CG    . ARG A 1 3682 ? 205.720 193.072 232.847 1.00 18.77  ? 3682 ARG A CG    1 
ATOM   15446 C  CD    . ARG A 1 3682 ? 204.673 193.137 231.749 1.00 20.56  ? 3682 ARG A CD    1 
ATOM   15447 N  NE    . ARG A 1 3682 ? 204.225 194.500 231.495 1.00 21.36  ? 3682 ARG A NE    1 
ATOM   15448 C  CZ    . ARG A 1 3682 ? 204.571 195.216 230.434 1.00 26.64  ? 3682 ARG A CZ    1 
ATOM   15449 N  NH1   . ARG A 1 3682 ? 205.379 194.730 229.507 1.00 23.41  ? 3682 ARG A NH1   1 
ATOM   15450 N  NH2   . ARG A 1 3682 ? 204.096 196.450 230.301 1.00 28.62  ? 3682 ARG A NH2   1 
ATOM   15451 N  N     . ASP A 1 3683 ? 209.880 195.497 233.420 1.00 24.95  ? 3683 ASP A N     1 
ATOM   15452 C  CA    . ASP A 1 3683 ? 211.147 196.010 232.929 1.00 22.18  ? 3683 ASP A CA    1 
ATOM   15453 C  C     . ASP A 1 3683 ? 212.263 195.541 233.848 1.00 27.57  ? 3683 ASP A C     1 
ATOM   15454 O  O     . ASP A 1 3683 ? 212.311 195.967 235.010 1.00 27.55  ? 3683 ASP A O     1 
ATOM   15455 C  CB    . ASP A 1 3683 ? 211.116 197.535 232.863 1.00 22.50  ? 3683 ASP A CB    1 
ATOM   15456 C  CG    . ASP A 1 3683 ? 212.305 198.113 232.123 1.00 30.33  ? 3683 ASP A CG    1 
ATOM   15457 O  OD1   . ASP A 1 3683 ? 212.589 199.315 232.303 1.00 25.30  ? 3683 ASP A OD1   1 
ATOM   15458 O  OD2   . ASP A 1 3683 ? 212.955 197.369 231.360 1.00 36.43  ? 3683 ASP A OD2   1 
ATOM   15459 N  N     . PRO A 1 3684 ? 213.172 194.675 233.389 1.00 27.61  ? 3684 PRO A N     1 
ATOM   15460 C  CA    . PRO A 1 3684 ? 214.264 194.221 234.259 1.00 26.82  ? 3684 PRO A CA    1 
ATOM   15461 C  C     . PRO A 1 3684 ? 215.394 195.224 234.411 1.00 28.09  ? 3684 PRO A C     1 
ATOM   15462 O  O     . PRO A 1 3684 ? 216.258 195.027 235.275 1.00 35.59  ? 3684 PRO A O     1 
ATOM   15463 C  CB    . PRO A 1 3684 ? 214.756 192.951 233.556 1.00 27.57  ? 3684 PRO A CB    1 
ATOM   15464 C  CG    . PRO A 1 3684 ? 214.466 193.199 232.117 1.00 21.92  ? 3684 PRO A CG    1 
ATOM   15465 C  CD    . PRO A 1 3684 ? 213.201 194.017 232.072 1.00 21.90  ? 3684 PRO A CD    1 
ATOM   15466 N  N     . THR A 1 3685 ? 215.421 196.285 233.606 1.00 28.17  ? 3685 THR A N     1 
ATOM   15467 C  CA    . THR A 1 3685 ? 216.499 197.264 233.630 1.00 33.39  ? 3685 THR A CA    1 
ATOM   15468 C  C     . THR A 1 3685 ? 216.080 198.587 234.256 1.00 36.20  ? 3685 THR A C     1 
ATOM   15469 O  O     . THR A 1 3685 ? 216.822 199.570 234.155 1.00 40.49  ? 3685 THR A O     1 
ATOM   15470 C  CB    . THR A 1 3685 ? 217.027 197.503 232.215 1.00 36.10  ? 3685 THR A CB    1 
ATOM   15471 O  OG1   . THR A 1 3685 ? 215.970 197.999 231.385 1.00 32.86  ? 3685 THR A OG1   1 
ATOM   15472 C  CG2   . THR A 1 3685 ? 217.562 196.209 231.622 1.00 32.25  ? 3685 THR A CG2   1 
ATOM   15473 N  N     . VAL A 1 3686 ? 214.919 198.640 234.896 1.00 32.78  ? 3686 VAL A N     1 
ATOM   15474 C  CA    . VAL A 1 3686 ? 214.438 199.877 235.498 1.00 30.37  ? 3686 VAL A CA    1 
ATOM   15475 C  C     . VAL A 1 3686 ? 215.231 200.166 236.765 1.00 32.41  ? 3686 VAL A C     1 
ATOM   15476 O  O     . VAL A 1 3686 ? 215.515 199.265 237.564 1.00 34.59  ? 3686 VAL A O     1 
ATOM   15477 C  CB    . VAL A 1 3686 ? 212.925 199.791 235.776 1.00 24.53  ? 3686 VAL A CB    1 
ATOM   15478 C  CG1   . VAL A 1 3686 ? 212.612 198.640 236.714 1.00 27.59  ? 3686 VAL A CG1   1 
ATOM   15479 C  CG2   . VAL A 1 3686 ? 212.410 201.103 236.348 1.00 24.44  ? 3686 VAL A CG2   1 
ATOM   15480 N  N     . GLU A 1 3687 ? 215.615 201.427 236.938 1.00 38.83  ? 3687 GLU A N     1 
ATOM   15481 C  CA    . GLU A 1 3687 ? 216.315 201.880 238.130 1.00 28.92  ? 3687 GLU A CA    1 
ATOM   15482 C  C     . GLU A 1 3687 ? 215.316 202.519 239.084 1.00 29.92  ? 3687 GLU A C     1 
ATOM   15483 O  O     . GLU A 1 3687 ? 214.508 203.359 238.674 1.00 32.55  ? 3687 GLU A O     1 
ATOM   15484 C  CB    . GLU A 1 3687 ? 217.423 202.874 237.777 1.00 28.77  ? 3687 GLU A CB    1 
ATOM   15485 C  CG    . GLU A 1 3687 ? 218.581 202.272 236.993 1.00 44.18  ? 3687 GLU A CG    1 
ATOM   15486 C  CD    . GLU A 1 3687 ? 218.303 202.179 235.508 1.00 54.44  ? 3687 GLU A CD    1 
ATOM   15487 O  OE1   . GLU A 1 3687 ? 217.230 202.643 235.070 1.00 59.77  ? 3687 GLU A OE1   1 
ATOM   15488 O  OE2   . GLU A 1 3687 ? 219.157 201.634 234.778 1.00 48.57  ? 3687 GLU A OE2   1 
ATOM   15489 N  N     . PHE A 1 3688 ? 215.371 202.118 240.345 1.00 29.00  ? 3688 PHE A N     1 
ATOM   15490 C  CA    . PHE A 1 3688 ? 214.463 202.638 241.347 1.00 23.42  ? 3688 PHE A CA    1 
ATOM   15491 C  C     . PHE A 1 3688 ? 215.176 203.638 242.250 1.00 26.94  ? 3688 PHE A C     1 
ATOM   15492 O  O     . PHE A 1 3688 ? 216.369 203.488 242.535 1.00 35.08  ? 3688 PHE A O     1 
ATOM   15493 C  CB    . PHE A 1 3688 ? 213.883 201.508 242.204 1.00 25.57  ? 3688 PHE A CB    1 
ATOM   15494 C  CG    . PHE A 1 3688 ? 212.996 200.568 241.444 1.00 22.41  ? 3688 PHE A CG    1 
ATOM   15495 C  CD1   . PHE A 1 3688 ? 211.688 200.913 241.155 1.00 18.91  ? 3688 PHE A CD1   1 
ATOM   15496 C  CD2   . PHE A 1 3688 ? 213.473 199.345 241.012 1.00 18.25  ? 3688 PHE A CD2   1 
ATOM   15497 C  CE1   . PHE A 1 3688 ? 210.871 200.053 240.456 1.00 17.27  ? 3688 PHE A CE1   1 
ATOM   15498 C  CE2   . PHE A 1 3688 ? 212.660 198.480 240.312 1.00 17.99  ? 3688 PHE A CE2   1 
ATOM   15499 C  CZ    . PHE A 1 3688 ? 211.357 198.834 240.033 1.00 17.60  ? 3688 PHE A CZ    1 
ATOM   15500 N  N     . PRO A 1 3689 ? 214.475 204.675 242.711 1.00 27.97  ? 3689 PRO A N     1 
ATOM   15501 C  CA    . PRO A 1 3689 ? 215.093 205.612 243.643 1.00 24.03  ? 3689 PRO A CA    1 
ATOM   15502 C  C     . PRO A 1 3689 ? 215.351 204.944 244.981 1.00 25.36  ? 3689 PRO A C     1 
ATOM   15503 O  O     . PRO A 1 3689 ? 214.660 203.981 245.355 1.00 23.82  ? 3689 PRO A O     1 
ATOM   15504 C  CB    . PRO A 1 3689 ? 214.046 206.733 243.764 1.00 29.89  ? 3689 PRO A CB    1 
ATOM   15505 C  CG    . PRO A 1 3689 ? 212.756 206.068 243.438 1.00 28.13  ? 3689 PRO A CG    1 
ATOM   15506 C  CD    . PRO A 1 3689 ? 213.078 205.031 242.404 1.00 30.65  ? 3689 PRO A CD    1 
ATOM   15507 N  N     . PRO A 1 3690 ? 216.350 205.412 245.735 1.00 23.43  ? 3690 PRO A N     1 
ATOM   15508 C  CA    . PRO A 1 3690 ? 216.656 204.770 247.024 1.00 21.73  ? 3690 PRO A CA    1 
ATOM   15509 C  C     . PRO A 1 3690 ? 215.498 204.786 248.006 1.00 19.79  ? 3690 PRO A C     1 
ATOM   15510 O  O     . PRO A 1 3690 ? 215.369 203.851 248.807 1.00 21.33  ? 3690 PRO A O     1 
ATOM   15511 C  CB    . PRO A 1 3690 ? 217.849 205.585 247.547 1.00 18.01  ? 3690 PRO A CB    1 
ATOM   15512 C  CG    . PRO A 1 3690 ? 218.436 206.228 246.338 1.00 17.24  ? 3690 PRO A CG    1 
ATOM   15513 C  CD    . PRO A 1 3690 ? 217.284 206.506 245.425 1.00 17.34  ? 3690 PRO A CD    1 
ATOM   15514 N  N     . ASP A 1 3691 ? 214.652 205.818 247.970 1.00 19.91  ? 3691 ASP A N     1 
ATOM   15515 C  CA    . ASP A 1 3691 ? 213.528 205.879 248.899 1.00 24.38  ? 3691 ASP A CA    1 
ATOM   15516 C  C     . ASP A 1 3691 ? 212.564 204.721 248.680 1.00 25.47  ? 3691 ASP A C     1 
ATOM   15517 O  O     . ASP A 1 3691 ? 212.069 204.125 249.643 1.00 23.11  ? 3691 ASP A O     1 
ATOM   15518 C  CB    . ASP A 1 3691 ? 212.813 207.227 248.775 1.00 25.28  ? 3691 ASP A CB    1 
ATOM   15519 C  CG    . ASP A 1 3691 ? 212.203 207.453 247.403 1.00 37.06  ? 3691 ASP A CG    1 
ATOM   15520 O  OD1   . ASP A 1 3691 ? 212.362 206.590 246.518 1.00 36.22  ? 3691 ASP A OD1   1 
ATOM   15521 O  OD2   . ASP A 1 3691 ? 211.557 208.503 247.208 1.00 48.24  ? 3691 ASP A OD2   1 
ATOM   15522 N  N     . LEU A 1 3692 ? 212.286 204.384 247.419 1.00 27.07  ? 3692 LEU A N     1 
ATOM   15523 C  CA    . LEU A 1 3692 ? 211.448 203.227 247.130 1.00 20.23  ? 3692 LEU A CA    1 
ATOM   15524 C  C     . LEU A 1 3692 ? 212.179 201.919 247.393 1.00 17.05  ? 3692 LEU A C     1 
ATOM   15525 O  O     . LEU A 1 3692 ? 211.559 200.948 247.839 1.00 18.10  ? 3692 LEU A O     1 
ATOM   15526 C  CB    . LEU A 1 3692 ? 210.960 203.278 245.681 1.00 23.11  ? 3692 LEU A CB    1 
ATOM   15527 C  CG    . LEU A 1 3692 ? 209.997 202.169 245.255 1.00 21.25  ? 3692 LEU A CG    1 
ATOM   15528 C  CD1   . LEU A 1 3692 ? 208.794 202.121 246.180 1.00 18.54  ? 3692 LEU A CD1   1 
ATOM   15529 C  CD2   . LEU A 1 3692 ? 209.556 202.366 243.816 1.00 21.08  ? 3692 LEU A CD2   1 
ATOM   15530 N  N     . CYS A 1 3693 ? 213.490 201.875 247.131 1.00 16.72  ? 3693 CYS A N     1 
ATOM   15531 C  CA    . CYS A 1 3693 ? 214.266 200.674 247.417 1.00 15.76  ? 3693 CYS A CA    1 
ATOM   15532 C  C     . CYS A 1 3693 ? 214.270 200.355 248.904 1.00 16.65  ? 3693 CYS A C     1 
ATOM   15533 O  O     . CYS A 1 3693 ? 214.399 199.187 249.288 1.00 20.82  ? 3693 CYS A O     1 
ATOM   15534 C  CB    . CYS A 1 3693 ? 215.701 200.839 246.917 1.00 20.46  ? 3693 CYS A CB    1 
ATOM   15535 S  SG    . CYS A 1 3693 ? 215.873 200.980 245.129 1.00 28.66  ? 3693 CYS A SG    1 
ATOM   15536 N  N     . SER A 1 3694 ? 214.143 201.376 249.752 1.00 15.86  ? 3694 SER A N     1 
ATOM   15537 C  CA    . SER A 1 3694 ? 214.128 201.146 251.191 1.00 13.33  ? 3694 SER A CA    1 
ATOM   15538 C  C     . SER A 1 3694 ? 212.811 200.551 251.676 1.00 15.06  ? 3694 SER A C     1 
ATOM   15539 O  O     . SER A 1 3694 ? 212.804 199.798 252.654 1.00 16.33  ? 3694 SER A O     1 
ATOM   15540 C  CB    . SER A 1 3694 ? 214.417 202.453 251.932 1.00 10.48  ? 3694 SER A CB    1 
ATOM   15541 O  OG    . SER A 1 3694 ? 213.481 203.456 251.585 1.00 16.41  ? 3694 SER A OG    1 
ATOM   15542 N  N     . ARG A 1 3695 ? 211.695 200.864 251.016 1.00 14.22  ? 3695 ARG A N     1 
ATOM   15543 C  CA    . ARG A 1 3695 ? 210.380 200.478 251.514 1.00 13.01  ? 3695 ARG A CA    1 
ATOM   15544 C  C     . ARG A 1 3695 ? 209.902 199.122 251.013 1.00 14.34  ? 3695 ARG A C     1 
ATOM   15545 O  O     . ARG A 1 3695 ? 208.879 198.630 251.500 1.00 15.24  ? 3695 ARG A O     1 
ATOM   15546 C  CB    . ARG A 1 3695 ? 209.337 201.536 251.137 1.00 14.33  ? 3695 ARG A CB    1 
ATOM   15547 C  CG    . ARG A 1 3695 ? 209.752 202.968 251.424 1.00 13.66  ? 3695 ARG A CG    1 
ATOM   15548 C  CD    . ARG A 1 3695 ? 208.673 203.950 250.985 1.00 15.96  ? 3695 ARG A CD    1 
ATOM   15549 N  NE    . ARG A 1 3695 ? 209.228 205.237 250.579 1.00 21.35  ? 3695 ARG A NE    1 
ATOM   15550 C  CZ    . ARG A 1 3695 ? 209.585 206.200 251.417 1.00 17.28  ? 3695 ARG A CZ    1 
ATOM   15551 N  NH1   . ARG A 1 3695 ? 209.456 206.062 252.726 1.00 15.10  ? 3695 ARG A NH1   1 
ATOM   15552 N  NH2   . ARG A 1 3695 ? 210.085 207.332 250.930 1.00 16.76  ? 3695 ARG A NH2   1 
ATOM   15553 N  N     . VAL A 1 3696 ? 210.602 198.503 250.063 1.00 15.38  ? 3696 VAL A N     1 
ATOM   15554 C  CA    . VAL A 1 3696 ? 210.162 197.247 249.476 1.00 11.77  ? 3696 VAL A CA    1 
ATOM   15555 C  C     . VAL A 1 3696 ? 211.320 196.262 249.487 1.00 14.48  ? 3696 VAL A C     1 
ATOM   15556 O  O     . VAL A 1 3696 ? 212.488 196.639 249.593 1.00 21.53  ? 3696 VAL A O     1 
ATOM   15557 C  CB    . VAL A 1 3696 ? 209.634 197.422 248.035 1.00 11.49  ? 3696 VAL A CB    1 
ATOM   15558 C  CG1   . VAL A 1 3696 ? 208.458 198.385 248.005 1.00 14.53  ? 3696 VAL A CG1   1 
ATOM   15559 C  CG2   . VAL A 1 3696 ? 210.750 197.889 247.119 1.00 11.16  ? 3696 VAL A CG2   1 
ATOM   15560 N  N     . THR A 1 3697 ? 210.975 194.983 249.380 1.00 13.21  ? 3697 THR A N     1 
ATOM   15561 C  CA    . THR A 1 3697 ? 211.950 193.917 249.187 1.00 11.45  ? 3697 THR A CA    1 
ATOM   15562 C  C     . THR A 1 3697 ? 211.835 193.423 247.747 1.00 12.04  ? 3697 THR A C     1 
ATOM   15563 O  O     . THR A 1 3697 ? 210.753 193.035 247.295 1.00 12.27  ? 3697 THR A O     1 
ATOM   15564 C  CB    . THR A 1 3697 ? 211.761 192.791 250.207 1.00 13.71  ? 3697 THR A CB    1 
ATOM   15565 O  OG1   . THR A 1 3697 ? 212.833 191.846 250.090 1.00 30.26  ? 3697 THR A OG1   1 
ATOM   15566 C  CG2   . THR A 1 3697 ? 210.411 192.083 250.069 1.00 11.01  ? 3697 THR A CG2   1 
ATOM   15567 N  N     . PHE A 1 3698 ? 212.938 193.496 247.012 1.00 13.68  ? 3698 PHE A N     1 
ATOM   15568 C  CA    . PHE A 1 3698 ? 212.930 193.101 245.612 1.00 10.47  ? 3698 PHE A CA    1 
ATOM   15569 C  C     . PHE A 1 3698 ? 212.858 191.587 245.478 1.00 11.57  ? 3698 PHE A C     1 
ATOM   15570 O  O     . PHE A 1 3698 ? 213.475 190.848 246.250 1.00 13.55  ? 3698 PHE A O     1 
ATOM   15571 C  CB    . PHE A 1 3698 ? 214.169 193.642 244.904 1.00 9.79   ? 3698 PHE A CB    1 
ATOM   15572 C  CG    . PHE A 1 3698 ? 214.199 195.138 244.798 1.00 11.83  ? 3698 PHE A CG    1 
ATOM   15573 C  CD1   . PHE A 1 3698 ? 213.360 195.798 243.917 1.00 16.28  ? 3698 PHE A CD1   1 
ATOM   15574 C  CD2   . PHE A 1 3698 ? 215.057 195.886 245.586 1.00 11.08  ? 3698 PHE A CD2   1 
ATOM   15575 C  CE1   . PHE A 1 3698 ? 213.383 197.174 243.816 1.00 12.33  ? 3698 PHE A CE1   1 
ATOM   15576 C  CE2   . PHE A 1 3698 ? 215.081 197.262 245.491 1.00 15.72  ? 3698 PHE A CE2   1 
ATOM   15577 C  CZ    . PHE A 1 3698 ? 214.241 197.907 244.604 1.00 14.87  ? 3698 PHE A CZ    1 
ATOM   15578 N  N     . VAL A 1 3699 ? 212.081 191.127 244.502 1.00 13.17  ? 3699 VAL A N     1 
ATOM   15579 C  CA    . VAL A 1 3699 ? 211.963 189.712 244.168 1.00 10.65  ? 3699 VAL A CA    1 
ATOM   15580 C  C     . VAL A 1 3699 ? 212.183 189.616 242.663 1.00 10.81  ? 3699 VAL A C     1 
ATOM   15581 O  O     . VAL A 1 3699 ? 211.253 189.828 241.877 1.00 13.10  ? 3699 VAL A O     1 
ATOM   15582 C  CB    . VAL A 1 3699 ? 210.610 189.118 244.572 1.00 11.27  ? 3699 VAL A CB    1 
ATOM   15583 C  CG1   . VAL A 1 3699 ? 210.639 187.614 244.437 1.00 10.63  ? 3699 VAL A CG1   1 
ATOM   15584 C  CG2   . VAL A 1 3699 ? 210.257 189.512 245.995 1.00 13.71  ? 3699 VAL A CG2   1 
ATOM   15585 N  N     . ASN A 1 3700 ? 213.409 189.300 242.257 1.00 9.77   ? 3700 ASN A N     1 
ATOM   15586 C  CA    . ASN A 1 3700 ? 213.797 189.320 240.851 1.00 10.74  ? 3700 ASN A CA    1 
ATOM   15587 C  C     . ASN A 1 3700 ? 213.562 187.942 240.242 1.00 11.90  ? 3700 ASN A C     1 
ATOM   15588 O  O     . ASN A 1 3700 ? 214.215 186.966 240.623 1.00 12.48  ? 3700 ASN A O     1 
ATOM   15589 C  CB    . ASN A 1 3700 ? 215.256 189.741 240.712 1.00 11.12  ? 3700 ASN A CB    1 
ATOM   15590 C  CG    . ASN A 1 3700 ? 215.539 190.431 239.398 1.00 12.45  ? 3700 ASN A CG    1 
ATOM   15591 O  OD1   . ASN A 1 3700 ? 214.747 190.354 238.461 1.00 16.39  ? 3700 ASN A OD1   1 
ATOM   15592 N  ND2   . ASN A 1 3700 ? 216.671 191.118 239.325 1.00 10.48  ? 3700 ASN A ND2   1 
ATOM   15593 N  N     . PHE A 1 3701 ? 212.632 187.865 239.290 1.00 11.51  ? 3701 PHE A N     1 
ATOM   15594 C  CA    . PHE A 1 3701 ? 212.344 186.622 238.575 1.00 8.65   ? 3701 PHE A CA    1 
ATOM   15595 C  C     . PHE A 1 3701 ? 213.154 186.612 237.282 1.00 13.94  ? 3701 PHE A C     1 
ATOM   15596 O  O     . PHE A 1 3701 ? 212.653 186.883 236.189 1.00 16.52  ? 3701 PHE A O     1 
ATOM   15597 C  CB    . PHE A 1 3701 ? 210.852 186.489 238.301 1.00 11.94  ? 3701 PHE A CB    1 
ATOM   15598 C  CG    . PHE A 1 3701 ? 210.051 186.044 239.488 1.00 11.25  ? 3701 PHE A CG    1 
ATOM   15599 C  CD1   . PHE A 1 3701 ? 209.655 186.953 240.452 1.00 11.00  ? 3701 PHE A CD1   1 
ATOM   15600 C  CD2   . PHE A 1 3701 ? 209.682 184.719 239.631 1.00 7.11   ? 3701 PHE A CD2   1 
ATOM   15601 C  CE1   . PHE A 1 3701 ? 208.912 186.546 241.541 1.00 9.73   ? 3701 PHE A CE1   1 
ATOM   15602 C  CE2   . PHE A 1 3701 ? 208.940 184.307 240.717 1.00 9.77   ? 3701 PHE A CE2   1 
ATOM   15603 C  CZ    . PHE A 1 3701 ? 208.553 185.222 241.672 1.00 11.27  ? 3701 PHE A CZ    1 
ATOM   15604 N  N     . THR A 1 3702 ? 214.434 186.293 237.419 1.00 16.73  ? 3702 THR A N     1 
ATOM   15605 C  CA    . THR A 1 3702 ? 215.320 186.206 236.270 1.00 10.79  ? 3702 THR A CA    1 
ATOM   15606 C  C     . THR A 1 3702 ? 215.291 184.801 235.676 1.00 11.05  ? 3702 THR A C     1 
ATOM   15607 O  O     . THR A 1 3702 ? 214.779 183.851 236.272 1.00 13.27  ? 3702 THR A O     1 
ATOM   15608 C  CB    . THR A 1 3702 ? 216.749 186.587 236.659 1.00 10.62  ? 3702 THR A CB    1 
ATOM   15609 O  OG1   . THR A 1 3702 ? 217.229 185.689 237.667 1.00 17.98  ? 3702 THR A OG1   1 
ATOM   15610 C  CG2   . THR A 1 3702 ? 216.794 188.008 237.188 1.00 11.24  ? 3702 THR A CG2   1 
ATOM   15611 N  N     . VAL A 1 3703 ? 215.847 184.680 234.477 1.00 12.90  ? 3703 VAL A N     1 
ATOM   15612 C  CA    . VAL A 1 3703 ? 215.924 183.413 233.761 1.00 11.78  ? 3703 VAL A CA    1 
ATOM   15613 C  C     . VAL A 1 3703 ? 217.279 182.782 234.043 1.00 14.47  ? 3703 VAL A C     1 
ATOM   15614 O  O     . VAL A 1 3703 ? 218.321 183.422 233.858 1.00 12.15  ? 3703 VAL A O     1 
ATOM   15615 C  CB    . VAL A 1 3703 ? 215.710 183.612 232.251 1.00 12.22  ? 3703 VAL A CB    1 
ATOM   15616 C  CG1   . VAL A 1 3703 ? 215.718 182.275 231.530 1.00 13.38  ? 3703 VAL A CG1   1 
ATOM   15617 C  CG2   . VAL A 1 3703 ? 214.408 184.351 231.996 1.00 15.71  ? 3703 VAL A CG2   1 
ATOM   15618 N  N     . THR A 1 3704 ? 217.267 181.535 234.495 1.00 15.56  ? 3704 THR A N     1 
ATOM   15619 C  CA    . THR A 1 3704 ? 218.485 180.799 234.789 1.00 14.05  ? 3704 THR A CA    1 
ATOM   15620 C  C     . THR A 1 3704 ? 218.811 179.842 233.650 1.00 17.64  ? 3704 THR A C     1 
ATOM   15621 O  O     . THR A 1 3704 ? 217.955 179.497 232.831 1.00 19.19  ? 3704 THR A O     1 
ATOM   15622 C  CB    . THR A 1 3704 ? 218.351 180.019 236.099 1.00 17.81  ? 3704 THR A CB    1 
ATOM   15623 O  OG1   . THR A 1 3704 ? 217.497 178.888 235.897 1.00 15.43  ? 3704 THR A OG1   1 
ATOM   15624 C  CG2   . THR A 1 3704 ? 217.760 180.903 237.186 1.00 18.84  ? 3704 THR A CG2   1 
ATOM   15625 N  N     . ARG A 1 3705 ? 220.076 179.421 233.604 1.00 18.93  ? 3705 ARG A N     1 
ATOM   15626 C  CA    . ARG A 1 3705 ? 220.497 178.478 232.573 1.00 12.57  ? 3705 ARG A CA    1 
ATOM   15627 C  C     . ARG A 1 3705 ? 219.790 177.140 232.725 1.00 15.34  ? 3705 ARG A C     1 
ATOM   15628 O  O     . ARG A 1 3705 ? 219.298 176.574 231.742 1.00 20.15  ? 3705 ARG A O     1 
ATOM   15629 C  CB    . ARG A 1 3705 ? 222.013 178.294 232.617 1.00 13.45  ? 3705 ARG A CB    1 
ATOM   15630 C  CG    . ARG A 1 3705 ? 222.763 179.266 231.732 1.00 18.35  ? 3705 ARG A CG    1 
ATOM   15631 C  CD    . ARG A 1 3705 ? 224.165 179.537 232.238 1.00 23.25  ? 3705 ARG A CD    1 
ATOM   15632 N  NE    . ARG A 1 3705 ? 224.618 180.869 231.854 1.00 24.42  ? 3705 ARG A NE    1 
ATOM   15633 C  CZ    . ARG A 1 3705 ? 225.078 181.186 230.652 1.00 31.89  ? 3705 ARG A CZ    1 
ATOM   15634 N  NH1   . ARG A 1 3705 ? 225.168 180.286 229.686 1.00 33.56  ? 3705 ARG A NH1   1 
ATOM   15635 N  NH2   . ARG A 1 3705 ? 225.456 182.437 230.412 1.00 27.44  ? 3705 ARG A NH2   1 
ATOM   15636 N  N     . SER A 1 3706 ? 219.716 176.624 233.954 1.00 15.56  ? 3706 SER A N     1 
ATOM   15637 C  CA    . SER A 1 3706 ? 219.105 175.318 234.178 1.00 12.94  ? 3706 SER A CA    1 
ATOM   15638 C  C     . SER A 1 3706 ? 217.621 175.326 233.832 1.00 16.48  ? 3706 SER A C     1 
ATOM   15639 O  O     . SER A 1 3706 ? 217.120 174.383 233.207 1.00 21.00  ? 3706 SER A O     1 
ATOM   15640 C  CB    . SER A 1 3706 ? 219.317 174.890 235.628 1.00 16.86  ? 3706 SER A CB    1 
ATOM   15641 O  OG    . SER A 1 3706 ? 218.897 175.906 236.521 1.00 22.19  ? 3706 SER A OG    1 
ATOM   15642 N  N     . SER A 1 3707 ? 216.900 176.375 234.233 1.00 16.25  ? 3707 SER A N     1 
ATOM   15643 C  CA    . SER A 1 3707 ? 215.471 176.436 233.946 1.00 14.62  ? 3707 SER A CA    1 
ATOM   15644 C  C     . SER A 1 3707 ? 215.214 176.520 232.450 1.00 17.44  ? 3707 SER A C     1 
ATOM   15645 O  O     . SER A 1 3707 ? 214.297 175.872 231.931 1.00 29.03  ? 3707 SER A O     1 
ATOM   15646 C  CB    . SER A 1 3707 ? 214.836 177.624 234.667 1.00 15.52  ? 3707 SER A CB    1 
ATOM   15647 O  OG    . SER A 1 3707 ? 215.309 178.851 234.141 1.00 22.42  ? 3707 SER A OG    1 
ATOM   15648 N  N     . LEU A 1 3708 ? 216.013 177.315 231.736 1.00 15.46  ? 3708 LEU A N     1 
ATOM   15649 C  CA    . LEU A 1 3708 ? 215.842 177.414 230.291 1.00 11.85  ? 3708 LEU A CA    1 
ATOM   15650 C  C     . LEU A 1 3708 ? 216.184 176.100 229.602 1.00 15.57  ? 3708 LEU A C     1 
ATOM   15651 O  O     . LEU A 1 3708 ? 215.513 175.708 228.642 1.00 21.88  ? 3708 LEU A O     1 
ATOM   15652 C  CB    . LEU A 1 3708 ? 216.694 178.550 229.733 1.00 13.16  ? 3708 LEU A CB    1 
ATOM   15653 C  CG    . LEU A 1 3708 ? 216.409 178.856 228.265 1.00 11.41  ? 3708 LEU A CG    1 
ATOM   15654 C  CD1   . LEU A 1 3708 ? 214.981 179.341 228.088 1.00 11.44  ? 3708 LEU A CD1   1 
ATOM   15655 C  CD2   . LEU A 1 3708 ? 217.388 179.875 227.746 1.00 9.58   ? 3708 LEU A CD2   1 
ATOM   15656 N  N     . GLN A 1 3709 ? 217.230 175.412 230.067 1.00 16.47  ? 3709 GLN A N     1 
ATOM   15657 C  CA    . GLN A 1 3709 ? 217.548 174.101 229.510 1.00 13.89  ? 3709 GLN A CA    1 
ATOM   15658 C  C     . GLN A 1 3709 ? 216.407 173.119 229.728 1.00 17.97  ? 3709 GLN A C     1 
ATOM   15659 O  O     . GLN A 1 3709 ? 216.048 172.363 228.819 1.00 25.95  ? 3709 GLN A O     1 
ATOM   15660 C  CB    . GLN A 1 3709 ? 218.840 173.560 230.123 1.00 14.60  ? 3709 GLN A CB    1 
ATOM   15661 C  CG    . GLN A 1 3709 ? 220.080 174.345 229.754 1.00 19.43  ? 3709 GLN A CG    1 
ATOM   15662 C  CD    . GLN A 1 3709 ? 221.331 173.789 230.397 1.00 26.56  ? 3709 GLN A CD    1 
ATOM   15663 O  OE1   . GLN A 1 3709 ? 221.269 172.842 231.181 1.00 36.20  ? 3709 GLN A OE1   1 
ATOM   15664 N  NE2   . GLN A 1 3709 ? 222.475 174.377 230.071 1.00 23.29  ? 3709 GLN A NE2   1 
ATOM   15665 N  N     . SER A 1 3710 ? 215.820 173.119 230.927 1.00 16.91  ? 3710 SER A N     1 
ATOM   15666 C  CA    . SER A 1 3710 ? 214.689 172.237 231.194 1.00 18.74  ? 3710 SER A CA    1 
ATOM   15667 C  C     . SER A 1 3710 ? 213.500 172.582 230.305 1.00 19.44  ? 3710 SER A C     1 
ATOM   15668 O  O     . SER A 1 3710 ? 212.839 171.686 229.766 1.00 28.78  ? 3710 SER A O     1 
ATOM   15669 C  CB    . SER A 1 3710 ? 214.298 172.317 232.669 1.00 19.35  ? 3710 SER A CB    1 
ATOM   15670 O  OG    . SER A 1 3710 ? 215.205 171.589 233.476 1.00 25.15  ? 3710 SER A OG    1 
ATOM   15671 N  N     . GLN A 1 3711 ? 213.218 173.875 230.139 1.00 14.63  ? 3711 GLN A N     1 
ATOM   15672 C  CA    . GLN A 1 3711 ? 212.101 174.297 229.298 1.00 16.61  ? 3711 GLN A CA    1 
ATOM   15673 C  C     . GLN A 1 3711 ? 212.309 173.866 227.852 1.00 18.90  ? 3711 GLN A C     1 
ATOM   15674 O  O     . GLN A 1 3711 ? 211.392 173.339 227.208 1.00 23.55  ? 3711 GLN A O     1 
ATOM   15675 C  CB    . GLN A 1 3711 ? 211.933 175.813 229.391 1.00 21.92  ? 3711 GLN A CB    1 
ATOM   15676 C  CG    . GLN A 1 3711 ? 210.682 176.355 228.727 1.00 32.04  ? 3711 GLN A CG    1 
ATOM   15677 C  CD    . GLN A 1 3711 ? 210.441 177.815 229.054 1.00 39.64  ? 3711 GLN A CD    1 
ATOM   15678 O  OE1   . GLN A 1 3711 ? 211.295 178.481 229.638 1.00 34.18  ? 3711 GLN A OE1   1 
ATOM   15679 N  NE2   . GLN A 1 3711 ? 209.273 178.323 228.676 1.00 35.56  ? 3711 GLN A NE2   1 
ATOM   15680 N  N     . CYS A 1 3712 ? 213.517 174.076 227.325 1.00 17.63  ? 3712 CYS A N     1 
ATOM   15681 C  CA    . CYS A 1 3712 ? 213.799 173.708 225.941 1.00 16.12  ? 3712 CYS A CA    1 
ATOM   15682 C  C     . CYS A 1 3712 ? 213.769 172.197 225.749 1.00 17.41  ? 3712 CYS A C     1 
ATOM   15683 O  O     . CYS A 1 3712 ? 213.281 171.709 224.724 1.00 22.08  ? 3712 CYS A O     1 
ATOM   15684 C  CB    . CYS A 1 3712 ? 215.146 174.287 225.513 1.00 15.15  ? 3712 CYS A CB    1 
ATOM   15685 S  SG    . CYS A 1 3712 ? 215.174 176.092 225.456 1.00 23.80  ? 3712 CYS A SG    1 
ATOM   15686 N  N     . LEU A 1 3713 ? 214.282 171.441 226.724 1.00 16.93  ? 3713 LEU A N     1 
ATOM   15687 C  CA    . LEU A 1 3713 ? 214.224 169.986 226.637 1.00 17.96  ? 3713 LEU A CA    1 
ATOM   15688 C  C     . LEU A 1 3713 ? 212.784 169.493 226.650 1.00 20.66  ? 3713 LEU A C     1 
ATOM   15689 O  O     . LEU A 1 3713 ? 212.414 168.608 225.871 1.00 23.79  ? 3713 LEU A O     1 
ATOM   15690 C  CB    . LEU A 1 3713 ? 215.018 169.361 227.783 1.00 19.28  ? 3713 LEU A CB    1 
ATOM   15691 C  CG    . LEU A 1 3713 ? 215.020 167.833 227.871 1.00 22.91  ? 3713 LEU A CG    1 
ATOM   15692 C  CD1   . LEU A 1 3713 ? 215.424 167.217 226.544 1.00 21.59  ? 3713 LEU A CD1   1 
ATOM   15693 C  CD2   . LEU A 1 3713 ? 215.938 167.360 228.984 1.00 21.53  ? 3713 LEU A CD2   1 
ATOM   15694 N  N     . ASN A 1 3714 ? 211.951 170.060 227.527 1.00 20.05  ? 3714 ASN A N     1 
ATOM   15695 C  CA    . ASN A 1 3714 ? 210.547 169.669 227.556 1.00 23.37  ? 3714 ASN A CA    1 
ATOM   15696 C  C     . ASN A 1 3714 ? 209.859 170.003 226.240 1.00 23.50  ? 3714 ASN A C     1 
ATOM   15697 O  O     . ASN A 1 3714 ? 209.075 169.200 225.718 1.00 29.23  ? 3714 ASN A O     1 
ATOM   15698 C  CB    . ASN A 1 3714 ? 209.838 170.352 228.725 1.00 25.73  ? 3714 ASN A CB    1 
ATOM   15699 C  CG    . ASN A 1 3714 ? 210.046 169.623 230.035 1.00 34.02  ? 3714 ASN A CG    1 
ATOM   15700 O  OD1   . ASN A 1 3714 ? 211.178 169.391 230.457 1.00 32.06  ? 3714 ASN A OD1   1 
ATOM   15701 N  ND2   . ASN A 1 3714 ? 208.950 169.259 230.690 1.00 44.65  ? 3714 ASN A ND2   1 
ATOM   15702 N  N     . GLU A 1 3715 ? 210.148 171.181 225.682 1.00 20.84  ? 3715 GLU A N     1 
ATOM   15703 C  CA    . GLU A 1 3715 ? 209.521 171.575 224.424 1.00 26.12  ? 3715 GLU A CA    1 
ATOM   15704 C  C     . GLU A 1 3715 ? 209.941 170.653 223.283 1.00 24.90  ? 3715 GLU A C     1 
ATOM   15705 O  O     . GLU A 1 3715 ? 209.101 170.239 222.474 1.00 24.74  ? 3715 GLU A O     1 
ATOM   15706 C  CB    . GLU A 1 3715 ? 209.864 173.030 224.106 1.00 23.53  ? 3715 GLU A CB    1 
ATOM   15707 C  CG    . GLU A 1 3715 ? 209.054 173.632 222.972 1.00 32.02  ? 3715 GLU A CG    1 
ATOM   15708 C  CD    . GLU A 1 3715 ? 207.577 173.728 223.300 1.00 46.75  ? 3715 GLU A CD    1 
ATOM   15709 O  OE1   . GLU A 1 3715 ? 207.240 173.894 224.491 1.00 47.25  ? 3715 GLU A OE1   1 
ATOM   15710 O  OE2   . GLU A 1 3715 ? 206.751 173.637 222.368 1.00 51.32  ? 3715 GLU A OE2   1 
ATOM   15711 N  N     . VAL A 1 3716 ? 211.231 170.311 223.203 1.00 23.86  ? 3716 VAL A N     1 
ATOM   15712 C  CA    . VAL A 1 3716 ? 211.685 169.449 222.117 1.00 22.95  ? 3716 VAL A CA    1 
ATOM   15713 C  C     . VAL A 1 3716 ? 211.162 168.027 222.289 1.00 26.25  ? 3716 VAL A C     1 
ATOM   15714 O  O     . VAL A 1 3716 ? 210.869 167.349 221.299 1.00 28.69  ? 3716 VAL A O     1 
ATOM   15715 C  CB    . VAL A 1 3716 ? 213.222 169.483 221.981 1.00 21.15  ? 3716 VAL A CB    1 
ATOM   15716 C  CG1   . VAL A 1 3716 ? 213.904 168.817 223.156 1.00 21.16  ? 3716 VAL A CG1   1 
ATOM   15717 C  CG2   . VAL A 1 3716 ? 213.650 168.833 220.676 1.00 22.23  ? 3716 VAL A CG2   1 
ATOM   15718 N  N     . LEU A 1 3717 ? 211.031 167.544 223.530 1.00 28.77  ? 3717 LEU A N     1 
ATOM   15719 C  CA    . LEU A 1 3717 ? 210.445 166.221 223.721 1.00 29.57  ? 3717 LEU A CA    1 
ATOM   15720 C  C     . LEU A 1 3717 ? 208.967 166.215 223.359 1.00 30.89  ? 3717 LEU A C     1 
ATOM   15721 O  O     . LEU A 1 3717 ? 208.468 165.240 222.788 1.00 36.51  ? 3717 LEU A O     1 
ATOM   15722 C  CB    . LEU A 1 3717 ? 210.652 165.740 225.157 1.00 28.19  ? 3717 LEU A CB    1 
ATOM   15723 C  CG    . LEU A 1 3717 ? 212.098 165.473 225.576 1.00 34.03  ? 3717 LEU A CG    1 
ATOM   15724 C  CD1   . LEU A 1 3717 ? 212.176 165.137 227.058 1.00 33.41  ? 3717 LEU A CD1   1 
ATOM   15725 C  CD2   . LEU A 1 3717 ? 212.682 164.353 224.736 1.00 36.15  ? 3717 LEU A CD2   1 
ATOM   15726 N  N     . LYS A 1 3718 ? 208.249 167.293 223.677 1.00 32.72  ? 3718 LYS A N     1 
ATOM   15727 C  CA    . LYS A 1 3718 ? 206.849 167.382 223.277 1.00 35.07  ? 3718 LYS A CA    1 
ATOM   15728 C  C     . LYS A 1 3718 ? 206.714 167.428 221.759 1.00 36.72  ? 3718 LYS A C     1 
ATOM   15729 O  O     . LYS A 1 3718 ? 205.796 166.825 221.193 1.00 40.08  ? 3718 LYS A O     1 
ATOM   15730 C  CB    . LYS A 1 3718 ? 206.195 168.605 223.918 1.00 32.64  ? 3718 LYS A CB    1 
ATOM   15731 C  CG    . LYS A 1 3718 ? 204.721 168.762 223.593 1.00 39.24  ? 3718 LYS A CG    1 
ATOM   15732 C  CD    . LYS A 1 3718 ? 204.101 169.909 224.374 1.00 44.44  ? 3718 LYS A CD    1 
ATOM   15733 C  CE    . LYS A 1 3718 ? 204.577 171.252 223.854 1.00 48.96  ? 3718 LYS A CE    1 
ATOM   15734 N  NZ    . LYS A 1 3718 ? 204.053 171.531 222.489 1.00 59.32  ? 3718 LYS A NZ    1 
ATOM   15735 N  N     . ALA A 1 3719 ? 207.618 168.142 221.086 1.00 37.57  ? 3719 ALA A N     1 
ATOM   15736 C  CA    . ALA A 1 3719 ? 207.527 168.275 219.635 1.00 31.63  ? 3719 ALA A CA    1 
ATOM   15737 C  C     . ALA A 1 3719 ? 207.913 166.983 218.921 1.00 29.75  ? 3719 ALA A C     1 
ATOM   15738 O  O     . ALA A 1 3719 ? 207.232 166.563 217.978 1.00 34.81  ? 3719 ALA A O     1 
ATOM   15739 C  CB    . ALA A 1 3719 ? 208.406 169.431 219.161 1.00 26.10  ? 3719 ALA A CB    1 
ATOM   15740 N  N     . GLU A 1 3720 ? 208.997 166.338 219.351 1.00 31.08  ? 3720 GLU A N     1 
ATOM   15741 C  CA    . GLU A 1 3720 ? 209.555 165.206 218.620 1.00 31.64  ? 3720 GLU A CA    1 
ATOM   15742 C  C     . GLU A 1 3720 ? 209.018 163.862 219.096 1.00 36.60  ? 3720 GLU A C     1 
ATOM   15743 O  O     . GLU A 1 3720 ? 208.772 162.972 218.276 1.00 40.58  ? 3720 GLU A O     1 
ATOM   15744 C  CB    . GLU A 1 3720 ? 211.082 165.216 218.729 1.00 32.82  ? 3720 GLU A CB    1 
ATOM   15745 C  CG    . GLU A 1 3720 ? 211.746 166.311 217.918 1.00 37.23  ? 3720 GLU A CG    1 
ATOM   15746 C  CD    . GLU A 1 3720 ? 211.387 166.239 216.449 1.00 40.18  ? 3720 GLU A CD    1 
ATOM   15747 O  OE1   . GLU A 1 3720 ? 211.770 165.248 215.793 1.00 38.45  ? 3720 GLU A OE1   1 
ATOM   15748 O  OE2   . GLU A 1 3720 ? 210.721 167.170 215.950 1.00 38.58  ? 3720 GLU A OE2   1 
ATOM   15749 N  N     . ARG A 1 3721 ? 208.831 163.692 220.402 1.00 37.26  ? 3721 ARG A N     1 
ATOM   15750 C  CA    . ARG A 1 3721 ? 208.357 162.436 220.982 1.00 37.33  ? 3721 ARG A CA    1 
ATOM   15751 C  C     . ARG A 1 3721 ? 207.152 162.730 221.863 1.00 38.03  ? 3721 ARG A C     1 
ATOM   15752 O  O     . ARG A 1 3721 ? 207.243 162.691 223.096 1.00 40.56  ? 3721 ARG A O     1 
ATOM   15753 C  CB    . ARG A 1 3721 ? 209.468 161.747 221.776 1.00 34.74  ? 3721 ARG A CB    1 
ATOM   15754 C  CG    . ARG A 1 3721 ? 210.765 161.553 221.005 1.00 31.64  ? 3721 ARG A CG    1 
ATOM   15755 C  CD    . ARG A 1 3721 ? 210.637 160.454 219.963 1.00 42.55  ? 3721 ARG A CD    1 
ATOM   15756 N  NE    . ARG A 1 3721 ? 211.102 159.164 220.460 1.00 48.56  ? 3721 ARG A NE    1 
ATOM   15757 C  CZ    . ARG A 1 3721 ? 212.377 158.816 220.568 1.00 43.81  ? 3721 ARG A CZ    1 
ATOM   15758 N  NH1   . ARG A 1 3721 ? 213.351 159.640 220.217 1.00 38.78  ? 3721 ARG A NH1   1 
ATOM   15759 N  NH2   . ARG A 1 3721 ? 212.682 157.610 221.037 1.00 35.98  ? 3721 ARG A NH2   1 
ATOM   15760 N  N     . PRO A 1 3722 ? 206.001 163.041 221.257 1.00 37.38  ? 3722 PRO A N     1 
ATOM   15761 C  CA    . PRO A 1 3722 ? 204.825 163.408 222.069 1.00 40.57  ? 3722 PRO A CA    1 
ATOM   15762 C  C     . PRO A 1 3722 ? 204.383 162.317 223.028 1.00 43.66  ? 3722 PRO A C     1 
ATOM   15763 O  O     . PRO A 1 3722 ? 203.944 162.620 224.145 1.00 46.35  ? 3722 PRO A O     1 
ATOM   15764 C  CB    . PRO A 1 3722 ? 203.754 163.709 221.011 1.00 40.64  ? 3722 PRO A CB    1 
ATOM   15765 C  CG    . PRO A 1 3722 ? 204.198 162.961 219.795 1.00 38.46  ? 3722 PRO A CG    1 
ATOM   15766 C  CD    . PRO A 1 3722 ? 205.692 163.005 219.819 1.00 34.41  ? 3722 PRO A CD    1 
ATOM   15767 N  N     . ASP A 1 3723 ? 204.487 161.048 222.623 1.00 44.80  ? 3723 ASP A N     1 
ATOM   15768 C  CA    . ASP A 1 3723 ? 204.127 159.959 223.525 1.00 45.30  ? 3723 ASP A CA    1 
ATOM   15769 C  C     . ASP A 1 3723 ? 205.049 159.925 224.737 1.00 48.60  ? 3723 ASP A C     1 
ATOM   15770 O  O     . ASP A 1 3723 ? 204.590 159.740 225.870 1.00 55.37  ? 3723 ASP A O     1 
ATOM   15771 C  CB    . ASP A 1 3723 ? 204.160 158.625 222.779 1.00 42.84  ? 3723 ASP A CB    1 
ATOM   15772 C  CG    . ASP A 1 3723 ? 205.516 158.329 222.170 1.00 47.16  ? 3723 ASP A CG    1 
ATOM   15773 O  OD1   . ASP A 1 3723 ? 206.123 159.253 221.589 1.00 45.51  ? 3723 ASP A OD1   1 
ATOM   15774 O  OD2   . ASP A 1 3723 ? 205.974 157.173 222.272 1.00 49.09  ? 3723 ASP A OD2   1 
ATOM   15775 N  N     . VAL A 1 3724 ? 206.351 160.123 224.521 1.00 41.38  ? 3724 VAL A N     1 
ATOM   15776 C  CA    . VAL A 1 3724 ? 207.299 160.130 225.632 1.00 41.21  ? 3724 VAL A CA    1 
ATOM   15777 C  C     . VAL A 1 3724 ? 207.035 161.316 226.551 1.00 48.50  ? 3724 VAL A C     1 
ATOM   15778 O  O     . VAL A 1 3724 ? 207.138 161.204 227.777 1.00 54.19  ? 3724 VAL A O     1 
ATOM   15779 C  CB    . VAL A 1 3724 ? 208.744 160.128 225.100 1.00 40.43  ? 3724 VAL A CB    1 
ATOM   15780 C  CG1   . VAL A 1 3724 ? 209.738 160.143 226.250 1.00 37.26  ? 3724 VAL A CG1   1 
ATOM   15781 C  CG2   . VAL A 1 3724 ? 208.976 158.922 224.208 1.00 37.77  ? 3724 VAL A CG2   1 
ATOM   15782 N  N     . ASP A 1 3725 ? 206.695 162.473 225.975 1.00 47.71  ? 3725 ASP A N     1 
ATOM   15783 C  CA    . ASP A 1 3725 ? 206.398 163.645 226.793 1.00 46.02  ? 3725 ASP A CA    1 
ATOM   15784 C  C     . ASP A 1 3725 ? 205.145 163.433 227.635 1.00 52.79  ? 3725 ASP A C     1 
ATOM   15785 O  O     . ASP A 1 3725 ? 205.112 163.794 228.818 1.00 63.52  ? 3725 ASP A O     1 
ATOM   15786 C  CB    . ASP A 1 3725 ? 206.248 164.880 225.907 1.00 41.89  ? 3725 ASP A CB    1 
ATOM   15787 C  CG    . ASP A 1 3725 ? 205.804 166.103 226.685 1.00 56.00  ? 3725 ASP A CG    1 
ATOM   15788 O  OD1   . ASP A 1 3725 ? 206.483 166.463 227.669 1.00 52.72  ? 3725 ASP A OD1   1 
ATOM   15789 O  OD2   . ASP A 1 3725 ? 204.775 166.705 226.313 1.00 62.60  ? 3725 ASP A OD2   1 
ATOM   15790 N  N     . GLU A 1 3726 ? 204.101 162.849 227.046 1.00 52.84  ? 3726 GLU A N     1 
ATOM   15791 C  CA    . GLU A 1 3726 ? 202.891 162.580 227.813 1.00 51.83  ? 3726 GLU A CA    1 
ATOM   15792 C  C     . GLU A 1 3726 ? 203.166 161.551 228.904 1.00 52.55  ? 3726 GLU A C     1 
ATOM   15793 O  O     . GLU A 1 3726 ? 202.664 161.674 230.031 1.00 57.12  ? 3726 GLU A O     1 
ATOM   15794 C  CB    . GLU A 1 3726 ? 201.781 162.118 226.865 1.00 53.90  ? 3726 GLU A CB    1 
ATOM   15795 C  CG    . GLU A 1 3726 ? 200.381 162.029 227.461 1.00 65.76  ? 3726 GLU A CG    1 
ATOM   15796 C  CD    . GLU A 1 3726 ? 200.116 160.731 228.189 1.00 75.19  ? 3726 GLU A CD    1 
ATOM   15797 O  OE1   . GLU A 1 3726 ? 200.725 159.705 227.827 1.00 73.01  ? 3726 GLU A OE1   1 
ATOM   15798 O  OE2   . GLU A 1 3726 ? 199.273 160.739 229.110 1.00 73.89  ? 3726 GLU A OE2   1 
ATOM   15799 N  N     . LYS A 1 3727 ? 203.997 160.550 228.597 1.00 54.00  ? 3727 LYS A N     1 
ATOM   15800 C  CA    . LYS A 1 3727 ? 204.352 159.547 229.592 1.00 58.05  ? 3727 LYS A CA    1 
ATOM   15801 C  C     . LYS A 1 3727 ? 205.135 160.156 230.750 1.00 57.89  ? 3727 LYS A C     1 
ATOM   15802 O  O     . LYS A 1 3727 ? 204.875 159.835 231.914 1.00 67.38  ? 3727 LYS A O     1 
ATOM   15803 C  CB    . LYS A 1 3727 ? 205.149 158.419 228.935 1.00 54.99  ? 3727 LYS A CB    1 
ATOM   15804 C  CG    . LYS A 1 3727 ? 205.843 157.492 229.917 1.00 57.15  ? 3727 LYS A CG    1 
ATOM   15805 C  CD    . LYS A 1 3727 ? 206.697 156.467 229.192 1.00 60.15  ? 3727 LYS A CD    1 
ATOM   15806 C  CE    . LYS A 1 3727 ? 205.860 155.650 228.224 1.00 61.67  ? 3727 LYS A CE    1 
ATOM   15807 N  NZ    . LYS A 1 3727 ? 204.806 154.863 228.924 1.00 57.53  ? 3727 LYS A NZ    1 
ATOM   15808 N  N     . ARG A 1 3728 ? 206.098 161.037 230.461 1.00 52.15  ? 3728 ARG A N     1 
ATOM   15809 C  CA    . ARG A 1 3728 ? 206.844 161.664 231.551 1.00 54.33  ? 3728 ARG A CA    1 
ATOM   15810 C  C     . ARG A 1 3728 ? 205.957 162.601 232.361 1.00 57.58  ? 3728 ARG A C     1 
ATOM   15811 O  O     . ARG A 1 3728 ? 206.134 162.729 233.577 1.00 62.09  ? 3728 ARG A O     1 
ATOM   15812 C  CB    . ARG A 1 3728 ? 208.077 162.415 231.042 1.00 47.64  ? 3728 ARG A CB    1 
ATOM   15813 C  CG    . ARG A 1 3728 ? 207.805 163.482 230.013 1.00 53.33  ? 3728 ARG A CG    1 
ATOM   15814 C  CD    . ARG A 1 3728 ? 208.943 164.480 229.906 1.00 50.91  ? 3728 ARG A CD    1 
ATOM   15815 N  NE    . ARG A 1 3728 ? 209.003 165.326 231.093 1.00 47.24  ? 3728 ARG A NE    1 
ATOM   15816 C  CZ    . ARG A 1 3728 ? 210.123 165.718 231.686 1.00 46.70  ? 3728 ARG A CZ    1 
ATOM   15817 N  NH1   . ARG A 1 3728 ? 211.310 165.356 231.228 1.00 43.64  ? 3728 ARG A NH1   1 
ATOM   15818 N  NH2   . ARG A 1 3728 ? 210.048 166.494 232.762 1.00 54.65  ? 3728 ARG A NH2   1 
ATOM   15819 N  N     . SER A 1 3729 ? 205.005 163.276 231.713 1.00 53.44  ? 3729 SER A N     1 
ATOM   15820 C  CA    . SER A 1 3729 ? 204.068 164.098 232.474 1.00 53.80  ? 3729 SER A CA    1 
ATOM   15821 C  C     . SER A 1 3729 ? 203.258 163.241 233.442 1.00 59.03  ? 3729 SER A C     1 
ATOM   15822 O  O     . SER A 1 3729 ? 203.104 163.589 234.624 1.00 57.62  ? 3729 SER A O     1 
ATOM   15823 C  CB    . SER A 1 3729 ? 203.146 164.857 231.522 1.00 57.01  ? 3729 SER A CB    1 
ATOM   15824 O  OG    . SER A 1 3729 ? 203.894 165.561 230.546 1.00 59.81  ? 3729 SER A OG    1 
ATOM   15825 N  N     . ASP A 1 3730 ? 202.759 162.098 232.962 1.00 58.99  ? 3730 ASP A N     1 
ATOM   15826 C  CA    . ASP A 1 3730 ? 202.051 161.174 233.841 1.00 61.90  ? 3730 ASP A CA    1 
ATOM   15827 C  C     . ASP A 1 3730 ? 202.952 160.682 234.965 1.00 64.27  ? 3730 ASP A C     1 
ATOM   15828 O  O     . ASP A 1 3730 ? 202.512 160.549 236.110 1.00 69.00  ? 3730 ASP A O     1 
ATOM   15829 C  CB    . ASP A 1 3730 ? 201.513 159.987 233.044 1.00 63.29  ? 3730 ASP A CB    1 
ATOM   15830 C  CG    . ASP A 1 3730 ? 200.364 160.361 232.142 1.00 68.46  ? 3730 ASP A CG    1 
ATOM   15831 O  OD1   . ASP A 1 3730 ? 199.896 161.517 232.213 1.00 66.30  ? 3730 ASP A OD1   1 
ATOM   15832 O  OD2   . ASP A 1 3730 ? 199.918 159.486 231.371 1.00 69.95  ? 3730 ASP A OD2   1 
ATOM   15833 N  N     . LEU A 1 3731 ? 204.214 160.392 234.649 1.00 58.96  ? 3731 LEU A N     1 
ATOM   15834 C  CA    . LEU A 1 3731 ? 205.138 159.883 235.657 1.00 59.92  ? 3731 LEU A CA    1 
ATOM   15835 C  C     . LEU A 1 3731 ? 205.425 160.919 236.735 1.00 63.05  ? 3731 LEU A C     1 
ATOM   15836 O  O     . LEU A 1 3731 ? 205.478 160.581 237.921 1.00 67.44  ? 3731 LEU A O     1 
ATOM   15837 C  CB    . LEU A 1 3731 ? 206.433 159.423 234.995 1.00 62.80  ? 3731 LEU A CB    1 
ATOM   15838 C  CG    . LEU A 1 3731 ? 206.580 157.915 234.801 1.00 63.87  ? 3731 LEU A CG    1 
ATOM   15839 C  CD1   . LEU A 1 3731 ? 205.570 157.379 233.799 1.00 58.71  ? 3731 LEU A CD1   1 
ATOM   15840 C  CD2   . LEU A 1 3731 ? 207.987 157.606 234.354 1.00 66.17  ? 3731 LEU A CD2   1 
ATOM   15841 N  N     . LEU A 1 3732 ? 205.628 162.181 236.349 1.00 63.70  ? 3732 LEU A N     1 
ATOM   15842 C  CA    . LEU A 1 3732 ? 205.826 163.233 237.343 1.00 62.81  ? 3732 LEU A CA    1 
ATOM   15843 C  C     . LEU A 1 3732 ? 204.590 163.400 238.219 1.00 64.07  ? 3732 LEU A C     1 
ATOM   15844 O  O     . LEU A 1 3732 ? 204.701 163.537 239.444 1.00 62.41  ? 3732 LEU A O     1 
ATOM   15845 C  CB    . LEU A 1 3732 ? 206.191 164.558 236.672 1.00 54.89  ? 3732 LEU A CB    1 
ATOM   15846 C  CG    . LEU A 1 3732 ? 207.655 164.873 236.338 1.00 55.59  ? 3732 LEU A CG    1 
ATOM   15847 C  CD1   . LEU A 1 3732 ? 208.472 164.980 237.620 1.00 57.99  ? 3732 LEU A CD1   1 
ATOM   15848 C  CD2   . LEU A 1 3732 ? 208.286 163.868 235.399 1.00 55.44  ? 3732 LEU A CD2   1 
ATOM   15849 N  N     . LYS A 1 3733 ? 203.400 163.390 237.610 1.00 67.71  ? 3733 LYS A N     1 
ATOM   15850 C  CA    . LYS A 1 3733 ? 202.183 163.506 238.411 1.00 63.48  ? 3733 LYS A CA    1 
ATOM   15851 C  C     . LYS A 1 3733 ? 202.056 162.343 239.391 1.00 69.70  ? 3733 LYS A C     1 
ATOM   15852 O  O     . LYS A 1 3733 ? 201.747 162.544 240.575 1.00 72.59  ? 3733 LYS A O     1 
ATOM   15853 C  CB    . LYS A 1 3733 ? 200.958 163.579 237.502 1.00 60.12  ? 3733 LYS A CB    1 
ATOM   15854 C  CG    . LYS A 1 3733 ? 199.710 164.098 238.190 1.00 65.99  ? 3733 LYS A CG    1 
ATOM   15855 C  CD    . LYS A 1 3733 ? 199.697 165.617 238.235 1.00 67.58  ? 3733 LYS A CD    1 
ATOM   15856 C  CE    . LYS A 1 3733 ? 198.293 166.149 238.472 1.00 68.77  ? 3733 LYS A CE    1 
ATOM   15857 N  NZ    . LYS A 1 3733 ? 198.028 166.383 239.918 1.00 67.73  ? 3733 LYS A NZ    1 
ATOM   15858 N  N     . LEU A 1 3734 ? 202.311 161.122 238.915 1.00 68.86  ? 3734 LEU A N     1 
ATOM   15859 C  CA    . LEU A 1 3734 ? 202.209 159.948 239.773 1.00 68.43  ? 3734 LEU A CA    1 
ATOM   15860 C  C     . LEU A 1 3734 ? 203.236 159.990 240.893 1.00 69.73  ? 3734 LEU A C     1 
ATOM   15861 O  O     . LEU A 1 3734 ? 202.926 159.643 242.035 1.00 74.42  ? 3734 LEU A O     1 
ATOM   15862 C  CB    . LEU A 1 3734 ? 202.376 158.673 238.944 1.00 63.24  ? 3734 LEU A CB    1 
ATOM   15863 C  CG    . LEU A 1 3734 ? 201.100 157.956 238.497 1.00 71.68  ? 3734 LEU A CG    1 
ATOM   15864 C  CD1   . LEU A 1 3734 ? 200.125 158.921 237.835 1.00 72.75  ? 3734 LEU A CD1   1 
ATOM   15865 C  CD2   . LEU A 1 3734 ? 201.434 156.799 237.568 1.00 68.95  ? 3734 LEU A CD2   1 
ATOM   15866 N  N     . GLN A 1 3735 ? 204.467 160.406 240.588 1.00 67.00  ? 3735 GLN A N     1 
ATOM   15867 C  CA    . GLN A 1 3735 ? 205.504 160.476 241.612 1.00 62.12  ? 3735 GLN A CA    1 
ATOM   15868 C  C     . GLN A 1 3735 ? 205.170 161.522 242.666 1.00 63.09  ? 3735 GLN A C     1 
ATOM   15869 O  O     . GLN A 1 3735 ? 205.386 161.293 243.862 1.00 66.47  ? 3735 GLN A O     1 
ATOM   15870 C  CB    . GLN A 1 3735 ? 206.856 160.771 240.967 1.00 64.84  ? 3735 GLN A CB    1 
ATOM   15871 C  CG    . GLN A 1 3735 ? 207.488 159.574 240.280 1.00 68.04  ? 3735 GLN A CG    1 
ATOM   15872 C  CD    . GLN A 1 3735 ? 208.870 159.874 239.736 1.00 79.67  ? 3735 GLN A CD    1 
ATOM   15873 O  OE1   . GLN A 1 3735 ? 209.252 161.035 239.587 1.00 79.67  ? 3735 GLN A OE1   1 
ATOM   15874 N  NE2   . GLN A 1 3735 ? 209.628 158.827 239.432 1.00 74.82  ? 3735 GLN A NE2   1 
ATOM   15875 N  N     . GLY A 1 3736 ? 204.648 162.677 242.247 1.00 63.63  ? 3736 GLY A N     1 
ATOM   15876 C  CA    . GLY A 1 3736 ? 204.237 163.677 243.219 1.00 65.16  ? 3736 GLY A CA    1 
ATOM   15877 C  C     . GLY A 1 3736 ? 203.126 163.179 244.120 1.00 69.48  ? 3736 GLY A C     1 
ATOM   15878 O  O     . GLY A 1 3736 ? 203.185 163.326 245.347 1.00 67.31  ? 3736 GLY A O     1 
ATOM   15879 N  N     . GLU A 1 3737 ? 202.101 162.560 243.524 1.00 73.64  ? 3737 GLU A N     1 
ATOM   15880 C  CA    . GLU A 1 3737 ? 201.014 161.997 244.320 1.00 69.36  ? 3737 GLU A CA    1 
ATOM   15881 C  C     . GLU A 1 3737 ? 201.525 160.912 245.259 1.00 63.81  ? 3737 GLU A C     1 
ATOM   15882 O  O     . GLU A 1 3737 ? 201.077 160.808 246.406 1.00 69.27  ? 3737 GLU A O     1 
ATOM   15883 C  CB    . GLU A 1 3737 ? 199.927 161.440 243.403 1.00 70.99  ? 3737 GLU A CB    1 
ATOM   15884 C  CG    . GLU A 1 3737 ? 199.091 162.501 242.711 1.00 77.25  ? 3737 GLU A CG    1 
ATOM   15885 C  CD    . GLU A 1 3737 ? 198.171 161.916 241.660 1.00 89.62  ? 3737 GLU A CD    1 
ATOM   15886 O  OE1   . GLU A 1 3737 ? 198.212 160.685 241.453 1.00 85.69  ? 3737 GLU A OE1   1 
ATOM   15887 O  OE2   . GLU A 1 3737 ? 197.407 162.685 241.039 1.00 91.00  ? 3737 GLU A OE2   1 
ATOM   15888 N  N     . PHE A 1 3738 ? 202.475 160.103 244.793 1.00 64.04  ? 3738 PHE A N     1 
ATOM   15889 C  CA    . PHE A 1 3738 ? 202.982 158.990 245.584 1.00 68.69  ? 3738 PHE A CA    1 
ATOM   15890 C  C     . PHE A 1 3738 ? 203.794 159.488 246.772 1.00 69.64  ? 3738 PHE A C     1 
ATOM   15891 O  O     . PHE A 1 3738 ? 203.675 158.958 247.883 1.00 71.83  ? 3738 PHE A O     1 
ATOM   15892 C  CB    . PHE A 1 3738 ? 203.832 158.088 244.693 1.00 66.68  ? 3738 PHE A CB    1 
ATOM   15893 C  CG    . PHE A 1 3738 ? 203.029 157.152 243.836 1.00 69.95  ? 3738 PHE A CG    1 
ATOM   15894 C  CD1   . PHE A 1 3738 ? 201.645 157.168 243.874 1.00 66.97  ? 3738 PHE A CD1   1 
ATOM   15895 C  CD2   . PHE A 1 3738 ? 203.660 156.294 242.952 1.00 71.91  ? 3738 PHE A CD2   1 
ATOM   15896 C  CE1   . PHE A 1 3738 ? 200.906 156.322 243.072 1.00 67.09  ? 3738 PHE A CE1   1 
ATOM   15897 C  CE2   . PHE A 1 3738 ? 202.926 155.449 242.144 1.00 69.37  ? 3738 PHE A CE2   1 
ATOM   15898 C  CZ    . PHE A 1 3738 ? 201.547 155.463 242.204 1.00 69.03  ? 3738 PHE A CZ    1 
ATOM   15899 N  N     . GLN A 1 3739 ? 204.630 160.505 246.553 1.00 69.86  ? 3739 GLN A N     1 
ATOM   15900 C  CA    . GLN A 1 3739 ? 205.393 161.084 247.653 1.00 69.10  ? 3739 GLN A CA    1 
ATOM   15901 C  C     . GLN A 1 3739 ? 204.475 161.774 248.652 1.00 65.76  ? 3739 GLN A C     1 
ATOM   15902 O  O     . GLN A 1 3739 ? 204.693 161.688 249.868 1.00 66.81  ? 3739 GLN A O     1 
ATOM   15903 C  CB    . GLN A 1 3739 ? 206.440 162.056 247.111 1.00 68.31  ? 3739 GLN A CB    1 
ATOM   15904 C  CG    . GLN A 1 3739 ? 207.560 161.416 246.284 1.00 69.74  ? 3739 GLN A CG    1 
ATOM   15905 C  CD    . GLN A 1 3739 ? 208.502 160.519 247.083 1.00 76.19  ? 3739 GLN A CD    1 
ATOM   15906 O  OE1   . GLN A 1 3739 ? 208.120 159.903 248.078 1.00 72.01  ? 3739 GLN A OE1   1 
ATOM   15907 N  NE2   . GLN A 1 3739 ? 209.752 160.447 246.637 1.00 75.85  ? 3739 GLN A NE2   1 
ATOM   15908 N  N     . LEU A 1 3740 ? 203.434 162.457 248.161 1.00 65.54  ? 3740 LEU A N     1 
ATOM   15909 C  CA    . LEU A 1 3740 ? 202.450 163.037 249.068 1.00 59.93  ? 3740 LEU A CA    1 
ATOM   15910 C  C     . LEU A 1 3740 ? 201.768 161.958 249.898 1.00 64.58  ? 3740 LEU A C     1 
ATOM   15911 O  O     . LEU A 1 3740 ? 201.572 162.126 251.107 1.00 71.99  ? 3740 LEU A O     1 
ATOM   15912 C  CB    . LEU A 1 3740 ? 201.415 163.836 248.278 1.00 55.58  ? 3740 LEU A CB    1 
ATOM   15913 C  CG    . LEU A 1 3740 ? 200.273 164.443 249.096 1.00 56.21  ? 3740 LEU A CG    1 
ATOM   15914 C  CD1   . LEU A 1 3740 ? 200.665 165.806 249.634 1.00 57.96  ? 3740 LEU A CD1   1 
ATOM   15915 C  CD2   . LEU A 1 3740 ? 199.007 164.535 248.261 1.00 58.68  ? 3740 LEU A CD2   1 
ATOM   15916 N  N     . ARG A 1 3741 ? 201.402 160.842 249.264 1.00 66.40  ? 3741 ARG A N     1 
ATOM   15917 C  CA    . ARG A 1 3741 ? 200.764 159.748 249.987 1.00 67.61  ? 3741 ARG A CA    1 
ATOM   15918 C  C     . ARG A 1 3741 ? 201.697 159.158 251.036 1.00 66.04  ? 3741 ARG A C     1 
ATOM   15919 O  O     . ARG A 1 3741 ? 201.267 158.850 252.151 1.00 68.84  ? 3741 ARG A O     1 
ATOM   15920 C  CB    . ARG A 1 3741 ? 200.305 158.669 249.006 1.00 71.55  ? 3741 ARG A CB    1 
ATOM   15921 C  CG    . ARG A 1 3741 ? 199.228 157.746 249.554 1.00 79.16  ? 3741 ARG A CG    1 
ATOM   15922 C  CD    . ARG A 1 3741 ? 198.054 158.527 250.117 1.00 76.01  ? 3741 ARG A CD    1 
ATOM   15923 N  NE    . ARG A 1 3741 ? 197.285 157.734 251.067 1.00 82.83  ? 3741 ARG A NE    1 
ATOM   15924 C  CZ    . ARG A 1 3741 ? 196.190 158.155 251.684 1.00 88.37  ? 3741 ARG A CZ    1 
ATOM   15925 N  NH1   . ARG A 1 3741 ? 195.700 159.365 251.473 1.00 84.08  ? 3741 ARG A NH1   1 
ATOM   15926 N  NH2   . ARG A 1 3741 ? 195.569 157.341 252.533 1.00 86.78  ? 3741 ARG A NH2   1 
ATOM   15927 N  N     . LEU A 1 3742 ? 202.977 158.990 250.697 1.00 62.72  ? 3742 LEU A N     1 
ATOM   15928 C  CA    . LEU A 1 3742 ? 203.933 158.468 251.670 1.00 57.54  ? 3742 LEU A CA    1 
ATOM   15929 C  C     . LEU A 1 3742 ? 204.087 159.413 252.857 1.00 67.61  ? 3742 LEU A C     1 
ATOM   15930 O  O     . LEU A 1 3742 ? 204.138 158.970 254.012 1.00 73.77  ? 3742 LEU A O     1 
ATOM   15931 C  CB    . LEU A 1 3742 ? 205.287 158.225 251.004 1.00 55.40  ? 3742 LEU A CB    1 
ATOM   15932 C  CG    . LEU A 1 3742 ? 205.463 156.906 250.251 1.00 60.87  ? 3742 LEU A CG    1 
ATOM   15933 C  CD1   . LEU A 1 3742 ? 206.912 156.718 249.837 1.00 58.46  ? 3742 LEU A CD1   1 
ATOM   15934 C  CD2   . LEU A 1 3742 ? 204.987 155.734 251.094 1.00 65.27  ? 3742 LEU A CD2   1 
ATOM   15935 N  N     . ARG A 1 3743 ? 204.167 160.719 252.590 1.00 68.15  ? 3743 ARG A N     1 
ATOM   15936 C  CA    . ARG A 1 3743 ? 204.276 161.690 253.675 1.00 64.02  ? 3743 ARG A CA    1 
ATOM   15937 C  C     . ARG A 1 3743 ? 203.034 161.670 254.561 1.00 69.48  ? 3743 ARG A C     1 
ATOM   15938 O  O     . ARG A 1 3743 ? 203.140 161.709 255.796 1.00 71.71  ? 3743 ARG A O     1 
ATOM   15939 C  CB    . ARG A 1 3743 ? 204.513 163.084 253.100 1.00 60.39  ? 3743 ARG A CB    1 
ATOM   15940 C  CG    . ARG A 1 3743 ? 205.950 163.331 252.668 1.00 64.57  ? 3743 ARG A CG    1 
ATOM   15941 C  CD    . ARG A 1 3743 ? 206.166 164.773 252.242 1.00 56.60  ? 3743 ARG A CD    1 
ATOM   15942 N  NE    . ARG A 1 3743 ? 205.935 164.957 250.815 1.00 53.18  ? 3743 ARG A NE    1 
ATOM   15943 C  CZ    . ARG A 1 3743 ? 204.895 165.599 250.300 1.00 53.20  ? 3743 ARG A CZ    1 
ATOM   15944 N  NH1   . ARG A 1 3743 ? 203.957 166.123 251.070 1.00 46.57  ? 3743 ARG A NH1   1 
ATOM   15945 N  NH2   . ARG A 1 3743 ? 204.794 165.717 248.980 1.00 55.75  ? 3743 ARG A NH2   1 
ATOM   15946 N  N     . GLN A 1 3744 ? 201.848 161.604 253.949 1.00 67.97  ? 3744 GLN A N     1 
ATOM   15947 C  CA    . GLN A 1 3744 ? 200.616 161.528 254.726 1.00 65.78  ? 3744 GLN A CA    1 
ATOM   15948 C  C     . GLN A 1 3744 ? 200.564 160.252 255.555 1.00 68.67  ? 3744 GLN A C     1 
ATOM   15949 O  O     . GLN A 1 3744 ? 200.103 160.269 256.700 1.00 70.11  ? 3744 GLN A O     1 
ATOM   15950 C  CB    . GLN A 1 3744 ? 199.398 161.612 253.806 1.00 65.47  ? 3744 GLN A CB    1 
ATOM   15951 C  CG    . GLN A 1 3744 ? 199.267 162.920 253.047 1.00 67.90  ? 3744 GLN A CG    1 
ATOM   15952 C  CD    . GLN A 1 3744 ? 197.869 163.134 252.501 1.00 73.83  ? 3744 GLN A CD    1 
ATOM   15953 O  OE1   . GLN A 1 3744 ? 197.669 163.207 251.289 1.00 71.67  ? 3744 GLN A OE1   1 
ATOM   15954 N  NE2   . GLN A 1 3744 ? 196.894 163.239 253.396 1.00 71.22  ? 3744 GLN A NE2   1 
ATOM   15955 N  N     . LEU A 1 3745 ? 201.020 159.132 254.990 1.00 71.49  ? 3745 LEU A N     1 
ATOM   15956 C  CA    . LEU A 1 3745 ? 201.028 157.876 255.732 1.00 74.00  ? 3745 LEU A CA    1 
ATOM   15957 C  C     . LEU A 1 3745 ? 201.970 157.945 256.924 1.00 73.08  ? 3745 LEU A C     1 
ATOM   15958 O  O     . LEU A 1 3745 ? 201.635 157.467 258.014 1.00 81.66  ? 3745 LEU A O     1 
ATOM   15959 C  CB    . LEU A 1 3745 ? 201.418 156.724 254.808 1.00 69.49  ? 3745 LEU A CB    1 
ATOM   15960 C  CG    . LEU A 1 3745 ? 200.366 156.300 253.784 1.00 71.59  ? 3745 LEU A CG    1 
ATOM   15961 C  CD1   . LEU A 1 3745 ? 200.826 155.065 253.035 1.00 79.27  ? 3745 LEU A CD1   1 
ATOM   15962 C  CD2   . LEU A 1 3745 ? 199.027 156.060 254.452 1.00 74.30  ? 3745 LEU A CD2   1 
ATOM   15963 N  N     . GLU A 1 3746 ? 203.154 158.532 256.737 1.00 68.85  ? 3746 GLU A N     1 
ATOM   15964 C  CA    . GLU A 1 3746 ? 204.084 158.682 257.851 1.00 74.71  ? 3746 GLU A CA    1 
ATOM   15965 C  C     . GLU A 1 3746 ? 203.489 159.562 258.943 1.00 74.69  ? 3746 GLU A C     1 
ATOM   15966 O  O     . GLU A 1 3746 ? 203.550 159.226 260.134 1.00 78.29  ? 3746 GLU A O     1 
ATOM   15967 C  CB    . GLU A 1 3746 ? 205.409 159.258 257.352 1.00 73.74  ? 3746 GLU A CB    1 
ATOM   15968 C  CG    . GLU A 1 3746 ? 206.547 159.156 258.353 1.00 74.44  ? 3746 GLU A CG    1 
ATOM   15969 C  CD    . GLU A 1 3746 ? 206.624 157.792 259.010 1.00 86.45  ? 3746 GLU A CD    1 
ATOM   15970 O  OE1   . GLU A 1 3746 ? 207.242 156.881 258.420 1.00 81.49  ? 3746 GLU A OE1   1 
ATOM   15971 O  OE2   . GLU A 1 3746 ? 206.074 157.633 260.120 1.00 92.06  ? 3746 GLU A OE2   1 
ATOM   15972 N  N     . LYS A 1 3747 ? 202.887 160.689 258.550 1.00 74.15  ? 3747 LYS A N     1 
ATOM   15973 C  CA    . LYS A 1 3747 ? 202.275 161.581 259.531 1.00 72.23  ? 3747 LYS A CA    1 
ATOM   15974 C  C     . LYS A 1 3747 ? 201.136 160.892 260.269 1.00 75.01  ? 3747 LYS A C     1 
ATOM   15975 O  O     . LYS A 1 3747 ? 201.010 161.021 261.492 1.00 79.20  ? 3747 LYS A O     1 
ATOM   15976 C  CB    . LYS A 1 3747 ? 201.777 162.854 258.847 1.00 71.69  ? 3747 LYS A CB    1 
ATOM   15977 C  CG    . LYS A 1 3747 ? 202.824 163.948 258.727 1.00 72.26  ? 3747 LYS A CG    1 
ATOM   15978 C  CD    . LYS A 1 3747 ? 202.191 165.327 258.817 1.00 74.30  ? 3747 LYS A CD    1 
ATOM   15979 C  CE    . LYS A 1 3747 ? 201.791 165.840 257.444 1.00 75.88  ? 3747 LYS A CE    1 
ATOM   15980 N  NZ    . LYS A 1 3747 ? 201.939 167.318 257.338 1.00 73.28  ? 3747 LYS A NZ    1 
ATOM   15981 N  N     . SER A 1 3748 ? 200.294 160.153 259.543 1.00 75.84  ? 3748 SER A N     1 
ATOM   15982 C  CA    . SER A 1 3748 ? 199.165 159.472 260.162 1.00 74.95  ? 3748 SER A CA    1 
ATOM   15983 C  C     . SER A 1 3748 ? 199.628 158.385 261.124 1.00 78.03  ? 3748 SER A C     1 
ATOM   15984 O  O     . SER A 1 3748 ? 199.055 158.226 262.207 1.00 81.28  ? 3748 SER A O     1 
ATOM   15985 C  CB    . SER A 1 3748 ? 198.256 158.884 259.083 1.00 72.78  ? 3748 SER A CB    1 
ATOM   15986 O  OG    . SER A 1 3748 ? 198.837 157.731 258.501 1.00 73.56  ? 3748 SER A OG    1 
ATOM   15987 N  N     . LEU A 1 3749 ? 200.656 157.622 260.743 1.00 73.13  ? 3749 LEU A N     1 
ATOM   15988 C  CA    . LEU A 1 3749 ? 201.163 156.582 261.631 1.00 71.98  ? 3749 LEU A CA    1 
ATOM   15989 C  C     . LEU A 1 3749 ? 201.764 157.187 262.893 1.00 76.45  ? 3749 LEU A C     1 
ATOM   15990 O  O     . LEU A 1 3749 ? 201.534 156.687 264.002 1.00 84.50  ? 3749 LEU A O     1 
ATOM   15991 C  CB    . LEU A 1 3749 ? 202.183 155.719 260.886 1.00 82.33  ? 3749 LEU A CB    1 
ATOM   15992 C  CG    . LEU A 1 3749 ? 202.725 154.438 261.528 1.00 88.55  ? 3749 LEU A CG    1 
ATOM   15993 C  CD1   . LEU A 1 3749 ? 203.121 153.454 260.441 1.00 79.70  ? 3749 LEU A CD1   1 
ATOM   15994 C  CD2   . LEU A 1 3749 ? 203.915 154.718 262.431 1.00 85.79  ? 3749 LEU A CD2   1 
ATOM   15995 N  N     . LEU A 1 3750 ? 202.528 158.274 262.745 1.00 81.80  ? 3750 LEU A N     1 
ATOM   15996 C  CA    . LEU A 1 3750 ? 203.089 158.938 263.919 1.00 80.65  ? 3750 LEU A CA    1 
ATOM   15997 C  C     . LEU A 1 3750 ? 201.990 159.493 264.818 1.00 79.25  ? 3750 LEU A C     1 
ATOM   15998 O  O     . LEU A 1 3750 ? 202.068 159.382 266.046 1.00 78.75  ? 3750 LEU A O     1 
ATOM   15999 C  CB    . LEU A 1 3750 ? 204.047 160.048 263.488 1.00 79.17  ? 3750 LEU A CB    1 
ATOM   16000 C  CG    . LEU A 1 3750 ? 205.127 160.437 264.501 1.00 79.32  ? 3750 LEU A CG    1 
ATOM   16001 C  CD1   . LEU A 1 3750 ? 205.719 159.205 265.166 1.00 78.33  ? 3750 LEU A CD1   1 
ATOM   16002 C  CD2   . LEU A 1 3750 ? 206.214 161.260 263.833 1.00 70.37  ? 3750 LEU A CD2   1 
ATOM   16003 N  N     . GLN A 1 3751 ? 200.949 160.082 264.223 1.00 75.02  ? 3751 GLN A N     1 
ATOM   16004 C  CA    . GLN A 1 3751 ? 199.840 160.607 265.015 1.00 77.93  ? 3751 GLN A CA    1 
ATOM   16005 C  C     . GLN A 1 3751 ? 199.102 159.492 265.747 1.00 85.36  ? 3751 GLN A C     1 
ATOM   16006 O  O     . GLN A 1 3751 ? 198.725 159.648 266.915 1.00 92.20  ? 3751 GLN A O     1 
ATOM   16007 C  CB    . GLN A 1 3751 ? 198.884 161.388 264.113 1.00 77.27  ? 3751 GLN A CB    1 
ATOM   16008 C  CG    . GLN A 1 3751 ? 197.511 161.633 264.711 1.00 83.44  ? 3751 GLN A CG    1 
ATOM   16009 C  CD    . GLN A 1 3751 ? 196.504 162.102 263.680 1.00 88.39  ? 3751 GLN A CD    1 
ATOM   16010 O  OE1   . GLN A 1 3751 ? 195.698 161.317 263.182 1.00 95.00  ? 3751 GLN A OE1   1 
ATOM   16011 N  NE2   . GLN A 1 3751 ? 196.548 163.387 263.352 1.00 83.18  ? 3751 GLN A NE2   1 
ATOM   16012 N  N     . ALA A 1 3752 ? 198.884 158.359 265.075 1.00 83.34  ? 3752 ALA A N     1 
ATOM   16013 C  CA    . ALA A 1 3752 ? 198.215 157.232 265.716 1.00 82.69  ? 3752 ALA A CA    1 
ATOM   16014 C  C     . ALA A 1 3752 ? 199.035 156.694 266.880 1.00 85.75  ? 3752 ALA A C     1 
ATOM   16015 O  O     . ALA A 1 3752 ? 198.487 156.385 267.944 1.00 87.53  ? 3752 ALA A O     1 
ATOM   16016 C  CB    . ALA A 1 3752 ? 197.942 156.130 264.694 1.00 80.91  ? 3752 ALA A CB    1 
ATOM   16017 N  N     . LEU A 1 3753 ? 200.354 156.573 266.698 1.00 81.58  ? 3753 LEU A N     1 
ATOM   16018 C  CA    . LEU A 1 3753 ? 201.200 156.159 267.813 1.00 85.55  ? 3753 LEU A CA    1 
ATOM   16019 C  C     . LEU A 1 3753 ? 201.214 157.201 268.925 1.00 91.15  ? 3753 LEU A C     1 
ATOM   16020 O  O     . LEU A 1 3753 ? 201.417 156.855 270.093 1.00 96.73  ? 3753 LEU A O     1 
ATOM   16021 C  CB    . LEU A 1 3753 ? 202.621 155.876 267.330 1.00 83.70  ? 3753 LEU A CB    1 
ATOM   16022 C  CG    . LEU A 1 3753 ? 202.804 154.538 266.616 1.00 85.73  ? 3753 LEU A CG    1 
ATOM   16023 C  CD1   . LEU A 1 3753 ? 204.228 154.387 266.122 1.00 93.26  ? 3753 LEU A CD1   1 
ATOM   16024 C  CD2   . LEU A 1 3753 ? 202.436 153.396 267.543 1.00 91.14  ? 3753 LEU A CD2   1 
ATOM   16025 N  N     . ASN A 1 3754 ? 201.018 158.473 268.581 1.00 92.00  ? 3754 ASN A N     1 
ATOM   16026 C  CA    . ASN A 1 3754 ? 200.917 159.507 269.603 1.00 90.08  ? 3754 ASN A CA    1 
ATOM   16027 C  C     . ASN A 1 3754 ? 199.634 159.374 270.413 1.00 90.34  ? 3754 ASN A C     1 
ATOM   16028 O  O     . ASN A 1 3754 ? 199.648 159.579 271.632 1.00 90.22  ? 3754 ASN A O     1 
ATOM   16029 C  CB    . ASN A 1 3754 ? 200.984 160.892 268.959 1.00 89.16  ? 3754 ASN A CB    1 
ATOM   16030 C  CG    . ASN A 1 3754 ? 202.398 161.426 268.872 1.00 87.76  ? 3754 ASN A CG    1 
ATOM   16031 O  OD1   . ASN A 1 3754 ? 203.350 160.669 268.679 1.00 87.62  ? 3754 ASN A OD1   1 
ATOM   16032 N  ND2   . ASN A 1 3754 ? 202.543 162.738 269.016 1.00 79.84  ? 3754 ASN A ND2   1 
ATOM   16033 N  N     . GLU A 1 3755 ? 198.524 159.033 269.760 1.00 93.40  ? 3755 GLU A N     1 
ATOM   16034 C  CA    . GLU A 1 3755 ? 197.215 159.032 270.399 1.00 91.71  ? 3755 GLU A CA    1 
ATOM   16035 C  C     . GLU A 1 3755 ? 196.867 157.718 271.091 1.00 92.74  ? 3755 GLU A C     1 
ATOM   16036 O  O     . GLU A 1 3755 ? 195.817 157.643 271.739 1.00 85.36  ? 3755 GLU A O     1 
ATOM   16037 C  CB    . GLU A 1 3755 ? 196.128 159.360 269.369 1.00 89.18  ? 3755 GLU A CB    1 
ATOM   16038 C  CG    . GLU A 1 3755 ? 196.196 160.777 268.826 1.00 95.96  ? 3755 GLU A CG    1 
ATOM   16039 C  CD    . GLU A 1 3755 ? 196.525 161.799 269.897 1.00 100.60 ? 3755 GLU A CD    1 
ATOM   16040 O  OE1   . GLU A 1 3755 ? 195.689 162.002 270.803 1.00 99.59  ? 3755 GLU A OE1   1 
ATOM   16041 O  OE2   . GLU A 1 3755 ? 197.620 162.396 269.835 1.00 99.46  ? 3755 GLU A OE2   1 
ATOM   16042 N  N     . VAL A 1 3756 ? 197.705 156.686 270.973 1.00 96.69  ? 3756 VAL A N     1 
ATOM   16043 C  CA    . VAL A 1 3756 ? 197.400 155.422 271.638 1.00 98.47  ? 3756 VAL A CA    1 
ATOM   16044 C  C     . VAL A 1 3756 ? 197.602 155.571 273.145 1.00 102.49 ? 3756 VAL A C     1 
ATOM   16045 O  O     . VAL A 1 3756 ? 198.383 156.402 273.623 1.00 104.57 ? 3756 VAL A O     1 
ATOM   16046 C  CB    . VAL A 1 3756 ? 198.252 154.278 271.059 1.00 105.08 ? 3756 VAL A CB    1 
ATOM   16047 C  CG1   . VAL A 1 3756 ? 199.722 154.487 271.371 1.00 103.65 ? 3756 VAL A CG1   1 
ATOM   16048 C  CG2   . VAL A 1 3756 ? 197.770 152.915 271.552 1.00 104.50 ? 3756 VAL A CG2   1 
ATOM   16049 N  N     . LYS A 1 3757 ? 196.877 154.749 273.906 1.00 104.48 ? 3757 LYS A N     1 
ATOM   16050 C  CA    . LYS A 1 3757 ? 196.825 154.854 275.359 1.00 102.22 ? 3757 LYS A CA    1 
ATOM   16051 C  C     . LYS A 1 3757 ? 197.903 154.022 276.047 1.00 105.16 ? 3757 LYS A C     1 
ATOM   16052 O  O     . LYS A 1 3757 ? 197.721 153.594 277.191 1.00 102.71 ? 3757 LYS A O     1 
ATOM   16053 C  CB    . LYS A 1 3757 ? 195.440 154.452 275.865 1.00 98.23  ? 3757 LYS A CB    1 
ATOM   16054 C  CG    . LYS A 1 3757 ? 194.288 155.043 275.065 1.00 95.01  ? 3757 LYS A CG    1 
ATOM   16055 C  CD    . LYS A 1 3757 ? 194.370 156.561 275.004 1.00 92.38  ? 3757 LYS A CD    1 
ATOM   16056 C  CE    . LYS A 1 3757 ? 194.142 157.184 276.373 1.00 90.80  ? 3757 LYS A CE    1 
ATOM   16057 N  NZ    . LYS A 1 3757 ? 194.214 158.670 276.325 1.00 82.86  ? 3757 LYS A NZ    1 
ATOM   16058 N  N     . GLY A 1 3758 ? 199.025 153.783 275.371 1.00 109.02 ? 3758 GLY A N     1 
ATOM   16059 C  CA    . GLY A 1 3758 ? 200.151 153.099 275.971 1.00 107.42 ? 3758 GLY A CA    1 
ATOM   16060 C  C     . GLY A 1 3758 ? 200.140 151.592 275.864 1.00 111.04 ? 3758 GLY A C     1 
ATOM   16061 O  O     . GLY A 1 3758 ? 201.093 150.952 276.328 1.00 109.84 ? 3758 GLY A O     1 
ATOM   16062 N  N     . ARG A 1 3759 ? 199.106 150.996 275.267 1.00 114.97 ? 3759 ARG A N     1 
ATOM   16063 C  CA    . ARG A 1 3759 ? 199.014 149.539 275.125 1.00 116.04 ? 3759 ARG A CA    1 
ATOM   16064 C  C     . ARG A 1 3759 ? 198.418 149.240 273.750 1.00 118.30 ? 3759 ARG A C     1 
ATOM   16065 O  O     . ARG A 1 3759 ? 197.195 149.218 273.581 1.00 115.89 ? 3759 ARG A O     1 
ATOM   16066 C  CB    . ARG A 1 3759 ? 198.186 148.928 276.248 1.00 115.31 ? 3759 ARG A CB    1 
ATOM   16067 C  CG    . ARG A 1 3759 ? 198.935 148.782 277.563 1.00 111.26 ? 3759 ARG A CG    1 
ATOM   16068 C  CD    . ARG A 1 3759 ? 200.077 147.787 277.441 1.00 115.36 ? 3759 ARG A CD    1 
ATOM   16069 N  NE    . ARG A 1 3759 ? 199.704 146.622 276.649 1.00 120.83 ? 3759 ARG A NE    1 
ATOM   16070 C  CZ    . ARG A 1 3759 ? 199.484 145.414 277.149 1.00 120.52 ? 3759 ARG A CZ    1 
ATOM   16071 N  NH1   . ARG A 1 3759 ? 199.588 145.174 278.445 1.00 118.09 ? 3759 ARG A NH1   1 
ATOM   16072 N  NH2   . ARG A 1 3759 ? 199.149 144.423 276.328 1.00 116.76 ? 3759 ARG A NH2   1 
ATOM   16073 N  N     . ILE A 1 3760 ? 199.294 149.007 272.771 1.00 116.13 ? 3760 ILE A N     1 
ATOM   16074 C  CA    . ILE A 1 3760 ? 198.839 148.725 271.413 1.00 114.85 ? 3760 ILE A CA    1 
ATOM   16075 C  C     . ILE A 1 3760 ? 198.156 147.364 271.345 1.00 117.07 ? 3760 ILE A C     1 
ATOM   16076 O  O     . ILE A 1 3760 ? 197.147 147.198 270.650 1.00 120.29 ? 3760 ILE A O     1 
ATOM   16077 C  CB    . ILE A 1 3760 ? 200.018 148.823 270.427 1.00 113.07 ? 3760 ILE A CB    1 
ATOM   16078 C  CG1   . ILE A 1 3760 ? 200.626 150.224 270.462 1.00 110.78 ? 3760 ILE A CG1   1 
ATOM   16079 C  CG2   . ILE A 1 3760 ? 199.571 148.477 269.016 1.00 112.74 ? 3760 ILE A CG2   1 
ATOM   16080 C  CD1   . ILE A 1 3760 ? 201.818 150.391 269.547 1.00 106.98 ? 3760 ILE A CD1   1 
ATOM   16081 N  N     . LEU A 1 3761 ? 198.689 146.372 272.063 1.00 113.68 ? 3761 LEU A N     1 
ATOM   16082 C  CA    . LEU A 1 3761 ? 198.100 145.036 272.032 1.00 114.24 ? 3761 LEU A CA    1 
ATOM   16083 C  C     . LEU A 1 3761 ? 196.683 145.029 272.591 1.00 119.74 ? 3761 LEU A C     1 
ATOM   16084 O  O     . LEU A 1 3761 ? 195.843 144.244 272.135 1.00 118.12 ? 3761 LEU A O     1 
ATOM   16085 C  CB    . LEU A 1 3761 ? 198.971 144.048 272.812 1.00 116.20 ? 3761 LEU A CB    1 
ATOM   16086 C  CG    . LEU A 1 3761 ? 200.247 143.500 272.167 1.00 116.68 ? 3761 LEU A CG    1 
ATOM   16087 C  CD1   . LEU A 1 3761 ? 201.334 144.555 272.084 1.00 110.44 ? 3761 LEU A CD1   1 
ATOM   16088 C  CD2   . LEU A 1 3761 ? 200.744 142.279 272.926 1.00 114.74 ? 3761 LEU A CD2   1 
ATOM   16089 N  N     . ASP A 1 3762 ? 196.401 145.882 273.577 1.00 121.57 ? 3762 ASP A N     1 
ATOM   16090 C  CA    . ASP A 1 3762 ? 195.079 145.889 274.196 1.00 121.22 ? 3762 ASP A CA    1 
ATOM   16091 C  C     . ASP A 1 3762 ? 193.997 146.308 273.207 1.00 118.72 ? 3762 ASP A C     1 
ATOM   16092 O  O     . ASP A 1 3762 ? 192.904 145.729 273.190 1.00 116.39 ? 3762 ASP A O     1 
ATOM   16093 C  CB    . ASP A 1 3762 ? 195.076 146.810 275.416 1.00 120.18 ? 3762 ASP A CB    1 
ATOM   16094 C  CG    . ASP A 1 3762 ? 195.908 146.264 276.559 1.00 119.22 ? 3762 ASP A CG    1 
ATOM   16095 O  OD1   . ASP A 1 3762 ? 196.484 145.167 276.405 1.00 120.37 ? 3762 ASP A OD1   1 
ATOM   16096 O  OD2   . ASP A 1 3762 ? 195.987 146.932 277.612 1.00 114.34 ? 3762 ASP A OD2   1 
ATOM   16097 N  N     . ASP A 1 3763 ? 194.278 147.310 272.377 1.00 117.72 ? 3763 ASP A N     1 
ATOM   16098 C  CA    . ASP A 1 3763 ? 193.297 147.854 271.442 1.00 119.06 ? 3763 ASP A CA    1 
ATOM   16099 C  C     . ASP A 1 3763 ? 193.570 147.290 270.052 1.00 120.02 ? 3763 ASP A C     1 
ATOM   16100 O  O     . ASP A 1 3763 ? 194.629 147.543 269.468 1.00 118.78 ? 3763 ASP A O     1 
ATOM   16101 C  CB    . ASP A 1 3763 ? 193.345 149.380 271.436 1.00 120.33 ? 3763 ASP A CB    1 
ATOM   16102 C  CG    . ASP A 1 3763 ? 192.037 150.001 270.984 1.00 116.79 ? 3763 ASP A CG    1 
ATOM   16103 O  OD1   . ASP A 1 3763 ? 191.038 149.889 271.724 1.00 108.83 ? 3763 ASP A OD1   1 
ATOM   16104 O  OD2   . ASP A 1 3763 ? 192.009 150.602 269.890 1.00 115.18 ? 3763 ASP A OD2   1 
ATOM   16105 N  N     . ASP A 1 3764 ? 192.610 146.531 269.522 1.00 119.78 ? 3764 ASP A N     1 
ATOM   16106 C  CA    . ASP A 1 3764 ? 192.754 145.946 268.196 1.00 117.41 ? 3764 ASP A CA    1 
ATOM   16107 C  C     . ASP A 1 3764 ? 192.561 146.960 267.076 1.00 116.02 ? 3764 ASP A C     1 
ATOM   16108 O  O     . ASP A 1 3764 ? 193.103 146.765 265.982 1.00 114.19 ? 3764 ASP A O     1 
ATOM   16109 C  CB    . ASP A 1 3764 ? 191.766 144.790 268.022 1.00 115.23 ? 3764 ASP A CB    1 
ATOM   16110 C  CG    . ASP A 1 3764 ? 192.069 143.623 268.941 1.00 111.77 ? 3764 ASP A CG    1 
ATOM   16111 O  OD1   . ASP A 1 3764 ? 193.025 143.726 269.738 1.00 113.25 ? 3764 ASP A OD1   1 
ATOM   16112 O  OD2   . ASP A 1 3764 ? 191.352 142.603 268.867 1.00 105.27 ? 3764 ASP A OD2   1 
ATOM   16113 N  N     . THR A 1 3765 ? 191.794 148.028 267.318 1.00 114.99 ? 3765 THR A N     1 
ATOM   16114 C  CA    . THR A 1 3765 ? 191.593 149.045 266.289 1.00 117.40 ? 3765 THR A CA    1 
ATOM   16115 C  C     . THR A 1 3765 ? 192.901 149.748 265.944 1.00 117.13 ? 3765 THR A C     1 
ATOM   16116 O  O     . THR A 1 3765 ? 193.188 149.999 264.766 1.00 115.20 ? 3765 THR A O     1 
ATOM   16117 C  CB    . THR A 1 3765 ? 190.544 150.058 266.748 1.00 116.46 ? 3765 THR A CB    1 
ATOM   16118 O  OG1   . THR A 1 3765 ? 189.356 149.368 267.158 1.00 109.60 ? 3765 THR A OG1   1 
ATOM   16119 C  CG2   . THR A 1 3765 ? 190.201 151.018 265.619 1.00 105.73 ? 3765 THR A CG2   1 
ATOM   16120 N  N     . ILE A 1 3766 ? 193.705 150.073 266.960 1.00 115.65 ? 3766 ILE A N     1 
ATOM   16121 C  CA    . ILE A 1 3766 ? 195.002 150.698 266.716 1.00 115.14 ? 3766 ILE A CA    1 
ATOM   16122 C  C     . ILE A 1 3766 ? 195.902 149.756 265.927 1.00 113.52 ? 3766 ILE A C     1 
ATOM   16123 O  O     . ILE A 1 3766 ? 196.620 150.179 265.012 1.00 112.34 ? 3766 ILE A O     1 
ATOM   16124 C  CB    . ILE A 1 3766 ? 195.647 151.120 268.050 1.00 114.53 ? 3766 ILE A CB    1 
ATOM   16125 C  CG1   . ILE A 1 3766 ? 194.798 152.193 268.735 1.00 108.68 ? 3766 ILE A CG1   1 
ATOM   16126 C  CG2   . ILE A 1 3766 ? 197.063 151.625 267.829 1.00 110.40 ? 3766 ILE A CG2   1 
ATOM   16127 C  CD1   . ILE A 1 3766 ? 194.638 153.457 267.920 1.00 99.39  ? 3766 ILE A CD1   1 
ATOM   16128 N  N     . ILE A 1 3767 ? 195.873 148.465 266.264 1.00 112.99 ? 3767 ILE A N     1 
ATOM   16129 C  CA    . ILE A 1 3767 ? 196.670 147.477 265.542 1.00 111.68 ? 3767 ILE A CA    1 
ATOM   16130 C  C     . ILE A 1 3767 ? 196.253 147.423 264.078 1.00 109.71 ? 3767 ILE A C     1 
ATOM   16131 O  O     . ILE A 1 3767 ? 197.098 147.393 263.172 1.00 107.11 ? 3767 ILE A O     1 
ATOM   16132 C  CB    . ILE A 1 3767 ? 196.541 146.096 266.209 1.00 108.65 ? 3767 ILE A CB    1 
ATOM   16133 C  CG1   . ILE A 1 3767 ? 197.160 146.112 267.607 1.00 110.50 ? 3767 ILE A CG1   1 
ATOM   16134 C  CG2   . ILE A 1 3767 ? 197.178 145.025 265.343 1.00 103.86 ? 3767 ILE A CG2   1 
ATOM   16135 C  CD1   . ILE A 1 3767 ? 197.100 144.778 268.316 1.00 107.34 ? 3767 ILE A CD1   1 
ATOM   16136 N  N     . THR A 1 3768 ? 194.942 147.395 263.826 1.00 108.91 ? 3768 THR A N     1 
ATOM   16137 C  CA    . THR A 1 3768 ? 194.457 147.333 262.451 1.00 108.40 ? 3768 THR A CA    1 
ATOM   16138 C  C     . THR A 1 3768 ? 194.853 148.580 261.672 1.00 106.04 ? 3768 THR A C     1 
ATOM   16139 O  O     . THR A 1 3768 ? 195.278 148.487 260.515 1.00 103.36 ? 3768 THR A O     1 
ATOM   16140 C  CB    . THR A 1 3768 ? 192.940 147.146 262.427 1.00 108.54 ? 3768 THR A CB    1 
ATOM   16141 O  OG1   . THR A 1 3768 ? 192.325 148.095 263.305 1.00 113.50 ? 3768 THR A OG1   1 
ATOM   16142 C  CG2   . THR A 1 3768 ? 192.569 145.737 262.866 1.00 102.43 ? 3768 THR A CG2   1 
ATOM   16143 N  N     . THR A 1 3769 ? 194.725 149.756 262.291 1.00 106.57 ? 3769 THR A N     1 
ATOM   16144 C  CA    . THR A 1 3769 ? 195.126 150.983 261.610 1.00 102.94 ? 3769 THR A CA    1 
ATOM   16145 C  C     . THR A 1 3769 ? 196.616 150.973 261.294 1.00 101.29 ? 3769 THR A C     1 
ATOM   16146 O  O     . THR A 1 3769 ? 197.025 151.345 260.188 1.00 99.20  ? 3769 THR A O     1 
ATOM   16147 C  CB    . THR A 1 3769 ? 194.769 152.203 262.457 1.00 100.73 ? 3769 THR A CB    1 
ATOM   16148 O  OG1   . THR A 1 3769 ? 195.306 152.048 263.777 1.00 106.45 ? 3769 THR A OG1   1 
ATOM   16149 C  CG2   . THR A 1 3769 ? 193.259 152.370 262.541 1.00 92.61  ? 3769 THR A CG2   1 
ATOM   16150 N  N     . LEU A 1 3770 ? 197.443 150.530 262.246 1.00 99.53  ? 3770 LEU A N     1 
ATOM   16151 C  CA    . LEU A 1 3770 ? 198.884 150.497 262.020 1.00 98.26  ? 3770 LEU A CA    1 
ATOM   16152 C  C     . LEU A 1 3770 ? 199.244 149.547 260.883 1.00 100.63 ? 3770 LEU A C     1 
ATOM   16153 O  O     . LEU A 1 3770 ? 200.050 149.886 260.007 1.00 102.31 ? 3770 LEU A O     1 
ATOM   16154 C  CB    . LEU A 1 3770 ? 199.608 150.093 263.305 1.00 97.77  ? 3770 LEU A CB    1 
ATOM   16155 C  CG    . LEU A 1 3770 ? 199.755 151.159 264.391 1.00 100.49 ? 3770 LEU A CG    1 
ATOM   16156 C  CD1   . LEU A 1 3770 ? 200.806 150.743 265.408 1.00 91.28  ? 3770 LEU A CD1   1 
ATOM   16157 C  CD2   . LEU A 1 3770 ? 200.096 152.511 263.783 1.00 98.27  ? 3770 LEU A CD2   1 
ATOM   16158 N  N     . GLU A 1 3771 ? 198.650 148.351 260.876 1.00 101.49 ? 3771 GLU A N     1 
ATOM   16159 C  CA    . GLU A 1 3771 ? 198.991 147.382 259.837 1.00 93.87  ? 3771 GLU A CA    1 
ATOM   16160 C  C     . GLU A 1 3771 ? 198.479 147.831 258.472 1.00 94.09  ? 3771 GLU A C     1 
ATOM   16161 O  O     . GLU A 1 3771 ? 199.153 147.626 257.456 1.00 93.63  ? 3771 GLU A O     1 
ATOM   16162 C  CB    . GLU A 1 3771 ? 198.458 145.994 260.203 1.00 101.20 ? 3771 GLU A CB    1 
ATOM   16163 C  CG    . GLU A 1 3771 ? 196.947 145.867 260.253 1.00 104.92 ? 3771 GLU A CG    1 
ATOM   16164 C  CD    . GLU A 1 3771 ? 196.493 144.487 260.683 1.00 105.15 ? 3771 GLU A CD    1 
ATOM   16165 O  OE1   . GLU A 1 3771 ? 197.362 143.636 260.967 1.00 104.53 ? 3771 GLU A OE1   1 
ATOM   16166 O  OE2   . GLU A 1 3771 ? 195.268 144.254 260.742 1.00 105.26 ? 3771 GLU A OE2   1 
ATOM   16167 N  N     . ASN A 1 3772 ? 197.299 148.460 258.425 1.00 96.76  ? 3772 ASN A N     1 
ATOM   16168 C  CA    . ASN A 1 3772 ? 196.799 148.994 257.163 1.00 95.24  ? 3772 ASN A CA    1 
ATOM   16169 C  C     . ASN A 1 3772 ? 197.707 150.099 256.636 1.00 94.19  ? 3772 ASN A C     1 
ATOM   16170 O  O     . ASN A 1 3772 ? 198.007 150.149 255.436 1.00 93.74  ? 3772 ASN A O     1 
ATOM   16171 C  CB    . ASN A 1 3772 ? 195.372 149.511 257.338 1.00 88.74  ? 3772 ASN A CB    1 
ATOM   16172 C  CG    . ASN A 1 3772 ? 194.385 148.402 257.643 1.00 93.54  ? 3772 ASN A CG    1 
ATOM   16173 O  OD1   . ASN A 1 3772 ? 194.739 147.224 257.651 1.00 96.15  ? 3772 ASN A OD1   1 
ATOM   16174 N  ND2   . ASN A 1 3772 ? 193.136 148.776 257.899 1.00 89.24  ? 3772 ASN A ND2   1 
ATOM   16175 N  N     . LEU A 1 3773 ? 198.157 150.994 257.521 1.00 91.95  ? 3773 LEU A N     1 
ATOM   16176 C  CA    . LEU A 1 3773 ? 199.062 152.057 257.100 1.00 89.52  ? 3773 LEU A CA    1 
ATOM   16177 C  C     . LEU A 1 3773 ? 200.382 151.488 256.596 1.00 90.86  ? 3773 LEU A C     1 
ATOM   16178 O  O     . LEU A 1 3773 ? 200.928 151.963 255.593 1.00 92.62  ? 3773 LEU A O     1 
ATOM   16179 C  CB    . LEU A 1 3773 ? 199.300 153.032 258.254 1.00 86.71  ? 3773 LEU A CB    1 
ATOM   16180 C  CG    . LEU A 1 3773 ? 198.113 153.899 258.676 1.00 81.60  ? 3773 LEU A CG    1 
ATOM   16181 C  CD1   . LEU A 1 3773 ? 198.471 154.742 259.888 1.00 78.88  ? 3773 LEU A CD1   1 
ATOM   16182 C  CD2   . LEU A 1 3773 ? 197.639 154.774 257.531 1.00 83.12  ? 3773 LEU A CD2   1 
ATOM   16183 N  N     . LYS A 1 3774 ? 200.911 150.468 257.277 1.00 83.47  ? 3774 LYS A N     1 
ATOM   16184 C  CA    . LYS A 1 3774 ? 202.158 149.853 256.831 1.00 88.07  ? 3774 LYS A CA    1 
ATOM   16185 C  C     . LYS A 1 3774 ? 201.993 149.173 255.474 1.00 91.79  ? 3774 LYS A C     1 
ATOM   16186 O  O     . LYS A 1 3774 ? 202.879 149.260 254.615 1.00 90.80  ? 3774 LYS A O     1 
ATOM   16187 C  CB    . LYS A 1 3774 ? 202.656 148.856 257.877 1.00 88.27  ? 3774 LYS A CB    1 
ATOM   16188 C  CG    . LYS A 1 3774 ? 203.688 149.430 258.830 1.00 87.42  ? 3774 LYS A CG    1 
ATOM   16189 C  CD    . LYS A 1 3774 ? 204.987 149.753 258.106 1.00 92.12  ? 3774 LYS A CD    1 
ATOM   16190 C  CE    . LYS A 1 3774 ? 205.508 148.547 257.333 1.00 95.21  ? 3774 LYS A CE    1 
ATOM   16191 N  NZ    . LYS A 1 3774 ? 206.898 148.755 256.843 1.00 99.13  ? 3774 LYS A NZ    1 
ATOM   16192 N  N     . ARG A 1 3775 ? 200.869 148.481 255.268 1.00 86.80  ? 3775 ARG A N     1 
ATOM   16193 C  CA    . ARG A 1 3775 ? 200.621 147.840 253.980 1.00 87.21  ? 3775 ARG A CA    1 
ATOM   16194 C  C     . ARG A 1 3775 ? 200.510 148.871 252.864 1.00 89.69  ? 3775 ARG A C     1 
ATOM   16195 O  O     . ARG A 1 3775 ? 201.061 148.681 251.768 1.00 92.62  ? 3775 ARG A O     1 
ATOM   16196 C  CB    . ARG A 1 3775 ? 199.353 146.991 254.060 1.00 85.72  ? 3775 ARG A CB    1 
ATOM   16197 C  CG    . ARG A 1 3775 ? 199.125 146.087 252.863 1.00 87.06  ? 3775 ARG A CG    1 
ATOM   16198 C  CD    . ARG A 1 3775 ? 197.861 145.265 253.040 1.00 91.82  ? 3775 ARG A CD    1 
ATOM   16199 N  NE    . ARG A 1 3775 ? 197.728 144.762 254.403 1.00 98.12  ? 3775 ARG A NE    1 
ATOM   16200 C  CZ    . ARG A 1 3775 ? 196.647 144.916 255.155 1.00 95.29  ? 3775 ARG A CZ    1 
ATOM   16201 N  NH1   . ARG A 1 3775 ? 195.578 145.553 254.708 1.00 87.04  ? 3775 ARG A NH1   1 
ATOM   16202 N  NH2   . ARG A 1 3775 ? 196.639 144.418 256.389 1.00 92.07  ? 3775 ARG A NH2   1 
ATOM   16203 N  N     . GLU A 1 3776 ? 199.802 149.973 253.126 1.00 86.19  ? 3776 GLU A N     1 
ATOM   16204 C  CA    . GLU A 1 3776 ? 199.702 151.037 252.134 1.00 86.96  ? 3776 GLU A CA    1 
ATOM   16205 C  C     . GLU A 1 3776 ? 201.071 151.634 251.833 1.00 89.23  ? 3776 GLU A C     1 
ATOM   16206 O  O     . GLU A 1 3776 ? 201.394 151.911 250.672 1.00 92.07  ? 3776 GLU A O     1 
ATOM   16207 C  CB    . GLU A 1 3776 ? 198.738 152.119 252.620 1.00 82.47  ? 3776 GLU A CB    1 
ATOM   16208 C  CG    . GLU A 1 3776 ? 198.208 153.016 251.515 1.00 88.01  ? 3776 GLU A CG    1 
ATOM   16209 C  CD    . GLU A 1 3776 ? 197.106 153.940 251.992 1.00 94.28  ? 3776 GLU A CD    1 
ATOM   16210 O  OE1   . GLU A 1 3776 ? 196.761 153.887 253.190 1.00 97.81  ? 3776 GLU A OE1   1 
ATOM   16211 O  OE2   . GLU A 1 3776 ? 196.584 154.718 251.168 1.00 92.61  ? 3776 GLU A OE2   1 
ATOM   16212 N  N     . ALA A 1 3777 ? 201.892 151.830 252.868 1.00 86.32  ? 3777 ALA A N     1 
ATOM   16213 C  CA    . ALA A 1 3777 ? 203.234 152.358 252.655 1.00 86.79  ? 3777 ALA A CA    1 
ATOM   16214 C  C     . ALA A 1 3777 ? 204.062 151.422 251.785 1.00 86.44  ? 3777 ALA A C     1 
ATOM   16215 O  O     . ALA A 1 3777 ? 204.766 151.873 250.874 1.00 86.20  ? 3777 ALA A O     1 
ATOM   16216 C  CB    . ALA A 1 3777 ? 203.925 152.593 253.998 1.00 83.48  ? 3777 ALA A CB    1 
ATOM   16217 N  N     . ALA A 1 3778 ? 203.988 150.115 252.047 1.00 88.81  ? 3778 ALA A N     1 
ATOM   16218 C  CA    . ALA A 1 3778 ? 204.755 149.160 251.252 1.00 85.19  ? 3778 ALA A CA    1 
ATOM   16219 C  C     . ALA A 1 3778 ? 204.310 149.163 249.794 1.00 84.52  ? 3778 ALA A C     1 
ATOM   16220 O  O     . ALA A 1 3778 ? 205.146 149.173 248.878 1.00 83.16  ? 3778 ALA A O     1 
ATOM   16221 C  CB    . ALA A 1 3778 ? 204.629 147.759 251.848 1.00 80.22  ? 3778 ALA A CB    1 
ATOM   16222 N  N     . GLU A 1 3779 ? 202.994 149.155 249.556 1.00 86.59  ? 3779 GLU A N     1 
ATOM   16223 C  CA    . GLU A 1 3779 ? 202.514 149.139 248.176 1.00 84.56  ? 3779 GLU A CA    1 
ATOM   16224 C  C     . GLU A 1 3779 ? 202.883 150.428 247.446 1.00 82.11  ? 3779 GLU A C     1 
ATOM   16225 O  O     . GLU A 1 3779 ? 203.281 150.393 246.273 1.00 84.61  ? 3779 GLU A O     1 
ATOM   16226 C  CB    . GLU A 1 3779 ? 201.003 148.883 248.137 1.00 89.01  ? 3779 GLU A CB    1 
ATOM   16227 C  CG    . GLU A 1 3779 ? 200.117 150.062 248.496 1.00 92.91  ? 3779 GLU A CG    1 
ATOM   16228 C  CD    . GLU A 1 3779 ? 198.642 149.717 248.449 1.00 103.70 ? 3779 GLU A CD    1 
ATOM   16229 O  OE1   . GLU A 1 3779 ? 198.313 148.535 248.211 1.00 103.78 ? 3779 GLU A OE1   1 
ATOM   16230 O  OE2   . GLU A 1 3779 ? 197.810 150.627 248.649 1.00 104.74 ? 3779 GLU A OE2   1 
ATOM   16231 N  N     . VAL A 1 3780 ? 202.794 151.572 248.130 1.00 82.80  ? 3780 VAL A N     1 
ATOM   16232 C  CA    . VAL A 1 3780 ? 203.162 152.833 247.497 1.00 77.67  ? 3780 VAL A CA    1 
ATOM   16233 C  C     . VAL A 1 3780 ? 204.661 152.873 247.221 1.00 78.99  ? 3780 VAL A C     1 
ATOM   16234 O  O     . VAL A 1 3780 ? 205.096 153.417 246.203 1.00 82.32  ? 3780 VAL A O     1 
ATOM   16235 C  CB    . VAL A 1 3780 ? 202.700 154.022 248.359 1.00 71.72  ? 3780 VAL A CB    1 
ATOM   16236 C  CG1   . VAL A 1 3780 ? 203.241 155.328 247.806 1.00 69.10  ? 3780 VAL A CG1   1 
ATOM   16237 C  CG2   . VAL A 1 3780 ? 201.184 154.070 248.407 1.00 74.16  ? 3780 VAL A CG2   1 
ATOM   16238 N  N     . THR A 1 3781 ? 205.474 152.294 248.108 1.00 73.01  ? 3781 THR A N     1 
ATOM   16239 C  CA    . THR A 1 3781 ? 206.915 152.252 247.871 1.00 72.53  ? 3781 THR A CA    1 
ATOM   16240 C  C     . THR A 1 3781 ? 207.253 151.396 246.653 1.00 82.55  ? 3781 THR A C     1 
ATOM   16241 O  O     . THR A 1 3781 ? 208.127 151.754 245.853 1.00 84.19  ? 3781 THR A O     1 
ATOM   16242 C  CB    . THR A 1 3781 ? 207.635 151.726 249.112 1.00 75.01  ? 3781 THR A CB    1 
ATOM   16243 O  OG1   . THR A 1 3781 ? 207.166 152.428 250.269 1.00 79.93  ? 3781 THR A OG1   1 
ATOM   16244 C  CG2   . THR A 1 3781 ? 209.136 151.926 248.983 1.00 71.08  ? 3781 THR A CG2   1 
ATOM   16245 N  N     . ARG A 1 3782 ? 206.576 150.253 246.503 1.00 81.56  ? 3782 ARG A N     1 
ATOM   16246 C  CA    . ARG A 1 3782 ? 206.788 149.428 245.315 1.00 79.42  ? 3782 ARG A CA    1 
ATOM   16247 C  C     . ARG A 1 3782 ? 206.380 150.173 244.048 1.00 79.91  ? 3782 ARG A C     1 
ATOM   16248 O  O     . ARG A 1 3782 ? 207.085 150.132 243.026 1.00 82.50  ? 3782 ARG A O     1 
ATOM   16249 C  CB    . ARG A 1 3782 ? 206.012 148.118 245.448 1.00 80.49  ? 3782 ARG A CB    1 
ATOM   16250 C  CG    . ARG A 1 3782 ? 206.025 147.255 244.200 1.00 89.11  ? 3782 ARG A CG    1 
ATOM   16251 C  CD    . ARG A 1 3782 ? 204.869 146.269 244.208 1.00 86.84  ? 3782 ARG A CD    1 
ATOM   16252 N  NE    . ARG A 1 3782 ? 203.639 146.872 243.709 1.00 89.82  ? 3782 ARG A NE    1 
ATOM   16253 C  CZ    . ARG A 1 3782 ? 203.374 147.085 242.427 1.00 94.04  ? 3782 ARG A CZ    1 
ATOM   16254 N  NH1   . ARG A 1 3782 ? 204.230 146.746 241.478 1.00 93.67  ? 3782 ARG A NH1   1 
ATOM   16255 N  NH2   . ARG A 1 3782 ? 202.218 147.650 242.088 1.00 92.70  ? 3782 ARG A NH2   1 
ATOM   16256 N  N     . LYS A 1 3783 ? 205.242 150.868 244.096 1.00 76.03  ? 3783 LYS A N     1 
ATOM   16257 C  CA    . LYS A 1 3783 ? 204.826 151.666 242.948 1.00 79.34  ? 3783 LYS A CA    1 
ATOM   16258 C  C     . LYS A 1 3783 ? 205.837 152.771 242.655 1.00 75.49  ? 3783 LYS A C     1 
ATOM   16259 O  O     . LYS A 1 3783 ? 206.118 153.080 241.492 1.00 76.03  ? 3783 LYS A O     1 
ATOM   16260 C  CB    . LYS A 1 3783 ? 203.433 152.240 243.199 1.00 71.65  ? 3783 LYS A CB    1 
ATOM   16261 C  CG    . LYS A 1 3783 ? 202.334 151.191 243.152 1.00 71.54  ? 3783 LYS A CG    1 
ATOM   16262 C  CD    . LYS A 1 3783 ? 201.168 151.551 244.057 1.00 68.63  ? 3783 LYS A CD    1 
ATOM   16263 C  CE    . LYS A 1 3783 ? 200.220 152.520 243.381 1.00 63.47  ? 3783 LYS A CE    1 
ATOM   16264 N  NZ    . LYS A 1 3783 ? 199.596 151.925 242.167 1.00 65.43  ? 3783 LYS A NZ    1 
ATOM   16265 N  N     . VAL A 1 3784 ? 206.415 153.358 243.704 1.00 74.03  ? 3784 VAL A N     1 
ATOM   16266 C  CA    . VAL A 1 3784 ? 207.413 154.408 243.533 1.00 72.90  ? 3784 VAL A CA    1 
ATOM   16267 C  C     . VAL A 1 3784 ? 208.654 153.861 242.842 1.00 77.90  ? 3784 VAL A C     1 
ATOM   16268 O  O     . VAL A 1 3784 ? 209.212 154.503 241.947 1.00 83.76  ? 3784 VAL A O     1 
ATOM   16269 C  CB    . VAL A 1 3784 ? 207.755 155.047 244.892 1.00 70.68  ? 3784 VAL A CB    1 
ATOM   16270 C  CG1   . VAL A 1 3784 ? 209.106 155.744 244.836 1.00 65.33  ? 3784 VAL A CG1   1 
ATOM   16271 C  CG2   . VAL A 1 3784 ? 206.676 156.027 245.301 1.00 70.90  ? 3784 VAL A CG2   1 
ATOM   16272 N  N     . GLU A 1 3785 ? 209.112 152.674 243.245 1.00 74.56  ? 3785 GLU A N     1 
ATOM   16273 C  CA    . GLU A 1 3785 ? 210.329 152.139 242.635 1.00 80.24  ? 3785 GLU A CA    1 
ATOM   16274 C  C     . GLU A 1 3785 ? 210.096 151.753 241.175 1.00 79.57  ? 3785 GLU A C     1 
ATOM   16275 O  O     . GLU A 1 3785 ? 210.962 151.993 240.319 1.00 81.97  ? 3785 GLU A O     1 
ATOM   16276 C  CB    . GLU A 1 3785 ? 210.874 150.956 243.442 1.00 83.33  ? 3785 GLU A CB    1 
ATOM   16277 C  CG    . GLU A 1 3785 ? 210.013 149.711 243.466 1.00 84.76  ? 3785 GLU A CG    1 
ATOM   16278 C  CD    . GLU A 1 3785 ? 210.595 148.617 244.338 1.00 88.05  ? 3785 GLU A CD    1 
ATOM   16279 O  OE1   . GLU A 1 3785 ? 211.662 148.842 244.946 1.00 92.30  ? 3785 GLU A OE1   1 
ATOM   16280 O  OE2   . GLU A 1 3785 ? 209.983 147.530 244.419 1.00 90.55  ? 3785 GLU A OE2   1 
ATOM   16281 N  N     . GLU A 1 3786 ? 208.931 151.179 240.855 1.00 77.78  ? 3786 GLU A N     1 
ATOM   16282 C  CA    . GLU A 1 3786 ? 208.672 150.868 239.448 1.00 76.96  ? 3786 GLU A CA    1 
ATOM   16283 C  C     . GLU A 1 3786 ? 208.535 152.144 238.616 1.00 78.68  ? 3786 GLU A C     1 
ATOM   16284 O  O     . GLU A 1 3786 ? 209.026 152.211 237.476 1.00 79.86  ? 3786 GLU A O     1 
ATOM   16285 C  CB    . GLU A 1 3786 ? 207.437 149.973 239.311 1.00 75.94  ? 3786 GLU A CB    1 
ATOM   16286 C  CG    . GLU A 1 3786 ? 206.128 150.587 239.758 1.00 76.69  ? 3786 GLU A CG    1 
ATOM   16287 C  CD    . GLU A 1 3786 ? 205.012 149.569 239.863 1.00 83.91  ? 3786 GLU A CD    1 
ATOM   16288 O  OE1   . GLU A 1 3786 ? 205.299 148.359 239.755 1.00 87.35  ? 3786 GLU A OE1   1 
ATOM   16289 O  OE2   . GLU A 1 3786 ? 203.849 149.980 240.054 1.00 86.68  ? 3786 GLU A OE2   1 
ATOM   16290 N  N     . THR A 1 3787 ? 207.899 153.179 239.177 1.00 74.90  ? 3787 THR A N     1 
ATOM   16291 C  CA    . THR A 1 3787 ? 207.815 154.454 238.476 1.00 72.03  ? 3787 THR A CA    1 
ATOM   16292 C  C     . THR A 1 3787 ? 209.193 155.075 238.288 1.00 76.61  ? 3787 THR A C     1 
ATOM   16293 O  O     . THR A 1 3787 ? 209.448 155.719 237.268 1.00 78.82  ? 3787 THR A O     1 
ATOM   16294 C  CB    . THR A 1 3787 ? 206.895 155.410 239.235 1.00 74.02  ? 3787 THR A CB    1 
ATOM   16295 O  OG1   . THR A 1 3787 ? 205.676 154.734 239.565 1.00 79.12  ? 3787 THR A OG1   1 
ATOM   16296 C  CG2   . THR A 1 3787 ? 206.567 156.624 238.380 1.00 73.89  ? 3787 THR A CG2   1 
ATOM   16297 N  N     . ASP A 1 3788 ? 210.092 154.891 239.258 1.00 77.88  ? 3788 ASP A N     1 
ATOM   16298 C  CA    . ASP A 1 3788 ? 211.461 155.377 239.111 1.00 77.21  ? 3788 ASP A CA    1 
ATOM   16299 C  C     . ASP A 1 3788 ? 212.189 154.648 237.990 1.00 71.78  ? 3788 ASP A C     1 
ATOM   16300 O  O     . ASP A 1 3788 ? 212.972 155.256 237.250 1.00 72.42  ? 3788 ASP A O     1 
ATOM   16301 C  CB    . ASP A 1 3788 ? 212.215 155.224 240.430 1.00 78.04  ? 3788 ASP A CB    1 
ATOM   16302 C  CG    . ASP A 1 3788 ? 212.084 156.442 241.322 1.00 87.45  ? 3788 ASP A CG    1 
ATOM   16303 O  OD1   . ASP A 1 3788 ? 211.387 157.399 240.924 1.00 88.72  ? 3788 ASP A OD1   1 
ATOM   16304 O  OD2   . ASP A 1 3788 ? 212.677 156.443 242.422 1.00 92.95  ? 3788 ASP A OD2   1 
ATOM   16305 N  N     . ILE A 1 3789 ? 211.957 153.340 237.861 1.00 69.90  ? 3789 ILE A N     1 
ATOM   16306 C  CA    . ILE A 1 3789 ? 212.545 152.594 236.748 1.00 74.65  ? 3789 ILE A CA    1 
ATOM   16307 C  C     . ILE A 1 3789 ? 212.061 153.159 235.417 1.00 71.27  ? 3789 ILE A C     1 
ATOM   16308 O  O     . ILE A 1 3789 ? 212.850 153.394 234.488 1.00 67.46  ? 3789 ILE A O     1 
ATOM   16309 C  CB    . ILE A 1 3789 ? 212.223 151.095 236.876 1.00 69.55  ? 3789 ILE A CB    1 
ATOM   16310 C  CG1   . ILE A 1 3789 ? 212.893 150.507 238.120 1.00 68.48  ? 3789 ILE A CG1   1 
ATOM   16311 C  CG2   . ILE A 1 3789 ? 212.657 150.346 235.626 1.00 61.24  ? 3789 ILE A CG2   1 
ATOM   16312 C  CD1   . ILE A 1 3789 ? 212.729 149.009 238.251 1.00 66.44  ? 3789 ILE A CD1   1 
ATOM   16313 N  N     . VAL A 1 3790 ? 210.752 153.403 235.310 1.00 70.48  ? 3790 VAL A N     1 
ATOM   16314 C  CA    . VAL A 1 3790 ? 210.215 153.956 234.066 1.00 67.72  ? 3790 VAL A CA    1 
ATOM   16315 C  C     . VAL A 1 3790 ? 210.758 155.365 233.824 1.00 66.68  ? 3790 VAL A C     1 
ATOM   16316 O  O     . VAL A 1 3790 ? 210.994 155.771 232.677 1.00 67.04  ? 3790 VAL A O     1 
ATOM   16317 C  CB    . VAL A 1 3790 ? 208.676 153.928 234.089 1.00 69.07  ? 3790 VAL A CB    1 
ATOM   16318 C  CG1   . VAL A 1 3790 ? 208.112 154.434 232.771 1.00 61.48  ? 3790 VAL A CG1   1 
ATOM   16319 C  CG2   . VAL A 1 3790 ? 208.180 152.519 234.373 1.00 70.29  ? 3790 VAL A CG2   1 
ATOM   16320 N  N     . MET A 1 3791 ? 210.963 156.133 234.897 1.00 66.93  ? 3791 MET A N     1 
ATOM   16321 C  CA    . MET A 1 3791 ? 211.525 157.474 234.766 1.00 63.18  ? 3791 MET A CA    1 
ATOM   16322 C  C     . MET A 1 3791 ? 212.951 157.429 234.239 1.00 67.11  ? 3791 MET A C     1 
ATOM   16323 O  O     . MET A 1 3791 ? 213.338 158.260 233.410 1.00 67.12  ? 3791 MET A O     1 
ATOM   16324 C  CB    . MET A 1 3791 ? 211.475 158.193 236.113 1.00 72.05  ? 3791 MET A CB    1 
ATOM   16325 C  CG    . MET A 1 3791 ? 212.242 159.502 236.144 1.00 78.31  ? 3791 MET A CG    1 
ATOM   16326 S  SD    . MET A 1 3791 ? 211.444 160.759 235.130 1.00 84.08  ? 3791 MET A SD    1 
ATOM   16327 C  CE    . MET A 1 3791 ? 209.770 160.653 235.752 1.00 68.10  ? 3791 MET A CE    1 
ATOM   16328 N  N     . GLN A 1 3792 ? 213.753 156.478 234.721 1.00 71.30  ? 3792 GLN A N     1 
ATOM   16329 C  CA    . GLN A 1 3792 ? 215.090 156.295 234.166 1.00 66.19  ? 3792 GLN A CA    1 
ATOM   16330 C  C     . GLN A 1 3792 ? 215.024 155.911 232.694 1.00 62.66  ? 3792 GLN A C     1 
ATOM   16331 O  O     . GLN A 1 3792 ? 215.843 156.377 231.889 1.00 61.49  ? 3792 GLN A O     1 
ATOM   16332 C  CB    . GLN A 1 3792 ? 215.854 155.236 234.958 1.00 66.84  ? 3792 GLN A CB    1 
ATOM   16333 C  CG    . GLN A 1 3792 ? 216.186 155.641 236.383 1.00 71.39  ? 3792 GLN A CG    1 
ATOM   16334 C  CD    . GLN A 1 3792 ? 216.881 154.533 237.151 1.00 84.38  ? 3792 GLN A CD    1 
ATOM   16335 O  OE1   . GLN A 1 3792 ? 216.727 153.352 236.836 1.00 83.36  ? 3792 GLN A OE1   1 
ATOM   16336 N  NE2   . GLN A 1 3792 ? 217.651 154.909 238.166 1.00 77.59  ? 3792 GLN A NE2   1 
ATOM   16337 N  N     . GLU A 1 3793 ? 214.053 155.071 232.328 1.00 60.34  ? 3793 GLU A N     1 
ATOM   16338 C  CA    . GLU A 1 3793 ? 213.868 154.729 230.921 1.00 65.33  ? 3793 GLU A CA    1 
ATOM   16339 C  C     . GLU A 1 3793 ? 213.598 155.977 230.083 1.00 62.65  ? 3793 GLU A C     1 
ATOM   16340 O  O     . GLU A 1 3793 ? 214.180 156.149 229.007 1.00 62.53  ? 3793 GLU A O     1 
ATOM   16341 C  CB    . GLU A 1 3793 ? 212.729 153.718 230.777 1.00 67.86  ? 3793 GLU A CB    1 
ATOM   16342 C  CG    . GLU A 1 3793 ? 211.993 153.747 229.441 1.00 68.00  ? 3793 GLU A CG    1 
ATOM   16343 C  CD    . GLU A 1 3793 ? 212.903 153.472 228.258 1.00 75.63  ? 3793 GLU A CD    1 
ATOM   16344 O  OE1   . GLU A 1 3793 ? 213.583 152.426 228.259 1.00 78.17  ? 3793 GLU A OE1   1 
ATOM   16345 O  OE2   . GLU A 1 3793 ? 212.930 154.301 227.323 1.00 74.81  ? 3793 GLU A OE2   1 
ATOM   16346 N  N     . VAL A 1 3794 ? 212.729 156.863 230.571 1.00 60.44  ? 3794 VAL A N     1 
ATOM   16347 C  CA    . VAL A 1 3794 ? 212.416 158.089 229.834 1.00 54.63  ? 3794 VAL A CA    1 
ATOM   16348 C  C     . VAL A 1 3794 ? 213.634 159.010 229.767 1.00 55.26  ? 3794 VAL A C     1 
ATOM   16349 O  O     . VAL A 1 3794 ? 213.900 159.648 228.737 1.00 53.36  ? 3794 VAL A O     1 
ATOM   16350 C  CB    . VAL A 1 3794 ? 211.204 158.795 230.469 1.00 49.12  ? 3794 VAL A CB    1 
ATOM   16351 C  CG1   . VAL A 1 3794 ? 210.961 160.143 229.810 1.00 51.77  ? 3794 VAL A CG1   1 
ATOM   16352 C  CG2   . VAL A 1 3794 ? 209.967 157.920 230.364 1.00 54.78  ? 3794 VAL A CG2   1 
ATOM   16353 N  N     . GLU A 1 3795 ? 214.385 159.105 230.867 1.00 54.33  ? 3795 GLU A N     1 
ATOM   16354 C  CA    . GLU A 1 3795 ? 215.580 159.942 230.885 1.00 48.91  ? 3795 GLU A CA    1 
ATOM   16355 C  C     . GLU A 1 3795 ? 216.617 159.451 229.886 1.00 50.45  ? 3795 GLU A C     1 
ATOM   16356 O  O     . GLU A 1 3795 ? 217.370 160.257 229.322 1.00 51.33  ? 3795 GLU A O     1 
ATOM   16357 C  CB    . GLU A 1 3795 ? 216.170 159.977 232.296 1.00 53.65  ? 3795 GLU A CB    1 
ATOM   16358 C  CG    . GLU A 1 3795 ? 217.376 160.885 232.451 1.00 58.47  ? 3795 GLU A CG    1 
ATOM   16359 C  CD    . GLU A 1 3795 ? 217.894 160.924 233.875 1.00 66.55  ? 3795 GLU A CD    1 
ATOM   16360 O  OE1   . GLU A 1 3795 ? 217.321 160.224 234.735 1.00 69.33  ? 3795 GLU A OE1   1 
ATOM   16361 O  OE2   . GLU A 1 3795 ? 218.873 161.655 234.133 1.00 70.89  ? 3795 GLU A OE2   1 
ATOM   16362 N  N     . THR A 1 3796 ? 216.673 158.136 229.656 1.00 55.70  ? 3796 THR A N     1 
ATOM   16363 C  CA    . THR A 1 3796 ? 217.564 157.607 228.627 1.00 55.77  ? 3796 THR A CA    1 
ATOM   16364 C  C     . THR A 1 3796 ? 217.267 158.234 227.269 1.00 46.23  ? 3796 THR A C     1 
ATOM   16365 O  O     . THR A 1 3796 ? 218.187 158.613 226.536 1.00 45.52  ? 3796 THR A O     1 
ATOM   16366 C  CB    . THR A 1 3796 ? 217.440 156.085 228.552 1.00 60.26  ? 3796 THR A CB    1 
ATOM   16367 O  OG1   . THR A 1 3796 ? 217.803 155.510 229.814 1.00 67.00  ? 3796 THR A OG1   1 
ATOM   16368 C  CG2   . THR A 1 3796 ? 218.347 155.525 227.467 1.00 50.30  ? 3796 THR A CG2   1 
ATOM   16369 N  N     . VAL A 1 3797 ? 215.984 158.358 226.921 1.00 48.65  ? 3797 VAL A N     1 
ATOM   16370 C  CA    . VAL A 1 3797 ? 215.609 159.011 225.670 1.00 44.52  ? 3797 VAL A CA    1 
ATOM   16371 C  C     . VAL A 1 3797 ? 215.925 160.502 225.724 1.00 44.40  ? 3797 VAL A C     1 
ATOM   16372 O  O     . VAL A 1 3797 ? 216.423 161.081 224.752 1.00 43.50  ? 3797 VAL A O     1 
ATOM   16373 C  CB    . VAL A 1 3797 ? 214.122 158.753 225.367 1.00 39.61  ? 3797 VAL A CB    1 
ATOM   16374 C  CG1   . VAL A 1 3797 ? 213.631 159.661 224.249 1.00 35.72  ? 3797 VAL A CG1   1 
ATOM   16375 C  CG2   . VAL A 1 3797 ? 213.899 157.292 225.012 1.00 44.42  ? 3797 VAL A CG2   1 
ATOM   16376 N  N     . SER A 1 3798 ? 215.644 161.146 226.861 1.00 41.55  ? 3798 SER A N     1 
ATOM   16377 C  CA    . SER A 1 3798 ? 215.866 162.588 226.981 1.00 36.24  ? 3798 SER A CA    1 
ATOM   16378 C  C     . SER A 1 3798 ? 217.339 162.977 226.860 1.00 37.63  ? 3798 SER A C     1 
ATOM   16379 O  O     . SER A 1 3798 ? 217.642 164.133 226.520 1.00 33.12  ? 3798 SER A O     1 
ATOM   16380 C  CB    . SER A 1 3798 ? 215.307 163.093 228.311 1.00 36.22  ? 3798 SER A CB    1 
ATOM   16381 O  OG    . SER A 1 3798 ? 214.009 162.579 228.545 1.00 47.09  ? 3798 SER A OG    1 
ATOM   16382 N  N     . GLN A 1 3799 ? 218.252 162.049 227.161 1.00 37.02  ? 3799 GLN A N     1 
ATOM   16383 C  CA    . GLN A 1 3799 ? 219.679 162.344 227.034 1.00 34.93  ? 3799 GLN A CA    1 
ATOM   16384 C  C     . GLN A 1 3799 ? 220.049 162.777 225.620 1.00 36.67  ? 3799 GLN A C     1 
ATOM   16385 O  O     . GLN A 1 3799 ? 220.957 163.596 225.442 1.00 35.09  ? 3799 GLN A O     1 
ATOM   16386 C  CB    . GLN A 1 3799 ? 220.515 161.126 227.435 1.00 41.68  ? 3799 GLN A CB    1 
ATOM   16387 C  CG    . GLN A 1 3799 ? 220.406 160.725 228.896 1.00 44.78  ? 3799 GLN A CG    1 
ATOM   16388 C  CD    . GLN A 1 3799 ? 220.906 161.800 229.837 1.00 54.13  ? 3799 GLN A CD    1 
ATOM   16389 O  OE1   . GLN A 1 3799 ? 220.124 162.435 230.543 1.00 58.89  ? 3799 GLN A OE1   1 
ATOM   16390 N  NE2   . GLN A 1 3799 ? 222.217 162.010 229.852 1.00 48.89  ? 3799 GLN A NE2   1 
ATOM   16391 N  N     . GLN A 1 3800 ? 219.371 162.234 224.605 1.00 32.61  ? 3800 GLN A N     1 
ATOM   16392 C  CA    . GLN A 1 3800 ? 219.706 162.574 223.225 1.00 26.46  ? 3800 GLN A CA    1 
ATOM   16393 C  C     . GLN A 1 3800 ? 219.384 164.031 222.912 1.00 30.74  ? 3800 GLN A C     1 
ATOM   16394 O  O     . GLN A 1 3800 ? 220.140 164.699 222.199 1.00 31.99  ? 3800 GLN A O     1 
ATOM   16395 C  CB    . GLN A 1 3800 ? 218.969 161.644 222.263 1.00 31.00  ? 3800 GLN A CB    1 
ATOM   16396 C  CG    . GLN A 1 3800 ? 219.544 161.630 220.858 1.00 40.68  ? 3800 GLN A CG    1 
ATOM   16397 C  CD    . GLN A 1 3800 ? 218.660 160.896 219.872 1.00 38.14  ? 3800 GLN A CD    1 
ATOM   16398 O  OE1   . GLN A 1 3800 ? 217.554 160.477 220.206 1.00 41.00  ? 3800 GLN A OE1   1 
ATOM   16399 N  NE2   . GLN A 1 3800 ? 219.146 160.734 218.650 1.00 38.83  ? 3800 GLN A NE2   1 
ATOM   16400 N  N     . TYR A 1 3801 ? 218.265 164.537 223.427 1.00 29.46  ? 3801 TYR A N     1 
ATOM   16401 C  CA    . TYR A 1 3801 ? 217.850 165.908 223.166 1.00 22.61  ? 3801 TYR A CA    1 
ATOM   16402 C  C     . TYR A 1 3801 ? 218.419 166.909 224.162 1.00 23.73  ? 3801 TYR A C     1 
ATOM   16403 O  O     . TYR A 1 3801 ? 218.247 168.116 223.962 1.00 22.31  ? 3801 TYR A O     1 
ATOM   16404 C  CB    . TYR A 1 3801 ? 216.321 166.001 223.161 1.00 26.21  ? 3801 TYR A CB    1 
ATOM   16405 C  CG    . TYR A 1 3801 ? 215.664 165.158 222.095 1.00 25.93  ? 3801 TYR A CG    1 
ATOM   16406 C  CD1   . TYR A 1 3801 ? 215.310 163.840 222.344 1.00 28.26  ? 3801 TYR A CD1   1 
ATOM   16407 C  CD2   . TYR A 1 3801 ? 215.396 165.682 220.839 1.00 26.48  ? 3801 TYR A CD2   1 
ATOM   16408 C  CE1   . TYR A 1 3801 ? 214.711 163.066 221.370 1.00 34.18  ? 3801 TYR A CE1   1 
ATOM   16409 C  CE2   . TYR A 1 3801 ? 214.796 164.916 219.858 1.00 27.24  ? 3801 TYR A CE2   1 
ATOM   16410 C  CZ    . TYR A 1 3801 ? 214.456 163.610 220.130 1.00 34.77  ? 3801 TYR A CZ    1 
ATOM   16411 O  OH    . TYR A 1 3801 ? 213.858 162.845 219.156 1.00 39.54  ? 3801 TYR A OH    1 
ATOM   16412 N  N     . LEU A 1 3802 ? 219.068 166.443 225.227 1.00 26.74  ? 3802 LEU A N     1 
ATOM   16413 C  CA    . LEU A 1 3802 ? 219.728 167.356 226.163 1.00 24.34  ? 3802 LEU A CA    1 
ATOM   16414 C  C     . LEU A 1 3802 ? 220.713 168.329 225.511 1.00 19.57  ? 3802 LEU A C     1 
ATOM   16415 O  O     . LEU A 1 3802 ? 220.676 169.526 225.849 1.00 22.17  ? 3802 LEU A O     1 
ATOM   16416 C  CB    . LEU A 1 3802 ? 220.415 166.524 227.256 1.00 28.34  ? 3802 LEU A CB    1 
ATOM   16417 C  CG    . LEU A 1 3802 ? 220.990 167.275 228.456 1.00 30.19  ? 3802 LEU A CG    1 
ATOM   16418 C  CD1   . LEU A 1 3802 ? 219.871 167.868 229.294 1.00 29.28  ? 3802 LEU A CD1   1 
ATOM   16419 C  CD2   . LEU A 1 3802 ? 221.858 166.352 229.292 1.00 28.22  ? 3802 LEU A CD2   1 
ATOM   16420 N  N     . PRO A 1 3803 ? 221.615 167.908 224.610 1.00 21.77  ? 3803 PRO A N     1 
ATOM   16421 C  CA    . PRO A 1 3803 ? 222.554 168.881 224.019 1.00 17.90  ? 3803 PRO A CA    1 
ATOM   16422 C  C     . PRO A 1 3803 ? 221.875 170.008 223.265 1.00 16.41  ? 3803 PRO A C     1 
ATOM   16423 O  O     . PRO A 1 3803 ? 222.387 171.136 223.260 1.00 14.35  ? 3803 PRO A O     1 
ATOM   16424 C  CB    . PRO A 1 3803 ? 223.413 168.019 223.083 1.00 12.28  ? 3803 PRO A CB    1 
ATOM   16425 C  CG    . PRO A 1 3803 ? 223.305 166.650 223.625 1.00 22.63  ? 3803 PRO A CG    1 
ATOM   16426 C  CD    . PRO A 1 3803 ? 221.907 166.540 224.144 1.00 25.02  ? 3803 PRO A CD    1 
ATOM   16427 N  N     . LEU A 1 3804 ? 220.737 169.739 222.622 1.00 17.52  ? 3804 LEU A N     1 
ATOM   16428 C  CA    . LEU A 1 3804 ? 220.003 170.808 221.958 1.00 11.91  ? 3804 LEU A CA    1 
ATOM   16429 C  C     . LEU A 1 3804 ? 219.529 171.848 222.963 1.00 14.36  ? 3804 LEU A C     1 
ATOM   16430 O  O     . LEU A 1 3804 ? 219.603 173.052 222.701 1.00 15.78  ? 3804 LEU A O     1 
ATOM   16431 C  CB    . LEU A 1 3804 ? 218.821 170.234 221.179 1.00 11.36  ? 3804 LEU A CB    1 
ATOM   16432 C  CG    . LEU A 1 3804 ? 217.920 171.261 220.493 1.00 16.77  ? 3804 LEU A CG    1 
ATOM   16433 C  CD1   . LEU A 1 3804 ? 218.725 172.111 219.525 1.00 15.19  ? 3804 LEU A CD1   1 
ATOM   16434 C  CD2   . LEU A 1 3804 ? 216.767 170.581 219.777 1.00 15.69  ? 3804 LEU A CD2   1 
ATOM   16435 N  N     . SER A 1 3805 ? 219.045 171.402 224.125 1.00 14.03  ? 3805 SER A N     1 
ATOM   16436 C  CA    . SER A 1 3805 ? 218.622 172.340 225.161 1.00 12.96  ? 3805 SER A CA    1 
ATOM   16437 C  C     . SER A 1 3805 ? 219.800 173.156 225.682 1.00 13.42  ? 3805 SER A C     1 
ATOM   16438 O  O     . SER A 1 3805 ? 219.668 174.362 225.936 1.00 15.12  ? 3805 SER A O     1 
ATOM   16439 C  CB    . SER A 1 3805 ? 217.942 171.587 226.302 1.00 14.76  ? 3805 SER A CB    1 
ATOM   16440 O  OG    . SER A 1 3805 ? 218.840 170.693 226.935 1.00 21.34  ? 3805 SER A OG    1 
ATOM   16441 N  N     . THR A 1 3806 ? 220.959 172.515 225.856 1.00 12.63  ? 3806 THR A N     1 
ATOM   16442 C  CA    . THR A 1 3806 ? 222.143 173.262 226.280 1.00 14.30  ? 3806 THR A CA    1 
ATOM   16443 C  C     . THR A 1 3806 ? 222.518 174.330 225.257 1.00 12.41  ? 3806 THR A C     1 
ATOM   16444 O  O     . THR A 1 3806 ? 222.816 175.478 225.618 1.00 12.90  ? 3806 THR A O     1 
ATOM   16445 C  CB    . THR A 1 3806 ? 223.311 172.304 226.512 1.00 17.32  ? 3806 THR A CB    1 
ATOM   16446 O  OG1   . THR A 1 3806 ? 222.971 171.376 227.549 1.00 18.93  ? 3806 THR A OG1   1 
ATOM   16447 C  CG2   . THR A 1 3806 ? 224.559 173.073 226.918 1.00 13.49  ? 3806 THR A CG2   1 
ATOM   16448 N  N     . ALA A 1 3807 ? 222.497 173.970 223.971 1.00 13.67  ? 3807 ALA A N     1 
ATOM   16449 C  CA    . ALA A 1 3807 ? 222.799 174.942 222.924 1.00 11.94  ? 3807 ALA A CA    1 
ATOM   16450 C  C     . ALA A 1 3807 ? 221.779 176.072 222.913 1.00 12.54  ? 3807 ALA A C     1 
ATOM   16451 O  O     . ALA A 1 3807 ? 222.134 177.236 222.697 1.00 14.24  ? 3807 ALA A O     1 
ATOM   16452 C  CB    . ALA A 1 3807 ? 222.850 174.248 221.564 1.00 10.72  ? 3807 ALA A CB    1 
ATOM   16453 N  N     . CYS A 1 3808 ? 220.504 175.745 223.131 1.00 11.93  ? 3808 CYS A N     1 
ATOM   16454 C  CA    . CYS A 1 3808 ? 219.466 176.770 223.178 1.00 12.31  ? 3808 CYS A CA    1 
ATOM   16455 C  C     . CYS A 1 3808 ? 219.721 177.758 224.305 1.00 12.83  ? 3808 CYS A C     1 
ATOM   16456 O  O     . CYS A 1 3808 ? 219.594 178.975 224.118 1.00 14.88  ? 3808 CYS A O     1 
ATOM   16457 C  CB    . CYS A 1 3808 ? 218.098 176.114 223.350 1.00 11.35  ? 3808 CYS A CB    1 
ATOM   16458 S  SG    . CYS A 1 3808 ? 217.512 175.214 221.913 1.00 24.69  ? 3808 CYS A SG    1 
ATOM   16459 N  N     . SER A 1 3809 ? 220.069 177.251 225.489 1.00 10.62  ? 3809 SER A N     1 
ATOM   16460 C  CA    . SER A 1 3809 ? 220.376 178.139 226.606 1.00 10.20  ? 3809 SER A CA    1 
ATOM   16461 C  C     . SER A 1 3809 ? 221.570 179.028 226.285 1.00 12.82  ? 3809 SER A C     1 
ATOM   16462 O  O     . SER A 1 3809 ? 221.552 180.235 226.565 1.00 16.34  ? 3809 SER A O     1 
ATOM   16463 C  CB    . SER A 1 3809 ? 220.636 177.323 227.870 1.00 14.60  ? 3809 SER A CB    1 
ATOM   16464 O  OG    . SER A 1 3809 ? 221.990 176.912 227.942 1.00 15.53  ? 3809 SER A OG    1 
ATOM   16465 N  N     . SER A 1 3810 ? 222.613 178.448 225.685 1.00 12.56  ? 3810 SER A N     1 
ATOM   16466 C  CA    . SER A 1 3810 ? 223.786 179.242 225.329 1.00 8.50   ? 3810 SER A CA    1 
ATOM   16467 C  C     . SER A 1 3810 ? 223.426 180.347 224.342 1.00 8.82   ? 3810 SER A C     1 
ATOM   16468 O  O     . SER A 1 3810 ? 223.866 181.494 224.492 1.00 8.62   ? 3810 SER A O     1 
ATOM   16469 C  CB    . SER A 1 3810 ? 224.872 178.337 224.750 1.00 7.99   ? 3810 SER A CB    1 
ATOM   16470 O  OG    . SER A 1 3810 ? 225.119 177.232 225.600 1.00 11.20  ? 3810 SER A OG    1 
ATOM   16471 N  N     . ILE A 1 3811 ? 222.611 180.025 223.337 1.00 11.00  ? 3811 ILE A N     1 
ATOM   16472 C  CA    . ILE A 1 3811 ? 222.246 181.008 222.323 1.00 9.23   ? 3811 ILE A CA    1 
ATOM   16473 C  C     . ILE A 1 3811 ? 221.398 182.120 222.928 1.00 10.24  ? 3811 ILE A C     1 
ATOM   16474 O  O     . ILE A 1 3811 ? 221.592 183.307 222.624 1.00 13.54  ? 3811 ILE A O     1 
ATOM   16475 C  CB    . ILE A 1 3811 ? 221.526 180.315 221.152 1.00 8.43   ? 3811 ILE A CB    1 
ATOM   16476 C  CG1   . ILE A 1 3811 ? 222.477 179.367 220.424 1.00 10.20  ? 3811 ILE A CG1   1 
ATOM   16477 C  CG2   . ILE A 1 3811 ? 221.013 181.335 220.172 1.00 10.41  ? 3811 ILE A CG2   1 
ATOM   16478 C  CD1   . ILE A 1 3811 ? 221.822 178.603 219.300 1.00 11.02  ? 3811 ILE A CD1   1 
ATOM   16479 N  N     . TYR A 1 3812 ? 220.438 181.764 223.788 1.00 10.84  ? 3812 TYR A N     1 
ATOM   16480 C  CA    . TYR A 1 3812 ? 219.615 182.793 224.416 1.00 10.88  ? 3812 TYR A CA    1 
ATOM   16481 C  C     . TYR A 1 3812 ? 220.453 183.714 225.288 1.00 9.82   ? 3812 TYR A C     1 
ATOM   16482 O  O     . TYR A 1 3812 ? 220.254 184.934 225.284 1.00 11.40  ? 3812 TYR A O     1 
ATOM   16483 C  CB    . TYR A 1 3812 ? 218.500 182.176 225.252 1.00 13.52  ? 3812 TYR A CB    1 
ATOM   16484 C  CG    . TYR A 1 3812 ? 217.835 183.206 226.140 1.00 13.86  ? 3812 TYR A CG    1 
ATOM   16485 C  CD1   . TYR A 1 3812 ? 217.031 184.198 225.599 1.00 15.28  ? 3812 TYR A CD1   1 
ATOM   16486 C  CD2   . TYR A 1 3812 ? 218.050 183.216 227.513 1.00 14.08  ? 3812 TYR A CD2   1 
ATOM   16487 C  CE1   . TYR A 1 3812 ? 216.436 185.151 226.400 1.00 15.90  ? 3812 TYR A CE1   1 
ATOM   16488 C  CE2   . TYR A 1 3812 ? 217.459 184.164 228.320 1.00 14.87  ? 3812 TYR A CE2   1 
ATOM   16489 C  CZ    . TYR A 1 3812 ? 216.654 185.129 227.759 1.00 17.18  ? 3812 TYR A CZ    1 
ATOM   16490 O  OH    . TYR A 1 3812 ? 216.064 186.076 228.562 1.00 22.66  ? 3812 TYR A OH    1 
ATOM   16491 N  N     . PHE A 1 3813 ? 221.382 183.152 226.065 1.00 9.86   ? 3813 PHE A N     1 
ATOM   16492 C  CA    . PHE A 1 3813 ? 222.206 184.008 226.910 1.00 9.61   ? 3813 PHE A CA    1 
ATOM   16493 C  C     . PHE A 1 3813 ? 223.163 184.856 226.083 1.00 10.53  ? 3813 PHE A C     1 
ATOM   16494 O  O     . PHE A 1 3813 ? 223.502 185.975 226.487 1.00 13.92  ? 3813 PHE A O     1 
ATOM   16495 C  CB    . PHE A 1 3813 ? 222.950 183.165 227.942 1.00 12.93  ? 3813 PHE A CB    1 
ATOM   16496 C  CG    . PHE A 1 3813 ? 222.143 182.894 229.180 1.00 19.21  ? 3813 PHE A CG    1 
ATOM   16497 C  CD1   . PHE A 1 3813 ? 221.303 181.796 229.250 1.00 19.68  ? 3813 PHE A CD1   1 
ATOM   16498 C  CD2   . PHE A 1 3813 ? 222.209 183.749 230.265 1.00 22.19  ? 3813 PHE A CD2   1 
ATOM   16499 C  CE1   . PHE A 1 3813 ? 220.550 181.553 230.382 1.00 17.98  ? 3813 PHE A CE1   1 
ATOM   16500 C  CE2   . PHE A 1 3813 ? 221.462 183.509 231.401 1.00 21.37  ? 3813 PHE A CE2   1 
ATOM   16501 C  CZ    . PHE A 1 3813 ? 220.633 182.408 231.459 1.00 19.60  ? 3813 PHE A CZ    1 
ATOM   16502 N  N     . THR A 1 3814 ? 223.583 184.363 224.916 1.00 9.13   ? 3814 THR A N     1 
ATOM   16503 C  CA    . THR A 1 3814 ? 224.346 185.201 223.998 1.00 7.72   ? 3814 THR A CA    1 
ATOM   16504 C  C     . THR A 1 3814 ? 223.517 186.386 223.513 1.00 9.94   ? 3814 THR A C     1 
ATOM   16505 O  O     . THR A 1 3814 ? 224.004 187.523 223.481 1.00 11.64  ? 3814 THR A O     1 
ATOM   16506 C  CB    . THR A 1 3814 ? 224.843 184.368 222.818 1.00 11.10  ? 3814 THR A CB    1 
ATOM   16507 O  OG1   . THR A 1 3814 ? 225.724 183.345 223.297 1.00 11.77  ? 3814 THR A OG1   1 
ATOM   16508 C  CG2   . THR A 1 3814 ? 225.587 185.238 221.819 1.00 11.50  ? 3814 THR A CG2   1 
ATOM   16509 N  N     . MET A 1 3815 ? 222.254 186.145 223.145 1.00 10.28  ? 3815 MET A N     1 
ATOM   16510 C  CA    . MET A 1 3815 ? 221.392 187.267 222.774 1.00 8.86   ? 3815 MET A CA    1 
ATOM   16511 C  C     . MET A 1 3815 ? 221.218 188.237 223.936 1.00 9.50   ? 3815 MET A C     1 
ATOM   16512 O  O     . MET A 1 3815 ? 221.209 189.457 223.739 1.00 16.24  ? 3815 MET A O     1 
ATOM   16513 C  CB    . MET A 1 3815 ? 220.018 186.798 222.294 1.00 8.96   ? 3815 MET A CB    1 
ATOM   16514 C  CG    . MET A 1 3815 ? 219.983 185.805 221.158 1.00 7.09   ? 3815 MET A CG    1 
ATOM   16515 S  SD    . MET A 1 3815 ? 218.304 185.166 221.010 1.00 20.14  ? 3815 MET A SD    1 
ATOM   16516 C  CE    . MET A 1 3815 ? 218.545 183.761 219.939 1.00 14.81  ? 3815 MET A CE    1 
ATOM   16517 N  N     . GLU A 1 3816 ? 221.054 187.710 225.149 1.00 9.80   ? 3816 GLU A N     1 
ATOM   16518 C  CA    . GLU A 1 3816 ? 220.873 188.575 226.310 1.00 12.75  ? 3816 GLU A CA    1 
ATOM   16519 C  C     . GLU A 1 3816 ? 222.103 189.445 226.543 1.00 12.41  ? 3816 GLU A C     1 
ATOM   16520 O  O     . GLU A 1 3816 ? 221.981 190.633 226.863 1.00 13.61  ? 3816 GLU A O     1 
ATOM   16521 C  CB    . GLU A 1 3816 ? 220.562 187.735 227.548 1.00 13.12  ? 3816 GLU A CB    1 
ATOM   16522 C  CG    . GLU A 1 3816 ? 220.278 188.556 228.793 1.00 24.03  ? 3816 GLU A CG    1 
ATOM   16523 C  CD    . GLU A 1 3816 ? 219.924 187.697 229.990 1.00 40.95  ? 3816 GLU A CD    1 
ATOM   16524 O  OE1   . GLU A 1 3816 ? 219.920 186.456 229.852 1.00 48.32  ? 3816 GLU A OE1   1 
ATOM   16525 O  OE2   . GLU A 1 3816 ? 219.653 188.261 231.070 1.00 37.24  ? 3816 GLU A OE2   1 
ATOM   16526 N  N     . SER A 1 3817 ? 223.296 188.873 226.385 1.00 11.44  ? 3817 SER A N     1 
ATOM   16527 C  CA    . SER A 1 3817 ? 224.530 189.634 226.529 1.00 12.75  ? 3817 SER A CA    1 
ATOM   16528 C  C     . SER A 1 3817 ? 224.805 190.556 225.348 1.00 12.02  ? 3817 SER A C     1 
ATOM   16529 O  O     . SER A 1 3817 ? 225.651 191.447 225.467 1.00 12.54  ? 3817 SER A O     1 
ATOM   16530 C  CB    . SER A 1 3817 ? 225.715 188.685 226.717 1.00 14.52  ? 3817 SER A CB    1 
ATOM   16531 O  OG    . SER A 1 3817 ? 226.091 188.092 225.487 1.00 16.64  ? 3817 SER A OG    1 
ATOM   16532 N  N     . LEU A 1 3818 ? 224.120 190.361 224.217 1.00 13.40  ? 3818 LEU A N     1 
ATOM   16533 C  CA    . LEU A 1 3818 ? 224.331 191.222 223.056 1.00 9.94   ? 3818 LEU A CA    1 
ATOM   16534 C  C     . LEU A 1 3818 ? 224.040 192.690 223.344 1.00 11.67  ? 3818 LEU A C     1 
ATOM   16535 O  O     . LEU A 1 3818 ? 224.536 193.558 222.618 1.00 13.32  ? 3818 LEU A O     1 
ATOM   16536 C  CB    . LEU A 1 3818 ? 223.461 190.757 221.889 1.00 9.35   ? 3818 LEU A CB    1 
ATOM   16537 C  CG    . LEU A 1 3818 ? 224.067 189.759 220.902 1.00 12.77  ? 3818 LEU A CG    1 
ATOM   16538 C  CD1   . LEU A 1 3818 ? 222.981 189.210 219.997 1.00 9.97   ? 3818 LEU A CD1   1 
ATOM   16539 C  CD2   . LEU A 1 3818 ? 225.173 190.406 220.089 1.00 11.71  ? 3818 LEU A CD2   1 
ATOM   16540 N  N     . LYS A 1 3819 ? 223.248 192.991 224.375 1.00 12.63  ? 3819 LYS A N     1 
ATOM   16541 C  CA    . LYS A 1 3819 ? 222.925 194.377 224.696 1.00 8.05   ? 3819 LYS A CA    1 
ATOM   16542 C  C     . LYS A 1 3819 ? 224.123 195.162 225.212 1.00 13.00  ? 3819 LYS A C     1 
ATOM   16543 O  O     . LYS A 1 3819 ? 224.032 196.389 225.327 1.00 13.53  ? 3819 LYS A O     1 
ATOM   16544 C  CB    . LYS A 1 3819 ? 221.791 194.429 225.721 1.00 7.38   ? 3819 LYS A CB    1 
ATOM   16545 C  CG    . LYS A 1 3819 ? 222.204 194.073 227.139 1.00 10.69  ? 3819 LYS A CG    1 
ATOM   16546 C  CD    . LYS A 1 3819 ? 221.069 194.318 228.119 1.00 10.70  ? 3819 LYS A CD    1 
ATOM   16547 C  CE    . LYS A 1 3819 ? 220.244 193.061 228.343 1.00 18.06  ? 3819 LYS A CE    1 
ATOM   16548 N  NZ    . LYS A 1 3819 ? 220.892 192.116 229.292 1.00 24.74  ? 3819 LYS A NZ    1 
ATOM   16549 N  N     . GLN A 1 3820 ? 225.234 194.495 225.529 1.00 17.40  ? 3820 GLN A N     1 
ATOM   16550 C  CA    . GLN A 1 3820 ? 226.422 195.199 225.995 1.00 14.83  ? 3820 GLN A CA    1 
ATOM   16551 C  C     . GLN A 1 3820 ? 227.162 195.913 224.872 1.00 16.85  ? 3820 GLN A C     1 
ATOM   16552 O  O     . GLN A 1 3820 ? 227.905 196.860 225.147 1.00 24.22  ? 3820 GLN A O     1 
ATOM   16553 C  CB    . GLN A 1 3820 ? 227.366 194.226 226.699 1.00 16.75  ? 3820 GLN A CB    1 
ATOM   16554 C  CG    . GLN A 1 3820 ? 226.729 193.483 227.858 1.00 17.03  ? 3820 GLN A CG    1 
ATOM   16555 C  CD    . GLN A 1 3820 ? 226.320 194.410 228.981 1.00 29.47  ? 3820 GLN A CD    1 
ATOM   16556 O  OE1   . GLN A 1 3820 ? 225.168 194.410 229.413 1.00 38.63  ? 3820 GLN A OE1   1 
ATOM   16557 N  NE2   . GLN A 1 3820 ? 227.266 195.207 229.464 1.00 35.44  ? 3820 GLN A NE2   1 
ATOM   16558 N  N     . ILE A 1 3821 ? 226.986 195.485 223.619 1.00 12.02  ? 3821 ILE A N     1 
ATOM   16559 C  CA    . ILE A 1 3821 ? 227.693 196.106 222.502 1.00 11.39  ? 3821 ILE A CA    1 
ATOM   16560 C  C     . ILE A 1 3821 ? 226.866 197.169 221.794 1.00 13.54  ? 3821 ILE A C     1 
ATOM   16561 O  O     . ILE A 1 3821 ? 227.429 197.946 221.005 1.00 19.31  ? 3821 ILE A O     1 
ATOM   16562 C  CB    . ILE A 1 3821 ? 228.167 195.051 221.480 1.00 14.20  ? 3821 ILE A CB    1 
ATOM   16563 C  CG1   . ILE A 1 3821 ? 226.983 194.476 220.703 1.00 15.58  ? 3821 ILE A CG1   1 
ATOM   16564 C  CG2   . ILE A 1 3821 ? 228.940 193.944 222.177 1.00 13.20  ? 3821 ILE A CG2   1 
ATOM   16565 C  CD1   . ILE A 1 3821 ? 227.385 193.556 219.573 1.00 10.90  ? 3821 ILE A CD1   1 
ATOM   16566 N  N     . HIS A 1 3822 ? 225.561 197.237 222.048 1.00 12.26  ? 3822 HIS A N     1 
ATOM   16567 C  CA    . HIS A 1 3822 ? 224.710 198.260 221.457 1.00 7.77   ? 3822 HIS A CA    1 
ATOM   16568 C  C     . HIS A 1 3822 ? 223.400 198.309 222.223 1.00 9.89   ? 3822 HIS A C     1 
ATOM   16569 O  O     . HIS A 1 3822 ? 222.829 197.265 222.549 1.00 13.97  ? 3822 HIS A O     1 
ATOM   16570 C  CB    . HIS A 1 3822 ? 224.445 197.982 219.972 1.00 7.85   ? 3822 HIS A CB    1 
ATOM   16571 C  CG    . HIS A 1 3822 ? 224.075 199.199 219.185 1.00 8.13   ? 3822 HIS A CG    1 
ATOM   16572 N  ND1   . HIS A 1 3822 ? 222.799 199.718 219.174 1.00 7.78   ? 3822 HIS A ND1   1 
ATOM   16573 C  CD2   . HIS A 1 3822 ? 224.815 199.998 218.380 1.00 10.29  ? 3822 HIS A CD2   1 
ATOM   16574 C  CE1   . HIS A 1 3822 ? 222.768 200.786 218.397 1.00 7.96   ? 3822 HIS A CE1   1 
ATOM   16575 N  NE2   . HIS A 1 3822 ? 223.978 200.977 217.903 1.00 9.70   ? 3822 HIS A NE2   1 
ATOM   16576 N  N     . PHE A 1 3823 ? 222.927 199.526 222.502 1.00 11.84  ? 3823 PHE A N     1 
ATOM   16577 C  CA    . PHE A 1 3823 ? 221.703 199.701 223.275 1.00 7.96   ? 3823 PHE A CA    1 
ATOM   16578 C  C     . PHE A 1 3823 ? 220.468 199.212 222.531 1.00 7.86   ? 3823 PHE A C     1 
ATOM   16579 O  O     . PHE A 1 3823 ? 219.448 198.931 223.169 1.00 13.82  ? 3823 PHE A O     1 
ATOM   16580 C  CB    . PHE A 1 3823 ? 221.532 201.170 223.660 1.00 6.54   ? 3823 PHE A CB    1 
ATOM   16581 C  CG    . PHE A 1 3823 ? 221.534 202.109 222.487 1.00 11.25  ? 3823 PHE A CG    1 
ATOM   16582 C  CD1   . PHE A 1 3823 ? 220.362 202.399 221.810 1.00 11.93  ? 3823 PHE A CD1   1 
ATOM   16583 C  CD2   . PHE A 1 3823 ? 222.709 202.703 222.061 1.00 10.64  ? 3823 PHE A CD2   1 
ATOM   16584 C  CE1   . PHE A 1 3823 ? 220.362 203.255 220.732 1.00 9.89   ? 3823 PHE A CE1   1 
ATOM   16585 C  CE2   . PHE A 1 3823 ? 222.714 203.563 220.984 1.00 12.63  ? 3823 PHE A CE2   1 
ATOM   16586 C  CZ    . PHE A 1 3823 ? 221.538 203.839 220.319 1.00 12.56  ? 3823 PHE A CZ    1 
ATOM   16587 N  N     . LEU A 1 3824 ? 220.530 199.109 221.205 1.00 7.42   ? 3824 LEU A N     1 
ATOM   16588 C  CA    . LEU A 1 3824 ? 219.387 198.674 220.415 1.00 7.01   ? 3824 LEU A CA    1 
ATOM   16589 C  C     . LEU A 1 3824 ? 219.197 197.164 220.421 1.00 7.07   ? 3824 LEU A C     1 
ATOM   16590 O  O     . LEU A 1 3824 ? 218.146 196.687 219.982 1.00 10.35  ? 3824 LEU A O     1 
ATOM   16591 C  CB    . LEU A 1 3824 ? 219.534 199.163 218.973 1.00 6.63   ? 3824 LEU A CB    1 
ATOM   16592 C  CG    . LEU A 1 3824 ? 218.262 199.270 218.134 1.00 5.98   ? 3824 LEU A CG    1 
ATOM   16593 C  CD1   . LEU A 1 3824 ? 217.471 200.502 218.527 1.00 12.50  ? 3824 LEU A CD1   1 
ATOM   16594 C  CD2   . LEU A 1 3824 ? 218.608 199.301 216.659 1.00 7.66   ? 3824 LEU A CD2   1 
ATOM   16595 N  N     . TYR A 1 3825 ? 220.173 196.403 220.910 1.00 7.30   ? 3825 TYR A N     1 
ATOM   16596 C  CA    . TYR A 1 3825 ? 220.116 194.943 220.844 1.00 7.81   ? 3825 TYR A CA    1 
ATOM   16597 C  C     . TYR A 1 3825 ? 219.407 194.381 222.078 1.00 6.77   ? 3825 TYR A C     1 
ATOM   16598 O  O     . TYR A 1 3825 ? 219.973 193.649 222.888 1.00 8.49   ? 3825 TYR A O     1 
ATOM   16599 C  CB    . TYR A 1 3825 ? 221.520 194.365 220.695 1.00 8.96   ? 3825 TYR A CB    1 
ATOM   16600 C  CG    . TYR A 1 3825 ? 222.275 194.837 219.468 1.00 6.75   ? 3825 TYR A CG    1 
ATOM   16601 C  CD1   . TYR A 1 3825 ? 221.636 195.539 218.454 1.00 7.12   ? 3825 TYR A CD1   1 
ATOM   16602 C  CD2   . TYR A 1 3825 ? 223.631 194.582 219.330 1.00 8.63   ? 3825 TYR A CD2   1 
ATOM   16603 C  CE1   . TYR A 1 3825 ? 222.325 195.972 217.342 1.00 7.15   ? 3825 TYR A CE1   1 
ATOM   16604 C  CE2   . TYR A 1 3825 ? 224.327 195.011 218.220 1.00 10.51  ? 3825 TYR A CE2   1 
ATOM   16605 C  CZ    . TYR A 1 3825 ? 223.670 195.705 217.230 1.00 7.71   ? 3825 TYR A CZ    1 
ATOM   16606 O  OH    . TYR A 1 3825 ? 224.359 196.132 216.122 1.00 8.72   ? 3825 TYR A OH    1 
ATOM   16607 N  N     . GLN A 1 3826 ? 218.135 194.742 222.205 1.00 6.43   ? 3826 GLN A N     1 
ATOM   16608 C  CA    . GLN A 1 3826 ? 217.300 194.314 223.319 1.00 6.36   ? 3826 GLN A CA    1 
ATOM   16609 C  C     . GLN A 1 3826 ? 216.414 193.165 222.863 1.00 7.48   ? 3826 GLN A C     1 
ATOM   16610 O  O     . GLN A 1 3826 ? 215.606 193.326 221.943 1.00 10.11  ? 3826 GLN A O     1 
ATOM   16611 C  CB    . GLN A 1 3826 ? 216.451 195.472 223.842 1.00 7.50   ? 3826 GLN A CB    1 
ATOM   16612 C  CG    . GLN A 1 3826 ? 217.245 196.714 224.200 1.00 6.80   ? 3826 GLN A CG    1 
ATOM   16613 C  CD    . GLN A 1 3826 ? 218.187 196.486 225.363 1.00 5.91   ? 3826 GLN A CD    1 
ATOM   16614 O  OE1   . GLN A 1 3826 ? 217.888 195.719 226.277 1.00 8.09   ? 3826 GLN A OE1   1 
ATOM   16615 N  NE2   . GLN A 1 3826 ? 219.329 197.159 225.339 1.00 4.36   ? 3826 GLN A NE2   1 
ATOM   16616 N  N     . TYR A 1 3827 ? 216.564 192.011 223.507 1.00 8.42   ? 3827 TYR A N     1 
ATOM   16617 C  CA    . TYR A 1 3827 ? 215.802 190.821 223.162 1.00 9.25   ? 3827 TYR A CA    1 
ATOM   16618 C  C     . TYR A 1 3827 ? 215.205 190.217 224.422 1.00 11.65  ? 3827 TYR A C     1 
ATOM   16619 O  O     . TYR A 1 3827 ? 215.878 190.115 225.452 1.00 17.83  ? 3827 TYR A O     1 
ATOM   16620 C  CB    . TYR A 1 3827 ? 216.679 189.788 222.449 1.00 5.93   ? 3827 TYR A CB    1 
ATOM   16621 C  CG    . TYR A 1 3827 ? 217.437 190.357 221.278 1.00 7.51   ? 3827 TYR A CG    1 
ATOM   16622 C  CD1   . TYR A 1 3827 ? 216.773 190.774 220.133 1.00 7.57   ? 3827 TYR A CD1   1 
ATOM   16623 C  CD2   . TYR A 1 3827 ? 218.817 190.493 221.319 1.00 8.63   ? 3827 TYR A CD2   1 
ATOM   16624 C  CE1   . TYR A 1 3827 ? 217.461 191.301 219.063 1.00 7.63   ? 3827 TYR A CE1   1 
ATOM   16625 C  CE2   . TYR A 1 3827 ? 219.513 191.020 220.254 1.00 8.53   ? 3827 TYR A CE2   1 
ATOM   16626 C  CZ    . TYR A 1 3827 ? 218.831 191.423 219.128 1.00 9.09   ? 3827 TYR A CZ    1 
ATOM   16627 O  OH    . TYR A 1 3827 ? 219.523 191.948 218.062 1.00 11.91  ? 3827 TYR A OH    1 
ATOM   16628 N  N     . SER A 1 3828 ? 213.943 189.820 224.335 1.00 11.07  ? 3828 SER A N     1 
ATOM   16629 C  CA    . SER A 1 3828 ? 213.265 189.171 225.443 1.00 11.60  ? 3828 SER A CA    1 
ATOM   16630 C  C     . SER A 1 3828 ? 213.354 187.656 225.299 1.00 15.91  ? 3828 SER A C     1 
ATOM   16631 O  O     . SER A 1 3828 ? 213.765 187.125 224.266 1.00 20.03  ? 3828 SER A O     1 
ATOM   16632 C  CB    . SER A 1 3828 ? 211.805 189.614 225.514 1.00 12.43  ? 3828 SER A CB    1 
ATOM   16633 O  OG    . SER A 1 3828 ? 211.151 189.406 224.275 1.00 13.14  ? 3828 SER A OG    1 
ATOM   16634 N  N     . LEU A 1 3829 ? 212.968 186.954 226.366 1.00 13.31  ? 3829 LEU A N     1 
ATOM   16635 C  CA    . LEU A 1 3829 ? 212.901 185.500 226.297 1.00 10.28  ? 3829 LEU A CA    1 
ATOM   16636 C  C     . LEU A 1 3829 ? 211.870 185.044 225.274 1.00 11.57  ? 3829 LEU A C     1 
ATOM   16637 O  O     . LEU A 1 3829 ? 212.034 183.988 224.655 1.00 15.05  ? 3829 LEU A O     1 
ATOM   16638 C  CB    . LEU A 1 3829 ? 212.583 184.920 227.674 1.00 13.10  ? 3829 LEU A CB    1 
ATOM   16639 C  CG    . LEU A 1 3829 ? 212.463 183.398 227.755 1.00 10.62  ? 3829 LEU A CG    1 
ATOM   16640 C  CD1   . LEU A 1 3829 ? 213.789 182.746 227.412 1.00 13.30  ? 3829 LEU A CD1   1 
ATOM   16641 C  CD2   . LEU A 1 3829 ? 211.987 182.960 229.128 1.00 11.28  ? 3829 LEU A CD2   1 
ATOM   16642 N  N     . GLN A 1 3830 ? 210.811 185.832 225.078 1.00 10.28  ? 3830 GLN A N     1 
ATOM   16643 C  CA    . GLN A 1 3830 ? 209.775 185.459 224.123 1.00 10.85  ? 3830 GLN A CA    1 
ATOM   16644 C  C     . GLN A 1 3830 ? 210.297 185.444 222.692 1.00 14.10  ? 3830 GLN A C     1 
ATOM   16645 O  O     . GLN A 1 3830 ? 209.855 184.620 221.888 1.00 16.56  ? 3830 GLN A O     1 
ATOM   16646 C  CB    . GLN A 1 3830 ? 208.583 186.405 224.245 1.00 12.01  ? 3830 GLN A CB    1 
ATOM   16647 C  CG    . GLN A 1 3830 ? 207.301 185.858 223.645 1.00 15.11  ? 3830 GLN A CG    1 
ATOM   16648 C  CD    . GLN A 1 3830 ? 207.118 184.379 223.913 1.00 23.35  ? 3830 GLN A CD    1 
ATOM   16649 O  OE1   . GLN A 1 3830 ? 207.007 183.954 225.062 1.00 27.80  ? 3830 GLN A OE1   1 
ATOM   16650 N  NE2   . GLN A 1 3830 ? 207.090 183.584 222.850 1.00 19.26  ? 3830 GLN A NE2   1 
ATOM   16651 N  N     . PHE A 1 3831 ? 211.227 186.338 222.353 1.00 13.25  ? 3831 PHE A N     1 
ATOM   16652 C  CA    . PHE A 1 3831 ? 211.806 186.336 221.011 1.00 10.17  ? 3831 PHE A CA    1 
ATOM   16653 C  C     . PHE A 1 3831 ? 212.553 185.035 220.740 1.00 14.47  ? 3831 PHE A C     1 
ATOM   16654 O  O     . PHE A 1 3831 ? 212.375 184.399 219.691 1.00 19.57  ? 3831 PHE A O     1 
ATOM   16655 C  CB    . PHE A 1 3831 ? 212.734 187.542 220.857 1.00 9.57   ? 3831 PHE A CB    1 
ATOM   16656 C  CG    . PHE A 1 3831 ? 213.335 187.683 219.490 1.00 11.58  ? 3831 PHE A CG    1 
ATOM   16657 C  CD1   . PHE A 1 3831 ? 212.530 187.813 218.373 1.00 12.97  ? 3831 PHE A CD1   1 
ATOM   16658 C  CD2   . PHE A 1 3831 ? 214.709 187.696 219.323 1.00 11.93  ? 3831 PHE A CD2   1 
ATOM   16659 C  CE1   . PHE A 1 3831 ? 213.084 187.947 217.115 1.00 15.64  ? 3831 PHE A CE1   1 
ATOM   16660 C  CE2   . PHE A 1 3831 ? 215.268 187.829 218.070 1.00 9.46   ? 3831 PHE A CE2   1 
ATOM   16661 C  CZ    . PHE A 1 3831 ? 214.455 187.956 216.965 1.00 9.80   ? 3831 PHE A CZ    1 
ATOM   16662 N  N     . PHE A 1 3832 ? 213.387 184.612 221.693 1.00 16.06  ? 3832 PHE A N     1 
ATOM   16663 C  CA    . PHE A 1 3832 ? 214.099 183.349 221.544 1.00 12.10  ? 3832 PHE A CA    1 
ATOM   16664 C  C     . PHE A 1 3832 ? 213.135 182.172 221.536 1.00 12.50  ? 3832 PHE A C     1 
ATOM   16665 O  O     . PHE A 1 3832 ? 213.355 181.190 220.820 1.00 15.71  ? 3832 PHE A O     1 
ATOM   16666 C  CB    . PHE A 1 3832 ? 215.126 183.187 222.662 1.00 10.48  ? 3832 PHE A CB    1 
ATOM   16667 C  CG    . PHE A 1 3832 ? 215.709 181.810 222.743 1.00 14.58  ? 3832 PHE A CG    1 
ATOM   16668 C  CD1   . PHE A 1 3832 ? 216.626 181.379 221.801 1.00 15.95  ? 3832 PHE A CD1   1 
ATOM   16669 C  CD2   . PHE A 1 3832 ? 215.327 180.940 223.748 1.00 14.99  ? 3832 PHE A CD2   1 
ATOM   16670 C  CE1   . PHE A 1 3832 ? 217.160 180.112 221.868 1.00 17.16  ? 3832 PHE A CE1   1 
ATOM   16671 C  CE2   . PHE A 1 3832 ? 215.857 179.672 223.818 1.00 13.80  ? 3832 PHE A CE2   1 
ATOM   16672 C  CZ    . PHE A 1 3832 ? 216.772 179.257 222.876 1.00 14.80  ? 3832 PHE A CZ    1 
ATOM   16673 N  N     . LEU A 1 3833 ? 212.070 182.242 222.335 1.00 12.57  ? 3833 LEU A N     1 
ATOM   16674 C  CA    . LEU A 1 3833 ? 211.084 181.168 222.339 1.00 9.47   ? 3833 LEU A CA    1 
ATOM   16675 C  C     . LEU A 1 3833 ? 210.369 181.071 220.999 1.00 11.80  ? 3833 LEU A C     1 
ATOM   16676 O  O     . LEU A 1 3833 ? 210.069 179.970 220.531 1.00 18.98  ? 3833 LEU A O     1 
ATOM   16677 C  CB    . LEU A 1 3833 ? 210.084 181.378 223.475 1.00 13.39  ? 3833 LEU A CB    1 
ATOM   16678 C  CG    . LEU A 1 3833 ? 210.599 181.096 224.889 1.00 11.38  ? 3833 LEU A CG    1 
ATOM   16679 C  CD1   . LEU A 1 3833 ? 209.470 181.185 225.900 1.00 15.68  ? 3833 LEU A CD1   1 
ATOM   16680 C  CD2   . LEU A 1 3833 ? 211.280 179.742 224.963 1.00 7.70   ? 3833 LEU A CD2   1 
ATOM   16681 N  N     . ASP A 1 3834 ? 210.082 182.212 220.367 1.00 16.89  ? 3834 ASP A N     1 
ATOM   16682 C  CA    . ASP A 1 3834 ? 209.496 182.195 219.030 1.00 14.54  ? 3834 ASP A CA    1 
ATOM   16683 C  C     . ASP A 1 3834 ? 210.466 181.616 218.008 1.00 15.75  ? 3834 ASP A C     1 
ATOM   16684 O  O     . ASP A 1 3834 ? 210.055 180.877 217.107 1.00 18.22  ? 3834 ASP A O     1 
ATOM   16685 C  CB    . ASP A 1 3834 ? 209.064 183.603 218.617 1.00 15.24  ? 3834 ASP A CB    1 
ATOM   16686 C  CG    . ASP A 1 3834 ? 208.073 184.217 219.584 1.00 24.11  ? 3834 ASP A CG    1 
ATOM   16687 O  OD1   . ASP A 1 3834 ? 208.080 185.456 219.738 1.00 23.34  ? 3834 ASP A OD1   1 
ATOM   16688 O  OD2   . ASP A 1 3834 ? 207.285 183.462 220.192 1.00 25.89  ? 3834 ASP A OD2   1 
ATOM   16689 N  N     . ILE A 1 3835 ? 211.755 181.947 218.125 1.00 14.63  ? 3835 ILE A N     1 
ATOM   16690 C  CA    . ILE A 1 3835 ? 212.755 181.337 217.246 1.00 13.72  ? 3835 ILE A CA    1 
ATOM   16691 C  C     . ILE A 1 3835 ? 212.757 179.822 217.421 1.00 13.15  ? 3835 ILE A C     1 
ATOM   16692 O  O     . ILE A 1 3835 ? 212.753 179.057 216.446 1.00 17.13  ? 3835 ILE A O     1 
ATOM   16693 C  CB    . ILE A 1 3835 ? 214.148 181.933 217.522 1.00 14.00  ? 3835 ILE A CB    1 
ATOM   16694 C  CG1   . ILE A 1 3835 ? 214.241 183.364 216.995 1.00 12.02  ? 3835 ILE A CG1   1 
ATOM   16695 C  CG2   . ILE A 1 3835 ? 215.235 181.065 216.909 1.00 14.01  ? 3835 ILE A CG2   1 
ATOM   16696 C  CD1   . ILE A 1 3835 ? 215.541 184.051 217.341 1.00 11.72  ? 3835 ILE A CD1   1 
ATOM   16697 N  N     . TYR A 1 3836 ? 212.745 179.371 218.673 1.00 13.80  ? 3836 TYR A N     1 
ATOM   16698 C  CA    . TYR A 1 3836 ? 212.781 177.945 218.973 1.00 13.79  ? 3836 TYR A CA    1 
ATOM   16699 C  C     . TYR A 1 3836 ? 211.523 177.242 218.475 1.00 15.61  ? 3836 TYR A C     1 
ATOM   16700 O  O     . TYR A 1 3836 ? 211.588 176.107 217.990 1.00 18.82  ? 3836 TYR A O     1 
ATOM   16701 C  CB    . TYR A 1 3836 ? 212.970 177.763 220.479 1.00 12.65  ? 3836 TYR A CB    1 
ATOM   16702 C  CG    . TYR A 1 3836 ? 213.215 176.351 220.944 1.00 16.34  ? 3836 TYR A CG    1 
ATOM   16703 C  CD1   . TYR A 1 3836 ? 214.261 175.602 220.429 1.00 17.83  ? 3836 TYR A CD1   1 
ATOM   16704 C  CD2   . TYR A 1 3836 ? 212.439 175.791 221.947 1.00 16.92  ? 3836 TYR A CD2   1 
ATOM   16705 C  CE1   . TYR A 1 3836 ? 214.494 174.318 220.863 1.00 17.80  ? 3836 TYR A CE1   1 
ATOM   16706 C  CE2   . TYR A 1 3836 ? 212.672 174.512 222.394 1.00 16.45  ? 3836 TYR A CE2   1 
ATOM   16707 C  CZ    . TYR A 1 3836 ? 213.701 173.780 221.849 1.00 17.73  ? 3836 TYR A CZ    1 
ATOM   16708 O  OH    . TYR A 1 3836 ? 213.937 172.505 222.291 1.00 25.49  ? 3836 TYR A OH    1 
ATOM   16709 N  N     . HIS A 1 3837 ? 210.370 177.905 218.587 1.00 14.89  ? 3837 HIS A N     1 
ATOM   16710 C  CA    . HIS A 1 3837 ? 209.128 177.360 218.052 1.00 19.01  ? 3837 HIS A CA    1 
ATOM   16711 C  C     . HIS A 1 3837 ? 209.179 177.248 216.533 1.00 22.52  ? 3837 HIS A C     1 
ATOM   16712 O  O     . HIS A 1 3837 ? 208.786 176.223 215.965 1.00 27.41  ? 3837 HIS A O     1 
ATOM   16713 C  CB    . HIS A 1 3837 ? 207.953 178.237 218.485 1.00 22.22  ? 3837 HIS A CB    1 
ATOM   16714 C  CG    . HIS A 1 3837 ? 206.614 177.596 218.303 1.00 35.94  ? 3837 HIS A CG    1 
ATOM   16715 N  ND1   . HIS A 1 3837 ? 205.806 177.858 217.218 1.00 37.81  ? 3837 HIS A ND1   1 
ATOM   16716 C  CD2   . HIS A 1 3837 ? 205.933 176.717 219.075 1.00 38.15  ? 3837 HIS A CD2   1 
ATOM   16717 C  CE1   . HIS A 1 3837 ? 204.690 177.162 217.323 1.00 42.32  ? 3837 HIS A CE1   1 
ATOM   16718 N  NE2   . HIS A 1 3837 ? 204.740 176.462 218.443 1.00 46.48  ? 3837 HIS A NE2   1 
ATOM   16719 N  N     . ASN A 1 3838 ? 209.657 178.296 215.859 1.00 25.20  ? 3838 ASN A N     1 
ATOM   16720 C  CA    . ASN A 1 3838 ? 209.783 178.267 214.406 1.00 20.48  ? 3838 ASN A CA    1 
ATOM   16721 C  C     . ASN A 1 3838 ? 210.806 177.243 213.939 1.00 23.87  ? 3838 ASN A C     1 
ATOM   16722 O  O     . ASN A 1 3838 ? 210.774 176.838 212.772 1.00 35.02  ? 3838 ASN A O     1 
ATOM   16723 C  CB    . ASN A 1 3838 ? 210.168 179.652 213.884 1.00 22.98  ? 3838 ASN A CB    1 
ATOM   16724 C  CG    . ASN A 1 3838 ? 210.151 179.729 212.371 1.00 27.19  ? 3838 ASN A CG    1 
ATOM   16725 O  OD1   . ASN A 1 3838 ? 209.090 179.742 211.751 1.00 31.87  ? 3838 ASN A OD1   1 
ATOM   16726 N  ND2   . ASN A 1 3838 ? 211.333 179.770 211.768 1.00 24.50  ? 3838 ASN A ND2   1 
ATOM   16727 N  N     . VAL A 1 3839 ? 211.727 176.841 214.810 1.00 21.06  ? 3839 VAL A N     1 
ATOM   16728 C  CA    . VAL A 1 3839 ? 212.691 175.813 214.432 1.00 17.34  ? 3839 VAL A CA    1 
ATOM   16729 C  C     . VAL A 1 3839 ? 212.111 174.419 214.656 1.00 19.35  ? 3839 VAL A C     1 
ATOM   16730 O  O     . VAL A 1 3839 ? 212.240 173.535 213.803 1.00 22.89  ? 3839 VAL A O     1 
ATOM   16731 C  CB    . VAL A 1 3839 ? 214.009 176.020 215.200 1.00 15.84  ? 3839 VAL A CB    1 
ATOM   16732 C  CG1   . VAL A 1 3839 ? 214.872 174.777 215.131 1.00 18.81  ? 3839 VAL A CG1   1 
ATOM   16733 C  CG2   . VAL A 1 3839 ? 214.750 177.217 214.637 1.00 12.81  ? 3839 VAL A CG2   1 
ATOM   16734 N  N     . LEU A 1 3840 ? 211.462 174.202 215.803 1.00 26.26  ? 3840 LEU A N     1 
ATOM   16735 C  CA    . LEU A 1 3840 ? 210.843 172.907 216.073 1.00 21.27  ? 3840 LEU A CA    1 
ATOM   16736 C  C     . LEU A 1 3840 ? 209.645 172.664 215.163 1.00 22.58  ? 3840 LEU A C     1 
ATOM   16737 O  O     . LEU A 1 3840 ? 209.521 171.597 214.551 1.00 23.45  ? 3840 LEU A O     1 
ATOM   16738 C  CB    . LEU A 1 3840 ? 210.421 172.818 217.540 1.00 19.93  ? 3840 LEU A CB    1 
ATOM   16739 C  CG    . LEU A 1 3840 ? 211.523 172.711 218.593 1.00 20.78  ? 3840 LEU A CG    1 
ATOM   16740 C  CD1   . LEU A 1 3840 ? 210.911 172.673 219.977 1.00 21.47  ? 3840 LEU A CD1   1 
ATOM   16741 C  CD2   . LEU A 1 3840 ? 212.369 171.476 218.354 1.00 21.38  ? 3840 LEU A CD2   1 
ATOM   16742 N  N     . TYR A 1 3841 ? 208.750 173.640 215.068 1.00 28.80  ? 3841 TYR A N     1 
ATOM   16743 C  CA    . TYR A 1 3841 ? 207.566 173.559 214.229 1.00 26.37  ? 3841 TYR A CA    1 
ATOM   16744 C  C     . TYR A 1 3841 ? 207.743 174.447 213.006 1.00 32.02  ? 3841 TYR A C     1 
ATOM   16745 O  O     . TYR A 1 3841 ? 208.719 175.193 212.900 1.00 38.70  ? 3841 TYR A O     1 
ATOM   16746 C  CB    . TYR A 1 3841 ? 206.315 173.976 215.009 1.00 23.55  ? 3841 TYR A CB    1 
ATOM   16747 C  CG    . TYR A 1 3841 ? 206.033 173.106 216.209 1.00 30.35  ? 3841 TYR A CG    1 
ATOM   16748 C  CD1   . TYR A 1 3841 ? 206.111 171.724 216.124 1.00 37.19  ? 3841 TYR A CD1   1 
ATOM   16749 C  CD2   . TYR A 1 3841 ? 205.709 173.668 217.434 1.00 31.28  ? 3841 TYR A CD2   1 
ATOM   16750 C  CE1   . TYR A 1 3841 ? 205.857 170.927 217.222 1.00 35.35  ? 3841 TYR A CE1   1 
ATOM   16751 C  CE2   . TYR A 1 3841 ? 205.457 172.881 218.537 1.00 37.46  ? 3841 TYR A CE2   1 
ATOM   16752 C  CZ    . TYR A 1 3841 ? 205.531 171.513 218.427 1.00 40.31  ? 3841 TYR A CZ    1 
ATOM   16753 O  OH    . TYR A 1 3841 ? 205.278 170.729 219.528 1.00 47.18  ? 3841 TYR A OH    1 
ATOM   16754 N  N     . GLU A 1 3842 ? 206.778 174.355 212.085 1.00 27.03  ? 3842 GLU A N     1 
ATOM   16755 C  CA    . GLU A 1 3842 ? 206.777 175.101 210.818 1.00 32.07  ? 3842 GLU A CA    1 
ATOM   16756 C  C     . GLU A 1 3842 ? 208.171 175.173 210.193 1.00 34.53  ? 3842 GLU A C     1 
ATOM   16757 O  O     . GLU A 1 3842 ? 208.597 176.214 209.688 1.00 31.35  ? 3842 GLU A O     1 
ATOM   16758 C  CB    . GLU A 1 3842 ? 206.173 176.504 210.985 1.00 33.02  ? 3842 GLU A CB    1 
ATOM   16759 C  CG    . GLU A 1 3842 ? 206.844 177.420 211.997 1.00 32.69  ? 3842 GLU A CG    1 
ATOM   16760 C  CD    . GLU A 1 3842 ? 205.883 178.425 212.602 1.00 35.62  ? 3842 GLU A CD    1 
ATOM   16761 O  OE1   . GLU A 1 3842 ? 204.902 178.791 211.924 1.00 32.69  ? 3842 GLU A OE1   1 
ATOM   16762 O  OE2   . GLU A 1 3842 ? 206.108 178.847 213.755 1.00 34.48  ? 3842 GLU A OE2   1 
ATOM   16763 N  N     . ASN A 1 3843 ? 208.887 174.049 210.222 1.00 31.68  ? 3843 ASN A N     1 
ATOM   16764 C  CA    . ASN A 1 3843 ? 210.213 173.958 209.634 1.00 27.61  ? 3843 ASN A CA    1 
ATOM   16765 C  C     . ASN A 1 3843 ? 210.111 173.290 208.274 1.00 35.69  ? 3843 ASN A C     1 
ATOM   16766 O  O     . ASN A 1 3843 ? 209.705 172.120 208.202 1.00 43.83  ? 3843 ASN A O     1 
ATOM   16767 C  CB    . ASN A 1 3843 ? 211.154 173.172 210.545 1.00 29.37  ? 3843 ASN A CB    1 
ATOM   16768 C  CG    . ASN A 1 3843 ? 212.600 173.604 210.403 1.00 31.66  ? 3843 ASN A CG    1 
ATOM   16769 O  OD1   . ASN A 1 3843 ? 212.913 174.529 209.654 1.00 39.49  ? 3843 ASN A OD1   1 
ATOM   16770 N  ND2   . ASN A 1 3843 ? 213.490 172.937 211.125 1.00 26.32  ? 3843 ASN A ND2   1 
ATOM   16771 N  N     . PRO A 1 3844 ? 210.451 173.974 207.181 1.00 37.40  ? 3844 PRO A N     1 
ATOM   16772 C  CA    . PRO A 1 3844 ? 210.371 173.332 205.858 1.00 37.38  ? 3844 PRO A CA    1 
ATOM   16773 C  C     . PRO A 1 3844 ? 211.298 172.139 205.703 1.00 36.41  ? 3844 PRO A C     1 
ATOM   16774 O  O     . PRO A 1 3844 ? 211.039 171.281 204.850 1.00 43.04  ? 3844 PRO A O     1 
ATOM   16775 C  CB    . PRO A 1 3844 ? 210.753 174.464 204.893 1.00 36.62  ? 3844 PRO A CB    1 
ATOM   16776 C  CG    . PRO A 1 3844 ? 210.526 175.725 205.667 1.00 39.06  ? 3844 PRO A CG    1 
ATOM   16777 C  CD    . PRO A 1 3844 ? 210.849 175.387 207.086 1.00 34.12  ? 3844 PRO A CD    1 
ATOM   16778 N  N     . ASN A 1 3845 ? 212.363 172.051 206.495 1.00 33.72  ? 3845 ASN A N     1 
ATOM   16779 C  CA    . ASN A 1 3845 ? 213.323 170.963 206.378 1.00 34.61  ? 3845 ASN A CA    1 
ATOM   16780 C  C     . ASN A 1 3845 ? 212.855 169.675 207.042 1.00 32.12  ? 3845 ASN A C     1 
ATOM   16781 O  O     . ASN A 1 3845 ? 213.546 168.657 206.930 1.00 36.34  ? 3845 ASN A O     1 
ATOM   16782 C  CB    . ASN A 1 3845 ? 214.670 171.383 206.974 1.00 36.09  ? 3845 ASN A CB    1 
ATOM   16783 C  CG    . ASN A 1 3845 ? 215.169 172.699 206.415 1.00 33.57  ? 3845 ASN A CG    1 
ATOM   16784 O  OD1   . ASN A 1 3845 ? 214.512 173.731 206.543 1.00 35.75  ? 3845 ASN A OD1   1 
ATOM   16785 N  ND2   . ASN A 1 3845 ? 216.339 172.669 205.790 1.00 38.73  ? 3845 ASN A ND2   1 
ATOM   16786 N  N     . LEU A 1 3846 ? 211.713 169.690 207.730 1.00 30.81  ? 3846 LEU A N     1 
ATOM   16787 C  CA    . LEU A 1 3846 ? 211.209 168.522 208.441 1.00 36.02  ? 3846 LEU A CA    1 
ATOM   16788 C  C     . LEU A 1 3846 ? 209.906 167.994 207.850 1.00 40.64  ? 3846 LEU A C     1 
ATOM   16789 O  O     . LEU A 1 3846 ? 209.193 167.238 208.516 1.00 45.43  ? 3846 LEU A O     1 
ATOM   16790 C  CB    . LEU A 1 3846 ? 211.016 168.850 209.923 1.00 34.99  ? 3846 LEU A CB    1 
ATOM   16791 C  CG    . LEU A 1 3846 ? 212.276 169.048 210.763 1.00 28.56  ? 3846 LEU A CG    1 
ATOM   16792 C  CD1   . LEU A 1 3846 ? 211.904 169.371 212.198 1.00 23.49  ? 3846 LEU A CD1   1 
ATOM   16793 C  CD2   . LEU A 1 3846 ? 213.154 167.816 210.700 1.00 28.10  ? 3846 LEU A CD2   1 
ATOM   16794 N  N     . LYS A 1 3847 ? 209.578 168.382 206.615 1.00 45.49  ? 3847 LYS A N     1 
ATOM   16795 C  CA    . LYS A 1 3847 ? 208.280 168.032 206.046 1.00 52.07  ? 3847 LYS A CA    1 
ATOM   16796 C  C     . LYS A 1 3847 ? 208.135 166.526 205.866 1.00 58.41  ? 3847 LYS A C     1 
ATOM   16797 O  O     . LYS A 1 3847 ? 207.153 165.928 206.322 1.00 58.10  ? 3847 LYS A O     1 
ATOM   16798 C  CB    . LYS A 1 3847 ? 208.083 168.754 204.713 1.00 48.07  ? 3847 LYS A CB    1 
ATOM   16799 C  CG    . LYS A 1 3847 ? 207.279 170.038 204.822 1.00 56.67  ? 3847 LYS A CG    1 
ATOM   16800 C  CD    . LYS A 1 3847 ? 206.011 169.826 205.632 1.00 58.50  ? 3847 LYS A CD    1 
ATOM   16801 C  CE    . LYS A 1 3847 ? 204.890 170.733 205.152 1.00 53.70  ? 3847 LYS A CE    1 
ATOM   16802 N  NZ    . LYS A 1 3847 ? 203.598 170.419 205.822 1.00 53.62  ? 3847 LYS A NZ    1 
ATOM   16803 N  N     . GLY A 1 3848 ? 209.099 165.893 205.206 1.00 50.27  ? 3848 GLY A N     1 
ATOM   16804 C  CA    . GLY A 1 3848 ? 209.049 164.473 204.945 1.00 48.61  ? 3848 GLY A CA    1 
ATOM   16805 C  C     . GLY A 1 3848 ? 210.034 163.635 205.721 1.00 44.53  ? 3848 GLY A C     1 
ATOM   16806 O  O     . GLY A 1 3848 ? 210.074 162.415 205.531 1.00 47.05  ? 3848 GLY A O     1 
ATOM   16807 N  N     . VAL A 1 3849 ? 210.828 164.244 206.591 1.00 48.30  ? 3849 VAL A N     1 
ATOM   16808 C  CA    . VAL A 1 3849 ? 211.877 163.531 207.308 1.00 44.49  ? 3849 VAL A CA    1 
ATOM   16809 C  C     . VAL A 1 3849 ? 211.273 162.825 208.513 1.00 39.20  ? 3849 VAL A C     1 
ATOM   16810 O  O     . VAL A 1 3849 ? 210.490 163.410 209.270 1.00 36.85  ? 3849 VAL A O     1 
ATOM   16811 C  CB    . VAL A 1 3849 ? 212.990 164.508 207.722 1.00 38.62  ? 3849 VAL A CB    1 
ATOM   16812 C  CG1   . VAL A 1 3849 ? 214.040 163.793 208.528 1.00 30.25  ? 3849 VAL A CG1   1 
ATOM   16813 C  CG2   . VAL A 1 3849 ? 213.604 165.161 206.495 1.00 44.63  ? 3849 VAL A CG2   1 
ATOM   16814 N  N     . THR A 1 3850 ? 211.634 161.557 208.695 1.00 35.50  ? 3850 THR A N     1 
ATOM   16815 C  CA    . THR A 1 3850 ? 211.054 160.719 209.739 1.00 38.54  ? 3850 THR A CA    1 
ATOM   16816 C  C     . THR A 1 3850 ? 212.052 160.297 210.807 1.00 40.90  ? 3850 THR A C     1 
ATOM   16817 O  O     . THR A 1 3850 ? 211.705 160.284 211.992 1.00 37.17  ? 3850 THR A O     1 
ATOM   16818 C  CB    . THR A 1 3850 ? 210.414 159.469 209.107 1.00 41.92  ? 3850 THR A CB    1 
ATOM   16819 O  OG1   . THR A 1 3850 ? 209.173 159.830 208.488 1.00 34.96  ? 3850 THR A OG1   1 
ATOM   16820 C  CG2   . THR A 1 3850 ? 210.152 158.393 210.151 1.00 38.18  ? 3850 THR A CG2   1 
ATOM   16821 N  N     . ASP A 1 3851 ? 213.286 159.969 210.425 1.00 42.12  ? 3851 ASP A N     1 
ATOM   16822 C  CA    . ASP A 1 3851 ? 214.270 159.487 211.389 1.00 46.28  ? 3851 ASP A CA    1 
ATOM   16823 C  C     . ASP A 1 3851 ? 214.506 160.514 212.489 1.00 46.50  ? 3851 ASP A C     1 
ATOM   16824 O  O     . ASP A 1 3851 ? 214.701 161.701 212.217 1.00 45.70  ? 3851 ASP A O     1 
ATOM   16825 C  CB    . ASP A 1 3851 ? 215.584 159.159 210.685 1.00 40.20  ? 3851 ASP A CB    1 
ATOM   16826 C  CG    . ASP A 1 3851 ? 216.519 158.343 211.553 1.00 47.00  ? 3851 ASP A CG    1 
ATOM   16827 O  OD1   . ASP A 1 3851 ? 216.074 157.856 212.613 1.00 44.20  ? 3851 ASP A OD1   1 
ATOM   16828 O  OD2   . ASP A 1 3851 ? 217.699 158.188 211.177 1.00 59.14  ? 3851 ASP A OD2   1 
ATOM   16829 N  N     . HIS A 1 3852 ? 214.494 160.045 213.739 1.00 40.46  ? 3852 HIS A N     1 
ATOM   16830 C  CA    . HIS A 1 3852 ? 214.576 160.954 214.877 1.00 37.34  ? 3852 HIS A CA    1 
ATOM   16831 C  C     . HIS A 1 3852 ? 215.931 161.648 214.952 1.00 40.58  ? 3852 HIS A C     1 
ATOM   16832 O  O     . HIS A 1 3852 ? 216.001 162.850 215.227 1.00 45.79  ? 3852 HIS A O     1 
ATOM   16833 C  CB    . HIS A 1 3852 ? 214.289 160.198 216.173 1.00 38.72  ? 3852 HIS A CB    1 
ATOM   16834 C  CG    . HIS A 1 3852 ? 212.841 159.880 216.379 1.00 43.29  ? 3852 HIS A CG    1 
ATOM   16835 N  ND1   . HIS A 1 3852 ? 212.382 158.598 216.586 1.00 41.54  ? 3852 HIS A ND1   1 
ATOM   16836 C  CD2   . HIS A 1 3852 ? 211.750 160.681 216.409 1.00 43.02  ? 3852 HIS A CD2   1 
ATOM   16837 C  CE1   . HIS A 1 3852 ? 211.070 158.622 216.736 1.00 40.54  ? 3852 HIS A CE1   1 
ATOM   16838 N  NE2   . HIS A 1 3852 ? 210.661 159.873 216.632 1.00 40.29  ? 3852 HIS A NE2   1 
ATOM   16839 N  N     . THR A 1 3853 ? 217.020 160.909 214.724 1.00 36.76  ? 3853 THR A N     1 
ATOM   16840 C  CA    . THR A 1 3853 ? 218.350 161.488 214.884 1.00 35.18  ? 3853 THR A CA    1 
ATOM   16841 C  C     . THR A 1 3853 ? 218.643 162.530 213.811 1.00 38.17  ? 3853 THR A C     1 
ATOM   16842 O  O     . THR A 1 3853 ? 219.185 163.603 214.105 1.00 33.60  ? 3853 THR A O     1 
ATOM   16843 C  CB    . THR A 1 3853 ? 219.407 160.386 214.862 1.00 37.31  ? 3853 THR A CB    1 
ATOM   16844 O  OG1   . THR A 1 3853 ? 218.956 159.277 215.650 1.00 36.84  ? 3853 THR A OG1   1 
ATOM   16845 C  CG2   . THR A 1 3853 ? 220.722 160.900 215.430 1.00 38.51  ? 3853 THR A CG2   1 
ATOM   16846 N  N     . GLN A 1 3854 ? 218.291 162.236 212.557 1.00 37.92  ? 3854 GLN A N     1 
ATOM   16847 C  CA    . GLN A 1 3854 ? 218.513 163.213 211.499 1.00 37.33  ? 3854 GLN A CA    1 
ATOM   16848 C  C     . GLN A 1 3854 ? 217.560 164.397 211.627 1.00 29.76  ? 3854 GLN A C     1 
ATOM   16849 O  O     . GLN A 1 3854 ? 217.933 165.527 211.287 1.00 28.46  ? 3854 GLN A O     1 
ATOM   16850 C  CB    . GLN A 1 3854 ? 218.405 162.533 210.132 1.00 37.58  ? 3854 GLN A CB    1 
ATOM   16851 C  CG    . GLN A 1 3854 ? 216.999 162.315 209.628 1.00 42.51  ? 3854 GLN A CG    1 
ATOM   16852 C  CD    . GLN A 1 3854 ? 216.959 161.982 208.151 1.00 46.27  ? 3854 GLN A CD    1 
ATOM   16853 O  OE1   . GLN A 1 3854 ? 216.973 162.872 207.301 1.00 43.69  ? 3854 GLN A OE1   1 
ATOM   16854 N  NE2   . GLN A 1 3854 ? 216.904 160.694 207.837 1.00 41.93  ? 3854 GLN A NE2   1 
ATOM   16855 N  N     . ARG A 1 3855 ? 216.351 164.173 212.150 1.00 31.55  ? 3855 ARG A N     1 
ATOM   16856 C  CA    . ARG A 1 3855 ? 215.484 165.295 212.495 1.00 29.79  ? 3855 ARG A CA    1 
ATOM   16857 C  C     . ARG A 1 3855 ? 216.123 166.172 213.561 1.00 26.38  ? 3855 ARG A C     1 
ATOM   16858 O  O     . ARG A 1 3855 ? 216.059 167.401 213.482 1.00 24.90  ? 3855 ARG A O     1 
ATOM   16859 C  CB    . ARG A 1 3855 ? 214.118 164.799 212.972 1.00 28.44  ? 3855 ARG A CB    1 
ATOM   16860 C  CG    . ARG A 1 3855 ? 213.169 164.402 211.862 1.00 27.69  ? 3855 ARG A CG    1 
ATOM   16861 C  CD    . ARG A 1 3855 ? 211.791 164.059 212.397 1.00 25.50  ? 3855 ARG A CD    1 
ATOM   16862 N  NE    . ARG A 1 3855 ? 211.137 165.217 212.995 1.00 26.29  ? 3855 ARG A NE    1 
ATOM   16863 C  CZ    . ARG A 1 3855 ? 210.101 165.849 212.461 1.00 27.78  ? 3855 ARG A CZ    1 
ATOM   16864 N  NH1   . ARG A 1 3855 ? 209.583 165.472 211.304 1.00 31.59  ? 3855 ARG A NH1   1 
ATOM   16865 N  NH2   . ARG A 1 3855 ? 209.573 166.887 213.102 1.00 24.44  ? 3855 ARG A NH2   1 
ATOM   16866 N  N     . LEU A 1 3856 ? 216.736 165.554 214.573 1.00 23.41  ? 3856 LEU A N     1 
ATOM   16867 C  CA    . LEU A 1 3856 ? 217.399 166.321 215.622 1.00 22.70  ? 3856 LEU A CA    1 
ATOM   16868 C  C     . LEU A 1 3856 ? 218.561 167.128 215.060 1.00 19.51  ? 3856 LEU A C     1 
ATOM   16869 O  O     . LEU A 1 3856 ? 218.772 168.281 215.452 1.00 20.14  ? 3856 LEU A O     1 
ATOM   16870 C  CB    . LEU A 1 3856 ? 217.877 165.387 216.733 1.00 21.86  ? 3856 LEU A CB    1 
ATOM   16871 C  CG    . LEU A 1 3856 ? 218.466 166.041 217.985 1.00 22.95  ? 3856 LEU A CG    1 
ATOM   16872 C  CD1   . LEU A 1 3856 ? 217.596 167.193 218.453 1.00 22.21  ? 3856 LEU A CD1   1 
ATOM   16873 C  CD2   . LEU A 1 3856 ? 218.637 165.017 219.092 1.00 25.97  ? 3856 LEU A CD2   1 
ATOM   16874 N  N     . SER A 1 3857 ? 219.331 166.536 214.146 1.00 24.97  ? 3857 SER A N     1 
ATOM   16875 C  CA    . SER A 1 3857 ? 220.416 167.276 213.505 1.00 20.98  ? 3857 SER A CA    1 
ATOM   16876 C  C     . SER A 1 3857 ? 219.880 168.454 212.699 1.00 18.78  ? 3857 SER A C     1 
ATOM   16877 O  O     . SER A 1 3857 ? 220.450 169.555 212.730 1.00 20.72  ? 3857 SER A O     1 
ATOM   16878 C  CB    . SER A 1 3857 ? 221.233 166.343 212.614 1.00 22.08  ? 3857 SER A CB    1 
ATOM   16879 O  OG    . SER A 1 3857 ? 220.486 165.944 211.478 1.00 31.03  ? 3857 SER A OG    1 
ATOM   16880 N  N     . ILE A 1 3858 ? 218.782 168.239 211.969 1.00 19.32  ? 3858 ILE A N     1 
ATOM   16881 C  CA    . ILE A 1 3858 ? 218.167 169.316 211.197 1.00 20.49  ? 3858 ILE A CA    1 
ATOM   16882 C  C     . ILE A 1 3858 ? 217.722 170.443 212.122 1.00 21.47  ? 3858 ILE A C     1 
ATOM   16883 O  O     . ILE A 1 3858 ? 217.944 171.626 211.840 1.00 26.43  ? 3858 ILE A O     1 
ATOM   16884 C  CB    . ILE A 1 3858 ? 216.992 168.771 210.365 1.00 23.39  ? 3858 ILE A CB    1 
ATOM   16885 C  CG1   . ILE A 1 3858 ? 217.505 168.030 209.131 1.00 25.72  ? 3858 ILE A CG1   1 
ATOM   16886 C  CG2   . ILE A 1 3858 ? 216.057 169.894 209.960 1.00 22.13  ? 3858 ILE A CG2   1 
ATOM   16887 C  CD1   . ILE A 1 3858 ? 216.410 167.372 208.321 1.00 24.46  ? 3858 ILE A CD1   1 
ATOM   16888 N  N     . ILE A 1 3859 ? 217.085 170.088 213.239 1.00 19.55  ? 3859 ILE A N     1 
ATOM   16889 C  CA    . ILE A 1 3859 ? 216.641 171.091 214.206 1.00 16.37  ? 3859 ILE A CA    1 
ATOM   16890 C  C     . ILE A 1 3859 ? 217.830 171.842 214.789 1.00 16.02  ? 3859 ILE A C     1 
ATOM   16891 O  O     . ILE A 1 3859 ? 217.782 173.064 214.960 1.00 16.36  ? 3859 ILE A O     1 
ATOM   16892 C  CB    . ILE A 1 3859 ? 215.788 170.437 215.310 1.00 17.94  ? 3859 ILE A CB    1 
ATOM   16893 C  CG1   . ILE A 1 3859 ? 214.562 169.748 214.712 1.00 21.42  ? 3859 ILE A CG1   1 
ATOM   16894 C  CG2   . ILE A 1 3859 ? 215.380 171.459 216.353 1.00 22.08  ? 3859 ILE A CG2   1 
ATOM   16895 C  CD1   . ILE A 1 3859 ? 213.699 169.048 215.734 1.00 23.39  ? 3859 ILE A CD1   1 
ATOM   16896 N  N     . THR A 1 3860 ? 218.910 171.128 215.110 1.00 17.88  ? 3860 THR A N     1 
ATOM   16897 C  CA    . THR A 1 3860 ? 220.081 171.779 215.686 1.00 15.41  ? 3860 THR A CA    1 
ATOM   16898 C  C     . THR A 1 3860 ? 220.693 172.781 214.716 1.00 18.55  ? 3860 THR A C     1 
ATOM   16899 O  O     . THR A 1 3860 ? 221.086 173.883 215.117 1.00 19.53  ? 3860 THR A O     1 
ATOM   16900 C  CB    . THR A 1 3860 ? 221.115 170.732 216.101 1.00 16.74  ? 3860 THR A CB    1 
ATOM   16901 O  OG1   . THR A 1 3860 ? 220.467 169.681 216.827 1.00 18.91  ? 3860 THR A OG1   1 
ATOM   16902 C  CG2   . THR A 1 3860 ? 222.183 171.360 216.979 1.00 16.96  ? 3860 THR A CG2   1 
ATOM   16903 N  N     . LYS A 1 3861 ? 220.784 172.420 213.434 1.00 17.91  ? 3861 LYS A N     1 
ATOM   16904 C  CA    . LYS A 1 3861 ? 221.331 173.348 212.447 1.00 15.12  ? 3861 LYS A CA    1 
ATOM   16905 C  C     . LYS A 1 3861 ? 220.400 174.539 212.232 1.00 14.87  ? 3861 LYS A C     1 
ATOM   16906 O  O     . LYS A 1 3861 ? 220.840 175.701 212.214 1.00 12.59  ? 3861 LYS A O     1 
ATOM   16907 C  CB    . LYS A 1 3861 ? 221.587 172.614 211.132 1.00 15.70  ? 3861 LYS A CB    1 
ATOM   16908 C  CG    . LYS A 1 3861 ? 222.257 173.457 210.063 1.00 20.25  ? 3861 LYS A CG    1 
ATOM   16909 C  CD    . LYS A 1 3861 ? 222.551 172.632 208.821 1.00 22.21  ? 3861 LYS A CD    1 
ATOM   16910 C  CE    . LYS A 1 3861 ? 223.213 173.471 207.744 1.00 27.19  ? 3861 LYS A CE    1 
ATOM   16911 N  NZ    . LYS A 1 3861 ? 223.499 172.671 206.522 1.00 30.72  ? 3861 LYS A NZ    1 
ATOM   16912 N  N     . ASP A 1 3862 ? 219.102 174.268 212.072 1.00 19.17  ? 3862 ASP A N     1 
ATOM   16913 C  CA    . ASP A 1 3862 ? 218.137 175.330 211.832 1.00 15.60  ? 3862 ASP A CA    1 
ATOM   16914 C  C     . ASP A 1 3862 ? 217.996 176.263 213.022 1.00 14.63  ? 3862 ASP A C     1 
ATOM   16915 O  O     . ASP A 1 3862 ? 217.651 177.428 212.831 1.00 15.02  ? 3862 ASP A O     1 
ATOM   16916 C  CB    . ASP A 1 3862 ? 216.778 174.735 211.470 1.00 16.92  ? 3862 ASP A CB    1 
ATOM   16917 C  CG    . ASP A 1 3862 ? 216.781 174.057 210.115 1.00 37.51  ? 3862 ASP A CG    1 
ATOM   16918 O  OD1   . ASP A 1 3862 ? 217.566 174.477 209.239 1.00 39.80  ? 3862 ASP A OD1   1 
ATOM   16919 O  OD2   . ASP A 1 3862 ? 215.996 173.107 209.922 1.00 45.21  ? 3862 ASP A OD2   1 
ATOM   16920 N  N     . LEU A 1 3863 ? 218.262 175.786 214.238 1.00 13.68  ? 3863 LEU A N     1 
ATOM   16921 C  CA    . LEU A 1 3863 ? 218.223 176.668 215.397 1.00 9.90   ? 3863 LEU A CA    1 
ATOM   16922 C  C     . LEU A 1 3863 ? 219.248 177.783 215.258 1.00 9.43   ? 3863 LEU A C     1 
ATOM   16923 O  O     . LEU A 1 3863 ? 218.911 178.968 215.359 1.00 11.72  ? 3863 LEU A O     1 
ATOM   16924 C  CB    . LEU A 1 3863 ? 218.463 175.864 216.674 1.00 10.94  ? 3863 LEU A CB    1 
ATOM   16925 C  CG    . LEU A 1 3863 ? 218.706 176.670 217.948 1.00 11.20  ? 3863 LEU A CG    1 
ATOM   16926 C  CD1   . LEU A 1 3863 ? 217.404 177.242 218.485 1.00 9.82   ? 3863 LEU A CD1   1 
ATOM   16927 C  CD2   . LEU A 1 3863 ? 219.402 175.818 218.994 1.00 9.65   ? 3863 LEU A CD2   1 
ATOM   16928 N  N     . PHE A 1 3864 ? 220.504 177.417 214.991 1.00 10.41  ? 3864 PHE A N     1 
ATOM   16929 C  CA    . PHE A 1 3864 ? 221.538 178.422 214.779 1.00 9.19   ? 3864 PHE A CA    1 
ATOM   16930 C  C     . PHE A 1 3864 ? 221.202 179.312 213.592 1.00 7.44   ? 3864 PHE A C     1 
ATOM   16931 O  O     . PHE A 1 3864 ? 221.334 180.540 213.670 1.00 7.63   ? 3864 PHE A O     1 
ATOM   16932 C  CB    . PHE A 1 3864 ? 222.895 177.751 214.567 1.00 7.98   ? 3864 PHE A CB    1 
ATOM   16933 C  CG    . PHE A 1 3864 ? 223.498 177.183 215.819 1.00 11.56  ? 3864 PHE A CG    1 
ATOM   16934 C  CD1   . PHE A 1 3864 ? 224.298 177.965 216.634 1.00 8.34   ? 3864 PHE A CD1   1 
ATOM   16935 C  CD2   . PHE A 1 3864 ? 223.280 175.864 216.173 1.00 13.72  ? 3864 PHE A CD2   1 
ATOM   16936 C  CE1   . PHE A 1 3864 ? 224.860 177.444 217.780 1.00 8.81   ? 3864 PHE A CE1   1 
ATOM   16937 C  CE2   . PHE A 1 3864 ? 223.839 175.338 217.320 1.00 10.74  ? 3864 PHE A CE2   1 
ATOM   16938 C  CZ    . PHE A 1 3864 ? 224.629 176.128 218.124 1.00 8.59   ? 3864 PHE A CZ    1 
ATOM   16939 N  N     . GLN A 1 3865 ? 220.749 178.712 212.485 1.00 8.22   ? 3865 GLN A N     1 
ATOM   16940 C  CA    . GLN A 1 3865 ? 220.478 179.504 211.288 1.00 7.59   ? 3865 GLN A CA    1 
ATOM   16941 C  C     . GLN A 1 3865 ? 219.386 180.543 211.538 1.00 8.35   ? 3865 GLN A C     1 
ATOM   16942 O  O     . GLN A 1 3865 ? 219.565 181.733 211.247 1.00 8.21   ? 3865 GLN A O     1 
ATOM   16943 C  CB    . GLN A 1 3865 ? 220.095 178.588 210.126 1.00 8.85   ? 3865 GLN A CB    1 
ATOM   16944 C  CG    . GLN A 1 3865 ? 219.987 179.311 208.795 1.00 7.70   ? 3865 GLN A CG    1 
ATOM   16945 C  CD    . GLN A 1 3865 ? 221.296 179.938 208.368 1.00 7.49   ? 3865 GLN A CD    1 
ATOM   16946 O  OE1   . GLN A 1 3865 ? 222.189 179.258 207.864 1.00 10.49  ? 3865 GLN A OE1   1 
ATOM   16947 N  NE2   . GLN A 1 3865 ? 221.421 181.243 208.571 1.00 8.77   ? 3865 GLN A NE2   1 
ATOM   16948 N  N     . VAL A 1 3866 ? 218.250 180.110 212.088 1.00 7.47   ? 3866 VAL A N     1 
ATOM   16949 C  CA    . VAL A 1 3866 ? 217.122 181.009 212.301 1.00 6.59   ? 3866 VAL A CA    1 
ATOM   16950 C  C     . VAL A 1 3866 ? 217.449 182.039 213.375 1.00 8.37   ? 3866 VAL A C     1 
ATOM   16951 O  O     . VAL A 1 3866 ? 217.061 183.208 213.266 1.00 11.64  ? 3866 VAL A O     1 
ATOM   16952 C  CB    . VAL A 1 3866 ? 215.858 180.202 212.648 1.00 8.34   ? 3866 VAL A CB    1 
ATOM   16953 C  CG1   . VAL A 1 3866 ? 214.732 181.122 213.087 1.00 10.53  ? 3866 VAL A CG1   1 
ATOM   16954 C  CG2   . VAL A 1 3866 ? 215.425 179.364 211.456 1.00 6.67   ? 3866 VAL A CG2   1 
ATOM   16955 N  N     . ALA A 1 3867 ? 218.162 181.630 214.429 1.00 8.17   ? 3867 ALA A N     1 
ATOM   16956 C  CA    . ALA A 1 3867 ? 218.555 182.584 215.457 1.00 6.79   ? 3867 ALA A CA    1 
ATOM   16957 C  C     . ALA A 1 3867 ? 219.426 183.684 214.870 1.00 8.09   ? 3867 ALA A C     1 
ATOM   16958 O  O     . ALA A 1 3867 ? 219.184 184.874 215.105 1.00 12.02  ? 3867 ALA A O     1 
ATOM   16959 C  CB    . ALA A 1 3867 ? 219.283 181.865 216.592 1.00 8.10   ? 3867 ALA A CB    1 
ATOM   16960 N  N     . PHE A 1 3868 ? 220.431 183.304 214.074 1.00 8.03   ? 3868 PHE A N     1 
ATOM   16961 C  CA    . PHE A 1 3868 ? 221.285 184.307 213.451 1.00 6.49   ? 3868 PHE A CA    1 
ATOM   16962 C  C     . PHE A 1 3868 ? 220.481 185.215 212.536 1.00 7.11   ? 3868 PHE A C     1 
ATOM   16963 O  O     . PHE A 1 3868 ? 220.631 186.438 212.576 1.00 9.19   ? 3868 PHE A O     1 
ATOM   16964 C  CB    . PHE A 1 3868 ? 222.415 183.645 212.669 1.00 6.36   ? 3868 PHE A CB    1 
ATOM   16965 C  CG    . PHE A 1 3868 ? 223.279 184.622 211.922 1.00 7.78   ? 3868 PHE A CG    1 
ATOM   16966 C  CD1   . PHE A 1 3868 ? 224.233 185.370 212.587 1.00 8.97   ? 3868 PHE A CD1   1 
ATOM   16967 C  CD2   . PHE A 1 3868 ? 223.122 184.807 210.561 1.00 6.78   ? 3868 PHE A CD2   1 
ATOM   16968 C  CE1   . PHE A 1 3868 ? 225.022 186.273 211.906 1.00 7.05   ? 3868 PHE A CE1   1 
ATOM   16969 C  CE2   . PHE A 1 3868 ? 223.907 185.712 209.877 1.00 6.93   ? 3868 PHE A CE2   1 
ATOM   16970 C  CZ    . PHE A 1 3868 ? 224.857 186.444 210.550 1.00 6.69   ? 3868 PHE A CZ    1 
ATOM   16971 N  N     . ASN A 1 3869 ? 219.614 184.634 211.704 1.00 6.76   ? 3869 ASN A N     1 
ATOM   16972 C  CA    . ASN A 1 3869 ? 218.844 185.445 210.767 1.00 5.44   ? 3869 ASN A CA    1 
ATOM   16973 C  C     . ASN A 1 3869 ? 217.986 186.467 211.501 1.00 6.87   ? 3869 ASN A C     1 
ATOM   16974 O  O     . ASN A 1 3869 ? 218.056 187.673 211.227 1.00 10.92  ? 3869 ASN A O     1 
ATOM   16975 C  CB    . ASN A 1 3869 ? 217.977 184.546 209.887 1.00 5.84   ? 3869 ASN A CB    1 
ATOM   16976 C  CG    . ASN A 1 3869 ? 218.786 183.758 208.878 1.00 9.14   ? 3869 ASN A CG    1 
ATOM   16977 O  OD1   . ASN A 1 3869 ? 219.998 183.932 208.765 1.00 13.83  ? 3869 ASN A OD1   1 
ATOM   16978 N  ND2   . ASN A 1 3869 ? 218.118 182.886 208.136 1.00 9.25   ? 3869 ASN A ND2   1 
ATOM   16979 N  N     . ARG A 1 3870 ? 217.191 186.000 212.468 1.00 6.90   ? 3870 ARG A N     1 
ATOM   16980 C  CA    . ARG A 1 3870 ? 216.269 186.888 213.167 1.00 7.38   ? 3870 ARG A CA    1 
ATOM   16981 C  C     . ARG A 1 3870 ? 217.011 187.951 213.965 1.00 6.39   ? 3870 ARG A C     1 
ATOM   16982 O  O     . ARG A 1 3870 ? 216.611 189.122 213.969 1.00 6.17   ? 3870 ARG A O     1 
ATOM   16983 C  CB    . ARG A 1 3870 ? 215.352 186.076 214.080 1.00 6.70   ? 3870 ARG A CB    1 
ATOM   16984 C  CG    . ARG A 1 3870 ? 214.399 185.154 213.345 1.00 7.72   ? 3870 ARG A CG    1 
ATOM   16985 C  CD    . ARG A 1 3870 ? 213.045 185.113 214.026 1.00 10.97  ? 3870 ARG A CD    1 
ATOM   16986 N  NE    . ARG A 1 3870 ? 212.150 184.147 213.400 1.00 20.34  ? 3870 ARG A NE    1 
ATOM   16987 C  CZ    . ARG A 1 3870 ? 210.926 183.877 213.827 1.00 20.58  ? 3870 ARG A CZ    1 
ATOM   16988 N  NH1   . ARG A 1 3870 ? 210.409 184.491 214.878 1.00 22.83  ? 3870 ARG A NH1   1 
ATOM   16989 N  NH2   . ARG A 1 3870 ? 210.203 182.962 213.187 1.00 19.37  ? 3870 ARG A NH2   1 
ATOM   16990 N  N     . VAL A 1 3871 ? 218.087 187.570 214.657 1.00 6.45   ? 3871 VAL A N     1 
ATOM   16991 C  CA    . VAL A 1 3871 ? 218.794 188.533 215.494 1.00 6.51   ? 3871 VAL A CA    1 
ATOM   16992 C  C     . VAL A 1 3871 ? 219.543 189.547 214.633 1.00 7.02   ? 3871 VAL A C     1 
ATOM   16993 O  O     . VAL A 1 3871 ? 219.519 190.752 214.907 1.00 6.48   ? 3871 VAL A O     1 
ATOM   16994 C  CB    . VAL A 1 3871 ? 219.732 187.801 216.470 1.00 6.69   ? 3871 VAL A CB    1 
ATOM   16995 C  CG1   . VAL A 1 3871 ? 220.669 188.778 217.146 1.00 6.41   ? 3871 VAL A CG1   1 
ATOM   16996 C  CG2   . VAL A 1 3871 ? 218.921 187.047 217.509 1.00 6.58   ? 3871 VAL A CG2   1 
ATOM   16997 N  N     . ALA A 1 3872 ? 220.205 189.080 213.569 1.00 8.23   ? 3872 ALA A N     1 
ATOM   16998 C  CA    . ALA A 1 3872 ? 220.992 189.963 212.721 1.00 4.65   ? 3872 ALA A CA    1 
ATOM   16999 C  C     . ALA A 1 3872 ? 220.131 190.851 211.838 1.00 6.50   ? 3872 ALA A C     1 
ATOM   17000 O  O     . ALA A 1 3872 ? 220.628 191.866 211.341 1.00 10.02  ? 3872 ALA A O     1 
ATOM   17001 C  CB    . ALA A 1 3872 ? 221.946 189.142 211.854 1.00 3.96   ? 3872 ALA A CB    1 
ATOM   17002 N  N     . ARG A 1 3873 ? 218.862 190.496 211.620 1.00 7.14   ? 3873 ARG A N     1 
ATOM   17003 C  CA    . ARG A 1 3873 ? 217.981 191.412 210.905 1.00 6.78   ? 3873 ARG A CA    1 
ATOM   17004 C  C     . ARG A 1 3873 ? 217.780 192.720 211.660 1.00 6.93   ? 3873 ARG A C     1 
ATOM   17005 O  O     . ARG A 1 3873 ? 217.404 193.725 211.047 1.00 7.62   ? 3873 ARG A O     1 
ATOM   17006 C  CB    . ARG A 1 3873 ? 216.630 190.749 210.637 1.00 10.42  ? 3873 ARG A CB    1 
ATOM   17007 C  CG    . ARG A 1 3873 ? 216.555 190.030 209.303 1.00 16.58  ? 3873 ARG A CG    1 
ATOM   17008 C  CD    . ARG A 1 3873 ? 217.115 190.890 208.185 1.00 18.46  ? 3873 ARG A CD    1 
ATOM   17009 N  NE    . ARG A 1 3873 ? 217.087 190.206 206.898 1.00 23.84  ? 3873 ARG A NE    1 
ATOM   17010 C  CZ    . ARG A 1 3873 ? 217.815 190.558 205.848 1.00 21.71  ? 3873 ARG A CZ    1 
ATOM   17011 N  NH1   . ARG A 1 3873 ? 218.642 191.589 205.896 1.00 17.31  ? 3873 ARG A NH1   1 
ATOM   17012 N  NH2   . ARG A 1 3873 ? 217.714 189.856 204.724 1.00 19.65  ? 3873 ARG A NH2   1 
ATOM   17013 N  N     . GLY A 1 3874 ? 218.022 192.730 212.968 1.00 6.16   ? 3874 GLY A N     1 
ATOM   17014 C  CA    . GLY A 1 3874 ? 217.892 193.937 213.758 1.00 5.52   ? 3874 GLY A CA    1 
ATOM   17015 C  C     . GLY A 1 3874 ? 219.201 194.399 214.363 1.00 6.85   ? 3874 GLY A C     1 
ATOM   17016 O  O     . GLY A 1 3874 ? 219.218 194.999 215.441 1.00 11.49  ? 3874 GLY A O     1 
ATOM   17017 N  N     . MET A 1 3875 ? 220.305 194.126 213.674 1.00 6.04   ? 3875 MET A N     1 
ATOM   17018 C  CA    . MET A 1 3875 ? 221.630 194.525 214.120 1.00 6.48   ? 3875 MET A CA    1 
ATOM   17019 C  C     . MET A 1 3875 ? 222.341 195.275 213.005 1.00 9.59   ? 3875 MET A C     1 
ATOM   17020 O  O     . MET A 1 3875 ? 222.028 195.107 211.824 1.00 10.77  ? 3875 MET A O     1 
ATOM   17021 C  CB    . MET A 1 3875 ? 222.479 193.315 214.533 1.00 5.72   ? 3875 MET A CB    1 
ATOM   17022 C  CG    . MET A 1 3875 ? 221.988 192.587 215.763 1.00 8.78   ? 3875 MET A CG    1 
ATOM   17023 S  SD    . MET A 1 3875 ? 222.984 191.131 216.131 1.00 28.20  ? 3875 MET A SD    1 
ATOM   17024 C  CE    . MET A 1 3875 ? 224.509 191.872 216.682 1.00 9.48   ? 3875 MET A CE    1 
ATOM   17025 N  N     . LEU A 1 3876 ? 223.297 196.113 213.394 1.00 8.56   ? 3876 LEU A N     1 
ATOM   17026 C  CA    . LEU A 1 3876 ? 224.180 196.732 212.422 1.00 5.96   ? 3876 LEU A CA    1 
ATOM   17027 C  C     . LEU A 1 3876 ? 225.041 195.667 211.752 1.00 8.97   ? 3876 LEU A C     1 
ATOM   17028 O  O     . LEU A 1 3876 ? 225.397 194.654 212.359 1.00 12.02  ? 3876 LEU A O     1 
ATOM   17029 C  CB    . LEU A 1 3876 ? 225.063 197.784 213.092 1.00 7.25   ? 3876 LEU A CB    1 
ATOM   17030 C  CG    . LEU A 1 3876 ? 224.337 198.836 213.934 1.00 7.50   ? 3876 LEU A CG    1 
ATOM   17031 C  CD1   . LEU A 1 3876 ? 225.319 199.589 214.812 1.00 10.56  ? 3876 LEU A CD1   1 
ATOM   17032 C  CD2   . LEU A 1 3876 ? 223.560 199.796 213.052 1.00 4.16   ? 3876 LEU A CD2   1 
ATOM   17033 N  N     . HIS A 1 3877 ? 225.366 195.900 210.478 1.00 7.40   ? 3877 HIS A N     1 
ATOM   17034 C  CA    . HIS A 1 3877 ? 226.091 194.894 209.709 1.00 6.15   ? 3877 HIS A CA    1 
ATOM   17035 C  C     . HIS A 1 3877 ? 227.478 194.638 210.284 1.00 7.06   ? 3877 HIS A C     1 
ATOM   17036 O  O     . HIS A 1 3877 ? 228.038 193.548 210.110 1.00 9.16   ? 3877 HIS A O     1 
ATOM   17037 C  CB    . HIS A 1 3877 ? 226.189 195.317 208.245 1.00 6.98   ? 3877 HIS A CB    1 
ATOM   17038 C  CG    . HIS A 1 3877 ? 226.601 194.209 207.330 1.00 8.85   ? 3877 HIS A CG    1 
ATOM   17039 N  ND1   . HIS A 1 3877 ? 227.920 193.950 207.021 1.00 8.16   ? 3877 HIS A ND1   1 
ATOM   17040 C  CD2   . HIS A 1 3877 ? 225.871 193.284 206.663 1.00 6.84   ? 3877 HIS A CD2   1 
ATOM   17041 C  CE1   . HIS A 1 3877 ? 227.983 192.916 206.202 1.00 10.82  ? 3877 HIS A CE1   1 
ATOM   17042 N  NE2   . HIS A 1 3877 ? 226.754 192.494 205.968 1.00 11.36  ? 3877 HIS A NE2   1 
ATOM   17043 N  N     . GLN A 1 3878 ? 228.053 195.628 210.969 1.00 9.47   ? 3878 GLN A N     1 
ATOM   17044 C  CA    . GLN A 1 3878 ? 229.380 195.449 211.549 1.00 7.53   ? 3878 GLN A CA    1 
ATOM   17045 C  C     . GLN A 1 3878 ? 229.371 194.428 212.679 1.00 11.85  ? 3878 GLN A C     1 
ATOM   17046 O  O     . GLN A 1 3878 ? 230.393 193.782 212.938 1.00 19.28  ? 3878 GLN A O     1 
ATOM   17047 C  CB    . GLN A 1 3878 ? 229.917 196.790 212.043 1.00 9.96   ? 3878 GLN A CB    1 
ATOM   17048 C  CG    . GLN A 1 3878 ? 228.882 197.649 212.747 1.00 12.46  ? 3878 GLN A CG    1 
ATOM   17049 C  CD    . GLN A 1 3878 ? 229.507 198.784 213.530 1.00 20.25  ? 3878 GLN A CD    1 
ATOM   17050 O  OE1   . GLN A 1 3878 ? 230.636 198.677 214.007 1.00 25.71  ? 3878 GLN A OE1   1 
ATOM   17051 N  NE2   . GLN A 1 3878 ? 228.775 199.883 213.664 1.00 18.26  ? 3878 GLN A NE2   1 
ATOM   17052 N  N     . ASP A 1 3879 ? 228.237 194.264 213.358 1.00 11.05  ? 3879 ASP A N     1 
ATOM   17053 C  CA    . ASP A 1 3879 ? 228.124 193.328 214.467 1.00 8.73   ? 3879 ASP A CA    1 
ATOM   17054 C  C     . ASP A 1 3879 ? 227.658 191.945 214.032 1.00 9.55   ? 3879 ASP A C     1 
ATOM   17055 O  O     . ASP A 1 3879 ? 227.568 191.039 214.873 1.00 14.60  ? 3879 ASP A O     1 
ATOM   17056 C  CB    . ASP A 1 3879 ? 227.164 193.889 215.517 1.00 9.69   ? 3879 ASP A CB    1 
ATOM   17057 C  CG    . ASP A 1 3879 ? 227.519 195.300 215.929 1.00 14.33  ? 3879 ASP A CG    1 
ATOM   17058 O  OD1   . ASP A 1 3879 ? 228.724 195.597 216.040 1.00 14.00  ? 3879 ASP A OD1   1 
ATOM   17059 O  OD2   . ASP A 1 3879 ? 226.595 196.111 216.141 1.00 16.94  ? 3879 ASP A OD2   1 
ATOM   17060 N  N     . HIS A 1 3880 ? 227.359 191.768 212.744 1.00 8.42   ? 3880 HIS A N     1 
ATOM   17061 C  CA    . HIS A 1 3880 ? 226.912 190.473 212.246 1.00 8.76   ? 3880 HIS A CA    1 
ATOM   17062 C  C     . HIS A 1 3880 ? 227.994 189.421 212.438 1.00 10.73  ? 3880 HIS A C     1 
ATOM   17063 O  O     . HIS A 1 3880 ? 227.724 188.303 212.894 1.00 15.39  ? 3880 HIS A O     1 
ATOM   17064 C  CB    . HIS A 1 3880 ? 226.539 190.593 210.768 1.00 7.83   ? 3880 HIS A CB    1 
ATOM   17065 C  CG    . HIS A 1 3880 ? 225.196 191.206 210.529 1.00 6.84   ? 3880 HIS A CG    1 
ATOM   17066 N  ND1   . HIS A 1 3880 ? 224.613 191.258 209.282 1.00 5.91   ? 3880 HIS A ND1   1 
ATOM   17067 C  CD2   . HIS A 1 3880 ? 224.331 191.814 211.374 1.00 7.17   ? 3880 HIS A CD2   1 
ATOM   17068 C  CE1   . HIS A 1 3880 ? 223.442 191.862 209.370 1.00 6.18   ? 3880 HIS A CE1   1 
ATOM   17069 N  NE2   . HIS A 1 3880 ? 223.246 192.209 210.629 1.00 6.57   ? 3880 HIS A NE2   1 
ATOM   17070 N  N     . ILE A 1 3881 ? 229.237 189.772 212.101 1.00 11.69  ? 3881 ILE A N     1 
ATOM   17071 C  CA    . ILE A 1 3881 ? 230.349 188.841 212.268 1.00 10.34  ? 3881 ILE A CA    1 
ATOM   17072 C  C     . ILE A 1 3881 ? 230.594 188.572 213.746 1.00 9.62   ? 3881 ILE A C     1 
ATOM   17073 O  O     . ILE A 1 3881 ? 230.942 187.453 214.137 1.00 10.24  ? 3881 ILE A O     1 
ATOM   17074 C  CB    . ILE A 1 3881 ? 231.609 189.379 211.561 1.00 10.51  ? 3881 ILE A CB    1 
ATOM   17075 C  CG1   . ILE A 1 3881 ? 232.789 188.423 211.756 1.00 11.32  ? 3881 ILE A CG1   1 
ATOM   17076 C  CG2   . ILE A 1 3881 ? 231.955 190.778 212.050 1.00 9.02   ? 3881 ILE A CG2   1 
ATOM   17077 C  CD1   . ILE A 1 3881 ? 232.543 187.032 211.216 1.00 8.39   ? 3881 ILE A CD1   1 
ATOM   17078 N  N     . THR A 1 3882 ? 230.402 189.588 214.591 1.00 9.78   ? 3882 THR A N     1 
ATOM   17079 C  CA    . THR A 1 3882 ? 230.574 189.396 216.026 1.00 8.84   ? 3882 THR A CA    1 
ATOM   17080 C  C     . THR A 1 3882 ? 229.578 188.381 216.571 1.00 9.50   ? 3882 THR A C     1 
ATOM   17081 O  O     . THR A 1 3882 ? 229.937 187.517 217.377 1.00 13.03  ? 3882 THR A O     1 
ATOM   17082 C  CB    . THR A 1 3882 ? 230.428 190.733 216.754 1.00 11.36  ? 3882 THR A CB    1 
ATOM   17083 O  OG1   . THR A 1 3882 ? 231.409 191.656 216.264 1.00 17.60  ? 3882 THR A OG1   1 
ATOM   17084 C  CG2   . THR A 1 3882 ? 230.621 190.549 218.248 1.00 11.26  ? 3882 THR A CG2   1 
ATOM   17085 N  N     . PHE A 1 3883 ? 228.318 188.471 216.141 1.00 8.14   ? 3883 PHE A N     1 
ATOM   17086 C  CA    . PHE A 1 3883 ? 227.321 187.501 216.589 1.00 5.21   ? 3883 PHE A CA    1 
ATOM   17087 C  C     . PHE A 1 3883 ? 227.593 186.115 216.013 1.00 7.36   ? 3883 PHE A C     1 
ATOM   17088 O  O     . PHE A 1 3883 ? 227.453 185.099 216.709 1.00 8.43   ? 3883 PHE A O     1 
ATOM   17089 C  CB    . PHE A 1 3883 ? 225.916 187.967 216.212 1.00 6.05   ? 3883 PHE A CB    1 
ATOM   17090 C  CG    . PHE A 1 3883 ? 224.824 187.136 216.821 1.00 5.71   ? 3883 PHE A CG    1 
ATOM   17091 C  CD1   . PHE A 1 3883 ? 224.892 186.748 218.146 1.00 5.53   ? 3883 PHE A CD1   1 
ATOM   17092 C  CD2   . PHE A 1 3883 ? 223.743 186.726 216.064 1.00 6.75   ? 3883 PHE A CD2   1 
ATOM   17093 C  CE1   . PHE A 1 3883 ? 223.896 185.979 218.708 1.00 5.67   ? 3883 PHE A CE1   1 
ATOM   17094 C  CE2   . PHE A 1 3883 ? 222.744 185.954 216.622 1.00 6.00   ? 3883 PHE A CE2   1 
ATOM   17095 C  CZ    . PHE A 1 3883 ? 222.819 185.582 217.946 1.00 4.82   ? 3883 PHE A CZ    1 
ATOM   17096 N  N     . ALA A 1 3884 ? 227.973 186.053 214.734 1.00 8.99   ? 3884 ALA A N     1 
ATOM   17097 C  CA    . ALA A 1 3884 ? 228.221 184.763 214.099 1.00 7.50   ? 3884 ALA A CA    1 
ATOM   17098 C  C     . ALA A 1 3884 ? 229.416 184.061 214.725 1.00 7.67   ? 3884 ALA A C     1 
ATOM   17099 O  O     . ALA A 1 3884 ? 229.449 182.829 214.803 1.00 8.81   ? 3884 ALA A O     1 
ATOM   17100 C  CB    . ALA A 1 3884 ? 228.431 184.947 212.598 1.00 8.46   ? 3884 ALA A CB    1 
ATOM   17101 N  N     . MET A 1 3885 ? 230.408 184.827 215.179 1.00 8.27   ? 3885 MET A N     1 
ATOM   17102 C  CA    . MET A 1 3885 ? 231.566 184.235 215.839 1.00 9.42   ? 3885 MET A CA    1 
ATOM   17103 C  C     . MET A 1 3885 ? 231.157 183.550 217.137 1.00 9.80   ? 3885 MET A C     1 
ATOM   17104 O  O     . MET A 1 3885 ? 231.597 182.432 217.434 1.00 9.82   ? 3885 MET A O     1 
ATOM   17105 C  CB    . MET A 1 3885 ? 232.610 185.321 216.102 1.00 13.15  ? 3885 MET A CB    1 
ATOM   17106 C  CG    . MET A 1 3885 ? 233.530 185.605 214.927 1.00 11.58  ? 3885 MET A CG    1 
ATOM   17107 S  SD    . MET A 1 3885 ? 234.720 184.296 214.607 1.00 26.93  ? 3885 MET A SD    1 
ATOM   17108 C  CE    . MET A 1 3885 ? 236.124 184.878 215.550 1.00 19.57  ? 3885 MET A CE    1 
ATOM   17109 N  N     . LEU A 1 3886 ? 230.300 184.209 217.919 1.00 10.08  ? 3886 LEU A N     1 
ATOM   17110 C  CA    . LEU A 1 3886 ? 229.813 183.611 219.157 1.00 8.63   ? 3886 LEU A CA    1 
ATOM   17111 C  C     . LEU A 1 3886 ? 228.960 182.382 218.878 1.00 6.57   ? 3886 LEU A C     1 
ATOM   17112 O  O     . LEU A 1 3886 ? 229.035 181.387 219.608 1.00 8.53   ? 3886 LEU A O     1 
ATOM   17113 C  CB    . LEU A 1 3886 ? 229.020 184.641 219.959 1.00 7.16   ? 3886 LEU A CB    1 
ATOM   17114 C  CG    . LEU A 1 3886 ? 229.791 185.872 220.426 1.00 6.23   ? 3886 LEU A CG    1 
ATOM   17115 C  CD1   . LEU A 1 3886 ? 228.877 186.779 221.218 1.00 8.32   ? 3886 LEU A CD1   1 
ATOM   17116 C  CD2   . LEU A 1 3886 ? 231.002 185.474 221.249 1.00 6.28   ? 3886 LEU A CD2   1 
ATOM   17117 N  N     . LEU A 1 3887 ? 228.133 182.436 217.833 1.00 6.77   ? 3887 LEU A N     1 
ATOM   17118 C  CA    . LEU A 1 3887 ? 227.335 181.266 217.474 1.00 7.10   ? 3887 LEU A CA    1 
ATOM   17119 C  C     . LEU A 1 3887 ? 228.225 180.100 217.054 1.00 7.21   ? 3887 LEU A C     1 
ATOM   17120 O  O     . LEU A 1 3887 ? 227.958 178.943 217.403 1.00 9.98   ? 3887 LEU A O     1 
ATOM   17121 C  CB    . LEU A 1 3887 ? 226.348 181.624 216.367 1.00 8.49   ? 3887 LEU A CB    1 
ATOM   17122 C  CG    . LEU A 1 3887 ? 225.188 182.523 216.795 1.00 4.91   ? 3887 LEU A CG    1 
ATOM   17123 C  CD1   . LEU A 1 3887 ? 224.327 182.881 215.603 1.00 5.63   ? 3887 LEU A CD1   1 
ATOM   17124 C  CD2   . LEU A 1 3887 ? 224.357 181.850 217.872 1.00 4.61   ? 3887 LEU A CD2   1 
ATOM   17125 N  N     . ALA A 1 3888 ? 229.288 180.388 216.301 1.00 7.97   ? 3888 ALA A N     1 
ATOM   17126 C  CA    . ALA A 1 3888 ? 230.234 179.348 215.914 1.00 9.33   ? 3888 ALA A CA    1 
ATOM   17127 C  C     . ALA A 1 3888 ? 230.936 178.764 217.131 1.00 8.69   ? 3888 ALA A C     1 
ATOM   17128 O  O     . ALA A 1 3888 ? 231.180 177.556 217.191 1.00 11.77  ? 3888 ALA A O     1 
ATOM   17129 C  CB    . ALA A 1 3888 ? 231.251 179.907 214.921 1.00 8.14   ? 3888 ALA A CB    1 
ATOM   17130 N  N     . ARG A 1 3889 ? 231.279 179.607 218.107 1.00 7.63   ? 3889 ARG A N     1 
ATOM   17131 C  CA    . ARG A 1 3889 ? 231.879 179.099 219.337 1.00 8.92   ? 3889 ARG A CA    1 
ATOM   17132 C  C     . ARG A 1 3889 ? 230.905 178.211 220.104 1.00 11.30  ? 3889 ARG A C     1 
ATOM   17133 O  O     . ARG A 1 3889 ? 231.301 177.181 220.666 1.00 15.41  ? 3889 ARG A O     1 
ATOM   17134 C  CB    . ARG A 1 3889 ? 232.353 180.258 220.212 1.00 9.99   ? 3889 ARG A CB    1 
ATOM   17135 C  CG    . ARG A 1 3889 ? 233.515 181.034 219.626 1.00 14.01  ? 3889 ARG A CG    1 
ATOM   17136 C  CD    . ARG A 1 3889 ? 234.326 181.703 220.715 1.00 18.51  ? 3889 ARG A CD    1 
ATOM   17137 N  NE    . ARG A 1 3889 ? 234.784 180.748 221.716 1.00 16.63  ? 3889 ARG A NE    1 
ATOM   17138 C  CZ    . ARG A 1 3889 ? 235.489 181.072 222.790 1.00 19.47  ? 3889 ARG A CZ    1 
ATOM   17139 N  NH1   . ARG A 1 3889 ? 235.840 182.323 223.034 1.00 19.66  ? 3889 ARG A NH1   1 
ATOM   17140 N  NH2   . ARG A 1 3889 ? 235.852 180.117 223.640 1.00 22.64  ? 3889 ARG A NH2   1 
ATOM   17141 N  N     . ILE A 1 3890 ? 229.628 178.600 220.148 1.00 9.95   ? 3890 ILE A N     1 
ATOM   17142 C  CA    . ILE A 1 3890 ? 228.621 177.781 220.818 1.00 7.93   ? 3890 ILE A CA    1 
ATOM   17143 C  C     . ILE A 1 3890 ? 228.507 176.421 220.140 1.00 9.58   ? 3890 ILE A C     1 
ATOM   17144 O  O     . ILE A 1 3890 ? 228.458 175.378 220.802 1.00 12.28  ? 3890 ILE A O     1 
ATOM   17145 C  CB    . ILE A 1 3890 ? 227.264 178.507 220.846 1.00 7.91   ? 3890 ILE A CB    1 
ATOM   17146 C  CG1   . ILE A 1 3890 ? 227.286 179.655 221.853 1.00 8.27   ? 3890 ILE A CG1   1 
ATOM   17147 C  CG2   . ILE A 1 3890 ? 226.143 177.539 221.187 1.00 10.94  ? 3890 ILE A CG2   1 
ATOM   17148 C  CD1   . ILE A 1 3890 ? 226.297 180.745 221.530 1.00 7.09   ? 3890 ILE A CD1   1 
ATOM   17149 N  N     . LYS A 1 3891 ? 228.462 176.415 218.806 1.00 9.55   ? 3891 LYS A N     1 
ATOM   17150 C  CA    . LYS A 1 3891 ? 228.426 175.151 218.077 1.00 10.19  ? 3891 LYS A CA    1 
ATOM   17151 C  C     . LYS A 1 3891 ? 229.682 174.318 218.296 1.00 16.51  ? 3891 LYS A C     1 
ATOM   17152 O  O     . LYS A 1 3891 ? 229.583 173.095 218.435 1.00 24.58  ? 3891 LYS A O     1 
ATOM   17153 C  CB    . LYS A 1 3891 ? 228.230 175.398 216.582 1.00 10.71  ? 3891 LYS A CB    1 
ATOM   17154 C  CG    . LYS A 1 3891 ? 227.746 174.173 215.828 1.00 11.88  ? 3891 LYS A CG    1 
ATOM   17155 C  CD    . LYS A 1 3891 ? 227.685 174.422 214.334 1.00 19.05  ? 3891 LYS A CD    1 
ATOM   17156 C  CE    . LYS A 1 3891 ? 226.954 173.296 213.627 1.00 26.68  ? 3891 LYS A CE    1 
ATOM   17157 N  NZ    . LYS A 1 3891 ? 225.580 173.106 214.167 1.00 33.12  ? 3891 LYS A NZ    1 
ATOM   17158 N  N     . LEU A 1 3892 ? 230.854 174.953 218.324 1.00 13.87  ? 3892 LEU A N     1 
ATOM   17159 C  CA    . LEU A 1 3892 ? 232.107 174.247 218.558 1.00 15.42  ? 3892 LEU A CA    1 
ATOM   17160 C  C     . LEU A 1 3892 ? 232.149 173.601 219.935 1.00 17.20  ? 3892 LEU A C     1 
ATOM   17161 O  O     . LEU A 1 3892 ? 232.630 172.470 220.070 1.00 16.80  ? 3892 LEU A O     1 
ATOM   17162 C  CB    . LEU A 1 3892 ? 233.281 175.212 218.391 1.00 16.03  ? 3892 LEU A CB    1 
ATOM   17163 C  CG    . LEU A 1 3892 ? 234.695 174.639 218.458 1.00 18.13  ? 3892 LEU A CG    1 
ATOM   17164 C  CD1   . LEU A 1 3892 ? 234.825 173.435 217.545 1.00 24.33  ? 3892 LEU A CD1   1 
ATOM   17165 C  CD2   . LEU A 1 3892 ? 235.713 175.705 218.097 1.00 18.82  ? 3892 LEU A CD2   1 
ATOM   17166 N  N     . LYS A 1 3893 ? 231.659 174.297 220.961 1.00 18.98  ? 3893 LYS A N     1 
ATOM   17167 C  CA    . LYS A 1 3893 ? 231.601 173.719 222.298 1.00 21.01  ? 3893 LYS A CA    1 
ATOM   17168 C  C     . LYS A 1 3893 ? 230.676 172.508 222.354 1.00 25.47  ? 3893 LYS A C     1 
ATOM   17169 O  O     . LYS A 1 3893 ? 230.892 171.605 223.171 1.00 33.13  ? 3893 LYS A O     1 
ATOM   17170 C  CB    . LYS A 1 3893 ? 231.152 174.779 223.304 1.00 16.32  ? 3893 LYS A CB    1 
ATOM   17171 C  CG    . LYS A 1 3893 ? 231.159 174.323 224.752 1.00 21.87  ? 3893 LYS A CG    1 
ATOM   17172 C  CD    . LYS A 1 3893 ? 230.774 175.456 225.685 1.00 28.03  ? 3893 LYS A CD    1 
ATOM   17173 C  CE    . LYS A 1 3893 ? 230.769 175.001 227.134 1.00 33.38  ? 3893 LYS A CE    1 
ATOM   17174 N  NZ    . LYS A 1 3893 ? 230.389 176.106 228.056 1.00 34.64  ? 3893 LYS A NZ    1 
ATOM   17175 N  N     . GLY A 1 3894 ? 229.663 172.464 221.496 1.00 20.99  ? 3894 GLY A N     1 
ATOM   17176 C  CA    . GLY A 1 3894 ? 228.705 171.383 221.456 1.00 23.67  ? 3894 GLY A CA    1 
ATOM   17177 C  C     . GLY A 1 3894 ? 229.086 170.195 220.604 1.00 29.25  ? 3894 GLY A C     1 
ATOM   17178 O  O     . GLY A 1 3894 ? 228.266 169.289 220.427 1.00 34.06  ? 3894 GLY A O     1 
ATOM   17179 N  N     . THR A 1 3895 ? 230.301 170.166 220.065 1.00 33.23  ? 3895 THR A N     1 
ATOM   17180 C  CA    . THR A 1 3895 ? 230.774 169.056 219.248 1.00 38.20  ? 3895 THR A CA    1 
ATOM   17181 C  C     . THR A 1 3895 ? 231.664 168.152 220.090 1.00 42.81  ? 3895 THR A C     1 
ATOM   17182 O  O     . THR A 1 3895 ? 232.635 168.620 220.694 1.00 43.35  ? 3895 THR A O     1 
ATOM   17183 C  CB    . THR A 1 3895 ? 231.540 169.561 218.024 1.00 38.69  ? 3895 THR A CB    1 
ATOM   17184 O  OG1   . THR A 1 3895 ? 230.679 170.381 217.223 1.00 24.44  ? 3895 THR A OG1   1 
ATOM   17185 C  CG2   . THR A 1 3895 ? 232.039 168.393 217.191 1.00 36.28  ? 3895 THR A CG2   1 
ATOM   17186 N  N     . VAL A 1 3896 ? 231.323 166.862 220.135 1.00 48.14  ? 3896 VAL A N     1 
ATOM   17187 C  CA    . VAL A 1 3896 ? 232.055 165.927 220.983 1.00 51.92  ? 3896 VAL A CA    1 
ATOM   17188 C  C     . VAL A 1 3896 ? 233.467 165.706 220.455 1.00 51.62  ? 3896 VAL A C     1 
ATOM   17189 O  O     . VAL A 1 3896 ? 234.441 165.745 221.217 1.00 52.88  ? 3896 VAL A O     1 
ATOM   17190 C  CB    . VAL A 1 3896 ? 231.284 164.601 221.104 1.00 56.68  ? 3896 VAL A CB    1 
ATOM   17191 C  CG1   . VAL A 1 3896 ? 231.967 163.680 222.102 1.00 57.29  ? 3896 VAL A CG1   1 
ATOM   17192 C  CG2   . VAL A 1 3896 ? 229.843 164.862 221.512 1.00 50.70  ? 3896 VAL A CG2   1 
ATOM   17193 N  N     . GLY A 1 3897 ? 233.605 165.474 219.153 1.00 47.34  ? 3897 GLY A N     1 
ATOM   17194 C  CA    . GLY A 1 3897 ? 234.902 165.184 218.576 1.00 46.03  ? 3897 GLY A CA    1 
ATOM   17195 C  C     . GLY A 1 3897 ? 235.707 166.416 218.222 1.00 45.03  ? 3897 GLY A C     1 
ATOM   17196 O  O     . GLY A 1 3897 ? 236.256 166.509 217.121 1.00 52.04  ? 3897 GLY A O     1 
ATOM   17197 N  N     . GLU A 1 3898 ? 235.785 167.373 219.147 1.00 43.28  ? 3898 GLU A N     1 
ATOM   17198 C  CA    . GLU A 1 3898 ? 236.530 168.602 218.934 1.00 48.63  ? 3898 GLU A CA    1 
ATOM   17199 C  C     . GLU A 1 3898 ? 237.226 169.020 220.220 1.00 44.65  ? 3898 GLU A C     1 
ATOM   17200 O  O     . GLU A 1 3898 ? 236.641 168.907 221.309 1.00 42.77  ? 3898 GLU A O     1 
ATOM   17201 C  CB    . GLU A 1 3898 ? 235.616 169.738 218.455 1.00 44.80  ? 3898 GLU A CB    1 
ATOM   17202 C  CG    . GLU A 1 3898 ? 235.449 169.812 216.947 1.00 45.36  ? 3898 GLU A CG    1 
ATOM   17203 C  CD    . GLU A 1 3898 ? 236.761 170.051 216.228 1.00 50.34  ? 3898 GLU A CD    1 
ATOM   17204 O  OE1   . GLU A 1 3898 ? 237.535 170.925 216.672 1.00 50.95  ? 3898 GLU A OE1   1 
ATOM   17205 O  OE2   . GLU A 1 3898 ? 237.019 169.365 215.218 1.00 52.37  ? 3898 GLU A OE2   1 
ATOM   17206 N  N     . PRO A 1 3899 ? 238.464 169.497 220.132 1.00 37.18  ? 3899 PRO A N     1 
ATOM   17207 C  CA    . PRO A 1 3899 ? 239.126 170.060 221.312 1.00 41.12  ? 3899 PRO A CA    1 
ATOM   17208 C  C     . PRO A 1 3899 ? 238.450 171.345 221.763 1.00 39.96  ? 3899 PRO A C     1 
ATOM   17209 O  O     . PRO A 1 3899 ? 237.796 172.046 220.989 1.00 48.28  ? 3899 PRO A O     1 
ATOM   17210 C  CB    . PRO A 1 3899 ? 240.557 170.325 220.832 1.00 41.32  ? 3899 PRO A CB    1 
ATOM   17211 C  CG    . PRO A 1 3899 ? 240.719 169.484 219.605 1.00 43.09  ? 3899 PRO A CG    1 
ATOM   17212 C  CD    . PRO A 1 3899 ? 239.366 169.425 218.973 1.00 39.69  ? 3899 PRO A CD    1 
ATOM   17213 N  N     . THR A 1 3900 ? 238.611 171.642 223.054 1.00 36.29  ? 3900 THR A N     1 
ATOM   17214 C  CA    . THR A 1 3900 ? 238.016 172.853 223.610 1.00 42.42  ? 3900 THR A CA    1 
ATOM   17215 C  C     . THR A 1 3900 ? 238.611 174.104 222.976 1.00 45.54  ? 3900 THR A C     1 
ATOM   17216 O  O     . THR A 1 3900 ? 237.906 175.101 222.779 1.00 47.77  ? 3900 THR A O     1 
ATOM   17217 C  CB    . THR A 1 3900 ? 238.201 172.885 225.126 1.00 48.22  ? 3900 THR A CB    1 
ATOM   17218 O  OG1   . THR A 1 3900 ? 239.598 172.900 225.441 1.00 45.81  ? 3900 THR A OG1   1 
ATOM   17219 C  CG2   . THR A 1 3900 ? 237.557 171.664 225.764 1.00 46.01  ? 3900 THR A CG2   1 
ATOM   17220 N  N     . TYR A 1 3901 ? 239.906 174.067 222.651 1.00 46.45  ? 3901 TYR A N     1 
ATOM   17221 C  CA    . TYR A 1 3901 ? 240.615 175.202 222.057 1.00 38.72  ? 3901 TYR A CA    1 
ATOM   17222 C  C     . TYR A 1 3901 ? 240.481 176.449 222.926 1.00 39.79  ? 3901 TYR A C     1 
ATOM   17223 O  O     . TYR A 1 3901 ? 240.353 177.567 222.424 1.00 41.06  ? 3901 TYR A O     1 
ATOM   17224 C  CB    . TYR A 1 3901 ? 240.135 175.473 220.629 1.00 33.84  ? 3901 TYR A CB    1 
ATOM   17225 C  CG    . TYR A 1 3901 ? 240.746 174.543 219.609 1.00 43.06  ? 3901 TYR A CG    1 
ATOM   17226 C  CD1   . TYR A 1 3901 ? 239.977 173.583 218.968 1.00 36.47  ? 3901 TYR A CD1   1 
ATOM   17227 C  CD2   . TYR A 1 3901 ? 242.098 174.610 219.306 1.00 47.53  ? 3901 TYR A CD2   1 
ATOM   17228 C  CE1   . TYR A 1 3901 ? 240.534 172.724 218.041 1.00 36.91  ? 3901 TYR A CE1   1 
ATOM   17229 C  CE2   . TYR A 1 3901 ? 242.666 173.755 218.381 1.00 48.23  ? 3901 TYR A CE2   1 
ATOM   17230 C  CZ    . TYR A 1 3901 ? 241.879 172.813 217.754 1.00 45.42  ? 3901 TYR A CZ    1 
ATOM   17231 O  OH    . TYR A 1 3901 ? 242.444 171.961 216.834 1.00 51.81  ? 3901 TYR A OH    1 
ATOM   17232 N  N     . ASP A 1 3902 ? 240.512 176.250 224.245 1.00 44.39  ? 3902 ASP A N     1 
ATOM   17233 C  CA    . ASP A 1 3902 ? 240.309 177.362 225.166 1.00 40.36  ? 3902 ASP A CA    1 
ATOM   17234 C  C     . ASP A 1 3902 ? 241.475 178.340 225.128 1.00 35.15  ? 3902 ASP A C     1 
ATOM   17235 O  O     . ASP A 1 3902 ? 241.267 179.556 225.071 1.00 35.35  ? 3902 ASP A O     1 
ATOM   17236 C  CB    . ASP A 1 3902 ? 240.100 176.833 226.585 1.00 43.68  ? 3902 ASP A CB    1 
ATOM   17237 C  CG    . ASP A 1 3902 ? 238.636 176.713 226.951 1.00 48.49  ? 3902 ASP A CG    1 
ATOM   17238 O  OD1   . ASP A 1 3902 ? 237.782 176.969 226.078 1.00 49.97  ? 3902 ASP A OD1   1 
ATOM   17239 O  OD2   . ASP A 1 3902 ? 238.339 176.362 228.112 1.00 54.67  ? 3902 ASP A OD2   1 
ATOM   17240 N  N     . ALA A 1 3903 ? 242.708 177.829 225.155 1.00 37.62  ? 3903 ALA A N     1 
ATOM   17241 C  CA    . ALA A 1 3903 ? 243.875 178.705 225.181 1.00 34.19  ? 3903 ALA A CA    1 
ATOM   17242 C  C     . ALA A 1 3903 ? 243.984 179.523 223.902 1.00 35.36  ? 3903 ALA A C     1 
ATOM   17243 O  O     . ALA A 1 3903 ? 244.358 180.703 223.939 1.00 37.67  ? 3903 ALA A O     1 
ATOM   17244 C  CB    . ALA A 1 3903 ? 245.144 177.881 225.403 1.00 37.63  ? 3903 ALA A CB    1 
ATOM   17245 N  N     . GLU A 1 3904 ? 243.666 178.912 222.759 1.00 33.16  ? 3904 GLU A N     1 
ATOM   17246 C  CA    . GLU A 1 3904 ? 243.718 179.628 221.490 1.00 28.79  ? 3904 GLU A CA    1 
ATOM   17247 C  C     . GLU A 1 3904 ? 242.750 180.805 221.488 1.00 33.15  ? 3904 GLU A C     1 
ATOM   17248 O  O     . GLU A 1 3904 ? 243.104 181.914 221.073 1.00 37.23  ? 3904 GLU A O     1 
ATOM   17249 C  CB    . GLU A 1 3904 ? 243.411 178.669 220.341 1.00 33.98  ? 3904 GLU A CB    1 
ATOM   17250 C  CG    . GLU A 1 3904 ? 244.631 177.963 219.778 1.00 40.74  ? 3904 GLU A CG    1 
ATOM   17251 C  CD    . GLU A 1 3904 ? 245.109 176.826 220.662 1.00 49.09  ? 3904 GLU A CD    1 
ATOM   17252 O  OE1   . GLU A 1 3904 ? 244.363 176.431 221.582 1.00 47.65  ? 3904 GLU A OE1   1 
ATOM   17253 O  OE2   . GLU A 1 3904 ? 246.231 176.328 220.434 1.00 44.32  ? 3904 GLU A OE2   1 
ATOM   17254 N  N     . PHE A 1 3905 ? 241.525 180.590 221.972 1.00 27.72  ? 3905 PHE A N     1 
ATOM   17255 C  CA    . PHE A 1 3905 ? 240.555 181.679 222.013 1.00 25.54  ? 3905 PHE A CA    1 
ATOM   17256 C  C     . PHE A 1 3905 ? 240.914 182.723 223.063 1.00 28.49  ? 3905 PHE A C     1 
ATOM   17257 O  O     . PHE A 1 3905 ? 240.660 183.915 222.855 1.00 33.56  ? 3905 PHE A O     1 
ATOM   17258 C  CB    . PHE A 1 3905 ? 239.153 181.125 222.256 1.00 26.94  ? 3905 PHE A CB    1 
ATOM   17259 C  CG    . PHE A 1 3905 ? 238.487 180.609 221.015 1.00 27.22  ? 3905 PHE A CG    1 
ATOM   17260 C  CD1   . PHE A 1 3905 ? 238.191 181.464 219.968 1.00 22.77  ? 3905 PHE A CD1   1 
ATOM   17261 C  CD2   . PHE A 1 3905 ? 238.172 179.268 220.886 1.00 30.15  ? 3905 PHE A CD2   1 
ATOM   17262 C  CE1   . PHE A 1 3905 ? 237.586 180.994 218.822 1.00 22.90  ? 3905 PHE A CE1   1 
ATOM   17263 C  CE2   . PHE A 1 3905 ? 237.567 178.792 219.742 1.00 26.94  ? 3905 PHE A CE2   1 
ATOM   17264 C  CZ    . PHE A 1 3905 ? 237.274 179.656 218.708 1.00 24.42  ? 3905 PHE A CZ    1 
ATOM   17265 N  N     . GLN A 1 3906 ? 241.497 182.305 224.190 1.00 30.54  ? 3906 GLN A N     1 
ATOM   17266 C  CA    . GLN A 1 3906 ? 241.956 183.277 225.179 1.00 30.12  ? 3906 GLN A CA    1 
ATOM   17267 C  C     . GLN A 1 3906 ? 243.038 184.178 224.602 1.00 31.66  ? 3906 GLN A C     1 
ATOM   17268 O  O     . GLN A 1 3906 ? 243.038 185.390 224.842 1.00 34.64  ? 3906 GLN A O     1 
ATOM   17269 C  CB    . GLN A 1 3906 ? 242.465 182.572 226.438 1.00 32.19  ? 3906 GLN A CB    1 
ATOM   17270 C  CG    . GLN A 1 3906 ? 241.407 181.788 227.195 1.00 45.79  ? 3906 GLN A CG    1 
ATOM   17271 C  CD    . GLN A 1 3906 ? 240.339 182.681 227.794 1.00 50.37  ? 3906 GLN A CD    1 
ATOM   17272 O  OE1   . GLN A 1 3906 ? 240.628 183.769 228.288 1.00 44.53  ? 3906 GLN A OE1   1 
ATOM   17273 N  NE2   . GLN A 1 3906 ? 239.092 182.223 227.752 1.00 55.49  ? 3906 GLN A NE2   1 
ATOM   17274 N  N     . HIS A 1 3907 ? 243.974 183.605 223.842 1.00 29.50  ? 3907 HIS A N     1 
ATOM   17275 C  CA    . HIS A 1 3907 ? 244.988 184.438 223.204 1.00 30.86  ? 3907 HIS A CA    1 
ATOM   17276 C  C     . HIS A 1 3907 ? 244.404 185.260 222.063 1.00 31.41  ? 3907 HIS A C     1 
ATOM   17277 O  O     . HIS A 1 3907 ? 244.912 186.342 221.756 1.00 35.60  ? 3907 HIS A O     1 
ATOM   17278 C  CB    . HIS A 1 3907 ? 246.146 183.586 222.693 1.00 36.07  ? 3907 HIS A CB    1 
ATOM   17279 C  CG    . HIS A 1 3907 ? 247.265 184.392 222.115 1.00 37.34  ? 3907 HIS A CG    1 
ATOM   17280 N  ND1   . HIS A 1 3907 ? 247.471 184.517 220.758 1.00 39.87  ? 3907 HIS A ND1   1 
ATOM   17281 C  CD2   . HIS A 1 3907 ? 248.226 185.136 222.711 1.00 40.27  ? 3907 HIS A CD2   1 
ATOM   17282 C  CE1   . HIS A 1 3907 ? 248.516 185.296 220.544 1.00 41.26  ? 3907 HIS A CE1   1 
ATOM   17283 N  NE2   . HIS A 1 3907 ? 248.993 185.684 221.712 1.00 45.27  ? 3907 HIS A NE2   1 
ATOM   17284 N  N     . PHE A 1 3908 ? 243.353 184.760 221.414 1.00 31.75  ? 3908 PHE A N     1 
ATOM   17285 C  CA    . PHE A 1 3908 ? 242.696 185.532 220.367 1.00 24.72  ? 3908 PHE A CA    1 
ATOM   17286 C  C     . PHE A 1 3908 ? 242.008 186.761 220.945 1.00 22.30  ? 3908 PHE A C     1 
ATOM   17287 O  O     . PHE A 1 3908 ? 241.995 187.827 220.320 1.00 23.84  ? 3908 PHE A O     1 
ATOM   17288 C  CB    . PHE A 1 3908 ? 241.692 184.648 219.627 1.00 23.67  ? 3908 PHE A CB    1 
ATOM   17289 C  CG    . PHE A 1 3908 ? 241.040 185.317 218.452 1.00 24.02  ? 3908 PHE A CG    1 
ATOM   17290 C  CD1   . PHE A 1 3908 ? 241.803 185.799 217.403 1.00 18.41  ? 3908 PHE A CD1   1 
ATOM   17291 C  CD2   . PHE A 1 3908 ? 239.665 185.456 218.393 1.00 23.82  ? 3908 PHE A CD2   1 
ATOM   17292 C  CE1   . PHE A 1 3908 ? 241.206 186.410 216.321 1.00 14.55  ? 3908 PHE A CE1   1 
ATOM   17293 C  CE2   . PHE A 1 3908 ? 239.065 186.066 217.310 1.00 19.24  ? 3908 PHE A CE2   1 
ATOM   17294 C  CZ    . PHE A 1 3908 ? 239.837 186.543 216.274 1.00 14.80  ? 3908 PHE A CZ    1 
ATOM   17295 N  N     . LEU A 1 3909 ? 241.432 186.631 222.140 1.00 25.47  ? 3909 LEU A N     1 
ATOM   17296 C  CA    . LEU A 1 3909 ? 240.673 187.732 222.722 1.00 29.40  ? 3909 LEU A CA    1 
ATOM   17297 C  C     . LEU A 1 3909 ? 241.551 188.659 223.552 1.00 32.94  ? 3909 LEU A C     1 
ATOM   17298 O  O     . LEU A 1 3909 ? 241.433 189.884 223.450 1.00 36.27  ? 3909 LEU A O     1 
ATOM   17299 C  CB    . LEU A 1 3909 ? 239.528 187.184 223.573 1.00 25.73  ? 3909 LEU A CB    1 
ATOM   17300 C  CG    . LEU A 1 3909 ? 238.446 186.432 222.801 1.00 25.18  ? 3909 LEU A CG    1 
ATOM   17301 C  CD1   . LEU A 1 3909 ? 237.435 185.813 223.748 1.00 32.47  ? 3909 LEU A CD1   1 
ATOM   17302 C  CD2   . LEU A 1 3909 ? 237.767 187.358 221.815 1.00 21.33  ? 3909 LEU A CD2   1 
ATOM   17303 N  N     . ARG A 1 3910 ? 242.431 188.101 224.380 1.00 35.00  ? 3910 ARG A N     1 
ATOM   17304 C  CA    . ARG A 1 3910 ? 243.257 188.876 225.297 1.00 34.41  ? 3910 ARG A CA    1 
ATOM   17305 C  C     . ARG A 1 3910 ? 244.740 188.644 225.039 1.00 42.16  ? 3910 ARG A C     1 
ATOM   17306 O  O     . ARG A 1 3910 ? 245.550 188.597 225.966 1.00 51.14  ? 3910 ARG A O     1 
ATOM   17307 C  CB    . ARG A 1 3910 ? 242.910 188.548 226.747 1.00 38.85  ? 3910 ARG A CB    1 
ATOM   17308 C  CG    . ARG A 1 3910 ? 241.527 188.998 227.174 1.00 37.89  ? 3910 ARG A CG    1 
ATOM   17309 C  CD    . ARG A 1 3910 ? 241.260 188.633 228.623 1.00 47.76  ? 3910 ARG A CD    1 
ATOM   17310 N  NE    . ARG A 1 3910 ? 239.927 189.037 229.052 1.00 58.10  ? 3910 ARG A NE    1 
ATOM   17311 C  CZ    . ARG A 1 3910 ? 239.421 188.789 230.251 1.00 59.02  ? 3910 ARG A CZ    1 
ATOM   17312 N  NH1   . ARG A 1 3910 ? 240.110 188.136 231.171 1.00 55.17  ? 3910 ARG A NH1   1 
ATOM   17313 N  NH2   . ARG A 1 3910 ? 238.189 189.206 230.533 1.00 54.69  ? 3910 ARG A NH2   1 
ATOM   17314 N  N     . GLY A 1 3911 ? 245.117 188.493 223.767 1.00 42.65  ? 3911 GLY A N     1 
ATOM   17315 C  CA    . GLY A 1 3911 ? 246.520 188.340 223.434 1.00 45.69  ? 3911 GLY A CA    1 
ATOM   17316 C  C     . GLY A 1 3911 ? 247.322 189.620 223.495 1.00 53.64  ? 3911 GLY A C     1 
ATOM   17317 O  O     . GLY A 1 3911 ? 248.549 189.563 223.611 1.00 58.57  ? 3911 GLY A O     1 
ATOM   17318 N  N     . ASN A 1 3912 ? 246.658 190.770 223.427 1.00 53.15  ? 3912 ASN A N     1 
ATOM   17319 C  CA    . ASN A 1 3912 ? 247.318 192.064 223.494 1.00 53.45  ? 3912 ASN A CA    1 
ATOM   17320 C  C     . ASN A 1 3912 ? 247.596 192.517 224.922 1.00 64.99  ? 3912 ASN A C     1 
ATOM   17321 O  O     . ASN A 1 3912 ? 248.148 193.604 225.117 1.00 69.67  ? 3912 ASN A O     1 
ATOM   17322 C  CB    . ASN A 1 3912 ? 246.482 193.117 222.753 1.00 56.29  ? 3912 ASN A CB    1 
ATOM   17323 C  CG    . ASN A 1 3912 ? 245.104 193.323 223.367 1.00 65.54  ? 3912 ASN A CG    1 
ATOM   17324 O  OD1   . ASN A 1 3912 ? 244.782 192.772 224.419 1.00 66.88  ? 3912 ASN A OD1   1 
ATOM   17325 N  ND2   . ASN A 1 3912 ? 244.280 194.121 222.698 1.00 59.61  ? 3912 ASN A ND2   1 
ATOM   17326 N  N     . GLU A 1 3913 ? 247.223 191.714 225.916 1.00 62.69  ? 3913 GLU A N     1 
ATOM   17327 C  CA    . GLU A 1 3913 ? 247.473 192.021 227.317 1.00 64.08  ? 3913 GLU A CA    1 
ATOM   17328 C  C     . GLU A 1 3913 ? 248.751 191.383 227.843 1.00 69.36  ? 3913 GLU A C     1 
ATOM   17329 O  O     . GLU A 1 3913 ? 249.030 191.487 229.043 1.00 73.56  ? 3913 GLU A O     1 
ATOM   17330 C  CB    . GLU A 1 3913 ? 246.283 191.572 228.172 1.00 62.18  ? 3913 GLU A CB    1 
ATOM   17331 C  CG    . GLU A 1 3913 ? 244.941 192.092 227.688 1.00 55.19  ? 3913 GLU A CG    1 
ATOM   17332 C  CD    . GLU A 1 3913 ? 243.814 191.787 228.657 1.00 60.04  ? 3913 GLU A CD    1 
ATOM   17333 O  OE1   . GLU A 1 3913 ? 244.081 191.155 229.700 1.00 59.45  ? 3913 GLU A OE1   1 
ATOM   17334 O  OE2   . GLU A 1 3913 ? 242.663 192.181 228.377 1.00 61.92  ? 3913 GLU A OE2   1 
ATOM   17335 N  N     . ILE A 1 3914 ? 249.529 190.725 226.988 1.00 67.33  ? 3914 ILE A N     1 
ATOM   17336 C  CA    . ILE A 1 3914 ? 250.768 190.086 227.416 1.00 71.81  ? 3914 ILE A CA    1 
ATOM   17337 C  C     . ILE A 1 3914 ? 251.853 191.145 227.555 1.00 78.31  ? 3914 ILE A C     1 
ATOM   17338 O  O     . ILE A 1 3914 ? 252.118 191.909 226.619 1.00 72.11  ? 3914 ILE A O     1 
ATOM   17339 C  CB    . ILE A 1 3914 ? 251.187 188.990 226.422 1.00 67.67  ? 3914 ILE A CB    1 
ATOM   17340 C  CG1   . ILE A 1 3914 ? 250.093 187.928 226.305 1.00 66.64  ? 3914 ILE A CG1   1 
ATOM   17341 C  CG2   . ILE A 1 3914 ? 252.500 188.356 226.849 1.00 66.55  ? 3914 ILE A CG2   1 
ATOM   17342 C  CD1   . ILE A 1 3914 ? 249.793 187.216 227.604 1.00 67.64  ? 3914 ILE A CD1   1 
ATOM   17343 N  N     . VAL A 1 3915 ? 252.487 191.189 228.727 1.00 86.55  ? 3915 VAL A N     1 
ATOM   17344 C  CA    . VAL A 1 3915 ? 253.542 192.163 228.977 1.00 88.50  ? 3915 VAL A CA    1 
ATOM   17345 C  C     . VAL A 1 3915 ? 254.790 191.764 228.203 1.00 84.76  ? 3915 VAL A C     1 
ATOM   17346 O  O     . VAL A 1 3915 ? 255.232 190.609 228.255 1.00 82.49  ? 3915 VAL A O     1 
ATOM   17347 C  CB    . VAL A 1 3915 ? 253.831 192.270 230.481 1.00 89.20  ? 3915 VAL A CB    1 
ATOM   17348 C  CG1   . VAL A 1 3915 ? 254.796 193.414 230.757 1.00 86.05  ? 3915 VAL A CG1   1 
ATOM   17349 C  CG2   . VAL A 1 3915 ? 252.537 192.452 231.259 1.00 79.80  ? 3915 VAL A CG2   1 
ATOM   17350 N  N     . LEU A 1 3916 ? 255.364 192.719 227.478 1.00 83.55  ? 3916 LEU A N     1 
ATOM   17351 C  CA    . LEU A 1 3916 ? 256.557 192.494 226.674 1.00 88.68  ? 3916 LEU A CA    1 
ATOM   17352 C  C     . LEU A 1 3916 ? 257.690 193.394 227.167 1.00 101.72 ? 3916 LEU A C     1 
ATOM   17353 O  O     . LEU A 1 3916 ? 257.570 194.089 228.179 1.00 104.40 ? 3916 LEU A O     1 
ATOM   17354 C  CB    . LEU A 1 3916 ? 256.261 192.729 225.192 1.00 81.28  ? 3916 LEU A CB    1 
ATOM   17355 C  CG    . LEU A 1 3916 ? 255.478 191.627 224.477 1.00 81.47  ? 3916 LEU A CG    1 
ATOM   17356 C  CD1   . LEU A 1 3916 ? 255.277 191.980 223.013 1.00 69.70  ? 3916 LEU A CD1   1 
ATOM   17357 C  CD2   . LEU A 1 3916 ? 256.185 190.288 224.622 1.00 75.79  ? 3916 LEU A CD2   1 
ATOM   17358 N  N     . SER A 1 3917 ? 258.800 193.373 226.432 1.00 106.14 ? 3917 SER A N     1 
ATOM   17359 C  CA    . SER A 1 3917 ? 259.970 194.168 226.769 1.00 107.96 ? 3917 SER A CA    1 
ATOM   17360 C  C     . SER A 1 3917 ? 260.710 194.517 225.487 1.00 109.60 ? 3917 SER A C     1 
ATOM   17361 O  O     . SER A 1 3917 ? 260.445 193.959 224.419 1.00 106.80 ? 3917 SER A O     1 
ATOM   17362 C  CB    . SER A 1 3917 ? 260.890 193.426 227.747 1.00 106.02 ? 3917 SER A CB    1 
ATOM   17363 O  OG    . SER A 1 3917 ? 260.210 193.106 228.947 1.00 105.10 ? 3917 SER A OG    1 
ATOM   17364 N  N     . ALA A 1 3918 ? 261.645 195.464 225.604 1.00 110.88 ? 3918 ALA A N     1 
ATOM   17365 C  CA    . ALA A 1 3918 ? 262.434 195.873 224.446 1.00 107.04 ? 3918 ALA A CA    1 
ATOM   17366 C  C     . ALA A 1 3918 ? 263.275 194.719 223.916 1.00 109.09 ? 3918 ALA A C     1 
ATOM   17367 O  O     . ALA A 1 3918 ? 263.403 194.541 222.698 1.00 103.90 ? 3918 ALA A O     1 
ATOM   17368 C  CB    . ALA A 1 3918 ? 263.321 197.063 224.808 1.00 92.21  ? 3918 ALA A CB    1 
ATOM   17369 N  N     . GLY A 1 3919 ? 263.857 193.922 224.815 1.00 111.54 ? 3919 GLY A N     1 
ATOM   17370 C  CA    . GLY A 1 3919 ? 264.671 192.797 224.393 1.00 107.76 ? 3919 GLY A CA    1 
ATOM   17371 C  C     . GLY A 1 3919 ? 263.881 191.640 223.820 1.00 99.99  ? 3919 GLY A C     1 
ATOM   17372 O  O     . GLY A 1 3919 ? 264.450 190.812 223.102 1.00 91.70  ? 3919 GLY A O     1 
ATOM   17373 N  N     . SER A 1 3920 ? 262.583 191.562 224.124 1.00 103.59 ? 3920 SER A N     1 
ATOM   17374 C  CA    . SER A 1 3920 ? 261.764 190.477 223.592 1.00 98.99  ? 3920 SER A CA    1 
ATOM   17375 C  C     . SER A 1 3920 ? 261.658 190.557 222.075 1.00 96.03  ? 3920 SER A C     1 
ATOM   17376 O  O     . SER A 1 3920 ? 261.678 189.526 221.390 1.00 91.59  ? 3920 SER A O     1 
ATOM   17377 C  CB    . SER A 1 3920 ? 260.374 190.503 224.229 1.00 93.82  ? 3920 SER A CB    1 
ATOM   17378 O  OG    . SER A 1 3920 ? 260.439 190.207 225.612 1.00 91.13  ? 3920 SER A OG    1 
ATOM   17379 N  N     . THR A 1 3921 ? 261.543 191.762 221.534 1.00 94.52  ? 3921 THR A N     1 
ATOM   17380 C  CA    . THR A 1 3921 ? 261.423 191.933 220.091 1.00 88.59  ? 3921 THR A CA    1 
ATOM   17381 C  C     . THR A 1 3921 ? 262.749 191.612 219.414 1.00 84.26  ? 3921 THR A C     1 
ATOM   17382 O  O     . THR A 1 3921 ? 263.750 192.287 219.687 1.00 84.21  ? 3921 THR A O     1 
ATOM   17383 C  CB    . THR A 1 3921 ? 260.995 193.360 219.765 1.00 86.98  ? 3921 THR A CB    1 
ATOM   17384 O  OG1   . THR A 1 3921 ? 259.768 193.661 220.443 1.00 81.29  ? 3921 THR A OG1   1 
ATOM   17385 C  CG2   . THR A 1 3921 ? 260.800 193.532 218.269 1.00 75.91  ? 3921 THR A CG2   1 
ATOM   17386 N  N     . PRO A 1 3922 ? 262.809 190.614 218.534 1.00 85.69  ? 3922 PRO A N     1 
ATOM   17387 C  CA    . PRO A 1 3922 ? 264.075 190.251 217.886 1.00 86.91  ? 3922 PRO A CA    1 
ATOM   17388 C  C     . PRO A 1 3922 ? 264.312 190.883 216.523 1.00 87.95  ? 3922 PRO A C     1 
ATOM   17389 O  O     . PRO A 1 3922 ? 265.323 190.555 215.890 1.00 91.02  ? 3922 PRO A O     1 
ATOM   17390 C  CB    . PRO A 1 3922 ? 263.946 188.728 217.761 1.00 86.66  ? 3922 PRO A CB    1 
ATOM   17391 C  CG    . PRO A 1 3922 ? 262.477 188.485 217.611 1.00 89.04  ? 3922 PRO A CG    1 
ATOM   17392 C  CD    . PRO A 1 3922 ? 261.733 189.668 218.198 1.00 90.20  ? 3922 PRO A CD    1 
ATOM   17393 N  N     . ARG A 1 3923 ? 263.427 191.768 216.062 1.00 86.35  ? 3923 ARG A N     1 
ATOM   17394 C  CA    . ARG A 1 3923 ? 263.608 192.500 214.807 1.00 77.92  ? 3923 ARG A CA    1 
ATOM   17395 C  C     . ARG A 1 3923 ? 263.748 191.517 213.636 1.00 75.11  ? 3923 ARG A C     1 
ATOM   17396 O  O     . ARG A 1 3923 ? 264.817 191.320 213.053 1.00 77.04  ? 3923 ARG A O     1 
ATOM   17397 C  CB    . ARG A 1 3923 ? 264.787 193.486 214.939 1.00 76.49  ? 3923 ARG A CB    1 
ATOM   17398 C  CG    . ARG A 1 3923 ? 265.494 193.996 213.677 1.00 76.33  ? 3923 ARG A CG    1 
ATOM   17399 C  CD    . ARG A 1 3923 ? 264.573 194.840 212.804 1.00 78.74  ? 3923 ARG A CD    1 
ATOM   17400 N  NE    . ARG A 1 3923 ? 265.039 194.961 211.425 1.00 78.90  ? 3923 ARG A NE    1 
ATOM   17401 C  CZ    . ARG A 1 3923 ? 265.220 193.952 210.582 1.00 81.17  ? 3923 ARG A CZ    1 
ATOM   17402 N  NH1   . ARG A 1 3923 ? 264.980 192.701 210.937 1.00 83.67  ? 3923 ARG A NH1   1 
ATOM   17403 N  NH2   . ARG A 1 3923 ? 265.655 194.205 209.351 1.00 79.81  ? 3923 ARG A NH2   1 
ATOM   17404 N  N     . ILE A 1 3924 ? 262.641 190.824 213.363 1.00 70.66  ? 3924 ILE A N     1 
ATOM   17405 C  CA    . ILE A 1 3924 ? 262.588 189.895 212.240 1.00 67.55  ? 3924 ILE A CA    1 
ATOM   17406 C  C     . ILE A 1 3924 ? 262.693 190.682 210.940 1.00 70.40  ? 3924 ILE A C     1 
ATOM   17407 O  O     . ILE A 1 3924 ? 262.074 191.743 210.787 1.00 68.63  ? 3924 ILE A O     1 
ATOM   17408 C  CB    . ILE A 1 3924 ? 261.293 189.067 212.270 1.00 66.97  ? 3924 ILE A CB    1 
ATOM   17409 C  CG1   . ILE A 1 3924 ? 261.207 188.195 213.526 1.00 71.53  ? 3924 ILE A CG1   1 
ATOM   17410 C  CG2   . ILE A 1 3924 ? 261.184 188.194 211.028 1.00 65.95  ? 3924 ILE A CG2   1 
ATOM   17411 C  CD1   . ILE A 1 3924 ? 260.552 188.881 214.706 1.00 70.07  ? 3924 ILE A CD1   1 
ATOM   17412 N  N     . GLN A 1 3925 ? 263.489 190.173 210.001 1.00 72.92  ? 3925 GLN A N     1 
ATOM   17413 C  CA    . GLN A 1 3925 ? 263.620 190.828 208.707 1.00 73.36  ? 3925 GLN A CA    1 
ATOM   17414 C  C     . GLN A 1 3925 ? 262.299 190.771 207.953 1.00 72.29  ? 3925 GLN A C     1 
ATOM   17415 O  O     . GLN A 1 3925 ? 261.646 189.725 207.893 1.00 69.07  ? 3925 GLN A O     1 
ATOM   17416 C  CB    . GLN A 1 3925 ? 264.732 190.170 207.891 1.00 76.86  ? 3925 GLN A CB    1 
ATOM   17417 C  CG    . GLN A 1 3925 ? 265.137 190.953 206.652 1.00 79.10  ? 3925 GLN A CG    1 
ATOM   17418 C  CD    . GLN A 1 3925 ? 264.485 190.435 205.389 1.00 84.40  ? 3925 GLN A CD    1 
ATOM   17419 O  OE1   . GLN A 1 3925 ? 263.735 189.459 205.420 1.00 82.97  ? 3925 GLN A OE1   1 
ATOM   17420 N  NE2   . GLN A 1 3925 ? 264.768 191.086 204.267 1.00 83.14  ? 3925 GLN A NE2   1 
ATOM   17421 N  N     . GLY A 1 3926 ? 261.903 191.904 207.376 1.00 75.26  ? 3926 GLY A N     1 
ATOM   17422 C  CA    . GLY A 1 3926 ? 260.649 191.999 206.664 1.00 67.01  ? 3926 GLY A CA    1 
ATOM   17423 C  C     . GLY A 1 3926 ? 259.424 192.156 207.536 1.00 60.53  ? 3926 GLY A C     1 
ATOM   17424 O  O     . GLY A 1 3926 ? 258.305 192.146 207.007 1.00 57.63  ? 3926 GLY A O     1 
ATOM   17425 N  N     . LEU A 1 3927 ? 259.592 192.299 208.848 1.00 58.07  ? 3927 LEU A N     1 
ATOM   17426 C  CA    . LEU A 1 3927 ? 258.486 192.439 209.783 1.00 48.94  ? 3927 LEU A CA    1 
ATOM   17427 C  C     . LEU A 1 3927 ? 258.593 193.780 210.492 1.00 52.92  ? 3927 LEU A C     1 
ATOM   17428 O  O     . LEU A 1 3927 ? 259.665 194.135 210.992 1.00 61.06  ? 3927 LEU A O     1 
ATOM   17429 C  CB    . LEU A 1 3927 ? 258.484 191.300 210.807 1.00 54.47  ? 3927 LEU A CB    1 
ATOM   17430 C  CG    . LEU A 1 3927 ? 257.515 190.141 210.573 1.00 49.65  ? 3927 LEU A CG    1 
ATOM   17431 C  CD1   . LEU A 1 3927 ? 257.784 189.473 209.236 1.00 50.95  ? 3927 LEU A CD1   1 
ATOM   17432 C  CD2   . LEU A 1 3927 ? 257.610 189.132 211.706 1.00 43.69  ? 3927 LEU A CD2   1 
ATOM   17433 N  N     . THR A 1 3928 ? 257.488 194.517 210.537 1.00 55.82  ? 3928 THR A N     1 
ATOM   17434 C  CA    . THR A 1 3928 ? 257.473 195.786 211.246 1.00 56.30  ? 3928 THR A CA    1 
ATOM   17435 C  C     . THR A 1 3928 ? 257.485 195.546 212.756 1.00 53.06  ? 3928 THR A C     1 
ATOM   17436 O  O     . THR A 1 3928 ? 257.399 194.413 213.237 1.00 48.04  ? 3928 THR A O     1 
ATOM   17437 C  CB    . THR A 1 3928 ? 256.252 196.615 210.848 1.00 55.03  ? 3928 THR A CB    1 
ATOM   17438 O  OG1   . THR A 1 3928 ? 255.057 195.911 211.201 1.00 57.06  ? 3928 THR A OG1   1 
ATOM   17439 C  CG2   . THR A 1 3928 ? 256.253 196.875 209.350 1.00 47.76  ? 3928 THR A CG2   1 
ATOM   17440 N  N     . VAL A 1 3929 ? 257.596 196.643 213.509 1.00 60.26  ? 3929 VAL A N     1 
ATOM   17441 C  CA    . VAL A 1 3929 ? 257.720 196.539 214.962 1.00 56.64  ? 3929 VAL A CA    1 
ATOM   17442 C  C     . VAL A 1 3929 ? 256.474 195.900 215.562 1.00 57.67  ? 3929 VAL A C     1 
ATOM   17443 O  O     . VAL A 1 3929 ? 256.562 194.963 216.362 1.00 61.71  ? 3929 VAL A O     1 
ATOM   17444 C  CB    . VAL A 1 3929 ? 257.997 197.924 215.577 1.00 58.87  ? 3929 VAL A CB    1 
ATOM   17445 C  CG1   . VAL A 1 3929 ? 258.012 197.835 217.094 1.00 58.09  ? 3929 VAL A CG1   1 
ATOM   17446 C  CG2   . VAL A 1 3929 ? 259.315 198.477 215.059 1.00 58.41  ? 3929 VAL A CG2   1 
ATOM   17447 N  N     . GLU A 1 3930 ? 255.293 196.392 215.177 1.00 59.62  ? 3930 GLU A N     1 
ATOM   17448 C  CA    . GLU A 1 3930 ? 254.057 195.837 215.722 1.00 60.30  ? 3930 GLU A CA    1 
ATOM   17449 C  C     . GLU A 1 3930 ? 253.859 194.386 215.302 1.00 52.37  ? 3930 GLU A C     1 
ATOM   17450 O  O     . GLU A 1 3930 ? 253.397 193.569 216.107 1.00 54.68  ? 3930 GLU A O     1 
ATOM   17451 C  CB    . GLU A 1 3930 ? 252.861 196.701 215.311 1.00 60.33  ? 3930 GLU A CB    1 
ATOM   17452 C  CG    . GLU A 1 3930 ? 252.490 196.652 213.837 1.00 63.73  ? 3930 GLU A CG    1 
ATOM   17453 C  CD    . GLU A 1 3930 ? 253.319 197.600 212.990 1.00 66.75  ? 3930 GLU A CD    1 
ATOM   17454 O  OE1   . GLU A 1 3930 ? 254.362 198.085 213.475 1.00 63.15  ? 3930 GLU A OE1   1 
ATOM   17455 O  OE2   . GLU A 1 3930 ? 252.923 197.863 211.834 1.00 66.51  ? 3930 GLU A OE2   1 
ATOM   17456 N  N     . GLN A 1 3931 ? 254.221 194.041 214.064 1.00 54.35  ? 3931 GLN A N     1 
ATOM   17457 C  CA    . GLN A 1 3931 ? 254.169 192.644 213.645 1.00 54.01  ? 3931 GLN A CA    1 
ATOM   17458 C  C     . GLN A 1 3931 ? 255.122 191.791 214.472 1.00 52.03  ? 3931 GLN A C     1 
ATOM   17459 O  O     . GLN A 1 3931 ? 254.796 190.654 214.826 1.00 55.44  ? 3931 GLN A O     1 
ATOM   17460 C  CB    . GLN A 1 3931 ? 254.494 192.524 212.158 1.00 45.29  ? 3931 GLN A CB    1 
ATOM   17461 C  CG    . GLN A 1 3931 ? 253.458 193.149 211.241 1.00 45.30  ? 3931 GLN A CG    1 
ATOM   17462 C  CD    . GLN A 1 3931 ? 253.826 193.025 209.778 1.00 53.65  ? 3931 GLN A CD    1 
ATOM   17463 O  OE1   . GLN A 1 3931 ? 254.897 192.527 209.434 1.00 55.42  ? 3931 GLN A OE1   1 
ATOM   17464 N  NE2   . GLN A 1 3931 ? 252.936 193.480 208.905 1.00 57.83  ? 3931 GLN A NE2   1 
ATOM   17465 N  N     . ALA A 1 3932 ? 256.306 192.321 214.784 1.00 51.38  ? 3932 ALA A N     1 
ATOM   17466 C  CA    . ALA A 1 3932 ? 257.258 191.575 215.598 1.00 50.69  ? 3932 ALA A CA    1 
ATOM   17467 C  C     . ALA A 1 3932 ? 256.723 191.339 217.006 1.00 49.29  ? 3932 ALA A C     1 
ATOM   17468 O  O     . ALA A 1 3932 ? 256.854 190.235 217.551 1.00 49.92  ? 3932 ALA A O     1 
ATOM   17469 C  CB    . ALA A 1 3932 ? 258.595 192.312 215.647 1.00 60.93  ? 3932 ALA A CB    1 
ATOM   17470 N  N     . GLU A 1 3933 ? 256.118 192.363 217.615 1.00 51.25  ? 3933 GLU A N     1 
ATOM   17471 C  CA    . GLU A 1 3933 ? 255.526 192.177 218.938 1.00 53.17  ? 3933 GLU A CA    1 
ATOM   17472 C  C     . GLU A 1 3933 ? 254.380 191.177 218.890 1.00 50.09  ? 3933 GLU A C     1 
ATOM   17473 O  O     . GLU A 1 3933 ? 254.218 190.365 219.808 1.00 53.43  ? 3933 GLU A O     1 
ATOM   17474 C  CB    . GLU A 1 3933 ? 255.051 193.512 219.514 1.00 57.01  ? 3933 GLU A CB    1 
ATOM   17475 C  CG    . GLU A 1 3933 ? 256.028 194.660 219.350 1.00 60.49  ? 3933 GLU A CG    1 
ATOM   17476 C  CD    . GLU A 1 3933 ? 255.353 196.017 219.433 1.00 71.40  ? 3933 GLU A CD    1 
ATOM   17477 O  OE1   . GLU A 1 3933 ? 255.961 196.951 219.997 1.00 66.93  ? 3933 GLU A OE1   1 
ATOM   17478 O  OE2   . GLU A 1 3933 ? 254.212 196.148 218.942 1.00 74.27  ? 3933 GLU A OE2   1 
ATOM   17479 N  N     . ALA A 1 3934 ? 253.571 191.219 217.828 1.00 50.36  ? 3934 ALA A N     1 
ATOM   17480 C  CA    . ALA A 1 3934 ? 252.496 190.243 217.681 1.00 45.28  ? 3934 ALA A CA    1 
ATOM   17481 C  C     . ALA A 1 3934 ? 253.050 188.829 217.552 1.00 44.46  ? 3934 ALA A C     1 
ATOM   17482 O  O     . ALA A 1 3934 ? 252.495 187.884 218.124 1.00 47.35  ? 3934 ALA A O     1 
ATOM   17483 C  CB    . ALA A 1 3934 ? 251.630 190.595 216.473 1.00 34.50  ? 3934 ALA A CB    1 
ATOM   17484 N  N     . VAL A 1 3935 ? 254.140 188.666 216.802 1.00 45.96  ? 3935 VAL A N     1 
ATOM   17485 C  CA    . VAL A 1 3935 ? 254.761 187.352 216.650 1.00 45.30  ? 3935 VAL A CA    1 
ATOM   17486 C  C     . VAL A 1 3935 ? 255.276 186.850 217.991 1.00 48.99  ? 3935 VAL A C     1 
ATOM   17487 O  O     . VAL A 1 3935 ? 255.083 185.684 218.356 1.00 55.68  ? 3935 VAL A O     1 
ATOM   17488 C  CB    . VAL A 1 3935 ? 255.885 187.410 215.599 1.00 43.71  ? 3935 VAL A CB    1 
ATOM   17489 C  CG1   . VAL A 1 3935 ? 256.751 186.162 215.670 1.00 46.26  ? 3935 VAL A CG1   1 
ATOM   17490 C  CG2   . VAL A 1 3935 ? 255.301 187.574 214.218 1.00 39.49  ? 3935 VAL A CG2   1 
ATOM   17491 N  N     . VAL A 1 3936 ? 255.942 187.725 218.748 1.00 44.41  ? 3936 VAL A N     1 
ATOM   17492 C  CA    . VAL A 1 3936 ? 256.459 187.328 220.054 1.00 45.67  ? 3936 VAL A CA    1 
ATOM   17493 C  C     . VAL A 1 3936 ? 255.316 186.943 220.987 1.00 47.64  ? 3936 VAL A C     1 
ATOM   17494 O  O     . VAL A 1 3936 ? 255.405 185.952 221.722 1.00 52.44  ? 3936 VAL A O     1 
ATOM   17495 C  CB    . VAL A 1 3936 ? 257.330 188.447 220.652 1.00 55.70  ? 3936 VAL A CB    1 
ATOM   17496 C  CG1   . VAL A 1 3936 ? 257.775 188.082 222.060 1.00 55.34  ? 3936 VAL A CG1   1 
ATOM   17497 C  CG2   . VAL A 1 3936 ? 258.540 188.699 219.772 1.00 59.17  ? 3936 VAL A CG2   1 
ATOM   17498 N  N     . ARG A 1 3937 ? 254.226 187.713 220.969 1.00 43.52  ? 3937 ARG A N     1 
ATOM   17499 C  CA    . ARG A 1 3937 ? 253.081 187.398 221.818 1.00 45.82  ? 3937 ARG A CA    1 
ATOM   17500 C  C     . ARG A 1 3937 ? 252.448 186.068 221.424 1.00 47.13  ? 3937 ARG A C     1 
ATOM   17501 O  O     . ARG A 1 3937 ? 252.055 185.280 222.292 1.00 54.48  ? 3937 ARG A O     1 
ATOM   17502 C  CB    . ARG A 1 3937 ? 252.055 188.527 221.744 1.00 48.61  ? 3937 ARG A CB    1 
ATOM   17503 C  CG    . ARG A 1 3937 ? 252.404 189.739 222.590 1.00 51.32  ? 3937 ARG A CG    1 
ATOM   17504 C  CD    . ARG A 1 3937 ? 251.283 190.762 222.570 1.00 60.31  ? 3937 ARG A CD    1 
ATOM   17505 N  NE    . ARG A 1 3937 ? 251.454 191.791 223.590 1.00 70.67  ? 3937 ARG A NE    1 
ATOM   17506 C  CZ    . ARG A 1 3937 ? 251.818 193.041 223.341 1.00 69.97  ? 3937 ARG A CZ    1 
ATOM   17507 N  NH1   . ARG A 1 3937 ? 252.060 193.458 222.109 1.00 67.39  ? 3937 ARG A NH1   1 
ATOM   17508 N  NH2   . ARG A 1 3937 ? 251.938 193.895 224.352 1.00 68.27  ? 3937 ARG A NH2   1 
ATOM   17509 N  N     . LEU A 1 3938 ? 252.336 185.802 220.121 1.00 47.05  ? 3938 LEU A N     1 
ATOM   17510 C  CA    . LEU A 1 3938 ? 251.789 184.529 219.666 1.00 45.56  ? 3938 LEU A CA    1 
ATOM   17511 C  C     . LEU A 1 3938 ? 252.717 183.368 220.001 1.00 53.34  ? 3938 LEU A C     1 
ATOM   17512 O  O     . LEU A 1 3938 ? 252.254 182.233 220.162 1.00 57.22  ? 3938 LEU A O     1 
ATOM   17513 C  CB    . LEU A 1 3938 ? 251.521 184.585 218.161 1.00 40.49  ? 3938 LEU A CB    1 
ATOM   17514 C  CG    . LEU A 1 3938 ? 250.868 183.368 217.499 1.00 49.11  ? 3938 LEU A CG    1 
ATOM   17515 C  CD1   . LEU A 1 3938 ? 249.510 183.068 218.114 1.00 40.52  ? 3938 LEU A CD1   1 
ATOM   17516 C  CD2   . LEU A 1 3938 ? 250.742 183.577 215.998 1.00 43.60  ? 3938 LEU A CD2   1 
ATOM   17517 N  N     . SER A 1 3939 ? 254.021 183.632 220.114 1.00 55.54  ? 3939 SER A N     1 
ATOM   17518 C  CA    . SER A 1 3939 ? 254.974 182.572 220.428 1.00 55.92  ? 3939 SER A CA    1 
ATOM   17519 C  C     . SER A 1 3939 ? 254.755 181.978 221.814 1.00 58.29  ? 3939 SER A C     1 
ATOM   17520 O  O     . SER A 1 3939 ? 255.282 180.898 222.101 1.00 55.66  ? 3939 SER A O     1 
ATOM   17521 C  CB    . SER A 1 3939 ? 256.403 183.103 220.314 1.00 55.01  ? 3939 SER A CB    1 
ATOM   17522 O  OG    . SER A 1 3939 ? 256.697 183.996 221.375 1.00 52.40  ? 3939 SER A OG    1 
ATOM   17523 N  N     . CYS A 1 3940 ? 253.999 182.658 222.680 1.00 58.95  ? 3940 CYS A N     1 
ATOM   17524 C  CA    . CYS A 1 3940 ? 253.745 182.130 224.017 1.00 54.58  ? 3940 CYS A CA    1 
ATOM   17525 C  C     . CYS A 1 3940 ? 252.929 180.844 223.970 1.00 60.29  ? 3940 CYS A C     1 
ATOM   17526 O  O     . CYS A 1 3940 ? 253.033 180.012 224.878 1.00 67.42  ? 3940 CYS A O     1 
ATOM   17527 C  CB    . CYS A 1 3940 ? 253.031 183.178 224.870 1.00 52.05  ? 3940 CYS A CB    1 
ATOM   17528 S  SG    . CYS A 1 3940 ? 253.979 184.693 225.142 1.00 65.67  ? 3940 CYS A SG    1 
ATOM   17529 N  N     . LEU A 1 3941 ? 252.115 180.667 222.935 1.00 61.84  ? 3941 LEU A N     1 
ATOM   17530 C  CA    . LEU A 1 3941 ? 251.322 179.454 222.818 1.00 57.44  ? 3941 LEU A CA    1 
ATOM   17531 C  C     . LEU A 1 3941 ? 252.225 178.262 222.503 1.00 57.90  ? 3941 LEU A C     1 
ATOM   17532 O  O     . LEU A 1 3941 ? 253.228 178.413 221.800 1.00 59.91  ? 3941 LEU A O     1 
ATOM   17533 C  CB    . LEU A 1 3941 ? 250.261 179.610 221.730 1.00 57.85  ? 3941 LEU A CB    1 
ATOM   17534 C  CG    . LEU A 1 3941 ? 248.844 179.891 222.233 1.00 53.18  ? 3941 LEU A CG    1 
ATOM   17535 C  CD1   . LEU A 1 3941 ? 248.821 181.169 223.054 1.00 51.90  ? 3941 LEU A CD1   1 
ATOM   17536 C  CD2   . LEU A 1 3941 ? 247.863 179.972 221.077 1.00 45.53  ? 3941 LEU A CD2   1 
ATOM   17537 N  N     . PRO A 1 3942 ? 251.899 177.071 223.013 1.00 58.46  ? 3942 PRO A N     1 
ATOM   17538 C  CA    . PRO A 1 3942 ? 252.749 175.900 222.729 1.00 58.49  ? 3942 PRO A CA    1 
ATOM   17539 C  C     . PRO A 1 3942 ? 252.804 175.527 221.258 1.00 55.89  ? 3942 PRO A C     1 
ATOM   17540 O  O     . PRO A 1 3942 ? 253.796 174.933 220.818 1.00 57.68  ? 3942 PRO A O     1 
ATOM   17541 C  CB    . PRO A 1 3942 ? 252.114 174.783 223.569 1.00 53.79  ? 3942 PRO A CB    1 
ATOM   17542 C  CG    . PRO A 1 3942 ? 250.752 175.250 223.917 1.00 56.08  ? 3942 PRO A CG    1 
ATOM   17543 C  CD    . PRO A 1 3942 ? 250.709 176.739 223.814 1.00 56.51  ? 3942 PRO A CD    1 
ATOM   17544 N  N     . ALA A 1 3943 ? 251.769 175.849 220.482 1.00 54.43  ? 3943 ALA A N     1 
ATOM   17545 C  CA    . ALA A 1 3943 ? 251.761 175.481 219.071 1.00 58.18  ? 3943 ALA A CA    1 
ATOM   17546 C  C     . ALA A 1 3943 ? 252.582 176.435 218.213 1.00 59.61  ? 3943 ALA A C     1 
ATOM   17547 O  O     . ALA A 1 3943 ? 252.827 176.133 217.040 1.00 58.03  ? 3943 ALA A O     1 
ATOM   17548 C  CB    . ALA A 1 3943 ? 250.324 175.421 218.552 1.00 54.68  ? 3943 ALA A CB    1 
ATOM   17549 N  N     . PHE A 1 3944 ? 253.005 177.573 218.761 1.00 56.41  ? 3944 PHE A N     1 
ATOM   17550 C  CA    . PHE A 1 3944 ? 253.728 178.587 218.004 1.00 51.89  ? 3944 PHE A CA    1 
ATOM   17551 C  C     . PHE A 1 3944 ? 255.086 178.907 218.621 1.00 59.39  ? 3944 PHE A C     1 
ATOM   17552 O  O     . PHE A 1 3944 ? 255.606 180.012 218.445 1.00 59.54  ? 3944 PHE A O     1 
ATOM   17553 C  CB    . PHE A 1 3944 ? 252.889 179.858 217.884 1.00 52.43  ? 3944 PHE A CB    1 
ATOM   17554 C  CG    . PHE A 1 3944 ? 251.639 179.688 217.073 1.00 46.55  ? 3944 PHE A CG    1 
ATOM   17555 C  CD1   . PHE A 1 3944 ? 251.680 179.736 215.692 1.00 41.75  ? 3944 PHE A CD1   1 
ATOM   17556 C  CD2   . PHE A 1 3944 ? 250.419 179.480 217.693 1.00 52.05  ? 3944 PHE A CD2   1 
ATOM   17557 C  CE1   . PHE A 1 3944 ? 250.530 179.578 214.946 1.00 44.37  ? 3944 PHE A CE1   1 
ATOM   17558 C  CE2   . PHE A 1 3944 ? 249.266 179.325 216.952 1.00 48.29  ? 3944 PHE A CE2   1 
ATOM   17559 C  CZ    . PHE A 1 3944 ? 249.322 179.375 215.577 1.00 44.01  ? 3944 PHE A CZ    1 
ATOM   17560 N  N     . LYS A 1 3945 ? 255.671 177.954 219.352 1.00 63.78  ? 3945 LYS A N     1 
ATOM   17561 C  CA    . LYS A 1 3945 ? 256.971 178.194 219.970 1.00 62.73  ? 3945 LYS A CA    1 
ATOM   17562 C  C     . LYS A 1 3945 ? 258.046 178.432 218.919 1.00 67.17  ? 3945 LYS A C     1 
ATOM   17563 O  O     . LYS A 1 3945 ? 258.875 179.338 219.062 1.00 70.43  ? 3945 LYS A O     1 
ATOM   17564 C  CB    . LYS A 1 3945 ? 257.352 177.020 220.872 1.00 61.86  ? 3945 LYS A CB    1 
ATOM   17565 C  CG    . LYS A 1 3945 ? 256.272 176.625 221.860 1.00 64.40  ? 3945 LYS A CG    1 
ATOM   17566 C  CD    . LYS A 1 3945 ? 256.157 177.637 222.988 1.00 64.74  ? 3945 LYS A CD    1 
ATOM   17567 C  CE    . LYS A 1 3945 ? 256.076 176.950 224.341 1.00 61.34  ? 3945 LYS A CE    1 
ATOM   17568 N  NZ    . LYS A 1 3945 ? 255.432 177.821 225.363 1.00 62.62  ? 3945 LYS A NZ    1 
ATOM   17569 N  N     . ASP A 1 3946 ? 258.050 177.632 217.857 1.00 64.72  ? 3946 ASP A N     1 
ATOM   17570 C  CA    . ASP A 1 3946 ? 258.989 177.816 216.755 1.00 68.91  ? 3946 ASP A CA    1 
ATOM   17571 C  C     . ASP A 1 3946 ? 258.307 178.602 215.637 1.00 64.65  ? 3946 ASP A C     1 
ATOM   17572 O  O     . ASP A 1 3946 ? 257.958 178.079 214.580 1.00 70.77  ? 3946 ASP A O     1 
ATOM   17573 C  CB    . ASP A 1 3946 ? 259.505 176.464 216.267 1.00 72.72  ? 3946 ASP A CB    1 
ATOM   17574 C  CG    . ASP A 1 3946 ? 260.736 176.591 215.388 1.00 74.66  ? 3946 ASP A CG    1 
ATOM   17575 O  OD1   . ASP A 1 3946 ? 260.638 177.199 214.302 1.00 67.77  ? 3946 ASP A OD1   1 
ATOM   17576 O  OD2   . ASP A 1 3946 ? 261.805 176.083 215.787 1.00 81.16  ? 3946 ASP A OD2   1 
ATOM   17577 N  N     . LEU A 1 3947 ? 258.113 179.891 215.902 1.00 53.94  ? 3947 LEU A N     1 
ATOM   17578 C  CA    . LEU A 1 3947 ? 257.468 180.795 214.957 1.00 60.23  ? 3947 LEU A CA    1 
ATOM   17579 C  C     . LEU A 1 3947 ? 258.431 181.774 214.309 1.00 62.75  ? 3947 LEU A C     1 
ATOM   17580 O  O     . LEU A 1 3947 ? 258.375 181.973 213.093 1.00 62.97  ? 3947 LEU A O     1 
ATOM   17581 C  CB    . LEU A 1 3947 ? 256.347 181.576 215.651 1.00 57.67  ? 3947 LEU A CB    1 
ATOM   17582 C  CG    . LEU A 1 3947 ? 255.553 182.545 214.776 1.00 50.52  ? 3947 LEU A CG    1 
ATOM   17583 C  CD1   . LEU A 1 3947 ? 254.942 181.814 213.591 1.00 45.49  ? 3947 LEU A CD1   1 
ATOM   17584 C  CD2   . LEU A 1 3947 ? 254.477 183.242 215.588 1.00 48.85  ? 3947 LEU A CD2   1 
ATOM   17585 N  N     . ILE A 1 3948 ? 259.313 182.396 215.093 1.00 61.30  ? 3948 ILE A N     1 
ATOM   17586 C  CA    . ILE A 1 3948 ? 260.300 183.310 214.527 1.00 58.86  ? 3948 ILE A CA    1 
ATOM   17587 C  C     . ILE A 1 3948 ? 261.236 182.556 213.589 1.00 66.36  ? 3948 ILE A C     1 
ATOM   17588 O  O     . ILE A 1 3948 ? 261.537 183.012 212.478 1.00 63.01  ? 3948 ILE A O     1 
ATOM   17589 C  CB    . ILE A 1 3948 ? 261.080 184.023 215.648 1.00 58.70  ? 3948 ILE A CB    1 
ATOM   17590 C  CG1   . ILE A 1 3948 ? 260.149 184.888 216.506 1.00 62.73  ? 3948 ILE A CG1   1 
ATOM   17591 C  CG2   . ILE A 1 3948 ? 262.193 184.875 215.065 1.00 65.63  ? 3948 ILE A CG2   1 
ATOM   17592 C  CD1   . ILE A 1 3948 ? 259.537 184.166 217.692 1.00 56.14  ? 3948 ILE A CD1   1 
ATOM   17593 N  N     . ALA A 1 3949 ? 261.702 181.383 214.025 1.00 62.26  ? 3949 ALA A N     1 
ATOM   17594 C  CA    . ALA A 1 3949 ? 262.580 180.574 213.188 1.00 61.23  ? 3949 ALA A CA    1 
ATOM   17595 C  C     . ALA A 1 3949 ? 261.864 180.106 211.929 1.00 58.37  ? 3949 ALA A C     1 
ATOM   17596 O  O     . ALA A 1 3949 ? 262.460 180.066 210.847 1.00 66.99  ? 3949 ALA A O     1 
ATOM   17597 C  CB    . ALA A 1 3949 ? 263.110 179.381 213.982 1.00 65.35  ? 3949 ALA A CB    1 
ATOM   17598 N  N     . LYS A 1 3950 ? 260.588 179.734 212.051 1.00 56.19  ? 3950 LYS A N     1 
ATOM   17599 C  CA    . LYS A 1 3950 ? 259.826 179.314 210.879 1.00 59.84  ? 3950 LYS A CA    1 
ATOM   17600 C  C     . LYS A 1 3950 ? 259.644 180.462 209.894 1.00 65.01  ? 3950 LYS A C     1 
ATOM   17601 O  O     . LYS A 1 3950 ? 259.718 180.259 208.676 1.00 61.51  ? 3950 LYS A O     1 
ATOM   17602 C  CB    . LYS A 1 3950 ? 258.472 178.751 211.308 1.00 54.64  ? 3950 LYS A CB    1 
ATOM   17603 C  CG    . LYS A 1 3950 ? 258.478 177.255 211.567 1.00 54.58  ? 3950 LYS A CG    1 
ATOM   17604 C  CD    . LYS A 1 3950 ? 257.069 176.692 211.561 1.00 48.01  ? 3950 LYS A CD    1 
ATOM   17605 C  CE    . LYS A 1 3950 ? 257.060 175.222 211.947 1.00 47.85  ? 3950 LYS A CE    1 
ATOM   17606 N  NZ    . LYS A 1 3950 ? 257.525 175.014 213.345 1.00 52.54  ? 3950 LYS A NZ    1 
ATOM   17607 N  N     . VAL A 1 3951 ? 259.392 181.671 210.401 1.00 61.04  ? 3951 VAL A N     1 
ATOM   17608 C  CA    . VAL A 1 3951 ? 259.249 182.830 209.527 1.00 55.10  ? 3951 VAL A CA    1 
ATOM   17609 C  C     . VAL A 1 3951 ? 260.565 183.137 208.823 1.00 64.08  ? 3951 VAL A C     1 
ATOM   17610 O  O     . VAL A 1 3951 ? 260.588 183.429 207.620 1.00 66.26  ? 3951 VAL A O     1 
ATOM   17611 C  CB    . VAL A 1 3951 ? 258.732 184.040 210.326 1.00 56.54  ? 3951 VAL A CB    1 
ATOM   17612 C  CG1   . VAL A 1 3951 ? 259.002 185.338 209.578 1.00 49.88  ? 3951 VAL A CG1   1 
ATOM   17613 C  CG2   . VAL A 1 3951 ? 257.247 183.888 210.610 1.00 54.54  ? 3951 VAL A CG2   1 
ATOM   17614 N  N     . GLN A 1 3952 ? 261.683 183.075 209.553 1.00 64.45  ? 3952 GLN A N     1 
ATOM   17615 C  CA    . GLN A 1 3952 ? 262.980 183.320 208.928 1.00 63.05  ? 3952 GLN A CA    1 
ATOM   17616 C  C     . GLN A 1 3952 ? 263.305 182.261 207.882 1.00 60.73  ? 3952 GLN A C     1 
ATOM   17617 O  O     . GLN A 1 3952 ? 263.868 182.573 206.827 1.00 64.14  ? 3952 GLN A O     1 
ATOM   17618 C  CB    . GLN A 1 3952 ? 264.083 183.375 209.985 1.00 63.92  ? 3952 GLN A CB    1 
ATOM   17619 C  CG    . GLN A 1 3952 ? 264.048 184.605 210.876 1.00 65.05  ? 3952 GLN A CG    1 
ATOM   17620 C  CD    . GLN A 1 3952 ? 264.809 184.403 212.171 1.00 71.45  ? 3952 GLN A CD    1 
ATOM   17621 O  OE1   . GLN A 1 3952 ? 265.485 183.391 212.355 1.00 74.34  ? 3952 GLN A OE1   1 
ATOM   17622 N  NE2   . GLN A 1 3952 ? 264.720 185.377 213.068 1.00 70.84  ? 3952 GLN A NE2   1 
ATOM   17623 N  N     . ALA A 1 3953 ? 262.968 181.000 208.161 1.00 62.80  ? 3953 ALA A N     1 
ATOM   17624 C  CA    . ALA A 1 3953 ? 263.324 179.913 207.253 1.00 70.42  ? 3953 ALA A CA    1 
ATOM   17625 C  C     . ALA A 1 3953 ? 262.609 180.042 205.913 1.00 74.20  ? 3953 ALA A C     1 
ATOM   17626 O  O     . ALA A 1 3953 ? 263.206 179.791 204.860 1.00 79.14  ? 3953 ALA A O     1 
ATOM   17627 C  CB    . ALA A 1 3953 ? 263.007 178.566 207.901 1.00 63.27  ? 3953 ALA A CB    1 
ATOM   17628 N  N     . ASP A 1 3954 ? 261.335 180.423 205.930 1.00 75.30  ? 3954 ASP A N     1 
ATOM   17629 C  CA    . ASP A 1 3954 ? 260.550 180.480 204.705 1.00 78.10  ? 3954 ASP A CA    1 
ATOM   17630 C  C     . ASP A 1 3954 ? 260.995 181.646 203.830 1.00 76.71  ? 3954 ASP A C     1 
ATOM   17631 O  O     . ASP A 1 3954 ? 261.140 182.776 204.305 1.00 72.52  ? 3954 ASP A O     1 
ATOM   17632 C  CB    . ASP A 1 3954 ? 259.064 180.604 205.036 1.00 74.45  ? 3954 ASP A CB    1 
ATOM   17633 C  CG    . ASP A 1 3954 ? 258.174 180.347 203.833 1.00 74.99  ? 3954 ASP A CG    1 
ATOM   17634 O  OD1   . ASP A 1 3954 ? 258.694 179.910 202.785 1.00 75.27  ? 3954 ASP A OD1   1 
ATOM   17635 O  OD2   . ASP A 1 3954 ? 256.952 180.583 203.937 1.00 69.22  ? 3954 ASP A OD2   1 
ATOM   17636 N  N     . GLU A 1 3955 ? 261.212 181.365 202.545 1.00 80.36  ? 3955 GLU A N     1 
ATOM   17637 C  CA    . GLU A 1 3955 ? 261.503 182.400 201.563 1.00 88.02  ? 3955 GLU A CA    1 
ATOM   17638 C  C     . GLU A 1 3955 ? 260.266 182.875 200.816 1.00 83.46  ? 3955 GLU A C     1 
ATOM   17639 O  O     . GLU A 1 3955 ? 260.306 183.940 200.193 1.00 81.53  ? 3955 GLU A O     1 
ATOM   17640 C  CB    . GLU A 1 3955 ? 262.540 181.897 200.549 1.00 88.70  ? 3955 GLU A CB    1 
ATOM   17641 C  CG    . GLU A 1 3955 ? 262.071 180.713 199.717 1.00 86.09  ? 3955 GLU A CG    1 
ATOM   17642 C  CD    . GLU A 1 3955 ? 262.366 179.380 200.377 1.00 85.74  ? 3955 GLU A CD    1 
ATOM   17643 O  OE1   . GLU A 1 3955 ? 262.961 179.377 201.476 1.00 85.10  ? 3955 GLU A OE1   1 
ATOM   17644 O  OE2   . GLU A 1 3955 ? 262.004 178.335 199.798 1.00 83.62  ? 3955 GLU A OE2   1 
ATOM   17645 N  N     . GLN A 1 3956 ? 259.177 182.110 200.866 1.00 79.48  ? 3956 GLN A N     1 
ATOM   17646 C  CA    . GLN A 1 3956 ? 257.907 182.488 200.263 1.00 73.28  ? 3956 GLN A CA    1 
ATOM   17647 C  C     . GLN A 1 3956 ? 257.041 183.322 201.199 1.00 68.94  ? 3956 GLN A C     1 
ATOM   17648 O  O     . GLN A 1 3956 ? 255.937 183.720 200.813 1.00 68.48  ? 3956 GLN A O     1 
ATOM   17649 C  CB    . GLN A 1 3956 ? 257.144 181.229 199.833 1.00 76.73  ? 3956 GLN A CB    1 
ATOM   17650 C  CG    . GLN A 1 3956 ? 256.209 181.423 198.655 1.00 75.88  ? 3956 GLN A CG    1 
ATOM   17651 C  CD    . GLN A 1 3956 ? 256.077 180.175 197.805 1.00 89.86  ? 3956 GLN A CD    1 
ATOM   17652 O  OE1   . GLN A 1 3956 ? 256.219 179.057 198.299 1.00 95.89  ? 3956 GLN A OE1   1 
ATOM   17653 N  NE2   . GLN A 1 3956 ? 255.804 180.361 196.519 1.00 91.02  ? 3956 GLN A NE2   1 
ATOM   17654 N  N     . PHE A 1 3957 ? 257.514 183.589 202.417 1.00 68.00  ? 3957 PHE A N     1 
ATOM   17655 C  CA    . PHE A 1 3957 ? 256.717 184.334 203.386 1.00 60.18  ? 3957 PHE A CA    1 
ATOM   17656 C  C     . PHE A 1 3957 ? 256.532 185.788 202.968 1.00 53.49  ? 3957 PHE A C     1 
ATOM   17657 O  O     . PHE A 1 3957 ? 255.515 186.407 203.304 1.00 52.54  ? 3957 PHE A O     1 
ATOM   17658 C  CB    . PHE A 1 3957 ? 257.381 184.248 204.762 1.00 53.86  ? 3957 PHE A CB    1 
ATOM   17659 C  CG    . PHE A 1 3957 ? 256.611 184.929 205.855 1.00 49.44  ? 3957 PHE A CG    1 
ATOM   17660 C  CD1   . PHE A 1 3957 ? 255.483 184.337 206.395 1.00 46.75  ? 3957 PHE A CD1   1 
ATOM   17661 C  CD2   . PHE A 1 3957 ? 257.025 186.151 206.352 1.00 42.58  ? 3957 PHE A CD2   1 
ATOM   17662 C  CE1   . PHE A 1 3957 ? 254.776 184.957 207.406 1.00 43.01  ? 3957 PHE A CE1   1 
ATOM   17663 C  CE2   . PHE A 1 3957 ? 256.322 186.776 207.361 1.00 43.57  ? 3957 PHE A CE2   1 
ATOM   17664 C  CZ    . PHE A 1 3957 ? 255.197 186.177 207.890 1.00 44.77  ? 3957 PHE A CZ    1 
ATOM   17665 N  N     . GLY A 1 3958 ? 257.499 186.347 202.236 1.00 51.24  ? 3958 GLY A N     1 
ATOM   17666 C  CA    . GLY A 1 3958 ? 257.423 187.753 201.873 1.00 45.55  ? 3958 GLY A CA    1 
ATOM   17667 C  C     . GLY A 1 3958 ? 256.253 188.071 200.962 1.00 47.84  ? 3958 GLY A C     1 
ATOM   17668 O  O     . GLY A 1 3958 ? 255.547 189.062 201.167 1.00 48.92  ? 3958 GLY A O     1 
ATOM   17669 N  N     . ILE A 1 3959 ? 256.032 187.240 199.941 1.00 48.29  ? 3959 ILE A N     1 
ATOM   17670 C  CA    . ILE A 1 3959 ? 254.923 187.484 199.023 1.00 47.88  ? 3959 ILE A CA    1 
ATOM   17671 C  C     . ILE A 1 3959 ? 253.589 187.259 199.726 1.00 47.68  ? 3959 ILE A C     1 
ATOM   17672 O  O     . ILE A 1 3959 ? 252.589 187.916 199.413 1.00 43.09  ? 3959 ILE A O     1 
ATOM   17673 C  CB    . ILE A 1 3959 ? 255.059 186.616 197.757 1.00 46.68  ? 3959 ILE A CB    1 
ATOM   17674 C  CG1   . ILE A 1 3959 ? 255.010 185.128 198.100 1.00 51.60  ? 3959 ILE A CG1   1 
ATOM   17675 C  CG2   . ILE A 1 3959 ? 256.344 186.950 197.017 1.00 51.54  ? 3959 ILE A CG2   1 
ATOM   17676 C  CD1   . ILE A 1 3959 ? 254.904 184.237 196.883 1.00 67.74  ? 3959 ILE A CD1   1 
ATOM   17677 N  N     . TRP A 1 3960 ? 253.550 186.325 200.679 1.00 46.12  ? 3960 TRP A N     1 
ATOM   17678 C  CA    . TRP A 1 3960 ? 252.325 186.106 201.440 1.00 37.14  ? 3960 TRP A CA    1 
ATOM   17679 C  C     . TRP A 1 3960 ? 252.006 187.299 202.332 1.00 35.57  ? 3960 TRP A C     1 
ATOM   17680 O  O     . TRP A 1 3960 ? 250.836 187.665 202.490 1.00 38.28  ? 3960 TRP A O     1 
ATOM   17681 C  CB    . TRP A 1 3960 ? 252.436 184.837 202.280 1.00 32.32  ? 3960 TRP A CB    1 
ATOM   17682 C  CG    . TRP A 1 3960 ? 251.237 184.628 203.147 1.00 28.92  ? 3960 TRP A CG    1 
ATOM   17683 C  CD1   . TRP A 1 3960 ? 250.054 184.063 202.779 1.00 29.48  ? 3960 TRP A CD1   1 
ATOM   17684 C  CD2   . TRP A 1 3960 ? 251.089 185.013 204.517 1.00 29.12  ? 3960 TRP A CD2   1 
ATOM   17685 N  NE1   . TRP A 1 3960 ? 249.183 184.054 203.839 1.00 27.74  ? 3960 TRP A NE1   1 
ATOM   17686 C  CE2   . TRP A 1 3960 ? 249.793 184.636 204.918 1.00 23.88  ? 3960 TRP A CE2   1 
ATOM   17687 C  CE3   . TRP A 1 3960 ? 251.928 185.635 205.446 1.00 34.61  ? 3960 TRP A CE3   1 
ATOM   17688 C  CZ2   . TRP A 1 3960 ? 249.318 184.857 206.206 1.00 25.65  ? 3960 TRP A CZ2   1 
ATOM   17689 C  CZ3   . TRP A 1 3960 ? 251.454 185.854 206.722 1.00 30.16  ? 3960 TRP A CZ3   1 
ATOM   17690 C  CH2   . TRP A 1 3960 ? 250.161 185.466 207.091 1.00 30.81  ? 3960 TRP A CH2   1 
ATOM   17691 N  N     . LEU A 1 3961 ? 253.031 187.905 202.936 1.00 33.83  ? 3961 LEU A N     1 
ATOM   17692 C  CA    . LEU A 1 3961 ? 252.794 189.046 203.815 1.00 40.38  ? 3961 LEU A CA    1 
ATOM   17693 C  C     . LEU A 1 3961 ? 252.189 190.218 203.054 1.00 41.23  ? 3961 LEU A C     1 
ATOM   17694 O  O     . LEU A 1 3961 ? 251.340 190.942 203.587 1.00 39.75  ? 3961 LEU A O     1 
ATOM   17695 C  CB    . LEU A 1 3961 ? 254.095 189.462 204.501 1.00 41.00  ? 3961 LEU A CB    1 
ATOM   17696 C  CG    . LEU A 1 3961 ? 253.932 190.200 205.830 1.00 40.79  ? 3961 LEU A CG    1 
ATOM   17697 C  CD1   . LEU A 1 3961 ? 253.656 189.226 206.960 1.00 39.32  ? 3961 LEU A CD1   1 
ATOM   17698 C  CD2   . LEU A 1 3961 ? 255.167 191.036 206.131 1.00 46.08  ? 3961 LEU A CD2   1 
ATOM   17699 N  N     . ASP A 1 3962 ? 252.610 190.423 201.809 1.00 41.71  ? 3962 ASP A N     1 
ATOM   17700 C  CA    . ASP A 1 3962 ? 252.084 191.492 200.972 1.00 44.17  ? 3962 ASP A CA    1 
ATOM   17701 C  C     . ASP A 1 3962 ? 250.988 191.014 200.028 1.00 40.03  ? 3962 ASP A C     1 
ATOM   17702 O  O     . ASP A 1 3962 ? 250.611 191.749 199.110 1.00 41.28  ? 3962 ASP A O     1 
ATOM   17703 C  CB    . ASP A 1 3962 ? 253.216 192.144 200.176 1.00 54.26  ? 3962 ASP A CB    1 
ATOM   17704 C  CG    . ASP A 1 3962 ? 254.169 192.928 201.056 1.00 64.97  ? 3962 ASP A CG    1 
ATOM   17705 O  OD1   . ASP A 1 3962 ? 253.726 193.439 202.106 1.00 60.18  ? 3962 ASP A OD1   1 
ATOM   17706 O  OD2   . ASP A 1 3962 ? 255.360 193.036 200.698 1.00 77.47  ? 3962 ASP A OD2   1 
ATOM   17707 N  N     . SER A 1 3963 ? 250.475 189.804 200.231 1.00 41.11  ? 3963 SER A N     1 
ATOM   17708 C  CA    . SER A 1 3963 ? 249.404 189.285 199.394 1.00 34.63  ? 3963 SER A CA    1 
ATOM   17709 C  C     . SER A 1 3963 ? 248.120 190.080 199.603 1.00 35.57  ? 3963 SER A C     1 
ATOM   17710 O  O     . SER A 1 3963 ? 247.853 190.598 200.689 1.00 33.17  ? 3963 SER A O     1 
ATOM   17711 C  CB    . SER A 1 3963 ? 249.158 187.807 199.698 1.00 33.02  ? 3963 SER A CB    1 
ATOM   17712 O  OG    . SER A 1 3963 ? 248.096 187.293 198.913 1.00 38.15  ? 3963 SER A OG    1 
ATOM   17713 N  N     . SER A 1 3964 ? 247.324 190.177 198.536 1.00 36.55  ? 3964 SER A N     1 
ATOM   17714 C  CA    . SER A 1 3964 ? 246.072 190.922 198.611 1.00 33.44  ? 3964 SER A CA    1 
ATOM   17715 C  C     . SER A 1 3964 ? 245.092 190.267 199.576 1.00 34.14  ? 3964 SER A C     1 
ATOM   17716 O  O     . SER A 1 3964 ? 244.433 190.953 200.365 1.00 35.48  ? 3964 SER A O     1 
ATOM   17717 C  CB    . SER A 1 3964 ? 245.453 191.047 197.220 1.00 35.19  ? 3964 SER A CB    1 
ATOM   17718 O  OG    . SER A 1 3964 ? 245.058 189.781 196.725 1.00 36.95  ? 3964 SER A OG    1 
ATOM   17719 N  N     . SER A 1 3965 ? 244.984 188.941 199.530 1.00 37.24  ? 3965 SER A N     1 
ATOM   17720 C  CA    . SER A 1 3965 ? 244.089 188.180 200.402 1.00 31.98  ? 3965 SER A CA    1 
ATOM   17721 C  C     . SER A 1 3965 ? 244.885 187.054 201.046 1.00 30.11  ? 3965 SER A C     1 
ATOM   17722 O  O     . SER A 1 3965 ? 244.746 185.882 200.670 1.00 32.98  ? 3965 SER A O     1 
ATOM   17723 C  CB    . SER A 1 3965 ? 242.891 187.640 199.622 1.00 31.22  ? 3965 SER A CB    1 
ATOM   17724 O  OG    . SER A 1 3965 ? 243.301 186.680 198.665 1.00 43.17  ? 3965 SER A OG    1 
ATOM   17725 N  N     . PRO A 1 3966 ? 245.734 187.375 202.026 1.00 26.82  ? 3966 PRO A N     1 
ATOM   17726 C  CA    . PRO A 1 3966 ? 246.572 186.334 202.645 1.00 25.68  ? 3966 PRO A CA    1 
ATOM   17727 C  C     . PRO A 1 3966 ? 245.784 185.262 203.374 1.00 23.88  ? 3966 PRO A C     1 
ATOM   17728 O  O     . PRO A 1 3966 ? 246.298 184.151 203.549 1.00 28.12  ? 3966 PRO A O     1 
ATOM   17729 C  CB    . PRO A 1 3966 ? 247.458 187.131 203.612 1.00 24.80  ? 3966 PRO A CB    1 
ATOM   17730 C  CG    . PRO A 1 3966 ? 246.657 188.343 203.930 1.00 22.24  ? 3966 PRO A CG    1 
ATOM   17731 C  CD    . PRO A 1 3966 ? 245.921 188.686 202.669 1.00 25.53  ? 3966 PRO A CD    1 
ATOM   17732 N  N     . GLU A 1 3967 ? 244.557 185.556 203.808 1.00 28.38  ? 3967 GLU A N     1 
ATOM   17733 C  CA    . GLU A 1 3967 ? 243.763 184.580 204.546 1.00 24.24  ? 3967 GLU A CA    1 
ATOM   17734 C  C     . GLU A 1 3967 ? 243.341 183.397 203.684 1.00 25.92  ? 3967 GLU A C     1 
ATOM   17735 O  O     . GLU A 1 3967 ? 242.978 182.351 204.229 1.00 30.14  ? 3967 GLU A O     1 
ATOM   17736 C  CB    . GLU A 1 3967 ? 242.533 185.261 205.146 1.00 23.10  ? 3967 GLU A CB    1 
ATOM   17737 C  CG    . GLU A 1 3967 ? 241.315 185.264 204.237 1.00 24.68  ? 3967 GLU A CG    1 
ATOM   17738 C  CD    . GLU A 1 3967 ? 241.176 186.557 203.458 1.00 27.68  ? 3967 GLU A CD    1 
ATOM   17739 O  OE1   . GLU A 1 3967 ? 242.063 187.425 203.583 1.00 27.75  ? 3967 GLU A OE1   1 
ATOM   17740 O  OE2   . GLU A 1 3967 ? 240.179 186.704 202.722 1.00 33.78  ? 3967 GLU A OE2   1 
ATOM   17741 N  N     . GLN A 1 3968 ? 243.371 183.541 202.356 1.00 29.94  ? 3968 GLN A N     1 
ATOM   17742 C  CA    . GLN A 1 3968 ? 242.994 182.434 201.484 1.00 27.75  ? 3968 GLN A CA    1 
ATOM   17743 C  C     . GLN A 1 3968 ? 243.971 181.272 201.609 1.00 30.45  ? 3968 GLN A C     1 
ATOM   17744 O  O     . GLN A 1 3968 ? 243.556 180.108 201.661 1.00 39.38  ? 3968 GLN A O     1 
ATOM   17745 C  CB    . GLN A 1 3968 ? 242.918 182.912 200.035 1.00 33.07  ? 3968 GLN A CB    1 
ATOM   17746 C  CG    . GLN A 1 3968 ? 241.896 184.008 199.795 1.00 37.02  ? 3968 GLN A CG    1 
ATOM   17747 C  CD    . GLN A 1 3968 ? 240.472 183.529 199.971 1.00 35.74  ? 3968 GLN A CD    1 
ATOM   17748 O  OE1   . GLN A 1 3968 ? 239.804 183.878 200.944 1.00 37.43  ? 3968 GLN A OE1   1 
ATOM   17749 N  NE2   . GLN A 1 3968 ? 239.995 182.730 199.025 1.00 38.70  ? 3968 GLN A NE2   1 
ATOM   17750 N  N     . THR A 1 3969 ? 245.271 181.564 201.651 1.00 31.38  ? 3969 THR A N     1 
ATOM   17751 C  CA    . THR A 1 3969 ? 246.323 180.549 201.736 1.00 33.41  ? 3969 THR A CA    1 
ATOM   17752 C  C     . THR A 1 3969 ? 247.304 180.975 202.824 1.00 31.48  ? 3969 THR A C     1 
ATOM   17753 O  O     . THR A 1 3969 ? 248.288 181.663 202.547 1.00 32.43  ? 3969 THR A O     1 
ATOM   17754 C  CB    . THR A 1 3969 ? 247.028 180.366 200.391 1.00 36.93  ? 3969 THR A CB    1 
ATOM   17755 O  OG1   . THR A 1 3969 ? 247.652 181.597 200.005 1.00 33.40  ? 3969 THR A OG1   1 
ATOM   17756 C  CG2   . THR A 1 3969 ? 246.044 179.937 199.312 1.00 33.79  ? 3969 THR A CG2   1 
ATOM   17757 N  N     . VAL A 1 3970 ? 247.038 180.558 204.058 1.00 28.97  ? 3970 VAL A N     1 
ATOM   17758 C  CA    . VAL A 1 3970 ? 247.911 180.865 205.188 1.00 31.28  ? 3970 VAL A CA    1 
ATOM   17759 C  C     . VAL A 1 3970 ? 248.947 179.755 205.325 1.00 36.43  ? 3970 VAL A C     1 
ATOM   17760 O  O     . VAL A 1 3970 ? 248.580 178.572 205.373 1.00 40.88  ? 3970 VAL A O     1 
ATOM   17761 C  CB    . VAL A 1 3970 ? 247.106 181.041 206.484 1.00 27.54  ? 3970 VAL A CB    1 
ATOM   17762 C  CG1   . VAL A 1 3970 ? 248.006 181.524 207.608 1.00 25.90  ? 3970 VAL A CG1   1 
ATOM   17763 C  CG2   . VAL A 1 3970 ? 245.957 182.009 206.266 1.00 24.54  ? 3970 VAL A CG2   1 
ATOM   17764 N  N     . PRO A 1 3971 ? 250.239 180.078 205.377 1.00 32.01  ? 3971 PRO A N     1 
ATOM   17765 C  CA    . PRO A 1 3971 ? 251.256 179.026 205.489 1.00 36.00  ? 3971 PRO A CA    1 
ATOM   17766 C  C     . PRO A 1 3971 ? 251.135 178.260 206.797 1.00 42.61  ? 3971 PRO A C     1 
ATOM   17767 O  O     . PRO A 1 3971 ? 250.704 178.793 207.822 1.00 45.00  ? 3971 PRO A O     1 
ATOM   17768 C  CB    . PRO A 1 3971 ? 252.577 179.800 205.412 1.00 35.42  ? 3971 PRO A CB    1 
ATOM   17769 C  CG    . PRO A 1 3971 ? 252.228 181.189 205.835 1.00 33.43  ? 3971 PRO A CG    1 
ATOM   17770 C  CD    . PRO A 1 3971 ? 250.837 181.422 205.332 1.00 32.70  ? 3971 PRO A CD    1 
ATOM   17771 N  N     . TYR A 1 3972 ? 251.527 176.986 206.748 1.00 43.86  ? 3972 TYR A N     1 
ATOM   17772 C  CA    . TYR A 1 3972 ? 251.446 176.087 207.901 1.00 43.31  ? 3972 TYR A CA    1 
ATOM   17773 C  C     . TYR A 1 3972 ? 252.587 176.414 208.867 1.00 41.67  ? 3972 TYR A C     1 
ATOM   17774 O  O     . TYR A 1 3972 ? 253.566 175.679 209.018 1.00 50.80  ? 3972 TYR A O     1 
ATOM   17775 C  CB    . TYR A 1 3972 ? 251.479 174.638 207.434 1.00 44.71  ? 3972 TYR A CB    1 
ATOM   17776 C  CG    . TYR A 1 3972 ? 251.360 173.604 208.532 1.00 54.26  ? 3972 TYR A CG    1 
ATOM   17777 C  CD1   . TYR A 1 3972 ? 250.137 173.344 209.137 1.00 50.54  ? 3972 TYR A CD1   1 
ATOM   17778 C  CD2   . TYR A 1 3972 ? 252.463 172.866 208.942 1.00 61.47  ? 3972 TYR A CD2   1 
ATOM   17779 C  CE1   . TYR A 1 3972 ? 250.023 172.394 210.134 1.00 57.34  ? 3972 TYR A CE1   1 
ATOM   17780 C  CE2   . TYR A 1 3972 ? 252.359 171.916 209.937 1.00 62.93  ? 3972 TYR A CE2   1 
ATOM   17781 C  CZ    . TYR A 1 3972 ? 251.137 171.683 210.529 1.00 66.19  ? 3972 TYR A CZ    1 
ATOM   17782 O  OH    . TYR A 1 3972 ? 251.031 170.734 211.521 1.00 76.92  ? 3972 TYR A OH    1 
ATOM   17783 N  N     . LEU A 1 3973 ? 252.451 177.563 209.521 1.00 39.89  ? 3973 LEU A N     1 
ATOM   17784 C  CA    . LEU A 1 3973 ? 253.476 178.079 210.429 1.00 41.94  ? 3973 LEU A CA    1 
ATOM   17785 C  C     . LEU A 1 3973 ? 253.205 177.700 211.882 1.00 45.21  ? 3973 LEU A C     1 
ATOM   17786 O  O     . LEU A 1 3973 ? 253.193 178.554 212.766 1.00 49.85  ? 3973 LEU A O     1 
ATOM   17787 C  CB    . LEU A 1 3973 ? 253.585 179.591 210.274 1.00 42.60  ? 3973 LEU A CB    1 
ATOM   17788 C  CG    . LEU A 1 3973 ? 254.237 180.114 208.995 1.00 40.15  ? 3973 LEU A CG    1 
ATOM   17789 C  CD1   . LEU A 1 3973 ? 254.568 181.587 209.140 1.00 42.47  ? 3973 LEU A CD1   1 
ATOM   17790 C  CD2   . LEU A 1 3973 ? 255.486 179.311 208.666 1.00 40.18  ? 3973 LEU A CD2   1 
ATOM   17791 N  N     . TRP A 1 3974 ? 252.990 176.414 212.145 1.00 46.28  ? 3974 TRP A N     1 
ATOM   17792 C  CA    . TRP A 1 3974 ? 252.836 175.948 213.517 1.00 53.89  ? 3974 TRP A CA    1 
ATOM   17793 C  C     . TRP A 1 3974 ? 253.148 174.461 213.568 1.00 59.57  ? 3974 TRP A C     1 
ATOM   17794 O  O     . TRP A 1 3974 ? 253.101 173.762 212.553 1.00 59.34  ? 3974 TRP A O     1 
ATOM   17795 C  CB    . TRP A 1 3974 ? 251.432 176.235 214.067 1.00 49.44  ? 3974 TRP A CB    1 
ATOM   17796 C  CG    . TRP A 1 3974 ? 250.323 175.472 213.404 1.00 56.07  ? 3974 TRP A CG    1 
ATOM   17797 C  CD1   . TRP A 1 3974 ? 249.904 174.209 213.705 1.00 55.94  ? 3974 TRP A CD1   1 
ATOM   17798 C  CD2   . TRP A 1 3974 ? 249.479 175.931 212.343 1.00 51.20  ? 3974 TRP A CD2   1 
ATOM   17799 N  NE1   . TRP A 1 3974 ? 248.859 173.850 212.893 1.00 51.59  ? 3974 TRP A NE1   1 
ATOM   17800 C  CE2   . TRP A 1 3974 ? 248.577 174.891 212.047 1.00 49.78  ? 3974 TRP A CE2   1 
ATOM   17801 C  CE3   . TRP A 1 3974 ? 249.400 177.120 211.612 1.00 39.46  ? 3974 TRP A CE3   1 
ATOM   17802 C  CZ2   . TRP A 1 3974 ? 247.611 175.002 211.052 1.00 44.11  ? 3974 TRP A CZ2   1 
ATOM   17803 C  CZ3   . TRP A 1 3974 ? 248.441 177.227 210.625 1.00 40.42  ? 3974 TRP A CZ3   1 
ATOM   17804 C  CH2   . TRP A 1 3974 ? 247.558 176.175 210.354 1.00 46.04  ? 3974 TRP A CH2   1 
ATOM   17805 N  N     . SER A 1 3975 ? 253.465 173.989 214.769 1.00 61.34  ? 3975 SER A N     1 
ATOM   17806 C  CA    . SER A 1 3975 ? 253.878 172.611 214.995 1.00 64.67  ? 3975 SER A CA    1 
ATOM   17807 C  C     . SER A 1 3975 ? 252.801 171.873 215.774 1.00 66.38  ? 3975 SER A C     1 
ATOM   17808 O  O     . SER A 1 3975 ? 252.397 172.313 216.856 1.00 67.13  ? 3975 SER A O     1 
ATOM   17809 C  CB    . SER A 1 3975 ? 255.207 172.558 215.752 1.00 69.37  ? 3975 SER A CB    1 
ATOM   17810 O  OG    . SER A 1 3975 ? 255.127 173.285 216.966 1.00 67.47  ? 3975 SER A OG    1 
ATOM   17811 N  N     . GLU A 1 3976 ? 252.343 170.750 215.225 1.00 70.23  ? 3976 GLU A N     1 
ATOM   17812 C  CA    . GLU A 1 3976 ? 251.331 169.917 215.858 1.00 79.48  ? 3976 GLU A CA    1 
ATOM   17813 C  C     . GLU A 1 3976 ? 251.805 168.473 215.857 1.00 84.93  ? 3976 GLU A C     1 
ATOM   17814 O  O     . GLU A 1 3976 ? 252.267 167.970 214.828 1.00 84.08  ? 3976 GLU A O     1 
ATOM   17815 C  CB    . GLU A 1 3976 ? 249.984 170.034 215.135 1.00 80.21  ? 3976 GLU A CB    1 
ATOM   17816 C  CG    . GLU A 1 3976 ? 249.197 171.289 215.475 1.00 80.98  ? 3976 GLU A CG    1 
ATOM   17817 C  CD    . GLU A 1 3976 ? 248.265 171.093 216.654 1.00 83.55  ? 3976 GLU A CD    1 
ATOM   17818 O  OE1   . GLU A 1 3976 ? 248.457 170.118 217.411 1.00 86.12  ? 3976 GLU A OE1   1 
ATOM   17819 O  OE2   . GLU A 1 3976 ? 247.340 171.915 216.825 1.00 76.54  ? 3976 GLU A OE2   1 
ATOM   17820 N  N     . GLU A 1 3977 ? 251.699 167.814 217.012 1.00 86.44  ? 3977 GLU A N     1 
ATOM   17821 C  CA    . GLU A 1 3977 ? 252.056 166.400 217.088 1.00 89.23  ? 3977 GLU A CA    1 
ATOM   17822 C  C     . GLU A 1 3977 ? 251.127 165.552 216.229 1.00 87.53  ? 3977 GLU A C     1 
ATOM   17823 O  O     . GLU A 1 3977 ? 251.577 164.639 215.527 1.00 87.76  ? 3977 GLU A O     1 
ATOM   17824 C  CB    . GLU A 1 3977 ? 252.025 165.932 218.543 1.00 83.84  ? 3977 GLU A CB    1 
ATOM   17825 C  CG    . GLU A 1 3977 ? 253.323 166.177 219.295 1.00 89.70  ? 3977 GLU A CG    1 
ATOM   17826 C  CD    . GLU A 1 3977 ? 253.507 167.630 219.687 1.00 92.52  ? 3977 GLU A CD    1 
ATOM   17827 O  OE1   . GLU A 1 3977 ? 252.532 168.406 219.589 1.00 89.28  ? 3977 GLU A OE1   1 
ATOM   17828 O  OE2   . GLU A 1 3977 ? 254.629 167.998 220.094 1.00 91.06  ? 3977 GLU A OE2   1 
ATOM   17829 N  N     . THR A 1 3978 ? 249.828 165.839 216.272 1.00 84.14  ? 3978 THR A N     1 
ATOM   17830 C  CA    . THR A 1 3978 ? 248.838 165.151 215.464 1.00 84.07  ? 3978 THR A CA    1 
ATOM   17831 C  C     . THR A 1 3978 ? 248.205 166.128 214.481 1.00 85.03  ? 3978 THR A C     1 
ATOM   17832 O  O     . THR A 1 3978 ? 248.135 167.330 214.759 1.00 85.44  ? 3978 THR A O     1 
ATOM   17833 C  CB    . THR A 1 3978 ? 247.741 164.523 216.334 1.00 82.06  ? 3978 THR A CB    1 
ATOM   17834 O  OG1   . THR A 1 3978 ? 247.058 165.552 217.062 1.00 86.67  ? 3978 THR A OG1   1 
ATOM   17835 C  CG2   . THR A 1 3978 ? 248.343 163.529 217.315 1.00 75.97  ? 3978 THR A CG2   1 
ATOM   17836 N  N     . PRO A 1 3979 ? 247.752 165.651 213.321 1.00 77.24  ? 3979 PRO A N     1 
ATOM   17837 C  CA    . PRO A 1 3979 ? 247.104 166.554 212.363 1.00 66.92  ? 3979 PRO A CA    1 
ATOM   17838 C  C     . PRO A 1 3979 ? 245.883 167.221 212.978 1.00 70.86  ? 3979 PRO A C     1 
ATOM   17839 O  O     . PRO A 1 3979 ? 245.113 166.599 213.712 1.00 73.77  ? 3979 PRO A O     1 
ATOM   17840 C  CB    . PRO A 1 3979 ? 246.720 165.628 211.204 1.00 70.93  ? 3979 PRO A CB    1 
ATOM   17841 C  CG    . PRO A 1 3979 ? 247.663 164.477 211.315 1.00 72.17  ? 3979 PRO A CG    1 
ATOM   17842 C  CD    . PRO A 1 3979 ? 247.904 164.289 212.781 1.00 71.50  ? 3979 PRO A CD    1 
ATOM   17843 N  N     . ALA A 1 3980 ? 245.712 168.501 212.667 1.00 71.56  ? 3980 ALA A N     1 
ATOM   17844 C  CA    . ALA A 1 3980 ? 244.650 169.299 213.256 1.00 62.18  ? 3980 ALA A CA    1 
ATOM   17845 C  C     . ALA A 1 3980 ? 243.364 169.177 212.449 1.00 55.84  ? 3980 ALA A C     1 
ATOM   17846 O  O     . ALA A 1 3980 ? 243.384 168.960 211.235 1.00 53.71  ? 3980 ALA A O     1 
ATOM   17847 C  CB    . ALA A 1 3980 ? 245.067 170.767 213.352 1.00 53.33  ? 3980 ALA A CB    1 
ATOM   17848 N  N     . THR A 1 3981 ? 242.240 169.318 213.146 1.00 50.89  ? 3981 THR A N     1 
ATOM   17849 C  CA    . THR A 1 3981 ? 240.944 169.324 212.499 1.00 43.56  ? 3981 THR A CA    1 
ATOM   17850 C  C     . THR A 1 3981 ? 240.772 170.604 211.686 1.00 40.96  ? 3981 THR A C     1 
ATOM   17851 O  O     . THR A 1 3981 ? 241.461 171.597 211.926 1.00 41.62  ? 3981 THR A O     1 
ATOM   17852 C  CB    . THR A 1 3981 ? 239.836 169.203 213.543 1.00 46.54  ? 3981 THR A CB    1 
ATOM   17853 O  OG1   . THR A 1 3981 ? 239.890 170.324 214.434 1.00 46.91  ? 3981 THR A OG1   1 
ATOM   17854 C  CG2   . THR A 1 3981 ? 239.995 167.919 214.339 1.00 48.97  ? 3981 THR A CG2   1 
ATOM   17855 N  N     . PRO A 1 3982 ? 239.868 170.600 210.700 1.00 42.91  ? 3982 PRO A N     1 
ATOM   17856 C  CA    . PRO A 1 3982 ? 239.643 171.827 209.919 1.00 39.29  ? 3982 PRO A CA    1 
ATOM   17857 C  C     . PRO A 1 3982 ? 239.252 173.022 210.769 1.00 31.82  ? 3982 PRO A C     1 
ATOM   17858 O  O     . PRO A 1 3982 ? 239.651 174.149 210.454 1.00 29.74  ? 3982 PRO A O     1 
ATOM   17859 C  CB    . PRO A 1 3982 ? 238.519 171.428 208.948 1.00 33.70  ? 3982 PRO A CB    1 
ATOM   17860 C  CG    . PRO A 1 3982 ? 237.968 170.138 209.474 1.00 35.84  ? 3982 PRO A CG    1 
ATOM   17861 C  CD    . PRO A 1 3982 ? 239.104 169.463 210.160 1.00 37.45  ? 3982 PRO A CD    1 
ATOM   17862 N  N     . ILE A 1 3983 ? 238.487 172.813 211.842 1.00 34.61  ? 3983 ILE A N     1 
ATOM   17863 C  CA    . ILE A 1 3983 ? 238.162 173.914 212.742 1.00 31.60  ? 3983 ILE A CA    1 
ATOM   17864 C  C     . ILE A 1 3983 ? 239.415 174.407 213.456 1.00 29.26  ? 3983 ILE A C     1 
ATOM   17865 O  O     . ILE A 1 3983 ? 239.630 175.616 213.599 1.00 32.85  ? 3983 ILE A O     1 
ATOM   17866 C  CB    . ILE A 1 3983 ? 237.069 173.488 213.738 1.00 31.59  ? 3983 ILE A CB    1 
ATOM   17867 C  CG1   . ILE A 1 3983 ? 235.816 173.029 212.991 1.00 32.00  ? 3983 ILE A CG1   1 
ATOM   17868 C  CG2   . ILE A 1 3983 ? 236.728 174.632 214.671 1.00 25.36  ? 3983 ILE A CG2   1 
ATOM   17869 C  CD1   . ILE A 1 3983 ? 235.660 171.523 212.926 1.00 40.28  ? 3983 ILE A CD1   1 
ATOM   17870 N  N     . GLY A 1 3984 ? 240.262 173.484 213.913 1.00 29.98  ? 3984 GLY A N     1 
ATOM   17871 C  CA    . GLY A 1 3984 ? 241.509 173.891 214.538 1.00 32.57  ? 3984 GLY A CA    1 
ATOM   17872 C  C     . GLY A 1 3984 ? 242.457 174.561 213.564 1.00 31.96  ? 3984 GLY A C     1 
ATOM   17873 O  O     . GLY A 1 3984 ? 243.166 175.509 213.922 1.00 35.53  ? 3984 GLY A O     1 
ATOM   17874 N  N     . GLN A 1 3985 ? 242.489 174.077 212.321 1.00 34.39  ? 3985 GLN A N     1 
ATOM   17875 C  CA    . GLN A 1 3985 ? 243.267 174.748 211.287 1.00 32.83  ? 3985 GLN A CA    1 
ATOM   17876 C  C     . GLN A 1 3985 ? 242.758 176.164 211.061 1.00 30.63  ? 3985 GLN A C     1 
ATOM   17877 O  O     . GLN A 1 3985 ? 243.550 177.099 210.896 1.00 34.28  ? 3985 GLN A O     1 
ATOM   17878 C  CB    . GLN A 1 3985 ? 243.213 173.943 209.991 1.00 33.65  ? 3985 GLN A CB    1 
ATOM   17879 C  CG    . GLN A 1 3985 ? 244.125 172.730 209.976 1.00 45.43  ? 3985 GLN A CG    1 
ATOM   17880 C  CD    . GLN A 1 3985 ? 244.092 171.995 208.652 1.00 61.30  ? 3985 GLN A CD    1 
ATOM   17881 O  OE1   . GLN A 1 3985 ? 244.144 172.609 207.586 1.00 57.61  ? 3985 GLN A OE1   1 
ATOM   17882 N  NE2   . GLN A 1 3985 ? 244.010 170.672 208.711 1.00 61.54  ? 3985 GLN A NE2   1 
ATOM   17883 N  N     . ALA A 1 3986 ? 241.435 176.341 211.058 1.00 27.37  ? 3986 ALA A N     1 
ATOM   17884 C  CA    . ALA A 1 3986 ? 240.860 177.674 210.920 1.00 25.47  ? 3986 ALA A CA    1 
ATOM   17885 C  C     . ALA A 1 3986 ? 241.238 178.566 212.095 1.00 24.70  ? 3986 ALA A C     1 
ATOM   17886 O  O     . ALA A 1 3986 ? 241.525 179.752 211.913 1.00 26.69  ? 3986 ALA A O     1 
ATOM   17887 C  CB    . ALA A 1 3986 ? 239.342 177.578 210.785 1.00 20.77  ? 3986 ALA A CB    1 
ATOM   17888 N  N     . ILE A 1 3987 ? 241.236 178.014 213.311 1.00 23.13  ? 3987 ILE A N     1 
ATOM   17889 C  CA    . ILE A 1 3987 ? 241.610 178.799 214.487 1.00 24.92  ? 3987 ILE A CA    1 
ATOM   17890 C  C     . ILE A 1 3987 ? 243.068 179.237 214.400 1.00 25.18  ? 3987 ILE A C     1 
ATOM   17891 O  O     . ILE A 1 3987 ? 243.409 180.389 214.703 1.00 29.36  ? 3987 ILE A O     1 
ATOM   17892 C  CB    . ILE A 1 3987 ? 241.336 177.999 215.774 1.00 27.73  ? 3987 ILE A CB    1 
ATOM   17893 C  CG1   . ILE A 1 3987 ? 239.839 177.727 215.926 1.00 28.18  ? 3987 ILE A CG1   1 
ATOM   17894 C  CG2   . ILE A 1 3987 ? 241.860 178.743 216.990 1.00 31.96  ? 3987 ILE A CG2   1 
ATOM   17895 C  CD1   . ILE A 1 3987 ? 239.486 176.905 217.140 1.00 32.02  ? 3987 ILE A CD1   1 
ATOM   17896 N  N     . HIS A 1 3988 ? 243.951 178.326 213.993 1.00 26.75  ? 3988 HIS A N     1 
ATOM   17897 C  CA    . HIS A 1 3988 ? 245.363 178.672 213.861 1.00 28.25  ? 3988 HIS A CA    1 
ATOM   17898 C  C     . HIS A 1 3988 ? 245.582 179.703 212.758 1.00 29.44  ? 3988 HIS A C     1 
ATOM   17899 O  O     . HIS A 1 3988 ? 246.400 180.620 212.910 1.00 30.65  ? 3988 HIS A O     1 
ATOM   17900 C  CB    . HIS A 1 3988 ? 246.185 177.412 213.606 1.00 35.08  ? 3988 HIS A CB    1 
ATOM   17901 C  CG    . HIS A 1 3988 ? 246.371 176.562 214.823 1.00 34.68  ? 3988 HIS A CG    1 
ATOM   17902 N  ND1   . HIS A 1 3988 ? 245.748 175.344 214.984 1.00 40.37  ? 3988 HIS A ND1   1 
ATOM   17903 C  CD2   . HIS A 1 3988 ? 247.105 176.759 215.944 1.00 35.48  ? 3988 HIS A CD2   1 
ATOM   17904 C  CE1   . HIS A 1 3988 ? 246.091 174.826 216.148 1.00 44.88  ? 3988 HIS A CE1   1 
ATOM   17905 N  NE2   . HIS A 1 3988 ? 246.914 175.665 216.752 1.00 40.92  ? 3988 HIS A NE2   1 
ATOM   17906 N  N     . ARG A 1 3989 ? 244.864 179.570 211.640 1.00 27.37  ? 3989 ARG A N     1 
ATOM   17907 C  CA    . ARG A 1 3989 ? 244.944 180.574 210.585 1.00 22.64  ? 3989 ARG A CA    1 
ATOM   17908 C  C     . ARG A 1 3989 ? 244.437 181.924 211.073 1.00 21.43  ? 3989 ARG A C     1 
ATOM   17909 O  O     . ARG A 1 3989 ? 244.984 182.968 210.709 1.00 21.32  ? 3989 ARG A O     1 
ATOM   17910 C  CB    . ARG A 1 3989 ? 244.156 180.119 209.359 1.00 23.90  ? 3989 ARG A CB    1 
ATOM   17911 C  CG    . ARG A 1 3989 ? 244.800 178.993 208.576 1.00 24.39  ? 3989 ARG A CG    1 
ATOM   17912 C  CD    . ARG A 1 3989 ? 244.159 178.863 207.208 1.00 30.98  ? 3989 ARG A CD    1 
ATOM   17913 N  NE    . ARG A 1 3989 ? 243.798 177.486 206.890 1.00 34.97  ? 3989 ARG A NE    1 
ATOM   17914 C  CZ    . ARG A 1 3989 ? 244.643 176.584 206.410 1.00 41.99  ? 3989 ARG A CZ    1 
ATOM   17915 N  NH1   . ARG A 1 3989 ? 245.910 176.880 206.174 1.00 39.40  ? 3989 ARG A NH1   1 
ATOM   17916 N  NH2   . ARG A 1 3989 ? 244.203 175.355 206.158 1.00 43.85  ? 3989 ARG A NH2   1 
ATOM   17917 N  N     . LEU A 1 3990 ? 243.383 181.918 211.890 1.00 18.66  ? 3990 LEU A N     1 
ATOM   17918 C  CA    . LEU A 1 3990 ? 242.872 183.156 212.465 1.00 18.41  ? 3990 LEU A CA    1 
ATOM   17919 C  C     . LEU A 1 3990 ? 243.917 183.816 213.353 1.00 24.41  ? 3990 LEU A C     1 
ATOM   17920 O  O     . LEU A 1 3990 ? 244.110 185.036 213.301 1.00 25.55  ? 3990 LEU A O     1 
ATOM   17921 C  CB    . LEU A 1 3990 ? 241.596 182.863 213.251 1.00 15.27  ? 3990 LEU A CB    1 
ATOM   17922 C  CG    . LEU A 1 3990 ? 240.718 184.018 213.731 1.00 14.00  ? 3990 LEU A CG    1 
ATOM   17923 C  CD1   . LEU A 1 3990 ? 240.370 184.950 212.589 1.00 14.46  ? 3990 LEU A CD1   1 
ATOM   17924 C  CD2   . LEU A 1 3990 ? 239.458 183.475 214.383 1.00 14.18  ? 3990 LEU A CD2   1 
ATOM   17925 N  N     . LEU A 1 3991 ? 244.605 183.020 214.174 1.00 27.32  ? 3991 LEU A N     1 
ATOM   17926 C  CA    . LEU A 1 3991 ? 245.655 183.567 215.027 1.00 25.01  ? 3991 LEU A CA    1 
ATOM   17927 C  C     . LEU A 1 3991 ? 246.798 184.146 214.201 1.00 25.81  ? 3991 LEU A C     1 
ATOM   17928 O  O     . LEU A 1 3991 ? 247.295 185.243 214.492 1.00 28.88  ? 3991 LEU A O     1 
ATOM   17929 C  CB    . LEU A 1 3991 ? 246.171 182.489 215.978 1.00 28.96  ? 3991 LEU A CB    1 
ATOM   17930 C  CG    . LEU A 1 3991 ? 245.294 182.198 217.194 1.00 33.35  ? 3991 LEU A CG    1 
ATOM   17931 C  CD1   . LEU A 1 3991 ? 245.468 180.758 217.634 1.00 35.31  ? 3991 LEU A CD1   1 
ATOM   17932 C  CD2   . LEU A 1 3991 ? 245.605 183.153 218.332 1.00 30.94  ? 3991 LEU A CD2   1 
ATOM   17933 N  N     . LEU A 1 3992 ? 247.230 183.423 213.164 1.00 23.06  ? 3992 LEU A N     1 
ATOM   17934 C  CA    . LEU A 1 3992 ? 248.302 183.929 212.311 1.00 25.58  ? 3992 LEU A CA    1 
ATOM   17935 C  C     . LEU A 1 3992 ? 247.888 185.204 211.588 1.00 25.97  ? 3992 LEU A C     1 
ATOM   17936 O  O     . LEU A 1 3992 ? 248.699 186.122 211.431 1.00 30.74  ? 3992 LEU A O     1 
ATOM   17937 C  CB    . LEU A 1 3992 ? 248.741 182.867 211.305 1.00 29.37  ? 3992 LEU A CB    1 
ATOM   17938 C  CG    . LEU A 1 3992 ? 249.412 181.622 211.875 1.00 28.60  ? 3992 LEU A CG    1 
ATOM   17939 C  CD1   . LEU A 1 3992 ? 249.658 180.610 210.775 1.00 33.77  ? 3992 LEU A CD1   1 
ATOM   17940 C  CD2   . LEU A 1 3992 ? 250.720 182.025 212.523 1.00 24.04  ? 3992 LEU A CD2   1 
ATOM   17941 N  N     . ILE A 1 3993 ? 246.640 185.272 211.124 1.00 25.14  ? 3993 ILE A N     1 
ATOM   17942 C  CA    . ILE A 1 3993 ? 246.163 186.480 210.461 1.00 20.58  ? 3993 ILE A CA    1 
ATOM   17943 C  C     . ILE A 1 3993 ? 246.141 187.648 211.439 1.00 19.26  ? 3993 ILE A C     1 
ATOM   17944 O  O     . ILE A 1 3993 ? 246.559 188.761 211.103 1.00 23.48  ? 3993 ILE A O     1 
ATOM   17945 C  CB    . ILE A 1 3993 ? 244.779 186.229 209.834 1.00 19.28  ? 3993 ILE A CB    1 
ATOM   17946 C  CG1   . ILE A 1 3993 ? 244.924 185.486 208.505 1.00 19.21  ? 3993 ILE A CG1   1 
ATOM   17947 C  CG2   . ILE A 1 3993 ? 244.038 187.535 209.624 1.00 18.03  ? 3993 ILE A CG2   1 
ATOM   17948 C  CD1   . ILE A 1 3993 ? 245.568 186.304 207.415 1.00 16.79  ? 3993 ILE A CD1   1 
ATOM   17949 N  N     . GLN A 1 3994 ? 245.672 187.411 212.665 1.00 23.28  ? 3994 GLN A N     1 
ATOM   17950 C  CA    . GLN A 1 3994 ? 245.636 188.477 213.661 1.00 22.22  ? 3994 GLN A CA    1 
ATOM   17951 C  C     . GLN A 1 3994 ? 247.039 188.971 213.989 1.00 23.98  ? 3994 GLN A C     1 
ATOM   17952 O  O     . GLN A 1 3994 ? 247.247 190.170 214.210 1.00 24.84  ? 3994 GLN A O     1 
ATOM   17953 C  CB    . GLN A 1 3994 ? 244.927 187.989 214.924 1.00 21.22  ? 3994 GLN A CB    1 
ATOM   17954 C  CG    . GLN A 1 3994 ? 244.560 189.092 215.901 1.00 16.14  ? 3994 GLN A CG    1 
ATOM   17955 C  CD    . GLN A 1 3994 ? 244.229 188.561 217.280 1.00 18.26  ? 3994 GLN A CD    1 
ATOM   17956 O  OE1   . GLN A 1 3994 ? 244.529 187.415 217.606 1.00 25.96  ? 3994 GLN A OE1   1 
ATOM   17957 N  NE2   . GLN A 1 3994 ? 243.599 189.395 218.098 1.00 26.17  ? 3994 GLN A NE2   1 
ATOM   17958 N  N     . ALA A 1 3995 ? 248.013 188.062 214.032 1.00 27.52  ? 3995 ALA A N     1 
ATOM   17959 C  CA    . ALA A 1 3995 ? 249.383 188.469 214.331 1.00 25.93  ? 3995 ALA A CA    1 
ATOM   17960 C  C     . ALA A 1 3995 ? 250.024 189.197 213.155 1.00 27.90  ? 3995 ALA A C     1 
ATOM   17961 O  O     . ALA A 1 3995 ? 250.752 190.178 213.347 1.00 31.76  ? 3995 ALA A O     1 
ATOM   17962 C  CB    . ALA A 1 3995 ? 250.216 187.251 214.726 1.00 30.77  ? 3995 ALA A CB    1 
ATOM   17963 N  N     . PHE A 1 3996 ? 249.764 188.739 211.931 1.00 32.52  ? 3996 PHE A N     1 
ATOM   17964 C  CA    . PHE A 1 3996 ? 250.455 189.232 210.742 1.00 24.32  ? 3996 PHE A CA    1 
ATOM   17965 C  C     . PHE A 1 3996 ? 249.678 190.338 210.032 1.00 26.70  ? 3996 PHE A C     1 
ATOM   17966 O  O     . PHE A 1 3996 ? 250.194 191.443 209.842 1.00 35.56  ? 3996 PHE A O     1 
ATOM   17967 C  CB    . PHE A 1 3996 ? 250.717 188.067 209.782 1.00 24.48  ? 3996 PHE A CB    1 
ATOM   17968 C  CG    . PHE A 1 3996 ? 251.794 187.131 210.242 1.00 35.82  ? 3996 PHE A CG    1 
ATOM   17969 C  CD1   . PHE A 1 3996 ? 252.970 187.619 210.782 1.00 35.34  ? 3996 PHE A CD1   1 
ATOM   17970 C  CD2   . PHE A 1 3996 ? 251.624 185.760 210.149 1.00 37.92  ? 3996 PHE A CD2   1 
ATOM   17971 C  CE1   . PHE A 1 3996 ? 253.962 186.757 211.204 1.00 34.71  ? 3996 PHE A CE1   1 
ATOM   17972 C  CE2   . PHE A 1 3996 ? 252.612 184.895 210.574 1.00 40.18  ? 3996 PHE A CE2   1 
ATOM   17973 C  CZ    . PHE A 1 3996 ? 253.782 185.395 211.102 1.00 42.30  ? 3996 PHE A CZ    1 
ATOM   17974 N  N     . ARG A 1 3997 ? 248.442 190.053 209.629 1.00 26.61  ? 3997 ARG A N     1 
ATOM   17975 C  CA    . ARG A 1 3997 ? 247.649 190.952 208.793 1.00 21.50  ? 3997 ARG A CA    1 
ATOM   17976 C  C     . ARG A 1 3997 ? 246.313 191.212 209.474 1.00 19.02  ? 3997 ARG A C     1 
ATOM   17977 O  O     . ARG A 1 3997 ? 245.291 190.615 209.110 1.00 23.18  ? 3997 ARG A O     1 
ATOM   17978 C  CB    . ARG A 1 3997 ? 247.445 190.365 207.395 1.00 20.06  ? 3997 ARG A CB    1 
ATOM   17979 C  CG    . ARG A 1 3997 ? 248.726 190.197 206.596 1.00 18.50  ? 3997 ARG A CG    1 
ATOM   17980 C  CD    . ARG A 1 3997 ? 249.206 191.522 206.038 1.00 23.37  ? 3997 ARG A CD    1 
ATOM   17981 N  NE    . ARG A 1 3997 ? 248.223 192.126 205.146 1.00 23.33  ? 3997 ARG A NE    1 
ATOM   17982 C  CZ    . ARG A 1 3997 ? 248.055 191.784 203.876 1.00 22.06  ? 3997 ARG A CZ    1 
ATOM   17983 N  NH1   . ARG A 1 3997 ? 248.795 190.846 203.309 1.00 24.37  ? 3997 ARG A NH1   1 
ATOM   17984 N  NH2   . ARG A 1 3997 ? 247.122 192.400 203.157 1.00 24.15  ? 3997 ARG A NH2   1 
ATOM   17985 N  N     . PRO A 1 3998 ? 246.286 192.094 210.477 1.00 18.11  ? 3998 PRO A N     1 
ATOM   17986 C  CA    . PRO A 1 3998 ? 245.012 192.385 211.156 1.00 19.31  ? 3998 PRO A CA    1 
ATOM   17987 C  C     . PRO A 1 3998 ? 243.955 192.970 210.238 1.00 17.25  ? 3998 PRO A C     1 
ATOM   17988 O  O     . PRO A 1 3998 ? 242.758 192.811 210.509 1.00 21.29  ? 3998 PRO A O     1 
ATOM   17989 C  CB    . PRO A 1 3998 ? 245.420 193.377 212.256 1.00 18.59  ? 3998 PRO A CB    1 
ATOM   17990 C  CG    . PRO A 1 3998 ? 246.717 193.948 211.800 1.00 16.13  ? 3998 PRO A CG    1 
ATOM   17991 C  CD    . PRO A 1 3998 ? 247.406 192.857 211.047 1.00 17.93  ? 3998 PRO A CD    1 
ATOM   17992 N  N     . ASP A 1 3999 ? 244.361 193.641 209.157 1.00 18.66  ? 3999 ASP A N     1 
ATOM   17993 C  CA    . ASP A 1 3999 ? 243.394 194.223 208.233 1.00 15.91  ? 3999 ASP A CA    1 
ATOM   17994 C  C     . ASP A 1 3999 ? 242.506 193.161 207.600 1.00 16.13  ? 3999 ASP A C     1 
ATOM   17995 O  O     . ASP A 1 3999 ? 241.355 193.442 207.252 1.00 22.06  ? 3999 ASP A O     1 
ATOM   17996 C  CB    . ASP A 1 3999 ? 244.121 195.024 207.153 1.00 17.95  ? 3999 ASP A CB    1 
ATOM   17997 C  CG    . ASP A 1 3999 ? 245.192 194.212 206.448 1.00 26.51  ? 3999 ASP A CG    1 
ATOM   17998 O  OD1   . ASP A 1 3999 ? 246.264 193.989 207.047 1.00 28.13  ? 3999 ASP A OD1   1 
ATOM   17999 O  OD2   . ASP A 1 3999 ? 244.963 193.799 205.291 1.00 26.77  ? 3999 ASP A OD2   1 
ATOM   18000 N  N     . ARG A 1 4000 ? 243.017 191.944 207.441 1.00 15.53  ? 4000 ARG A N     1 
ATOM   18001 C  CA    . ARG A 1 4000 ? 242.237 190.840 206.899 1.00 17.09  ? 4000 ARG A CA    1 
ATOM   18002 C  C     . ARG A 1 4000 ? 241.535 190.028 207.978 1.00 14.56  ? 4000 ARG A C     1 
ATOM   18003 O  O     . ARG A 1 4000 ? 240.842 189.059 207.646 1.00 16.38  ? 4000 ARG A O     1 
ATOM   18004 C  CB    . ARG A 1 4000 ? 243.133 189.921 206.065 1.00 16.38  ? 4000 ARG A CB    1 
ATOM   18005 C  CG    . ARG A 1 4000 ? 243.941 190.646 205.007 1.00 18.68  ? 4000 ARG A CG    1 
ATOM   18006 C  CD    . ARG A 1 4000 ? 243.038 191.410 204.058 1.00 19.18  ? 4000 ARG A CD    1 
ATOM   18007 N  NE    . ARG A 1 4000 ? 242.035 190.550 203.445 1.00 18.96  ? 4000 ARG A NE    1 
ATOM   18008 C  CZ    . ARG A 1 4000 ? 240.968 190.993 202.796 1.00 24.03  ? 4000 ARG A CZ    1 
ATOM   18009 N  NH1   . ARG A 1 4000 ? 240.724 192.286 202.668 1.00 25.51  ? 4000 ARG A NH1   1 
ATOM   18010 N  NH2   . ARG A 1 4000 ? 240.122 190.116 202.262 1.00 21.44  ? 4000 ARG A NH2   1 
ATOM   18011 N  N     . LEU A 1 4001 ? 241.678 190.418 209.249 1.00 13.26  ? 4001 LEU A N     1 
ATOM   18012 C  CA    . LEU A 1 4001 ? 241.142 189.628 210.354 1.00 10.53  ? 4001 LEU A CA    1 
ATOM   18013 C  C     . LEU A 1 4001 ? 239.666 189.319 210.152 1.00 9.29   ? 4001 LEU A C     1 
ATOM   18014 O  O     . LEU A 1 4001 ? 239.252 188.155 210.198 1.00 14.27  ? 4001 LEU A O     1 
ATOM   18015 C  CB    . LEU A 1 4001 ? 241.354 190.372 211.674 1.00 8.79   ? 4001 LEU A CB    1 
ATOM   18016 C  CG    . LEU A 1 4001 ? 241.078 189.587 212.957 1.00 9.84   ? 4001 LEU A CG    1 
ATOM   18017 C  CD1   . LEU A 1 4001 ? 241.865 188.290 212.969 1.00 16.56  ? 4001 LEU A CD1   1 
ATOM   18018 C  CD2   . LEU A 1 4001 ? 241.394 190.423 214.185 1.00 10.95  ? 4001 LEU A CD2   1 
ATOM   18019 N  N     . LEU A 1 4002 ? 238.865 190.355 209.885 1.00 9.02   ? 4002 LEU A N     1 
ATOM   18020 C  CA    . LEU A 1 4002 ? 237.438 190.158 209.657 1.00 7.93   ? 4002 LEU A CA    1 
ATOM   18021 C  C     . LEU A 1 4002 ? 237.201 189.103 208.588 1.00 9.07   ? 4002 LEU A C     1 
ATOM   18022 O  O     . LEU A 1 4002 ? 236.425 188.160 208.790 1.00 12.21  ? 4002 LEU A O     1 
ATOM   18023 C  CB    . LEU A 1 4002 ? 236.783 191.482 209.258 1.00 9.12   ? 4002 LEU A CB    1 
ATOM   18024 C  CG    . LEU A 1 4002 ? 236.403 192.431 210.394 1.00 9.30   ? 4002 LEU A CG    1 
ATOM   18025 C  CD1   . LEU A 1 4002 ? 235.659 193.635 209.847 1.00 14.78  ? 4002 LEU A CD1   1 
ATOM   18026 C  CD2   . LEU A 1 4002 ? 235.570 191.714 211.441 1.00 11.89  ? 4002 LEU A CD2   1 
ATOM   18027 N  N     . ALA A 1 4003 ? 237.902 189.222 207.457 1.00 10.63  ? 4003 ALA A N     1 
ATOM   18028 C  CA    . ALA A 1 4003 ? 237.766 188.225 206.402 1.00 10.15  ? 4003 ALA A CA    1 
ATOM   18029 C  C     . ALA A 1 4003 ? 238.068 186.835 206.938 1.00 12.54  ? 4003 ALA A C     1 
ATOM   18030 O  O     . ALA A 1 4003 ? 237.260 185.909 206.785 1.00 12.61  ? 4003 ALA A O     1 
ATOM   18031 C  CB    . ALA A 1 4003 ? 238.691 188.570 205.234 1.00 9.17   ? 4003 ALA A CB    1 
ATOM   18032 N  N     . MET A 1 4004 ? 239.199 186.688 207.631 1.00 13.89  ? 4004 MET A N     1 
ATOM   18033 C  CA    . MET A 1 4004 ? 239.541 185.396 208.207 1.00 12.67  ? 4004 MET A CA    1 
ATOM   18034 C  C     . MET A 1 4004 ? 238.456 184.935 209.166 1.00 12.47  ? 4004 MET A C     1 
ATOM   18035 O  O     . MET A 1 4004 ? 238.081 183.755 209.173 1.00 16.65  ? 4004 MET A O     1 
ATOM   18036 C  CB    . MET A 1 4004 ? 240.894 185.478 208.913 1.00 11.00  ? 4004 MET A CB    1 
ATOM   18037 C  CG    . MET A 1 4004 ? 241.496 184.133 209.279 1.00 16.93  ? 4004 MET A CG    1 
ATOM   18038 S  SD    . MET A 1 4004 ? 241.654 183.002 207.885 1.00 31.91  ? 4004 MET A SD    1 
ATOM   18039 C  CE    . MET A 1 4004 ? 240.800 181.565 208.521 1.00 20.15  ? 4004 MET A CE    1 
ATOM   18040 N  N     . ALA A 1 4005 ? 237.901 185.868 209.947 1.00 9.81   ? 4005 ALA A N     1 
ATOM   18041 C  CA    . ALA A 1 4005 ? 236.823 185.515 210.859 1.00 7.39   ? 4005 ALA A CA    1 
ATOM   18042 C  C     . ALA A 1 4005 ? 235.664 184.889 210.103 1.00 10.33  ? 4005 ALA A C     1 
ATOM   18043 O  O     . ALA A 1 4005 ? 235.139 183.845 210.511 1.00 14.94  ? 4005 ALA A O     1 
ATOM   18044 C  CB    . ALA A 1 4005 ? 236.361 186.749 211.632 1.00 9.79   ? 4005 ALA A CB    1 
ATOM   18045 N  N     . HIS A 1 4006 ? 235.286 185.483 208.966 1.00 10.54  ? 4006 HIS A N     1 
ATOM   18046 C  CA    . HIS A 1 4006 ? 234.218 184.901 208.164 1.00 12.14  ? 4006 HIS A CA    1 
ATOM   18047 C  C     . HIS A 1 4006 ? 234.556 183.470 207.785 1.00 11.24  ? 4006 HIS A C     1 
ATOM   18048 O  O     . HIS A 1 4006 ? 233.719 182.569 207.925 1.00 13.60  ? 4006 HIS A O     1 
ATOM   18049 C  CB    . HIS A 1 4006 ? 233.970 185.748 206.916 1.00 10.98  ? 4006 HIS A CB    1 
ATOM   18050 C  CG    . HIS A 1 4006 ? 233.073 186.922 207.154 1.00 11.01  ? 4006 HIS A CG    1 
ATOM   18051 N  ND1   . HIS A 1 4006 ? 233.505 188.077 207.768 1.00 13.10  ? 4006 HIS A ND1   1 
ATOM   18052 C  CD2   . HIS A 1 4006 ? 231.765 187.117 206.864 1.00 12.89  ? 4006 HIS A CD2   1 
ATOM   18053 C  CE1   . HIS A 1 4006 ? 232.503 188.935 207.843 1.00 15.65  ? 4006 HIS A CE1   1 
ATOM   18054 N  NE2   . HIS A 1 4006 ? 231.436 188.376 207.302 1.00 16.63  ? 4006 HIS A NE2   1 
ATOM   18055 N  N     . MET A 1 4007 ? 235.800 183.234 207.359 1.00 13.81  ? 4007 MET A N     1 
ATOM   18056 C  CA    . MET A 1 4007 ? 236.215 181.880 207.022 1.00 12.37  ? 4007 MET A CA    1 
ATOM   18057 C  C     . MET A 1 4007 ? 235.995 180.942 208.197 1.00 12.38  ? 4007 MET A C     1 
ATOM   18058 O  O     . MET A 1 4007 ? 235.450 179.844 208.029 1.00 14.27  ? 4007 MET A O     1 
ATOM   18059 C  CB    . MET A 1 4007 ? 237.679 181.874 206.584 1.00 13.11  ? 4007 MET A CB    1 
ATOM   18060 C  CG    . MET A 1 4007 ? 237.887 182.278 205.133 1.00 14.12  ? 4007 MET A CG    1 
ATOM   18061 S  SD    . MET A 1 4007 ? 239.575 182.016 204.557 1.00 34.85  ? 4007 MET A SD    1 
ATOM   18062 C  CE    . MET A 1 4007 ? 239.367 180.553 203.548 1.00 24.02  ? 4007 MET A CE    1 
ATOM   18063 N  N     . PHE A 1 4008 ? 236.356 181.385 209.406 1.00 14.61  ? 4008 PHE A N     1 
ATOM   18064 C  CA    . PHE A 1 4008 ? 236.142 180.555 210.587 1.00 12.60  ? 4008 PHE A CA    1 
ATOM   18065 C  C     . PHE A 1 4008 ? 234.675 180.180 210.725 1.00 11.64  ? 4008 PHE A C     1 
ATOM   18066 O  O     . PHE A 1 4008 ? 234.345 179.011 210.965 1.00 14.08  ? 4008 PHE A O     1 
ATOM   18067 C  CB    . PHE A 1 4008 ? 236.637 181.283 211.836 1.00 10.60  ? 4008 PHE A CB    1 
ATOM   18068 C  CG    . PHE A 1 4008 ? 236.336 180.559 213.118 1.00 12.94  ? 4008 PHE A CG    1 
ATOM   18069 C  CD1   . PHE A 1 4008 ? 237.036 179.418 213.465 1.00 16.34  ? 4008 PHE A CD1   1 
ATOM   18070 C  CD2   . PHE A 1 4008 ? 235.356 181.022 213.976 1.00 11.05  ? 4008 PHE A CD2   1 
ATOM   18071 C  CE1   . PHE A 1 4008 ? 236.760 178.753 214.642 1.00 15.30  ? 4008 PHE A CE1   1 
ATOM   18072 C  CE2   . PHE A 1 4008 ? 235.077 180.362 215.155 1.00 12.35  ? 4008 PHE A CE2   1 
ATOM   18073 C  CZ    . PHE A 1 4008 ? 235.782 179.227 215.489 1.00 14.31  ? 4008 PHE A CZ    1 
ATOM   18074 N  N     . VAL A 1 4009 ? 233.777 181.149 210.532 1.00 9.83   ? 4009 VAL A N     1 
ATOM   18075 C  CA    . VAL A 1 4009 ? 232.352 180.851 210.608 1.00 9.72   ? 4009 VAL A CA    1 
ATOM   18076 C  C     . VAL A 1 4009 ? 231.982 179.808 209.564 1.00 13.82  ? 4009 VAL A C     1 
ATOM   18077 O  O     . VAL A 1 4009 ? 231.249 178.851 209.850 1.00 20.60  ? 4009 VAL A O     1 
ATOM   18078 C  CB    . VAL A 1 4009 ? 231.524 182.140 210.449 1.00 9.39   ? 4009 VAL A CB    1 
ATOM   18079 C  CG1   . VAL A 1 4009 ? 230.042 181.818 210.400 1.00 11.29  ? 4009 VAL A CG1   1 
ATOM   18080 C  CG2   . VAL A 1 4009 ? 231.823 183.102 211.585 1.00 7.98   ? 4009 VAL A CG2   1 
ATOM   18081 N  N     . SER A 1 4010 ? 232.519 179.949 208.351 1.00 12.61  ? 4010 SER A N     1 
ATOM   18082 C  CA    . SER A 1 4010 ? 232.233 178.984 207.299 1.00 13.11  ? 4010 SER A CA    1 
ATOM   18083 C  C     . SER A 1 4010 ? 232.734 177.590 207.647 1.00 16.28  ? 4010 SER A C     1 
ATOM   18084 O  O     . SER A 1 4010 ? 232.198 176.605 207.129 1.00 20.04  ? 4010 SER A O     1 
ATOM   18085 C  CB    . SER A 1 4010 ? 232.848 179.449 205.980 1.00 18.04  ? 4010 SER A CB    1 
ATOM   18086 O  OG    . SER A 1 4010 ? 232.256 180.659 205.542 1.00 22.93  ? 4010 SER A OG    1 
ATOM   18087 N  N     . THR A 1 4011 ? 233.742 177.480 208.516 1.00 16.04  ? 4011 THR A N     1 
ATOM   18088 C  CA    . THR A 1 4011 ? 234.227 176.156 208.888 1.00 14.80  ? 4011 THR A CA    1 
ATOM   18089 C  C     . THR A 1 4011 ? 233.327 175.499 209.924 1.00 20.70  ? 4011 THR A C     1 
ATOM   18090 O  O     . THR A 1 4011 ? 233.419 174.286 210.140 1.00 30.94  ? 4011 THR A O     1 
ATOM   18091 C  CB    . THR A 1 4011 ? 235.660 176.238 209.414 1.00 16.87  ? 4011 THR A CB    1 
ATOM   18092 O  OG1   . THR A 1 4011 ? 235.684 176.980 210.640 1.00 22.03  ? 4011 THR A OG1   1 
ATOM   18093 C  CG2   . THR A 1 4011 ? 236.566 176.906 208.395 1.00 15.48  ? 4011 THR A CG2   1 
ATOM   18094 N  N     . ASN A 1 4012 ? 232.454 176.270 210.571 1.00 15.71  ? 4012 ASN A N     1 
ATOM   18095 C  CA    . ASN A 1 4012 ? 231.602 175.742 211.631 1.00 15.39  ? 4012 ASN A CA    1 
ATOM   18096 C  C     . ASN A 1 4012 ? 230.133 175.702 211.225 1.00 17.39  ? 4012 ASN A C     1 
ATOM   18097 O  O     . ASN A 1 4012 ? 229.478 174.663 211.353 1.00 19.84  ? 4012 ASN A O     1 
ATOM   18098 C  CB    . ASN A 1 4012 ? 231.781 176.572 212.908 1.00 16.60  ? 4012 ASN A CB    1 
ATOM   18099 C  CG    . ASN A 1 4012 ? 233.067 176.247 213.637 1.00 18.64  ? 4012 ASN A CG    1 
ATOM   18100 O  OD1   . ASN A 1 4012 ? 233.366 175.085 213.904 1.00 33.21  ? 4012 ASN A OD1   1 
ATOM   18101 N  ND2   . ASN A 1 4012 ? 233.838 177.274 213.959 1.00 14.79  ? 4012 ASN A ND2   1 
ATOM   18102 N  N     . LEU A 1 4013 ? 229.601 176.819 210.739 1.00 14.94  ? 4013 LEU A N     1 
ATOM   18103 C  CA    . LEU A 1 4013 ? 228.177 176.948 210.473 1.00 13.42  ? 4013 LEU A CA    1 
ATOM   18104 C  C     . LEU A 1 4013 ? 227.823 176.862 208.994 1.00 16.68  ? 4013 LEU A C     1 
ATOM   18105 O  O     . LEU A 1 4013 ? 226.657 177.058 208.640 1.00 19.83  ? 4013 LEU A O     1 
ATOM   18106 C  CB    . LEU A 1 4013 ? 227.660 178.264 211.054 1.00 14.45  ? 4013 LEU A CB    1 
ATOM   18107 C  CG    . LEU A 1 4013 ? 227.821 178.431 212.566 1.00 9.64   ? 4013 LEU A CG    1 
ATOM   18108 C  CD1   . LEU A 1 4013 ? 228.090 179.882 212.914 1.00 7.37   ? 4013 LEU A CD1   1 
ATOM   18109 C  CD2   . LEU A 1 4013 ? 226.592 177.922 213.293 1.00 10.81  ? 4013 LEU A CD2   1 
ATOM   18110 N  N     . GLY A 1 4014 ? 228.786 176.575 208.128 1.00 16.84  ? 4014 GLY A N     1 
ATOM   18111 C  CA    . GLY A 1 4014 ? 228.510 176.432 206.715 1.00 13.08  ? 4014 GLY A CA    1 
ATOM   18112 C  C     . GLY A 1 4014 ? 228.889 177.670 205.919 1.00 22.33  ? 4014 GLY A C     1 
ATOM   18113 O  O     . GLY A 1 4014 ? 229.018 178.778 206.447 1.00 23.23  ? 4014 GLY A O     1 
ATOM   18114 N  N     . GLU A 1 4015 ? 229.062 177.469 204.612 1.00 28.41  ? 4015 GLU A N     1 
ATOM   18115 C  CA    . GLU A 1 4015 ? 229.511 178.553 203.743 1.00 24.99  ? 4015 GLU A CA    1 
ATOM   18116 C  C     . GLU A 1 4015 ? 228.429 179.604 203.532 1.00 26.60  ? 4015 GLU A C     1 
ATOM   18117 O  O     . GLU A 1 4015 ? 228.745 180.771 203.275 1.00 26.20  ? 4015 GLU A O     1 
ATOM   18118 C  CB    . GLU A 1 4015 ? 229.967 177.990 202.398 1.00 22.33  ? 4015 GLU A CB    1 
ATOM   18119 C  CG    . GLU A 1 4015 ? 231.204 177.116 202.478 1.00 32.56  ? 4015 GLU A CG    1 
ATOM   18120 C  CD    . GLU A 1 4015 ? 232.442 177.892 202.878 1.00 43.06  ? 4015 GLU A CD    1 
ATOM   18121 O  OE1   . GLU A 1 4015 ? 232.534 179.087 202.529 1.00 47.19  ? 4015 GLU A OE1   1 
ATOM   18122 O  OE2   . GLU A 1 4015 ? 233.324 177.305 203.540 1.00 40.96  ? 4015 GLU A OE2   1 
ATOM   18123 N  N     . SER A 1 4016 ? 227.158 179.218 203.632 1.00 22.34  ? 4016 SER A N     1 
ATOM   18124 C  CA    . SER A 1 4016 ? 226.043 180.119 203.374 1.00 19.44  ? 4016 SER A CA    1 
ATOM   18125 C  C     . SER A 1 4016 ? 225.330 180.544 204.652 1.00 22.17  ? 4016 SER A C     1 
ATOM   18126 O  O     . SER A 1 4016 ? 224.157 180.926 204.605 1.00 22.76  ? 4016 SER A O     1 
ATOM   18127 C  CB    . SER A 1 4016 ? 225.054 179.470 202.406 1.00 23.53  ? 4016 SER A CB    1 
ATOM   18128 O  OG    . SER A 1 4016 ? 224.642 178.198 202.873 1.00 26.73  ? 4016 SER A OG    1 
ATOM   18129 N  N     . PHE A 1 4017 ? 226.014 180.481 205.796 1.00 18.86  ? 4017 PHE A N     1 
ATOM   18130 C  CA    . PHE A 1 4017 ? 225.382 180.843 207.060 1.00 13.33  ? 4017 PHE A CA    1 
ATOM   18131 C  C     . PHE A 1 4017 ? 225.016 182.323 207.093 1.00 13.12  ? 4017 PHE A C     1 
ATOM   18132 O  O     . PHE A 1 4017 ? 223.941 182.695 207.577 1.00 15.93  ? 4017 PHE A O     1 
ATOM   18133 C  CB    . PHE A 1 4017 ? 226.305 180.489 208.226 1.00 12.49  ? 4017 PHE A CB    1 
ATOM   18134 C  CG    . PHE A 1 4017 ? 225.664 180.645 209.572 1.00 9.72   ? 4017 PHE A CG    1 
ATOM   18135 C  CD1   . PHE A 1 4017 ? 224.705 179.747 210.003 1.00 7.02   ? 4017 PHE A CD1   1 
ATOM   18136 C  CD2   . PHE A 1 4017 ? 226.021 181.689 210.408 1.00 10.83  ? 4017 PHE A CD2   1 
ATOM   18137 C  CE1   . PHE A 1 4017 ? 224.116 179.885 211.240 1.00 7.06   ? 4017 PHE A CE1   1 
ATOM   18138 C  CE2   . PHE A 1 4017 ? 225.431 181.832 211.645 1.00 8.92   ? 4017 PHE A CE2   1 
ATOM   18139 C  CZ    . PHE A 1 4017 ? 224.480 180.927 212.062 1.00 6.19   ? 4017 PHE A CZ    1 
ATOM   18140 N  N     . MET A 1 4018 ? 225.897 183.180 206.582 1.00 13.22  ? 4018 MET A N     1 
ATOM   18141 C  CA    . MET A 1 4018 ? 225.680 184.620 206.578 1.00 12.93  ? 4018 MET A CA    1 
ATOM   18142 C  C     . MET A 1 4018 ? 225.216 185.144 205.223 1.00 19.33  ? 4018 MET A C     1 
ATOM   18143 O  O     . MET A 1 4018 ? 225.238 186.358 204.996 1.00 23.63  ? 4018 MET A O     1 
ATOM   18144 C  CB    . MET A 1 4018 ? 226.953 185.348 207.008 1.00 11.55  ? 4018 MET A CB    1 
ATOM   18145 C  CG    . MET A 1 4018 ? 227.471 184.958 208.375 1.00 7.85   ? 4018 MET A CG    1 
ATOM   18146 S  SD    . MET A 1 4018 ? 229.054 185.744 208.714 1.00 14.65  ? 4018 MET A SD    1 
ATOM   18147 C  CE    . MET A 1 4018 ? 228.517 187.126 209.710 1.00 6.50   ? 4018 MET A CE    1 
ATOM   18148 N  N     . SER A 1 4019 ? 224.798 184.258 204.322 1.00 20.76  ? 4019 SER A N     1 
ATOM   18149 C  CA    . SER A 1 4019 ? 224.384 184.674 202.989 1.00 21.49  ? 4019 SER A CA    1 
ATOM   18150 C  C     . SER A 1 4019 ? 223.038 185.388 202.972 1.00 22.22  ? 4019 SER A C     1 
ATOM   18151 O  O     . SER A 1 4019 ? 222.740 186.084 201.997 1.00 27.33  ? 4019 SER A O     1 
ATOM   18152 C  CB    . SER A 1 4019 ? 224.336 183.464 202.054 1.00 23.11  ? 4019 SER A CB    1 
ATOM   18153 O  OG    . SER A 1 4019 ? 223.324 182.556 202.448 1.00 30.00  ? 4019 SER A OG    1 
ATOM   18154 N  N     . ILE A 1 4020 ? 222.218 185.230 204.011 1.00 20.58  ? 4020 ILE A N     1 
ATOM   18155 C  CA    . ILE A 1 4020 ? 220.920 185.899 204.035 1.00 19.92  ? 4020 ILE A CA    1 
ATOM   18156 C  C     . ILE A 1 4020 ? 221.093 187.401 204.224 1.00 20.86  ? 4020 ILE A C     1 
ATOM   18157 O  O     . ILE A 1 4020 ? 220.370 188.204 203.621 1.00 22.05  ? 4020 ILE A O     1 
ATOM   18158 C  CB    . ILE A 1 4020 ? 220.024 185.285 205.125 1.00 19.49  ? 4020 ILE A CB    1 
ATOM   18159 C  CG1   . ILE A 1 4020 ? 219.805 183.797 204.848 1.00 22.47  ? 4020 ILE A CG1   1 
ATOM   18160 C  CG2   . ILE A 1 4020 ? 218.692 186.009 205.199 1.00 12.53  ? 4020 ILE A CG2   1 
ATOM   18161 C  CD1   . ILE A 1 4020 ? 219.040 183.527 203.575 1.00 15.75  ? 4020 ILE A CD1   1 
ATOM   18162 N  N     . MET A 1 4021 ? 222.052 187.806 205.057 1.00 21.21  ? 4021 MET A N     1 
ATOM   18163 C  CA    . MET A 1 4021 ? 222.252 189.219 205.359 1.00 17.96  ? 4021 MET A CA    1 
ATOM   18164 C  C     . MET A 1 4021 ? 222.725 190.030 204.160 1.00 22.43  ? 4021 MET A C     1 
ATOM   18165 O  O     . MET A 1 4021 ? 222.616 191.260 204.191 1.00 26.61  ? 4021 MET A O     1 
ATOM   18166 C  CB    . MET A 1 4021 ? 223.249 189.369 206.508 1.00 15.39  ? 4021 MET A CB    1 
ATOM   18167 C  CG    . MET A 1 4021 ? 222.766 188.786 207.825 1.00 15.12  ? 4021 MET A CG    1 
ATOM   18168 S  SD    . MET A 1 4021 ? 221.120 189.371 208.276 1.00 24.42  ? 4021 MET A SD    1 
ATOM   18169 C  CE    . MET A 1 4021 ? 220.157 187.876 208.080 1.00 10.22  ? 4021 MET A CE    1 
ATOM   18170 N  N     . GLU A 1 4022 ? 223.240 189.388 203.116 1.00 27.17  ? 4022 GLU A N     1 
ATOM   18171 C  CA    . GLU A 1 4022 ? 223.663 190.094 201.916 1.00 22.65  ? 4022 GLU A CA    1 
ATOM   18172 C  C     . GLU A 1 4022 ? 222.557 190.202 200.877 1.00 19.30  ? 4022 GLU A C     1 
ATOM   18173 O  O     . GLU A 1 4022 ? 222.789 190.762 199.801 1.00 22.58  ? 4022 GLU A O     1 
ATOM   18174 C  CB    . GLU A 1 4022 ? 224.890 189.408 201.301 1.00 25.02  ? 4022 GLU A CB    1 
ATOM   18175 C  CG    . GLU A 1 4022 ? 224.582 188.136 200.533 1.00 29.32  ? 4022 GLU A CG    1 
ATOM   18176 C  CD    . GLU A 1 4022 ? 225.825 187.328 200.215 1.00 38.50  ? 4022 GLU A CD    1 
ATOM   18177 O  OE1   . GLU A 1 4022 ? 226.751 187.301 201.054 1.00 41.24  ? 4022 GLU A OE1   1 
ATOM   18178 O  OE2   . GLU A 1 4022 ? 225.879 186.723 199.125 1.00 37.74  ? 4022 GLU A OE2   1 
ATOM   18179 N  N     . GLN A 1 4023 ? 221.365 189.688 201.172 1.00 21.76  ? 4023 GLN A N     1 
ATOM   18180 C  CA    . GLN A 1 4023 ? 220.195 189.737 200.314 1.00 20.60  ? 4023 GLN A CA    1 
ATOM   18181 C  C     . GLN A 1 4023 ? 219.224 190.808 200.798 1.00 26.34  ? 4023 GLN A C     1 
ATOM   18182 O  O     . GLN A 1 4023 ? 219.193 191.133 201.988 1.00 26.23  ? 4023 GLN A O     1 
ATOM   18183 C  CB    . GLN A 1 4023 ? 219.484 188.381 200.287 1.00 17.44  ? 4023 GLN A CB    1 
ATOM   18184 C  CG    . GLN A 1 4023 ? 220.396 187.207 199.976 1.00 23.31  ? 4023 GLN A CG    1 
ATOM   18185 C  CD    . GLN A 1 4023 ? 221.004 187.291 198.590 1.00 30.35  ? 4023 GLN A CD    1 
ATOM   18186 O  OE1   . GLN A 1 4023 ? 220.403 187.839 197.667 1.00 30.61  ? 4023 GLN A OE1   1 
ATOM   18187 N  NE2   . GLN A 1 4023 ? 222.205 186.746 198.439 1.00 26.85  ? 4023 GLN A NE2   1 
ATOM   18188 N  N     . PRO A 1 4024 ? 218.433 191.387 199.895 1.00 26.75  ? 4024 PRO A N     1 
ATOM   18189 C  CA    . PRO A 1 4024 ? 217.460 192.401 200.317 1.00 21.30  ? 4024 PRO A CA    1 
ATOM   18190 C  C     . PRO A 1 4024 ? 216.459 191.829 201.310 1.00 23.03  ? 4024 PRO A C     1 
ATOM   18191 O  O     . PRO A 1 4024 ? 216.044 190.672 201.210 1.00 27.37  ? 4024 PRO A O     1 
ATOM   18192 C  CB    . PRO A 1 4024 ? 216.783 192.815 199.005 1.00 13.65  ? 4024 PRO A CB    1 
ATOM   18193 C  CG    . PRO A 1 4024 ? 217.101 191.725 198.035 1.00 16.95  ? 4024 PRO A CG    1 
ATOM   18194 C  CD    . PRO A 1 4024 ? 218.441 191.209 198.434 1.00 20.37  ? 4024 PRO A CD    1 
ATOM   18195 N  N     . LEU A 1 4025 ? 216.078 192.658 202.278 1.00 24.27  ? 4025 LEU A N     1 
ATOM   18196 C  CA    . LEU A 1 4025 ? 215.144 192.232 203.309 1.00 24.52  ? 4025 LEU A CA    1 
ATOM   18197 C  C     . LEU A 1 4025 ? 213.784 191.921 202.698 1.00 32.60  ? 4025 LEU A C     1 
ATOM   18198 O  O     . LEU A 1 4025 ? 213.218 192.734 201.961 1.00 31.70  ? 4025 LEU A O     1 
ATOM   18199 C  CB    . LEU A 1 4025 ? 215.013 193.321 204.375 1.00 21.66  ? 4025 LEU A CB    1 
ATOM   18200 C  CG    . LEU A 1 4025 ? 213.944 193.146 205.452 1.00 18.68  ? 4025 LEU A CG    1 
ATOM   18201 C  CD1   . LEU A 1 4025 ? 214.112 191.821 206.166 1.00 26.71  ? 4025 LEU A CD1   1 
ATOM   18202 C  CD2   . LEU A 1 4025 ? 213.993 194.296 206.441 1.00 16.39  ? 4025 LEU A CD2   1 
ATOM   18203 N  N     . ASP A 1 4026 ? 213.261 190.739 203.008 1.00 31.70  ? 4026 ASP A N     1 
ATOM   18204 C  CA    . ASP A 1 4026 ? 211.963 190.284 202.521 1.00 31.47  ? 4026 ASP A CA    1 
ATOM   18205 C  C     . ASP A 1 4026 ? 210.959 190.490 203.650 1.00 30.89  ? 4026 ASP A C     1 
ATOM   18206 O  O     . ASP A 1 4026 ? 210.653 189.568 204.407 1.00 33.92  ? 4026 ASP A O     1 
ATOM   18207 C  CB    . ASP A 1 4026 ? 212.015 188.829 202.074 1.00 38.89  ? 4026 ASP A CB    1 
ATOM   18208 C  CG    . ASP A 1 4026 ? 210.683 188.333 201.553 1.00 42.49  ? 4026 ASP A CG    1 
ATOM   18209 O  OD1   . ASP A 1 4026 ? 210.159 188.932 200.591 1.00 48.12  ? 4026 ASP A OD1   1 
ATOM   18210 O  OD2   . ASP A 1 4026 ? 210.160 187.347 202.108 1.00 34.22  ? 4026 ASP A OD2   1 
ATOM   18211 N  N     . LEU A 1 4027 ? 210.442 191.713 203.753 1.00 31.46  ? 4027 LEU A N     1 
ATOM   18212 C  CA    . LEU A 1 4027 ? 209.544 192.057 204.845 1.00 29.55  ? 4027 LEU A CA    1 
ATOM   18213 C  C     . LEU A 1 4027 ? 208.165 191.431 204.692 1.00 26.52  ? 4027 LEU A C     1 
ATOM   18214 O  O     . LEU A 1 4027 ? 207.417 191.379 205.670 1.00 26.31  ? 4027 LEU A O     1 
ATOM   18215 C  CB    . LEU A 1 4027 ? 209.422 193.574 204.953 1.00 25.41  ? 4027 LEU A CB    1 
ATOM   18216 C  CG    . LEU A 1 4027 ? 210.358 194.280 205.927 1.00 27.08  ? 4027 LEU A CG    1 
ATOM   18217 C  CD1   . LEU A 1 4027 ? 210.054 195.759 205.924 1.00 24.63  ? 4027 LEU A CD1   1 
ATOM   18218 C  CD2   . LEU A 1 4027 ? 210.217 193.704 207.326 1.00 26.45  ? 4027 LEU A CD2   1 
ATOM   18219 N  N     . THR A 1 4028 ? 207.813 190.955 203.497 1.00 30.25  ? 4028 THR A N     1 
ATOM   18220 C  CA    . THR A 1 4028 ? 206.490 190.373 203.298 1.00 32.83  ? 4028 THR A CA    1 
ATOM   18221 C  C     . THR A 1 4028 ? 206.318 189.101 204.120 1.00 32.18  ? 4028 THR A C     1 
ATOM   18222 O  O     . THR A 1 4028 ? 205.335 188.948 204.855 1.00 35.65  ? 4028 THR A O     1 
ATOM   18223 C  CB    . THR A 1 4028 ? 206.260 190.088 201.814 1.00 34.20  ? 4028 THR A CB    1 
ATOM   18224 O  OG1   . THR A 1 4028 ? 206.350 191.310 201.073 1.00 37.23  ? 4028 THR A OG1   1 
ATOM   18225 C  CG2   . THR A 1 4028 ? 204.885 189.475 201.600 1.00 33.36  ? 4028 THR A CG2   1 
ATOM   18226 N  N     . HIS A 1 4029 ? 207.273 188.175 204.014 1.00 28.23  ? 4029 HIS A N     1 
ATOM   18227 C  CA    . HIS A 1 4029 ? 207.182 186.928 204.763 1.00 27.91  ? 4029 HIS A CA    1 
ATOM   18228 C  C     . HIS A 1 4029 ? 207.371 187.154 206.257 1.00 31.46  ? 4029 HIS A C     1 
ATOM   18229 O  O     . HIS A 1 4029 ? 206.795 186.423 207.071 1.00 31.37  ? 4029 HIS A O     1 
ATOM   18230 C  CB    . HIS A 1 4029 ? 208.212 185.925 204.242 1.00 31.42  ? 4029 HIS A CB    1 
ATOM   18231 C  CG    . HIS A 1 4029 ? 208.248 184.640 205.010 1.00 42.69  ? 4029 HIS A CG    1 
ATOM   18232 N  ND1   . HIS A 1 4029 ? 209.419 184.090 205.484 1.00 44.74  ? 4029 HIS A ND1   1 
ATOM   18233 C  CD2   . HIS A 1 4029 ? 207.257 183.799 205.388 1.00 37.48  ? 4029 HIS A CD2   1 
ATOM   18234 C  CE1   . HIS A 1 4029 ? 209.148 182.964 206.121 1.00 47.72  ? 4029 HIS A CE1   1 
ATOM   18235 N  NE2   . HIS A 1 4029 ? 207.843 182.765 206.078 1.00 40.49  ? 4029 HIS A NE2   1 
ATOM   18236 N  N     . ILE A 1 4030 ? 208.165 188.158 206.636 1.00 33.41  ? 4030 ILE A N     1 
ATOM   18237 C  CA    . ILE A 1 4030 ? 208.418 188.431 208.048 1.00 27.28  ? 4030 ILE A CA    1 
ATOM   18238 C  C     . ILE A 1 4030 ? 207.323 189.270 208.688 1.00 25.09  ? 4030 ILE A C     1 
ATOM   18239 O  O     . ILE A 1 4030 ? 207.282 189.385 209.917 1.00 30.50  ? 4030 ILE A O     1 
ATOM   18240 C  CB    . ILE A 1 4030 ? 209.797 189.103 208.196 1.00 23.80  ? 4030 ILE A CB    1 
ATOM   18241 C  CG1   . ILE A 1 4030 ? 210.838 188.335 207.385 1.00 24.27  ? 4030 ILE A CG1   1 
ATOM   18242 C  CG2   . ILE A 1 4030 ? 210.246 189.129 209.640 1.00 25.52  ? 4030 ILE A CG2   1 
ATOM   18243 C  CD1   . ILE A 1 4030 ? 212.175 189.020 207.315 1.00 24.36  ? 4030 ILE A CD1   1 
ATOM   18244 N  N     . VAL A 1 4031 ? 206.423 189.848 207.899 1.00 26.51  ? 4031 VAL A N     1 
ATOM   18245 C  CA    . VAL A 1 4031 ? 205.299 190.604 208.432 1.00 25.94  ? 4031 VAL A CA    1 
ATOM   18246 C  C     . VAL A 1 4031 ? 204.012 189.788 208.402 1.00 28.41  ? 4031 VAL A C     1 
ATOM   18247 O  O     . VAL A 1 4031 ? 203.250 189.797 209.369 1.00 29.73  ? 4031 VAL A O     1 
ATOM   18248 C  CB    . VAL A 1 4031 ? 205.140 191.937 207.668 1.00 26.76  ? 4031 VAL A CB    1 
ATOM   18249 C  CG1   . VAL A 1 4031 ? 203.735 192.494 207.833 1.00 23.22  ? 4031 VAL A CG1   1 
ATOM   18250 C  CG2   . VAL A 1 4031 ? 206.168 192.945 208.156 1.00 22.51  ? 4031 VAL A CG2   1 
ATOM   18251 N  N     . GLY A 1 4032 ? 203.758 189.072 207.304 1.00 26.96  ? 4032 GLY A N     1 
ATOM   18252 C  CA    . GLY A 1 4032 ? 202.596 188.198 207.263 1.00 28.14  ? 4032 GLY A CA    1 
ATOM   18253 C  C     . GLY A 1 4032 ? 202.670 187.091 208.296 1.00 31.62  ? 4032 GLY A C     1 
ATOM   18254 O  O     . GLY A 1 4032 ? 201.669 186.755 208.935 1.00 35.01  ? 4032 GLY A O     1 
ATOM   18255 N  N     . THR A 1 4033 ? 203.850 186.508 208.469 1.00 31.22  ? 4033 THR A N     1 
ATOM   18256 C  CA    . THR A 1 4033 ? 204.128 185.546 209.521 1.00 26.17  ? 4033 THR A CA    1 
ATOM   18257 C  C     . THR A 1 4033 ? 205.269 186.075 210.381 1.00 31.54  ? 4033 THR A C     1 
ATOM   18258 O  O     . THR A 1 4033 ? 205.784 187.171 210.157 1.00 38.18  ? 4033 THR A O     1 
ATOM   18259 C  CB    . THR A 1 4033 ? 204.488 184.172 208.941 1.00 28.94  ? 4033 THR A CB    1 
ATOM   18260 O  OG1   . THR A 1 4033 ? 205.454 184.331 207.896 1.00 27.28  ? 4033 THR A OG1   1 
ATOM   18261 C  CG2   . THR A 1 4033 ? 203.249 183.494 208.376 1.00 33.21  ? 4033 THR A CG2   1 
ATOM   18262 N  N     . GLU A 1 4034 ? 205.645 185.292 211.390 1.00 27.22  ? 4034 GLU A N     1 
ATOM   18263 C  CA    . GLU A 1 4034 ? 206.779 185.536 212.279 1.00 25.59  ? 4034 GLU A CA    1 
ATOM   18264 C  C     . GLU A 1 4034 ? 206.598 186.755 213.175 1.00 27.71  ? 4034 GLU A C     1 
ATOM   18265 O  O     . GLU A 1 4034 ? 207.475 187.026 214.004 1.00 28.63  ? 4034 GLU A O     1 
ATOM   18266 C  CB    . GLU A 1 4034 ? 208.097 185.701 211.507 1.00 27.96  ? 4034 GLU A CB    1 
ATOM   18267 C  CG    . GLU A 1 4034 ? 208.572 184.445 210.807 1.00 36.52  ? 4034 GLU A CG    1 
ATOM   18268 C  CD    . GLU A 1 4034 ? 209.864 184.659 210.045 1.00 43.04  ? 4034 GLU A CD    1 
ATOM   18269 O  OE1   . GLU A 1 4034 ? 210.320 185.818 209.961 1.00 34.00  ? 4034 GLU A OE1   1 
ATOM   18270 O  OE2   . GLU A 1 4034 ? 210.419 183.668 209.523 1.00 48.50  ? 4034 GLU A OE2   1 
ATOM   18271 N  N     . VAL A 1 4035 ? 205.500 187.498 213.046 1.00 24.51  ? 4035 VAL A N     1 
ATOM   18272 C  CA    . VAL A 1 4035 ? 205.210 188.645 213.899 1.00 24.68  ? 4035 VAL A CA    1 
ATOM   18273 C  C     . VAL A 1 4035 ? 203.762 188.548 214.350 1.00 26.99  ? 4035 VAL A C     1 
ATOM   18274 O  O     . VAL A 1 4035 ? 202.854 188.453 213.516 1.00 24.65  ? 4035 VAL A O     1 
ATOM   18275 C  CB    . VAL A 1 4035 ? 205.464 189.986 213.188 1.00 18.71  ? 4035 VAL A CB    1 
ATOM   18276 C  CG1   . VAL A 1 4035 ? 205.012 191.139 214.063 1.00 18.04  ? 4035 VAL A CG1   1 
ATOM   18277 C  CG2   . VAL A 1 4035 ? 206.936 190.145 212.874 1.00 21.18  ? 4035 VAL A CG2   1 
ATOM   18278 N  N     . LYS A 1 4036 ? 203.548 188.570 215.660 1.00 27.79  ? 4036 LYS A N     1 
ATOM   18279 C  CA    . LYS A 1 4036 ? 202.206 188.565 216.213 1.00 22.96  ? 4036 LYS A CA    1 
ATOM   18280 C  C     . LYS A 1 4036 ? 201.558 189.937 216.039 1.00 22.86  ? 4036 LYS A C     1 
ATOM   18281 O  O     . LYS A 1 4036 ? 202.254 190.948 215.914 1.00 26.71  ? 4036 LYS A O     1 
ATOM   18282 C  CB    . LYS A 1 4036 ? 202.244 188.191 217.691 1.00 30.52  ? 4036 LYS A CB    1 
ATOM   18283 C  CG    . LYS A 1 4036 ? 202.702 186.766 217.951 1.00 37.92  ? 4036 LYS A CG    1 
ATOM   18284 C  CD    . LYS A 1 4036 ? 202.706 186.447 219.435 1.00 45.04  ? 4036 LYS A CD    1 
ATOM   18285 C  CE    . LYS A 1 4036 ? 203.078 184.995 219.682 1.00 41.79  ? 4036 LYS A CE    1 
ATOM   18286 N  NZ    . LYS A 1 4036 ? 204.489 184.715 219.299 1.00 39.53  ? 4036 LYS A NZ    1 
ATOM   18287 N  N     . PRO A 1 4037 ? 200.224 189.997 216.009 1.00 23.58  ? 4037 PRO A N     1 
ATOM   18288 C  CA    . PRO A 1 4037 ? 199.558 191.302 215.864 1.00 24.78  ? 4037 PRO A CA    1 
ATOM   18289 C  C     . PRO A 1 4037 ? 199.878 192.277 216.984 1.00 22.03  ? 4037 PRO A C     1 
ATOM   18290 O  O     . PRO A 1 4037 ? 199.890 193.491 216.745 1.00 28.45  ? 4037 PRO A O     1 
ATOM   18291 C  CB    . PRO A 1 4037 ? 198.067 190.937 215.838 1.00 20.77  ? 4037 PRO A CB    1 
ATOM   18292 C  CG    . PRO A 1 4037 ? 197.987 189.558 216.405 1.00 24.01  ? 4037 PRO A CG    1 
ATOM   18293 C  CD    . PRO A 1 4037 ? 199.258 188.887 216.009 1.00 27.85  ? 4037 PRO A CD    1 
ATOM   18294 N  N     . ASN A 1 4038 ? 200.136 191.792 218.194 1.00 19.83  ? 4038 ASN A N     1 
ATOM   18295 C  CA    . ASN A 1 4038 ? 200.466 192.654 219.319 1.00 23.64  ? 4038 ASN A CA    1 
ATOM   18296 C  C     . ASN A 1 4038 ? 201.945 193.012 219.390 1.00 24.20  ? 4038 ASN A C     1 
ATOM   18297 O  O     . ASN A 1 4038 ? 202.338 193.791 220.265 1.00 21.65  ? 4038 ASN A O     1 
ATOM   18298 C  CB    . ASN A 1 4038 ? 200.020 192.001 220.636 1.00 23.74  ? 4038 ASN A CB    1 
ATOM   18299 C  CG    . ASN A 1 4038 ? 200.748 190.698 220.930 1.00 35.27  ? 4038 ASN A CG    1 
ATOM   18300 O  OD1   . ASN A 1 4038 ? 201.683 190.309 220.229 1.00 31.80  ? 4038 ASN A OD1   1 
ATOM   18301 N  ND2   . ASN A 1 4038 ? 200.320 190.018 221.985 1.00 52.81  ? 4038 ASN A ND2   1 
ATOM   18302 N  N     . THR A 1 4039 ? 202.770 192.469 218.497 1.00 22.43  ? 4039 THR A N     1 
ATOM   18303 C  CA    . THR A 1 4039 ? 204.197 192.742 218.509 1.00 18.55  ? 4039 THR A CA    1 
ATOM   18304 C  C     . THR A 1 4039 ? 204.501 193.848 217.511 1.00 17.51  ? 4039 THR A C     1 
ATOM   18305 O  O     . THR A 1 4039 ? 204.353 193.631 216.299 1.00 20.83  ? 4039 THR A O     1 
ATOM   18306 C  CB    . THR A 1 4039 ? 204.989 191.483 218.165 1.00 19.87  ? 4039 THR A CB    1 
ATOM   18307 O  OG1   . THR A 1 4039 ? 204.561 190.405 219.006 1.00 36.03  ? 4039 THR A OG1   1 
ATOM   18308 C  CG2   . THR A 1 4039 ? 206.474 191.714 218.367 1.00 13.47  ? 4039 THR A CG2   1 
ATOM   18309 N  N     . PRO A 1 4040 ? 204.912 195.032 217.956 1.00 13.54  ? 4040 PRO A N     1 
ATOM   18310 C  CA    . PRO A 1 4040 ? 205.212 196.108 217.006 1.00 12.46  ? 4040 PRO A CA    1 
ATOM   18311 C  C     . PRO A 1 4040 ? 206.430 195.790 216.154 1.00 11.91  ? 4040 PRO A C     1 
ATOM   18312 O  O     . PRO A 1 4040 ? 207.366 195.113 216.584 1.00 13.81  ? 4040 PRO A O     1 
ATOM   18313 C  CB    . PRO A 1 4040 ? 205.470 197.319 217.910 1.00 10.63  ? 4040 PRO A CB    1 
ATOM   18314 C  CG    . PRO A 1 4040 ? 205.852 196.734 219.224 1.00 13.55  ? 4040 PRO A CG    1 
ATOM   18315 C  CD    . PRO A 1 4040 ? 205.078 195.463 219.354 1.00 12.23  ? 4040 PRO A CD    1 
ATOM   18316 N  N     . VAL A 1 4041 ? 206.406 196.297 214.928 1.00 11.35  ? 4041 VAL A N     1 
ATOM   18317 C  CA    . VAL A 1 4041 ? 207.520 196.183 213.996 1.00 9.85   ? 4041 VAL A CA    1 
ATOM   18318 C  C     . VAL A 1 4041 ? 208.320 197.473 214.117 1.00 10.30  ? 4041 VAL A C     1 
ATOM   18319 O  O     . VAL A 1 4041 ? 207.945 198.505 213.554 1.00 10.15  ? 4041 VAL A O     1 
ATOM   18320 C  CB    . VAL A 1 4041 ? 207.039 195.945 212.562 1.00 10.01  ? 4041 VAL A CB    1 
ATOM   18321 C  CG1   . VAL A 1 4041 ? 208.219 195.688 211.643 1.00 11.44  ? 4041 VAL A CG1   1 
ATOM   18322 C  CG2   . VAL A 1 4041 ? 206.058 194.786 212.515 1.00 8.95   ? 4041 VAL A CG2   1 
ATOM   18323 N  N     . LEU A 1 4042 ? 209.416 197.424 214.870 1.00 11.54  ? 4042 LEU A N     1 
ATOM   18324 C  CA    . LEU A 1 4042 ? 210.285 198.579 215.027 1.00 9.44   ? 4042 LEU A CA    1 
ATOM   18325 C  C     . LEU A 1 4042 ? 211.240 198.627 213.845 1.00 9.90   ? 4042 LEU A C     1 
ATOM   18326 O  O     . LEU A 1 4042 ? 211.941 197.649 213.572 1.00 11.38  ? 4042 LEU A O     1 
ATOM   18327 C  CB    . LEU A 1 4042 ? 211.065 198.486 216.336 1.00 9.58   ? 4042 LEU A CB    1 
ATOM   18328 C  CG    . LEU A 1 4042 ? 210.271 198.162 217.601 1.00 7.46   ? 4042 LEU A CG    1 
ATOM   18329 C  CD1   . LEU A 1 4042 ? 211.168 198.265 218.812 1.00 12.38  ? 4042 LEU A CD1   1 
ATOM   18330 C  CD2   . LEU A 1 4042 ? 209.081 199.084 217.739 1.00 8.87   ? 4042 LEU A CD2   1 
ATOM   18331 N  N     . MET A 1 4043 ? 211.244 199.741 213.123 1.00 14.84  ? 4043 MET A N     1 
ATOM   18332 C  CA    . MET A 1 4043 ? 212.187 199.936 212.029 1.00 13.66  ? 4043 MET A CA    1 
ATOM   18333 C  C     . MET A 1 4043 ? 213.157 201.056 212.392 1.00 17.07  ? 4043 MET A C     1 
ATOM   18334 O  O     . MET A 1 4043 ? 212.895 202.246 212.210 1.00 15.08  ? 4043 MET A O     1 
ATOM   18335 C  CB    . MET A 1 4043 ? 211.444 200.210 210.729 1.00 9.95   ? 4043 MET A CB    1 
ATOM   18336 C  CG    . MET A 1 4043 ? 210.659 199.008 210.254 1.00 15.65  ? 4043 MET A CG    1 
ATOM   18337 S  SD    . MET A 1 4043 ? 209.767 199.296 208.732 1.00 43.47  ? 4043 MET A SD    1 
ATOM   18338 C  CE    . MET A 1 4043 ? 208.913 197.735 208.566 1.00 39.20  ? 4043 MET A CE    1 
ATOM   18339 N  N     . CYS A 1 4044 ? 214.289 200.638 212.953 1.00 17.46  ? 4044 CYS A N     1 
ATOM   18340 C  CA    . CYS A 1 4044 ? 215.319 201.583 213.358 1.00 13.28  ? 4044 CYS A CA    1 
ATOM   18341 C  C     . CYS A 1 4044 ? 216.270 201.830 212.198 1.00 12.36  ? 4044 CYS A C     1 
ATOM   18342 O  O     . CYS A 1 4044 ? 216.778 200.886 211.584 1.00 13.04  ? 4044 CYS A O     1 
ATOM   18343 C  CB    . CYS A 1 4044 ? 216.084 201.052 214.567 1.00 16.40  ? 4044 CYS A CB    1 
ATOM   18344 S  SG    . CYS A 1 4044 ? 215.041 200.421 215.901 1.00 37.28  ? 4044 CYS A SG    1 
ATOM   18345 N  N     . SER A 1 4045 ? 216.519 203.098 211.901 1.00 14.47  ? 4045 SER A N     1 
ATOM   18346 C  CA    . SER A 1 4045 ? 217.317 203.462 210.743 1.00 10.49  ? 4045 SER A CA    1 
ATOM   18347 C  C     . SER A 1 4045 ? 218.459 204.375 211.157 1.00 12.07  ? 4045 SER A C     1 
ATOM   18348 O  O     . SER A 1 4045 ? 218.321 205.208 212.057 1.00 15.99  ? 4045 SER A O     1 
ATOM   18349 C  CB    . SER A 1 4045 ? 216.462 204.149 209.677 1.00 13.22  ? 4045 SER A CB    1 
ATOM   18350 O  OG    . SER A 1 4045 ? 215.584 203.231 209.053 1.00 26.96  ? 4045 SER A OG    1 
ATOM   18351 N  N     . VAL A 1 4046 ? 219.594 204.201 210.488 1.00 13.93  ? 4046 VAL A N     1 
ATOM   18352 C  CA    . VAL A 1 4046 ? 220.736 205.100 210.623 1.00 15.67  ? 4046 VAL A CA    1 
ATOM   18353 C  C     . VAL A 1 4046 ? 220.338 206.418 209.970 1.00 20.36  ? 4046 VAL A C     1 
ATOM   18354 O  O     . VAL A 1 4046 ? 219.413 206.433 209.145 1.00 24.93  ? 4046 VAL A O     1 
ATOM   18355 C  CB    . VAL A 1 4046 ? 221.998 204.501 209.982 1.00 16.48  ? 4046 VAL A CB    1 
ATOM   18356 C  CG1   . VAL A 1 4046 ? 222.396 203.218 210.691 1.00 12.88  ? 4046 VAL A CG1   1 
ATOM   18357 C  CG2   . VAL A 1 4046 ? 221.772 204.248 208.503 1.00 15.10  ? 4046 VAL A CG2   1 
ATOM   18358 N  N     . PRO A 1 4047 ? 220.975 207.540 210.308 1.00 19.05  ? 4047 PRO A N     1 
ATOM   18359 C  CA    . PRO A 1 4047 ? 220.572 208.816 209.705 1.00 19.79  ? 4047 PRO A CA    1 
ATOM   18360 C  C     . PRO A 1 4047 ? 220.678 208.778 208.188 1.00 21.80  ? 4047 PRO A C     1 
ATOM   18361 O  O     . PRO A 1 4047 ? 221.631 208.239 207.623 1.00 22.34  ? 4047 PRO A O     1 
ATOM   18362 C  CB    . PRO A 1 4047 ? 221.551 209.825 210.317 1.00 16.59  ? 4047 PRO A CB    1 
ATOM   18363 C  CG    . PRO A 1 4047 ? 222.686 209.003 210.831 1.00 20.68  ? 4047 PRO A CG    1 
ATOM   18364 C  CD    . PRO A 1 4047 ? 222.069 207.720 211.276 1.00 17.44  ? 4047 PRO A CD    1 
ATOM   18365 N  N     . GLY A 1 4048 ? 219.678 209.362 207.531 1.00 22.48  ? 4048 GLY A N     1 
ATOM   18366 C  CA    . GLY A 1 4048 ? 219.600 209.372 206.089 1.00 21.10  ? 4048 GLY A CA    1 
ATOM   18367 C  C     . GLY A 1 4048 ? 218.827 208.229 205.470 1.00 19.74  ? 4048 GLY A C     1 
ATOM   18368 O  O     . GLY A 1 4048 ? 218.612 208.238 204.252 1.00 21.30  ? 4048 GLY A O     1 
ATOM   18369 N  N     . TYR A 1 4049 ? 218.405 207.247 206.259 1.00 19.32  ? 4049 TYR A N     1 
ATOM   18370 C  CA    . TYR A 1 4049 ? 217.589 206.149 205.765 1.00 20.78  ? 4049 TYR A CA    1 
ATOM   18371 C  C     . TYR A 1 4049 ? 216.222 206.208 206.427 1.00 24.32  ? 4049 TYR A C     1 
ATOM   18372 O  O     . TYR A 1 4049 ? 216.115 206.453 207.630 1.00 27.09  ? 4049 TYR A O     1 
ATOM   18373 C  CB    . TYR A 1 4049 ? 218.256 204.793 206.021 1.00 15.59  ? 4049 TYR A CB    1 
ATOM   18374 C  CG    . TYR A 1 4049 ? 219.228 204.412 204.933 1.00 19.98  ? 4049 TYR A CG    1 
ATOM   18375 C  CD1   . TYR A 1 4049 ? 220.435 205.084 204.790 1.00 19.74  ? 4049 TYR A CD1   1 
ATOM   18376 C  CD2   . TYR A 1 4049 ? 218.931 203.399 204.033 1.00 15.22  ? 4049 TYR A CD2   1 
ATOM   18377 C  CE1   . TYR A 1 4049 ? 221.321 204.752 203.788 1.00 16.28  ? 4049 TYR A CE1   1 
ATOM   18378 C  CE2   . TYR A 1 4049 ? 219.815 203.058 203.028 1.00 21.23  ? 4049 TYR A CE2   1 
ATOM   18379 C  CZ    . TYR A 1 4049 ? 221.007 203.739 202.911 1.00 21.79  ? 4049 TYR A CZ    1 
ATOM   18380 O  OH    . TYR A 1 4049 ? 221.891 203.407 201.911 1.00 22.63  ? 4049 TYR A OH    1 
ATOM   18381 N  N     . ASP A 1 4050 ? 215.180 206.006 205.627 1.00 21.48  ? 4050 ASP A N     1 
ATOM   18382 C  CA    . ASP A 1 4050 ? 213.808 206.064 206.104 1.00 28.54  ? 4050 ASP A CA    1 
ATOM   18383 C  C     . ASP A 1 4050 ? 213.080 204.807 205.662 1.00 30.55  ? 4050 ASP A C     1 
ATOM   18384 O  O     . ASP A 1 4050 ? 213.087 204.468 204.474 1.00 34.09  ? 4050 ASP A O     1 
ATOM   18385 C  CB    . ASP A 1 4050 ? 213.096 207.314 205.578 1.00 28.55  ? 4050 ASP A CB    1 
ATOM   18386 C  CG    . ASP A 1 4050 ? 211.637 207.362 205.971 1.00 32.28  ? 4050 ASP A CG    1 
ATOM   18387 O  OD1   . ASP A 1 4050 ? 211.345 207.283 207.182 1.00 29.64  ? 4050 ASP A OD1   1 
ATOM   18388 O  OD2   . ASP A 1 4050 ? 210.783 207.483 205.069 1.00 29.86  ? 4050 ASP A OD2   1 
ATOM   18389 N  N     . ALA A 1 4051 ? 212.457 204.119 206.614 1.00 27.33  ? 4051 ALA A N     1 
ATOM   18390 C  CA    . ALA A 1 4051 ? 211.747 202.880 206.342 1.00 25.92  ? 4051 ALA A CA    1 
ATOM   18391 C  C     . ALA A 1 4051 ? 210.257 203.085 206.102 1.00 25.30  ? 4051 ALA A C     1 
ATOM   18392 O  O     . ALA A 1 4051 ? 209.545 202.107 205.857 1.00 29.64  ? 4051 ALA A O     1 
ATOM   18393 C  CB    . ALA A 1 4051 ? 211.955 201.893 207.495 1.00 22.05  ? 4051 ALA A CB    1 
ATOM   18394 N  N     . SER A 1 4052 ? 209.771 204.326 206.165 1.00 21.65  ? 4052 SER A N     1 
ATOM   18395 C  CA    . SER A 1 4052 ? 208.351 204.580 205.939 1.00 23.04  ? 4052 SER A CA    1 
ATOM   18396 C  C     . SER A 1 4052 ? 207.945 204.213 204.517 1.00 26.24  ? 4052 SER A C     1 
ATOM   18397 O  O     . SER A 1 4052 ? 206.858 203.664 204.291 1.00 25.74  ? 4052 SER A O     1 
ATOM   18398 C  CB    . SER A 1 4052 ? 208.033 206.045 206.233 1.00 25.43  ? 4052 SER A CB    1 
ATOM   18399 O  OG    . SER A 1 4052 ? 208.508 206.425 207.513 1.00 24.97  ? 4052 SER A OG    1 
ATOM   18400 N  N     . GLY A 1 4053 ? 208.808 204.517 203.543 1.00 21.84  ? 4053 GLY A N     1 
ATOM   18401 C  CA    . GLY A 1 4053 ? 208.513 204.162 202.166 1.00 20.72  ? 4053 GLY A CA    1 
ATOM   18402 C  C     . GLY A 1 4053 ? 208.391 202.666 201.965 1.00 23.71  ? 4053 GLY A C     1 
ATOM   18403 O  O     . GLY A 1 4053 ? 207.561 202.202 201.183 1.00 28.26  ? 4053 GLY A O     1 
ATOM   18404 N  N     . HIS A 1 4054 ? 209.214 201.890 202.673 1.00 23.62  ? 4054 HIS A N     1 
ATOM   18405 C  CA    . HIS A 1 4054 ? 209.113 200.438 202.588 1.00 21.50  ? 4054 HIS A CA    1 
ATOM   18406 C  C     . HIS A 1 4054 ? 207.763 199.948 203.095 1.00 22.76  ? 4054 HIS A C     1 
ATOM   18407 O  O     . HIS A 1 4054 ? 207.140 199.076 202.479 1.00 25.82  ? 4054 HIS A O     1 
ATOM   18408 C  CB    . HIS A 1 4054 ? 210.251 199.791 203.376 1.00 24.22  ? 4054 HIS A CB    1 
ATOM   18409 C  CG    . HIS A 1 4054 ? 211.616 200.157 202.879 1.00 33.14  ? 4054 HIS A CG    1 
ATOM   18410 N  ND1   . HIS A 1 4054 ? 212.724 200.171 203.696 1.00 38.99  ? 4054 HIS A ND1   1 
ATOM   18411 C  CD2   . HIS A 1 4054 ? 212.051 200.516 201.648 1.00 31.67  ? 4054 HIS A CD2   1 
ATOM   18412 C  CE1   . HIS A 1 4054 ? 213.784 200.523 202.992 1.00 39.74  ? 4054 HIS A CE1   1 
ATOM   18413 N  NE2   . HIS A 1 4054 ? 213.404 200.739 201.746 1.00 48.71  ? 4054 HIS A NE2   1 
ATOM   18414 N  N     . VAL A 1 4055 ? 207.296 200.495 204.217 1.00 26.15  ? 4055 VAL A N     1 
ATOM   18415 C  CA    . VAL A 1 4055 ? 206.005 200.077 204.754 1.00 22.63  ? 4055 VAL A CA    1 
ATOM   18416 C  C     . VAL A 1 4055 ? 204.885 200.466 203.803 1.00 24.07  ? 4055 VAL A C     1 
ATOM   18417 O  O     . VAL A 1 4055 ? 203.956 199.685 203.566 1.00 26.74  ? 4055 VAL A O     1 
ATOM   18418 C  CB    . VAL A 1 4055 ? 205.788 200.682 206.151 1.00 20.14  ? 4055 VAL A CB    1 
ATOM   18419 C  CG1   . VAL A 1 4055 ? 204.549 200.098 206.806 1.00 14.90  ? 4055 VAL A CG1   1 
ATOM   18420 C  CG2   . VAL A 1 4055 ? 207.010 200.471 207.019 1.00 20.62  ? 4055 VAL A CG2   1 
ATOM   18421 N  N     . GLU A 1 4056 ? 204.943 201.682 203.256 1.00 25.31  ? 4056 GLU A N     1 
ATOM   18422 C  CA    . GLU A 1 4056 ? 203.919 202.106 202.307 1.00 26.56  ? 4056 GLU A CA    1 
ATOM   18423 C  C     . GLU A 1 4056 ? 203.902 201.208 201.077 1.00 28.32  ? 4056 GLU A C     1 
ATOM   18424 O  O     . GLU A 1 4056 ? 202.832 200.782 200.622 1.00 26.54  ? 4056 GLU A O     1 
ATOM   18425 C  CB    . GLU A 1 4056 ? 204.154 203.561 201.908 1.00 31.66  ? 4056 GLU A CB    1 
ATOM   18426 C  CG    . GLU A 1 4056 ? 203.816 204.559 203.008 1.00 33.46  ? 4056 GLU A CG    1 
ATOM   18427 C  CD    . GLU A 1 4056 ? 204.480 205.918 202.815 1.00 48.02  ? 4056 GLU A CD    1 
ATOM   18428 O  OE1   . GLU A 1 4056 ? 204.967 206.204 201.702 1.00 43.02  ? 4056 GLU A OE1   1 
ATOM   18429 O  OE2   . GLU A 1 4056 ? 204.507 206.710 203.781 1.00 52.17  ? 4056 GLU A OE2   1 
ATOM   18430 N  N     . ASP A 1 4057 ? 205.081 200.901 200.530 1.00 29.33  ? 4057 ASP A N     1 
ATOM   18431 C  CA    . ASP A 1 4057 ? 205.152 200.041 199.355 1.00 31.32  ? 4057 ASP A CA    1 
ATOM   18432 C  C     . ASP A 1 4057 ? 204.619 198.652 199.658 1.00 31.07  ? 4057 ASP A C     1 
ATOM   18433 O  O     . ASP A 1 4057 ? 203.865 198.087 198.859 1.00 39.04  ? 4057 ASP A O     1 
ATOM   18434 C  CB    . ASP A 1 4057 ? 206.590 199.961 198.839 1.00 31.03  ? 4057 ASP A CB    1 
ATOM   18435 C  CG    . ASP A 1 4057 ? 207.070 201.266 198.237 1.00 46.70  ? 4057 ASP A CG    1 
ATOM   18436 O  OD1   . ASP A 1 4057 ? 206.232 202.027 197.710 1.00 45.24  ? 4057 ASP A OD1   1 
ATOM   18437 O  OD2   . ASP A 1 4057 ? 208.291 201.526 198.289 1.00 39.89  ? 4057 ASP A OD2   1 
ATOM   18438 N  N     . LEU A 1 4058 ? 204.992 198.087 200.808 1.00 25.29  ? 4058 LEU A N     1 
ATOM   18439 C  CA    . LEU A 1 4058 ? 204.548 196.739 201.140 1.00 25.29  ? 4058 LEU A CA    1 
ATOM   18440 C  C     . LEU A 1 4058 ? 203.043 196.696 201.366 1.00 27.77  ? 4058 LEU A C     1 
ATOM   18441 O  O     . LEU A 1 4058 ? 202.376 195.737 200.960 1.00 38.57  ? 4058 LEU A O     1 
ATOM   18442 C  CB    . LEU A 1 4058 ? 205.305 196.227 202.366 1.00 22.32  ? 4058 LEU A CB    1 
ATOM   18443 C  CG    . LEU A 1 4058 ? 205.125 194.757 202.757 1.00 25.80  ? 4058 LEU A CG    1 
ATOM   18444 C  CD1   . LEU A 1 4058 ? 206.361 194.266 203.464 1.00 27.97  ? 4058 LEU A CD1   1 
ATOM   18445 C  CD2   . LEU A 1 4058 ? 203.923 194.537 203.649 1.00 28.97  ? 4058 LEU A CD2   1 
ATOM   18446 N  N     . ALA A 1 4059 ? 202.490 197.719 202.022 1.00 24.96  ? 4059 ALA A N     1 
ATOM   18447 C  CA    . ALA A 1 4059 ? 201.044 197.790 202.193 1.00 24.29  ? 4059 ALA A CA    1 
ATOM   18448 C  C     . ALA A 1 4059 ? 200.340 197.907 200.848 1.00 33.33  ? 4059 ALA A C     1 
ATOM   18449 O  O     . ALA A 1 4059 ? 199.257 197.341 200.656 1.00 32.44  ? 4059 ALA A O     1 
ATOM   18450 C  CB    . ALA A 1 4059 ? 200.678 198.963 203.100 1.00 21.29  ? 4059 ALA A CB    1 
ATOM   18451 N  N     . ALA A 1 4060 ? 200.935 198.645 199.909 1.00 33.31  ? 4060 ALA A N     1 
ATOM   18452 C  CA    . ALA A 1 4060 ? 200.375 198.712 198.564 1.00 29.49  ? 4060 ALA A CA    1 
ATOM   18453 C  C     . ALA A 1 4060 ? 200.419 197.357 197.866 1.00 35.35  ? 4060 ALA A C     1 
ATOM   18454 O  O     . ALA A 1 4060 ? 199.477 197.004 197.147 1.00 45.86  ? 4060 ALA A O     1 
ATOM   18455 C  CB    . ALA A 1 4060 ? 201.119 199.758 197.737 1.00 30.55  ? 4060 ALA A CB    1 
ATOM   18456 N  N     . GLU A 1 4061 ? 201.501 196.597 198.053 1.00 33.24  ? 4061 GLU A N     1 
ATOM   18457 C  CA    . GLU A 1 4061 ? 201.618 195.293 197.401 1.00 37.02  ? 4061 GLU A CA    1 
ATOM   18458 C  C     . GLU A 1 4061 ? 200.560 194.317 197.897 1.00 34.48  ? 4061 GLU A C     1 
ATOM   18459 O  O     . GLU A 1 4061 ? 199.980 193.566 197.104 1.00 39.33  ? 4061 GLU A O     1 
ATOM   18460 C  CB    . GLU A 1 4061 ? 203.017 194.715 197.621 1.00 43.79  ? 4061 GLU A CB    1 
ATOM   18461 C  CG    . GLU A 1 4061 ? 204.164 195.571 197.095 1.00 51.11  ? 4061 GLU A CG    1 
ATOM   18462 C  CD    . GLU A 1 4061 ? 204.348 195.479 195.588 1.00 59.72  ? 4061 GLU A CD    1 
ATOM   18463 O  OE1   . GLU A 1 4061 ? 203.387 195.121 194.876 1.00 56.41  ? 4061 GLU A OE1   1 
ATOM   18464 O  OE2   . GLU A 1 4061 ? 205.467 195.765 195.113 1.00 67.42  ? 4061 GLU A OE2   1 
ATOM   18465 N  N     . GLN A 1 4062 ? 200.297 194.308 199.201 1.00 37.73  ? 4062 GLN A N     1 
ATOM   18466 C  CA    . GLN A 1 4062 ? 199.358 193.369 199.799 1.00 35.12  ? 4062 GLN A CA    1 
ATOM   18467 C  C     . GLN A 1 4062 ? 197.912 193.830 199.704 1.00 39.17  ? 4062 GLN A C     1 
ATOM   18468 O  O     . GLN A 1 4062 ? 197.019 193.106 200.158 1.00 41.01  ? 4062 GLN A O     1 
ATOM   18469 C  CB    . GLN A 1 4062 ? 199.715 193.128 201.270 1.00 32.08  ? 4062 GLN A CB    1 
ATOM   18470 C  CG    . GLN A 1 4062 ? 201.001 192.354 201.486 1.00 31.99  ? 4062 GLN A CG    1 
ATOM   18471 C  CD    . GLN A 1 4062 ? 201.094 191.770 202.881 1.00 48.88  ? 4062 GLN A CD    1 
ATOM   18472 O  OE1   . GLN A 1 4062 ? 202.162 191.752 203.491 1.00 51.84  ? 4062 GLN A OE1   1 
ATOM   18473 N  NE2   . GLN A 1 4062 ? 199.968 191.288 203.395 1.00 42.52  ? 4062 GLN A NE2   1 
ATOM   18474 N  N     . ASN A 1 4063 ? 197.663 195.007 199.127 1.00 37.77  ? 4063 ASN A N     1 
ATOM   18475 C  CA    . ASN A 1 4063 ? 196.330 195.606 199.079 1.00 38.90  ? 4063 ASN A CA    1 
ATOM   18476 C  C     . ASN A 1 4063 ? 195.766 195.699 200.500 1.00 37.66  ? 4063 ASN A C     1 
ATOM   18477 O  O     . ASN A 1 4063 ? 194.716 195.144 200.831 1.00 35.99  ? 4063 ASN A O     1 
ATOM   18478 C  CB    . ASN A 1 4063 ? 195.410 194.825 198.127 1.00 43.53  ? 4063 ASN A CB    1 
ATOM   18479 C  CG    . ASN A 1 4063 ? 193.947 195.237 198.225 1.00 50.81  ? 4063 ASN A CG    1 
ATOM   18480 O  OD1   . ASN A 1 4063 ? 193.630 196.386 198.537 1.00 51.04  ? 4063 ASN A OD1   1 
ATOM   18481 N  ND2   . ASN A 1 4063 ? 193.049 194.295 197.960 1.00 49.63  ? 4063 ASN A ND2   1 
ATOM   18482 N  N     . THR A 1 4064 ? 196.525 196.361 201.368 1.00 32.52  ? 4064 THR A N     1 
ATOM   18483 C  CA    . THR A 1 4064 ? 196.142 196.581 202.754 1.00 33.56  ? 4064 THR A CA    1 
ATOM   18484 C  C     . THR A 1 4064 ? 196.112 198.077 203.023 1.00 33.34  ? 4064 THR A C     1 
ATOM   18485 O  O     . THR A 1 4064 ? 197.085 198.781 202.739 1.00 35.46  ? 4064 THR A O     1 
ATOM   18486 C  CB    . THR A 1 4064 ? 197.113 195.890 203.716 1.00 29.36  ? 4064 THR A CB    1 
ATOM   18487 O  OG1   . THR A 1 4064 ? 197.274 194.518 203.335 1.00 33.22  ? 4064 THR A OG1   1 
ATOM   18488 C  CG2   . THR A 1 4064 ? 196.585 195.952 205.139 1.00 25.93  ? 4064 THR A CG2   1 
ATOM   18489 N  N     . GLN A 1 4065 ? 194.997 198.560 203.562 1.00 30.55  ? 4065 GLN A N     1 
ATOM   18490 C  CA    . GLN A 1 4065 ? 194.893 199.972 203.896 1.00 37.42  ? 4065 GLN A CA    1 
ATOM   18491 C  C     . GLN A 1 4065 ? 195.683 200.265 205.164 1.00 35.30  ? 4065 GLN A C     1 
ATOM   18492 O  O     . GLN A 1 4065 ? 195.536 199.575 206.176 1.00 34.65  ? 4065 GLN A O     1 
ATOM   18493 C  CB    . GLN A 1 4065 ? 193.430 200.373 204.069 1.00 31.67  ? 4065 GLN A CB    1 
ATOM   18494 C  CG    . GLN A 1 4065 ? 192.745 200.783 202.773 1.00 37.92  ? 4065 GLN A CG    1 
ATOM   18495 C  CD    . GLN A 1 4065 ? 193.655 201.569 201.843 1.00 46.39  ? 4065 GLN A CD    1 
ATOM   18496 O  OE1   . GLN A 1 4065 ? 194.273 202.557 202.243 1.00 44.76  ? 4065 GLN A OE1   1 
ATOM   18497 N  NE2   . GLN A 1 4065 ? 193.743 201.128 200.593 1.00 38.31  ? 4065 GLN A NE2   1 
ATOM   18498 N  N     . ILE A 1 4066 ? 196.527 201.293 205.107 1.00 26.89  ? 4066 ILE A N     1 
ATOM   18499 C  CA    . ILE A 1 4066 ? 197.401 201.652 206.214 1.00 23.32  ? 4066 ILE A CA    1 
ATOM   18500 C  C     . ILE A 1 4066 ? 197.224 203.130 206.529 1.00 27.28  ? 4066 ILE A C     1 
ATOM   18501 O  O     . ILE A 1 4066 ? 197.134 203.967 205.624 1.00 29.53  ? 4066 ILE A O     1 
ATOM   18502 C  CB    . ILE A 1 4066 ? 198.879 201.326 205.904 1.00 22.31  ? 4066 ILE A CB    1 
ATOM   18503 C  CG1   . ILE A 1 4066 ? 199.763 201.665 207.104 1.00 20.76  ? 4066 ILE A CG1   1 
ATOM   18504 C  CG2   . ILE A 1 4066 ? 199.350 202.046 204.647 1.00 21.24  ? 4066 ILE A CG2   1 
ATOM   18505 C  CD1   . ILE A 1 4066 ? 201.220 201.395 206.875 1.00 18.12  ? 4066 ILE A CD1   1 
ATOM   18506 N  N     . THR A 1 4067 ? 197.149 203.443 207.819 1.00 24.93  ? 4067 THR A N     1 
ATOM   18507 C  CA    . THR A 1 4067 ? 197.091 204.817 208.296 1.00 20.59  ? 4067 THR A CA    1 
ATOM   18508 C  C     . THR A 1 4067 ? 198.474 205.217 208.794 1.00 20.32  ? 4067 THR A C     1 
ATOM   18509 O  O     . THR A 1 4067 ? 199.002 204.601 209.725 1.00 22.15  ? 4067 THR A O     1 
ATOM   18510 C  CB    . THR A 1 4067 ? 196.057 204.972 209.410 1.00 25.89  ? 4067 THR A CB    1 
ATOM   18511 O  OG1   . THR A 1 4067 ? 194.741 204.806 208.871 1.00 35.69  ? 4067 THR A OG1   1 
ATOM   18512 C  CG2   . THR A 1 4067 ? 196.167 206.346 210.049 1.00 20.13  ? 4067 THR A CG2   1 
ATOM   18513 N  N     . SER A 1 4068 ? 199.056 206.237 208.174 1.00 22.74  ? 4068 SER A N     1 
ATOM   18514 C  CA    . SER A 1 4068 ? 200.379 206.727 208.534 1.00 16.19  ? 4068 SER A CA    1 
ATOM   18515 C  C     . SER A 1 4068 ? 200.244 208.039 209.293 1.00 14.31  ? 4068 SER A C     1 
ATOM   18516 O  O     . SER A 1 4068 ? 199.554 208.957 208.837 1.00 19.21  ? 4068 SER A O     1 
ATOM   18517 C  CB    . SER A 1 4068 ? 201.248 206.919 207.292 1.00 20.53  ? 4068 SER A CB    1 
ATOM   18518 O  OG    . SER A 1 4068 ? 201.256 205.750 206.492 1.00 26.14  ? 4068 SER A OG    1 
ATOM   18519 N  N     . ILE A 1 4069 ? 200.896 208.121 210.449 1.00 14.64  ? 4069 ILE A N     1 
ATOM   18520 C  CA    . ILE A 1 4069 ? 200.829 209.292 211.313 1.00 13.50  ? 4069 ILE A CA    1 
ATOM   18521 C  C     . ILE A 1 4069 ? 202.242 209.665 211.734 1.00 16.04  ? 4069 ILE A C     1 
ATOM   18522 O  O     . ILE A 1 4069 ? 203.026 208.797 212.133 1.00 14.56  ? 4069 ILE A O     1 
ATOM   18523 C  CB    . ILE A 1 4069 ? 199.941 209.040 212.546 1.00 16.03  ? 4069 ILE A CB    1 
ATOM   18524 C  CG1   . ILE A 1 4069 ? 198.492 208.809 212.116 1.00 17.30  ? 4069 ILE A CG1   1 
ATOM   18525 C  CG2   . ILE A 1 4069 ? 200.031 210.202 213.521 1.00 15.56  ? 4069 ILE A CG2   1 
ATOM   18526 C  CD1   . ILE A 1 4069 ? 197.711 207.937 213.057 1.00 18.23  ? 4069 ILE A CD1   1 
ATOM   18527 N  N     . ALA A 1 4070 ? 202.566 210.951 211.644 1.00 14.75  ? 4070 ALA A N     1 
ATOM   18528 C  CA    . ALA A 1 4070 ? 203.869 211.455 212.052 1.00 10.94  ? 4070 ALA A CA    1 
ATOM   18529 C  C     . ALA A 1 4070 ? 203.787 211.956 213.488 1.00 15.41  ? 4070 ALA A C     1 
ATOM   18530 O  O     . ALA A 1 4070 ? 202.913 212.764 213.822 1.00 22.37  ? 4070 ALA A O     1 
ATOM   18531 C  CB    . ALA A 1 4070 ? 204.333 212.566 211.114 1.00 11.82  ? 4070 ALA A CB    1 
ATOM   18532 N  N     . ILE A 1 4071 ? 204.693 211.481 214.328 1.00 13.60  ? 4071 ILE A N     1 
ATOM   18533 C  CA    . ILE A 1 4071 ? 204.687 211.808 215.748 1.00 14.69  ? 4071 ILE A CA    1 
ATOM   18534 C  C     . ILE A 1 4071 ? 205.322 213.176 215.959 1.00 21.38  ? 4071 ILE A C     1 
ATOM   18535 O  O     . ILE A 1 4071 ? 206.199 213.602 215.199 1.00 18.62  ? 4071 ILE A O     1 
ATOM   18536 C  CB    . ILE A 1 4071 ? 205.416 210.699 216.538 1.00 10.41  ? 4071 ILE A CB    1 
ATOM   18537 C  CG1   . ILE A 1 4071 ? 204.669 209.373 216.391 1.00 13.52  ? 4071 ILE A CG1   1 
ATOM   18538 C  CG2   . ILE A 1 4071 ? 205.557 211.052 218.007 1.00 11.09  ? 4071 ILE A CG2   1 
ATOM   18539 C  CD1   . ILE A 1 4071 ? 203.232 209.430 216.847 1.00 12.56  ? 4071 ILE A CD1   1 
ATOM   18540 N  N     . GLY A 1 4072 ? 204.875 213.879 216.999 1.00 21.63  ? 4072 GLY A N     1 
ATOM   18541 C  CA    . GLY A 1 4072 ? 205.469 215.153 217.348 1.00 15.22  ? 4072 GLY A CA    1 
ATOM   18542 C  C     . GLY A 1 4072 ? 204.510 216.198 217.879 1.00 18.13  ? 4072 GLY A C     1 
ATOM   18543 O  O     . GLY A 1 4072 ? 204.922 217.097 218.618 1.00 24.43  ? 4072 GLY A O     1 
ATOM   18544 N  N     . SER A 1 4073 ? 203.234 216.095 217.525 1.00 26.27  ? 4073 SER A N     1 
ATOM   18545 C  CA    . SER A 1 4073 ? 202.225 217.041 217.972 1.00 24.47  ? 4073 SER A CA    1 
ATOM   18546 C  C     . SER A 1 4073 ? 201.173 216.324 218.808 1.00 29.65  ? 4073 SER A C     1 
ATOM   18547 O  O     . SER A 1 4073 ? 201.023 215.101 218.742 1.00 30.13  ? 4073 SER A O     1 
ATOM   18548 C  CB    . SER A 1 4073 ? 201.558 217.749 216.785 1.00 14.95  ? 4073 SER A CB    1 
ATOM   18549 O  OG    . SER A 1 4073 ? 200.946 216.818 215.911 1.00 20.66  ? 4073 SER A OG    1 
ATOM   18550 N  N     . ALA A 1 4074 ? 200.450 217.107 219.615 1.00 26.70  ? 4074 ALA A N     1 
ATOM   18551 C  CA    . ALA A 1 4074 ? 199.370 216.543 220.421 1.00 31.05  ? 4074 ALA A CA    1 
ATOM   18552 C  C     . ALA A 1 4074 ? 198.279 215.953 219.539 1.00 26.68  ? 4074 ALA A C     1 
ATOM   18553 O  O     . ALA A 1 4074 ? 197.757 214.864 219.820 1.00 29.94  ? 4074 ALA A O     1 
ATOM   18554 C  CB    . ALA A 1 4074 ? 198.795 217.612 221.349 1.00 26.90  ? 4074 ALA A CB    1 
ATOM   18555 N  N     . GLU A 1 4075 ? 197.917 216.663 218.468 1.00 25.49  ? 4075 GLU A N     1 
ATOM   18556 C  CA    . GLU A 1 4075 ? 196.997 216.101 217.487 1.00 28.64  ? 4075 GLU A CA    1 
ATOM   18557 C  C     . GLU A 1 4075 ? 197.548 214.814 216.897 1.00 29.16  ? 4075 GLU A C     1 
ATOM   18558 O  O     . GLU A 1 4075 ? 196.780 213.896 216.588 1.00 27.27  ? 4075 GLU A O     1 
ATOM   18559 C  CB    . GLU A 1 4075 ? 196.717 217.121 216.381 1.00 28.03  ? 4075 GLU A CB    1 
ATOM   18560 C  CG    . GLU A 1 4075 ? 196.382 218.519 216.884 1.00 37.32  ? 4075 GLU A CG    1 
ATOM   18561 C  CD    . GLU A 1 4075 ? 197.590 219.434 216.937 1.00 42.54  ? 4075 GLU A CD    1 
ATOM   18562 O  OE1   . GLU A 1 4075 ? 198.673 218.968 217.344 1.00 44.59  ? 4075 GLU A OE1   1 
ATOM   18563 O  OE2   . GLU A 1 4075 ? 197.457 220.620 216.573 1.00 34.67  ? 4075 GLU A OE2   1 
ATOM   18564 N  N     . GLY A 1 4076 ? 198.870 214.722 216.747 1.00 30.96  ? 4076 GLY A N     1 
ATOM   18565 C  CA    . GLY A 1 4076 ? 199.468 213.481 216.286 1.00 24.11  ? 4076 GLY A CA    1 
ATOM   18566 C  C     . GLY A 1 4076 ? 199.241 212.330 217.247 1.00 20.88  ? 4076 GLY A C     1 
ATOM   18567 O  O     . GLY A 1 4076 ? 198.918 211.218 216.829 1.00 28.16  ? 4076 GLY A O     1 
ATOM   18568 N  N     . PHE A 1 4077 ? 199.403 212.582 218.549 1.00 23.20  ? 4077 PHE A N     1 
ATOM   18569 C  CA    . PHE A 1 4077 ? 199.151 211.540 219.540 1.00 17.52  ? 4077 PHE A CA    1 
ATOM   18570 C  C     . PHE A 1 4077 ? 197.685 211.126 219.549 1.00 21.25  ? 4077 PHE A C     1 
ATOM   18571 O  O     . PHE A 1 4077 ? 197.371 209.933 219.647 1.00 25.36  ? 4077 PHE A O     1 
ATOM   18572 C  CB    . PHE A 1 4077 ? 199.577 212.015 220.928 1.00 14.28  ? 4077 PHE A CB    1 
ATOM   18573 C  CG    . PHE A 1 4077 ? 201.046 212.292 221.051 1.00 19.44  ? 4077 PHE A CG    1 
ATOM   18574 C  CD1   . PHE A 1 4077 ? 201.977 211.357 220.635 1.00 19.05  ? 4077 PHE A CD1   1 
ATOM   18575 C  CD2   . PHE A 1 4077 ? 201.495 213.487 221.580 1.00 20.62  ? 4077 PHE A CD2   1 
ATOM   18576 C  CE1   . PHE A 1 4077 ? 203.328 211.609 220.749 1.00 16.56  ? 4077 PHE A CE1   1 
ATOM   18577 C  CE2   . PHE A 1 4077 ? 202.844 213.745 221.694 1.00 20.23  ? 4077 PHE A CE2   1 
ATOM   18578 C  CZ    . PHE A 1 4077 ? 203.761 212.804 221.278 1.00 17.21  ? 4077 PHE A CZ    1 
ATOM   18579 N  N     . ASN A 1 4078 ? 196.773 212.098 219.461 1.00 19.32  ? 4078 ASN A N     1 
ATOM   18580 C  CA    . ASN A 1 4078 ? 195.352 211.765 219.424 1.00 18.31  ? 4078 ASN A CA    1 
ATOM   18581 C  C     . ASN A 1 4078 ? 195.013 210.936 218.191 1.00 21.13  ? 4078 ASN A C     1 
ATOM   18582 O  O     . ASN A 1 4078 ? 194.273 209.946 218.279 1.00 23.29  ? 4078 ASN A O     1 
ATOM   18583 C  CB    . ASN A 1 4078 ? 194.516 213.044 219.464 1.00 23.01  ? 4078 ASN A CB    1 
ATOM   18584 C  CG    . ASN A 1 4078 ? 194.399 213.618 220.862 1.00 27.68  ? 4078 ASN A CG    1 
ATOM   18585 O  OD1   . ASN A 1 4078 ? 195.318 214.267 221.358 1.00 27.34  ? 4078 ASN A OD1   1 
ATOM   18586 N  ND2   . ASN A 1 4078 ? 193.262 213.377 221.506 1.00 34.87  ? 4078 ASN A ND2   1 
ATOM   18587 N  N     . GLN A 1 4079 ? 195.557 211.320 217.032 1.00 23.72  ? 4079 GLN A N     1 
ATOM   18588 C  CA    . GLN A 1 4079 ? 195.330 210.558 215.812 1.00 20.62  ? 4079 GLN A CA    1 
ATOM   18589 C  C     . GLN A 1 4079 ? 195.903 209.154 215.924 1.00 19.34  ? 4079 GLN A C     1 
ATOM   18590 O  O     . GLN A 1 4079 ? 195.286 208.190 215.464 1.00 25.92  ? 4079 GLN A O     1 
ATOM   18591 C  CB    . GLN A 1 4079 ? 195.941 211.288 214.617 1.00 22.14  ? 4079 GLN A CB    1 
ATOM   18592 C  CG    . GLN A 1 4079 ? 195.251 211.000 213.297 1.00 27.59  ? 4079 GLN A CG    1 
ATOM   18593 C  CD    . GLN A 1 4079 ? 196.038 211.508 212.107 1.00 37.93  ? 4079 GLN A CD    1 
ATOM   18594 O  OE1   . GLN A 1 4079 ? 196.725 212.526 212.191 1.00 33.07  ? 4079 GLN A OE1   1 
ATOM   18595 N  NE2   . GLN A 1 4079 ? 195.943 210.798 210.990 1.00 36.15  ? 4079 GLN A NE2   1 
ATOM   18596 N  N     . ALA A 1 4080 ? 197.090 209.021 216.519 1.00 17.76  ? 4080 ALA A N     1 
ATOM   18597 C  CA    . ALA A 1 4080 ? 197.693 207.704 216.685 1.00 19.29  ? 4080 ALA A CA    1 
ATOM   18598 C  C     . ALA A 1 4080 ? 196.837 206.815 217.574 1.00 21.32  ? 4080 ALA A C     1 
ATOM   18599 O  O     . ALA A 1 4080 ? 196.607 205.642 217.255 1.00 26.75  ? 4080 ALA A O     1 
ATOM   18600 C  CB    . ALA A 1 4080 ? 199.103 207.841 217.258 1.00 14.92  ? 4080 ALA A CB    1 
ATOM   18601 N  N     . ASP A 1 4081 ? 196.350 207.357 218.692 1.00 21.96  ? 4081 ASP A N     1 
ATOM   18602 C  CA    . ASP A 1 4081 ? 195.498 206.574 219.582 1.00 21.60  ? 4081 ASP A CA    1 
ATOM   18603 C  C     . ASP A 1 4081 ? 194.221 206.143 218.874 1.00 19.95  ? 4081 ASP A C     1 
ATOM   18604 O  O     . ASP A 1 4081 ? 193.817 204.976 218.951 1.00 22.73  ? 4081 ASP A O     1 
ATOM   18605 C  CB    . ASP A 1 4081 ? 195.171 207.379 220.839 1.00 26.02  ? 4081 ASP A CB    1 
ATOM   18606 C  CG    . ASP A 1 4081 ? 196.378 207.585 221.729 1.00 38.52  ? 4081 ASP A CG    1 
ATOM   18607 O  OD1   . ASP A 1 4081 ? 197.280 206.721 221.719 1.00 38.36  ? 4081 ASP A OD1   1 
ATOM   18608 O  OD2   . ASP A 1 4081 ? 196.425 208.610 222.441 1.00 39.28  ? 4081 ASP A OD2   1 
ATOM   18609 N  N     . LYS A 1 4082 ? 193.578 207.074 218.162 1.00 23.70  ? 4082 LYS A N     1 
ATOM   18610 C  CA    . LYS A 1 4082 ? 192.342 206.743 217.462 1.00 24.00  ? 4082 LYS A CA    1 
ATOM   18611 C  C     . LYS A 1 4082 ? 192.580 205.693 216.383 1.00 21.45  ? 4082 LYS A C     1 
ATOM   18612 O  O     . LYS A 1 4082 ? 191.797 204.743 216.244 1.00 24.16  ? 4082 LYS A O     1 
ATOM   18613 C  CB    . LYS A 1 4082 ? 191.737 208.012 216.859 1.00 21.07  ? 4082 LYS A CB    1 
ATOM   18614 C  CG    . LYS A 1 4082 ? 190.378 207.820 216.214 1.00 33.65  ? 4082 LYS A CG    1 
ATOM   18615 C  CD    . LYS A 1 4082 ? 189.891 209.116 215.586 1.00 37.17  ? 4082 LYS A CD    1 
ATOM   18616 C  CE    . LYS A 1 4082 ? 189.447 210.110 216.646 1.00 44.30  ? 4082 LYS A CE    1 
ATOM   18617 N  NZ    . LYS A 1 4082 ? 188.858 211.339 216.043 1.00 39.01  ? 4082 LYS A NZ    1 
ATOM   18618 N  N     . ALA A 1 4083 ? 193.664 205.838 215.618 1.00 21.23  ? 4083 ALA A N     1 
ATOM   18619 C  CA    . ALA A 1 4083 ? 193.959 204.893 214.548 1.00 23.84  ? 4083 ALA A CA    1 
ATOM   18620 C  C     . ALA A 1 4083 ? 194.261 203.507 215.098 1.00 22.84  ? 4083 ALA A C     1 
ATOM   18621 O  O     . ALA A 1 4083 ? 193.797 202.503 214.548 1.00 21.92  ? 4083 ALA A O     1 
ATOM   18622 C  CB    . ALA A 1 4083 ? 195.130 205.402 213.709 1.00 19.59  ? 4083 ALA A CB    1 
ATOM   18623 N  N     . ILE A 1 4084 ? 195.038 203.429 216.181 1.00 21.33  ? 4084 ILE A N     1 
ATOM   18624 C  CA    . ILE A 1 4084 ? 195.341 202.131 216.777 1.00 19.74  ? 4084 ILE A CA    1 
ATOM   18625 C  C     . ILE A 1 4084 ? 194.072 201.485 217.315 1.00 22.02  ? 4084 ILE A C     1 
ATOM   18626 O  O     . ILE A 1 4084 ? 193.842 200.283 217.125 1.00 21.78  ? 4084 ILE A O     1 
ATOM   18627 C  CB    . ILE A 1 4084 ? 196.415 202.280 217.870 1.00 19.18  ? 4084 ILE A CB    1 
ATOM   18628 C  CG1   . ILE A 1 4084 ? 197.764 202.638 217.245 1.00 17.51  ? 4084 ILE A CG1   1 
ATOM   18629 C  CG2   . ILE A 1 4084 ? 196.533 201.001 218.684 1.00 17.53  ? 4084 ILE A CG2   1 
ATOM   18630 C  CD1   . ILE A 1 4084 ? 198.823 203.006 218.255 1.00 13.20  ? 4084 ILE A CD1   1 
ATOM   18631 N  N     . ASN A 1 4085 ? 193.225 202.269 217.988 1.00 24.52  ? 4085 ASN A N     1 
ATOM   18632 C  CA    . ASN A 1 4085 ? 191.990 201.721 218.535 1.00 18.46  ? 4085 ASN A CA    1 
ATOM   18633 C  C     . ASN A 1 4085 ? 191.075 201.209 217.431 1.00 19.05  ? 4085 ASN A C     1 
ATOM   18634 O  O     . ASN A 1 4085 ? 190.409 200.179 217.594 1.00 22.27  ? 4085 ASN A O     1 
ATOM   18635 C  CB    . ASN A 1 4085 ? 191.277 202.778 219.378 1.00 20.00  ? 4085 ASN A CB    1 
ATOM   18636 C  CG    . ASN A 1 4085 ? 191.970 203.026 220.701 1.00 25.91  ? 4085 ASN A CG    1 
ATOM   18637 O  OD1   . ASN A 1 4085 ? 192.920 202.331 221.055 1.00 24.27  ? 4085 ASN A OD1   1 
ATOM   18638 N  ND2   . ASN A 1 4085 ? 191.498 204.023 221.439 1.00 26.62  ? 4085 ASN A ND2   1 
ATOM   18639 N  N     . THR A 1 4086 ? 191.021 201.916 216.302 1.00 21.76  ? 4086 THR A N     1 
ATOM   18640 C  CA    . THR A 1 4086 ? 190.201 201.448 215.188 1.00 22.21  ? 4086 THR A CA    1 
ATOM   18641 C  C     . THR A 1 4086 ? 190.797 200.201 214.543 1.00 25.75  ? 4086 THR A C     1 
ATOM   18642 O  O     . THR A 1 4086 ? 190.065 199.263 214.202 1.00 27.21  ? 4086 THR A O     1 
ATOM   18643 C  CB    . THR A 1 4086 ? 190.040 202.559 214.152 1.00 20.05  ? 4086 THR A CB    1 
ATOM   18644 O  OG1   . THR A 1 4086 ? 189.546 203.742 214.791 1.00 29.35  ? 4086 THR A OG1   1 
ATOM   18645 C  CG2   . THR A 1 4086 ? 189.066 202.137 213.067 1.00 21.94  ? 4086 THR A CG2   1 
ATOM   18646 N  N     . ALA A 1 4087 ? 192.121 200.167 214.374 1.00 23.65  ? 4087 ALA A N     1 
ATOM   18647 C  CA    . ALA A 1 4087 ? 192.755 199.096 213.617 1.00 19.67  ? 4087 ALA A CA    1 
ATOM   18648 C  C     . ALA A 1 4087 ? 192.859 197.795 214.402 1.00 21.19  ? 4087 ALA A C     1 
ATOM   18649 O  O     . ALA A 1 4087 ? 192.860 196.718 213.795 1.00 18.59  ? 4087 ALA A O     1 
ATOM   18650 C  CB    . ALA A 1 4087 ? 194.143 199.534 213.151 1.00 21.59  ? 4087 ALA A CB    1 
ATOM   18651 N  N     . VAL A 1 4088 ? 192.961 197.858 215.733 1.00 20.50  ? 4088 VAL A N     1 
ATOM   18652 C  CA    . VAL A 1 4088 ? 193.026 196.622 216.507 1.00 21.12  ? 4088 VAL A CA    1 
ATOM   18653 C  C     . VAL A 1 4088 ? 191.730 195.832 216.397 1.00 25.43  ? 4088 VAL A C     1 
ATOM   18654 O  O     . VAL A 1 4088 ? 191.722 194.620 216.635 1.00 30.12  ? 4088 VAL A O     1 
ATOM   18655 C  CB    . VAL A 1 4088 ? 193.371 196.902 217.985 1.00 18.51  ? 4088 VAL A CB    1 
ATOM   18656 C  CG1   . VAL A 1 4088 ? 194.782 197.444 218.105 1.00 16.32  ? 4088 VAL A CG1   1 
ATOM   18657 C  CG2   . VAL A 1 4088 ? 192.364 197.854 218.603 1.00 25.85  ? 4088 VAL A CG2   1 
ATOM   18658 N  N     . LYS A 1 4089 ? 190.630 196.491 216.038 1.00 24.04  ? 4089 LYS A N     1 
ATOM   18659 C  CA    . LYS A 1 4089 ? 189.360 195.820 215.791 1.00 25.10  ? 4089 LYS A CA    1 
ATOM   18660 C  C     . LYS A 1 4089 ? 189.109 195.555 214.314 1.00 23.81  ? 4089 LYS A C     1 
ATOM   18661 O  O     . LYS A 1 4089 ? 188.649 194.466 213.956 1.00 26.97  ? 4089 LYS A O     1 
ATOM   18662 C  CB    . LYS A 1 4089 ? 188.205 196.649 216.360 1.00 24.53  ? 4089 LYS A CB    1 
ATOM   18663 C  CG    . LYS A 1 4089 ? 187.918 196.389 217.826 1.00 27.45  ? 4089 LYS A CG    1 
ATOM   18664 C  CD    . LYS A 1 4089 ? 187.443 197.653 218.523 1.00 36.66  ? 4089 LYS A CD    1 
ATOM   18665 C  CE    . LYS A 1 4089 ? 187.390 197.465 220.030 1.00 43.47  ? 4089 LYS A CE    1 
ATOM   18666 N  NZ    . LYS A 1 4089 ? 186.644 198.566 220.698 1.00 55.03  ? 4089 LYS A NZ    1 
ATOM   18667 N  N     . SER A 1 4090 ? 189.399 196.525 213.444 1.00 22.60  ? 4090 SER A N     1 
ATOM   18668 C  CA    . SER A 1 4090 ? 189.143 196.348 212.018 1.00 22.06  ? 4090 SER A CA    1 
ATOM   18669 C  C     . SER A 1 4090 ? 190.159 195.426 211.357 1.00 20.87  ? 4090 SER A C     1 
ATOM   18670 O  O     . SER A 1 4090 ? 189.811 194.703 210.418 1.00 27.22  ? 4090 SER A O     1 
ATOM   18671 C  CB    . SER A 1 4090 ? 189.136 197.703 211.311 1.00 29.10  ? 4090 SER A CB    1 
ATOM   18672 O  OG    . SER A 1 4090 ? 190.393 198.344 211.427 1.00 28.83  ? 4090 SER A OG    1 
ATOM   18673 N  N     . GLY A 1 4091 ? 191.403 195.435 211.822 1.00 23.58  ? 4091 GLY A N     1 
ATOM   18674 C  CA    . GLY A 1 4091 ? 192.453 194.651 211.211 1.00 20.29  ? 4091 GLY A CA    1 
ATOM   18675 C  C     . GLY A 1 4091 ? 193.335 195.394 210.233 1.00 23.28  ? 4091 GLY A C     1 
ATOM   18676 O  O     . GLY A 1 4091 ? 194.111 194.751 209.520 1.00 20.37  ? 4091 GLY A O     1 
ATOM   18677 N  N     . ARG A 1 4092 ? 193.239 196.719 210.175 1.00 25.53  ? 4092 ARG A N     1 
ATOM   18678 C  CA    . ARG A 1 4092 ? 194.064 197.507 209.276 1.00 20.07  ? 4092 ARG A CA    1 
ATOM   18679 C  C     . ARG A 1 4092 ? 195.466 197.666 209.858 1.00 17.11  ? 4092 ARG A C     1 
ATOM   18680 O  O     . ARG A 1 4092 ? 195.799 197.119 210.912 1.00 14.01  ? 4092 ARG A O     1 
ATOM   18681 C  CB    . ARG A 1 4092 ? 193.412 198.863 209.014 1.00 26.15  ? 4092 ARG A CB    1 
ATOM   18682 C  CG    . ARG A 1 4092 ? 192.087 198.779 208.273 1.00 30.27  ? 4092 ARG A CG    1 
ATOM   18683 C  CD    . ARG A 1 4092 ? 191.466 200.154 208.055 1.00 42.75  ? 4092 ARG A CD    1 
ATOM   18684 N  NE    . ARG A 1 4092 ? 192.249 200.987 207.149 1.00 44.78  ? 4092 ARG A NE    1 
ATOM   18685 C  CZ    . ARG A 1 4092 ? 192.942 202.055 207.519 1.00 47.15  ? 4092 ARG A CZ    1 
ATOM   18686 N  NH1   . ARG A 1 4092 ? 192.992 202.443 208.783 1.00 45.96  ? 4092 ARG A NH1   1 
ATOM   18687 N  NH2   . ARG A 1 4092 ? 193.601 202.752 206.598 1.00 38.91  ? 4092 ARG A NH2   1 
ATOM   18688 N  N     . TRP A 1 4093 ? 196.304 198.428 209.161 1.00 24.41  ? 4093 TRP A N     1 
ATOM   18689 C  CA    . TRP A 1 4093 ? 197.681 198.657 209.572 1.00 15.84  ? 4093 TRP A CA    1 
ATOM   18690 C  C     . TRP A 1 4093 ? 197.870 200.106 209.997 1.00 18.43  ? 4093 TRP A C     1 
ATOM   18691 O  O     . TRP A 1 4093 ? 197.281 201.019 209.411 1.00 21.51  ? 4093 TRP A O     1 
ATOM   18692 C  CB    . TRP A 1 4093 ? 198.653 198.321 208.442 1.00 13.45  ? 4093 TRP A CB    1 
ATOM   18693 C  CG    . TRP A 1 4093 ? 198.764 196.861 208.152 1.00 14.20  ? 4093 TRP A CG    1 
ATOM   18694 C  CD1   . TRP A 1 4093 ? 198.002 195.860 208.676 1.00 14.71  ? 4093 TRP A CD1   1 
ATOM   18695 C  CD2   . TRP A 1 4093 ? 199.692 196.237 207.262 1.00 15.24  ? 4093 TRP A CD2   1 
ATOM   18696 N  NE1   . TRP A 1 4093 ? 198.400 194.649 208.168 1.00 15.75  ? 4093 TRP A NE1   1 
ATOM   18697 C  CE2   . TRP A 1 4093 ? 199.436 194.854 207.297 1.00 16.95  ? 4093 TRP A CE2   1 
ATOM   18698 C  CE3   . TRP A 1 4093 ? 200.715 196.712 206.438 1.00 16.86  ? 4093 TRP A CE3   1 
ATOM   18699 C  CZ2   . TRP A 1 4093 ? 200.166 193.942 206.541 1.00 18.41  ? 4093 TRP A CZ2   1 
ATOM   18700 C  CZ3   . TRP A 1 4093 ? 201.436 195.807 205.691 1.00 13.55  ? 4093 TRP A CZ3   1 
ATOM   18701 C  CH2   . TRP A 1 4093 ? 201.158 194.439 205.747 1.00 14.17  ? 4093 TRP A CH2   1 
ATOM   18702 N  N     . VAL A 1 4094 ? 198.691 200.312 211.022 1.00 18.51  ? 4094 VAL A N     1 
ATOM   18703 C  CA    . VAL A 1 4094 ? 199.012 201.647 211.511 1.00 14.17  ? 4094 VAL A CA    1 
ATOM   18704 C  C     . VAL A 1 4094 ? 200.523 201.809 211.515 1.00 16.46  ? 4094 VAL A C     1 
ATOM   18705 O  O     . VAL A 1 4094 ? 201.237 200.973 212.078 1.00 13.39  ? 4094 VAL A O     1 
ATOM   18706 C  CB    . VAL A 1 4094 ? 198.441 201.899 212.920 1.00 11.14  ? 4094 VAL A CB    1 
ATOM   18707 C  CG1   . VAL A 1 4094 ? 198.889 203.255 213.435 1.00 14.41  ? 4094 VAL A CG1   1 
ATOM   18708 C  CG2   . VAL A 1 4094 ? 196.930 201.815 212.900 1.00 17.78  ? 4094 VAL A CG2   1 
ATOM   18709 N  N     . MET A 1 4095 ? 201.008 202.878 210.889 1.00 15.56  ? 4095 MET A N     1 
ATOM   18710 C  CA    . MET A 1 4095 ? 202.419 203.235 210.913 1.00 13.37  ? 4095 MET A CA    1 
ATOM   18711 C  C     . MET A 1 4095 ? 202.584 204.570 211.620 1.00 14.94  ? 4095 MET A C     1 
ATOM   18712 O  O     . MET A 1 4095 ? 201.840 205.519 211.348 1.00 15.75  ? 4095 MET A O     1 
ATOM   18713 C  CB    . MET A 1 4095 ? 203.006 203.312 209.502 1.00 14.96  ? 4095 MET A CB    1 
ATOM   18714 C  CG    . MET A 1 4095 ? 204.491 203.632 209.481 1.00 15.02  ? 4095 MET A CG    1 
ATOM   18715 S  SD    . MET A 1 4095 ? 205.181 203.695 207.820 1.00 32.49  ? 4095 MET A SD    1 
ATOM   18716 C  CE    . MET A 1 4095 ? 204.467 205.214 207.209 1.00 22.93  ? 4095 MET A CE    1 
ATOM   18717 N  N     . LEU A 1 4096 ? 203.543 204.632 212.538 1.00 11.04  ? 4096 LEU A N     1 
ATOM   18718 C  CA    . LEU A 1 4096 ? 203.883 205.854 213.253 1.00 10.68  ? 4096 LEU A CA    1 
ATOM   18719 C  C     . LEU A 1 4096 ? 205.336 206.200 212.960 1.00 13.58  ? 4096 LEU A C     1 
ATOM   18720 O  O     . LEU A 1 4096 ? 206.232 205.371 213.167 1.00 13.27  ? 4096 LEU A O     1 
ATOM   18721 C  CB    . LEU A 1 4096 ? 203.642 205.698 214.757 1.00 11.65  ? 4096 LEU A CB    1 
ATOM   18722 C  CG    . LEU A 1 4096 ? 202.272 205.130 215.134 1.00 7.42   ? 4096 LEU A CG    1 
ATOM   18723 C  CD1   . LEU A 1 4096 ? 202.175 204.886 216.628 1.00 7.11   ? 4096 LEU A CD1   1 
ATOM   18724 C  CD2   . LEU A 1 4096 ? 201.161 206.056 214.670 1.00 9.09   ? 4096 LEU A CD2   1 
ATOM   18725 N  N     . LYS A 1 4097 ? 205.559 207.421 212.485 1.00 15.02  ? 4097 LYS A N     1 
ATOM   18726 C  CA    . LYS A 1 4097 ? 206.865 207.868 212.029 1.00 9.44   ? 4097 LYS A CA    1 
ATOM   18727 C  C     . LYS A 1 4097 ? 207.529 208.760 213.070 1.00 9.12   ? 4097 LYS A C     1 
ATOM   18728 O  O     . LYS A 1 4097 ? 206.868 209.537 213.763 1.00 11.72  ? 4097 LYS A O     1 
ATOM   18729 C  CB    . LYS A 1 4097 ? 206.752 208.624 210.704 1.00 9.48   ? 4097 LYS A CB    1 
ATOM   18730 C  CG    . LYS A 1 4097 ? 205.830 207.980 209.686 1.00 8.35   ? 4097 LYS A CG    1 
ATOM   18731 C  CD    . LYS A 1 4097 ? 205.976 208.647 208.331 1.00 10.50  ? 4097 LYS A CD    1 
ATOM   18732 C  CE    . LYS A 1 4097 ? 204.641 208.750 207.613 1.00 22.98  ? 4097 LYS A CE    1 
ATOM   18733 N  NZ    . LYS A 1 4097 ? 203.670 209.600 208.352 1.00 19.84  ? 4097 LYS A NZ    1 
ATOM   18734 N  N     . ASN A 1 4098 ? 208.854 208.638 213.162 1.00 8.95   ? 4098 ASN A N     1 
ATOM   18735 C  CA    . ASN A 1 4098 ? 209.675 209.469 214.044 1.00 8.66   ? 4098 ASN A CA    1 
ATOM   18736 C  C     . ASN A 1 4098 ? 209.218 209.368 215.496 1.00 10.64  ? 4098 ASN A C     1 
ATOM   18737 O  O     . ASN A 1 4098 ? 209.129 210.370 216.210 1.00 15.57  ? 4098 ASN A O     1 
ATOM   18738 C  CB    . ASN A 1 4098 ? 209.682 210.926 213.575 1.00 12.54  ? 4098 ASN A CB    1 
ATOM   18739 C  CG    . ASN A 1 4098 ? 209.850 211.055 212.075 1.00 10.76  ? 4098 ASN A CG    1 
ATOM   18740 O  OD1   . ASN A 1 4098 ? 209.059 211.717 211.405 1.00 8.73   ? 4098 ASN A OD1   1 
ATOM   18741 N  ND2   . ASN A 1 4098 ? 210.886 210.425 211.539 1.00 10.55  ? 4098 ASN A ND2   1 
ATOM   18742 N  N     . VAL A 1 4099 ? 208.927 208.144 215.943 1.00 12.55  ? 4099 VAL A N     1 
ATOM   18743 C  CA    . VAL A 1 4099 ? 208.506 207.923 217.321 1.00 10.02  ? 4099 VAL A CA    1 
ATOM   18744 C  C     . VAL A 1 4099 ? 209.620 208.174 218.323 1.00 9.30   ? 4099 VAL A C     1 
ATOM   18745 O  O     . VAL A 1 4099 ? 209.349 208.268 219.524 1.00 11.76  ? 4099 VAL A O     1 
ATOM   18746 C  CB    . VAL A 1 4099 ? 207.962 206.491 217.501 1.00 7.29   ? 4099 VAL A CB    1 
ATOM   18747 C  CG1   . VAL A 1 4099 ? 206.749 206.273 216.620 1.00 9.53   ? 4099 VAL A CG1   1 
ATOM   18748 C  CG2   . VAL A 1 4099 ? 209.039 205.472 217.185 1.00 8.58   ? 4099 VAL A CG2   1 
ATOM   18749 N  N     . HIS A 1 4100 ? 210.868 208.283 217.862 1.00 10.62  ? 4100 HIS A N     1 
ATOM   18750 C  CA    . HIS A 1 4100 ? 211.976 208.599 218.755 1.00 10.23  ? 4100 HIS A CA    1 
ATOM   18751 C  C     . HIS A 1 4100 ? 211.933 210.034 219.260 1.00 11.45  ? 4100 HIS A C     1 
ATOM   18752 O  O     . HIS A 1 4100 ? 212.668 210.363 220.197 1.00 14.00  ? 4100 HIS A O     1 
ATOM   18753 C  CB    . HIS A 1 4100 ? 213.308 208.337 218.051 1.00 11.41  ? 4100 HIS A CB    1 
ATOM   18754 C  CG    . HIS A 1 4100 ? 213.567 209.244 216.888 1.00 12.05  ? 4100 HIS A CG    1 
ATOM   18755 N  ND1   . HIS A 1 4100 ? 213.049 209.011 215.633 1.00 10.78  ? 4100 HIS A ND1   1 
ATOM   18756 C  CD2   . HIS A 1 4100 ? 214.292 210.382 216.791 1.00 12.48  ? 4100 HIS A CD2   1 
ATOM   18757 C  CE1   . HIS A 1 4100 ? 213.443 209.967 214.812 1.00 10.66  ? 4100 HIS A CE1   1 
ATOM   18758 N  NE2   . HIS A 1 4100 ? 214.199 210.813 215.489 1.00 13.71  ? 4100 HIS A NE2   1 
ATOM   18759 N  N     . LEU A 1 4101 ? 211.099 210.889 218.670 1.00 11.02  ? 4101 LEU A N     1 
ATOM   18760 C  CA    . LEU A 1 4101 ? 210.960 212.262 219.132 1.00 9.43   ? 4101 LEU A CA    1 
ATOM   18761 C  C     . LEU A 1 4101 ? 210.015 212.394 220.318 1.00 10.80  ? 4101 LEU A C     1 
ATOM   18762 O  O     . LEU A 1 4101 ? 209.912 213.485 220.888 1.00 16.40  ? 4101 LEU A O     1 
ATOM   18763 C  CB    . LEU A 1 4101 ? 210.478 213.156 217.987 1.00 11.31  ? 4101 LEU A CB    1 
ATOM   18764 C  CG    . LEU A 1 4101 ? 211.349 213.157 216.730 1.00 10.73  ? 4101 LEU A CG    1 
ATOM   18765 C  CD1   . LEU A 1 4101 ? 210.640 213.864 215.590 1.00 11.71  ? 4101 LEU A CD1   1 
ATOM   18766 C  CD2   . LEU A 1 4101 ? 212.691 213.807 217.012 1.00 9.61   ? 4101 LEU A CD2   1 
ATOM   18767 N  N     . ALA A 1 4102 ? 209.326 211.321 220.700 1.00 11.67  ? 4102 ALA A N     1 
ATOM   18768 C  CA    . ALA A 1 4102 ? 208.456 211.304 221.873 1.00 10.61  ? 4102 ALA A CA    1 
ATOM   18769 C  C     . ALA A 1 4102 ? 208.794 210.083 222.717 1.00 13.29  ? 4102 ALA A C     1 
ATOM   18770 O  O     . ALA A 1 4102 ? 208.027 209.114 222.770 1.00 11.24  ? 4102 ALA A O     1 
ATOM   18771 C  CB    . ALA A 1 4102 ? 206.982 211.303 221.467 1.00 11.54  ? 4102 ALA A CB    1 
ATOM   18772 N  N     . PRO A 1 4103 ? 209.951 210.092 223.383 1.00 16.25  ? 4103 PRO A N     1 
ATOM   18773 C  CA    . PRO A 1 4103 ? 210.340 208.918 224.182 1.00 16.71  ? 4103 PRO A CA    1 
ATOM   18774 C  C     . PRO A 1 4103 ? 209.374 208.600 225.307 1.00 18.48  ? 4103 PRO A C     1 
ATOM   18775 O  O     . PRO A 1 4103 ? 209.165 207.421 225.615 1.00 20.65  ? 4103 PRO A O     1 
ATOM   18776 C  CB    . PRO A 1 4103 ? 211.725 209.306 224.717 1.00 17.66  ? 4103 PRO A CB    1 
ATOM   18777 C  CG    . PRO A 1 4103 ? 211.726 210.793 224.714 1.00 18.24  ? 4103 PRO A CG    1 
ATOM   18778 C  CD    . PRO A 1 4103 ? 210.905 211.203 223.530 1.00 16.63  ? 4103 PRO A CD    1 
ATOM   18779 N  N     . GLY A 1 4104 ? 208.781 209.616 225.937 1.00 19.83  ? 4104 GLY A N     1 
ATOM   18780 C  CA    . GLY A 1 4104 ? 207.839 209.353 227.011 1.00 17.81  ? 4104 GLY A CA    1 
ATOM   18781 C  C     . GLY A 1 4104 ? 206.591 208.634 226.538 1.00 17.77  ? 4104 GLY A C     1 
ATOM   18782 O  O     . GLY A 1 4104 ? 206.175 207.640 227.137 1.00 22.45  ? 4104 GLY A O     1 
ATOM   18783 N  N     . TRP A 1 4105 ? 205.994 209.107 225.439 1.00 17.42  ? 4105 TRP A N     1 
ATOM   18784 C  CA    . TRP A 1 4105 ? 204.754 208.532 224.928 1.00 16.24  ? 4105 TRP A CA    1 
ATOM   18785 C  C     . TRP A 1 4105 ? 204.923 207.082 224.492 1.00 17.37  ? 4105 TRP A C     1 
ATOM   18786 O  O     . TRP A 1 4105 ? 203.951 206.315 224.526 1.00 18.04  ? 4105 TRP A O     1 
ATOM   18787 C  CB    . TRP A 1 4105 ? 204.242 209.385 223.764 1.00 15.83  ? 4105 TRP A CB    1 
ATOM   18788 C  CG    . TRP A 1 4105 ? 203.013 208.858 223.097 1.00 16.74  ? 4105 TRP A CG    1 
ATOM   18789 C  CD1   . TRP A 1 4105 ? 201.726 209.008 223.518 1.00 18.45  ? 4105 TRP A CD1   1 
ATOM   18790 C  CD2   . TRP A 1 4105 ? 202.953 208.103 221.883 1.00 17.25  ? 4105 TRP A CD2   1 
ATOM   18791 N  NE1   . TRP A 1 4105 ? 200.867 208.391 222.643 1.00 17.65  ? 4105 TRP A NE1   1 
ATOM   18792 C  CE2   . TRP A 1 4105 ? 201.596 207.826 221.630 1.00 14.92  ? 4105 TRP A CE2   1 
ATOM   18793 C  CE3   . TRP A 1 4105 ? 203.916 207.630 220.986 1.00 18.38  ? 4105 TRP A CE3   1 
ATOM   18794 C  CZ2   . TRP A 1 4105 ? 201.178 207.099 220.522 1.00 16.28  ? 4105 TRP A CZ2   1 
ATOM   18795 C  CZ3   . TRP A 1 4105 ? 203.498 206.908 219.886 1.00 18.09  ? 4105 TRP A CZ3   1 
ATOM   18796 C  CH2   . TRP A 1 4105 ? 202.142 206.650 219.663 1.00 17.33  ? 4105 TRP A CH2   1 
ATOM   18797 N  N     . LEU A 1 4106 ? 206.135 206.692 224.094 1.00 18.61  ? 4106 LEU A N     1 
ATOM   18798 C  CA    . LEU A 1 4106 ? 206.383 205.317 223.677 1.00 16.40  ? 4106 LEU A CA    1 
ATOM   18799 C  C     . LEU A 1 4106 ? 206.151 204.340 224.821 1.00 20.42  ? 4106 LEU A C     1 
ATOM   18800 O  O     . LEU A 1 4106 ? 205.737 203.199 224.595 1.00 24.19  ? 4106 LEU A O     1 
ATOM   18801 C  CB    . LEU A 1 4106 ? 207.807 205.188 223.137 1.00 15.97  ? 4106 LEU A CB    1 
ATOM   18802 C  CG    . LEU A 1 4106 ? 208.013 205.577 221.671 1.00 11.49  ? 4106 LEU A CG    1 
ATOM   18803 C  CD1   . LEU A 1 4106 ? 209.457 205.364 221.259 1.00 11.68  ? 4106 LEU A CD1   1 
ATOM   18804 C  CD2   . LEU A 1 4106 ? 207.078 204.793 220.770 1.00 12.11  ? 4106 LEU A CD2   1 
ATOM   18805 N  N     . MET A 1 4107 ? 206.397 204.772 226.061 1.00 20.23  ? 4107 MET A N     1 
ATOM   18806 C  CA    . MET A 1 4107 ? 206.164 203.892 227.202 1.00 17.71  ? 4107 MET A CA    1 
ATOM   18807 C  C     . MET A 1 4107 ? 204.679 203.601 227.386 1.00 16.71  ? 4107 MET A C     1 
ATOM   18808 O  O     . MET A 1 4107 ? 204.283 202.436 227.533 1.00 18.89  ? 4107 MET A O     1 
ATOM   18809 C  CB    . MET A 1 4107 ? 206.761 204.505 228.467 1.00 23.16  ? 4107 MET A CB    1 
ATOM   18810 C  CG    . MET A 1 4107 ? 208.279 204.590 228.447 1.00 29.76  ? 4107 MET A CG    1 
ATOM   18811 S  SD    . MET A 1 4107 ? 208.968 205.389 229.908 1.00 75.47  ? 4107 MET A SD    1 
ATOM   18812 C  CE    . MET A 1 4107 ? 208.647 204.145 231.155 1.00 57.00  ? 4107 MET A CE    1 
ATOM   18813 N  N     . GLN A 1 4108 ? 203.836 204.640 227.379 1.00 17.60  ? 4108 GLN A N     1 
ATOM   18814 C  CA    . GLN A 1 4108 ? 202.399 204.397 227.458 1.00 21.89  ? 4108 GLN A CA    1 
ATOM   18815 C  C     . GLN A 1 4108 ? 201.915 203.591 226.262 1.00 18.66  ? 4108 GLN A C     1 
ATOM   18816 O  O     . GLN A 1 4108 ? 200.995 202.776 226.391 1.00 19.68  ? 4108 GLN A O     1 
ATOM   18817 C  CB    . GLN A 1 4108 ? 201.613 205.706 227.573 1.00 25.13  ? 4108 GLN A CB    1 
ATOM   18818 C  CG    . GLN A 1 4108 ? 201.822 206.482 228.870 1.00 35.96  ? 4108 GLN A CG    1 
ATOM   18819 C  CD    . GLN A 1 4108 ? 203.069 207.327 228.863 1.00 38.25  ? 4108 GLN A CD    1 
ATOM   18820 O  OE1   . GLN A 1 4108 ? 203.630 207.607 227.809 1.00 38.57  ? 4108 GLN A OE1   1 
ATOM   18821 N  NE2   . GLN A 1 4108 ? 203.511 207.746 230.042 1.00 41.47  ? 4108 GLN A NE2   1 
ATOM   18822 N  N     . LEU A 1 4109 ? 202.528 203.790 225.093 1.00 19.77  ? 4109 LEU A N     1 
ATOM   18823 C  CA    . LEU A 1 4109 ? 202.169 202.970 223.939 1.00 17.79  ? 4109 LEU A CA    1 
ATOM   18824 C  C     . LEU A 1 4109 ? 202.496 201.500 224.186 1.00 17.52  ? 4109 LEU A C     1 
ATOM   18825 O  O     . LEU A 1 4109 ? 201.711 200.613 223.833 1.00 18.93  ? 4109 LEU A O     1 
ATOM   18826 C  CB    . LEU A 1 4109 ? 202.885 203.480 222.688 1.00 18.53  ? 4109 LEU A CB    1 
ATOM   18827 C  CG    . LEU A 1 4109 ? 202.875 202.543 221.480 1.00 16.59  ? 4109 LEU A CG    1 
ATOM   18828 C  CD1   . LEU A 1 4109 ? 201.481 202.452 220.891 1.00 13.47  ? 4109 LEU A CD1   1 
ATOM   18829 C  CD2   . LEU A 1 4109 ? 203.870 203.005 220.433 1.00 14.28  ? 4109 LEU A CD2   1 
ATOM   18830 N  N     . GLU A 1 4110 ? 203.652 201.225 224.793 1.00 17.02  ? 4110 GLU A N     1 
ATOM   18831 C  CA    . GLU A 1 4110 ? 204.032 199.848 225.090 1.00 17.93  ? 4110 GLU A CA    1 
ATOM   18832 C  C     . GLU A 1 4110 ? 203.078 199.211 226.094 1.00 22.49  ? 4110 GLU A C     1 
ATOM   18833 O  O     . GLU A 1 4110 ? 202.667 198.056 225.925 1.00 24.50  ? 4110 GLU A O     1 
ATOM   18834 C  CB    . GLU A 1 4110 ? 205.470 199.807 225.608 1.00 20.30  ? 4110 GLU A CB    1 
ATOM   18835 C  CG    . GLU A 1 4110 ? 206.122 198.433 225.567 1.00 21.19  ? 4110 GLU A CG    1 
ATOM   18836 C  CD    . GLU A 1 4110 ? 205.894 197.638 226.838 1.00 35.59  ? 4110 GLU A CD    1 
ATOM   18837 O  OE1   . GLU A 1 4110 ? 206.092 198.201 227.934 1.00 32.42  ? 4110 GLU A OE1   1 
ATOM   18838 O  OE2   . GLU A 1 4110 ? 205.522 196.449 226.741 1.00 37.14  ? 4110 GLU A OE2   1 
ATOM   18839 N  N     . LYS A 1 4111 ? 202.719 199.948 227.149 1.00 23.63  ? 4111 LYS A N     1 
ATOM   18840 C  CA    . LYS A 1 4111 ? 201.754 199.419 228.114 1.00 18.39  ? 4111 LYS A CA    1 
ATOM   18841 C  C     . LYS A 1 4111 ? 200.387 199.195 227.476 1.00 21.65  ? 4111 LYS A C     1 
ATOM   18842 O  O     . LYS A 1 4111 ? 199.699 198.218 227.796 1.00 26.10  ? 4111 LYS A O     1 
ATOM   18843 C  CB    . LYS A 1 4111 ? 201.639 200.333 229.336 1.00 16.07  ? 4111 LYS A CB    1 
ATOM   18844 C  CG    . LYS A 1 4111 ? 202.746 200.158 230.377 1.00 28.70  ? 4111 LYS A CG    1 
ATOM   18845 C  CD    . LYS A 1 4111 ? 204.074 200.721 229.928 1.00 33.42  ? 4111 LYS A CD    1 
ATOM   18846 C  CE    . LYS A 1 4111 ? 205.127 200.617 231.012 1.00 34.17  ? 4111 LYS A CE    1 
ATOM   18847 N  NZ    . LYS A 1 4111 ? 206.461 201.067 230.521 1.00 36.46  ? 4111 LYS A NZ    1 
ATOM   18848 N  N     . LYS A 1 4112 ? 199.968 200.091 226.579 1.00 19.05  ? 4112 LYS A N     1 
ATOM   18849 C  CA    . LYS A 1 4112 ? 198.697 199.904 225.888 1.00 16.54  ? 4112 LYS A CA    1 
ATOM   18850 C  C     . LYS A 1 4112 ? 198.736 198.670 224.993 1.00 23.83  ? 4112 LYS A C     1 
ATOM   18851 O  O     . LYS A 1 4112 ? 197.755 197.922 224.907 1.00 26.37  ? 4112 LYS A O     1 
ATOM   18852 C  CB    . LYS A 1 4112 ? 198.358 201.155 225.077 1.00 16.05  ? 4112 LYS A CB    1 
ATOM   18853 C  CG    . LYS A 1 4112 ? 197.439 200.913 223.893 1.00 27.63  ? 4112 LYS A CG    1 
ATOM   18854 C  CD    . LYS A 1 4112 ? 197.217 202.188 223.104 1.00 22.45  ? 4112 LYS A CD    1 
ATOM   18855 C  CE    . LYS A 1 4112 ? 196.004 202.072 222.200 1.00 22.62  ? 4112 LYS A CE    1 
ATOM   18856 N  NZ    . LYS A 1 4112 ? 194.870 201.396 222.885 1.00 32.53  ? 4112 LYS A NZ    1 
ATOM   18857 N  N     . LEU A 1 4113 ? 199.867 198.442 224.322 1.00 26.17  ? 4113 LEU A N     1 
ATOM   18858 C  CA    . LEU A 1 4113 ? 200.003 197.279 223.453 1.00 20.74  ? 4113 LEU A CA    1 
ATOM   18859 C  C     . LEU A 1 4113 ? 200.029 195.982 224.250 1.00 23.26  ? 4113 LEU A C     1 
ATOM   18860 O  O     . LEU A 1 4113 ? 199.495 194.961 223.802 1.00 23.59  ? 4113 LEU A O     1 
ATOM   18861 C  CB    . LEU A 1 4113 ? 201.269 197.403 222.609 1.00 18.38  ? 4113 LEU A CB    1 
ATOM   18862 C  CG    . LEU A 1 4113 ? 201.227 198.351 221.413 1.00 17.68  ? 4113 LEU A CG    1 
ATOM   18863 C  CD1   . LEU A 1 4113 ? 202.635 198.606 220.906 1.00 15.97  ? 4113 LEU A CD1   1 
ATOM   18864 C  CD2   . LEU A 1 4113 ? 200.349 197.783 220.312 1.00 17.64  ? 4113 LEU A CD2   1 
ATOM   18865 N  N     . HIS A 1 4114 ? 200.662 195.998 225.428 1.00 26.48  ? 4114 HIS A N     1 
ATOM   18866 C  CA    . HIS A 1 4114 ? 200.829 194.768 226.198 1.00 26.19  ? 4114 HIS A CA    1 
ATOM   18867 C  C     . HIS A 1 4114 ? 199.485 194.176 226.607 1.00 27.51  ? 4114 HIS A C     1 
ATOM   18868 O  O     . HIS A 1 4114 ? 199.275 192.963 226.503 1.00 23.02  ? 4114 HIS A O     1 
ATOM   18869 C  CB    . HIS A 1 4114 ? 201.692 195.037 227.430 1.00 26.33  ? 4114 HIS A CB    1 
ATOM   18870 C  CG    . HIS A 1 4114 ? 201.934 193.824 228.274 1.00 29.95  ? 4114 HIS A CG    1 
ATOM   18871 N  ND1   . HIS A 1 4114 ? 202.670 192.746 227.833 1.00 30.80  ? 4114 HIS A ND1   1 
ATOM   18872 C  CD2   . HIS A 1 4114 ? 201.532 193.517 229.529 1.00 24.34  ? 4114 HIS A CD2   1 
ATOM   18873 C  CE1   . HIS A 1 4114 ? 202.715 191.829 228.782 1.00 25.95  ? 4114 HIS A CE1   1 
ATOM   18874 N  NE2   . HIS A 1 4114 ? 202.032 192.272 229.822 1.00 23.70  ? 4114 HIS A NE2   1 
ATOM   18875 N  N     . SER A 1 4115 ? 198.563 195.018 227.071 1.00 31.69  ? 4115 SER A N     1 
ATOM   18876 C  CA    . SER A 1 4115 ? 197.230 194.567 227.470 1.00 35.55  ? 4115 SER A CA    1 
ATOM   18877 C  C     . SER A 1 4115 ? 196.255 194.783 226.312 1.00 32.94  ? 4115 SER A C     1 
ATOM   18878 O  O     . SER A 1 4115 ? 195.375 195.643 226.340 1.00 34.79  ? 4115 SER A O     1 
ATOM   18879 C  CB    . SER A 1 4115 ? 196.779 195.295 228.730 1.00 39.96  ? 4115 SER A CB    1 
ATOM   18880 O  OG    . SER A 1 4115 ? 196.668 196.688 228.495 1.00 30.69  ? 4115 SER A OG    1 
ATOM   18881 N  N     . LEU A 1 4116 ? 196.429 193.965 225.277 1.00 29.98  ? 4116 LEU A N     1 
ATOM   18882 C  CA    . LEU A 1 4116 ? 195.657 194.125 224.055 1.00 27.81  ? 4116 LEU A CA    1 
ATOM   18883 C  C     . LEU A 1 4116 ? 195.706 192.829 223.259 1.00 33.06  ? 4116 LEU A C     1 
ATOM   18884 O  O     . LEU A 1 4116 ? 196.758 192.192 223.165 1.00 43.86  ? 4116 LEU A O     1 
ATOM   18885 C  CB    . LEU A 1 4116 ? 196.202 195.291 223.221 1.00 31.41  ? 4116 LEU A CB    1 
ATOM   18886 C  CG    . LEU A 1 4116 ? 195.308 195.909 222.150 1.00 33.64  ? 4116 LEU A CG    1 
ATOM   18887 C  CD1   . LEU A 1 4116 ? 194.000 196.381 222.754 1.00 28.94  ? 4116 LEU A CD1   1 
ATOM   18888 C  CD2   . LEU A 1 4116 ? 196.038 197.062 221.488 1.00 28.91  ? 4116 LEU A CD2   1 
ATOM   18889 N  N     . GLN A 1 4117 ? 194.563 192.448 222.689 1.00 32.98  ? 4117 GLN A N     1 
ATOM   18890 C  CA    . GLN A 1 4117 ? 194.444 191.258 221.847 1.00 33.66  ? 4117 GLN A CA    1 
ATOM   18891 C  C     . GLN A 1 4117 ? 193.792 191.691 220.541 1.00 34.34  ? 4117 GLN A C     1 
ATOM   18892 O  O     . GLN A 1 4117 ? 192.575 191.552 220.359 1.00 35.48  ? 4117 GLN A O     1 
ATOM   18893 C  CB    . GLN A 1 4117 ? 193.642 190.158 222.544 1.00 32.87  ? 4117 GLN A CB    1 
ATOM   18894 C  CG    . GLN A 1 4117 ? 193.540 188.852 221.763 1.00 46.03  ? 4117 GLN A CG    1 
ATOM   18895 C  CD    . GLN A 1 4117 ? 194.887 188.334 221.291 1.00 49.13  ? 4117 GLN A CD    1 
ATOM   18896 O  OE1   . GLN A 1 4117 ? 195.037 187.918 220.141 1.00 41.94  ? 4117 GLN A OE1   1 
ATOM   18897 N  NE2   . GLN A 1 4117 ? 195.872 188.339 222.184 1.00 49.93  ? 4117 GLN A NE2   1 
ATOM   18898 N  N     . PRO A 1 4118 ? 194.573 192.224 219.611 1.00 34.61  ? 4118 PRO A N     1 
ATOM   18899 C  CA    . PRO A 1 4118 ? 194.007 192.859 218.419 1.00 32.53  ? 4118 PRO A CA    1 
ATOM   18900 C  C     . PRO A 1 4118 ? 193.570 191.830 217.381 1.00 30.70  ? 4118 PRO A C     1 
ATOM   18901 O  O     . PRO A 1 4118 ? 193.625 190.621 217.596 1.00 31.10  ? 4118 PRO A O     1 
ATOM   18902 C  CB    . PRO A 1 4118 ? 195.166 193.713 217.907 1.00 24.41  ? 4118 PRO A CB    1 
ATOM   18903 C  CG    . PRO A 1 4118 ? 196.381 192.977 218.336 1.00 22.79  ? 4118 PRO A CG    1 
ATOM   18904 C  CD    . PRO A 1 4118 ? 196.045 192.288 219.630 1.00 27.86  ? 4118 PRO A CD    1 
ATOM   18905 N  N     . HIS A 1 4119 ? 193.126 192.346 216.237 1.00 25.43  ? 4119 HIS A N     1 
ATOM   18906 C  CA    . HIS A 1 4119 ? 192.705 191.505 215.128 1.00 24.68  ? 4119 HIS A CA    1 
ATOM   18907 C  C     . HIS A 1 4119 ? 193.894 190.720 214.580 1.00 27.60  ? 4119 HIS A C     1 
ATOM   18908 O  O     . HIS A 1 4119 ? 195.057 191.067 214.801 1.00 34.06  ? 4119 HIS A O     1 
ATOM   18909 C  CB    . HIS A 1 4119 ? 192.080 192.362 214.026 1.00 26.73  ? 4119 HIS A CB    1 
ATOM   18910 C  CG    . HIS A 1 4119 ? 191.251 191.589 213.048 1.00 28.35  ? 4119 HIS A CG    1 
ATOM   18911 N  ND1   . HIS A 1 4119 ? 191.571 191.496 211.711 1.00 29.73  ? 4119 HIS A ND1   1 
ATOM   18912 C  CD2   . HIS A 1 4119 ? 190.105 190.886 213.211 1.00 32.21  ? 4119 HIS A CD2   1 
ATOM   18913 C  CE1   . HIS A 1 4119 ? 190.663 190.761 211.093 1.00 30.21  ? 4119 HIS A CE1   1 
ATOM   18914 N  NE2   . HIS A 1 4119 ? 189.763 190.380 211.981 1.00 42.94  ? 4119 HIS A NE2   1 
ATOM   18915 N  N     . ALA A 1 4120 ? 193.587 189.640 213.860 1.00 24.50  ? 4120 ALA A N     1 
ATOM   18916 C  CA    . ALA A 1 4120 ? 194.639 188.767 213.351 1.00 22.02  ? 4120 ALA A CA    1 
ATOM   18917 C  C     . ALA A 1 4120 ? 195.538 189.495 212.361 1.00 30.30  ? 4120 ALA A C     1 
ATOM   18918 O  O     . ALA A 1 4120 ? 196.763 189.321 212.380 1.00 37.65  ? 4120 ALA A O     1 
ATOM   18919 C  CB    . ALA A 1 4120 ? 194.025 187.527 212.704 1.00 26.05  ? 4120 ALA A CB    1 
ATOM   18920 N  N     . CYS A 1 4121 ? 194.955 190.313 211.491 1.00 28.54  ? 4121 CYS A N     1 
ATOM   18921 C  CA    . CYS A 1 4121 ? 195.700 190.989 210.439 1.00 23.52  ? 4121 CYS A CA    1 
ATOM   18922 C  C     . CYS A 1 4121 ? 196.236 192.352 210.861 1.00 24.39  ? 4121 CYS A C     1 
ATOM   18923 O  O     . CYS A 1 4121 ? 196.881 193.021 210.048 1.00 25.45  ? 4121 CYS A O     1 
ATOM   18924 C  CB    . CYS A 1 4121 ? 194.824 191.146 209.193 1.00 26.55  ? 4121 CYS A CB    1 
ATOM   18925 S  SG    . CYS A 1 4121 ? 194.344 189.587 208.417 1.00 49.02  ? 4121 CYS A SG    1 
ATOM   18926 N  N     . PHE A 1 4122 ? 195.988 192.779 212.096 1.00 21.76  ? 4122 PHE A N     1 
ATOM   18927 C  CA    . PHE A 1 4122 ? 196.467 194.078 212.544 1.00 17.66  ? 4122 PHE A CA    1 
ATOM   18928 C  C     . PHE A 1 4122 ? 197.987 194.102 212.616 1.00 17.81  ? 4122 PHE A C     1 
ATOM   18929 O  O     . PHE A 1 4122 ? 198.619 193.154 213.091 1.00 23.63  ? 4122 PHE A O     1 
ATOM   18930 C  CB    . PHE A 1 4122 ? 195.886 194.423 213.913 1.00 15.34  ? 4122 PHE A CB    1 
ATOM   18931 C  CG    . PHE A 1 4122 ? 196.563 195.589 214.579 1.00 13.62  ? 4122 PHE A CG    1 
ATOM   18932 C  CD1   . PHE A 1 4122 ? 196.437 196.867 214.065 1.00 15.66  ? 4122 PHE A CD1   1 
ATOM   18933 C  CD2   . PHE A 1 4122 ? 197.341 195.402 215.708 1.00 11.68  ? 4122 PHE A CD2   1 
ATOM   18934 C  CE1   . PHE A 1 4122 ? 197.061 197.939 214.674 1.00 13.09  ? 4122 PHE A CE1   1 
ATOM   18935 C  CE2   . PHE A 1 4122 ? 197.969 196.468 216.320 1.00 8.66   ? 4122 PHE A CE2   1 
ATOM   18936 C  CZ    . PHE A 1 4122 ? 197.829 197.738 215.801 1.00 10.99  ? 4122 PHE A CZ    1 
ATOM   18937 N  N     . ARG A 1 4123 ? 198.572 195.199 212.142 1.00 13.71  ? 4123 ARG A N     1 
ATOM   18938 C  CA    . ARG A 1 4123 ? 200.007 195.416 212.237 1.00 10.12  ? 4123 ARG A CA    1 
ATOM   18939 C  C     . ARG A 1 4123 ? 200.274 196.853 212.655 1.00 9.48   ? 4123 ARG A C     1 
ATOM   18940 O  O     . ARG A 1 4123 ? 199.582 197.778 212.217 1.00 14.94  ? 4123 ARG A O     1 
ATOM   18941 C  CB    . ARG A 1 4123 ? 200.717 195.109 210.914 1.00 12.12  ? 4123 ARG A CB    1 
ATOM   18942 C  CG    . ARG A 1 4123 ? 200.694 193.643 210.530 1.00 13.88  ? 4123 ARG A CG    1 
ATOM   18943 C  CD    . ARG A 1 4123 ? 201.480 192.806 211.524 1.00 18.70  ? 4123 ARG A CD    1 
ATOM   18944 N  NE    . ARG A 1 4123 ? 201.455 191.389 211.186 1.00 20.96  ? 4123 ARG A NE    1 
ATOM   18945 C  CZ    . ARG A 1 4123 ? 200.454 190.568 211.472 1.00 18.36  ? 4123 ARG A CZ    1 
ATOM   18946 N  NH1   . ARG A 1 4123 ? 199.384 190.987 212.126 1.00 20.56  ? 4123 ARG A NH1   1 
ATOM   18947 N  NH2   . ARG A 1 4123 ? 200.531 189.296 211.096 1.00 20.21  ? 4123 ARG A NH2   1 
ATOM   18948 N  N     . LEU A 1 4124 ? 201.274 197.025 213.513 1.00 8.01   ? 4124 LEU A N     1 
ATOM   18949 C  CA    . LEU A 1 4124 ? 201.715 198.334 213.971 1.00 8.75   ? 4124 LEU A CA    1 
ATOM   18950 C  C     . LEU A 1 4124 ? 203.199 198.472 213.676 1.00 10.49  ? 4124 LEU A C     1 
ATOM   18951 O  O     . LEU A 1 4124 ? 204.013 197.712 214.207 1.00 11.61  ? 4124 LEU A O     1 
ATOM   18952 C  CB    . LEU A 1 4124 ? 201.446 198.523 215.465 1.00 7.14   ? 4124 LEU A CB    1 
ATOM   18953 C  CG    . LEU A 1 4124 ? 201.905 199.861 216.045 1.00 7.31   ? 4124 LEU A CG    1 
ATOM   18954 C  CD1   . LEU A 1 4124 ? 201.100 201.002 215.454 1.00 8.96   ? 4124 LEU A CD1   1 
ATOM   18955 C  CD2   . LEU A 1 4124 ? 201.805 199.855 217.558 1.00 7.64   ? 4124 LEU A CD2   1 
ATOM   18956 N  N     . PHE A 1 4125 ? 203.546 199.437 212.834 1.00 12.90  ? 4125 PHE A N     1 
ATOM   18957 C  CA    . PHE A 1 4125 ? 204.923 199.732 212.479 1.00 8.70   ? 4125 PHE A CA    1 
ATOM   18958 C  C     . PHE A 1 4125 ? 205.341 201.036 213.141 1.00 9.09   ? 4125 PHE A C     1 
ATOM   18959 O  O     . PHE A 1 4125 ? 204.579 202.007 213.152 1.00 11.56  ? 4125 PHE A O     1 
ATOM   18960 C  CB    . PHE A 1 4125 ? 205.094 199.837 210.960 1.00 8.17   ? 4125 PHE A CB    1 
ATOM   18961 C  CG    . PHE A 1 4125 ? 204.626 198.621 210.207 1.00 8.53   ? 4125 PHE A CG    1 
ATOM   18962 C  CD1   . PHE A 1 4125 ? 203.287 198.447 209.902 1.00 11.13  ? 4125 PHE A CD1   1 
ATOM   18963 C  CD2   . PHE A 1 4125 ? 205.530 197.657 209.795 1.00 9.64   ? 4125 PHE A CD2   1 
ATOM   18964 C  CE1   . PHE A 1 4125 ? 202.859 197.332 209.212 1.00 9.16   ? 4125 PHE A CE1   1 
ATOM   18965 C  CE2   . PHE A 1 4125 ? 205.106 196.545 209.097 1.00 10.21  ? 4125 PHE A CE2   1 
ATOM   18966 C  CZ    . PHE A 1 4125 ? 203.769 196.382 208.809 1.00 10.42  ? 4125 PHE A CZ    1 
ATOM   18967 N  N     . LEU A 1 4126 ? 206.541 201.047 213.714 1.00 9.39   ? 4126 LEU A N     1 
ATOM   18968 C  CA    . LEU A 1 4126 ? 207.092 202.232 214.367 1.00 9.17   ? 4126 LEU A CA    1 
ATOM   18969 C  C     . LEU A 1 4126 ? 208.448 202.512 213.732 1.00 11.00  ? 4126 LEU A C     1 
ATOM   18970 O  O     . LEU A 1 4126 ? 209.420 201.803 214.006 1.00 11.03  ? 4126 LEU A O     1 
ATOM   18971 C  CB    . LEU A 1 4126 ? 207.216 202.030 215.876 1.00 9.22   ? 4126 LEU A CB    1 
ATOM   18972 C  CG    . LEU A 1 4126 ? 205.979 201.535 216.625 1.00 6.39   ? 4126 LEU A CG    1 
ATOM   18973 C  CD1   . LEU A 1 4126 ? 206.277 201.360 218.102 1.00 6.79   ? 4126 LEU A CD1   1 
ATOM   18974 C  CD2   . LEU A 1 4126 ? 204.817 202.482 216.425 1.00 5.83   ? 4126 LEU A CD2   1 
ATOM   18975 N  N     . THR A 1 4127 ? 208.517 203.526 212.874 1.00 14.54  ? 4127 THR A N     1 
ATOM   18976 C  CA    . THR A 1 4127 ? 209.779 203.897 212.247 1.00 12.01  ? 4127 THR A CA    1 
ATOM   18977 C  C     . THR A 1 4127 ? 210.493 204.909 213.131 1.00 10.71  ? 4127 THR A C     1 
ATOM   18978 O  O     . THR A 1 4127 ? 209.877 205.867 213.608 1.00 12.00  ? 4127 THR A O     1 
ATOM   18979 C  CB    . THR A 1 4127 ? 209.560 204.470 210.847 1.00 10.74  ? 4127 THR A CB    1 
ATOM   18980 O  OG1   . THR A 1 4127 ? 208.764 205.656 210.932 1.00 13.74  ? 4127 THR A OG1   1 
ATOM   18981 C  CG2   . THR A 1 4127 ? 208.853 203.459 209.962 1.00 15.69  ? 4127 THR A CG2   1 
ATOM   18982 N  N     . MET A 1 4128 ? 211.787 204.692 213.355 1.00 10.59  ? 4128 MET A N     1 
ATOM   18983 C  CA    . MET A 1 4128 ? 212.527 205.519 214.294 1.00 9.38   ? 4128 MET A CA    1 
ATOM   18984 C  C     . MET A 1 4128 ? 213.987 205.576 213.878 1.00 14.48  ? 4128 MET A C     1 
ATOM   18985 O  O     . MET A 1 4128 ? 214.455 204.781 213.059 1.00 20.87  ? 4128 MET A O     1 
ATOM   18986 C  CB    . MET A 1 4128 ? 212.413 204.979 215.723 1.00 13.04  ? 4128 MET A CB    1 
ATOM   18987 C  CG    . MET A 1 4128 ? 213.052 203.610 215.902 1.00 17.36  ? 4128 MET A CG    1 
ATOM   18988 S  SD    . MET A 1 4128 ? 212.838 202.913 217.548 1.00 42.03  ? 4128 MET A SD    1 
ATOM   18989 C  CE    . MET A 1 4128 ? 211.108 202.459 217.501 1.00 16.02  ? 4128 MET A CE    1 
ATOM   18990 N  N     . GLU A 1 4129 ? 214.701 206.534 214.453 1.00 14.48  ? 4129 GLU A N     1 
ATOM   18991 C  CA    . GLU A 1 4129 ? 216.144 206.604 214.315 1.00 13.53  ? 4129 GLU A CA    1 
ATOM   18992 C  C     . GLU A 1 4129 ? 216.808 205.861 215.469 1.00 18.82  ? 4129 GLU A C     1 
ATOM   18993 O  O     . GLU A 1 4129 ? 216.229 205.686 216.543 1.00 25.55  ? 4129 GLU A O     1 
ATOM   18994 C  CB    . GLU A 1 4129 ? 216.615 208.057 214.280 1.00 13.80  ? 4129 GLU A CB    1 
ATOM   18995 C  CG    . GLU A 1 4129 ? 216.799 208.608 212.880 1.00 22.64  ? 4129 GLU A CG    1 
ATOM   18996 C  CD    . GLU A 1 4129 ? 217.395 210.000 212.876 1.00 34.04  ? 4129 GLU A CD    1 
ATOM   18997 O  OE1   . GLU A 1 4129 ? 217.704 210.517 213.968 1.00 26.52  ? 4129 GLU A OE1   1 
ATOM   18998 O  OE2   . GLU A 1 4129 ? 217.555 210.574 211.779 1.00 34.40  ? 4129 GLU A OE2   1 
ATOM   18999 N  N     . ILE A 1 4130 ? 218.040 205.421 215.234 1.00 17.19  ? 4130 ILE A N     1 
ATOM   19000 C  CA    . ILE A 1 4130 ? 218.780 204.677 216.245 1.00 14.75  ? 4130 ILE A CA    1 
ATOM   19001 C  C     . ILE A 1 4130 ? 219.363 205.657 217.252 1.00 15.86  ? 4130 ILE A C     1 
ATOM   19002 O  O     . ILE A 1 4130 ? 220.462 206.188 217.058 1.00 20.26  ? 4130 ILE A O     1 
ATOM   19003 C  CB    . ILE A 1 4130 ? 219.882 203.811 215.610 1.00 12.65  ? 4130 ILE A CB    1 
ATOM   19004 C  CG1   . ILE A 1 4130 ? 219.298 202.941 214.499 1.00 13.14  ? 4130 ILE A CG1   1 
ATOM   19005 C  CG2   . ILE A 1 4130 ? 220.550 202.945 216.664 1.00 13.00  ? 4130 ILE A CG2   1 
ATOM   19006 C  CD1   . ILE A 1 4130 ? 220.295 201.990 213.883 1.00 12.69  ? 4130 ILE A CD1   1 
ATOM   19007 N  N     . ASN A 1 4131 ? 218.625 205.912 218.327 1.00 14.57  ? 4131 ASN A N     1 
ATOM   19008 C  CA    . ASN A 1 4131 ? 219.077 206.772 219.406 1.00 16.30  ? 4131 ASN A CA    1 
ATOM   19009 C  C     . ASN A 1 4131 ? 218.714 206.155 220.750 1.00 16.69  ? 4131 ASN A C     1 
ATOM   19010 O  O     . ASN A 1 4131 ? 217.779 205.350 220.835 1.00 15.75  ? 4131 ASN A O     1 
ATOM   19011 C  CB    . ASN A 1 4131 ? 218.524 208.207 219.246 1.00 17.22  ? 4131 ASN A CB    1 
ATOM   19012 C  CG    . ASN A 1 4131 ? 217.087 208.389 219.739 1.00 21.22  ? 4131 ASN A CG    1 
ATOM   19013 O  OD1   . ASN A 1 4131 ? 216.409 207.458 220.162 1.00 26.18  ? 4131 ASN A OD1   1 
ATOM   19014 N  ND2   . ASN A 1 4131 ? 216.619 209.626 219.666 1.00 23.29  ? 4131 ASN A ND2   1 
ATOM   19015 N  N     . PRO A 1 4132 ? 219.469 206.473 221.807 1.00 14.14  ? 4132 PRO A N     1 
ATOM   19016 C  CA    . PRO A 1 4132 ? 219.241 205.808 223.101 1.00 14.34  ? 4132 PRO A CA    1 
ATOM   19017 C  C     . PRO A 1 4132 ? 217.975 206.244 223.821 1.00 18.08  ? 4132 PRO A C     1 
ATOM   19018 O  O     . PRO A 1 4132 ? 217.619 205.615 224.825 1.00 22.92  ? 4132 PRO A O     1 
ATOM   19019 C  CB    . PRO A 1 4132 ? 220.489 206.177 223.911 1.00 14.28  ? 4132 PRO A CB    1 
ATOM   19020 C  CG    . PRO A 1 4132 ? 221.007 207.413 223.267 1.00 12.86  ? 4132 PRO A CG    1 
ATOM   19021 C  CD    . PRO A 1 4132 ? 220.702 207.275 221.812 1.00 9.63   ? 4132 PRO A CD    1 
ATOM   19022 N  N     . LYS A 1 4133 ? 217.286 207.289 223.356 1.00 17.79  ? 4133 LYS A N     1 
ATOM   19023 C  CA    . LYS A 1 4133 ? 216.083 207.740 224.048 1.00 18.56  ? 4133 LYS A CA    1 
ATOM   19024 C  C     . LYS A 1 4133 ? 214.924 206.762 223.910 1.00 21.19  ? 4133 LYS A C     1 
ATOM   19025 O  O     . LYS A 1 4133 ? 213.977 206.834 224.700 1.00 22.85  ? 4133 LYS A O     1 
ATOM   19026 C  CB    . LYS A 1 4133 ? 215.658 209.118 223.539 1.00 24.68  ? 4133 LYS A CB    1 
ATOM   19027 C  CG    . LYS A 1 4133 ? 216.628 210.236 223.882 1.00 31.89  ? 4133 LYS A CG    1 
ATOM   19028 C  CD    . LYS A 1 4133 ? 216.065 211.595 223.494 1.00 25.30  ? 4133 LYS A CD    1 
ATOM   19029 C  CE    . LYS A 1 4133 ? 216.096 211.805 221.991 1.00 36.56  ? 4133 LYS A CE    1 
ATOM   19030 N  NZ    . LYS A 1 4133 ? 215.652 213.172 221.607 1.00 42.82  ? 4133 LYS A NZ    1 
ATOM   19031 N  N     . VAL A 1 4134 ? 214.968 205.862 222.933 1.00 18.23  ? 4134 VAL A N     1 
ATOM   19032 C  CA    . VAL A 1 4134 ? 213.877 204.893 222.768 1.00 15.28  ? 4134 VAL A CA    1 
ATOM   19033 C  C     . VAL A 1 4134 ? 213.845 203.967 223.979 1.00 14.97  ? 4134 VAL A C     1 
ATOM   19034 O  O     . VAL A 1 4134 ? 214.900 203.438 224.381 1.00 14.84  ? 4134 VAL A O     1 
ATOM   19035 C  CB    . VAL A 1 4134 ? 214.054 204.095 221.466 1.00 15.11  ? 4134 VAL A CB    1 
ATOM   19036 C  CG1   . VAL A 1 4134 ? 212.868 203.173 221.240 1.00 13.17  ? 4134 VAL A CG1   1 
ATOM   19037 C  CG2   . VAL A 1 4134 ? 214.227 205.037 220.290 1.00 17.85  ? 4134 VAL A CG2   1 
ATOM   19038 N  N     . PRO A 1 4135 ? 212.686 203.749 224.602 1.00 15.44  ? 4135 PRO A N     1 
ATOM   19039 C  CA    . PRO A 1 4135 ? 212.640 202.901 225.799 1.00 14.96  ? 4135 PRO A CA    1 
ATOM   19040 C  C     . PRO A 1 4135 ? 213.099 201.479 225.509 1.00 14.88  ? 4135 PRO A C     1 
ATOM   19041 O  O     . PRO A 1 4135 ? 212.818 200.918 224.448 1.00 15.98  ? 4135 PRO A O     1 
ATOM   19042 C  CB    . PRO A 1 4135 ? 211.162 202.941 226.203 1.00 14.82  ? 4135 PRO A CB    1 
ATOM   19043 C  CG    . PRO A 1 4135 ? 210.628 204.184 225.583 1.00 15.26  ? 4135 PRO A CG    1 
ATOM   19044 C  CD    . PRO A 1 4135 ? 211.382 204.361 224.304 1.00 13.18  ? 4135 PRO A CD    1 
ATOM   19045 N  N     . VAL A 1 4136 ? 213.810 200.898 226.476 1.00 15.05  ? 4136 VAL A N     1 
ATOM   19046 C  CA    . VAL A 1 4136 ? 214.304 199.532 226.329 1.00 13.22  ? 4136 VAL A CA    1 
ATOM   19047 C  C     . VAL A 1 4136 ? 213.143 198.545 226.320 1.00 12.01  ? 4136 VAL A C     1 
ATOM   19048 O  O     . VAL A 1 4136 ? 213.159 197.552 225.581 1.00 16.12  ? 4136 VAL A O     1 
ATOM   19049 C  CB    . VAL A 1 4136 ? 215.318 199.216 227.443 1.00 9.29   ? 4136 VAL A CB    1 
ATOM   19050 C  CG1   . VAL A 1 4136 ? 215.537 197.718 227.570 1.00 13.85  ? 4136 VAL A CG1   1 
ATOM   19051 C  CG2   . VAL A 1 4136 ? 216.634 199.923 227.174 1.00 8.10   ? 4136 VAL A CG2   1 
ATOM   19052 N  N     . ASN A 1 4137 ? 212.117 198.805 227.131 1.00 13.04  ? 4137 ASN A N     1 
ATOM   19053 C  CA    . ASN A 1 4137 ? 210.982 197.893 227.212 1.00 13.75  ? 4137 ASN A CA    1 
ATOM   19054 C  C     . ASN A 1 4137 ? 210.236 197.836 225.884 1.00 13.90  ? 4137 ASN A C     1 
ATOM   19055 O  O     . ASN A 1 4137 ? 209.783 196.766 225.461 1.00 13.58  ? 4137 ASN A O     1 
ATOM   19056 C  CB    . ASN A 1 4137 ? 210.059 198.326 228.354 1.00 21.84  ? 4137 ASN A CB    1 
ATOM   19057 C  CG    . ASN A 1 4137 ? 208.966 197.311 228.652 1.00 36.95  ? 4137 ASN A CG    1 
ATOM   19058 O  OD1   . ASN A 1 4137 ? 208.859 196.275 227.998 1.00 37.61  ? 4137 ASN A OD1   1 
ATOM   19059 N  ND2   . ASN A 1 4137 ? 208.154 197.606 229.659 1.00 32.56  ? 4137 ASN A ND2   1 
ATOM   19060 N  N     . LEU A 1 4138 ? 210.106 198.979 225.204 1.00 13.36  ? 4138 LEU A N     1 
ATOM   19061 C  CA    . LEU A 1 4138 ? 209.503 198.987 223.874 1.00 12.01  ? 4138 LEU A CA    1 
ATOM   19062 C  C     . LEU A 1 4138 ? 210.338 198.186 222.883 1.00 10.85  ? 4138 LEU A C     1 
ATOM   19063 O  O     . LEU A 1 4138 ? 209.792 197.473 222.033 1.00 11.36  ? 4138 LEU A O     1 
ATOM   19064 C  CB    . LEU A 1 4138 ? 209.331 200.421 223.377 1.00 11.91  ? 4138 LEU A CB    1 
ATOM   19065 C  CG    . LEU A 1 4138 ? 208.685 200.540 221.995 1.00 12.71  ? 4138 LEU A CG    1 
ATOM   19066 C  CD1   . LEU A 1 4138 ? 207.170 200.477 222.092 1.00 15.48  ? 4138 LEU A CD1   1 
ATOM   19067 C  CD2   . LEU A 1 4138 ? 209.137 201.798 221.283 1.00 11.29  ? 4138 LEU A CD2   1 
ATOM   19068 N  N     . LEU A 1 4139 ? 211.665 198.304 222.965 1.00 10.69  ? 4139 LEU A N     1 
ATOM   19069 C  CA    . LEU A 1 4139 ? 212.533 197.522 222.090 1.00 9.12   ? 4139 LEU A CA    1 
ATOM   19070 C  C     . LEU A 1 4139 ? 212.354 196.030 222.333 1.00 8.54   ? 4139 LEU A C     1 
ATOM   19071 O  O     . LEU A 1 4139 ? 212.318 195.237 221.385 1.00 10.52  ? 4139 LEU A O     1 
ATOM   19072 C  CB    . LEU A 1 4139 ? 213.993 197.923 222.300 1.00 12.49  ? 4139 LEU A CB    1 
ATOM   19073 C  CG    . LEU A 1 4139 ? 214.415 199.326 221.864 1.00 11.06  ? 4139 LEU A CG    1 
ATOM   19074 C  CD1   . LEU A 1 4139 ? 215.852 199.590 222.272 1.00 8.11   ? 4139 LEU A CD1   1 
ATOM   19075 C  CD2   . LEU A 1 4139 ? 214.246 199.496 220.366 1.00 11.90  ? 4139 LEU A CD2   1 
ATOM   19076 N  N     . ARG A 1 4140 ? 212.242 195.629 223.601 1.00 8.61   ? 4140 ARG A N     1 
ATOM   19077 C  CA    . ARG A 1 4140 ? 212.031 194.221 223.915 1.00 8.97   ? 4140 ARG A CA    1 
ATOM   19078 C  C     . ARG A 1 4140 ? 210.650 193.749 223.479 1.00 8.81   ? 4140 ARG A C     1 
ATOM   19079 O  O     . ARG A 1 4140 ? 210.480 192.574 223.132 1.00 8.61   ? 4140 ARG A O     1 
ATOM   19080 C  CB    . ARG A 1 4140 ? 212.219 193.984 225.412 1.00 9.76   ? 4140 ARG A CB    1 
ATOM   19081 C  CG    . ARG A 1 4140 ? 213.651 194.124 225.892 1.00 11.44  ? 4140 ARG A CG    1 
ATOM   19082 C  CD    . ARG A 1 4140 ? 213.752 193.875 227.387 1.00 12.45  ? 4140 ARG A CD    1 
ATOM   19083 N  NE    . ARG A 1 4140 ? 214.394 192.599 227.683 1.00 14.68  ? 4140 ARG A NE    1 
ATOM   19084 C  CZ    . ARG A 1 4140 ? 213.785 191.572 228.259 1.00 19.04  ? 4140 ARG A CZ    1 
ATOM   19085 N  NH1   . ARG A 1 4140 ? 212.512 191.631 228.612 1.00 20.80  ? 4140 ARG A NH1   1 
ATOM   19086 N  NH2   . ARG A 1 4140 ? 214.471 190.454 228.481 1.00 21.02  ? 4140 ARG A NH2   1 
ATOM   19087 N  N     . ALA A 1 4141 ? 209.659 194.642 223.488 1.00 8.79   ? 4141 ALA A N     1 
ATOM   19088 C  CA    . ALA A 1 4141 ? 208.288 194.245 223.188 1.00 7.86   ? 4141 ALA A CA    1 
ATOM   19089 C  C     . ALA A 1 4141 ? 208.058 193.972 221.709 1.00 11.31  ? 4141 ALA A C     1 
ATOM   19090 O  O     . ALA A 1 4141 ? 207.108 193.261 221.367 1.00 17.91  ? 4141 ALA A O     1 
ATOM   19091 C  CB    . ALA A 1 4141 ? 207.318 195.323 223.669 1.00 11.98  ? 4141 ALA A CB    1 
ATOM   19092 N  N     . GLY A 1 4142 ? 208.900 194.512 220.823 1.00 11.19  ? 4142 GLY A N     1 
ATOM   19093 C  CA    . GLY A 1 4142 ? 208.696 194.372 219.400 1.00 8.44   ? 4142 GLY A CA    1 
ATOM   19094 C  C     . GLY A 1 4142 ? 209.932 193.821 218.712 1.00 7.82   ? 4142 GLY A C     1 
ATOM   19095 O  O     . GLY A 1 4142 ? 211.010 193.726 219.301 1.00 10.58  ? 4142 GLY A O     1 
ATOM   19096 N  N     . ARG A 1 4143 ? 209.751 193.455 217.446 1.00 9.18   ? 4143 ARG A N     1 
ATOM   19097 C  CA    . ARG A 1 4143 ? 210.837 192.942 216.624 1.00 8.86   ? 4143 ARG A CA    1 
ATOM   19098 C  C     . ARG A 1 4143 ? 211.511 194.091 215.886 1.00 8.42   ? 4143 ARG A C     1 
ATOM   19099 O  O     . ARG A 1 4143 ? 210.837 194.918 215.261 1.00 8.32   ? 4143 ARG A O     1 
ATOM   19100 C  CB    . ARG A 1 4143 ? 210.329 191.896 215.632 1.00 7.33   ? 4143 ARG A CB    1 
ATOM   19101 C  CG    . ARG A 1 4143 ? 211.437 191.268 214.805 1.00 13.79  ? 4143 ARG A CG    1 
ATOM   19102 C  CD    . ARG A 1 4143 ? 211.052 189.902 214.276 1.00 17.31  ? 4143 ARG A CD    1 
ATOM   19103 N  NE    . ARG A 1 4143 ? 212.043 189.396 213.334 1.00 17.37  ? 4143 ARG A NE    1 
ATOM   19104 C  CZ    . ARG A 1 4143 ? 211.877 188.324 212.573 1.00 27.31  ? 4143 ARG A CZ    1 
ATOM   19105 N  NH1   . ARG A 1 4143 ? 210.771 187.602 212.628 1.00 27.62  ? 4143 ARG A NH1   1 
ATOM   19106 N  NH2   . ARG A 1 4143 ? 212.845 187.969 211.733 1.00 20.62  ? 4143 ARG A NH2   1 
ATOM   19107 N  N     . ILE A 1 4144 ? 212.839 194.126 215.949 1.00 6.96   ? 4144 ILE A N     1 
ATOM   19108 C  CA    . ILE A 1 4144 ? 213.640 195.242 215.460 1.00 6.35   ? 4144 ILE A CA    1 
ATOM   19109 C  C     . ILE A 1 4144 ? 214.223 194.897 214.099 1.00 8.06   ? 4144 ILE A C     1 
ATOM   19110 O  O     . ILE A 1 4144 ? 214.728 193.788 213.886 1.00 8.51   ? 4144 ILE A O     1 
ATOM   19111 C  CB    . ILE A 1 4144 ? 214.755 195.597 216.461 1.00 6.42   ? 4144 ILE A CB    1 
ATOM   19112 C  CG1   . ILE A 1 4144 ? 214.159 195.882 217.840 1.00 8.35   ? 4144 ILE A CG1   1 
ATOM   19113 C  CG2   . ILE A 1 4144 ? 215.570 196.780 215.968 1.00 7.32   ? 4144 ILE A CG2   1 
ATOM   19114 C  CD1   . ILE A 1 4144 ? 215.183 195.930 218.944 1.00 9.48   ? 4144 ILE A CD1   1 
ATOM   19115 N  N     . PHE A 1 4145 ? 214.141 195.847 213.170 1.00 9.60   ? 4145 PHE A N     1 
ATOM   19116 C  CA    . PHE A 1 4145 ? 214.776 195.752 211.864 1.00 6.29   ? 4145 PHE A CA    1 
ATOM   19117 C  C     . PHE A 1 4145 ? 215.621 196.998 211.650 1.00 9.44   ? 4145 PHE A C     1 
ATOM   19118 O  O     . PHE A 1 4145 ? 215.113 198.120 211.751 1.00 11.28  ? 4145 PHE A O     1 
ATOM   19119 C  CB    . PHE A 1 4145 ? 213.739 195.616 210.747 1.00 7.66   ? 4145 PHE A CB    1 
ATOM   19120 C  CG    . PHE A 1 4145 ? 212.895 194.384 210.858 1.00 12.34  ? 4145 PHE A CG    1 
ATOM   19121 C  CD1   . PHE A 1 4145 ? 213.347 193.174 210.368 1.00 11.31  ? 4145 PHE A CD1   1 
ATOM   19122 C  CD2   . PHE A 1 4145 ? 211.655 194.432 211.470 1.00 11.87  ? 4145 PHE A CD2   1 
ATOM   19123 C  CE1   . PHE A 1 4145 ? 212.576 192.039 210.474 1.00 11.91  ? 4145 PHE A CE1   1 
ATOM   19124 C  CE2   . PHE A 1 4145 ? 210.882 193.299 211.580 1.00 11.31  ? 4145 PHE A CE2   1 
ATOM   19125 C  CZ    . PHE A 1 4145 ? 211.341 192.103 211.082 1.00 15.51  ? 4145 PHE A CZ    1 
ATOM   19126 N  N     . VAL A 1 4146 ? 216.900 196.799 211.352 1.00 7.21   ? 4146 VAL A N     1 
ATOM   19127 C  CA    . VAL A 1 4146 ? 217.845 197.890 211.160 1.00 6.93   ? 4146 VAL A CA    1 
ATOM   19128 C  C     . VAL A 1 4146 ? 217.977 198.163 209.669 1.00 7.66   ? 4146 VAL A C     1 
ATOM   19129 O  O     . VAL A 1 4146 ? 218.228 197.244 208.879 1.00 16.70  ? 4146 VAL A O     1 
ATOM   19130 C  CB    . VAL A 1 4146 ? 219.211 197.560 211.785 1.00 6.88   ? 4146 VAL A CB    1 
ATOM   19131 C  CG1   . VAL A 1 4146 ? 220.287 198.478 211.235 1.00 8.20   ? 4146 VAL A CG1   1 
ATOM   19132 C  CG2   . VAL A 1 4146 ? 219.135 197.678 213.295 1.00 6.46   ? 4146 VAL A CG2   1 
ATOM   19133 N  N     . PHE A 1 4147 ? 217.798 199.421 209.282 1.00 7.98   ? 4147 PHE A N     1 
ATOM   19134 C  CA    . PHE A 1 4147 ? 217.927 199.842 207.893 1.00 9.93   ? 4147 PHE A CA    1 
ATOM   19135 C  C     . PHE A 1 4147 ? 219.157 200.728 207.758 1.00 8.81   ? 4147 PHE A C     1 
ATOM   19136 O  O     . PHE A 1 4147 ? 219.269 201.753 208.438 1.00 9.90   ? 4147 PHE A O     1 
ATOM   19137 C  CB    . PHE A 1 4147 ? 216.669 200.569 207.420 1.00 11.18  ? 4147 PHE A CB    1 
ATOM   19138 C  CG    . PHE A 1 4147 ? 215.479 199.668 207.259 1.00 15.02  ? 4147 PHE A CG    1 
ATOM   19139 C  CD1   . PHE A 1 4147 ? 214.649 199.397 208.333 1.00 14.08  ? 4147 PHE A CD1   1 
ATOM   19140 C  CD2   . PHE A 1 4147 ? 215.205 199.072 206.043 1.00 21.16  ? 4147 PHE A CD2   1 
ATOM   19141 C  CE1   . PHE A 1 4147 ? 213.561 198.564 208.191 1.00 13.88  ? 4147 PHE A CE1   1 
ATOM   19142 C  CE2   . PHE A 1 4147 ? 214.118 198.235 205.896 1.00 25.86  ? 4147 PHE A CE2   1 
ATOM   19143 C  CZ    . PHE A 1 4147 ? 213.294 197.982 206.971 1.00 20.01  ? 4147 PHE A CZ    1 
ATOM   19144 N  N     . GLU A 1 4148 ? 220.069 200.332 206.880 1.00 9.20   ? 4148 GLU A N     1 
ATOM   19145 C  CA    . GLU A 1 4148 ? 221.353 201.000 206.724 1.00 7.79   ? 4148 GLU A CA    1 
ATOM   19146 C  C     . GLU A 1 4148 ? 221.816 200.788 205.294 1.00 12.50  ? 4148 GLU A C     1 
ATOM   19147 O  O     . GLU A 1 4148 ? 221.182 200.048 204.531 1.00 15.97  ? 4148 GLU A O     1 
ATOM   19148 C  CB    . GLU A 1 4148 ? 222.383 200.462 207.726 1.00 9.85   ? 4148 GLU A CB    1 
ATOM   19149 C  CG    . GLU A 1 4148 ? 222.439 198.951 207.826 1.00 11.41  ? 4148 GLU A CG    1 
ATOM   19150 C  CD    . GLU A 1 4148 ? 223.481 198.479 208.818 1.00 14.18  ? 4148 GLU A CD    1 
ATOM   19151 O  OE1   . GLU A 1 4148 ? 224.228 199.328 209.345 1.00 10.18  ? 4148 GLU A OE1   1 
ATOM   19152 O  OE2   . GLU A 1 4148 ? 223.551 197.260 209.072 1.00 24.58  ? 4148 GLU A OE2   1 
ATOM   19153 N  N     . PRO A 1 4149 ? 222.905 201.439 204.886 1.00 14.99  ? 4149 PRO A N     1 
ATOM   19154 C  CA    . PRO A 1 4149 ? 223.459 201.184 203.550 1.00 11.77  ? 4149 PRO A CA    1 
ATOM   19155 C  C     . PRO A 1 4149 ? 223.796 199.716 203.366 1.00 10.97  ? 4149 PRO A C     1 
ATOM   19156 O  O     . PRO A 1 4149 ? 224.254 199.051 204.308 1.00 17.01  ? 4149 PRO A O     1 
ATOM   19157 C  CB    . PRO A 1 4149 ? 224.723 202.053 203.520 1.00 12.79  ? 4149 PRO A CB    1 
ATOM   19158 C  CG    . PRO A 1 4149 ? 224.415 203.172 204.427 1.00 13.59  ? 4149 PRO A CG    1 
ATOM   19159 C  CD    . PRO A 1 4149 ? 223.530 202.622 205.510 1.00 12.93  ? 4149 PRO A CD    1 
ATOM   19160 N  N     . PRO A 1 4150 ? 223.571 199.173 202.171 1.00 11.00  ? 4150 PRO A N     1 
ATOM   19161 C  CA    . PRO A 1 4150 ? 223.878 197.767 201.941 1.00 12.62  ? 4150 PRO A CA    1 
ATOM   19162 C  C     . PRO A 1 4150 ? 225.360 197.507 202.107 1.00 14.28  ? 4150 PRO A C     1 
ATOM   19163 O  O     . PRO A 1 4150 ? 226.199 198.394 201.858 1.00 17.36  ? 4150 PRO A O     1 
ATOM   19164 C  CB    . PRO A 1 4150 ? 223.422 197.539 200.493 1.00 9.75   ? 4150 PRO A CB    1 
ATOM   19165 C  CG    . PRO A 1 4150 ? 222.397 198.592 200.255 1.00 10.80  ? 4150 PRO A CG    1 
ATOM   19166 C  CD    . PRO A 1 4150 ? 222.880 199.783 201.023 1.00 14.80  ? 4150 PRO A CD    1 
ATOM   19167 N  N     . PRO A 1 4151 ? 225.734 196.299 202.537 1.00 12.11  ? 4151 PRO A N     1 
ATOM   19168 C  CA    . PRO A 1 4151 ? 227.145 196.037 202.868 1.00 13.69  ? 4151 PRO A CA    1 
ATOM   19169 C  C     . PRO A 1 4151 ? 228.112 196.233 201.714 1.00 17.68  ? 4151 PRO A C     1 
ATOM   19170 O  O     . PRO A 1 4151 ? 229.277 196.574 201.956 1.00 23.68  ? 4151 PRO A O     1 
ATOM   19171 C  CB    . PRO A 1 4151 ? 227.124 194.576 203.341 1.00 9.25   ? 4151 PRO A CB    1 
ATOM   19172 C  CG    . PRO A 1 4151 ? 225.854 194.007 202.806 1.00 12.79  ? 4151 PRO A CG    1 
ATOM   19173 C  CD    . PRO A 1 4151 ? 224.879 195.134 202.807 1.00 10.78  ? 4151 PRO A CD    1 
ATOM   19174 N  N     . GLY A 1 4152 ? 227.683 196.027 200.471 1.00 12.77  ? 4152 GLY A N     1 
ATOM   19175 C  CA    . GLY A 1 4152 ? 228.598 196.125 199.355 1.00 11.04  ? 4152 GLY A CA    1 
ATOM   19176 C  C     . GLY A 1 4152 ? 227.897 196.505 198.068 1.00 8.87   ? 4152 GLY A C     1 
ATOM   19177 O  O     . GLY A 1 4152 ? 226.696 196.779 198.044 1.00 12.65  ? 4152 GLY A O     1 
ATOM   19178 N  N     . VAL A 1 4153 ? 228.679 196.521 196.986 1.00 7.69   ? 4153 VAL A N     1 
ATOM   19179 C  CA    . VAL A 1 4153 ? 228.147 196.883 195.675 1.00 7.91   ? 4153 VAL A CA    1 
ATOM   19180 C  C     . VAL A 1 4153 ? 227.112 195.865 195.217 1.00 7.16   ? 4153 VAL A C     1 
ATOM   19181 O  O     . VAL A 1 4153 ? 226.045 196.229 194.705 1.00 7.21   ? 4153 VAL A O     1 
ATOM   19182 C  CB    . VAL A 1 4153 ? 229.296 197.021 194.658 1.00 5.56   ? 4153 VAL A CB    1 
ATOM   19183 C  CG1   . VAL A 1 4153 ? 228.758 197.060 193.238 1.00 4.80   ? 4153 VAL A CG1   1 
ATOM   19184 C  CG2   . VAL A 1 4153 ? 230.117 198.262 194.955 1.00 7.52   ? 4153 VAL A CG2   1 
ATOM   19185 N  N     . LYS A 1 4154 ? 227.409 194.576 195.391 1.00 6.50   ? 4154 LYS A N     1 
ATOM   19186 C  CA    . LYS A 1 4154 ? 226.485 193.532 194.959 1.00 5.42   ? 4154 LYS A CA    1 
ATOM   19187 C  C     . LYS A 1 4154 ? 225.169 193.616 195.720 1.00 5.77   ? 4154 LYS A C     1 
ATOM   19188 O  O     . LYS A 1 4154 ? 224.086 193.554 195.123 1.00 6.11   ? 4154 LYS A O     1 
ATOM   19189 C  CB    . LYS A 1 4154 ? 227.133 192.160 195.146 1.00 5.28   ? 4154 LYS A CB    1 
ATOM   19190 C  CG    . LYS A 1 4154 ? 226.264 190.990 194.726 1.00 5.95   ? 4154 LYS A CG    1 
ATOM   19191 C  CD    . LYS A 1 4154 ? 226.936 189.668 195.051 1.00 8.42   ? 4154 LYS A CD    1 
ATOM   19192 C  CE    . LYS A 1 4154 ? 225.988 188.503 194.850 1.00 13.59  ? 4154 LYS A CE    1 
ATOM   19193 N  NZ    . LYS A 1 4154 ? 226.597 187.214 195.276 1.00 16.53  ? 4154 LYS A NZ    1 
ATOM   19194 N  N     . ALA A 1 4155 ? 225.244 193.767 197.043 1.00 6.42   ? 4155 ALA A N     1 
ATOM   19195 C  CA    . ALA A 1 4155 ? 224.034 193.888 197.848 1.00 6.12   ? 4155 ALA A CA    1 
ATOM   19196 C  C     . ALA A 1 4155 ? 223.254 195.144 197.487 1.00 5.93   ? 4155 ALA A C     1 
ATOM   19197 O  O     . ALA A 1 4155 ? 222.020 195.120 197.421 1.00 9.37   ? 4155 ALA A O     1 
ATOM   19198 C  CB    . ALA A 1 4155 ? 224.389 193.884 199.334 1.00 6.43   ? 4155 ALA A CB    1 
ATOM   19199 N  N     . ASN A 1 4156 ? 223.960 196.254 197.254 1.00 6.13   ? 4156 ASN A N     1 
ATOM   19200 C  CA    . ASN A 1 4156 ? 223.288 197.496 196.887 1.00 5.40   ? 4156 ASN A CA    1 
ATOM   19201 C  C     . ASN A 1 4156 ? 222.543 197.345 195.569 1.00 5.99   ? 4156 ASN A C     1 
ATOM   19202 O  O     . ASN A 1 4156 ? 221.389 197.773 195.446 1.00 6.13   ? 4156 ASN A O     1 
ATOM   19203 C  CB    . ASN A 1 4156 ? 224.309 198.634 196.817 1.00 5.54   ? 4156 ASN A CB    1 
ATOM   19204 C  CG    . ASN A 1 4156 ? 223.672 199.988 196.553 1.00 6.88   ? 4156 ASN A CG    1 
ATOM   19205 O  OD1   . ASN A 1 4156 ? 223.029 200.204 195.527 1.00 10.29  ? 4156 ASN A OD1   1 
ATOM   19206 N  ND2   . ASN A 1 4156 ? 223.850 200.910 197.490 1.00 5.00   ? 4156 ASN A ND2   1 
ATOM   19207 N  N     . MET A 1 4157 ? 223.179 196.722 194.575 1.00 5.92   ? 4157 MET A N     1 
ATOM   19208 C  CA    . MET A 1 4157 ? 222.528 196.559 193.280 1.00 4.79   ? 4157 MET A CA    1 
ATOM   19209 C  C     . MET A 1 4157 ? 221.358 195.588 193.373 1.00 6.69   ? 4157 MET A C     1 
ATOM   19210 O  O     . MET A 1 4157 ? 220.325 195.790 192.723 1.00 9.65   ? 4157 MET A O     1 
ATOM   19211 C  CB    . MET A 1 4157 ? 223.542 196.090 192.238 1.00 4.18   ? 4157 MET A CB    1 
ATOM   19212 C  CG    . MET A 1 4157 ? 224.522 197.171 191.819 1.00 4.12   ? 4157 MET A CG    1 
ATOM   19213 S  SD    . MET A 1 4157 ? 225.299 196.874 190.225 1.00 7.50   ? 4157 MET A SD    1 
ATOM   19214 C  CE    . MET A 1 4157 ? 223.860 196.549 189.217 1.00 7.72   ? 4157 MET A CE    1 
ATOM   19215 N  N     . LEU A 1 4158 ? 221.496 194.530 194.177 1.00 8.22   ? 4158 LEU A N     1 
ATOM   19216 C  CA    . LEU A 1 4158 ? 220.384 193.605 194.373 1.00 5.64   ? 4158 LEU A CA    1 
ATOM   19217 C  C     . LEU A 1 4158 ? 219.199 194.301 195.027 1.00 6.50   ? 4158 LEU A C     1 
ATOM   19218 O  O     . LEU A 1 4158 ? 218.049 194.100 194.619 1.00 10.61  ? 4158 LEU A O     1 
ATOM   19219 C  CB    . LEU A 1 4158 ? 220.832 192.408 195.209 1.00 6.13   ? 4158 LEU A CB    1 
ATOM   19220 C  CG    . LEU A 1 4158 ? 221.676 191.354 194.492 1.00 7.29   ? 4158 LEU A CG    1 
ATOM   19221 C  CD1   . LEU A 1 4158 ? 222.116 190.272 195.462 1.00 11.08  ? 4158 LEU A CD1   1 
ATOM   19222 C  CD2   . LEU A 1 4158 ? 220.911 190.750 193.328 1.00 4.64   ? 4158 LEU A CD2   1 
ATOM   19223 N  N     . ARG A 1 4159 ? 219.459 195.130 196.041 1.00 6.47   ? 4159 ARG A N     1 
ATOM   19224 C  CA    . ARG A 1 4159 ? 218.380 195.879 196.676 1.00 7.97   ? 4159 ARG A CA    1 
ATOM   19225 C  C     . ARG A 1 4159 ? 217.731 196.847 195.696 1.00 9.54   ? 4159 ARG A C     1 
ATOM   19226 O  O     . ARG A 1 4159 ? 216.503 196.989 195.673 1.00 11.37  ? 4159 ARG A O     1 
ATOM   19227 C  CB    . ARG A 1 4159 ? 218.909 196.633 197.895 1.00 7.37   ? 4159 ARG A CB    1 
ATOM   19228 C  CG    . ARG A 1 4159 ? 217.854 197.465 198.606 1.00 9.18   ? 4159 ARG A CG    1 
ATOM   19229 C  CD    . ARG A 1 4159 ? 218.458 198.285 199.729 1.00 18.24  ? 4159 ARG A CD    1 
ATOM   19230 N  NE    . ARG A 1 4159 ? 219.246 197.470 200.645 1.00 29.13  ? 4159 ARG A NE    1 
ATOM   19231 C  CZ    . ARG A 1 4159 ? 219.395 197.729 201.937 1.00 25.78  ? 4159 ARG A CZ    1 
ATOM   19232 N  NH1   . ARG A 1 4159 ? 218.819 198.777 202.503 1.00 19.20  ? 4159 ARG A NH1   1 
ATOM   19233 N  NH2   . ARG A 1 4159 ? 220.144 196.918 202.679 1.00 19.17  ? 4159 ARG A NH2   1 
ATOM   19234 N  N     . THR A 1 4160 ? 218.543 197.523 194.880 1.00 9.42   ? 4160 THR A N     1 
ATOM   19235 C  CA    . THR A 1 4160 ? 217.996 198.458 193.903 1.00 7.21   ? 4160 THR A CA    1 
ATOM   19236 C  C     . THR A 1 4160 ? 217.100 197.743 192.901 1.00 10.89  ? 4160 THR A C     1 
ATOM   19237 O  O     . THR A 1 4160 ? 216.009 198.226 192.576 1.00 14.26  ? 4160 THR A O     1 
ATOM   19238 C  CB    . THR A 1 4160 ? 219.133 199.187 193.184 1.00 7.56   ? 4160 THR A CB    1 
ATOM   19239 O  OG1   . THR A 1 4160 ? 219.718 200.151 194.067 1.00 9.69   ? 4160 THR A OG1   1 
ATOM   19240 C  CG2   . THR A 1 4160 ? 218.619 199.895 191.943 1.00 7.90   ? 4160 THR A CG2   1 
ATOM   19241 N  N     . PHE A 1 4161 ? 217.537 196.581 192.411 1.00 12.30  ? 4161 PHE A N     1 
ATOM   19242 C  CA    . PHE A 1 4161 ? 216.730 195.842 191.445 1.00 12.18  ? 4161 PHE A CA    1 
ATOM   19243 C  C     . PHE A 1 4161 ? 215.479 195.255 192.083 1.00 12.12  ? 4161 PHE A C     1 
ATOM   19244 O  O     . PHE A 1 4161 ? 214.446 195.136 191.415 1.00 18.17  ? 4161 PHE A O     1 
ATOM   19245 C  CB    . PHE A 1 4161 ? 217.568 194.747 190.790 1.00 11.06  ? 4161 PHE A CB    1 
ATOM   19246 C  CG    . PHE A 1 4161 ? 218.357 195.221 189.606 1.00 15.35  ? 4161 PHE A CG    1 
ATOM   19247 C  CD1   . PHE A 1 4161 ? 217.714 195.722 188.488 1.00 12.42  ? 4161 PHE A CD1   1 
ATOM   19248 C  CD2   . PHE A 1 4161 ? 219.739 195.173 189.611 1.00 20.04  ? 4161 PHE A CD2   1 
ATOM   19249 C  CE1   . PHE A 1 4161 ? 218.435 196.164 187.397 1.00 13.83  ? 4161 PHE A CE1   1 
ATOM   19250 C  CE2   . PHE A 1 4161 ? 220.465 195.613 188.523 1.00 15.13  ? 4161 PHE A CE2   1 
ATOM   19251 C  CZ    . PHE A 1 4161 ? 219.812 196.108 187.415 1.00 12.24  ? 4161 PHE A CZ    1 
ATOM   19252 N  N     . SER A 1 4162 ? 215.545 194.884 193.363 1.00 10.64  ? 4162 SER A N     1 
ATOM   19253 C  CA    . SER A 1 4162 ? 214.359 194.370 194.037 1.00 13.15  ? 4162 SER A CA    1 
ATOM   19254 C  C     . SER A 1 4162 ? 213.342 195.471 194.310 1.00 15.79  ? 4162 SER A C     1 
ATOM   19255 O  O     . SER A 1 4162 ? 212.133 195.224 194.242 1.00 19.51  ? 4162 SER A O     1 
ATOM   19256 C  CB    . SER A 1 4162 ? 214.756 193.679 195.341 1.00 12.73  ? 4162 SER A CB    1 
ATOM   19257 O  OG    . SER A 1 4162 ? 214.957 194.623 196.376 1.00 20.57  ? 4162 SER A OG    1 
ATOM   19258 N  N     . SER A 1 4163 ? 213.807 196.684 194.625 1.00 16.37  ? 4163 SER A N     1 
ATOM   19259 C  CA    . SER A 1 4163 ? 212.884 197.771 194.938 1.00 13.36  ? 4163 SER A CA    1 
ATOM   19260 C  C     . SER A 1 4163 ? 212.109 198.222 193.705 1.00 16.48  ? 4163 SER A C     1 
ATOM   19261 O  O     . SER A 1 4163 ? 210.898 198.463 193.781 1.00 28.63  ? 4163 SER A O     1 
ATOM   19262 C  CB    . SER A 1 4163 ? 213.646 198.943 195.552 1.00 16.07  ? 4163 SER A CB    1 
ATOM   19263 O  OG    . SER A 1 4163 ? 214.318 199.696 194.557 1.00 20.36  ? 4163 SER A OG    1 
ATOM   19264 N  N     . ILE A 1 4164 ? 212.782 198.348 192.570 1.00 15.33  ? 4164 ILE A N     1 
ATOM   19265 C  CA    . ILE A 1 4164 ? 212.111 198.801 191.346 1.00 17.85  ? 4164 ILE A CA    1 
ATOM   19266 C  C     . ILE A 1 4164 ? 211.221 197.683 190.815 1.00 18.90  ? 4164 ILE A C     1 
ATOM   19267 O  O     . ILE A 1 4164 ? 211.671 196.527 190.727 1.00 21.23  ? 4164 ILE A O     1 
ATOM   19268 C  CB    . ILE A 1 4164 ? 213.141 199.231 190.302 1.00 18.72  ? 4164 ILE A CB    1 
ATOM   19269 C  CG1   . ILE A 1 4164 ? 214.058 200.313 190.873 1.00 14.06  ? 4164 ILE A CG1   1 
ATOM   19270 C  CG2   . ILE A 1 4164 ? 212.455 199.726 189.040 1.00 22.03  ? 4164 ILE A CG2   1 
ATOM   19271 C  CD1   . ILE A 1 4164 ? 215.151 200.739 189.928 1.00 17.46  ? 4164 ILE A CD1   1 
ATOM   19272 N  N     . PRO A 1 4165 ? 209.967 197.965 190.459 1.00 24.87  ? 4165 PRO A N     1 
ATOM   19273 C  CA    . PRO A 1 4165 ? 209.100 196.916 189.910 1.00 21.97  ? 4165 PRO A CA    1 
ATOM   19274 C  C     . PRO A 1 4165 ? 209.634 196.368 188.596 1.00 20.71  ? 4165 PRO A C     1 
ATOM   19275 O  O     . PRO A 1 4165 ? 210.288 197.069 187.822 1.00 24.84  ? 4165 PRO A O     1 
ATOM   19276 C  CB    . PRO A 1 4165 ? 207.759 197.632 189.711 1.00 19.40  ? 4165 PRO A CB    1 
ATOM   19277 C  CG    . PRO A 1 4165 ? 207.814 198.810 190.624 1.00 19.99  ? 4165 PRO A CG    1 
ATOM   19278 C  CD    . PRO A 1 4165 ? 209.246 199.234 190.654 1.00 23.35  ? 4165 PRO A CD    1 
ATOM   19279 N  N     . VAL A 1 4166 ? 209.350 195.087 188.356 1.00 24.39  ? 4166 VAL A N     1 
ATOM   19280 C  CA    . VAL A 1 4166 ? 209.811 194.433 187.134 1.00 28.14  ? 4166 VAL A CA    1 
ATOM   19281 C  C     . VAL A 1 4166 ? 209.149 195.055 185.910 1.00 30.01  ? 4166 VAL A C     1 
ATOM   19282 O  O     . VAL A 1 4166 ? 209.788 195.230 184.865 1.00 33.06  ? 4166 VAL A O     1 
ATOM   19283 C  CB    . VAL A 1 4166 ? 209.552 192.917 187.211 1.00 26.72  ? 4166 VAL A CB    1 
ATOM   19284 C  CG1   . VAL A 1 4166 ? 210.205 192.205 186.037 1.00 23.70  ? 4166 VAL A CG1   1 
ATOM   19285 C  CG2   . VAL A 1 4166 ? 210.063 192.359 188.527 1.00 27.54  ? 4166 VAL A CG2   1 
ATOM   19286 N  N     . SER A 1 4167 ? 207.862 195.392 186.015 1.00 31.79  ? 4167 SER A N     1 
ATOM   19287 C  CA    . SER A 1 4167 ? 207.152 195.973 184.880 1.00 30.36  ? 4167 SER A CA    1 
ATOM   19288 C  C     . SER A 1 4167 ? 207.720 197.332 184.491 1.00 32.02  ? 4167 SER A C     1 
ATOM   19289 O  O     . SER A 1 4167 ? 207.615 197.735 183.327 1.00 36.69  ? 4167 SER A O     1 
ATOM   19290 C  CB    . SER A 1 4167 ? 205.664 196.099 185.199 1.00 28.02  ? 4167 SER A CB    1 
ATOM   19291 O  OG    . SER A 1 4167 ? 205.451 196.981 186.285 1.00 29.05  ? 4167 SER A OG    1 
ATOM   19292 N  N     . ARG A 1 4168 ? 208.312 198.052 185.444 1.00 29.30  ? 4168 ARG A N     1 
ATOM   19293 C  CA    . ARG A 1 4168 ? 208.894 199.354 185.134 1.00 23.94  ? 4168 ARG A CA    1 
ATOM   19294 C  C     . ARG A 1 4168 ? 210.128 199.209 184.254 1.00 29.67  ? 4168 ARG A C     1 
ATOM   19295 O  O     . ARG A 1 4168 ? 210.292 199.941 183.270 1.00 34.91  ? 4168 ARG A O     1 
ATOM   19296 C  CB    . ARG A 1 4168 ? 209.236 200.095 186.425 1.00 20.73  ? 4168 ARG A CB    1 
ATOM   19297 C  CG    . ARG A 1 4168 ? 210.027 201.370 186.209 1.00 25.17  ? 4168 ARG A CG    1 
ATOM   19298 C  CD    . ARG A 1 4168 ? 210.071 202.217 187.465 1.00 26.92  ? 4168 ARG A CD    1 
ATOM   19299 N  NE    . ARG A 1 4168 ? 210.063 203.641 187.156 1.00 19.81  ? 4168 ARG A NE    1 
ATOM   19300 C  CZ    . ARG A 1 4168 ? 210.220 204.602 188.055 1.00 18.81  ? 4168 ARG A CZ    1 
ATOM   19301 N  NH1   . ARG A 1 4168 ? 210.416 204.328 189.333 1.00 22.69  ? 4168 ARG A NH1   1 
ATOM   19302 N  NH2   . ARG A 1 4168 ? 210.184 205.871 187.660 1.00 21.47  ? 4168 ARG A NH2   1 
ATOM   19303 N  N     . ILE A 1 4169 ? 211.012 198.270 184.594 1.00 29.69  ? 4169 ILE A N     1 
ATOM   19304 C  CA    . ILE A 1 4169 ? 212.239 198.089 183.825 1.00 27.01  ? 4169 ILE A CA    1 
ATOM   19305 C  C     . ILE A 1 4169 ? 211.933 197.512 182.448 1.00 29.67  ? 4169 ILE A C     1 
ATOM   19306 O  O     . ILE A 1 4169 ? 212.520 197.926 181.443 1.00 32.08  ? 4169 ILE A O     1 
ATOM   19307 C  CB    . ILE A 1 4169 ? 213.229 197.205 184.605 1.00 24.77  ? 4169 ILE A CB    1 
ATOM   19308 C  CG1   . ILE A 1 4169 ? 213.358 197.702 186.046 1.00 20.12  ? 4169 ILE A CG1   1 
ATOM   19309 C  CG2   . ILE A 1 4169 ? 214.584 197.195 183.922 1.00 22.84  ? 4169 ILE A CG2   1 
ATOM   19310 C  CD1   . ILE A 1 4169 ? 214.407 196.974 186.850 1.00 22.60  ? 4169 ILE A CD1   1 
ATOM   19311 N  N     . CYS A 1 4170 ? 211.015 196.552 182.379 1.00 30.61  ? 4170 CYS A N     1 
ATOM   19312 C  CA    . CYS A 1 4170 ? 210.629 195.931 181.114 1.00 35.71  ? 4170 CYS A CA    1 
ATOM   19313 C  C     . CYS A 1 4170 ? 209.486 196.739 180.516 1.00 40.48  ? 4170 CYS A C     1 
ATOM   19314 O  O     . CYS A 1 4170 ? 208.319 196.541 180.863 1.00 47.81  ? 4170 CYS A O     1 
ATOM   19315 C  CB    . CYS A 1 4170 ? 210.237 194.474 181.327 1.00 44.96  ? 4170 CYS A CB    1 
ATOM   19316 S  SG    . CYS A 1 4170 ? 211.375 193.544 182.379 1.00 62.40  ? 4170 CYS A SG    1 
ATOM   19317 N  N     . LYS A 1 4171 ? 209.820 197.651 179.607 1.00 44.62  ? 4171 LYS A N     1 
ATOM   19318 C  CA    . LYS A 1 4171 ? 208.838 198.518 178.970 1.00 39.49  ? 4171 LYS A CA    1 
ATOM   19319 C  C     . LYS A 1 4171 ? 209.146 198.569 177.477 1.00 50.82  ? 4171 LYS A C     1 
ATOM   19320 O  O     . LYS A 1 4171 ? 209.907 197.749 176.953 1.00 61.72  ? 4171 LYS A O     1 
ATOM   19321 C  CB    . LYS A 1 4171 ? 208.826 199.908 179.616 1.00 36.55  ? 4171 LYS A CB    1 
ATOM   19322 C  CG    . LYS A 1 4171 ? 207.700 200.104 180.618 1.00 33.99  ? 4171 LYS A CG    1 
ATOM   19323 C  CD    . LYS A 1 4171 ? 207.458 201.573 180.908 1.00 40.58  ? 4171 LYS A CD    1 
ATOM   19324 C  CE    . LYS A 1 4171 ? 206.765 202.257 179.744 1.00 44.44  ? 4171 LYS A CE    1 
ATOM   19325 N  NZ    . LYS A 1 4171 ? 206.143 203.547 180.152 1.00 40.52  ? 4171 LYS A NZ    1 
ATOM   19326 N  N     . SER A 1 4172 ? 208.535 199.534 176.790 1.00 51.15  ? 4172 SER A N     1 
ATOM   19327 C  CA    . SER A 1 4172 ? 208.590 199.588 175.329 1.00 52.54  ? 4172 SER A CA    1 
ATOM   19328 C  C     . SER A 1 4172 ? 210.006 199.575 174.761 1.00 49.32  ? 4172 SER A C     1 
ATOM   19329 O  O     . SER A 1 4172 ? 210.264 198.780 173.843 1.00 59.15  ? 4172 SER A O     1 
ATOM   19330 C  CB    . SER A 1 4172 ? 207.806 200.815 174.842 1.00 58.95  ? 4172 SER A CB    1 
ATOM   19331 O  OG    . SER A 1 4172 ? 206.466 200.779 175.298 1.00 54.90  ? 4172 SER A OG    1 
ATOM   19332 N  N     . PRO A 1 4173 ? 210.964 200.393 175.237 1.00 44.57  ? 4173 PRO A N     1 
ATOM   19333 C  CA    . PRO A 1 4173 ? 212.325 200.281 174.697 1.00 44.00  ? 4173 PRO A CA    1 
ATOM   19334 C  C     . PRO A 1 4173 ? 213.157 199.241 175.433 1.00 45.98  ? 4173 PRO A C     1 
ATOM   19335 O  O     . PRO A 1 4173 ? 213.206 199.236 176.667 1.00 47.42  ? 4173 PRO A O     1 
ATOM   19336 C  CB    . PRO A 1 4173 ? 212.890 201.694 174.882 1.00 34.50  ? 4173 PRO A CB    1 
ATOM   19337 C  CG    . PRO A 1 4173 ? 212.173 202.228 176.069 1.00 39.37  ? 4173 PRO A CG    1 
ATOM   19338 C  CD    . PRO A 1 4173 ? 210.847 201.517 176.185 1.00 42.68  ? 4173 PRO A CD    1 
ATOM   19339 N  N     . ASN A 1 4174 ? 213.808 198.349 174.683 1.00 41.03  ? 4174 ASN A N     1 
ATOM   19340 C  CA    . ASN A 1 4174 ? 214.650 197.331 175.302 1.00 41.25  ? 4174 ASN A CA    1 
ATOM   19341 C  C     . ASN A 1 4174 ? 215.882 197.927 175.970 1.00 37.37  ? 4174 ASN A C     1 
ATOM   19342 O  O     . ASN A 1 4174 ? 216.474 197.279 176.840 1.00 36.50  ? 4174 ASN A O     1 
ATOM   19343 C  CB    . ASN A 1 4174 ? 215.081 196.295 174.262 1.00 37.37  ? 4174 ASN A CB    1 
ATOM   19344 C  CG    . ASN A 1 4174 ? 213.919 195.473 173.741 1.00 47.05  ? 4174 ASN A CG    1 
ATOM   19345 O  OD1   . ASN A 1 4174 ? 212.793 195.589 174.225 1.00 46.49  ? 4174 ASN A OD1   1 
ATOM   19346 N  ND2   . ASN A 1 4174 ? 214.188 194.633 172.749 1.00 47.43  ? 4174 ASN A ND2   1 
ATOM   19347 N  N     . GLU A 1 4175 ? 216.276 199.141 175.584 1.00 34.33  ? 4175 GLU A N     1 
ATOM   19348 C  CA    . GLU A 1 4175 ? 217.455 199.776 176.159 1.00 26.82  ? 4175 GLU A CA    1 
ATOM   19349 C  C     . GLU A 1 4175 ? 217.202 200.280 177.574 1.00 24.13  ? 4175 GLU A C     1 
ATOM   19350 O  O     . GLU A 1 4175 ? 218.160 200.591 178.296 1.00 23.16  ? 4175 GLU A O     1 
ATOM   19351 C  CB    . GLU A 1 4175 ? 217.901 200.926 175.255 1.00 29.82  ? 4175 GLU A CB    1 
ATOM   19352 C  CG    . GLU A 1 4175 ? 218.572 200.478 173.961 1.00 32.18  ? 4175 GLU A CG    1 
ATOM   19353 C  CD    . GLU A 1 4175 ? 217.596 199.910 172.945 1.00 42.74  ? 4175 GLU A CD    1 
ATOM   19354 O  OE1   . GLU A 1 4175 ? 216.371 200.040 173.147 1.00 46.31  ? 4175 GLU A OE1   1 
ATOM   19355 O  OE2   . GLU A 1 4175 ? 218.055 199.324 171.942 1.00 46.62  ? 4175 GLU A OE2   1 
ATOM   19356 N  N     . ARG A 1 4176 ? 215.934 200.359 177.981 1.00 23.21  ? 4176 ARG A N     1 
ATOM   19357 C  CA    . ARG A 1 4176 ? 215.591 200.842 179.313 1.00 17.73  ? 4176 ARG A CA    1 
ATOM   19358 C  C     . ARG A 1 4176 ? 216.188 199.947 180.391 1.00 17.87  ? 4176 ARG A C     1 
ATOM   19359 O  O     . ARG A 1 4176 ? 216.601 200.425 181.453 1.00 18.86  ? 4176 ARG A O     1 
ATOM   19360 C  CB    . ARG A 1 4176 ? 214.069 200.923 179.454 1.00 23.40  ? 4176 ARG A CB    1 
ATOM   19361 C  CG    . ARG A 1 4176 ? 213.580 201.296 180.840 1.00 26.27  ? 4176 ARG A CG    1 
ATOM   19362 C  CD    . ARG A 1 4176 ? 212.063 201.308 180.897 1.00 26.09  ? 4176 ARG A CD    1 
ATOM   19363 N  NE    . ARG A 1 4176 ? 211.473 201.991 179.753 1.00 33.05  ? 4176 ARG A NE    1 
ATOM   19364 C  CZ    . ARG A 1 4176 ? 210.756 203.104 179.834 1.00 33.73  ? 4176 ARG A CZ    1 
ATOM   19365 N  NH1   . ARG A 1 4176 ? 210.525 203.694 180.995 1.00 31.49  ? 4176 ARG A NH1   1 
ATOM   19366 N  NH2   . ARG A 1 4176 ? 210.257 203.637 178.723 1.00 33.45  ? 4176 ARG A NH2   1 
ATOM   19367 N  N     . ALA A 1 4177 ? 216.244 198.639 180.131 1.00 24.73  ? 4177 ALA A N     1 
ATOM   19368 C  CA    . ALA A 1 4177 ? 216.822 197.715 181.101 1.00 18.66  ? 4177 ALA A CA    1 
ATOM   19369 C  C     . ALA A 1 4177 ? 218.298 198.008 181.332 1.00 15.39  ? 4177 ALA A C     1 
ATOM   19370 O  O     . ALA A 1 4177 ? 218.773 198.020 182.473 1.00 16.93  ? 4177 ALA A O     1 
ATOM   19371 C  CB    . ALA A 1 4177 ? 216.622 196.274 180.630 1.00 19.77  ? 4177 ALA A CB    1 
ATOM   19372 N  N     . ARG A 1 4178 ? 219.043 198.259 180.254 1.00 14.53  ? 4178 ARG A N     1 
ATOM   19373 C  CA    . ARG A 1 4178 ? 220.464 198.554 180.400 1.00 11.24  ? 4178 ARG A CA    1 
ATOM   19374 C  C     . ARG A 1 4178 ? 220.670 199.916 181.052 1.00 11.84  ? 4178 ARG A C     1 
ATOM   19375 O  O     . ARG A 1 4178 ? 221.613 200.108 181.828 1.00 13.51  ? 4178 ARG A O     1 
ATOM   19376 C  CB    . ARG A 1 4178 ? 221.162 198.489 179.043 1.00 11.84  ? 4178 ARG A CB    1 
ATOM   19377 C  CG    . ARG A 1 4178 ? 222.666 198.298 179.145 1.00 10.33  ? 4178 ARG A CG    1 
ATOM   19378 C  CD    . ARG A 1 4178 ? 223.323 198.362 177.783 1.00 16.00  ? 4178 ARG A CD    1 
ATOM   19379 N  NE    . ARG A 1 4178 ? 224.543 197.571 177.709 1.00 23.60  ? 4178 ARG A NE    1 
ATOM   19380 C  CZ    . ARG A 1 4178 ? 224.574 196.258 177.520 1.00 27.38  ? 4178 ARG A CZ    1 
ATOM   19381 N  NH1   . ARG A 1 4178 ? 223.465 195.554 177.372 1.00 23.85  ? 4178 ARG A NH1   1 
ATOM   19382 N  NH2   . ARG A 1 4178 ? 225.749 195.638 177.473 1.00 33.32  ? 4178 ARG A NH2   1 
ATOM   19383 N  N     . LEU A 1 4179 ? 219.793 200.876 180.750 1.00 15.14  ? 4179 LEU A N     1 
ATOM   19384 C  CA    . LEU A 1 4179 ? 219.871 202.170 181.423 1.00 10.16  ? 4179 LEU A CA    1 
ATOM   19385 C  C     . LEU A 1 4179 ? 219.647 202.021 182.923 1.00 9.86   ? 4179 LEU A C     1 
ATOM   19386 O  O     . LEU A 1 4179 ? 220.350 202.632 183.735 1.00 12.62  ? 4179 LEU A O     1 
ATOM   19387 C  CB    . LEU A 1 4179 ? 218.858 203.145 180.820 1.00 10.92  ? 4179 LEU A CB    1 
ATOM   19388 C  CG    . LEU A 1 4179 ? 219.103 203.569 179.374 1.00 12.30  ? 4179 LEU A CG    1 
ATOM   19389 C  CD1   . LEU A 1 4179 ? 218.278 204.795 179.028 1.00 13.91  ? 4179 LEU A CD1   1 
ATOM   19390 C  CD2   . LEU A 1 4179 ? 220.576 203.836 179.148 1.00 9.87   ? 4179 LEU A CD2   1 
ATOM   19391 N  N     . TYR A 1 4180 ? 218.668 201.202 183.309 1.00 12.99  ? 4180 TYR A N     1 
ATOM   19392 C  CA    . TYR A 1 4180 ? 218.420 200.962 184.727 1.00 10.73  ? 4180 TYR A CA    1 
ATOM   19393 C  C     . TYR A 1 4180 ? 219.586 200.233 185.381 1.00 9.42   ? 4180 TYR A C     1 
ATOM   19394 O  O     . TYR A 1 4180 ? 219.918 200.498 186.541 1.00 8.03   ? 4180 TYR A O     1 
ATOM   19395 C  CB    . TYR A 1 4180 ? 217.121 200.179 184.911 1.00 10.63  ? 4180 TYR A CB    1 
ATOM   19396 C  CG    . TYR A 1 4180 ? 215.906 201.059 185.069 1.00 13.90  ? 4180 TYR A CG    1 
ATOM   19397 C  CD1   . TYR A 1 4180 ? 215.414 201.800 184.005 1.00 15.09  ? 4180 TYR A CD1   1 
ATOM   19398 C  CD2   . TYR A 1 4180 ? 215.251 201.150 186.288 1.00 19.33  ? 4180 TYR A CD2   1 
ATOM   19399 C  CE1   . TYR A 1 4180 ? 214.305 202.607 184.150 1.00 18.01  ? 4180 TYR A CE1   1 
ATOM   19400 C  CE2   . TYR A 1 4180 ? 214.142 201.951 186.443 1.00 19.46  ? 4180 TYR A CE2   1 
ATOM   19401 C  CZ    . TYR A 1 4180 ? 213.672 202.678 185.371 1.00 22.31  ? 4180 TYR A CZ    1 
ATOM   19402 O  OH    . TYR A 1 4180 ? 212.566 203.476 185.526 1.00 27.60  ? 4180 TYR A OH    1 
ATOM   19403 N  N     . PHE A 1 4181 ? 220.210 199.298 184.664 1.00 10.57  ? 4181 PHE A N     1 
ATOM   19404 C  CA    . PHE A 1 4181 ? 221.382 198.618 185.209 1.00 8.31   ? 4181 PHE A CA    1 
ATOM   19405 C  C     . PHE A 1 4181 ? 222.527 199.598 185.435 1.00 8.78   ? 4181 PHE A C     1 
ATOM   19406 O  O     . PHE A 1 4181 ? 223.221 199.542 186.458 1.00 8.39   ? 4181 PHE A O     1 
ATOM   19407 C  CB    . PHE A 1 4181 ? 221.821 197.487 184.280 1.00 9.90   ? 4181 PHE A CB    1 
ATOM   19408 C  CG    . PHE A 1 4181 ? 223.123 196.858 184.678 1.00 10.65  ? 4181 PHE A CG    1 
ATOM   19409 C  CD1   . PHE A 1 4181 ? 223.158 195.853 185.626 1.00 9.62   ? 4181 PHE A CD1   1 
ATOM   19410 C  CD2   . PHE A 1 4181 ? 224.313 197.280 184.115 1.00 13.02  ? 4181 PHE A CD2   1 
ATOM   19411 C  CE1   . PHE A 1 4181 ? 224.354 195.279 185.998 1.00 11.80  ? 4181 PHE A CE1   1 
ATOM   19412 C  CE2   . PHE A 1 4181 ? 225.510 196.711 184.485 1.00 11.75  ? 4181 PHE A CE2   1 
ATOM   19413 C  CZ    . PHE A 1 4181 ? 225.530 195.711 185.427 1.00 13.05  ? 4181 PHE A CZ    1 
ATOM   19414 N  N     . LEU A 1 4182 ? 222.752 200.496 184.473 1.00 11.94  ? 4182 LEU A N     1 
ATOM   19415 C  CA    . LEU A 1 4182 ? 223.773 201.526 184.638 1.00 7.94   ? 4182 LEU A CA    1 
ATOM   19416 C  C     . LEU A 1 4182 ? 223.451 202.423 185.825 1.00 5.61   ? 4182 LEU A C     1 
ATOM   19417 O  O     . LEU A 1 4182 ? 224.339 202.802 186.594 1.00 6.66   ? 4182 LEU A O     1 
ATOM   19418 C  CB    . LEU A 1 4182 ? 223.895 202.352 183.358 1.00 6.62   ? 4182 LEU A CB    1 
ATOM   19419 C  CG    . LEU A 1 4182 ? 224.646 201.719 182.188 1.00 7.93   ? 4182 LEU A CG    1 
ATOM   19420 C  CD1   . LEU A 1 4182 ? 224.436 202.539 180.929 1.00 13.15  ? 4182 LEU A CD1   1 
ATOM   19421 C  CD2   . LEU A 1 4182 ? 226.125 201.598 182.509 1.00 10.68  ? 4182 LEU A CD2   1 
ATOM   19422 N  N     . LEU A 1 4183 ? 222.174 202.771 185.983 1.00 5.51   ? 4183 LEU A N     1 
ATOM   19423 C  CA    . LEU A 1 4183 ? 221.746 203.577 187.120 1.00 4.93   ? 4183 LEU A CA    1 
ATOM   19424 C  C     . LEU A 1 4183 ? 222.034 202.865 188.436 1.00 5.70   ? 4183 LEU A C     1 
ATOM   19425 O  O     . LEU A 1 4183 ? 222.518 203.477 189.395 1.00 6.03   ? 4183 LEU A O     1 
ATOM   19426 C  CB    . LEU A 1 4183 ? 220.255 203.885 186.989 1.00 6.70   ? 4183 LEU A CB    1 
ATOM   19427 C  CG    . LEU A 1 4183 ? 219.702 205.086 187.746 1.00 8.22   ? 4183 LEU A CG    1 
ATOM   19428 C  CD1   . LEU A 1 4183 ? 220.644 206.254 187.597 1.00 8.06   ? 4183 LEU A CD1   1 
ATOM   19429 C  CD2   . LEU A 1 4183 ? 218.327 205.435 187.219 1.00 7.19   ? 4183 LEU A CD2   1 
ATOM   19430 N  N     . ALA A 1 4184 ? 221.733 201.566 188.499 1.00 6.05   ? 4184 ALA A N     1 
ATOM   19431 C  CA    . ALA A 1 4184 ? 221.978 200.797 189.714 1.00 4.66   ? 4184 ALA A CA    1 
ATOM   19432 C  C     . ALA A 1 4184 ? 223.465 200.710 190.026 1.00 4.68   ? 4184 ALA A C     1 
ATOM   19433 O  O     . ALA A 1 4184 ? 223.873 200.860 191.182 1.00 5.46   ? 4184 ALA A O     1 
ATOM   19434 C  CB    . ALA A 1 4184 ? 221.378 199.398 189.579 1.00 6.42   ? 4184 ALA A CB    1 
ATOM   19435 N  N     . TRP A 1 4185 ? 224.291 200.466 189.006 1.00 4.36   ? 4185 TRP A N     1 
ATOM   19436 C  CA    . TRP A 1 4185 ? 225.735 200.421 189.218 1.00 3.23   ? 4185 TRP A CA    1 
ATOM   19437 C  C     . TRP A 1 4185 ? 226.255 201.764 189.714 1.00 4.15   ? 4185 TRP A C     1 
ATOM   19438 O  O     . TRP A 1 4185 ? 227.066 201.822 190.646 1.00 5.92   ? 4185 TRP A O     1 
ATOM   19439 C  CB    . TRP A 1 4185 ? 226.448 200.016 187.929 1.00 4.45   ? 4185 TRP A CB    1 
ATOM   19440 C  CG    . TRP A 1 4185 ? 227.942 200.035 188.051 1.00 4.78   ? 4185 TRP A CG    1 
ATOM   19441 C  CD1   . TRP A 1 4185 ? 228.782 201.033 187.656 1.00 3.32   ? 4185 TRP A CD1   1 
ATOM   19442 C  CD2   . TRP A 1 4185 ? 228.774 199.007 188.600 1.00 5.38   ? 4185 TRP A CD2   1 
ATOM   19443 N  NE1   . TRP A 1 4185 ? 230.083 200.694 187.929 1.00 4.09   ? 4185 TRP A NE1   1 
ATOM   19444 C  CE2   . TRP A 1 4185 ? 230.105 199.454 188.508 1.00 5.34   ? 4185 TRP A CE2   1 
ATOM   19445 C  CE3   . TRP A 1 4185 ? 228.521 197.752 189.161 1.00 4.29   ? 4185 TRP A CE3   1 
ATOM   19446 C  CZ2   . TRP A 1 4185 ? 231.180 198.691 188.956 1.00 5.69   ? 4185 TRP A CZ2   1 
ATOM   19447 C  CZ3   . TRP A 1 4185 ? 229.589 196.998 189.605 1.00 4.79   ? 4185 TRP A CZ3   1 
ATOM   19448 C  CH2   . TRP A 1 4185 ? 230.901 197.470 189.501 1.00 5.90   ? 4185 TRP A CH2   1 
ATOM   19449 N  N     . PHE A 1 4186 ? 225.793 202.853 189.099 1.00 4.05   ? 4186 PHE A N     1 
ATOM   19450 C  CA    . PHE A 1 4186 ? 226.213 204.189 189.505 1.00 3.35   ? 4186 PHE A CA    1 
ATOM   19451 C  C     . PHE A 1 4186 ? 225.842 204.444 190.963 1.00 3.80   ? 4186 PHE A C     1 
ATOM   19452 O  O     . PHE A 1 4186 ? 226.685 204.843 191.778 1.00 4.70   ? 4186 PHE A O     1 
ATOM   19453 C  CB    . PHE A 1 4186 ? 225.548 205.213 188.582 1.00 4.69   ? 4186 PHE A CB    1 
ATOM   19454 C  CG    . PHE A 1 4186 ? 225.879 206.645 188.891 1.00 5.85   ? 4186 PHE A CG    1 
ATOM   19455 C  CD1   . PHE A 1 4186 ? 227.086 207.190 188.491 1.00 6.59   ? 4186 PHE A CD1   1 
ATOM   19456 C  CD2   . PHE A 1 4186 ? 224.986 207.443 189.583 1.00 4.08   ? 4186 PHE A CD2   1 
ATOM   19457 C  CE1   . PHE A 1 4186 ? 227.389 208.511 188.759 1.00 7.88   ? 4186 PHE A CE1   1 
ATOM   19458 C  CE2   . PHE A 1 4186 ? 225.289 208.759 189.867 1.00 3.65   ? 4186 PHE A CE2   1 
ATOM   19459 C  CZ    . PHE A 1 4186 ? 226.491 209.294 189.455 1.00 6.42   ? 4186 PHE A CZ    1 
ATOM   19460 N  N     . HIS A 1 4187 ? 224.579 204.185 191.309 1.00 4.42   ? 4187 HIS A N     1 
ATOM   19461 C  CA    . HIS A 1 4187 ? 224.112 204.399 192.671 1.00 3.30   ? 4187 HIS A CA    1 
ATOM   19462 C  C     . HIS A 1 4187 ? 224.906 203.568 193.665 1.00 4.33   ? 4187 HIS A C     1 
ATOM   19463 O  O     . HIS A 1 4187 ? 225.289 204.072 194.727 1.00 5.71   ? 4187 HIS A O     1 
ATOM   19464 C  CB    . HIS A 1 4187 ? 222.622 204.066 192.758 1.00 4.19   ? 4187 HIS A CB    1 
ATOM   19465 C  CG    . HIS A 1 4187 ? 222.006 204.374 194.086 1.00 5.08   ? 4187 HIS A CG    1 
ATOM   19466 N  ND1   . HIS A 1 4187 ? 221.834 205.662 194.543 1.00 6.27   ? 4187 HIS A ND1   1 
ATOM   19467 C  CD2   . HIS A 1 4187 ? 221.515 203.563 195.051 1.00 5.39   ? 4187 HIS A CD2   1 
ATOM   19468 C  CE1   . HIS A 1 4187 ? 221.267 205.631 195.735 1.00 6.72   ? 4187 HIS A CE1   1 
ATOM   19469 N  NE2   . HIS A 1 4187 ? 221.062 204.369 196.066 1.00 6.89   ? 4187 HIS A NE2   1 
ATOM   19470 N  N     . ALA A 1 4188 ? 225.182 202.305 193.332 1.00 4.55   ? 4188 ALA A N     1 
ATOM   19471 C  CA    . ALA A 1 4188 ? 225.961 201.453 194.222 1.00 4.36   ? 4188 ALA A CA    1 
ATOM   19472 C  C     . ALA A 1 4188 ? 227.370 201.997 194.417 1.00 4.76   ? 4188 ALA A C     1 
ATOM   19473 O  O     . ALA A 1 4188 ? 227.881 202.021 195.541 1.00 8.28   ? 4188 ALA A O     1 
ATOM   19474 C  CB    . ALA A 1 4188 ? 226.003 200.026 193.676 1.00 4.58   ? 4188 ALA A CB    1 
ATOM   19475 N  N     . ILE A 1 4189 ? 228.012 202.449 193.336 1.00 4.30   ? 4189 ILE A N     1 
ATOM   19476 C  CA    . ILE A 1 4189 ? 229.384 202.943 193.448 1.00 3.63   ? 4189 ILE A CA    1 
ATOM   19477 C  C     . ILE A 1 4189 ? 229.448 204.170 194.347 1.00 4.27   ? 4189 ILE A C     1 
ATOM   19478 O  O     . ILE A 1 4189 ? 230.279 204.242 195.264 1.00 5.47   ? 4189 ILE A O     1 
ATOM   19479 C  CB    . ILE A 1 4189 ? 229.972 203.236 192.053 1.00 4.58   ? 4189 ILE A CB    1 
ATOM   19480 C  CG1   . ILE A 1 4189 ? 230.063 201.954 191.222 1.00 4.47   ? 4189 ILE A CG1   1 
ATOM   19481 C  CG2   . ILE A 1 4189 ? 231.335 203.896 192.175 1.00 5.25   ? 4189 ILE A CG2   1 
ATOM   19482 C  CD1   . ILE A 1 4189 ? 230.756 200.813 191.921 1.00 3.89   ? 4189 ILE A CD1   1 
ATOM   19483 N  N     . ILE A 1 4190 ? 228.579 205.153 194.106 1.00 4.25   ? 4190 ILE A N     1 
ATOM   19484 C  CA    . ILE A 1 4190 ? 228.625 206.367 194.925 1.00 4.52   ? 4190 ILE A CA    1 
ATOM   19485 C  C     . ILE A 1 4190 ? 228.187 206.104 196.364 1.00 4.25   ? 4190 ILE A C     1 
ATOM   19486 O  O     . ILE A 1 4190 ? 228.747 206.684 197.301 1.00 5.00   ? 4190 ILE A O     1 
ATOM   19487 C  CB    . ILE A 1 4190 ? 227.850 207.525 194.264 1.00 3.86   ? 4190 ILE A CB    1 
ATOM   19488 C  CG1   . ILE A 1 4190 ? 228.549 207.962 192.972 1.00 6.97   ? 4190 ILE A CG1   1 
ATOM   19489 C  CG2   . ILE A 1 4190 ? 227.704 208.688 195.201 1.00 9.06   ? 4190 ILE A CG2   1 
ATOM   19490 C  CD1   . ILE A 1 4190 ? 228.169 207.281 191.754 1.00 7.65   ? 4190 ILE A CD1   1 
ATOM   19491 N  N     . GLN A 1 4191 ? 227.207 205.229 196.579 1.00 5.06   ? 4191 GLN A N     1 
ATOM   19492 C  CA    . GLN A 1 4191 ? 226.846 204.923 197.958 1.00 4.16   ? 4191 GLN A CA    1 
ATOM   19493 C  C     . GLN A 1 4191 ? 227.935 204.154 198.691 1.00 4.40   ? 4191 GLN A C     1 
ATOM   19494 O  O     . GLN A 1 4191 ? 228.115 204.354 199.898 1.00 4.20   ? 4191 GLN A O     1 
ATOM   19495 C  CB    . GLN A 1 4191 ? 225.533 204.138 198.010 1.00 3.50   ? 4191 GLN A CB    1 
ATOM   19496 C  CG    . GLN A 1 4191 ? 224.302 205.022 198.021 1.00 4.82   ? 4191 GLN A CG    1 
ATOM   19497 C  CD    . GLN A 1 4191 ? 223.120 204.371 198.706 1.00 9.29   ? 4191 GLN A CD    1 
ATOM   19498 O  OE1   . GLN A 1 4191 ? 222.884 203.175 198.559 1.00 15.17  ? 4191 GLN A OE1   1 
ATOM   19499 N  NE2   . GLN A 1 4191 ? 222.369 205.162 199.463 1.00 11.26  ? 4191 GLN A NE2   1 
ATOM   19500 N  N     . GLU A 1 4192 ? 228.672 203.289 197.995 1.00 4.51   ? 4192 GLU A N     1 
ATOM   19501 C  CA    . GLU A 1 4192 ? 229.748 202.537 198.622 1.00 5.75   ? 4192 GLU A CA    1 
ATOM   19502 C  C     . GLU A 1 4192 ? 230.995 203.378 198.853 1.00 7.30   ? 4192 GLU A C     1 
ATOM   19503 O  O     . GLU A 1 4192 ? 231.765 203.076 199.771 1.00 9.56   ? 4192 GLU A O     1 
ATOM   19504 C  CB    . GLU A 1 4192 ? 230.092 201.315 197.769 1.00 6.15   ? 4192 GLU A CB    1 
ATOM   19505 C  CG    . GLU A 1 4192 ? 230.653 200.145 198.553 1.00 14.66  ? 4192 GLU A CG    1 
ATOM   19506 C  CD    . GLU A 1 4192 ? 229.630 199.522 199.479 1.00 24.18  ? 4192 GLU A CD    1 
ATOM   19507 O  OE1   . GLU A 1 4192 ? 230.036 198.915 200.492 1.00 22.99  ? 4192 GLU A OE1   1 
ATOM   19508 O  OE2   . GLU A 1 4192 ? 228.420 199.636 199.192 1.00 25.72  ? 4192 GLU A OE2   1 
ATOM   19509 N  N     . ARG A 1 4193 ? 231.220 204.415 198.043 1.00 7.00   ? 4193 ARG A N     1 
ATOM   19510 C  CA    . ARG A 1 4193 ? 232.334 205.319 198.303 1.00 6.12   ? 4193 ARG A CA    1 
ATOM   19511 C  C     . ARG A 1 4193 ? 232.126 206.165 199.552 1.00 6.93   ? 4193 ARG A C     1 
ATOM   19512 O  O     . ARG A 1 4193 ? 233.097 206.731 200.065 1.00 8.86   ? 4193 ARG A O     1 
ATOM   19513 C  CB    . ARG A 1 4193 ? 232.579 206.238 197.105 1.00 6.20   ? 4193 ARG A CB    1 
ATOM   19514 C  CG    . ARG A 1 4193 ? 233.229 205.554 195.921 1.00 7.36   ? 4193 ARG A CG    1 
ATOM   19515 C  CD    . ARG A 1 4193 ? 233.436 206.527 194.776 1.00 7.11   ? 4193 ARG A CD    1 
ATOM   19516 N  NE    . ARG A 1 4193 ? 234.475 207.503 195.080 1.00 6.31   ? 4193 ARG A NE    1 
ATOM   19517 C  CZ    . ARG A 1 4193 ? 235.680 207.512 194.528 1.00 5.79   ? 4193 ARG A CZ    1 
ATOM   19518 N  NH1   . ARG A 1 4193 ? 236.032 206.614 193.625 1.00 5.00   ? 4193 ARG A NH1   1 
ATOM   19519 N  NH2   . ARG A 1 4193 ? 236.554 208.444 194.895 1.00 8.12   ? 4193 ARG A NH2   1 
ATOM   19520 N  N     . LEU A 1 4194 ? 230.892 206.268 200.048 1.00 6.97   ? 4194 LEU A N     1 
ATOM   19521 C  CA    . LEU A 1 4194 ? 230.634 207.034 201.261 1.00 6.45   ? 4194 LEU A CA    1 
ATOM   19522 C  C     . LEU A 1 4194 ? 231.297 206.423 202.489 1.00 8.13   ? 4194 LEU A C     1 
ATOM   19523 O  O     . LEU A 1 4194 ? 231.540 207.139 203.464 1.00 8.90   ? 4194 LEU A O     1 
ATOM   19524 C  CB    . LEU A 1 4194 ? 229.128 207.158 201.495 1.00 5.52   ? 4194 LEU A CB    1 
ATOM   19525 C  CG    . LEU A 1 4194 ? 228.367 208.104 200.565 1.00 6.43   ? 4194 LEU A CG    1 
ATOM   19526 C  CD1   . LEU A 1 4194 ? 226.872 207.864 200.663 1.00 7.10   ? 4194 LEU A CD1   1 
ATOM   19527 C  CD2   . LEU A 1 4194 ? 228.698 209.549 200.890 1.00 9.66   ? 4194 LEU A CD2   1 
ATOM   19528 N  N     . ARG A 1 4195 ? 231.586 205.119 202.464 1.00 8.61   ? 4195 ARG A N     1 
ATOM   19529 C  CA    . ARG A 1 4195 ? 232.255 204.486 203.596 1.00 8.98   ? 4195 ARG A CA    1 
ATOM   19530 C  C     . ARG A 1 4195 ? 233.653 205.053 203.796 1.00 9.61   ? 4195 ARG A C     1 
ATOM   19531 O  O     . ARG A 1 4195 ? 234.098 205.245 204.934 1.00 10.90  ? 4195 ARG A O     1 
ATOM   19532 C  CB    . ARG A 1 4195 ? 232.312 202.974 203.390 1.00 7.97   ? 4195 ARG A CB    1 
ATOM   19533 C  CG    . ARG A 1 4195 ? 230.990 202.361 202.972 1.00 12.41  ? 4195 ARG A CG    1 
ATOM   19534 C  CD    . ARG A 1 4195 ? 231.067 200.845 202.947 1.00 20.27  ? 4195 ARG A CD    1 
ATOM   19535 N  NE    . ARG A 1 4195 ? 229.753 200.231 202.796 1.00 25.54  ? 4195 ARG A NE    1 
ATOM   19536 C  CZ    . ARG A 1 4195 ? 228.859 200.120 203.769 1.00 21.91  ? 4195 ARG A CZ    1 
ATOM   19537 N  NH1   . ARG A 1 4195 ? 229.107 200.564 204.990 1.00 18.38  ? 4195 ARG A NH1   1 
ATOM   19538 N  NH2   . ARG A 1 4195 ? 227.687 199.548 203.511 1.00 15.52  ? 4195 ARG A NH2   1 
ATOM   19539 N  N     . TYR A 1 4196 ? 234.363 205.319 202.702 1.00 8.85   ? 4196 TYR A N     1 
ATOM   19540 C  CA    . TYR A 1 4196 ? 235.700 205.909 202.762 1.00 10.54  ? 4196 TYR A CA    1 
ATOM   19541 C  C     . TYR A 1 4196 ? 235.560 207.427 202.664 1.00 13.86  ? 4196 TYR A C     1 
ATOM   19542 O  O     . TYR A 1 4196 ? 235.896 208.063 201.664 1.00 15.11  ? 4196 TYR A O     1 
ATOM   19543 C  CB    . TYR A 1 4196 ? 236.576 205.332 201.659 1.00 8.17   ? 4196 TYR A CB    1 
ATOM   19544 C  CG    . TYR A 1 4196 ? 236.383 203.843 201.483 1.00 10.63  ? 4196 TYR A CG    1 
ATOM   19545 C  CD1   . TYR A 1 4196 ? 235.461 203.348 200.571 1.00 10.48  ? 4196 TYR A CD1   1 
ATOM   19546 C  CD2   . TYR A 1 4196 ? 237.096 202.932 202.249 1.00 12.36  ? 4196 TYR A CD2   1 
ATOM   19547 C  CE1   . TYR A 1 4196 ? 235.267 201.993 200.414 1.00 11.20  ? 4196 TYR A CE1   1 
ATOM   19548 C  CE2   . TYR A 1 4196 ? 236.909 201.572 202.097 1.00 11.75  ? 4196 TYR A CE2   1 
ATOM   19549 C  CZ    . TYR A 1 4196 ? 235.993 201.108 201.178 1.00 12.44  ? 4196 TYR A CZ    1 
ATOM   19550 O  OH    . TYR A 1 4196 ? 235.799 199.758 201.017 1.00 14.02  ? 4196 TYR A OH    1 
ATOM   19551 N  N     . ALA A 1 4197 ? 235.042 208.000 203.751 1.00 14.74  ? 4197 ALA A N     1 
ATOM   19552 C  CA    . ALA A 1 4197 ? 234.553 209.378 203.724 1.00 12.79  ? 4197 ALA A CA    1 
ATOM   19553 C  C     . ALA A 1 4197 ? 235.610 210.401 203.330 1.00 22.19  ? 4197 ALA A C     1 
ATOM   19554 O  O     . ALA A 1 4197 ? 235.312 211.255 202.478 1.00 29.49  ? 4197 ALA A O     1 
ATOM   19555 C  CB    . ALA A 1 4197 ? 233.923 209.721 205.078 1.00 22.78  ? 4197 ALA A CB    1 
ATOM   19556 N  N     . PRO A 1 4198 ? 236.821 210.409 203.899 1.00 22.30  ? 4198 PRO A N     1 
ATOM   19557 C  CA    . PRO A 1 4198 ? 237.802 211.420 203.468 1.00 14.61  ? 4198 PRO A CA    1 
ATOM   19558 C  C     . PRO A 1 4198 ? 238.205 211.307 202.007 1.00 12.11  ? 4198 PRO A C     1 
ATOM   19559 O  O     . PRO A 1 4198 ? 238.463 212.334 201.369 1.00 17.19  ? 4198 PRO A O     1 
ATOM   19560 C  CB    . PRO A 1 4198 ? 238.995 211.175 204.401 1.00 18.38  ? 4198 PRO A CB    1 
ATOM   19561 C  CG    . PRO A 1 4198 ? 238.430 210.454 205.569 1.00 20.92  ? 4198 PRO A CG    1 
ATOM   19562 C  CD    . PRO A 1 4198 ? 237.344 209.597 205.013 1.00 16.62  ? 4198 PRO A CD    1 
ATOM   19563 N  N     . LEU A 1 4199 ? 238.262 210.096 201.451 1.00 12.72  ? 4199 LEU A N     1 
ATOM   19564 C  CA    . LEU A 1 4199 ? 238.792 209.883 200.107 1.00 9.24   ? 4199 LEU A CA    1 
ATOM   19565 C  C     . LEU A 1 4199 ? 237.709 209.630 199.067 1.00 12.99  ? 4199 LEU A C     1 
ATOM   19566 O  O     . LEU A 1 4199 ? 237.754 210.210 197.979 1.00 20.40  ? 4199 LEU A O     1 
ATOM   19567 C  CB    . LEU A 1 4199 ? 239.784 208.716 200.107 1.00 8.27   ? 4199 LEU A CB    1 
ATOM   19568 C  CG    . LEU A 1 4199 ? 241.238 209.045 200.438 1.00 9.43   ? 4199 LEU A CG    1 
ATOM   19569 C  CD1   . LEU A 1 4199 ? 241.423 209.281 201.930 1.00 12.36  ? 4199 LEU A CD1   1 
ATOM   19570 C  CD2   . LEU A 1 4199 ? 242.143 207.930 199.948 1.00 9.01   ? 4199 LEU A CD2   1 
ATOM   19571 N  N     . GLY A 1 4200 ? 236.743 208.759 199.370 1.00 13.08  ? 4200 GLY A N     1 
ATOM   19572 C  CA    . GLY A 1 4200 ? 235.681 208.489 198.415 1.00 10.20  ? 4200 GLY A CA    1 
ATOM   19573 C  C     . GLY A 1 4200 ? 234.874 209.730 198.087 1.00 11.34  ? 4200 GLY A C     1 
ATOM   19574 O  O     . GLY A 1 4200 ? 234.420 209.908 196.955 1.00 10.59  ? 4200 GLY A O     1 
ATOM   19575 N  N     . TRP A 1 4201 ? 234.684 210.597 199.072 1.00 10.92  ? 4201 TRP A N     1 
ATOM   19576 C  CA    . TRP A 1 4201 ? 234.071 211.904 198.879 1.00 9.75   ? 4201 TRP A CA    1 
ATOM   19577 C  C     . TRP A 1 4201 ? 234.828 212.878 199.774 1.00 16.29  ? 4201 TRP A C     1 
ATOM   19578 O  O     . TRP A 1 4201 ? 235.931 212.586 200.248 1.00 25.48  ? 4201 TRP A O     1 
ATOM   19579 C  CB    . TRP A 1 4201 ? 232.563 211.840 199.162 1.00 10.64  ? 4201 TRP A CB    1 
ATOM   19580 C  CG    . TRP A 1 4201 ? 231.802 211.123 198.093 1.00 9.96   ? 4201 TRP A CG    1 
ATOM   19581 C  CD1   . TRP A 1 4201 ? 231.203 209.902 198.191 1.00 6.38   ? 4201 TRP A CD1   1 
ATOM   19582 C  CD2   . TRP A 1 4201 ? 231.567 211.579 196.757 1.00 11.56  ? 4201 TRP A CD2   1 
ATOM   19583 N  NE1   . TRP A 1 4201 ? 230.606 209.572 196.999 1.00 5.92   ? 4201 TRP A NE1   1 
ATOM   19584 C  CE2   . TRP A 1 4201 ? 230.816 210.586 196.102 1.00 8.69   ? 4201 TRP A CE2   1 
ATOM   19585 C  CE3   . TRP A 1 4201 ? 231.917 212.733 196.052 1.00 10.16  ? 4201 TRP A CE3   1 
ATOM   19586 C  CZ2   . TRP A 1 4201 ? 230.410 210.713 194.777 1.00 9.66   ? 4201 TRP A CZ2   1 
ATOM   19587 C  CZ3   . TRP A 1 4201 ? 231.513 212.855 194.739 1.00 10.31  ? 4201 TRP A CZ3   1 
ATOM   19588 C  CH2   . TRP A 1 4201 ? 230.767 211.852 194.116 1.00 9.71   ? 4201 TRP A CH2   1 
ATOM   19589 N  N     . SER A 1 4202 ? 234.264 214.063 199.993 1.00 16.91  ? 4202 SER A N     1 
ATOM   19590 C  CA    . SER A 1 4202 ? 234.818 214.988 200.970 1.00 15.83  ? 4202 SER A CA    1 
ATOM   19591 C  C     . SER A 1 4202 ? 233.986 215.086 202.237 1.00 22.00  ? 4202 SER A C     1 
ATOM   19592 O  O     . SER A 1 4202 ? 234.513 215.511 203.271 1.00 29.37  ? 4202 SER A O     1 
ATOM   19593 C  CB    . SER A 1 4202 ? 234.974 216.389 200.364 1.00 14.91  ? 4202 SER A CB    1 
ATOM   19594 O  OG    . SER A 1 4202 ? 235.909 216.380 199.302 1.00 24.74  ? 4202 SER A OG    1 
ATOM   19595 N  N     . LYS A 1 4203 ? 232.715 214.701 202.185 1.00 19.64  ? 4203 LYS A N     1 
ATOM   19596 C  CA    . LYS A 1 4203 ? 231.854 214.702 203.355 1.00 18.47  ? 4203 LYS A CA    1 
ATOM   19597 C  C     . LYS A 1 4203 ? 230.773 213.650 203.165 1.00 17.65  ? 4203 LYS A C     1 
ATOM   19598 O  O     . LYS A 1 4203 ? 230.547 213.156 202.058 1.00 18.82  ? 4203 LYS A O     1 
ATOM   19599 C  CB    . LYS A 1 4203 ? 231.234 216.081 203.600 1.00 19.86  ? 4203 LYS A CB    1 
ATOM   19600 C  CG    . LYS A 1 4203 ? 230.607 216.705 202.371 1.00 15.63  ? 4203 LYS A CG    1 
ATOM   19601 C  CD    . LYS A 1 4203 ? 230.031 218.071 202.689 1.00 23.01  ? 4203 LYS A CD    1 
ATOM   19602 C  CE    . LYS A 1 4203 ? 231.125 219.049 203.082 1.00 28.22  ? 4203 LYS A CE    1 
ATOM   19603 N  NZ    . LYS A 1 4203 ? 232.085 219.289 201.970 1.00 25.71  ? 4203 LYS A NZ    1 
ATOM   19604 N  N     . LYS A 1 4204 ? 230.106 213.309 204.267 1.00 18.78  ? 4204 LYS A N     1 
ATOM   19605 C  CA    . LYS A 1 4204 ? 229.072 212.276 204.261 1.00 18.29  ? 4204 LYS A CA    1 
ATOM   19606 C  C     . LYS A 1 4204 ? 227.809 212.837 203.616 1.00 16.58  ? 4204 LYS A C     1 
ATOM   19607 O  O     . LYS A 1 4204 ? 226.858 213.256 204.279 1.00 21.16  ? 4204 LYS A O     1 
ATOM   19608 C  CB    . LYS A 1 4204 ? 228.805 211.779 205.676 1.00 19.32  ? 4204 LYS A CB    1 
ATOM   19609 C  CG    . LYS A 1 4204 ? 229.993 211.102 206.331 1.00 18.82  ? 4204 LYS A CG    1 
ATOM   19610 C  CD    . LYS A 1 4204 ? 230.367 209.832 205.591 1.00 16.93  ? 4204 LYS A CD    1 
ATOM   19611 C  CE    . LYS A 1 4204 ? 229.326 208.746 205.802 1.00 25.76  ? 4204 LYS A CE    1 
ATOM   19612 N  NZ    . LYS A 1 4204 ? 229.711 207.467 205.147 1.00 28.94  ? 4204 LYS A NZ    1 
ATOM   19613 N  N     . TYR A 1 4205 ? 227.807 212.843 202.286 1.00 12.79  ? 4205 TYR A N     1 
ATOM   19614 C  CA    . TYR A 1 4205 ? 226.612 213.219 201.547 1.00 13.17  ? 4205 TYR A CA    1 
ATOM   19615 C  C     . TYR A 1 4205 ? 225.514 212.184 201.754 1.00 16.27  ? 4205 TYR A C     1 
ATOM   19616 O  O     . TYR A 1 4205 ? 225.776 210.996 201.955 1.00 20.69  ? 4205 TYR A O     1 
ATOM   19617 C  CB    . TYR A 1 4205 ? 226.913 213.357 200.058 1.00 12.64  ? 4205 TYR A CB    1 
ATOM   19618 C  CG    . TYR A 1 4205 ? 227.826 214.504 199.709 1.00 10.82  ? 4205 TYR A CG    1 
ATOM   19619 C  CD1   . TYR A 1 4205 ? 227.448 215.815 199.955 1.00 10.43  ? 4205 TYR A CD1   1 
ATOM   19620 C  CD2   . TYR A 1 4205 ? 229.060 214.277 199.124 1.00 10.42  ? 4205 TYR A CD2   1 
ATOM   19621 C  CE1   . TYR A 1 4205 ? 228.277 216.867 199.632 1.00 10.76  ? 4205 TYR A CE1   1 
ATOM   19622 C  CE2   . TYR A 1 4205 ? 229.894 215.321 198.800 1.00 13.91  ? 4205 TYR A CE2   1 
ATOM   19623 C  CZ    . TYR A 1 4205 ? 229.499 216.615 199.056 1.00 13.39  ? 4205 TYR A CZ    1 
ATOM   19624 O  OH    . TYR A 1 4205 ? 230.329 217.662 198.733 1.00 13.59  ? 4205 TYR A OH    1 
ATOM   19625 N  N     . GLU A 1 4206 ? 224.271 212.651 201.700 1.00 17.25  ? 4206 GLU A N     1 
ATOM   19626 C  CA    . GLU A 1 4206 ? 223.123 211.780 201.944 1.00 12.61  ? 4206 GLU A CA    1 
ATOM   19627 C  C     . GLU A 1 4206 ? 222.570 211.242 200.625 1.00 14.40  ? 4206 GLU A C     1 
ATOM   19628 O  O     . GLU A 1 4206 ? 221.398 211.400 200.287 1.00 15.34  ? 4206 GLU A O     1 
ATOM   19629 C  CB    . GLU A 1 4206 ? 222.056 212.528 202.734 1.00 16.28  ? 4206 GLU A CB    1 
ATOM   19630 C  CG    . GLU A 1 4206 ? 222.494 212.898 204.138 1.00 23.25  ? 4206 GLU A CG    1 
ATOM   19631 C  CD    . GLU A 1 4206 ? 222.707 211.688 205.015 1.00 29.21  ? 4206 GLU A CD    1 
ATOM   19632 O  OE1   . GLU A 1 4206 ? 222.003 210.680 204.812 1.00 29.13  ? 4206 GLU A OE1   1 
ATOM   19633 O  OE2   . GLU A 1 4206 ? 223.579 211.739 205.907 1.00 32.61  ? 4206 GLU A OE2   1 
ATOM   19634 N  N     . PHE A 1 4207 ? 223.451 210.587 199.874 1.00 14.20  ? 4207 PHE A N     1 
ATOM   19635 C  CA    . PHE A 1 4207 ? 223.065 209.925 198.631 1.00 8.04   ? 4207 PHE A CA    1 
ATOM   19636 C  C     . PHE A 1 4207 ? 222.202 208.724 198.978 1.00 12.98  ? 4207 PHE A C     1 
ATOM   19637 O  O     . PHE A 1 4207 ? 222.707 207.670 199.371 1.00 16.59  ? 4207 PHE A O     1 
ATOM   19638 C  CB    . PHE A 1 4207 ? 224.300 209.507 197.842 1.00 7.94   ? 4207 PHE A CB    1 
ATOM   19639 C  CG    . PHE A 1 4207 ? 225.100 210.657 197.305 1.00 9.71   ? 4207 PHE A CG    1 
ATOM   19640 C  CD1   . PHE A 1 4207 ? 224.487 211.662 196.581 1.00 9.63   ? 4207 PHE A CD1   1 
ATOM   19641 C  CD2   . PHE A 1 4207 ? 226.461 210.733 197.527 1.00 8.82   ? 4207 PHE A CD2   1 
ATOM   19642 C  CE1   . PHE A 1 4207 ? 225.222 212.717 196.080 1.00 11.15  ? 4207 PHE A CE1   1 
ATOM   19643 C  CE2   . PHE A 1 4207 ? 227.201 211.784 197.025 1.00 10.62  ? 4207 PHE A CE2   1 
ATOM   19644 C  CZ    . PHE A 1 4207 ? 226.579 212.778 196.305 1.00 11.70  ? 4207 PHE A CZ    1 
ATOM   19645 N  N     . GLY A 1 4208 ? 220.889 208.877 198.838 1.00 12.58  ? 4208 GLY A N     1 
ATOM   19646 C  CA    . GLY A 1 4208 ? 219.976 207.855 199.302 1.00 11.18  ? 4208 GLY A CA    1 
ATOM   19647 C  C     . GLY A 1 4208 ? 218.994 207.347 198.270 1.00 9.74   ? 4208 GLY A C     1 
ATOM   19648 O  O     . GLY A 1 4208 ? 219.207 207.482 197.063 1.00 9.80   ? 4208 GLY A O     1 
ATOM   19649 N  N     . GLU A 1 4209 ? 217.898 206.762 198.755 1.00 12.43  ? 4209 GLU A N     1 
ATOM   19650 C  CA    . GLU A 1 4209 ? 216.951 206.082 197.880 1.00 17.81  ? 4209 GLU A CA    1 
ATOM   19651 C  C     . GLU A 1 4209 ? 216.091 207.077 197.106 1.00 14.56  ? 4209 GLU A C     1 
ATOM   19652 O  O     . GLU A 1 4209 ? 215.625 206.768 196.002 1.00 15.20  ? 4209 GLU A O     1 
ATOM   19653 C  CB    . GLU A 1 4209 ? 216.107 205.127 198.729 1.00 25.62  ? 4209 GLU A CB    1 
ATOM   19654 C  CG    . GLU A 1 4209 ? 215.217 204.146 197.984 1.00 34.82  ? 4209 GLU A CG    1 
ATOM   19655 C  CD    . GLU A 1 4209 ? 213.892 204.735 197.573 1.00 46.72  ? 4209 GLU A CD    1 
ATOM   19656 O  OE1   . GLU A 1 4209 ? 213.402 205.652 198.263 1.00 42.96  ? 4209 GLU A OE1   1 
ATOM   19657 O  OE2   . GLU A 1 4209 ? 213.324 204.249 196.574 1.00 48.62  ? 4209 GLU A OE2   1 
ATOM   19658 N  N     . SER A 1 4210 ? 215.884 208.276 197.660 1.00 12.95  ? 4210 SER A N     1 
ATOM   19659 C  CA    . SER A 1 4210 ? 215.137 209.308 196.947 1.00 11.63  ? 4210 SER A CA    1 
ATOM   19660 C  C     . SER A 1 4210 ? 215.880 209.764 195.698 1.00 9.58   ? 4210 SER A C     1 
ATOM   19661 O  O     . SER A 1 4210 ? 215.262 210.034 194.662 1.00 7.52   ? 4210 SER A O     1 
ATOM   19662 C  CB    . SER A 1 4210 ? 214.865 210.492 197.873 1.00 10.87  ? 4210 SER A CB    1 
ATOM   19663 O  OG    . SER A 1 4210 ? 216.024 210.837 198.610 1.00 15.92  ? 4210 SER A OG    1 
ATOM   19664 N  N     . ASP A 1 4211 ? 217.209 209.867 195.779 1.00 11.83  ? 4211 ASP A N     1 
ATOM   19665 C  CA    . ASP A 1 4211 ? 217.999 210.185 194.595 1.00 7.50   ? 4211 ASP A CA    1 
ATOM   19666 C  C     . ASP A 1 4211 ? 217.844 209.106 193.533 1.00 8.93   ? 4211 ASP A C     1 
ATOM   19667 O  O     . ASP A 1 4211 ? 217.759 209.408 192.337 1.00 12.88  ? 4211 ASP A O     1 
ATOM   19668 C  CB    . ASP A 1 4211 ? 219.469 210.359 194.970 1.00 8.91   ? 4211 ASP A CB    1 
ATOM   19669 C  CG    . ASP A 1 4211 ? 219.716 211.599 195.803 1.00 15.91  ? 4211 ASP A CG    1 
ATOM   19670 O  OD1   . ASP A 1 4211 ? 218.961 212.582 195.648 1.00 23.32  ? 4211 ASP A OD1   1 
ATOM   19671 O  OD2   . ASP A 1 4211 ? 220.667 211.594 196.610 1.00 16.99  ? 4211 ASP A OD2   1 
ATOM   19672 N  N     . LEU A 1 4212 ? 217.810 207.839 193.951 1.00 8.34   ? 4212 LEU A N     1 
ATOM   19673 C  CA    . LEU A 1 4212 ? 217.605 206.754 192.999 1.00 6.66   ? 4212 LEU A CA    1 
ATOM   19674 C  C     . LEU A 1 4212 ? 216.235 206.853 192.338 1.00 7.14   ? 4212 LEU A C     1 
ATOM   19675 O  O     . LEU A 1 4212 ? 216.113 206.666 191.122 1.00 10.69  ? 4212 LEU A O     1 
ATOM   19676 C  CB    . LEU A 1 4212 ? 217.776 205.405 193.696 1.00 8.85   ? 4212 LEU A CB    1 
ATOM   19677 C  CG    . LEU A 1 4212 ? 217.487 204.164 192.851 1.00 8.29   ? 4212 LEU A CG    1 
ATOM   19678 C  CD1   . LEU A 1 4212 ? 218.600 203.933 191.845 1.00 6.73   ? 4212 LEU A CD1   1 
ATOM   19679 C  CD2   . LEU A 1 4212 ? 217.307 202.947 193.739 1.00 10.09  ? 4212 LEU A CD2   1 
ATOM   19680 N  N     . ARG A 1 4213 ? 215.191 207.152 193.120 1.00 7.29   ? 4213 ARG A N     1 
ATOM   19681 C  CA    . ARG A 1 4213 ? 213.867 207.330 192.526 1.00 8.01   ? 4213 ARG A CA    1 
ATOM   19682 C  C     . ARG A 1 4213 ? 213.848 208.488 191.539 1.00 9.42   ? 4213 ARG A C     1 
ATOM   19683 O  O     . ARG A 1 4213 ? 213.251 208.383 190.461 1.00 14.61  ? 4213 ARG A O     1 
ATOM   19684 C  CB    . ARG A 1 4213 ? 212.806 207.551 193.603 1.00 14.04  ? 4213 ARG A CB    1 
ATOM   19685 C  CG    . ARG A 1 4213 ? 212.529 206.361 194.491 1.00 19.00  ? 4213 ARG A CG    1 
ATOM   19686 C  CD    . ARG A 1 4213 ? 211.433 206.695 195.491 1.00 38.57  ? 4213 ARG A CD    1 
ATOM   19687 N  NE    . ARG A 1 4213 ? 211.183 205.610 196.431 1.00 44.77  ? 4213 ARG A NE    1 
ATOM   19688 C  CZ    . ARG A 1 4213 ? 210.321 204.624 196.225 1.00 45.94  ? 4213 ARG A CZ    1 
ATOM   19689 N  NH1   . ARG A 1 4213 ? 209.603 204.554 195.115 1.00 58.38  ? 4213 ARG A NH1   1 
ATOM   19690 N  NH2   . ARG A 1 4213 ? 210.173 203.686 197.155 1.00 47.13  ? 4213 ARG A NH2   1 
ATOM   19691 N  N     . SER A 1 4214 ? 214.476 209.611 191.896 1.00 9.31   ? 4214 SER A N     1 
ATOM   19692 C  CA    . SER A 1 4214 ? 214.494 210.760 190.999 1.00 6.62   ? 4214 SER A CA    1 
ATOM   19693 C  C     . SER A 1 4214 ? 215.234 210.441 189.708 1.00 6.52   ? 4214 SER A C     1 
ATOM   19694 O  O     . SER A 1 4214 ? 214.792 210.821 188.618 1.00 8.45   ? 4214 SER A O     1 
ATOM   19695 C  CB    . SER A 1 4214 ? 215.123 211.964 191.700 1.00 7.26   ? 4214 SER A CB    1 
ATOM   19696 O  OG    . SER A 1 4214 ? 214.456 212.248 192.915 1.00 7.70   ? 4214 SER A OG    1 
ATOM   19697 N  N     . ALA A 1 4215 ? 216.363 209.736 189.811 1.00 8.09   ? 4215 ALA A N     1 
ATOM   19698 C  CA    . ALA A 1 4215 ? 217.107 209.352 188.617 1.00 6.57   ? 4215 ALA A CA    1 
ATOM   19699 C  C     . ALA A 1 4215 ? 216.304 208.392 187.748 1.00 7.54   ? 4215 ALA A C     1 
ATOM   19700 O  O     . ALA A 1 4215 ? 216.317 208.504 186.518 1.00 11.68  ? 4215 ALA A O     1 
ATOM   19701 C  CB    . ALA A 1 4215 ? 218.446 208.733 189.012 1.00 7.16   ? 4215 ALA A CB    1 
ATOM   19702 N  N     . CYS A 1 4216 ? 215.606 207.438 188.368 1.00 8.54   ? 4216 CYS A N     1 
ATOM   19703 C  CA    . CYS A 1 4216 ? 214.774 206.517 187.601 1.00 9.29   ? 4216 CYS A CA    1 
ATOM   19704 C  C     . CYS A 1 4216 ? 213.645 207.254 186.893 1.00 12.71  ? 4216 CYS A C     1 
ATOM   19705 O  O     . CYS A 1 4216 ? 213.340 206.966 185.730 1.00 15.08  ? 4216 CYS A O     1 
ATOM   19706 C  CB    . CYS A 1 4216 ? 214.214 205.430 188.518 1.00 13.50  ? 4216 CYS A CB    1 
ATOM   19707 S  SG    . CYS A 1 4216 ? 215.441 204.246 189.109 1.00 19.30  ? 4216 CYS A SG    1 
ATOM   19708 N  N     . ASP A 1 4217 ? 213.016 208.210 187.581 1.00 13.73  ? 4217 ASP A N     1 
ATOM   19709 C  CA    . ASP A 1 4217 ? 211.960 209.003 186.960 1.00 11.77  ? 4217 ASP A CA    1 
ATOM   19710 C  C     . ASP A 1 4217 ? 212.500 209.820 185.793 1.00 12.16  ? 4217 ASP A C     1 
ATOM   19711 O  O     . ASP A 1 4217 ? 211.852 209.922 184.744 1.00 16.27  ? 4217 ASP A O     1 
ATOM   19712 C  CB    . ASP A 1 4217 ? 211.312 209.918 187.997 1.00 11.66  ? 4217 ASP A CB    1 
ATOM   19713 C  CG    . ASP A 1 4217 ? 210.463 209.158 188.996 1.00 27.55  ? 4217 ASP A CG    1 
ATOM   19714 O  OD1   . ASP A 1 4217 ? 210.400 209.585 190.168 1.00 34.91  ? 4217 ASP A OD1   1 
ATOM   19715 O  OD2   . ASP A 1 4217 ? 209.857 208.137 188.610 1.00 29.33  ? 4217 ASP A OD2   1 
ATOM   19716 N  N     . THR A 1 4218 ? 213.683 210.416 185.961 1.00 9.97   ? 4218 THR A N     1 
ATOM   19717 C  CA    . THR A 1 4218 ? 214.295 211.176 184.876 1.00 8.78   ? 4218 THR A CA    1 
ATOM   19718 C  C     . THR A 1 4218 ? 214.594 210.284 183.679 1.00 11.06  ? 4218 THR A C     1 
ATOM   19719 O  O     . THR A 1 4218 ? 214.326 210.657 182.528 1.00 15.00  ? 4218 THR A O     1 
ATOM   19720 C  CB    . THR A 1 4218 ? 215.573 211.853 185.373 1.00 7.75   ? 4218 THR A CB    1 
ATOM   19721 O  OG1   . THR A 1 4218 ? 215.238 212.872 186.324 1.00 8.82   ? 4218 THR A OG1   1 
ATOM   19722 C  CG2   . THR A 1 4218 ? 216.341 212.474 184.218 1.00 9.29   ? 4218 THR A CG2   1 
ATOM   19723 N  N     . VAL A 1 4219 ? 215.149 209.097 183.932 1.00 12.81  ? 4219 VAL A N     1 
ATOM   19724 C  CA    . VAL A 1 4219 ? 215.456 208.167 182.850 1.00 13.47  ? 4219 VAL A CA    1 
ATOM   19725 C  C     . VAL A 1 4219 ? 214.182 207.778 182.117 1.00 17.31  ? 4219 VAL A C     1 
ATOM   19726 O  O     . VAL A 1 4219 ? 214.128 207.789 180.882 1.00 24.53  ? 4219 VAL A O     1 
ATOM   19727 C  CB    . VAL A 1 4219 ? 216.195 206.932 183.397 1.00 10.22  ? 4219 VAL A CB    1 
ATOM   19728 C  CG1   . VAL A 1 4219 ? 216.137 205.789 182.396 1.00 13.78  ? 4219 VAL A CG1   1 
ATOM   19729 C  CG2   . VAL A 1 4219 ? 217.634 207.279 183.727 1.00 10.88  ? 4219 VAL A CG2   1 
ATOM   19730 N  N     . ASP A 1 4220 ? 213.130 207.446 182.870 1.00 16.50  ? 4220 ASP A N     1 
ATOM   19731 C  CA    . ASP A 1 4220 ? 211.860 207.074 182.254 1.00 17.69  ? 4220 ASP A CA    1 
ATOM   19732 C  C     . ASP A 1 4220 ? 211.314 208.205 181.393 1.00 20.97  ? 4220 ASP A C     1 
ATOM   19733 O  O     . ASP A 1 4220 ? 210.940 207.991 180.235 1.00 29.43  ? 4220 ASP A O     1 
ATOM   19734 C  CB    . ASP A 1 4220 ? 210.850 206.691 183.335 1.00 22.75  ? 4220 ASP A CB    1 
ATOM   19735 C  CG    . ASP A 1 4220 ? 210.956 205.240 183.743 1.00 33.22  ? 4220 ASP A CG    1 
ATOM   19736 O  OD1   . ASP A 1 4220 ? 211.662 204.478 183.053 1.00 43.67  ? 4220 ASP A OD1   1 
ATOM   19737 O  OD2   . ASP A 1 4220 ? 210.334 204.863 184.757 1.00 33.41  ? 4220 ASP A OD2   1 
ATOM   19738 N  N     . THR A 1 4221 ? 211.276 209.422 181.941 1.00 17.24  ? 4221 THR A N     1 
ATOM   19739 C  CA    . THR A 1 4221 ? 210.701 210.549 181.214 1.00 19.89  ? 4221 THR A CA    1 
ATOM   19740 C  C     . THR A 1 4221 ? 211.468 210.825 179.929 1.00 17.79  ? 4221 THR A C     1 
ATOM   19741 O  O     . THR A 1 4221 ? 210.872 210.966 178.855 1.00 24.04  ? 4221 THR A O     1 
ATOM   19742 C  CB    . THR A 1 4221 ? 210.680 211.793 182.104 1.00 17.28  ? 4221 THR A CB    1 
ATOM   19743 O  OG1   . THR A 1 4221 ? 209.808 211.574 183.219 1.00 28.69  ? 4221 THR A OG1   1 
ATOM   19744 C  CG2   . THR A 1 4221 ? 210.193 213.000 181.319 1.00 13.84  ? 4221 THR A CG2   1 
ATOM   19745 N  N     . TRP A 1 4222 ? 212.799 210.887 180.012 1.00 16.19  ? 4222 TRP A N     1 
ATOM   19746 C  CA    . TRP A 1 4222 ? 213.571 211.258 178.833 1.00 15.94  ? 4222 TRP A CA    1 
ATOM   19747 C  C     . TRP A 1 4222 ? 213.615 210.135 177.803 1.00 19.72  ? 4222 TRP A C     1 
ATOM   19748 O  O     . TRP A 1 4222 ? 213.614 210.409 176.597 1.00 24.92  ? 4222 TRP A O     1 
ATOM   19749 C  CB    . TRP A 1 4222 ? 214.975 211.693 179.244 1.00 11.69  ? 4222 TRP A CB    1 
ATOM   19750 C  CG    . TRP A 1 4222 ? 214.979 213.093 179.753 1.00 10.01  ? 4222 TRP A CG    1 
ATOM   19751 C  CD1   . TRP A 1 4222 ? 214.932 213.491 181.055 1.00 10.26  ? 4222 TRP A CD1   1 
ATOM   19752 C  CD2   . TRP A 1 4222 ? 214.993 214.291 178.968 1.00 13.12  ? 4222 TRP A CD2   1 
ATOM   19753 N  NE1   . TRP A 1 4222 ? 214.930 214.862 181.131 1.00 12.95  ? 4222 TRP A NE1   1 
ATOM   19754 C  CE2   . TRP A 1 4222 ? 214.968 215.377 179.863 1.00 12.02  ? 4222 TRP A CE2   1 
ATOM   19755 C  CE3   . TRP A 1 4222 ? 215.033 214.550 177.595 1.00 14.04  ? 4222 TRP A CE3   1 
ATOM   19756 C  CZ2   . TRP A 1 4222 ? 214.981 216.699 179.430 1.00 13.85  ? 4222 TRP A CZ2   1 
ATOM   19757 C  CZ3   . TRP A 1 4222 ? 215.047 215.863 177.168 1.00 11.14  ? 4222 TRP A CZ3   1 
ATOM   19758 C  CH2   . TRP A 1 4222 ? 215.022 216.921 178.082 1.00 13.78  ? 4222 TRP A CH2   1 
ATOM   19759 N  N     . LEU A 1 4223 ? 213.640 208.875 178.244 1.00 20.09  ? 4223 LEU A N     1 
ATOM   19760 C  CA    . LEU A 1 4223 ? 213.566 207.770 177.298 1.00 22.11  ? 4223 LEU A CA    1 
ATOM   19761 C  C     . LEU A 1 4223 ? 212.222 207.747 176.585 1.00 27.18  ? 4223 LEU A C     1 
ATOM   19762 O  O     . LEU A 1 4223 ? 212.164 207.534 175.368 1.00 31.45  ? 4223 LEU A O     1 
ATOM   19763 C  CB    . LEU A 1 4223 ? 213.814 206.446 178.018 1.00 22.65  ? 4223 LEU A CB    1 
ATOM   19764 C  CG    . LEU A 1 4223 ? 214.349 205.315 177.144 1.00 28.36  ? 4223 LEU A CG    1 
ATOM   19765 C  CD1   . LEU A 1 4223 ? 215.479 205.819 176.266 1.00 30.64  ? 4223 LEU A CD1   1 
ATOM   19766 C  CD2   . LEU A 1 4223 ? 214.809 204.156 177.999 1.00 25.45  ? 4223 LEU A CD2   1 
ATOM   19767 N  N     . ASP A 1 4224 ? 211.128 207.968 177.321 1.00 25.28  ? 4224 ASP A N     1 
ATOM   19768 C  CA    . ASP A 1 4224 ? 209.814 208.010 176.693 1.00 23.54  ? 4224 ASP A CA    1 
ATOM   19769 C  C     . ASP A 1 4224 ? 209.707 209.176 175.721 1.00 33.40  ? 4224 ASP A C     1 
ATOM   19770 O  O     . ASP A 1 4224 ? 209.086 209.053 174.659 1.00 40.82  ? 4224 ASP A O     1 
ATOM   19771 C  CB    . ASP A 1 4224 ? 208.725 208.098 177.763 1.00 31.49  ? 4224 ASP A CB    1 
ATOM   19772 C  CG    . ASP A 1 4224 ? 208.624 206.835 178.595 1.00 42.00  ? 4224 ASP A CG    1 
ATOM   19773 O  OD1   . ASP A 1 4224 ? 209.252 205.824 178.220 1.00 47.27  ? 4224 ASP A OD1   1 
ATOM   19774 O  OD2   . ASP A 1 4224 ? 207.918 206.854 179.625 1.00 40.40  ? 4224 ASP A OD2   1 
ATOM   19775 N  N     . ASP A 1 4225 ? 210.295 210.322 176.070 1.00 33.70  ? 4225 ASP A N     1 
ATOM   19776 C  CA    . ASP A 1 4225 ? 210.296 211.457 175.155 1.00 29.31  ? 4225 ASP A CA    1 
ATOM   19777 C  C     . ASP A 1 4225 ? 211.070 211.134 173.882 1.00 31.66  ? 4225 ASP A C     1 
ATOM   19778 O  O     . ASP A 1 4225 ? 210.614 211.433 172.773 1.00 43.11  ? 4225 ASP A O     1 
ATOM   19779 C  CB    . ASP A 1 4225 ? 210.883 212.689 175.845 1.00 30.22  ? 4225 ASP A CB    1 
ATOM   19780 C  CG    . ASP A 1 4225 ? 210.950 213.892 174.928 1.00 44.68  ? 4225 ASP A CG    1 
ATOM   19781 O  OD1   . ASP A 1 4225 ? 209.906 214.257 174.350 1.00 46.00  ? 4225 ASP A OD1   1 
ATOM   19782 O  OD2   . ASP A 1 4225 ? 212.046 214.473 174.783 1.00 48.67  ? 4225 ASP A OD2   1 
ATOM   19783 N  N     . THR A 1 4226 ? 212.244 210.517 174.023 1.00 31.40  ? 4226 THR A N     1 
ATOM   19784 C  CA    . THR A 1 4226 ? 213.051 210.208 172.846 1.00 32.41  ? 4226 THR A CA    1 
ATOM   19785 C  C     . THR A 1 4226 ? 212.460 209.045 172.058 1.00 35.78  ? 4226 THR A C     1 
ATOM   19786 O  O     . THR A 1 4226 ? 212.455 209.064 170.821 1.00 40.88  ? 4226 THR A O     1 
ATOM   19787 C  CB    . THR A 1 4226 ? 214.491 209.909 173.266 1.00 35.09  ? 4226 THR A CB    1 
ATOM   19788 O  OG1   . THR A 1 4226 ? 215.148 211.134 173.615 1.00 38.06  ? 4226 THR A OG1   1 
ATOM   19789 C  CG2   . THR A 1 4226 ? 215.260 209.239 172.140 1.00 33.08  ? 4226 THR A CG2   1 
ATOM   19790 N  N     . ALA A 1 4227 ? 211.934 208.038 172.750 1.00 38.53  ? 4227 ALA A N     1 
ATOM   19791 C  CA    . ALA A 1 4227 ? 211.370 206.849 172.114 1.00 36.85  ? 4227 ALA A CA    1 
ATOM   19792 C  C     . ALA A 1 4227 ? 209.850 206.921 172.211 1.00 50.42  ? 4227 ALA A C     1 
ATOM   19793 O  O     . ALA A 1 4227 ? 209.271 206.638 173.263 1.00 54.69  ? 4227 ALA A O     1 
ATOM   19794 C  CB    . ALA A 1 4227 ? 211.908 205.580 172.765 1.00 38.56  ? 4227 ALA A CB    1 
ATOM   19795 N  N     . LYS A 1 4228 ? 209.201 207.289 171.105 1.00 50.78  ? 4228 LYS A N     1 
ATOM   19796 C  CA    . LYS A 1 4228 ? 207.741 207.373 171.051 1.00 51.24  ? 4228 LYS A CA    1 
ATOM   19797 C  C     . LYS A 1 4228 ? 207.151 205.970 170.895 1.00 49.08  ? 4228 LYS A C     1 
ATOM   19798 O  O     . LYS A 1 4228 ? 206.481 205.635 169.916 1.00 51.88  ? 4228 LYS A O     1 
ATOM   19799 C  CB    . LYS A 1 4228 ? 207.294 208.287 169.918 1.00 51.57  ? 4228 LYS A CB    1 
ATOM   19800 C  CG    . LYS A 1 4228 ? 207.779 209.723 170.018 1.00 50.26  ? 4228 LYS A CG    1 
ATOM   19801 C  CD    . LYS A 1 4228 ? 207.171 210.423 171.221 1.00 53.00  ? 4228 LYS A CD    1 
ATOM   19802 C  CE    . LYS A 1 4228 ? 207.512 211.905 171.230 1.00 50.16  ? 4228 LYS A CE    1 
ATOM   19803 N  NZ    . LYS A 1 4228 ? 208.951 212.157 171.492 1.00 43.99  ? 4228 LYS A NZ    1 
ATOM   19804 N  N     . GLY A 1 4229 ? 207.415 205.136 171.899 1.00 49.26  ? 4229 GLY A N     1 
ATOM   19805 C  CA    . GLY A 1 4229 ? 206.890 203.789 171.925 1.00 50.14  ? 4229 GLY A CA    1 
ATOM   19806 C  C     . GLY A 1 4229 ? 207.615 202.794 171.048 1.00 51.83  ? 4229 GLY A C     1 
ATOM   19807 O  O     . GLY A 1 4229 ? 207.179 201.639 170.967 1.00 56.86  ? 4229 GLY A O     1 
ATOM   19808 N  N     . ARG A 1 4230 ? 208.696 203.196 170.386 1.00 49.24  ? 4230 ARG A N     1 
ATOM   19809 C  CA    . ARG A 1 4230 ? 209.440 202.273 169.542 1.00 46.92  ? 4230 ARG A CA    1 
ATOM   19810 C  C     . ARG A 1 4230 ? 210.074 201.175 170.385 1.00 55.31  ? 4230 ARG A C     1 
ATOM   19811 O  O     . ARG A 1 4230 ? 210.582 201.423 171.481 1.00 57.44  ? 4230 ARG A O     1 
ATOM   19812 C  CB    . ARG A 1 4230 ? 210.516 203.018 168.754 1.00 50.55  ? 4230 ARG A CB    1 
ATOM   19813 C  CG    . ARG A 1 4230 ? 209.985 204.151 167.896 1.00 49.03  ? 4230 ARG A CG    1 
ATOM   19814 C  CD    . ARG A 1 4230 ? 210.970 204.511 166.798 1.00 52.42  ? 4230 ARG A CD    1 
ATOM   19815 N  NE    . ARG A 1 4230 ? 212.321 204.702 167.313 1.00 57.11  ? 4230 ARG A NE    1 
ATOM   19816 C  CZ    . ARG A 1 4230 ? 213.142 205.665 166.921 1.00 69.50  ? 4230 ARG A CZ    1 
ATOM   19817 N  NH1   . ARG A 1 4230 ? 212.781 206.551 166.007 1.00 70.06  ? 4230 ARG A NH1   1 
ATOM   19818 N  NH2   . ARG A 1 4230 ? 214.357 205.743 167.459 1.00 65.00  ? 4230 ARG A NH2   1 
ATOM   19819 N  N     . GLN A 1 4231 ? 210.035 199.947 169.862 1.00 57.00  ? 4231 GLN A N     1 
ATOM   19820 C  CA    . GLN A 1 4231 ? 210.572 198.808 170.600 1.00 52.85  ? 4231 GLN A CA    1 
ATOM   19821 C  C     . GLN A 1 4231 ? 212.074 198.935 170.824 1.00 54.55  ? 4231 GLN A C     1 
ATOM   19822 O  O     . GLN A 1 4231 ? 212.564 198.614 171.911 1.00 52.01  ? 4231 GLN A O     1 
ATOM   19823 C  CB    . GLN A 1 4231 ? 210.253 197.508 169.862 1.00 51.60  ? 4231 GLN A CB    1 
ATOM   19824 C  CG    . GLN A 1 4231 ? 210.705 196.252 170.589 1.00 55.75  ? 4231 GLN A CG    1 
ATOM   19825 C  CD    . GLN A 1 4231 ? 209.950 196.022 171.883 1.00 66.80  ? 4231 GLN A CD    1 
ATOM   19826 O  OE1   . GLN A 1 4231 ? 208.736 196.218 171.953 1.00 65.17  ? 4231 GLN A OE1   1 
ATOM   19827 N  NE2   . GLN A 1 4231 ? 210.668 195.602 172.919 1.00 65.26  ? 4231 GLN A NE2   1 
ATOM   19828 N  N     . ASN A 1 4232 ? 212.814 199.395 169.819 1.00 50.36  ? 4232 ASN A N     1 
ATOM   19829 C  CA    . ASN A 1 4232 ? 214.260 199.520 169.904 1.00 46.21  ? 4232 ASN A CA    1 
ATOM   19830 C  C     . ASN A 1 4232 ? 214.690 200.893 169.415 1.00 47.79  ? 4232 ASN A C     1 
ATOM   19831 O  O     . ASN A 1 4232 ? 214.113 201.433 168.467 1.00 52.58  ? 4232 ASN A O     1 
ATOM   19832 C  CB    . ASN A 1 4232 ? 214.959 198.433 169.080 1.00 43.81  ? 4232 ASN A CB    1 
ATOM   19833 C  CG    . ASN A 1 4232 ? 214.814 197.056 169.692 1.00 45.83  ? 4232 ASN A CG    1 
ATOM   19834 O  OD1   . ASN A 1 4232 ? 214.764 196.908 170.912 1.00 51.96  ? 4232 ASN A OD1   1 
ATOM   19835 N  ND2   . ASN A 1 4232 ? 214.746 196.036 168.844 1.00 48.85  ? 4232 ASN A ND2   1 
ATOM   19836 N  N     . ILE A 1 4233 ? 215.706 201.455 170.065 1.00 44.08  ? 4233 ILE A N     1 
ATOM   19837 C  CA    . ILE A 1 4233 ? 216.316 202.712 169.653 1.00 40.30  ? 4233 ILE A CA    1 
ATOM   19838 C  C     . ILE A 1 4233 ? 217.825 202.525 169.642 1.00 38.37  ? 4233 ILE A C     1 
ATOM   19839 O  O     . ILE A 1 4233 ? 218.354 201.675 170.368 1.00 41.10  ? 4233 ILE A O     1 
ATOM   19840 C  CB    . ILE A 1 4233 ? 215.926 203.880 170.579 1.00 46.05  ? 4233 ILE A CB    1 
ATOM   19841 C  CG1   . ILE A 1 4233 ? 216.422 203.624 172.002 1.00 40.75  ? 4233 ILE A CG1   1 
ATOM   19842 C  CG2   . ILE A 1 4233 ? 214.422 204.099 170.568 1.00 44.52  ? 4233 ILE A CG2   1 
ATOM   19843 C  CD1   . ILE A 1 4233 ? 216.286 204.817 172.907 1.00 35.00  ? 4233 ILE A CD1   1 
ATOM   19844 N  N     . SER A 1 4234 ? 218.512 203.307 168.820 1.00 35.05  ? 4234 SER A N     1 
ATOM   19845 C  CA    . SER A 1 4234 ? 219.961 203.218 168.765 1.00 32.37  ? 4234 SER A CA    1 
ATOM   19846 C  C     . SER A 1 4234 ? 220.565 203.801 170.040 1.00 35.42  ? 4234 SER A C     1 
ATOM   19847 O  O     . SER A 1 4234 ? 220.013 204.747 170.612 1.00 35.57  ? 4234 SER A O     1 
ATOM   19848 C  CB    . SER A 1 4234 ? 220.501 203.957 167.540 1.00 35.56  ? 4234 SER A CB    1 
ATOM   19849 O  OG    . SER A 1 4234 ? 221.918 203.947 167.523 1.00 37.36  ? 4234 SER A OG    1 
ATOM   19850 N  N     . PRO A 1 4235 ? 221.685 203.255 170.520 1.00 34.84  ? 4235 PRO A N     1 
ATOM   19851 C  CA    . PRO A 1 4235 ? 222.341 203.851 171.695 1.00 32.83  ? 4235 PRO A CA    1 
ATOM   19852 C  C     . PRO A 1 4235 ? 222.756 205.295 171.485 1.00 30.04  ? 4235 PRO A C     1 
ATOM   19853 O  O     . PRO A 1 4235 ? 222.784 206.069 172.448 1.00 26.36  ? 4235 PRO A O     1 
ATOM   19854 C  CB    . PRO A 1 4235 ? 223.554 202.938 171.915 1.00 29.78  ? 4235 PRO A CB    1 
ATOM   19855 C  CG    . PRO A 1 4235 ? 223.167 201.643 171.292 1.00 31.12  ? 4235 PRO A CG    1 
ATOM   19856 C  CD    . PRO A 1 4235 ? 222.328 201.998 170.105 1.00 33.02  ? 4235 PRO A CD    1 
ATOM   19857 N  N     . ASP A 1 4236 ? 223.086 205.682 170.251 1.00 31.75  ? 4236 ASP A N     1 
ATOM   19858 C  CA    . ASP A 1 4236 ? 223.466 207.064 169.988 1.00 29.08  ? 4236 ASP A CA    1 
ATOM   19859 C  C     . ASP A 1 4236 ? 222.271 208.003 170.070 1.00 31.41  ? 4236 ASP A C     1 
ATOM   19860 O  O     . ASP A 1 4236 ? 222.444 209.206 170.295 1.00 33.18  ? 4236 ASP A O     1 
ATOM   19861 C  CB    . ASP A 1 4236 ? 224.134 207.168 168.618 1.00 32.53  ? 4236 ASP A CB    1 
ATOM   19862 C  CG    . ASP A 1 4236 ? 225.430 206.388 168.546 1.00 41.39  ? 4236 ASP A CG    1 
ATOM   19863 O  OD1   . ASP A 1 4236 ? 225.369 205.143 168.469 1.00 37.60  ? 4236 ASP A OD1   1 
ATOM   19864 O  OD2   . ASP A 1 4236 ? 226.508 207.018 168.567 1.00 48.22  ? 4236 ASP A OD2   1 
ATOM   19865 N  N     . LYS A 1 4237 ? 221.057 207.479 169.892 1.00 30.66  ? 4237 LYS A N     1 
ATOM   19866 C  CA    . LYS A 1 4237 ? 219.851 208.290 169.989 1.00 24.99  ? 4237 LYS A CA    1 
ATOM   19867 C  C     . LYS A 1 4237 ? 219.389 208.504 171.424 1.00 29.28  ? 4237 LYS A C     1 
ATOM   19868 O  O     . LYS A 1 4237 ? 218.511 209.342 171.652 1.00 40.60  ? 4237 LYS A O     1 
ATOM   19869 C  CB    . LYS A 1 4237 ? 218.722 207.648 169.179 1.00 31.36  ? 4237 LYS A CB    1 
ATOM   19870 C  CG    . LYS A 1 4237 ? 218.969 207.610 167.680 1.00 34.21  ? 4237 LYS A CG    1 
ATOM   19871 C  CD    . LYS A 1 4237 ? 219.613 208.894 167.187 1.00 33.00  ? 4237 LYS A CD    1 
ATOM   19872 C  CE    . LYS A 1 4237 ? 219.391 209.080 165.697 1.00 31.91  ? 4237 LYS A CE    1 
ATOM   19873 N  NZ    . LYS A 1 4237 ? 217.952 208.959 165.337 1.00 31.92  ? 4237 LYS A NZ    1 
ATOM   19874 N  N     . ILE A 1 4238 ? 219.943 207.773 172.382 1.00 25.30  ? 4238 ILE A N     1 
ATOM   19875 C  CA    . ILE A 1 4238 ? 219.562 207.950 173.788 1.00 18.57  ? 4238 ILE A CA    1 
ATOM   19876 C  C     . ILE A 1 4238 ? 220.001 209.334 174.254 1.00 17.30  ? 4238 ILE A C     1 
ATOM   19877 O  O     . ILE A 1 4238 ? 221.151 209.734 173.998 1.00 19.78  ? 4238 ILE A O     1 
ATOM   19878 C  CB    . ILE A 1 4238 ? 220.190 206.854 174.650 1.00 18.98  ? 4238 ILE A CB    1 
ATOM   19879 C  CG1   . ILE A 1 4238 ? 219.779 205.472 174.140 1.00 24.54  ? 4238 ILE A CG1   1 
ATOM   19880 C  CG2   . ILE A 1 4238 ? 219.795 207.022 176.109 1.00 16.90  ? 4238 ILE A CG2   1 
ATOM   19881 C  CD1   . ILE A 1 4238 ? 220.251 204.332 175.017 1.00 19.71  ? 4238 ILE A CD1   1 
ATOM   19882 N  N     . PRO A 1 4239 ? 219.142 210.100 174.929 1.00 18.28  ? 4239 PRO A N     1 
ATOM   19883 C  CA    . PRO A 1 4239 ? 219.556 211.426 175.406 1.00 16.02  ? 4239 PRO A CA    1 
ATOM   19884 C  C     . PRO A 1 4239 ? 220.556 211.343 176.548 1.00 12.21  ? 4239 PRO A C     1 
ATOM   19885 O  O     . PRO A 1 4239 ? 220.208 211.571 177.710 1.00 12.51  ? 4239 PRO A O     1 
ATOM   19886 C  CB    . PRO A 1 4239 ? 218.237 212.064 175.855 1.00 18.94  ? 4239 PRO A CB    1 
ATOM   19887 C  CG    . PRO A 1 4239 ? 217.360 210.909 176.192 1.00 16.49  ? 4239 PRO A CG    1 
ATOM   19888 C  CD    . PRO A 1 4239 ? 217.727 209.820 175.228 1.00 19.37  ? 4239 PRO A CD    1 
ATOM   19889 N  N     . TRP A 1 4240 ? 221.806 211.008 176.219 1.00 13.92  ? 4240 TRP A N     1 
ATOM   19890 C  CA    . TRP A 1 4240 ? 222.837 210.874 177.244 1.00 11.28  ? 4240 TRP A CA    1 
ATOM   19891 C  C     . TRP A 1 4240 ? 223.135 212.205 177.919 1.00 9.66   ? 4240 TRP A C     1 
ATOM   19892 O  O     . TRP A 1 4240 ? 223.313 212.259 179.141 1.00 8.52   ? 4240 TRP A O     1 
ATOM   19893 C  CB    . TRP A 1 4240 ? 224.109 210.295 176.628 1.00 12.06  ? 4240 TRP A CB    1 
ATOM   19894 C  CG    . TRP A 1 4240 ? 223.948 208.902 176.124 1.00 13.79  ? 4240 TRP A CG    1 
ATOM   19895 C  CD1   . TRP A 1 4240 ? 223.914 208.500 174.823 1.00 14.76  ? 4240 TRP A CD1   1 
ATOM   19896 C  CD2   . TRP A 1 4240 ? 223.812 207.717 176.914 1.00 17.22  ? 4240 TRP A CD2   1 
ATOM   19897 N  NE1   . TRP A 1 4240 ? 223.758 207.139 174.751 1.00 19.62  ? 4240 TRP A NE1   1 
ATOM   19898 C  CE2   . TRP A 1 4240 ? 223.694 206.634 176.023 1.00 16.52  ? 4240 TRP A CE2   1 
ATOM   19899 C  CE3   . TRP A 1 4240 ? 223.776 207.466 178.288 1.00 16.31  ? 4240 TRP A CE3   1 
ATOM   19900 C  CZ2   . TRP A 1 4240 ? 223.541 205.323 176.461 1.00 17.61  ? 4240 TRP A CZ2   1 
ATOM   19901 C  CZ3   . TRP A 1 4240 ? 223.625 206.164 178.719 1.00 11.78  ? 4240 TRP A CZ3   1 
ATOM   19902 C  CH2   . TRP A 1 4240 ? 223.511 205.110 177.810 1.00 15.24  ? 4240 TRP A CH2   1 
ATOM   19903 N  N     . SER A 1 4241 ? 223.204 213.285 177.138 1.00 12.55  ? 4241 SER A N     1 
ATOM   19904 C  CA    . SER A 1 4241 ? 223.544 214.589 177.700 1.00 9.10   ? 4241 SER A CA    1 
ATOM   19905 C  C     . SER A 1 4241 ? 222.498 215.048 178.705 1.00 8.83   ? 4241 SER A C     1 
ATOM   19906 O  O     . SER A 1 4241 ? 222.839 215.577 179.769 1.00 8.08   ? 4241 SER A O     1 
ATOM   19907 C  CB    . SER A 1 4241 ? 223.698 215.616 176.582 1.00 12.32  ? 4241 SER A CB    1 
ATOM   19908 O  OG    . SER A 1 4241 ? 222.495 215.743 175.843 1.00 31.13  ? 4241 SER A OG    1 
ATOM   19909 N  N     . ALA A 1 4242 ? 221.217 214.851 178.387 1.00 10.35  ? 4242 ALA A N     1 
ATOM   19910 C  CA    . ALA A 1 4242 ? 220.152 215.255 179.299 1.00 7.41   ? 4242 ALA A CA    1 
ATOM   19911 C  C     . ALA A 1 4242 ? 220.260 214.516 180.626 1.00 8.10   ? 4242 ALA A C     1 
ATOM   19912 O  O     . ALA A 1 4242 ? 220.197 215.129 181.699 1.00 9.29   ? 4242 ALA A O     1 
ATOM   19913 C  CB    . ALA A 1 4242 ? 218.790 215.000 178.654 1.00 7.49   ? 4242 ALA A CB    1 
ATOM   19914 N  N     . LEU A 1 4243 ? 220.434 213.195 180.569 1.00 9.47   ? 4243 LEU A N     1 
ATOM   19915 C  CA    . LEU A 1 4243 ? 220.533 212.403 181.790 1.00 8.23   ? 4243 LEU A CA    1 
ATOM   19916 C  C     . LEU A 1 4243 ? 221.760 212.793 182.599 1.00 8.65   ? 4243 LEU A C     1 
ATOM   19917 O  O     . LEU A 1 4243 ? 221.678 212.962 183.822 1.00 11.72  ? 4243 LEU A O     1 
ATOM   19918 C  CB    . LEU A 1 4243 ? 220.569 210.915 181.444 1.00 7.55   ? 4243 LEU A CB    1 
ATOM   19919 C  CG    . LEU A 1 4243 ? 219.330 210.368 180.736 1.00 7.96   ? 4243 LEU A CG    1 
ATOM   19920 C  CD1   . LEU A 1 4243 ? 219.617 209.004 180.130 1.00 17.54  ? 4243 LEU A CD1   1 
ATOM   19921 C  CD2   . LEU A 1 4243 ? 218.151 210.303 181.686 1.00 9.02   ? 4243 LEU A CD2   1 
ATOM   19922 N  N     . LYS A 1 4244 ? 222.905 212.951 181.932 1.00 8.17   ? 4244 LYS A N     1 
ATOM   19923 C  CA    . LYS A 1 4244 ? 224.133 213.300 182.637 1.00 6.80   ? 4244 LYS A CA    1 
ATOM   19924 C  C     . LYS A 1 4244 ? 224.011 214.657 183.314 1.00 7.44   ? 4244 LYS A C     1 
ATOM   19925 O  O     . LYS A 1 4244 ? 224.388 214.818 184.479 1.00 10.77  ? 4244 LYS A O     1 
ATOM   19926 C  CB    . LYS A 1 4244 ? 225.317 213.284 181.672 1.00 8.66   ? 4244 LYS A CB    1 
ATOM   19927 C  CG    . LYS A 1 4244 ? 225.809 211.897 181.318 1.00 8.75   ? 4244 LYS A CG    1 
ATOM   19928 C  CD    . LYS A 1 4244 ? 227.180 211.951 180.671 1.00 8.99   ? 4244 LYS A CD    1 
ATOM   19929 C  CE    . LYS A 1 4244 ? 227.149 212.752 179.384 1.00 8.62   ? 4244 LYS A CE    1 
ATOM   19930 N  NZ    . LYS A 1 4244 ? 228.462 212.726 178.688 1.00 19.39  ? 4244 LYS A NZ    1 
ATOM   19931 N  N     . THR A 1 4245 ? 223.472 215.650 182.601 1.00 7.13   ? 4245 THR A N     1 
ATOM   19932 C  CA    . THR A 1 4245 ? 223.336 216.981 183.181 1.00 6.26   ? 4245 THR A CA    1 
ATOM   19933 C  C     . THR A 1 4245 ? 222.343 216.986 184.335 1.00 7.91   ? 4245 THR A C     1 
ATOM   19934 O  O     . THR A 1 4245 ? 222.605 217.593 185.380 1.00 7.98   ? 4245 THR A O     1 
ATOM   19935 C  CB    . THR A 1 4245 ? 222.914 217.982 182.107 1.00 7.79   ? 4245 THR A CB    1 
ATOM   19936 O  OG1   . THR A 1 4245 ? 223.740 217.819 180.948 1.00 9.43   ? 4245 THR A OG1   1 
ATOM   19937 C  CG2   . THR A 1 4245 ? 223.055 219.404 182.621 1.00 8.22   ? 4245 THR A CG2   1 
ATOM   19938 N  N     . LEU A 1 4246 ? 221.202 216.310 184.177 1.00 6.46   ? 4246 LEU A N     1 
ATOM   19939 C  CA    . LEU A 1 4246 ? 220.208 216.312 185.242 1.00 6.26   ? 4246 LEU A CA    1 
ATOM   19940 C  C     . LEU A 1 4246 ? 220.701 215.568 186.475 1.00 7.20   ? 4246 LEU A C     1 
ATOM   19941 O  O     . LEU A 1 4246 ? 220.350 215.941 187.599 1.00 13.14  ? 4246 LEU A O     1 
ATOM   19942 C  CB    . LEU A 1 4246 ? 218.893 215.717 184.741 1.00 7.97   ? 4246 LEU A CB    1 
ATOM   19943 C  CG    . LEU A 1 4246 ? 218.003 216.687 183.960 1.00 6.24   ? 4246 LEU A CG    1 
ATOM   19944 C  CD1   . LEU A 1 4246 ? 216.668 216.056 183.646 1.00 8.31   ? 4246 LEU A CD1   1 
ATOM   19945 C  CD2   . LEU A 1 4246 ? 217.810 217.980 184.734 1.00 5.47   ? 4246 LEU A CD2   1 
ATOM   19946 N  N     . MET A 1 4247 ? 221.508 214.521 186.296 1.00 6.93   ? 4247 MET A N     1 
ATOM   19947 C  CA    . MET A 1 4247 ? 222.063 213.830 187.452 1.00 6.17   ? 4247 MET A CA    1 
ATOM   19948 C  C     . MET A 1 4247 ? 223.217 214.595 188.086 1.00 8.45   ? 4247 MET A C     1 
ATOM   19949 O  O     . MET A 1 4247 ? 223.402 214.520 189.306 1.00 11.27  ? 4247 MET A O     1 
ATOM   19950 C  CB    . MET A 1 4247 ? 222.512 212.424 187.059 1.00 8.56   ? 4247 MET A CB    1 
ATOM   19951 C  CG    . MET A 1 4247 ? 221.370 211.503 186.675 1.00 8.77   ? 4247 MET A CG    1 
ATOM   19952 S  SD    . MET A 1 4247 ? 221.955 209.890 186.145 1.00 34.77  ? 4247 MET A SD    1 
ATOM   19953 C  CE    . MET A 1 4247 ? 222.524 209.244 187.710 1.00 17.06  ? 4247 MET A CE    1 
ATOM   19954 N  N     . ALA A 1 4248 ? 224.002 215.326 187.293 1.00 8.34   ? 4248 ALA A N     1 
ATOM   19955 C  CA    . ALA A 1 4248 ? 225.132 216.070 187.828 1.00 5.90   ? 4248 ALA A CA    1 
ATOM   19956 C  C     . ALA A 1 4248 ? 224.742 217.418 188.414 1.00 8.34   ? 4248 ALA A C     1 
ATOM   19957 O  O     . ALA A 1 4248 ? 225.544 218.010 189.143 1.00 13.58  ? 4248 ALA A O     1 
ATOM   19958 C  CB    . ALA A 1 4248 ? 226.184 216.281 186.738 1.00 5.90   ? 4248 ALA A CB    1 
ATOM   19959 N  N     . GLN A 1 4249 ? 223.545 217.917 188.121 1.00 8.75   ? 4249 GLN A N     1 
ATOM   19960 C  CA    . GLN A 1 4249 ? 223.139 219.233 188.584 1.00 6.46   ? 4249 GLN A CA    1 
ATOM   19961 C  C     . GLN A 1 4249 ? 221.917 219.225 189.487 1.00 8.04   ? 4249 GLN A C     1 
ATOM   19962 O  O     . GLN A 1 4249 ? 221.817 220.085 190.362 1.00 11.57  ? 4249 GLN A O     1 
ATOM   19963 C  CB    . GLN A 1 4249 ? 222.862 220.157 187.388 1.00 6.73   ? 4249 GLN A CB    1 
ATOM   19964 C  CG    . GLN A 1 4249 ? 224.012 220.251 186.401 1.00 6.07   ? 4249 GLN A CG    1 
ATOM   19965 C  CD    . GLN A 1 4249 ? 224.887 221.461 186.634 1.00 8.63   ? 4249 GLN A CD    1 
ATOM   19966 O  OE1   . GLN A 1 4249 ? 224.489 222.592 186.359 1.00 9.40   ? 4249 GLN A OE1   1 
ATOM   19967 N  NE2   . GLN A 1 4249 ? 226.090 221.229 187.143 1.00 9.30   ? 4249 GLN A NE2   1 
ATOM   19968 N  N     . SER A 1 4250 ? 220.992 218.285 189.307 1.00 8.00   ? 4250 SER A N     1 
ATOM   19969 C  CA    . SER A 1 4250 ? 219.725 218.301 190.030 1.00 5.87   ? 4250 SER A CA    1 
ATOM   19970 C  C     . SER A 1 4250 ? 219.549 217.112 190.961 1.00 8.21   ? 4250 SER A C     1 
ATOM   19971 O  O     . SER A 1 4250 ? 219.220 217.300 192.137 1.00 12.57  ? 4250 SER A O     1 
ATOM   19972 C  CB    . SER A 1 4250 ? 218.556 218.363 189.036 1.00 6.06   ? 4250 SER A CB    1 
ATOM   19973 O  OG    . SER A 1 4250 ? 218.783 219.348 188.045 1.00 8.77   ? 4250 SER A OG    1 
ATOM   19974 N  N     . ILE A 1 4251 ? 219.754 215.890 190.474 1.00 7.79   ? 4251 ILE A N     1 
ATOM   19975 C  CA    . ILE A 1 4251 ? 219.435 214.709 191.272 1.00 8.74   ? 4251 ILE A CA    1 
ATOM   19976 C  C     . ILE A 1 4251 ? 220.538 214.424 192.284 1.00 9.31   ? 4251 ILE A C     1 
ATOM   19977 O  O     . ILE A 1 4251 ? 220.319 214.475 193.499 1.00 10.35  ? 4251 ILE A O     1 
ATOM   19978 C  CB    . ILE A 1 4251 ? 219.182 213.494 190.363 1.00 7.97   ? 4251 ILE A CB    1 
ATOM   19979 C  CG1   . ILE A 1 4251 ? 218.140 213.831 189.296 1.00 5.18   ? 4251 ILE A CG1   1 
ATOM   19980 C  CG2   . ILE A 1 4251 ? 218.746 212.298 191.188 1.00 6.20   ? 4251 ILE A CG2   1 
ATOM   19981 C  CD1   . ILE A 1 4251 ? 218.213 212.946 188.077 1.00 5.13   ? 4251 ILE A CD1   1 
ATOM   19982 N  N     . TYR A 1 4252 ? 221.741 214.119 191.799 1.00 9.87   ? 4252 TYR A N     1 
ATOM   19983 C  CA    . TYR A 1 4252 ? 222.854 213.790 192.679 1.00 7.36   ? 4252 TYR A CA    1 
ATOM   19984 C  C     . TYR A 1 4252 ? 223.767 214.973 192.956 1.00 8.64   ? 4252 TYR A C     1 
ATOM   19985 O  O     . TYR A 1 4252 ? 224.350 215.048 194.042 1.00 9.31   ? 4252 TYR A O     1 
ATOM   19986 C  CB    . TYR A 1 4252 ? 223.681 212.646 192.085 1.00 5.70   ? 4252 TYR A CB    1 
ATOM   19987 C  CG    . TYR A 1 4252 ? 223.038 211.288 192.228 1.00 5.58   ? 4252 TYR A CG    1 
ATOM   19988 C  CD1   . TYR A 1 4252 ? 223.263 210.505 193.351 1.00 7.06   ? 4252 TYR A CD1   1 
ATOM   19989 C  CD2   . TYR A 1 4252 ? 222.207 210.786 191.238 1.00 5.87   ? 4252 TYR A CD2   1 
ATOM   19990 C  CE1   . TYR A 1 4252 ? 222.676 209.263 193.483 1.00 5.74   ? 4252 TYR A CE1   1 
ATOM   19991 C  CE2   . TYR A 1 4252 ? 221.618 209.547 191.362 1.00 5.31   ? 4252 TYR A CE2   1 
ATOM   19992 C  CZ    . TYR A 1 4252 ? 221.856 208.789 192.485 1.00 5.97   ? 4252 TYR A CZ    1 
ATOM   19993 O  OH    . TYR A 1 4252 ? 221.268 207.553 192.608 1.00 7.38   ? 4252 TYR A OH    1 
ATOM   19994 N  N     . GLY A 1 4253 ? 223.904 215.896 192.006 1.00 9.30   ? 4253 GLY A N     1 
ATOM   19995 C  CA    . GLY A 1 4253 ? 224.723 217.071 192.224 1.00 7.22   ? 4253 GLY A CA    1 
ATOM   19996 C  C     . GLY A 1 4253 ? 224.110 218.116 193.124 1.00 9.71   ? 4253 GLY A C     1 
ATOM   19997 O  O     . GLY A 1 4253 ? 224.812 219.040 193.544 1.00 12.78  ? 4253 GLY A O     1 
ATOM   19998 N  N     . GLY A 1 4254 ? 222.817 217.992 193.430 1.00 8.13   ? 4254 GLY A N     1 
ATOM   19999 C  CA    . GLY A 1 4254 ? 222.190 218.934 194.340 1.00 6.99   ? 4254 GLY A CA    1 
ATOM   20000 C  C     . GLY A 1 4254 ? 222.763 218.856 195.742 1.00 8.95   ? 4254 GLY A C     1 
ATOM   20001 O  O     . GLY A 1 4254 ? 222.907 219.877 196.420 1.00 11.09  ? 4254 GLY A O     1 
ATOM   20002 N  N     . ARG A 1 4255 ? 223.097 217.649 196.196 1.00 8.17   ? 4255 ARG A N     1 
ATOM   20003 C  CA    . ARG A 1 4255 ? 223.694 217.484 197.514 1.00 9.27   ? 4255 ARG A CA    1 
ATOM   20004 C  C     . ARG A 1 4255 ? 225.156 217.912 197.543 1.00 10.41  ? 4255 ARG A C     1 
ATOM   20005 O  O     . ARG A 1 4255 ? 225.671 218.261 198.611 1.00 14.60  ? 4255 ARG A O     1 
ATOM   20006 C  CB    . ARG A 1 4255 ? 223.571 216.031 197.968 1.00 10.65  ? 4255 ARG A CB    1 
ATOM   20007 C  CG    . ARG A 1 4255 ? 222.177 215.458 197.826 1.00 10.48  ? 4255 ARG A CG    1 
ATOM   20008 C  CD    . ARG A 1 4255 ? 222.096 214.063 198.414 1.00 12.12  ? 4255 ARG A CD    1 
ATOM   20009 N  NE    . ARG A 1 4255 ? 220.722 213.580 198.468 1.00 14.03  ? 4255 ARG A NE    1 
ATOM   20010 C  CZ    . ARG A 1 4255 ? 219.836 213.946 199.384 1.00 14.23  ? 4255 ARG A CZ    1 
ATOM   20011 N  NH1   . ARG A 1 4255 ? 220.150 214.794 200.348 1.00 11.74  ? 4255 ARG A NH1   1 
ATOM   20012 N  NH2   . ARG A 1 4255 ? 218.605 213.447 199.331 1.00 22.04  ? 4255 ARG A NH2   1 
ATOM   20013 N  N     . VAL A 1 4256 ? 225.832 217.895 196.398 1.00 8.00   ? 4256 VAL A N     1 
ATOM   20014 C  CA    . VAL A 1 4256 ? 227.266 218.163 196.365 1.00 11.45  ? 4256 VAL A CA    1 
ATOM   20015 C  C     . VAL A 1 4256 ? 227.503 219.656 196.553 1.00 14.77  ? 4256 VAL A C     1 
ATOM   20016 O  O     . VAL A 1 4256 ? 226.988 220.485 195.794 1.00 18.04  ? 4256 VAL A O     1 
ATOM   20017 C  CB    . VAL A 1 4256 ? 227.885 217.663 195.055 1.00 10.21  ? 4256 VAL A CB    1 
ATOM   20018 C  CG1   . VAL A 1 4256 ? 229.273 218.243 194.876 1.00 12.88  ? 4256 VAL A CG1   1 
ATOM   20019 C  CG2   . VAL A 1 4256 ? 227.935 216.146 195.042 1.00 11.76  ? 4256 VAL A CG2   1 
ATOM   20020 N  N     . ASP A 1 4257 ? 228.298 220.004 197.566 1.00 12.32  ? 4257 ASP A N     1 
ATOM   20021 C  CA    . ASP A 1 4257 ? 228.611 221.390 197.885 1.00 13.90  ? 4257 ASP A CA    1 
ATOM   20022 C  C     . ASP A 1 4257 ? 230.097 221.697 197.729 1.00 18.33  ? 4257 ASP A C     1 
ATOM   20023 O  O     . ASP A 1 4257 ? 230.584 222.684 198.286 1.00 21.97  ? 4257 ASP A O     1 
ATOM   20024 C  CB    . ASP A 1 4257 ? 228.139 221.730 199.300 1.00 14.56  ? 4257 ASP A CB    1 
ATOM   20025 C  CG    . ASP A 1 4257 ? 228.653 220.756 200.344 1.00 26.40  ? 4257 ASP A CG    1 
ATOM   20026 O  OD1   . ASP A 1 4257 ? 229.882 220.556 200.432 1.00 26.33  ? 4257 ASP A OD1   1 
ATOM   20027 O  OD2   . ASP A 1 4257 ? 227.822 220.189 201.084 1.00 31.02  ? 4257 ASP A OD2   1 
ATOM   20028 N  N     . ASN A 1 4258 ? 230.825 220.873 196.980 1.00 18.66  ? 4258 ASN A N     1 
ATOM   20029 C  CA    . ASN A 1 4258 ? 232.257 221.039 196.790 1.00 15.15  ? 4258 ASN A CA    1 
ATOM   20030 C  C     . ASN A 1 4258 ? 232.581 220.952 195.307 1.00 18.16  ? 4258 ASN A C     1 
ATOM   20031 O  O     . ASN A 1 4258 ? 231.936 220.215 194.557 1.00 18.57  ? 4258 ASN A O     1 
ATOM   20032 C  CB    . ASN A 1 4258 ? 233.048 219.975 197.568 1.00 15.17  ? 4258 ASN A CB    1 
ATOM   20033 C  CG    . ASN A 1 4258 ? 234.543 220.236 197.567 1.00 21.51  ? 4258 ASN A CG    1 
ATOM   20034 O  OD1   . ASN A 1 4258 ? 235.020 221.199 196.967 1.00 35.04  ? 4258 ASN A OD1   1 
ATOM   20035 N  ND2   . ASN A 1 4258 ? 235.291 219.374 198.243 1.00 18.92  ? 4258 ASN A ND2   1 
ATOM   20036 N  N     . GLU A 1 4259 ? 233.585 221.725 194.887 1.00 17.14  ? 4259 GLU A N     1 
ATOM   20037 C  CA    . GLU A 1 4259 ? 233.999 221.708 193.488 1.00 17.41  ? 4259 GLU A CA    1 
ATOM   20038 C  C     . GLU A 1 4259 ? 234.606 220.364 193.104 1.00 15.54  ? 4259 GLU A C     1 
ATOM   20039 O  O     . GLU A 1 4259 ? 234.337 219.840 192.017 1.00 19.42  ? 4259 GLU A O     1 
ATOM   20040 C  CB    . GLU A 1 4259 ? 234.983 222.852 193.226 1.00 21.07  ? 4259 GLU A CB    1 
ATOM   20041 C  CG    . GLU A 1 4259 ? 235.316 223.095 191.758 1.00 34.80  ? 4259 GLU A CG    1 
ATOM   20042 C  CD    . GLU A 1 4259 ? 236.413 222.184 191.237 1.00 46.24  ? 4259 GLU A CD    1 
ATOM   20043 O  OE1   . GLU A 1 4259 ? 237.273 221.769 192.041 1.00 34.90  ? 4259 GLU A OE1   1 
ATOM   20044 O  OE2   . GLU A 1 4259 ? 236.415 221.882 190.025 1.00 56.47  ? 4259 GLU A OE2   1 
ATOM   20045 N  N     . PHE A 1 4260 ? 235.422 219.784 193.985 1.00 11.42  ? 4260 PHE A N     1 
ATOM   20046 C  CA    . PHE A 1 4260 ? 236.083 218.521 193.679 1.00 14.47  ? 4260 PHE A CA    1 
ATOM   20047 C  C     . PHE A 1 4260 ? 235.132 217.333 193.769 1.00 12.28  ? 4260 PHE A C     1 
ATOM   20048 O  O     . PHE A 1 4260 ? 235.250 216.389 192.980 1.00 9.68   ? 4260 PHE A O     1 
ATOM   20049 C  CB    . PHE A 1 4260 ? 237.283 218.337 194.607 1.00 12.34  ? 4260 PHE A CB    1 
ATOM   20050 C  CG    . PHE A 1 4260 ? 238.153 219.556 194.700 1.00 10.22  ? 4260 PHE A CG    1 
ATOM   20051 C  CD1   . PHE A 1 4260 ? 239.086 219.829 193.714 1.00 11.52  ? 4260 PHE A CD1   1 
ATOM   20052 C  CD2   . PHE A 1 4260 ? 238.016 220.447 195.750 1.00 14.93  ? 4260 PHE A CD2   1 
ATOM   20053 C  CE1   . PHE A 1 4260 ? 239.878 220.953 193.784 1.00 12.59  ? 4260 PHE A CE1   1 
ATOM   20054 C  CE2   . PHE A 1 4260 ? 238.807 221.575 195.825 1.00 12.89  ? 4260 PHE A CE2   1 
ATOM   20055 C  CZ    . PHE A 1 4260 ? 239.738 221.829 194.840 1.00 13.29  ? 4260 PHE A CZ    1 
ATOM   20056 N  N     . ASP A 1 4261 ? 234.180 217.363 194.704 1.00 13.76  ? 4261 ASP A N     1 
ATOM   20057 C  CA    . ASP A 1 4261 ? 233.146 216.335 194.727 1.00 10.11  ? 4261 ASP A CA    1 
ATOM   20058 C  C     . ASP A 1 4261 ? 232.281 216.405 193.475 1.00 11.80  ? 4261 ASP A C     1 
ATOM   20059 O  O     . ASP A 1 4261 ? 231.900 215.370 192.913 1.00 14.74  ? 4261 ASP A O     1 
ATOM   20060 C  CB    . ASP A 1 4261 ? 232.296 216.481 195.986 1.00 13.10  ? 4261 ASP A CB    1 
ATOM   20061 C  CG    . ASP A 1 4261 ? 233.078 216.195 197.251 1.00 16.82  ? 4261 ASP A CG    1 
ATOM   20062 O  OD1   . ASP A 1 4261 ? 234.190 215.636 197.151 1.00 16.57  ? 4261 ASP A OD1   1 
ATOM   20063 O  OD2   . ASP A 1 4261 ? 232.590 216.542 198.343 1.00 20.60  ? 4261 ASP A OD2   1 
ATOM   20064 N  N     . GLN A 1 4262 ? 231.965 217.621 193.021 1.00 10.31  ? 4262 GLN A N     1 
ATOM   20065 C  CA    . GLN A 1 4262 ? 231.246 217.778 191.762 1.00 8.94   ? 4262 GLN A CA    1 
ATOM   20066 C  C     . GLN A 1 4262 ? 232.065 217.244 190.597 1.00 8.75   ? 4262 GLN A C     1 
ATOM   20067 O  O     . GLN A 1 4262 ? 231.523 216.618 189.679 1.00 11.36  ? 4262 GLN A O     1 
ATOM   20068 C  CB    . GLN A 1 4262 ? 230.896 219.248 191.539 1.00 11.59  ? 4262 GLN A CB    1 
ATOM   20069 C  CG    . GLN A 1 4262 ? 230.045 219.499 190.309 1.00 7.58   ? 4262 GLN A CG    1 
ATOM   20070 C  CD    . GLN A 1 4262 ? 228.624 219.015 190.483 1.00 7.43   ? 4262 GLN A CD    1 
ATOM   20071 O  OE1   . GLN A 1 4262 ? 227.931 219.418 191.416 1.00 10.81  ? 4262 GLN A OE1   1 
ATOM   20072 N  NE2   . GLN A 1 4262 ? 228.180 218.145 189.586 1.00 6.62   ? 4262 GLN A NE2   1 
ATOM   20073 N  N     . ARG A 1 4263 ? 233.376 217.486 190.618 1.00 8.84   ? 4263 ARG A N     1 
ATOM   20074 C  CA    . ARG A 1 4263 ? 234.247 216.964 189.574 1.00 7.59   ? 4263 ARG A CA    1 
ATOM   20075 C  C     . ARG A 1 4263 ? 234.240 215.440 189.562 1.00 9.77   ? 4263 ARG A C     1 
ATOM   20076 O  O     . ARG A 1 4263 ? 234.236 214.823 188.496 1.00 9.63   ? 4263 ARG A O     1 
ATOM   20077 C  CB    . ARG A 1 4263 ? 235.664 217.501 189.768 1.00 8.82   ? 4263 ARG A CB    1 
ATOM   20078 C  CG    . ARG A 1 4263 ? 236.657 217.058 188.718 1.00 11.72  ? 4263 ARG A CG    1 
ATOM   20079 C  CD    . ARG A 1 4263 ? 238.002 217.716 188.948 1.00 12.39  ? 4263 ARG A CD    1 
ATOM   20080 N  NE    . ARG A 1 4263 ? 238.586 217.333 190.227 1.00 15.74  ? 4263 ARG A NE    1 
ATOM   20081 C  CZ    . ARG A 1 4263 ? 239.712 217.831 190.715 1.00 18.12  ? 4263 ARG A CZ    1 
ATOM   20082 N  NH1   . ARG A 1 4263 ? 240.400 218.753 190.062 1.00 17.69  ? 4263 ARG A NH1   1 
ATOM   20083 N  NH2   . ARG A 1 4263 ? 240.162 217.392 191.887 1.00 15.14  ? 4263 ARG A NH2   1 
ATOM   20084 N  N     . LEU A 1 4264 ? 234.242 214.818 190.743 1.00 9.02   ? 4264 LEU A N     1 
ATOM   20085 C  CA    . LEU A 1 4264 ? 234.210 213.358 190.817 1.00 6.65   ? 4264 LEU A CA    1 
ATOM   20086 C  C     . LEU A 1 4264 ? 232.865 212.805 190.346 1.00 10.19  ? 4264 LEU A C     1 
ATOM   20087 O  O     . LEU A 1 4264 ? 232.806 211.755 189.689 1.00 12.01  ? 4264 LEU A O     1 
ATOM   20088 C  CB    . LEU A 1 4264 ? 234.511 212.912 192.246 1.00 8.19   ? 4264 LEU A CB    1 
ATOM   20089 C  CG    . LEU A 1 4264 ? 234.431 211.422 192.573 1.00 11.34  ? 4264 LEU A CG    1 
ATOM   20090 C  CD1   . LEU A 1 4264 ? 235.315 210.617 191.637 1.00 11.81  ? 4264 LEU A CD1   1 
ATOM   20091 C  CD2   . LEU A 1 4264 ? 234.826 211.192 194.015 1.00 8.38   ? 4264 LEU A CD2   1 
ATOM   20092 N  N     . LEU A 1 4265 ? 231.773 213.494 190.677 1.00 8.52   ? 4265 LEU A N     1 
ATOM   20093 C  CA    . LEU A 1 4265 ? 230.467 213.071 190.183 1.00 6.12   ? 4265 LEU A CA    1 
ATOM   20094 C  C     . LEU A 1 4265 ? 230.399 213.168 188.663 1.00 8.43   ? 4265 LEU A C     1 
ATOM   20095 O  O     . LEU A 1 4265 ? 229.862 212.272 187.997 1.00 9.86   ? 4265 LEU A O     1 
ATOM   20096 C  CB    . LEU A 1 4265 ? 229.365 213.908 190.829 1.00 7.22   ? 4265 LEU A CB    1 
ATOM   20097 C  CG    . LEU A 1 4265 ? 227.928 213.545 190.459 1.00 7.47   ? 4265 LEU A CG    1 
ATOM   20098 C  CD1   . LEU A 1 4265 ? 227.462 212.325 191.234 1.00 5.94   ? 4265 LEU A CD1   1 
ATOM   20099 C  CD2   . LEU A 1 4265 ? 227.010 214.720 190.711 1.00 9.37   ? 4265 LEU A CD2   1 
ATOM   20100 N  N     . ASN A 1 4266 ? 230.936 214.253 188.098 1.00 10.07  ? 4266 ASN A N     1 
ATOM   20101 C  CA    . ASN A 1 4266 ? 230.991 214.392 186.646 1.00 9.72   ? 4266 ASN A CA    1 
ATOM   20102 C  C     . ASN A 1 4266 ? 231.873 213.318 186.026 1.00 9.42   ? 4266 ASN A C     1 
ATOM   20103 O  O     . ASN A 1 4266 ? 231.544 212.766 184.972 1.00 10.97  ? 4266 ASN A O     1 
ATOM   20104 C  CB    . ASN A 1 4266 ? 231.498 215.784 186.274 1.00 10.17  ? 4266 ASN A CB    1 
ATOM   20105 C  CG    . ASN A 1 4266 ? 230.559 216.885 186.720 1.00 10.76  ? 4266 ASN A CG    1 
ATOM   20106 O  OD1   . ASN A 1 4266 ? 229.458 216.621 187.201 1.00 10.72  ? 4266 ASN A OD1   1 
ATOM   20107 N  ND2   . ASN A 1 4266 ? 230.993 218.130 186.569 1.00 13.16  ? 4266 ASN A ND2   1 
ATOM   20108 N  N     . THR A 1 4267 ? 233.018 213.038 186.654 1.00 12.26  ? 4267 THR A N     1 
ATOM   20109 C  CA    . THR A 1 4267 ? 233.820 211.862 186.329 1.00 11.89  ? 4267 THR A CA    1 
ATOM   20110 C  C     . THR A 1 4267 ? 232.956 210.629 186.135 1.00 13.64  ? 4267 THR A C     1 
ATOM   20111 O  O     . THR A 1 4267 ? 232.938 210.028 185.053 1.00 14.07  ? 4267 THR A O     1 
ATOM   20112 C  CB    . THR A 1 4267 ? 234.832 211.616 187.452 1.00 15.43  ? 4267 THR A CB    1 
ATOM   20113 O  OG1   . THR A 1 4267 ? 235.736 212.725 187.569 1.00 18.92  ? 4267 THR A OG1   1 
ATOM   20114 C  CG2   . THR A 1 4267 ? 235.538 210.273 187.322 1.00 18.58  ? 4267 THR A CG2   1 
ATOM   20115 N  N     . PHE A 1 4268 ? 232.239 210.234 187.185 1.00 12.77  ? 4268 PHE A N     1 
ATOM   20116 C  CA    . PHE A 1 4268 ? 231.506 208.975 187.138 1.00 10.73  ? 4268 PHE A CA    1 
ATOM   20117 C  C     . PHE A 1 4268 ? 230.403 209.016 186.089 1.00 10.26  ? 4268 PHE A C     1 
ATOM   20118 O  O     . PHE A 1 4268 ? 230.200 208.043 185.351 1.00 11.64  ? 4268 PHE A O     1 
ATOM   20119 C  CB    . PHE A 1 4268 ? 230.945 208.654 188.520 1.00 10.32  ? 4268 PHE A CB    1 
ATOM   20120 C  CG    . PHE A 1 4268 ? 231.910 207.914 189.394 1.00 11.84  ? 4268 PHE A CG    1 
ATOM   20121 C  CD1   . PHE A 1 4268 ? 232.591 206.812 188.915 1.00 14.23  ? 4268 PHE A CD1   1 
ATOM   20122 C  CD2   . PHE A 1 4268 ? 232.161 208.342 190.684 1.00 15.77  ? 4268 PHE A CD2   1 
ATOM   20123 C  CE1   . PHE A 1 4268 ? 233.489 206.137 189.714 1.00 20.84  ? 4268 PHE A CE1   1 
ATOM   20124 C  CE2   . PHE A 1 4268 ? 233.058 207.672 191.486 1.00 15.32  ? 4268 PHE A CE2   1 
ATOM   20125 C  CZ    . PHE A 1 4268 ? 233.723 206.568 191.001 1.00 17.20  ? 4268 PHE A CZ    1 
ATOM   20126 N  N     . LEU A 1 4269 ? 229.694 210.143 185.992 1.00 11.80  ? 4269 LEU A N     1 
ATOM   20127 C  CA    . LEU A 1 4269 ? 228.580 210.233 185.052 1.00 11.00  ? 4269 LEU A CA    1 
ATOM   20128 C  C     . LEU A 1 4269 ? 229.055 210.187 183.605 1.00 10.22  ? 4269 LEU A C     1 
ATOM   20129 O  O     . LEU A 1 4269 ? 228.444 209.513 182.769 1.00 13.99  ? 4269 LEU A O     1 
ATOM   20130 C  CB    . LEU A 1 4269 ? 227.773 211.500 185.318 1.00 9.27   ? 4269 LEU A CB    1 
ATOM   20131 C  CG    . LEU A 1 4269 ? 226.767 211.350 186.458 1.00 8.05   ? 4269 LEU A CG    1 
ATOM   20132 C  CD1   . LEU A 1 4269 ? 226.416 212.699 187.046 1.00 7.02   ? 4269 LEU A CD1   1 
ATOM   20133 C  CD2   . LEU A 1 4269 ? 225.524 210.628 185.977 1.00 8.19   ? 4269 LEU A CD2   1 
ATOM   20134 N  N     . GLU A 1 4270 ? 230.139 210.898 183.283 1.00 10.85  ? 4270 GLU A N     1 
ATOM   20135 C  CA    . GLU A 1 4270 ? 230.667 210.853 181.924 1.00 11.60  ? 4270 GLU A CA    1 
ATOM   20136 C  C     . GLU A 1 4270 ? 231.245 209.482 181.602 1.00 12.98  ? 4270 GLU A C     1 
ATOM   20137 O  O     . GLU A 1 4270 ? 231.124 209.005 180.469 1.00 12.54  ? 4270 GLU A O     1 
ATOM   20138 C  CB    . GLU A 1 4270 ? 231.724 211.938 181.727 1.00 10.79  ? 4270 GLU A CB    1 
ATOM   20139 C  CG    . GLU A 1 4270 ? 231.214 213.357 181.920 1.00 17.91  ? 4270 GLU A CG    1 
ATOM   20140 C  CD    . GLU A 1 4270 ? 230.547 213.909 180.677 1.00 30.10  ? 4270 GLU A CD    1 
ATOM   20141 O  OE1   . GLU A 1 4270 ? 230.748 213.333 179.587 1.00 30.78  ? 4270 GLU A OE1   1 
ATOM   20142 O  OE2   . GLU A 1 4270 ? 229.825 214.922 180.790 1.00 33.33  ? 4270 GLU A OE2   1 
ATOM   20143 N  N     . ARG A 1 4271 ? 231.882 208.835 182.582 1.00 17.47  ? 4271 ARG A N     1 
ATOM   20144 C  CA    . ARG A 1 4271 ? 232.483 207.532 182.323 1.00 12.65  ? 4271 ARG A CA    1 
ATOM   20145 C  C     . ARG A 1 4271 ? 231.424 206.457 182.112 1.00 13.23  ? 4271 ARG A C     1 
ATOM   20146 O  O     . ARG A 1 4271 ? 231.606 205.556 181.286 1.00 17.00  ? 4271 ARG A O     1 
ATOM   20147 C  CB    . ARG A 1 4271 ? 233.414 207.151 183.472 1.00 15.45  ? 4271 ARG A CB    1 
ATOM   20148 C  CG    . ARG A 1 4271 ? 234.635 206.363 183.042 1.00 22.94  ? 4271 ARG A CG    1 
ATOM   20149 C  CD    . ARG A 1 4271 ? 235.558 206.105 184.218 1.00 29.58  ? 4271 ARG A CD    1 
ATOM   20150 N  NE    . ARG A 1 4271 ? 234.813 205.814 185.438 1.00 31.95  ? 4271 ARG A NE    1 
ATOM   20151 C  CZ    . ARG A 1 4271 ? 234.238 204.652 185.706 1.00 24.84  ? 4271 ARG A CZ    1 
ATOM   20152 N  NH1   . ARG A 1 4271 ? 234.299 203.638 184.857 1.00 18.57  ? 4271 ARG A NH1   1 
ATOM   20153 N  NH2   . ARG A 1 4271 ? 233.582 204.502 186.851 1.00 24.87  ? 4271 ARG A NH2   1 
ATOM   20154 N  N     . LEU A 1 4272 ? 230.312 206.534 182.843 1.00 11.71  ? 4272 LEU A N     1 
ATOM   20155 C  CA    . LEU A 1 4272 ? 229.327 205.459 182.803 1.00 9.22   ? 4272 LEU A CA    1 
ATOM   20156 C  C     . LEU A 1 4272 ? 228.239 205.684 181.757 1.00 10.21  ? 4272 LEU A C     1 
ATOM   20157 O  O     . LEU A 1 4272 ? 227.883 204.756 181.024 1.00 12.12  ? 4272 LEU A O     1 
ATOM   20158 C  CB    . LEU A 1 4272 ? 228.695 205.283 184.187 1.00 8.74   ? 4272 LEU A CB    1 
ATOM   20159 C  CG    . LEU A 1 4272 ? 229.543 204.516 185.202 1.00 8.83   ? 4272 LEU A CG    1 
ATOM   20160 C  CD1   . LEU A 1 4272 ? 228.762 204.285 186.482 1.00 8.19   ? 4272 LEU A CD1   1 
ATOM   20161 C  CD2   . LEU A 1 4272 ? 230.021 203.201 184.613 1.00 11.34  ? 4272 LEU A CD2   1 
ATOM   20162 N  N     . PHE A 1 4273 ? 227.696 206.898 181.673 1.00 13.04  ? 4273 PHE A N     1 
ATOM   20163 C  CA    . PHE A 1 4273 ? 226.534 207.167 180.825 1.00 12.99  ? 4273 PHE A CA    1 
ATOM   20164 C  C     . PHE A 1 4273 ? 227.009 207.663 179.466 1.00 15.46  ? 4273 PHE A C     1 
ATOM   20165 O  O     . PHE A 1 4273 ? 227.251 208.853 179.261 1.00 14.71  ? 4273 PHE A O     1 
ATOM   20166 C  CB    . PHE A 1 4273 ? 225.603 208.165 181.499 1.00 9.15   ? 4273 PHE A CB    1 
ATOM   20167 C  CG    . PHE A 1 4273 ? 224.862 207.598 182.676 1.00 12.89  ? 4273 PHE A CG    1 
ATOM   20168 C  CD1   . PHE A 1 4273 ? 225.449 207.563 183.928 1.00 14.67  ? 4273 PHE A CD1   1 
ATOM   20169 C  CD2   . PHE A 1 4273 ? 223.585 207.088 182.526 1.00 14.69  ? 4273 PHE A CD2   1 
ATOM   20170 C  CE1   . PHE A 1 4273 ? 224.773 207.038 185.010 1.00 12.29  ? 4273 PHE A CE1   1 
ATOM   20171 C  CE2   . PHE A 1 4273 ? 222.905 206.561 183.606 1.00 10.73  ? 4273 PHE A CE2   1 
ATOM   20172 C  CZ    . PHE A 1 4273 ? 223.500 206.537 184.849 1.00 7.99   ? 4273 PHE A CZ    1 
ATOM   20173 N  N     . THR A 1 4274 ? 227.134 206.735 178.522 1.00 16.34  ? 4274 THR A N     1 
ATOM   20174 C  CA    . THR A 1 4274 ? 227.559 207.057 177.166 1.00 14.75  ? 4274 THR A CA    1 
ATOM   20175 C  C     . THR A 1 4274 ? 227.128 205.924 176.247 1.00 17.55  ? 4274 THR A C     1 
ATOM   20176 O  O     . THR A 1 4274 ? 226.716 204.854 176.698 1.00 22.11  ? 4274 THR A O     1 
ATOM   20177 C  CB    . THR A 1 4274 ? 229.073 207.279 177.086 1.00 17.26  ? 4274 THR A CB    1 
ATOM   20178 O  OG1   . THR A 1 4274 ? 229.452 207.510 175.724 1.00 23.26  ? 4274 THR A OG1   1 
ATOM   20179 C  CG2   . THR A 1 4274 ? 229.817 206.065 177.616 1.00 14.85  ? 4274 THR A CG2   1 
ATOM   20180 N  N     . THR A 1 4275 ? 227.217 206.182 174.939 1.00 21.80  ? 4275 THR A N     1 
ATOM   20181 C  CA    . THR A 1 4275 ? 226.912 205.143 173.961 1.00 22.11  ? 4275 THR A CA    1 
ATOM   20182 C  C     . THR A 1 4275 ? 227.862 203.960 174.087 1.00 21.70  ? 4275 THR A C     1 
ATOM   20183 O  O     . THR A 1 4275 ? 227.471 202.816 173.825 1.00 22.45  ? 4275 THR A O     1 
ATOM   20184 C  CB    . THR A 1 4275 ? 226.968 205.716 172.544 1.00 20.36  ? 4275 THR A CB    1 
ATOM   20185 O  OG1   . THR A 1 4275 ? 228.330 205.967 172.182 1.00 29.96  ? 4275 THR A OG1   1 
ATOM   20186 C  CG2   . THR A 1 4275 ? 226.192 207.018 172.467 1.00 23.02  ? 4275 THR A CG2   1 
ATOM   20187 N  N     . ARG A 1 4276 ? 229.106 204.210 174.505 1.00 19.62  ? 4276 ARG A N     1 
ATOM   20188 C  CA    . ARG A 1 4276 ? 230.081 203.135 174.633 1.00 25.27  ? 4276 ARG A CA    1 
ATOM   20189 C  C     . ARG A 1 4276 ? 229.675 202.113 175.682 1.00 26.91  ? 4276 ARG A C     1 
ATOM   20190 O  O     . ARG A 1 4276 ? 230.210 200.999 175.689 1.00 29.35  ? 4276 ARG A O     1 
ATOM   20191 C  CB    . ARG A 1 4276 ? 231.459 203.709 174.971 1.00 23.55  ? 4276 ARG A CB    1 
ATOM   20192 C  CG    . ARG A 1 4276 ? 232.038 204.629 173.906 1.00 30.21  ? 4276 ARG A CG    1 
ATOM   20193 C  CD    . ARG A 1 4276 ? 232.556 203.860 172.695 1.00 41.21  ? 4276 ARG A CD    1 
ATOM   20194 N  NE    . ARG A 1 4276 ? 231.477 203.358 171.853 1.00 43.78  ? 4276 ARG A NE    1 
ATOM   20195 C  CZ    . ARG A 1 4276 ? 230.787 204.099 170.997 1.00 42.71  ? 4276 ARG A CZ    1 
ATOM   20196 N  NH1   . ARG A 1 4276 ? 231.052 205.383 170.823 1.00 45.16  ? 4276 ARG A NH1   1 
ATOM   20197 N  NH2   . ARG A 1 4276 ? 229.804 203.537 170.300 1.00 38.95  ? 4276 ARG A NH2   1 
ATOM   20198 N  N     . SER A 1 4277 ? 228.738 202.463 176.564 1.00 23.66  ? 4277 SER A N     1 
ATOM   20199 C  CA    . SER A 1 4277 ? 228.221 201.513 177.537 1.00 20.36  ? 4277 SER A CA    1 
ATOM   20200 C  C     . SER A 1 4277 ? 227.400 200.406 176.896 1.00 23.28  ? 4277 SER A C     1 
ATOM   20201 O  O     . SER A 1 4277 ? 227.139 199.394 177.553 1.00 29.53  ? 4277 SER A O     1 
ATOM   20202 C  CB    . SER A 1 4277 ? 227.375 202.243 178.580 1.00 20.17  ? 4277 SER A CB    1 
ATOM   20203 O  OG    . SER A 1 4277 ? 228.180 203.069 179.403 1.00 25.60  ? 4277 SER A OG    1 
ATOM   20204 N  N     . PHE A 1 4278 ? 226.986 200.568 175.641 1.00 23.23  ? 4278 PHE A N     1 
ATOM   20205 C  CA    . PHE A 1 4278 ? 226.219 199.546 174.945 1.00 21.76  ? 4278 PHE A CA    1 
ATOM   20206 C  C     . PHE A 1 4278 ? 227.088 198.620 174.106 1.00 32.43  ? 4278 PHE A C     1 
ATOM   20207 O  O     . PHE A 1 4278 ? 226.553 197.750 173.411 1.00 36.19  ? 4278 PHE A O     1 
ATOM   20208 C  CB    . PHE A 1 4278 ? 225.148 200.198 174.070 1.00 21.80  ? 4278 PHE A CB    1 
ATOM   20209 C  CG    . PHE A 1 4278 ? 223.895 200.540 174.815 1.00 23.71  ? 4278 PHE A CG    1 
ATOM   20210 C  CD1   . PHE A 1 4278 ? 223.858 201.626 175.672 1.00 22.28  ? 4278 PHE A CD1   1 
ATOM   20211 C  CD2   . PHE A 1 4278 ? 222.758 199.769 174.672 1.00 20.74  ? 4278 PHE A CD2   1 
ATOM   20212 C  CE1   . PHE A 1 4278 ? 222.710 201.938 176.366 1.00 16.71  ? 4278 PHE A CE1   1 
ATOM   20213 C  CE2   . PHE A 1 4278 ? 221.609 200.077 175.365 1.00 17.83  ? 4278 PHE A CE2   1 
ATOM   20214 C  CZ    . PHE A 1 4278 ? 221.584 201.162 176.213 1.00 17.35  ? 4278 PHE A CZ    1 
ATOM   20215 N  N     . ASP A 1 4279 ? 228.405 198.785 174.153 1.00 34.10  ? 4279 ASP A N     1 
ATOM   20216 C  CA    . ASP A 1 4279 ? 229.310 197.897 173.445 1.00 34.47  ? 4279 ASP A CA    1 
ATOM   20217 C  C     . ASP A 1 4279 ? 229.638 196.678 174.304 1.00 35.72  ? 4279 ASP A C     1 
ATOM   20218 O  O     . ASP A 1 4279 ? 229.512 196.696 175.531 1.00 34.03  ? 4279 ASP A O     1 
ATOM   20219 C  CB    . ASP A 1 4279 ? 230.591 198.637 173.063 1.00 38.96  ? 4279 ASP A CB    1 
ATOM   20220 C  CG    . ASP A 1 4279 ? 230.326 199.829 172.166 1.00 43.99  ? 4279 ASP A CG    1 
ATOM   20221 O  OD1   . ASP A 1 4279 ? 229.160 200.018 171.758 1.00 39.79  ? 4279 ASP A OD1   1 
ATOM   20222 O  OD2   . ASP A 1 4279 ? 231.279 200.580 171.870 1.00 43.71  ? 4279 ASP A OD2   1 
ATOM   20223 N  N     . SER A 1 4280 ? 230.061 195.603 173.638 1.00 39.43  ? 4280 SER A N     1 
ATOM   20224 C  CA    . SER A 1 4280 ? 230.381 194.366 174.339 1.00 42.76  ? 4280 SER A CA    1 
ATOM   20225 C  C     . SER A 1 4280 ? 231.725 194.422 175.050 1.00 38.13  ? 4280 SER A C     1 
ATOM   20226 O  O     . SER A 1 4280 ? 231.991 193.576 175.910 1.00 34.60  ? 4280 SER A O     1 
ATOM   20227 C  CB    . SER A 1 4280 ? 230.364 193.188 173.362 1.00 44.66  ? 4280 SER A CB    1 
ATOM   20228 O  OG    . SER A 1 4280 ? 231.150 193.463 172.216 1.00 46.77  ? 4280 SER A OG    1 
ATOM   20229 N  N     . GLU A 1 4281 ? 232.571 195.394 174.718 1.00 37.82  ? 4281 GLU A N     1 
ATOM   20230 C  CA    . GLU A 1 4281 ? 233.885 195.542 175.326 1.00 39.18  ? 4281 GLU A CA    1 
ATOM   20231 C  C     . GLU A 1 4281 ? 233.902 196.561 176.458 1.00 41.02  ? 4281 GLU A C     1 
ATOM   20232 O  O     . GLU A 1 4281 ? 234.979 196.890 176.964 1.00 44.91  ? 4281 GLU A O     1 
ATOM   20233 C  CB    . GLU A 1 4281 ? 234.913 195.923 174.256 1.00 52.62  ? 4281 GLU A CB    1 
ATOM   20234 C  CG    . GLU A 1 4281 ? 234.555 197.174 173.463 1.00 60.07  ? 4281 GLU A CG    1 
ATOM   20235 C  CD    . GLU A 1 4281 ? 235.101 198.447 174.083 1.00 65.30  ? 4281 GLU A CD    1 
ATOM   20236 O  OE1   . GLU A 1 4281 ? 236.096 198.368 174.834 1.00 67.36  ? 4281 GLU A OE1   1 
ATOM   20237 O  OE2   . GLU A 1 4281 ? 234.531 199.528 173.823 1.00 59.19  ? 4281 GLU A OE2   1 
ATOM   20238 N  N     . PHE A 1 4282 ? 232.740 197.064 176.864 1.00 37.41  ? 4282 PHE A N     1 
ATOM   20239 C  CA    . PHE A 1 4282 ? 232.683 198.081 177.906 1.00 30.29  ? 4282 PHE A CA    1 
ATOM   20240 C  C     . PHE A 1 4282 ? 233.124 197.513 179.249 1.00 28.16  ? 4282 PHE A C     1 
ATOM   20241 O  O     . PHE A 1 4282 ? 232.787 196.380 179.606 1.00 30.68  ? 4282 PHE A O     1 
ATOM   20242 C  CB    . PHE A 1 4282 ? 231.269 198.646 178.021 1.00 25.84  ? 4282 PHE A CB    1 
ATOM   20243 C  CG    . PHE A 1 4282 ? 231.173 199.860 178.896 1.00 24.30  ? 4282 PHE A CG    1 
ATOM   20244 C  CD1   . PHE A 1 4282 ? 231.777 201.046 178.521 1.00 18.18  ? 4282 PHE A CD1   1 
ATOM   20245 C  CD2   . PHE A 1 4282 ? 230.483 199.814 180.093 1.00 21.08  ? 4282 PHE A CD2   1 
ATOM   20246 C  CE1   . PHE A 1 4282 ? 231.692 202.163 179.324 1.00 18.11  ? 4282 PHE A CE1   1 
ATOM   20247 C  CE2   . PHE A 1 4282 ? 230.396 200.927 180.901 1.00 18.01  ? 4282 PHE A CE2   1 
ATOM   20248 C  CZ    . PHE A 1 4282 ? 231.000 202.105 180.515 1.00 20.67  ? 4282 PHE A CZ    1 
ATOM   20249 N  N     . LYS A 1 4283 ? 233.883 198.309 179.995 1.00 24.10  ? 4283 LYS A N     1 
ATOM   20250 C  CA    . LYS A 1 4283 ? 234.356 197.944 181.323 1.00 22.80  ? 4283 LYS A CA    1 
ATOM   20251 C  C     . LYS A 1 4283 ? 233.704 198.859 182.350 1.00 19.96  ? 4283 LYS A C     1 
ATOM   20252 O  O     . LYS A 1 4283 ? 233.814 200.086 182.250 1.00 23.84  ? 4283 LYS A O     1 
ATOM   20253 C  CB    . LYS A 1 4283 ? 235.879 198.047 181.411 1.00 25.35  ? 4283 LYS A CB    1 
ATOM   20254 C  CG    . LYS A 1 4283 ? 236.622 197.328 180.302 1.00 32.46  ? 4283 LYS A CG    1 
ATOM   20255 C  CD    . LYS A 1 4283 ? 238.112 197.263 180.601 1.00 30.62  ? 4283 LYS A CD    1 
ATOM   20256 C  CE    . LYS A 1 4283 ? 238.897 196.771 179.398 1.00 29.17  ? 4283 LYS A CE    1 
ATOM   20257 N  NZ    . LYS A 1 4283 ? 238.784 195.299 179.224 1.00 31.34  ? 4283 LYS A NZ    1 
ATOM   20258 N  N     . LEU A 1 4284 ? 233.023 198.264 183.331 1.00 17.05  ? 4284 LEU A N     1 
ATOM   20259 C  CA    . LEU A 1 4284 ? 232.448 199.059 184.411 1.00 17.89  ? 4284 LEU A CA    1 
ATOM   20260 C  C     . LEU A 1 4284 ? 233.537 199.607 185.324 1.00 17.26  ? 4284 LEU A C     1 
ATOM   20261 O  O     . LEU A 1 4284 ? 233.462 200.757 185.773 1.00 15.26  ? 4284 LEU A O     1 
ATOM   20262 C  CB    . LEU A 1 4284 ? 231.449 198.221 185.207 1.00 10.08  ? 4284 LEU A CB    1 
ATOM   20263 C  CG    . LEU A 1 4284 ? 230.056 198.095 184.592 1.00 9.90   ? 4284 LEU A CG    1 
ATOM   20264 C  CD1   . LEU A 1 4284 ? 229.251 197.027 185.310 1.00 13.07  ? 4284 LEU A CD1   1 
ATOM   20265 C  CD2   . LEU A 1 4284 ? 229.334 199.429 184.617 1.00 9.11   ? 4284 LEU A CD2   1 
ATOM   20266 N  N     . ALA A 1 4285 ? 234.550 198.795 185.612 1.00 18.76  ? 4285 ALA A N     1 
ATOM   20267 C  CA    . ALA A 1 4285 ? 235.701 199.210 186.396 1.00 19.83  ? 4285 ALA A CA    1 
ATOM   20268 C  C     . ALA A 1 4285 ? 236.944 198.578 185.791 1.00 31.12  ? 4285 ALA A C     1 
ATOM   20269 O  O     . ALA A 1 4285 ? 236.861 197.635 185.003 1.00 32.72  ? 4285 ALA A O     1 
ATOM   20270 C  CB    . ALA A 1 4285 ? 235.556 198.818 187.872 1.00 17.47  ? 4285 ALA A CB    1 
ATOM   20271 N  N     . CYS A 1 4286 ? 238.104 199.113 186.160 1.00 41.54  ? 4286 CYS A N     1 
ATOM   20272 C  CA    . CYS A 1 4286 ? 239.376 198.647 185.631 1.00 43.90  ? 4286 CYS A CA    1 
ATOM   20273 C  C     . CYS A 1 4286 ? 240.329 198.306 186.767 1.00 52.66  ? 4286 CYS A C     1 
ATOM   20274 O  O     . CYS A 1 4286 ? 240.263 198.896 187.851 1.00 50.78  ? 4286 CYS A O     1 
ATOM   20275 C  CB    . CYS A 1 4286 ? 240.017 199.698 184.715 1.00 42.48  ? 4286 CYS A CB    1 
ATOM   20276 S  SG    . CYS A 1 4286 ? 238.906 200.376 183.460 1.00 64.09  ? 4286 CYS A SG    1 
ATOM   20277 N  N     . LYS A 1 4287 ? 241.216 197.351 186.492 1.00 57.49  ? 4287 LYS A N     1 
ATOM   20278 C  CA    . LYS A 1 4287 ? 242.263 196.878 187.406 1.00 58.11  ? 4287 LYS A CA    1 
ATOM   20279 C  C     . LYS A 1 4287 ? 241.761 196.780 188.848 1.00 55.24  ? 4287 LYS A C     1 
ATOM   20280 O  O     . LYS A 1 4287 ? 242.310 197.371 189.779 1.00 52.14  ? 4287 LYS A O     1 
ATOM   20281 C  CB    . LYS A 1 4287 ? 243.522 197.749 187.305 1.00 61.60  ? 4287 LYS A CB    1 
ATOM   20282 C  CG    . LYS A 1 4287 ? 243.338 199.244 187.540 1.00 55.97  ? 4287 LYS A CG    1 
ATOM   20283 C  CD    . LYS A 1 4287 ? 244.471 200.042 186.918 1.00 61.24  ? 4287 LYS A CD    1 
ATOM   20284 C  CE    . LYS A 1 4287 ? 244.494 199.871 185.407 1.00 59.93  ? 4287 LYS A CE    1 
ATOM   20285 N  NZ    . LYS A 1 4287 ? 245.586 200.660 184.774 1.00 58.18  ? 4287 LYS A NZ    1 
ATOM   20286 N  N     . VAL A 1 4288 ? 240.693 195.999 189.017 1.00 52.35  ? 4288 VAL A N     1 
ATOM   20287 C  CA    . VAL A 1 4288 ? 240.120 195.809 190.346 1.00 45.66  ? 4288 VAL A CA    1 
ATOM   20288 C  C     . VAL A 1 4288 ? 241.081 195.036 191.241 1.00 51.93  ? 4288 VAL A C     1 
ATOM   20289 O  O     . VAL A 1 4288 ? 241.261 195.373 192.417 1.00 55.42  ? 4288 VAL A O     1 
ATOM   20290 C  CB    . VAL A 1 4288 ? 238.744 195.127 190.242 1.00 35.69  ? 4288 VAL A CB    1 
ATOM   20291 C  CG1   . VAL A 1 4288 ? 237.709 196.121 189.747 1.00 32.06  ? 4288 VAL A CG1   1 
ATOM   20292 C  CG2   . VAL A 1 4288 ? 238.807 193.931 189.312 1.00 51.48  ? 4288 VAL A CG2   1 
ATOM   20293 N  N     . ASP A 1 4289 ? 241.711 193.990 190.709 1.00 58.61  ? 4289 ASP A N     1 
ATOM   20294 C  CA    . ASP A 1 4289 ? 242.750 193.270 191.438 1.00 67.86  ? 4289 ASP A CA    1 
ATOM   20295 C  C     . ASP A 1 4289 ? 243.652 192.584 190.425 1.00 79.09  ? 4289 ASP A C     1 
ATOM   20296 O  O     . ASP A 1 4289 ? 243.197 191.718 189.670 1.00 77.99  ? 4289 ASP A O     1 
ATOM   20297 C  CB    . ASP A 1 4289 ? 242.155 192.252 192.419 1.00 65.40  ? 4289 ASP A CB    1 
ATOM   20298 C  CG    . ASP A 1 4289 ? 241.142 191.330 191.770 1.00 73.34  ? 4289 ASP A CG    1 
ATOM   20299 O  OD1   . ASP A 1 4289 ? 240.616 191.680 190.695 1.00 73.44  ? 4289 ASP A OD1   1 
ATOM   20300 O  OD2   . ASP A 1 4289 ? 240.873 190.250 192.338 1.00 77.75  ? 4289 ASP A OD2   1 
ATOM   20301 N  N     . GLY A 1 4290 ? 244.923 192.975 190.403 1.00 80.64  ? 4290 GLY A N     1 
ATOM   20302 C  CA    . GLY A 1 4290 ? 245.849 192.442 189.425 1.00 87.11  ? 4290 GLY A CA    1 
ATOM   20303 C  C     . GLY A 1 4290 ? 245.659 193.065 188.059 1.00 88.22  ? 4290 GLY A C     1 
ATOM   20304 O  O     . GLY A 1 4290 ? 245.978 194.239 187.857 1.00 85.74  ? 4290 GLY A O     1 
ATOM   20305 N  N     . HIS A 1 4291 ? 245.133 192.289 187.111 1.00 90.60  ? 4291 HIS A N     1 
ATOM   20306 C  CA    . HIS A 1 4291 ? 244.898 192.777 185.760 1.00 96.03  ? 4291 HIS A CA    1 
ATOM   20307 C  C     . HIS A 1 4291 ? 243.474 192.574 185.262 1.00 93.72  ? 4291 HIS A C     1 
ATOM   20308 O  O     . HIS A 1 4291 ? 243.135 193.112 184.202 1.00 90.65  ? 4291 HIS A O     1 
ATOM   20309 C  CB    . HIS A 1 4291 ? 245.867 192.109 184.771 1.00 98.30  ? 4291 HIS A CB    1 
ATOM   20310 C  CG    . HIS A 1 4291 ? 245.548 190.674 184.490 1.00 101.26 ? 4291 HIS A CG    1 
ATOM   20311 N  ND1   . HIS A 1 4291 ? 245.836 189.660 185.377 1.00 99.88  ? 4291 HIS A ND1   1 
ATOM   20312 C  CD2   . HIS A 1 4291 ? 244.965 190.084 183.420 1.00 101.14 ? 4291 HIS A CD2   1 
ATOM   20313 C  CE1   . HIS A 1 4291 ? 245.444 188.507 184.867 1.00 98.85  ? 4291 HIS A CE1   1 
ATOM   20314 N  NE2   . HIS A 1 4291 ? 244.913 188.735 183.680 1.00 101.82 ? 4291 HIS A NE2   1 
ATOM   20315 N  N     . LYS A 1 4292 ? 242.636 191.825 185.975 1.00 87.31  ? 4292 LYS A N     1 
ATOM   20316 C  CA    . LYS A 1 4292 ? 241.262 191.636 185.542 1.00 74.88  ? 4292 LYS A CA    1 
ATOM   20317 C  C     . LYS A 1 4292 ? 240.427 192.876 185.854 1.00 64.04  ? 4292 LYS A C     1 
ATOM   20318 O  O     . LYS A 1 4292 ? 240.828 193.755 186.622 1.00 62.82  ? 4292 LYS A O     1 
ATOM   20319 C  CB    . LYS A 1 4292 ? 240.647 190.406 186.208 1.00 71.69  ? 4292 LYS A CB    1 
ATOM   20320 C  CG    . LYS A 1 4292 ? 240.466 190.538 187.707 1.00 70.37  ? 4292 LYS A CG    1 
ATOM   20321 C  CD    . LYS A 1 4292 ? 239.899 189.263 188.308 1.00 75.54  ? 4292 LYS A CD    1 
ATOM   20322 C  CE    . LYS A 1 4292 ? 238.454 189.053 187.887 1.00 74.47  ? 4292 LYS A CE    1 
ATOM   20323 N  NZ    . LYS A 1 4292 ? 237.557 190.101 188.449 1.00 67.97  ? 4292 LYS A NZ    1 
ATOM   20324 N  N     . ASP A 1 4293 ? 239.245 192.936 185.247 1.00 52.56  ? 4293 ASP A N     1 
ATOM   20325 C  CA    . ASP A 1 4293 ? 238.379 194.095 185.389 1.00 45.46  ? 4293 ASP A CA    1 
ATOM   20326 C  C     . ASP A 1 4293 ? 236.924 193.656 185.309 1.00 40.75  ? 4293 ASP A C     1 
ATOM   20327 O  O     . ASP A 1 4293 ? 236.604 192.587 184.783 1.00 49.42  ? 4293 ASP A O     1 
ATOM   20328 C  CB    . ASP A 1 4293 ? 238.689 195.154 184.323 1.00 44.91  ? 4293 ASP A CB    1 
ATOM   20329 C  CG    . ASP A 1 4293 ? 238.737 194.577 182.921 1.00 46.72  ? 4293 ASP A CG    1 
ATOM   20330 O  OD1   . ASP A 1 4293 ? 237.744 193.959 182.487 1.00 45.22  ? 4293 ASP A OD1   1 
ATOM   20331 O  OD2   . ASP A 1 4293 ? 239.779 194.742 182.251 1.00 54.00  ? 4293 ASP A OD2   1 
ATOM   20332 N  N     . ILE A 1 4294 ? 236.045 194.498 185.843 1.00 29.72  ? 4294 ILE A N     1 
ATOM   20333 C  CA    . ILE A 1 4294 ? 234.612 194.231 185.812 1.00 23.86  ? 4294 ILE A CA    1 
ATOM   20334 C  C     . ILE A 1 4294 ? 234.102 194.479 184.399 1.00 22.40  ? 4294 ILE A C     1 
ATOM   20335 O  O     . ILE A 1 4294 ? 234.382 195.524 183.799 1.00 25.69  ? 4294 ILE A O     1 
ATOM   20336 C  CB    . ILE A 1 4294 ? 233.873 195.108 186.833 1.00 24.81  ? 4294 ILE A CB    1 
ATOM   20337 C  CG1   . ILE A 1 4294 ? 234.409 194.860 188.245 1.00 19.19  ? 4294 ILE A CG1   1 
ATOM   20338 C  CG2   . ILE A 1 4294 ? 232.379 194.836 186.785 1.00 19.39  ? 4294 ILE A CG2   1 
ATOM   20339 C  CD1   . ILE A 1 4294 ? 234.236 193.443 188.727 1.00 21.84  ? 4294 ILE A CD1   1 
ATOM   20340 N  N     . GLN A 1 4295 ? 233.354 193.522 183.864 1.00 28.90  ? 4295 GLN A N     1 
ATOM   20341 C  CA    . GLN A 1 4295 ? 232.879 193.579 182.490 1.00 27.23  ? 4295 GLN A CA    1 
ATOM   20342 C  C     . GLN A 1 4295 ? 231.406 193.963 182.441 1.00 25.00  ? 4295 GLN A C     1 
ATOM   20343 O  O     . GLN A 1 4295 ? 230.603 193.507 183.259 1.00 28.32  ? 4295 GLN A O     1 
ATOM   20344 C  CB    . GLN A 1 4295 ? 233.085 192.235 181.786 1.00 31.48  ? 4295 GLN A CB    1 
ATOM   20345 C  CG    . GLN A 1 4295 ? 234.389 192.139 181.019 1.00 36.41  ? 4295 GLN A CG    1 
ATOM   20346 C  CD    . GLN A 1 4295 ? 234.406 193.031 179.796 1.00 40.11  ? 4295 GLN A CD    1 
ATOM   20347 O  OE1   . GLN A 1 4295 ? 235.309 193.851 179.623 1.00 35.87  ? 4295 GLN A OE1   1 
ATOM   20348 N  NE2   . GLN A 1 4295 ? 233.403 192.879 178.940 1.00 31.72  ? 4295 GLN A NE2   1 
ATOM   20349 N  N     . MET A 1 4296 ? 231.066 194.808 181.479 1.00 24.65  ? 4296 MET A N     1 
ATOM   20350 C  CA    . MET A 1 4296 ? 229.675 195.179 181.254 1.00 20.41  ? 4296 MET A CA    1 
ATOM   20351 C  C     . MET A 1 4296 ? 228.898 193.966 180.757 1.00 24.81  ? 4296 MET A C     1 
ATOM   20352 O  O     . MET A 1 4296 ? 229.319 193.325 179.787 1.00 31.05  ? 4296 MET A O     1 
ATOM   20353 C  CB    . MET A 1 4296 ? 229.604 196.310 180.232 1.00 23.77  ? 4296 MET A CB    1 
ATOM   20354 C  CG    . MET A 1 4296 ? 228.240 196.950 180.041 1.00 26.03  ? 4296 MET A CG    1 
ATOM   20355 S  SD    . MET A 1 4296 ? 227.474 197.527 181.561 1.00 25.93  ? 4296 MET A SD    1 
ATOM   20356 C  CE    . MET A 1 4296 ? 225.779 197.691 181.016 1.00 20.02  ? 4296 MET A CE    1 
ATOM   20357 N  N     . PRO A 1 4297 ? 227.780 193.611 181.388 1.00 24.04  ? 4297 PRO A N     1 
ATOM   20358 C  CA    . PRO A 1 4297 ? 226.983 192.484 180.891 1.00 25.12  ? 4297 PRO A CA    1 
ATOM   20359 C  C     . PRO A 1 4297 ? 226.481 192.738 179.478 1.00 29.46  ? 4297 PRO A C     1 
ATOM   20360 O  O     . PRO A 1 4297 ? 226.152 193.864 179.101 1.00 33.16  ? 4297 PRO A O     1 
ATOM   20361 C  CB    . PRO A 1 4297 ? 225.821 192.395 181.889 1.00 19.00  ? 4297 PRO A CB    1 
ATOM   20362 C  CG    . PRO A 1 4297 ? 226.251 193.183 183.070 1.00 18.44  ? 4297 PRO A CG    1 
ATOM   20363 C  CD    . PRO A 1 4297 ? 227.188 194.227 182.585 1.00 18.67  ? 4297 PRO A CD    1 
ATOM   20364 N  N     . ASP A 1 4298 ? 226.427 191.667 178.693 1.00 30.53  ? 4298 ASP A N     1 
ATOM   20365 C  CA    . ASP A 1 4298 ? 225.983 191.734 177.308 1.00 36.41  ? 4298 ASP A CA    1 
ATOM   20366 C  C     . ASP A 1 4298 ? 224.475 191.597 177.156 1.00 40.82  ? 4298 ASP A C     1 
ATOM   20367 O  O     . ASP A 1 4298 ? 223.973 191.648 176.028 1.00 41.00  ? 4298 ASP A O     1 
ATOM   20368 C  CB    . ASP A 1 4298 ? 226.691 190.657 176.477 1.00 38.97  ? 4298 ASP A CB    1 
ATOM   20369 C  CG    . ASP A 1 4298 ? 226.362 189.243 176.936 1.00 52.32  ? 4298 ASP A CG    1 
ATOM   20370 O  OD1   . ASP A 1 4298 ? 225.617 189.080 177.926 1.00 51.11  ? 4298 ASP A OD1   1 
ATOM   20371 O  OD2   . ASP A 1 4298 ? 226.848 188.288 176.296 1.00 57.92  ? 4298 ASP A OD2   1 
ATOM   20372 N  N     . GLY A 1 4299 ? 223.745 191.431 178.256 1.00 34.16  ? 4299 GLY A N     1 
ATOM   20373 C  CA    . GLY A 1 4299 ? 222.328 191.164 178.166 1.00 34.25  ? 4299 GLY A CA    1 
ATOM   20374 C  C     . GLY A 1 4299 ? 221.516 192.381 177.768 1.00 36.44  ? 4299 GLY A C     1 
ATOM   20375 O  O     . GLY A 1 4299 ? 221.985 193.519 177.774 1.00 44.43  ? 4299 GLY A O     1 
ATOM   20376 N  N     . ILE A 1 4300 ? 220.260 192.119 177.410 1.00 26.32  ? 4300 ILE A N     1 
ATOM   20377 C  CA    . ILE A 1 4300 ? 219.308 193.158 177.038 1.00 26.23  ? 4300 ILE A CA    1 
ATOM   20378 C  C     . ILE A 1 4300 ? 218.011 193.069 177.824 1.00 30.17  ? 4300 ILE A C     1 
ATOM   20379 O  O     . ILE A 1 4300 ? 217.073 193.818 177.532 1.00 30.13  ? 4300 ILE A O     1 
ATOM   20380 C  CB    . ILE A 1 4300 ? 219.013 193.136 175.524 1.00 26.94  ? 4300 ILE A CB    1 
ATOM   20381 C  CG1   . ILE A 1 4300 ? 218.374 191.807 175.122 1.00 37.29  ? 4300 ILE A CG1   1 
ATOM   20382 C  CG2   . ILE A 1 4300 ? 220.282 193.386 174.725 1.00 28.38  ? 4300 ILE A CG2   1 
ATOM   20383 C  CD1   . ILE A 1 4300 ? 217.843 191.790 173.707 1.00 40.65  ? 4300 ILE A CD1   1 
ATOM   20384 N  N     . ARG A 1 4301 ? 217.924 192.181 178.810 1.00 32.87  ? 4301 ARG A N     1 
ATOM   20385 C  CA    . ARG A 1 4301 ? 216.729 192.012 179.619 1.00 29.69  ? 4301 ARG A CA    1 
ATOM   20386 C  C     . ARG A 1 4301 ? 217.078 192.137 181.096 1.00 25.08  ? 4301 ARG A C     1 
ATOM   20387 O  O     . ARG A 1 4301 ? 218.218 191.905 181.509 1.00 25.53  ? 4301 ARG A O     1 
ATOM   20388 C  CB    . ARG A 1 4301 ? 216.058 190.662 179.345 1.00 32.53  ? 4301 ARG A CB    1 
ATOM   20389 C  CG    . ARG A 1 4301 ? 215.447 190.550 177.959 1.00 39.93  ? 4301 ARG A CG    1 
ATOM   20390 C  CD    . ARG A 1 4301 ? 214.629 189.279 177.817 1.00 47.18  ? 4301 ARG A CD    1 
ATOM   20391 N  NE    . ARG A 1 4301 ? 215.455 188.084 177.941 1.00 51.71  ? 4301 ARG A NE    1 
ATOM   20392 C  CZ    . ARG A 1 4301 ? 216.082 187.499 176.930 1.00 61.11  ? 4301 ARG A CZ    1 
ATOM   20393 N  NH1   . ARG A 1 4301 ? 215.998 187.973 175.697 1.00 66.42  ? 4301 ARG A NH1   1 
ATOM   20394 N  NH2   . ARG A 1 4301 ? 216.811 186.412 177.162 1.00 59.82  ? 4301 ARG A NH2   1 
ATOM   20395 N  N     . ARG A 1 4302 ? 216.072 192.511 181.891 1.00 22.04  ? 4302 ARG A N     1 
ATOM   20396 C  CA    . ARG A 1 4302 ? 216.296 192.776 183.310 1.00 20.42  ? 4302 ARG A CA    1 
ATOM   20397 C  C     . ARG A 1 4302 ? 216.779 191.533 184.047 1.00 22.66  ? 4302 ARG A C     1 
ATOM   20398 O  O     . ARG A 1 4302 ? 217.691 191.612 184.882 1.00 24.74  ? 4302 ARG A O     1 
ATOM   20399 C  CB    . ARG A 1 4302 ? 215.016 193.306 183.952 1.00 21.76  ? 4302 ARG A CB    1 
ATOM   20400 C  CG    . ARG A 1 4302 ? 215.080 193.367 185.467 1.00 19.75  ? 4302 ARG A CG    1 
ATOM   20401 C  CD    . ARG A 1 4302 ? 213.698 193.334 186.088 1.00 25.02  ? 4302 ARG A CD    1 
ATOM   20402 N  NE    . ARG A 1 4302 ? 213.762 193.242 187.541 1.00 30.56  ? 4302 ARG A NE    1 
ATOM   20403 C  CZ    . ARG A 1 4302 ? 214.016 192.125 188.210 1.00 30.64  ? 4302 ARG A CZ    1 
ATOM   20404 N  NH1   . ARG A 1 4302 ? 214.219 190.977 187.585 1.00 25.22  ? 4302 ARG A NH1   1 
ATOM   20405 N  NH2   . ARG A 1 4302 ? 214.065 192.161 189.538 1.00 21.70  ? 4302 ARG A NH2   1 
ATOM   20406 N  N     . GLU A 1 4303 ? 216.172 190.379 183.762 1.00 24.45  ? 4303 GLU A N     1 
ATOM   20407 C  CA    . GLU A 1 4303 ? 216.537 189.163 184.481 1.00 21.89  ? 4303 GLU A CA    1 
ATOM   20408 C  C     . GLU A 1 4303 ? 217.989 188.787 184.218 1.00 21.46  ? 4303 GLU A C     1 
ATOM   20409 O  O     . GLU A 1 4303 ? 218.671 188.266 185.106 1.00 24.04  ? 4303 GLU A O     1 
ATOM   20410 C  CB    . GLU A 1 4303 ? 215.588 188.021 184.105 1.00 26.42  ? 4303 GLU A CB    1 
ATOM   20411 C  CG    . GLU A 1 4303 ? 215.917 187.292 182.811 1.00 33.60  ? 4303 GLU A CG    1 
ATOM   20412 C  CD    . GLU A 1 4303 ? 215.329 187.967 181.588 1.00 44.36  ? 4303 GLU A CD    1 
ATOM   20413 O  OE1   . GLU A 1 4303 ? 215.692 187.573 180.460 1.00 44.10  ? 4303 GLU A OE1   1 
ATOM   20414 O  OE2   . GLU A 1 4303 ? 214.503 188.889 181.754 1.00 41.09  ? 4303 GLU A OE2   1 
ATOM   20415 N  N     . GLU A 1 4304 ? 218.491 189.078 183.018 1.00 24.20  ? 4304 GLU A N     1 
ATOM   20416 C  CA    . GLU A 1 4304 ? 219.886 188.789 182.709 1.00 24.18  ? 4304 GLU A CA    1 
ATOM   20417 C  C     . GLU A 1 4304 ? 220.827 189.692 183.499 1.00 22.51  ? 4304 GLU A C     1 
ATOM   20418 O  O     . GLU A 1 4304 ? 221.869 189.241 183.988 1.00 24.64  ? 4304 GLU A O     1 
ATOM   20419 C  CB    . GLU A 1 4304 ? 220.114 188.921 181.204 1.00 21.20  ? 4304 GLU A CB    1 
ATOM   20420 C  CG    . GLU A 1 4304 ? 219.378 187.851 180.407 1.00 36.17  ? 4304 GLU A CG    1 
ATOM   20421 C  CD    . GLU A 1 4304 ? 219.573 187.976 178.911 1.00 52.87  ? 4304 GLU A CD    1 
ATOM   20422 O  OE1   . GLU A 1 4304 ? 220.180 188.968 178.468 1.00 49.46  ? 4304 GLU A OE1   1 
ATOM   20423 O  OE2   . GLU A 1 4304 ? 219.120 187.074 178.176 1.00 65.00  ? 4304 GLU A OE2   1 
ATOM   20424 N  N     . PHE A 1 4305 ? 220.470 190.971 183.652 1.00 22.64  ? 4305 PHE A N     1 
ATOM   20425 C  CA    . PHE A 1 4305 ? 221.269 191.864 184.486 1.00 18.27  ? 4305 PHE A CA    1 
ATOM   20426 C  C     . PHE A 1 4305 ? 221.261 191.420 185.944 1.00 18.54  ? 4305 PHE A C     1 
ATOM   20427 O  O     . PHE A 1 4305 ? 222.304 191.438 186.610 1.00 17.50  ? 4305 PHE A O     1 
ATOM   20428 C  CB    . PHE A 1 4305 ? 220.760 193.299 184.359 1.00 14.36  ? 4305 PHE A CB    1 
ATOM   20429 C  CG    . PHE A 1 4305 ? 221.020 193.915 183.017 1.00 15.74  ? 4305 PHE A CG    1 
ATOM   20430 C  CD1   . PHE A 1 4305 ? 222.309 194.003 182.521 1.00 15.56  ? 4305 PHE A CD1   1 
ATOM   20431 C  CD2   . PHE A 1 4305 ? 219.978 194.402 182.247 1.00 18.52  ? 4305 PHE A CD2   1 
ATOM   20432 C  CE1   . PHE A 1 4305 ? 222.554 194.567 181.286 1.00 15.04  ? 4305 PHE A CE1   1 
ATOM   20433 C  CE2   . PHE A 1 4305 ? 220.218 194.964 181.010 1.00 18.17  ? 4305 PHE A CE2   1 
ATOM   20434 C  CZ    . PHE A 1 4305 ? 221.508 195.047 180.529 1.00 16.04  ? 4305 PHE A CZ    1 
ATOM   20435 N  N     . VAL A 1 4306 ? 220.097 191.020 186.460 1.00 17.09  ? 4306 VAL A N     1 
ATOM   20436 C  CA    . VAL A 1 4306 ? 220.031 190.544 187.841 1.00 18.66  ? 4306 VAL A CA    1 
ATOM   20437 C  C     . VAL A 1 4306 ? 220.868 189.281 188.006 1.00 19.81  ? 4306 VAL A C     1 
ATOM   20438 O  O     . VAL A 1 4306 ? 221.569 189.106 189.011 1.00 19.20  ? 4306 VAL A O     1 
ATOM   20439 C  CB    . VAL A 1 4306 ? 218.566 190.317 188.261 1.00 20.52  ? 4306 VAL A CB    1 
ATOM   20440 C  CG1   . VAL A 1 4306 ? 218.500 189.724 189.660 1.00 16.24  ? 4306 VAL A CG1   1 
ATOM   20441 C  CG2   . VAL A 1 4306 ? 217.789 191.620 188.193 1.00 19.24  ? 4306 VAL A CG2   1 
ATOM   20442 N  N     . GLN A 1 4307 ? 220.814 188.386 187.017 1.00 21.88  ? 4307 GLN A N     1 
ATOM   20443 C  CA    . GLN A 1 4307 ? 221.597 187.158 187.064 1.00 20.71  ? 4307 GLN A CA    1 
ATOM   20444 C  C     . GLN A 1 4307 ? 223.092 187.458 187.020 1.00 20.15  ? 4307 GLN A C     1 
ATOM   20445 O  O     . GLN A 1 4307 ? 223.892 186.759 187.653 1.00 24.30  ? 4307 GLN A O     1 
ATOM   20446 C  CB    . GLN A 1 4307 ? 221.165 186.249 185.909 1.00 28.49  ? 4307 GLN A CB    1 
ATOM   20447 C  CG    . GLN A 1 4307 ? 221.730 184.838 185.898 1.00 41.01  ? 4307 GLN A CG    1 
ATOM   20448 C  CD    . GLN A 1 4307 ? 223.083 184.740 185.230 1.00 48.46  ? 4307 GLN A CD    1 
ATOM   20449 O  OE1   . GLN A 1 4307 ? 223.403 185.514 184.328 1.00 50.89  ? 4307 GLN A OE1   1 
ATOM   20450 N  NE2   . GLN A 1 4307 ? 223.872 183.760 185.645 1.00 44.19  ? 4307 GLN A NE2   1 
ATOM   20451 N  N     . TRP A 1 4308 ? 223.488 188.493 186.277 1.00 19.32  ? 4308 TRP A N     1 
ATOM   20452 C  CA    . TRP A 1 4308 ? 224.877 188.943 186.309 1.00 18.24  ? 4308 TRP A CA    1 
ATOM   20453 C  C     . TRP A 1 4308 ? 225.256 189.476 187.686 1.00 13.77  ? 4308 TRP A C     1 
ATOM   20454 O  O     . TRP A 1 4308 ? 226.361 189.221 188.177 1.00 14.16  ? 4308 TRP A O     1 
ATOM   20455 C  CB    . TRP A 1 4308 ? 225.110 190.017 185.247 1.00 15.80  ? 4308 TRP A CB    1 
ATOM   20456 C  CG    . TRP A 1 4308 ? 226.502 190.585 185.258 1.00 16.28  ? 4308 TRP A CG    1 
ATOM   20457 C  CD1   . TRP A 1 4308 ? 227.570 190.145 184.537 1.00 14.54  ? 4308 TRP A CD1   1 
ATOM   20458 C  CD2   . TRP A 1 4308 ? 226.971 191.701 186.030 1.00 16.06  ? 4308 TRP A CD2   1 
ATOM   20459 N  NE1   . TRP A 1 4308 ? 228.675 190.915 184.809 1.00 16.21  ? 4308 TRP A NE1   1 
ATOM   20460 C  CE2   . TRP A 1 4308 ? 228.332 191.877 185.722 1.00 14.18  ? 4308 TRP A CE2   1 
ATOM   20461 C  CE3   . TRP A 1 4308 ? 226.369 192.566 186.948 1.00 12.65  ? 4308 TRP A CE3   1 
ATOM   20462 C  CZ2   . TRP A 1 4308 ? 229.104 192.882 186.300 1.00 12.44  ? 4308 TRP A CZ2   1 
ATOM   20463 C  CZ3   . TRP A 1 4308 ? 227.137 193.561 187.523 1.00 9.32   ? 4308 TRP A CZ3   1 
ATOM   20464 C  CH2   . TRP A 1 4308 ? 228.488 193.711 187.195 1.00 12.03  ? 4308 TRP A CH2   1 
ATOM   20465 N  N     . VAL A 1 4309 ? 224.357 190.237 188.314 1.00 14.01  ? 4309 VAL A N     1 
ATOM   20466 C  CA    . VAL A 1 4309 ? 224.644 190.784 189.638 1.00 12.90  ? 4309 VAL A CA    1 
ATOM   20467 C  C     . VAL A 1 4309 ? 224.798 189.660 190.653 1.00 16.83  ? 4309 VAL A C     1 
ATOM   20468 O  O     . VAL A 1 4309 ? 225.619 189.741 191.575 1.00 20.29  ? 4309 VAL A O     1 
ATOM   20469 C  CB    . VAL A 1 4309 ? 223.547 191.782 190.057 1.00 15.18  ? 4309 VAL A CB    1 
ATOM   20470 C  CG1   . VAL A 1 4309 ? 223.782 192.272 191.479 1.00 7.12   ? 4309 VAL A CG1   1 
ATOM   20471 C  CG2   . VAL A 1 4309 ? 223.501 192.955 189.099 1.00 10.08  ? 4309 VAL A CG2   1 
ATOM   20472 N  N     . GLU A 1 4310 ? 224.015 188.591 190.498 1.00 18.96  ? 4310 GLU A N     1 
ATOM   20473 C  CA    . GLU A 1 4310 ? 224.076 187.480 191.442 1.00 15.09  ? 4310 GLU A CA    1 
ATOM   20474 C  C     . GLU A 1 4310 ? 225.419 186.760 191.394 1.00 17.63  ? 4310 GLU A C     1 
ATOM   20475 O  O     . GLU A 1 4310 ? 225.876 186.238 192.418 1.00 22.45  ? 4310 GLU A O     1 
ATOM   20476 C  CB    . GLU A 1 4310 ? 222.932 186.506 191.172 1.00 16.04  ? 4310 GLU A CB    1 
ATOM   20477 C  CG    . GLU A 1 4310 ? 221.560 187.086 191.471 1.00 21.29  ? 4310 GLU A CG    1 
ATOM   20478 C  CD    . GLU A 1 4310 ? 220.435 186.117 191.179 1.00 38.95  ? 4310 GLU A CD    1 
ATOM   20479 O  OE1   . GLU A 1 4310 ? 220.710 185.032 190.624 1.00 48.55  ? 4310 GLU A OE1   1 
ATOM   20480 O  OE2   . GLU A 1 4310 ? 219.273 186.440 191.502 1.00 36.19  ? 4310 GLU A OE2   1 
ATOM   20481 N  N     . LEU A 1 4311 ? 226.067 186.715 190.230 1.00 17.16  ? 4311 LEU A N     1 
ATOM   20482 C  CA    . LEU A 1 4311 ? 227.352 186.041 190.091 1.00 20.50  ? 4311 LEU A CA    1 
ATOM   20483 C  C     . LEU A 1 4311 ? 228.541 186.963 190.317 1.00 24.16  ? 4311 LEU A C     1 
ATOM   20484 O  O     . LEU A 1 4311 ? 229.624 186.697 189.782 1.00 26.36  ? 4311 LEU A O     1 
ATOM   20485 C  CB    . LEU A 1 4311 ? 227.478 185.385 188.715 1.00 19.70  ? 4311 LEU A CB    1 
ATOM   20486 C  CG    . LEU A 1 4311 ? 226.303 184.654 188.078 1.00 28.68  ? 4311 LEU A CG    1 
ATOM   20487 C  CD1   . LEU A 1 4311 ? 226.798 183.952 186.829 1.00 29.26  ? 4311 LEU A CD1   1 
ATOM   20488 C  CD2   . LEU A 1 4311 ? 225.695 183.657 189.049 1.00 24.77  ? 4311 LEU A CD2   1 
ATOM   20489 N  N     . LEU A 1 4312 ? 228.375 188.036 191.081 1.00 17.14  ? 4312 LEU A N     1 
ATOM   20490 C  CA    . LEU A 1 4312 ? 229.516 188.871 191.407 1.00 18.09  ? 4312 LEU A CA    1 
ATOM   20491 C  C     . LEU A 1 4312 ? 230.480 188.102 192.311 1.00 22.87  ? 4312 LEU A C     1 
ATOM   20492 O  O     . LEU A 1 4312 ? 230.055 187.306 193.152 1.00 28.11  ? 4312 LEU A O     1 
ATOM   20493 C  CB    . LEU A 1 4312 ? 229.065 190.167 192.075 1.00 16.46  ? 4312 LEU A CB    1 
ATOM   20494 C  CG    . LEU A 1 4312 ? 228.651 191.262 191.086 1.00 14.27  ? 4312 LEU A CG    1 
ATOM   20495 C  CD1   . LEU A 1 4312 ? 228.335 192.564 191.800 1.00 12.39  ? 4312 LEU A CD1   1 
ATOM   20496 C  CD2   . LEU A 1 4312 ? 229.729 191.481 190.034 1.00 13.95  ? 4312 LEU A CD2   1 
ATOM   20497 N  N     . PRO A 1 4313 ? 231.789 188.325 192.154 1.00 18.81  ? 4313 PRO A N     1 
ATOM   20498 C  CA    . PRO A 1 4313 ? 232.773 187.435 192.794 1.00 25.21  ? 4313 PRO A CA    1 
ATOM   20499 C  C     . PRO A 1 4313 ? 232.746 187.442 194.314 1.00 33.22  ? 4313 PRO A C     1 
ATOM   20500 O  O     . PRO A 1 4313 ? 233.353 186.553 194.922 1.00 39.15  ? 4313 PRO A O     1 
ATOM   20501 C  CB    . PRO A 1 4313 ? 234.116 187.959 192.263 1.00 24.32  ? 4313 PRO A CB    1 
ATOM   20502 C  CG    . PRO A 1 4313 ? 233.766 188.727 191.026 1.00 27.01  ? 4313 PRO A CG    1 
ATOM   20503 C  CD    . PRO A 1 4313 ? 232.434 189.336 191.304 1.00 21.74  ? 4313 PRO A CD    1 
ATOM   20504 N  N     . ASP A 1 4314 ? 232.071 188.406 194.941 1.00 31.38  ? 4314 ASP A N     1 
ATOM   20505 C  CA    . ASP A 1 4314 ? 232.055 188.543 196.399 1.00 35.06  ? 4314 ASP A CA    1 
ATOM   20506 C  C     . ASP A 1 4314 ? 233.478 188.735 196.927 1.00 35.56  ? 4314 ASP A C     1 
ATOM   20507 O  O     . ASP A 1 4314 ? 233.853 188.256 197.998 1.00 33.86  ? 4314 ASP A O     1 
ATOM   20508 C  CB    . ASP A 1 4314 ? 231.357 187.346 197.058 1.00 40.46  ? 4314 ASP A CB    1 
ATOM   20509 C  CG    . ASP A 1 4314 ? 231.184 187.512 198.558 1.00 58.87  ? 4314 ASP A CG    1 
ATOM   20510 O  OD1   . ASP A 1 4314 ? 230.312 188.305 198.974 1.00 61.11  ? 4314 ASP A OD1   1 
ATOM   20511 O  OD2   . ASP A 1 4314 ? 231.910 186.841 199.322 1.00 59.45  ? 4314 ASP A OD2   1 
ATOM   20512 N  N     . THR A 1 4315 ? 234.281 189.451 196.144 1.00 33.81  ? 4315 THR A N     1 
ATOM   20513 C  CA    . THR A 1 4315 ? 235.638 189.834 196.511 1.00 20.25  ? 4315 THR A CA    1 
ATOM   20514 C  C     . THR A 1 4315 ? 235.814 191.331 196.321 1.00 21.20  ? 4315 THR A C     1 
ATOM   20515 O  O     . THR A 1 4315 ? 236.806 191.793 195.749 1.00 28.32  ? 4315 THR A O     1 
ATOM   20516 C  CB    . THR A 1 4315 ? 236.680 189.065 195.696 1.00 25.87  ? 4315 THR A CB    1 
ATOM   20517 O  OG1   . THR A 1 4315 ? 236.609 189.468 194.322 1.00 36.02  ? 4315 THR A OG1   1 
ATOM   20518 C  CG2   . THR A 1 4315 ? 236.444 187.566 195.789 1.00 28.88  ? 4315 THR A CG2   1 
ATOM   20519 N  N     . GLN A 1 4316 ? 234.841 192.107 196.792 1.00 18.13  ? 4316 GLN A N     1 
ATOM   20520 C  CA    . GLN A 1 4316 ? 234.836 193.542 196.543 1.00 13.31  ? 4316 GLN A CA    1 
ATOM   20521 C  C     . GLN A 1 4316 ? 235.993 194.230 197.252 1.00 14.53  ? 4316 GLN A C     1 
ATOM   20522 O  O     . GLN A 1 4316 ? 236.288 193.954 198.418 1.00 18.31  ? 4316 GLN A O     1 
ATOM   20523 C  CB    . GLN A 1 4316 ? 233.513 194.157 196.992 1.00 13.03  ? 4316 GLN A CB    1 
ATOM   20524 C  CG    . GLN A 1 4316 ? 233.311 195.581 196.511 1.00 13.15  ? 4316 GLN A CG    1 
ATOM   20525 C  CD    . GLN A 1 4316 ? 232.283 196.332 197.327 1.00 15.15  ? 4316 GLN A CD    1 
ATOM   20526 O  OE1   . GLN A 1 4316 ? 231.110 195.964 197.358 1.00 16.94  ? 4316 GLN A OE1   1 
ATOM   20527 N  NE2   . GLN A 1 4316 ? 232.719 197.392 197.996 1.00 15.36  ? 4316 GLN A NE2   1 
ATOM   20528 N  N     . THR A 1 4317 ? 236.640 195.133 196.535 1.00 16.11  ? 4317 THR A N     1 
ATOM   20529 C  CA    . THR A 1 4317 ? 237.738 195.953 197.016 1.00 13.70  ? 4317 THR A CA    1 
ATOM   20530 C  C     . THR A 1 4317 ? 237.443 197.395 196.647 1.00 13.55  ? 4317 THR A C     1 
ATOM   20531 O  O     . THR A 1 4317 ? 236.633 197.657 195.751 1.00 14.79  ? 4317 THR A O     1 
ATOM   20532 C  CB    . THR A 1 4317 ? 239.075 195.513 196.398 1.00 14.04  ? 4317 THR A CB    1 
ATOM   20533 O  OG1   . THR A 1 4317 ? 238.935 195.406 194.978 1.00 17.08  ? 4317 THR A OG1   1 
ATOM   20534 C  CG2   . THR A 1 4317 ? 239.508 194.172 196.961 1.00 14.81  ? 4317 THR A CG2   1 
ATOM   20535 N  N     . PRO A 1 4318 ? 238.068 198.359 197.327 1.00 16.30  ? 4318 PRO A N     1 
ATOM   20536 C  CA    . PRO A 1 4318 ? 237.858 199.765 196.948 1.00 11.85  ? 4318 PRO A CA    1 
ATOM   20537 C  C     . PRO A 1 4318 ? 238.254 200.071 195.514 1.00 11.64  ? 4318 PRO A C     1 
ATOM   20538 O  O     . PRO A 1 4318 ? 237.810 201.089 194.970 1.00 14.31  ? 4318 PRO A O     1 
ATOM   20539 C  CB    . PRO A 1 4318 ? 238.725 200.540 197.951 1.00 13.20  ? 4318 PRO A CB    1 
ATOM   20540 C  CG    . PRO A 1 4318 ? 239.567 199.511 198.646 1.00 15.38  ? 4318 PRO A CG    1 
ATOM   20541 C  CD    . PRO A 1 4318 ? 238.806 198.238 198.592 1.00 12.52  ? 4318 PRO A CD    1 
ATOM   20542 N  N     . SER A 1 4319 ? 239.073 199.224 194.885 1.00 12.07  ? 4319 SER A N     1 
ATOM   20543 C  CA    . SER A 1 4319 ? 239.361 199.381 193.464 1.00 11.89  ? 4319 SER A CA    1 
ATOM   20544 C  C     . SER A 1 4319 ? 238.117 199.216 192.603 1.00 12.26  ? 4319 SER A C     1 
ATOM   20545 O  O     . SER A 1 4319 ? 238.072 199.756 191.492 1.00 16.77  ? 4319 SER A O     1 
ATOM   20546 C  CB    . SER A 1 4319 ? 240.430 198.381 193.031 1.00 18.61  ? 4319 SER A CB    1 
ATOM   20547 O  OG    . SER A 1 4319 ? 240.089 197.067 193.433 1.00 25.91  ? 4319 SER A OG    1 
ATOM   20548 N  N     . TRP A 1 4320 ? 237.110 198.477 193.082 1.00 11.20  ? 4320 TRP A N     1 
ATOM   20549 C  CA    . TRP A 1 4320 ? 235.825 198.444 192.390 1.00 10.19  ? 4320 TRP A CA    1 
ATOM   20550 C  C     . TRP A 1 4320 ? 235.229 199.836 192.280 1.00 8.91   ? 4320 TRP A C     1 
ATOM   20551 O  O     . TRP A 1 4320 ? 234.524 200.141 191.311 1.00 9.52   ? 4320 TRP A O     1 
ATOM   20552 C  CB    . TRP A 1 4320 ? 234.842 197.536 193.130 1.00 12.41  ? 4320 TRP A CB    1 
ATOM   20553 C  CG    . TRP A 1 4320 ? 235.054 196.069 192.951 1.00 11.02  ? 4320 TRP A CG    1 
ATOM   20554 C  CD1   . TRP A 1 4320 ? 236.239 195.427 192.764 1.00 12.49  ? 4320 TRP A CD1   1 
ATOM   20555 C  CD2   . TRP A 1 4320 ? 234.045 195.055 192.959 1.00 13.05  ? 4320 TRP A CD2   1 
ATOM   20556 N  NE1   . TRP A 1 4320 ? 236.032 194.075 192.649 1.00 16.76  ? 4320 TRP A NE1   1 
ATOM   20557 C  CE2   . TRP A 1 4320 ? 234.691 193.821 192.766 1.00 16.24  ? 4320 TRP A CE2   1 
ATOM   20558 C  CE3   . TRP A 1 4320 ? 232.654 195.073 193.109 1.00 13.00  ? 4320 TRP A CE3   1 
ATOM   20559 C  CZ2   . TRP A 1 4320 ? 233.997 192.614 192.717 1.00 17.67  ? 4320 TRP A CZ2   1 
ATOM   20560 C  CZ3   . TRP A 1 4320 ? 231.967 193.876 193.063 1.00 11.49  ? 4320 TRP A CZ3   1 
ATOM   20561 C  CH2   . TRP A 1 4320 ? 232.638 192.663 192.867 1.00 13.05  ? 4320 TRP A CH2   1 
ATOM   20562 N  N     . LEU A 1 4321 ? 235.497 200.687 193.264 1.00 7.76   ? 4321 LEU A N     1 
ATOM   20563 C  CA    . LEU A 1 4321 ? 234.938 202.025 193.350 1.00 6.69   ? 4321 LEU A CA    1 
ATOM   20564 C  C     . LEU A 1 4321 ? 235.797 203.067 192.649 1.00 8.54   ? 4321 LEU A C     1 
ATOM   20565 O  O     . LEU A 1 4321 ? 235.388 204.228 192.557 1.00 11.07  ? 4321 LEU A O     1 
ATOM   20566 C  CB    . LEU A 1 4321 ? 234.772 202.410 194.822 1.00 9.45   ? 4321 LEU A CB    1 
ATOM   20567 C  CG    . LEU A 1 4321 ? 233.781 201.566 195.622 1.00 6.76   ? 4321 LEU A CG    1 
ATOM   20568 C  CD1   . LEU A 1 4321 ? 233.813 201.949 197.091 1.00 7.03   ? 4321 LEU A CD1   1 
ATOM   20569 C  CD2   . LEU A 1 4321 ? 232.387 201.705 195.059 1.00 6.76   ? 4321 LEU A CD2   1 
ATOM   20570 N  N     . GLY A 1 4322 ? 236.969 202.681 192.151 1.00 9.08   ? 4322 GLY A N     1 
ATOM   20571 C  CA    . GLY A 1 4322 ? 237.935 203.613 191.616 1.00 9.09   ? 4322 GLY A CA    1 
ATOM   20572 C  C     . GLY A 1 4322 ? 238.972 204.078 192.614 1.00 11.95  ? 4322 GLY A C     1 
ATOM   20573 O  O     . GLY A 1 4322 ? 239.966 204.690 192.209 1.00 14.80  ? 4322 GLY A O     1 
ATOM   20574 N  N     . LEU A 1 4323 ? 238.770 203.806 193.898 1.00 10.70  ? 4323 LEU A N     1 
ATOM   20575 C  CA    . LEU A 1 4323 ? 239.703 204.188 194.942 1.00 9.30   ? 4323 LEU A CA    1 
ATOM   20576 C  C     . LEU A 1 4323 ? 240.880 203.218 195.000 1.00 12.65  ? 4323 LEU A C     1 
ATOM   20577 O  O     . LEU A 1 4323 ? 240.801 202.100 194.485 1.00 13.63  ? 4323 LEU A O     1 
ATOM   20578 C  CB    . LEU A 1 4323 ? 238.986 204.228 196.288 1.00 8.92   ? 4323 LEU A CB    1 
ATOM   20579 C  CG    . LEU A 1 4323 ? 237.975 205.354 196.495 1.00 10.00  ? 4323 LEU A CG    1 
ATOM   20580 C  CD1   . LEU A 1 4323 ? 236.870 204.911 197.433 1.00 7.49   ? 4323 LEU A CD1   1 
ATOM   20581 C  CD2   . LEU A 1 4323 ? 238.665 206.595 197.030 1.00 8.92   ? 4323 LEU A CD2   1 
ATOM   20582 N  N     . PRO A 1 4324 ? 241.993 203.626 195.611 1.00 14.73  ? 4324 PRO A N     1 
ATOM   20583 C  CA    . PRO A 1 4324 ? 243.099 202.685 195.817 1.00 11.18  ? 4324 PRO A CA    1 
ATOM   20584 C  C     . PRO A 1 4324 ? 242.696 201.559 196.757 1.00 15.22  ? 4324 PRO A C     1 
ATOM   20585 O  O     . PRO A 1 4324 ? 241.818 201.713 197.609 1.00 18.35  ? 4324 PRO A O     1 
ATOM   20586 C  CB    . PRO A 1 4324 ? 244.203 203.558 196.426 1.00 10.02  ? 4324 PRO A CB    1 
ATOM   20587 C  CG    . PRO A 1 4324 ? 243.492 204.746 196.977 1.00 10.65  ? 4324 PRO A CG    1 
ATOM   20588 C  CD    . PRO A 1 4324 ? 242.342 204.985 196.056 1.00 11.83  ? 4324 PRO A CD    1 
ATOM   20589 N  N     . ASN A 1 4325 ? 243.351 200.408 196.588 1.00 15.77  ? 4325 ASN A N     1 
ATOM   20590 C  CA    . ASN A 1 4325 ? 243.001 199.226 197.369 1.00 13.65  ? 4325 ASN A CA    1 
ATOM   20591 C  C     . ASN A 1 4325 ? 243.305 199.383 198.853 1.00 17.40  ? 4325 ASN A C     1 
ATOM   20592 O  O     . ASN A 1 4325 ? 242.674 198.707 199.672 1.00 24.85  ? 4325 ASN A O     1 
ATOM   20593 C  CB    . ASN A 1 4325 ? 243.732 197.999 196.824 1.00 20.15  ? 4325 ASN A CB    1 
ATOM   20594 C  CG    . ASN A 1 4325 ? 242.990 197.339 195.681 1.00 19.95  ? 4325 ASN A CG    1 
ATOM   20595 O  OD1   . ASN A 1 4325 ? 241.778 197.147 195.743 1.00 14.15  ? 4325 ASN A OD1   1 
ATOM   20596 N  ND2   . ASN A 1 4325 ? 243.717 196.978 194.631 1.00 27.75  ? 4325 ASN A ND2   1 
ATOM   20597 N  N     . ASN A 1 4326 ? 244.243 200.253 199.222 1.00 17.84  ? 4326 ASN A N     1 
ATOM   20598 C  CA    . ASN A 1 4326 ? 244.621 200.403 200.622 1.00 17.23  ? 4326 ASN A CA    1 
ATOM   20599 C  C     . ASN A 1 4326 ? 243.675 201.303 201.404 1.00 16.24  ? 4326 ASN A C     1 
ATOM   20600 O  O     . ASN A 1 4326 ? 243.857 201.453 202.618 1.00 18.70  ? 4326 ASN A O     1 
ATOM   20601 C  CB    . ASN A 1 4326 ? 246.054 200.935 200.728 1.00 16.65  ? 4326 ASN A CB    1 
ATOM   20602 C  CG    . ASN A 1 4326 ? 246.287 202.173 199.881 1.00 19.77  ? 4326 ASN A CG    1 
ATOM   20603 O  OD1   . ASN A 1 4326 ? 245.547 203.152 199.967 1.00 20.89  ? 4326 ASN A OD1   1 
ATOM   20604 N  ND2   . ASN A 1 4326 ? 247.324 202.133 199.055 1.00 27.04  ? 4326 ASN A ND2   1 
ATOM   20605 N  N     . ALA A 1 4327 ? 242.670 201.890 200.748 1.00 14.61  ? 4327 ALA A N     1 
ATOM   20606 C  CA    . ALA A 1 4327 ? 241.753 202.791 201.439 1.00 18.26  ? 4327 ALA A CA    1 
ATOM   20607 C  C     . ALA A 1 4327 ? 241.039 202.100 202.593 1.00 22.30  ? 4327 ALA A C     1 
ATOM   20608 O  O     . ALA A 1 4327 ? 240.739 202.738 203.609 1.00 21.46  ? 4327 ALA A O     1 
ATOM   20609 C  CB    . ALA A 1 4327 ? 240.731 203.358 200.454 1.00 11.96  ? 4327 ALA A CB    1 
ATOM   20610 N  N     . GLU A 1 4328 ? 240.762 200.806 202.462 1.00 23.40  ? 4328 GLU A N     1 
ATOM   20611 C  CA    . GLU A 1 4328 ? 240.103 200.054 203.518 1.00 18.47  ? 4328 GLU A CA    1 
ATOM   20612 C  C     . GLU A 1 4328 ? 241.069 199.520 204.566 1.00 18.15  ? 4328 GLU A C     1 
ATOM   20613 O  O     . GLU A 1 4328 ? 240.615 199.086 205.632 1.00 18.07  ? 4328 GLU A O     1 
ATOM   20614 C  CB    . GLU A 1 4328 ? 239.315 198.886 202.917 1.00 15.86  ? 4328 GLU A CB    1 
ATOM   20615 C  CG    . GLU A 1 4328 ? 240.163 197.924 202.102 1.00 18.62  ? 4328 GLU A CG    1 
ATOM   20616 C  CD    . GLU A 1 4328 ? 239.372 196.738 201.588 1.00 34.52  ? 4328 GLU A CD    1 
ATOM   20617 O  OE1   . GLU A 1 4328 ? 238.139 196.714 201.783 1.00 31.08  ? 4328 GLU A OE1   1 
ATOM   20618 O  OE2   . GLU A 1 4328 ? 239.983 195.827 200.990 1.00 35.09  ? 4328 GLU A OE2   1 
ATOM   20619 N  N     . ARG A 1 4329 ? 242.380 199.577 204.308 1.00 21.12  ? 4329 ARG A N     1 
ATOM   20620 C  CA    . ARG A 1 4329 ? 243.335 198.861 205.150 1.00 17.28  ? 4329 ARG A CA    1 
ATOM   20621 C  C     . ARG A 1 4329 ? 243.250 199.311 206.602 1.00 17.04  ? 4329 ARG A C     1 
ATOM   20622 O  O     . ARG A 1 4329 ? 243.272 198.482 207.518 1.00 20.44  ? 4329 ARG A O     1 
ATOM   20623 C  CB    . ARG A 1 4329 ? 244.754 199.047 204.616 1.00 18.39  ? 4329 ARG A CB    1 
ATOM   20624 C  CG    . ARG A 1 4329 ? 245.835 198.678 205.617 1.00 19.19  ? 4329 ARG A CG    1 
ATOM   20625 C  CD    . ARG A 1 4329 ? 247.176 198.473 204.945 1.00 22.58  ? 4329 ARG A CD    1 
ATOM   20626 N  NE    . ARG A 1 4329 ? 247.154 197.351 204.016 1.00 30.38  ? 4329 ARG A NE    1 
ATOM   20627 C  CZ    . ARG A 1 4329 ? 247.973 196.311 204.079 1.00 30.85  ? 4329 ARG A CZ    1 
ATOM   20628 N  NH1   . ARG A 1 4329 ? 248.886 196.206 205.031 1.00 32.66  ? 4329 ARG A NH1   1 
ATOM   20629 N  NH2   . ARG A 1 4329 ? 247.876 195.352 203.162 1.00 29.40  ? 4329 ARG A NH2   1 
ATOM   20630 N  N     . VAL A 1 4330 ? 243.152 200.619 206.835 1.00 17.98  ? 4330 VAL A N     1 
ATOM   20631 C  CA    . VAL A 1 4330 ? 242.959 201.105 208.197 1.00 16.86  ? 4330 VAL A CA    1 
ATOM   20632 C  C     . VAL A 1 4330 ? 241.589 200.689 208.718 1.00 15.77  ? 4330 VAL A C     1 
ATOM   20633 O  O     . VAL A 1 4330 ? 241.469 200.127 209.814 1.00 21.16  ? 4330 VAL A O     1 
ATOM   20634 C  CB    . VAL A 1 4330 ? 243.152 202.631 208.256 1.00 16.67  ? 4330 VAL A CB    1 
ATOM   20635 C  CG1   . VAL A 1 4330 ? 242.487 203.205 209.496 1.00 18.54  ? 4330 VAL A CG1   1 
ATOM   20636 C  CG2   . VAL A 1 4330 ? 244.630 202.974 208.239 1.00 12.85  ? 4330 VAL A CG2   1 
ATOM   20637 N  N     . LEU A 1 4331 ? 240.542 200.923 207.924 1.00 14.62  ? 4331 LEU A N     1 
ATOM   20638 C  CA    . LEU A 1 4331 ? 239.184 200.671 208.396 1.00 15.36  ? 4331 LEU A CA    1 
ATOM   20639 C  C     . LEU A 1 4331 ? 238.984 199.197 208.716 1.00 14.62  ? 4331 LEU A C     1 
ATOM   20640 O  O     . LEU A 1 4331 ? 238.587 198.839 209.832 1.00 15.86  ? 4331 LEU A O     1 
ATOM   20641 C  CB    . LEU A 1 4331 ? 238.164 201.139 207.355 1.00 17.57  ? 4331 LEU A CB    1 
ATOM   20642 C  CG    . LEU A 1 4331 ? 237.767 202.620 207.321 1.00 17.02  ? 4331 LEU A CG    1 
ATOM   20643 C  CD1   . LEU A 1 4331 ? 237.068 203.014 208.614 1.00 16.72  ? 4331 LEU A CD1   1 
ATOM   20644 C  CD2   . LEU A 1 4331 ? 238.953 203.537 207.047 1.00 16.29  ? 4331 LEU A CD2   1 
ATOM   20645 N  N     . LEU A 1 4332 ? 239.311 198.322 207.761 1.00 15.93  ? 4332 LEU A N     1 
ATOM   20646 C  CA    . LEU A 1 4332 ? 239.218 196.888 207.998 1.00 14.64  ? 4332 LEU A CA    1 
ATOM   20647 C  C     . LEU A 1 4332 ? 240.091 196.450 209.163 1.00 15.36  ? 4332 LEU A C     1 
ATOM   20648 O  O     . LEU A 1 4332 ? 239.823 195.404 209.764 1.00 17.93  ? 4332 LEU A O     1 
ATOM   20649 C  CB    . LEU A 1 4332 ? 239.605 196.117 206.736 1.00 9.78   ? 4332 LEU A CB    1 
ATOM   20650 C  CG    . LEU A 1 4332 ? 238.586 196.095 205.598 1.00 8.40   ? 4332 LEU A CG    1 
ATOM   20651 C  CD1   . LEU A 1 4332 ? 238.988 195.068 204.559 1.00 15.32  ? 4332 LEU A CD1   1 
ATOM   20652 C  CD2   . LEU A 1 4332 ? 237.196 195.800 206.129 1.00 10.66  ? 4332 LEU A CD2   1 
ATOM   20653 N  N     . THR A 1 4333 ? 241.127 197.220 209.495 1.00 13.34  ? 4333 THR A N     1 
ATOM   20654 C  CA    . THR A 1 4333 ? 241.874 196.951 210.715 1.00 13.34  ? 4333 THR A CA    1 
ATOM   20655 C  C     . THR A 1 4333 ? 241.040 197.309 211.937 1.00 14.84  ? 4333 THR A C     1 
ATOM   20656 O  O     . THR A 1 4333 ? 240.771 196.457 212.793 1.00 21.03  ? 4333 THR A O     1 
ATOM   20657 C  CB    . THR A 1 4333 ? 243.192 197.727 210.712 1.00 14.52  ? 4333 THR A CB    1 
ATOM   20658 O  OG1   . THR A 1 4333 ? 243.968 197.351 209.568 1.00 20.52  ? 4333 THR A OG1   1 
ATOM   20659 C  CG2   . THR A 1 4333 ? 243.988 197.429 211.973 1.00 14.27  ? 4333 THR A CG2   1 
ATOM   20660 N  N     . THR A 1 4334 ? 240.580 198.562 212.005 1.00 14.13  ? 4334 THR A N     1 
ATOM   20661 C  CA    . THR A 1 4334 ? 239.900 199.042 213.203 1.00 16.07  ? 4334 THR A CA    1 
ATOM   20662 C  C     . THR A 1 4334 ? 238.693 198.175 213.530 1.00 14.17  ? 4334 THR A C     1 
ATOM   20663 O  O     . THR A 1 4334 ? 238.579 197.645 214.642 1.00 16.65  ? 4334 THR A O     1 
ATOM   20664 C  CB    . THR A 1 4334 ? 239.481 200.502 213.018 1.00 18.71  ? 4334 THR A CB    1 
ATOM   20665 O  OG1   . THR A 1 4334 ? 240.637 201.345 213.083 1.00 21.60  ? 4334 THR A OG1   1 
ATOM   20666 C  CG2   . THR A 1 4334 ? 238.497 200.918 214.098 1.00 21.08  ? 4334 THR A CG2   1 
ATOM   20667 N  N     . GLN A 1 4335 ? 237.808 197.980 212.548 1.00 16.15  ? 4335 GLN A N     1 
ATOM   20668 C  CA    . GLN A 1 4335 ? 236.645 197.127 212.753 1.00 18.20  ? 4335 GLN A CA    1 
ATOM   20669 C  C     . GLN A 1 4335 ? 237.059 195.764 213.286 1.00 15.90  ? 4335 GLN A C     1 
ATOM   20670 O  O     . GLN A 1 4335 ? 236.466 195.262 214.250 1.00 18.72  ? 4335 GLN A O     1 
ATOM   20671 C  CB    . GLN A 1 4335 ? 235.864 196.980 211.448 1.00 17.46  ? 4335 GLN A CB    1 
ATOM   20672 C  CG    . GLN A 1 4335 ? 235.016 198.188 211.095 1.00 24.34  ? 4335 GLN A CG    1 
ATOM   20673 C  CD    . GLN A 1 4335 ? 234.202 197.981 209.835 1.00 33.54  ? 4335 GLN A CD    1 
ATOM   20674 O  OE1   . GLN A 1 4335 ? 234.752 197.767 208.754 1.00 30.11  ? 4335 GLN A OE1   1 
ATOM   20675 N  NE2   . GLN A 1 4335 ? 232.882 198.043 209.966 1.00 30.49  ? 4335 GLN A NE2   1 
ATOM   20676 N  N     . GLY A 1 4336 ? 238.105 195.174 212.703 1.00 13.88  ? 4336 GLY A N     1 
ATOM   20677 C  CA    . GLY A 1 4336 ? 238.584 193.897 213.206 1.00 11.44  ? 4336 GLY A CA    1 
ATOM   20678 C  C     . GLY A 1 4336 ? 238.915 193.965 214.682 1.00 12.39  ? 4336 GLY A C     1 
ATOM   20679 O  O     . GLY A 1 4336 ? 238.388 193.190 215.486 1.00 21.40  ? 4336 GLY A O     1 
ATOM   20680 N  N     . VAL A 1 4337 ? 239.735 194.947 215.067 1.00 12.22  ? 4337 VAL A N     1 
ATOM   20681 C  CA    . VAL A 1 4337 ? 240.025 195.146 216.481 1.00 14.29  ? 4337 VAL A CA    1 
ATOM   20682 C  C     . VAL A 1 4337 ? 238.732 195.372 217.245 1.00 13.89  ? 4337 VAL A C     1 
ATOM   20683 O  O     . VAL A 1 4337 ? 238.498 194.765 218.299 1.00 15.97  ? 4337 VAL A O     1 
ATOM   20684 C  CB    . VAL A 1 4337 ? 241.011 196.315 216.668 1.00 11.75  ? 4337 VAL A CB    1 
ATOM   20685 C  CG1   . VAL A 1 4337 ? 240.951 196.841 218.090 1.00 8.46   ? 4337 VAL A CG1   1 
ATOM   20686 C  CG2   . VAL A 1 4337 ? 242.422 195.877 216.318 1.00 10.55  ? 4337 VAL A CG2   1 
ATOM   20687 N  N     . ASP A 1 4338 ? 237.847 196.204 216.689 1.00 12.76  ? 4338 ASP A N     1 
ATOM   20688 C  CA    . ASP A 1 4338 ? 236.562 196.459 217.325 1.00 13.62  ? 4338 ASP A CA    1 
ATOM   20689 C  C     . ASP A 1 4338 ? 235.820 195.157 217.576 1.00 16.16  ? 4338 ASP A C     1 
ATOM   20690 O  O     . ASP A 1 4338 ? 235.281 194.942 218.670 1.00 19.12  ? 4338 ASP A O     1 
ATOM   20691 C  CB    . ASP A 1 4338 ? 235.734 197.403 216.452 1.00 18.72  ? 4338 ASP A CB    1 
ATOM   20692 C  CG    . ASP A 1 4338 ? 234.781 198.261 217.257 1.00 37.25  ? 4338 ASP A CG    1 
ATOM   20693 O  OD1   . ASP A 1 4338 ? 235.251 199.006 218.142 1.00 44.80  ? 4338 ASP A OD1   1 
ATOM   20694 O  OD2   . ASP A 1 4338 ? 233.564 198.205 216.991 1.00 36.78  ? 4338 ASP A OD2   1 
ATOM   20695 N  N     . MET A 1 4339 ? 235.837 194.250 216.593 1.00 14.34  ? 4339 MET A N     1 
ATOM   20696 C  CA    . MET A 1 4339 ? 235.171 192.965 216.765 1.00 11.52  ? 4339 MET A CA    1 
ATOM   20697 C  C     . MET A 1 4339 ? 235.700 192.254 218.000 1.00 16.83  ? 4339 MET A C     1 
ATOM   20698 O  O     . MET A 1 4339 ? 234.924 191.822 218.863 1.00 17.67  ? 4339 MET A O     1 
ATOM   20699 C  CB    . MET A 1 4339 ? 235.357 192.104 215.513 1.00 11.43  ? 4339 MET A CB    1 
ATOM   20700 C  CG    . MET A 1 4339 ? 234.535 190.823 215.511 1.00 15.03  ? 4339 MET A CG    1 
ATOM   20701 S  SD    . MET A 1 4339 ? 235.263 189.497 214.530 1.00 24.61  ? 4339 MET A SD    1 
ATOM   20702 C  CE    . MET A 1 4339 ? 236.797 189.218 215.404 1.00 14.86  ? 4339 MET A CE    1 
ATOM   20703 N  N     . ILE A 1 4340 ? 237.029 192.200 218.139 1.00 17.73  ? 4340 ILE A N     1 
ATOM   20704 C  CA    . ILE A 1 4340 ? 237.630 191.571 219.313 1.00 16.29  ? 4340 ILE A CA    1 
ATOM   20705 C  C     . ILE A 1 4340 ? 237.070 192.201 220.576 1.00 15.41  ? 4340 ILE A C     1 
ATOM   20706 O  O     . ILE A 1 4340 ? 236.610 191.504 221.490 1.00 16.31  ? 4340 ILE A O     1 
ATOM   20707 C  CB    . ILE A 1 4340 ? 239.164 191.689 219.265 1.00 18.61  ? 4340 ILE A CB    1 
ATOM   20708 C  CG1   . ILE A 1 4340 ? 239.719 191.024 218.008 1.00 16.62  ? 4340 ILE A CG1   1 
ATOM   20709 C  CG2   . ILE A 1 4340 ? 239.784 191.076 220.508 1.00 23.35  ? 4340 ILE A CG2   1 
ATOM   20710 C  CD1   . ILE A 1 4340 ? 239.418 189.557 217.933 1.00 19.46  ? 4340 ILE A CD1   1 
ATOM   20711 N  N     . SER A 1 4341 ? 237.038 193.536 220.610 1.00 13.84  ? 4341 SER A N     1 
ATOM   20712 C  CA    . SER A 1 4341 ? 236.541 194.229 221.791 1.00 13.03  ? 4341 SER A CA    1 
ATOM   20713 C  C     . SER A 1 4341 ? 235.126 193.781 222.116 1.00 13.73  ? 4341 SER A C     1 
ATOM   20714 O  O     . SER A 1 4341 ? 234.813 193.464 223.270 1.00 15.32  ? 4341 SER A O     1 
ATOM   20715 C  CB    . SER A 1 4341 ? 236.599 195.741 221.571 1.00 18.99  ? 4341 SER A CB    1 
ATOM   20716 O  OG    . SER A 1 4341 ? 237.922 196.161 221.291 1.00 19.40  ? 4341 SER A OG    1 
ATOM   20717 N  N     . LYS A 1 4342 ? 234.269 193.695 221.096 1.00 15.96  ? 4342 LYS A N     1 
ATOM   20718 C  CA    . LYS A 1 4342 ? 232.908 193.238 221.338 1.00 15.21  ? 4342 LYS A CA    1 
ATOM   20719 C  C     . LYS A 1 4342 ? 232.906 191.804 221.847 1.00 16.21  ? 4342 LYS A C     1 
ATOM   20720 O  O     . LYS A 1 4342 ? 232.228 191.489 222.833 1.00 22.08  ? 4342 LYS A O     1 
ATOM   20721 C  CB    . LYS A 1 4342 ? 232.073 193.377 220.068 1.00 16.16  ? 4342 LYS A CB    1 
ATOM   20722 C  CG    . LYS A 1 4342 ? 231.837 194.820 219.666 1.00 12.49  ? 4342 LYS A CG    1 
ATOM   20723 C  CD    . LYS A 1 4342 ? 231.209 194.924 218.293 1.00 15.39  ? 4342 LYS A CD    1 
ATOM   20724 C  CE    . LYS A 1 4342 ? 231.164 196.368 217.829 1.00 18.73  ? 4342 LYS A CE    1 
ATOM   20725 N  NZ    . LYS A 1 4342 ? 230.569 197.269 218.851 1.00 18.16  ? 4342 LYS A NZ    1 
ATOM   20726 N  N     . MET A 1 4343 ? 233.708 190.934 221.225 1.00 17.24  ? 4343 MET A N     1 
ATOM   20727 C  CA    . MET A 1 4343 ? 233.814 189.564 221.708 1.00 14.67  ? 4343 MET A CA    1 
ATOM   20728 C  C     . MET A 1 4343 ? 234.377 189.505 223.117 1.00 19.95  ? 4343 MET A C     1 
ATOM   20729 O  O     . MET A 1 4343 ? 234.156 188.514 223.821 1.00 32.49  ? 4343 MET A O     1 
ATOM   20730 C  CB    . MET A 1 4343 ? 234.681 188.729 220.767 1.00 18.86  ? 4343 MET A CB    1 
ATOM   20731 C  CG    . MET A 1 4343 ? 234.007 188.316 219.477 1.00 15.71  ? 4343 MET A CG    1 
ATOM   20732 S  SD    . MET A 1 4343 ? 235.083 187.261 218.491 1.00 38.32  ? 4343 MET A SD    1 
ATOM   20733 C  CE    . MET A 1 4343 ? 234.572 185.639 219.052 1.00 23.79  ? 4343 MET A CE    1 
ATOM   20734 N  N     . LEU A 1 4344 ? 235.097 190.540 223.546 1.00 17.60  ? 4344 LEU A N     1 
ATOM   20735 C  CA    . LEU A 1 4344 ? 235.572 190.593 224.917 1.00 18.74  ? 4344 LEU A CA    1 
ATOM   20736 C  C     . LEU A 1 4344 ? 234.564 191.241 225.852 1.00 20.18  ? 4344 LEU A C     1 
ATOM   20737 O  O     . LEU A 1 4344 ? 234.576 190.949 227.053 1.00 29.39  ? 4344 LEU A O     1 
ATOM   20738 C  CB    . LEU A 1 4344 ? 236.903 191.346 224.988 1.00 22.53  ? 4344 LEU A CB    1 
ATOM   20739 C  CG    . LEU A 1 4344 ? 237.767 191.058 226.214 1.00 28.23  ? 4344 LEU A CG    1 
ATOM   20740 C  CD1   . LEU A 1 4344 ? 237.902 189.560 226.416 1.00 27.97  ? 4344 LEU A CD1   1 
ATOM   20741 C  CD2   . LEU A 1 4344 ? 239.131 191.703 226.070 1.00 30.70  ? 4344 LEU A CD2   1 
ATOM   20742 N  N     . LYS A 1 4345 ? 233.686 192.097 225.329 1.00 19.42  ? 4345 LYS A N     1 
ATOM   20743 C  CA    . LYS A 1 4345 ? 232.686 192.749 226.162 1.00 17.95  ? 4345 LYS A CA    1 
ATOM   20744 C  C     . LYS A 1 4345 ? 231.566 191.800 226.562 1.00 21.53  ? 4345 LYS A C     1 
ATOM   20745 O  O     . LYS A 1 4345 ? 230.916 192.020 227.590 1.00 25.20  ? 4345 LYS A O     1 
ATOM   20746 C  CB    . LYS A 1 4345 ? 232.116 193.965 225.426 1.00 16.70  ? 4345 LYS A CB    1 
ATOM   20747 C  CG    . LYS A 1 4345 ? 231.104 194.778 226.213 1.00 20.63  ? 4345 LYS A CG    1 
ATOM   20748 C  CD    . LYS A 1 4345 ? 231.750 195.470 227.396 1.00 25.90  ? 4345 LYS A CD    1 
ATOM   20749 C  CE    . LYS A 1 4345 ? 230.729 196.268 228.185 1.00 26.90  ? 4345 LYS A CE    1 
ATOM   20750 N  NZ    . LYS A 1 4345 ? 230.193 197.409 227.396 1.00 33.73  ? 4345 LYS A NZ    1 
ATOM   20751 N  N     . MET A 1 4346 ? 231.347 190.740 225.787 1.00 22.14  ? 4346 MET A N     1 
ATOM   20752 C  CA    . MET A 1 4346 ? 230.269 189.788 226.016 1.00 25.16  ? 4346 MET A CA    1 
ATOM   20753 C  C     . MET A 1 4346 ? 230.773 188.501 226.664 1.00 28.30  ? 4346 MET A C     1 
ATOM   20754 O  O     . MET A 1 4346 ? 230.147 187.447 226.538 1.00 25.21  ? 4346 MET A O     1 
ATOM   20755 C  CB    . MET A 1 4346 ? 229.555 189.489 224.700 1.00 19.47  ? 4346 MET A CB    1 
ATOM   20756 C  CG    . MET A 1 4346 ? 228.633 190.602 224.243 1.00 22.42  ? 4346 MET A CG    1 
ATOM   20757 S  SD    . MET A 1 4346 ? 227.738 190.199 222.735 1.00 45.48  ? 4346 MET A SD    1 
ATOM   20758 C  CE    . MET A 1 4346 ? 229.057 190.312 221.532 1.00 23.58  ? 4346 MET A CE    1 
ATOM   20759 N  N     . GLN A 1 4347 ? 231.901 188.579 227.363 1.00 35.82  ? 4347 GLN A N     1 
ATOM   20760 C  CA    . GLN A 1 4347 ? 232.499 187.410 227.994 1.00 41.72  ? 4347 GLN A CA    1 
ATOM   20761 C  C     . GLN A 1 4347 ? 232.044 187.278 229.445 1.00 43.54  ? 4347 GLN A C     1 
ATOM   20762 O  O     . GLN A 1 4347 ? 231.292 186.366 229.791 1.00 41.51  ? 4347 GLN A O     1 
ATOM   20763 C  CB    . GLN A 1 4347 ? 234.025 187.488 227.924 1.00 38.95  ? 4347 GLN A CB    1 
ATOM   20764 C  CG    . GLN A 1 4347 ? 234.731 186.182 228.230 1.00 45.29  ? 4347 GLN A CG    1 
ATOM   20765 C  CD    . GLN A 1 4347 ? 234.627 185.188 227.091 1.00 50.39  ? 4347 GLN A CD    1 
ATOM   20766 O  OE1   . GLN A 1 4347 ? 234.723 185.556 225.920 1.00 38.88  ? 4347 GLN A OE1   1 
ATOM   20767 N  NE2   . GLN A 1 4347 ? 234.431 183.919 227.428 1.00 57.07  ? 4347 GLN A NE2   1 
ATOM   20768 N  N     . PRO A 1 4374 ? 245.338 212.289 245.499 1.00 49.23  ? 4374 PRO A N     1 
ATOM   20769 C  CA    . PRO A 1 4374 ? 244.950 211.056 244.807 1.00 57.53  ? 4374 PRO A CA    1 
ATOM   20770 C  C     . PRO A 1 4374 ? 245.905 210.697 243.672 1.00 57.46  ? 4374 PRO A C     1 
ATOM   20771 O  O     . PRO A 1 4374 ? 246.825 211.460 243.376 1.00 52.31  ? 4374 PRO A O     1 
ATOM   20772 C  CB    . PRO A 1 4374 ? 243.551 211.378 244.260 1.00 52.56  ? 4374 PRO A CB    1 
ATOM   20773 C  CG    . PRO A 1 4374 ? 243.175 212.744 244.820 1.00 51.17  ? 4374 PRO A CG    1 
ATOM   20774 C  CD    . PRO A 1 4374 ? 244.165 213.089 245.882 1.00 47.14  ? 4374 PRO A CD    1 
ATOM   20775 N  N     . ALA A 1 4375 ? 245.683 209.535 243.053 1.00 58.87  ? 4375 ALA A N     1 
ATOM   20776 C  CA    . ALA A 1 4375 ? 246.547 209.097 241.960 1.00 61.86  ? 4375 ALA A CA    1 
ATOM   20777 C  C     . ALA A 1 4375 ? 246.436 210.027 240.759 1.00 57.73  ? 4375 ALA A C     1 
ATOM   20778 O  O     . ALA A 1 4375 ? 247.442 210.316 240.093 1.00 51.54  ? 4375 ALA A O     1 
ATOM   20779 C  CB    . ALA A 1 4375 ? 246.202 207.663 241.562 1.00 56.37  ? 4375 ALA A CB    1 
ATOM   20780 N  N     . TRP A 1 4376 ? 245.221 210.497 240.460 1.00 52.99  ? 4376 TRP A N     1 
ATOM   20781 C  CA    . TRP A 1 4376 ? 245.040 211.392 239.323 1.00 51.05  ? 4376 TRP A CA    1 
ATOM   20782 C  C     . TRP A 1 4376 ? 245.810 212.689 239.531 1.00 49.29  ? 4376 TRP A C     1 
ATOM   20783 O  O     . TRP A 1 4376 ? 246.380 213.237 238.582 1.00 44.52  ? 4376 TRP A O     1 
ATOM   20784 C  CB    . TRP A 1 4376 ? 243.552 211.655 239.081 1.00 44.53  ? 4376 TRP A CB    1 
ATOM   20785 C  CG    . TRP A 1 4376 ? 242.873 212.530 240.093 1.00 52.14  ? 4376 TRP A CG    1 
ATOM   20786 C  CD1   . TRP A 1 4376 ? 242.087 212.122 241.129 1.00 59.57  ? 4376 TRP A CD1   1 
ATOM   20787 C  CD2   . TRP A 1 4376 ? 242.855 213.963 240.118 1.00 53.52  ? 4376 TRP A CD2   1 
ATOM   20788 N  NE1   . TRP A 1 4376 ? 241.615 213.209 241.824 1.00 58.77  ? 4376 TRP A NE1   1 
ATOM   20789 C  CE2   . TRP A 1 4376 ? 242.070 214.352 241.219 1.00 54.42  ? 4376 TRP A CE2   1 
ATOM   20790 C  CE3   . TRP A 1 4376 ? 243.444 214.954 239.327 1.00 51.89  ? 4376 TRP A CE3   1 
ATOM   20791 C  CZ2   . TRP A 1 4376 ? 241.856 215.688 241.547 1.00 49.13  ? 4376 TRP A CZ2   1 
ATOM   20792 C  CZ3   . TRP A 1 4376 ? 243.233 216.277 239.656 1.00 45.75  ? 4376 TRP A CZ3   1 
ATOM   20793 C  CH2   . TRP A 1 4376 ? 242.443 216.633 240.754 1.00 47.08  ? 4376 TRP A CH2   1 
ATOM   20794 N  N     . MET A 1 4377 ? 245.863 213.173 240.775 1.00 45.85  ? 4377 MET A N     1 
ATOM   20795 C  CA    . MET A 1 4377 ? 246.671 214.347 241.086 1.00 44.35  ? 4377 MET A CA    1 
ATOM   20796 C  C     . MET A 1 4377 ? 248.129 214.130 240.697 1.00 41.67  ? 4377 MET A C     1 
ATOM   20797 O  O     . MET A 1 4377 ? 248.736 214.972 240.027 1.00 41.64  ? 4377 MET A O     1 
ATOM   20798 C  CB    . MET A 1 4377 ? 246.566 214.671 242.577 1.00 48.77  ? 4377 MET A CB    1 
ATOM   20799 C  CG    . MET A 1 4377 ? 246.922 216.101 242.938 1.00 43.54  ? 4377 MET A CG    1 
ATOM   20800 S  SD    . MET A 1 4377 ? 245.990 216.749 244.339 1.00 61.97  ? 4377 MET A SD    1 
ATOM   20801 C  CE    . MET A 1 4377 ? 244.397 217.053 243.590 1.00 52.77  ? 4377 MET A CE    1 
ATOM   20802 N  N     . ARG A 1 4378 ? 248.703 212.994 241.099 1.00 47.02  ? 4378 ARG A N     1 
ATOM   20803 C  CA    . ARG A 1 4378 ? 250.121 212.747 240.856 1.00 45.30  ? 4378 ARG A CA    1 
ATOM   20804 C  C     . ARG A 1 4378 ? 250.410 212.563 239.371 1.00 45.07  ? 4378 ARG A C     1 
ATOM   20805 O  O     . ARG A 1 4378 ? 251.389 213.114 238.844 1.00 45.66  ? 4378 ARG A O     1 
ATOM   20806 C  CB    . ARG A 1 4378 ? 250.578 211.524 241.651 1.00 48.31  ? 4378 ARG A CB    1 
ATOM   20807 C  CG    . ARG A 1 4378 ? 250.294 211.615 243.139 1.00 51.15  ? 4378 ARG A CG    1 
ATOM   20808 C  CD    . ARG A 1 4378 ? 250.520 210.279 243.830 1.00 59.23  ? 4378 ARG A CD    1 
ATOM   20809 N  NE    . ARG A 1 4378 ? 251.699 210.300 244.689 1.00 62.07  ? 4378 ARG A NE    1 
ATOM   20810 C  CZ    . ARG A 1 4378 ? 251.725 210.808 245.913 1.00 61.63  ? 4378 ARG A CZ    1 
ATOM   20811 N  NH1   . ARG A 1 4378 ? 250.648 211.345 246.462 1.00 62.04  ? 4378 ARG A NH1   1 
ATOM   20812 N  NH2   . ARG A 1 4378 ? 252.860 210.774 246.605 1.00 54.06  ? 4378 ARG A NH2   1 
ATOM   20813 N  N     . THR A 1 4379 ? 249.574 211.784 238.676 1.00 37.78  ? 4379 THR A N     1 
ATOM   20814 C  CA    . THR A 1 4379 ? 249.823 211.572 237.253 1.00 38.29  ? 4379 THR A CA    1 
ATOM   20815 C  C     . THR A 1 4379 ? 249.642 212.864 236.466 1.00 42.90  ? 4379 THR A C     1 
ATOM   20816 O  O     . THR A 1 4379 ? 250.407 213.138 235.534 1.00 41.82  ? 4379 THR A O     1 
ATOM   20817 C  CB    . THR A 1 4379 ? 248.932 210.454 236.699 1.00 43.43  ? 4379 THR A CB    1 
ATOM   20818 O  OG1   . THR A 1 4379 ? 249.213 210.262 235.307 1.00 49.76  ? 4379 THR A OG1   1 
ATOM   20819 C  CG2   . THR A 1 4379 ? 247.463 210.778 236.860 1.00 41.60  ? 4379 THR A CG2   1 
ATOM   20820 N  N     . LEU A 1 4380 ? 248.658 213.692 236.840 1.00 39.55  ? 4380 LEU A N     1 
ATOM   20821 C  CA    . LEU A 1 4380 ? 248.491 214.982 236.186 1.00 34.48  ? 4380 LEU A CA    1 
ATOM   20822 C  C     . LEU A 1 4380 ? 249.669 215.903 236.473 1.00 32.50  ? 4380 LEU A C     1 
ATOM   20823 O  O     . LEU A 1 4380 ? 250.101 216.651 235.594 1.00 37.74  ? 4380 LEU A O     1 
ATOM   20824 C  CB    . LEU A 1 4380 ? 247.180 215.631 236.626 1.00 37.25  ? 4380 LEU A CB    1 
ATOM   20825 C  CG    . LEU A 1 4380 ? 246.751 216.882 235.857 1.00 34.27  ? 4380 LEU A CG    1 
ATOM   20826 C  CD1   . LEU A 1 4380 ? 246.622 216.584 234.375 1.00 30.52  ? 4380 LEU A CD1   1 
ATOM   20827 C  CD2   . LEU A 1 4380 ? 245.445 217.425 236.408 1.00 31.86  ? 4380 LEU A CD2   1 
ATOM   20828 N  N     . HIS A 1 4381 ? 250.195 215.866 237.700 1.00 29.25  ? 4381 HIS A N     1 
ATOM   20829 C  CA    . HIS A 1 4381 ? 251.365 216.675 238.026 1.00 33.23  ? 4381 HIS A CA    1 
ATOM   20830 C  C     . HIS A 1 4381 ? 252.549 216.292 237.151 1.00 36.47  ? 4381 HIS A C     1 
ATOM   20831 O  O     . HIS A 1 4381 ? 253.217 217.158 236.570 1.00 35.50  ? 4381 HIS A O     1 
ATOM   20832 C  CB    . HIS A 1 4381 ? 251.714 216.508 239.507 1.00 30.70  ? 4381 HIS A CB    1 
ATOM   20833 C  CG    . HIS A 1 4381 ? 252.887 217.324 239.951 1.00 31.63  ? 4381 HIS A CG    1 
ATOM   20834 N  ND1   . HIS A 1 4381 ? 254.188 216.981 239.658 1.00 36.32  ? 4381 HIS A ND1   1 
ATOM   20835 C  CD2   . HIS A 1 4381 ? 252.954 218.463 240.680 1.00 33.93  ? 4381 HIS A CD2   1 
ATOM   20836 C  CE1   . HIS A 1 4381 ? 255.008 217.877 240.181 1.00 34.77  ? 4381 HIS A CE1   1 
ATOM   20837 N  NE2   . HIS A 1 4381 ? 254.284 218.786 240.807 1.00 34.72  ? 4381 HIS A NE2   1 
ATOM   20838 N  N     . THR A 1 4382 ? 252.816 214.989 237.038 1.00 39.94  ? 4382 THR A N     1 
ATOM   20839 C  CA    . THR A 1 4382 ? 253.929 214.537 236.208 1.00 39.54  ? 4382 THR A CA    1 
ATOM   20840 C  C     . THR A 1 4382 ? 253.710 214.904 234.745 1.00 36.57  ? 4382 THR A C     1 
ATOM   20841 O  O     . THR A 1 4382 ? 254.634 215.381 234.070 1.00 36.78  ? 4382 THR A O     1 
ATOM   20842 C  CB    . THR A 1 4382 ? 254.121 213.029 236.361 1.00 45.34  ? 4382 THR A CB    1 
ATOM   20843 O  OG1   . THR A 1 4382 ? 254.241 212.701 237.751 1.00 45.39  ? 4382 THR A OG1   1 
ATOM   20844 C  CG2   . THR A 1 4382 ? 255.375 212.573 235.628 1.00 39.86  ? 4382 THR A CG2   1 
ATOM   20845 N  N     . THR A 1 4383 ? 252.488 214.704 234.244 1.00 31.67  ? 4383 THR A N     1 
ATOM   20846 C  CA    . THR A 1 4383 ? 252.195 215.010 232.849 1.00 34.30  ? 4383 THR A CA    1 
ATOM   20847 C  C     . THR A 1 4383 ? 252.360 216.497 232.561 1.00 34.32  ? 4383 THR A C     1 
ATOM   20848 O  O     . THR A 1 4383 ? 252.932 216.877 231.532 1.00 35.19  ? 4383 THR A O     1 
ATOM   20849 C  CB    . THR A 1 4383 ? 250.776 214.555 232.506 1.00 32.33  ? 4383 THR A CB    1 
ATOM   20850 O  OG1   . THR A 1 4383 ? 250.645 213.153 232.767 1.00 45.61  ? 4383 THR A OG1   1 
ATOM   20851 C  CG2   . THR A 1 4383 ? 250.479 214.811 231.048 1.00 27.09  ? 4383 THR A CG2   1 
ATOM   20852 N  N     . ALA A 1 4384 ? 251.875 217.353 233.461 1.00 34.92  ? 4384 ALA A N     1 
ATOM   20853 C  CA    . ALA A 1 4384 ? 251.966 218.791 233.246 1.00 31.61  ? 4384 ALA A CA    1 
ATOM   20854 C  C     . ALA A 1 4384 ? 253.405 219.278 233.350 1.00 31.33  ? 4384 ALA A C     1 
ATOM   20855 O  O     . ALA A 1 4384 ? 253.815 220.172 232.601 1.00 33.81  ? 4384 ALA A O     1 
ATOM   20856 C  CB    . ALA A 1 4384 ? 251.070 219.527 234.239 1.00 35.39  ? 4384 ALA A CB    1 
ATOM   20857 N  N     . SER A 1 4385 ? 254.189 218.712 234.272 1.00 32.94  ? 4385 SER A N     1 
ATOM   20858 C  CA    . SER A 1 4385 ? 255.602 219.073 234.343 1.00 33.02  ? 4385 SER A CA    1 
ATOM   20859 C  C     . SER A 1 4385 ? 256.335 218.670 233.068 1.00 37.77  ? 4385 SER A C     1 
ATOM   20860 O  O     . SER A 1 4385 ? 257.137 219.446 232.529 1.00 38.83  ? 4385 SER A O     1 
ATOM   20861 C  CB    . SER A 1 4385 ? 256.249 218.426 235.567 1.00 30.97  ? 4385 SER A CB    1 
ATOM   20862 O  OG    . SER A 1 4385 ? 255.527 218.741 236.744 1.00 37.91  ? 4385 SER A OG    1 
ATOM   20863 N  N     . ASN A 1 4386 ? 256.057 217.468 232.559 1.00 34.72  ? 4386 ASN A N     1 
ATOM   20864 C  CA    . ASN A 1 4386 ? 256.663 217.052 231.299 1.00 37.09  ? 4386 ASN A CA    1 
ATOM   20865 C  C     . ASN A 1 4386 ? 256.257 217.983 230.164 1.00 40.01  ? 4386 ASN A C     1 
ATOM   20866 O  O     . ASN A 1 4386 ? 257.102 218.404 229.365 1.00 41.88  ? 4386 ASN A O     1 
ATOM   20867 C  CB    . ASN A 1 4386 ? 256.277 215.610 230.981 1.00 37.67  ? 4386 ASN A CB    1 
ATOM   20868 C  CG    . ASN A 1 4386 ? 257.145 214.602 231.705 1.00 47.01  ? 4386 ASN A CG    1 
ATOM   20869 O  OD1   . ASN A 1 4386 ? 256.646 213.638 232.285 1.00 49.61  ? 4386 ASN A OD1   1 
ATOM   20870 N  ND2   . ASN A 1 4386 ? 258.454 214.821 231.675 1.00 54.13  ? 4386 ASN A ND2   1 
ATOM   20871 N  N     . TRP A 1 4387 ? 254.971 218.336 230.093 1.00 38.42  ? 4387 TRP A N     1 
ATOM   20872 C  CA    . TRP A 1 4387 ? 254.503 219.251 229.058 1.00 30.07  ? 4387 TRP A CA    1 
ATOM   20873 C  C     . TRP A 1 4387 ? 255.218 220.591 229.145 1.00 27.69  ? 4387 TRP A C     1 
ATOM   20874 O  O     . TRP A 1 4387 ? 255.668 221.131 228.128 1.00 29.47  ? 4387 TRP A O     1 
ATOM   20875 C  CB    . TRP A 1 4387 ? 252.996 219.444 229.183 1.00 25.15  ? 4387 TRP A CB    1 
ATOM   20876 C  CG    . TRP A 1 4387 ? 252.200 218.322 228.615 1.00 22.58  ? 4387 TRP A CG    1 
ATOM   20877 C  CD1   . TRP A 1 4387 ? 252.635 217.364 227.750 1.00 22.98  ? 4387 TRP A CD1   1 
ATOM   20878 C  CD2   . TRP A 1 4387 ? 250.838 218.010 228.912 1.00 24.57  ? 4387 TRP A CD2   1 
ATOM   20879 N  NE1   . TRP A 1 4387 ? 251.615 216.488 227.466 1.00 28.37  ? 4387 TRP A NE1   1 
ATOM   20880 C  CE2   . TRP A 1 4387 ? 250.503 216.862 228.172 1.00 25.40  ? 4387 TRP A CE2   1 
ATOM   20881 C  CE3   . TRP A 1 4387 ? 249.865 218.596 229.726 1.00 29.12  ? 4387 TRP A CE3   1 
ATOM   20882 C  CZ2   . TRP A 1 4387 ? 249.236 216.290 228.219 1.00 21.65  ? 4387 TRP A CZ2   1 
ATOM   20883 C  CZ3   . TRP A 1 4387 ? 248.612 218.027 229.774 1.00 31.49  ? 4387 TRP A CZ3   1 
ATOM   20884 C  CH2   . TRP A 1 4387 ? 248.309 216.882 229.031 1.00 29.58  ? 4387 TRP A CH2   1 
ATOM   20885 N  N     . LEU A 1 4388 ? 255.347 221.139 230.354 1.00 30.15  ? 4388 LEU A N     1 
ATOM   20886 C  CA    . LEU A 1 4388 ? 256.079 222.388 230.526 1.00 31.13  ? 4388 LEU A CA    1 
ATOM   20887 C  C     . LEU A 1 4388 ? 257.532 222.241 230.097 1.00 36.02  ? 4388 LEU A C     1 
ATOM   20888 O  O     . LEU A 1 4388 ? 258.151 223.216 229.659 1.00 33.69  ? 4388 LEU A O     1 
ATOM   20889 C  CB    . LEU A 1 4388 ? 255.996 222.851 231.980 1.00 26.78  ? 4388 LEU A CB    1 
ATOM   20890 C  CG    . LEU A 1 4388 ? 254.731 223.620 232.363 1.00 21.87  ? 4388 LEU A CG    1 
ATOM   20891 C  CD1   . LEU A 1 4388 ? 254.703 223.904 233.855 1.00 23.54  ? 4388 LEU A CD1   1 
ATOM   20892 C  CD2   . LEU A 1 4388 ? 254.627 224.909 231.566 1.00 20.73  ? 4388 LEU A CD2   1 
ATOM   20893 N  N     . HIS A 1 4389 ? 258.092 221.036 230.221 1.00 40.31  ? 4389 HIS A N     1 
ATOM   20894 C  CA    . HIS A 1 4389 ? 259.464 220.822 229.767 1.00 36.73  ? 4389 HIS A CA    1 
ATOM   20895 C  C     . HIS A 1 4389 ? 259.561 220.805 228.244 1.00 32.46  ? 4389 HIS A C     1 
ATOM   20896 O  O     . HIS A 1 4389 ? 260.463 221.428 227.671 1.00 37.69  ? 4389 HIS A O     1 
ATOM   20897 C  CB    . HIS A 1 4389 ? 260.018 219.529 230.361 1.00 46.68  ? 4389 HIS A CB    1 
ATOM   20898 C  CG    . HIS A 1 4389 ? 260.651 219.709 231.706 1.00 56.15  ? 4389 HIS A CG    1 
ATOM   20899 N  ND1   . HIS A 1 4389 ? 261.555 220.715 231.973 1.00 51.27  ? 4389 HIS A ND1   1 
ATOM   20900 C  CD2   . HIS A 1 4389 ? 260.505 219.019 232.861 1.00 58.25  ? 4389 HIS A CD2   1 
ATOM   20901 C  CE1   . HIS A 1 4389 ? 261.942 220.633 233.232 1.00 57.69  ? 4389 HIS A CE1   1 
ATOM   20902 N  NE2   . HIS A 1 4389 ? 261.321 219.613 233.794 1.00 59.44  ? 4389 HIS A NE2   1 
ATOM   20903 N  N     . LEU A 1 4390 ? 258.652 220.098 227.566 1.00 30.46  ? 4390 LEU A N     1 
ATOM   20904 C  CA    . LEU A 1 4390 ? 258.724 220.019 226.105 1.00 25.28  ? 4390 LEU A CA    1 
ATOM   20905 C  C     . LEU A 1 4390 ? 258.394 221.354 225.445 1.00 28.53  ? 4390 LEU A C     1 
ATOM   20906 O  O     . LEU A 1 4390 ? 259.117 221.805 224.549 1.00 32.95  ? 4390 LEU A O     1 
ATOM   20907 C  CB    . LEU A 1 4390 ? 257.807 218.917 225.568 1.00 24.87  ? 4390 LEU A CB    1 
ATOM   20908 C  CG    . LEU A 1 4390 ? 258.237 217.445 225.644 1.00 36.16  ? 4390 LEU A CG    1 
ATOM   20909 C  CD1   . LEU A 1 4390 ? 258.221 216.868 227.044 1.00 29.61  ? 4390 LEU A CD1   1 
ATOM   20910 C  CD2   . LEU A 1 4390 ? 257.369 216.606 224.716 1.00 36.82  ? 4390 LEU A CD2   1 
ATOM   20911 N  N     . ILE A 1 4391 ? 257.306 221.993 225.857 1.00 27.43  ? 4391 ILE A N     1 
ATOM   20912 C  CA    . ILE A 1 4391 ? 256.900 223.251 225.217 1.00 24.74  ? 4391 ILE A CA    1 
ATOM   20913 C  C     . ILE A 1 4391 ? 257.939 224.327 225.512 1.00 28.49  ? 4391 ILE A C     1 
ATOM   20914 O  O     . ILE A 1 4391 ? 258.372 224.461 226.671 1.00 29.83  ? 4391 ILE A O     1 
ATOM   20915 C  CB    . ILE A 1 4391 ? 255.511 223.672 225.700 1.00 22.73  ? 4391 ILE A CB    1 
ATOM   20916 C  CG1   . ILE A 1 4391 ? 254.541 222.493 225.632 1.00 22.72  ? 4391 ILE A CG1   1 
ATOM   20917 C  CG2   . ILE A 1 4391 ? 254.980 224.823 224.870 1.00 24.36  ? 4391 ILE A CG2   1 
ATOM   20918 C  CD1   . ILE A 1 4391 ? 253.161 222.810 226.155 1.00 21.70  ? 4391 ILE A CD1   1 
ATOM   20919 N  N     . PRO A 1 4392 ? 258.373 225.099 224.514 1.00 23.58  ? 4392 PRO A N     1 
ATOM   20920 C  CA    . PRO A 1 4392 ? 259.405 226.115 224.758 1.00 25.14  ? 4392 PRO A CA    1 
ATOM   20921 C  C     . PRO A 1 4392 ? 258.952 227.156 225.771 1.00 26.01  ? 4392 PRO A C     1 
ATOM   20922 O  O     . PRO A 1 4392 ? 257.768 227.470 225.891 1.00 29.94  ? 4392 PRO A O     1 
ATOM   20923 C  CB    . PRO A 1 4392 ? 259.620 226.738 223.375 1.00 21.53  ? 4392 PRO A CB    1 
ATOM   20924 C  CG    . PRO A 1 4392 ? 259.208 225.671 222.421 1.00 22.29  ? 4392 PRO A CG    1 
ATOM   20925 C  CD    . PRO A 1 4392 ? 258.065 224.961 223.082 1.00 18.57  ? 4392 PRO A CD    1 
ATOM   20926 N  N     . GLN A 1 4393 ? 259.927 227.688 226.512 1.00 23.69  ? 4393 GLN A N     1 
ATOM   20927 C  CA    . GLN A 1 4393 ? 259.613 228.583 227.619 1.00 27.31  ? 4393 GLN A CA    1 
ATOM   20928 C  C     . GLN A 1 4393 ? 259.092 229.932 227.130 1.00 28.58  ? 4393 GLN A C     1 
ATOM   20929 O  O     . GLN A 1 4393 ? 258.156 230.486 227.717 1.00 32.81  ? 4393 GLN A O     1 
ATOM   20930 C  CB    . GLN A 1 4393 ? 260.845 228.770 228.506 1.00 30.22  ? 4393 GLN A CB    1 
ATOM   20931 C  CG    . GLN A 1 4393 ? 261.278 227.503 229.230 1.00 38.45  ? 4393 GLN A CG    1 
ATOM   20932 C  CD    . GLN A 1 4393 ? 262.763 227.483 229.543 1.00 55.10  ? 4393 GLN A CD    1 
ATOM   20933 O  OE1   . GLN A 1 4393 ? 263.594 227.266 228.663 1.00 52.03  ? 4393 GLN A OE1   1 
ATOM   20934 N  NE2   . GLN A 1 4393 ? 263.102 227.710 230.807 1.00 56.57  ? 4393 GLN A NE2   1 
ATOM   20935 N  N     . THR A 1 4394 ? 259.678 230.478 226.067 1.00 28.97  ? 4394 THR A N     1 
ATOM   20936 C  CA    . THR A 1 4394 ? 259.319 231.817 225.623 1.00 27.18  ? 4394 THR A CA    1 
ATOM   20937 C  C     . THR A 1 4394 ? 259.382 231.914 224.106 1.00 25.53  ? 4394 THR A C     1 
ATOM   20938 O  O     . THR A 1 4394 ? 260.050 231.126 223.434 1.00 26.13  ? 4394 THR A O     1 
ATOM   20939 C  CB    . THR A 1 4394 ? 260.228 232.884 226.246 1.00 31.55  ? 4394 THR A CB    1 
ATOM   20940 O  OG1   . THR A 1 4394 ? 259.734 234.188 225.914 1.00 33.11  ? 4394 THR A OG1   1 
ATOM   20941 C  CG2   . THR A 1 4394 ? 261.653 232.741 225.730 1.00 22.79  ? 4394 THR A CG2   1 
ATOM   20942 N  N     . LEU A 1 4395 ? 258.659 232.901 223.580 1.00 25.30  ? 4395 LEU A N     1 
ATOM   20943 C  CA    . LEU A 1 4395 ? 258.701 233.276 222.174 1.00 20.61  ? 4395 LEU A CA    1 
ATOM   20944 C  C     . LEU A 1 4395 ? 258.855 234.786 222.090 1.00 22.85  ? 4395 LEU A C     1 
ATOM   20945 O  O     . LEU A 1 4395 ? 258.130 235.522 222.768 1.00 25.87  ? 4395 LEU A O     1 
ATOM   20946 C  CB    . LEU A 1 4395 ? 257.437 232.821 221.434 1.00 19.17  ? 4395 LEU A CB    1 
ATOM   20947 C  CG    . LEU A 1 4395 ? 257.322 233.207 219.958 1.00 20.07  ? 4395 LEU A CG    1 
ATOM   20948 C  CD1   . LEU A 1 4395 ? 258.560 232.783 219.188 1.00 18.79  ? 4395 LEU A CD1   1 
ATOM   20949 C  CD2   . LEU A 1 4395 ? 256.072 232.599 219.342 1.00 12.36  ? 4395 LEU A CD2   1 
ATOM   20950 N  N     . SER A 1 4396 ? 259.792 235.244 221.266 1.00 25.67  ? 4396 SER A N     1 
ATOM   20951 C  CA    . SER A 1 4396 ? 260.132 236.660 221.193 1.00 27.08  ? 4396 SER A CA    1 
ATOM   20952 C  C     . SER A 1 4396 ? 259.353 237.339 220.073 1.00 25.73  ? 4396 SER A C     1 
ATOM   20953 O  O     . SER A 1 4396 ? 259.330 236.851 218.939 1.00 31.42  ? 4396 SER A O     1 
ATOM   20954 C  CB    . SER A 1 4396 ? 261.634 236.839 220.972 1.00 29.66  ? 4396 SER A CB    1 
ATOM   20955 O  OG    . SER A 1 4396 ? 262.377 236.278 222.040 1.00 32.16  ? 4396 SER A OG    1 
ATOM   20956 N  N     . HIS A 1 4397 ? 258.723 238.465 220.397 1.00 28.70  ? 4397 HIS A N     1 
ATOM   20957 C  CA    . HIS A 1 4397 ? 257.995 239.239 219.402 1.00 28.40  ? 4397 HIS A CA    1 
ATOM   20958 C  C     . HIS A 1 4397 ? 258.951 239.851 218.385 1.00 26.75  ? 4397 HIS A C     1 
ATOM   20959 O  O     . HIS A 1 4397 ? 260.110 240.148 218.685 1.00 32.09  ? 4397 HIS A O     1 
ATOM   20960 C  CB    . HIS A 1 4397 ? 257.180 240.344 220.073 1.00 24.00  ? 4397 HIS A CB    1 
ATOM   20961 C  CG    . HIS A 1 4397 ? 255.840 239.896 220.567 1.00 27.48  ? 4397 HIS A CG    1 
ATOM   20962 N  ND1   . HIS A 1 4397 ? 255.109 240.614 221.488 1.00 25.57  ? 4397 HIS A ND1   1 
ATOM   20963 C  CD2   . HIS A 1 4397 ? 255.098 238.803 220.268 1.00 29.44  ? 4397 HIS A CD2   1 
ATOM   20964 C  CE1   . HIS A 1 4397 ? 253.976 239.983 221.736 1.00 23.84  ? 4397 HIS A CE1   1 
ATOM   20965 N  NE2   . HIS A 1 4397 ? 253.944 238.882 221.009 1.00 27.64  ? 4397 HIS A NE2   1 
ATOM   20966 N  N     . LEU A 1 4398 ? 258.451 240.035 217.166 1.00 27.40  ? 4398 LEU A N     1 
ATOM   20967 C  CA    . LEU A 1 4398 ? 259.248 240.654 216.117 1.00 27.78  ? 4398 LEU A CA    1 
ATOM   20968 C  C     . LEU A 1 4398 ? 259.386 242.150 216.364 1.00 38.01  ? 4398 LEU A C     1 
ATOM   20969 O  O     . LEU A 1 4398 ? 258.409 242.838 216.673 1.00 42.84  ? 4398 LEU A O     1 
ATOM   20970 C  CB    . LEU A 1 4398 ? 258.610 240.405 214.752 1.00 26.06  ? 4398 LEU A CB    1 
ATOM   20971 C  CG    . LEU A 1 4398 ? 258.557 238.956 214.267 1.00 23.61  ? 4398 LEU A CG    1 
ATOM   20972 C  CD1   . LEU A 1 4398 ? 258.245 238.899 212.781 1.00 25.21  ? 4398 LEU A CD1   1 
ATOM   20973 C  CD2   . LEU A 1 4398 ? 259.862 238.247 214.570 1.00 25.04  ? 4398 LEU A CD2   1 
ATOM   20974 N  N     . LYS A 1 4399 ? 260.610 242.655 216.226 1.00 41.06  ? 4399 LYS A N     1 
ATOM   20975 C  CA    . LYS A 1 4399 ? 260.852 244.079 216.409 1.00 44.48  ? 4399 LYS A CA    1 
ATOM   20976 C  C     . LYS A 1 4399 ? 260.250 244.865 215.251 1.00 46.83  ? 4399 LYS A C     1 
ATOM   20977 O  O     . LYS A 1 4399 ? 260.436 244.513 214.083 1.00 44.92  ? 4399 LYS A O     1 
ATOM   20978 C  CB    . LYS A 1 4399 ? 262.350 244.355 216.515 1.00 46.81  ? 4399 LYS A CB    1 
ATOM   20979 C  CG    . LYS A 1 4399 ? 263.017 243.725 217.726 1.00 48.95  ? 4399 LYS A CG    1 
ATOM   20980 C  CD    . LYS A 1 4399 ? 264.487 244.100 217.800 1.00 53.48  ? 4399 LYS A CD    1 
ATOM   20981 C  CE    . LYS A 1 4399 ? 265.289 243.423 216.699 1.00 50.42  ? 4399 LYS A CE    1 
ATOM   20982 N  NZ    . LYS A 1 4399 ? 265.331 241.944 216.864 1.00 40.80  ? 4399 LYS A NZ    1 
ATOM   20983 N  N     . ARG A 1 4400 ? 259.530 245.935 215.578 1.00 49.96  ? 4400 ARG A N     1 
ATOM   20984 C  CA    . ARG A 1 4400 ? 258.886 246.770 214.577 1.00 41.22  ? 4400 ARG A CA    1 
ATOM   20985 C  C     . ARG A 1 4400 ? 259.837 247.863 214.110 1.00 49.54  ? 4400 ARG A C     1 
ATOM   20986 O  O     . ARG A 1 4400 ? 260.532 248.487 214.917 1.00 55.30  ? 4400 ARG A O     1 
ATOM   20987 C  CB    . ARG A 1 4400 ? 257.607 247.393 215.137 1.00 46.24  ? 4400 ARG A CB    1 
ATOM   20988 C  CG    . ARG A 1 4400 ? 256.379 246.512 215.005 1.00 44.45  ? 4400 ARG A CG    1 
ATOM   20989 C  CD    . ARG A 1 4400 ? 255.105 247.340 214.993 1.00 43.86  ? 4400 ARG A CD    1 
ATOM   20990 N  NE    . ARG A 1 4400 ? 253.986 246.609 214.412 1.00 45.69  ? 4400 ARG A NE    1 
ATOM   20991 C  CZ    . ARG A 1 4400 ? 252.880 247.175 213.949 1.00 45.04  ? 4400 ARG A CZ    1 
ATOM   20992 N  NH1   . ARG A 1 4400 ? 252.709 248.487 213.982 1.00 43.63  ? 4400 ARG A NH1   1 
ATOM   20993 N  NH2   . ARG A 1 4400 ? 251.921 246.407 213.443 1.00 41.64  ? 4400 ARG A NH2   1 
ATOM   20994 N  N     . THR A 1 4401 ? 259.861 248.090 212.799 1.00 53.00  ? 4401 THR A N     1 
ATOM   20995 C  CA    . THR A 1 4401 ? 260.724 249.089 212.189 1.00 53.07  ? 4401 THR A CA    1 
ATOM   20996 C  C     . THR A 1 4401 ? 259.934 249.795 211.091 1.00 57.06  ? 4401 THR A C     1 
ATOM   20997 O  O     . THR A 1 4401 ? 258.979 249.243 210.540 1.00 62.79  ? 4401 THR A O     1 
ATOM   20998 C  CB    . THR A 1 4401 ? 262.006 248.438 211.640 1.00 52.68  ? 4401 THR A CB    1 
ATOM   20999 O  OG1   . THR A 1 4401 ? 262.690 247.774 212.711 1.00 55.24  ? 4401 THR A OG1   1 
ATOM   21000 C  CG2   . THR A 1 4401 ? 262.950 249.477 211.074 1.00 51.22  ? 4401 THR A CG2   1 
ATOM   21001 N  N     . VAL A 1 4402 ? 260.332 251.036 210.790 1.00 57.05  ? 4402 VAL A N     1 
ATOM   21002 C  CA    . VAL A 1 4402 ? 259.548 251.871 209.882 1.00 59.13  ? 4402 VAL A CA    1 
ATOM   21003 C  C     . VAL A 1 4402 ? 259.461 251.245 208.492 1.00 61.58  ? 4402 VAL A C     1 
ATOM   21004 O  O     . VAL A 1 4402 ? 258.414 251.313 207.835 1.00 62.33  ? 4402 VAL A O     1 
ATOM   21005 C  CB    . VAL A 1 4402 ? 260.118 253.303 209.838 1.00 58.28  ? 4402 VAL A CB    1 
ATOM   21006 C  CG1   . VAL A 1 4402 ? 260.016 253.946 211.210 1.00 56.41  ? 4402 VAL A CG1   1 
ATOM   21007 C  CG2   . VAL A 1 4402 ? 261.561 253.303 209.373 1.00 56.05  ? 4402 VAL A CG2   1 
ATOM   21008 N  N     . GLU A 1 4403 ? 260.546 250.628 208.016 1.00 58.98  ? 4403 GLU A N     1 
ATOM   21009 C  CA    . GLU A 1 4403 ? 260.473 249.954 206.725 1.00 57.03  ? 4403 GLU A CA    1 
ATOM   21010 C  C     . GLU A 1 4403 ? 259.957 248.525 206.833 1.00 51.85  ? 4403 GLU A C     1 
ATOM   21011 O  O     . GLU A 1 4403 ? 259.672 247.906 205.801 1.00 54.09  ? 4403 GLU A O     1 
ATOM   21012 C  CB    . GLU A 1 4403 ? 261.836 249.953 206.021 1.00 52.91  ? 4403 GLU A CB    1 
ATOM   21013 C  CG    . GLU A 1 4403 ? 262.902 249.084 206.664 1.00 58.23  ? 4403 GLU A CG    1 
ATOM   21014 C  CD    . GLU A 1 4403 ? 263.655 249.795 207.765 1.00 67.69  ? 4403 GLU A CD    1 
ATOM   21015 O  OE1   . GLU A 1 4403 ? 263.173 250.844 208.233 1.00 69.27  ? 4403 GLU A OE1   1 
ATOM   21016 O  OE2   . GLU A 1 4403 ? 264.728 249.301 208.167 1.00 74.59  ? 4403 GLU A OE2   1 
ATOM   21017 N  N     . ASN A 1 4404 ? 259.835 247.984 208.046 1.00 47.68  ? 4404 ASN A N     1 
ATOM   21018 C  CA    . ASN A 1 4404 ? 259.264 246.652 208.209 1.00 42.87  ? 4404 ASN A CA    1 
ATOM   21019 C  C     . ASN A 1 4404 ? 257.748 246.655 208.069 1.00 41.37  ? 4404 ASN A C     1 
ATOM   21020 O  O     . ASN A 1 4404 ? 257.170 245.658 207.623 1.00 40.03  ? 4404 ASN A O     1 
ATOM   21021 C  CB    . ASN A 1 4404 ? 259.653 246.067 209.568 1.00 41.84  ? 4404 ASN A CB    1 
ATOM   21022 C  CG    . ASN A 1 4404 ? 261.087 245.588 209.609 1.00 49.99  ? 4404 ASN A CG    1 
ATOM   21023 O  OD1   . ASN A 1 4404 ? 261.761 245.521 208.581 1.00 56.50  ? 4404 ASN A OD1   1 
ATOM   21024 N  ND2   . ASN A 1 4404 ? 261.560 245.237 210.799 1.00 43.85  ? 4404 ASN A ND2   1 
ATOM   21025 N  N     . ILE A 1 4405 ? 257.095 247.758 208.441 1.00 46.60  ? 4405 ILE A N     1 
ATOM   21026 C  CA    . ILE A 1 4405 ? 255.634 247.800 208.465 1.00 43.24  ? 4405 ILE A CA    1 
ATOM   21027 C  C     . ILE A 1 4405 ? 255.066 247.642 207.060 1.00 38.48  ? 4405 ILE A C     1 
ATOM   21028 O  O     . ILE A 1 4405 ? 254.047 246.970 206.859 1.00 44.15  ? 4405 ILE A O     1 
ATOM   21029 C  CB    . ILE A 1 4405 ? 255.154 249.102 209.133 1.00 51.02  ? 4405 ILE A CB    1 
ATOM   21030 C  CG1   . ILE A 1 4405 ? 255.584 249.143 210.601 1.00 49.86  ? 4405 ILE A CG1   1 
ATOM   21031 C  CG2   . ILE A 1 4405 ? 253.644 249.243 209.020 1.00 52.72  ? 4405 ILE A CG2   1 
ATOM   21032 C  CD1   . ILE A 1 4405 ? 255.446 247.818 211.323 1.00 45.01  ? 4405 ILE A CD1   1 
ATOM   21033 N  N     . LYS A 1 4406 ? 255.716 248.247 206.066 1.00 39.74  ? 4406 LYS A N     1 
ATOM   21034 C  CA    . LYS A 1 4406 ? 255.208 248.197 204.701 1.00 42.65  ? 4406 LYS A CA    1 
ATOM   21035 C  C     . LYS A 1 4406 ? 255.348 246.816 204.067 1.00 44.95  ? 4406 LYS A C     1 
ATOM   21036 O  O     . LYS A 1 4406 ? 254.762 246.575 203.007 1.00 42.91  ? 4406 LYS A O     1 
ATOM   21037 C  CB    . LYS A 1 4406 ? 255.924 249.238 203.839 1.00 46.52  ? 4406 LYS A CB    1 
ATOM   21038 C  CG    . LYS A 1 4406 ? 255.776 250.666 204.339 1.00 52.91  ? 4406 LYS A CG    1 
ATOM   21039 C  CD    . LYS A 1 4406 ? 256.700 251.611 203.589 1.00 66.40  ? 4406 LYS A CD    1 
ATOM   21040 C  CE    . LYS A 1 4406 ? 257.122 252.782 204.461 1.00 68.79  ? 4406 LYS A CE    1 
ATOM   21041 N  NZ    . LYS A 1 4406 ? 257.390 252.363 205.863 1.00 65.62  ? 4406 LYS A NZ    1 
ATOM   21042 N  N     . ASP A 1 4407 ? 256.103 245.915 204.678 1.00 41.26  ? 4407 ASP A N     1 
ATOM   21043 C  CA    . ASP A 1 4407 ? 256.303 244.584 204.110 1.00 29.92  ? 4407 ASP A CA    1 
ATOM   21044 C  C     . ASP A 1 4407 ? 255.150 243.665 204.490 1.00 31.77  ? 4407 ASP A C     1 
ATOM   21045 O  O     . ASP A 1 4407 ? 254.929 243.428 205.685 1.00 28.58  ? 4407 ASP A O     1 
ATOM   21046 C  CB    . ASP A 1 4407 ? 257.629 244.007 204.595 1.00 31.47  ? 4407 ASP A CB    1 
ATOM   21047 C  CG    . ASP A 1 4407 ? 257.867 242.594 204.103 1.00 34.09  ? 4407 ASP A CG    1 
ATOM   21048 O  OD1   . ASP A 1 4407 ? 257.411 242.261 202.989 1.00 34.23  ? 4407 ASP A OD1   1 
ATOM   21049 O  OD2   . ASP A 1 4407 ? 258.511 241.814 204.833 1.00 38.36  ? 4407 ASP A OD2   1 
ATOM   21050 N  N     . PRO A 1 4408 ? 254.387 243.138 203.526 1.00 30.84  ? 4408 PRO A N     1 
ATOM   21051 C  CA    . PRO A 1 4408 ? 253.308 242.204 203.890 1.00 28.50  ? 4408 PRO A CA    1 
ATOM   21052 C  C     . PRO A 1 4408 ? 253.808 240.935 204.555 1.00 23.70  ? 4408 PRO A C     1 
ATOM   21053 O  O     . PRO A 1 4408 ? 253.137 240.402 205.451 1.00 24.92  ? 4408 PRO A O     1 
ATOM   21054 C  CB    . PRO A 1 4408 ? 252.627 241.918 202.543 1.00 25.42  ? 4408 PRO A CB    1 
ATOM   21055 C  CG    . PRO A 1 4408 ? 253.671 242.211 201.519 1.00 22.30  ? 4408 PRO A CG    1 
ATOM   21056 C  CD    . PRO A 1 4408 ? 254.487 243.338 202.071 1.00 28.51  ? 4408 PRO A CD    1 
ATOM   21057 N  N     . LEU A 1 4409 ? 254.974 240.434 204.141 1.00 25.78  ? 4409 LEU A N     1 
ATOM   21058 C  CA    . LEU A 1 4409 ? 255.541 239.252 204.780 1.00 24.20  ? 4409 LEU A CA    1 
ATOM   21059 C  C     . LEU A 1 4409 ? 255.834 239.515 206.249 1.00 22.04  ? 4409 LEU A C     1 
ATOM   21060 O  O     . LEU A 1 4409 ? 255.544 238.674 207.112 1.00 22.16  ? 4409 LEU A O     1 
ATOM   21061 C  CB    . LEU A 1 4409 ? 256.814 238.821 204.055 1.00 20.84  ? 4409 LEU A CB    1 
ATOM   21062 C  CG    . LEU A 1 4409 ? 256.661 237.938 202.817 1.00 19.85  ? 4409 LEU A CG    1 
ATOM   21063 C  CD1   . LEU A 1 4409 ? 258.028 237.581 202.265 1.00 20.91  ? 4409 LEU A CD1   1 
ATOM   21064 C  CD2   . LEU A 1 4409 ? 255.866 236.687 203.141 1.00 20.56  ? 4409 LEU A CD2   1 
ATOM   21065 N  N     . PHE A 1 4410 ? 256.407 240.681 206.554 1.00 23.44  ? 4410 PHE A N     1 
ATOM   21066 C  CA    . PHE A 1 4410 ? 256.695 241.010 207.943 1.00 21.37  ? 4410 PHE A CA    1 
ATOM   21067 C  C     . PHE A 1 4410 ? 255.412 241.149 208.748 1.00 21.23  ? 4410 PHE A C     1 
ATOM   21068 O  O     . PHE A 1 4410 ? 255.364 240.745 209.910 1.00 26.79  ? 4410 PHE A O     1 
ATOM   21069 C  CB    . PHE A 1 4410 ? 257.525 242.290 208.039 1.00 25.20  ? 4410 PHE A CB    1 
ATOM   21070 C  CG    . PHE A 1 4410 ? 257.738 242.758 209.451 1.00 29.81  ? 4410 PHE A CG    1 
ATOM   21071 C  CD1   . PHE A 1 4410 ? 258.762 242.228 210.217 1.00 34.90  ? 4410 PHE A CD1   1 
ATOM   21072 C  CD2   . PHE A 1 4410 ? 256.909 243.711 210.019 1.00 30.13  ? 4410 PHE A CD2   1 
ATOM   21073 C  CE1   . PHE A 1 4410 ? 258.960 242.645 211.518 1.00 34.22  ? 4410 PHE A CE1   1 
ATOM   21074 C  CE2   . PHE A 1 4410 ? 257.103 244.130 211.318 1.00 33.84  ? 4410 PHE A CE2   1 
ATOM   21075 C  CZ    . PHE A 1 4410 ? 258.130 243.598 212.068 1.00 37.12  ? 4410 PHE A CZ    1 
ATOM   21076 N  N     . ARG A 1 4411 ? 254.367 241.735 208.158 1.00 19.72  ? 4411 ARG A N     1 
ATOM   21077 C  CA    . ARG A 1 4411 ? 253.100 241.848 208.874 1.00 17.94  ? 4411 ARG A CA    1 
ATOM   21078 C  C     . ARG A 1 4411 ? 252.517 240.477 209.187 1.00 17.91  ? 4411 ARG A C     1 
ATOM   21079 O  O     . ARG A 1 4411 ? 252.065 240.226 210.314 1.00 19.71  ? 4411 ARG A O     1 
ATOM   21080 C  CB    . ARG A 1 4411 ? 252.099 242.676 208.069 1.00 21.55  ? 4411 ARG A CB    1 
ATOM   21081 C  CG    . ARG A 1 4411 ? 252.457 244.143 207.927 1.00 24.06  ? 4411 ARG A CG    1 
ATOM   21082 C  CD    . ARG A 1 4411 ? 251.403 244.872 207.114 1.00 23.16  ? 4411 ARG A CD    1 
ATOM   21083 N  NE    . ARG A 1 4411 ? 251.714 246.284 206.936 1.00 39.92  ? 4411 ARG A NE    1 
ATOM   21084 C  CZ    . ARG A 1 4411 ? 250.983 247.126 206.220 1.00 41.93  ? 4411 ARG A CZ    1 
ATOM   21085 N  NH1   . ARG A 1 4411 ? 249.891 246.727 205.589 1.00 35.11  ? 4411 ARG A NH1   1 
ATOM   21086 N  NH2   . ARG A 1 4411 ? 251.354 248.400 206.137 1.00 43.87  ? 4411 ARG A NH2   1 
ATOM   21087 N  N     . PHE A 1 4412 ? 252.525 239.570 208.205 1.00 18.75  ? 4412 PHE A N     1 
ATOM   21088 C  CA    . PHE A 1 4412 ? 251.996 238.232 208.444 1.00 16.25  ? 4412 PHE A CA    1 
ATOM   21089 C  C     . PHE A 1 4412 ? 252.791 237.520 209.529 1.00 16.85  ? 4412 PHE A C     1 
ATOM   21090 O  O     . PHE A 1 4412 ? 252.218 236.909 210.440 1.00 17.57  ? 4412 PHE A O     1 
ATOM   21091 C  CB    . PHE A 1 4412 ? 252.009 237.409 207.157 1.00 16.64  ? 4412 PHE A CB    1 
ATOM   21092 C  CG    . PHE A 1 4412 ? 251.857 235.935 207.394 1.00 15.78  ? 4412 PHE A CG    1 
ATOM   21093 C  CD1   . PHE A 1 4412 ? 250.612 235.394 207.665 1.00 18.73  ? 4412 PHE A CD1   1 
ATOM   21094 C  CD2   . PHE A 1 4412 ? 252.956 235.094 207.377 1.00 16.36  ? 4412 PHE A CD2   1 
ATOM   21095 C  CE1   . PHE A 1 4412 ? 250.464 234.045 207.896 1.00 17.30  ? 4412 PHE A CE1   1 
ATOM   21096 C  CE2   . PHE A 1 4412 ? 252.813 233.745 207.613 1.00 18.44  ? 4412 PHE A CE2   1 
ATOM   21097 C  CZ    . PHE A 1 4412 ? 251.565 233.219 207.872 1.00 19.87  ? 4412 PHE A CZ    1 
ATOM   21098 N  N     . PHE A 1 4413 ? 254.122 237.590 209.449 1.00 18.05  ? 4413 PHE A N     1 
ATOM   21099 C  CA    . PHE A 1 4413 ? 254.943 236.895 210.433 1.00 15.74  ? 4413 PHE A CA    1 
ATOM   21100 C  C     . PHE A 1 4413 ? 254.828 237.532 211.811 1.00 17.59  ? 4413 PHE A C     1 
ATOM   21101 O  O     . PHE A 1 4413 ? 254.867 236.822 212.818 1.00 23.20  ? 4413 PHE A O     1 
ATOM   21102 C  CB    . PHE A 1 4413 ? 256.398 236.854 209.969 1.00 17.47  ? 4413 PHE A CB    1 
ATOM   21103 C  CG    . PHE A 1 4413 ? 256.670 235.788 208.947 1.00 20.84  ? 4413 PHE A CG    1 
ATOM   21104 C  CD1   . PHE A 1 4413 ? 256.266 234.483 209.169 1.00 20.71  ? 4413 PHE A CD1   1 
ATOM   21105 C  CD2   . PHE A 1 4413 ? 257.323 236.090 207.766 1.00 23.24  ? 4413 PHE A CD2   1 
ATOM   21106 C  CE1   . PHE A 1 4413 ? 256.509 233.500 208.233 1.00 21.47  ? 4413 PHE A CE1   1 
ATOM   21107 C  CE2   . PHE A 1 4413 ? 257.569 235.110 206.827 1.00 24.61  ? 4413 PHE A CE2   1 
ATOM   21108 C  CZ    . PHE A 1 4413 ? 257.162 233.814 207.061 1.00 26.18  ? 4413 PHE A CZ    1 
ATOM   21109 N  N     . GLU A 1 4414 ? 254.668 238.854 211.880 1.00 17.93  ? 4414 GLU A N     1 
ATOM   21110 C  CA    . GLU A 1 4414 ? 254.447 239.510 213.162 1.00 18.10  ? 4414 GLU A CA    1 
ATOM   21111 C  C     . GLU A 1 4414 ? 253.143 239.056 213.795 1.00 18.89  ? 4414 GLU A C     1 
ATOM   21112 O  O     . GLU A 1 4414 ? 253.100 238.771 214.996 1.00 19.36  ? 4414 GLU A O     1 
ATOM   21113 C  CB    . GLU A 1 4414 ? 254.445 241.028 212.986 1.00 17.19  ? 4414 GLU A CB    1 
ATOM   21114 C  CG    . GLU A 1 4414 ? 254.298 241.790 214.292 1.00 27.83  ? 4414 GLU A CG    1 
ATOM   21115 C  CD    . GLU A 1 4414 ? 254.344 243.292 214.104 1.00 46.18  ? 4414 GLU A CD    1 
ATOM   21116 O  OE1   . GLU A 1 4414 ? 254.468 243.745 212.949 1.00 56.59  ? 4414 GLU A OE1   1 
ATOM   21117 O  OE2   . GLU A 1 4414 ? 254.250 244.019 215.115 1.00 47.09  ? 4414 GLU A OE2   1 
ATOM   21118 N  N     . ARG A 1 4415 ? 252.065 238.988 213.009 1.00 16.30  ? 4415 ARG A N     1 
ATOM   21119 C  CA    . ARG A 1 4415 ? 250.800 238.510 213.560 1.00 15.80  ? 4415 ARG A CA    1 
ATOM   21120 C  C     . ARG A 1 4415 ? 250.912 237.057 214.006 1.00 19.07  ? 4415 ARG A C     1 
ATOM   21121 O  O     . ARG A 1 4415 ? 250.390 236.681 215.064 1.00 21.45  ? 4415 ARG A O     1 
ATOM   21122 C  CB    . ARG A 1 4415 ? 249.677 238.676 212.539 1.00 16.76  ? 4415 ARG A CB    1 
ATOM   21123 C  CG    . ARG A 1 4415 ? 248.308 238.316 213.088 1.00 15.34  ? 4415 ARG A CG    1 
ATOM   21124 C  CD    . ARG A 1 4415 ? 247.196 238.724 212.143 1.00 19.35  ? 4415 ARG A CD    1 
ATOM   21125 N  NE    . ARG A 1 4415 ? 247.152 237.894 210.947 1.00 18.57  ? 4415 ARG A NE    1 
ATOM   21126 C  CZ    . ARG A 1 4415 ? 246.334 238.102 209.924 1.00 21.61  ? 4415 ARG A CZ    1 
ATOM   21127 N  NH1   . ARG A 1 4415 ? 245.483 239.113 209.916 1.00 26.00  ? 4415 ARG A NH1   1 
ATOM   21128 N  NH2   . ARG A 1 4415 ? 246.373 237.275 208.884 1.00 26.57  ? 4415 ARG A NH2   1 
ATOM   21129 N  N     . GLU A 1 4416 ? 251.599 236.230 213.214 1.00 16.73  ? 4416 GLU A N     1 
ATOM   21130 C  CA    . GLU A 1 4416 ? 251.802 234.835 213.590 1.00 14.56  ? 4416 GLU A CA    1 
ATOM   21131 C  C     . GLU A 1 4416 ? 252.558 234.729 214.906 1.00 17.57  ? 4416 GLU A C     1 
ATOM   21132 O  O     . GLU A 1 4416 ? 252.183 233.953 215.792 1.00 21.73  ? 4416 GLU A O     1 
ATOM   21133 C  CB    . GLU A 1 4416 ? 252.557 234.102 212.481 1.00 18.51  ? 4416 GLU A CB    1 
ATOM   21134 C  CG    . GLU A 1 4416 ? 251.694 233.680 211.308 1.00 26.71  ? 4416 GLU A CG    1 
ATOM   21135 C  CD    . GLU A 1 4416 ? 250.796 232.508 211.636 1.00 27.31  ? 4416 GLU A CD    1 
ATOM   21136 O  OE1   . GLU A 1 4416 ? 249.574 232.608 211.403 1.00 26.42  ? 4416 GLU A OE1   1 
ATOM   21137 O  OE2   . GLU A 1 4416 ? 251.315 231.483 212.123 1.00 30.67  ? 4416 GLU A OE2   1 
ATOM   21138 N  N     . VAL A 1 4417 ? 253.625 235.516 215.055 1.00 16.75  ? 4417 VAL A N     1 
ATOM   21139 C  CA    . VAL A 1 4417 ? 254.432 235.463 216.267 1.00 14.55  ? 4417 VAL A CA    1 
ATOM   21140 C  C     . VAL A 1 4417 ? 253.640 235.971 217.464 1.00 15.89  ? 4417 VAL A C     1 
ATOM   21141 O  O     . VAL A 1 4417 ? 253.743 235.420 218.562 1.00 18.25  ? 4417 VAL A O     1 
ATOM   21142 C  CB    . VAL A 1 4417 ? 255.742 236.249 216.067 1.00 16.60  ? 4417 VAL A CB    1 
ATOM   21143 C  CG1   . VAL A 1 4417 ? 256.448 236.461 217.396 1.00 20.76  ? 4417 VAL A CG1   1 
ATOM   21144 C  CG2   . VAL A 1 4417 ? 256.651 235.513 215.102 1.00 13.21  ? 4417 VAL A CG2   1 
ATOM   21145 N  N     . LYS A 1 4418 ? 252.837 237.020 217.278 1.00 15.55  ? 4418 LYS A N     1 
ATOM   21146 C  CA    . LYS A 1 4418 ? 252.038 237.533 218.387 1.00 13.65  ? 4418 LYS A CA    1 
ATOM   21147 C  C     . LYS A 1 4418 ? 251.007 236.510 218.848 1.00 15.97  ? 4418 LYS A C     1 
ATOM   21148 O  O     . LYS A 1 4418 ? 250.848 236.272 220.052 1.00 18.07  ? 4418 LYS A O     1 
ATOM   21149 C  CB    . LYS A 1 4418 ? 251.354 238.844 217.996 1.00 18.40  ? 4418 LYS A CB    1 
ATOM   21150 C  CG    . LYS A 1 4418 ? 252.304 240.006 217.767 1.00 19.52  ? 4418 LYS A CG    1 
ATOM   21151 C  CD    . LYS A 1 4418 ? 251.537 241.299 217.548 1.00 23.06  ? 4418 LYS A CD    1 
ATOM   21152 C  CE    . LYS A 1 4418 ? 250.890 241.327 216.174 1.00 25.65  ? 4418 LYS A CE    1 
ATOM   21153 N  NZ    . LYS A 1 4418 ? 250.227 242.629 215.899 1.00 27.73  ? 4418 LYS A NZ    1 
ATOM   21154 N  N     . MET A 1 4419 ? 250.296 235.889 217.900 1.00 18.77  ? 4419 MET A N     1 
ATOM   21155 C  CA    . MET A 1 4419 ? 249.324 234.866 218.279 1.00 15.39  ? 4419 MET A CA    1 
ATOM   21156 C  C     . MET A 1 4419 ? 250.003 233.677 218.945 1.00 16.36  ? 4419 MET A C     1 
ATOM   21157 O  O     . MET A 1 4419 ? 249.511 233.162 219.959 1.00 16.00  ? 4419 MET A O     1 
ATOM   21158 C  CB    . MET A 1 4419 ? 248.520 234.417 217.059 1.00 16.02  ? 4419 MET A CB    1 
ATOM   21159 C  CG    . MET A 1 4419 ? 247.722 235.526 216.401 1.00 20.64  ? 4419 MET A CG    1 
ATOM   21160 S  SD    . MET A 1 4419 ? 246.914 235.013 214.874 1.00 55.22  ? 4419 MET A SD    1 
ATOM   21161 C  CE    . MET A 1 4419 ? 248.212 234.048 214.112 1.00 26.56  ? 4419 MET A CE    1 
ATOM   21162 N  N     . GLY A 1 4420 ? 251.140 233.239 218.401 1.00 16.90  ? 4420 GLY A N     1 
ATOM   21163 C  CA    . GLY A 1 4420 ? 251.859 232.132 219.005 1.00 13.56  ? 4420 GLY A CA    1 
ATOM   21164 C  C     . GLY A 1 4420 ? 252.350 232.448 220.403 1.00 14.07  ? 4420 GLY A C     1 
ATOM   21165 O  O     . GLY A 1 4420 ? 252.260 231.613 221.301 1.00 20.44  ? 4420 GLY A O     1 
ATOM   21166 N  N     . ALA A 1 4421 ? 252.864 233.661 220.609 1.00 10.56  ? 4421 ALA A N     1 
ATOM   21167 C  CA    . ALA A 1 4421 ? 253.351 234.052 221.928 1.00 12.16  ? 4421 ALA A CA    1 
ATOM   21168 C  C     . ALA A 1 4421 ? 252.212 234.149 222.932 1.00 13.57  ? 4421 ALA A C     1 
ATOM   21169 O  O     . ALA A 1 4421 ? 252.356 233.719 224.082 1.00 17.52  ? 4421 ALA A O     1 
ATOM   21170 C  CB    . ALA A 1 4421 ? 254.102 235.379 221.837 1.00 12.14  ? 4421 ALA A CB    1 
ATOM   21171 N  N     . LYS A 1 4422 ? 251.074 234.714 222.523 1.00 13.01  ? 4422 LYS A N     1 
ATOM   21172 C  CA    . LYS A 1 4422 ? 249.939 234.810 223.435 1.00 12.75  ? 4422 LYS A CA    1 
ATOM   21173 C  C     . LYS A 1 4422 ? 249.424 233.428 223.817 1.00 17.28  ? 4422 LYS A C     1 
ATOM   21174 O  O     . LYS A 1 4422 ? 249.179 233.151 224.999 1.00 17.48  ? 4422 LYS A O     1 
ATOM   21175 C  CB    . LYS A 1 4422 ? 248.829 235.649 222.804 1.00 12.90  ? 4422 LYS A CB    1 
ATOM   21176 C  CG    . LYS A 1 4422 ? 247.625 235.857 223.703 1.00 20.21  ? 4422 LYS A CG    1 
ATOM   21177 C  CD    . LYS A 1 4422 ? 246.612 236.790 223.063 1.00 25.79  ? 4422 LYS A CD    1 
ATOM   21178 C  CE    . LYS A 1 4422 ? 245.345 236.880 223.896 1.00 44.93  ? 4422 LYS A CE    1 
ATOM   21179 N  NZ    . LYS A 1 4422 ? 245.595 237.526 225.215 1.00 43.86  ? 4422 LYS A NZ    1 
ATOM   21180 N  N     . LEU A 1 4423 ? 249.274 232.537 222.832 1.00 17.35  ? 4423 LEU A N     1 
ATOM   21181 C  CA    . LEU A 1 4423 ? 248.820 231.184 223.131 1.00 13.20  ? 4423 LEU A CA    1 
ATOM   21182 C  C     . LEU A 1 4423 ? 249.837 230.431 223.980 1.00 14.11  ? 4423 LEU A C     1 
ATOM   21183 O  O     . LEU A 1 4423 ? 249.462 229.669 224.875 1.00 18.89  ? 4423 LEU A O     1 
ATOM   21184 C  CB    . LEU A 1 4423 ? 248.527 230.427 221.838 1.00 17.65  ? 4423 LEU A CB    1 
ATOM   21185 C  CG    . LEU A 1 4423 ? 247.817 229.086 222.023 1.00 18.79  ? 4423 LEU A CG    1 
ATOM   21186 C  CD1   . LEU A 1 4423 ? 246.577 229.256 222.875 1.00 16.21  ? 4423 LEU A CD1   1 
ATOM   21187 C  CD2   . LEU A 1 4423 ? 247.453 228.490 220.674 1.00 20.10  ? 4423 LEU A CD2   1 
ATOM   21188 N  N     . LEU A 1 4424 ? 251.129 230.627 223.709 1.00 13.50  ? 4424 LEU A N     1 
ATOM   21189 C  CA    . LEU A 1 4424 ? 252.164 229.968 224.494 1.00 14.69  ? 4424 LEU A CA    1 
ATOM   21190 C  C     . LEU A 1 4424 ? 252.125 230.427 225.943 1.00 17.15  ? 4424 LEU A C     1 
ATOM   21191 O  O     . LEU A 1 4424 ? 252.211 229.607 226.864 1.00 20.37  ? 4424 LEU A O     1 
ATOM   21192 C  CB    . LEU A 1 4424 ? 253.534 230.245 223.876 1.00 13.31  ? 4424 LEU A CB    1 
ATOM   21193 C  CG    . LEU A 1 4424 ? 254.760 229.903 224.719 1.00 18.30  ? 4424 LEU A CG    1 
ATOM   21194 C  CD1   . LEU A 1 4424 ? 254.836 228.408 224.938 1.00 19.64  ? 4424 LEU A CD1   1 
ATOM   21195 C  CD2   . LEU A 1 4424 ? 256.025 230.414 224.057 1.00 19.57  ? 4424 LEU A CD2   1 
ATOM   21196 N  N     . GLN A 1 4425 ? 251.982 231.735 226.163 1.00 17.68  ? 4425 GLN A N     1 
ATOM   21197 C  CA    . GLN A 1 4425 ? 251.885 232.249 227.523 1.00 16.89  ? 4425 GLN A CA    1 
ATOM   21198 C  C     . GLN A 1 4425 ? 250.648 231.706 228.227 1.00 17.14  ? 4425 GLN A C     1 
ATOM   21199 O  O     . GLN A 1 4425 ? 250.720 231.299 229.392 1.00 16.60  ? 4425 GLN A O     1 
ATOM   21200 C  CB    . GLN A 1 4425 ? 251.874 233.776 227.502 1.00 17.17  ? 4425 GLN A CB    1 
ATOM   21201 C  CG    . GLN A 1 4425 ? 251.973 234.420 228.871 1.00 18.78  ? 4425 GLN A CG    1 
ATOM   21202 C  CD    . GLN A 1 4425 ? 251.465 235.846 228.878 1.00 25.38  ? 4425 GLN A CD    1 
ATOM   21203 O  OE1   . GLN A 1 4425 ? 250.282 236.096 228.652 1.00 32.75  ? 4425 GLN A OE1   1 
ATOM   21204 N  NE2   . GLN A 1 4425 ? 252.360 236.791 229.138 1.00 25.08  ? 4425 GLN A NE2   1 
ATOM   21205 N  N     . ASP A 1 4426 ? 249.509 231.672 227.530 1.00 18.04  ? 4426 ASP A N     1 
ATOM   21206 C  CA    . ASP A 1 4426 ? 248.285 231.163 228.144 1.00 20.73  ? 4426 ASP A CA    1 
ATOM   21207 C  C     . ASP A 1 4426 ? 248.421 229.691 228.518 1.00 21.22  ? 4426 ASP A C     1 
ATOM   21208 O  O     . ASP A 1 4426 ? 248.056 229.282 229.627 1.00 23.20  ? 4426 ASP A O     1 
ATOM   21209 C  CB    . ASP A 1 4426 ? 247.101 231.371 227.200 1.00 18.78  ? 4426 ASP A CB    1 
ATOM   21210 C  CG    . ASP A 1 4426 ? 246.747 232.832 227.023 1.00 30.88  ? 4426 ASP A CG    1 
ATOM   21211 O  OD1   . ASP A 1 4426 ? 247.293 233.673 227.768 1.00 31.75  ? 4426 ASP A OD1   1 
ATOM   21212 O  OD2   . ASP A 1 4426 ? 245.921 233.143 226.139 1.00 39.11  ? 4426 ASP A OD2   1 
ATOM   21213 N  N     . VAL A 1 4427 ? 248.959 228.880 227.604 1.00 17.23  ? 4427 VAL A N     1 
ATOM   21214 C  CA    . VAL A 1 4427 ? 249.081 227.446 227.853 1.00 16.23  ? 4427 VAL A CA    1 
ATOM   21215 C  C     . VAL A 1 4427 ? 250.079 227.178 228.972 1.00 19.59  ? 4427 VAL A C     1 
ATOM   21216 O  O     . VAL A 1 4427 ? 249.836 226.339 229.848 1.00 21.49  ? 4427 VAL A O     1 
ATOM   21217 C  CB    . VAL A 1 4427 ? 249.466 226.713 226.555 1.00 18.42  ? 4427 VAL A CB    1 
ATOM   21218 C  CG1   . VAL A 1 4427 ? 249.923 225.294 226.853 1.00 17.34  ? 4427 VAL A CG1   1 
ATOM   21219 C  CG2   . VAL A 1 4427 ? 248.294 226.703 225.589 1.00 18.28  ? 4427 VAL A CG2   1 
ATOM   21220 N  N     . ARG A 1 4428 ? 251.214 227.881 228.965 1.00 19.24  ? 4428 ARG A N     1 
ATOM   21221 C  CA    . ARG A 1 4428 ? 252.203 227.693 230.020 1.00 18.00  ? 4428 ARG A CA    1 
ATOM   21222 C  C     . ARG A 1 4428 ? 251.658 228.122 231.375 1.00 19.57  ? 4428 ARG A C     1 
ATOM   21223 O  O     . ARG A 1 4428 ? 251.909 227.456 232.385 1.00 22.09  ? 4428 ARG A O     1 
ATOM   21224 C  CB    . ARG A 1 4428 ? 253.482 228.457 229.681 1.00 18.83  ? 4428 ARG A CB    1 
ATOM   21225 C  CG    . ARG A 1 4428 ? 254.302 227.822 228.571 1.00 17.80  ? 4428 ARG A CG    1 
ATOM   21226 C  CD    . ARG A 1 4428 ? 255.715 228.376 228.542 1.00 21.16  ? 4428 ARG A CD    1 
ATOM   21227 N  NE    . ARG A 1 4428 ? 256.516 227.897 229.662 1.00 22.73  ? 4428 ARG A NE    1 
ATOM   21228 C  CZ    . ARG A 1 4428 ? 257.113 226.714 229.704 1.00 24.94  ? 4428 ARG A CZ    1 
ATOM   21229 N  NH1   . ARG A 1 4428 ? 257.026 225.859 228.699 1.00 27.65  ? 4428 ARG A NH1   1 
ATOM   21230 N  NH2   . ARG A 1 4428 ? 257.815 226.381 230.783 1.00 23.12  ? 4428 ARG A NH2   1 
ATOM   21231 N  N     . GLN A 1 4429 ? 250.912 229.230 231.423 1.00 19.82  ? 4429 GLN A N     1 
ATOM   21232 C  CA    . GLN A 1 4429 ? 250.321 229.657 232.686 1.00 20.07  ? 4429 GLN A CA    1 
ATOM   21233 C  C     . GLN A 1 4429 ? 249.294 228.649 233.185 1.00 21.43  ? 4429 GLN A C     1 
ATOM   21234 O  O     . GLN A 1 4429 ? 249.245 228.345 234.383 1.00 23.54  ? 4429 GLN A O     1 
ATOM   21235 C  CB    . GLN A 1 4429 ? 249.688 231.039 232.526 1.00 22.55  ? 4429 GLN A CB    1 
ATOM   21236 C  CG    . GLN A 1 4429 ? 249.389 231.737 233.839 1.00 23.11  ? 4429 GLN A CG    1 
ATOM   21237 C  CD    . GLN A 1 4429 ? 250.571 231.725 234.786 1.00 31.09  ? 4429 GLN A CD    1 
ATOM   21238 O  OE1   . GLN A 1 4429 ? 250.463 231.280 235.927 1.00 30.31  ? 4429 GLN A OE1   1 
ATOM   21239 N  NE2   . GLN A 1 4429 ? 251.711 232.216 234.314 1.00 29.23  ? 4429 GLN A NE2   1 
ATOM   21240 N  N     . ASP A 1 4430 ? 248.466 228.118 232.282 1.00 19.49  ? 4430 ASP A N     1 
ATOM   21241 C  CA    . ASP A 1 4430 ? 247.490 227.111 232.687 1.00 19.99  ? 4430 ASP A CA    1 
ATOM   21242 C  C     . ASP A 1 4430 ? 248.178 225.856 233.208 1.00 23.13  ? 4430 ASP A C     1 
ATOM   21243 O  O     . ASP A 1 4430 ? 247.750 225.275 234.212 1.00 25.30  ? 4430 ASP A O     1 
ATOM   21244 C  CB    . ASP A 1 4430 ? 246.568 226.774 231.516 1.00 24.74  ? 4430 ASP A CB    1 
ATOM   21245 C  CG    . ASP A 1 4430 ? 245.651 227.922 231.148 1.00 30.26  ? 4430 ASP A CG    1 
ATOM   21246 O  OD1   . ASP A 1 4430 ? 245.719 228.979 231.810 1.00 32.72  ? 4430 ASP A OD1   1 
ATOM   21247 O  OD2   . ASP A 1 4430 ? 244.858 227.767 230.197 1.00 34.74  ? 4430 ASP A OD2   1 
ATOM   21248 N  N     . LEU A 1 4431 ? 249.252 225.427 232.542 1.00 23.59  ? 4431 LEU A N     1 
ATOM   21249 C  CA    . LEU A 1 4431 ? 249.990 224.254 233.000 1.00 20.01  ? 4431 LEU A CA    1 
ATOM   21250 C  C     . LEU A 1 4431 ? 250.642 224.505 234.354 1.00 22.79  ? 4431 LEU A C     1 
ATOM   21251 O  O     . LEU A 1 4431 ? 250.669 223.614 235.212 1.00 28.48  ? 4431 LEU A O     1 
ATOM   21252 C  CB    . LEU A 1 4431 ? 251.038 223.860 231.963 1.00 22.94  ? 4431 LEU A CB    1 
ATOM   21253 C  CG    . LEU A 1 4431 ? 250.511 223.085 230.754 1.00 18.04  ? 4431 LEU A CG    1 
ATOM   21254 C  CD1   . LEU A 1 4431 ? 251.640 222.774 229.791 1.00 19.61  ? 4431 LEU A CD1   1 
ATOM   21255 C  CD2   . LEU A 1 4431 ? 249.811 221.816 231.201 1.00 15.25  ? 4431 LEU A CD2   1 
ATOM   21256 N  N     . ALA A 1 4432 ? 251.178 225.710 234.562 1.00 21.11  ? 4432 ALA A N     1 
ATOM   21257 C  CA    . ALA A 1 4432 ? 251.767 226.046 235.853 1.00 24.65  ? 4432 ALA A CA    1 
ATOM   21258 C  C     . ALA A 1 4432 ? 250.721 226.030 236.959 1.00 29.34  ? 4432 ALA A C     1 
ATOM   21259 O  O     . ALA A 1 4432 ? 250.982 225.537 238.063 1.00 29.46  ? 4432 ALA A O     1 
ATOM   21260 C  CB    . ALA A 1 4432 ? 252.448 227.412 235.777 1.00 25.69  ? 4432 ALA A CB    1 
ATOM   21261 N  N     . ASP A 1 4433 ? 249.530 226.568 236.683 1.00 29.83  ? 4433 ASP A N     1 
ATOM   21262 C  CA    . ASP A 1 4433 ? 248.459 226.529 237.675 1.00 27.68  ? 4433 ASP A CA    1 
ATOM   21263 C  C     . ASP A 1 4433 ? 248.017 225.099 237.959 1.00 26.30  ? 4433 ASP A C     1 
ATOM   21264 O  O     . ASP A 1 4433 ? 247.710 224.755 239.106 1.00 29.48  ? 4433 ASP A O     1 
ATOM   21265 C  CB    . ASP A 1 4433 ? 247.276 227.379 237.214 1.00 27.81  ? 4433 ASP A CB    1 
ATOM   21266 C  CG    . ASP A 1 4433 ? 247.672 228.807 236.900 1.00 33.94  ? 4433 ASP A CG    1 
ATOM   21267 O  OD1   . ASP A 1 4433 ? 248.876 229.126 236.990 1.00 34.10  ? 4433 ASP A OD1   1 
ATOM   21268 O  OD2   . ASP A 1 4433 ? 246.779 229.612 236.562 1.00 36.74  ? 4433 ASP A OD2   1 
ATOM   21269 N  N     . VAL A 1 4434 ? 247.972 224.251 236.929 1.00 26.69  ? 4434 VAL A N     1 
ATOM   21270 C  CA    . VAL A 1 4434 ? 247.637 222.845 237.142 1.00 25.73  ? 4434 VAL A CA    1 
ATOM   21271 C  C     . VAL A 1 4434 ? 248.683 222.179 238.028 1.00 27.58  ? 4434 VAL A C     1 
ATOM   21272 O  O     . VAL A 1 4434 ? 248.349 221.405 238.934 1.00 27.69  ? 4434 VAL A O     1 
ATOM   21273 C  CB    . VAL A 1 4434 ? 247.488 222.117 235.792 1.00 25.09  ? 4434 VAL A CB    1 
ATOM   21274 C  CG1   . VAL A 1 4434 ? 247.468 220.614 235.996 1.00 31.58  ? 4434 VAL A CG1   1 
ATOM   21275 C  CG2   . VAL A 1 4434 ? 246.221 222.563 235.094 1.00 24.43  ? 4434 VAL A CG2   1 
ATOM   21276 N  N     . VAL A 1 4435 ? 249.962 222.471 237.784 1.00 28.16  ? 4435 VAL A N     1 
ATOM   21277 C  CA    . VAL A 1 4435 ? 251.027 221.906 238.609 1.00 28.99  ? 4435 VAL A CA    1 
ATOM   21278 C  C     . VAL A 1 4435 ? 250.887 222.371 240.052 1.00 34.42  ? 4435 VAL A C     1 
ATOM   21279 O  O     . VAL A 1 4435 ? 251.014 221.577 240.992 1.00 39.37  ? 4435 VAL A O     1 
ATOM   21280 C  CB    . VAL A 1 4435 ? 252.407 222.270 238.029 1.00 33.41  ? 4435 VAL A CB    1 
ATOM   21281 C  CG1   . VAL A 1 4435 ? 253.499 222.042 239.064 1.00 37.91  ? 4435 VAL A CG1   1 
ATOM   21282 C  CG2   . VAL A 1 4435 ? 252.686 221.463 236.777 1.00 34.30  ? 4435 VAL A CG2   1 
ATOM   21283 N  N     . GLN A 1 4436 ? 250.619 223.664 240.252 1.00 33.98  ? 4436 GLN A N     1 
ATOM   21284 C  CA    . GLN A 1 4436 ? 250.461 224.189 241.605 1.00 30.50  ? 4436 GLN A CA    1 
ATOM   21285 C  C     . GLN A 1 4436 ? 249.272 223.551 242.312 1.00 28.77  ? 4436 GLN A C     1 
ATOM   21286 O  O     . GLN A 1 4436 ? 249.340 223.251 243.510 1.00 38.81  ? 4436 GLN A O     1 
ATOM   21287 C  CB    . GLN A 1 4436 ? 250.312 225.710 241.572 1.00 32.11  ? 4436 GLN A CB    1 
ATOM   21288 C  CG    . GLN A 1 4436 ? 251.530 226.444 241.044 1.00 38.92  ? 4436 GLN A CG    1 
ATOM   21289 C  CD    . GLN A 1 4436 ? 252.735 226.302 241.950 1.00 53.88  ? 4436 GLN A CD    1 
ATOM   21290 O  OE1   . GLN A 1 4436 ? 252.611 226.320 243.175 1.00 53.15  ? 4436 GLN A OE1   1 
ATOM   21291 N  NE2   . GLN A 1 4436 ? 253.912 226.159 241.352 1.00 54.82  ? 4436 GLN A NE2   1 
ATOM   21292 N  N     . VAL A 1 4437 ? 248.168 223.345 241.591 1.00 26.56  ? 4437 VAL A N     1 
ATOM   21293 C  CA    . VAL A 1 4437 ? 247.010 222.675 242.177 1.00 28.93  ? 4437 VAL A CA    1 
ATOM   21294 C  C     . VAL A 1 4437 ? 247.366 221.247 242.568 1.00 30.60  ? 4437 VAL A C     1 
ATOM   21295 O  O     . VAL A 1 4437 ? 247.010 220.776 243.656 1.00 31.69  ? 4437 VAL A O     1 
ATOM   21296 C  CB    . VAL A 1 4437 ? 245.818 222.713 241.203 1.00 25.75  ? 4437 VAL A CB    1 
ATOM   21297 C  CG1   . VAL A 1 4437 ? 244.825 221.617 241.540 1.00 24.08  ? 4437 VAL A CG1   1 
ATOM   21298 C  CG2   . VAL A 1 4437 ? 245.144 224.071 241.244 1.00 23.40  ? 4437 VAL A CG2   1 
ATOM   21299 N  N     . CYS A 1 4438 ? 248.081 220.537 241.693 1.00 34.22  ? 4438 CYS A N     1 
ATOM   21300 C  CA    . CYS A 1 4438 ? 248.473 219.167 241.991 1.00 32.98  ? 4438 CYS A CA    1 
ATOM   21301 C  C     . CYS A 1 4438 ? 249.468 219.084 243.141 1.00 35.68  ? 4438 CYS A C     1 
ATOM   21302 O  O     . CYS A 1 4438 ? 249.566 218.032 243.781 1.00 43.44  ? 4438 CYS A O     1 
ATOM   21303 C  CB    . CYS A 1 4438 ? 249.054 218.504 240.744 1.00 32.84  ? 4438 CYS A CB    1 
ATOM   21304 S  SG    . CYS A 1 4438 ? 247.848 218.210 239.434 1.00 41.97  ? 4438 CYS A SG    1 
ATOM   21305 N  N     . GLU A 1 4439 ? 250.202 220.159 243.416 1.00 40.57  ? 4439 GLU A N     1 
ATOM   21306 C  CA    . GLU A 1 4439 ? 251.079 220.208 244.577 1.00 38.14  ? 4439 GLU A CA    1 
ATOM   21307 C  C     . GLU A 1 4439 ? 250.338 220.562 245.858 1.00 37.74  ? 4439 GLU A C     1 
ATOM   21308 O  O     . GLU A 1 4439 ? 250.948 220.540 246.933 1.00 45.75  ? 4439 GLU A O     1 
ATOM   21309 C  CB    . GLU A 1 4439 ? 252.209 221.213 244.343 1.00 39.16  ? 4439 GLU A CB    1 
ATOM   21310 C  CG    . GLU A 1 4439 ? 253.188 220.809 243.255 1.00 39.96  ? 4439 GLU A CG    1 
ATOM   21311 C  CD    . GLU A 1 4439 ? 254.279 221.840 243.043 1.00 58.03  ? 4439 GLU A CD    1 
ATOM   21312 O  OE1   . GLU A 1 4439 ? 254.201 222.926 243.655 1.00 60.57  ? 4439 GLU A OE1   1 
ATOM   21313 O  OE2   . GLU A 1 4439 ? 255.215 221.564 242.262 1.00 57.08  ? 4439 GLU A OE2   1 
ATOM   21314 N  N     . GLY A 1 4440 ? 249.050 220.883 245.772 1.00 35.21  ? 4440 GLY A N     1 
ATOM   21315 C  CA    . GLY A 1 4440 ? 248.275 221.249 246.938 1.00 32.06  ? 4440 GLY A CA    1 
ATOM   21316 C  C     . GLY A 1 4440 ? 248.511 222.650 247.447 1.00 39.66  ? 4440 GLY A C     1 
ATOM   21317 O  O     . GLY A 1 4440 ? 248.087 222.964 248.566 1.00 44.06  ? 4440 GLY A O     1 
ATOM   21318 N  N     . LYS A 1 4441 ? 249.170 223.505 246.666 1.00 38.82  ? 4441 LYS A N     1 
ATOM   21319 C  CA    . LYS A 1 4441 ? 249.502 224.852 247.117 1.00 42.66  ? 4441 LYS A CA    1 
ATOM   21320 C  C     . LYS A 1 4441 ? 248.360 225.837 246.874 1.00 46.18  ? 4441 LYS A C     1 
ATOM   21321 O  O     . LYS A 1 4441 ? 247.863 226.462 247.816 1.00 51.98  ? 4441 LYS A O     1 
ATOM   21322 C  CB    . LYS A 1 4441 ? 250.785 225.332 246.431 1.00 39.06  ? 4441 LYS A CB    1 
ATOM   21323 C  CG    . LYS A 1 4441 ? 252.049 224.674 246.960 1.00 50.72  ? 4441 LYS A CG    1 
ATOM   21324 C  CD    . LYS A 1 4441 ? 253.283 225.185 246.234 1.00 59.59  ? 4441 LYS A CD    1 
ATOM   21325 C  CE    . LYS A 1 4441 ? 254.537 224.466 246.701 1.00 57.26  ? 4441 LYS A CE    1 
ATOM   21326 N  NZ    . LYS A 1 4441 ? 255.705 224.769 245.829 1.00 57.44  ? 4441 LYS A NZ    1 
ATOM   21327 N  N     . LYS A 1 4442 ? 247.935 225.984 245.624 1.00 35.17  ? 4442 LYS A N     1 
ATOM   21328 C  CA    . LYS A 1 4442 ? 246.928 226.972 245.270 1.00 33.12  ? 4442 LYS A CA    1 
ATOM   21329 C  C     . LYS A 1 4442 ? 245.549 226.327 245.174 1.00 32.77  ? 4442 LYS A C     1 
ATOM   21330 O  O     . LYS A 1 4442 ? 245.413 225.149 244.833 1.00 26.12  ? 4442 LYS A O     1 
ATOM   21331 C  CB    . LYS A 1 4442 ? 247.279 227.671 243.953 1.00 28.92  ? 4442 LYS A CB    1 
ATOM   21332 C  CG    . LYS A 1 4442 ? 246.878 226.919 242.699 1.00 26.52  ? 4442 LYS A CG    1 
ATOM   21333 C  CD    . LYS A 1 4442 ? 247.241 227.710 241.455 1.00 25.66  ? 4442 LYS A CD    1 
ATOM   21334 C  CE    . LYS A 1 4442 ? 246.451 229.003 241.375 1.00 29.03  ? 4442 LYS A CE    1 
ATOM   21335 N  NZ    . LYS A 1 4442 ? 246.780 229.778 240.148 1.00 33.00  ? 4442 LYS A NZ    1 
ATOM   21336 N  N     . LYS A 1 4443 ? 244.528 227.117 245.497 1.00 35.42  ? 4443 LYS A N     1 
ATOM   21337 C  CA    . LYS A 1 4443 ? 243.161 226.622 245.541 1.00 28.12  ? 4443 LYS A CA    1 
ATOM   21338 C  C     . LYS A 1 4443 ? 242.569 226.535 244.141 1.00 25.52  ? 4443 LYS A C     1 
ATOM   21339 O  O     . LYS A 1 4443 ? 242.813 227.395 243.291 1.00 29.37  ? 4443 LYS A O     1 
ATOM   21340 C  CB    . LYS A 1 4443 ? 242.298 227.528 246.418 1.00 27.15  ? 4443 LYS A CB    1 
ATOM   21341 C  CG    . LYS A 1 4443 ? 242.647 227.472 247.895 1.00 38.58  ? 4443 LYS A CG    1 
ATOM   21342 C  CD    . LYS A 1 4443 ? 241.806 228.445 248.703 1.00 50.28  ? 4443 LYS A CD    1 
ATOM   21343 C  CE    . LYS A 1 4443 ? 240.358 227.986 248.783 1.00 53.45  ? 4443 LYS A CE    1 
ATOM   21344 N  NZ    . LYS A 1 4443 ? 240.217 226.741 249.589 1.00 38.53  ? 4443 LYS A NZ    1 
ATOM   21345 N  N     . GLN A 1 4444 ? 241.785 225.485 243.910 1.00 22.62  ? 4444 GLN A N     1 
ATOM   21346 C  CA    . GLN A 1 4444 ? 241.143 225.297 242.617 1.00 18.44  ? 4444 GLN A CA    1 
ATOM   21347 C  C     . GLN A 1 4444 ? 240.058 226.340 242.391 1.00 19.05  ? 4444 GLN A C     1 
ATOM   21348 O  O     . GLN A 1 4444 ? 239.331 226.717 243.313 1.00 23.10  ? 4444 GLN A O     1 
ATOM   21349 C  CB    . GLN A 1 4444 ? 240.543 223.896 242.521 1.00 23.83  ? 4444 GLN A CB    1 
ATOM   21350 C  CG    . GLN A 1 4444 ? 241.435 222.883 241.831 1.00 28.64  ? 4444 GLN A CG    1 
ATOM   21351 C  CD    . GLN A 1 4444 ? 240.803 221.508 241.757 1.00 39.85  ? 4444 GLN A CD    1 
ATOM   21352 O  OE1   . GLN A 1 4444 ? 240.037 221.213 240.840 1.00 30.80  ? 4444 GLN A OE1   1 
ATOM   21353 N  NE2   . GLN A 1 4444 ? 241.120 220.657 242.726 1.00 38.75  ? 4444 GLN A NE2   1 
ATOM   21354 N  N     . THR A 1 4445 ? 239.951 226.804 241.151 1.00 16.74  ? 4445 THR A N     1 
ATOM   21355 C  CA    . THR A 1 4445 ? 238.905 227.716 240.717 1.00 11.94  ? 4445 THR A CA    1 
ATOM   21356 C  C     . THR A 1 4445 ? 237.990 226.998 239.730 1.00 12.54  ? 4445 THR A C     1 
ATOM   21357 O  O     . THR A 1 4445 ? 238.201 225.831 239.391 1.00 12.54  ? 4445 THR A O     1 
ATOM   21358 C  CB    . THR A 1 4445 ? 239.511 228.977 240.095 1.00 12.15  ? 4445 THR A CB    1 
ATOM   21359 O  OG1   . THR A 1 4445 ? 240.307 228.618 238.960 1.00 13.77  ? 4445 THR A OG1   1 
ATOM   21360 C  CG2   . THR A 1 4445 ? 240.385 229.699 241.104 1.00 11.24  ? 4445 THR A CG2   1 
ATOM   21361 N  N     . ASN A 1 4446 ? 236.957 227.708 239.271 1.00 13.37  ? 4446 ASN A N     1 
ATOM   21362 C  CA    . ASN A 1 4446 ? 236.046 227.132 238.286 1.00 11.48  ? 4446 ASN A CA    1 
ATOM   21363 C  C     . ASN A 1 4446 ? 236.773 226.824 236.983 1.00 11.80  ? 4446 ASN A C     1 
ATOM   21364 O  O     . ASN A 1 4446 ? 236.652 225.723 236.431 1.00 17.93  ? 4446 ASN A O     1 
ATOM   21365 C  CB    . ASN A 1 4446 ? 234.875 228.083 238.034 1.00 9.29   ? 4446 ASN A CB    1 
ATOM   21366 C  CG    . ASN A 1 4446 ? 233.685 227.790 238.920 1.00 8.36   ? 4446 ASN A CG    1 
ATOM   21367 O  OD1   . ASN A 1 4446 ? 233.271 226.641 239.064 1.00 12.01  ? 4446 ASN A OD1   1 
ATOM   21368 N  ND2   . ASN A 1 4446 ? 233.119 228.834 239.512 1.00 8.11   ? 4446 ASN A ND2   1 
ATOM   21369 N  N     . TYR A 1 4447 ? 237.541 227.793 236.479 1.00 12.29  ? 4447 TYR A N     1 
ATOM   21370 C  CA    . TYR A 1 4447 ? 238.315 227.565 235.264 1.00 16.97  ? 4447 TYR A CA    1 
ATOM   21371 C  C     . TYR A 1 4447 ? 239.343 226.466 235.473 1.00 16.49  ? 4447 TYR A C     1 
ATOM   21372 O  O     . TYR A 1 4447 ? 239.544 225.617 234.596 1.00 18.03  ? 4447 TYR A O     1 
ATOM   21373 C  CB    . TYR A 1 4447 ? 239.000 228.859 234.823 1.00 19.42  ? 4447 TYR A CB    1 
ATOM   21374 C  CG    . TYR A 1 4447 ? 239.971 228.663 233.683 1.00 19.21  ? 4447 TYR A CG    1 
ATOM   21375 C  CD1   . TYR A 1 4447 ? 239.523 228.302 232.421 1.00 20.62  ? 4447 TYR A CD1   1 
ATOM   21376 C  CD2   . TYR A 1 4447 ? 241.336 228.823 233.872 1.00 21.12  ? 4447 TYR A CD2   1 
ATOM   21377 C  CE1   . TYR A 1 4447 ? 240.404 228.116 231.376 1.00 27.40  ? 4447 TYR A CE1   1 
ATOM   21378 C  CE2   . TYR A 1 4447 ? 242.226 228.638 232.833 1.00 27.85  ? 4447 TYR A CE2   1 
ATOM   21379 C  CZ    . TYR A 1 4447 ? 241.753 228.285 231.587 1.00 32.34  ? 4447 TYR A CZ    1 
ATOM   21380 O  OH    . TYR A 1 4447 ? 242.632 228.100 230.546 1.00 32.63  ? 4447 TYR A OH    1 
ATOM   21381 N  N     . LEU A 1 4448 ? 240.009 226.468 236.629 1.00 15.47  ? 4448 LEU A N     1 
ATOM   21382 C  CA    . LEU A 1 4448 ? 240.973 225.417 236.929 1.00 13.99  ? 4448 LEU A CA    1 
ATOM   21383 C  C     . LEU A 1 4448 ? 240.294 224.058 237.013 1.00 16.88  ? 4448 LEU A C     1 
ATOM   21384 O  O     . LEU A 1 4448 ? 240.840 223.057 236.542 1.00 21.86  ? 4448 LEU A O     1 
ATOM   21385 C  CB    . LEU A 1 4448 ? 241.709 225.738 238.228 1.00 13.81  ? 4448 LEU A CB    1 
ATOM   21386 C  CG    . LEU A 1 4448 ? 242.900 226.680 238.067 1.00 14.90  ? 4448 LEU A CG    1 
ATOM   21387 C  CD1   . LEU A 1 4448 ? 243.564 226.955 239.406 1.00 16.63  ? 4448 LEU A CD1   1 
ATOM   21388 C  CD2   . LEU A 1 4448 ? 243.894 226.098 237.079 1.00 18.72  ? 4448 LEU A CD2   1 
ATOM   21389 N  N     . ARG A 1 4449 ? 239.099 224.004 237.606 1.00 18.28  ? 4449 ARG A N     1 
ATOM   21390 C  CA    . ARG A 1 4449 ? 238.367 222.744 237.683 1.00 13.98  ? 4449 ARG A CA    1 
ATOM   21391 C  C     . ARG A 1 4449 ? 238.036 222.219 236.293 1.00 14.87  ? 4449 ARG A C     1 
ATOM   21392 O  O     . ARG A 1 4449 ? 238.246 221.038 235.996 1.00 22.68  ? 4449 ARG A O     1 
ATOM   21393 C  CB    . ARG A 1 4449 ? 237.092 222.932 238.503 1.00 13.37  ? 4449 ARG A CB    1 
ATOM   21394 C  CG    . ARG A 1 4449 ? 237.284 222.770 239.997 1.00 17.27  ? 4449 ARG A CG    1 
ATOM   21395 C  CD    . ARG A 1 4449 ? 235.951 222.743 240.719 1.00 16.71  ? 4449 ARG A CD    1 
ATOM   21396 N  NE    . ARG A 1 4449 ? 235.440 224.089 240.945 1.00 15.32  ? 4449 ARG A NE    1 
ATOM   21397 C  CZ    . ARG A 1 4449 ? 235.873 224.907 241.895 1.00 18.53  ? 4449 ARG A CZ    1 
ATOM   21398 N  NH1   . ARG A 1 4449 ? 236.831 224.548 242.733 1.00 23.59  ? 4449 ARG A NH1   1 
ATOM   21399 N  NH2   . ARG A 1 4449 ? 235.333 226.117 242.004 1.00 12.15  ? 4449 ARG A NH2   1 
ATOM   21400 N  N     . THR A 1 4450 ? 237.519 223.092 235.422 1.00 14.12  ? 4450 THR A N     1 
ATOM   21401 C  CA    . THR A 1 4450 ? 237.177 222.666 234.068 1.00 17.02  ? 4450 THR A CA    1 
ATOM   21402 C  C     . THR A 1 4450 ? 238.413 222.216 233.297 1.00 17.89  ? 4450 THR A C     1 
ATOM   21403 O  O     . THR A 1 4450 ? 238.389 221.181 232.617 1.00 20.30  ? 4450 THR A O     1 
ATOM   21404 C  CB    . THR A 1 4450 ? 236.468 223.801 233.326 1.00 14.72  ? 4450 THR A CB    1 
ATOM   21405 O  OG1   . THR A 1 4450 ? 235.339 224.239 234.090 1.00 16.56  ? 4450 THR A OG1   1 
ATOM   21406 C  CG2   . THR A 1 4450 ? 235.995 223.335 231.960 1.00 14.22  ? 4450 THR A CG2   1 
ATOM   21407 N  N     . LEU A 1 4451 ? 239.505 222.976 233.400 1.00 17.55  ? 4451 LEU A N     1 
ATOM   21408 C  CA    . LEU A 1 4451 ? 240.726 222.632 232.681 1.00 15.88  ? 4451 LEU A CA    1 
ATOM   21409 C  C     . LEU A 1 4451 ? 241.311 221.317 233.181 1.00 18.49  ? 4451 LEU A C     1 
ATOM   21410 O  O     . LEU A 1 4451 ? 241.769 220.493 232.383 1.00 25.96  ? 4451 LEU A O     1 
ATOM   21411 C  CB    . LEU A 1 4451 ? 241.738 223.769 232.817 1.00 15.88  ? 4451 LEU A CB    1 
ATOM   21412 C  CG    . LEU A 1 4451 ? 243.194 223.504 232.437 1.00 16.47  ? 4451 LEU A CG    1 
ATOM   21413 C  CD1   . LEU A 1 4451 ? 243.351 223.442 230.932 1.00 17.47  ? 4451 LEU A CD1   1 
ATOM   21414 C  CD2   . LEU A 1 4451 ? 244.077 224.589 233.017 1.00 20.86  ? 4451 LEU A CD2   1 
ATOM   21415 N  N     . ILE A 1 4452 ? 241.296 221.098 234.497 1.00 15.44  ? 4452 ILE A N     1 
ATOM   21416 C  CA    . ILE A 1 4452 ? 241.821 219.859 235.056 1.00 20.85  ? 4452 ILE A CA    1 
ATOM   21417 C  C     . ILE A 1 4452 ? 240.954 218.676 234.647 1.00 20.00  ? 4452 ILE A C     1 
ATOM   21418 O  O     . ILE A 1 4452 ? 241.468 217.598 234.326 1.00 24.92  ? 4452 ILE A O     1 
ATOM   21419 C  CB    . ILE A 1 4452 ? 241.942 219.980 236.586 1.00 25.63  ? 4452 ILE A CB    1 
ATOM   21420 C  CG1   . ILE A 1 4452 ? 243.165 220.818 236.952 1.00 20.00  ? 4452 ILE A CG1   1 
ATOM   21421 C  CG2   . ILE A 1 4452 ? 242.028 218.609 237.235 1.00 20.73  ? 4452 ILE A CG2   1 
ATOM   21422 C  CD1   . ILE A 1 4452 ? 243.156 221.307 238.374 1.00 17.85  ? 4452 ILE A CD1   1 
ATOM   21423 N  N     . ASN A 1 4453 ? 239.630 218.852 234.650 1.00 19.23  ? 4453 ASN A N     1 
ATOM   21424 C  CA    . ASN A 1 4453 ? 238.749 217.779 234.199 1.00 22.31  ? 4453 ASN A CA    1 
ATOM   21425 C  C     . ASN A 1 4453 ? 239.020 217.429 232.742 1.00 25.29  ? 4453 ASN A C     1 
ATOM   21426 O  O     . ASN A 1 4453 ? 239.101 216.247 232.384 1.00 28.37  ? 4453 ASN A O     1 
ATOM   21427 C  CB    . ASN A 1 4453 ? 237.288 218.182 234.391 1.00 21.94  ? 4453 ASN A CB    1 
ATOM   21428 C  CG    . ASN A 1 4453 ? 236.781 217.883 235.787 1.00 37.17  ? 4453 ASN A CG    1 
ATOM   21429 O  OD1   . ASN A 1 4453 ? 237.220 216.928 236.429 1.00 39.31  ? 4453 ASN A OD1   1 
ATOM   21430 N  ND2   . ASN A 1 4453 ? 235.848 218.697 236.265 1.00 39.04  ? 4453 ASN A ND2   1 
ATOM   21431 N  N     . GLU A 1 4454 ? 239.176 218.446 231.890 1.00 23.99  ? 4454 GLU A N     1 
ATOM   21432 C  CA    . GLU A 1 4454 ? 239.465 218.194 230.483 1.00 22.67  ? 4454 GLU A CA    1 
ATOM   21433 C  C     . GLU A 1 4454 ? 240.807 217.492 230.307 1.00 23.65  ? 4454 GLU A C     1 
ATOM   21434 O  O     . GLU A 1 4454 ? 240.925 216.554 229.510 1.00 30.05  ? 4454 GLU A O     1 
ATOM   21435 C  CB    . GLU A 1 4454 ? 239.438 219.509 229.703 1.00 25.51  ? 4454 GLU A CB    1 
ATOM   21436 C  CG    . GLU A 1 4454 ? 238.033 220.037 229.435 1.00 31.55  ? 4454 GLU A CG    1 
ATOM   21437 C  CD    . GLU A 1 4454 ? 238.018 221.203 228.465 1.00 37.98  ? 4454 GLU A CD    1 
ATOM   21438 O  OE1   . GLU A 1 4454 ? 237.628 221.003 227.296 1.00 43.54  ? 4454 GLU A OE1   1 
ATOM   21439 O  OE2   . GLU A 1 4454 ? 238.394 222.322 228.874 1.00 38.40  ? 4454 GLU A OE2   1 
ATOM   21440 N  N     . LEU A 1 4455 ? 241.830 217.931 231.044 1.00 23.38  ? 4455 LEU A N     1 
ATOM   21441 C  CA    . LEU A 1 4455 ? 243.150 217.321 230.922 1.00 20.40  ? 4455 LEU A CA    1 
ATOM   21442 C  C     . LEU A 1 4455 ? 243.145 215.871 231.393 1.00 23.77  ? 4455 LEU A C     1 
ATOM   21443 O  O     . LEU A 1 4455 ? 243.746 215.003 230.749 1.00 28.61  ? 4455 LEU A O     1 
ATOM   21444 C  CB    . LEU A 1 4455 ? 244.177 218.134 231.711 1.00 20.84  ? 4455 LEU A CB    1 
ATOM   21445 C  CG    . LEU A 1 4455 ? 244.626 219.455 231.087 1.00 22.45  ? 4455 LEU A CG    1 
ATOM   21446 C  CD1   . LEU A 1 4455 ? 245.859 219.985 231.795 1.00 27.37  ? 4455 LEU A CD1   1 
ATOM   21447 C  CD2   . LEU A 1 4455 ? 244.893 219.282 229.602 1.00 28.08  ? 4455 LEU A CD2   1 
ATOM   21448 N  N     . VAL A 1 4456 ? 242.482 215.592 232.516 1.00 27.09  ? 4456 VAL A N     1 
ATOM   21449 C  CA    . VAL A 1 4456 ? 242.435 214.228 233.032 1.00 26.64  ? 4456 VAL A CA    1 
ATOM   21450 C  C     . VAL A 1 4456 ? 241.653 213.326 232.088 1.00 28.27  ? 4456 VAL A C     1 
ATOM   21451 O  O     . VAL A 1 4456 ? 242.075 212.203 231.790 1.00 29.19  ? 4456 VAL A O     1 
ATOM   21452 C  CB    . VAL A 1 4456 ? 241.842 214.220 234.453 1.00 23.30  ? 4456 VAL A CB    1 
ATOM   21453 C  CG1   . VAL A 1 4456 ? 241.375 212.824 234.832 1.00 25.45  ? 4456 VAL A CG1   1 
ATOM   21454 C  CG2   . VAL A 1 4456 ? 242.865 214.730 235.453 1.00 27.87  ? 4456 VAL A CG2   1 
ATOM   21455 N  N     . LYS A 1 4457 ? 240.510 213.802 231.591 1.00 27.04  ? 4457 LYS A N     1 
ATOM   21456 C  CA    . LYS A 1 4457 ? 239.711 212.998 230.677 1.00 28.34  ? 4457 LYS A CA    1 
ATOM   21457 C  C     . LYS A 1 4457 ? 240.298 212.936 229.273 1.00 29.70  ? 4457 LYS A C     1 
ATOM   21458 O  O     . LYS A 1 4457 ? 239.807 212.156 228.451 1.00 37.24  ? 4457 LYS A O     1 
ATOM   21459 C  CB    . LYS A 1 4457 ? 238.281 213.537 230.626 1.00 27.50  ? 4457 LYS A CB    1 
ATOM   21460 C  CG    . LYS A 1 4457 ? 237.511 213.372 231.925 1.00 27.66  ? 4457 LYS A CG    1 
ATOM   21461 C  CD    . LYS A 1 4457 ? 236.072 212.958 231.666 1.00 29.72  ? 4457 LYS A CD    1 
ATOM   21462 C  CE    . LYS A 1 4457 ? 235.445 213.791 230.561 1.00 26.96  ? 4457 LYS A CE    1 
ATOM   21463 N  NZ    . LYS A 1 4457 ? 233.958 213.772 230.625 1.00 29.30  ? 4457 LYS A NZ    1 
ATOM   21464 N  N     . GLY A 1 4458 ? 241.326 213.729 228.980 1.00 27.40  ? 4458 GLY A N     1 
ATOM   21465 C  CA    . GLY A 1 4458 ? 242.011 213.659 227.707 1.00 24.56  ? 4458 GLY A CA    1 
ATOM   21466 C  C     . GLY A 1 4458 ? 241.464 214.540 226.606 1.00 26.37  ? 4458 GLY A C     1 
ATOM   21467 O  O     . GLY A 1 4458 ? 241.974 214.477 225.482 1.00 28.85  ? 4458 GLY A O     1 
ATOM   21468 N  N     . ILE A 1 4459 ? 240.450 215.351 226.883 1.00 23.51  ? 4459 ILE A N     1 
ATOM   21469 C  CA    . ILE A 1 4459 ? 239.881 216.251 225.885 1.00 27.66  ? 4459 ILE A CA    1 
ATOM   21470 C  C     . ILE A 1 4459 ? 240.704 217.531 225.840 1.00 29.12  ? 4459 ILE A C     1 
ATOM   21471 O  O     . ILE A 1 4459 ? 241.060 218.091 226.883 1.00 32.59  ? 4459 ILE A O     1 
ATOM   21472 C  CB    . ILE A 1 4459 ? 238.401 216.553 226.184 1.00 25.82  ? 4459 ILE A CB    1 
ATOM   21473 C  CG1   . ILE A 1 4459 ? 237.548 215.284 226.081 1.00 25.53  ? 4459 ILE A CG1   1 
ATOM   21474 C  CG2   . ILE A 1 4459 ? 237.869 217.632 225.252 1.00 27.11  ? 4459 ILE A CG2   1 
ATOM   21475 C  CD1   . ILE A 1 4459 ? 237.423 214.505 227.361 1.00 29.44  ? 4459 ILE A CD1   1 
ATOM   21476 N  N     . LEU A 1 4460 ? 241.020 217.981 224.631 1.00 22.56  ? 4460 LEU A N     1 
ATOM   21477 C  CA    . LEU A 1 4460 ? 241.738 219.236 224.458 1.00 23.39  ? 4460 LEU A CA    1 
ATOM   21478 C  C     . LEU A 1 4460 ? 240.886 220.393 224.971 1.00 29.88  ? 4460 LEU A C     1 
ATOM   21479 O  O     . LEU A 1 4460 ? 239.710 220.502 224.597 1.00 35.61  ? 4460 LEU A O     1 
ATOM   21480 C  CB    . LEU A 1 4460 ? 242.088 219.443 222.987 1.00 27.19  ? 4460 LEU A CB    1 
ATOM   21481 C  CG    . LEU A 1 4460 ? 242.492 220.845 222.528 1.00 26.67  ? 4460 LEU A CG    1 
ATOM   21482 C  CD1   . LEU A 1 4460 ? 243.862 221.219 223.062 1.00 23.48  ? 4460 LEU A CD1   1 
ATOM   21483 C  CD2   . LEU A 1 4460 ? 242.463 220.924 221.013 1.00 23.59  ? 4460 LEU A CD2   1 
ATOM   21484 N  N     . PRO A 1 4461 ? 241.424 221.259 225.828 1.00 27.97  ? 4461 PRO A N     1 
ATOM   21485 C  CA    . PRO A 1 4461 ? 240.629 222.379 226.343 1.00 25.89  ? 4461 PRO A CA    1 
ATOM   21486 C  C     . PRO A 1 4461 ? 240.153 223.289 225.221 1.00 28.77  ? 4461 PRO A C     1 
ATOM   21487 O  O     . PRO A 1 4461 ? 240.876 223.549 224.257 1.00 34.17  ? 4461 PRO A O     1 
ATOM   21488 C  CB    . PRO A 1 4461 ? 241.601 223.104 227.280 1.00 24.02  ? 4461 PRO A CB    1 
ATOM   21489 C  CG    . PRO A 1 4461 ? 242.601 222.073 227.656 1.00 25.48  ? 4461 PRO A CG    1 
ATOM   21490 C  CD    . PRO A 1 4461 ? 242.756 221.197 226.453 1.00 30.73  ? 4461 PRO A CD    1 
ATOM   21491 N  N     . ARG A 1 4462 ? 238.919 223.775 225.357 1.00 30.07  ? 4462 ARG A N     1 
ATOM   21492 C  CA    . ARG A 1 4462 ? 238.372 224.689 224.363 1.00 36.16  ? 4462 ARG A CA    1 
ATOM   21493 C  C     . ARG A 1 4462 ? 239.045 226.053 224.408 1.00 36.05  ? 4462 ARG A C     1 
ATOM   21494 O  O     . ARG A 1 4462 ? 238.989 226.792 223.420 1.00 39.33  ? 4462 ARG A O     1 
ATOM   21495 C  CB    . ARG A 1 4462 ? 236.863 224.841 224.558 1.00 33.13  ? 4462 ARG A CB    1 
ATOM   21496 C  CG    . ARG A 1 4462 ? 236.103 223.526 224.531 1.00 35.29  ? 4462 ARG A CG    1 
ATOM   21497 C  CD    . ARG A 1 4462 ? 236.114 222.915 223.140 1.00 46.81  ? 4462 ARG A CD    1 
ATOM   21498 N  NE    . ARG A 1 4462 ? 237.104 221.850 223.024 1.00 56.54  ? 4462 ARG A NE    1 
ATOM   21499 C  CZ    . ARG A 1 4462 ? 237.883 221.661 221.968 1.00 43.50  ? 4462 ARG A CZ    1 
ATOM   21500 N  NH1   . ARG A 1 4462 ? 237.817 222.453 220.910 1.00 40.22  ? 4462 ARG A NH1   1 
ATOM   21501 N  NH2   . ARG A 1 4462 ? 238.752 220.653 221.973 1.00 30.14  ? 4462 ARG A NH2   1 
ATOM   21502 N  N     . SER A 1 4463 ? 239.681 226.399 225.527 1.00 28.80  ? 4463 SER A N     1 
ATOM   21503 C  CA    . SER A 1 4463 ? 240.380 227.669 225.657 1.00 22.58  ? 4463 SER A CA    1 
ATOM   21504 C  C     . SER A 1 4463 ? 241.778 227.641 225.056 1.00 25.49  ? 4463 SER A C     1 
ATOM   21505 O  O     . SER A 1 4463 ? 242.407 228.699 224.948 1.00 27.50  ? 4463 SER A O     1 
ATOM   21506 C  CB    . SER A 1 4463 ? 240.461 228.070 227.130 1.00 30.23  ? 4463 SER A CB    1 
ATOM   21507 O  OG    . SER A 1 4463 ? 241.271 227.165 227.860 1.00 35.03  ? 4463 SER A OG    1 
ATOM   21508 N  N     . TRP A 1 4464 ? 242.279 226.469 224.665 1.00 24.69  ? 4464 TRP A N     1 
ATOM   21509 C  CA    . TRP A 1 4464 ? 243.587 226.352 224.034 1.00 20.25  ? 4464 TRP A CA    1 
ATOM   21510 C  C     . TRP A 1 4464 ? 243.514 226.241 222.519 1.00 25.17  ? 4464 TRP A C     1 
ATOM   21511 O  O     . TRP A 1 4464 ? 244.459 226.646 221.835 1.00 28.22  ? 4464 TRP A O     1 
ATOM   21512 C  CB    . TRP A 1 4464 ? 244.335 225.130 224.579 1.00 24.10  ? 4464 TRP A CB    1 
ATOM   21513 C  CG    . TRP A 1 4464 ? 244.829 225.282 225.981 1.00 23.08  ? 4464 TRP A CG    1 
ATOM   21514 C  CD1   . TRP A 1 4464 ? 244.641 226.349 226.807 1.00 25.97  ? 4464 TRP A CD1   1 
ATOM   21515 C  CD2   . TRP A 1 4464 ? 245.600 224.330 226.723 1.00 20.03  ? 4464 TRP A CD2   1 
ATOM   21516 N  NE1   . TRP A 1 4464 ? 245.246 226.121 228.018 1.00 22.61  ? 4464 TRP A NE1   1 
ATOM   21517 C  CE2   . TRP A 1 4464 ? 245.842 224.888 227.991 1.00 23.05  ? 4464 TRP A CE2   1 
ATOM   21518 C  CE3   . TRP A 1 4464 ? 246.108 223.060 226.437 1.00 21.58  ? 4464 TRP A CE3   1 
ATOM   21519 C  CZ2   . TRP A 1 4464 ? 246.570 224.221 228.974 1.00 21.29  ? 4464 TRP A CZ2   1 
ATOM   21520 C  CZ3   . TRP A 1 4464 ? 246.830 222.400 227.412 1.00 20.75  ? 4464 TRP A CZ3   1 
ATOM   21521 C  CH2   . TRP A 1 4464 ? 247.054 222.981 228.665 1.00 17.32  ? 4464 TRP A CH2   1 
ATOM   21522 N  N     . SER A 1 4465 ? 242.420 225.703 221.980 1.00 28.64  ? 4465 SER A N     1 
ATOM   21523 C  CA    . SER A 1 4465 ? 242.298 225.455 220.545 1.00 28.15  ? 4465 SER A CA    1 
ATOM   21524 C  C     . SER A 1 4465 ? 241.893 226.751 219.848 1.00 23.71  ? 4465 SER A C     1 
ATOM   21525 O  O     . SER A 1 4465 ? 240.727 226.992 219.526 1.00 27.12  ? 4465 SER A O     1 
ATOM   21526 C  CB    . SER A 1 4465 ? 241.295 224.339 220.278 1.00 36.40  ? 4465 SER A CB    1 
ATOM   21527 O  OG    . SER A 1 4465 ? 239.976 224.848 220.190 1.00 41.99  ? 4465 SER A OG    1 
ATOM   21528 N  N     . HIS A 1 4466 ? 242.889 227.601 219.610 1.00 22.24  ? 4466 HIS A N     1 
ATOM   21529 C  CA    . HIS A 1 4466 ? 242.686 228.852 218.896 1.00 22.10  ? 4466 HIS A CA    1 
ATOM   21530 C  C     . HIS A 1 4466 ? 243.114 228.782 217.437 1.00 25.06  ? 4466 HIS A C     1 
ATOM   21531 O  O     . HIS A 1 4466 ? 243.050 229.798 216.738 1.00 33.34  ? 4466 HIS A O     1 
ATOM   21532 C  CB    . HIS A 1 4466 ? 243.424 229.991 219.605 1.00 19.56  ? 4466 HIS A CB    1 
ATOM   21533 C  CG    . HIS A 1 4466 ? 242.886 230.293 220.969 1.00 23.05  ? 4466 HIS A CG    1 
ATOM   21534 N  ND1   . HIS A 1 4466 ? 241.702 230.967 221.169 1.00 32.83  ? 4466 HIS A ND1   1 
ATOM   21535 C  CD2   . HIS A 1 4466 ? 243.368 230.009 222.202 1.00 24.79  ? 4466 HIS A CD2   1 
ATOM   21536 C  CE1   . HIS A 1 4466 ? 241.478 231.087 222.465 1.00 31.39  ? 4466 HIS A CE1   1 
ATOM   21537 N  NE2   . HIS A 1 4466 ? 242.475 230.514 223.114 1.00 30.36  ? 4466 HIS A NE2   1 
ATOM   21538 N  N     . TYR A 1 4467 ? 243.548 227.618 216.960 1.00 22.84  ? 4467 TYR A N     1 
ATOM   21539 C  CA    . TYR A 1 4467 ? 243.789 227.405 215.542 1.00 16.82  ? 4467 TYR A CA    1 
ATOM   21540 C  C     . TYR A 1 4467 ? 243.057 226.144 215.112 1.00 17.91  ? 4467 TYR A C     1 
ATOM   21541 O  O     . TYR A 1 4467 ? 242.614 225.347 215.942 1.00 18.69  ? 4467 TYR A O     1 
ATOM   21542 C  CB    . TYR A 1 4467 ? 245.287 227.310 215.214 1.00 18.24  ? 4467 TYR A CB    1 
ATOM   21543 C  CG    . TYR A 1 4467 ? 246.072 226.316 216.041 1.00 19.13  ? 4467 TYR A CG    1 
ATOM   21544 C  CD1   . TYR A 1 4467 ? 246.669 226.695 217.234 1.00 17.21  ? 4467 TYR A CD1   1 
ATOM   21545 C  CD2   . TYR A 1 4467 ? 246.239 225.007 215.613 1.00 18.77  ? 4467 TYR A CD2   1 
ATOM   21546 C  CE1   . TYR A 1 4467 ? 247.397 225.795 217.986 1.00 17.38  ? 4467 TYR A CE1   1 
ATOM   21547 C  CE2   . TYR A 1 4467 ? 246.963 224.101 216.358 1.00 18.19  ? 4467 TYR A CE2   1 
ATOM   21548 C  CZ    . TYR A 1 4467 ? 247.541 224.499 217.543 1.00 21.02  ? 4467 TYR A CZ    1 
ATOM   21549 O  OH    . TYR A 1 4467 ? 248.265 223.596 218.287 1.00 22.52  ? 4467 TYR A OH    1 
ATOM   21550 N  N     . THR A 1 4468 ? 242.916 225.980 213.798 1.00 17.82  ? 4468 THR A N     1 
ATOM   21551 C  CA    . THR A 1 4468 ? 242.135 224.871 213.267 1.00 17.66  ? 4468 THR A CA    1 
ATOM   21552 C  C     . THR A 1 4468 ? 242.794 223.539 213.599 1.00 22.00  ? 4468 THR A C     1 
ATOM   21553 O  O     . THR A 1 4468 ? 243.992 223.346 213.372 1.00 25.58  ? 4468 THR A O     1 
ATOM   21554 C  CB    . THR A 1 4468 ? 241.969 225.013 211.756 1.00 15.06  ? 4468 THR A CB    1 
ATOM   21555 O  OG1   . THR A 1 4468 ? 241.371 226.279 211.456 1.00 18.66  ? 4468 THR A OG1   1 
ATOM   21556 C  CG2   . THR A 1 4468 ? 241.082 223.906 211.224 1.00 15.95  ? 4468 THR A CG2   1 
ATOM   21557 N  N     . VAL A 1 4469 ? 241.999 222.618 214.136 1.00 20.15  ? 4469 VAL A N     1 
ATOM   21558 C  CA    . VAL A 1 4469 ? 242.481 221.329 214.622 1.00 15.82  ? 4469 VAL A CA    1 
ATOM   21559 C  C     . VAL A 1 4469 ? 241.546 220.235 214.119 1.00 20.18  ? 4469 VAL A C     1 
ATOM   21560 O  O     . VAL A 1 4469 ? 240.331 220.458 214.028 1.00 24.12  ? 4469 VAL A O     1 
ATOM   21561 C  CB    . VAL A 1 4469 ? 242.572 221.326 216.160 1.00 19.81  ? 4469 VAL A CB    1 
ATOM   21562 C  CG1   . VAL A 1 4469 ? 242.965 219.965 216.683 1.00 21.02  ? 4469 VAL A CG1   1 
ATOM   21563 C  CG2   . VAL A 1 4469 ? 243.572 222.369 216.639 1.00 30.01  ? 4469 VAL A CG2   1 
ATOM   21564 N  N     . PRO A 1 4470 ? 242.058 219.053 213.767 1.00 20.76  ? 4470 PRO A N     1 
ATOM   21565 C  CA    . PRO A 1 4470 ? 241.166 217.918 213.509 1.00 16.39  ? 4470 PRO A CA    1 
ATOM   21566 C  C     . PRO A 1 4470 ? 240.324 217.601 214.735 1.00 22.70  ? 4470 PRO A C     1 
ATOM   21567 O  O     . PRO A 1 4470 ? 240.763 217.757 215.878 1.00 27.70  ? 4470 PRO A O     1 
ATOM   21568 C  CB    . PRO A 1 4470 ? 242.132 216.774 213.180 1.00 17.09  ? 4470 PRO A CB    1 
ATOM   21569 C  CG    . PRO A 1 4470 ? 243.354 217.447 212.682 1.00 17.33  ? 4470 PRO A CG    1 
ATOM   21570 C  CD    . PRO A 1 4470 ? 243.454 218.757 213.406 1.00 18.58  ? 4470 PRO A CD    1 
ATOM   21571 N  N     . ALA A 1 4471 ? 239.095 217.147 214.482 1.00 19.07  ? 4471 ALA A N     1 
ATOM   21572 C  CA    . ALA A 1 4471 ? 238.113 217.003 215.553 1.00 26.16  ? 4471 ALA A CA    1 
ATOM   21573 C  C     . ALA A 1 4471 ? 238.571 216.008 216.613 1.00 25.69  ? 4471 ALA A C     1 
ATOM   21574 O  O     . ALA A 1 4471 ? 238.378 216.237 217.813 1.00 25.47  ? 4471 ALA A O     1 
ATOM   21575 C  CB    . ALA A 1 4471 ? 236.764 216.583 214.972 1.00 29.13  ? 4471 ALA A CB    1 
ATOM   21576 N  N     . GLY A 1 4472 ? 239.172 214.900 216.195 1.00 20.94  ? 4472 GLY A N     1 
ATOM   21577 C  CA    . GLY A 1 4472 ? 239.521 213.833 217.106 1.00 27.68  ? 4472 GLY A CA    1 
ATOM   21578 C  C     . GLY A 1 4472 ? 240.887 213.917 217.750 1.00 32.45  ? 4472 GLY A C     1 
ATOM   21579 O  O     . GLY A 1 4472 ? 241.298 212.956 218.406 1.00 33.04  ? 4472 GLY A O     1 
ATOM   21580 N  N     . MET A 1 4473 ? 241.607 215.024 217.587 1.00 30.92  ? 4473 MET A N     1 
ATOM   21581 C  CA    . MET A 1 4473 ? 242.954 215.116 218.133 1.00 30.58  ? 4473 MET A CA    1 
ATOM   21582 C  C     . MET A 1 4473 ? 242.908 215.224 219.653 1.00 28.95  ? 4473 MET A C     1 
ATOM   21583 O  O     . MET A 1 4473 ? 242.136 216.010 220.210 1.00 23.92  ? 4473 MET A O     1 
ATOM   21584 C  CB    . MET A 1 4473 ? 243.697 216.309 217.531 1.00 28.21  ? 4473 MET A CB    1 
ATOM   21585 C  CG    . MET A 1 4473 ? 244.905 216.751 218.341 1.00 25.08  ? 4473 MET A CG    1 
ATOM   21586 S  SD    . MET A 1 4473 ? 245.783 218.158 217.639 1.00 35.07  ? 4473 MET A SD    1 
ATOM   21587 C  CE    . MET A 1 4473 ? 245.794 217.726 215.905 1.00 22.87  ? 4473 MET A CE    1 
ATOM   21588 N  N     . THR A 1 4474 ? 243.740 214.429 220.322 1.00 29.20  ? 4474 THR A N     1 
ATOM   21589 C  CA    . THR A 1 4474 ? 243.795 214.398 221.774 1.00 25.29  ? 4474 THR A CA    1 
ATOM   21590 C  C     . THR A 1 4474 ? 244.781 215.444 222.289 1.00 24.45  ? 4474 THR A C     1 
ATOM   21591 O  O     . THR A 1 4474 ? 245.378 216.207 221.527 1.00 29.63  ? 4474 THR A O     1 
ATOM   21592 C  CB    . THR A 1 4474 ? 244.170 213.001 222.264 1.00 25.56  ? 4474 THR A CB    1 
ATOM   21593 O  OG1   . THR A 1 4474 ? 245.517 212.702 221.880 1.00 28.82  ? 4474 THR A OG1   1 
ATOM   21594 C  CG2   . THR A 1 4474 ? 243.236 211.962 221.667 1.00 23.35  ? 4474 THR A CG2   1 
ATOM   21595 N  N     . VAL A 1 4475 ? 244.954 215.479 223.612 1.00 24.01  ? 4475 VAL A N     1 
ATOM   21596 C  CA    . VAL A 1 4475 ? 245.776 216.518 224.224 1.00 21.88  ? 4475 VAL A CA    1 
ATOM   21597 C  C     . VAL A 1 4475 ? 247.255 216.285 223.932 1.00 19.64  ? 4475 VAL A C     1 
ATOM   21598 O  O     . VAL A 1 4475 ? 248.014 217.237 223.724 1.00 24.01  ? 4475 VAL A O     1 
ATOM   21599 C  CB    . VAL A 1 4475 ? 245.503 216.595 225.737 1.00 25.47  ? 4475 VAL A CB    1 
ATOM   21600 C  CG1   . VAL A 1 4475 ? 246.423 217.603 226.384 1.00 28.06  ? 4475 VAL A CG1   1 
ATOM   21601 C  CG2   . VAL A 1 4475 ? 244.059 216.952 225.997 1.00 26.74  ? 4475 VAL A CG2   1 
ATOM   21602 N  N     . ILE A 1 4476 ? 247.693 215.024 223.926 1.00 20.56  ? 4476 ILE A N     1 
ATOM   21603 C  CA    . ILE A 1 4476 ? 249.095 214.720 223.642 1.00 21.93  ? 4476 ILE A CA    1 
ATOM   21604 C  C     . ILE A 1 4476 ? 249.468 215.181 222.238 1.00 18.34  ? 4476 ILE A C     1 
ATOM   21605 O  O     . ILE A 1 4476 ? 250.502 215.833 222.027 1.00 18.07  ? 4476 ILE A O     1 
ATOM   21606 C  CB    . ILE A 1 4476 ? 249.362 213.215 223.824 1.00 23.51  ? 4476 ILE A CB    1 
ATOM   21607 C  CG1   . ILE A 1 4476 ? 249.038 212.772 225.251 1.00 19.80  ? 4476 ILE A CG1   1 
ATOM   21608 C  CG2   . ILE A 1 4476 ? 250.807 212.882 223.485 1.00 23.13  ? 4476 ILE A CG2   1 
ATOM   21609 C  CD1   . ILE A 1 4476 ? 249.870 213.455 226.301 1.00 25.34  ? 4476 ILE A CD1   1 
ATOM   21610 N  N     . GLN A 1 4477 ? 248.624 214.850 221.258 1.00 18.11  ? 4477 GLN A N     1 
ATOM   21611 C  CA    . GLN A 1 4477 ? 248.882 215.260 219.883 1.00 20.86  ? 4477 GLN A CA    1 
ATOM   21612 C  C     . GLN A 1 4477 ? 248.878 216.775 219.752 1.00 23.82  ? 4477 GLN A C     1 
ATOM   21613 O  O     . GLN A 1 4477 ? 249.720 217.348 219.050 1.00 24.95  ? 4477 GLN A O     1 
ATOM   21614 C  CB    . GLN A 1 4477 ? 247.844 214.638 218.950 1.00 18.90  ? 4477 GLN A CB    1 
ATOM   21615 C  CG    . GLN A 1 4477 ? 247.634 213.150 219.164 1.00 19.47  ? 4477 GLN A CG    1 
ATOM   21616 C  CD    . GLN A 1 4477 ? 246.537 212.585 218.286 1.00 23.12  ? 4477 GLN A CD    1 
ATOM   21617 O  OE1   . GLN A 1 4477 ? 245.388 213.019 218.353 1.00 20.87  ? 4477 GLN A OE1   1 
ATOM   21618 N  NE2   . GLN A 1 4477 ? 246.886 211.612 217.454 1.00 27.59  ? 4477 GLN A NE2   1 
ATOM   21619 N  N     . TRP A 1 4478 ? 247.935 217.443 220.423 1.00 19.13  ? 4478 TRP A N     1 
ATOM   21620 C  CA    . TRP A 1 4478 ? 247.880 218.897 220.350 1.00 13.40  ? 4478 TRP A CA    1 
ATOM   21621 C  C     . TRP A 1 4478 ? 249.114 219.528 220.974 1.00 16.38  ? 4478 TRP A C     1 
ATOM   21622 O  O     . TRP A 1 4478 ? 249.631 220.523 220.463 1.00 20.25  ? 4478 TRP A O     1 
ATOM   21623 C  CB    . TRP A 1 4478 ? 246.617 219.425 221.027 1.00 14.28  ? 4478 TRP A CB    1 
ATOM   21624 C  CG    . TRP A 1 4478 ? 246.423 220.897 220.808 1.00 16.83  ? 4478 TRP A CG    1 
ATOM   21625 C  CD1   . TRP A 1 4478 ? 245.683 221.487 219.826 1.00 12.21  ? 4478 TRP A CD1   1 
ATOM   21626 C  CD2   . TRP A 1 4478 ? 246.993 221.967 221.575 1.00 17.24  ? 4478 TRP A CD2   1 
ATOM   21627 N  NE1   . TRP A 1 4478 ? 245.748 222.852 219.938 1.00 17.49  ? 4478 TRP A NE1   1 
ATOM   21628 C  CE2   . TRP A 1 4478 ? 246.547 223.173 221.003 1.00 19.06  ? 4478 TRP A CE2   1 
ATOM   21629 C  CE3   . TRP A 1 4478 ? 247.833 222.020 222.692 1.00 13.00  ? 4478 TRP A CE3   1 
ATOM   21630 C  CZ2   . TRP A 1 4478 ? 246.912 224.419 221.509 1.00 14.85  ? 4478 TRP A CZ2   1 
ATOM   21631 C  CZ3   . TRP A 1 4478 ? 248.195 223.256 223.191 1.00 16.32  ? 4478 TRP A CZ3   1 
ATOM   21632 C  CH2   . TRP A 1 4478 ? 247.735 224.439 222.601 1.00 18.99  ? 4478 TRP A CH2   1 
ATOM   21633 N  N     . VAL A 1 4479 ? 249.592 218.975 222.088 1.00 15.26  ? 4479 VAL A N     1 
ATOM   21634 C  CA    . VAL A 1 4479 ? 250.780 219.522 222.734 1.00 17.00  ? 4479 VAL A CA    1 
ATOM   21635 C  C     . VAL A 1 4479 ? 252.000 219.347 221.839 1.00 18.47  ? 4479 VAL A C     1 
ATOM   21636 O  O     . VAL A 1 4479 ? 252.820 220.264 221.702 1.00 23.06  ? 4479 VAL A O     1 
ATOM   21637 C  CB    . VAL A 1 4479 ? 250.983 218.879 224.117 1.00 16.24  ? 4479 VAL A CB    1 
ATOM   21638 C  CG1   . VAL A 1 4479 ? 252.405 219.101 224.607 1.00 19.73  ? 4479 VAL A CG1   1 
ATOM   21639 C  CG2   . VAL A 1 4479 ? 249.984 219.443 225.110 1.00 15.63  ? 4479 VAL A CG2   1 
ATOM   21640 N  N     . SER A 1 4480 ? 252.140 218.177 221.211 1.00 16.12  ? 4480 SER A N     1 
ATOM   21641 C  CA    . SER A 1 4480 ? 253.262 217.974 220.295 1.00 15.92  ? 4480 SER A CA    1 
ATOM   21642 C  C     . SER A 1 4480 ? 253.190 218.930 219.108 1.00 18.78  ? 4480 SER A C     1 
ATOM   21643 O  O     . SER A 1 4480 ? 254.200 219.536 218.720 1.00 20.91  ? 4480 SER A O     1 
ATOM   21644 C  CB    . SER A 1 4480 ? 253.296 216.523 219.817 1.00 18.39  ? 4480 SER A CB    1 
ATOM   21645 O  OG    . SER A 1 4480 ? 253.484 215.632 220.902 1.00 25.07  ? 4480 SER A OG    1 
ATOM   21646 N  N     . ASP A 1 4481 ? 251.999 219.085 218.522 1.00 17.54  ? 4481 ASP A N     1 
ATOM   21647 C  CA    . ASP A 1 4481 ? 251.832 220.001 217.398 1.00 17.92  ? 4481 ASP A CA    1 
ATOM   21648 C  C     . ASP A 1 4481 ? 252.119 221.439 217.811 1.00 20.79  ? 4481 ASP A C     1 
ATOM   21649 O  O     . ASP A 1 4481 ? 252.741 222.198 217.058 1.00 22.19  ? 4481 ASP A O     1 
ATOM   21650 C  CB    . ASP A 1 4481 ? 250.418 219.876 216.833 1.00 19.94  ? 4481 ASP A CB    1 
ATOM   21651 C  CG    . ASP A 1 4481 ? 250.361 220.123 215.341 1.00 32.10  ? 4481 ASP A CG    1 
ATOM   21652 O  OD1   . ASP A 1 4481 ? 249.245 220.293 214.810 1.00 29.00  ? 4481 ASP A OD1   1 
ATOM   21653 O  OD2   . ASP A 1 4481 ? 251.432 220.146 214.700 1.00 42.47  ? 4481 ASP A OD2   1 
ATOM   21654 N  N     . PHE A 1 4482 ? 251.663 221.832 219.000 1.00 17.92  ? 4482 PHE A N     1 
ATOM   21655 C  CA    . PHE A 1 4482 ? 251.900 223.180 219.496 1.00 15.06  ? 4482 PHE A CA    1 
ATOM   21656 C  C     . PHE A 1 4482 ? 253.383 223.425 219.727 1.00 18.27  ? 4482 PHE A C     1 
ATOM   21657 O  O     . PHE A 1 4482 ? 253.888 224.512 219.433 1.00 21.63  ? 4482 PHE A O     1 
ATOM   21658 C  CB    . PHE A 1 4482 ? 251.105 223.402 220.783 1.00 16.87  ? 4482 PHE A CB    1 
ATOM   21659 C  CG    . PHE A 1 4482 ? 251.163 224.807 221.301 1.00 15.95  ? 4482 PHE A CG    1 
ATOM   21660 C  CD1   . PHE A 1 4482 ? 250.583 225.844 220.591 1.00 16.15  ? 4482 PHE A CD1   1 
ATOM   21661 C  CD2   . PHE A 1 4482 ? 251.792 225.092 222.500 1.00 15.27  ? 4482 PHE A CD2   1 
ATOM   21662 C  CE1   . PHE A 1 4482 ? 250.634 227.135 221.064 1.00 14.88  ? 4482 PHE A CE1   1 
ATOM   21663 C  CE2   . PHE A 1 4482 ? 251.845 226.384 222.978 1.00 14.73  ? 4482 PHE A CE2   1 
ATOM   21664 C  CZ    . PHE A 1 4482 ? 251.265 227.406 222.259 1.00 18.06  ? 4482 PHE A CZ    1 
ATOM   21665 N  N     . SER A 1 4483 ? 254.096 222.429 220.257 1.00 18.20  ? 4483 SER A N     1 
ATOM   21666 C  CA    . SER A 1 4483 ? 255.538 222.564 220.421 1.00 20.34  ? 4483 SER A CA    1 
ATOM   21667 C  C     . SER A 1 4483 ? 256.228 222.727 219.073 1.00 19.59  ? 4483 SER A C     1 
ATOM   21668 O  O     . SER A 1 4483 ? 257.128 223.562 218.926 1.00 21.94  ? 4483 SER A O     1 
ATOM   21669 C  CB    . SER A 1 4483 ? 256.099 221.357 221.172 1.00 25.06  ? 4483 SER A CB    1 
ATOM   21670 O  OG    . SER A 1 4483 ? 255.326 221.070 222.324 1.00 26.26  ? 4483 SER A OG    1 
ATOM   21671 N  N     . GLU A 1 4484 ? 255.811 221.944 218.074 1.00 22.57  ? 4484 GLU A N     1 
ATOM   21672 C  CA    . GLU A 1 4484 ? 256.384 222.090 216.738 1.00 18.77  ? 4484 GLU A CA    1 
ATOM   21673 C  C     . GLU A 1 4484 ? 256.136 223.486 216.179 1.00 19.31  ? 4484 GLU A C     1 
ATOM   21674 O  O     . GLU A 1 4484 ? 257.047 224.118 215.625 1.00 19.91  ? 4484 GLU A O     1 
ATOM   21675 C  CB    . GLU A 1 4484 ? 255.801 221.030 215.803 1.00 19.52  ? 4484 GLU A CB    1 
ATOM   21676 C  CG    . GLU A 1 4484 ? 256.636 219.766 215.689 1.00 28.35  ? 4484 GLU A CG    1 
ATOM   21677 C  CD    . GLU A 1 4484 ? 258.080 220.049 215.331 1.00 34.08  ? 4484 GLU A CD    1 
ATOM   21678 O  OE1   . GLU A 1 4484 ? 258.318 220.808 214.368 1.00 37.14  ? 4484 GLU A OE1   1 
ATOM   21679 O  OE2   . GLU A 1 4484 ? 258.978 219.513 216.012 1.00 30.49  ? 4484 GLU A OE2   1 
ATOM   21680 N  N     . ARG A 1 4485 ? 254.908 223.987 216.324 1.00 19.39  ? 4485 ARG A N     1 
ATOM   21681 C  CA    . ARG A 1 4485 ? 254.571 225.310 215.809 1.00 18.47  ? 4485 ARG A CA    1 
ATOM   21682 C  C     . ARG A 1 4485 ? 255.346 226.405 216.531 1.00 18.84  ? 4485 ARG A C     1 
ATOM   21683 O  O     . ARG A 1 4485 ? 255.801 227.368 215.903 1.00 21.48  ? 4485 ARG A O     1 
ATOM   21684 C  CB    . ARG A 1 4485 ? 253.067 225.549 215.929 1.00 17.05  ? 4485 ARG A CB    1 
ATOM   21685 C  CG    . ARG A 1 4485 ? 252.229 224.618 215.074 1.00 15.84  ? 4485 ARG A CG    1 
ATOM   21686 C  CD    . ARG A 1 4485 ? 250.747 224.825 215.317 1.00 14.91  ? 4485 ARG A CD    1 
ATOM   21687 N  NE    . ARG A 1 4485 ? 249.938 223.902 214.531 1.00 17.01  ? 4485 ARG A NE    1 
ATOM   21688 C  CZ    . ARG A 1 4485 ? 249.011 224.275 213.661 1.00 18.76  ? 4485 ARG A CZ    1 
ATOM   21689 N  NH1   . ARG A 1 4485 ? 248.744 225.550 213.438 1.00 18.82  ? 4485 ARG A NH1   1 
ATOM   21690 N  NH2   . ARG A 1 4485 ? 248.335 223.343 212.995 1.00 18.92  ? 4485 ARG A NH2   1 
ATOM   21691 N  N     . ILE A 1 4486 ? 255.504 226.281 217.850 1.00 18.25  ? 4486 ILE A N     1 
ATOM   21692 C  CA    . ILE A 1 4486 ? 256.233 227.293 218.606 1.00 15.80  ? 4486 ILE A CA    1 
ATOM   21693 C  C     . ILE A 1 4486 ? 257.711 227.271 218.240 1.00 20.31  ? 4486 ILE A C     1 
ATOM   21694 O  O     . ILE A 1 4486 ? 258.355 228.322 218.160 1.00 24.24  ? 4486 ILE A O     1 
ATOM   21695 C  CB    . ILE A 1 4486 ? 256.013 227.102 220.118 1.00 18.65  ? 4486 ILE A CB    1 
ATOM   21696 C  CG1   . ILE A 1 4486 ? 254.553 227.370 220.483 1.00 17.25  ? 4486 ILE A CG1   1 
ATOM   21697 C  CG2   . ILE A 1 4486 ? 256.916 228.030 220.914 1.00 17.52  ? 4486 ILE A CG2   1 
ATOM   21698 C  CD1   . ILE A 1 4486 ? 254.067 228.746 220.095 1.00 15.53  ? 4486 ILE A CD1   1 
ATOM   21699 N  N     . LYS A 1 4487 ? 258.275 226.083 218.003 1.00 17.24  ? 4487 LYS A N     1 
ATOM   21700 C  CA    . LYS A 1 4487 ? 259.660 226.016 217.547 1.00 16.35  ? 4487 LYS A CA    1 
ATOM   21701 C  C     . LYS A 1 4487 ? 259.821 226.649 216.169 1.00 18.73  ? 4487 LYS A C     1 
ATOM   21702 O  O     . LYS A 1 4487 ? 260.810 227.350 215.910 1.00 20.77  ? 4487 LYS A O     1 
ATOM   21703 C  CB    . LYS A 1 4487 ? 260.149 224.567 217.547 1.00 17.97  ? 4487 LYS A CB    1 
ATOM   21704 C  CG    . LYS A 1 4487 ? 260.261 223.962 218.940 1.00 25.15  ? 4487 LYS A CG    1 
ATOM   21705 C  CD    . LYS A 1 4487 ? 260.899 222.585 218.912 1.00 23.81  ? 4487 LYS A CD    1 
ATOM   21706 C  CE    . LYS A 1 4487 ? 259.937 221.545 218.362 1.00 33.16  ? 4487 LYS A CE    1 
ATOM   21707 N  NZ    . LYS A 1 4487 ? 260.502 220.169 218.428 1.00 30.79  ? 4487 LYS A NZ    1 
ATOM   21708 N  N     . GLN A 1 4488 ? 258.859 226.421 215.270 1.00 17.77  ? 4488 GLN A N     1 
ATOM   21709 C  CA    . GLN A 1 4488 ? 258.911 227.074 213.965 1.00 17.84  ? 4488 GLN A CA    1 
ATOM   21710 C  C     . GLN A 1 4488 ? 258.828 228.590 214.103 1.00 20.30  ? 4488 GLN A C     1 
ATOM   21711 O  O     . GLN A 1 4488 ? 259.535 229.328 213.407 1.00 20.08  ? 4488 GLN A O     1 
ATOM   21712 C  CB    . GLN A 1 4488 ? 257.787 226.561 213.066 1.00 20.77  ? 4488 GLN A CB    1 
ATOM   21713 C  CG    . GLN A 1 4488 ? 257.655 227.331 211.762 1.00 24.25  ? 4488 GLN A CG    1 
ATOM   21714 C  CD    . GLN A 1 4488 ? 256.409 226.969 210.986 1.00 21.65  ? 4488 GLN A CD    1 
ATOM   21715 O  OE1   . GLN A 1 4488 ? 256.483 226.542 209.836 1.00 20.02  ? 4488 GLN A OE1   1 
ATOM   21716 N  NE2   . GLN A 1 4488 ? 255.252 227.145 211.611 1.00 23.48  ? 4488 GLN A NE2   1 
ATOM   21717 N  N     . LEU A 1 4489 ? 257.962 229.073 214.997 1.00 21.29  ? 4489 LEU A N     1 
ATOM   21718 C  CA    . LEU A 1 4489 ? 257.854 230.511 215.222 1.00 17.21  ? 4489 LEU A CA    1 
ATOM   21719 C  C     . LEU A 1 4489 ? 259.134 231.077 215.824 1.00 17.01  ? 4489 LEU A C     1 
ATOM   21720 O  O     . LEU A 1 4489 ? 259.532 232.201 215.502 1.00 18.29  ? 4489 LEU A O     1 
ATOM   21721 C  CB    . LEU A 1 4489 ? 256.653 230.812 216.116 1.00 16.21  ? 4489 LEU A CB    1 
ATOM   21722 C  CG    . LEU A 1 4489 ? 255.289 230.653 215.444 1.00 16.74  ? 4489 LEU A CG    1 
ATOM   21723 C  CD1   . LEU A 1 4489 ? 254.178 231.121 216.366 1.00 13.56  ? 4489 LEU A CD1   1 
ATOM   21724 C  CD2   . LEU A 1 4489 ? 255.251 231.415 214.131 1.00 13.79  ? 4489 LEU A CD2   1 
ATOM   21725 N  N     . GLN A 1 4490 ? 259.784 230.320 216.709 1.00 18.99  ? 4490 GLN A N     1 
ATOM   21726 C  CA    . GLN A 1 4490 ? 261.069 230.747 217.253 1.00 16.71  ? 4490 GLN A CA    1 
ATOM   21727 C  C     . GLN A 1 4490 ? 262.120 230.848 216.158 1.00 18.77  ? 4490 GLN A C     1 
ATOM   21728 O  O     . GLN A 1 4490 ? 262.918 231.791 216.137 1.00 23.35  ? 4490 GLN A O     1 
ATOM   21729 C  CB    . GLN A 1 4490 ? 261.528 229.777 218.342 1.00 13.21  ? 4490 GLN A CB    1 
ATOM   21730 C  CG    . GLN A 1 4490 ? 260.739 229.865 219.633 1.00 14.56  ? 4490 GLN A CG    1 
ATOM   21731 C  CD    . GLN A 1 4490 ? 261.286 228.948 220.706 1.00 18.97  ? 4490 GLN A CD    1 
ATOM   21732 O  OE1   . GLN A 1 4490 ? 261.473 227.754 220.481 1.00 20.99  ? 4490 GLN A OE1   1 
ATOM   21733 N  NE2   . GLN A 1 4490 ? 261.541 229.503 221.884 1.00 22.48  ? 4490 GLN A NE2   1 
ATOM   21734 N  N     . ASN A 1 4491 ? 262.136 229.878 215.241 1.00 21.60  ? 4491 ASN A N     1 
ATOM   21735 C  CA    . ASN A 1 4491 ? 263.058 229.946 214.112 1.00 19.85  ? 4491 ASN A CA    1 
ATOM   21736 C  C     . ASN A 1 4491 ? 262.768 231.161 213.239 1.00 20.27  ? 4491 ASN A C     1 
ATOM   21737 O  O     . ASN A 1 4491 ? 263.693 231.838 212.775 1.00 25.41  ? 4491 ASN A O     1 
ATOM   21738 C  CB    . ASN A 1 4491 ? 262.976 228.661 213.289 1.00 21.31  ? 4491 ASN A CB    1 
ATOM   21739 C  CG    . ASN A 1 4491 ? 263.669 227.494 213.962 1.00 29.32  ? 4491 ASN A CG    1 
ATOM   21740 O  OD1   . ASN A 1 4491 ? 263.062 226.450 214.198 1.00 27.23  ? 4491 ASN A OD1   1 
ATOM   21741 N  ND2   . ASN A 1 4491 ? 264.948 227.667 214.274 1.00 34.33  ? 4491 ASN A ND2   1 
ATOM   21742 N  N     . ILE A 1 4492 ? 261.487 231.451 213.006 1.00 21.93  ? 4492 ILE A N     1 
ATOM   21743 C  CA    . ILE A 1 4492 ? 261.110 232.614 212.207 1.00 23.85  ? 4492 ILE A CA    1 
ATOM   21744 C  C     . ILE A 1 4492 ? 261.563 233.900 212.888 1.00 25.98  ? 4492 ILE A C     1 
ATOM   21745 O  O     . ILE A 1 4492 ? 262.086 234.815 212.239 1.00 35.24  ? 4492 ILE A O     1 
ATOM   21746 C  CB    . ILE A 1 4492 ? 259.591 232.613 211.950 1.00 22.62  ? 4492 ILE A CB    1 
ATOM   21747 C  CG1   . ILE A 1 4492 ? 259.226 231.542 210.921 1.00 20.94  ? 4492 ILE A CG1   1 
ATOM   21748 C  CG2   . ILE A 1 4492 ? 259.121 233.983 211.485 1.00 19.48  ? 4492 ILE A CG2   1 
ATOM   21749 C  CD1   . ILE A 1 4492 ? 257.740 231.316 210.781 1.00 19.73  ? 4492 ILE A CD1   1 
ATOM   21750 N  N     . SER A 1 4493 ? 261.365 233.992 214.205 1.00 22.01  ? 4493 SER A N     1 
ATOM   21751 C  CA    . SER A 1 4493 ? 261.786 235.179 214.942 1.00 20.57  ? 4493 SER A CA    1 
ATOM   21752 C  C     . SER A 1 4493 ? 263.300 235.339 214.915 1.00 27.68  ? 4493 SER A C     1 
ATOM   21753 O  O     . SER A 1 4493 ? 263.810 236.457 214.777 1.00 35.11  ? 4493 SER A O     1 
ATOM   21754 C  CB    . SER A 1 4493 ? 261.281 235.106 216.383 1.00 21.62  ? 4493 SER A CB    1 
ATOM   21755 O  OG    . SER A 1 4493 ? 259.902 235.417 216.457 1.00 28.07  ? 4493 SER A OG    1 
ATOM   21756 N  N     . LEU A 1 4494 ? 264.034 234.235 215.059 1.00 27.69  ? 4494 LEU A N     1 
ATOM   21757 C  CA    . LEU A 1 4494 ? 265.489 234.302 214.988 1.00 27.84  ? 4494 LEU A CA    1 
ATOM   21758 C  C     . LEU A 1 4494 ? 265.950 234.751 213.608 1.00 33.40  ? 4494 LEU A C     1 
ATOM   21759 O  O     . LEU A 1 4494 ? 266.884 235.551 213.487 1.00 41.72  ? 4494 LEU A O     1 
ATOM   21760 C  CB    . LEU A 1 4494 ? 266.098 232.948 215.345 1.00 29.18  ? 4494 LEU A CB    1 
ATOM   21761 C  CG    . LEU A 1 4494 ? 267.626 232.898 215.373 1.00 38.62  ? 4494 LEU A CG    1 
ATOM   21762 C  CD1   . LEU A 1 4494 ? 268.168 233.833 216.441 1.00 34.40  ? 4494 LEU A CD1   1 
ATOM   21763 C  CD2   . LEU A 1 4494 ? 268.118 231.476 215.598 1.00 40.96  ? 4494 LEU A CD2   1 
ATOM   21764 N  N     . ALA A 1 4495 ? 265.308 234.244 212.553 1.00 33.19  ? 4495 ALA A N     1 
ATOM   21765 C  CA    . ALA A 1 4495 ? 265.652 234.672 211.202 1.00 35.27  ? 4495 ALA A CA    1 
ATOM   21766 C  C     . ALA A 1 4495 ? 265.363 236.155 211.004 1.00 40.34  ? 4495 ALA A C     1 
ATOM   21767 O  O     . ALA A 1 4495 ? 266.157 236.873 210.384 1.00 45.10  ? 4495 ALA A O     1 
ATOM   21768 C  CB    . ALA A 1 4495 ? 264.890 233.834 210.177 1.00 28.99  ? 4495 ALA A CB    1 
ATOM   21769 N  N     . ALA A 1 4496 ? 264.229 236.631 211.522 1.00 37.39  ? 4496 ALA A N     1 
ATOM   21770 C  CA    . ALA A 1 4496 ? 263.887 238.044 211.390 1.00 36.44  ? 4496 ALA A CA    1 
ATOM   21771 C  C     . ALA A 1 4496 ? 264.876 238.930 212.137 1.00 40.75  ? 4496 ALA A C     1 
ATOM   21772 O  O     . ALA A 1 4496 ? 265.295 239.973 211.622 1.00 45.47  ? 4496 ALA A O     1 
ATOM   21773 C  CB    . ALA A 1 4496 ? 262.466 238.288 211.893 1.00 31.61  ? 4496 ALA A CB    1 
ATOM   21774 N  N     . ALA A 1 4497 ? 265.258 238.535 213.353 1.00 43.07  ? 4497 ALA A N     1 
ATOM   21775 C  CA    . ALA A 1 4497 ? 266.187 239.345 214.135 1.00 42.69  ? 4497 ALA A CA    1 
ATOM   21776 C  C     . ALA A 1 4497 ? 267.585 239.337 213.526 1.00 49.52  ? 4497 ALA A C     1 
ATOM   21777 O  O     . ALA A 1 4497 ? 268.223 240.389 213.413 1.00 49.80  ? 4497 ALA A O     1 
ATOM   21778 C  CB    . ALA A 1 4497 ? 266.226 238.850 215.579 1.00 33.71  ? 4497 ALA A CB    1 
ATOM   21779 N  N     . SER A 1 4498 ? 268.077 238.159 213.133 1.00 49.77  ? 4498 SER A N     1 
ATOM   21780 C  CA    . SER A 1 4498 ? 269.414 238.067 212.552 1.00 51.83  ? 4498 SER A CA    1 
ATOM   21781 C  C     . SER A 1 4498 ? 269.495 238.802 211.220 1.00 51.04  ? 4498 SER A C     1 
ATOM   21782 O  O     . SER A 1 4498 ? 270.494 239.471 210.934 1.00 56.63  ? 4498 SER A O     1 
ATOM   21783 C  CB    . SER A 1 4498 ? 269.809 236.601 212.381 1.00 57.52  ? 4498 SER A CB    1 
ATOM   21784 O  OG    . SER A 1 4498 ? 269.774 235.913 213.620 1.00 57.63  ? 4498 SER A OG    1 
ATOM   21785 N  N     . GLY A 1 4499 ? 268.460 238.684 210.393 1.00 54.64  ? 4499 GLY A N     1 
ATOM   21786 C  CA    . GLY A 1 4499 ? 268.441 239.343 209.102 1.00 55.99  ? 4499 GLY A CA    1 
ATOM   21787 C  C     . GLY A 1 4499 ? 267.544 240.563 209.076 1.00 55.53  ? 4499 GLY A C     1 
ATOM   21788 O  O     . GLY A 1 4499 ? 267.931 241.640 209.539 1.00 59.53  ? 4499 GLY A O     1 
ATOM   21789 N  N     . GLY A 1 4500 ? 266.345 240.404 208.534 1.00 56.47  ? 4500 GLY A N     1 
ATOM   21790 C  CA    . GLY A 1 4500 ? 265.414 241.511 208.467 1.00 56.96  ? 4500 GLY A CA    1 
ATOM   21791 C  C     . GLY A 1 4500 ? 264.189 241.129 207.674 1.00 65.17  ? 4500 GLY A C     1 
ATOM   21792 O  O     . GLY A 1 4500 ? 263.891 239.946 207.495 1.00 60.05  ? 4500 GLY A O     1 
ATOM   21793 N  N     . ALA A 1 4501 ? 263.472 242.151 207.200 1.00 67.38  ? 4501 ALA A N     1 
ATOM   21794 C  CA    . ALA A 1 4501 ? 262.300 241.905 206.368 1.00 65.95  ? 4501 ALA A CA    1 
ATOM   21795 C  C     . ALA A 1 4501 ? 262.675 241.207 205.068 1.00 62.86  ? 4501 ALA A C     1 
ATOM   21796 O  O     . ALA A 1 4501 ? 261.890 240.408 204.544 1.00 60.28  ? 4501 ALA A O     1 
ATOM   21797 C  CB    . ALA A 1 4501 ? 261.574 243.218 206.078 1.00 60.74  ? 4501 ALA A CB    1 
ATOM   21798 N  N     . LYS A 1 4502 ? 263.862 241.496 204.531 1.00 58.54  ? 4502 LYS A N     1 
ATOM   21799 C  CA    . LYS A 1 4502 ? 264.309 240.813 203.321 1.00 60.35  ? 4502 LYS A CA    1 
ATOM   21800 C  C     . LYS A 1 4502 ? 264.675 239.360 203.601 1.00 62.16  ? 4502 LYS A C     1 
ATOM   21801 O  O     . LYS A 1 4502 ? 264.554 238.511 202.711 1.00 57.85  ? 4502 LYS A O     1 
ATOM   21802 C  CB    . LYS A 1 4502 ? 265.494 241.557 202.705 1.00 61.52  ? 4502 LYS A CB    1 
ATOM   21803 C  CG    . LYS A 1 4502 ? 266.750 241.562 203.563 1.00 68.81  ? 4502 LYS A CG    1 
ATOM   21804 C  CD    . LYS A 1 4502 ? 267.868 242.355 202.905 1.00 73.94  ? 4502 LYS A CD    1 
ATOM   21805 C  CE    . LYS A 1 4502 ? 269.128 242.342 203.756 1.00 77.29  ? 4502 LYS A CE    1 
ATOM   21806 N  NZ    . LYS A 1 4502 ? 270.232 243.118 203.128 1.00 74.64  ? 4502 LYS A NZ    1 
ATOM   21807 N  N     . GLU A 1 4503 ? 265.124 239.058 204.821 1.00 58.11  ? 4503 GLU A N     1 
ATOM   21808 C  CA    . GLU A 1 4503 ? 265.479 237.686 205.165 1.00 56.38  ? 4503 GLU A CA    1 
ATOM   21809 C  C     . GLU A 1 4503 ? 264.241 236.805 205.289 1.00 54.28  ? 4503 GLU A C     1 
ATOM   21810 O  O     . GLU A 1 4503 ? 264.310 235.598 205.027 1.00 54.62  ? 4503 GLU A O     1 
ATOM   21811 C  CB    . GLU A 1 4503 ? 266.291 237.674 206.463 1.00 63.41  ? 4503 GLU A CB    1 
ATOM   21812 C  CG    . GLU A 1 4503 ? 266.387 236.329 207.165 1.00 56.51  ? 4503 GLU A CG    1 
ATOM   21813 C  CD    . GLU A 1 4503 ? 267.300 235.358 206.441 1.00 72.09  ? 4503 GLU A CD    1 
ATOM   21814 O  OE1   . GLU A 1 4503 ? 268.322 235.808 205.880 1.00 71.81  ? 4503 GLU A OE1   1 
ATOM   21815 O  OE2   . GLU A 1 4503 ? 267.000 234.145 206.435 1.00 69.22  ? 4503 GLU A OE2   1 
ATOM   21816 N  N     . LEU A 1 4504 ? 263.101 237.391 205.664 1.00 53.12  ? 4504 LEU A N     1 
ATOM   21817 C  CA    . LEU A 1 4504 ? 261.875 236.620 205.840 1.00 44.63  ? 4504 LEU A CA    1 
ATOM   21818 C  C     . LEU A 1 4504 ? 261.386 235.993 204.543 1.00 38.50  ? 4504 LEU A C     1 
ATOM   21819 O  O     . LEU A 1 4504 ? 260.576 235.062 204.585 1.00 41.38  ? 4504 LEU A O     1 
ATOM   21820 C  CB    . LEU A 1 4504 ? 260.778 237.507 206.428 1.00 42.79  ? 4504 LEU A CB    1 
ATOM   21821 C  CG    . LEU A 1 4504 ? 261.005 238.021 207.848 1.00 43.59  ? 4504 LEU A CG    1 
ATOM   21822 C  CD1   . LEU A 1 4504 ? 259.909 238.995 208.242 1.00 38.70  ? 4504 LEU A CD1   1 
ATOM   21823 C  CD2   . LEU A 1 4504 ? 261.072 236.859 208.825 1.00 37.81  ? 4504 LEU A CD2   1 
ATOM   21824 N  N     . LYS A 1 4505 ? 261.848 236.484 203.394 1.00 37.53  ? 4505 LYS A N     1 
ATOM   21825 C  CA    . LYS A 1 4505 ? 261.419 235.920 202.121 1.00 33.64  ? 4505 LYS A CA    1 
ATOM   21826 C  C     . LYS A 1 4505 ? 262.103 234.591 201.824 1.00 33.31  ? 4505 LYS A C     1 
ATOM   21827 O  O     . LYS A 1 4505 ? 261.497 233.716 201.195 1.00 40.00  ? 4505 LYS A O     1 
ATOM   21828 C  CB    . LYS A 1 4505 ? 261.685 236.922 200.995 1.00 31.26  ? 4505 LYS A CB    1 
ATOM   21829 C  CG    . LYS A 1 4505 ? 261.123 236.523 199.642 1.00 26.93  ? 4505 LYS A CG    1 
ATOM   21830 C  CD    . LYS A 1 4505 ? 262.192 235.891 198.774 1.00 32.90  ? 4505 LYS A CD    1 
ATOM   21831 C  CE    . LYS A 1 4505 ? 261.643 235.477 197.427 1.00 31.50  ? 4505 LYS A CE    1 
ATOM   21832 N  NZ    . LYS A 1 4505 ? 262.685 234.773 196.640 1.00 32.45  ? 4505 LYS A NZ    1 
ATOM   21833 N  N     . ASN A 1 4506 ? 263.346 234.417 202.264 1.00 34.12  ? 4506 ASN A N     1 
ATOM   21834 C  CA    . ASN A 1 4506 ? 264.136 233.244 201.920 1.00 29.76  ? 4506 ASN A CA    1 
ATOM   21835 C  C     . ASN A 1 4506 ? 263.954 232.082 202.888 1.00 30.64  ? 4506 ASN A C     1 
ATOM   21836 O  O     . ASN A 1 4506 ? 264.585 231.038 202.698 1.00 33.06  ? 4506 ASN A O     1 
ATOM   21837 C  CB    . ASN A 1 4506 ? 265.621 233.614 201.845 1.00 37.31  ? 4506 ASN A CB    1 
ATOM   21838 C  CG    . ASN A 1 4506 ? 265.919 234.596 200.731 1.00 43.33  ? 4506 ASN A CG    1 
ATOM   21839 O  OD1   . ASN A 1 4506 ? 266.267 235.749 200.979 1.00 49.17  ? 4506 ASN A OD1   1 
ATOM   21840 N  ND2   . ASN A 1 4506 ? 265.784 234.139 199.491 1.00 39.76  ? 4506 ASN A ND2   1 
ATOM   21841 N  N     . ILE A 1 4507 ? 263.125 232.226 203.904 1.00 31.71  ? 4507 ILE A N     1 
ATOM   21842 C  CA    . ILE A 1 4507 ? 262.900 231.149 204.859 1.00 32.07  ? 4507 ILE A CA    1 
ATOM   21843 C  C     . ILE A 1 4507 ? 261.834 230.213 204.308 1.00 32.37  ? 4507 ILE A C     1 
ATOM   21844 O  O     . ILE A 1 4507 ? 260.923 230.626 203.584 1.00 34.75  ? 4507 ILE A O     1 
ATOM   21845 C  CB    . ILE A 1 4507 ? 262.506 231.695 206.247 1.00 32.99  ? 4507 ILE A CB    1 
ATOM   21846 C  CG1   . ILE A 1 4507 ? 261.130 232.360 206.195 1.00 32.71  ? 4507 ILE A CG1   1 
ATOM   21847 C  CG2   . ILE A 1 4507 ? 263.557 232.671 206.752 1.00 36.13  ? 4507 ILE A CG2   1 
ATOM   21848 C  CD1   . ILE A 1 4507 ? 260.547 232.657 207.557 1.00 33.39  ? 4507 ILE A CD1   1 
ATOM   21849 N  N     . HIS A 1 4508 ? 261.960 228.934 204.642 1.00 30.76  ? 4508 HIS A N     1 
ATOM   21850 C  CA    . HIS A 1 4508 ? 260.977 227.924 204.276 1.00 20.47  ? 4508 HIS A CA    1 
ATOM   21851 C  C     . HIS A 1 4508 ? 260.083 227.666 205.481 1.00 25.46  ? 4508 HIS A C     1 
ATOM   21852 O  O     . HIS A 1 4508 ? 260.577 227.335 206.564 1.00 38.55  ? 4508 HIS A O     1 
ATOM   21853 C  CB    . HIS A 1 4508 ? 261.652 226.633 203.820 1.00 22.29  ? 4508 HIS A CB    1 
ATOM   21854 C  CG    . HIS A 1 4508 ? 262.791 226.845 202.873 1.00 27.69  ? 4508 HIS A CG    1 
ATOM   21855 N  ND1   . HIS A 1 4508 ? 262.643 227.491 201.664 1.00 31.68  ? 4508 HIS A ND1   1 
ATOM   21856 C  CD2   . HIS A 1 4508 ? 264.093 226.482 202.950 1.00 25.93  ? 4508 HIS A CD2   1 
ATOM   21857 C  CE1   . HIS A 1 4508 ? 263.808 227.526 201.043 1.00 30.41  ? 4508 HIS A CE1   1 
ATOM   21858 N  NE2   . HIS A 1 4508 ? 264.704 226.920 201.800 1.00 31.98  ? 4508 HIS A NE2   1 
ATOM   21859 N  N     . VAL A 1 4509 ? 258.777 227.817 205.293 1.00 22.97  ? 4509 VAL A N     1 
ATOM   21860 C  CA    . VAL A 1 4509 ? 257.820 227.637 206.372 1.00 23.14  ? 4509 VAL A CA    1 
ATOM   21861 C  C     . VAL A 1 4509 ? 257.021 226.367 206.121 1.00 21.06  ? 4509 VAL A C     1 
ATOM   21862 O  O     . VAL A 1 4509 ? 256.905 225.879 204.993 1.00 20.93  ? 4509 VAL A O     1 
ATOM   21863 C  CB    . VAL A 1 4509 ? 256.878 228.849 206.522 1.00 19.44  ? 4509 VAL A CB    1 
ATOM   21864 C  CG1   . VAL A 1 4509 ? 257.671 230.098 206.866 1.00 23.43  ? 4509 VAL A CG1   1 
ATOM   21865 C  CG2   . VAL A 1 4509 ? 256.066 229.050 205.256 1.00 19.52  ? 4509 VAL A CG2   1 
ATOM   21866 N  N     . CYS A 1 4510 ? 256.468 225.826 207.201 1.00 20.01  ? 4510 CYS A N     1 
ATOM   21867 C  CA    . CYS A 1 4510 ? 255.547 224.699 207.135 1.00 15.69  ? 4510 CYS A CA    1 
ATOM   21868 C  C     . CYS A 1 4510 ? 254.131 225.260 207.199 1.00 19.04  ? 4510 CYS A C     1 
ATOM   21869 O  O     . CYS A 1 4510 ? 253.747 225.879 208.198 1.00 15.34  ? 4510 CYS A O     1 
ATOM   21870 C  CB    . CYS A 1 4510 ? 255.809 223.712 208.270 1.00 17.56  ? 4510 CYS A CB    1 
ATOM   21871 S  SG    . CYS A 1 4510 ? 254.710 222.277 208.287 1.00 28.36  ? 4510 CYS A SG    1 
ATOM   21872 N  N     . LEU A 1 4511 ? 253.361 225.049 206.129 1.00 18.53  ? 4511 LEU A N     1 
ATOM   21873 C  CA    . LEU A 1 4511 ? 252.012 225.600 206.068 1.00 13.26  ? 4511 LEU A CA    1 
ATOM   21874 C  C     . LEU A 1 4511 ? 251.116 225.017 207.152 1.00 14.40  ? 4511 LEU A C     1 
ATOM   21875 O  O     . LEU A 1 4511 ? 250.216 225.702 207.646 1.00 19.71  ? 4511 LEU A O     1 
ATOM   21876 C  CB    . LEU A 1 4511 ? 251.406 225.351 204.688 1.00 12.92  ? 4511 LEU A CB    1 
ATOM   21877 C  CG    . LEU A 1 4511 ? 251.772 226.353 203.592 1.00 14.69  ? 4511 LEU A CG    1 
ATOM   21878 C  CD1   . LEU A 1 4511 ? 250.918 226.128 202.356 1.00 18.99  ? 4511 LEU A CD1   1 
ATOM   21879 C  CD2   . LEU A 1 4511 ? 251.629 227.780 204.094 1.00 16.84  ? 4511 LEU A CD2   1 
ATOM   21880 N  N     . GLY A 1 4512 ? 251.347 223.760 207.535 1.00 13.84  ? 4512 GLY A N     1 
ATOM   21881 C  CA    . GLY A 1 4512 ? 250.570 223.160 208.603 1.00 14.63  ? 4512 GLY A CA    1 
ATOM   21882 C  C     . GLY A 1 4512 ? 250.906 223.690 209.979 1.00 20.17  ? 4512 GLY A C     1 
ATOM   21883 O  O     . GLY A 1 4512 ? 250.084 223.575 210.893 1.00 22.78  ? 4512 GLY A O     1 
ATOM   21884 N  N     . GLY A 1 4513 ? 252.091 224.266 210.148 1.00 17.33  ? 4513 GLY A N     1 
ATOM   21885 C  CA    . GLY A 1 4513 ? 252.514 224.856 211.397 1.00 13.72  ? 4513 GLY A CA    1 
ATOM   21886 C  C     . GLY A 1 4513 ? 252.153 226.313 211.573 1.00 19.29  ? 4513 GLY A C     1 
ATOM   21887 O  O     . GLY A 1 4513 ? 252.555 226.922 212.571 1.00 26.80  ? 4513 GLY A O     1 
ATOM   21888 N  N     . LEU A 1 4514 ? 251.414 226.896 210.636 1.00 18.71  ? 4514 LEU A N     1 
ATOM   21889 C  CA    . LEU A 1 4514 ? 250.981 228.282 210.720 1.00 16.34  ? 4514 LEU A CA    1 
ATOM   21890 C  C     . LEU A 1 4514 ? 249.512 228.337 211.114 1.00 18.36  ? 4514 LEU A C     1 
ATOM   21891 O  O     . LEU A 1 4514 ? 248.712 227.504 210.677 1.00 25.63  ? 4514 LEU A O     1 
ATOM   21892 C  CB    . LEU A 1 4514 ? 251.192 229.005 209.390 1.00 17.12  ? 4514 LEU A CB    1 
ATOM   21893 C  CG    . LEU A 1 4514 ? 252.637 229.149 208.912 1.00 15.50  ? 4514 LEU A CG    1 
ATOM   21894 C  CD1   . LEU A 1 4514 ? 252.679 229.779 207.532 1.00 16.31  ? 4514 LEU A CD1   1 
ATOM   21895 C  CD2   . LEU A 1 4514 ? 253.447 229.967 209.900 1.00 16.80  ? 4514 LEU A CD2   1 
ATOM   21896 N  N     . PHE A 1 4515 ? 249.165 229.318 211.950 1.00 18.39  ? 4515 PHE A N     1 
ATOM   21897 C  CA    . PHE A 1 4515 ? 247.781 229.447 212.397 1.00 23.26  ? 4515 PHE A CA    1 
ATOM   21898 C  C     . PHE A 1 4515 ? 246.851 229.738 211.227 1.00 23.80  ? 4515 PHE A C     1 
ATOM   21899 O  O     . PHE A 1 4515 ? 245.753 229.178 211.139 1.00 33.46  ? 4515 PHE A O     1 
ATOM   21900 C  CB    . PHE A 1 4515 ? 247.670 230.541 213.458 1.00 23.54  ? 4515 PHE A CB    1 
ATOM   21901 C  CG    . PHE A 1 4515 ? 248.511 230.291 214.676 1.00 26.20  ? 4515 PHE A CG    1 
ATOM   21902 C  CD1   . PHE A 1 4515 ? 249.812 230.757 214.743 1.00 23.57  ? 4515 PHE A CD1   1 
ATOM   21903 C  CD2   . PHE A 1 4515 ? 248.007 229.578 215.748 1.00 22.64  ? 4515 PHE A CD2   1 
ATOM   21904 C  CE1   . PHE A 1 4515 ? 250.589 230.525 215.857 1.00 27.05  ? 4515 PHE A CE1   1 
ATOM   21905 C  CE2   . PHE A 1 4515 ? 248.782 229.342 216.865 1.00 23.15  ? 4515 PHE A CE2   1 
ATOM   21906 C  CZ    . PHE A 1 4515 ? 250.073 229.815 216.920 1.00 24.55  ? 4515 PHE A CZ    1 
ATOM   21907 N  N     . VAL A 1 4516 ? 247.273 230.614 210.322 1.00 23.15  ? 4516 VAL A N     1 
ATOM   21908 C  CA    . VAL A 1 4516 ? 246.503 230.956 209.128 1.00 21.69  ? 4516 VAL A CA    1 
ATOM   21909 C  C     . VAL A 1 4516 ? 247.397 230.859 207.892 1.00 20.75  ? 4516 VAL A C     1 
ATOM   21910 O  O     . VAL A 1 4516 ? 248.061 231.833 207.514 1.00 23.31  ? 4516 VAL A O     1 
ATOM   21911 C  CB    . VAL A 1 4516 ? 245.834 232.334 209.285 1.00 19.23  ? 4516 VAL A CB    1 
ATOM   21912 C  CG1   . VAL A 1 4516 ? 244.793 232.277 210.381 1.00 21.71  ? 4516 VAL A CG1   1 
ATOM   21913 C  CG2   . VAL A 1 4516 ? 246.852 233.386 209.696 1.00 18.89  ? 4516 VAL A CG2   1 
ATOM   21914 N  N     . PRO A 1 4517 ? 247.452 229.695 207.237 1.00 18.96  ? 4517 PRO A N     1 
ATOM   21915 C  CA    . PRO A 1 4517 ? 248.319 229.566 206.055 1.00 18.30  ? 4517 PRO A CA    1 
ATOM   21916 C  C     . PRO A 1 4517 ? 247.804 230.312 204.836 1.00 19.39  ? 4517 PRO A C     1 
ATOM   21917 O  O     . PRO A 1 4517 ? 248.610 230.741 203.998 1.00 21.46  ? 4517 PRO A O     1 
ATOM   21918 C  CB    . PRO A 1 4517 ? 248.360 228.051 205.817 1.00 20.28  ? 4517 PRO A CB    1 
ATOM   21919 C  CG    . PRO A 1 4517 ? 247.087 227.547 206.398 1.00 23.73  ? 4517 PRO A CG    1 
ATOM   21920 C  CD    . PRO A 1 4517 ? 246.758 228.437 207.564 1.00 19.48  ? 4517 PRO A CD    1 
ATOM   21921 N  N     . GLU A 1 4518 ? 246.486 230.476 204.703 1.00 19.74  ? 4518 GLU A N     1 
ATOM   21922 C  CA    . GLU A 1 4518 ? 245.959 231.268 203.598 1.00 18.08  ? 4518 GLU A CA    1 
ATOM   21923 C  C     . GLU A 1 4518 ? 246.430 232.712 203.689 1.00 23.37  ? 4518 GLU A C     1 
ATOM   21924 O  O     . GLU A 1 4518 ? 246.652 233.362 202.659 1.00 24.13  ? 4518 GLU A O     1 
ATOM   21925 C  CB    . GLU A 1 4518 ? 244.430 231.188 203.571 1.00 21.87  ? 4518 GLU A CB    1 
ATOM   21926 C  CG    . GLU A 1 4518 ? 243.728 231.886 204.726 1.00 29.68  ? 4518 GLU A CG    1 
ATOM   21927 C  CD    . GLU A 1 4518 ? 243.616 231.015 205.965 1.00 35.42  ? 4518 GLU A CD    1 
ATOM   21928 O  OE1   . GLU A 1 4518 ? 244.326 229.993 206.049 1.00 31.57  ? 4518 GLU A OE1   1 
ATOM   21929 O  OE2   . GLU A 1 4518 ? 242.814 231.357 206.859 1.00 37.52  ? 4518 GLU A OE2   1 
ATOM   21930 N  N     . ALA A 1 4519 ? 246.619 233.218 204.909 1.00 21.60  ? 4519 ALA A N     1 
ATOM   21931 C  CA    . ALA A 1 4519 ? 247.219 234.535 205.072 1.00 19.15  ? 4519 ALA A CA    1 
ATOM   21932 C  C     . ALA A 1 4519 ? 248.656 234.546 204.572 1.00 20.26  ? 4519 ALA A C     1 
ATOM   21933 O  O     . ALA A 1 4519 ? 249.115 235.547 204.017 1.00 27.11  ? 4519 ALA A O     1 
ATOM   21934 C  CB    . ALA A 1 4519 ? 247.153 234.969 206.535 1.00 15.63  ? 4519 ALA A CB    1 
ATOM   21935 N  N     . TYR A 1 4520 ? 249.385 233.442 204.758 1.00 17.37  ? 4520 TYR A N     1 
ATOM   21936 C  CA    . TYR A 1 4520 ? 250.735 233.360 204.209 1.00 16.55  ? 4520 TYR A CA    1 
ATOM   21937 C  C     . TYR A 1 4520 ? 250.717 233.389 202.688 1.00 17.94  ? 4520 TYR A C     1 
ATOM   21938 O  O     . TYR A 1 4520 ? 251.550 234.056 202.062 1.00 21.36  ? 4520 TYR A O     1 
ATOM   21939 C  CB    . TYR A 1 4520 ? 251.442 232.097 204.692 1.00 15.19  ? 4520 TYR A CB    1 
ATOM   21940 C  CG    . TYR A 1 4520 ? 252.826 231.944 204.105 1.00 16.44  ? 4520 TYR A CG    1 
ATOM   21941 C  CD1   . TYR A 1 4520 ? 253.861 232.780 204.497 1.00 17.30  ? 4520 TYR A CD1   1 
ATOM   21942 C  CD2   . TYR A 1 4520 ? 253.092 230.981 203.143 1.00 16.25  ? 4520 TYR A CD2   1 
ATOM   21943 C  CE1   . TYR A 1 4520 ? 255.124 232.650 203.958 1.00 18.06  ? 4520 TYR A CE1   1 
ATOM   21944 C  CE2   . TYR A 1 4520 ? 254.351 230.844 202.601 1.00 13.93  ? 4520 TYR A CE2   1 
ATOM   21945 C  CZ    . TYR A 1 4520 ? 255.363 231.682 203.010 1.00 15.80  ? 4520 TYR A CZ    1 
ATOM   21946 O  OH    . TYR A 1 4520 ? 256.620 231.549 202.470 1.00 19.41  ? 4520 TYR A OH    1 
ATOM   21947 N  N     . ILE A 1 4521 ? 249.788 232.653 202.074 1.00 16.17  ? 4521 ILE A N     1 
ATOM   21948 C  CA    . ILE A 1 4521 ? 249.687 232.670 200.617 1.00 12.99  ? 4521 ILE A CA    1 
ATOM   21949 C  C     . ILE A 1 4521 ? 249.373 234.077 200.126 1.00 15.66  ? 4521 ILE A C     1 
ATOM   21950 O  O     . ILE A 1 4521 ? 249.975 234.569 199.162 1.00 21.36  ? 4521 ILE A O     1 
ATOM   21951 C  CB    . ILE A 1 4521 ? 248.635 231.653 200.137 1.00 14.35  ? 4521 ILE A CB    1 
ATOM   21952 C  CG1   . ILE A 1 4521 ? 248.821 230.311 200.848 1.00 18.55  ? 4521 ILE A CG1   1 
ATOM   21953 C  CG2   . ILE A 1 4521 ? 248.714 231.473 198.632 1.00 12.56  ? 4521 ILE A CG2   1 
ATOM   21954 C  CD1   . ILE A 1 4521 ? 250.028 229.534 200.380 1.00 16.52  ? 4521 ILE A CD1   1 
ATOM   21955 N  N     . THR A 1 4522 ? 248.432 234.750 200.793 1.00 19.38  ? 4522 THR A N     1 
ATOM   21956 C  CA    . THR A 1 4522 ? 248.089 236.117 200.416 1.00 16.55  ? 4522 THR A CA    1 
ATOM   21957 C  C     . THR A 1 4522 ? 249.273 237.057 200.599 1.00 17.84  ? 4522 THR A C     1 
ATOM   21958 O  O     . THR A 1 4522 ? 249.497 237.951 199.778 1.00 21.21  ? 4522 THR A O     1 
ATOM   21959 C  CB    . THR A 1 4522 ? 246.889 236.600 201.229 1.00 17.74  ? 4522 THR A CB    1 
ATOM   21960 O  OG1   . THR A 1 4522 ? 245.831 235.638 201.141 1.00 25.38  ? 4522 THR A OG1   1 
ATOM   21961 C  CG2   . THR A 1 4522 ? 246.395 237.942 200.712 1.00 16.02  ? 4522 THR A CG2   1 
ATOM   21962 N  N     . ALA A 1 4523 ? 250.040 236.878 201.677 1.00 18.40  ? 4523 ALA A N     1 
ATOM   21963 C  CA    . ALA A 1 4523 ? 251.196 237.733 201.924 1.00 16.27  ? 4523 ALA A CA    1 
ATOM   21964 C  C     . ALA A 1 4523 ? 252.270 237.537 200.863 1.00 16.74  ? 4523 ALA A C     1 
ATOM   21965 O  O     . ALA A 1 4523 ? 252.885 238.508 200.412 1.00 21.80  ? 4523 ALA A O     1 
ATOM   21966 C  CB    . ALA A 1 4523 ? 251.763 237.459 203.316 1.00 22.95  ? 4523 ALA A CB    1 
ATOM   21967 N  N     . THR A 1 4524 ? 252.520 236.289 200.459 1.00 16.90  ? 4524 THR A N     1 
ATOM   21968 C  CA    . THR A 1 4524 ? 253.487 236.043 199.392 1.00 14.46  ? 4524 THR A CA    1 
ATOM   21969 C  C     . THR A 1 4524 ? 253.014 236.645 198.075 1.00 15.56  ? 4524 THR A C     1 
ATOM   21970 O  O     . THR A 1 4524 ? 253.807 237.237 197.330 1.00 20.73  ? 4524 THR A O     1 
ATOM   21971 C  CB    . THR A 1 4524 ? 253.736 234.543 199.237 1.00 12.25  ? 4524 THR A CB    1 
ATOM   21972 O  OG1   . THR A 1 4524 ? 252.498 233.879 198.956 1.00 16.45  ? 4524 THR A OG1   1 
ATOM   21973 C  CG2   . THR A 1 4524 ? 254.336 233.971 200.507 1.00 13.24  ? 4524 THR A CG2   1 
ATOM   21974 N  N     . ARG A 1 4525 ? 251.720 236.507 197.778 1.00 14.63  ? 4525 ARG A N     1 
ATOM   21975 C  CA    . ARG A 1 4525 ? 251.165 237.118 196.574 1.00 15.92  ? 4525 ARG A CA    1 
ATOM   21976 C  C     . ARG A 1 4525 ? 251.320 238.635 196.608 1.00 16.69  ? 4525 ARG A C     1 
ATOM   21977 O  O     . ARG A 1 4525 ? 251.695 239.253 195.604 1.00 15.71  ? 4525 ARG A O     1 
ATOM   21978 C  CB    . ARG A 1 4525 ? 249.697 236.716 196.436 1.00 13.66  ? 4525 ARG A CB    1 
ATOM   21979 C  CG    . ARG A 1 4525 ? 249.056 237.035 195.103 1.00 13.78  ? 4525 ARG A CG    1 
ATOM   21980 C  CD    . ARG A 1 4525 ? 247.544 237.037 195.243 1.00 13.57  ? 4525 ARG A CD    1 
ATOM   21981 N  NE    . ARG A 1 4525 ? 246.864 236.970 193.958 1.00 18.11  ? 4525 ARG A NE    1 
ATOM   21982 C  CZ    . ARG A 1 4525 ? 245.848 236.162 193.693 1.00 19.09  ? 4525 ARG A CZ    1 
ATOM   21983 N  NH1   . ARG A 1 4525 ? 245.378 235.325 194.603 1.00 14.26  ? 4525 ARG A NH1   1 
ATOM   21984 N  NH2   . ARG A 1 4525 ? 245.289 236.195 192.488 1.00 19.98  ? 4525 ARG A NH2   1 
ATOM   21985 N  N     . GLN A 1 4526 ? 251.051 239.246 197.763 1.00 17.69  ? 4526 GLN A N     1 
ATOM   21986 C  CA    . GLN A 1 4526 ? 251.205 240.688 197.917 1.00 17.38  ? 4526 GLN A CA    1 
ATOM   21987 C  C     . GLN A 1 4526 ? 252.657 241.114 197.754 1.00 16.96  ? 4526 GLN A C     1 
ATOM   21988 O  O     . GLN A 1 4526 ? 252.942 242.147 197.138 1.00 21.17  ? 4526 GLN A O     1 
ATOM   21989 C  CB    . GLN A 1 4526 ? 250.679 241.119 199.287 1.00 17.83  ? 4526 GLN A CB    1 
ATOM   21990 C  CG    . GLN A 1 4526 ? 249.223 241.541 199.299 1.00 21.56  ? 4526 GLN A CG    1 
ATOM   21991 C  CD    . GLN A 1 4526 ? 248.889 242.424 200.482 1.00 23.79  ? 4526 GLN A CD    1 
ATOM   21992 O  OE1   . GLN A 1 4526 ? 248.683 241.938 201.592 1.00 35.27  ? 4526 GLN A OE1   1 
ATOM   21993 N  NE2   . GLN A 1 4526 ? 248.841 243.729 200.254 1.00 19.58  ? 4526 GLN A NE2   1 
ATOM   21994 N  N     . TYR A 1 4527 ? 253.587 240.339 198.315 1.00 15.24  ? 4527 TYR A N     1 
ATOM   21995 C  CA    . TYR A 1 4527 ? 255.003 240.665 198.186 1.00 16.30  ? 4527 TYR A CA    1 
ATOM   21996 C  C     . TYR A 1 4527 ? 255.442 240.621 196.730 1.00 16.01  ? 4527 TYR A C     1 
ATOM   21997 O  O     . TYR A 1 4527 ? 256.145 241.522 196.256 1.00 14.93  ? 4527 TYR A O     1 
ATOM   21998 C  CB    . TYR A 1 4527 ? 255.836 239.702 199.033 1.00 15.47  ? 4527 TYR A CB    1 
ATOM   21999 C  CG    . TYR A 1 4527 ? 257.330 239.909 198.936 1.00 16.22  ? 4527 TYR A CG    1 
ATOM   22000 C  CD1   . TYR A 1 4527 ? 257.976 240.817 199.762 1.00 17.84  ? 4527 TYR A CD1   1 
ATOM   22001 C  CD2   . TYR A 1 4527 ? 258.096 239.191 198.027 1.00 15.74  ? 4527 TYR A CD2   1 
ATOM   22002 C  CE1   . TYR A 1 4527 ? 259.341 241.010 199.682 1.00 20.97  ? 4527 TYR A CE1   1 
ATOM   22003 C  CE2   . TYR A 1 4527 ? 259.461 239.378 197.940 1.00 19.80  ? 4527 TYR A CE2   1 
ATOM   22004 C  CZ    . TYR A 1 4527 ? 260.077 240.289 198.770 1.00 20.82  ? 4527 TYR A CZ    1 
ATOM   22005 O  OH    . TYR A 1 4527 ? 261.437 240.480 198.690 1.00 18.01  ? 4527 TYR A OH    1 
ATOM   22006 N  N     . VAL A 1 4528 ? 255.025 239.585 196.000 1.00 15.55  ? 4528 VAL A N     1 
ATOM   22007 C  CA    . VAL A 1 4528 ? 255.380 239.493 194.587 1.00 13.68  ? 4528 VAL A CA    1 
ATOM   22008 C  C     . VAL A 1 4528 ? 254.756 240.638 193.800 1.00 15.46  ? 4528 VAL A C     1 
ATOM   22009 O  O     . VAL A 1 4528 ? 255.400 241.233 192.928 1.00 18.99  ? 4528 VAL A O     1 
ATOM   22010 C  CB    . VAL A 1 4528 ? 254.973 238.123 194.017 1.00 16.92  ? 4528 VAL A CB    1 
ATOM   22011 C  CG1   . VAL A 1 4528 ? 255.137 238.108 192.506 1.00 15.75  ? 4528 VAL A CG1   1 
ATOM   22012 C  CG2   . VAL A 1 4528 ? 255.803 237.025 194.652 1.00 18.05  ? 4528 VAL A CG2   1 
ATOM   22013 N  N     . ALA A 1 4529 ? 253.493 240.966 194.090 1.00 16.14  ? 4529 ALA A N     1 
ATOM   22014 C  CA    . ALA A 1 4529 ? 252.829 242.049 193.372 1.00 14.89  ? 4529 ALA A CA    1 
ATOM   22015 C  C     . ALA A 1 4529 ? 253.514 243.387 193.622 1.00 19.49  ? 4529 ALA A C     1 
ATOM   22016 O  O     . ALA A 1 4529 ? 253.699 244.180 192.692 1.00 29.18  ? 4529 ALA A O     1 
ATOM   22017 C  CB    . ALA A 1 4529 ? 251.357 242.117 193.774 1.00 18.26  ? 4529 ALA A CB    1 
ATOM   22018 N  N     . GLN A 1 4530 ? 253.896 243.658 194.870 1.00 20.17  ? 4530 GLN A N     1 
ATOM   22019 C  CA    . GLN A 1 4530 ? 254.537 244.930 195.187 1.00 19.14  ? 4530 GLN A CA    1 
ATOM   22020 C  C     . GLN A 1 4530 ? 255.947 245.001 194.614 1.00 19.35  ? 4530 GLN A C     1 
ATOM   22021 O  O     . GLN A 1 4530 ? 256.389 246.068 194.174 1.00 24.98  ? 4530 GLN A O     1 
ATOM   22022 C  CB    . GLN A 1 4530 ? 254.563 245.142 196.700 1.00 20.86  ? 4530 GLN A CB    1 
ATOM   22023 C  CG    . GLN A 1 4530 ? 253.293 245.751 197.263 1.00 21.36  ? 4530 GLN A CG    1 
ATOM   22024 C  CD    . GLN A 1 4530 ? 253.224 245.656 198.771 1.00 27.83  ? 4530 GLN A CD    1 
ATOM   22025 O  OE1   . GLN A 1 4530 ? 254.249 245.613 199.450 1.00 23.94  ? 4530 GLN A OE1   1 
ATOM   22026 N  NE2   . GLN A 1 4530 ? 252.009 245.615 199.307 1.00 29.39  ? 4530 GLN A NE2   1 
ATOM   22027 N  N     . ALA A 1 4531 ? 256.671 243.880 194.621 1.00 23.52  ? 4531 ALA A N     1 
ATOM   22028 C  CA    . ALA A 1 4531 ? 258.042 243.882 194.123 1.00 21.90  ? 4531 ALA A CA    1 
ATOM   22029 C  C     . ALA A 1 4531 ? 258.095 244.217 192.637 1.00 21.14  ? 4531 ALA A C     1 
ATOM   22030 O  O     . ALA A 1 4531 ? 258.972 244.968 192.195 1.00 27.54  ? 4531 ALA A O     1 
ATOM   22031 C  CB    . ALA A 1 4531 ? 258.700 242.529 194.392 1.00 21.42  ? 4531 ALA A CB    1 
ATOM   22032 N  N     . ASN A 1 4532 ? 257.171 243.669 191.851 1.00 20.43  ? 4532 ASN A N     1 
ATOM   22033 C  CA    . ASN A 1 4532 ? 257.139 243.884 190.412 1.00 23.85  ? 4532 ASN A CA    1 
ATOM   22034 C  C     . ASN A 1 4532 ? 256.168 244.983 189.998 1.00 26.75  ? 4532 ASN A C     1 
ATOM   22035 O  O     . ASN A 1 4532 ? 255.993 245.219 188.799 1.00 27.86  ? 4532 ASN A O     1 
ATOM   22036 C  CB    . ASN A 1 4532 ? 256.789 242.582 189.693 1.00 25.50  ? 4532 ASN A CB    1 
ATOM   22037 C  CG    . ASN A 1 4532 ? 257.849 241.514 189.869 1.00 31.24  ? 4532 ASN A CG    1 
ATOM   22038 O  OD1   . ASN A 1 4532 ? 258.656 241.270 188.973 1.00 37.34  ? 4532 ASN A OD1   1 
ATOM   22039 N  ND2   . ASN A 1 4532 ? 257.848 240.863 191.026 1.00 31.02  ? 4532 ASN A ND2   1 
ATOM   22040 N  N     . SER A 1 4533 ? 255.531 245.652 190.962 1.00 26.73  ? 4533 SER A N     1 
ATOM   22041 C  CA    . SER A 1 4533 ? 254.566 246.721 190.694 1.00 26.31  ? 4533 SER A CA    1 
ATOM   22042 C  C     . SER A 1 4533 ? 253.403 246.221 189.840 1.00 28.17  ? 4533 SER A C     1 
ATOM   22043 O  O     . SER A 1 4533 ? 252.843 246.957 189.025 1.00 29.78  ? 4533 SER A O     1 
ATOM   22044 C  CB    . SER A 1 4533 ? 255.240 247.930 190.041 1.00 35.47  ? 4533 SER A CB    1 
ATOM   22045 O  OG    . SER A 1 4533 ? 256.184 248.522 190.916 1.00 43.03  ? 4533 SER A OG    1 
ATOM   22046 N  N     . TRP A 1 4534 ? 253.035 244.957 190.028 1.00 26.75  ? 4534 TRP A N     1 
ATOM   22047 C  CA    . TRP A 1 4534 ? 251.913 244.372 189.318 1.00 25.42  ? 4534 TRP A CA    1 
ATOM   22048 C  C     . TRP A 1 4534 ? 250.628 244.563 190.117 1.00 32.90  ? 4534 TRP A C     1 
ATOM   22049 O  O     . TRP A 1 4534 ? 250.641 244.955 191.286 1.00 36.11  ? 4534 TRP A O     1 
ATOM   22050 C  CB    . TRP A 1 4534 ? 252.163 242.890 189.042 1.00 29.72  ? 4534 TRP A CB    1 
ATOM   22051 C  CG    . TRP A 1 4534 ? 253.277 242.626 188.084 1.00 33.09  ? 4534 TRP A CG    1 
ATOM   22052 C  CD1   . TRP A 1 4534 ? 253.742 243.466 187.114 1.00 30.24  ? 4534 TRP A CD1   1 
ATOM   22053 C  CD2   . TRP A 1 4534 ? 254.065 241.434 187.995 1.00 30.09  ? 4534 TRP A CD2   1 
ATOM   22054 N  NE1   . TRP A 1 4534 ? 254.774 242.871 186.430 1.00 34.35  ? 4534 TRP A NE1   1 
ATOM   22055 C  CE2   . TRP A 1 4534 ? 254.991 241.623 186.950 1.00 33.71  ? 4534 TRP A CE2   1 
ATOM   22056 C  CE3   . TRP A 1 4534 ? 254.081 240.227 188.699 1.00 27.79  ? 4534 TRP A CE3   1 
ATOM   22057 C  CZ2   . TRP A 1 4534 ? 255.922 240.652 186.594 1.00 33.59  ? 4534 TRP A CZ2   1 
ATOM   22058 C  CZ3   . TRP A 1 4534 ? 255.003 239.263 188.343 1.00 31.14  ? 4534 TRP A CZ3   1 
ATOM   22059 C  CH2   . TRP A 1 4534 ? 255.912 239.481 187.301 1.00 35.47  ? 4534 TRP A CH2   1 
ATOM   22060 N  N     . SER A 1 4535 ? 249.501 244.274 189.478 1.00 30.72  ? 4535 SER A N     1 
ATOM   22061 C  CA    . SER A 1 4535 ? 248.207 244.301 190.137 1.00 27.97  ? 4535 SER A CA    1 
ATOM   22062 C  C     . SER A 1 4535 ? 247.988 242.984 190.870 1.00 30.03  ? 4535 SER A C     1 
ATOM   22063 O  O     . SER A 1 4535 ? 248.389 241.916 190.400 1.00 32.48  ? 4535 SER A O     1 
ATOM   22064 C  CB    . SER A 1 4535 ? 247.079 244.539 189.133 1.00 35.49  ? 4535 SER A CB    1 
ATOM   22065 O  OG    . SER A 1 4535 ? 245.851 244.761 189.801 1.00 33.49  ? 4535 SER A OG    1 
ATOM   22066 N  N     . LEU A 1 4536 ? 247.351 243.073 192.037 1.00 25.92  ? 4536 LEU A N     1 
ATOM   22067 C  CA    . LEU A 1 4536 ? 247.263 241.913 192.917 1.00 22.30  ? 4536 LEU A CA    1 
ATOM   22068 C  C     . LEU A 1 4536 ? 246.358 240.836 192.329 1.00 25.95  ? 4536 LEU A C     1 
ATOM   22069 O  O     . LEU A 1 4536 ? 246.601 239.639 192.521 1.00 22.44  ? 4536 LEU A O     1 
ATOM   22070 C  CB    . LEU A 1 4536 ? 246.757 242.348 194.289 1.00 18.02  ? 4536 LEU A CB    1 
ATOM   22071 C  CG    . LEU A 1 4536 ? 246.785 241.323 195.417 1.00 14.10  ? 4536 LEU A CG    1 
ATOM   22072 C  CD1   . LEU A 1 4536 ? 248.047 240.491 195.340 1.00 11.91  ? 4536 LEU A CD1   1 
ATOM   22073 C  CD2   . LEU A 1 4536 ? 246.691 242.026 196.750 1.00 18.12  ? 4536 LEU A CD2   1 
ATOM   22074 N  N     . GLU A 1 4537 ? 245.316 241.240 191.603 1.00 30.32  ? 4537 GLU A N     1 
ATOM   22075 C  CA    . GLU A 1 4537 ? 244.310 240.301 191.124 1.00 27.91  ? 4537 GLU A CA    1 
ATOM   22076 C  C     . GLU A 1 4537 ? 244.733 239.548 189.869 1.00 29.32  ? 4537 GLU A C     1 
ATOM   22077 O  O     . GLU A 1 4537 ? 244.062 238.578 189.501 1.00 28.11  ? 4537 GLU A O     1 
ATOM   22078 C  CB    . GLU A 1 4537 ? 242.999 241.043 190.858 1.00 23.53  ? 4537 GLU A CB    1 
ATOM   22079 C  CG    . GLU A 1 4537 ? 242.890 241.599 189.454 1.00 27.01  ? 4537 GLU A CG    1 
ATOM   22080 C  CD    . GLU A 1 4537 ? 243.422 243.011 189.354 1.00 34.43  ? 4537 GLU A CD    1 
ATOM   22081 O  OE1   . GLU A 1 4537 ? 243.951 243.518 190.364 1.00 32.44  ? 4537 GLU A OE1   1 
ATOM   22082 O  OE2   . GLU A 1 4537 ? 243.314 243.613 188.266 1.00 37.50  ? 4537 GLU A OE2   1 
ATOM   22083 N  N     . GLU A 1 4538 ? 245.814 239.960 189.206 1.00 31.00  ? 4538 GLU A N     1 
ATOM   22084 C  CA    . GLU A 1 4538 ? 246.252 239.324 187.971 1.00 33.40  ? 4538 GLU A CA    1 
ATOM   22085 C  C     . GLU A 1 4538 ? 247.445 238.399 188.183 1.00 33.21  ? 4538 GLU A C     1 
ATOM   22086 O  O     . GLU A 1 4538 ? 248.246 238.206 187.263 1.00 38.16  ? 4538 GLU A O     1 
ATOM   22087 C  CB    . GLU A 1 4538 ? 246.579 240.381 186.917 1.00 36.52  ? 4538 GLU A CB    1 
ATOM   22088 C  CG    . GLU A 1 4538 ? 245.367 241.160 186.436 1.00 47.04  ? 4538 GLU A CG    1 
ATOM   22089 C  CD    . GLU A 1 4538 ? 245.721 242.212 185.406 1.00 62.68  ? 4538 GLU A CD    1 
ATOM   22090 O  OE1   . GLU A 1 4538 ? 246.928 242.421 185.158 1.00 66.63  ? 4538 GLU A OE1   1 
ATOM   22091 O  OE2   . GLU A 1 4538 ? 244.793 242.829 184.841 1.00 60.51  ? 4538 GLU A OE2   1 
ATOM   22092 N  N     . LEU A 1 4539 ? 247.576 237.819 189.372 1.00 29.99  ? 4539 LEU A N     1 
ATOM   22093 C  CA    . LEU A 1 4539 ? 248.674 236.920 189.695 1.00 25.13  ? 4539 LEU A CA    1 
ATOM   22094 C  C     . LEU A 1 4539 ? 248.136 235.516 189.938 1.00 27.88  ? 4539 LEU A C     1 
ATOM   22095 O  O     . LEU A 1 4539 ? 247.149 235.340 190.659 1.00 33.58  ? 4539 LEU A O     1 
ATOM   22096 C  CB    . LEU A 1 4539 ? 249.441 237.410 190.924 1.00 22.61  ? 4539 LEU A CB    1 
ATOM   22097 C  CG    . LEU A 1 4539 ? 250.244 238.698 190.738 1.00 24.93  ? 4539 LEU A CG    1 
ATOM   22098 C  CD1   . LEU A 1 4539 ? 251.205 238.897 191.894 1.00 19.96  ? 4539 LEU A CD1   1 
ATOM   22099 C  CD2   . LEU A 1 4539 ? 250.989 238.674 189.416 1.00 26.23  ? 4539 LEU A CD2   1 
ATOM   22100 N  N     . CYS A 1 4540 ? 248.787 234.527 189.334 1.00 27.49  ? 4540 CYS A N     1 
ATOM   22101 C  CA    . CYS A 1 4540 ? 248.456 233.127 189.529 1.00 28.10  ? 4540 CYS A CA    1 
ATOM   22102 C  C     . CYS A 1 4540 ? 249.667 232.389 190.086 1.00 22.57  ? 4540 CYS A C     1 
ATOM   22103 O  O     . CYS A 1 4540 ? 250.799 232.878 190.034 1.00 30.10  ? 4540 CYS A O     1 
ATOM   22104 C  CB    . CYS A 1 4540 ? 247.976 232.474 188.225 1.00 29.71  ? 4540 CYS A CB    1 
ATOM   22105 S  SG    . CYS A 1 4540 ? 249.204 232.405 186.909 1.00 55.07  ? 4540 CYS A SG    1 
ATOM   22106 N  N     . LEU A 1 4541 ? 249.413 231.203 190.627 1.00 17.05  ? 4541 LEU A N     1 
ATOM   22107 C  CA    . LEU A 1 4541 ? 250.407 230.448 191.372 1.00 19.48  ? 4541 LEU A CA    1 
ATOM   22108 C  C     . LEU A 1 4541 ? 250.869 229.236 190.575 1.00 20.02  ? 4541 LEU A C     1 
ATOM   22109 O  O     . LEU A 1 4541 ? 250.051 228.510 190.001 1.00 25.13  ? 4541 LEU A O     1 
ATOM   22110 C  CB    . LEU A 1 4541 ? 249.839 229.998 192.721 1.00 15.83  ? 4541 LEU A CB    1 
ATOM   22111 C  CG    . LEU A 1 4541 ? 250.845 229.464 193.738 1.00 15.12  ? 4541 LEU A CG    1 
ATOM   22112 C  CD1   . LEU A 1 4541 ? 251.950 230.481 193.957 1.00 15.88  ? 4541 LEU A CD1   1 
ATOM   22113 C  CD2   . LEU A 1 4541 ? 250.152 229.132 195.045 1.00 13.44  ? 4541 LEU A CD2   1 
ATOM   22114 N  N     . GLU A 1 4542 ? 252.182 229.021 190.543 1.00 17.63  ? 4542 GLU A N     1 
ATOM   22115 C  CA    . GLU A 1 4542 ? 252.783 227.849 189.928 1.00 18.70  ? 4542 GLU A CA    1 
ATOM   22116 C  C     . GLU A 1 4542 ? 253.590 227.100 190.977 1.00 22.02  ? 4542 GLU A C     1 
ATOM   22117 O  O     . GLU A 1 4542 ? 254.215 227.712 191.848 1.00 23.54  ? 4542 GLU A O     1 
ATOM   22118 C  CB    . GLU A 1 4542 ? 253.674 228.235 188.746 1.00 16.54  ? 4542 GLU A CB    1 
ATOM   22119 C  CG    . GLU A 1 4542 ? 252.911 228.785 187.554 1.00 25.45  ? 4542 GLU A CG    1 
ATOM   22120 C  CD    . GLU A 1 4542 ? 253.810 229.078 186.371 1.00 39.22  ? 4542 GLU A CD    1 
ATOM   22121 O  OE1   . GLU A 1 4542 ? 255.044 229.086 186.548 1.00 48.96  ? 4542 GLU A OE1   1 
ATOM   22122 O  OE2   . GLU A 1 4542 ? 253.281 229.301 185.263 1.00 38.44  ? 4542 GLU A OE2   1 
ATOM   22123 N  N     . VAL A 1 4543 ? 253.573 225.774 190.895 1.00 16.90  ? 4543 VAL A N     1 
ATOM   22124 C  CA    . VAL A 1 4543 ? 254.147 224.908 191.917 1.00 19.01  ? 4543 VAL A CA    1 
ATOM   22125 C  C     . VAL A 1 4543 ? 255.289 224.111 191.307 1.00 25.67  ? 4543 VAL A C     1 
ATOM   22126 O  O     . VAL A 1 4543 ? 255.127 223.492 190.249 1.00 34.47  ? 4543 VAL A O     1 
ATOM   22127 C  CB    . VAL A 1 4543 ? 253.080 223.978 192.514 1.00 23.44  ? 4543 VAL A CB    1 
ATOM   22128 C  CG1   . VAL A 1 4543 ? 253.705 223.009 193.494 1.00 26.01  ? 4543 VAL A CG1   1 
ATOM   22129 C  CG2   . VAL A 1 4543 ? 252.010 224.802 193.198 1.00 25.52  ? 4543 VAL A CG2   1 
ATOM   22130 N  N     . ASN A 1 4544 ? 256.442 224.132 191.971 1.00 22.67  ? 4544 ASN A N     1 
ATOM   22131 C  CA    . ASN A 1 4544 ? 257.608 223.372 191.533 1.00 24.18  ? 4544 ASN A CA    1 
ATOM   22132 C  C     . ASN A 1 4544 ? 258.151 222.574 192.709 1.00 28.73  ? 4544 ASN A C     1 
ATOM   22133 O  O     . ASN A 1 4544 ? 258.588 223.158 193.704 1.00 34.48  ? 4544 ASN A O     1 
ATOM   22134 C  CB    . ASN A 1 4544 ? 258.679 224.301 190.960 1.00 24.80  ? 4544 ASN A CB    1 
ATOM   22135 C  CG    . ASN A 1 4544 ? 259.956 223.575 190.609 1.00 26.59  ? 4544 ASN A CG    1 
ATOM   22136 O  OD1   . ASN A 1 4544 ? 261.047 224.007 190.976 1.00 39.33  ? 4544 ASN A OD1   1 
ATOM   22137 N  ND2   . ASN A 1 4544 ? 259.830 222.466 189.894 1.00 26.18  ? 4544 ASN A ND2   1 
ATOM   22138 N  N     . VAL A 1 4545 ? 258.135 221.251 192.600 1.00 25.07  ? 4545 VAL A N     1 
ATOM   22139 C  CA    . VAL A 1 4545 ? 258.568 220.386 193.693 1.00 24.81  ? 4545 VAL A CA    1 
ATOM   22140 C  C     . VAL A 1 4545 ? 260.029 220.014 193.480 1.00 29.66  ? 4545 VAL A C     1 
ATOM   22141 O  O     . VAL A 1 4545 ? 260.382 219.402 192.467 1.00 29.71  ? 4545 VAL A O     1 
ATOM   22142 C  CB    . VAL A 1 4545 ? 257.687 219.132 193.792 1.00 24.79  ? 4545 VAL A CB    1 
ATOM   22143 C  CG1   . VAL A 1 4545 ? 258.203 218.211 194.884 1.00 24.88  ? 4545 VAL A CG1   1 
ATOM   22144 C  CG2   . VAL A 1 4545 ? 256.245 219.523 194.062 1.00 18.52  ? 4545 VAL A CG2   1 
ATOM   22145 N  N     . THR A 1 4546 ? 260.882 220.389 194.435 1.00 40.50  ? 4546 THR A N     1 
ATOM   22146 C  CA    . THR A 1 4546 ? 262.305 220.084 194.385 1.00 42.20  ? 4546 THR A CA    1 
ATOM   22147 C  C     . THR A 1 4546 ? 262.780 219.653 195.765 1.00 46.32  ? 4546 THR A C     1 
ATOM   22148 O  O     . THR A 1 4546 ? 262.042 219.717 196.752 1.00 47.83  ? 4546 THR A O     1 
ATOM   22149 C  CB    . THR A 1 4546 ? 263.140 221.282 193.907 1.00 52.82  ? 4546 THR A CB    1 
ATOM   22150 O  OG1   . THR A 1 4546 ? 263.063 222.339 194.873 1.00 46.35  ? 4546 THR A OG1   1 
ATOM   22151 C  CG2   . THR A 1 4546 ? 262.666 221.786 192.553 1.00 46.83  ? 4546 THR A CG2   1 
ATOM   22152 N  N     . THR A 1 4547 ? 264.033 219.208 195.823 1.00 57.57  ? 4547 THR A N     1 
ATOM   22153 C  CA    . THR A 1 4547 ? 264.662 218.873 197.092 1.00 63.47  ? 4547 THR A CA    1 
ATOM   22154 C  C     . THR A 1 4547 ? 264.945 220.141 197.894 1.00 60.27  ? 4547 THR A C     1 
ATOM   22155 O  O     . THR A 1 4547 ? 265.202 221.211 197.336 1.00 61.27  ? 4547 THR A O     1 
ATOM   22156 C  CB    . THR A 1 4547 ? 265.960 218.098 196.858 1.00 62.37  ? 4547 THR A CB    1 
ATOM   22157 O  OG1   . THR A 1 4547 ? 265.756 217.123 195.827 1.00 61.08  ? 4547 THR A OG1   1 
ATOM   22158 C  CG2   . THR A 1 4547 ? 266.401 217.388 198.128 1.00 58.93  ? 4547 THR A CG2   1 
ATOM   22159 N  N     . SER A 1 4548 ? 264.884 220.011 199.222 1.00 51.38  ? 4548 SER A N     1 
ATOM   22160 C  CA    . SER A 1 4548 ? 265.054 221.175 200.087 1.00 63.02  ? 4548 SER A CA    1 
ATOM   22161 C  C     . SER A 1 4548 ? 266.445 221.780 199.948 1.00 70.51  ? 4548 SER A C     1 
ATOM   22162 O  O     . SER A 1 4548 ? 266.592 223.005 199.854 1.00 67.04  ? 4548 SER A O     1 
ATOM   22163 C  CB    . SER A 1 4548 ? 264.777 220.795 201.540 1.00 61.42  ? 4548 SER A CB    1 
ATOM   22164 O  OG    . SER A 1 4548 ? 264.827 221.934 202.381 1.00 51.88  ? 4548 SER A OG    1 
ATOM   22165 N  N     . GLN A 1 4549 ? 267.482 220.941 199.937 1.00 75.90  ? 4549 GLN A N     1 
ATOM   22166 C  CA    . GLN A 1 4549 ? 268.841 221.459 199.820 1.00 80.12  ? 4549 GLN A CA    1 
ATOM   22167 C  C     . GLN A 1 4549 ? 269.148 221.923 198.400 1.00 77.17  ? 4549 GLN A C     1 
ATOM   22168 O  O     . GLN A 1 4549 ? 269.761 222.980 198.210 1.00 76.67  ? 4549 GLN A O     1 
ATOM   22169 C  CB    . GLN A 1 4549 ? 269.850 220.401 200.265 1.00 76.26  ? 4549 GLN A CB    1 
ATOM   22170 C  CG    . GLN A 1 4549 ? 271.270 220.928 200.393 1.00 85.33  ? 4549 GLN A CG    1 
ATOM   22171 C  CD    . GLN A 1 4549 ? 271.342 222.219 201.185 1.00 82.82  ? 4549 GLN A CD    1 
ATOM   22172 O  OE1   . GLN A 1 4549 ? 271.716 223.266 200.656 1.00 83.17  ? 4549 GLN A OE1   1 
ATOM   22173 N  NE2   . GLN A 1 4549 ? 270.984 222.152 202.462 1.00 76.06  ? 4549 GLN A NE2   1 
ATOM   22174 N  N     . GLY A 1 4550 ? 268.734 221.154 197.398 1.00 72.37  ? 4550 GLY A N     1 
ATOM   22175 C  CA    . GLY A 1 4550 ? 269.004 221.508 196.018 1.00 79.77  ? 4550 GLY A CA    1 
ATOM   22176 C  C     . GLY A 1 4550 ? 267.914 222.345 195.382 1.00 83.14  ? 4550 GLY A C     1 
ATOM   22177 O  O     . GLY A 1 4550 ? 267.203 221.872 194.491 1.00 81.94  ? 4550 GLY A O     1 
ATOM   22178 N  N     . ALA A 1 4551 ? 267.772 223.592 195.826 1.00 84.16  ? 4551 ALA A N     1 
ATOM   22179 C  CA    . ALA A 1 4551 ? 266.752 224.476 195.284 1.00 77.41  ? 4551 ALA A CA    1 
ATOM   22180 C  C     . ALA A 1 4551 ? 267.248 225.912 195.336 1.00 77.41  ? 4551 ALA A C     1 
ATOM   22181 O  O     . ALA A 1 4551 ? 268.099 226.271 196.154 1.00 71.56  ? 4551 ALA A O     1 
ATOM   22182 C  CB    . ALA A 1 4551 ? 265.429 224.342 196.044 1.00 69.13  ? 4551 ALA A CB    1 
ATOM   22183 N  N     . THR A 1 4552 ? 266.700 226.734 194.441 1.00 77.26  ? 4552 THR A N     1 
ATOM   22184 C  CA    . THR A 1 4552 ? 266.997 228.159 194.380 1.00 73.99  ? 4552 THR A CA    1 
ATOM   22185 C  C     . THR A 1 4552 ? 265.689 228.925 194.276 1.00 59.47  ? 4552 THR A C     1 
ATOM   22186 O  O     . THR A 1 4552 ? 264.808 228.549 193.496 1.00 58.48  ? 4552 THR A O     1 
ATOM   22187 C  CB    . THR A 1 4552 ? 267.904 228.493 193.188 1.00 80.73  ? 4552 THR A CB    1 
ATOM   22188 O  OG1   . THR A 1 4552 ? 267.295 228.028 191.977 1.00 84.76  ? 4552 THR A OG1   1 
ATOM   22189 C  CG2   . THR A 1 4552 ? 269.269 227.841 193.349 1.00 69.73  ? 4552 THR A CG2   1 
ATOM   22190 N  N     . LEU A 1 4553 ? 265.564 229.994 195.057 1.00 47.05  ? 4553 LEU A N     1 
ATOM   22191 C  CA    . LEU A 1 4553 ? 264.360 230.816 195.084 1.00 46.14  ? 4553 LEU A CA    1 
ATOM   22192 C  C     . LEU A 1 4553 ? 264.649 232.147 194.404 1.00 42.12  ? 4553 LEU A C     1 
ATOM   22193 O  O     . LEU A 1 4553 ? 265.526 232.895 194.847 1.00 44.77  ? 4553 LEU A O     1 
ATOM   22194 C  CB    . LEU A 1 4553 ? 263.882 231.041 196.518 1.00 40.99  ? 4553 LEU A CB    1 
ATOM   22195 C  CG    . LEU A 1 4553 ? 263.542 229.801 197.346 1.00 38.24  ? 4553 LEU A CG    1 
ATOM   22196 C  CD1   . LEU A 1 4553 ? 262.940 230.204 198.681 1.00 34.24  ? 4553 LEU A CD1   1 
ATOM   22197 C  CD2   . LEU A 1 4553 ? 262.594 228.887 196.585 1.00 33.02  ? 4553 LEU A CD2   1 
ATOM   22198 N  N     . ASP A 1 4554 ? 263.910 232.440 193.337 1.00 36.63  ? 4554 ASP A N     1 
ATOM   22199 C  CA    . ASP A 1 4554 ? 264.041 233.717 192.651 1.00 40.47  ? 4554 ASP A CA    1 
ATOM   22200 C  C     . ASP A 1 4554 ? 263.157 234.751 193.348 1.00 40.21  ? 4554 ASP A C     1 
ATOM   22201 O  O     . ASP A 1 4554 ? 262.628 234.516 194.438 1.00 37.66  ? 4554 ASP A O     1 
ATOM   22202 C  CB    . ASP A 1 4554 ? 263.723 233.559 191.164 1.00 45.36  ? 4554 ASP A CB    1 
ATOM   22203 C  CG    . ASP A 1 4554 ? 262.291 233.116 190.902 1.00 45.71  ? 4554 ASP A CG    1 
ATOM   22204 O  OD1   . ASP A 1 4554 ? 261.536 232.883 191.866 1.00 43.31  ? 4554 ASP A OD1   1 
ATOM   22205 O  OD2   . ASP A 1 4554 ? 261.919 232.998 189.717 1.00 52.93  ? 4554 ASP A OD2   1 
ATOM   22206 N  N     . ALA A 1 4555 ? 262.976 235.911 192.717 1.00 41.00  ? 4555 ALA A N     1 
ATOM   22207 C  CA    . ALA A 1 4555 ? 262.234 237.002 193.336 1.00 39.41  ? 4555 ALA A CA    1 
ATOM   22208 C  C     . ALA A 1 4555 ? 260.761 236.680 193.553 1.00 36.70  ? 4555 ALA A C     1 
ATOM   22209 O  O     . ALA A 1 4555 ? 260.091 237.412 194.287 1.00 37.25  ? 4555 ALA A O     1 
ATOM   22210 C  CB    . ALA A 1 4555 ? 262.362 238.268 192.488 1.00 33.40  ? 4555 ALA A CB    1 
ATOM   22211 N  N     . CYS A 1 4556 ? 260.243 235.617 192.940 1.00 34.98  ? 4556 CYS A N     1 
ATOM   22212 C  CA    . CYS A 1 4556 ? 258.834 235.271 193.056 1.00 30.45  ? 4556 CYS A CA    1 
ATOM   22213 C  C     . CYS A 1 4556 ? 258.586 233.921 193.715 1.00 30.70  ? 4556 CYS A C     1 
ATOM   22214 O  O     . CYS A 1 4556 ? 257.423 233.555 193.913 1.00 31.64  ? 4556 CYS A O     1 
ATOM   22215 C  CB    . CYS A 1 4556 ? 258.173 235.287 191.671 1.00 33.70  ? 4556 CYS A CB    1 
ATOM   22216 S  SG    . CYS A 1 4556 ? 258.312 236.865 190.797 1.00 52.04  ? 4556 CYS A SG    1 
ATOM   22217 N  N     . SER A 1 4557 ? 259.631 233.178 194.067 1.00 28.50  ? 4557 SER A N     1 
ATOM   22218 C  CA    . SER A 1 4557 ? 259.485 231.834 194.608 1.00 24.19  ? 4557 SER A CA    1 
ATOM   22219 C  C     . SER A 1 4557 ? 259.558 231.851 196.129 1.00 27.53  ? 4557 SER A C     1 
ATOM   22220 O  O     . SER A 1 4557 ? 260.419 232.512 196.716 1.00 27.70  ? 4557 SER A O     1 
ATOM   22221 C  CB    . SER A 1 4557 ? 260.562 230.901 194.053 1.00 30.71  ? 4557 SER A CB    1 
ATOM   22222 O  OG    . SER A 1 4557 ? 260.345 230.630 192.681 1.00 36.43  ? 4557 SER A OG    1 
ATOM   22223 N  N     . PHE A 1 4558 ? 258.645 231.118 196.759 1.00 24.37  ? 4558 PHE A N     1 
ATOM   22224 C  CA    . PHE A 1 4558 ? 258.624 230.934 198.202 1.00 20.29  ? 4558 PHE A CA    1 
ATOM   22225 C  C     . PHE A 1 4558 ? 258.662 229.448 198.523 1.00 22.05  ? 4558 PHE A C     1 
ATOM   22226 O  O     . PHE A 1 4558 ? 258.011 228.641 197.852 1.00 25.07  ? 4558 PHE A O     1 
ATOM   22227 C  CB    . PHE A 1 4558 ? 257.388 231.582 198.827 1.00 15.07  ? 4558 PHE A CB    1 
ATOM   22228 C  CG    . PHE A 1 4558 ? 257.350 233.074 198.683 1.00 17.36  ? 4558 PHE A CG    1 
ATOM   22229 C  CD1   . PHE A 1 4558 ? 256.882 233.659 197.521 1.00 17.65  ? 4558 PHE A CD1   1 
ATOM   22230 C  CD2   . PHE A 1 4558 ? 257.794 233.891 199.706 1.00 19.24  ? 4558 PHE A CD2   1 
ATOM   22231 C  CE1   . PHE A 1 4558 ? 256.851 235.031 197.387 1.00 16.43  ? 4558 PHE A CE1   1 
ATOM   22232 C  CE2   . PHE A 1 4558 ? 257.763 235.262 199.577 1.00 19.69  ? 4558 PHE A CE2   1 
ATOM   22233 C  CZ    . PHE A 1 4558 ? 257.291 235.832 198.415 1.00 19.22  ? 4558 PHE A CZ    1 
ATOM   22234 N  N     . GLY A 1 4559 ? 259.429 229.092 199.551 1.00 21.98  ? 4559 GLY A N     1 
ATOM   22235 C  CA    . GLY A 1 4559 ? 259.612 227.699 199.922 1.00 16.26  ? 4559 GLY A CA    1 
ATOM   22236 C  C     . GLY A 1 4559 ? 258.622 227.254 200.986 1.00 18.04  ? 4559 GLY A C     1 
ATOM   22237 O  O     . GLY A 1 4559 ? 258.349 227.974 201.944 1.00 22.35  ? 4559 GLY A O     1 
ATOM   22238 N  N     . VAL A 1 4560 ? 258.088 226.050 200.798 1.00 20.43  ? 4560 VAL A N     1 
ATOM   22239 C  CA    . VAL A 1 4560 ? 257.107 225.457 201.696 1.00 14.81  ? 4560 VAL A CA    1 
ATOM   22240 C  C     . VAL A 1 4560 ? 257.529 224.020 201.972 1.00 22.77  ? 4560 VAL A C     1 
ATOM   22241 O  O     . VAL A 1 4560 ? 257.929 223.299 201.052 1.00 25.40  ? 4560 VAL A O     1 
ATOM   22242 C  CB    . VAL A 1 4560 ? 255.686 225.504 201.097 1.00 13.15  ? 4560 VAL A CB    1 
ATOM   22243 C  CG1   . VAL A 1 4560 ? 254.731 224.643 201.903 1.00 19.80  ? 4560 VAL A CG1   1 
ATOM   22244 C  CG2   . VAL A 1 4560 ? 255.186 226.936 201.027 1.00 16.69  ? 4560 VAL A CG2   1 
ATOM   22245 N  N     . THR A 1 4561 ? 257.457 223.612 203.236 1.00 19.94  ? 4561 THR A N     1 
ATOM   22246 C  CA    . THR A 1 4561 ? 257.781 222.254 203.641 1.00 17.15  ? 4561 THR A CA    1 
ATOM   22247 C  C     . THR A 1 4561 ? 256.590 221.631 204.357 1.00 19.49  ? 4561 THR A C     1 
ATOM   22248 O  O     . THR A 1 4561 ? 255.694 222.328 204.841 1.00 23.25  ? 4561 THR A O     1 
ATOM   22249 C  CB    . THR A 1 4561 ? 259.016 222.215 204.553 1.00 17.71  ? 4561 THR A CB    1 
ATOM   22250 O  OG1   . THR A 1 4561 ? 258.731 222.899 205.779 1.00 23.48  ? 4561 THR A OG1   1 
ATOM   22251 C  CG2   . THR A 1 4561 ? 260.205 222.876 203.875 1.00 21.99  ? 4561 THR A CG2   1 
ATOM   22252 N  N     . GLY A 1 4562 ? 256.587 220.302 204.415 1.00 18.95  ? 4562 GLY A N     1 
ATOM   22253 C  CA    . GLY A 1 4562 ? 255.558 219.568 205.117 1.00 12.87  ? 4562 GLY A CA    1 
ATOM   22254 C  C     . GLY A 1 4562 ? 254.356 219.165 204.292 1.00 14.28  ? 4562 GLY A C     1 
ATOM   22255 O  O     . GLY A 1 4562 ? 253.464 218.493 204.822 1.00 19.92  ? 4562 GLY A O     1 
ATOM   22256 N  N     . LEU A 1 4563 ? 254.295 219.556 203.022 1.00 16.61  ? 4563 LEU A N     1 
ATOM   22257 C  CA    . LEU A 1 4563 ? 253.189 219.143 202.170 1.00 12.73  ? 4563 LEU A CA    1 
ATOM   22258 C  C     . LEU A 1 4563 ? 253.271 217.650 201.879 1.00 14.01  ? 4563 LEU A C     1 
ATOM   22259 O  O     . LEU A 1 4563 ? 254.346 217.113 201.600 1.00 14.87  ? 4563 LEU A O     1 
ATOM   22260 C  CB    . LEU A 1 4563 ? 253.198 219.934 200.862 1.00 12.05  ? 4563 LEU A CB    1 
ATOM   22261 C  CG    . LEU A 1 4563 ? 253.006 221.449 200.951 1.00 13.33  ? 4563 LEU A CG    1 
ATOM   22262 C  CD1   . LEU A 1 4563 ? 252.606 222.011 199.599 1.00 17.45  ? 4563 LEU A CD1   1 
ATOM   22263 C  CD2   . LEU A 1 4563 ? 251.972 221.806 202.004 1.00 16.46  ? 4563 LEU A CD2   1 
ATOM   22264 N  N     . LYS A 1 4564 ? 252.124 216.979 201.945 1.00 15.53  ? 4564 LYS A N     1 
ATOM   22265 C  CA    . LYS A 1 4564 ? 252.035 215.543 201.720 1.00 14.48  ? 4564 LYS A CA    1 
ATOM   22266 C  C     . LYS A 1 4564 ? 251.084 215.272 200.565 1.00 15.15  ? 4564 LYS A C     1 
ATOM   22267 O  O     . LYS A 1 4564 ? 249.941 215.732 200.580 1.00 17.38  ? 4564 LYS A O     1 
ATOM   22268 C  CB    . LYS A 1 4564 ? 251.553 214.820 202.981 1.00 14.43  ? 4564 LYS A CB    1 
ATOM   22269 C  CG    . LYS A 1 4564 ? 252.388 215.100 204.219 1.00 12.06  ? 4564 LYS A CG    1 
ATOM   22270 C  CD    . LYS A 1 4564 ? 253.699 214.341 204.184 1.00 15.57  ? 4564 LYS A CD    1 
ATOM   22271 C  CE    . LYS A 1 4564 ? 254.410 214.403 205.525 1.00 20.29  ? 4564 LYS A CE    1 
ATOM   22272 N  NZ    . LYS A 1 4564 ? 254.774 215.796 205.898 1.00 14.62  ? 4564 LYS A NZ    1 
ATOM   22273 N  N     . LEU A 1 4565 ? 251.553 214.519 199.575 1.00 12.76  ? 4565 LEU A N     1 
ATOM   22274 C  CA    . LEU A 1 4565 ? 250.743 214.162 198.416 1.00 11.95  ? 4565 LEU A CA    1 
ATOM   22275 C  C     . LEU A 1 4565 ? 250.071 212.819 198.678 1.00 13.74  ? 4565 LEU A C     1 
ATOM   22276 O  O     . LEU A 1 4565 ? 250.753 211.818 198.916 1.00 20.22  ? 4565 LEU A O     1 
ATOM   22277 C  CB    . LEU A 1 4565 ? 251.610 214.099 197.162 1.00 11.87  ? 4565 LEU A CB    1 
ATOM   22278 C  CG    . LEU A 1 4565 ? 250.913 213.882 195.821 1.00 12.12  ? 4565 LEU A CG    1 
ATOM   22279 C  CD1   . LEU A 1 4565 ? 249.842 214.932 195.595 1.00 12.04  ? 4565 LEU A CD1   1 
ATOM   22280 C  CD2   . LEU A 1 4565 ? 251.936 213.910 194.704 1.00 15.57  ? 4565 LEU A CD2   1 
ATOM   22281 N  N     . GLN A 1 4566 ? 248.741 212.796 198.633 1.00 12.82  ? 4566 GLN A N     1 
ATOM   22282 C  CA    . GLN A 1 4566 ? 247.977 211.607 198.983 1.00 11.67  ? 4566 GLN A CA    1 
ATOM   22283 C  C     . GLN A 1 4566 ? 247.721 210.773 197.733 1.00 12.18  ? 4566 GLN A C     1 
ATOM   22284 O  O     . GLN A 1 4566 ? 247.105 211.253 196.777 1.00 12.07  ? 4566 GLN A O     1 
ATOM   22285 C  CB    . GLN A 1 4566 ? 246.659 211.996 199.647 1.00 12.09  ? 4566 GLN A CB    1 
ATOM   22286 C  CG    . GLN A 1 4566 ? 246.813 212.965 200.805 1.00 13.14  ? 4566 GLN A CG    1 
ATOM   22287 C  CD    . GLN A 1 4566 ? 247.567 212.363 201.972 1.00 14.43  ? 4566 GLN A CD    1 
ATOM   22288 O  OE1   . GLN A 1 4566 ? 248.628 212.851 202.357 1.00 13.44  ? 4566 GLN A OE1   1 
ATOM   22289 N  NE2   . GLN A 1 4566 ? 247.019 211.299 202.545 1.00 21.21  ? 4566 GLN A NE2   1 
ATOM   22290 N  N     . GLY A 1 4567 ? 248.193 209.529 197.746 1.00 18.45  ? 4567 GLY A N     1 
ATOM   22291 C  CA    . GLY A 1 4567 ? 247.918 208.616 196.656 1.00 16.95  ? 4567 GLY A CA    1 
ATOM   22292 C  C     . GLY A 1 4567 ? 248.673 208.887 195.377 1.00 16.00  ? 4567 GLY A C     1 
ATOM   22293 O  O     . GLY A 1 4567 ? 248.275 208.389 194.321 1.00 21.17  ? 4567 GLY A O     1 
ATOM   22294 N  N     . ALA A 1 4568 ? 249.754 209.659 195.435 1.00 14.41  ? 4568 ALA A N     1 
ATOM   22295 C  CA    . ALA A 1 4568 ? 250.540 209.939 194.243 1.00 15.08  ? 4568 ALA A CA    1 
ATOM   22296 C  C     . ALA A 1 4568 ? 251.966 210.268 194.653 1.00 17.71  ? 4568 ALA A C     1 
ATOM   22297 O  O     . ALA A 1 4568 ? 252.235 210.643 195.796 1.00 21.32  ? 4568 ALA A O     1 
ATOM   22298 C  CB    . ALA A 1 4568 ? 249.934 211.083 193.425 1.00 14.28  ? 4568 ALA A CB    1 
ATOM   22299 N  N     . THR A 1 4569 ? 252.876 210.118 193.697 1.00 19.07  ? 4569 THR A N     1 
ATOM   22300 C  CA    . THR A 1 4569 ? 254.286 210.428 193.877 1.00 21.86  ? 4569 THR A CA    1 
ATOM   22301 C  C     . THR A 1 4569 ? 254.711 211.454 192.836 1.00 21.02  ? 4569 THR A C     1 
ATOM   22302 O  O     . THR A 1 4569 ? 254.211 211.452 191.707 1.00 24.93  ? 4569 THR A O     1 
ATOM   22303 C  CB    . THR A 1 4569 ? 255.160 209.176 193.756 1.00 22.44  ? 4569 THR A CB    1 
ATOM   22304 O  OG1   . THR A 1 4569 ? 254.854 208.491 192.536 1.00 25.74  ? 4569 THR A OG1   1 
ATOM   22305 C  CG2   . THR A 1 4569 ? 254.920 208.244 194.931 1.00 20.61  ? 4569 THR A CG2   1 
ATOM   22306 N  N     . CYS A 1 4570 ? 255.631 212.331 193.223 1.00 25.11  ? 4570 CYS A N     1 
ATOM   22307 C  CA    . CYS A 1 4570 ? 256.109 213.405 192.363 1.00 25.22  ? 4570 CYS A CA    1 
ATOM   22308 C  C     . CYS A 1 4570 ? 257.552 213.125 191.967 1.00 32.05  ? 4570 CYS A C     1 
ATOM   22309 O  O     . CYS A 1 4570 ? 258.430 213.034 192.831 1.00 34.40  ? 4570 CYS A O     1 
ATOM   22310 C  CB    . CYS A 1 4570 ? 255.995 214.758 193.064 1.00 26.51  ? 4570 CYS A CB    1 
ATOM   22311 S  SG    . CYS A 1 4570 ? 256.129 216.182 191.966 1.00 37.05  ? 4570 CYS A SG    1 
ATOM   22312 N  N     . ASN A 1 4571 ? 257.788 212.988 190.666 1.00 35.34  ? 4571 ASN A N     1 
ATOM   22313 C  CA    . ASN A 1 4571 ? 259.126 212.844 190.112 1.00 32.21  ? 4571 ASN A CA    1 
ATOM   22314 C  C     . ASN A 1 4571 ? 259.288 213.843 188.978 1.00 32.77  ? 4571 ASN A C     1 
ATOM   22315 O  O     . ASN A 1 4571 ? 258.460 213.881 188.062 1.00 34.70  ? 4571 ASN A O     1 
ATOM   22316 C  CB    . ASN A 1 4571 ? 259.375 211.419 189.608 1.00 35.52  ? 4571 ASN A CB    1 
ATOM   22317 C  CG    . ASN A 1 4571 ? 260.827 211.175 189.246 1.00 46.51  ? 4571 ASN A CG    1 
ATOM   22318 O  OD1   . ASN A 1 4571 ? 261.735 211.574 189.974 1.00 50.97  ? 4571 ASN A OD1   1 
ATOM   22319 N  ND2   . ASN A 1 4571 ? 261.052 210.515 188.117 1.00 39.98  ? 4571 ASN A ND2   1 
ATOM   22320 N  N     . ASN A 1 4572 ? 260.351 214.645 189.044 1.00 32.39  ? 4572 ASN A N     1 
ATOM   22321 C  CA    . ASN A 1 4572 ? 260.623 215.679 188.045 1.00 35.95  ? 4572 ASN A CA    1 
ATOM   22322 C  C     . ASN A 1 4572 ? 259.415 216.594 187.861 1.00 33.97  ? 4572 ASN A C     1 
ATOM   22323 O  O     . ASN A 1 4572 ? 259.057 216.972 186.743 1.00 31.17  ? 4572 ASN A O     1 
ATOM   22324 C  CB    . ASN A 1 4572 ? 261.051 215.060 186.713 1.00 42.59  ? 4572 ASN A CB    1 
ATOM   22325 C  CG    . ASN A 1 4572 ? 261.931 215.984 185.898 1.00 46.95  ? 4572 ASN A CG    1 
ATOM   22326 O  OD1   . ASN A 1 4572 ? 261.954 217.194 186.119 1.00 55.78  ? 4572 ASN A OD1   1 
ATOM   22327 N  ND2   . ASN A 1 4572 ? 262.662 215.418 184.946 1.00 51.31  ? 4572 ASN A ND2   1 
ATOM   22328 N  N     . ASN A 1 4573 ? 258.779 216.943 188.980 1.00 35.14  ? 4573 ASN A N     1 
ATOM   22329 C  CA    . ASN A 1 4573 ? 257.601 217.810 188.999 1.00 29.90  ? 4573 ASN A CA    1 
ATOM   22330 C  C     . ASN A 1 4573 ? 256.453 217.225 188.181 1.00 33.32  ? 4573 ASN A C     1 
ATOM   22331 O  O     . ASN A 1 4573 ? 255.655 217.960 187.595 1.00 33.27  ? 4573 ASN A O     1 
ATOM   22332 C  CB    . ASN A 1 4573 ? 257.945 219.223 188.515 1.00 28.76  ? 4573 ASN A CB    1 
ATOM   22333 C  CG    . ASN A 1 4573 ? 257.133 220.291 189.213 1.00 28.38  ? 4573 ASN A CG    1 
ATOM   22334 O  OD1   . ASN A 1 4573 ? 257.093 220.351 190.441 1.00 32.84  ? 4573 ASN A OD1   1 
ATOM   22335 N  ND2   . ASN A 1 4573 ? 256.484 221.147 188.434 1.00 27.64  ? 4573 ASN A ND2   1 
ATOM   22336 N  N     . LYS A 1 4574 ? 256.362 215.897 188.134 1.00 36.12  ? 4574 LYS A N     1 
ATOM   22337 C  CA    . LYS A 1 4574 ? 255.283 215.203 187.444 1.00 28.36  ? 4574 LYS A CA    1 
ATOM   22338 C  C     . LYS A 1 4574 ? 254.693 214.148 188.366 1.00 30.51  ? 4574 LYS A C     1 
ATOM   22339 O  O     . LYS A 1 4574 ? 255.424 213.455 189.077 1.00 29.77  ? 4574 LYS A O     1 
ATOM   22340 C  CB    . LYS A 1 4574 ? 255.775 214.561 186.145 1.00 29.72  ? 4574 LYS A CB    1 
ATOM   22341 C  CG    . LYS A 1 4574 ? 256.206 215.567 185.092 1.00 32.38  ? 4574 LYS A CG    1 
ATOM   22342 C  CD    . LYS A 1 4574 ? 256.595 214.884 183.795 1.00 35.77  ? 4574 LYS A CD    1 
ATOM   22343 C  CE    . LYS A 1 4574 ? 257.091 215.892 182.775 1.00 40.05  ? 4574 LYS A CE    1 
ATOM   22344 N  NZ    . LYS A 1 4574 ? 256.150 217.034 182.627 1.00 44.92  ? 4574 LYS A NZ    1 
ATOM   22345 N  N     . LEU A 1 4575 ? 253.368 214.026 188.346 1.00 31.90  ? 4575 LEU A N     1 
ATOM   22346 C  CA    . LEU A 1 4575 ? 252.649 213.172 189.281 1.00 22.22  ? 4575 LEU A CA    1 
ATOM   22347 C  C     . LEU A 1 4575 ? 252.331 211.822 188.656 1.00 24.13  ? 4575 LEU A C     1 
ATOM   22348 O  O     . LEU A 1 4575 ? 251.933 211.740 187.490 1.00 28.95  ? 4575 LEU A O     1 
ATOM   22349 C  CB    . LEU A 1 4575 ? 251.352 213.839 189.743 1.00 22.51  ? 4575 LEU A CB    1 
ATOM   22350 C  CG    . LEU A 1 4575 ? 251.467 215.182 190.466 1.00 23.17  ? 4575 LEU A CG    1 
ATOM   22351 C  CD1   . LEU A 1 4575 ? 250.194 215.460 191.239 1.00 25.29  ? 4575 LEU A CD1   1 
ATOM   22352 C  CD2   . LEU A 1 4575 ? 252.670 215.208 191.387 1.00 20.92  ? 4575 LEU A CD2   1 
ATOM   22353 N  N     . SER A 1 4576 ? 252.507 210.764 189.445 1.00 26.36  ? 4576 SER A N     1 
ATOM   22354 C  CA    . SER A 1 4576 ? 252.158 209.409 189.042 1.00 22.46  ? 4576 SER A CA    1 
ATOM   22355 C  C     . SER A 1 4576 ? 251.396 208.732 190.170 1.00 22.86  ? 4576 SER A C     1 
ATOM   22356 O  O     . SER A 1 4576 ? 251.726 208.911 191.345 1.00 29.35  ? 4576 SER A O     1 
ATOM   22357 C  CB    . SER A 1 4576 ? 253.403 208.589 188.687 1.00 24.52  ? 4576 SER A CB    1 
ATOM   22358 O  OG    . SER A 1 4576 ? 254.124 209.185 187.624 1.00 33.85  ? 4576 SER A OG    1 
ATOM   22359 N  N     . LEU A 1 4577 ? 250.381 207.952 189.810 1.00 23.84  ? 4577 LEU A N     1 
ATOM   22360 C  CA    . LEU A 1 4577 ? 249.586 207.254 190.811 1.00 19.33  ? 4577 LEU A CA    1 
ATOM   22361 C  C     . LEU A 1 4577 ? 250.440 206.235 191.554 1.00 19.42  ? 4577 LEU A C     1 
ATOM   22362 O  O     . LEU A 1 4577 ? 251.262 205.533 190.959 1.00 26.35  ? 4577 LEU A O     1 
ATOM   22363 C  CB    . LEU A 1 4577 ? 248.396 206.559 190.154 1.00 19.37  ? 4577 LEU A CB    1 
ATOM   22364 C  CG    . LEU A 1 4577 ? 247.282 207.464 189.635 1.00 17.23  ? 4577 LEU A CG    1 
ATOM   22365 C  CD1   . LEU A 1 4577 ? 246.245 206.644 188.897 1.00 17.52  ? 4577 LEU A CD1   1 
ATOM   22366 C  CD2   . LEU A 1 4577 ? 246.647 208.242 190.772 1.00 17.41  ? 4577 LEU A CD2   1 
ATOM   22367 N  N     . SER A 1 4578 ? 250.239 206.154 192.868 1.00 17.15  ? 4578 SER A N     1 
ATOM   22368 C  CA    . SER A 1 4578 ? 251.002 205.248 193.712 1.00 21.81  ? 4578 SER A CA    1 
ATOM   22369 C  C     . SER A 1 4578 ? 250.067 204.555 194.690 1.00 27.47  ? 4578 SER A C     1 
ATOM   22370 O  O     . SER A 1 4578 ? 248.973 205.040 194.989 1.00 31.38  ? 4578 SER A O     1 
ATOM   22371 C  CB    . SER A 1 4578 ? 252.108 205.983 194.478 1.00 22.10  ? 4578 SER A CB    1 
ATOM   22372 O  OG    . SER A 1 4578 ? 251.574 206.709 195.570 1.00 21.49  ? 4578 SER A OG    1 
ATOM   22373 N  N     . ASN A 1 4579 ? 250.513 203.405 195.186 1.00 28.16  ? 4579 ASN A N     1 
ATOM   22374 C  CA    . ASN A 1 4579 ? 249.762 202.642 196.172 1.00 25.16  ? 4579 ASN A CA    1 
ATOM   22375 C  C     . ASN A 1 4579 ? 250.108 203.024 197.604 1.00 24.23  ? 4579 ASN A C     1 
ATOM   22376 O  O     . ASN A 1 4579 ? 249.588 202.407 198.538 1.00 30.53  ? 4579 ASN A O     1 
ATOM   22377 C  CB    . ASN A 1 4579 ? 249.993 201.143 195.964 1.00 27.66  ? 4579 ASN A CB    1 
ATOM   22378 C  CG    . ASN A 1 4579 ? 249.291 200.615 194.729 1.00 37.39  ? 4579 ASN A CG    1 
ATOM   22379 O  OD1   . ASN A 1 4579 ? 249.916 200.012 193.856 1.00 40.94  ? 4579 ASN A OD1   1 
ATOM   22380 N  ND2   . ASN A 1 4579 ? 247.986 200.846 194.646 1.00 35.88  ? 4579 ASN A ND2   1 
ATOM   22381 N  N     . ALA A 1 4580 ? 250.975 204.013 197.797 1.00 23.09  ? 4580 ALA A N     1 
ATOM   22382 C  CA    . ALA A 1 4580 ? 251.289 204.503 199.129 1.00 18.70  ? 4580 ALA A CA    1 
ATOM   22383 C  C     . ALA A 1 4580 ? 250.210 205.465 199.611 1.00 23.06  ? 4580 ALA A C     1 
ATOM   22384 O  O     . ALA A 1 4580 ? 249.564 206.156 198.818 1.00 28.62  ? 4580 ALA A O     1 
ATOM   22385 C  CB    . ALA A 1 4580 ? 252.651 205.197 199.140 1.00 18.72  ? 4580 ALA A CB    1 
ATOM   22386 N  N     . ILE A 1 4581 ? 250.013 205.498 200.929 1.00 23.89  ? 4581 ILE A N     1 
ATOM   22387 C  CA    . ILE A 1 4581 ? 248.995 206.370 201.510 1.00 24.99  ? 4581 ILE A CA    1 
ATOM   22388 C  C     . ILE A 1 4581 ? 249.354 207.833 201.281 1.00 28.33  ? 4581 ILE A C     1 
ATOM   22389 O  O     . ILE A 1 4581 ? 248.510 208.645 200.883 1.00 24.54  ? 4581 ILE A O     1 
ATOM   22390 C  CB    . ILE A 1 4581 ? 248.813 206.059 203.006 1.00 28.88  ? 4581 ILE A CB    1 
ATOM   22391 C  CG1   . ILE A 1 4581 ? 248.091 204.722 203.188 1.00 26.96  ? 4581 ILE A CG1   1 
ATOM   22392 C  CG2   . ILE A 1 4581 ? 248.054 207.180 203.700 1.00 28.41  ? 4581 ILE A CG2   1 
ATOM   22393 C  CD1   . ILE A 1 4581 ? 246.660 204.734 202.707 1.00 20.98  ? 4581 ILE A CD1   1 
ATOM   22394 N  N     . SER A 1 4582 ? 250.612 208.191 201.524 1.00 28.14  ? 4582 SER A N     1 
ATOM   22395 C  CA    . SER A 1 4582 ? 251.059 209.564 201.354 1.00 20.58  ? 4582 SER A CA    1 
ATOM   22396 C  C     . SER A 1 4582 ? 252.546 209.576 201.042 1.00 25.50  ? 4582 SER A C     1 
ATOM   22397 O  O     . SER A 1 4582 ? 253.292 208.684 201.453 1.00 34.06  ? 4582 SER A O     1 
ATOM   22398 C  CB    . SER A 1 4582 ? 250.776 210.409 202.601 1.00 24.72  ? 4582 SER A CB    1 
ATOM   22399 O  OG    . SER A 1 4582 ? 251.476 209.911 203.726 1.00 31.73  ? 4582 SER A OG    1 
ATOM   22400 N  N     . THR A 1 4583 ? 252.965 210.602 200.306 1.00 22.85  ? 4583 THR A N     1 
ATOM   22401 C  CA    . THR A 1 4583 ? 254.358 210.813 199.948 1.00 21.78  ? 4583 THR A CA    1 
ATOM   22402 C  C     . THR A 1 4583 ? 254.764 212.211 200.389 1.00 23.30  ? 4583 THR A C     1 
ATOM   22403 O  O     . THR A 1 4583 ? 254.057 213.184 200.111 1.00 20.47  ? 4583 THR A O     1 
ATOM   22404 C  CB    . THR A 1 4583 ? 254.573 210.642 198.439 1.00 19.77  ? 4583 THR A CB    1 
ATOM   22405 O  OG1   . THR A 1 4583 ? 254.506 209.251 198.103 1.00 20.00  ? 4583 THR A OG1   1 
ATOM   22406 C  CG2   . THR A 1 4583 ? 255.928 211.190 198.023 1.00 20.25  ? 4583 THR A CG2   1 
ATOM   22407 N  N     . ALA A 1 4584 ? 255.895 212.309 201.081 1.00 29.81  ? 4584 ALA A N     1 
ATOM   22408 C  CA    . ALA A 1 4584 ? 256.355 213.588 201.604 1.00 23.91  ? 4584 ALA A CA    1 
ATOM   22409 C  C     . ALA A 1 4584 ? 257.061 214.375 200.507 1.00 24.98  ? 4584 ALA A C     1 
ATOM   22410 O  O     . ALA A 1 4584 ? 258.101 213.944 199.996 1.00 26.19  ? 4584 ALA A O     1 
ATOM   22411 C  CB    . ALA A 1 4584 ? 257.285 213.370 202.796 1.00 23.75  ? 4584 ALA A CB    1 
ATOM   22412 N  N     . LEU A 1 4585 ? 256.498 215.521 200.145 1.00 23.61  ? 4585 LEU A N     1 
ATOM   22413 C  CA    . LEU A 1 4585 ? 257.150 216.413 199.195 1.00 21.42  ? 4585 LEU A CA    1 
ATOM   22414 C  C     . LEU A 1 4585 ? 258.282 217.150 199.898 1.00 28.00  ? 4585 LEU A C     1 
ATOM   22415 O  O     . LEU A 1 4585 ? 258.030 217.847 200.888 1.00 33.28  ? 4585 LEU A O     1 
ATOM   22416 C  CB    . LEU A 1 4585 ? 256.150 217.405 198.620 1.00 21.54  ? 4585 LEU A CB    1 
ATOM   22417 C  CG    . LEU A 1 4585 ? 254.978 216.810 197.840 1.00 16.25  ? 4585 LEU A CG    1 
ATOM   22418 C  CD1   . LEU A 1 4585 ? 254.005 217.895 197.418 1.00 10.91  ? 4585 LEU A CD1   1 
ATOM   22419 C  CD2   . LEU A 1 4585 ? 255.483 216.049 196.629 1.00 20.60  ? 4585 LEU A CD2   1 
ATOM   22420 N  N     . PRO A 1 4586 ? 259.530 217.023 199.435 1.00 28.66  ? 4586 PRO A N     1 
ATOM   22421 C  CA    . PRO A 1 4586 ? 260.656 217.628 200.162 1.00 32.37  ? 4586 PRO A CA    1 
ATOM   22422 C  C     . PRO A 1 4586 ? 260.536 219.137 200.307 1.00 32.42  ? 4586 PRO A C     1 
ATOM   22423 O  O     . PRO A 1 4586 ? 260.505 219.658 201.425 1.00 34.90  ? 4586 PRO A O     1 
ATOM   22424 C  CB    . PRO A 1 4586 ? 261.875 217.242 199.312 1.00 34.14  ? 4586 PRO A CB    1 
ATOM   22425 C  CG    . PRO A 1 4586 ? 261.324 216.839 197.983 1.00 33.84  ? 4586 PRO A CG    1 
ATOM   22426 C  CD    . PRO A 1 4586 ? 259.964 216.288 198.238 1.00 26.79  ? 4586 PRO A CD    1 
ATOM   22427 N  N     . LEU A 1 4587 ? 260.457 219.847 199.185 1.00 32.38  ? 4587 LEU A N     1 
ATOM   22428 C  CA    . LEU A 1 4587 ? 260.294 221.291 199.196 1.00 27.16  ? 4587 LEU A CA    1 
ATOM   22429 C  C     . LEU A 1 4587 ? 259.418 221.702 198.025 1.00 29.61  ? 4587 LEU A C     1 
ATOM   22430 O  O     . LEU A 1 4587 ? 259.576 221.194 196.911 1.00 35.03  ? 4587 LEU A O     1 
ATOM   22431 C  CB    . LEU A 1 4587 ? 261.645 222.013 199.121 1.00 34.52  ? 4587 LEU A CB    1 
ATOM   22432 C  CG    . LEU A 1 4587 ? 261.601 223.541 199.113 1.00 32.28  ? 4587 LEU A CG    1 
ATOM   22433 C  CD1   . LEU A 1 4587 ? 261.206 224.076 200.477 1.00 29.86  ? 4587 LEU A CD1   1 
ATOM   22434 C  CD2   . LEU A 1 4587 ? 262.938 224.109 198.683 1.00 30.58  ? 4587 LEU A CD2   1 
ATOM   22435 N  N     . THR A 1 4588 ? 258.489 222.617 198.285 1.00 24.59  ? 4588 THR A N     1 
ATOM   22436 C  CA    . THR A 1 4588 ? 257.574 223.122 197.274 1.00 21.78  ? 4588 THR A CA    1 
ATOM   22437 C  C     . THR A 1 4588 ? 257.846 224.602 197.059 1.00 26.69  ? 4588 THR A C     1 
ATOM   22438 O  O     . THR A 1 4588 ? 257.866 225.379 198.016 1.00 25.35  ? 4588 THR A O     1 
ATOM   22439 C  CB    . THR A 1 4588 ? 256.119 222.903 197.694 1.00 21.28  ? 4588 THR A CB    1 
ATOM   22440 O  OG1   . THR A 1 4588 ? 255.861 221.499 197.821 1.00 30.19  ? 4588 THR A OG1   1 
ATOM   22441 C  CG2   . THR A 1 4588 ? 255.176 223.492 196.671 1.00 23.04  ? 4588 THR A CG2   1 
ATOM   22442 N  N     . GLN A 1 4589 ? 258.061 224.988 195.807 1.00 28.57  ? 4589 GLN A N     1 
ATOM   22443 C  CA    . GLN A 1 4589 ? 258.276 226.378 195.436 1.00 23.92  ? 4589 GLN A CA    1 
ATOM   22444 C  C     . GLN A 1 4589 ? 256.972 226.913 194.862 1.00 22.02  ? 4589 GLN A C     1 
ATOM   22445 O  O     . GLN A 1 4589 ? 256.504 226.439 193.820 1.00 31.02  ? 4589 GLN A O     1 
ATOM   22446 C  CB    . GLN A 1 4589 ? 259.413 226.503 194.426 1.00 27.13  ? 4589 GLN A CB    1 
ATOM   22447 C  CG    . GLN A 1 4589 ? 260.752 226.004 194.929 1.00 33.43  ? 4589 GLN A CG    1 
ATOM   22448 C  CD    . GLN A 1 4589 ? 261.857 226.191 193.911 1.00 46.45  ? 4589 GLN A CD    1 
ATOM   22449 O  OE1   . GLN A 1 4589 ? 262.471 225.225 193.460 1.00 53.00  ? 4589 GLN A OE1   1 
ATOM   22450 N  NE2   . GLN A 1 4589 ? 262.113 227.438 193.538 1.00 42.92  ? 4589 GLN A NE2   1 
ATOM   22451 N  N     . LEU A 1 4590 ? 256.380 227.876 195.562 1.00 22.43  ? 4590 LEU A N     1 
ATOM   22452 C  CA    . LEU A 1 4590 ? 255.224 228.612 195.071 1.00 18.41  ? 4590 LEU A CA    1 
ATOM   22453 C  C     . LEU A 1 4590 ? 255.722 229.880 194.393 1.00 22.79  ? 4590 LEU A C     1 
ATOM   22454 O  O     . LEU A 1 4590 ? 256.360 230.721 195.035 1.00 27.12  ? 4590 LEU A O     1 
ATOM   22455 C  CB    . LEU A 1 4590 ? 254.268 228.950 196.214 1.00 19.51  ? 4590 LEU A CB    1 
ATOM   22456 C  CG    . LEU A 1 4590 ? 253.927 227.837 197.202 1.00 19.85  ? 4590 LEU A CG    1 
ATOM   22457 C  CD1   . LEU A 1 4590 ? 252.950 228.343 198.246 1.00 19.26  ? 4590 LEU A CD1   1 
ATOM   22458 C  CD2   . LEU A 1 4590 ? 253.351 226.641 196.474 1.00 20.62  ? 4590 LEU A CD2   1 
ATOM   22459 N  N     . ARG A 1 4591 ? 255.447 230.010 193.100 1.00 22.38  ? 4591 ARG A N     1 
ATOM   22460 C  CA    . ARG A 1 4591 ? 255.962 231.105 192.292 1.00 18.73  ? 4591 ARG A CA    1 
ATOM   22461 C  C     . ARG A 1 4591 ? 254.793 231.854 191.666 1.00 22.47  ? 4591 ARG A C     1 
ATOM   22462 O  O     . ARG A 1 4591 ? 253.975 231.261 190.956 1.00 25.36  ? 4591 ARG A O     1 
ATOM   22463 C  CB    . ARG A 1 4591 ? 256.926 230.563 191.231 1.00 19.25  ? 4591 ARG A CB    1 
ATOM   22464 C  CG    . ARG A 1 4591 ? 257.613 231.589 190.348 1.00 26.98  ? 4591 ARG A CG    1 
ATOM   22465 C  CD    . ARG A 1 4591 ? 258.581 230.876 189.405 1.00 39.29  ? 4591 ARG A CD    1 
ATOM   22466 N  NE    . ARG A 1 4591 ? 259.321 231.784 188.538 1.00 53.52  ? 4591 ARG A NE    1 
ATOM   22467 C  CZ    . ARG A 1 4591 ? 258.918 232.179 187.339 1.00 57.95  ? 4591 ARG A CZ    1 
ATOM   22468 N  NH1   . ARG A 1 4591 ? 257.822 231.691 186.784 1.00 49.74  ? 4591 ARG A NH1   1 
ATOM   22469 N  NH2   . ARG A 1 4591 ? 259.649 233.063 186.667 1.00 57.00  ? 4591 ARG A NH2   1 
ATOM   22470 N  N     . TRP A 1 4592 ? 254.705 233.148 191.957 1.00 21.33  ? 4592 TRP A N     1 
ATOM   22471 C  CA    . TRP A 1 4592 ? 253.599 233.975 191.495 1.00 20.47  ? 4592 TRP A CA    1 
ATOM   22472 C  C     . TRP A 1 4592 ? 253.973 234.597 190.156 1.00 24.72  ? 4592 TRP A C     1 
ATOM   22473 O  O     . TRP A 1 4592 ? 255.037 235.212 190.027 1.00 33.13  ? 4592 TRP A O     1 
ATOM   22474 C  CB    . TRP A 1 4592 ? 253.269 235.057 192.523 1.00 19.77  ? 4592 TRP A CB    1 
ATOM   22475 C  CG    . TRP A 1 4592 ? 252.630 234.525 193.765 1.00 16.20  ? 4592 TRP A CG    1 
ATOM   22476 C  CD1   . TRP A 1 4592 ? 253.235 234.312 194.967 1.00 15.38  ? 4592 TRP A CD1   1 
ATOM   22477 C  CD2   . TRP A 1 4592 ? 251.261 234.142 193.930 1.00 16.11  ? 4592 TRP A CD2   1 
ATOM   22478 N  NE1   . TRP A 1 4592 ? 252.329 233.816 195.871 1.00 16.36  ? 4592 TRP A NE1   1 
ATOM   22479 C  CE2   . TRP A 1 4592 ? 251.108 233.703 195.258 1.00 14.76  ? 4592 TRP A CE2   1 
ATOM   22480 C  CE3   . TRP A 1 4592 ? 250.149 234.125 193.084 1.00 17.33  ? 4592 TRP A CE3   1 
ATOM   22481 C  CZ2   . TRP A 1 4592 ? 249.892 233.253 195.760 1.00 13.25  ? 4592 TRP A CZ2   1 
ATOM   22482 C  CZ3   . TRP A 1 4592 ? 248.942 233.680 193.585 1.00 14.27  ? 4592 TRP A CZ3   1 
ATOM   22483 C  CH2   . TRP A 1 4592 ? 248.823 233.249 194.909 1.00 12.73  ? 4592 TRP A CH2   1 
ATOM   22484 N  N     . VAL A 1 4593 ? 253.104 234.431 189.161 1.00 26.53  ? 4593 VAL A N     1 
ATOM   22485 C  CA    . VAL A 1 4593 ? 253.358 234.905 187.809 1.00 33.81  ? 4593 VAL A CA    1 
ATOM   22486 C  C     . VAL A 1 4593 ? 252.125 235.638 187.301 1.00 34.54  ? 4593 VAL A C     1 
ATOM   22487 O  O     . VAL A 1 4593 ? 251.053 235.593 187.901 1.00 32.61  ? 4593 VAL A O     1 
ATOM   22488 C  CB    . VAL A 1 4593 ? 253.739 233.760 186.848 1.00 30.68  ? 4593 VAL A CB    1 
ATOM   22489 C  CG1   . VAL A 1 4593 ? 255.101 233.220 187.201 1.00 27.61  ? 4593 VAL A CG1   1 
ATOM   22490 C  CG2   . VAL A 1 4593 ? 252.704 232.657 186.909 1.00 26.53  ? 4593 VAL A CG2   1 
ATOM   22491 N  N     . LYS A 1 4594 ? 252.300 236.331 186.180 1.00 37.38  ? 4594 LYS A N     1 
ATOM   22492 C  CA    . LYS A 1 4594 ? 251.185 237.033 185.561 1.00 37.94  ? 4594 LYS A CA    1 
ATOM   22493 C  C     . LYS A 1 4594 ? 250.258 236.044 184.869 1.00 37.95  ? 4594 LYS A C     1 
ATOM   22494 O  O     . LYS A 1 4594 ? 250.708 235.091 184.225 1.00 39.58  ? 4594 LYS A O     1 
ATOM   22495 C  CB    . LYS A 1 4594 ? 251.699 238.068 184.560 1.00 39.44  ? 4594 LYS A CB    1 
ATOM   22496 C  CG    . LYS A 1 4594 ? 252.619 239.112 185.170 1.00 37.35  ? 4594 LYS A CG    1 
ATOM   22497 C  CD    . LYS A 1 4594 ? 252.597 240.407 184.376 1.00 37.89  ? 4594 LYS A CD    1 
ATOM   22498 C  CE    . LYS A 1 4594 ? 251.187 240.954 184.255 1.00 41.20  ? 4594 LYS A CE    1 
ATOM   22499 N  NZ    . LYS A 1 4594 ? 250.537 241.098 185.586 1.00 43.43  ? 4594 LYS A NZ    1 
ATOM   22500 N  N     . GLN A 1 4595 ? 248.955 236.270 185.011 1.00 39.68  ? 4595 GLN A N     1 
ATOM   22501 C  CA    . GLN A 1 4595 ? 247.970 235.406 184.377 1.00 50.43  ? 4595 GLN A CA    1 
ATOM   22502 C  C     . GLN A 1 4595 ? 248.038 235.545 182.862 1.00 57.64  ? 4595 GLN A C     1 
ATOM   22503 O  O     . GLN A 1 4595 ? 248.146 236.652 182.327 1.00 58.30  ? 4595 GLN A O     1 
ATOM   22504 C  CB    . GLN A 1 4595 ? 246.568 235.748 184.880 1.00 52.72  ? 4595 GLN A CB    1 
ATOM   22505 C  CG    . GLN A 1 4595 ? 245.466 234.856 184.335 1.00 65.73  ? 4595 GLN A CG    1 
ATOM   22506 C  CD    . GLN A 1 4595 ? 245.637 233.406 184.739 1.00 69.94  ? 4595 GLN A CD    1 
ATOM   22507 O  OE1   . GLN A 1 4595 ? 246.037 232.567 183.931 1.00 67.81  ? 4595 GLN A OE1   1 
ATOM   22508 N  NE2   . GLN A 1 4595 ? 245.328 233.101 185.994 1.00 62.99  ? 4595 GLN A NE2   1 
ATOM   22509 N  N     . THR A 1 4596 ? 247.978 234.407 182.165 1.00 64.57  ? 4596 THR A N     1 
ATOM   22510 C  CA    . THR A 1 4596 ? 248.051 234.388 180.712 1.00 71.10  ? 4596 THR A CA    1 
ATOM   22511 C  C     . THR A 1 4596 ? 246.726 234.075 180.035 1.00 79.01  ? 4596 THR A C     1 
ATOM   22512 O  O     . THR A 1 4596 ? 246.569 234.402 178.853 1.00 81.53  ? 4596 THR A O     1 
ATOM   22513 C  CB    . THR A 1 4596 ? 249.097 233.367 180.238 1.00 71.74  ? 4596 THR A CB    1 
ATOM   22514 O  OG1   . THR A 1 4596 ? 248.656 232.042 180.562 1.00 78.12  ? 4596 THR A OG1   1 
ATOM   22515 C  CG2   . THR A 1 4596 ? 250.437 233.630 180.906 1.00 58.40  ? 4596 THR A CG2   1 
ATOM   22516 N  N     . ASN A 1 4597 ? 245.781 233.458 180.747 1.00 80.85  ? 4597 ASN A N     1 
ATOM   22517 C  CA    . ASN A 1 4597 ? 244.456 233.141 180.207 1.00 84.90  ? 4597 ASN A CA    1 
ATOM   22518 C  C     . ASN A 1 4597 ? 244.557 232.290 178.944 1.00 83.52  ? 4597 ASN A C     1 
ATOM   22519 O  O     . ASN A 1 4597 ? 243.805 232.477 177.985 1.00 82.01  ? 4597 ASN A O     1 
ATOM   22520 C  CB    . ASN A 1 4597 ? 243.650 234.413 179.945 1.00 85.61  ? 4597 ASN A CB    1 
ATOM   22521 C  CG    . ASN A 1 4597 ? 243.335 235.175 181.215 1.00 86.43  ? 4597 ASN A CG    1 
ATOM   22522 O  OD1   . ASN A 1 4597 ? 243.832 236.281 181.430 1.00 84.77  ? 4597 ASN A OD1   1 
ATOM   22523 N  ND2   . ASN A 1 4597 ? 242.504 234.587 182.067 1.00 88.13  ? 4597 ASN A ND2   1 
ATOM   22524 N  N     . THR A 1 4598 ? 245.494 231.345 178.943 1.00 84.56  ? 4598 THR A N     1 
ATOM   22525 C  CA    . THR A 1 4598 ? 245.734 230.459 177.808 1.00 83.80  ? 4598 THR A CA    1 
ATOM   22526 C  C     . THR A 1 4598 ? 245.298 229.029 178.117 1.00 87.56  ? 4598 THR A C     1 
ATOM   22527 O  O     . THR A 1 4598 ? 245.939 228.064 177.697 1.00 81.77  ? 4598 THR A O     1 
ATOM   22528 C  CB    . THR A 1 4598 ? 247.203 230.489 177.398 1.00 78.89  ? 4598 THR A CB    1 
ATOM   22529 O  OG1   . THR A 1 4598 ? 248.026 230.188 178.531 1.00 75.33  ? 4598 THR A OG1   1 
ATOM   22530 C  CG2   . THR A 1 4598 ? 247.576 231.859 176.854 1.00 77.79  ? 4598 THR A CG2   1 
ATOM   22531 N  N     . GLU A 1 4599 ? 244.202 228.891 178.856 1.00 95.26  ? 4599 GLU A N     1 
ATOM   22532 C  CA    . GLU A 1 4599 ? 243.613 227.595 179.222 1.00 94.81  ? 4599 GLU A CA    1 
ATOM   22533 C  C     . GLU A 1 4599 ? 244.660 226.786 179.993 1.00 92.59  ? 4599 GLU A C     1 
ATOM   22534 O  O     . GLU A 1 4599 ? 245.488 227.350 180.720 1.00 95.21  ? 4599 GLU A O     1 
ATOM   22535 C  CB    . GLU A 1 4599 ? 243.069 226.907 177.983 1.00 88.92  ? 4599 GLU A CB    1 
ATOM   22536 C  CG    . GLU A 1 4599 ? 242.097 227.753 177.178 1.00 96.25  ? 4599 GLU A CG    1 
ATOM   22537 C  CD    . GLU A 1 4599 ? 242.061 227.361 175.714 1.00 97.19  ? 4599 GLU A CD    1 
ATOM   22538 O  OE1   . GLU A 1 4599 ? 242.001 226.147 175.424 1.00 94.38  ? 4599 GLU A OE1   1 
ATOM   22539 O  OE2   . GLU A 1 4599 ? 242.092 228.265 174.854 1.00 93.03  ? 4599 GLU A OE2   1 
ATOM   22540 N  N     . LYS A 1 4600 ? 244.632 225.463 179.846 1.00 78.98  ? 4600 LYS A N     1 
ATOM   22541 C  CA    . LYS A 1 4600 ? 245.604 224.600 180.499 1.00 71.91  ? 4600 LYS A CA    1 
ATOM   22542 C  C     . LYS A 1 4600 ? 245.768 223.331 179.676 1.00 66.56  ? 4600 LYS A C     1 
ATOM   22543 O  O     . LYS A 1 4600 ? 244.900 222.967 178.878 1.00 60.23  ? 4600 LYS A O     1 
ATOM   22544 C  CB    . LYS A 1 4600 ? 245.187 224.262 181.936 1.00 63.77  ? 4600 LYS A CB    1 
ATOM   22545 C  CG    . LYS A 1 4600 ? 243.921 223.432 182.039 1.00 65.20  ? 4600 LYS A CG    1 
ATOM   22546 C  CD    . LYS A 1 4600 ? 243.597 223.107 183.487 1.00 64.06  ? 4600 LYS A CD    1 
ATOM   22547 C  CE    . LYS A 1 4600 ? 243.102 224.337 184.233 1.00 65.04  ? 4600 LYS A CE    1 
ATOM   22548 N  NZ    . LYS A 1 4600 ? 241.792 224.815 183.710 1.00 79.83  ? 4600 LYS A NZ    1 
ATOM   22549 N  N     . LYS A 1 4601 ? 246.898 222.662 179.883 1.00 65.13  ? 4601 LYS A N     1 
ATOM   22550 C  CA    . LYS A 1 4601 ? 247.197 221.445 179.144 1.00 57.31  ? 4601 LYS A CA    1 
ATOM   22551 C  C     . LYS A 1 4601 ? 246.264 220.316 179.567 1.00 54.40  ? 4601 LYS A C     1 
ATOM   22552 O  O     . LYS A 1 4601 ? 245.749 220.290 180.688 1.00 49.22  ? 4601 LYS A O     1 
ATOM   22553 C  CB    . LYS A 1 4601 ? 248.654 221.036 179.364 1.00 55.12  ? 4601 LYS A CB    1 
ATOM   22554 C  CG    . LYS A 1 4601 ? 249.660 221.986 178.733 1.00 63.12  ? 4601 LYS A CG    1 
ATOM   22555 C  CD    . LYS A 1 4601 ? 251.090 221.574 179.044 1.00 65.15  ? 4601 LYS A CD    1 
ATOM   22556 C  CE    . LYS A 1 4601 ? 251.476 220.303 178.308 1.00 61.82  ? 4601 LYS A CE    1 
ATOM   22557 N  NZ    . LYS A 1 4601 ? 251.553 220.520 176.836 1.00 53.54  ? 4601 LYS A NZ    1 
ATOM   22558 N  N     . ALA A 1 4602 ? 246.039 219.377 178.644 1.00 52.82  ? 4602 ALA A N     1 
ATOM   22559 C  CA    . ALA A 1 4602 ? 245.173 218.241 178.941 1.00 50.91  ? 4602 ALA A CA    1 
ATOM   22560 C  C     . ALA A 1 4602 ? 245.761 217.356 180.031 1.00 43.77  ? 4602 ALA A C     1 
ATOM   22561 O  O     . ALA A 1 4602 ? 245.015 216.674 180.744 1.00 33.79  ? 4602 ALA A O     1 
ATOM   22562 C  CB    . ALA A 1 4602 ? 244.919 217.425 177.673 1.00 43.78  ? 4602 ALA A CB    1 
ATOM   22563 N  N     . SER A 1 4603 ? 247.085 217.350 180.175 1.00 43.71  ? 4603 SER A N     1 
ATOM   22564 C  CA    . SER A 1 4603 ? 247.739 216.570 181.215 1.00 45.04  ? 4603 SER A CA    1 
ATOM   22565 C  C     . SER A 1 4603 ? 247.817 217.304 182.547 1.00 40.24  ? 4603 SER A C     1 
ATOM   22566 O  O     . SER A 1 4603 ? 248.346 216.745 183.513 1.00 41.60  ? 4603 SER A O     1 
ATOM   22567 C  CB    . SER A 1 4603 ? 249.147 216.173 180.765 1.00 42.54  ? 4603 SER A CB    1 
ATOM   22568 O  OG    . SER A 1 4603 ? 249.800 217.256 180.126 1.00 42.94  ? 4603 SER A OG    1 
ATOM   22569 N  N     . VAL A 1 4604 ? 247.314 218.529 182.626 1.00 37.25  ? 4604 VAL A N     1 
ATOM   22570 C  CA    . VAL A 1 4604 ? 247.375 219.295 183.864 1.00 34.20  ? 4604 VAL A CA    1 
ATOM   22571 C  C     . VAL A 1 4604 ? 246.193 218.918 184.745 1.00 32.10  ? 4604 VAL A C     1 
ATOM   22572 O  O     . VAL A 1 4604 ? 245.038 218.928 184.302 1.00 41.59  ? 4604 VAL A O     1 
ATOM   22573 C  CB    . VAL A 1 4604 ? 247.398 220.804 183.573 1.00 38.43  ? 4604 VAL A CB    1 
ATOM   22574 C  CG1   . VAL A 1 4604 ? 246.941 221.588 184.791 1.00 28.94  ? 4604 VAL A CG1   1 
ATOM   22575 C  CG2   . VAL A 1 4604 ? 248.794 221.235 183.154 1.00 40.25  ? 4604 VAL A CG2   1 
ATOM   22576 N  N     . VAL A 1 4605 ? 246.483 218.581 185.997 1.00 21.98  ? 4605 VAL A N     1 
ATOM   22577 C  CA    . VAL A 1 4605 ? 245.476 218.216 186.985 1.00 17.79  ? 4605 VAL A CA    1 
ATOM   22578 C  C     . VAL A 1 4605 ? 245.485 219.255 188.100 1.00 18.02  ? 4605 VAL A C     1 
ATOM   22579 O  O     . VAL A 1 4605 ? 246.548 219.737 188.510 1.00 21.54  ? 4605 VAL A O     1 
ATOM   22580 C  CB    . VAL A 1 4605 ? 245.713 216.791 187.531 1.00 18.40  ? 4605 VAL A CB    1 
ATOM   22581 C  CG1   . VAL A 1 4605 ? 246.913 216.746 188.469 1.00 17.40  ? 4605 VAL A CG1   1 
ATOM   22582 C  CG2   . VAL A 1 4605 ? 244.473 216.280 188.231 1.00 17.94  ? 4605 VAL A CG2   1 
ATOM   22583 N  N     . THR A 1 4606 ? 244.297 219.627 188.561 1.00 14.10  ? 4606 THR A N     1 
ATOM   22584 C  CA    . THR A 1 4606 ? 244.144 220.570 189.661 1.00 12.87  ? 4606 THR A CA    1 
ATOM   22585 C  C     . THR A 1 4606 ? 243.842 219.792 190.934 1.00 19.20  ? 4606 THR A C     1 
ATOM   22586 O  O     . THR A 1 4606 ? 242.842 219.069 191.003 1.00 21.42  ? 4606 THR A O     1 
ATOM   22587 C  CB    . THR A 1 4606 ? 243.037 221.584 189.373 1.00 16.96  ? 4606 THR A CB    1 
ATOM   22588 O  OG1   . THR A 1 4606 ? 243.414 222.400 188.258 1.00 30.87  ? 4606 THR A OG1   1 
ATOM   22589 C  CG2   . THR A 1 4606 ? 242.807 222.473 190.582 1.00 12.44  ? 4606 THR A CG2   1 
ATOM   22590 N  N     . LEU A 1 4607 ? 244.704 219.941 191.934 1.00 14.96  ? 4607 LEU A N     1 
ATOM   22591 C  CA    . LEU A 1 4607 ? 244.599 219.214 193.182 1.00 11.27  ? 4607 LEU A CA    1 
ATOM   22592 C  C     . LEU A 1 4607 ? 244.327 220.171 194.328 1.00 13.71  ? 4607 LEU A C     1 
ATOM   22593 O  O     . LEU A 1 4607 ? 244.994 221.209 194.437 1.00 15.92  ? 4607 LEU A O     1 
ATOM   22594 C  CB    . LEU A 1 4607 ? 245.886 218.433 193.461 1.00 8.48   ? 4607 LEU A CB    1 
ATOM   22595 C  CG    . LEU A 1 4607 ? 246.203 217.249 192.550 1.00 11.40  ? 4607 LEU A CG    1 
ATOM   22596 C  CD1   . LEU A 1 4607 ? 247.259 216.380 193.196 1.00 11.26  ? 4607 LEU A CD1   1 
ATOM   22597 C  CD2   . LEU A 1 4607 ? 244.953 216.443 192.250 1.00 11.97  ? 4607 LEU A CD2   1 
ATOM   22598 N  N     . PRO A 1 4608 ? 243.360 219.864 195.187 1.00 14.00  ? 4608 PRO A N     1 
ATOM   22599 C  CA    . PRO A 1 4608 ? 243.164 220.670 196.395 1.00 11.35  ? 4608 PRO A CA    1 
ATOM   22600 C  C     . PRO A 1 4608 ? 244.308 220.479 197.377 1.00 11.16  ? 4608 PRO A C     1 
ATOM   22601 O  O     . PRO A 1 4608 ? 244.962 219.435 197.410 1.00 13.10  ? 4608 PRO A O     1 
ATOM   22602 C  CB    . PRO A 1 4608 ? 241.849 220.131 196.967 1.00 10.04  ? 4608 PRO A CB    1 
ATOM   22603 C  CG    . PRO A 1 4608 ? 241.755 218.742 196.448 1.00 8.30   ? 4608 PRO A CG    1 
ATOM   22604 C  CD    . PRO A 1 4608 ? 242.430 218.725 195.112 1.00 7.51   ? 4608 PRO A CD    1 
ATOM   22605 N  N     . VAL A 1 4609 ? 244.546 221.505 198.185 1.00 11.53  ? 4609 VAL A N     1 
ATOM   22606 C  CA    . VAL A 1 4609 ? 245.528 221.442 199.264 1.00 11.80  ? 4609 VAL A CA    1 
ATOM   22607 C  C     . VAL A 1 4609 ? 244.748 221.630 200.559 1.00 11.73  ? 4609 VAL A C     1 
ATOM   22608 O  O     . VAL A 1 4609 ? 244.428 222.752 200.960 1.00 14.55  ? 4609 VAL A O     1 
ATOM   22609 C  CB    . VAL A 1 4609 ? 246.638 222.483 199.115 1.00 7.80   ? 4609 VAL A CB    1 
ATOM   22610 C  CG1   . VAL A 1 4609 ? 247.681 222.298 200.202 1.00 7.47   ? 4609 VAL A CG1   1 
ATOM   22611 C  CG2   . VAL A 1 4609 ? 247.275 222.377 197.743 1.00 7.37   ? 4609 VAL A CG2   1 
ATOM   22612 N  N     . TYR A 1 4610 ? 244.430 220.523 201.219 1.00 12.03  ? 4610 TYR A N     1 
ATOM   22613 C  CA    . TYR A 1 4610 ? 243.665 220.573 202.451 1.00 9.91   ? 4610 TYR A CA    1 
ATOM   22614 C  C     . TYR A 1 4610 ? 244.583 220.820 203.643 1.00 10.30  ? 4610 TYR A C     1 
ATOM   22615 O  O     . TYR A 1 4610 ? 245.777 220.510 203.621 1.00 13.10  ? 4610 TYR A O     1 
ATOM   22616 C  CB    . TYR A 1 4610 ? 242.877 219.279 202.643 1.00 8.43   ? 4610 TYR A CB    1 
ATOM   22617 C  CG    . TYR A 1 4610 ? 241.823 219.056 201.587 1.00 9.35   ? 4610 TYR A CG    1 
ATOM   22618 C  CD1   . TYR A 1 4610 ? 240.712 219.883 201.507 1.00 9.17   ? 4610 TYR A CD1   1 
ATOM   22619 C  CD2   . TYR A 1 4610 ? 241.943 218.029 200.666 1.00 9.24   ? 4610 TYR A CD2   1 
ATOM   22620 C  CE1   . TYR A 1 4610 ? 239.747 219.686 200.543 1.00 9.39   ? 4610 TYR A CE1   1 
ATOM   22621 C  CE2   . TYR A 1 4610 ? 240.983 217.825 199.699 1.00 8.86   ? 4610 TYR A CE2   1 
ATOM   22622 C  CZ    . TYR A 1 4610 ? 239.888 218.655 199.643 1.00 12.31  ? 4610 TYR A CZ    1 
ATOM   22623 O  OH    . TYR A 1 4610 ? 238.929 218.453 198.679 1.00 19.82  ? 4610 TYR A OH    1 
ATOM   22624 N  N     . LEU A 1 4611 ? 244.003 221.397 204.694 1.00 12.31  ? 4611 LEU A N     1 
ATOM   22625 C  CA    . LEU A 1 4611 ? 244.784 221.729 205.879 1.00 10.96  ? 4611 LEU A CA    1 
ATOM   22626 C  C     . LEU A 1 4611 ? 245.229 220.476 206.622 1.00 14.55  ? 4611 LEU A C     1 
ATOM   22627 O  O     . LEU A 1 4611 ? 246.357 220.413 207.122 1.00 19.48  ? 4611 LEU A O     1 
ATOM   22628 C  CB    . LEU A 1 4611 ? 243.973 222.644 206.795 1.00 13.07  ? 4611 LEU A CB    1 
ATOM   22629 C  CG    . LEU A 1 4611 ? 244.691 223.197 208.023 1.00 14.43  ? 4611 LEU A CG    1 
ATOM   22630 C  CD1   . LEU A 1 4611 ? 245.986 223.883 207.618 1.00 17.30  ? 4611 LEU A CD1   1 
ATOM   22631 C  CD2   . LEU A 1 4611 ? 243.785 224.163 208.751 1.00 15.95  ? 4611 LEU A CD2   1 
ATOM   22632 N  N     . ASN A 1 4612 ? 244.364 219.470 206.703 1.00 16.36  ? 4612 ASN A N     1 
ATOM   22633 C  CA    . ASN A 1 4612 ? 244.670 218.244 207.429 1.00 11.95  ? 4612 ASN A CA    1 
ATOM   22634 C  C     . ASN A 1 4612 ? 243.991 217.076 206.721 1.00 10.67  ? 4612 ASN A C     1 
ATOM   22635 O  O     . ASN A 1 4612 ? 243.390 217.237 205.654 1.00 9.33   ? 4612 ASN A O     1 
ATOM   22636 C  CB    . ASN A 1 4612 ? 244.241 218.370 208.897 1.00 10.44  ? 4612 ASN A CB    1 
ATOM   22637 C  CG    . ASN A 1 4612 ? 242.876 219.007 209.053 1.00 13.64  ? 4612 ASN A CG    1 
ATOM   22638 O  OD1   . ASN A 1 4612 ? 242.053 218.974 208.140 1.00 14.37  ? 4612 ASN A OD1   1 
ATOM   22639 N  ND2   . ASN A 1 4612 ? 242.633 219.603 210.211 1.00 18.19  ? 4612 ASN A ND2   1 
ATOM   22640 N  N     . PHE A 1 4613 ? 244.092 215.889 207.323 1.00 11.17  ? 4613 PHE A N     1 
ATOM   22641 C  CA    . PHE A 1 4613 ? 243.546 214.681 206.715 1.00 8.40   ? 4613 PHE A CA    1 
ATOM   22642 C  C     . PHE A 1 4613 ? 242.025 214.691 206.653 1.00 9.40   ? 4613 PHE A C     1 
ATOM   22643 O  O     . PHE A 1 4613 ? 241.448 213.955 205.845 1.00 11.36  ? 4613 PHE A O     1 
ATOM   22644 C  CB    . PHE A 1 4613 ? 244.036 213.446 207.477 1.00 10.30  ? 4613 PHE A CB    1 
ATOM   22645 C  CG    . PHE A 1 4613 ? 243.370 213.244 208.810 1.00 13.65  ? 4613 PHE A CG    1 
ATOM   22646 C  CD1   . PHE A 1 4613 ? 242.229 212.469 208.926 1.00 11.74  ? 4613 PHE A CD1   1 
ATOM   22647 C  CD2   . PHE A 1 4613 ? 243.891 213.832 209.950 1.00 12.20  ? 4613 PHE A CD2   1 
ATOM   22648 C  CE1   . PHE A 1 4613 ? 241.621 212.287 210.149 1.00 15.23  ? 4613 PHE A CE1   1 
ATOM   22649 C  CE2   . PHE A 1 4613 ? 243.288 213.654 211.175 1.00 14.00  ? 4613 PHE A CE2   1 
ATOM   22650 C  CZ    . PHE A 1 4613 ? 242.151 212.880 211.275 1.00 21.94  ? 4613 PHE A CZ    1 
ATOM   22651 N  N     . THR A 1 4614 ? 241.364 215.500 207.483 1.00 8.69   ? 4614 THR A N     1 
ATOM   22652 C  CA    . THR A 1 4614 ? 239.909 215.556 207.467 1.00 8.13   ? 4614 THR A CA    1 
ATOM   22653 C  C     . THR A 1 4614 ? 239.362 216.142 206.173 1.00 9.61   ? 4614 THR A C     1 
ATOM   22654 O  O     . THR A 1 4614 ? 238.187 215.922 205.861 1.00 17.03  ? 4614 THR A O     1 
ATOM   22655 C  CB    . THR A 1 4614 ? 239.399 216.370 208.657 1.00 8.29   ? 4614 THR A CB    1 
ATOM   22656 O  OG1   . THR A 1 4614 ? 239.938 217.695 208.596 1.00 12.21  ? 4614 THR A OG1   1 
ATOM   22657 C  CG2   . THR A 1 4614 ? 239.819 215.721 209.963 1.00 8.78   ? 4614 THR A CG2   1 
ATOM   22658 N  N     . ARG A 1 4615 ? 240.184 216.880 205.424 1.00 7.60   ? 4615 ARG A N     1 
ATOM   22659 C  CA    . ARG A 1 4615 ? 239.786 217.486 204.153 1.00 8.74   ? 4615 ARG A CA    1 
ATOM   22660 C  C     . ARG A 1 4615 ? 238.595 218.426 204.323 1.00 14.39  ? 4615 ARG A C     1 
ATOM   22661 O  O     . ARG A 1 4615 ? 237.764 218.561 203.423 1.00 25.68  ? 4615 ARG A O     1 
ATOM   22662 C  CB    . ARG A 1 4615 ? 239.476 216.418 203.099 1.00 7.22   ? 4615 ARG A CB    1 
ATOM   22663 C  CG    . ARG A 1 4615 ? 240.625 215.466 202.823 1.00 6.42   ? 4615 ARG A CG    1 
ATOM   22664 C  CD    . ARG A 1 4615 ? 240.494 214.831 201.454 1.00 5.42   ? 4615 ARG A CD    1 
ATOM   22665 N  NE    . ARG A 1 4615 ? 241.506 213.808 201.228 1.00 6.45   ? 4615 ARG A NE    1 
ATOM   22666 C  CZ    . ARG A 1 4615 ? 241.734 213.227 200.058 1.00 6.20   ? 4615 ARG A CZ    1 
ATOM   22667 N  NH1   . ARG A 1 4615 ? 241.029 213.536 198.984 1.00 4.02   ? 4615 ARG A NH1   1 
ATOM   22668 N  NH2   . ARG A 1 4615 ? 242.694 212.310 199.966 1.00 7.74   ? 4615 ARG A NH2   1 
ATOM   22669 N  N     . ALA A 1 4616 ? 238.509 219.084 205.477 1.00 11.85  ? 4616 ALA A N     1 
ATOM   22670 C  CA    . ALA A 1 4616 ? 237.393 219.975 205.764 1.00 17.65  ? 4616 ALA A CA    1 
ATOM   22671 C  C     . ALA A 1 4616 ? 237.677 221.419 205.379 1.00 26.85  ? 4616 ALA A C     1 
ATOM   22672 O  O     . ALA A 1 4616 ? 236.739 222.169 205.087 1.00 30.47  ? 4616 ALA A O     1 
ATOM   22673 C  CB    . ALA A 1 4616 ? 237.029 219.903 207.248 1.00 16.95  ? 4616 ALA A CB    1 
ATOM   22674 N  N     . ASP A 1 4617 ? 238.942 221.827 205.374 1.00 28.60  ? 4617 ASP A N     1 
ATOM   22675 C  CA    . ASP A 1 4617 ? 239.333 223.188 205.035 1.00 20.61  ? 4617 ASP A CA    1 
ATOM   22676 C  C     . ASP A 1 4617 ? 240.258 223.162 203.828 1.00 15.75  ? 4617 ASP A C     1 
ATOM   22677 O  O     . ASP A 1 4617 ? 241.262 222.444 203.825 1.00 14.55  ? 4617 ASP A O     1 
ATOM   22678 C  CB    . ASP A 1 4617 ? 240.019 223.874 206.216 1.00 24.30  ? 4617 ASP A CB    1 
ATOM   22679 C  CG    . ASP A 1 4617 ? 239.064 224.158 207.355 1.00 41.69  ? 4617 ASP A CG    1 
ATOM   22680 O  OD1   . ASP A 1 4617 ? 237.860 224.358 207.088 1.00 44.74  ? 4617 ASP A OD1   1 
ATOM   22681 O  OD2   . ASP A 1 4617 ? 239.514 224.178 208.517 1.00 42.05  ? 4617 ASP A OD2   1 
ATOM   22682 N  N     . LEU A 1 4618 ? 239.918 223.948 202.814 1.00 17.52  ? 4618 LEU A N     1 
ATOM   22683 C  CA    . LEU A 1 4618 ? 240.691 224.025 201.582 1.00 13.70  ? 4618 LEU A CA    1 
ATOM   22684 C  C     . LEU A 1 4618 ? 241.533 225.294 201.608 1.00 17.91  ? 4618 LEU A C     1 
ATOM   22685 O  O     . LEU A 1 4618 ? 240.996 226.399 201.734 1.00 20.80  ? 4618 LEU A O     1 
ATOM   22686 C  CB    . LEU A 1 4618 ? 239.768 224.013 200.366 1.00 14.06  ? 4618 LEU A CB    1 
ATOM   22687 C  CG    . LEU A 1 4618 ? 240.393 224.400 199.027 1.00 18.61  ? 4618 LEU A CG    1 
ATOM   22688 C  CD1   . LEU A 1 4618 ? 241.229 223.260 198.499 1.00 15.30  ? 4618 LEU A CD1   1 
ATOM   22689 C  CD2   . LEU A 1 4618 ? 239.315 224.783 198.029 1.00 16.53  ? 4618 LEU A CD2   1 
ATOM   22690 N  N     . ILE A 1 4619 ? 242.851 225.133 201.485 1.00 16.85  ? 4619 ILE A N     1 
ATOM   22691 C  CA    . ILE A 1 4619 ? 243.746 226.284 201.524 1.00 14.30  ? 4619 ILE A CA    1 
ATOM   22692 C  C     . ILE A 1 4619 ? 243.875 226.909 200.142 1.00 14.30  ? 4619 ILE A C     1 
ATOM   22693 O  O     . ILE A 1 4619 ? 243.618 228.103 199.959 1.00 17.56  ? 4619 ILE A O     1 
ATOM   22694 C  CB    . ILE A 1 4619 ? 245.117 225.875 202.093 1.00 16.25  ? 4619 ILE A CB    1 
ATOM   22695 C  CG1   . ILE A 1 4619 ? 244.940 224.985 203.324 1.00 14.62  ? 4619 ILE A CG1   1 
ATOM   22696 C  CG2   . ILE A 1 4619 ? 245.933 227.106 202.452 1.00 19.00  ? 4619 ILE A CG2   1 
ATOM   22697 C  CD1   . ILE A 1 4619 ? 244.194 225.649 204.461 1.00 18.12  ? 4619 ILE A CD1   1 
ATOM   22698 N  N     . PHE A 1 4620 ? 244.265 226.115 199.151 1.00 12.09  ? 4620 PHE A N     1 
ATOM   22699 C  CA    . PHE A 1 4620 ? 244.375 226.583 197.774 1.00 13.73  ? 4620 PHE A CA    1 
ATOM   22700 C  C     . PHE A 1 4620 ? 244.381 225.367 196.853 1.00 15.43  ? 4620 PHE A C     1 
ATOM   22701 O  O     . PHE A 1 4620 ? 244.099 224.241 197.278 1.00 16.16  ? 4620 PHE A O     1 
ATOM   22702 C  CB    . PHE A 1 4620 ? 245.614 227.469 197.579 1.00 11.21  ? 4620 PHE A CB    1 
ATOM   22703 C  CG    . PHE A 1 4620 ? 246.918 226.800 197.927 1.00 11.75  ? 4620 PHE A CG    1 
ATOM   22704 C  CD1   . PHE A 1 4620 ? 247.276 226.580 199.246 1.00 15.40  ? 4620 PHE A CD1   1 
ATOM   22705 C  CD2   . PHE A 1 4620 ? 247.797 226.417 196.931 1.00 10.08  ? 4620 PHE A CD2   1 
ATOM   22706 C  CE1   . PHE A 1 4620 ? 248.475 225.973 199.564 1.00 11.80  ? 4620 PHE A CE1   1 
ATOM   22707 C  CE2   . PHE A 1 4620 ? 249.000 225.812 197.244 1.00 8.13   ? 4620 PHE A CE2   1 
ATOM   22708 C  CZ    . PHE A 1 4620 ? 249.338 225.589 198.560 1.00 8.97   ? 4620 PHE A CZ    1 
ATOM   22709 N  N     . THR A 1 4621 ? 244.684 225.601 195.579 1.00 16.77  ? 4621 THR A N     1 
ATOM   22710 C  CA    . THR A 1 4621 ? 244.728 224.552 194.572 1.00 13.45  ? 4621 THR A CA    1 
ATOM   22711 C  C     . THR A 1 4621 ? 246.057 224.619 193.836 1.00 13.97  ? 4621 THR A C     1 
ATOM   22712 O  O     . THR A 1 4621 ? 246.598 225.706 193.614 1.00 17.58  ? 4621 THR A O     1 
ATOM   22713 C  CB    . THR A 1 4621 ? 243.574 224.680 193.573 1.00 14.30  ? 4621 THR A CB    1 
ATOM   22714 O  OG1   . THR A 1 4621 ? 243.670 225.933 192.887 1.00 24.35  ? 4621 THR A OG1   1 
ATOM   22715 C  CG2   . THR A 1 4621 ? 242.232 224.600 194.287 1.00 10.24  ? 4621 THR A CG2   1 
ATOM   22716 N  N     . VAL A 1 4622 ? 246.578 223.456 193.462 1.00 14.06  ? 4622 VAL A N     1 
ATOM   22717 C  CA    . VAL A 1 4622 ? 247.851 223.352 192.761 1.00 14.53  ? 4622 VAL A CA    1 
ATOM   22718 C  C     . VAL A 1 4622 ? 247.613 222.699 191.408 1.00 15.53  ? 4622 VAL A C     1 
ATOM   22719 O  O     . VAL A 1 4622 ? 246.864 221.723 191.301 1.00 18.47  ? 4622 VAL A O     1 
ATOM   22720 C  CB    . VAL A 1 4622 ? 248.896 222.564 193.579 1.00 19.85  ? 4622 VAL A CB    1 
ATOM   22721 C  CG1   . VAL A 1 4622 ? 249.244 223.315 194.846 1.00 14.21  ? 4622 VAL A CG1   1 
ATOM   22722 C  CG2   . VAL A 1 4622 ? 248.386 221.170 193.918 1.00 20.16  ? 4622 VAL A CG2   1 
ATOM   22723 N  N     . ASP A 1 4623 ? 248.237 223.248 190.371 1.00 18.22  ? 4623 ASP A N     1 
ATOM   22724 C  CA    . ASP A 1 4623 ? 248.149 222.697 189.024 1.00 19.52  ? 4623 ASP A CA    1 
ATOM   22725 C  C     . ASP A 1 4623 ? 249.429 221.920 188.739 1.00 19.32  ? 4623 ASP A C     1 
ATOM   22726 O  O     . ASP A 1 4623 ? 250.502 222.511 188.586 1.00 22.76  ? 4623 ASP A O     1 
ATOM   22727 C  CB    . ASP A 1 4623 ? 247.927 223.803 187.995 1.00 22.29  ? 4623 ASP A CB    1 
ATOM   22728 C  CG    . ASP A 1 4623 ? 246.464 224.166 187.840 1.00 28.81  ? 4623 ASP A CG    1 
ATOM   22729 O  OD1   . ASP A 1 4623 ? 246.066 225.250 188.315 1.00 44.53  ? 4623 ASP A OD1   1 
ATOM   22730 O  OD2   . ASP A 1 4623 ? 245.711 223.371 187.242 1.00 26.48  ? 4623 ASP A OD2   1 
ATOM   22731 N  N     . PHE A 1 4624 ? 249.314 220.599 188.680 1.00 17.45  ? 4624 PHE A N     1 
ATOM   22732 C  CA    . PHE A 1 4624 ? 250.433 219.716 188.398 1.00 17.66  ? 4624 PHE A CA    1 
ATOM   22733 C  C     . PHE A 1 4624 ? 250.320 219.160 186.986 1.00 24.19  ? 4624 PHE A C     1 
ATOM   22734 O  O     . PHE A 1 4624 ? 249.261 219.205 186.359 1.00 30.01  ? 4624 PHE A O     1 
ATOM   22735 C  CB    . PHE A 1 4624 ? 250.484 218.569 189.408 1.00 19.46  ? 4624 PHE A CB    1 
ATOM   22736 C  CG    . PHE A 1 4624 ? 251.282 218.877 190.639 1.00 21.37  ? 4624 PHE A CG    1 
ATOM   22737 C  CD1   . PHE A 1 4624 ? 252.660 218.985 190.579 1.00 23.15  ? 4624 PHE A CD1   1 
ATOM   22738 C  CD2   . PHE A 1 4624 ? 250.653 219.062 191.858 1.00 21.47  ? 4624 PHE A CD2   1 
ATOM   22739 C  CE1   . PHE A 1 4624 ? 253.395 219.269 191.712 1.00 24.49  ? 4624 PHE A CE1   1 
ATOM   22740 C  CE2   . PHE A 1 4624 ? 251.383 219.345 192.994 1.00 19.00  ? 4624 PHE A CE2   1 
ATOM   22741 C  CZ    . PHE A 1 4624 ? 252.756 219.450 192.920 1.00 20.56  ? 4624 PHE A CZ    1 
ATOM   22742 N  N     . GLU A 1 4625 ? 251.428 218.624 186.490 1.00 28.74  ? 4625 GLU A N     1 
ATOM   22743 C  CA    . GLU A 1 4625 ? 251.488 218.005 185.168 1.00 27.52  ? 4625 GLU A CA    1 
ATOM   22744 C  C     . GLU A 1 4625 ? 251.773 216.521 185.362 1.00 32.46  ? 4625 GLU A C     1 
ATOM   22745 O  O     . GLU A 1 4625 ? 252.913 216.131 185.631 1.00 43.69  ? 4625 GLU A O     1 
ATOM   22746 C  CB    . GLU A 1 4625 ? 252.554 218.671 184.304 1.00 32.42  ? 4625 GLU A CB    1 
ATOM   22747 C  CG    . GLU A 1 4625 ? 252.379 218.438 182.815 1.00 50.39  ? 4625 GLU A CG    1 
ATOM   22748 C  CD    . GLU A 1 4625 ? 253.584 218.882 182.013 1.00 56.74  ? 4625 GLU A CD    1 
ATOM   22749 O  OE1   . GLU A 1 4625 ? 254.229 219.875 182.408 1.00 51.20  ? 4625 GLU A OE1   1 
ATOM   22750 O  OE2   . GLU A 1 4625 ? 253.888 218.236 180.987 1.00 62.44  ? 4625 GLU A OE2   1 
ATOM   22751 N  N     . ILE A 1 4626 ? 250.739 215.692 185.223 1.00 29.44  ? 4626 ILE A N     1 
ATOM   22752 C  CA    . ILE A 1 4626 ? 250.913 214.260 185.425 1.00 29.34  ? 4626 ILE A CA    1 
ATOM   22753 C  C     . ILE A 1 4626 ? 251.752 213.679 184.294 1.00 33.18  ? 4626 ILE A C     1 
ATOM   22754 O  O     . ILE A 1 4626 ? 251.781 214.202 183.173 1.00 39.76  ? 4626 ILE A O     1 
ATOM   22755 C  CB    . ILE A 1 4626 ? 249.553 213.544 185.525 1.00 31.66  ? 4626 ILE A CB    1 
ATOM   22756 C  CG1   . ILE A 1 4626 ? 248.780 213.682 184.217 1.00 29.65  ? 4626 ILE A CG1   1 
ATOM   22757 C  CG2   . ILE A 1 4626 ? 248.741 214.107 186.675 1.00 28.67  ? 4626 ILE A CG2   1 
ATOM   22758 C  CD1   . ILE A 1 4626 ? 247.558 212.818 184.155 1.00 30.24  ? 4626 ILE A CD1   1 
ATOM   22759 N  N     . ALA A 1 4627 ? 252.444 212.584 184.593 1.00 33.69  ? 4627 ALA A N     1 
ATOM   22760 C  CA    . ALA A 1 4627 ? 253.291 211.937 183.605 1.00 36.71  ? 4627 ALA A CA    1 
ATOM   22761 C  C     . ALA A 1 4627 ? 252.440 211.246 182.542 1.00 40.92  ? 4627 ALA A C     1 
ATOM   22762 O  O     . ALA A 1 4627 ? 251.224 211.089 182.679 1.00 42.94  ? 4627 ALA A O     1 
ATOM   22763 C  CB    . ALA A 1 4627 ? 254.226 210.935 184.278 1.00 33.31  ? 4627 ALA A CB    1 
ATOM   22764 N  N     . THR A 1 4628 ? 253.103 210.830 181.465 1.00 45.68  ? 4628 THR A N     1 
ATOM   22765 C  CA    . THR A 1 4628 ? 252.424 210.116 180.397 1.00 41.61  ? 4628 THR A CA    1 
ATOM   22766 C  C     . THR A 1 4628 ? 251.932 208.760 180.899 1.00 47.15  ? 4628 THR A C     1 
ATOM   22767 O  O     . THR A 1 4628 ? 252.351 208.264 181.950 1.00 45.77  ? 4628 THR A O     1 
ATOM   22768 C  CB    . THR A 1 4628 ? 253.351 209.935 179.198 1.00 47.18  ? 4628 THR A CB    1 
ATOM   22769 O  OG1   . THR A 1 4628 ? 254.431 209.062 179.553 1.00 50.89  ? 4628 THR A OG1   1 
ATOM   22770 C  CG2   . THR A 1 4628 ? 253.913 211.277 178.755 1.00 42.54  ? 4628 THR A CG2   1 
ATOM   22771 N  N     . LYS A 1 4629 ? 251.009 208.170 180.136 1.00 49.07  ? 4629 LYS A N     1 
ATOM   22772 C  CA    . LYS A 1 4629 ? 250.321 206.916 180.431 1.00 49.79  ? 4629 LYS A CA    1 
ATOM   22773 C  C     . LYS A 1 4629 ? 249.345 207.080 181.596 1.00 49.09  ? 4629 LYS A C     1 
ATOM   22774 O  O     . LYS A 1 4629 ? 248.512 206.193 181.828 1.00 52.60  ? 4629 LYS A O     1 
ATOM   22775 C  CB    . LYS A 1 4629 ? 251.324 205.773 180.695 1.00 50.46  ? 4629 LYS A CB    1 
ATOM   22776 C  CG    . LYS A 1 4629 ? 250.813 204.521 181.396 1.00 58.31  ? 4629 LYS A CG    1 
ATOM   22777 C  CD    . LYS A 1 4629 ? 251.628 203.298 181.010 1.00 64.55  ? 4629 LYS A CD    1 
ATOM   22778 C  CE    . LYS A 1 4629 ? 251.253 202.094 181.861 1.00 58.84  ? 4629 LYS A CE    1 
ATOM   22779 N  NZ    . LYS A 1 4629 ? 251.494 200.811 181.148 1.00 60.26  ? 4629 LYS A NZ    1 
ATOM   22780 N  N     . GLU A 1 4630 ? 249.353 208.222 182.273 1.00 47.64  ? 4630 GLU A N     1 
ATOM   22781 C  CA    . GLU A 1 4630 ? 248.466 208.479 183.395 1.00 39.81  ? 4630 GLU A CA    1 
ATOM   22782 C  C     . GLU A 1 4630 ? 247.210 209.198 182.921 1.00 40.59  ? 4630 GLU A C     1 
ATOM   22783 O  O     . GLU A 1 4630 ? 247.225 209.927 181.926 1.00 47.61  ? 4630 GLU A O     1 
ATOM   22784 C  CB    . GLU A 1 4630 ? 249.169 209.308 184.471 1.00 39.09  ? 4630 GLU A CB    1 
ATOM   22785 C  CG    . GLU A 1 4630 ? 250.293 208.571 185.179 1.00 38.67  ? 4630 GLU A CG    1 
ATOM   22786 C  CD    . GLU A 1 4630 ? 249.784 207.471 186.089 1.00 45.04  ? 4630 GLU A CD    1 
ATOM   22787 O  OE1   . GLU A 1 4630 ? 249.560 206.344 185.600 1.00 52.46  ? 4630 GLU A OE1   1 
ATOM   22788 O  OE2   . GLU A 1 4630 ? 249.606 207.733 187.297 1.00 41.46  ? 4630 GLU A OE2   1 
ATOM   22789 N  N     . ASP A 1 4631 ? 246.120 208.982 183.649 1.00 37.73  ? 4631 ASP A N     1 
ATOM   22790 C  CA    . ASP A 1 4631 ? 244.814 209.494 183.273 1.00 33.10  ? 4631 ASP A CA    1 
ATOM   22791 C  C     . ASP A 1 4631 ? 244.295 210.419 184.365 1.00 29.96  ? 4631 ASP A C     1 
ATOM   22792 O  O     . ASP A 1 4631 ? 244.020 209.950 185.479 1.00 33.27  ? 4631 ASP A O     1 
ATOM   22793 C  CB    . ASP A 1 4631 ? 243.853 208.330 183.041 1.00 34.46  ? 4631 ASP A CB    1 
ATOM   22794 C  CG    . ASP A 1 4631 ? 242.515 208.771 182.504 1.00 39.80  ? 4631 ASP A CG    1 
ATOM   22795 O  OD1   . ASP A 1 4631 ? 242.439 209.135 181.312 1.00 47.15  ? 4631 ASP A OD1   1 
ATOM   22796 O  OD2   . ASP A 1 4631 ? 241.533 208.720 183.267 1.00 37.89  ? 4631 ASP A OD2   1 
ATOM   22797 N  N     . PRO A 1 4632 ? 244.161 211.724 184.106 1.00 25.71  ? 4632 PRO A N     1 
ATOM   22798 C  CA    . PRO A 1 4632 ? 243.731 212.643 185.176 1.00 29.94  ? 4632 PRO A CA    1 
ATOM   22799 C  C     . PRO A 1 4632 ? 242.360 212.311 185.724 1.00 26.02  ? 4632 PRO A C     1 
ATOM   22800 O  O     . PRO A 1 4632 ? 242.062 212.608 186.890 1.00 23.31  ? 4632 PRO A O     1 
ATOM   22801 C  CB    . PRO A 1 4632 ? 243.739 214.015 184.485 1.00 26.54  ? 4632 PRO A CB    1 
ATOM   22802 C  CG    . PRO A 1 4632 ? 243.629 213.712 183.031 1.00 23.62  ? 4632 PRO A CG    1 
ATOM   22803 C  CD    . PRO A 1 4632 ? 244.329 212.410 182.815 1.00 28.49  ? 4632 PRO A CD    1 
ATOM   22804 N  N     . ARG A 1 4633 ? 241.512 211.703 184.900 1.00 28.12  ? 4633 ARG A N     1 
ATOM   22805 C  CA    . ARG A 1 4633 ? 240.189 211.298 185.346 1.00 23.90  ? 4633 ARG A CA    1 
ATOM   22806 C  C     . ARG A 1 4633 ? 240.312 210.279 186.477 1.00 21.64  ? 4633 ARG A C     1 
ATOM   22807 O  O     . ARG A 1 4633 ? 239.607 210.363 187.492 1.00 21.43  ? 4633 ARG A O     1 
ATOM   22808 C  CB    . ARG A 1 4633 ? 239.429 210.726 184.148 1.00 27.07  ? 4633 ARG A CB    1 
ATOM   22809 C  CG    . ARG A 1 4633 ? 238.038 210.248 184.407 1.00 30.13  ? 4633 ARG A CG    1 
ATOM   22810 C  CD    . ARG A 1 4633 ? 237.179 211.438 184.767 1.00 34.33  ? 4633 ARG A CD    1 
ATOM   22811 N  NE    . ARG A 1 4633 ? 237.023 212.381 183.667 1.00 37.65  ? 4633 ARG A NE    1 
ATOM   22812 C  CZ    . ARG A 1 4633 ? 236.519 213.600 183.796 1.00 38.23  ? 4633 ARG A CZ    1 
ATOM   22813 N  NH1   . ARG A 1 4633 ? 236.125 214.065 184.972 1.00 30.57  ? 4633 ARG A NH1   1 
ATOM   22814 N  NH2   . ARG A 1 4633 ? 236.403 214.372 182.721 1.00 44.73  ? 4633 ARG A NH2   1 
ATOM   22815 N  N     . SER A 1 4634 ? 241.246 209.333 186.331 1.00 25.52  ? 4634 SER A N     1 
ATOM   22816 C  CA    . SER A 1 4634 ? 241.556 208.393 187.402 1.00 21.15  ? 4634 SER A CA    1 
ATOM   22817 C  C     . SER A 1 4634 ? 242.141 209.094 188.621 1.00 17.58  ? 4634 SER A C     1 
ATOM   22818 O  O     . SER A 1 4634 ? 241.901 208.664 189.755 1.00 17.98  ? 4634 SER A O     1 
ATOM   22819 C  CB    . SER A 1 4634 ? 242.521 207.323 186.894 1.00 20.72  ? 4634 SER A CB    1 
ATOM   22820 O  OG    . SER A 1 4634 ? 243.863 207.754 187.018 1.00 20.83  ? 4634 SER A OG    1 
ATOM   22821 N  N     . PHE A 1 4635 ? 242.928 210.155 188.414 1.00 21.30  ? 4635 PHE A N     1 
ATOM   22822 C  CA    . PHE A 1 4635 ? 243.383 210.961 189.542 1.00 15.76  ? 4635 PHE A CA    1 
ATOM   22823 C  C     . PHE A 1 4635 ? 242.201 211.513 190.324 1.00 16.50  ? 4635 PHE A C     1 
ATOM   22824 O  O     . PHE A 1 4635 ? 242.223 211.548 191.560 1.00 12.44  ? 4635 PHE A O     1 
ATOM   22825 C  CB    . PHE A 1 4635 ? 244.275 212.106 189.062 1.00 15.55  ? 4635 PHE A CB    1 
ATOM   22826 C  CG    . PHE A 1 4635 ? 245.724 211.742 188.936 1.00 15.50  ? 4635 PHE A CG    1 
ATOM   22827 C  CD1   . PHE A 1 4635 ? 246.172 210.973 187.878 1.00 20.26  ? 4635 PHE A CD1   1 
ATOM   22828 C  CD2   . PHE A 1 4635 ? 246.642 212.184 189.872 1.00 13.95  ? 4635 PHE A CD2   1 
ATOM   22829 C  CE1   . PHE A 1 4635 ? 247.508 210.644 187.763 1.00 24.15  ? 4635 PHE A CE1   1 
ATOM   22830 C  CE2   . PHE A 1 4635 ? 247.977 211.857 189.762 1.00 18.35  ? 4635 PHE A CE2   1 
ATOM   22831 C  CZ    . PHE A 1 4635 ? 248.411 211.087 188.706 1.00 22.09  ? 4635 PHE A CZ    1 
ATOM   22832 N  N     . TYR A 1 4636 ? 241.160 211.955 189.616 1.00 19.30  ? 4636 TYR A N     1 
ATOM   22833 C  CA    . TYR A 1 4636 ? 239.943 212.388 190.293 1.00 12.00  ? 4636 TYR A CA    1 
ATOM   22834 C  C     . TYR A 1 4636 ? 239.288 211.235 191.045 1.00 15.55  ? 4636 TYR A C     1 
ATOM   22835 O  O     . TYR A 1 4636 ? 238.830 211.411 192.179 1.00 14.32  ? 4636 TYR A O     1 
ATOM   22836 C  CB    . TYR A 1 4636 ? 238.960 212.992 189.292 1.00 13.75  ? 4636 TYR A CB    1 
ATOM   22837 C  CG    . TYR A 1 4636 ? 239.514 214.140 188.482 1.00 16.08  ? 4636 TYR A CG    1 
ATOM   22838 C  CD1   . TYR A 1 4636 ? 240.535 214.939 188.977 1.00 12.41  ? 4636 TYR A CD1   1 
ATOM   22839 C  CD2   . TYR A 1 4636 ? 239.014 214.425 187.220 1.00 21.51  ? 4636 TYR A CD2   1 
ATOM   22840 C  CE1   . TYR A 1 4636 ? 241.041 215.985 188.236 1.00 13.77  ? 4636 TYR A CE1   1 
ATOM   22841 C  CE2   . TYR A 1 4636 ? 239.514 215.470 186.472 1.00 21.56  ? 4636 TYR A CE2   1 
ATOM   22842 C  CZ    . TYR A 1 4636 ? 240.527 216.246 186.985 1.00 19.18  ? 4636 TYR A CZ    1 
ATOM   22843 O  OH    . TYR A 1 4636 ? 241.028 217.289 186.243 1.00 27.03  ? 4636 TYR A OH    1 
ATOM   22844 N  N     . GLU A 1 4637 ? 239.231 210.048 190.429 1.00 20.66  ? 4637 GLU A N     1 
ATOM   22845 C  CA    . GLU A 1 4637 ? 238.550 208.926 191.076 1.00 13.84  ? 4637 GLU A CA    1 
ATOM   22846 C  C     . GLU A 1 4637 ? 239.257 208.463 192.345 1.00 9.25   ? 4637 GLU A C     1 
ATOM   22847 O  O     . GLU A 1 4637 ? 238.596 208.010 193.285 1.00 11.53  ? 4637 GLU A O     1 
ATOM   22848 C  CB    . GLU A 1 4637 ? 238.409 207.744 190.118 1.00 17.47  ? 4637 GLU A CB    1 
ATOM   22849 C  CG    . GLU A 1 4637 ? 237.885 208.090 188.747 1.00 29.21  ? 4637 GLU A CG    1 
ATOM   22850 C  CD    . GLU A 1 4637 ? 237.797 206.882 187.838 1.00 38.89  ? 4637 GLU A CD    1 
ATOM   22851 O  OE1   . GLU A 1 4637 ? 237.949 205.748 188.339 1.00 37.65  ? 4637 GLU A OE1   1 
ATOM   22852 O  OE2   . GLU A 1 4637 ? 237.574 207.064 186.624 1.00 34.22  ? 4637 GLU A OE2   1 
ATOM   22853 N  N     . ARG A 1 4638 ? 240.582 208.557 192.396 1.00 10.10  ? 4638 ARG A N     1 
ATOM   22854 C  CA    . ARG A 1 4638 ? 241.342 208.008 193.512 1.00 11.06  ? 4638 ARG A CA    1 
ATOM   22855 C  C     . ARG A 1 4638 ? 241.521 208.989 194.664 1.00 10.42  ? 4638 ARG A C     1 
ATOM   22856 O  O     . ARG A 1 4638 ? 242.188 208.648 195.646 1.00 9.61   ? 4638 ARG A O     1 
ATOM   22857 C  CB    . ARG A 1 4638 ? 242.710 207.518 193.029 1.00 8.70   ? 4638 ARG A CB    1 
ATOM   22858 C  CG    . ARG A 1 4638 ? 242.621 206.343 192.076 1.00 9.40   ? 4638 ARG A CG    1 
ATOM   22859 C  CD    . ARG A 1 4638 ? 243.981 205.887 191.600 1.00 14.52  ? 4638 ARG A CD    1 
ATOM   22860 N  NE    . ARG A 1 4638 ? 244.851 205.492 192.699 1.00 15.56  ? 4638 ARG A NE    1 
ATOM   22861 C  CZ    . ARG A 1 4638 ? 245.493 204.335 192.763 1.00 15.05  ? 4638 ARG A CZ    1 
ATOM   22862 N  NH1   . ARG A 1 4638 ? 245.368 203.422 191.814 1.00 13.50  ? 4638 ARG A NH1   1 
ATOM   22863 N  NH2   . ARG A 1 4638 ? 246.283 204.088 193.804 1.00 23.07  ? 4638 ARG A NH2   1 
ATOM   22864 N  N     . GLY A 1 4639 ? 240.944 210.182 194.576 1.00 10.84  ? 4639 GLY A N     1 
ATOM   22865 C  CA    . GLY A 1 4639 ? 241.018 211.139 195.667 1.00 7.46   ? 4639 GLY A CA    1 
ATOM   22866 C  C     . GLY A 1 4639 ? 242.405 211.663 195.962 1.00 7.39   ? 4639 GLY A C     1 
ATOM   22867 O  O     . GLY A 1 4639 ? 242.786 211.767 197.135 1.00 12.41  ? 4639 GLY A O     1 
ATOM   22868 N  N     . VAL A 1 4640 ? 243.171 211.996 194.931 1.00 7.14   ? 4640 VAL A N     1 
ATOM   22869 C  CA    . VAL A 1 4640 ? 244.517 212.527 195.113 1.00 7.30   ? 4640 VAL A CA    1 
ATOM   22870 C  C     . VAL A 1 4640 ? 244.421 213.987 195.532 1.00 7.94   ? 4640 VAL A C     1 
ATOM   22871 O  O     . VAL A 1 4640 ? 243.727 214.785 194.892 1.00 9.97   ? 4640 VAL A O     1 
ATOM   22872 C  CB    . VAL A 1 4640 ? 245.342 212.368 193.827 1.00 7.10   ? 4640 VAL A CB    1 
ATOM   22873 C  CG1   . VAL A 1 4640 ? 246.746 212.900 194.026 1.00 7.25   ? 4640 VAL A CG1   1 
ATOM   22874 C  CG2   . VAL A 1 4640 ? 245.376 210.911 193.402 1.00 8.21   ? 4640 VAL A CG2   1 
ATOM   22875 N  N     . ALA A 1 4641 ? 245.114 214.341 196.610 1.00 7.42   ? 4641 ALA A N     1 
ATOM   22876 C  CA    . ALA A 1 4641 ? 245.073 215.698 197.137 1.00 8.27   ? 4641 ALA A CA    1 
ATOM   22877 C  C     . ALA A 1 4641 ? 246.401 215.996 197.825 1.00 10.68  ? 4641 ALA A C     1 
ATOM   22878 O  O     . ALA A 1 4641 ? 247.334 215.189 197.793 1.00 12.57  ? 4641 ALA A O     1 
ATOM   22879 C  CB    . ALA A 1 4641 ? 243.879 215.873 198.085 1.00 6.89   ? 4641 ALA A CB    1 
ATOM   22880 N  N     . VAL A 1 4642 ? 246.486 217.171 198.444 1.00 11.29  ? 4642 VAL A N     1 
ATOM   22881 C  CA    . VAL A 1 4642 ? 247.665 217.599 199.184 1.00 8.89   ? 4642 VAL A CA    1 
ATOM   22882 C  C     . VAL A 1 4642 ? 247.232 218.013 200.582 1.00 9.12   ? 4642 VAL A C     1 
ATOM   22883 O  O     . VAL A 1 4642 ? 246.230 218.716 200.751 1.00 8.65   ? 4642 VAL A O     1 
ATOM   22884 C  CB    . VAL A 1 4642 ? 248.403 218.754 198.474 1.00 7.11   ? 4642 VAL A CB    1 
ATOM   22885 C  CG1   . VAL A 1 4642 ? 249.668 219.122 199.228 1.00 8.62   ? 4642 VAL A CG1   1 
ATOM   22886 C  CG2   . VAL A 1 4642 ? 248.730 218.376 197.040 1.00 8.78   ? 4642 VAL A CG2   1 
ATOM   22887 N  N     . LEU A 1 4643 ? 247.978 217.562 201.585 1.00 10.01  ? 4643 LEU A N     1 
ATOM   22888 C  CA    . LEU A 1 4643 ? 247.717 217.877 202.982 1.00 10.61  ? 4643 LEU A CA    1 
ATOM   22889 C  C     . LEU A 1 4643 ? 248.838 218.755 203.519 1.00 11.06  ? 4643 LEU A C     1 
ATOM   22890 O  O     . LEU A 1 4643 ? 250.019 218.463 203.303 1.00 11.64  ? 4643 LEU A O     1 
ATOM   22891 C  CB    . LEU A 1 4643 ? 247.598 216.604 203.822 1.00 14.02  ? 4643 LEU A CB    1 
ATOM   22892 C  CG    . LEU A 1 4643 ? 246.561 215.562 203.404 1.00 9.44   ? 4643 LEU A CG    1 
ATOM   22893 C  CD1   . LEU A 1 4643 ? 246.417 214.510 204.484 1.00 8.28   ? 4643 LEU A CD1   1 
ATOM   22894 C  CD2   . LEU A 1 4643 ? 245.224 216.218 203.111 1.00 11.46  ? 4643 LEU A CD2   1 
ATOM   22895 N  N     . CYS A 1 4644 ? 248.463 219.829 204.217 1.00 14.08  ? 4644 CYS A N     1 
ATOM   22896 C  CA    . CYS A 1 4644 ? 249.456 220.732 204.788 1.00 16.75  ? 4644 CYS A CA    1 
ATOM   22897 C  C     . CYS A 1 4644 ? 250.165 220.129 205.991 1.00 18.78  ? 4644 CYS A C     1 
ATOM   22898 O  O     . CYS A 1 4644 ? 251.284 220.546 206.308 1.00 24.92  ? 4644 CYS A O     1 
ATOM   22899 C  CB    . CYS A 1 4644 ? 248.797 222.055 205.180 1.00 12.24  ? 4644 CYS A CB    1 
ATOM   22900 S  SG    . CYS A 1 4644 ? 248.310 223.083 203.780 1.00 29.44  ? 4644 CYS A SG    1 
ATOM   22901 N  N     . THR A 1 4645 ? 249.547 219.167 206.667 1.00 16.48  ? 4645 THR A N     1 
ATOM   22902 C  CA    . THR A 1 4645 ? 250.165 218.512 207.812 1.00 19.53  ? 4645 THR A CA    1 
ATOM   22903 C  C     . THR A 1 4645 ? 249.601 217.110 207.999 1.00 14.88  ? 4645 THR A C     1 
ATOM   22904 O  O     . THR A 1 4645 ? 248.582 216.757 207.406 1.00 13.71  ? 4645 THR A O     1 
ATOM   22905 C  CB    . THR A 1 4645 ? 249.960 219.318 209.108 1.00 25.20  ? 4645 THR A CB    1 
ATOM   22906 O  OG1   . THR A 1 4645 ? 250.572 218.629 210.204 1.00 32.99  ? 4645 THR A OG1   1 
ATOM   22907 C  CG2   . THR A 1 4645 ? 248.479 219.497 209.397 1.00 17.88  ? 4645 THR A CG2   1 
HETATM 22908 P  PB    . ADP B 2 .    ? 220.634 233.571 201.749 1.00 2.49   ? 4701 ADP A PB    1 
HETATM 22909 O  O1B   . ADP B 2 .    ? 220.501 233.816 203.231 1.00 7.62   ? 4701 ADP A O1B   1 
HETATM 22910 O  O2B   . ADP B 2 .    ? 221.918 232.872 201.382 1.00 5.48   ? 4701 ADP A O2B   1 
HETATM 22911 O  O3B   . ADP B 2 .    ? 219.418 232.906 201.161 1.00 7.64   ? 4701 ADP A O3B   1 
HETATM 22912 P  PA    . ADP B 2 .    ? 219.524 236.038 200.670 1.00 9.53   ? 4701 ADP A PA    1 
HETATM 22913 O  O1A   . ADP B 2 .    ? 218.812 235.491 199.479 1.00 3.14   ? 4701 ADP A O1A   1 
HETATM 22914 O  O2A   . ADP B 2 .    ? 218.722 236.333 201.893 1.00 18.12  ? 4701 ADP A O2A   1 
HETATM 22915 O  O3A   . ADP B 2 .    ? 220.700 235.025 201.064 1.00 7.35   ? 4701 ADP A O3A   1 
HETATM 22916 O  "O5'" . ADP B 2 .    ? 220.359 237.341 200.253 1.00 9.22   ? 4701 ADP A "O5'" 1 
HETATM 22917 C  "C5'" . ADP B 2 .    ? 221.417 237.195 199.276 1.00 8.61   ? 4701 ADP A "C5'" 1 
HETATM 22918 C  "C4'" . ADP B 2 .    ? 221.999 238.549 198.962 1.00 8.99   ? 4701 ADP A "C4'" 1 
HETATM 22919 O  "O4'" . ADP B 2 .    ? 222.784 238.445 197.747 1.00 11.14  ? 4701 ADP A "O4'" 1 
HETATM 22920 C  "C3'" . ADP B 2 .    ? 220.985 239.656 198.661 1.00 9.82   ? 4701 ADP A "C3'" 1 
HETATM 22921 O  "O3'" . ADP B 2 .    ? 221.564 240.940 198.844 1.00 20.60  ? 4701 ADP A "O3'" 1 
HETATM 22922 C  "C2'" . ADP B 2 .    ? 220.704 239.381 197.184 1.00 9.04   ? 4701 ADP A "C2'" 1 
HETATM 22923 O  "O2'" . ADP B 2 .    ? 220.105 240.465 196.507 1.00 18.89  ? 4701 ADP A "O2'" 1 
HETATM 22924 C  "C1'" . ADP B 2 .    ? 222.115 239.089 196.685 1.00 7.94   ? 4701 ADP A "C1'" 1 
HETATM 22925 N  N9    . ADP B 2 .    ? 222.146 238.210 195.523 1.00 4.91   ? 4701 ADP A N9    1 
HETATM 22926 C  C8    . ADP B 2 .    ? 222.125 236.839 195.533 1.00 3.86   ? 4701 ADP A C8    1 
HETATM 22927 N  N7    . ADP B 2 .    ? 222.163 236.310 194.337 1.00 3.38   ? 4701 ADP A N7    1 
HETATM 22928 C  C5    . ADP B 2 .    ? 222.210 237.401 193.481 1.00 2.89   ? 4701 ADP A C5    1 
HETATM 22929 C  C6    . ADP B 2 .    ? 222.263 237.500 192.079 1.00 3.52   ? 4701 ADP A C6    1 
HETATM 22930 N  N6    . ADP B 2 .    ? 222.279 236.450 191.264 1.00 3.36   ? 4701 ADP A N6    1 
HETATM 22931 N  N1    . ADP B 2 .    ? 222.301 238.742 191.543 1.00 4.92   ? 4701 ADP A N1    1 
HETATM 22932 C  C2    . ADP B 2 .    ? 222.286 239.795 192.368 1.00 3.91   ? 4701 ADP A C2    1 
HETATM 22933 N  N3    . ADP B 2 .    ? 222.237 239.823 193.697 1.00 5.28   ? 4701 ADP A N3    1 
HETATM 22934 C  C4    . ADP B 2 .    ? 222.201 238.579 194.201 1.00 4.35   ? 4701 ADP A C4    1 
HETATM 22935 P  PG    . ATP C 3 .    ? 228.073 249.851 227.056 1.00 3.19   ? 4702 ATP A PG    1 
HETATM 22936 O  O1G   . ATP C 3 .    ? 228.842 248.879 226.201 1.00 4.96   ? 4702 ATP A O1G   1 
HETATM 22937 O  O2G   . ATP C 3 .    ? 226.625 249.962 226.656 1.00 5.55   ? 4702 ATP A O2G   1 
HETATM 22938 O  O3G   . ATP C 3 .    ? 228.249 249.594 228.530 1.00 3.79   ? 4702 ATP A O3G   1 
HETATM 22939 P  PB    . ATP C 3 .    ? 229.046 252.129 225.450 1.00 2.14   ? 4702 ATP A PB    1 
HETATM 22940 O  O1B   . ATP C 3 .    ? 230.208 251.494 224.765 1.00 3.23   ? 4702 ATP A O1B   1 
HETATM 22941 O  O2B   . ATP C 3 .    ? 227.774 252.345 224.702 1.00 3.48   ? 4702 ATP A O2B   1 
HETATM 22942 O  O3B   . ATP C 3 .    ? 228.722 251.301 226.781 1.00 2.54   ? 4702 ATP A O3B   1 
HETATM 22943 P  PA    . ATP C 3 .    ? 228.665 254.763 226.637 1.00 2.98   ? 4702 ATP A PA    1 
HETATM 22944 O  O1A   . ATP C 3 .    ? 227.387 254.245 227.205 1.00 7.55   ? 4702 ATP A O1A   1 
HETATM 22945 O  O2A   . ATP C 3 .    ? 228.598 255.814 225.580 1.00 2.65   ? 4702 ATP A O2A   1 
HETATM 22946 O  O3A   . ATP C 3 .    ? 229.512 253.522 226.079 1.00 2.03   ? 4702 ATP A O3A   1 
HETATM 22947 O  "O5'" . ATP C 3 .    ? 229.605 255.265 227.834 1.00 8.38   ? 4702 ATP A "O5'" 1 
HETATM 22948 C  "C5'" . ATP C 3 .    ? 230.865 255.907 227.521 1.00 6.00   ? 4702 ATP A "C5'" 1 
HETATM 22949 C  "C4'" . ATP C 3 .    ? 231.351 256.647 228.739 1.00 6.31   ? 4702 ATP A "C4'" 1 
HETATM 22950 O  "O4'" . ATP C 3 .    ? 232.199 257.744 228.318 1.00 11.01  ? 4702 ATP A "O4'" 1 
HETATM 22951 C  "C3'" . ATP C 3 .    ? 230.265 257.342 229.561 1.00 6.16   ? 4702 ATP A "C3'" 1 
HETATM 22952 O  "O3'" . ATP C 3 .    ? 230.751 257.712 230.844 1.00 27.38  ? 4702 ATP A "O3'" 1 
HETATM 22953 C  "C2'" . ATP C 3 .    ? 230.014 258.571 228.688 1.00 5.23   ? 4702 ATP A "C2'" 1 
HETATM 22954 O  "O2'" . ATP C 3 .    ? 229.374 259.623 229.379 1.00 7.83   ? 4702 ATP A "O2'" 1 
HETATM 22955 C  "C1'" . ATP C 3 .    ? 231.437 258.932 228.265 1.00 5.53   ? 4702 ATP A "C1'" 1 
HETATM 22956 N  N9    . ATP C 3 .    ? 231.519 259.460 226.910 1.00 5.84   ? 4702 ATP A N9    1 
HETATM 22957 C  C8    . ATP C 3 .    ? 230.960 258.933 225.775 1.00 5.63   ? 4702 ATP A C8    1 
HETATM 22958 N  N7    . ATP C 3 .    ? 231.206 259.658 224.707 1.00 5.05   ? 4702 ATP A N7    1 
HETATM 22959 C  C5    . ATP C 3 .    ? 231.956 260.729 225.176 1.00 5.01   ? 4702 ATP A C5    1 
HETATM 22960 C  C6    . ATP C 3 .    ? 232.523 261.848 224.537 1.00 4.96   ? 4702 ATP A C6    1 
HETATM 22961 N  N6    . ATP C 3 .    ? 232.417 262.086 223.234 1.00 5.58   ? 4702 ATP A N6    1 
HETATM 22962 N  N1    . ATP C 3 .    ? 233.213 262.720 225.309 1.00 5.83   ? 4702 ATP A N1    1 
HETATM 22963 C  C2    . ATP C 3 .    ? 233.313 262.476 226.622 1.00 5.80   ? 4702 ATP A C2    1 
HETATM 22964 N  N3    . ATP C 3 .    ? 232.825 261.461 227.329 1.00 7.00   ? 4702 ATP A N3    1 
HETATM 22965 C  C4    . ATP C 3 .    ? 232.148 260.615 226.536 1.00 7.45   ? 4702 ATP A C4    1 
HETATM 22966 P  PB    . ADP D 2 .    ? 227.900 237.368 254.561 1.00 5.89   ? 4703 ADP A PB    1 
HETATM 22967 O  O1B   . ADP D 2 .    ? 227.132 238.617 254.220 1.00 8.20   ? 4703 ADP A O1B   1 
HETATM 22968 O  O2B   . ADP D 2 .    ? 227.196 236.109 254.121 1.00 21.87  ? 4703 ADP A O2B   1 
HETATM 22969 O  O3B   . ADP D 2 .    ? 229.336 237.425 254.106 1.00 7.58   ? 4703 ADP A O3B   1 
HETATM 22970 P  PA    . ADP D 2 .    ? 226.804 237.514 257.272 1.00 11.09  ? 4703 ADP A PA    1 
HETATM 22971 O  O1A   . ADP D 2 .    ? 226.582 238.978 257.460 1.00 7.09   ? 4703 ADP A O1A   1 
HETATM 22972 O  O2A   . ADP D 2 .    ? 225.632 236.664 256.907 1.00 13.46  ? 4703 ADP A O2A   1 
HETATM 22973 O  O3A   . ADP D 2 .    ? 227.947 237.307 256.170 1.00 13.06  ? 4703 ADP A O3A   1 
HETATM 22974 O  "O5'" . ADP D 2 .    ? 227.516 236.909 258.573 1.00 10.71  ? 4703 ADP A "O5'" 1 
HETATM 22975 C  "C5'" . ADP D 2 .    ? 228.809 237.433 258.958 1.00 8.25   ? 4703 ADP A "C5'" 1 
HETATM 22976 C  "C4'" . ADP D 2 .    ? 229.246 236.768 260.239 1.00 8.83   ? 4703 ADP A "C4'" 1 
HETATM 22977 O  "O4'" . ADP D 2 .    ? 230.457 237.412 260.714 1.00 11.61  ? 4703 ADP A "O4'" 1 
HETATM 22978 C  "C3'" . ADP D 2 .    ? 228.253 236.852 261.404 1.00 8.44   ? 4703 ADP A "C3'" 1 
HETATM 22979 O  "O3'" . ADP D 2 .    ? 228.301 235.676 262.198 1.00 11.80  ? 4703 ADP A "O3'" 1 
HETATM 22980 C  "C2'" . ADP D 2 .    ? 228.783 238.052 262.188 1.00 6.93   ? 4703 ADP A "C2'" 1 
HETATM 22981 O  "O2'" . ADP D 2 .    ? 228.358 238.065 263.534 1.00 14.58  ? 4703 ADP A "O2'" 1 
HETATM 22982 C  "C1'" . ADP D 2 .    ? 230.283 237.827 262.048 1.00 8.50   ? 4703 ADP A "C1'" 1 
HETATM 22983 N  N9    . ADP D 2 .    ? 231.083 239.027 262.258 1.00 7.06   ? 4703 ADP A N9    1 
HETATM 22984 C  C8    . ADP D 2 .    ? 232.161 239.421 261.507 1.00 6.94   ? 4703 ADP A C8    1 
HETATM 22985 N  N7    . ADP D 2 .    ? 232.699 240.541 261.916 1.00 9.18   ? 4703 ADP A N7    1 
HETATM 22986 C  C5    . ADP D 2 .    ? 231.938 240.906 263.016 1.00 8.90   ? 4703 ADP A C5    1 
HETATM 22987 C  C6    . ADP D 2 .    ? 232.009 242.007 263.891 1.00 11.31  ? 4703 ADP A C6    1 
HETATM 22988 N  N6    . ADP D 2 .    ? 232.918 242.973 263.793 1.00 11.25  ? 4703 ADP A N6    1 
HETATM 22989 N  N1    . ADP D 2 .    ? 231.097 242.071 264.889 1.00 14.99  ? 4703 ADP A N1    1 
HETATM 22990 C  C2    . ADP D 2 .    ? 230.185 241.097 264.984 1.00 10.12  ? 4703 ADP A C2    1 
HETATM 22991 N  N3    . ADP D 2 .    ? 230.023 240.020 264.222 1.00 8.01   ? 4703 ADP A N3    1 
HETATM 22992 C  C4    . ADP D 2 .    ? 230.940 239.978 263.242 1.00 7.48   ? 4703 ADP A C4    1 
HETATM 22993 P  PB    . ADP E 2 .    ? 214.435 208.237 256.337 1.00 13.76  ? 4704 ADP A PB    1 
HETATM 22994 O  O1B   . ADP E 2 .    ? 215.668 208.231 257.205 1.00 18.32  ? 4704 ADP A O1B   1 
HETATM 22995 O  O2B   . ADP E 2 .    ? 213.604 209.481 256.514 1.00 12.96  ? 4704 ADP A O2B   1 
HETATM 22996 O  O3B   . ADP E 2 .    ? 214.736 207.937 254.892 1.00 15.20  ? 4704 ADP A O3B   1 
HETATM 22997 P  PA    . ADP E 2 .    ? 212.216 206.940 257.790 1.00 20.78  ? 4704 ADP A PA    1 
HETATM 22998 O  O1A   . ADP E 2 .    ? 212.495 207.608 259.094 1.00 9.45   ? 4704 ADP A O1A   1 
HETATM 22999 O  O2A   . ADP E 2 .    ? 211.039 207.406 256.998 1.00 23.05  ? 4704 ADP A O2A   1 
HETATM 23000 O  O3A   . ADP E 2 .    ? 213.521 207.018 256.861 1.00 26.51  ? 4704 ADP A O3A   1 
HETATM 23001 O  "O5'" . ADP E 2 .    ? 212.114 205.356 258.011 1.00 18.69  ? 4704 ADP A "O5'" 1 
HETATM 23002 C  "C5'" . ADP E 2 .    ? 211.025 204.837 258.811 1.00 23.50  ? 4704 ADP A "C5'" 1 
HETATM 23003 C  "C4'" . ADP E 2 .    ? 211.076 203.330 258.809 1.00 16.26  ? 4704 ADP A "C4'" 1 
HETATM 23004 O  "O4'" . ADP E 2 .    ? 212.360 202.904 259.332 1.00 16.93  ? 4704 ADP A "O4'" 1 
HETATM 23005 C  "C3'" . ADP E 2 .    ? 210.047 202.633 259.703 1.00 15.02  ? 4704 ADP A "C3'" 1 
HETATM 23006 O  "O3'" . ADP E 2 .    ? 209.816 201.299 259.271 1.00 24.13  ? 4704 ADP A "O3'" 1 
HETATM 23007 C  "C2'" . ADP E 2 .    ? 210.776 202.659 261.046 1.00 20.19  ? 4704 ADP A "C2'" 1 
HETATM 23008 O  "O2'" . ADP E 2 .    ? 210.262 201.738 261.985 1.00 31.92  ? 4704 ADP A "O2'" 1 
HETATM 23009 C  "C1'" . ADP E 2 .    ? 212.189 202.303 260.597 1.00 17.29  ? 4704 ADP A "C1'" 1 
HETATM 23010 N  N9    . ADP E 2 .    ? 213.231 202.797 261.487 1.00 15.28  ? 4704 ADP A N9    1 
HETATM 23011 C  C8    . ADP E 2 .    ? 213.889 203.997 261.392 1.00 16.62  ? 4704 ADP A C8    1 
HETATM 23012 N  N7    . ADP E 2 .    ? 214.775 204.180 262.338 1.00 18.05  ? 4704 ADP A N7    1 
HETATM 23013 C  C5    . ADP E 2 .    ? 214.691 203.034 263.114 1.00 14.73  ? 4704 ADP A C5    1 
HETATM 23014 C  C6    . ADP E 2 .    ? 215.377 202.624 264.273 1.00 16.81  ? 4704 ADP A C6    1 
HETATM 23015 N  N6    . ADP E 2 .    ? 216.315 203.350 264.873 1.00 20.32  ? 4704 ADP A N6    1 
HETATM 23016 N  N1    . ADP E 2 .    ? 215.052 201.418 264.797 1.00 16.32  ? 4704 ADP A N1    1 
HETATM 23017 C  C2    . ADP E 2 .    ? 214.107 200.692 264.188 1.00 16.38  ? 4704 ADP A C2    1 
HETATM 23018 N  N3    . ADP E 2 .    ? 213.399 200.974 263.099 1.00 14.56  ? 4704 ADP A N3    1 
HETATM 23019 C  C4    . ADP E 2 .    ? 213.740 202.173 262.602 1.00 13.56  ? 4704 ADP A C4    1 
HETATM 23020 MG MG    . MG  F 4 .    ? 225.497 251.681 226.057 1.00 2.69   ? 4705 MG  A MG    1 
# 
