data_9BLZ
# 
_entry.id   9BLZ 
# 
_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   9BLZ         pdb_00009blz 10.2210/pdb9blz/pdb 
WWPDB D_1000283514 ?            ?                   
EMDB  EMD-44682    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1  'Structure model' 1 0 2025-04-23 ? 
2  'EM metadata'     1 0 2025-04-23 ? 
3  'Additional map'  1 0 2025-04-23 1 
4  FSC               1 0 2025-04-23 ? 
5  'Half map'        1 0 2025-04-23 1 
6  'Half map'        1 0 2025-04-23 2 
7  Image             1 0 2025-04-23 ? 
8  Mask              1 0 2025-04-23 1 
9  'Primary map'     1 0 2025-04-23 ? 
10 'Structure model' 1 1 2025-04-30 ? 
11 'Structure model' 1 2 2025-05-21 ? 
12 'EM metadata'     1 1 2025-05-21 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Additional map'  repository 'Initial release' ? ? 
4 4 FSC               repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 'Half map'        repository 'Initial release' ? ? 
7 7 Image             repository 'Initial release' ? ? 
8 8 Mask              repository 'Initial release' ? ? 
9 9 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 10 'Structure model' 'Data collection'      
2 10 'Structure model' 'Database references'  
3 11 'Structure model' 'Data collection'      
4 12 'EM metadata'     'Data processing'      
5 12 'EM metadata'     'Experimental summary' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 10 'Structure model' citation        
2 10 'Structure model' citation_author 
3 10 'Structure model' em_admin        
4 11 'Structure model' em_admin        
5 11 'Structure model' em_software     
6 12 'EM metadata'     em_admin        
7 12 'EM metadata'     em_software     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  10 'Structure model' '_citation.country'                 
2  10 'Structure model' '_citation.journal_abbrev'          
3  10 'Structure model' '_citation.journal_id_CSD'          
4  10 'Structure model' '_citation.journal_id_ISSN'         
5  10 'Structure model' '_citation.pdbx_database_id_DOI'    
6  10 'Structure model' '_citation.pdbx_database_id_PubMed' 
7  10 'Structure model' '_citation.title'                   
8  10 'Structure model' '_citation.year'                    
9  10 'Structure model' '_em_admin.last_update'             
10 11 'Structure model' '_em_admin.last_update'             
11 11 'Structure model' '_em_software.name'                 
12 12 'EM metadata'     '_em_admin.last_update'             
13 12 'EM metadata'     '_em_software.name'                 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BLZ 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'State-1(phi motor) of full-length human dynein-1 in 5mM ATP' 
_pdbx_database_related.db_id          EMD-44682 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jack.zhang@yale.edu 
_pdbx_contact_author.name_first         Jack 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8617-2855 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chai, P.'  1 0000-0001-9702-978X 
'Zhang, K.' 2 0000-0001-8617-2855 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'The mechanochemical cycle of reactive full-length human dynein 1.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-025-01543-3 
_citation.pdbx_database_id_PubMed   40263469 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chai, P.'       1 0000-0001-9702-978X 
primary 'Yang, J.'       2 ?                   
primary 'Geohring, I.C.' 3 ?                   
primary 'Markus, S.M.'   4 0000-0002-3098-0236 
primary 'Wang, Y.'       5 0000-0002-8020-3937 
primary 'Zhang, K.'      6 0000-0001-8617-2855 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Cytoplasmic dynein 1 heavy chain 1' 533083.250 1    ? ? ? ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"           427.201    3    ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"          507.181    1    ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                      24.305     2    ? ? ? ? 
5 water       nat water                                18.015     1857 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytoplasmic dynein heavy chain 1,Dynein heavy chain,cytosolic' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 'MAGNESIUM ION'             MG  
5 water                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    SER n 
1 3    GLU n 
1 4    PRO n 
1 5    GLY n 
1 6    GLY n 
1 7    GLY n 
1 8    GLY n 
1 9    GLY n 
1 10   GLU n 
1 11   ASP n 
1 12   GLY n 
1 13   SER n 
1 14   ALA n 
1 15   GLY n 
1 16   LEU n 
1 17   GLU n 
1 18   VAL n 
1 19   SER n 
1 20   ALA n 
1 21   VAL n 
1 22   GLN n 
1 23   ASN n 
1 24   VAL n 
1 25   ALA n 
1 26   ASP n 
1 27   VAL n 
1 28   SER n 
1 29   VAL n 
1 30   LEU n 
1 31   GLN n 
1 32   LYS n 
1 33   HIS n 
1 34   LEU n 
1 35   ARG n 
1 36   LYS n 
1 37   LEU n 
1 38   VAL n 
1 39   PRO n 
1 40   LEU n 
1 41   LEU n 
1 42   LEU n 
1 43   GLU n 
1 44   ASP n 
1 45   GLY n 
1 46   GLY n 
1 47   GLU n 
1 48   ALA n 
1 49   PRO n 
1 50   ALA n 
1 51   ALA n 
1 52   LEU n 
1 53   GLU n 
1 54   ALA n 
1 55   ALA n 
1 56   LEU n 
1 57   GLU n 
1 58   GLU n 
1 59   LYS n 
1 60   SER n 
1 61   ALA n 
1 62   LEU n 
1 63   GLU n 
1 64   GLN n 
1 65   MET n 
1 66   ARG n 
1 67   LYS n 
1 68   PHE n 
1 69   LEU n 
1 70   SER n 
1 71   ASP n 
1 72   PRO n 
1 73   GLN n 
1 74   VAL n 
1 75   HIS n 
1 76   THR n 
1 77   VAL n 
1 78   LEU n 
1 79   VAL n 
1 80   GLU n 
1 81   ARG n 
1 82   SER n 
1 83   THR n 
1 84   LEU n 
1 85   LYS n 
1 86   GLU n 
1 87   ASP n 
1 88   VAL n 
1 89   GLY n 
1 90   ASP n 
1 91   GLU n 
1 92   GLY n 
1 93   GLU n 
1 94   GLU n 
1 95   GLU n 
1 96   LYS n 
1 97   GLU n 
1 98   PHE n 
1 99   ILE n 
1 100  SER n 
1 101  TYR n 
1 102  ASN n 
1 103  ILE n 
1 104  ASN n 
1 105  ILE n 
1 106  ASP n 
1 107  ILE n 
1 108  HIS n 
1 109  TYR n 
1 110  GLY n 
1 111  VAL n 
1 112  LYS n 
1 113  SER n 
1 114  ASN n 
1 115  SER n 
1 116  LEU n 
1 117  ALA n 
1 118  PHE n 
1 119  ILE n 
1 120  LYS n 
1 121  ARG n 
1 122  THR n 
1 123  PRO n 
1 124  VAL n 
1 125  ILE n 
1 126  ASP n 
1 127  ALA n 
1 128  ASP n 
1 129  LYS n 
1 130  PRO n 
1 131  VAL n 
1 132  SER n 
1 133  SER n 
1 134  GLN n 
1 135  LEU n 
1 136  ARG n 
1 137  VAL n 
1 138  LEU n 
1 139  THR n 
1 140  LEU n 
1 141  SER n 
1 142  GLU n 
1 143  ASP n 
1 144  SER n 
1 145  PRO n 
1 146  TYR n 
1 147  GLU n 
1 148  THR n 
1 149  LEU n 
1 150  HIS n 
1 151  SER n 
1 152  PHE n 
1 153  ILE n 
1 154  SER n 
1 155  ASN n 
1 156  ALA n 
1 157  VAL n 
1 158  ALA n 
1 159  PRO n 
1 160  PHE n 
1 161  PHE n 
1 162  LYS n 
1 163  SER n 
1 164  TYR n 
1 165  ILE n 
1 166  ARG n 
1 167  GLU n 
1 168  SER n 
1 169  GLY n 
1 170  LYS n 
1 171  ALA n 
1 172  ASP n 
1 173  ARG n 
1 174  ASP n 
1 175  GLY n 
1 176  ASP n 
1 177  LYS n 
1 178  MET n 
1 179  ALA n 
1 180  PRO n 
1 181  SER n 
1 182  VAL n 
1 183  GLU n 
1 184  LYS n 
1 185  LYS n 
1 186  ILE n 
1 187  ALA n 
1 188  GLU n 
1 189  LEU n 
1 190  GLU n 
1 191  MET n 
1 192  GLY n 
1 193  LEU n 
1 194  LEU n 
1 195  HIS n 
1 196  LEU n 
1 197  GLN n 
1 198  GLN n 
1 199  ASN n 
1 200  ILE n 
1 201  GLU n 
1 202  ILE n 
1 203  PRO n 
1 204  GLU n 
1 205  ILE n 
1 206  SER n 
1 207  LEU n 
1 208  PRO n 
1 209  ILE n 
1 210  HIS n 
1 211  PRO n 
1 212  MET n 
1 213  ILE n 
1 214  THR n 
1 215  ASN n 
1 216  VAL n 
1 217  ALA n 
1 218  LYS n 
1 219  GLN n 
1 220  CYS n 
1 221  TYR n 
1 222  GLU n 
1 223  ARG n 
1 224  GLY n 
1 225  GLU n 
1 226  LYS n 
1 227  PRO n 
1 228  LYS n 
1 229  VAL n 
1 230  THR n 
1 231  ASP n 
1 232  PHE n 
1 233  GLY n 
1 234  ASP n 
1 235  LYS n 
1 236  VAL n 
1 237  GLU n 
1 238  ASP n 
1 239  PRO n 
1 240  THR n 
1 241  PHE n 
1 242  LEU n 
1 243  ASN n 
1 244  GLN n 
1 245  LEU n 
1 246  GLN n 
1 247  SER n 
1 248  GLY n 
1 249  VAL n 
1 250  ASN n 
1 251  ARG n 
1 252  TRP n 
1 253  ILE n 
1 254  ARG n 
1 255  GLU n 
1 256  ILE n 
1 257  GLN n 
1 258  LYS n 
1 259  VAL n 
1 260  THR n 
1 261  LYS n 
1 262  LEU n 
1 263  ASP n 
1 264  ARG n 
1 265  ASP n 
1 266  PRO n 
1 267  ALA n 
1 268  SER n 
1 269  GLY n 
1 270  THR n 
1 271  ALA n 
1 272  LEU n 
1 273  GLN n 
1 274  GLU n 
1 275  ILE n 
1 276  SER n 
1 277  PHE n 
1 278  TRP n 
1 279  LEU n 
1 280  ASN n 
1 281  LEU n 
1 282  GLU n 
1 283  ARG n 
1 284  ALA n 
1 285  LEU n 
1 286  TYR n 
1 287  ARG n 
1 288  ILE n 
1 289  GLN n 
1 290  GLU n 
1 291  LYS n 
1 292  ARG n 
1 293  GLU n 
1 294  SER n 
1 295  PRO n 
1 296  GLU n 
1 297  VAL n 
1 298  LEU n 
1 299  LEU n 
1 300  THR n 
1 301  LEU n 
1 302  ASP n 
1 303  ILE n 
1 304  LEU n 
1 305  LYS n 
1 306  HIS n 
1 307  GLY n 
1 308  LYS n 
1 309  ARG n 
1 310  PHE n 
1 311  HIS n 
1 312  ALA n 
1 313  THR n 
1 314  VAL n 
1 315  SER n 
1 316  PHE n 
1 317  ASP n 
1 318  THR n 
1 319  ASP n 
1 320  THR n 
1 321  GLY n 
1 322  LEU n 
1 323  LYS n 
1 324  GLN n 
1 325  ALA n 
1 326  LEU n 
1 327  GLU n 
1 328  THR n 
1 329  VAL n 
1 330  ASN n 
1 331  ASP n 
1 332  TYR n 
1 333  ASN n 
1 334  PRO n 
1 335  LEU n 
1 336  MET n 
1 337  LYS n 
1 338  ASP n 
1 339  PHE n 
1 340  PRO n 
1 341  LEU n 
1 342  ASN n 
1 343  ASP n 
1 344  LEU n 
1 345  LEU n 
1 346  SER n 
1 347  ALA n 
1 348  THR n 
1 349  GLU n 
1 350  LEU n 
1 351  ASP n 
1 352  LYS n 
1 353  ILE n 
1 354  ARG n 
1 355  GLN n 
1 356  ALA n 
1 357  LEU n 
1 358  VAL n 
1 359  ALA n 
1 360  ILE n 
1 361  PHE n 
1 362  THR n 
1 363  HIS n 
1 364  LEU n 
1 365  ARG n 
1 366  LYS n 
1 367  ILE n 
1 368  ARG n 
1 369  ASN n 
1 370  THR n 
1 371  LYS n 
1 372  TYR n 
1 373  PRO n 
1 374  ILE n 
1 375  GLN n 
1 376  ARG n 
1 377  ALA n 
1 378  LEU n 
1 379  ARG n 
1 380  LEU n 
1 381  VAL n 
1 382  GLU n 
1 383  ALA n 
1 384  ILE n 
1 385  SER n 
1 386  ARG n 
1 387  ASP n 
1 388  LEU n 
1 389  SER n 
1 390  SER n 
1 391  GLN n 
1 392  LEU n 
1 393  LEU n 
1 394  LYS n 
1 395  VAL n 
1 396  LEU n 
1 397  GLY n 
1 398  THR n 
1 399  ARG n 
1 400  LYS n 
1 401  LEU n 
1 402  MET n 
1 403  HIS n 
1 404  VAL n 
1 405  ALA n 
1 406  TYR n 
1 407  GLU n 
1 408  GLU n 
1 409  PHE n 
1 410  GLU n 
1 411  LYS n 
1 412  VAL n 
1 413  MET n 
1 414  VAL n 
1 415  ALA n 
1 416  CYS n 
1 417  PHE n 
1 418  GLU n 
1 419  VAL n 
1 420  PHE n 
1 421  GLN n 
1 422  THR n 
1 423  TRP n 
1 424  ASP n 
1 425  ASP n 
1 426  GLU n 
1 427  TYR n 
1 428  GLU n 
1 429  LYS n 
1 430  LEU n 
1 431  GLN n 
1 432  VAL n 
1 433  LEU n 
1 434  LEU n 
1 435  ARG n 
1 436  ASP n 
1 437  ILE n 
1 438  VAL n 
1 439  LYS n 
1 440  ARG n 
1 441  LYS n 
1 442  ARG n 
1 443  GLU n 
1 444  GLU n 
1 445  ASN n 
1 446  LEU n 
1 447  LYS n 
1 448  MET n 
1 449  VAL n 
1 450  TRP n 
1 451  ARG n 
1 452  ILE n 
1 453  ASN n 
1 454  PRO n 
1 455  ALA n 
1 456  HIS n 
1 457  ARG n 
1 458  LYS n 
1 459  LEU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  LEU n 
1 464  ASP n 
1 465  GLN n 
1 466  MET n 
1 467  ARG n 
1 468  LYS n 
1 469  PHE n 
1 470  ARG n 
1 471  ARG n 
1 472  GLN n 
1 473  HIS n 
1 474  GLU n 
1 475  GLN n 
1 476  LEU n 
1 477  ARG n 
1 478  ALA n 
1 479  VAL n 
1 480  ILE n 
1 481  VAL n 
1 482  ARG n 
1 483  VAL n 
1 484  LEU n 
1 485  ARG n 
1 486  PRO n 
1 487  GLN n 
1 488  VAL n 
1 489  THR n 
1 490  ALA n 
1 491  VAL n 
1 492  ALA n 
1 493  GLN n 
1 494  GLN n 
1 495  ASN n 
1 496  GLN n 
1 497  GLY n 
1 498  GLU n 
1 499  VAL n 
1 500  PRO n 
1 501  GLU n 
1 502  PRO n 
1 503  GLN n 
1 504  ASP n 
1 505  MET n 
1 506  LYS n 
1 507  VAL n 
1 508  ALA n 
1 509  GLU n 
1 510  VAL n 
1 511  LEU n 
1 512  PHE n 
1 513  ASP n 
1 514  ALA n 
1 515  ALA n 
1 516  ASP n 
1 517  ALA n 
1 518  ASN n 
1 519  ALA n 
1 520  ILE n 
1 521  GLU n 
1 522  GLU n 
1 523  VAL n 
1 524  ASN n 
1 525  LEU n 
1 526  ALA n 
1 527  TYR n 
1 528  GLU n 
1 529  ASN n 
1 530  VAL n 
1 531  LYS n 
1 532  GLU n 
1 533  VAL n 
1 534  ASP n 
1 535  GLY n 
1 536  LEU n 
1 537  ASP n 
1 538  VAL n 
1 539  SER n 
1 540  LYS n 
1 541  GLU n 
1 542  GLY n 
1 543  THR n 
1 544  GLU n 
1 545  ALA n 
1 546  TRP n 
1 547  GLU n 
1 548  ALA n 
1 549  ALA n 
1 550  MET n 
1 551  LYS n 
1 552  ARG n 
1 553  TYR n 
1 554  ASP n 
1 555  GLU n 
1 556  ARG n 
1 557  ILE n 
1 558  ASP n 
1 559  ARG n 
1 560  VAL n 
1 561  GLU n 
1 562  THR n 
1 563  ARG n 
1 564  ILE n 
1 565  THR n 
1 566  ALA n 
1 567  ARG n 
1 568  LEU n 
1 569  ARG n 
1 570  ASP n 
1 571  GLN n 
1 572  LEU n 
1 573  GLY n 
1 574  THR n 
1 575  ALA n 
1 576  LYS n 
1 577  ASN n 
1 578  ALA n 
1 579  ASN n 
1 580  GLU n 
1 581  MET n 
1 582  PHE n 
1 583  ARG n 
1 584  ILE n 
1 585  PHE n 
1 586  SER n 
1 587  ARG n 
1 588  PHE n 
1 589  ASN n 
1 590  ALA n 
1 591  LEU n 
1 592  PHE n 
1 593  VAL n 
1 594  ARG n 
1 595  PRO n 
1 596  HIS n 
1 597  ILE n 
1 598  ARG n 
1 599  GLY n 
1 600  ALA n 
1 601  ILE n 
1 602  ARG n 
1 603  GLU n 
1 604  TYR n 
1 605  GLN n 
1 606  THR n 
1 607  GLN n 
1 608  LEU n 
1 609  ILE n 
1 610  GLN n 
1 611  ARG n 
1 612  VAL n 
1 613  LYS n 
1 614  ASP n 
1 615  ASP n 
1 616  ILE n 
1 617  GLU n 
1 618  SER n 
1 619  LEU n 
1 620  HIS n 
1 621  ASP n 
1 622  LYS n 
1 623  PHE n 
1 624  LYS n 
1 625  VAL n 
1 626  GLN n 
1 627  TYR n 
1 628  PRO n 
1 629  GLN n 
1 630  SER n 
1 631  GLN n 
1 632  ALA n 
1 633  CYS n 
1 634  LYS n 
1 635  MET n 
1 636  SER n 
1 637  HIS n 
1 638  VAL n 
1 639  ARG n 
1 640  ASP n 
1 641  LEU n 
1 642  PRO n 
1 643  PRO n 
1 644  VAL n 
1 645  SER n 
1 646  GLY n 
1 647  SER n 
1 648  ILE n 
1 649  ILE n 
1 650  TRP n 
1 651  ALA n 
1 652  LYS n 
1 653  GLN n 
1 654  ILE n 
1 655  ASP n 
1 656  ARG n 
1 657  GLN n 
1 658  LEU n 
1 659  THR n 
1 660  ALA n 
1 661  TYR n 
1 662  MET n 
1 663  LYS n 
1 664  ARG n 
1 665  VAL n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LEU n 
1 670  GLY n 
1 671  LYS n 
1 672  GLY n 
1 673  TRP n 
1 674  GLU n 
1 675  ASN n 
1 676  HIS n 
1 677  VAL n 
1 678  GLU n 
1 679  GLY n 
1 680  GLN n 
1 681  LYS n 
1 682  LEU n 
1 683  LYS n 
1 684  GLN n 
1 685  ASP n 
1 686  GLY n 
1 687  ASP n 
1 688  SER n 
1 689  PHE n 
1 690  ARG n 
1 691  MET n 
1 692  LYS n 
1 693  LEU n 
1 694  ASN n 
1 695  THR n 
1 696  GLN n 
1 697  GLU n 
1 698  ILE n 
1 699  PHE n 
1 700  ASP n 
1 701  ASP n 
1 702  TRP n 
1 703  ALA n 
1 704  ARG n 
1 705  LYS n 
1 706  VAL n 
1 707  GLN n 
1 708  GLN n 
1 709  ARG n 
1 710  ASN n 
1 711  LEU n 
1 712  GLY n 
1 713  VAL n 
1 714  SER n 
1 715  GLY n 
1 716  ARG n 
1 717  ILE n 
1 718  PHE n 
1 719  THR n 
1 720  ILE n 
1 721  GLU n 
1 722  SER n 
1 723  THR n 
1 724  ARG n 
1 725  VAL n 
1 726  ARG n 
1 727  GLY n 
1 728  ARG n 
1 729  THR n 
1 730  GLY n 
1 731  ASN n 
1 732  VAL n 
1 733  LEU n 
1 734  LYS n 
1 735  LEU n 
1 736  LYS n 
1 737  VAL n 
1 738  ASN n 
1 739  PHE n 
1 740  LEU n 
1 741  PRO n 
1 742  GLU n 
1 743  ILE n 
1 744  ILE n 
1 745  THR n 
1 746  LEU n 
1 747  SER n 
1 748  LYS n 
1 749  GLU n 
1 750  VAL n 
1 751  ARG n 
1 752  ASN n 
1 753  LEU n 
1 754  LYS n 
1 755  TRP n 
1 756  LEU n 
1 757  GLY n 
1 758  PHE n 
1 759  ARG n 
1 760  VAL n 
1 761  PRO n 
1 762  LEU n 
1 763  ALA n 
1 764  ILE n 
1 765  VAL n 
1 766  ASN n 
1 767  LYS n 
1 768  ALA n 
1 769  HIS n 
1 770  GLN n 
1 771  ALA n 
1 772  ASN n 
1 773  GLN n 
1 774  LEU n 
1 775  TYR n 
1 776  PRO n 
1 777  PHE n 
1 778  ALA n 
1 779  ILE n 
1 780  SER n 
1 781  LEU n 
1 782  ILE n 
1 783  GLU n 
1 784  SER n 
1 785  VAL n 
1 786  ARG n 
1 787  THR n 
1 788  TYR n 
1 789  GLU n 
1 790  ARG n 
1 791  THR n 
1 792  CYS n 
1 793  GLU n 
1 794  LYS n 
1 795  VAL n 
1 796  GLU n 
1 797  GLU n 
1 798  ARG n 
1 799  ASN n 
1 800  THR n 
1 801  ILE n 
1 802  SER n 
1 803  LEU n 
1 804  LEU n 
1 805  VAL n 
1 806  ALA n 
1 807  GLY n 
1 808  LEU n 
1 809  LYS n 
1 810  LYS n 
1 811  GLU n 
1 812  VAL n 
1 813  GLN n 
1 814  ALA n 
1 815  LEU n 
1 816  ILE n 
1 817  ALA n 
1 818  GLU n 
1 819  GLY n 
1 820  ILE n 
1 821  ALA n 
1 822  LEU n 
1 823  VAL n 
1 824  TRP n 
1 825  GLU n 
1 826  SER n 
1 827  TYR n 
1 828  LYS n 
1 829  LEU n 
1 830  ASP n 
1 831  PRO n 
1 832  TYR n 
1 833  VAL n 
1 834  GLN n 
1 835  ARG n 
1 836  LEU n 
1 837  ALA n 
1 838  GLU n 
1 839  THR n 
1 840  VAL n 
1 841  PHE n 
1 842  ASN n 
1 843  PHE n 
1 844  GLN n 
1 845  GLU n 
1 846  LYS n 
1 847  VAL n 
1 848  ASP n 
1 849  ASP n 
1 850  LEU n 
1 851  LEU n 
1 852  ILE n 
1 853  ILE n 
1 854  GLU n 
1 855  GLU n 
1 856  LYS n 
1 857  ILE n 
1 858  ASP n 
1 859  LEU n 
1 860  GLU n 
1 861  VAL n 
1 862  ARG n 
1 863  SER n 
1 864  LEU n 
1 865  GLU n 
1 866  THR n 
1 867  CYS n 
1 868  MET n 
1 869  TYR n 
1 870  ASP n 
1 871  HIS n 
1 872  LYS n 
1 873  THR n 
1 874  PHE n 
1 875  SER n 
1 876  GLU n 
1 877  ILE n 
1 878  LEU n 
1 879  ASN n 
1 880  ARG n 
1 881  VAL n 
1 882  GLN n 
1 883  LYS n 
1 884  ALA n 
1 885  VAL n 
1 886  ASP n 
1 887  ASP n 
1 888  LEU n 
1 889  ASN n 
1 890  LEU n 
1 891  HIS n 
1 892  SER n 
1 893  TYR n 
1 894  SER n 
1 895  ASN n 
1 896  LEU n 
1 897  PRO n 
1 898  ILE n 
1 899  TRP n 
1 900  VAL n 
1 901  ASN n 
1 902  LYS n 
1 903  LEU n 
1 904  ASP n 
1 905  MET n 
1 906  GLU n 
1 907  ILE n 
1 908  GLU n 
1 909  ARG n 
1 910  ILE n 
1 911  LEU n 
1 912  GLY n 
1 913  VAL n 
1 914  ARG n 
1 915  LEU n 
1 916  GLN n 
1 917  ALA n 
1 918  GLY n 
1 919  LEU n 
1 920  ARG n 
1 921  ALA n 
1 922  TRP n 
1 923  THR n 
1 924  GLN n 
1 925  VAL n 
1 926  LEU n 
1 927  LEU n 
1 928  GLY n 
1 929  GLN n 
1 930  ALA n 
1 931  GLU n 
1 932  ASP n 
1 933  LYS n 
1 934  ALA n 
1 935  GLU n 
1 936  VAL n 
1 937  ASP n 
1 938  MET n 
1 939  ASP n 
1 940  THR n 
1 941  ASP n 
1 942  ALA n 
1 943  PRO n 
1 944  GLN n 
1 945  VAL n 
1 946  SER n 
1 947  HIS n 
1 948  LYS n 
1 949  PRO n 
1 950  GLY n 
1 951  GLY n 
1 952  GLU n 
1 953  PRO n 
1 954  LYS n 
1 955  ILE n 
1 956  LYS n 
1 957  ASN n 
1 958  VAL n 
1 959  VAL n 
1 960  HIS n 
1 961  GLU n 
1 962  LEU n 
1 963  ARG n 
1 964  ILE n 
1 965  THR n 
1 966  ASN n 
1 967  GLN n 
1 968  VAL n 
1 969  ILE n 
1 970  TYR n 
1 971  LEU n 
1 972  ASN n 
1 973  PRO n 
1 974  PRO n 
1 975  ILE n 
1 976  GLU n 
1 977  GLU n 
1 978  CYS n 
1 979  ARG n 
1 980  TYR n 
1 981  LYS n 
1 982  LEU n 
1 983  TYR n 
1 984  GLN n 
1 985  GLU n 
1 986  MET n 
1 987  PHE n 
1 988  ALA n 
1 989  TRP n 
1 990  LYS n 
1 991  MET n 
1 992  VAL n 
1 993  VAL n 
1 994  LEU n 
1 995  SER n 
1 996  LEU n 
1 997  PRO n 
1 998  ARG n 
1 999  ILE n 
1 1000 GLN n 
1 1001 SER n 
1 1002 GLN n 
1 1003 ARG n 
1 1004 TYR n 
1 1005 GLN n 
1 1006 VAL n 
1 1007 GLY n 
1 1008 VAL n 
1 1009 HIS n 
1 1010 TYR n 
1 1011 GLU n 
1 1012 LEU n 
1 1013 THR n 
1 1014 GLU n 
1 1015 GLU n 
1 1016 GLU n 
1 1017 LYS n 
1 1018 PHE n 
1 1019 TYR n 
1 1020 ARG n 
1 1021 ASN n 
1 1022 ALA n 
1 1023 LEU n 
1 1024 THR n 
1 1025 ARG n 
1 1026 MET n 
1 1027 PRO n 
1 1028 ASP n 
1 1029 GLY n 
1 1030 PRO n 
1 1031 VAL n 
1 1032 ALA n 
1 1033 LEU n 
1 1034 GLU n 
1 1035 GLU n 
1 1036 SER n 
1 1037 TYR n 
1 1038 SER n 
1 1039 ALA n 
1 1040 VAL n 
1 1041 MET n 
1 1042 GLY n 
1 1043 ILE n 
1 1044 VAL n 
1 1045 SER n 
1 1046 GLU n 
1 1047 VAL n 
1 1048 GLU n 
1 1049 GLN n 
1 1050 TYR n 
1 1051 VAL n 
1 1052 LYS n 
1 1053 VAL n 
1 1054 TRP n 
1 1055 LEU n 
1 1056 GLN n 
1 1057 TYR n 
1 1058 GLN n 
1 1059 CYS n 
1 1060 LEU n 
1 1061 TRP n 
1 1062 ASP n 
1 1063 MET n 
1 1064 GLN n 
1 1065 ALA n 
1 1066 GLU n 
1 1067 ASN n 
1 1068 ILE n 
1 1069 TYR n 
1 1070 ASN n 
1 1071 ARG n 
1 1072 LEU n 
1 1073 GLY n 
1 1074 GLU n 
1 1075 ASP n 
1 1076 LEU n 
1 1077 ASN n 
1 1078 LYS n 
1 1079 TRP n 
1 1080 GLN n 
1 1081 ALA n 
1 1082 LEU n 
1 1083 LEU n 
1 1084 VAL n 
1 1085 GLN n 
1 1086 ILE n 
1 1087 ARG n 
1 1088 LYS n 
1 1089 ALA n 
1 1090 ARG n 
1 1091 GLY n 
1 1092 THR n 
1 1093 PHE n 
1 1094 ASP n 
1 1095 ASN n 
1 1096 ALA n 
1 1097 GLU n 
1 1098 THR n 
1 1099 LYS n 
1 1100 LYS n 
1 1101 GLU n 
1 1102 PHE n 
1 1103 GLY n 
1 1104 PRO n 
1 1105 VAL n 
1 1106 VAL n 
1 1107 ILE n 
1 1108 ASP n 
1 1109 TYR n 
1 1110 GLY n 
1 1111 LYS n 
1 1112 VAL n 
1 1113 GLN n 
1 1114 SER n 
1 1115 LYS n 
1 1116 VAL n 
1 1117 ASN n 
1 1118 LEU n 
1 1119 LYS n 
1 1120 TYR n 
1 1121 ASP n 
1 1122 SER n 
1 1123 TRP n 
1 1124 HIS n 
1 1125 LYS n 
1 1126 GLU n 
1 1127 VAL n 
1 1128 LEU n 
1 1129 SER n 
1 1130 LYS n 
1 1131 PHE n 
1 1132 GLY n 
1 1133 GLN n 
1 1134 MET n 
1 1135 LEU n 
1 1136 GLY n 
1 1137 SER n 
1 1138 ASN n 
1 1139 MET n 
1 1140 THR n 
1 1141 GLU n 
1 1142 PHE n 
1 1143 HIS n 
1 1144 SER n 
1 1145 GLN n 
1 1146 ILE n 
1 1147 SER n 
1 1148 LYS n 
1 1149 SER n 
1 1150 ARG n 
1 1151 GLN n 
1 1152 GLU n 
1 1153 LEU n 
1 1154 GLU n 
1 1155 GLN n 
1 1156 HIS n 
1 1157 SER n 
1 1158 VAL n 
1 1159 ASP n 
1 1160 THR n 
1 1161 ALA n 
1 1162 SER n 
1 1163 THR n 
1 1164 SER n 
1 1165 ASP n 
1 1166 ALA n 
1 1167 VAL n 
1 1168 THR n 
1 1169 PHE n 
1 1170 ILE n 
1 1171 THR n 
1 1172 TYR n 
1 1173 VAL n 
1 1174 GLN n 
1 1175 SER n 
1 1176 LEU n 
1 1177 LYS n 
1 1178 ARG n 
1 1179 LYS n 
1 1180 ILE n 
1 1181 LYS n 
1 1182 GLN n 
1 1183 PHE n 
1 1184 GLU n 
1 1185 LYS n 
1 1186 GLN n 
1 1187 VAL n 
1 1188 GLU n 
1 1189 LEU n 
1 1190 TYR n 
1 1191 ARG n 
1 1192 ASN n 
1 1193 GLY n 
1 1194 GLN n 
1 1195 ARG n 
1 1196 LEU n 
1 1197 LEU n 
1 1198 GLU n 
1 1199 LYS n 
1 1200 GLN n 
1 1201 ARG n 
1 1202 PHE n 
1 1203 GLN n 
1 1204 PHE n 
1 1205 PRO n 
1 1206 PRO n 
1 1207 SER n 
1 1208 TRP n 
1 1209 LEU n 
1 1210 TYR n 
1 1211 ILE n 
1 1212 ASP n 
1 1213 ASN n 
1 1214 ILE n 
1 1215 GLU n 
1 1216 GLY n 
1 1217 GLU n 
1 1218 TRP n 
1 1219 GLY n 
1 1220 ALA n 
1 1221 PHE n 
1 1222 ASN n 
1 1223 ASP n 
1 1224 ILE n 
1 1225 MET n 
1 1226 ARG n 
1 1227 ARG n 
1 1228 LYS n 
1 1229 ASP n 
1 1230 SER n 
1 1231 ALA n 
1 1232 ILE n 
1 1233 GLN n 
1 1234 GLN n 
1 1235 GLN n 
1 1236 VAL n 
1 1237 ALA n 
1 1238 ASN n 
1 1239 LEU n 
1 1240 GLN n 
1 1241 MET n 
1 1242 LYS n 
1 1243 ILE n 
1 1244 VAL n 
1 1245 GLN n 
1 1246 GLU n 
1 1247 ASP n 
1 1248 ARG n 
1 1249 ALA n 
1 1250 VAL n 
1 1251 GLU n 
1 1252 SER n 
1 1253 ARG n 
1 1254 THR n 
1 1255 THR n 
1 1256 ASP n 
1 1257 LEU n 
1 1258 LEU n 
1 1259 THR n 
1 1260 ASP n 
1 1261 TRP n 
1 1262 GLU n 
1 1263 LYS n 
1 1264 THR n 
1 1265 LYS n 
1 1266 PRO n 
1 1267 VAL n 
1 1268 THR n 
1 1269 GLY n 
1 1270 ASN n 
1 1271 LEU n 
1 1272 ARG n 
1 1273 PRO n 
1 1274 GLU n 
1 1275 GLU n 
1 1276 ALA n 
1 1277 LEU n 
1 1278 GLN n 
1 1279 ALA n 
1 1280 LEU n 
1 1281 THR n 
1 1282 ILE n 
1 1283 TYR n 
1 1284 GLU n 
1 1285 GLY n 
1 1286 LYS n 
1 1287 PHE n 
1 1288 GLY n 
1 1289 ARG n 
1 1290 LEU n 
1 1291 LYS n 
1 1292 ASP n 
1 1293 ASP n 
1 1294 ARG n 
1 1295 GLU n 
1 1296 LYS n 
1 1297 CYS n 
1 1298 ALA n 
1 1299 LYS n 
1 1300 ALA n 
1 1301 LYS n 
1 1302 GLU n 
1 1303 ALA n 
1 1304 LEU n 
1 1305 GLU n 
1 1306 LEU n 
1 1307 THR n 
1 1308 ASP n 
1 1309 THR n 
1 1310 GLY n 
1 1311 LEU n 
1 1312 LEU n 
1 1313 SER n 
1 1314 GLY n 
1 1315 SER n 
1 1316 GLU n 
1 1317 GLU n 
1 1318 ARG n 
1 1319 VAL n 
1 1320 GLN n 
1 1321 VAL n 
1 1322 ALA n 
1 1323 LEU n 
1 1324 GLU n 
1 1325 GLU n 
1 1326 LEU n 
1 1327 GLN n 
1 1328 ASP n 
1 1329 LEU n 
1 1330 LYS n 
1 1331 GLY n 
1 1332 VAL n 
1 1333 TRP n 
1 1334 SER n 
1 1335 GLU n 
1 1336 LEU n 
1 1337 SER n 
1 1338 LYS n 
1 1339 VAL n 
1 1340 TRP n 
1 1341 GLU n 
1 1342 GLN n 
1 1343 ILE n 
1 1344 ASP n 
1 1345 GLN n 
1 1346 MET n 
1 1347 LYS n 
1 1348 GLU n 
1 1349 GLN n 
1 1350 PRO n 
1 1351 TRP n 
1 1352 VAL n 
1 1353 SER n 
1 1354 VAL n 
1 1355 GLN n 
1 1356 PRO n 
1 1357 ARG n 
1 1358 LYS n 
1 1359 LEU n 
1 1360 ARG n 
1 1361 GLN n 
1 1362 ASN n 
1 1363 LEU n 
1 1364 ASP n 
1 1365 ALA n 
1 1366 LEU n 
1 1367 LEU n 
1 1368 ASN n 
1 1369 GLN n 
1 1370 LEU n 
1 1371 LYS n 
1 1372 SER n 
1 1373 PHE n 
1 1374 PRO n 
1 1375 ALA n 
1 1376 ARG n 
1 1377 LEU n 
1 1378 ARG n 
1 1379 GLN n 
1 1380 TYR n 
1 1381 ALA n 
1 1382 SER n 
1 1383 TYR n 
1 1384 GLU n 
1 1385 PHE n 
1 1386 VAL n 
1 1387 GLN n 
1 1388 ARG n 
1 1389 LEU n 
1 1390 LEU n 
1 1391 LYS n 
1 1392 GLY n 
1 1393 TYR n 
1 1394 MET n 
1 1395 LYS n 
1 1396 ILE n 
1 1397 ASN n 
1 1398 MET n 
1 1399 LEU n 
1 1400 VAL n 
1 1401 ILE n 
1 1402 GLU n 
1 1403 LEU n 
1 1404 LYS n 
1 1405 SER n 
1 1406 GLU n 
1 1407 ALA n 
1 1408 LEU n 
1 1409 LYS n 
1 1410 ASP n 
1 1411 ARG n 
1 1412 HIS n 
1 1413 TRP n 
1 1414 LYS n 
1 1415 GLN n 
1 1416 LEU n 
1 1417 MET n 
1 1418 LYS n 
1 1419 ARG n 
1 1420 LEU n 
1 1421 HIS n 
1 1422 VAL n 
1 1423 ASN n 
1 1424 TRP n 
1 1425 VAL n 
1 1426 VAL n 
1 1427 SER n 
1 1428 GLU n 
1 1429 LEU n 
1 1430 THR n 
1 1431 LEU n 
1 1432 GLY n 
1 1433 GLN n 
1 1434 ILE n 
1 1435 TRP n 
1 1436 ASP n 
1 1437 VAL n 
1 1438 ASP n 
1 1439 LEU n 
1 1440 GLN n 
1 1441 LYS n 
1 1442 ASN n 
1 1443 GLU n 
1 1444 ALA n 
1 1445 ILE n 
1 1446 VAL n 
1 1447 LYS n 
1 1448 ASP n 
1 1449 VAL n 
1 1450 LEU n 
1 1451 LEU n 
1 1452 VAL n 
1 1453 ALA n 
1 1454 GLN n 
1 1455 GLY n 
1 1456 GLU n 
1 1457 MET n 
1 1458 ALA n 
1 1459 LEU n 
1 1460 GLU n 
1 1461 GLU n 
1 1462 PHE n 
1 1463 LEU n 
1 1464 LYS n 
1 1465 GLN n 
1 1466 ILE n 
1 1467 ARG n 
1 1468 GLU n 
1 1469 VAL n 
1 1470 TRP n 
1 1471 ASN n 
1 1472 THR n 
1 1473 TYR n 
1 1474 GLU n 
1 1475 LEU n 
1 1476 ASP n 
1 1477 LEU n 
1 1478 VAL n 
1 1479 ASN n 
1 1480 TYR n 
1 1481 GLN n 
1 1482 ASN n 
1 1483 LYS n 
1 1484 CYS n 
1 1485 ARG n 
1 1486 LEU n 
1 1487 ILE n 
1 1488 ARG n 
1 1489 GLY n 
1 1490 TRP n 
1 1491 ASP n 
1 1492 ASP n 
1 1493 LEU n 
1 1494 PHE n 
1 1495 ASN n 
1 1496 LYS n 
1 1497 VAL n 
1 1498 LYS n 
1 1499 GLU n 
1 1500 HIS n 
1 1501 ILE n 
1 1502 ASN n 
1 1503 SER n 
1 1504 VAL n 
1 1505 SER n 
1 1506 ALA n 
1 1507 MET n 
1 1508 LYS n 
1 1509 LEU n 
1 1510 SER n 
1 1511 PRO n 
1 1512 TYR n 
1 1513 TYR n 
1 1514 LYS n 
1 1515 VAL n 
1 1516 PHE n 
1 1517 GLU n 
1 1518 GLU n 
1 1519 ASP n 
1 1520 ALA n 
1 1521 LEU n 
1 1522 SER n 
1 1523 TRP n 
1 1524 GLU n 
1 1525 ASP n 
1 1526 LYS n 
1 1527 LEU n 
1 1528 ASN n 
1 1529 ARG n 
1 1530 ILE n 
1 1531 MET n 
1 1532 ALA n 
1 1533 LEU n 
1 1534 PHE n 
1 1535 ASP n 
1 1536 VAL n 
1 1537 TRP n 
1 1538 ILE n 
1 1539 ASP n 
1 1540 VAL n 
1 1541 GLN n 
1 1542 ARG n 
1 1543 ARG n 
1 1544 TRP n 
1 1545 VAL n 
1 1546 TYR n 
1 1547 LEU n 
1 1548 GLU n 
1 1549 GLY n 
1 1550 ILE n 
1 1551 PHE n 
1 1552 THR n 
1 1553 GLY n 
1 1554 SER n 
1 1555 ALA n 
1 1556 ASP n 
1 1557 ILE n 
1 1558 LYS n 
1 1559 HIS n 
1 1560 LEU n 
1 1561 LEU n 
1 1562 PRO n 
1 1563 VAL n 
1 1564 GLU n 
1 1565 THR n 
1 1566 GLN n 
1 1567 ARG n 
1 1568 PHE n 
1 1569 GLN n 
1 1570 SER n 
1 1571 ILE n 
1 1572 SER n 
1 1573 THR n 
1 1574 GLU n 
1 1575 PHE n 
1 1576 LEU n 
1 1577 ALA n 
1 1578 LEU n 
1 1579 MET n 
1 1580 LYS n 
1 1581 LYS n 
1 1582 VAL n 
1 1583 SER n 
1 1584 LYS n 
1 1585 SER n 
1 1586 PRO n 
1 1587 LEU n 
1 1588 VAL n 
1 1589 MET n 
1 1590 ASP n 
1 1591 VAL n 
1 1592 LEU n 
1 1593 ASN n 
1 1594 ILE n 
1 1595 GLN n 
1 1596 GLY n 
1 1597 VAL n 
1 1598 GLN n 
1 1599 ARG n 
1 1600 SER n 
1 1601 LEU n 
1 1602 GLU n 
1 1603 ARG n 
1 1604 LEU n 
1 1605 ALA n 
1 1606 ASP n 
1 1607 LEU n 
1 1608 LEU n 
1 1609 GLY n 
1 1610 LYS n 
1 1611 ILE n 
1 1612 GLN n 
1 1613 LYS n 
1 1614 ALA n 
1 1615 LEU n 
1 1616 GLY n 
1 1617 GLU n 
1 1618 TYR n 
1 1619 LEU n 
1 1620 GLU n 
1 1621 ARG n 
1 1622 GLU n 
1 1623 ARG n 
1 1624 SER n 
1 1625 SER n 
1 1626 PHE n 
1 1627 PRO n 
1 1628 ARG n 
1 1629 PHE n 
1 1630 TYR n 
1 1631 PHE n 
1 1632 VAL n 
1 1633 GLY n 
1 1634 ASP n 
1 1635 GLU n 
1 1636 ASP n 
1 1637 LEU n 
1 1638 LEU n 
1 1639 GLU n 
1 1640 ILE n 
1 1641 ILE n 
1 1642 GLY n 
1 1643 ASN n 
1 1644 SER n 
1 1645 LYS n 
1 1646 ASN n 
1 1647 VAL n 
1 1648 ALA n 
1 1649 LYS n 
1 1650 LEU n 
1 1651 GLN n 
1 1652 LYS n 
1 1653 HIS n 
1 1654 PHE n 
1 1655 LYS n 
1 1656 LYS n 
1 1657 MET n 
1 1658 PHE n 
1 1659 ALA n 
1 1660 GLY n 
1 1661 VAL n 
1 1662 SER n 
1 1663 SER n 
1 1664 ILE n 
1 1665 ILE n 
1 1666 LEU n 
1 1667 ASN n 
1 1668 GLU n 
1 1669 ASP n 
1 1670 ASN n 
1 1671 SER n 
1 1672 VAL n 
1 1673 VAL n 
1 1674 LEU n 
1 1675 GLY n 
1 1676 ILE n 
1 1677 SER n 
1 1678 SER n 
1 1679 ARG n 
1 1680 GLU n 
1 1681 GLY n 
1 1682 GLU n 
1 1683 GLU n 
1 1684 VAL n 
1 1685 MET n 
1 1686 PHE n 
1 1687 LYS n 
1 1688 THR n 
1 1689 PRO n 
1 1690 VAL n 
1 1691 SER n 
1 1692 ILE n 
1 1693 THR n 
1 1694 GLU n 
1 1695 HIS n 
1 1696 PRO n 
1 1697 LYS n 
1 1698 ILE n 
1 1699 ASN n 
1 1700 GLU n 
1 1701 TRP n 
1 1702 LEU n 
1 1703 THR n 
1 1704 LEU n 
1 1705 VAL n 
1 1706 GLU n 
1 1707 LYS n 
1 1708 GLU n 
1 1709 MET n 
1 1710 ARG n 
1 1711 VAL n 
1 1712 THR n 
1 1713 LEU n 
1 1714 ALA n 
1 1715 LYS n 
1 1716 LEU n 
1 1717 LEU n 
1 1718 ALA n 
1 1719 GLU n 
1 1720 SER n 
1 1721 VAL n 
1 1722 THR n 
1 1723 GLU n 
1 1724 VAL n 
1 1725 GLU n 
1 1726 ILE n 
1 1727 PHE n 
1 1728 GLY n 
1 1729 LYS n 
1 1730 ALA n 
1 1731 THR n 
1 1732 SER n 
1 1733 ILE n 
1 1734 ASP n 
1 1735 PRO n 
1 1736 ASN n 
1 1737 THR n 
1 1738 TYR n 
1 1739 ILE n 
1 1740 THR n 
1 1741 TRP n 
1 1742 ILE n 
1 1743 ASP n 
1 1744 LYS n 
1 1745 TYR n 
1 1746 GLN n 
1 1747 ALA n 
1 1748 GLN n 
1 1749 LEU n 
1 1750 VAL n 
1 1751 VAL n 
1 1752 LEU n 
1 1753 SER n 
1 1754 ALA n 
1 1755 GLN n 
1 1756 ILE n 
1 1757 ALA n 
1 1758 TRP n 
1 1759 SER n 
1 1760 GLU n 
1 1761 ASN n 
1 1762 VAL n 
1 1763 GLU n 
1 1764 THR n 
1 1765 ALA n 
1 1766 LEU n 
1 1767 SER n 
1 1768 SER n 
1 1769 MET n 
1 1770 GLY n 
1 1771 GLY n 
1 1772 GLY n 
1 1773 GLY n 
1 1774 ASP n 
1 1775 ALA n 
1 1776 ALA n 
1 1777 PRO n 
1 1778 LEU n 
1 1779 HIS n 
1 1780 SER n 
1 1781 VAL n 
1 1782 LEU n 
1 1783 SER n 
1 1784 ASN n 
1 1785 VAL n 
1 1786 GLU n 
1 1787 VAL n 
1 1788 THR n 
1 1789 LEU n 
1 1790 ASN n 
1 1791 VAL n 
1 1792 LEU n 
1 1793 ALA n 
1 1794 ASP n 
1 1795 SER n 
1 1796 VAL n 
1 1797 LEU n 
1 1798 MET n 
1 1799 GLU n 
1 1800 GLN n 
1 1801 PRO n 
1 1802 PRO n 
1 1803 LEU n 
1 1804 ARG n 
1 1805 ARG n 
1 1806 ARG n 
1 1807 LYS n 
1 1808 LEU n 
1 1809 GLU n 
1 1810 HIS n 
1 1811 LEU n 
1 1812 ILE n 
1 1813 THR n 
1 1814 GLU n 
1 1815 LEU n 
1 1816 VAL n 
1 1817 HIS n 
1 1818 GLN n 
1 1819 ARG n 
1 1820 ASP n 
1 1821 VAL n 
1 1822 THR n 
1 1823 ARG n 
1 1824 SER n 
1 1825 LEU n 
1 1826 ILE n 
1 1827 LYS n 
1 1828 SER n 
1 1829 LYS n 
1 1830 ILE n 
1 1831 ASP n 
1 1832 ASN n 
1 1833 ALA n 
1 1834 LYS n 
1 1835 SER n 
1 1836 PHE n 
1 1837 GLU n 
1 1838 TRP n 
1 1839 LEU n 
1 1840 SER n 
1 1841 GLN n 
1 1842 MET n 
1 1843 ARG n 
1 1844 PHE n 
1 1845 TYR n 
1 1846 PHE n 
1 1847 ASP n 
1 1848 PRO n 
1 1849 LYS n 
1 1850 GLN n 
1 1851 THR n 
1 1852 ASP n 
1 1853 VAL n 
1 1854 LEU n 
1 1855 GLN n 
1 1856 GLN n 
1 1857 LEU n 
1 1858 SER n 
1 1859 ILE n 
1 1860 GLN n 
1 1861 MET n 
1 1862 ALA n 
1 1863 ASN n 
1 1864 ALA n 
1 1865 LYS n 
1 1866 PHE n 
1 1867 ASN n 
1 1868 TYR n 
1 1869 GLY n 
1 1870 PHE n 
1 1871 GLU n 
1 1872 TYR n 
1 1873 LEU n 
1 1874 GLY n 
1 1875 VAL n 
1 1876 GLN n 
1 1877 ASP n 
1 1878 LYS n 
1 1879 LEU n 
1 1880 VAL n 
1 1881 GLN n 
1 1882 THR n 
1 1883 PRO n 
1 1884 LEU n 
1 1885 THR n 
1 1886 ASP n 
1 1887 ARG n 
1 1888 CYS n 
1 1889 TYR n 
1 1890 LEU n 
1 1891 THR n 
1 1892 MET n 
1 1893 THR n 
1 1894 GLN n 
1 1895 ALA n 
1 1896 LEU n 
1 1897 GLU n 
1 1898 ALA n 
1 1899 ARG n 
1 1900 LEU n 
1 1901 GLY n 
1 1902 GLY n 
1 1903 SER n 
1 1904 PRO n 
1 1905 PHE n 
1 1906 GLY n 
1 1907 PRO n 
1 1908 ALA n 
1 1909 GLY n 
1 1910 THR n 
1 1911 GLY n 
1 1912 LYS n 
1 1913 THR n 
1 1914 GLU n 
1 1915 SER n 
1 1916 VAL n 
1 1917 LYS n 
1 1918 ALA n 
1 1919 LEU n 
1 1920 GLY n 
1 1921 HIS n 
1 1922 GLN n 
1 1923 LEU n 
1 1924 GLY n 
1 1925 ARG n 
1 1926 PHE n 
1 1927 VAL n 
1 1928 LEU n 
1 1929 VAL n 
1 1930 PHE n 
1 1931 ASN n 
1 1932 CYS n 
1 1933 ASP n 
1 1934 GLU n 
1 1935 THR n 
1 1936 PHE n 
1 1937 ASP n 
1 1938 PHE n 
1 1939 GLN n 
1 1940 ALA n 
1 1941 MET n 
1 1942 GLY n 
1 1943 ARG n 
1 1944 ILE n 
1 1945 PHE n 
1 1946 VAL n 
1 1947 GLY n 
1 1948 LEU n 
1 1949 CYS n 
1 1950 GLN n 
1 1951 VAL n 
1 1952 GLY n 
1 1953 ALA n 
1 1954 TRP n 
1 1955 GLY n 
1 1956 CYS n 
1 1957 PHE n 
1 1958 ASP n 
1 1959 GLU n 
1 1960 PHE n 
1 1961 ASN n 
1 1962 ARG n 
1 1963 LEU n 
1 1964 GLU n 
1 1965 GLU n 
1 1966 ARG n 
1 1967 MET n 
1 1968 LEU n 
1 1969 SER n 
1 1970 ALA n 
1 1971 VAL n 
1 1972 SER n 
1 1973 GLN n 
1 1974 GLN n 
1 1975 VAL n 
1 1976 GLN n 
1 1977 CYS n 
1 1978 ILE n 
1 1979 GLN n 
1 1980 GLU n 
1 1981 ALA n 
1 1982 LEU n 
1 1983 ARG n 
1 1984 GLU n 
1 1985 HIS n 
1 1986 SER n 
1 1987 ASN n 
1 1988 PRO n 
1 1989 ASN n 
1 1990 TYR n 
1 1991 ASP n 
1 1992 LYS n 
1 1993 THR n 
1 1994 SER n 
1 1995 ALA n 
1 1996 PRO n 
1 1997 ILE n 
1 1998 THR n 
1 1999 CYS n 
1 2000 GLU n 
1 2001 LEU n 
1 2002 LEU n 
1 2003 ASN n 
1 2004 LYS n 
1 2005 GLN n 
1 2006 VAL n 
1 2007 LYS n 
1 2008 VAL n 
1 2009 SER n 
1 2010 PRO n 
1 2011 ASP n 
1 2012 MET n 
1 2013 ALA n 
1 2014 ILE n 
1 2015 PHE n 
1 2016 ILE n 
1 2017 THR n 
1 2018 MET n 
1 2019 ASN n 
1 2020 PRO n 
1 2021 GLY n 
1 2022 TYR n 
1 2023 ALA n 
1 2024 GLY n 
1 2025 ARG n 
1 2026 SER n 
1 2027 ASN n 
1 2028 LEU n 
1 2029 PRO n 
1 2030 ASP n 
1 2031 ASN n 
1 2032 LEU n 
1 2033 LYS n 
1 2034 LYS n 
1 2035 LEU n 
1 2036 PHE n 
1 2037 ARG n 
1 2038 SER n 
1 2039 LEU n 
1 2040 ALA n 
1 2041 MET n 
1 2042 THR n 
1 2043 LYS n 
1 2044 PRO n 
1 2045 ASP n 
1 2046 ARG n 
1 2047 GLN n 
1 2048 LEU n 
1 2049 ILE n 
1 2050 ALA n 
1 2051 GLN n 
1 2052 VAL n 
1 2053 MET n 
1 2054 LEU n 
1 2055 TYR n 
1 2056 SER n 
1 2057 GLN n 
1 2058 GLY n 
1 2059 PHE n 
1 2060 ARG n 
1 2061 THR n 
1 2062 ALA n 
1 2063 GLU n 
1 2064 VAL n 
1 2065 LEU n 
1 2066 ALA n 
1 2067 ASN n 
1 2068 LYS n 
1 2069 ILE n 
1 2070 VAL n 
1 2071 PRO n 
1 2072 PHE n 
1 2073 PHE n 
1 2074 LYS n 
1 2075 LEU n 
1 2076 CYS n 
1 2077 ASP n 
1 2078 GLU n 
1 2079 GLN n 
1 2080 LEU n 
1 2081 SER n 
1 2082 SER n 
1 2083 GLN n 
1 2084 SER n 
1 2085 HIS n 
1 2086 TYR n 
1 2087 ASP n 
1 2088 PHE n 
1 2089 GLY n 
1 2090 LEU n 
1 2091 ARG n 
1 2092 ALA n 
1 2093 LEU n 
1 2094 LYS n 
1 2095 SER n 
1 2096 VAL n 
1 2097 LEU n 
1 2098 VAL n 
1 2099 SER n 
1 2100 ALA n 
1 2101 GLY n 
1 2102 ASN n 
1 2103 VAL n 
1 2104 LYS n 
1 2105 ARG n 
1 2106 GLU n 
1 2107 ARG n 
1 2108 ILE n 
1 2109 GLN n 
1 2110 LYS n 
1 2111 ILE n 
1 2112 LYS n 
1 2113 ARG n 
1 2114 GLU n 
1 2115 LYS n 
1 2116 GLU n 
1 2117 GLU n 
1 2118 ARG n 
1 2119 GLY n 
1 2120 GLU n 
1 2121 ALA n 
1 2122 VAL n 
1 2123 ASP n 
1 2124 GLU n 
1 2125 GLY n 
1 2126 GLU n 
1 2127 ILE n 
1 2128 ALA n 
1 2129 GLU n 
1 2130 ASN n 
1 2131 LEU n 
1 2132 PRO n 
1 2133 GLU n 
1 2134 GLN n 
1 2135 GLU n 
1 2136 ILE n 
1 2137 LEU n 
1 2138 ILE n 
1 2139 GLN n 
1 2140 SER n 
1 2141 VAL n 
1 2142 CYS n 
1 2143 GLU n 
1 2144 THR n 
1 2145 MET n 
1 2146 VAL n 
1 2147 PRO n 
1 2148 LYS n 
1 2149 LEU n 
1 2150 VAL n 
1 2151 ALA n 
1 2152 GLU n 
1 2153 ASP n 
1 2154 ILE n 
1 2155 PRO n 
1 2156 LEU n 
1 2157 LEU n 
1 2158 PHE n 
1 2159 SER n 
1 2160 LEU n 
1 2161 LEU n 
1 2162 SER n 
1 2163 ASP n 
1 2164 VAL n 
1 2165 PHE n 
1 2166 PRO n 
1 2167 GLY n 
1 2168 VAL n 
1 2169 GLN n 
1 2170 TYR n 
1 2171 HIS n 
1 2172 ARG n 
1 2173 GLY n 
1 2174 GLU n 
1 2175 MET n 
1 2176 THR n 
1 2177 ALA n 
1 2178 LEU n 
1 2179 ARG n 
1 2180 GLU n 
1 2181 GLU n 
1 2182 LEU n 
1 2183 LYS n 
1 2184 LYS n 
1 2185 VAL n 
1 2186 CYS n 
1 2187 GLN n 
1 2188 GLU n 
1 2189 MET n 
1 2190 TYR n 
1 2191 LEU n 
1 2192 THR n 
1 2193 TYR n 
1 2194 GLY n 
1 2195 ASP n 
1 2196 GLY n 
1 2197 GLU n 
1 2198 GLU n 
1 2199 VAL n 
1 2200 GLY n 
1 2201 GLY n 
1 2202 MET n 
1 2203 TRP n 
1 2204 VAL n 
1 2205 GLU n 
1 2206 LYS n 
1 2207 VAL n 
1 2208 LEU n 
1 2209 GLN n 
1 2210 LEU n 
1 2211 TYR n 
1 2212 GLN n 
1 2213 ILE n 
1 2214 THR n 
1 2215 GLN n 
1 2216 ILE n 
1 2217 ASN n 
1 2218 HIS n 
1 2219 GLY n 
1 2220 LEU n 
1 2221 MET n 
1 2222 MET n 
1 2223 VAL n 
1 2224 GLY n 
1 2225 PRO n 
1 2226 SER n 
1 2227 GLY n 
1 2228 SER n 
1 2229 GLY n 
1 2230 LYS n 
1 2231 SER n 
1 2232 MET n 
1 2233 ALA n 
1 2234 TRP n 
1 2235 ARG n 
1 2236 VAL n 
1 2237 LEU n 
1 2238 LEU n 
1 2239 LYS n 
1 2240 ALA n 
1 2241 LEU n 
1 2242 GLU n 
1 2243 ARG n 
1 2244 LEU n 
1 2245 GLU n 
1 2246 GLY n 
1 2247 VAL n 
1 2248 GLU n 
1 2249 GLY n 
1 2250 VAL n 
1 2251 ALA n 
1 2252 HIS n 
1 2253 ILE n 
1 2254 ILE n 
1 2255 ASP n 
1 2256 PRO n 
1 2257 LYS n 
1 2258 ALA n 
1 2259 ILE n 
1 2260 SER n 
1 2261 LYS n 
1 2262 ASP n 
1 2263 HIS n 
1 2264 LEU n 
1 2265 TYR n 
1 2266 GLY n 
1 2267 THR n 
1 2268 LEU n 
1 2269 ASP n 
1 2270 PRO n 
1 2271 ASN n 
1 2272 THR n 
1 2273 ARG n 
1 2274 GLU n 
1 2275 TRP n 
1 2276 THR n 
1 2277 ASP n 
1 2278 GLY n 
1 2279 LEU n 
1 2280 PHE n 
1 2281 THR n 
1 2282 HIS n 
1 2283 VAL n 
1 2284 LEU n 
1 2285 ARG n 
1 2286 LYS n 
1 2287 ILE n 
1 2288 ILE n 
1 2289 ASP n 
1 2290 SER n 
1 2291 VAL n 
1 2292 ARG n 
1 2293 GLY n 
1 2294 GLU n 
1 2295 LEU n 
1 2296 GLN n 
1 2297 LYS n 
1 2298 ARG n 
1 2299 GLN n 
1 2300 TRP n 
1 2301 ILE n 
1 2302 VAL n 
1 2303 PHE n 
1 2304 ASP n 
1 2305 GLY n 
1 2306 ASP n 
1 2307 VAL n 
1 2308 ASP n 
1 2309 PRO n 
1 2310 GLU n 
1 2311 TRP n 
1 2312 VAL n 
1 2313 GLU n 
1 2314 ASN n 
1 2315 LEU n 
1 2316 ASN n 
1 2317 SER n 
1 2318 VAL n 
1 2319 LEU n 
1 2320 ASP n 
1 2321 ASP n 
1 2322 ASN n 
1 2323 LYS n 
1 2324 LEU n 
1 2325 LEU n 
1 2326 THR n 
1 2327 LEU n 
1 2328 PRO n 
1 2329 ASN n 
1 2330 GLY n 
1 2331 GLU n 
1 2332 ARG n 
1 2333 LEU n 
1 2334 SER n 
1 2335 LEU n 
1 2336 PRO n 
1 2337 PRO n 
1 2338 ASN n 
1 2339 VAL n 
1 2340 ARG n 
1 2341 ILE n 
1 2342 MET n 
1 2343 PHE n 
1 2344 GLU n 
1 2345 VAL n 
1 2346 GLN n 
1 2347 ASP n 
1 2348 LEU n 
1 2349 LYS n 
1 2350 TYR n 
1 2351 ALA n 
1 2352 THR n 
1 2353 LEU n 
1 2354 ALA n 
1 2355 THR n 
1 2356 VAL n 
1 2357 SER n 
1 2358 ARG n 
1 2359 CYS n 
1 2360 GLY n 
1 2361 MET n 
1 2362 VAL n 
1 2363 TRP n 
1 2364 PHE n 
1 2365 SER n 
1 2366 GLU n 
1 2367 ASP n 
1 2368 VAL n 
1 2369 LEU n 
1 2370 SER n 
1 2371 THR n 
1 2372 ASP n 
1 2373 MET n 
1 2374 ILE n 
1 2375 PHE n 
1 2376 ASN n 
1 2377 ASN n 
1 2378 PHE n 
1 2379 LEU n 
1 2380 ALA n 
1 2381 ARG n 
1 2382 LEU n 
1 2383 ARG n 
1 2384 SER n 
1 2385 ILE n 
1 2386 PRO n 
1 2387 LEU n 
1 2388 ASP n 
1 2389 GLU n 
1 2390 GLY n 
1 2391 GLU n 
1 2392 ASP n 
1 2393 GLU n 
1 2394 ALA n 
1 2395 GLN n 
1 2396 ARG n 
1 2397 ARG n 
1 2398 ARG n 
1 2399 LYS n 
1 2400 GLY n 
1 2401 LYS n 
1 2402 GLU n 
1 2403 ASP n 
1 2404 GLU n 
1 2405 GLY n 
1 2406 GLU n 
1 2407 GLU n 
1 2408 ALA n 
1 2409 ALA n 
1 2410 SER n 
1 2411 PRO n 
1 2412 MET n 
1 2413 LEU n 
1 2414 GLN n 
1 2415 ILE n 
1 2416 GLN n 
1 2417 ARG n 
1 2418 ASP n 
1 2419 ALA n 
1 2420 ALA n 
1 2421 THR n 
1 2422 ILE n 
1 2423 MET n 
1 2424 GLN n 
1 2425 PRO n 
1 2426 TYR n 
1 2427 PHE n 
1 2428 THR n 
1 2429 SER n 
1 2430 ASN n 
1 2431 GLY n 
1 2432 LEU n 
1 2433 VAL n 
1 2434 THR n 
1 2435 LYS n 
1 2436 ALA n 
1 2437 LEU n 
1 2438 GLU n 
1 2439 HIS n 
1 2440 ALA n 
1 2441 PHE n 
1 2442 GLN n 
1 2443 LEU n 
1 2444 GLU n 
1 2445 HIS n 
1 2446 ILE n 
1 2447 MET n 
1 2448 ASP n 
1 2449 LEU n 
1 2450 THR n 
1 2451 ARG n 
1 2452 LEU n 
1 2453 ARG n 
1 2454 CYS n 
1 2455 LEU n 
1 2456 GLY n 
1 2457 SER n 
1 2458 LEU n 
1 2459 PHE n 
1 2460 SER n 
1 2461 MET n 
1 2462 LEU n 
1 2463 HIS n 
1 2464 GLN n 
1 2465 ALA n 
1 2466 CYS n 
1 2467 ARG n 
1 2468 ASN n 
1 2469 VAL n 
1 2470 ALA n 
1 2471 GLN n 
1 2472 TYR n 
1 2473 ASN n 
1 2474 ALA n 
1 2475 ASN n 
1 2476 HIS n 
1 2477 PRO n 
1 2478 ASP n 
1 2479 PHE n 
1 2480 PRO n 
1 2481 MET n 
1 2482 GLN n 
1 2483 ILE n 
1 2484 GLU n 
1 2485 GLN n 
1 2486 LEU n 
1 2487 GLU n 
1 2488 ARG n 
1 2489 TYR n 
1 2490 ILE n 
1 2491 GLN n 
1 2492 ARG n 
1 2493 TYR n 
1 2494 LEU n 
1 2495 VAL n 
1 2496 TYR n 
1 2497 ALA n 
1 2498 ILE n 
1 2499 LEU n 
1 2500 TRP n 
1 2501 SER n 
1 2502 LEU n 
1 2503 SER n 
1 2504 GLY n 
1 2505 ASP n 
1 2506 SER n 
1 2507 ARG n 
1 2508 LEU n 
1 2509 LYS n 
1 2510 MET n 
1 2511 ARG n 
1 2512 ALA n 
1 2513 GLU n 
1 2514 LEU n 
1 2515 GLY n 
1 2516 GLU n 
1 2517 TYR n 
1 2518 ILE n 
1 2519 ARG n 
1 2520 ARG n 
1 2521 ILE n 
1 2522 THR n 
1 2523 THR n 
1 2524 VAL n 
1 2525 PRO n 
1 2526 LEU n 
1 2527 PRO n 
1 2528 THR n 
1 2529 ALA n 
1 2530 PRO n 
1 2531 ASN n 
1 2532 ILE n 
1 2533 PRO n 
1 2534 ILE n 
1 2535 ILE n 
1 2536 ASP n 
1 2537 TYR n 
1 2538 GLU n 
1 2539 VAL n 
1 2540 SER n 
1 2541 ILE n 
1 2542 SER n 
1 2543 GLY n 
1 2544 GLU n 
1 2545 TRP n 
1 2546 SER n 
1 2547 PRO n 
1 2548 TRP n 
1 2549 GLN n 
1 2550 ALA n 
1 2551 LYS n 
1 2552 VAL n 
1 2553 PRO n 
1 2554 GLN n 
1 2555 ILE n 
1 2556 GLU n 
1 2557 VAL n 
1 2558 GLU n 
1 2559 THR n 
1 2560 HIS n 
1 2561 LYS n 
1 2562 VAL n 
1 2563 ALA n 
1 2564 ALA n 
1 2565 PRO n 
1 2566 ASP n 
1 2567 VAL n 
1 2568 VAL n 
1 2569 VAL n 
1 2570 PRO n 
1 2571 THR n 
1 2572 LEU n 
1 2573 ASP n 
1 2574 THR n 
1 2575 VAL n 
1 2576 ARG n 
1 2577 HIS n 
1 2578 GLU n 
1 2579 ALA n 
1 2580 LEU n 
1 2581 LEU n 
1 2582 TYR n 
1 2583 THR n 
1 2584 TRP n 
1 2585 LEU n 
1 2586 ALA n 
1 2587 GLU n 
1 2588 HIS n 
1 2589 LYS n 
1 2590 PRO n 
1 2591 LEU n 
1 2592 VAL n 
1 2593 LEU n 
1 2594 CYS n 
1 2595 GLY n 
1 2596 PRO n 
1 2597 PRO n 
1 2598 GLY n 
1 2599 SER n 
1 2600 GLY n 
1 2601 LYS n 
1 2602 THR n 
1 2603 MET n 
1 2604 THR n 
1 2605 LEU n 
1 2606 PHE n 
1 2607 SER n 
1 2608 ALA n 
1 2609 LEU n 
1 2610 ARG n 
1 2611 ALA n 
1 2612 LEU n 
1 2613 PRO n 
1 2614 ASP n 
1 2615 MET n 
1 2616 GLU n 
1 2617 VAL n 
1 2618 VAL n 
1 2619 GLY n 
1 2620 LEU n 
1 2621 ASN n 
1 2622 PHE n 
1 2623 SER n 
1 2624 SER n 
1 2625 ALA n 
1 2626 THR n 
1 2627 THR n 
1 2628 PRO n 
1 2629 GLU n 
1 2630 LEU n 
1 2631 LEU n 
1 2632 LEU n 
1 2633 LYS n 
1 2634 THR n 
1 2635 PHE n 
1 2636 ASP n 
1 2637 HIS n 
1 2638 TYR n 
1 2639 CYS n 
1 2640 GLU n 
1 2641 TYR n 
1 2642 ARG n 
1 2643 ARG n 
1 2644 THR n 
1 2645 PRO n 
1 2646 ASN n 
1 2647 GLY n 
1 2648 VAL n 
1 2649 VAL n 
1 2650 LEU n 
1 2651 ALA n 
1 2652 PRO n 
1 2653 VAL n 
1 2654 GLN n 
1 2655 LEU n 
1 2656 GLY n 
1 2657 LYS n 
1 2658 TRP n 
1 2659 LEU n 
1 2660 VAL n 
1 2661 LEU n 
1 2662 PHE n 
1 2663 CYS n 
1 2664 ASP n 
1 2665 GLU n 
1 2666 ILE n 
1 2667 ASN n 
1 2668 LEU n 
1 2669 PRO n 
1 2670 ASP n 
1 2671 MET n 
1 2672 ASP n 
1 2673 LYS n 
1 2674 TYR n 
1 2675 GLY n 
1 2676 THR n 
1 2677 GLN n 
1 2678 ARG n 
1 2679 VAL n 
1 2680 ILE n 
1 2681 SER n 
1 2682 PHE n 
1 2683 ILE n 
1 2684 ARG n 
1 2685 GLN n 
1 2686 MET n 
1 2687 VAL n 
1 2688 GLU n 
1 2689 HIS n 
1 2690 GLY n 
1 2691 GLY n 
1 2692 PHE n 
1 2693 TYR n 
1 2694 ARG n 
1 2695 THR n 
1 2696 SER n 
1 2697 ASP n 
1 2698 GLN n 
1 2699 THR n 
1 2700 TRP n 
1 2701 VAL n 
1 2702 LYS n 
1 2703 LEU n 
1 2704 GLU n 
1 2705 ARG n 
1 2706 ILE n 
1 2707 GLN n 
1 2708 PHE n 
1 2709 VAL n 
1 2710 GLY n 
1 2711 ALA n 
1 2712 CYS n 
1 2713 ASN n 
1 2714 PRO n 
1 2715 PRO n 
1 2716 THR n 
1 2717 ASP n 
1 2718 PRO n 
1 2719 GLY n 
1 2720 ARG n 
1 2721 LYS n 
1 2722 PRO n 
1 2723 LEU n 
1 2724 SER n 
1 2725 HIS n 
1 2726 ARG n 
1 2727 PHE n 
1 2728 LEU n 
1 2729 ARG n 
1 2730 HIS n 
1 2731 VAL n 
1 2732 PRO n 
1 2733 VAL n 
1 2734 VAL n 
1 2735 TYR n 
1 2736 VAL n 
1 2737 ASP n 
1 2738 TYR n 
1 2739 PRO n 
1 2740 GLY n 
1 2741 PRO n 
1 2742 ALA n 
1 2743 SER n 
1 2744 LEU n 
1 2745 THR n 
1 2746 GLN n 
1 2747 ILE n 
1 2748 TYR n 
1 2749 GLY n 
1 2750 THR n 
1 2751 PHE n 
1 2752 ASN n 
1 2753 ARG n 
1 2754 ALA n 
1 2755 MET n 
1 2756 LEU n 
1 2757 ARG n 
1 2758 LEU n 
1 2759 ILE n 
1 2760 PRO n 
1 2761 SER n 
1 2762 LEU n 
1 2763 ARG n 
1 2764 THR n 
1 2765 TYR n 
1 2766 ALA n 
1 2767 GLU n 
1 2768 PRO n 
1 2769 LEU n 
1 2770 THR n 
1 2771 ALA n 
1 2772 ALA n 
1 2773 MET n 
1 2774 VAL n 
1 2775 GLU n 
1 2776 PHE n 
1 2777 TYR n 
1 2778 THR n 
1 2779 MET n 
1 2780 SER n 
1 2781 GLN n 
1 2782 GLU n 
1 2783 ARG n 
1 2784 PHE n 
1 2785 THR n 
1 2786 GLN n 
1 2787 ASP n 
1 2788 THR n 
1 2789 GLN n 
1 2790 PRO n 
1 2791 HIS n 
1 2792 TYR n 
1 2793 ILE n 
1 2794 TYR n 
1 2795 SER n 
1 2796 PRO n 
1 2797 ARG n 
1 2798 GLU n 
1 2799 MET n 
1 2800 THR n 
1 2801 ARG n 
1 2802 TRP n 
1 2803 VAL n 
1 2804 ARG n 
1 2805 GLY n 
1 2806 ILE n 
1 2807 PHE n 
1 2808 GLU n 
1 2809 ALA n 
1 2810 LEU n 
1 2811 ARG n 
1 2812 PRO n 
1 2813 LEU n 
1 2814 GLU n 
1 2815 THR n 
1 2816 LEU n 
1 2817 PRO n 
1 2818 VAL n 
1 2819 GLU n 
1 2820 GLY n 
1 2821 LEU n 
1 2822 ILE n 
1 2823 ARG n 
1 2824 ILE n 
1 2825 TRP n 
1 2826 ALA n 
1 2827 HIS n 
1 2828 GLU n 
1 2829 ALA n 
1 2830 LEU n 
1 2831 ARG n 
1 2832 LEU n 
1 2833 PHE n 
1 2834 GLN n 
1 2835 ASP n 
1 2836 ARG n 
1 2837 LEU n 
1 2838 VAL n 
1 2839 GLU n 
1 2840 ASP n 
1 2841 GLU n 
1 2842 GLU n 
1 2843 ARG n 
1 2844 ARG n 
1 2845 TRP n 
1 2846 THR n 
1 2847 ASP n 
1 2848 GLU n 
1 2849 ASN n 
1 2850 ILE n 
1 2851 ASP n 
1 2852 THR n 
1 2853 VAL n 
1 2854 ALA n 
1 2855 LEU n 
1 2856 LYS n 
1 2857 HIS n 
1 2858 PHE n 
1 2859 PRO n 
1 2860 ASN n 
1 2861 ILE n 
1 2862 ASP n 
1 2863 ARG n 
1 2864 GLU n 
1 2865 LYS n 
1 2866 ALA n 
1 2867 MET n 
1 2868 SER n 
1 2869 ARG n 
1 2870 PRO n 
1 2871 ILE n 
1 2872 LEU n 
1 2873 TYR n 
1 2874 SER n 
1 2875 ASN n 
1 2876 TRP n 
1 2877 LEU n 
1 2878 SER n 
1 2879 LYS n 
1 2880 ASP n 
1 2881 TYR n 
1 2882 ILE n 
1 2883 PRO n 
1 2884 VAL n 
1 2885 ASP n 
1 2886 GLN n 
1 2887 GLU n 
1 2888 GLU n 
1 2889 LEU n 
1 2890 ARG n 
1 2891 ASP n 
1 2892 TYR n 
1 2893 VAL n 
1 2894 LYS n 
1 2895 ALA n 
1 2896 ARG n 
1 2897 LEU n 
1 2898 LYS n 
1 2899 VAL n 
1 2900 PHE n 
1 2901 TYR n 
1 2902 GLU n 
1 2903 GLU n 
1 2904 GLU n 
1 2905 LEU n 
1 2906 ASP n 
1 2907 VAL n 
1 2908 PRO n 
1 2909 LEU n 
1 2910 VAL n 
1 2911 LEU n 
1 2912 PHE n 
1 2913 ASN n 
1 2914 GLU n 
1 2915 VAL n 
1 2916 LEU n 
1 2917 ASP n 
1 2918 HIS n 
1 2919 VAL n 
1 2920 LEU n 
1 2921 ARG n 
1 2922 ILE n 
1 2923 ASP n 
1 2924 ARG n 
1 2925 ILE n 
1 2926 PHE n 
1 2927 ARG n 
1 2928 GLN n 
1 2929 PRO n 
1 2930 GLN n 
1 2931 GLY n 
1 2932 HIS n 
1 2933 LEU n 
1 2934 LEU n 
1 2935 LEU n 
1 2936 ILE n 
1 2937 GLY n 
1 2938 VAL n 
1 2939 SER n 
1 2940 GLY n 
1 2941 ALA n 
1 2942 GLY n 
1 2943 LYS n 
1 2944 THR n 
1 2945 THR n 
1 2946 LEU n 
1 2947 SER n 
1 2948 ARG n 
1 2949 PHE n 
1 2950 VAL n 
1 2951 ALA n 
1 2952 TRP n 
1 2953 MET n 
1 2954 ASN n 
1 2955 GLY n 
1 2956 LEU n 
1 2957 SER n 
1 2958 VAL n 
1 2959 TYR n 
1 2960 GLN n 
1 2961 ILE n 
1 2962 LYS n 
1 2963 VAL n 
1 2964 HIS n 
1 2965 ARG n 
1 2966 LYS n 
1 2967 TYR n 
1 2968 THR n 
1 2969 GLY n 
1 2970 GLU n 
1 2971 ASP n 
1 2972 PHE n 
1 2973 ASP n 
1 2974 GLU n 
1 2975 ASP n 
1 2976 LEU n 
1 2977 ARG n 
1 2978 THR n 
1 2979 VAL n 
1 2980 LEU n 
1 2981 ARG n 
1 2982 ARG n 
1 2983 SER n 
1 2984 GLY n 
1 2985 CYS n 
1 2986 LYS n 
1 2987 ASN n 
1 2988 GLU n 
1 2989 LYS n 
1 2990 ILE n 
1 2991 ALA n 
1 2992 PHE n 
1 2993 ILE n 
1 2994 MET n 
1 2995 ASP n 
1 2996 GLU n 
1 2997 SER n 
1 2998 ASN n 
1 2999 VAL n 
1 3000 LEU n 
1 3001 ASP n 
1 3002 SER n 
1 3003 GLY n 
1 3004 PHE n 
1 3005 LEU n 
1 3006 GLU n 
1 3007 ARG n 
1 3008 MET n 
1 3009 ASN n 
1 3010 THR n 
1 3011 LEU n 
1 3012 LEU n 
1 3013 ALA n 
1 3014 ASN n 
1 3015 GLY n 
1 3016 GLU n 
1 3017 VAL n 
1 3018 PRO n 
1 3019 GLY n 
1 3020 LEU n 
1 3021 PHE n 
1 3022 GLU n 
1 3023 GLY n 
1 3024 ASP n 
1 3025 GLU n 
1 3026 TYR n 
1 3027 ALA n 
1 3028 THR n 
1 3029 LEU n 
1 3030 MET n 
1 3031 THR n 
1 3032 GLN n 
1 3033 CYS n 
1 3034 LYS n 
1 3035 GLU n 
1 3036 GLY n 
1 3037 ALA n 
1 3038 GLN n 
1 3039 LYS n 
1 3040 GLU n 
1 3041 GLY n 
1 3042 LEU n 
1 3043 MET n 
1 3044 LEU n 
1 3045 ASP n 
1 3046 SER n 
1 3047 HIS n 
1 3048 GLU n 
1 3049 GLU n 
1 3050 LEU n 
1 3051 TYR n 
1 3052 LYS n 
1 3053 TRP n 
1 3054 PHE n 
1 3055 THR n 
1 3056 SER n 
1 3057 GLN n 
1 3058 VAL n 
1 3059 ILE n 
1 3060 ARG n 
1 3061 ASN n 
1 3062 LEU n 
1 3063 HIS n 
1 3064 VAL n 
1 3065 VAL n 
1 3066 PHE n 
1 3067 THR n 
1 3068 MET n 
1 3069 ASN n 
1 3070 PRO n 
1 3071 SER n 
1 3072 SER n 
1 3073 GLU n 
1 3074 GLY n 
1 3075 LEU n 
1 3076 LYS n 
1 3077 ASP n 
1 3078 ARG n 
1 3079 ALA n 
1 3080 ALA n 
1 3081 THR n 
1 3082 SER n 
1 3083 PRO n 
1 3084 ALA n 
1 3085 LEU n 
1 3086 PHE n 
1 3087 ASN n 
1 3088 ARG n 
1 3089 CYS n 
1 3090 VAL n 
1 3091 LEU n 
1 3092 ASN n 
1 3093 TRP n 
1 3094 PHE n 
1 3095 GLY n 
1 3096 ASP n 
1 3097 TRP n 
1 3098 SER n 
1 3099 THR n 
1 3100 GLU n 
1 3101 ALA n 
1 3102 LEU n 
1 3103 TYR n 
1 3104 GLN n 
1 3105 VAL n 
1 3106 GLY n 
1 3107 LYS n 
1 3108 GLU n 
1 3109 PHE n 
1 3110 THR n 
1 3111 SER n 
1 3112 LYS n 
1 3113 MET n 
1 3114 ASP n 
1 3115 LEU n 
1 3116 GLU n 
1 3117 LYS n 
1 3118 PRO n 
1 3119 ASN n 
1 3120 TYR n 
1 3121 ILE n 
1 3122 VAL n 
1 3123 PRO n 
1 3124 ASP n 
1 3125 TYR n 
1 3126 MET n 
1 3127 PRO n 
1 3128 VAL n 
1 3129 VAL n 
1 3130 TYR n 
1 3131 ASP n 
1 3132 LYS n 
1 3133 LEU n 
1 3134 PRO n 
1 3135 GLN n 
1 3136 PRO n 
1 3137 PRO n 
1 3138 SER n 
1 3139 HIS n 
1 3140 ARG n 
1 3141 GLU n 
1 3142 ALA n 
1 3143 ILE n 
1 3144 VAL n 
1 3145 ASN n 
1 3146 SER n 
1 3147 CYS n 
1 3148 VAL n 
1 3149 PHE n 
1 3150 VAL n 
1 3151 HIS n 
1 3152 GLN n 
1 3153 THR n 
1 3154 LEU n 
1 3155 HIS n 
1 3156 GLN n 
1 3157 ALA n 
1 3158 ASN n 
1 3159 ALA n 
1 3160 ARG n 
1 3161 LEU n 
1 3162 ALA n 
1 3163 LYS n 
1 3164 ARG n 
1 3165 GLY n 
1 3166 GLY n 
1 3167 ARG n 
1 3168 THR n 
1 3169 MET n 
1 3170 ALA n 
1 3171 ILE n 
1 3172 THR n 
1 3173 PRO n 
1 3174 ARG n 
1 3175 HIS n 
1 3176 TYR n 
1 3177 LEU n 
1 3178 ASP n 
1 3179 PHE n 
1 3180 ILE n 
1 3181 ASN n 
1 3182 HIS n 
1 3183 TYR n 
1 3184 ALA n 
1 3185 ASN n 
1 3186 LEU n 
1 3187 PHE n 
1 3188 HIS n 
1 3189 GLU n 
1 3190 LYS n 
1 3191 ARG n 
1 3192 SER n 
1 3193 GLU n 
1 3194 LEU n 
1 3195 GLU n 
1 3196 GLU n 
1 3197 GLN n 
1 3198 GLN n 
1 3199 MET n 
1 3200 HIS n 
1 3201 LEU n 
1 3202 ASN n 
1 3203 VAL n 
1 3204 GLY n 
1 3205 LEU n 
1 3206 ARG n 
1 3207 LYS n 
1 3208 ILE n 
1 3209 LYS n 
1 3210 GLU n 
1 3211 THR n 
1 3212 VAL n 
1 3213 ASP n 
1 3214 GLN n 
1 3215 VAL n 
1 3216 GLU n 
1 3217 GLU n 
1 3218 LEU n 
1 3219 ARG n 
1 3220 ARG n 
1 3221 ASP n 
1 3222 LEU n 
1 3223 ARG n 
1 3224 ILE n 
1 3225 LYS n 
1 3226 SER n 
1 3227 GLN n 
1 3228 GLU n 
1 3229 LEU n 
1 3230 GLU n 
1 3231 VAL n 
1 3232 LYS n 
1 3233 ASN n 
1 3234 ALA n 
1 3235 ALA n 
1 3236 ALA n 
1 3237 ASN n 
1 3238 ASP n 
1 3239 LYS n 
1 3240 LEU n 
1 3241 LYS n 
1 3242 LYS n 
1 3243 MET n 
1 3244 VAL n 
1 3245 LYS n 
1 3246 ASP n 
1 3247 GLN n 
1 3248 GLN n 
1 3249 GLU n 
1 3250 ALA n 
1 3251 GLU n 
1 3252 LYS n 
1 3253 LYS n 
1 3254 LYS n 
1 3255 VAL n 
1 3256 MET n 
1 3257 SER n 
1 3258 GLN n 
1 3259 GLU n 
1 3260 ILE n 
1 3261 GLN n 
1 3262 GLU n 
1 3263 GLN n 
1 3264 LEU n 
1 3265 HIS n 
1 3266 LYS n 
1 3267 GLN n 
1 3268 GLN n 
1 3269 GLU n 
1 3270 VAL n 
1 3271 ILE n 
1 3272 ALA n 
1 3273 ASP n 
1 3274 LYS n 
1 3275 GLN n 
1 3276 MET n 
1 3277 SER n 
1 3278 VAL n 
1 3279 LYS n 
1 3280 GLU n 
1 3281 ASP n 
1 3282 LEU n 
1 3283 ASP n 
1 3284 LYS n 
1 3285 VAL n 
1 3286 GLU n 
1 3287 PRO n 
1 3288 ALA n 
1 3289 VAL n 
1 3290 ILE n 
1 3291 GLU n 
1 3292 ALA n 
1 3293 GLN n 
1 3294 ASN n 
1 3295 ALA n 
1 3296 VAL n 
1 3297 LYS n 
1 3298 SER n 
1 3299 ILE n 
1 3300 LYS n 
1 3301 LYS n 
1 3302 GLN n 
1 3303 HIS n 
1 3304 LEU n 
1 3305 VAL n 
1 3306 GLU n 
1 3307 VAL n 
1 3308 ARG n 
1 3309 SER n 
1 3310 MET n 
1 3311 ALA n 
1 3312 ASN n 
1 3313 PRO n 
1 3314 PRO n 
1 3315 ALA n 
1 3316 ALA n 
1 3317 VAL n 
1 3318 LYS n 
1 3319 LEU n 
1 3320 ALA n 
1 3321 LEU n 
1 3322 GLU n 
1 3323 SER n 
1 3324 ILE n 
1 3325 CYS n 
1 3326 LEU n 
1 3327 LEU n 
1 3328 LEU n 
1 3329 GLY n 
1 3330 GLU n 
1 3331 SER n 
1 3332 THR n 
1 3333 THR n 
1 3334 ASP n 
1 3335 TRP n 
1 3336 LYS n 
1 3337 GLN n 
1 3338 ILE n 
1 3339 ARG n 
1 3340 SER n 
1 3341 ILE n 
1 3342 ILE n 
1 3343 MET n 
1 3344 ARG n 
1 3345 GLU n 
1 3346 ASN n 
1 3347 PHE n 
1 3348 ILE n 
1 3349 PRO n 
1 3350 THR n 
1 3351 ILE n 
1 3352 VAL n 
1 3353 ASN n 
1 3354 PHE n 
1 3355 SER n 
1 3356 ALA n 
1 3357 GLU n 
1 3358 GLU n 
1 3359 ILE n 
1 3360 SER n 
1 3361 ASP n 
1 3362 ALA n 
1 3363 ILE n 
1 3364 ARG n 
1 3365 GLU n 
1 3366 LYS n 
1 3367 MET n 
1 3368 LYS n 
1 3369 LYS n 
1 3370 ASN n 
1 3371 TYR n 
1 3372 MET n 
1 3373 SER n 
1 3374 ASN n 
1 3375 PRO n 
1 3376 SER n 
1 3377 TYR n 
1 3378 ASN n 
1 3379 TYR n 
1 3380 GLU n 
1 3381 ILE n 
1 3382 VAL n 
1 3383 ASN n 
1 3384 ARG n 
1 3385 ALA n 
1 3386 SER n 
1 3387 LEU n 
1 3388 ALA n 
1 3389 CYS n 
1 3390 GLY n 
1 3391 PRO n 
1 3392 MET n 
1 3393 VAL n 
1 3394 LYS n 
1 3395 TRP n 
1 3396 ALA n 
1 3397 ILE n 
1 3398 ALA n 
1 3399 GLN n 
1 3400 LEU n 
1 3401 ASN n 
1 3402 TYR n 
1 3403 ALA n 
1 3404 ASP n 
1 3405 MET n 
1 3406 LEU n 
1 3407 LYS n 
1 3408 ARG n 
1 3409 VAL n 
1 3410 GLU n 
1 3411 PRO n 
1 3412 LEU n 
1 3413 ARG n 
1 3414 ASN n 
1 3415 GLU n 
1 3416 LEU n 
1 3417 GLN n 
1 3418 LYS n 
1 3419 LEU n 
1 3420 GLU n 
1 3421 ASP n 
1 3422 ASP n 
1 3423 ALA n 
1 3424 LYS n 
1 3425 ASP n 
1 3426 ASN n 
1 3427 GLN n 
1 3428 GLN n 
1 3429 LYS n 
1 3430 ALA n 
1 3431 ASN n 
1 3432 GLU n 
1 3433 VAL n 
1 3434 GLU n 
1 3435 GLN n 
1 3436 MET n 
1 3437 ILE n 
1 3438 ARG n 
1 3439 ASP n 
1 3440 LEU n 
1 3441 GLU n 
1 3442 ALA n 
1 3443 SER n 
1 3444 ILE n 
1 3445 ALA n 
1 3446 ARG n 
1 3447 TYR n 
1 3448 LYS n 
1 3449 GLU n 
1 3450 GLU n 
1 3451 TYR n 
1 3452 ALA n 
1 3453 VAL n 
1 3454 LEU n 
1 3455 ILE n 
1 3456 SER n 
1 3457 GLU n 
1 3458 ALA n 
1 3459 GLN n 
1 3460 ALA n 
1 3461 ILE n 
1 3462 LYS n 
1 3463 ALA n 
1 3464 ASP n 
1 3465 LEU n 
1 3466 ALA n 
1 3467 ALA n 
1 3468 VAL n 
1 3469 GLU n 
1 3470 ALA n 
1 3471 LYS n 
1 3472 VAL n 
1 3473 ASN n 
1 3474 ARG n 
1 3475 SER n 
1 3476 THR n 
1 3477 ALA n 
1 3478 LEU n 
1 3479 LEU n 
1 3480 LYS n 
1 3481 SER n 
1 3482 LEU n 
1 3483 SER n 
1 3484 ALA n 
1 3485 GLU n 
1 3486 ARG n 
1 3487 GLU n 
1 3488 ARG n 
1 3489 TRP n 
1 3490 GLU n 
1 3491 LYS n 
1 3492 THR n 
1 3493 SER n 
1 3494 GLU n 
1 3495 THR n 
1 3496 PHE n 
1 3497 LYS n 
1 3498 ASN n 
1 3499 GLN n 
1 3500 MET n 
1 3501 SER n 
1 3502 THR n 
1 3503 ILE n 
1 3504 ALA n 
1 3505 GLY n 
1 3506 ASP n 
1 3507 CYS n 
1 3508 LEU n 
1 3509 LEU n 
1 3510 SER n 
1 3511 ALA n 
1 3512 ALA n 
1 3513 PHE n 
1 3514 ILE n 
1 3515 ALA n 
1 3516 TYR n 
1 3517 ALA n 
1 3518 GLY n 
1 3519 TYR n 
1 3520 PHE n 
1 3521 ASP n 
1 3522 GLN n 
1 3523 GLN n 
1 3524 MET n 
1 3525 ARG n 
1 3526 GLN n 
1 3527 ASN n 
1 3528 LEU n 
1 3529 PHE n 
1 3530 THR n 
1 3531 THR n 
1 3532 TRP n 
1 3533 SER n 
1 3534 HIS n 
1 3535 HIS n 
1 3536 LEU n 
1 3537 GLN n 
1 3538 GLN n 
1 3539 ALA n 
1 3540 ASN n 
1 3541 ILE n 
1 3542 GLN n 
1 3543 PHE n 
1 3544 ARG n 
1 3545 THR n 
1 3546 ASP n 
1 3547 ILE n 
1 3548 ALA n 
1 3549 ARG n 
1 3550 THR n 
1 3551 GLU n 
1 3552 TYR n 
1 3553 LEU n 
1 3554 SER n 
1 3555 ASN n 
1 3556 ALA n 
1 3557 ASP n 
1 3558 GLU n 
1 3559 ARG n 
1 3560 LEU n 
1 3561 ARG n 
1 3562 TRP n 
1 3563 GLN n 
1 3564 ALA n 
1 3565 SER n 
1 3566 SER n 
1 3567 LEU n 
1 3568 PRO n 
1 3569 ALA n 
1 3570 ASP n 
1 3571 ASP n 
1 3572 LEU n 
1 3573 CYS n 
1 3574 THR n 
1 3575 GLU n 
1 3576 ASN n 
1 3577 ALA n 
1 3578 ILE n 
1 3579 MET n 
1 3580 LEU n 
1 3581 LYS n 
1 3582 ARG n 
1 3583 PHE n 
1 3584 ASN n 
1 3585 ARG n 
1 3586 TYR n 
1 3587 PRO n 
1 3588 LEU n 
1 3589 ILE n 
1 3590 ILE n 
1 3591 ASP n 
1 3592 PRO n 
1 3593 SER n 
1 3594 GLY n 
1 3595 GLN n 
1 3596 ALA n 
1 3597 THR n 
1 3598 GLU n 
1 3599 PHE n 
1 3600 ILE n 
1 3601 MET n 
1 3602 ASN n 
1 3603 GLU n 
1 3604 TYR n 
1 3605 LYS n 
1 3606 ASP n 
1 3607 ARG n 
1 3608 LYS n 
1 3609 ILE n 
1 3610 THR n 
1 3611 ARG n 
1 3612 THR n 
1 3613 SER n 
1 3614 PHE n 
1 3615 LEU n 
1 3616 ASP n 
1 3617 ASP n 
1 3618 ALA n 
1 3619 PHE n 
1 3620 ARG n 
1 3621 LYS n 
1 3622 ASN n 
1 3623 LEU n 
1 3624 GLU n 
1 3625 SER n 
1 3626 ALA n 
1 3627 LEU n 
1 3628 ARG n 
1 3629 PHE n 
1 3630 GLY n 
1 3631 ASN n 
1 3632 PRO n 
1 3633 LEU n 
1 3634 LEU n 
1 3635 VAL n 
1 3636 GLN n 
1 3637 ASP n 
1 3638 VAL n 
1 3639 GLU n 
1 3640 SER n 
1 3641 TYR n 
1 3642 ASP n 
1 3643 PRO n 
1 3644 VAL n 
1 3645 LEU n 
1 3646 ASN n 
1 3647 PRO n 
1 3648 VAL n 
1 3649 LEU n 
1 3650 ASN n 
1 3651 ARG n 
1 3652 GLU n 
1 3653 VAL n 
1 3654 ARG n 
1 3655 ARG n 
1 3656 THR n 
1 3657 GLY n 
1 3658 GLY n 
1 3659 ARG n 
1 3660 VAL n 
1 3661 LEU n 
1 3662 ILE n 
1 3663 THR n 
1 3664 LEU n 
1 3665 GLY n 
1 3666 ASP n 
1 3667 GLN n 
1 3668 ASP n 
1 3669 ILE n 
1 3670 ASP n 
1 3671 LEU n 
1 3672 SER n 
1 3673 PRO n 
1 3674 SER n 
1 3675 PHE n 
1 3676 VAL n 
1 3677 ILE n 
1 3678 PHE n 
1 3679 LEU n 
1 3680 SER n 
1 3681 THR n 
1 3682 ARG n 
1 3683 ASP n 
1 3684 PRO n 
1 3685 THR n 
1 3686 VAL n 
1 3687 GLU n 
1 3688 PHE n 
1 3689 PRO n 
1 3690 PRO n 
1 3691 ASP n 
1 3692 LEU n 
1 3693 CYS n 
1 3694 SER n 
1 3695 ARG n 
1 3696 VAL n 
1 3697 THR n 
1 3698 PHE n 
1 3699 VAL n 
1 3700 ASN n 
1 3701 PHE n 
1 3702 THR n 
1 3703 VAL n 
1 3704 THR n 
1 3705 ARG n 
1 3706 SER n 
1 3707 SER n 
1 3708 LEU n 
1 3709 GLN n 
1 3710 SER n 
1 3711 GLN n 
1 3712 CYS n 
1 3713 LEU n 
1 3714 ASN n 
1 3715 GLU n 
1 3716 VAL n 
1 3717 LEU n 
1 3718 LYS n 
1 3719 ALA n 
1 3720 GLU n 
1 3721 ARG n 
1 3722 PRO n 
1 3723 ASP n 
1 3724 VAL n 
1 3725 ASP n 
1 3726 GLU n 
1 3727 LYS n 
1 3728 ARG n 
1 3729 SER n 
1 3730 ASP n 
1 3731 LEU n 
1 3732 LEU n 
1 3733 LYS n 
1 3734 LEU n 
1 3735 GLN n 
1 3736 GLY n 
1 3737 GLU n 
1 3738 PHE n 
1 3739 GLN n 
1 3740 LEU n 
1 3741 ARG n 
1 3742 LEU n 
1 3743 ARG n 
1 3744 GLN n 
1 3745 LEU n 
1 3746 GLU n 
1 3747 LYS n 
1 3748 SER n 
1 3749 LEU n 
1 3750 LEU n 
1 3751 GLN n 
1 3752 ALA n 
1 3753 LEU n 
1 3754 ASN n 
1 3755 GLU n 
1 3756 VAL n 
1 3757 LYS n 
1 3758 GLY n 
1 3759 ARG n 
1 3760 ILE n 
1 3761 LEU n 
1 3762 ASP n 
1 3763 ASP n 
1 3764 ASP n 
1 3765 THR n 
1 3766 ILE n 
1 3767 ILE n 
1 3768 THR n 
1 3769 THR n 
1 3770 LEU n 
1 3771 GLU n 
1 3772 ASN n 
1 3773 LEU n 
1 3774 LYS n 
1 3775 ARG n 
1 3776 GLU n 
1 3777 ALA n 
1 3778 ALA n 
1 3779 GLU n 
1 3780 VAL n 
1 3781 THR n 
1 3782 ARG n 
1 3783 LYS n 
1 3784 VAL n 
1 3785 GLU n 
1 3786 GLU n 
1 3787 THR n 
1 3788 ASP n 
1 3789 ILE n 
1 3790 VAL n 
1 3791 MET n 
1 3792 GLN n 
1 3793 GLU n 
1 3794 VAL n 
1 3795 GLU n 
1 3796 THR n 
1 3797 VAL n 
1 3798 SER n 
1 3799 GLN n 
1 3800 GLN n 
1 3801 TYR n 
1 3802 LEU n 
1 3803 PRO n 
1 3804 LEU n 
1 3805 SER n 
1 3806 THR n 
1 3807 ALA n 
1 3808 CYS n 
1 3809 SER n 
1 3810 SER n 
1 3811 ILE n 
1 3812 TYR n 
1 3813 PHE n 
1 3814 THR n 
1 3815 MET n 
1 3816 GLU n 
1 3817 SER n 
1 3818 LEU n 
1 3819 LYS n 
1 3820 GLN n 
1 3821 ILE n 
1 3822 HIS n 
1 3823 PHE n 
1 3824 LEU n 
1 3825 TYR n 
1 3826 GLN n 
1 3827 TYR n 
1 3828 SER n 
1 3829 LEU n 
1 3830 GLN n 
1 3831 PHE n 
1 3832 PHE n 
1 3833 LEU n 
1 3834 ASP n 
1 3835 ILE n 
1 3836 TYR n 
1 3837 HIS n 
1 3838 ASN n 
1 3839 VAL n 
1 3840 LEU n 
1 3841 TYR n 
1 3842 GLU n 
1 3843 ASN n 
1 3844 PRO n 
1 3845 ASN n 
1 3846 LEU n 
1 3847 LYS n 
1 3848 GLY n 
1 3849 VAL n 
1 3850 THR n 
1 3851 ASP n 
1 3852 HIS n 
1 3853 THR n 
1 3854 GLN n 
1 3855 ARG n 
1 3856 LEU n 
1 3857 SER n 
1 3858 ILE n 
1 3859 ILE n 
1 3860 THR n 
1 3861 LYS n 
1 3862 ASP n 
1 3863 LEU n 
1 3864 PHE n 
1 3865 GLN n 
1 3866 VAL n 
1 3867 ALA n 
1 3868 PHE n 
1 3869 ASN n 
1 3870 ARG n 
1 3871 VAL n 
1 3872 ALA n 
1 3873 ARG n 
1 3874 GLY n 
1 3875 MET n 
1 3876 LEU n 
1 3877 HIS n 
1 3878 GLN n 
1 3879 ASP n 
1 3880 HIS n 
1 3881 ILE n 
1 3882 THR n 
1 3883 PHE n 
1 3884 ALA n 
1 3885 MET n 
1 3886 LEU n 
1 3887 LEU n 
1 3888 ALA n 
1 3889 ARG n 
1 3890 ILE n 
1 3891 LYS n 
1 3892 LEU n 
1 3893 LYS n 
1 3894 GLY n 
1 3895 THR n 
1 3896 VAL n 
1 3897 GLY n 
1 3898 GLU n 
1 3899 PRO n 
1 3900 THR n 
1 3901 TYR n 
1 3902 ASP n 
1 3903 ALA n 
1 3904 GLU n 
1 3905 PHE n 
1 3906 GLN n 
1 3907 HIS n 
1 3908 PHE n 
1 3909 LEU n 
1 3910 ARG n 
1 3911 GLY n 
1 3912 ASN n 
1 3913 GLU n 
1 3914 ILE n 
1 3915 VAL n 
1 3916 LEU n 
1 3917 SER n 
1 3918 ALA n 
1 3919 GLY n 
1 3920 SER n 
1 3921 THR n 
1 3922 PRO n 
1 3923 ARG n 
1 3924 ILE n 
1 3925 GLN n 
1 3926 GLY n 
1 3927 LEU n 
1 3928 THR n 
1 3929 VAL n 
1 3930 GLU n 
1 3931 GLN n 
1 3932 ALA n 
1 3933 GLU n 
1 3934 ALA n 
1 3935 VAL n 
1 3936 VAL n 
1 3937 ARG n 
1 3938 LEU n 
1 3939 SER n 
1 3940 CYS n 
1 3941 LEU n 
1 3942 PRO n 
1 3943 ALA n 
1 3944 PHE n 
1 3945 LYS n 
1 3946 ASP n 
1 3947 LEU n 
1 3948 ILE n 
1 3949 ALA n 
1 3950 LYS n 
1 3951 VAL n 
1 3952 GLN n 
1 3953 ALA n 
1 3954 ASP n 
1 3955 GLU n 
1 3956 GLN n 
1 3957 PHE n 
1 3958 GLY n 
1 3959 ILE n 
1 3960 TRP n 
1 3961 LEU n 
1 3962 ASP n 
1 3963 SER n 
1 3964 SER n 
1 3965 SER n 
1 3966 PRO n 
1 3967 GLU n 
1 3968 GLN n 
1 3969 THR n 
1 3970 VAL n 
1 3971 PRO n 
1 3972 TYR n 
1 3973 LEU n 
1 3974 TRP n 
1 3975 SER n 
1 3976 GLU n 
1 3977 GLU n 
1 3978 THR n 
1 3979 PRO n 
1 3980 ALA n 
1 3981 THR n 
1 3982 PRO n 
1 3983 ILE n 
1 3984 GLY n 
1 3985 GLN n 
1 3986 ALA n 
1 3987 ILE n 
1 3988 HIS n 
1 3989 ARG n 
1 3990 LEU n 
1 3991 LEU n 
1 3992 LEU n 
1 3993 ILE n 
1 3994 GLN n 
1 3995 ALA n 
1 3996 PHE n 
1 3997 ARG n 
1 3998 PRO n 
1 3999 ASP n 
1 4000 ARG n 
1 4001 LEU n 
1 4002 LEU n 
1 4003 ALA n 
1 4004 MET n 
1 4005 ALA n 
1 4006 HIS n 
1 4007 MET n 
1 4008 PHE n 
1 4009 VAL n 
1 4010 SER n 
1 4011 THR n 
1 4012 ASN n 
1 4013 LEU n 
1 4014 GLY n 
1 4015 GLU n 
1 4016 SER n 
1 4017 PHE n 
1 4018 MET n 
1 4019 SER n 
1 4020 ILE n 
1 4021 MET n 
1 4022 GLU n 
1 4023 GLN n 
1 4024 PRO n 
1 4025 LEU n 
1 4026 ASP n 
1 4027 LEU n 
1 4028 THR n 
1 4029 HIS n 
1 4030 ILE n 
1 4031 VAL n 
1 4032 GLY n 
1 4033 THR n 
1 4034 GLU n 
1 4035 VAL n 
1 4036 LYS n 
1 4037 PRO n 
1 4038 ASN n 
1 4039 THR n 
1 4040 PRO n 
1 4041 VAL n 
1 4042 LEU n 
1 4043 MET n 
1 4044 CYS n 
1 4045 SER n 
1 4046 VAL n 
1 4047 PRO n 
1 4048 GLY n 
1 4049 TYR n 
1 4050 ASP n 
1 4051 ALA n 
1 4052 SER n 
1 4053 GLY n 
1 4054 HIS n 
1 4055 VAL n 
1 4056 GLU n 
1 4057 ASP n 
1 4058 LEU n 
1 4059 ALA n 
1 4060 ALA n 
1 4061 GLU n 
1 4062 GLN n 
1 4063 ASN n 
1 4064 THR n 
1 4065 GLN n 
1 4066 ILE n 
1 4067 THR n 
1 4068 SER n 
1 4069 ILE n 
1 4070 ALA n 
1 4071 ILE n 
1 4072 GLY n 
1 4073 SER n 
1 4074 ALA n 
1 4075 GLU n 
1 4076 GLY n 
1 4077 PHE n 
1 4078 ASN n 
1 4079 GLN n 
1 4080 ALA n 
1 4081 ASP n 
1 4082 LYS n 
1 4083 ALA n 
1 4084 ILE n 
1 4085 ASN n 
1 4086 THR n 
1 4087 ALA n 
1 4088 VAL n 
1 4089 LYS n 
1 4090 SER n 
1 4091 GLY n 
1 4092 ARG n 
1 4093 TRP n 
1 4094 VAL n 
1 4095 MET n 
1 4096 LEU n 
1 4097 LYS n 
1 4098 ASN n 
1 4099 VAL n 
1 4100 HIS n 
1 4101 LEU n 
1 4102 ALA n 
1 4103 PRO n 
1 4104 GLY n 
1 4105 TRP n 
1 4106 LEU n 
1 4107 MET n 
1 4108 GLN n 
1 4109 LEU n 
1 4110 GLU n 
1 4111 LYS n 
1 4112 LYS n 
1 4113 LEU n 
1 4114 HIS n 
1 4115 SER n 
1 4116 LEU n 
1 4117 GLN n 
1 4118 PRO n 
1 4119 HIS n 
1 4120 ALA n 
1 4121 CYS n 
1 4122 PHE n 
1 4123 ARG n 
1 4124 LEU n 
1 4125 PHE n 
1 4126 LEU n 
1 4127 THR n 
1 4128 MET n 
1 4129 GLU n 
1 4130 ILE n 
1 4131 ASN n 
1 4132 PRO n 
1 4133 LYS n 
1 4134 VAL n 
1 4135 PRO n 
1 4136 VAL n 
1 4137 ASN n 
1 4138 LEU n 
1 4139 LEU n 
1 4140 ARG n 
1 4141 ALA n 
1 4142 GLY n 
1 4143 ARG n 
1 4144 ILE n 
1 4145 PHE n 
1 4146 VAL n 
1 4147 PHE n 
1 4148 GLU n 
1 4149 PRO n 
1 4150 PRO n 
1 4151 PRO n 
1 4152 GLY n 
1 4153 VAL n 
1 4154 LYS n 
1 4155 ALA n 
1 4156 ASN n 
1 4157 MET n 
1 4158 LEU n 
1 4159 ARG n 
1 4160 THR n 
1 4161 PHE n 
1 4162 SER n 
1 4163 SER n 
1 4164 ILE n 
1 4165 PRO n 
1 4166 VAL n 
1 4167 SER n 
1 4168 ARG n 
1 4169 ILE n 
1 4170 CYS n 
1 4171 LYS n 
1 4172 SER n 
1 4173 PRO n 
1 4174 ASN n 
1 4175 GLU n 
1 4176 ARG n 
1 4177 ALA n 
1 4178 ARG n 
1 4179 LEU n 
1 4180 TYR n 
1 4181 PHE n 
1 4182 LEU n 
1 4183 LEU n 
1 4184 ALA n 
1 4185 TRP n 
1 4186 PHE n 
1 4187 HIS n 
1 4188 ALA n 
1 4189 ILE n 
1 4190 ILE n 
1 4191 GLN n 
1 4192 GLU n 
1 4193 ARG n 
1 4194 LEU n 
1 4195 ARG n 
1 4196 TYR n 
1 4197 ALA n 
1 4198 PRO n 
1 4199 LEU n 
1 4200 GLY n 
1 4201 TRP n 
1 4202 SER n 
1 4203 LYS n 
1 4204 LYS n 
1 4205 TYR n 
1 4206 GLU n 
1 4207 PHE n 
1 4208 GLY n 
1 4209 GLU n 
1 4210 SER n 
1 4211 ASP n 
1 4212 LEU n 
1 4213 ARG n 
1 4214 SER n 
1 4215 ALA n 
1 4216 CYS n 
1 4217 ASP n 
1 4218 THR n 
1 4219 VAL n 
1 4220 ASP n 
1 4221 THR n 
1 4222 TRP n 
1 4223 LEU n 
1 4224 ASP n 
1 4225 ASP n 
1 4226 THR n 
1 4227 ALA n 
1 4228 LYS n 
1 4229 GLY n 
1 4230 ARG n 
1 4231 GLN n 
1 4232 ASN n 
1 4233 ILE n 
1 4234 SER n 
1 4235 PRO n 
1 4236 ASP n 
1 4237 LYS n 
1 4238 ILE n 
1 4239 PRO n 
1 4240 TRP n 
1 4241 SER n 
1 4242 ALA n 
1 4243 LEU n 
1 4244 LYS n 
1 4245 THR n 
1 4246 LEU n 
1 4247 MET n 
1 4248 ALA n 
1 4249 GLN n 
1 4250 SER n 
1 4251 ILE n 
1 4252 TYR n 
1 4253 GLY n 
1 4254 GLY n 
1 4255 ARG n 
1 4256 VAL n 
1 4257 ASP n 
1 4258 ASN n 
1 4259 GLU n 
1 4260 PHE n 
1 4261 ASP n 
1 4262 GLN n 
1 4263 ARG n 
1 4264 LEU n 
1 4265 LEU n 
1 4266 ASN n 
1 4267 THR n 
1 4268 PHE n 
1 4269 LEU n 
1 4270 GLU n 
1 4271 ARG n 
1 4272 LEU n 
1 4273 PHE n 
1 4274 THR n 
1 4275 THR n 
1 4276 ARG n 
1 4277 SER n 
1 4278 PHE n 
1 4279 ASP n 
1 4280 SER n 
1 4281 GLU n 
1 4282 PHE n 
1 4283 LYS n 
1 4284 LEU n 
1 4285 ALA n 
1 4286 CYS n 
1 4287 LYS n 
1 4288 VAL n 
1 4289 ASP n 
1 4290 GLY n 
1 4291 HIS n 
1 4292 LYS n 
1 4293 ASP n 
1 4294 ILE n 
1 4295 GLN n 
1 4296 MET n 
1 4297 PRO n 
1 4298 ASP n 
1 4299 GLY n 
1 4300 ILE n 
1 4301 ARG n 
1 4302 ARG n 
1 4303 GLU n 
1 4304 GLU n 
1 4305 PHE n 
1 4306 VAL n 
1 4307 GLN n 
1 4308 TRP n 
1 4309 VAL n 
1 4310 GLU n 
1 4311 LEU n 
1 4312 LEU n 
1 4313 PRO n 
1 4314 ASP n 
1 4315 THR n 
1 4316 GLN n 
1 4317 THR n 
1 4318 PRO n 
1 4319 SER n 
1 4320 TRP n 
1 4321 LEU n 
1 4322 GLY n 
1 4323 LEU n 
1 4324 PRO n 
1 4325 ASN n 
1 4326 ASN n 
1 4327 ALA n 
1 4328 GLU n 
1 4329 ARG n 
1 4330 VAL n 
1 4331 LEU n 
1 4332 LEU n 
1 4333 THR n 
1 4334 THR n 
1 4335 GLN n 
1 4336 GLY n 
1 4337 VAL n 
1 4338 ASP n 
1 4339 MET n 
1 4340 ILE n 
1 4341 SER n 
1 4342 LYS n 
1 4343 MET n 
1 4344 LEU n 
1 4345 LYS n 
1 4346 MET n 
1 4347 GLN n 
1 4348 MET n 
1 4349 LEU n 
1 4350 GLU n 
1 4351 ASP n 
1 4352 GLU n 
1 4353 ASP n 
1 4354 ASP n 
1 4355 LEU n 
1 4356 ALA n 
1 4357 TYR n 
1 4358 ALA n 
1 4359 GLU n 
1 4360 THR n 
1 4361 GLU n 
1 4362 LYS n 
1 4363 LYS n 
1 4364 THR n 
1 4365 ARG n 
1 4366 THR n 
1 4367 ASP n 
1 4368 SER n 
1 4369 THR n 
1 4370 SER n 
1 4371 ASP n 
1 4372 GLY n 
1 4373 ARG n 
1 4374 PRO n 
1 4375 ALA n 
1 4376 TRP n 
1 4377 MET n 
1 4378 ARG n 
1 4379 THR n 
1 4380 LEU n 
1 4381 HIS n 
1 4382 THR n 
1 4383 THR n 
1 4384 ALA n 
1 4385 SER n 
1 4386 ASN n 
1 4387 TRP n 
1 4388 LEU n 
1 4389 HIS n 
1 4390 LEU n 
1 4391 ILE n 
1 4392 PRO n 
1 4393 GLN n 
1 4394 THR n 
1 4395 LEU n 
1 4396 SER n 
1 4397 HIS n 
1 4398 LEU n 
1 4399 LYS n 
1 4400 ARG n 
1 4401 THR n 
1 4402 VAL n 
1 4403 GLU n 
1 4404 ASN n 
1 4405 ILE n 
1 4406 LYS n 
1 4407 ASP n 
1 4408 PRO n 
1 4409 LEU n 
1 4410 PHE n 
1 4411 ARG n 
1 4412 PHE n 
1 4413 PHE n 
1 4414 GLU n 
1 4415 ARG n 
1 4416 GLU n 
1 4417 VAL n 
1 4418 LYS n 
1 4419 MET n 
1 4420 GLY n 
1 4421 ALA n 
1 4422 LYS n 
1 4423 LEU n 
1 4424 LEU n 
1 4425 GLN n 
1 4426 ASP n 
1 4427 VAL n 
1 4428 ARG n 
1 4429 GLN n 
1 4430 ASP n 
1 4431 LEU n 
1 4432 ALA n 
1 4433 ASP n 
1 4434 VAL n 
1 4435 VAL n 
1 4436 GLN n 
1 4437 VAL n 
1 4438 CYS n 
1 4439 GLU n 
1 4440 GLY n 
1 4441 LYS n 
1 4442 LYS n 
1 4443 LYS n 
1 4444 GLN n 
1 4445 THR n 
1 4446 ASN n 
1 4447 TYR n 
1 4448 LEU n 
1 4449 ARG n 
1 4450 THR n 
1 4451 LEU n 
1 4452 ILE n 
1 4453 ASN n 
1 4454 GLU n 
1 4455 LEU n 
1 4456 VAL n 
1 4457 LYS n 
1 4458 GLY n 
1 4459 ILE n 
1 4460 LEU n 
1 4461 PRO n 
1 4462 ARG n 
1 4463 SER n 
1 4464 TRP n 
1 4465 SER n 
1 4466 HIS n 
1 4467 TYR n 
1 4468 THR n 
1 4469 VAL n 
1 4470 PRO n 
1 4471 ALA n 
1 4472 GLY n 
1 4473 MET n 
1 4474 THR n 
1 4475 VAL n 
1 4476 ILE n 
1 4477 GLN n 
1 4478 TRP n 
1 4479 VAL n 
1 4480 SER n 
1 4481 ASP n 
1 4482 PHE n 
1 4483 SER n 
1 4484 GLU n 
1 4485 ARG n 
1 4486 ILE n 
1 4487 LYS n 
1 4488 GLN n 
1 4489 LEU n 
1 4490 GLN n 
1 4491 ASN n 
1 4492 ILE n 
1 4493 SER n 
1 4494 LEU n 
1 4495 ALA n 
1 4496 ALA n 
1 4497 ALA n 
1 4498 SER n 
1 4499 GLY n 
1 4500 GLY n 
1 4501 ALA n 
1 4502 LYS n 
1 4503 GLU n 
1 4504 LEU n 
1 4505 LYS n 
1 4506 ASN n 
1 4507 ILE n 
1 4508 HIS n 
1 4509 VAL n 
1 4510 CYS n 
1 4511 LEU n 
1 4512 GLY n 
1 4513 GLY n 
1 4514 LEU n 
1 4515 PHE n 
1 4516 VAL n 
1 4517 PRO n 
1 4518 GLU n 
1 4519 ALA n 
1 4520 TYR n 
1 4521 ILE n 
1 4522 THR n 
1 4523 ALA n 
1 4524 THR n 
1 4525 ARG n 
1 4526 GLN n 
1 4527 TYR n 
1 4528 VAL n 
1 4529 ALA n 
1 4530 GLN n 
1 4531 ALA n 
1 4532 ASN n 
1 4533 SER n 
1 4534 TRP n 
1 4535 SER n 
1 4536 LEU n 
1 4537 GLU n 
1 4538 GLU n 
1 4539 LEU n 
1 4540 CYS n 
1 4541 LEU n 
1 4542 GLU n 
1 4543 VAL n 
1 4544 ASN n 
1 4545 VAL n 
1 4546 THR n 
1 4547 THR n 
1 4548 SER n 
1 4549 GLN n 
1 4550 GLY n 
1 4551 ALA n 
1 4552 THR n 
1 4553 LEU n 
1 4554 ASP n 
1 4555 ALA n 
1 4556 CYS n 
1 4557 SER n 
1 4558 PHE n 
1 4559 GLY n 
1 4560 VAL n 
1 4561 THR n 
1 4562 GLY n 
1 4563 LEU n 
1 4564 LYS n 
1 4565 LEU n 
1 4566 GLN n 
1 4567 GLY n 
1 4568 ALA n 
1 4569 THR n 
1 4570 CYS n 
1 4571 ASN n 
1 4572 ASN n 
1 4573 ASN n 
1 4574 LYS n 
1 4575 LEU n 
1 4576 SER n 
1 4577 LEU n 
1 4578 SER n 
1 4579 ASN n 
1 4580 ALA n 
1 4581 ILE n 
1 4582 SER n 
1 4583 THR n 
1 4584 ALA n 
1 4585 LEU n 
1 4586 PRO n 
1 4587 LEU n 
1 4588 THR n 
1 4589 GLN n 
1 4590 LEU n 
1 4591 ARG n 
1 4592 TRP n 
1 4593 VAL n 
1 4594 LYS n 
1 4595 GLN n 
1 4596 THR n 
1 4597 ASN n 
1 4598 THR n 
1 4599 GLU n 
1 4600 LYS n 
1 4601 LYS n 
1 4602 ALA n 
1 4603 SER n 
1 4604 VAL n 
1 4605 VAL n 
1 4606 THR n 
1 4607 LEU n 
1 4608 PRO n 
1 4609 VAL n 
1 4610 TYR n 
1 4611 LEU n 
1 4612 ASN n 
1 4613 PHE n 
1 4614 THR n 
1 4615 ARG n 
1 4616 ALA n 
1 4617 ASP n 
1 4618 LEU n 
1 4619 ILE n 
1 4620 PHE n 
1 4621 THR n 
1 4622 VAL n 
1 4623 ASP n 
1 4624 PHE n 
1 4625 GLU n 
1 4626 ILE n 
1 4627 ALA n 
1 4628 THR n 
1 4629 LYS n 
1 4630 GLU n 
1 4631 ASP n 
1 4632 PRO n 
1 4633 ARG n 
1 4634 SER n 
1 4635 PHE n 
1 4636 TYR n 
1 4637 GLU n 
1 4638 ARG n 
1 4639 GLY n 
1 4640 VAL n 
1 4641 ALA n 
1 4642 VAL n 
1 4643 LEU n 
1 4644 CYS n 
1 4645 THR n 
1 4646 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   4646 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O10 P2' 427.201 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                       ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    GLU 3    3    ?    ?   ?   A . n 
A 1 4    PRO 4    4    ?    ?   ?   A . n 
A 1 5    GLY 5    5    ?    ?   ?   A . n 
A 1 6    GLY 6    6    ?    ?   ?   A . n 
A 1 7    GLY 7    7    ?    ?   ?   A . n 
A 1 8    GLY 8    8    ?    ?   ?   A . n 
A 1 9    GLY 9    9    ?    ?   ?   A . n 
A 1 10   GLU 10   10   ?    ?   ?   A . n 
A 1 11   ASP 11   11   ?    ?   ?   A . n 
A 1 12   GLY 12   12   ?    ?   ?   A . n 
A 1 13   SER 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   GLY 15   15   ?    ?   ?   A . n 
A 1 16   LEU 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   SER 19   19   ?    ?   ?   A . n 
A 1 20   ALA 20   20   ?    ?   ?   A . n 
A 1 21   VAL 21   21   ?    ?   ?   A . n 
A 1 22   GLN 22   22   ?    ?   ?   A . n 
A 1 23   ASN 23   23   ?    ?   ?   A . n 
A 1 24   VAL 24   24   ?    ?   ?   A . n 
A 1 25   ALA 25   25   ?    ?   ?   A . n 
A 1 26   ASP 26   26   ?    ?   ?   A . n 
A 1 27   VAL 27   27   ?    ?   ?   A . n 
A 1 28   SER 28   28   ?    ?   ?   A . n 
A 1 29   VAL 29   29   ?    ?   ?   A . n 
A 1 30   LEU 30   30   ?    ?   ?   A . n 
A 1 31   GLN 31   31   ?    ?   ?   A . n 
A 1 32   LYS 32   32   ?    ?   ?   A . n 
A 1 33   HIS 33   33   ?    ?   ?   A . n 
A 1 34   LEU 34   34   ?    ?   ?   A . n 
A 1 35   ARG 35   35   ?    ?   ?   A . n 
A 1 36   LYS 36   36   ?    ?   ?   A . n 
A 1 37   LEU 37   37   ?    ?   ?   A . n 
A 1 38   VAL 38   38   ?    ?   ?   A . n 
A 1 39   PRO 39   39   ?    ?   ?   A . n 
A 1 40   LEU 40   40   ?    ?   ?   A . n 
A 1 41   LEU 41   41   ?    ?   ?   A . n 
A 1 42   LEU 42   42   ?    ?   ?   A . n 
A 1 43   GLU 43   43   ?    ?   ?   A . n 
A 1 44   ASP 44   44   ?    ?   ?   A . n 
A 1 45   GLY 45   45   ?    ?   ?   A . n 
A 1 46   GLY 46   46   ?    ?   ?   A . n 
A 1 47   GLU 47   47   ?    ?   ?   A . n 
A 1 48   ALA 48   48   ?    ?   ?   A . n 
A 1 49   PRO 49   49   ?    ?   ?   A . n 
A 1 50   ALA 50   50   ?    ?   ?   A . n 
A 1 51   ALA 51   51   ?    ?   ?   A . n 
A 1 52   LEU 52   52   ?    ?   ?   A . n 
A 1 53   GLU 53   53   ?    ?   ?   A . n 
A 1 54   ALA 54   54   ?    ?   ?   A . n 
A 1 55   ALA 55   55   ?    ?   ?   A . n 
A 1 56   LEU 56   56   ?    ?   ?   A . n 
A 1 57   GLU 57   57   ?    ?   ?   A . n 
A 1 58   GLU 58   58   ?    ?   ?   A . n 
A 1 59   LYS 59   59   ?    ?   ?   A . n 
A 1 60   SER 60   60   ?    ?   ?   A . n 
A 1 61   ALA 61   61   ?    ?   ?   A . n 
A 1 62   LEU 62   62   ?    ?   ?   A . n 
A 1 63   GLU 63   63   ?    ?   ?   A . n 
A 1 64   GLN 64   64   ?    ?   ?   A . n 
A 1 65   MET 65   65   ?    ?   ?   A . n 
A 1 66   ARG 66   66   ?    ?   ?   A . n 
A 1 67   LYS 67   67   ?    ?   ?   A . n 
A 1 68   PHE 68   68   ?    ?   ?   A . n 
A 1 69   LEU 69   69   ?    ?   ?   A . n 
A 1 70   SER 70   70   ?    ?   ?   A . n 
A 1 71   ASP 71   71   ?    ?   ?   A . n 
A 1 72   PRO 72   72   ?    ?   ?   A . n 
A 1 73   GLN 73   73   ?    ?   ?   A . n 
A 1 74   VAL 74   74   ?    ?   ?   A . n 
A 1 75   HIS 75   75   ?    ?   ?   A . n 
A 1 76   THR 76   76   ?    ?   ?   A . n 
A 1 77   VAL 77   77   ?    ?   ?   A . n 
A 1 78   LEU 78   78   ?    ?   ?   A . n 
A 1 79   VAL 79   79   ?    ?   ?   A . n 
A 1 80   GLU 80   80   ?    ?   ?   A . n 
A 1 81   ARG 81   81   ?    ?   ?   A . n 
A 1 82   SER 82   82   ?    ?   ?   A . n 
A 1 83   THR 83   83   ?    ?   ?   A . n 
A 1 84   LEU 84   84   ?    ?   ?   A . n 
A 1 85   LYS 85   85   ?    ?   ?   A . n 
A 1 86   GLU 86   86   ?    ?   ?   A . n 
A 1 87   ASP 87   87   ?    ?   ?   A . n 
A 1 88   VAL 88   88   ?    ?   ?   A . n 
A 1 89   GLY 89   89   ?    ?   ?   A . n 
A 1 90   ASP 90   90   ?    ?   ?   A . n 
A 1 91   GLU 91   91   ?    ?   ?   A . n 
A 1 92   GLY 92   92   ?    ?   ?   A . n 
A 1 93   GLU 93   93   ?    ?   ?   A . n 
A 1 94   GLU 94   94   ?    ?   ?   A . n 
A 1 95   GLU 95   95   ?    ?   ?   A . n 
A 1 96   LYS 96   96   ?    ?   ?   A . n 
A 1 97   GLU 97   97   ?    ?   ?   A . n 
A 1 98   PHE 98   98   ?    ?   ?   A . n 
A 1 99   ILE 99   99   ?    ?   ?   A . n 
A 1 100  SER 100  100  ?    ?   ?   A . n 
A 1 101  TYR 101  101  ?    ?   ?   A . n 
A 1 102  ASN 102  102  ?    ?   ?   A . n 
A 1 103  ILE 103  103  ?    ?   ?   A . n 
A 1 104  ASN 104  104  ?    ?   ?   A . n 
A 1 105  ILE 105  105  ?    ?   ?   A . n 
A 1 106  ASP 106  106  ?    ?   ?   A . n 
A 1 107  ILE 107  107  ?    ?   ?   A . n 
A 1 108  HIS 108  108  ?    ?   ?   A . n 
A 1 109  TYR 109  109  ?    ?   ?   A . n 
A 1 110  GLY 110  110  ?    ?   ?   A . n 
A 1 111  VAL 111  111  ?    ?   ?   A . n 
A 1 112  LYS 112  112  ?    ?   ?   A . n 
A 1 113  SER 113  113  ?    ?   ?   A . n 
A 1 114  ASN 114  114  ?    ?   ?   A . n 
A 1 115  SER 115  115  ?    ?   ?   A . n 
A 1 116  LEU 116  116  ?    ?   ?   A . n 
A 1 117  ALA 117  117  ?    ?   ?   A . n 
A 1 118  PHE 118  118  ?    ?   ?   A . n 
A 1 119  ILE 119  119  ?    ?   ?   A . n 
A 1 120  LYS 120  120  ?    ?   ?   A . n 
A 1 121  ARG 121  121  ?    ?   ?   A . n 
A 1 122  THR 122  122  ?    ?   ?   A . n 
A 1 123  PRO 123  123  ?    ?   ?   A . n 
A 1 124  VAL 124  124  ?    ?   ?   A . n 
A 1 125  ILE 125  125  ?    ?   ?   A . n 
A 1 126  ASP 126  126  ?    ?   ?   A . n 
A 1 127  ALA 127  127  ?    ?   ?   A . n 
A 1 128  ASP 128  128  ?    ?   ?   A . n 
A 1 129  LYS 129  129  ?    ?   ?   A . n 
A 1 130  PRO 130  130  ?    ?   ?   A . n 
A 1 131  VAL 131  131  ?    ?   ?   A . n 
A 1 132  SER 132  132  ?    ?   ?   A . n 
A 1 133  SER 133  133  ?    ?   ?   A . n 
A 1 134  GLN 134  134  ?    ?   ?   A . n 
A 1 135  LEU 135  135  ?    ?   ?   A . n 
A 1 136  ARG 136  136  ?    ?   ?   A . n 
A 1 137  VAL 137  137  ?    ?   ?   A . n 
A 1 138  LEU 138  138  ?    ?   ?   A . n 
A 1 139  THR 139  139  ?    ?   ?   A . n 
A 1 140  LEU 140  140  ?    ?   ?   A . n 
A 1 141  SER 141  141  ?    ?   ?   A . n 
A 1 142  GLU 142  142  ?    ?   ?   A . n 
A 1 143  ASP 143  143  ?    ?   ?   A . n 
A 1 144  SER 144  144  ?    ?   ?   A . n 
A 1 145  PRO 145  145  ?    ?   ?   A . n 
A 1 146  TYR 146  146  ?    ?   ?   A . n 
A 1 147  GLU 147  147  ?    ?   ?   A . n 
A 1 148  THR 148  148  ?    ?   ?   A . n 
A 1 149  LEU 149  149  ?    ?   ?   A . n 
A 1 150  HIS 150  150  ?    ?   ?   A . n 
A 1 151  SER 151  151  ?    ?   ?   A . n 
A 1 152  PHE 152  152  ?    ?   ?   A . n 
A 1 153  ILE 153  153  ?    ?   ?   A . n 
A 1 154  SER 154  154  ?    ?   ?   A . n 
A 1 155  ASN 155  155  ?    ?   ?   A . n 
A 1 156  ALA 156  156  ?    ?   ?   A . n 
A 1 157  VAL 157  157  ?    ?   ?   A . n 
A 1 158  ALA 158  158  ?    ?   ?   A . n 
A 1 159  PRO 159  159  ?    ?   ?   A . n 
A 1 160  PHE 160  160  ?    ?   ?   A . n 
A 1 161  PHE 161  161  ?    ?   ?   A . n 
A 1 162  LYS 162  162  ?    ?   ?   A . n 
A 1 163  SER 163  163  ?    ?   ?   A . n 
A 1 164  TYR 164  164  ?    ?   ?   A . n 
A 1 165  ILE 165  165  ?    ?   ?   A . n 
A 1 166  ARG 166  166  ?    ?   ?   A . n 
A 1 167  GLU 167  167  ?    ?   ?   A . n 
A 1 168  SER 168  168  ?    ?   ?   A . n 
A 1 169  GLY 169  169  ?    ?   ?   A . n 
A 1 170  LYS 170  170  ?    ?   ?   A . n 
A 1 171  ALA 171  171  ?    ?   ?   A . n 
A 1 172  ASP 172  172  ?    ?   ?   A . n 
A 1 173  ARG 173  173  ?    ?   ?   A . n 
A 1 174  ASP 174  174  ?    ?   ?   A . n 
A 1 175  GLY 175  175  ?    ?   ?   A . n 
A 1 176  ASP 176  176  ?    ?   ?   A . n 
A 1 177  LYS 177  177  ?    ?   ?   A . n 
A 1 178  MET 178  178  ?    ?   ?   A . n 
A 1 179  ALA 179  179  ?    ?   ?   A . n 
A 1 180  PRO 180  180  ?    ?   ?   A . n 
A 1 181  SER 181  181  ?    ?   ?   A . n 
A 1 182  VAL 182  182  ?    ?   ?   A . n 
A 1 183  GLU 183  183  ?    ?   ?   A . n 
A 1 184  LYS 184  184  ?    ?   ?   A . n 
A 1 185  LYS 185  185  ?    ?   ?   A . n 
A 1 186  ILE 186  186  ?    ?   ?   A . n 
A 1 187  ALA 187  187  ?    ?   ?   A . n 
A 1 188  GLU 188  188  ?    ?   ?   A . n 
A 1 189  LEU 189  189  ?    ?   ?   A . n 
A 1 190  GLU 190  190  ?    ?   ?   A . n 
A 1 191  MET 191  191  ?    ?   ?   A . n 
A 1 192  GLY 192  192  ?    ?   ?   A . n 
A 1 193  LEU 193  193  ?    ?   ?   A . n 
A 1 194  LEU 194  194  ?    ?   ?   A . n 
A 1 195  HIS 195  195  ?    ?   ?   A . n 
A 1 196  LEU 196  196  ?    ?   ?   A . n 
A 1 197  GLN 197  197  ?    ?   ?   A . n 
A 1 198  GLN 198  198  ?    ?   ?   A . n 
A 1 199  ASN 199  199  ?    ?   ?   A . n 
A 1 200  ILE 200  200  ?    ?   ?   A . n 
A 1 201  GLU 201  201  ?    ?   ?   A . n 
A 1 202  ILE 202  202  ?    ?   ?   A . n 
A 1 203  PRO 203  203  ?    ?   ?   A . n 
A 1 204  GLU 204  204  ?    ?   ?   A . n 
A 1 205  ILE 205  205  ?    ?   ?   A . n 
A 1 206  SER 206  206  ?    ?   ?   A . n 
A 1 207  LEU 207  207  ?    ?   ?   A . n 
A 1 208  PRO 208  208  ?    ?   ?   A . n 
A 1 209  ILE 209  209  ?    ?   ?   A . n 
A 1 210  HIS 210  210  ?    ?   ?   A . n 
A 1 211  PRO 211  211  ?    ?   ?   A . n 
A 1 212  MET 212  212  ?    ?   ?   A . n 
A 1 213  ILE 213  213  ?    ?   ?   A . n 
A 1 214  THR 214  214  ?    ?   ?   A . n 
A 1 215  ASN 215  215  ?    ?   ?   A . n 
A 1 216  VAL 216  216  ?    ?   ?   A . n 
A 1 217  ALA 217  217  ?    ?   ?   A . n 
A 1 218  LYS 218  218  ?    ?   ?   A . n 
A 1 219  GLN 219  219  ?    ?   ?   A . n 
A 1 220  CYS 220  220  ?    ?   ?   A . n 
A 1 221  TYR 221  221  ?    ?   ?   A . n 
A 1 222  GLU 222  222  ?    ?   ?   A . n 
A 1 223  ARG 223  223  ?    ?   ?   A . n 
A 1 224  GLY 224  224  ?    ?   ?   A . n 
A 1 225  GLU 225  225  ?    ?   ?   A . n 
A 1 226  LYS 226  226  ?    ?   ?   A . n 
A 1 227  PRO 227  227  ?    ?   ?   A . n 
A 1 228  LYS 228  228  ?    ?   ?   A . n 
A 1 229  VAL 229  229  ?    ?   ?   A . n 
A 1 230  THR 230  230  ?    ?   ?   A . n 
A 1 231  ASP 231  231  ?    ?   ?   A . n 
A 1 232  PHE 232  232  ?    ?   ?   A . n 
A 1 233  GLY 233  233  ?    ?   ?   A . n 
A 1 234  ASP 234  234  ?    ?   ?   A . n 
A 1 235  LYS 235  235  ?    ?   ?   A . n 
A 1 236  VAL 236  236  ?    ?   ?   A . n 
A 1 237  GLU 237  237  ?    ?   ?   A . n 
A 1 238  ASP 238  238  ?    ?   ?   A . n 
A 1 239  PRO 239  239  ?    ?   ?   A . n 
A 1 240  THR 240  240  ?    ?   ?   A . n 
A 1 241  PHE 241  241  ?    ?   ?   A . n 
A 1 242  LEU 242  242  ?    ?   ?   A . n 
A 1 243  ASN 243  243  ?    ?   ?   A . n 
A 1 244  GLN 244  244  ?    ?   ?   A . n 
A 1 245  LEU 245  245  ?    ?   ?   A . n 
A 1 246  GLN 246  246  ?    ?   ?   A . n 
A 1 247  SER 247  247  ?    ?   ?   A . n 
A 1 248  GLY 248  248  ?    ?   ?   A . n 
A 1 249  VAL 249  249  ?    ?   ?   A . n 
A 1 250  ASN 250  250  ?    ?   ?   A . n 
A 1 251  ARG 251  251  ?    ?   ?   A . n 
A 1 252  TRP 252  252  ?    ?   ?   A . n 
A 1 253  ILE 253  253  ?    ?   ?   A . n 
A 1 254  ARG 254  254  ?    ?   ?   A . n 
A 1 255  GLU 255  255  ?    ?   ?   A . n 
A 1 256  ILE 256  256  ?    ?   ?   A . n 
A 1 257  GLN 257  257  ?    ?   ?   A . n 
A 1 258  LYS 258  258  ?    ?   ?   A . n 
A 1 259  VAL 259  259  ?    ?   ?   A . n 
A 1 260  THR 260  260  ?    ?   ?   A . n 
A 1 261  LYS 261  261  ?    ?   ?   A . n 
A 1 262  LEU 262  262  ?    ?   ?   A . n 
A 1 263  ASP 263  263  ?    ?   ?   A . n 
A 1 264  ARG 264  264  ?    ?   ?   A . n 
A 1 265  ASP 265  265  ?    ?   ?   A . n 
A 1 266  PRO 266  266  ?    ?   ?   A . n 
A 1 267  ALA 267  267  ?    ?   ?   A . n 
A 1 268  SER 268  268  ?    ?   ?   A . n 
A 1 269  GLY 269  269  ?    ?   ?   A . n 
A 1 270  THR 270  270  ?    ?   ?   A . n 
A 1 271  ALA 271  271  ?    ?   ?   A . n 
A 1 272  LEU 272  272  ?    ?   ?   A . n 
A 1 273  GLN 273  273  ?    ?   ?   A . n 
A 1 274  GLU 274  274  ?    ?   ?   A . n 
A 1 275  ILE 275  275  ?    ?   ?   A . n 
A 1 276  SER 276  276  ?    ?   ?   A . n 
A 1 277  PHE 277  277  ?    ?   ?   A . n 
A 1 278  TRP 278  278  ?    ?   ?   A . n 
A 1 279  LEU 279  279  ?    ?   ?   A . n 
A 1 280  ASN 280  280  ?    ?   ?   A . n 
A 1 281  LEU 281  281  ?    ?   ?   A . n 
A 1 282  GLU 282  282  ?    ?   ?   A . n 
A 1 283  ARG 283  283  ?    ?   ?   A . n 
A 1 284  ALA 284  284  ?    ?   ?   A . n 
A 1 285  LEU 285  285  ?    ?   ?   A . n 
A 1 286  TYR 286  286  ?    ?   ?   A . n 
A 1 287  ARG 287  287  ?    ?   ?   A . n 
A 1 288  ILE 288  288  ?    ?   ?   A . n 
A 1 289  GLN 289  289  ?    ?   ?   A . n 
A 1 290  GLU 290  290  ?    ?   ?   A . n 
A 1 291  LYS 291  291  ?    ?   ?   A . n 
A 1 292  ARG 292  292  ?    ?   ?   A . n 
A 1 293  GLU 293  293  ?    ?   ?   A . n 
A 1 294  SER 294  294  ?    ?   ?   A . n 
A 1 295  PRO 295  295  ?    ?   ?   A . n 
A 1 296  GLU 296  296  ?    ?   ?   A . n 
A 1 297  VAL 297  297  ?    ?   ?   A . n 
A 1 298  LEU 298  298  ?    ?   ?   A . n 
A 1 299  LEU 299  299  ?    ?   ?   A . n 
A 1 300  THR 300  300  ?    ?   ?   A . n 
A 1 301  LEU 301  301  ?    ?   ?   A . n 
A 1 302  ASP 302  302  ?    ?   ?   A . n 
A 1 303  ILE 303  303  ?    ?   ?   A . n 
A 1 304  LEU 304  304  ?    ?   ?   A . n 
A 1 305  LYS 305  305  ?    ?   ?   A . n 
A 1 306  HIS 306  306  ?    ?   ?   A . n 
A 1 307  GLY 307  307  ?    ?   ?   A . n 
A 1 308  LYS 308  308  ?    ?   ?   A . n 
A 1 309  ARG 309  309  ?    ?   ?   A . n 
A 1 310  PHE 310  310  ?    ?   ?   A . n 
A 1 311  HIS 311  311  ?    ?   ?   A . n 
A 1 312  ALA 312  312  ?    ?   ?   A . n 
A 1 313  THR 313  313  ?    ?   ?   A . n 
A 1 314  VAL 314  314  ?    ?   ?   A . n 
A 1 315  SER 315  315  ?    ?   ?   A . n 
A 1 316  PHE 316  316  ?    ?   ?   A . n 
A 1 317  ASP 317  317  ?    ?   ?   A . n 
A 1 318  THR 318  318  ?    ?   ?   A . n 
A 1 319  ASP 319  319  ?    ?   ?   A . n 
A 1 320  THR 320  320  ?    ?   ?   A . n 
A 1 321  GLY 321  321  ?    ?   ?   A . n 
A 1 322  LEU 322  322  ?    ?   ?   A . n 
A 1 323  LYS 323  323  ?    ?   ?   A . n 
A 1 324  GLN 324  324  ?    ?   ?   A . n 
A 1 325  ALA 325  325  ?    ?   ?   A . n 
A 1 326  LEU 326  326  ?    ?   ?   A . n 
A 1 327  GLU 327  327  ?    ?   ?   A . n 
A 1 328  THR 328  328  ?    ?   ?   A . n 
A 1 329  VAL 329  329  ?    ?   ?   A . n 
A 1 330  ASN 330  330  ?    ?   ?   A . n 
A 1 331  ASP 331  331  ?    ?   ?   A . n 
A 1 332  TYR 332  332  ?    ?   ?   A . n 
A 1 333  ASN 333  333  ?    ?   ?   A . n 
A 1 334  PRO 334  334  ?    ?   ?   A . n 
A 1 335  LEU 335  335  ?    ?   ?   A . n 
A 1 336  MET 336  336  ?    ?   ?   A . n 
A 1 337  LYS 337  337  ?    ?   ?   A . n 
A 1 338  ASP 338  338  ?    ?   ?   A . n 
A 1 339  PHE 339  339  ?    ?   ?   A . n 
A 1 340  PRO 340  340  ?    ?   ?   A . n 
A 1 341  LEU 341  341  ?    ?   ?   A . n 
A 1 342  ASN 342  342  ?    ?   ?   A . n 
A 1 343  ASP 343  343  ?    ?   ?   A . n 
A 1 344  LEU 344  344  ?    ?   ?   A . n 
A 1 345  LEU 345  345  ?    ?   ?   A . n 
A 1 346  SER 346  346  ?    ?   ?   A . n 
A 1 347  ALA 347  347  ?    ?   ?   A . n 
A 1 348  THR 348  348  ?    ?   ?   A . n 
A 1 349  GLU 349  349  ?    ?   ?   A . n 
A 1 350  LEU 350  350  ?    ?   ?   A . n 
A 1 351  ASP 351  351  ?    ?   ?   A . n 
A 1 352  LYS 352  352  ?    ?   ?   A . n 
A 1 353  ILE 353  353  ?    ?   ?   A . n 
A 1 354  ARG 354  354  ?    ?   ?   A . n 
A 1 355  GLN 355  355  ?    ?   ?   A . n 
A 1 356  ALA 356  356  ?    ?   ?   A . n 
A 1 357  LEU 357  357  ?    ?   ?   A . n 
A 1 358  VAL 358  358  ?    ?   ?   A . n 
A 1 359  ALA 359  359  ?    ?   ?   A . n 
A 1 360  ILE 360  360  ?    ?   ?   A . n 
A 1 361  PHE 361  361  ?    ?   ?   A . n 
A 1 362  THR 362  362  ?    ?   ?   A . n 
A 1 363  HIS 363  363  ?    ?   ?   A . n 
A 1 364  LEU 364  364  ?    ?   ?   A . n 
A 1 365  ARG 365  365  ?    ?   ?   A . n 
A 1 366  LYS 366  366  ?    ?   ?   A . n 
A 1 367  ILE 367  367  ?    ?   ?   A . n 
A 1 368  ARG 368  368  ?    ?   ?   A . n 
A 1 369  ASN 369  369  ?    ?   ?   A . n 
A 1 370  THR 370  370  ?    ?   ?   A . n 
A 1 371  LYS 371  371  ?    ?   ?   A . n 
A 1 372  TYR 372  372  ?    ?   ?   A . n 
A 1 373  PRO 373  373  ?    ?   ?   A . n 
A 1 374  ILE 374  374  ?    ?   ?   A . n 
A 1 375  GLN 375  375  ?    ?   ?   A . n 
A 1 376  ARG 376  376  ?    ?   ?   A . n 
A 1 377  ALA 377  377  ?    ?   ?   A . n 
A 1 378  LEU 378  378  ?    ?   ?   A . n 
A 1 379  ARG 379  379  ?    ?   ?   A . n 
A 1 380  LEU 380  380  ?    ?   ?   A . n 
A 1 381  VAL 381  381  ?    ?   ?   A . n 
A 1 382  GLU 382  382  ?    ?   ?   A . n 
A 1 383  ALA 383  383  ?    ?   ?   A . n 
A 1 384  ILE 384  384  ?    ?   ?   A . n 
A 1 385  SER 385  385  ?    ?   ?   A . n 
A 1 386  ARG 386  386  ?    ?   ?   A . n 
A 1 387  ASP 387  387  ?    ?   ?   A . n 
A 1 388  LEU 388  388  ?    ?   ?   A . n 
A 1 389  SER 389  389  ?    ?   ?   A . n 
A 1 390  SER 390  390  ?    ?   ?   A . n 
A 1 391  GLN 391  391  ?    ?   ?   A . n 
A 1 392  LEU 392  392  ?    ?   ?   A . n 
A 1 393  LEU 393  393  ?    ?   ?   A . n 
A 1 394  LYS 394  394  ?    ?   ?   A . n 
A 1 395  VAL 395  395  ?    ?   ?   A . n 
A 1 396  LEU 396  396  ?    ?   ?   A . n 
A 1 397  GLY 397  397  ?    ?   ?   A . n 
A 1 398  THR 398  398  ?    ?   ?   A . n 
A 1 399  ARG 399  399  ?    ?   ?   A . n 
A 1 400  LYS 400  400  ?    ?   ?   A . n 
A 1 401  LEU 401  401  ?    ?   ?   A . n 
A 1 402  MET 402  402  ?    ?   ?   A . n 
A 1 403  HIS 403  403  ?    ?   ?   A . n 
A 1 404  VAL 404  404  ?    ?   ?   A . n 
A 1 405  ALA 405  405  ?    ?   ?   A . n 
A 1 406  TYR 406  406  ?    ?   ?   A . n 
A 1 407  GLU 407  407  ?    ?   ?   A . n 
A 1 408  GLU 408  408  ?    ?   ?   A . n 
A 1 409  PHE 409  409  ?    ?   ?   A . n 
A 1 410  GLU 410  410  ?    ?   ?   A . n 
A 1 411  LYS 411  411  ?    ?   ?   A . n 
A 1 412  VAL 412  412  ?    ?   ?   A . n 
A 1 413  MET 413  413  ?    ?   ?   A . n 
A 1 414  VAL 414  414  ?    ?   ?   A . n 
A 1 415  ALA 415  415  ?    ?   ?   A . n 
A 1 416  CYS 416  416  ?    ?   ?   A . n 
A 1 417  PHE 417  417  ?    ?   ?   A . n 
A 1 418  GLU 418  418  ?    ?   ?   A . n 
A 1 419  VAL 419  419  ?    ?   ?   A . n 
A 1 420  PHE 420  420  ?    ?   ?   A . n 
A 1 421  GLN 421  421  ?    ?   ?   A . n 
A 1 422  THR 422  422  ?    ?   ?   A . n 
A 1 423  TRP 423  423  ?    ?   ?   A . n 
A 1 424  ASP 424  424  ?    ?   ?   A . n 
A 1 425  ASP 425  425  ?    ?   ?   A . n 
A 1 426  GLU 426  426  ?    ?   ?   A . n 
A 1 427  TYR 427  427  ?    ?   ?   A . n 
A 1 428  GLU 428  428  ?    ?   ?   A . n 
A 1 429  LYS 429  429  ?    ?   ?   A . n 
A 1 430  LEU 430  430  ?    ?   ?   A . n 
A 1 431  GLN 431  431  ?    ?   ?   A . n 
A 1 432  VAL 432  432  ?    ?   ?   A . n 
A 1 433  LEU 433  433  ?    ?   ?   A . n 
A 1 434  LEU 434  434  ?    ?   ?   A . n 
A 1 435  ARG 435  435  ?    ?   ?   A . n 
A 1 436  ASP 436  436  ?    ?   ?   A . n 
A 1 437  ILE 437  437  ?    ?   ?   A . n 
A 1 438  VAL 438  438  ?    ?   ?   A . n 
A 1 439  LYS 439  439  ?    ?   ?   A . n 
A 1 440  ARG 440  440  ?    ?   ?   A . n 
A 1 441  LYS 441  441  ?    ?   ?   A . n 
A 1 442  ARG 442  442  ?    ?   ?   A . n 
A 1 443  GLU 443  443  ?    ?   ?   A . n 
A 1 444  GLU 444  444  ?    ?   ?   A . n 
A 1 445  ASN 445  445  ?    ?   ?   A . n 
A 1 446  LEU 446  446  ?    ?   ?   A . n 
A 1 447  LYS 447  447  ?    ?   ?   A . n 
A 1 448  MET 448  448  ?    ?   ?   A . n 
A 1 449  VAL 449  449  ?    ?   ?   A . n 
A 1 450  TRP 450  450  ?    ?   ?   A . n 
A 1 451  ARG 451  451  ?    ?   ?   A . n 
A 1 452  ILE 452  452  ?    ?   ?   A . n 
A 1 453  ASN 453  453  ?    ?   ?   A . n 
A 1 454  PRO 454  454  ?    ?   ?   A . n 
A 1 455  ALA 455  455  ?    ?   ?   A . n 
A 1 456  HIS 456  456  ?    ?   ?   A . n 
A 1 457  ARG 457  457  ?    ?   ?   A . n 
A 1 458  LYS 458  458  ?    ?   ?   A . n 
A 1 459  LEU 459  459  ?    ?   ?   A . n 
A 1 460  GLN 460  460  ?    ?   ?   A . n 
A 1 461  ALA 461  461  ?    ?   ?   A . n 
A 1 462  ARG 462  462  ?    ?   ?   A . n 
A 1 463  LEU 463  463  ?    ?   ?   A . n 
A 1 464  ASP 464  464  ?    ?   ?   A . n 
A 1 465  GLN 465  465  ?    ?   ?   A . n 
A 1 466  MET 466  466  ?    ?   ?   A . n 
A 1 467  ARG 467  467  ?    ?   ?   A . n 
A 1 468  LYS 468  468  ?    ?   ?   A . n 
A 1 469  PHE 469  469  ?    ?   ?   A . n 
A 1 470  ARG 470  470  ?    ?   ?   A . n 
A 1 471  ARG 471  471  ?    ?   ?   A . n 
A 1 472  GLN 472  472  ?    ?   ?   A . n 
A 1 473  HIS 473  473  ?    ?   ?   A . n 
A 1 474  GLU 474  474  ?    ?   ?   A . n 
A 1 475  GLN 475  475  ?    ?   ?   A . n 
A 1 476  LEU 476  476  ?    ?   ?   A . n 
A 1 477  ARG 477  477  ?    ?   ?   A . n 
A 1 478  ALA 478  478  ?    ?   ?   A . n 
A 1 479  VAL 479  479  ?    ?   ?   A . n 
A 1 480  ILE 480  480  ?    ?   ?   A . n 
A 1 481  VAL 481  481  ?    ?   ?   A . n 
A 1 482  ARG 482  482  ?    ?   ?   A . n 
A 1 483  VAL 483  483  ?    ?   ?   A . n 
A 1 484  LEU 484  484  ?    ?   ?   A . n 
A 1 485  ARG 485  485  ?    ?   ?   A . n 
A 1 486  PRO 486  486  ?    ?   ?   A . n 
A 1 487  GLN 487  487  ?    ?   ?   A . n 
A 1 488  VAL 488  488  ?    ?   ?   A . n 
A 1 489  THR 489  489  ?    ?   ?   A . n 
A 1 490  ALA 490  490  ?    ?   ?   A . n 
A 1 491  VAL 491  491  ?    ?   ?   A . n 
A 1 492  ALA 492  492  ?    ?   ?   A . n 
A 1 493  GLN 493  493  ?    ?   ?   A . n 
A 1 494  GLN 494  494  ?    ?   ?   A . n 
A 1 495  ASN 495  495  ?    ?   ?   A . n 
A 1 496  GLN 496  496  ?    ?   ?   A . n 
A 1 497  GLY 497  497  ?    ?   ?   A . n 
A 1 498  GLU 498  498  ?    ?   ?   A . n 
A 1 499  VAL 499  499  ?    ?   ?   A . n 
A 1 500  PRO 500  500  ?    ?   ?   A . n 
A 1 501  GLU 501  501  ?    ?   ?   A . n 
A 1 502  PRO 502  502  ?    ?   ?   A . n 
A 1 503  GLN 503  503  ?    ?   ?   A . n 
A 1 504  ASP 504  504  ?    ?   ?   A . n 
A 1 505  MET 505  505  ?    ?   ?   A . n 
A 1 506  LYS 506  506  ?    ?   ?   A . n 
A 1 507  VAL 507  507  ?    ?   ?   A . n 
A 1 508  ALA 508  508  ?    ?   ?   A . n 
A 1 509  GLU 509  509  ?    ?   ?   A . n 
A 1 510  VAL 510  510  ?    ?   ?   A . n 
A 1 511  LEU 511  511  ?    ?   ?   A . n 
A 1 512  PHE 512  512  ?    ?   ?   A . n 
A 1 513  ASP 513  513  ?    ?   ?   A . n 
A 1 514  ALA 514  514  ?    ?   ?   A . n 
A 1 515  ALA 515  515  ?    ?   ?   A . n 
A 1 516  ASP 516  516  ?    ?   ?   A . n 
A 1 517  ALA 517  517  ?    ?   ?   A . n 
A 1 518  ASN 518  518  ?    ?   ?   A . n 
A 1 519  ALA 519  519  ?    ?   ?   A . n 
A 1 520  ILE 520  520  ?    ?   ?   A . n 
A 1 521  GLU 521  521  ?    ?   ?   A . n 
A 1 522  GLU 522  522  ?    ?   ?   A . n 
A 1 523  VAL 523  523  ?    ?   ?   A . n 
A 1 524  ASN 524  524  ?    ?   ?   A . n 
A 1 525  LEU 525  525  ?    ?   ?   A . n 
A 1 526  ALA 526  526  ?    ?   ?   A . n 
A 1 527  TYR 527  527  ?    ?   ?   A . n 
A 1 528  GLU 528  528  ?    ?   ?   A . n 
A 1 529  ASN 529  529  ?    ?   ?   A . n 
A 1 530  VAL 530  530  ?    ?   ?   A . n 
A 1 531  LYS 531  531  ?    ?   ?   A . n 
A 1 532  GLU 532  532  ?    ?   ?   A . n 
A 1 533  VAL 533  533  ?    ?   ?   A . n 
A 1 534  ASP 534  534  ?    ?   ?   A . n 
A 1 535  GLY 535  535  ?    ?   ?   A . n 
A 1 536  LEU 536  536  ?    ?   ?   A . n 
A 1 537  ASP 537  537  ?    ?   ?   A . n 
A 1 538  VAL 538  538  ?    ?   ?   A . n 
A 1 539  SER 539  539  ?    ?   ?   A . n 
A 1 540  LYS 540  540  ?    ?   ?   A . n 
A 1 541  GLU 541  541  ?    ?   ?   A . n 
A 1 542  GLY 542  542  ?    ?   ?   A . n 
A 1 543  THR 543  543  ?    ?   ?   A . n 
A 1 544  GLU 544  544  ?    ?   ?   A . n 
A 1 545  ALA 545  545  ?    ?   ?   A . n 
A 1 546  TRP 546  546  ?    ?   ?   A . n 
A 1 547  GLU 547  547  ?    ?   ?   A . n 
A 1 548  ALA 548  548  ?    ?   ?   A . n 
A 1 549  ALA 549  549  ?    ?   ?   A . n 
A 1 550  MET 550  550  ?    ?   ?   A . n 
A 1 551  LYS 551  551  ?    ?   ?   A . n 
A 1 552  ARG 552  552  ?    ?   ?   A . n 
A 1 553  TYR 553  553  ?    ?   ?   A . n 
A 1 554  ASP 554  554  ?    ?   ?   A . n 
A 1 555  GLU 555  555  ?    ?   ?   A . n 
A 1 556  ARG 556  556  ?    ?   ?   A . n 
A 1 557  ILE 557  557  ?    ?   ?   A . n 
A 1 558  ASP 558  558  ?    ?   ?   A . n 
A 1 559  ARG 559  559  ?    ?   ?   A . n 
A 1 560  VAL 560  560  ?    ?   ?   A . n 
A 1 561  GLU 561  561  ?    ?   ?   A . n 
A 1 562  THR 562  562  ?    ?   ?   A . n 
A 1 563  ARG 563  563  ?    ?   ?   A . n 
A 1 564  ILE 564  564  ?    ?   ?   A . n 
A 1 565  THR 565  565  ?    ?   ?   A . n 
A 1 566  ALA 566  566  ?    ?   ?   A . n 
A 1 567  ARG 567  567  ?    ?   ?   A . n 
A 1 568  LEU 568  568  ?    ?   ?   A . n 
A 1 569  ARG 569  569  ?    ?   ?   A . n 
A 1 570  ASP 570  570  ?    ?   ?   A . n 
A 1 571  GLN 571  571  ?    ?   ?   A . n 
A 1 572  LEU 572  572  ?    ?   ?   A . n 
A 1 573  GLY 573  573  ?    ?   ?   A . n 
A 1 574  THR 574  574  ?    ?   ?   A . n 
A 1 575  ALA 575  575  ?    ?   ?   A . n 
A 1 576  LYS 576  576  ?    ?   ?   A . n 
A 1 577  ASN 577  577  ?    ?   ?   A . n 
A 1 578  ALA 578  578  ?    ?   ?   A . n 
A 1 579  ASN 579  579  ?    ?   ?   A . n 
A 1 580  GLU 580  580  ?    ?   ?   A . n 
A 1 581  MET 581  581  ?    ?   ?   A . n 
A 1 582  PHE 582  582  ?    ?   ?   A . n 
A 1 583  ARG 583  583  ?    ?   ?   A . n 
A 1 584  ILE 584  584  ?    ?   ?   A . n 
A 1 585  PHE 585  585  ?    ?   ?   A . n 
A 1 586  SER 586  586  ?    ?   ?   A . n 
A 1 587  ARG 587  587  ?    ?   ?   A . n 
A 1 588  PHE 588  588  ?    ?   ?   A . n 
A 1 589  ASN 589  589  ?    ?   ?   A . n 
A 1 590  ALA 590  590  ?    ?   ?   A . n 
A 1 591  LEU 591  591  ?    ?   ?   A . n 
A 1 592  PHE 592  592  ?    ?   ?   A . n 
A 1 593  VAL 593  593  ?    ?   ?   A . n 
A 1 594  ARG 594  594  ?    ?   ?   A . n 
A 1 595  PRO 595  595  ?    ?   ?   A . n 
A 1 596  HIS 596  596  ?    ?   ?   A . n 
A 1 597  ILE 597  597  ?    ?   ?   A . n 
A 1 598  ARG 598  598  ?    ?   ?   A . n 
A 1 599  GLY 599  599  ?    ?   ?   A . n 
A 1 600  ALA 600  600  ?    ?   ?   A . n 
A 1 601  ILE 601  601  ?    ?   ?   A . n 
A 1 602  ARG 602  602  ?    ?   ?   A . n 
A 1 603  GLU 603  603  ?    ?   ?   A . n 
A 1 604  TYR 604  604  ?    ?   ?   A . n 
A 1 605  GLN 605  605  ?    ?   ?   A . n 
A 1 606  THR 606  606  ?    ?   ?   A . n 
A 1 607  GLN 607  607  ?    ?   ?   A . n 
A 1 608  LEU 608  608  ?    ?   ?   A . n 
A 1 609  ILE 609  609  ?    ?   ?   A . n 
A 1 610  GLN 610  610  ?    ?   ?   A . n 
A 1 611  ARG 611  611  ?    ?   ?   A . n 
A 1 612  VAL 612  612  ?    ?   ?   A . n 
A 1 613  LYS 613  613  ?    ?   ?   A . n 
A 1 614  ASP 614  614  ?    ?   ?   A . n 
A 1 615  ASP 615  615  ?    ?   ?   A . n 
A 1 616  ILE 616  616  ?    ?   ?   A . n 
A 1 617  GLU 617  617  ?    ?   ?   A . n 
A 1 618  SER 618  618  ?    ?   ?   A . n 
A 1 619  LEU 619  619  ?    ?   ?   A . n 
A 1 620  HIS 620  620  ?    ?   ?   A . n 
A 1 621  ASP 621  621  ?    ?   ?   A . n 
A 1 622  LYS 622  622  ?    ?   ?   A . n 
A 1 623  PHE 623  623  ?    ?   ?   A . n 
A 1 624  LYS 624  624  ?    ?   ?   A . n 
A 1 625  VAL 625  625  ?    ?   ?   A . n 
A 1 626  GLN 626  626  ?    ?   ?   A . n 
A 1 627  TYR 627  627  ?    ?   ?   A . n 
A 1 628  PRO 628  628  ?    ?   ?   A . n 
A 1 629  GLN 629  629  ?    ?   ?   A . n 
A 1 630  SER 630  630  ?    ?   ?   A . n 
A 1 631  GLN 631  631  ?    ?   ?   A . n 
A 1 632  ALA 632  632  ?    ?   ?   A . n 
A 1 633  CYS 633  633  ?    ?   ?   A . n 
A 1 634  LYS 634  634  ?    ?   ?   A . n 
A 1 635  MET 635  635  ?    ?   ?   A . n 
A 1 636  SER 636  636  ?    ?   ?   A . n 
A 1 637  HIS 637  637  ?    ?   ?   A . n 
A 1 638  VAL 638  638  ?    ?   ?   A . n 
A 1 639  ARG 639  639  ?    ?   ?   A . n 
A 1 640  ASP 640  640  ?    ?   ?   A . n 
A 1 641  LEU 641  641  ?    ?   ?   A . n 
A 1 642  PRO 642  642  ?    ?   ?   A . n 
A 1 643  PRO 643  643  ?    ?   ?   A . n 
A 1 644  VAL 644  644  ?    ?   ?   A . n 
A 1 645  SER 645  645  ?    ?   ?   A . n 
A 1 646  GLY 646  646  ?    ?   ?   A . n 
A 1 647  SER 647  647  ?    ?   ?   A . n 
A 1 648  ILE 648  648  ?    ?   ?   A . n 
A 1 649  ILE 649  649  ?    ?   ?   A . n 
A 1 650  TRP 650  650  ?    ?   ?   A . n 
A 1 651  ALA 651  651  ?    ?   ?   A . n 
A 1 652  LYS 652  652  ?    ?   ?   A . n 
A 1 653  GLN 653  653  ?    ?   ?   A . n 
A 1 654  ILE 654  654  ?    ?   ?   A . n 
A 1 655  ASP 655  655  ?    ?   ?   A . n 
A 1 656  ARG 656  656  ?    ?   ?   A . n 
A 1 657  GLN 657  657  ?    ?   ?   A . n 
A 1 658  LEU 658  658  ?    ?   ?   A . n 
A 1 659  THR 659  659  ?    ?   ?   A . n 
A 1 660  ALA 660  660  ?    ?   ?   A . n 
A 1 661  TYR 661  661  ?    ?   ?   A . n 
A 1 662  MET 662  662  ?    ?   ?   A . n 
A 1 663  LYS 663  663  ?    ?   ?   A . n 
A 1 664  ARG 664  664  ?    ?   ?   A . n 
A 1 665  VAL 665  665  ?    ?   ?   A . n 
A 1 666  GLU 666  666  ?    ?   ?   A . n 
A 1 667  ASP 667  667  ?    ?   ?   A . n 
A 1 668  VAL 668  668  ?    ?   ?   A . n 
A 1 669  LEU 669  669  ?    ?   ?   A . n 
A 1 670  GLY 670  670  ?    ?   ?   A . n 
A 1 671  LYS 671  671  ?    ?   ?   A . n 
A 1 672  GLY 672  672  ?    ?   ?   A . n 
A 1 673  TRP 673  673  ?    ?   ?   A . n 
A 1 674  GLU 674  674  ?    ?   ?   A . n 
A 1 675  ASN 675  675  ?    ?   ?   A . n 
A 1 676  HIS 676  676  ?    ?   ?   A . n 
A 1 677  VAL 677  677  ?    ?   ?   A . n 
A 1 678  GLU 678  678  ?    ?   ?   A . n 
A 1 679  GLY 679  679  ?    ?   ?   A . n 
A 1 680  GLN 680  680  ?    ?   ?   A . n 
A 1 681  LYS 681  681  ?    ?   ?   A . n 
A 1 682  LEU 682  682  ?    ?   ?   A . n 
A 1 683  LYS 683  683  ?    ?   ?   A . n 
A 1 684  GLN 684  684  ?    ?   ?   A . n 
A 1 685  ASP 685  685  ?    ?   ?   A . n 
A 1 686  GLY 686  686  ?    ?   ?   A . n 
A 1 687  ASP 687  687  ?    ?   ?   A . n 
A 1 688  SER 688  688  ?    ?   ?   A . n 
A 1 689  PHE 689  689  ?    ?   ?   A . n 
A 1 690  ARG 690  690  ?    ?   ?   A . n 
A 1 691  MET 691  691  ?    ?   ?   A . n 
A 1 692  LYS 692  692  ?    ?   ?   A . n 
A 1 693  LEU 693  693  ?    ?   ?   A . n 
A 1 694  ASN 694  694  ?    ?   ?   A . n 
A 1 695  THR 695  695  ?    ?   ?   A . n 
A 1 696  GLN 696  696  ?    ?   ?   A . n 
A 1 697  GLU 697  697  ?    ?   ?   A . n 
A 1 698  ILE 698  698  ?    ?   ?   A . n 
A 1 699  PHE 699  699  ?    ?   ?   A . n 
A 1 700  ASP 700  700  ?    ?   ?   A . n 
A 1 701  ASP 701  701  ?    ?   ?   A . n 
A 1 702  TRP 702  702  ?    ?   ?   A . n 
A 1 703  ALA 703  703  ?    ?   ?   A . n 
A 1 704  ARG 704  704  ?    ?   ?   A . n 
A 1 705  LYS 705  705  ?    ?   ?   A . n 
A 1 706  VAL 706  706  ?    ?   ?   A . n 
A 1 707  GLN 707  707  ?    ?   ?   A . n 
A 1 708  GLN 708  708  ?    ?   ?   A . n 
A 1 709  ARG 709  709  ?    ?   ?   A . n 
A 1 710  ASN 710  710  ?    ?   ?   A . n 
A 1 711  LEU 711  711  ?    ?   ?   A . n 
A 1 712  GLY 712  712  ?    ?   ?   A . n 
A 1 713  VAL 713  713  ?    ?   ?   A . n 
A 1 714  SER 714  714  ?    ?   ?   A . n 
A 1 715  GLY 715  715  ?    ?   ?   A . n 
A 1 716  ARG 716  716  ?    ?   ?   A . n 
A 1 717  ILE 717  717  ?    ?   ?   A . n 
A 1 718  PHE 718  718  ?    ?   ?   A . n 
A 1 719  THR 719  719  ?    ?   ?   A . n 
A 1 720  ILE 720  720  ?    ?   ?   A . n 
A 1 721  GLU 721  721  ?    ?   ?   A . n 
A 1 722  SER 722  722  ?    ?   ?   A . n 
A 1 723  THR 723  723  ?    ?   ?   A . n 
A 1 724  ARG 724  724  ?    ?   ?   A . n 
A 1 725  VAL 725  725  ?    ?   ?   A . n 
A 1 726  ARG 726  726  ?    ?   ?   A . n 
A 1 727  GLY 727  727  ?    ?   ?   A . n 
A 1 728  ARG 728  728  ?    ?   ?   A . n 
A 1 729  THR 729  729  ?    ?   ?   A . n 
A 1 730  GLY 730  730  ?    ?   ?   A . n 
A 1 731  ASN 731  731  ?    ?   ?   A . n 
A 1 732  VAL 732  732  ?    ?   ?   A . n 
A 1 733  LEU 733  733  ?    ?   ?   A . n 
A 1 734  LYS 734  734  ?    ?   ?   A . n 
A 1 735  LEU 735  735  ?    ?   ?   A . n 
A 1 736  LYS 736  736  ?    ?   ?   A . n 
A 1 737  VAL 737  737  ?    ?   ?   A . n 
A 1 738  ASN 738  738  ?    ?   ?   A . n 
A 1 739  PHE 739  739  ?    ?   ?   A . n 
A 1 740  LEU 740  740  ?    ?   ?   A . n 
A 1 741  PRO 741  741  ?    ?   ?   A . n 
A 1 742  GLU 742  742  ?    ?   ?   A . n 
A 1 743  ILE 743  743  ?    ?   ?   A . n 
A 1 744  ILE 744  744  ?    ?   ?   A . n 
A 1 745  THR 745  745  ?    ?   ?   A . n 
A 1 746  LEU 746  746  ?    ?   ?   A . n 
A 1 747  SER 747  747  ?    ?   ?   A . n 
A 1 748  LYS 748  748  ?    ?   ?   A . n 
A 1 749  GLU 749  749  ?    ?   ?   A . n 
A 1 750  VAL 750  750  ?    ?   ?   A . n 
A 1 751  ARG 751  751  ?    ?   ?   A . n 
A 1 752  ASN 752  752  ?    ?   ?   A . n 
A 1 753  LEU 753  753  ?    ?   ?   A . n 
A 1 754  LYS 754  754  ?    ?   ?   A . n 
A 1 755  TRP 755  755  ?    ?   ?   A . n 
A 1 756  LEU 756  756  ?    ?   ?   A . n 
A 1 757  GLY 757  757  ?    ?   ?   A . n 
A 1 758  PHE 758  758  ?    ?   ?   A . n 
A 1 759  ARG 759  759  ?    ?   ?   A . n 
A 1 760  VAL 760  760  ?    ?   ?   A . n 
A 1 761  PRO 761  761  ?    ?   ?   A . n 
A 1 762  LEU 762  762  ?    ?   ?   A . n 
A 1 763  ALA 763  763  ?    ?   ?   A . n 
A 1 764  ILE 764  764  ?    ?   ?   A . n 
A 1 765  VAL 765  765  ?    ?   ?   A . n 
A 1 766  ASN 766  766  ?    ?   ?   A . n 
A 1 767  LYS 767  767  ?    ?   ?   A . n 
A 1 768  ALA 768  768  ?    ?   ?   A . n 
A 1 769  HIS 769  769  ?    ?   ?   A . n 
A 1 770  GLN 770  770  ?    ?   ?   A . n 
A 1 771  ALA 771  771  ?    ?   ?   A . n 
A 1 772  ASN 772  772  ?    ?   ?   A . n 
A 1 773  GLN 773  773  ?    ?   ?   A . n 
A 1 774  LEU 774  774  ?    ?   ?   A . n 
A 1 775  TYR 775  775  ?    ?   ?   A . n 
A 1 776  PRO 776  776  ?    ?   ?   A . n 
A 1 777  PHE 777  777  ?    ?   ?   A . n 
A 1 778  ALA 778  778  ?    ?   ?   A . n 
A 1 779  ILE 779  779  ?    ?   ?   A . n 
A 1 780  SER 780  780  ?    ?   ?   A . n 
A 1 781  LEU 781  781  ?    ?   ?   A . n 
A 1 782  ILE 782  782  ?    ?   ?   A . n 
A 1 783  GLU 783  783  ?    ?   ?   A . n 
A 1 784  SER 784  784  ?    ?   ?   A . n 
A 1 785  VAL 785  785  ?    ?   ?   A . n 
A 1 786  ARG 786  786  ?    ?   ?   A . n 
A 1 787  THR 787  787  ?    ?   ?   A . n 
A 1 788  TYR 788  788  ?    ?   ?   A . n 
A 1 789  GLU 789  789  ?    ?   ?   A . n 
A 1 790  ARG 790  790  ?    ?   ?   A . n 
A 1 791  THR 791  791  ?    ?   ?   A . n 
A 1 792  CYS 792  792  ?    ?   ?   A . n 
A 1 793  GLU 793  793  ?    ?   ?   A . n 
A 1 794  LYS 794  794  ?    ?   ?   A . n 
A 1 795  VAL 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLU 797  797  ?    ?   ?   A . n 
A 1 798  ARG 798  798  ?    ?   ?   A . n 
A 1 799  ASN 799  799  ?    ?   ?   A . n 
A 1 800  THR 800  800  ?    ?   ?   A . n 
A 1 801  ILE 801  801  ?    ?   ?   A . n 
A 1 802  SER 802  802  ?    ?   ?   A . n 
A 1 803  LEU 803  803  ?    ?   ?   A . n 
A 1 804  LEU 804  804  ?    ?   ?   A . n 
A 1 805  VAL 805  805  ?    ?   ?   A . n 
A 1 806  ALA 806  806  ?    ?   ?   A . n 
A 1 807  GLY 807  807  ?    ?   ?   A . n 
A 1 808  LEU 808  808  ?    ?   ?   A . n 
A 1 809  LYS 809  809  ?    ?   ?   A . n 
A 1 810  LYS 810  810  ?    ?   ?   A . n 
A 1 811  GLU 811  811  ?    ?   ?   A . n 
A 1 812  VAL 812  812  ?    ?   ?   A . n 
A 1 813  GLN 813  813  ?    ?   ?   A . n 
A 1 814  ALA 814  814  ?    ?   ?   A . n 
A 1 815  LEU 815  815  ?    ?   ?   A . n 
A 1 816  ILE 816  816  ?    ?   ?   A . n 
A 1 817  ALA 817  817  ?    ?   ?   A . n 
A 1 818  GLU 818  818  ?    ?   ?   A . n 
A 1 819  GLY 819  819  ?    ?   ?   A . n 
A 1 820  ILE 820  820  ?    ?   ?   A . n 
A 1 821  ALA 821  821  ?    ?   ?   A . n 
A 1 822  LEU 822  822  ?    ?   ?   A . n 
A 1 823  VAL 823  823  ?    ?   ?   A . n 
A 1 824  TRP 824  824  ?    ?   ?   A . n 
A 1 825  GLU 825  825  ?    ?   ?   A . n 
A 1 826  SER 826  826  ?    ?   ?   A . n 
A 1 827  TYR 827  827  ?    ?   ?   A . n 
A 1 828  LYS 828  828  ?    ?   ?   A . n 
A 1 829  LEU 829  829  ?    ?   ?   A . n 
A 1 830  ASP 830  830  ?    ?   ?   A . n 
A 1 831  PRO 831  831  ?    ?   ?   A . n 
A 1 832  TYR 832  832  ?    ?   ?   A . n 
A 1 833  VAL 833  833  ?    ?   ?   A . n 
A 1 834  GLN 834  834  ?    ?   ?   A . n 
A 1 835  ARG 835  835  ?    ?   ?   A . n 
A 1 836  LEU 836  836  ?    ?   ?   A . n 
A 1 837  ALA 837  837  ?    ?   ?   A . n 
A 1 838  GLU 838  838  ?    ?   ?   A . n 
A 1 839  THR 839  839  ?    ?   ?   A . n 
A 1 840  VAL 840  840  ?    ?   ?   A . n 
A 1 841  PHE 841  841  ?    ?   ?   A . n 
A 1 842  ASN 842  842  ?    ?   ?   A . n 
A 1 843  PHE 843  843  ?    ?   ?   A . n 
A 1 844  GLN 844  844  ?    ?   ?   A . n 
A 1 845  GLU 845  845  ?    ?   ?   A . n 
A 1 846  LYS 846  846  ?    ?   ?   A . n 
A 1 847  VAL 847  847  ?    ?   ?   A . n 
A 1 848  ASP 848  848  ?    ?   ?   A . n 
A 1 849  ASP 849  849  ?    ?   ?   A . n 
A 1 850  LEU 850  850  ?    ?   ?   A . n 
A 1 851  LEU 851  851  ?    ?   ?   A . n 
A 1 852  ILE 852  852  ?    ?   ?   A . n 
A 1 853  ILE 853  853  ?    ?   ?   A . n 
A 1 854  GLU 854  854  ?    ?   ?   A . n 
A 1 855  GLU 855  855  ?    ?   ?   A . n 
A 1 856  LYS 856  856  ?    ?   ?   A . n 
A 1 857  ILE 857  857  ?    ?   ?   A . n 
A 1 858  ASP 858  858  ?    ?   ?   A . n 
A 1 859  LEU 859  859  ?    ?   ?   A . n 
A 1 860  GLU 860  860  ?    ?   ?   A . n 
A 1 861  VAL 861  861  ?    ?   ?   A . n 
A 1 862  ARG 862  862  ?    ?   ?   A . n 
A 1 863  SER 863  863  ?    ?   ?   A . n 
A 1 864  LEU 864  864  ?    ?   ?   A . n 
A 1 865  GLU 865  865  ?    ?   ?   A . n 
A 1 866  THR 866  866  ?    ?   ?   A . n 
A 1 867  CYS 867  867  ?    ?   ?   A . n 
A 1 868  MET 868  868  ?    ?   ?   A . n 
A 1 869  TYR 869  869  ?    ?   ?   A . n 
A 1 870  ASP 870  870  ?    ?   ?   A . n 
A 1 871  HIS 871  871  ?    ?   ?   A . n 
A 1 872  LYS 872  872  ?    ?   ?   A . n 
A 1 873  THR 873  873  ?    ?   ?   A . n 
A 1 874  PHE 874  874  ?    ?   ?   A . n 
A 1 875  SER 875  875  ?    ?   ?   A . n 
A 1 876  GLU 876  876  ?    ?   ?   A . n 
A 1 877  ILE 877  877  ?    ?   ?   A . n 
A 1 878  LEU 878  878  ?    ?   ?   A . n 
A 1 879  ASN 879  879  ?    ?   ?   A . n 
A 1 880  ARG 880  880  ?    ?   ?   A . n 
A 1 881  VAL 881  881  ?    ?   ?   A . n 
A 1 882  GLN 882  882  ?    ?   ?   A . n 
A 1 883  LYS 883  883  ?    ?   ?   A . n 
A 1 884  ALA 884  884  ?    ?   ?   A . n 
A 1 885  VAL 885  885  ?    ?   ?   A . n 
A 1 886  ASP 886  886  ?    ?   ?   A . n 
A 1 887  ASP 887  887  ?    ?   ?   A . n 
A 1 888  LEU 888  888  ?    ?   ?   A . n 
A 1 889  ASN 889  889  ?    ?   ?   A . n 
A 1 890  LEU 890  890  ?    ?   ?   A . n 
A 1 891  HIS 891  891  ?    ?   ?   A . n 
A 1 892  SER 892  892  ?    ?   ?   A . n 
A 1 893  TYR 893  893  ?    ?   ?   A . n 
A 1 894  SER 894  894  ?    ?   ?   A . n 
A 1 895  ASN 895  895  ?    ?   ?   A . n 
A 1 896  LEU 896  896  ?    ?   ?   A . n 
A 1 897  PRO 897  897  ?    ?   ?   A . n 
A 1 898  ILE 898  898  ?    ?   ?   A . n 
A 1 899  TRP 899  899  ?    ?   ?   A . n 
A 1 900  VAL 900  900  ?    ?   ?   A . n 
A 1 901  ASN 901  901  ?    ?   ?   A . n 
A 1 902  LYS 902  902  ?    ?   ?   A . n 
A 1 903  LEU 903  903  ?    ?   ?   A . n 
A 1 904  ASP 904  904  ?    ?   ?   A . n 
A 1 905  MET 905  905  ?    ?   ?   A . n 
A 1 906  GLU 906  906  ?    ?   ?   A . n 
A 1 907  ILE 907  907  ?    ?   ?   A . n 
A 1 908  GLU 908  908  ?    ?   ?   A . n 
A 1 909  ARG 909  909  ?    ?   ?   A . n 
A 1 910  ILE 910  910  ?    ?   ?   A . n 
A 1 911  LEU 911  911  ?    ?   ?   A . n 
A 1 912  GLY 912  912  ?    ?   ?   A . n 
A 1 913  VAL 913  913  ?    ?   ?   A . n 
A 1 914  ARG 914  914  ?    ?   ?   A . n 
A 1 915  LEU 915  915  ?    ?   ?   A . n 
A 1 916  GLN 916  916  ?    ?   ?   A . n 
A 1 917  ALA 917  917  ?    ?   ?   A . n 
A 1 918  GLY 918  918  ?    ?   ?   A . n 
A 1 919  LEU 919  919  ?    ?   ?   A . n 
A 1 920  ARG 920  920  ?    ?   ?   A . n 
A 1 921  ALA 921  921  ?    ?   ?   A . n 
A 1 922  TRP 922  922  ?    ?   ?   A . n 
A 1 923  THR 923  923  ?    ?   ?   A . n 
A 1 924  GLN 924  924  ?    ?   ?   A . n 
A 1 925  VAL 925  925  ?    ?   ?   A . n 
A 1 926  LEU 926  926  ?    ?   ?   A . n 
A 1 927  LEU 927  927  ?    ?   ?   A . n 
A 1 928  GLY 928  928  ?    ?   ?   A . n 
A 1 929  GLN 929  929  ?    ?   ?   A . n 
A 1 930  ALA 930  930  ?    ?   ?   A . n 
A 1 931  GLU 931  931  ?    ?   ?   A . n 
A 1 932  ASP 932  932  ?    ?   ?   A . n 
A 1 933  LYS 933  933  ?    ?   ?   A . n 
A 1 934  ALA 934  934  ?    ?   ?   A . n 
A 1 935  GLU 935  935  ?    ?   ?   A . n 
A 1 936  VAL 936  936  ?    ?   ?   A . n 
A 1 937  ASP 937  937  ?    ?   ?   A . n 
A 1 938  MET 938  938  ?    ?   ?   A . n 
A 1 939  ASP 939  939  ?    ?   ?   A . n 
A 1 940  THR 940  940  ?    ?   ?   A . n 
A 1 941  ASP 941  941  ?    ?   ?   A . n 
A 1 942  ALA 942  942  ?    ?   ?   A . n 
A 1 943  PRO 943  943  ?    ?   ?   A . n 
A 1 944  GLN 944  944  ?    ?   ?   A . n 
A 1 945  VAL 945  945  ?    ?   ?   A . n 
A 1 946  SER 946  946  ?    ?   ?   A . n 
A 1 947  HIS 947  947  ?    ?   ?   A . n 
A 1 948  LYS 948  948  ?    ?   ?   A . n 
A 1 949  PRO 949  949  ?    ?   ?   A . n 
A 1 950  GLY 950  950  ?    ?   ?   A . n 
A 1 951  GLY 951  951  ?    ?   ?   A . n 
A 1 952  GLU 952  952  ?    ?   ?   A . n 
A 1 953  PRO 953  953  ?    ?   ?   A . n 
A 1 954  LYS 954  954  ?    ?   ?   A . n 
A 1 955  ILE 955  955  ?    ?   ?   A . n 
A 1 956  LYS 956  956  ?    ?   ?   A . n 
A 1 957  ASN 957  957  ?    ?   ?   A . n 
A 1 958  VAL 958  958  ?    ?   ?   A . n 
A 1 959  VAL 959  959  ?    ?   ?   A . n 
A 1 960  HIS 960  960  ?    ?   ?   A . n 
A 1 961  GLU 961  961  ?    ?   ?   A . n 
A 1 962  LEU 962  962  ?    ?   ?   A . n 
A 1 963  ARG 963  963  ?    ?   ?   A . n 
A 1 964  ILE 964  964  ?    ?   ?   A . n 
A 1 965  THR 965  965  ?    ?   ?   A . n 
A 1 966  ASN 966  966  ?    ?   ?   A . n 
A 1 967  GLN 967  967  ?    ?   ?   A . n 
A 1 968  VAL 968  968  ?    ?   ?   A . n 
A 1 969  ILE 969  969  ?    ?   ?   A . n 
A 1 970  TYR 970  970  ?    ?   ?   A . n 
A 1 971  LEU 971  971  ?    ?   ?   A . n 
A 1 972  ASN 972  972  ?    ?   ?   A . n 
A 1 973  PRO 973  973  ?    ?   ?   A . n 
A 1 974  PRO 974  974  ?    ?   ?   A . n 
A 1 975  ILE 975  975  ?    ?   ?   A . n 
A 1 976  GLU 976  976  ?    ?   ?   A . n 
A 1 977  GLU 977  977  ?    ?   ?   A . n 
A 1 978  CYS 978  978  ?    ?   ?   A . n 
A 1 979  ARG 979  979  ?    ?   ?   A . n 
A 1 980  TYR 980  980  ?    ?   ?   A . n 
A 1 981  LYS 981  981  ?    ?   ?   A . n 
A 1 982  LEU 982  982  ?    ?   ?   A . n 
A 1 983  TYR 983  983  ?    ?   ?   A . n 
A 1 984  GLN 984  984  ?    ?   ?   A . n 
A 1 985  GLU 985  985  ?    ?   ?   A . n 
A 1 986  MET 986  986  ?    ?   ?   A . n 
A 1 987  PHE 987  987  ?    ?   ?   A . n 
A 1 988  ALA 988  988  ?    ?   ?   A . n 
A 1 989  TRP 989  989  ?    ?   ?   A . n 
A 1 990  LYS 990  990  ?    ?   ?   A . n 
A 1 991  MET 991  991  ?    ?   ?   A . n 
A 1 992  VAL 992  992  ?    ?   ?   A . n 
A 1 993  VAL 993  993  ?    ?   ?   A . n 
A 1 994  LEU 994  994  ?    ?   ?   A . n 
A 1 995  SER 995  995  ?    ?   ?   A . n 
A 1 996  LEU 996  996  ?    ?   ?   A . n 
A 1 997  PRO 997  997  ?    ?   ?   A . n 
A 1 998  ARG 998  998  ?    ?   ?   A . n 
A 1 999  ILE 999  999  ?    ?   ?   A . n 
A 1 1000 GLN 1000 1000 ?    ?   ?   A . n 
A 1 1001 SER 1001 1001 ?    ?   ?   A . n 
A 1 1002 GLN 1002 1002 ?    ?   ?   A . n 
A 1 1003 ARG 1003 1003 ?    ?   ?   A . n 
A 1 1004 TYR 1004 1004 ?    ?   ?   A . n 
A 1 1005 GLN 1005 1005 ?    ?   ?   A . n 
A 1 1006 VAL 1006 1006 ?    ?   ?   A . n 
A 1 1007 GLY 1007 1007 ?    ?   ?   A . n 
A 1 1008 VAL 1008 1008 ?    ?   ?   A . n 
A 1 1009 HIS 1009 1009 ?    ?   ?   A . n 
A 1 1010 TYR 1010 1010 ?    ?   ?   A . n 
A 1 1011 GLU 1011 1011 ?    ?   ?   A . n 
A 1 1012 LEU 1012 1012 ?    ?   ?   A . n 
A 1 1013 THR 1013 1013 ?    ?   ?   A . n 
A 1 1014 GLU 1014 1014 ?    ?   ?   A . n 
A 1 1015 GLU 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLU 1016 1016 ?    ?   ?   A . n 
A 1 1017 LYS 1017 1017 ?    ?   ?   A . n 
A 1 1018 PHE 1018 1018 ?    ?   ?   A . n 
A 1 1019 TYR 1019 1019 ?    ?   ?   A . n 
A 1 1020 ARG 1020 1020 ?    ?   ?   A . n 
A 1 1021 ASN 1021 1021 ?    ?   ?   A . n 
A 1 1022 ALA 1022 1022 ?    ?   ?   A . n 
A 1 1023 LEU 1023 1023 ?    ?   ?   A . n 
A 1 1024 THR 1024 1024 ?    ?   ?   A . n 
A 1 1025 ARG 1025 1025 ?    ?   ?   A . n 
A 1 1026 MET 1026 1026 ?    ?   ?   A . n 
A 1 1027 PRO 1027 1027 ?    ?   ?   A . n 
A 1 1028 ASP 1028 1028 ?    ?   ?   A . n 
A 1 1029 GLY 1029 1029 ?    ?   ?   A . n 
A 1 1030 PRO 1030 1030 ?    ?   ?   A . n 
A 1 1031 VAL 1031 1031 ?    ?   ?   A . n 
A 1 1032 ALA 1032 1032 ?    ?   ?   A . n 
A 1 1033 LEU 1033 1033 ?    ?   ?   A . n 
A 1 1034 GLU 1034 1034 ?    ?   ?   A . n 
A 1 1035 GLU 1035 1035 ?    ?   ?   A . n 
A 1 1036 SER 1036 1036 ?    ?   ?   A . n 
A 1 1037 TYR 1037 1037 ?    ?   ?   A . n 
A 1 1038 SER 1038 1038 ?    ?   ?   A . n 
A 1 1039 ALA 1039 1039 ?    ?   ?   A . n 
A 1 1040 VAL 1040 1040 ?    ?   ?   A . n 
A 1 1041 MET 1041 1041 ?    ?   ?   A . n 
A 1 1042 GLY 1042 1042 ?    ?   ?   A . n 
A 1 1043 ILE 1043 1043 ?    ?   ?   A . n 
A 1 1044 VAL 1044 1044 ?    ?   ?   A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   A . n 
A 1 1046 GLU 1046 1046 ?    ?   ?   A . n 
A 1 1047 VAL 1047 1047 ?    ?   ?   A . n 
A 1 1048 GLU 1048 1048 ?    ?   ?   A . n 
A 1 1049 GLN 1049 1049 ?    ?   ?   A . n 
A 1 1050 TYR 1050 1050 ?    ?   ?   A . n 
A 1 1051 VAL 1051 1051 ?    ?   ?   A . n 
A 1 1052 LYS 1052 1052 ?    ?   ?   A . n 
A 1 1053 VAL 1053 1053 ?    ?   ?   A . n 
A 1 1054 TRP 1054 1054 ?    ?   ?   A . n 
A 1 1055 LEU 1055 1055 ?    ?   ?   A . n 
A 1 1056 GLN 1056 1056 ?    ?   ?   A . n 
A 1 1057 TYR 1057 1057 ?    ?   ?   A . n 
A 1 1058 GLN 1058 1058 ?    ?   ?   A . n 
A 1 1059 CYS 1059 1059 ?    ?   ?   A . n 
A 1 1060 LEU 1060 1060 ?    ?   ?   A . n 
A 1 1061 TRP 1061 1061 ?    ?   ?   A . n 
A 1 1062 ASP 1062 1062 ?    ?   ?   A . n 
A 1 1063 MET 1063 1063 ?    ?   ?   A . n 
A 1 1064 GLN 1064 1064 ?    ?   ?   A . n 
A 1 1065 ALA 1065 1065 ?    ?   ?   A . n 
A 1 1066 GLU 1066 1066 ?    ?   ?   A . n 
A 1 1067 ASN 1067 1067 ?    ?   ?   A . n 
A 1 1068 ILE 1068 1068 ?    ?   ?   A . n 
A 1 1069 TYR 1069 1069 ?    ?   ?   A . n 
A 1 1070 ASN 1070 1070 ?    ?   ?   A . n 
A 1 1071 ARG 1071 1071 ?    ?   ?   A . n 
A 1 1072 LEU 1072 1072 ?    ?   ?   A . n 
A 1 1073 GLY 1073 1073 ?    ?   ?   A . n 
A 1 1074 GLU 1074 1074 ?    ?   ?   A . n 
A 1 1075 ASP 1075 1075 ?    ?   ?   A . n 
A 1 1076 LEU 1076 1076 ?    ?   ?   A . n 
A 1 1077 ASN 1077 1077 ?    ?   ?   A . n 
A 1 1078 LYS 1078 1078 ?    ?   ?   A . n 
A 1 1079 TRP 1079 1079 ?    ?   ?   A . n 
A 1 1080 GLN 1080 1080 ?    ?   ?   A . n 
A 1 1081 ALA 1081 1081 ?    ?   ?   A . n 
A 1 1082 LEU 1082 1082 ?    ?   ?   A . n 
A 1 1083 LEU 1083 1083 ?    ?   ?   A . n 
A 1 1084 VAL 1084 1084 ?    ?   ?   A . n 
A 1 1085 GLN 1085 1085 ?    ?   ?   A . n 
A 1 1086 ILE 1086 1086 ?    ?   ?   A . n 
A 1 1087 ARG 1087 1087 ?    ?   ?   A . n 
A 1 1088 LYS 1088 1088 ?    ?   ?   A . n 
A 1 1089 ALA 1089 1089 ?    ?   ?   A . n 
A 1 1090 ARG 1090 1090 ?    ?   ?   A . n 
A 1 1091 GLY 1091 1091 ?    ?   ?   A . n 
A 1 1092 THR 1092 1092 ?    ?   ?   A . n 
A 1 1093 PHE 1093 1093 ?    ?   ?   A . n 
A 1 1094 ASP 1094 1094 ?    ?   ?   A . n 
A 1 1095 ASN 1095 1095 ?    ?   ?   A . n 
A 1 1096 ALA 1096 1096 ?    ?   ?   A . n 
A 1 1097 GLU 1097 1097 ?    ?   ?   A . n 
A 1 1098 THR 1098 1098 ?    ?   ?   A . n 
A 1 1099 LYS 1099 1099 ?    ?   ?   A . n 
A 1 1100 LYS 1100 1100 ?    ?   ?   A . n 
A 1 1101 GLU 1101 1101 ?    ?   ?   A . n 
A 1 1102 PHE 1102 1102 ?    ?   ?   A . n 
A 1 1103 GLY 1103 1103 ?    ?   ?   A . n 
A 1 1104 PRO 1104 1104 ?    ?   ?   A . n 
A 1 1105 VAL 1105 1105 ?    ?   ?   A . n 
A 1 1106 VAL 1106 1106 ?    ?   ?   A . n 
A 1 1107 ILE 1107 1107 ?    ?   ?   A . n 
A 1 1108 ASP 1108 1108 ?    ?   ?   A . n 
A 1 1109 TYR 1109 1109 ?    ?   ?   A . n 
A 1 1110 GLY 1110 1110 ?    ?   ?   A . n 
A 1 1111 LYS 1111 1111 ?    ?   ?   A . n 
A 1 1112 VAL 1112 1112 ?    ?   ?   A . n 
A 1 1113 GLN 1113 1113 ?    ?   ?   A . n 
A 1 1114 SER 1114 1114 ?    ?   ?   A . n 
A 1 1115 LYS 1115 1115 ?    ?   ?   A . n 
A 1 1116 VAL 1116 1116 ?    ?   ?   A . n 
A 1 1117 ASN 1117 1117 ?    ?   ?   A . n 
A 1 1118 LEU 1118 1118 ?    ?   ?   A . n 
A 1 1119 LYS 1119 1119 ?    ?   ?   A . n 
A 1 1120 TYR 1120 1120 ?    ?   ?   A . n 
A 1 1121 ASP 1121 1121 ?    ?   ?   A . n 
A 1 1122 SER 1122 1122 ?    ?   ?   A . n 
A 1 1123 TRP 1123 1123 ?    ?   ?   A . n 
A 1 1124 HIS 1124 1124 ?    ?   ?   A . n 
A 1 1125 LYS 1125 1125 ?    ?   ?   A . n 
A 1 1126 GLU 1126 1126 ?    ?   ?   A . n 
A 1 1127 VAL 1127 1127 ?    ?   ?   A . n 
A 1 1128 LEU 1128 1128 ?    ?   ?   A . n 
A 1 1129 SER 1129 1129 ?    ?   ?   A . n 
A 1 1130 LYS 1130 1130 ?    ?   ?   A . n 
A 1 1131 PHE 1131 1131 ?    ?   ?   A . n 
A 1 1132 GLY 1132 1132 ?    ?   ?   A . n 
A 1 1133 GLN 1133 1133 ?    ?   ?   A . n 
A 1 1134 MET 1134 1134 ?    ?   ?   A . n 
A 1 1135 LEU 1135 1135 ?    ?   ?   A . n 
A 1 1136 GLY 1136 1136 ?    ?   ?   A . n 
A 1 1137 SER 1137 1137 ?    ?   ?   A . n 
A 1 1138 ASN 1138 1138 ?    ?   ?   A . n 
A 1 1139 MET 1139 1139 ?    ?   ?   A . n 
A 1 1140 THR 1140 1140 ?    ?   ?   A . n 
A 1 1141 GLU 1141 1141 ?    ?   ?   A . n 
A 1 1142 PHE 1142 1142 ?    ?   ?   A . n 
A 1 1143 HIS 1143 1143 ?    ?   ?   A . n 
A 1 1144 SER 1144 1144 ?    ?   ?   A . n 
A 1 1145 GLN 1145 1145 ?    ?   ?   A . n 
A 1 1146 ILE 1146 1146 ?    ?   ?   A . n 
A 1 1147 SER 1147 1147 ?    ?   ?   A . n 
A 1 1148 LYS 1148 1148 ?    ?   ?   A . n 
A 1 1149 SER 1149 1149 ?    ?   ?   A . n 
A 1 1150 ARG 1150 1150 ?    ?   ?   A . n 
A 1 1151 GLN 1151 1151 ?    ?   ?   A . n 
A 1 1152 GLU 1152 1152 ?    ?   ?   A . n 
A 1 1153 LEU 1153 1153 ?    ?   ?   A . n 
A 1 1154 GLU 1154 1154 ?    ?   ?   A . n 
A 1 1155 GLN 1155 1155 ?    ?   ?   A . n 
A 1 1156 HIS 1156 1156 ?    ?   ?   A . n 
A 1 1157 SER 1157 1157 ?    ?   ?   A . n 
A 1 1158 VAL 1158 1158 ?    ?   ?   A . n 
A 1 1159 ASP 1159 1159 ?    ?   ?   A . n 
A 1 1160 THR 1160 1160 ?    ?   ?   A . n 
A 1 1161 ALA 1161 1161 ?    ?   ?   A . n 
A 1 1162 SER 1162 1162 ?    ?   ?   A . n 
A 1 1163 THR 1163 1163 ?    ?   ?   A . n 
A 1 1164 SER 1164 1164 ?    ?   ?   A . n 
A 1 1165 ASP 1165 1165 ?    ?   ?   A . n 
A 1 1166 ALA 1166 1166 ?    ?   ?   A . n 
A 1 1167 VAL 1167 1167 ?    ?   ?   A . n 
A 1 1168 THR 1168 1168 ?    ?   ?   A . n 
A 1 1169 PHE 1169 1169 ?    ?   ?   A . n 
A 1 1170 ILE 1170 1170 ?    ?   ?   A . n 
A 1 1171 THR 1171 1171 ?    ?   ?   A . n 
A 1 1172 TYR 1172 1172 ?    ?   ?   A . n 
A 1 1173 VAL 1173 1173 ?    ?   ?   A . n 
A 1 1174 GLN 1174 1174 ?    ?   ?   A . n 
A 1 1175 SER 1175 1175 ?    ?   ?   A . n 
A 1 1176 LEU 1176 1176 ?    ?   ?   A . n 
A 1 1177 LYS 1177 1177 ?    ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?    ?   ?   A . n 
A 1 1179 LYS 1179 1179 ?    ?   ?   A . n 
A 1 1180 ILE 1180 1180 ?    ?   ?   A . n 
A 1 1181 LYS 1181 1181 ?    ?   ?   A . n 
A 1 1182 GLN 1182 1182 ?    ?   ?   A . n 
A 1 1183 PHE 1183 1183 ?    ?   ?   A . n 
A 1 1184 GLU 1184 1184 ?    ?   ?   A . n 
A 1 1185 LYS 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLN 1186 1186 ?    ?   ?   A . n 
A 1 1187 VAL 1187 1187 ?    ?   ?   A . n 
A 1 1188 GLU 1188 1188 ?    ?   ?   A . n 
A 1 1189 LEU 1189 1189 ?    ?   ?   A . n 
A 1 1190 TYR 1190 1190 ?    ?   ?   A . n 
A 1 1191 ARG 1191 1191 ?    ?   ?   A . n 
A 1 1192 ASN 1192 1192 ?    ?   ?   A . n 
A 1 1193 GLY 1193 1193 ?    ?   ?   A . n 
A 1 1194 GLN 1194 1194 ?    ?   ?   A . n 
A 1 1195 ARG 1195 1195 ?    ?   ?   A . n 
A 1 1196 LEU 1196 1196 ?    ?   ?   A . n 
A 1 1197 LEU 1197 1197 ?    ?   ?   A . n 
A 1 1198 GLU 1198 1198 ?    ?   ?   A . n 
A 1 1199 LYS 1199 1199 ?    ?   ?   A . n 
A 1 1200 GLN 1200 1200 ?    ?   ?   A . n 
A 1 1201 ARG 1201 1201 ?    ?   ?   A . n 
A 1 1202 PHE 1202 1202 ?    ?   ?   A . n 
A 1 1203 GLN 1203 1203 ?    ?   ?   A . n 
A 1 1204 PHE 1204 1204 ?    ?   ?   A . n 
A 1 1205 PRO 1205 1205 ?    ?   ?   A . n 
A 1 1206 PRO 1206 1206 ?    ?   ?   A . n 
A 1 1207 SER 1207 1207 ?    ?   ?   A . n 
A 1 1208 TRP 1208 1208 ?    ?   ?   A . n 
A 1 1209 LEU 1209 1209 ?    ?   ?   A . n 
A 1 1210 TYR 1210 1210 ?    ?   ?   A . n 
A 1 1211 ILE 1211 1211 ?    ?   ?   A . n 
A 1 1212 ASP 1212 1212 ?    ?   ?   A . n 
A 1 1213 ASN 1213 1213 ?    ?   ?   A . n 
A 1 1214 ILE 1214 1214 ?    ?   ?   A . n 
A 1 1215 GLU 1215 1215 ?    ?   ?   A . n 
A 1 1216 GLY 1216 1216 ?    ?   ?   A . n 
A 1 1217 GLU 1217 1217 ?    ?   ?   A . n 
A 1 1218 TRP 1218 1218 ?    ?   ?   A . n 
A 1 1219 GLY 1219 1219 ?    ?   ?   A . n 
A 1 1220 ALA 1220 1220 ?    ?   ?   A . n 
A 1 1221 PHE 1221 1221 ?    ?   ?   A . n 
A 1 1222 ASN 1222 1222 ?    ?   ?   A . n 
A 1 1223 ASP 1223 1223 ?    ?   ?   A . n 
A 1 1224 ILE 1224 1224 ?    ?   ?   A . n 
A 1 1225 MET 1225 1225 ?    ?   ?   A . n 
A 1 1226 ARG 1226 1226 ?    ?   ?   A . n 
A 1 1227 ARG 1227 1227 ?    ?   ?   A . n 
A 1 1228 LYS 1228 1228 ?    ?   ?   A . n 
A 1 1229 ASP 1229 1229 ?    ?   ?   A . n 
A 1 1230 SER 1230 1230 ?    ?   ?   A . n 
A 1 1231 ALA 1231 1231 ?    ?   ?   A . n 
A 1 1232 ILE 1232 1232 ?    ?   ?   A . n 
A 1 1233 GLN 1233 1233 ?    ?   ?   A . n 
A 1 1234 GLN 1234 1234 ?    ?   ?   A . n 
A 1 1235 GLN 1235 1235 ?    ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?    ?   ?   A . n 
A 1 1237 ALA 1237 1237 ?    ?   ?   A . n 
A 1 1238 ASN 1238 1238 ?    ?   ?   A . n 
A 1 1239 LEU 1239 1239 ?    ?   ?   A . n 
A 1 1240 GLN 1240 1240 ?    ?   ?   A . n 
A 1 1241 MET 1241 1241 ?    ?   ?   A . n 
A 1 1242 LYS 1242 1242 ?    ?   ?   A . n 
A 1 1243 ILE 1243 1243 ?    ?   ?   A . n 
A 1 1244 VAL 1244 1244 ?    ?   ?   A . n 
A 1 1245 GLN 1245 1245 ?    ?   ?   A . n 
A 1 1246 GLU 1246 1246 ?    ?   ?   A . n 
A 1 1247 ASP 1247 1247 ?    ?   ?   A . n 
A 1 1248 ARG 1248 1248 ?    ?   ?   A . n 
A 1 1249 ALA 1249 1249 ?    ?   ?   A . n 
A 1 1250 VAL 1250 1250 ?    ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?    ?   ?   A . n 
A 1 1252 SER 1252 1252 ?    ?   ?   A . n 
A 1 1253 ARG 1253 1253 ?    ?   ?   A . n 
A 1 1254 THR 1254 1254 ?    ?   ?   A . n 
A 1 1255 THR 1255 1255 ?    ?   ?   A . n 
A 1 1256 ASP 1256 1256 ?    ?   ?   A . n 
A 1 1257 LEU 1257 1257 ?    ?   ?   A . n 
A 1 1258 LEU 1258 1258 ?    ?   ?   A . n 
A 1 1259 THR 1259 1259 ?    ?   ?   A . n 
A 1 1260 ASP 1260 1260 ?    ?   ?   A . n 
A 1 1261 TRP 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLU 1262 1262 ?    ?   ?   A . n 
A 1 1263 LYS 1263 1263 ?    ?   ?   A . n 
A 1 1264 THR 1264 1264 ?    ?   ?   A . n 
A 1 1265 LYS 1265 1265 ?    ?   ?   A . n 
A 1 1266 PRO 1266 1266 ?    ?   ?   A . n 
A 1 1267 VAL 1267 1267 ?    ?   ?   A . n 
A 1 1268 THR 1268 1268 ?    ?   ?   A . n 
A 1 1269 GLY 1269 1269 ?    ?   ?   A . n 
A 1 1270 ASN 1270 1270 ?    ?   ?   A . n 
A 1 1271 LEU 1271 1271 ?    ?   ?   A . n 
A 1 1272 ARG 1272 1272 ?    ?   ?   A . n 
A 1 1273 PRO 1273 1273 ?    ?   ?   A . n 
A 1 1274 GLU 1274 1274 ?    ?   ?   A . n 
A 1 1275 GLU 1275 1275 ?    ?   ?   A . n 
A 1 1276 ALA 1276 1276 ?    ?   ?   A . n 
A 1 1277 LEU 1277 1277 ?    ?   ?   A . n 
A 1 1278 GLN 1278 1278 ?    ?   ?   A . n 
A 1 1279 ALA 1279 1279 ?    ?   ?   A . n 
A 1 1280 LEU 1280 1280 ?    ?   ?   A . n 
A 1 1281 THR 1281 1281 ?    ?   ?   A . n 
A 1 1282 ILE 1282 1282 ?    ?   ?   A . n 
A 1 1283 TYR 1283 1283 ?    ?   ?   A . n 
A 1 1284 GLU 1284 1284 ?    ?   ?   A . n 
A 1 1285 GLY 1285 1285 ?    ?   ?   A . n 
A 1 1286 LYS 1286 1286 ?    ?   ?   A . n 
A 1 1287 PHE 1287 1287 ?    ?   ?   A . n 
A 1 1288 GLY 1288 1288 ?    ?   ?   A . n 
A 1 1289 ARG 1289 1289 ?    ?   ?   A . n 
A 1 1290 LEU 1290 1290 ?    ?   ?   A . n 
A 1 1291 LYS 1291 1291 ?    ?   ?   A . n 
A 1 1292 ASP 1292 1292 ?    ?   ?   A . n 
A 1 1293 ASP 1293 1293 ?    ?   ?   A . n 
A 1 1294 ARG 1294 1294 ?    ?   ?   A . n 
A 1 1295 GLU 1295 1295 ?    ?   ?   A . n 
A 1 1296 LYS 1296 1296 ?    ?   ?   A . n 
A 1 1297 CYS 1297 1297 ?    ?   ?   A . n 
A 1 1298 ALA 1298 1298 ?    ?   ?   A . n 
A 1 1299 LYS 1299 1299 ?    ?   ?   A . n 
A 1 1300 ALA 1300 1300 ?    ?   ?   A . n 
A 1 1301 LYS 1301 1301 ?    ?   ?   A . n 
A 1 1302 GLU 1302 1302 ?    ?   ?   A . n 
A 1 1303 ALA 1303 1303 ?    ?   ?   A . n 
A 1 1304 LEU 1304 1304 ?    ?   ?   A . n 
A 1 1305 GLU 1305 1305 ?    ?   ?   A . n 
A 1 1306 LEU 1306 1306 ?    ?   ?   A . n 
A 1 1307 THR 1307 1307 ?    ?   ?   A . n 
A 1 1308 ASP 1308 1308 ?    ?   ?   A . n 
A 1 1309 THR 1309 1309 ?    ?   ?   A . n 
A 1 1310 GLY 1310 1310 ?    ?   ?   A . n 
A 1 1311 LEU 1311 1311 ?    ?   ?   A . n 
A 1 1312 LEU 1312 1312 ?    ?   ?   A . n 
A 1 1313 SER 1313 1313 ?    ?   ?   A . n 
A 1 1314 GLY 1314 1314 ?    ?   ?   A . n 
A 1 1315 SER 1315 1315 ?    ?   ?   A . n 
A 1 1316 GLU 1316 1316 ?    ?   ?   A . n 
A 1 1317 GLU 1317 1317 ?    ?   ?   A . n 
A 1 1318 ARG 1318 1318 ?    ?   ?   A . n 
A 1 1319 VAL 1319 1319 ?    ?   ?   A . n 
A 1 1320 GLN 1320 1320 ?    ?   ?   A . n 
A 1 1321 VAL 1321 1321 ?    ?   ?   A . n 
A 1 1322 ALA 1322 1322 ?    ?   ?   A . n 
A 1 1323 LEU 1323 1323 ?    ?   ?   A . n 
A 1 1324 GLU 1324 1324 ?    ?   ?   A . n 
A 1 1325 GLU 1325 1325 ?    ?   ?   A . n 
A 1 1326 LEU 1326 1326 ?    ?   ?   A . n 
A 1 1327 GLN 1327 1327 ?    ?   ?   A . n 
A 1 1328 ASP 1328 1328 ?    ?   ?   A . n 
A 1 1329 LEU 1329 1329 ?    ?   ?   A . n 
A 1 1330 LYS 1330 1330 ?    ?   ?   A . n 
A 1 1331 GLY 1331 1331 ?    ?   ?   A . n 
A 1 1332 VAL 1332 1332 ?    ?   ?   A . n 
A 1 1333 TRP 1333 1333 ?    ?   ?   A . n 
A 1 1334 SER 1334 1334 ?    ?   ?   A . n 
A 1 1335 GLU 1335 1335 ?    ?   ?   A . n 
A 1 1336 LEU 1336 1336 ?    ?   ?   A . n 
A 1 1337 SER 1337 1337 ?    ?   ?   A . n 
A 1 1338 LYS 1338 1338 ?    ?   ?   A . n 
A 1 1339 VAL 1339 1339 ?    ?   ?   A . n 
A 1 1340 TRP 1340 1340 ?    ?   ?   A . n 
A 1 1341 GLU 1341 1341 ?    ?   ?   A . n 
A 1 1342 GLN 1342 1342 ?    ?   ?   A . n 
A 1 1343 ILE 1343 1343 ?    ?   ?   A . n 
A 1 1344 ASP 1344 1344 ?    ?   ?   A . n 
A 1 1345 GLN 1345 1345 ?    ?   ?   A . n 
A 1 1346 MET 1346 1346 ?    ?   ?   A . n 
A 1 1347 LYS 1347 1347 ?    ?   ?   A . n 
A 1 1348 GLU 1348 1348 ?    ?   ?   A . n 
A 1 1349 GLN 1349 1349 ?    ?   ?   A . n 
A 1 1350 PRO 1350 1350 ?    ?   ?   A . n 
A 1 1351 TRP 1351 1351 ?    ?   ?   A . n 
A 1 1352 VAL 1352 1352 ?    ?   ?   A . n 
A 1 1353 SER 1353 1353 ?    ?   ?   A . n 
A 1 1354 VAL 1354 1354 ?    ?   ?   A . n 
A 1 1355 GLN 1355 1355 ?    ?   ?   A . n 
A 1 1356 PRO 1356 1356 ?    ?   ?   A . n 
A 1 1357 ARG 1357 1357 ?    ?   ?   A . n 
A 1 1358 LYS 1358 1358 ?    ?   ?   A . n 
A 1 1359 LEU 1359 1359 ?    ?   ?   A . n 
A 1 1360 ARG 1360 1360 ?    ?   ?   A . n 
A 1 1361 GLN 1361 1361 ?    ?   ?   A . n 
A 1 1362 ASN 1362 1362 ?    ?   ?   A . n 
A 1 1363 LEU 1363 1363 ?    ?   ?   A . n 
A 1 1364 ASP 1364 1364 ?    ?   ?   A . n 
A 1 1365 ALA 1365 1365 ?    ?   ?   A . n 
A 1 1366 LEU 1366 1366 ?    ?   ?   A . n 
A 1 1367 LEU 1367 1367 ?    ?   ?   A . n 
A 1 1368 ASN 1368 1368 ?    ?   ?   A . n 
A 1 1369 GLN 1369 1369 ?    ?   ?   A . n 
A 1 1370 LEU 1370 1370 ?    ?   ?   A . n 
A 1 1371 LYS 1371 1371 ?    ?   ?   A . n 
A 1 1372 SER 1372 1372 ?    ?   ?   A . n 
A 1 1373 PHE 1373 1373 ?    ?   ?   A . n 
A 1 1374 PRO 1374 1374 ?    ?   ?   A . n 
A 1 1375 ALA 1375 1375 ?    ?   ?   A . n 
A 1 1376 ARG 1376 1376 ?    ?   ?   A . n 
A 1 1377 LEU 1377 1377 ?    ?   ?   A . n 
A 1 1378 ARG 1378 1378 ?    ?   ?   A . n 
A 1 1379 GLN 1379 1379 ?    ?   ?   A . n 
A 1 1380 TYR 1380 1380 ?    ?   ?   A . n 
A 1 1381 ALA 1381 1381 ?    ?   ?   A . n 
A 1 1382 SER 1382 1382 ?    ?   ?   A . n 
A 1 1383 TYR 1383 1383 ?    ?   ?   A . n 
A 1 1384 GLU 1384 1384 ?    ?   ?   A . n 
A 1 1385 PHE 1385 1385 ?    ?   ?   A . n 
A 1 1386 VAL 1386 1386 ?    ?   ?   A . n 
A 1 1387 GLN 1387 1387 ?    ?   ?   A . n 
A 1 1388 ARG 1388 1388 ?    ?   ?   A . n 
A 1 1389 LEU 1389 1389 ?    ?   ?   A . n 
A 1 1390 LEU 1390 1390 ?    ?   ?   A . n 
A 1 1391 LYS 1391 1391 ?    ?   ?   A . n 
A 1 1392 GLY 1392 1392 ?    ?   ?   A . n 
A 1 1393 TYR 1393 1393 ?    ?   ?   A . n 
A 1 1394 MET 1394 1394 ?    ?   ?   A . n 
A 1 1395 LYS 1395 1395 ?    ?   ?   A . n 
A 1 1396 ILE 1396 1396 ?    ?   ?   A . n 
A 1 1397 ASN 1397 1397 ?    ?   ?   A . n 
A 1 1398 MET 1398 1398 ?    ?   ?   A . n 
A 1 1399 LEU 1399 1399 ?    ?   ?   A . n 
A 1 1400 VAL 1400 1400 ?    ?   ?   A . n 
A 1 1401 ILE 1401 1401 ?    ?   ?   A . n 
A 1 1402 GLU 1402 1402 ?    ?   ?   A . n 
A 1 1403 LEU 1403 1403 ?    ?   ?   A . n 
A 1 1404 LYS 1404 1404 ?    ?   ?   A . n 
A 1 1405 SER 1405 1405 ?    ?   ?   A . n 
A 1 1406 GLU 1406 1406 ?    ?   ?   A . n 
A 1 1407 ALA 1407 1407 ?    ?   ?   A . n 
A 1 1408 LEU 1408 1408 ?    ?   ?   A . n 
A 1 1409 LYS 1409 1409 ?    ?   ?   A . n 
A 1 1410 ASP 1410 1410 ?    ?   ?   A . n 
A 1 1411 ARG 1411 1411 ?    ?   ?   A . n 
A 1 1412 HIS 1412 1412 ?    ?   ?   A . n 
A 1 1413 TRP 1413 1413 ?    ?   ?   A . n 
A 1 1414 LYS 1414 1414 ?    ?   ?   A . n 
A 1 1415 GLN 1415 1415 ?    ?   ?   A . n 
A 1 1416 LEU 1416 1416 ?    ?   ?   A . n 
A 1 1417 MET 1417 1417 ?    ?   ?   A . n 
A 1 1418 LYS 1418 1418 ?    ?   ?   A . n 
A 1 1419 ARG 1419 1419 ?    ?   ?   A . n 
A 1 1420 LEU 1420 1420 ?    ?   ?   A . n 
A 1 1421 HIS 1421 1421 ?    ?   ?   A . n 
A 1 1422 VAL 1422 1422 ?    ?   ?   A . n 
A 1 1423 ASN 1423 1423 ?    ?   ?   A . n 
A 1 1424 TRP 1424 1424 ?    ?   ?   A . n 
A 1 1425 VAL 1425 1425 ?    ?   ?   A . n 
A 1 1426 VAL 1426 1426 ?    ?   ?   A . n 
A 1 1427 SER 1427 1427 ?    ?   ?   A . n 
A 1 1428 GLU 1428 1428 ?    ?   ?   A . n 
A 1 1429 LEU 1429 1429 ?    ?   ?   A . n 
A 1 1430 THR 1430 1430 ?    ?   ?   A . n 
A 1 1431 LEU 1431 1431 ?    ?   ?   A . n 
A 1 1432 GLY 1432 1432 ?    ?   ?   A . n 
A 1 1433 GLN 1433 1433 ?    ?   ?   A . n 
A 1 1434 ILE 1434 1434 ?    ?   ?   A . n 
A 1 1435 TRP 1435 1435 ?    ?   ?   A . n 
A 1 1436 ASP 1436 1436 ?    ?   ?   A . n 
A 1 1437 VAL 1437 1437 ?    ?   ?   A . n 
A 1 1438 ASP 1438 1438 ?    ?   ?   A . n 
A 1 1439 LEU 1439 1439 ?    ?   ?   A . n 
A 1 1440 GLN 1440 1440 ?    ?   ?   A . n 
A 1 1441 LYS 1441 1441 ?    ?   ?   A . n 
A 1 1442 ASN 1442 1442 ?    ?   ?   A . n 
A 1 1443 GLU 1443 1443 ?    ?   ?   A . n 
A 1 1444 ALA 1444 1444 ?    ?   ?   A . n 
A 1 1445 ILE 1445 1445 ?    ?   ?   A . n 
A 1 1446 VAL 1446 1446 ?    ?   ?   A . n 
A 1 1447 LYS 1447 1447 ?    ?   ?   A . n 
A 1 1448 ASP 1448 1448 ?    ?   ?   A . n 
A 1 1449 VAL 1449 1449 ?    ?   ?   A . n 
A 1 1450 LEU 1450 1450 ?    ?   ?   A . n 
A 1 1451 LEU 1451 1451 ?    ?   ?   A . n 
A 1 1452 VAL 1452 1452 ?    ?   ?   A . n 
A 1 1453 ALA 1453 1453 ?    ?   ?   A . n 
A 1 1454 GLN 1454 1454 ?    ?   ?   A . n 
A 1 1455 GLY 1455 1455 ?    ?   ?   A . n 
A 1 1456 GLU 1456 1456 ?    ?   ?   A . n 
A 1 1457 MET 1457 1457 1457 MET MET A . n 
A 1 1458 ALA 1458 1458 1458 ALA ALA A . n 
A 1 1459 LEU 1459 1459 1459 LEU LEU A . n 
A 1 1460 GLU 1460 1460 1460 GLU GLU A . n 
A 1 1461 GLU 1461 1461 1461 GLU GLU A . n 
A 1 1462 PHE 1462 1462 1462 PHE PHE A . n 
A 1 1463 LEU 1463 1463 1463 LEU LEU A . n 
A 1 1464 LYS 1464 1464 1464 LYS LYS A . n 
A 1 1465 GLN 1465 1465 1465 GLN GLN A . n 
A 1 1466 ILE 1466 1466 1466 ILE ILE A . n 
A 1 1467 ARG 1467 1467 1467 ARG ARG A . n 
A 1 1468 GLU 1468 1468 1468 GLU GLU A . n 
A 1 1469 VAL 1469 1469 1469 VAL VAL A . n 
A 1 1470 TRP 1470 1470 1470 TRP TRP A . n 
A 1 1471 ASN 1471 1471 1471 ASN ASN A . n 
A 1 1472 THR 1472 1472 1472 THR THR A . n 
A 1 1473 TYR 1473 1473 1473 TYR TYR A . n 
A 1 1474 GLU 1474 1474 1474 GLU GLU A . n 
A 1 1475 LEU 1475 1475 1475 LEU LEU A . n 
A 1 1476 ASP 1476 1476 1476 ASP ASP A . n 
A 1 1477 LEU 1477 1477 1477 LEU LEU A . n 
A 1 1478 VAL 1478 1478 1478 VAL VAL A . n 
A 1 1479 ASN 1479 1479 1479 ASN ASN A . n 
A 1 1480 TYR 1480 1480 1480 TYR TYR A . n 
A 1 1481 GLN 1481 1481 1481 GLN GLN A . n 
A 1 1482 ASN 1482 1482 1482 ASN ASN A . n 
A 1 1483 LYS 1483 1483 1483 LYS LYS A . n 
A 1 1484 CYS 1484 1484 1484 CYS CYS A . n 
A 1 1485 ARG 1485 1485 1485 ARG ARG A . n 
A 1 1486 LEU 1486 1486 1486 LEU LEU A . n 
A 1 1487 ILE 1487 1487 1487 ILE ILE A . n 
A 1 1488 ARG 1488 1488 1488 ARG ARG A . n 
A 1 1489 GLY 1489 1489 1489 GLY GLY A . n 
A 1 1490 TRP 1490 1490 1490 TRP TRP A . n 
A 1 1491 ASP 1491 1491 1491 ASP ASP A . n 
A 1 1492 ASP 1492 1492 1492 ASP ASP A . n 
A 1 1493 LEU 1493 1493 1493 LEU LEU A . n 
A 1 1494 PHE 1494 1494 1494 PHE PHE A . n 
A 1 1495 ASN 1495 1495 1495 ASN ASN A . n 
A 1 1496 LYS 1496 1496 1496 LYS LYS A . n 
A 1 1497 VAL 1497 1497 1497 VAL VAL A . n 
A 1 1498 LYS 1498 1498 1498 LYS LYS A . n 
A 1 1499 GLU 1499 1499 1499 GLU GLU A . n 
A 1 1500 HIS 1500 1500 1500 HIS HIS A . n 
A 1 1501 ILE 1501 1501 1501 ILE ILE A . n 
A 1 1502 ASN 1502 1502 1502 ASN ASN A . n 
A 1 1503 SER 1503 1503 1503 SER SER A . n 
A 1 1504 VAL 1504 1504 1504 VAL VAL A . n 
A 1 1505 SER 1505 1505 1505 SER SER A . n 
A 1 1506 ALA 1506 1506 1506 ALA ALA A . n 
A 1 1507 MET 1507 1507 1507 MET MET A . n 
A 1 1508 LYS 1508 1508 1508 LYS LYS A . n 
A 1 1509 LEU 1509 1509 1509 LEU LEU A . n 
A 1 1510 SER 1510 1510 1510 SER SER A . n 
A 1 1511 PRO 1511 1511 1511 PRO PRO A . n 
A 1 1512 TYR 1512 1512 1512 TYR TYR A . n 
A 1 1513 TYR 1513 1513 1513 TYR TYR A . n 
A 1 1514 LYS 1514 1514 1514 LYS LYS A . n 
A 1 1515 VAL 1515 1515 1515 VAL VAL A . n 
A 1 1516 PHE 1516 1516 1516 PHE PHE A . n 
A 1 1517 GLU 1517 1517 1517 GLU GLU A . n 
A 1 1518 GLU 1518 1518 1518 GLU GLU A . n 
A 1 1519 ASP 1519 1519 1519 ASP ASP A . n 
A 1 1520 ALA 1520 1520 1520 ALA ALA A . n 
A 1 1521 LEU 1521 1521 1521 LEU LEU A . n 
A 1 1522 SER 1522 1522 1522 SER SER A . n 
A 1 1523 TRP 1523 1523 1523 TRP TRP A . n 
A 1 1524 GLU 1524 1524 1524 GLU GLU A . n 
A 1 1525 ASP 1525 1525 1525 ASP ASP A . n 
A 1 1526 LYS 1526 1526 1526 LYS LYS A . n 
A 1 1527 LEU 1527 1527 1527 LEU LEU A . n 
A 1 1528 ASN 1528 1528 1528 ASN ASN A . n 
A 1 1529 ARG 1529 1529 1529 ARG ARG A . n 
A 1 1530 ILE 1530 1530 1530 ILE ILE A . n 
A 1 1531 MET 1531 1531 1531 MET MET A . n 
A 1 1532 ALA 1532 1532 1532 ALA ALA A . n 
A 1 1533 LEU 1533 1533 1533 LEU LEU A . n 
A 1 1534 PHE 1534 1534 1534 PHE PHE A . n 
A 1 1535 ASP 1535 1535 1535 ASP ASP A . n 
A 1 1536 VAL 1536 1536 1536 VAL VAL A . n 
A 1 1537 TRP 1537 1537 1537 TRP TRP A . n 
A 1 1538 ILE 1538 1538 1538 ILE ILE A . n 
A 1 1539 ASP 1539 1539 1539 ASP ASP A . n 
A 1 1540 VAL 1540 1540 1540 VAL VAL A . n 
A 1 1541 GLN 1541 1541 1541 GLN GLN A . n 
A 1 1542 ARG 1542 1542 1542 ARG ARG A . n 
A 1 1543 ARG 1543 1543 1543 ARG ARG A . n 
A 1 1544 TRP 1544 1544 1544 TRP TRP A . n 
A 1 1545 VAL 1545 1545 1545 VAL VAL A . n 
A 1 1546 TYR 1546 1546 1546 TYR TYR A . n 
A 1 1547 LEU 1547 1547 1547 LEU LEU A . n 
A 1 1548 GLU 1548 1548 1548 GLU GLU A . n 
A 1 1549 GLY 1549 1549 1549 GLY GLY A . n 
A 1 1550 ILE 1550 1550 1550 ILE ILE A . n 
A 1 1551 PHE 1551 1551 1551 PHE PHE A . n 
A 1 1552 THR 1552 1552 1552 THR THR A . n 
A 1 1553 GLY 1553 1553 1553 GLY GLY A . n 
A 1 1554 SER 1554 1554 1554 SER SER A . n 
A 1 1555 ALA 1555 1555 1555 ALA ALA A . n 
A 1 1556 ASP 1556 1556 1556 ASP ASP A . n 
A 1 1557 ILE 1557 1557 1557 ILE ILE A . n 
A 1 1558 LYS 1558 1558 1558 LYS LYS A . n 
A 1 1559 HIS 1559 1559 1559 HIS HIS A . n 
A 1 1560 LEU 1560 1560 1560 LEU LEU A . n 
A 1 1561 LEU 1561 1561 1561 LEU LEU A . n 
A 1 1562 PRO 1562 1562 1562 PRO PRO A . n 
A 1 1563 VAL 1563 1563 1563 VAL VAL A . n 
A 1 1564 GLU 1564 1564 1564 GLU GLU A . n 
A 1 1565 THR 1565 1565 1565 THR THR A . n 
A 1 1566 GLN 1566 1566 1566 GLN GLN A . n 
A 1 1567 ARG 1567 1567 1567 ARG ARG A . n 
A 1 1568 PHE 1568 1568 1568 PHE PHE A . n 
A 1 1569 GLN 1569 1569 1569 GLN GLN A . n 
A 1 1570 SER 1570 1570 1570 SER SER A . n 
A 1 1571 ILE 1571 1571 1571 ILE ILE A . n 
A 1 1572 SER 1572 1572 1572 SER SER A . n 
A 1 1573 THR 1573 1573 1573 THR THR A . n 
A 1 1574 GLU 1574 1574 1574 GLU GLU A . n 
A 1 1575 PHE 1575 1575 1575 PHE PHE A . n 
A 1 1576 LEU 1576 1576 1576 LEU LEU A . n 
A 1 1577 ALA 1577 1577 1577 ALA ALA A . n 
A 1 1578 LEU 1578 1578 1578 LEU LEU A . n 
A 1 1579 MET 1579 1579 1579 MET MET A . n 
A 1 1580 LYS 1580 1580 1580 LYS LYS A . n 
A 1 1581 LYS 1581 1581 1581 LYS LYS A . n 
A 1 1582 VAL 1582 1582 1582 VAL VAL A . n 
A 1 1583 SER 1583 1583 1583 SER SER A . n 
A 1 1584 LYS 1584 1584 1584 LYS LYS A . n 
A 1 1585 SER 1585 1585 1585 SER SER A . n 
A 1 1586 PRO 1586 1586 1586 PRO PRO A . n 
A 1 1587 LEU 1587 1587 1587 LEU LEU A . n 
A 1 1588 VAL 1588 1588 1588 VAL VAL A . n 
A 1 1589 MET 1589 1589 1589 MET MET A . n 
A 1 1590 ASP 1590 1590 1590 ASP ASP A . n 
A 1 1591 VAL 1591 1591 1591 VAL VAL A . n 
A 1 1592 LEU 1592 1592 1592 LEU LEU A . n 
A 1 1593 ASN 1593 1593 1593 ASN ASN A . n 
A 1 1594 ILE 1594 1594 1594 ILE ILE A . n 
A 1 1595 GLN 1595 1595 1595 GLN GLN A . n 
A 1 1596 GLY 1596 1596 1596 GLY GLY A . n 
A 1 1597 VAL 1597 1597 1597 VAL VAL A . n 
A 1 1598 GLN 1598 1598 1598 GLN GLN A . n 
A 1 1599 ARG 1599 1599 1599 ARG ARG A . n 
A 1 1600 SER 1600 1600 1600 SER SER A . n 
A 1 1601 LEU 1601 1601 1601 LEU LEU A . n 
A 1 1602 GLU 1602 1602 1602 GLU GLU A . n 
A 1 1603 ARG 1603 1603 1603 ARG ARG A . n 
A 1 1604 LEU 1604 1604 1604 LEU LEU A . n 
A 1 1605 ALA 1605 1605 1605 ALA ALA A . n 
A 1 1606 ASP 1606 1606 1606 ASP ASP A . n 
A 1 1607 LEU 1607 1607 1607 LEU LEU A . n 
A 1 1608 LEU 1608 1608 1608 LEU LEU A . n 
A 1 1609 GLY 1609 1609 1609 GLY GLY A . n 
A 1 1610 LYS 1610 1610 1610 LYS LYS A . n 
A 1 1611 ILE 1611 1611 1611 ILE ILE A . n 
A 1 1612 GLN 1612 1612 1612 GLN GLN A . n 
A 1 1613 LYS 1613 1613 1613 LYS LYS A . n 
A 1 1614 ALA 1614 1614 1614 ALA ALA A . n 
A 1 1615 LEU 1615 1615 1615 LEU LEU A . n 
A 1 1616 GLY 1616 1616 1616 GLY GLY A . n 
A 1 1617 GLU 1617 1617 1617 GLU GLU A . n 
A 1 1618 TYR 1618 1618 1618 TYR TYR A . n 
A 1 1619 LEU 1619 1619 1619 LEU LEU A . n 
A 1 1620 GLU 1620 1620 1620 GLU GLU A . n 
A 1 1621 ARG 1621 1621 1621 ARG ARG A . n 
A 1 1622 GLU 1622 1622 1622 GLU GLU A . n 
A 1 1623 ARG 1623 1623 1623 ARG ARG A . n 
A 1 1624 SER 1624 1624 1624 SER SER A . n 
A 1 1625 SER 1625 1625 1625 SER SER A . n 
A 1 1626 PHE 1626 1626 1626 PHE PHE A . n 
A 1 1627 PRO 1627 1627 1627 PRO PRO A . n 
A 1 1628 ARG 1628 1628 1628 ARG ARG A . n 
A 1 1629 PHE 1629 1629 1629 PHE PHE A . n 
A 1 1630 TYR 1630 1630 1630 TYR TYR A . n 
A 1 1631 PHE 1631 1631 1631 PHE PHE A . n 
A 1 1632 VAL 1632 1632 1632 VAL VAL A . n 
A 1 1633 GLY 1633 1633 1633 GLY GLY A . n 
A 1 1634 ASP 1634 1634 1634 ASP ASP A . n 
A 1 1635 GLU 1635 1635 1635 GLU GLU A . n 
A 1 1636 ASP 1636 1636 1636 ASP ASP A . n 
A 1 1637 LEU 1637 1637 1637 LEU LEU A . n 
A 1 1638 LEU 1638 1638 1638 LEU LEU A . n 
A 1 1639 GLU 1639 1639 1639 GLU GLU A . n 
A 1 1640 ILE 1640 1640 1640 ILE ILE A . n 
A 1 1641 ILE 1641 1641 1641 ILE ILE A . n 
A 1 1642 GLY 1642 1642 1642 GLY GLY A . n 
A 1 1643 ASN 1643 1643 1643 ASN ASN A . n 
A 1 1644 SER 1644 1644 1644 SER SER A . n 
A 1 1645 LYS 1645 1645 1645 LYS LYS A . n 
A 1 1646 ASN 1646 1646 1646 ASN ASN A . n 
A 1 1647 VAL 1647 1647 1647 VAL VAL A . n 
A 1 1648 ALA 1648 1648 1648 ALA ALA A . n 
A 1 1649 LYS 1649 1649 1649 LYS LYS A . n 
A 1 1650 LEU 1650 1650 1650 LEU LEU A . n 
A 1 1651 GLN 1651 1651 1651 GLN GLN A . n 
A 1 1652 LYS 1652 1652 1652 LYS LYS A . n 
A 1 1653 HIS 1653 1653 1653 HIS HIS A . n 
A 1 1654 PHE 1654 1654 1654 PHE PHE A . n 
A 1 1655 LYS 1655 1655 1655 LYS LYS A . n 
A 1 1656 LYS 1656 1656 1656 LYS LYS A . n 
A 1 1657 MET 1657 1657 1657 MET MET A . n 
A 1 1658 PHE 1658 1658 1658 PHE PHE A . n 
A 1 1659 ALA 1659 1659 1659 ALA ALA A . n 
A 1 1660 GLY 1660 1660 1660 GLY GLY A . n 
A 1 1661 VAL 1661 1661 1661 VAL VAL A . n 
A 1 1662 SER 1662 1662 1662 SER SER A . n 
A 1 1663 SER 1663 1663 1663 SER SER A . n 
A 1 1664 ILE 1664 1664 1664 ILE ILE A . n 
A 1 1665 ILE 1665 1665 1665 ILE ILE A . n 
A 1 1666 LEU 1666 1666 1666 LEU LEU A . n 
A 1 1667 ASN 1667 1667 1667 ASN ASN A . n 
A 1 1668 GLU 1668 1668 1668 GLU GLU A . n 
A 1 1669 ASP 1669 1669 1669 ASP ASP A . n 
A 1 1670 ASN 1670 1670 1670 ASN ASN A . n 
A 1 1671 SER 1671 1671 1671 SER SER A . n 
A 1 1672 VAL 1672 1672 1672 VAL VAL A . n 
A 1 1673 VAL 1673 1673 1673 VAL VAL A . n 
A 1 1674 LEU 1674 1674 1674 LEU LEU A . n 
A 1 1675 GLY 1675 1675 1675 GLY GLY A . n 
A 1 1676 ILE 1676 1676 1676 ILE ILE A . n 
A 1 1677 SER 1677 1677 1677 SER SER A . n 
A 1 1678 SER 1678 1678 1678 SER SER A . n 
A 1 1679 ARG 1679 1679 1679 ARG ARG A . n 
A 1 1680 GLU 1680 1680 1680 GLU GLU A . n 
A 1 1681 GLY 1681 1681 1681 GLY GLY A . n 
A 1 1682 GLU 1682 1682 1682 GLU GLU A . n 
A 1 1683 GLU 1683 1683 1683 GLU GLU A . n 
A 1 1684 VAL 1684 1684 1684 VAL VAL A . n 
A 1 1685 MET 1685 1685 1685 MET MET A . n 
A 1 1686 PHE 1686 1686 1686 PHE PHE A . n 
A 1 1687 LYS 1687 1687 1687 LYS LYS A . n 
A 1 1688 THR 1688 1688 1688 THR THR A . n 
A 1 1689 PRO 1689 1689 1689 PRO PRO A . n 
A 1 1690 VAL 1690 1690 1690 VAL VAL A . n 
A 1 1691 SER 1691 1691 1691 SER SER A . n 
A 1 1692 ILE 1692 1692 1692 ILE ILE A . n 
A 1 1693 THR 1693 1693 1693 THR THR A . n 
A 1 1694 GLU 1694 1694 1694 GLU GLU A . n 
A 1 1695 HIS 1695 1695 1695 HIS HIS A . n 
A 1 1696 PRO 1696 1696 1696 PRO PRO A . n 
A 1 1697 LYS 1697 1697 1697 LYS LYS A . n 
A 1 1698 ILE 1698 1698 1698 ILE ILE A . n 
A 1 1699 ASN 1699 1699 1699 ASN ASN A . n 
A 1 1700 GLU 1700 1700 1700 GLU GLU A . n 
A 1 1701 TRP 1701 1701 1701 TRP TRP A . n 
A 1 1702 LEU 1702 1702 1702 LEU LEU A . n 
A 1 1703 THR 1703 1703 1703 THR THR A . n 
A 1 1704 LEU 1704 1704 1704 LEU LEU A . n 
A 1 1705 VAL 1705 1705 1705 VAL VAL A . n 
A 1 1706 GLU 1706 1706 1706 GLU GLU A . n 
A 1 1707 LYS 1707 1707 1707 LYS LYS A . n 
A 1 1708 GLU 1708 1708 1708 GLU GLU A . n 
A 1 1709 MET 1709 1709 1709 MET MET A . n 
A 1 1710 ARG 1710 1710 1710 ARG ARG A . n 
A 1 1711 VAL 1711 1711 1711 VAL VAL A . n 
A 1 1712 THR 1712 1712 1712 THR THR A . n 
A 1 1713 LEU 1713 1713 1713 LEU LEU A . n 
A 1 1714 ALA 1714 1714 1714 ALA ALA A . n 
A 1 1715 LYS 1715 1715 1715 LYS LYS A . n 
A 1 1716 LEU 1716 1716 1716 LEU LEU A . n 
A 1 1717 LEU 1717 1717 1717 LEU LEU A . n 
A 1 1718 ALA 1718 1718 1718 ALA ALA A . n 
A 1 1719 GLU 1719 1719 1719 GLU GLU A . n 
A 1 1720 SER 1720 1720 1720 SER SER A . n 
A 1 1721 VAL 1721 1721 1721 VAL VAL A . n 
A 1 1722 THR 1722 1722 1722 THR THR A . n 
A 1 1723 GLU 1723 1723 1723 GLU GLU A . n 
A 1 1724 VAL 1724 1724 1724 VAL VAL A . n 
A 1 1725 GLU 1725 1725 1725 GLU GLU A . n 
A 1 1726 ILE 1726 1726 1726 ILE ILE A . n 
A 1 1727 PHE 1727 1727 1727 PHE PHE A . n 
A 1 1728 GLY 1728 1728 1728 GLY GLY A . n 
A 1 1729 LYS 1729 1729 1729 LYS LYS A . n 
A 1 1730 ALA 1730 1730 1730 ALA ALA A . n 
A 1 1731 THR 1731 1731 1731 THR THR A . n 
A 1 1732 SER 1732 1732 1732 SER SER A . n 
A 1 1733 ILE 1733 1733 1733 ILE ILE A . n 
A 1 1734 ASP 1734 1734 1734 ASP ASP A . n 
A 1 1735 PRO 1735 1735 1735 PRO PRO A . n 
A 1 1736 ASN 1736 1736 1736 ASN ASN A . n 
A 1 1737 THR 1737 1737 1737 THR THR A . n 
A 1 1738 TYR 1738 1738 1738 TYR TYR A . n 
A 1 1739 ILE 1739 1739 1739 ILE ILE A . n 
A 1 1740 THR 1740 1740 1740 THR THR A . n 
A 1 1741 TRP 1741 1741 1741 TRP TRP A . n 
A 1 1742 ILE 1742 1742 1742 ILE ILE A . n 
A 1 1743 ASP 1743 1743 1743 ASP ASP A . n 
A 1 1744 LYS 1744 1744 1744 LYS LYS A . n 
A 1 1745 TYR 1745 1745 1745 TYR TYR A . n 
A 1 1746 GLN 1746 1746 1746 GLN GLN A . n 
A 1 1747 ALA 1747 1747 1747 ALA ALA A . n 
A 1 1748 GLN 1748 1748 1748 GLN GLN A . n 
A 1 1749 LEU 1749 1749 1749 LEU LEU A . n 
A 1 1750 VAL 1750 1750 1750 VAL VAL A . n 
A 1 1751 VAL 1751 1751 1751 VAL VAL A . n 
A 1 1752 LEU 1752 1752 1752 LEU LEU A . n 
A 1 1753 SER 1753 1753 1753 SER SER A . n 
A 1 1754 ALA 1754 1754 1754 ALA ALA A . n 
A 1 1755 GLN 1755 1755 1755 GLN GLN A . n 
A 1 1756 ILE 1756 1756 1756 ILE ILE A . n 
A 1 1757 ALA 1757 1757 1757 ALA ALA A . n 
A 1 1758 TRP 1758 1758 1758 TRP TRP A . n 
A 1 1759 SER 1759 1759 1759 SER SER A . n 
A 1 1760 GLU 1760 1760 1760 GLU GLU A . n 
A 1 1761 ASN 1761 1761 1761 ASN ASN A . n 
A 1 1762 VAL 1762 1762 1762 VAL VAL A . n 
A 1 1763 GLU 1763 1763 1763 GLU GLU A . n 
A 1 1764 THR 1764 1764 1764 THR THR A . n 
A 1 1765 ALA 1765 1765 1765 ALA ALA A . n 
A 1 1766 LEU 1766 1766 1766 LEU LEU A . n 
A 1 1767 SER 1767 1767 1767 SER SER A . n 
A 1 1768 SER 1768 1768 1768 SER SER A . n 
A 1 1769 MET 1769 1769 1769 MET MET A . n 
A 1 1770 GLY 1770 1770 1770 GLY GLY A . n 
A 1 1771 GLY 1771 1771 1771 GLY GLY A . n 
A 1 1772 GLY 1772 1772 1772 GLY GLY A . n 
A 1 1773 GLY 1773 1773 1773 GLY GLY A . n 
A 1 1774 ASP 1774 1774 1774 ASP ASP A . n 
A 1 1775 ALA 1775 1775 1775 ALA ALA A . n 
A 1 1776 ALA 1776 1776 1776 ALA ALA A . n 
A 1 1777 PRO 1777 1777 1777 PRO PRO A . n 
A 1 1778 LEU 1778 1778 1778 LEU LEU A . n 
A 1 1779 HIS 1779 1779 1779 HIS HIS A . n 
A 1 1780 SER 1780 1780 1780 SER SER A . n 
A 1 1781 VAL 1781 1781 1781 VAL VAL A . n 
A 1 1782 LEU 1782 1782 1782 LEU LEU A . n 
A 1 1783 SER 1783 1783 1783 SER SER A . n 
A 1 1784 ASN 1784 1784 1784 ASN ASN A . n 
A 1 1785 VAL 1785 1785 1785 VAL VAL A . n 
A 1 1786 GLU 1786 1786 1786 GLU GLU A . n 
A 1 1787 VAL 1787 1787 1787 VAL VAL A . n 
A 1 1788 THR 1788 1788 1788 THR THR A . n 
A 1 1789 LEU 1789 1789 1789 LEU LEU A . n 
A 1 1790 ASN 1790 1790 1790 ASN ASN A . n 
A 1 1791 VAL 1791 1791 1791 VAL VAL A . n 
A 1 1792 LEU 1792 1792 1792 LEU LEU A . n 
A 1 1793 ALA 1793 1793 1793 ALA ALA A . n 
A 1 1794 ASP 1794 1794 1794 ASP ASP A . n 
A 1 1795 SER 1795 1795 1795 SER SER A . n 
A 1 1796 VAL 1796 1796 1796 VAL VAL A . n 
A 1 1797 LEU 1797 1797 1797 LEU LEU A . n 
A 1 1798 MET 1798 1798 1798 MET MET A . n 
A 1 1799 GLU 1799 1799 1799 GLU GLU A . n 
A 1 1800 GLN 1800 1800 1800 GLN GLN A . n 
A 1 1801 PRO 1801 1801 1801 PRO PRO A . n 
A 1 1802 PRO 1802 1802 1802 PRO PRO A . n 
A 1 1803 LEU 1803 1803 1803 LEU LEU A . n 
A 1 1804 ARG 1804 1804 1804 ARG ARG A . n 
A 1 1805 ARG 1805 1805 1805 ARG ARG A . n 
A 1 1806 ARG 1806 1806 1806 ARG ARG A . n 
A 1 1807 LYS 1807 1807 1807 LYS LYS A . n 
A 1 1808 LEU 1808 1808 1808 LEU LEU A . n 
A 1 1809 GLU 1809 1809 1809 GLU GLU A . n 
A 1 1810 HIS 1810 1810 1810 HIS HIS A . n 
A 1 1811 LEU 1811 1811 1811 LEU LEU A . n 
A 1 1812 ILE 1812 1812 1812 ILE ILE A . n 
A 1 1813 THR 1813 1813 1813 THR THR A . n 
A 1 1814 GLU 1814 1814 1814 GLU GLU A . n 
A 1 1815 LEU 1815 1815 1815 LEU LEU A . n 
A 1 1816 VAL 1816 1816 1816 VAL VAL A . n 
A 1 1817 HIS 1817 1817 1817 HIS HIS A . n 
A 1 1818 GLN 1818 1818 1818 GLN GLN A . n 
A 1 1819 ARG 1819 1819 1819 ARG ARG A . n 
A 1 1820 ASP 1820 1820 1820 ASP ASP A . n 
A 1 1821 VAL 1821 1821 1821 VAL VAL A . n 
A 1 1822 THR 1822 1822 1822 THR THR A . n 
A 1 1823 ARG 1823 1823 1823 ARG ARG A . n 
A 1 1824 SER 1824 1824 1824 SER SER A . n 
A 1 1825 LEU 1825 1825 1825 LEU LEU A . n 
A 1 1826 ILE 1826 1826 1826 ILE ILE A . n 
A 1 1827 LYS 1827 1827 1827 LYS LYS A . n 
A 1 1828 SER 1828 1828 1828 SER SER A . n 
A 1 1829 LYS 1829 1829 1829 LYS LYS A . n 
A 1 1830 ILE 1830 1830 1830 ILE ILE A . n 
A 1 1831 ASP 1831 1831 1831 ASP ASP A . n 
A 1 1832 ASN 1832 1832 1832 ASN ASN A . n 
A 1 1833 ALA 1833 1833 1833 ALA ALA A . n 
A 1 1834 LYS 1834 1834 1834 LYS LYS A . n 
A 1 1835 SER 1835 1835 1835 SER SER A . n 
A 1 1836 PHE 1836 1836 1836 PHE PHE A . n 
A 1 1837 GLU 1837 1837 1837 GLU GLU A . n 
A 1 1838 TRP 1838 1838 1838 TRP TRP A . n 
A 1 1839 LEU 1839 1839 1839 LEU LEU A . n 
A 1 1840 SER 1840 1840 1840 SER SER A . n 
A 1 1841 GLN 1841 1841 1841 GLN GLN A . n 
A 1 1842 MET 1842 1842 1842 MET MET A . n 
A 1 1843 ARG 1843 1843 1843 ARG ARG A . n 
A 1 1844 PHE 1844 1844 1844 PHE PHE A . n 
A 1 1845 TYR 1845 1845 1845 TYR TYR A . n 
A 1 1846 PHE 1846 1846 1846 PHE PHE A . n 
A 1 1847 ASP 1847 1847 1847 ASP ASP A . n 
A 1 1848 PRO 1848 1848 1848 PRO PRO A . n 
A 1 1849 LYS 1849 1849 1849 LYS LYS A . n 
A 1 1850 GLN 1850 1850 1850 GLN GLN A . n 
A 1 1851 THR 1851 1851 1851 THR THR A . n 
A 1 1852 ASP 1852 1852 1852 ASP ASP A . n 
A 1 1853 VAL 1853 1853 1853 VAL VAL A . n 
A 1 1854 LEU 1854 1854 1854 LEU LEU A . n 
A 1 1855 GLN 1855 1855 1855 GLN GLN A . n 
A 1 1856 GLN 1856 1856 1856 GLN GLN A . n 
A 1 1857 LEU 1857 1857 1857 LEU LEU A . n 
A 1 1858 SER 1858 1858 1858 SER SER A . n 
A 1 1859 ILE 1859 1859 1859 ILE ILE A . n 
A 1 1860 GLN 1860 1860 1860 GLN GLN A . n 
A 1 1861 MET 1861 1861 1861 MET MET A . n 
A 1 1862 ALA 1862 1862 1862 ALA ALA A . n 
A 1 1863 ASN 1863 1863 1863 ASN ASN A . n 
A 1 1864 ALA 1864 1864 1864 ALA ALA A . n 
A 1 1865 LYS 1865 1865 1865 LYS LYS A . n 
A 1 1866 PHE 1866 1866 1866 PHE PHE A . n 
A 1 1867 ASN 1867 1867 1867 ASN ASN A . n 
A 1 1868 TYR 1868 1868 1868 TYR TYR A . n 
A 1 1869 GLY 1869 1869 1869 GLY GLY A . n 
A 1 1870 PHE 1870 1870 1870 PHE PHE A . n 
A 1 1871 GLU 1871 1871 1871 GLU GLU A . n 
A 1 1872 TYR 1872 1872 1872 TYR TYR A . n 
A 1 1873 LEU 1873 1873 1873 LEU LEU A . n 
A 1 1874 GLY 1874 1874 1874 GLY GLY A . n 
A 1 1875 VAL 1875 1875 1875 VAL VAL A . n 
A 1 1876 GLN 1876 1876 1876 GLN GLN A . n 
A 1 1877 ASP 1877 1877 1877 ASP ASP A . n 
A 1 1878 LYS 1878 1878 1878 LYS LYS A . n 
A 1 1879 LEU 1879 1879 1879 LEU LEU A . n 
A 1 1880 VAL 1880 1880 1880 VAL VAL A . n 
A 1 1881 GLN 1881 1881 1881 GLN GLN A . n 
A 1 1882 THR 1882 1882 1882 THR THR A . n 
A 1 1883 PRO 1883 1883 1883 PRO PRO A . n 
A 1 1884 LEU 1884 1884 1884 LEU LEU A . n 
A 1 1885 THR 1885 1885 1885 THR THR A . n 
A 1 1886 ASP 1886 1886 1886 ASP ASP A . n 
A 1 1887 ARG 1887 1887 1887 ARG ARG A . n 
A 1 1888 CYS 1888 1888 1888 CYS CYS A . n 
A 1 1889 TYR 1889 1889 1889 TYR TYR A . n 
A 1 1890 LEU 1890 1890 1890 LEU LEU A . n 
A 1 1891 THR 1891 1891 1891 THR THR A . n 
A 1 1892 MET 1892 1892 1892 MET MET A . n 
A 1 1893 THR 1893 1893 1893 THR THR A . n 
A 1 1894 GLN 1894 1894 1894 GLN GLN A . n 
A 1 1895 ALA 1895 1895 1895 ALA ALA A . n 
A 1 1896 LEU 1896 1896 1896 LEU LEU A . n 
A 1 1897 GLU 1897 1897 1897 GLU GLU A . n 
A 1 1898 ALA 1898 1898 1898 ALA ALA A . n 
A 1 1899 ARG 1899 1899 1899 ARG ARG A . n 
A 1 1900 LEU 1900 1900 1900 LEU LEU A . n 
A 1 1901 GLY 1901 1901 1901 GLY GLY A . n 
A 1 1902 GLY 1902 1902 1902 GLY GLY A . n 
A 1 1903 SER 1903 1903 1903 SER SER A . n 
A 1 1904 PRO 1904 1904 1904 PRO PRO A . n 
A 1 1905 PHE 1905 1905 1905 PHE PHE A . n 
A 1 1906 GLY 1906 1906 1906 GLY GLY A . n 
A 1 1907 PRO 1907 1907 1907 PRO PRO A . n 
A 1 1908 ALA 1908 1908 1908 ALA ALA A . n 
A 1 1909 GLY 1909 1909 1909 GLY GLY A . n 
A 1 1910 THR 1910 1910 1910 THR THR A . n 
A 1 1911 GLY 1911 1911 1911 GLY GLY A . n 
A 1 1912 LYS 1912 1912 1912 LYS LYS A . n 
A 1 1913 THR 1913 1913 1913 THR THR A . n 
A 1 1914 GLU 1914 1914 1914 GLU GLU A . n 
A 1 1915 SER 1915 1915 1915 SER SER A . n 
A 1 1916 VAL 1916 1916 1916 VAL VAL A . n 
A 1 1917 LYS 1917 1917 1917 LYS LYS A . n 
A 1 1918 ALA 1918 1918 1918 ALA ALA A . n 
A 1 1919 LEU 1919 1919 1919 LEU LEU A . n 
A 1 1920 GLY 1920 1920 1920 GLY GLY A . n 
A 1 1921 HIS 1921 1921 1921 HIS HIS A . n 
A 1 1922 GLN 1922 1922 1922 GLN GLN A . n 
A 1 1923 LEU 1923 1923 1923 LEU LEU A . n 
A 1 1924 GLY 1924 1924 1924 GLY GLY A . n 
A 1 1925 ARG 1925 1925 1925 ARG ARG A . n 
A 1 1926 PHE 1926 1926 1926 PHE PHE A . n 
A 1 1927 VAL 1927 1927 1927 VAL VAL A . n 
A 1 1928 LEU 1928 1928 1928 LEU LEU A . n 
A 1 1929 VAL 1929 1929 1929 VAL VAL A . n 
A 1 1930 PHE 1930 1930 1930 PHE PHE A . n 
A 1 1931 ASN 1931 1931 1931 ASN ASN A . n 
A 1 1932 CYS 1932 1932 1932 CYS CYS A . n 
A 1 1933 ASP 1933 1933 1933 ASP ASP A . n 
A 1 1934 GLU 1934 1934 1934 GLU GLU A . n 
A 1 1935 THR 1935 1935 1935 THR THR A . n 
A 1 1936 PHE 1936 1936 1936 PHE PHE A . n 
A 1 1937 ASP 1937 1937 1937 ASP ASP A . n 
A 1 1938 PHE 1938 1938 1938 PHE PHE A . n 
A 1 1939 GLN 1939 1939 1939 GLN GLN A . n 
A 1 1940 ALA 1940 1940 1940 ALA ALA A . n 
A 1 1941 MET 1941 1941 1941 MET MET A . n 
A 1 1942 GLY 1942 1942 1942 GLY GLY A . n 
A 1 1943 ARG 1943 1943 1943 ARG ARG A . n 
A 1 1944 ILE 1944 1944 1944 ILE ILE A . n 
A 1 1945 PHE 1945 1945 1945 PHE PHE A . n 
A 1 1946 VAL 1946 1946 1946 VAL VAL A . n 
A 1 1947 GLY 1947 1947 1947 GLY GLY A . n 
A 1 1948 LEU 1948 1948 1948 LEU LEU A . n 
A 1 1949 CYS 1949 1949 1949 CYS CYS A . n 
A 1 1950 GLN 1950 1950 1950 GLN GLN A . n 
A 1 1951 VAL 1951 1951 1951 VAL VAL A . n 
A 1 1952 GLY 1952 1952 1952 GLY GLY A . n 
A 1 1953 ALA 1953 1953 1953 ALA ALA A . n 
A 1 1954 TRP 1954 1954 1954 TRP TRP A . n 
A 1 1955 GLY 1955 1955 1955 GLY GLY A . n 
A 1 1956 CYS 1956 1956 1956 CYS CYS A . n 
A 1 1957 PHE 1957 1957 1957 PHE PHE A . n 
A 1 1958 ASP 1958 1958 1958 ASP ASP A . n 
A 1 1959 GLU 1959 1959 1959 GLU GLU A . n 
A 1 1960 PHE 1960 1960 1960 PHE PHE A . n 
A 1 1961 ASN 1961 1961 1961 ASN ASN A . n 
A 1 1962 ARG 1962 1962 1962 ARG ARG A . n 
A 1 1963 LEU 1963 1963 1963 LEU LEU A . n 
A 1 1964 GLU 1964 1964 1964 GLU GLU A . n 
A 1 1965 GLU 1965 1965 1965 GLU GLU A . n 
A 1 1966 ARG 1966 1966 1966 ARG ARG A . n 
A 1 1967 MET 1967 1967 1967 MET MET A . n 
A 1 1968 LEU 1968 1968 1968 LEU LEU A . n 
A 1 1969 SER 1969 1969 1969 SER SER A . n 
A 1 1970 ALA 1970 1970 1970 ALA ALA A . n 
A 1 1971 VAL 1971 1971 1971 VAL VAL A . n 
A 1 1972 SER 1972 1972 1972 SER SER A . n 
A 1 1973 GLN 1973 1973 1973 GLN GLN A . n 
A 1 1974 GLN 1974 1974 1974 GLN GLN A . n 
A 1 1975 VAL 1975 1975 1975 VAL VAL A . n 
A 1 1976 GLN 1976 1976 1976 GLN GLN A . n 
A 1 1977 CYS 1977 1977 1977 CYS CYS A . n 
A 1 1978 ILE 1978 1978 1978 ILE ILE A . n 
A 1 1979 GLN 1979 1979 1979 GLN GLN A . n 
A 1 1980 GLU 1980 1980 1980 GLU GLU A . n 
A 1 1981 ALA 1981 1981 1981 ALA ALA A . n 
A 1 1982 LEU 1982 1982 1982 LEU LEU A . n 
A 1 1983 ARG 1983 1983 1983 ARG ARG A . n 
A 1 1984 GLU 1984 1984 1984 GLU GLU A . n 
A 1 1985 HIS 1985 1985 1985 HIS HIS A . n 
A 1 1986 SER 1986 1986 1986 SER SER A . n 
A 1 1987 ASN 1987 1987 1987 ASN ASN A . n 
A 1 1988 PRO 1988 1988 1988 PRO PRO A . n 
A 1 1989 ASN 1989 1989 1989 ASN ASN A . n 
A 1 1990 TYR 1990 1990 1990 TYR TYR A . n 
A 1 1991 ASP 1991 1991 1991 ASP ASP A . n 
A 1 1992 LYS 1992 1992 1992 LYS LYS A . n 
A 1 1993 THR 1993 1993 1993 THR THR A . n 
A 1 1994 SER 1994 1994 1994 SER SER A . n 
A 1 1995 ALA 1995 1995 1995 ALA ALA A . n 
A 1 1996 PRO 1996 1996 1996 PRO PRO A . n 
A 1 1997 ILE 1997 1997 1997 ILE ILE A . n 
A 1 1998 THR 1998 1998 1998 THR THR A . n 
A 1 1999 CYS 1999 1999 1999 CYS CYS A . n 
A 1 2000 GLU 2000 2000 2000 GLU GLU A . n 
A 1 2001 LEU 2001 2001 2001 LEU LEU A . n 
A 1 2002 LEU 2002 2002 2002 LEU LEU A . n 
A 1 2003 ASN 2003 2003 2003 ASN ASN A . n 
A 1 2004 LYS 2004 2004 2004 LYS LYS A . n 
A 1 2005 GLN 2005 2005 2005 GLN GLN A . n 
A 1 2006 VAL 2006 2006 2006 VAL VAL A . n 
A 1 2007 LYS 2007 2007 2007 LYS LYS A . n 
A 1 2008 VAL 2008 2008 2008 VAL VAL A . n 
A 1 2009 SER 2009 2009 2009 SER SER A . n 
A 1 2010 PRO 2010 2010 2010 PRO PRO A . n 
A 1 2011 ASP 2011 2011 2011 ASP ASP A . n 
A 1 2012 MET 2012 2012 2012 MET MET A . n 
A 1 2013 ALA 2013 2013 2013 ALA ALA A . n 
A 1 2014 ILE 2014 2014 2014 ILE ILE A . n 
A 1 2015 PHE 2015 2015 2015 PHE PHE A . n 
A 1 2016 ILE 2016 2016 2016 ILE ILE A . n 
A 1 2017 THR 2017 2017 2017 THR THR A . n 
A 1 2018 MET 2018 2018 2018 MET MET A . n 
A 1 2019 ASN 2019 2019 2019 ASN ASN A . n 
A 1 2020 PRO 2020 2020 2020 PRO PRO A . n 
A 1 2021 GLY 2021 2021 2021 GLY GLY A . n 
A 1 2022 TYR 2022 2022 2022 TYR TYR A . n 
A 1 2023 ALA 2023 2023 2023 ALA ALA A . n 
A 1 2024 GLY 2024 2024 2024 GLY GLY A . n 
A 1 2025 ARG 2025 2025 2025 ARG ARG A . n 
A 1 2026 SER 2026 2026 2026 SER SER A . n 
A 1 2027 ASN 2027 2027 2027 ASN ASN A . n 
A 1 2028 LEU 2028 2028 2028 LEU LEU A . n 
A 1 2029 PRO 2029 2029 2029 PRO PRO A . n 
A 1 2030 ASP 2030 2030 2030 ASP ASP A . n 
A 1 2031 ASN 2031 2031 2031 ASN ASN A . n 
A 1 2032 LEU 2032 2032 2032 LEU LEU A . n 
A 1 2033 LYS 2033 2033 2033 LYS LYS A . n 
A 1 2034 LYS 2034 2034 2034 LYS LYS A . n 
A 1 2035 LEU 2035 2035 2035 LEU LEU A . n 
A 1 2036 PHE 2036 2036 2036 PHE PHE A . n 
A 1 2037 ARG 2037 2037 2037 ARG ARG A . n 
A 1 2038 SER 2038 2038 2038 SER SER A . n 
A 1 2039 LEU 2039 2039 2039 LEU LEU A . n 
A 1 2040 ALA 2040 2040 2040 ALA ALA A . n 
A 1 2041 MET 2041 2041 2041 MET MET A . n 
A 1 2042 THR 2042 2042 2042 THR THR A . n 
A 1 2043 LYS 2043 2043 2043 LYS LYS A . n 
A 1 2044 PRO 2044 2044 2044 PRO PRO A . n 
A 1 2045 ASP 2045 2045 2045 ASP ASP A . n 
A 1 2046 ARG 2046 2046 2046 ARG ARG A . n 
A 1 2047 GLN 2047 2047 2047 GLN GLN A . n 
A 1 2048 LEU 2048 2048 2048 LEU LEU A . n 
A 1 2049 ILE 2049 2049 2049 ILE ILE A . n 
A 1 2050 ALA 2050 2050 2050 ALA ALA A . n 
A 1 2051 GLN 2051 2051 2051 GLN GLN A . n 
A 1 2052 VAL 2052 2052 2052 VAL VAL A . n 
A 1 2053 MET 2053 2053 2053 MET MET A . n 
A 1 2054 LEU 2054 2054 2054 LEU LEU A . n 
A 1 2055 TYR 2055 2055 2055 TYR TYR A . n 
A 1 2056 SER 2056 2056 2056 SER SER A . n 
A 1 2057 GLN 2057 2057 2057 GLN GLN A . n 
A 1 2058 GLY 2058 2058 2058 GLY GLY A . n 
A 1 2059 PHE 2059 2059 2059 PHE PHE A . n 
A 1 2060 ARG 2060 2060 2060 ARG ARG A . n 
A 1 2061 THR 2061 2061 2061 THR THR A . n 
A 1 2062 ALA 2062 2062 2062 ALA ALA A . n 
A 1 2063 GLU 2063 2063 2063 GLU GLU A . n 
A 1 2064 VAL 2064 2064 2064 VAL VAL A . n 
A 1 2065 LEU 2065 2065 2065 LEU LEU A . n 
A 1 2066 ALA 2066 2066 2066 ALA ALA A . n 
A 1 2067 ASN 2067 2067 2067 ASN ASN A . n 
A 1 2068 LYS 2068 2068 2068 LYS LYS A . n 
A 1 2069 ILE 2069 2069 2069 ILE ILE A . n 
A 1 2070 VAL 2070 2070 2070 VAL VAL A . n 
A 1 2071 PRO 2071 2071 2071 PRO PRO A . n 
A 1 2072 PHE 2072 2072 2072 PHE PHE A . n 
A 1 2073 PHE 2073 2073 2073 PHE PHE A . n 
A 1 2074 LYS 2074 2074 2074 LYS LYS A . n 
A 1 2075 LEU 2075 2075 2075 LEU LEU A . n 
A 1 2076 CYS 2076 2076 2076 CYS CYS A . n 
A 1 2077 ASP 2077 2077 2077 ASP ASP A . n 
A 1 2078 GLU 2078 2078 2078 GLU GLU A . n 
A 1 2079 GLN 2079 2079 2079 GLN GLN A . n 
A 1 2080 LEU 2080 2080 2080 LEU LEU A . n 
A 1 2081 SER 2081 2081 2081 SER SER A . n 
A 1 2082 SER 2082 2082 2082 SER SER A . n 
A 1 2083 GLN 2083 2083 2083 GLN GLN A . n 
A 1 2084 SER 2084 2084 2084 SER SER A . n 
A 1 2085 HIS 2085 2085 2085 HIS HIS A . n 
A 1 2086 TYR 2086 2086 2086 TYR TYR A . n 
A 1 2087 ASP 2087 2087 2087 ASP ASP A . n 
A 1 2088 PHE 2088 2088 2088 PHE PHE A . n 
A 1 2089 GLY 2089 2089 2089 GLY GLY A . n 
A 1 2090 LEU 2090 2090 2090 LEU LEU A . n 
A 1 2091 ARG 2091 2091 2091 ARG ARG A . n 
A 1 2092 ALA 2092 2092 2092 ALA ALA A . n 
A 1 2093 LEU 2093 2093 2093 LEU LEU A . n 
A 1 2094 LYS 2094 2094 2094 LYS LYS A . n 
A 1 2095 SER 2095 2095 2095 SER SER A . n 
A 1 2096 VAL 2096 2096 2096 VAL VAL A . n 
A 1 2097 LEU 2097 2097 2097 LEU LEU A . n 
A 1 2098 VAL 2098 2098 2098 VAL VAL A . n 
A 1 2099 SER 2099 2099 2099 SER SER A . n 
A 1 2100 ALA 2100 2100 2100 ALA ALA A . n 
A 1 2101 GLY 2101 2101 2101 GLY GLY A . n 
A 1 2102 ASN 2102 2102 2102 ASN ASN A . n 
A 1 2103 VAL 2103 2103 2103 VAL VAL A . n 
A 1 2104 LYS 2104 2104 2104 LYS LYS A . n 
A 1 2105 ARG 2105 2105 2105 ARG ARG A . n 
A 1 2106 GLU 2106 2106 2106 GLU GLU A . n 
A 1 2107 ARG 2107 2107 2107 ARG ARG A . n 
A 1 2108 ILE 2108 2108 2108 ILE ILE A . n 
A 1 2109 GLN 2109 2109 2109 GLN GLN A . n 
A 1 2110 LYS 2110 2110 2110 LYS LYS A . n 
A 1 2111 ILE 2111 2111 2111 ILE ILE A . n 
A 1 2112 LYS 2112 2112 2112 LYS LYS A . n 
A 1 2113 ARG 2113 2113 2113 ARG ARG A . n 
A 1 2114 GLU 2114 2114 2114 GLU GLU A . n 
A 1 2115 LYS 2115 2115 2115 LYS LYS A . n 
A 1 2116 GLU 2116 2116 2116 GLU GLU A . n 
A 1 2117 GLU 2117 2117 2117 GLU GLU A . n 
A 1 2118 ARG 2118 2118 2118 ARG ARG A . n 
A 1 2119 GLY 2119 2119 2119 GLY GLY A . n 
A 1 2120 GLU 2120 2120 2120 GLU GLU A . n 
A 1 2121 ALA 2121 2121 2121 ALA ALA A . n 
A 1 2122 VAL 2122 2122 2122 VAL VAL A . n 
A 1 2123 ASP 2123 2123 2123 ASP ASP A . n 
A 1 2124 GLU 2124 2124 2124 GLU GLU A . n 
A 1 2125 GLY 2125 2125 2125 GLY GLY A . n 
A 1 2126 GLU 2126 2126 2126 GLU GLU A . n 
A 1 2127 ILE 2127 2127 2127 ILE ILE A . n 
A 1 2128 ALA 2128 2128 2128 ALA ALA A . n 
A 1 2129 GLU 2129 2129 2129 GLU GLU A . n 
A 1 2130 ASN 2130 2130 2130 ASN ASN A . n 
A 1 2131 LEU 2131 2131 2131 LEU LEU A . n 
A 1 2132 PRO 2132 2132 2132 PRO PRO A . n 
A 1 2133 GLU 2133 2133 2133 GLU GLU A . n 
A 1 2134 GLN 2134 2134 2134 GLN GLN A . n 
A 1 2135 GLU 2135 2135 2135 GLU GLU A . n 
A 1 2136 ILE 2136 2136 2136 ILE ILE A . n 
A 1 2137 LEU 2137 2137 2137 LEU LEU A . n 
A 1 2138 ILE 2138 2138 2138 ILE ILE A . n 
A 1 2139 GLN 2139 2139 2139 GLN GLN A . n 
A 1 2140 SER 2140 2140 2140 SER SER A . n 
A 1 2141 VAL 2141 2141 2141 VAL VAL A . n 
A 1 2142 CYS 2142 2142 2142 CYS CYS A . n 
A 1 2143 GLU 2143 2143 2143 GLU GLU A . n 
A 1 2144 THR 2144 2144 2144 THR THR A . n 
A 1 2145 MET 2145 2145 2145 MET MET A . n 
A 1 2146 VAL 2146 2146 2146 VAL VAL A . n 
A 1 2147 PRO 2147 2147 2147 PRO PRO A . n 
A 1 2148 LYS 2148 2148 2148 LYS LYS A . n 
A 1 2149 LEU 2149 2149 2149 LEU LEU A . n 
A 1 2150 VAL 2150 2150 2150 VAL VAL A . n 
A 1 2151 ALA 2151 2151 2151 ALA ALA A . n 
A 1 2152 GLU 2152 2152 2152 GLU GLU A . n 
A 1 2153 ASP 2153 2153 2153 ASP ASP A . n 
A 1 2154 ILE 2154 2154 2154 ILE ILE A . n 
A 1 2155 PRO 2155 2155 2155 PRO PRO A . n 
A 1 2156 LEU 2156 2156 2156 LEU LEU A . n 
A 1 2157 LEU 2157 2157 2157 LEU LEU A . n 
A 1 2158 PHE 2158 2158 2158 PHE PHE A . n 
A 1 2159 SER 2159 2159 2159 SER SER A . n 
A 1 2160 LEU 2160 2160 2160 LEU LEU A . n 
A 1 2161 LEU 2161 2161 2161 LEU LEU A . n 
A 1 2162 SER 2162 2162 2162 SER SER A . n 
A 1 2163 ASP 2163 2163 2163 ASP ASP A . n 
A 1 2164 VAL 2164 2164 2164 VAL VAL A . n 
A 1 2165 PHE 2165 2165 2165 PHE PHE A . n 
A 1 2166 PRO 2166 2166 2166 PRO PRO A . n 
A 1 2167 GLY 2167 2167 2167 GLY GLY A . n 
A 1 2168 VAL 2168 2168 2168 VAL VAL A . n 
A 1 2169 GLN 2169 2169 2169 GLN GLN A . n 
A 1 2170 TYR 2170 2170 2170 TYR TYR A . n 
A 1 2171 HIS 2171 2171 2171 HIS HIS A . n 
A 1 2172 ARG 2172 2172 2172 ARG ARG A . n 
A 1 2173 GLY 2173 2173 2173 GLY GLY A . n 
A 1 2174 GLU 2174 2174 2174 GLU GLU A . n 
A 1 2175 MET 2175 2175 2175 MET MET A . n 
A 1 2176 THR 2176 2176 2176 THR THR A . n 
A 1 2177 ALA 2177 2177 2177 ALA ALA A . n 
A 1 2178 LEU 2178 2178 2178 LEU LEU A . n 
A 1 2179 ARG 2179 2179 2179 ARG ARG A . n 
A 1 2180 GLU 2180 2180 2180 GLU GLU A . n 
A 1 2181 GLU 2181 2181 2181 GLU GLU A . n 
A 1 2182 LEU 2182 2182 2182 LEU LEU A . n 
A 1 2183 LYS 2183 2183 2183 LYS LYS A . n 
A 1 2184 LYS 2184 2184 2184 LYS LYS A . n 
A 1 2185 VAL 2185 2185 2185 VAL VAL A . n 
A 1 2186 CYS 2186 2186 2186 CYS CYS A . n 
A 1 2187 GLN 2187 2187 2187 GLN GLN A . n 
A 1 2188 GLU 2188 2188 2188 GLU GLU A . n 
A 1 2189 MET 2189 2189 2189 MET MET A . n 
A 1 2190 TYR 2190 2190 2190 TYR TYR A . n 
A 1 2191 LEU 2191 2191 2191 LEU LEU A . n 
A 1 2192 THR 2192 2192 2192 THR THR A . n 
A 1 2193 TYR 2193 2193 2193 TYR TYR A . n 
A 1 2194 GLY 2194 2194 2194 GLY GLY A . n 
A 1 2195 ASP 2195 2195 2195 ASP ASP A . n 
A 1 2196 GLY 2196 2196 2196 GLY GLY A . n 
A 1 2197 GLU 2197 2197 2197 GLU GLU A . n 
A 1 2198 GLU 2198 2198 2198 GLU GLU A . n 
A 1 2199 VAL 2199 2199 2199 VAL VAL A . n 
A 1 2200 GLY 2200 2200 2200 GLY GLY A . n 
A 1 2201 GLY 2201 2201 2201 GLY GLY A . n 
A 1 2202 MET 2202 2202 2202 MET MET A . n 
A 1 2203 TRP 2203 2203 2203 TRP TRP A . n 
A 1 2204 VAL 2204 2204 2204 VAL VAL A . n 
A 1 2205 GLU 2205 2205 2205 GLU GLU A . n 
A 1 2206 LYS 2206 2206 2206 LYS LYS A . n 
A 1 2207 VAL 2207 2207 2207 VAL VAL A . n 
A 1 2208 LEU 2208 2208 2208 LEU LEU A . n 
A 1 2209 GLN 2209 2209 2209 GLN GLN A . n 
A 1 2210 LEU 2210 2210 2210 LEU LEU A . n 
A 1 2211 TYR 2211 2211 2211 TYR TYR A . n 
A 1 2212 GLN 2212 2212 2212 GLN GLN A . n 
A 1 2213 ILE 2213 2213 2213 ILE ILE A . n 
A 1 2214 THR 2214 2214 2214 THR THR A . n 
A 1 2215 GLN 2215 2215 2215 GLN GLN A . n 
A 1 2216 ILE 2216 2216 2216 ILE ILE A . n 
A 1 2217 ASN 2217 2217 2217 ASN ASN A . n 
A 1 2218 HIS 2218 2218 2218 HIS HIS A . n 
A 1 2219 GLY 2219 2219 2219 GLY GLY A . n 
A 1 2220 LEU 2220 2220 2220 LEU LEU A . n 
A 1 2221 MET 2221 2221 2221 MET MET A . n 
A 1 2222 MET 2222 2222 2222 MET MET A . n 
A 1 2223 VAL 2223 2223 2223 VAL VAL A . n 
A 1 2224 GLY 2224 2224 2224 GLY GLY A . n 
A 1 2225 PRO 2225 2225 2225 PRO PRO A . n 
A 1 2226 SER 2226 2226 2226 SER SER A . n 
A 1 2227 GLY 2227 2227 2227 GLY GLY A . n 
A 1 2228 SER 2228 2228 2228 SER SER A . n 
A 1 2229 GLY 2229 2229 2229 GLY GLY A . n 
A 1 2230 LYS 2230 2230 2230 LYS LYS A . n 
A 1 2231 SER 2231 2231 2231 SER SER A . n 
A 1 2232 MET 2232 2232 2232 MET MET A . n 
A 1 2233 ALA 2233 2233 2233 ALA ALA A . n 
A 1 2234 TRP 2234 2234 2234 TRP TRP A . n 
A 1 2235 ARG 2235 2235 2235 ARG ARG A . n 
A 1 2236 VAL 2236 2236 2236 VAL VAL A . n 
A 1 2237 LEU 2237 2237 2237 LEU LEU A . n 
A 1 2238 LEU 2238 2238 2238 LEU LEU A . n 
A 1 2239 LYS 2239 2239 2239 LYS LYS A . n 
A 1 2240 ALA 2240 2240 2240 ALA ALA A . n 
A 1 2241 LEU 2241 2241 2241 LEU LEU A . n 
A 1 2242 GLU 2242 2242 2242 GLU GLU A . n 
A 1 2243 ARG 2243 2243 2243 ARG ARG A . n 
A 1 2244 LEU 2244 2244 2244 LEU LEU A . n 
A 1 2245 GLU 2245 2245 2245 GLU GLU A . n 
A 1 2246 GLY 2246 2246 2246 GLY GLY A . n 
A 1 2247 VAL 2247 2247 2247 VAL VAL A . n 
A 1 2248 GLU 2248 2248 2248 GLU GLU A . n 
A 1 2249 GLY 2249 2249 2249 GLY GLY A . n 
A 1 2250 VAL 2250 2250 2250 VAL VAL A . n 
A 1 2251 ALA 2251 2251 2251 ALA ALA A . n 
A 1 2252 HIS 2252 2252 2252 HIS HIS A . n 
A 1 2253 ILE 2253 2253 2253 ILE ILE A . n 
A 1 2254 ILE 2254 2254 2254 ILE ILE A . n 
A 1 2255 ASP 2255 2255 2255 ASP ASP A . n 
A 1 2256 PRO 2256 2256 2256 PRO PRO A . n 
A 1 2257 LYS 2257 2257 2257 LYS LYS A . n 
A 1 2258 ALA 2258 2258 2258 ALA ALA A . n 
A 1 2259 ILE 2259 2259 2259 ILE ILE A . n 
A 1 2260 SER 2260 2260 2260 SER SER A . n 
A 1 2261 LYS 2261 2261 2261 LYS LYS A . n 
A 1 2262 ASP 2262 2262 2262 ASP ASP A . n 
A 1 2263 HIS 2263 2263 2263 HIS HIS A . n 
A 1 2264 LEU 2264 2264 2264 LEU LEU A . n 
A 1 2265 TYR 2265 2265 2265 TYR TYR A . n 
A 1 2266 GLY 2266 2266 2266 GLY GLY A . n 
A 1 2267 THR 2267 2267 2267 THR THR A . n 
A 1 2268 LEU 2268 2268 2268 LEU LEU A . n 
A 1 2269 ASP 2269 2269 2269 ASP ASP A . n 
A 1 2270 PRO 2270 2270 2270 PRO PRO A . n 
A 1 2271 ASN 2271 2271 2271 ASN ASN A . n 
A 1 2272 THR 2272 2272 2272 THR THR A . n 
A 1 2273 ARG 2273 2273 2273 ARG ARG A . n 
A 1 2274 GLU 2274 2274 2274 GLU GLU A . n 
A 1 2275 TRP 2275 2275 2275 TRP TRP A . n 
A 1 2276 THR 2276 2276 2276 THR THR A . n 
A 1 2277 ASP 2277 2277 2277 ASP ASP A . n 
A 1 2278 GLY 2278 2278 2278 GLY GLY A . n 
A 1 2279 LEU 2279 2279 2279 LEU LEU A . n 
A 1 2280 PHE 2280 2280 2280 PHE PHE A . n 
A 1 2281 THR 2281 2281 2281 THR THR A . n 
A 1 2282 HIS 2282 2282 2282 HIS HIS A . n 
A 1 2283 VAL 2283 2283 2283 VAL VAL A . n 
A 1 2284 LEU 2284 2284 2284 LEU LEU A . n 
A 1 2285 ARG 2285 2285 2285 ARG ARG A . n 
A 1 2286 LYS 2286 2286 2286 LYS LYS A . n 
A 1 2287 ILE 2287 2287 2287 ILE ILE A . n 
A 1 2288 ILE 2288 2288 2288 ILE ILE A . n 
A 1 2289 ASP 2289 2289 2289 ASP ASP A . n 
A 1 2290 SER 2290 2290 2290 SER SER A . n 
A 1 2291 VAL 2291 2291 2291 VAL VAL A . n 
A 1 2292 ARG 2292 2292 2292 ARG ARG A . n 
A 1 2293 GLY 2293 2293 2293 GLY GLY A . n 
A 1 2294 GLU 2294 2294 2294 GLU GLU A . n 
A 1 2295 LEU 2295 2295 2295 LEU LEU A . n 
A 1 2296 GLN 2296 2296 2296 GLN GLN A . n 
A 1 2297 LYS 2297 2297 2297 LYS LYS A . n 
A 1 2298 ARG 2298 2298 2298 ARG ARG A . n 
A 1 2299 GLN 2299 2299 2299 GLN GLN A . n 
A 1 2300 TRP 2300 2300 2300 TRP TRP A . n 
A 1 2301 ILE 2301 2301 2301 ILE ILE A . n 
A 1 2302 VAL 2302 2302 2302 VAL VAL A . n 
A 1 2303 PHE 2303 2303 2303 PHE PHE A . n 
A 1 2304 ASP 2304 2304 2304 ASP ASP A . n 
A 1 2305 GLY 2305 2305 2305 GLY GLY A . n 
A 1 2306 ASP 2306 2306 2306 ASP ASP A . n 
A 1 2307 VAL 2307 2307 2307 VAL VAL A . n 
A 1 2308 ASP 2308 2308 2308 ASP ASP A . n 
A 1 2309 PRO 2309 2309 2309 PRO PRO A . n 
A 1 2310 GLU 2310 2310 2310 GLU GLU A . n 
A 1 2311 TRP 2311 2311 2311 TRP TRP A . n 
A 1 2312 VAL 2312 2312 2312 VAL VAL A . n 
A 1 2313 GLU 2313 2313 2313 GLU GLU A . n 
A 1 2314 ASN 2314 2314 2314 ASN ASN A . n 
A 1 2315 LEU 2315 2315 2315 LEU LEU A . n 
A 1 2316 ASN 2316 2316 2316 ASN ASN A . n 
A 1 2317 SER 2317 2317 2317 SER SER A . n 
A 1 2318 VAL 2318 2318 2318 VAL VAL A . n 
A 1 2319 LEU 2319 2319 2319 LEU LEU A . n 
A 1 2320 ASP 2320 2320 2320 ASP ASP A . n 
A 1 2321 ASP 2321 2321 2321 ASP ASP A . n 
A 1 2322 ASN 2322 2322 2322 ASN ASN A . n 
A 1 2323 LYS 2323 2323 2323 LYS LYS A . n 
A 1 2324 LEU 2324 2324 2324 LEU LEU A . n 
A 1 2325 LEU 2325 2325 2325 LEU LEU A . n 
A 1 2326 THR 2326 2326 2326 THR THR A . n 
A 1 2327 LEU 2327 2327 2327 LEU LEU A . n 
A 1 2328 PRO 2328 2328 2328 PRO PRO A . n 
A 1 2329 ASN 2329 2329 2329 ASN ASN A . n 
A 1 2330 GLY 2330 2330 2330 GLY GLY A . n 
A 1 2331 GLU 2331 2331 2331 GLU GLU A . n 
A 1 2332 ARG 2332 2332 2332 ARG ARG A . n 
A 1 2333 LEU 2333 2333 2333 LEU LEU A . n 
A 1 2334 SER 2334 2334 2334 SER SER A . n 
A 1 2335 LEU 2335 2335 2335 LEU LEU A . n 
A 1 2336 PRO 2336 2336 2336 PRO PRO A . n 
A 1 2337 PRO 2337 2337 2337 PRO PRO A . n 
A 1 2338 ASN 2338 2338 2338 ASN ASN A . n 
A 1 2339 VAL 2339 2339 2339 VAL VAL A . n 
A 1 2340 ARG 2340 2340 2340 ARG ARG A . n 
A 1 2341 ILE 2341 2341 2341 ILE ILE A . n 
A 1 2342 MET 2342 2342 2342 MET MET A . n 
A 1 2343 PHE 2343 2343 2343 PHE PHE A . n 
A 1 2344 GLU 2344 2344 2344 GLU GLU A . n 
A 1 2345 VAL 2345 2345 2345 VAL VAL A . n 
A 1 2346 GLN 2346 2346 2346 GLN GLN A . n 
A 1 2347 ASP 2347 2347 2347 ASP ASP A . n 
A 1 2348 LEU 2348 2348 2348 LEU LEU A . n 
A 1 2349 LYS 2349 2349 2349 LYS LYS A . n 
A 1 2350 TYR 2350 2350 2350 TYR TYR A . n 
A 1 2351 ALA 2351 2351 2351 ALA ALA A . n 
A 1 2352 THR 2352 2352 2352 THR THR A . n 
A 1 2353 LEU 2353 2353 2353 LEU LEU A . n 
A 1 2354 ALA 2354 2354 2354 ALA ALA A . n 
A 1 2355 THR 2355 2355 2355 THR THR A . n 
A 1 2356 VAL 2356 2356 2356 VAL VAL A . n 
A 1 2357 SER 2357 2357 2357 SER SER A . n 
A 1 2358 ARG 2358 2358 2358 ARG ARG A . n 
A 1 2359 CYS 2359 2359 2359 CYS CYS A . n 
A 1 2360 GLY 2360 2360 2360 GLY GLY A . n 
A 1 2361 MET 2361 2361 2361 MET MET A . n 
A 1 2362 VAL 2362 2362 2362 VAL VAL A . n 
A 1 2363 TRP 2363 2363 2363 TRP TRP A . n 
A 1 2364 PHE 2364 2364 2364 PHE PHE A . n 
A 1 2365 SER 2365 2365 2365 SER SER A . n 
A 1 2366 GLU 2366 2366 2366 GLU GLU A . n 
A 1 2367 ASP 2367 2367 2367 ASP ASP A . n 
A 1 2368 VAL 2368 2368 2368 VAL VAL A . n 
A 1 2369 LEU 2369 2369 2369 LEU LEU A . n 
A 1 2370 SER 2370 2370 2370 SER SER A . n 
A 1 2371 THR 2371 2371 2371 THR THR A . n 
A 1 2372 ASP 2372 2372 2372 ASP ASP A . n 
A 1 2373 MET 2373 2373 2373 MET MET A . n 
A 1 2374 ILE 2374 2374 2374 ILE ILE A . n 
A 1 2375 PHE 2375 2375 2375 PHE PHE A . n 
A 1 2376 ASN 2376 2376 2376 ASN ASN A . n 
A 1 2377 ASN 2377 2377 2377 ASN ASN A . n 
A 1 2378 PHE 2378 2378 2378 PHE PHE A . n 
A 1 2379 LEU 2379 2379 2379 LEU LEU A . n 
A 1 2380 ALA 2380 2380 2380 ALA ALA A . n 
A 1 2381 ARG 2381 2381 2381 ARG ARG A . n 
A 1 2382 LEU 2382 2382 2382 LEU LEU A . n 
A 1 2383 ARG 2383 2383 2383 ARG ARG A . n 
A 1 2384 SER 2384 2384 2384 SER SER A . n 
A 1 2385 ILE 2385 2385 2385 ILE ILE A . n 
A 1 2386 PRO 2386 2386 2386 PRO PRO A . n 
A 1 2387 LEU 2387 2387 2387 LEU LEU A . n 
A 1 2388 ASP 2388 2388 2388 ASP ASP A . n 
A 1 2389 GLU 2389 2389 2389 GLU GLU A . n 
A 1 2390 GLY 2390 2390 ?    ?   ?   A . n 
A 1 2391 GLU 2391 2391 ?    ?   ?   A . n 
A 1 2392 ASP 2392 2392 ?    ?   ?   A . n 
A 1 2393 GLU 2393 2393 ?    ?   ?   A . n 
A 1 2394 ALA 2394 2394 ?    ?   ?   A . n 
A 1 2395 GLN 2395 2395 ?    ?   ?   A . n 
A 1 2396 ARG 2396 2396 ?    ?   ?   A . n 
A 1 2397 ARG 2397 2397 ?    ?   ?   A . n 
A 1 2398 ARG 2398 2398 ?    ?   ?   A . n 
A 1 2399 LYS 2399 2399 ?    ?   ?   A . n 
A 1 2400 GLY 2400 2400 ?    ?   ?   A . n 
A 1 2401 LYS 2401 2401 ?    ?   ?   A . n 
A 1 2402 GLU 2402 2402 ?    ?   ?   A . n 
A 1 2403 ASP 2403 2403 ?    ?   ?   A . n 
A 1 2404 GLU 2404 2404 ?    ?   ?   A . n 
A 1 2405 GLY 2405 2405 ?    ?   ?   A . n 
A 1 2406 GLU 2406 2406 ?    ?   ?   A . n 
A 1 2407 GLU 2407 2407 ?    ?   ?   A . n 
A 1 2408 ALA 2408 2408 ?    ?   ?   A . n 
A 1 2409 ALA 2409 2409 ?    ?   ?   A . n 
A 1 2410 SER 2410 2410 2410 SER SER A . n 
A 1 2411 PRO 2411 2411 2411 PRO PRO A . n 
A 1 2412 MET 2412 2412 2412 MET MET A . n 
A 1 2413 LEU 2413 2413 2413 LEU LEU A . n 
A 1 2414 GLN 2414 2414 2414 GLN GLN A . n 
A 1 2415 ILE 2415 2415 2415 ILE ILE A . n 
A 1 2416 GLN 2416 2416 2416 GLN GLN A . n 
A 1 2417 ARG 2417 2417 2417 ARG ARG A . n 
A 1 2418 ASP 2418 2418 2418 ASP ASP A . n 
A 1 2419 ALA 2419 2419 2419 ALA ALA A . n 
A 1 2420 ALA 2420 2420 2420 ALA ALA A . n 
A 1 2421 THR 2421 2421 2421 THR THR A . n 
A 1 2422 ILE 2422 2422 2422 ILE ILE A . n 
A 1 2423 MET 2423 2423 2423 MET MET A . n 
A 1 2424 GLN 2424 2424 2424 GLN GLN A . n 
A 1 2425 PRO 2425 2425 2425 PRO PRO A . n 
A 1 2426 TYR 2426 2426 2426 TYR TYR A . n 
A 1 2427 PHE 2427 2427 2427 PHE PHE A . n 
A 1 2428 THR 2428 2428 2428 THR THR A . n 
A 1 2429 SER 2429 2429 2429 SER SER A . n 
A 1 2430 ASN 2430 2430 2430 ASN ASN A . n 
A 1 2431 GLY 2431 2431 2431 GLY GLY A . n 
A 1 2432 LEU 2432 2432 2432 LEU LEU A . n 
A 1 2433 VAL 2433 2433 2433 VAL VAL A . n 
A 1 2434 THR 2434 2434 2434 THR THR A . n 
A 1 2435 LYS 2435 2435 2435 LYS LYS A . n 
A 1 2436 ALA 2436 2436 2436 ALA ALA A . n 
A 1 2437 LEU 2437 2437 2437 LEU LEU A . n 
A 1 2438 GLU 2438 2438 2438 GLU GLU A . n 
A 1 2439 HIS 2439 2439 2439 HIS HIS A . n 
A 1 2440 ALA 2440 2440 2440 ALA ALA A . n 
A 1 2441 PHE 2441 2441 2441 PHE PHE A . n 
A 1 2442 GLN 2442 2442 2442 GLN GLN A . n 
A 1 2443 LEU 2443 2443 2443 LEU LEU A . n 
A 1 2444 GLU 2444 2444 2444 GLU GLU A . n 
A 1 2445 HIS 2445 2445 2445 HIS HIS A . n 
A 1 2446 ILE 2446 2446 2446 ILE ILE A . n 
A 1 2447 MET 2447 2447 2447 MET MET A . n 
A 1 2448 ASP 2448 2448 2448 ASP ASP A . n 
A 1 2449 LEU 2449 2449 2449 LEU LEU A . n 
A 1 2450 THR 2450 2450 2450 THR THR A . n 
A 1 2451 ARG 2451 2451 2451 ARG ARG A . n 
A 1 2452 LEU 2452 2452 2452 LEU LEU A . n 
A 1 2453 ARG 2453 2453 2453 ARG ARG A . n 
A 1 2454 CYS 2454 2454 2454 CYS CYS A . n 
A 1 2455 LEU 2455 2455 2455 LEU LEU A . n 
A 1 2456 GLY 2456 2456 2456 GLY GLY A . n 
A 1 2457 SER 2457 2457 2457 SER SER A . n 
A 1 2458 LEU 2458 2458 2458 LEU LEU A . n 
A 1 2459 PHE 2459 2459 2459 PHE PHE A . n 
A 1 2460 SER 2460 2460 2460 SER SER A . n 
A 1 2461 MET 2461 2461 2461 MET MET A . n 
A 1 2462 LEU 2462 2462 2462 LEU LEU A . n 
A 1 2463 HIS 2463 2463 2463 HIS HIS A . n 
A 1 2464 GLN 2464 2464 2464 GLN GLN A . n 
A 1 2465 ALA 2465 2465 2465 ALA ALA A . n 
A 1 2466 CYS 2466 2466 2466 CYS CYS A . n 
A 1 2467 ARG 2467 2467 2467 ARG ARG A . n 
A 1 2468 ASN 2468 2468 2468 ASN ASN A . n 
A 1 2469 VAL 2469 2469 2469 VAL VAL A . n 
A 1 2470 ALA 2470 2470 2470 ALA ALA A . n 
A 1 2471 GLN 2471 2471 2471 GLN GLN A . n 
A 1 2472 TYR 2472 2472 2472 TYR TYR A . n 
A 1 2473 ASN 2473 2473 2473 ASN ASN A . n 
A 1 2474 ALA 2474 2474 2474 ALA ALA A . n 
A 1 2475 ASN 2475 2475 2475 ASN ASN A . n 
A 1 2476 HIS 2476 2476 2476 HIS HIS A . n 
A 1 2477 PRO 2477 2477 2477 PRO PRO A . n 
A 1 2478 ASP 2478 2478 2478 ASP ASP A . n 
A 1 2479 PHE 2479 2479 2479 PHE PHE A . n 
A 1 2480 PRO 2480 2480 2480 PRO PRO A . n 
A 1 2481 MET 2481 2481 2481 MET MET A . n 
A 1 2482 GLN 2482 2482 2482 GLN GLN A . n 
A 1 2483 ILE 2483 2483 2483 ILE ILE A . n 
A 1 2484 GLU 2484 2484 2484 GLU GLU A . n 
A 1 2485 GLN 2485 2485 2485 GLN GLN A . n 
A 1 2486 LEU 2486 2486 2486 LEU LEU A . n 
A 1 2487 GLU 2487 2487 2487 GLU GLU A . n 
A 1 2488 ARG 2488 2488 2488 ARG ARG A . n 
A 1 2489 TYR 2489 2489 2489 TYR TYR A . n 
A 1 2490 ILE 2490 2490 2490 ILE ILE A . n 
A 1 2491 GLN 2491 2491 2491 GLN GLN A . n 
A 1 2492 ARG 2492 2492 2492 ARG ARG A . n 
A 1 2493 TYR 2493 2493 2493 TYR TYR A . n 
A 1 2494 LEU 2494 2494 2494 LEU LEU A . n 
A 1 2495 VAL 2495 2495 2495 VAL VAL A . n 
A 1 2496 TYR 2496 2496 2496 TYR TYR A . n 
A 1 2497 ALA 2497 2497 2497 ALA ALA A . n 
A 1 2498 ILE 2498 2498 2498 ILE ILE A . n 
A 1 2499 LEU 2499 2499 2499 LEU LEU A . n 
A 1 2500 TRP 2500 2500 2500 TRP TRP A . n 
A 1 2501 SER 2501 2501 2501 SER SER A . n 
A 1 2502 LEU 2502 2502 2502 LEU LEU A . n 
A 1 2503 SER 2503 2503 2503 SER SER A . n 
A 1 2504 GLY 2504 2504 2504 GLY GLY A . n 
A 1 2505 ASP 2505 2505 2505 ASP ASP A . n 
A 1 2506 SER 2506 2506 2506 SER SER A . n 
A 1 2507 ARG 2507 2507 2507 ARG ARG A . n 
A 1 2508 LEU 2508 2508 2508 LEU LEU A . n 
A 1 2509 LYS 2509 2509 2509 LYS LYS A . n 
A 1 2510 MET 2510 2510 2510 MET MET A . n 
A 1 2511 ARG 2511 2511 2511 ARG ARG A . n 
A 1 2512 ALA 2512 2512 2512 ALA ALA A . n 
A 1 2513 GLU 2513 2513 2513 GLU GLU A . n 
A 1 2514 LEU 2514 2514 2514 LEU LEU A . n 
A 1 2515 GLY 2515 2515 2515 GLY GLY A . n 
A 1 2516 GLU 2516 2516 2516 GLU GLU A . n 
A 1 2517 TYR 2517 2517 2517 TYR TYR A . n 
A 1 2518 ILE 2518 2518 2518 ILE ILE A . n 
A 1 2519 ARG 2519 2519 2519 ARG ARG A . n 
A 1 2520 ARG 2520 2520 2520 ARG ARG A . n 
A 1 2521 ILE 2521 2521 2521 ILE ILE A . n 
A 1 2522 THR 2522 2522 2522 THR THR A . n 
A 1 2523 THR 2523 2523 2523 THR THR A . n 
A 1 2524 VAL 2524 2524 2524 VAL VAL A . n 
A 1 2525 PRO 2525 2525 2525 PRO PRO A . n 
A 1 2526 LEU 2526 2526 2526 LEU LEU A . n 
A 1 2527 PRO 2527 2527 2527 PRO PRO A . n 
A 1 2528 THR 2528 2528 2528 THR THR A . n 
A 1 2529 ALA 2529 2529 2529 ALA ALA A . n 
A 1 2530 PRO 2530 2530 2530 PRO PRO A . n 
A 1 2531 ASN 2531 2531 2531 ASN ASN A . n 
A 1 2532 ILE 2532 2532 2532 ILE ILE A . n 
A 1 2533 PRO 2533 2533 2533 PRO PRO A . n 
A 1 2534 ILE 2534 2534 2534 ILE ILE A . n 
A 1 2535 ILE 2535 2535 2535 ILE ILE A . n 
A 1 2536 ASP 2536 2536 2536 ASP ASP A . n 
A 1 2537 TYR 2537 2537 2537 TYR TYR A . n 
A 1 2538 GLU 2538 2538 2538 GLU GLU A . n 
A 1 2539 VAL 2539 2539 2539 VAL VAL A . n 
A 1 2540 SER 2540 2540 2540 SER SER A . n 
A 1 2541 ILE 2541 2541 2541 ILE ILE A . n 
A 1 2542 SER 2542 2542 2542 SER SER A . n 
A 1 2543 GLY 2543 2543 2543 GLY GLY A . n 
A 1 2544 GLU 2544 2544 2544 GLU GLU A . n 
A 1 2545 TRP 2545 2545 2545 TRP TRP A . n 
A 1 2546 SER 2546 2546 2546 SER SER A . n 
A 1 2547 PRO 2547 2547 2547 PRO PRO A . n 
A 1 2548 TRP 2548 2548 2548 TRP TRP A . n 
A 1 2549 GLN 2549 2549 2549 GLN GLN A . n 
A 1 2550 ALA 2550 2550 2550 ALA ALA A . n 
A 1 2551 LYS 2551 2551 2551 LYS LYS A . n 
A 1 2552 VAL 2552 2552 2552 VAL VAL A . n 
A 1 2553 PRO 2553 2553 2553 PRO PRO A . n 
A 1 2554 GLN 2554 2554 2554 GLN GLN A . n 
A 1 2555 ILE 2555 2555 2555 ILE ILE A . n 
A 1 2556 GLU 2556 2556 2556 GLU GLU A . n 
A 1 2557 VAL 2557 2557 2557 VAL VAL A . n 
A 1 2558 GLU 2558 2558 2558 GLU GLU A . n 
A 1 2559 THR 2559 2559 2559 THR THR A . n 
A 1 2560 HIS 2560 2560 2560 HIS HIS A . n 
A 1 2561 LYS 2561 2561 2561 LYS LYS A . n 
A 1 2562 VAL 2562 2562 2562 VAL VAL A . n 
A 1 2563 ALA 2563 2563 2563 ALA ALA A . n 
A 1 2564 ALA 2564 2564 2564 ALA ALA A . n 
A 1 2565 PRO 2565 2565 2565 PRO PRO A . n 
A 1 2566 ASP 2566 2566 2566 ASP ASP A . n 
A 1 2567 VAL 2567 2567 2567 VAL VAL A . n 
A 1 2568 VAL 2568 2568 2568 VAL VAL A . n 
A 1 2569 VAL 2569 2569 2569 VAL VAL A . n 
A 1 2570 PRO 2570 2570 2570 PRO PRO A . n 
A 1 2571 THR 2571 2571 2571 THR THR A . n 
A 1 2572 LEU 2572 2572 2572 LEU LEU A . n 
A 1 2573 ASP 2573 2573 2573 ASP ASP A . n 
A 1 2574 THR 2574 2574 2574 THR THR A . n 
A 1 2575 VAL 2575 2575 2575 VAL VAL A . n 
A 1 2576 ARG 2576 2576 2576 ARG ARG A . n 
A 1 2577 HIS 2577 2577 2577 HIS HIS A . n 
A 1 2578 GLU 2578 2578 2578 GLU GLU A . n 
A 1 2579 ALA 2579 2579 2579 ALA ALA A . n 
A 1 2580 LEU 2580 2580 2580 LEU LEU A . n 
A 1 2581 LEU 2581 2581 2581 LEU LEU A . n 
A 1 2582 TYR 2582 2582 2582 TYR TYR A . n 
A 1 2583 THR 2583 2583 2583 THR THR A . n 
A 1 2584 TRP 2584 2584 2584 TRP TRP A . n 
A 1 2585 LEU 2585 2585 2585 LEU LEU A . n 
A 1 2586 ALA 2586 2586 2586 ALA ALA A . n 
A 1 2587 GLU 2587 2587 2587 GLU GLU A . n 
A 1 2588 HIS 2588 2588 2588 HIS HIS A . n 
A 1 2589 LYS 2589 2589 2589 LYS LYS A . n 
A 1 2590 PRO 2590 2590 2590 PRO PRO A . n 
A 1 2591 LEU 2591 2591 2591 LEU LEU A . n 
A 1 2592 VAL 2592 2592 2592 VAL VAL A . n 
A 1 2593 LEU 2593 2593 2593 LEU LEU A . n 
A 1 2594 CYS 2594 2594 2594 CYS CYS A . n 
A 1 2595 GLY 2595 2595 2595 GLY GLY A . n 
A 1 2596 PRO 2596 2596 2596 PRO PRO A . n 
A 1 2597 PRO 2597 2597 2597 PRO PRO A . n 
A 1 2598 GLY 2598 2598 2598 GLY GLY A . n 
A 1 2599 SER 2599 2599 2599 SER SER A . n 
A 1 2600 GLY 2600 2600 2600 GLY GLY A . n 
A 1 2601 LYS 2601 2601 2601 LYS LYS A . n 
A 1 2602 THR 2602 2602 2602 THR THR A . n 
A 1 2603 MET 2603 2603 2603 MET MET A . n 
A 1 2604 THR 2604 2604 2604 THR THR A . n 
A 1 2605 LEU 2605 2605 2605 LEU LEU A . n 
A 1 2606 PHE 2606 2606 2606 PHE PHE A . n 
A 1 2607 SER 2607 2607 2607 SER SER A . n 
A 1 2608 ALA 2608 2608 2608 ALA ALA A . n 
A 1 2609 LEU 2609 2609 2609 LEU LEU A . n 
A 1 2610 ARG 2610 2610 2610 ARG ARG A . n 
A 1 2611 ALA 2611 2611 2611 ALA ALA A . n 
A 1 2612 LEU 2612 2612 2612 LEU LEU A . n 
A 1 2613 PRO 2613 2613 2613 PRO PRO A . n 
A 1 2614 ASP 2614 2614 2614 ASP ASP A . n 
A 1 2615 MET 2615 2615 2615 MET MET A . n 
A 1 2616 GLU 2616 2616 2616 GLU GLU A . n 
A 1 2617 VAL 2617 2617 2617 VAL VAL A . n 
A 1 2618 VAL 2618 2618 2618 VAL VAL A . n 
A 1 2619 GLY 2619 2619 2619 GLY GLY A . n 
A 1 2620 LEU 2620 2620 2620 LEU LEU A . n 
A 1 2621 ASN 2621 2621 2621 ASN ASN A . n 
A 1 2622 PHE 2622 2622 2622 PHE PHE A . n 
A 1 2623 SER 2623 2623 2623 SER SER A . n 
A 1 2624 SER 2624 2624 2624 SER SER A . n 
A 1 2625 ALA 2625 2625 2625 ALA ALA A . n 
A 1 2626 THR 2626 2626 2626 THR THR A . n 
A 1 2627 THR 2627 2627 2627 THR THR A . n 
A 1 2628 PRO 2628 2628 2628 PRO PRO A . n 
A 1 2629 GLU 2629 2629 2629 GLU GLU A . n 
A 1 2630 LEU 2630 2630 2630 LEU LEU A . n 
A 1 2631 LEU 2631 2631 2631 LEU LEU A . n 
A 1 2632 LEU 2632 2632 2632 LEU LEU A . n 
A 1 2633 LYS 2633 2633 2633 LYS LYS A . n 
A 1 2634 THR 2634 2634 2634 THR THR A . n 
A 1 2635 PHE 2635 2635 2635 PHE PHE A . n 
A 1 2636 ASP 2636 2636 2636 ASP ASP A . n 
A 1 2637 HIS 2637 2637 2637 HIS HIS A . n 
A 1 2638 TYR 2638 2638 2638 TYR TYR A . n 
A 1 2639 CYS 2639 2639 2639 CYS CYS A . n 
A 1 2640 GLU 2640 2640 2640 GLU GLU A . n 
A 1 2641 TYR 2641 2641 2641 TYR TYR A . n 
A 1 2642 ARG 2642 2642 2642 ARG ARG A . n 
A 1 2643 ARG 2643 2643 2643 ARG ARG A . n 
A 1 2644 THR 2644 2644 2644 THR THR A . n 
A 1 2645 PRO 2645 2645 2645 PRO PRO A . n 
A 1 2646 ASN 2646 2646 2646 ASN ASN A . n 
A 1 2647 GLY 2647 2647 2647 GLY GLY A . n 
A 1 2648 VAL 2648 2648 2648 VAL VAL A . n 
A 1 2649 VAL 2649 2649 2649 VAL VAL A . n 
A 1 2650 LEU 2650 2650 2650 LEU LEU A . n 
A 1 2651 ALA 2651 2651 2651 ALA ALA A . n 
A 1 2652 PRO 2652 2652 2652 PRO PRO A . n 
A 1 2653 VAL 2653 2653 2653 VAL VAL A . n 
A 1 2654 GLN 2654 2654 2654 GLN GLN A . n 
A 1 2655 LEU 2655 2655 2655 LEU LEU A . n 
A 1 2656 GLY 2656 2656 2656 GLY GLY A . n 
A 1 2657 LYS 2657 2657 2657 LYS LYS A . n 
A 1 2658 TRP 2658 2658 2658 TRP TRP A . n 
A 1 2659 LEU 2659 2659 2659 LEU LEU A . n 
A 1 2660 VAL 2660 2660 2660 VAL VAL A . n 
A 1 2661 LEU 2661 2661 2661 LEU LEU A . n 
A 1 2662 PHE 2662 2662 2662 PHE PHE A . n 
A 1 2663 CYS 2663 2663 2663 CYS CYS A . n 
A 1 2664 ASP 2664 2664 2664 ASP ASP A . n 
A 1 2665 GLU 2665 2665 2665 GLU GLU A . n 
A 1 2666 ILE 2666 2666 2666 ILE ILE A . n 
A 1 2667 ASN 2667 2667 2667 ASN ASN A . n 
A 1 2668 LEU 2668 2668 2668 LEU LEU A . n 
A 1 2669 PRO 2669 2669 2669 PRO PRO A . n 
A 1 2670 ASP 2670 2670 2670 ASP ASP A . n 
A 1 2671 MET 2671 2671 2671 MET MET A . n 
A 1 2672 ASP 2672 2672 2672 ASP ASP A . n 
A 1 2673 LYS 2673 2673 2673 LYS LYS A . n 
A 1 2674 TYR 2674 2674 2674 TYR TYR A . n 
A 1 2675 GLY 2675 2675 2675 GLY GLY A . n 
A 1 2676 THR 2676 2676 2676 THR THR A . n 
A 1 2677 GLN 2677 2677 2677 GLN GLN A . n 
A 1 2678 ARG 2678 2678 2678 ARG ARG A . n 
A 1 2679 VAL 2679 2679 2679 VAL VAL A . n 
A 1 2680 ILE 2680 2680 2680 ILE ILE A . n 
A 1 2681 SER 2681 2681 2681 SER SER A . n 
A 1 2682 PHE 2682 2682 2682 PHE PHE A . n 
A 1 2683 ILE 2683 2683 2683 ILE ILE A . n 
A 1 2684 ARG 2684 2684 2684 ARG ARG A . n 
A 1 2685 GLN 2685 2685 2685 GLN GLN A . n 
A 1 2686 MET 2686 2686 2686 MET MET A . n 
A 1 2687 VAL 2687 2687 2687 VAL VAL A . n 
A 1 2688 GLU 2688 2688 2688 GLU GLU A . n 
A 1 2689 HIS 2689 2689 2689 HIS HIS A . n 
A 1 2690 GLY 2690 2690 2690 GLY GLY A . n 
A 1 2691 GLY 2691 2691 2691 GLY GLY A . n 
A 1 2692 PHE 2692 2692 2692 PHE PHE A . n 
A 1 2693 TYR 2693 2693 2693 TYR TYR A . n 
A 1 2694 ARG 2694 2694 2694 ARG ARG A . n 
A 1 2695 THR 2695 2695 2695 THR THR A . n 
A 1 2696 SER 2696 2696 2696 SER SER A . n 
A 1 2697 ASP 2697 2697 2697 ASP ASP A . n 
A 1 2698 GLN 2698 2698 2698 GLN GLN A . n 
A 1 2699 THR 2699 2699 2699 THR THR A . n 
A 1 2700 TRP 2700 2700 2700 TRP TRP A . n 
A 1 2701 VAL 2701 2701 2701 VAL VAL A . n 
A 1 2702 LYS 2702 2702 2702 LYS LYS A . n 
A 1 2703 LEU 2703 2703 2703 LEU LEU A . n 
A 1 2704 GLU 2704 2704 2704 GLU GLU A . n 
A 1 2705 ARG 2705 2705 2705 ARG ARG A . n 
A 1 2706 ILE 2706 2706 2706 ILE ILE A . n 
A 1 2707 GLN 2707 2707 2707 GLN GLN A . n 
A 1 2708 PHE 2708 2708 2708 PHE PHE A . n 
A 1 2709 VAL 2709 2709 2709 VAL VAL A . n 
A 1 2710 GLY 2710 2710 2710 GLY GLY A . n 
A 1 2711 ALA 2711 2711 2711 ALA ALA A . n 
A 1 2712 CYS 2712 2712 2712 CYS CYS A . n 
A 1 2713 ASN 2713 2713 2713 ASN ASN A . n 
A 1 2714 PRO 2714 2714 2714 PRO PRO A . n 
A 1 2715 PRO 2715 2715 2715 PRO PRO A . n 
A 1 2716 THR 2716 2716 2716 THR THR A . n 
A 1 2717 ASP 2717 2717 2717 ASP ASP A . n 
A 1 2718 PRO 2718 2718 2718 PRO PRO A . n 
A 1 2719 GLY 2719 2719 2719 GLY GLY A . n 
A 1 2720 ARG 2720 2720 2720 ARG ARG A . n 
A 1 2721 LYS 2721 2721 2721 LYS LYS A . n 
A 1 2722 PRO 2722 2722 2722 PRO PRO A . n 
A 1 2723 LEU 2723 2723 2723 LEU LEU A . n 
A 1 2724 SER 2724 2724 2724 SER SER A . n 
A 1 2725 HIS 2725 2725 2725 HIS HIS A . n 
A 1 2726 ARG 2726 2726 2726 ARG ARG A . n 
A 1 2727 PHE 2727 2727 2727 PHE PHE A . n 
A 1 2728 LEU 2728 2728 2728 LEU LEU A . n 
A 1 2729 ARG 2729 2729 2729 ARG ARG A . n 
A 1 2730 HIS 2730 2730 2730 HIS HIS A . n 
A 1 2731 VAL 2731 2731 2731 VAL VAL A . n 
A 1 2732 PRO 2732 2732 2732 PRO PRO A . n 
A 1 2733 VAL 2733 2733 2733 VAL VAL A . n 
A 1 2734 VAL 2734 2734 2734 VAL VAL A . n 
A 1 2735 TYR 2735 2735 2735 TYR TYR A . n 
A 1 2736 VAL 2736 2736 2736 VAL VAL A . n 
A 1 2737 ASP 2737 2737 2737 ASP ASP A . n 
A 1 2738 TYR 2738 2738 2738 TYR TYR A . n 
A 1 2739 PRO 2739 2739 2739 PRO PRO A . n 
A 1 2740 GLY 2740 2740 2740 GLY GLY A . n 
A 1 2741 PRO 2741 2741 2741 PRO PRO A . n 
A 1 2742 ALA 2742 2742 2742 ALA ALA A . n 
A 1 2743 SER 2743 2743 2743 SER SER A . n 
A 1 2744 LEU 2744 2744 2744 LEU LEU A . n 
A 1 2745 THR 2745 2745 2745 THR THR A . n 
A 1 2746 GLN 2746 2746 2746 GLN GLN A . n 
A 1 2747 ILE 2747 2747 2747 ILE ILE A . n 
A 1 2748 TYR 2748 2748 2748 TYR TYR A . n 
A 1 2749 GLY 2749 2749 2749 GLY GLY A . n 
A 1 2750 THR 2750 2750 2750 THR THR A . n 
A 1 2751 PHE 2751 2751 2751 PHE PHE A . n 
A 1 2752 ASN 2752 2752 2752 ASN ASN A . n 
A 1 2753 ARG 2753 2753 2753 ARG ARG A . n 
A 1 2754 ALA 2754 2754 2754 ALA ALA A . n 
A 1 2755 MET 2755 2755 2755 MET MET A . n 
A 1 2756 LEU 2756 2756 2756 LEU LEU A . n 
A 1 2757 ARG 2757 2757 2757 ARG ARG A . n 
A 1 2758 LEU 2758 2758 2758 LEU LEU A . n 
A 1 2759 ILE 2759 2759 2759 ILE ILE A . n 
A 1 2760 PRO 2760 2760 2760 PRO PRO A . n 
A 1 2761 SER 2761 2761 2761 SER SER A . n 
A 1 2762 LEU 2762 2762 2762 LEU LEU A . n 
A 1 2763 ARG 2763 2763 2763 ARG ARG A . n 
A 1 2764 THR 2764 2764 2764 THR THR A . n 
A 1 2765 TYR 2765 2765 2765 TYR TYR A . n 
A 1 2766 ALA 2766 2766 2766 ALA ALA A . n 
A 1 2767 GLU 2767 2767 2767 GLU GLU A . n 
A 1 2768 PRO 2768 2768 2768 PRO PRO A . n 
A 1 2769 LEU 2769 2769 2769 LEU LEU A . n 
A 1 2770 THR 2770 2770 2770 THR THR A . n 
A 1 2771 ALA 2771 2771 2771 ALA ALA A . n 
A 1 2772 ALA 2772 2772 2772 ALA ALA A . n 
A 1 2773 MET 2773 2773 2773 MET MET A . n 
A 1 2774 VAL 2774 2774 2774 VAL VAL A . n 
A 1 2775 GLU 2775 2775 2775 GLU GLU A . n 
A 1 2776 PHE 2776 2776 2776 PHE PHE A . n 
A 1 2777 TYR 2777 2777 2777 TYR TYR A . n 
A 1 2778 THR 2778 2778 2778 THR THR A . n 
A 1 2779 MET 2779 2779 2779 MET MET A . n 
A 1 2780 SER 2780 2780 2780 SER SER A . n 
A 1 2781 GLN 2781 2781 2781 GLN GLN A . n 
A 1 2782 GLU 2782 2782 2782 GLU GLU A . n 
A 1 2783 ARG 2783 2783 2783 ARG ARG A . n 
A 1 2784 PHE 2784 2784 2784 PHE PHE A . n 
A 1 2785 THR 2785 2785 2785 THR THR A . n 
A 1 2786 GLN 2786 2786 2786 GLN GLN A . n 
A 1 2787 ASP 2787 2787 2787 ASP ASP A . n 
A 1 2788 THR 2788 2788 2788 THR THR A . n 
A 1 2789 GLN 2789 2789 2789 GLN GLN A . n 
A 1 2790 PRO 2790 2790 2790 PRO PRO A . n 
A 1 2791 HIS 2791 2791 2791 HIS HIS A . n 
A 1 2792 TYR 2792 2792 2792 TYR TYR A . n 
A 1 2793 ILE 2793 2793 2793 ILE ILE A . n 
A 1 2794 TYR 2794 2794 2794 TYR TYR A . n 
A 1 2795 SER 2795 2795 2795 SER SER A . n 
A 1 2796 PRO 2796 2796 2796 PRO PRO A . n 
A 1 2797 ARG 2797 2797 2797 ARG ARG A . n 
A 1 2798 GLU 2798 2798 2798 GLU GLU A . n 
A 1 2799 MET 2799 2799 2799 MET MET A . n 
A 1 2800 THR 2800 2800 2800 THR THR A . n 
A 1 2801 ARG 2801 2801 2801 ARG ARG A . n 
A 1 2802 TRP 2802 2802 2802 TRP TRP A . n 
A 1 2803 VAL 2803 2803 2803 VAL VAL A . n 
A 1 2804 ARG 2804 2804 2804 ARG ARG A . n 
A 1 2805 GLY 2805 2805 2805 GLY GLY A . n 
A 1 2806 ILE 2806 2806 2806 ILE ILE A . n 
A 1 2807 PHE 2807 2807 2807 PHE PHE A . n 
A 1 2808 GLU 2808 2808 2808 GLU GLU A . n 
A 1 2809 ALA 2809 2809 2809 ALA ALA A . n 
A 1 2810 LEU 2810 2810 2810 LEU LEU A . n 
A 1 2811 ARG 2811 2811 2811 ARG ARG A . n 
A 1 2812 PRO 2812 2812 2812 PRO PRO A . n 
A 1 2813 LEU 2813 2813 2813 LEU LEU A . n 
A 1 2814 GLU 2814 2814 2814 GLU GLU A . n 
A 1 2815 THR 2815 2815 2815 THR THR A . n 
A 1 2816 LEU 2816 2816 2816 LEU LEU A . n 
A 1 2817 PRO 2817 2817 2817 PRO PRO A . n 
A 1 2818 VAL 2818 2818 2818 VAL VAL A . n 
A 1 2819 GLU 2819 2819 2819 GLU GLU A . n 
A 1 2820 GLY 2820 2820 2820 GLY GLY A . n 
A 1 2821 LEU 2821 2821 2821 LEU LEU A . n 
A 1 2822 ILE 2822 2822 2822 ILE ILE A . n 
A 1 2823 ARG 2823 2823 2823 ARG ARG A . n 
A 1 2824 ILE 2824 2824 2824 ILE ILE A . n 
A 1 2825 TRP 2825 2825 2825 TRP TRP A . n 
A 1 2826 ALA 2826 2826 2826 ALA ALA A . n 
A 1 2827 HIS 2827 2827 2827 HIS HIS A . n 
A 1 2828 GLU 2828 2828 2828 GLU GLU A . n 
A 1 2829 ALA 2829 2829 2829 ALA ALA A . n 
A 1 2830 LEU 2830 2830 2830 LEU LEU A . n 
A 1 2831 ARG 2831 2831 2831 ARG ARG A . n 
A 1 2832 LEU 2832 2832 2832 LEU LEU A . n 
A 1 2833 PHE 2833 2833 2833 PHE PHE A . n 
A 1 2834 GLN 2834 2834 2834 GLN GLN A . n 
A 1 2835 ASP 2835 2835 2835 ASP ASP A . n 
A 1 2836 ARG 2836 2836 2836 ARG ARG A . n 
A 1 2837 LEU 2837 2837 2837 LEU LEU A . n 
A 1 2838 VAL 2838 2838 2838 VAL VAL A . n 
A 1 2839 GLU 2839 2839 2839 GLU GLU A . n 
A 1 2840 ASP 2840 2840 2840 ASP ASP A . n 
A 1 2841 GLU 2841 2841 2841 GLU GLU A . n 
A 1 2842 GLU 2842 2842 2842 GLU GLU A . n 
A 1 2843 ARG 2843 2843 2843 ARG ARG A . n 
A 1 2844 ARG 2844 2844 2844 ARG ARG A . n 
A 1 2845 TRP 2845 2845 2845 TRP TRP A . n 
A 1 2846 THR 2846 2846 2846 THR THR A . n 
A 1 2847 ASP 2847 2847 2847 ASP ASP A . n 
A 1 2848 GLU 2848 2848 2848 GLU GLU A . n 
A 1 2849 ASN 2849 2849 2849 ASN ASN A . n 
A 1 2850 ILE 2850 2850 2850 ILE ILE A . n 
A 1 2851 ASP 2851 2851 2851 ASP ASP A . n 
A 1 2852 THR 2852 2852 2852 THR THR A . n 
A 1 2853 VAL 2853 2853 2853 VAL VAL A . n 
A 1 2854 ALA 2854 2854 2854 ALA ALA A . n 
A 1 2855 LEU 2855 2855 2855 LEU LEU A . n 
A 1 2856 LYS 2856 2856 2856 LYS LYS A . n 
A 1 2857 HIS 2857 2857 2857 HIS HIS A . n 
A 1 2858 PHE 2858 2858 2858 PHE PHE A . n 
A 1 2859 PRO 2859 2859 2859 PRO PRO A . n 
A 1 2860 ASN 2860 2860 2860 ASN ASN A . n 
A 1 2861 ILE 2861 2861 2861 ILE ILE A . n 
A 1 2862 ASP 2862 2862 2862 ASP ASP A . n 
A 1 2863 ARG 2863 2863 2863 ARG ARG A . n 
A 1 2864 GLU 2864 2864 2864 GLU GLU A . n 
A 1 2865 LYS 2865 2865 2865 LYS LYS A . n 
A 1 2866 ALA 2866 2866 2866 ALA ALA A . n 
A 1 2867 MET 2867 2867 2867 MET MET A . n 
A 1 2868 SER 2868 2868 2868 SER SER A . n 
A 1 2869 ARG 2869 2869 2869 ARG ARG A . n 
A 1 2870 PRO 2870 2870 2870 PRO PRO A . n 
A 1 2871 ILE 2871 2871 2871 ILE ILE A . n 
A 1 2872 LEU 2872 2872 2872 LEU LEU A . n 
A 1 2873 TYR 2873 2873 2873 TYR TYR A . n 
A 1 2874 SER 2874 2874 2874 SER SER A . n 
A 1 2875 ASN 2875 2875 2875 ASN ASN A . n 
A 1 2876 TRP 2876 2876 2876 TRP TRP A . n 
A 1 2877 LEU 2877 2877 2877 LEU LEU A . n 
A 1 2878 SER 2878 2878 2878 SER SER A . n 
A 1 2879 LYS 2879 2879 2879 LYS LYS A . n 
A 1 2880 ASP 2880 2880 2880 ASP ASP A . n 
A 1 2881 TYR 2881 2881 2881 TYR TYR A . n 
A 1 2882 ILE 2882 2882 2882 ILE ILE A . n 
A 1 2883 PRO 2883 2883 2883 PRO PRO A . n 
A 1 2884 VAL 2884 2884 2884 VAL VAL A . n 
A 1 2885 ASP 2885 2885 2885 ASP ASP A . n 
A 1 2886 GLN 2886 2886 2886 GLN GLN A . n 
A 1 2887 GLU 2887 2887 2887 GLU GLU A . n 
A 1 2888 GLU 2888 2888 2888 GLU GLU A . n 
A 1 2889 LEU 2889 2889 2889 LEU LEU A . n 
A 1 2890 ARG 2890 2890 2890 ARG ARG A . n 
A 1 2891 ASP 2891 2891 2891 ASP ASP A . n 
A 1 2892 TYR 2892 2892 2892 TYR TYR A . n 
A 1 2893 VAL 2893 2893 2893 VAL VAL A . n 
A 1 2894 LYS 2894 2894 2894 LYS LYS A . n 
A 1 2895 ALA 2895 2895 2895 ALA ALA A . n 
A 1 2896 ARG 2896 2896 2896 ARG ARG A . n 
A 1 2897 LEU 2897 2897 2897 LEU LEU A . n 
A 1 2898 LYS 2898 2898 2898 LYS LYS A . n 
A 1 2899 VAL 2899 2899 2899 VAL VAL A . n 
A 1 2900 PHE 2900 2900 2900 PHE PHE A . n 
A 1 2901 TYR 2901 2901 2901 TYR TYR A . n 
A 1 2902 GLU 2902 2902 2902 GLU GLU A . n 
A 1 2903 GLU 2903 2903 2903 GLU GLU A . n 
A 1 2904 GLU 2904 2904 2904 GLU GLU A . n 
A 1 2905 LEU 2905 2905 2905 LEU LEU A . n 
A 1 2906 ASP 2906 2906 2906 ASP ASP A . n 
A 1 2907 VAL 2907 2907 2907 VAL VAL A . n 
A 1 2908 PRO 2908 2908 2908 PRO PRO A . n 
A 1 2909 LEU 2909 2909 2909 LEU LEU A . n 
A 1 2910 VAL 2910 2910 2910 VAL VAL A . n 
A 1 2911 LEU 2911 2911 2911 LEU LEU A . n 
A 1 2912 PHE 2912 2912 2912 PHE PHE A . n 
A 1 2913 ASN 2913 2913 2913 ASN ASN A . n 
A 1 2914 GLU 2914 2914 2914 GLU GLU A . n 
A 1 2915 VAL 2915 2915 2915 VAL VAL A . n 
A 1 2916 LEU 2916 2916 2916 LEU LEU A . n 
A 1 2917 ASP 2917 2917 2917 ASP ASP A . n 
A 1 2918 HIS 2918 2918 2918 HIS HIS A . n 
A 1 2919 VAL 2919 2919 2919 VAL VAL A . n 
A 1 2920 LEU 2920 2920 2920 LEU LEU A . n 
A 1 2921 ARG 2921 2921 2921 ARG ARG A . n 
A 1 2922 ILE 2922 2922 2922 ILE ILE A . n 
A 1 2923 ASP 2923 2923 2923 ASP ASP A . n 
A 1 2924 ARG 2924 2924 2924 ARG ARG A . n 
A 1 2925 ILE 2925 2925 2925 ILE ILE A . n 
A 1 2926 PHE 2926 2926 2926 PHE PHE A . n 
A 1 2927 ARG 2927 2927 2927 ARG ARG A . n 
A 1 2928 GLN 2928 2928 2928 GLN GLN A . n 
A 1 2929 PRO 2929 2929 2929 PRO PRO A . n 
A 1 2930 GLN 2930 2930 2930 GLN GLN A . n 
A 1 2931 GLY 2931 2931 2931 GLY GLY A . n 
A 1 2932 HIS 2932 2932 2932 HIS HIS A . n 
A 1 2933 LEU 2933 2933 2933 LEU LEU A . n 
A 1 2934 LEU 2934 2934 2934 LEU LEU A . n 
A 1 2935 LEU 2935 2935 2935 LEU LEU A . n 
A 1 2936 ILE 2936 2936 2936 ILE ILE A . n 
A 1 2937 GLY 2937 2937 2937 GLY GLY A . n 
A 1 2938 VAL 2938 2938 2938 VAL VAL A . n 
A 1 2939 SER 2939 2939 2939 SER SER A . n 
A 1 2940 GLY 2940 2940 2940 GLY GLY A . n 
A 1 2941 ALA 2941 2941 2941 ALA ALA A . n 
A 1 2942 GLY 2942 2942 2942 GLY GLY A . n 
A 1 2943 LYS 2943 2943 2943 LYS LYS A . n 
A 1 2944 THR 2944 2944 2944 THR THR A . n 
A 1 2945 THR 2945 2945 2945 THR THR A . n 
A 1 2946 LEU 2946 2946 2946 LEU LEU A . n 
A 1 2947 SER 2947 2947 2947 SER SER A . n 
A 1 2948 ARG 2948 2948 2948 ARG ARG A . n 
A 1 2949 PHE 2949 2949 2949 PHE PHE A . n 
A 1 2950 VAL 2950 2950 2950 VAL VAL A . n 
A 1 2951 ALA 2951 2951 2951 ALA ALA A . n 
A 1 2952 TRP 2952 2952 2952 TRP TRP A . n 
A 1 2953 MET 2953 2953 2953 MET MET A . n 
A 1 2954 ASN 2954 2954 2954 ASN ASN A . n 
A 1 2955 GLY 2955 2955 2955 GLY GLY A . n 
A 1 2956 LEU 2956 2956 2956 LEU LEU A . n 
A 1 2957 SER 2957 2957 2957 SER SER A . n 
A 1 2958 VAL 2958 2958 2958 VAL VAL A . n 
A 1 2959 TYR 2959 2959 2959 TYR TYR A . n 
A 1 2960 GLN 2960 2960 2960 GLN GLN A . n 
A 1 2961 ILE 2961 2961 2961 ILE ILE A . n 
A 1 2962 LYS 2962 2962 2962 LYS LYS A . n 
A 1 2963 VAL 2963 2963 2963 VAL VAL A . n 
A 1 2964 HIS 2964 2964 2964 HIS HIS A . n 
A 1 2965 ARG 2965 2965 2965 ARG ARG A . n 
A 1 2966 LYS 2966 2966 2966 LYS LYS A . n 
A 1 2967 TYR 2967 2967 2967 TYR TYR A . n 
A 1 2968 THR 2968 2968 2968 THR THR A . n 
A 1 2969 GLY 2969 2969 2969 GLY GLY A . n 
A 1 2970 GLU 2970 2970 2970 GLU GLU A . n 
A 1 2971 ASP 2971 2971 2971 ASP ASP A . n 
A 1 2972 PHE 2972 2972 2972 PHE PHE A . n 
A 1 2973 ASP 2973 2973 2973 ASP ASP A . n 
A 1 2974 GLU 2974 2974 2974 GLU GLU A . n 
A 1 2975 ASP 2975 2975 2975 ASP ASP A . n 
A 1 2976 LEU 2976 2976 2976 LEU LEU A . n 
A 1 2977 ARG 2977 2977 2977 ARG ARG A . n 
A 1 2978 THR 2978 2978 2978 THR THR A . n 
A 1 2979 VAL 2979 2979 2979 VAL VAL A . n 
A 1 2980 LEU 2980 2980 2980 LEU LEU A . n 
A 1 2981 ARG 2981 2981 2981 ARG ARG A . n 
A 1 2982 ARG 2982 2982 2982 ARG ARG A . n 
A 1 2983 SER 2983 2983 2983 SER SER A . n 
A 1 2984 GLY 2984 2984 2984 GLY GLY A . n 
A 1 2985 CYS 2985 2985 2985 CYS CYS A . n 
A 1 2986 LYS 2986 2986 2986 LYS LYS A . n 
A 1 2987 ASN 2987 2987 2987 ASN ASN A . n 
A 1 2988 GLU 2988 2988 2988 GLU GLU A . n 
A 1 2989 LYS 2989 2989 2989 LYS LYS A . n 
A 1 2990 ILE 2990 2990 2990 ILE ILE A . n 
A 1 2991 ALA 2991 2991 2991 ALA ALA A . n 
A 1 2992 PHE 2992 2992 2992 PHE PHE A . n 
A 1 2993 ILE 2993 2993 2993 ILE ILE A . n 
A 1 2994 MET 2994 2994 2994 MET MET A . n 
A 1 2995 ASP 2995 2995 2995 ASP ASP A . n 
A 1 2996 GLU 2996 2996 2996 GLU GLU A . n 
A 1 2997 SER 2997 2997 2997 SER SER A . n 
A 1 2998 ASN 2998 2998 2998 ASN ASN A . n 
A 1 2999 VAL 2999 2999 2999 VAL VAL A . n 
A 1 3000 LEU 3000 3000 3000 LEU LEU A . n 
A 1 3001 ASP 3001 3001 3001 ASP ASP A . n 
A 1 3002 SER 3002 3002 3002 SER SER A . n 
A 1 3003 GLY 3003 3003 3003 GLY GLY A . n 
A 1 3004 PHE 3004 3004 3004 PHE PHE A . n 
A 1 3005 LEU 3005 3005 3005 LEU LEU A . n 
A 1 3006 GLU 3006 3006 3006 GLU GLU A . n 
A 1 3007 ARG 3007 3007 3007 ARG ARG A . n 
A 1 3008 MET 3008 3008 3008 MET MET A . n 
A 1 3009 ASN 3009 3009 3009 ASN ASN A . n 
A 1 3010 THR 3010 3010 3010 THR THR A . n 
A 1 3011 LEU 3011 3011 3011 LEU LEU A . n 
A 1 3012 LEU 3012 3012 3012 LEU LEU A . n 
A 1 3013 ALA 3013 3013 3013 ALA ALA A . n 
A 1 3014 ASN 3014 3014 3014 ASN ASN A . n 
A 1 3015 GLY 3015 3015 3015 GLY GLY A . n 
A 1 3016 GLU 3016 3016 3016 GLU GLU A . n 
A 1 3017 VAL 3017 3017 3017 VAL VAL A . n 
A 1 3018 PRO 3018 3018 3018 PRO PRO A . n 
A 1 3019 GLY 3019 3019 3019 GLY GLY A . n 
A 1 3020 LEU 3020 3020 3020 LEU LEU A . n 
A 1 3021 PHE 3021 3021 3021 PHE PHE A . n 
A 1 3022 GLU 3022 3022 3022 GLU GLU A . n 
A 1 3023 GLY 3023 3023 3023 GLY GLY A . n 
A 1 3024 ASP 3024 3024 3024 ASP ASP A . n 
A 1 3025 GLU 3025 3025 3025 GLU GLU A . n 
A 1 3026 TYR 3026 3026 3026 TYR TYR A . n 
A 1 3027 ALA 3027 3027 3027 ALA ALA A . n 
A 1 3028 THR 3028 3028 3028 THR THR A . n 
A 1 3029 LEU 3029 3029 3029 LEU LEU A . n 
A 1 3030 MET 3030 3030 3030 MET MET A . n 
A 1 3031 THR 3031 3031 3031 THR THR A . n 
A 1 3032 GLN 3032 3032 3032 GLN GLN A . n 
A 1 3033 CYS 3033 3033 3033 CYS CYS A . n 
A 1 3034 LYS 3034 3034 3034 LYS LYS A . n 
A 1 3035 GLU 3035 3035 3035 GLU GLU A . n 
A 1 3036 GLY 3036 3036 3036 GLY GLY A . n 
A 1 3037 ALA 3037 3037 3037 ALA ALA A . n 
A 1 3038 GLN 3038 3038 3038 GLN GLN A . n 
A 1 3039 LYS 3039 3039 3039 LYS LYS A . n 
A 1 3040 GLU 3040 3040 3040 GLU GLU A . n 
A 1 3041 GLY 3041 3041 3041 GLY GLY A . n 
A 1 3042 LEU 3042 3042 3042 LEU LEU A . n 
A 1 3043 MET 3043 3043 3043 MET MET A . n 
A 1 3044 LEU 3044 3044 3044 LEU LEU A . n 
A 1 3045 ASP 3045 3045 3045 ASP ASP A . n 
A 1 3046 SER 3046 3046 3046 SER SER A . n 
A 1 3047 HIS 3047 3047 3047 HIS HIS A . n 
A 1 3048 GLU 3048 3048 3048 GLU GLU A . n 
A 1 3049 GLU 3049 3049 3049 GLU GLU A . n 
A 1 3050 LEU 3050 3050 3050 LEU LEU A . n 
A 1 3051 TYR 3051 3051 3051 TYR TYR A . n 
A 1 3052 LYS 3052 3052 3052 LYS LYS A . n 
A 1 3053 TRP 3053 3053 3053 TRP TRP A . n 
A 1 3054 PHE 3054 3054 3054 PHE PHE A . n 
A 1 3055 THR 3055 3055 3055 THR THR A . n 
A 1 3056 SER 3056 3056 3056 SER SER A . n 
A 1 3057 GLN 3057 3057 3057 GLN GLN A . n 
A 1 3058 VAL 3058 3058 3058 VAL VAL A . n 
A 1 3059 ILE 3059 3059 3059 ILE ILE A . n 
A 1 3060 ARG 3060 3060 3060 ARG ARG A . n 
A 1 3061 ASN 3061 3061 3061 ASN ASN A . n 
A 1 3062 LEU 3062 3062 3062 LEU LEU A . n 
A 1 3063 HIS 3063 3063 3063 HIS HIS A . n 
A 1 3064 VAL 3064 3064 3064 VAL VAL A . n 
A 1 3065 VAL 3065 3065 3065 VAL VAL A . n 
A 1 3066 PHE 3066 3066 3066 PHE PHE A . n 
A 1 3067 THR 3067 3067 3067 THR THR A . n 
A 1 3068 MET 3068 3068 3068 MET MET A . n 
A 1 3069 ASN 3069 3069 3069 ASN ASN A . n 
A 1 3070 PRO 3070 3070 3070 PRO PRO A . n 
A 1 3071 SER 3071 3071 3071 SER SER A . n 
A 1 3072 SER 3072 3072 3072 SER SER A . n 
A 1 3073 GLU 3073 3073 3073 GLU GLU A . n 
A 1 3074 GLY 3074 3074 3074 GLY GLY A . n 
A 1 3075 LEU 3075 3075 3075 LEU LEU A . n 
A 1 3076 LYS 3076 3076 3076 LYS LYS A . n 
A 1 3077 ASP 3077 3077 3077 ASP ASP A . n 
A 1 3078 ARG 3078 3078 3078 ARG ARG A . n 
A 1 3079 ALA 3079 3079 3079 ALA ALA A . n 
A 1 3080 ALA 3080 3080 3080 ALA ALA A . n 
A 1 3081 THR 3081 3081 3081 THR THR A . n 
A 1 3082 SER 3082 3082 3082 SER SER A . n 
A 1 3083 PRO 3083 3083 3083 PRO PRO A . n 
A 1 3084 ALA 3084 3084 3084 ALA ALA A . n 
A 1 3085 LEU 3085 3085 3085 LEU LEU A . n 
A 1 3086 PHE 3086 3086 3086 PHE PHE A . n 
A 1 3087 ASN 3087 3087 3087 ASN ASN A . n 
A 1 3088 ARG 3088 3088 3088 ARG ARG A . n 
A 1 3089 CYS 3089 3089 3089 CYS CYS A . n 
A 1 3090 VAL 3090 3090 3090 VAL VAL A . n 
A 1 3091 LEU 3091 3091 3091 LEU LEU A . n 
A 1 3092 ASN 3092 3092 3092 ASN ASN A . n 
A 1 3093 TRP 3093 3093 3093 TRP TRP A . n 
A 1 3094 PHE 3094 3094 3094 PHE PHE A . n 
A 1 3095 GLY 3095 3095 3095 GLY GLY A . n 
A 1 3096 ASP 3096 3096 3096 ASP ASP A . n 
A 1 3097 TRP 3097 3097 3097 TRP TRP A . n 
A 1 3098 SER 3098 3098 3098 SER SER A . n 
A 1 3099 THR 3099 3099 3099 THR THR A . n 
A 1 3100 GLU 3100 3100 3100 GLU GLU A . n 
A 1 3101 ALA 3101 3101 3101 ALA ALA A . n 
A 1 3102 LEU 3102 3102 3102 LEU LEU A . n 
A 1 3103 TYR 3103 3103 3103 TYR TYR A . n 
A 1 3104 GLN 3104 3104 3104 GLN GLN A . n 
A 1 3105 VAL 3105 3105 3105 VAL VAL A . n 
A 1 3106 GLY 3106 3106 3106 GLY GLY A . n 
A 1 3107 LYS 3107 3107 3107 LYS LYS A . n 
A 1 3108 GLU 3108 3108 3108 GLU GLU A . n 
A 1 3109 PHE 3109 3109 3109 PHE PHE A . n 
A 1 3110 THR 3110 3110 3110 THR THR A . n 
A 1 3111 SER 3111 3111 3111 SER SER A . n 
A 1 3112 LYS 3112 3112 3112 LYS LYS A . n 
A 1 3113 MET 3113 3113 3113 MET MET A . n 
A 1 3114 ASP 3114 3114 3114 ASP ASP A . n 
A 1 3115 LEU 3115 3115 3115 LEU LEU A . n 
A 1 3116 GLU 3116 3116 3116 GLU GLU A . n 
A 1 3117 LYS 3117 3117 3117 LYS LYS A . n 
A 1 3118 PRO 3118 3118 3118 PRO PRO A . n 
A 1 3119 ASN 3119 3119 3119 ASN ASN A . n 
A 1 3120 TYR 3120 3120 3120 TYR TYR A . n 
A 1 3121 ILE 3121 3121 3121 ILE ILE A . n 
A 1 3122 VAL 3122 3122 3122 VAL VAL A . n 
A 1 3123 PRO 3123 3123 3123 PRO PRO A . n 
A 1 3124 ASP 3124 3124 3124 ASP ASP A . n 
A 1 3125 TYR 3125 3125 3125 TYR TYR A . n 
A 1 3126 MET 3126 3126 3126 MET MET A . n 
A 1 3127 PRO 3127 3127 3127 PRO PRO A . n 
A 1 3128 VAL 3128 3128 3128 VAL VAL A . n 
A 1 3129 VAL 3129 3129 3129 VAL VAL A . n 
A 1 3130 TYR 3130 3130 3130 TYR TYR A . n 
A 1 3131 ASP 3131 3131 3131 ASP ASP A . n 
A 1 3132 LYS 3132 3132 3132 LYS LYS A . n 
A 1 3133 LEU 3133 3133 3133 LEU LEU A . n 
A 1 3134 PRO 3134 3134 3134 PRO PRO A . n 
A 1 3135 GLN 3135 3135 3135 GLN GLN A . n 
A 1 3136 PRO 3136 3136 3136 PRO PRO A . n 
A 1 3137 PRO 3137 3137 3137 PRO PRO A . n 
A 1 3138 SER 3138 3138 3138 SER SER A . n 
A 1 3139 HIS 3139 3139 3139 HIS HIS A . n 
A 1 3140 ARG 3140 3140 3140 ARG ARG A . n 
A 1 3141 GLU 3141 3141 3141 GLU GLU A . n 
A 1 3142 ALA 3142 3142 3142 ALA ALA A . n 
A 1 3143 ILE 3143 3143 3143 ILE ILE A . n 
A 1 3144 VAL 3144 3144 3144 VAL VAL A . n 
A 1 3145 ASN 3145 3145 3145 ASN ASN A . n 
A 1 3146 SER 3146 3146 3146 SER SER A . n 
A 1 3147 CYS 3147 3147 3147 CYS CYS A . n 
A 1 3148 VAL 3148 3148 3148 VAL VAL A . n 
A 1 3149 PHE 3149 3149 3149 PHE PHE A . n 
A 1 3150 VAL 3150 3150 3150 VAL VAL A . n 
A 1 3151 HIS 3151 3151 3151 HIS HIS A . n 
A 1 3152 GLN 3152 3152 3152 GLN GLN A . n 
A 1 3153 THR 3153 3153 3153 THR THR A . n 
A 1 3154 LEU 3154 3154 3154 LEU LEU A . n 
A 1 3155 HIS 3155 3155 3155 HIS HIS A . n 
A 1 3156 GLN 3156 3156 3156 GLN GLN A . n 
A 1 3157 ALA 3157 3157 3157 ALA ALA A . n 
A 1 3158 ASN 3158 3158 3158 ASN ASN A . n 
A 1 3159 ALA 3159 3159 3159 ALA ALA A . n 
A 1 3160 ARG 3160 3160 3160 ARG ARG A . n 
A 1 3161 LEU 3161 3161 3161 LEU LEU A . n 
A 1 3162 ALA 3162 3162 3162 ALA ALA A . n 
A 1 3163 LYS 3163 3163 3163 LYS LYS A . n 
A 1 3164 ARG 3164 3164 3164 ARG ARG A . n 
A 1 3165 GLY 3165 3165 3165 GLY GLY A . n 
A 1 3166 GLY 3166 3166 3166 GLY GLY A . n 
A 1 3167 ARG 3167 3167 3167 ARG ARG A . n 
A 1 3168 THR 3168 3168 3168 THR THR A . n 
A 1 3169 MET 3169 3169 3169 MET MET A . n 
A 1 3170 ALA 3170 3170 3170 ALA ALA A . n 
A 1 3171 ILE 3171 3171 3171 ILE ILE A . n 
A 1 3172 THR 3172 3172 3172 THR THR A . n 
A 1 3173 PRO 3173 3173 3173 PRO PRO A . n 
A 1 3174 ARG 3174 3174 3174 ARG ARG A . n 
A 1 3175 HIS 3175 3175 3175 HIS HIS A . n 
A 1 3176 TYR 3176 3176 3176 TYR TYR A . n 
A 1 3177 LEU 3177 3177 3177 LEU LEU A . n 
A 1 3178 ASP 3178 3178 3178 ASP ASP A . n 
A 1 3179 PHE 3179 3179 3179 PHE PHE A . n 
A 1 3180 ILE 3180 3180 3180 ILE ILE A . n 
A 1 3181 ASN 3181 3181 3181 ASN ASN A . n 
A 1 3182 HIS 3182 3182 3182 HIS HIS A . n 
A 1 3183 TYR 3183 3183 3183 TYR TYR A . n 
A 1 3184 ALA 3184 3184 3184 ALA ALA A . n 
A 1 3185 ASN 3185 3185 3185 ASN ASN A . n 
A 1 3186 LEU 3186 3186 3186 LEU LEU A . n 
A 1 3187 PHE 3187 3187 3187 PHE PHE A . n 
A 1 3188 HIS 3188 3188 3188 HIS HIS A . n 
A 1 3189 GLU 3189 3189 3189 GLU GLU A . n 
A 1 3190 LYS 3190 3190 3190 LYS LYS A . n 
A 1 3191 ARG 3191 3191 3191 ARG ARG A . n 
A 1 3192 SER 3192 3192 3192 SER SER A . n 
A 1 3193 GLU 3193 3193 3193 GLU GLU A . n 
A 1 3194 LEU 3194 3194 3194 LEU LEU A . n 
A 1 3195 GLU 3195 3195 3195 GLU GLU A . n 
A 1 3196 GLU 3196 3196 3196 GLU GLU A . n 
A 1 3197 GLN 3197 3197 3197 GLN GLN A . n 
A 1 3198 GLN 3198 3198 3198 GLN GLN A . n 
A 1 3199 MET 3199 3199 3199 MET MET A . n 
A 1 3200 HIS 3200 3200 3200 HIS HIS A . n 
A 1 3201 LEU 3201 3201 3201 LEU LEU A . n 
A 1 3202 ASN 3202 3202 3202 ASN ASN A . n 
A 1 3203 VAL 3203 3203 3203 VAL VAL A . n 
A 1 3204 GLY 3204 3204 3204 GLY GLY A . n 
A 1 3205 LEU 3205 3205 3205 LEU LEU A . n 
A 1 3206 ARG 3206 3206 3206 ARG ARG A . n 
A 1 3207 LYS 3207 3207 3207 LYS LYS A . n 
A 1 3208 ILE 3208 3208 3208 ILE ILE A . n 
A 1 3209 LYS 3209 3209 3209 LYS LYS A . n 
A 1 3210 GLU 3210 3210 3210 GLU GLU A . n 
A 1 3211 THR 3211 3211 3211 THR THR A . n 
A 1 3212 VAL 3212 3212 3212 VAL VAL A . n 
A 1 3213 ASP 3213 3213 3213 ASP ASP A . n 
A 1 3214 GLN 3214 3214 3214 GLN GLN A . n 
A 1 3215 VAL 3215 3215 3215 VAL VAL A . n 
A 1 3216 GLU 3216 3216 3216 GLU GLU A . n 
A 1 3217 GLU 3217 3217 3217 GLU GLU A . n 
A 1 3218 LEU 3218 3218 ?    ?   ?   A . n 
A 1 3219 ARG 3219 3219 ?    ?   ?   A . n 
A 1 3220 ARG 3220 3220 ?    ?   ?   A . n 
A 1 3221 ASP 3221 3221 ?    ?   ?   A . n 
A 1 3222 LEU 3222 3222 ?    ?   ?   A . n 
A 1 3223 ARG 3223 3223 ?    ?   ?   A . n 
A 1 3224 ILE 3224 3224 ?    ?   ?   A . n 
A 1 3225 LYS 3225 3225 ?    ?   ?   A . n 
A 1 3226 SER 3226 3226 ?    ?   ?   A . n 
A 1 3227 GLN 3227 3227 ?    ?   ?   A . n 
A 1 3228 GLU 3228 3228 ?    ?   ?   A . n 
A 1 3229 LEU 3229 3229 ?    ?   ?   A . n 
A 1 3230 GLU 3230 3230 ?    ?   ?   A . n 
A 1 3231 VAL 3231 3231 ?    ?   ?   A . n 
A 1 3232 LYS 3232 3232 ?    ?   ?   A . n 
A 1 3233 ASN 3233 3233 ?    ?   ?   A . n 
A 1 3234 ALA 3234 3234 ?    ?   ?   A . n 
A 1 3235 ALA 3235 3235 ?    ?   ?   A . n 
A 1 3236 ALA 3236 3236 ?    ?   ?   A . n 
A 1 3237 ASN 3237 3237 ?    ?   ?   A . n 
A 1 3238 ASP 3238 3238 ?    ?   ?   A . n 
A 1 3239 LYS 3239 3239 ?    ?   ?   A . n 
A 1 3240 LEU 3240 3240 ?    ?   ?   A . n 
A 1 3241 LYS 3241 3241 ?    ?   ?   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 ?    ?   ?   A . n 
A 1 3450 GLU 3450 3450 ?    ?   ?   A . n 
A 1 3451 TYR 3451 3451 ?    ?   ?   A . n 
A 1 3452 ALA 3452 3452 ?    ?   ?   A . n 
A 1 3453 VAL 3453 3453 ?    ?   ?   A . n 
A 1 3454 LEU 3454 3454 ?    ?   ?   A . n 
A 1 3455 ILE 3455 3455 ?    ?   ?   A . n 
A 1 3456 SER 3456 3456 ?    ?   ?   A . n 
A 1 3457 GLU 3457 3457 ?    ?   ?   A . n 
A 1 3458 ALA 3458 3458 ?    ?   ?   A . n 
A 1 3459 GLN 3459 3459 ?    ?   ?   A . n 
A 1 3460 ALA 3460 3460 ?    ?   ?   A . n 
A 1 3461 ILE 3461 3461 ?    ?   ?   A . n 
A 1 3462 LYS 3462 3462 ?    ?   ?   A . n 
A 1 3463 ALA 3463 3463 ?    ?   ?   A . n 
A 1 3464 ASP 3464 3464 ?    ?   ?   A . n 
A 1 3465 LEU 3465 3465 ?    ?   ?   A . n 
A 1 3466 ALA 3466 3466 ?    ?   ?   A . n 
A 1 3467 ALA 3467 3467 ?    ?   ?   A . n 
A 1 3468 VAL 3468 3468 ?    ?   ?   A . n 
A 1 3469 GLU 3469 3469 ?    ?   ?   A . n 
A 1 3470 ALA 3470 3470 ?    ?   ?   A . n 
A 1 3471 LYS 3471 3471 ?    ?   ?   A . n 
A 1 3472 VAL 3472 3472 3472 VAL VAL A . n 
A 1 3473 ASN 3473 3473 3473 ASN ASN A . n 
A 1 3474 ARG 3474 3474 3474 ARG ARG A . n 
A 1 3475 SER 3475 3475 3475 SER SER A . n 
A 1 3476 THR 3476 3476 3476 THR THR A . n 
A 1 3477 ALA 3477 3477 3477 ALA ALA A . n 
A 1 3478 LEU 3478 3478 3478 LEU LEU A . n 
A 1 3479 LEU 3479 3479 3479 LEU LEU A . n 
A 1 3480 LYS 3480 3480 3480 LYS LYS A . n 
A 1 3481 SER 3481 3481 3481 SER SER A . n 
A 1 3482 LEU 3482 3482 3482 LEU LEU A . n 
A 1 3483 SER 3483 3483 3483 SER SER A . n 
A 1 3484 ALA 3484 3484 3484 ALA ALA A . n 
A 1 3485 GLU 3485 3485 3485 GLU GLU A . n 
A 1 3486 ARG 3486 3486 3486 ARG ARG A . n 
A 1 3487 GLU 3487 3487 3487 GLU GLU A . n 
A 1 3488 ARG 3488 3488 3488 ARG ARG A . n 
A 1 3489 TRP 3489 3489 3489 TRP TRP A . n 
A 1 3490 GLU 3490 3490 3490 GLU GLU A . n 
A 1 3491 LYS 3491 3491 3491 LYS LYS A . n 
A 1 3492 THR 3492 3492 3492 THR THR A . n 
A 1 3493 SER 3493 3493 3493 SER SER A . n 
A 1 3494 GLU 3494 3494 3494 GLU GLU A . n 
A 1 3495 THR 3495 3495 3495 THR THR A . n 
A 1 3496 PHE 3496 3496 3496 PHE PHE A . n 
A 1 3497 LYS 3497 3497 3497 LYS LYS A . n 
A 1 3498 ASN 3498 3498 3498 ASN ASN A . n 
A 1 3499 GLN 3499 3499 3499 GLN GLN A . n 
A 1 3500 MET 3500 3500 3500 MET MET A . n 
A 1 3501 SER 3501 3501 3501 SER SER A . n 
A 1 3502 THR 3502 3502 3502 THR THR A . n 
A 1 3503 ILE 3503 3503 3503 ILE ILE A . n 
A 1 3504 ALA 3504 3504 3504 ALA ALA A . n 
A 1 3505 GLY 3505 3505 3505 GLY GLY A . n 
A 1 3506 ASP 3506 3506 3506 ASP ASP A . n 
A 1 3507 CYS 3507 3507 3507 CYS CYS A . n 
A 1 3508 LEU 3508 3508 3508 LEU LEU A . n 
A 1 3509 LEU 3509 3509 3509 LEU LEU A . n 
A 1 3510 SER 3510 3510 3510 SER SER A . n 
A 1 3511 ALA 3511 3511 3511 ALA ALA A . n 
A 1 3512 ALA 3512 3512 3512 ALA ALA A . n 
A 1 3513 PHE 3513 3513 3513 PHE PHE A . n 
A 1 3514 ILE 3514 3514 3514 ILE ILE A . n 
A 1 3515 ALA 3515 3515 3515 ALA ALA A . n 
A 1 3516 TYR 3516 3516 3516 TYR TYR A . n 
A 1 3517 ALA 3517 3517 3517 ALA ALA A . n 
A 1 3518 GLY 3518 3518 3518 GLY GLY A . n 
A 1 3519 TYR 3519 3519 3519 TYR TYR A . n 
A 1 3520 PHE 3520 3520 3520 PHE PHE A . n 
A 1 3521 ASP 3521 3521 3521 ASP ASP A . n 
A 1 3522 GLN 3522 3522 3522 GLN GLN A . n 
A 1 3523 GLN 3523 3523 3523 GLN GLN A . n 
A 1 3524 MET 3524 3524 3524 MET MET A . n 
A 1 3525 ARG 3525 3525 3525 ARG ARG A . n 
A 1 3526 GLN 3526 3526 3526 GLN GLN A . n 
A 1 3527 ASN 3527 3527 3527 ASN ASN A . n 
A 1 3528 LEU 3528 3528 3528 LEU LEU A . n 
A 1 3529 PHE 3529 3529 3529 PHE PHE A . n 
A 1 3530 THR 3530 3530 3530 THR THR A . n 
A 1 3531 THR 3531 3531 3531 THR THR A . n 
A 1 3532 TRP 3532 3532 3532 TRP TRP A . n 
A 1 3533 SER 3533 3533 3533 SER SER A . n 
A 1 3534 HIS 3534 3534 3534 HIS HIS A . n 
A 1 3535 HIS 3535 3535 3535 HIS HIS A . n 
A 1 3536 LEU 3536 3536 3536 LEU LEU A . n 
A 1 3537 GLN 3537 3537 3537 GLN GLN A . n 
A 1 3538 GLN 3538 3538 3538 GLN GLN A . n 
A 1 3539 ALA 3539 3539 3539 ALA ALA A . n 
A 1 3540 ASN 3540 3540 3540 ASN ASN A . n 
A 1 3541 ILE 3541 3541 3541 ILE ILE A . n 
A 1 3542 GLN 3542 3542 3542 GLN GLN A . n 
A 1 3543 PHE 3543 3543 3543 PHE PHE A . n 
A 1 3544 ARG 3544 3544 3544 ARG ARG A . n 
A 1 3545 THR 3545 3545 3545 THR THR A . n 
A 1 3546 ASP 3546 3546 3546 ASP ASP A . n 
A 1 3547 ILE 3547 3547 3547 ILE ILE A . n 
A 1 3548 ALA 3548 3548 3548 ALA ALA A . n 
A 1 3549 ARG 3549 3549 3549 ARG ARG A . n 
A 1 3550 THR 3550 3550 3550 THR THR A . n 
A 1 3551 GLU 3551 3551 3551 GLU GLU A . n 
A 1 3552 TYR 3552 3552 3552 TYR TYR A . n 
A 1 3553 LEU 3553 3553 3553 LEU LEU A . n 
A 1 3554 SER 3554 3554 3554 SER SER A . n 
A 1 3555 ASN 3555 3555 3555 ASN ASN A . n 
A 1 3556 ALA 3556 3556 3556 ALA ALA A . n 
A 1 3557 ASP 3557 3557 3557 ASP ASP A . n 
A 1 3558 GLU 3558 3558 3558 GLU GLU A . n 
A 1 3559 ARG 3559 3559 3559 ARG ARG A . n 
A 1 3560 LEU 3560 3560 3560 LEU LEU A . n 
A 1 3561 ARG 3561 3561 3561 ARG ARG A . n 
A 1 3562 TRP 3562 3562 3562 TRP TRP A . n 
A 1 3563 GLN 3563 3563 3563 GLN GLN A . n 
A 1 3564 ALA 3564 3564 3564 ALA ALA A . n 
A 1 3565 SER 3565 3565 3565 SER SER A . n 
A 1 3566 SER 3566 3566 3566 SER SER A . n 
A 1 3567 LEU 3567 3567 3567 LEU LEU A . n 
A 1 3568 PRO 3568 3568 3568 PRO PRO A . n 
A 1 3569 ALA 3569 3569 3569 ALA ALA A . n 
A 1 3570 ASP 3570 3570 3570 ASP ASP A . n 
A 1 3571 ASP 3571 3571 3571 ASP ASP A . n 
A 1 3572 LEU 3572 3572 3572 LEU LEU A . n 
A 1 3573 CYS 3573 3573 3573 CYS CYS A . n 
A 1 3574 THR 3574 3574 3574 THR THR A . n 
A 1 3575 GLU 3575 3575 3575 GLU GLU A . n 
A 1 3576 ASN 3576 3576 3576 ASN ASN A . n 
A 1 3577 ALA 3577 3577 3577 ALA ALA A . n 
A 1 3578 ILE 3578 3578 3578 ILE ILE A . n 
A 1 3579 MET 3579 3579 3579 MET MET A . n 
A 1 3580 LEU 3580 3580 3580 LEU LEU A . n 
A 1 3581 LYS 3581 3581 3581 LYS LYS A . n 
A 1 3582 ARG 3582 3582 3582 ARG ARG A . n 
A 1 3583 PHE 3583 3583 3583 PHE PHE A . n 
A 1 3584 ASN 3584 3584 3584 ASN ASN A . n 
A 1 3585 ARG 3585 3585 3585 ARG ARG A . n 
A 1 3586 TYR 3586 3586 3586 TYR TYR A . n 
A 1 3587 PRO 3587 3587 3587 PRO PRO A . n 
A 1 3588 LEU 3588 3588 3588 LEU LEU A . n 
A 1 3589 ILE 3589 3589 3589 ILE ILE A . n 
A 1 3590 ILE 3590 3590 3590 ILE ILE A . n 
A 1 3591 ASP 3591 3591 3591 ASP ASP A . n 
A 1 3592 PRO 3592 3592 3592 PRO PRO A . n 
A 1 3593 SER 3593 3593 3593 SER SER A . n 
A 1 3594 GLY 3594 3594 3594 GLY GLY A . n 
A 1 3595 GLN 3595 3595 3595 GLN GLN A . n 
A 1 3596 ALA 3596 3596 3596 ALA ALA A . n 
A 1 3597 THR 3597 3597 3597 THR THR A . n 
A 1 3598 GLU 3598 3598 3598 GLU GLU A . n 
A 1 3599 PHE 3599 3599 3599 PHE PHE A . n 
A 1 3600 ILE 3600 3600 3600 ILE ILE A . n 
A 1 3601 MET 3601 3601 3601 MET MET A . n 
A 1 3602 ASN 3602 3602 3602 ASN ASN A . n 
A 1 3603 GLU 3603 3603 3603 GLU GLU A . n 
A 1 3604 TYR 3604 3604 3604 TYR TYR A . n 
A 1 3605 LYS 3605 3605 3605 LYS LYS A . n 
A 1 3606 ASP 3606 3606 3606 ASP ASP A . n 
A 1 3607 ARG 3607 3607 3607 ARG ARG A . n 
A 1 3608 LYS 3608 3608 3608 LYS LYS A . n 
A 1 3609 ILE 3609 3609 3609 ILE ILE A . n 
A 1 3610 THR 3610 3610 3610 THR THR A . n 
A 1 3611 ARG 3611 3611 3611 ARG ARG A . n 
A 1 3612 THR 3612 3612 3612 THR THR A . n 
A 1 3613 SER 3613 3613 3613 SER SER A . n 
A 1 3614 PHE 3614 3614 3614 PHE PHE A . n 
A 1 3615 LEU 3615 3615 3615 LEU LEU A . n 
A 1 3616 ASP 3616 3616 3616 ASP ASP A . n 
A 1 3617 ASP 3617 3617 3617 ASP ASP A . n 
A 1 3618 ALA 3618 3618 3618 ALA ALA A . n 
A 1 3619 PHE 3619 3619 3619 PHE PHE A . n 
A 1 3620 ARG 3620 3620 3620 ARG ARG A . n 
A 1 3621 LYS 3621 3621 3621 LYS LYS A . n 
A 1 3622 ASN 3622 3622 3622 ASN ASN A . n 
A 1 3623 LEU 3623 3623 3623 LEU LEU A . n 
A 1 3624 GLU 3624 3624 3624 GLU GLU A . n 
A 1 3625 SER 3625 3625 3625 SER SER A . n 
A 1 3626 ALA 3626 3626 3626 ALA ALA A . n 
A 1 3627 LEU 3627 3627 3627 LEU LEU A . n 
A 1 3628 ARG 3628 3628 3628 ARG ARG A . n 
A 1 3629 PHE 3629 3629 3629 PHE PHE A . n 
A 1 3630 GLY 3630 3630 3630 GLY GLY A . n 
A 1 3631 ASN 3631 3631 3631 ASN ASN A . n 
A 1 3632 PRO 3632 3632 3632 PRO PRO A . n 
A 1 3633 LEU 3633 3633 3633 LEU LEU A . n 
A 1 3634 LEU 3634 3634 3634 LEU LEU A . n 
A 1 3635 VAL 3635 3635 3635 VAL VAL A . n 
A 1 3636 GLN 3636 3636 3636 GLN GLN A . n 
A 1 3637 ASP 3637 3637 3637 ASP ASP A . n 
A 1 3638 VAL 3638 3638 3638 VAL VAL A . n 
A 1 3639 GLU 3639 3639 3639 GLU GLU A . n 
A 1 3640 SER 3640 3640 3640 SER SER A . n 
A 1 3641 TYR 3641 3641 3641 TYR TYR A . n 
A 1 3642 ASP 3642 3642 3642 ASP ASP A . n 
A 1 3643 PRO 3643 3643 3643 PRO PRO A . n 
A 1 3644 VAL 3644 3644 3644 VAL VAL A . n 
A 1 3645 LEU 3645 3645 3645 LEU LEU A . n 
A 1 3646 ASN 3646 3646 3646 ASN ASN A . n 
A 1 3647 PRO 3647 3647 3647 PRO PRO A . n 
A 1 3648 VAL 3648 3648 3648 VAL VAL A . n 
A 1 3649 LEU 3649 3649 3649 LEU LEU A . n 
A 1 3650 ASN 3650 3650 3650 ASN ASN A . n 
A 1 3651 ARG 3651 3651 3651 ARG ARG A . n 
A 1 3652 GLU 3652 3652 3652 GLU GLU A . n 
A 1 3653 VAL 3653 3653 3653 VAL VAL A . n 
A 1 3654 ARG 3654 3654 3654 ARG ARG A . n 
A 1 3655 ARG 3655 3655 3655 ARG ARG A . n 
A 1 3656 THR 3656 3656 3656 THR THR A . n 
A 1 3657 GLY 3657 3657 3657 GLY GLY A . n 
A 1 3658 GLY 3658 3658 3658 GLY GLY A . n 
A 1 3659 ARG 3659 3659 3659 ARG ARG A . n 
A 1 3660 VAL 3660 3660 3660 VAL VAL A . n 
A 1 3661 LEU 3661 3661 3661 LEU LEU A . n 
A 1 3662 ILE 3662 3662 3662 ILE ILE A . n 
A 1 3663 THR 3663 3663 3663 THR THR A . n 
A 1 3664 LEU 3664 3664 3664 LEU LEU A . n 
A 1 3665 GLY 3665 3665 3665 GLY GLY A . n 
A 1 3666 ASP 3666 3666 3666 ASP ASP A . n 
A 1 3667 GLN 3667 3667 3667 GLN GLN A . n 
A 1 3668 ASP 3668 3668 3668 ASP ASP A . n 
A 1 3669 ILE 3669 3669 3669 ILE ILE A . n 
A 1 3670 ASP 3670 3670 3670 ASP ASP A . n 
A 1 3671 LEU 3671 3671 3671 LEU LEU A . n 
A 1 3672 SER 3672 3672 3672 SER SER A . n 
A 1 3673 PRO 3673 3673 3673 PRO PRO A . n 
A 1 3674 SER 3674 3674 3674 SER SER A . n 
A 1 3675 PHE 3675 3675 3675 PHE PHE A . n 
A 1 3676 VAL 3676 3676 3676 VAL VAL A . n 
A 1 3677 ILE 3677 3677 3677 ILE ILE A . n 
A 1 3678 PHE 3678 3678 3678 PHE PHE A . n 
A 1 3679 LEU 3679 3679 3679 LEU LEU A . n 
A 1 3680 SER 3680 3680 3680 SER SER A . n 
A 1 3681 THR 3681 3681 3681 THR THR A . n 
A 1 3682 ARG 3682 3682 3682 ARG ARG A . n 
A 1 3683 ASP 3683 3683 3683 ASP ASP A . n 
A 1 3684 PRO 3684 3684 3684 PRO PRO A . n 
A 1 3685 THR 3685 3685 3685 THR THR A . n 
A 1 3686 VAL 3686 3686 3686 VAL VAL A . n 
A 1 3687 GLU 3687 3687 3687 GLU GLU A . n 
A 1 3688 PHE 3688 3688 3688 PHE PHE A . n 
A 1 3689 PRO 3689 3689 3689 PRO PRO A . n 
A 1 3690 PRO 3690 3690 3690 PRO PRO A . n 
A 1 3691 ASP 3691 3691 3691 ASP ASP A . n 
A 1 3692 LEU 3692 3692 3692 LEU LEU A . n 
A 1 3693 CYS 3693 3693 3693 CYS CYS A . n 
A 1 3694 SER 3694 3694 3694 SER SER A . n 
A 1 3695 ARG 3695 3695 3695 ARG ARG A . n 
A 1 3696 VAL 3696 3696 3696 VAL VAL A . n 
A 1 3697 THR 3697 3697 3697 THR THR A . n 
A 1 3698 PHE 3698 3698 3698 PHE PHE A . n 
A 1 3699 VAL 3699 3699 3699 VAL VAL A . n 
A 1 3700 ASN 3700 3700 3700 ASN ASN A . n 
A 1 3701 PHE 3701 3701 3701 PHE PHE A . n 
A 1 3702 THR 3702 3702 3702 THR THR A . n 
A 1 3703 VAL 3703 3703 3703 VAL VAL A . n 
A 1 3704 THR 3704 3704 3704 THR THR A . n 
A 1 3705 ARG 3705 3705 3705 ARG ARG A . n 
A 1 3706 SER 3706 3706 3706 SER SER A . n 
A 1 3707 SER 3707 3707 3707 SER SER A . n 
A 1 3708 LEU 3708 3708 3708 LEU LEU A . n 
A 1 3709 GLN 3709 3709 3709 GLN GLN A . n 
A 1 3710 SER 3710 3710 3710 SER SER A . n 
A 1 3711 GLN 3711 3711 3711 GLN GLN A . n 
A 1 3712 CYS 3712 3712 3712 CYS CYS A . n 
A 1 3713 LEU 3713 3713 3713 LEU LEU A . n 
A 1 3714 ASN 3714 3714 3714 ASN ASN A . n 
A 1 3715 GLU 3715 3715 3715 GLU GLU A . n 
A 1 3716 VAL 3716 3716 3716 VAL VAL A . n 
A 1 3717 LEU 3717 3717 3717 LEU LEU A . n 
A 1 3718 LYS 3718 3718 3718 LYS LYS A . n 
A 1 3719 ALA 3719 3719 3719 ALA ALA A . n 
A 1 3720 GLU 3720 3720 3720 GLU GLU A . n 
A 1 3721 ARG 3721 3721 3721 ARG ARG A . n 
A 1 3722 PRO 3722 3722 3722 PRO PRO A . n 
A 1 3723 ASP 3723 3723 3723 ASP ASP A . n 
A 1 3724 VAL 3724 3724 3724 VAL VAL A . n 
A 1 3725 ASP 3725 3725 3725 ASP ASP A . n 
A 1 3726 GLU 3726 3726 3726 GLU GLU A . n 
A 1 3727 LYS 3727 3727 3727 LYS LYS A . n 
A 1 3728 ARG 3728 3728 3728 ARG ARG A . n 
A 1 3729 SER 3729 3729 3729 SER SER A . n 
A 1 3730 ASP 3730 3730 3730 ASP ASP A . n 
A 1 3731 LEU 3731 3731 3731 LEU LEU A . n 
A 1 3732 LEU 3732 3732 3732 LEU LEU A . n 
A 1 3733 LYS 3733 3733 3733 LYS LYS A . n 
A 1 3734 LEU 3734 3734 3734 LEU LEU A . n 
A 1 3735 GLN 3735 3735 3735 GLN GLN A . n 
A 1 3736 GLY 3736 3736 3736 GLY GLY A . n 
A 1 3737 GLU 3737 3737 3737 GLU GLU A . n 
A 1 3738 PHE 3738 3738 3738 PHE PHE A . n 
A 1 3739 GLN 3739 3739 3739 GLN GLN A . n 
A 1 3740 LEU 3740 3740 3740 LEU LEU A . n 
A 1 3741 ARG 3741 3741 3741 ARG ARG A . n 
A 1 3742 LEU 3742 3742 3742 LEU LEU A . n 
A 1 3743 ARG 3743 3743 3743 ARG ARG A . n 
A 1 3744 GLN 3744 3744 3744 GLN GLN A . n 
A 1 3745 LEU 3745 3745 3745 LEU LEU A . n 
A 1 3746 GLU 3746 3746 3746 GLU GLU A . n 
A 1 3747 LYS 3747 3747 3747 LYS LYS A . n 
A 1 3748 SER 3748 3748 3748 SER SER A . n 
A 1 3749 LEU 3749 3749 3749 LEU LEU A . n 
A 1 3750 LEU 3750 3750 3750 LEU LEU A . n 
A 1 3751 GLN 3751 3751 3751 GLN GLN A . n 
A 1 3752 ALA 3752 3752 3752 ALA ALA A . n 
A 1 3753 LEU 3753 3753 3753 LEU LEU A . n 
A 1 3754 ASN 3754 3754 3754 ASN ASN A . n 
A 1 3755 GLU 3755 3755 3755 GLU GLU A . n 
A 1 3756 VAL 3756 3756 3756 VAL VAL A . n 
A 1 3757 LYS 3757 3757 3757 LYS LYS A . n 
A 1 3758 GLY 3758 3758 3758 GLY GLY A . n 
A 1 3759 ARG 3759 3759 3759 ARG ARG A . n 
A 1 3760 ILE 3760 3760 3760 ILE ILE A . n 
A 1 3761 LEU 3761 3761 3761 LEU LEU A . n 
A 1 3762 ASP 3762 3762 3762 ASP ASP A . n 
A 1 3763 ASP 3763 3763 3763 ASP ASP A . n 
A 1 3764 ASP 3764 3764 3764 ASP ASP A . n 
A 1 3765 THR 3765 3765 3765 THR THR A . n 
A 1 3766 ILE 3766 3766 3766 ILE ILE A . n 
A 1 3767 ILE 3767 3767 3767 ILE ILE A . n 
A 1 3768 THR 3768 3768 3768 THR THR A . n 
A 1 3769 THR 3769 3769 3769 THR THR A . n 
A 1 3770 LEU 3770 3770 3770 LEU LEU A . n 
A 1 3771 GLU 3771 3771 3771 GLU GLU A . n 
A 1 3772 ASN 3772 3772 3772 ASN ASN A . n 
A 1 3773 LEU 3773 3773 3773 LEU LEU A . n 
A 1 3774 LYS 3774 3774 3774 LYS LYS A . n 
A 1 3775 ARG 3775 3775 3775 ARG ARG A . n 
A 1 3776 GLU 3776 3776 3776 GLU GLU A . n 
A 1 3777 ALA 3777 3777 3777 ALA ALA A . n 
A 1 3778 ALA 3778 3778 3778 ALA ALA A . n 
A 1 3779 GLU 3779 3779 3779 GLU GLU A . n 
A 1 3780 VAL 3780 3780 3780 VAL VAL A . n 
A 1 3781 THR 3781 3781 3781 THR THR A . n 
A 1 3782 ARG 3782 3782 3782 ARG ARG A . n 
A 1 3783 LYS 3783 3783 3783 LYS LYS A . n 
A 1 3784 VAL 3784 3784 3784 VAL VAL A . n 
A 1 3785 GLU 3785 3785 3785 GLU GLU A . n 
A 1 3786 GLU 3786 3786 3786 GLU GLU A . n 
A 1 3787 THR 3787 3787 3787 THR THR A . n 
A 1 3788 ASP 3788 3788 3788 ASP ASP A . n 
A 1 3789 ILE 3789 3789 3789 ILE ILE A . n 
A 1 3790 VAL 3790 3790 3790 VAL VAL A . n 
A 1 3791 MET 3791 3791 3791 MET MET A . n 
A 1 3792 GLN 3792 3792 3792 GLN GLN A . n 
A 1 3793 GLU 3793 3793 3793 GLU GLU A . n 
A 1 3794 VAL 3794 3794 3794 VAL VAL A . n 
A 1 3795 GLU 3795 3795 3795 GLU GLU A . n 
A 1 3796 THR 3796 3796 3796 THR THR A . n 
A 1 3797 VAL 3797 3797 3797 VAL VAL A . n 
A 1 3798 SER 3798 3798 3798 SER SER A . n 
A 1 3799 GLN 3799 3799 3799 GLN GLN A . n 
A 1 3800 GLN 3800 3800 3800 GLN GLN A . n 
A 1 3801 TYR 3801 3801 3801 TYR TYR A . n 
A 1 3802 LEU 3802 3802 3802 LEU LEU A . n 
A 1 3803 PRO 3803 3803 3803 PRO PRO A . n 
A 1 3804 LEU 3804 3804 3804 LEU LEU A . n 
A 1 3805 SER 3805 3805 3805 SER SER A . n 
A 1 3806 THR 3806 3806 3806 THR THR A . n 
A 1 3807 ALA 3807 3807 3807 ALA ALA A . n 
A 1 3808 CYS 3808 3808 3808 CYS CYS A . n 
A 1 3809 SER 3809 3809 3809 SER SER A . n 
A 1 3810 SER 3810 3810 3810 SER SER A . n 
A 1 3811 ILE 3811 3811 3811 ILE ILE A . n 
A 1 3812 TYR 3812 3812 3812 TYR TYR A . n 
A 1 3813 PHE 3813 3813 3813 PHE PHE A . n 
A 1 3814 THR 3814 3814 3814 THR THR A . n 
A 1 3815 MET 3815 3815 3815 MET MET A . n 
A 1 3816 GLU 3816 3816 3816 GLU GLU A . n 
A 1 3817 SER 3817 3817 3817 SER SER A . n 
A 1 3818 LEU 3818 3818 3818 LEU LEU A . n 
A 1 3819 LYS 3819 3819 3819 LYS LYS A . n 
A 1 3820 GLN 3820 3820 3820 GLN GLN A . n 
A 1 3821 ILE 3821 3821 3821 ILE ILE A . n 
A 1 3822 HIS 3822 3822 3822 HIS HIS A . n 
A 1 3823 PHE 3823 3823 3823 PHE PHE A . n 
A 1 3824 LEU 3824 3824 3824 LEU LEU A . n 
A 1 3825 TYR 3825 3825 3825 TYR TYR A . n 
A 1 3826 GLN 3826 3826 3826 GLN GLN A . n 
A 1 3827 TYR 3827 3827 3827 TYR TYR A . n 
A 1 3828 SER 3828 3828 3828 SER SER A . n 
A 1 3829 LEU 3829 3829 3829 LEU LEU A . n 
A 1 3830 GLN 3830 3830 3830 GLN GLN A . n 
A 1 3831 PHE 3831 3831 3831 PHE PHE A . n 
A 1 3832 PHE 3832 3832 3832 PHE PHE A . n 
A 1 3833 LEU 3833 3833 3833 LEU LEU A . n 
A 1 3834 ASP 3834 3834 3834 ASP ASP A . n 
A 1 3835 ILE 3835 3835 3835 ILE ILE A . n 
A 1 3836 TYR 3836 3836 3836 TYR TYR A . n 
A 1 3837 HIS 3837 3837 3837 HIS HIS A . n 
A 1 3838 ASN 3838 3838 3838 ASN ASN A . n 
A 1 3839 VAL 3839 3839 3839 VAL VAL A . n 
A 1 3840 LEU 3840 3840 3840 LEU LEU A . n 
A 1 3841 TYR 3841 3841 3841 TYR TYR A . n 
A 1 3842 GLU 3842 3842 3842 GLU GLU A . n 
A 1 3843 ASN 3843 3843 3843 ASN ASN A . n 
A 1 3844 PRO 3844 3844 3844 PRO PRO A . n 
A 1 3845 ASN 3845 3845 3845 ASN ASN A . n 
A 1 3846 LEU 3846 3846 3846 LEU LEU A . n 
A 1 3847 LYS 3847 3847 3847 LYS LYS A . n 
A 1 3848 GLY 3848 3848 3848 GLY GLY A . n 
A 1 3849 VAL 3849 3849 3849 VAL VAL A . n 
A 1 3850 THR 3850 3850 3850 THR THR A . n 
A 1 3851 ASP 3851 3851 3851 ASP ASP A . n 
A 1 3852 HIS 3852 3852 3852 HIS HIS A . n 
A 1 3853 THR 3853 3853 3853 THR THR A . n 
A 1 3854 GLN 3854 3854 3854 GLN GLN A . n 
A 1 3855 ARG 3855 3855 3855 ARG ARG A . n 
A 1 3856 LEU 3856 3856 3856 LEU LEU A . n 
A 1 3857 SER 3857 3857 3857 SER SER A . n 
A 1 3858 ILE 3858 3858 3858 ILE ILE A . n 
A 1 3859 ILE 3859 3859 3859 ILE ILE A . n 
A 1 3860 THR 3860 3860 3860 THR THR A . n 
A 1 3861 LYS 3861 3861 3861 LYS LYS A . n 
A 1 3862 ASP 3862 3862 3862 ASP ASP A . n 
A 1 3863 LEU 3863 3863 3863 LEU LEU A . n 
A 1 3864 PHE 3864 3864 3864 PHE PHE A . n 
A 1 3865 GLN 3865 3865 3865 GLN GLN A . n 
A 1 3866 VAL 3866 3866 3866 VAL VAL A . n 
A 1 3867 ALA 3867 3867 3867 ALA ALA A . n 
A 1 3868 PHE 3868 3868 3868 PHE PHE A . n 
A 1 3869 ASN 3869 3869 3869 ASN ASN A . n 
A 1 3870 ARG 3870 3870 3870 ARG ARG A . n 
A 1 3871 VAL 3871 3871 3871 VAL VAL A . n 
A 1 3872 ALA 3872 3872 3872 ALA ALA A . n 
A 1 3873 ARG 3873 3873 3873 ARG ARG A . n 
A 1 3874 GLY 3874 3874 3874 GLY GLY A . n 
A 1 3875 MET 3875 3875 3875 MET MET A . n 
A 1 3876 LEU 3876 3876 3876 LEU LEU A . n 
A 1 3877 HIS 3877 3877 3877 HIS HIS A . n 
A 1 3878 GLN 3878 3878 3878 GLN GLN A . n 
A 1 3879 ASP 3879 3879 3879 ASP ASP A . n 
A 1 3880 HIS 3880 3880 3880 HIS HIS A . n 
A 1 3881 ILE 3881 3881 3881 ILE ILE A . n 
A 1 3882 THR 3882 3882 3882 THR THR A . n 
A 1 3883 PHE 3883 3883 3883 PHE PHE A . n 
A 1 3884 ALA 3884 3884 3884 ALA ALA A . n 
A 1 3885 MET 3885 3885 3885 MET MET A . n 
A 1 3886 LEU 3886 3886 3886 LEU LEU A . n 
A 1 3887 LEU 3887 3887 3887 LEU LEU A . n 
A 1 3888 ALA 3888 3888 3888 ALA ALA A . n 
A 1 3889 ARG 3889 3889 3889 ARG ARG A . n 
A 1 3890 ILE 3890 3890 3890 ILE ILE A . n 
A 1 3891 LYS 3891 3891 3891 LYS LYS A . n 
A 1 3892 LEU 3892 3892 3892 LEU LEU A . n 
A 1 3893 LYS 3893 3893 3893 LYS LYS A . n 
A 1 3894 GLY 3894 3894 3894 GLY GLY A . n 
A 1 3895 THR 3895 3895 3895 THR THR A . n 
A 1 3896 VAL 3896 3896 3896 VAL VAL A . n 
A 1 3897 GLY 3897 3897 3897 GLY GLY A . n 
A 1 3898 GLU 3898 3898 3898 GLU GLU A . n 
A 1 3899 PRO 3899 3899 3899 PRO PRO A . n 
A 1 3900 THR 3900 3900 3900 THR THR A . n 
A 1 3901 TYR 3901 3901 3901 TYR TYR A . n 
A 1 3902 ASP 3902 3902 3902 ASP ASP A . n 
A 1 3903 ALA 3903 3903 3903 ALA ALA A . n 
A 1 3904 GLU 3904 3904 3904 GLU GLU A . n 
A 1 3905 PHE 3905 3905 3905 PHE PHE A . n 
A 1 3906 GLN 3906 3906 3906 GLN GLN A . n 
A 1 3907 HIS 3907 3907 3907 HIS HIS A . n 
A 1 3908 PHE 3908 3908 3908 PHE PHE A . n 
A 1 3909 LEU 3909 3909 3909 LEU LEU A . n 
A 1 3910 ARG 3910 3910 3910 ARG ARG A . n 
A 1 3911 GLY 3911 3911 3911 GLY GLY A . n 
A 1 3912 ASN 3912 3912 3912 ASN ASN A . n 
A 1 3913 GLU 3913 3913 3913 GLU GLU A . n 
A 1 3914 ILE 3914 3914 3914 ILE ILE A . n 
A 1 3915 VAL 3915 3915 3915 VAL VAL A . n 
A 1 3916 LEU 3916 3916 3916 LEU LEU A . n 
A 1 3917 SER 3917 3917 3917 SER SER A . n 
A 1 3918 ALA 3918 3918 3918 ALA ALA A . n 
A 1 3919 GLY 3919 3919 3919 GLY GLY A . n 
A 1 3920 SER 3920 3920 3920 SER SER A . n 
A 1 3921 THR 3921 3921 3921 THR THR A . n 
A 1 3922 PRO 3922 3922 3922 PRO PRO A . n 
A 1 3923 ARG 3923 3923 3923 ARG ARG A . n 
A 1 3924 ILE 3924 3924 3924 ILE ILE A . n 
A 1 3925 GLN 3925 3925 3925 GLN GLN A . n 
A 1 3926 GLY 3926 3926 3926 GLY GLY A . n 
A 1 3927 LEU 3927 3927 3927 LEU LEU A . n 
A 1 3928 THR 3928 3928 3928 THR THR A . n 
A 1 3929 VAL 3929 3929 3929 VAL VAL A . n 
A 1 3930 GLU 3930 3930 3930 GLU GLU A . n 
A 1 3931 GLN 3931 3931 3931 GLN GLN A . n 
A 1 3932 ALA 3932 3932 3932 ALA ALA A . n 
A 1 3933 GLU 3933 3933 3933 GLU GLU A . n 
A 1 3934 ALA 3934 3934 3934 ALA ALA A . n 
A 1 3935 VAL 3935 3935 3935 VAL VAL A . n 
A 1 3936 VAL 3936 3936 3936 VAL VAL A . n 
A 1 3937 ARG 3937 3937 3937 ARG ARG A . n 
A 1 3938 LEU 3938 3938 3938 LEU LEU A . n 
A 1 3939 SER 3939 3939 3939 SER SER A . n 
A 1 3940 CYS 3940 3940 3940 CYS CYS A . n 
A 1 3941 LEU 3941 3941 3941 LEU LEU A . n 
A 1 3942 PRO 3942 3942 3942 PRO PRO A . n 
A 1 3943 ALA 3943 3943 3943 ALA ALA A . n 
A 1 3944 PHE 3944 3944 3944 PHE PHE A . n 
A 1 3945 LYS 3945 3945 3945 LYS LYS A . n 
A 1 3946 ASP 3946 3946 3946 ASP ASP A . n 
A 1 3947 LEU 3947 3947 3947 LEU LEU A . n 
A 1 3948 ILE 3948 3948 3948 ILE ILE A . n 
A 1 3949 ALA 3949 3949 3949 ALA ALA A . n 
A 1 3950 LYS 3950 3950 3950 LYS LYS A . n 
A 1 3951 VAL 3951 3951 3951 VAL VAL A . n 
A 1 3952 GLN 3952 3952 3952 GLN GLN A . n 
A 1 3953 ALA 3953 3953 3953 ALA ALA A . n 
A 1 3954 ASP 3954 3954 3954 ASP ASP A . n 
A 1 3955 GLU 3955 3955 3955 GLU GLU A . n 
A 1 3956 GLN 3956 3956 3956 GLN GLN A . n 
A 1 3957 PHE 3957 3957 3957 PHE PHE A . n 
A 1 3958 GLY 3958 3958 3958 GLY GLY A . n 
A 1 3959 ILE 3959 3959 3959 ILE ILE A . n 
A 1 3960 TRP 3960 3960 3960 TRP TRP A . n 
A 1 3961 LEU 3961 3961 3961 LEU LEU A . n 
A 1 3962 ASP 3962 3962 3962 ASP ASP A . n 
A 1 3963 SER 3963 3963 3963 SER SER A . n 
A 1 3964 SER 3964 3964 3964 SER SER A . n 
A 1 3965 SER 3965 3965 3965 SER SER A . n 
A 1 3966 PRO 3966 3966 3966 PRO PRO A . n 
A 1 3967 GLU 3967 3967 3967 GLU GLU A . n 
A 1 3968 GLN 3968 3968 3968 GLN GLN A . n 
A 1 3969 THR 3969 3969 3969 THR THR A . n 
A 1 3970 VAL 3970 3970 3970 VAL VAL A . n 
A 1 3971 PRO 3971 3971 3971 PRO PRO A . n 
A 1 3972 TYR 3972 3972 3972 TYR TYR A . n 
A 1 3973 LEU 3973 3973 3973 LEU LEU A . n 
A 1 3974 TRP 3974 3974 3974 TRP TRP A . n 
A 1 3975 SER 3975 3975 3975 SER SER A . n 
A 1 3976 GLU 3976 3976 3976 GLU GLU A . n 
A 1 3977 GLU 3977 3977 3977 GLU GLU A . n 
A 1 3978 THR 3978 3978 3978 THR THR A . n 
A 1 3979 PRO 3979 3979 3979 PRO PRO A . n 
A 1 3980 ALA 3980 3980 3980 ALA ALA A . n 
A 1 3981 THR 3981 3981 3981 THR THR A . n 
A 1 3982 PRO 3982 3982 3982 PRO PRO A . n 
A 1 3983 ILE 3983 3983 3983 ILE ILE A . n 
A 1 3984 GLY 3984 3984 3984 GLY GLY A . n 
A 1 3985 GLN 3985 3985 3985 GLN GLN A . n 
A 1 3986 ALA 3986 3986 3986 ALA ALA A . n 
A 1 3987 ILE 3987 3987 3987 ILE ILE A . n 
A 1 3988 HIS 3988 3988 3988 HIS HIS A . n 
A 1 3989 ARG 3989 3989 3989 ARG ARG A . n 
A 1 3990 LEU 3990 3990 3990 LEU LEU A . n 
A 1 3991 LEU 3991 3991 3991 LEU LEU A . n 
A 1 3992 LEU 3992 3992 3992 LEU LEU A . n 
A 1 3993 ILE 3993 3993 3993 ILE ILE A . n 
A 1 3994 GLN 3994 3994 3994 GLN GLN A . n 
A 1 3995 ALA 3995 3995 3995 ALA ALA A . n 
A 1 3996 PHE 3996 3996 3996 PHE PHE A . n 
A 1 3997 ARG 3997 3997 3997 ARG ARG A . n 
A 1 3998 PRO 3998 3998 3998 PRO PRO A . n 
A 1 3999 ASP 3999 3999 3999 ASP ASP A . n 
A 1 4000 ARG 4000 4000 4000 ARG ARG A . n 
A 1 4001 LEU 4001 4001 4001 LEU LEU A . n 
A 1 4002 LEU 4002 4002 4002 LEU LEU A . n 
A 1 4003 ALA 4003 4003 4003 ALA ALA A . n 
A 1 4004 MET 4004 4004 4004 MET MET A . n 
A 1 4005 ALA 4005 4005 4005 ALA ALA A . n 
A 1 4006 HIS 4006 4006 4006 HIS HIS A . n 
A 1 4007 MET 4007 4007 4007 MET MET A . n 
A 1 4008 PHE 4008 4008 4008 PHE PHE A . n 
A 1 4009 VAL 4009 4009 4009 VAL VAL A . n 
A 1 4010 SER 4010 4010 4010 SER SER A . n 
A 1 4011 THR 4011 4011 4011 THR THR A . n 
A 1 4012 ASN 4012 4012 4012 ASN ASN A . n 
A 1 4013 LEU 4013 4013 4013 LEU LEU A . n 
A 1 4014 GLY 4014 4014 4014 GLY GLY A . n 
A 1 4015 GLU 4015 4015 4015 GLU GLU A . n 
A 1 4016 SER 4016 4016 4016 SER SER A . n 
A 1 4017 PHE 4017 4017 4017 PHE PHE A . n 
A 1 4018 MET 4018 4018 4018 MET MET A . n 
A 1 4019 SER 4019 4019 4019 SER SER A . n 
A 1 4020 ILE 4020 4020 4020 ILE ILE A . n 
A 1 4021 MET 4021 4021 4021 MET MET A . n 
A 1 4022 GLU 4022 4022 4022 GLU GLU A . n 
A 1 4023 GLN 4023 4023 4023 GLN GLN A . n 
A 1 4024 PRO 4024 4024 4024 PRO PRO A . n 
A 1 4025 LEU 4025 4025 4025 LEU LEU A . n 
A 1 4026 ASP 4026 4026 4026 ASP ASP A . n 
A 1 4027 LEU 4027 4027 4027 LEU LEU A . n 
A 1 4028 THR 4028 4028 4028 THR THR A . n 
A 1 4029 HIS 4029 4029 4029 HIS HIS A . n 
A 1 4030 ILE 4030 4030 4030 ILE ILE A . n 
A 1 4031 VAL 4031 4031 4031 VAL VAL A . n 
A 1 4032 GLY 4032 4032 4032 GLY GLY A . n 
A 1 4033 THR 4033 4033 4033 THR THR A . n 
A 1 4034 GLU 4034 4034 4034 GLU GLU A . n 
A 1 4035 VAL 4035 4035 4035 VAL VAL A . n 
A 1 4036 LYS 4036 4036 4036 LYS LYS A . n 
A 1 4037 PRO 4037 4037 4037 PRO PRO A . n 
A 1 4038 ASN 4038 4038 4038 ASN ASN A . n 
A 1 4039 THR 4039 4039 4039 THR THR A . n 
A 1 4040 PRO 4040 4040 4040 PRO PRO A . n 
A 1 4041 VAL 4041 4041 4041 VAL VAL A . n 
A 1 4042 LEU 4042 4042 4042 LEU LEU A . n 
A 1 4043 MET 4043 4043 4043 MET MET A . n 
A 1 4044 CYS 4044 4044 4044 CYS CYS A . n 
A 1 4045 SER 4045 4045 4045 SER SER A . n 
A 1 4046 VAL 4046 4046 4046 VAL VAL A . n 
A 1 4047 PRO 4047 4047 4047 PRO PRO A . n 
A 1 4048 GLY 4048 4048 4048 GLY GLY A . n 
A 1 4049 TYR 4049 4049 4049 TYR TYR A . n 
A 1 4050 ASP 4050 4050 4050 ASP ASP A . n 
A 1 4051 ALA 4051 4051 4051 ALA ALA A . n 
A 1 4052 SER 4052 4052 4052 SER SER A . n 
A 1 4053 GLY 4053 4053 4053 GLY GLY A . n 
A 1 4054 HIS 4054 4054 4054 HIS HIS A . n 
A 1 4055 VAL 4055 4055 4055 VAL VAL A . n 
A 1 4056 GLU 4056 4056 4056 GLU GLU A . n 
A 1 4057 ASP 4057 4057 4057 ASP ASP A . n 
A 1 4058 LEU 4058 4058 4058 LEU LEU A . n 
A 1 4059 ALA 4059 4059 4059 ALA ALA A . n 
A 1 4060 ALA 4060 4060 4060 ALA ALA A . n 
A 1 4061 GLU 4061 4061 4061 GLU GLU A . n 
A 1 4062 GLN 4062 4062 4062 GLN GLN A . n 
A 1 4063 ASN 4063 4063 4063 ASN ASN A . n 
A 1 4064 THR 4064 4064 4064 THR THR A . n 
A 1 4065 GLN 4065 4065 4065 GLN GLN A . n 
A 1 4066 ILE 4066 4066 4066 ILE ILE A . n 
A 1 4067 THR 4067 4067 4067 THR THR A . n 
A 1 4068 SER 4068 4068 4068 SER SER A . n 
A 1 4069 ILE 4069 4069 4069 ILE ILE A . n 
A 1 4070 ALA 4070 4070 4070 ALA ALA A . n 
A 1 4071 ILE 4071 4071 4071 ILE ILE A . n 
A 1 4072 GLY 4072 4072 4072 GLY GLY A . n 
A 1 4073 SER 4073 4073 4073 SER SER A . n 
A 1 4074 ALA 4074 4074 4074 ALA ALA A . n 
A 1 4075 GLU 4075 4075 4075 GLU GLU A . n 
A 1 4076 GLY 4076 4076 4076 GLY GLY A . n 
A 1 4077 PHE 4077 4077 4077 PHE PHE A . n 
A 1 4078 ASN 4078 4078 4078 ASN ASN A . n 
A 1 4079 GLN 4079 4079 4079 GLN GLN A . n 
A 1 4080 ALA 4080 4080 4080 ALA ALA A . n 
A 1 4081 ASP 4081 4081 4081 ASP ASP A . n 
A 1 4082 LYS 4082 4082 4082 LYS LYS A . n 
A 1 4083 ALA 4083 4083 4083 ALA ALA A . n 
A 1 4084 ILE 4084 4084 4084 ILE ILE A . n 
A 1 4085 ASN 4085 4085 4085 ASN ASN A . n 
A 1 4086 THR 4086 4086 4086 THR THR A . n 
A 1 4087 ALA 4087 4087 4087 ALA ALA A . n 
A 1 4088 VAL 4088 4088 4088 VAL VAL A . n 
A 1 4089 LYS 4089 4089 4089 LYS LYS A . n 
A 1 4090 SER 4090 4090 4090 SER SER A . n 
A 1 4091 GLY 4091 4091 4091 GLY GLY A . n 
A 1 4092 ARG 4092 4092 4092 ARG ARG A . n 
A 1 4093 TRP 4093 4093 4093 TRP TRP A . n 
A 1 4094 VAL 4094 4094 4094 VAL VAL A . n 
A 1 4095 MET 4095 4095 4095 MET MET A . n 
A 1 4096 LEU 4096 4096 4096 LEU LEU A . n 
A 1 4097 LYS 4097 4097 4097 LYS LYS A . n 
A 1 4098 ASN 4098 4098 4098 ASN ASN A . n 
A 1 4099 VAL 4099 4099 4099 VAL VAL A . n 
A 1 4100 HIS 4100 4100 4100 HIS HIS A . n 
A 1 4101 LEU 4101 4101 4101 LEU LEU A . n 
A 1 4102 ALA 4102 4102 4102 ALA ALA A . n 
A 1 4103 PRO 4103 4103 4103 PRO PRO A . n 
A 1 4104 GLY 4104 4104 4104 GLY GLY A . n 
A 1 4105 TRP 4105 4105 4105 TRP TRP A . n 
A 1 4106 LEU 4106 4106 4106 LEU LEU A . n 
A 1 4107 MET 4107 4107 4107 MET MET A . n 
A 1 4108 GLN 4108 4108 4108 GLN GLN A . n 
A 1 4109 LEU 4109 4109 4109 LEU LEU A . n 
A 1 4110 GLU 4110 4110 4110 GLU GLU A . n 
A 1 4111 LYS 4111 4111 4111 LYS LYS A . n 
A 1 4112 LYS 4112 4112 4112 LYS LYS A . n 
A 1 4113 LEU 4113 4113 4113 LEU LEU A . n 
A 1 4114 HIS 4114 4114 4114 HIS HIS A . n 
A 1 4115 SER 4115 4115 4115 SER SER A . n 
A 1 4116 LEU 4116 4116 4116 LEU LEU A . n 
A 1 4117 GLN 4117 4117 4117 GLN GLN A . n 
A 1 4118 PRO 4118 4118 4118 PRO PRO A . n 
A 1 4119 HIS 4119 4119 4119 HIS HIS A . n 
A 1 4120 ALA 4120 4120 4120 ALA ALA A . n 
A 1 4121 CYS 4121 4121 4121 CYS CYS A . n 
A 1 4122 PHE 4122 4122 4122 PHE PHE A . n 
A 1 4123 ARG 4123 4123 4123 ARG ARG A . n 
A 1 4124 LEU 4124 4124 4124 LEU LEU A . n 
A 1 4125 PHE 4125 4125 4125 PHE PHE A . n 
A 1 4126 LEU 4126 4126 4126 LEU LEU A . n 
A 1 4127 THR 4127 4127 4127 THR THR A . n 
A 1 4128 MET 4128 4128 4128 MET MET A . n 
A 1 4129 GLU 4129 4129 4129 GLU GLU A . n 
A 1 4130 ILE 4130 4130 4130 ILE ILE A . n 
A 1 4131 ASN 4131 4131 4131 ASN ASN A . n 
A 1 4132 PRO 4132 4132 4132 PRO PRO A . n 
A 1 4133 LYS 4133 4133 4133 LYS LYS A . n 
A 1 4134 VAL 4134 4134 4134 VAL VAL A . n 
A 1 4135 PRO 4135 4135 4135 PRO PRO A . n 
A 1 4136 VAL 4136 4136 4136 VAL VAL A . n 
A 1 4137 ASN 4137 4137 4137 ASN ASN A . n 
A 1 4138 LEU 4138 4138 4138 LEU LEU A . n 
A 1 4139 LEU 4139 4139 4139 LEU LEU A . n 
A 1 4140 ARG 4140 4140 4140 ARG ARG A . n 
A 1 4141 ALA 4141 4141 4141 ALA ALA A . n 
A 1 4142 GLY 4142 4142 4142 GLY GLY A . n 
A 1 4143 ARG 4143 4143 4143 ARG ARG A . n 
A 1 4144 ILE 4144 4144 4144 ILE ILE A . n 
A 1 4145 PHE 4145 4145 4145 PHE PHE A . n 
A 1 4146 VAL 4146 4146 4146 VAL VAL A . n 
A 1 4147 PHE 4147 4147 4147 PHE PHE A . n 
A 1 4148 GLU 4148 4148 4148 GLU GLU A . n 
A 1 4149 PRO 4149 4149 4149 PRO PRO A . n 
A 1 4150 PRO 4150 4150 4150 PRO PRO A . n 
A 1 4151 PRO 4151 4151 4151 PRO PRO A . n 
A 1 4152 GLY 4152 4152 4152 GLY GLY A . n 
A 1 4153 VAL 4153 4153 4153 VAL VAL A . n 
A 1 4154 LYS 4154 4154 4154 LYS LYS A . n 
A 1 4155 ALA 4155 4155 4155 ALA ALA A . n 
A 1 4156 ASN 4156 4156 4156 ASN ASN A . n 
A 1 4157 MET 4157 4157 4157 MET MET A . n 
A 1 4158 LEU 4158 4158 4158 LEU LEU A . n 
A 1 4159 ARG 4159 4159 4159 ARG ARG A . n 
A 1 4160 THR 4160 4160 4160 THR THR A . n 
A 1 4161 PHE 4161 4161 4161 PHE PHE A . n 
A 1 4162 SER 4162 4162 4162 SER SER A . n 
A 1 4163 SER 4163 4163 4163 SER SER A . n 
A 1 4164 ILE 4164 4164 4164 ILE ILE A . n 
A 1 4165 PRO 4165 4165 4165 PRO PRO A . n 
A 1 4166 VAL 4166 4166 4166 VAL VAL A . n 
A 1 4167 SER 4167 4167 4167 SER SER A . n 
A 1 4168 ARG 4168 4168 4168 ARG ARG A . n 
A 1 4169 ILE 4169 4169 4169 ILE ILE A . n 
A 1 4170 CYS 4170 4170 4170 CYS CYS A . n 
A 1 4171 LYS 4171 4171 4171 LYS LYS A . n 
A 1 4172 SER 4172 4172 4172 SER SER A . n 
A 1 4173 PRO 4173 4173 4173 PRO PRO A . n 
A 1 4174 ASN 4174 4174 4174 ASN ASN A . n 
A 1 4175 GLU 4175 4175 4175 GLU GLU A . n 
A 1 4176 ARG 4176 4176 4176 ARG ARG A . n 
A 1 4177 ALA 4177 4177 4177 ALA ALA A . n 
A 1 4178 ARG 4178 4178 4178 ARG ARG A . n 
A 1 4179 LEU 4179 4179 4179 LEU LEU A . n 
A 1 4180 TYR 4180 4180 4180 TYR TYR A . n 
A 1 4181 PHE 4181 4181 4181 PHE PHE A . n 
A 1 4182 LEU 4182 4182 4182 LEU LEU A . n 
A 1 4183 LEU 4183 4183 4183 LEU LEU A . n 
A 1 4184 ALA 4184 4184 4184 ALA ALA A . n 
A 1 4185 TRP 4185 4185 4185 TRP TRP A . n 
A 1 4186 PHE 4186 4186 4186 PHE PHE A . n 
A 1 4187 HIS 4187 4187 4187 HIS HIS A . n 
A 1 4188 ALA 4188 4188 4188 ALA ALA A . n 
A 1 4189 ILE 4189 4189 4189 ILE ILE A . n 
A 1 4190 ILE 4190 4190 4190 ILE ILE A . n 
A 1 4191 GLN 4191 4191 4191 GLN GLN A . n 
A 1 4192 GLU 4192 4192 4192 GLU GLU A . n 
A 1 4193 ARG 4193 4193 4193 ARG ARG A . n 
A 1 4194 LEU 4194 4194 4194 LEU LEU A . n 
A 1 4195 ARG 4195 4195 4195 ARG ARG A . n 
A 1 4196 TYR 4196 4196 4196 TYR TYR A . n 
A 1 4197 ALA 4197 4197 4197 ALA ALA A . n 
A 1 4198 PRO 4198 4198 4198 PRO PRO A . n 
A 1 4199 LEU 4199 4199 4199 LEU LEU A . n 
A 1 4200 GLY 4200 4200 4200 GLY GLY A . n 
A 1 4201 TRP 4201 4201 4201 TRP TRP A . n 
A 1 4202 SER 4202 4202 4202 SER SER A . n 
A 1 4203 LYS 4203 4203 4203 LYS LYS A . n 
A 1 4204 LYS 4204 4204 4204 LYS LYS A . n 
A 1 4205 TYR 4205 4205 4205 TYR TYR A . n 
A 1 4206 GLU 4206 4206 4206 GLU GLU A . n 
A 1 4207 PHE 4207 4207 4207 PHE PHE A . n 
A 1 4208 GLY 4208 4208 4208 GLY GLY A . n 
A 1 4209 GLU 4209 4209 4209 GLU GLU A . n 
A 1 4210 SER 4210 4210 4210 SER SER A . n 
A 1 4211 ASP 4211 4211 4211 ASP ASP A . n 
A 1 4212 LEU 4212 4212 4212 LEU LEU A . n 
A 1 4213 ARG 4213 4213 4213 ARG ARG A . n 
A 1 4214 SER 4214 4214 4214 SER SER A . n 
A 1 4215 ALA 4215 4215 4215 ALA ALA A . n 
A 1 4216 CYS 4216 4216 4216 CYS CYS A . n 
A 1 4217 ASP 4217 4217 4217 ASP ASP A . n 
A 1 4218 THR 4218 4218 4218 THR THR A . n 
A 1 4219 VAL 4219 4219 4219 VAL VAL A . n 
A 1 4220 ASP 4220 4220 4220 ASP ASP A . n 
A 1 4221 THR 4221 4221 4221 THR THR A . n 
A 1 4222 TRP 4222 4222 4222 TRP TRP A . n 
A 1 4223 LEU 4223 4223 4223 LEU LEU A . n 
A 1 4224 ASP 4224 4224 4224 ASP ASP A . n 
A 1 4225 ASP 4225 4225 4225 ASP ASP A . n 
A 1 4226 THR 4226 4226 4226 THR THR A . n 
A 1 4227 ALA 4227 4227 4227 ALA ALA A . n 
A 1 4228 LYS 4228 4228 4228 LYS LYS A . n 
A 1 4229 GLY 4229 4229 4229 GLY GLY A . n 
A 1 4230 ARG 4230 4230 4230 ARG ARG A . n 
A 1 4231 GLN 4231 4231 4231 GLN GLN A . n 
A 1 4232 ASN 4232 4232 4232 ASN ASN A . n 
A 1 4233 ILE 4233 4233 4233 ILE ILE A . n 
A 1 4234 SER 4234 4234 4234 SER SER A . n 
A 1 4235 PRO 4235 4235 4235 PRO PRO A . n 
A 1 4236 ASP 4236 4236 4236 ASP ASP A . n 
A 1 4237 LYS 4237 4237 4237 LYS LYS A . n 
A 1 4238 ILE 4238 4238 4238 ILE ILE A . n 
A 1 4239 PRO 4239 4239 4239 PRO PRO A . n 
A 1 4240 TRP 4240 4240 4240 TRP TRP A . n 
A 1 4241 SER 4241 4241 4241 SER SER A . n 
A 1 4242 ALA 4242 4242 4242 ALA ALA A . n 
A 1 4243 LEU 4243 4243 4243 LEU LEU A . n 
A 1 4244 LYS 4244 4244 4244 LYS LYS A . n 
A 1 4245 THR 4245 4245 4245 THR THR A . n 
A 1 4246 LEU 4246 4246 4246 LEU LEU A . n 
A 1 4247 MET 4247 4247 4247 MET MET A . n 
A 1 4248 ALA 4248 4248 4248 ALA ALA A . n 
A 1 4249 GLN 4249 4249 4249 GLN GLN A . n 
A 1 4250 SER 4250 4250 4250 SER SER A . n 
A 1 4251 ILE 4251 4251 4251 ILE ILE A . n 
A 1 4252 TYR 4252 4252 4252 TYR TYR A . n 
A 1 4253 GLY 4253 4253 4253 GLY GLY A . n 
A 1 4254 GLY 4254 4254 4254 GLY GLY A . n 
A 1 4255 ARG 4255 4255 4255 ARG ARG A . n 
A 1 4256 VAL 4256 4256 4256 VAL VAL A . n 
A 1 4257 ASP 4257 4257 4257 ASP ASP A . n 
A 1 4258 ASN 4258 4258 4258 ASN ASN A . n 
A 1 4259 GLU 4259 4259 4259 GLU GLU A . n 
A 1 4260 PHE 4260 4260 4260 PHE PHE A . n 
A 1 4261 ASP 4261 4261 4261 ASP ASP A . n 
A 1 4262 GLN 4262 4262 4262 GLN GLN A . n 
A 1 4263 ARG 4263 4263 4263 ARG ARG A . n 
A 1 4264 LEU 4264 4264 4264 LEU LEU A . n 
A 1 4265 LEU 4265 4265 4265 LEU LEU A . n 
A 1 4266 ASN 4266 4266 4266 ASN ASN A . n 
A 1 4267 THR 4267 4267 4267 THR THR A . n 
A 1 4268 PHE 4268 4268 4268 PHE PHE A . n 
A 1 4269 LEU 4269 4269 4269 LEU LEU A . n 
A 1 4270 GLU 4270 4270 4270 GLU GLU A . n 
A 1 4271 ARG 4271 4271 4271 ARG ARG A . n 
A 1 4272 LEU 4272 4272 4272 LEU LEU A . n 
A 1 4273 PHE 4273 4273 4273 PHE PHE A . n 
A 1 4274 THR 4274 4274 4274 THR THR A . n 
A 1 4275 THR 4275 4275 4275 THR THR A . n 
A 1 4276 ARG 4276 4276 4276 ARG ARG A . n 
A 1 4277 SER 4277 4277 4277 SER SER A . n 
A 1 4278 PHE 4278 4278 4278 PHE PHE A . n 
A 1 4279 ASP 4279 4279 4279 ASP ASP A . n 
A 1 4280 SER 4280 4280 4280 SER SER A . n 
A 1 4281 GLU 4281 4281 4281 GLU GLU A . n 
A 1 4282 PHE 4282 4282 4282 PHE PHE A . n 
A 1 4283 LYS 4283 4283 4283 LYS LYS A . n 
A 1 4284 LEU 4284 4284 4284 LEU LEU A . n 
A 1 4285 ALA 4285 4285 4285 ALA ALA A . n 
A 1 4286 CYS 4286 4286 4286 CYS CYS A . n 
A 1 4287 LYS 4287 4287 4287 LYS LYS A . n 
A 1 4288 VAL 4288 4288 4288 VAL VAL A . n 
A 1 4289 ASP 4289 4289 4289 ASP ASP A . n 
A 1 4290 GLY 4290 4290 4290 GLY GLY A . n 
A 1 4291 HIS 4291 4291 4291 HIS HIS A . n 
A 1 4292 LYS 4292 4292 4292 LYS LYS A . n 
A 1 4293 ASP 4293 4293 4293 ASP ASP A . n 
A 1 4294 ILE 4294 4294 4294 ILE ILE A . n 
A 1 4295 GLN 4295 4295 4295 GLN GLN A . n 
A 1 4296 MET 4296 4296 4296 MET MET A . n 
A 1 4297 PRO 4297 4297 4297 PRO PRO A . n 
A 1 4298 ASP 4298 4298 4298 ASP ASP A . n 
A 1 4299 GLY 4299 4299 4299 GLY GLY A . n 
A 1 4300 ILE 4300 4300 4300 ILE ILE A . n 
A 1 4301 ARG 4301 4301 4301 ARG ARG A . n 
A 1 4302 ARG 4302 4302 4302 ARG ARG A . n 
A 1 4303 GLU 4303 4303 4303 GLU GLU A . n 
A 1 4304 GLU 4304 4304 4304 GLU GLU A . n 
A 1 4305 PHE 4305 4305 4305 PHE PHE A . n 
A 1 4306 VAL 4306 4306 4306 VAL VAL A . n 
A 1 4307 GLN 4307 4307 4307 GLN GLN A . n 
A 1 4308 TRP 4308 4308 4308 TRP TRP A . n 
A 1 4309 VAL 4309 4309 4309 VAL VAL A . n 
A 1 4310 GLU 4310 4310 4310 GLU GLU A . n 
A 1 4311 LEU 4311 4311 4311 LEU LEU A . n 
A 1 4312 LEU 4312 4312 4312 LEU LEU A . n 
A 1 4313 PRO 4313 4313 4313 PRO PRO A . n 
A 1 4314 ASP 4314 4314 4314 ASP ASP A . n 
A 1 4315 THR 4315 4315 4315 THR THR A . n 
A 1 4316 GLN 4316 4316 4316 GLN GLN A . n 
A 1 4317 THR 4317 4317 4317 THR THR A . n 
A 1 4318 PRO 4318 4318 4318 PRO PRO A . n 
A 1 4319 SER 4319 4319 4319 SER SER A . n 
A 1 4320 TRP 4320 4320 4320 TRP TRP A . n 
A 1 4321 LEU 4321 4321 4321 LEU LEU A . n 
A 1 4322 GLY 4322 4322 4322 GLY GLY A . n 
A 1 4323 LEU 4323 4323 4323 LEU LEU A . n 
A 1 4324 PRO 4324 4324 4324 PRO PRO A . n 
A 1 4325 ASN 4325 4325 4325 ASN ASN A . n 
A 1 4326 ASN 4326 4326 4326 ASN ASN A . n 
A 1 4327 ALA 4327 4327 4327 ALA ALA A . n 
A 1 4328 GLU 4328 4328 4328 GLU GLU A . n 
A 1 4329 ARG 4329 4329 4329 ARG ARG A . n 
A 1 4330 VAL 4330 4330 4330 VAL VAL A . n 
A 1 4331 LEU 4331 4331 4331 LEU LEU A . n 
A 1 4332 LEU 4332 4332 4332 LEU LEU A . n 
A 1 4333 THR 4333 4333 4333 THR THR A . n 
A 1 4334 THR 4334 4334 4334 THR THR A . n 
A 1 4335 GLN 4335 4335 4335 GLN GLN A . n 
A 1 4336 GLY 4336 4336 4336 GLY GLY A . n 
A 1 4337 VAL 4337 4337 4337 VAL VAL A . n 
A 1 4338 ASP 4338 4338 4338 ASP ASP A . n 
A 1 4339 MET 4339 4339 4339 MET MET A . n 
A 1 4340 ILE 4340 4340 4340 ILE ILE A . n 
A 1 4341 SER 4341 4341 4341 SER SER A . n 
A 1 4342 LYS 4342 4342 4342 LYS LYS A . n 
A 1 4343 MET 4343 4343 4343 MET MET A . n 
A 1 4344 LEU 4344 4344 4344 LEU LEU A . n 
A 1 4345 LYS 4345 4345 4345 LYS LYS A . n 
A 1 4346 MET 4346 4346 4346 MET MET A . n 
A 1 4347 GLN 4347 4347 4347 GLN GLN A . n 
A 1 4348 MET 4348 4348 ?    ?   ?   A . n 
A 1 4349 LEU 4349 4349 ?    ?   ?   A . n 
A 1 4350 GLU 4350 4350 ?    ?   ?   A . n 
A 1 4351 ASP 4351 4351 ?    ?   ?   A . n 
A 1 4352 GLU 4352 4352 ?    ?   ?   A . n 
A 1 4353 ASP 4353 4353 ?    ?   ?   A . n 
A 1 4354 ASP 4354 4354 ?    ?   ?   A . n 
A 1 4355 LEU 4355 4355 ?    ?   ?   A . n 
A 1 4356 ALA 4356 4356 ?    ?   ?   A . n 
A 1 4357 TYR 4357 4357 ?    ?   ?   A . n 
A 1 4358 ALA 4358 4358 ?    ?   ?   A . n 
A 1 4359 GLU 4359 4359 ?    ?   ?   A . n 
A 1 4360 THR 4360 4360 ?    ?   ?   A . n 
A 1 4361 GLU 4361 4361 ?    ?   ?   A . n 
A 1 4362 LYS 4362 4362 ?    ?   ?   A . n 
A 1 4363 LYS 4363 4363 ?    ?   ?   A . n 
A 1 4364 THR 4364 4364 ?    ?   ?   A . n 
A 1 4365 ARG 4365 4365 ?    ?   ?   A . n 
A 1 4366 THR 4366 4366 ?    ?   ?   A . n 
A 1 4367 ASP 4367 4367 ?    ?   ?   A . n 
A 1 4368 SER 4368 4368 ?    ?   ?   A . n 
A 1 4369 THR 4369 4369 ?    ?   ?   A . n 
A 1 4370 SER 4370 4370 ?    ?   ?   A . n 
A 1 4371 ASP 4371 4371 ?    ?   ?   A . n 
A 1 4372 GLY 4372 4372 ?    ?   ?   A . n 
A 1 4373 ARG 4373 4373 ?    ?   ?   A . n 
A 1 4374 PRO 4374 4374 4374 PRO PRO A . n 
A 1 4375 ALA 4375 4375 4375 ALA ALA A . n 
A 1 4376 TRP 4376 4376 4376 TRP TRP A . n 
A 1 4377 MET 4377 4377 4377 MET MET A . n 
A 1 4378 ARG 4378 4378 4378 ARG ARG A . n 
A 1 4379 THR 4379 4379 4379 THR THR A . n 
A 1 4380 LEU 4380 4380 4380 LEU LEU A . n 
A 1 4381 HIS 4381 4381 4381 HIS HIS A . n 
A 1 4382 THR 4382 4382 4382 THR THR A . n 
A 1 4383 THR 4383 4383 4383 THR THR A . n 
A 1 4384 ALA 4384 4384 4384 ALA ALA A . n 
A 1 4385 SER 4385 4385 4385 SER SER A . n 
A 1 4386 ASN 4386 4386 4386 ASN ASN A . n 
A 1 4387 TRP 4387 4387 4387 TRP TRP A . n 
A 1 4388 LEU 4388 4388 4388 LEU LEU A . n 
A 1 4389 HIS 4389 4389 4389 HIS HIS A . n 
A 1 4390 LEU 4390 4390 4390 LEU LEU A . n 
A 1 4391 ILE 4391 4391 4391 ILE ILE A . n 
A 1 4392 PRO 4392 4392 4392 PRO PRO A . n 
A 1 4393 GLN 4393 4393 4393 GLN GLN A . n 
A 1 4394 THR 4394 4394 4394 THR THR A . n 
A 1 4395 LEU 4395 4395 4395 LEU LEU A . n 
A 1 4396 SER 4396 4396 4396 SER SER A . n 
A 1 4397 HIS 4397 4397 4397 HIS HIS A . n 
A 1 4398 LEU 4398 4398 4398 LEU LEU A . n 
A 1 4399 LYS 4399 4399 4399 LYS LYS A . n 
A 1 4400 ARG 4400 4400 4400 ARG ARG A . n 
A 1 4401 THR 4401 4401 4401 THR THR A . n 
A 1 4402 VAL 4402 4402 4402 VAL VAL A . n 
A 1 4403 GLU 4403 4403 4403 GLU GLU A . n 
A 1 4404 ASN 4404 4404 4404 ASN ASN A . n 
A 1 4405 ILE 4405 4405 4405 ILE ILE A . n 
A 1 4406 LYS 4406 4406 4406 LYS LYS A . n 
A 1 4407 ASP 4407 4407 4407 ASP ASP A . n 
A 1 4408 PRO 4408 4408 4408 PRO PRO A . n 
A 1 4409 LEU 4409 4409 4409 LEU LEU A . n 
A 1 4410 PHE 4410 4410 4410 PHE PHE A . n 
A 1 4411 ARG 4411 4411 4411 ARG ARG A . n 
A 1 4412 PHE 4412 4412 4412 PHE PHE A . n 
A 1 4413 PHE 4413 4413 4413 PHE PHE A . n 
A 1 4414 GLU 4414 4414 4414 GLU GLU A . n 
A 1 4415 ARG 4415 4415 4415 ARG ARG A . n 
A 1 4416 GLU 4416 4416 4416 GLU GLU A . n 
A 1 4417 VAL 4417 4417 4417 VAL VAL A . n 
A 1 4418 LYS 4418 4418 4418 LYS LYS A . n 
A 1 4419 MET 4419 4419 4419 MET MET A . n 
A 1 4420 GLY 4420 4420 4420 GLY GLY A . n 
A 1 4421 ALA 4421 4421 4421 ALA ALA A . n 
A 1 4422 LYS 4422 4422 4422 LYS LYS A . n 
A 1 4423 LEU 4423 4423 4423 LEU LEU A . n 
A 1 4424 LEU 4424 4424 4424 LEU LEU A . n 
A 1 4425 GLN 4425 4425 4425 GLN GLN A . n 
A 1 4426 ASP 4426 4426 4426 ASP ASP A . n 
A 1 4427 VAL 4427 4427 4427 VAL VAL A . n 
A 1 4428 ARG 4428 4428 4428 ARG ARG A . n 
A 1 4429 GLN 4429 4429 4429 GLN GLN A . n 
A 1 4430 ASP 4430 4430 4430 ASP ASP A . n 
A 1 4431 LEU 4431 4431 4431 LEU LEU A . n 
A 1 4432 ALA 4432 4432 4432 ALA ALA A . n 
A 1 4433 ASP 4433 4433 4433 ASP ASP A . n 
A 1 4434 VAL 4434 4434 4434 VAL VAL A . n 
A 1 4435 VAL 4435 4435 4435 VAL VAL A . n 
A 1 4436 GLN 4436 4436 4436 GLN GLN A . n 
A 1 4437 VAL 4437 4437 4437 VAL VAL A . n 
A 1 4438 CYS 4438 4438 4438 CYS CYS A . n 
A 1 4439 GLU 4439 4439 4439 GLU GLU A . n 
A 1 4440 GLY 4440 4440 4440 GLY GLY A . n 
A 1 4441 LYS 4441 4441 4441 LYS LYS A . n 
A 1 4442 LYS 4442 4442 4442 LYS LYS A . n 
A 1 4443 LYS 4443 4443 4443 LYS LYS A . n 
A 1 4444 GLN 4444 4444 4444 GLN GLN A . n 
A 1 4445 THR 4445 4445 4445 THR THR A . n 
A 1 4446 ASN 4446 4446 4446 ASN ASN A . n 
A 1 4447 TYR 4447 4447 4447 TYR TYR A . n 
A 1 4448 LEU 4448 4448 4448 LEU LEU A . n 
A 1 4449 ARG 4449 4449 4449 ARG ARG A . n 
A 1 4450 THR 4450 4450 4450 THR THR A . n 
A 1 4451 LEU 4451 4451 4451 LEU LEU A . n 
A 1 4452 ILE 4452 4452 4452 ILE ILE A . n 
A 1 4453 ASN 4453 4453 4453 ASN ASN A . n 
A 1 4454 GLU 4454 4454 4454 GLU GLU A . n 
A 1 4455 LEU 4455 4455 4455 LEU LEU A . n 
A 1 4456 VAL 4456 4456 4456 VAL VAL A . n 
A 1 4457 LYS 4457 4457 4457 LYS LYS A . n 
A 1 4458 GLY 4458 4458 4458 GLY GLY A . n 
A 1 4459 ILE 4459 4459 4459 ILE ILE A . n 
A 1 4460 LEU 4460 4460 4460 LEU LEU A . n 
A 1 4461 PRO 4461 4461 4461 PRO PRO A . n 
A 1 4462 ARG 4462 4462 4462 ARG ARG A . n 
A 1 4463 SER 4463 4463 4463 SER SER A . n 
A 1 4464 TRP 4464 4464 4464 TRP TRP A . n 
A 1 4465 SER 4465 4465 4465 SER SER A . n 
A 1 4466 HIS 4466 4466 4466 HIS HIS A . n 
A 1 4467 TYR 4467 4467 4467 TYR TYR A . n 
A 1 4468 THR 4468 4468 4468 THR THR A . n 
A 1 4469 VAL 4469 4469 4469 VAL VAL A . n 
A 1 4470 PRO 4470 4470 4470 PRO PRO A . n 
A 1 4471 ALA 4471 4471 4471 ALA ALA A . n 
A 1 4472 GLY 4472 4472 4472 GLY GLY A . n 
A 1 4473 MET 4473 4473 4473 MET MET A . n 
A 1 4474 THR 4474 4474 4474 THR THR A . n 
A 1 4475 VAL 4475 4475 4475 VAL VAL A . n 
A 1 4476 ILE 4476 4476 4476 ILE ILE A . n 
A 1 4477 GLN 4477 4477 4477 GLN GLN A . n 
A 1 4478 TRP 4478 4478 4478 TRP TRP A . n 
A 1 4479 VAL 4479 4479 4479 VAL VAL A . n 
A 1 4480 SER 4480 4480 4480 SER SER A . n 
A 1 4481 ASP 4481 4481 4481 ASP ASP A . n 
A 1 4482 PHE 4482 4482 4482 PHE PHE A . n 
A 1 4483 SER 4483 4483 4483 SER SER A . n 
A 1 4484 GLU 4484 4484 4484 GLU GLU A . n 
A 1 4485 ARG 4485 4485 4485 ARG ARG A . n 
A 1 4486 ILE 4486 4486 4486 ILE ILE A . n 
A 1 4487 LYS 4487 4487 4487 LYS LYS A . n 
A 1 4488 GLN 4488 4488 4488 GLN GLN A . n 
A 1 4489 LEU 4489 4489 4489 LEU LEU A . n 
A 1 4490 GLN 4490 4490 4490 GLN GLN A . n 
A 1 4491 ASN 4491 4491 4491 ASN ASN A . n 
A 1 4492 ILE 4492 4492 4492 ILE ILE A . n 
A 1 4493 SER 4493 4493 4493 SER SER A . n 
A 1 4494 LEU 4494 4494 4494 LEU LEU A . n 
A 1 4495 ALA 4495 4495 4495 ALA ALA A . n 
A 1 4496 ALA 4496 4496 4496 ALA ALA A . n 
A 1 4497 ALA 4497 4497 4497 ALA ALA A . n 
A 1 4498 SER 4498 4498 4498 SER SER A . n 
A 1 4499 GLY 4499 4499 4499 GLY GLY A . n 
A 1 4500 GLY 4500 4500 4500 GLY GLY A . n 
A 1 4501 ALA 4501 4501 4501 ALA ALA A . n 
A 1 4502 LYS 4502 4502 4502 LYS LYS A . n 
A 1 4503 GLU 4503 4503 4503 GLU GLU A . n 
A 1 4504 LEU 4504 4504 4504 LEU LEU A . n 
A 1 4505 LYS 4505 4505 4505 LYS LYS A . n 
A 1 4506 ASN 4506 4506 4506 ASN ASN A . n 
A 1 4507 ILE 4507 4507 4507 ILE ILE A . n 
A 1 4508 HIS 4508 4508 4508 HIS HIS A . n 
A 1 4509 VAL 4509 4509 4509 VAL VAL A . n 
A 1 4510 CYS 4510 4510 4510 CYS CYS A . n 
A 1 4511 LEU 4511 4511 4511 LEU LEU A . n 
A 1 4512 GLY 4512 4512 4512 GLY GLY A . n 
A 1 4513 GLY 4513 4513 4513 GLY GLY A . n 
A 1 4514 LEU 4514 4514 4514 LEU LEU A . n 
A 1 4515 PHE 4515 4515 4515 PHE PHE A . n 
A 1 4516 VAL 4516 4516 4516 VAL VAL A . n 
A 1 4517 PRO 4517 4517 4517 PRO PRO A . n 
A 1 4518 GLU 4518 4518 4518 GLU GLU A . n 
A 1 4519 ALA 4519 4519 4519 ALA ALA A . n 
A 1 4520 TYR 4520 4520 4520 TYR TYR A . n 
A 1 4521 ILE 4521 4521 4521 ILE ILE A . n 
A 1 4522 THR 4522 4522 4522 THR THR A . n 
A 1 4523 ALA 4523 4523 4523 ALA ALA A . n 
A 1 4524 THR 4524 4524 4524 THR THR A . n 
A 1 4525 ARG 4525 4525 4525 ARG ARG A . n 
A 1 4526 GLN 4526 4526 4526 GLN GLN A . n 
A 1 4527 TYR 4527 4527 4527 TYR TYR A . n 
A 1 4528 VAL 4528 4528 4528 VAL VAL A . n 
A 1 4529 ALA 4529 4529 4529 ALA ALA A . n 
A 1 4530 GLN 4530 4530 4530 GLN GLN A . n 
A 1 4531 ALA 4531 4531 4531 ALA ALA A . n 
A 1 4532 ASN 4532 4532 4532 ASN ASN A . n 
A 1 4533 SER 4533 4533 4533 SER SER A . n 
A 1 4534 TRP 4534 4534 4534 TRP TRP A . n 
A 1 4535 SER 4535 4535 4535 SER SER A . n 
A 1 4536 LEU 4536 4536 4536 LEU LEU A . n 
A 1 4537 GLU 4537 4537 4537 GLU GLU A . n 
A 1 4538 GLU 4538 4538 4538 GLU GLU A . n 
A 1 4539 LEU 4539 4539 4539 LEU LEU A . n 
A 1 4540 CYS 4540 4540 4540 CYS CYS A . n 
A 1 4541 LEU 4541 4541 4541 LEU LEU A . n 
A 1 4542 GLU 4542 4542 4542 GLU GLU A . n 
A 1 4543 VAL 4543 4543 4543 VAL VAL A . n 
A 1 4544 ASN 4544 4544 4544 ASN ASN A . n 
A 1 4545 VAL 4545 4545 4545 VAL VAL A . n 
A 1 4546 THR 4546 4546 4546 THR THR A . n 
A 1 4547 THR 4547 4547 4547 THR THR A . n 
A 1 4548 SER 4548 4548 4548 SER SER A . n 
A 1 4549 GLN 4549 4549 4549 GLN GLN A . n 
A 1 4550 GLY 4550 4550 4550 GLY GLY A . n 
A 1 4551 ALA 4551 4551 4551 ALA ALA A . n 
A 1 4552 THR 4552 4552 4552 THR THR A . n 
A 1 4553 LEU 4553 4553 4553 LEU LEU A . n 
A 1 4554 ASP 4554 4554 4554 ASP ASP A . n 
A 1 4555 ALA 4555 4555 4555 ALA ALA A . n 
A 1 4556 CYS 4556 4556 4556 CYS CYS A . n 
A 1 4557 SER 4557 4557 4557 SER SER A . n 
A 1 4558 PHE 4558 4558 4558 PHE PHE A . n 
A 1 4559 GLY 4559 4559 4559 GLY GLY A . n 
A 1 4560 VAL 4560 4560 4560 VAL VAL A . n 
A 1 4561 THR 4561 4561 4561 THR THR A . n 
A 1 4562 GLY 4562 4562 4562 GLY GLY A . n 
A 1 4563 LEU 4563 4563 4563 LEU LEU A . n 
A 1 4564 LYS 4564 4564 4564 LYS LYS A . n 
A 1 4565 LEU 4565 4565 4565 LEU LEU A . n 
A 1 4566 GLN 4566 4566 4566 GLN GLN A . n 
A 1 4567 GLY 4567 4567 4567 GLY GLY A . n 
A 1 4568 ALA 4568 4568 4568 ALA ALA A . n 
A 1 4569 THR 4569 4569 4569 THR THR A . n 
A 1 4570 CYS 4570 4570 4570 CYS CYS A . n 
A 1 4571 ASN 4571 4571 4571 ASN ASN A . n 
A 1 4572 ASN 4572 4572 4572 ASN ASN A . n 
A 1 4573 ASN 4573 4573 4573 ASN ASN A . n 
A 1 4574 LYS 4574 4574 4574 LYS LYS A . n 
A 1 4575 LEU 4575 4575 4575 LEU LEU A . n 
A 1 4576 SER 4576 4576 4576 SER SER A . n 
A 1 4577 LEU 4577 4577 4577 LEU LEU A . n 
A 1 4578 SER 4578 4578 4578 SER SER A . n 
A 1 4579 ASN 4579 4579 4579 ASN ASN A . n 
A 1 4580 ALA 4580 4580 4580 ALA ALA A . n 
A 1 4581 ILE 4581 4581 4581 ILE ILE A . n 
A 1 4582 SER 4582 4582 4582 SER SER A . n 
A 1 4583 THR 4583 4583 4583 THR THR A . n 
A 1 4584 ALA 4584 4584 4584 ALA ALA A . n 
A 1 4585 LEU 4585 4585 4585 LEU LEU A . n 
A 1 4586 PRO 4586 4586 4586 PRO PRO A . n 
A 1 4587 LEU 4587 4587 4587 LEU LEU A . n 
A 1 4588 THR 4588 4588 4588 THR THR A . n 
A 1 4589 GLN 4589 4589 4589 GLN GLN A . n 
A 1 4590 LEU 4590 4590 4590 LEU LEU A . n 
A 1 4591 ARG 4591 4591 4591 ARG ARG A . n 
A 1 4592 TRP 4592 4592 4592 TRP TRP A . n 
A 1 4593 VAL 4593 4593 4593 VAL VAL A . n 
A 1 4594 LYS 4594 4594 4594 LYS LYS A . n 
A 1 4595 GLN 4595 4595 4595 GLN GLN A . n 
A 1 4596 THR 4596 4596 4596 THR THR A . n 
A 1 4597 ASN 4597 4597 4597 ASN ASN A . n 
A 1 4598 THR 4598 4598 4598 THR THR A . n 
A 1 4599 GLU 4599 4599 4599 GLU GLU A . n 
A 1 4600 LYS 4600 4600 4600 LYS LYS A . n 
A 1 4601 LYS 4601 4601 4601 LYS LYS A . n 
A 1 4602 ALA 4602 4602 4602 ALA ALA A . n 
A 1 4603 SER 4603 4603 4603 SER SER A . n 
A 1 4604 VAL 4604 4604 4604 VAL VAL A . n 
A 1 4605 VAL 4605 4605 4605 VAL VAL A . n 
A 1 4606 THR 4606 4606 4606 THR THR A . n 
A 1 4607 LEU 4607 4607 4607 LEU LEU A . n 
A 1 4608 PRO 4608 4608 4608 PRO PRO A . n 
A 1 4609 VAL 4609 4609 4609 VAL VAL A . n 
A 1 4610 TYR 4610 4610 4610 TYR TYR A . n 
A 1 4611 LEU 4611 4611 4611 LEU LEU A . n 
A 1 4612 ASN 4612 4612 4612 ASN ASN A . n 
A 1 4613 PHE 4613 4613 4613 PHE PHE A . n 
A 1 4614 THR 4614 4614 4614 THR THR A . n 
A 1 4615 ARG 4615 4615 4615 ARG ARG A . n 
A 1 4616 ALA 4616 4616 4616 ALA ALA A . n 
A 1 4617 ASP 4617 4617 4617 ASP ASP A . n 
A 1 4618 LEU 4618 4618 4618 LEU LEU A . n 
A 1 4619 ILE 4619 4619 4619 ILE ILE A . n 
A 1 4620 PHE 4620 4620 4620 PHE PHE A . n 
A 1 4621 THR 4621 4621 4621 THR THR A . n 
A 1 4622 VAL 4622 4622 4622 VAL VAL A . n 
A 1 4623 ASP 4623 4623 4623 ASP ASP A . n 
A 1 4624 PHE 4624 4624 4624 PHE PHE A . n 
A 1 4625 GLU 4625 4625 4625 GLU GLU A . n 
A 1 4626 ILE 4626 4626 4626 ILE ILE A . n 
A 1 4627 ALA 4627 4627 4627 ALA ALA A . n 
A 1 4628 THR 4628 4628 4628 THR THR A . n 
A 1 4629 LYS 4629 4629 4629 LYS LYS A . n 
A 1 4630 GLU 4630 4630 4630 GLU GLU A . n 
A 1 4631 ASP 4631 4631 4631 ASP ASP A . n 
A 1 4632 PRO 4632 4632 4632 PRO PRO A . n 
A 1 4633 ARG 4633 4633 4633 ARG ARG A . n 
A 1 4634 SER 4634 4634 4634 SER SER A . n 
A 1 4635 PHE 4635 4635 4635 PHE PHE A . n 
A 1 4636 TYR 4636 4636 4636 TYR TYR A . n 
A 1 4637 GLU 4637 4637 4637 GLU GLU A . n 
A 1 4638 ARG 4638 4638 4638 ARG ARG A . n 
A 1 4639 GLY 4639 4639 4639 GLY GLY A . n 
A 1 4640 VAL 4640 4640 4640 VAL VAL A . n 
A 1 4641 ALA 4641 4641 4641 ALA ALA A . n 
A 1 4642 VAL 4642 4642 4642 VAL VAL A . n 
A 1 4643 LEU 4643 4643 4643 LEU LEU A . n 
A 1 4644 CYS 4644 4644 4644 CYS CYS A . n 
A 1 4645 THR 4645 4645 4645 THR THR A . n 
A 1 4646 GLU 4646 4646 ?    ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ADP 1    4701 4701 ADP ADP A . 
C 3 ATP 1    4702 4702 ATP ATP A . 
D 2 ADP 1    4703 4703 ADP ADP A . 
E 2 ADP 1    4704 4704 ADP ADP A . 
F 4 MG  1    4705 4705 MG  MG  A . 
G 4 MG  1    4706 4706 MG  MG  A . 
H 5 HOH 1    4801 685  HOH HOH A . 
H 5 HOH 2    4802 757  HOH HOH A . 
H 5 HOH 3    4803 1941 HOH HOH A . 
H 5 HOH 4    4804 1853 HOH HOH A . 
H 5 HOH 5    4805 1158 HOH HOH A . 
H 5 HOH 6    4806 867  HOH HOH A . 
H 5 HOH 7    4807 1743 HOH HOH A . 
H 5 HOH 8    4808 1380 HOH HOH A . 
H 5 HOH 9    4809 1164 HOH HOH A . 
H 5 HOH 10   4810 1912 HOH HOH A . 
H 5 HOH 11   4811 1801 HOH HOH A . 
H 5 HOH 12   4812 2269 HOH HOH A . 
H 5 HOH 13   4813 1307 HOH HOH A . 
H 5 HOH 14   4814 704  HOH HOH A . 
H 5 HOH 15   4815 476  HOH HOH A . 
H 5 HOH 16   4816 1282 HOH HOH A . 
H 5 HOH 17   4817 614  HOH HOH A . 
H 5 HOH 18   4818 1774 HOH HOH A . 
H 5 HOH 19   4819 1392 HOH HOH A . 
H 5 HOH 20   4820 1662 HOH HOH A . 
H 5 HOH 21   4821 1675 HOH HOH A . 
H 5 HOH 22   4822 660  HOH HOH A . 
H 5 HOH 23   4823 2324 HOH HOH A . 
H 5 HOH 24   4824 554  HOH HOH A . 
H 5 HOH 25   4825 2181 HOH HOH A . 
H 5 HOH 26   4826 1383 HOH HOH A . 
H 5 HOH 27   4827 1971 HOH HOH A . 
H 5 HOH 28   4828 1752 HOH HOH A . 
H 5 HOH 29   4829 487  HOH HOH A . 
H 5 HOH 30   4830 616  HOH HOH A . 
H 5 HOH 31   4831 2126 HOH HOH A . 
H 5 HOH 32   4832 1446 HOH HOH A . 
H 5 HOH 33   4833 2014 HOH HOH A . 
H 5 HOH 34   4834 1616 HOH HOH A . 
H 5 HOH 35   4835 1767 HOH HOH A . 
H 5 HOH 36   4836 1805 HOH HOH A . 
H 5 HOH 37   4837 1928 HOH HOH A . 
H 5 HOH 38   4838 2039 HOH HOH A . 
H 5 HOH 39   4839 1560 HOH HOH A . 
H 5 HOH 40   4840 893  HOH HOH A . 
H 5 HOH 41   4841 1932 HOH HOH A . 
H 5 HOH 42   4842 766  HOH HOH A . 
H 5 HOH 43   4843 1363 HOH HOH A . 
H 5 HOH 44   4844 1854 HOH HOH A . 
H 5 HOH 45   4845 706  HOH HOH A . 
H 5 HOH 46   4846 2152 HOH HOH A . 
H 5 HOH 47   4847 1755 HOH HOH A . 
H 5 HOH 48   4848 1803 HOH HOH A . 
H 5 HOH 49   4849 525  HOH HOH A . 
H 5 HOH 50   4850 1525 HOH HOH A . 
H 5 HOH 51   4851 1162 HOH HOH A . 
H 5 HOH 52   4852 2228 HOH HOH A . 
H 5 HOH 53   4853 593  HOH HOH A . 
H 5 HOH 54   4854 1140 HOH HOH A . 
H 5 HOH 55   4855 1130 HOH HOH A . 
H 5 HOH 56   4856 1122 HOH HOH A . 
H 5 HOH 57   4857 474  HOH HOH A . 
H 5 HOH 58   4858 1470 HOH HOH A . 
H 5 HOH 59   4859 1504 HOH HOH A . 
H 5 HOH 60   4860 1351 HOH HOH A . 
H 5 HOH 61   4861 2070 HOH HOH A . 
H 5 HOH 62   4862 832  HOH HOH A . 
H 5 HOH 63   4863 1373 HOH HOH A . 
H 5 HOH 64   4864 606  HOH HOH A . 
H 5 HOH 65   4865 1442 HOH HOH A . 
H 5 HOH 66   4866 1710 HOH HOH A . 
H 5 HOH 67   4867 1058 HOH HOH A . 
H 5 HOH 68   4868 1636 HOH HOH A . 
H 5 HOH 69   4869 1951 HOH HOH A . 
H 5 HOH 70   4870 1285 HOH HOH A . 
H 5 HOH 71   4871 1417 HOH HOH A . 
H 5 HOH 72   4872 1489 HOH HOH A . 
H 5 HOH 73   4873 2251 HOH HOH A . 
H 5 HOH 74   4874 1354 HOH HOH A . 
H 5 HOH 75   4875 741  HOH HOH A . 
H 5 HOH 76   4876 1017 HOH HOH A . 
H 5 HOH 77   4877 1601 HOH HOH A . 
H 5 HOH 78   4878 2192 HOH HOH A . 
H 5 HOH 79   4879 1678 HOH HOH A . 
H 5 HOH 80   4880 1210 HOH HOH A . 
H 5 HOH 81   4881 2174 HOH HOH A . 
H 5 HOH 82   4882 2293 HOH HOH A . 
H 5 HOH 83   4883 1405 HOH HOH A . 
H 5 HOH 84   4884 2136 HOH HOH A . 
H 5 HOH 85   4885 459  HOH HOH A . 
H 5 HOH 86   4886 1920 HOH HOH A . 
H 5 HOH 87   4887 433  HOH HOH A . 
H 5 HOH 88   4888 2011 HOH HOH A . 
H 5 HOH 89   4889 817  HOH HOH A . 
H 5 HOH 90   4890 1406 HOH HOH A . 
H 5 HOH 91   4891 896  HOH HOH A . 
H 5 HOH 92   4892 1682 HOH HOH A . 
H 5 HOH 93   4893 619  HOH HOH A . 
H 5 HOH 94   4894 1834 HOH HOH A . 
H 5 HOH 95   4895 1357 HOH HOH A . 
H 5 HOH 96   4896 1653 HOH HOH A . 
H 5 HOH 97   4897 1335 HOH HOH A . 
H 5 HOH 98   4898 1577 HOH HOH A . 
H 5 HOH 99   4899 1996 HOH HOH A . 
H 5 HOH 100  4900 1956 HOH HOH A . 
H 5 HOH 101  4901 1055 HOH HOH A . 
H 5 HOH 102  4902 1864 HOH HOH A . 
H 5 HOH 103  4903 998  HOH HOH A . 
H 5 HOH 104  4904 802  HOH HOH A . 
H 5 HOH 105  4905 504  HOH HOH A . 
H 5 HOH 106  4906 1338 HOH HOH A . 
H 5 HOH 107  4907 2144 HOH HOH A . 
H 5 HOH 108  4908 430  HOH HOH A . 
H 5 HOH 109  4909 1145 HOH HOH A . 
H 5 HOH 110  4910 1155 HOH HOH A . 
H 5 HOH 111  4911 2252 HOH HOH A . 
H 5 HOH 112  4912 631  HOH HOH A . 
H 5 HOH 113  4913 1843 HOH HOH A . 
H 5 HOH 114  4914 1924 HOH HOH A . 
H 5 HOH 115  4915 444  HOH HOH A . 
H 5 HOH 116  4916 1233 HOH HOH A . 
H 5 HOH 117  4917 1815 HOH HOH A . 
H 5 HOH 118  4918 1479 HOH HOH A . 
H 5 HOH 119  4919 545  HOH HOH A . 
H 5 HOH 120  4920 1314 HOH HOH A . 
H 5 HOH 121  4921 1428 HOH HOH A . 
H 5 HOH 122  4922 881  HOH HOH A . 
H 5 HOH 123  4923 1115 HOH HOH A . 
H 5 HOH 124  4924 1009 HOH HOH A . 
H 5 HOH 125  4925 1441 HOH HOH A . 
H 5 HOH 126  4926 957  HOH HOH A . 
H 5 HOH 127  4927 601  HOH HOH A . 
H 5 HOH 128  4928 1200 HOH HOH A . 
H 5 HOH 129  4929 1572 HOH HOH A . 
H 5 HOH 130  4930 1269 HOH HOH A . 
H 5 HOH 131  4931 1772 HOH HOH A . 
H 5 HOH 132  4932 1013 HOH HOH A . 
H 5 HOH 133  4933 524  HOH HOH A . 
H 5 HOH 134  4934 533  HOH HOH A . 
H 5 HOH 135  4935 1680 HOH HOH A . 
H 5 HOH 136  4936 772  HOH HOH A . 
H 5 HOH 137  4937 1382 HOH HOH A . 
H 5 HOH 138  4938 552  HOH HOH A . 
H 5 HOH 139  4939 894  HOH HOH A . 
H 5 HOH 140  4940 1384 HOH HOH A . 
H 5 HOH 141  4941 635  HOH HOH A . 
H 5 HOH 142  4942 587  HOH HOH A . 
H 5 HOH 143  4943 510  HOH HOH A . 
H 5 HOH 144  4944 938  HOH HOH A . 
H 5 HOH 145  4945 1301 HOH HOH A . 
H 5 HOH 146  4946 2110 HOH HOH A . 
H 5 HOH 147  4947 1873 HOH HOH A . 
H 5 HOH 148  4948 912  HOH HOH A . 
H 5 HOH 149  4949 1468 HOH HOH A . 
H 5 HOH 150  4950 1007 HOH HOH A . 
H 5 HOH 151  4951 1870 HOH HOH A . 
H 5 HOH 152  4952 1673 HOH HOH A . 
H 5 HOH 153  4953 1809 HOH HOH A . 
H 5 HOH 154  4954 472  HOH HOH A . 
H 5 HOH 155  4955 740  HOH HOH A . 
H 5 HOH 156  4956 577  HOH HOH A . 
H 5 HOH 157  4957 799  HOH HOH A . 
H 5 HOH 158  4958 1129 HOH HOH A . 
H 5 HOH 159  4959 2062 HOH HOH A . 
H 5 HOH 160  4960 2019 HOH HOH A . 
H 5 HOH 161  4961 1790 HOH HOH A . 
H 5 HOH 162  4962 154  HOH HOH A . 
H 5 HOH 163  4963 1876 HOH HOH A . 
H 5 HOH 164  4964 1474 HOH HOH A . 
H 5 HOH 165  4965 503  HOH HOH A . 
H 5 HOH 166  4966 1808 HOH HOH A . 
H 5 HOH 167  4967 1685 HOH HOH A . 
H 5 HOH 168  4968 557  HOH HOH A . 
H 5 HOH 169  4969 1543 HOH HOH A . 
H 5 HOH 170  4970 1940 HOH HOH A . 
H 5 HOH 171  4971 1111 HOH HOH A . 
H 5 HOH 172  4972 1344 HOH HOH A . 
H 5 HOH 173  4973 946  HOH HOH A . 
H 5 HOH 174  4974 1850 HOH HOH A . 
H 5 HOH 175  4975 1311 HOH HOH A . 
H 5 HOH 176  4976 473  HOH HOH A . 
H 5 HOH 177  4977 665  HOH HOH A . 
H 5 HOH 178  4978 1420 HOH HOH A . 
H 5 HOH 179  4979 800  HOH HOH A . 
H 5 HOH 180  4980 1882 HOH HOH A . 
H 5 HOH 181  4981 1411 HOH HOH A . 
H 5 HOH 182  4982 705  HOH HOH A . 
H 5 HOH 183  4983 1704 HOH HOH A . 
H 5 HOH 184  4984 776  HOH HOH A . 
H 5 HOH 185  4985 1473 HOH HOH A . 
H 5 HOH 186  4986 1520 HOH HOH A . 
H 5 HOH 187  4987 622  HOH HOH A . 
H 5 HOH 188  4988 1377 HOH HOH A . 
H 5 HOH 189  4989 1989 HOH HOH A . 
H 5 HOH 190  4990 1535 HOH HOH A . 
H 5 HOH 191  4991 1770 HOH HOH A . 
H 5 HOH 192  4992 901  HOH HOH A . 
H 5 HOH 193  4993 1245 HOH HOH A . 
H 5 HOH 194  4994 1448 HOH HOH A . 
H 5 HOH 195  4995 1356 HOH HOH A . 
H 5 HOH 196  4996 1665 HOH HOH A . 
H 5 HOH 197  4997 2259 HOH HOH A . 
H 5 HOH 198  4998 2151 HOH HOH A . 
H 5 HOH 199  4999 1603 HOH HOH A . 
H 5 HOH 200  5000 1863 HOH HOH A . 
H 5 HOH 201  5001 673  HOH HOH A . 
H 5 HOH 202  5002 2111 HOH HOH A . 
H 5 HOH 203  5003 963  HOH HOH A . 
H 5 HOH 204  5004 629  HOH HOH A . 
H 5 HOH 205  5005 952  HOH HOH A . 
H 5 HOH 206  5006 966  HOH HOH A . 
H 5 HOH 207  5007 2217 HOH HOH A . 
H 5 HOH 208  5008 746  HOH HOH A . 
H 5 HOH 209  5009 773  HOH HOH A . 
H 5 HOH 210  5010 1353 HOH HOH A . 
H 5 HOH 211  5011 1488 HOH HOH A . 
H 5 HOH 212  5012 2223 HOH HOH A . 
H 5 HOH 213  5013 978  HOH HOH A . 
H 5 HOH 214  5014 516  HOH HOH A . 
H 5 HOH 215  5015 2187 HOH HOH A . 
H 5 HOH 216  5016 883  HOH HOH A . 
H 5 HOH 217  5017 1044 HOH HOH A . 
H 5 HOH 218  5018 1352 HOH HOH A . 
H 5 HOH 219  5019 2099 HOH HOH A . 
H 5 HOH 220  5020 436  HOH HOH A . 
H 5 HOH 221  5021 1762 HOH HOH A . 
H 5 HOH 222  5022 852  HOH HOH A . 
H 5 HOH 223  5023 1599 HOH HOH A . 
H 5 HOH 224  5024 924  HOH HOH A . 
H 5 HOH 225  5025 856  HOH HOH A . 
H 5 HOH 226  5026 2146 HOH HOH A . 
H 5 HOH 227  5027 559  HOH HOH A . 
H 5 HOH 228  5028 1742 HOH HOH A . 
H 5 HOH 229  5029 2005 HOH HOH A . 
H 5 HOH 230  5030 1015 HOH HOH A . 
H 5 HOH 231  5031 2141 HOH HOH A . 
H 5 HOH 232  5032 1897 HOH HOH A . 
H 5 HOH 233  5033 2095 HOH HOH A . 
H 5 HOH 234  5034 742  HOH HOH A . 
H 5 HOH 235  5035 1708 HOH HOH A . 
H 5 HOH 236  5036 916  HOH HOH A . 
H 5 HOH 237  5037 2284 HOH HOH A . 
H 5 HOH 238  5038 523  HOH HOH A . 
H 5 HOH 239  5039 1365 HOH HOH A . 
H 5 HOH 240  5040 1280 HOH HOH A . 
H 5 HOH 241  5041 1202 HOH HOH A . 
H 5 HOH 242  5042 612  HOH HOH A . 
H 5 HOH 243  5043 457  HOH HOH A . 
H 5 HOH 244  5044 769  HOH HOH A . 
H 5 HOH 245  5045 1005 HOH HOH A . 
H 5 HOH 246  5046 1831 HOH HOH A . 
H 5 HOH 247  5047 567  HOH HOH A . 
H 5 HOH 248  5048 1039 HOH HOH A . 
H 5 HOH 249  5049 1270 HOH HOH A . 
H 5 HOH 250  5050 804  HOH HOH A . 
H 5 HOH 251  5051 1444 HOH HOH A . 
H 5 HOH 252  5052 497  HOH HOH A . 
H 5 HOH 253  5053 1731 HOH HOH A . 
H 5 HOH 254  5054 718  HOH HOH A . 
H 5 HOH 255  5055 1487 HOH HOH A . 
H 5 HOH 256  5056 2003 HOH HOH A . 
H 5 HOH 257  5057 1524 HOH HOH A . 
H 5 HOH 258  5058 2317 HOH HOH A . 
H 5 HOH 259  5059 825  HOH HOH A . 
H 5 HOH 260  5060 2218 HOH HOH A . 
H 5 HOH 261  5061 464  HOH HOH A . 
H 5 HOH 262  5062 739  HOH HOH A . 
H 5 HOH 263  5063 1332 HOH HOH A . 
H 5 HOH 264  5064 2051 HOH HOH A . 
H 5 HOH 265  5065 1551 HOH HOH A . 
H 5 HOH 266  5066 2262 HOH HOH A . 
H 5 HOH 267  5067 561  HOH HOH A . 
H 5 HOH 268  5068 1780 HOH HOH A . 
H 5 HOH 269  5069 1674 HOH HOH A . 
H 5 HOH 270  5070 1483 HOH HOH A . 
H 5 HOH 271  5071 2155 HOH HOH A . 
H 5 HOH 272  5072 1317 HOH HOH A . 
H 5 HOH 273  5073 570  HOH HOH A . 
H 5 HOH 274  5074 1707 HOH HOH A . 
H 5 HOH 275  5075 1679 HOH HOH A . 
H 5 HOH 276  5076 664  HOH HOH A . 
H 5 HOH 277  5077 2313 HOH HOH A . 
H 5 HOH 278  5078 2287 HOH HOH A . 
H 5 HOH 279  5079 1016 HOH HOH A . 
H 5 HOH 280  5080 770  HOH HOH A . 
H 5 HOH 281  5081 1169 HOH HOH A . 
H 5 HOH 282  5082 1947 HOH HOH A . 
H 5 HOH 283  5083 439  HOH HOH A . 
H 5 HOH 284  5084 925  HOH HOH A . 
H 5 HOH 285  5085 874  HOH HOH A . 
H 5 HOH 286  5086 1038 HOH HOH A . 
H 5 HOH 287  5087 1660 HOH HOH A . 
H 5 HOH 288  5088 1025 HOH HOH A . 
H 5 HOH 289  5089 452  HOH HOH A . 
H 5 HOH 290  5090 1569 HOH HOH A . 
H 5 HOH 291  5091 721  HOH HOH A . 
H 5 HOH 292  5092 1594 HOH HOH A . 
H 5 HOH 293  5093 677  HOH HOH A . 
H 5 HOH 294  5094 726  HOH HOH A . 
H 5 HOH 295  5095 594  HOH HOH A . 
H 5 HOH 296  5096 710  HOH HOH A . 
H 5 HOH 297  5097 1079 HOH HOH A . 
H 5 HOH 298  5098 1042 HOH HOH A . 
H 5 HOH 299  5099 500  HOH HOH A . 
H 5 HOH 300  5100 1271 HOH HOH A . 
H 5 HOH 301  5101 1851 HOH HOH A . 
H 5 HOH 302  5102 2279 HOH HOH A . 
H 5 HOH 303  5103 538  HOH HOH A . 
H 5 HOH 304  5104 1213 HOH HOH A . 
H 5 HOH 305  5105 1304 HOH HOH A . 
H 5 HOH 306  5106 466  HOH HOH A . 
H 5 HOH 307  5107 1391 HOH HOH A . 
H 5 HOH 308  5108 671  HOH HOH A . 
H 5 HOH 309  5109 847  HOH HOH A . 
H 5 HOH 310  5110 1027 HOH HOH A . 
H 5 HOH 311  5111 2239 HOH HOH A . 
H 5 HOH 312  5112 1303 HOH HOH A . 
H 5 HOH 313  5113 600  HOH HOH A . 
H 5 HOH 314  5114 1586 HOH HOH A . 
H 5 HOH 315  5115 1262 HOH HOH A . 
H 5 HOH 316  5116 2052 HOH HOH A . 
H 5 HOH 317  5117 623  HOH HOH A . 
H 5 HOH 318  5118 1472 HOH HOH A . 
H 5 HOH 319  5119 1341 HOH HOH A . 
H 5 HOH 320  5120 646  HOH HOH A . 
H 5 HOH 321  5121 1658 HOH HOH A . 
H 5 HOH 322  5122 954  HOH HOH A . 
H 5 HOH 323  5123 1692 HOH HOH A . 
H 5 HOH 324  5124 1782 HOH HOH A . 
H 5 HOH 325  5125 1961 HOH HOH A . 
H 5 HOH 326  5126 2129 HOH HOH A . 
H 5 HOH 327  5127 875  HOH HOH A . 
H 5 HOH 328  5128 1085 HOH HOH A . 
H 5 HOH 329  5129 948  HOH HOH A . 
H 5 HOH 330  5130 1862 HOH HOH A . 
H 5 HOH 331  5131 518  HOH HOH A . 
H 5 HOH 332  5132 431  HOH HOH A . 
H 5 HOH 333  5133 1033 HOH HOH A . 
H 5 HOH 334  5134 834  HOH HOH A . 
H 5 HOH 335  5135 1950 HOH HOH A . 
H 5 HOH 336  5136 857  HOH HOH A . 
H 5 HOH 337  5137 2315 HOH HOH A . 
H 5 HOH 338  5138 475  HOH HOH A . 
H 5 HOH 339  5139 546  HOH HOH A . 
H 5 HOH 340  5140 1074 HOH HOH A . 
H 5 HOH 341  5141 1527 HOH HOH A . 
H 5 HOH 342  5142 633  HOH HOH A . 
H 5 HOH 343  5143 1367 HOH HOH A . 
H 5 HOH 344  5144 1466 HOH HOH A . 
H 5 HOH 345  5145 1152 HOH HOH A . 
H 5 HOH 346  5146 970  HOH HOH A . 
H 5 HOH 347  5147 1884 HOH HOH A . 
H 5 HOH 348  5148 1242 HOH HOH A . 
H 5 HOH 349  5149 2233 HOH HOH A . 
H 5 HOH 350  5150 2008 HOH HOH A . 
H 5 HOH 351  5151 1097 HOH HOH A . 
H 5 HOH 352  5152 1093 HOH HOH A . 
H 5 HOH 353  5153 1327 HOH HOH A . 
H 5 HOH 354  5154 796  HOH HOH A . 
H 5 HOH 355  5155 2130 HOH HOH A . 
H 5 HOH 356  5156 2137 HOH HOH A . 
H 5 HOH 357  5157 1757 HOH HOH A . 
H 5 HOH 358  5158 442  HOH HOH A . 
H 5 HOH 359  5159 1043 HOH HOH A . 
H 5 HOH 360  5160 539  HOH HOH A . 
H 5 HOH 361  5161 1847 HOH HOH A . 
H 5 HOH 362  5162 585  HOH HOH A . 
H 5 HOH 363  5163 558  HOH HOH A . 
H 5 HOH 364  5164 1266 HOH HOH A . 
H 5 HOH 365  5165 1050 HOH HOH A . 
H 5 HOH 366  5166 581  HOH HOH A . 
H 5 HOH 367  5167 1939 HOH HOH A . 
H 5 HOH 368  5168 595  HOH HOH A . 
H 5 HOH 369  5169 1192 HOH HOH A . 
H 5 HOH 370  5170 634  HOH HOH A . 
H 5 HOH 371  5171 1538 HOH HOH A . 
H 5 HOH 372  5172 494  HOH HOH A . 
H 5 HOH 373  5173 1267 HOH HOH A . 
H 5 HOH 374  5174 864  HOH HOH A . 
H 5 HOH 375  5175 576  HOH HOH A . 
H 5 HOH 376  5176 1565 HOH HOH A . 
H 5 HOH 377  5177 783  HOH HOH A . 
H 5 HOH 378  5178 1056 HOH HOH A . 
H 5 HOH 379  5179 1732 HOH HOH A . 
H 5 HOH 380  5180 758  HOH HOH A . 
H 5 HOH 381  5181 1720 HOH HOH A . 
H 5 HOH 382  5182 701  HOH HOH A . 
H 5 HOH 383  5183 764  HOH HOH A . 
H 5 HOH 384  5184 1161 HOH HOH A . 
H 5 HOH 385  5185 1754 HOH HOH A . 
H 5 HOH 386  5186 1396 HOH HOH A . 
H 5 HOH 387  5187 767  HOH HOH A . 
H 5 HOH 388  5188 485  HOH HOH A . 
H 5 HOH 389  5189 672  HOH HOH A . 
H 5 HOH 390  5190 1914 HOH HOH A . 
H 5 HOH 391  5191 2214 HOH HOH A . 
H 5 HOH 392  5192 1505 HOH HOH A . 
H 5 HOH 393  5193 1727 HOH HOH A . 
H 5 HOH 394  5194 1857 HOH HOH A . 
H 5 HOH 395  5195 1310 HOH HOH A . 
H 5 HOH 396  5196 586  HOH HOH A . 
H 5 HOH 397  5197 890  HOH HOH A . 
H 5 HOH 398  5198 541  HOH HOH A . 
H 5 HOH 399  5199 1907 HOH HOH A . 
H 5 HOH 400  5200 984  HOH HOH A . 
H 5 HOH 401  5201 479  HOH HOH A . 
H 5 HOH 402  5202 1963 HOH HOH A . 
H 5 HOH 403  5203 492  HOH HOH A . 
H 5 HOH 404  5204 2071 HOH HOH A . 
H 5 HOH 405  5205 1045 HOH HOH A . 
H 5 HOH 406  5206 2204 HOH HOH A . 
H 5 HOH 407  5207 604  HOH HOH A . 
H 5 HOH 408  5208 849  HOH HOH A . 
H 5 HOH 409  5209 661  HOH HOH A . 
H 5 HOH 410  5210 2033 HOH HOH A . 
H 5 HOH 411  5211 531  HOH HOH A . 
H 5 HOH 412  5212 1386 HOH HOH A . 
H 5 HOH 413  5213 1889 HOH HOH A . 
H 5 HOH 414  5214 734  HOH HOH A . 
H 5 HOH 415  5215 1198 HOH HOH A . 
H 5 HOH 416  5216 481  HOH HOH A . 
H 5 HOH 417  5217 462  HOH HOH A . 
H 5 HOH 418  5218 1534 HOH HOH A . 
H 5 HOH 419  5219 1858 HOH HOH A . 
H 5 HOH 420  5220 1090 HOH HOH A . 
H 5 HOH 421  5221 968  HOH HOH A . 
H 5 HOH 422  5222 1895 HOH HOH A . 
H 5 HOH 423  5223 666  HOH HOH A . 
H 5 HOH 424  5224 1037 HOH HOH A . 
H 5 HOH 425  5225 2323 HOH HOH A . 
H 5 HOH 426  5226 1796 HOH HOH A . 
H 5 HOH 427  5227 1813 HOH HOH A . 
H 5 HOH 428  5228 520  HOH HOH A . 
H 5 HOH 429  5229 1900 HOH HOH A . 
H 5 HOH 430  5230 1081 HOH HOH A . 
H 5 HOH 431  5231 2281 HOH HOH A . 
H 5 HOH 432  5232 2    HOH HOH A . 
H 5 HOH 433  5233 517  HOH HOH A . 
H 5 HOH 434  5234 2307 HOH HOH A . 
H 5 HOH 435  5235 1330 HOH HOH A . 
H 5 HOH 436  5236 827  HOH HOH A . 
H 5 HOH 437  5237 1791 HOH HOH A . 
H 5 HOH 438  5238 1991 HOH HOH A . 
H 5 HOH 439  5239 2140 HOH HOH A . 
H 5 HOH 440  5240 1537 HOH HOH A . 
H 5 HOH 441  5241 1874 HOH HOH A . 
H 5 HOH 442  5242 568  HOH HOH A . 
H 5 HOH 443  5243 1429 HOH HOH A . 
H 5 HOH 444  5244 1571 HOH HOH A . 
H 5 HOH 445  5245 434  HOH HOH A . 
H 5 HOH 446  5246 1621 HOH HOH A . 
H 5 HOH 447  5247 2286 HOH HOH A . 
H 5 HOH 448  5248 2203 HOH HOH A . 
H 5 HOH 449  5249 1320 HOH HOH A . 
H 5 HOH 450  5250 515  HOH HOH A . 
H 5 HOH 451  5251 1024 HOH HOH A . 
H 5 HOH 452  5252 1574 HOH HOH A . 
H 5 HOH 453  5253 1461 HOH HOH A . 
H 5 HOH 454  5254 1604 HOH HOH A . 
H 5 HOH 455  5255 2213 HOH HOH A . 
H 5 HOH 456  5256 1185 HOH HOH A . 
H 5 HOH 457  5257 1972 HOH HOH A . 
H 5 HOH 458  5258 1583 HOH HOH A . 
H 5 HOH 459  5259 580  HOH HOH A . 
H 5 HOH 460  5260 1281 HOH HOH A . 
H 5 HOH 461  5261 654  HOH HOH A . 
H 5 HOH 462  5262 1668 HOH HOH A . 
H 5 HOH 463  5263 508  HOH HOH A . 
H 5 HOH 464  5264 1973 HOH HOH A . 
H 5 HOH 465  5265 618  HOH HOH A . 
H 5 HOH 466  5266 873  HOH HOH A . 
H 5 HOH 467  5267 1000 HOH HOH A . 
H 5 HOH 468  5268 186  HOH HOH A . 
H 5 HOH 469  5269 2086 HOH HOH A . 
H 5 HOH 470  5270 865  HOH HOH A . 
H 5 HOH 471  5271 1209 HOH HOH A . 
H 5 HOH 472  5272 2191 HOH HOH A . 
H 5 HOH 473  5273 1602 HOH HOH A . 
H 5 HOH 474  5274 1646 HOH HOH A . 
H 5 HOH 475  5275 1816 HOH HOH A . 
H 5 HOH 476  5276 1218 HOH HOH A . 
H 5 HOH 477  5277 877  HOH HOH A . 
H 5 HOH 478  5278 1388 HOH HOH A . 
H 5 HOH 479  5279 1561 HOH HOH A . 
H 5 HOH 480  5280 846  HOH HOH A . 
H 5 HOH 481  5281 573  HOH HOH A . 
H 5 HOH 482  5282 1494 HOH HOH A . 
H 5 HOH 483  5283 2207 HOH HOH A . 
H 5 HOH 484  5284 2050 HOH HOH A . 
H 5 HOH 485  5285 1211 HOH HOH A . 
H 5 HOH 486  5286 1393 HOH HOH A . 
H 5 HOH 487  5287 1026 HOH HOH A . 
H 5 HOH 488  5288 578  HOH HOH A . 
H 5 HOH 489  5289 458  HOH HOH A . 
H 5 HOH 490  5290 470  HOH HOH A . 
H 5 HOH 491  5291 1495 HOH HOH A . 
H 5 HOH 492  5292 2285 HOH HOH A . 
H 5 HOH 493  5293 1375 HOH HOH A . 
H 5 HOH 494  5294 1177 HOH HOH A . 
H 5 HOH 495  5295 491  HOH HOH A . 
H 5 HOH 496  5296 1287 HOH HOH A . 
H 5 HOH 497  5297 775  HOH HOH A . 
H 5 HOH 498  5298 657  HOH HOH A . 
H 5 HOH 499  5299 1666 HOH HOH A . 
H 5 HOH 500  5300 708  HOH HOH A . 
H 5 HOH 501  5301 1852 HOH HOH A . 
H 5 HOH 502  5302 754  HOH HOH A . 
H 5 HOH 503  5303 496  HOH HOH A . 
H 5 HOH 504  5304 1080 HOH HOH A . 
H 5 HOH 505  5305 698  HOH HOH A . 
H 5 HOH 506  5306 1513 HOH HOH A . 
H 5 HOH 507  5307 756  HOH HOH A . 
H 5 HOH 508  5308 722  HOH HOH A . 
H 5 HOH 509  5309 1677 HOH HOH A . 
H 5 HOH 510  5310 1250 HOH HOH A . 
H 5 HOH 511  5311 956  HOH HOH A . 
H 5 HOH 512  5312 528  HOH HOH A . 
H 5 HOH 513  5313 2006 HOH HOH A . 
H 5 HOH 514  5314 1585 HOH HOH A . 
H 5 HOH 515  5315 1575 HOH HOH A . 
H 5 HOH 516  5316 1835 HOH HOH A . 
H 5 HOH 517  5317 744  HOH HOH A . 
H 5 HOH 518  5318 655  HOH HOH A . 
H 5 HOH 519  5319 653  HOH HOH A . 
H 5 HOH 520  5320 512  HOH HOH A . 
H 5 HOH 521  5321 900  HOH HOH A . 
H 5 HOH 522  5322 506  HOH HOH A . 
H 5 HOH 523  5323 1292 HOH HOH A . 
H 5 HOH 524  5324 2124 HOH HOH A . 
H 5 HOH 525  5325 1184 HOH HOH A . 
H 5 HOH 526  5326 980  HOH HOH A . 
H 5 HOH 527  5327 589  HOH HOH A . 
H 5 HOH 528  5328 1002 HOH HOH A . 
H 5 HOH 529  5329 2173 HOH HOH A . 
H 5 HOH 530  5330 450  HOH HOH A . 
H 5 HOH 531  5331 1825 HOH HOH A . 
H 5 HOH 532  5332 1832 HOH HOH A . 
H 5 HOH 533  5333 495  HOH HOH A . 
H 5 HOH 534  5334 899  HOH HOH A . 
H 5 HOH 535  5335 571  HOH HOH A . 
H 5 HOH 536  5336 1747 HOH HOH A . 
H 5 HOH 537  5337 1236 HOH HOH A . 
H 5 HOH 538  5338 1160 HOH HOH A . 
H 5 HOH 539  5339 2002 HOH HOH A . 
H 5 HOH 540  5340 1629 HOH HOH A . 
H 5 HOH 541  5341 1047 HOH HOH A . 
H 5 HOH 542  5342 1923 HOH HOH A . 
H 5 HOH 543  5343 645  HOH HOH A . 
H 5 HOH 544  5344 2185 HOH HOH A . 
H 5 HOH 545  5345 717  HOH HOH A . 
H 5 HOH 546  5346 2240 HOH HOH A . 
H 5 HOH 547  5347 507  HOH HOH A . 
H 5 HOH 548  5348 467  HOH HOH A . 
H 5 HOH 549  5349 1197 HOH HOH A . 
H 5 HOH 550  5350 591  HOH HOH A . 
H 5 HOH 551  5351 1992 HOH HOH A . 
H 5 HOH 552  5352 922  HOH HOH A . 
H 5 HOH 553  5353 987  HOH HOH A . 
H 5 HOH 554  5354 432  HOH HOH A . 
H 5 HOH 555  5355 1273 HOH HOH A . 
H 5 HOH 556  5356 1826 HOH HOH A . 
H 5 HOH 557  5357 553  HOH HOH A . 
H 5 HOH 558  5358 461  HOH HOH A . 
H 5 HOH 559  5359 1885 HOH HOH A . 
H 5 HOH 560  5360 1361 HOH HOH A . 
H 5 HOH 561  5361 699  HOH HOH A . 
H 5 HOH 562  5362 1922 HOH HOH A . 
H 5 HOH 563  5363 1089 HOH HOH A . 
H 5 HOH 564  5364 484  HOH HOH A . 
H 5 HOH 565  5365 1849 HOH HOH A . 
H 5 HOH 566  5366 2010 HOH HOH A . 
H 5 HOH 567  5367 768  HOH HOH A . 
H 5 HOH 568  5368 1293 HOH HOH A . 
H 5 HOH 569  5369 1522 HOH HOH A . 
H 5 HOH 570  5370 1088 HOH HOH A . 
H 5 HOH 571  5371 1137 HOH HOH A . 
H 5 HOH 572  5372 1485 HOH HOH A . 
H 5 HOH 573  5373 465  HOH HOH A . 
H 5 HOH 574  5374 1618 HOH HOH A . 
H 5 HOH 575  5375 1686 HOH HOH A . 
H 5 HOH 576  5376 603  HOH HOH A . 
H 5 HOH 577  5377 790  HOH HOH A . 
H 5 HOH 578  5378 929  HOH HOH A . 
H 5 HOH 579  5379 1133 HOH HOH A . 
H 5 HOH 580  5380 1749 HOH HOH A . 
H 5 HOH 581  5381 753  HOH HOH A . 
H 5 HOH 582  5382 1326 HOH HOH A . 
H 5 HOH 583  5383 647  HOH HOH A . 
H 5 HOH 584  5384 1509 HOH HOH A . 
H 5 HOH 585  5385 694  HOH HOH A . 
H 5 HOH 586  5386 498  HOH HOH A . 
H 5 HOH 587  5387 1252 HOH HOH A . 
H 5 HOH 588  5388 943  HOH HOH A . 
H 5 HOH 589  5389 445  HOH HOH A . 
H 5 HOH 590  5390 1219 HOH HOH A . 
H 5 HOH 591  5391 2081 HOH HOH A . 
H 5 HOH 592  5392 917  HOH HOH A . 
H 5 HOH 593  5393 148  HOH HOH A . 
H 5 HOH 594  5394 794  HOH HOH A . 
H 5 HOH 595  5395 1012 HOH HOH A . 
H 5 HOH 596  5396 977  HOH HOH A . 
H 5 HOH 597  5397 1143 HOH HOH A . 
H 5 HOH 598  5398 1424 HOH HOH A . 
H 5 HOH 599  5399 1593 HOH HOH A . 
H 5 HOH 600  5400 1918 HOH HOH A . 
H 5 HOH 601  5401 995  HOH HOH A . 
H 5 HOH 602  5402 1540 HOH HOH A . 
H 5 HOH 603  5403 1094 HOH HOH A . 
H 5 HOH 604  5404 1349 HOH HOH A . 
H 5 HOH 605  5405 1690 HOH HOH A . 
H 5 HOH 606  5406 939  HOH HOH A . 
H 5 HOH 607  5407 1234 HOH HOH A . 
H 5 HOH 608  5408 2238 HOH HOH A . 
H 5 HOH 609  5409 1578 HOH HOH A . 
H 5 HOH 610  5410 1030 HOH HOH A . 
H 5 HOH 611  5411 808  HOH HOH A . 
H 5 HOH 612  5412 1545 HOH HOH A . 
H 5 HOH 613  5413 1166 HOH HOH A . 
H 5 HOH 614  5414 1669 HOH HOH A . 
H 5 HOH 615  5415 2266 HOH HOH A . 
H 5 HOH 616  5416 848  HOH HOH A . 
H 5 HOH 617  5417 1035 HOH HOH A . 
H 5 HOH 618  5418 1670 HOH HOH A . 
H 5 HOH 619  5419 514  HOH HOH A . 
H 5 HOH 620  5420 2084 HOH HOH A . 
H 5 HOH 621  5421 697  HOH HOH A . 
H 5 HOH 622  5422 1207 HOH HOH A . 
H 5 HOH 623  5423 440  HOH HOH A . 
H 5 HOH 624  5424 1073 HOH HOH A . 
H 5 HOH 625  5425 2029 HOH HOH A . 
H 5 HOH 626  5426 2308 HOH HOH A . 
H 5 HOH 627  5427 1913 HOH HOH A . 
H 5 HOH 628  5428 1694 HOH HOH A . 
H 5 HOH 629  5429 1979 HOH HOH A . 
H 5 HOH 630  5430 999  HOH HOH A . 
H 5 HOH 631  5431 843  HOH HOH A . 
H 5 HOH 632  5432 2125 HOH HOH A . 
H 5 HOH 633  5433 1296 HOH HOH A . 
H 5 HOH 634  5434 2122 HOH HOH A . 
H 5 HOH 635  5435 1264 HOH HOH A . 
H 5 HOH 636  5436 555  HOH HOH A . 
H 5 HOH 637  5437 1981 HOH HOH A . 
H 5 HOH 638  5438 2320 HOH HOH A . 
H 5 HOH 639  5439 1643 HOH HOH A . 
H 5 HOH 640  5440 1931 HOH HOH A . 
H 5 HOH 641  5441 1687 HOH HOH A . 
H 5 HOH 642  5442 1408 HOH HOH A . 
H 5 HOH 643  5443 1529 HOH HOH A . 
H 5 HOH 644  5444 1334 HOH HOH A . 
H 5 HOH 645  5445 1437 HOH HOH A . 
H 5 HOH 646  5446 686  HOH HOH A . 
H 5 HOH 647  5447 792  HOH HOH A . 
H 5 HOH 648  5448 1744 HOH HOH A . 
H 5 HOH 649  5449 2053 HOH HOH A . 
H 5 HOH 650  5450 1958 HOH HOH A . 
H 5 HOH 651  5451 1091 HOH HOH A . 
H 5 HOH 652  5452 527  HOH HOH A . 
H 5 HOH 653  5453 1117 HOH HOH A . 
H 5 HOH 654  5454 838  HOH HOH A . 
H 5 HOH 655  5455 2182 HOH HOH A . 
H 5 HOH 656  5456 1244 HOH HOH A . 
H 5 HOH 657  5457 1458 HOH HOH A . 
H 5 HOH 658  5458 471  HOH HOH A . 
H 5 HOH 659  5459 950  HOH HOH A . 
H 5 HOH 660  5460 1083 HOH HOH A . 
H 5 HOH 661  5461 1425 HOH HOH A . 
H 5 HOH 662  5462 2245 HOH HOH A . 
H 5 HOH 663  5463 1201 HOH HOH A . 
H 5 HOH 664  5464 641  HOH HOH A . 
H 5 HOH 665  5465 1766 HOH HOH A . 
H 5 HOH 666  5466 1397 HOH HOH A . 
H 5 HOH 667  5467 1859 HOH HOH A . 
H 5 HOH 668  5468 540  HOH HOH A . 
H 5 HOH 669  5469 1451 HOH HOH A . 
H 5 HOH 670  5470 1072 HOH HOH A . 
H 5 HOH 671  5471 1346 HOH HOH A . 
H 5 HOH 672  5472 1993 HOH HOH A . 
H 5 HOH 673  5473 870  HOH HOH A . 
H 5 HOH 674  5474 1006 HOH HOH A . 
H 5 HOH 675  5475 615  HOH HOH A . 
H 5 HOH 676  5476 788  HOH HOH A . 
H 5 HOH 677  5477 1132 HOH HOH A . 
H 5 HOH 678  5478 2131 HOH HOH A . 
H 5 HOH 679  5479 752  HOH HOH A . 
H 5 HOH 680  5480 1276 HOH HOH A . 
H 5 HOH 681  5481 1077 HOH HOH A . 
H 5 HOH 682  5482 597  HOH HOH A . 
H 5 HOH 683  5483 598  HOH HOH A . 
H 5 HOH 684  5484 1557 HOH HOH A . 
H 5 HOH 685  5485 1427 HOH HOH A . 
H 5 HOH 686  5486 1881 HOH HOH A . 
H 5 HOH 687  5487 1833 HOH HOH A . 
H 5 HOH 688  5488 695  HOH HOH A . 
H 5 HOH 689  5489 1011 HOH HOH A . 
H 5 HOH 690  5490 2321 HOH HOH A . 
H 5 HOH 691  5491 1300 HOH HOH A . 
H 5 HOH 692  5492 676  HOH HOH A . 
H 5 HOH 693  5493 903  HOH HOH A . 
H 5 HOH 694  5494 1418 HOH HOH A . 
H 5 HOH 695  5495 532  HOH HOH A . 
H 5 HOH 696  5496 544  HOH HOH A . 
H 5 HOH 697  5497 1449 HOH HOH A . 
H 5 HOH 698  5498 1004 HOH HOH A . 
H 5 HOH 699  5499 454  HOH HOH A . 
H 5 HOH 700  5500 1092 HOH HOH A . 
H 5 HOH 701  5501 2216 HOH HOH A . 
H 5 HOH 702  5502 727  HOH HOH A . 
H 5 HOH 703  5503 569  HOH HOH A . 
H 5 HOH 704  5504 1966 HOH HOH A . 
H 5 HOH 705  5505 1114 HOH HOH A . 
H 5 HOH 706  5506 1450 HOH HOH A . 
H 5 HOH 707  5507 493  HOH HOH A . 
H 5 HOH 708  5508 621  HOH HOH A . 
H 5 HOH 709  5509 469  HOH HOH A . 
H 5 HOH 710  5510 1099 HOH HOH A . 
H 5 HOH 711  5511 1068 HOH HOH A . 
H 5 HOH 712  5512 2294 HOH HOH A . 
H 5 HOH 713  5513 879  HOH HOH A . 
H 5 HOH 714  5514 869  HOH HOH A . 
H 5 HOH 715  5515 2038 HOH HOH A . 
H 5 HOH 716  5516 853  HOH HOH A . 
H 5 HOH 717  5517 639  HOH HOH A . 
H 5 HOH 718  5518 549  HOH HOH A . 
H 5 HOH 719  5519 456  HOH HOH A . 
H 5 HOH 720  5520 632  HOH HOH A . 
H 5 HOH 721  5521 1549 HOH HOH A . 
H 5 HOH 722  5522 501  HOH HOH A . 
H 5 HOH 723  5523 1683 HOH HOH A . 
H 5 HOH 724  5524 2049 HOH HOH A . 
H 5 HOH 725  5525 1075 HOH HOH A . 
H 5 HOH 726  5526 1523 HOH HOH A . 
H 5 HOH 727  5527 1323 HOH HOH A . 
H 5 HOH 728  5528 435  HOH HOH A . 
H 5 HOH 729  5529 1306 HOH HOH A . 
H 5 HOH 730  5530 969  HOH HOH A . 
H 5 HOH 731  5531 2097 HOH HOH A . 
H 5 HOH 732  5532 803  HOH HOH A . 
H 5 HOH 733  5533 1018 HOH HOH A . 
H 5 HOH 734  5534 947  HOH HOH A . 
H 5 HOH 735  5535 1579 HOH HOH A . 
H 5 HOH 736  5536 887  HOH HOH A . 
H 5 HOH 737  5537 2047 HOH HOH A . 
H 5 HOH 738  5538 572  HOH HOH A . 
H 5 HOH 739  5539 680  HOH HOH A . 
H 5 HOH 740  5540 1588 HOH HOH A . 
H 5 HOH 741  5541 1279 HOH HOH A . 
H 5 HOH 742  5542 1087 HOH HOH A . 
H 5 HOH 743  5543 1034 HOH HOH A . 
H 5 HOH 744  5544 1069 HOH HOH A . 
H 5 HOH 745  5545 582  HOH HOH A . 
H 5 HOH 746  5546 1566 HOH HOH A . 
H 5 HOH 747  5547 712  HOH HOH A . 
H 5 HOH 748  5548 1239 HOH HOH A . 
H 5 HOH 749  5549 814  HOH HOH A . 
H 5 HOH 750  5550 2073 HOH HOH A . 
H 5 HOH 751  5551 1454 HOH HOH A . 
H 5 HOH 752  5552 1531 HOH HOH A . 
H 5 HOH 753  5553 2247 HOH HOH A . 
H 5 HOH 754  5554 1    HOH HOH A . 
H 5 HOH 755  5555 932  HOH HOH A . 
H 5 HOH 756  5556 1559 HOH HOH A . 
H 5 HOH 757  5557 1257 HOH HOH A . 
H 5 HOH 758  5558 668  HOH HOH A . 
H 5 HOH 759  5559 682  HOH HOH A . 
H 5 HOH 760  5560 82   HOH HOH A . 
H 5 HOH 761  5561 951  HOH HOH A . 
H 5 HOH 762  5562 611  HOH HOH A . 
H 5 HOH 763  5563 1777 HOH HOH A . 
H 5 HOH 764  5564 630  HOH HOH A . 
H 5 HOH 765  5565 448  HOH HOH A . 
H 5 HOH 766  5566 1855 HOH HOH A . 
H 5 HOH 767  5567 1555 HOH HOH A . 
H 5 HOH 768  5568 1322 HOH HOH A . 
H 5 HOH 769  5569 1635 HOH HOH A . 
H 5 HOH 770  5570 1217 HOH HOH A . 
H 5 HOH 771  5571 1456 HOH HOH A . 
H 5 HOH 772  5572 851  HOH HOH A . 
H 5 HOH 773  5573 693  HOH HOH A . 
H 5 HOH 774  5574 1978 HOH HOH A . 
H 5 HOH 775  5575 1385 HOH HOH A . 
H 5 HOH 776  5576 1394 HOH HOH A . 
H 5 HOH 777  5577 521  HOH HOH A . 
H 5 HOH 778  5578 996  HOH HOH A . 
H 5 HOH 779  5579 1596 HOH HOH A . 
H 5 HOH 780  5580 1695 HOH HOH A . 
H 5 HOH 781  5581 455  HOH HOH A . 
H 5 HOH 782  5582 662  HOH HOH A . 
H 5 HOH 783  5583 1589 HOH HOH A . 
H 5 HOH 784  5584 602  HOH HOH A . 
H 5 HOH 785  5585 1308 HOH HOH A . 
H 5 HOH 786  5586 1139 HOH HOH A . 
H 5 HOH 787  5587 1960 HOH HOH A . 
H 5 HOH 788  5588 691  HOH HOH A . 
H 5 HOH 789  5589 1259 HOH HOH A . 
H 5 HOH 790  5590 1119 HOH HOH A . 
H 5 HOH 791  5591 859  HOH HOH A . 
H 5 HOH 792  5592 841  HOH HOH A . 
H 5 HOH 793  5593 831  HOH HOH A . 
H 5 HOH 794  5594 1147 HOH HOH A . 
H 5 HOH 795  5595 2023 HOH HOH A . 
H 5 HOH 796  5596 2034 HOH HOH A . 
H 5 HOH 797  5597 983  HOH HOH A . 
H 5 HOH 798  5598 626  HOH HOH A . 
H 5 HOH 799  5599 451  HOH HOH A . 
H 5 HOH 800  5600 1512 HOH HOH A . 
H 5 HOH 801  5601 584  HOH HOH A . 
H 5 HOH 802  5602 1389 HOH HOH A . 
H 5 HOH 803  5603 1501 HOH HOH A . 
H 5 HOH 804  5604 437  HOH HOH A . 
H 5 HOH 805  5605 1113 HOH HOH A . 
H 5 HOH 806  5606 1188 HOH HOH A . 
H 5 HOH 807  5607 449  HOH HOH A . 
H 5 HOH 808  5608 751  HOH HOH A . 
H 5 HOH 809  5609 1632 HOH HOH A . 
H 5 HOH 810  5610 1587 HOH HOH A . 
H 5 HOH 811  5611 526  HOH HOH A . 
H 5 HOH 812  5612 509  HOH HOH A . 
H 5 HOH 813  5613 648  HOH HOH A . 
H 5 HOH 814  5614 1841 HOH HOH A . 
H 5 HOH 815  5615 1054 HOH HOH A . 
H 5 HOH 816  5616 460  HOH HOH A . 
H 5 HOH 817  5617 1359 HOH HOH A . 
H 5 HOH 818  5618 1246 HOH HOH A . 
H 5 HOH 819  5619 826  HOH HOH A . 
H 5 HOH 820  5620 918  HOH HOH A . 
H 5 HOH 821  5621 1530 HOH HOH A . 
H 5 HOH 822  5622 543  HOH HOH A . 
H 5 HOH 823  5623 1021 HOH HOH A . 
H 5 HOH 824  5624 620  HOH HOH A . 
H 5 HOH 825  5625 1368 HOH HOH A . 
H 5 HOH 826  5626 659  HOH HOH A . 
H 5 HOH 827  5627 1893 HOH HOH A . 
H 5 HOH 828  5628 1773 HOH HOH A . 
H 5 HOH 829  5629 1480 HOH HOH A . 
H 5 HOH 830  5630 1806 HOH HOH A . 
H 5 HOH 831  5631 793  HOH HOH A . 
H 5 HOH 832  5632 1659 HOH HOH A . 
H 5 HOH 833  5633 1919 HOH HOH A . 
H 5 HOH 834  5634 888  HOH HOH A . 
H 5 HOH 835  5635 565  HOH HOH A . 
H 5 HOH 836  5636 2067 HOH HOH A . 
H 5 HOH 837  5637 961  HOH HOH A . 
H 5 HOH 838  5638 1415 HOH HOH A . 
H 5 HOH 839  5639 692  HOH HOH A . 
H 5 HOH 840  5640 596  HOH HOH A . 
H 5 HOH 841  5641 2004 HOH HOH A . 
H 5 HOH 842  5642 535  HOH HOH A . 
H 5 HOH 843  5643 486  HOH HOH A . 
H 5 HOH 844  5644 906  HOH HOH A . 
H 5 HOH 845  5645 2035 HOH HOH A . 
H 5 HOH 846  5646 811  HOH HOH A . 
H 5 HOH 847  5647 636  HOH HOH A . 
H 5 HOH 848  5648 1343 HOH HOH A . 
H 5 HOH 849  5649 2065 HOH HOH A . 
H 5 HOH 850  5650 806  HOH HOH A . 
H 5 HOH 851  5651 1100 HOH HOH A . 
H 5 HOH 852  5652 1517 HOH HOH A . 
H 5 HOH 853  5653 488  HOH HOH A . 
H 5 HOH 854  5654 1467 HOH HOH A . 
H 5 HOH 855  5655 1573 HOH HOH A . 
H 5 HOH 856  5656 1222 HOH HOH A . 
H 5 HOH 857  5657 1821 HOH HOH A . 
H 5 HOH 858  5658 2253 HOH HOH A . 
H 5 HOH 859  5659 1965 HOH HOH A . 
H 5 HOH 860  5660 1414 HOH HOH A . 
H 5 HOH 861  5661 863  HOH HOH A . 
H 5 HOH 862  5662 1934 HOH HOH A . 
H 5 HOH 863  5663 658  HOH HOH A . 
H 5 HOH 864  5664 1614 HOH HOH A . 
H 5 HOH 865  5665 750  HOH HOH A . 
H 5 HOH 866  5666 489  HOH HOH A . 
H 5 HOH 867  5667 1358 HOH HOH A . 
H 5 HOH 868  5668 690  HOH HOH A . 
H 5 HOH 869  5669 2027 HOH HOH A . 
H 5 HOH 870  5670 2161 HOH HOH A . 
H 5 HOH 871  5671 1498 HOH HOH A . 
H 5 HOH 872  5672 1915 HOH HOH A . 
H 5 HOH 873  5673 1325 HOH HOH A . 
H 5 HOH 874  5674 1106 HOH HOH A . 
H 5 HOH 875  5675 562  HOH HOH A . 
H 5 HOH 876  5676 1730 HOH HOH A . 
H 5 HOH 877  5677 711  HOH HOH A . 
H 5 HOH 878  5678 2166 HOH HOH A . 
H 5 HOH 879  5679 599  HOH HOH A . 
H 5 HOH 880  5680 707  HOH HOH A . 
H 5 HOH 881  5681 640  HOH HOH A . 
H 5 HOH 882  5682 810  HOH HOH A . 
H 5 HOH 883  5683 1657 HOH HOH A . 
H 5 HOH 884  5684 1268 HOH HOH A . 
H 5 HOH 885  5685 1829 HOH HOH A . 
H 5 HOH 886  5686 1580 HOH HOH A . 
H 5 HOH 887  5687 642  HOH HOH A . 
H 5 HOH 888  5688 1134 HOH HOH A . 
H 5 HOH 889  5689 1500 HOH HOH A . 
H 5 HOH 890  5690 1220 HOH HOH A . 
H 5 HOH 891  5691 1095 HOH HOH A . 
H 5 HOH 892  5692 651  HOH HOH A . 
H 5 HOH 893  5693 1783 HOH HOH A . 
H 5 HOH 894  5694 1771 HOH HOH A . 
H 5 HOH 895  5695 1023 HOH HOH A . 
H 5 HOH 896  5696 858  HOH HOH A . 
H 5 HOH 897  5697 1248 HOH HOH A . 
H 5 HOH 898  5698 815  HOH HOH A . 
H 5 HOH 899  5699 1401 HOH HOH A . 
H 5 HOH 900  5700 2197 HOH HOH A . 
H 5 HOH 901  5701 447  HOH HOH A . 
H 5 HOH 902  5702 1997 HOH HOH A . 
H 5 HOH 903  5703 2075 HOH HOH A . 
H 5 HOH 904  5704 2055 HOH HOH A . 
H 5 HOH 905  5705 1953 HOH HOH A . 
H 5 HOH 906  5706 1131 HOH HOH A . 
H 5 HOH 907  5707 1729 HOH HOH A . 
H 5 HOH 908  5708 982  HOH HOH A . 
H 5 HOH 909  5709 277  HOH HOH A . 
H 5 HOH 910  5710 1108 HOH HOH A . 
H 5 HOH 911  5711 1788 HOH HOH A . 
H 5 HOH 912  5712 181  HOH HOH A . 
H 5 HOH 913  5713 675  HOH HOH A . 
H 5 HOH 914  5714 1049 HOH HOH A . 
H 5 HOH 915  5715 926  HOH HOH A . 
H 5 HOH 916  5716 1434 HOH HOH A . 
H 5 HOH 917  5717 441  HOH HOH A . 
H 5 HOH 918  5718 1651 HOH HOH A . 
H 5 HOH 919  5719 1541 HOH HOH A . 
H 5 HOH 920  5720 564  HOH HOH A . 
H 5 HOH 921  5721 2106 HOH HOH A . 
H 5 HOH 922  5722 1648 HOH HOH A . 
H 5 HOH 923  5723 1637 HOH HOH A . 
H 5 HOH 924  5724 1171 HOH HOH A . 
H 5 HOH 925  5725 897  HOH HOH A . 
H 5 HOH 926  5726 265  HOH HOH A . 
H 5 HOH 927  5727 2234 HOH HOH A . 
H 5 HOH 928  5728 959  HOH HOH A . 
H 5 HOH 929  5729 608  HOH HOH A . 
H 5 HOH 930  5730 511  HOH HOH A . 
H 5 HOH 931  5731 945  HOH HOH A . 
H 5 HOH 932  5732 2212 HOH HOH A . 
H 5 HOH 933  5733 2157 HOH HOH A . 
H 5 HOH 934  5734 1709 HOH HOH A . 
H 5 HOH 935  5735 1615 HOH HOH A . 
H 5 HOH 936  5736 813  HOH HOH A . 
H 5 HOH 937  5737 679  HOH HOH A . 
H 5 HOH 938  5738 2300 HOH HOH A . 
H 5 HOH 939  5739 1036 HOH HOH A . 
H 5 HOH 940  5740 1174 HOH HOH A . 
H 5 HOH 941  5741 590  HOH HOH A . 
H 5 HOH 942  5742 837  HOH HOH A . 
H 5 HOH 943  5743 684  HOH HOH A . 
H 5 HOH 944  5744 2312 HOH HOH A . 
H 5 HOH 945  5745 678  HOH HOH A . 
H 5 HOH 946  5746 2135 HOH HOH A . 
H 5 HOH 947  5747 1671 HOH HOH A . 
H 5 HOH 948  5748 1713 HOH HOH A . 
H 5 HOH 949  5749 529  HOH HOH A . 
H 5 HOH 950  5750 2226 HOH HOH A . 
H 5 HOH 951  5751 1120 HOH HOH A . 
H 5 HOH 952  5752 560  HOH HOH A . 
H 5 HOH 953  5753 2200 HOH HOH A . 
H 5 HOH 954  5754 1318 HOH HOH A . 
H 5 HOH 955  5755 967  HOH HOH A . 
H 5 HOH 956  5756 1957 HOH HOH A . 
H 5 HOH 957  5757 911  HOH HOH A . 
H 5 HOH 958  5758 1355 HOH HOH A . 
H 5 HOH 959  5759 724  HOH HOH A . 
H 5 HOH 960  5760 855  HOH HOH A . 
H 5 HOH 961  5761 1179 HOH HOH A . 
H 5 HOH 962  5762 884  HOH HOH A . 
H 5 HOH 963  5763 468  HOH HOH A . 
H 5 HOH 964  5764 1288 HOH HOH A . 
H 5 HOH 965  5765 965  HOH HOH A . 
H 5 HOH 966  5766 1619 HOH HOH A . 
H 5 HOH 967  5767 443  HOH HOH A . 
H 5 HOH 968  5768 1552 HOH HOH A . 
H 5 HOH 969  5769 898  HOH HOH A . 
H 5 HOH 970  5770 563  HOH HOH A . 
H 5 HOH 971  5771 2145 HOH HOH A . 
H 5 HOH 972  5772 1124 HOH HOH A . 
H 5 HOH 973  5773 1342 HOH HOH A . 
H 5 HOH 974  5774 607  HOH HOH A . 
H 5 HOH 975  5775 1082 HOH HOH A . 
H 5 HOH 976  5776 1861 HOH HOH A . 
H 5 HOH 977  5777 438  HOH HOH A . 
H 5 HOH 978  5778 1909 HOH HOH A . 
H 5 HOH 979  5779 818  HOH HOH A . 
H 5 HOH 980  5780 1020 HOH HOH A . 
H 5 HOH 981  5781 1110 HOH HOH A . 
H 5 HOH 982  5782 1462 HOH HOH A . 
H 5 HOH 983  5783 958  HOH HOH A . 
H 5 HOH 984  5784 1718 HOH HOH A . 
H 5 HOH 985  5785 2303 HOH HOH A . 
H 5 HOH 986  5786 1295 HOH HOH A . 
H 5 HOH 987  5787 822  HOH HOH A . 
H 5 HOH 988  5788 670  HOH HOH A . 
H 5 HOH 989  5789 1802 HOH HOH A . 
H 5 HOH 990  5790 700  HOH HOH A . 
H 5 HOH 991  5791 763  HOH HOH A . 
H 5 HOH 992  5792 547  HOH HOH A . 
H 5 HOH 993  5793 828  HOH HOH A . 
H 5 HOH 994  5794 1187 HOH HOH A . 
H 5 HOH 995  5795 490  HOH HOH A . 
H 5 HOH 996  5796 1060 HOH HOH A . 
H 5 HOH 997  5797 1943 HOH HOH A . 
H 5 HOH 998  5798 798  HOH HOH A . 
H 5 HOH 999  5799 548  HOH HOH A . 
H 5 HOH 1000 5800 1733 HOH HOH A . 
H 5 HOH 1001 5801 231  HOH HOH A . 
H 5 HOH 1002 5802 605  HOH HOH A . 
H 5 HOH 1003 5803 522  HOH HOH A . 
H 5 HOH 1004 5804 1553 HOH HOH A . 
H 5 HOH 1005 5805 2163 HOH HOH A . 
H 5 HOH 1006 5806 1728 HOH HOH A . 
H 5 HOH 1007 5807 801  HOH HOH A . 
H 5 HOH 1008 5808 575  HOH HOH A . 
H 5 HOH 1009 5809 1263 HOH HOH A . 
H 5 HOH 1010 5810 914  HOH HOH A . 
H 5 HOH 1011 5811 1478 HOH HOH A . 
H 5 HOH 1012 5812 482  HOH HOH A . 
H 5 HOH 1013 5813 1481 HOH HOH A . 
H 5 HOH 1014 5814 2263 HOH HOH A . 
H 5 HOH 1015 5815 1610 HOH HOH A . 
H 5 HOH 1016 5816 1278 HOH HOH A . 
H 5 HOH 1017 5817 2096 HOH HOH A . 
H 5 HOH 1018 5818 1098 HOH HOH A . 
H 5 HOH 1019 5819 550  HOH HOH A . 
H 5 HOH 1020 5820 613  HOH HOH A . 
H 5 HOH 1021 5821 556  HOH HOH A . 
H 5 HOH 1022 5822 483  HOH HOH A . 
H 5 HOH 1023 5823 2040 HOH HOH A . 
H 5 HOH 1024 5824 2150 HOH HOH A . 
H 5 HOH 1025 5825 1299 HOH HOH A . 
H 5 HOH 1026 5826 1655 HOH HOH A . 
H 5 HOH 1027 5827 1289 HOH HOH A . 
H 5 HOH 1028 5828 1070 HOH HOH A . 
H 5 HOH 1029 5829 1431 HOH HOH A . 
H 5 HOH 1030 5830 453  HOH HOH A . 
H 5 HOH 1031 5831 1652 HOH HOH A . 
H 5 HOH 1032 5832 780  HOH HOH A . 
H 5 HOH 1033 5833 1584 HOH HOH A . 
H 5 HOH 1034 5834 2248 HOH HOH A . 
H 5 HOH 1035 5835 2139 HOH HOH A . 
H 5 HOH 1036 5836 933  HOH HOH A . 
H 5 HOH 1037 5837 1309 HOH HOH A . 
H 5 HOH 1038 5838 779  HOH HOH A . 
H 5 HOH 1039 5839 1146 HOH HOH A . 
H 5 HOH 1040 5840 2078 HOH HOH A . 
H 5 HOH 1041 5841 1410 HOH HOH A . 
H 5 HOH 1042 5842 907  HOH HOH A . 
H 5 HOH 1043 5843 1316 HOH HOH A . 
H 5 HOH 1044 5844 2222 HOH HOH A . 
H 5 HOH 1045 5845 1445 HOH HOH A . 
H 5 HOH 1046 5846 1980 HOH HOH A . 
H 5 HOH 1047 5847 1740 HOH HOH A . 
H 5 HOH 1048 5848 2042 HOH HOH A . 
H 5 HOH 1049 5849 1693 HOH HOH A . 
H 5 HOH 1050 5850 2064 HOH HOH A . 
H 5 HOH 1051 5851 1336 HOH HOH A . 
H 5 HOH 1052 5852 1121 HOH HOH A . 
H 5 HOH 1053 5853 2210 HOH HOH A . 
H 5 HOH 1054 5854 905  HOH HOH A . 
H 5 HOH 1055 5855 1672 HOH HOH A . 
H 5 HOH 1056 5856 502  HOH HOH A . 
H 5 HOH 1057 5857 226  HOH HOH A . 
H 5 HOH 1058 5858 1804 HOH HOH A . 
H 5 HOH 1059 5859 1402 HOH HOH A . 
H 5 HOH 1060 5860 1700 HOH HOH A . 
H 5 HOH 1061 5861 1898 HOH HOH A . 
H 5 HOH 1062 5862 1554 HOH HOH A . 
H 5 HOH 1063 5863 638  HOH HOH A . 
H 5 HOH 1064 5864 1255 HOH HOH A . 
H 5 HOH 1065 5865 2167 HOH HOH A . 
H 5 HOH 1066 5866 2134 HOH HOH A . 
H 5 HOH 1067 5867 880  HOH HOH A . 
H 5 HOH 1068 5868 830  HOH HOH A . 
H 5 HOH 1069 5869 1173 HOH HOH A . 
H 5 HOH 1070 5870 2116 HOH HOH A . 
H 5 HOH 1071 5871 1014 HOH HOH A . 
H 5 HOH 1072 5872 1321 HOH HOH A . 
H 5 HOH 1073 5873 180  HOH HOH A . 
H 5 HOH 1074 5874 669  HOH HOH A . 
H 5 HOH 1075 5875 1305 HOH HOH A . 
H 5 HOH 1076 5876 627  HOH HOH A . 
H 5 HOH 1077 5877 1078 HOH HOH A . 
H 5 HOH 1078 5878 1875 HOH HOH A . 
H 5 HOH 1079 5879 737  HOH HOH A . 
H 5 HOH 1080 5880 716  HOH HOH A . 
H 5 HOH 1081 5881 786  HOH HOH A . 
H 5 HOH 1082 5882 1926 HOH HOH A . 
H 5 HOH 1083 5883 908  HOH HOH A . 
H 5 HOH 1084 5884 962  HOH HOH A . 
H 5 HOH 1085 5885 2026 HOH HOH A . 
H 5 HOH 1086 5886 1125 HOH HOH A . 
H 5 HOH 1087 5887 1902 HOH HOH A . 
H 5 HOH 1088 5888 1937 HOH HOH A . 
H 5 HOH 1089 5889 1789 HOH HOH A . 
H 5 HOH 1090 5890 777  HOH HOH A . 
H 5 HOH 1091 5891 860  HOH HOH A . 
H 5 HOH 1092 5892 1768 HOH HOH A . 
H 5 HOH 1093 5893 1457 HOH HOH A . 
H 5 HOH 1094 5894 1714 HOH HOH A . 
H 5 HOH 1095 5895 1350 HOH HOH A . 
H 5 HOH 1096 5896 934  HOH HOH A . 
H 5 HOH 1097 5897 1985 HOH HOH A . 
H 5 HOH 1098 5898 689  HOH HOH A . 
H 5 HOH 1099 5899 1921 HOH HOH A . 
H 5 HOH 1100 5900 1226 HOH HOH A . 
H 5 HOH 1101 5901 1484 HOH HOH A . 
H 5 HOH 1102 5902 193  HOH HOH A . 
H 5 HOH 1103 5903 46   HOH HOH A . 
H 5 HOH 1104 5904 743  HOH HOH A . 
H 5 HOH 1105 5905 2183 HOH HOH A . 
H 5 HOH 1106 5906 537  HOH HOH A . 
H 5 HOH 1107 5907 833  HOH HOH A . 
H 5 HOH 1108 5908 2272 HOH HOH A . 
H 5 HOH 1109 5909 842  HOH HOH A . 
H 5 HOH 1110 5910 1871 HOH HOH A . 
H 5 HOH 1111 5911 1676 HOH HOH A . 
H 5 HOH 1112 5912 60   HOH HOH A . 
H 5 HOH 1113 5913 1994 HOH HOH A . 
H 5 HOH 1114 5914 1221 HOH HOH A . 
H 5 HOH 1115 5915 1168 HOH HOH A . 
H 5 HOH 1116 5916 1890 HOH HOH A . 
H 5 HOH 1117 5917 1624 HOH HOH A . 
H 5 HOH 1118 5918 1800 HOH HOH A . 
H 5 HOH 1119 5919 2301 HOH HOH A . 
H 5 HOH 1120 5920 617  HOH HOH A . 
H 5 HOH 1121 5921 1528 HOH HOH A . 
H 5 HOH 1122 5922 20   HOH HOH A . 
H 5 HOH 1123 5923 1328 HOH HOH A . 
H 5 HOH 1124 5924 854  HOH HOH A . 
H 5 HOH 1125 5925 728  HOH HOH A . 
H 5 HOH 1126 5926 2058 HOH HOH A . 
H 5 HOH 1127 5927 2250 HOH HOH A . 
H 5 HOH 1128 5928 588  HOH HOH A . 
H 5 HOH 1129 5929 1948 HOH HOH A . 
H 5 HOH 1130 5930 1623 HOH HOH A . 
H 5 HOH 1131 5931 1053 HOH HOH A . 
H 5 HOH 1132 5932 2123 HOH HOH A . 
H 5 HOH 1133 5933 2030 HOH HOH A . 
H 5 HOH 1134 5934 2195 HOH HOH A . 
H 5 HOH 1135 5935 1999 HOH HOH A . 
H 5 HOH 1136 5936 1567 HOH HOH A . 
H 5 HOH 1137 5937 816  HOH HOH A . 
H 5 HOH 1138 5938 1759 HOH HOH A . 
H 5 HOH 1139 5939 1848 HOH HOH A . 
H 5 HOH 1140 5940 1746 HOH HOH A . 
H 5 HOH 1141 5941 1819 HOH HOH A . 
H 5 HOH 1142 5942 1180 HOH HOH A . 
H 5 HOH 1143 5943 1128 HOH HOH A . 
H 5 HOH 1144 5944 2045 HOH HOH A . 
H 5 HOH 1145 5945 1869 HOH HOH A . 
H 5 HOH 1146 5946 781  HOH HOH A . 
H 5 HOH 1147 5947 1644 HOH HOH A . 
H 5 HOH 1148 5948 1277 HOH HOH A . 
H 5 HOH 1149 5949 876  HOH HOH A . 
H 5 HOH 1150 5950 1374 HOH HOH A . 
H 5 HOH 1151 5951 732  HOH HOH A . 
H 5 HOH 1152 5952 1533 HOH HOH A . 
H 5 HOH 1153 5953 878  HOH HOH A . 
H 5 HOH 1154 5954 1040 HOH HOH A . 
H 5 HOH 1155 5955 505  HOH HOH A . 
H 5 HOH 1156 5956 1340 HOH HOH A . 
H 5 HOH 1157 5957 1830 HOH HOH A . 
H 5 HOH 1158 5958 723  HOH HOH A . 
H 5 HOH 1159 5959 1608 HOH HOH A . 
H 5 HOH 1160 5960 1905 HOH HOH A . 
H 5 HOH 1161 5961 478  HOH HOH A . 
H 5 HOH 1162 5962 795  HOH HOH A . 
H 5 HOH 1163 5963 1627 HOH HOH A . 
H 5 HOH 1164 5964 1195 HOH HOH A . 
H 5 HOH 1165 5965 1518 HOH HOH A . 
H 5 HOH 1166 5966 920  HOH HOH A . 
H 5 HOH 1167 5967 1186 HOH HOH A . 
H 5 HOH 1168 5968 1471 HOH HOH A . 
H 5 HOH 1169 5969 1807 HOH HOH A . 
H 5 HOH 1170 5970 778  HOH HOH A . 
H 5 HOH 1171 5971 1362 HOH HOH A . 
H 5 HOH 1172 5972 1371 HOH HOH A . 
H 5 HOH 1173 5973 2198 HOH HOH A . 
H 5 HOH 1174 5974 1879 HOH HOH A . 
H 5 HOH 1175 5975 536  HOH HOH A . 
H 5 HOH 1176 5976 2209 HOH HOH A . 
H 5 HOH 1177 5977 1426 HOH HOH A . 
H 5 HOH 1178 5978 729  HOH HOH A . 
H 5 HOH 1179 5979 1138 HOH HOH A . 
H 5 HOH 1180 5980 142  HOH HOH A . 
H 5 HOH 1181 5981 2115 HOH HOH A . 
H 5 HOH 1182 5982 1942 HOH HOH A . 
H 5 HOH 1183 5983 2190 HOH HOH A . 
H 5 HOH 1184 5984 1272 HOH HOH A . 
H 5 HOH 1185 5985 844  HOH HOH A . 
H 5 HOH 1186 5986 2235 HOH HOH A . 
H 5 HOH 1187 5987 1845 HOH HOH A . 
H 5 HOH 1188 5988 1103 HOH HOH A . 
H 5 HOH 1189 5989 2188 HOH HOH A . 
H 5 HOH 1190 5990 2264 HOH HOH A . 
H 5 HOH 1191 5991 1891 HOH HOH A . 
H 5 HOH 1192 5992 891  HOH HOH A . 
H 5 HOH 1193 5993 1238 HOH HOH A . 
H 5 HOH 1194 5994 1243 HOH HOH A . 
H 5 HOH 1195 5995 1215 HOH HOH A . 
H 5 HOH 1196 5996 1302 HOH HOH A . 
H 5 HOH 1197 5997 845  HOH HOH A . 
H 5 HOH 1198 5998 886  HOH HOH A . 
H 5 HOH 1199 5999 1126 HOH HOH A . 
H 5 HOH 1200 6000 1447 HOH HOH A . 
H 5 HOH 1201 6001 499  HOH HOH A . 
H 5 HOH 1202 6002 1191 HOH HOH A . 
H 5 HOH 1203 6003 1157 HOH HOH A . 
H 5 HOH 1204 6004 992  HOH HOH A . 
H 5 HOH 1205 6005 735  HOH HOH A . 
H 5 HOH 1206 6006 1625 HOH HOH A . 
H 5 HOH 1207 6007 1283 HOH HOH A . 
H 5 HOH 1208 6008 1333 HOH HOH A . 
H 5 HOH 1209 6009 994  HOH HOH A . 
H 5 HOH 1210 6010 144  HOH HOH A . 
H 5 HOH 1211 6011 1142 HOH HOH A . 
H 5 HOH 1212 6012 652  HOH HOH A . 
H 5 HOH 1213 6013 1799 HOH HOH A . 
H 5 HOH 1214 6014 892  HOH HOH A . 
H 5 HOH 1215 6015 1640 HOH HOH A . 
H 5 HOH 1216 6016 805  HOH HOH A . 
H 5 HOH 1217 6017 715  HOH HOH A . 
H 5 HOH 1218 6018 1633 HOH HOH A . 
H 5 HOH 1219 6019 919  HOH HOH A . 
H 5 HOH 1220 6020 714  HOH HOH A . 
H 5 HOH 1221 6021 1820 HOH HOH A . 
H 5 HOH 1222 6022 1057 HOH HOH A . 
H 5 HOH 1223 6023 1258 HOH HOH A . 
H 5 HOH 1224 6024 1840 HOH HOH A . 
H 5 HOH 1225 6025 1364 HOH HOH A . 
H 5 HOH 1226 6026 787  HOH HOH A . 
H 5 HOH 1227 6027 1312 HOH HOH A . 
H 5 HOH 1228 6028 1781 HOH HOH A . 
H 5 HOH 1229 6029 2007 HOH HOH A . 
H 5 HOH 1230 6030 1794 HOH HOH A . 
H 5 HOH 1231 6031 477  HOH HOH A . 
H 5 HOH 1232 6032 1741 HOH HOH A . 
H 5 HOH 1233 6033 1376 HOH HOH A . 
H 5 HOH 1234 6034 823  HOH HOH A . 
H 5 HOH 1235 6035 1721 HOH HOH A . 
H 5 HOH 1236 6036 2310 HOH HOH A . 
H 5 HOH 1237 6037 1313 HOH HOH A . 
H 5 HOH 1238 6038 762  HOH HOH A . 
H 5 HOH 1239 6039 1366 HOH HOH A . 
H 5 HOH 1240 6040 650  HOH HOH A . 
H 5 HOH 1241 6041 1654 HOH HOH A . 
H 5 HOH 1242 6042 1022 HOH HOH A . 
H 5 HOH 1243 6043 1982 HOH HOH A . 
H 5 HOH 1244 6044 579  HOH HOH A . 
H 5 HOH 1245 6045 2046 HOH HOH A . 
H 5 HOH 1246 6046 1634 HOH HOH A . 
H 5 HOH 1247 6047 1933 HOH HOH A . 
H 5 HOH 1248 6048 1206 HOH HOH A . 
H 5 HOH 1249 6049 988  HOH HOH A . 
H 5 HOH 1250 6050 1828 HOH HOH A . 
H 5 HOH 1251 6051 1339 HOH HOH A . 
H 5 HOH 1252 6052 1176 HOH HOH A . 
H 5 HOH 1253 6053 643  HOH HOH A . 
H 5 HOH 1254 6054 974  HOH HOH A . 
H 5 HOH 1255 6055 782  HOH HOH A . 
H 5 HOH 1256 6056 2093 HOH HOH A . 
H 5 HOH 1257 6057 1251 HOH HOH A . 
H 5 HOH 1258 6058 2107 HOH HOH A . 
H 5 HOH 1259 6059 1839 HOH HOH A . 
H 5 HOH 1260 6060 1811 HOH HOH A . 
H 5 HOH 1261 6061 1946 HOH HOH A . 
H 5 HOH 1262 6062 2088 HOH HOH A . 
H 5 HOH 1263 6063 931  HOH HOH A . 
H 5 HOH 1264 6064 1435 HOH HOH A . 
H 5 HOH 1265 6065 1818 HOH HOH A . 
H 5 HOH 1266 6066 1061 HOH HOH A . 
H 5 HOH 1267 6067 1409 HOH HOH A . 
H 5 HOH 1268 6068 1256 HOH HOH A . 
H 5 HOH 1269 6069 1856 HOH HOH A . 
H 5 HOH 1270 6070 949  HOH HOH A . 
H 5 HOH 1271 6071 1681 HOH HOH A . 
H 5 HOH 1272 6072 1892 HOH HOH A . 
H 5 HOH 1273 6073 2291 HOH HOH A . 
H 5 HOH 1274 6074 1546 HOH HOH A . 
H 5 HOH 1275 6075 2098 HOH HOH A . 
H 5 HOH 1276 6076 1550 HOH HOH A . 
H 5 HOH 1277 6077 1413 HOH HOH A . 
H 5 HOH 1278 6078 1229 HOH HOH A . 
H 5 HOH 1279 6079 1123 HOH HOH A . 
H 5 HOH 1280 6080 1476 HOH HOH A . 
H 5 HOH 1281 6081 789  HOH HOH A . 
H 5 HOH 1282 6082 725  HOH HOH A . 
H 5 HOH 1283 6083 2041 HOH HOH A . 
H 5 HOH 1284 6084 1906 HOH HOH A . 
H 5 HOH 1285 6085 2242 HOH HOH A . 
H 5 HOH 1286 6086 1378 HOH HOH A . 
H 5 HOH 1287 6087 69   HOH HOH A . 
H 5 HOH 1288 6088 1649 HOH HOH A . 
H 5 HOH 1289 6089 730  HOH HOH A . 
H 5 HOH 1290 6090 625  HOH HOH A . 
H 5 HOH 1291 6091 1491 HOH HOH A . 
H 5 HOH 1292 6092 2108 HOH HOH A . 
H 5 HOH 1293 6093 895  HOH HOH A . 
H 5 HOH 1294 6094 2246 HOH HOH A . 
H 5 HOH 1295 6095 2104 HOH HOH A . 
H 5 HOH 1296 6096 1838 HOH HOH A . 
H 5 HOH 1297 6097 1477 HOH HOH A . 
H 5 HOH 1298 6098 760  HOH HOH A . 
H 5 HOH 1299 6099 1516 HOH HOH A . 
H 5 HOH 1300 6100 1609 HOH HOH A . 
H 5 HOH 1301 6101 713  HOH HOH A . 
H 5 HOH 1302 6102 850  HOH HOH A . 
H 5 HOH 1303 6103 719  HOH HOH A . 
H 5 HOH 1304 6104 2282 HOH HOH A . 
H 5 HOH 1305 6105 940  HOH HOH A . 
H 5 HOH 1306 6106 993  HOH HOH A . 
H 5 HOH 1307 6107 1607 HOH HOH A . 
H 5 HOH 1308 6108 1065 HOH HOH A . 
H 5 HOH 1309 6109 1497 HOH HOH A . 
H 5 HOH 1310 6110 1748 HOH HOH A . 
H 5 HOH 1311 6111 1952 HOH HOH A . 
H 5 HOH 1312 6112 904  HOH HOH A . 
H 5 HOH 1313 6113 2077 HOH HOH A . 
H 5 HOH 1314 6114 1432 HOH HOH A . 
H 5 HOH 1315 6115 2249 HOH HOH A . 
H 5 HOH 1316 6116 1031 HOH HOH A . 
H 5 HOH 1317 6117 1595 HOH HOH A . 
H 5 HOH 1318 6118 1810 HOH HOH A . 
H 5 HOH 1319 6119 1970 HOH HOH A . 
H 5 HOH 1320 6120 1196 HOH HOH A . 
H 5 HOH 1321 6121 2020 HOH HOH A . 
H 5 HOH 1322 6122 955  HOH HOH A . 
H 5 HOH 1323 6123 1656 HOH HOH A . 
H 5 HOH 1324 6124 1460 HOH HOH A . 
H 5 HOH 1325 6125 1216 HOH HOH A . 
H 5 HOH 1326 6126 1510 HOH HOH A . 
H 5 HOH 1327 6127 1949 HOH HOH A . 
H 5 HOH 1328 6128 1899 HOH HOH A . 
H 5 HOH 1329 6129 1719 HOH HOH A . 
H 5 HOH 1330 6130 1532 HOH HOH A . 
H 5 HOH 1331 6131 1639 HOH HOH A . 
H 5 HOH 1332 6132 129  HOH HOH A . 
H 5 HOH 1333 6133 2074 HOH HOH A . 
H 5 HOH 1334 6134 1688 HOH HOH A . 
H 5 HOH 1335 6135 1183 HOH HOH A . 
H 5 HOH 1336 6136 835  HOH HOH A . 
H 5 HOH 1337 6137 1779 HOH HOH A . 
H 5 HOH 1338 6138 609  HOH HOH A . 
H 5 HOH 1339 6139 1019 HOH HOH A . 
H 5 HOH 1340 6140 1650 HOH HOH A . 
H 5 HOH 1341 6141 774  HOH HOH A . 
H 5 HOH 1342 6142 1761 HOH HOH A . 
H 5 HOH 1343 6143 2179 HOH HOH A . 
H 5 HOH 1344 6144 463  HOH HOH A . 
H 5 HOH 1345 6145 1230 HOH HOH A . 
H 5 HOH 1346 6146 1439 HOH HOH A . 
H 5 HOH 1347 6147 1372 HOH HOH A . 
H 5 HOH 1348 6148 1576 HOH HOH A . 
H 5 HOH 1349 6149 1917 HOH HOH A . 
H 5 HOH 1350 6150 1204 HOH HOH A . 
H 5 HOH 1351 6151 156  HOH HOH A . 
H 5 HOH 1352 6152 19   HOH HOH A . 
H 5 HOH 1353 6153 1526 HOH HOH A . 
H 5 HOH 1354 6154 1294 HOH HOH A . 
H 5 HOH 1355 6155 913  HOH HOH A . 
H 5 HOH 1356 6156 1237 HOH HOH A . 
H 5 HOH 1357 6157 1734 HOH HOH A . 
H 5 HOH 1358 6158 398  HOH HOH A . 
H 5 HOH 1359 6159 1663 HOH HOH A . 
H 5 HOH 1360 6160 1260 HOH HOH A . 
H 5 HOH 1361 6161 2178 HOH HOH A . 
H 5 HOH 1362 6162 927  HOH HOH A . 
H 5 HOH 1363 6163 960  HOH HOH A . 
H 5 HOH 1364 6164 761  HOH HOH A . 
H 5 HOH 1365 6165 23   HOH HOH A . 
H 5 HOH 1366 6166 1452 HOH HOH A . 
H 5 HOH 1367 6167 1756 HOH HOH A . 
H 5 HOH 1368 6168 1440 HOH HOH A . 
H 5 HOH 1369 6169 1785 HOH HOH A . 
H 5 HOH 1370 6170 1795 HOH HOH A . 
H 5 HOH 1371 6171 293  HOH HOH A . 
H 5 HOH 1372 6172 145  HOH HOH A . 
H 5 HOH 1373 6173 530  HOH HOH A . 
H 5 HOH 1374 6174 944  HOH HOH A . 
H 5 HOH 1375 6175 2231 HOH HOH A . 
H 5 HOH 1376 6176 2229 HOH HOH A . 
H 5 HOH 1377 6177 2009 HOH HOH A . 
H 5 HOH 1378 6178 1511 HOH HOH A . 
H 5 HOH 1379 6179 1107 HOH HOH A . 
H 5 HOH 1380 6180 866  HOH HOH A . 
H 5 HOH 1381 6181 972  HOH HOH A . 
H 5 HOH 1382 6182 1613 HOH HOH A . 
H 5 HOH 1383 6183 1029 HOH HOH A . 
H 5 HOH 1384 6184 1369 HOH HOH A . 
H 5 HOH 1385 6185 709  HOH HOH A . 
H 5 HOH 1386 6186 480  HOH HOH A . 
H 5 HOH 1387 6187 2254 HOH HOH A . 
H 5 HOH 1388 6188 637  HOH HOH A . 
H 5 HOH 1389 6189 2160 HOH HOH A . 
H 5 HOH 1390 6190 836  HOH HOH A . 
H 5 HOH 1391 6191 656  HOH HOH A . 
H 5 HOH 1392 6192 2227 HOH HOH A . 
H 5 HOH 1393 6193 2302 HOH HOH A . 
H 5 HOH 1394 6194 1765 HOH HOH A . 
H 5 HOH 1395 6195 1170 HOH HOH A . 
H 5 HOH 1396 6196 1506 HOH HOH A . 
H 5 HOH 1397 6197 610  HOH HOH A . 
H 5 HOH 1398 6198 1827 HOH HOH A . 
H 5 HOH 1399 6199 2230 HOH HOH A . 
H 5 HOH 1400 6200 513  HOH HOH A . 
H 5 HOH 1401 6201 1968 HOH HOH A . 
H 5 HOH 1402 6202 1175 HOH HOH A . 
H 5 HOH 1403 6203 1136 HOH HOH A . 
H 5 HOH 1404 6204 1453 HOH HOH A . 
H 5 HOH 1405 6205 1842 HOH HOH A . 
H 5 HOH 1406 6206 1760 HOH HOH A . 
H 5 HOH 1407 6207 1208 HOH HOH A . 
H 5 HOH 1408 6208 1894 HOH HOH A . 
H 5 HOH 1409 6209 1499 HOH HOH A . 
H 5 HOH 1410 6210 1591 HOH HOH A . 
H 5 HOH 1411 6211 1347 HOH HOH A . 
H 5 HOH 1412 6212 18   HOH HOH A . 
H 5 HOH 1413 6213 21   HOH HOH A . 
H 5 HOH 1414 6214 2172 HOH HOH A . 
H 5 HOH 1415 6215 1475 HOH HOH A . 
H 5 HOH 1416 6216 1399 HOH HOH A . 
H 5 HOH 1417 6217 765  HOH HOH A . 
H 5 HOH 1418 6218 2206 HOH HOH A . 
H 5 HOH 1419 6219 1872 HOH HOH A . 
H 5 HOH 1420 6220 92   HOH HOH A . 
H 5 HOH 1421 6221 2100 HOH HOH A . 
H 5 HOH 1422 6222 41   HOH HOH A . 
H 5 HOH 1423 6223 164  HOH HOH A . 
H 5 HOH 1424 6224 2318 HOH HOH A . 
H 5 HOH 1425 6225 1101 HOH HOH A . 
H 5 HOH 1426 6226 1582 HOH HOH A . 
H 5 HOH 1427 6227 1564 HOH HOH A . 
H 5 HOH 1428 6228 233  HOH HOH A . 
H 5 HOH 1429 6229 1493 HOH HOH A . 
H 5 HOH 1430 6230 2278 HOH HOH A . 
H 5 HOH 1431 6231 1052 HOH HOH A . 
H 5 HOH 1432 6232 1490 HOH HOH A . 
H 5 HOH 1433 6233 1231 HOH HOH A . 
H 5 HOH 1434 6234 2225 HOH HOH A . 
H 5 HOH 1435 6235 2083 HOH HOH A . 
H 5 HOH 1436 6236 305  HOH HOH A . 
H 5 HOH 1437 6237 840  HOH HOH A . 
H 5 HOH 1438 6238 2304 HOH HOH A . 
H 5 HOH 1439 6239 937  HOH HOH A . 
H 5 HOH 1440 6240 247  HOH HOH A . 
H 5 HOH 1441 6241 1010 HOH HOH A . 
H 5 HOH 1442 6242 1631 HOH HOH A . 
H 5 HOH 1443 6243 542  HOH HOH A . 
H 5 HOH 1444 6244 1706 HOH HOH A . 
H 5 HOH 1445 6245 2219 HOH HOH A . 
H 5 HOH 1446 6246 2273 HOH HOH A . 
H 5 HOH 1447 6247 27   HOH HOH A . 
H 5 HOH 1448 6248 312  HOH HOH A . 
H 5 HOH 1449 6249 749  HOH HOH A . 
H 5 HOH 1450 6250 177  HOH HOH A . 
H 5 HOH 1451 6251 1886 HOH HOH A . 
H 5 HOH 1452 6252 97   HOH HOH A . 
H 5 HOH 1453 6253 28   HOH HOH A . 
H 5 HOH 1454 6254 401  HOH HOH A . 
H 5 HOH 1455 6255 1887 HOH HOH A . 
H 5 HOH 1456 6256 1291 HOH HOH A . 
H 5 HOH 1457 6257 1459 HOH HOH A . 
H 5 HOH 1458 6258 140  HOH HOH A . 
H 5 HOH 1459 6259 910  HOH HOH A . 
H 5 HOH 1460 6260 1455 HOH HOH A . 
H 5 HOH 1461 6261 1062 HOH HOH A . 
H 5 HOH 1462 6262 1792 HOH HOH A . 
H 5 HOH 1463 6263 1703 HOH HOH A . 
H 5 HOH 1464 6264 915  HOH HOH A . 
H 5 HOH 1465 6265 309  HOH HOH A . 
H 5 HOH 1466 6266 26   HOH HOH A . 
H 5 HOH 1467 6267 1502 HOH HOH A . 
H 5 HOH 1468 6268 184  HOH HOH A . 
H 5 HOH 1469 6269 1745 HOH HOH A . 
H 5 HOH 1470 6270 2121 HOH HOH A . 
H 5 HOH 1471 6271 22   HOH HOH A . 
H 5 HOH 1472 6272 745  HOH HOH A . 
H 5 HOH 1473 6273 93   HOH HOH A . 
H 5 HOH 1474 6274 218  HOH HOH A . 
H 5 HOH 1475 6275 103  HOH HOH A . 
H 5 HOH 1476 6276 1908 HOH HOH A . 
H 5 HOH 1477 6277 8    HOH HOH A . 
H 5 HOH 1478 6278 979  HOH HOH A . 
H 5 HOH 1479 6279 33   HOH HOH A . 
H 5 HOH 1480 6280 339  HOH HOH A . 
H 5 HOH 1481 6281 1597 HOH HOH A . 
H 5 HOH 1482 6282 1003 HOH HOH A . 
H 5 HOH 1483 6283 1508 HOH HOH A . 
H 5 HOH 1484 6284 138  HOH HOH A . 
H 5 HOH 1485 6285 397  HOH HOH A . 
H 5 HOH 1486 6286 733  HOH HOH A . 
H 5 HOH 1487 6287 269  HOH HOH A . 
H 5 HOH 1488 6288 2154 HOH HOH A . 
H 5 HOH 1489 6289 12   HOH HOH A . 
H 5 HOH 1490 6290 1987 HOH HOH A . 
H 5 HOH 1491 6291 244  HOH HOH A . 
H 5 HOH 1492 6292 889  HOH HOH A . 
H 5 HOH 1493 6293 1416 HOH HOH A . 
H 5 HOH 1494 6294 52   HOH HOH A . 
H 5 HOH 1495 6295 2117 HOH HOH A . 
H 5 HOH 1496 6296 36   HOH HOH A . 
H 5 HOH 1497 6297 687  HOH HOH A . 
H 5 HOH 1498 6298 1430 HOH HOH A . 
H 5 HOH 1499 6299 83   HOH HOH A . 
H 5 HOH 1500 6300 389  HOH HOH A . 
H 5 HOH 1501 6301 1469 HOH HOH A . 
H 5 HOH 1502 6302 375  HOH HOH A . 
H 5 HOH 1503 6303 2087 HOH HOH A . 
H 5 HOH 1504 6304 1515 HOH HOH A . 
H 5 HOH 1505 6305 349  HOH HOH A . 
H 5 HOH 1506 6306 75   HOH HOH A . 
H 5 HOH 1507 6307 885  HOH HOH A . 
H 5 HOH 1508 6308 1105 HOH HOH A . 
H 5 HOH 1509 6309 1214 HOH HOH A . 
H 5 HOH 1510 6310 134  HOH HOH A . 
H 5 HOH 1511 6311 95   HOH HOH A . 
H 5 HOH 1512 6312 126  HOH HOH A . 
H 5 HOH 1513 6313 381  HOH HOH A . 
H 5 HOH 1514 6314 1165 HOH HOH A . 
H 5 HOH 1515 6315 162  HOH HOH A . 
H 5 HOH 1516 6316 1331 HOH HOH A . 
H 5 HOH 1517 6317 2316 HOH HOH A . 
H 5 HOH 1518 6318 1403 HOH HOH A . 
H 5 HOH 1519 6319 1929 HOH HOH A . 
H 5 HOH 1520 6320 446  HOH HOH A . 
H 5 HOH 1521 6321 2169 HOH HOH A . 
H 5 HOH 1522 6322 16   HOH HOH A . 
H 5 HOH 1523 6323 29   HOH HOH A . 
H 5 HOH 1524 6324 53   HOH HOH A . 
H 5 HOH 1525 6325 411  HOH HOH A . 
H 5 HOH 1526 6326 551  HOH HOH A . 
H 5 HOH 1527 6327 1008 HOH HOH A . 
H 5 HOH 1528 6328 1423 HOH HOH A . 
H 5 HOH 1529 6329 1127 HOH HOH A . 
H 5 HOH 1530 6330 574  HOH HOH A . 
H 5 HOH 1531 6331 34   HOH HOH A . 
H 5 HOH 1532 6332 360  HOH HOH A . 
H 5 HOH 1533 6333 380  HOH HOH A . 
H 5 HOH 1534 6334 1630 HOH HOH A . 
H 5 HOH 1535 6335 281  HOH HOH A . 
H 5 HOH 1536 6336 39   HOH HOH A . 
H 5 HOH 1537 6337 115  HOH HOH A . 
H 5 HOH 1538 6338 991  HOH HOH A . 
H 5 HOH 1539 6339 209  HOH HOH A . 
H 5 HOH 1540 6340 785  HOH HOH A . 
H 5 HOH 1541 6341 797  HOH HOH A . 
H 5 HOH 1542 6342 341  HOH HOH A . 
H 5 HOH 1543 6343 1911 HOH HOH A . 
H 5 HOH 1544 6344 755  HOH HOH A . 
H 5 HOH 1545 6345 141  HOH HOH A . 
H 5 HOH 1546 6346 592  HOH HOH A . 
H 5 HOH 1547 6347 1638 HOH HOH A . 
H 5 HOH 1548 6348 404  HOH HOH A . 
H 5 HOH 1549 6349 942  HOH HOH A . 
H 5 HOH 1550 6350 1611 HOH HOH A . 
H 5 HOH 1551 6351 1379 HOH HOH A . 
H 5 HOH 1552 6352 1797 HOH HOH A . 
H 5 HOH 1553 6353 215  HOH HOH A . 
H 5 HOH 1554 6354 1486 HOH HOH A . 
H 5 HOH 1555 6355 116  HOH HOH A . 
H 5 HOH 1556 6356 285  HOH HOH A . 
H 5 HOH 1557 6357 122  HOH HOH A . 
H 5 HOH 1558 6358 1702 HOH HOH A . 
H 5 HOH 1559 6359 72   HOH HOH A . 
H 5 HOH 1560 6360 1712 HOH HOH A . 
H 5 HOH 1561 6361 173  HOH HOH A . 
H 5 HOH 1562 6362 1071 HOH HOH A . 
H 5 HOH 1563 6363 2325 HOH HOH A . 
H 5 HOH 1564 6364 35   HOH HOH A . 
H 5 HOH 1565 6365 5    HOH HOH A . 
H 5 HOH 1566 6366 2289 HOH HOH A . 
H 5 HOH 1567 6367 212  HOH HOH A . 
H 5 HOH 1568 6368 337  HOH HOH A . 
H 5 HOH 1569 6369 299  HOH HOH A . 
H 5 HOH 1570 6370 2119 HOH HOH A . 
H 5 HOH 1571 6371 1878 HOH HOH A . 
H 5 HOH 1572 6372 703  HOH HOH A . 
H 5 HOH 1573 6373 153  HOH HOH A . 
H 5 HOH 1574 6374 981  HOH HOH A . 
H 5 HOH 1575 6375 137  HOH HOH A . 
H 5 HOH 1576 6376 251  HOH HOH A . 
H 5 HOH 1577 6377 347  HOH HOH A . 
H 5 HOH 1578 6378 2224 HOH HOH A . 
H 5 HOH 1579 6379 74   HOH HOH A . 
H 5 HOH 1580 6380 101  HOH HOH A . 
H 5 HOH 1581 6381 118  HOH HOH A . 
H 5 HOH 1582 6382 1696 HOH HOH A . 
H 5 HOH 1583 6383 1224 HOH HOH A . 
H 5 HOH 1584 6384 81   HOH HOH A . 
H 5 HOH 1585 6385 198  HOH HOH A . 
H 5 HOH 1586 6386 70   HOH HOH A . 
H 5 HOH 1587 6387 644  HOH HOH A . 
H 5 HOH 1588 6388 1822 HOH HOH A . 
H 5 HOH 1589 6389 117  HOH HOH A . 
H 5 HOH 1590 6390 139  HOH HOH A . 
H 5 HOH 1591 6391 1750 HOH HOH A . 
H 5 HOH 1592 6392 424  HOH HOH A . 
H 5 HOH 1593 6393 355  HOH HOH A . 
H 5 HOH 1594 6394 112  HOH HOH A . 
H 5 HOH 1595 6395 245  HOH HOH A . 
H 5 HOH 1596 6396 58   HOH HOH A . 
H 5 HOH 1597 6397 165  HOH HOH A . 
H 5 HOH 1598 6398 295  HOH HOH A . 
H 5 HOH 1599 6399 152  HOH HOH A . 
H 5 HOH 1600 6400 102  HOH HOH A . 
H 5 HOH 1601 6401 288  HOH HOH A . 
H 5 HOH 1602 6402 80   HOH HOH A . 
H 5 HOH 1603 6403 192  HOH HOH A . 
H 5 HOH 1604 6404 24   HOH HOH A . 
H 5 HOH 1605 6405 1465 HOH HOH A . 
H 5 HOH 1606 6406 84   HOH HOH A . 
H 5 HOH 1607 6407 323  HOH HOH A . 
H 5 HOH 1608 6408 86   HOH HOH A . 
H 5 HOH 1609 6409 351  HOH HOH A . 
H 5 HOH 1610 6410 989  HOH HOH A . 
H 5 HOH 1611 6411 56   HOH HOH A . 
H 5 HOH 1612 6412 150  HOH HOH A . 
H 5 HOH 1613 6413 1716 HOH HOH A . 
H 5 HOH 1614 6414 237  HOH HOH A . 
H 5 HOH 1615 6415 123  HOH HOH A . 
H 5 HOH 1616 6416 294  HOH HOH A . 
H 5 HOH 1617 6417 298  HOH HOH A . 
H 5 HOH 1618 6418 353  HOH HOH A . 
H 5 HOH 1619 6419 188  HOH HOH A . 
H 5 HOH 1620 6420 2112 HOH HOH A . 
H 5 HOH 1621 6421 406  HOH HOH A . 
H 5 HOH 1622 6422 201  HOH HOH A . 
H 5 HOH 1623 6423 94   HOH HOH A . 
H 5 HOH 1624 6424 133  HOH HOH A . 
H 5 HOH 1625 6425 357  HOH HOH A . 
H 5 HOH 1626 6426 279  HOH HOH A . 
H 5 HOH 1627 6427 392  HOH HOH A . 
H 5 HOH 1628 6428 2261 HOH HOH A . 
H 5 HOH 1629 6429 67   HOH HOH A . 
H 5 HOH 1630 6430 358  HOH HOH A . 
H 5 HOH 1631 6431 399  HOH HOH A . 
H 5 HOH 1632 6432 168  HOH HOH A . 
H 5 HOH 1633 6433 197  HOH HOH A . 
H 5 HOH 1634 6434 73   HOH HOH A . 
H 5 HOH 1635 6435 166  HOH HOH A . 
H 5 HOH 1636 6436 170  HOH HOH A . 
H 5 HOH 1637 6437 415  HOH HOH A . 
H 5 HOH 1638 6438 206  HOH HOH A . 
H 5 HOH 1639 6439 37   HOH HOH A . 
H 5 HOH 1640 6440 178  HOH HOH A . 
H 5 HOH 1641 6441 259  HOH HOH A . 
H 5 HOH 1642 6442 91   HOH HOH A . 
H 5 HOH 1643 6443 196  HOH HOH A . 
H 5 HOH 1644 6444 334  HOH HOH A . 
H 5 HOH 1645 6445 149  HOH HOH A . 
H 5 HOH 1646 6446 1617 HOH HOH A . 
H 5 HOH 1647 6447 124  HOH HOH A . 
H 5 HOH 1648 6448 2309 HOH HOH A . 
H 5 HOH 1649 6449 1964 HOH HOH A . 
H 5 HOH 1650 6450 110  HOH HOH A . 
H 5 HOH 1651 6451 328  HOH HOH A . 
H 5 HOH 1652 6452 143  HOH HOH A . 
H 5 HOH 1653 6453 107  HOH HOH A . 
H 5 HOH 1654 6454 79   HOH HOH A . 
H 5 HOH 1655 6455 2102 HOH HOH A . 
H 5 HOH 1656 6456 114  HOH HOH A . 
H 5 HOH 1657 6457 2270 HOH HOH A . 
H 5 HOH 1658 6458 267  HOH HOH A . 
H 5 HOH 1659 6459 232  HOH HOH A . 
H 5 HOH 1660 6460 390  HOH HOH A . 
H 5 HOH 1661 6461 151  HOH HOH A . 
H 5 HOH 1662 6462 2177 HOH HOH A . 
H 5 HOH 1663 6463 345  HOH HOH A . 
H 5 HOH 1664 6464 221  HOH HOH A . 
H 5 HOH 1665 6465 147  HOH HOH A . 
H 5 HOH 1666 6466 417  HOH HOH A . 
H 5 HOH 1667 6467 155  HOH HOH A . 
H 5 HOH 1668 6468 224  HOH HOH A . 
H 5 HOH 1669 6469 109  HOH HOH A . 
H 5 HOH 1670 6470 15   HOH HOH A . 
H 5 HOH 1671 6471 204  HOH HOH A . 
H 5 HOH 1672 6472 519  HOH HOH A . 
H 5 HOH 1673 6473 106  HOH HOH A . 
H 5 HOH 1674 6474 306  HOH HOH A . 
H 5 HOH 1675 6475 199  HOH HOH A . 
H 5 HOH 1676 6476 43   HOH HOH A . 
H 5 HOH 1677 6477 382  HOH HOH A . 
H 5 HOH 1678 6478 77   HOH HOH A . 
H 5 HOH 1679 6479 387  HOH HOH A . 
H 5 HOH 1680 6480 49   HOH HOH A . 
H 5 HOH 1681 6481 55   HOH HOH A . 
H 5 HOH 1682 6482 44   HOH HOH A . 
H 5 HOH 1683 6483 179  HOH HOH A . 
H 5 HOH 1684 6484 228  HOH HOH A . 
H 5 HOH 1685 6485 105  HOH HOH A . 
H 5 HOH 1686 6486 395  HOH HOH A . 
H 5 HOH 1687 6487 90   HOH HOH A . 
H 5 HOH 1688 6488 128  HOH HOH A . 
H 5 HOH 1689 6489 290  HOH HOH A . 
H 5 HOH 1690 6490 964  HOH HOH A . 
H 5 HOH 1691 6491 65   HOH HOH A . 
H 5 HOH 1692 6492 343  HOH HOH A . 
H 5 HOH 1693 6493 391  HOH HOH A . 
H 5 HOH 1694 6494 182  HOH HOH A . 
H 5 HOH 1695 6495 361  HOH HOH A . 
H 5 HOH 1696 6496 4    HOH HOH A . 
H 5 HOH 1697 6497 408  HOH HOH A . 
H 5 HOH 1698 6498 100  HOH HOH A . 
H 5 HOH 1699 6499 291  HOH HOH A . 
H 5 HOH 1700 6500 317  HOH HOH A . 
H 5 HOH 1701 6501 371  HOH HOH A . 
H 5 HOH 1702 6502 311  HOH HOH A . 
H 5 HOH 1703 6503 213  HOH HOH A . 
H 5 HOH 1704 6504 923  HOH HOH A . 
H 5 HOH 1705 6505 260  HOH HOH A . 
H 5 HOH 1706 6506 249  HOH HOH A . 
H 5 HOH 1707 6507 784  HOH HOH A . 
H 5 HOH 1708 6508 211  HOH HOH A . 
H 5 HOH 1709 6509 287  HOH HOH A . 
H 5 HOH 1710 6510 98   HOH HOH A . 
H 5 HOH 1711 6511 315  HOH HOH A . 
H 5 HOH 1712 6512 6    HOH HOH A . 
H 5 HOH 1713 6513 400  HOH HOH A . 
H 5 HOH 1714 6514 318  HOH HOH A . 
H 5 HOH 1715 6515 1787 HOH HOH A . 
H 5 HOH 1716 6516 385  HOH HOH A . 
H 5 HOH 1717 6517 333  HOH HOH A . 
H 5 HOH 1718 6518 208  HOH HOH A . 
H 5 HOH 1719 6519 59   HOH HOH A . 
H 5 HOH 1720 6520 261  HOH HOH A . 
H 5 HOH 1721 6521 88   HOH HOH A . 
H 5 HOH 1722 6522 230  HOH HOH A . 
H 5 HOH 1723 6523 263  HOH HOH A . 
H 5 HOH 1724 6524 321  HOH HOH A . 
H 5 HOH 1725 6525 322  HOH HOH A . 
H 5 HOH 1726 6526 405  HOH HOH A . 
H 5 HOH 1727 6527 1544 HOH HOH A . 
H 5 HOH 1728 6528 66   HOH HOH A . 
H 5 HOH 1729 6529 325  HOH HOH A . 
H 5 HOH 1730 6530 68   HOH HOH A . 
H 5 HOH 1731 6531 200  HOH HOH A . 
H 5 HOH 1732 6532 282  HOH HOH A . 
H 5 HOH 1733 6533 236  HOH HOH A . 
H 5 HOH 1734 6534 423  HOH HOH A . 
H 5 HOH 1735 6535 136  HOH HOH A . 
H 5 HOH 1736 6536 256  HOH HOH A . 
H 5 HOH 1737 6537 246  HOH HOH A . 
H 5 HOH 1738 6538 78   HOH HOH A . 
H 5 HOH 1739 6539 393  HOH HOH A . 
H 5 HOH 1740 6540 414  HOH HOH A . 
H 5 HOH 1741 6541 108  HOH HOH A . 
H 5 HOH 1742 6542 354  HOH HOH A . 
H 5 HOH 1743 6543 429  HOH HOH A . 
H 5 HOH 1744 6544 194  HOH HOH A . 
H 5 HOH 1745 6545 111  HOH HOH A . 
H 5 HOH 1746 6546 286  HOH HOH A . 
H 5 HOH 1747 6547 30   HOH HOH A . 
H 5 HOH 1748 6548 42   HOH HOH A . 
H 5 HOH 1749 6549 307  HOH HOH A . 
H 5 HOH 1750 6550 190  HOH HOH A . 
H 5 HOH 1751 6551 227  HOH HOH A . 
H 5 HOH 1752 6552 51   HOH HOH A . 
H 5 HOH 1753 6553 132  HOH HOH A . 
H 5 HOH 1754 6554 250  HOH HOH A . 
H 5 HOH 1755 6555 327  HOH HOH A . 
H 5 HOH 1756 6556 216  HOH HOH A . 
H 5 HOH 1757 6557 54   HOH HOH A . 
H 5 HOH 1758 6558 425  HOH HOH A . 
H 5 HOH 1759 6559 76   HOH HOH A . 
H 5 HOH 1760 6560 255  HOH HOH A . 
H 5 HOH 1761 6561 301  HOH HOH A . 
H 5 HOH 1762 6562 40   HOH HOH A . 
H 5 HOH 1763 6563 252  HOH HOH A . 
H 5 HOH 1764 6564 205  HOH HOH A . 
H 5 HOH 1765 6565 348  HOH HOH A . 
H 5 HOH 1766 6566 64   HOH HOH A . 
H 5 HOH 1767 6567 1901 HOH HOH A . 
H 5 HOH 1768 6568 384  HOH HOH A . 
H 5 HOH 1769 6569 163  HOH HOH A . 
H 5 HOH 1770 6570 71   HOH HOH A . 
H 5 HOH 1771 6571 420  HOH HOH A . 
H 5 HOH 1772 6572 167  HOH HOH A . 
H 5 HOH 1773 6573 7    HOH HOH A . 
H 5 HOH 1774 6574 130  HOH HOH A . 
H 5 HOH 1775 6575 159  HOH HOH A . 
H 5 HOH 1776 6576 2322 HOH HOH A . 
H 5 HOH 1777 6577 416  HOH HOH A . 
H 5 HOH 1778 6578 121  HOH HOH A . 
H 5 HOH 1779 6579 248  HOH HOH A . 
H 5 HOH 1780 6580 271  HOH HOH A . 
H 5 HOH 1781 6581 338  HOH HOH A . 
H 5 HOH 1782 6582 302  HOH HOH A . 
H 5 HOH 1783 6583 210  HOH HOH A . 
H 5 HOH 1784 6584 254  HOH HOH A . 
H 5 HOH 1785 6585 203  HOH HOH A . 
H 5 HOH 1786 6586 2237 HOH HOH A . 
H 5 HOH 1787 6587 268  HOH HOH A . 
H 5 HOH 1788 6588 428  HOH HOH A . 
H 5 HOH 1789 6589 283  HOH HOH A . 
H 5 HOH 1790 6590 63   HOH HOH A . 
H 5 HOH 1791 6591 284  HOH HOH A . 
H 5 HOH 1792 6592 264  HOH HOH A . 
H 5 HOH 1793 6593 373  HOH HOH A . 
H 5 HOH 1794 6594 120  HOH HOH A . 
H 5 HOH 1795 6595 331  HOH HOH A . 
H 5 HOH 1796 6596 278  HOH HOH A . 
H 5 HOH 1797 6597 418  HOH HOH A . 
H 5 HOH 1798 6598 266  HOH HOH A . 
H 5 HOH 1799 6599 1556 HOH HOH A . 
H 5 HOH 1800 6600 326  HOH HOH A . 
H 5 HOH 1801 6601 191  HOH HOH A . 
H 5 HOH 1802 6602 396  HOH HOH A . 
H 5 HOH 1803 6603 303  HOH HOH A . 
H 5 HOH 1804 6604 99   HOH HOH A . 
H 5 HOH 1805 6605 229  HOH HOH A . 
H 5 HOH 1806 6606 17   HOH HOH A . 
H 5 HOH 1807 6607 257  HOH HOH A . 
H 5 HOH 1808 6608 57   HOH HOH A . 
H 5 HOH 1809 6609 296  HOH HOH A . 
H 5 HOH 1810 6610 289  HOH HOH A . 
H 5 HOH 1811 6611 388  HOH HOH A . 
H 5 HOH 1812 6612 146  HOH HOH A . 
H 5 HOH 1813 6613 356  HOH HOH A . 
H 5 HOH 1814 6614 340  HOH HOH A . 
H 5 HOH 1815 6615 234  HOH HOH A . 
H 5 HOH 1816 6616 310  HOH HOH A . 
H 5 HOH 1817 6617 243  HOH HOH A . 
H 5 HOH 1818 6618 104  HOH HOH A . 
H 5 HOH 1819 6619 50   HOH HOH A . 
H 5 HOH 1820 6620 421  HOH HOH A . 
H 5 HOH 1821 6621 175  HOH HOH A . 
H 5 HOH 1822 6622 369  HOH HOH A . 
H 5 HOH 1823 6623 320  HOH HOH A . 
H 5 HOH 1824 6624 274  HOH HOH A . 
H 5 HOH 1825 6625 335  HOH HOH A . 
H 5 HOH 1826 6626 427  HOH HOH A . 
H 5 HOH 1827 6627 368  HOH HOH A . 
H 5 HOH 1828 6628 1945 HOH HOH A . 
H 5 HOH 1829 6629 195  HOH HOH A . 
H 5 HOH 1830 6630 125  HOH HOH A . 
H 5 HOH 1831 6631 223  HOH HOH A . 
H 5 HOH 1832 6632 374  HOH HOH A . 
H 5 HOH 1833 6633 176  HOH HOH A . 
H 5 HOH 1834 6634 25   HOH HOH A . 
H 5 HOH 1835 6635 413  HOH HOH A . 
H 5 HOH 1836 6636 412  HOH HOH A . 
H 5 HOH 1837 6637 422  HOH HOH A . 
H 5 HOH 1838 6638 169  HOH HOH A . 
H 5 HOH 1839 6639 241  HOH HOH A . 
H 5 HOH 1840 6640 275  HOH HOH A . 
H 5 HOH 1841 6641 96   HOH HOH A . 
H 5 HOH 1842 6642 336  HOH HOH A . 
H 5 HOH 1843 6643 258  HOH HOH A . 
H 5 HOH 1844 6644 240  HOH HOH A . 
H 5 HOH 1845 6645 222  HOH HOH A . 
H 5 HOH 1846 6646 238  HOH HOH A . 
H 5 HOH 1847 6647 426  HOH HOH A . 
H 5 HOH 1848 6648 174  HOH HOH A . 
H 5 HOH 1849 6649 674  HOH HOH A . 
H 5 HOH 1850 6650 61   HOH HOH A . 
H 5 HOH 1851 6651 214  HOH HOH A . 
H 5 HOH 1852 6652 239  HOH HOH A . 
H 5 HOH 1853 6653 217  HOH HOH A . 
H 5 HOH 1854 6654 350  HOH HOH A . 
H 5 HOH 1855 6655 367  HOH HOH A . 
H 5 HOH 1856 6656 280  HOH HOH A . 
H 5 HOH 1857 6657 62   HOH HOH A . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BLZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BLZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_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                   9BLZ 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9BLZ 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.002 ? 23919 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.545 ? 32445 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 5.737 ? 3191  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.041 ? 3645  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004 ? 4156  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9BLZ 
_struct.title                        'State-1(phi motor) of full-length human dynein-1 in 5mM ATP' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BLZ 
_struct_keywords.text            'dynein-1, MOTOR PROTEIN' 
_struct_keywords.pdbx_keywords   'MOTOR PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 2 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DYHC1_HUMAN 
_struct_ref.pdbx_db_accession          Q14204 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BLZ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 4646 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q14204 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  4646 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       4646 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 MET A 1457 ? TYR A 1473 ? MET A 1457 TYR A 1473 1 ? 17 
HELX_P HELX_P2   AA2 GLY A 1489 ? LYS A 1508 ? GLY A 1489 LYS A 1508 1 ? 20 
HELX_P HELX_P3   AA3 TYR A 1513 ? VAL A 1515 ? TYR A 1513 VAL A 1515 5 ? 3  
HELX_P HELX_P4   AA4 PHE A 1516 ? GLY A 1553 ? PHE A 1516 GLY A 1553 1 ? 38 
HELX_P HELX_P5   AA5 ALA A 1555 ? LEU A 1561 ? ALA A 1555 LEU A 1561 1 ? 7  
HELX_P HELX_P6   AA6 LEU A 1561 ? SER A 1585 ? LEU A 1561 SER A 1585 1 ? 25 
HELX_P HELX_P7   AA7 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P8   AA8 GLY A 1596 ? LEU A 1615 ? GLY A 1596 LEU A 1615 1 ? 20 
HELX_P HELX_P9   AA9 LEU A 1615 ? PHE A 1626 ? LEU A 1615 PHE A 1626 1 ? 12 
HELX_P HELX_P10  AB1 PRO A 1627 ? VAL A 1632 ? PRO A 1627 VAL A 1632 5 ? 6  
HELX_P HELX_P11  AB2 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P12  AB3 ASN A 1646 ? LYS A 1652 ? ASN A 1646 LYS A 1652 5 ? 7  
HELX_P HELX_P13  AB4 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P14  AB5 LYS A 1697 ? GLY A 1728 ? LYS A 1697 GLY A 1728 1 ? 32 
HELX_P HELX_P15  AB6 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P16  AB7 GLN A 1746 ? MET A 1769 ? GLN A 1746 MET A 1769 1 ? 24 
HELX_P HELX_P17  AB8 GLY A 1770 ? GLY A 1772 ? GLY A 1770 GLY A 1772 5 ? 3  
HELX_P HELX_P18  AB9 PRO A 1777 ? MET A 1798 ? PRO A 1777 MET A 1798 1 ? 22 
HELX_P HELX_P19  AC1 PRO A 1801 ? SER A 1828 ? PRO A 1801 SER A 1828 1 ? 28 
HELX_P HELX_P20  AC2 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P21  AC3 ASP A 1852 ? GLN A 1855 ? ASP A 1852 GLN A 1855 5 ? 4  
HELX_P HELX_P22  AC4 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P23  AC5 GLY A 1911 ? LEU A 1923 ? GLY A 1911 LEU A 1923 1 ? 13 
HELX_P HELX_P24  AC6 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P25  AC7 PHE A 1960 ? LEU A 1963 ? PHE A 1960 LEU A 1963 5 ? 4  
HELX_P HELX_P26  AC8 GLU A 1964 ? ASN A 1987 ? GLU A 1964 ASN A 1987 1 ? 24 
HELX_P HELX_P27  AC9 PRO A 2029 ? LYS A 2034 ? PRO A 2029 LYS A 2034 1 ? 6  
HELX_P HELX_P28  AD1 ASP A 2045 ? GLY A 2058 ? ASP A 2045 GLY A 2058 1 ? 14 
HELX_P HELX_P29  AD2 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P30  AD3 GLY A 2089 ? ARG A 2118 ? GLY A 2089 ARG A 2118 1 ? 30 
HELX_P HELX_P31  AD4 ASP A 2123 ? ASN A 2130 ? ASP A 2123 ASN A 2130 1 ? 8  
HELX_P HELX_P32  AD5 PRO A 2132 ? VAL A 2146 ? PRO A 2132 VAL A 2146 1 ? 15 
HELX_P HELX_P33  AD6 PRO A 2147 ? LEU A 2149 ? PRO A 2147 LEU A 2149 5 ? 3  
HELX_P HELX_P34  AD7 VAL A 2150 ? GLU A 2152 ? VAL A 2150 GLU A 2152 5 ? 3  
HELX_P HELX_P35  AD8 ASP A 2153 ? PHE A 2165 ? ASP A 2153 PHE A 2165 1 ? 13 
HELX_P HELX_P36  AD9 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P37  AE1 GLY A 2200 ? GLN A 2215 ? GLY A 2200 GLN A 2215 1 ? 16 
HELX_P HELX_P38  AE2 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P39  AE3 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P40  AE4 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P41  AE5 GLY A 2293 ? LYS A 2297 ? GLY A 2293 LYS A 2297 5 ? 5  
HELX_P HELX_P42  AE6 ASP A 2308 ? GLU A 2313 ? ASP A 2308 GLU A 2313 1 ? 6  
HELX_P HELX_P43  AE7 LEU A 2315 ? ASP A 2320 ? LEU A 2315 ASP A 2320 1 ? 6  
HELX_P HELX_P44  AE8 THR A 2352 ? ARG A 2358 ? THR A 2352 ARG A 2358 1 ? 7  
HELX_P HELX_P45  AE9 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P46  AF1 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P47  AF2 PRO A 2425 ? THR A 2428 ? PRO A 2425 THR A 2428 5 ? 4  
HELX_P HELX_P48  AF3 GLY A 2431 ? LEU A 2443 ? GLY A 2431 LEU A 2443 1 ? 13 
HELX_P HELX_P49  AF4 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P50  AF5 GLN A 2482 ? GLY A 2504 ? GLN A 2482 GLY A 2504 1 ? 23 
HELX_P HELX_P51  AF6 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P52  AF7 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P53  AF8 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P54  AF9 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P55  AG1 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P56  AG2 GLY A 2600 ? ALA A 2611 ? GLY A 2600 ALA A 2611 1 ? 12 
HELX_P HELX_P57  AG3 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P58  AG4 GLN A 2677 ? GLY A 2690 ? GLN A 2677 GLY A 2690 1 ? 14 
HELX_P HELX_P59  AG5 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P60  AG6 GLY A 2740 ? LEU A 2756 ? GLY A 2740 LEU A 2756 1 ? 17 
HELX_P HELX_P61  AG7 ARG A 2757 ? LEU A 2758 ? ARG A 2757 LEU A 2758 5 ? 2  
HELX_P HELX_P62  AG8 ILE A 2759 ? THR A 2764 ? ILE A 2759 THR A 2764 5 ? 6  
HELX_P HELX_P63  AG9 TYR A 2765 ? PHE A 2784 ? TYR A 2765 PHE A 2784 1 ? 20 
HELX_P HELX_P64  AH1 SER A 2795 ? ALA A 2809 ? SER A 2795 ALA A 2809 1 ? 15 
HELX_P HELX_P65  AH2 PRO A 2817 ? PHE A 2833 ? PRO A 2817 PHE A 2833 1 ? 17 
HELX_P HELX_P66  AH3 GLN A 2834 ? LEU A 2837 ? GLN A 2834 LEU A 2837 5 ? 4  
HELX_P HELX_P67  AH4 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P68  AH5 ASP A 2862 ? SER A 2868 ? ASP A 2862 SER A 2868 1 ? 7  
HELX_P HELX_P69  AH6 ASP A 2885 ? GLU A 2904 ? ASP A 2885 GLU A 2904 1 ? 20 
HELX_P HELX_P70  AH7 PHE A 2912 ? ARG A 2927 ? PHE A 2912 ARG A 2927 1 ? 16 
HELX_P HELX_P71  AH8 GLY A 2942 ? ASN A 2954 ? GLY A 2942 ASN A 2954 1 ? 13 
HELX_P HELX_P72  AH9 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P73  AI1 SER A 2997 ? VAL A 2999 ? SER A 2997 VAL A 2999 5 ? 3  
HELX_P HELX_P74  AI2 ASP A 3001 ? GLY A 3015 ? ASP A 3001 GLY A 3015 1 ? 15 
HELX_P HELX_P75  AI3 GLY A 3023 ? GLU A 3040 ? GLY A 3023 GLU A 3040 1 ? 18 
HELX_P HELX_P76  AI4 SER A 3046 ? ASN A 3061 ? SER A 3046 ASN A 3061 1 ? 16 
HELX_P HELX_P77  AI5 SER A 3071 ? SER A 3082 ? SER A 3071 SER A 3082 1 ? 12 
HELX_P HELX_P78  AI6 PRO A 3083 ? ASN A 3087 ? PRO A 3083 ASN A 3087 5 ? 5  
HELX_P HELX_P79  AI7 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P80  AI8 SER A 3138 ? ARG A 3164 ? SER A 3138 ARG A 3164 1 ? 27 
HELX_P HELX_P81  AI9 THR A 3172 ? GLU A 3217 ? THR A 3172 GLU A 3217 1 ? 46 
HELX_P HELX_P82  AJ1 ASN A 3473 ? LEU A 3482 ? ASN A 3473 LEU A 3482 1 ? 10 
HELX_P HELX_P83  AJ2 LEU A 3482 ? THR A 3495 ? LEU A 3482 THR A 3495 1 ? 14 
HELX_P HELX_P84  AJ3 THR A 3495 ? ALA A 3517 ? THR A 3495 ALA A 3517 1 ? 23 
HELX_P HELX_P85  AJ4 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P86  AJ5 ALA A 3548 ? SER A 3554 ? ALA A 3548 SER A 3554 1 ? 7  
HELX_P HELX_P87  AJ6 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P88  AJ7 ASP A 3570 ? PHE A 3583 ? ASP A 3570 PHE A 3583 1 ? 14 
HELX_P HELX_P89  AJ8 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P90  AJ9 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P91  AK1 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P92  AK2 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P93  AK3 LEU A 3645 ? ASN A 3650 ? LEU A 3645 ASN A 3650 1 ? 6  
HELX_P HELX_P94  AK4 PRO A 3689 ? ARG A 3695 ? PRO A 3689 ARG A 3695 1 ? 7  
HELX_P HELX_P95  AK5 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P96  AK6 ARG A 3721 ? GLU A 3755 ? ARG A 3721 GLU A 3755 1 ? 35 
HELX_P HELX_P97  AK7 ASP A 3763 ? GLN A 3799 ? ASP A 3763 GLN A 3799 1 ? 37 
HELX_P HELX_P98  AK8 TYR A 3801 ? LEU A 3818 ? TYR A 3801 LEU A 3818 1 ? 18 
HELX_P HELX_P99  AK9 LYS A 3819 ? ILE A 3821 ? LYS A 3819 ILE A 3821 5 ? 3  
HELX_P HELX_P100 AL1 SER A 3828 ? GLU A 3842 ? SER A 3828 GLU A 3842 1 ? 15 
HELX_P HELX_P101 AL2 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P102 AL3 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P103 AL4 LEU A 3876 ? GLY A 3894 ? LEU A 3876 GLY A 3894 1 ? 19 
HELX_P HELX_P104 AL5 TYR A 3901 ? LEU A 3909 ? TYR A 3901 LEU A 3909 1 ? 9  
HELX_P HELX_P105 AL6 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P106 AL7 ASP A 3946 ? ASP A 3954 ? ASP A 3946 ASP A 3954 1 ? 9  
HELX_P HELX_P107 AL8 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P108 AL9 SER A 3965 ? VAL A 3970 ? SER A 3965 VAL A 3970 5 ? 6  
HELX_P HELX_P109 AM1 THR A 3981 ? ARG A 3997 ? THR A 3981 ARG A 3997 1 ? 17 
HELX_P HELX_P110 AM2 ARG A 4000 ? GLY A 4014 ? ARG A 4000 GLY A 4014 1 ? 15 
HELX_P HELX_P111 AM3 MET A 4018 ? GLN A 4023 ? MET A 4018 GLN A 4023 5 ? 6  
HELX_P HELX_P112 AM4 ASP A 4026 ? GLU A 4034 ? ASP A 4026 GLU A 4034 1 ? 9  
HELX_P HELX_P113 AM5 ALA A 4051 ? ASN A 4063 ? ALA A 4051 ASN A 4063 1 ? 13 
HELX_P HELX_P114 AM6 SER A 4073 ? VAL A 4088 ? SER A 4073 VAL A 4088 1 ? 16 
HELX_P HELX_P115 AM7 ASN A 4098 ? LEU A 4101 ? ASN A 4098 LEU A 4101 5 ? 4  
HELX_P HELX_P116 AM8 ALA A 4102 ? SER A 4115 ? ALA A 4102 SER A 4115 1 ? 14 
HELX_P HELX_P117 AM9 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P118 AN1 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P119 AN2 PRO A 4165 ? CYS A 4170 ? PRO A 4165 CYS A 4170 1 ? 6  
HELX_P HELX_P120 AN3 GLU A 4175 ? TYR A 4196 ? GLU A 4175 TYR A 4196 1 ? 22 
HELX_P HELX_P121 AN4 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P122 AN5 SER A 4234 ? ILE A 4238 ? SER A 4234 ILE A 4238 5 ? 5  
HELX_P HELX_P123 AN6 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P124 AN7 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P125 AN8 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P126 AN9 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P127 AO1 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P128 AO2 PRO A 4324 ? ALA A 4327 ? PRO A 4324 ALA A 4327 5 ? 4  
HELX_P HELX_P129 AO3 GLU A 4328 ? MET A 4346 ? GLU A 4328 MET A 4346 1 ? 19 
HELX_P HELX_P130 AO4 ALA A 4375 ? ILE A 4391 ? ALA A 4375 ILE A 4391 1 ? 17 
HELX_P HELX_P131 AO5 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P132 AO6 THR A 4445 ? LYS A 4457 ? THR A 4445 LYS A 4457 1 ? 13 
HELX_P HELX_P133 AO7 THR A 4474 ? SER A 4498 ? THR A 4474 SER A 4498 1 ? 25 
HELX_P HELX_P134 AO8 GLY A 4500 ? LYS A 4505 ? GLY A 4500 LYS A 4505 5 ? 6  
HELX_P HELX_P135 AO9 VAL A 4516 ? ASN A 4532 ? VAL A 4516 ASN A 4532 1 ? 17 
HELX_P HELX_P136 AP1 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P137 AP2 ASP A 4631 ? ARG A 4638 ? ASP A 4631 ARG A 4638 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A THR 1913 OG1 ? ? ? 1_555 F MG  . MG ? ? A THR 1913 A MG  4705 1_555 ? ? ? ? ? ? ? 2.099 ? ? 
metalc2  metalc ? ? A SER 2231 OG  ? ? ? 1_555 G MG  . MG ? ? A SER 2231 A MG  4706 1_555 ? ? ? ? ? ? ? 1.876 ? ? 
metalc3  metalc ? ? A GLU 2344 OE2 ? ? ? 1_555 G MG  . MG ? ? A GLU 2344 A MG  4706 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
metalc4  metalc ? ? B ADP .    O3B ? ? ? 1_555 F MG  . MG ? ? A ADP 4701 A MG  4705 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
metalc5  metalc ? ? C ATP .    O2G ? ? ? 1_555 G MG  . MG ? ? A ATP 4702 A MG  4706 1_555 ? ? ? ? ? ? ? 1.907 ? ? 
metalc6  metalc ? ? C ATP .    O2B ? ? ? 1_555 G MG  . MG ? ? A ATP 4702 A MG  4706 1_555 ? ? ? ? ? ? ? 2.666 ? ? 
metalc7  metalc ? ? C ATP .    O3B ? ? ? 1_555 G MG  . MG ? ? A ATP 4702 A MG  4706 1_555 ? ? ? ? ? ? ? 2.967 ? ? 
metalc8  metalc ? ? F MG  .    MG  ? ? ? 1_555 H HOH . O  ? ? A MG  4705 A HOH 5172 1_555 ? ? ? ? ? ? ? 2.094 ? ? 
metalc9  metalc ? ? F MG  .    MG  ? ? ? 1_555 H HOH . O  ? ? A MG  4705 A HOH 5188 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc10 metalc ? ? F MG  .    MG  ? ? ? 1_555 H HOH . O  ? ? A MG  4705 A HOH 5232 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
metalc11 metalc ? ? F MG  .    MG  ? ? ? 1_555 H HOH . O  ? ? A MG  4705 A HOH 5554 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
metalc12 metalc ? ? G MG  .    MG  ? ? ? 1_555 H HOH . O  ? ? A MG  4706 A HOH 4823 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc13 metalc ? ? G MG  .    MG  ? ? ? 1_555 H HOH . O  ? ? A MG  4706 A HOH 4887 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O3B ? B ADP .    ? A ADP 4701 ? 1_555 110.0 ? 
2  OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5172 ? 1_555 154.1 ? 
3  O3B ? B ADP .    ? A ADP 4701 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5172 ? 1_555 91.2  ? 
4  OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5188 ? 1_555 97.5  ? 
5  O3B ? B ADP .    ? A ADP 4701 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5188 ? 1_555 108.5 ? 
6  O   ? H HOH .    ? A HOH 5172 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5188 ? 1_555 89.1  ? 
7  OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5232 ? 1_555 82.3  ? 
8  O3B ? B ADP .    ? A ADP 4701 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5232 ? 1_555 164.3 ? 
9  O   ? H HOH .    ? A HOH 5172 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5232 ? 1_555 74.6  ? 
10 O   ? H HOH .    ? A HOH 5188 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5232 ? 1_555 78.4  ? 
11 OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5554 ? 1_555 85.8  ? 
12 O3B ? B ADP .    ? A ADP 4701 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5554 ? 1_555 85.5  ? 
13 O   ? H HOH .    ? A HOH 5172 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5554 ? 1_555 81.1  ? 
14 O   ? H HOH .    ? A HOH 5188 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5554 ? 1_555 163.3 ? 
15 O   ? H HOH .    ? A HOH 5232 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 5554 ? 1_555 85.9  ? 
16 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 75.4  ? 
17 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 153.0 ? 
18 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 90.1  ? 
19 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 73.7  ? 
20 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 104.0 ? 
21 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 88.2  ? 
22 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 120.3 ? 
23 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 135.7 ? 
24 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 56.6  ? 
25 O2B ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O3B ? C ATP .    ? A ATP 4702 ? 1_555 52.5  ? 
26 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O   ? H HOH .    ? A HOH 4823 ? 1_555 93.6  ? 
27 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O   ? H HOH .    ? A HOH 4823 ? 1_555 150.3 ? 
28 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O   ? H HOH .    ? A HOH 4823 ? 1_555 109.3 ? 
29 O2B ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O   ? H HOH .    ? A HOH 4823 ? 1_555 99.1  ? 
30 O3B ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O   ? H HOH .    ? A HOH 4823 ? 1_555 73.7  ? 
31 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O   ? H HOH .    ? A HOH 4887 ? 1_555 97.8  ? 
32 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O   ? H HOH .    ? A HOH 4887 ? 1_555 68.4  ? 
33 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O   ? H HOH .    ? A HOH 4887 ? 1_555 97.8  ? 
34 O2B ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O   ? H HOH .    ? A HOH 4887 ? 1_555 170.2 ? 
35 O3B ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O   ? H HOH .    ? A HOH 4887 ? 1_555 137.3 ? 
36 O   ? H HOH .    ? A HOH 4823 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O   ? H HOH .    ? A HOH 4887 ? 1_555 86.3  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 2 ? 
AB5 ? 5 ? 
AB6 ? 5 ? 
AB7 ? 3 ? 
AB8 ? 5 ? 
AB9 ? 2 ? 
AC1 ? 4 ? 
AC2 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB3 1 2 ? anti-parallel 
AB3 2 3 ? parallel      
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB6 4 5 ? parallel      
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? parallel      
AB8 3 4 ? parallel      
AB8 4 5 ? parallel      
AB9 1 2 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? parallel      
AC2 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 1476 ? TYR A 1480 ? ASP A 1476 TYR A 1480 
AA1 2 CYS A 1484 ? ARG A 1488 ? CYS A 1484 ARG A 1488 
AA2 1 SER A 1663 ? LEU A 1666 ? SER A 1663 LEU A 1666 
AA2 2 VAL A 1672 ? SER A 1677 ? VAL A 1672 SER A 1677 
AA2 3 GLU A 1683 ? SER A 1691 ? GLU A 1683 SER A 1691 
AA3 1 MET A 1842 ? PHE A 1846 ? MET A 1842 PHE A 1846 
AA3 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA3 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA4 1 GLY A 1901 ? PHE A 1905 ? GLY A 1901 PHE A 1905 
AA4 2 PHE A 2036 ? ALA A 2040 ? PHE A 2036 ALA A 2040 
AA5 1 VAL A 1927 ? ASN A 1931 ? VAL A 1927 ASN A 1931 
AA5 2 TRP A 1954 ? ASP A 1958 ? TRP A 1954 ASP A 1958 
AA5 3 ALA A 2013 ? THR A 2017 ? ALA A 2013 THR A 2017 
AA6 1 THR A 1998 ? LEU A 2001 ? THR A 1998 LEU A 2001 
AA6 2 LYS A 2004 ? LYS A 2007 ? LYS A 2004 LYS A 2007 
AA7 1 GLY A 2249 ? ILE A 2254 ? GLY A 2249 ILE A 2254 
AA7 2 ARG A 2298 ? ASP A 2304 ? ARG A 2298 ASP A 2304 
AA7 3 VAL A 2339 ? VAL A 2345 ? VAL A 2339 VAL A 2345 
AA7 4 GLY A 2219 ? VAL A 2223 ? GLY A 2219 VAL A 2223 
AA7 5 GLY A 2360 ? TRP A 2363 ? GLY A 2360 TRP A 2363 
AA8 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA8 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AA9 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA9 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AB1 1 TYR A 2537 ? SER A 2540 ? TYR A 2537 SER A 2540 
AB1 2 GLU A 2544 ? PRO A 2547 ? GLU A 2544 PRO A 2547 
AB2 1 MET A 2615 ? LEU A 2620 ? MET A 2615 LEU A 2620 
AB2 2 TRP A 2658 ? CYS A 2663 ? TRP A 2658 CYS A 2663 
AB2 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB2 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB2 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB3 1 CYS A 2639 ? THR A 2644 ? CYS A 2639 THR A 2644 
AB3 2 GLY A 2647 ? PRO A 2652 ? GLY A 2647 PRO A 2652 
AB3 3 THR A 2699 ? LEU A 2703 ? THR A 2699 LEU A 2703 
AB3 4 GLY A 2691 ? ARG A 2694 ? GLY A 2691 ARG A 2694 
AB4 1 TYR A 2873 ? SER A 2874 ? TYR A 2873 SER A 2874 
AB4 2 ILE A 2882 ? PRO A 2883 ? ILE A 2882 PRO A 2883 
AB5 1 SER A 2957 ? TYR A 2959 ? SER A 2957 TYR A 2959 
AB5 2 ILE A 2990 ? ASP A 2995 ? ILE A 2990 ASP A 2995 
AB5 3 LEU A 3062 ? MET A 3068 ? LEU A 3062 MET A 3068 
AB5 4 HIS A 2932 ? GLY A 2937 ? HIS A 2932 GLY A 2937 
AB5 5 CYS A 3089 ? GLY A 3095 ? CYS A 3089 GLY A 3095 
AB6 1 THR A 3610 ? SER A 3613 ? THR A 3610 SER A 3613 
AB6 2 PRO A 3632 ? GLN A 3636 ? PRO A 3632 GLN A 3636 
AB6 3 VAL A 3676 ? THR A 3681 ? VAL A 3676 THR A 3681 
AB6 4 TYR A 3586 ? ILE A 3590 ? TYR A 3586 ILE A 3590 
AB6 5 VAL A 3696 ? ASN A 3700 ? VAL A 3696 ASN A 3700 
AB7 1 VAL A 3653 ? THR A 3656 ? VAL A 3653 THR A 3656 
AB7 2 ARG A 3659 ? LEU A 3664 ? ARG A 3659 LEU A 3664 
AB7 3 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB8 1 ILE A 4066 ? ALA A 4070 ? ILE A 4066 ALA A 4070 
AB8 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB8 3 ARG A 4123 ? GLU A 4129 ? ARG A 4123 GLU A 4129 
AB8 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB8 5 ARG A 4143 ? PHE A 4147 ? ARG A 4143 PHE A 4147 
AB9 1 LYS A 4283 ? ALA A 4285 ? LYS A 4283 ALA A 4285 
AB9 2 ILE A 4294 ? GLN A 4295 ? ILE A 4294 GLN A 4295 
AC1 1 VAL A 4509 ? CYS A 4510 ? VAL A 4509 CYS A 4510 
AC1 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AC1 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AC1 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AC2 1 LEU A 4575 ? ALA A 4584 ? LEU A 4575 ALA A 4584 
AC2 2 LYS A 4564 ? CYS A 4570 ? LYS A 4564 CYS A 4570 
AC2 3 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AC2 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AC2 5 LEU A 4618 ? GLU A 4625 ? LEU A 4618 GLU A 4625 
# 
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 TYR A 1480 ? N TYR A 1480 O CYS A 1484 ? O CYS A 1484 
AA2 1 2 N ILE A 1665 ? N ILE A 1665 O GLY A 1675 ? O GLY A 1675 
AA2 2 3 N VAL A 1673 ? N VAL A 1673 O VAL A 1690 ? O VAL A 1690 
AA3 1 2 N ARG A 1843 ? N ARG A 1843 O GLN A 1860 ? O GLN A 1860 
AA3 2 3 N ILE A 1859 ? N ILE A 1859 O PHE A 1866 ? O PHE A 1866 
AA4 1 2 N GLY A 1901 ? N GLY A 1901 O ARG A 2037 ? O ARG A 2037 
AA5 1 2 N LEU A 1928 ? N LEU A 1928 O CYS A 1956 ? O CYS A 1956 
AA5 2 3 N GLY A 1955 ? N GLY A 1955 O PHE A 2015 ? O PHE A 2015 
AA6 1 2 N CYS A 1999 ? N CYS A 1999 O VAL A 2006 ? O VAL A 2006 
AA7 1 2 N VAL A 2250 ? N VAL A 2250 O ARG A 2298 ? O ARG A 2298 
AA7 2 3 N ILE A 2301 ? N ILE A 2301 O MET A 2342 ? O MET A 2342 
AA7 3 4 O ILE A 2341 ? O ILE A 2341 N LEU A 2220 ? N LEU A 2220 
AA7 4 5 N MET A 2221 ? N MET A 2221 O GLY A 2360 ? O GLY A 2360 
AA8 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA9 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AB1 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB2 1 2 N LEU A 2620 ? N LEU A 2620 O PHE A 2662 ? O PHE A 2662 
AB2 2 3 N CYS A 2663 ? N CYS A 2663 O ALA A 2711 ? O ALA A 2711 
AB2 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2591 ? N LEU A 2591 
AB2 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB3 1 2 N GLU A 2640 ? N GLU A 2640 O ALA A 2651 ? O ALA A 2651 
AB3 2 3 N VAL A 2648 ? N VAL A 2648 O LYS A 2702 ? O LYS A 2702 
AB3 3 4 O VAL A 2701 ? O VAL A 2701 N PHE A 2692 ? N PHE A 2692 
AB4 1 2 N SER A 2874 ? N SER A 2874 O ILE A 2882 ? O ILE A 2882 
AB5 1 2 N TYR A 2959 ? N TYR A 2959 O ALA A 2991 ? O ALA A 2991 
AB5 2 3 N MET A 2994 ? N MET A 2994 O VAL A 3065 ? O VAL A 3065 
AB5 3 4 O PHE A 3066 ? O PHE A 3066 N LEU A 2933 ? N LEU A 2933 
AB5 4 5 N LEU A 2934 ? N LEU A 2934 O ASN A 3092 ? O ASN A 3092 
AB6 1 2 N THR A 3612 ? N THR A 3612 O LEU A 3634 ? O LEU A 3634 
AB6 2 3 N VAL A 3635 ? N VAL A 3635 O PHE A 3678 ? O PHE A 3678 
AB6 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB6 4 5 N LEU A 3588 ? N LEU A 3588 O THR A 3697 ? O THR A 3697 
AB7 1 2 N ARG A 3654 ? N ARG A 3654 O LEU A 3661 ? O LEU A 3661 
AB7 2 3 N ILE A 3662 ? N ILE A 3662 O ILE A 3669 ? O ILE A 3669 
AB8 1 2 N THR A 4067 ? N THR A 4067 O MET A 4095 ? O MET A 4095 
AB8 2 3 N LEU A 4096 ? N LEU A 4096 O PHE A 4125 ? O PHE A 4125 
AB8 3 4 O LEU A 4124 ? O LEU A 4124 N VAL A 4041 ? N VAL A 4041 
AB8 4 5 N CYS A 4044 ? N CYS A 4044 O PHE A 4147 ? O PHE A 4147 
AB9 1 2 N ALA A 4285 ? N ALA A 4285 O ILE A 4294 ? O ILE A 4294 
AC1 1 2 N VAL A 4509 ? N VAL A 4509 O THR A 4561 ? O THR A 4561 
AC1 2 3 N VAL A 4560 ? N VAL A 4560 O THR A 4588 ? O THR A 4588 
AC1 3 4 O GLN A 4589 ? O GLN A 4589 N ASN A 4544 ? N ASN A 4544 
AC2 1 2 O THR A 4583 ? O THR A 4583 N LEU A 4565 ? N LEU A 4565 
AC2 2 3 N GLN A 4566 ? N GLN A 4566 O ALA A 4641 ? O ALA A 4641 
AC2 3 4 O VAL A 4642 ? O VAL A 4642 N TYR A 4610 ? N TYR A 4610 
AC2 4 5 N VAL A 4609 ? N VAL A 4609 O ILE A 4619 ? O ILE A 4619 
# 
_pdbx_entry_details.entry_id                   9BLZ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NE2 A GLN 1612 ? ? OE1 A GLU 1635 ? ? 2.08 
2 1 OH  A TYR 2794 ? ? O   A HOH 4801 ? ? 2.13 
3 1 OG  A SER 4234 ? ? OD1 A ASP 4236 ? ? 2.14 
4 1 OE1 A GLU 2775 ? ? NE2 A HIS 2857 ? ? 2.18 
5 1 O   A HOH 4891 ? ? O   A HOH 5372 ? ? 2.18 
6 1 O   A GLY 2940 ? ? O   A HOH 4802 ? ? 2.18 
7 1 O   A HOH 4813 ? ? O   A HOH 5827 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 CYS A 1484 ? ? -161.24 -166.31 
2  1 ALA A 1862 ? ? 56.94   -120.83 
3  1 THR A 2061 ? ? -98.37  37.06   
4  1 THR A 2764 ? ? -59.46  -7.12   
5  1 LYS A 3608 ? ? 61.60   62.65   
6  1 PRO A 3643 ? ? -64.52  0.38    
7  1 ARG A 3910 ? ? 50.88   -104.99 
8  1 ASP A 3946 ? ? -95.71  51.95   
9  1 CYS A 4170 ? ? -98.60  40.13   
10 1 GLU A 4206 ? ? -97.25  59.58   
11 1 PRO A 4239 ? ? -69.93  75.09   
12 1 TYR A 4252 ? ? 76.28   -5.60   
13 1 ASN A 4597 ? ? 35.72   48.34   
14 1 GLU A 4599 ? ? 56.89   -158.47 
15 1 ALA A 4602 ? ? 64.70   -0.71   
16 1 ILE A 4619 ? ? -91.85  -60.81  
17 1 PHE A 4620 ? ? -162.19 -168.95 
18 1 THR A 4628 ? ? 45.03   -131.77 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BLZ 
_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                    9BLZ 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.2 
_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               872840 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ATP' 
_em_buffer.pH            7.2 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'state-1 (phi motor) of full-length human dynein-1 in 5mM ATP' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BLZ 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             5000 
_em_imaging.calibrated_defocus_min          3000 
_em_imaging.calibrated_defocus_max          3000 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        105000 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            50 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              9BLZ 
_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                9BLZ 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A MET 1    ? A MET 1    
2    1 Y 1 A SER 2    ? A SER 2    
3    1 Y 1 A GLU 3    ? A GLU 3    
4    1 Y 1 A PRO 4    ? A PRO 4    
5    1 Y 1 A GLY 5    ? A GLY 5    
6    1 Y 1 A GLY 6    ? A GLY 6    
7    1 Y 1 A GLY 7    ? A GLY 7    
8    1 Y 1 A GLY 8    ? A GLY 8    
9    1 Y 1 A GLY 9    ? A GLY 9    
10   1 Y 1 A GLU 10   ? A GLU 10   
11   1 Y 1 A ASP 11   ? A ASP 11   
12   1 Y 1 A GLY 12   ? A GLY 12   
13   1 Y 1 A SER 13   ? A SER 13   
14   1 Y 1 A ALA 14   ? A ALA 14   
15   1 Y 1 A GLY 15   ? A GLY 15   
16   1 Y 1 A LEU 16   ? A LEU 16   
17   1 Y 1 A GLU 17   ? A GLU 17   
18   1 Y 1 A VAL 18   ? A VAL 18   
19   1 Y 1 A SER 19   ? A SER 19   
20   1 Y 1 A ALA 20   ? A ALA 20   
21   1 Y 1 A VAL 21   ? A VAL 21   
22   1 Y 1 A GLN 22   ? A GLN 22   
23   1 Y 1 A ASN 23   ? A ASN 23   
24   1 Y 1 A VAL 24   ? A VAL 24   
25   1 Y 1 A ALA 25   ? A ALA 25   
26   1 Y 1 A ASP 26   ? A ASP 26   
27   1 Y 1 A VAL 27   ? A VAL 27   
28   1 Y 1 A SER 28   ? A SER 28   
29   1 Y 1 A VAL 29   ? A VAL 29   
30   1 Y 1 A LEU 30   ? A LEU 30   
31   1 Y 1 A GLN 31   ? A GLN 31   
32   1 Y 1 A LYS 32   ? A LYS 32   
33   1 Y 1 A HIS 33   ? A HIS 33   
34   1 Y 1 A LEU 34   ? A LEU 34   
35   1 Y 1 A ARG 35   ? A ARG 35   
36   1 Y 1 A LYS 36   ? A LYS 36   
37   1 Y 1 A LEU 37   ? A LEU 37   
38   1 Y 1 A VAL 38   ? A VAL 38   
39   1 Y 1 A PRO 39   ? A PRO 39   
40   1 Y 1 A LEU 40   ? A LEU 40   
41   1 Y 1 A LEU 41   ? A LEU 41   
42   1 Y 1 A LEU 42   ? A LEU 42   
43   1 Y 1 A GLU 43   ? A GLU 43   
44   1 Y 1 A ASP 44   ? A ASP 44   
45   1 Y 1 A GLY 45   ? A GLY 45   
46   1 Y 1 A GLY 46   ? A GLY 46   
47   1 Y 1 A GLU 47   ? A GLU 47   
48   1 Y 1 A ALA 48   ? A ALA 48   
49   1 Y 1 A PRO 49   ? A PRO 49   
50   1 Y 1 A ALA 50   ? A ALA 50   
51   1 Y 1 A ALA 51   ? A ALA 51   
52   1 Y 1 A LEU 52   ? A LEU 52   
53   1 Y 1 A GLU 53   ? A GLU 53   
54   1 Y 1 A ALA 54   ? A ALA 54   
55   1 Y 1 A ALA 55   ? A ALA 55   
56   1 Y 1 A LEU 56   ? A LEU 56   
57   1 Y 1 A GLU 57   ? A GLU 57   
58   1 Y 1 A GLU 58   ? A GLU 58   
59   1 Y 1 A LYS 59   ? A LYS 59   
60   1 Y 1 A SER 60   ? A SER 60   
61   1 Y 1 A ALA 61   ? A ALA 61   
62   1 Y 1 A LEU 62   ? A LEU 62   
63   1 Y 1 A GLU 63   ? A GLU 63   
64   1 Y 1 A GLN 64   ? A GLN 64   
65   1 Y 1 A MET 65   ? A MET 65   
66   1 Y 1 A ARG 66   ? A ARG 66   
67   1 Y 1 A LYS 67   ? A LYS 67   
68   1 Y 1 A PHE 68   ? A PHE 68   
69   1 Y 1 A LEU 69   ? A LEU 69   
70   1 Y 1 A SER 70   ? A SER 70   
71   1 Y 1 A ASP 71   ? A ASP 71   
72   1 Y 1 A PRO 72   ? A PRO 72   
73   1 Y 1 A GLN 73   ? A GLN 73   
74   1 Y 1 A VAL 74   ? A VAL 74   
75   1 Y 1 A HIS 75   ? A HIS 75   
76   1 Y 1 A THR 76   ? A THR 76   
77   1 Y 1 A VAL 77   ? A VAL 77   
78   1 Y 1 A LEU 78   ? A LEU 78   
79   1 Y 1 A VAL 79   ? A VAL 79   
80   1 Y 1 A GLU 80   ? A GLU 80   
81   1 Y 1 A ARG 81   ? A ARG 81   
82   1 Y 1 A SER 82   ? A SER 82   
83   1 Y 1 A THR 83   ? A THR 83   
84   1 Y 1 A LEU 84   ? A LEU 84   
85   1 Y 1 A LYS 85   ? A LYS 85   
86   1 Y 1 A GLU 86   ? A GLU 86   
87   1 Y 1 A ASP 87   ? A ASP 87   
88   1 Y 1 A VAL 88   ? A VAL 88   
89   1 Y 1 A GLY 89   ? A GLY 89   
90   1 Y 1 A ASP 90   ? A ASP 90   
91   1 Y 1 A GLU 91   ? A GLU 91   
92   1 Y 1 A GLY 92   ? A GLY 92   
93   1 Y 1 A GLU 93   ? A GLU 93   
94   1 Y 1 A GLU 94   ? A GLU 94   
95   1 Y 1 A GLU 95   ? A GLU 95   
96   1 Y 1 A LYS 96   ? A LYS 96   
97   1 Y 1 A GLU 97   ? A GLU 97   
98   1 Y 1 A PHE 98   ? A PHE 98   
99   1 Y 1 A ILE 99   ? A ILE 99   
100  1 Y 1 A SER 100  ? A SER 100  
101  1 Y 1 A TYR 101  ? A TYR 101  
102  1 Y 1 A ASN 102  ? A ASN 102  
103  1 Y 1 A ILE 103  ? A ILE 103  
104  1 Y 1 A ASN 104  ? A ASN 104  
105  1 Y 1 A ILE 105  ? A ILE 105  
106  1 Y 1 A ASP 106  ? A ASP 106  
107  1 Y 1 A ILE 107  ? A ILE 107  
108  1 Y 1 A HIS 108  ? A HIS 108  
109  1 Y 1 A TYR 109  ? A TYR 109  
110  1 Y 1 A GLY 110  ? A GLY 110  
111  1 Y 1 A VAL 111  ? A VAL 111  
112  1 Y 1 A LYS 112  ? A LYS 112  
113  1 Y 1 A SER 113  ? A SER 113  
114  1 Y 1 A ASN 114  ? A ASN 114  
115  1 Y 1 A SER 115  ? A SER 115  
116  1 Y 1 A LEU 116  ? A LEU 116  
117  1 Y 1 A ALA 117  ? A ALA 117  
118  1 Y 1 A PHE 118  ? A PHE 118  
119  1 Y 1 A ILE 119  ? A ILE 119  
120  1 Y 1 A LYS 120  ? A LYS 120  
121  1 Y 1 A ARG 121  ? A ARG 121  
122  1 Y 1 A THR 122  ? A THR 122  
123  1 Y 1 A PRO 123  ? A PRO 123  
124  1 Y 1 A VAL 124  ? A VAL 124  
125  1 Y 1 A ILE 125  ? A ILE 125  
126  1 Y 1 A ASP 126  ? A ASP 126  
127  1 Y 1 A ALA 127  ? A ALA 127  
128  1 Y 1 A ASP 128  ? A ASP 128  
129  1 Y 1 A LYS 129  ? A LYS 129  
130  1 Y 1 A PRO 130  ? A PRO 130  
131  1 Y 1 A VAL 131  ? A VAL 131  
132  1 Y 1 A SER 132  ? A SER 132  
133  1 Y 1 A SER 133  ? A SER 133  
134  1 Y 1 A GLN 134  ? A GLN 134  
135  1 Y 1 A LEU 135  ? A LEU 135  
136  1 Y 1 A ARG 136  ? A ARG 136  
137  1 Y 1 A VAL 137  ? A VAL 137  
138  1 Y 1 A LEU 138  ? A LEU 138  
139  1 Y 1 A THR 139  ? A THR 139  
140  1 Y 1 A LEU 140  ? A LEU 140  
141  1 Y 1 A SER 141  ? A SER 141  
142  1 Y 1 A GLU 142  ? A GLU 142  
143  1 Y 1 A ASP 143  ? A ASP 143  
144  1 Y 1 A SER 144  ? A SER 144  
145  1 Y 1 A PRO 145  ? A PRO 145  
146  1 Y 1 A TYR 146  ? A TYR 146  
147  1 Y 1 A GLU 147  ? A GLU 147  
148  1 Y 1 A THR 148  ? A THR 148  
149  1 Y 1 A LEU 149  ? A LEU 149  
150  1 Y 1 A HIS 150  ? A HIS 150  
151  1 Y 1 A SER 151  ? A SER 151  
152  1 Y 1 A PHE 152  ? A PHE 152  
153  1 Y 1 A ILE 153  ? A ILE 153  
154  1 Y 1 A SER 154  ? A SER 154  
155  1 Y 1 A ASN 155  ? A ASN 155  
156  1 Y 1 A ALA 156  ? A ALA 156  
157  1 Y 1 A VAL 157  ? A VAL 157  
158  1 Y 1 A ALA 158  ? A ALA 158  
159  1 Y 1 A PRO 159  ? A PRO 159  
160  1 Y 1 A PHE 160  ? A PHE 160  
161  1 Y 1 A PHE 161  ? A PHE 161  
162  1 Y 1 A LYS 162  ? A LYS 162  
163  1 Y 1 A SER 163  ? A SER 163  
164  1 Y 1 A TYR 164  ? A TYR 164  
165  1 Y 1 A ILE 165  ? A ILE 165  
166  1 Y 1 A ARG 166  ? A ARG 166  
167  1 Y 1 A GLU 167  ? A GLU 167  
168  1 Y 1 A SER 168  ? A SER 168  
169  1 Y 1 A GLY 169  ? A GLY 169  
170  1 Y 1 A LYS 170  ? A LYS 170  
171  1 Y 1 A ALA 171  ? A ALA 171  
172  1 Y 1 A ASP 172  ? A ASP 172  
173  1 Y 1 A ARG 173  ? A ARG 173  
174  1 Y 1 A ASP 174  ? A ASP 174  
175  1 Y 1 A GLY 175  ? A GLY 175  
176  1 Y 1 A ASP 176  ? A ASP 176  
177  1 Y 1 A LYS 177  ? A LYS 177  
178  1 Y 1 A MET 178  ? A MET 178  
179  1 Y 1 A ALA 179  ? A ALA 179  
180  1 Y 1 A PRO 180  ? A PRO 180  
181  1 Y 1 A SER 181  ? A SER 181  
182  1 Y 1 A VAL 182  ? A VAL 182  
183  1 Y 1 A GLU 183  ? A GLU 183  
184  1 Y 1 A LYS 184  ? A LYS 184  
185  1 Y 1 A LYS 185  ? A LYS 185  
186  1 Y 1 A ILE 186  ? A ILE 186  
187  1 Y 1 A ALA 187  ? A ALA 187  
188  1 Y 1 A GLU 188  ? A GLU 188  
189  1 Y 1 A LEU 189  ? A LEU 189  
190  1 Y 1 A GLU 190  ? A GLU 190  
191  1 Y 1 A MET 191  ? A MET 191  
192  1 Y 1 A GLY 192  ? A GLY 192  
193  1 Y 1 A LEU 193  ? A LEU 193  
194  1 Y 1 A LEU 194  ? A LEU 194  
195  1 Y 1 A HIS 195  ? A HIS 195  
196  1 Y 1 A LEU 196  ? A LEU 196  
197  1 Y 1 A GLN 197  ? A GLN 197  
198  1 Y 1 A GLN 198  ? A GLN 198  
199  1 Y 1 A ASN 199  ? A ASN 199  
200  1 Y 1 A ILE 200  ? A ILE 200  
201  1 Y 1 A GLU 201  ? A GLU 201  
202  1 Y 1 A ILE 202  ? A ILE 202  
203  1 Y 1 A PRO 203  ? A PRO 203  
204  1 Y 1 A GLU 204  ? A GLU 204  
205  1 Y 1 A ILE 205  ? A ILE 205  
206  1 Y 1 A SER 206  ? A SER 206  
207  1 Y 1 A LEU 207  ? A LEU 207  
208  1 Y 1 A PRO 208  ? A PRO 208  
209  1 Y 1 A ILE 209  ? A ILE 209  
210  1 Y 1 A HIS 210  ? A HIS 210  
211  1 Y 1 A PRO 211  ? A PRO 211  
212  1 Y 1 A MET 212  ? A MET 212  
213  1 Y 1 A ILE 213  ? A ILE 213  
214  1 Y 1 A THR 214  ? A THR 214  
215  1 Y 1 A ASN 215  ? A ASN 215  
216  1 Y 1 A VAL 216  ? A VAL 216  
217  1 Y 1 A ALA 217  ? A ALA 217  
218  1 Y 1 A LYS 218  ? A LYS 218  
219  1 Y 1 A GLN 219  ? A GLN 219  
220  1 Y 1 A CYS 220  ? A CYS 220  
221  1 Y 1 A TYR 221  ? A TYR 221  
222  1 Y 1 A GLU 222  ? A GLU 222  
223  1 Y 1 A ARG 223  ? A ARG 223  
224  1 Y 1 A GLY 224  ? A GLY 224  
225  1 Y 1 A GLU 225  ? A GLU 225  
226  1 Y 1 A LYS 226  ? A LYS 226  
227  1 Y 1 A PRO 227  ? A PRO 227  
228  1 Y 1 A LYS 228  ? A LYS 228  
229  1 Y 1 A VAL 229  ? A VAL 229  
230  1 Y 1 A THR 230  ? A THR 230  
231  1 Y 1 A ASP 231  ? A ASP 231  
232  1 Y 1 A PHE 232  ? A PHE 232  
233  1 Y 1 A GLY 233  ? A GLY 233  
234  1 Y 1 A ASP 234  ? A ASP 234  
235  1 Y 1 A LYS 235  ? A LYS 235  
236  1 Y 1 A VAL 236  ? A VAL 236  
237  1 Y 1 A GLU 237  ? A GLU 237  
238  1 Y 1 A ASP 238  ? A ASP 238  
239  1 Y 1 A PRO 239  ? A PRO 239  
240  1 Y 1 A THR 240  ? A THR 240  
241  1 Y 1 A PHE 241  ? A PHE 241  
242  1 Y 1 A LEU 242  ? A LEU 242  
243  1 Y 1 A ASN 243  ? A ASN 243  
244  1 Y 1 A GLN 244  ? A GLN 244  
245  1 Y 1 A LEU 245  ? A LEU 245  
246  1 Y 1 A GLN 246  ? A GLN 246  
247  1 Y 1 A SER 247  ? A SER 247  
248  1 Y 1 A GLY 248  ? A GLY 248  
249  1 Y 1 A VAL 249  ? A VAL 249  
250  1 Y 1 A ASN 250  ? A ASN 250  
251  1 Y 1 A ARG 251  ? A ARG 251  
252  1 Y 1 A TRP 252  ? A TRP 252  
253  1 Y 1 A ILE 253  ? A ILE 253  
254  1 Y 1 A ARG 254  ? A ARG 254  
255  1 Y 1 A GLU 255  ? A GLU 255  
256  1 Y 1 A ILE 256  ? A ILE 256  
257  1 Y 1 A GLN 257  ? A GLN 257  
258  1 Y 1 A LYS 258  ? A LYS 258  
259  1 Y 1 A VAL 259  ? A VAL 259  
260  1 Y 1 A THR 260  ? A THR 260  
261  1 Y 1 A LYS 261  ? A LYS 261  
262  1 Y 1 A LEU 262  ? A LEU 262  
263  1 Y 1 A ASP 263  ? A ASP 263  
264  1 Y 1 A ARG 264  ? A ARG 264  
265  1 Y 1 A ASP 265  ? A ASP 265  
266  1 Y 1 A PRO 266  ? A PRO 266  
267  1 Y 1 A ALA 267  ? A ALA 267  
268  1 Y 1 A SER 268  ? A SER 268  
269  1 Y 1 A GLY 269  ? A GLY 269  
270  1 Y 1 A THR 270  ? A THR 270  
271  1 Y 1 A ALA 271  ? A ALA 271  
272  1 Y 1 A LEU 272  ? A LEU 272  
273  1 Y 1 A GLN 273  ? A GLN 273  
274  1 Y 1 A GLU 274  ? A GLU 274  
275  1 Y 1 A ILE 275  ? A ILE 275  
276  1 Y 1 A SER 276  ? A SER 276  
277  1 Y 1 A PHE 277  ? A PHE 277  
278  1 Y 1 A TRP 278  ? A TRP 278  
279  1 Y 1 A LEU 279  ? A LEU 279  
280  1 Y 1 A ASN 280  ? A ASN 280  
281  1 Y 1 A LEU 281  ? A LEU 281  
282  1 Y 1 A GLU 282  ? A GLU 282  
283  1 Y 1 A ARG 283  ? A ARG 283  
284  1 Y 1 A ALA 284  ? A ALA 284  
285  1 Y 1 A LEU 285  ? A LEU 285  
286  1 Y 1 A TYR 286  ? A TYR 286  
287  1 Y 1 A ARG 287  ? A ARG 287  
288  1 Y 1 A ILE 288  ? A ILE 288  
289  1 Y 1 A GLN 289  ? A GLN 289  
290  1 Y 1 A GLU 290  ? A GLU 290  
291  1 Y 1 A LYS 291  ? A LYS 291  
292  1 Y 1 A ARG 292  ? A ARG 292  
293  1 Y 1 A GLU 293  ? A GLU 293  
294  1 Y 1 A SER 294  ? A SER 294  
295  1 Y 1 A PRO 295  ? A PRO 295  
296  1 Y 1 A GLU 296  ? A GLU 296  
297  1 Y 1 A VAL 297  ? A VAL 297  
298  1 Y 1 A LEU 298  ? A LEU 298  
299  1 Y 1 A LEU 299  ? A LEU 299  
300  1 Y 1 A THR 300  ? A THR 300  
301  1 Y 1 A LEU 301  ? A LEU 301  
302  1 Y 1 A ASP 302  ? A ASP 302  
303  1 Y 1 A ILE 303  ? A ILE 303  
304  1 Y 1 A LEU 304  ? A LEU 304  
305  1 Y 1 A LYS 305  ? A LYS 305  
306  1 Y 1 A HIS 306  ? A HIS 306  
307  1 Y 1 A GLY 307  ? A GLY 307  
308  1 Y 1 A LYS 308  ? A LYS 308  
309  1 Y 1 A ARG 309  ? A ARG 309  
310  1 Y 1 A PHE 310  ? A PHE 310  
311  1 Y 1 A HIS 311  ? A HIS 311  
312  1 Y 1 A ALA 312  ? A ALA 312  
313  1 Y 1 A THR 313  ? A THR 313  
314  1 Y 1 A VAL 314  ? A VAL 314  
315  1 Y 1 A SER 315  ? A SER 315  
316  1 Y 1 A PHE 316  ? A PHE 316  
317  1 Y 1 A ASP 317  ? A ASP 317  
318  1 Y 1 A THR 318  ? A THR 318  
319  1 Y 1 A ASP 319  ? A ASP 319  
320  1 Y 1 A THR 320  ? A THR 320  
321  1 Y 1 A GLY 321  ? A GLY 321  
322  1 Y 1 A LEU 322  ? A LEU 322  
323  1 Y 1 A LYS 323  ? A LYS 323  
324  1 Y 1 A GLN 324  ? A GLN 324  
325  1 Y 1 A ALA 325  ? A ALA 325  
326  1 Y 1 A LEU 326  ? A LEU 326  
327  1 Y 1 A GLU 327  ? A GLU 327  
328  1 Y 1 A THR 328  ? A THR 328  
329  1 Y 1 A VAL 329  ? A VAL 329  
330  1 Y 1 A ASN 330  ? A ASN 330  
331  1 Y 1 A ASP 331  ? A ASP 331  
332  1 Y 1 A TYR 332  ? A TYR 332  
333  1 Y 1 A ASN 333  ? A ASN 333  
334  1 Y 1 A PRO 334  ? A PRO 334  
335  1 Y 1 A LEU 335  ? A LEU 335  
336  1 Y 1 A MET 336  ? A MET 336  
337  1 Y 1 A LYS 337  ? A LYS 337  
338  1 Y 1 A ASP 338  ? A ASP 338  
339  1 Y 1 A PHE 339  ? A PHE 339  
340  1 Y 1 A PRO 340  ? A PRO 340  
341  1 Y 1 A LEU 341  ? A LEU 341  
342  1 Y 1 A ASN 342  ? A ASN 342  
343  1 Y 1 A ASP 343  ? A ASP 343  
344  1 Y 1 A LEU 344  ? A LEU 344  
345  1 Y 1 A LEU 345  ? A LEU 345  
346  1 Y 1 A SER 346  ? A SER 346  
347  1 Y 1 A ALA 347  ? A ALA 347  
348  1 Y 1 A THR 348  ? A THR 348  
349  1 Y 1 A GLU 349  ? A GLU 349  
350  1 Y 1 A LEU 350  ? A LEU 350  
351  1 Y 1 A ASP 351  ? A ASP 351  
352  1 Y 1 A LYS 352  ? A LYS 352  
353  1 Y 1 A ILE 353  ? A ILE 353  
354  1 Y 1 A ARG 354  ? A ARG 354  
355  1 Y 1 A GLN 355  ? A GLN 355  
356  1 Y 1 A ALA 356  ? A ALA 356  
357  1 Y 1 A LEU 357  ? A LEU 357  
358  1 Y 1 A VAL 358  ? A VAL 358  
359  1 Y 1 A ALA 359  ? A ALA 359  
360  1 Y 1 A ILE 360  ? A ILE 360  
361  1 Y 1 A PHE 361  ? A PHE 361  
362  1 Y 1 A THR 362  ? A THR 362  
363  1 Y 1 A HIS 363  ? A HIS 363  
364  1 Y 1 A LEU 364  ? A LEU 364  
365  1 Y 1 A ARG 365  ? A ARG 365  
366  1 Y 1 A LYS 366  ? A LYS 366  
367  1 Y 1 A ILE 367  ? A ILE 367  
368  1 Y 1 A ARG 368  ? A ARG 368  
369  1 Y 1 A ASN 369  ? A ASN 369  
370  1 Y 1 A THR 370  ? A THR 370  
371  1 Y 1 A LYS 371  ? A LYS 371  
372  1 Y 1 A TYR 372  ? A TYR 372  
373  1 Y 1 A PRO 373  ? A PRO 373  
374  1 Y 1 A ILE 374  ? A ILE 374  
375  1 Y 1 A GLN 375  ? A GLN 375  
376  1 Y 1 A ARG 376  ? A ARG 376  
377  1 Y 1 A ALA 377  ? A ALA 377  
378  1 Y 1 A LEU 378  ? A LEU 378  
379  1 Y 1 A ARG 379  ? A ARG 379  
380  1 Y 1 A LEU 380  ? A LEU 380  
381  1 Y 1 A VAL 381  ? A VAL 381  
382  1 Y 1 A GLU 382  ? A GLU 382  
383  1 Y 1 A ALA 383  ? A ALA 383  
384  1 Y 1 A ILE 384  ? A ILE 384  
385  1 Y 1 A SER 385  ? A SER 385  
386  1 Y 1 A ARG 386  ? A ARG 386  
387  1 Y 1 A ASP 387  ? A ASP 387  
388  1 Y 1 A LEU 388  ? A LEU 388  
389  1 Y 1 A SER 389  ? A SER 389  
390  1 Y 1 A SER 390  ? A SER 390  
391  1 Y 1 A GLN 391  ? A GLN 391  
392  1 Y 1 A LEU 392  ? A LEU 392  
393  1 Y 1 A LEU 393  ? A LEU 393  
394  1 Y 1 A LYS 394  ? A LYS 394  
395  1 Y 1 A VAL 395  ? A VAL 395  
396  1 Y 1 A LEU 396  ? A LEU 396  
397  1 Y 1 A GLY 397  ? A GLY 397  
398  1 Y 1 A THR 398  ? A THR 398  
399  1 Y 1 A ARG 399  ? A ARG 399  
400  1 Y 1 A LYS 400  ? A LYS 400  
401  1 Y 1 A LEU 401  ? A LEU 401  
402  1 Y 1 A MET 402  ? A MET 402  
403  1 Y 1 A HIS 403  ? A HIS 403  
404  1 Y 1 A VAL 404  ? A VAL 404  
405  1 Y 1 A ALA 405  ? A ALA 405  
406  1 Y 1 A TYR 406  ? A TYR 406  
407  1 Y 1 A GLU 407  ? A GLU 407  
408  1 Y 1 A GLU 408  ? A GLU 408  
409  1 Y 1 A PHE 409  ? A PHE 409  
410  1 Y 1 A GLU 410  ? A GLU 410  
411  1 Y 1 A LYS 411  ? A LYS 411  
412  1 Y 1 A VAL 412  ? A VAL 412  
413  1 Y 1 A MET 413  ? A MET 413  
414  1 Y 1 A VAL 414  ? A VAL 414  
415  1 Y 1 A ALA 415  ? A ALA 415  
416  1 Y 1 A CYS 416  ? A CYS 416  
417  1 Y 1 A PHE 417  ? A PHE 417  
418  1 Y 1 A GLU 418  ? A GLU 418  
419  1 Y 1 A VAL 419  ? A VAL 419  
420  1 Y 1 A PHE 420  ? A PHE 420  
421  1 Y 1 A GLN 421  ? A GLN 421  
422  1 Y 1 A THR 422  ? A THR 422  
423  1 Y 1 A TRP 423  ? A TRP 423  
424  1 Y 1 A ASP 424  ? A ASP 424  
425  1 Y 1 A ASP 425  ? A ASP 425  
426  1 Y 1 A GLU 426  ? A GLU 426  
427  1 Y 1 A TYR 427  ? A TYR 427  
428  1 Y 1 A GLU 428  ? A GLU 428  
429  1 Y 1 A LYS 429  ? A LYS 429  
430  1 Y 1 A LEU 430  ? A LEU 430  
431  1 Y 1 A GLN 431  ? A GLN 431  
432  1 Y 1 A VAL 432  ? A VAL 432  
433  1 Y 1 A LEU 433  ? A LEU 433  
434  1 Y 1 A LEU 434  ? A LEU 434  
435  1 Y 1 A ARG 435  ? A ARG 435  
436  1 Y 1 A ASP 436  ? A ASP 436  
437  1 Y 1 A ILE 437  ? A ILE 437  
438  1 Y 1 A VAL 438  ? A VAL 438  
439  1 Y 1 A LYS 439  ? A LYS 439  
440  1 Y 1 A ARG 440  ? A ARG 440  
441  1 Y 1 A LYS 441  ? A LYS 441  
442  1 Y 1 A ARG 442  ? A ARG 442  
443  1 Y 1 A GLU 443  ? A GLU 443  
444  1 Y 1 A GLU 444  ? A GLU 444  
445  1 Y 1 A ASN 445  ? A ASN 445  
446  1 Y 1 A LEU 446  ? A LEU 446  
447  1 Y 1 A LYS 447  ? A LYS 447  
448  1 Y 1 A MET 448  ? A MET 448  
449  1 Y 1 A VAL 449  ? A VAL 449  
450  1 Y 1 A TRP 450  ? A TRP 450  
451  1 Y 1 A ARG 451  ? A ARG 451  
452  1 Y 1 A ILE 452  ? A ILE 452  
453  1 Y 1 A ASN 453  ? A ASN 453  
454  1 Y 1 A PRO 454  ? A PRO 454  
455  1 Y 1 A ALA 455  ? A ALA 455  
456  1 Y 1 A HIS 456  ? A HIS 456  
457  1 Y 1 A ARG 457  ? A ARG 457  
458  1 Y 1 A LYS 458  ? A LYS 458  
459  1 Y 1 A LEU 459  ? A LEU 459  
460  1 Y 1 A GLN 460  ? A GLN 460  
461  1 Y 1 A ALA 461  ? A ALA 461  
462  1 Y 1 A ARG 462  ? A ARG 462  
463  1 Y 1 A LEU 463  ? A LEU 463  
464  1 Y 1 A ASP 464  ? A ASP 464  
465  1 Y 1 A GLN 465  ? A GLN 465  
466  1 Y 1 A MET 466  ? A MET 466  
467  1 Y 1 A ARG 467  ? A ARG 467  
468  1 Y 1 A LYS 468  ? A LYS 468  
469  1 Y 1 A PHE 469  ? A PHE 469  
470  1 Y 1 A ARG 470  ? A ARG 470  
471  1 Y 1 A ARG 471  ? A ARG 471  
472  1 Y 1 A GLN 472  ? A GLN 472  
473  1 Y 1 A HIS 473  ? A HIS 473  
474  1 Y 1 A GLU 474  ? A GLU 474  
475  1 Y 1 A GLN 475  ? A GLN 475  
476  1 Y 1 A LEU 476  ? A LEU 476  
477  1 Y 1 A ARG 477  ? A ARG 477  
478  1 Y 1 A ALA 478  ? A ALA 478  
479  1 Y 1 A VAL 479  ? A VAL 479  
480  1 Y 1 A ILE 480  ? A ILE 480  
481  1 Y 1 A VAL 481  ? A VAL 481  
482  1 Y 1 A ARG 482  ? A ARG 482  
483  1 Y 1 A VAL 483  ? A VAL 483  
484  1 Y 1 A LEU 484  ? A LEU 484  
485  1 Y 1 A ARG 485  ? A ARG 485  
486  1 Y 1 A PRO 486  ? A PRO 486  
487  1 Y 1 A GLN 487  ? A GLN 487  
488  1 Y 1 A VAL 488  ? A VAL 488  
489  1 Y 1 A THR 489  ? A THR 489  
490  1 Y 1 A ALA 490  ? A ALA 490  
491  1 Y 1 A VAL 491  ? A VAL 491  
492  1 Y 1 A ALA 492  ? A ALA 492  
493  1 Y 1 A GLN 493  ? A GLN 493  
494  1 Y 1 A GLN 494  ? A GLN 494  
495  1 Y 1 A ASN 495  ? A ASN 495  
496  1 Y 1 A GLN 496  ? A GLN 496  
497  1 Y 1 A GLY 497  ? A GLY 497  
498  1 Y 1 A GLU 498  ? A GLU 498  
499  1 Y 1 A VAL 499  ? A VAL 499  
500  1 Y 1 A PRO 500  ? A PRO 500  
501  1 Y 1 A GLU 501  ? A GLU 501  
502  1 Y 1 A PRO 502  ? A PRO 502  
503  1 Y 1 A GLN 503  ? A GLN 503  
504  1 Y 1 A ASP 504  ? A ASP 504  
505  1 Y 1 A MET 505  ? A MET 505  
506  1 Y 1 A LYS 506  ? A LYS 506  
507  1 Y 1 A VAL 507  ? A VAL 507  
508  1 Y 1 A ALA 508  ? A ALA 508  
509  1 Y 1 A GLU 509  ? A GLU 509  
510  1 Y 1 A VAL 510  ? A VAL 510  
511  1 Y 1 A LEU 511  ? A LEU 511  
512  1 Y 1 A PHE 512  ? A PHE 512  
513  1 Y 1 A ASP 513  ? A ASP 513  
514  1 Y 1 A ALA 514  ? A ALA 514  
515  1 Y 1 A ALA 515  ? A ALA 515  
516  1 Y 1 A ASP 516  ? A ASP 516  
517  1 Y 1 A ALA 517  ? A ALA 517  
518  1 Y 1 A ASN 518  ? A ASN 518  
519  1 Y 1 A ALA 519  ? A ALA 519  
520  1 Y 1 A ILE 520  ? A ILE 520  
521  1 Y 1 A GLU 521  ? A GLU 521  
522  1 Y 1 A GLU 522  ? A GLU 522  
523  1 Y 1 A VAL 523  ? A VAL 523  
524  1 Y 1 A ASN 524  ? A ASN 524  
525  1 Y 1 A LEU 525  ? A LEU 525  
526  1 Y 1 A ALA 526  ? A ALA 526  
527  1 Y 1 A TYR 527  ? A TYR 527  
528  1 Y 1 A GLU 528  ? A GLU 528  
529  1 Y 1 A ASN 529  ? A ASN 529  
530  1 Y 1 A VAL 530  ? A VAL 530  
531  1 Y 1 A LYS 531  ? A LYS 531  
532  1 Y 1 A GLU 532  ? A GLU 532  
533  1 Y 1 A VAL 533  ? A VAL 533  
534  1 Y 1 A ASP 534  ? A ASP 534  
535  1 Y 1 A GLY 535  ? A GLY 535  
536  1 Y 1 A LEU 536  ? A LEU 536  
537  1 Y 1 A ASP 537  ? A ASP 537  
538  1 Y 1 A VAL 538  ? A VAL 538  
539  1 Y 1 A SER 539  ? A SER 539  
540  1 Y 1 A LYS 540  ? A LYS 540  
541  1 Y 1 A GLU 541  ? A GLU 541  
542  1 Y 1 A GLY 542  ? A GLY 542  
543  1 Y 1 A THR 543  ? A THR 543  
544  1 Y 1 A GLU 544  ? A GLU 544  
545  1 Y 1 A ALA 545  ? A ALA 545  
546  1 Y 1 A TRP 546  ? A TRP 546  
547  1 Y 1 A GLU 547  ? A GLU 547  
548  1 Y 1 A ALA 548  ? A ALA 548  
549  1 Y 1 A ALA 549  ? A ALA 549  
550  1 Y 1 A MET 550  ? A MET 550  
551  1 Y 1 A LYS 551  ? A LYS 551  
552  1 Y 1 A ARG 552  ? A ARG 552  
553  1 Y 1 A TYR 553  ? A TYR 553  
554  1 Y 1 A ASP 554  ? A ASP 554  
555  1 Y 1 A GLU 555  ? A GLU 555  
556  1 Y 1 A ARG 556  ? A ARG 556  
557  1 Y 1 A ILE 557  ? A ILE 557  
558  1 Y 1 A ASP 558  ? A ASP 558  
559  1 Y 1 A ARG 559  ? A ARG 559  
560  1 Y 1 A VAL 560  ? A VAL 560  
561  1 Y 1 A GLU 561  ? A GLU 561  
562  1 Y 1 A THR 562  ? A THR 562  
563  1 Y 1 A ARG 563  ? A ARG 563  
564  1 Y 1 A ILE 564  ? A ILE 564  
565  1 Y 1 A THR 565  ? A THR 565  
566  1 Y 1 A ALA 566  ? A ALA 566  
567  1 Y 1 A ARG 567  ? A ARG 567  
568  1 Y 1 A LEU 568  ? A LEU 568  
569  1 Y 1 A ARG 569  ? A ARG 569  
570  1 Y 1 A ASP 570  ? A ASP 570  
571  1 Y 1 A GLN 571  ? A GLN 571  
572  1 Y 1 A LEU 572  ? A LEU 572  
573  1 Y 1 A GLY 573  ? A GLY 573  
574  1 Y 1 A THR 574  ? A THR 574  
575  1 Y 1 A ALA 575  ? A ALA 575  
576  1 Y 1 A LYS 576  ? A LYS 576  
577  1 Y 1 A ASN 577  ? A ASN 577  
578  1 Y 1 A ALA 578  ? A ALA 578  
579  1 Y 1 A ASN 579  ? A ASN 579  
580  1 Y 1 A GLU 580  ? A GLU 580  
581  1 Y 1 A MET 581  ? A MET 581  
582  1 Y 1 A PHE 582  ? A PHE 582  
583  1 Y 1 A ARG 583  ? A ARG 583  
584  1 Y 1 A ILE 584  ? A ILE 584  
585  1 Y 1 A PHE 585  ? A PHE 585  
586  1 Y 1 A SER 586  ? A SER 586  
587  1 Y 1 A ARG 587  ? A ARG 587  
588  1 Y 1 A PHE 588  ? A PHE 588  
589  1 Y 1 A ASN 589  ? A ASN 589  
590  1 Y 1 A ALA 590  ? A ALA 590  
591  1 Y 1 A LEU 591  ? A LEU 591  
592  1 Y 1 A PHE 592  ? A PHE 592  
593  1 Y 1 A VAL 593  ? A VAL 593  
594  1 Y 1 A ARG 594  ? A ARG 594  
595  1 Y 1 A PRO 595  ? A PRO 595  
596  1 Y 1 A HIS 596  ? A HIS 596  
597  1 Y 1 A ILE 597  ? A ILE 597  
598  1 Y 1 A ARG 598  ? A ARG 598  
599  1 Y 1 A GLY 599  ? A GLY 599  
600  1 Y 1 A ALA 600  ? A ALA 600  
601  1 Y 1 A ILE 601  ? A ILE 601  
602  1 Y 1 A ARG 602  ? A ARG 602  
603  1 Y 1 A GLU 603  ? A GLU 603  
604  1 Y 1 A TYR 604  ? A TYR 604  
605  1 Y 1 A GLN 605  ? A GLN 605  
606  1 Y 1 A THR 606  ? A THR 606  
607  1 Y 1 A GLN 607  ? A GLN 607  
608  1 Y 1 A LEU 608  ? A LEU 608  
609  1 Y 1 A ILE 609  ? A ILE 609  
610  1 Y 1 A GLN 610  ? A GLN 610  
611  1 Y 1 A ARG 611  ? A ARG 611  
612  1 Y 1 A VAL 612  ? A VAL 612  
613  1 Y 1 A LYS 613  ? A LYS 613  
614  1 Y 1 A ASP 614  ? A ASP 614  
615  1 Y 1 A ASP 615  ? A ASP 615  
616  1 Y 1 A ILE 616  ? A ILE 616  
617  1 Y 1 A GLU 617  ? A GLU 617  
618  1 Y 1 A SER 618  ? A SER 618  
619  1 Y 1 A LEU 619  ? A LEU 619  
620  1 Y 1 A HIS 620  ? A HIS 620  
621  1 Y 1 A ASP 621  ? A ASP 621  
622  1 Y 1 A LYS 622  ? A LYS 622  
623  1 Y 1 A PHE 623  ? A PHE 623  
624  1 Y 1 A LYS 624  ? A LYS 624  
625  1 Y 1 A VAL 625  ? A VAL 625  
626  1 Y 1 A GLN 626  ? A GLN 626  
627  1 Y 1 A TYR 627  ? A TYR 627  
628  1 Y 1 A PRO 628  ? A PRO 628  
629  1 Y 1 A GLN 629  ? A GLN 629  
630  1 Y 1 A SER 630  ? A SER 630  
631  1 Y 1 A GLN 631  ? A GLN 631  
632  1 Y 1 A ALA 632  ? A ALA 632  
633  1 Y 1 A CYS 633  ? A CYS 633  
634  1 Y 1 A LYS 634  ? A LYS 634  
635  1 Y 1 A MET 635  ? A MET 635  
636  1 Y 1 A SER 636  ? A SER 636  
637  1 Y 1 A HIS 637  ? A HIS 637  
638  1 Y 1 A VAL 638  ? A VAL 638  
639  1 Y 1 A ARG 639  ? A ARG 639  
640  1 Y 1 A ASP 640  ? A ASP 640  
641  1 Y 1 A LEU 641  ? A LEU 641  
642  1 Y 1 A PRO 642  ? A PRO 642  
643  1 Y 1 A PRO 643  ? A PRO 643  
644  1 Y 1 A VAL 644  ? A VAL 644  
645  1 Y 1 A SER 645  ? A SER 645  
646  1 Y 1 A GLY 646  ? A GLY 646  
647  1 Y 1 A SER 647  ? A SER 647  
648  1 Y 1 A ILE 648  ? A ILE 648  
649  1 Y 1 A ILE 649  ? A ILE 649  
650  1 Y 1 A TRP 650  ? A TRP 650  
651  1 Y 1 A ALA 651  ? A ALA 651  
652  1 Y 1 A LYS 652  ? A LYS 652  
653  1 Y 1 A GLN 653  ? A GLN 653  
654  1 Y 1 A ILE 654  ? A ILE 654  
655  1 Y 1 A ASP 655  ? A ASP 655  
656  1 Y 1 A ARG 656  ? A ARG 656  
657  1 Y 1 A GLN 657  ? A GLN 657  
658  1 Y 1 A LEU 658  ? A LEU 658  
659  1 Y 1 A THR 659  ? A THR 659  
660  1 Y 1 A ALA 660  ? A ALA 660  
661  1 Y 1 A TYR 661  ? A TYR 661  
662  1 Y 1 A MET 662  ? A MET 662  
663  1 Y 1 A LYS 663  ? A LYS 663  
664  1 Y 1 A ARG 664  ? A ARG 664  
665  1 Y 1 A VAL 665  ? A VAL 665  
666  1 Y 1 A GLU 666  ? A GLU 666  
667  1 Y 1 A ASP 667  ? A ASP 667  
668  1 Y 1 A VAL 668  ? A VAL 668  
669  1 Y 1 A LEU 669  ? A LEU 669  
670  1 Y 1 A GLY 670  ? A GLY 670  
671  1 Y 1 A LYS 671  ? A LYS 671  
672  1 Y 1 A GLY 672  ? A GLY 672  
673  1 Y 1 A TRP 673  ? A TRP 673  
674  1 Y 1 A GLU 674  ? A GLU 674  
675  1 Y 1 A ASN 675  ? A ASN 675  
676  1 Y 1 A HIS 676  ? A HIS 676  
677  1 Y 1 A VAL 677  ? A VAL 677  
678  1 Y 1 A GLU 678  ? A GLU 678  
679  1 Y 1 A GLY 679  ? A GLY 679  
680  1 Y 1 A GLN 680  ? A GLN 680  
681  1 Y 1 A LYS 681  ? A LYS 681  
682  1 Y 1 A LEU 682  ? A LEU 682  
683  1 Y 1 A LYS 683  ? A LYS 683  
684  1 Y 1 A GLN 684  ? A GLN 684  
685  1 Y 1 A ASP 685  ? A ASP 685  
686  1 Y 1 A GLY 686  ? A GLY 686  
687  1 Y 1 A ASP 687  ? A ASP 687  
688  1 Y 1 A SER 688  ? A SER 688  
689  1 Y 1 A PHE 689  ? A PHE 689  
690  1 Y 1 A ARG 690  ? A ARG 690  
691  1 Y 1 A MET 691  ? A MET 691  
692  1 Y 1 A LYS 692  ? A LYS 692  
693  1 Y 1 A LEU 693  ? A LEU 693  
694  1 Y 1 A ASN 694  ? A ASN 694  
695  1 Y 1 A THR 695  ? A THR 695  
696  1 Y 1 A GLN 696  ? A GLN 696  
697  1 Y 1 A GLU 697  ? A GLU 697  
698  1 Y 1 A ILE 698  ? A ILE 698  
699  1 Y 1 A PHE 699  ? A PHE 699  
700  1 Y 1 A ASP 700  ? A ASP 700  
701  1 Y 1 A ASP 701  ? A ASP 701  
702  1 Y 1 A TRP 702  ? A TRP 702  
703  1 Y 1 A ALA 703  ? A ALA 703  
704  1 Y 1 A ARG 704  ? A ARG 704  
705  1 Y 1 A LYS 705  ? A LYS 705  
706  1 Y 1 A VAL 706  ? A VAL 706  
707  1 Y 1 A GLN 707  ? A GLN 707  
708  1 Y 1 A GLN 708  ? A GLN 708  
709  1 Y 1 A ARG 709  ? A ARG 709  
710  1 Y 1 A ASN 710  ? A ASN 710  
711  1 Y 1 A LEU 711  ? A LEU 711  
712  1 Y 1 A GLY 712  ? A GLY 712  
713  1 Y 1 A VAL 713  ? A VAL 713  
714  1 Y 1 A SER 714  ? A SER 714  
715  1 Y 1 A GLY 715  ? A GLY 715  
716  1 Y 1 A ARG 716  ? A ARG 716  
717  1 Y 1 A ILE 717  ? A ILE 717  
718  1 Y 1 A PHE 718  ? A PHE 718  
719  1 Y 1 A THR 719  ? A THR 719  
720  1 Y 1 A ILE 720  ? A ILE 720  
721  1 Y 1 A GLU 721  ? A GLU 721  
722  1 Y 1 A SER 722  ? A SER 722  
723  1 Y 1 A THR 723  ? A THR 723  
724  1 Y 1 A ARG 724  ? A ARG 724  
725  1 Y 1 A VAL 725  ? A VAL 725  
726  1 Y 1 A ARG 726  ? A ARG 726  
727  1 Y 1 A GLY 727  ? A GLY 727  
728  1 Y 1 A ARG 728  ? A ARG 728  
729  1 Y 1 A THR 729  ? A THR 729  
730  1 Y 1 A GLY 730  ? A GLY 730  
731  1 Y 1 A ASN 731  ? A ASN 731  
732  1 Y 1 A VAL 732  ? A VAL 732  
733  1 Y 1 A LEU 733  ? A LEU 733  
734  1 Y 1 A LYS 734  ? A LYS 734  
735  1 Y 1 A LEU 735  ? A LEU 735  
736  1 Y 1 A LYS 736  ? A LYS 736  
737  1 Y 1 A VAL 737  ? A VAL 737  
738  1 Y 1 A ASN 738  ? A ASN 738  
739  1 Y 1 A PHE 739  ? A PHE 739  
740  1 Y 1 A LEU 740  ? A LEU 740  
741  1 Y 1 A PRO 741  ? A PRO 741  
742  1 Y 1 A GLU 742  ? A GLU 742  
743  1 Y 1 A ILE 743  ? A ILE 743  
744  1 Y 1 A ILE 744  ? A ILE 744  
745  1 Y 1 A THR 745  ? A THR 745  
746  1 Y 1 A LEU 746  ? A LEU 746  
747  1 Y 1 A SER 747  ? A SER 747  
748  1 Y 1 A LYS 748  ? A LYS 748  
749  1 Y 1 A GLU 749  ? A GLU 749  
750  1 Y 1 A VAL 750  ? A VAL 750  
751  1 Y 1 A ARG 751  ? A ARG 751  
752  1 Y 1 A ASN 752  ? A ASN 752  
753  1 Y 1 A LEU 753  ? A LEU 753  
754  1 Y 1 A LYS 754  ? A LYS 754  
755  1 Y 1 A TRP 755  ? A TRP 755  
756  1 Y 1 A LEU 756  ? A LEU 756  
757  1 Y 1 A GLY 757  ? A GLY 757  
758  1 Y 1 A PHE 758  ? A PHE 758  
759  1 Y 1 A ARG 759  ? A ARG 759  
760  1 Y 1 A VAL 760  ? A VAL 760  
761  1 Y 1 A PRO 761  ? A PRO 761  
762  1 Y 1 A LEU 762  ? A LEU 762  
763  1 Y 1 A ALA 763  ? A ALA 763  
764  1 Y 1 A ILE 764  ? A ILE 764  
765  1 Y 1 A VAL 765  ? A VAL 765  
766  1 Y 1 A ASN 766  ? A ASN 766  
767  1 Y 1 A LYS 767  ? A LYS 767  
768  1 Y 1 A ALA 768  ? A ALA 768  
769  1 Y 1 A HIS 769  ? A HIS 769  
770  1 Y 1 A GLN 770  ? A GLN 770  
771  1 Y 1 A ALA 771  ? A ALA 771  
772  1 Y 1 A ASN 772  ? A ASN 772  
773  1 Y 1 A GLN 773  ? A GLN 773  
774  1 Y 1 A LEU 774  ? A LEU 774  
775  1 Y 1 A TYR 775  ? A TYR 775  
776  1 Y 1 A PRO 776  ? A PRO 776  
777  1 Y 1 A PHE 777  ? A PHE 777  
778  1 Y 1 A ALA 778  ? A ALA 778  
779  1 Y 1 A ILE 779  ? A ILE 779  
780  1 Y 1 A SER 780  ? A SER 780  
781  1 Y 1 A LEU 781  ? A LEU 781  
782  1 Y 1 A ILE 782  ? A ILE 782  
783  1 Y 1 A GLU 783  ? A GLU 783  
784  1 Y 1 A SER 784  ? A SER 784  
785  1 Y 1 A VAL 785  ? A VAL 785  
786  1 Y 1 A ARG 786  ? A ARG 786  
787  1 Y 1 A THR 787  ? A THR 787  
788  1 Y 1 A TYR 788  ? A TYR 788  
789  1 Y 1 A GLU 789  ? A GLU 789  
790  1 Y 1 A ARG 790  ? A ARG 790  
791  1 Y 1 A THR 791  ? A THR 791  
792  1 Y 1 A CYS 792  ? A CYS 792  
793  1 Y 1 A GLU 793  ? A GLU 793  
794  1 Y 1 A LYS 794  ? A LYS 794  
795  1 Y 1 A VAL 795  ? A VAL 795  
796  1 Y 1 A GLU 796  ? A GLU 796  
797  1 Y 1 A GLU 797  ? A GLU 797  
798  1 Y 1 A ARG 798  ? A ARG 798  
799  1 Y 1 A ASN 799  ? A ASN 799  
800  1 Y 1 A THR 800  ? A THR 800  
801  1 Y 1 A ILE 801  ? A ILE 801  
802  1 Y 1 A SER 802  ? A SER 802  
803  1 Y 1 A LEU 803  ? A LEU 803  
804  1 Y 1 A LEU 804  ? A LEU 804  
805  1 Y 1 A VAL 805  ? A VAL 805  
806  1 Y 1 A ALA 806  ? A ALA 806  
807  1 Y 1 A GLY 807  ? A GLY 807  
808  1 Y 1 A LEU 808  ? A LEU 808  
809  1 Y 1 A LYS 809  ? A LYS 809  
810  1 Y 1 A LYS 810  ? A LYS 810  
811  1 Y 1 A GLU 811  ? A GLU 811  
812  1 Y 1 A VAL 812  ? A VAL 812  
813  1 Y 1 A GLN 813  ? A GLN 813  
814  1 Y 1 A ALA 814  ? A ALA 814  
815  1 Y 1 A LEU 815  ? A LEU 815  
816  1 Y 1 A ILE 816  ? A ILE 816  
817  1 Y 1 A ALA 817  ? A ALA 817  
818  1 Y 1 A GLU 818  ? A GLU 818  
819  1 Y 1 A GLY 819  ? A GLY 819  
820  1 Y 1 A ILE 820  ? A ILE 820  
821  1 Y 1 A ALA 821  ? A ALA 821  
822  1 Y 1 A LEU 822  ? A LEU 822  
823  1 Y 1 A VAL 823  ? A VAL 823  
824  1 Y 1 A TRP 824  ? A TRP 824  
825  1 Y 1 A GLU 825  ? A GLU 825  
826  1 Y 1 A SER 826  ? A SER 826  
827  1 Y 1 A TYR 827  ? A TYR 827  
828  1 Y 1 A LYS 828  ? A LYS 828  
829  1 Y 1 A LEU 829  ? A LEU 829  
830  1 Y 1 A ASP 830  ? A ASP 830  
831  1 Y 1 A PRO 831  ? A PRO 831  
832  1 Y 1 A TYR 832  ? A TYR 832  
833  1 Y 1 A VAL 833  ? A VAL 833  
834  1 Y 1 A GLN 834  ? A GLN 834  
835  1 Y 1 A ARG 835  ? A ARG 835  
836  1 Y 1 A LEU 836  ? A LEU 836  
837  1 Y 1 A ALA 837  ? A ALA 837  
838  1 Y 1 A GLU 838  ? A GLU 838  
839  1 Y 1 A THR 839  ? A THR 839  
840  1 Y 1 A VAL 840  ? A VAL 840  
841  1 Y 1 A PHE 841  ? A PHE 841  
842  1 Y 1 A ASN 842  ? A ASN 842  
843  1 Y 1 A PHE 843  ? A PHE 843  
844  1 Y 1 A GLN 844  ? A GLN 844  
845  1 Y 1 A GLU 845  ? A GLU 845  
846  1 Y 1 A LYS 846  ? A LYS 846  
847  1 Y 1 A VAL 847  ? A VAL 847  
848  1 Y 1 A ASP 848  ? A ASP 848  
849  1 Y 1 A ASP 849  ? A ASP 849  
850  1 Y 1 A LEU 850  ? A LEU 850  
851  1 Y 1 A LEU 851  ? A LEU 851  
852  1 Y 1 A ILE 852  ? A ILE 852  
853  1 Y 1 A ILE 853  ? A ILE 853  
854  1 Y 1 A GLU 854  ? A GLU 854  
855  1 Y 1 A GLU 855  ? A GLU 855  
856  1 Y 1 A LYS 856  ? A LYS 856  
857  1 Y 1 A ILE 857  ? A ILE 857  
858  1 Y 1 A ASP 858  ? A ASP 858  
859  1 Y 1 A LEU 859  ? A LEU 859  
860  1 Y 1 A GLU 860  ? A GLU 860  
861  1 Y 1 A VAL 861  ? A VAL 861  
862  1 Y 1 A ARG 862  ? A ARG 862  
863  1 Y 1 A SER 863  ? A SER 863  
864  1 Y 1 A LEU 864  ? A LEU 864  
865  1 Y 1 A GLU 865  ? A GLU 865  
866  1 Y 1 A THR 866  ? A THR 866  
867  1 Y 1 A CYS 867  ? A CYS 867  
868  1 Y 1 A MET 868  ? A MET 868  
869  1 Y 1 A TYR 869  ? A TYR 869  
870  1 Y 1 A ASP 870  ? A ASP 870  
871  1 Y 1 A HIS 871  ? A HIS 871  
872  1 Y 1 A LYS 872  ? A LYS 872  
873  1 Y 1 A THR 873  ? A THR 873  
874  1 Y 1 A PHE 874  ? A PHE 874  
875  1 Y 1 A SER 875  ? A SER 875  
876  1 Y 1 A GLU 876  ? A GLU 876  
877  1 Y 1 A ILE 877  ? A ILE 877  
878  1 Y 1 A LEU 878  ? A LEU 878  
879  1 Y 1 A ASN 879  ? A ASN 879  
880  1 Y 1 A ARG 880  ? A ARG 880  
881  1 Y 1 A VAL 881  ? A VAL 881  
882  1 Y 1 A GLN 882  ? A GLN 882  
883  1 Y 1 A LYS 883  ? A LYS 883  
884  1 Y 1 A ALA 884  ? A ALA 884  
885  1 Y 1 A VAL 885  ? A VAL 885  
886  1 Y 1 A ASP 886  ? A ASP 886  
887  1 Y 1 A ASP 887  ? A ASP 887  
888  1 Y 1 A LEU 888  ? A LEU 888  
889  1 Y 1 A ASN 889  ? A ASN 889  
890  1 Y 1 A LEU 890  ? A LEU 890  
891  1 Y 1 A HIS 891  ? A HIS 891  
892  1 Y 1 A SER 892  ? A SER 892  
893  1 Y 1 A TYR 893  ? A TYR 893  
894  1 Y 1 A SER 894  ? A SER 894  
895  1 Y 1 A ASN 895  ? A ASN 895  
896  1 Y 1 A LEU 896  ? A LEU 896  
897  1 Y 1 A PRO 897  ? A PRO 897  
898  1 Y 1 A ILE 898  ? A ILE 898  
899  1 Y 1 A TRP 899  ? A TRP 899  
900  1 Y 1 A VAL 900  ? A VAL 900  
901  1 Y 1 A ASN 901  ? A ASN 901  
902  1 Y 1 A LYS 902  ? A LYS 902  
903  1 Y 1 A LEU 903  ? A LEU 903  
904  1 Y 1 A ASP 904  ? A ASP 904  
905  1 Y 1 A MET 905  ? A MET 905  
906  1 Y 1 A GLU 906  ? A GLU 906  
907  1 Y 1 A ILE 907  ? A ILE 907  
908  1 Y 1 A GLU 908  ? A GLU 908  
909  1 Y 1 A ARG 909  ? A ARG 909  
910  1 Y 1 A ILE 910  ? A ILE 910  
911  1 Y 1 A LEU 911  ? A LEU 911  
912  1 Y 1 A GLY 912  ? A GLY 912  
913  1 Y 1 A VAL 913  ? A VAL 913  
914  1 Y 1 A ARG 914  ? A ARG 914  
915  1 Y 1 A LEU 915  ? A LEU 915  
916  1 Y 1 A GLN 916  ? A GLN 916  
917  1 Y 1 A ALA 917  ? A ALA 917  
918  1 Y 1 A GLY 918  ? A GLY 918  
919  1 Y 1 A LEU 919  ? A LEU 919  
920  1 Y 1 A ARG 920  ? A ARG 920  
921  1 Y 1 A ALA 921  ? A ALA 921  
922  1 Y 1 A TRP 922  ? A TRP 922  
923  1 Y 1 A THR 923  ? A THR 923  
924  1 Y 1 A GLN 924  ? A GLN 924  
925  1 Y 1 A VAL 925  ? A VAL 925  
926  1 Y 1 A LEU 926  ? A LEU 926  
927  1 Y 1 A LEU 927  ? A LEU 927  
928  1 Y 1 A GLY 928  ? A GLY 928  
929  1 Y 1 A GLN 929  ? A GLN 929  
930  1 Y 1 A ALA 930  ? A ALA 930  
931  1 Y 1 A GLU 931  ? A GLU 931  
932  1 Y 1 A ASP 932  ? A ASP 932  
933  1 Y 1 A LYS 933  ? A LYS 933  
934  1 Y 1 A ALA 934  ? A ALA 934  
935  1 Y 1 A GLU 935  ? A GLU 935  
936  1 Y 1 A VAL 936  ? A VAL 936  
937  1 Y 1 A ASP 937  ? A ASP 937  
938  1 Y 1 A MET 938  ? A MET 938  
939  1 Y 1 A ASP 939  ? A ASP 939  
940  1 Y 1 A THR 940  ? A THR 940  
941  1 Y 1 A ASP 941  ? A ASP 941  
942  1 Y 1 A ALA 942  ? A ALA 942  
943  1 Y 1 A PRO 943  ? A PRO 943  
944  1 Y 1 A GLN 944  ? A GLN 944  
945  1 Y 1 A VAL 945  ? A VAL 945  
946  1 Y 1 A SER 946  ? A SER 946  
947  1 Y 1 A HIS 947  ? A HIS 947  
948  1 Y 1 A LYS 948  ? A LYS 948  
949  1 Y 1 A PRO 949  ? A PRO 949  
950  1 Y 1 A GLY 950  ? A GLY 950  
951  1 Y 1 A GLY 951  ? A GLY 951  
952  1 Y 1 A GLU 952  ? A GLU 952  
953  1 Y 1 A PRO 953  ? A PRO 953  
954  1 Y 1 A LYS 954  ? A LYS 954  
955  1 Y 1 A ILE 955  ? A ILE 955  
956  1 Y 1 A LYS 956  ? A LYS 956  
957  1 Y 1 A ASN 957  ? A ASN 957  
958  1 Y 1 A VAL 958  ? A VAL 958  
959  1 Y 1 A VAL 959  ? A VAL 959  
960  1 Y 1 A HIS 960  ? A HIS 960  
961  1 Y 1 A GLU 961  ? A GLU 961  
962  1 Y 1 A LEU 962  ? A LEU 962  
963  1 Y 1 A ARG 963  ? A ARG 963  
964  1 Y 1 A ILE 964  ? A ILE 964  
965  1 Y 1 A THR 965  ? A THR 965  
966  1 Y 1 A ASN 966  ? A ASN 966  
967  1 Y 1 A GLN 967  ? A GLN 967  
968  1 Y 1 A VAL 968  ? A VAL 968  
969  1 Y 1 A ILE 969  ? A ILE 969  
970  1 Y 1 A TYR 970  ? A TYR 970  
971  1 Y 1 A LEU 971  ? A LEU 971  
972  1 Y 1 A ASN 972  ? A ASN 972  
973  1 Y 1 A PRO 973  ? A PRO 973  
974  1 Y 1 A PRO 974  ? A PRO 974  
975  1 Y 1 A ILE 975  ? A ILE 975  
976  1 Y 1 A GLU 976  ? A GLU 976  
977  1 Y 1 A GLU 977  ? A GLU 977  
978  1 Y 1 A CYS 978  ? A CYS 978  
979  1 Y 1 A ARG 979  ? A ARG 979  
980  1 Y 1 A TYR 980  ? A TYR 980  
981  1 Y 1 A LYS 981  ? A LYS 981  
982  1 Y 1 A LEU 982  ? A LEU 982  
983  1 Y 1 A TYR 983  ? A TYR 983  
984  1 Y 1 A GLN 984  ? A GLN 984  
985  1 Y 1 A GLU 985  ? A GLU 985  
986  1 Y 1 A MET 986  ? A MET 986  
987  1 Y 1 A PHE 987  ? A PHE 987  
988  1 Y 1 A ALA 988  ? A ALA 988  
989  1 Y 1 A TRP 989  ? A TRP 989  
990  1 Y 1 A LYS 990  ? A LYS 990  
991  1 Y 1 A MET 991  ? A MET 991  
992  1 Y 1 A VAL 992  ? A VAL 992  
993  1 Y 1 A VAL 993  ? A VAL 993  
994  1 Y 1 A LEU 994  ? A LEU 994  
995  1 Y 1 A SER 995  ? A SER 995  
996  1 Y 1 A LEU 996  ? A LEU 996  
997  1 Y 1 A PRO 997  ? A PRO 997  
998  1 Y 1 A ARG 998  ? A ARG 998  
999  1 Y 1 A ILE 999  ? A ILE 999  
1000 1 Y 1 A GLN 1000 ? A GLN 1000 
1001 1 Y 1 A SER 1001 ? A SER 1001 
1002 1 Y 1 A GLN 1002 ? A GLN 1002 
1003 1 Y 1 A ARG 1003 ? A ARG 1003 
1004 1 Y 1 A TYR 1004 ? A TYR 1004 
1005 1 Y 1 A GLN 1005 ? A GLN 1005 
1006 1 Y 1 A VAL 1006 ? A VAL 1006 
1007 1 Y 1 A GLY 1007 ? A GLY 1007 
1008 1 Y 1 A VAL 1008 ? A VAL 1008 
1009 1 Y 1 A HIS 1009 ? A HIS 1009 
1010 1 Y 1 A TYR 1010 ? A TYR 1010 
1011 1 Y 1 A GLU 1011 ? A GLU 1011 
1012 1 Y 1 A LEU 1012 ? A LEU 1012 
1013 1 Y 1 A THR 1013 ? A THR 1013 
1014 1 Y 1 A GLU 1014 ? A GLU 1014 
1015 1 Y 1 A GLU 1015 ? A GLU 1015 
1016 1 Y 1 A GLU 1016 ? A GLU 1016 
1017 1 Y 1 A LYS 1017 ? A LYS 1017 
1018 1 Y 1 A PHE 1018 ? A PHE 1018 
1019 1 Y 1 A TYR 1019 ? A TYR 1019 
1020 1 Y 1 A ARG 1020 ? A ARG 1020 
1021 1 Y 1 A ASN 1021 ? A ASN 1021 
1022 1 Y 1 A ALA 1022 ? A ALA 1022 
1023 1 Y 1 A LEU 1023 ? A LEU 1023 
1024 1 Y 1 A THR 1024 ? A THR 1024 
1025 1 Y 1 A ARG 1025 ? A ARG 1025 
1026 1 Y 1 A MET 1026 ? A MET 1026 
1027 1 Y 1 A PRO 1027 ? A PRO 1027 
1028 1 Y 1 A ASP 1028 ? A ASP 1028 
1029 1 Y 1 A GLY 1029 ? A GLY 1029 
1030 1 Y 1 A PRO 1030 ? A PRO 1030 
1031 1 Y 1 A VAL 1031 ? A VAL 1031 
1032 1 Y 1 A ALA 1032 ? A ALA 1032 
1033 1 Y 1 A LEU 1033 ? A LEU 1033 
1034 1 Y 1 A GLU 1034 ? A GLU 1034 
1035 1 Y 1 A GLU 1035 ? A GLU 1035 
1036 1 Y 1 A SER 1036 ? A SER 1036 
1037 1 Y 1 A TYR 1037 ? A TYR 1037 
1038 1 Y 1 A SER 1038 ? A SER 1038 
1039 1 Y 1 A ALA 1039 ? A ALA 1039 
1040 1 Y 1 A VAL 1040 ? A VAL 1040 
1041 1 Y 1 A MET 1041 ? A MET 1041 
1042 1 Y 1 A GLY 1042 ? A GLY 1042 
1043 1 Y 1 A ILE 1043 ? A ILE 1043 
1044 1 Y 1 A VAL 1044 ? A VAL 1044 
1045 1 Y 1 A SER 1045 ? A SER 1045 
1046 1 Y 1 A GLU 1046 ? A GLU 1046 
1047 1 Y 1 A VAL 1047 ? A VAL 1047 
1048 1 Y 1 A GLU 1048 ? A GLU 1048 
1049 1 Y 1 A GLN 1049 ? A GLN 1049 
1050 1 Y 1 A TYR 1050 ? A TYR 1050 
1051 1 Y 1 A VAL 1051 ? A VAL 1051 
1052 1 Y 1 A LYS 1052 ? A LYS 1052 
1053 1 Y 1 A VAL 1053 ? A VAL 1053 
1054 1 Y 1 A TRP 1054 ? A TRP 1054 
1055 1 Y 1 A LEU 1055 ? A LEU 1055 
1056 1 Y 1 A GLN 1056 ? A GLN 1056 
1057 1 Y 1 A TYR 1057 ? A TYR 1057 
1058 1 Y 1 A GLN 1058 ? A GLN 1058 
1059 1 Y 1 A CYS 1059 ? A CYS 1059 
1060 1 Y 1 A LEU 1060 ? A LEU 1060 
1061 1 Y 1 A TRP 1061 ? A TRP 1061 
1062 1 Y 1 A ASP 1062 ? A ASP 1062 
1063 1 Y 1 A MET 1063 ? A MET 1063 
1064 1 Y 1 A GLN 1064 ? A GLN 1064 
1065 1 Y 1 A ALA 1065 ? A ALA 1065 
1066 1 Y 1 A GLU 1066 ? A GLU 1066 
1067 1 Y 1 A ASN 1067 ? A ASN 1067 
1068 1 Y 1 A ILE 1068 ? A ILE 1068 
1069 1 Y 1 A TYR 1069 ? A TYR 1069 
1070 1 Y 1 A ASN 1070 ? A ASN 1070 
1071 1 Y 1 A ARG 1071 ? A ARG 1071 
1072 1 Y 1 A LEU 1072 ? A LEU 1072 
1073 1 Y 1 A GLY 1073 ? A GLY 1073 
1074 1 Y 1 A GLU 1074 ? A GLU 1074 
1075 1 Y 1 A ASP 1075 ? A ASP 1075 
1076 1 Y 1 A LEU 1076 ? A LEU 1076 
1077 1 Y 1 A ASN 1077 ? A ASN 1077 
1078 1 Y 1 A LYS 1078 ? A LYS 1078 
1079 1 Y 1 A TRP 1079 ? A TRP 1079 
1080 1 Y 1 A GLN 1080 ? A GLN 1080 
1081 1 Y 1 A ALA 1081 ? A ALA 1081 
1082 1 Y 1 A LEU 1082 ? A LEU 1082 
1083 1 Y 1 A LEU 1083 ? A LEU 1083 
1084 1 Y 1 A VAL 1084 ? A VAL 1084 
1085 1 Y 1 A GLN 1085 ? A GLN 1085 
1086 1 Y 1 A ILE 1086 ? A ILE 1086 
1087 1 Y 1 A ARG 1087 ? A ARG 1087 
1088 1 Y 1 A LYS 1088 ? A LYS 1088 
1089 1 Y 1 A ALA 1089 ? A ALA 1089 
1090 1 Y 1 A ARG 1090 ? A ARG 1090 
1091 1 Y 1 A GLY 1091 ? A GLY 1091 
1092 1 Y 1 A THR 1092 ? A THR 1092 
1093 1 Y 1 A PHE 1093 ? A PHE 1093 
1094 1 Y 1 A ASP 1094 ? A ASP 1094 
1095 1 Y 1 A ASN 1095 ? A ASN 1095 
1096 1 Y 1 A ALA 1096 ? A ALA 1096 
1097 1 Y 1 A GLU 1097 ? A GLU 1097 
1098 1 Y 1 A THR 1098 ? A THR 1098 
1099 1 Y 1 A LYS 1099 ? A LYS 1099 
1100 1 Y 1 A LYS 1100 ? A LYS 1100 
1101 1 Y 1 A GLU 1101 ? A GLU 1101 
1102 1 Y 1 A PHE 1102 ? A PHE 1102 
1103 1 Y 1 A GLY 1103 ? A GLY 1103 
1104 1 Y 1 A PRO 1104 ? A PRO 1104 
1105 1 Y 1 A VAL 1105 ? A VAL 1105 
1106 1 Y 1 A VAL 1106 ? A VAL 1106 
1107 1 Y 1 A ILE 1107 ? A ILE 1107 
1108 1 Y 1 A ASP 1108 ? A ASP 1108 
1109 1 Y 1 A TYR 1109 ? A TYR 1109 
1110 1 Y 1 A GLY 1110 ? A GLY 1110 
1111 1 Y 1 A LYS 1111 ? A LYS 1111 
1112 1 Y 1 A VAL 1112 ? A VAL 1112 
1113 1 Y 1 A GLN 1113 ? A GLN 1113 
1114 1 Y 1 A SER 1114 ? A SER 1114 
1115 1 Y 1 A LYS 1115 ? A LYS 1115 
1116 1 Y 1 A VAL 1116 ? A VAL 1116 
1117 1 Y 1 A ASN 1117 ? A ASN 1117 
1118 1 Y 1 A LEU 1118 ? A LEU 1118 
1119 1 Y 1 A LYS 1119 ? A LYS 1119 
1120 1 Y 1 A TYR 1120 ? A TYR 1120 
1121 1 Y 1 A ASP 1121 ? A ASP 1121 
1122 1 Y 1 A SER 1122 ? A SER 1122 
1123 1 Y 1 A TRP 1123 ? A TRP 1123 
1124 1 Y 1 A HIS 1124 ? A HIS 1124 
1125 1 Y 1 A LYS 1125 ? A LYS 1125 
1126 1 Y 1 A GLU 1126 ? A GLU 1126 
1127 1 Y 1 A VAL 1127 ? A VAL 1127 
1128 1 Y 1 A LEU 1128 ? A LEU 1128 
1129 1 Y 1 A SER 1129 ? A SER 1129 
1130 1 Y 1 A LYS 1130 ? A LYS 1130 
1131 1 Y 1 A PHE 1131 ? A PHE 1131 
1132 1 Y 1 A GLY 1132 ? A GLY 1132 
1133 1 Y 1 A GLN 1133 ? A GLN 1133 
1134 1 Y 1 A MET 1134 ? A MET 1134 
1135 1 Y 1 A LEU 1135 ? A LEU 1135 
1136 1 Y 1 A GLY 1136 ? A GLY 1136 
1137 1 Y 1 A SER 1137 ? A SER 1137 
1138 1 Y 1 A ASN 1138 ? A ASN 1138 
1139 1 Y 1 A MET 1139 ? A MET 1139 
1140 1 Y 1 A THR 1140 ? A THR 1140 
1141 1 Y 1 A GLU 1141 ? A GLU 1141 
1142 1 Y 1 A PHE 1142 ? A PHE 1142 
1143 1 Y 1 A HIS 1143 ? A HIS 1143 
1144 1 Y 1 A SER 1144 ? A SER 1144 
1145 1 Y 1 A GLN 1145 ? A GLN 1145 
1146 1 Y 1 A ILE 1146 ? A ILE 1146 
1147 1 Y 1 A SER 1147 ? A SER 1147 
1148 1 Y 1 A LYS 1148 ? A LYS 1148 
1149 1 Y 1 A SER 1149 ? A SER 1149 
1150 1 Y 1 A ARG 1150 ? A ARG 1150 
1151 1 Y 1 A GLN 1151 ? A GLN 1151 
1152 1 Y 1 A GLU 1152 ? A GLU 1152 
1153 1 Y 1 A LEU 1153 ? A LEU 1153 
1154 1 Y 1 A GLU 1154 ? A GLU 1154 
1155 1 Y 1 A GLN 1155 ? A GLN 1155 
1156 1 Y 1 A HIS 1156 ? A HIS 1156 
1157 1 Y 1 A SER 1157 ? A SER 1157 
1158 1 Y 1 A VAL 1158 ? A VAL 1158 
1159 1 Y 1 A ASP 1159 ? A ASP 1159 
1160 1 Y 1 A THR 1160 ? A THR 1160 
1161 1 Y 1 A ALA 1161 ? A ALA 1161 
1162 1 Y 1 A SER 1162 ? A SER 1162 
1163 1 Y 1 A THR 1163 ? A THR 1163 
1164 1 Y 1 A SER 1164 ? A SER 1164 
1165 1 Y 1 A ASP 1165 ? A ASP 1165 
1166 1 Y 1 A ALA 1166 ? A ALA 1166 
1167 1 Y 1 A VAL 1167 ? A VAL 1167 
1168 1 Y 1 A THR 1168 ? A THR 1168 
1169 1 Y 1 A PHE 1169 ? A PHE 1169 
1170 1 Y 1 A ILE 1170 ? A ILE 1170 
1171 1 Y 1 A THR 1171 ? A THR 1171 
1172 1 Y 1 A TYR 1172 ? A TYR 1172 
1173 1 Y 1 A VAL 1173 ? A VAL 1173 
1174 1 Y 1 A GLN 1174 ? A GLN 1174 
1175 1 Y 1 A SER 1175 ? A SER 1175 
1176 1 Y 1 A LEU 1176 ? A LEU 1176 
1177 1 Y 1 A LYS 1177 ? A LYS 1177 
1178 1 Y 1 A ARG 1178 ? A ARG 1178 
1179 1 Y 1 A LYS 1179 ? A LYS 1179 
1180 1 Y 1 A ILE 1180 ? A ILE 1180 
1181 1 Y 1 A LYS 1181 ? A LYS 1181 
1182 1 Y 1 A GLN 1182 ? A GLN 1182 
1183 1 Y 1 A PHE 1183 ? A PHE 1183 
1184 1 Y 1 A GLU 1184 ? A GLU 1184 
1185 1 Y 1 A LYS 1185 ? A LYS 1185 
1186 1 Y 1 A GLN 1186 ? A GLN 1186 
1187 1 Y 1 A VAL 1187 ? A VAL 1187 
1188 1 Y 1 A GLU 1188 ? A GLU 1188 
1189 1 Y 1 A LEU 1189 ? A LEU 1189 
1190 1 Y 1 A TYR 1190 ? A TYR 1190 
1191 1 Y 1 A ARG 1191 ? A ARG 1191 
1192 1 Y 1 A ASN 1192 ? A ASN 1192 
1193 1 Y 1 A GLY 1193 ? A GLY 1193 
1194 1 Y 1 A GLN 1194 ? A GLN 1194 
1195 1 Y 1 A ARG 1195 ? A ARG 1195 
1196 1 Y 1 A LEU 1196 ? A LEU 1196 
1197 1 Y 1 A LEU 1197 ? A LEU 1197 
1198 1 Y 1 A GLU 1198 ? A GLU 1198 
1199 1 Y 1 A LYS 1199 ? A LYS 1199 
1200 1 Y 1 A GLN 1200 ? A GLN 1200 
1201 1 Y 1 A ARG 1201 ? A ARG 1201 
1202 1 Y 1 A PHE 1202 ? A PHE 1202 
1203 1 Y 1 A GLN 1203 ? A GLN 1203 
1204 1 Y 1 A PHE 1204 ? A PHE 1204 
1205 1 Y 1 A PRO 1205 ? A PRO 1205 
1206 1 Y 1 A PRO 1206 ? A PRO 1206 
1207 1 Y 1 A SER 1207 ? A SER 1207 
1208 1 Y 1 A TRP 1208 ? A TRP 1208 
1209 1 Y 1 A LEU 1209 ? A LEU 1209 
1210 1 Y 1 A TYR 1210 ? A TYR 1210 
1211 1 Y 1 A ILE 1211 ? A ILE 1211 
1212 1 Y 1 A ASP 1212 ? A ASP 1212 
1213 1 Y 1 A ASN 1213 ? A ASN 1213 
1214 1 Y 1 A ILE 1214 ? A ILE 1214 
1215 1 Y 1 A GLU 1215 ? A GLU 1215 
1216 1 Y 1 A GLY 1216 ? A GLY 1216 
1217 1 Y 1 A GLU 1217 ? A GLU 1217 
1218 1 Y 1 A TRP 1218 ? A TRP 1218 
1219 1 Y 1 A GLY 1219 ? A GLY 1219 
1220 1 Y 1 A ALA 1220 ? A ALA 1220 
1221 1 Y 1 A PHE 1221 ? A PHE 1221 
1222 1 Y 1 A ASN 1222 ? A ASN 1222 
1223 1 Y 1 A ASP 1223 ? A ASP 1223 
1224 1 Y 1 A ILE 1224 ? A ILE 1224 
1225 1 Y 1 A MET 1225 ? A MET 1225 
1226 1 Y 1 A ARG 1226 ? A ARG 1226 
1227 1 Y 1 A ARG 1227 ? A ARG 1227 
1228 1 Y 1 A LYS 1228 ? A LYS 1228 
1229 1 Y 1 A ASP 1229 ? A ASP 1229 
1230 1 Y 1 A SER 1230 ? A SER 1230 
1231 1 Y 1 A ALA 1231 ? A ALA 1231 
1232 1 Y 1 A ILE 1232 ? A ILE 1232 
1233 1 Y 1 A GLN 1233 ? A GLN 1233 
1234 1 Y 1 A GLN 1234 ? A GLN 1234 
1235 1 Y 1 A GLN 1235 ? A GLN 1235 
1236 1 Y 1 A VAL 1236 ? A VAL 1236 
1237 1 Y 1 A ALA 1237 ? A ALA 1237 
1238 1 Y 1 A ASN 1238 ? A ASN 1238 
1239 1 Y 1 A LEU 1239 ? A LEU 1239 
1240 1 Y 1 A GLN 1240 ? A GLN 1240 
1241 1 Y 1 A MET 1241 ? A MET 1241 
1242 1 Y 1 A LYS 1242 ? A LYS 1242 
1243 1 Y 1 A ILE 1243 ? A ILE 1243 
1244 1 Y 1 A VAL 1244 ? A VAL 1244 
1245 1 Y 1 A GLN 1245 ? A GLN 1245 
1246 1 Y 1 A GLU 1246 ? A GLU 1246 
1247 1 Y 1 A ASP 1247 ? A ASP 1247 
1248 1 Y 1 A ARG 1248 ? A ARG 1248 
1249 1 Y 1 A ALA 1249 ? A ALA 1249 
1250 1 Y 1 A VAL 1250 ? A VAL 1250 
1251 1 Y 1 A GLU 1251 ? A GLU 1251 
1252 1 Y 1 A SER 1252 ? A SER 1252 
1253 1 Y 1 A ARG 1253 ? A ARG 1253 
1254 1 Y 1 A THR 1254 ? A THR 1254 
1255 1 Y 1 A THR 1255 ? A THR 1255 
1256 1 Y 1 A ASP 1256 ? A ASP 1256 
1257 1 Y 1 A LEU 1257 ? A LEU 1257 
1258 1 Y 1 A LEU 1258 ? A LEU 1258 
1259 1 Y 1 A THR 1259 ? A THR 1259 
1260 1 Y 1 A ASP 1260 ? A ASP 1260 
1261 1 Y 1 A TRP 1261 ? A TRP 1261 
1262 1 Y 1 A GLU 1262 ? A GLU 1262 
1263 1 Y 1 A LYS 1263 ? A LYS 1263 
1264 1 Y 1 A THR 1264 ? A THR 1264 
1265 1 Y 1 A LYS 1265 ? A LYS 1265 
1266 1 Y 1 A PRO 1266 ? A PRO 1266 
1267 1 Y 1 A VAL 1267 ? A VAL 1267 
1268 1 Y 1 A THR 1268 ? A THR 1268 
1269 1 Y 1 A GLY 1269 ? A GLY 1269 
1270 1 Y 1 A ASN 1270 ? A ASN 1270 
1271 1 Y 1 A LEU 1271 ? A LEU 1271 
1272 1 Y 1 A ARG 1272 ? A ARG 1272 
1273 1 Y 1 A PRO 1273 ? A PRO 1273 
1274 1 Y 1 A GLU 1274 ? A GLU 1274 
1275 1 Y 1 A GLU 1275 ? A GLU 1275 
1276 1 Y 1 A ALA 1276 ? A ALA 1276 
1277 1 Y 1 A LEU 1277 ? A LEU 1277 
1278 1 Y 1 A GLN 1278 ? A GLN 1278 
1279 1 Y 1 A ALA 1279 ? A ALA 1279 
1280 1 Y 1 A LEU 1280 ? A LEU 1280 
1281 1 Y 1 A THR 1281 ? A THR 1281 
1282 1 Y 1 A ILE 1282 ? A ILE 1282 
1283 1 Y 1 A TYR 1283 ? A TYR 1283 
1284 1 Y 1 A GLU 1284 ? A GLU 1284 
1285 1 Y 1 A GLY 1285 ? A GLY 1285 
1286 1 Y 1 A LYS 1286 ? A LYS 1286 
1287 1 Y 1 A PHE 1287 ? A PHE 1287 
1288 1 Y 1 A GLY 1288 ? A GLY 1288 
1289 1 Y 1 A ARG 1289 ? A ARG 1289 
1290 1 Y 1 A LEU 1290 ? A LEU 1290 
1291 1 Y 1 A LYS 1291 ? A LYS 1291 
1292 1 Y 1 A ASP 1292 ? A ASP 1292 
1293 1 Y 1 A ASP 1293 ? A ASP 1293 
1294 1 Y 1 A ARG 1294 ? A ARG 1294 
1295 1 Y 1 A GLU 1295 ? A GLU 1295 
1296 1 Y 1 A LYS 1296 ? A LYS 1296 
1297 1 Y 1 A CYS 1297 ? A CYS 1297 
1298 1 Y 1 A ALA 1298 ? A ALA 1298 
1299 1 Y 1 A LYS 1299 ? A LYS 1299 
1300 1 Y 1 A ALA 1300 ? A ALA 1300 
1301 1 Y 1 A LYS 1301 ? A LYS 1301 
1302 1 Y 1 A GLU 1302 ? A GLU 1302 
1303 1 Y 1 A ALA 1303 ? A ALA 1303 
1304 1 Y 1 A LEU 1304 ? A LEU 1304 
1305 1 Y 1 A GLU 1305 ? A GLU 1305 
1306 1 Y 1 A LEU 1306 ? A LEU 1306 
1307 1 Y 1 A THR 1307 ? A THR 1307 
1308 1 Y 1 A ASP 1308 ? A ASP 1308 
1309 1 Y 1 A THR 1309 ? A THR 1309 
1310 1 Y 1 A GLY 1310 ? A GLY 1310 
1311 1 Y 1 A LEU 1311 ? A LEU 1311 
1312 1 Y 1 A LEU 1312 ? A LEU 1312 
1313 1 Y 1 A SER 1313 ? A SER 1313 
1314 1 Y 1 A GLY 1314 ? A GLY 1314 
1315 1 Y 1 A SER 1315 ? A SER 1315 
1316 1 Y 1 A GLU 1316 ? A GLU 1316 
1317 1 Y 1 A GLU 1317 ? A GLU 1317 
1318 1 Y 1 A ARG 1318 ? A ARG 1318 
1319 1 Y 1 A VAL 1319 ? A VAL 1319 
1320 1 Y 1 A GLN 1320 ? A GLN 1320 
1321 1 Y 1 A VAL 1321 ? A VAL 1321 
1322 1 Y 1 A ALA 1322 ? A ALA 1322 
1323 1 Y 1 A LEU 1323 ? A LEU 1323 
1324 1 Y 1 A GLU 1324 ? A GLU 1324 
1325 1 Y 1 A GLU 1325 ? A GLU 1325 
1326 1 Y 1 A LEU 1326 ? A LEU 1326 
1327 1 Y 1 A GLN 1327 ? A GLN 1327 
1328 1 Y 1 A ASP 1328 ? A ASP 1328 
1329 1 Y 1 A LEU 1329 ? A LEU 1329 
1330 1 Y 1 A LYS 1330 ? A LYS 1330 
1331 1 Y 1 A GLY 1331 ? A GLY 1331 
1332 1 Y 1 A VAL 1332 ? A VAL 1332 
1333 1 Y 1 A TRP 1333 ? A TRP 1333 
1334 1 Y 1 A SER 1334 ? A SER 1334 
1335 1 Y 1 A GLU 1335 ? A GLU 1335 
1336 1 Y 1 A LEU 1336 ? A LEU 1336 
1337 1 Y 1 A SER 1337 ? A SER 1337 
1338 1 Y 1 A LYS 1338 ? A LYS 1338 
1339 1 Y 1 A VAL 1339 ? A VAL 1339 
1340 1 Y 1 A TRP 1340 ? A TRP 1340 
1341 1 Y 1 A GLU 1341 ? A GLU 1341 
1342 1 Y 1 A GLN 1342 ? A GLN 1342 
1343 1 Y 1 A ILE 1343 ? A ILE 1343 
1344 1 Y 1 A ASP 1344 ? A ASP 1344 
1345 1 Y 1 A GLN 1345 ? A GLN 1345 
1346 1 Y 1 A MET 1346 ? A MET 1346 
1347 1 Y 1 A LYS 1347 ? A LYS 1347 
1348 1 Y 1 A GLU 1348 ? A GLU 1348 
1349 1 Y 1 A GLN 1349 ? A GLN 1349 
1350 1 Y 1 A PRO 1350 ? A PRO 1350 
1351 1 Y 1 A TRP 1351 ? A TRP 1351 
1352 1 Y 1 A VAL 1352 ? A VAL 1352 
1353 1 Y 1 A SER 1353 ? A SER 1353 
1354 1 Y 1 A VAL 1354 ? A VAL 1354 
1355 1 Y 1 A GLN 1355 ? A GLN 1355 
1356 1 Y 1 A PRO 1356 ? A PRO 1356 
1357 1 Y 1 A ARG 1357 ? A ARG 1357 
1358 1 Y 1 A LYS 1358 ? A LYS 1358 
1359 1 Y 1 A LEU 1359 ? A LEU 1359 
1360 1 Y 1 A ARG 1360 ? A ARG 1360 
1361 1 Y 1 A GLN 1361 ? A GLN 1361 
1362 1 Y 1 A ASN 1362 ? A ASN 1362 
1363 1 Y 1 A LEU 1363 ? A LEU 1363 
1364 1 Y 1 A ASP 1364 ? A ASP 1364 
1365 1 Y 1 A ALA 1365 ? A ALA 1365 
1366 1 Y 1 A LEU 1366 ? A LEU 1366 
1367 1 Y 1 A LEU 1367 ? A LEU 1367 
1368 1 Y 1 A ASN 1368 ? A ASN 1368 
1369 1 Y 1 A GLN 1369 ? A GLN 1369 
1370 1 Y 1 A LEU 1370 ? A LEU 1370 
1371 1 Y 1 A LYS 1371 ? A LYS 1371 
1372 1 Y 1 A SER 1372 ? A SER 1372 
1373 1 Y 1 A PHE 1373 ? A PHE 1373 
1374 1 Y 1 A PRO 1374 ? A PRO 1374 
1375 1 Y 1 A ALA 1375 ? A ALA 1375 
1376 1 Y 1 A ARG 1376 ? A ARG 1376 
1377 1 Y 1 A LEU 1377 ? A LEU 1377 
1378 1 Y 1 A ARG 1378 ? A ARG 1378 
1379 1 Y 1 A GLN 1379 ? A GLN 1379 
1380 1 Y 1 A TYR 1380 ? A TYR 1380 
1381 1 Y 1 A ALA 1381 ? A ALA 1381 
1382 1 Y 1 A SER 1382 ? A SER 1382 
1383 1 Y 1 A TYR 1383 ? A TYR 1383 
1384 1 Y 1 A GLU 1384 ? A GLU 1384 
1385 1 Y 1 A PHE 1385 ? A PHE 1385 
1386 1 Y 1 A VAL 1386 ? A VAL 1386 
1387 1 Y 1 A GLN 1387 ? A GLN 1387 
1388 1 Y 1 A ARG 1388 ? A ARG 1388 
1389 1 Y 1 A LEU 1389 ? A LEU 1389 
1390 1 Y 1 A LEU 1390 ? A LEU 1390 
1391 1 Y 1 A LYS 1391 ? A LYS 1391 
1392 1 Y 1 A GLY 1392 ? A GLY 1392 
1393 1 Y 1 A TYR 1393 ? A TYR 1393 
1394 1 Y 1 A MET 1394 ? A MET 1394 
1395 1 Y 1 A LYS 1395 ? A LYS 1395 
1396 1 Y 1 A ILE 1396 ? A ILE 1396 
1397 1 Y 1 A ASN 1397 ? A ASN 1397 
1398 1 Y 1 A MET 1398 ? A MET 1398 
1399 1 Y 1 A LEU 1399 ? A LEU 1399 
1400 1 Y 1 A VAL 1400 ? A VAL 1400 
1401 1 Y 1 A ILE 1401 ? A ILE 1401 
1402 1 Y 1 A GLU 1402 ? A GLU 1402 
1403 1 Y 1 A LEU 1403 ? A LEU 1403 
1404 1 Y 1 A LYS 1404 ? A LYS 1404 
1405 1 Y 1 A SER 1405 ? A SER 1405 
1406 1 Y 1 A GLU 1406 ? A GLU 1406 
1407 1 Y 1 A ALA 1407 ? A ALA 1407 
1408 1 Y 1 A LEU 1408 ? A LEU 1408 
1409 1 Y 1 A LYS 1409 ? A LYS 1409 
1410 1 Y 1 A ASP 1410 ? A ASP 1410 
1411 1 Y 1 A ARG 1411 ? A ARG 1411 
1412 1 Y 1 A HIS 1412 ? A HIS 1412 
1413 1 Y 1 A TRP 1413 ? A TRP 1413 
1414 1 Y 1 A LYS 1414 ? A LYS 1414 
1415 1 Y 1 A GLN 1415 ? A GLN 1415 
1416 1 Y 1 A LEU 1416 ? A LEU 1416 
1417 1 Y 1 A MET 1417 ? A MET 1417 
1418 1 Y 1 A LYS 1418 ? A LYS 1418 
1419 1 Y 1 A ARG 1419 ? A ARG 1419 
1420 1 Y 1 A LEU 1420 ? A LEU 1420 
1421 1 Y 1 A HIS 1421 ? A HIS 1421 
1422 1 Y 1 A VAL 1422 ? A VAL 1422 
1423 1 Y 1 A ASN 1423 ? A ASN 1423 
1424 1 Y 1 A TRP 1424 ? A TRP 1424 
1425 1 Y 1 A VAL 1425 ? A VAL 1425 
1426 1 Y 1 A VAL 1426 ? A VAL 1426 
1427 1 Y 1 A SER 1427 ? A SER 1427 
1428 1 Y 1 A GLU 1428 ? A GLU 1428 
1429 1 Y 1 A LEU 1429 ? A LEU 1429 
1430 1 Y 1 A THR 1430 ? A THR 1430 
1431 1 Y 1 A LEU 1431 ? A LEU 1431 
1432 1 Y 1 A GLY 1432 ? A GLY 1432 
1433 1 Y 1 A GLN 1433 ? A GLN 1433 
1434 1 Y 1 A ILE 1434 ? A ILE 1434 
1435 1 Y 1 A TRP 1435 ? A TRP 1435 
1436 1 Y 1 A ASP 1436 ? A ASP 1436 
1437 1 Y 1 A VAL 1437 ? A VAL 1437 
1438 1 Y 1 A ASP 1438 ? A ASP 1438 
1439 1 Y 1 A LEU 1439 ? A LEU 1439 
1440 1 Y 1 A GLN 1440 ? A GLN 1440 
1441 1 Y 1 A LYS 1441 ? A LYS 1441 
1442 1 Y 1 A ASN 1442 ? A ASN 1442 
1443 1 Y 1 A GLU 1443 ? A GLU 1443 
1444 1 Y 1 A ALA 1444 ? A ALA 1444 
1445 1 Y 1 A ILE 1445 ? A ILE 1445 
1446 1 Y 1 A VAL 1446 ? A VAL 1446 
1447 1 Y 1 A LYS 1447 ? A LYS 1447 
1448 1 Y 1 A ASP 1448 ? A ASP 1448 
1449 1 Y 1 A VAL 1449 ? A VAL 1449 
1450 1 Y 1 A LEU 1450 ? A LEU 1450 
1451 1 Y 1 A LEU 1451 ? A LEU 1451 
1452 1 Y 1 A VAL 1452 ? A VAL 1452 
1453 1 Y 1 A ALA 1453 ? A ALA 1453 
1454 1 Y 1 A GLN 1454 ? A GLN 1454 
1455 1 Y 1 A GLY 1455 ? A GLY 1455 
1456 1 Y 1 A GLU 1456 ? A GLU 1456 
1457 1 Y 1 A GLY 2390 ? A GLY 2390 
1458 1 Y 1 A GLU 2391 ? A GLU 2391 
1459 1 Y 1 A ASP 2392 ? A ASP 2392 
1460 1 Y 1 A GLU 2393 ? A GLU 2393 
1461 1 Y 1 A ALA 2394 ? A ALA 2394 
1462 1 Y 1 A GLN 2395 ? A GLN 2395 
1463 1 Y 1 A ARG 2396 ? A ARG 2396 
1464 1 Y 1 A ARG 2397 ? A ARG 2397 
1465 1 Y 1 A ARG 2398 ? A ARG 2398 
1466 1 Y 1 A LYS 2399 ? A LYS 2399 
1467 1 Y 1 A GLY 2400 ? A GLY 2400 
1468 1 Y 1 A LYS 2401 ? A LYS 2401 
1469 1 Y 1 A GLU 2402 ? A GLU 2402 
1470 1 Y 1 A ASP 2403 ? A ASP 2403 
1471 1 Y 1 A GLU 2404 ? A GLU 2404 
1472 1 Y 1 A GLY 2405 ? A GLY 2405 
1473 1 Y 1 A GLU 2406 ? A GLU 2406 
1474 1 Y 1 A GLU 2407 ? A GLU 2407 
1475 1 Y 1 A ALA 2408 ? A ALA 2408 
1476 1 Y 1 A ALA 2409 ? A ALA 2409 
1477 1 Y 1 A LEU 3218 ? A LEU 3218 
1478 1 Y 1 A ARG 3219 ? A ARG 3219 
1479 1 Y 1 A ARG 3220 ? A ARG 3220 
1480 1 Y 1 A ASP 3221 ? A ASP 3221 
1481 1 Y 1 A LEU 3222 ? A LEU 3222 
1482 1 Y 1 A ARG 3223 ? A ARG 3223 
1483 1 Y 1 A ILE 3224 ? A ILE 3224 
1484 1 Y 1 A LYS 3225 ? A LYS 3225 
1485 1 Y 1 A SER 3226 ? A SER 3226 
1486 1 Y 1 A GLN 3227 ? A GLN 3227 
1487 1 Y 1 A GLU 3228 ? A GLU 3228 
1488 1 Y 1 A LEU 3229 ? A LEU 3229 
1489 1 Y 1 A GLU 3230 ? A GLU 3230 
1490 1 Y 1 A VAL 3231 ? A VAL 3231 
1491 1 Y 1 A LYS 3232 ? A LYS 3232 
1492 1 Y 1 A ASN 3233 ? A ASN 3233 
1493 1 Y 1 A ALA 3234 ? A ALA 3234 
1494 1 Y 1 A ALA 3235 ? A ALA 3235 
1495 1 Y 1 A ALA 3236 ? A ALA 3236 
1496 1 Y 1 A ASN 3237 ? A ASN 3237 
1497 1 Y 1 A ASP 3238 ? A ASP 3238 
1498 1 Y 1 A LYS 3239 ? A LYS 3239 
1499 1 Y 1 A LEU 3240 ? A LEU 3240 
1500 1 Y 1 A LYS 3241 ? A LYS 3241 
1501 1 Y 1 A LYS 3242 ? A LYS 3242 
1502 1 Y 1 A MET 3243 ? A MET 3243 
1503 1 Y 1 A VAL 3244 ? A VAL 3244 
1504 1 Y 1 A LYS 3245 ? A LYS 3245 
1505 1 Y 1 A ASP 3246 ? A ASP 3246 
1506 1 Y 1 A GLN 3247 ? A GLN 3247 
1507 1 Y 1 A GLN 3248 ? A GLN 3248 
1508 1 Y 1 A GLU 3249 ? A GLU 3249 
1509 1 Y 1 A ALA 3250 ? A ALA 3250 
1510 1 Y 1 A GLU 3251 ? A GLU 3251 
1511 1 Y 1 A LYS 3252 ? A LYS 3252 
1512 1 Y 1 A LYS 3253 ? A LYS 3253 
1513 1 Y 1 A LYS 3254 ? A LYS 3254 
1514 1 Y 1 A VAL 3255 ? A VAL 3255 
1515 1 Y 1 A MET 3256 ? A MET 3256 
1516 1 Y 1 A SER 3257 ? A SER 3257 
1517 1 Y 1 A GLN 3258 ? A GLN 3258 
1518 1 Y 1 A GLU 3259 ? A GLU 3259 
1519 1 Y 1 A ILE 3260 ? A ILE 3260 
1520 1 Y 1 A GLN 3261 ? A GLN 3261 
1521 1 Y 1 A GLU 3262 ? A GLU 3262 
1522 1 Y 1 A GLN 3263 ? A GLN 3263 
1523 1 Y 1 A LEU 3264 ? A LEU 3264 
1524 1 Y 1 A HIS 3265 ? A HIS 3265 
1525 1 Y 1 A LYS 3266 ? A LYS 3266 
1526 1 Y 1 A GLN 3267 ? A GLN 3267 
1527 1 Y 1 A GLN 3268 ? A GLN 3268 
1528 1 Y 1 A GLU 3269 ? A GLU 3269 
1529 1 Y 1 A VAL 3270 ? A VAL 3270 
1530 1 Y 1 A ILE 3271 ? A ILE 3271 
1531 1 Y 1 A ALA 3272 ? A ALA 3272 
1532 1 Y 1 A ASP 3273 ? A ASP 3273 
1533 1 Y 1 A LYS 3274 ? A LYS 3274 
1534 1 Y 1 A GLN 3275 ? A GLN 3275 
1535 1 Y 1 A MET 3276 ? A MET 3276 
1536 1 Y 1 A SER 3277 ? A SER 3277 
1537 1 Y 1 A VAL 3278 ? A VAL 3278 
1538 1 Y 1 A LYS 3279 ? A LYS 3279 
1539 1 Y 1 A GLU 3280 ? A GLU 3280 
1540 1 Y 1 A ASP 3281 ? A ASP 3281 
1541 1 Y 1 A LEU 3282 ? A LEU 3282 
1542 1 Y 1 A ASP 3283 ? A ASP 3283 
1543 1 Y 1 A LYS 3284 ? A LYS 3284 
1544 1 Y 1 A VAL 3285 ? A VAL 3285 
1545 1 Y 1 A GLU 3286 ? A GLU 3286 
1546 1 Y 1 A PRO 3287 ? A PRO 3287 
1547 1 Y 1 A ALA 3288 ? A ALA 3288 
1548 1 Y 1 A VAL 3289 ? A VAL 3289 
1549 1 Y 1 A ILE 3290 ? A ILE 3290 
1550 1 Y 1 A GLU 3291 ? A GLU 3291 
1551 1 Y 1 A ALA 3292 ? A ALA 3292 
1552 1 Y 1 A GLN 3293 ? A GLN 3293 
1553 1 Y 1 A ASN 3294 ? A ASN 3294 
1554 1 Y 1 A ALA 3295 ? A ALA 3295 
1555 1 Y 1 A VAL 3296 ? A VAL 3296 
1556 1 Y 1 A LYS 3297 ? A LYS 3297 
1557 1 Y 1 A SER 3298 ? A SER 3298 
1558 1 Y 1 A ILE 3299 ? A ILE 3299 
1559 1 Y 1 A LYS 3300 ? A LYS 3300 
1560 1 Y 1 A LYS 3301 ? A LYS 3301 
1561 1 Y 1 A GLN 3302 ? A GLN 3302 
1562 1 Y 1 A HIS 3303 ? A HIS 3303 
1563 1 Y 1 A LEU 3304 ? A LEU 3304 
1564 1 Y 1 A VAL 3305 ? A VAL 3305 
1565 1 Y 1 A GLU 3306 ? A GLU 3306 
1566 1 Y 1 A VAL 3307 ? A VAL 3307 
1567 1 Y 1 A ARG 3308 ? A ARG 3308 
1568 1 Y 1 A SER 3309 ? A SER 3309 
1569 1 Y 1 A MET 3310 ? A MET 3310 
1570 1 Y 1 A ALA 3311 ? A ALA 3311 
1571 1 Y 1 A ASN 3312 ? A ASN 3312 
1572 1 Y 1 A PRO 3313 ? A PRO 3313 
1573 1 Y 1 A PRO 3314 ? A PRO 3314 
1574 1 Y 1 A ALA 3315 ? A ALA 3315 
1575 1 Y 1 A ALA 3316 ? A ALA 3316 
1576 1 Y 1 A VAL 3317 ? A VAL 3317 
1577 1 Y 1 A LYS 3318 ? A LYS 3318 
1578 1 Y 1 A LEU 3319 ? A LEU 3319 
1579 1 Y 1 A ALA 3320 ? A ALA 3320 
1580 1 Y 1 A LEU 3321 ? A LEU 3321 
1581 1 Y 1 A GLU 3322 ? A GLU 3322 
1582 1 Y 1 A SER 3323 ? A SER 3323 
1583 1 Y 1 A ILE 3324 ? A ILE 3324 
1584 1 Y 1 A CYS 3325 ? A CYS 3325 
1585 1 Y 1 A LEU 3326 ? A LEU 3326 
1586 1 Y 1 A LEU 3327 ? A LEU 3327 
1587 1 Y 1 A LEU 3328 ? A LEU 3328 
1588 1 Y 1 A GLY 3329 ? A GLY 3329 
1589 1 Y 1 A GLU 3330 ? A GLU 3330 
1590 1 Y 1 A SER 3331 ? A SER 3331 
1591 1 Y 1 A THR 3332 ? A THR 3332 
1592 1 Y 1 A THR 3333 ? A THR 3333 
1593 1 Y 1 A ASP 3334 ? A ASP 3334 
1594 1 Y 1 A TRP 3335 ? A TRP 3335 
1595 1 Y 1 A LYS 3336 ? A LYS 3336 
1596 1 Y 1 A GLN 3337 ? A GLN 3337 
1597 1 Y 1 A ILE 3338 ? A ILE 3338 
1598 1 Y 1 A ARG 3339 ? A ARG 3339 
1599 1 Y 1 A SER 3340 ? A SER 3340 
1600 1 Y 1 A ILE 3341 ? A ILE 3341 
1601 1 Y 1 A ILE 3342 ? A ILE 3342 
1602 1 Y 1 A MET 3343 ? A MET 3343 
1603 1 Y 1 A ARG 3344 ? A ARG 3344 
1604 1 Y 1 A GLU 3345 ? A GLU 3345 
1605 1 Y 1 A ASN 3346 ? A ASN 3346 
1606 1 Y 1 A PHE 3347 ? A PHE 3347 
1607 1 Y 1 A ILE 3348 ? A ILE 3348 
1608 1 Y 1 A PRO 3349 ? A PRO 3349 
1609 1 Y 1 A THR 3350 ? A THR 3350 
1610 1 Y 1 A ILE 3351 ? A ILE 3351 
1611 1 Y 1 A VAL 3352 ? A VAL 3352 
1612 1 Y 1 A ASN 3353 ? A ASN 3353 
1613 1 Y 1 A PHE 3354 ? A PHE 3354 
1614 1 Y 1 A SER 3355 ? A SER 3355 
1615 1 Y 1 A ALA 3356 ? A ALA 3356 
1616 1 Y 1 A GLU 3357 ? A GLU 3357 
1617 1 Y 1 A GLU 3358 ? A GLU 3358 
1618 1 Y 1 A ILE 3359 ? A ILE 3359 
1619 1 Y 1 A SER 3360 ? A SER 3360 
1620 1 Y 1 A ASP 3361 ? A ASP 3361 
1621 1 Y 1 A ALA 3362 ? A ALA 3362 
1622 1 Y 1 A ILE 3363 ? A ILE 3363 
1623 1 Y 1 A ARG 3364 ? A ARG 3364 
1624 1 Y 1 A GLU 3365 ? A GLU 3365 
1625 1 Y 1 A LYS 3366 ? A LYS 3366 
1626 1 Y 1 A MET 3367 ? A MET 3367 
1627 1 Y 1 A LYS 3368 ? A LYS 3368 
1628 1 Y 1 A LYS 3369 ? A LYS 3369 
1629 1 Y 1 A ASN 3370 ? A ASN 3370 
1630 1 Y 1 A TYR 3371 ? A TYR 3371 
1631 1 Y 1 A MET 3372 ? A MET 3372 
1632 1 Y 1 A SER 3373 ? A SER 3373 
1633 1 Y 1 A ASN 3374 ? A ASN 3374 
1634 1 Y 1 A PRO 3375 ? A PRO 3375 
1635 1 Y 1 A SER 3376 ? A SER 3376 
1636 1 Y 1 A TYR 3377 ? A TYR 3377 
1637 1 Y 1 A ASN 3378 ? A ASN 3378 
1638 1 Y 1 A TYR 3379 ? A TYR 3379 
1639 1 Y 1 A GLU 3380 ? A GLU 3380 
1640 1 Y 1 A ILE 3381 ? A ILE 3381 
1641 1 Y 1 A VAL 3382 ? A VAL 3382 
1642 1 Y 1 A ASN 3383 ? A ASN 3383 
1643 1 Y 1 A ARG 3384 ? A ARG 3384 
1644 1 Y 1 A ALA 3385 ? A ALA 3385 
1645 1 Y 1 A SER 3386 ? A SER 3386 
1646 1 Y 1 A LEU 3387 ? A LEU 3387 
1647 1 Y 1 A ALA 3388 ? A ALA 3388 
1648 1 Y 1 A CYS 3389 ? A CYS 3389 
1649 1 Y 1 A GLY 3390 ? A GLY 3390 
1650 1 Y 1 A PRO 3391 ? A PRO 3391 
1651 1 Y 1 A MET 3392 ? A MET 3392 
1652 1 Y 1 A VAL 3393 ? A VAL 3393 
1653 1 Y 1 A LYS 3394 ? A LYS 3394 
1654 1 Y 1 A TRP 3395 ? A TRP 3395 
1655 1 Y 1 A ALA 3396 ? A ALA 3396 
1656 1 Y 1 A ILE 3397 ? A ILE 3397 
1657 1 Y 1 A ALA 3398 ? A ALA 3398 
1658 1 Y 1 A GLN 3399 ? A GLN 3399 
1659 1 Y 1 A LEU 3400 ? A LEU 3400 
1660 1 Y 1 A ASN 3401 ? A ASN 3401 
1661 1 Y 1 A TYR 3402 ? A TYR 3402 
1662 1 Y 1 A ALA 3403 ? A ALA 3403 
1663 1 Y 1 A ASP 3404 ? A ASP 3404 
1664 1 Y 1 A MET 3405 ? A MET 3405 
1665 1 Y 1 A LEU 3406 ? A LEU 3406 
1666 1 Y 1 A LYS 3407 ? A LYS 3407 
1667 1 Y 1 A ARG 3408 ? A ARG 3408 
1668 1 Y 1 A VAL 3409 ? A VAL 3409 
1669 1 Y 1 A GLU 3410 ? A GLU 3410 
1670 1 Y 1 A PRO 3411 ? A PRO 3411 
1671 1 Y 1 A LEU 3412 ? A LEU 3412 
1672 1 Y 1 A ARG 3413 ? A ARG 3413 
1673 1 Y 1 A ASN 3414 ? A ASN 3414 
1674 1 Y 1 A GLU 3415 ? A GLU 3415 
1675 1 Y 1 A LEU 3416 ? A LEU 3416 
1676 1 Y 1 A GLN 3417 ? A GLN 3417 
1677 1 Y 1 A LYS 3418 ? A LYS 3418 
1678 1 Y 1 A LEU 3419 ? A LEU 3419 
1679 1 Y 1 A GLU 3420 ? A GLU 3420 
1680 1 Y 1 A ASP 3421 ? A ASP 3421 
1681 1 Y 1 A ASP 3422 ? A ASP 3422 
1682 1 Y 1 A ALA 3423 ? A ALA 3423 
1683 1 Y 1 A LYS 3424 ? A LYS 3424 
1684 1 Y 1 A ASP 3425 ? A ASP 3425 
1685 1 Y 1 A ASN 3426 ? A ASN 3426 
1686 1 Y 1 A GLN 3427 ? A GLN 3427 
1687 1 Y 1 A GLN 3428 ? A GLN 3428 
1688 1 Y 1 A LYS 3429 ? A LYS 3429 
1689 1 Y 1 A ALA 3430 ? A ALA 3430 
1690 1 Y 1 A ASN 3431 ? A ASN 3431 
1691 1 Y 1 A GLU 3432 ? A GLU 3432 
1692 1 Y 1 A VAL 3433 ? A VAL 3433 
1693 1 Y 1 A GLU 3434 ? A GLU 3434 
1694 1 Y 1 A GLN 3435 ? A GLN 3435 
1695 1 Y 1 A MET 3436 ? A MET 3436 
1696 1 Y 1 A ILE 3437 ? A ILE 3437 
1697 1 Y 1 A ARG 3438 ? A ARG 3438 
1698 1 Y 1 A ASP 3439 ? A ASP 3439 
1699 1 Y 1 A LEU 3440 ? A LEU 3440 
1700 1 Y 1 A GLU 3441 ? A GLU 3441 
1701 1 Y 1 A ALA 3442 ? A ALA 3442 
1702 1 Y 1 A SER 3443 ? A SER 3443 
1703 1 Y 1 A ILE 3444 ? A ILE 3444 
1704 1 Y 1 A ALA 3445 ? A ALA 3445 
1705 1 Y 1 A ARG 3446 ? A ARG 3446 
1706 1 Y 1 A TYR 3447 ? A TYR 3447 
1707 1 Y 1 A LYS 3448 ? A LYS 3448 
1708 1 Y 1 A GLU 3449 ? A GLU 3449 
1709 1 Y 1 A GLU 3450 ? A GLU 3450 
1710 1 Y 1 A TYR 3451 ? A TYR 3451 
1711 1 Y 1 A ALA 3452 ? A ALA 3452 
1712 1 Y 1 A VAL 3453 ? A VAL 3453 
1713 1 Y 1 A LEU 3454 ? A LEU 3454 
1714 1 Y 1 A ILE 3455 ? A ILE 3455 
1715 1 Y 1 A SER 3456 ? A SER 3456 
1716 1 Y 1 A GLU 3457 ? A GLU 3457 
1717 1 Y 1 A ALA 3458 ? A ALA 3458 
1718 1 Y 1 A GLN 3459 ? A GLN 3459 
1719 1 Y 1 A ALA 3460 ? A ALA 3460 
1720 1 Y 1 A ILE 3461 ? A ILE 3461 
1721 1 Y 1 A LYS 3462 ? A LYS 3462 
1722 1 Y 1 A ALA 3463 ? A ALA 3463 
1723 1 Y 1 A ASP 3464 ? A ASP 3464 
1724 1 Y 1 A LEU 3465 ? A LEU 3465 
1725 1 Y 1 A ALA 3466 ? A ALA 3466 
1726 1 Y 1 A ALA 3467 ? A ALA 3467 
1727 1 Y 1 A VAL 3468 ? A VAL 3468 
1728 1 Y 1 A GLU 3469 ? A GLU 3469 
1729 1 Y 1 A ALA 3470 ? A ALA 3470 
1730 1 Y 1 A LYS 3471 ? A LYS 3471 
1731 1 Y 1 A MET 4348 ? A MET 4348 
1732 1 Y 1 A LEU 4349 ? A LEU 4349 
1733 1 Y 1 A GLU 4350 ? A GLU 4350 
1734 1 Y 1 A ASP 4351 ? A ASP 4351 
1735 1 Y 1 A GLU 4352 ? A GLU 4352 
1736 1 Y 1 A ASP 4353 ? A ASP 4353 
1737 1 Y 1 A ASP 4354 ? A ASP 4354 
1738 1 Y 1 A LEU 4355 ? A LEU 4355 
1739 1 Y 1 A ALA 4356 ? A ALA 4356 
1740 1 Y 1 A TYR 4357 ? A TYR 4357 
1741 1 Y 1 A ALA 4358 ? A ALA 4358 
1742 1 Y 1 A GLU 4359 ? A GLU 4359 
1743 1 Y 1 A THR 4360 ? A THR 4360 
1744 1 Y 1 A GLU 4361 ? A GLU 4361 
1745 1 Y 1 A LYS 4362 ? A LYS 4362 
1746 1 Y 1 A LYS 4363 ? A LYS 4363 
1747 1 Y 1 A THR 4364 ? A THR 4364 
1748 1 Y 1 A ARG 4365 ? A ARG 4365 
1749 1 Y 1 A THR 4366 ? A THR 4366 
1750 1 Y 1 A ASP 4367 ? A ASP 4367 
1751 1 Y 1 A SER 4368 ? A SER 4368 
1752 1 Y 1 A THR 4369 ? A THR 4369 
1753 1 Y 1 A SER 4370 ? A SER 4370 
1754 1 Y 1 A ASP 4371 ? A ASP 4371 
1755 1 Y 1 A GLY 4372 ? A GLY 4372 
1756 1 Y 1 A ARG 4373 ? A ARG 4373 
1757 1 Y 1 A GLU 4646 ? A GLU 4646 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
ATP PG     P  N N 116 
ATP O1G    O  N N 117 
ATP O2G    O  N N 118 
ATP O3G    O  N N 119 
ATP PB     P  N R 120 
ATP O1B    O  N N 121 
ATP O2B    O  N N 122 
ATP O3B    O  N N 123 
ATP PA     P  N R 124 
ATP O1A    O  N N 125 
ATP O2A    O  N N 126 
ATP O3A    O  N N 127 
ATP "O5'"  O  N N 128 
ATP "C5'"  C  N N 129 
ATP "C4'"  C  N R 130 
ATP "O4'"  O  N N 131 
ATP "C3'"  C  N S 132 
ATP "O3'"  O  N N 133 
ATP "C2'"  C  N R 134 
ATP "O2'"  O  N N 135 
ATP "C1'"  C  N R 136 
ATP N9     N  Y N 137 
ATP C8     C  Y N 138 
ATP N7     N  Y N 139 
ATP C5     C  Y N 140 
ATP C6     C  Y N 141 
ATP N6     N  N N 142 
ATP N1     N  Y N 143 
ATP C2     C  Y N 144 
ATP N3     N  Y N 145 
ATP C4     C  Y N 146 
ATP HOG2   H  N N 147 
ATP HOG3   H  N N 148 
ATP HOB2   H  N N 149 
ATP HOA2   H  N N 150 
ATP "H5'1" H  N N 151 
ATP "H5'2" H  N N 152 
ATP "H4'"  H  N N 153 
ATP "H3'"  H  N N 154 
ATP "HO3'" H  N N 155 
ATP "H2'"  H  N N 156 
ATP "HO2'" H  N N 157 
ATP "H1'"  H  N N 158 
ATP H8     H  N N 159 
ATP HN61   H  N N 160 
ATP HN62   H  N N 161 
ATP H2     H  N N 162 
CYS N      N  N N 163 
CYS CA     C  N R 164 
CYS C      C  N N 165 
CYS O      O  N N 166 
CYS CB     C  N N 167 
CYS SG     S  N N 168 
CYS OXT    O  N N 169 
CYS H      H  N N 170 
CYS H2     H  N N 171 
CYS HA     H  N N 172 
CYS HB2    H  N N 173 
CYS HB3    H  N N 174 
CYS HG     H  N N 175 
CYS HXT    H  N N 176 
GLN N      N  N N 177 
GLN CA     C  N S 178 
GLN C      C  N N 179 
GLN O      O  N N 180 
GLN CB     C  N N 181 
GLN CG     C  N N 182 
GLN CD     C  N N 183 
GLN OE1    O  N N 184 
GLN NE2    N  N N 185 
GLN OXT    O  N N 186 
GLN H      H  N N 187 
GLN H2     H  N N 188 
GLN HA     H  N N 189 
GLN HB2    H  N N 190 
GLN HB3    H  N N 191 
GLN HG2    H  N N 192 
GLN HG3    H  N N 193 
GLN HE21   H  N N 194 
GLN HE22   H  N N 195 
GLN HXT    H  N N 196 
GLU N      N  N N 197 
GLU CA     C  N S 198 
GLU C      C  N N 199 
GLU O      O  N N 200 
GLU CB     C  N N 201 
GLU CG     C  N N 202 
GLU CD     C  N N 203 
GLU OE1    O  N N 204 
GLU OE2    O  N N 205 
GLU OXT    O  N N 206 
GLU H      H  N N 207 
GLU H2     H  N N 208 
GLU HA     H  N N 209 
GLU HB2    H  N N 210 
GLU HB3    H  N N 211 
GLU HG2    H  N N 212 
GLU HG3    H  N N 213 
GLU HE2    H  N N 214 
GLU HXT    H  N N 215 
GLY N      N  N N 216 
GLY CA     C  N N 217 
GLY C      C  N N 218 
GLY O      O  N N 219 
GLY OXT    O  N N 220 
GLY H      H  N N 221 
GLY H2     H  N N 222 
GLY HA2    H  N N 223 
GLY HA3    H  N N 224 
GLY HXT    H  N N 225 
HIS N      N  N N 226 
HIS CA     C  N S 227 
HIS C      C  N N 228 
HIS O      O  N N 229 
HIS CB     C  N N 230 
HIS CG     C  Y N 231 
HIS ND1    N  Y N 232 
HIS CD2    C  Y N 233 
HIS CE1    C  Y N 234 
HIS NE2    N  Y N 235 
HIS OXT    O  N N 236 
HIS H      H  N N 237 
HIS H2     H  N N 238 
HIS HA     H  N N 239 
HIS HB2    H  N N 240 
HIS HB3    H  N N 241 
HIS HD1    H  N N 242 
HIS HD2    H  N N 243 
HIS HE1    H  N N 244 
HIS HE2    H  N N 245 
HIS HXT    H  N N 246 
HOH O      O  N N 247 
HOH H1     H  N N 248 
HOH H2     H  N N 249 
ILE N      N  N N 250 
ILE CA     C  N S 251 
ILE C      C  N N 252 
ILE O      O  N N 253 
ILE CB     C  N S 254 
ILE CG1    C  N N 255 
ILE CG2    C  N N 256 
ILE CD1    C  N N 257 
ILE OXT    O  N N 258 
ILE H      H  N N 259 
ILE H2     H  N N 260 
ILE HA     H  N N 261 
ILE HB     H  N N 262 
ILE HG12   H  N N 263 
ILE HG13   H  N N 264 
ILE HG21   H  N N 265 
ILE HG22   H  N N 266 
ILE HG23   H  N N 267 
ILE HD11   H  N N 268 
ILE HD12   H  N N 269 
ILE HD13   H  N N 270 
ILE HXT    H  N N 271 
LEU N      N  N N 272 
LEU CA     C  N S 273 
LEU C      C  N N 274 
LEU O      O  N N 275 
LEU CB     C  N N 276 
LEU CG     C  N N 277 
LEU CD1    C  N N 278 
LEU CD2    C  N N 279 
LEU OXT    O  N N 280 
LEU H      H  N N 281 
LEU H2     H  N N 282 
LEU HA     H  N N 283 
LEU HB2    H  N N 284 
LEU HB3    H  N N 285 
LEU HG     H  N N 286 
LEU HD11   H  N N 287 
LEU HD12   H  N N 288 
LEU HD13   H  N N 289 
LEU HD21   H  N N 290 
LEU HD22   H  N N 291 
LEU HD23   H  N N 292 
LEU HXT    H  N N 293 
LYS N      N  N N 294 
LYS CA     C  N S 295 
LYS C      C  N N 296 
LYS O      O  N N 297 
LYS CB     C  N N 298 
LYS CG     C  N N 299 
LYS CD     C  N N 300 
LYS CE     C  N N 301 
LYS NZ     N  N N 302 
LYS OXT    O  N N 303 
LYS H      H  N N 304 
LYS H2     H  N N 305 
LYS HA     H  N N 306 
LYS HB2    H  N N 307 
LYS HB3    H  N N 308 
LYS HG2    H  N N 309 
LYS HG3    H  N N 310 
LYS HD2    H  N N 311 
LYS HD3    H  N N 312 
LYS HE2    H  N N 313 
LYS HE3    H  N N 314 
LYS HZ1    H  N N 315 
LYS HZ2    H  N N 316 
LYS HZ3    H  N N 317 
LYS HXT    H  N N 318 
MET N      N  N N 319 
MET CA     C  N S 320 
MET C      C  N N 321 
MET O      O  N N 322 
MET CB     C  N N 323 
MET CG     C  N N 324 
MET SD     S  N N 325 
MET CE     C  N N 326 
MET OXT    O  N N 327 
MET H      H  N N 328 
MET H2     H  N N 329 
MET HA     H  N N 330 
MET HB2    H  N N 331 
MET HB3    H  N N 332 
MET HG2    H  N N 333 
MET HG3    H  N N 334 
MET HE1    H  N N 335 
MET HE2    H  N N 336 
MET HE3    H  N N 337 
MET HXT    H  N N 338 
MG  MG     MG N N 339 
PHE N      N  N N 340 
PHE CA     C  N S 341 
PHE C      C  N N 342 
PHE O      O  N N 343 
PHE CB     C  N N 344 
PHE CG     C  Y N 345 
PHE CD1    C  Y N 346 
PHE CD2    C  Y N 347 
PHE CE1    C  Y N 348 
PHE CE2    C  Y N 349 
PHE CZ     C  Y N 350 
PHE OXT    O  N N 351 
PHE H      H  N N 352 
PHE H2     H  N N 353 
PHE HA     H  N N 354 
PHE HB2    H  N N 355 
PHE HB3    H  N N 356 
PHE HD1    H  N N 357 
PHE HD2    H  N N 358 
PHE HE1    H  N N 359 
PHE HE2    H  N N 360 
PHE HZ     H  N N 361 
PHE HXT    H  N N 362 
PRO N      N  N N 363 
PRO CA     C  N S 364 
PRO C      C  N N 365 
PRO O      O  N N 366 
PRO CB     C  N N 367 
PRO CG     C  N N 368 
PRO CD     C  N N 369 
PRO OXT    O  N N 370 
PRO H      H  N N 371 
PRO HA     H  N N 372 
PRO HB2    H  N N 373 
PRO HB3    H  N N 374 
PRO HG2    H  N N 375 
PRO HG3    H  N N 376 
PRO HD2    H  N N 377 
PRO HD3    H  N N 378 
PRO HXT    H  N N 379 
SER N      N  N N 380 
SER CA     C  N S 381 
SER C      C  N N 382 
SER O      O  N N 383 
SER CB     C  N N 384 
SER OG     O  N N 385 
SER OXT    O  N N 386 
SER H      H  N N 387 
SER H2     H  N N 388 
SER HA     H  N N 389 
SER HB2    H  N N 390 
SER HB3    H  N N 391 
SER HG     H  N N 392 
SER HXT    H  N N 393 
THR N      N  N N 394 
THR CA     C  N S 395 
THR C      C  N N 396 
THR O      O  N N 397 
THR CB     C  N R 398 
THR OG1    O  N N 399 
THR CG2    C  N N 400 
THR OXT    O  N N 401 
THR H      H  N N 402 
THR H2     H  N N 403 
THR HA     H  N N 404 
THR HB     H  N N 405 
THR HG1    H  N N 406 
THR HG21   H  N N 407 
THR HG22   H  N N 408 
THR HG23   H  N N 409 
THR HXT    H  N N 410 
TRP N      N  N N 411 
TRP CA     C  N S 412 
TRP C      C  N N 413 
TRP O      O  N N 414 
TRP CB     C  N N 415 
TRP CG     C  Y N 416 
TRP CD1    C  Y N 417 
TRP CD2    C  Y N 418 
TRP NE1    N  Y N 419 
TRP CE2    C  Y N 420 
TRP CE3    C  Y N 421 
TRP CZ2    C  Y N 422 
TRP CZ3    C  Y N 423 
TRP CH2    C  Y N 424 
TRP OXT    O  N N 425 
TRP H      H  N N 426 
TRP H2     H  N N 427 
TRP HA     H  N N 428 
TRP HB2    H  N N 429 
TRP HB3    H  N N 430 
TRP HD1    H  N N 431 
TRP HE1    H  N N 432 
TRP HE3    H  N N 433 
TRP HZ2    H  N N 434 
TRP HZ3    H  N N 435 
TRP HH2    H  N N 436 
TRP HXT    H  N N 437 
TYR N      N  N N 438 
TYR CA     C  N S 439 
TYR C      C  N N 440 
TYR O      O  N N 441 
TYR CB     C  N N 442 
TYR CG     C  Y N 443 
TYR CD1    C  Y N 444 
TYR CD2    C  Y N 445 
TYR CE1    C  Y N 446 
TYR CE2    C  Y N 447 
TYR CZ     C  Y N 448 
TYR OH     O  N N 449 
TYR OXT    O  N N 450 
TYR H      H  N N 451 
TYR H2     H  N N 452 
TYR HA     H  N N 453 
TYR HB2    H  N N 454 
TYR HB3    H  N N 455 
TYR HD1    H  N N 456 
TYR HD2    H  N N 457 
TYR HE1    H  N N 458 
TYR HE2    H  N N 459 
TYR HH     H  N N 460 
TYR HXT    H  N N 461 
VAL N      N  N N 462 
VAL CA     C  N S 463 
VAL C      C  N N 464 
VAL O      O  N N 465 
VAL CB     C  N N 466 
VAL CG1    C  N N 467 
VAL CG2    C  N N 468 
VAL OXT    O  N N 469 
VAL H      H  N N 470 
VAL H2     H  N N 471 
VAL HA     H  N N 472 
VAL HB     H  N N 473 
VAL HG11   H  N N 474 
VAL HG12   H  N N 475 
VAL HG13   H  N N 476 
VAL HG21   H  N N 477 
VAL HG22   H  N N 478 
VAL HG23   H  N N 479 
VAL HXT    H  N N 480 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
ATP PG    O1G    doub N N 114 
ATP PG    O2G    sing N N 115 
ATP PG    O3G    sing N N 116 
ATP PG    O3B    sing N N 117 
ATP O2G   HOG2   sing N N 118 
ATP O3G   HOG3   sing N N 119 
ATP PB    O1B    doub N N 120 
ATP PB    O2B    sing N N 121 
ATP PB    O3B    sing N N 122 
ATP PB    O3A    sing N N 123 
ATP O2B   HOB2   sing N N 124 
ATP PA    O1A    doub N N 125 
ATP PA    O2A    sing N N 126 
ATP PA    O3A    sing N N 127 
ATP PA    "O5'"  sing N N 128 
ATP O2A   HOA2   sing N N 129 
ATP "O5'" "C5'"  sing N N 130 
ATP "C5'" "C4'"  sing N N 131 
ATP "C5'" "H5'1" sing N N 132 
ATP "C5'" "H5'2" sing N N 133 
ATP "C4'" "O4'"  sing N N 134 
ATP "C4'" "C3'"  sing N N 135 
ATP "C4'" "H4'"  sing N N 136 
ATP "O4'" "C1'"  sing N N 137 
ATP "C3'" "O3'"  sing N N 138 
ATP "C3'" "C2'"  sing N N 139 
ATP "C3'" "H3'"  sing N N 140 
ATP "O3'" "HO3'" sing N N 141 
ATP "C2'" "O2'"  sing N N 142 
ATP "C2'" "C1'"  sing N N 143 
ATP "C2'" "H2'"  sing N N 144 
ATP "O2'" "HO2'" sing N N 145 
ATP "C1'" N9     sing N N 146 
ATP "C1'" "H1'"  sing N N 147 
ATP N9    C8     sing Y N 148 
ATP N9    C4     sing Y N 149 
ATP C8    N7     doub Y N 150 
ATP C8    H8     sing N N 151 
ATP N7    C5     sing Y N 152 
ATP C5    C6     sing Y N 153 
ATP C5    C4     doub Y N 154 
ATP C6    N6     sing N N 155 
ATP C6    N1     doub Y N 156 
ATP N6    HN61   sing N N 157 
ATP N6    HN62   sing N N 158 
ATP N1    C2     sing Y N 159 
ATP C2    N3     doub Y N 160 
ATP C2    H2     sing N N 161 
ATP N3    C4     sing Y N 162 
CYS N     CA     sing N N 163 
CYS N     H      sing N N 164 
CYS N     H2     sing N N 165 
CYS CA    C      sing N N 166 
CYS CA    CB     sing N N 167 
CYS CA    HA     sing N N 168 
CYS C     O      doub N N 169 
CYS C     OXT    sing N N 170 
CYS CB    SG     sing N N 171 
CYS CB    HB2    sing N N 172 
CYS CB    HB3    sing N N 173 
CYS SG    HG     sing N N 174 
CYS OXT   HXT    sing N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
HOH O     H1     sing N N 243 
HOH O     H2     sing N N 244 
ILE N     CA     sing N N 245 
ILE N     H      sing N N 246 
ILE N     H2     sing N N 247 
ILE CA    C      sing N N 248 
ILE CA    CB     sing N N 249 
ILE CA    HA     sing N N 250 
ILE C     O      doub N N 251 
ILE C     OXT    sing N N 252 
ILE CB    CG1    sing N N 253 
ILE CB    CG2    sing N N 254 
ILE CB    HB     sing N N 255 
ILE CG1   CD1    sing N N 256 
ILE CG1   HG12   sing N N 257 
ILE CG1   HG13   sing N N 258 
ILE CG2   HG21   sing N N 259 
ILE CG2   HG22   sing N N 260 
ILE CG2   HG23   sing N N 261 
ILE CD1   HD11   sing N N 262 
ILE CD1   HD12   sing N N 263 
ILE CD1   HD13   sing N N 264 
ILE OXT   HXT    sing N N 265 
LEU N     CA     sing N N 266 
LEU N     H      sing N N 267 
LEU N     H2     sing N N 268 
LEU CA    C      sing N N 269 
LEU CA    CB     sing N N 270 
LEU CA    HA     sing N N 271 
LEU C     O      doub N N 272 
LEU C     OXT    sing N N 273 
LEU CB    CG     sing N N 274 
LEU CB    HB2    sing N N 275 
LEU CB    HB3    sing N N 276 
LEU CG    CD1    sing N N 277 
LEU CG    CD2    sing N N 278 
LEU CG    HG     sing N N 279 
LEU CD1   HD11   sing N N 280 
LEU CD1   HD12   sing N N 281 
LEU CD1   HD13   sing N N 282 
LEU CD2   HD21   sing N N 283 
LEU CD2   HD22   sing N N 284 
LEU CD2   HD23   sing N N 285 
LEU OXT   HXT    sing N N 286 
LYS N     CA     sing N N 287 
LYS N     H      sing N N 288 
LYS N     H2     sing N N 289 
LYS CA    C      sing N N 290 
LYS CA    CB     sing N N 291 
LYS CA    HA     sing N N 292 
LYS C     O      doub N N 293 
LYS C     OXT    sing N N 294 
LYS CB    CG     sing N N 295 
LYS CB    HB2    sing N N 296 
LYS CB    HB3    sing N N 297 
LYS CG    CD     sing N N 298 
LYS CG    HG2    sing N N 299 
LYS CG    HG3    sing N N 300 
LYS CD    CE     sing N N 301 
LYS CD    HD2    sing N N 302 
LYS CD    HD3    sing N N 303 
LYS CE    NZ     sing N N 304 
LYS CE    HE2    sing N N 305 
LYS CE    HE3    sing N N 306 
LYS NZ    HZ1    sing N N 307 
LYS NZ    HZ2    sing N N 308 
LYS NZ    HZ3    sing N N 309 
LYS OXT   HXT    sing N N 310 
MET N     CA     sing N N 311 
MET N     H      sing N N 312 
MET N     H2     sing N N 313 
MET CA    C      sing N N 314 
MET CA    CB     sing N N 315 
MET CA    HA     sing N N 316 
MET C     O      doub N N 317 
MET C     OXT    sing N N 318 
MET CB    CG     sing N N 319 
MET CB    HB2    sing N N 320 
MET CB    HB3    sing N N 321 
MET CG    SD     sing N N 322 
MET CG    HG2    sing N N 323 
MET CG    HG3    sing N N 324 
MET SD    CE     sing N N 325 
MET CE    HE1    sing N N 326 
MET CE    HE2    sing N N 327 
MET CE    HE3    sing N N 328 
MET OXT   HXT    sing N N 329 
PHE N     CA     sing N N 330 
PHE N     H      sing N N 331 
PHE N     H2     sing N N 332 
PHE CA    C      sing N N 333 
PHE CA    CB     sing N N 334 
PHE CA    HA     sing N N 335 
PHE C     O      doub N N 336 
PHE C     OXT    sing N N 337 
PHE CB    CG     sing N N 338 
PHE CB    HB2    sing N N 339 
PHE CB    HB3    sing N N 340 
PHE CG    CD1    doub Y N 341 
PHE CG    CD2    sing Y N 342 
PHE CD1   CE1    sing Y N 343 
PHE CD1   HD1    sing N N 344 
PHE CD2   CE2    doub Y N 345 
PHE CD2   HD2    sing N N 346 
PHE CE1   CZ     doub Y N 347 
PHE CE1   HE1    sing N N 348 
PHE CE2   CZ     sing Y N 349 
PHE CE2   HE2    sing N N 350 
PHE CZ    HZ     sing N N 351 
PHE OXT   HXT    sing N N 352 
PRO N     CA     sing N N 353 
PRO N     CD     sing N N 354 
PRO N     H      sing N N 355 
PRO CA    C      sing N N 356 
PRO CA    CB     sing N N 357 
PRO CA    HA     sing N N 358 
PRO C     O      doub N N 359 
PRO C     OXT    sing N N 360 
PRO CB    CG     sing N N 361 
PRO CB    HB2    sing N N 362 
PRO CB    HB3    sing N N 363 
PRO CG    CD     sing N N 364 
PRO CG    HG2    sing N N 365 
PRO CG    HG3    sing N N 366 
PRO CD    HD2    sing N N 367 
PRO CD    HD3    sing N N 368 
PRO OXT   HXT    sing N N 369 
SER N     CA     sing N N 370 
SER N     H      sing N N 371 
SER N     H2     sing N N 372 
SER CA    C      sing N N 373 
SER CA    CB     sing N N 374 
SER CA    HA     sing N N 375 
SER C     O      doub N N 376 
SER C     OXT    sing N N 377 
SER CB    OG     sing N N 378 
SER CB    HB2    sing N N 379 
SER CB    HB3    sing N N 380 
SER OG    HG     sing N N 381 
SER OXT   HXT    sing N N 382 
THR N     CA     sing N N 383 
THR N     H      sing N N 384 
THR N     H2     sing N N 385 
THR CA    C      sing N N 386 
THR CA    CB     sing N N 387 
THR CA    HA     sing N N 388 
THR C     O      doub N N 389 
THR C     OXT    sing N N 390 
THR CB    OG1    sing N N 391 
THR CB    CG2    sing N N 392 
THR CB    HB     sing N N 393 
THR OG1   HG1    sing N N 394 
THR CG2   HG21   sing N N 395 
THR CG2   HG22   sing N N 396 
THR CG2   HG23   sing N N 397 
THR OXT   HXT    sing N N 398 
TRP N     CA     sing N N 399 
TRP N     H      sing N N 400 
TRP N     H2     sing N N 401 
TRP CA    C      sing N N 402 
TRP CA    CB     sing N N 403 
TRP CA    HA     sing N N 404 
TRP C     O      doub N N 405 
TRP C     OXT    sing N N 406 
TRP CB    CG     sing N N 407 
TRP CB    HB2    sing N N 408 
TRP CB    HB3    sing N N 409 
TRP CG    CD1    doub Y N 410 
TRP CG    CD2    sing Y N 411 
TRP CD1   NE1    sing Y N 412 
TRP CD1   HD1    sing N N 413 
TRP CD2   CE2    doub Y N 414 
TRP CD2   CE3    sing Y N 415 
TRP NE1   CE2    sing Y N 416 
TRP NE1   HE1    sing N N 417 
TRP CE2   CZ2    sing Y N 418 
TRP CE3   CZ3    doub Y N 419 
TRP CE3   HE3    sing N N 420 
TRP CZ2   CH2    doub Y N 421 
TRP CZ2   HZ2    sing N N 422 
TRP CZ3   CH2    sing Y N 423 
TRP CZ3   HZ3    sing N N 424 
TRP CH2   HH2    sing N N 425 
TRP OXT   HXT    sing N N 426 
TYR N     CA     sing N N 427 
TYR N     H      sing N N 428 
TYR N     H2     sing N N 429 
TYR CA    C      sing N N 430 
TYR CA    CB     sing N N 431 
TYR CA    HA     sing N N 432 
TYR C     O      doub N N 433 
TYR C     OXT    sing N N 434 
TYR CB    CG     sing N N 435 
TYR CB    HB2    sing N N 436 
TYR CB    HB3    sing N N 437 
TYR CG    CD1    doub Y N 438 
TYR CG    CD2    sing Y N 439 
TYR CD1   CE1    sing Y N 440 
TYR CD1   HD1    sing N N 441 
TYR CD2   CE2    doub Y N 442 
TYR CD2   HD2    sing N N 443 
TYR CE1   CZ     doub Y N 444 
TYR CE1   HE1    sing N N 445 
TYR CE2   CZ     sing Y N 446 
TYR CE2   HE2    sing N N 447 
TYR CZ    OH     sing N N 448 
TYR OH    HH     sing N N 449 
TYR OXT   HXT    sing N N 450 
VAL N     CA     sing N N 451 
VAL N     H      sing N N 452 
VAL N     H2     sing N N 453 
VAL CA    C      sing N N 454 
VAL CA    CB     sing N N 455 
VAL CA    HA     sing N N 456 
VAL C     O      doub N N 457 
VAL C     OXT    sing N N 458 
VAL CB    CG1    sing N N 459 
VAL CB    CG2    sing N N 460 
VAL CB    HB     sing N N 461 
VAL CG1   HG11   sing N N 462 
VAL CG1   HG12   sing N N 463 
VAL CG1   HG13   sing N N 464 
VAL CG2   HG21   sing N N 465 
VAL CG2   HG22   sing N N 466 
VAL CG2   HG23   sing N N 467 
VAL OXT   HXT    sing N N 468 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-02 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BLZ 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-1(phi motor) of full-length human dynein-1 in 5mM ATP' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                1.5 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         40 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?         ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 SerialEM  4 
MASKING                    ? 3  ? ? ? ?         ? 
'CTF CORRECTION'           ? 4  1 ? ? ?         ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ? 
'MODEL FITTING'            ? 7  ? ? ? ?         ? 
'MODEL REFINEMENT'         ? 8  ? ? ? PHENIX    ? 
OTHER                      ? 9  ? ? ? ?         ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?         ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? cryoSPARC 4 
CLASSIFICATION             ? 12 1 ? ? ?         ? 
RECONSTRUCTION             ? 13 1 ? ? cryoSPARC 4 
# 
_em_specimen.concentration           2 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM142959 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM139483 2 
# 
_atom_sites.entry_id                    9BLZ 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . MET A 1 1457 ? 109.833 71.013  161.349 1.00 77.51  ? 1457 MET A N     1 
ATOM   2     C  CA    . MET A 1 1457 ? 109.240 69.747  161.762 1.00 82.56  ? 1457 MET A CA    1 
ATOM   3     C  C     . MET A 1 1457 ? 107.855 69.591  161.142 1.00 83.79  ? 1457 MET A C     1 
ATOM   4     O  O     . MET A 1 1457 ? 107.389 68.476  160.907 1.00 85.21  ? 1457 MET A O     1 
ATOM   5     C  CB    . MET A 1 1457 ? 109.157 69.667  163.289 1.00 88.75  ? 1457 MET A CB    1 
ATOM   6     C  CG    . MET A 1 1457 ? 108.700 68.321  163.831 1.00 87.98  ? 1457 MET A CG    1 
ATOM   7     S  SD    . MET A 1 1457 ? 109.887 67.005  163.491 1.00 99.62  ? 1457 MET A SD    1 
ATOM   8     C  CE    . MET A 1 1457 ? 108.831 65.561  163.560 1.00 87.54  ? 1457 MET A CE    1 
ATOM   9     N  N     . ALA A 1 1458 ? 107.203 70.726  160.874 1.00 82.07  ? 1458 ALA A N     1 
ATOM   10    C  CA    . ALA A 1 1458 ? 105.871 70.694  160.278 1.00 81.42  ? 1458 ALA A CA    1 
ATOM   11    C  C     . ALA A 1 1458 ? 105.920 70.205  158.835 1.00 81.57  ? 1458 ALA A C     1 
ATOM   12    O  O     . ALA A 1 1458 ? 104.933 69.667  158.320 1.00 83.52  ? 1458 ALA A O     1 
ATOM   13    C  CB    . ALA A 1 1458 ? 105.227 72.078  160.355 1.00 78.73  ? 1458 ALA A CB    1 
ATOM   14    N  N     . LEU A 1 1459 ? 107.055 70.400  158.160 1.00 78.83  ? 1459 LEU A N     1 
ATOM   15    C  CA    . LEU A 1 1459 ? 107.203 69.891  156.800 1.00 80.35  ? 1459 LEU A CA    1 
ATOM   16    C  C     . LEU A 1 1459 ? 107.135 68.369  156.781 1.00 79.87  ? 1459 LEU A C     1 
ATOM   17    O  O     . LEU A 1 1459 ? 106.492 67.771  155.907 1.00 81.03  ? 1459 LEU A O     1 
ATOM   18    C  CB    . LEU A 1 1459 ? 108.518 70.382  156.191 1.00 76.76  ? 1459 LEU A CB    1 
ATOM   19    C  CG    . LEU A 1 1459 ? 108.638 71.845  155.752 1.00 80.67  ? 1459 LEU A CG    1 
ATOM   20    C  CD1   . LEU A 1 1459 ? 108.706 72.806  156.934 1.00 80.78  ? 1459 LEU A CD1   1 
ATOM   21    C  CD2   . LEU A 1 1459 ? 109.850 72.017  154.855 1.00 77.54  ? 1459 LEU A CD2   1 
ATOM   22    N  N     . GLU A 1 1460 ? 107.798 67.722  157.742 1.00 77.50  ? 1460 GLU A N     1 
ATOM   23    C  CA    . GLU A 1 1460 ? 107.692 66.273  157.853 1.00 79.18  ? 1460 GLU A CA    1 
ATOM   24    C  C     . GLU A 1 1460 ? 106.260 65.859  158.161 1.00 79.38  ? 1460 GLU A C     1 
ATOM   25    O  O     . GLU A 1 1460 ? 105.800 64.807  157.708 1.00 79.06  ? 1460 GLU A O     1 
ATOM   26    C  CB    . GLU A 1 1460 ? 108.653 65.751  158.922 1.00 81.47  ? 1460 GLU A CB    1 
ATOM   27    C  CG    . GLU A 1 1460 ? 108.556 64.253  159.166 1.00 84.92  ? 1460 GLU A CG    1 
ATOM   28    C  CD    . GLU A 1 1460 ? 109.535 63.765  160.214 1.00 90.14  ? 1460 GLU A CD    1 
ATOM   29    O  OE1   . GLU A 1 1460 ? 110.756 63.930  160.010 1.00 88.20  ? 1460 GLU A OE1   1 
ATOM   30    O  OE2   . GLU A 1 1460 ? 109.085 63.213  161.239 1.00 89.46  ? 1460 GLU A OE2   1 
ATOM   31    N  N     . GLU A 1 1461 ? 105.533 66.688  158.914 1.00 77.57  ? 1461 GLU A N     1 
ATOM   32    C  CA    . GLU A 1 1461 ? 104.117 66.421  159.150 1.00 77.20  ? 1461 GLU A CA    1 
ATOM   33    C  C     . GLU A 1 1461 ? 103.324 66.467  157.850 1.00 76.83  ? 1461 GLU A C     1 
ATOM   34    O  O     . GLU A 1 1461 ? 102.457 65.621  157.613 1.00 78.01  ? 1461 GLU A O     1 
ATOM   35    C  CB    . GLU A 1 1461 ? 103.552 67.417  160.164 1.00 78.78  ? 1461 GLU A CB    1 
ATOM   36    C  CG    . GLU A 1 1461 ? 104.349 67.516  161.451 1.00 88.62  ? 1461 GLU A CG    1 
ATOM   37    C  CD    . GLU A 1 1461 ? 104.761 66.157  161.982 1.00 94.09  ? 1461 GLU A CD    1 
ATOM   38    O  OE1   . GLU A 1 1461 ? 103.867 65.339  162.285 1.00 90.22  ? 1461 GLU A OE1   1 
ATOM   39    O  OE2   . GLU A 1 1461 ? 105.978 65.906  162.093 1.00 96.06  ? 1461 GLU A OE2   1 
ATOM   40    N  N     . PHE A 1 1462 ? 103.605 67.453  156.994 1.00 77.60  ? 1462 PHE A N     1 
ATOM   41    C  CA    . PHE A 1 1462 ? 102.909 67.539  155.712 1.00 72.71  ? 1462 PHE A CA    1 
ATOM   42    C  C     . PHE A 1 1462 ? 103.208 66.321  154.845 1.00 66.44  ? 1462 PHE A C     1 
ATOM   43    O  O     . PHE A 1 1462 ? 102.303 65.738  154.230 1.00 62.74  ? 1462 PHE A O     1 
ATOM   44    C  CB    . PHE A 1 1462 ? 103.297 68.826  154.980 1.00 69.51  ? 1462 PHE A CB    1 
ATOM   45    C  CG    . PHE A 1 1462 ? 103.132 70.074  155.803 1.00 78.97  ? 1462 PHE A CG    1 
ATOM   46    C  CD1   . PHE A 1 1462 ? 102.143 70.164  156.769 1.00 83.57  ? 1462 PHE A CD1   1 
ATOM   47    C  CD2   . PHE A 1 1462 ? 103.966 71.163  155.602 1.00 80.30  ? 1462 PHE A CD2   1 
ATOM   48    C  CE1   . PHE A 1 1462 ? 101.993 71.313  157.523 1.00 83.32  ? 1462 PHE A CE1   1 
ATOM   49    C  CE2   . PHE A 1 1462 ? 103.820 72.314  156.352 1.00 85.23  ? 1462 PHE A CE2   1 
ATOM   50    C  CZ    . PHE A 1 1462 ? 102.833 72.389  157.314 1.00 84.56  ? 1462 PHE A CZ    1 
ATOM   51    N  N     . LEU A 1 1463 ? 104.481 65.920  154.787 1.00 68.31  ? 1463 LEU A N     1 
ATOM   52    C  CA    . LEU A 1 1463 ? 104.842 64.727  154.025 1.00 65.98  ? 1463 LEU A CA    1 
ATOM   53    C  C     . LEU A 1 1463 ? 104.156 63.485  154.583 1.00 65.49  ? 1463 LEU A C     1 
ATOM   54    O  O     . LEU A 1 1463 ? 103.677 62.636  153.821 1.00 63.59  ? 1463 LEU A O     1 
ATOM   55    C  CB    . LEU A 1 1463 ? 106.361 64.537  154.004 1.00 67.00  ? 1463 LEU A CB    1 
ATOM   56    C  CG    . LEU A 1 1463 ? 107.203 65.273  152.954 1.00 62.91  ? 1463 LEU A CG    1 
ATOM   57    C  CD1   . LEU A 1 1463 ? 106.837 64.800  151.555 1.00 58.36  ? 1463 LEU A CD1   1 
ATOM   58    C  CD2   . LEU A 1 1463 ? 107.077 66.781  153.048 1.00 62.45  ? 1463 LEU A CD2   1 
ATOM   59    N  N     . LYS A 1 1464 ? 104.094 63.364  155.910 1.00 66.67  ? 1464 LYS A N     1 
ATOM   60    C  CA    . LYS A 1 1464 ? 103.443 62.213  156.525 1.00 64.44  ? 1464 LYS A CA    1 
ATOM   61    C  C     . LYS A 1 1464 ? 101.952 62.194  156.216 1.00 62.12  ? 1464 LYS A C     1 
ATOM   62    O  O     . LYS A 1 1464 ? 101.379 61.133  155.950 1.00 61.40  ? 1464 LYS A O     1 
ATOM   63    C  CB    . LYS A 1 1464 ? 103.682 62.220  158.035 1.00 68.95  ? 1464 LYS A CB    1 
ATOM   64    C  CG    . LYS A 1 1464 ? 103.076 61.032  158.761 1.00 72.38  ? 1464 LYS A CG    1 
ATOM   65    C  CD    . LYS A 1 1464 ? 103.465 61.026  160.229 1.00 77.15  ? 1464 LYS A CD    1 
ATOM   66    C  CE    . LYS A 1 1464 ? 102.754 62.134  160.986 1.00 80.63  ? 1464 LYS A CE    1 
ATOM   67    N  NZ    . LYS A 1 1464 ? 101.289 61.883  161.079 1.00 82.91  ? 1464 LYS A NZ    1 
ATOM   68    N  N     . GLN A 1 1465 ? 101.302 63.360  156.260 1.00 63.41  ? 1465 GLN A N     1 
ATOM   69    C  CA    . GLN A 1 1465 ? 99.880  63.427  155.932 1.00 60.89  ? 1465 GLN A CA    1 
ATOM   70    C  C     . GLN A 1 1465 ? 99.634  63.033  154.483 1.00 57.00  ? 1465 GLN A C     1 
ATOM   71    O  O     . GLN A 1 1465 ? 98.680  62.308  154.181 1.00 56.64  ? 1465 GLN A O     1 
ATOM   72    C  CB    . GLN A 1 1465 ? 99.327  64.826  156.209 1.00 62.10  ? 1465 GLN A CB    1 
ATOM   73    C  CG    . GLN A 1 1465 ? 99.438  65.277  157.653 1.00 66.83  ? 1465 GLN A CG    1 
ATOM   74    C  CD    . GLN A 1 1465 ? 99.323  66.780  157.802 1.00 73.07  ? 1465 GLN A CD    1 
ATOM   75    O  OE1   . GLN A 1 1465 ? 100.234 67.438  158.307 1.00 75.96  ? 1465 GLN A OE1   1 
ATOM   76    N  NE2   . GLN A 1 1465 ? 98.201  67.334  157.360 1.00 74.59  ? 1465 GLN A NE2   1 
ATOM   77    N  N     . ILE A 1 1466 ? 100.488 63.498  153.569 1.00 55.41  ? 1466 ILE A N     1 
ATOM   78    C  CA    . ILE A 1 1466 ? 100.339 63.122  152.163 1.00 46.30  ? 1466 ILE A CA    1 
ATOM   79    C  C     . ILE A 1 1466 ? 100.512 61.614  152.000 1.00 44.65  ? 1466 ILE A C     1 
ATOM   80    O  O     . ILE A 1 1466 ? 99.752  60.951  151.275 1.00 45.02  ? 1466 ILE A O     1 
ATOM   81    C  CB    . ILE A 1 1466 ? 101.334 63.909  151.291 1.00 43.56  ? 1466 ILE A CB    1 
ATOM   82    C  CG1   . ILE A 1 1466 ? 100.802 65.317  151.019 1.00 41.82  ? 1466 ILE A CG1   1 
ATOM   83    C  CG2   . ILE A 1 1466 ? 101.593 63.188  149.980 1.00 45.95  ? 1466 ILE A CG2   1 
ATOM   84    C  CD1   . ILE A 1 1466 ? 101.868 66.300  150.594 1.00 39.77  ? 1466 ILE A CD1   1 
ATOM   85    N  N     . ARG A 1 1467 ? 101.512 61.049  152.682 1.00 47.28  ? 1467 ARG A N     1 
ATOM   86    C  CA    . ARG A 1 1467 ? 101.750 59.612  152.611 1.00 47.35  ? 1467 ARG A CA    1 
ATOM   87    C  C     . ARG A 1 1467 ? 100.564 58.824  153.154 1.00 51.02  ? 1467 ARG A C     1 
ATOM   88    O  O     . ARG A 1 1467 ? 100.146 57.827  152.558 1.00 49.53  ? 1467 ARG A O     1 
ATOM   89    C  CB    . ARG A 1 1467 ? 103.030 59.255  153.369 1.00 51.34  ? 1467 ARG A CB    1 
ATOM   90    C  CG    . ARG A 1 1467 ? 103.354 57.769  153.378 1.00 54.45  ? 1467 ARG A CG    1 
ATOM   91    C  CD    . ARG A 1 1467 ? 104.355 57.405  152.295 1.00 55.12  ? 1467 ARG A CD    1 
ATOM   92    N  NE    . ARG A 1 1467 ? 105.485 58.325  152.259 1.00 64.10  ? 1467 ARG A NE    1 
ATOM   93    C  CZ    . ARG A 1 1467 ? 106.493 58.238  151.401 1.00 63.86  ? 1467 ARG A CZ    1 
ATOM   94    N  NH1   . ARG A 1 1467 ? 106.545 57.281  150.490 1.00 59.34  ? 1467 ARG A NH1   1 
ATOM   95    N  NH2   . ARG A 1 1467 ? 107.473 59.136  151.459 1.00 57.41  ? 1467 ARG A NH2   1 
ATOM   96    N  N     . GLU A 1 1468 ? 100.006 59.256  154.288 1.00 51.09  ? 1468 GLU A N     1 
ATOM   97    C  CA    . GLU A 1 1468 ? 98.861  58.548  154.855 1.00 52.65  ? 1468 GLU A CA    1 
ATOM   98    C  C     . GLU A 1 1468 ? 97.637  58.686  153.962 1.00 50.69  ? 1468 GLU A C     1 
ATOM   99    O  O     . GLU A 1 1468 ? 96.814  57.766  153.879 1.00 46.73  ? 1468 GLU A O     1 
ATOM   100   C  CB    . GLU A 1 1468 ? 98.548  59.050  156.266 1.00 52.07  ? 1468 GLU A CB    1 
ATOM   101   C  CG    . GLU A 1 1468 ? 99.601  58.717  157.312 1.00 62.46  ? 1468 GLU A CG    1 
ATOM   102   C  CD    . GLU A 1 1468 ? 99.694  59.763  158.408 1.00 76.63  ? 1468 GLU A CD    1 
ATOM   103   O  OE1   . GLU A 1 1468 ? 99.722  60.969  158.091 1.00 77.05  ? 1468 GLU A OE1   1 
ATOM   104   O  OE2   . GLU A 1 1468 ? 99.737  59.374  159.594 1.00 75.15  ? 1468 GLU A OE2   1 
ATOM   105   N  N     . VAL A 1 1469 ? 97.491  59.832  153.295 1.00 48.71  ? 1469 VAL A N     1 
ATOM   106   C  CA    . VAL A 1 1469 ? 96.372  60.016  152.378 1.00 41.65  ? 1469 VAL A CA    1 
ATOM   107   C  C     . VAL A 1 1469 ? 96.470  59.032  151.220 1.00 40.64  ? 1469 VAL A C     1 
ATOM   108   O  O     . VAL A 1 1469 ? 95.516  58.305  150.923 1.00 41.94  ? 1469 VAL A O     1 
ATOM   109   C  CB    . VAL A 1 1469 ? 96.311  61.472  151.882 1.00 41.29  ? 1469 VAL A CB    1 
ATOM   110   C  CG1   . VAL A 1 1469 ? 95.493  61.564  150.603 1.00 39.27  ? 1469 VAL A CG1   1 
ATOM   111   C  CG2   . VAL A 1 1469 ? 95.715  62.368  152.954 1.00 38.87  ? 1469 VAL A CG2   1 
ATOM   112   N  N     . TRP A 1 1470 ? 97.632  58.966  150.569 1.00 40.88  ? 1470 TRP A N     1 
ATOM   113   C  CA    . TRP A 1 1470 ? 97.737  58.108  149.391 1.00 36.81  ? 1470 TRP A CA    1 
ATOM   114   C  C     . TRP A 1 1470 ? 98.065  56.653  149.705 1.00 42.07  ? 1470 TRP A C     1 
ATOM   115   O  O     . TRP A 1 1470 ? 98.101  55.837  148.779 1.00 43.57  ? 1470 TRP A O     1 
ATOM   116   C  CB    . TRP A 1 1470 ? 98.763  58.654  148.393 1.00 34.68  ? 1470 TRP A CB    1 
ATOM   117   C  CG    . TRP A 1 1470 ? 98.456  60.036  147.940 1.00 34.98  ? 1470 TRP A CG    1 
ATOM   118   C  CD1   . TRP A 1 1470 ? 99.042  61.188  148.362 1.00 34.15  ? 1470 TRP A CD1   1 
ATOM   119   C  CD2   . TRP A 1 1470 ? 97.436  60.420  147.010 1.00 31.28  ? 1470 TRP A CD2   1 
ATOM   120   N  NE1   . TRP A 1 1470 ? 98.478  62.264  147.726 1.00 32.11  ? 1470 TRP A NE1   1 
ATOM   121   C  CE2   . TRP A 1 1470 ? 97.483  61.821  146.896 1.00 30.71  ? 1470 TRP A CE2   1 
ATOM   122   C  CE3   . TRP A 1 1470 ? 96.497  59.713  146.254 1.00 27.68  ? 1470 TRP A CE3   1 
ATOM   123   C  CZ2   . TRP A 1 1470 ? 96.628  62.531  146.057 1.00 28.45  ? 1470 TRP A CZ2   1 
ATOM   124   C  CZ3   . TRP A 1 1470 ? 95.649  60.418  145.422 1.00 27.26  ? 1470 TRP A CZ3   1 
ATOM   125   C  CH2   . TRP A 1 1470 ? 95.720  61.812  145.331 1.00 25.81  ? 1470 TRP A CH2   1 
ATOM   126   N  N     . ASN A 1 1471 ? 98.305  56.299  150.967 1.00 47.77  ? 1471 ASN A N     1 
ATOM   127   C  CA    . ASN A 1 1471 ? 98.436  54.886  151.299 1.00 44.87  ? 1471 ASN A CA    1 
ATOM   128   C  C     . ASN A 1 1471 ? 97.083  54.210  151.473 1.00 46.82  ? 1471 ASN A C     1 
ATOM   129   O  O     . ASN A 1 1471 ? 97.018  52.976  151.486 1.00 47.61  ? 1471 ASN A O     1 
ATOM   130   C  CB    . ASN A 1 1471 ? 99.276  54.714  152.566 1.00 50.38  ? 1471 ASN A CB    1 
ATOM   131   C  CG    . ASN A 1 1471 ? 100.759 54.909  152.311 1.00 59.52  ? 1471 ASN A CG    1 
ATOM   132   O  OD1   . ASN A 1 1471 ? 101.178 55.168  151.182 1.00 57.02  ? 1471 ASN A OD1   1 
ATOM   133   N  ND2   . ASN A 1 1471 ? 101.562 54.784  153.361 1.00 61.80  ? 1471 ASN A ND2   1 
ATOM   134   N  N     . THR A 1 1472 ? 96.006  54.986  151.609 1.00 44.85  ? 1472 THR A N     1 
ATOM   135   C  CA    . THR A 1 1472 ? 94.670  54.434  151.772 1.00 44.71  ? 1472 THR A CA    1 
ATOM   136   C  C     . THR A 1 1472 ? 93.634  55.018  150.823 1.00 47.39  ? 1472 THR A C     1 
ATOM   137   O  O     . THR A 1 1472 ? 92.508  54.509  150.790 1.00 55.51  ? 1472 THR A O     1 
ATOM   138   C  CB    . THR A 1 1472 ? 94.169  54.632  153.212 1.00 46.31  ? 1472 THR A CB    1 
ATOM   139   O  OG1   . THR A 1 1472 ? 94.061  56.033  153.494 1.00 45.75  ? 1472 THR A OG1   1 
ATOM   140   C  CG2   . THR A 1 1472 ? 95.116  53.985  154.212 1.00 45.30  ? 1472 THR A CG2   1 
ATOM   141   N  N     . TYR A 1 1473 ? 93.963  56.058  150.060 1.00 43.05  ? 1473 TYR A N     1 
ATOM   142   C  CA    . TYR A 1 1473 ? 92.977  56.670  149.178 1.00 40.28  ? 1473 TYR A CA    1 
ATOM   143   C  C     . TYR A 1 1473 ? 92.692  55.754  147.997 1.00 43.53  ? 1473 TYR A C     1 
ATOM   144   O  O     . TYR A 1 1473 ? 93.599  55.401  147.238 1.00 42.00  ? 1473 TYR A O     1 
ATOM   145   C  CB    . TYR A 1 1473 ? 93.469  58.031  148.689 1.00 40.64  ? 1473 TYR A CB    1 
ATOM   146   C  CG    . TYR A 1 1473 ? 92.461  58.776  147.846 1.00 41.32  ? 1473 TYR A CG    1 
ATOM   147   C  CD1   . TYR A 1 1473 ? 91.382  59.422  148.431 1.00 44.49  ? 1473 TYR A CD1   1 
ATOM   148   C  CD2   . TYR A 1 1473 ? 92.592  58.838  146.467 1.00 45.02  ? 1473 TYR A CD2   1 
ATOM   149   C  CE1   . TYR A 1 1473 ? 90.458  60.105  147.665 1.00 44.57  ? 1473 TYR A CE1   1 
ATOM   150   C  CE2   . TYR A 1 1473 ? 91.673  59.517  145.693 1.00 45.76  ? 1473 TYR A CE2   1 
ATOM   151   C  CZ    . TYR A 1 1473 ? 90.609  60.150  146.297 1.00 44.08  ? 1473 TYR A CZ    1 
ATOM   152   O  OH    . TYR A 1 1473 ? 89.691  60.829  145.530 1.00 42.05  ? 1473 TYR A OH    1 
ATOM   153   N  N     . GLU A 1 1474 ? 91.427  55.375  147.845 1.00 45.47  ? 1474 GLU A N     1 
ATOM   154   C  CA    . GLU A 1 1474 ? 90.995  54.494  146.771 1.00 42.44  ? 1474 GLU A CA    1 
ATOM   155   C  C     . GLU A 1 1474 ? 90.094  55.266  145.824 1.00 46.02  ? 1474 GLU A C     1 
ATOM   156   O  O     . GLU A 1 1474 ? 89.156  55.937  146.265 1.00 49.75  ? 1474 GLU A O     1 
ATOM   157   C  CB    . GLU A 1 1474 ? 90.252  53.271  147.316 1.00 42.78  ? 1474 GLU A CB    1 
ATOM   158   C  CG    . GLU A 1 1474 ? 91.106  52.026  147.442 1.00 46.18  ? 1474 GLU A CG    1 
ATOM   159   C  CD    . GLU A 1 1474 ? 90.383  50.899  148.147 1.00 51.51  ? 1474 GLU A CD    1 
ATOM   160   O  OE1   . GLU A 1 1474 ? 89.148  50.991  148.306 1.00 60.60  ? 1474 GLU A OE1   1 
ATOM   161   O  OE2   . GLU A 1 1474 ? 91.049  49.916  148.536 1.00 52.66  ? 1474 GLU A OE2   1 
ATOM   162   N  N     . LEU A 1 1475 ? 90.388  55.177  144.530 1.00 40.03  ? 1475 LEU A N     1 
ATOM   163   C  CA    . LEU A 1 1475 ? 89.458  55.674  143.530 1.00 40.52  ? 1475 LEU A CA    1 
ATOM   164   C  C     . LEU A 1 1475 ? 88.119  54.961  143.689 1.00 43.92  ? 1475 LEU A C     1 
ATOM   165   O  O     . LEU A 1 1475 ? 88.065  53.746  143.898 1.00 40.46  ? 1475 LEU A O     1 
ATOM   166   C  CB    . LEU A 1 1475 ? 90.049  55.482  142.127 1.00 31.82  ? 1475 LEU A CB    1 
ATOM   167   C  CG    . LEU A 1 1475 ? 90.382  54.074  141.614 1.00 33.27  ? 1475 LEU A CG    1 
ATOM   168   C  CD1   . LEU A 1 1475 ? 89.179  53.360  141.036 1.00 40.62  ? 1475 LEU A CD1   1 
ATOM   169   C  CD2   . LEU A 1 1475 ? 91.525  54.108  140.603 1.00 28.14  ? 1475 LEU A CD2   1 
ATOM   170   N  N     . ASP A 1 1476 ? 87.033  55.727  143.632 1.00 41.41  ? 1476 ASP A N     1 
ATOM   171   C  CA    . ASP A 1 1476 ? 85.722  55.196  143.991 1.00 40.80  ? 1476 ASP A CA    1 
ATOM   172   C  C     . ASP A 1 1476 ? 85.054  54.620  142.748 1.00 41.86  ? 1476 ASP A C     1 
ATOM   173   O  O     . ASP A 1 1476 ? 84.964  55.286  141.708 1.00 41.58  ? 1476 ASP A O     1 
ATOM   174   C  CB    . ASP A 1 1476 ? 84.859  56.273  144.643 1.00 44.94  ? 1476 ASP A CB    1 
ATOM   175   C  CG    . ASP A 1 1476 ? 83.412  55.844  144.797 1.00 54.52  ? 1476 ASP A CG    1 
ATOM   176   O  OD1   . ASP A 1 1476 ? 82.512  56.649  144.486 1.00 55.58  ? 1476 ASP A OD1   1 
ATOM   177   O  OD2   . ASP A 1 1476 ? 83.174  54.696  145.227 1.00 54.18  ? 1476 ASP A OD2   1 
ATOM   178   N  N     . LEU A 1 1477 ? 84.595  53.377  142.858 1.00 38.25  ? 1477 LEU A N     1 
ATOM   179   C  CA    . LEU A 1 1477 ? 84.033  52.656  141.731 1.00 34.93  ? 1477 LEU A CA    1 
ATOM   180   C  C     . LEU A 1 1477 ? 82.520  52.515  141.875 1.00 43.53  ? 1477 LEU A C     1 
ATOM   181   O  O     . LEU A 1 1477 ? 81.964  52.525  142.976 1.00 46.33  ? 1477 LEU A O     1 
ATOM   182   C  CB    . LEU A 1 1477 ? 84.678  51.275  141.606 1.00 29.61  ? 1477 LEU A CB    1 
ATOM   183   C  CG    . LEU A 1 1477 ? 86.142  51.235  141.162 1.00 30.94  ? 1477 LEU A CG    1 
ATOM   184   C  CD1   . LEU A 1 1477 ? 86.729  49.845  141.355 1.00 39.47  ? 1477 LEU A CD1   1 
ATOM   185   C  CD2   . LEU A 1 1477 ? 86.278  51.677  139.717 1.00 27.82  ? 1477 LEU A CD2   1 
ATOM   186   N  N     . VAL A 1 1478 ? 81.857  52.387  140.729 1.00 40.37  ? 1478 VAL A N     1 
ATOM   187   C  CA    . VAL A 1 1478 ? 80.412  52.198  140.670 1.00 37.12  ? 1478 VAL A CA    1 
ATOM   188   C  C     . VAL A 1 1478 ? 80.081  51.202  139.565 1.00 36.02  ? 1478 VAL A C     1 
ATOM   189   O  O     . VAL A 1 1478 ? 80.656  51.253  138.471 1.00 31.49  ? 1478 VAL A O     1 
ATOM   190   C  CB    . VAL A 1 1478 ? 79.681  53.540  140.467 1.00 38.82  ? 1478 VAL A CB    1 
ATOM   191   C  CG1   . VAL A 1 1478 ? 80.048  54.173  139.129 1.00 32.36  ? 1478 VAL A CG1   1 
ATOM   192   C  CG2   . VAL A 1 1478 ? 78.176  53.345  140.571 1.00 37.94  ? 1478 VAL A CG2   1 
ATOM   193   N  N     . ASN A 1 1479 ? 79.172  50.273  139.852 1.00 39.55  ? 1479 ASN A N     1 
ATOM   194   C  CA    . ASN A 1 1479 ? 78.768  49.293  138.854 1.00 38.71  ? 1479 ASN A CA    1 
ATOM   195   C  C     . ASN A 1 1479 ? 78.041  49.976  137.704 1.00 38.57  ? 1479 ASN A C     1 
ATOM   196   O  O     . ASN A 1 1479 ? 77.138  50.790  137.914 1.00 34.03  ? 1479 ASN A O     1 
ATOM   197   C  CB    . ASN A 1 1479 ? 77.868  48.228  139.482 1.00 42.00  ? 1479 ASN A CB    1 
ATOM   198   C  CG    . ASN A 1 1479 ? 77.303  47.264  138.454 1.00 42.77  ? 1479 ASN A CG    1 
ATOM   199   O  OD1   . ASN A 1 1479 ? 78.048  46.609  137.727 1.00 41.91  ? 1479 ASN A OD1   1 
ATOM   200   N  ND2   . ASN A 1 1479 ? 75.979  47.174  138.391 1.00 43.06  ? 1479 ASN A ND2   1 
ATOM   201   N  N     . TYR A 1 1480 ? 78.443  49.644  136.480 1.00 33.82  ? 1480 TYR A N     1 
ATOM   202   C  CA    . TYR A 1 1480 ? 77.831  50.191  135.275 1.00 34.37  ? 1480 TYR A CA    1 
ATOM   203   C  C     . TYR A 1 1480 ? 77.235  49.017  134.504 1.00 37.56  ? 1480 TYR A C     1 
ATOM   204   O  O     . TYR A 1 1480 ? 77.975  48.180  133.959 1.00 33.43  ? 1480 TYR A O     1 
ATOM   205   C  CB    . TYR A 1 1480 ? 78.837  50.968  134.431 1.00 29.92  ? 1480 TYR A CB    1 
ATOM   206   C  CG    . TYR A 1 1480 ? 78.254  51.490  133.136 1.00 28.20  ? 1480 TYR A CG    1 
ATOM   207   C  CD1   . TYR A 1 1480 ? 77.515  52.667  133.119 1.00 28.06  ? 1480 TYR A CD1   1 
ATOM   208   C  CD2   . TYR A 1 1480 ? 78.421  50.807  131.941 1.00 27.22  ? 1480 TYR A CD2   1 
ATOM   209   C  CE1   . TYR A 1 1480 ? 76.974  53.155  131.948 1.00 25.96  ? 1480 TYR A CE1   1 
ATOM   210   C  CE2   . TYR A 1 1480 ? 77.881  51.287  130.763 1.00 28.27  ? 1480 TYR A CE2   1 
ATOM   211   C  CZ    . TYR A 1 1480 ? 77.159  52.463  130.773 1.00 27.59  ? 1480 TYR A CZ    1 
ATOM   212   O  OH    . TYR A 1 1480 ? 76.616  52.948  129.605 1.00 29.00  ? 1480 TYR A OH    1 
ATOM   213   N  N     . GLN A 1 1481 ? 75.893  48.965  134.529 1.00 36.43  ? 1481 GLN A N     1 
ATOM   214   C  CA    . GLN A 1 1481 ? 75.055  48.033  133.762 1.00 37.04  ? 1481 GLN A CA    1 
ATOM   215   C  C     . GLN A 1 1481 ? 75.577  46.601  133.803 1.00 38.75  ? 1481 GLN A C     1 
ATOM   216   O  O     . GLN A 1 1481 ? 75.486  45.865  132.818 1.00 40.98  ? 1481 GLN A O     1 
ATOM   217   C  CB    . GLN A 1 1481 ? 74.880  48.507  132.318 1.00 33.90  ? 1481 GLN A CB    1 
ATOM   218   C  CG    . GLN A 1 1481 ? 74.469  49.963  132.192 1.00 30.05  ? 1481 GLN A CG    1 
ATOM   219   C  CD    . GLN A 1 1481 ? 74.527  50.466  130.765 1.00 30.04  ? 1481 GLN A CD    1 
ATOM   220   O  OE1   . GLN A 1 1481 ? 74.899  49.731  129.851 1.00 37.59  ? 1481 GLN A OE1   1 
ATOM   221   N  NE2   . GLN A 1 1481 ? 74.148  51.722  130.564 1.00 32.88  ? 1481 GLN A NE2   1 
ATOM   222   N  N     . ASN A 1 1482 ? 76.143  46.210  134.946 1.00 35.60  ? 1482 ASN A N     1 
ATOM   223   C  CA    . ASN A 1 1482 ? 76.724  44.883  135.133 1.00 39.11  ? 1482 ASN A CA    1 
ATOM   224   C  C     . ASN A 1 1482 ? 77.857  44.652  134.141 1.00 36.90  ? 1482 ASN A C     1 
ATOM   225   O  O     . ASN A 1 1482 ? 78.429  43.559  134.081 1.00 37.99  ? 1482 ASN A O     1 
ATOM   226   C  CB    . ASN A 1 1482 ? 75.658  43.791  134.999 1.00 41.51  ? 1482 ASN A CB    1 
ATOM   227   C  CG    . ASN A 1 1482 ? 74.683  43.783  136.159 1.00 51.35  ? 1482 ASN A CG    1 
ATOM   228   O  OD1   . ASN A 1 1482 ? 74.536  44.778  136.868 1.00 46.81  ? 1482 ASN A OD1   1 
ATOM   229   N  ND2   . ASN A 1 1482 ? 74.012  42.655  136.360 1.00 48.90  ? 1482 ASN A ND2   1 
ATOM   230   N  N     . LYS A 1 1483 ? 78.185  45.680  133.356 1.00 38.09  ? 1483 LYS A N     1 
ATOM   231   C  CA    . LYS A 1 1483 ? 79.251  45.559  132.375 1.00 35.31  ? 1483 LYS A CA    1 
ATOM   232   C  C     . LYS A 1 1483 ? 80.614  45.833  132.987 1.00 38.40  ? 1483 LYS A C     1 
ATOM   233   O  O     . LYS A 1 1483 ? 81.584  45.148  132.640 1.00 38.01  ? 1483 LYS A O     1 
ATOM   234   C  CB    . LYS A 1 1483 ? 79.005  46.501  131.195 1.00 36.85  ? 1483 LYS A CB    1 
ATOM   235   C  CG    . LYS A 1 1483 ? 77.686  46.290  130.472 1.00 43.02  ? 1483 LYS A CG    1 
ATOM   236   C  CD    . LYS A 1 1483 ? 77.446  47.392  129.450 1.00 40.07  ? 1483 LYS A CD    1 
ATOM   237   C  CE    . LYS A 1 1483 ? 76.248  47.085  128.566 1.00 40.08  ? 1483 LYS A CE    1 
ATOM   238   N  NZ    . LYS A 1 1483 ? 76.464  45.866  127.738 1.00 43.77  ? 1483 LYS A NZ    1 
ATOM   239   N  N     . CYS A 1 1484 ? 80.723  46.802  133.894 1.00 34.47  ? 1484 CYS A N     1 
ATOM   240   C  CA    . CYS A 1 1484 ? 82.023  47.011  134.533 1.00 30.26  ? 1484 CYS A CA    1 
ATOM   241   C  C     . CYS A 1 1484 ? 81.834  47.803  135.818 1.00 32.56  ? 1484 CYS A C     1 
ATOM   242   O  O     . CYS A 1 1484 ? 80.723  47.944  136.334 1.00 34.72  ? 1484 CYS A O     1 
ATOM   243   C  CB    . CYS A 1 1484 ? 83.010  47.734  133.616 1.00 31.21  ? 1484 CYS A CB    1 
ATOM   244   S  SG    . CYS A 1 1484 ? 82.510  49.398  133.143 1.00 37.73  ? 1484 CYS A SG    1 
ATOM   245   N  N     . ARG A 1 1485 ? 82.951  48.302  136.342 1.00 33.15  ? 1485 ARG A N     1 
ATOM   246   C  CA    . ARG A 1 1485 ? 82.979  49.206  137.487 1.00 30.80  ? 1485 ARG A CA    1 
ATOM   247   C  C     . ARG A 1 1485 ? 83.722  50.464  137.045 1.00 31.80  ? 1485 ARG A C     1 
ATOM   248   O  O     . ARG A 1 1485 ? 84.955  50.473  136.970 1.00 41.28  ? 1485 ARG A O     1 
ATOM   249   C  CB    . ARG A 1 1485 ? 83.643  48.547  138.693 1.00 33.49  ? 1485 ARG A CB    1 
ATOM   250   C  CG    . ARG A 1 1485 ? 82.868  47.370  139.269 1.00 35.55  ? 1485 ARG A CG    1 
ATOM   251   C  CD    . ARG A 1 1485 ? 83.607  46.742  140.442 1.00 47.79  ? 1485 ARG A CD    1 
ATOM   252   N  NE    . ARG A 1 1485 ? 83.689  47.649  141.581 1.00 46.06  ? 1485 ARG A NE    1 
ATOM   253   C  CZ    . ARG A 1 1485 ? 84.413  47.424  142.669 1.00 46.45  ? 1485 ARG A CZ    1 
ATOM   254   N  NH1   . ARG A 1 1485 ? 85.133  46.323  142.806 1.00 49.51  ? 1485 ARG A NH1   1 
ATOM   255   N  NH2   . ARG A 1 1485 ? 84.415  48.328  143.645 1.00 42.95  ? 1485 ARG A NH2   1 
ATOM   256   N  N     . LEU A 1 1486 ? 82.969  51.517  136.745 1.00 23.89  ? 1486 LEU A N     1 
ATOM   257   C  CA    . LEU A 1 1486 ? 83.562  52.775  136.318 1.00 24.11  ? 1486 LEU A CA    1 
ATOM   258   C  C     . LEU A 1 1486 ? 83.999  53.600  137.526 1.00 22.03  ? 1486 LEU A C     1 
ATOM   259   O  O     . LEU A 1 1486 ? 83.638  53.316  138.668 1.00 25.32  ? 1486 LEU A O     1 
ATOM   260   C  CB    . LEU A 1 1486 ? 82.575  53.574  135.470 1.00 24.02  ? 1486 LEU A CB    1 
ATOM   261   C  CG    . LEU A 1 1486 ? 82.268  53.014  134.082 1.00 19.85  ? 1486 LEU A CG    1 
ATOM   262   C  CD1   . LEU A 1 1486 ? 81.281  53.910  133.359 1.00 17.54  ? 1486 LEU A CD1   1 
ATOM   263   C  CD2   . LEU A 1 1486 ? 83.548  52.867  133.277 1.00 21.32  ? 1486 LEU A CD2   1 
ATOM   264   N  N     . ILE A 1 1487 ? 84.789  54.636  137.262 1.00 21.77  ? 1487 ILE A N     1 
ATOM   265   C  CA    . ILE A 1 1487 ? 85.285  55.517  138.314 1.00 23.23  ? 1487 ILE A CA    1 
ATOM   266   C  C     . ILE A 1 1487 ? 84.419  56.766  138.390 1.00 23.44  ? 1487 ILE A C     1 
ATOM   267   O  O     . ILE A 1 1487 ? 84.141  57.406  137.368 1.00 31.08  ? 1487 ILE A O     1 
ATOM   268   C  CB    . ILE A 1 1487 ? 86.757  55.892  138.078 1.00 20.19  ? 1487 ILE A CB    1 
ATOM   269   C  CG1   . ILE A 1 1487 ? 87.641  54.658  138.219 1.00 24.15  ? 1487 ILE A CG1   1 
ATOM   270   C  CG2   . ILE A 1 1487 ? 87.190  56.974  139.053 1.00 19.39  ? 1487 ILE A CG2   1 
ATOM   271   C  CD1   . ILE A 1 1487 ? 89.080  54.889  137.853 1.00 19.37  ? 1487 ILE A CD1   1 
ATOM   272   N  N     . ARG A 1 1488 ? 83.989  57.115  139.599 1.00 21.80  ? 1488 ARG A N     1 
ATOM   273   C  CA    . ARG A 1 1488 ? 83.332  58.392  139.847 1.00 27.87  ? 1488 ARG A CA    1 
ATOM   274   C  C     . ARG A 1 1488 ? 84.130  59.172  140.891 1.00 28.22  ? 1488 ARG A C     1 
ATOM   275   O  O     . ARG A 1 1488 ? 85.221  58.767  141.300 1.00 29.03  ? 1488 ARG A O     1 
ATOM   276   C  CB    . ARG A 1 1488 ? 81.879  58.199  140.292 1.00 31.49  ? 1488 ARG A CB    1 
ATOM   277   C  CG    . ARG A 1 1488 ? 81.734  57.512  141.631 1.00 36.52  ? 1488 ARG A CG    1 
ATOM   278   C  CD    . ARG A 1 1488 ? 80.278  57.282  142.024 1.00 48.49  ? 1488 ARG A CD    1 
ATOM   279   N  NE    . ARG A 1 1488 ? 80.178  56.625  143.323 1.00 62.42  ? 1488 ARG A NE    1 
ATOM   280   C  CZ    . ARG A 1 1488 ? 79.040  56.313  143.928 1.00 65.61  ? 1488 ARG A CZ    1 
ATOM   281   N  NH1   . ARG A 1 1488 ? 77.867  56.594  143.385 1.00 65.01  ? 1488 ARG A NH1   1 
ATOM   282   N  NH2   . ARG A 1 1488 ? 79.080  55.702  145.109 1.00 71.48  ? 1488 ARG A NH2   1 
ATOM   283   N  N     . GLY A 1 1489 ? 83.574  60.296  141.331 1.00 27.88  ? 1489 GLY A N     1 
ATOM   284   C  CA    . GLY A 1 1489 ? 84.282  61.151  142.270 1.00 33.82  ? 1489 GLY A CA    1 
ATOM   285   C  C     . GLY A 1 1489 ? 85.502  61.841  141.697 1.00 31.10  ? 1489 GLY A C     1 
ATOM   286   O  O     . GLY A 1 1489 ? 86.571  61.822  142.319 1.00 33.55  ? 1489 GLY A O     1 
ATOM   287   N  N     . TRP A 1 1490 ? 85.373  62.435  140.510 1.00 29.37  ? 1490 TRP A N     1 
ATOM   288   C  CA    . TRP A 1 1490 ? 86.523  63.057  139.861 1.00 25.32  ? 1490 TRP A CA    1 
ATOM   289   C  C     . TRP A 1 1490 ? 86.916  64.367  140.536 1.00 34.80  ? 1490 TRP A C     1 
ATOM   290   O  O     . TRP A 1 1490 ? 88.108  64.673  140.671 1.00 35.17  ? 1490 TRP A O     1 
ATOM   291   C  CB    . TRP A 1 1490 ? 86.224  63.279  138.381 1.00 23.95  ? 1490 TRP A CB    1 
ATOM   292   C  CG    . TRP A 1 1490 ? 86.214  62.015  137.602 1.00 20.14  ? 1490 TRP A CG    1 
ATOM   293   C  CD1   . TRP A 1 1490 ? 85.125  61.321  137.165 1.00 18.72  ? 1490 TRP A CD1   1 
ATOM   294   C  CD2   . TRP A 1 1490 ? 87.357  61.261  137.200 1.00 24.79  ? 1490 TRP A CD2   1 
ATOM   295   N  NE1   . TRP A 1 1490 ? 85.524  60.193  136.492 1.00 18.46  ? 1490 TRP A NE1   1 
ATOM   296   C  CE2   . TRP A 1 1490 ? 86.892  60.133  136.502 1.00 20.83  ? 1490 TRP A CE2   1 
ATOM   297   C  CE3   . TRP A 1 1490 ? 88.733  61.437  137.354 1.00 23.83  ? 1490 TRP A CE3   1 
ATOM   298   C  CZ2   . TRP A 1 1490 ? 87.755  59.189  135.960 1.00 14.96  ? 1490 TRP A CZ2   1 
ATOM   299   C  CZ3   . TRP A 1 1490 ? 89.586  60.501  136.816 1.00 21.15  ? 1490 TRP A CZ3   1 
ATOM   300   C  CH2   . TRP A 1 1490 ? 89.094  59.395  136.130 1.00 15.24  ? 1490 TRP A CH2   1 
ATOM   301   N  N     . ASP A 1 1491 ? 85.928  65.167  140.948 1.00 32.84  ? 1491 ASP A N     1 
ATOM   302   C  CA    . ASP A 1 1491 ? 86.245  66.462  141.543 1.00 30.99  ? 1491 ASP A CA    1 
ATOM   303   C  C     . ASP A 1 1491 ? 87.072  66.288  142.811 1.00 34.22  ? 1491 ASP A C     1 
ATOM   304   O  O     . ASP A 1 1491 ? 88.054  67.004  143.027 1.00 36.91  ? 1491 ASP A O     1 
ATOM   305   C  CB    . ASP A 1 1491 ? 84.963  67.263  141.813 1.00 36.71  ? 1491 ASP A CB    1 
ATOM   306   C  CG    . ASP A 1 1491 ? 84.082  66.642  142.884 1.00 48.88  ? 1491 ASP A CG    1 
ATOM   307   O  OD1   . ASP A 1 1491 ? 83.201  67.354  143.414 1.00 46.16  ? 1491 ASP A OD1   1 
ATOM   308   O  OD2   . ASP A 1 1491 ? 84.243  65.439  143.173 1.00 50.02  ? 1491 ASP A OD2   1 
ATOM   309   N  N     . ASP A 1 1492 ? 86.715  65.304  143.639 1.00 34.17  ? 1492 ASP A N     1 
ATOM   310   C  CA    . ASP A 1 1492 ? 87.452  65.068  144.877 1.00 35.01  ? 1492 ASP A CA    1 
ATOM   311   C  C     . ASP A 1 1492 ? 88.890  64.643  144.598 1.00 34.92  ? 1492 ASP A C     1 
ATOM   312   O  O     . ASP A 1 1492 ? 89.831  65.162  145.210 1.00 32.38  ? 1492 ASP A O     1 
ATOM   313   C  CB    . ASP A 1 1492 ? 86.726  64.015  145.715 1.00 36.39  ? 1492 ASP A CB    1 
ATOM   314   C  CG    . ASP A 1 1492 ? 85.232  64.263  145.793 1.00 45.16  ? 1492 ASP A CG    1 
ATOM   315   O  OD1   . ASP A 1 1492 ? 84.835  65.337  146.290 1.00 50.00  ? 1492 ASP A OD1   1 
ATOM   316   O  OD2   . ASP A 1 1492 ? 84.455  63.390  145.351 1.00 50.90  ? 1492 ASP A OD2   1 
ATOM   317   N  N     . LEU A 1 1493 ? 89.082  63.702  143.670 1.00 35.35  ? 1493 LEU A N     1 
ATOM   318   C  CA    . LEU A 1 1493 ? 90.424  63.211  143.370 1.00 29.31  ? 1493 LEU A CA    1 
ATOM   319   C  C     . LEU A 1 1493 ? 91.304  64.320  142.809 1.00 27.95  ? 1493 LEU A C     1 
ATOM   320   O  O     . LEU A 1 1493 ? 92.442  64.521  143.259 1.00 31.78  ? 1493 LEU A O     1 
ATOM   321   C  CB    . LEU A 1 1493 ? 90.341  62.037  142.391 1.00 30.05  ? 1493 LEU A CB    1 
ATOM   322   C  CG    . LEU A 1 1493 ? 91.619  61.576  141.687 1.00 32.78  ? 1493 LEU A CG    1 
ATOM   323   C  CD1   . LEU A 1 1493 ? 92.643  61.032  142.671 1.00 31.31  ? 1493 LEU A CD1   1 
ATOM   324   C  CD2   . LEU A 1 1493 ? 91.277  60.533  140.638 1.00 24.91  ? 1493 LEU A CD2   1 
ATOM   325   N  N     . PHE A 1 1494 ? 90.786  65.061  141.826 1.00 28.71  ? 1494 PHE A N     1 
ATOM   326   C  CA    . PHE A 1 1494 ? 91.571  66.140  141.238 1.00 25.69  ? 1494 PHE A CA    1 
ATOM   327   C  C     . PHE A 1 1494 ? 91.861  67.238  142.253 1.00 30.84  ? 1494 PHE A C     1 
ATOM   328   O  O     . PHE A 1 1494 ? 92.964  67.791  142.269 1.00 28.61  ? 1494 PHE A O     1 
ATOM   329   C  CB    . PHE A 1 1494 ? 90.863  66.705  140.006 1.00 25.73  ? 1494 PHE A CB    1 
ATOM   330   C  CG    . PHE A 1 1494 ? 90.844  65.763  138.835 1.00 28.47  ? 1494 PHE A CG    1 
ATOM   331   C  CD1   . PHE A 1 1494 ? 89.678  65.542  138.123 1.00 26.74  ? 1494 PHE A CD1   1 
ATOM   332   C  CD2   . PHE A 1 1494 ? 91.998  65.106  138.442 1.00 29.85  ? 1494 PHE A CD2   1 
ATOM   333   C  CE1   . PHE A 1 1494 ? 89.664  64.679  137.044 1.00 23.35  ? 1494 PHE A CE1   1 
ATOM   334   C  CE2   . PHE A 1 1494 ? 91.989  64.242  137.364 1.00 22.57  ? 1494 PHE A CE2   1 
ATOM   335   C  CZ    . PHE A 1 1494 ? 90.821  64.030  136.664 1.00 20.65  ? 1494 PHE A CZ    1 
ATOM   336   N  N     . ASN A 1 1495 ? 90.893  67.567  143.113 1.00 31.49  ? 1495 ASN A N     1 
ATOM   337   C  CA    . ASN A 1 1495 ? 91.128  68.588  144.129 1.00 32.47  ? 1495 ASN A CA    1 
ATOM   338   C  C     . ASN A 1 1495 ? 92.199  68.144  145.117 1.00 29.32  ? 1495 ASN A C     1 
ATOM   339   O  O     . ASN A 1 1495 ? 93.058  68.938  145.518 1.00 32.19  ? 1495 ASN A O     1 
ATOM   340   C  CB    . ASN A 1 1495 ? 89.822  68.917  144.852 1.00 29.82  ? 1495 ASN A CB    1 
ATOM   341   C  CG    . ASN A 1 1495 ? 88.846  69.675  143.974 1.00 34.33  ? 1495 ASN A CG    1 
ATOM   342   O  OD1   . ASN A 1 1495 ? 89.245  70.385  143.052 1.00 39.50  ? 1495 ASN A OD1   1 
ATOM   343   N  ND2   . ASN A 1 1495 ? 87.557  69.518  144.250 1.00 36.86  ? 1495 ASN A ND2   1 
ATOM   344   N  N     . LYS A 1 1496 ? 92.160  66.873  145.528 1.00 29.47  ? 1496 LYS A N     1 
ATOM   345   C  CA    . LYS A 1 1496 ? 93.181  66.359  146.433 1.00 31.77  ? 1496 LYS A CA    1 
ATOM   346   C  C     . LYS A 1 1496 ? 94.563  66.437  145.798 1.00 32.07  ? 1496 LYS A C     1 
ATOM   347   O  O     . LYS A 1 1496 ? 95.527  66.886  146.437 1.00 34.45  ? 1496 LYS A O     1 
ATOM   348   C  CB    . LYS A 1 1496 ? 92.852  64.919  146.827 1.00 29.81  ? 1496 LYS A CB    1 
ATOM   349   C  CG    . LYS A 1 1496 ? 93.822  64.299  147.819 1.00 35.69  ? 1496 LYS A CG    1 
ATOM   350   C  CD    . LYS A 1 1496 ? 93.783  65.026  149.151 1.00 42.29  ? 1496 LYS A CD    1 
ATOM   351   C  CE    . LYS A 1 1496 ? 92.468  64.778  149.873 1.00 43.33  ? 1496 LYS A CE    1 
ATOM   352   N  NZ    . LYS A 1 1496 ? 92.431  65.432  151.210 1.00 44.92  ? 1496 LYS A NZ    1 
ATOM   353   N  N     . VAL A 1 1497 ? 94.675  66.023  144.532 1.00 30.26  ? 1497 VAL A N     1 
ATOM   354   C  CA    . VAL A 1 1497 ? 95.965  66.088  143.847 1.00 28.36  ? 1497 VAL A CA    1 
ATOM   355   C  C     . VAL A 1 1497 ? 96.442  67.532  143.747 1.00 31.63  ? 1497 VAL A C     1 
ATOM   356   O  O     . VAL A 1 1497 ? 97.608  67.836  144.021 1.00 30.47  ? 1497 VAL A O     1 
ATOM   357   C  CB    . VAL A 1 1497 ? 95.882  65.422  142.461 1.00 25.36  ? 1497 VAL A CB    1 
ATOM   358   C  CG1   . VAL A 1 1497 ? 97.230  65.498  141.763 1.00 23.84  ? 1497 VAL A CG1   1 
ATOM   359   C  CG2   . VAL A 1 1497 ? 95.453  63.975  142.594 1.00 25.69  ? 1497 VAL A CG2   1 
ATOM   360   N  N     . LYS A 1 1498 ? 95.543  68.445  143.364 1.00 31.78  ? 1498 LYS A N     1 
ATOM   361   C  CA    . LYS A 1 1498 ? 95.927  69.846  143.217 1.00 31.82  ? 1498 LYS A CA    1 
ATOM   362   C  C     . LYS A 1 1498 ? 96.404  70.436  144.535 1.00 34.27  ? 1498 LYS A C     1 
ATOM   363   O  O     . LYS A 1 1498 ? 97.406  71.158  144.570 1.00 36.61  ? 1498 LYS A O     1 
ATOM   364   C  CB    . LYS A 1 1498 ? 94.763  70.672  142.668 1.00 35.11  ? 1498 LYS A CB    1 
ATOM   365   C  CG    . LYS A 1 1498 ? 94.368  70.345  141.244 1.00 41.76  ? 1498 LYS A CG    1 
ATOM   366   C  CD    . LYS A 1 1498 ? 93.245  71.242  140.754 1.00 44.83  ? 1498 LYS A CD    1 
ATOM   367   C  CE    . LYS A 1 1498 ? 92.804  70.848  139.355 1.00 45.39  ? 1498 LYS A CE    1 
ATOM   368   N  NZ    . LYS A 1 1498 ? 93.864  71.120  138.345 1.00 44.83  ? 1498 LYS A NZ    1 
ATOM   369   N  N     . GLU A 1 1499 ? 95.705  70.145  145.633 1.00 30.81  ? 1499 GLU A N     1 
ATOM   370   C  CA    . GLU A 1 1499 ? 96.067  70.784  146.893 1.00 34.47  ? 1499 GLU A CA    1 
ATOM   371   C  C     . GLU A 1 1499 ? 97.332  70.169  147.488 1.00 35.14  ? 1499 GLU A C     1 
ATOM   372   O  O     . GLU A 1 1499 ? 98.130  70.877  148.114 1.00 39.92  ? 1499 GLU A O     1 
ATOM   373   C  CB    . GLU A 1 1499 ? 94.874  70.758  147.856 1.00 31.10  ? 1499 GLU A CB    1 
ATOM   374   C  CG    . GLU A 1 1499 ? 94.437  69.421  148.429 1.00 38.25  ? 1499 GLU A CG    1 
ATOM   375   C  CD    . GLU A 1 1499 ? 95.191  69.028  149.680 1.00 46.94  ? 1499 GLU A CD    1 
ATOM   376   O  OE1   . GLU A 1 1499 ? 95.015  67.879  150.130 1.00 48.15  ? 1499 GLU A OE1   1 
ATOM   377   O  OE2   . GLU A 1 1499 ? 95.950  69.864  150.213 1.00 46.01  ? 1499 GLU A OE2   1 
ATOM   378   N  N     . HIS A 1 1500 ? 97.575  68.874  147.255 1.00 32.57  ? 1500 HIS A N     1 
ATOM   379   C  CA    . HIS A 1 1500 ? 98.876  68.319  147.629 1.00 32.99  ? 1500 HIS A CA    1 
ATOM   380   C  C     . HIS A 1 1500 ? 100.008 68.902  146.787 1.00 37.57  ? 1500 HIS A C     1 
ATOM   381   O  O     . HIS A 1 1500 ? 101.097 69.168  147.312 1.00 42.81  ? 1500 HIS A O     1 
ATOM   382   C  CB    . HIS A 1 1500 ? 98.857  66.794  147.542 1.00 30.84  ? 1500 HIS A CB    1 
ATOM   383   C  CG    . HIS A 1 1500 ? 98.113  66.142  148.664 1.00 37.45  ? 1500 HIS A CG    1 
ATOM   384   N  ND1   . HIS A 1 1500 ? 97.987  64.776  148.781 1.00 36.19  ? 1500 HIS A ND1   1 
ATOM   385   C  CD2   . HIS A 1 1500 ? 97.512  66.668  149.756 1.00 36.55  ? 1500 HIS A CD2   1 
ATOM   386   C  CE1   . HIS A 1 1500 ? 97.304  64.489  149.874 1.00 34.81  ? 1500 HIS A CE1   1 
ATOM   387   N  NE2   . HIS A 1 1500 ? 97.003  65.621  150.484 1.00 35.50  ? 1500 HIS A NE2   1 
ATOM   388   N  N     . ILE A 1 1501 ? 99.782  69.110  145.487 1.00 38.04  ? 1501 ILE A N     1 
ATOM   389   C  CA    . ILE A 1 1501 ? 100.808 69.745  144.661 1.00 34.78  ? 1501 ILE A CA    1 
ATOM   390   C  C     . ILE A 1 1501 ? 101.082 71.162  145.147 1.00 42.45  ? 1501 ILE A C     1 
ATOM   391   O  O     . ILE A 1 1501 ? 102.236 71.603  145.205 1.00 45.77  ? 1501 ILE A O     1 
ATOM   392   C  CB    . ILE A 1 1501 ? 100.406 69.723  143.174 1.00 30.27  ? 1501 ILE A CB    1 
ATOM   393   C  CG1   . ILE A 1 1501 ? 100.303 68.285  142.664 1.00 31.79  ? 1501 ILE A CG1   1 
ATOM   394   C  CG2   . ILE A 1 1501 ? 101.403 70.508  142.336 1.00 32.96  ? 1501 ILE A CG2   1 
ATOM   395   C  CD1   . ILE A 1 1501 ? 99.894  68.179  141.212 1.00 25.87  ? 1501 ILE A CD1   1 
ATOM   396   N  N     . ASN A 1 1502 ? 100.026 71.900  145.496 1.00 39.88  ? 1502 ASN A N     1 
ATOM   397   C  CA    . ASN A 1 1502 ? 100.205 73.253  146.011 1.00 39.34  ? 1502 ASN A CA    1 
ATOM   398   C  C     . ASN A 1 1502 ? 100.978 73.249  147.324 1.00 48.09  ? 1502 ASN A C     1 
ATOM   399   O  O     . ASN A 1 1502 ? 101.851 74.096  147.536 1.00 53.35  ? 1502 ASN A O     1 
ATOM   400   C  CB    . ASN A 1 1502 ? 98.850  73.939  146.186 1.00 39.23  ? 1502 ASN A CB    1 
ATOM   401   C  CG    . ASN A 1 1502 ? 98.069  74.025  144.891 1.00 50.00  ? 1502 ASN A CG    1 
ATOM   402   O  OD1   . ASN A 1 1502 ? 98.648  74.094  143.807 1.00 52.34  ? 1502 ASN A OD1   1 
ATOM   403   N  ND2   . ASN A 1 1502 ? 96.745  74.022  144.997 1.00 52.32  ? 1502 ASN A ND2   1 
ATOM   404   N  N     . SER A 1 1503 ? 100.674 72.303  148.217 1.00 42.83  ? 1503 SER A N     1 
ATOM   405   C  CA    . SER A 1 1503 ? 101.418 72.213  149.471 1.00 41.95  ? 1503 SER A CA    1 
ATOM   406   C  C     . SER A 1 1503 ? 102.888 71.894  149.224 1.00 50.28  ? 1503 SER A C     1 
ATOM   407   O  O     . SER A 1 1503 ? 103.776 72.482  149.857 1.00 57.60  ? 1503 SER A O     1 
ATOM   408   C  CB    . SER A 1 1503 ? 100.786 71.160  150.381 1.00 36.59  ? 1503 SER A CB    1 
ATOM   409   O  OG    . SER A 1 1503 ? 100.973 69.857  149.858 1.00 43.61  ? 1503 SER A OG    1 
ATOM   410   N  N     . VAL A 1 1504 ? 103.165 70.964  148.305 1.00 46.00  ? 1504 VAL A N     1 
ATOM   411   C  CA    . VAL A 1 1504 ? 104.547 70.595  148.005 1.00 46.51  ? 1504 VAL A CA    1 
ATOM   412   C  C     . VAL A 1 1504 ? 105.298 71.777  147.406 1.00 56.42  ? 1504 VAL A C     1 
ATOM   413   O  O     . VAL A 1 1504 ? 106.462 72.028  147.740 1.00 64.60  ? 1504 VAL A O     1 
ATOM   414   C  CB    . VAL A 1 1504 ? 104.580 69.365  147.078 1.00 43.37  ? 1504 VAL A CB    1 
ATOM   415   C  CG1   . VAL A 1 1504 ? 105.957 69.197  146.453 1.00 50.03  ? 1504 VAL A CG1   1 
ATOM   416   C  CG2   . VAL A 1 1504 ? 104.188 68.113  147.847 1.00 39.69  ? 1504 VAL A CG2   1 
ATOM   417   N  N     . SER A 1 1505 ? 104.649 72.519  146.507 1.00 55.86  ? 1505 SER A N     1 
ATOM   418   C  CA    . SER A 1 1505 ? 105.283 73.698  145.926 1.00 59.85  ? 1505 SER A CA    1 
ATOM   419   C  C     . SER A 1 1505 ? 105.515 74.778  146.976 1.00 61.47  ? 1505 SER A C     1 
ATOM   420   O  O     . SER A 1 1505 ? 106.550 75.454  146.960 1.00 65.26  ? 1505 SER A O     1 
ATOM   421   C  CB    . SER A 1 1505 ? 104.430 74.238  144.777 1.00 55.53  ? 1505 SER A CB    1 
ATOM   422   O  OG    . SER A 1 1505 ? 105.163 75.154  143.984 1.00 65.52  ? 1505 SER A OG    1 
ATOM   423   N  N     . ALA A 1 1506 ? 104.564 74.953  147.896 1.00 57.65  ? 1506 ALA A N     1 
ATOM   424   C  CA    . ALA A 1 1506 ? 104.677 76.010  148.895 1.00 63.52  ? 1506 ALA A CA    1 
ATOM   425   C  C     . ALA A 1 1506 ? 105.765 75.706  149.915 1.00 65.66  ? 1506 ALA A C     1 
ATOM   426   O  O     . ALA A 1 1506 ? 106.470 76.617  150.364 1.00 68.60  ? 1506 ALA A O     1 
ATOM   427   C  CB    . ALA A 1 1506 ? 103.332 76.218  149.591 1.00 59.94  ? 1506 ALA A CB    1 
ATOM   428   N  N     . MET A 1 1507 ? 105.919 74.436  150.301 1.00 61.47  ? 1507 MET A N     1 
ATOM   429   C  CA    . MET A 1 1507 ? 106.941 74.112  151.291 1.00 64.55  ? 1507 MET A CA    1 
ATOM   430   C  C     . MET A 1 1507 ? 108.357 74.293  150.758 1.00 71.15  ? 1507 MET A C     1 
ATOM   431   O  O     . MET A 1 1507 ? 109.298 74.316  151.558 1.00 75.77  ? 1507 MET A O     1 
ATOM   432   C  CB    . MET A 1 1507 ? 106.766 72.684  151.814 1.00 64.75  ? 1507 MET A CB    1 
ATOM   433   C  CG    . MET A 1 1507 ? 106.962 71.594  150.782 1.00 61.13  ? 1507 MET A CG    1 
ATOM   434   S  SD    . MET A 1 1507 ? 106.642 69.954  151.458 1.00 82.11  ? 1507 MET A SD    1 
ATOM   435   C  CE    . MET A 1 1507 ? 104.857 69.971  151.597 1.00 56.63  ? 1507 MET A CE    1 
ATOM   436   N  N     . LYS A 1 1508 ? 108.533 74.420  149.440 1.00 68.55  ? 1508 LYS A N     1 
ATOM   437   C  CA    . LYS A 1 1508 ? 109.851 74.745  148.904 1.00 73.00  ? 1508 LYS A CA    1 
ATOM   438   C  C     . LYS A 1 1508 ? 110.293 76.144  149.315 1.00 77.11  ? 1508 LYS A C     1 
ATOM   439   O  O     . LYS A 1 1508 ? 111.496 76.401  149.436 1.00 77.11  ? 1508 LYS A O     1 
ATOM   440   C  CB    . LYS A 1 1508 ? 109.852 74.621  147.380 1.00 69.37  ? 1508 LYS A CB    1 
ATOM   441   C  CG    . LYS A 1 1508 ? 109.320 73.299  146.854 1.00 68.97  ? 1508 LYS A CG    1 
ATOM   442   C  CD    . LYS A 1 1508 ? 109.156 73.340  145.343 1.00 73.19  ? 1508 LYS A CD    1 
ATOM   443   C  CE    . LYS A 1 1508 ? 108.521 72.062  144.818 1.00 70.63  ? 1508 LYS A CE    1 
ATOM   444   N  NZ    . LYS A 1 1508 ? 108.296 72.120  143.347 1.00 71.13  ? 1508 LYS A NZ    1 
ATOM   445   N  N     . LEU A 1 1509 ? 109.342 77.056  149.529 1.00 75.12  ? 1509 LEU A N     1 
ATOM   446   C  CA    . LEU A 1 1509 ? 109.691 78.415  149.930 1.00 77.14  ? 1509 LEU A CA    1 
ATOM   447   C  C     . LEU A 1 1509 ? 110.266 78.458  151.340 1.00 76.84  ? 1509 LEU A C     1 
ATOM   448   O  O     . LEU A 1 1509 ? 111.032 79.372  151.666 1.00 77.93  ? 1509 LEU A O     1 
ATOM   449   C  CB    . LEU A 1 1509 ? 108.464 79.322  149.829 1.00 74.91  ? 1509 LEU A CB    1 
ATOM   450   C  CG    . LEU A 1 1509 ? 107.629 79.202  148.553 1.00 78.71  ? 1509 LEU A CG    1 
ATOM   451   C  CD1   . LEU A 1 1509 ? 106.415 80.116  148.618 1.00 75.67  ? 1509 LEU A CD1   1 
ATOM   452   C  CD2   . LEU A 1 1509 ? 108.472 79.513  147.326 1.00 73.03  ? 1509 LEU A CD2   1 
ATOM   453   N  N     . SER A 1 1510 ? 109.908 77.495  152.183 1.00 78.56  ? 1510 SER A N     1 
ATOM   454   C  CA    . SER A 1 1510 ? 110.419 77.471  153.545 1.00 84.30  ? 1510 SER A CA    1 
ATOM   455   C  C     . SER A 1 1510 ? 111.920 77.188  153.541 1.00 87.35  ? 1510 SER A C     1 
ATOM   456   O  O     . SER A 1 1510 ? 112.411 76.443  152.687 1.00 82.60  ? 1510 SER A O     1 
ATOM   457   C  CB    . SER A 1 1510 ? 109.688 76.415  154.372 1.00 78.93  ? 1510 SER A CB    1 
ATOM   458   O  OG    . SER A 1 1510 ? 109.959 75.113  153.885 1.00 79.77  ? 1510 SER A OG    1 
ATOM   459   N  N     . PRO A 1 1511 ? 112.675 77.764  154.481 1.00 89.07  ? 1511 PRO A N     1 
ATOM   460   C  CA    . PRO A 1 1511 ? 114.128 77.543  154.502 1.00 86.88  ? 1511 PRO A CA    1 
ATOM   461   C  C     . PRO A 1 1511 ? 114.512 76.176  155.047 1.00 86.52  ? 1511 PRO A C     1 
ATOM   462   O  O     . PRO A 1 1511 ? 115.691 75.806  155.038 1.00 84.79  ? 1511 PRO A O     1 
ATOM   463   C  CB    . PRO A 1 1511 ? 114.630 78.671  155.408 1.00 83.96  ? 1511 PRO A CB    1 
ATOM   464   C  CG    . PRO A 1 1511 ? 113.503 78.872  156.367 1.00 82.11  ? 1511 PRO A CG    1 
ATOM   465   C  CD    . PRO A 1 1511 ? 112.248 78.692  155.544 1.00 81.83  ? 1511 PRO A CD    1 
ATOM   466   N  N     . TYR A 1 1512 ? 113.526 75.418  155.524 1.00 86.05  ? 1512 TYR A N     1 
ATOM   467   C  CA    . TYR A 1 1512 ? 113.750 74.089  156.078 1.00 87.08  ? 1512 TYR A CA    1 
ATOM   468   C  C     . TYR A 1 1512 ? 113.423 72.986  155.079 1.00 85.24  ? 1512 TYR A C     1 
ATOM   469   O  O     . TYR A 1 1512 ? 113.302 71.821  155.472 1.00 86.11  ? 1512 TYR A O     1 
ATOM   470   C  CB    . TYR A 1 1512 ? 112.925 73.901  157.354 1.00 89.68  ? 1512 TYR A CB    1 
ATOM   471   C  CG    . TYR A 1 1512 ? 113.038 75.038  158.349 1.00 91.36  ? 1512 TYR A CG    1 
ATOM   472   C  CD1   . TYR A 1 1512 ? 114.230 75.734  158.512 1.00 92.77  ? 1512 TYR A CD1   1 
ATOM   473   C  CD2   . TYR A 1 1512 ? 111.948 75.417  159.122 1.00 87.84  ? 1512 TYR A CD2   1 
ATOM   474   C  CE1   . TYR A 1 1512 ? 114.332 76.773  159.419 1.00 94.07  ? 1512 TYR A CE1   1 
ATOM   475   C  CE2   . TYR A 1 1512 ? 112.041 76.454  160.030 1.00 86.99  ? 1512 TYR A CE2   1 
ATOM   476   C  CZ    . TYR A 1 1512 ? 113.235 77.129  160.175 1.00 91.88  ? 1512 TYR A CZ    1 
ATOM   477   O  OH    . TYR A 1 1512 ? 113.332 78.162  161.078 1.00 90.04  ? 1512 TYR A OH    1 
ATOM   478   N  N     . TYR A 1 1513 ? 113.276 73.328  153.798 1.00 81.63  ? 1513 TYR A N     1 
ATOM   479   C  CA    . TYR A 1 1513 ? 112.833 72.356  152.805 1.00 81.83  ? 1513 TYR A CA    1 
ATOM   480   C  C     . TYR A 1 1513 ? 113.937 71.376  152.425 1.00 83.04  ? 1513 TYR A C     1 
ATOM   481   O  O     . TYR A 1 1513 ? 113.643 70.227  152.073 1.00 85.06  ? 1513 TYR A O     1 
ATOM   482   C  CB    . TYR A 1 1513 ? 112.313 73.094  151.569 1.00 79.25  ? 1513 TYR A CB    1 
ATOM   483   C  CG    . TYR A 1 1513 ? 111.929 72.206  150.409 1.00 79.53  ? 1513 TYR A CG    1 
ATOM   484   C  CD1   . TYR A 1 1513 ? 110.674 71.617  150.348 1.00 76.35  ? 1513 TYR A CD1   1 
ATOM   485   C  CD2   . TYR A 1 1513 ? 112.809 71.983  149.358 1.00 75.83  ? 1513 TYR A CD2   1 
ATOM   486   C  CE1   . TYR A 1 1513 ? 110.314 70.813  149.285 1.00 75.00  ? 1513 TYR A CE1   1 
ATOM   487   C  CE2   . TYR A 1 1513 ? 112.458 71.182  148.291 1.00 74.08  ? 1513 TYR A CE2   1 
ATOM   488   C  CZ    . TYR A 1 1513 ? 111.210 70.599  148.259 1.00 74.40  ? 1513 TYR A CZ    1 
ATOM   489   O  OH    . TYR A 1 1513 ? 110.855 69.800  147.197 1.00 70.05  ? 1513 TYR A OH    1 
ATOM   490   N  N     . LYS A 1 1514 ? 115.202 71.801  152.508 1.00 80.43  ? 1514 LYS A N     1 
ATOM   491   C  CA    . LYS A 1 1514 ? 116.302 70.987  151.997 1.00 79.87  ? 1514 LYS A CA    1 
ATOM   492   C  C     . LYS A 1 1514 ? 116.338 69.610  152.648 1.00 80.54  ? 1514 LYS A C     1 
ATOM   493   O  O     . LYS A 1 1514 ? 116.452 68.592  151.954 1.00 75.14  ? 1514 LYS A O     1 
ATOM   494   C  CB    . LYS A 1 1514 ? 117.632 71.711  152.213 1.00 77.10  ? 1514 LYS A CB    1 
ATOM   495   C  CG    . LYS A 1 1514 ? 117.767 73.071  151.523 1.00 83.95  ? 1514 LYS A CG    1 
ATOM   496   C  CD    . LYS A 1 1514 ? 117.910 72.960  150.004 1.00 87.01  ? 1514 LYS A CD    1 
ATOM   497   C  CE    . LYS A 1 1514 ? 116.580 73.107  149.276 1.00 84.54  ? 1514 LYS A CE    1 
ATOM   498   N  NZ    . LYS A 1 1514 ? 116.756 73.104  147.797 1.00 86.84  ? 1514 LYS A NZ    1 
ATOM   499   N  N     . VAL A 1 1515 ? 116.216 69.557  153.978 1.00 82.23  ? 1515 VAL A N     1 
ATOM   500   C  CA    . VAL A 1 1515 ? 116.297 68.281  154.687 1.00 82.68  ? 1515 VAL A CA    1 
ATOM   501   C  C     . VAL A 1 1515 ? 115.203 67.333  154.212 1.00 83.22  ? 1515 VAL A C     1 
ATOM   502   O  O     . VAL A 1 1515 ? 115.374 66.107  154.221 1.00 83.86  ? 1515 VAL A O     1 
ATOM   503   C  CB    . VAL A 1 1515 ? 116.235 68.514  156.210 1.00 86.68  ? 1515 VAL A CB    1 
ATOM   504   C  CG1   . VAL A 1 1515 ? 114.924 69.181  156.603 1.00 82.73  ? 1515 VAL A CG1   1 
ATOM   505   C  CG2   . VAL A 1 1515 ? 116.430 67.206  156.967 1.00 76.96  ? 1515 VAL A CG2   1 
ATOM   506   N  N     . PHE A 1 1516 ? 114.069 67.881  153.772 1.00 79.62  ? 1516 PHE A N     1 
ATOM   507   C  CA    . PHE A 1 1516 ? 112.966 67.084  153.255 1.00 75.99  ? 1516 PHE A CA    1 
ATOM   508   C  C     . PHE A 1 1516 ? 112.765 67.285  151.757 1.00 73.62  ? 1516 PHE A C     1 
ATOM   509   O  O     . PHE A 1 1516 ? 111.672 67.027  151.243 1.00 71.55  ? 1516 PHE A O     1 
ATOM   510   C  CB    . PHE A 1 1516 ? 111.678 67.406  154.014 1.00 73.69  ? 1516 PHE A CB    1 
ATOM   511   C  CG    . PHE A 1 1516 ? 111.789 67.216  155.500 1.00 77.09  ? 1516 PHE A CG    1 
ATOM   512   C  CD1   . PHE A 1 1516 ? 112.536 66.175  156.026 1.00 78.44  ? 1516 PHE A CD1   1 
ATOM   513   C  CD2   . PHE A 1 1516 ? 111.152 68.083  156.371 1.00 79.15  ? 1516 PHE A CD2   1 
ATOM   514   C  CE1   . PHE A 1 1516 ? 112.642 65.999  157.392 1.00 82.94  ? 1516 PHE A CE1   1 
ATOM   515   C  CE2   . PHE A 1 1516 ? 111.254 67.913  157.738 1.00 83.32  ? 1516 PHE A CE2   1 
ATOM   516   C  CZ    . PHE A 1 1516 ? 112.000 66.870  158.249 1.00 83.94  ? 1516 PHE A CZ    1 
ATOM   517   N  N     . GLU A 1 1517 ? 113.798 67.746  151.049 1.00 71.97  ? 1517 GLU A N     1 
ATOM   518   C  CA    . GLU A 1 1517 ? 113.652 68.026  149.623 1.00 68.09  ? 1517 GLU A CA    1 
ATOM   519   C  C     . GLU A 1 1517 ? 113.359 66.755  148.835 1.00 62.04  ? 1517 GLU A C     1 
ATOM   520   O  O     . GLU A 1 1517 ? 112.305 66.639  148.195 1.00 62.15  ? 1517 GLU A O     1 
ATOM   521   C  CB    . GLU A 1 1517 ? 114.912 68.710  149.093 1.00 72.16  ? 1517 GLU A CB    1 
ATOM   522   C  CG    . GLU A 1 1517 ? 114.954 68.832  147.579 1.00 73.11  ? 1517 GLU A CG    1 
ATOM   523   C  CD    . GLU A 1 1517 ? 116.009 69.808  147.101 1.00 78.72  ? 1517 GLU A CD    1 
ATOM   524   O  OE1   . GLU A 1 1517 ? 117.200 69.599  147.413 1.00 82.32  ? 1517 GLU A OE1   1 
ATOM   525   O  OE2   . GLU A 1 1517 ? 115.647 70.785  146.413 1.00 80.73  ? 1517 GLU A OE2   1 
ATOM   526   N  N     . GLU A 1 1518 ? 114.273 65.779  148.899 1.00 59.23  ? 1518 GLU A N     1 
ATOM   527   C  CA    . GLU A 1 1518 ? 114.186 64.589  148.054 1.00 61.09  ? 1518 GLU A CA    1 
ATOM   528   C  C     . GLU A 1 1518 ? 112.796 63.970  148.101 1.00 59.50  ? 1518 GLU A C     1 
ATOM   529   O  O     . GLU A 1 1518 ? 112.089 63.926  147.085 1.00 59.53  ? 1518 GLU A O     1 
ATOM   530   C  CB    . GLU A 1 1518 ? 115.237 63.566  148.487 1.00 56.13  ? 1518 GLU A CB    1 
ATOM   531   C  CG    . GLU A 1 1518 ? 115.202 62.266  147.701 1.00 65.92  ? 1518 GLU A CG    1 
ATOM   532   C  CD    . GLU A 1 1518 ? 116.187 61.240  148.227 1.00 74.98  ? 1518 GLU A CD    1 
ATOM   533   O  OE1   . GLU A 1 1518 ? 116.067 60.853  149.409 1.00 75.99  ? 1518 GLU A OE1   1 
ATOM   534   O  OE2   . GLU A 1 1518 ? 117.079 60.820  147.461 1.00 73.56  ? 1518 GLU A OE2   1 
ATOM   535   N  N     . ASP A 1 1519 ? 112.372 63.527  149.289 1.00 59.05  ? 1519 ASP A N     1 
ATOM   536   C  CA    . ASP A 1 1519 ? 111.050 62.927  149.433 1.00 55.43  ? 1519 ASP A CA    1 
ATOM   537   C  C     . ASP A 1 1519 ? 109.974 63.825  148.843 1.00 51.78  ? 1519 ASP A C     1 
ATOM   538   O  O     . ASP A 1 1519 ? 109.161 63.374  148.025 1.00 52.83  ? 1519 ASP A O     1 
ATOM   539   C  CB    . ASP A 1 1519 ? 110.763 62.643  150.908 1.00 55.63  ? 1519 ASP A CB    1 
ATOM   540   C  CG    . ASP A 1 1519 ? 109.789 61.499  151.102 1.00 66.70  ? 1519 ASP A CG    1 
ATOM   541   O  OD1   . ASP A 1 1519 ? 109.899 60.491  150.373 1.00 67.91  ? 1519 ASP A OD1   1 
ATOM   542   O  OD2   . ASP A 1 1519 ? 108.912 61.608  151.985 1.00 71.31  ? 1519 ASP A OD2   1 
ATOM   543   N  N     . ALA A 1 1520 ? 109.988 65.113  149.201 1.00 50.36  ? 1520 ALA A N     1 
ATOM   544   C  CA    . ALA A 1 1520 ? 108.993 66.031  148.659 1.00 51.18  ? 1520 ALA A CA    1 
ATOM   545   C  C     . ALA A 1 1520 ? 109.020 66.017  147.140 1.00 47.40  ? 1520 ALA A C     1 
ATOM   546   O  O     . ALA A 1 1520 ? 107.979 65.823  146.497 1.00 48.12  ? 1520 ALA A O     1 
ATOM   547   C  CB    . ALA A 1 1520 ? 109.229 67.444  149.191 1.00 50.14  ? 1520 ALA A CB    1 
ATOM   548   N  N     . LEU A 1 1521 ? 110.213 66.153  146.551 1.00 46.48  ? 1521 LEU A N     1 
ATOM   549   C  CA    . LEU A 1 1521 ? 110.327 66.086  145.099 1.00 46.92  ? 1521 LEU A CA    1 
ATOM   550   C  C     . LEU A 1 1521 ? 109.702 64.802  144.579 1.00 43.06  ? 1521 LEU A C     1 
ATOM   551   O  O     . LEU A 1 1521 ? 108.876 64.829  143.658 1.00 45.07  ? 1521 LEU A O     1 
ATOM   552   C  CB    . LEU A 1 1521 ? 111.793 66.181  144.675 1.00 49.39  ? 1521 LEU A CB    1 
ATOM   553   C  CG    . LEU A 1 1521 ? 112.509 67.514  144.891 1.00 57.85  ? 1521 LEU A CG    1 
ATOM   554   C  CD1   . LEU A 1 1521 ? 113.936 67.433  144.373 1.00 50.18  ? 1521 LEU A CD1   1 
ATOM   555   C  CD2   . LEU A 1 1521 ? 111.753 68.644  144.214 1.00 58.31  ? 1521 LEU A CD2   1 
ATOM   556   N  N     . SER A 1 1522 ? 110.040 63.672  145.211 1.00 39.56  ? 1522 SER A N     1 
ATOM   557   C  CA    . SER A 1 1522 ? 109.458 62.399  144.809 1.00 43.42  ? 1522 SER A CA    1 
ATOM   558   C  C     . SER A 1 1522 ? 107.942 62.489  144.785 1.00 37.95  ? 1522 SER A C     1 
ATOM   559   O  O     . SER A 1 1522 ? 107.310 62.188  143.763 1.00 34.72  ? 1522 SER A O     1 
ATOM   560   C  CB    . SER A 1 1522 ? 109.918 61.289  145.754 1.00 44.33  ? 1522 SER A CB    1 
ATOM   561   O  OG    . SER A 1 1522 ? 109.058 61.183  146.875 1.00 44.08  ? 1522 SER A OG    1 
ATOM   562   N  N     . TRP A 1 1523 ? 107.346 62.982  145.875 1.00 38.49  ? 1523 TRP A N     1 
ATOM   563   C  CA    . TRP A 1 1523 ? 105.894 63.089  145.911 1.00 37.33  ? 1523 TRP A CA    1 
ATOM   564   C  C     . TRP A 1 1523 ? 105.389 63.967  144.781 1.00 36.45  ? 1523 TRP A C     1 
ATOM   565   O  O     . TRP A 1 1523 ? 104.443 63.591  144.077 1.00 37.80  ? 1523 TRP A O     1 
ATOM   566   C  CB    . TRP A 1 1523 ? 105.428 63.619  147.266 1.00 37.45  ? 1523 TRP A CB    1 
ATOM   567   C  CG    . TRP A 1 1523 ? 105.266 62.530  148.267 1.00 44.76  ? 1523 TRP A CG    1 
ATOM   568   C  CD1   . TRP A 1 1523 ? 106.076 62.261  149.329 1.00 47.51  ? 1523 TRP A CD1   1 
ATOM   569   C  CD2   . TRP A 1 1523 ? 104.242 61.530  148.277 1.00 49.79  ? 1523 TRP A CD2   1 
ATOM   570   N  NE1   . TRP A 1 1523 ? 105.607 61.165  150.014 1.00 49.26  ? 1523 TRP A NE1   1 
ATOM   571   C  CE2   . TRP A 1 1523 ? 104.483 60.698  149.386 1.00 49.28  ? 1523 TRP A CE2   1 
ATOM   572   C  CE3   . TRP A 1 1523 ? 103.139 61.264  147.460 1.00 42.67  ? 1523 TRP A CE3   1 
ATOM   573   C  CZ2   . TRP A 1 1523 ? 103.664 59.617  149.698 1.00 48.22  ? 1523 TRP A CZ2   1 
ATOM   574   C  CZ3   . TRP A 1 1523 ? 102.326 60.191  147.772 1.00 40.83  ? 1523 TRP A CZ3   1 
ATOM   575   C  CH2   . TRP A 1 1523 ? 102.592 59.381  148.882 1.00 46.11  ? 1523 TRP A CH2   1 
ATOM   576   N  N     . GLU A 1 1524 ? 106.053 65.105  144.549 1.00 35.50  ? 1524 GLU A N     1 
ATOM   577   C  CA    . GLU A 1 1524 ? 105.670 65.955  143.430 1.00 33.08  ? 1524 GLU A CA    1 
ATOM   578   C  C     . GLU A 1 1524 ? 105.604 65.137  142.152 1.00 27.90  ? 1524 GLU A C     1 
ATOM   579   O  O     . GLU A 1 1524 ? 104.562 65.090  141.484 1.00 28.62  ? 1524 GLU A O     1 
ATOM   580   C  CB    . GLU A 1 1524 ? 106.661 67.111  143.287 1.00 38.02  ? 1524 GLU A CB    1 
ATOM   581   C  CG    . GLU A 1 1524 ? 106.555 67.861  141.970 1.00 40.18  ? 1524 GLU A CG    1 
ATOM   582   C  CD    . GLU A 1 1524 ? 107.835 68.590  141.610 1.00 51.39  ? 1524 GLU A CD    1 
ATOM   583   O  OE1   . GLU A 1 1524 ? 108.905 67.947  141.602 1.00 49.23  ? 1524 GLU A OE1   1 
ATOM   584   O  OE2   . GLU A 1 1524 ? 107.771 69.806  141.332 1.00 53.72  ? 1524 GLU A OE2   1 
ATOM   585   N  N     . ASP A 1 1525 ? 106.676 64.393  141.863 1.00 27.97  ? 1525 ASP A N     1 
ATOM   586   C  CA    . ASP A 1 1525 ? 106.686 63.543  140.681 1.00 26.31  ? 1525 ASP A CA    1 
ATOM   587   C  C     . ASP A 1 1525 ? 105.474 62.626  140.678 1.00 26.64  ? 1525 ASP A C     1 
ATOM   588   O  O     . ASP A 1 1525 ? 104.668 62.646  139.738 1.00 26.05  ? 1525 ASP A O     1 
ATOM   589   C  CB    . ASP A 1 1525 ? 107.983 62.735  140.633 1.00 26.77  ? 1525 ASP A CB    1 
ATOM   590   C  CG    . ASP A 1 1525 ? 108.158 61.987  139.329 1.00 36.99  ? 1525 ASP A CG    1 
ATOM   591   O  OD1   . ASP A 1 1525 ? 108.627 62.601  138.348 1.00 40.38  ? 1525 ASP A OD1   1 
ATOM   592   O  OD2   . ASP A 1 1525 ? 107.836 60.782  139.288 1.00 36.74  ? 1525 ASP A OD2   1 
ATOM   593   N  N     . LYS A 1 1526 ? 105.274 61.893  141.778 1.00 26.33  ? 1526 LYS A N     1 
ATOM   594   C  CA    . LYS A 1 1526 ? 104.137 60.985  141.855 1.00 25.62  ? 1526 LYS A CA    1 
ATOM   595   C  C     . LYS A 1 1526 ? 102.843 61.738  141.605 1.00 23.99  ? 1526 LYS A C     1 
ATOM   596   O  O     . LYS A 1 1526 ? 102.035 61.342  140.753 1.00 23.75  ? 1526 LYS A O     1 
ATOM   597   C  CB    . LYS A 1 1526 ? 104.108 60.287  143.215 1.00 29.36  ? 1526 LYS A CB    1 
ATOM   598   C  CG    . LYS A 1 1526 ? 105.367 59.503  143.538 1.00 36.69  ? 1526 LYS A CG    1 
ATOM   599   C  CD    . LYS A 1 1526 ? 105.079 58.368  144.506 1.00 35.82  ? 1526 LYS A CD    1 
ATOM   600   C  CE    . LYS A 1 1526 ? 105.213 58.824  145.948 1.00 43.05  ? 1526 LYS A CE    1 
ATOM   601   N  NZ    . LYS A 1 1526 ? 105.933 57.823  146.783 1.00 45.28  ? 1526 LYS A NZ    1 
ATOM   602   N  N     . LEU A 1 1527 ? 102.673 62.882  142.276 1.00 23.31  ? 1527 LEU A N     1 
ATOM   603   C  CA    . LEU A 1 1527 ? 101.447 63.646  142.096 1.00 21.45  ? 1527 LEU A CA    1 
ATOM   604   C  C     . LEU A 1 1527 ? 101.259 64.004  140.633 1.00 20.92  ? 1527 LEU A C     1 
ATOM   605   O  O     . LEU A 1 1527 ? 100.191 63.752  140.058 1.00 21.75  ? 1527 LEU A O     1 
ATOM   606   C  CB    . LEU A 1 1527 ? 101.471 64.900  142.968 1.00 29.00  ? 1527 LEU A CB    1 
ATOM   607   C  CG    . LEU A 1 1527 ? 101.449 64.676  144.482 1.00 29.71  ? 1527 LEU A CG    1 
ATOM   608   C  CD1   . LEU A 1 1527 ? 101.683 65.983  145.223 1.00 31.89  ? 1527 LEU A CD1   1 
ATOM   609   C  CD2   . LEU A 1 1527 ? 100.138 64.039  144.912 1.00 23.90  ? 1527 LEU A CD2   1 
ATOM   610   N  N     . ASN A 1 1528 ? 102.319 64.502  139.990 1.00 22.24  ? 1528 ASN A N     1 
ATOM   611   C  CA    . ASN A 1 1528 ? 102.196 64.871  138.588 1.00 18.30  ? 1528 ASN A CA    1 
ATOM   612   C  C     . ASN A 1 1528 ? 101.802 63.663  137.757 1.00 17.80  ? 1528 ASN A C     1 
ATOM   613   O  O     . ASN A 1 1528 ? 100.896 63.748  136.918 1.00 17.66  ? 1528 ASN A O     1 
ATOM   614   C  CB    . ASN A 1 1528 ? 103.500 65.481  138.079 1.00 19.03  ? 1528 ASN A CB    1 
ATOM   615   C  CG    . ASN A 1 1528 ? 103.747 66.868  138.634 1.00 19.59  ? 1528 ASN A CG    1 
ATOM   616   O  OD1   . ASN A 1 1528 ? 102.912 67.761  138.496 1.00 25.07  ? 1528 ASN A OD1   1 
ATOM   617   N  ND2   . ASN A 1 1528 ? 104.904 67.059  139.251 1.00 22.28  ? 1528 ASN A ND2   1 
ATOM   618   N  N     . ARG A 1 1529 ? 102.423 62.511  138.032 1.00 20.55  ? 1529 ARG A N     1 
ATOM   619   C  CA    . ARG A 1 1529 ? 102.068 61.307  137.296 1.00 17.73  ? 1529 ARG A CA    1 
ATOM   620   C  C     . ARG A 1 1529 ? 100.590 60.997  137.467 1.00 15.55  ? 1529 ARG A C     1 
ATOM   621   O  O     . ARG A 1 1529 ? 99.884  60.747  136.481 1.00 17.52  ? 1529 ARG A O     1 
ATOM   622   C  CB    . ARG A 1 1529 ? 102.942 60.137  137.748 1.00 16.80  ? 1529 ARG A CB    1 
ATOM   623   C  CG    . ARG A 1 1529 ? 104.401 60.302  137.348 1.00 20.35  ? 1529 ARG A CG    1 
ATOM   624   C  CD    . ARG A 1 1529 ? 105.321 59.288  138.011 1.00 25.93  ? 1529 ARG A CD    1 
ATOM   625   N  NE    . ARG A 1 1529 ? 104.869 57.913  137.834 1.00 28.95  ? 1529 ARG A NE    1 
ATOM   626   C  CZ    . ARG A 1 1529 ? 104.588 57.085  138.831 1.00 32.78  ? 1529 ARG A CZ    1 
ATOM   627   N  NH1   . ARG A 1 1529 ? 104.722 57.454  140.094 1.00 26.67  ? 1529 ARG A NH1   1 
ATOM   628   N  NH2   . ARG A 1 1529 ? 104.172 55.853  138.553 1.00 31.61  ? 1529 ARG A NH2   1 
ATOM   629   N  N     . ILE A 1 1530 ? 100.088 61.088  138.702 1.00 15.76  ? 1530 ILE A N     1 
ATOM   630   C  CA    . ILE A 1 1530 ? 98.657  60.909  138.920 1.00 15.46  ? 1530 ILE A CA    1 
ATOM   631   C  C     . ILE A 1 1530 ? 97.884  61.919  138.086 1.00 19.61  ? 1530 ILE A C     1 
ATOM   632   O  O     . ILE A 1 1530 ? 97.009  61.555  137.287 1.00 20.69  ? 1530 ILE A O     1 
ATOM   633   C  CB    . ILE A 1 1530 ? 98.318  61.033  140.416 1.00 18.52  ? 1530 ILE A CB    1 
ATOM   634   C  CG1   . ILE A 1 1530 ? 98.998  59.919  141.213 1.00 19.41  ? 1530 ILE A CG1   1 
ATOM   635   C  CG2   . ILE A 1 1530 ? 96.814  60.998  140.627 1.00 18.97  ? 1530 ILE A CG2   1 
ATOM   636   C  CD1   . ILE A 1 1530 ? 98.937  60.114  142.712 1.00 24.04  ? 1530 ILE A CD1   1 
ATOM   637   N  N     . MET A 1 1531 ? 98.270  63.195  138.189 1.00 19.75  ? 1531 MET A N     1 
ATOM   638   C  CA    . MET A 1 1531 ? 97.566  64.242  137.460 1.00 14.26  ? 1531 MET A CA    1 
ATOM   639   C  C     . MET A 1 1531 ? 97.625  63.996  135.961 1.00 15.90  ? 1531 MET A C     1 
ATOM   640   O  O     . MET A 1 1531 ? 96.754  64.457  135.216 1.00 23.28  ? 1531 MET A O     1 
ATOM   641   C  CB    . MET A 1 1531 ? 98.142  65.613  137.811 1.00 18.05  ? 1531 MET A CB    1 
ATOM   642   C  CG    . MET A 1 1531 ? 97.299  66.767  137.303 1.00 20.51  ? 1531 MET A CG    1 
ATOM   643   S  SD    . MET A 1 1531 ? 95.607  66.681  137.916 1.00 41.28  ? 1531 MET A SD    1 
ATOM   644   C  CE    . MET A 1 1531 ? 95.717  67.753  139.338 1.00 34.84  ? 1531 MET A CE    1 
ATOM   645   N  N     . ALA A 1 1532 ? 98.640  63.267  135.497 1.00 15.20  ? 1532 ALA A N     1 
ATOM   646   C  CA    . ALA A 1 1532 ? 98.637  62.853  134.102 1.00 15.23  ? 1532 ALA A CA    1 
ATOM   647   C  C     . ALA A 1 1532 ? 97.556  61.810  133.857 1.00 15.17  ? 1532 ALA A C     1 
ATOM   648   O  O     . ALA A 1 1532 ? 96.575  62.065  133.145 1.00 21.55  ? 1532 ALA A O     1 
ATOM   649   C  CB    . ALA A 1 1532 ? 100.014 62.317  133.709 1.00 15.43  ? 1532 ALA A CB    1 
ATOM   650   N  N     . LEU A 1 1533 ? 97.679  60.655  134.518 1.00 11.95  ? 1533 LEU A N     1 
ATOM   651   C  CA    . LEU A 1 1533 ? 96.935  59.467  134.109 1.00 15.65  ? 1533 LEU A CA    1 
ATOM   652   C  C     . LEU A 1 1533 ? 95.435  59.717  134.126 1.00 14.50  ? 1533 LEU A C     1 
ATOM   653   O  O     . LEU A 1 1533 ? 94.744  59.525  133.116 1.00 14.06  ? 1533 LEU A O     1 
ATOM   654   C  CB    . LEU A 1 1533 ? 97.294  58.296  135.024 1.00 12.42  ? 1533 LEU A CB    1 
ATOM   655   C  CG    . LEU A 1 1533 ? 96.509  56.997  134.842 1.00 14.33  ? 1533 LEU A CG    1 
ATOM   656   C  CD1   . LEU A 1 1533 ? 96.799  56.365  133.487 1.00 13.88  ? 1533 LEU A CD1   1 
ATOM   657   C  CD2   . LEU A 1 1533 ? 96.806  56.025  135.978 1.00 16.59  ? 1533 LEU A CD2   1 
ATOM   658   N  N     . PHE A 1 1534 ? 94.921  60.193  135.256 1.00 14.12  ? 1534 PHE A N     1 
ATOM   659   C  CA    . PHE A 1 1534 ? 93.484  60.369  135.381 1.00 15.85  ? 1534 PHE A CA    1 
ATOM   660   C  C     . PHE A 1 1534 ? 92.982  61.501  134.501 1.00 14.30  ? 1534 PHE A C     1 
ATOM   661   O  O     . PHE A 1 1534 ? 91.838  61.452  134.035 1.00 17.10  ? 1534 PHE A O     1 
ATOM   662   C  CB    . PHE A 1 1534 ? 93.125  60.593  136.845 1.00 16.32  ? 1534 PHE A CB    1 
ATOM   663   C  CG    . PHE A 1 1534 ? 93.354  59.385  137.698 1.00 18.83  ? 1534 PHE A CG    1 
ATOM   664   C  CD1   . PHE A 1 1534 ? 92.892  58.142  137.294 1.00 19.84  ? 1534 PHE A CD1   1 
ATOM   665   C  CD2   . PHE A 1 1534 ? 94.072  59.477  138.874 1.00 24.86  ? 1534 PHE A CD2   1 
ATOM   666   C  CE1   . PHE A 1 1534 ? 93.113  57.022  138.066 1.00 20.99  ? 1534 PHE A CE1   1 
ATOM   667   C  CE2   . PHE A 1 1534 ? 94.296  58.362  139.649 1.00 26.30  ? 1534 PHE A CE2   1 
ATOM   668   C  CZ    . PHE A 1 1534 ? 93.817  57.131  139.246 1.00 24.84  ? 1534 PHE A CZ    1 
ATOM   669   N  N     . ASP A 1 1535 ? 93.826  62.502  134.221 1.00 13.30  ? 1535 ASP A N     1 
ATOM   670   C  CA    . ASP A 1 1535 ? 93.392  63.554  133.309 1.00 14.58  ? 1535 ASP A CA    1 
ATOM   671   C  C     . ASP A 1 1535 ? 93.101  62.989  131.929 1.00 13.82  ? 1535 ASP A C     1 
ATOM   672   O  O     . ASP A 1 1535 ? 92.316  63.568  131.171 1.00 15.76  ? 1535 ASP A O     1 
ATOM   673   C  CB    . ASP A 1 1535 ? 94.436  64.664  133.222 1.00 17.92  ? 1535 ASP A CB    1 
ATOM   674   C  CG    . ASP A 1 1535 ? 93.885  65.931  132.602 1.00 21.70  ? 1535 ASP A CG    1 
ATOM   675   O  OD1   . ASP A 1 1535 ? 92.971  66.536  133.197 1.00 18.43  ? 1535 ASP A OD1   1 
ATOM   676   O  OD2   . ASP A 1 1535 ? 94.364  66.325  131.519 1.00 20.54  ? 1535 ASP A OD2   1 
ATOM   677   N  N     . VAL A 1 1536 ? 93.718  61.858  131.591 1.00 11.91  ? 1536 VAL A N     1 
ATOM   678   C  CA    . VAL A 1 1536 ? 93.308  61.127  130.400 1.00 14.08  ? 1536 VAL A CA    1 
ATOM   679   C  C     . VAL A 1 1536 ? 92.138  60.210  130.717 1.00 12.14  ? 1536 VAL A C     1 
ATOM   680   O  O     . VAL A 1 1536 ? 91.149  60.169  129.972 1.00 15.51  ? 1536 VAL A O     1 
ATOM   681   C  CB    . VAL A 1 1536 ? 94.503  60.350  129.824 1.00 14.70  ? 1536 VAL A CB    1 
ATOM   682   C  CG1   . VAL A 1 1536 ? 94.049  59.450  128.690 1.00 14.23  ? 1536 VAL A CG1   1 
ATOM   683   C  CG2   . VAL A 1 1536 ? 95.571  61.319  129.336 1.00 10.71  ? 1536 VAL A CG2   1 
ATOM   684   N  N     . TRP A 1 1537 ? 92.219  59.515  131.859 1.00 10.59  ? 1537 TRP A N     1 
ATOM   685   C  CA    . TRP A 1 1537 ? 91.317  58.408  132.148 1.00 12.18  ? 1537 TRP A CA    1 
ATOM   686   C  C     . TRP A 1 1537 ? 89.880  58.837  131.905 1.00 12.64  ? 1537 TRP A C     1 
ATOM   687   O  O     . TRP A 1 1537 ? 89.165  58.246  131.081 1.00 12.53  ? 1537 TRP A O     1 
ATOM   688   C  CB    . TRP A 1 1537 ? 91.446  57.997  133.614 1.00 16.08  ? 1537 TRP A CB    1 
ATOM   689   C  CG    . TRP A 1 1537 ? 90.644  56.797  133.978 1.00 22.83  ? 1537 TRP A CG    1 
ATOM   690   C  CD1   . TRP A 1 1537 ? 89.454  56.770  134.609 1.00 28.10  ? 1537 TRP A CD1   1 
ATOM   691   C  CD2   . TRP A 1 1537 ? 91.125  55.446  134.015 1.00 21.97  ? 1537 TRP A CD2   1 
ATOM   692   N  NE1   . TRP A 1 1537 ? 89.067  55.482  134.855 1.00 32.85  ? 1537 TRP A NE1   1 
ATOM   693   C  CE2   . TRP A 1 1537 ? 90.098  54.648  134.532 1.00 30.04  ? 1537 TRP A CE2   1 
ATOM   694   C  CE3   . TRP A 1 1537 ? 92.303  54.831  133.606 1.00 28.89  ? 1537 TRP A CE3   1 
ATOM   695   C  CZ2   . TRP A 1 1537 ? 90.217  53.269  134.660 1.00 33.15  ? 1537 TRP A CZ2   1 
ATOM   696   C  CZ3   . TRP A 1 1537 ? 92.412  53.470  133.720 1.00 28.54  ? 1537 TRP A CZ3   1 
ATOM   697   C  CH2   . TRP A 1 1537 ? 91.380  52.703  134.247 1.00 26.18  ? 1537 TRP A CH2   1 
ATOM   698   N  N     . ILE A 1 1538 ? 89.494  59.952  132.539 1.00 9.54   ? 1538 ILE A N     1 
ATOM   699   C  CA    . ILE A 1 1538 ? 88.121  60.453  132.511 1.00 14.14  ? 1538 ILE A CA    1 
ATOM   700   C  C     . ILE A 1 1538 ? 87.627  60.614  131.081 1.00 12.47  ? 1538 ILE A C     1 
ATOM   701   O  O     . ILE A 1 1538 ? 86.578  60.072  130.708 1.00 14.19  ? 1538 ILE A O     1 
ATOM   702   C  CB    . ILE A 1 1538 ? 88.036  61.772  133.308 1.00 14.80  ? 1538 ILE A CB    1 
ATOM   703   C  CG1   . ILE A 1 1538 ? 86.588  62.248  133.475 1.00 14.95  ? 1538 ILE A CG1   1 
ATOM   704   C  CG2   . ILE A 1 1538 ? 88.974  62.851  132.760 1.00 11.43  ? 1538 ILE A CG2   1 
ATOM   705   C  CD1   . ILE A 1 1538 ? 86.438  63.350  134.500 1.00 12.07  ? 1538 ILE A CD1   1 
ATOM   706   N  N     . ASP A 1 1539 ? 88.405  61.308  130.242 1.00 10.17  ? 1539 ASP A N     1 
ATOM   707   C  CA    . ASP A 1 1539 ? 87.971  61.504  128.866 1.00 11.13  ? 1539 ASP A CA    1 
ATOM   708   C  C     . ASP A 1 1539 ? 87.714  60.160  128.215 1.00 11.99  ? 1539 ASP A C     1 
ATOM   709   O  O     . ASP A 1 1539 ? 86.603  59.895  127.733 1.00 14.32  ? 1539 ASP A O     1 
ATOM   710   C  CB    . ASP A 1 1539 ? 89.016  62.303  128.087 1.00 15.76  ? 1539 ASP A CB    1 
ATOM   711   C  CG    . ASP A 1 1539 ? 89.049  63.768  128.485 1.00 20.70  ? 1539 ASP A CG    1 
ATOM   712   O  OD1   . ASP A 1 1539 ? 88.019  64.280  128.973 1.00 20.91  ? 1539 ASP A OD1   1 
ATOM   713   O  OD2   . ASP A 1 1539 ? 90.109  64.406  128.315 1.00 24.31  ? 1539 ASP A OD2   1 
ATOM   714   N  N     . VAL A 1 1540 ? 88.701  59.262  128.304 1.00 9.46   ? 1540 VAL A N     1 
ATOM   715   C  CA    . VAL A 1 1540 ? 88.526  57.894  127.835 1.00 10.72  ? 1540 VAL A CA    1 
ATOM   716   C  C     . VAL A 1 1540 ? 87.209  57.339  128.346 1.00 8.11   ? 1540 VAL A C     1 
ATOM   717   O  O     . VAL A 1 1540 ? 86.298  57.034  127.562 1.00 10.37  ? 1540 VAL A O     1 
ATOM   718   C  CB    . VAL A 1 1540 ? 89.716  57.026  128.281 1.00 11.33  ? 1540 VAL A CB    1 
ATOM   719   C  CG1   . VAL A 1 1540 ? 89.454  55.562  127.977 1.00 7.72   ? 1540 VAL A CG1   1 
ATOM   720   C  CG2   . VAL A 1 1540 ? 90.996  57.500  127.612 1.00 10.19  ? 1540 VAL A CG2   1 
ATOM   721   N  N     . GLN A 1 1541 ? 87.052  57.303  129.674 1.00 9.02   ? 1541 GLN A N     1 
ATOM   722   C  CA    . GLN A 1 1541 ? 85.839  56.737  130.246 1.00 9.49   ? 1541 GLN A CA    1 
ATOM   723   C  C     . GLN A 1 1541 ? 84.616  57.397  129.640 1.00 9.05   ? 1541 GLN A C     1 
ATOM   724   O  O     . GLN A 1 1541 ? 83.768  56.715  129.046 1.00 9.16   ? 1541 GLN A O     1 
ATOM   725   C  CB    . GLN A 1 1541 ? 85.842  56.894  131.766 1.00 10.03  ? 1541 GLN A CB    1 
ATOM   726   C  CG    . GLN A 1 1541 ? 84.634  56.268  132.444 1.00 10.75  ? 1541 GLN A CG    1 
ATOM   727   C  CD    . GLN A 1 1541 ? 84.718  56.307  133.957 1.00 15.77  ? 1541 GLN A CD    1 
ATOM   728   O  OE1   . GLN A 1 1541 ? 85.642  55.758  134.554 1.00 21.35  ? 1541 GLN A OE1   1 
ATOM   729   N  NE2   . GLN A 1 1541 ? 83.747  56.958  134.585 1.00 15.25  ? 1541 GLN A NE2   1 
ATOM   730   N  N     . ARG A 1 1542 ? 84.578  58.733  129.666 1.00 8.29   ? 1542 ARG A N     1 
ATOM   731   C  CA    . ARG A 1 1542 ? 83.421  59.438  129.134 1.00 11.26  ? 1542 ARG A CA    1 
ATOM   732   C  C     . ARG A 1 1542 ? 83.139  58.982  127.715 1.00 8.69   ? 1542 ARG A C     1 
ATOM   733   O  O     . ARG A 1 1542 ? 82.056  58.457  127.422 1.00 7.86   ? 1542 ARG A O     1 
ATOM   734   C  CB    . ARG A 1 1542 ? 83.663  60.946  129.181 1.00 12.94  ? 1542 ARG A CB    1 
ATOM   735   C  CG    . ARG A 1 1542 ? 82.536  61.779  128.608 1.00 14.46  ? 1542 ARG A CG    1 
ATOM   736   C  CD    . ARG A 1 1542 ? 82.829  63.259  128.765 1.00 20.45  ? 1542 ARG A CD    1 
ATOM   737   N  NE    . ARG A 1 1542 ? 84.115  63.615  128.176 1.00 19.86  ? 1542 ARG A NE    1 
ATOM   738   C  CZ    . ARG A 1 1542 ? 84.318  63.822  126.882 1.00 27.41  ? 1542 ARG A CZ    1 
ATOM   739   N  NH1   . ARG A 1 1542 ? 83.337  63.710  126.002 1.00 26.03  ? 1542 ARG A NH1   1 
ATOM   740   N  NH2   . ARG A 1 1542 ? 85.537  64.143  126.461 1.00 26.74  ? 1542 ARG A NH2   1 
ATOM   741   N  N     . ARG A 1 1543 ? 84.158  59.051  126.855 1.00 8.99   ? 1543 ARG A N     1 
ATOM   742   C  CA    . ARG A 1 1543 ? 83.953  58.662  125.470 1.00 9.82   ? 1543 ARG A CA    1 
ATOM   743   C  C     . ARG A 1 1543 ? 83.463  57.230  125.401 1.00 8.01   ? 1543 ARG A C     1 
ATOM   744   O  O     . ARG A 1 1543 ? 82.375  56.963  124.863 1.00 10.07  ? 1543 ARG A O     1 
ATOM   745   C  CB    . ARG A 1 1543 ? 85.245  58.846  124.675 1.00 9.35   ? 1543 ARG A CB    1 
ATOM   746   C  CG    . ARG A 1 1543 ? 85.375  60.226  124.053 1.00 17.81  ? 1543 ARG A CG    1 
ATOM   747   C  CD    . ARG A 1 1543 ? 86.823  60.628  123.861 1.00 24.89  ? 1543 ARG A CD    1 
ATOM   748   N  NE    . ARG A 1 1543 ? 87.001  62.073  123.919 1.00 34.48  ? 1543 ARG A NE    1 
ATOM   749   C  CZ    . ARG A 1 1543 ? 87.110  62.857  122.855 1.00 42.56  ? 1543 ARG A CZ    1 
ATOM   750   N  NH1   . ARG A 1 1543 ? 87.073  62.365  121.628 1.00 37.99  ? 1543 ARG A NH1   1 
ATOM   751   N  NH2   . ARG A 1 1543 ? 87.259  64.167  123.027 1.00 46.37  ? 1543 ARG A NH2   1 
ATOM   752   N  N     . TRP A 1 1544 ? 84.185  56.320  126.066 1.00 6.71   ? 1544 TRP A N     1 
ATOM   753   C  CA    . TRP A 1 1544 ? 83.826  54.913  125.991 1.00 6.55   ? 1544 TRP A CA    1 
ATOM   754   C  C     . TRP A 1 1544 ? 82.360  54.737  126.326 1.00 6.88   ? 1544 TRP A C     1 
ATOM   755   O  O     . TRP A 1 1544 ? 81.622  54.075  125.582 1.00 8.41   ? 1544 TRP A O     1 
ATOM   756   C  CB    . TRP A 1 1544 ? 84.694  54.082  126.935 1.00 8.24   ? 1544 TRP A CB    1 
ATOM   757   C  CG    . TRP A 1 1544 ? 84.351  52.629  126.894 1.00 7.00   ? 1544 TRP A CG    1 
ATOM   758   C  CD1   . TRP A 1 1544 ? 84.849  51.695  126.035 1.00 8.46   ? 1544 TRP A CD1   1 
ATOM   759   C  CD2   . TRP A 1 1544 ? 83.392  51.950  127.712 1.00 6.11   ? 1544 TRP A CD2   1 
ATOM   760   N  NE1   . TRP A 1 1544 ? 84.280  50.471  126.284 1.00 7.59   ? 1544 TRP A NE1   1 
ATOM   761   C  CE2   . TRP A 1 1544 ? 83.381  50.602  127.309 1.00 6.08   ? 1544 TRP A CE2   1 
ATOM   762   C  CE3   . TRP A 1 1544 ? 82.552  52.350  128.755 1.00 8.33   ? 1544 TRP A CE3   1 
ATOM   763   C  CZ2   . TRP A 1 1544 ? 82.563  49.652  127.909 1.00 9.46   ? 1544 TRP A CZ2   1 
ATOM   764   C  CZ3   . TRP A 1 1544 ? 81.741  51.405  129.349 1.00 8.24   ? 1544 TRP A CZ3   1 
ATOM   765   C  CH2   . TRP A 1 1544 ? 81.750  50.073  128.922 1.00 9.64   ? 1544 TRP A CH2   1 
ATOM   766   N  N     . VAL A 1 1545 ? 81.899  55.433  127.371 1.00 7.68   ? 1545 VAL A N     1 
ATOM   767   C  CA    . VAL A 1 1545 ? 80.525  55.265  127.825 1.00 8.33   ? 1545 VAL A CA    1 
ATOM   768   C  C     . VAL A 1 1545 ? 79.574  55.434  126.652 1.00 9.88   ? 1545 VAL A C     1 
ATOM   769   O  O     . VAL A 1 1545 ? 78.921  54.476  126.216 1.00 11.51  ? 1545 VAL A O     1 
ATOM   770   C  CB    . VAL A 1 1545 ? 80.204  56.247  128.966 1.00 11.04  ? 1545 VAL A CB    1 
ATOM   771   C  CG1   . VAL A 1 1545 ? 78.699  56.399  129.136 1.00 13.15  ? 1545 VAL A CG1   1 
ATOM   772   C  CG2   . VAL A 1 1545 ? 80.840  55.776  130.261 1.00 10.40  ? 1545 VAL A CG2   1 
ATOM   773   N  N     . TYR A 1 1546 ? 79.570  56.624  126.045 1.00 8.30   ? 1546 TYR A N     1 
ATOM   774   C  CA    . TYR A 1 1546 ? 78.570  56.821  125.009 1.00 10.24  ? 1546 TYR A CA    1 
ATOM   775   C  C     . TYR A 1 1546 ? 78.877  55.960  123.797 1.00 10.72  ? 1546 TYR A C     1 
ATOM   776   O  O     . TYR A 1 1546 ? 77.950  55.422  123.178 1.00 12.78  ? 1546 TYR A O     1 
ATOM   777   C  CB    . TYR A 1 1546 ? 78.424  58.308  124.651 1.00 10.14  ? 1546 TYR A CB    1 
ATOM   778   C  CG    . TYR A 1 1546 ? 79.621  59.012  124.047 1.00 10.07  ? 1546 TYR A CG    1 
ATOM   779   C  CD1   . TYR A 1 1546 ? 80.018  58.766  122.739 1.00 10.01  ? 1546 TYR A CD1   1 
ATOM   780   C  CD2   . TYR A 1 1546 ? 80.318  59.968  124.772 1.00 9.32   ? 1546 TYR A CD2   1 
ATOM   781   C  CE1   . TYR A 1 1546 ? 81.096  59.424  122.185 1.00 12.91  ? 1546 TYR A CE1   1 
ATOM   782   C  CE2   . TYR A 1 1546 ? 81.395  60.634  124.225 1.00 11.42  ? 1546 TYR A CE2   1 
ATOM   783   C  CZ    . TYR A 1 1546 ? 81.781  60.357  122.932 1.00 15.85  ? 1546 TYR A CZ    1 
ATOM   784   O  OH    . TYR A 1 1546 ? 82.852  61.017  122.378 1.00 20.86  ? 1546 TYR A OH    1 
ATOM   785   N  N     . LEU A 1 1547 ? 80.162  55.733  123.511 1.00 8.63   ? 1547 LEU A N     1 
ATOM   786   C  CA    . LEU A 1 1547 ? 80.494  54.864  122.392 1.00 9.22   ? 1547 LEU A CA    1 
ATOM   787   C  C     . LEU A 1 1547 ? 79.945  53.468  122.631 1.00 8.31   ? 1547 LEU A C     1 
ATOM   788   O  O     . LEU A 1 1547 ? 79.363  52.860  121.725 1.00 10.24  ? 1547 LEU A O     1 
ATOM   789   C  CB    . LEU A 1 1547 ? 82.004  54.839  122.166 1.00 8.08   ? 1547 LEU A CB    1 
ATOM   790   C  CG    . LEU A 1 1547 ? 82.532  56.073  121.433 1.00 8.79   ? 1547 LEU A CG    1 
ATOM   791   C  CD1   . LEU A 1 1547 ? 84.040  56.025  121.279 1.00 8.21   ? 1547 LEU A CD1   1 
ATOM   792   C  CD2   . LEU A 1 1547 ? 81.858  56.216  120.080 1.00 7.28   ? 1547 LEU A CD2   1 
ATOM   793   N  N     . GLU A 1 1548 ? 80.057  52.976  123.868 1.00 10.77  ? 1548 GLU A N     1 
ATOM   794   C  CA    . GLU A 1 1548 ? 79.476  51.678  124.178 1.00 15.15  ? 1548 GLU A CA    1 
ATOM   795   C  C     . GLU A 1 1548 ? 77.976  51.702  123.928 1.00 13.03  ? 1548 GLU A C     1 
ATOM   796   O  O     . GLU A 1 1548 ? 77.435  50.816  123.252 1.00 18.33  ? 1548 GLU A O     1 
ATOM   797   C  CB    . GLU A 1 1548 ? 79.805  51.299  125.623 1.00 12.14  ? 1548 GLU A CB    1 
ATOM   798   C  CG    . GLU A 1 1548 ? 79.640  49.828  125.976 1.00 16.44  ? 1548 GLU A CG    1 
ATOM   799   C  CD    . GLU A 1 1548 ? 78.199  49.430  126.210 1.00 29.47  ? 1548 GLU A CD    1 
ATOM   800   O  OE1   . GLU A 1 1548 ? 77.491  50.152  126.941 1.00 26.30  ? 1548 GLU A OE1   1 
ATOM   801   O  OE2   . GLU A 1 1548 ? 77.783  48.381  125.679 1.00 33.88  ? 1548 GLU A OE2   1 
ATOM   802   N  N     . GLY A 1 1549 ? 77.307  52.768  124.379 1.00 12.55  ? 1549 GLY A N     1 
ATOM   803   C  CA    . GLY A 1 1549 ? 75.870  52.860  124.190 1.00 17.23  ? 1549 GLY A CA    1 
ATOM   804   C  C     . GLY A 1 1549 ? 75.480  52.883  122.726 1.00 17.67  ? 1549 GLY A C     1 
ATOM   805   O  O     . GLY A 1 1549 ? 74.333  52.596  122.373 1.00 26.97  ? 1549 GLY A O     1 
ATOM   806   N  N     . ILE A 1 1550 ? 76.428  53.222  121.854 1.00 18.55  ? 1550 ILE A N     1 
ATOM   807   C  CA    . ILE A 1 1550 ? 76.133  53.262  120.428 1.00 17.63  ? 1550 ILE A CA    1 
ATOM   808   C  C     . ILE A 1 1550 ? 76.383  51.898  119.795 1.00 22.26  ? 1550 ILE A C     1 
ATOM   809   O  O     . ILE A 1 1550 ? 75.667  51.481  118.878 1.00 29.99  ? 1550 ILE A O     1 
ATOM   810   C  CB    . ILE A 1 1550 ? 76.950  54.376  119.751 1.00 16.02  ? 1550 ILE A CB    1 
ATOM   811   C  CG1   . ILE A 1 1550 ? 76.508  55.733  120.299 1.00 18.15  ? 1550 ILE A CG1   1 
ATOM   812   C  CG2   . ILE A 1 1550 ? 76.778  54.337  118.242 1.00 20.36  ? 1550 ILE A CG2   1 
ATOM   813   C  CD1   . ILE A 1 1550 ? 77.383  56.874  119.880 1.00 14.10  ? 1550 ILE A CD1   1 
ATOM   814   N  N     . PHE A 1 1551 ? 77.384  51.169  120.291 1.00 22.66  ? 1551 PHE A N     1 
ATOM   815   C  CA    . PHE A 1 1551 ? 77.732  49.888  119.687 1.00 20.24  ? 1551 PHE A CA    1 
ATOM   816   C  C     . PHE A 1 1551 ? 77.067  48.706  120.375 1.00 26.14  ? 1551 PHE A C     1 
ATOM   817   O  O     . PHE A 1 1551 ? 77.409  47.555  120.076 1.00 33.97  ? 1551 PHE A O     1 
ATOM   818   C  CB    . PHE A 1 1551 ? 79.251  49.705  119.663 1.00 16.25  ? 1551 PHE A CB    1 
ATOM   819   C  CG    . PHE A 1 1551 ? 79.955  50.613  118.694 1.00 15.02  ? 1551 PHE A CG    1 
ATOM   820   C  CD1   . PHE A 1 1551 ? 80.087  50.255  117.362 1.00 17.44  ? 1551 PHE A CD1   1 
ATOM   821   C  CD2   . PHE A 1 1551 ? 80.490  51.818  119.113 1.00 12.89  ? 1551 PHE A CD2   1 
ATOM   822   C  CE1   . PHE A 1 1551 ? 80.733  51.086  116.467 1.00 15.21  ? 1551 PHE A CE1   1 
ATOM   823   C  CE2   . PHE A 1 1551 ? 81.138  52.653  118.224 1.00 10.46  ? 1551 PHE A CE2   1 
ATOM   824   C  CZ    . PHE A 1 1551 ? 81.260  52.286  116.900 1.00 16.57  ? 1551 PHE A CZ    1 
ATOM   825   N  N     . THR A 1 1552 ? 76.134  48.962  121.287 1.00 26.67  ? 1552 THR A N     1 
ATOM   826   C  CA    . THR A 1 1552 ? 75.350  47.902  121.913 1.00 31.05  ? 1552 THR A CA    1 
ATOM   827   C  C     . THR A 1 1552 ? 73.846  48.058  121.730 1.00 45.30  ? 1552 THR A C     1 
ATOM   828   O  O     . THR A 1 1552 ? 73.167  47.050  121.509 1.00 47.79  ? 1552 THR A O     1 
ATOM   829   C  CB    . THR A 1 1552 ? 75.667  47.825  123.415 1.00 33.77  ? 1552 THR A CB    1 
ATOM   830   O  OG1   . THR A 1 1552 ? 77.047  47.486  123.596 1.00 33.84  ? 1552 THR A OG1   1 
ATOM   831   C  CG2   . THR A 1 1552 ? 74.805  46.779  124.107 1.00 33.88  ? 1552 THR A CG2   1 
ATOM   832   N  N     . GLY A 1 1553 ? 73.302  49.271  121.776 1.00 41.52  ? 1553 GLY A N     1 
ATOM   833   C  CA    . GLY A 1 1553 ? 71.882  49.501  121.640 1.00 46.58  ? 1553 GLY A CA    1 
ATOM   834   C  C     . GLY A 1 1553 ? 71.360  49.602  120.227 1.00 50.25  ? 1553 GLY A C     1 
ATOM   835   O  O     . GLY A 1 1553 ? 70.154  49.795  120.039 1.00 56.83  ? 1553 GLY A O     1 
ATOM   836   N  N     . SER A 1 1554 ? 72.221  49.481  119.219 1.00 48.19  ? 1554 SER A N     1 
ATOM   837   C  CA    . SER A 1 1554 ? 71.799  49.549  117.822 1.00 59.90  ? 1554 SER A CA    1 
ATOM   838   C  C     . SER A 1 1554 ? 72.511  48.447  117.051 1.00 58.60  ? 1554 SER A C     1 
ATOM   839   O  O     . SER A 1 1554 ? 73.733  48.498  116.878 1.00 56.10  ? 1554 SER A O     1 
ATOM   840   C  CB    . SER A 1 1554 ? 72.099  50.920  117.216 1.00 58.64  ? 1554 SER A CB    1 
ATOM   841   O  OG    . SER A 1 1554 ? 73.493  51.165  117.172 1.00 53.83  ? 1554 SER A OG    1 
ATOM   842   N  N     . ALA A 1 1555 ? 71.750  47.452  116.591 1.00 64.56  ? 1555 ALA A N     1 
ATOM   843   C  CA    . ALA A 1 1555 ? 72.322  46.364  115.810 1.00 67.16  ? 1555 ALA A CA    1 
ATOM   844   C  C     . ALA A 1 1555 ? 72.529  46.732  114.347 1.00 63.47  ? 1555 ALA A C     1 
ATOM   845   O  O     . ALA A 1 1555 ? 73.267  46.033  113.646 1.00 64.62  ? 1555 ALA A O     1 
ATOM   846   C  CB    . ALA A 1 1555 ? 71.434  45.122  115.906 1.00 67.91  ? 1555 ALA A CB    1 
ATOM   847   N  N     . ASP A 1 1556 ? 71.896  47.808  113.873 1.00 62.87  ? 1556 ASP A N     1 
ATOM   848   C  CA    . ASP A 1 1556 ? 72.052  48.200  112.476 1.00 64.61  ? 1556 ASP A CA    1 
ATOM   849   C  C     . ASP A 1 1556 ? 73.438  48.769  112.199 1.00 59.57  ? 1556 ASP A C     1 
ATOM   850   O  O     . ASP A 1 1556 ? 73.963  48.602  111.092 1.00 58.55  ? 1556 ASP A O     1 
ATOM   851   C  CB    . ASP A 1 1556 ? 70.975  49.214  112.092 1.00 65.12  ? 1556 ASP A CB    1 
ATOM   852   C  CG    . ASP A 1 1556 ? 70.823  50.320  113.117 1.00 69.31  ? 1556 ASP A CG    1 
ATOM   853   O  OD1   . ASP A 1 1556 ? 70.467  50.013  114.274 1.00 68.79  ? 1556 ASP A OD1   1 
ATOM   854   O  OD2   . ASP A 1 1556 ? 71.059  51.495  112.766 1.00 66.76  ? 1556 ASP A OD2   1 
ATOM   855   N  N     . ILE A 1 1557 ? 74.041  49.443  113.182 1.00 55.20  ? 1557 ILE A N     1 
ATOM   856   C  CA    . ILE A 1 1557 ? 75.355  50.043  112.971 1.00 51.41  ? 1557 ILE A CA    1 
ATOM   857   C  C     . ILE A 1 1557 ? 76.421  48.972  112.776 1.00 51.55  ? 1557 ILE A C     1 
ATOM   858   O  O     . ILE A 1 1557 ? 77.437  49.214  112.111 1.00 46.43  ? 1557 ILE A O     1 
ATOM   859   C  CB    . ILE A 1 1557 ? 75.703  50.995  114.133 1.00 44.39  ? 1557 ILE A CB    1 
ATOM   860   C  CG1   . ILE A 1 1557 ? 76.811  51.965  113.715 1.00 38.47  ? 1557 ILE A CG1   1 
ATOM   861   C  CG2   . ILE A 1 1557 ? 76.107  50.219  115.379 1.00 39.93  ? 1557 ILE A CG2   1 
ATOM   862   C  CD1   . ILE A 1 1557 ? 77.153  52.990  114.771 1.00 32.20  ? 1557 ILE A CD1   1 
ATOM   863   N  N     . LYS A 1 1558 ? 76.221  47.782  113.346 1.00 51.71  ? 1558 LYS A N     1 
ATOM   864   C  CA    . LYS A 1 1558 ? 77.196  46.707  113.193 1.00 48.65  ? 1558 LYS A CA    1 
ATOM   865   C  C     . LYS A 1 1558 ? 77.318  46.286  111.733 1.00 48.99  ? 1558 LYS A C     1 
ATOM   866   O  O     . LYS A 1 1558 ? 78.424  46.113  111.210 1.00 42.15  ? 1558 LYS A O     1 
ATOM   867   C  CB    . LYS A 1 1558 ? 76.804  45.519  114.073 1.00 48.05  ? 1558 LYS A CB    1 
ATOM   868   C  CG    . LYS A 1 1558 ? 77.791  44.367  114.029 1.00 50.61  ? 1558 LYS A CG    1 
ATOM   869   C  CD    . LYS A 1 1558 ? 77.408  43.269  115.006 1.00 55.99  ? 1558 LYS A CD    1 
ATOM   870   C  CE    . LYS A 1 1558 ? 78.312  42.059  114.851 1.00 54.19  ? 1558 LYS A CE    1 
ATOM   871   N  NZ    . LYS A 1 1558 ? 79.716  42.369  115.239 1.00 46.06  ? 1558 LYS A NZ    1 
ATOM   872   N  N     . HIS A 1 1559 ? 76.180  46.113  111.056 1.00 58.56  ? 1559 HIS A N     1 
ATOM   873   C  CA    . HIS A 1 1559 ? 76.213  45.815  109.628 1.00 59.62  ? 1559 HIS A CA    1 
ATOM   874   C  C     . HIS A 1 1559 ? 76.620  47.041  108.821 1.00 53.89  ? 1559 HIS A C     1 
ATOM   875   O  O     . HIS A 1 1559 ? 77.328  46.926  107.814 1.00 53.49  ? 1559 HIS A O     1 
ATOM   876   C  CB    . HIS A 1 1559 ? 74.851  45.297  109.165 1.00 64.18  ? 1559 HIS A CB    1 
ATOM   877   C  CG    . HIS A 1 1559 ? 74.231  44.304  110.097 1.00 74.28  ? 1559 HIS A CG    1 
ATOM   878   N  ND1   . HIS A 1 1559 ? 73.389  44.671  111.124 1.00 77.94  ? 1559 HIS A ND1   1 
ATOM   879   C  CD2   . HIS A 1 1559 ? 74.331  42.955  110.157 1.00 78.33  ? 1559 HIS A CD2   1 
ATOM   880   C  CE1   . HIS A 1 1559 ? 72.997  43.591  111.777 1.00 81.41  ? 1559 HIS A CE1   1 
ATOM   881   N  NE2   . HIS A 1 1559 ? 73.554  42.537  111.210 1.00 88.32  ? 1559 HIS A NE2   1 
ATOM   882   N  N     . LEU A 1 1560 ? 76.172  48.225  109.245 1.00 52.53  ? 1560 LEU A N     1 
ATOM   883   C  CA    . LEU A 1 1560 ? 76.492  49.449  108.518 1.00 52.14  ? 1560 LEU A CA    1 
ATOM   884   C  C     . LEU A 1 1560 ? 77.985  49.754  108.566 1.00 54.61  ? 1560 LEU A C     1 
ATOM   885   O  O     . LEU A 1 1560 ? 78.580  50.142  107.554 1.00 54.80  ? 1560 LEU A O     1 
ATOM   886   C  CB    . LEU A 1 1560 ? 75.681  50.613  109.088 1.00 53.92  ? 1560 LEU A CB    1 
ATOM   887   C  CG    . LEU A 1 1560 ? 76.060  52.032  108.665 1.00 59.87  ? 1560 LEU A CG    1 
ATOM   888   C  CD1   . LEU A 1 1560 ? 75.809  52.238  107.180 1.00 59.74  ? 1560 LEU A CD1   1 
ATOM   889   C  CD2   . LEU A 1 1560 ? 75.285  53.047  109.490 1.00 53.64  ? 1560 LEU A CD2   1 
ATOM   890   N  N     . LEU A 1 1561 ? 78.608  49.585  109.731 1.00 52.26  ? 1561 LEU A N     1 
ATOM   891   C  CA    . LEU A 1 1561 ? 80.024  49.892  109.935 1.00 45.62  ? 1561 LEU A CA    1 
ATOM   892   C  C     . LEU A 1 1561 ? 80.718  48.694  110.570 1.00 45.11  ? 1561 LEU A C     1 
ATOM   893   O  O     . LEU A 1 1561 ? 80.955  48.668  111.783 1.00 42.24  ? 1561 LEU A O     1 
ATOM   894   C  CB    . LEU A 1 1561 ? 80.193  51.141  110.801 1.00 45.30  ? 1561 LEU A CB    1 
ATOM   895   C  CG    . LEU A 1 1561 ? 79.399  52.378  110.382 1.00 49.96  ? 1561 LEU A CG    1 
ATOM   896   C  CD1   . LEU A 1 1561 ? 79.447  53.437  111.470 1.00 43.80  ? 1561 LEU A CD1   1 
ATOM   897   C  CD2   . LEU A 1 1561 ? 79.942  52.923  109.074 1.00 46.39  ? 1561 LEU A CD2   1 
ATOM   898   N  N     . PRO A 1 1562 ? 81.062  47.680  109.772 1.00 44.77  ? 1562 PRO A N     1 
ATOM   899   C  CA    . PRO A 1 1562 ? 81.703  46.488  110.359 1.00 41.98  ? 1562 PRO A CA    1 
ATOM   900   C  C     . PRO A 1 1562 ? 83.117  46.741  110.859 1.00 35.86  ? 1562 PRO A C     1 
ATOM   901   O  O     . PRO A 1 1562 ? 83.477  46.283  111.953 1.00 32.93  ? 1562 PRO A O     1 
ATOM   902   C  CB    . PRO A 1 1562 ? 81.668  45.480  109.202 1.00 39.29  ? 1562 PRO A CB    1 
ATOM   903   C  CG    . PRO A 1 1562 ? 81.654  46.325  107.971 1.00 43.65  ? 1562 PRO A CG    1 
ATOM   904   C  CD    . PRO A 1 1562 ? 80.853  47.546  108.320 1.00 38.96  ? 1562 PRO A CD    1 
ATOM   905   N  N     . VAL A 1 1563 ? 83.935  47.455  110.082 1.00 40.63  ? 1563 VAL A N     1 
ATOM   906   C  CA    . VAL A 1 1563 ? 85.320  47.700  110.479 1.00 42.25  ? 1563 VAL A CA    1 
ATOM   907   C  C     . VAL A 1 1563 ? 85.368  48.540  111.749 1.00 38.61  ? 1563 VAL A C     1 
ATOM   908   O  O     . VAL A 1 1563 ? 86.108  48.234  112.692 1.00 38.46  ? 1563 VAL A O     1 
ATOM   909   C  CB    . VAL A 1 1563 ? 86.097  48.369  109.330 1.00 45.99  ? 1563 VAL A CB    1 
ATOM   910   C  CG1   . VAL A 1 1563 ? 87.467  48.825  109.806 1.00 42.27  ? 1563 VAL A CG1   1 
ATOM   911   C  CG2   . VAL A 1 1563 ? 86.225  47.417  108.152 1.00 47.23  ? 1563 VAL A CG2   1 
ATOM   912   N  N     . GLU A 1 1564 ? 84.571  49.611  111.792 1.00 38.08  ? 1564 GLU A N     1 
ATOM   913   C  CA    . GLU A 1 1564 ? 84.518  50.449  112.985 1.00 37.68  ? 1564 GLU A CA    1 
ATOM   914   C  C     . GLU A 1 1564 ? 83.990  49.666  114.180 1.00 30.83  ? 1564 GLU A C     1 
ATOM   915   O  O     . GLU A 1 1564 ? 84.478  49.831  115.306 1.00 28.53  ? 1564 GLU A O     1 
ATOM   916   C  CB    . GLU A 1 1564 ? 83.654  51.689  112.733 1.00 34.60  ? 1564 GLU A CB    1 
ATOM   917   C  CG    . GLU A 1 1564 ? 84.170  52.666  111.667 1.00 43.07  ? 1564 GLU A CG    1 
ATOM   918   C  CD    . GLU A 1 1564 ? 84.250  52.073  110.272 1.00 55.31  ? 1564 GLU A CD    1 
ATOM   919   O  OE1   . GLU A 1 1564 ? 83.204  51.639  109.745 1.00 56.03  ? 1564 GLU A OE1   1 
ATOM   920   O  OE2   . GLU A 1 1564 ? 85.359  52.045  109.699 1.00 63.03  ? 1564 GLU A OE2   1 
ATOM   921   N  N     . THR A 1 1565 ? 82.993  48.808  113.954 1.00 27.55  ? 1565 THR A N     1 
ATOM   922   C  CA    . THR A 1 1565 ? 82.445  48.005  115.042 1.00 26.52  ? 1565 THR A CA    1 
ATOM   923   C  C     . THR A 1 1565 ? 83.497  47.065  115.618 1.00 30.51  ? 1565 THR A C     1 
ATOM   924   O  O     . THR A 1 1565 ? 83.621  46.940  116.840 1.00 31.77  ? 1565 THR A O     1 
ATOM   925   C  CB    . THR A 1 1565 ? 81.228  47.218  114.553 1.00 27.87  ? 1565 THR A CB    1 
ATOM   926   O  OG1   . THR A 1 1565 ? 80.107  48.102  114.427 1.00 33.56  ? 1565 THR A OG1   1 
ATOM   927   C  CG2   . THR A 1 1565 ? 80.874  46.106  115.528 1.00 25.08  ? 1565 THR A CG2   1 
ATOM   928   N  N     . GLN A 1 1566 ? 84.283  46.414  114.757 1.00 27.95  ? 1566 GLN A N     1 
ATOM   929   C  CA    . GLN A 1 1566 ? 85.316  45.506  115.249 1.00 32.71  ? 1566 GLN A CA    1 
ATOM   930   C  C     . GLN A 1 1566 ? 86.446  46.263  115.944 1.00 30.82  ? 1566 GLN A C     1 
ATOM   931   O  O     . GLN A 1 1566 ? 86.986  45.794  116.957 1.00 30.14  ? 1566 GLN A O     1 
ATOM   932   C  CB    . GLN A 1 1566 ? 85.859  44.659  114.096 1.00 36.38  ? 1566 GLN A CB    1 
ATOM   933   C  CG    . GLN A 1 1566 ? 86.793  43.532  114.519 1.00 38.87  ? 1566 GLN A CG    1 
ATOM   934   C  CD    . GLN A 1 1566 ? 88.236  43.977  114.658 1.00 45.03  ? 1566 GLN A CD    1 
ATOM   935   O  OE1   . GLN A 1 1566 ? 88.681  44.901  113.977 1.00 45.91  ? 1566 GLN A OE1   1 
ATOM   936   N  NE2   . GLN A 1 1566 ? 88.974  43.319  115.543 1.00 44.76  ? 1566 GLN A NE2   1 
ATOM   937   N  N     . ARG A 1 1567 ? 86.818  47.430  115.411 1.00 29.43  ? 1567 ARG A N     1 
ATOM   938   C  CA    . ARG A 1 1567 ? 87.824  48.254  116.071 1.00 28.22  ? 1567 ARG A CA    1 
ATOM   939   C  C     . ARG A 1 1567 ? 87.370  48.635  117.473 1.00 31.25  ? 1567 ARG A C     1 
ATOM   940   O  O     . ARG A 1 1567 ? 88.123  48.492  118.446 1.00 37.02  ? 1567 ARG A O     1 
ATOM   941   C  CB    . ARG A 1 1567 ? 88.110  49.502  115.234 1.00 26.92  ? 1567 ARG A CB    1 
ATOM   942   C  CG    . ARG A 1 1567 ? 88.827  49.218  113.925 1.00 39.08  ? 1567 ARG A CG    1 
ATOM   943   C  CD    . ARG A 1 1567 ? 89.145  50.497  113.167 1.00 47.37  ? 1567 ARG A CD    1 
ATOM   944   N  NE    . ARG A 1 1567 ? 90.046  51.375  113.902 1.00 54.45  ? 1567 ARG A NE    1 
ATOM   945   C  CZ    . ARG A 1 1567 ? 90.470  52.550  113.459 1.00 60.24  ? 1567 ARG A CZ    1 
ATOM   946   N  NH1   . ARG A 1 1567 ? 90.092  53.023  112.282 1.00 62.15  ? 1567 ARG A NH1   1 
ATOM   947   N  NH2   . ARG A 1 1567 ? 91.295  53.270  114.214 1.00 56.94  ? 1567 ARG A NH2   1 
ATOM   948   N  N     . PHE A 1 1568 ? 86.122  49.096  117.599 1.00 26.71  ? 1568 PHE A N     1 
ATOM   949   C  CA    . PHE A 1 1568 ? 85.603  49.426  118.919 1.00 23.32  ? 1568 PHE A CA    1 
ATOM   950   C  C     . PHE A 1 1568 ? 85.482  48.188  119.797 1.00 23.31  ? 1568 PHE A C     1 
ATOM   951   O  O     . PHE A 1 1568 ? 85.606  48.291  121.018 1.00 24.04  ? 1568 PHE A O     1 
ATOM   952   C  CB    . PHE A 1 1568 ? 84.249  50.128  118.812 1.00 19.81  ? 1568 PHE A CB    1 
ATOM   953   C  CG    . PHE A 1 1568 ? 83.560  50.293  120.135 1.00 15.15  ? 1568 PHE A CG    1 
ATOM   954   C  CD1   . PHE A 1 1568 ? 83.851  51.376  120.947 1.00 11.55  ? 1568 PHE A CD1   1 
ATOM   955   C  CD2   . PHE A 1 1568 ? 82.634  49.361  120.576 1.00 11.89  ? 1568 PHE A CD2   1 
ATOM   956   C  CE1   . PHE A 1 1568 ? 83.233  51.527  122.168 1.00 9.63   ? 1568 PHE A CE1   1 
ATOM   957   C  CE2   . PHE A 1 1568 ? 82.015  49.509  121.798 1.00 13.09  ? 1568 PHE A CE2   1 
ATOM   958   C  CZ    . PHE A 1 1568 ? 82.315  50.593  122.593 1.00 12.91  ? 1568 PHE A CZ    1 
ATOM   959   N  N     . GLN A 1 1569 ? 85.223  47.022  119.204 1.00 27.98  ? 1569 GLN A N     1 
ATOM   960   C  CA    . GLN A 1 1569 ? 85.170  45.790  119.984 1.00 31.62  ? 1569 GLN A CA    1 
ATOM   961   C  C     . GLN A 1 1569 ? 86.515  45.503  120.639 1.00 30.63  ? 1569 GLN A C     1 
ATOM   962   O  O     . GLN A 1 1569 ? 86.586  45.192  121.833 1.00 30.41  ? 1569 GLN A O     1 
ATOM   963   C  CB    . GLN A 1 1569 ? 84.743  44.627  119.087 1.00 36.31  ? 1569 GLN A CB    1 
ATOM   964   C  CG    . GLN A 1 1569 ? 84.772  43.270  119.767 1.00 44.65  ? 1569 GLN A CG    1 
ATOM   965   C  CD    . GLN A 1 1569 ? 83.975  43.247  121.054 1.00 46.69  ? 1569 GLN A CD    1 
ATOM   966   O  OE1   . GLN A 1 1569 ? 82.769  43.490  121.055 1.00 41.36  ? 1569 GLN A OE1   1 
ATOM   967   N  NE2   . GLN A 1 1569 ? 84.647  42.955  122.160 1.00 45.64  ? 1569 GLN A NE2   1 
ATOM   968   N  N     . SER A 1 1570 ? 87.598  45.618  119.867 1.00 29.09  ? 1570 SER A N     1 
ATOM   969   C  CA    . SER A 1 1570 ? 88.932  45.434  120.441 1.00 29.61  ? 1570 SER A CA    1 
ATOM   970   C  C     . SER A 1 1570 ? 89.232  46.495  121.496 1.00 31.40  ? 1570 SER A C     1 
ATOM   971   O  O     . SER A 1 1570 ? 89.787  46.188  122.566 1.00 37.37  ? 1570 SER A O     1 
ATOM   972   C  CB    . SER A 1 1570 ? 89.987  45.465  119.336 1.00 31.82  ? 1570 SER A CB    1 
ATOM   973   O  OG    . SER A 1 1570 ? 89.642  44.593  118.275 1.00 37.59  ? 1570 SER A OG    1 
ATOM   974   N  N     . ILE A 1 1571 ? 88.871  47.748  121.208 1.00 26.85  ? 1571 ILE A N     1 
ATOM   975   C  CA    . ILE A 1 1571 ? 89.099  48.832  122.158 1.00 23.98  ? 1571 ILE A CA    1 
ATOM   976   C  C     . ILE A 1 1571 ? 88.380  48.550  123.469 1.00 24.05  ? 1571 ILE A C     1 
ATOM   977   O  O     . ILE A 1 1571 ? 88.948  48.714  124.553 1.00 24.13  ? 1571 ILE A O     1 
ATOM   978   C  CB    . ILE A 1 1571 ? 88.642  50.169  121.551 1.00 22.44  ? 1571 ILE A CB    1 
ATOM   979   C  CG1   . ILE A 1 1571 ? 89.463  50.509  120.311 1.00 22.01  ? 1571 ILE A CG1   1 
ATOM   980   C  CG2   . ILE A 1 1571 ? 88.772  51.278  122.575 1.00 21.42  ? 1571 ILE A CG2   1 
ATOM   981   C  CD1   . ILE A 1 1571 ? 88.892  51.662  119.525 1.00 22.92  ? 1571 ILE A CD1   1 
ATOM   982   N  N     . SER A 1 1572 ? 87.122  48.113  123.387 1.00 21.17  ? 1572 SER A N     1 
ATOM   983   C  CA    . SER A 1 1572 ? 86.333  47.844  124.582 1.00 21.04  ? 1572 SER A CA    1 
ATOM   984   C  C     . SER A 1 1572 ? 86.852  46.621  125.321 1.00 24.77  ? 1572 SER A C     1 
ATOM   985   O  O     . SER A 1 1572 ? 86.775  46.557  126.549 1.00 24.73  ? 1572 SER A O     1 
ATOM   986   C  CB    . SER A 1 1572 ? 84.862  47.664  124.205 1.00 18.96  ? 1572 SER A CB    1 
ATOM   987   O  OG    . SER A 1 1572 ? 84.046  47.553  125.358 1.00 27.63  ? 1572 SER A OG    1 
ATOM   988   N  N     . THR A 1 1573 ? 87.379  45.634  124.594 1.00 27.66  ? 1573 THR A N     1 
ATOM   989   C  CA    . THR A 1 1573 ? 87.992  44.486  125.255 1.00 28.67  ? 1573 THR A CA    1 
ATOM   990   C  C     . THR A 1 1573 ? 89.169  44.926  126.117 1.00 26.59  ? 1573 THR A C     1 
ATOM   991   O  O     . THR A 1 1573 ? 89.265  44.564  127.299 1.00 24.16  ? 1573 THR A O     1 
ATOM   992   C  CB    . THR A 1 1573 ? 88.438  43.459  124.215 1.00 32.36  ? 1573 THR A CB    1 
ATOM   993   O  OG1   . THR A 1 1573 ? 87.308  43.042  123.439 1.00 37.39  ? 1573 THR A OG1   1 
ATOM   994   C  CG2   . THR A 1 1573 ? 89.055  42.246  124.894 1.00 34.24  ? 1573 THR A CG2   1 
ATOM   995   N  N     . GLU A 1 1574 ? 90.063  45.738  125.545 1.00 26.17  ? 1574 GLU A N     1 
ATOM   996   C  CA    . GLU A 1 1574 ? 91.182  46.255  126.330 1.00 27.51  ? 1574 GLU A CA    1 
ATOM   997   C  C     . GLU A 1 1574 ? 90.690  47.129  127.478 1.00 29.08  ? 1574 GLU A C     1 
ATOM   998   O  O     . GLU A 1 1574 ? 91.223  47.069  128.596 1.00 28.48  ? 1574 GLU A O     1 
ATOM   999   C  CB    . GLU A 1 1574 ? 92.137  47.041  125.436 1.00 30.02  ? 1574 GLU A CB    1 
ATOM   1000  C  CG    . GLU A 1 1574 ? 92.864  46.195  124.413 1.00 40.73  ? 1574 GLU A CG    1 
ATOM   1001  C  CD    . GLU A 1 1574 ? 93.785  47.014  123.535 1.00 53.09  ? 1574 GLU A CD    1 
ATOM   1002  O  OE1   . GLU A 1 1574 ? 93.763  48.258  123.643 1.00 47.13  ? 1574 GLU A OE1   1 
ATOM   1003  O  OE2   . GLU A 1 1574 ? 94.527  46.412  122.731 1.00 63.77  ? 1574 GLU A OE2   1 
ATOM   1004  N  N     . PHE A 1 1575 ? 89.665  47.944  127.217 1.00 26.93  ? 1575 PHE A N     1 
ATOM   1005  C  CA    . PHE A 1 1575 ? 89.146  48.855  128.229 1.00 20.84  ? 1575 PHE A CA    1 
ATOM   1006  C  C     . PHE A 1 1575 ? 88.583  48.075  129.412 1.00 20.88  ? 1575 PHE A C     1 
ATOM   1007  O  O     . PHE A 1 1575 ? 88.854  48.406  130.568 1.00 19.76  ? 1575 PHE A O     1 
ATOM   1008  C  CB    . PHE A 1 1575 ? 88.094  49.769  127.587 1.00 17.27  ? 1575 PHE A CB    1 
ATOM   1009  C  CG    . PHE A 1 1575 ? 87.424  50.725  128.539 1.00 15.46  ? 1575 PHE A CG    1 
ATOM   1010  C  CD1   . PHE A 1 1575 ? 86.261  50.379  129.205 1.00 11.24  ? 1575 PHE A CD1   1 
ATOM   1011  C  CD2   . PHE A 1 1575 ? 87.951  51.991  128.740 1.00 17.66  ? 1575 PHE A CD2   1 
ATOM   1012  C  CE1   . PHE A 1 1575 ? 85.651  51.272  130.069 1.00 11.73  ? 1575 PHE A CE1   1 
ATOM   1013  C  CE2   . PHE A 1 1575 ? 87.344  52.885  129.601 1.00 16.61  ? 1575 PHE A CE2   1 
ATOM   1014  C  CZ    . PHE A 1 1575 ? 86.191  52.525  130.264 1.00 14.15  ? 1575 PHE A CZ    1 
ATOM   1015  N  N     . LEU A 1 1576 ? 87.846  46.994  129.137 1.00 24.09  ? 1576 LEU A N     1 
ATOM   1016  C  CA    . LEU A 1 1576 ? 87.264  46.180  130.205 1.00 26.13  ? 1576 LEU A CA    1 
ATOM   1017  C  C     . LEU A 1 1576 ? 88.318  45.358  130.940 1.00 27.77  ? 1576 LEU A C     1 
ATOM   1018  O  O     . LEU A 1 1576 ? 88.170  45.088  132.137 1.00 23.33  ? 1576 LEU A O     1 
ATOM   1019  C  CB    . LEU A 1 1576 ? 86.172  45.264  129.649 1.00 28.99  ? 1576 LEU A CB    1 
ATOM   1020  C  CG    . LEU A 1 1576 ? 84.727  45.773  129.581 1.00 29.35  ? 1576 LEU A CG    1 
ATOM   1021  C  CD1   . LEU A 1 1576 ? 84.585  46.975  128.674 1.00 21.79  ? 1576 LEU A CD1   1 
ATOM   1022  C  CD2   . LEU A 1 1576 ? 83.792  44.655  129.141 1.00 30.76  ? 1576 LEU A CD2   1 
ATOM   1023  N  N     . ALA A 1 1577 ? 89.372  44.920  130.248 1.00 26.02  ? 1577 ALA A N     1 
ATOM   1024  C  CA    . ALA A 1 1577 ? 90.462  44.257  130.960 1.00 28.37  ? 1577 ALA A CA    1 
ATOM   1025  C  C     . ALA A 1 1577 ? 91.118  45.220  131.942 1.00 29.38  ? 1577 ALA A C     1 
ATOM   1026  O  O     . ALA A 1 1577 ? 91.396  44.871  133.099 1.00 29.13  ? 1577 ALA A O     1 
ATOM   1027  C  CB    . ALA A 1 1577 ? 91.488  43.707  129.972 1.00 24.61  ? 1577 ALA A CB    1 
ATOM   1028  N  N     . LEU A 1 1578 ? 91.348  46.454  131.494 1.00 26.04  ? 1578 LEU A N     1 
ATOM   1029  C  CA    . LEU A 1 1578 ? 91.854  47.489  132.385 1.00 23.55  ? 1578 LEU A CA    1 
ATOM   1030  C  C     . LEU A 1 1578 ? 90.868  47.763  133.521 1.00 26.52  ? 1578 LEU A C     1 
ATOM   1031  O  O     . LEU A 1 1578 ? 91.271  48.028  134.659 1.00 29.86  ? 1578 LEU A O     1 
ATOM   1032  C  CB    . LEU A 1 1578 ? 92.143  48.748  131.568 1.00 21.39  ? 1578 LEU A CB    1 
ATOM   1033  C  CG    . LEU A 1 1578 ? 92.551  50.058  132.225 1.00 25.21  ? 1578 LEU A CG    1 
ATOM   1034  C  CD1   . LEU A 1 1578 ? 93.994  49.979  132.664 1.00 24.23  ? 1578 LEU A CD1   1 
ATOM   1035  C  CD2   . LEU A 1 1578 ? 92.376  51.169  131.205 1.00 25.20  ? 1578 LEU A CD2   1 
ATOM   1036  N  N     . MET A 1 1579 ? 89.566  47.695  133.226 1.00 29.51  ? 1579 MET A N     1 
ATOM   1037  C  CA    . MET A 1 1579 ? 88.537  47.856  134.253 1.00 26.11  ? 1579 MET A CA    1 
ATOM   1038  C  C     . MET A 1 1579 ? 88.658  46.795  135.334 1.00 31.72  ? 1579 MET A C     1 
ATOM   1039  O  O     . MET A 1 1579 ? 88.572  47.096  136.530 1.00 35.38  ? 1579 MET A O     1 
ATOM   1040  C  CB    . MET A 1 1579 ? 87.145  47.761  133.625 1.00 37.94  ? 1579 MET A CB    1 
ATOM   1041  C  CG    . MET A 1 1579 ? 86.751  48.847  132.656 1.00 34.31  ? 1579 MET A CG    1 
ATOM   1042  S  SD    . MET A 1 1579 ? 86.706  50.477  133.400 1.00 53.34  ? 1579 MET A SD    1 
ATOM   1043  C  CE    . MET A 1 1579 ? 88.255  51.127  132.788 1.00 25.04  ? 1579 MET A CE    1 
ATOM   1044  N  N     . LYS A 1 1580 ? 88.819  45.541  134.921 1.00 35.14  ? 1580 LYS A N     1 
ATOM   1045  C  CA    . LYS A 1 1580 ? 88.981  44.460  135.881 1.00 37.13  ? 1580 LYS A CA    1 
ATOM   1046  C  C     . LYS A 1 1580 ? 90.247  44.652  136.706 1.00 37.69  ? 1580 LYS A C     1 
ATOM   1047  O  O     . LYS A 1 1580 ? 90.236  44.463  137.930 1.00 35.30  ? 1580 LYS A O     1 
ATOM   1048  C  CB    . LYS A 1 1580 ? 88.976  43.120  135.143 1.00 40.20  ? 1580 LYS A CB    1 
ATOM   1049  C  CG    . LYS A 1 1580 ? 89.122  41.902  136.032 1.00 51.47  ? 1580 LYS A CG    1 
ATOM   1050  C  CD    . LYS A 1 1580 ? 90.576  41.476  136.142 1.00 53.90  ? 1580 LYS A CD    1 
ATOM   1051  C  CE    . LYS A 1 1580 ? 91.042  40.890  134.819 1.00 58.84  ? 1580 LYS A CE    1 
ATOM   1052  N  NZ    . LYS A 1 1580 ? 92.456  40.427  134.823 1.00 64.08  ? 1580 LYS A NZ    1 
ATOM   1053  N  N     . LYS A 1 1581 ? 91.344  45.053  136.057 1.00 36.34  ? 1581 LYS A N     1 
ATOM   1054  C  CA    . LYS A 1 1581 ? 92.586  45.265  136.795 1.00 31.57  ? 1581 LYS A CA    1 
ATOM   1055  C  C     . LYS A 1 1581 ? 92.426  46.372  137.831 1.00 33.31  ? 1581 LYS A C     1 
ATOM   1056  O  O     . LYS A 1 1581 ? 92.950  46.269  138.947 1.00 35.49  ? 1581 LYS A O     1 
ATOM   1057  C  CB    . LYS A 1 1581 ? 93.733  45.584  135.837 1.00 25.08  ? 1581 LYS A CB    1 
ATOM   1058  C  CG    . LYS A 1 1581 ? 94.230  44.389  135.043 1.00 27.57  ? 1581 LYS A CG    1 
ATOM   1059  C  CD    . LYS A 1 1581 ? 95.383  44.782  134.129 1.00 25.19  ? 1581 LYS A CD    1 
ATOM   1060  C  CE    . LYS A 1 1581 ? 94.990  45.891  133.166 1.00 32.26  ? 1581 LYS A CE    1 
ATOM   1061  N  NZ    . LYS A 1 1581 ? 96.043  46.139  132.142 1.00 32.81  ? 1581 LYS A NZ    1 
ATOM   1062  N  N     . VAL A 1 1582 ? 91.707  47.439  137.481 1.00 31.90  ? 1582 VAL A N     1 
ATOM   1063  C  CA    . VAL A 1 1582 ? 91.422  48.489  138.455 1.00 27.85  ? 1582 VAL A CA    1 
ATOM   1064  C  C     . VAL A 1 1582 ? 90.533  47.952  139.570 1.00 33.06  ? 1582 VAL A C     1 
ATOM   1065  O  O     . VAL A 1 1582 ? 90.708  48.295  140.745 1.00 33.03  ? 1582 VAL A O     1 
ATOM   1066  C  CB    . VAL A 1 1582 ? 90.793  49.711  137.758 1.00 26.73  ? 1582 VAL A CB    1 
ATOM   1067  C  CG1   . VAL A 1 1582 ? 90.286  50.716  138.784 1.00 25.87  ? 1582 VAL A CG1   1 
ATOM   1068  C  CG2   . VAL A 1 1582 ? 91.802  50.361  136.831 1.00 27.64  ? 1582 VAL A CG2   1 
ATOM   1069  N  N     . SER A 1 1583 ? 89.576  47.087  139.223 1.00 40.24  ? 1583 SER A N     1 
ATOM   1070  C  CA    . SER A 1 1583 ? 88.672  46.543  140.231 1.00 39.79  ? 1583 SER A CA    1 
ATOM   1071  C  C     . SER A 1 1583 ? 89.415  45.708  141.266 1.00 47.06  ? 1583 SER A C     1 
ATOM   1072  O  O     . SER A 1 1583 ? 89.088  45.772  142.456 1.00 49.88  ? 1583 SER A O     1 
ATOM   1073  C  CB    . SER A 1 1583 ? 87.577  45.708  139.569 1.00 43.51  ? 1583 SER A CB    1 
ATOM   1074  O  OG    . SER A 1 1583 ? 86.691  45.181  140.541 1.00 53.28  ? 1583 SER A OG    1 
ATOM   1075  N  N     . LYS A 1 1584 ? 90.405  44.919  140.842 1.00 43.59  ? 1584 LYS A N     1 
ATOM   1076  C  CA    . LYS A 1 1584 ? 91.157  44.118  141.808 1.00 44.51  ? 1584 LYS A CA    1 
ATOM   1077  C  C     . LYS A 1 1584 ? 91.927  44.996  142.791 1.00 47.99  ? 1584 LYS A C     1 
ATOM   1078  O  O     . LYS A 1 1584 ? 91.989  44.692  143.988 1.00 48.45  ? 1584 LYS A O     1 
ATOM   1079  C  CB    . LYS A 1 1584 ? 92.104  43.149  141.097 1.00 45.06  ? 1584 LYS A CB    1 
ATOM   1080  C  CG    . LYS A 1 1584 ? 91.454  42.290  140.031 1.00 50.34  ? 1584 LYS A CG    1 
ATOM   1081  C  CD    . LYS A 1 1584 ? 90.258  41.551  140.612 1.00 58.72  ? 1584 LYS A CD    1 
ATOM   1082  C  CE    . LYS A 1 1584 ? 89.506  40.768  139.552 1.00 61.57  ? 1584 LYS A CE    1 
ATOM   1083  N  NZ    . LYS A 1 1584 ? 90.394  39.787  138.866 1.00 57.82  ? 1584 LYS A NZ    1 
ATOM   1084  N  N     . SER A 1 1585 ? 92.527  46.083  142.309 1.00 44.84  ? 1585 SER A N     1 
ATOM   1085  C  CA    . SER A 1 1585 ? 93.316  46.989  143.145 1.00 40.01  ? 1585 SER A CA    1 
ATOM   1086  C  C     . SER A 1 1585 ? 92.815  48.414  142.954 1.00 36.54  ? 1585 SER A C     1 
ATOM   1087  O  O     . SER A 1 1585 ? 93.372  49.182  142.158 1.00 34.56  ? 1585 SER A O     1 
ATOM   1088  C  CB    . SER A 1 1585 ? 94.807  46.882  142.822 1.00 42.45  ? 1585 SER A CB    1 
ATOM   1089  O  OG    . SER A 1 1585 ? 95.289  45.570  143.053 1.00 51.87  ? 1585 SER A OG    1 
ATOM   1090  N  N     . PRO A 1 1586 ? 91.756  48.803  143.670 1.00 37.78  ? 1586 PRO A N     1 
ATOM   1091  C  CA    . PRO A 1 1586 ? 91.229  50.171  143.526 1.00 38.38  ? 1586 PRO A CA    1 
ATOM   1092  C  C     . PRO A 1 1586 ? 92.138  51.253  144.093 1.00 39.15  ? 1586 PRO A C     1 
ATOM   1093  O  O     . PRO A 1 1586 ? 91.856  52.437  143.875 1.00 36.44  ? 1586 PRO A O     1 
ATOM   1094  C  CB    . PRO A 1 1586 ? 89.895  50.115  144.282 1.00 36.60  ? 1586 PRO A CB    1 
ATOM   1095  C  CG    . PRO A 1 1586 ? 90.066  48.999  145.256 1.00 38.70  ? 1586 PRO A CG    1 
ATOM   1096  C  CD    . PRO A 1 1586 ? 90.916  47.979  144.555 1.00 38.36  ? 1586 PRO A CD    1 
ATOM   1097  N  N     . LEU A 1 1587 ? 93.195  50.895  144.821 1.00 42.76  ? 1587 LEU A N     1 
ATOM   1098  C  CA    . LEU A 1 1587 ? 94.101  51.901  145.365 1.00 38.04  ? 1587 LEU A CA    1 
ATOM   1099  C  C     . LEU A 1 1587 ? 94.770  52.688  144.246 1.00 36.09  ? 1587 LEU A C     1 
ATOM   1100  O  O     . LEU A 1 1587 ? 95.202  52.125  143.238 1.00 38.51  ? 1587 LEU A O     1 
ATOM   1101  C  CB    . LEU A 1 1587 ? 95.157  51.243  146.255 1.00 40.86  ? 1587 LEU A CB    1 
ATOM   1102  C  CG    . LEU A 1 1587 ? 94.705  50.920  147.680 1.00 44.74  ? 1587 LEU A CG    1 
ATOM   1103  C  CD1   . LEU A 1 1587 ? 95.612  49.879  148.315 1.00 52.16  ? 1587 LEU A CD1   1 
ATOM   1104  C  CD2   . LEU A 1 1587 ? 94.660  52.187  148.523 1.00 37.43  ? 1587 LEU A CD2   1 
ATOM   1105  N  N     . VAL A 1 1588 ? 94.854  54.006  144.440 1.00 33.14  ? 1588 VAL A N     1 
ATOM   1106  C  CA    . VAL A 1 1588 ? 95.355  54.894  143.394 1.00 31.72  ? 1588 VAL A CA    1 
ATOM   1107  C  C     . VAL A 1 1588 ? 96.825  54.623  143.108 1.00 32.32  ? 1588 VAL A C     1 
ATOM   1108  O  O     . VAL A 1 1588 ? 97.271  54.695  141.956 1.00 32.75  ? 1588 VAL A O     1 
ATOM   1109  C  CB    . VAL A 1 1588 ? 95.115  56.362  143.789 1.00 29.83  ? 1588 VAL A CB    1 
ATOM   1110  C  CG1   . VAL A 1 1588 ? 95.587  57.297  142.691 1.00 20.75  ? 1588 VAL A CG1   1 
ATOM   1111  C  CG2   . VAL A 1 1588 ? 93.644  56.580  144.074 1.00 32.68  ? 1588 VAL A CG2   1 
ATOM   1112  N  N     . MET A 1 1589 ? 97.604  54.319  144.146 1.00 33.08  ? 1589 MET A N     1 
ATOM   1113  C  CA    . MET A 1 1589 ? 99.035  54.113  143.955 1.00 27.61  ? 1589 MET A CA    1 
ATOM   1114  C  C     . MET A 1 1589 ? 99.294  52.897  143.071 1.00 31.64  ? 1589 MET A C     1 
ATOM   1115  O  O     . MET A 1 1589 ? 100.123 52.943  142.155 1.00 40.47  ? 1589 MET A O     1 
ATOM   1116  C  CB    . MET A 1 1589 ? 99.728  53.953  145.310 1.00 25.31  ? 1589 MET A CB    1 
ATOM   1117  C  CG    . MET A 1 1589 ? 99.856  55.234  146.151 1.00 30.46  ? 1589 MET A CG    1 
ATOM   1118  S  SD    . MET A 1 1589 ? 100.261 56.812  145.358 1.00 42.31  ? 1589 MET A SD    1 
ATOM   1119  C  CE    . MET A 1 1589 ? 101.548 56.362  144.195 1.00 32.63  ? 1589 MET A CE    1 
ATOM   1120  N  N     . ASP A 1 1590 ? 98.579  51.798  143.326 1.00 32.44  ? 1590 ASP A N     1 
ATOM   1121  C  CA    . ASP A 1 1590 ? 98.777  50.578  142.549 1.00 36.51  ? 1590 ASP A CA    1 
ATOM   1122  C  C     . ASP A 1 1590 ? 98.270  50.759  141.120 1.00 36.80  ? 1590 ASP A C     1 
ATOM   1123  O  O     . ASP A 1 1590 ? 98.855  50.228  140.169 1.00 40.46  ? 1590 ASP A O     1 
ATOM   1124  C  CB    . ASP A 1 1590 ? 98.084  49.403  143.248 1.00 40.68  ? 1590 ASP A CB    1 
ATOM   1125  C  CG    . ASP A 1 1590 ? 98.420  48.053  142.622 1.00 58.04  ? 1590 ASP A CG    1 
ATOM   1126  O  OD1   . ASP A 1 1590 ? 99.164  48.007  141.622 1.00 53.18  ? 1590 ASP A OD1   1 
ATOM   1127  O  OD2   . ASP A 1 1590 ? 97.954  47.024  143.155 1.00 65.53  ? 1590 ASP A OD2   1 
ATOM   1128  N  N     . VAL A 1 1591 ? 97.177  51.509  140.950 1.00 31.84  ? 1591 VAL A N     1 
ATOM   1129  C  CA    . VAL A 1 1591 ? 96.708  51.835  139.605 1.00 29.34  ? 1591 VAL A CA    1 
ATOM   1130  C  C     . VAL A 1 1591 ? 97.770  52.625  138.853 1.00 30.33  ? 1591 VAL A C     1 
ATOM   1131  O  O     . VAL A 1 1591 ? 98.052  52.357  137.678 1.00 34.55  ? 1591 VAL A O     1 
ATOM   1132  C  CB    . VAL A 1 1591 ? 95.370  52.597  139.668 1.00 31.60  ? 1591 VAL A CB    1 
ATOM   1133  C  CG1   . VAL A 1 1591 ? 94.968  53.087  138.284 1.00 25.97  ? 1591 VAL A CG1   1 
ATOM   1134  C  CG2   . VAL A 1 1591 ? 94.284  51.710  140.245 1.00 31.60  ? 1591 VAL A CG2   1 
ATOM   1135  N  N     . LEU A 1 1592 ? 98.382  53.605  139.520 1.00 27.03  ? 1592 LEU A N     1 
ATOM   1136  C  CA    . LEU A 1 1592 ? 99.481  54.353  138.924 1.00 29.33  ? 1592 LEU A CA    1 
ATOM   1137  C  C     . LEU A 1 1592 ? 100.690 53.471  138.643 1.00 30.63  ? 1592 LEU A C     1 
ATOM   1138  O  O     . LEU A 1 1592 ? 101.460 53.767  137.722 1.00 30.97  ? 1592 LEU A O     1 
ATOM   1139  C  CB    . LEU A 1 1592 ? 99.875  55.510  139.843 1.00 26.96  ? 1592 LEU A CB    1 
ATOM   1140  C  CG    . LEU A 1 1592 ? 100.959 56.471  139.355 1.00 29.02  ? 1592 LEU A CG    1 
ATOM   1141  C  CD1   . LEU A 1 1592 ? 100.448 57.295  138.185 1.00 22.57  ? 1592 LEU A CD1   1 
ATOM   1142  C  CD2   . LEU A 1 1592 ? 101.430 57.367  140.487 1.00 23.09  ? 1592 LEU A CD2   1 
ATOM   1143  N  N     . ASN A 1 1593 ? 100.868 52.394  139.408 1.00 36.06  ? 1593 ASN A N     1 
ATOM   1144  C  CA    . ASN A 1 1593 ? 101.978 51.471  139.221 1.00 36.74  ? 1593 ASN A CA    1 
ATOM   1145  C  C     . ASN A 1 1593 ? 101.678 50.360  138.222 1.00 35.70  ? 1593 ASN A C     1 
ATOM   1146  O  O     . ASN A 1 1593 ? 102.532 49.490  138.019 1.00 40.18  ? 1593 ASN A O     1 
ATOM   1147  C  CB    . ASN A 1 1593 ? 102.384 50.850  140.563 1.00 39.41  ? 1593 ASN A CB    1 
ATOM   1148  C  CG    . ASN A 1 1593 ? 102.881 51.882  141.556 1.00 42.67  ? 1593 ASN A CG    1 
ATOM   1149  O  OD1   . ASN A 1 1593 ? 102.965 53.070  141.245 1.00 39.03  ? 1593 ASN A OD1   1 
ATOM   1150  N  ND2   . ASN A 1 1593 ? 103.210 51.433  142.762 1.00 43.62  ? 1593 ASN A ND2   1 
ATOM   1151  N  N     . ILE A 1 1594 ? 100.492 50.356  137.608 1.00 34.40  ? 1594 ILE A N     1 
ATOM   1152  C  CA    . ILE A 1 1594 ? 100.208 49.386  136.558 1.00 32.43  ? 1594 ILE A CA    1 
ATOM   1153  C  C     . ILE A 1 1594 ? 101.159 49.618  135.396 1.00 33.39  ? 1594 ILE A C     1 
ATOM   1154  O  O     . ILE A 1 1594 ? 101.380 50.757  134.972 1.00 38.68  ? 1594 ILE A O     1 
ATOM   1155  C  CB    . ILE A 1 1594 ? 98.735  49.477  136.118 1.00 33.82  ? 1594 ILE A CB    1 
ATOM   1156  C  CG1   . ILE A 1 1594 ? 97.806  49.091  137.270 1.00 29.27  ? 1594 ILE A CG1   1 
ATOM   1157  C  CG2   . ILE A 1 1594 ? 98.475  48.593  134.908 1.00 27.31  ? 1594 ILE A CG2   1 
ATOM   1158  C  CD1   . ILE A 1 1594 ? 96.347  49.384  136.998 1.00 30.90  ? 1594 ILE A CD1   1 
ATOM   1159  N  N     . GLN A 1 1595 ? 101.729 48.531  134.882 1.00 37.89  ? 1595 GLN A N     1 
ATOM   1160  C  CA    . GLN A 1 1595 ? 102.760 48.627  133.858 1.00 40.26  ? 1595 GLN A CA    1 
ATOM   1161  C  C     . GLN A 1 1595 ? 102.201 49.230  132.575 1.00 39.93  ? 1595 GLN A C     1 
ATOM   1162  O  O     . GLN A 1 1595 ? 101.338 48.640  131.919 1.00 34.97  ? 1595 GLN A O     1 
ATOM   1163  C  CB    . GLN A 1 1595 ? 103.347 47.238  133.594 1.00 42.09  ? 1595 GLN A CB    1 
ATOM   1164  C  CG    . GLN A 1 1595 ? 104.568 47.207  132.689 1.00 47.20  ? 1595 GLN A CG    1 
ATOM   1165  C  CD    . GLN A 1 1595 ? 104.208 47.149  131.218 1.00 62.66  ? 1595 GLN A CD    1 
ATOM   1166  O  OE1   . GLN A 1 1595 ? 103.164 46.615  130.843 1.00 66.64  ? 1595 GLN A OE1   1 
ATOM   1167  N  NE2   . GLN A 1 1595 ? 105.078 47.692  130.375 1.00 61.82  ? 1595 GLN A NE2   1 
ATOM   1168  N  N     . GLY A 1 1596 ? 102.696 50.416  132.223 1.00 40.89  ? 1596 GLY A N     1 
ATOM   1169  C  CA    . GLY A 1 1596 ? 102.308 51.057  130.982 1.00 34.89  ? 1596 GLY A CA    1 
ATOM   1170  C  C     . GLY A 1 1596 ? 100.898 51.595  130.947 1.00 32.28  ? 1596 GLY A C     1 
ATOM   1171  O  O     . GLY A 1 1596 ? 100.315 51.704  129.865 1.00 36.54  ? 1596 GLY A O     1 
ATOM   1172  N  N     . VAL A 1 1597 ? 100.326 51.936  132.105 1.00 30.48  ? 1597 VAL A N     1 
ATOM   1173  C  CA    . VAL A 1 1597 ? 98.935  52.381  132.147 1.00 25.74  ? 1597 VAL A CA    1 
ATOM   1174  C  C     . VAL A 1 1597 ? 98.773  53.729  131.450 1.00 23.47  ? 1597 VAL A C     1 
ATOM   1175  O  O     . VAL A 1 1597 ? 97.760  53.984  130.787 1.00 28.49  ? 1597 VAL A O     1 
ATOM   1176  C  CB    . VAL A 1 1597 ? 98.431  52.414  133.606 1.00 26.66  ? 1597 VAL A CB    1 
ATOM   1177  C  CG1   . VAL A 1 1597 ? 99.185  53.449  134.432 1.00 26.43  ? 1597 VAL A CG1   1 
ATOM   1178  C  CG2   . VAL A 1 1597 ? 96.933  52.660  133.655 1.00 26.51  ? 1597 VAL A CG2   1 
ATOM   1179  N  N     . GLN A 1 1598 ? 99.773  54.607  131.574 1.00 21.50  ? 1598 GLN A N     1 
ATOM   1180  C  CA    . GLN A 1 1598 ? 99.698  55.921  130.939 1.00 19.10  ? 1598 GLN A CA    1 
ATOM   1181  C  C     . GLN A 1 1598 ? 99.592  55.793  129.424 1.00 22.02  ? 1598 GLN A C     1 
ATOM   1182  O  O     . GLN A 1 1598 ? 98.711  56.394  128.791 1.00 23.99  ? 1598 GLN A O     1 
ATOM   1183  C  CB    . GLN A 1 1598 ? 100.925 56.747  131.326 1.00 18.09  ? 1598 GLN A CB    1 
ATOM   1184  C  CG    . GLN A 1 1598 ? 100.929 58.167  130.790 1.00 17.62  ? 1598 GLN A CG    1 
ATOM   1185  C  CD    . GLN A 1 1598 ? 99.804  59.003  131.357 1.00 17.80  ? 1598 GLN A CD    1 
ATOM   1186  O  OE1   . GLN A 1 1598 ? 99.700  59.178  132.569 1.00 24.35  ? 1598 GLN A OE1   1 
ATOM   1187  N  NE2   . GLN A 1 1598 ? 98.957  59.529  130.482 1.00 17.26  ? 1598 GLN A NE2   1 
ATOM   1188  N  N     . ARG A 1 1599 ? 100.484 55.000  128.826 1.00 27.47  ? 1599 ARG A N     1 
ATOM   1189  C  CA    . ARG A 1 1599 ? 100.444 54.788  127.384 1.00 26.80  ? 1599 ARG A CA    1 
ATOM   1190  C  C     . ARG A 1 1599 ? 99.171  54.063  126.974 1.00 22.09  ? 1599 ARG A C     1 
ATOM   1191  O  O     . ARG A 1 1599 ? 98.623  54.319  125.896 1.00 20.92  ? 1599 ARG A O     1 
ATOM   1192  C  CB    . ARG A 1 1599 ? 101.678 54.004  126.939 1.00 32.12  ? 1599 ARG A CB    1 
ATOM   1193  C  CG    . ARG A 1 1599 ? 102.979 54.777  127.065 1.00 43.84  ? 1599 ARG A CG    1 
ATOM   1194  C  CD    . ARG A 1 1599 ? 104.131 54.025  126.424 1.00 56.57  ? 1599 ARG A CD    1 
ATOM   1195  N  NE    . ARG A 1 1599 ? 104.394 52.762  127.104 1.00 62.47  ? 1599 ARG A NE    1 
ATOM   1196  C  CZ    . ARG A 1 1599 ? 105.204 52.626  128.144 1.00 58.47  ? 1599 ARG A CZ    1 
ATOM   1197  N  NH1   . ARG A 1 1599 ? 105.851 53.660  128.657 1.00 60.54  ? 1599 ARG A NH1   1 
ATOM   1198  N  NH2   . ARG A 1 1599 ? 105.369 51.422  128.684 1.00 56.34  ? 1599 ARG A NH2   1 
ATOM   1199  N  N     . SER A 1 1600 ? 98.686  53.153  127.822 1.00 18.99  ? 1600 SER A N     1 
ATOM   1200  C  CA    . SER A 1 1600 ? 97.445  52.447  127.523 1.00 21.50  ? 1600 SER A CA    1 
ATOM   1201  C  C     . SER A 1 1600 ? 96.276  53.418  127.414 1.00 25.29  ? 1600 SER A C     1 
ATOM   1202  O  O     . SER A 1 1600 ? 95.492  53.358  126.461 1.00 25.91  ? 1600 SER A O     1 
ATOM   1203  C  CB    . SER A 1 1600 ? 97.172  51.391  128.595 1.00 22.20  ? 1600 SER A CB    1 
ATOM   1204  O  OG    . SER A 1 1600 ? 98.242  50.466  128.683 1.00 30.75  ? 1600 SER A OG    1 
ATOM   1205  N  N     . LEU A 1 1601 ? 96.153  54.334  128.379 1.00 18.71  ? 1601 LEU A N     1 
ATOM   1206  C  CA    . LEU A 1 1601 ? 95.070  55.312  128.321 1.00 18.04  ? 1601 LEU A CA    1 
ATOM   1207  C  C     . LEU A 1 1601 ? 95.239  56.277  127.156 1.00 18.08  ? 1601 LEU A C     1 
ATOM   1208  O  O     . LEU A 1 1601 ? 94.251  56.670  126.527 1.00 21.87  ? 1601 LEU A O     1 
ATOM   1209  C  CB    . LEU A 1 1601 ? 94.951  56.082  129.637 1.00 19.34  ? 1601 LEU A CB    1 
ATOM   1210  C  CG    . LEU A 1 1601 ? 94.150  55.420  130.759 1.00 13.84  ? 1601 LEU A CG    1 
ATOM   1211  C  CD1   . LEU A 1 1601 ? 92.705  55.285  130.288 1.00 14.81  ? 1601 LEU A CD1   1 
ATOM   1212  C  CD2   . LEU A 1 1601 ? 94.705  54.082  131.211 1.00 20.30  ? 1601 LEU A CD2   1 
ATOM   1213  N  N     . GLU A 1 1602 ? 96.475  56.683  126.857 1.00 16.40  ? 1602 GLU A N     1 
ATOM   1214  C  CA    . GLU A 1 1602 ? 96.685  57.572  125.715 1.00 17.94  ? 1602 GLU A CA    1 
ATOM   1215  C  C     . GLU A 1 1602 ? 96.266  56.898  124.408 1.00 15.54  ? 1602 GLU A C     1 
ATOM   1216  O  O     . GLU A 1 1602 ? 95.579  57.500  123.569 1.00 14.47  ? 1602 GLU A O     1 
ATOM   1217  C  CB    . GLU A 1 1602 ? 98.148  58.017  125.665 1.00 19.85  ? 1602 GLU A CB    1 
ATOM   1218  C  CG    . GLU A 1 1602 ? 98.514  59.041  126.734 1.00 21.19  ? 1602 GLU A CG    1 
ATOM   1219  C  CD    . GLU A 1 1602 ? 99.978  59.443  126.691 1.00 46.33  ? 1602 GLU A CD    1 
ATOM   1220  O  OE1   . GLU A 1 1602 ? 100.667 59.087  125.713 1.00 63.87  ? 1602 GLU A OE1   1 
ATOM   1221  O  OE2   . GLU A 1 1602 ? 100.439 60.121  127.635 1.00 35.65  ? 1602 GLU A OE2   1 
ATOM   1222  N  N     . ARG A 1 1603 ? 96.657  55.633  124.232 1.00 15.68  ? 1603 ARG A N     1 
ATOM   1223  C  CA    . ARG A 1 1603 ? 96.264  54.883  123.043 1.00 18.50  ? 1603 ARG A CA    1 
ATOM   1224  C  C     . ARG A 1 1603 ? 94.754  54.692  122.978 1.00 19.38  ? 1603 ARG A C     1 
ATOM   1225  O  O     . ARG A 1 1603 ? 94.152  54.809  121.904 1.00 18.97  ? 1603 ARG A O     1 
ATOM   1226  C  CB    . ARG A 1 1603 ? 96.982  53.534  123.025 1.00 20.97  ? 1603 ARG A CB    1 
ATOM   1227  C  CG    . ARG A 1 1603 ? 96.711  52.690  121.795 1.00 27.54  ? 1603 ARG A CG    1 
ATOM   1228  C  CD    . ARG A 1 1603 ? 97.506  51.398  121.842 1.00 32.27  ? 1603 ARG A CD    1 
ATOM   1229  N  NE    . ARG A 1 1603 ? 97.294  50.581  120.654 1.00 47.53  ? 1603 ARG A NE    1 
ATOM   1230  C  CZ    . ARG A 1 1603 ? 96.340  49.668  120.539 1.00 45.56  ? 1603 ARG A CZ    1 
ATOM   1231  N  NH1   . ARG A 1 1603 ? 95.495  49.424  121.527 1.00 36.48  ? 1603 ARG A NH1   1 
ATOM   1232  N  NH2   . ARG A 1 1603 ? 96.232  48.981  119.405 1.00 48.03  ? 1603 ARG A NH2   1 
ATOM   1233  N  N     . LEU A 1 1604 ? 94.124  54.392  124.118 1.00 17.07  ? 1604 LEU A N     1 
ATOM   1234  C  CA    . LEU A 1 1604 ? 92.673  54.244  124.143 1.00 17.33  ? 1604 LEU A CA    1 
ATOM   1235  C  C     . LEU A 1 1604 ? 91.983  55.546  123.761 1.00 16.80  ? 1604 LEU A C     1 
ATOM   1236  O  O     . LEU A 1 1604 ? 90.990  55.535  123.026 1.00 22.38  ? 1604 LEU A O     1 
ATOM   1237  C  CB    . LEU A 1 1604 ? 92.210  53.778  125.523 1.00 14.88  ? 1604 LEU A CB    1 
ATOM   1238  C  CG    . LEU A 1 1604 ? 92.521  52.331  125.909 1.00 15.05  ? 1604 LEU A CG    1 
ATOM   1239  C  CD1   . LEU A 1 1604 ? 92.076  52.053  127.335 1.00 12.13  ? 1604 LEU A CD1   1 
ATOM   1240  C  CD2   . LEU A 1 1604 ? 91.862  51.362  124.941 1.00 22.62  ? 1604 LEU A CD2   1 
ATOM   1241  N  N     . ALA A 1 1605 ? 92.493  56.676  124.251 1.00 13.76  ? 1605 ALA A N     1 
ATOM   1242  C  CA    . ALA A 1 1605 ? 91.919  57.968  123.892 1.00 15.33  ? 1605 ALA A CA    1 
ATOM   1243  C  C     . ALA A 1 1605 ? 92.020  58.212  122.393 1.00 19.34  ? 1605 ALA A C     1 
ATOM   1244  O  O     . ALA A 1 1605 ? 91.048  58.630  121.751 1.00 23.23  ? 1605 ALA A O     1 
ATOM   1245  C  CB    . ALA A 1 1605 ? 92.613  59.085  124.671 1.00 12.16  ? 1605 ALA A CB    1 
ATOM   1246  N  N     . ASP A 1 1606 ? 93.193  57.941  121.814 1.00 20.50  ? 1606 ASP A N     1 
ATOM   1247  C  CA    . ASP A 1 1606 ? 93.369  58.141  120.377 1.00 20.48  ? 1606 ASP A CA    1 
ATOM   1248  C  C     . ASP A 1 1606 ? 92.417  57.256  119.576 1.00 22.39  ? 1606 ASP A C     1 
ATOM   1249  O  O     . ASP A 1 1606 ? 91.770  57.712  118.622 1.00 22.13  ? 1606 ASP A O     1 
ATOM   1250  C  CB    . ASP A 1 1606 ? 94.823  57.866  119.990 1.00 21.68  ? 1606 ASP A CB    1 
ATOM   1251  C  CG    . ASP A 1 1606 ? 95.112  58.189  118.538 1.00 42.65  ? 1606 ASP A CG    1 
ATOM   1252  O  OD1   . ASP A 1 1606 ? 95.196  59.388  118.200 1.00 40.28  ? 1606 ASP A OD1   1 
ATOM   1253  O  OD2   . ASP A 1 1606 ? 95.262  57.244  117.736 1.00 43.11  ? 1606 ASP A OD2   1 
ATOM   1254  N  N     . LEU A 1 1607 ? 92.307  55.984  119.964 1.00 19.11  ? 1607 LEU A N     1 
ATOM   1255  C  CA    . LEU A 1 1607 ? 91.460  55.048  119.232 1.00 18.93  ? 1607 LEU A CA    1 
ATOM   1256  C  C     . LEU A 1 1607 ? 89.986  55.431  119.341 1.00 21.88  ? 1607 LEU A C     1 
ATOM   1257  O  O     . LEU A 1 1607 ? 89.238  55.378  118.353 1.00 27.88  ? 1607 LEU A O     1 
ATOM   1258  C  CB    . LEU A 1 1607 ? 91.698  53.631  119.754 1.00 20.31  ? 1607 LEU A CB    1 
ATOM   1259  C  CG    . LEU A 1 1607 ? 93.061  52.987  119.490 1.00 25.64  ? 1607 LEU A CG    1 
ATOM   1260  C  CD1   . LEU A 1 1607 ? 93.155  51.639  120.188 1.00 26.28  ? 1607 LEU A CD1   1 
ATOM   1261  C  CD2   . LEU A 1 1607 ? 93.321  52.837  118.002 1.00 25.11  ? 1607 LEU A CD2   1 
ATOM   1262  N  N     . LEU A 1 1608 ? 89.547  55.816  120.544 1.00 17.62  ? 1608 LEU A N     1 
ATOM   1263  C  CA    . LEU A 1 1608 ? 88.165  56.242  120.730 1.00 15.87  ? 1608 LEU A CA    1 
ATOM   1264  C  C     . LEU A 1 1608 ? 87.865  57.496  119.921 1.00 18.15  ? 1608 LEU A C     1 
ATOM   1265  O  O     . LEU A 1 1608 ? 86.778  57.626  119.349 1.00 20.45  ? 1608 LEU A O     1 
ATOM   1266  C  CB    . LEU A 1 1608 ? 87.879  56.474  122.214 1.00 13.13  ? 1608 LEU A CB    1 
ATOM   1267  C  CG    . LEU A 1 1608 ? 87.835  55.234  123.112 1.00 10.93  ? 1608 LEU A CG    1 
ATOM   1268  C  CD1   . LEU A 1 1608 ? 87.545  55.617  124.554 1.00 8.51   ? 1608 LEU A CD1   1 
ATOM   1269  C  CD2   . LEU A 1 1608 ? 86.810  54.236  122.610 1.00 10.20  ? 1608 LEU A CD2   1 
ATOM   1270  N  N     . GLY A 1 1609 ? 88.817  58.431  119.862 1.00 16.95  ? 1609 GLY A N     1 
ATOM   1271  C  CA    . GLY A 1 1609 ? 88.630  59.601  119.020 1.00 18.96  ? 1609 GLY A CA    1 
ATOM   1272  C  C     . GLY A 1 1609 ? 88.493  59.248  117.552 1.00 23.73  ? 1609 GLY A C     1 
ATOM   1273  O  O     . GLY A 1 1609 ? 87.676  59.832  116.834 1.00 26.28  ? 1609 GLY A O     1 
ATOM   1274  N  N     . LYS A 1 1610 ? 89.297  58.292  117.081 1.00 24.39  ? 1610 LYS A N     1 
ATOM   1275  C  CA    . LYS A 1 1610 ? 89.181  57.880  115.684 1.00 22.49  ? 1610 LYS A CA    1 
ATOM   1276  C  C     . LYS A 1 1610 ? 87.822  57.245  115.399 1.00 23.57  ? 1610 LYS A C     1 
ATOM   1277  O  O     . LYS A 1 1610 ? 87.206  57.524  114.364 1.00 29.99  ? 1610 LYS A O     1 
ATOM   1278  C  CB    . LYS A 1 1610 ? 90.325  56.936  115.312 1.00 27.18  ? 1610 LYS A CB    1 
ATOM   1279  C  CG    . LYS A 1 1610 ? 91.684  57.620  115.320 1.00 30.09  ? 1610 LYS A CG    1 
ATOM   1280  C  CD    . LYS A 1 1610 ? 92.782  56.716  114.789 1.00 37.21  ? 1610 LYS A CD    1 
ATOM   1281  C  CE    . LYS A 1 1610 ? 93.146  55.637  115.787 1.00 41.01  ? 1610 LYS A CE    1 
ATOM   1282  N  NZ    . LYS A 1 1610 ? 94.297  54.820  115.314 1.00 53.83  ? 1610 LYS A NZ    1 
ATOM   1283  N  N     . ILE A 1 1611 ? 87.326  56.408  116.314 1.00 18.67  ? 1611 ILE A N     1 
ATOM   1284  C  CA    . ILE A 1 1611 ? 85.988  55.833  116.141 1.00 19.75  ? 1611 ILE A CA    1 
ATOM   1285  C  C     . ILE A 1 1611 ? 84.932  56.939  116.126 1.00 23.72  ? 1611 ILE A C     1 
ATOM   1286  O  O     . ILE A 1 1611 ? 83.980  56.919  115.326 1.00 31.63  ? 1611 ILE A O     1 
ATOM   1287  C  CB    . ILE A 1 1611 ? 85.705  54.793  117.240 1.00 18.07  ? 1611 ILE A CB    1 
ATOM   1288  C  CG1   . ILE A 1 1611 ? 86.747  53.674  117.195 1.00 20.96  ? 1611 ILE A CG1   1 
ATOM   1289  C  CG2   . ILE A 1 1611 ? 84.308  54.218  117.085 1.00 15.72  ? 1611 ILE A CG2   1 
ATOM   1290  C  CD1   . ILE A 1 1611 ? 86.761  52.909  115.893 1.00 34.10  ? 1611 ILE A CD1   1 
ATOM   1291  N  N     . GLN A 1 1612 ? 85.087  57.916  117.023 1.00 21.08  ? 1612 GLN A N     1 
ATOM   1292  C  CA    . GLN A 1 1612 ? 84.198  59.072  117.059 1.00 21.89  ? 1612 GLN A CA    1 
ATOM   1293  C  C     . GLN A 1 1612 ? 84.124  59.763  115.706 1.00 24.58  ? 1612 GLN A C     1 
ATOM   1294  O  O     . GLN A 1 1612 ? 83.033  59.977  115.163 1.00 31.14  ? 1612 GLN A O     1 
ATOM   1295  C  CB    . GLN A 1 1612 ? 84.691  60.054  118.118 1.00 23.69  ? 1612 GLN A CB    1 
ATOM   1296  C  CG    . GLN A 1 1612 ? 83.801  61.252  118.291 1.00 24.63  ? 1612 GLN A CG    1 
ATOM   1297  C  CD    . GLN A 1 1612 ? 84.279  62.179  119.376 1.00 31.36  ? 1612 GLN A CD    1 
ATOM   1298  O  OE1   . GLN A 1 1612 ? 85.316  61.949  119.998 1.00 37.19  ? 1612 GLN A OE1   1 
ATOM   1299  N  NE2   . GLN A 1 1612 ? 83.541  63.256  119.589 1.00 35.82  ? 1612 GLN A NE2   1 
ATOM   1300  N  N     . LYS A 1 1613 ? 85.279  60.117  115.143 1.00 24.39  ? 1613 LYS A N     1 
ATOM   1301  C  CA    . LYS A 1 1613 ? 85.282  60.795  113.849 1.00 25.70  ? 1613 LYS A CA    1 
ATOM   1302  C  C     . LYS A 1 1613 ? 84.820  59.866  112.729 1.00 27.39  ? 1613 LYS A C     1 
ATOM   1303  O  O     . LYS A 1 1613 ? 84.421  60.330  111.655 1.00 33.08  ? 1613 LYS A O     1 
ATOM   1304  C  CB    . LYS A 1 1613 ? 86.663  61.385  113.537 1.00 25.90  ? 1613 LYS A CB    1 
ATOM   1305  C  CG    . LYS A 1 1613 ? 87.100  62.642  114.337 1.00 33.04  ? 1613 LYS A CG    1 
ATOM   1306  C  CD    . LYS A 1 1613 ? 86.877  62.603  115.844 1.00 37.92  ? 1613 LYS A CD    1 
ATOM   1307  C  CE    . LYS A 1 1613 ? 87.857  63.518  116.572 1.00 38.98  ? 1613 LYS A CE    1 
ATOM   1308  N  NZ    . LYS A 1 1613 ? 87.550  63.630  118.026 1.00 33.19  ? 1613 LYS A NZ    1 
ATOM   1309  N  N     . ALA A 1 1614 ? 84.866  58.552  112.958 1.00 25.36  ? 1614 ALA A N     1 
ATOM   1310  C  CA    . ALA A 1 1614 ? 84.339  57.614  111.971 1.00 26.43  ? 1614 ALA A CA    1 
ATOM   1311  C  C     . ALA A 1 1614 ? 82.815  57.542  111.958 1.00 27.63  ? 1614 ALA A C     1 
ATOM   1312  O  O     . ALA A 1 1614 ? 82.243  57.201  110.917 1.00 28.95  ? 1614 ALA A O     1 
ATOM   1313  C  CB    . ALA A 1 1614 ? 84.914  56.219  112.215 1.00 27.70  ? 1614 ALA A CB    1 
ATOM   1314  N  N     . LEU A 1 1615 ? 82.148  57.841  113.072 1.00 27.39  ? 1615 LEU A N     1 
ATOM   1315  C  CA    . LEU A 1 1615 ? 80.695  57.659  113.160 1.00 27.35  ? 1615 LEU A CA    1 
ATOM   1316  C  C     . LEU A 1 1615 ? 79.868  58.790  112.526 1.00 24.97  ? 1615 LEU A C     1 
ATOM   1317  O  O     . LEU A 1 1615 ? 78.679  58.923  112.848 1.00 23.19  ? 1615 LEU A O     1 
ATOM   1318  C  CB    . LEU A 1 1615 ? 80.269  57.486  114.621 1.00 24.03  ? 1615 LEU A CB    1 
ATOM   1319  C  CG    . LEU A 1 1615 ? 80.881  56.325  115.403 1.00 26.65  ? 1615 LEU A CG    1 
ATOM   1320  C  CD1   . LEU A 1 1615 ? 80.237  56.206  116.774 1.00 23.00  ? 1615 LEU A CD1   1 
ATOM   1321  C  CD2   . LEU A 1 1615 ? 80.735  55.029  114.624 1.00 27.69  ? 1615 LEU A CD2   1 
ATOM   1322  N  N     . GLY A 1 1616 ? 80.451  59.583  111.622 1.00 27.58  ? 1616 GLY A N     1 
ATOM   1323  C  CA    . GLY A 1 1616 ? 79.769  60.783  111.144 1.00 24.74  ? 1616 GLY A CA    1 
ATOM   1324  C  C     . GLY A 1 1616 ? 78.517  60.506  110.326 1.00 26.81  ? 1616 GLY A C     1 
ATOM   1325  O  O     . GLY A 1 1616 ? 77.484  61.161  110.505 1.00 30.98  ? 1616 GLY A O     1 
ATOM   1326  N  N     . GLU A 1 1617 ? 78.594  59.553  109.394 1.00 29.54  ? 1617 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1617 ? 77.439  59.299  108.536 1.00 30.12  ? 1617 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1617 ? 76.315  58.631  109.320 1.00 29.01  ? 1617 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1617 ? 75.130  58.855  109.040 1.00 34.66  ? 1617 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1617 ? 77.850  58.465  107.319 1.00 36.65  ? 1617 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1617 ? 78.412  57.087  107.620 1.00 49.61  ? 1617 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1617 ? 77.332  56.035  107.770 1.00 55.93  ? 1617 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1617 ? 76.203  56.266  107.287 1.00 53.91  ? 1617 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1617 ? 77.609  54.979  108.372 1.00 56.25  ? 1617 GLU A OE2   1 
ATOM   1335  N  N     . TYR A 1 1618 ? 76.668  57.822  110.321 1.00 24.66  ? 1618 TYR A N     1 
ATOM   1336  C  CA    . TYR A 1 1618 ? 75.667  57.328  111.258 1.00 27.41  ? 1618 TYR A CA    1 
ATOM   1337  C  C     . TYR A 1 1618 ? 75.006  58.475  112.010 1.00 24.79  ? 1618 TYR A C     1 
ATOM   1338  O  O     . TYR A 1 1618 ? 73.786  58.457  112.223 1.00 26.94  ? 1618 TYR A O     1 
ATOM   1339  C  CB    . TYR A 1 1618 ? 76.305  56.340  112.236 1.00 25.04  ? 1618 TYR A CB    1 
ATOM   1340  C  CG    . TYR A 1 1618 ? 75.364  55.825  113.301 1.00 24.81  ? 1618 TYR A CG    1 
ATOM   1341  C  CD1   . TYR A 1 1618 ? 74.525  54.747  113.053 1.00 31.51  ? 1618 TYR A CD1   1 
ATOM   1342  C  CD2   . TYR A 1 1618 ? 75.324  56.408  114.561 1.00 25.14  ? 1618 TYR A CD2   1 
ATOM   1343  C  CE1   . TYR A 1 1618 ? 73.668  54.271  114.027 1.00 32.80  ? 1618 TYR A CE1   1 
ATOM   1344  C  CE2   . TYR A 1 1618 ? 74.470  55.939  115.540 1.00 28.82  ? 1618 TYR A CE2   1 
ATOM   1345  C  CZ    . TYR A 1 1618 ? 73.644  54.871  115.267 1.00 38.58  ? 1618 TYR A CZ    1 
ATOM   1346  O  OH    . TYR A 1 1618 ? 72.791  54.399  116.239 1.00 42.62  ? 1618 TYR A OH    1 
ATOM   1347  N  N     . LEU A 1 1619 ? 75.790  59.477  112.417 1.00 21.54  ? 1619 LEU A N     1 
ATOM   1348  C  CA    . LEU A 1 1619 ? 75.208  60.661  113.044 1.00 20.77  ? 1619 LEU A CA    1 
ATOM   1349  C  C     . LEU A 1 1619 ? 74.212  61.348  112.119 1.00 22.00  ? 1619 LEU A C     1 
ATOM   1350  O  O     . LEU A 1 1619 ? 73.137  61.773  112.554 1.00 20.74  ? 1619 LEU A O     1 
ATOM   1351  C  CB    . LEU A 1 1619 ? 76.309  61.635  113.460 1.00 22.50  ? 1619 LEU A CB    1 
ATOM   1352  C  CG    . LEU A 1 1619 ? 77.224  61.139  114.570 1.00 21.40  ? 1619 LEU A CG    1 
ATOM   1353  C  CD1   . LEU A 1 1619 ? 78.579  61.810  114.512 1.00 24.21  ? 1619 LEU A CD1   1 
ATOM   1354  C  CD2   . LEU A 1 1619 ? 76.538  61.446  115.875 1.00 18.79  ? 1619 LEU A CD2   1 
ATOM   1355  N  N     . GLU A 1 1620 ? 74.561  61.480  110.840 1.00 21.39  ? 1620 GLU A N     1 
ATOM   1356  C  CA    . GLU A 1 1620 ? 73.638  62.104  109.891 1.00 22.54  ? 1620 GLU A CA    1 
ATOM   1357  C  C     . GLU A 1 1620 ? 72.355  61.290  109.738 1.00 21.92  ? 1620 GLU A C     1 
ATOM   1358  O  O     . GLU A 1 1620 ? 71.247  61.849  109.714 1.00 27.54  ? 1620 GLU A O     1 
ATOM   1359  C  CB    . GLU A 1 1620 ? 74.319  62.295  108.536 1.00 24.48  ? 1620 GLU A CB    1 
ATOM   1360  C  CG    . GLU A 1 1620 ? 75.217  63.517  108.466 1.00 26.94  ? 1620 GLU A CG    1 
ATOM   1361  C  CD    . GLU A 1 1620 ? 74.479  64.800  108.803 1.00 29.27  ? 1620 GLU A CD    1 
ATOM   1362  O  OE1   . GLU A 1 1620 ? 73.531  65.152  108.069 1.00 22.32  ? 1620 GLU A OE1   1 
ATOM   1363  O  OE2   . GLU A 1 1620 ? 74.842  65.454  109.802 1.00 27.53  ? 1620 GLU A OE2   1 
ATOM   1364  N  N     . ARG A 1 1621 ? 72.481  59.964  109.639 1.00 18.87  ? 1621 ARG A N     1 
ATOM   1365  C  CA    . ARG A 1 1621 ? 71.292  59.136  109.465 1.00 22.30  ? 1621 ARG A CA    1 
ATOM   1366  C  C     . ARG A 1 1621 ? 70.397  59.199  110.698 1.00 24.83  ? 1621 ARG A C     1 
ATOM   1367  O  O     . ARG A 1 1621 ? 69.166  59.167  110.583 1.00 24.48  ? 1621 ARG A O     1 
ATOM   1368  C  CB    . ARG A 1 1621 ? 71.684  57.692  109.151 1.00 32.52  ? 1621 ARG A CB    1 
ATOM   1369  C  CG    . ARG A 1 1621 ? 70.491  56.781  108.887 1.00 33.22  ? 1621 ARG A CG    1 
ATOM   1370  C  CD    . ARG A 1 1621 ? 70.912  55.355  108.567 1.00 45.85  ? 1621 ARG A CD    1 
ATOM   1371  N  NE    . ARG A 1 1621 ? 71.602  54.710  109.676 1.00 56.19  ? 1621 ARG A NE    1 
ATOM   1372  C  CZ    . ARG A 1 1621 ? 70.988  54.126  110.696 1.00 62.24  ? 1621 ARG A CZ    1 
ATOM   1373  N  NH1   . ARG A 1 1621 ? 69.668  54.096  110.783 1.00 62.34  ? 1621 ARG A NH1   1 
ATOM   1374  N  NH2   . ARG A 1 1621 ? 71.716  53.554  111.650 1.00 64.46  ? 1621 ARG A NH2   1 
ATOM   1375  N  N     . GLU A 1 1622 ? 70.996  59.289  111.890 1.00 23.21  ? 1622 GLU A N     1 
ATOM   1376  C  CA    . GLU A 1 1622 ? 70.194  59.467  113.097 1.00 19.95  ? 1622 GLU A CA    1 
ATOM   1377  C  C     . GLU A 1 1622 ? 69.560  60.852  113.160 1.00 19.92  ? 1622 GLU A C     1 
ATOM   1378  O  O     . GLU A 1 1622 ? 68.429  60.990  113.640 1.00 17.67  ? 1622 GLU A O     1 
ATOM   1379  C  CB    . GLU A 1 1622 ? 71.041  59.211  114.345 1.00 23.63  ? 1622 GLU A CB    1 
ATOM   1380  C  CG    . GLU A 1 1622 ? 71.632  57.808  114.444 1.00 32.25  ? 1622 GLU A CG    1 
ATOM   1381  C  CD    . GLU A 1 1622 ? 70.598  56.742  114.776 1.00 41.21  ? 1622 GLU A CD    1 
ATOM   1382  O  OE1   . GLU A 1 1622 ? 69.651  56.543  113.986 1.00 44.78  ? 1622 GLU A OE1   1 
ATOM   1383  O  OE2   . GLU A 1 1622 ? 70.734  56.099  115.838 1.00 42.96  ? 1622 GLU A OE2   1 
ATOM   1384  N  N     . ARG A 1 1623 ? 70.270  61.885  112.694 1.00 18.84  ? 1623 ARG A N     1 
ATOM   1385  C  CA    . ARG A 1 1623 ? 69.675  63.216  112.607 1.00 16.84  ? 1623 ARG A CA    1 
ATOM   1386  C  C     . ARG A 1 1623 ? 68.449  63.212  111.713 1.00 18.32  ? 1623 ARG A C     1 
ATOM   1387  O  O     . ARG A 1 1623 ? 67.500  63.969  111.952 1.00 16.95  ? 1623 ARG A O     1 
ATOM   1388  C  CB    . ARG A 1 1623 ? 70.695  64.225  112.078 1.00 11.84  ? 1623 ARG A CB    1 
ATOM   1389  C  CG    . ARG A 1 1623 ? 71.661  64.740  113.118 1.00 11.04  ? 1623 ARG A CG    1 
ATOM   1390  C  CD    . ARG A 1 1623 ? 72.669  65.697  112.517 1.00 12.54  ? 1623 ARG A CD    1 
ATOM   1391  N  NE    . ARG A 1 1623 ? 73.539  66.269  113.538 1.00 12.55  ? 1623 ARG A NE    1 
ATOM   1392  C  CZ    . ARG A 1 1623 ? 74.848  66.069  113.602 1.00 13.66  ? 1623 ARG A CZ    1 
ATOM   1393  N  NH1   . ARG A 1 1623 ? 75.476  65.314  112.715 1.00 16.49  ? 1623 ARG A NH1   1 
ATOM   1394  N  NH2   . ARG A 1 1623 ? 75.544  66.639  114.581 1.00 14.91  ? 1623 ARG A NH2   1 
ATOM   1395  N  N     . SER A 1 1624 ? 68.458  62.378  110.672 1.00 20.70  ? 1624 SER A N     1 
ATOM   1396  C  CA    . SER A 1 1624 ? 67.281  62.262  109.815 1.00 21.05  ? 1624 SER A CA    1 
ATOM   1397  C  C     . SER A 1 1624 ? 66.044  61.854  110.613 1.00 20.07  ? 1624 SER A C     1 
ATOM   1398  O  O     . SER A 1 1624 ? 64.925  62.267  110.289 1.00 26.97  ? 1624 SER A O     1 
ATOM   1399  C  CB    . SER A 1 1624 ? 67.546  61.262  108.690 1.00 24.42  ? 1624 SER A CB    1 
ATOM   1400  O  OG    . SER A 1 1624 ? 68.710  61.610  107.961 1.00 30.87  ? 1624 SER A OG    1 
ATOM   1401  N  N     . SER A 1 1625 ? 66.224  61.046  111.663 1.00 20.09  ? 1625 SER A N     1 
ATOM   1402  C  CA    . SER A 1 1625 ? 65.075  60.537  112.409 1.00 18.63  ? 1625 SER A CA    1 
ATOM   1403  C  C     . SER A 1 1625 ? 64.432  61.620  113.271 1.00 19.45  ? 1625 SER A C     1 
ATOM   1404  O  O     . SER A 1 1625 ? 63.204  61.762  113.285 1.00 28.40  ? 1625 SER A O     1 
ATOM   1405  C  CB    . SER A 1 1625 ? 65.496  59.350  113.275 1.00 17.83  ? 1625 SER A CB    1 
ATOM   1406  O  OG    . SER A 1 1625 ? 66.464  59.736  114.235 1.00 22.34  ? 1625 SER A OG    1 
ATOM   1407  N  N     . PHE A 1 1626 ? 65.241  62.391  113.997 1.00 18.09  ? 1626 PHE A N     1 
ATOM   1408  C  CA    . PHE A 1 1626 ? 64.751  63.432  114.900 1.00 10.94  ? 1626 PHE A CA    1 
ATOM   1409  C  C     . PHE A 1 1626 ? 65.384  64.744  114.459 1.00 12.02  ? 1626 PHE A C     1 
ATOM   1410  O  O     . PHE A 1 1626 ? 66.523  65.056  114.830 1.00 14.32  ? 1626 PHE A O     1 
ATOM   1411  C  CB    . PHE A 1 1626 ? 65.066  63.096  116.357 1.00 9.50   ? 1626 PHE A CB    1 
ATOM   1412  C  CG    . PHE A 1 1626 ? 64.426  64.023  117.354 1.00 9.33   ? 1626 PHE A CG    1 
ATOM   1413  C  CD1   . PHE A 1 1626 ? 63.103  63.849  117.728 1.00 7.36   ? 1626 PHE A CD1   1 
ATOM   1414  C  CD2   . PHE A 1 1626 ? 65.153  65.045  117.942 1.00 8.45   ? 1626 PHE A CD2   1 
ATOM   1415  C  CE1   . PHE A 1 1626 ? 62.510  64.691  118.649 1.00 6.27   ? 1626 PHE A CE1   1 
ATOM   1416  C  CE2   . PHE A 1 1626 ? 64.566  65.888  118.868 1.00 6.79   ? 1626 PHE A CE2   1 
ATOM   1417  C  CZ    . PHE A 1 1626 ? 63.243  65.711  119.221 1.00 6.54   ? 1626 PHE A CZ    1 
ATOM   1418  N  N     . PRO A 1 1627 ? 64.666  65.542  113.660 1.00 13.37  ? 1627 PRO A N     1 
ATOM   1419  C  CA    . PRO A 1 1627 ? 65.294  66.666  112.947 1.00 9.00   ? 1627 PRO A CA    1 
ATOM   1420  C  C     . PRO A 1 1627 ? 65.934  67.725  113.832 1.00 8.92   ? 1627 PRO A C     1 
ATOM   1421  O  O     . PRO A 1 1627 ? 66.817  68.456  113.373 1.00 9.86   ? 1627 PRO A O     1 
ATOM   1422  C  CB    . PRO A 1 1627 ? 64.126  67.260  112.147 1.00 9.82   ? 1627 PRO A CB    1 
ATOM   1423  C  CG    . PRO A 1 1627 ? 62.885  66.711  112.791 1.00 11.38  ? 1627 PRO A CG    1 
ATOM   1424  C  CD    . PRO A 1 1627 ? 63.269  65.349  113.245 1.00 13.53  ? 1627 PRO A CD    1 
ATOM   1425  N  N     . ARG A 1 1628 ? 65.504  67.837  115.089 1.00 6.40   ? 1628 ARG A N     1 
ATOM   1426  C  CA    . ARG A 1 1628 ? 66.146  68.793  115.983 1.00 7.26   ? 1628 ARG A CA    1 
ATOM   1427  C  C     . ARG A 1 1628 ? 67.612  68.458  116.226 1.00 9.01   ? 1628 ARG A C     1 
ATOM   1428  O  O     . ARG A 1 1628 ? 68.399  69.367  116.523 1.00 9.85   ? 1628 ARG A O     1 
ATOM   1429  C  CB    . ARG A 1 1628 ? 65.373  68.866  117.300 1.00 6.53   ? 1628 ARG A CB    1 
ATOM   1430  C  CG    . ARG A 1 1628 ? 63.954  69.389  117.120 1.00 5.49   ? 1628 ARG A CG    1 
ATOM   1431  C  CD    . ARG A 1 1628 ? 63.199  69.486  118.429 1.00 5.30   ? 1628 ARG A CD    1 
ATOM   1432  N  NE    . ARG A 1 1628 ? 61.830  69.947  118.225 1.00 8.25   ? 1628 ARG A NE    1 
ATOM   1433  C  CZ    . ARG A 1 1628 ? 61.350  71.096  118.679 1.00 6.39   ? 1628 ARG A CZ    1 
ATOM   1434  N  NH1   . ARG A 1 1628 ? 62.107  71.942  119.358 1.00 5.70   ? 1628 ARG A NH1   1 
ATOM   1435  N  NH2   . ARG A 1 1628 ? 60.079  71.408  118.441 1.00 5.25   ? 1628 ARG A NH2   1 
ATOM   1436  N  N     . PHE A 1 1629 ? 68.003  67.191  116.055 1.00 8.70   ? 1629 PHE A N     1 
ATOM   1437  C  CA    . PHE A 1 1629 ? 69.411  66.816  116.118 1.00 6.70   ? 1629 PHE A CA    1 
ATOM   1438  C  C     . PHE A 1 1629 ? 70.247  67.544  115.074 1.00 7.14   ? 1629 PHE A C     1 
ATOM   1439  O  O     . PHE A 1 1629 ? 71.469  67.632  115.233 1.00 9.08   ? 1629 PHE A O     1 
ATOM   1440  C  CB    . PHE A 1 1629 ? 69.573  65.306  115.933 1.00 7.15   ? 1629 PHE A CB    1 
ATOM   1441  C  CG    . PHE A 1 1629 ? 69.060  64.487  117.083 1.00 7.16   ? 1629 PHE A CG    1 
ATOM   1442  C  CD1   . PHE A 1 1629 ? 69.041  65.000  118.368 1.00 6.97   ? 1629 PHE A CD1   1 
ATOM   1443  C  CD2   . PHE A 1 1629 ? 68.613  63.192  116.878 1.00 5.54   ? 1629 PHE A CD2   1 
ATOM   1444  C  CE1   . PHE A 1 1629 ? 68.575  64.241  119.425 1.00 5.57   ? 1629 PHE A CE1   1 
ATOM   1445  C  CE2   . PHE A 1 1629 ? 68.147  62.429  117.930 1.00 5.30   ? 1629 PHE A CE2   1 
ATOM   1446  C  CZ    . PHE A 1 1629 ? 68.128  62.954  119.205 1.00 6.85   ? 1629 PHE A CZ    1 
ATOM   1447  N  N     . TYR A 1 1630 ? 69.623  68.060  114.011 1.00 7.65   ? 1630 TYR A N     1 
ATOM   1448  C  CA    . TYR A 1 1630 ? 70.356  68.852  113.031 1.00 9.11   ? 1630 TYR A CA    1 
ATOM   1449  C  C     . TYR A 1 1630 ? 70.972  70.102  113.642 1.00 7.92   ? 1630 TYR A C     1 
ATOM   1450  O  O     . TYR A 1 1630 ? 71.898  70.671  113.055 1.00 7.70   ? 1630 TYR A O     1 
ATOM   1451  C  CB    . TYR A 1 1630 ? 69.446  69.250  111.867 1.00 7.56   ? 1630 TYR A CB    1 
ATOM   1452  C  CG    . TYR A 1 1630 ? 69.245  68.169  110.829 1.00 10.22  ? 1630 TYR A CG    1 
ATOM   1453  C  CD1   . TYR A 1 1630 ? 70.164  67.987  109.805 1.00 9.79   ? 1630 TYR A CD1   1 
ATOM   1454  C  CD2   . TYR A 1 1630 ? 68.132  67.342  110.863 1.00 12.38  ? 1630 TYR A CD2   1 
ATOM   1455  C  CE1   . TYR A 1 1630 ? 69.986  67.004  108.851 1.00 11.72  ? 1630 TYR A CE1   1 
ATOM   1456  C  CE2   . TYR A 1 1630 ? 67.944  66.358  109.914 1.00 13.44  ? 1630 TYR A CE2   1 
ATOM   1457  C  CZ    . TYR A 1 1630 ? 68.873  66.193  108.911 1.00 13.97  ? 1630 TYR A CZ    1 
ATOM   1458  O  OH    . TYR A 1 1630 ? 68.688  65.213  107.963 1.00 22.84  ? 1630 TYR A OH    1 
ATOM   1459  N  N     . PHE A 1 1631 ? 70.486  70.546  114.801 1.00 8.46   ? 1631 PHE A N     1 
ATOM   1460  C  CA    . PHE A 1 1631 ? 71.051  71.706  115.477 1.00 9.97   ? 1631 PHE A CA    1 
ATOM   1461  C  C     . PHE A 1 1631 ? 71.832  71.304  116.725 1.00 11.40  ? 1631 PHE A C     1 
ATOM   1462  O  O     . PHE A 1 1631 ? 71.878  72.046  117.709 1.00 16.54  ? 1631 PHE A O     1 
ATOM   1463  C  CB    . PHE A 1 1631 ? 69.955  72.714  115.811 1.00 9.72   ? 1631 PHE A CB    1 
ATOM   1464  C  CG    . PHE A 1 1631 ? 69.070  73.041  114.643 1.00 8.28   ? 1631 PHE A CG    1 
ATOM   1465  C  CD1   . PHE A 1 1631 ? 69.470  73.965  113.693 1.00 8.97   ? 1631 PHE A CD1   1 
ATOM   1466  C  CD2   . PHE A 1 1631 ? 67.839  72.426  114.495 1.00 7.42   ? 1631 PHE A CD2   1 
ATOM   1467  C  CE1   . PHE A 1 1631 ? 68.662  74.266  112.614 1.00 9.51   ? 1631 PHE A CE1   1 
ATOM   1468  C  CE2   . PHE A 1 1631 ? 67.024  72.725  113.420 1.00 7.37   ? 1631 PHE A CE2   1 
ATOM   1469  C  CZ    . PHE A 1 1631 ? 67.436  73.647  112.478 1.00 7.45   ? 1631 PHE A CZ    1 
ATOM   1470  N  N     . VAL A 1 1632 ? 72.446  70.124  116.688 1.00 11.07  ? 1632 VAL A N     1 
ATOM   1471  C  CA    . VAL A 1 1632 ? 73.263  69.602  117.774 1.00 10.22  ? 1632 VAL A CA    1 
ATOM   1472  C  C     . VAL A 1 1632 ? 74.551  69.053  117.176 1.00 10.94  ? 1632 VAL A C     1 
ATOM   1473  O  O     . VAL A 1 1632 ? 74.528  68.398  116.129 1.00 8.22   ? 1632 VAL A O     1 
ATOM   1474  C  CB    . VAL A 1 1632 ? 72.507  68.517  118.572 1.00 8.00   ? 1632 VAL A CB    1 
ATOM   1475  C  CG1   . VAL A 1 1632 ? 73.445  67.754  119.481 1.00 8.40   ? 1632 VAL A CG1   1 
ATOM   1476  C  CG2   . VAL A 1 1632 ? 71.387  69.143  119.380 1.00 8.37   ? 1632 VAL A CG2   1 
ATOM   1477  N  N     . GLY A 1 1633 ? 75.675  69.328  117.837 1.00 15.67  ? 1633 GLY A N     1 
ATOM   1478  C  CA    . GLY A 1 1633 ? 76.959  68.911  117.314 1.00 13.57  ? 1633 GLY A CA    1 
ATOM   1479  C  C     . GLY A 1 1633 ? 77.163  67.410  117.376 1.00 11.03  ? 1633 GLY A C     1 
ATOM   1480  O  O     . GLY A 1 1633 ? 76.407  66.668  118.004 1.00 11.17  ? 1633 GLY A O     1 
ATOM   1481  N  N     . ASP A 1 1634 ? 78.221  66.959  116.697 1.00 12.43  ? 1634 ASP A N     1 
ATOM   1482  C  CA    . ASP A 1 1634 ? 78.493  65.528  116.595 1.00 14.28  ? 1634 ASP A CA    1 
ATOM   1483  C  C     . ASP A 1 1634 ? 78.839  64.929  117.954 1.00 15.34  ? 1634 ASP A C     1 
ATOM   1484  O  O     . ASP A 1 1634 ? 78.325  63.868  118.324 1.00 14.04  ? 1634 ASP A O     1 
ATOM   1485  C  CB    . ASP A 1 1634 ? 79.620  65.286  115.591 1.00 15.84  ? 1634 ASP A CB    1 
ATOM   1486  C  CG    . ASP A 1 1634 ? 79.111  65.145  114.170 1.00 22.89  ? 1634 ASP A CG    1 
ATOM   1487  O  OD1   . ASP A 1 1634 ? 77.880  65.047  113.988 1.00 23.11  ? 1634 ASP A OD1   1 
ATOM   1488  O  OD2   . ASP A 1 1634 ? 79.940  65.128  113.236 1.00 29.64  ? 1634 ASP A OD2   1 
ATOM   1489  N  N     . GLU A 1 1635 ? 79.716  65.598  118.710 1.00 15.83  ? 1635 GLU A N     1 
ATOM   1490  C  CA    . GLU A 1 1635 ? 80.011  65.174  120.077 1.00 17.20  ? 1635 GLU A CA    1 
ATOM   1491  C  C     . GLU A 1 1635 ? 78.740  65.052  120.904 1.00 16.01  ? 1635 GLU A C     1 
ATOM   1492  O  O     . GLU A 1 1635 ? 78.491  64.022  121.544 1.00 17.45  ? 1635 GLU A O     1 
ATOM   1493  C  CB    . GLU A 1 1635 ? 80.974  66.167  120.733 1.00 26.57  ? 1635 GLU A CB    1 
ATOM   1494  C  CG    . GLU A 1 1635 ? 81.367  65.830  122.170 1.00 29.69  ? 1635 GLU A CG    1 
ATOM   1495  C  CD    . GLU A 1 1635 ? 82.165  64.554  122.298 1.00 33.17  ? 1635 GLU A CD    1 
ATOM   1496  O  OE1   . GLU A 1 1635 ? 82.838  64.174  121.324 1.00 44.04  ? 1635 GLU A OE1   1 
ATOM   1497  O  OE2   . GLU A 1 1635 ? 82.119  63.928  123.377 1.00 33.86  ? 1635 GLU A OE2   1 
ATOM   1498  N  N     . ASP A 1 1636 ? 77.918  66.100  120.894 1.00 15.13  ? 1636 ASP A N     1 
ATOM   1499  C  CA    . ASP A 1 1636 ? 76.718  66.103  121.717 1.00 15.33  ? 1636 ASP A CA    1 
ATOM   1500  C  C     . ASP A 1 1636 ? 75.712  65.071  121.228 1.00 12.74  ? 1636 ASP A C     1 
ATOM   1501  O  O     . ASP A 1 1636 ? 75.027  64.436  122.035 1.00 12.65  ? 1636 ASP A O     1 
ATOM   1502  C  CB    . ASP A 1 1636 ? 76.110  67.502  121.736 1.00 15.99  ? 1636 ASP A CB    1 
ATOM   1503  C  CG    . ASP A 1 1636 ? 77.065  68.539  122.288 1.00 24.48  ? 1636 ASP A CG    1 
ATOM   1504  O  OD1   . ASP A 1 1636 ? 77.931  68.173  123.110 1.00 32.18  ? 1636 ASP A OD1   1 
ATOM   1505  O  OD2   . ASP A 1 1636 ? 76.953  69.720  121.899 1.00 27.94  ? 1636 ASP A OD2   1 
ATOM   1506  N  N     . LEU A 1 1637 ? 75.608  64.883  119.909 1.00 9.64   ? 1637 LEU A N     1 
ATOM   1507  C  CA    . LEU A 1 1637 ? 74.685  63.880  119.384 1.00 9.38   ? 1637 LEU A CA    1 
ATOM   1508  C  C     . LEU A 1 1637 ? 75.107  62.475  119.797 1.00 11.08  ? 1637 LEU A C     1 
ATOM   1509  O  O     . LEU A 1 1637 ? 74.269  61.652  120.181 1.00 9.57   ? 1637 LEU A O     1 
ATOM   1510  C  CB    . LEU A 1 1637 ? 74.591  63.983  117.862 1.00 11.81  ? 1637 LEU A CB    1 
ATOM   1511  C  CG    . LEU A 1 1637 ? 73.594  63.002  117.234 1.00 9.40   ? 1637 LEU A CG    1 
ATOM   1512  C  CD1   . LEU A 1 1637 ? 72.249  63.042  117.954 1.00 4.97   ? 1637 LEU A CD1   1 
ATOM   1513  C  CD2   . LEU A 1 1637 ? 73.426  63.249  115.748 1.00 11.81  ? 1637 LEU A CD2   1 
ATOM   1514  N  N     . LEU A 1 1638 ? 76.408  62.177  119.713 1.00 12.70  ? 1638 LEU A N     1 
ATOM   1515  C  CA    . LEU A 1 1638 ? 76.902  60.891  120.200 1.00 10.59  ? 1638 LEU A CA    1 
ATOM   1516  C  C     . LEU A 1 1638 ? 76.628  60.723  121.686 1.00 9.87   ? 1638 LEU A C     1 
ATOM   1517  O  O     . LEU A 1 1638 ? 76.247  59.636  122.134 1.00 11.94  ? 1638 LEU A O     1 
ATOM   1518  C  CB    . LEU A 1 1638 ? 78.399  60.750  119.925 1.00 14.17  ? 1638 LEU A CB    1 
ATOM   1519  C  CG    . LEU A 1 1638 ? 78.903  60.765  118.486 1.00 17.46  ? 1638 LEU A CG    1 
ATOM   1520  C  CD1   . LEU A 1 1638 ? 80.392  60.922  118.481 1.00 16.23  ? 1638 LEU A CD1   1 
ATOM   1521  C  CD2   . LEU A 1 1638 ? 78.544  59.458  117.815 1.00 17.46  ? 1638 LEU A CD2   1 
ATOM   1522  N  N     . GLU A 1 1639 ? 76.824  61.785  122.467 1.00 11.06  ? 1639 GLU A N     1 
ATOM   1523  C  CA    . GLU A 1 1639 ? 76.579  61.694  123.902 1.00 13.69  ? 1639 GLU A CA    1 
ATOM   1524  C  C     . GLU A 1 1639 ? 75.104  61.418  124.182 1.00 14.36  ? 1639 GLU A C     1 
ATOM   1525  O  O     . GLU A 1 1639 ? 74.764  60.651  125.088 1.00 19.47  ? 1639 GLU A O     1 
ATOM   1526  C  CB    . GLU A 1 1639 ? 77.044  62.980  124.587 1.00 16.84  ? 1639 GLU A CB    1 
ATOM   1527  C  CG    . GLU A 1 1639 ? 77.067  62.921  126.103 1.00 24.00  ? 1639 GLU A CG    1 
ATOM   1528  C  CD    . GLU A 1 1639 ? 75.721  63.197  126.722 1.00 33.02  ? 1639 GLU A CD    1 
ATOM   1529  O  OE1   . GLU A 1 1639 ? 74.924  63.932  126.109 1.00 31.72  ? 1639 GLU A OE1   1 
ATOM   1530  O  OE2   . GLU A 1 1639 ? 75.458  62.674  127.823 1.00 36.77  ? 1639 GLU A OE2   1 
ATOM   1531  N  N     . ILE A 1 1640 ? 74.212  62.041  123.406 1.00 13.42  ? 1640 ILE A N     1 
ATOM   1532  C  CA    . ILE A 1 1640 ? 72.775  61.826  123.574 1.00 14.56  ? 1640 ILE A CA    1 
ATOM   1533  C  C     . ILE A 1 1640 ? 72.393  60.398  123.202 1.00 14.13  ? 1640 ILE A C     1 
ATOM   1534  O  O     . ILE A 1 1640 ? 71.676  59.716  123.944 1.00 15.90  ? 1640 ILE A O     1 
ATOM   1535  C  CB    . ILE A 1 1640 ? 71.977  62.856  122.751 1.00 16.37  ? 1640 ILE A CB    1 
ATOM   1536  C  CG1   . ILE A 1 1640 ? 72.230  64.276  123.263 1.00 13.27  ? 1640 ILE A CG1   1 
ATOM   1537  C  CG2   . ILE A 1 1640 ? 70.493  62.522  122.742 1.00 9.39   ? 1640 ILE A CG2   1 
ATOM   1538  C  CD1   . ILE A 1 1640 ? 71.793  65.354  122.299 1.00 10.53  ? 1640 ILE A CD1   1 
ATOM   1539  N  N     . ILE A 1 1641 ? 72.855  59.927  122.042 1.00 11.93  ? 1641 ILE A N     1 
ATOM   1540  C  CA    . ILE A 1 1641 ? 72.456  58.604  121.566 1.00 11.50  ? 1641 ILE A CA    1 
ATOM   1541  C  C     . ILE A 1 1641 ? 73.021  57.512  122.468 1.00 14.86  ? 1641 ILE A C     1 
ATOM   1542  O  O     . ILE A 1 1641 ? 72.315  56.567  122.841 1.00 16.52  ? 1641 ILE A O     1 
ATOM   1543  C  CB    . ILE A 1 1641 ? 72.882  58.402  120.099 1.00 16.15  ? 1641 ILE A CB    1 
ATOM   1544  C  CG1   . ILE A 1 1641 ? 72.294  59.498  119.206 1.00 12.93  ? 1641 ILE A CG1   1 
ATOM   1545  C  CG2   . ILE A 1 1641 ? 72.462  57.028  119.603 1.00 19.50  ? 1641 ILE A CG2   1 
ATOM   1546  C  CD1   . ILE A 1 1641 ? 70.816  59.742  119.416 1.00 12.82  ? 1641 ILE A CD1   1 
ATOM   1547  N  N     . GLY A 1 1642 ? 74.298  57.625  122.838 1.00 12.95  ? 1642 GLY A N     1 
ATOM   1548  C  CA    . GLY A 1 1642 ? 74.930  56.599  123.647 1.00 13.17  ? 1642 GLY A CA    1 
ATOM   1549  C  C     . GLY A 1 1642 ? 74.477  56.579  125.090 1.00 16.48  ? 1642 GLY A C     1 
ATOM   1550  O  O     . GLY A 1 1642 ? 74.654  55.563  125.769 1.00 18.90  ? 1642 GLY A O     1 
ATOM   1551  N  N     . ASN A 1 1643 ? 73.894  57.676  125.575 1.00 19.75  ? 1643 ASN A N     1 
ATOM   1552  C  CA    . ASN A 1 1643 ? 73.367  57.749  126.932 1.00 20.15  ? 1643 ASN A CA    1 
ATOM   1553  C  C     . ASN A 1 1643 ? 71.844  57.753  126.954 1.00 24.41  ? 1643 ASN A C     1 
ATOM   1554  O  O     . ASN A 1 1643 ? 71.240  58.451  127.774 1.00 29.65  ? 1643 ASN A O     1 
ATOM   1555  C  CB    . ASN A 1 1643 ? 73.913  58.984  127.649 1.00 20.50  ? 1643 ASN A CB    1 
ATOM   1556  C  CG    . ASN A 1 1643 ? 75.395  58.878  127.947 1.00 21.87  ? 1643 ASN A CG    1 
ATOM   1557  O  OD1   . ASN A 1 1643 ? 75.834  57.964  128.643 1.00 27.20  ? 1643 ASN A OD1   1 
ATOM   1558  N  ND2   . ASN A 1 1643 ? 76.174  59.814  127.419 1.00 20.79  ? 1643 ASN A ND2   1 
ATOM   1559  N  N     . SER A 1 1644 ? 71.212  56.989  126.060 1.00 29.00  ? 1644 SER A N     1 
ATOM   1560  C  CA    . SER A 1 1644 ? 69.754  56.940  126.018 1.00 29.70  ? 1644 SER A CA    1 
ATOM   1561  C  C     . SER A 1 1644 ? 69.181  56.371  127.309 1.00 35.11  ? 1644 SER A C     1 
ATOM   1562  O  O     . SER A 1 1644 ? 68.132  56.820  127.784 1.00 38.38  ? 1644 SER A O     1 
ATOM   1563  C  CB    . SER A 1 1644 ? 69.294  56.114  124.817 1.00 27.50  ? 1644 SER A CB    1 
ATOM   1564  O  OG    . SER A 1 1644 ? 69.591  56.774  123.600 1.00 30.06  ? 1644 SER A OG    1 
ATOM   1565  N  N     . LYS A 1 1645 ? 69.854  55.375  127.889 1.00 31.45  ? 1645 LYS A N     1 
ATOM   1566  C  CA    . LYS A 1 1645 ? 69.365  54.770  129.124 1.00 34.15  ? 1645 LYS A CA    1 
ATOM   1567  C  C     . LYS A 1 1645 ? 69.503  55.729  130.301 1.00 39.68  ? 1645 LYS A C     1 
ATOM   1568  O  O     . LYS A 1 1645 ? 68.561  55.907  131.083 1.00 41.03  ? 1645 LYS A O     1 
ATOM   1569  C  CB    . LYS A 1 1645 ? 70.111  53.465  129.396 1.00 36.93  ? 1645 LYS A CB    1 
ATOM   1570  C  CG    . LYS A 1 1645 ? 69.909  52.406  128.324 1.00 41.93  ? 1645 LYS A CG    1 
ATOM   1571  C  CD    . LYS A 1 1645 ? 70.686  51.140  128.640 1.00 46.53  ? 1645 LYS A CD    1 
ATOM   1572  C  CE    . LYS A 1 1645 ? 70.455  50.075  127.581 1.00 55.53  ? 1645 LYS A CE    1 
ATOM   1573  N  NZ    . LYS A 1 1645 ? 71.224  48.832  127.862 1.00 58.35  ? 1645 LYS A NZ    1 
ATOM   1574  N  N     . ASN A 1 1646 ? 70.670  56.359  130.443 1.00 35.49  ? 1646 ASN A N     1 
ATOM   1575  C  CA    . ASN A 1 1646 ? 70.913  57.311  131.528 1.00 34.73  ? 1646 ASN A CA    1 
ATOM   1576  C  C     . ASN A 1 1646 ? 70.483  58.695  131.048 1.00 38.77  ? 1646 ASN A C     1 
ATOM   1577  O  O     . ASN A 1 1646 ? 71.257  59.469  130.478 1.00 38.74  ? 1646 ASN A O     1 
ATOM   1578  C  CB    . ASN A 1 1646 ? 72.374  57.280  131.957 1.00 41.03  ? 1646 ASN A CB    1 
ATOM   1579  C  CG    . ASN A 1 1646 ? 72.668  58.236  133.095 1.00 51.23  ? 1646 ASN A CG    1 
ATOM   1580  O  OD1   . ASN A 1 1646 ? 71.946  58.275  134.091 1.00 53.64  ? 1646 ASN A OD1   1 
ATOM   1581  N  ND2   . ASN A 1 1646 ? 73.739  59.006  132.959 1.00 47.98  ? 1646 ASN A ND2   1 
ATOM   1582  N  N     . VAL A 1 1647 ? 69.208  59.004  131.293 1.00 38.26  ? 1647 VAL A N     1 
ATOM   1583  C  CA    . VAL A 1 1647 ? 68.588  60.197  130.728 1.00 34.12  ? 1647 VAL A CA    1 
ATOM   1584  C  C     . VAL A 1 1647 ? 69.063  61.482  131.392 1.00 34.51  ? 1647 VAL A C     1 
ATOM   1585  O  O     . VAL A 1 1647 ? 68.902  62.564  130.817 1.00 38.11  ? 1647 VAL A O     1 
ATOM   1586  C  CB    . VAL A 1 1647 ? 67.053  60.075  130.811 1.00 31.73  ? 1647 VAL A CB    1 
ATOM   1587  C  CG1   . VAL A 1 1647 ? 66.552  59.036  129.821 1.00 30.91  ? 1647 VAL A CG1   1 
ATOM   1588  C  CG2   . VAL A 1 1647 ? 66.635  59.704  132.219 1.00 29.90  ? 1647 VAL A CG2   1 
ATOM   1589  N  N     . ALA A 1 1648 ? 69.648  61.396  132.590 1.00 33.08  ? 1648 ALA A N     1 
ATOM   1590  C  CA    . ALA A 1 1648 ? 70.081  62.606  133.284 1.00 31.23  ? 1648 ALA A CA    1 
ATOM   1591  C  C     . ALA A 1 1648 ? 71.112  63.372  132.465 1.00 32.93  ? 1648 ALA A C     1 
ATOM   1592  O  O     . ALA A 1 1648 ? 71.020  64.598  132.322 1.00 34.77  ? 1648 ALA A O     1 
ATOM   1593  C  CB    . ALA A 1 1648 ? 70.642  62.251  134.661 1.00 28.84  ? 1648 ALA A CB    1 
ATOM   1594  N  N     . LYS A 1 1649 ? 72.075  62.662  131.881 1.00 31.72  ? 1649 LYS A N     1 
ATOM   1595  C  CA    . LYS A 1 1649 ? 73.079  63.298  131.041 1.00 29.23  ? 1649 LYS A CA    1 
ATOM   1596  C  C     . LYS A 1 1649 ? 72.479  63.982  129.820 1.00 24.32  ? 1649 LYS A C     1 
ATOM   1597  O  O     . LYS A 1 1649 ? 73.154  64.815  129.205 1.00 22.49  ? 1649 LYS A O     1 
ATOM   1598  C  CB    . LYS A 1 1649 ? 74.121  62.268  130.599 1.00 32.57  ? 1649 LYS A CB    1 
ATOM   1599  C  CG    . LYS A 1 1649 ? 74.991  61.741  131.725 1.00 35.78  ? 1649 LYS A CG    1 
ATOM   1600  C  CD    . LYS A 1 1649 ? 76.019  60.747  131.210 1.00 36.28  ? 1649 LYS A CD    1 
ATOM   1601  C  CE    . LYS A 1 1649 ? 76.874  60.204  132.343 1.00 47.32  ? 1649 LYS A CE    1 
ATOM   1602  N  NZ    . LYS A 1 1649 ? 77.880  59.219  131.860 1.00 38.32  ? 1649 LYS A NZ    1 
ATOM   1603  N  N     . LEU A 1 1650 ? 71.238  63.654  129.454 1.00 24.41  ? 1650 LEU A N     1 
ATOM   1604  C  CA    . LEU A 1 1650 ? 70.579  64.336  128.350 1.00 20.97  ? 1650 LEU A CA    1 
ATOM   1605  C  C     . LEU A 1 1650 ? 70.190  65.768  128.688 1.00 18.18  ? 1650 LEU A C     1 
ATOM   1606  O  O     . LEU A 1 1650 ? 70.074  66.590  127.769 1.00 15.56  ? 1650 LEU A O     1 
ATOM   1607  C  CB    . LEU A 1 1650 ? 69.325  63.573  127.915 1.00 21.71  ? 1650 LEU A CB    1 
ATOM   1608  C  CG    . LEU A 1 1650 ? 69.438  62.095  127.542 1.00 26.94  ? 1650 LEU A CG    1 
ATOM   1609  C  CD1   . LEU A 1 1650 ? 68.054  61.474  127.439 1.00 28.72  ? 1650 LEU A CD1   1 
ATOM   1610  C  CD2   . LEU A 1 1650 ? 70.194  61.921  126.245 1.00 23.66  ? 1650 LEU A CD2   1 
ATOM   1611  N  N     . GLN A 1 1651 ? 70.006  66.086  129.977 1.00 15.76  ? 1651 GLN A N     1 
ATOM   1612  C  CA    . GLN A 1 1651 ? 69.401  67.364  130.352 1.00 13.53  ? 1651 GLN A CA    1 
ATOM   1613  C  C     . GLN A 1 1651 ? 70.118  68.538  129.698 1.00 15.76  ? 1651 GLN A C     1 
ATOM   1614  O  O     . GLN A 1 1651 ? 69.490  69.359  129.012 1.00 17.09  ? 1651 GLN A O     1 
ATOM   1615  C  CB    . GLN A 1 1651 ? 69.400  67.524  131.874 1.00 15.71  ? 1651 GLN A CB    1 
ATOM   1616  C  CG    . GLN A 1 1651 ? 68.604  66.472  132.647 1.00 16.67  ? 1651 GLN A CG    1 
ATOM   1617  C  CD    . GLN A 1 1651 ? 67.103  66.559  132.438 1.00 13.92  ? 1651 GLN A CD    1 
ATOM   1618  O  OE1   . GLN A 1 1651 ? 66.611  67.387  131.675 1.00 17.35  ? 1651 GLN A OE1   1 
ATOM   1619  N  NE2   . GLN A 1 1651 ? 66.365  65.699  133.128 1.00 13.04  ? 1651 GLN A NE2   1 
ATOM   1620  N  N     . LYS A 1 1652 ? 71.445  68.588  129.835 1.00 16.32  ? 1652 LYS A N     1 
ATOM   1621  C  CA    . LYS A 1 1652 ? 72.226  69.727  129.372 1.00 17.79  ? 1652 LYS A CA    1 
ATOM   1622  C  C     . LYS A 1 1652 ? 72.031  70.020  127.890 1.00 13.35  ? 1652 LYS A C     1 
ATOM   1623  O  O     . LYS A 1 1652 ? 72.350  71.128  127.450 1.00 13.25  ? 1652 LYS A O     1 
ATOM   1624  C  CB    . LYS A 1 1652 ? 73.711  69.490  129.656 1.00 19.89  ? 1652 LYS A CB    1 
ATOM   1625  C  CG    . LYS A 1 1652 ? 74.379  68.547  128.668 1.00 20.04  ? 1652 LYS A CG    1 
ATOM   1626  C  CD    . LYS A 1 1652 ? 75.893  68.592  128.773 1.00 24.06  ? 1652 LYS A CD    1 
ATOM   1627  C  CE    . LYS A 1 1652 ? 76.380  67.895  130.032 1.00 25.88  ? 1652 LYS A CE    1 
ATOM   1628  N  NZ    . LYS A 1 1652 ? 77.865  67.783  130.062 1.00 25.91  ? 1652 LYS A NZ    1 
ATOM   1629  N  N     . HIS A 1 1653 ? 71.516  69.068  127.112 1.00 13.40  ? 1653 HIS A N     1 
ATOM   1630  C  CA    . HIS A 1 1653 ? 71.402  69.271  125.674 1.00 14.58  ? 1653 HIS A CA    1 
ATOM   1631  C  C     . HIS A 1 1653 ? 70.038  69.778  125.225 1.00 9.99   ? 1653 HIS A C     1 
ATOM   1632  O  O     . HIS A 1 1653 ? 69.916  70.208  124.071 1.00 10.11  ? 1653 HIS A O     1 
ATOM   1633  C  CB    . HIS A 1 1653 ? 71.724  67.973  124.927 1.00 12.34  ? 1653 HIS A CB    1 
ATOM   1634  C  CG    . HIS A 1 1653 ? 73.019  67.349  125.338 1.00 18.00  ? 1653 HIS A CG    1 
ATOM   1635  N  ND1   . HIS A 1 1653 ? 74.228  67.711  124.783 1.00 19.52  ? 1653 HIS A ND1   1 
ATOM   1636  C  CD2   . HIS A 1 1653 ? 73.296  66.389  126.250 1.00 18.46  ? 1653 HIS A CD2   1 
ATOM   1637  C  CE1   . HIS A 1 1653 ? 75.194  67.000  125.336 1.00 16.57  ? 1653 HIS A CE1   1 
ATOM   1638  N  NE2   . HIS A 1 1653 ? 74.655  66.190  126.229 1.00 23.05  ? 1653 HIS A NE2   1 
ATOM   1639  N  N     . PHE A 1 1654 ? 69.016  69.763  126.089 1.00 8.26   ? 1654 PHE A N     1 
ATOM   1640  C  CA    . PHE A 1 1654 ? 67.681  70.125  125.614 1.00 8.37   ? 1654 PHE A CA    1 
ATOM   1641  C  C     . PHE A 1 1654 ? 67.622  71.567  125.122 1.00 8.74   ? 1654 PHE A C     1 
ATOM   1642  O  O     . PHE A 1 1654 ? 66.912  71.867  124.154 1.00 8.84   ? 1654 PHE A O     1 
ATOM   1643  C  CB    . PHE A 1 1654 ? 66.627  69.876  126.692 1.00 7.34   ? 1654 PHE A CB    1 
ATOM   1644  C  CG    . PHE A 1 1654 ? 66.395  68.424  126.982 1.00 9.14   ? 1654 PHE A CG    1 
ATOM   1645  C  CD1   . PHE A 1 1654 ? 65.685  67.639  126.089 1.00 8.83   ? 1654 PHE A CD1   1 
ATOM   1646  C  CD2   . PHE A 1 1654 ? 66.864  67.845  128.144 1.00 10.55  ? 1654 PHE A CD2   1 
ATOM   1647  C  CE1   . PHE A 1 1654 ? 65.462  66.302  126.343 1.00 8.89   ? 1654 PHE A CE1   1 
ATOM   1648  C  CE2   . PHE A 1 1654 ? 66.642  66.506  128.405 1.00 10.37  ? 1654 PHE A CE2   1 
ATOM   1649  C  CZ    . PHE A 1 1654 ? 65.942  65.734  127.502 1.00 9.57   ? 1654 PHE A CZ    1 
ATOM   1650  N  N     . LYS A 1 1655 ? 68.375  72.472  125.755 1.00 10.53  ? 1655 LYS A N     1 
ATOM   1651  C  CA    . LYS A 1 1655 ? 68.346  73.864  125.319 1.00 9.50   ? 1655 LYS A CA    1 
ATOM   1652  C  C     . LYS A 1 1655 ? 68.864  74.017  123.893 1.00 10.30  ? 1655 LYS A C     1 
ATOM   1653  O  O     . LYS A 1 1655 ? 68.567  75.018  123.232 1.00 13.48  ? 1655 LYS A O     1 
ATOM   1654  C  CB    . LYS A 1 1655 ? 69.151  74.747  126.275 1.00 13.13  ? 1655 LYS A CB    1 
ATOM   1655  C  CG    . LYS A 1 1655 ? 70.638  74.463  126.291 1.00 18.13  ? 1655 LYS A CG    1 
ATOM   1656  C  CD    . LYS A 1 1655 ? 71.379  75.405  127.226 1.00 20.85  ? 1655 LYS A CD    1 
ATOM   1657  C  CE    . LYS A 1 1655 ? 71.098  75.077  128.682 1.00 32.25  ? 1655 LYS A CE    1 
ATOM   1658  N  NZ    . LYS A 1 1655 ? 71.647  73.748  129.067 1.00 27.41  ? 1655 LYS A NZ    1 
ATOM   1659  N  N     . LYS A 1 1656 ? 69.637  73.044  123.402 1.00 10.86  ? 1656 LYS A N     1 
ATOM   1660  C  CA    . LYS A 1 1656 ? 70.039  73.077  121.999 1.00 11.00  ? 1656 LYS A CA    1 
ATOM   1661  C  C     . LYS A 1 1656 ? 68.876  72.737  121.076 1.00 11.41  ? 1656 LYS A C     1 
ATOM   1662  O  O     . LYS A 1 1656 ? 68.719  73.353  120.016 1.00 16.11  ? 1656 LYS A O     1 
ATOM   1663  C  CB    . LYS A 1 1656 ? 71.209  72.123  121.750 1.00 12.21  ? 1656 LYS A CB    1 
ATOM   1664  C  CG    . LYS A 1 1656 ? 72.525  72.549  122.374 1.00 14.10  ? 1656 LYS A CG    1 
ATOM   1665  C  CD    . LYS A 1 1656 ? 73.451  71.360  122.570 1.00 16.09  ? 1656 LYS A CD    1 
ATOM   1666  C  CE    . LYS A 1 1656 ? 74.631  71.724  123.453 1.00 22.66  ? 1656 LYS A CE    1 
ATOM   1667  N  NZ    . LYS A 1 1656 ? 75.422  70.533  123.850 1.00 24.21  ? 1656 LYS A NZ    1 
ATOM   1668  N  N     . MET A 1 1657 ? 68.049  71.764  121.457 1.00 8.58   ? 1657 MET A N     1 
ATOM   1669  C  CA    . MET A 1 1657 ? 67.008  71.255  120.574 1.00 7.23   ? 1657 MET A CA    1 
ATOM   1670  C  C     . MET A 1 1657 ? 65.674  71.969  120.731 1.00 6.38   ? 1657 MET A C     1 
ATOM   1671  O  O     . MET A 1 1657 ? 64.758  71.711  119.947 1.00 6.01   ? 1657 MET A O     1 
ATOM   1672  C  CB    . MET A 1 1657 ? 66.806  69.753  120.805 1.00 7.72   ? 1657 MET A CB    1 
ATOM   1673  C  CG    . MET A 1 1657 ? 68.073  68.928  120.695 1.00 7.70   ? 1657 MET A CG    1 
ATOM   1674  S  SD    . MET A 1 1657 ? 67.813  67.200  121.134 1.00 13.47  ? 1657 MET A SD    1 
ATOM   1675  C  CE    . MET A 1 1657 ? 67.796  67.301  122.922 1.00 6.25   ? 1657 MET A CE    1 
ATOM   1676  N  N     . PHE A 1 1658 ? 65.539  72.863  121.706 1.00 8.19   ? 1658 PHE A N     1 
ATOM   1677  C  CA    . PHE A 1 1658 ? 64.248  73.466  121.996 1.00 6.48   ? 1658 PHE A CA    1 
ATOM   1678  C  C     . PHE A 1 1658 ? 64.416  74.954  122.261 1.00 7.81   ? 1658 PHE A C     1 
ATOM   1679  O  O     . PHE A 1 1658 ? 65.488  75.424  122.648 1.00 8.56   ? 1658 PHE A O     1 
ATOM   1680  C  CB    . PHE A 1 1658 ? 63.575  72.797  123.197 1.00 4.68   ? 1658 PHE A CB    1 
ATOM   1681  C  CG    . PHE A 1 1658 ? 63.017  71.437  122.901 1.00 4.75   ? 1658 PHE A CG    1 
ATOM   1682  C  CD1   . PHE A 1 1658 ? 63.810  70.308  123.020 1.00 5.21   ? 1658 PHE A CD1   1 
ATOM   1683  C  CD2   . PHE A 1 1658 ? 61.697  71.284  122.515 1.00 5.05   ? 1658 PHE A CD2   1 
ATOM   1684  C  CE1   . PHE A 1 1658 ? 63.299  69.054  122.751 1.00 5.15   ? 1658 PHE A CE1   1 
ATOM   1685  C  CE2   . PHE A 1 1658 ? 61.179  70.033  122.245 1.00 5.16   ? 1658 PHE A CE2   1 
ATOM   1686  C  CZ    . PHE A 1 1658 ? 61.982  68.916  122.364 1.00 6.09   ? 1658 PHE A CZ    1 
ATOM   1687  N  N     . ALA A 1 1659 ? 63.325  75.691  122.044 1.00 7.12   ? 1659 ALA A N     1 
ATOM   1688  C  CA    . ALA A 1 1659 ? 63.337  77.125  122.303 1.00 7.45   ? 1659 ALA A CA    1 
ATOM   1689  C  C     . ALA A 1 1659 ? 63.395  77.421  123.796 1.00 9.86   ? 1659 ALA A C     1 
ATOM   1690  O  O     . ALA A 1 1659 ? 64.192  78.258  124.237 1.00 12.39  ? 1659 ALA A O     1 
ATOM   1691  C  CB    . ALA A 1 1659 ? 62.107  77.778  121.674 1.00 6.26   ? 1659 ALA A CB    1 
ATOM   1692  N  N     . GLY A 1 1660 ? 62.565  76.749  124.588 1.00 8.09   ? 1660 GLY A N     1 
ATOM   1693  C  CA    . GLY A 1 1660 ? 62.472  77.059  126.000 1.00 6.72   ? 1660 GLY A CA    1 
ATOM   1694  C  C     . GLY A 1 1660 ? 62.591  75.868  126.928 1.00 7.91   ? 1660 GLY A C     1 
ATOM   1695  O  O     . GLY A 1 1660 ? 62.460  76.017  128.146 1.00 9.58   ? 1660 GLY A O     1 
ATOM   1696  N  N     . VAL A 1 1661 ? 62.834  74.682  126.376 1.00 9.67   ? 1661 VAL A N     1 
ATOM   1697  C  CA    . VAL A 1 1661 ? 62.982  73.473  127.180 1.00 8.93   ? 1661 VAL A CA    1 
ATOM   1698  C  C     . VAL A 1 1661 ? 64.451  73.372  127.576 1.00 9.68   ? 1661 VAL A C     1 
ATOM   1699  O  O     . VAL A 1 1661 ? 65.301  72.983  126.775 1.00 10.83  ? 1661 VAL A O     1 
ATOM   1700  C  CB    . VAL A 1 1661 ? 62.509  72.225  126.434 1.00 9.52   ? 1661 VAL A CB    1 
ATOM   1701  C  CG1   . VAL A 1 1661 ? 62.771  70.976  127.265 1.00 6.29   ? 1661 VAL A CG1   1 
ATOM   1702  C  CG2   . VAL A 1 1661 ? 61.037  72.343  126.069 1.00 6.09   ? 1661 VAL A CG2   1 
ATOM   1703  N  N     . SER A 1 1662 ? 64.751  73.733  128.822 1.00 11.86  ? 1662 SER A N     1 
ATOM   1704  C  CA    . SER A 1 1662 ? 66.102  73.597  129.347 1.00 11.16  ? 1662 SER A CA    1 
ATOM   1705  C  C     . SER A 1 1662 ? 66.337  72.238  129.989 1.00 11.07  ? 1662 SER A C     1 
ATOM   1706  O  O     . SER A 1 1662 ? 67.466  71.735  129.968 1.00 14.61  ? 1662 SER A O     1 
ATOM   1707  C  CB    . SER A 1 1662 ? 66.387  74.704  130.365 1.00 12.65  ? 1662 SER A CB    1 
ATOM   1708  O  OG    . SER A 1 1662 ? 67.705  74.603  130.874 1.00 19.60  ? 1662 SER A OG    1 
ATOM   1709  N  N     . SER A 1 1663 ? 65.295  71.636  130.554 1.00 10.70  ? 1663 SER A N     1 
ATOM   1710  C  CA    . SER A 1 1663 ? 65.395  70.314  131.151 1.00 11.28  ? 1663 SER A CA    1 
ATOM   1711  C  C     . SER A 1 1663 ? 64.023  69.662  131.115 1.00 11.36  ? 1663 SER A C     1 
ATOM   1712  O  O     . SER A 1 1663 ? 62.998  70.336  130.984 1.00 13.52  ? 1663 SER A O     1 
ATOM   1713  C  CB    . SER A 1 1663 ? 65.925  70.381  132.588 1.00 13.45  ? 1663 SER A CB    1 
ATOM   1714  O  OG    . SER A 1 1663 ? 64.899  70.751  133.492 1.00 13.24  ? 1663 SER A OG    1 
ATOM   1715  N  N     . ILE A 1 1664 ? 64.017  68.338  131.233 1.00 11.96  ? 1664 ILE A N     1 
ATOM   1716  C  CA    . ILE A 1 1664 ? 62.784  67.567  131.302 1.00 11.72  ? 1664 ILE A CA    1 
ATOM   1717  C  C     . ILE A 1 1664 ? 62.581  67.107  132.737 1.00 13.14  ? 1664 ILE A C     1 
ATOM   1718  O  O     . ILE A 1 1664 ? 63.535  66.972  133.512 1.00 14.01  ? 1664 ILE A O     1 
ATOM   1719  C  CB    . ILE A 1 1664 ? 62.791  66.363  130.336 1.00 10.98  ? 1664 ILE A CB    1 
ATOM   1720  C  CG1   . ILE A 1 1664 ? 63.935  65.405  130.678 1.00 11.37  ? 1664 ILE A CG1   1 
ATOM   1721  C  CG2   . ILE A 1 1664 ? 62.885  66.837  128.895 1.00 9.92   ? 1664 ILE A CG2   1 
ATOM   1722  C  CD1   . ILE A 1 1664 ? 63.900  64.110  129.899 1.00 13.16  ? 1664 ILE A CD1   1 
ATOM   1723  N  N     . ILE A 1 1665 ? 61.323  66.872  133.092 1.00 12.88  ? 1665 ILE A N     1 
ATOM   1724  C  CA    . ILE A 1 1665 ? 60.960  66.425  134.431 1.00 11.80  ? 1665 ILE A CA    1 
ATOM   1725  C  C     . ILE A 1 1665 ? 60.756  64.918  134.394 1.00 15.43  ? 1665 ILE A C     1 
ATOM   1726  O  O     . ILE A 1 1665 ? 59.992  64.406  133.571 1.00 13.76  ? 1665 ILE A O     1 
ATOM   1727  C  CB    . ILE A 1 1665 ? 59.702  67.145  134.936 1.00 12.27  ? 1665 ILE A CB    1 
ATOM   1728  C  CG1   . ILE A 1 1665 ? 59.861  68.655  134.765 1.00 9.48   ? 1665 ILE A CG1   1 
ATOM   1729  C  CG2   . ILE A 1 1665 ? 59.426  66.786  136.388 1.00 13.20  ? 1665 ILE A CG2   1 
ATOM   1730  C  CD1   . ILE A 1 1665 ? 58.585  69.424  134.955 1.00 8.17   ? 1665 ILE A CD1   1 
ATOM   1731  N  N     . LEU A 1 1666 ? 61.436  64.210  135.287 1.00 17.99  ? 1666 LEU A N     1 
ATOM   1732  C  CA    . LEU A 1 1666 ? 61.458  62.757  135.282 1.00 16.86  ? 1666 LEU A CA    1 
ATOM   1733  C  C     . LEU A 1 1666 ? 60.946  62.218  136.610 1.00 25.08  ? 1666 LEU A C     1 
ATOM   1734  O  O     . LEU A 1 1666 ? 61.104  62.849  137.659 1.00 31.05  ? 1666 LEU A O     1 
ATOM   1735  C  CB    . LEU A 1 1666 ? 62.876  62.246  135.017 1.00 18.42  ? 1666 LEU A CB    1 
ATOM   1736  C  CG    . LEU A 1 1666 ? 63.408  62.565  133.619 1.00 19.98  ? 1666 LEU A CG    1 
ATOM   1737  C  CD1   . LEU A 1 1666 ? 64.923  62.512  133.599 1.00 21.53  ? 1666 LEU A CD1   1 
ATOM   1738  C  CD2   . LEU A 1 1666 ? 62.822  61.614  132.586 1.00 19.39  ? 1666 LEU A CD2   1 
ATOM   1739  N  N     . ASN A 1 1667 ? 60.324  61.043  136.554 1.00 25.12  ? 1667 ASN A N     1 
ATOM   1740  C  CA    . ASN A 1 1667 ? 59.834  60.402  137.763 1.00 28.79  ? 1667 ASN A CA    1 
ATOM   1741  C  C     . ASN A 1 1667 ? 60.999  59.843  138.582 1.00 32.75  ? 1667 ASN A C     1 
ATOM   1742  O  O     . ASN A 1 1667 ? 62.174  60.011  138.245 1.00 32.65  ? 1667 ASN A O     1 
ATOM   1743  C  CB    . ASN A 1 1667 ? 58.836  59.295  137.420 1.00 22.18  ? 1667 ASN A CB    1 
ATOM   1744  C  CG    . ASN A 1 1667 ? 59.433  58.219  136.533 1.00 26.64  ? 1667 ASN A CG    1 
ATOM   1745  O  OD1   . ASN A 1 1667 ? 60.538  58.366  136.014 1.00 29.50  ? 1667 ASN A OD1   1 
ATOM   1746  N  ND2   . ASN A 1 1667 ? 58.704  57.123  136.367 1.00 26.69  ? 1667 ASN A ND2   1 
ATOM   1747  N  N     . GLU A 1 1668 ? 60.653  59.171  139.682 1.00 35.90  ? 1668 GLU A N     1 
ATOM   1748  C  CA    . GLU A 1 1668 ? 61.677  58.624  140.567 1.00 42.56  ? 1668 GLU A CA    1 
ATOM   1749  C  C     . GLU A 1 1668 ? 62.486  57.534  139.873 1.00 38.27  ? 1668 GLU A C     1 
ATOM   1750  O  O     . GLU A 1 1668 ? 63.684  57.376  140.134 1.00 33.17  ? 1668 GLU A O     1 
ATOM   1751  C  CB    . GLU A 1 1668 ? 61.032  58.090  141.848 1.00 42.75  ? 1668 GLU A CB    1 
ATOM   1752  C  CG    . GLU A 1 1668 ? 60.176  56.840  141.663 1.00 50.29  ? 1668 GLU A CG    1 
ATOM   1753  C  CD    . GLU A 1 1668 ? 58.752  57.149  141.235 1.00 56.15  ? 1668 GLU A CD    1 
ATOM   1754  O  OE1   . GLU A 1 1668 ? 58.490  58.287  140.791 1.00 54.65  ? 1668 GLU A OE1   1 
ATOM   1755  O  OE2   . GLU A 1 1668 ? 57.892  56.250  141.342 1.00 58.57  ? 1668 GLU A OE2   1 
ATOM   1756  N  N     . ASP A 1 1669 ? 61.848  56.776  138.980 1.00 35.49  ? 1669 ASP A N     1 
ATOM   1757  C  CA    . ASP A 1 1669 ? 62.516  55.687  138.282 1.00 36.78  ? 1669 ASP A CA    1 
ATOM   1758  C  C     . ASP A 1 1669 ? 63.347  56.209  137.113 1.00 34.61  ? 1669 ASP A C     1 
ATOM   1759  O  O     . ASP A 1 1669 ? 64.227  55.497  136.620 1.00 37.82  ? 1669 ASP A O     1 
ATOM   1760  C  CB    . ASP A 1 1669 ? 61.446  54.681  137.818 1.00 36.01  ? 1669 ASP A CB    1 
ATOM   1761  C  CG    . ASP A 1 1669 ? 62.017  53.370  137.266 1.00 46.08  ? 1669 ASP A CG    1 
ATOM   1762  O  OD1   . ASP A 1 1669 ? 61.241  52.393  137.207 1.00 56.03  ? 1669 ASP A OD1   1 
ATOM   1763  O  OD2   . ASP A 1 1669 ? 63.211  53.269  136.933 1.00 49.10  ? 1669 ASP A OD2   1 
ATOM   1764  N  N     . ASN A 1 1670 ? 63.120  57.460  136.700 1.00 32.22  ? 1670 ASN A N     1 
ATOM   1765  C  CA    . ASN A 1 1670 ? 63.710  58.060  135.505 1.00 30.42  ? 1670 ASN A CA    1 
ATOM   1766  C  C     . ASN A 1 1670 ? 63.256  57.363  134.231 1.00 32.24  ? 1670 ASN A C     1 
ATOM   1767  O  O     . ASN A 1 1670 ? 63.943  57.426  133.206 1.00 35.06  ? 1670 ASN A O     1 
ATOM   1768  C  CB    . ASN A 1 1670 ? 65.244  58.083  135.573 1.00 28.65  ? 1670 ASN A CB    1 
ATOM   1769  C  CG    . ASN A 1 1670 ? 65.782  59.362  136.180 1.00 33.26  ? 1670 ASN A CG    1 
ATOM   1770  O  OD1   . ASN A 1 1670 ? 66.270  60.241  135.471 1.00 37.53  ? 1670 ASN A OD1   1 
ATOM   1771  N  ND2   . ASN A 1 1670 ? 65.696  59.472  137.500 1.00 34.42  ? 1670 ASN A ND2   1 
ATOM   1772  N  N     . SER A 1 1671 ? 62.101  56.700  134.278 1.00 31.30  ? 1671 SER A N     1 
ATOM   1773  C  CA    . SER A 1 1671 ? 61.570  55.948  133.152 1.00 27.61  ? 1671 SER A CA    1 
ATOM   1774  C  C     . SER A 1 1671 ? 60.341  56.591  132.522 1.00 26.25  ? 1671 SER A C     1 
ATOM   1775  O  O     . SER A 1 1671 ? 59.877  56.111  131.483 1.00 25.13  ? 1671 SER A O     1 
ATOM   1776  C  CB    . SER A 1 1671 ? 61.221  54.522  133.593 1.00 30.94  ? 1671 SER A CB    1 
ATOM   1777  O  OG    . SER A 1 1671 ? 60.281  54.536  134.654 1.00 28.32  ? 1671 SER A OG    1 
ATOM   1778  N  N     . VAL A 1 1672 ? 59.794  57.643  133.128 1.00 26.47  ? 1672 VAL A N     1 
ATOM   1779  C  CA    . VAL A 1 1672 ? 58.602  58.310  132.617 1.00 21.30  ? 1672 VAL A CA    1 
ATOM   1780  C  C     . VAL A 1 1672 ? 58.855  59.811  132.630 1.00 17.77  ? 1672 VAL A C     1 
ATOM   1781  O  O     . VAL A 1 1672 ? 59.241  60.368  133.663 1.00 21.31  ? 1672 VAL A O     1 
ATOM   1782  C  CB    . VAL A 1 1672 ? 57.347  57.971  133.442 1.00 21.48  ? 1672 VAL A CB    1 
ATOM   1783  C  CG1   . VAL A 1 1672 ? 56.172  58.800  132.978 1.00 17.98  ? 1672 VAL A CG1   1 
ATOM   1784  C  CG2   . VAL A 1 1672 ? 57.024  56.488  133.341 1.00 20.25  ? 1672 VAL A CG2   1 
ATOM   1785  N  N     . VAL A 1 1673 ? 58.641  60.464  131.490 1.00 18.25  ? 1673 VAL A N     1 
ATOM   1786  C  CA    . VAL A 1 1673 ? 58.807  61.911  131.385 1.00 14.76  ? 1673 VAL A CA    1 
ATOM   1787  C  C     . VAL A 1 1673 ? 57.488  62.566  131.786 1.00 13.23  ? 1673 VAL A C     1 
ATOM   1788  O  O     . VAL A 1 1673 ? 56.512  62.530  131.034 1.00 16.14  ? 1673 VAL A O     1 
ATOM   1789  C  CB    . VAL A 1 1673 ? 59.230  62.329  129.973 1.00 12.85  ? 1673 VAL A CB    1 
ATOM   1790  C  CG1   . VAL A 1 1673 ? 59.404  63.838  129.894 1.00 12.60  ? 1673 VAL A CG1   1 
ATOM   1791  C  CG2   . VAL A 1 1673 ? 60.511  61.616  129.571 1.00 12.17  ? 1673 VAL A CG2   1 
ATOM   1792  N  N     . LEU A 1 1674 ? 57.458  63.165  132.978 1.00 10.96  ? 1674 LEU A N     1 
ATOM   1793  C  CA    . LEU A 1 1674 ? 56.227  63.772  133.474 1.00 13.43  ? 1674 LEU A CA    1 
ATOM   1794  C  C     . LEU A 1 1674 ? 55.990  65.147  132.861 1.00 11.50  ? 1674 LEU A C     1 
ATOM   1795  O  O     . LEU A 1 1674 ? 54.839  65.559  132.678 1.00 14.65  ? 1674 LEU A O     1 
ATOM   1796  C  CB    . LEU A 1 1674 ? 56.267  63.871  134.999 1.00 17.17  ? 1674 LEU A CB    1 
ATOM   1797  C  CG    . LEU A 1 1674 ? 56.484  62.568  135.769 1.00 18.12  ? 1674 LEU A CG    1 
ATOM   1798  C  CD1   . LEU A 1 1674 ? 56.468  62.825  137.265 1.00 16.92  ? 1674 LEU A CD1   1 
ATOM   1799  C  CD2   . LEU A 1 1674 ? 55.426  61.547  135.388 1.00 13.05  ? 1674 LEU A CD2   1 
ATOM   1800  N  N     . GLY A 1 1675 ? 57.053  65.871  132.548 1.00 9.60   ? 1675 GLY A N     1 
ATOM   1801  C  CA    . GLY A 1 1675 ? 56.892  67.209  132.027 1.00 7.45   ? 1675 GLY A CA    1 
ATOM   1802  C  C     . GLY A 1 1675 ? 58.209  67.821  131.611 1.00 7.42   ? 1675 GLY A C     1 
ATOM   1803  O  O     . GLY A 1 1675 ? 59.218  67.130  131.467 1.00 11.13  ? 1675 GLY A O     1 
ATOM   1804  N  N     . ILE A 1 1676 ? 58.181  69.141  131.419 1.00 6.72   ? 1676 ILE A N     1 
ATOM   1805  C  CA    . ILE A 1 1676 ? 59.339  69.891  130.947 1.00 9.02   ? 1676 ILE A CA    1 
ATOM   1806  C  C     . ILE A 1 1676 ? 59.535  71.126  131.818 1.00 9.43   ? 1676 ILE A C     1 
ATOM   1807  O  O     . ILE A 1 1676 ? 58.625  71.573  132.517 1.00 10.33  ? 1676 ILE A O     1 
ATOM   1808  C  CB    . ILE A 1 1676 ? 59.201  70.291  129.459 1.00 11.44  ? 1676 ILE A CB    1 
ATOM   1809  C  CG1   . ILE A 1 1676 ? 57.974  71.182  129.252 1.00 8.19   ? 1676 ILE A CG1   1 
ATOM   1810  C  CG2   . ILE A 1 1676 ? 59.152  69.058  128.565 1.00 7.61   ? 1676 ILE A CG2   1 
ATOM   1811  C  CD1   . ILE A 1 1676 ? 57.892  71.800  127.877 1.00 8.07   ? 1676 ILE A CD1   1 
ATOM   1812  N  N     . SER A 1 1677 ? 60.750  71.672  131.775 1.00 8.57   ? 1677 SER A N     1 
ATOM   1813  C  CA    . SER A 1 1677 ? 61.117  72.822  132.589 1.00 8.75   ? 1677 SER A CA    1 
ATOM   1814  C  C     . SER A 1 1677 ? 61.908  73.826  131.761 1.00 10.71  ? 1677 SER A C     1 
ATOM   1815  O  O     . SER A 1 1677 ? 62.563  73.475  130.777 1.00 9.80   ? 1677 SER A O     1 
ATOM   1816  C  CB    . SER A 1 1677 ? 61.942  72.404  133.813 1.00 12.41  ? 1677 SER A CB    1 
ATOM   1817  O  OG    . SER A 1 1677 ? 61.188  71.586  134.685 1.00 23.66  ? 1677 SER A OG    1 
ATOM   1818  N  N     . SER A 1 1678 ? 61.838  75.087  132.175 1.00 12.83  ? 1678 SER A N     1 
ATOM   1819  C  CA    . SER A 1 1678 ? 62.616  76.151  131.562 1.00 13.06  ? 1678 SER A CA    1 
ATOM   1820  C  C     . SER A 1 1678 ? 63.861  76.445  132.396 1.00 16.15  ? 1678 SER A C     1 
ATOM   1821  O  O     . SER A 1 1678 ? 64.062  75.893  133.479 1.00 16.90  ? 1678 SER A O     1 
ATOM   1822  C  CB    . SER A 1 1678 ? 61.768  77.412  131.398 1.00 13.93  ? 1678 SER A CB    1 
ATOM   1823  O  OG    . SER A 1 1678 ? 61.384  77.936  132.656 1.00 14.98  ? 1678 SER A OG    1 
ATOM   1824  N  N     . ARG A 1 1679 ? 64.711  77.332  131.871 1.00 16.60  ? 1679 ARG A N     1 
ATOM   1825  C  CA    . ARG A 1 1679 ? 65.946  77.671  132.573 1.00 20.01  ? 1679 ARG A CA    1 
ATOM   1826  C  C     . ARG A 1 1679 ? 65.660  78.383  133.891 1.00 27.54  ? 1679 ARG A C     1 
ATOM   1827  O  O     . ARG A 1 1679 ? 66.317  78.115  134.903 1.00 32.75  ? 1679 ARG A O     1 
ATOM   1828  C  CB    . ARG A 1 1679 ? 66.847  78.529  131.682 1.00 18.03  ? 1679 ARG A CB    1 
ATOM   1829  C  CG    . ARG A 1 1679 ? 66.183  79.770  131.107 1.00 25.11  ? 1679 ARG A CG    1 
ATOM   1830  C  CD    . ARG A 1 1679 ? 67.167  80.590  130.290 1.00 35.70  ? 1679 ARG A CD    1 
ATOM   1831  N  NE    . ARG A 1 1679 ? 66.553  81.790  129.735 1.00 49.47  ? 1679 ARG A NE    1 
ATOM   1832  C  CZ    . ARG A 1 1679 ? 67.188  82.675  128.979 1.00 52.78  ? 1679 ARG A CZ    1 
ATOM   1833  N  NH1   . ARG A 1 1679 ? 68.463  82.525  128.662 1.00 55.23  ? 1679 ARG A NH1   1 
ATOM   1834  N  NH2   . ARG A 1 1679 ? 66.526  83.737  128.528 1.00 49.20  ? 1679 ARG A NH2   1 
ATOM   1835  N  N     . GLU A 1 1680 ? 64.687  79.299  133.898 1.00 25.37  ? 1680 GLU A N     1 
ATOM   1836  C  CA    . GLU A 1 1680 ? 64.362  80.024  135.122 1.00 25.14  ? 1680 GLU A CA    1 
ATOM   1837  C  C     . GLU A 1 1680 ? 63.789  79.094  136.184 1.00 23.58  ? 1680 GLU A C     1 
ATOM   1838  O  O     . GLU A 1 1680 ? 64.110  79.226  137.371 1.00 30.11  ? 1680 GLU A O     1 
ATOM   1839  C  CB    . GLU A 1 1680 ? 63.384  81.161  134.822 1.00 24.17  ? 1680 GLU A CB    1 
ATOM   1840  C  CG    . GLU A 1 1680 ? 63.918  82.210  133.861 1.00 29.00  ? 1680 GLU A CG    1 
ATOM   1841  C  CD    . GLU A 1 1680 ? 63.686  81.846  132.409 1.00 27.50  ? 1680 GLU A CD    1 
ATOM   1842  O  OE1   . GLU A 1 1680 ? 63.075  80.788  132.149 1.00 22.08  ? 1680 GLU A OE1   1 
ATOM   1843  O  OE2   . GLU A 1 1680 ? 64.120  82.616  131.526 1.00 31.06  ? 1680 GLU A OE2   1 
ATOM   1844  N  N     . GLY A 1 1681 ? 62.943  78.152  135.781 1.00 18.18  ? 1681 GLY A N     1 
ATOM   1845  C  CA    . GLY A 1 1681 ? 62.342  77.233  136.725 1.00 17.90  ? 1681 GLY A CA    1 
ATOM   1846  C  C     . GLY A 1 1681 ? 60.882  76.951  136.444 1.00 17.68  ? 1681 GLY A C     1 
ATOM   1847  O  O     . GLY A 1 1681 ? 60.267  76.115  137.113 1.00 21.11  ? 1681 GLY A O     1 
ATOM   1848  N  N     . GLU A 1 1682 ? 60.312  77.649  135.463 1.00 18.14  ? 1682 GLU A N     1 
ATOM   1849  C  CA    . GLU A 1 1682 ? 58.920  77.423  135.098 1.00 15.47  ? 1682 GLU A CA    1 
ATOM   1850  C  C     . GLU A 1 1682 ? 58.740  76.004  134.577 1.00 16.85  ? 1682 GLU A C     1 
ATOM   1851  O  O     . GLU A 1 1682 ? 59.534  75.521  133.764 1.00 16.76  ? 1682 GLU A O     1 
ATOM   1852  C  CB    . GLU A 1 1682 ? 58.476  78.441  134.048 1.00 12.87  ? 1682 GLU A CB    1 
ATOM   1853  C  CG    . GLU A 1 1682 ? 56.985  78.425  133.761 1.00 10.43  ? 1682 GLU A CG    1 
ATOM   1854  C  CD    . GLU A 1 1682 ? 56.591  79.418  132.687 1.00 13.73  ? 1682 GLU A CD    1 
ATOM   1855  O  OE1   . GLU A 1 1682 ? 57.041  79.259  131.533 1.00 12.31  ? 1682 GLU A OE1   1 
ATOM   1856  O  OE2   . GLU A 1 1682 ? 55.836  80.363  132.998 1.00 15.31  ? 1682 GLU A OE2   1 
ATOM   1857  N  N     . GLU A 1 1683 ? 57.691  75.337  135.047 1.00 16.79  ? 1683 GLU A N     1 
ATOM   1858  C  CA    . GLU A 1 1683 ? 57.481  73.923  134.783 1.00 13.24  ? 1683 GLU A CA    1 
ATOM   1859  C  C     . GLU A 1 1683 ? 56.128  73.706  134.124 1.00 14.21  ? 1683 GLU A C     1 
ATOM   1860  O  O     . GLU A 1 1683 ? 55.141  74.355  134.483 1.00 15.05  ? 1683 GLU A O     1 
ATOM   1861  C  CB    . GLU A 1 1683 ? 57.566  73.109  136.078 1.00 13.72  ? 1683 GLU A CB    1 
ATOM   1862  C  CG    . GLU A 1 1683 ? 58.979  72.824  136.551 1.00 24.48  ? 1683 GLU A CG    1 
ATOM   1863  C  CD    . GLU A 1 1683 ? 59.012  71.920  137.767 1.00 31.88  ? 1683 GLU A CD    1 
ATOM   1864  O  OE1   . GLU A 1 1683 ? 59.922  71.069  137.851 1.00 29.75  ? 1683 GLU A OE1   1 
ATOM   1865  O  OE2   . GLU A 1 1683 ? 58.127  72.058  138.636 1.00 30.64  ? 1683 GLU A OE2   1 
ATOM   1866  N  N     . VAL A 1 1684 ? 56.088  72.792  133.158 1.00 10.21  ? 1684 VAL A N     1 
ATOM   1867  C  CA    . VAL A 1 1684 ? 54.856  72.374  132.502 1.00 8.73   ? 1684 VAL A CA    1 
ATOM   1868  C  C     . VAL A 1 1684 ? 54.695  70.877  132.727 1.00 8.97   ? 1684 VAL A C     1 
ATOM   1869  O  O     . VAL A 1 1684 ? 55.625  70.102  132.470 1.00 9.47   ? 1684 VAL A O     1 
ATOM   1870  C  CB    . VAL A 1 1684 ? 54.872  72.701  130.998 1.00 7.27   ? 1684 VAL A CB    1 
ATOM   1871  C  CG1   . VAL A 1 1684 ? 53.585  72.226  130.344 1.00 4.65   ? 1684 VAL A CG1   1 
ATOM   1872  C  CG2   . VAL A 1 1684 ? 55.093  74.188  130.763 1.00 7.67   ? 1684 VAL A CG2   1 
ATOM   1873  N  N     . MET A 1 1685 ? 53.520  70.471  133.205 1.00 7.10   ? 1685 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1685 ? 53.215  69.067  133.457 1.00 7.46   ? 1685 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1685 ? 52.425  68.515  132.278 1.00 9.75   ? 1685 MET A C     1 
ATOM   1876  O  O     . MET A 1 1685 ? 51.378  69.065  131.920 1.00 12.26  ? 1685 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1685 ? 52.416  68.894  134.750 1.00 7.93   ? 1685 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1685 ? 53.162  69.269  136.015 1.00 11.44  ? 1685 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1685 ? 54.650  68.288  136.305 1.00 24.75  ? 1685 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1685 ? 53.946  66.686  136.685 1.00 16.22  ? 1685 MET A CE    1 
ATOM   1881  N  N     . PHE A 1 1686 ? 52.921  67.431  131.685 1.00 9.54   ? 1686 PHE A N     1 
ATOM   1882  C  CA    . PHE A 1 1686 ? 52.205  66.787  130.593 1.00 9.06   ? 1686 PHE A CA    1 
ATOM   1883  C  C     . PHE A 1 1686 ? 50.842  66.298  131.067 1.00 13.79  ? 1686 PHE A C     1 
ATOM   1884  O  O     . PHE A 1 1686 ? 50.704  65.771  132.175 1.00 18.88  ? 1686 PHE A O     1 
ATOM   1885  C  CB    . PHE A 1 1686 ? 53.013  65.610  130.044 1.00 9.54   ? 1686 PHE A CB    1 
ATOM   1886  C  CG    . PHE A 1 1686 ? 54.247  66.012  129.288 1.00 8.22   ? 1686 PHE A CG    1 
ATOM   1887  C  CD1   . PHE A 1 1686 ? 54.279  67.183  128.550 1.00 8.31   ? 1686 PHE A CD1   1 
ATOM   1888  C  CD2   . PHE A 1 1686 ? 55.375  65.208  129.308 1.00 7.98   ? 1686 PHE A CD2   1 
ATOM   1889  C  CE1   . PHE A 1 1686 ? 55.415  67.547  127.851 1.00 7.98   ? 1686 PHE A CE1   1 
ATOM   1890  C  CE2   . PHE A 1 1686 ? 56.512  65.567  128.612 1.00 8.47   ? 1686 PHE A CE2   1 
ATOM   1891  C  CZ    . PHE A 1 1686 ? 56.532  66.737  127.882 1.00 7.25   ? 1686 PHE A CZ    1 
ATOM   1892  N  N     . LYS A 1 1687 ? 49.825  66.485  130.224 1.00 11.48  ? 1687 LYS A N     1 
ATOM   1893  C  CA    . LYS A 1 1687 ? 48.503  65.956  130.548 1.00 13.67  ? 1687 LYS A CA    1 
ATOM   1894  C  C     . LYS A 1 1687 ? 48.521  64.434  130.594 1.00 17.34  ? 1687 LYS A C     1 
ATOM   1895  O  O     . LYS A 1 1687 ? 47.892  63.824  131.466 1.00 23.84  ? 1687 LYS A O     1 
ATOM   1896  C  CB    . LYS A 1 1687 ? 47.470  66.461  129.544 1.00 13.81  ? 1687 LYS A CB    1 
ATOM   1897  C  CG    . LYS A 1 1687 ? 47.309  67.972  129.541 1.00 12.91  ? 1687 LYS A CG    1 
ATOM   1898  C  CD    . LYS A 1 1687 ? 46.702  68.460  130.846 1.00 14.05  ? 1687 LYS A CD    1 
ATOM   1899  C  CE    . LYS A 1 1687 ? 46.466  69.960  130.822 1.00 13.23  ? 1687 LYS A CE    1 
ATOM   1900  N  NZ    . LYS A 1 1687 ? 45.912  70.449  132.114 1.00 20.47  ? 1687 LYS A NZ    1 
ATOM   1901  N  N     . THR A 1 1688 ? 49.233  63.805  129.666 1.00 18.58  ? 1688 THR A N     1 
ATOM   1902  C  CA    . THR A 1 1688 ? 49.516  62.373  129.730 1.00 24.92  ? 1688 THR A CA    1 
ATOM   1903  C  C     . THR A 1 1688 ? 51.026  62.179  129.658 1.00 20.71  ? 1688 THR A C     1 
ATOM   1904  O  O     . THR A 1 1688 ? 51.683  62.743  128.758 1.00 16.14  ? 1688 THR A O     1 
ATOM   1905  C  CB    . THR A 1 1688 ? 48.781  61.597  128.634 1.00 27.15  ? 1688 THR A CB    1 
ATOM   1906  O  OG1   . THR A 1 1688 ? 48.956  60.189  128.839 1.00 35.40  ? 1688 THR A OG1   1 
ATOM   1907  C  CG2   . THR A 1 1688 ? 49.247  61.981  127.236 1.00 22.74  ? 1688 THR A CG2   1 
ATOM   1908  N  N     . PRO A 1 1689 ? 51.624  61.455  130.603 1.00 22.14  ? 1689 PRO A N     1 
ATOM   1909  C  CA    . PRO A 1 1689 ? 53.083  61.301  130.600 1.00 19.88  ? 1689 PRO A CA    1 
ATOM   1910  C  C     . PRO A 1 1689 ? 53.558  60.425  129.450 1.00 14.95  ? 1689 PRO A C     1 
ATOM   1911  O  O     . PRO A 1 1689 ? 52.819  59.589  128.927 1.00 21.80  ? 1689 PRO A O     1 
ATOM   1912  C  CB    . PRO A 1 1689 ? 53.380  60.648  131.956 1.00 21.58  ? 1689 PRO A CB    1 
ATOM   1913  C  CG    . PRO A 1 1689 ? 52.135  60.784  132.765 1.00 22.27  ? 1689 PRO A CG    1 
ATOM   1914  C  CD    . PRO A 1 1689 ? 50.997  60.894  131.810 1.00 20.84  ? 1689 PRO A CD    1 
ATOM   1915  N  N     . VAL A 1 1690 ? 54.812  60.629  129.060 1.00 15.08  ? 1690 VAL A N     1 
ATOM   1916  C  CA    . VAL A 1 1690 ? 55.452  59.860  127.999 1.00 16.08  ? 1690 VAL A CA    1 
ATOM   1917  C  C     . VAL A 1 1690 ? 56.335  58.810  128.660 1.00 16.24  ? 1690 VAL A C     1 
ATOM   1918  O  O     . VAL A 1 1690 ? 57.275  59.143  129.390 1.00 17.63  ? 1690 VAL A O     1 
ATOM   1919  C  CB    . VAL A 1 1690 ? 56.262  60.761  127.057 1.00 13.23  ? 1690 VAL A CB    1 
ATOM   1920  C  CG1   . VAL A 1 1690 ? 57.067  59.918  126.079 1.00 9.45   ? 1690 VAL A CG1   1 
ATOM   1921  C  CG2   . VAL A 1 1690 ? 55.340  61.716  126.315 1.00 9.44   ? 1690 VAL A CG2   1 
ATOM   1922  N  N     . SER A 1 1691 ? 56.040  57.538  128.405 1.00 16.53  ? 1691 SER A N     1 
ATOM   1923  C  CA    . SER A 1 1691 ? 56.768  56.443  129.032 1.00 17.93  ? 1691 SER A CA    1 
ATOM   1924  C  C     . SER A 1 1691 ? 57.983  56.074  128.188 1.00 19.74  ? 1691 SER A C     1 
ATOM   1925  O  O     . SER A 1 1691 ? 57.845  55.697  127.020 1.00 15.31  ? 1691 SER A O     1 
ATOM   1926  C  CB    . SER A 1 1691 ? 55.854  55.234  129.217 1.00 20.48  ? 1691 SER A CB    1 
ATOM   1927  O  OG    . SER A 1 1691 ? 56.589  54.099  129.639 1.00 25.71  ? 1691 SER A OG    1 
ATOM   1928  N  N     . ILE A 1 1692 ? 59.172  56.187  128.781 1.00 21.05  ? 1692 ILE A N     1 
ATOM   1929  C  CA    . ILE A 1 1692 ? 60.392  55.783  128.091 1.00 20.11  ? 1692 ILE A CA    1 
ATOM   1930  C  C     . ILE A 1 1692 ? 60.453  54.265  127.936 1.00 24.36  ? 1692 ILE A C     1 
ATOM   1931  O  O     . ILE A 1 1692 ? 60.953  53.762  126.924 1.00 24.24  ? 1692 ILE A O     1 
ATOM   1932  C  CB    . ILE A 1 1692 ? 61.624  56.337  128.828 1.00 21.04  ? 1692 ILE A CB    1 
ATOM   1933  C  CG1   . ILE A 1 1692 ? 61.729  57.850  128.621 1.00 16.90  ? 1692 ILE A CG1   1 
ATOM   1934  C  CG2   . ILE A 1 1692 ? 62.902  55.652  128.363 1.00 22.97  ? 1692 ILE A CG2   1 
ATOM   1935  C  CD1   . ILE A 1 1692 ? 62.818  58.506  129.438 1.00 15.37  ? 1692 ILE A CD1   1 
ATOM   1936  N  N     . THR A 1 1693 ? 59.942  53.515  128.916 1.00 24.88  ? 1693 THR A N     1 
ATOM   1937  C  CA    . THR A 1 1693 ? 59.964  52.058  128.821 1.00 26.46  ? 1693 THR A CA    1 
ATOM   1938  C  C     . THR A 1 1693 ? 59.144  51.564  127.636 1.00 24.94  ? 1693 THR A C     1 
ATOM   1939  O  O     . THR A 1 1693 ? 59.540  50.614  126.951 1.00 29.23  ? 1693 THR A O     1 
ATOM   1940  C  CB    . THR A 1 1693 ? 59.449  51.435  130.118 1.00 31.14  ? 1693 THR A CB    1 
ATOM   1941  O  OG1   . THR A 1 1693 ? 58.056  51.731  130.275 1.00 34.60  ? 1693 THR A OG1   1 
ATOM   1942  C  CG2   . THR A 1 1693 ? 60.217  51.977  131.310 1.00 27.13  ? 1693 THR A CG2   1 
ATOM   1943  N  N     . GLU A 1 1694 ? 57.996  52.194  127.380 1.00 25.47  ? 1694 GLU A N     1 
ATOM   1944  C  CA    . GLU A 1 1694 ? 57.158  51.778  126.260 1.00 25.86  ? 1694 GLU A CA    1 
ATOM   1945  C  C     . GLU A 1 1694 ? 57.828  52.075  124.924 1.00 24.65  ? 1694 GLU A C     1 
ATOM   1946  O  O     . GLU A 1 1694 ? 57.638  51.338  123.950 1.00 21.66  ? 1694 GLU A O     1 
ATOM   1947  C  CB    . GLU A 1 1694 ? 55.795  52.464  126.343 1.00 30.52  ? 1694 GLU A CB    1 
ATOM   1948  C  CG    . GLU A 1 1694 ? 54.957  52.044  127.540 1.00 38.94  ? 1694 GLU A CG    1 
ATOM   1949  C  CD    . GLU A 1 1694 ? 54.522  50.593  127.470 1.00 57.72  ? 1694 GLU A CD    1 
ATOM   1950  O  OE1   . GLU A 1 1694 ? 54.317  50.084  126.348 1.00 61.50  ? 1694 GLU A OE1   1 
ATOM   1951  O  OE2   . GLU A 1 1694 ? 54.386  49.961  128.539 1.00 67.08  ? 1694 GLU A OE2   1 
ATOM   1952  N  N     . HIS A 1 1695 ? 58.612  53.150  124.857 1.00 26.41  ? 1695 HIS A N     1 
ATOM   1953  C  CA    . HIS A 1 1695 ? 59.290  53.576  123.633 1.00 25.34  ? 1695 HIS A CA    1 
ATOM   1954  C  C     . HIS A 1 1695 ? 60.759  53.815  123.956 1.00 23.94  ? 1695 HIS A C     1 
ATOM   1955  O  O     . HIS A 1 1695 ? 61.203  54.965  124.075 1.00 21.37  ? 1695 HIS A O     1 
ATOM   1956  C  CB    . HIS A 1 1695 ? 58.629  54.826  123.052 1.00 21.20  ? 1695 HIS A CB    1 
ATOM   1957  C  CG    . HIS A 1 1695 ? 57.138  54.834  123.190 1.00 23.35  ? 1695 HIS A CG    1 
ATOM   1958  N  ND1   . HIS A 1 1695 ? 56.298  54.341  122.216 1.00 21.56  ? 1695 HIS A ND1   1 
ATOM   1959  C  CD2   . HIS A 1 1695 ? 56.338  55.257  124.198 1.00 21.51  ? 1695 HIS A CD2   1 
ATOM   1960  C  CE1   . HIS A 1 1695 ? 55.044  54.471  122.611 1.00 21.19  ? 1695 HIS A CE1   1 
ATOM   1961  N  NE2   . HIS A 1 1695 ? 55.041  55.023  123.811 1.00 20.84  ? 1695 HIS A NE2   1 
ATOM   1962  N  N     . PRO A 1 1696 ? 61.542  52.742  124.120 1.00 26.58  ? 1696 PRO A N     1 
ATOM   1963  C  CA    . PRO A 1 1696 ? 62.937  52.912  124.564 1.00 22.64  ? 1696 PRO A CA    1 
ATOM   1964  C  C     . PRO A 1 1696 ? 63.797  53.739  123.625 1.00 19.36  ? 1696 PRO A C     1 
ATOM   1965  O  O     . PRO A 1 1696 ? 64.682  54.467  124.090 1.00 21.25  ? 1696 PRO A O     1 
ATOM   1966  C  CB    . PRO A 1 1696 ? 63.438  51.464  124.663 1.00 22.92  ? 1696 PRO A CB    1 
ATOM   1967  C  CG    . PRO A 1 1696 ? 62.195  50.664  124.897 1.00 22.67  ? 1696 PRO A CG    1 
ATOM   1968  C  CD    . PRO A 1 1696 ? 61.180  51.320  124.011 1.00 20.94  ? 1696 PRO A CD    1 
ATOM   1969  N  N     . LYS A 1 1697 ? 63.572  53.644  122.316 1.00 19.88  ? 1697 LYS A N     1 
ATOM   1970  C  CA    . LYS A 1 1697 ? 64.445  54.306  121.356 1.00 20.05  ? 1697 LYS A CA    1 
ATOM   1971  C  C     . LYS A 1 1697 ? 64.319  55.820  121.492 1.00 18.57  ? 1697 LYS A C     1 
ATOM   1972  O  O     . LYS A 1 1697 ? 63.213  56.358  121.582 1.00 18.24  ? 1697 LYS A O     1 
ATOM   1973  C  CB    . LYS A 1 1697 ? 64.100  53.843  119.939 1.00 23.20  ? 1697 LYS A CB    1 
ATOM   1974  C  CG    . LYS A 1 1697 ? 65.023  54.364  118.855 1.00 26.39  ? 1697 LYS A CG    1 
ATOM   1975  C  CD    . LYS A 1 1697 ? 64.651  53.775  117.501 1.00 37.77  ? 1697 LYS A CD    1 
ATOM   1976  C  CE    . LYS A 1 1697 ? 65.555  54.283  116.391 1.00 48.04  ? 1697 LYS A CE    1 
ATOM   1977  N  NZ    . LYS A 1 1697 ? 65.184  53.706  115.070 1.00 44.89  ? 1697 LYS A NZ    1 
ATOM   1978  N  N     . ILE A 1 1698 ? 65.467  56.503  121.509 1.00 18.89  ? 1698 ILE A N     1 
ATOM   1979  C  CA    . ILE A 1 1698 ? 65.522  57.859  122.054 1.00 15.35  ? 1698 ILE A CA    1 
ATOM   1980  C  C     . ILE A 1 1698 ? 64.759  58.843  121.172 1.00 12.79  ? 1698 ILE A C     1 
ATOM   1981  O  O     . ILE A 1 1698 ? 64.044  59.720  121.673 1.00 12.33  ? 1698 ILE A O     1 
ATOM   1982  C  CB    . ILE A 1 1698 ? 66.983  58.293  122.283 1.00 17.52  ? 1698 ILE A CB    1 
ATOM   1983  C  CG1   . ILE A 1 1698 ? 67.027  59.588  123.097 1.00 14.42  ? 1698 ILE A CG1   1 
ATOM   1984  C  CG2   . ILE A 1 1698 ? 67.752  58.419  120.971 1.00 16.09  ? 1698 ILE A CG2   1 
ATOM   1985  C  CD1   . ILE A 1 1698 ? 68.333  59.812  123.813 1.00 20.12  ? 1698 ILE A CD1   1 
ATOM   1986  N  N     . ASN A 1 1699 ? 64.887  58.713  119.849 1.00 14.63  ? 1699 ASN A N     1 
ATOM   1987  C  CA    . ASN A 1 1699 ? 64.207  59.652  118.964 1.00 11.54  ? 1699 ASN A CA    1 
ATOM   1988  C  C     . ASN A 1 1699 ? 62.694  59.496  119.056 1.00 11.66  ? 1699 ASN A C     1 
ATOM   1989  O  O     . ASN A 1 1699 ? 61.958  60.485  118.969 1.00 12.07  ? 1699 ASN A O     1 
ATOM   1990  C  CB    . ASN A 1 1699 ? 64.689  59.475  117.524 1.00 11.82  ? 1699 ASN A CB    1 
ATOM   1991  C  CG    . ASN A 1 1699 ? 64.620  58.041  117.058 1.00 19.05  ? 1699 ASN A CG    1 
ATOM   1992  O  OD1   . ASN A 1 1699 ? 65.310  57.177  117.590 1.00 25.32  ? 1699 ASN A OD1   1 
ATOM   1993  N  ND2   . ASN A 1 1699 ? 63.789  57.779  116.057 1.00 18.66  ? 1699 ASN A ND2   1 
ATOM   1994  N  N     . GLU A 1 1700 ? 62.214  58.268  119.264 1.00 11.01  ? 1700 GLU A N     1 
ATOM   1995  C  CA    . GLU A 1 1700 ? 60.777  58.043  119.379 1.00 13.37  ? 1700 GLU A CA    1 
ATOM   1996  C  C     . GLU A 1 1700 ? 60.193  58.786  120.576 1.00 11.98  ? 1700 GLU A C     1 
ATOM   1997  O  O     . GLU A 1 1700 ? 59.223  59.543  120.442 1.00 12.04  ? 1700 GLU A O     1 
ATOM   1998  C  CB    . GLU A 1 1700 ? 60.478  56.546  119.479 1.00 14.28  ? 1700 GLU A CB    1 
ATOM   1999  C  CG    . GLU A 1 1700 ? 60.755  55.760  118.211 1.00 21.80  ? 1700 GLU A CG    1 
ATOM   2000  C  CD    . GLU A 1 1700 ? 60.886  54.272  118.470 1.00 42.52  ? 1700 GLU A CD    1 
ATOM   2001  O  OE1   . GLU A 1 1700 ? 60.363  53.800  119.502 1.00 39.60  ? 1700 GLU A OE1   1 
ATOM   2002  O  OE2   . GLU A 1 1700 ? 61.498  53.571  117.639 1.00 42.99  ? 1700 GLU A OE2   1 
ATOM   2003  N  N     . TRP A 1 1701 ? 60.773  58.592  121.765 1.00 9.37   ? 1701 TRP A N     1 
ATOM   2004  C  CA    . TRP A 1 1701 ? 60.178  59.237  122.929 1.00 8.48   ? 1701 TRP A CA    1 
ATOM   2005  C  C     . TRP A 1 1701 ? 60.509  60.722  122.974 1.00 7.45   ? 1701 TRP A C     1 
ATOM   2006  O  O     . TRP A 1 1701 ? 59.771  61.490  123.591 1.00 9.21   ? 1701 TRP A O     1 
ATOM   2007  C  CB    . TRP A 1 1701 ? 60.589  58.544  124.234 1.00 10.56  ? 1701 TRP A CB    1 
ATOM   2008  C  CG    . TRP A 1 1701 ? 62.030  58.646  124.630 1.00 13.90  ? 1701 TRP A CG    1 
ATOM   2009  C  CD1   . TRP A 1 1701 ? 63.018  57.747  124.365 1.00 12.75  ? 1701 TRP A CD1   1 
ATOM   2010  C  CD2   . TRP A 1 1701 ? 62.635  59.692  125.401 1.00 13.66  ? 1701 TRP A CD2   1 
ATOM   2011  N  NE1   . TRP A 1 1701 ? 64.204  58.173  124.912 1.00 13.11  ? 1701 TRP A NE1   1 
ATOM   2012  C  CE2   . TRP A 1 1701 ? 63.997  59.367  125.549 1.00 14.91  ? 1701 TRP A CE2   1 
ATOM   2013  C  CE3   . TRP A 1 1701 ? 62.159  60.877  125.971 1.00 9.34   ? 1701 TRP A CE3   1 
ATOM   2014  C  CZ2   . TRP A 1 1701 ? 64.889  60.181  126.244 1.00 14.23  ? 1701 TRP A CZ2   1 
ATOM   2015  C  CZ3   . TRP A 1 1701 ? 63.046  61.684  126.659 1.00 10.74  ? 1701 TRP A CZ3   1 
ATOM   2016  C  CH2   . TRP A 1 1701 ? 64.395  61.333  126.790 1.00 14.39  ? 1701 TRP A CH2   1 
ATOM   2017  N  N     . LEU A 1 1702 ? 61.576  61.161  122.299 1.00 7.24   ? 1702 LEU A N     1 
ATOM   2018  C  CA    . LEU A 1 1702 ? 61.788  62.600  122.153 1.00 6.90   ? 1702 LEU A CA    1 
ATOM   2019  C  C     . LEU A 1 1702 ? 60.709  63.231  121.278 1.00 8.06   ? 1702 LEU A C     1 
ATOM   2020  O  O     . LEU A 1 1702 ? 60.198  64.315  121.592 1.00 8.94   ? 1702 LEU A O     1 
ATOM   2021  C  CB    . LEU A 1 1702 ? 63.179  62.876  121.584 1.00 6.18   ? 1702 LEU A CB    1 
ATOM   2022  C  CG    . LEU A 1 1702 ? 64.335  62.836  122.585 1.00 6.73   ? 1702 LEU A CG    1 
ATOM   2023  C  CD1   . LEU A 1 1702 ? 65.652  63.162  121.901 1.00 8.01   ? 1702 LEU A CD1   1 
ATOM   2024  C  CD2   . LEU A 1 1702 ? 64.077  63.791  123.741 1.00 6.30   ? 1702 LEU A CD2   1 
ATOM   2025  N  N     . THR A 1 1703 ? 60.342  62.561  120.181 1.00 6.80   ? 1703 THR A N     1 
ATOM   2026  C  CA    . THR A 1 1703 ? 59.231  63.027  119.357 1.00 7.59   ? 1703 THR A CA    1 
ATOM   2027  C  C     . THR A 1 1703 ? 57.932  63.041  120.152 1.00 7.55   ? 1703 THR A C     1 
ATOM   2028  O  O     . THR A 1 1703 ? 57.136  63.985  120.047 1.00 9.98   ? 1703 THR A O     1 
ATOM   2029  C  CB    . THR A 1 1703 ? 59.095  62.138  118.118 1.00 8.26   ? 1703 THR A CB    1 
ATOM   2030  O  OG1   . THR A 1 1703 ? 60.183  62.393  117.222 1.00 10.99  ? 1703 THR A OG1   1 
ATOM   2031  C  CG2   . THR A 1 1703 ? 57.779  62.400  117.399 1.00 9.66   ? 1703 THR A CG2   1 
ATOM   2032  N  N     . LEU A 1 1704 ? 57.702  61.999  120.953 1.00 5.61   ? 1704 LEU A N     1 
ATOM   2033  C  CA    . LEU A 1 1704 ? 56.512  61.962  121.796 1.00 7.13   ? 1704 LEU A CA    1 
ATOM   2034  C  C     . LEU A 1 1704 ? 56.518  63.094  122.817 1.00 7.16   ? 1704 LEU A C     1 
ATOM   2035  O  O     . LEU A 1 1704 ? 55.474  63.693  123.088 1.00 6.79   ? 1704 LEU A O     1 
ATOM   2036  C  CB    . LEU A 1 1704 ? 56.398  60.608  122.493 1.00 7.18   ? 1704 LEU A CB    1 
ATOM   2037  C  CG    . LEU A 1 1704 ? 56.230  59.401  121.571 1.00 9.86   ? 1704 LEU A CG    1 
ATOM   2038  C  CD1   . LEU A 1 1704 ? 56.183  58.121  122.378 1.00 11.89  ? 1704 LEU A CD1   1 
ATOM   2039  C  CD2   . LEU A 1 1704 ? 54.978  59.547  120.721 1.00 6.68   ? 1704 LEU A CD2   1 
ATOM   2040  N  N     . VAL A 1 1705 ? 57.683  63.400  123.391 1.00 6.59   ? 1705 VAL A N     1 
ATOM   2041  C  CA    . VAL A 1 1705 ? 57.786  64.501  124.346 1.00 6.74   ? 1705 VAL A CA    1 
ATOM   2042  C  C     . VAL A 1 1705 ? 57.455  65.825  123.670 1.00 7.37   ? 1705 VAL A C     1 
ATOM   2043  O  O     . VAL A 1 1705 ? 56.743  66.662  124.230 1.00 11.57  ? 1705 VAL A O     1 
ATOM   2044  C  CB    . VAL A 1 1705 ? 59.183  64.527  124.992 1.00 6.11   ? 1705 VAL A CB    1 
ATOM   2045  C  CG1   . VAL A 1 1705 ? 59.444  65.872  125.652 1.00 3.55   ? 1705 VAL A CG1   1 
ATOM   2046  C  CG2   . VAL A 1 1705 ? 59.305  63.417  126.021 1.00 5.71   ? 1705 VAL A CG2   1 
ATOM   2047  N  N     . GLU A 1 1706 ? 57.966  66.034  122.456 1.00 5.13   ? 1706 GLU A N     1 
ATOM   2048  C  CA    . GLU A 1 1706 ? 57.686  67.282  121.745 1.00 6.98   ? 1706 GLU A CA    1 
ATOM   2049  C  C     . GLU A 1 1706 ? 56.199  67.410  121.409 1.00 7.85   ? 1706 GLU A C     1 
ATOM   2050  O  O     . GLU A 1 1706 ? 55.583  68.468  121.624 1.00 7.25   ? 1706 GLU A O     1 
ATOM   2051  C  CB    . GLU A 1 1706 ? 58.549  67.359  120.485 1.00 8.62   ? 1706 GLU A CB    1 
ATOM   2052  C  CG    . GLU A 1 1706 ? 58.022  68.274  119.396 1.00 11.69  ? 1706 GLU A CG    1 
ATOM   2053  C  CD    . GLU A 1 1706 ? 58.633  67.964  118.043 1.00 18.97  ? 1706 GLU A CD    1 
ATOM   2054  O  OE1   . GLU A 1 1706 ? 59.109  68.903  117.372 1.00 20.92  ? 1706 GLU A OE1   1 
ATOM   2055  O  OE2   . GLU A 1 1706 ? 58.645  66.778  117.654 1.00 20.40  ? 1706 GLU A OE2   1 
ATOM   2056  N  N     . LYS A 1 1707 ? 55.600  66.332  120.894 1.00 8.54   ? 1707 LYS A N     1 
ATOM   2057  C  CA    . LYS A 1 1707 ? 54.173  66.358  120.580 1.00 7.20   ? 1707 LYS A CA    1 
ATOM   2058  C  C     . LYS A 1 1707 ? 53.335  66.590  121.830 1.00 5.32   ? 1707 LYS A C     1 
ATOM   2059  O  O     . LYS A 1 1707 ? 52.376  67.373  121.807 1.00 5.56   ? 1707 LYS A O     1 
ATOM   2060  C  CB    . LYS A 1 1707 ? 53.753  65.056  119.898 1.00 7.94   ? 1707 LYS A CB    1 
ATOM   2061  C  CG    . LYS A 1 1707 ? 54.171  64.937  118.444 1.00 13.59  ? 1707 LYS A CG    1 
ATOM   2062  C  CD    . LYS A 1 1707 ? 54.188  63.483  118.000 1.00 17.26  ? 1707 LYS A CD    1 
ATOM   2063  C  CE    . LYS A 1 1707 ? 54.235  63.363  116.486 1.00 19.50  ? 1707 LYS A CE    1 
ATOM   2064  N  NZ    . LYS A 1 1707 ? 55.279  64.238  115.887 1.00 21.58  ? 1707 LYS A NZ    1 
ATOM   2065  N  N     . GLU A 1 1708 ? 53.679  65.918  122.930 1.00 6.57   ? 1708 GLU A N     1 
ATOM   2066  C  CA    . GLU A 1 1708 ? 52.929  66.088  124.165 1.00 6.28   ? 1708 GLU A CA    1 
ATOM   2067  C  C     . GLU A 1 1708 ? 53.135  67.474  124.754 1.00 4.83   ? 1708 GLU A C     1 
ATOM   2068  O  O     . GLU A 1 1708 ? 52.220  68.017  125.371 1.00 4.07   ? 1708 GLU A O     1 
ATOM   2069  C  CB    . GLU A 1 1708 ? 53.320  65.007  125.172 1.00 5.94   ? 1708 GLU A CB    1 
ATOM   2070  C  CG    . GLU A 1 1708 ? 52.522  65.052  126.458 1.00 8.83   ? 1708 GLU A CG    1 
ATOM   2071  C  CD    . GLU A 1 1708 ? 51.050  64.764  126.241 1.00 18.36  ? 1708 GLU A CD    1 
ATOM   2072  O  OE1   . GLU A 1 1708 ? 50.717  64.050  125.272 1.00 23.76  ? 1708 GLU A OE1   1 
ATOM   2073  O  OE2   . GLU A 1 1708 ? 50.225  65.257  127.038 1.00 16.98  ? 1708 GLU A OE2   1 
ATOM   2074  N  N     . MET A 1 1709 ? 54.312  68.068  124.561 1.00 5.14   ? 1709 MET A N     1 
ATOM   2075  C  CA    . MET A 1 1709 ? 54.523  69.454  124.959 1.00 4.16   ? 1709 MET A CA    1 
ATOM   2076  C  C     . MET A 1 1709 ? 53.561  70.374  124.224 1.00 4.30   ? 1709 MET A C     1 
ATOM   2077  O  O     . MET A 1 1709 ? 52.879  71.207  124.836 1.00 3.22   ? 1709 MET A O     1 
ATOM   2078  C  CB    . MET A 1 1709 ? 55.974  69.857  124.688 1.00 3.64   ? 1709 MET A CB    1 
ATOM   2079  C  CG    . MET A 1 1709 ? 56.179  71.351  124.491 1.00 3.79   ? 1709 MET A CG    1 
ATOM   2080  S  SD    . MET A 1 1709 ? 57.808  71.751  123.830 1.00 9.51   ? 1709 MET A SD    1 
ATOM   2081  C  CE    . MET A 1 1709 ? 57.424  71.953  122.093 1.00 4.34   ? 1709 MET A CE    1 
ATOM   2082  N  N     . ARG A 1 1710 ? 53.479  70.220  122.899 1.00 4.73   ? 1710 ARG A N     1 
ATOM   2083  C  CA    . ARG A 1 1710 ? 52.572  71.059  122.119 1.00 2.99   ? 1710 ARG A CA    1 
ATOM   2084  C  C     . ARG A 1 1710 ? 51.121  70.856  122.550 1.00 3.15   ? 1710 ARG A C     1 
ATOM   2085  O  O     . ARG A 1 1710 ? 50.376  71.825  122.755 1.00 2.79   ? 1710 ARG A O     1 
ATOM   2086  C  CB    . ARG A 1 1710 ? 52.743  70.771  120.628 1.00 3.02   ? 1710 ARG A CB    1 
ATOM   2087  C  CG    . ARG A 1 1710 ? 54.130  71.087  120.095 1.00 3.18   ? 1710 ARG A CG    1 
ATOM   2088  C  CD    . ARG A 1 1710 ? 54.080  71.475  118.627 1.00 3.35   ? 1710 ARG A CD    1 
ATOM   2089  N  NE    . ARG A 1 1710 ? 55.225  70.965  117.884 1.00 11.39  ? 1710 ARG A NE    1 
ATOM   2090  C  CZ    . ARG A 1 1710 ? 56.294  71.686  117.574 1.00 11.03  ? 1710 ARG A CZ    1 
ATOM   2091  N  NH1   . ARG A 1 1710 ? 56.399  72.955  117.930 1.00 6.27   ? 1710 ARG A NH1   1 
ATOM   2092  N  NH2   . ARG A 1 1710 ? 57.282  71.118  116.889 1.00 9.43   ? 1710 ARG A NH2   1 
ATOM   2093  N  N     . VAL A 1 1711 ? 50.709  69.598  122.722 1.00 3.34   ? 1711 VAL A N     1 
ATOM   2094  C  CA    . VAL A 1 1711 ? 49.315  69.308  123.053 1.00 3.34   ? 1711 VAL A CA    1 
ATOM   2095  C  C     . VAL A 1 1711 ? 48.984  69.793  124.462 1.00 3.32   ? 1711 VAL A C     1 
ATOM   2096  O  O     . VAL A 1 1711 ? 47.885  70.304  124.719 1.00 5.19   ? 1711 VAL A O     1 
ATOM   2097  C  CB    . VAL A 1 1711 ? 49.031  67.804  122.879 1.00 5.28   ? 1711 VAL A CB    1 
ATOM   2098  C  CG1   . VAL A 1 1711 ? 47.656  67.446  123.418 1.00 4.91   ? 1711 VAL A CG1   1 
ATOM   2099  C  CG2   . VAL A 1 1711 ? 49.148  67.411  121.414 1.00 5.64   ? 1711 VAL A CG2   1 
ATOM   2100  N  N     . THR A 1 1712 ? 49.925  69.640  125.396 1.00 3.60   ? 1712 THR A N     1 
ATOM   2101  C  CA    . THR A 1 1712 ? 49.719  70.107  126.760 1.00 4.25   ? 1712 THR A CA    1 
ATOM   2102  C  C     . THR A 1 1712 ? 49.599  71.622  126.806 1.00 3.58   ? 1712 THR A C     1 
ATOM   2103  O  O     . THR A 1 1712 ? 48.757  72.164  127.529 1.00 3.14   ? 1712 THR A O     1 
ATOM   2104  C  CB    . THR A 1 1712 ? 50.863  69.629  127.655 1.00 4.35   ? 1712 THR A CB    1 
ATOM   2105  O  OG1   . THR A 1 1712 ? 50.867  68.198  127.708 1.00 7.57   ? 1712 THR A OG1   1 
ATOM   2106  C  CG2   . THR A 1 1712 ? 50.707  70.183  129.058 1.00 3.85   ? 1712 THR A CG2   1 
ATOM   2107  N  N     . LEU A 1 1713 ? 50.441  72.327  126.047 1.00 3.72   ? 1713 LEU A N     1 
ATOM   2108  C  CA    . LEU A 1 1713 ? 50.308  73.779  125.975 1.00 2.48   ? 1713 LEU A CA    1 
ATOM   2109  C  C     . LEU A 1 1713 ? 48.962  74.171  125.378 1.00 2.45   ? 1713 LEU A C     1 
ATOM   2110  O  O     . LEU A 1 1713 ? 48.329  75.130  125.831 1.00 3.29   ? 1713 LEU A O     1 
ATOM   2111  C  CB    . LEU A 1 1713 ? 51.462  74.384  125.176 1.00 2.86   ? 1713 LEU A CB    1 
ATOM   2112  C  CG    . LEU A 1 1713 ? 52.850  74.226  125.801 1.00 2.77   ? 1713 LEU A CG    1 
ATOM   2113  C  CD1   . LEU A 1 1713 ? 53.887  75.010  125.023 1.00 2.47   ? 1713 LEU A CD1   1 
ATOM   2114  C  CD2   . LEU A 1 1713 ? 52.831  74.663  127.257 1.00 1.82   ? 1713 LEU A CD2   1 
ATOM   2115  N  N     . ALA A 1 1714 ? 48.497  73.426  124.372 1.00 2.90   ? 1714 ALA A N     1 
ATOM   2116  C  CA    . ALA A 1 1714 ? 47.186  73.713  123.793 1.00 2.82   ? 1714 ALA A CA    1 
ATOM   2117  C  C     . ALA A 1 1714 ? 46.066  73.539  124.817 1.00 3.58   ? 1714 ALA A C     1 
ATOM   2118  O  O     . ALA A 1 1714 ? 45.173  74.388  124.924 1.00 4.81   ? 1714 ALA A O     1 
ATOM   2119  C  CB    . ALA A 1 1714 ? 46.944  72.821  122.575 1.00 4.01   ? 1714 ALA A CB    1 
ATOM   2120  N  N     . LYS A 1 1715 ? 46.099  72.448  125.585 1.00 3.33   ? 1715 LYS A N     1 
ATOM   2121  C  CA    . LYS A 1 1715 ? 45.049  72.208  126.576 1.00 4.81   ? 1715 LYS A CA    1 
ATOM   2122  C  C     . LYS A 1 1715 ? 45.115  73.219  127.717 1.00 4.93   ? 1715 LYS A C     1 
ATOM   2123  O  O     . LYS A 1 1715 ? 44.077  73.694  128.206 1.00 5.72   ? 1715 LYS A O     1 
ATOM   2124  C  CB    . LYS A 1 1715 ? 45.155  70.782  127.114 1.00 7.15   ? 1715 LYS A CB    1 
ATOM   2125  C  CG    . LYS A 1 1715 ? 44.930  69.708  126.065 1.00 8.75   ? 1715 LYS A CG    1 
ATOM   2126  C  CD    . LYS A 1 1715 ? 44.782  68.336  126.701 1.00 15.58  ? 1715 LYS A CD    1 
ATOM   2127  C  CE    . LYS A 1 1715 ? 44.730  67.242  125.648 1.00 16.51  ? 1715 LYS A CE    1 
ATOM   2128  N  NZ    . LYS A 1 1715 ? 43.649  67.477  124.652 1.00 26.73  ? 1715 LYS A NZ    1 
ATOM   2129  N  N     . LEU A 1 1716 ? 46.328  73.551  128.163 1.00 4.67   ? 1716 LEU A N     1 
ATOM   2130  C  CA    . LEU A 1 1716 ? 46.488  74.559  129.201 1.00 4.59   ? 1716 LEU A CA    1 
ATOM   2131  C  C     . LEU A 1 1716 ? 45.997  75.917  128.721 1.00 5.33   ? 1716 LEU A C     1 
ATOM   2132  O  O     . LEU A 1 1716 ? 45.414  76.677  129.497 1.00 6.50   ? 1716 LEU A O     1 
ATOM   2133  C  CB    . LEU A 1 1716 ? 47.949  74.633  129.641 1.00 3.95   ? 1716 LEU A CB    1 
ATOM   2134  C  CG    . LEU A 1 1716 ? 48.498  73.478  130.480 1.00 4.44   ? 1716 LEU A CG    1 
ATOM   2135  C  CD1   . LEU A 1 1716 ? 50.000  73.622  130.662 1.00 4.18   ? 1716 LEU A CD1   1 
ATOM   2136  C  CD2   . LEU A 1 1716 ? 47.798  73.417  131.826 1.00 6.35   ? 1716 LEU A CD2   1 
ATOM   2137  N  N     . LEU A 1 1717 ? 46.221  76.240  127.444 1.00 4.00   ? 1717 LEU A N     1 
ATOM   2138  C  CA    . LEU A 1 1717 ? 45.650  77.458  126.879 1.00 4.02   ? 1717 LEU A CA    1 
ATOM   2139  C  C     . LEU A 1 1717 ? 44.130  77.392  126.853 1.00 5.65   ? 1717 LEU A C     1 
ATOM   2140  O  O     . LEU A 1 1717 ? 43.457  78.392  127.123 1.00 5.08   ? 1717 LEU A O     1 
ATOM   2141  C  CB    . LEU A 1 1717 ? 46.189  77.699  125.471 1.00 3.66   ? 1717 LEU A CB    1 
ATOM   2142  C  CG    . LEU A 1 1717 ? 45.735  79.012  124.825 1.00 3.71   ? 1717 LEU A CG    1 
ATOM   2143  C  CD1   . LEU A 1 1717 ? 46.262  80.218  125.593 1.00 2.21   ? 1717 LEU A CD1   1 
ATOM   2144  C  CD2   . LEU A 1 1717 ? 46.144  79.075  123.364 1.00 2.69   ? 1717 LEU A CD2   1 
ATOM   2145  N  N     . ALA A 1 1718 ? 43.571  76.230  126.514 1.00 7.27   ? 1718 ALA A N     1 
ATOM   2146  C  CA    . ALA A 1 1718 ? 42.122  76.080  126.504 1.00 7.70   ? 1718 ALA A CA    1 
ATOM   2147  C  C     . ALA A 1 1718 ? 41.503  76.319  127.873 1.00 10.64  ? 1718 ALA A C     1 
ATOM   2148  O  O     . ALA A 1 1718 ? 40.430  76.928  127.952 1.00 15.02  ? 1718 ALA A O     1 
ATOM   2149  C  CB    . ALA A 1 1718 ? 41.738  74.690  125.997 1.00 8.94   ? 1718 ALA A CB    1 
ATOM   2150  N  N     . GLU A 1 1719 ? 42.152  75.867  128.943 1.00 9.52   ? 1719 GLU A N     1 
ATOM   2151  C  CA    . GLU A 1 1719 ? 41.692  76.157  130.300 1.00 8.89   ? 1719 GLU A CA    1 
ATOM   2152  C  C     . GLU A 1 1719 ? 41.968  77.598  130.722 1.00 10.82  ? 1719 GLU A C     1 
ATOM   2153  O  O     . GLU A 1 1719 ? 41.122  78.241  131.368 1.00 13.18  ? 1719 GLU A O     1 
ATOM   2154  C  CB    . GLU A 1 1719 ? 42.353  75.197  131.294 1.00 10.89  ? 1719 GLU A CB    1 
ATOM   2155  C  CG    . GLU A 1 1719 ? 42.121  73.726  130.987 1.00 13.88  ? 1719 GLU A CG    1 
ATOM   2156  C  CD    . GLU A 1 1719 ? 43.267  72.847  131.447 1.00 18.17  ? 1719 GLU A CD    1 
ATOM   2157  O  OE1   . GLU A 1 1719 ? 44.261  73.389  131.972 1.00 15.45  ? 1719 GLU A OE1   1 
ATOM   2158  O  OE2   . GLU A 1 1719 ? 43.175  71.612  131.281 1.00 19.38  ? 1719 GLU A OE2   1 
ATOM   2159  N  N     . SER A 1 1720 ? 43.135  78.126  130.351 1.00 9.63   ? 1720 SER A N     1 
ATOM   2160  C  CA    . SER A 1 1720 ? 43.497  79.485  130.723 1.00 6.54   ? 1720 SER A CA    1 
ATOM   2161  C  C     . SER A 1 1720 ? 42.541  80.492  130.104 1.00 8.85   ? 1720 SER A C     1 
ATOM   2162  O  O     . SER A 1 1720 ? 42.179  81.484  130.741 1.00 10.48  ? 1720 SER A O     1 
ATOM   2163  C  CB    . SER A 1 1720 ? 44.939  79.775  130.308 1.00 5.98   ? 1720 SER A CB    1 
ATOM   2164  O  OG    . SER A 1 1720 ? 45.352  81.052  130.760 1.00 4.84   ? 1720 SER A OG    1 
ATOM   2165  N  N     . VAL A 1 1721 ? 42.119  80.251  128.861 1.00 9.20   ? 1721 VAL A N     1 
ATOM   2166  C  CA    . VAL A 1 1721 ? 41.209  81.173  128.186 1.00 9.84   ? 1721 VAL A CA    1 
ATOM   2167  C  C     . VAL A 1 1721 ? 39.858  81.202  128.891 1.00 12.47  ? 1721 VAL A C     1 
ATOM   2168  O  O     . VAL A 1 1721 ? 39.288  82.272  129.142 1.00 12.82  ? 1721 VAL A O     1 
ATOM   2169  C  CB    . VAL A 1 1721 ? 41.065  80.794  126.701 1.00 8.10   ? 1721 VAL A CB    1 
ATOM   2170  C  CG1   . VAL A 1 1721 ? 39.847  81.470  126.092 1.00 10.01  ? 1721 VAL A CG1   1 
ATOM   2171  C  CG2   . VAL A 1 1721 ? 42.321  81.175  125.938 1.00 6.21   ? 1721 VAL A CG2   1 
ATOM   2172  N  N     . THR A 1 1722 ? 39.323  80.024  129.224 1.00 14.11  ? 1722 THR A N     1 
ATOM   2173  C  CA    . THR A 1 1722 ? 38.002  79.986  129.840 1.00 20.23  ? 1722 THR A CA    1 
ATOM   2174  C  C     . THR A 1 1722 ? 38.037  80.506  131.269 1.00 15.62  ? 1722 THR A C     1 
ATOM   2175  O  O     . THR A 1 1722 ? 36.989  80.865  131.819 1.00 19.33  ? 1722 THR A O     1 
ATOM   2176  C  CB    . THR A 1 1722 ? 37.417  78.571  129.794 1.00 22.17  ? 1722 THR A CB    1 
ATOM   2177  O  OG1   . THR A 1 1722 ? 36.086  78.590  130.324 1.00 28.26  ? 1722 THR A OG1   1 
ATOM   2178  C  CG2   . THR A 1 1722 ? 38.250  77.607  130.608 1.00 14.34  ? 1722 THR A CG2   1 
ATOM   2179  N  N     . GLU A 1 1723 ? 39.218  80.562  131.893 1.00 15.95  ? 1723 GLU A N     1 
ATOM   2180  C  CA    . GLU A 1 1723 ? 39.259  81.250  133.183 1.00 16.45  ? 1723 GLU A CA    1 
ATOM   2181  C  C     . GLU A 1 1723 ? 39.507  82.753  133.039 1.00 18.08  ? 1723 GLU A C     1 
ATOM   2182  O  O     . GLU A 1 1723 ? 38.994  83.539  133.843 1.00 20.86  ? 1723 GLU A O     1 
ATOM   2183  C  CB    . GLU A 1 1723 ? 40.305  80.630  134.106 1.00 16.40  ? 1723 GLU A CB    1 
ATOM   2184  C  CG    . GLU A 1 1723 ? 40.179  79.135  134.309 1.00 26.01  ? 1723 GLU A CG    1 
ATOM   2185  C  CD    . GLU A 1 1723 ? 41.271  78.584  135.204 1.00 33.57  ? 1723 GLU A CD    1 
ATOM   2186  O  OE1   . GLU A 1 1723 ? 42.085  79.386  135.710 1.00 25.18  ? 1723 GLU A OE1   1 
ATOM   2187  O  OE2   . GLU A 1 1723 ? 41.314  77.353  135.405 1.00 27.92  ? 1723 GLU A OE2   1 
ATOM   2188  N  N     . VAL A 1 1724 ? 40.287  83.183  132.040 1.00 17.47  ? 1724 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 1724 ? 40.589  84.609  131.923 1.00 16.16  ? 1724 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 1724 ? 39.382  85.362  131.382 1.00 20.57  ? 1724 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 1724 ? 39.235  86.567  131.623 1.00 23.31  ? 1724 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 1724 ? 41.835  84.853  131.043 1.00 12.64  ? 1724 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 1724 ? 41.656  84.264  129.668 1.00 13.28  ? 1724 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 1724 ? 42.166  86.330  130.943 1.00 13.24  ? 1724 VAL A CG2   1 
ATOM   2195  N  N     . GLU A 1 1725 ? 38.493  84.673  130.658 1.00 20.83  ? 1725 GLU A N     1 
ATOM   2196  C  CA    . GLU A 1 1725 ? 37.318  85.342  130.103 1.00 25.08  ? 1725 GLU A CA    1 
ATOM   2197  C  C     . GLU A 1 1725 ? 36.482  86.001  131.195 1.00 29.09  ? 1725 GLU A C     1 
ATOM   2198  O  O     . GLU A 1 1725 ? 35.769  86.978  130.935 1.00 37.43  ? 1725 GLU A O     1 
ATOM   2199  C  CB    . GLU A 1 1725 ? 36.474  84.346  129.307 1.00 27.97  ? 1725 GLU A CB    1 
ATOM   2200  C  CG    . GLU A 1 1725 ? 36.983  84.094  127.898 1.00 24.89  ? 1725 GLU A CG    1 
ATOM   2201  C  CD    . GLU A 1 1725 ? 36.199  83.015  127.180 1.00 28.57  ? 1725 GLU A CD    1 
ATOM   2202  O  OE1   . GLU A 1 1725 ? 36.166  81.871  127.680 1.00 26.85  ? 1725 GLU A OE1   1 
ATOM   2203  O  OE2   . GLU A 1 1725 ? 35.618  83.310  126.114 1.00 33.27  ? 1725 GLU A OE2   1 
ATOM   2204  N  N     . ILE A 1 1726 ? 36.553  85.480  132.421 1.00 26.17  ? 1726 ILE A N     1 
ATOM   2205  C  CA    . ILE A 1 1726 ? 35.884  86.128  133.547 1.00 27.26  ? 1726 ILE A CA    1 
ATOM   2206  C  C     . ILE A 1 1726 ? 36.515  87.486  133.830 1.00 26.85  ? 1726 ILE A C     1 
ATOM   2207  O  O     . ILE A 1 1726 ? 35.816  88.476  134.079 1.00 28.14  ? 1726 ILE A O     1 
ATOM   2208  C  CB    . ILE A 1 1726 ? 35.921  85.220  134.790 1.00 22.93  ? 1726 ILE A CB    1 
ATOM   2209  C  CG1   . ILE A 1 1726 ? 35.568  83.778  134.415 1.00 26.31  ? 1726 ILE A CG1   1 
ATOM   2210  C  CG2   . ILE A 1 1726 ? 34.982  85.747  135.862 1.00 26.44  ? 1726 ILE A CG2   1 
ATOM   2211  C  CD1   . ILE A 1 1726 ? 34.203  83.624  133.778 1.00 21.20  ? 1726 ILE A CD1   1 
ATOM   2212  N  N     . PHE A 1 1727 ? 37.849  87.551  133.803 1.00 25.73  ? 1727 PHE A N     1 
ATOM   2213  C  CA    . PHE A 1 1727 ? 38.541  88.812  134.057 1.00 25.61  ? 1727 PHE A CA    1 
ATOM   2214  C  C     . PHE A 1 1727 ? 38.198  89.850  132.996 1.00 27.19  ? 1727 PHE A C     1 
ATOM   2215  O  O     . PHE A 1 1727 ? 37.980  91.026  133.308 1.00 30.72  ? 1727 PHE A O     1 
ATOM   2216  C  CB    . PHE A 1 1727 ? 40.050  88.578  134.113 1.00 22.72  ? 1727 PHE A CB    1 
ATOM   2217  C  CG    . PHE A 1 1727 ? 40.483  87.724  135.263 1.00 22.54  ? 1727 PHE A CG    1 
ATOM   2218  C  CD1   . PHE A 1 1727 ? 39.850  87.821  136.491 1.00 19.38  ? 1727 PHE A CD1   1 
ATOM   2219  C  CD2   . PHE A 1 1727 ? 41.514  86.816  135.115 1.00 18.76  ? 1727 PHE A CD2   1 
ATOM   2220  C  CE1   . PHE A 1 1727 ? 40.245  87.033  137.552 1.00 20.93  ? 1727 PHE A CE1   1 
ATOM   2221  C  CE2   . PHE A 1 1727 ? 41.911  86.027  136.170 1.00 17.02  ? 1727 PHE A CE2   1 
ATOM   2222  C  CZ    . PHE A 1 1727 ? 41.278  86.134  137.391 1.00 22.88  ? 1727 PHE A CZ    1 
ATOM   2223  N  N     . GLY A 1 1728 ? 38.153  89.433  131.734 1.00 28.34  ? 1728 GLY A N     1 
ATOM   2224  C  CA    . GLY A 1 1728 ? 37.687  90.315  130.690 1.00 24.73  ? 1728 GLY A CA    1 
ATOM   2225  C  C     . GLY A 1 1728 ? 36.212  90.628  130.837 1.00 32.95  ? 1728 GLY A C     1 
ATOM   2226  O  O     . GLY A 1 1728 ? 35.464  89.922  131.516 1.00 33.57  ? 1728 GLY A O     1 
ATOM   2227  N  N     . LYS A 1 1729 ? 35.801  91.716  130.179 1.00 35.88  ? 1729 LYS A N     1 
ATOM   2228  C  CA    . LYS A 1 1729 ? 34.439  92.263  130.260 1.00 47.83  ? 1729 LYS A CA    1 
ATOM   2229  C  C     . LYS A 1 1729 ? 33.893  92.206  131.687 1.00 48.83  ? 1729 LYS A C     1 
ATOM   2230  O  O     . LYS A 1 1729 ? 32.754  91.798  131.929 1.00 48.07  ? 1729 LYS A O     1 
ATOM   2231  C  CB    . LYS A 1 1729 ? 33.489  91.578  129.265 1.00 48.28  ? 1729 LYS A CB    1 
ATOM   2232  C  CG    . LYS A 1 1729 ? 33.367  90.060  129.354 1.00 44.65  ? 1729 LYS A CG    1 
ATOM   2233  C  CD    . LYS A 1 1729 ? 32.415  89.517  128.301 1.00 45.19  ? 1729 LYS A CD    1 
ATOM   2234  C  CE    . LYS A 1 1729 ? 32.850  89.928  126.904 1.00 45.84  ? 1729 LYS A CE    1 
ATOM   2235  N  NZ    . LYS A 1 1729 ? 31.870  89.509  125.865 1.00 50.88  ? 1729 LYS A NZ    1 
ATOM   2236  N  N     . ALA A 1 1730 ? 34.720  92.627  132.642 1.00 46.56  ? 1730 ALA A N     1 
ATOM   2237  C  CA    . ALA A 1 1730 ? 34.348  92.697  134.049 1.00 44.35  ? 1730 ALA A CA    1 
ATOM   2238  C  C     . ALA A 1 1730 ? 34.709  94.075  134.580 1.00 51.05  ? 1730 ALA A C     1 
ATOM   2239  O  O     . ALA A 1 1730 ? 35.782  94.602  134.266 1.00 52.96  ? 1730 ALA A O     1 
ATOM   2240  C  CB    . ALA A 1 1730 ? 35.048  91.608  134.867 1.00 30.78  ? 1730 ALA A CB    1 
ATOM   2241  N  N     . THR A 1 1731 ? 33.813  94.656  135.380 1.00 48.51  ? 1731 THR A N     1 
ATOM   2242  C  CA    . THR A 1 1731 ? 34.014  96.024  135.851 1.00 47.74  ? 1731 THR A CA    1 
ATOM   2243  C  C     . THR A 1 1731 ? 35.206  96.119  136.797 1.00 44.40  ? 1731 THR A C     1 
ATOM   2244  O  O     . THR A 1 1731 ? 36.071  96.988  136.639 1.00 44.44  ? 1731 THR A O     1 
ATOM   2245  C  CB    . THR A 1 1731 ? 32.744  96.534  136.533 1.00 50.67  ? 1731 THR A CB    1 
ATOM   2246  O  OG1   . THR A 1 1731 ? 32.420  95.685  137.641 1.00 55.39  ? 1731 THR A OG1   1 
ATOM   2247  C  CG2   . THR A 1 1731 ? 31.582  96.545  135.552 1.00 47.95  ? 1731 THR A CG2   1 
ATOM   2248  N  N     . SER A 1 1732 ? 35.269  95.233  137.786 1.00 45.32  ? 1732 SER A N     1 
ATOM   2249  C  CA    . SER A 1 1732 ? 36.325  95.255  138.787 1.00 43.05  ? 1732 SER A CA    1 
ATOM   2250  C  C     . SER A 1 1732 ? 37.011  93.898  138.854 1.00 40.68  ? 1732 SER A C     1 
ATOM   2251  O  O     . SER A 1 1732 ? 36.375  92.852  138.695 1.00 48.51  ? 1732 SER A O     1 
ATOM   2252  C  CB    . SER A 1 1732 ? 35.773  95.628  140.169 1.00 42.47  ? 1732 SER A CB    1 
ATOM   2253  O  OG    . SER A 1 1732 ? 34.752  94.731  140.569 1.00 48.82  ? 1732 SER A OG    1 
ATOM   2254  N  N     . ILE A 1 1733 ? 38.319  93.925  139.095 1.00 32.21  ? 1733 ILE A N     1 
ATOM   2255  C  CA    . ILE A 1 1733 ? 39.135  92.721  139.187 1.00 32.50  ? 1733 ILE A CA    1 
ATOM   2256  C  C     . ILE A 1 1733 ? 39.716  92.655  140.592 1.00 31.87  ? 1733 ILE A C     1 
ATOM   2257  O  O     . ILE A 1 1733 ? 40.406  93.584  141.030 1.00 36.65  ? 1733 ILE A O     1 
ATOM   2258  C  CB    . ILE A 1 1733 ? 40.247  92.695  138.131 1.00 35.36  ? 1733 ILE A CB    1 
ATOM   2259  C  CG1   . ILE A 1 1733 ? 39.644  92.707  136.725 1.00 28.43  ? 1733 ILE A CG1   1 
ATOM   2260  C  CG2   . ILE A 1 1733 ? 41.147  91.483  138.334 1.00 28.05  ? 1733 ILE A CG2   1 
ATOM   2261  C  CD1   . ILE A 1 1733 ? 40.621  92.337  135.638 1.00 19.01  ? 1733 ILE A CD1   1 
ATOM   2262  N  N     . ASP A 1 1734 ? 39.436  91.567  141.296 1.00 31.31  ? 1734 ASP A N     1 
ATOM   2263  C  CA    . ASP A 1 1734 ? 40.044  91.352  142.600 1.00 30.77  ? 1734 ASP A CA    1 
ATOM   2264  C  C     . ASP A 1 1734 ? 41.511  90.976  142.417 1.00 29.65  ? 1734 ASP A C     1 
ATOM   2265  O  O     . ASP A 1 1734 ? 41.816  90.049  141.653 1.00 27.67  ? 1734 ASP A O     1 
ATOM   2266  C  CB    . ASP A 1 1734 ? 39.306  90.255  143.365 1.00 34.48  ? 1734 ASP A CB    1 
ATOM   2267  C  CG    . ASP A 1 1734 ? 40.083  89.761  144.569 1.00 38.51  ? 1734 ASP A CG    1 
ATOM   2268  O  OD1   . ASP A 1 1734 ? 40.422  90.588  145.441 1.00 42.23  ? 1734 ASP A OD1   1 
ATOM   2269  O  OD2   . ASP A 1 1734 ? 40.354  88.544  144.644 1.00 35.77  ? 1734 ASP A OD2   1 
ATOM   2270  N  N     . PRO A 1 1735 ? 42.443  91.673  143.073 1.00 29.49  ? 1735 PRO A N     1 
ATOM   2271  C  CA    . PRO A 1 1735 ? 43.866  91.351  142.871 1.00 31.44  ? 1735 PRO A CA    1 
ATOM   2272  C  C     . PRO A 1 1735 ? 44.227  89.916  143.220 1.00 27.68  ? 1735 PRO A C     1 
ATOM   2273  O  O     . PRO A 1 1735 ? 45.061  89.316  142.534 1.00 22.82  ? 1735 PRO A O     1 
ATOM   2274  C  CB    . PRO A 1 1735 ? 44.579  92.357  143.786 1.00 29.49  ? 1735 PRO A CB    1 
ATOM   2275  C  CG    . PRO A 1 1735 ? 43.617  93.491  143.917 1.00 29.00  ? 1735 PRO A CG    1 
ATOM   2276  C  CD    . PRO A 1 1735 ? 42.258  92.857  143.928 1.00 33.12  ? 1735 PRO A CD    1 
ATOM   2277  N  N     . ASN A 1 1736 ? 43.618  89.343  144.260 1.00 27.08  ? 1736 ASN A N     1 
ATOM   2278  C  CA    . ASN A 1 1736 ? 43.985  87.994  144.683 1.00 29.63  ? 1736 ASN A CA    1 
ATOM   2279  C  C     . ASN A 1 1736 ? 43.695  86.975  143.585 1.00 26.65  ? 1736 ASN A C     1 
ATOM   2280  O  O     . ASN A 1 1736 ? 44.556  86.158  143.235 1.00 24.20  ? 1736 ASN A O     1 
ATOM   2281  C  CB    . ASN A 1 1736 ? 43.239  87.635  145.970 1.00 31.82  ? 1736 ASN A CB    1 
ATOM   2282  C  CG    . ASN A 1 1736 ? 43.725  86.337  146.593 1.00 37.80  ? 1736 ASN A CG    1 
ATOM   2283  O  OD1   . ASN A 1 1736 ? 44.611  85.667  146.062 1.00 42.64  ? 1736 ASN A OD1   1 
ATOM   2284  N  ND2   . ASN A 1 1736 ? 43.141  85.976  147.729 1.00 42.73  ? 1736 ASN A ND2   1 
ATOM   2285  N  N     . THR A 1 1737 ? 42.484  87.018  143.024 1.00 21.85  ? 1737 THR A N     1 
ATOM   2286  C  CA    . THR A 1 1737 ? 42.115  86.078  141.970 1.00 24.10  ? 1737 THR A CA    1 
ATOM   2287  C  C     . THR A 1 1737 ? 42.989  86.268  140.737 1.00 21.45  ? 1737 THR A C     1 
ATOM   2288  O  O     . THR A 1 1737 ? 43.438  85.293  140.121 1.00 20.35  ? 1737 THR A O     1 
ATOM   2289  C  CB    . THR A 1 1737 ? 40.636  86.247  141.617 1.00 24.76  ? 1737 THR A CB    1 
ATOM   2290  O  OG1   . THR A 1 1737 ? 39.848  86.190  142.812 1.00 32.72  ? 1737 THR A OG1   1 
ATOM   2291  C  CG2   . THR A 1 1737 ? 40.183  85.147  140.672 1.00 24.22  ? 1737 THR A CG2   1 
ATOM   2292  N  N     . TYR A 1 1738 ? 43.249  87.524  140.369 1.00 18.53  ? 1738 TYR A N     1 
ATOM   2293  C  CA    . TYR A 1 1738 ? 44.088  87.809  139.209 1.00 14.45  ? 1738 TYR A CA    1 
ATOM   2294  C  C     . TYR A 1 1738 ? 45.492  87.244  139.385 1.00 14.93  ? 1738 TYR A C     1 
ATOM   2295  O  O     . TYR A 1 1738 ? 46.030  86.591  138.483 1.00 14.12  ? 1738 TYR A O     1 
ATOM   2296  C  CB    . TYR A 1 1738 ? 44.148  89.317  138.973 1.00 16.79  ? 1738 TYR A CB    1 
ATOM   2297  C  CG    . TYR A 1 1738 ? 44.668  89.694  137.609 1.00 13.62  ? 1738 TYR A CG    1 
ATOM   2298  C  CD1   . TYR A 1 1738 ? 44.332  88.951  136.490 1.00 14.79  ? 1738 TYR A CD1   1 
ATOM   2299  C  CD2   . TYR A 1 1738 ? 45.519  90.778  137.446 1.00 16.00  ? 1738 TYR A CD2   1 
ATOM   2300  C  CE1   . TYR A 1 1738 ? 44.812  89.287  135.246 1.00 13.33  ? 1738 TYR A CE1   1 
ATOM   2301  C  CE2   . TYR A 1 1738 ? 46.005  91.120  136.201 1.00 13.87  ? 1738 TYR A CE2   1 
ATOM   2302  C  CZ    . TYR A 1 1738 ? 45.648  90.369  135.104 1.00 14.89  ? 1738 TYR A CZ    1 
ATOM   2303  O  OH    . TYR A 1 1738 ? 46.127  90.697  133.857 1.00 15.82  ? 1738 TYR A OH    1 
ATOM   2304  N  N     . ILE A 1 1739 ? 46.104  87.489  140.545 1.00 17.84  ? 1739 ILE A N     1 
ATOM   2305  C  CA    . ILE A 1 1739 ? 47.478  87.046  140.763 1.00 14.66  ? 1739 ILE A CA    1 
ATOM   2306  C  C     . ILE A 1 1739 ? 47.539  85.528  140.852 1.00 13.98  ? 1739 ILE A C     1 
ATOM   2307  O  O     . ILE A 1 1739 ? 48.489  84.901  140.367 1.00 15.68  ? 1739 ILE A O     1 
ATOM   2308  C  CB    . ILE A 1 1739 ? 48.068  87.725  142.013 1.00 16.94  ? 1739 ILE A CB    1 
ATOM   2309  C  CG1   . ILE A 1 1739 ? 48.006  89.245  141.849 1.00 20.11  ? 1739 ILE A CG1   1 
ATOM   2310  C  CG2   . ILE A 1 1739 ? 49.493  87.264  142.259 1.00 12.66  ? 1739 ILE A CG2   1 
ATOM   2311  C  CD1   . ILE A 1 1739 ? 48.750  89.763  140.649 1.00 19.73  ? 1739 ILE A CD1   1 
ATOM   2312  N  N     . THR A 1 1740 ? 46.522  84.910  141.458 1.00 14.08  ? 1740 THR A N     1 
ATOM   2313  C  CA    . THR A 1 1740 ? 46.452  83.453  141.463 1.00 15.27  ? 1740 THR A CA    1 
ATOM   2314  C  C     . THR A 1 1740 ? 46.361  82.908  140.043 1.00 14.40  ? 1740 THR A C     1 
ATOM   2315  O  O     . THR A 1 1740 ? 46.989  81.894  139.717 1.00 13.18  ? 1740 THR A O     1 
ATOM   2316  C  CB    . THR A 1 1740 ? 45.257  82.987  142.296 1.00 18.37  ? 1740 THR A CB    1 
ATOM   2317  O  OG1   . THR A 1 1740 ? 45.296  83.617  143.583 1.00 21.12  ? 1740 THR A OG1   1 
ATOM   2318  C  CG2   . THR A 1 1740 ? 45.286  81.478  142.477 1.00 17.78  ? 1740 THR A CG2   1 
ATOM   2319  N  N     . TRP A 1 1741 ? 45.587  83.574  139.182 1.00 15.56  ? 1741 TRP A N     1 
ATOM   2320  C  CA    . TRP A 1 1741 ? 45.470  83.130  137.797 1.00 9.72   ? 1741 TRP A CA    1 
ATOM   2321  C  C     . TRP A 1 1741 ? 46.802  83.249  137.069 1.00 8.76   ? 1741 TRP A C     1 
ATOM   2322  O  O     . TRP A 1 1741 ? 47.190  82.353  136.310 1.00 14.41  ? 1741 TRP A O     1 
ATOM   2323  C  CB    . TRP A 1 1741 ? 44.391  83.935  137.076 1.00 8.48   ? 1741 TRP A CB    1 
ATOM   2324  C  CG    . TRP A 1 1741 ? 44.469  83.827  135.583 1.00 9.87   ? 1741 TRP A CG    1 
ATOM   2325  C  CD1   . TRP A 1 1741 ? 43.976  82.819  134.827 1.00 9.25   ? 1741 TRP A CD1   1 
ATOM   2326  C  CD2   . TRP A 1 1741 ? 45.050  84.766  134.667 1.00 9.14   ? 1741 TRP A CD2   1 
ATOM   2327  N  NE1   . TRP A 1 1741 ? 44.221  83.050  133.497 1.00 7.58   ? 1741 TRP A NE1   1 
ATOM   2328  C  CE2   . TRP A 1 1741 ? 44.879  84.244  133.371 1.00 8.81   ? 1741 TRP A CE2   1 
ATOM   2329  C  CE3   . TRP A 1 1741 ? 45.699  85.993  134.817 1.00 7.46   ? 1741 TRP A CE3   1 
ATOM   2330  C  CZ2   . TRP A 1 1741 ? 45.335  84.903  132.232 1.00 9.20   ? 1741 TRP A CZ2   1 
ATOM   2331  C  CZ3   . TRP A 1 1741 ? 46.156  86.645  133.685 1.00 7.16   ? 1741 TRP A CZ3   1 
ATOM   2332  C  CH2   . TRP A 1 1741 ? 45.967  86.101  132.410 1.00 6.85   ? 1741 TRP A CH2   1 
ATOM   2333  N  N     . ILE A 1 1742 ? 47.517  84.358  137.282 1.00 7.37   ? 1742 ILE A N     1 
ATOM   2334  C  CA    . ILE A 1 1742 ? 48.821  84.519  136.640 1.00 10.43  ? 1742 ILE A CA    1 
ATOM   2335  C  C     . ILE A 1 1742 ? 49.794  83.456  137.134 1.00 11.78  ? 1742 ILE A C     1 
ATOM   2336  O  O     . ILE A 1 1742 ? 50.608  82.932  136.364 1.00 12.91  ? 1742 ILE A O     1 
ATOM   2337  C  CB    . ILE A 1 1742 ? 49.382  85.937  136.860 1.00 10.78  ? 1742 ILE A CB    1 
ATOM   2338  C  CG1   . ILE A 1 1742 ? 48.326  87.000  136.572 1.00 12.14  ? 1742 ILE A CG1   1 
ATOM   2339  C  CG2   . ILE A 1 1742 ? 50.574  86.164  135.955 1.00 9.33   ? 1742 ILE A CG2   1 
ATOM   2340  C  CD1   . ILE A 1 1742 ? 48.705  88.392  137.019 1.00 12.88  ? 1742 ILE A CD1   1 
ATOM   2341  N  N     . ASP A 1 1743 ? 49.731  83.122  138.425 1.00 12.89  ? 1743 ASP A N     1 
ATOM   2342  C  CA    . ASP A 1 1743 ? 50.631  82.111  138.971 1.00 13.20  ? 1743 ASP A CA    1 
ATOM   2343  C  C     . ASP A 1 1743 ? 50.290  80.714  138.467 1.00 13.15  ? 1743 ASP A C     1 
ATOM   2344  O  O     . ASP A 1 1743 ? 51.187  79.877  138.317 1.00 14.15  ? 1743 ASP A O     1 
ATOM   2345  C  CB    . ASP A 1 1743 ? 50.591  82.138  140.498 1.00 14.38  ? 1743 ASP A CB    1 
ATOM   2346  C  CG    . ASP A 1 1743 ? 51.215  83.389  141.076 1.00 18.70  ? 1743 ASP A CG    1 
ATOM   2347  O  OD1   . ASP A 1 1743 ? 52.132  83.947  140.437 1.00 20.14  ? 1743 ASP A OD1   1 
ATOM   2348  O  OD2   . ASP A 1 1743 ? 50.788  83.815  142.169 1.00 21.25  ? 1743 ASP A OD2   1 
ATOM   2349  N  N     . LYS A 1 1744 ? 49.009  80.443  138.208 1.00 8.51   ? 1744 LYS A N     1 
ATOM   2350  C  CA    . LYS A 1 1744 ? 48.595  79.092  137.842 1.00 8.82   ? 1744 LYS A CA    1 
ATOM   2351  C  C     . LYS A 1 1744 ? 49.132  78.684  136.474 1.00 11.23  ? 1744 LYS A C     1 
ATOM   2352  O  O     . LYS A 1 1744 ? 49.518  77.527  136.275 1.00 14.81  ? 1744 LYS A O     1 
ATOM   2353  C  CB    . LYS A 1 1744 ? 47.071  78.989  137.873 1.00 11.12  ? 1744 LYS A CB    1 
ATOM   2354  C  CG    . LYS A 1 1744 ? 46.537  77.580  137.677 1.00 11.01  ? 1744 LYS A CG    1 
ATOM   2355  C  CD    . LYS A 1 1744 ? 45.019  77.563  137.680 1.00 11.62  ? 1744 LYS A CD    1 
ATOM   2356  C  CE    . LYS A 1 1744 ? 44.481  76.222  138.144 1.00 19.64  ? 1744 LYS A CE    1 
ATOM   2357  N  NZ    . LYS A 1 1744 ? 44.923  75.112  137.256 1.00 19.48  ? 1744 LYS A NZ    1 
ATOM   2358  N  N     . TYR A 1 1745 ? 49.168  79.610  135.522 1.00 11.88  ? 1745 TYR A N     1 
ATOM   2359  C  CA    . TYR A 1 1745 ? 49.519  79.290  134.147 1.00 7.94   ? 1745 TYR A CA    1 
ATOM   2360  C  C     . TYR A 1 1745 ? 50.841  79.930  133.748 1.00 7.00   ? 1745 TYR A C     1 
ATOM   2361  O  O     . TYR A 1 1745 ? 51.344  80.847  134.401 1.00 8.50   ? 1745 TYR A O     1 
ATOM   2362  C  CB    . TYR A 1 1745 ? 48.405  79.719  133.188 1.00 5.47   ? 1745 TYR A CB    1 
ATOM   2363  C  CG    . TYR A 1 1745 ? 47.165  78.874  133.336 1.00 6.49   ? 1745 TYR A CG    1 
ATOM   2364  C  CD1   . TYR A 1 1745 ? 47.026  77.687  132.630 1.00 6.87   ? 1745 TYR A CD1   1 
ATOM   2365  C  CD2   . TYR A 1 1745 ? 46.154  79.237  134.209 1.00 7.67   ? 1745 TYR A CD2   1 
ATOM   2366  C  CE1   . TYR A 1 1745 ? 45.903  76.901  132.771 1.00 9.00   ? 1745 TYR A CE1   1 
ATOM   2367  C  CE2   . TYR A 1 1745 ? 45.031  78.454  134.360 1.00 8.43   ? 1745 TYR A CE2   1 
ATOM   2368  C  CZ    . TYR A 1 1745 ? 44.907  77.291  133.638 1.00 11.13  ? 1745 TYR A CZ    1 
ATOM   2369  O  OH    . TYR A 1 1745 ? 43.783  76.515  133.790 1.00 14.40  ? 1745 TYR A OH    1 
ATOM   2370  N  N     . GLN A 1 1746 ? 51.398  79.416  132.656 1.00 5.71   ? 1746 GLN A N     1 
ATOM   2371  C  CA    . GLN A 1 1746 ? 52.715  79.831  132.201 1.00 5.03   ? 1746 GLN A CA    1 
ATOM   2372  C  C     . GLN A 1 1746 ? 52.668  81.236  131.612 1.00 6.05   ? 1746 GLN A C     1 
ATOM   2373  O  O     . GLN A 1 1746 ? 51.631  81.698  131.127 1.00 8.78   ? 1746 GLN A O     1 
ATOM   2374  C  CB    . GLN A 1 1746 ? 53.252  78.837  131.171 1.00 6.57   ? 1746 GLN A CB    1 
ATOM   2375  C  CG    . GLN A 1 1746 ? 53.757  77.535  131.782 1.00 6.59   ? 1746 GLN A CG    1 
ATOM   2376  C  CD    . GLN A 1 1746 ? 52.632  76.603  132.203 1.00 7.90   ? 1746 GLN A CD    1 
ATOM   2377  O  OE1   . GLN A 1 1746 ? 51.456  76.894  131.991 1.00 7.31   ? 1746 GLN A OE1   1 
ATOM   2378  N  NE2   . GLN A 1 1746 ? 52.989  75.484  132.819 1.00 7.07   ? 1746 GLN A NE2   1 
ATOM   2379  N  N     . ALA A 1 1747 ? 53.816  81.916  131.663 1.00 5.25   ? 1747 ALA A N     1 
ATOM   2380  C  CA    . ALA A 1 1747 ? 53.902  83.301  131.207 1.00 7.59   ? 1747 ALA A CA    1 
ATOM   2381  C  C     . ALA A 1 1747 ? 53.466  83.436  129.754 1.00 5.94   ? 1747 ALA A C     1 
ATOM   2382  O  O     . ALA A 1 1747 ? 52.678  84.326  129.403 1.00 6.44   ? 1747 ALA A O     1 
ATOM   2383  C  CB    . ALA A 1 1747 ? 55.330  83.810  131.392 1.00 6.64   ? 1747 ALA A CB    1 
ATOM   2384  N  N     . GLN A 1 1748 ? 53.986  82.558  128.892 1.00 5.75   ? 1748 GLN A N     1 
ATOM   2385  C  CA    . GLN A 1 1748 ? 53.514  82.475  127.515 1.00 4.49   ? 1748 GLN A CA    1 
ATOM   2386  C  C     . GLN A 1 1748 ? 51.998  82.350  127.463 1.00 4.00   ? 1748 GLN A C     1 
ATOM   2387  O  O     . GLN A 1 1748 ? 51.324  83.112  126.756 1.00 3.74   ? 1748 GLN A O     1 
ATOM   2388  C  CB    . GLN A 1 1748 ? 54.173  81.277  126.830 1.00 4.89   ? 1748 GLN A CB    1 
ATOM   2389  C  CG    . GLN A 1 1748 ? 53.822  81.082  125.371 1.00 6.14   ? 1748 GLN A CG    1 
ATOM   2390  C  CD    . GLN A 1 1748 ? 54.553  79.897  124.760 1.00 6.67   ? 1748 GLN A CD    1 
ATOM   2391  O  OE1   . GLN A 1 1748 ? 55.308  79.203  125.440 1.00 3.90   ? 1748 GLN A OE1   1 
ATOM   2392  N  NE2   . GLN A 1 1748 ? 54.321  79.655  123.476 1.00 5.97   ? 1748 GLN A NE2   1 
ATOM   2393  N  N     . LEU A 1 1749 ? 51.446  81.411  128.232 1.00 4.33   ? 1749 LEU A N     1 
ATOM   2394  C  CA    . LEU A 1 1749 ? 50.008  81.173  128.217 1.00 3.47   ? 1749 LEU A CA    1 
ATOM   2395  C  C     . LEU A 1 1749 ? 49.245  82.360  128.786 1.00 3.76   ? 1749 LEU A C     1 
ATOM   2396  O  O     . LEU A 1 1749 ? 48.164  82.698  128.296 1.00 3.24   ? 1749 LEU A O     1 
ATOM   2397  C  CB    . LEU A 1 1749 ? 49.690  79.904  129.003 1.00 5.23   ? 1749 LEU A CB    1 
ATOM   2398  C  CG    . LEU A 1 1749 ? 50.514  78.678  128.613 1.00 6.88   ? 1749 LEU A CG    1 
ATOM   2399  C  CD1   . LEU A 1 1749 ? 49.937  77.439  129.249 1.00 5.48   ? 1749 LEU A CD1   1 
ATOM   2400  C  CD2   . LEU A 1 1749 ? 50.581  78.517  127.106 1.00 6.57   ? 1749 LEU A CD2   1 
ATOM   2401  N  N     . VAL A 1 1750 ? 49.790  83.003  129.821 1.00 3.84   ? 1750 VAL A N     1 
ATOM   2402  C  CA    . VAL A 1 1750 ? 49.114  84.141  130.440 1.00 4.40   ? 1750 VAL A CA    1 
ATOM   2403  C  C     . VAL A 1 1750 ? 48.995  85.294  129.448 1.00 4.16   ? 1750 VAL A C     1 
ATOM   2404  O  O     . VAL A 1 1750 ? 47.914  85.872  129.259 1.00 5.05   ? 1750 VAL A O     1 
ATOM   2405  C  CB    . VAL A 1 1750 ? 49.858  84.563  131.720 1.00 6.23   ? 1750 VAL A CB    1 
ATOM   2406  C  CG1   . VAL A 1 1750 ? 49.422  85.938  132.166 1.00 8.43   ? 1750 VAL A CG1   1 
ATOM   2407  C  CG2   . VAL A 1 1750 ? 49.624  83.548  132.828 1.00 5.28   ? 1750 VAL A CG2   1 
ATOM   2408  N  N     . VAL A 1 1751 ? 50.105  85.636  128.789 1.00 3.58   ? 1751 VAL A N     1 
ATOM   2409  C  CA    . VAL A 1 1751 ? 50.074  86.724  127.817 1.00 3.69   ? 1751 VAL A CA    1 
ATOM   2410  C  C     . VAL A 1 1751 ? 49.178  86.365  126.637 1.00 2.73   ? 1751 VAL A C     1 
ATOM   2411  O  O     . VAL A 1 1751 ? 48.408  87.202  126.148 1.00 2.95   ? 1751 VAL A O     1 
ATOM   2412  C  CB    . VAL A 1 1751 ? 51.502  87.080  127.365 1.00 3.79   ? 1751 VAL A CB    1 
ATOM   2413  C  CG1   . VAL A 1 1751 ? 51.468  88.035  126.180 1.00 3.68   ? 1751 VAL A CG1   1 
ATOM   2414  C  CG2   . VAL A 1 1751 ? 52.277  87.696  128.517 1.00 3.84   ? 1751 VAL A CG2   1 
ATOM   2415  N  N     . LEU A 1 1752 ? 49.253  85.116  126.169 1.00 2.02   ? 1752 LEU A N     1 
ATOM   2416  C  CA    . LEU A 1 1752 ? 48.412  84.692  125.056 1.00 2.27   ? 1752 LEU A CA    1 
ATOM   2417  C  C     . LEU A 1 1752 ? 46.932  84.790  125.411 1.00 2.17   ? 1752 LEU A C     1 
ATOM   2418  O  O     . LEU A 1 1752 ? 46.121  85.251  124.600 1.00 1.71   ? 1752 LEU A O     1 
ATOM   2419  C  CB    . LEU A 1 1752 ? 48.783  83.267  124.650 1.00 1.79   ? 1752 LEU A CB    1 
ATOM   2420  C  CG    . LEU A 1 1752 ? 48.267  82.728  123.320 1.00 2.17   ? 1752 LEU A CG    1 
ATOM   2421  C  CD1   . LEU A 1 1752 ? 48.534  83.717  122.200 1.00 1.84   ? 1752 LEU A CD1   1 
ATOM   2422  C  CD2   . LEU A 1 1752 ? 48.940  81.398  123.030 1.00 1.90   ? 1752 LEU A CD2   1 
ATOM   2423  N  N     . SER A 1 1753 ? 46.565  84.366  126.623 1.00 2.70   ? 1753 SER A N     1 
ATOM   2424  C  CA    . SER A 1 1753 ? 45.174  84.437  127.056 1.00 3.35   ? 1753 SER A CA    1 
ATOM   2425  C  C     . SER A 1 1753 ? 44.699  85.879  127.164 1.00 2.51   ? 1753 SER A C     1 
ATOM   2426  O  O     . SER A 1 1753 ? 43.560  86.192  126.798 1.00 2.49   ? 1753 SER A O     1 
ATOM   2427  C  CB    . SER A 1 1753 ? 45.006  83.717  128.395 1.00 3.17   ? 1753 SER A CB    1 
ATOM   2428  O  OG    . SER A 1 1753 ? 45.280  82.334  128.268 1.00 6.54   ? 1753 SER A OG    1 
ATOM   2429  N  N     . ALA A 1 1754 ? 45.549  86.770  127.681 1.00 2.41   ? 1754 ALA A N     1 
ATOM   2430  C  CA    . ALA A 1 1754 ? 45.169  88.179  127.740 1.00 3.16   ? 1754 ALA A CA    1 
ATOM   2431  C  C     . ALA A 1 1754 ? 44.936  88.744  126.342 1.00 2.19   ? 1754 ALA A C     1 
ATOM   2432  O  O     . ALA A 1 1754 ? 43.946  89.453  126.105 1.00 2.35   ? 1754 ALA A O     1 
ATOM   2433  C  CB    . ALA A 1 1754 ? 46.237  88.985  128.478 1.00 2.75   ? 1754 ALA A CB    1 
ATOM   2434  N  N     . GLN A 1 1755 ? 45.832  88.425  125.400 1.00 2.37   ? 1755 GLN A N     1 
ATOM   2435  C  CA    . GLN A 1 1755 ? 45.664  88.901  124.030 1.00 2.10   ? 1755 GLN A CA    1 
ATOM   2436  C  C     . GLN A 1 1755 ? 44.370  88.380  123.422 1.00 2.29   ? 1755 GLN A C     1 
ATOM   2437  O  O     . GLN A 1 1755 ? 43.618  89.140  122.797 1.00 4.05   ? 1755 GLN A O     1 
ATOM   2438  C  CB    . GLN A 1 1755 ? 46.856  88.487  123.168 1.00 1.73   ? 1755 GLN A CB    1 
ATOM   2439  C  CG    . GLN A 1 1755 ? 48.188  89.032  123.637 1.00 3.12   ? 1755 GLN A CG    1 
ATOM   2440  C  CD    . GLN A 1 1755 ? 49.347  88.551  122.789 1.00 3.01   ? 1755 GLN A CD    1 
ATOM   2441  O  OE1   . GLN A 1 1755 ? 49.597  87.351  122.680 1.00 2.84   ? 1755 GLN A OE1   1 
ATOM   2442  N  NE2   . GLN A 1 1755 ? 50.060  89.489  122.179 1.00 3.35   ? 1755 GLN A NE2   1 
ATOM   2443  N  N     . ILE A 1 1756 ? 44.083  87.090  123.612 1.00 1.77   ? 1756 ILE A N     1 
ATOM   2444  C  CA    . ILE A 1 1756 ? 42.828  86.527  123.121 1.00 2.56   ? 1756 ILE A CA    1 
ATOM   2445  C  C     . ILE A 1 1756 ? 41.648  87.294  123.701 1.00 3.05   ? 1756 ILE A C     1 
ATOM   2446  O  O     . ILE A 1 1756 ? 40.895  87.944  122.967 1.00 6.99   ? 1756 ILE A O     1 
ATOM   2447  C  CB    . ILE A 1 1756 ? 42.741  85.024  123.439 1.00 3.89   ? 1756 ILE A CB    1 
ATOM   2448  C  CG1   . ILE A 1 1756 ? 43.875  84.269  122.743 1.00 2.99   ? 1756 ILE A CG1   1 
ATOM   2449  C  CG2   . ILE A 1 1756 ? 41.389  84.468  123.026 1.00 5.31   ? 1756 ILE A CG2   1 
ATOM   2450  C  CD1   . ILE A 1 1756 ? 44.003  82.824  123.163 1.00 2.60   ? 1756 ILE A CD1   1 
ATOM   2451  N  N     . ALA A 1 1757 ? 41.536  87.310  125.034 1.00 3.58   ? 1757 ALA A N     1 
ATOM   2452  C  CA    . ALA A 1 1757 ? 40.393  87.930  125.697 1.00 5.12   ? 1757 ALA A CA    1 
ATOM   2453  C  C     . ALA A 1 1757 ? 40.153  89.348  125.195 1.00 5.14   ? 1757 ALA A C     1 
ATOM   2454  O  O     . ALA A 1 1757 ? 39.018  89.722  124.870 1.00 4.37   ? 1757 ALA A O     1 
ATOM   2455  C  CB    . ALA A 1 1757 ? 40.605  87.922  127.213 1.00 2.82   ? 1757 ALA A CB    1 
ATOM   2456  N  N     . TRP A 1 1758 ? 41.224  90.138  125.077 1.00 3.50   ? 1758 TRP A N     1 
ATOM   2457  C  CA    . TRP A 1 1758 ? 41.079  91.471  124.503 1.00 4.05   ? 1758 TRP A CA    1 
ATOM   2458  C  C     . TRP A 1 1758 ? 40.560  91.401  123.070 1.00 4.63   ? 1758 TRP A C     1 
ATOM   2459  O  O     . TRP A 1 1758 ? 39.723  92.221  122.666 1.00 4.92   ? 1758 TRP A O     1 
ATOM   2460  C  CB    . TRP A 1 1758 ? 42.412  92.216  124.562 1.00 4.26   ? 1758 TRP A CB    1 
ATOM   2461  C  CG    . TRP A 1 1758 ? 42.387  93.542  123.870 1.00 3.28   ? 1758 TRP A CG    1 
ATOM   2462  C  CD1   . TRP A 1 1758 ? 41.763  94.677  124.298 1.00 3.44   ? 1758 TRP A CD1   1 
ATOM   2463  C  CD2   . TRP A 1 1758 ? 43.008  93.872  122.623 1.00 2.67   ? 1758 TRP A CD2   1 
ATOM   2464  N  NE1   . TRP A 1 1758 ? 41.960  95.694  123.398 1.00 2.96   ? 1758 TRP A NE1   1 
ATOM   2465  C  CE2   . TRP A 1 1758 ? 42.720  95.225  122.359 1.00 2.72   ? 1758 TRP A CE2   1 
ATOM   2466  C  CE3   . TRP A 1 1758 ? 43.779  93.155  121.704 1.00 3.01   ? 1758 TRP A CE3   1 
ATOM   2467  C  CZ2   . TRP A 1 1758 ? 43.178  95.876  121.215 1.00 2.89   ? 1758 TRP A CZ2   1 
ATOM   2468  C  CZ3   . TRP A 1 1758 ? 44.232  93.802  120.570 1.00 4.20   ? 1758 TRP A CZ3   1 
ATOM   2469  C  CH2   . TRP A 1 1758 ? 43.930  95.148  120.335 1.00 3.17   ? 1758 TRP A CH2   1 
ATOM   2470  N  N     . SER A 1 1759 ? 41.032  90.420  122.293 1.00 3.74   ? 1759 SER A N     1 
ATOM   2471  C  CA    . SER A 1 1759 ? 40.610  90.316  120.899 1.00 3.40   ? 1759 SER A CA    1 
ATOM   2472  C  C     . SER A 1 1759 ? 39.109  90.067  120.781 1.00 5.12   ? 1759 SER A C     1 
ATOM   2473  O  O     . SER A 1 1759 ? 38.420  90.773  120.036 1.00 5.75   ? 1759 SER A O     1 
ATOM   2474  C  CB    . SER A 1 1759 ? 41.398  89.218  120.184 1.00 2.68   ? 1759 SER A CB    1 
ATOM   2475  O  OG    . SER A 1 1759 ? 42.669  89.687  119.775 1.00 4.78   ? 1759 SER A OG    1 
ATOM   2476  N  N     . GLU A 1 1760 ? 38.576  89.072  121.502 1.00 5.81   ? 1760 GLU A N     1 
ATOM   2477  C  CA    . GLU A 1 1760 ? 37.135  88.853  121.336 1.00 8.65   ? 1760 GLU A CA    1 
ATOM   2478  C  C     . GLU A 1 1760 ? 36.318  89.941  122.022 1.00 9.15   ? 1760 GLU A C     1 
ATOM   2479  O  O     . GLU A 1 1760 ? 35.179  90.187  121.615 1.00 10.48  ? 1760 GLU A O     1 
ATOM   2480  C  CB    . GLU A 1 1760 ? 36.605  87.483  121.802 1.00 15.41  ? 1760 GLU A CB    1 
ATOM   2481  C  CG    . GLU A 1 1760 ? 36.588  87.166  123.289 1.00 16.81  ? 1760 GLU A CG    1 
ATOM   2482  C  CD    . GLU A 1 1760 ? 37.876  86.600  123.776 1.00 27.96  ? 1760 GLU A CD    1 
ATOM   2483  O  OE1   . GLU A 1 1760 ? 38.857  86.719  123.041 1.00 29.24  ? 1760 GLU A OE1   1 
ATOM   2484  O  OE2   . GLU A 1 1760 ? 37.908  86.034  124.887 1.00 23.06  ? 1760 GLU A OE2   1 
ATOM   2485  N  N     . ASN A 1 1761 ? 36.864  90.625  123.035 1.00 7.46   ? 1761 ASN A N     1 
ATOM   2486  C  CA    . ASN A 1 1761 ? 36.145  91.786  123.558 1.00 7.04   ? 1761 ASN A CA    1 
ATOM   2487  C  C     . ASN A 1 1761 ? 35.986  92.858  122.486 1.00 6.86   ? 1761 ASN A C     1 
ATOM   2488  O  O     . ASN A 1 1761 ? 34.891  93.409  122.304 1.00 7.56   ? 1761 ASN A O     1 
ATOM   2489  C  CB    . ASN A 1 1761 ? 36.859  92.360  124.783 1.00 9.08   ? 1761 ASN A CB    1 
ATOM   2490  C  CG    . ASN A 1 1761 ? 36.827  91.426  125.976 1.00 14.05  ? 1761 ASN A CG    1 
ATOM   2491  O  OD1   . ASN A 1 1761 ? 37.375  91.738  127.033 1.00 16.19  ? 1761 ASN A OD1   1 
ATOM   2492  N  ND2   . ASN A 1 1761 ? 36.172  90.282  125.821 1.00 15.99  ? 1761 ASN A ND2   1 
ATOM   2493  N  N     . VAL A 1 1762 ? 37.062  93.148  121.752 1.00 5.21   ? 1762 VAL A N     1 
ATOM   2494  C  CA    . VAL A 1 1762 ? 36.983  94.153  120.696 1.00 5.87   ? 1762 VAL A CA    1 
ATOM   2495  C  C     . VAL A 1 1762 ? 36.066  93.680  119.574 1.00 9.46   ? 1762 VAL A C     1 
ATOM   2496  O  O     . VAL A 1 1762 ? 35.305  94.471  119.001 1.00 11.84  ? 1762 VAL A O     1 
ATOM   2497  C  CB    . VAL A 1 1762 ? 38.388  94.504  120.176 1.00 4.04   ? 1762 VAL A CB    1 
ATOM   2498  C  CG1   . VAL A 1 1762 ? 38.292  95.531  119.059 1.00 2.85   ? 1762 VAL A CG1   1 
ATOM   2499  C  CG2   . VAL A 1 1762 ? 39.251  95.029  121.307 1.00 3.19   ? 1762 VAL A CG2   1 
ATOM   2500  N  N     . GLU A 1 1763 ? 36.125  92.388  119.234 1.00 8.44   ? 1763 GLU A N     1 
ATOM   2501  C  CA    . GLU A 1 1763 ? 35.229  91.857  118.209 1.00 7.96   ? 1763 GLU A CA    1 
ATOM   2502  C  C     . GLU A 1 1763 ? 33.768  92.000  118.618 1.00 13.09  ? 1763 GLU A C     1 
ATOM   2503  O  O     . GLU A 1 1763 ? 32.924  92.384  117.800 1.00 18.31  ? 1763 GLU A O     1 
ATOM   2504  C  CB    . GLU A 1 1763 ? 35.557  90.392  117.911 1.00 12.60  ? 1763 GLU A CB    1 
ATOM   2505  C  CG    . GLU A 1 1763 ? 36.964  90.134  117.392 1.00 14.28  ? 1763 GLU A CG    1 
ATOM   2506  C  CD    . GLU A 1 1763 ? 37.189  90.658  115.983 1.00 17.68  ? 1763 GLU A CD    1 
ATOM   2507  O  OE1   . GLU A 1 1763 ? 36.221  91.124  115.346 1.00 18.70  ? 1763 GLU A OE1   1 
ATOM   2508  O  OE2   . GLU A 1 1763 ? 38.344  90.605  115.510 1.00 18.31  ? 1763 GLU A OE2   1 
ATOM   2509  N  N     . THR A 1 1764 ? 33.450  91.697  119.879 1.00 11.11  ? 1764 THR A N     1 
ATOM   2510  C  CA    . THR A 1 1764 ? 32.079  91.842  120.357 1.00 12.37  ? 1764 THR A CA    1 
ATOM   2511  C  C     . THR A 1 1764 ? 31.633  93.297  120.305 1.00 14.02  ? 1764 THR A C     1 
ATOM   2512  O  O     . THR A 1 1764 ? 30.514  93.601  119.874 1.00 18.58  ? 1764 THR A O     1 
ATOM   2513  C  CB    . THR A 1 1764 ? 31.960  91.291  121.778 1.00 12.99  ? 1764 THR A CB    1 
ATOM   2514  O  OG1   . THR A 1 1764 ? 32.418  89.934  121.805 1.00 15.92  ? 1764 THR A OG1   1 
ATOM   2515  C  CG2   . THR A 1 1764 ? 30.516  91.341  122.249 1.00 13.89  ? 1764 THR A CG2   1 
ATOM   2516  N  N     . ALA A 1 1765 ? 32.504  94.215  120.735 1.00 13.90  ? 1765 ALA A N     1 
ATOM   2517  C  CA    . ALA A 1 1765 ? 32.156  95.634  120.699 1.00 14.06  ? 1765 ALA A CA    1 
ATOM   2518  C  C     . ALA A 1 1765 ? 31.900  96.104  119.271 1.00 20.99  ? 1765 ALA A C     1 
ATOM   2519  O  O     . ALA A 1 1765 ? 30.918  96.808  119.000 1.00 27.87  ? 1765 ALA A O     1 
ATOM   2520  C  CB    . ALA A 1 1765 ? 33.265  96.459  121.351 1.00 12.69  ? 1765 ALA A CB    1 
ATOM   2521  N  N     . LEU A 1 1766 ? 32.771  95.714  118.338 1.00 15.40  ? 1766 LEU A N     1 
ATOM   2522  C  CA    . LEU A 1 1766 ? 32.618  96.153  116.955 1.00 19.07  ? 1766 LEU A CA    1 
ATOM   2523  C  C     . LEU A 1 1766 ? 31.380  95.543  116.311 1.00 24.88  ? 1766 LEU A C     1 
ATOM   2524  O  O     . LEU A 1 1766 ? 30.705  96.196  115.507 1.00 31.51  ? 1766 LEU A O     1 
ATOM   2525  C  CB    . LEU A 1 1766 ? 33.872  95.808  116.154 1.00 18.16  ? 1766 LEU A CB    1 
ATOM   2526  C  CG    . LEU A 1 1766 ? 35.118  96.598  116.555 1.00 16.83  ? 1766 LEU A CG    1 
ATOM   2527  C  CD1   . LEU A 1 1766 ? 36.327  96.125  115.776 1.00 8.72   ? 1766 LEU A CD1   1 
ATOM   2528  C  CD2   . LEU A 1 1766 ? 34.896  98.088  116.353 1.00 16.60  ? 1766 LEU A CD2   1 
ATOM   2529  N  N     . SER A 1 1767 ? 31.067  94.288  116.645 1.00 23.37  ? 1767 SER A N     1 
ATOM   2530  C  CA    . SER A 1 1767 ? 29.846  93.676  116.135 1.00 25.35  ? 1767 SER A CA    1 
ATOM   2531  C  C     . SER A 1 1767 ? 28.612  94.375  116.689 1.00 31.75  ? 1767 SER A C     1 
ATOM   2532  O  O     . SER A 1 1767 ? 27.612  94.541  115.982 1.00 38.91  ? 1767 SER A O     1 
ATOM   2533  C  CB    . SER A 1 1767 ? 29.824  92.187  116.476 1.00 21.95  ? 1767 SER A CB    1 
ATOM   2534  O  OG    . SER A 1 1767 ? 30.924  91.517  115.888 1.00 25.12  ? 1767 SER A OG    1 
ATOM   2535  N  N     . SER A 1 1768 ? 28.663  94.787  117.959 1.00 33.53  ? 1768 SER A N     1 
ATOM   2536  C  CA    . SER A 1 1768 ? 27.558  95.545  118.535 1.00 30.24  ? 1768 SER A CA    1 
ATOM   2537  C  C     . SER A 1 1768 ? 27.390  96.899  117.856 1.00 37.11  ? 1768 SER A C     1 
ATOM   2538  O  O     . SER A 1 1768 ? 26.258  97.350  117.651 1.00 51.08  ? 1768 SER A O     1 
ATOM   2539  C  CB    . SER A 1 1768 ? 27.774  95.728  120.037 1.00 30.25  ? 1768 SER A CB    1 
ATOM   2540  O  OG    . SER A 1 1768 ? 26.747  96.520  120.606 1.00 39.65  ? 1768 SER A OG    1 
ATOM   2541  N  N     . MET A 1 1769 ? 28.494  97.557  117.501 1.00 39.40  ? 1769 MET A N     1 
ATOM   2542  C  CA    . MET A 1 1769 ? 28.437  98.864  116.853 1.00 38.58  ? 1769 MET A CA    1 
ATOM   2543  C  C     . MET A 1 1769 ? 28.151  98.786  115.355 1.00 49.01  ? 1769 MET A C     1 
ATOM   2544  O  O     . MET A 1 1769 ? 28.419  99.760  114.641 1.00 50.69  ? 1769 MET A O     1 
ATOM   2545  C  CB    . MET A 1 1769 ? 29.738  99.637  117.084 1.00 35.08  ? 1769 MET A CB    1 
ATOM   2546  C  CG    . MET A 1 1769 ? 30.104  99.805  118.537 1.00 33.06  ? 1769 MET A CG    1 
ATOM   2547  S  SD    . MET A 1 1769 ? 31.865  100.072 118.795 1.00 42.40  ? 1769 MET A SD    1 
ATOM   2548  C  CE    . MET A 1 1769 ? 32.032  101.744 118.181 1.00 35.62  ? 1769 MET A CE    1 
ATOM   2549  N  N     . GLY A 1 1770 ? 27.617  97.665  114.864 1.00 51.59  ? 1770 GLY A N     1 
ATOM   2550  C  CA    . GLY A 1 1770 ? 27.364  97.536  113.438 1.00 59.62  ? 1770 GLY A CA    1 
ATOM   2551  C  C     . GLY A 1 1770 ? 26.342  98.522  112.907 1.00 67.39  ? 1770 GLY A C     1 
ATOM   2552  O  O     . GLY A 1 1770 ? 26.242  98.723  111.694 1.00 68.78  ? 1770 GLY A O     1 
ATOM   2553  N  N     . GLY A 1 1771 ? 25.573  99.147  113.795 1.00 67.39  ? 1771 GLY A N     1 
ATOM   2554  C  CA    . GLY A 1 1771 ? 24.566  100.105 113.382 1.00 74.46  ? 1771 GLY A CA    1 
ATOM   2555  C  C     . GLY A 1 1771 ? 25.120  101.478 113.057 1.00 81.70  ? 1771 GLY A C     1 
ATOM   2556  O  O     . GLY A 1 1771 ? 24.381  102.361 112.612 1.00 82.07  ? 1771 GLY A O     1 
ATOM   2557  N  N     . GLY A 1 1772 ? 26.418  101.672 113.278 1.00 77.07  ? 1772 GLY A N     1 
ATOM   2558  C  CA    . GLY A 1 1772 ? 27.051  102.945 112.992 1.00 75.56  ? 1772 GLY A CA    1 
ATOM   2559  C  C     . GLY A 1 1772 ? 26.780  104.002 114.042 1.00 79.92  ? 1772 GLY A C     1 
ATOM   2560  O  O     . GLY A 1 1772 ? 27.692  104.420 114.762 1.00 70.52  ? 1772 GLY A O     1 
ATOM   2561  N  N     . GLY A 1 1773 ? 25.528  104.444 114.139 1.00 85.31  ? 1773 GLY A N     1 
ATOM   2562  C  CA    . GLY A 1 1773 ? 25.131  105.441 115.111 1.00 81.96  ? 1773 GLY A CA    1 
ATOM   2563  C  C     . GLY A 1 1773 ? 24.847  104.921 116.500 1.00 84.01  ? 1773 GLY A C     1 
ATOM   2564  O  O     . GLY A 1 1773 ? 24.477  105.703 117.380 1.00 85.27  ? 1773 GLY A O     1 
ATOM   2565  N  N     . ASP A 1 1774 ? 25.006  103.620 116.723 1.00 81.72  ? 1774 ASP A N     1 
ATOM   2566  C  CA    . ASP A 1 1774 ? 24.737  103.033 118.025 1.00 79.96  ? 1774 ASP A CA    1 
ATOM   2567  C  C     . ASP A 1 1774 ? 25.791  103.462 119.043 1.00 74.75  ? 1774 ASP A C     1 
ATOM   2568  O  O     . ASP A 1 1774 ? 26.857  103.980 118.699 1.00 66.92  ? 1774 ASP A O     1 
ATOM   2569  C  CB    . ASP A 1 1774 ? 24.699  101.507 117.928 1.00 77.36  ? 1774 ASP A CB    1 
ATOM   2570  C  CG    . ASP A 1 1774 ? 23.505  101.003 117.145 1.00 85.21  ? 1774 ASP A CG    1 
ATOM   2571  O  OD1   . ASP A 1 1774 ? 22.460  101.686 117.146 1.00 92.11  ? 1774 ASP A OD1   1 
ATOM   2572  O  OD2   . ASP A 1 1774 ? 23.611  99.922  116.528 1.00 72.67  ? 1774 ASP A OD2   1 
ATOM   2573  N  N     . ALA A 1 1775 ? 25.473  103.240 120.317 1.00 75.88  ? 1775 ALA A N     1 
ATOM   2574  C  CA    . ALA A 1 1775 ? 26.413  103.542 121.386 1.00 69.43  ? 1775 ALA A CA    1 
ATOM   2575  C  C     . ALA A 1 1775 ? 27.639  102.642 121.283 1.00 59.40  ? 1775 ALA A C     1 
ATOM   2576  O  O     . ALA A 1 1775 ? 27.585  101.539 120.733 1.00 54.75  ? 1775 ALA A O     1 
ATOM   2577  C  CB    . ALA A 1 1775 ? 25.744  103.372 122.750 1.00 58.68  ? 1775 ALA A CB    1 
ATOM   2578  N  N     . ALA A 1 1776 ? 28.758  103.126 121.821 1.00 53.26  ? 1776 ALA A N     1 
ATOM   2579  C  CA    . ALA A 1 1776 ? 30.030  102.440 121.666 1.00 45.83  ? 1776 ALA A CA    1 
ATOM   2580  C  C     . ALA A 1 1776 ? 30.402  101.712 122.948 1.00 43.26  ? 1776 ALA A C     1 
ATOM   2581  O  O     . ALA A 1 1776 ? 30.712  102.369 123.954 1.00 30.76  ? 1776 ALA A O     1 
ATOM   2582  C  CB    . ALA A 1 1776 ? 31.126  103.435 121.286 1.00 30.73  ? 1776 ALA A CB    1 
ATOM   2583  N  N     . PRO A 1 1777 ? 30.389  100.378 122.970 1.00 46.30  ? 1777 PRO A N     1 
ATOM   2584  C  CA    . PRO A 1 1777 ? 30.991  99.638  124.084 1.00 37.82  ? 1777 PRO A CA    1 
ATOM   2585  C  C     . PRO A 1 1777 ? 32.494  99.442  123.962 1.00 24.00  ? 1777 PRO A C     1 
ATOM   2586  O  O     . PRO A 1 1777 ? 33.068  98.700  124.764 1.00 21.74  ? 1777 PRO A O     1 
ATOM   2587  C  CB    . PRO A 1 1777 ? 30.260  98.286  124.036 1.00 33.85  ? 1777 PRO A CB    1 
ATOM   2588  C  CG    . PRO A 1 1777 ? 29.690  98.170  122.657 1.00 34.26  ? 1777 PRO A CG    1 
ATOM   2589  C  CD    . PRO A 1 1777 ? 29.825  99.484  121.948 1.00 36.82  ? 1777 PRO A CD    1 
ATOM   2590  N  N     . LEU A 1 1778 ? 33.135  100.076 122.976 1.00 18.85  ? 1778 LEU A N     1 
ATOM   2591  C  CA    . LEU A 1 1778 ? 34.592  100.094 122.924 1.00 16.96  ? 1778 LEU A CA    1 
ATOM   2592  C  C     . LEU A 1 1778 ? 35.174  100.793 124.144 1.00 16.97  ? 1778 LEU A C     1 
ATOM   2593  O  O     . LEU A 1 1778 ? 36.251  100.419 124.626 1.00 16.07  ? 1778 LEU A O     1 
ATOM   2594  C  CB    . LEU A 1 1778 ? 35.059  100.784 121.642 1.00 18.32  ? 1778 LEU A CB    1 
ATOM   2595  C  CG    . LEU A 1 1778 ? 35.480  99.906  120.463 1.00 22.30  ? 1778 LEU A CG    1 
ATOM   2596  C  CD1   . LEU A 1 1778 ? 36.051  100.766 119.345 1.00 20.22  ? 1778 LEU A CD1   1 
ATOM   2597  C  CD2   . LEU A 1 1778 ? 36.485  98.856  120.902 1.00 13.78  ? 1778 LEU A CD2   1 
ATOM   2598  N  N     . HIS A 1 1779 ? 34.475  101.814 124.649 1.00 17.57  ? 1779 HIS A N     1 
ATOM   2599  C  CA    . HIS A 1 1779 ? 34.889  102.463 125.886 1.00 18.69  ? 1779 HIS A CA    1 
ATOM   2600  C  C     . HIS A 1 1779 ? 34.917  101.479 127.047 1.00 15.80  ? 1779 HIS A C     1 
ATOM   2601  O  O     . HIS A 1 1779 ? 35.750  101.608 127.948 1.00 17.08  ? 1779 HIS A O     1 
ATOM   2602  C  CB    . HIS A 1 1779 ? 33.955  103.631 126.204 1.00 21.26  ? 1779 HIS A CB    1 
ATOM   2603  C  CG    . HIS A 1 1779 ? 34.031  104.754 125.217 1.00 25.64  ? 1779 HIS A CG    1 
ATOM   2604  N  ND1   . HIS A 1 1779 ? 33.037  105.001 124.294 1.00 31.24  ? 1779 HIS A ND1   1 
ATOM   2605  C  CD2   . HIS A 1 1779 ? 34.978  105.699 125.011 1.00 26.23  ? 1779 HIS A CD2   1 
ATOM   2606  C  CE1   . HIS A 1 1779 ? 33.371  106.048 123.561 1.00 28.96  ? 1779 HIS A CE1   1 
ATOM   2607  N  NE2   . HIS A 1 1779 ? 34.543  106.491 123.976 1.00 30.39  ? 1779 HIS A NE2   1 
ATOM   2608  N  N     . SER A 1 1780 ? 34.024  100.485 127.042 1.00 13.27  ? 1780 SER A N     1 
ATOM   2609  C  CA    . SER A 1 1780 ? 34.034  99.481  128.101 1.00 17.26  ? 1780 SER A CA    1 
ATOM   2610  C  C     . SER A 1 1780 ? 35.262  98.581  128.002 1.00 16.98  ? 1780 SER A C     1 
ATOM   2611  O  O     . SER A 1 1780 ? 35.842  98.199  129.025 1.00 15.94  ? 1780 SER A O     1 
ATOM   2612  C  CB    . SER A 1 1780 ? 32.751  98.653  128.050 1.00 22.72  ? 1780 SER A CB    1 
ATOM   2613  O  OG    . SER A 1 1780 ? 31.619  99.458  128.327 1.00 35.63  ? 1780 SER A OG    1 
ATOM   2614  N  N     . VAL A 1 1781 ? 35.668  98.227  126.781 1.00 14.26  ? 1781 VAL A N     1 
ATOM   2615  C  CA    . VAL A 1 1781 ? 36.909  97.478  126.596 1.00 12.47  ? 1781 VAL A CA    1 
ATOM   2616  C  C     . VAL A 1 1781 ? 38.091  98.300  127.095 1.00 12.79  ? 1781 VAL A C     1 
ATOM   2617  O  O     . VAL A 1 1781 ? 38.984  97.792  127.790 1.00 17.50  ? 1781 VAL A O     1 
ATOM   2618  C  CB    . VAL A 1 1781 ? 37.079  97.082  125.117 1.00 16.09  ? 1781 VAL A CB    1 
ATOM   2619  C  CG1   . VAL A 1 1781 ? 38.469  96.513  124.868 1.00 10.47  ? 1781 VAL A CG1   1 
ATOM   2620  C  CG2   . VAL A 1 1781 ? 36.002  96.089  124.704 1.00 13.50  ? 1781 VAL A CG2   1 
ATOM   2621  N  N     . LEU A 1 1782 ? 38.105  99.590  126.746 1.00 11.83  ? 1782 LEU A N     1 
ATOM   2622  C  CA    . LEU A 1 1782 ? 39.123  100.493 127.270 1.00 11.55  ? 1782 LEU A CA    1 
ATOM   2623  C  C     . LEU A 1 1782 ? 39.142  100.481 128.793 1.00 12.52  ? 1782 LEU A C     1 
ATOM   2624  O  O     . LEU A 1 1782 ? 40.210  100.399 129.403 1.00 13.04  ? 1782 LEU A O     1 
ATOM   2625  C  CB    . LEU A 1 1782 ? 38.877  101.913 126.763 1.00 12.50  ? 1782 LEU A CB    1 
ATOM   2626  C  CG    . LEU A 1 1782 ? 39.756  102.984 127.415 1.00 19.21  ? 1782 LEU A CG    1 
ATOM   2627  C  CD1   . LEU A 1 1782 ? 41.209  102.846 126.980 1.00 14.50  ? 1782 LEU A CD1   1 
ATOM   2628  C  CD2   . LEU A 1 1782 ? 39.221  104.385 127.157 1.00 14.17  ? 1782 LEU A CD2   1 
ATOM   2629  N  N     . SER A 1 1783 ? 37.966  100.565 129.419 1.00 10.55  ? 1783 SER A N     1 
ATOM   2630  C  CA    . SER A 1 1783 ? 37.883  100.614 130.876 1.00 14.32  ? 1783 SER A CA    1 
ATOM   2631  C  C     . SER A 1 1783 ? 38.391  99.323  131.506 1.00 14.00  ? 1783 SER A C     1 
ATOM   2632  O  O     . SER A 1 1783 ? 39.068  99.348  132.540 1.00 14.76  ? 1783 SER A O     1 
ATOM   2633  C  CB    . SER A 1 1783 ? 36.442  100.893 131.305 1.00 17.56  ? 1783 SER A CB    1 
ATOM   2634  O  OG    . SER A 1 1783 ? 36.267  100.657 132.690 1.00 26.04  ? 1783 SER A OG    1 
ATOM   2635  N  N     . ASN A 1 1784 ? 38.045  98.178  130.912 1.00 16.28  ? 1784 ASN A N     1 
ATOM   2636  C  CA    . ASN A 1 1784 ? 38.532  96.904  131.431 1.00 12.39  ? 1784 ASN A CA    1 
ATOM   2637  C  C     . ASN A 1 1784 ? 40.051  96.826  131.349 1.00 11.61  ? 1784 ASN A C     1 
ATOM   2638  O  O     . ASN A 1 1784 ? 40.713  96.387  132.301 1.00 13.70  ? 1784 ASN A O     1 
ATOM   2639  C  CB    . ASN A 1 1784 ? 37.893  95.744  130.668 1.00 19.29  ? 1784 ASN A CB    1 
ATOM   2640  C  CG    . ASN A 1 1784 ? 38.445  94.394  131.088 1.00 24.46  ? 1784 ASN A CG    1 
ATOM   2641  O  OD1   . ASN A 1 1784 ? 38.261  93.961  132.225 1.00 20.93  ? 1784 ASN A OD1   1 
ATOM   2642  N  ND2   . ASN A 1 1784 ? 39.128  93.723  130.169 1.00 21.04  ? 1784 ASN A ND2   1 
ATOM   2643  N  N     . VAL A 1 1785 ? 40.623  97.261  130.223 1.00 10.50  ? 1785 VAL A N     1 
ATOM   2644  C  CA    . VAL A 1 1785 ? 42.078  97.271  130.099 1.00 10.46  ? 1785 VAL A CA    1 
ATOM   2645  C  C     . VAL A 1 1785 ? 42.695  98.236  131.107 1.00 11.99  ? 1785 VAL A C     1 
ATOM   2646  O  O     . VAL A 1 1785 ? 43.743  97.950  131.696 1.00 12.69  ? 1785 VAL A O     1 
ATOM   2647  C  CB    . VAL A 1 1785 ? 42.495  97.604  128.654 1.00 9.76   ? 1785 VAL A CB    1 
ATOM   2648  C  CG1   . VAL A 1 1785 ? 44.010  97.645  128.530 1.00 6.86   ? 1785 VAL A CG1   1 
ATOM   2649  C  CG2   . VAL A 1 1785 ? 41.918  96.581  127.689 1.00 10.66  ? 1785 VAL A CG2   1 
ATOM   2650  N  N     . GLU A 1 1786 ? 42.050  99.385  131.331 1.00 11.86  ? 1786 GLU A N     1 
ATOM   2651  C  CA    . GLU A 1 1786 ? 42.539  100.343 132.322 1.00 13.38  ? 1786 GLU A CA    1 
ATOM   2652  C  C     . GLU A 1 1786 ? 42.569  99.729  133.715 1.00 13.61  ? 1786 GLU A C     1 
ATOM   2653  O  O     . GLU A 1 1786 ? 43.551  99.872  134.449 1.00 14.09  ? 1786 GLU A O     1 
ATOM   2654  C  CB    . GLU A 1 1786 ? 41.664  101.599 132.334 1.00 17.07  ? 1786 GLU A CB    1 
ATOM   2655  C  CG    . GLU A 1 1786 ? 41.699  102.452 131.082 1.00 21.18  ? 1786 GLU A CG    1 
ATOM   2656  C  CD    . GLU A 1 1786 ? 43.043  103.103 130.850 1.00 34.91  ? 1786 GLU A CD    1 
ATOM   2657  O  OE1   . GLU A 1 1786 ? 43.735  103.417 131.841 1.00 43.71  ? 1786 GLU A OE1   1 
ATOM   2658  O  OE2   . GLU A 1 1786 ? 43.396  103.320 129.674 1.00 36.06  ? 1786 GLU A OE2   1 
ATOM   2659  N  N     . VAL A 1 1787 ? 41.485  99.054  134.100 1.00 12.42  ? 1787 VAL A N     1 
ATOM   2660  C  CA    . VAL A 1 1787 ? 41.408  98.458  135.430 1.00 17.55  ? 1787 VAL A CA    1 
ATOM   2661  C  C     . VAL A 1 1787 ? 42.459  97.367  135.588 1.00 15.77  ? 1787 VAL A C     1 
ATOM   2662  O  O     . VAL A 1 1787 ? 43.140  97.278  136.623 1.00 17.31  ? 1787 VAL A O     1 
ATOM   2663  C  CB    . VAL A 1 1787 ? 39.986  97.925  135.689 1.00 16.68  ? 1787 VAL A CB    1 
ATOM   2664  C  CG1   . VAL A 1 1787 ? 39.993  96.874  136.791 1.00 22.34  ? 1787 VAL A CG1   1 
ATOM   2665  C  CG2   . VAL A 1 1787 ? 39.049  99.068  136.040 1.00 18.59  ? 1787 VAL A CG2   1 
ATOM   2666  N  N     . THR A 1 1788 ? 42.617  96.522  134.567 1.00 11.33  ? 1788 THR A N     1 
ATOM   2667  C  CA    . THR A 1 1788 ? 43.601  95.450  134.657 1.00 11.40  ? 1788 THR A CA    1 
ATOM   2668  C  C     . THR A 1 1788 ? 45.016  96.016  134.729 1.00 10.87  ? 1788 THR A C     1 
ATOM   2669  O  O     . THR A 1 1788 ? 45.860  95.516  135.480 1.00 13.95  ? 1788 THR A O     1 
ATOM   2670  C  CB    . THR A 1 1788 ? 43.455  94.500  133.471 1.00 12.49  ? 1788 THR A CB    1 
ATOM   2671  O  OG1   . THR A 1 1788 ? 42.108  94.019  133.412 1.00 14.22  ? 1788 THR A OG1   1 
ATOM   2672  C  CG2   . THR A 1 1788 ? 44.365  93.308  133.665 1.00 12.35  ? 1788 THR A CG2   1 
ATOM   2673  N  N     . LEU A 1 1789 ? 45.290  97.072  133.956 1.00 10.45  ? 1789 LEU A N     1 
ATOM   2674  C  CA    . LEU A 1 1789 ? 46.596  97.721  134.016 1.00 9.38   ? 1789 LEU A CA    1 
ATOM   2675  C  C     . LEU A 1 1789 ? 46.833  98.366  135.374 1.00 13.52  ? 1789 LEU A C     1 
ATOM   2676  O  O     . LEU A 1 1789 ? 47.964  98.382  135.870 1.00 18.49  ? 1789 LEU A O     1 
ATOM   2677  C  CB    . LEU A 1 1789 ? 46.721  98.762  132.904 1.00 7.82   ? 1789 LEU A CB    1 
ATOM   2678  C  CG    . LEU A 1 1789 ? 47.271  98.280  131.562 1.00 8.47   ? 1789 LEU A CG    1 
ATOM   2679  C  CD1   . LEU A 1 1789 ? 47.118  99.357  130.499 1.00 6.72   ? 1789 LEU A CD1   1 
ATOM   2680  C  CD2   . LEU A 1 1789 ? 48.729  97.868  131.706 1.00 4.50   ? 1789 LEU A CD2   1 
ATOM   2681  N  N     . ASN A 1 1790 ? 45.784  98.921  135.982 1.00 13.53  ? 1790 ASN A N     1 
ATOM   2682  C  CA    . ASN A 1 1790 ? 45.916  99.483  137.322 1.00 16.77  ? 1790 ASN A CA    1 
ATOM   2683  C  C     . ASN A 1 1790 ? 46.292  98.402  138.326 1.00 18.65  ? 1790 ASN A C     1 
ATOM   2684  O  O     . ASN A 1 1790 ? 47.172  98.599  139.173 1.00 21.72  ? 1790 ASN A O     1 
ATOM   2685  C  CB    . ASN A 1 1790 ? 44.613  100.169 137.732 1.00 18.83  ? 1790 ASN A CB    1 
ATOM   2686  C  CG    . ASN A 1 1790 ? 44.515  101.590 137.218 1.00 30.97  ? 1790 ASN A CG    1 
ATOM   2687  O  OD1   . ASN A 1 1790 ? 45.480  102.351 137.277 1.00 26.16  ? 1790 ASN A OD1   1 
ATOM   2688  N  ND2   . ASN A 1 1790 ? 43.345  101.954 136.707 1.00 30.65  ? 1790 ASN A ND2   1 
ATOM   2689  N  N     . VAL A 1 1791 ? 45.636  97.243  138.235 1.00 15.33  ? 1791 VAL A N     1 
ATOM   2690  C  CA    . VAL A 1 1791 ? 45.969  96.132  139.125 1.00 16.78  ? 1791 VAL A CA    1 
ATOM   2691  C  C     . VAL A 1 1791 ? 47.403  95.669  138.890 1.00 17.79  ? 1791 VAL A C     1 
ATOM   2692  O  O     . VAL A 1 1791 ? 48.149  95.392  139.839 1.00 18.94  ? 1791 VAL A O     1 
ATOM   2693  C  CB    . VAL A 1 1791 ? 44.962  94.981  138.942 1.00 15.76  ? 1791 VAL A CB    1 
ATOM   2694  C  CG1   . VAL A 1 1791 ? 45.380  93.771  139.761 1.00 13.07  ? 1791 VAL A CG1   1 
ATOM   2695  C  CG2   . VAL A 1 1791 ? 43.566  95.435  139.331 1.00 15.91  ? 1791 VAL A CG2   1 
ATOM   2696  N  N     . LEU A 1 1792 ? 47.813  95.584  137.621 1.00 15.15  ? 1792 LEU A N     1 
ATOM   2697  C  CA    . LEU A 1 1792 ? 49.171  95.157  137.295 1.00 12.48  ? 1792 LEU A CA    1 
ATOM   2698  C  C     . LEU A 1 1792 ? 50.209  96.135  137.838 1.00 14.12  ? 1792 LEU A C     1 
ATOM   2699  O  O     . LEU A 1 1792 ? 51.243  95.723  138.381 1.00 12.15  ? 1792 LEU A O     1 
ATOM   2700  C  CB    . LEU A 1 1792 ? 49.311  95.015  135.780 1.00 10.84  ? 1792 LEU A CB    1 
ATOM   2701  C  CG    . LEU A 1 1792 ? 48.628  93.818  135.118 1.00 10.99  ? 1792 LEU A CG    1 
ATOM   2702  C  CD1   . LEU A 1 1792 ? 48.739  93.921  133.607 1.00 7.74   ? 1792 LEU A CD1   1 
ATOM   2703  C  CD2   . LEU A 1 1792 ? 49.226  92.514  135.610 1.00 7.80   ? 1792 LEU A CD2   1 
ATOM   2704  N  N     . ALA A 1 1793 ? 49.955  97.437  137.690 1.00 15.09  ? 1793 ALA A N     1 
ATOM   2705  C  CA    . ALA A 1 1793 ? 50.872  98.442  138.214 1.00 15.93  ? 1793 ALA A CA    1 
ATOM   2706  C  C     . ALA A 1 1793 ? 50.943  98.381  139.733 1.00 20.60  ? 1793 ALA A C     1 
ATOM   2707  O  O     . ALA A 1 1793 ? 52.031  98.470  140.313 1.00 24.84  ? 1793 ALA A O     1 
ATOM   2708  C  CB    . ALA A 1 1793 ? 50.450  99.834  137.749 1.00 19.93  ? 1793 ALA A CB    1 
ATOM   2709  N  N     . ASP A 1 1794 ? 49.794  98.215  140.394 1.00 21.20  ? 1794 ASP A N     1 
ATOM   2710  C  CA    . ASP A 1 1794 ? 49.794  98.067  141.845 1.00 21.43  ? 1794 ASP A CA    1 
ATOM   2711  C  C     . ASP A 1 1794 ? 50.610  96.853  142.267 1.00 21.17  ? 1794 ASP A C     1 
ATOM   2712  O  O     . ASP A 1 1794 ? 51.327  96.895  143.273 1.00 28.02  ? 1794 ASP A O     1 
ATOM   2713  C  CB    . ASP A 1 1794 ? 48.359  97.957  142.360 1.00 27.64  ? 1794 ASP A CB    1 
ATOM   2714  C  CG    . ASP A 1 1794 ? 47.625  99.282  142.326 1.00 39.69  ? 1794 ASP A CG    1 
ATOM   2715  O  OD1   . ASP A 1 1794 ? 46.378  99.270  142.252 1.00 38.45  ? 1794 ASP A OD1   1 
ATOM   2716  O  OD2   . ASP A 1 1794 ? 48.294  100.336 142.372 1.00 42.65  ? 1794 ASP A OD2   1 
ATOM   2717  N  N     . SER A 1 1795 ? 50.508  95.759  141.510 1.00 21.32  ? 1795 SER A N     1 
ATOM   2718  C  CA    . SER A 1 1795 ? 51.300  94.572  141.814 1.00 20.46  ? 1795 SER A CA    1 
ATOM   2719  C  C     . SER A 1 1795 ? 52.792  94.836  141.644 1.00 20.79  ? 1795 SER A C     1 
ATOM   2720  O  O     . SER A 1 1795 ? 53.602  94.400  142.470 1.00 25.40  ? 1795 SER A O     1 
ATOM   2721  C  CB    . SER A 1 1795 ? 50.858  93.406  140.931 1.00 16.07  ? 1795 SER A CB    1 
ATOM   2722  O  OG    . SER A 1 1795 ? 49.495  93.088  141.152 1.00 17.91  ? 1795 SER A OG    1 
ATOM   2723  N  N     . VAL A 1 1796 ? 53.179  95.542  140.579 1.00 17.46  ? 1796 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1796 ? 54.609  95.706  140.324 1.00 21.02  ? 1796 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1796 ? 55.219  96.769  141.232 1.00 26.33  ? 1796 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1796 ? 56.444  96.822  141.391 1.00 24.87  ? 1796 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1796 ? 54.887  96.014  138.839 1.00 13.92  ? 1796 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1796 ? 54.441  94.854  137.965 1.00 15.15  ? 1796 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1796 ? 54.239  97.315  138.416 1.00 12.67  ? 1796 VAL A CG2   1 
ATOM   2730  N  N     . LEU A 1 1797 ? 54.397  97.633  141.836 1.00 26.28  ? 1797 LEU A N     1 
ATOM   2731  C  CA    . LEU A 1 1797 ? 54.940  98.574  142.815 1.00 25.39  ? 1797 LEU A CA    1 
ATOM   2732  C  C     . LEU A 1 1797 ? 55.466  97.849  144.048 1.00 27.25  ? 1797 LEU A C     1 
ATOM   2733  O  O     . LEU A 1 1797 ? 56.436  98.295  144.672 1.00 36.22  ? 1797 LEU A O     1 
ATOM   2734  C  CB    . LEU A 1 1797 ? 53.891  99.612  143.215 1.00 23.37  ? 1797 LEU A CB    1 
ATOM   2735  C  CG    . LEU A 1 1797 ? 53.337  100.538 142.132 1.00 27.11  ? 1797 LEU A CG    1 
ATOM   2736  C  CD1   . LEU A 1 1797 ? 52.330  101.514 142.721 1.00 28.44  ? 1797 LEU A CD1   1 
ATOM   2737  C  CD2   . LEU A 1 1797 ? 54.464  101.281 141.435 1.00 21.95  ? 1797 LEU A CD2   1 
ATOM   2738  N  N     . MET A 1 1798 ? 54.844  96.735  144.416 1.00 27.72  ? 1798 MET A N     1 
ATOM   2739  C  CA    . MET A 1 1798 ? 55.258  95.978  145.587 1.00 29.27  ? 1798 MET A CA    1 
ATOM   2740  C  C     . MET A 1 1798 ? 56.109  94.777  145.181 1.00 29.14  ? 1798 MET A C     1 
ATOM   2741  O  O     . MET A 1 1798 ? 56.083  94.324  144.035 1.00 31.71  ? 1798 MET A O     1 
ATOM   2742  C  CB    . MET A 1 1798 ? 54.037  95.523  146.389 1.00 30.64  ? 1798 MET A CB    1 
ATOM   2743  C  CG    . MET A 1 1798 ? 53.138  94.538  145.663 1.00 29.01  ? 1798 MET A CG    1 
ATOM   2744  S  SD    . MET A 1 1798 ? 51.727  94.032  146.665 1.00 53.54  ? 1798 MET A SD    1 
ATOM   2745  C  CE    . MET A 1 1798 ? 52.527  92.982  147.874 1.00 52.53  ? 1798 MET A CE    1 
ATOM   2746  N  N     . GLU A 1 1799 ? 56.878  94.272  146.144 1.00 31.57  ? 1799 GLU A N     1 
ATOM   2747  C  CA    . GLU A 1 1799 ? 57.791  93.167  145.884 1.00 34.13  ? 1799 GLU A CA    1 
ATOM   2748  C  C     . GLU A 1 1799 ? 57.025  91.905  145.505 1.00 33.21  ? 1799 GLU A C     1 
ATOM   2749  O  O     . GLU A 1 1799 ? 55.982  91.584  146.082 1.00 32.52  ? 1799 GLU A O     1 
ATOM   2750  C  CB    . GLU A 1 1799 ? 58.665  92.896  147.108 1.00 42.57  ? 1799 GLU A CB    1 
ATOM   2751  C  CG    . GLU A 1 1799 ? 59.773  91.883  146.865 1.00 50.72  ? 1799 GLU A CG    1 
ATOM   2752  C  CD    . GLU A 1 1799 ? 60.582  91.592  148.112 1.00 67.25  ? 1799 GLU A CD    1 
ATOM   2753  O  OE1   . GLU A 1 1799 ? 60.268  92.169  149.174 1.00 71.67  ? 1799 GLU A OE1   1 
ATOM   2754  O  OE2   . GLU A 1 1799 ? 61.531  90.784  148.032 1.00 75.36  ? 1799 GLU A OE2   1 
ATOM   2755  N  N     . GLN A 1 1800 ? 57.555  91.186  144.524 1.00 30.07  ? 1800 GLN A N     1 
ATOM   2756  C  CA    . GLN A 1 1800 ? 56.910  90.006  143.974 1.00 25.41  ? 1800 GLN A CA    1 
ATOM   2757  C  C     . GLN A 1 1800 ? 57.966  88.943  143.713 1.00 22.26  ? 1800 GLN A C     1 
ATOM   2758  O  O     . GLN A 1 1800 ? 59.152  89.260  143.575 1.00 20.65  ? 1800 GLN A O     1 
ATOM   2759  C  CB    . GLN A 1 1800 ? 56.169  90.332  142.669 1.00 16.49  ? 1800 GLN A CB    1 
ATOM   2760  C  CG    . GLN A 1 1800 ? 55.075  91.377  142.818 1.00 19.99  ? 1800 GLN A CG    1 
ATOM   2761  C  CD    . GLN A 1 1800 ? 53.803  90.823  143.420 1.00 22.16  ? 1800 GLN A CD    1 
ATOM   2762  O  OE1   . GLN A 1 1800 ? 53.717  89.640  143.742 1.00 25.48  ? 1800 GLN A OE1   1 
ATOM   2763  N  NE2   . GLN A 1 1800 ? 52.801  91.681  143.571 1.00 20.48  ? 1800 GLN A NE2   1 
ATOM   2764  N  N     . PRO A 1 1801 ? 57.569  87.674  143.653 1.00 19.15  ? 1801 PRO A N     1 
ATOM   2765  C  CA    . PRO A 1 1801 ? 58.496  86.625  143.206 1.00 16.05  ? 1801 PRO A CA    1 
ATOM   2766  C  C     . PRO A 1 1801 ? 58.986  86.907  141.798 1.00 16.02  ? 1801 PRO A C     1 
ATOM   2767  O  O     . PRO A 1 1801 ? 58.235  87.445  140.970 1.00 16.62  ? 1801 PRO A O     1 
ATOM   2768  C  CB    . PRO A 1 1801 ? 57.644  85.348  143.258 1.00 14.00  ? 1801 PRO A CB    1 
ATOM   2769  C  CG    . PRO A 1 1801 ? 56.552  85.653  144.219 1.00 18.49  ? 1801 PRO A CG    1 
ATOM   2770  C  CD    . PRO A 1 1801 ? 56.282  87.123  144.112 1.00 17.88  ? 1801 PRO A CD    1 
ATOM   2771  N  N     . PRO A 1 1802 ? 60.245  86.574  141.493 1.00 19.59  ? 1802 PRO A N     1 
ATOM   2772  C  CA    . PRO A 1 1802 ? 60.817  86.980  140.195 1.00 17.43  ? 1802 PRO A CA    1 
ATOM   2773  C  C     . PRO A 1 1802 ? 60.046  86.472  138.987 1.00 15.39  ? 1802 PRO A C     1 
ATOM   2774  O  O     . PRO A 1 1802 ? 59.826  87.234  138.038 1.00 18.50  ? 1802 PRO A O     1 
ATOM   2775  C  CB    . PRO A 1 1802 ? 62.235  86.395  140.252 1.00 15.75  ? 1802 PRO A CB    1 
ATOM   2776  C  CG    . PRO A 1 1802 ? 62.533  86.284  141.715 1.00 21.47  ? 1802 PRO A CG    1 
ATOM   2777  C  CD    . PRO A 1 1802 ? 61.231  85.873  142.332 1.00 18.88  ? 1802 PRO A CD    1 
ATOM   2778  N  N     . LEU A 1 1803 ? 59.622  85.207  138.997 1.00 12.39  ? 1803 LEU A N     1 
ATOM   2779  C  CA    . LEU A 1 1803 ? 58.848  84.677  137.878 1.00 14.42  ? 1803 LEU A CA    1 
ATOM   2780  C  C     . LEU A 1 1803 ? 57.523  85.415  137.740 1.00 15.61  ? 1803 LEU A C     1 
ATOM   2781  O  O     . LEU A 1 1803 ? 57.128  85.822  136.637 1.00 16.82  ? 1803 LEU A O     1 
ATOM   2782  C  CB    . LEU A 1 1803 ? 58.618  83.177  138.075 1.00 17.79  ? 1803 LEU A CB    1 
ATOM   2783  C  CG    . LEU A 1 1803 ? 57.759  82.443  137.045 1.00 19.37  ? 1803 LEU A CG    1 
ATOM   2784  C  CD1   . LEU A 1 1803 ? 58.320  82.640  135.653 1.00 14.36  ? 1803 LEU A CD1   1 
ATOM   2785  C  CD2   . LEU A 1 1803 ? 57.661  80.963  137.380 1.00 19.62  ? 1803 LEU A CD2   1 
ATOM   2786  N  N     . ARG A 1 1804 ? 56.831  85.616  138.863 1.00 15.08  ? 1804 ARG A N     1 
ATOM   2787  C  CA    . ARG A 1 1804 ? 55.582  86.363  138.840 1.00 12.43  ? 1804 ARG A CA    1 
ATOM   2788  C  C     . ARG A 1 1804 ? 55.821  87.814  138.441 1.00 11.47  ? 1804 ARG A C     1 
ATOM   2789  O  O     . ARG A 1 1804 ? 55.001  88.415  137.739 1.00 15.11  ? 1804 ARG A O     1 
ATOM   2790  C  CB    . ARG A 1 1804 ? 54.894  86.269  140.203 1.00 14.98  ? 1804 ARG A CB    1 
ATOM   2791  C  CG    . ARG A 1 1804 ? 53.621  87.081  140.303 1.00 13.40  ? 1804 ARG A CG    1 
ATOM   2792  C  CD    . ARG A 1 1804 ? 53.171  87.293  141.731 1.00 16.45  ? 1804 ARG A CD    1 
ATOM   2793  N  NE    . ARG A 1 1804 ? 52.874  86.041  142.416 1.00 19.38  ? 1804 ARG A NE    1 
ATOM   2794  C  CZ    . ARG A 1 1804 ? 52.476  85.958  143.678 1.00 17.49  ? 1804 ARG A CZ    1 
ATOM   2795  N  NH1   . ARG A 1 1804 ? 52.316  87.039  144.424 1.00 17.36  ? 1804 ARG A NH1   1 
ATOM   2796  N  NH2   . ARG A 1 1804 ? 52.228  84.763  144.203 1.00 18.82  ? 1804 ARG A NH2   1 
ATOM   2797  N  N     . ARG A 1 1805 ? 56.950  88.389  138.864 1.00 11.54  ? 1805 ARG A N     1 
ATOM   2798  C  CA    . ARG A 1 1805 ? 57.273  89.759  138.474 1.00 12.28  ? 1805 ARG A CA    1 
ATOM   2799  C  C     . ARG A 1 1805 ? 57.451  89.880  136.965 1.00 13.48  ? 1805 ARG A C     1 
ATOM   2800  O  O     . ARG A 1 1805 ? 56.967  90.838  136.349 1.00 15.25  ? 1805 ARG A O     1 
ATOM   2801  C  CB    . ARG A 1 1805 ? 58.535  90.229  139.199 1.00 14.05  ? 1805 ARG A CB    1 
ATOM   2802  C  CG    . ARG A 1 1805 ? 58.817  91.714  139.043 1.00 16.03  ? 1805 ARG A CG    1 
ATOM   2803  C  CD    . ARG A 1 1805 ? 60.285  92.038  139.255 1.00 18.99  ? 1805 ARG A CD    1 
ATOM   2804  N  NE    . ARG A 1 1805 ? 61.122  91.538  138.171 1.00 26.10  ? 1805 ARG A NE    1 
ATOM   2805  C  CZ    . ARG A 1 1805 ? 62.103  90.660  138.325 1.00 26.46  ? 1805 ARG A CZ    1 
ATOM   2806  N  NH1   . ARG A 1 1805 ? 62.404  90.161  139.513 1.00 21.81  ? 1805 ARG A NH1   1 
ATOM   2807  N  NH2   . ARG A 1 1805 ? 62.802  90.274  137.262 1.00 26.80  ? 1805 ARG A NH2   1 
ATOM   2808  N  N     . ARG A 1 1806 ? 58.144  88.920  136.350 1.00 13.30  ? 1806 ARG A N     1 
ATOM   2809  C  CA    . ARG A 1 1806 ? 58.344  88.976  134.905 1.00 11.70  ? 1806 ARG A CA    1 
ATOM   2810  C  C     . ARG A 1 1806 ? 57.034  88.731  134.160 1.00 8.48   ? 1806 ARG A C     1 
ATOM   2811  O  O     . ARG A 1 1806 ? 56.776  89.354  133.119 1.00 8.10   ? 1806 ARG A O     1 
ATOM   2812  C  CB    . ARG A 1 1806 ? 59.434  87.982  134.495 1.00 12.44  ? 1806 ARG A CB    1 
ATOM   2813  C  CG    . ARG A 1 1806 ? 60.738  88.235  135.251 1.00 16.15  ? 1806 ARG A CG    1 
ATOM   2814  C  CD    . ARG A 1 1806 ? 61.972  87.515  134.712 1.00 18.26  ? 1806 ARG A CD    1 
ATOM   2815  N  NE    . ARG A 1 1806 ? 62.377  87.975  133.388 1.00 29.01  ? 1806 ARG A NE    1 
ATOM   2816  C  CZ    . ARG A 1 1806 ? 62.616  87.175  132.357 1.00 32.20  ? 1806 ARG A CZ    1 
ATOM   2817  N  NH1   . ARG A 1 1806 ? 62.596  85.860  132.485 1.00 25.69  ? 1806 ARG A NH1   1 
ATOM   2818  N  NH2   . ARG A 1 1806 ? 62.913  87.711  131.177 1.00 31.40  ? 1806 ARG A NH2   1 
ATOM   2819  N  N     . LYS A 1 1807 ? 56.175  87.855  134.694 1.00 8.36   ? 1807 LYS A N     1 
ATOM   2820  C  CA    . LYS A 1 1807 ? 54.842  87.700  134.115 1.00 7.59   ? 1807 LYS A CA    1 
ATOM   2821  C  C     . LYS A 1 1807 ? 54.065  89.012  134.167 1.00 8.40   ? 1807 LYS A C     1 
ATOM   2822  O  O     . LYS A 1 1807 ? 53.405  89.398  133.193 1.00 7.95   ? 1807 LYS A O     1 
ATOM   2823  C  CB    . LYS A 1 1807 ? 54.065  86.596  134.834 1.00 9.25   ? 1807 LYS A CB    1 
ATOM   2824  C  CG    . LYS A 1 1807 ? 54.597  85.191  134.645 1.00 8.92   ? 1807 LYS A CG    1 
ATOM   2825  C  CD    . LYS A 1 1807 ? 53.779  84.195  135.451 1.00 9.93   ? 1807 LYS A CD    1 
ATOM   2826  C  CE    . LYS A 1 1807 ? 54.209  82.765  135.177 1.00 11.03  ? 1807 LYS A CE    1 
ATOM   2827  N  NZ    . LYS A 1 1807 ? 53.422  81.792  135.984 1.00 10.28  ? 1807 LYS A NZ    1 
ATOM   2828  N  N     . LEU A 1 1808 ? 54.134  89.712  135.304 1.00 9.20   ? 1808 LEU A N     1 
ATOM   2829  C  CA    . LEU A 1 1808 ? 53.451  90.996  135.429 1.00 6.90   ? 1808 LEU A CA    1 
ATOM   2830  C  C     . LEU A 1 1808 ? 54.008  92.018  134.446 1.00 5.88   ? 1808 LEU A C     1 
ATOM   2831  O  O     . LEU A 1 1808 ? 53.253  92.804  133.868 1.00 7.31   ? 1808 LEU A O     1 
ATOM   2832  C  CB    . LEU A 1 1808 ? 53.561  91.527  136.859 1.00 11.10  ? 1808 LEU A CB    1 
ATOM   2833  C  CG    . LEU A 1 1808 ? 52.927  90.737  138.005 1.00 10.25  ? 1808 LEU A CG    1 
ATOM   2834  C  CD1   . LEU A 1 1808 ? 53.495  91.182  139.340 1.00 11.09  ? 1808 LEU A CD1   1 
ATOM   2835  C  CD2   . LEU A 1 1808 ? 51.414  90.871  137.993 1.00 11.49  ? 1808 LEU A CD2   1 
ATOM   2836  N  N     . GLU A 1 1809 ? 55.329  92.037  134.261 1.00 5.95   ? 1809 GLU A N     1 
ATOM   2837  C  CA    . GLU A 1 1809 ? 55.926  92.979  133.316 1.00 7.61   ? 1809 GLU A CA    1 
ATOM   2838  C  C     . GLU A 1 1809 ? 55.451  92.711  131.891 1.00 5.79   ? 1809 GLU A C     1 
ATOM   2839  O  O     . GLU A 1 1809 ? 55.124  93.646  131.146 1.00 5.11   ? 1809 GLU A O     1 
ATOM   2840  C  CB    . GLU A 1 1809 ? 57.450  92.907  133.397 1.00 6.94   ? 1809 GLU A CB    1 
ATOM   2841  C  CG    . GLU A 1 1809 ? 58.024  93.413  134.708 1.00 13.58  ? 1809 GLU A CG    1 
ATOM   2842  C  CD    . GLU A 1 1809 ? 59.490  93.069  134.871 1.00 26.37  ? 1809 GLU A CD    1 
ATOM   2843  O  OE1   . GLU A 1 1809 ? 60.045  92.389  133.982 1.00 25.54  ? 1809 GLU A OE1   1 
ATOM   2844  O  OE2   . GLU A 1 1809 ? 60.088  93.477  135.888 1.00 27.07  ? 1809 GLU A OE2   1 
ATOM   2845  N  N     . HIS A 1 1810 ? 55.404  91.436  131.496 1.00 6.85   ? 1810 HIS A N     1 
ATOM   2846  C  CA    . HIS A 1 1810 ? 54.917  91.099  130.160 1.00 4.59   ? 1810 HIS A CA    1 
ATOM   2847  C  C     . HIS A 1 1810 ? 53.450  91.476  129.996 1.00 4.87   ? 1810 HIS A C     1 
ATOM   2848  O  O     . HIS A 1 1810 ? 53.045  91.995  128.946 1.00 5.83   ? 1810 HIS A O     1 
ATOM   2849  C  CB    . HIS A 1 1810 ? 55.123  89.610  129.892 1.00 5.60   ? 1810 HIS A CB    1 
ATOM   2850  C  CG    . HIS A 1 1810 ? 56.551  89.172  129.973 1.00 9.99   ? 1810 HIS A CG    1 
ATOM   2851  N  ND1   . HIS A 1 1810 ? 56.960  87.906  129.617 1.00 11.64  ? 1810 HIS A ND1   1 
ATOM   2852  C  CD2   . HIS A 1 1810 ? 57.670  89.837  130.349 1.00 12.88  ? 1810 HIS A CD2   1 
ATOM   2853  C  CE1   . HIS A 1 1810 ? 58.265  87.803  129.791 1.00 13.32  ? 1810 HIS A CE1   1 
ATOM   2854  N  NE2   . HIS A 1 1810 ? 58.721  88.961  130.231 1.00 16.22  ? 1810 HIS A NE2   1 
ATOM   2855  N  N     . LEU A 1 1811 ? 52.639  91.220  131.027 1.00 3.60   ? 1811 LEU A N     1 
ATOM   2856  C  CA    . LEU A 1 1811 ? 51.237  91.619  130.990 1.00 3.27   ? 1811 LEU A CA    1 
ATOM   2857  C  C     . LEU A 1 1811 ? 51.103  93.129  130.848 1.00 3.37   ? 1811 LEU A C     1 
ATOM   2858  O  O     . LEU A 1 1811 ? 50.260  93.620  130.091 1.00 3.75   ? 1811 LEU A O     1 
ATOM   2859  C  CB    . LEU A 1 1811 ? 50.521  91.132  132.249 1.00 4.76   ? 1811 LEU A CB    1 
ATOM   2860  C  CG    . LEU A 1 1811 ? 50.125  89.659  132.298 1.00 5.28   ? 1811 LEU A CG    1 
ATOM   2861  C  CD1   . LEU A 1 1811 ? 49.411  89.351  133.598 1.00 7.33   ? 1811 LEU A CD1   1 
ATOM   2862  C  CD2   . LEU A 1 1811 ? 49.233  89.336  131.119 1.00 3.52   ? 1811 LEU A CD2   1 
ATOM   2863  N  N     . ILE A 1 1812 ? 51.926  93.882  131.579 1.00 3.65   ? 1812 ILE A N     1 
ATOM   2864  C  CA    . ILE A 1 1812 ? 51.880  95.337  131.492 1.00 3.34   ? 1812 ILE A CA    1 
ATOM   2865  C  C     . ILE A 1 1812 ? 52.205  95.797  130.080 1.00 4.06   ? 1812 ILE A C     1 
ATOM   2866  O  O     . ILE A 1 1812 ? 51.513  96.653  129.521 1.00 4.20   ? 1812 ILE A O     1 
ATOM   2867  C  CB    . ILE A 1 1812 ? 52.832  95.969  132.524 1.00 5.32   ? 1812 ILE A CB    1 
ATOM   2868  C  CG1   . ILE A 1 1812 ? 52.270  95.814  133.937 1.00 6.44   ? 1812 ILE A CG1   1 
ATOM   2869  C  CG2   . ILE A 1 1812 ? 53.085  97.426  132.195 1.00 5.70   ? 1812 ILE A CG2   1 
ATOM   2870  C  CD1   . ILE A 1 1812 ? 53.145  96.420  135.002 1.00 7.00   ? 1812 ILE A CD1   1 
ATOM   2871  N  N     . THR A 1 1813 ? 53.254  95.233  129.478 1.00 3.49   ? 1813 THR A N     1 
ATOM   2872  C  CA    . THR A 1 1813 ? 53.614  95.622  128.116 1.00 3.47   ? 1813 THR A CA    1 
ATOM   2873  C  C     . THR A 1 1813 ? 52.474  95.335  127.142 1.00 3.91   ? 1813 THR A C     1 
ATOM   2874  O  O     . THR A 1 1813 ? 52.071  96.204  126.350 1.00 4.61   ? 1813 THR A O     1 
ATOM   2875  C  CB    . THR A 1 1813 ? 54.887  94.892  127.685 1.00 4.32   ? 1813 THR A CB    1 
ATOM   2876  O  OG1   . THR A 1 1813 ? 55.935  95.161  128.625 1.00 5.85   ? 1813 THR A OG1   1 
ATOM   2877  C  CG2   . THR A 1 1813 ? 55.326  95.352  126.302 1.00 3.99   ? 1813 THR A CG2   1 
ATOM   2878  N  N     . GLU A 1 1814 ? 51.921  94.121  127.208 1.00 3.70   ? 1814 GLU A N     1 
ATOM   2879  C  CA    . GLU A 1 1814 ? 50.869  93.743  126.271 1.00 3.68   ? 1814 GLU A CA    1 
ATOM   2880  C  C     . GLU A 1 1814 ? 49.621  94.600  126.448 1.00 4.28   ? 1814 GLU A C     1 
ATOM   2881  O  O     . GLU A 1 1814 ? 49.010  95.029  125.462 1.00 4.70   ? 1814 GLU A O     1 
ATOM   2882  C  CB    . GLU A 1 1814 ? 50.528  92.264  126.430 1.00 4.08   ? 1814 GLU A CB    1 
ATOM   2883  C  CG    . GLU A 1 1814 ? 49.462  91.787  125.465 1.00 5.24   ? 1814 GLU A CG    1 
ATOM   2884  C  CD    . GLU A 1 1814 ? 49.790  92.129  124.024 1.00 11.21  ? 1814 GLU A CD    1 
ATOM   2885  O  OE1   . GLU A 1 1814 ? 50.845  91.680  123.530 1.00 12.77  ? 1814 GLU A OE1   1 
ATOM   2886  O  OE2   . GLU A 1 1814 ? 48.994  92.851  123.388 1.00 9.77   ? 1814 GLU A OE2   1 
ATOM   2887  N  N     . LEU A 1 1815 ? 49.224  94.870  127.692 1.00 3.63   ? 1815 LEU A N     1 
ATOM   2888  C  CA    . LEU A 1 1815 ? 48.006  95.645  127.897 1.00 3.82   ? 1815 LEU A CA    1 
ATOM   2889  C  C     . LEU A 1 1815 ? 48.229  97.134  127.659 1.00 3.83   ? 1815 LEU A C     1 
ATOM   2890  O  O     . LEU A 1 1815 ? 47.277  97.857  127.360 1.00 3.63   ? 1815 LEU A O     1 
ATOM   2891  C  CB    . LEU A 1 1815 ? 47.428  95.385  129.285 1.00 4.11   ? 1815 LEU A CB    1 
ATOM   2892  C  CG    . LEU A 1 1815 ? 46.573  94.114  129.375 1.00 6.84   ? 1815 LEU A CG    1 
ATOM   2893  C  CD1   . LEU A 1 1815 ? 47.368  92.814  129.310 1.00 5.28   ? 1815 LEU A CD1   1 
ATOM   2894  C  CD2   . LEU A 1 1815 ? 45.720  94.165  130.614 1.00 7.56   ? 1815 LEU A CD2   1 
ATOM   2895  N  N     . VAL A 1 1816 ? 49.470  97.613  127.750 1.00 3.60   ? 1816 VAL A N     1 
ATOM   2896  C  CA    . VAL A 1 1816 ? 49.758  98.966  127.281 1.00 4.18   ? 1816 VAL A CA    1 
ATOM   2897  C  C     . VAL A 1 1816 ? 49.558  99.047  125.773 1.00 5.42   ? 1816 VAL A C     1 
ATOM   2898  O  O     . VAL A 1 1816 ? 48.964  100.005 125.254 1.00 8.85   ? 1816 VAL A O     1 
ATOM   2899  C  CB    . VAL A 1 1816 ? 51.175  99.397  127.698 1.00 4.73   ? 1816 VAL A CB    1 
ATOM   2900  C  CG1   . VAL A 1 1816 ? 51.624  100.602 126.892 1.00 8.51   ? 1816 VAL A CG1   1 
ATOM   2901  C  CG2   . VAL A 1 1816 ? 51.195  99.738  129.176 1.00 3.82   ? 1816 VAL A CG2   1 
ATOM   2902  N  N     . HIS A 1 1817 ? 50.029  98.028  125.048 1.00 3.76   ? 1817 HIS A N     1 
ATOM   2903  C  CA    . HIS A 1 1817 ? 49.739  97.964  123.617 1.00 3.65   ? 1817 HIS A CA    1 
ATOM   2904  C  C     . HIS A 1 1817 ? 48.237  97.939  123.356 1.00 3.36   ? 1817 HIS A C     1 
ATOM   2905  O  O     . HIS A 1 1817 ? 47.736  98.632  122.461 1.00 5.52   ? 1817 HIS A O     1 
ATOM   2906  C  CB    . HIS A 1 1817 ? 50.393  96.737  122.986 1.00 4.55   ? 1817 HIS A CB    1 
ATOM   2907  C  CG    . HIS A 1 1817 ? 50.156  96.633  121.513 1.00 5.87   ? 1817 HIS A CG    1 
ATOM   2908  N  ND1   . HIS A 1 1817 ? 49.865  95.440  120.887 1.00 6.43   ? 1817 HIS A ND1   1 
ATOM   2909  C  CD2   . HIS A 1 1817 ? 50.153  97.577  120.542 1.00 5.35   ? 1817 HIS A CD2   1 
ATOM   2910  C  CE1   . HIS A 1 1817 ? 49.697  95.653  119.594 1.00 5.33   ? 1817 HIS A CE1   1 
ATOM   2911  N  NE2   . HIS A 1 1817 ? 49.870  96.941  119.358 1.00 4.66   ? 1817 HIS A NE2   1 
ATOM   2912  N  N     . GLN A 1 1818 ? 47.506  97.121  124.116 1.00 3.71   ? 1818 GLN A N     1 
ATOM   2913  C  CA    . GLN A 1 1818 ? 46.063  97.009  123.921 1.00 2.78   ? 1818 GLN A CA    1 
ATOM   2914  C  C     . GLN A 1 1818 ? 45.361  98.331  124.209 1.00 3.76   ? 1818 GLN A C     1 
ATOM   2915  O  O     . GLN A 1 1818 ? 44.429  98.716  123.494 1.00 4.75   ? 1818 GLN A O     1 
ATOM   2916  C  CB    . GLN A 1 1818 ? 45.499  95.897  124.805 1.00 2.22   ? 1818 GLN A CB    1 
ATOM   2917  C  CG    . GLN A 1 1818 ? 45.976  94.504  124.431 1.00 3.03   ? 1818 GLN A CG    1 
ATOM   2918  C  CD    . GLN A 1 1818 ? 45.517  93.449  125.416 1.00 4.34   ? 1818 GLN A CD    1 
ATOM   2919  O  OE1   . GLN A 1 1818 ? 44.903  93.761  126.435 1.00 5.48   ? 1818 GLN A OE1   1 
ATOM   2920  N  NE2   . GLN A 1 1818 ? 45.812  92.189  125.115 1.00 2.67   ? 1818 GLN A NE2   1 
ATOM   2921  N  N     . ARG A 1 1819 ? 45.790  99.032  125.259 1.00 3.97   ? 1819 ARG A N     1 
ATOM   2922  C  CA    . ARG A 1 1819 ? 45.237  100.344 125.573 1.00 5.41   ? 1819 ARG A CA    1 
ATOM   2923  C  C     . ARG A 1 1819 ? 45.488  101.332 124.444 1.00 6.49   ? 1819 ARG A C     1 
ATOM   2924  O  O     . ARG A 1 1819 ? 44.587  102.087 124.060 1.00 7.00   ? 1819 ARG A O     1 
ATOM   2925  C  CB    . ARG A 1 1819 ? 45.837  100.852 126.884 1.00 8.85   ? 1819 ARG A CB    1 
ATOM   2926  C  CG    . ARG A 1 1819 ? 45.362  102.227 127.309 1.00 11.87  ? 1819 ARG A CG    1 
ATOM   2927  C  CD    . ARG A 1 1819 ? 46.210  102.769 128.450 1.00 14.54  ? 1819 ARG A CD    1 
ATOM   2928  N  NE    . ARG A 1 1819 ? 47.627  102.838 128.118 1.00 16.32  ? 1819 ARG A NE    1 
ATOM   2929  C  CZ    . ARG A 1 1819 ? 48.589  103.082 128.998 1.00 16.54  ? 1819 ARG A CZ    1 
ATOM   2930  N  NH1   . ARG A 1 1819 ? 48.320  103.282 130.278 1.00 15.52  ? 1819 ARG A NH1   1 
ATOM   2931  N  NH2   . ARG A 1 1819 ? 49.851  103.128 128.583 1.00 15.71  ? 1819 ARG A NH2   1 
ATOM   2932  N  N     . ASP A 1 1820 ? 46.703  101.334 123.890 1.00 5.92   ? 1820 ASP A N     1 
ATOM   2933  C  CA    . ASP A 1 1820 ? 46.998  102.230 122.777 1.00 7.46   ? 1820 ASP A CA    1 
ATOM   2934  C  C     . ASP A 1 1820 ? 46.130  101.911 121.564 1.00 6.96   ? 1820 ASP A C     1 
ATOM   2935  O  O     . ASP A 1 1820 ? 45.593  102.819 120.915 1.00 8.22   ? 1820 ASP A O     1 
ATOM   2936  C  CB    . ASP A 1 1820 ? 48.480  102.142 122.416 1.00 14.25  ? 1820 ASP A CB    1 
ATOM   2937  C  CG    . ASP A 1 1820 ? 49.365  102.868 123.409 1.00 33.50  ? 1820 ASP A CG    1 
ATOM   2938  O  OD1   . ASP A 1 1820 ? 48.831  103.656 124.217 1.00 29.49  ? 1820 ASP A OD1   1 
ATOM   2939  O  OD2   . ASP A 1 1820 ? 50.594  102.647 123.385 1.00 35.90  ? 1820 ASP A OD2   1 
ATOM   2940  N  N     . VAL A 1 1821 ? 45.969  100.623 121.253 1.00 4.16   ? 1821 VAL A N     1 
ATOM   2941  C  CA    . VAL A 1 1821 ? 45.183  100.235 120.084 1.00 5.96   ? 1821 VAL A CA    1 
ATOM   2942  C  C     . VAL A 1 1821 ? 43.713  100.594 120.279 1.00 6.49   ? 1821 VAL A C     1 
ATOM   2943  O  O     . VAL A 1 1821 ? 43.052  101.083 119.354 1.00 7.85   ? 1821 VAL A O     1 
ATOM   2944  C  CB    . VAL A 1 1821 ? 45.371  98.736  119.788 1.00 5.01   ? 1821 VAL A CB    1 
ATOM   2945  C  CG1   . VAL A 1 1821 ? 44.378  98.271  118.734 1.00 3.11   ? 1821 VAL A CG1   1 
ATOM   2946  C  CG2   . VAL A 1 1821 ? 46.797  98.465  119.337 1.00 3.18   ? 1821 VAL A CG2   1 
ATOM   2947  N  N     . THR A 1 1822 ? 43.178  100.359 121.479 1.00 4.60   ? 1822 THR A N     1 
ATOM   2948  C  CA    . THR A 1 1822 ? 41.785  100.703 121.746 1.00 6.47   ? 1822 THR A CA    1 
ATOM   2949  C  C     . THR A 1 1822 ? 41.574  102.211 121.708 1.00 9.56   ? 1822 THR A C     1 
ATOM   2950  O  O     . THR A 1 1822 ? 40.537  102.687 121.230 1.00 9.67   ? 1822 THR A O     1 
ATOM   2951  C  CB    . THR A 1 1822 ? 41.351  100.129 123.095 1.00 8.68   ? 1822 THR A CB    1 
ATOM   2952  O  OG1   . THR A 1 1822 ? 41.542  98.709  123.093 1.00 5.38   ? 1822 THR A OG1   1 
ATOM   2953  C  CG2   . THR A 1 1822 ? 39.883  100.428 123.357 1.00 8.47   ? 1822 THR A CG2   1 
ATOM   2954  N  N     . ARG A 1 1823 ? 42.547  102.981 122.205 1.00 8.60   ? 1823 ARG A N     1 
ATOM   2955  C  CA    . ARG A 1 1823 ? 42.458  104.433 122.112 1.00 7.92   ? 1823 ARG A CA    1 
ATOM   2956  C  C     . ARG A 1 1823 ? 42.450  104.886 120.660 1.00 9.41   ? 1823 ARG A C     1 
ATOM   2957  O  O     . ARG A 1 1823 ? 41.688  105.784 120.285 1.00 13.96  ? 1823 ARG A O     1 
ATOM   2958  C  CB    . ARG A 1 1823 ? 43.615  105.077 122.877 1.00 7.83   ? 1823 ARG A CB    1 
ATOM   2959  C  CG    . ARG A 1 1823 ? 43.358  105.229 124.366 1.00 7.99   ? 1823 ARG A CG    1 
ATOM   2960  C  CD    . ARG A 1 1823 ? 44.629  105.565 125.125 1.00 13.06  ? 1823 ARG A CD    1 
ATOM   2961  N  NE    . ARG A 1 1823 ? 44.362  105.822 126.535 1.00 21.40  ? 1823 ARG A NE    1 
ATOM   2962  C  CZ    . ARG A 1 1823 ? 45.298  105.978 127.461 1.00 25.65  ? 1823 ARG A CZ    1 
ATOM   2963  N  NH1   . ARG A 1 1823 ? 46.585  105.910 127.160 1.00 22.60  ? 1823 ARG A NH1   1 
ATOM   2964  N  NH2   . ARG A 1 1823 ? 44.935  106.205 128.719 1.00 25.46  ? 1823 ARG A NH2   1 
ATOM   2965  N  N     . SER A 1 1824 ? 43.288  104.267 119.825 1.00 8.09   ? 1824 SER A N     1 
ATOM   2966  C  CA    . SER A 1 1824 ? 43.289  104.596 118.403 1.00 8.50   ? 1824 SER A CA    1 
ATOM   2967  C  C     . SER A 1 1824 ? 41.952  104.255 117.754 1.00 10.82  ? 1824 SER A C     1 
ATOM   2968  O  O     . SER A 1 1824 ? 41.437  105.025 116.936 1.00 17.57  ? 1824 SER A O     1 
ATOM   2969  C  CB    . SER A 1 1824 ? 44.431  103.867 117.698 1.00 8.52   ? 1824 SER A CB    1 
ATOM   2970  O  OG    . SER A 1 1824 ? 44.431  104.144 116.309 1.00 16.66  ? 1824 SER A OG    1 
ATOM   2971  N  N     . LEU A 1 1825 ? 41.379  103.101 118.104 1.00 9.20   ? 1825 LEU A N     1 
ATOM   2972  C  CA    . LEU A 1 1825 ? 40.108  102.696 117.509 1.00 9.98   ? 1825 LEU A CA    1 
ATOM   2973  C  C     . LEU A 1 1825 ? 38.974  103.625 117.926 1.00 14.35  ? 1825 LEU A C     1 
ATOM   2974  O  O     . LEU A 1 1825 ? 38.135  104.001 117.099 1.00 20.12  ? 1825 LEU A O     1 
ATOM   2975  C  CB    . LEU A 1 1825 ? 39.784  101.251 117.889 1.00 11.57  ? 1825 LEU A CB    1 
ATOM   2976  C  CG    . LEU A 1 1825 ? 40.674  100.170 117.274 1.00 11.30  ? 1825 LEU A CG    1 
ATOM   2977  C  CD1   . LEU A 1 1825 ? 40.191  98.789  117.676 1.00 6.35   ? 1825 LEU A CD1   1 
ATOM   2978  C  CD2   . LEU A 1 1825 ? 40.711  100.306 115.761 1.00 11.01  ? 1825 LEU A CD2   1 
ATOM   2979  N  N     . ILE A 1 1826 ? 38.925  104.003 119.204 1.00 14.22  ? 1826 ILE A N     1 
ATOM   2980  C  CA    . ILE A 1 1826 ? 37.869  104.896 119.668 1.00 14.52  ? 1826 ILE A CA    1 
ATOM   2981  C  C     . ILE A 1 1826 ? 38.049  106.292 119.081 1.00 17.03  ? 1826 ILE A C     1 
ATOM   2982  O  O     . ILE A 1 1826 ? 37.070  106.967 118.740 1.00 23.98  ? 1826 ILE A O     1 
ATOM   2983  C  CB    . ILE A 1 1826 ? 37.820  104.918 121.206 1.00 14.88  ? 1826 ILE A CB    1 
ATOM   2984  C  CG1   . ILE A 1 1826 ? 37.380  103.550 121.734 1.00 15.61  ? 1826 ILE A CG1   1 
ATOM   2985  C  CG2   . ILE A 1 1826 ? 36.892  106.012 121.705 1.00 16.45  ? 1826 ILE A CG2   1 
ATOM   2986  C  CD1   . ILE A 1 1826 ? 37.462  103.406 123.236 1.00 12.45  ? 1826 ILE A CD1   1 
ATOM   2987  N  N     . LYS A 1 1827 ? 39.298  106.741 118.940 1.00 15.43  ? 1827 LYS A N     1 
ATOM   2988  C  CA    . LYS A 1 1827 ? 39.552  108.071 118.399 1.00 18.47  ? 1827 LYS A CA    1 
ATOM   2989  C  C     . LYS A 1 1827 ? 39.085  108.195 116.953 1.00 23.18  ? 1827 LYS A C     1 
ATOM   2990  O  O     . LYS A 1 1827 ? 38.693  109.285 116.520 1.00 29.87  ? 1827 LYS A O     1 
ATOM   2991  C  CB    . LYS A 1 1827 ? 41.042  108.398 118.508 1.00 23.36  ? 1827 LYS A CB    1 
ATOM   2992  C  CG    . LYS A 1 1827 ? 41.426  109.787 118.025 1.00 32.68  ? 1827 LYS A CG    1 
ATOM   2993  C  CD    . LYS A 1 1827 ? 42.925  110.010 118.140 1.00 37.22  ? 1827 LYS A CD    1 
ATOM   2994  C  CE    . LYS A 1 1827 ? 43.287  111.469 117.917 1.00 49.13  ? 1827 LYS A CE    1 
ATOM   2995  N  NZ    . LYS A 1 1827 ? 42.641  112.358 118.921 1.00 65.29  ? 1827 LYS A NZ    1 
ATOM   2996  N  N     . SER A 1 1828 ? 39.098  107.097 116.199 1.00 18.82  ? 1828 SER A N     1 
ATOM   2997  C  CA    . SER A 1 1828 ? 38.788  107.125 114.776 1.00 21.67  ? 1828 SER A CA    1 
ATOM   2998  C  C     . SER A 1 1828 ? 37.353  106.703 114.472 1.00 26.24  ? 1828 SER A C     1 
ATOM   2999  O  O     . SER A 1 1828 ? 37.004  106.535 113.299 1.00 26.82  ? 1828 SER A O     1 
ATOM   3000  C  CB    . SER A 1 1828 ? 39.772  106.243 114.007 1.00 22.34  ? 1828 SER A CB    1 
ATOM   3001  O  OG    . SER A 1 1828 ? 41.102  106.701 114.171 1.00 26.46  ? 1828 SER A OG    1 
ATOM   3002  N  N     . LYS A 1 1829 ? 36.520  106.539 115.497 1.00 23.58  ? 1829 LYS A N     1 
ATOM   3003  C  CA    . LYS A 1 1829 ? 35.115  106.159 115.339 1.00 32.12  ? 1829 LYS A CA    1 
ATOM   3004  C  C     . LYS A 1 1829 ? 34.983  104.875 114.522 1.00 27.68  ? 1829 LYS A C     1 
ATOM   3005  O  O     . LYS A 1 1829 ? 34.408  104.848 113.434 1.00 33.46  ? 1829 LYS A O     1 
ATOM   3006  C  CB    . LYS A 1 1829 ? 34.296  107.283 114.704 1.00 30.25  ? 1829 LYS A CB    1 
ATOM   3007  C  CG    . LYS A 1 1829 ? 33.867  108.397 115.644 1.00 32.29  ? 1829 LYS A CG    1 
ATOM   3008  C  CD    . LYS A 1 1829 ? 35.019  109.302 116.035 1.00 32.44  ? 1829 LYS A CD    1 
ATOM   3009  C  CE    . LYS A 1 1829 ? 34.525  110.452 116.893 1.00 47.67  ? 1829 LYS A CE    1 
ATOM   3010  N  NZ    . LYS A 1 1829 ? 35.640  111.298 117.393 1.00 55.85  ? 1829 LYS A NZ    1 
ATOM   3011  N  N     . ILE A 1 1830 ? 35.528  103.798 115.073 1.00 23.97  ? 1830 ILE A N     1 
ATOM   3012  C  CA    . ILE A 1 1830 ? 35.561  102.515 114.385 1.00 25.52  ? 1830 ILE A CA    1 
ATOM   3013  C  C     . ILE A 1 1830 ? 34.408  101.665 114.901 1.00 31.24  ? 1830 ILE A C     1 
ATOM   3014  O  O     . ILE A 1 1830 ? 34.355  101.335 116.091 1.00 38.57  ? 1830 ILE A O     1 
ATOM   3015  C  CB    . ILE A 1 1830 ? 36.908  101.810 114.591 1.00 23.73  ? 1830 ILE A CB    1 
ATOM   3016  C  CG1   . ILE A 1 1830 ? 38.048  102.755 114.213 1.00 24.93  ? 1830 ILE A CG1   1 
ATOM   3017  C  CG2   . ILE A 1 1830 ? 36.972  100.547 113.764 1.00 18.28  ? 1830 ILE A CG2   1 
ATOM   3018  C  CD1   . ILE A 1 1830 ? 37.910  103.351 112.837 1.00 24.59  ? 1830 ILE A CD1   1 
ATOM   3019  N  N     . ASP A 1 1831 ? 33.487  101.308 114.007 1.00 26.92  ? 1831 ASP A N     1 
ATOM   3020  C  CA    . ASP A 1 1831 ? 32.272  100.603 114.386 1.00 33.60  ? 1831 ASP A CA    1 
ATOM   3021  C  C     . ASP A 1 1831 ? 32.018  99.338  113.578 1.00 32.48  ? 1831 ASP A C     1 
ATOM   3022  O  O     . ASP A 1 1831 ? 31.021  98.651  113.832 1.00 32.63  ? 1831 ASP A O     1 
ATOM   3023  C  CB    . ASP A 1 1831 ? 31.066  101.548 114.273 1.00 40.05  ? 1831 ASP A CB    1 
ATOM   3024  C  CG    . ASP A 1 1831 ? 30.842  102.054 112.856 1.00 45.46  ? 1831 ASP A CG    1 
ATOM   3025  O  OD1   . ASP A 1 1831 ? 30.573  101.238 111.949 1.00 44.31  ? 1831 ASP A OD1   1 
ATOM   3026  O  OD2   . ASP A 1 1831 ? 30.945  103.281 112.648 1.00 48.31  ? 1831 ASP A OD2   1 
ATOM   3027  N  N     . ASN A 1 1832 ? 32.881  99.005  112.623 1.00 25.40  ? 1832 ASN A N     1 
ATOM   3028  C  CA    . ASN A 1 1832 ? 32.738  97.806  111.809 1.00 20.60  ? 1832 ASN A CA    1 
ATOM   3029  C  C     . ASN A 1 1832 ? 33.961  96.926  112.008 1.00 20.69  ? 1832 ASN A C     1 
ATOM   3030  O  O     . ASN A 1 1832 ? 35.094  97.395  111.870 1.00 22.40  ? 1832 ASN A O     1 
ATOM   3031  C  CB    . ASN A 1 1832 ? 32.575  98.161  110.328 1.00 22.51  ? 1832 ASN A CB    1 
ATOM   3032  C  CG    . ASN A 1 1832 ? 32.218  96.959  109.472 1.00 26.68  ? 1832 ASN A CG    1 
ATOM   3033  O  OD1   . ASN A 1 1832 ? 32.111  95.836  109.966 1.00 33.94  ? 1832 ASN A OD1   1 
ATOM   3034  N  ND2   . ASN A 1 1832 ? 32.035  97.191  108.178 1.00 26.77  ? 1832 ASN A ND2   1 
ATOM   3035  N  N     . ALA A 1 1833 ? 33.730  95.648  112.316 1.00 18.18  ? 1833 ALA A N     1 
ATOM   3036  C  CA    . ALA A 1 1833 ? 34.828  94.715  112.536 1.00 14.69  ? 1833 ALA A CA    1 
ATOM   3037  C  C     . ALA A 1 1833 ? 35.618  94.418  111.269 1.00 18.05  ? 1833 ALA A C     1 
ATOM   3038  O  O     . ALA A 1 1833 ? 36.744  93.917  111.368 1.00 18.45  ? 1833 ALA A O     1 
ATOM   3039  C  CB    . ALA A 1 1833 ? 34.298  93.409  113.131 1.00 17.46  ? 1833 ALA A CB    1 
ATOM   3040  N  N     . LYS A 1 1834 ? 35.067  94.708  110.091 1.00 18.19  ? 1834 LYS A N     1 
ATOM   3041  C  CA    . LYS A 1 1834 ? 35.766  94.479  108.835 1.00 17.65  ? 1834 LYS A CA    1 
ATOM   3042  C  C     . LYS A 1 1834 ? 36.598  95.673  108.385 1.00 13.74  ? 1834 LYS A C     1 
ATOM   3043  O  O     . LYS A 1 1834 ? 37.227  95.601  107.324 1.00 15.11  ? 1834 LYS A O     1 
ATOM   3044  C  CB    . LYS A 1 1834 ? 34.769  94.110  107.729 1.00 20.69  ? 1834 LYS A CB    1 
ATOM   3045  C  CG    . LYS A 1 1834 ? 33.942  92.841  107.967 1.00 21.22  ? 1834 LYS A CG    1 
ATOM   3046  C  CD    . LYS A 1 1834 ? 34.761  91.552  107.864 1.00 28.74  ? 1834 LYS A CD    1 
ATOM   3047  C  CE    . LYS A 1 1834 ? 35.286  91.070  109.211 1.00 39.30  ? 1834 LYS A CE    1 
ATOM   3048  N  NZ    . LYS A 1 1834 ? 35.985  89.759  109.092 1.00 54.44  ? 1834 LYS A NZ    1 
ATOM   3049  N  N     . SER A 1 1835 ? 36.613  96.761  109.150 1.00 9.69   ? 1835 SER A N     1 
ATOM   3050  C  CA    . SER A 1 1835 ? 37.441  97.905  108.795 1.00 12.40  ? 1835 SER A CA    1 
ATOM   3051  C  C     . SER A 1 1835 ? 38.915  97.548  108.945 1.00 11.42  ? 1835 SER A C     1 
ATOM   3052  O  O     . SER A 1 1835 ? 39.296  96.795  109.846 1.00 11.84  ? 1835 SER A O     1 
ATOM   3053  C  CB    . SER A 1 1835 ? 37.088  99.107  109.669 1.00 13.03  ? 1835 SER A CB    1 
ATOM   3054  O  OG    . SER A 1 1835 ? 37.421  98.872  111.023 1.00 18.56  ? 1835 SER A OG    1 
ATOM   3055  N  N     . PHE A 1 1836 ? 39.745  98.085  108.047 1.00 8.87   ? 1836 PHE A N     1 
ATOM   3056  C  CA    . PHE A 1 1836 ? 41.140  97.659  107.985 1.00 7.91   ? 1836 PHE A CA    1 
ATOM   3057  C  C     . PHE A 1 1836 ? 41.933  98.069  109.220 1.00 7.46   ? 1836 PHE A C     1 
ATOM   3058  O  O     . PHE A 1 1836 ? 42.821  97.325  109.651 1.00 6.46   ? 1836 PHE A O     1 
ATOM   3059  C  CB    . PHE A 1 1836 ? 41.806  98.197  106.720 1.00 4.65   ? 1836 PHE A CB    1 
ATOM   3060  C  CG    . PHE A 1 1836 ? 43.183  97.648  106.490 1.00 4.92   ? 1836 PHE A CG    1 
ATOM   3061  C  CD1   . PHE A 1 1836 ? 43.361  96.388  105.945 1.00 4.69   ? 1836 PHE A CD1   1 
ATOM   3062  C  CD2   . PHE A 1 1836 ? 44.301  98.397  106.812 1.00 4.05   ? 1836 PHE A CD2   1 
ATOM   3063  C  CE1   . PHE A 1 1836 ? 44.628  95.883  105.733 1.00 4.27   ? 1836 PHE A CE1   1 
ATOM   3064  C  CE2   . PHE A 1 1836 ? 45.569  97.897  106.602 1.00 3.46   ? 1836 PHE A CE2   1 
ATOM   3065  C  CZ    . PHE A 1 1836 ? 45.733  96.640  106.061 1.00 4.37   ? 1836 PHE A CZ    1 
ATOM   3066  N  N     . GLU A 1 1837 ? 41.638  99.233  109.806 1.00 7.79   ? 1837 GLU A N     1 
ATOM   3067  C  CA    . GLU A 1 1837 ? 42.399  99.675  110.973 1.00 11.25  ? 1837 GLU A CA    1 
ATOM   3068  C  C     . GLU A 1 1837 ? 42.203  98.743  112.166 1.00 8.84   ? 1837 GLU A C     1 
ATOM   3069  O  O     . GLU A 1 1837 ? 42.954  98.811  113.145 1.00 8.21   ? 1837 GLU A O     1 
ATOM   3070  C  CB    . GLU A 1 1837 ? 42.043  101.118 111.340 1.00 13.88  ? 1837 GLU A CB    1 
ATOM   3071  C  CG    . GLU A 1 1837 ? 40.572  101.378 111.565 1.00 17.36  ? 1837 GLU A CG    1 
ATOM   3072  C  CD    . GLU A 1 1837 ? 39.846  101.682 110.269 1.00 25.95  ? 1837 GLU A CD    1 
ATOM   3073  O  OE1   . GLU A 1 1837 ? 38.603  101.780 110.282 1.00 32.07  ? 1837 GLU A OE1   1 
ATOM   3074  O  OE2   . GLU A 1 1837 ? 40.526  101.842 109.234 1.00 20.45  ? 1837 GLU A OE2   1 
ATOM   3075  N  N     . TRP A 1 1838 ? 41.189  97.879  112.113 1.00 7.41   ? 1838 TRP A N     1 
ATOM   3076  C  CA    . TRP A 1 1838 ? 41.116  96.745  113.027 1.00 5.39   ? 1838 TRP A CA    1 
ATOM   3077  C  C     . TRP A 1 1838 ? 41.747  95.491  112.436 1.00 4.40   ? 1838 TRP A C     1 
ATOM   3078  O  O     . TRP A 1 1838 ? 42.425  94.745  113.150 1.00 4.26   ? 1838 TRP A O     1 
ATOM   3079  C  CB    . TRP A 1 1838 ? 39.664  96.454  113.407 1.00 5.70   ? 1838 TRP A CB    1 
ATOM   3080  C  CG    . TRP A 1 1838 ? 39.480  95.261  114.311 1.00 4.90   ? 1838 TRP A CG    1 
ATOM   3081  C  CD1   . TRP A 1 1838 ? 38.598  94.236  114.130 1.00 4.49   ? 1838 TRP A CD1   1 
ATOM   3082  C  CD2   . TRP A 1 1838 ? 40.172  94.979  115.539 1.00 3.32   ? 1838 TRP A CD2   1 
ATOM   3083  N  NE1   . TRP A 1 1838 ? 38.703  93.332  115.156 1.00 3.23   ? 1838 TRP A NE1   1 
ATOM   3084  C  CE2   . TRP A 1 1838 ? 39.660  93.763  116.035 1.00 3.54   ? 1838 TRP A CE2   1 
ATOM   3085  C  CE3   . TRP A 1 1838 ? 41.175  95.632  116.263 1.00 2.55   ? 1838 TRP A CE3   1 
ATOM   3086  C  CZ2   . TRP A 1 1838 ? 40.116  93.188  117.219 1.00 2.62   ? 1838 TRP A CZ2   1 
ATOM   3087  C  CZ3   . TRP A 1 1838 ? 41.628  95.058  117.437 1.00 2.18   ? 1838 TRP A CZ3   1 
ATOM   3088  C  CH2   . TRP A 1 1838 ? 41.100  93.847  117.902 1.00 3.35   ? 1838 TRP A CH2   1 
ATOM   3089  N  N     . LEU A 1 1839 ? 41.527  95.240  111.143 1.00 5.24   ? 1839 LEU A N     1 
ATOM   3090  C  CA    . LEU A 1 1839 ? 42.122  94.070  110.505 1.00 3.82   ? 1839 LEU A CA    1 
ATOM   3091  C  C     . LEU A 1 1839 ? 43.642  94.165  110.489 1.00 3.14   ? 1839 LEU A C     1 
ATOM   3092  O  O     . LEU A 1 1839 ? 44.336  93.147  110.595 1.00 4.03   ? 1839 LEU A O     1 
ATOM   3093  C  CB    . LEU A 1 1839 ? 41.578  93.910  109.085 1.00 5.53   ? 1839 LEU A CB    1 
ATOM   3094  C  CG    . LEU A 1 1839 ? 40.100  93.535  108.964 1.00 7.74   ? 1839 LEU A CG    1 
ATOM   3095  C  CD1   . LEU A 1 1839 ? 39.704  93.392  107.505 1.00 9.15   ? 1839 LEU A CD1   1 
ATOM   3096  C  CD2   . LEU A 1 1839 ? 39.804  92.255  109.729 1.00 7.02   ? 1839 LEU A CD2   1 
ATOM   3097  N  N     . SER A 1 1840 ? 44.178  95.381  110.361 1.00 3.86   ? 1840 SER A N     1 
ATOM   3098  C  CA    . SER A 1 1840 ? 45.626  95.559  110.403 1.00 3.75   ? 1840 SER A CA    1 
ATOM   3099  C  C     . SER A 1 1840 ? 46.196  95.183  111.764 1.00 3.11   ? 1840 SER A C     1 
ATOM   3100  O  O     . SER A 1 1840 ? 47.367  94.801  111.861 1.00 4.33   ? 1840 SER A O     1 
ATOM   3101  C  CB    . SER A 1 1840 ? 45.990  97.002  110.054 1.00 4.68   ? 1840 SER A CB    1 
ATOM   3102  O  OG    . SER A 1 1840 ? 45.265  97.920  110.854 1.00 5.47   ? 1840 SER A OG    1 
ATOM   3103  N  N     . GLN A 1 1841 ? 45.393  95.283  112.820 1.00 4.14   ? 1841 GLN A N     1 
ATOM   3104  C  CA    . GLN A 1 1841 ? 45.839  94.861  114.139 1.00 4.20   ? 1841 GLN A CA    1 
ATOM   3105  C  C     . GLN A 1 1841 ? 45.936  93.342  114.206 1.00 2.39   ? 1841 GLN A C     1 
ATOM   3106  O  O     . GLN A 1 1841 ? 45.240  92.618  113.489 1.00 2.63   ? 1841 GLN A O     1 
ATOM   3107  C  CB    . GLN A 1 1841 ? 44.884  95.368  115.220 1.00 3.32   ? 1841 GLN A CB    1 
ATOM   3108  C  CG    . GLN A 1 1841 ? 44.548  96.843  115.120 1.00 5.11   ? 1841 GLN A CG    1 
ATOM   3109  C  CD    . GLN A 1 1841 ? 45.780  97.716  114.999 1.00 6.31   ? 1841 GLN A CD    1 
ATOM   3110  O  OE1   . GLN A 1 1841 ? 46.634  97.730  115.884 1.00 7.44   ? 1841 GLN A OE1   1 
ATOM   3111  N  NE2   . GLN A 1 1841 ? 45.877  98.452  113.899 1.00 7.25   ? 1841 GLN A NE2   1 
ATOM   3112  N  N     . MET A 1 1842 ? 46.816  92.861  115.078 1.00 1.98   ? 1842 MET A N     1 
ATOM   3113  C  CA    . MET A 1 1842 ? 46.984  91.425  115.268 1.00 2.10   ? 1842 MET A CA    1 
ATOM   3114  C  C     . MET A 1 1842 ? 45.898  90.921  116.210 1.00 1.89   ? 1842 MET A C     1 
ATOM   3115  O  O     . MET A 1 1842 ? 45.815  91.353  117.364 1.00 2.09   ? 1842 MET A O     1 
ATOM   3116  C  CB    . MET A 1 1842 ? 48.376  91.124  115.809 1.00 1.72   ? 1842 MET A CB    1 
ATOM   3117  C  CG    . MET A 1 1842 ? 48.643  89.654  116.051 1.00 3.02   ? 1842 MET A CG    1 
ATOM   3118  S  SD    . MET A 1 1842 ? 50.374  89.358  116.441 1.00 13.40  ? 1842 MET A SD    1 
ATOM   3119  C  CE    . MET A 1 1842 ? 51.025  89.083  114.796 1.00 2.41   ? 1842 MET A CE    1 
ATOM   3120  N  N     . ARG A 1 1843 ? 45.068  90.010  115.722 1.00 1.50   ? 1843 ARG A N     1 
ATOM   3121  C  CA    . ARG A 1 1843 ? 43.879  89.552  116.418 1.00 1.97   ? 1843 ARG A CA    1 
ATOM   3122  C  C     . ARG A 1 1843 ? 43.976  88.059  116.707 1.00 1.50   ? 1843 ARG A C     1 
ATOM   3123  O  O     . ARG A 1 1843 ? 44.648  87.305  115.998 1.00 1.77   ? 1843 ARG A O     1 
ATOM   3124  C  CB    . ARG A 1 1843 ? 42.633  89.858  115.585 1.00 2.20   ? 1843 ARG A CB    1 
ATOM   3125  C  CG    . ARG A 1 1843 ? 42.368  91.345  115.434 1.00 2.37   ? 1843 ARG A CG    1 
ATOM   3126  C  CD    . ARG A 1 1843 ? 41.634  91.669  114.144 1.00 4.23   ? 1843 ARG A CD    1 
ATOM   3127  N  NE    . ARG A 1 1843 ? 42.478  91.491  112.969 1.00 3.43   ? 1843 ARG A NE    1 
ATOM   3128  C  CZ    . ARG A 1 1843 ? 42.231  90.629  111.993 1.00 3.40   ? 1843 ARG A CZ    1 
ATOM   3129  N  NH1   . ARG A 1 1843 ? 41.170  89.840  112.020 1.00 5.19   ? 1843 ARG A NH1   1 
ATOM   3130  N  NH2   . ARG A 1 1843 ? 43.069  90.559  110.963 1.00 2.88   ? 1843 ARG A NH2   1 
ATOM   3131  N  N     . PHE A 1 1844 ? 43.280  87.638  117.761 1.00 2.22   ? 1844 PHE A N     1 
ATOM   3132  C  CA    . PHE A 1 1844 ? 43.413  86.294  118.313 1.00 2.48   ? 1844 PHE A CA    1 
ATOM   3133  C  C     . PHE A 1 1844 ? 42.020  85.702  118.473 1.00 3.15   ? 1844 PHE A C     1 
ATOM   3134  O  O     . PHE A 1 1844 ? 41.249  86.150  119.327 1.00 4.92   ? 1844 PHE A O     1 
ATOM   3135  C  CB    . PHE A 1 1844 ? 44.143  86.328  119.656 1.00 1.71   ? 1844 PHE A CB    1 
ATOM   3136  C  CG    . PHE A 1 1844 ? 45.515  86.936  119.588 1.00 2.01   ? 1844 PHE A CG    1 
ATOM   3137  C  CD1   . PHE A 1 1844 ? 45.680  88.311  119.643 1.00 2.24   ? 1844 PHE A CD1   1 
ATOM   3138  C  CD2   . PHE A 1 1844 ? 46.638  86.137  119.477 1.00 1.59   ? 1844 PHE A CD2   1 
ATOM   3139  C  CE1   . PHE A 1 1844 ? 46.939  88.876  119.581 1.00 1.77   ? 1844 PHE A CE1   1 
ATOM   3140  C  CE2   . PHE A 1 1844 ? 47.900  86.696  119.416 1.00 1.73   ? 1844 PHE A CE2   1 
ATOM   3141  C  CZ    . PHE A 1 1844 ? 48.050  88.067  119.469 1.00 1.33   ? 1844 PHE A CZ    1 
ATOM   3142  N  N     . TYR A 1 1845 ? 41.698  84.698  117.663 1.00 3.69   ? 1845 TYR A N     1 
ATOM   3143  C  CA    . TYR A 1 1845 ? 40.400  84.039  117.719 1.00 4.38   ? 1845 TYR A CA    1 
ATOM   3144  C  C     . TYR A 1 1845 ? 40.571  82.623  118.249 1.00 6.55   ? 1845 TYR A C     1 
ATOM   3145  O  O     . TYR A 1 1845 ? 41.310  81.822  117.669 1.00 6.07   ? 1845 TYR A O     1 
ATOM   3146  C  CB    . TYR A 1 1845 ? 39.734  84.021  116.342 1.00 5.49   ? 1845 TYR A CB    1 
ATOM   3147  C  CG    . TYR A 1 1845 ? 39.661  85.381  115.688 1.00 12.36  ? 1845 TYR A CG    1 
ATOM   3148  C  CD1   . TYR A 1 1845 ? 40.695  85.848  114.886 1.00 7.92   ? 1845 TYR A CD1   1 
ATOM   3149  C  CD2   . TYR A 1 1845 ? 38.556  86.202  115.874 1.00 13.28  ? 1845 TYR A CD2   1 
ATOM   3150  C  CE1   . TYR A 1 1845 ? 40.629  87.092  114.291 1.00 7.64   ? 1845 TYR A CE1   1 
ATOM   3151  C  CE2   . TYR A 1 1845 ? 38.481  87.444  115.282 1.00 12.26  ? 1845 TYR A CE2   1 
ATOM   3152  C  CZ    . TYR A 1 1845 ? 39.519  87.885  114.491 1.00 10.53  ? 1845 TYR A CZ    1 
ATOM   3153  O  OH    . TYR A 1 1845 ? 39.447  89.125  113.899 1.00 14.07  ? 1845 TYR A OH    1 
ATOM   3154  N  N     . PHE A 1 1846 ? 39.882  82.316  119.344 1.00 6.57   ? 1846 PHE A N     1 
ATOM   3155  C  CA    . PHE A 1 1846 ? 39.973  81.014  119.991 1.00 8.41   ? 1846 PHE A CA    1 
ATOM   3156  C  C     . PHE A 1 1846 ? 38.631  80.312  119.857 1.00 11.67  ? 1846 PHE A C     1 
ATOM   3157  O  O     . PHE A 1 1846 ? 37.596  80.864  120.245 1.00 15.95  ? 1846 PHE A O     1 
ATOM   3158  C  CB    . PHE A 1 1846 ? 40.374  81.161  121.462 1.00 10.05  ? 1846 PHE A CB    1 
ATOM   3159  C  CG    . PHE A 1 1846 ? 40.565  79.852  122.175 1.00 11.25  ? 1846 PHE A CG    1 
ATOM   3160  C  CD1   . PHE A 1 1846 ? 39.506  79.236  122.821 1.00 12.86  ? 1846 PHE A CD1   1 
ATOM   3161  C  CD2   . PHE A 1 1846 ? 41.806  79.239  122.198 1.00 10.14  ? 1846 PHE A CD2   1 
ATOM   3162  C  CE1   . PHE A 1 1846 ? 39.682  78.035  123.476 1.00 14.31  ? 1846 PHE A CE1   1 
ATOM   3163  C  CE2   . PHE A 1 1846 ? 41.987  78.038  122.851 1.00 11.20  ? 1846 PHE A CE2   1 
ATOM   3164  C  CZ    . PHE A 1 1846 ? 40.924  77.436  123.491 1.00 13.04  ? 1846 PHE A CZ    1 
ATOM   3165  N  N     . ASP A 1 1847 ? 38.650  79.099  119.309 1.00 15.93  ? 1847 ASP A N     1 
ATOM   3166  C  CA    . ASP A 1 1847 ? 37.436  78.318  119.099 1.00 21.10  ? 1847 ASP A CA    1 
ATOM   3167  C  C     . ASP A 1 1847 ? 37.536  77.030  119.906 1.00 25.80  ? 1847 ASP A C     1 
ATOM   3168  O  O     . ASP A 1 1847 ? 38.140  76.051  119.439 1.00 28.52  ? 1847 ASP A O     1 
ATOM   3169  C  CB    . ASP A 1 1847 ? 37.245  78.010  117.609 1.00 18.41  ? 1847 ASP A CB    1 
ATOM   3170  C  CG    . ASP A 1 1847 ? 35.989  77.198  117.325 1.00 33.69  ? 1847 ASP A CG    1 
ATOM   3171  O  OD1   . ASP A 1 1847 ? 35.202  76.937  118.259 1.00 37.34  ? 1847 ASP A OD1   1 
ATOM   3172  O  OD2   . ASP A 1 1847 ? 35.791  76.816  116.153 1.00 44.04  ? 1847 ASP A OD2   1 
ATOM   3173  N  N     . PRO A 1 1848 ? 36.973  76.976  121.115 1.00 27.32  ? 1848 PRO A N     1 
ATOM   3174  C  CA    . PRO A 1 1848 ? 37.035  75.731  121.899 1.00 28.96  ? 1848 PRO A CA    1 
ATOM   3175  C  C     . PRO A 1 1848 ? 36.312  74.565  121.248 1.00 36.38  ? 1848 PRO A C     1 
ATOM   3176  O  O     . PRO A 1 1848 ? 36.633  73.410  121.554 1.00 35.47  ? 1848 PRO A O     1 
ATOM   3177  C  CB    . PRO A 1 1848 ? 36.381  76.125  123.230 1.00 30.51  ? 1848 PRO A CB    1 
ATOM   3178  C  CG    . PRO A 1 1848 ? 35.488  77.272  122.877 1.00 28.17  ? 1848 PRO A CG    1 
ATOM   3179  C  CD    . PRO A 1 1848 ? 36.235  78.035  121.823 1.00 25.66  ? 1848 PRO A CD    1 
ATOM   3180  N  N     . LYS A 1 1849 ? 35.348  74.826  120.362 1.00 35.21  ? 1849 LYS A N     1 
ATOM   3181  C  CA    . LYS A 1 1849 ? 34.627  73.744  119.702 1.00 36.82  ? 1849 LYS A CA    1 
ATOM   3182  C  C     . LYS A 1 1849 ? 35.494  72.995  118.698 1.00 34.31  ? 1849 LYS A C     1 
ATOM   3183  O  O     . LYS A 1 1849 ? 35.087  71.930  118.221 1.00 43.69  ? 1849 LYS A O     1 
ATOM   3184  C  CB    . LYS A 1 1849 ? 33.379  74.290  119.006 1.00 40.88  ? 1849 LYS A CB    1 
ATOM   3185  C  CG    . LYS A 1 1849 ? 32.405  74.986  119.941 1.00 50.90  ? 1849 LYS A CG    1 
ATOM   3186  C  CD    . LYS A 1 1849 ? 31.172  75.467  119.196 1.00 58.44  ? 1849 LYS A CD    1 
ATOM   3187  C  CE    . LYS A 1 1849 ? 30.178  76.121  120.141 1.00 65.76  ? 1849 LYS A CE    1 
ATOM   3188  N  NZ    . LYS A 1 1849 ? 28.949  76.569  119.431 1.00 65.05  ? 1849 LYS A NZ    1 
ATOM   3189  N  N     . GLN A 1 1850 ? 36.665  73.530  118.357 1.00 33.55  ? 1850 GLN A N     1 
ATOM   3190  C  CA    . GLN A 1 1850 ? 37.563  72.853  117.431 1.00 35.73  ? 1850 GLN A CA    1 
ATOM   3191  C  C     . GLN A 1 1850 ? 38.028  71.525  118.015 1.00 36.69  ? 1850 GLN A C     1 
ATOM   3192  O  O     . GLN A 1 1850 ? 38.454  71.456  119.171 1.00 34.68  ? 1850 GLN A O     1 
ATOM   3193  C  CB    . GLN A 1 1850 ? 38.763  73.751  117.121 1.00 27.76  ? 1850 GLN A CB    1 
ATOM   3194  C  CG    . GLN A 1 1850 ? 39.834  73.099  116.265 1.00 29.33  ? 1850 GLN A CG    1 
ATOM   3195  C  CD    . GLN A 1 1850 ? 39.384  72.864  114.837 1.00 37.45  ? 1850 GLN A CD    1 
ATOM   3196  O  OE1   . GLN A 1 1850 ? 38.447  73.501  114.356 1.00 42.61  ? 1850 GLN A OE1   1 
ATOM   3197  N  NE2   . GLN A 1 1850 ? 40.053  71.946  114.150 1.00 40.21  ? 1850 GLN A NE2   1 
ATOM   3198  N  N     . THR A 1 1851 ? 37.938  70.467  117.206 1.00 41.08  ? 1851 THR A N     1 
ATOM   3199  C  CA    . THR A 1 1851 ? 38.279  69.134  117.694 1.00 38.65  ? 1851 THR A CA    1 
ATOM   3200  C  C     . THR A 1 1851 ? 39.774  69.001  117.960 1.00 36.87  ? 1851 THR A C     1 
ATOM   3201  O  O     . THR A 1 1851 ? 40.179  68.440  118.984 1.00 37.41  ? 1851 THR A O     1 
ATOM   3202  C  CB    . THR A 1 1851 ? 37.818  68.073  116.694 1.00 49.70  ? 1851 THR A CB    1 
ATOM   3203  O  OG1   . THR A 1 1851 ? 38.492  68.266  115.444 1.00 53.09  ? 1851 THR A OG1   1 
ATOM   3204  C  CG2   . THR A 1 1851 ? 36.316  68.167  116.474 1.00 48.12  ? 1851 THR A CG2   1 
ATOM   3205  N  N     . ASP A 1 1852 ? 40.606  69.507  117.054 1.00 34.14  ? 1852 ASP A N     1 
ATOM   3206  C  CA    . ASP A 1 1852 ? 42.051  69.449  117.231 1.00 28.49  ? 1852 ASP A CA    1 
ATOM   3207  C  C     . ASP A 1 1852 ? 42.473  70.567  118.177 1.00 28.85  ? 1852 ASP A C     1 
ATOM   3208  O  O     . ASP A 1 1852 ? 42.195  71.743  117.921 1.00 27.68  ? 1852 ASP A O     1 
ATOM   3209  C  CB    . ASP A 1 1852 ? 42.756  69.571  115.880 1.00 23.42  ? 1852 ASP A CB    1 
ATOM   3210  C  CG    . ASP A 1 1852 ? 44.272  69.464  115.988 1.00 30.88  ? 1852 ASP A CG    1 
ATOM   3211  O  OD1   . ASP A 1 1852 ? 44.796  69.284  117.108 1.00 29.57  ? 1852 ASP A OD1   1 
ATOM   3212  O  OD2   . ASP A 1 1852 ? 44.943  69.558  114.940 1.00 27.72  ? 1852 ASP A OD2   1 
ATOM   3213  N  N     . VAL A 1 1853 ? 43.143  70.199  119.272 1.00 22.14  ? 1853 VAL A N     1 
ATOM   3214  C  CA    . VAL A 1 1853 ? 43.537  71.188  120.271 1.00 19.55  ? 1853 VAL A CA    1 
ATOM   3215  C  C     . VAL A 1 1853 ? 44.557  72.164  119.703 1.00 16.23  ? 1853 VAL A C     1 
ATOM   3216  O  O     . VAL A 1 1853 ? 44.589  73.338  120.092 1.00 17.24  ? 1853 VAL A O     1 
ATOM   3217  C  CB    . VAL A 1 1853 ? 44.069  70.485  121.536 1.00 21.29  ? 1853 VAL A CB    1 
ATOM   3218  C  CG1   . VAL A 1 1853 ? 42.925  69.833  122.296 1.00 23.20  ? 1853 VAL A CG1   1 
ATOM   3219  C  CG2   . VAL A 1 1853 ? 45.129  69.456  121.172 1.00 18.95  ? 1853 VAL A CG2   1 
ATOM   3220  N  N     . LEU A 1 1854 ? 45.402  71.706  118.780 1.00 14.06  ? 1854 LEU A N     1 
ATOM   3221  C  CA    . LEU A 1 1854 ? 46.430  72.552  118.190 1.00 12.18  ? 1854 LEU A CA    1 
ATOM   3222  C  C     . LEU A 1 1854 ? 45.873  73.598  117.232 1.00 13.70  ? 1854 LEU A C     1 
ATOM   3223  O  O     . LEU A 1 1854 ? 46.621  74.488  116.815 1.00 14.12  ? 1854 LEU A O     1 
ATOM   3224  C  CB    . LEU A 1 1854 ? 47.460  71.688  117.458 1.00 12.62  ? 1854 LEU A CB    1 
ATOM   3225  C  CG    . LEU A 1 1854 ? 48.312  70.766  118.333 1.00 10.15  ? 1854 LEU A CG    1 
ATOM   3226  C  CD1   . LEU A 1 1854 ? 49.300  69.983  117.486 1.00 7.56   ? 1854 LEU A CD1   1 
ATOM   3227  C  CD2   . LEU A 1 1854 ? 49.035  71.564  119.408 1.00 5.54   ? 1854 LEU A CD2   1 
ATOM   3228  N  N     . GLN A 1 1855 ? 44.591  73.516  116.872 1.00 16.96  ? 1855 GLN A N     1 
ATOM   3229  C  CA    . GLN A 1 1855 ? 43.993  74.438  115.918 1.00 13.86  ? 1855 GLN A CA    1 
ATOM   3230  C  C     . GLN A 1 1855 ? 42.915  75.329  116.521 1.00 11.92  ? 1855 GLN A C     1 
ATOM   3231  O  O     . GLN A 1 1855 ? 42.242  76.046  115.773 1.00 15.19  ? 1855 GLN A O     1 
ATOM   3232  C  CB    . GLN A 1 1855 ? 43.402  73.665  114.731 1.00 19.87  ? 1855 GLN A CB    1 
ATOM   3233  C  CG    . GLN A 1 1855 ? 44.428  72.903  113.908 1.00 18.21  ? 1855 GLN A CG    1 
ATOM   3234  C  CD    . GLN A 1 1855 ? 45.632  73.750  113.550 1.00 24.19  ? 1855 GLN A CD    1 
ATOM   3235  O  OE1   . GLN A 1 1855 ? 46.765  73.416  113.896 1.00 28.92  ? 1855 GLN A OE1   1 
ATOM   3236  N  NE2   . GLN A 1 1855 ? 45.393  74.854  112.851 1.00 26.45  ? 1855 GLN A NE2   1 
ATOM   3237  N  N     . GLN A 1 1856 ? 42.728  75.307  117.843 1.00 11.65  ? 1856 GLN A N     1 
ATOM   3238  C  CA    . GLN A 1 1856 ? 41.683  76.127  118.448 1.00 12.87  ? 1856 GLN A CA    1 
ATOM   3239  C  C     . GLN A 1 1856 ? 42.017  77.612  118.381 1.00 9.59   ? 1856 GLN A C     1 
ATOM   3240  O  O     . GLN A 1 1856 ? 41.108  78.449  118.360 1.00 10.47  ? 1856 GLN A O     1 
ATOM   3241  C  CB    . GLN A 1 1856 ? 41.448  75.702  119.897 1.00 12.25  ? 1856 GLN A CB    1 
ATOM   3242  C  CG    . GLN A 1 1856 ? 41.211  74.213  120.078 1.00 17.09  ? 1856 GLN A CG    1 
ATOM   3243  C  CD    . GLN A 1 1856 ? 40.648  73.877  121.444 1.00 20.44  ? 1856 GLN A CD    1 
ATOM   3244  O  OE1   . GLN A 1 1856 ? 41.231  74.224  122.471 1.00 19.98  ? 1856 GLN A OE1   1 
ATOM   3245  N  NE2   . GLN A 1 1856 ? 39.508  73.198  121.463 1.00 24.83  ? 1856 GLN A NE2   1 
ATOM   3246  N  N     . LEU A 1 1857 ? 43.300  77.959  118.344 1.00 6.53   ? 1857 LEU A N     1 
ATOM   3247  C  CA    . LEU A 1 1857 ? 43.736  79.348  118.327 1.00 4.53   ? 1857 LEU A CA    1 
ATOM   3248  C  C     . LEU A 1 1857 ? 44.212  79.727  116.931 1.00 4.29   ? 1857 LEU A C     1 
ATOM   3249  O  O     . LEU A 1 1857 ? 45.017  79.010  116.328 1.00 5.03   ? 1857 LEU A O     1 
ATOM   3250  C  CB    . LEU A 1 1857 ? 44.854  79.582  119.343 1.00 2.86   ? 1857 LEU A CB    1 
ATOM   3251  C  CG    . LEU A 1 1857 ? 45.567  80.934  119.255 1.00 2.20   ? 1857 LEU A CG    1 
ATOM   3252  C  CD1   . LEU A 1 1857 ? 44.586  82.088  119.433 1.00 2.45   ? 1857 LEU A CD1   1 
ATOM   3253  C  CD2   . LEU A 1 1857 ? 46.690  81.018  120.267 1.00 2.68   ? 1857 LEU A CD2   1 
ATOM   3254  N  N     . SER A 1 1858 ? 43.715  80.854  116.426 1.00 3.54   ? 1858 SER A N     1 
ATOM   3255  C  CA    . SER A 1 1858 ? 44.128  81.409  115.144 1.00 2.79   ? 1858 SER A CA    1 
ATOM   3256  C  C     . SER A 1 1858 ? 44.571  82.848  115.363 1.00 2.48   ? 1858 SER A C     1 
ATOM   3257  O  O     . SER A 1 1858 ? 43.919  83.597  116.101 1.00 2.41   ? 1858 SER A O     1 
ATOM   3258  C  CB    . SER A 1 1858 ? 42.993  81.341  114.122 1.00 4.81   ? 1858 SER A CB    1 
ATOM   3259  O  OG    . SER A 1 1858 ? 43.379  81.930  112.893 1.00 9.96   ? 1858 SER A OG    1 
ATOM   3260  N  N     . ILE A 1 1859 ? 45.676  83.229  114.730 1.00 2.86   ? 1859 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 1859 ? 46.232  84.571  114.851 1.00 2.15   ? 1859 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 1859 ? 46.176  85.224  113.478 1.00 2.72   ? 1859 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 1859 ? 46.767  84.718  112.518 1.00 3.41   ? 1859 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 1859 ? 47.668  84.528  115.390 1.00 2.24   ? 1859 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 1859 ? 47.667  84.026  116.836 1.00 2.04   ? 1859 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 1859 ? 48.308  85.901  115.285 1.00 1.80   ? 1859 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 1859 ? 48.914  83.263  117.224 1.00 1.75   ? 1859 ILE A CD1   1 
ATOM   3268  N  N     . GLN A 1 1860 ? 45.476  86.348  113.377 1.00 3.86   ? 1860 GLN A N     1 
ATOM   3269  C  CA    . GLN A 1 1860 ? 45.206  86.974  112.090 1.00 2.93   ? 1860 GLN A CA    1 
ATOM   3270  C  C     . GLN A 1 1860 ? 45.691  88.415  112.088 1.00 1.96   ? 1860 GLN A C     1 
ATOM   3271  O  O     . GLN A 1 1860 ? 45.389  89.180  113.006 1.00 1.77   ? 1860 GLN A O     1 
ATOM   3272  C  CB    . GLN A 1 1860 ? 43.712  86.907  111.761 1.00 3.99   ? 1860 GLN A CB    1 
ATOM   3273  C  CG    . GLN A 1 1860 ? 43.147  85.496  111.814 1.00 6.54   ? 1860 GLN A CG    1 
ATOM   3274  C  CD    . GLN A 1 1860 ? 41.667  85.438  111.502 1.00 12.56  ? 1860 GLN A CD    1 
ATOM   3275  O  OE1   . GLN A 1 1860 ? 41.040  86.458  111.221 1.00 19.78  ? 1860 GLN A OE1   1 
ATOM   3276  N  NE2   . GLN A 1 1860 ? 41.100  84.240  111.552 1.00 12.91  ? 1860 GLN A NE2   1 
ATOM   3277  N  N     . MET A 1 1861 ? 46.441  88.779  111.052 1.00 2.52   ? 1861 MET A N     1 
ATOM   3278  C  CA    . MET A 1 1861 ? 46.891  90.150  110.844 1.00 2.25   ? 1861 MET A CA    1 
ATOM   3279  C  C     . MET A 1 1861 ? 46.659  90.504  109.384 1.00 2.97   ? 1861 MET A C     1 
ATOM   3280  O  O     . MET A 1 1861 ? 47.274  89.905  108.496 1.00 3.10   ? 1861 MET A O     1 
ATOM   3281  C  CB    . MET A 1 1861 ? 48.367  90.315  111.217 1.00 1.90   ? 1861 MET A CB    1 
ATOM   3282  C  CG    . MET A 1 1861 ? 48.797  91.758  111.428 1.00 1.92   ? 1861 MET A CG    1 
ATOM   3283  S  SD    . MET A 1 1861 ? 50.387  91.897  112.264 1.00 5.96   ? 1861 MET A SD    1 
ATOM   3284  C  CE    . MET A 1 1861 ? 50.368  93.623  112.740 1.00 1.75   ? 1861 MET A CE    1 
ATOM   3285  N  N     . ALA A 1 1862 ? 45.779  91.479  109.142 1.00 3.88   ? 1862 ALA A N     1 
ATOM   3286  C  CA    . ALA A 1 1862 ? 45.316  91.847  107.799 1.00 3.45   ? 1862 ALA A CA    1 
ATOM   3287  C  C     . ALA A 1 1862 ? 44.720  90.597  107.163 1.00 4.40   ? 1862 ALA A C     1 
ATOM   3288  O  O     . ALA A 1 1862 ? 43.765  90.038  107.729 1.00 5.12   ? 1862 ALA A O     1 
ATOM   3289  C  CB    . ALA A 1 1862 ? 46.458  92.513  107.027 1.00 2.97   ? 1862 ALA A CB    1 
ATOM   3290  N  N     . ASN A 1 1863 ? 45.224  90.122  106.024 1.00 4.64   ? 1863 ASN A N     1 
ATOM   3291  C  CA    . ASN A 1 1863 ? 44.739  88.882  105.434 1.00 5.04   ? 1863 ASN A CA    1 
ATOM   3292  C  C     . ASN A 1 1863 ? 45.557  87.665  105.842 1.00 7.81   ? 1863 ASN A C     1 
ATOM   3293  O  O     . ASN A 1 1863 ? 45.163  86.539  105.523 1.00 9.26   ? 1863 ASN A O     1 
ATOM   3294  C  CB    . ASN A 1 1863 ? 44.725  88.989  103.904 1.00 4.64   ? 1863 ASN A CB    1 
ATOM   3295  C  CG    . ASN A 1 1863 ? 46.045  89.477  103.341 1.00 6.82   ? 1863 ASN A CG    1 
ATOM   3296  O  OD1   . ASN A 1 1863 ? 46.446  90.618  103.569 1.00 6.93   ? 1863 ASN A OD1   1 
ATOM   3297  N  ND2   . ASN A 1 1863 ? 46.728  88.613  102.601 1.00 6.62   ? 1863 ASN A ND2   1 
ATOM   3298  N  N     . ALA A 1 1864 ? 46.674  87.864  106.536 1.00 5.54   ? 1864 ALA A N     1 
ATOM   3299  C  CA    . ALA A 1 1864 ? 47.526  86.755  106.945 1.00 4.58   ? 1864 ALA A CA    1 
ATOM   3300  C  C     . ALA A 1 1864 ? 46.901  86.020  108.125 1.00 4.37   ? 1864 ALA A C     1 
ATOM   3301  O  O     . ALA A 1 1864 ? 46.478  86.644  109.102 1.00 3.86   ? 1864 ALA A O     1 
ATOM   3302  C  CB    . ALA A 1 1864 ? 48.917  87.267  107.306 1.00 2.53   ? 1864 ALA A CB    1 
ATOM   3303  N  N     . LYS A 1 1865 ? 46.844  84.694  108.033 1.00 4.87   ? 1865 LYS A N     1 
ATOM   3304  C  CA    . LYS A 1 1865 ? 46.325  83.845  109.095 1.00 5.31   ? 1865 LYS A CA    1 
ATOM   3305  C  C     . LYS A 1 1865 ? 47.377  82.813  109.473 1.00 4.35   ? 1865 LYS A C     1 
ATOM   3306  O  O     . LYS A 1 1865 ? 48.042  82.244  108.601 1.00 7.86   ? 1865 LYS A O     1 
ATOM   3307  C  CB    . LYS A 1 1865 ? 45.031  83.146  108.668 1.00 5.40   ? 1865 LYS A CB    1 
ATOM   3308  C  CG    . LYS A 1 1865 ? 43.865  84.090  108.437 1.00 8.85   ? 1865 LYS A CG    1 
ATOM   3309  C  CD    . LYS A 1 1865 ? 42.612  83.335  108.028 1.00 22.63  ? 1865 LYS A CD    1 
ATOM   3310  C  CE    . LYS A 1 1865 ? 41.426  84.274  107.881 1.00 22.84  ? 1865 LYS A CE    1 
ATOM   3311  N  NZ    . LYS A 1 1865 ? 41.605  85.218  106.743 1.00 25.74  ? 1865 LYS A NZ    1 
ATOM   3312  N  N     . PHE A 1 1866 ? 47.526  82.574  110.773 1.00 2.81   ? 1866 PHE A N     1 
ATOM   3313  C  CA    . PHE A 1 1866 ? 48.543  81.670  111.282 1.00 3.27   ? 1866 PHE A CA    1 
ATOM   3314  C  C     . PHE A 1 1866 ? 47.958  80.806  112.386 1.00 2.89   ? 1866 PHE A C     1 
ATOM   3315  O  O     . PHE A 1 1866 ? 47.039  81.217  113.103 1.00 3.62   ? 1866 PHE A O     1 
ATOM   3316  C  CB    . PHE A 1 1866 ? 49.758  82.431  111.831 1.00 3.15   ? 1866 PHE A CB    1 
ATOM   3317  C  CG    . PHE A 1 1866 ? 50.391  83.363  110.843 1.00 3.69   ? 1866 PHE A CG    1 
ATOM   3318  C  CD1   . PHE A 1 1866 ? 51.386  82.919  109.991 1.00 4.00   ? 1866 PHE A CD1   1 
ATOM   3319  C  CD2   . PHE A 1 1866 ? 49.999  84.690  110.777 1.00 2.49   ? 1866 PHE A CD2   1 
ATOM   3320  C  CE1   . PHE A 1 1866 ? 51.971  83.778  109.085 1.00 7.06   ? 1866 PHE A CE1   1 
ATOM   3321  C  CE2   . PHE A 1 1866 ? 50.581  85.552  109.875 1.00 2.92   ? 1866 PHE A CE2   1 
ATOM   3322  C  CZ    . PHE A 1 1866 ? 51.568  85.097  109.027 1.00 4.24   ? 1866 PHE A CZ    1 
ATOM   3323  N  N     . ASN A 1 1867 ? 48.507  79.604  112.517 1.00 3.84   ? 1867 ASN A N     1 
ATOM   3324  C  CA    . ASN A 1 1867 ? 48.232  78.729  113.644 1.00 3.71   ? 1867 ASN A CA    1 
ATOM   3325  C  C     . ASN A 1 1867 ? 49.339  78.887  114.675 1.00 2.65   ? 1867 ASN A C     1 
ATOM   3326  O  O     . ASN A 1 1867 ? 50.509  79.056  114.321 1.00 3.65   ? 1867 ASN A O     1 
ATOM   3327  C  CB    . ASN A 1 1867 ? 48.122  77.269  113.191 1.00 5.66   ? 1867 ASN A CB    1 
ATOM   3328  C  CG    . ASN A 1 1867 ? 49.456  76.685  112.744 1.00 13.29  ? 1867 ASN A CG    1 
ATOM   3329  O  OD1   . ASN A 1 1867 ? 50.320  76.367  113.562 1.00 10.59  ? 1867 ASN A OD1   1 
ATOM   3330  N  ND2   . ASN A 1 1867 ? 49.628  76.549  111.435 1.00 18.49  ? 1867 ASN A ND2   1 
ATOM   3331  N  N     . TYR A 1 1868 ? 48.967  78.853  115.949 1.00 1.86   ? 1868 TYR A N     1 
ATOM   3332  C  CA    . TYR A 1 1868 ? 49.966  78.935  117.002 1.00 1.54   ? 1868 TYR A CA    1 
ATOM   3333  C  C     . TYR A 1 1868 ? 50.788  77.652  117.021 1.00 2.06   ? 1868 TYR A C     1 
ATOM   3334  O  O     . TYR A 1 1868 ? 50.235  76.549  117.017 1.00 2.72   ? 1868 TYR A O     1 
ATOM   3335  C  CB    . TYR A 1 1868 ? 49.295  79.178  118.353 1.00 1.57   ? 1868 TYR A CB    1 
ATOM   3336  C  CG    . TYR A 1 1868 ? 50.238  79.669  119.424 1.00 1.56   ? 1868 TYR A CG    1 
ATOM   3337  C  CD1   . TYR A 1 1868 ? 50.644  80.997  119.456 1.00 1.04   ? 1868 TYR A CD1   1 
ATOM   3338  C  CD2   . TYR A 1 1868 ? 50.705  78.817  120.415 1.00 1.04   ? 1868 TYR A CD2   1 
ATOM   3339  C  CE1   . TYR A 1 1868 ? 51.502  81.458  120.430 1.00 0.98   ? 1868 TYR A CE1   1 
ATOM   3340  C  CE2   . TYR A 1 1868 ? 51.563  79.270  121.397 1.00 0.99   ? 1868 TYR A CE2   1 
ATOM   3341  C  CZ    . TYR A 1 1868 ? 51.957  80.592  121.399 1.00 1.57   ? 1868 TYR A CZ    1 
ATOM   3342  O  OH    . TYR A 1 1868 ? 52.810  81.052  122.371 1.00 1.73   ? 1868 TYR A OH    1 
ATOM   3343  N  N     . GLY A 1 1869 ? 52.114  77.798  117.019 1.00 1.28   ? 1869 GLY A N     1 
ATOM   3344  C  CA    . GLY A 1 1869 ? 52.977  76.633  116.946 1.00 1.81   ? 1869 GLY A CA    1 
ATOM   3345  C  C     . GLY A 1 1869 ? 53.049  75.844  118.233 1.00 2.49   ? 1869 GLY A C     1 
ATOM   3346  O  O     . GLY A 1 1869 ? 53.391  74.658  118.214 1.00 1.91   ? 1869 GLY A O     1 
ATOM   3347  N  N     . PHE A 1 1870 ? 52.737  76.484  119.360 1.00 2.46   ? 1870 PHE A N     1 
ATOM   3348  C  CA    . PHE A 1 1870 ? 52.737  75.876  120.686 1.00 2.09   ? 1870 PHE A CA    1 
ATOM   3349  C  C     . PHE A 1 1870 ? 54.102  75.330  121.084 1.00 2.48   ? 1870 PHE A C     1 
ATOM   3350  O  O     . PHE A 1 1870 ? 54.188  74.397  121.888 1.00 2.95   ? 1870 PHE A O     1 
ATOM   3351  C  CB    . PHE A 1 1870 ? 51.673  74.777  120.799 1.00 1.75   ? 1870 PHE A CB    1 
ATOM   3352  C  CG    . PHE A 1 1870 ? 50.268  75.304  120.817 1.00 2.13   ? 1870 PHE A CG    1 
ATOM   3353  C  CD1   . PHE A 1 1870 ? 49.737  75.867  121.963 1.00 1.41   ? 1870 PHE A CD1   1 
ATOM   3354  C  CD2   . PHE A 1 1870 ? 49.478  75.237  119.683 1.00 2.43   ? 1870 PHE A CD2   1 
ATOM   3355  C  CE1   . PHE A 1 1870 ? 48.447  76.357  121.973 1.00 1.53   ? 1870 PHE A CE1   1 
ATOM   3356  C  CE2   . PHE A 1 1870 ? 48.187  75.722  119.690 1.00 2.34   ? 1870 PHE A CE2   1 
ATOM   3357  C  CZ    . PHE A 1 1870 ? 47.671  76.282  120.837 1.00 2.23   ? 1870 PHE A CZ    1 
ATOM   3358  N  N     . GLU A 1 1871 ? 55.173  75.881  120.520 1.00 2.94   ? 1871 GLU A N     1 
ATOM   3359  C  CA    . GLU A 1 1871 ? 56.511  75.611  121.026 1.00 2.64   ? 1871 GLU A CA    1 
ATOM   3360  C  C     . GLU A 1 1871 ? 56.649  76.212  122.417 1.00 3.40   ? 1871 GLU A C     1 
ATOM   3361  O  O     . GLU A 1 1871 ? 56.263  77.363  122.644 1.00 6.04   ? 1871 GLU A O     1 
ATOM   3362  C  CB    . GLU A 1 1871 ? 57.561  76.203  120.085 1.00 3.18   ? 1871 GLU A CB    1 
ATOM   3363  C  CG    . GLU A 1 1871 ? 59.006  75.996  120.521 1.00 4.29   ? 1871 GLU A CG    1 
ATOM   3364  C  CD    . GLU A 1 1871 ? 59.512  74.586  120.270 1.00 6.73   ? 1871 GLU A CD    1 
ATOM   3365  O  OE1   . GLU A 1 1871 ? 58.744  73.755  119.742 1.00 8.26   ? 1871 GLU A OE1   1 
ATOM   3366  O  OE2   . GLU A 1 1871 ? 60.683  74.310  120.603 1.00 7.10   ? 1871 GLU A OE2   1 
ATOM   3367  N  N     . TYR A 1 1872 ? 57.187  75.438  123.356 1.00 3.92   ? 1872 TYR A N     1 
ATOM   3368  C  CA    . TYR A 1 1872 ? 57.406  75.973  124.693 1.00 3.53   ? 1872 TYR A CA    1 
ATOM   3369  C  C     . TYR A 1 1872 ? 58.500  77.028  124.647 1.00 4.80   ? 1872 TYR A C     1 
ATOM   3370  O  O     . TYR A 1 1872 ? 59.613  76.763  124.181 1.00 6.83   ? 1872 TYR A O     1 
ATOM   3371  C  CB    . TYR A 1 1872 ? 57.782  74.867  125.675 1.00 4.13   ? 1872 TYR A CB    1 
ATOM   3372  C  CG    . TYR A 1 1872 ? 57.954  75.394  127.080 1.00 4.99   ? 1872 TYR A CG    1 
ATOM   3373  C  CD1   . TYR A 1 1872 ? 56.967  76.171  127.672 1.00 4.96   ? 1872 TYR A CD1   1 
ATOM   3374  C  CD2   . TYR A 1 1872 ? 59.116  75.157  127.798 1.00 6.48   ? 1872 TYR A CD2   1 
ATOM   3375  C  CE1   . TYR A 1 1872 ? 57.119  76.670  128.949 1.00 6.81   ? 1872 TYR A CE1   1 
ATOM   3376  C  CE2   . TYR A 1 1872 ? 59.278  75.654  129.077 1.00 7.23   ? 1872 TYR A CE2   1 
ATOM   3377  C  CZ    . TYR A 1 1872 ? 58.277  76.409  129.647 1.00 9.38   ? 1872 TYR A CZ    1 
ATOM   3378  O  OH    . TYR A 1 1872 ? 58.434  76.906  130.920 1.00 10.20  ? 1872 TYR A OH    1 
ATOM   3379  N  N     . LEU A 1 1873 ? 58.182  78.226  125.130 1.00 4.23   ? 1873 LEU A N     1 
ATOM   3380  C  CA    . LEU A 1 1873 ? 59.103  79.348  125.057 1.00 5.95   ? 1873 LEU A CA    1 
ATOM   3381  C  C     . LEU A 1 1873 ? 59.763  79.690  126.381 1.00 8.45   ? 1873 LEU A C     1 
ATOM   3382  O  O     . LEU A 1 1873 ? 60.647  80.552  126.404 1.00 10.67  ? 1873 LEU A O     1 
ATOM   3383  C  CB    . LEU A 1 1873 ? 58.380  80.587  124.514 1.00 8.36   ? 1873 LEU A CB    1 
ATOM   3384  C  CG    . LEU A 1 1873 ? 57.707  80.332  123.169 1.00 5.19   ? 1873 LEU A CG    1 
ATOM   3385  C  CD1   . LEU A 1 1873 ? 57.082  81.602  122.620 1.00 4.22   ? 1873 LEU A CD1   1 
ATOM   3386  C  CD2   . LEU A 1 1873 ? 58.722  79.748  122.199 1.00 5.24   ? 1873 LEU A CD2   1 
ATOM   3387  N  N     . GLY A 1 1874 ? 59.376  79.038  127.473 1.00 8.68   ? 1874 GLY A N     1 
ATOM   3388  C  CA    . GLY A 1 1874 ? 59.919  79.425  128.760 1.00 9.51   ? 1874 GLY A CA    1 
ATOM   3389  C  C     . GLY A 1 1874 ? 59.479  80.828  129.120 1.00 9.15   ? 1874 GLY A C     1 
ATOM   3390  O  O     . GLY A 1 1874 ? 58.324  81.217  128.918 1.00 10.72  ? 1874 GLY A O     1 
ATOM   3391  N  N     . VAL A 1 1875 ? 60.410  81.606  129.659 1.00 15.01  ? 1875 VAL A N     1 
ATOM   3392  C  CA    . VAL A 1 1875 ? 60.153  82.984  130.054 1.00 15.04  ? 1875 VAL A CA    1 
ATOM   3393  C  C     . VAL A 1 1875 ? 61.178  83.852  129.335 1.00 18.20  ? 1875 VAL A C     1 
ATOM   3394  O  O     . VAL A 1 1875 ? 62.360  83.870  129.697 1.00 27.21  ? 1875 VAL A O     1 
ATOM   3395  C  CB    . VAL A 1 1875 ? 60.222  83.168  131.573 1.00 13.67  ? 1875 VAL A CB    1 
ATOM   3396  C  CG1   . VAL A 1 1875 ? 59.772  84.565  131.947 1.00 14.35  ? 1875 VAL A CG1   1 
ATOM   3397  C  CG2   . VAL A 1 1875 ? 59.375  82.120  132.273 1.00 12.96  ? 1875 VAL A CG2   1 
ATOM   3398  N  N     . GLN A 1 1876 ? 60.729  84.576  128.316 1.00 18.04  ? 1876 GLN A N     1 
ATOM   3399  C  CA    . GLN A 1 1876 ? 61.597  85.381  127.471 1.00 19.87  ? 1876 GLN A CA    1 
ATOM   3400  C  C     . GLN A 1 1876 ? 61.209  86.851  127.522 1.00 24.11  ? 1876 GLN A C     1 
ATOM   3401  O  O     . GLN A 1 1876 ? 60.033  87.204  127.632 1.00 23.99  ? 1876 GLN A O     1 
ATOM   3402  C  CB    . GLN A 1 1876 ? 61.545  84.892  126.024 1.00 18.19  ? 1876 GLN A CB    1 
ATOM   3403  C  CG    . GLN A 1 1876 ? 62.131  83.520  125.809 1.00 21.29  ? 1876 GLN A CG    1 
ATOM   3404  C  CD    . GLN A 1 1876 ? 62.025  83.095  124.371 1.00 20.09  ? 1876 GLN A CD    1 
ATOM   3405  O  OE1   . GLN A 1 1876 ? 61.447  83.805  123.554 1.00 20.97  ? 1876 GLN A OE1   1 
ATOM   3406  N  NE2   . GLN A 1 1876 ? 62.617  81.959  124.041 1.00 19.94  ? 1876 GLN A NE2   1 
ATOM   3407  N  N     . ASP A 1 1877 ? 62.222  87.708  127.419 1.00 30.59  ? 1877 ASP A N     1 
ATOM   3408  C  CA    . ASP A 1 1877 ? 61.990  89.144  127.349 1.00 28.08  ? 1877 ASP A CA    1 
ATOM   3409  C  C     . ASP A 1 1877 ? 61.141  89.473  126.128 1.00 22.55  ? 1877 ASP A C     1 
ATOM   3410  O  O     . ASP A 1 1877 ? 61.412  88.993  125.022 1.00 20.17  ? 1877 ASP A O     1 
ATOM   3411  C  CB    . ASP A 1 1877 ? 63.320  89.893  127.287 1.00 33.84  ? 1877 ASP A CB    1 
ATOM   3412  C  CG    . ASP A 1 1877 ? 64.251  89.523  128.424 1.00 46.22  ? 1877 ASP A CG    1 
ATOM   3413  O  OD1   . ASP A 1 1877 ? 65.222  88.777  128.181 1.00 57.28  ? 1877 ASP A OD1   1 
ATOM   3414  O  OD2   . ASP A 1 1877 ? 64.013  89.980  129.561 1.00 50.72  ? 1877 ASP A OD2   1 
ATOM   3415  N  N     . LYS A 1 1878 ? 60.112  90.290  126.326 1.00 17.81  ? 1878 LYS A N     1 
ATOM   3416  C  CA    . LYS A 1 1878 ? 59.184  90.645  125.262 1.00 19.75  ? 1878 LYS A CA    1 
ATOM   3417  C  C     . LYS A 1 1878 ? 59.317  92.128  124.940 1.00 15.10  ? 1878 LYS A C     1 
ATOM   3418  O  O     . LYS A 1 1878 ? 59.387  92.964  125.847 1.00 15.52  ? 1878 LYS A O     1 
ATOM   3419  C  CB    . LYS A 1 1878 ? 57.749  90.286  125.646 1.00 14.48  ? 1878 LYS A CB    1 
ATOM   3420  C  CG    . LYS A 1 1878 ? 57.534  88.786  125.727 1.00 17.81  ? 1878 LYS A CG    1 
ATOM   3421  C  CD    . LYS A 1 1878 ? 56.110  88.413  126.076 1.00 17.67  ? 1878 LYS A CD    1 
ATOM   3422  C  CE    . LYS A 1 1878 ? 55.979  86.902  126.158 1.00 18.92  ? 1878 LYS A CE    1 
ATOM   3423  N  NZ    . LYS A 1 1878 ? 54.607  86.457  126.509 1.00 12.52  ? 1878 LYS A NZ    1 
ATOM   3424  N  N     . LEU A 1 1879 ? 59.353  92.440  123.647 1.00 12.09  ? 1879 LEU A N     1 
ATOM   3425  C  CA    . LEU A 1 1879 ? 59.628  93.797  123.199 1.00 7.92   ? 1879 LEU A CA    1 
ATOM   3426  C  C     . LEU A 1 1879 ? 58.454  94.720  123.497 1.00 7.23   ? 1879 LEU A C     1 
ATOM   3427  O  O     . LEU A 1 1879 ? 57.304  94.283  123.589 1.00 9.74   ? 1879 LEU A O     1 
ATOM   3428  C  CB    . LEU A 1 1879 ? 59.918  93.802  121.698 1.00 5.87   ? 1879 LEU A CB    1 
ATOM   3429  C  CG    . LEU A 1 1879 ? 61.232  93.178  121.227 1.00 4.76   ? 1879 LEU A CG    1 
ATOM   3430  C  CD1   . LEU A 1 1879 ? 61.484  93.521  119.768 1.00 3.16   ? 1879 LEU A CD1   1 
ATOM   3431  C  CD2   . LEU A 1 1879 ? 62.399  93.609  122.101 1.00 5.85   ? 1879 LEU A CD2   1 
ATOM   3432  N  N     . VAL A 1 1880 ? 58.755  96.009  123.653 1.00 5.86   ? 1880 VAL A N     1 
ATOM   3433  C  CA    . VAL A 1 1880 ? 57.707  97.018  123.710 1.00 4.68   ? 1880 VAL A CA    1 
ATOM   3434  C  C     . VAL A 1 1880 ? 57.080  97.145  122.329 1.00 4.57   ? 1880 VAL A C     1 
ATOM   3435  O  O     . VAL A 1 1880 ? 57.782  97.324  121.325 1.00 5.62   ? 1880 VAL A O     1 
ATOM   3436  C  CB    . VAL A 1 1880 ? 58.276  98.360  124.194 1.00 4.73   ? 1880 VAL A CB    1 
ATOM   3437  C  CG1   . VAL A 1 1880 ? 57.249  99.475  124.015 1.00 3.32   ? 1880 VAL A CG1   1 
ATOM   3438  C  CG2   . VAL A 1 1880 ? 58.729  98.257  125.640 1.00 4.37   ? 1880 VAL A CG2   1 
ATOM   3439  N  N     . GLN A 1 1881 ? 55.757  97.046  122.269 1.00 5.42   ? 1881 GLN A N     1 
ATOM   3440  C  CA    . GLN A 1 1881 ? 55.045  97.011  120.993 1.00 7.28   ? 1881 GLN A CA    1 
ATOM   3441  C  C     . GLN A 1 1881 ? 54.919  98.431  120.453 1.00 5.63   ? 1881 GLN A C     1 
ATOM   3442  O  O     . GLN A 1 1881 ? 53.914  99.109  120.673 1.00 8.56   ? 1881 GLN A O     1 
ATOM   3443  C  CB    . GLN A 1 1881 ? 53.681  96.358  121.179 1.00 8.12   ? 1881 GLN A CB    1 
ATOM   3444  C  CG    . GLN A 1 1881 ? 53.022  95.874  119.903 1.00 7.77   ? 1881 GLN A CG    1 
ATOM   3445  C  CD    . GLN A 1 1881 ? 53.786  94.758  119.221 1.00 11.56  ? 1881 GLN A CD    1 
ATOM   3446  O  OE1   . GLN A 1 1881 ? 54.074  93.726  119.827 1.00 18.11  ? 1881 GLN A OE1   1 
ATOM   3447  N  NE2   . GLN A 1 1881 ? 54.087  94.945  117.944 1.00 7.45   ? 1881 GLN A NE2   1 
ATOM   3448  N  N     . THR A 1 1882 ? 55.944  98.884  119.736 1.00 6.47   ? 1882 THR A N     1 
ATOM   3449  C  CA    . THR A 1 1882 ? 56.039  100.223 119.175 1.00 5.95   ? 1882 THR A CA    1 
ATOM   3450  C  C     . THR A 1 1882 ? 55.378  100.292 117.805 1.00 5.94   ? 1882 THR A C     1 
ATOM   3451  O  O     . THR A 1 1882 ? 55.137  99.264  117.167 1.00 5.59   ? 1882 THR A O     1 
ATOM   3452  C  CB    . THR A 1 1882 ? 57.509  100.646 119.058 1.00 6.04   ? 1882 THR A CB    1 
ATOM   3453  O  OG1   . THR A 1 1882 ? 58.129  99.945  117.973 1.00 6.13   ? 1882 THR A OG1   1 
ATOM   3454  C  CG2   . THR A 1 1882 ? 58.252  100.348 120.343 1.00 3.76   ? 1882 THR A CG2   1 
ATOM   3455  N  N     . PRO A 1 1883 ? 55.050  101.500 117.328 1.00 9.24   ? 1883 PRO A N     1 
ATOM   3456  C  CA    . PRO A 1 1883 ? 54.531  101.623 115.954 1.00 8.11   ? 1883 PRO A CA    1 
ATOM   3457  C  C     . PRO A 1 1883 ? 55.466  101.052 114.902 1.00 5.71   ? 1883 PRO A C     1 
ATOM   3458  O  O     . PRO A 1 1883 ? 55.000  100.444 113.929 1.00 5.04   ? 1883 PRO A O     1 
ATOM   3459  C  CB    . PRO A 1 1883 ? 54.352  103.138 115.800 1.00 6.21   ? 1883 PRO A CB    1 
ATOM   3460  C  CG    . PRO A 1 1883 ? 54.053  103.599 117.182 1.00 8.96   ? 1883 PRO A CG    1 
ATOM   3461  C  CD    . PRO A 1 1883 ? 54.969  102.782 118.051 1.00 8.18   ? 1883 PRO A CD    1 
ATOM   3462  N  N     . LEU A 1 1884 ? 56.778  101.230 115.070 1.00 5.44   ? 1884 LEU A N     1 
ATOM   3463  C  CA    . LEU A 1 1884 ? 57.727  100.562 114.187 1.00 5.66   ? 1884 LEU A CA    1 
ATOM   3464  C  C     . LEU A 1 1884 ? 57.607  99.050  114.309 1.00 3.42   ? 1884 LEU A C     1 
ATOM   3465  O  O     . LEU A 1 1884 ? 57.682  98.329  113.308 1.00 3.21   ? 1884 LEU A O     1 
ATOM   3466  C  CB    . LEU A 1 1884 ? 59.154  101.014 114.500 1.00 6.89   ? 1884 LEU A CB    1 
ATOM   3467  C  CG    . LEU A 1 1884 ? 60.260  100.368 113.661 1.00 7.88   ? 1884 LEU A CG    1 
ATOM   3468  C  CD1   . LEU A 1 1884 ? 60.057  100.661 112.180 1.00 5.50   ? 1884 LEU A CD1   1 
ATOM   3469  C  CD2   . LEU A 1 1884 ? 61.636  100.824 114.119 1.00 6.73   ? 1884 LEU A CD2   1 
ATOM   3470  N  N     . THR A 1 1885 ? 57.408  98.551  115.531 1.00 4.76   ? 1885 THR A N     1 
ATOM   3471  C  CA    . THR A 1 1885 ? 57.233  97.116  115.721 1.00 3.92   ? 1885 THR A CA    1 
ATOM   3472  C  C     . THR A 1 1885 ? 55.930  96.636  115.092 1.00 3.20   ? 1885 THR A C     1 
ATOM   3473  O  O     . THR A 1 1885 ? 55.873  95.538  114.529 1.00 3.10   ? 1885 THR A O     1 
ATOM   3474  C  CB    . THR A 1 1885 ? 57.278  96.772  117.211 1.00 4.03   ? 1885 THR A CB    1 
ATOM   3475  O  OG1   . THR A 1 1885 ? 58.518  97.227  117.766 1.00 6.99   ? 1885 THR A OG1   1 
ATOM   3476  C  CG2   . THR A 1 1885 ? 57.203  95.270  117.404 1.00 4.08   ? 1885 THR A CG2   1 
ATOM   3477  N  N     . ASP A 1 1886 ? 54.873  97.447  115.175 1.00 3.58   ? 1886 ASP A N     1 
ATOM   3478  C  CA    . ASP A 1 1886 ? 53.616  97.098  114.518 1.00 3.93   ? 1886 ASP A CA    1 
ATOM   3479  C  C     . ASP A 1 1886 ? 53.791  97.029  113.005 1.00 2.90   ? 1886 ASP A C     1 
ATOM   3480  O  O     . ASP A 1 1886 ? 53.280  96.114  112.349 1.00 2.78   ? 1886 ASP A O     1 
ATOM   3481  C  CB    . ASP A 1 1886 ? 52.531  98.109  114.888 1.00 4.93   ? 1886 ASP A CB    1 
ATOM   3482  C  CG    . ASP A 1 1886 ? 52.190  98.085  116.362 1.00 10.55  ? 1886 ASP A CG    1 
ATOM   3483  O  OD1   . ASP A 1 1886 ? 52.851  97.339  117.111 1.00 12.95  ? 1886 ASP A OD1   1 
ATOM   3484  O  OD2   . ASP A 1 1886 ? 51.260  98.809  116.771 1.00 13.47  ? 1886 ASP A OD2   1 
ATOM   3485  N  N     . ARG A 1 1887 ? 54.510  97.998  112.434 1.00 2.86   ? 1887 ARG A N     1 
ATOM   3486  C  CA    . ARG A 1 1887 ? 54.780  97.976  111.001 1.00 2.54   ? 1887 ARG A CA    1 
ATOM   3487  C  C     . ARG A 1 1887 ? 55.608  96.755  110.620 1.00 2.10   ? 1887 ARG A C     1 
ATOM   3488  O  O     . ARG A 1 1887 ? 55.367  96.129  109.579 1.00 2.68   ? 1887 ARG A O     1 
ATOM   3489  C  CB    . ARG A 1 1887 ? 55.491  99.264  110.585 1.00 2.45   ? 1887 ARG A CB    1 
ATOM   3490  C  CG    . ARG A 1 1887 ? 55.704  99.417  109.088 1.00 3.33   ? 1887 ARG A CG    1 
ATOM   3491  C  CD    . ARG A 1 1887 ? 56.547  100.646 108.782 1.00 4.37   ? 1887 ARG A CD    1 
ATOM   3492  N  NE    . ARG A 1 1887 ? 56.778  100.819 107.353 1.00 7.96   ? 1887 ARG A NE    1 
ATOM   3493  C  CZ    . ARG A 1 1887 ? 56.469  101.911 106.669 1.00 7.10   ? 1887 ARG A CZ    1 
ATOM   3494  N  NH1   . ARG A 1 1887 ? 55.915  102.960 107.254 1.00 6.98   ? 1887 ARG A NH1   1 
ATOM   3495  N  NH2   . ARG A 1 1887 ? 56.725  101.954 105.365 1.00 8.67   ? 1887 ARG A NH2   1 
ATOM   3496  N  N     . CYS A 1 1888 ? 56.589  96.403  111.454 1.00 2.04   ? 1888 CYS A N     1 
ATOM   3497  C  CA    . CYS A 1 1888 ? 57.389  95.209  111.207 1.00 2.44   ? 1888 CYS A CA    1 
ATOM   3498  C  C     . CYS A 1 1888 ? 56.523  93.958  111.218 1.00 1.83   ? 1888 CYS A C     1 
ATOM   3499  O  O     . CYS A 1 1888 ? 56.638  93.103  110.334 1.00 2.06   ? 1888 CYS A O     1 
ATOM   3500  C  CB    . CYS A 1 1888 ? 58.505  95.105  112.247 1.00 3.82   ? 1888 CYS A CB    1 
ATOM   3501  S  SG    . CYS A 1 1888 ? 59.682  93.769  111.952 1.00 7.58   ? 1888 CYS A SG    1 
ATOM   3502  N  N     . TYR A 1 1889 ? 55.642  93.840  112.213 1.00 1.70   ? 1889 TYR A N     1 
ATOM   3503  C  CA    . TYR A 1 1889 ? 54.740  92.696  112.274 1.00 1.76   ? 1889 TYR A CA    1 
ATOM   3504  C  C     . TYR A 1 1889 ? 53.866  92.629  111.031 1.00 1.39   ? 1889 TYR A C     1 
ATOM   3505  O  O     . TYR A 1 1889 ? 53.714  91.566  110.423 1.00 1.62   ? 1889 TYR A O     1 
ATOM   3506  C  CB    . TYR A 1 1889 ? 53.871  92.770  113.531 1.00 1.96   ? 1889 TYR A CB    1 
ATOM   3507  C  CG    . TYR A 1 1889 ? 54.540  92.303  114.804 1.00 2.11   ? 1889 TYR A CG    1 
ATOM   3508  C  CD1   . TYR A 1 1889 ? 55.921  92.344  114.950 1.00 2.11   ? 1889 TYR A CD1   1 
ATOM   3509  C  CD2   . TYR A 1 1889 ? 53.784  91.825  115.865 1.00 3.84   ? 1889 TYR A CD2   1 
ATOM   3510  C  CE1   . TYR A 1 1889 ? 56.527  91.919  116.116 1.00 2.49   ? 1889 TYR A CE1   1 
ATOM   3511  C  CE2   . TYR A 1 1889 ? 54.380  91.398  117.033 1.00 5.42   ? 1889 TYR A CE2   1 
ATOM   3512  C  CZ    . TYR A 1 1889 ? 55.751  91.447  117.153 1.00 4.66   ? 1889 TYR A CZ    1 
ATOM   3513  O  OH    . TYR A 1 1889 ? 56.344  91.022  118.318 1.00 3.48   ? 1889 TYR A OH    1 
ATOM   3514  N  N     . LEU A 1 1890 ? 53.297  93.766  110.629 1.00 1.32   ? 1890 LEU A N     1 
ATOM   3515  C  CA    . LEU A 1 1890 ? 52.407  93.784  109.472 1.00 1.57   ? 1890 LEU A CA    1 
ATOM   3516  C  C     . LEU A 1 1890 ? 53.143  93.353  108.207 1.00 1.55   ? 1890 LEU A C     1 
ATOM   3517  O  O     . LEU A 1 1890 ? 52.664  92.494  107.455 1.00 1.62   ? 1890 LEU A O     1 
ATOM   3518  C  CB    . LEU A 1 1890 ? 51.808  95.183  109.312 1.00 2.16   ? 1890 LEU A CB    1 
ATOM   3519  C  CG    . LEU A 1 1890 ? 50.748  95.411  108.234 1.00 1.39   ? 1890 LEU A CG    1 
ATOM   3520  C  CD1   . LEU A 1 1890 ? 49.603  94.422  108.379 1.00 1.30   ? 1890 LEU A CD1   1 
ATOM   3521  C  CD2   . LEU A 1 1890 ? 50.239  96.845  108.264 1.00 2.47   ? 1890 LEU A CD2   1 
ATOM   3522  N  N     . THR A 1 1891 ? 54.333  93.915  107.978 1.00 1.38   ? 1891 THR A N     1 
ATOM   3523  C  CA    . THR A 1 1891 ? 55.083  93.602  106.765 1.00 1.89   ? 1891 THR A CA    1 
ATOM   3524  C  C     . THR A 1 1891 ? 55.535  92.145  106.751 1.00 1.87   ? 1891 THR A C     1 
ATOM   3525  O  O     . THR A 1 1891 ? 55.408  91.452  105.734 1.00 1.70   ? 1891 THR A O     1 
ATOM   3526  C  CB    . THR A 1 1891 ? 56.285  94.538  106.634 1.00 2.68   ? 1891 THR A CB    1 
ATOM   3527  O  OG1   . THR A 1 1891 ? 55.828  95.891  106.513 1.00 3.85   ? 1891 THR A OG1   1 
ATOM   3528  C  CG2   . THR A 1 1891 ? 57.104  94.179  105.405 1.00 2.93   ? 1891 THR A CG2   1 
ATOM   3529  N  N     . MET A 1 1892 ? 56.062  91.656  107.877 1.00 1.38   ? 1892 MET A N     1 
ATOM   3530  C  CA    . MET A 1 1892 ? 56.547  90.281  107.913 1.00 1.52   ? 1892 MET A CA    1 
ATOM   3531  C  C     . MET A 1 1892 ? 55.401  89.280  107.805 1.00 1.28   ? 1892 MET A C     1 
ATOM   3532  O  O     . MET A 1 1892 ? 55.559  88.220  107.194 1.00 0.70   ? 1892 MET A O     1 
ATOM   3533  C  CB    . MET A 1 1892 ? 57.365  90.034  109.180 1.00 1.55   ? 1892 MET A CB    1 
ATOM   3534  C  CG    . MET A 1 1892 ? 58.578  90.939  109.402 1.00 1.78   ? 1892 MET A CG    1 
ATOM   3535  S  SD    . MET A 1 1892 ? 59.929  90.778  108.214 1.00 15.50  ? 1892 MET A SD    1 
ATOM   3536  C  CE    . MET A 1 1892 ? 59.482  91.969  106.954 1.00 2.17   ? 1892 MET A CE    1 
ATOM   3537  N  N     . THR A 1 1893 ? 54.236  89.594  108.380 1.00 1.06   ? 1893 THR A N     1 
ATOM   3538  C  CA    . THR A 1 1893 ? 53.095  88.695  108.234 1.00 1.18   ? 1893 THR A CA    1 
ATOM   3539  C  C     . THR A 1 1893 ? 52.565  88.700  106.805 1.00 1.71   ? 1893 THR A C     1 
ATOM   3540  O  O     . THR A 1 1893 ? 52.128  87.660  106.300 1.00 2.16   ? 1893 THR A O     1 
ATOM   3541  C  CB    . THR A 1 1893 ? 51.985  89.062  109.221 1.00 1.27   ? 1893 THR A CB    1 
ATOM   3542  O  OG1   . THR A 1 1893 ? 51.652  90.450  109.087 1.00 1.57   ? 1893 THR A OG1   1 
ATOM   3543  C  CG2   . THR A 1 1893 ? 52.413  88.762  110.653 1.00 1.27   ? 1893 THR A CG2   1 
ATOM   3544  N  N     . GLN A 1 1894 ? 52.594  89.856  106.136 1.00 1.63   ? 1894 GLN A N     1 
ATOM   3545  C  CA    . GLN A 1 1894 ? 52.253  89.879  104.716 1.00 2.07   ? 1894 GLN A CA    1 
ATOM   3546  C  C     . GLN A 1 1894 ? 53.226  89.034  103.905 1.00 2.10   ? 1894 GLN A C     1 
ATOM   3547  O  O     . GLN A 1 1894 ? 52.821  88.330  102.973 1.00 3.09   ? 1894 GLN A O     1 
ATOM   3548  C  CB    . GLN A 1 1894 ? 52.225  91.317  104.199 1.00 2.86   ? 1894 GLN A CB    1 
ATOM   3549  C  CG    . GLN A 1 1894 ? 50.909  92.034  104.444 1.00 2.46   ? 1894 GLN A CG    1 
ATOM   3550  C  CD    . GLN A 1 1894 ? 49.714  91.260  103.930 1.00 4.26   ? 1894 GLN A CD    1 
ATOM   3551  O  OE1   . GLN A 1 1894 ? 49.614  90.971  102.737 1.00 8.04   ? 1894 GLN A OE1   1 
ATOM   3552  N  NE2   . GLN A 1 1894 ? 48.798  90.920  104.827 1.00 4.17   ? 1894 GLN A NE2   1 
ATOM   3553  N  N     . ALA A 1 1895 ? 54.516  89.096  104.242 1.00 1.86   ? 1895 ALA A N     1 
ATOM   3554  C  CA    . ALA A 1 1895 ? 55.500  88.255  103.566 1.00 2.24   ? 1895 ALA A CA    1 
ATOM   3555  C  C     . ALA A 1 1895 ? 55.223  86.776  103.815 1.00 2.40   ? 1895 ALA A C     1 
ATOM   3556  O  O     . ALA A 1 1895 ? 55.313  85.951  102.898 1.00 2.47   ? 1895 ALA A O     1 
ATOM   3557  C  CB    . ALA A 1 1895 ? 56.910  88.624  104.026 1.00 1.81   ? 1895 ALA A CB    1 
ATOM   3558  N  N     . LEU A 1 1896 ? 54.891  86.423  105.058 1.00 2.06   ? 1896 LEU A N     1 
ATOM   3559  C  CA    . LEU A 1 1896 ? 54.617  85.030  105.400 1.00 2.53   ? 1896 LEU A CA    1 
ATOM   3560  C  C     . LEU A 1 1896 ? 53.387  84.510  104.665 1.00 3.53   ? 1896 LEU A C     1 
ATOM   3561  O  O     . LEU A 1 1896 ? 53.375  83.371  104.183 1.00 4.65   ? 1896 LEU A O     1 
ATOM   3562  C  CB    . LEU A 1 1896 ? 54.439  84.888  106.911 1.00 1.85   ? 1896 LEU A CB    1 
ATOM   3563  C  CG    . LEU A 1 1896 ? 55.663  85.145  107.790 1.00 2.42   ? 1896 LEU A CG    1 
ATOM   3564  C  CD1   . LEU A 1 1896 ? 55.259  85.295  109.248 1.00 1.92   ? 1896 LEU A CD1   1 
ATOM   3565  C  CD2   . LEU A 1 1896 ? 56.680  84.035  107.625 1.00 2.95   ? 1896 LEU A CD2   1 
ATOM   3566  N  N     . GLU A 1 1897 ? 52.335  85.329  104.577 1.00 3.04   ? 1897 GLU A N     1 
ATOM   3567  C  CA    . GLU A 1 1897 ? 51.133  84.901  103.868 1.00 5.16   ? 1897 GLU A CA    1 
ATOM   3568  C  C     . GLU A 1 1897 ? 51.401  84.694  102.385 1.00 5.52   ? 1897 GLU A C     1 
ATOM   3569  O  O     . GLU A 1 1897 ? 50.777  83.831  101.756 1.00 8.35   ? 1897 GLU A O     1 
ATOM   3570  C  CB    . GLU A 1 1897 ? 50.007  85.918  104.069 1.00 5.19   ? 1897 GLU A CB    1 
ATOM   3571  C  CG    . GLU A 1 1897 ? 48.619  85.404  103.691 1.00 6.95   ? 1897 GLU A CG    1 
ATOM   3572  C  CD    . GLU A 1 1897 ? 48.111  84.288  104.594 1.00 13.88  ? 1897 GLU A CD    1 
ATOM   3573  O  OE1   . GLU A 1 1897 ? 48.795  83.932  105.577 1.00 16.96  ? 1897 GLU A OE1   1 
ATOM   3574  O  OE2   . GLU A 1 1897 ? 47.014  83.760  104.315 1.00 19.20  ? 1897 GLU A OE2   1 
ATOM   3575  N  N     . ALA A 1 1898 ? 52.320  85.464  101.812 1.00 3.66   ? 1898 ALA A N     1 
ATOM   3576  C  CA    . ALA A 1 1898 ? 52.748  85.279  100.434 1.00 5.50   ? 1898 ALA A CA    1 
ATOM   3577  C  C     . ALA A 1 1898 ? 53.819  84.206  100.301 1.00 7.07   ? 1898 ALA A C     1 
ATOM   3578  O  O     . ALA A 1 1898 ? 54.353  84.015  99.203  1.00 9.72   ? 1898 ALA A O     1 
ATOM   3579  C  CB    . ALA A 1 1898 ? 53.259  86.601  99.857  1.00 4.35   ? 1898 ALA A CB    1 
ATOM   3580  N  N     . ARG A 1 1899 ? 54.140  83.510  101.393 1.00 5.95   ? 1899 ARG A N     1 
ATOM   3581  C  CA    . ARG A 1 1899 ? 55.190  82.491  101.412 1.00 6.58   ? 1899 ARG A CA    1 
ATOM   3582  C  C     . ARG A 1 1899 ? 56.526  83.077  100.966 1.00 5.86   ? 1899 ARG A C     1 
ATOM   3583  O  O     . ARG A 1 1899 ? 57.311  82.434  100.267 1.00 8.74   ? 1899 ARG A O     1 
ATOM   3584  C  CB    . ARG A 1 1899 ? 54.806  81.274  100.566 1.00 9.59   ? 1899 ARG A CB    1 
ATOM   3585  C  CG    . ARG A 1 1899 ? 53.926  80.259  101.289 1.00 14.81  ? 1899 ARG A CG    1 
ATOM   3586  C  CD    . ARG A 1 1899 ? 52.555  80.816  101.638 1.00 15.41  ? 1899 ARG A CD    1 
ATOM   3587  N  NE    . ARG A 1 1899 ? 51.821  79.934  102.537 1.00 23.82  ? 1899 ARG A NE    1 
ATOM   3588  C  CZ    . ARG A 1 1899 ? 50.683  80.255  103.137 1.00 22.73  ? 1899 ARG A CZ    1 
ATOM   3589  N  NH1   . ARG A 1 1899 ? 50.115  81.436  102.958 1.00 16.61  ? 1899 ARG A NH1   1 
ATOM   3590  N  NH2   . ARG A 1 1899 ? 50.101  79.368  103.940 1.00 28.58  ? 1899 ARG A NH2   1 
ATOM   3591  N  N     . LEU A 1 1900 ? 56.776  84.316  101.374 1.00 4.38   ? 1900 LEU A N     1 
ATOM   3592  C  CA    . LEU A 1 1900 ? 58.028  85.010  101.130 1.00 3.11   ? 1900 LEU A CA    1 
ATOM   3593  C  C     . LEU A 1 1900 ? 58.780  85.182  102.442 1.00 3.38   ? 1900 LEU A C     1 
ATOM   3594  O  O     . LEU A 1 1900 ? 58.188  85.224  103.524 1.00 4.55   ? 1900 LEU A O     1 
ATOM   3595  C  CB    . LEU A 1 1900 ? 57.780  86.378  100.485 1.00 4.44   ? 1900 LEU A CB    1 
ATOM   3596  C  CG    . LEU A 1 1900 ? 57.135  86.388  99.099  1.00 6.70   ? 1900 LEU A CG    1 
ATOM   3597  C  CD1   . LEU A 1 1900 ? 56.732  87.800  98.709  1.00 6.44   ? 1900 LEU A CD1   1 
ATOM   3598  C  CD2   . LEU A 1 1900 ? 58.085  85.802  98.071  1.00 4.81   ? 1900 LEU A CD2   1 
ATOM   3599  N  N     . GLY A 1 1901 ? 60.101  85.279  102.337 1.00 3.63   ? 1901 GLY A N     1 
ATOM   3600  C  CA    . GLY A 1 1901 ? 60.907  85.560  103.504 1.00 2.91   ? 1901 GLY A CA    1 
ATOM   3601  C  C     . GLY A 1 1901 ? 60.806  87.016  103.918 1.00 2.34   ? 1901 GLY A C     1 
ATOM   3602  O  O     . GLY A 1 1901 ? 60.414  87.884  103.143 1.00 3.37   ? 1901 GLY A O     1 
ATOM   3603  N  N     . GLY A 1 1902 ? 61.150  87.279  105.176 1.00 1.53   ? 1902 GLY A N     1 
ATOM   3604  C  CA    . GLY A 1 1902 ? 61.180  88.639  105.683 1.00 1.51   ? 1902 GLY A CA    1 
ATOM   3605  C  C     . GLY A 1 1902 ? 62.600  89.180  105.692 1.00 1.70   ? 1902 GLY A C     1 
ATOM   3606  O  O     . GLY A 1 1902 ? 63.561  88.434  105.864 1.00 2.01   ? 1902 GLY A O     1 
ATOM   3607  N  N     . SER A 1 1903 ? 62.720  90.492  105.504 1.00 2.60   ? 1903 SER A N     1 
ATOM   3608  C  CA    . SER A 1 1903 ? 64.023  91.154  105.429 1.00 2.60   ? 1903 SER A CA    1 
ATOM   3609  C  C     . SER A 1 1903 ? 63.942  92.533  106.064 1.00 2.39   ? 1903 SER A C     1 
ATOM   3610  O  O     . SER A 1 1903 ? 63.728  93.542  105.381 1.00 3.14   ? 1903 SER A O     1 
ATOM   3611  C  CB    . SER A 1 1903 ? 64.503  91.245  103.979 1.00 2.81   ? 1903 SER A CB    1 
ATOM   3612  O  OG    . SER A 1 1903 ? 65.883  91.552  103.916 1.00 7.29   ? 1903 SER A OG    1 
ATOM   3613  N  N     . PRO A 1 1904 ? 64.082  92.616  107.386 1.00 2.43   ? 1904 PRO A N     1 
ATOM   3614  C  CA    . PRO A 1 1904 ? 64.299  93.926  108.013 1.00 2.93   ? 1904 PRO A CA    1 
ATOM   3615  C  C     . PRO A 1 1904 ? 65.727  94.388  107.768 1.00 2.91   ? 1904 PRO A C     1 
ATOM   3616  O  O     . PRO A 1 1904 ? 66.681  93.635  107.975 1.00 3.40   ? 1904 PRO A O     1 
ATOM   3617  C  CB    . PRO A 1 1904 ? 64.032  93.667  109.502 1.00 2.57   ? 1904 PRO A CB    1 
ATOM   3618  C  CG    . PRO A 1 1904 ? 63.477  92.270  109.588 1.00 3.32   ? 1904 PRO A CG    1 
ATOM   3619  C  CD    . PRO A 1 1904 ? 63.951  91.542  108.382 1.00 2.81   ? 1904 PRO A CD    1 
ATOM   3620  N  N     . PHE A 1 1905 ? 65.872  95.628  107.309 1.00 3.12   ? 1905 PHE A N     1 
ATOM   3621  C  CA    . PHE A 1 1905 ? 67.183  96.198  107.042 1.00 3.50   ? 1905 PHE A CA    1 
ATOM   3622  C  C     . PHE A 1 1905 ? 67.291  97.577  107.675 1.00 3.27   ? 1905 PHE A C     1 
ATOM   3623  O  O     . PHE A 1 1905 ? 66.295  98.290  107.830 1.00 5.20   ? 1905 PHE A O     1 
ATOM   3624  C  CB    . PHE A 1 1905 ? 67.469  96.285  105.532 1.00 3.47   ? 1905 PHE A CB    1 
ATOM   3625  C  CG    . PHE A 1 1905 ? 66.557  97.218  104.785 1.00 2.96   ? 1905 PHE A CG    1 
ATOM   3626  C  CD1   . PHE A 1 1905 ? 65.343  96.775  104.288 1.00 2.67   ? 1905 PHE A CD1   1 
ATOM   3627  C  CD2   . PHE A 1 1905 ? 66.928  98.534  104.557 1.00 2.47   ? 1905 PHE A CD2   1 
ATOM   3628  C  CE1   . PHE A 1 1905 ? 64.510  97.629  103.592 1.00 3.30   ? 1905 PHE A CE1   1 
ATOM   3629  C  CE2   . PHE A 1 1905 ? 66.098  99.392  103.863 1.00 3.16   ? 1905 PHE A CE2   1 
ATOM   3630  C  CZ    . PHE A 1 1905 ? 64.889  98.938  103.379 1.00 3.97   ? 1905 PHE A CZ    1 
ATOM   3631  N  N     . GLY A 1 1906 ? 68.515  97.942  108.045 1.00 3.60   ? 1906 GLY A N     1 
ATOM   3632  C  CA    . GLY A 1 1906 ? 68.781  99.220  108.657 1.00 5.30   ? 1906 GLY A CA    1 
ATOM   3633  C  C     . GLY A 1 1906 ? 70.084  99.221  109.427 1.00 6.30   ? 1906 GLY A C     1 
ATOM   3634  O  O     . GLY A 1 1906 ? 70.828  98.236  109.438 1.00 5.67   ? 1906 GLY A O     1 
ATOM   3635  N  N     . PRO A 1 1907 ? 70.387  100.334 110.088 1.00 10.00  ? 1907 PRO A N     1 
ATOM   3636  C  CA    . PRO A 1 1907 ? 71.609  100.410 110.894 1.00 7.99   ? 1907 PRO A CA    1 
ATOM   3637  C  C     . PRO A 1 1907 ? 71.515  99.523  112.127 1.00 8.01   ? 1907 PRO A C     1 
ATOM   3638  O  O     . PRO A 1 1907 ? 70.439  99.114  112.564 1.00 8.85   ? 1907 PRO A O     1 
ATOM   3639  C  CB    . PRO A 1 1907 ? 71.694  101.891 111.264 1.00 8.84   ? 1907 PRO A CB    1 
ATOM   3640  C  CG    . PRO A 1 1907 ? 70.273  102.341 111.275 1.00 9.36   ? 1907 PRO A CG    1 
ATOM   3641  C  CD    . PRO A 1 1907 ? 69.599  101.577 110.164 1.00 7.52   ? 1907 PRO A CD    1 
ATOM   3642  N  N     . ALA A 1 1908 ? 72.685  99.217  112.682 1.00 7.84   ? 1908 ALA A N     1 
ATOM   3643  C  CA    . ALA A 1 1908 ? 72.764  98.334  113.836 1.00 7.98   ? 1908 ALA A CA    1 
ATOM   3644  C  C     . ALA A 1 1908 ? 72.071  98.948  115.046 1.00 9.53   ? 1908 ALA A C     1 
ATOM   3645  O  O     . ALA A 1 1908 ? 72.088  100.166 115.244 1.00 12.24  ? 1908 ALA A O     1 
ATOM   3646  C  CB    . ALA A 1 1908 ? 74.222  98.030  114.170 1.00 9.68   ? 1908 ALA A CB    1 
ATOM   3647  N  N     . GLY A 1 1909 ? 71.456  98.091  115.858 1.00 5.40   ? 1909 GLY A N     1 
ATOM   3648  C  CA    . GLY A 1 1909 ? 70.823  98.534  117.080 1.00 5.72   ? 1909 GLY A CA    1 
ATOM   3649  C  C     . GLY A 1 1909 ? 69.433  99.100  116.924 1.00 5.26   ? 1909 GLY A C     1 
ATOM   3650  O  O     . GLY A 1 1909 ? 68.993  99.877  117.779 1.00 7.24   ? 1909 GLY A O     1 
ATOM   3651  N  N     . THR A 1 1910 ? 68.720  98.743  115.857 1.00 4.83   ? 1910 THR A N     1 
ATOM   3652  C  CA    . THR A 1 1910 ? 67.375  99.254  115.639 1.00 5.14   ? 1910 THR A CA    1 
ATOM   3653  C  C     . THR A 1 1910 ? 66.281  98.264  116.020 1.00 4.10   ? 1910 THR A C     1 
ATOM   3654  O  O     . THR A 1 1910 ? 65.117  98.665  116.117 1.00 5.72   ? 1910 THR A O     1 
ATOM   3655  C  CB    . THR A 1 1910 ? 67.192  99.673  114.174 1.00 5.56   ? 1910 THR A CB    1 
ATOM   3656  O  OG1   . THR A 1 1910 ? 67.545  98.584  113.312 1.00 5.78   ? 1910 THR A OG1   1 
ATOM   3657  C  CG2   . THR A 1 1910 ? 68.062  100.878 113.853 1.00 6.95   ? 1910 THR A CG2   1 
ATOM   3658  N  N     . GLY A 1 1911 ? 66.616  96.996  116.232 1.00 3.57   ? 1911 GLY A N     1 
ATOM   3659  C  CA    . GLY A 1 1911 ? 65.643  96.011  116.652 1.00 2.38   ? 1911 GLY A CA    1 
ATOM   3660  C  C     . GLY A 1 1911 ? 65.251  94.974  115.622 1.00 2.82   ? 1911 GLY A C     1 
ATOM   3661  O  O     . GLY A 1 1911 ? 64.220  94.322  115.802 1.00 4.16   ? 1911 GLY A O     1 
ATOM   3662  N  N     . LYS A 1 1912 ? 66.049  94.838  114.558 1.00 3.42   ? 1912 LYS A N     1 
ATOM   3663  C  CA    . LYS A 1 1912 ? 65.724  93.886  113.463 1.00 2.59   ? 1912 LYS A CA    1 
ATOM   3664  C  C     . LYS A 1 1912 ? 65.653  92.457  114.023 1.00 2.35   ? 1912 LYS A C     1 
ATOM   3665  O  O     . LYS A 1 1912 ? 64.564  91.846  113.946 1.00 2.17   ? 1912 LYS A O     1 
ATOM   3666  C  CB    . LYS A 1 1912 ? 66.772  93.977  112.348 1.00 3.71   ? 1912 LYS A CB    1 
ATOM   3667  C  CG    . LYS A 1 1912 ? 66.811  95.297  111.590 1.00 2.82   ? 1912 LYS A CG    1 
ATOM   3668  C  CD    . LYS A 1 1912 ? 67.880  95.343  110.504 1.00 3.14   ? 1912 LYS A CD    1 
ATOM   3669  C  CE    . LYS A 1 1912 ? 69.269  95.262  111.053 1.00 3.97   ? 1912 LYS A CE    1 
ATOM   3670  N  NZ    . LYS A 1 1912 ? 69.589  96.424  111.886 1.00 3.48   ? 1912 LYS A NZ    1 
ATOM   3671  N  N     . THR A 1 1913 ? 66.764  91.953  114.567 1.00 3.09   ? 1913 THR A N     1 
ATOM   3672  C  CA    . THR A 1 1913 ? 66.801  90.560  115.068 1.00 3.77   ? 1913 THR A CA    1 
ATOM   3673  C  C     . THR A 1 1913 ? 65.738  90.380  116.131 1.00 3.31   ? 1913 THR A C     1 
ATOM   3674  O  O     . THR A 1 1913 ? 64.971  89.396  116.037 1.00 3.43   ? 1913 THR A O     1 
ATOM   3675  C  CB    . THR A 1 1913 ? 68.196  90.253  115.609 1.00 5.21   ? 1913 THR A CB    1 
ATOM   3676  O  OG1   . THR A 1 1913 ? 69.088  90.510  114.529 1.00 7.34   ? 1913 THR A OG1   1 
ATOM   3677  C  CG2   . THR A 1 1913 ? 68.333  88.814  116.074 1.00 5.90   ? 1913 THR A CG2   1 
ATOM   3678  N  N     . GLU A 1 1914 ? 65.680  91.294  117.104 1.00 3.33   ? 1914 GLU A N     1 
ATOM   3679  C  CA    . GLU A 1 1914 ? 64.703  91.174  118.218 1.00 3.05   ? 1914 GLU A CA    1 
ATOM   3680  C  C     . GLU A 1 1914 ? 63.280  91.123  117.641 1.00 2.42   ? 1914 GLU A C     1 
ATOM   3681  O  O     . GLU A 1 1914 ? 62.513  90.221  118.041 1.00 2.95   ? 1914 GLU A O     1 
ATOM   3682  C  CB    . GLU A 1 1914 ? 64.857  92.333  119.202 1.00 4.14   ? 1914 GLU A CB    1 
ATOM   3683  C  CG    . GLU A 1 1914 ? 66.207  92.334  119.913 1.00 9.37   ? 1914 GLU A CG    1 
ATOM   3684  C  CD    . GLU A 1 1914 ? 66.573  90.986  120.505 1.00 17.60  ? 1914 GLU A CD    1 
ATOM   3685  O  OE1   . GLU A 1 1914 ? 65.816  90.494  121.368 1.00 18.29  ? 1914 GLU A OE1   1 
ATOM   3686  O  OE2   . GLU A 1 1914 ? 67.611  90.424  120.097 1.00 18.35  ? 1914 GLU A OE2   1 
ATOM   3687  N  N     . SER A 1 1915 ? 62.950  92.049  116.736 1.00 2.13   ? 1915 SER A N     1 
ATOM   3688  C  CA    . SER A 1 1915 ? 61.604  92.091  116.172 1.00 1.80   ? 1915 SER A CA    1 
ATOM   3689  C  C     . SER A 1 1915 ? 61.237  90.768  115.517 1.00 1.63   ? 1915 SER A C     1 
ATOM   3690  O  O     . SER A 1 1915 ? 60.108  90.286  115.668 1.00 1.76   ? 1915 SER A O     1 
ATOM   3691  C  CB    . SER A 1 1915 ? 61.482  93.231  115.164 1.00 2.44   ? 1915 SER A CB    1 
ATOM   3692  O  OG    . SER A 1 1915 ? 61.771  94.473  115.778 1.00 3.73   ? 1915 SER A OG    1 
ATOM   3693  N  N     . VAL A 1 1916 ? 62.173  90.164  114.781 1.00 1.27   ? 1916 VAL A N     1 
ATOM   3694  C  CA    . VAL A 1 1916 ? 61.889  88.880  114.144 1.00 1.68   ? 1916 VAL A CA    1 
ATOM   3695  C  C     . VAL A 1 1916 ? 61.640  87.808  115.201 1.00 1.66   ? 1916 VAL A C     1 
ATOM   3696  O  O     . VAL A 1 1916 ? 60.695  87.012  115.098 1.00 1.19   ? 1916 VAL A O     1 
ATOM   3697  C  CB    . VAL A 1 1916 ? 63.033  88.486  113.191 1.00 1.71   ? 1916 VAL A CB    1 
ATOM   3698  C  CG1   . VAL A 1 1916 ? 62.857  87.055  112.707 1.00 1.18   ? 1916 VAL A CG1   1 
ATOM   3699  C  CG2   . VAL A 1 1916 ? 63.096  89.447  112.014 1.00 1.15   ? 1916 VAL A CG2   1 
ATOM   3700  N  N     . LYS A 1 1917 ? 62.476  87.783  116.244 1.00 2.06   ? 1917 LYS A N     1 
ATOM   3701  C  CA    . LYS A 1 1917 ? 62.282  86.815  117.319 1.00 2.71   ? 1917 LYS A CA    1 
ATOM   3702  C  C     . LYS A 1 1917 ? 60.959  87.042  118.039 1.00 2.10   ? 1917 LYS A C     1 
ATOM   3703  O  O     . LYS A 1 1917 ? 60.263  86.082  118.380 1.00 1.43   ? 1917 LYS A O     1 
ATOM   3704  C  CB    . LYS A 1 1917 ? 63.443  86.870  118.312 1.00 4.40   ? 1917 LYS A CB    1 
ATOM   3705  C  CG    . LYS A 1 1917 ? 64.770  86.395  117.751 1.00 5.52   ? 1917 LYS A CG    1 
ATOM   3706  C  CD    . LYS A 1 1917 ? 65.754  86.058  118.859 1.00 10.08  ? 1917 LYS A CD    1 
ATOM   3707  C  CE    . LYS A 1 1917 ? 66.003  87.249  119.764 1.00 13.91  ? 1917 LYS A CE    1 
ATOM   3708  N  NZ    . LYS A 1 1917 ? 66.894  86.899  120.904 1.00 11.80  ? 1917 LYS A NZ    1 
ATOM   3709  N  N     . ALA A 1 1918 ? 60.601  88.303  118.289 1.00 1.95   ? 1918 ALA A N     1 
ATOM   3710  C  CA    . ALA A 1 1918 ? 59.343  88.600  118.964 1.00 2.17   ? 1918 ALA A CA    1 
ATOM   3711  C  C     . ALA A 1 1918 ? 58.150  88.182  118.117 1.00 1.74   ? 1918 ALA A C     1 
ATOM   3712  O  O     . ALA A 1 1918 ? 57.162  87.663  118.644 1.00 1.91   ? 1918 ALA A O     1 
ATOM   3713  C  CB    . ALA A 1 1918 ? 59.269  90.087  119.305 1.00 2.12   ? 1918 ALA A CB    1 
ATOM   3714  N  N     . LEU A 1 1919 ? 58.219  88.409  116.803 1.00 1.40   ? 1919 LEU A N     1 
ATOM   3715  C  CA    . LEU A 1 1919 ? 57.151  87.952  115.922 1.00 1.14   ? 1919 LEU A CA    1 
ATOM   3716  C  C     . LEU A 1 1919 ? 57.023  86.435  115.955 1.00 1.08   ? 1919 LEU A C     1 
ATOM   3717  O  O     . LEU A 1 1919 ? 55.912  85.901  116.040 1.00 0.82   ? 1919 LEU A O     1 
ATOM   3718  C  CB    . LEU A 1 1919 ? 57.405  88.424  114.493 1.00 1.44   ? 1919 LEU A CB    1 
ATOM   3719  C  CG    . LEU A 1 1919 ? 56.354  87.942  113.493 1.00 1.44   ? 1919 LEU A CG    1 
ATOM   3720  C  CD1   . LEU A 1 1919 ? 54.962  88.394  113.904 1.00 1.05   ? 1919 LEU A CD1   1 
ATOM   3721  C  CD2   . LEU A 1 1919 ? 56.681  88.404  112.099 1.00 3.17   ? 1919 LEU A CD2   1 
ATOM   3722  N  N     . GLY A 1 1920 ? 58.152  85.725  115.887 1.00 1.00   ? 1920 GLY A N     1 
ATOM   3723  C  CA    . GLY A 1 1920 ? 58.099  84.272  115.935 1.00 0.89   ? 1920 GLY A CA    1 
ATOM   3724  C  C     . GLY A 1 1920 ? 57.563  83.746  117.252 1.00 0.96   ? 1920 GLY A C     1 
ATOM   3725  O  O     . GLY A 1 1920 ? 56.784  82.790  117.281 1.00 1.34   ? 1920 GLY A O     1 
ATOM   3726  N  N     . HIS A 1 1921 ? 57.974  84.363  118.361 1.00 1.38   ? 1921 HIS A N     1 
ATOM   3727  C  CA    . HIS A 1 1921 ? 57.532  83.926  119.679 1.00 2.06   ? 1921 HIS A CA    1 
ATOM   3728  C  C     . HIS A 1 1921 ? 56.063  84.251  119.906 1.00 1.53   ? 1921 HIS A C     1 
ATOM   3729  O  O     . HIS A 1 1921 ? 55.361  83.507  120.598 1.00 2.31   ? 1921 HIS A O     1 
ATOM   3730  C  CB    . HIS A 1 1921 ? 58.414  84.572  120.746 1.00 2.92   ? 1921 HIS A CB    1 
ATOM   3731  C  CG    . HIS A 1 1921 ? 59.867  84.249  120.589 1.00 5.91   ? 1921 HIS A CG    1 
ATOM   3732  N  ND1   . HIS A 1 1921 ? 60.866  84.977  121.199 1.00 8.71   ? 1921 HIS A ND1   1 
ATOM   3733  C  CD2   . HIS A 1 1921 ? 60.490  83.281  119.875 1.00 5.26   ? 1921 HIS A CD2   1 
ATOM   3734  C  CE1   . HIS A 1 1921 ? 62.041  84.475  120.863 1.00 8.57   ? 1921 HIS A CE1   1 
ATOM   3735  N  NE2   . HIS A 1 1921 ? 61.841  83.441  120.067 1.00 10.11  ? 1921 HIS A NE2   1 
ATOM   3736  N  N     . GLN A 1 1922 ? 55.589  85.357  119.332 1.00 1.29   ? 1922 GLN A N     1 
ATOM   3737  C  CA    . GLN A 1 1922 ? 54.173  85.692  119.390 1.00 1.94   ? 1922 GLN A CA    1 
ATOM   3738  C  C     . GLN A 1 1922 ? 53.328  84.654  118.658 1.00 1.47   ? 1922 GLN A C     1 
ATOM   3739  O  O     . GLN A 1 1922 ? 52.168  84.428  119.021 1.00 1.27   ? 1922 GLN A O     1 
ATOM   3740  C  CB    . GLN A 1 1922 ? 53.966  87.094  118.811 1.00 2.30   ? 1922 GLN A CB    1 
ATOM   3741  C  CG    . GLN A 1 1922 ? 52.553  87.634  118.890 1.00 4.72   ? 1922 GLN A CG    1 
ATOM   3742  C  CD    . GLN A 1 1922 ? 52.067  87.804  120.309 1.00 7.96   ? 1922 GLN A CD    1 
ATOM   3743  O  OE1   . GLN A 1 1922 ? 52.534  88.679  121.036 1.00 10.50  ? 1922 GLN A OE1   1 
ATOM   3744  N  NE2   . GLN A 1 1922 ? 51.124  86.962  120.715 1.00 8.41   ? 1922 GLN A NE2   1 
ATOM   3745  N  N     . LEU A 1 1923 ? 53.891  84.008  117.637 1.00 1.61   ? 1923 LEU A N     1 
ATOM   3746  C  CA    . LEU A 1 1923 ? 53.224  82.938  116.906 1.00 1.22   ? 1923 LEU A CA    1 
ATOM   3747  C  C     . LEU A 1 1923 ? 53.510  81.556  117.482 1.00 1.62   ? 1923 LEU A C     1 
ATOM   3748  O  O     . LEU A 1 1923 ? 53.036  80.559  116.929 1.00 1.33   ? 1923 LEU A O     1 
ATOM   3749  C  CB    . LEU A 1 1923 ? 53.626  82.968  115.429 1.00 1.39   ? 1923 LEU A CB    1 
ATOM   3750  C  CG    . LEU A 1 1923 ? 53.096  84.104  114.554 1.00 1.32   ? 1923 LEU A CG    1 
ATOM   3751  C  CD1   . LEU A 1 1923 ? 53.392  83.837  113.087 1.00 1.67   ? 1923 LEU A CD1   1 
ATOM   3752  C  CD2   . LEU A 1 1923 ? 51.604  84.296  114.774 1.00 1.12   ? 1923 LEU A CD2   1 
ATOM   3753  N  N     . GLY A 1 1924 ? 54.266  81.472  118.573 1.00 1.72   ? 1924 GLY A N     1 
ATOM   3754  C  CA    . GLY A 1 1924 ? 54.640  80.177  119.115 1.00 1.45   ? 1924 GLY A CA    1 
ATOM   3755  C  C     . GLY A 1 1924 ? 55.573  79.387  118.226 1.00 1.52   ? 1924 GLY A C     1 
ATOM   3756  O  O     . GLY A 1 1924 ? 55.488  78.156  118.183 1.00 1.65   ? 1924 GLY A O     1 
ATOM   3757  N  N     . ARG A 1 1925 ? 56.473  80.065  117.521 1.00 1.15   ? 1925 ARG A N     1 
ATOM   3758  C  CA    . ARG A 1 1925 ? 57.406  79.428  116.603 1.00 1.88   ? 1925 ARG A CA    1 
ATOM   3759  C  C     . ARG A 1 1925 ? 58.778  79.302  117.251 1.00 1.61   ? 1925 ARG A C     1 
ATOM   3760  O  O     . ARG A 1 1925 ? 59.202  80.181  118.007 1.00 2.01   ? 1925 ARG A O     1 
ATOM   3761  C  CB    . ARG A 1 1925 ? 57.524  80.230  115.306 1.00 1.72   ? 1925 ARG A CB    1 
ATOM   3762  C  CG    . ARG A 1 1925 ? 56.254  80.286  114.479 1.00 1.72   ? 1925 ARG A CG    1 
ATOM   3763  C  CD    . ARG A 1 1925 ? 55.972  78.953  113.800 1.00 2.62   ? 1925 ARG A CD    1 
ATOM   3764  N  NE    . ARG A 1 1925 ? 54.856  79.021  112.862 1.00 3.77   ? 1925 ARG A NE    1 
ATOM   3765  C  CZ    . ARG A 1 1925 ? 53.603  79.315  113.185 1.00 3.85   ? 1925 ARG A CZ    1 
ATOM   3766  N  NH1   . ARG A 1 1925 ? 53.238  79.517  114.440 1.00 2.28   ? 1925 ARG A NH1   1 
ATOM   3767  N  NH2   . ARG A 1 1925 ? 52.688  79.392  112.223 1.00 3.98   ? 1925 ARG A NH2   1 
ATOM   3768  N  N     . PHE A 1 1926 ? 59.470  78.209  116.950 1.00 2.73   ? 1926 PHE A N     1 
ATOM   3769  C  CA    . PHE A 1 1926 ? 60.853  78.047  117.383 1.00 2.83   ? 1926 PHE A CA    1 
ATOM   3770  C  C     . PHE A 1 1926 ? 61.736  78.891  116.470 1.00 1.69   ? 1926 PHE A C     1 
ATOM   3771  O  O     . PHE A 1 1926 ? 61.875  78.594  115.280 1.00 2.26   ? 1926 PHE A O     1 
ATOM   3772  C  CB    . PHE A 1 1926 ? 61.240  76.570  117.348 1.00 3.51   ? 1926 PHE A CB    1 
ATOM   3773  C  CG    . PHE A 1 1926 ? 62.653  76.281  117.795 1.00 4.08   ? 1926 PHE A CG    1 
ATOM   3774  C  CD1   . PHE A 1 1926 ? 63.373  77.198  118.545 1.00 4.67   ? 1926 PHE A CD1   1 
ATOM   3775  C  CD2   . PHE A 1 1926 ? 63.248  75.068  117.488 1.00 4.30   ? 1926 PHE A CD2   1 
ATOM   3776  C  CE1   . PHE A 1 1926 ? 64.662  76.920  118.959 1.00 5.37   ? 1926 PHE A CE1   1 
ATOM   3777  C  CE2   . PHE A 1 1926 ? 64.536  74.783  117.902 1.00 5.86   ? 1926 PHE A CE2   1 
ATOM   3778  C  CZ    . PHE A 1 1926 ? 65.243  75.711  118.638 1.00 8.09   ? 1926 PHE A CZ    1 
ATOM   3779  N  N     . VAL A 1 1927 ? 62.316  79.955  117.014 1.00 1.77   ? 1927 VAL A N     1 
ATOM   3780  C  CA    . VAL A 1 1927 ? 63.110  80.902  116.239 1.00 2.40   ? 1927 VAL A CA    1 
ATOM   3781  C  C     . VAL A 1 1927 ? 64.582  80.634  116.514 1.00 2.66   ? 1927 VAL A C     1 
ATOM   3782  O  O     . VAL A 1 1927 ? 65.011  80.602  117.673 1.00 4.57   ? 1927 VAL A O     1 
ATOM   3783  C  CB    . VAL A 1 1927 ? 62.740  82.355  116.575 1.00 3.08   ? 1927 VAL A CB    1 
ATOM   3784  C  CG1   . VAL A 1 1927 ? 63.539  83.318  115.709 1.00 3.48   ? 1927 VAL A CG1   1 
ATOM   3785  C  CG2   . VAL A 1 1927 ? 61.250  82.577  116.391 1.00 1.72   ? 1927 VAL A CG2   1 
ATOM   3786  N  N     . LEU A 1 1928 ? 65.354  80.445  115.450 1.00 2.62   ? 1928 LEU A N     1 
ATOM   3787  C  CA    . LEU A 1 1928 ? 66.783  80.184  115.544 1.00 2.93   ? 1928 LEU A CA    1 
ATOM   3788  C  C     . LEU A 1 1928 ? 67.537  81.311  114.852 1.00 2.64   ? 1928 LEU A C     1 
ATOM   3789  O  O     . LEU A 1 1928 ? 67.264  81.623  113.688 1.00 2.63   ? 1928 LEU A O     1 
ATOM   3790  C  CB    . LEU A 1 1928 ? 67.142  78.833  114.924 1.00 4.39   ? 1928 LEU A CB    1 
ATOM   3791  C  CG    . LEU A 1 1928 ? 66.701  77.575  115.675 1.00 5.68   ? 1928 LEU A CG    1 
ATOM   3792  C  CD1   . LEU A 1 1928 ? 65.233  77.275  115.440 1.00 3.97   ? 1928 LEU A CD1   1 
ATOM   3793  C  CD2   . LEU A 1 1928 ? 67.558  76.389  115.279 1.00 5.43   ? 1928 LEU A CD2   1 
ATOM   3794  N  N     . VAL A 1 1929 ? 68.474  81.912  115.566 1.00 4.42   ? 1929 VAL A N     1 
ATOM   3795  C  CA    . VAL A 1 1929 ? 69.284  83.005  115.046 1.00 3.28   ? 1929 VAL A CA    1 
ATOM   3796  C  C     . VAL A 1 1929 ? 70.633  82.457  114.607 1.00 2.61   ? 1929 VAL A C     1 
ATOM   3797  O  O     . VAL A 1 1929 ? 71.266  81.675  115.326 1.00 4.00   ? 1929 VAL A O     1 
ATOM   3798  C  CB    . VAL A 1 1929 ? 69.446  84.113  116.105 1.00 3.81   ? 1929 VAL A CB    1 
ATOM   3799  C  CG1   . VAL A 1 1929 ? 70.500  85.114  115.674 1.00 5.78   ? 1929 VAL A CG1   1 
ATOM   3800  C  CG2   . VAL A 1 1929 ? 68.118  84.809  116.343 1.00 3.73   ? 1929 VAL A CG2   1 
ATOM   3801  N  N     . PHE A 1 1930 ? 71.071  82.855  113.415 1.00 2.78   ? 1930 PHE A N     1 
ATOM   3802  C  CA    . PHE A 1 1930 ? 72.372  82.467  112.883 1.00 3.11   ? 1930 PHE A CA    1 
ATOM   3803  C  C     . PHE A 1 1930 ? 73.174  83.726  112.596 1.00 3.95   ? 1930 PHE A C     1 
ATOM   3804  O  O     . PHE A 1 1930 ? 72.699  84.617  111.885 1.00 5.00   ? 1930 PHE A O     1 
ATOM   3805  C  CB    . PHE A 1 1930 ? 72.226  81.620  111.614 1.00 3.03   ? 1930 PHE A CB    1 
ATOM   3806  C  CG    . PHE A 1 1930 ? 71.301  80.444  111.767 1.00 3.28   ? 1930 PHE A CG    1 
ATOM   3807  C  CD1   . PHE A 1 1930 ? 69.943  80.576  111.531 1.00 2.86   ? 1930 PHE A CD1   1 
ATOM   3808  C  CD2   . PHE A 1 1930 ? 71.794  79.204  112.137 1.00 3.13   ? 1930 PHE A CD2   1 
ATOM   3809  C  CE1   . PHE A 1 1930 ? 69.094  79.496  111.670 1.00 3.30   ? 1930 PHE A CE1   1 
ATOM   3810  C  CE2   . PHE A 1 1930 ? 70.950  78.120  112.275 1.00 2.58   ? 1930 PHE A CE2   1 
ATOM   3811  C  CZ    . PHE A 1 1930 ? 69.598  78.267  112.043 1.00 3.86   ? 1930 PHE A CZ    1 
ATOM   3812  N  N     . ASN A 1 1931 ? 74.384  83.797  113.147 1.00 5.29   ? 1931 ASN A N     1 
ATOM   3813  C  CA    . ASN A 1 1931 ? 75.297  84.910  112.888 1.00 5.08   ? 1931 ASN A CA    1 
ATOM   3814  C  C     . ASN A 1 1931 ? 76.103  84.546  111.648 1.00 6.57   ? 1931 ASN A C     1 
ATOM   3815  O  O     . ASN A 1 1931 ? 77.125  83.862  111.715 1.00 9.93   ? 1931 ASN A O     1 
ATOM   3816  C  CB    . ASN A 1 1931 ? 76.187  85.172  114.097 1.00 4.83   ? 1931 ASN A CB    1 
ATOM   3817  C  CG    . ASN A 1 1931 ? 77.047  86.413  113.941 1.00 6.75   ? 1931 ASN A CG    1 
ATOM   3818  O  OD1   . ASN A 1 1931 ? 77.135  86.999  112.863 1.00 11.71  ? 1931 ASN A OD1   1 
ATOM   3819  N  ND2   . ASN A 1 1931 ? 77.682  86.824  115.029 1.00 7.33   ? 1931 ASN A ND2   1 
ATOM   3820  N  N     . CYS A 1 1932 ? 75.627  85.012  110.499 1.00 5.61   ? 1932 CYS A N     1 
ATOM   3821  C  CA    . CYS A 1 1932 ? 76.183  84.588  109.223 1.00 8.68   ? 1932 CYS A CA    1 
ATOM   3822  C  C     . CYS A 1 1932 ? 77.524  85.255  108.944 1.00 11.22  ? 1932 CYS A C     1 
ATOM   3823  O  O     . CYS A 1 1932 ? 77.753  86.412  109.307 1.00 12.49  ? 1932 CYS A O     1 
ATOM   3824  C  CB    . CYS A 1 1932 ? 75.201  84.903  108.097 1.00 8.14   ? 1932 CYS A CB    1 
ATOM   3825  S  SG    . CYS A 1 1932 ? 73.704  83.902  108.118 1.00 15.47  ? 1932 CYS A SG    1 
ATOM   3826  N  N     . ASP A 1 1933 ? 78.413  84.509  108.293 1.00 8.37   ? 1933 ASP A N     1 
ATOM   3827  C  CA    . ASP A 1 1933 ? 79.673  85.041  107.796 1.00 11.60  ? 1933 ASP A CA    1 
ATOM   3828  C  C     . ASP A 1 1933 ? 79.972  84.369  106.461 1.00 14.72  ? 1933 ASP A C     1 
ATOM   3829  O  O     . ASP A 1 1933 ? 79.140  83.642  105.911 1.00 13.58  ? 1933 ASP A O     1 
ATOM   3830  C  CB    . ASP A 1 1933 ? 80.803  84.845  108.813 1.00 14.98  ? 1933 ASP A CB    1 
ATOM   3831  C  CG    . ASP A 1 1933 ? 81.282  83.411  108.892 1.00 17.20  ? 1933 ASP A CG    1 
ATOM   3832  O  OD1   . ASP A 1 1933 ? 80.436  82.494  108.899 1.00 15.43  ? 1933 ASP A OD1   1 
ATOM   3833  O  OD2   . ASP A 1 1933 ? 82.511  83.201  108.954 1.00 23.48  ? 1933 ASP A OD2   1 
ATOM   3834  N  N     . GLU A 1 1934 ? 81.175  84.615  105.937 1.00 16.32  ? 1934 GLU A N     1 
ATOM   3835  C  CA    . GLU A 1 1934 ? 81.524  84.095  104.619 1.00 14.07  ? 1934 GLU A CA    1 
ATOM   3836  C  C     . GLU A 1 1934 ? 81.673  82.578  104.607 1.00 19.29  ? 1934 GLU A C     1 
ATOM   3837  O  O     . GLU A 1 1934 ? 81.686  81.980  103.526 1.00 24.56  ? 1934 GLU A O     1 
ATOM   3838  C  CB    . GLU A 1 1934 ? 82.812  84.749  104.110 1.00 19.23  ? 1934 GLU A CB    1 
ATOM   3839  C  CG    . GLU A 1 1934 ? 84.077  84.351  104.859 1.00 24.96  ? 1934 GLU A CG    1 
ATOM   3840  C  CD    . GLU A 1 1934 ? 84.207  85.023  106.213 1.00 29.09  ? 1934 GLU A CD    1 
ATOM   3841  O  OE1   . GLU A 1 1934 ? 83.350  85.868  106.549 1.00 29.58  ? 1934 GLU A OE1   1 
ATOM   3842  O  OE2   . GLU A 1 1934 ? 85.169  84.706  106.943 1.00 27.44  ? 1934 GLU A OE2   1 
ATOM   3843  N  N     . THR A 1 1935 ? 81.784  81.942  105.774 1.00 16.58  ? 1935 THR A N     1 
ATOM   3844  C  CA    . THR A 1 1935 ? 81.886  80.489  105.832 1.00 14.46  ? 1935 THR A CA    1 
ATOM   3845  C  C     . THR A 1 1935 ? 80.541  79.788  105.685 1.00 14.17  ? 1935 THR A C     1 
ATOM   3846  O  O     . THR A 1 1935 ? 80.515  78.561  105.546 1.00 15.40  ? 1935 THR A O     1 
ATOM   3847  C  CB    . THR A 1 1935 ? 82.546  80.050  107.142 1.00 12.37  ? 1935 THR A CB    1 
ATOM   3848  O  OG1   . THR A 1 1935 ? 81.671  80.332  108.242 1.00 15.55  ? 1935 THR A OG1   1 
ATOM   3849  C  CG2   . THR A 1 1935 ? 83.869  80.773  107.342 1.00 14.53  ? 1935 THR A CG2   1 
ATOM   3850  N  N     . PHE A 1 1936 ? 79.433  80.526  105.716 1.00 12.43  ? 1936 PHE A N     1 
ATOM   3851  C  CA    . PHE A 1 1936 ? 78.109  79.950  105.482 1.00 13.42  ? 1936 PHE A CA    1 
ATOM   3852  C  C     . PHE A 1 1936 ? 77.938  79.775  103.979 1.00 12.33  ? 1936 PHE A C     1 
ATOM   3853  O  O     . PHE A 1 1936 ? 77.387  80.632  103.287 1.00 16.78  ? 1936 PHE A O     1 
ATOM   3854  C  CB    . PHE A 1 1936 ? 77.019  80.837  106.074 1.00 11.27  ? 1936 PHE A CB    1 
ATOM   3855  C  CG    . PHE A 1 1936 ? 76.807  80.640  107.549 1.00 10.84  ? 1936 PHE A CG    1 
ATOM   3856  C  CD1   . PHE A 1 1936 ? 77.776  81.022  108.461 1.00 8.98   ? 1936 PHE A CD1   1 
ATOM   3857  C  CD2   . PHE A 1 1936 ? 75.632  80.081  108.025 1.00 8.56   ? 1936 PHE A CD2   1 
ATOM   3858  C  CE1   . PHE A 1 1936 ? 77.582  80.845  109.817 1.00 9.31   ? 1936 PHE A CE1   1 
ATOM   3859  C  CE2   . PHE A 1 1936 ? 75.432  79.901  109.380 1.00 7.39   ? 1936 PHE A CE2   1 
ATOM   3860  C  CZ    . PHE A 1 1936 ? 76.408  80.284  110.277 1.00 8.67   ? 1936 PHE A CZ    1 
ATOM   3861  N  N     . ASP A 1 1937 ? 78.419  78.646  103.467 1.00 15.08  ? 1937 ASP A N     1 
ATOM   3862  C  CA    . ASP A 1 1937 ? 78.433  78.393  102.035 1.00 12.51  ? 1937 ASP A CA    1 
ATOM   3863  C  C     . ASP A 1 1937 ? 77.140  77.700  101.604 1.00 11.45  ? 1937 ASP A C     1 
ATOM   3864  O  O     . ASP A 1 1937 ? 76.185  77.578  102.374 1.00 11.71  ? 1937 ASP A O     1 
ATOM   3865  C  CB    . ASP A 1 1937 ? 79.680  77.590  101.659 1.00 12.77  ? 1937 ASP A CB    1 
ATOM   3866  C  CG    . ASP A 1 1937 ? 79.814  76.297  102.448 1.00 19.19  ? 1937 ASP A CG    1 
ATOM   3867  O  OD1   . ASP A 1 1937 ? 78.792  75.752  102.913 1.00 22.76  ? 1937 ASP A OD1   1 
ATOM   3868  O  OD2   . ASP A 1 1937 ? 80.958  75.821  102.605 1.00 29.03  ? 1937 ASP A OD2   1 
ATOM   3869  N  N     . PHE A 1 1938 ? 77.107  77.236  100.353 1.00 11.37  ? 1938 PHE A N     1 
ATOM   3870  C  CA    . PHE A 1 1938 ? 75.897  76.633  99.801  1.00 8.40   ? 1938 PHE A CA    1 
ATOM   3871  C  C     . PHE A 1 1938 ? 75.497  75.376  100.566 1.00 8.38   ? 1938 PHE A C     1 
ATOM   3872  O  O     . PHE A 1 1938 ? 74.320  75.182  100.891 1.00 6.27   ? 1938 PHE A O     1 
ATOM   3873  C  CB    . PHE A 1 1938 ? 76.111  76.330  98.316  1.00 8.73   ? 1938 PHE A CB    1 
ATOM   3874  C  CG    . PHE A 1 1938 ? 75.014  75.517  97.693  1.00 10.46  ? 1938 PHE A CG    1 
ATOM   3875  C  CD1   . PHE A 1 1938 ? 73.846  76.120  97.262  1.00 8.46   ? 1938 PHE A CD1   1 
ATOM   3876  C  CD2   . PHE A 1 1938 ? 75.165  74.152  97.508  1.00 9.50   ? 1938 PHE A CD2   1 
ATOM   3877  C  CE1   . PHE A 1 1938 ? 72.840  75.376  96.680  1.00 8.67   ? 1938 PHE A CE1   1 
ATOM   3878  C  CE2   . PHE A 1 1938 ? 74.163  73.403  96.926  1.00 12.63  ? 1938 PHE A CE2   1 
ATOM   3879  C  CZ    . PHE A 1 1938 ? 72.999  74.016  96.511  1.00 11.26  ? 1938 PHE A CZ    1 
ATOM   3880  N  N     . GLN A 1 1939 ? 76.468  74.516  100.878 1.00 10.23  ? 1939 GLN A N     1 
ATOM   3881  C  CA    . GLN A 1 1939 ? 76.149  73.248  101.529 1.00 10.72  ? 1939 GLN A CA    1 
ATOM   3882  C  C     . GLN A 1 1939 ? 75.740  73.450  102.984 1.00 8.42   ? 1939 GLN A C     1 
ATOM   3883  O  O     . GLN A 1 1939 ? 74.807  72.797  103.469 1.00 8.12   ? 1939 GLN A O     1 
ATOM   3884  C  CB    . GLN A 1 1939 ? 77.340  72.297  101.428 1.00 12.10  ? 1939 GLN A CB    1 
ATOM   3885  C  CG    . GLN A 1 1939 ? 77.720  71.944  100.000 1.00 13.94  ? 1939 GLN A CG    1 
ATOM   3886  C  CD    . GLN A 1 1939 ? 78.935  71.043  99.924  1.00 31.50  ? 1939 GLN A CD    1 
ATOM   3887  O  OE1   . GLN A 1 1939 ? 79.940  71.389  99.304  1.00 31.07  ? 1939 GLN A OE1   1 
ATOM   3888  N  NE2   . GLN A 1 1939 ? 78.848  69.879  100.556 1.00 37.65  ? 1939 GLN A NE2   1 
ATOM   3889  N  N     . ALA A 1 1940 ? 76.428  74.343  103.699 1.00 8.75   ? 1940 ALA A N     1 
ATOM   3890  C  CA    . ALA A 1 1940 ? 76.071  74.616  105.088 1.00 8.49   ? 1940 ALA A CA    1 
ATOM   3891  C  C     . ALA A 1 1940 ? 74.680  75.230  105.184 1.00 5.98   ? 1940 ALA A C     1 
ATOM   3892  O  O     . ALA A 1 1940 ? 73.864  74.831  106.027 1.00 5.25   ? 1940 ALA A O     1 
ATOM   3893  C  CB    . ALA A 1 1940 ? 77.114  75.537  105.721 1.00 9.22   ? 1940 ALA A CB    1 
ATOM   3894  N  N     . MET A 1 1941 ? 74.390  76.202  104.316 1.00 5.92   ? 1941 MET A N     1 
ATOM   3895  C  CA    . MET A 1 1941 ? 73.059  76.797  104.286 1.00 5.28   ? 1941 MET A CA    1 
ATOM   3896  C  C     . MET A 1 1941 ? 72.008  75.763  103.910 1.00 5.42   ? 1941 MET A C     1 
ATOM   3897  O  O     . MET A 1 1941 ? 70.901  75.772  104.455 1.00 5.87   ? 1941 MET A O     1 
ATOM   3898  C  CB    . MET A 1 1941 ? 73.029  77.975  103.313 1.00 5.14   ? 1941 MET A CB    1 
ATOM   3899  C  CG    . MET A 1 1941 ? 73.866  79.169  103.749 1.00 7.84   ? 1941 MET A CG    1 
ATOM   3900  S  SD    . MET A 1 1941 ? 73.283  79.927  105.274 1.00 13.69  ? 1941 MET A SD    1 
ATOM   3901  C  CE    . MET A 1 1941 ? 71.603  80.338  104.815 1.00 5.65   ? 1941 MET A CE    1 
ATOM   3902  N  N     . GLY A 1 1942 ? 72.337  74.861  102.983 1.00 4.62   ? 1942 GLY A N     1 
ATOM   3903  C  CA    . GLY A 1 1942 ? 71.396  73.812  102.623 1.00 4.11   ? 1942 GLY A CA    1 
ATOM   3904  C  C     . GLY A 1 1942 ? 71.085  72.886  103.783 1.00 4.70   ? 1942 GLY A C     1 
ATOM   3905  O  O     . GLY A 1 1942 ? 69.933  72.510  104.002 1.00 6.33   ? 1942 GLY A O     1 
ATOM   3906  N  N     . ARG A 1 1943 ? 72.114  72.502  104.541 1.00 5.03   ? 1943 ARG A N     1 
ATOM   3907  C  CA    . ARG A 1 1943 ? 71.896  71.644  105.702 1.00 5.66   ? 1943 ARG A CA    1 
ATOM   3908  C  C     . ARG A 1 1943 ? 71.066  72.354  106.767 1.00 4.62   ? 1943 ARG A C     1 
ATOM   3909  O  O     . ARG A 1 1943 ? 70.170  71.751  107.377 1.00 6.35   ? 1943 ARG A O     1 
ATOM   3910  C  CB    . ARG A 1 1943 ? 73.238  71.188  106.274 1.00 6.42   ? 1943 ARG A CB    1 
ATOM   3911  C  CG    . ARG A 1 1943 ? 73.131  70.133  107.359 1.00 8.23   ? 1943 ARG A CG    1 
ATOM   3912  C  CD    . ARG A 1 1943 ? 74.472  69.448  107.588 1.00 10.90  ? 1943 ARG A CD    1 
ATOM   3913  N  NE    . ARG A 1 1943 ? 74.489  68.614  108.785 1.00 15.40  ? 1943 ARG A NE    1 
ATOM   3914  C  CZ    . ARG A 1 1943 ? 74.360  69.064  110.027 1.00 12.56  ? 1943 ARG A CZ    1 
ATOM   3915  N  NH1   . ARG A 1 1943 ? 74.235  70.355  110.288 1.00 9.03   ? 1943 ARG A NH1   1 
ATOM   3916  N  NH2   . ARG A 1 1943 ? 74.370  68.197  111.035 1.00 14.42  ? 1943 ARG A NH2   1 
ATOM   3917  N  N     . ILE A 1 1944 ? 71.345  73.638  107.001 1.00 3.40   ? 1944 ILE A N     1 
ATOM   3918  C  CA    . ILE A 1 1944 ? 70.553  74.409  107.957 1.00 3.86   ? 1944 ILE A CA    1 
ATOM   3919  C  C     . ILE A 1 1944 ? 69.102  74.504  107.498 1.00 3.75   ? 1944 ILE A C     1 
ATOM   3920  O  O     . ILE A 1 1944 ? 68.167  74.382  108.303 1.00 3.55   ? 1944 ILE A O     1 
ATOM   3921  C  CB    . ILE A 1 1944 ? 71.181  75.800  108.166 1.00 3.68   ? 1944 ILE A CB    1 
ATOM   3922  C  CG1   . ILE A 1 1944 ? 72.559  75.668  108.817 1.00 4.26   ? 1944 ILE A CG1   1 
ATOM   3923  C  CG2   . ILE A 1 1944 ? 70.276  76.683  109.001 1.00 2.58   ? 1944 ILE A CG2   1 
ATOM   3924  C  CD1   . ILE A 1 1944 ? 73.271  76.986  109.012 1.00 4.19   ? 1944 ILE A CD1   1 
ATOM   3925  N  N     . PHE A 1 1945 ? 68.891  74.725  106.197 1.00 4.14   ? 1945 PHE A N     1 
ATOM   3926  C  CA    . PHE A 1 1945 ? 67.538  74.780  105.659 1.00 4.35   ? 1945 PHE A CA    1 
ATOM   3927  C  C     . PHE A 1 1945 ? 66.829  73.443  105.815 1.00 4.02   ? 1945 PHE A C     1 
ATOM   3928  O  O     . PHE A 1 1945 ? 65.634  73.402  106.114 1.00 4.01   ? 1945 PHE A O     1 
ATOM   3929  C  CB    . PHE A 1 1945 ? 67.568  75.200  104.189 1.00 3.98   ? 1945 PHE A CB    1 
ATOM   3930  C  CG    . PHE A 1 1945 ? 67.875  76.656  103.976 1.00 4.49   ? 1945 PHE A CG    1 
ATOM   3931  C  CD1   . PHE A 1 1945 ? 67.433  77.613  104.874 1.00 4.32   ? 1945 PHE A CD1   1 
ATOM   3932  C  CD2   . PHE A 1 1945 ? 68.595  77.069  102.868 1.00 3.59   ? 1945 PHE A CD2   1 
ATOM   3933  C  CE1   . PHE A 1 1945 ? 67.710  78.952  104.676 1.00 4.61   ? 1945 PHE A CE1   1 
ATOM   3934  C  CE2   . PHE A 1 1945 ? 68.876  78.405  102.665 1.00 3.81   ? 1945 PHE A CE2   1 
ATOM   3935  C  CZ    . PHE A 1 1945 ? 68.432  79.348  103.570 1.00 4.71   ? 1945 PHE A CZ    1 
ATOM   3936  N  N     . VAL A 1 1946 ? 67.548  72.338  105.607 1.00 5.14   ? 1946 VAL A N     1 
ATOM   3937  C  CA    . VAL A 1 1946 ? 66.961  71.013  105.800 1.00 6.65   ? 1946 VAL A CA    1 
ATOM   3938  C  C     . VAL A 1 1946 ? 66.510  70.844  107.245 1.00 5.90   ? 1946 VAL A C     1 
ATOM   3939  O  O     . VAL A 1 1946 ? 65.392  70.382  107.523 1.00 8.63   ? 1946 VAL A O     1 
ATOM   3940  C  CB    . VAL A 1 1946 ? 67.967  69.919  105.396 1.00 6.14   ? 1946 VAL A CB    1 
ATOM   3941  C  CG1   . VAL A 1 1946 ? 67.526  68.564  105.919 1.00 6.83   ? 1946 VAL A CG1   1 
ATOM   3942  C  CG2   . VAL A 1 1946 ? 68.134  69.876  103.892 1.00 7.31   ? 1946 VAL A CG2   1 
ATOM   3943  N  N     . GLY A 1 1947 ? 67.378  71.220  108.186 1.00 3.78   ? 1947 GLY A N     1 
ATOM   3944  C  CA    . GLY A 1 1947 ? 67.024  71.108  109.592 1.00 4.05   ? 1947 GLY A CA    1 
ATOM   3945  C  C     . GLY A 1 1947 ? 65.796  71.923  109.948 1.00 4.17   ? 1947 GLY A C     1 
ATOM   3946  O  O     . GLY A 1 1947 ? 64.870  71.426  110.596 1.00 4.24   ? 1947 GLY A O     1 
ATOM   3947  N  N     . LEU A 1 1948 ? 65.759  73.183  109.509 1.00 4.15   ? 1948 LEU A N     1 
ATOM   3948  C  CA    . LEU A 1 1948 ? 64.616  74.034  109.829 1.00 4.43   ? 1948 LEU A CA    1 
ATOM   3949  C  C     . LEU A 1 1948 ? 63.343  73.591  109.115 1.00 4.14   ? 1948 LEU A C     1 
ATOM   3950  O  O     . LEU A 1 1948 ? 62.249  73.744  109.668 1.00 4.36   ? 1948 LEU A O     1 
ATOM   3951  C  CB    . LEU A 1 1948 ? 64.921  75.494  109.493 1.00 4.01   ? 1948 LEU A CB    1 
ATOM   3952  C  CG    . LEU A 1 1948 ? 66.088  76.163  110.220 1.00 4.36   ? 1948 LEU A CG    1 
ATOM   3953  C  CD1   . LEU A 1 1948 ? 66.718  77.232  109.343 1.00 3.31   ? 1948 LEU A CD1   1 
ATOM   3954  C  CD2   . LEU A 1 1948 ? 65.629  76.754  111.543 1.00 2.58   ? 1948 LEU A CD2   1 
ATOM   3955  N  N     . CYS A 1 1949 ? 63.458  73.051  107.899 1.00 4.83   ? 1949 CYS A N     1 
ATOM   3956  C  CA    . CYS A 1 1949 ? 62.283  72.574  107.180 1.00 5.48   ? 1949 CYS A CA    1 
ATOM   3957  C  C     . CYS A 1 1949 ? 61.674  71.363  107.869 1.00 5.65   ? 1949 CYS A C     1 
ATOM   3958  O  O     . CYS A 1 1949 ? 60.453  71.284  108.044 1.00 4.88   ? 1949 CYS A O     1 
ATOM   3959  C  CB    . CYS A 1 1949 ? 62.650  72.236  105.733 1.00 6.06   ? 1949 CYS A CB    1 
ATOM   3960  S  SG    . CYS A 1 1949 ? 62.880  73.660  104.647 1.00 7.63   ? 1949 CYS A SG    1 
ATOM   3961  N  N     . GLN A 1 1950 ? 62.510  70.400  108.267 1.00 6.22   ? 1950 GLN A N     1 
ATOM   3962  C  CA    . GLN A 1 1950 ? 61.968  69.222  108.937 1.00 7.90   ? 1950 GLN A CA    1 
ATOM   3963  C  C     . GLN A 1 1950 ? 61.454  69.561  110.331 1.00 8.39   ? 1950 GLN A C     1 
ATOM   3964  O  O     . GLN A 1 1950 ? 60.424  69.030  110.762 1.00 11.82  ? 1950 GLN A O     1 
ATOM   3965  C  CB    . GLN A 1 1950 ? 63.010  68.110  109.003 1.00 10.16  ? 1950 GLN A CB    1 
ATOM   3966  C  CG    . GLN A 1 1950 ? 63.537  67.657  107.662 1.00 10.63  ? 1950 GLN A CG    1 
ATOM   3967  C  CD    . GLN A 1 1950 ? 64.334  66.375  107.764 1.00 19.54  ? 1950 GLN A CD    1 
ATOM   3968  O  OE1   . GLN A 1 1950 ? 63.781  65.308  108.028 1.00 25.39  ? 1950 GLN A OE1   1 
ATOM   3969  N  NE2   . GLN A 1 1950 ? 65.641  66.473  107.565 1.00 22.84  ? 1950 GLN A NE2   1 
ATOM   3970  N  N     . VAL A 1 1951 ? 62.155  70.437  111.054 1.00 6.32   ? 1951 VAL A N     1 
ATOM   3971  C  CA    . VAL A 1 1951 ? 61.685  70.834  112.378 1.00 6.57   ? 1951 VAL A CA    1 
ATOM   3972  C  C     . VAL A 1 1951 ? 60.424  71.683  112.266 1.00 6.54   ? 1951 VAL A C     1 
ATOM   3973  O  O     . VAL A 1 1951 ? 59.491  71.542  113.066 1.00 9.92   ? 1951 VAL A O     1 
ATOM   3974  C  CB    . VAL A 1 1951 ? 62.802  71.568  113.145 1.00 7.35   ? 1951 VAL A CB    1 
ATOM   3975  C  CG1   . VAL A 1 1951 ? 62.244  72.259  114.380 1.00 4.18   ? 1951 VAL A CG1   1 
ATOM   3976  C  CG2   . VAL A 1 1951 ? 63.899  70.596  113.538 1.00 4.94   ? 1951 VAL A CG2   1 
ATOM   3977  N  N     . GLY A 1 1952 ? 60.363  72.555  111.265 1.00 5.99   ? 1952 GLY A N     1 
ATOM   3978  C  CA    . GLY A 1 1952 ? 59.295  73.528  111.177 1.00 4.19   ? 1952 GLY A CA    1 
ATOM   3979  C  C     . GLY A 1 1952 ? 59.575  74.820  111.902 1.00 3.62   ? 1952 GLY A C     1 
ATOM   3980  O  O     . GLY A 1 1952 ? 58.630  75.510  112.302 1.00 5.85   ? 1952 GLY A O     1 
ATOM   3981  N  N     . ALA A 1 1953 ? 60.841  75.167  112.085 1.00 2.86   ? 1953 ALA A N     1 
ATOM   3982  C  CA    . ALA A 1 1953 ? 61.245  76.309  112.885 1.00 2.56   ? 1953 ALA A CA    1 
ATOM   3983  C  C     . ALA A 1 1953 ? 61.606  77.497  111.999 1.00 2.35   ? 1953 ALA A C     1 
ATOM   3984  O  O     . ALA A 1 1953 ? 61.838  77.363  110.795 1.00 2.68   ? 1953 ALA A O     1 
ATOM   3985  C  CB    . ALA A 1 1953 ? 62.429  75.932  113.773 1.00 2.52   ? 1953 ALA A CB    1 
ATOM   3986  N  N     . TRP A 1 1954 ? 61.653  78.673  112.617 1.00 2.61   ? 1954 TRP A N     1 
ATOM   3987  C  CA    . TRP A 1 1954 ? 62.016  79.898  111.922 1.00 1.59   ? 1954 TRP A CA    1 
ATOM   3988  C  C     . TRP A 1 1954 ? 63.529  80.070  111.902 1.00 1.54   ? 1954 TRP A C     1 
ATOM   3989  O  O     . TRP A 1 1954 ? 64.204  79.871  112.915 1.00 2.17   ? 1954 TRP A O     1 
ATOM   3990  C  CB    . TRP A 1 1954 ? 61.369  81.114  112.586 1.00 1.32   ? 1954 TRP A CB    1 
ATOM   3991  C  CG    . TRP A 1 1954 ? 59.938  81.326  112.209 1.00 1.36   ? 1954 TRP A CG    1 
ATOM   3992  C  CD1   . TRP A 1 1954 ? 59.067  80.390  111.734 1.00 1.65   ? 1954 TRP A CD1   1 
ATOM   3993  C  CD2   . TRP A 1 1954 ? 59.211  82.559  112.266 1.00 1.09   ? 1954 TRP A CD2   1 
ATOM   3994  N  NE1   . TRP A 1 1954 ? 57.842  80.962  111.496 1.00 1.49   ? 1954 TRP A NE1   1 
ATOM   3995  C  CE2   . TRP A 1 1954 ? 57.904  82.293  111.814 1.00 1.24   ? 1954 TRP A CE2   1 
ATOM   3996  C  CE3   . TRP A 1 1954 ? 59.538  83.860  112.659 1.00 0.80   ? 1954 TRP A CE3   1 
ATOM   3997  C  CZ2   . TRP A 1 1954 ? 56.924  83.281  111.743 1.00 1.08   ? 1954 TRP A CZ2   1 
ATOM   3998  C  CZ3   . TRP A 1 1954 ? 58.565  84.840  112.584 1.00 0.88   ? 1954 TRP A CZ3   1 
ATOM   3999  C  CH2   . TRP A 1 1954 ? 57.273  84.545  112.132 1.00 0.83   ? 1954 TRP A CH2   1 
ATOM   4000  N  N     . GLY A 1 1955 ? 64.054  80.439  110.738 1.00 1.46   ? 1955 GLY A N     1 
ATOM   4001  C  CA    . GLY A 1 1955 ? 65.466  80.729  110.607 1.00 1.37   ? 1955 GLY A CA    1 
ATOM   4002  C  C     . GLY A 1 1955 ? 65.729  82.204  110.391 1.00 1.54   ? 1955 GLY A C     1 
ATOM   4003  O  O     . GLY A 1 1955 ? 65.301  82.776  109.384 1.00 2.32   ? 1955 GLY A O     1 
ATOM   4004  N  N     . CYS A 1 1956 ? 66.430  82.832  111.330 1.00 1.94   ? 1956 CYS A N     1 
ATOM   4005  C  CA    . CYS A 1 1956 ? 66.756  84.252  111.264 1.00 1.82   ? 1956 CYS A CA    1 
ATOM   4006  C  C     . CYS A 1 1956 ? 68.258  84.384  111.052 1.00 2.38   ? 1956 CYS A C     1 
ATOM   4007  O  O     . CYS A 1 1956 ? 69.048  84.084  111.953 1.00 3.84   ? 1956 CYS A O     1 
ATOM   4008  C  CB    . CYS A 1 1956 ? 66.312  84.977  112.532 1.00 3.39   ? 1956 CYS A CB    1 
ATOM   4009  S  SG    . CYS A 1 1956 ? 66.700  86.742  112.546 1.00 17.61  ? 1956 CYS A SG    1 
ATOM   4010  N  N     . PHE A 1 1957 ? 68.650  84.829  109.855 1.00 2.83   ? 1957 PHE A N     1 
ATOM   4011  C  CA    . PHE A 1 1957 ? 70.096  84.929  109.519 1.00 3.81   ? 1957 PHE A CA    1 
ATOM   4012  C  C     . PHE A 1 1957 ? 70.540  86.389  109.590 1.00 4.08   ? 1957 PHE A C     1 
ATOM   4013  O  O     . PHE A 1 1957 ? 70.221  87.172  108.669 1.00 4.40   ? 1957 PHE A O     1 
ATOM   4014  C  CB    . PHE A 1 1957 ? 70.296  84.306  108.134 1.00 3.39   ? 1957 PHE A CB    1 
ATOM   4015  C  CG    . PHE A 1 1957 ? 69.801  82.869  108.028 1.00 2.81   ? 1957 PHE A CG    1 
ATOM   4016  C  CD1   . PHE A 1 1957 ? 68.485  82.593  107.675 1.00 2.42   ? 1957 PHE A CD1   1 
ATOM   4017  C  CD2   . PHE A 1 1957 ? 70.652  81.800  108.285 1.00 3.50   ? 1957 PHE A CD2   1 
ATOM   4018  C  CE1   . PHE A 1 1957 ? 68.036  81.285  107.582 1.00 2.76   ? 1957 PHE A CE1   1 
ATOM   4019  C  CE2   . PHE A 1 1957 ? 70.198  80.494  108.188 1.00 2.79   ? 1957 PHE A CE2   1 
ATOM   4020  C  CZ    . PHE A 1 1957 ? 68.892  80.239  107.838 1.00 2.29   ? 1957 PHE A CZ    1 
ATOM   4021  N  N     . ASP A 1 1958 ? 71.261  86.747  110.657 1.00 5.62   ? 1958 ASP A N     1 
ATOM   4022  C  CA    . ASP A 1 1958 ? 71.764  88.139  110.817 1.00 5.85   ? 1958 ASP A CA    1 
ATOM   4023  C  C     . ASP A 1 1958 ? 73.034  88.310  109.975 1.00 8.94   ? 1958 ASP A C     1 
ATOM   4024  O  O     . ASP A 1 1958 ? 73.659  87.281  109.636 1.00 10.62  ? 1958 ASP A O     1 
ATOM   4025  C  CB    . ASP A 1 1958 ? 71.985  88.472  112.284 1.00 8.80   ? 1958 ASP A CB    1 
ATOM   4026  C  CG    . ASP A 1 1958 ? 70.810  88.174  113.203 1.00 11.42  ? 1958 ASP A CG    1 
ATOM   4027  O  OD1   . ASP A 1 1958 ? 69.760  87.731  112.689 1.00 11.12  ? 1958 ASP A OD1   1 
ATOM   4028  O  OD2   . ASP A 1 1958 ? 70.958  88.376  114.426 1.00 12.82  ? 1958 ASP A OD2   1 
ATOM   4029  N  N     . GLU A 1 1959 ? 73.398  89.556  109.653 1.00 10.00  ? 1959 GLU A N     1 
ATOM   4030  C  CA    . GLU A 1 1959 ? 74.593  89.811  108.806 1.00 10.74  ? 1959 GLU A CA    1 
ATOM   4031  C  C     . GLU A 1 1959 ? 74.563  88.851  107.609 1.00 9.35   ? 1959 GLU A C     1 
ATOM   4032  O  O     . GLU A 1 1959 ? 75.628  88.293  107.269 1.00 9.54   ? 1959 GLU A O     1 
ATOM   4033  C  CB    . GLU A 1 1959 ? 75.877  89.626  109.616 1.00 10.75  ? 1959 GLU A CB    1 
ATOM   4034  C  CG    . GLU A 1 1959 ? 76.307  90.883  110.365 1.00 16.66  ? 1959 GLU A CG    1 
ATOM   4035  C  CD    . GLU A 1 1959 ? 75.197  91.548  111.157 1.00 23.26  ? 1959 GLU A CD    1 
ATOM   4036  O  OE1   . GLU A 1 1959 ? 74.626  90.891  112.053 1.00 25.90  ? 1959 GLU A OE1   1 
ATOM   4037  O  OE2   . GLU A 1 1959 ? 74.905  92.729  110.875 1.00 21.62  ? 1959 GLU A OE2   1 
ATOM   4038  N  N     . PHE A 1 1960 ? 73.387  88.666  107.002 1.00 7.63   ? 1960 PHE A N     1 
ATOM   4039  C  CA    . PHE A 1 1960 ? 73.264  87.733  105.888 1.00 6.02   ? 1960 PHE A CA    1 
ATOM   4040  C  C     . PHE A 1 1960 ? 74.018  88.217  104.656 1.00 7.46   ? 1960 PHE A C     1 
ATOM   4041  O  O     . PHE A 1 1960 ? 74.393  87.404  103.804 1.00 6.50   ? 1960 PHE A O     1 
ATOM   4042  C  CB    . PHE A 1 1960 ? 71.785  87.508  105.580 1.00 4.55   ? 1960 PHE A CB    1 
ATOM   4043  C  CG    . PHE A 1 1960 ? 71.530  86.568  104.440 1.00 4.62   ? 1960 PHE A CG    1 
ATOM   4044  C  CD1   . PHE A 1 1960 ? 71.582  85.198  104.633 1.00 3.92   ? 1960 PHE A CD1   1 
ATOM   4045  C  CD2   . PHE A 1 1960 ? 71.171  87.052  103.194 1.00 3.90   ? 1960 PHE A CD2   1 
ATOM   4046  C  CE1   . PHE A 1 1960 ? 71.327  84.329  103.592 1.00 3.94   ? 1960 PHE A CE1   1 
ATOM   4047  C  CE2   . PHE A 1 1960 ? 70.906  86.187  102.153 1.00 5.40   ? 1960 PHE A CE2   1 
ATOM   4048  C  CZ    . PHE A 1 1960 ? 70.988  84.824  102.352 1.00 4.00   ? 1960 PHE A CZ    1 
ATOM   4049  N  N     . ASN A 1 1961 ? 74.260  89.524  104.548 1.00 7.53   ? 1961 ASN A N     1 
ATOM   4050  C  CA    . ASN A 1 1961 ? 75.064  90.043  103.449 1.00 7.59   ? 1961 ASN A CA    1 
ATOM   4051  C  C     . ASN A 1 1961 ? 76.557  89.834  103.664 1.00 8.58   ? 1961 ASN A C     1 
ATOM   4052  O  O     . ASN A 1 1961 ? 77.350  90.252  102.815 1.00 11.46  ? 1961 ASN A O     1 
ATOM   4053  C  CB    . ASN A 1 1961 ? 74.768  91.528  103.233 1.00 8.35   ? 1961 ASN A CB    1 
ATOM   4054  C  CG    . ASN A 1 1961 ? 74.939  92.350  104.496 1.00 14.20  ? 1961 ASN A CG    1 
ATOM   4055  O  OD1   . ASN A 1 1961 ? 75.272  91.823  105.556 1.00 16.71  ? 1961 ASN A OD1   1 
ATOM   4056  N  ND2   . ASN A 1 1961 ? 74.709  93.652  104.386 1.00 14.14  ? 1961 ASN A ND2   1 
ATOM   4057  N  N     . ARG A 1 1962 ? 76.958  89.207  104.773 1.00 9.63   ? 1962 ARG A N     1 
ATOM   4058  C  CA    . ARG A 1 1962 ? 78.362  88.869  104.968 1.00 10.66  ? 1962 ARG A CA    1 
ATOM   4059  C  C     . ARG A 1 1962 ? 78.752  87.604  104.214 1.00 11.90  ? 1962 ARG A C     1 
ATOM   4060  O  O     . ARG A 1 1962 ? 79.943  87.289  104.132 1.00 14.98  ? 1962 ARG A O     1 
ATOM   4061  C  CB    . ARG A 1 1962 ? 78.665  88.725  106.462 1.00 9.96   ? 1962 ARG A CB    1 
ATOM   4062  C  CG    . ARG A 1 1962 ? 78.521  90.034  107.225 1.00 12.22  ? 1962 ARG A CG    1 
ATOM   4063  C  CD    . ARG A 1 1962 ? 79.488  90.158  108.396 1.00 13.98  ? 1962 ARG A CD    1 
ATOM   4064  N  NE    . ARG A 1 1962 ? 79.329  89.095  109.381 1.00 12.41  ? 1962 ARG A NE    1 
ATOM   4065  C  CZ    . ARG A 1 1962 ? 80.313  88.317  109.810 1.00 11.80  ? 1962 ARG A CZ    1 
ATOM   4066  N  NH1   . ARG A 1 1962 ? 81.548  88.449  109.356 1.00 10.97  ? 1962 ARG A NH1   1 
ATOM   4067  N  NH2   . ARG A 1 1962 ? 80.053  87.388  110.725 1.00 11.80  ? 1962 ARG A NH2   1 
ATOM   4068  N  N     . LEU A 1 1963 ? 77.779  86.878  103.668 1.00 8.98   ? 1963 LEU A N     1 
ATOM   4069  C  CA    . LEU A 1 1963 ? 78.074  85.780  102.759 1.00 9.42   ? 1963 LEU A CA    1 
ATOM   4070  C  C     . LEU A 1 1963 ? 78.651  86.314  101.455 1.00 11.35  ? 1963 LEU A C     1 
ATOM   4071  O  O     . LEU A 1 1963 ? 78.462  87.477  101.096 1.00 14.52  ? 1963 LEU A O     1 
ATOM   4072  C  CB    . LEU A 1 1963 ? 76.814  84.967  102.458 1.00 10.72  ? 1963 LEU A CB    1 
ATOM   4073  C  CG    . LEU A 1 1963 ? 76.380  83.831  103.385 1.00 8.15   ? 1963 LEU A CG    1 
ATOM   4074  C  CD1   . LEU A 1 1963 ? 76.116  84.333  104.785 1.00 11.35  ? 1963 LEU A CD1   1 
ATOM   4075  C  CD2   . LEU A 1 1963 ? 75.146  83.139  102.824 1.00 5.66   ? 1963 LEU A CD2   1 
ATOM   4076  N  N     . GLU A 1 1964 ? 79.367  85.449  100.744 1.00 13.40  ? 1964 GLU A N     1 
ATOM   4077  C  CA    . GLU A 1 1964 ? 79.849  85.804  99.418  1.00 14.38  ? 1964 GLU A CA    1 
ATOM   4078  C  C     . GLU A 1 1964 ? 78.682  85.898  98.440  1.00 11.44  ? 1964 GLU A C     1 
ATOM   4079  O  O     . GLU A 1 1964 ? 77.661  85.221  98.591  1.00 11.85  ? 1964 GLU A O     1 
ATOM   4080  C  CB    . GLU A 1 1964 ? 80.872  84.778  98.932  1.00 15.26  ? 1964 GLU A CB    1 
ATOM   4081  C  CG    . GLU A 1 1964 ? 82.113  84.694  99.805  1.00 18.34  ? 1964 GLU A CG    1 
ATOM   4082  C  CD    . GLU A 1 1964 ? 82.879  83.400  99.611  1.00 37.38  ? 1964 GLU A CD    1 
ATOM   4083  O  OE1   . GLU A 1 1964 ? 84.013  83.298  100.123 1.00 44.78  ? 1964 GLU A OE1   1 
ATOM   4084  O  OE2   . GLU A 1 1964 ? 82.347  82.486  98.948  1.00 36.83  ? 1964 GLU A OE2   1 
ATOM   4085  N  N     . GLU A 1 1965 ? 78.841  86.756  97.429  1.00 10.52  ? 1965 GLU A N     1 
ATOM   4086  C  CA    . GLU A 1 1965 ? 77.766  86.980  96.467  1.00 10.60  ? 1965 GLU A CA    1 
ATOM   4087  C  C     . GLU A 1 1965 ? 77.418  85.701  95.715  1.00 9.19   ? 1965 GLU A C     1 
ATOM   4088  O  O     . GLU A 1 1965 ? 76.238  85.412  95.474  1.00 9.26   ? 1965 GLU A O     1 
ATOM   4089  C  CB    . GLU A 1 1965 ? 78.160  88.089  95.490  1.00 12.51  ? 1965 GLU A CB    1 
ATOM   4090  C  CG    . GLU A 1 1965 ? 78.612  89.375  96.163  1.00 17.43  ? 1965 GLU A CG    1 
ATOM   4091  C  CD    . GLU A 1 1965 ? 78.210  90.615  95.389  1.00 29.31  ? 1965 GLU A CD    1 
ATOM   4092  O  OE1   . GLU A 1 1965 ? 78.652  91.721  95.766  1.00 25.82  ? 1965 GLU A OE1   1 
ATOM   4093  O  OE2   . GLU A 1 1965 ? 77.453  90.485  94.404  1.00 36.55  ? 1965 GLU A OE2   1 
ATOM   4094  N  N     . ARG A 1 1966 ? 78.434  84.922  95.335  1.00 7.06   ? 1966 ARG A N     1 
ATOM   4095  C  CA    . ARG A 1 1966 ? 78.182  83.653  94.661  1.00 7.40   ? 1966 ARG A CA    1 
ATOM   4096  C  C     . ARG A 1 1966 ? 77.412  82.694  95.564  1.00 7.39   ? 1966 ARG A C     1 
ATOM   4097  O  O     . ARG A 1 1966 ? 76.515  81.978  95.103  1.00 6.57   ? 1966 ARG A O     1 
ATOM   4098  C  CB    . ARG A 1 1966 ? 79.505  83.039  94.196  1.00 11.30  ? 1966 ARG A CB    1 
ATOM   4099  C  CG    . ARG A 1 1966 ? 80.468  82.660  95.311  1.00 14.61  ? 1966 ARG A CG    1 
ATOM   4100  C  CD    . ARG A 1 1966 ? 81.856  82.364  94.767  1.00 23.92  ? 1966 ARG A CD    1 
ATOM   4101  N  NE    . ARG A 1 1966 ? 82.781  81.963  95.820  1.00 26.78  ? 1966 ARG A NE    1 
ATOM   4102  C  CZ    . ARG A 1 1966 ? 83.126  80.708  96.077  1.00 28.01  ? 1966 ARG A CZ    1 
ATOM   4103  N  NH1   . ARG A 1 1966 ? 82.637  79.700  95.374  1.00 23.43  ? 1966 ARG A NH1   1 
ATOM   4104  N  NH2   . ARG A 1 1966 ? 83.981  80.459  97.064  1.00 36.99  ? 1966 ARG A NH2   1 
ATOM   4105  N  N     . MET A 1 1967 ? 77.732  82.686  96.860  1.00 9.26   ? 1967 MET A N     1 
ATOM   4106  C  CA    . MET A 1 1967 ? 76.997  81.840  97.794  1.00 8.92   ? 1967 MET A CA    1 
ATOM   4107  C  C     . MET A 1 1967 ? 75.559  82.316  97.954  1.00 6.12   ? 1967 MET A C     1 
ATOM   4108  O  O     . MET A 1 1967 ? 74.643  81.498  98.085  1.00 5.45   ? 1967 MET A O     1 
ATOM   4109  C  CB    . MET A 1 1967 ? 77.713  81.804  99.143  1.00 8.21   ? 1967 MET A CB    1 
ATOM   4110  C  CG    . MET A 1 1967 ? 78.954  80.929  99.147  1.00 10.07  ? 1967 MET A CG    1 
ATOM   4111  S  SD    . MET A 1 1967 ? 78.700  79.384  98.252  1.00 12.80  ? 1967 MET A SD    1 
ATOM   4112  C  CE    . MET A 1 1967 ? 80.370  78.743  98.197  1.00 15.04  ? 1967 MET A CE    1 
ATOM   4113  N  N     . LEU A 1 1968 ? 75.343  83.633  97.946  1.00 4.78   ? 1968 LEU A N     1 
ATOM   4114  C  CA    . LEU A 1 1968 ? 73.984  84.165  98.003  1.00 5.40   ? 1968 LEU A CA    1 
ATOM   4115  C  C     . LEU A 1 1968 ? 73.178  83.714  96.792  1.00 7.85   ? 1968 LEU A C     1 
ATOM   4116  O  O     . LEU A 1 1968 ? 72.031  83.258  96.917  1.00 9.40   ? 1968 LEU A O     1 
ATOM   4117  C  CB    . LEU A 1 1968 ? 74.032  85.692  98.074  1.00 6.42   ? 1968 LEU A CB    1 
ATOM   4118  C  CG    . LEU A 1 1968 ? 74.698  86.310  99.305  1.00 8.77   ? 1968 LEU A CG    1 
ATOM   4119  C  CD1   . LEU A 1 1968 ? 74.938  87.799  99.096  1.00 8.83   ? 1968 LEU A CD1   1 
ATOM   4120  C  CD2   . LEU A 1 1968 ? 73.887  86.060  100.556 1.00 5.65   ? 1968 LEU A CD2   1 
ATOM   4121  N  N     . SER A 1 1969 ? 73.780  83.820  95.603  1.00 5.83   ? 1969 SER A N     1 
ATOM   4122  C  CA    . SER A 1 1969 ? 73.114  83.366  94.389  1.00 5.07   ? 1969 SER A CA    1 
ATOM   4123  C  C     . SER A 1 1969 ? 72.784  81.882  94.467  1.00 6.49   ? 1969 SER A C     1 
ATOM   4124  O  O     . SER A 1 1969 ? 71.669  81.469  94.128  1.00 8.28   ? 1969 SER A O     1 
ATOM   4125  C  CB    . SER A 1 1969 ? 73.991  83.661  93.171  1.00 6.98   ? 1969 SER A CB    1 
ATOM   4126  O  OG    . SER A 1 1969 ? 73.517  82.985  92.021  1.00 12.15  ? 1969 SER A OG    1 
ATOM   4127  N  N     . ALA A 1 1970 ? 73.735  81.068  94.931  1.00 6.50   ? 1970 ALA A N     1 
ATOM   4128  C  CA    . ALA A 1 1970 ? 73.494  79.632  95.039  1.00 6.47   ? 1970 ALA A CA    1 
ATOM   4129  C  C     . ALA A 1 1970 ? 72.373  79.322  96.027  1.00 7.24   ? 1970 ALA A C     1 
ATOM   4130  O  O     . ALA A 1 1970 ? 71.526  78.460  95.765  1.00 10.25  ? 1970 ALA A O     1 
ATOM   4131  C  CB    . ALA A 1 1970 ? 74.783  78.920  95.446  1.00 6.61   ? 1970 ALA A CB    1 
ATOM   4132  N  N     . VAL A 1 1971 ? 72.352  80.013  97.170  1.00 4.83   ? 1971 VAL A N     1 
ATOM   4133  C  CA    . VAL A 1 1971 ? 71.338  79.779  98.194  1.00 6.26   ? 1971 VAL A CA    1 
ATOM   4134  C  C     . VAL A 1 1971 ? 69.956  80.228  97.728  1.00 5.45   ? 1971 VAL A C     1 
ATOM   4135  O  O     . VAL A 1 1971 ? 68.934  79.726  98.229  1.00 5.40   ? 1971 VAL A O     1 
ATOM   4136  C  CB    . VAL A 1 1971 ? 71.783  80.486  99.493  1.00 6.03   ? 1971 VAL A CB    1 
ATOM   4137  C  CG1   . VAL A 1 1971 ? 70.622  80.708  100.455 1.00 5.66   ? 1971 VAL A CG1   1 
ATOM   4138  C  CG2   . VAL A 1 1971 ? 72.896  79.700  100.165 1.00 5.58   ? 1971 VAL A CG2   1 
ATOM   4139  N  N     . SER A 1 1972 ? 69.906  81.160  96.771  1.00 5.11   ? 1972 SER A N     1 
ATOM   4140  C  CA    . SER A 1 1972 ? 68.624  81.644  96.267  1.00 6.25   ? 1972 SER A CA    1 
ATOM   4141  C  C     . SER A 1 1972 ? 67.731  80.513  95.765  1.00 6.87   ? 1972 SER A C     1 
ATOM   4142  O  O     . SER A 1 1972 ? 66.512  80.550  95.958  1.00 7.79   ? 1972 SER A O     1 
ATOM   4143  C  CB    . SER A 1 1972 ? 68.851  82.666  95.155  1.00 6.34   ? 1972 SER A CB    1 
ATOM   4144  O  OG    . SER A 1 1972 ? 69.488  82.072  94.039  1.00 8.14   ? 1972 SER A OG    1 
ATOM   4145  N  N     . GLN A 1 1973 ? 68.308  79.495  95.119  1.00 8.56   ? 1973 GLN A N     1 
ATOM   4146  C  CA    . GLN A 1 1973 ? 67.457  78.449  94.558  1.00 10.01  ? 1973 GLN A CA    1 
ATOM   4147  C  C     . GLN A 1 1973 ? 66.932  77.501  95.631  1.00 8.40   ? 1973 GLN A C     1 
ATOM   4148  O  O     . GLN A 1 1973 ? 65.803  77.008  95.515  1.00 8.74   ? 1973 GLN A O     1 
ATOM   4149  C  CB    . GLN A 1 1973 ? 68.198  77.685  93.453  1.00 10.73  ? 1973 GLN A CB    1 
ATOM   4150  C  CG    . GLN A 1 1973 ? 69.441  76.910  93.857  1.00 17.11  ? 1973 GLN A CG    1 
ATOM   4151  C  CD    . GLN A 1 1973 ? 69.122  75.529  94.399  1.00 27.37  ? 1973 GLN A CD    1 
ATOM   4152  O  OE1   . GLN A 1 1973 ? 69.851  74.995  95.234  1.00 26.71  ? 1973 GLN A OE1   1 
ATOM   4153  N  NE2   . GLN A 1 1973 ? 68.010  74.961  93.954  1.00 24.96  ? 1973 GLN A NE2   1 
ATOM   4154  N  N     . GLN A 1 1974 ? 67.714  77.248  96.685  1.00 7.74   ? 1974 GLN A N     1 
ATOM   4155  C  CA    . GLN A 1 1974 ? 67.174  76.527  97.833  1.00 6.94   ? 1974 GLN A CA    1 
ATOM   4156  C  C     . GLN A 1 1974 ? 66.019  77.298  98.454  1.00 6.62   ? 1974 GLN A C     1 
ATOM   4157  O  O     . GLN A 1 1974 ? 64.972  76.720  98.776  1.00 7.24   ? 1974 GLN A O     1 
ATOM   4158  C  CB    . GLN A 1 1974 ? 68.267  76.284  98.875  1.00 6.82   ? 1974 GLN A CB    1 
ATOM   4159  C  CG    . GLN A 1 1974 ? 69.584  75.798  98.308  1.00 7.95   ? 1974 GLN A CG    1 
ATOM   4160  C  CD    . GLN A 1 1974 ? 70.632  75.558  99.376  1.00 7.45   ? 1974 GLN A CD    1 
ATOM   4161  O  OE1   . GLN A 1 1974 ? 71.200  74.471  99.469  1.00 9.03   ? 1974 GLN A OE1   1 
ATOM   4162  N  NE2   . GLN A 1 1974 ? 70.894  76.575  100.187 1.00 6.50   ? 1974 GLN A NE2   1 
ATOM   4163  N  N     . VAL A 1 1975 ? 66.187  78.614  98.609  1.00 6.98   ? 1975 VAL A N     1 
ATOM   4164  C  CA    . VAL A 1 1975 ? 65.110  79.431  99.161  1.00 6.97   ? 1975 VAL A CA    1 
ATOM   4165  C  C     . VAL A 1 1975 ? 63.875  79.345  98.273  1.00 8.92   ? 1975 VAL A C     1 
ATOM   4166  O  O     . VAL A 1 1975 ? 62.745  79.216  98.761  1.00 9.68   ? 1975 VAL A O     1 
ATOM   4167  C  CB    . VAL A 1 1975 ? 65.580  80.886  99.345  1.00 5.91   ? 1975 VAL A CB    1 
ATOM   4168  C  CG1   . VAL A 1 1975 ? 64.419  81.772  99.772  1.00 4.55   ? 1975 VAL A CG1   1 
ATOM   4169  C  CG2   . VAL A 1 1975 ? 66.710  80.954  100.360 1.00 4.14   ? 1975 VAL A CG2   1 
ATOM   4170  N  N     . GLN A 1 1976 ? 64.076  79.394  96.955  1.00 6.49   ? 1976 GLN A N     1 
ATOM   4171  C  CA    . GLN A 1 1976 ? 62.959  79.353  96.017  1.00 7.70   ? 1976 GLN A CA    1 
ATOM   4172  C  C     . GLN A 1 1976 ? 62.213  78.025  96.091  1.00 9.40   ? 1976 GLN A C     1 
ATOM   4173  O  O     . GLN A 1 1976 ? 60.977  77.998  96.095  1.00 16.47  ? 1976 GLN A O     1 
ATOM   4174  C  CB    . GLN A 1 1976 ? 63.467  79.609  94.598  1.00 11.02  ? 1976 GLN A CB    1 
ATOM   4175  C  CG    . GLN A 1 1976 ? 62.396  80.068  93.627  1.00 14.20  ? 1976 GLN A CG    1 
ATOM   4176  C  CD    . GLN A 1 1976 ? 62.977  80.596  92.331  1.00 25.71  ? 1976 GLN A CD    1 
ATOM   4177  O  OE1   . GLN A 1 1976 ? 62.810  81.768  91.994  1.00 30.64  ? 1976 GLN A OE1   1 
ATOM   4178  N  NE2   . GLN A 1 1976 ? 63.670  79.732  91.598  1.00 26.35  ? 1976 GLN A NE2   1 
ATOM   4179  N  N     . CYS A 1 1977 ? 62.943  76.907  96.141  1.00 7.22   ? 1977 CYS A N     1 
ATOM   4180  C  CA    . CYS A 1 1977 ? 62.263  75.613  96.179  1.00 8.34   ? 1977 CYS A CA    1 
ATOM   4181  C  C     . CYS A 1 1977 ? 61.536  75.412  97.505  1.00 10.00  ? 1977 CYS A C     1 
ATOM   4182  O  O     . CYS A 1 1977 ? 60.437  74.842  97.538  1.00 13.28  ? 1977 CYS A O     1 
ATOM   4183  C  CB    . CYS A 1 1977 ? 63.249  74.471  95.918  1.00 9.44   ? 1977 CYS A CB    1 
ATOM   4184  S  SG    . CYS A 1 1977 ? 64.500  74.196  97.185  1.00 32.90  ? 1977 CYS A SG    1 
ATOM   4185  N  N     . ILE A 1 1978 ? 62.121  75.889  98.606  1.00 7.80   ? 1978 ILE A N     1 
ATOM   4186  C  CA    . ILE A 1 1978 ? 61.434  75.808  99.893  1.00 7.82   ? 1978 ILE A CA    1 
ATOM   4187  C  C     . ILE A 1 1978 ? 60.164  76.654  99.877  1.00 8.59   ? 1978 ILE A C     1 
ATOM   4188  O  O     . ILE A 1 1978 ? 59.120  76.248  100.405 1.00 9.44   ? 1978 ILE A O     1 
ATOM   4189  C  CB    . ILE A 1 1978 ? 62.388  76.215  101.030 1.00 10.26  ? 1978 ILE A CB    1 
ATOM   4190  C  CG1   . ILE A 1 1978 ? 63.496  75.169  101.173 1.00 9.46   ? 1978 ILE A CG1   1 
ATOM   4191  C  CG2   . ILE A 1 1978 ? 61.631  76.372  102.335 1.00 7.20   ? 1978 ILE A CG2   1 
ATOM   4192  C  CD1   . ILE A 1 1978 ? 64.790  75.714  101.717 1.00 5.01   ? 1978 ILE A CD1   1 
ATOM   4193  N  N     . GLN A 1 1979 ? 60.246  77.839  99.268  1.00 9.72   ? 1979 GLN A N     1 
ATOM   4194  C  CA    . GLN A 1 1979 ? 59.063  78.739  99.208  1.00 9.77   ? 1979 GLN A CA    1 
ATOM   4195  C  C     . GLN A 1 1979 ? 57.952  78.054  98.393  1.00 13.19  ? 1979 GLN A C     1 
ATOM   4196  O  O     . GLN A 1 1979 ? 56.766  78.212  98.758  1.00 18.01  ? 1979 GLN A O     1 
ATOM   4197  C  CB    . GLN A 1 1979 ? 59.445  80.106  98.637  1.00 8.46   ? 1979 GLN A CB    1 
ATOM   4198  C  CG    . GLN A 1 1979 ? 60.248  80.973  99.602  1.00 8.80   ? 1979 GLN A CG    1 
ATOM   4199  C  CD    . GLN A 1 1979 ? 60.518  82.365  99.074  1.00 6.79   ? 1979 GLN A CD    1 
ATOM   4200  O  OE1   . GLN A 1 1979 ? 60.125  82.721  97.958  1.00 8.77   ? 1979 GLN A OE1   1 
ATOM   4201  N  NE2   . GLN A 1 1979 ? 61.198  83.169  99.879  1.00 4.14   ? 1979 GLN A NE2   1 
ATOM   4202  N  N     . GLU A 1 1980 ? 58.325  77.313  97.345  1.00 13.47  ? 1980 GLU A N     1 
ATOM   4203  C  CA    . GLU A 1 1980 ? 57.325  76.581  96.522  1.00 15.64  ? 1980 GLU A CA    1 
ATOM   4204  C  C     . GLU A 1 1980 ? 56.643  75.506  97.383  1.00 18.16  ? 1980 GLU A C     1 
ATOM   4205  O  O     . GLU A 1 1980 ? 55.408  75.345  97.262  1.00 23.43  ? 1980 GLU A O     1 
ATOM   4206  C  CB    . GLU A 1 1980 ? 57.990  75.952  95.299  1.00 17.19  ? 1980 GLU A CB    1 
ATOM   4207  C  CG    . GLU A 1 1980 ? 58.658  76.978  94.389  1.00 27.83  ? 1980 GLU A CG    1 
ATOM   4208  C  CD    . GLU A 1 1980 ? 57.770  78.168  94.077  1.00 48.39  ? 1980 GLU A CD    1 
ATOM   4209  O  OE1   . GLU A 1 1980 ? 56.679  77.960  93.505  1.00 61.30  ? 1980 GLU A OE1   1 
ATOM   4210  O  OE2   . GLU A 1 1980 ? 58.169  79.302  94.409  1.00 47.26  ? 1980 GLU A OE2   1 
ATOM   4211  N  N     . ALA A 1 1981 ? 57.417  74.800  98.212  1.00 16.76  ? 1981 ALA A N     1 
ATOM   4212  C  CA    . ALA A 1 1981 ? 56.845  73.756  99.096  1.00 18.40  ? 1981 ALA A CA    1 
ATOM   4213  C  C     . ALA A 1 1981 ? 55.840  74.395  100.057 1.00 21.25  ? 1981 ALA A C     1 
ATOM   4214  O  O     . ALA A 1 1981 ? 54.772  73.799  100.315 1.00 23.30  ? 1981 ALA A O     1 
ATOM   4215  C  CB    . ALA A 1 1981 ? 57.953  73.043  99.838  1.00 17.17  ? 1981 ALA A CB    1 
ATOM   4216  N  N     . LEU A 1 1982 ? 56.169  75.581  100.573 1.00 19.22  ? 1982 LEU A N     1 
ATOM   4217  C  CA    . LEU A 1 1982 ? 55.245  76.296  101.491 1.00 17.51  ? 1982 LEU A CA    1 
ATOM   4218  C  C     . LEU A 1 1982 ? 53.952  76.633  100.734 1.00 21.42  ? 1982 LEU A C     1 
ATOM   4219  O  O     . LEU A 1 1982 ? 52.865  76.562  101.349 1.00 24.46  ? 1982 LEU A O     1 
ATOM   4220  C  CB    . LEU A 1 1982 ? 55.943  77.550  102.009 1.00 15.41  ? 1982 LEU A CB    1 
ATOM   4221  C  CG    . LEU A 1 1982 ? 57.258  77.316  102.759 1.00 11.39  ? 1982 LEU A CG    1 
ATOM   4222  C  CD1   . LEU A 1 1982 ? 57.968  78.633  103.010 1.00 9.47   ? 1982 LEU A CD1   1 
ATOM   4223  C  CD2   . LEU A 1 1982 ? 56.997  76.587  104.065 1.00 12.88  ? 1982 LEU A CD2   1 
ATOM   4224  N  N     . ARG A 1 1983 ? 54.071  76.988  99.452  1.00 20.68  ? 1983 ARG A N     1 
ATOM   4225  C  CA    . ARG A 1 1983 ? 52.882  77.365  98.643  1.00 20.24  ? 1983 ARG A CA    1 
ATOM   4226  C  C     . ARG A 1 1983 ? 52.004  76.128  98.379  1.00 28.79  ? 1983 ARG A C     1 
ATOM   4227  O  O     . ARG A 1 1983 ? 50.763  76.280  98.387  1.00 35.47  ? 1983 ARG A O     1 
ATOM   4228  C  CB    . ARG A 1 1983 ? 53.341  78.071  97.361  1.00 16.09  ? 1983 ARG A CB    1 
ATOM   4229  C  CG    . ARG A 1 1983 ? 53.879  79.451  97.708  1.00 17.61  ? 1983 ARG A CG    1 
ATOM   4230  C  CD    . ARG A 1 1983 ? 54.556  80.164  96.554  1.00 19.89  ? 1983 ARG A CD    1 
ATOM   4231  N  NE    . ARG A 1 1983 ? 55.108  81.443  97.014  1.00 18.68  ? 1983 ARG A NE    1 
ATOM   4232  C  CZ    . ARG A 1 1983 ? 56.402  81.730  97.020  1.00 21.77  ? 1983 ARG A CZ    1 
ATOM   4233  N  NH1   . ARG A 1 1983 ? 57.263  80.883  96.488  1.00 25.17  ? 1983 ARG A NH1   1 
ATOM   4234  N  NH2   . ARG A 1 1983 ? 56.828  82.856  97.562  1.00 18.13  ? 1983 ARG A NH2   1 
ATOM   4235  N  N     . GLU A 1 1984 ? 52.608  74.956  98.156  1.00 30.23  ? 1984 GLU A N     1 
ATOM   4236  C  CA    . GLU A 1 1984 ? 51.776  73.732  97.991  1.00 31.96  ? 1984 GLU A CA    1 
ATOM   4237  C  C     . GLU A 1 1984 ? 51.053  73.460  99.323  1.00 33.62  ? 1984 GLU A C     1 
ATOM   4238  O  O     . GLU A 1 1984 ? 49.918  72.938  99.279  1.00 40.23  ? 1984 GLU A O     1 
ATOM   4239  C  CB    . GLU A 1 1984 ? 52.559  72.527  97.458  1.00 30.42  ? 1984 GLU A CB    1 
ATOM   4240  C  CG    . GLU A 1 1984 ? 53.945  72.348  98.067  1.00 32.43  ? 1984 GLU A CG    1 
ATOM   4241  C  CD    . GLU A 1 1984 ? 54.732  71.211  97.438  1.00 40.82  ? 1984 GLU A CD    1 
ATOM   4242  O  OE1   . GLU A 1 1984 ? 54.181  70.548  96.536  1.00 43.86  ? 1984 GLU A OE1   1 
ATOM   4243  O  OE2   . GLU A 1 1984 ? 55.893  70.991  97.842  1.00 33.95  ? 1984 GLU A OE2   1 
ATOM   4244  N  N     . HIS A 1 1985 ? 51.675  73.810  100.454 1.00 35.39  ? 1985 HIS A N     1 
ATOM   4245  C  CA    . HIS A 1 1985 ? 50.979  73.667  101.761 1.00 36.92  ? 1985 HIS A CA    1 
ATOM   4246  C  C     . HIS A 1 1985 ? 49.726  74.543  101.749 1.00 41.65  ? 1985 HIS A C     1 
ATOM   4247  O  O     . HIS A 1 1985 ? 48.640  74.063  102.140 1.00 42.66  ? 1985 HIS A O     1 
ATOM   4248  C  CB    . HIS A 1 1985 ? 51.874  74.107  102.924 1.00 28.54  ? 1985 HIS A CB    1 
ATOM   4249  C  CG    . HIS A 1 1985 ? 52.888  73.104  103.354 1.00 28.36  ? 1985 HIS A CG    1 
ATOM   4250  N  ND1   . HIS A 1 1985 ? 52.608  72.123  104.279 1.00 28.97  ? 1985 HIS A ND1   1 
ATOM   4251  C  CD2   . HIS A 1 1985 ? 54.165  72.929  103.000 1.00 31.59  ? 1985 HIS A CD2   1 
ATOM   4252  C  CE1   . HIS A 1 1985 ? 53.689  71.383  104.469 1.00 28.08  ? 1985 HIS A CE1   1 
ATOM   4253  N  NE2   . HIS A 1 1985 ? 54.647  71.857  103.703 1.00 28.60  ? 1985 HIS A NE2   1 
ATOM   4254  N  N     . SER A 1 1986 ? 49.873  75.795  101.304 1.00 43.52  ? 1986 SER A N     1 
ATOM   4255  C  CA    . SER A 1 1986 ? 48.726  76.742  101.287 1.00 38.55  ? 1986 SER A CA    1 
ATOM   4256  C  C     . SER A 1 1986 ? 47.626  76.225  100.348 1.00 52.95  ? 1986 SER A C     1 
ATOM   4257  O  O     . SER A 1 1986 ? 46.435  76.449  100.657 1.00 55.52  ? 1986 SER A O     1 
ATOM   4258  C  CB    . SER A 1 1986 ? 49.170  78.131  100.900 1.00 28.70  ? 1986 SER A CB    1 
ATOM   4259  O  OG    . SER A 1 1986 ? 49.701  78.152  99.582  1.00 34.77  ? 1986 SER A OG    1 
ATOM   4260  N  N     . ASN A 1 1987 ? 48.009  75.561  99.253  1.00 55.82  ? 1987 ASN A N     1 
ATOM   4261  C  CA    . ASN A 1 1987 ? 47.005  75.083  98.262  1.00 63.54  ? 1987 ASN A CA    1 
ATOM   4262  C  C     . ASN A 1 1987 ? 45.886  74.333  98.993  1.00 75.69  ? 1987 ASN A C     1 
ATOM   4263  O  O     . ASN A 1 1987 ? 46.186  73.325  99.670  1.00 75.57  ? 1987 ASN A O     1 
ATOM   4264  C  CB    . ASN A 1 1987 ? 47.647  74.229  97.175  1.00 62.93  ? 1987 ASN A CB    1 
ATOM   4265  C  CG    . ASN A 1 1987 ? 48.488  75.053  96.231  1.00 62.50  ? 1987 ASN A CG    1 
ATOM   4266  O  OD1   . ASN A 1 1987 ? 49.691  74.809  96.092  1.00 58.83  ? 1987 ASN A OD1   1 
ATOM   4267  N  ND2   . ASN A 1 1987 ? 47.877  76.028  95.573  1.00 58.37  ? 1987 ASN A ND2   1 
ATOM   4268  N  N     . PRO A 1 1988 ? 44.614  74.775  98.880  1.00 80.52  ? 1988 PRO A N     1 
ATOM   4269  C  CA    . PRO A 1 1988 ? 43.504  74.076  99.512  1.00 80.43  ? 1988 PRO A CA    1 
ATOM   4270  C  C     . PRO A 1 1988 ? 43.298  72.718  98.862  1.00 84.89  ? 1988 PRO A C     1 
ATOM   4271  O  O     . PRO A 1 1988 ? 43.023  71.737  99.580  1.00 85.54  ? 1988 PRO A O     1 
ATOM   4272  C  CB    . PRO A 1 1988 ? 42.317  75.022  99.282  1.00 78.31  ? 1988 PRO A CB    1 
ATOM   4273  C  CG    . PRO A 1 1988 ? 42.700  75.791  98.039  1.00 83.42  ? 1988 PRO A CG    1 
ATOM   4274  C  CD    . PRO A 1 1988 ? 44.207  75.955  98.136  1.00 78.45  ? 1988 PRO A CD    1 
ATOM   4275  N  N     . ASN A 1 1989 ? 43.418  72.660  97.532  1.00 82.08  ? 1989 ASN A N     1 
ATOM   4276  C  CA    . ASN A 1 1989 ? 43.282  71.369  96.803  1.00 82.33  ? 1989 ASN A CA    1 
ATOM   4277  C  C     . ASN A 1 1989 ? 44.054  70.289  97.565  1.00 86.01  ? 1989 ASN A C     1 
ATOM   4278  O  O     . ASN A 1 1989 ? 43.571  69.137  97.613  1.00 84.05  ? 1989 ASN A O     1 
ATOM   4279  C  CB    . ASN A 1 1989 ? 43.761  71.501  95.363  1.00 79.37  ? 1989 ASN A CB    1 
ATOM   4280  C  CG    . ASN A 1 1989 ? 45.121  72.152  95.278  1.00 79.45  ? 1989 ASN A CG    1 
ATOM   4281  O  OD1   . ASN A 1 1989 ? 46.101  71.621  95.810  1.00 76.58  ? 1989 ASN A OD1   1 
ATOM   4282  N  ND2   . ASN A 1 1989 ? 45.202  73.298  94.617  1.00 79.47  ? 1989 ASN A ND2   1 
ATOM   4283  N  N     . TYR A 1 1990 ? 45.204  70.651  98.139  1.00 85.72  ? 1990 TYR A N     1 
ATOM   4284  C  CA    . TYR A 1 1990 ? 46.015  69.693  98.878  1.00 85.96  ? 1990 TYR A CA    1 
ATOM   4285  C  C     . TYR A 1 1990 ? 45.299  69.262  100.151 1.00 84.77  ? 1990 TYR A C     1 
ATOM   4286  O  O     . TYR A 1 1990 ? 44.752  70.088  100.888 1.00 85.36  ? 1990 TYR A O     1 
ATOM   4287  C  CB    . TYR A 1 1990 ? 47.376  70.305  99.211  1.00 79.81  ? 1990 TYR A CB    1 
ATOM   4288  C  CG    . TYR A 1 1990 ? 48.042  69.726  100.440 1.00 77.89  ? 1990 TYR A CG    1 
ATOM   4289  C  CD1   . TYR A 1 1990 ? 48.697  68.503  100.390 1.00 78.17  ? 1990 TYR A CD1   1 
ATOM   4290  C  CD2   . TYR A 1 1990 ? 48.025  70.411  101.650 1.00 72.70  ? 1990 TYR A CD2   1 
ATOM   4291  C  CE1   . TYR A 1 1990 ? 49.310  67.974  101.510 1.00 79.49  ? 1990 TYR A CE1   1 
ATOM   4292  C  CE2   . TYR A 1 1990 ? 48.634  69.889  102.775 1.00 73.83  ? 1990 TYR A CE2   1 
ATOM   4293  C  CZ    . TYR A 1 1990 ? 49.275  68.671  102.700 1.00 79.02  ? 1990 TYR A CZ    1 
ATOM   4294  O  OH    . TYR A 1 1990 ? 49.883  68.149  103.818 1.00 71.31  ? 1990 TYR A OH    1 
ATOM   4295  N  N     . ASP A 1 1991 ? 45.304  67.958  100.408 1.00 86.22  ? 1991 ASP A N     1 
ATOM   4296  C  CA    . ASP A 1 1991 ? 44.642  67.378  101.567 1.00 87.91  ? 1991 ASP A CA    1 
ATOM   4297  C  C     . ASP A 1 1991 ? 45.683  66.840  102.537 1.00 89.47  ? 1991 ASP A C     1 
ATOM   4298  O  O     . ASP A 1 1991 ? 46.708  66.291  102.121 1.00 90.71  ? 1991 ASP A O     1 
ATOM   4299  C  CB    . ASP A 1 1991 ? 43.678  66.259  101.154 1.00 86.97  ? 1991 ASP A CB    1 
ATOM   4300  C  CG    . ASP A 1 1991 ? 44.376  65.128  100.425 1.00 90.21  ? 1991 ASP A CG    1 
ATOM   4301  O  OD1   . ASP A 1 1991 ? 45.055  65.402  99.413  1.00 83.72  ? 1991 ASP A OD1   1 
ATOM   4302  O  OD2   . ASP A 1 1991 ? 44.246  63.966  100.863 1.00 89.61  ? 1991 ASP A OD2   1 
ATOM   4303  N  N     . LYS A 1 1992 ? 45.415  67.007  103.835 1.00 88.21  ? 1992 LYS A N     1 
ATOM   4304  C  CA    . LYS A 1 1992 ? 46.351  66.555  104.858 1.00 89.89  ? 1992 LYS A CA    1 
ATOM   4305  C  C     . LYS A 1 1992 ? 46.551  65.046  104.836 1.00 91.22  ? 1992 LYS A C     1 
ATOM   4306  O  O     . LYS A 1 1992 ? 47.607  64.566  105.262 1.00 84.49  ? 1992 LYS A O     1 
ATOM   4307  C  CB    . LYS A 1 1992 ? 45.869  67.000  106.239 1.00 89.18  ? 1992 LYS A CB    1 
ATOM   4308  C  CG    . LYS A 1 1992 ? 45.741  68.507  106.393 1.00 86.56  ? 1992 LYS A CG    1 
ATOM   4309  C  CD    . LYS A 1 1992 ? 45.109  68.879  107.724 1.00 85.40  ? 1992 LYS A CD    1 
ATOM   4310  C  CE    . LYS A 1 1992 ? 43.700  68.320  107.843 1.00 84.87  ? 1992 LYS A CE    1 
ATOM   4311  N  NZ    . LYS A 1 1992 ? 43.056  68.707  109.128 1.00 101.52 ? 1992 LYS A NZ    1 
ATOM   4312  N  N     . THR A 1 1993 ? 45.567  64.289  104.353 1.00 92.97  ? 1993 THR A N     1 
ATOM   4313  C  CA    . THR A 1 1993 ? 45.679  62.836  104.235 1.00 92.35  ? 1993 THR A CA    1 
ATOM   4314  C  C     . THR A 1 1993 ? 46.252  62.410  102.891 1.00 90.97  ? 1993 THR A C     1 
ATOM   4315  O  O     . THR A 1 1993 ? 45.647  61.606  102.176 1.00 92.25  ? 1993 THR A O     1 
ATOM   4316  C  CB    . THR A 1 1993 ? 44.315  62.193  104.467 1.00 91.85  ? 1993 THR A CB    1 
ATOM   4317  O  OG1   . THR A 1 1993 ? 43.388  62.663  103.480 1.00 90.22  ? 1993 THR A OG1   1 
ATOM   4318  C  CG2   . THR A 1 1993 ? 43.792  62.542  105.853 1.00 87.96  ? 1993 THR A CG2   1 
ATOM   4319  N  N     . SER A 1 1994 ? 47.418  62.934  102.522 1.00 88.95  ? 1994 SER A N     1 
ATOM   4320  C  CA    . SER A 1 1994 ? 48.063  62.628  101.253 1.00 89.83  ? 1994 SER A CA    1 
ATOM   4321  C  C     . SER A 1 1994 ? 49.568  62.522  101.470 1.00 83.15  ? 1994 SER A C     1 
ATOM   4322  O  O     . SER A 1 1994 ? 50.051  62.430  102.602 1.00 78.22  ? 1994 SER A O     1 
ATOM   4323  C  CB    . SER A 1 1994 ? 47.735  63.689  100.194 1.00 84.39  ? 1994 SER A CB    1 
ATOM   4324  O  OG    . SER A 1 1994 ? 48.361  64.923  100.500 1.00 77.37  ? 1994 SER A OG    1 
ATOM   4325  N  N     . ALA A 1 1995 ? 50.309  62.529  100.368 1.00 81.02  ? 1995 ALA A N     1 
ATOM   4326  C  CA    . ALA A 1 1995 ? 51.760  62.480  100.443 1.00 74.95  ? 1995 ALA A CA    1 
ATOM   4327  C  C     . ALA A 1 1995 ? 52.287  63.745  101.116 1.00 74.84  ? 1995 ALA A C     1 
ATOM   4328  O  O     . ALA A 1 1995 ? 51.839  64.851  100.781 1.00 71.82  ? 1995 ALA A O     1 
ATOM   4329  C  CB    . ALA A 1 1995 ? 52.364  62.334  99.046  1.00 67.28  ? 1995 ALA A CB    1 
ATOM   4330  N  N     . PRO A 1 1996 ? 53.213  63.629  102.067 1.00 70.62  ? 1996 PRO A N     1 
ATOM   4331  C  CA    . PRO A 1 1996 ? 53.727  64.825  102.745 1.00 60.28  ? 1996 PRO A CA    1 
ATOM   4332  C  C     . PRO A 1 1996 ? 54.409  65.772  101.769 1.00 50.44  ? 1996 PRO A C     1 
ATOM   4333  O  O     . PRO A 1 1996 ? 55.049  65.348  100.805 1.00 46.56  ? 1996 PRO A O     1 
ATOM   4334  C  CB    . PRO A 1 1996 ? 54.722  64.254  103.763 1.00 53.81  ? 1996 PRO A CB    1 
ATOM   4335  C  CG    . PRO A 1 1996 ? 54.289  62.836  103.964 1.00 56.92  ? 1996 PRO A CG    1 
ATOM   4336  C  CD    . PRO A 1 1996 ? 53.776  62.390  102.628 1.00 61.95  ? 1996 PRO A CD    1 
ATOM   4337  N  N     . ILE A 1 1997 ? 54.255  67.072  102.029 1.00 46.09  ? 1997 ILE A N     1 
ATOM   4338  C  CA    . ILE A 1 1997 ? 54.906  68.082  101.205 1.00 34.03  ? 1997 ILE A CA    1 
ATOM   4339  C  C     . ILE A 1 1997 ? 56.414  67.949  101.336 1.00 29.34  ? 1997 ILE A C     1 
ATOM   4340  O  O     . ILE A 1 1997 ? 56.949  67.803  102.442 1.00 29.76  ? 1997 ILE A O     1 
ATOM   4341  C  CB    . ILE A 1 1997 ? 54.429  69.485  101.606 1.00 32.20  ? 1997 ILE A CB    1 
ATOM   4342  C  CG1   . ILE A 1 1997 ? 52.910  69.603  101.450 1.00 42.25  ? 1997 ILE A CG1   1 
ATOM   4343  C  CG2   . ILE A 1 1997 ? 55.162  70.546  100.807 1.00 29.00  ? 1997 ILE A CG2   1 
ATOM   4344  C  CD1   . ILE A 1 1997 ? 52.409  69.267  100.064 1.00 48.44  ? 1997 ILE A CD1   1 
ATOM   4345  N  N     . THR A 1 1998 ? 57.109  68.002  100.203 1.00 23.84  ? 1998 THR A N     1 
ATOM   4346  C  CA    . THR A 1 1998 ? 58.539  67.749  100.166 1.00 20.86  ? 1998 THR A CA    1 
ATOM   4347  C  C     . THR A 1 1998 ? 59.177  68.562  99.048  1.00 21.92  ? 1998 THR A C     1 
ATOM   4348  O  O     . THR A 1 1998 ? 58.624  68.662  97.950  1.00 32.05  ? 1998 THR A O     1 
ATOM   4349  C  CB    . THR A 1 1998 ? 58.813  66.249  99.969  1.00 25.52  ? 1998 THR A CB    1 
ATOM   4350  O  OG1   . THR A 1 1998 ? 58.545  65.550  101.191 1.00 30.88  ? 1998 THR A OG1   1 
ATOM   4351  C  CG2   . THR A 1 1998 ? 60.247  66.007  99.569  1.00 22.74  ? 1998 THR A CG2   1 
ATOM   4352  N  N     . CYS A 1 1999 ? 60.340  69.143  99.337  1.00 18.57  ? 1999 CYS A N     1 
ATOM   4353  C  CA    . CYS A 1 1999 ? 61.124  69.871  98.351  1.00 20.90  ? 1999 CYS A CA    1 
ATOM   4354  C  C     . CYS A 1 1999 ? 62.525  69.277  98.273  1.00 21.13  ? 1999 CYS A C     1 
ATOM   4355  O  O     . CYS A 1 1999 ? 62.968  68.561  99.173  1.00 16.62  ? 1999 CYS A O     1 
ATOM   4356  C  CB    . CYS A 1 1999 ? 61.206  71.366  98.689  1.00 17.79  ? 1999 CYS A CB    1 
ATOM   4357  S  SG    . CYS A 1 1999 ? 62.484  71.797  99.892  1.00 23.86  ? 1999 CYS A SG    1 
ATOM   4358  N  N     . GLU A 1 2000 ? 63.229  69.577  97.187  1.00 24.26  ? 2000 GLU A N     1 
ATOM   4359  C  CA    . GLU A 1 2000 ? 64.562  69.028  96.973  1.00 22.40  ? 2000 GLU A CA    1 
ATOM   4360  C  C     . GLU A 1 2000 ? 65.606  69.967  97.566  1.00 18.17  ? 2000 GLU A C     1 
ATOM   4361  O  O     . GLU A 1 2000 ? 65.772  71.099  97.099  1.00 15.28  ? 2000 GLU A O     1 
ATOM   4362  C  CB    . GLU A 1 2000 ? 64.830  68.796  95.487  1.00 25.39  ? 2000 GLU A CB    1 
ATOM   4363  C  CG    . GLU A 1 2000 ? 66.178  68.148  95.213  1.00 29.50  ? 2000 GLU A CG    1 
ATOM   4364  C  CD    . GLU A 1 2000 ? 66.412  67.876  93.741  1.00 43.58  ? 2000 GLU A CD    1 
ATOM   4365  O  OE1   . GLU A 1 2000 ? 65.530  68.212  92.924  1.00 51.58  ? 2000 GLU A OE1   1 
ATOM   4366  O  OE2   . GLU A 1 2000 ? 67.478  67.321  93.402  1.00 41.08  ? 2000 GLU A OE2   1 
ATOM   4367  N  N     . LEU A 1 2001 ? 66.305  69.492  98.595  1.00 15.94  ? 2001 LEU A N     1 
ATOM   4368  C  CA    . LEU A 1 2001 ? 67.393  70.226  99.228  1.00 15.39  ? 2001 LEU A CA    1 
ATOM   4369  C  C     . LEU A 1 2001 ? 68.614  69.322  99.276  1.00 16.33  ? 2001 LEU A C     1 
ATOM   4370  O  O     . LEU A 1 2001 ? 68.523  68.181  99.742  1.00 21.44  ? 2001 LEU A O     1 
ATOM   4371  C  CB    . LEU A 1 2001 ? 67.007  70.684  100.637 1.00 13.12  ? 2001 LEU A CB    1 
ATOM   4372  C  CG    . LEU A 1 2001 ? 66.070  71.886  100.754 1.00 12.91  ? 2001 LEU A CG    1 
ATOM   4373  C  CD1   . LEU A 1 2001 ? 65.825  72.228  102.215 1.00 7.51   ? 2001 LEU A CD1   1 
ATOM   4374  C  CD2   . LEU A 1 2001 ? 66.646  73.078  100.009 1.00 8.32   ? 2001 LEU A CD2   1 
ATOM   4375  N  N     . LEU A 1 2002 ? 69.750  69.832  98.794  1.00 17.74  ? 2002 LEU A N     1 
ATOM   4376  C  CA    . LEU A 1 2002 ? 71.006  69.079  98.761  1.00 19.41  ? 2002 LEU A CA    1 
ATOM   4377  C  C     . LEU A 1 2002 ? 70.825  67.724  98.082  1.00 23.78  ? 2002 LEU A C     1 
ATOM   4378  O  O     . LEU A 1 2002 ? 71.328  66.701  98.552  1.00 27.52  ? 2002 LEU A O     1 
ATOM   4379  C  CB    . LEU A 1 2002 ? 71.589  68.913  100.167 1.00 15.89  ? 2002 LEU A CB    1 
ATOM   4380  C  CG    . LEU A 1 2002 ? 71.886  70.207  100.926 1.00 13.18  ? 2002 LEU A CG    1 
ATOM   4381  C  CD1   . LEU A 1 2002 ? 72.464  69.908  102.299 1.00 11.54  ? 2002 LEU A CD1   1 
ATOM   4382  C  CD2   . LEU A 1 2002 ? 72.830  71.090  100.126 1.00 13.44  ? 2002 LEU A CD2   1 
ATOM   4383  N  N     . ASN A 1 2003 ? 70.085  67.720  96.970  1.00 26.30  ? 2003 ASN A N     1 
ATOM   4384  C  CA    . ASN A 1 2003 ? 69.808  66.520  96.183  1.00 26.31  ? 2003 ASN A CA    1 
ATOM   4385  C  C     . ASN A 1 2003 ? 69.073  65.454  96.991  1.00 26.97  ? 2003 ASN A C     1 
ATOM   4386  O  O     . ASN A 1 2003 ? 69.209  64.259  96.721  1.00 37.46  ? 2003 ASN A O     1 
ATOM   4387  C  CB    . ASN A 1 2003 ? 71.091  65.936  95.582  1.00 26.66  ? 2003 ASN A CB    1 
ATOM   4388  C  CG    . ASN A 1 2003 ? 71.720  66.852  94.552  1.00 38.21  ? 2003 ASN A CG    1 
ATOM   4389  O  OD1   . ASN A 1 2003 ? 71.113  67.162  93.527  1.00 36.17  ? 2003 ASN A OD1   1 
ATOM   4390  N  ND2   . ASN A 1 2003 ? 72.944  67.291  94.820  1.00 43.49  ? 2003 ASN A ND2   1 
ATOM   4391  N  N     . LYS A 1 2004 ? 68.288  65.869  97.984  1.00 24.63  ? 2004 LYS A N     1 
ATOM   4392  C  CA    . LYS A 1 2004 ? 67.505  64.943  98.789  1.00 21.30  ? 2004 LYS A CA    1 
ATOM   4393  C  C     . LYS A 1 2004 ? 66.084  65.465  98.927  1.00 22.29  ? 2004 LYS A C     1 
ATOM   4394  O  O     . LYS A 1 2004 ? 65.865  66.675  99.025  1.00 22.06  ? 2004 LYS A O     1 
ATOM   4395  C  CB    . LYS A 1 2004 ? 68.122  64.740  100.179 1.00 21.78  ? 2004 LYS A CB    1 
ATOM   4396  C  CG    . LYS A 1 2004 ? 69.517  64.142  100.162 1.00 27.66  ? 2004 LYS A CG    1 
ATOM   4397  C  CD    . LYS A 1 2004 ? 69.485  62.698  99.691  1.00 47.38  ? 2004 LYS A CD    1 
ATOM   4398  C  CE    . LYS A 1 2004 ? 70.878  62.092  99.664  1.00 51.21  ? 2004 LYS A CE    1 
ATOM   4399  N  NZ    . LYS A 1 2004 ? 71.437  61.930  101.034 1.00 56.00  ? 2004 LYS A NZ    1 
ATOM   4400  N  N     . GLN A 1 2005 ? 65.123  64.546  98.944  1.00 23.69  ? 2005 GLN A N     1 
ATOM   4401  C  CA    . GLN A 1 2005 ? 63.719  64.904  99.115  1.00 19.60  ? 2005 GLN A CA    1 
ATOM   4402  C  C     . GLN A 1 2005 ? 63.454  65.117  100.601 1.00 21.59  ? 2005 GLN A C     1 
ATOM   4403  O  O     . GLN A 1 2005 ? 63.401  64.155  101.374 1.00 24.97  ? 2005 GLN A O     1 
ATOM   4404  C  CB    . GLN A 1 2005 ? 62.819  63.817  98.537  1.00 23.75  ? 2005 GLN A CB    1 
ATOM   4405  C  CG    . GLN A 1 2005 ? 62.780  63.783  97.015  1.00 30.22  ? 2005 GLN A CG    1 
ATOM   4406  C  CD    . GLN A 1 2005 ? 62.611  65.158  96.398  1.00 28.19  ? 2005 GLN A CD    1 
ATOM   4407  O  OE1   . GLN A 1 2005 ? 61.636  65.859  96.670  1.00 27.68  ? 2005 GLN A OE1   1 
ATOM   4408  N  NE2   . GLN A 1 2005 ? 63.563  65.551  95.561  1.00 29.57  ? 2005 GLN A NE2   1 
ATOM   4409  N  N     . VAL A 1 2006 ? 63.284  66.375  101.004 1.00 17.81  ? 2006 VAL A N     1 
ATOM   4410  C  CA    . VAL A 1 2006 ? 63.174  66.764  102.403 1.00 17.50  ? 2006 VAL A CA    1 
ATOM   4411  C  C     . VAL A 1 2006 ? 61.760  67.267  102.657 1.00 15.53  ? 2006 VAL A C     1 
ATOM   4412  O  O     . VAL A 1 2006 ? 61.253  68.119  101.916 1.00 17.51  ? 2006 VAL A O     1 
ATOM   4413  C  CB    . VAL A 1 2006 ? 64.213  67.841  102.763 1.00 14.96  ? 2006 VAL A CB    1 
ATOM   4414  C  CG1   . VAL A 1 2006 ? 64.044  68.287  104.202 1.00 11.57  ? 2006 VAL A CG1   1 
ATOM   4415  C  CG2   . VAL A 1 2006 ? 65.622  67.321  102.522 1.00 12.81  ? 2006 VAL A CG2   1 
ATOM   4416  N  N     . LYS A 1 2007 ? 61.126  66.733  103.699 1.00 13.79  ? 2007 LYS A N     1 
ATOM   4417  C  CA    . LYS A 1 2007 ? 59.800  67.190  104.090 1.00 17.00  ? 2007 LYS A CA    1 
ATOM   4418  C  C     . LYS A 1 2007 ? 59.861  68.623  104.606 1.00 17.55  ? 2007 LYS A C     1 
ATOM   4419  O  O     . LYS A 1 2007 ? 60.780  68.999  105.339 1.00 12.93  ? 2007 LYS A O     1 
ATOM   4420  C  CB    . LYS A 1 2007 ? 59.221  66.266  105.162 1.00 21.36  ? 2007 LYS A CB    1 
ATOM   4421  C  CG    . LYS A 1 2007 ? 57.820  66.630  105.617 1.00 27.74  ? 2007 LYS A CG    1 
ATOM   4422  C  CD    . LYS A 1 2007 ? 57.263  65.586  106.572 1.00 37.87  ? 2007 LYS A CD    1 
ATOM   4423  C  CE    . LYS A 1 2007 ? 57.956  65.651  107.924 1.00 43.25  ? 2007 LYS A CE    1 
ATOM   4424  N  NZ    . LYS A 1 2007 ? 57.628  66.902  108.661 1.00 40.76  ? 2007 LYS A NZ    1 
ATOM   4425  N  N     . VAL A 1 2008 ? 58.875  69.425  104.218 1.00 16.03  ? 2008 VAL A N     1 
ATOM   4426  C  CA    . VAL A 1 2008 ? 58.797  70.829  104.603 1.00 11.89  ? 2008 VAL A CA    1 
ATOM   4427  C  C     . VAL A 1 2008 ? 57.579  71.012  105.495 1.00 11.74  ? 2008 VAL A C     1 
ATOM   4428  O  O     . VAL A 1 2008 ? 56.439  70.846  105.044 1.00 19.89  ? 2008 VAL A O     1 
ATOM   4429  C  CB    . VAL A 1 2008 ? 58.725  71.750  103.375 1.00 13.62  ? 2008 VAL A CB    1 
ATOM   4430  C  CG1   . VAL A 1 2008 ? 58.605  73.203  103.808 1.00 14.42  ? 2008 VAL A CG1   1 
ATOM   4431  C  CG2   . VAL A 1 2008 ? 59.945  71.549  102.493 1.00 11.46  ? 2008 VAL A CG2   1 
ATOM   4432  N  N     . SER A 1 2009 ? 57.817  71.346  106.758 1.00 12.90  ? 2009 SER A N     1 
ATOM   4433  C  CA    . SER A 1 2009 ? 56.720  71.668  107.659 1.00 11.87  ? 2009 SER A CA    1 
ATOM   4434  C  C     . SER A 1 2009 ? 56.179  73.062  107.344 1.00 12.49  ? 2009 SER A C     1 
ATOM   4435  O  O     . SER A 1 2009 ? 56.953  73.973  107.042 1.00 13.29  ? 2009 SER A O     1 
ATOM   4436  C  CB    . SER A 1 2009 ? 57.182  71.600  109.112 1.00 10.20  ? 2009 SER A CB    1 
ATOM   4437  O  OG    . SER A 1 2009 ? 56.145  71.975  110.001 1.00 14.74  ? 2009 SER A OG    1 
ATOM   4438  N  N     . PRO A 1 2010 ? 54.858  73.256  107.399 1.00 15.77  ? 2010 PRO A N     1 
ATOM   4439  C  CA    . PRO A 1 2010 ? 54.290  74.564  107.036 1.00 14.85  ? 2010 PRO A CA    1 
ATOM   4440  C  C     . PRO A 1 2010 ? 54.600  75.679  108.023 1.00 9.88   ? 2010 PRO A C     1 
ATOM   4441  O  O     . PRO A 1 2010 ? 54.376  76.849  107.687 1.00 13.02  ? 2010 PRO A O     1 
ATOM   4442  C  CB    . PRO A 1 2010 ? 52.785  74.279  106.977 1.00 11.33  ? 2010 PRO A CB    1 
ATOM   4443  C  CG    . PRO A 1 2010 ? 52.596  73.176  107.961 1.00 11.15  ? 2010 PRO A CG    1 
ATOM   4444  C  CD    . PRO A 1 2010 ? 53.813  72.299  107.803 1.00 13.39  ? 2010 PRO A CD    1 
ATOM   4445  N  N     . ASP A 1 2011 ? 55.104  75.369  109.214 1.00 8.95   ? 2011 ASP A N     1 
ATOM   4446  C  CA    . ASP A 1 2011 ? 55.328  76.375  110.244 1.00 8.19   ? 2011 ASP A CA    1 
ATOM   4447  C  C     . ASP A 1 2011 ? 56.686  77.056  110.145 1.00 6.20   ? 2011 ASP A C     1 
ATOM   4448  O  O     . ASP A 1 2011 ? 56.967  77.955  110.943 1.00 7.75   ? 2011 ASP A O     1 
ATOM   4449  C  CB    . ASP A 1 2011 ? 55.176  75.750  111.635 1.00 7.75   ? 2011 ASP A CB    1 
ATOM   4450  C  CG    . ASP A 1 2011 ? 53.739  75.737  112.114 1.00 14.05  ? 2011 ASP A CG    1 
ATOM   4451  O  OD1   . ASP A 1 2011 ? 52.852  76.173  111.351 1.00 16.61  ? 2011 ASP A OD1   1 
ATOM   4452  O  OD2   . ASP A 1 2011 ? 53.496  75.294  113.256 1.00 13.75  ? 2011 ASP A OD2   1 
ATOM   4453  N  N     . MET A 1 2012 ? 57.532  76.667  109.198 1.00 5.05   ? 2012 MET A N     1 
ATOM   4454  C  CA    . MET A 1 2012 ? 58.871  77.227  109.116 1.00 5.04   ? 2012 MET A CA    1 
ATOM   4455  C  C     . MET A 1 2012 ? 58.877  78.521  108.310 1.00 5.74   ? 2012 MET A C     1 
ATOM   4456  O  O     . MET A 1 2012 ? 57.986  78.777  107.496 1.00 7.80   ? 2012 MET A O     1 
ATOM   4457  C  CB    . MET A 1 2012 ? 59.848  76.218  108.507 1.00 4.68   ? 2012 MET A CB    1 
ATOM   4458  C  CG    . MET A 1 2012 ? 59.541  75.762  107.086 1.00 7.22   ? 2012 MET A CG    1 
ATOM   4459  S  SD    . MET A 1 2012 ? 60.032  76.943  105.818 1.00 32.28  ? 2012 MET A SD    1 
ATOM   4460  C  CE    . MET A 1 2012 ? 61.806  76.793  105.926 1.00 6.85   ? 2012 MET A CE    1 
ATOM   4461  N  N     . ALA A 1 2013 ? 59.903  79.337  108.548 1.00 3.04   ? 2013 ALA A N     1 
ATOM   4462  C  CA    . ALA A 1 2013 ? 60.076  80.594  107.836 1.00 2.45   ? 2013 ALA A CA    1 
ATOM   4463  C  C     . ALA A 1 2013 ? 61.558  80.938  107.795 1.00 2.59   ? 2013 ALA A C     1 
ATOM   4464  O  O     . ALA A 1 2013 ? 62.356  80.426  108.584 1.00 2.30   ? 2013 ALA A O     1 
ATOM   4465  C  CB    . ALA A 1 2013 ? 59.278  81.727  108.488 1.00 1.69   ? 2013 ALA A CB    1 
ATOM   4466  N  N     . ILE A 1 2014 ? 61.920  81.813  106.860 1.00 2.10   ? 2014 ILE A N     1 
ATOM   4467  C  CA    . ILE A 1 2014 ? 63.306  82.218  106.652 1.00 2.30   ? 2014 ILE A CA    1 
ATOM   4468  C  C     . ILE A 1 2014 ? 63.356  83.742  106.711 1.00 2.48   ? 2014 ILE A C     1 
ATOM   4469  O  O     . ILE A 1 2014 ? 62.669  84.419  105.937 1.00 2.44   ? 2014 ILE A O     1 
ATOM   4470  C  CB    . ILE A 1 2014 ? 63.854  81.695  105.315 1.00 3.06   ? 2014 ILE A CB    1 
ATOM   4471  C  CG1   . ILE A 1 2014 ? 63.548  80.209  105.151 1.00 6.99   ? 2014 ILE A CG1   1 
ATOM   4472  C  CG2   . ILE A 1 2014 ? 65.355  81.808  105.276 1.00 3.58   ? 2014 ILE A CG2   1 
ATOM   4473  C  CD1   . ILE A 1 2014 ? 64.018  79.640  103.829 1.00 6.60   ? 2014 ILE A CD1   1 
ATOM   4474  N  N     . PHE A 1 2015 ? 64.166  84.281  107.624 1.00 1.57   ? 2015 PHE A N     1 
ATOM   4475  C  CA    . PHE A 1 2015 ? 64.288  85.721  107.819 1.00 1.29   ? 2015 PHE A CA    1 
ATOM   4476  C  C     . PHE A 1 2015 ? 65.747  86.147  107.752 1.00 1.85   ? 2015 PHE A C     1 
ATOM   4477  O  O     . PHE A 1 2015 ? 66.633  85.436  108.233 1.00 2.30   ? 2015 PHE A O     1 
ATOM   4478  C  CB    . PHE A 1 2015 ? 63.693  86.164  109.162 1.00 1.40   ? 2015 PHE A CB    1 
ATOM   4479  C  CG    . PHE A 1 2015 ? 62.195  86.142  109.201 1.00 1.37   ? 2015 PHE A CG    1 
ATOM   4480  C  CD1   . PHE A 1 2015 ? 61.511  84.979  109.509 1.00 1.22   ? 2015 PHE A CD1   1 
ATOM   4481  C  CD2   . PHE A 1 2015 ? 61.470  87.291  108.939 1.00 1.06   ? 2015 PHE A CD2   1 
ATOM   4482  C  CE1   . PHE A 1 2015 ? 60.132  84.963  109.546 1.00 1.08   ? 2015 PHE A CE1   1 
ATOM   4483  C  CE2   . PHE A 1 2015 ? 60.090  87.280  108.976 1.00 1.36   ? 2015 PHE A CE2   1 
ATOM   4484  C  CZ    . PHE A 1 2015 ? 59.420  86.114  109.282 1.00 1.53   ? 2015 PHE A CZ    1 
ATOM   4485  N  N     . ILE A 1 2016 ? 65.991  87.327  107.173 1.00 1.62   ? 2016 ILE A N     1 
ATOM   4486  C  CA    . ILE A 1 2016 ? 67.386  87.853  107.072 1.00 1.99   ? 2016 ILE A CA    1 
ATOM   4487  C  C     . ILE A 1 2016 ? 67.413  89.320  107.529 1.00 3.10   ? 2016 ILE A C     1 
ATOM   4488  O  O     . ILE A 1 2016 ? 66.732  90.152  106.889 1.00 3.70   ? 2016 ILE A O     1 
ATOM   4489  C  CB    . ILE A 1 2016 ? 67.934  87.697  105.641 1.00 3.03   ? 2016 ILE A CB    1 
ATOM   4490  C  CG1   . ILE A 1 2016 ? 66.909  88.129  104.593 1.00 3.96   ? 2016 ILE A CG1   1 
ATOM   4491  C  CG2   . ILE A 1 2016 ? 68.422  86.269  105.399 1.00 2.13   ? 2016 ILE A CG2   1 
ATOM   4492  C  CD1   . ILE A 1 2016 ? 67.433  88.107  103.169 1.00 2.69   ? 2016 ILE A CD1   1 
ATOM   4493  N  N     . THR A 1 2017 ? 68.163  89.619  108.593 1.00 4.32   ? 2017 THR A N     1 
ATOM   4494  C  CA    . THR A 1 2017 ? 68.311  91.019  109.051 1.00 6.90   ? 2017 THR A CA    1 
ATOM   4495  C  C     . THR A 1 2017 ? 69.693  91.485  108.654 1.00 6.65   ? 2017 THR A C     1 
ATOM   4496  O  O     . THR A 1 2017 ? 70.670  90.793  109.018 1.00 10.08  ? 2017 THR A O     1 
ATOM   4497  C  CB    . THR A 1 2017 ? 68.089  91.096  110.560 1.00 6.13   ? 2017 THR A CB    1 
ATOM   4498  O  OG1   . THR A 1 2017 ? 69.079  90.247  111.132 1.00 7.46   ? 2017 THR A OG1   1 
ATOM   4499  C  CG2   . THR A 1 2017 ? 66.707  90.619  110.969 1.00 3.88   ? 2017 THR A CG2   1 
ATOM   4500  N  N     . MET A 1 2018 ? 69.793  92.603  107.928 1.00 7.51   ? 2018 MET A N     1 
ATOM   4501  C  CA    . MET A 1 2018 ? 71.123  93.030  107.418 1.00 11.00  ? 2018 MET A CA    1 
ATOM   4502  C  C     . MET A 1 2018 ? 71.271  94.557  107.466 1.00 9.34   ? 2018 MET A C     1 
ATOM   4503  O  O     . MET A 1 2018 ? 70.257  95.249  107.704 1.00 7.96   ? 2018 MET A O     1 
ATOM   4504  C  CB    . MET A 1 2018 ? 71.319  92.564  105.970 1.00 10.93  ? 2018 MET A CB    1 
ATOM   4505  C  CG    . MET A 1 2018 ? 70.196  92.982  105.039 1.00 15.90  ? 2018 MET A CG    1 
ATOM   4506  S  SD    . MET A 1 2018 ? 70.467  92.500  103.322 1.00 34.17  ? 2018 MET A SD    1 
ATOM   4507  C  CE    . MET A 1 2018 ? 71.826  93.592  102.883 1.00 22.00  ? 2018 MET A CE    1 
ATOM   4508  N  N     . ASN A 1 2019 ? 72.492  95.052  107.246 1.00 14.66  ? 2019 ASN A N     1 
ATOM   4509  C  CA    . ASN A 1 2019 ? 72.755  96.491  107.234 1.00 16.04  ? 2019 ASN A CA    1 
ATOM   4510  C  C     . ASN A 1 2019 ? 73.362  96.861  105.888 1.00 17.10  ? 2019 ASN A C     1 
ATOM   4511  O  O     . ASN A 1 2019 ? 74.568  96.650  105.669 1.00 22.16  ? 2019 ASN A O     1 
ATOM   4512  C  CB    . ASN A 1 2019 ? 73.688  96.887  108.378 1.00 15.52  ? 2019 ASN A CB    1 
ATOM   4513  C  CG    . ASN A 1 2019 ? 73.856  98.393  108.509 1.00 19.23  ? 2019 ASN A CG    1 
ATOM   4514  O  OD1   . ASN A 1 2019 ? 73.378  99.164  107.677 1.00 16.24  ? 2019 ASN A OD1   1 
ATOM   4515  N  ND2   . ASN A 1 2019 ? 74.537  98.818  109.567 1.00 17.26  ? 2019 ASN A ND2   1 
ATOM   4516  N  N     . PRO A 1 2020 ? 72.573  97.400  104.953 1.00 20.23  ? 2020 PRO A N     1 
ATOM   4517  C  CA    . PRO A 1 2020 ? 73.132  97.793  103.649 1.00 25.44  ? 2020 PRO A CA    1 
ATOM   4518  C  C     . PRO A 1 2020 ? 74.124  98.943  103.723 1.00 28.17  ? 2020 PRO A C     1 
ATOM   4519  O  O     . PRO A 1 2020 ? 74.881  99.141  102.764 1.00 33.64  ? 2020 PRO A O     1 
ATOM   4520  C  CB    . PRO A 1 2020 ? 71.887  98.189  102.838 1.00 23.01  ? 2020 PRO A CB    1 
ATOM   4521  C  CG    . PRO A 1 2020 ? 70.723  97.594  103.590 1.00 18.83  ? 2020 PRO A CG    1 
ATOM   4522  C  CD    . PRO A 1 2020 ? 71.126  97.647  105.025 1.00 16.14  ? 2020 PRO A CD    1 
ATOM   4523  N  N     . GLY A 1 2021 ? 74.146  99.705  104.819 1.00 25.81  ? 2021 GLY A N     1 
ATOM   4524  C  CA    . GLY A 1 2021 ? 75.013  100.867 104.888 1.00 29.78  ? 2021 GLY A CA    1 
ATOM   4525  C  C     . GLY A 1 2021 ? 76.482  100.544 105.047 1.00 35.15  ? 2021 GLY A C     1 
ATOM   4526  O  O     . GLY A 1 2021 ? 77.336  101.367 104.704 1.00 47.61  ? 2021 GLY A O     1 
ATOM   4527  N  N     . TYR A 1 2022 ? 76.804  99.360  105.562 1.00 27.11  ? 2022 TYR A N     1 
ATOM   4528  C  CA    . TYR A 1 2022 ? 78.199  98.986  105.756 1.00 33.09  ? 2022 TYR A CA    1 
ATOM   4529  C  C     . TYR A 1 2022 ? 78.894  98.768  104.419 1.00 36.90  ? 2022 TYR A C     1 
ATOM   4530  O  O     . TYR A 1 2022 ? 78.390  98.049  103.551 1.00 35.05  ? 2022 TYR A O     1 
ATOM   4531  C  CB    . TYR A 1 2022 ? 78.302  97.725  106.612 1.00 31.58  ? 2022 TYR A CB    1 
ATOM   4532  C  CG    . TYR A 1 2022 ? 78.101  97.963  108.090 1.00 33.46  ? 2022 TYR A CG    1 
ATOM   4533  C  CD1   . TYR A 1 2022 ? 77.842  96.909  108.954 1.00 30.02  ? 2022 TYR A CD1   1 
ATOM   4534  C  CD2   . TYR A 1 2022 ? 78.193  99.242  108.625 1.00 34.62  ? 2022 TYR A CD2   1 
ATOM   4535  C  CE1   . TYR A 1 2022 ? 77.666  97.121  110.308 1.00 31.24  ? 2022 TYR A CE1   1 
ATOM   4536  C  CE2   . TYR A 1 2022 ? 78.019  99.465  109.977 1.00 31.44  ? 2022 TYR A CE2   1 
ATOM   4537  C  CZ    . TYR A 1 2022 ? 77.755  98.401  110.814 1.00 31.59  ? 2022 TYR A CZ    1 
ATOM   4538  O  OH    . TYR A 1 2022 ? 77.582  98.619  112.161 1.00 26.97  ? 2022 TYR A OH    1 
ATOM   4539  N  N     . ALA A 1 2023 ? 80.057  99.393  104.258 1.00 41.36  ? 2023 ALA A N     1 
ATOM   4540  C  CA    . ALA A 1 2023 ? 80.883  99.173  103.082 1.00 40.16  ? 2023 ALA A CA    1 
ATOM   4541  C  C     . ALA A 1 2023 ? 81.597  97.831  103.183 1.00 43.29  ? 2023 ALA A C     1 
ATOM   4542  O  O     . ALA A 1 2023 ? 81.977  97.383  104.269 1.00 40.87  ? 2023 ALA A O     1 
ATOM   4543  C  CB    . ALA A 1 2023 ? 81.901  100.300 102.918 1.00 39.80  ? 2023 ALA A CB    1 
ATOM   4544  N  N     . GLY A 1 2024 ? 81.780  97.189  102.031 1.00 39.52  ? 2024 GLY A N     1 
ATOM   4545  C  CA    . GLY A 1 2024 ? 82.375  95.874  101.974 1.00 38.91  ? 2024 GLY A CA    1 
ATOM   4546  C  C     . GLY A 1 2024 ? 81.394  94.729  102.088 1.00 37.60  ? 2024 GLY A C     1 
ATOM   4547  O  O     . GLY A 1 2024 ? 81.790  93.574  101.887 1.00 44.22  ? 2024 GLY A O     1 
ATOM   4548  N  N     . ARG A 1 2025 ? 80.134  95.008  102.408 1.00 35.38  ? 2025 ARG A N     1 
ATOM   4549  C  CA    . ARG A 1 2025 ? 79.114  93.974  102.423 1.00 27.59  ? 2025 ARG A CA    1 
ATOM   4550  C  C     . ARG A 1 2025 ? 78.812  93.510  101.001 1.00 22.97  ? 2025 ARG A C     1 
ATOM   4551  O  O     . ARG A 1 2025 ? 78.961  94.256  100.029 1.00 28.20  ? 2025 ARG A O     1 
ATOM   4552  C  CB    . ARG A 1 2025 ? 77.837  94.487  103.089 1.00 27.35  ? 2025 ARG A CB    1 
ATOM   4553  C  CG    . ARG A 1 2025 ? 77.900  94.568  104.606 1.00 22.31  ? 2025 ARG A CG    1 
ATOM   4554  C  CD    . ARG A 1 2025 ? 78.258  93.230  105.227 1.00 19.47  ? 2025 ARG A CD    1 
ATOM   4555  N  NE    . ARG A 1 2025 ? 79.074  93.389  106.425 1.00 24.19  ? 2025 ARG A NE    1 
ATOM   4556  C  CZ    . ARG A 1 2025 ? 78.585  93.515  107.651 1.00 25.47  ? 2025 ARG A CZ    1 
ATOM   4557  N  NH1   . ARG A 1 2025 ? 77.283  93.509  107.881 1.00 25.96  ? 2025 ARG A NH1   1 
ATOM   4558  N  NH2   . ARG A 1 2025 ? 79.425  93.652  108.673 1.00 21.51  ? 2025 ARG A NH2   1 
ATOM   4559  N  N     . SER A 1 2026 ? 78.382  92.258  100.887 1.00 20.15  ? 2026 SER A N     1 
ATOM   4560  C  CA    . SER A 1 2026 ? 78.056  91.691  99.587  1.00 18.65  ? 2026 SER A CA    1 
ATOM   4561  C  C     . SER A 1 2026 ? 76.678  92.158  99.140  1.00 19.84  ? 2026 SER A C     1 
ATOM   4562  O  O     . SER A 1 2026 ? 75.710  92.087  99.904  1.00 20.53  ? 2026 SER A O     1 
ATOM   4563  C  CB    . SER A 1 2026 ? 78.102  90.166  99.642  1.00 13.81  ? 2026 SER A CB    1 
ATOM   4564  O  OG    . SER A 1 2026 ? 79.370  89.707  100.073 1.00 19.11  ? 2026 SER A OG    1 
ATOM   4565  N  N     . ASN A 1 2027 ? 76.593  92.637  97.903  1.00 23.30  ? 2027 ASN A N     1 
ATOM   4566  C  CA    . ASN A 1 2027 ? 75.308  93.032  97.345  1.00 22.06  ? 2027 ASN A CA    1 
ATOM   4567  C  C     . ASN A 1 2027 ? 74.467  91.797  97.050  1.00 19.98  ? 2027 ASN A C     1 
ATOM   4568  O  O     . ASN A 1 2027 ? 74.963  90.813  96.493  1.00 24.39  ? 2027 ASN A O     1 
ATOM   4569  C  CB    . ASN A 1 2027 ? 75.512  93.856  96.075  1.00 23.33  ? 2027 ASN A CB    1 
ATOM   4570  C  CG    . ASN A 1 2027 ? 75.994  95.263  96.366  1.00 33.91  ? 2027 ASN A CG    1 
ATOM   4571  O  OD1   . ASN A 1 2027 ? 75.577  95.884  97.343  1.00 30.80  ? 2027 ASN A OD1   1 
ATOM   4572  N  ND2   . ASN A 1 2027 ? 76.880  95.772  95.518  1.00 35.90  ? 2027 ASN A ND2   1 
ATOM   4573  N  N     . LEU A 1 2028 ? 73.200  91.847  97.427  1.00 16.62  ? 2028 LEU A N     1 
ATOM   4574  C  CA    . LEU A 1 2028 ? 72.322  90.712  97.185  1.00 15.78  ? 2028 LEU A CA    1 
ATOM   4575  C  C     . LEU A 1 2028 ? 71.836  90.719  95.736  1.00 18.00  ? 2028 LEU A C     1 
ATOM   4576  O  O     . LEU A 1 2028 ? 71.346  91.741  95.250  1.00 21.58  ? 2028 LEU A O     1 
ATOM   4577  C  CB    . LEU A 1 2028 ? 71.126  90.738  98.134  1.00 14.55  ? 2028 LEU A CB    1 
ATOM   4578  C  CG    . LEU A 1 2028 ? 71.249  89.985  99.463  1.00 13.29  ? 2028 LEU A CG    1 
ATOM   4579  C  CD1   . LEU A 1 2028 ? 72.411  90.504  100.298 1.00 10.85  ? 2028 LEU A CD1   1 
ATOM   4580  C  CD2   . LEU A 1 2028 ? 69.945  90.061  100.244 1.00 12.55  ? 2028 LEU A CD2   1 
ATOM   4581  N  N     . PRO A 1 2029 ? 71.977  89.601  95.025  1.00 16.99  ? 2029 PRO A N     1 
ATOM   4582  C  CA    . PRO A 1 2029 ? 71.457  89.528  93.655  1.00 13.52  ? 2029 PRO A CA    1 
ATOM   4583  C  C     . PRO A 1 2029 ? 69.940  89.654  93.623  1.00 15.61  ? 2029 PRO A C     1 
ATOM   4584  O  O     . PRO A 1 2029 ? 69.242  89.305  94.577  1.00 14.91  ? 2029 PRO A O     1 
ATOM   4585  C  CB    . PRO A 1 2029 ? 71.921  88.149  93.169  1.00 10.47  ? 2029 PRO A CB    1 
ATOM   4586  C  CG    . PRO A 1 2029 ? 72.234  87.383  94.415  1.00 10.71  ? 2029 PRO A CG    1 
ATOM   4587  C  CD    . PRO A 1 2029 ? 72.707  88.384  95.412  1.00 13.90  ? 2029 PRO A CD    1 
ATOM   4588  N  N     . ASP A 1 2030 ? 69.436  90.166  92.496  1.00 14.90  ? 2030 ASP A N     1 
ATOM   4589  C  CA    . ASP A 1 2030 ? 68.024  90.525  92.393  1.00 13.94  ? 2030 ASP A CA    1 
ATOM   4590  C  C     . ASP A 1 2030 ? 67.115  89.310  92.538  1.00 11.93  ? 2030 ASP A C     1 
ATOM   4591  O  O     . ASP A 1 2030 ? 66.044  89.398  93.152  1.00 11.55  ? 2030 ASP A O     1 
ATOM   4592  C  CB    . ASP A 1 2030 ? 67.761  91.230  91.064  1.00 18.93  ? 2030 ASP A CB    1 
ATOM   4593  C  CG    . ASP A 1 2030 ? 68.418  92.589  90.991  1.00 27.65  ? 2030 ASP A CG    1 
ATOM   4594  O  OD1   . ASP A 1 2030 ? 68.092  93.448  91.835  1.00 33.12  ? 2030 ASP A OD1   1 
ATOM   4595  O  OD2   . ASP A 1 2030 ? 69.256  92.802  90.090  1.00 29.66  ? 2030 ASP A OD2   1 
ATOM   4596  N  N     . ASN A 1 2031 ? 67.507  88.174  91.957  1.00 11.67  ? 2031 ASN A N     1 
ATOM   4597  C  CA    . ASN A 1 2031 ? 66.677  86.978  92.057  1.00 12.46  ? 2031 ASN A CA    1 
ATOM   4598  C  C     . ASN A 1 2031 ? 66.562  86.508  93.502  1.00 10.73  ? 2031 ASN A C     1 
ATOM   4599  O  O     . ASN A 1 2031 ? 65.562  85.890  93.883  1.00 10.04  ? 2031 ASN A O     1 
ATOM   4600  C  CB    . ASN A 1 2031 ? 67.236  85.871  91.163  1.00 12.09  ? 2031 ASN A CB    1 
ATOM   4601  C  CG    . ASN A 1 2031 ? 68.623  85.434  91.575  1.00 11.07  ? 2031 ASN A CG    1 
ATOM   4602  O  OD1   . ASN A 1 2031 ? 69.551  86.240  91.628  1.00 12.36  ? 2031 ASN A OD1   1 
ATOM   4603  N  ND2   . ASN A 1 2031 ? 68.773  84.149  91.871  1.00 10.40  ? 2031 ASN A ND2   1 
ATOM   4604  N  N     . LEU A 1 2032 ? 67.581  86.782  94.320  1.00 9.01   ? 2032 LEU A N     1 
ATOM   4605  C  CA    . LEU A 1 2032 ? 67.471  86.505  95.748  1.00 7.41   ? 2032 LEU A CA    1 
ATOM   4606  C  C     . LEU A 1 2032 ? 66.570  87.520  96.443  1.00 7.32   ? 2032 LEU A C     1 
ATOM   4607  O  O     . LEU A 1 2032 ? 65.759  87.151  97.301  1.00 6.21   ? 2032 LEU A O     1 
ATOM   4608  C  CB    . LEU A 1 2032 ? 68.857  86.490  96.392  1.00 8.54   ? 2032 LEU A CB    1 
ATOM   4609  C  CG    . LEU A 1 2032 ? 68.906  86.108  97.874  1.00 5.19   ? 2032 LEU A CG    1 
ATOM   4610  C  CD1   . LEU A 1 2032 ? 68.235  84.766  98.115  1.00 4.69   ? 2032 LEU A CD1   1 
ATOM   4611  C  CD2   . LEU A 1 2032 ? 70.341  86.088  98.375  1.00 5.21   ? 2032 LEU A CD2   1 
ATOM   4612  N  N     . LYS A 1 2033 ? 66.698  88.802  96.088  1.00 7.40   ? 2033 LYS A N     1 
ATOM   4613  C  CA    . LYS A 1 2033 ? 65.936  89.838  96.781  1.00 6.84   ? 2033 LYS A CA    1 
ATOM   4614  C  C     . LYS A 1 2033 ? 64.445  89.732  96.489  1.00 7.47   ? 2033 LYS A C     1 
ATOM   4615  O  O     . LYS A 1 2033 ? 63.617  90.084  97.337  1.00 8.23   ? 2033 LYS A O     1 
ATOM   4616  C  CB    . LYS A 1 2033 ? 66.460  91.225  96.408  1.00 8.30   ? 2033 LYS A CB    1 
ATOM   4617  C  CG    . LYS A 1 2033 ? 67.869  91.498  96.900  1.00 10.30  ? 2033 LYS A CG    1 
ATOM   4618  C  CD    . LYS A 1 2033 ? 68.344  92.886  96.509  1.00 12.47  ? 2033 LYS A CD    1 
ATOM   4619  C  CE    . LYS A 1 2033 ? 68.377  93.056  95.004  1.00 20.80  ? 2033 LYS A CE    1 
ATOM   4620  N  NZ    . LYS A 1 2033 ? 68.843  94.412  94.609  1.00 25.34  ? 2033 LYS A NZ    1 
ATOM   4621  N  N     . LYS A 1 2034 ? 64.077  89.252  95.298  1.00 7.94   ? 2034 LYS A N     1 
ATOM   4622  C  CA    . LYS A 1 2034 ? 62.658  89.112  94.989  1.00 8.71   ? 2034 LYS A CA    1 
ATOM   4623  C  C     . LYS A 1 2034 ? 61.994  88.029  95.829  1.00 6.86   ? 2034 LYS A C     1 
ATOM   4624  O  O     . LYS A 1 2034 ? 60.762  87.992  95.911  1.00 9.35   ? 2034 LYS A O     1 
ATOM   4625  C  CB    . LYS A 1 2034 ? 62.446  88.810  93.505  1.00 10.60  ? 2034 LYS A CB    1 
ATOM   4626  C  CG    . LYS A 1 2034 ? 62.880  87.423  93.073  1.00 12.94  ? 2034 LYS A CG    1 
ATOM   4627  C  CD    . LYS A 1 2034 ? 62.793  87.267  91.565  1.00 18.60  ? 2034 LYS A CD    1 
ATOM   4628  C  CE    . LYS A 1 2034 ? 63.304  85.908  91.118  1.00 21.48  ? 2034 LYS A CE    1 
ATOM   4629  N  NZ    . LYS A 1 2034 ? 63.306  85.778  89.635  1.00 28.10  ? 2034 LYS A NZ    1 
ATOM   4630  N  N     . LEU A 1 2035 ? 62.779  87.151  96.452  1.00 7.14   ? 2035 LEU A N     1 
ATOM   4631  C  CA    . LEU A 1 2035 ? 62.240  86.134  97.344  1.00 6.11   ? 2035 LEU A CA    1 
ATOM   4632  C  C     . LEU A 1 2035 ? 61.943  86.670  98.736  1.00 4.58   ? 2035 LEU A C     1 
ATOM   4633  O  O     . LEU A 1 2035 ? 61.373  85.940  99.554  1.00 4.69   ? 2035 LEU A O     1 
ATOM   4634  C  CB    . LEU A 1 2035 ? 63.213  84.957  97.450  1.00 4.71   ? 2035 LEU A CB    1 
ATOM   4635  C  CG    . LEU A 1 2035 ? 63.738  84.385  96.133  1.00 7.47   ? 2035 LEU A CG    1 
ATOM   4636  C  CD1   . LEU A 1 2035 ? 64.701  83.239  96.393  1.00 5.22   ? 2035 LEU A CD1   1 
ATOM   4637  C  CD2   . LEU A 1 2035 ? 62.589  83.934  95.246  1.00 11.36  ? 2035 LEU A CD2   1 
ATOM   4638  N  N     . PHE A 1 2036 ? 62.311  87.915  99.024  1.00 4.08   ? 2036 PHE A N     1 
ATOM   4639  C  CA    . PHE A 1 2036 ? 62.137  88.495  100.344 1.00 4.37   ? 2036 PHE A CA    1 
ATOM   4640  C  C     . PHE A 1 2036 ? 61.372  89.807  100.255 1.00 6.04   ? 2036 PHE A C     1 
ATOM   4641  O  O     . PHE A 1 2036 ? 61.470  90.544  99.270  1.00 7.13   ? 2036 PHE A O     1 
ATOM   4642  C  CB    . PHE A 1 2036 ? 63.486  88.736  101.027 1.00 3.15   ? 2036 PHE A CB    1 
ATOM   4643  C  CG    . PHE A 1 2036 ? 64.221  87.477  101.363 1.00 2.69   ? 2036 PHE A CG    1 
ATOM   4644  C  CD1   . PHE A 1 2036 ? 65.091  86.902  100.453 1.00 3.21   ? 2036 PHE A CD1   1 
ATOM   4645  C  CD2   . PHE A 1 2036 ? 64.027  86.855  102.581 1.00 2.40   ? 2036 PHE A CD2   1 
ATOM   4646  C  CE1   . PHE A 1 2036 ? 65.764  85.737  100.759 1.00 3.56   ? 2036 PHE A CE1   1 
ATOM   4647  C  CE2   . PHE A 1 2036 ? 64.691  85.693  102.889 1.00 3.34   ? 2036 PHE A CE2   1 
ATOM   4648  C  CZ    . PHE A 1 2036 ? 65.564  85.132  101.981 1.00 4.69   ? 2036 PHE A CZ    1 
ATOM   4649  N  N     . ARG A 1 2037 ? 60.608  90.085  101.305 1.00 6.05   ? 2037 ARG A N     1 
ATOM   4650  C  CA    . ARG A 1 2037 ? 59.907  91.348  101.474 1.00 5.38   ? 2037 ARG A CA    1 
ATOM   4651  C  C     . ARG A 1 2037 ? 60.691  92.181  102.480 1.00 3.63   ? 2037 ARG A C     1 
ATOM   4652  O  O     . ARG A 1 2037 ? 60.908  91.743  103.615 1.00 4.61   ? 2037 ARG A O     1 
ATOM   4653  C  CB    . ARG A 1 2037 ? 58.477  91.110  101.954 1.00 5.89   ? 2037 ARG A CB    1 
ATOM   4654  C  CG    . ARG A 1 2037 ? 57.503  90.761  100.845 1.00 8.85   ? 2037 ARG A CG    1 
ATOM   4655  C  CD    . ARG A 1 2037 ? 57.206  91.968  99.977  1.00 11.60  ? 2037 ARG A CD    1 
ATOM   4656  N  NE    . ARG A 1 2037 ? 56.233  92.839  100.623 1.00 20.35  ? 2037 ARG A NE    1 
ATOM   4657  C  CZ    . ARG A 1 2037 ? 54.925  92.624  100.629 1.00 14.63  ? 2037 ARG A CZ    1 
ATOM   4658  N  NH1   . ARG A 1 2037 ? 54.389  91.602  99.982  1.00 10.78  ? 2037 ARG A NH1   1 
ATOM   4659  N  NH2   . ARG A 1 2037 ? 54.135  93.451  101.307 1.00 13.20  ? 2037 ARG A NH2   1 
ATOM   4660  N  N     . SER A 1 2038 ? 61.122  93.365  102.061 1.00 3.73   ? 2038 SER A N     1 
ATOM   4661  C  CA    . SER A 1 2038 ? 62.042  94.181  102.838 1.00 4.72   ? 2038 SER A CA    1 
ATOM   4662  C  C     . SER A 1 2038 ? 61.302  95.291  103.571 1.00 4.20   ? 2038 SER A C     1 
ATOM   4663  O  O     . SER A 1 2038 ? 60.343  95.867  103.050 1.00 6.54   ? 2038 SER A O     1 
ATOM   4664  C  CB    . SER A 1 2038 ? 63.123  94.784  101.939 1.00 5.18   ? 2038 SER A CB    1 
ATOM   4665  O  OG    . SER A 1 2038 ? 62.562  95.684  101.000 1.00 10.55  ? 2038 SER A OG    1 
ATOM   4666  N  N     . LEU A 1 2039 ? 61.754  95.578  104.788 1.00 3.11   ? 2039 LEU A N     1 
ATOM   4667  C  CA    . LEU A 1 2039 ? 61.253  96.692  105.583 1.00 3.67   ? 2039 LEU A CA    1 
ATOM   4668  C  C     . LEU A 1 2039 ? 62.420  97.473  106.163 1.00 3.90   ? 2039 LEU A C     1 
ATOM   4669  O  O     . LEU A 1 2039 ? 63.309  96.891  106.793 1.00 3.61   ? 2039 LEU A O     1 
ATOM   4670  C  CB    . LEU A 1 2039 ? 60.340  96.220  106.716 1.00 4.21   ? 2039 LEU A CB    1 
ATOM   4671  C  CG    . LEU A 1 2039 ? 60.038  97.347  107.710 1.00 6.28   ? 2039 LEU A CG    1 
ATOM   4672  C  CD1   . LEU A 1 2039 ? 59.029  98.336  107.159 1.00 4.56   ? 2039 LEU A CD1   1 
ATOM   4673  C  CD2   . LEU A 1 2039 ? 59.577  96.798  109.035 1.00 4.92   ? 2039 LEU A CD2   1 
ATOM   4674  N  N     . ALA A 1 2040 ? 62.407  98.788  105.963 1.00 3.70   ? 2040 ALA A N     1 
ATOM   4675  C  CA    . ALA A 1 2040 ? 63.406  99.660  106.563 1.00 3.94   ? 2040 ALA A CA    1 
ATOM   4676  C  C     . ALA A 1 2040 ? 63.072  99.866  108.035 1.00 5.05   ? 2040 ALA A C     1 
ATOM   4677  O  O     . ALA A 1 2040 ? 61.943  100.232 108.377 1.00 5.42   ? 2040 ALA A O     1 
ATOM   4678  C  CB    . ALA A 1 2040 ? 63.463  100.998 105.831 1.00 3.89   ? 2040 ALA A CB    1 
ATOM   4679  N  N     . MET A 1 2041 ? 64.047  99.624  108.900 1.00 6.08   ? 2041 MET A N     1 
ATOM   4680  C  CA    . MET A 1 2041 ? 63.896  99.804  110.340 1.00 7.01   ? 2041 MET A CA    1 
ATOM   4681  C  C     . MET A 1 2041 ? 65.078  100.656 110.794 1.00 8.09   ? 2041 MET A C     1 
ATOM   4682  O  O     . MET A 1 2041 ? 66.150  100.140 111.113 1.00 14.08  ? 2041 MET A O     1 
ATOM   4683  C  CB    . MET A 1 2041 ? 63.845  98.459  111.052 1.00 6.10   ? 2041 MET A CB    1 
ATOM   4684  C  CG    . MET A 1 2041 ? 62.494  97.771  110.951 1.00 7.70   ? 2041 MET A CG    1 
ATOM   4685  S  SD    . MET A 1 2041 ? 62.443  96.146  111.723 1.00 17.51  ? 2041 MET A SD    1 
ATOM   4686  C  CE    . MET A 1 2041 ? 62.314  96.605  113.445 1.00 5.80   ? 2041 MET A CE    1 
ATOM   4687  N  N     . THR A 1 2042 ? 64.878  101.970 110.811 1.00 9.80   ? 2042 THR A N     1 
ATOM   4688  C  CA    . THR A 1 2042 ? 65.965  102.916 111.030 1.00 13.70  ? 2042 THR A CA    1 
ATOM   4689  C  C     . THR A 1 2042 ? 65.810  103.751 112.290 1.00 15.33  ? 2042 THR A C     1 
ATOM   4690  O  O     . THR A 1 2042 ? 66.808  104.045 112.951 1.00 18.64  ? 2042 THR A O     1 
ATOM   4691  C  CB    . THR A 1 2042 ? 66.098  103.855 109.820 1.00 15.68  ? 2042 THR A CB    1 
ATOM   4692  O  OG1   . THR A 1 2042 ? 64.890  104.611 109.664 1.00 27.86  ? 2042 THR A OG1   1 
ATOM   4693  C  CG2   . THR A 1 2042 ? 66.354  103.056 108.552 1.00 9.27   ? 2042 THR A CG2   1 
ATOM   4694  N  N     . LYS A 1 2043 ? 64.586  104.144 112.647 1.00 13.85  ? 2043 LYS A N     1 
ATOM   4695  C  CA    . LYS A 1 2043 ? 64.339  105.048 113.770 1.00 16.18  ? 2043 LYS A CA    1 
ATOM   4696  C  C     . LYS A 1 2043 ? 63.402  104.379 114.766 1.00 15.94  ? 2043 LYS A C     1 
ATOM   4697  O  O     . LYS A 1 2043 ? 62.174  104.545 114.690 1.00 12.54  ? 2043 LYS A O     1 
ATOM   4698  C  CB    . LYS A 1 2043 ? 63.761  106.376 113.284 1.00 17.80  ? 2043 LYS A CB    1 
ATOM   4699  C  CG    . LYS A 1 2043 ? 64.668  107.127 112.325 1.00 23.91  ? 2043 LYS A CG    1 
ATOM   4700  C  CD    . LYS A 1 2043 ? 65.946  107.574 113.015 1.00 29.89  ? 2043 LYS A CD    1 
ATOM   4701  C  CE    . LYS A 1 2043 ? 66.778  108.467 112.110 1.00 26.06  ? 2043 LYS A CE    1 
ATOM   4702  N  NZ    . LYS A 1 2043 ? 67.349  107.710 110.962 1.00 26.07  ? 2043 LYS A NZ    1 
ATOM   4703  N  N     . PRO A 1 2044 ? 63.934  103.613 115.713 1.00 15.59  ? 2044 PRO A N     1 
ATOM   4704  C  CA    . PRO A 1 2044 ? 63.085  103.021 116.750 1.00 10.45  ? 2044 PRO A CA    1 
ATOM   4705  C  C     . PRO A 1 2044 ? 62.540  104.082 117.694 1.00 10.87  ? 2044 PRO A C     1 
ATOM   4706  O  O     . PRO A 1 2044 ? 63.128  105.148 117.890 1.00 12.38  ? 2044 PRO A O     1 
ATOM   4707  C  CB    . PRO A 1 2044 ? 64.033  102.061 117.480 1.00 9.13   ? 2044 PRO A CB    1 
ATOM   4708  C  CG    . PRO A 1 2044 ? 65.186  101.873 116.542 1.00 9.90   ? 2044 PRO A CG    1 
ATOM   4709  C  CD    . PRO A 1 2044 ? 65.334  103.185 115.853 1.00 10.20  ? 2044 PRO A CD    1 
ATOM   4710  N  N     . ASP A 1 2045 ? 61.388  103.770 118.285 1.00 10.04  ? 2045 ASP A N     1 
ATOM   4711  C  CA    . ASP A 1 2045 ? 60.695  104.689 119.187 1.00 9.94   ? 2045 ASP A CA    1 
ATOM   4712  C  C     . ASP A 1 2045 ? 61.288  104.536 120.582 1.00 7.20   ? 2045 ASP A C     1 
ATOM   4713  O  O     . ASP A 1 2045 ? 60.824  103.739 121.399 1.00 7.88   ? 2045 ASP A O     1 
ATOM   4714  C  CB    . ASP A 1 2045 ? 59.196  104.424 119.167 1.00 10.38  ? 2045 ASP A CB    1 
ATOM   4715  C  CG    . ASP A 1 2045 ? 58.640  104.356 117.758 1.00 13.48  ? 2045 ASP A CG    1 
ATOM   4716  O  OD1   . ASP A 1 2045 ? 58.759  105.359 117.024 1.00 17.24  ? 2045 ASP A OD1   1 
ATOM   4717  O  OD2   . ASP A 1 2045 ? 58.094  103.300 117.380 1.00 11.39  ? 2045 ASP A OD2   1 
ATOM   4718  N  N     . ARG A 1 2046 ? 62.332  105.321 120.854 1.00 7.83   ? 2046 ARG A N     1 
ATOM   4719  C  CA    . ARG A 1 2046 ? 63.053  105.211 122.119 1.00 5.96   ? 2046 ARG A CA    1 
ATOM   4720  C  C     . ARG A 1 2046 ? 62.181  105.638 123.294 1.00 4.65   ? 2046 ARG A C     1 
ATOM   4721  O  O     . ARG A 1 2046 ? 62.199  105.007 124.359 1.00 4.04   ? 2046 ARG A O     1 
ATOM   4722  C  CB    . ARG A 1 2046 ? 64.327  106.052 122.055 1.00 9.59   ? 2046 ARG A CB    1 
ATOM   4723  C  CG    . ARG A 1 2046 ? 65.441  105.416 121.241 1.00 9.13   ? 2046 ARG A CG    1 
ATOM   4724  C  CD    . ARG A 1 2046 ? 66.568  106.398 120.975 1.00 12.37  ? 2046 ARG A CD    1 
ATOM   4725  N  NE    . ARG A 1 2046 ? 67.126  106.227 119.638 1.00 19.81  ? 2046 ARG A NE    1 
ATOM   4726  C  CZ    . ARG A 1 2046 ? 68.388  105.913 119.383 1.00 19.96  ? 2046 ARG A CZ    1 
ATOM   4727  N  NH1   . ARG A 1 2046 ? 69.266  105.735 120.356 1.00 14.40  ? 2046 ARG A NH1   1 
ATOM   4728  N  NH2   . ARG A 1 2046 ? 68.780  105.776 118.120 1.00 22.69  ? 2046 ARG A NH2   1 
ATOM   4729  N  N     . GLN A 1 2047 ? 61.411  106.715 123.119 1.00 6.05   ? 2047 GLN A N     1 
ATOM   4730  C  CA    . GLN A 1 2047 ? 60.625  107.258 124.222 1.00 6.24   ? 2047 GLN A CA    1 
ATOM   4731  C  C     . GLN A 1 2047 ? 59.572  106.257 124.682 1.00 8.06   ? 2047 GLN A C     1 
ATOM   4732  O  O     . GLN A 1 2047 ? 59.378  106.052 125.887 1.00 6.92   ? 2047 GLN A O     1 
ATOM   4733  C  CB    . GLN A 1 2047 ? 59.983  108.584 123.793 1.00 9.19   ? 2047 GLN A CB    1 
ATOM   4734  C  CG    . GLN A 1 2047 ? 59.117  109.308 124.839 1.00 14.47  ? 2047 GLN A CG    1 
ATOM   4735  C  CD    . GLN A 1 2047 ? 57.775  108.648 125.114 1.00 23.73  ? 2047 GLN A CD    1 
ATOM   4736  O  OE1   . GLN A 1 2047 ? 57.111  108.153 124.203 1.00 24.40  ? 2047 GLN A OE1   1 
ATOM   4737  N  NE2   . GLN A 1 2047 ? 57.369  108.644 126.379 1.00 22.96  ? 2047 GLN A NE2   1 
ATOM   4738  N  N     . LEU A 1 2048 ? 58.887  105.617 123.733 1.00 5.71   ? 2048 LEU A N     1 
ATOM   4739  C  CA    . LEU A 1 2048 ? 57.827  104.680 124.088 1.00 5.49   ? 2048 LEU A CA    1 
ATOM   4740  C  C     . LEU A 1 2048 ? 58.391  103.459 124.805 1.00 6.18   ? 2048 LEU A C     1 
ATOM   4741  O  O     . LEU A 1 2048 ? 57.834  103.004 125.810 1.00 6.71   ? 2048 LEU A O     1 
ATOM   4742  C  CB    . LEU A 1 2048 ? 57.053  104.266 122.838 1.00 6.83   ? 2048 LEU A CB    1 
ATOM   4743  C  CG    . LEU A 1 2048 ? 56.021  103.156 123.032 1.00 6.52   ? 2048 LEU A CG    1 
ATOM   4744  C  CD1   . LEU A 1 2048 ? 54.938  103.602 123.999 1.00 5.54   ? 2048 LEU A CD1   1 
ATOM   4745  C  CD2   . LEU A 1 2048 ? 55.417  102.749 121.704 1.00 6.95   ? 2048 LEU A CD2   1 
ATOM   4746  N  N     . ILE A 1 2049 ? 59.500  102.913 124.299 1.00 4.01   ? 2049 ILE A N     1 
ATOM   4747  C  CA    . ILE A 1 2049 ? 60.127  101.765 124.949 1.00 4.68   ? 2049 ILE A CA    1 
ATOM   4748  C  C     . ILE A 1 2049 ? 60.578  102.127 126.356 1.00 5.21   ? 2049 ILE A C     1 
ATOM   4749  O  O     . ILE A 1 2049 ? 60.366  101.363 127.307 1.00 7.49   ? 2049 ILE A O     1 
ATOM   4750  C  CB    . ILE A 1 2049 ? 61.300  101.237 124.102 1.00 4.70   ? 2049 ILE A CB    1 
ATOM   4751  C  CG1   . ILE A 1 2049 ? 60.807  100.757 122.738 1.00 5.51   ? 2049 ILE A CG1   1 
ATOM   4752  C  CG2   . ILE A 1 2049 ? 62.043  100.135 124.840 1.00 4.13   ? 2049 ILE A CG2   1 
ATOM   4753  C  CD1   . ILE A 1 2049 ? 61.915  100.500 121.745 1.00 3.17   ? 2049 ILE A CD1   1 
ATOM   4754  N  N     . ALA A 1 2050 ? 61.210  103.293 126.513 1.00 5.36   ? 2050 ALA A N     1 
ATOM   4755  C  CA    . ALA A 1 2050 ? 61.669  103.708 127.834 1.00 4.84   ? 2050 ALA A CA    1 
ATOM   4756  C  C     . ALA A 1 2050 ? 60.499  103.853 128.798 1.00 5.16   ? 2050 ALA A C     1 
ATOM   4757  O  O     . ALA A 1 2050 ? 60.548  103.361 129.933 1.00 5.26   ? 2050 ALA A O     1 
ATOM   4758  C  CB    . ALA A 1 2050 ? 62.455  105.015 127.731 1.00 4.63   ? 2050 ALA A CB    1 
ATOM   4759  N  N     . GLN A 1 2051 ? 59.424  104.507 128.352 1.00 7.99   ? 2051 GLN A N     1 
ATOM   4760  C  CA    . GLN A 1 2051 ? 58.261  104.697 129.212 1.00 8.90   ? 2051 GLN A CA    1 
ATOM   4761  C  C     . GLN A 1 2051 ? 57.631  103.366 129.598 1.00 7.09   ? 2051 GLN A C     1 
ATOM   4762  O  O     . GLN A 1 2051 ? 57.305  103.148 130.771 1.00 11.27  ? 2051 GLN A O     1 
ATOM   4763  C  CB    . GLN A 1 2051 ? 57.243  105.601 128.515 1.00 12.04  ? 2051 GLN A CB    1 
ATOM   4764  C  CG    . GLN A 1 2051 ? 56.071  106.027 129.385 1.00 22.36  ? 2051 GLN A CG    1 
ATOM   4765  C  CD    . GLN A 1 2051 ? 54.944  105.009 129.382 1.00 34.28  ? 2051 GLN A CD    1 
ATOM   4766  O  OE1   . GLN A 1 2051 ? 54.744  104.292 128.403 1.00 30.85  ? 2051 GLN A OE1   1 
ATOM   4767  N  NE2   . GLN A 1 2051 ? 54.208  104.935 130.485 1.00 29.09  ? 2051 GLN A NE2   1 
ATOM   4768  N  N     . VAL A 1 2052 ? 57.471  102.457 128.635 1.00 8.17   ? 2052 VAL A N     1 
ATOM   4769  C  CA    . VAL A 1 2052 ? 56.818  101.186 128.927 1.00 6.99   ? 2052 VAL A CA    1 
ATOM   4770  C  C     . VAL A 1 2052 ? 57.671  100.344 129.867 1.00 7.74   ? 2052 VAL A C     1 
ATOM   4771  O  O     . VAL A 1 2052 ? 57.155  99.731  130.808 1.00 9.83   ? 2052 VAL A O     1 
ATOM   4772  C  CB    . VAL A 1 2052 ? 56.492  100.437 127.622 1.00 5.06   ? 2052 VAL A CB    1 
ATOM   4773  C  CG1   . VAL A 1 2052 ? 55.990  99.034  127.923 1.00 3.73   ? 2052 VAL A CG1   1 
ATOM   4774  C  CG2   . VAL A 1 2052 ? 55.450  101.203 126.825 1.00 5.80   ? 2052 VAL A CG2   1 
ATOM   4775  N  N     . MET A 1 2053 ? 58.988  100.306 129.642 1.00 6.39   ? 2053 MET A N     1 
ATOM   4776  C  CA    . MET A 1 2053 ? 59.852  99.520  130.515 1.00 7.53   ? 2053 MET A CA    1 
ATOM   4777  C  C     . MET A 1 2053 ? 59.888  100.088 131.929 1.00 10.29  ? 2053 MET A C     1 
ATOM   4778  O  O     . MET A 1 2053 ? 59.824  99.331  132.904 1.00 13.68  ? 2053 MET A O     1 
ATOM   4779  C  CB    . MET A 1 2053 ? 61.260  99.441  129.934 1.00 6.64   ? 2053 MET A CB    1 
ATOM   4780  C  CG    . MET A 1 2053 ? 61.434  98.442  128.815 1.00 9.15   ? 2053 MET A CG    1 
ATOM   4781  S  SD    . MET A 1 2053 ? 63.087  98.577  128.119 1.00 24.47  ? 2053 MET A SD    1 
ATOM   4782  C  CE    . MET A 1 2053 ? 64.052  97.794  129.411 1.00 13.08  ? 2053 MET A CE    1 
ATOM   4783  N  N     . LEU A 1 2054 ? 59.988  101.415 132.069 1.00 8.00   ? 2054 LEU A N     1 
ATOM   4784  C  CA    . LEU A 1 2054 ? 59.984  102.005 133.406 1.00 9.06   ? 2054 LEU A CA    1 
ATOM   4785  C  C     . LEU A 1 2054 ? 58.647  101.793 134.105 1.00 12.48  ? 2054 LEU A C     1 
ATOM   4786  O  O     . LEU A 1 2054 ? 58.607  101.586 135.323 1.00 16.39  ? 2054 LEU A O     1 
ATOM   4787  C  CB    . LEU A 1 2054 ? 60.322  103.494 133.336 1.00 8.94   ? 2054 LEU A CB    1 
ATOM   4788  C  CG    . LEU A 1 2054 ? 61.743  103.856 132.909 1.00 11.28  ? 2054 LEU A CG    1 
ATOM   4789  C  CD1   . LEU A 1 2054 ? 61.853  105.331 132.587 1.00 9.15   ? 2054 LEU A CD1   1 
ATOM   4790  C  CD2   . LEU A 1 2054 ? 62.744  103.462 133.986 1.00 9.63   ? 2054 LEU A CD2   1 
ATOM   4791  N  N     . TYR A 1 2055 ? 57.543  101.844 133.357 1.00 9.71   ? 2055 TYR A N     1 
ATOM   4792  C  CA    . TYR A 1 2055 ? 56.237  101.622 133.965 1.00 10.88  ? 2055 TYR A CA    1 
ATOM   4793  C  C     . TYR A 1 2055 ? 56.071  100.167 134.390 1.00 11.24  ? 2055 TYR A C     1 
ATOM   4794  O  O     . TYR A 1 2055 ? 55.454  99.880  135.422 1.00 12.07  ? 2055 TYR A O     1 
ATOM   4795  C  CB    . TYR A 1 2055 ? 55.138  102.046 132.990 1.00 10.69  ? 2055 TYR A CB    1 
ATOM   4796  C  CG    . TYR A 1 2055 ? 53.726  101.830 133.483 1.00 10.88  ? 2055 TYR A CG    1 
ATOM   4797  C  CD1   . TYR A 1 2055 ? 53.122  102.743 134.336 1.00 14.74  ? 2055 TYR A CD1   1 
ATOM   4798  C  CD2   . TYR A 1 2055 ? 52.987  100.731 133.075 1.00 12.71  ? 2055 TYR A CD2   1 
ATOM   4799  C  CE1   . TYR A 1 2055 ? 51.829  102.556 134.783 1.00 15.31  ? 2055 TYR A CE1   1 
ATOM   4800  C  CE2   . TYR A 1 2055 ? 51.693  100.535 133.515 1.00 15.02  ? 2055 TYR A CE2   1 
ATOM   4801  C  CZ    . TYR A 1 2055 ? 51.118  101.451 134.368 1.00 21.98  ? 2055 TYR A CZ    1 
ATOM   4802  O  OH    . TYR A 1 2055 ? 49.829  101.258 134.808 1.00 31.84  ? 2055 TYR A OH    1 
ATOM   4803  N  N     . SER A 1 2056 ? 56.623  99.233  133.610 1.00 11.18  ? 2056 SER A N     1 
ATOM   4804  C  CA    . SER A 1 2056 ? 56.524  97.821  133.964 1.00 11.65  ? 2056 SER A CA    1 
ATOM   4805  C  C     . SER A 1 2056 ? 57.447  97.458  135.121 1.00 12.33  ? 2056 SER A C     1 
ATOM   4806  O  O     . SER A 1 2056 ? 57.134  96.549  135.897 1.00 13.21  ? 2056 SER A O     1 
ATOM   4807  C  CB    . SER A 1 2056 ? 56.834  96.948  132.748 1.00 8.51   ? 2056 SER A CB    1 
ATOM   4808  O  OG    . SER A 1 2056 ? 58.079  97.298  132.173 1.00 9.38   ? 2056 SER A OG    1 
ATOM   4809  N  N     . GLN A 1 2057 ? 58.585  98.145  135.252 1.00 13.27  ? 2057 GLN A N     1 
ATOM   4810  C  CA    . GLN A 1 2057 ? 59.499  97.869  136.353 1.00 13.39  ? 2057 GLN A CA    1 
ATOM   4811  C  C     . GLN A 1 2057 ? 59.016  98.442  137.678 1.00 14.95  ? 2057 GLN A C     1 
ATOM   4812  O  O     . GLN A 1 2057 ? 59.566  98.087  138.726 1.00 17.53  ? 2057 GLN A O     1 
ATOM   4813  C  CB    . GLN A 1 2057 ? 60.894  98.413  136.036 1.00 13.63  ? 2057 GLN A CB    1 
ATOM   4814  C  CG    . GLN A 1 2057 ? 61.608  97.682  134.910 1.00 12.59  ? 2057 GLN A CG    1 
ATOM   4815  C  CD    . GLN A 1 2057 ? 62.722  98.507  134.296 1.00 19.13  ? 2057 GLN A CD    1 
ATOM   4816  O  OE1   . GLN A 1 2057 ? 62.964  99.644  134.701 1.00 22.01  ? 2057 GLN A OE1   1 
ATOM   4817  N  NE2   . GLN A 1 2057 ? 63.405  97.939  133.309 1.00 21.11  ? 2057 GLN A NE2   1 
ATOM   4818  N  N     . GLY A 1 2058 ? 58.007  99.308  137.660 1.00 14.31  ? 2058 GLY A N     1 
ATOM   4819  C  CA    . GLY A 1 2058 ? 57.448  99.865  138.872 1.00 14.70  ? 2058 GLY A CA    1 
ATOM   4820  C  C     . GLY A 1 2058 ? 57.803  101.307 139.168 1.00 15.00  ? 2058 GLY A C     1 
ATOM   4821  O  O     . GLY A 1 2058 ? 57.494  101.784 140.265 1.00 23.48  ? 2058 GLY A O     1 
ATOM   4822  N  N     . PHE A 1 2059 ? 58.440  102.014 138.239 1.00 12.98  ? 2059 PHE A N     1 
ATOM   4823  C  CA    . PHE A 1 2059 ? 58.746  103.424 138.449 1.00 15.42  ? 2059 PHE A CA    1 
ATOM   4824  C  C     . PHE A 1 2059 ? 57.468  104.246 138.330 1.00 20.16  ? 2059 PHE A C     1 
ATOM   4825  O  O     . PHE A 1 2059 ? 56.786  104.199 137.300 1.00 22.01  ? 2059 PHE A O     1 
ATOM   4826  C  CB    . PHE A 1 2059 ? 59.788  103.897 137.439 1.00 14.89  ? 2059 PHE A CB    1 
ATOM   4827  C  CG    . PHE A 1 2059 ? 61.168  103.349 137.682 1.00 12.39  ? 2059 PHE A CG    1 
ATOM   4828  C  CD1   . PHE A 1 2059 ? 61.538  102.116 137.172 1.00 13.63  ? 2059 PHE A CD1   1 
ATOM   4829  C  CD2   . PHE A 1 2059 ? 62.097  104.072 138.411 1.00 12.16  ? 2059 PHE A CD2   1 
ATOM   4830  C  CE1   . PHE A 1 2059 ? 62.807  101.612 137.390 1.00 11.50  ? 2059 PHE A CE1   1 
ATOM   4831  C  CE2   . PHE A 1 2059 ? 63.368  103.575 138.630 1.00 12.34  ? 2059 PHE A CE2   1 
ATOM   4832  C  CZ    . PHE A 1 2059 ? 63.722  102.342 138.119 1.00 12.06  ? 2059 PHE A CZ    1 
ATOM   4833  N  N     . ARG A 1 2060 ? 57.141  105.001 139.382 1.00 24.23  ? 2060 ARG A N     1 
ATOM   4834  C  CA    . ARG A 1 2060 ? 55.902  105.772 139.378 1.00 25.12  ? 2060 ARG A CA    1 
ATOM   4835  C  C     . ARG A 1 2060 ? 55.987  106.973 138.444 1.00 27.32  ? 2060 ARG A C     1 
ATOM   4836  O  O     . ARG A 1 2060 ? 54.973  107.385 137.869 1.00 34.28  ? 2060 ARG A O     1 
ATOM   4837  C  CB    . ARG A 1 2060 ? 55.560  106.227 140.797 1.00 34.90  ? 2060 ARG A CB    1 
ATOM   4838  C  CG    . ARG A 1 2060 ? 54.216  106.929 140.917 1.00 55.46  ? 2060 ARG A CG    1 
ATOM   4839  C  CD    . ARG A 1 2060 ? 53.911  107.291 142.359 1.00 67.81  ? 2060 ARG A CD    1 
ATOM   4840  N  NE    . ARG A 1 2060 ? 54.858  108.268 142.882 1.00 68.66  ? 2060 ARG A NE    1 
ATOM   4841  C  CZ    . ARG A 1 2060 ? 55.732  108.019 143.847 1.00 72.34  ? 2060 ARG A CZ    1 
ATOM   4842  N  NH1   . ARG A 1 2060 ? 55.823  106.823 144.404 1.00 72.43  ? 2060 ARG A NH1   1 
ATOM   4843  N  NH2   . ARG A 1 2060 ? 56.540  108.992 144.258 1.00 74.03  ? 2060 ARG A NH2   1 
ATOM   4844  N  N     . THR A 1 2061 ? 57.179  107.540 138.274 1.00 25.96  ? 2061 THR A N     1 
ATOM   4845  C  CA    . THR A 1 2061 ? 57.395  108.698 137.410 1.00 20.60  ? 2061 THR A CA    1 
ATOM   4846  C  C     . THR A 1 2061 ? 57.930  108.286 136.046 1.00 22.36  ? 2061 THR A C     1 
ATOM   4847  O  O     . THR A 1 2061 ? 58.763  108.981 135.459 1.00 24.42  ? 2061 THR A O     1 
ATOM   4848  C  CB    . THR A 1 2061 ? 58.341  109.692 138.078 1.00 19.97  ? 2061 THR A CB    1 
ATOM   4849  O  OG1   . THR A 1 2061 ? 59.506  109.003 138.550 1.00 24.86  ? 2061 THR A OG1   1 
ATOM   4850  C  CG2   . THR A 1 2061 ? 57.653  110.372 139.251 1.00 18.81  ? 2061 THR A CG2   1 
ATOM   4851  N  N     . ALA A 1 2062 ? 57.450  107.151 135.527 1.00 27.53  ? 2062 ALA A N     1 
ATOM   4852  C  CA    . ALA A 1 2062 ? 58.009  106.576 134.306 1.00 18.39  ? 2062 ALA A CA    1 
ATOM   4853  C  C     . ALA A 1 2062 ? 57.944  107.550 133.136 1.00 21.01  ? 2062 ALA A C     1 
ATOM   4854  O  O     . ALA A 1 2062 ? 58.872  107.611 132.321 1.00 23.82  ? 2062 ALA A O     1 
ATOM   4855  C  CB    . ALA A 1 2062 ? 57.278  105.279 133.962 1.00 14.77  ? 2062 ALA A CB    1 
ATOM   4856  N  N     . GLU A 1 2063 ? 56.858  108.320 133.033 1.00 22.90  ? 2063 GLU A N     1 
ATOM   4857  C  CA    . GLU A 1 2063 ? 56.722  109.262 131.926 1.00 23.80  ? 2063 GLU A CA    1 
ATOM   4858  C  C     . GLU A 1 2063 ? 57.822  110.316 131.971 1.00 25.94  ? 2063 GLU A C     1 
ATOM   4859  O  O     . GLU A 1 2063 ? 58.521  110.550 130.976 1.00 26.12  ? 2063 GLU A O     1 
ATOM   4860  C  CB    . GLU A 1 2063 ? 55.346  109.938 131.956 1.00 33.63  ? 2063 GLU A CB    1 
ATOM   4861  C  CG    . GLU A 1 2063 ? 54.127  109.052 131.667 1.00 40.89  ? 2063 GLU A CG    1 
ATOM   4862  C  CD    . GLU A 1 2063 ? 54.081  107.782 132.493 1.00 44.90  ? 2063 GLU A CD    1 
ATOM   4863  O  OE1   . GLU A 1 2063 ? 54.169  106.683 131.909 1.00 39.68  ? 2063 GLU A OE1   1 
ATOM   4864  O  OE2   . GLU A 1 2063 ? 53.958  107.884 133.732 1.00 42.02  ? 2063 GLU A OE2   1 
ATOM   4865  N  N     . VAL A 1 2064 ? 57.991  110.956 133.130 1.00 24.49  ? 2064 VAL A N     1 
ATOM   4866  C  CA    . VAL A 1 2064 ? 59.008  111.993 133.279 1.00 24.03  ? 2064 VAL A CA    1 
ATOM   4867  C  C     . VAL A 1 2064 ? 60.401  111.398 133.128 1.00 21.27  ? 2064 VAL A C     1 
ATOM   4868  O  O     . VAL A 1 2064 ? 61.281  111.991 132.491 1.00 28.02  ? 2064 VAL A O     1 
ATOM   4869  C  CB    . VAL A 1 2064 ? 58.839  112.709 134.632 1.00 25.72  ? 2064 VAL A CB    1 
ATOM   4870  C  CG1   . VAL A 1 2064 ? 59.953  113.719 134.847 1.00 25.66  ? 2064 VAL A CG1   1 
ATOM   4871  C  CG2   . VAL A 1 2064 ? 57.477  113.381 134.709 1.00 21.08  ? 2064 VAL A CG2   1 
ATOM   4872  N  N     . LEU A 1 2065 ? 60.623  110.216 133.706 1.00 20.29  ? 2065 LEU A N     1 
ATOM   4873  C  CA    . LEU A 1 2065 ? 61.934  109.583 133.607 1.00 19.48  ? 2065 LEU A CA    1 
ATOM   4874  C  C     . LEU A 1 2065 ? 62.300  109.287 132.158 1.00 16.99  ? 2065 LEU A C     1 
ATOM   4875  O  O     . LEU A 1 2065 ? 63.440  109.518 131.744 1.00 24.71  ? 2065 LEU A O     1 
ATOM   4876  C  CB    . LEU A 1 2065 ? 61.968  108.306 134.445 1.00 16.56  ? 2065 LEU A CB    1 
ATOM   4877  C  CG    . LEU A 1 2065 ? 61.830  108.464 135.959 1.00 18.18  ? 2065 LEU A CG    1 
ATOM   4878  C  CD1   . LEU A 1 2065 ? 61.788  107.103 136.631 1.00 16.93  ? 2065 LEU A CD1   1 
ATOM   4879  C  CD2   . LEU A 1 2065 ? 62.966  109.301 136.512 1.00 19.07  ? 2065 LEU A CD2   1 
ATOM   4880  N  N     . ALA A 1 2066 ? 61.349  108.783 131.368 1.00 16.21  ? 2066 ALA A N     1 
ATOM   4881  C  CA    . ALA A 1 2066 ? 61.635  108.509 129.961 1.00 17.44  ? 2066 ALA A CA    1 
ATOM   4882  C  C     . ALA A 1 2066 ? 61.855  109.797 129.176 1.00 22.25  ? 2066 ALA A C     1 
ATOM   4883  O  O     . ALA A 1 2066 ? 62.812  109.900 128.388 1.00 26.67  ? 2066 ALA A O     1 
ATOM   4884  C  CB    . ALA A 1 2066 ? 60.502  107.688 129.347 1.00 12.68  ? 2066 ALA A CB    1 
ATOM   4885  N  N     . ASN A 1 2067 ? 60.982  110.792 129.381 1.00 24.06  ? 2067 ASN A N     1 
ATOM   4886  C  CA    . ASN A 1 2067 ? 61.113  112.082 128.713 1.00 22.21  ? 2067 ASN A CA    1 
ATOM   4887  C  C     . ASN A 1 2067 ? 62.387  112.813 129.098 1.00 24.82  ? 2067 ASN A C     1 
ATOM   4888  O  O     . ASN A 1 2067 ? 62.777  113.753 128.398 1.00 29.29  ? 2067 ASN A O     1 
ATOM   4889  C  CB    . ASN A 1 2067 ? 59.904  112.968 129.027 1.00 27.88  ? 2067 ASN A CB    1 
ATOM   4890  C  CG    . ASN A 1 2067 ? 58.685  112.609 128.203 1.00 36.71  ? 2067 ASN A CG    1 
ATOM   4891  O  OD1   . ASN A 1 2067 ? 57.637  112.256 128.744 1.00 37.89  ? 2067 ASN A OD1   1 
ATOM   4892  N  ND2   . ASN A 1 2067 ? 58.813  112.705 126.885 1.00 34.72  ? 2067 ASN A ND2   1 
ATOM   4893  N  N     . LYS A 1 2068 ? 63.021  112.435 130.205 1.00 19.65  ? 2068 LYS A N     1 
ATOM   4894  C  CA    . LYS A 1 2068 ? 64.327  112.971 130.561 1.00 21.05  ? 2068 LYS A CA    1 
ATOM   4895  C  C     . LYS A 1 2068 ? 65.483  112.111 130.068 1.00 19.55  ? 2068 LYS A C     1 
ATOM   4896  O  O     . LYS A 1 2068 ? 66.548  112.647 129.752 1.00 18.97  ? 2068 LYS A O     1 
ATOM   4897  C  CB    . LYS A 1 2068 ? 64.436  113.144 132.079 1.00 20.31  ? 2068 LYS A CB    1 
ATOM   4898  C  CG    . LYS A 1 2068 ? 63.563  114.249 132.647 1.00 21.20  ? 2068 LYS A CG    1 
ATOM   4899  C  CD    . LYS A 1 2068 ? 63.737  114.365 134.152 1.00 22.42  ? 2068 LYS A CD    1 
ATOM   4900  C  CE    . LYS A 1 2068 ? 63.048  115.606 134.693 1.00 25.36  ? 2068 LYS A CE    1 
ATOM   4901  N  NZ    . LYS A 1 2068 ? 63.576  116.850 134.069 1.00 25.41  ? 2068 LYS A NZ    1 
ATOM   4902  N  N     . ILE A 1 2069 ? 65.302  110.791 129.983 1.00 16.10  ? 2069 ILE A N     1 
ATOM   4903  C  CA    . ILE A 1 2069 ? 66.435  109.914 129.700 1.00 16.97  ? 2069 ILE A CA    1 
ATOM   4904  C  C     . ILE A 1 2069 ? 66.710  109.849 128.201 1.00 17.78  ? 2069 ILE A C     1 
ATOM   4905  O  O     . ILE A 1 2069 ? 67.871  109.829 127.775 1.00 19.72  ? 2069 ILE A O     1 
ATOM   4906  C  CB    . ILE A 1 2069 ? 66.213  108.515 130.310 1.00 17.05  ? 2069 ILE A CB    1 
ATOM   4907  C  CG1   . ILE A 1 2069 ? 67.504  107.698 130.246 1.00 17.24  ? 2069 ILE A CG1   1 
ATOM   4908  C  CG2   . ILE A 1 2069 ? 65.092  107.761 129.613 1.00 12.33  ? 2069 ILE A CG2   1 
ATOM   4909  C  CD1   . ILE A 1 2069 ? 68.682  108.372 130.906 1.00 12.54  ? 2069 ILE A CD1   1 
ATOM   4910  N  N     . VAL A 1 2070 ? 65.659  109.805 127.372 1.00 14.52  ? 2070 VAL A N     1 
ATOM   4911  C  CA    . VAL A 1 2070 ? 65.878  109.742 125.922 1.00 16.15  ? 2070 VAL A CA    1 
ATOM   4912  C  C     . VAL A 1 2070 ? 66.541  111.010 125.390 1.00 16.89  ? 2070 VAL A C     1 
ATOM   4913  O  O     . VAL A 1 2070 ? 67.574  110.901 124.702 1.00 17.24  ? 2070 VAL A O     1 
ATOM   4914  C  CB    . VAL A 1 2070 ? 64.561  109.398 125.201 1.00 14.07  ? 2070 VAL A CB    1 
ATOM   4915  C  CG1   . VAL A 1 2070 ? 64.740  109.494 123.695 1.00 9.14   ? 2070 VAL A CG1   1 
ATOM   4916  C  CG2   . VAL A 1 2070 ? 64.088  108.009 125.599 1.00 9.46   ? 2070 VAL A CG2   1 
ATOM   4917  N  N     . PRO A 1 2071 ? 66.037  112.219 125.668 1.00 17.60  ? 2071 PRO A N     1 
ATOM   4918  C  CA    . PRO A 1 2071 ? 66.783  113.416 125.253 1.00 20.15  ? 2071 PRO A CA    1 
ATOM   4919  C  C     . PRO A 1 2071 ? 68.145  113.526 125.908 1.00 16.53  ? 2071 PRO A C     1 
ATOM   4920  O  O     . PRO A 1 2071 ? 69.046  114.137 125.326 1.00 20.32  ? 2071 PRO A O     1 
ATOM   4921  C  CB    . PRO A 1 2071 ? 65.857  114.570 125.666 1.00 19.88  ? 2071 PRO A CB    1 
ATOM   4922  C  CG    . PRO A 1 2071 ? 64.512  113.953 125.761 1.00 20.95  ? 2071 PRO A CG    1 
ATOM   4923  C  CD    . PRO A 1 2071 ? 64.766  112.591 126.311 1.00 15.63  ? 2071 PRO A CD    1 
ATOM   4924  N  N     . PHE A 1 2072 ? 68.330  112.954 127.100 1.00 12.86  ? 2072 PHE A N     1 
ATOM   4925  C  CA    . PHE A 1 2072 ? 69.661  112.931 127.695 1.00 17.70  ? 2072 PHE A CA    1 
ATOM   4926  C  C     . PHE A 1 2072 ? 70.619  112.097 126.855 1.00 19.63  ? 2072 PHE A C     1 
ATOM   4927  O  O     . PHE A 1 2072 ? 71.784  112.464 126.676 1.00 20.03  ? 2072 PHE A O     1 
ATOM   4928  C  CB    . PHE A 1 2072 ? 69.605  112.402 129.127 1.00 16.15  ? 2072 PHE A CB    1 
ATOM   4929  C  CG    . PHE A 1 2072 ? 70.956  112.273 129.768 1.00 17.44  ? 2072 PHE A CG    1 
ATOM   4930  C  CD1   . PHE A 1 2072 ? 71.579  113.375 130.327 1.00 18.21  ? 2072 PHE A CD1   1 
ATOM   4931  C  CD2   . PHE A 1 2072 ? 71.604  111.050 129.808 1.00 16.77  ? 2072 PHE A CD2   1 
ATOM   4932  C  CE1   . PHE A 1 2072 ? 72.824  113.261 130.910 1.00 18.77  ? 2072 PHE A CE1   1 
ATOM   4933  C  CE2   . PHE A 1 2072 ? 72.847  110.929 130.392 1.00 15.24  ? 2072 PHE A CE2   1 
ATOM   4934  C  CZ    . PHE A 1 2072 ? 73.459  112.036 130.942 1.00 18.72  ? 2072 PHE A CZ    1 
ATOM   4935  N  N     . PHE A 1 2073 ? 70.147  110.961 126.338 1.00 17.20  ? 2073 PHE A N     1 
ATOM   4936  C  CA    . PHE A 1 2073 ? 70.980  110.167 125.442 1.00 17.84  ? 2073 PHE A CA    1 
ATOM   4937  C  C     . PHE A 1 2073 ? 71.282  110.923 124.156 1.00 19.52  ? 2073 PHE A C     1 
ATOM   4938  O  O     . PHE A 1 2073 ? 72.406  110.864 123.642 1.00 21.55  ? 2073 PHE A O     1 
ATOM   4939  C  CB    . PHE A 1 2073 ? 70.308  108.828 125.143 1.00 16.28  ? 2073 PHE A CB    1 
ATOM   4940  C  CG    . PHE A 1 2073 ? 70.734  107.724 126.063 1.00 11.56  ? 2073 PHE A CG    1 
ATOM   4941  C  CD1   . PHE A 1 2073 ? 70.110  107.540 127.285 1.00 13.28  ? 2073 PHE A CD1   1 
ATOM   4942  C  CD2   . PHE A 1 2073 ? 71.762  106.870 125.706 1.00 11.73  ? 2073 PHE A CD2   1 
ATOM   4943  C  CE1   . PHE A 1 2073 ? 70.506  106.524 128.133 1.00 11.88  ? 2073 PHE A CE1   1 
ATOM   4944  C  CE2   . PHE A 1 2073 ? 72.160  105.853 126.547 1.00 9.94   ? 2073 PHE A CE2   1 
ATOM   4945  C  CZ    . PHE A 1 2073 ? 71.532  105.680 127.762 1.00 8.75   ? 2073 PHE A CZ    1 
ATOM   4946  N  N     . LYS A 1 2074 ? 70.296  111.649 123.623 1.00 23.93  ? 2074 LYS A N     1 
ATOM   4947  C  CA    . LYS A 1 2074 ? 70.556  112.467 122.439 1.00 23.43  ? 2074 LYS A CA    1 
ATOM   4948  C  C     . LYS A 1 2074 ? 71.614  113.533 122.726 1.00 22.66  ? 2074 LYS A C     1 
ATOM   4949  O  O     . LYS A 1 2074 ? 72.524  113.765 121.916 1.00 24.00  ? 2074 LYS A O     1 
ATOM   4950  C  CB    . LYS A 1 2074 ? 69.257  113.110 121.955 1.00 26.24  ? 2074 LYS A CB    1 
ATOM   4951  C  CG    . LYS A 1 2074 ? 69.407  113.949 120.698 1.00 33.91  ? 2074 LYS A CG    1 
ATOM   4952  C  CD    . LYS A 1 2074 ? 69.836  113.095 119.518 1.00 39.61  ? 2074 LYS A CD    1 
ATOM   4953  C  CE    . LYS A 1 2074 ? 68.718  112.161 119.083 1.00 50.46  ? 2074 LYS A CE    1 
ATOM   4954  N  NZ    . LYS A 1 2074 ? 69.094  111.356 117.888 1.00 62.44  ? 2074 LYS A NZ    1 
ATOM   4955  N  N     . LEU A 1 2075 ? 71.512  114.183 123.887 1.00 21.39  ? 2075 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 2075 ? 72.449  115.243 124.242 1.00 22.60  ? 2075 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 2075 ? 73.831  114.681 124.548 1.00 24.84  ? 2075 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 2075 ? 74.836  115.375 124.384 1.00 27.79  ? 2075 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 2075 ? 71.917  116.035 125.436 1.00 23.34  ? 2075 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 2075 ? 70.705  116.930 125.176 1.00 28.55  ? 2075 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 2075 ? 69.941  117.177 126.467 1.00 24.75  ? 2075 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 2075 ? 71.135  118.244 124.544 1.00 32.98  ? 2075 LEU A CD2   1 
ATOM   4963  N  N     . CYS A 1 2076 ? 73.903  113.434 125.010 1.00 22.37  ? 2076 CYS A N     1 
ATOM   4964  C  CA    . CYS A 1 2076 ? 75.206  112.801 125.182 1.00 19.26  ? 2076 CYS A CA    1 
ATOM   4965  C  C     . CYS A 1 2076 ? 75.814  112.437 123.836 1.00 19.18  ? 2076 CYS A C     1 
ATOM   4966  O  O     . CYS A 1 2076 ? 77.032  112.527 123.650 1.00 19.92  ? 2076 CYS A O     1 
ATOM   4967  C  CB    . CYS A 1 2076 ? 75.084  111.567 126.073 1.00 15.34  ? 2076 CYS A CB    1 
ATOM   4968  S  SG    . CYS A 1 2076 ? 74.854  111.950 127.814 1.00 26.96  ? 2076 CYS A SG    1 
ATOM   4969  N  N     . ASP A 1 2077 ? 74.977  112.017 122.886 1.00 22.02  ? 2077 ASP A N     1 
ATOM   4970  C  CA    . ASP A 1 2077 ? 75.475  111.719 121.549 1.00 20.69  ? 2077 ASP A CA    1 
ATOM   4971  C  C     . ASP A 1 2077 ? 76.031  112.967 120.873 1.00 22.15  ? 2077 ASP A C     1 
ATOM   4972  O  O     . ASP A 1 2077 ? 77.075  112.910 120.212 1.00 30.98  ? 2077 ASP A O     1 
ATOM   4973  C  CB    . ASP A 1 2077 ? 74.365  111.100 120.701 1.00 20.91  ? 2077 ASP A CB    1 
ATOM   4974  C  CG    . ASP A 1 2077 ? 74.772  110.917 119.253 1.00 30.12  ? 2077 ASP A CG    1 
ATOM   4975  O  OD1   . ASP A 1 2077 ? 75.751  110.185 118.997 1.00 32.37  ? 2077 ASP A OD1   1 
ATOM   4976  O  OD2   . ASP A 1 2077 ? 74.114  111.505 118.370 1.00 36.47  ? 2077 ASP A OD2   1 
ATOM   4977  N  N     . GLU A 1 2078 ? 75.354  114.104 121.028 1.00 24.85  ? 2078 GLU A N     1 
ATOM   4978  C  CA    . GLU A 1 2078 ? 75.724  115.300 120.274 1.00 23.70  ? 2078 GLU A CA    1 
ATOM   4979  C  C     . GLU A 1 2078 ? 76.650  116.251 121.030 1.00 26.05  ? 2078 GLU A C     1 
ATOM   4980  O  O     . GLU A 1 2078 ? 77.618  116.753 120.452 1.00 30.89  ? 2078 GLU A O     1 
ATOM   4981  C  CB    . GLU A 1 2078 ? 74.457  116.034 119.824 1.00 27.37  ? 2078 GLU A CB    1 
ATOM   4982  C  CG    . GLU A 1 2078 ? 73.744  115.331 118.678 1.00 35.64  ? 2078 GLU A CG    1 
ATOM   4983  C  CD    . GLU A 1 2078 ? 72.286  115.713 118.572 1.00 47.59  ? 2078 GLU A CD    1 
ATOM   4984  O  OE1   . GLU A 1 2078 ? 71.808  116.462 119.446 1.00 43.66  ? 2078 GLU A OE1   1 
ATOM   4985  O  OE2   . GLU A 1 2078 ? 71.619  115.268 117.615 1.00 52.43  ? 2078 GLU A OE2   1 
ATOM   4986  N  N     . GLN A 1 2079 ? 76.378  116.515 122.309 1.00 23.61  ? 2079 GLN A N     1 
ATOM   4987  C  CA    . GLN A 1 2079 ? 77.174  117.480 123.064 1.00 26.21  ? 2079 GLN A CA    1 
ATOM   4988  C  C     . GLN A 1 2079 ? 78.559  116.937 123.398 1.00 32.87  ? 2079 GLN A C     1 
ATOM   4989  O  O     . GLN A 1 2079 ? 79.541  117.688 123.388 1.00 38.46  ? 2079 GLN A O     1 
ATOM   4990  C  CB    . GLN A 1 2079 ? 76.438  117.877 124.344 1.00 27.15  ? 2079 GLN A CB    1 
ATOM   4991  C  CG    . GLN A 1 2079 ? 75.137  118.629 124.115 1.00 31.62  ? 2079 GLN A CG    1 
ATOM   4992  C  CD    . GLN A 1 2079 ? 75.346  119.954 123.411 1.00 39.29  ? 2079 GLN A CD    1 
ATOM   4993  O  OE1   . GLN A 1 2079 ? 75.882  120.899 123.989 1.00 43.77  ? 2079 GLN A OE1   1 
ATOM   4994  N  NE2   . GLN A 1 2079 ? 74.924  120.029 122.155 1.00 43.30  ? 2079 GLN A NE2   1 
ATOM   4995  N  N     . LEU A 1 2080 ? 78.659  115.651 123.722 1.00 27.04  ? 2080 LEU A N     1 
ATOM   4996  C  CA    . LEU A 1 2080 ? 79.947  115.072 124.073 1.00 22.71  ? 2080 LEU A CA    1 
ATOM   4997  C  C     . LEU A 1 2080 ? 80.825  114.921 122.833 1.00 26.04  ? 2080 LEU A C     1 
ATOM   4998  O  O     . LEU A 1 2080 ? 80.342  114.840 121.701 1.00 31.98  ? 2080 LEU A O     1 
ATOM   4999  C  CB    . LEU A 1 2080 ? 79.766  113.715 124.753 1.00 19.08  ? 2080 LEU A CB    1 
ATOM   5000  C  CG    . LEU A 1 2080 ? 79.025  113.703 126.090 1.00 19.25  ? 2080 LEU A CG    1 
ATOM   5001  C  CD1   . LEU A 1 2080 ? 78.770  112.275 126.547 1.00 19.91  ? 2080 LEU A CD1   1 
ATOM   5002  C  CD2   . LEU A 1 2080 ? 79.809  114.470 127.140 1.00 22.76  ? 2080 LEU A CD2   1 
ATOM   5003  N  N     . SER A 1 2081 ? 82.136  114.880 123.065 1.00 23.63  ? 2081 SER A N     1 
ATOM   5004  C  CA    . SER A 1 2081 ? 83.090  114.790 121.972 1.00 25.82  ? 2081 SER A CA    1 
ATOM   5005  C  C     . SER A 1 2081 ? 82.949  113.455 121.242 1.00 23.10  ? 2081 SER A C     1 
ATOM   5006  O  O     . SER A 1 2081 ? 82.362  112.493 121.743 1.00 22.68  ? 2081 SER A O     1 
ATOM   5007  C  CB    . SER A 1 2081 ? 84.517  114.959 122.491 1.00 26.14  ? 2081 SER A CB    1 
ATOM   5008  O  OG    . SER A 1 2081 ? 84.982  113.770 123.105 1.00 19.31  ? 2081 SER A OG    1 
ATOM   5009  N  N     . SER A 1 2082 ? 83.507  113.407 120.036 1.00 22.65  ? 2082 SER A N     1 
ATOM   5010  C  CA    . SER A 1 2082 ? 83.387  112.240 119.174 1.00 23.58  ? 2082 SER A CA    1 
ATOM   5011  C  C     . SER A 1 2082 ? 84.530  111.271 119.442 1.00 23.91  ? 2082 SER A C     1 
ATOM   5012  O  O     . SER A 1 2082 ? 85.703  111.622 119.284 1.00 22.09  ? 2082 SER A O     1 
ATOM   5013  C  CB    . SER A 1 2082 ? 83.380  112.658 117.703 1.00 28.17  ? 2082 SER A CB    1 
ATOM   5014  O  OG    . SER A 1 2082 ? 82.324  113.563 117.436 1.00 40.25  ? 2082 SER A OG    1 
ATOM   5015  N  N     . GLN A 1 2083 ? 84.180  110.053 119.850 1.00 23.54  ? 2083 GLN A N     1 
ATOM   5016  C  CA    . GLN A 1 2083 ? 85.144  108.986 120.069 1.00 15.19  ? 2083 GLN A CA    1 
ATOM   5017  C  C     . GLN A 1 2083 ? 84.633  107.720 119.399 1.00 14.22  ? 2083 GLN A C     1 
ATOM   5018  O  O     . GLN A 1 2083 ? 83.421  107.509 119.300 1.00 14.98  ? 2083 GLN A O     1 
ATOM   5019  C  CB    . GLN A 1 2083 ? 85.382  108.732 121.564 1.00 10.51  ? 2083 GLN A CB    1 
ATOM   5020  C  CG    . GLN A 1 2083 ? 85.726  109.974 122.375 1.00 10.45  ? 2083 GLN A CG    1 
ATOM   5021  C  CD    . GLN A 1 2083 ? 87.139  110.471 122.130 1.00 17.41  ? 2083 GLN A CD    1 
ATOM   5022  O  OE1   . GLN A 1 2083 ? 87.910  109.857 121.393 1.00 19.85  ? 2083 GLN A OE1   1 
ATOM   5023  N  NE2   . GLN A 1 2083 ? 87.484  111.594 122.748 1.00 15.14  ? 2083 GLN A NE2   1 
ATOM   5024  N  N     . SER A 1 2084 ? 85.563  106.882 118.938 1.00 15.50  ? 2084 SER A N     1 
ATOM   5025  C  CA    . SER A 1 2084 ? 85.180  105.650 118.257 1.00 15.15  ? 2084 SER A CA    1 
ATOM   5026  C  C     . SER A 1 2084 ? 84.535  104.642 119.199 1.00 15.50  ? 2084 SER A C     1 
ATOM   5027  O  O     . SER A 1 2084 ? 83.783  103.776 118.740 1.00 20.13  ? 2084 SER A O     1 
ATOM   5028  C  CB    . SER A 1 2084 ? 86.400  105.023 117.580 1.00 13.84  ? 2084 SER A CB    1 
ATOM   5029  O  OG    . SER A 1 2084 ? 87.516  105.005 118.453 1.00 26.85  ? 2084 SER A OG    1 
ATOM   5030  N  N     . HIS A 1 2085 ? 84.808  104.734 120.500 1.00 10.46  ? 2085 HIS A N     1 
ATOM   5031  C  CA    . HIS A 1 2085 ? 84.255  103.816 121.485 1.00 11.53  ? 2085 HIS A CA    1 
ATOM   5032  C  C     . HIS A 1 2085 ? 83.023  104.383 122.182 1.00 12.95  ? 2085 HIS A C     1 
ATOM   5033  O  O     . HIS A 1 2085 ? 82.682  103.942 123.285 1.00 15.33  ? 2085 HIS A O     1 
ATOM   5034  C  CB    . HIS A 1 2085 ? 85.324  103.445 122.514 1.00 8.16   ? 2085 HIS A CB    1 
ATOM   5035  C  CG    . HIS A 1 2085 ? 85.768  104.594 123.365 1.00 8.49   ? 2085 HIS A CG    1 
ATOM   5036  N  ND1   . HIS A 1 2085 ? 86.740  105.485 122.964 1.00 8.84   ? 2085 HIS A ND1   1 
ATOM   5037  C  CD2   . HIS A 1 2085 ? 85.379  104.992 124.598 1.00 8.00   ? 2085 HIS A CD2   1 
ATOM   5038  C  CE1   . HIS A 1 2085 ? 86.924  106.387 123.911 1.00 7.39   ? 2085 HIS A CE1   1 
ATOM   5039  N  NE2   . HIS A 1 2085 ? 86.112  106.109 124.914 1.00 6.26   ? 2085 HIS A NE2   1 
ATOM   5040  N  N     . TYR A 1 2086 ? 82.350  105.346 121.561 1.00 12.32  ? 2086 TYR A N     1 
ATOM   5041  C  CA    . TYR A 1 2086 ? 81.157  105.966 122.122 1.00 11.01  ? 2086 TYR A CA    1 
ATOM   5042  C  C     . TYR A 1 2086 ? 79.919  105.406 121.438 1.00 14.42  ? 2086 TYR A C     1 
ATOM   5043  O  O     . TYR A 1 2086 ? 79.855  105.352 120.206 1.00 21.09  ? 2086 TYR A O     1 
ATOM   5044  C  CB    . TYR A 1 2086 ? 81.199  107.486 121.957 1.00 10.82  ? 2086 TYR A CB    1 
ATOM   5045  C  CG    . TYR A 1 2086 ? 81.988  108.217 123.018 1.00 10.57  ? 2086 TYR A CG    1 
ATOM   5046  C  CD1   . TYR A 1 2086 ? 82.933  107.557 123.792 1.00 9.77   ? 2086 TYR A CD1   1 
ATOM   5047  C  CD2   . TYR A 1 2086 ? 81.796  109.574 123.235 1.00 10.44  ? 2086 TYR A CD2   1 
ATOM   5048  C  CE1   . TYR A 1 2086 ? 83.656  108.228 124.758 1.00 8.30   ? 2086 TYR A CE1   1 
ATOM   5049  C  CE2   . TYR A 1 2086 ? 82.515  110.252 124.197 1.00 10.76  ? 2086 TYR A CE2   1 
ATOM   5050  C  CZ    . TYR A 1 2086 ? 83.443  109.576 124.956 1.00 10.48  ? 2086 TYR A CZ    1 
ATOM   5051  O  OH    . TYR A 1 2086 ? 84.161  110.252 125.913 1.00 11.58  ? 2086 TYR A OH    1 
ATOM   5052  N  N     . ASP A 1 2087 ? 78.942  104.989 122.239 1.00 13.33  ? 2087 ASP A N     1 
ATOM   5053  C  CA    . ASP A 1 2087 ? 77.652  104.547 121.725 1.00 13.52  ? 2087 ASP A CA    1 
ATOM   5054  C  C     . ASP A 1 2087 ? 76.564  105.010 122.678 1.00 11.79  ? 2087 ASP A C     1 
ATOM   5055  O  O     . ASP A 1 2087 ? 76.626  104.727 123.878 1.00 11.31  ? 2087 ASP A O     1 
ATOM   5056  C  CB    . ASP A 1 2087 ? 77.603  103.026 121.556 1.00 18.26  ? 2087 ASP A CB    1 
ATOM   5057  C  CG    . ASP A 1 2087 ? 76.316  102.558 120.906 1.00 23.12  ? 2087 ASP A CG    1 
ATOM   5058  O  OD1   . ASP A 1 2087 ? 76.165  102.746 119.681 1.00 19.54  ? 2087 ASP A OD1   1 
ATOM   5059  O  OD2   . ASP A 1 2087 ? 75.453  102.008 121.623 1.00 22.08  ? 2087 ASP A OD2   1 
ATOM   5060  N  N     . PHE A 1 2088 ? 75.575  105.717 122.143 1.00 11.83  ? 2088 PHE A N     1 
ATOM   5061  C  CA    . PHE A 1 2088 ? 74.412  106.166 122.896 1.00 10.45  ? 2088 PHE A CA    1 
ATOM   5062  C  C     . PHE A 1 2088 ? 73.137  105.751 122.182 1.00 11.21  ? 2088 PHE A C     1 
ATOM   5063  O  O     . PHE A 1 2088 ? 72.156  106.497 122.129 1.00 17.98  ? 2088 PHE A O     1 
ATOM   5064  C  CB    . PHE A 1 2088 ? 74.451  107.677 123.116 1.00 10.64  ? 2088 PHE A CB    1 
ATOM   5065  C  CG    . PHE A 1 2088 ? 75.753  108.173 123.676 1.00 14.29  ? 2088 PHE A CG    1 
ATOM   5066  C  CD1   . PHE A 1 2088 ? 75.961  108.217 125.045 1.00 13.31  ? 2088 PHE A CD1   1 
ATOM   5067  C  CD2   . PHE A 1 2088 ? 76.770  108.596 122.836 1.00 15.66  ? 2088 PHE A CD2   1 
ATOM   5068  C  CE1   . PHE A 1 2088 ? 77.159  108.671 125.564 1.00 16.19  ? 2088 PHE A CE1   1 
ATOM   5069  C  CE2   . PHE A 1 2088 ? 77.968  109.052 123.348 1.00 12.94  ? 2088 PHE A CE2   1 
ATOM   5070  C  CZ    . PHE A 1 2088 ? 78.163  109.090 124.714 1.00 12.45  ? 2088 PHE A CZ    1 
ATOM   5071  N  N     . GLY A 1 2089 ? 73.140  104.546 121.621 1.00 9.84   ? 2089 GLY A N     1 
ATOM   5072  C  CA    . GLY A 1 2089 ? 72.030  104.044 120.842 1.00 7.63   ? 2089 GLY A CA    1 
ATOM   5073  C  C     . GLY A 1 2089 ? 71.012  103.297 121.676 1.00 8.78   ? 2089 GLY A C     1 
ATOM   5074  O  O     . GLY A 1 2089 ? 70.916  103.465 122.894 1.00 10.37  ? 2089 GLY A O     1 
ATOM   5075  N  N     . LEU A 1 2090 ? 70.235  102.453 120.994 1.00 8.84   ? 2090 LEU A N     1 
ATOM   5076  C  CA    . LEU A 1 2090 ? 69.149  101.742 121.660 1.00 7.49   ? 2090 LEU A CA    1 
ATOM   5077  C  C     . LEU A 1 2090 ? 69.675  100.689 122.629 1.00 7.44   ? 2090 LEU A C     1 
ATOM   5078  O  O     . LEU A 1 2090 ? 69.074  100.457 123.682 1.00 7.12   ? 2090 LEU A O     1 
ATOM   5079  C  CB    . LEU A 1 2090 ? 68.224  101.110 120.620 1.00 6.52   ? 2090 LEU A CB    1 
ATOM   5080  C  CG    . LEU A 1 2090 ? 67.000  100.364 121.152 1.00 8.68   ? 2090 LEU A CG    1 
ATOM   5081  C  CD1   . LEU A 1 2090 ? 66.258  101.211 122.170 1.00 5.75   ? 2090 LEU A CD1   1 
ATOM   5082  C  CD2   . LEU A 1 2090 ? 66.079  99.984  120.006 1.00 6.81   ? 2090 LEU A CD2   1 
ATOM   5083  N  N     . ARG A 1 2091 ? 70.788  100.033 122.289 1.00 8.45   ? 2091 ARG A N     1 
ATOM   5084  C  CA    . ARG A 1 2091 ? 71.371  99.055  123.205 1.00 6.71   ? 2091 ARG A CA    1 
ATOM   5085  C  C     . ARG A 1 2091 ? 71.802  99.714  124.509 1.00 6.10   ? 2091 ARG A C     1 
ATOM   5086  O  O     . ARG A 1 2091 ? 71.575  99.174  125.597 1.00 6.07   ? 2091 ARG A O     1 
ATOM   5087  C  CB    . ARG A 1 2091 ? 72.559  98.350  122.551 1.00 8.35   ? 2091 ARG A CB    1 
ATOM   5088  C  CG    . ARG A 1 2091 ? 72.227  97.529  121.323 1.00 10.99  ? 2091 ARG A CG    1 
ATOM   5089  C  CD    . ARG A 1 2091 ? 73.482  96.849  120.790 1.00 11.05  ? 2091 ARG A CD    1 
ATOM   5090  N  NE    . ARG A 1 2091 ? 73.248  96.106  119.558 1.00 12.68  ? 2091 ARG A NE    1 
ATOM   5091  C  CZ    . ARG A 1 2091 ? 72.474  95.034  119.455 1.00 11.17  ? 2091 ARG A CZ    1 
ATOM   5092  N  NH1   . ARG A 1 2091 ? 71.898  94.490  120.515 1.00 10.07  ? 2091 ARG A NH1   1 
ATOM   5093  N  NH2   . ARG A 1 2091 ? 72.287  94.484  118.260 1.00 5.21   ? 2091 ARG A NH2   1 
ATOM   5094  N  N     . ALA A 1 2092 ? 72.434  100.885 124.413 1.00 6.04   ? 2092 ALA A N     1 
ATOM   5095  C  CA    . ALA A 1 2092 ? 72.887  101.587 125.609 1.00 6.10   ? 2092 ALA A CA    1 
ATOM   5096  C  C     . ALA A 1 2092 ? 71.710  101.981 126.493 1.00 5.76   ? 2092 ALA A C     1 
ATOM   5097  O  O     . ALA A 1 2092 ? 71.744  101.793 127.715 1.00 7.10   ? 2092 ALA A O     1 
ATOM   5098  C  CB    . ALA A 1 2092 ? 73.702  102.815 125.208 1.00 7.80   ? 2092 ALA A CB    1 
ATOM   5099  N  N     . LEU A 1 2093 ? 70.652  102.523 125.886 1.00 5.79   ? 2093 LEU A N     1 
ATOM   5100  C  CA    . LEU A 1 2093 ? 69.477  102.919 126.655 1.00 6.52   ? 2093 LEU A CA    1 
ATOM   5101  C  C     . LEU A 1 2093 ? 68.798  101.706 127.281 1.00 5.78   ? 2093 LEU A C     1 
ATOM   5102  O  O     . LEU A 1 2093 ? 68.352  101.757 128.431 1.00 6.75   ? 2093 LEU A O     1 
ATOM   5103  C  CB    . LEU A 1 2093 ? 68.506  103.695 125.763 1.00 6.33   ? 2093 LEU A CB    1 
ATOM   5104  C  CG    . LEU A 1 2093 ? 67.123  104.011 126.333 1.00 7.32   ? 2093 LEU A CG    1 
ATOM   5105  C  CD1   . LEU A 1 2093 ? 67.237  104.910 127.554 1.00 7.36   ? 2093 LEU A CD1   1 
ATOM   5106  C  CD2   . LEU A 1 2093 ? 66.259  104.667 125.274 1.00 5.85   ? 2093 LEU A CD2   1 
ATOM   5107  N  N     . LYS A 1 2094 ? 68.713  100.602 126.534 1.00 4.84   ? 2094 LYS A N     1 
ATOM   5108  C  CA    . LYS A 1 2094 ? 68.138  99.371  127.069 1.00 5.38   ? 2094 LYS A CA    1 
ATOM   5109  C  C     . LYS A 1 2094 ? 68.925  98.881  128.278 1.00 6.26   ? 2094 LYS A C     1 
ATOM   5110  O  O     . LYS A 1 2094 ? 68.345  98.483  129.299 1.00 7.07   ? 2094 LYS A O     1 
ATOM   5111  C  CB    . LYS A 1 2094 ? 68.111  98.300  125.978 1.00 7.45   ? 2094 LYS A CB    1 
ATOM   5112  C  CG    . LYS A 1 2094 ? 67.299  97.061  126.316 1.00 7.00   ? 2094 LYS A CG    1 
ATOM   5113  C  CD    . LYS A 1 2094 ? 65.810  97.325  126.210 1.00 8.26   ? 2094 LYS A CD    1 
ATOM   5114  C  CE    . LYS A 1 2094 ? 65.007  96.058  126.456 1.00 9.32   ? 2094 LYS A CE    1 
ATOM   5115  N  NZ    . LYS A 1 2094 ? 65.325  94.981  125.486 1.00 12.55  ? 2094 LYS A NZ    1 
ATOM   5116  N  N     . SER A 1 2095 ? 70.256  98.896  128.173 1.00 5.90   ? 2095 SER A N     1 
ATOM   5117  C  CA    . SER A 1 2095 ? 71.100  98.481  129.288 1.00 6.29   ? 2095 SER A CA    1 
ATOM   5118  C  C     . SER A 1 2095 ? 70.892  99.386  130.494 1.00 8.31   ? 2095 SER A C     1 
ATOM   5119  O  O     . SER A 1 2095 ? 70.795  98.912  131.632 1.00 11.54  ? 2095 SER A O     1 
ATOM   5120  C  CB    . SER A 1 2095 ? 72.567  98.479  128.857 1.00 8.93   ? 2095 SER A CB    1 
ATOM   5121  O  OG    . SER A 1 2095 ? 73.420  98.170  129.945 1.00 25.13  ? 2095 SER A OG    1 
ATOM   5122  N  N     . VAL A 1 2096 ? 70.809  100.698 130.259 1.00 5.69   ? 2096 VAL A N     1 
ATOM   5123  C  CA    . VAL A 1 2096 ? 70.594  101.638 131.356 1.00 6.82   ? 2096 VAL A CA    1 
ATOM   5124  C  C     . VAL A 1 2096 ? 69.251  101.381 132.028 1.00 7.10   ? 2096 VAL A C     1 
ATOM   5125  O  O     . VAL A 1 2096 ? 69.137  101.437 133.255 1.00 8.31   ? 2096 VAL A O     1 
ATOM   5126  C  CB    . VAL A 1 2096 ? 70.709  103.088 130.850 1.00 8.49   ? 2096 VAL A CB    1 
ATOM   5127  C  CG1   . VAL A 1 2096 ? 70.258  104.061 131.922 1.00 6.00   ? 2096 VAL A CG1   1 
ATOM   5128  C  CG2   . VAL A 1 2096 ? 72.141  103.388 130.440 1.00 8.22   ? 2096 VAL A CG2   1 
ATOM   5129  N  N     . LEU A 1 2097 ? 68.216  101.087 131.240 1.00 5.98   ? 2097 LEU A N     1 
ATOM   5130  C  CA    . LEU A 1 2097 ? 66.888  100.867 131.808 1.00 5.74   ? 2097 LEU A CA    1 
ATOM   5131  C  C     . LEU A 1 2097 ? 66.837  99.579  132.626 1.00 10.33  ? 2097 LEU A C     1 
ATOM   5132  O  O     . LEU A 1 2097 ? 66.257  99.549  133.723 1.00 14.49  ? 2097 LEU A O     1 
ATOM   5133  C  CB    . LEU A 1 2097 ? 65.853  100.844 130.685 1.00 7.04   ? 2097 LEU A CB    1 
ATOM   5134  C  CG    . LEU A 1 2097 ? 65.720  102.180 129.948 1.00 8.33   ? 2097 LEU A CG    1 
ATOM   5135  C  CD1   . LEU A 1 2097 ? 64.847  102.045 128.708 1.00 5.62   ? 2097 LEU A CD1   1 
ATOM   5136  C  CD2   . LEU A 1 2097 ? 65.217  103.285 130.868 1.00 6.04   ? 2097 LEU A CD2   1 
ATOM   5137  N  N     . VAL A 1 2098 ? 67.441  98.504  132.112 1.00 8.44   ? 2098 VAL A N     1 
ATOM   5138  C  CA    . VAL A 1 2098 ? 67.489  97.253  132.865 1.00 10.72  ? 2098 VAL A CA    1 
ATOM   5139  C  C     . VAL A 1 2098 ? 68.286  97.439  134.151 1.00 11.63  ? 2098 VAL A C     1 
ATOM   5140  O  O     . VAL A 1 2098 ? 67.896  96.952  135.224 1.00 13.02  ? 2098 VAL A O     1 
ATOM   5141  C  CB    . VAL A 1 2098 ? 68.069  96.126  131.988 1.00 14.76  ? 2098 VAL A CB    1 
ATOM   5142  C  CG1   . VAL A 1 2098 ? 68.405  94.906  132.832 1.00 11.67  ? 2098 VAL A CG1   1 
ATOM   5143  C  CG2   . VAL A 1 2098 ? 67.093  95.763  130.881 1.00 12.27  ? 2098 VAL A CG2   1 
ATOM   5144  N  N     . SER A 1 2099 ? 69.409  98.158  134.068 1.00 10.69  ? 2099 SER A N     1 
ATOM   5145  C  CA    . SER A 1 2099 ? 70.190  98.455  135.261 1.00 8.98   ? 2099 SER A CA    1 
ATOM   5146  C  C     . SER A 1 2099 ? 69.391  99.295  136.247 1.00 11.23  ? 2099 SER A C     1 
ATOM   5147  O  O     . SER A 1 2099 ? 69.525  99.128  137.461 1.00 13.01  ? 2099 SER A O     1 
ATOM   5148  C  CB    . SER A 1 2099 ? 71.487  99.164  134.873 1.00 11.02  ? 2099 SER A CB    1 
ATOM   5149  O  OG    . SER A 1 2099 ? 72.232  99.531  136.021 1.00 26.89  ? 2099 SER A OG    1 
ATOM   5150  N  N     . ALA A 1 2100 ? 68.560  100.211 135.745 1.00 8.89   ? 2100 ALA A N     1 
ATOM   5151  C  CA    . ALA A 1 2100 ? 67.713  101.011 136.622 1.00 11.15  ? 2100 ALA A CA    1 
ATOM   5152  C  C     . ALA A 1 2100 ? 66.725  100.131 137.371 1.00 14.67  ? 2100 ALA A C     1 
ATOM   5153  O  O     . ALA A 1 2100 ? 66.490  100.320 138.570 1.00 15.24  ? 2100 ALA A O     1 
ATOM   5154  C  CB    . ALA A 1 2100 ? 66.981  102.083 135.814 1.00 11.55  ? 2100 ALA A CB    1 
ATOM   5155  N  N     . GLY A 1 2101 ? 66.134  99.160  136.676 1.00 13.51  ? 2101 GLY A N     1 
ATOM   5156  C  CA    . GLY A 1 2101 ? 65.266  98.209  137.357 1.00 14.00  ? 2101 GLY A CA    1 
ATOM   5157  C  C     . GLY A 1 2101 ? 65.993  97.428  138.438 1.00 14.62  ? 2101 GLY A C     1 
ATOM   5158  O  O     . GLY A 1 2101 ? 65.496  97.286  139.565 1.00 15.79  ? 2101 GLY A O     1 
ATOM   5159  N  N     . ASN A 1 2102 ? 67.188  96.923  138.116 1.00 14.01  ? 2102 ASN A N     1 
ATOM   5160  C  CA    . ASN A 1 2102 ? 67.965  96.170  139.100 1.00 13.94  ? 2102 ASN A CA    1 
ATOM   5161  C  C     . ASN A 1 2102 ? 68.322  97.037  140.303 1.00 16.53  ? 2102 ASN A C     1 
ATOM   5162  O  O     . ASN A 1 2102 ? 68.246  96.589  141.455 1.00 21.06  ? 2102 ASN A O     1 
ATOM   5163  C  CB    . ASN A 1 2102 ? 69.232  95.601  138.459 1.00 13.30  ? 2102 ASN A CB    1 
ATOM   5164  C  CG    . ASN A 1 2102 ? 68.937  94.622  137.340 1.00 16.83  ? 2102 ASN A CG    1 
ATOM   5165  O  OD1   . ASN A 1 2102 ? 69.356  94.820  136.200 1.00 17.05  ? 2102 ASN A OD1   1 
ATOM   5166  N  ND2   . ASN A 1 2102 ? 68.222  93.553  137.663 1.00 19.69  ? 2102 ASN A ND2   1 
ATOM   5167  N  N     . VAL A 1 2103 ? 68.718  98.287  140.053 1.00 13.98  ? 2103 VAL A N     1 
ATOM   5168  C  CA    . VAL A 1 2103 ? 69.110  99.180  141.138 1.00 14.91  ? 2103 VAL A CA    1 
ATOM   5169  C  C     . VAL A 1 2103 ? 67.905  99.538  141.997 1.00 18.59  ? 2103 VAL A C     1 
ATOM   5170  O  O     . VAL A 1 2103 ? 68.015  99.647  143.221 1.00 23.06  ? 2103 VAL A O     1 
ATOM   5171  C  CB    . VAL A 1 2103 ? 69.817  100.432 140.585 1.00 16.24  ? 2103 VAL A CB    1 
ATOM   5172  C  CG1   . VAL A 1 2103 ? 70.077  101.432 141.699 1.00 17.22  ? 2103 VAL A CG1   1 
ATOM   5173  C  CG2   . VAL A 1 2103 ? 71.133  100.047 139.934 1.00 18.12  ? 2103 VAL A CG2   1 
ATOM   5174  N  N     . LYS A 1 2104 ? 66.735  99.716  141.380 1.00 18.21  ? 2104 LYS A N     1 
ATOM   5175  C  CA    . LYS A 1 2104 ? 65.536  99.979  142.168 1.00 18.55  ? 2104 LYS A CA    1 
ATOM   5176  C  C     . LYS A 1 2104 ? 65.217  98.803  143.082 1.00 19.10  ? 2104 LYS A C     1 
ATOM   5177  O  O     . LYS A 1 2104 ? 64.909  98.987  144.267 1.00 23.38  ? 2104 LYS A O     1 
ATOM   5178  C  CB    . LYS A 1 2104 ? 64.349  100.286 141.255 1.00 18.54  ? 2104 LYS A CB    1 
ATOM   5179  C  CG    . LYS A 1 2104 ? 63.124  100.776 142.014 1.00 18.60  ? 2104 LYS A CG    1 
ATOM   5180  C  CD    . LYS A 1 2104 ? 62.075  101.367 141.091 1.00 18.31  ? 2104 LYS A CD    1 
ATOM   5181  C  CE    . LYS A 1 2104 ? 61.336  100.280 140.332 1.00 22.00  ? 2104 LYS A CE    1 
ATOM   5182  N  NZ    . LYS A 1 2104 ? 60.511  99.437  141.241 1.00 22.05  ? 2104 LYS A NZ    1 
ATOM   5183  N  N     . ARG A 1 2105 ? 65.295  97.579  142.549 1.00 20.33  ? 2105 ARG A N     1 
ATOM   5184  C  CA    . ARG A 1 2105 ? 65.020  96.414  143.388 1.00 18.75  ? 2105 ARG A CA    1 
ATOM   5185  C  C     . ARG A 1 2105 ? 66.029  96.290  144.527 1.00 23.35  ? 2105 ARG A C     1 
ATOM   5186  O  O     . ARG A 1 2105 ? 65.648  96.030  145.677 1.00 28.43  ? 2105 ARG A O     1 
ATOM   5187  C  CB    . ARG A 1 2105 ? 64.988  95.139  142.545 1.00 16.95  ? 2105 ARG A CB    1 
ATOM   5188  C  CG    . ARG A 1 2105 ? 63.728  94.994  141.702 1.00 23.12  ? 2105 ARG A CG    1 
ATOM   5189  C  CD    . ARG A 1 2105 ? 63.654  93.629  141.024 1.00 23.67  ? 2105 ARG A CD    1 
ATOM   5190  N  NE    . ARG A 1 2105 ? 64.549  93.501  139.879 1.00 22.60  ? 2105 ARG A NE    1 
ATOM   5191  C  CZ    . ARG A 1 2105 ? 64.442  94.195  138.753 1.00 24.61  ? 2105 ARG A CZ    1 
ATOM   5192  N  NH1   . ARG A 1 2105 ? 63.461  95.063  138.564 1.00 31.18  ? 2105 ARG A NH1   1 
ATOM   5193  N  NH2   . ARG A 1 2105 ? 65.332  94.000  137.785 1.00 17.81  ? 2105 ARG A NH2   1 
ATOM   5194  N  N     . GLU A 1 2106 ? 67.319  96.491  144.238 1.00 24.48  ? 2106 GLU A N     1 
ATOM   5195  C  CA    . GLU A 1 2106 ? 68.317  96.353  145.295 1.00 29.88  ? 2106 GLU A CA    1 
ATOM   5196  C  C     . GLU A 1 2106 ? 68.190  97.474  146.321 1.00 31.45  ? 2106 GLU A C     1 
ATOM   5197  O  O     . GLU A 1 2106 ? 68.457  97.266  147.508 1.00 38.86  ? 2106 GLU A O     1 
ATOM   5198  C  CB    . GLU A 1 2106 ? 69.732  96.310  144.712 1.00 27.25  ? 2106 GLU A CB    1 
ATOM   5199  C  CG    . GLU A 1 2106 ? 70.190  97.584  144.039 1.00 32.12  ? 2106 GLU A CG    1 
ATOM   5200  C  CD    . GLU A 1 2106 ? 71.570  97.461  143.425 1.00 40.95  ? 2106 GLU A CD    1 
ATOM   5201  O  OE1   . GLU A 1 2106 ? 72.165  96.365  143.507 1.00 39.41  ? 2106 GLU A OE1   1 
ATOM   5202  O  OE2   . GLU A 1 2106 ? 72.063  98.461  142.862 1.00 38.31  ? 2106 GLU A OE2   1 
ATOM   5203  N  N     . ARG A 1 2107 ? 67.767  98.666  145.890 1.00 26.99  ? 2107 ARG A N     1 
ATOM   5204  C  CA    . ARG A 1 2107 ? 67.558  99.760  146.832 1.00 26.18  ? 2107 ARG A CA    1 
ATOM   5205  C  C     . ARG A 1 2107 ? 66.367  99.489  147.741 1.00 32.36  ? 2107 ARG A C     1 
ATOM   5206  O  O     . ARG A 1 2107 ? 66.416  99.791  148.938 1.00 41.75  ? 2107 ARG A O     1 
ATOM   5207  C  CB    . ARG A 1 2107 ? 67.371  101.078 146.082 1.00 25.76  ? 2107 ARG A CB    1 
ATOM   5208  C  CG    . ARG A 1 2107 ? 68.660  101.673 145.543 1.00 24.95  ? 2107 ARG A CG    1 
ATOM   5209  C  CD    . ARG A 1 2107 ? 68.736  103.164 145.821 1.00 28.32  ? 2107 ARG A CD    1 
ATOM   5210  N  NE    . ARG A 1 2107 ? 69.836  103.796 145.104 1.00 32.32  ? 2107 ARG A NE    1 
ATOM   5211  C  CZ    . ARG A 1 2107 ? 69.833  105.056 144.690 1.00 30.22  ? 2107 ARG A CZ    1 
ATOM   5212  N  NH1   . ARG A 1 2107 ? 68.794  105.848 144.896 1.00 31.62  ? 2107 ARG A NH1   1 
ATOM   5213  N  NH2   . ARG A 1 2107 ? 70.897  105.531 144.050 1.00 29.38  ? 2107 ARG A NH2   1 
ATOM   5214  N  N     . ILE A 1 2108 ? 65.287  98.924  147.196 1.00 32.99  ? 2108 ILE A N     1 
ATOM   5215  C  CA    . ILE A 1 2108 ? 64.158  98.545  148.044 1.00 34.07  ? 2108 ILE A CA    1 
ATOM   5216  C  C     . ILE A 1 2108 ? 64.582  97.479  149.047 1.00 40.79  ? 2108 ILE A C     1 
ATOM   5217  O  O     . ILE A 1 2108 ? 64.217  97.533  150.232 1.00 48.05  ? 2108 ILE A O     1 
ATOM   5218  C  CB    . ILE A 1 2108 ? 62.968  98.078  147.184 1.00 36.19  ? 2108 ILE A CB    1 
ATOM   5219  C  CG1   . ILE A 1 2108 ? 62.494  99.210  146.271 1.00 29.51  ? 2108 ILE A CG1   1 
ATOM   5220  C  CG2   . ILE A 1 2108 ? 61.828  97.591  148.066 1.00 38.70  ? 2108 ILE A CG2   1 
ATOM   5221  C  CD1   . ILE A 1 2108 ? 61.337  98.828  145.375 1.00 30.11  ? 2108 ILE A CD1   1 
ATOM   5222  N  N     . GLN A 1 2109 ? 65.364  96.495  148.592 1.00 43.43  ? 2109 GLN A N     1 
ATOM   5223  C  CA    . GLN A 1 2109 ? 65.853  95.464  149.502 1.00 44.98  ? 2109 GLN A CA    1 
ATOM   5224  C  C     . GLN A 1 2109 ? 66.742  96.059  150.590 1.00 50.12  ? 2109 GLN A C     1 
ATOM   5225  O  O     . GLN A 1 2109 ? 66.650  95.668  151.758 1.00 54.61  ? 2109 GLN A O     1 
ATOM   5226  C  CB    . GLN A 1 2109 ? 66.602  94.384  148.722 1.00 42.20  ? 2109 GLN A CB    1 
ATOM   5227  C  CG    . GLN A 1 2109 ? 65.707  93.537  147.834 1.00 48.00  ? 2109 GLN A CG    1 
ATOM   5228  C  CD    . GLN A 1 2109 ? 64.557  92.910  148.599 1.00 59.08  ? 2109 GLN A CD    1 
ATOM   5229  O  OE1   . GLN A 1 2109 ? 63.388  93.169  148.310 1.00 62.25  ? 2109 GLN A OE1   1 
ATOM   5230  N  NE2   . GLN A 1 2109 ? 64.883  92.080  149.583 1.00 59.58  ? 2109 GLN A NE2   1 
ATOM   5231  N  N     . LYS A 1 2110 ? 67.606  97.009  150.226 1.00 46.48  ? 2110 LYS A N     1 
ATOM   5232  C  CA    . LYS A 1 2110 ? 68.457  97.663  151.215 1.00 47.84  ? 2110 LYS A CA    1 
ATOM   5233  C  C     . LYS A 1 2110 ? 67.631  98.459  152.218 1.00 49.65  ? 2110 LYS A C     1 
ATOM   5234  O  O     . LYS A 1 2110 ? 67.925  98.454  153.419 1.00 60.03  ? 2110 LYS A O     1 
ATOM   5235  C  CB    . LYS A 1 2110 ? 69.469  98.568  150.513 1.00 49.66  ? 2110 LYS A CB    1 
ATOM   5236  C  CG    . LYS A 1 2110 ? 70.349  99.375  151.452 1.00 54.98  ? 2110 LYS A CG    1 
ATOM   5237  C  CD    . LYS A 1 2110 ? 70.829  100.655 150.787 1.00 58.81  ? 2110 LYS A CD    1 
ATOM   5238  C  CE    . LYS A 1 2110 ? 72.165  101.106 151.352 1.00 60.10  ? 2110 LYS A CE    1 
ATOM   5239  N  NZ    . LYS A 1 2110 ? 72.050  101.538 152.772 1.00 67.53  ? 2110 LYS A NZ    1 
ATOM   5240  N  N     . ILE A 1 2111 ? 66.597  99.156  151.742 1.00 46.24  ? 2111 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 2111 ? 65.752  99.941  152.637 1.00 47.06  ? 2111 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 2111 ? 65.050  99.035  153.638 1.00 54.35  ? 2111 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 2111 ? 65.018  99.323  154.841 1.00 61.05  ? 2111 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 2111 ? 64.745  100.781 151.828 1.00 44.33  ? 2111 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 2111 ? 65.461  101.922 151.103 1.00 40.31  ? 2111 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 2111 ? 63.657  101.330 152.734 1.00 43.17  ? 2111 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 2111 ? 64.560  102.722 150.189 1.00 38.86  ? 2111 ILE A CD1   1 
ATOM   5248  N  N     . LYS A 1 2112 ? 64.492  97.916  153.169 1.00 57.06  ? 2112 LYS A N     1 
ATOM   5249  C  CA    . LYS A 1 2112 ? 63.824  97.023  154.113 1.00 56.26  ? 2112 LYS A CA    1 
ATOM   5250  C  C     . LYS A 1 2112 ? 64.823  96.321  155.027 1.00 62.89  ? 2112 LYS A C     1 
ATOM   5251  O  O     . LYS A 1 2112 ? 64.497  96.030  156.183 1.00 69.19  ? 2112 LYS A O     1 
ATOM   5252  C  CB    . LYS A 1 2112 ? 62.944  96.008  153.381 1.00 55.49  ? 2112 LYS A CB    1 
ATOM   5253  C  CG    . LYS A 1 2112 ? 63.647  95.134  152.370 1.00 61.49  ? 2112 LYS A CG    1 
ATOM   5254  C  CD    . LYS A 1 2112 ? 62.645  94.241  151.657 1.00 64.17  ? 2112 LYS A CD    1 
ATOM   5255  C  CE    . LYS A 1 2112 ? 61.549  95.066  150.999 1.00 61.66  ? 2112 LYS A CE    1 
ATOM   5256  N  NZ    . LYS A 1 2112 ? 60.583  94.217  150.250 1.00 62.18  ? 2112 LYS A NZ    1 
ATOM   5257  N  N     . ARG A 1 2113 ? 66.046  96.065  154.551 1.00 62.17  ? 2113 ARG A N     1 
ATOM   5258  C  CA    . ARG A 1 2113 ? 67.073  95.513  155.431 1.00 63.19  ? 2113 ARG A CA    1 
ATOM   5259  C  C     . ARG A 1 2113 ? 67.417  96.484  156.553 1.00 67.02  ? 2113 ARG A C     1 
ATOM   5260  O  O     . ARG A 1 2113 ? 67.560  96.077  157.712 1.00 70.72  ? 2113 ARG A O     1 
ATOM   5261  C  CB    . ARG A 1 2113 ? 68.327  95.164  154.629 1.00 59.38  ? 2113 ARG A CB    1 
ATOM   5262  C  CG    . ARG A 1 2113 ? 68.405  93.714  154.185 1.00 59.79  ? 2113 ARG A CG    1 
ATOM   5263  C  CD    . ARG A 1 2113 ? 69.607  93.484  153.283 1.00 59.85  ? 2113 ARG A CD    1 
ATOM   5264  N  NE    . ARG A 1 2113 ? 69.464  94.146  151.993 1.00 61.23  ? 2113 ARG A NE    1 
ATOM   5265  C  CZ    . ARG A 1 2113 ? 70.373  94.109  151.028 1.00 61.92  ? 2113 ARG A CZ    1 
ATOM   5266  N  NH1   . ARG A 1 2113 ? 71.509  93.446  151.173 1.00 67.10  ? 2113 ARG A NH1   1 
ATOM   5267  N  NH2   . ARG A 1 2113 ? 70.137  94.754  149.889 1.00 55.67  ? 2113 ARG A NH2   1 
ATOM   5268  N  N     . GLU A 1 2114 ? 67.560  97.771  156.227 1.00 66.99  ? 2114 GLU A N     1 
ATOM   5269  C  CA    . GLU A 1 2114 ? 67.791  98.773  157.264 1.00 68.37  ? 2114 GLU A CA    1 
ATOM   5270  C  C     . GLU A 1 2114 ? 66.596  98.877  158.202 1.00 72.76  ? 2114 GLU A C     1 
ATOM   5271  O  O     . GLU A 1 2114 ? 66.760  99.106  159.407 1.00 78.42  ? 2114 GLU A O     1 
ATOM   5272  C  CB    . GLU A 1 2114 ? 68.097  100.134 156.635 1.00 66.04  ? 2114 GLU A CB    1 
ATOM   5273  C  CG    . GLU A 1 2114 ? 69.273  100.138 155.673 1.00 68.45  ? 2114 GLU A CG    1 
ATOM   5274  C  CD    . GLU A 1 2114 ? 70.440  99.308  156.171 1.00 74.09  ? 2114 GLU A CD    1 
ATOM   5275  O  OE1   . GLU A 1 2114 ? 70.980  99.627  157.252 1.00 79.12  ? 2114 GLU A OE1   1 
ATOM   5276  O  OE2   . GLU A 1 2114 ? 70.819  98.339  155.481 1.00 71.76  ? 2114 GLU A OE2   1 
ATOM   5277  N  N     . LYS A 1 2115 ? 65.384  98.716  157.667 1.00 68.18  ? 2115 LYS A N     1 
ATOM   5278  C  CA    . LYS A 1 2115 ? 64.194  98.769  158.511 1.00 70.16  ? 2115 LYS A CA    1 
ATOM   5279  C  C     . LYS A 1 2115 ? 64.115  97.580  159.461 1.00 77.45  ? 2115 LYS A C     1 
ATOM   5280  O  O     . LYS A 1 2115 ? 63.554  97.704  160.554 1.00 84.31  ? 2115 LYS A O     1 
ATOM   5281  C  CB    . LYS A 1 2115 ? 62.937  98.844  157.645 1.00 69.35  ? 2115 LYS A CB    1 
ATOM   5282  C  CG    . LYS A 1 2115 ? 62.649  100.232 157.097 1.00 67.77  ? 2115 LYS A CG    1 
ATOM   5283  C  CD    . LYS A 1 2115 ? 61.215  100.345 156.609 1.00 66.48  ? 2115 LYS A CD    1 
ATOM   5284  C  CE    . LYS A 1 2115 ? 60.833  101.791 156.345 1.00 58.33  ? 2115 LYS A CE    1 
ATOM   5285  N  NZ    . LYS A 1 2115 ? 61.569  102.360 155.184 1.00 61.68  ? 2115 LYS A NZ    1 
ATOM   5286  N  N     . GLU A 1 2116 ? 64.653  96.423  159.062 1.00 75.21  ? 2116 GLU A N     1 
ATOM   5287  C  CA    . GLU A 1 2116 ? 64.660  95.271  159.963 1.00 79.25  ? 2116 GLU A CA    1 
ATOM   5288  C  C     . GLU A 1 2116 ? 65.438  95.566  161.239 1.00 85.87  ? 2116 GLU A C     1 
ATOM   5289  O  O     . GLU A 1 2116 ? 64.998  95.209  162.339 1.00 90.05  ? 2116 GLU A O     1 
ATOM   5290  C  CB    . GLU A 1 2116 ? 65.241  94.039  159.266 1.00 80.21  ? 2116 GLU A CB    1 
ATOM   5291  C  CG    . GLU A 1 2116 ? 64.503  93.598  158.017 1.00 83.05  ? 2116 GLU A CG    1 
ATOM   5292  C  CD    . GLU A 1 2116 ? 62.997  93.654  158.180 1.00 87.43  ? 2116 GLU A CD    1 
ATOM   5293  O  OE1   . GLU A 1 2116 ? 62.470  92.985  159.094 1.00 82.48  ? 2116 GLU A OE1   1 
ATOM   5294  O  OE2   . GLU A 1 2116 ? 62.340  94.365  157.392 1.00 84.74  ? 2116 GLU A OE2   1 
ATOM   5295  N  N     . GLU A 1 2117 ? 66.594  96.213  161.118 1.00 84.33  ? 2117 GLU A N     1 
ATOM   5296  C  CA    . GLU A 1 2117 ? 67.413  96.547  162.274 1.00 82.85  ? 2117 GLU A CA    1 
ATOM   5297  C  C     . GLU A 1 2117 ? 67.019  97.870  162.922 1.00 82.51  ? 2117 GLU A C     1 
ATOM   5298  O  O     . GLU A 1 2117 ? 67.615  98.247  163.937 1.00 84.67  ? 2117 GLU A O     1 
ATOM   5299  C  CB    . GLU A 1 2117 ? 68.897  96.564  161.880 1.00 82.14  ? 2117 GLU A CB    1 
ATOM   5300  C  CG    . GLU A 1 2117 ? 69.264  97.537  160.768 1.00 86.17  ? 2117 GLU A CG    1 
ATOM   5301  C  CD    . GLU A 1 2117 ? 69.624  98.917  161.280 1.00 90.52  ? 2117 GLU A CD    1 
ATOM   5302  O  OE1   . GLU A 1 2117 ? 69.955  99.042  162.478 1.00 93.98  ? 2117 GLU A OE1   1 
ATOM   5303  O  OE2   . GLU A 1 2117 ? 69.586  99.876  160.481 1.00 86.19  ? 2117 GLU A OE2   1 
ATOM   5304  N  N     . ARG A 1 2118 ? 66.033  98.576  162.368 1.00 84.34  ? 2118 ARG A N     1 
ATOM   5305  C  CA    . ARG A 1 2118 ? 65.478  99.794  162.963 1.00 85.22  ? 2118 ARG A CA    1 
ATOM   5306  C  C     . ARG A 1 2118 ? 63.958  99.650  162.977 1.00 87.44  ? 2118 ARG A C     1 
ATOM   5307  O  O     . ARG A 1 2118 ? 63.277  100.086 162.045 1.00 88.86  ? 2118 ARG A O     1 
ATOM   5308  C  CB    . ARG A 1 2118 ? 65.920  101.040 162.199 1.00 85.42  ? 2118 ARG A CB    1 
ATOM   5309  C  CG    . ARG A 1 2118 ? 67.401  101.357 162.312 1.00 88.41  ? 2118 ARG A CG    1 
ATOM   5310  C  CD    . ARG A 1 2118 ? 67.836  101.502 163.762 1.00 94.12  ? 2118 ARG A CD    1 
ATOM   5311  N  NE    . ARG A 1 2118 ? 66.984  102.428 164.499 1.00 96.68  ? 2118 ARG A NE    1 
ATOM   5312  C  CZ    . ARG A 1 2118 ? 66.294  102.109 165.586 1.00 98.48  ? 2118 ARG A CZ    1 
ATOM   5313  N  NH1   . ARG A 1 2118 ? 66.332  100.889 166.096 1.00 95.81  ? 2118 ARG A NH1   1 
ATOM   5314  N  NH2   . ARG A 1 2118 ? 65.547  103.038 166.175 1.00 95.65  ? 2118 ARG A NH2   1 
ATOM   5315  N  N     . GLY A 1 2119 ? 63.430  99.045  164.037 1.00 88.04  ? 2119 GLY A N     1 
ATOM   5316  C  CA    . GLY A 1 2119 ? 61.999  98.839  164.144 1.00 90.45  ? 2119 GLY A CA    1 
ATOM   5317  C  C     . GLY A 1 2119 ? 61.505  97.721  163.242 1.00 90.26  ? 2119 GLY A C     1 
ATOM   5318  O  O     . GLY A 1 2119 ? 62.258  96.839  162.815 1.00 90.06  ? 2119 GLY A O     1 
ATOM   5319  N  N     . GLU A 1 2120 ? 60.198  97.758  162.963 1.00 88.78  ? 2120 GLU A N     1 
ATOM   5320  C  CA    . GLU A 1 2120 ? 59.585  96.777  162.075 1.00 95.77  ? 2120 GLU A CA    1 
ATOM   5321  C  C     . GLU A 1 2120 ? 58.560  97.391  161.128 1.00 91.30  ? 2120 GLU A C     1 
ATOM   5322  O  O     . GLU A 1 2120 ? 57.873  96.643  160.419 1.00 82.49  ? 2120 GLU A O     1 
ATOM   5323  C  CB    . GLU A 1 2120 ? 58.920  95.650  162.879 1.00 101.85 ? 2120 GLU A CB    1 
ATOM   5324  C  CG    . GLU A 1 2120 ? 59.883  94.784  163.675 1.00 98.95  ? 2120 GLU A CG    1 
ATOM   5325  C  CD    . GLU A 1 2120 ? 59.180  93.668  164.421 1.00 102.82 ? 2120 GLU A CD    1 
ATOM   5326  O  OE1   . GLU A 1 2120 ? 58.529  92.829  163.763 1.00 106.89 ? 2120 GLU A OE1   1 
ATOM   5327  O  OE2   . GLU A 1 2120 ? 59.277  93.629  165.666 1.00 102.48 ? 2120 GLU A OE2   1 
ATOM   5328  N  N     . ALA A 1 2121 ? 58.431  98.717  161.087 1.00 88.41  ? 2121 ALA A N     1 
ATOM   5329  C  CA    . ALA A 1 2121 ? 57.428  99.377  160.249 1.00 83.25  ? 2121 ALA A CA    1 
ATOM   5330  C  C     . ALA A 1 2121 ? 57.891  99.334  158.795 1.00 81.85  ? 2121 ALA A C     1 
ATOM   5331  O  O     . ALA A 1 2121 ? 58.437  100.294 158.248 1.00 82.05  ? 2121 ALA A O     1 
ATOM   5332  C  CB    . ALA A 1 2121 ? 57.193  100.807 160.719 1.00 76.97  ? 2121 ALA A CB    1 
ATOM   5333  N  N     . VAL A 1 2122 ? 57.659  98.191  158.159 1.00 81.49  ? 2122 VAL A N     1 
ATOM   5334  C  CA    . VAL A 1 2122 ? 58.061  97.967  156.771 1.00 77.77  ? 2122 VAL A CA    1 
ATOM   5335  C  C     . VAL A 1 2122 ? 56.781  97.958  155.942 1.00 76.00  ? 2122 VAL A C     1 
ATOM   5336  O  O     . VAL A 1 2122 ? 56.066  96.957  155.867 1.00 77.73  ? 2122 VAL A O     1 
ATOM   5337  C  CB    . VAL A 1 2122 ? 58.862  96.677  156.609 1.00 72.24  ? 2122 VAL A CB    1 
ATOM   5338  C  CG1   . VAL A 1 2122 ? 59.409  96.568  155.194 1.00 65.01  ? 2122 VAL A CG1   1 
ATOM   5339  C  CG2   . VAL A 1 2122 ? 59.987  96.622  157.630 1.00 77.44  ? 2122 VAL A CG2   1 
ATOM   5340  N  N     . ASP A 1 2123 ? 56.488  99.091  155.309 1.00 71.76  ? 2123 ASP A N     1 
ATOM   5341  C  CA    . ASP A 1 2123 ? 55.344  99.228  154.413 1.00 75.43  ? 2123 ASP A CA    1 
ATOM   5342  C  C     . ASP A 1 2123 ? 55.878  99.451  153.003 1.00 76.10  ? 2123 ASP A C     1 
ATOM   5343  O  O     . ASP A 1 2123 ? 56.555  100.451 152.741 1.00 72.93  ? 2123 ASP A O     1 
ATOM   5344  C  CB    . ASP A 1 2123 ? 54.437  100.376 154.852 1.00 71.21  ? 2123 ASP A CB    1 
ATOM   5345  C  CG    . ASP A 1 2123 ? 53.342  100.671 153.845 1.00 77.07  ? 2123 ASP A CG    1 
ATOM   5346  O  OD1   . ASP A 1 2123 ? 52.557  99.752  153.532 1.00 76.49  ? 2123 ASP A OD1   1 
ATOM   5347  O  OD2   . ASP A 1 2123 ? 53.263  101.823 153.370 1.00 78.37  ? 2123 ASP A OD2   1 
ATOM   5348  N  N     . GLU A 1 2124 ? 55.576  98.514  152.099 1.00 73.91  ? 2124 GLU A N     1 
ATOM   5349  C  CA    . GLU A 1 2124 ? 56.077  98.617  150.732 1.00 66.29  ? 2124 GLU A CA    1 
ATOM   5350  C  C     . GLU A 1 2124 ? 55.503  99.830  150.011 1.00 67.36  ? 2124 GLU A C     1 
ATOM   5351  O  O     . GLU A 1 2124 ? 56.180  100.426 149.166 1.00 68.29  ? 2124 GLU A O     1 
ATOM   5352  C  CB    . GLU A 1 2124 ? 55.771  97.334  149.953 1.00 65.92  ? 2124 GLU A CB    1 
ATOM   5353  C  CG    . GLU A 1 2124 ? 54.292  96.971  149.846 1.00 71.12  ? 2124 GLU A CG    1 
ATOM   5354  C  CD    . GLU A 1 2124 ? 53.738  96.332  151.108 1.00 75.64  ? 2124 GLU A CD    1 
ATOM   5355  O  OE1   . GLU A 1 2124 ? 54.510  96.140  152.072 1.00 78.46  ? 2124 GLU A OE1   1 
ATOM   5356  O  OE2   . GLU A 1 2124 ? 52.529  96.020  151.135 1.00 69.56  ? 2124 GLU A OE2   1 
ATOM   5357  N  N     . GLY A 1 2125 ? 54.262  100.209 150.326 1.00 68.62  ? 2125 GLY A N     1 
ATOM   5358  C  CA    . GLY A 1 2125 ? 53.696  101.408 149.730 1.00 68.34  ? 2125 GLY A CA    1 
ATOM   5359  C  C     . GLY A 1 2125 ? 54.450  102.664 150.122 1.00 69.86  ? 2125 GLY A C     1 
ATOM   5360  O  O     . GLY A 1 2125 ? 54.709  103.532 149.284 1.00 65.71  ? 2125 GLY A O     1 
ATOM   5361  N  N     . GLU A 1 2126 ? 54.816  102.777 151.401 1.00 75.27  ? 2126 GLU A N     1 
ATOM   5362  C  CA    . GLU A 1 2126 ? 55.600  103.923 151.853 1.00 72.04  ? 2126 GLU A CA    1 
ATOM   5363  C  C     . GLU A 1 2126 ? 56.970  103.950 151.186 1.00 67.21  ? 2126 GLU A C     1 
ATOM   5364  O  O     . GLU A 1 2126 ? 57.474  105.023 150.833 1.00 64.17  ? 2126 GLU A O     1 
ATOM   5365  C  CB    . GLU A 1 2126 ? 55.743  103.894 153.374 1.00 72.10  ? 2126 GLU A CB    1 
ATOM   5366  C  CG    . GLU A 1 2126 ? 56.536  105.054 153.951 1.00 81.88  ? 2126 GLU A CG    1 
ATOM   5367  C  CD    . GLU A 1 2126 ? 56.699  104.955 155.454 1.00 91.04  ? 2126 GLU A CD    1 
ATOM   5368  O  OE1   . GLU A 1 2126 ? 56.207  103.970 156.044 1.00 81.75  ? 2126 GLU A OE1   1 
ATOM   5369  O  OE2   . GLU A 1 2126 ? 57.320  105.862 156.048 1.00 96.33  ? 2126 GLU A OE2   1 
ATOM   5370  N  N     . ILE A 1 2127 ? 57.589  102.780 151.013 1.00 62.86  ? 2127 ILE A N     1 
ATOM   5371  C  CA    . ILE A 1 2127 ? 58.874  102.710 150.323 1.00 62.36  ? 2127 ILE A CA    1 
ATOM   5372  C  C     . ILE A 1 2127 ? 58.725  103.175 148.880 1.00 59.75  ? 2127 ILE A C     1 
ATOM   5373  O  O     . ILE A 1 2127 ? 59.559  103.931 148.365 1.00 56.63  ? 2127 ILE A O     1 
ATOM   5374  C  CB    . ILE A 1 2127 ? 59.446  101.282 150.406 1.00 59.07  ? 2127 ILE A CB    1 
ATOM   5375  C  CG1   . ILE A 1 2127 ? 60.098  101.049 151.770 1.00 55.27  ? 2127 ILE A CG1   1 
ATOM   5376  C  CG2   . ILE A 1 2127 ? 60.448  101.032 149.288 1.00 47.88  ? 2127 ILE A CG2   1 
ATOM   5377  C  CD1   . ILE A 1 2127 ? 60.111  99.599  152.200 1.00 56.23  ? 2127 ILE A CD1   1 
ATOM   5378  N  N     . ALA A 1 2128 ? 57.656  102.739 148.208 1.00 61.89  ? 2128 ALA A N     1 
ATOM   5379  C  CA    . ALA A 1 2128 ? 57.424  103.158 146.829 1.00 58.55  ? 2128 ALA A CA    1 
ATOM   5380  C  C     . ALA A 1 2128 ? 57.194  104.661 146.735 1.00 60.42  ? 2128 ALA A C     1 
ATOM   5381  O  O     . ALA A 1 2128 ? 57.674  105.311 145.798 1.00 58.17  ? 2128 ALA A O     1 
ATOM   5382  C  CB    . ALA A 1 2128 ? 56.238  102.394 146.242 1.00 55.56  ? 2128 ALA A CB    1 
ATOM   5383  N  N     . GLU A 1 2129 ? 56.453  105.231 147.689 1.00 65.48  ? 2129 GLU A N     1 
ATOM   5384  C  CA    . GLU A 1 2129 ? 56.193  106.669 147.664 1.00 65.86  ? 2129 GLU A CA    1 
ATOM   5385  C  C     . GLU A 1 2129 ? 57.483  107.468 147.815 1.00 63.47  ? 2129 GLU A C     1 
ATOM   5386  O  O     . GLU A 1 2129 ? 57.772  108.360 147.010 1.00 61.55  ? 2129 GLU A O     1 
ATOM   5387  C  CB    . GLU A 1 2129 ? 55.194  107.046 148.761 1.00 67.57  ? 2129 GLU A CB    1 
ATOM   5388  C  CG    . GLU A 1 2129 ? 53.795  106.452 148.601 1.00 71.18  ? 2129 GLU A CG    1 
ATOM   5389  C  CD    . GLU A 1 2129 ? 53.041  106.968 147.382 1.00 80.83  ? 2129 GLU A CD    1 
ATOM   5390  O  OE1   . GLU A 1 2129 ? 53.563  107.844 146.659 1.00 74.49  ? 2129 GLU A OE1   1 
ATOM   5391  O  OE2   . GLU A 1 2129 ? 51.911  106.490 147.146 1.00 89.40  ? 2129 GLU A OE2   1 
ATOM   5392  N  N     . ASN A 1 2130 ? 58.271  107.161 148.845 1.00 63.08  ? 2130 ASN A N     1 
ATOM   5393  C  CA    . ASN A 1 2130 ? 59.521  107.872 149.112 1.00 59.06  ? 2130 ASN A CA    1 
ATOM   5394  C  C     . ASN A 1 2130 ? 60.681  107.036 148.578 1.00 56.31  ? 2130 ASN A C     1 
ATOM   5395  O  O     . ASN A 1 2130 ? 61.403  106.370 149.320 1.00 53.88  ? 2130 ASN A O     1 
ATOM   5396  C  CB    . ASN A 1 2130 ? 59.664  108.164 150.602 1.00 58.35  ? 2130 ASN A CB    1 
ATOM   5397  C  CG    . ASN A 1 2130 ? 58.580  109.088 151.120 1.00 69.39  ? 2130 ASN A CG    1 
ATOM   5398  O  OD1   . ASN A 1 2130 ? 57.751  108.692 151.940 1.00 75.18  ? 2130 ASN A OD1   1 
ATOM   5399  N  ND2   . ASN A 1 2130 ? 58.580  110.327 150.643 1.00 75.44  ? 2130 ASN A ND2   1 
ATOM   5400  N  N     . LEU A 1 2131 ? 60.855  107.080 147.259 1.00 52.23  ? 2131 LEU A N     1 
ATOM   5401  C  CA    . LEU A 1 2131 ? 61.929  106.355 146.587 1.00 48.16  ? 2131 LEU A CA    1 
ATOM   5402  C  C     . LEU A 1 2131 ? 62.544  107.276 145.542 1.00 42.99  ? 2131 LEU A C     1 
ATOM   5403  O  O     . LEU A 1 2131 ? 61.822  107.765 144.650 1.00 43.00  ? 2131 LEU A O     1 
ATOM   5404  C  CB    . LEU A 1 2131 ? 61.408  105.067 145.946 1.00 46.37  ? 2131 LEU A CB    1 
ATOM   5405  C  CG    . LEU A 1 2131 ? 62.445  104.158 145.285 1.00 38.08  ? 2131 LEU A CG    1 
ATOM   5406  C  CD1   . LEU A 1 2131 ? 63.439  103.644 146.314 1.00 41.84  ? 2131 LEU A CD1   1 
ATOM   5407  C  CD2   . LEU A 1 2131 ? 61.761  103.004 144.574 1.00 39.43  ? 2131 LEU A CD2   1 
ATOM   5408  N  N     . PRO A 1 2132 ? 63.850  107.544 145.601 1.00 40.64  ? 2132 PRO A N     1 
ATOM   5409  C  CA    . PRO A 1 2132 ? 64.495  108.442 144.617 1.00 35.39  ? 2132 PRO A CA    1 
ATOM   5410  C  C     . PRO A 1 2132 ? 64.712  107.765 143.266 1.00 27.63  ? 2132 PRO A C     1 
ATOM   5411  O  O     . PRO A 1 2132 ? 65.780  107.249 142.939 1.00 26.30  ? 2132 PRO A O     1 
ATOM   5412  C  CB    . PRO A 1 2132 ? 65.817  108.801 145.303 1.00 36.86  ? 2132 PRO A CB    1 
ATOM   5413  C  CG    . PRO A 1 2132 ? 65.762  108.190 146.693 1.00 35.19  ? 2132 PRO A CG    1 
ATOM   5414  C  CD    . PRO A 1 2132 ? 64.808  107.057 146.602 1.00 37.31  ? 2132 PRO A CD    1 
ATOM   5415  N  N     . GLU A 1 2133 ? 63.652  107.765 142.453 1.00 26.76  ? 2133 GLU A N     1 
ATOM   5416  C  CA    . GLU A 1 2133 ? 63.713  107.130 141.140 1.00 25.30  ? 2133 GLU A CA    1 
ATOM   5417  C  C     . GLU A 1 2133 ? 64.738  107.809 140.240 1.00 20.94  ? 2133 GLU A C     1 
ATOM   5418  O  O     . GLU A 1 2133 ? 65.497  107.135 139.530 1.00 21.02  ? 2133 GLU A O     1 
ATOM   5419  C  CB    . GLU A 1 2133 ? 62.331  107.154 140.490 1.00 25.44  ? 2133 GLU A CB    1 
ATOM   5420  C  CG    . GLU A 1 2133 ? 61.282  106.355 141.240 1.00 27.70  ? 2133 GLU A CG    1 
ATOM   5421  C  CD    . GLU A 1 2133 ? 59.974  106.263 140.485 1.00 27.38  ? 2133 GLU A CD    1 
ATOM   5422  O  OE1   . GLU A 1 2133 ? 59.893  106.811 139.367 1.00 24.19  ? 2133 GLU A OE1   1 
ATOM   5423  O  OE2   . GLU A 1 2133 ? 59.025  105.644 141.011 1.00 28.58  ? 2133 GLU A OE2   1 
ATOM   5424  N  N     . GLN A 1 2134 ? 64.775  109.144 140.256 1.00 19.94  ? 2134 GLN A N     1 
ATOM   5425  C  CA    . GLN A 1 2134 ? 65.760  109.858 139.454 1.00 21.76  ? 2134 GLN A CA    1 
ATOM   5426  C  C     . GLN A 1 2134 ? 67.176  109.526 139.903 1.00 18.74  ? 2134 GLN A C     1 
ATOM   5427  O  O     . GLN A 1 2134 ? 68.077  109.398 139.072 1.00 20.76  ? 2134 GLN A O     1 
ATOM   5428  C  CB    . GLN A 1 2134 ? 65.515  111.365 139.519 1.00 21.89  ? 2134 GLN A CB    1 
ATOM   5429  C  CG    . GLN A 1 2134 ? 64.265  111.820 138.787 1.00 24.57  ? 2134 GLN A CG    1 
ATOM   5430  C  CD    . GLN A 1 2134 ? 64.226  113.319 138.576 1.00 26.78  ? 2134 GLN A CD    1 
ATOM   5431  O  OE1   . GLN A 1 2134 ? 65.147  114.037 138.963 1.00 33.13  ? 2134 GLN A OE1   1 
ATOM   5432  N  NE2   . GLN A 1 2134 ? 63.157  113.801 137.953 1.00 27.86  ? 2134 GLN A NE2   1 
ATOM   5433  N  N     . GLU A 1 2135 ? 67.391  109.381 141.212 1.00 22.81  ? 2135 GLU A N     1 
ATOM   5434  C  CA    . GLU A 1 2135 ? 68.716  109.010 141.700 1.00 24.07  ? 2135 GLU A CA    1 
ATOM   5435  C  C     . GLU A 1 2135 ? 69.111  107.620 141.213 1.00 20.08  ? 2135 GLU A C     1 
ATOM   5436  O  O     . GLU A 1 2135 ? 70.273  107.383 140.864 1.00 21.34  ? 2135 GLU A O     1 
ATOM   5437  C  CB    . GLU A 1 2135 ? 68.758  109.084 143.226 1.00 29.61  ? 2135 GLU A CB    1 
ATOM   5438  C  CG    . GLU A 1 2135 ? 70.154  108.959 143.812 1.00 33.81  ? 2135 GLU A CG    1 
ATOM   5439  C  CD    . GLU A 1 2135 ? 70.141  108.638 145.294 1.00 47.82  ? 2135 GLU A CD    1 
ATOM   5440  O  OE1   . GLU A 1 2135 ? 71.230  108.600 145.905 1.00 58.92  ? 2135 GLU A OE1   1 
ATOM   5441  O  OE2   . GLU A 1 2135 ? 69.043  108.424 145.848 1.00 49.07  ? 2135 GLU A OE2   1 
ATOM   5442  N  N     . ILE A 1 2136 ? 68.153  106.691 141.179 1.00 19.31  ? 2136 ILE A N     1 
ATOM   5443  C  CA    . ILE A 1 2136 ? 68.411  105.356 140.643 1.00 15.49  ? 2136 ILE A CA    1 
ATOM   5444  C  C     . ILE A 1 2136 ? 68.808  105.437 139.174 1.00 14.22  ? 2136 ILE A C     1 
ATOM   5445  O  O     . ILE A 1 2136 ? 69.765  104.786 138.727 1.00 13.81  ? 2136 ILE A O     1 
ATOM   5446  C  CB    . ILE A 1 2136 ? 67.174  104.461 140.845 1.00 16.50  ? 2136 ILE A CB    1 
ATOM   5447  C  CG1   . ILE A 1 2136 ? 66.875  104.293 142.337 1.00 19.97  ? 2136 ILE A CG1   1 
ATOM   5448  C  CG2   . ILE A 1 2136 ? 67.349  103.122 140.147 1.00 13.79  ? 2136 ILE A CG2   1 
ATOM   5449  C  CD1   . ILE A 1 2136 ? 65.549  103.630 142.624 1.00 22.16  ? 2136 ILE A CD1   1 
ATOM   5450  N  N     . LEU A 1 2137 ? 68.071  106.236 138.399 1.00 14.45  ? 2137 LEU A N     1 
ATOM   5451  C  CA    . LEU A 1 2137 ? 68.384  106.374 136.980 1.00 14.02  ? 2137 LEU A CA    1 
ATOM   5452  C  C     . LEU A 1 2137 ? 69.758  107.005 136.778 1.00 15.14  ? 2137 LEU A C     1 
ATOM   5453  O  O     . LEU A 1 2137 ? 70.514  106.592 135.891 1.00 14.85  ? 2137 LEU A O     1 
ATOM   5454  C  CB    . LEU A 1 2137 ? 67.298  107.192 136.282 1.00 14.84  ? 2137 LEU A CB    1 
ATOM   5455  C  CG    . LEU A 1 2137 ? 67.442  107.374 134.772 1.00 16.99  ? 2137 LEU A CG    1 
ATOM   5456  C  CD1   . LEU A 1 2137 ? 67.374  106.029 134.069 1.00 15.13  ? 2137 LEU A CD1   1 
ATOM   5457  C  CD2   . LEU A 1 2137 ? 66.365  108.307 134.245 1.00 18.57  ? 2137 LEU A CD2   1 
ATOM   5458  N  N     . ILE A 1 2138 ? 70.099  108.003 137.597 1.00 14.00  ? 2138 ILE A N     1 
ATOM   5459  C  CA    . ILE A 1 2138 ? 71.422  108.619 137.523 1.00 16.15  ? 2138 ILE A CA    1 
ATOM   5460  C  C     . ILE A 1 2138 ? 72.500  107.599 137.853 1.00 14.25  ? 2138 ILE A C     1 
ATOM   5461  O  O     . ILE A 1 2138 ? 73.556  107.563 137.213 1.00 15.54  ? 2138 ILE A O     1 
ATOM   5462  C  CB    . ILE A 1 2138 ? 71.509  109.843 138.455 1.00 20.06  ? 2138 ILE A CB    1 
ATOM   5463  C  CG1   . ILE A 1 2138 ? 70.461  110.888 138.084 1.00 23.57  ? 2138 ILE A CG1   1 
ATOM   5464  C  CG2   . ILE A 1 2138 ? 72.897  110.458 138.399 1.00 17.82  ? 2138 ILE A CG2   1 
ATOM   5465  C  CD1   . ILE A 1 2138 ? 70.605  111.428 136.703 1.00 21.42  ? 2138 ILE A CD1   1 
ATOM   5466  N  N     . GLN A 1 2139 ? 72.261  106.767 138.868 1.00 13.14  ? 2139 GLN A N     1 
ATOM   5467  C  CA    . GLN A 1 2139 ? 73.236  105.748 139.237 1.00 12.02  ? 2139 GLN A CA    1 
ATOM   5468  C  C     . GLN A 1 2139 ? 73.482  104.789 138.082 1.00 15.20  ? 2139 GLN A C     1 
ATOM   5469  O  O     . GLN A 1 2139 ? 74.631  104.454 137.771 1.00 21.49  ? 2139 GLN A O     1 
ATOM   5470  C  CB    . GLN A 1 2139 ? 72.757  104.988 140.473 1.00 12.00  ? 2139 GLN A CB    1 
ATOM   5471  C  CG    . GLN A 1 2139 ? 73.799  104.063 141.070 1.00 14.91  ? 2139 GLN A CG    1 
ATOM   5472  C  CD    . GLN A 1 2139 ? 73.260  103.253 142.231 1.00 18.28  ? 2139 GLN A CD    1 
ATOM   5473  O  OE1   . GLN A 1 2139 ? 72.741  103.805 143.200 1.00 25.52  ? 2139 GLN A OE1   1 
ATOM   5474  N  NE2   . GLN A 1 2139 ? 73.387  101.934 142.141 1.00 18.07  ? 2139 GLN A NE2   1 
ATOM   5475  N  N     . SER A 1 2140 ? 72.408  104.343 137.428 1.00 14.96  ? 2140 SER A N     1 
ATOM   5476  C  CA    . SER A 1 2140 ? 72.566  103.438 136.292 1.00 12.97  ? 2140 SER A CA    1 
ATOM   5477  C  C     . SER A 1 2140 ? 73.304  104.118 135.143 1.00 11.84  ? 2140 SER A C     1 
ATOM   5478  O  O     . SER A 1 2140 ? 74.216  103.535 134.541 1.00 13.32  ? 2140 SER A O     1 
ATOM   5479  C  CB    . SER A 1 2140 ? 71.200  102.929 135.837 1.00 12.66  ? 2140 SER A CB    1 
ATOM   5480  O  OG    . SER A 1 2140 ? 70.584  102.184 136.869 1.00 17.41  ? 2140 SER A OG    1 
ATOM   5481  N  N     . VAL A 1 2141 ? 72.932  105.364 134.839 1.00 12.35  ? 2141 VAL A N     1 
ATOM   5482  C  CA    . VAL A 1 2141 ? 73.570  106.092 133.745 1.00 11.98  ? 2141 VAL A CA    1 
ATOM   5483  C  C     . VAL A 1 2141 ? 75.060  106.251 134.011 1.00 12.75  ? 2141 VAL A C     1 
ATOM   5484  O  O     . VAL A 1 2141 ? 75.891  106.050 133.119 1.00 15.86  ? 2141 VAL A O     1 
ATOM   5485  C  CB    . VAL A 1 2141 ? 72.889  107.456 133.533 1.00 9.24   ? 2141 VAL A CB    1 
ATOM   5486  C  CG1   . VAL A 1 2141 ? 73.732  108.330 132.622 1.00 11.18  ? 2141 VAL A CG1   1 
ATOM   5487  C  CG2   . VAL A 1 2141 ? 71.509  107.269 132.940 1.00 10.64  ? 2141 VAL A CG2   1 
ATOM   5488  N  N     . CYS A 1 2142 ? 75.421  106.620 135.241 1.00 10.10  ? 2142 CYS A N     1 
ATOM   5489  C  CA    . CYS A 1 2142 ? 76.834  106.773 135.567 1.00 15.39  ? 2142 CYS A CA    1 
ATOM   5490  C  C     . CYS A 1 2142 ? 77.568  105.443 135.483 1.00 17.51  ? 2142 CYS A C     1 
ATOM   5491  O  O     . CYS A 1 2142 ? 78.562  105.332 134.758 1.00 17.65  ? 2142 CYS A O     1 
ATOM   5492  C  CB    . CYS A 1 2142 ? 76.995  107.400 136.951 1.00 20.14  ? 2142 CYS A CB    1 
ATOM   5493  S  SG    . CYS A 1 2142 ? 76.259  109.043 137.099 1.00 26.58  ? 2142 CYS A SG    1 
ATOM   5494  N  N     . GLU A 1 2143 ? 77.060  104.409 136.159 1.00 15.58  ? 2143 GLU A N     1 
ATOM   5495  C  CA    . GLU A 1 2143 ? 77.720  103.110 136.150 1.00 15.91  ? 2143 GLU A CA    1 
ATOM   5496  C  C     . GLU A 1 2143 ? 77.859  102.525 134.752 1.00 13.98  ? 2143 GLU A C     1 
ATOM   5497  O  O     . GLU A 1 2143 ? 78.739  101.685 134.540 1.00 15.54  ? 2143 GLU A O     1 
ATOM   5498  C  CB    . GLU A 1 2143 ? 76.965  102.123 137.043 1.00 14.68  ? 2143 GLU A CB    1 
ATOM   5499  C  CG    . GLU A 1 2143 ? 77.017  102.448 138.527 1.00 23.72  ? 2143 GLU A CG    1 
ATOM   5500  C  CD    . GLU A 1 2143 ? 76.090  101.570 139.346 1.00 29.46  ? 2143 GLU A CD    1 
ATOM   5501  O  OE1   . GLU A 1 2143 ? 75.369  100.743 138.748 1.00 31.24  ? 2143 GLU A OE1   1 
ATOM   5502  O  OE2   . GLU A 1 2143 ? 76.080  101.706 140.588 1.00 28.53  ? 2143 GLU A OE2   1 
ATOM   5503  N  N     . THR A 1 2144 ? 77.026  102.941 133.796 1.00 13.63  ? 2144 THR A N     1 
ATOM   5504  C  CA    . THR A 1 2144 ? 77.124  102.420 132.442 1.00 13.64  ? 2144 THR A CA    1 
ATOM   5505  C  C     . THR A 1 2144 ? 77.925  103.309 131.491 1.00 15.29  ? 2144 THR A C     1 
ATOM   5506  O  O     . THR A 1 2144 ? 78.592  102.777 130.595 1.00 22.77  ? 2144 THR A O     1 
ATOM   5507  C  CB    . THR A 1 2144 ? 75.713  102.180 131.872 1.00 17.98  ? 2144 THR A CB    1 
ATOM   5508  O  OG1   . THR A 1 2144 ? 75.145  101.023 132.498 1.00 14.33  ? 2144 THR A OG1   1 
ATOM   5509  C  CG2   . THR A 1 2144 ? 75.754  101.923 130.380 1.00 21.13  ? 2144 THR A CG2   1 
ATOM   5510  N  N     . MET A 1 2145 ? 77.940  104.630 131.690 1.00 13.86  ? 2145 MET A N     1 
ATOM   5511  C  CA    . MET A 1 2145 ? 78.540  105.535 130.713 1.00 12.63  ? 2145 MET A CA    1 
ATOM   5512  C  C     . MET A 1 2145 ? 79.859  106.148 131.171 1.00 12.58  ? 2145 MET A C     1 
ATOM   5513  O  O     . MET A 1 2145 ? 80.711  106.466 130.335 1.00 14.84  ? 2145 MET A O     1 
ATOM   5514  C  CB    . MET A 1 2145 ? 77.563  106.662 130.370 1.00 16.34  ? 2145 MET A CB    1 
ATOM   5515  C  CG    . MET A 1 2145 ? 76.245  106.210 129.778 1.00 16.87  ? 2145 MET A CG    1 
ATOM   5516  S  SD    . MET A 1 2145 ? 76.470  105.348 128.215 1.00 47.91  ? 2145 MET A SD    1 
ATOM   5517  C  CE    . MET A 1 2145 ? 74.930  104.451 128.110 1.00 18.32  ? 2145 MET A CE    1 
ATOM   5518  N  N     . VAL A 1 2146 ? 80.036  106.338 132.483 1.00 11.60  ? 2146 VAL A N     1 
ATOM   5519  C  CA    . VAL A 1 2146 ? 81.235  107.022 132.978 1.00 11.33  ? 2146 VAL A CA    1 
ATOM   5520  C  C     . VAL A 1 2146 ? 82.524  106.329 132.558 1.00 10.38  ? 2146 VAL A C     1 
ATOM   5521  O  O     . VAL A 1 2146 ? 83.452  107.021 132.115 1.00 11.45  ? 2146 VAL A O     1 
ATOM   5522  C  CB    . VAL A 1 2146 ? 81.131  107.232 134.495 1.00 13.02  ? 2146 VAL A CB    1 
ATOM   5523  C  CG1   . VAL A 1 2146 ? 82.487  107.579 135.091 1.00 9.53   ? 2146 VAL A CG1   1 
ATOM   5524  C  CG2   . VAL A 1 2146 ? 80.116  108.320 134.807 1.00 13.44  ? 2146 VAL A CG2   1 
ATOM   5525  N  N     . PRO A 1 2147 ? 82.670  105.000 132.660 1.00 9.18   ? 2147 PRO A N     1 
ATOM   5526  C  CA    . PRO A 1 2147 ? 83.966  104.392 132.313 1.00 8.23   ? 2147 PRO A CA    1 
ATOM   5527  C  C     . PRO A 1 2147 ? 84.399  104.605 130.872 1.00 5.97   ? 2147 PRO A C     1 
ATOM   5528  O  O     . PRO A 1 2147 ? 85.604  104.583 130.597 1.00 7.12   ? 2147 PRO A O     1 
ATOM   5529  C  CB    . PRO A 1 2147 ? 83.744  102.903 132.619 1.00 6.72   ? 2147 PRO A CB    1 
ATOM   5530  C  CG    . PRO A 1 2147 ? 82.276  102.727 132.553 1.00 9.53   ? 2147 PRO A CG    1 
ATOM   5531  C  CD    . PRO A 1 2147 ? 81.728  103.978 133.149 1.00 7.02   ? 2147 PRO A CD    1 
ATOM   5532  N  N     . LYS A 1 2148 ? 83.468  104.812 129.942 1.00 5.78   ? 2148 LYS A N     1 
ATOM   5533  C  CA    . LYS A 1 2148 ? 83.837  104.976 128.542 1.00 5.54   ? 2148 LYS A CA    1 
ATOM   5534  C  C     . LYS A 1 2148 ? 84.308  106.383 128.201 1.00 5.73   ? 2148 LYS A C     1 
ATOM   5535  O  O     . LYS A 1 2148 ? 84.899  106.578 127.135 1.00 8.49   ? 2148 LYS A O     1 
ATOM   5536  C  CB    . LYS A 1 2148 ? 82.661  104.618 127.627 1.00 6.84   ? 2148 LYS A CB    1 
ATOM   5537  C  CG    . LYS A 1 2148 ? 81.682  105.753 127.386 1.00 9.86   ? 2148 LYS A CG    1 
ATOM   5538  C  CD    . LYS A 1 2148 ? 80.577  105.328 126.435 1.00 12.25  ? 2148 LYS A CD    1 
ATOM   5539  C  CE    . LYS A 1 2148 ? 79.691  104.265 127.058 1.00 17.52  ? 2148 LYS A CE    1 
ATOM   5540  N  NZ    . LYS A 1 2148 ? 78.579  103.872 126.151 1.00 19.61  ? 2148 LYS A NZ    1 
ATOM   5541  N  N     . LEU A 1 2149 ? 84.073  107.359 129.070 1.00 7.26   ? 2149 LEU A N     1 
ATOM   5542  C  CA    . LEU A 1 2149 ? 84.341  108.745 128.723 1.00 8.06   ? 2149 LEU A CA    1 
ATOM   5543  C  C     . LEU A 1 2149 ? 85.808  109.099 128.925 1.00 7.76   ? 2149 LEU A C     1 
ATOM   5544  O  O     . LEU A 1 2149 ? 86.484  108.575 129.814 1.00 9.74   ? 2149 LEU A O     1 
ATOM   5545  C  CB    . LEU A 1 2149 ? 83.471  109.685 129.552 1.00 9.46   ? 2149 LEU A CB    1 
ATOM   5546  C  CG    . LEU A 1 2149 ? 81.959  109.545 129.393 1.00 9.89   ? 2149 LEU A CG    1 
ATOM   5547  C  CD1   . LEU A 1 2149 ? 81.268  110.496 130.342 1.00 12.96  ? 2149 LEU A CD1   1 
ATOM   5548  C  CD2   . LEU A 1 2149 ? 81.537  109.808 127.958 1.00 7.02   ? 2149 LEU A CD2   1 
ATOM   5549  N  N     . VAL A 1 2150 ? 86.294  110.006 128.080 1.00 9.40   ? 2150 VAL A N     1 
ATOM   5550  C  CA    . VAL A 1 2150 ? 87.615  110.598 128.252 1.00 11.84  ? 2150 VAL A CA    1 
ATOM   5551  C  C     . VAL A 1 2150 ? 87.532  111.608 129.388 1.00 14.42  ? 2150 VAL A C     1 
ATOM   5552  O  O     . VAL A 1 2150 ? 86.436  111.953 129.843 1.00 17.07  ? 2150 VAL A O     1 
ATOM   5553  C  CB    . VAL A 1 2150 ? 88.115  111.251 126.951 1.00 13.66  ? 2150 VAL A CB    1 
ATOM   5554  C  CG1   . VAL A 1 2150 ? 88.395  110.187 125.901 1.00 7.81   ? 2150 VAL A CG1   1 
ATOM   5555  C  CG2   . VAL A 1 2150 ? 87.101  112.262 126.440 1.00 15.52  ? 2150 VAL A CG2   1 
ATOM   5556  N  N     . ALA A 1 2151 ? 88.688  112.086 129.853 1.00 17.84  ? 2151 ALA A N     1 
ATOM   5557  C  CA    . ALA A 1 2151 ? 88.713  112.959 131.023 1.00 19.07  ? 2151 ALA A CA    1 
ATOM   5558  C  C     . ALA A 1 2151 ? 87.941  114.251 130.780 1.00 23.96  ? 2151 ALA A C     1 
ATOM   5559  O  O     . ALA A 1 2151 ? 87.216  114.725 131.663 1.00 19.43  ? 2151 ALA A O     1 
ATOM   5560  C  CB    . ALA A 1 2151 ? 90.158  113.264 131.418 1.00 12.52  ? 2151 ALA A CB    1 
ATOM   5561  N  N     . GLU A 1 2152 ? 88.081  114.835 129.590 1.00 25.58  ? 2152 GLU A N     1 
ATOM   5562  C  CA    . GLU A 1 2152 ? 87.437  116.107 129.285 1.00 23.32  ? 2152 GLU A CA    1 
ATOM   5563  C  C     . GLU A 1 2152 ? 85.929  115.992 129.098 1.00 24.28  ? 2152 GLU A C     1 
ATOM   5564  O  O     . GLU A 1 2152 ? 85.249  117.024 129.064 1.00 30.43  ? 2152 GLU A O     1 
ATOM   5565  C  CB    . GLU A 1 2152 ? 88.085  116.726 128.040 1.00 31.11  ? 2152 GLU A CB    1 
ATOM   5566  C  CG    . GLU A 1 2152 ? 87.970  115.892 126.768 1.00 35.38  ? 2152 GLU A CG    1 
ATOM   5567  C  CD    . GLU A 1 2152 ? 86.722  116.189 125.957 1.00 36.38  ? 2152 GLU A CD    1 
ATOM   5568  O  OE1   . GLU A 1 2152 ? 85.948  117.090 126.341 1.00 32.92  ? 2152 GLU A OE1   1 
ATOM   5569  O  OE2   . GLU A 1 2152 ? 86.517  115.515 124.926 1.00 36.38  ? 2152 GLU A OE2   1 
ATOM   5570  N  N     . ASP A 1 2153 ? 85.387  114.779 128.985 1.00 24.00  ? 2153 ASP A N     1 
ATOM   5571  C  CA    . ASP A 1 2153 ? 83.953  114.594 128.806 1.00 20.46  ? 2153 ASP A CA    1 
ATOM   5572  C  C     . ASP A 1 2153 ? 83.203  114.334 130.105 1.00 19.78  ? 2153 ASP A C     1 
ATOM   5573  O  O     . ASP A 1 2153 ? 81.975  114.462 130.125 1.00 24.40  ? 2153 ASP A O     1 
ATOM   5574  C  CB    . ASP A 1 2153 ? 83.683  113.435 127.836 1.00 15.53  ? 2153 ASP A CB    1 
ATOM   5575  C  CG    . ASP A 1 2153 ? 83.651  113.882 126.389 1.00 21.32  ? 2153 ASP A CG    1 
ATOM   5576  O  OD1   . ASP A 1 2153 ? 83.763  115.099 126.137 1.00 27.76  ? 2153 ASP A OD1   1 
ATOM   5577  O  OD2   . ASP A 1 2153 ? 83.514  113.015 125.501 1.00 19.78  ? 2153 ASP A OD2   1 
ATOM   5578  N  N     . ILE A 1 2154 ? 83.904  113.963 131.180 1.00 19.25  ? 2154 ILE A N     1 
ATOM   5579  C  CA    . ILE A 1 2154 ? 83.227  113.677 132.448 1.00 19.67  ? 2154 ILE A CA    1 
ATOM   5580  C  C     . ILE A 1 2154 ? 82.513  114.906 133.006 1.00 24.33  ? 2154 ILE A C     1 
ATOM   5581  O  O     . ILE A 1 2154 ? 81.317  114.804 133.333 1.00 30.40  ? 2154 ILE A O     1 
ATOM   5582  C  CB    . ILE A 1 2154 ? 84.216  113.058 133.446 1.00 20.36  ? 2154 ILE A CB    1 
ATOM   5583  C  CG1   . ILE A 1 2154 ? 85.128  112.055 132.739 1.00 18.12  ? 2154 ILE A CG1   1 
ATOM   5584  C  CG2   . ILE A 1 2154 ? 83.479  112.374 134.576 1.00 23.96  ? 2154 ILE A CG2   1 
ATOM   5585  C  CD1   . ILE A 1 2154 ? 86.082  111.331 133.663 1.00 19.57  ? 2154 ILE A CD1   1 
ATOM   5586  N  N     . PRO A 1 2155 ? 83.159  116.075 133.147 1.00 26.24  ? 2155 PRO A N     1 
ATOM   5587  C  CA    . PRO A 1 2155 ? 82.399  117.256 133.594 1.00 21.33  ? 2155 PRO A CA    1 
ATOM   5588  C  C     . PRO A 1 2155 ? 81.290  117.642 132.634 1.00 24.68  ? 2155 PRO A C     1 
ATOM   5589  O  O     . PRO A 1 2155 ? 80.248  118.144 133.072 1.00 30.91  ? 2155 PRO A O     1 
ATOM   5590  C  CB    . PRO A 1 2155 ? 83.474  118.349 133.703 1.00 24.33  ? 2155 PRO A CB    1 
ATOM   5591  C  CG    . PRO A 1 2155 ? 84.773  117.623 133.742 1.00 19.64  ? 2155 PRO A CG    1 
ATOM   5592  C  CD    . PRO A 1 2155 ? 84.572  116.412 132.901 1.00 19.40  ? 2155 PRO A CD    1 
ATOM   5593  N  N     . LEU A 1 2156 ? 81.481  117.414 131.332 1.00 20.03  ? 2156 LEU A N     1 
ATOM   5594  C  CA    . LEU A 1 2156 ? 80.418  117.693 130.373 1.00 21.01  ? 2156 LEU A CA    1 
ATOM   5595  C  C     . LEU A 1 2156 ? 79.182  116.853 130.663 1.00 22.87  ? 2156 LEU A C     1 
ATOM   5596  O  O     . LEU A 1 2156 ? 78.059  117.371 130.682 1.00 28.88  ? 2156 LEU A O     1 
ATOM   5597  C  CB    . LEU A 1 2156 ? 80.909  117.432 128.948 1.00 24.60  ? 2156 LEU A CB    1 
ATOM   5598  C  CG    . LEU A 1 2156 ? 81.901  118.403 128.302 1.00 30.31  ? 2156 LEU A CG    1 
ATOM   5599  C  CD1   . LEU A 1 2156 ? 81.871  118.255 126.788 1.00 34.97  ? 2156 LEU A CD1   1 
ATOM   5600  C  CD2   . LEU A 1 2156 ? 81.604  119.835 128.701 1.00 38.15  ? 2156 LEU A CD2   1 
ATOM   5601  N  N     . LEU A 1 2157 ? 79.369  115.555 130.912 1.00 25.14  ? 2157 LEU A N     1 
ATOM   5602  C  CA    . LEU A 1 2157 ? 78.219  114.694 131.157 1.00 22.85  ? 2157 LEU A CA    1 
ATOM   5603  C  C     . LEU A 1 2157 ? 77.599  114.979 132.519 1.00 18.94  ? 2157 LEU A C     1 
ATOM   5604  O  O     . LEU A 1 2157 ? 76.381  114.861 132.685 1.00 19.21  ? 2157 LEU A O     1 
ATOM   5605  C  CB    . LEU A 1 2157 ? 78.612  113.220 131.015 1.00 22.90  ? 2157 LEU A CB    1 
ATOM   5606  C  CG    . LEU A 1 2157 ? 77.477  112.187 131.076 1.00 19.32  ? 2157 LEU A CG    1 
ATOM   5607  C  CD1   . LEU A 1 2157 ? 77.809  110.969 130.240 1.00 20.68  ? 2157 LEU A CD1   1 
ATOM   5608  C  CD2   . LEU A 1 2157 ? 77.210  111.742 132.504 1.00 13.07  ? 2157 LEU A CD2   1 
ATOM   5609  N  N     . PHE A 1 2158 ? 78.410  115.367 133.507 1.00 18.90  ? 2158 PHE A N     1 
ATOM   5610  C  CA    . PHE A 1 2158 ? 77.820  115.776 134.781 1.00 23.43  ? 2158 PHE A CA    1 
ATOM   5611  C  C     . PHE A 1 2158 ? 76.998  117.053 134.632 1.00 23.74  ? 2158 PHE A C     1 
ATOM   5612  O  O     . PHE A 1 2158 ? 75.942  117.196 135.260 1.00 22.24  ? 2158 PHE A O     1 
ATOM   5613  C  CB    . PHE A 1 2158 ? 78.898  115.943 135.852 1.00 26.66  ? 2158 PHE A CB    1 
ATOM   5614  C  CG    . PHE A 1 2158 ? 79.397  114.642 136.413 1.00 33.69  ? 2158 PHE A CG    1 
ATOM   5615  C  CD1   . PHE A 1 2158 ? 80.751  114.362 136.467 1.00 33.40  ? 2158 PHE A CD1   1 
ATOM   5616  C  CD2   . PHE A 1 2158 ? 78.503  113.695 136.887 1.00 30.01  ? 2158 PHE A CD2   1 
ATOM   5617  C  CE1   . PHE A 1 2158 ? 81.202  113.165 136.991 1.00 39.65  ? 2158 PHE A CE1   1 
ATOM   5618  C  CE2   . PHE A 1 2158 ? 78.949  112.496 137.406 1.00 31.93  ? 2158 PHE A CE2   1 
ATOM   5619  C  CZ    . PHE A 1 2158 ? 80.300  112.230 137.457 1.00 42.57  ? 2158 PHE A CZ    1 
ATOM   5620  N  N     . SER A 1 2159 ? 77.460  117.993 133.804 1.00 23.52  ? 2159 SER A N     1 
ATOM   5621  C  CA    . SER A 1 2159 ? 76.667  119.190 133.540 1.00 26.77  ? 2159 SER A CA    1 
ATOM   5622  C  C     . SER A 1 2159 ? 75.378  118.846 132.804 1.00 27.42  ? 2159 SER A C     1 
ATOM   5623  O  O     . SER A 1 2159 ? 74.325  119.432 133.078 1.00 29.72  ? 2159 SER A O     1 
ATOM   5624  C  CB    . SER A 1 2159 ? 77.491  120.205 132.750 1.00 29.74  ? 2159 SER A CB    1 
ATOM   5625  O  OG    . SER A 1 2159 ? 78.596  120.652 133.513 1.00 39.78  ? 2159 SER A OG    1 
ATOM   5626  N  N     . LEU A 1 2160 ? 75.440  117.900 131.865 1.00 23.08  ? 2160 LEU A N     1 
ATOM   5627  C  CA    . LEU A 1 2160 ? 74.219  117.437 131.207 1.00 20.41  ? 2160 LEU A CA    1 
ATOM   5628  C  C     . LEU A 1 2160 ? 73.261  116.797 132.208 1.00 23.22  ? 2160 LEU A C     1 
ATOM   5629  O  O     . LEU A 1 2160 ? 72.044  117.004 132.134 1.00 26.05  ? 2160 LEU A O     1 
ATOM   5630  C  CB    . LEU A 1 2160 ? 74.556  116.455 130.085 1.00 21.64  ? 2160 LEU A CB    1 
ATOM   5631  C  CG    . LEU A 1 2160 ? 75.442  116.957 128.945 1.00 23.64  ? 2160 LEU A CG    1 
ATOM   5632  C  CD1   . LEU A 1 2160 ? 75.804  115.820 128.004 1.00 25.90  ? 2160 LEU A CD1   1 
ATOM   5633  C  CD2   . LEU A 1 2160 ? 74.740  118.069 128.188 1.00 27.22  ? 2160 LEU A CD2   1 
ATOM   5634  N  N     . LEU A 1 2161 ? 73.794  116.010 133.146 1.00 21.02  ? 2161 LEU A N     1 
ATOM   5635  C  CA    . LEU A 1 2161 ? 72.959  115.411 134.182 1.00 18.63  ? 2161 LEU A CA    1 
ATOM   5636  C  C     . LEU A 1 2161 ? 72.298  116.480 135.040 1.00 21.92  ? 2161 LEU A C     1 
ATOM   5637  O  O     . LEU A 1 2161 ? 71.110  116.380 135.365 1.00 24.37  ? 2161 LEU A O     1 
ATOM   5638  C  CB    . LEU A 1 2161 ? 73.794  114.478 135.059 1.00 19.95  ? 2161 LEU A CB    1 
ATOM   5639  C  CG    . LEU A 1 2161 ? 74.221  113.125 134.494 1.00 20.44  ? 2161 LEU A CG    1 
ATOM   5640  C  CD1   . LEU A 1 2161 ? 75.241  112.475 135.415 1.00 24.28  ? 2161 LEU A CD1   1 
ATOM   5641  C  CD2   . LEU A 1 2161 ? 73.021  112.224 134.308 1.00 13.06  ? 2161 LEU A CD2   1 
ATOM   5642  N  N     . SER A 1 2162 ? 73.056  117.510 135.420 1.00 24.91  ? 2162 SER A N     1 
ATOM   5643  C  CA    . SER A 1 2162 ? 72.487  118.594 136.215 1.00 26.95  ? 2162 SER A CA    1 
ATOM   5644  C  C     . SER A 1 2162 ? 71.428  119.354 135.427 1.00 27.30  ? 2162 SER A C     1 
ATOM   5645  O  O     . SER A 1 2162 ? 70.426  119.803 135.995 1.00 31.49  ? 2162 SER A O     1 
ATOM   5646  C  CB    . SER A 1 2162 ? 73.593  119.540 136.683 1.00 30.40  ? 2162 SER A CB    1 
ATOM   5647  O  OG    . SER A 1 2162 ? 74.194  120.206 135.587 1.00 34.90  ? 2162 SER A OG    1 
ATOM   5648  N  N     . ASP A 1 2163 ? 71.639  119.514 134.120 1.00 27.93  ? 2163 ASP A N     1 
ATOM   5649  C  CA    . ASP A 1 2163 ? 70.661  120.195 133.279 1.00 28.52  ? 2163 ASP A CA    1 
ATOM   5650  C  C     . ASP A 1 2163 ? 69.366  119.397 133.182 1.00 26.04  ? 2163 ASP A C     1 
ATOM   5651  O  O     . ASP A 1 2163 ? 68.269  119.957 133.288 1.00 32.82  ? 2163 ASP A O     1 
ATOM   5652  C  CB    . ASP A 1 2163 ? 71.249  120.431 131.888 1.00 32.35  ? 2163 ASP A CB    1 
ATOM   5653  C  CG    . ASP A 1 2163 ? 72.245  121.572 131.862 1.00 45.92  ? 2163 ASP A CG    1 
ATOM   5654  O  OD1   . ASP A 1 2163 ? 72.520  122.148 132.936 1.00 49.16  ? 2163 ASP A OD1   1 
ATOM   5655  O  OD2   . ASP A 1 2163 ? 72.758  121.888 130.769 1.00 48.49  ? 2163 ASP A OD2   1 
ATOM   5656  N  N     . VAL A 1 2164 ? 69.475  118.082 132.984 1.00 24.81  ? 2164 VAL A N     1 
ATOM   5657  C  CA    . VAL A 1 2164 ? 68.287  117.266 132.758 1.00 24.32  ? 2164 VAL A CA    1 
ATOM   5658  C  C     . VAL A 1 2164 ? 67.691  116.791 134.079 1.00 23.07  ? 2164 VAL A C     1 
ATOM   5659  O  O     . VAL A 1 2164 ? 66.469  116.656 134.209 1.00 26.41  ? 2164 VAL A O     1 
ATOM   5660  C  CB    . VAL A 1 2164 ? 68.629  116.089 131.827 1.00 23.29  ? 2164 VAL A CB    1 
ATOM   5661  C  CG1   . VAL A 1 2164 ? 67.396  115.245 131.555 1.00 23.18  ? 2164 VAL A CG1   1 
ATOM   5662  C  CG2   . VAL A 1 2164 ? 69.224  116.602 130.525 1.00 18.83  ? 2164 VAL A CG2   1 
ATOM   5663  N  N     . PHE A 1 2165 ? 68.532  116.545 135.084 1.00 24.77  ? 2165 PHE A N     1 
ATOM   5664  C  CA    . PHE A 1 2165 ? 68.098  116.065 136.394 1.00 23.43  ? 2165 PHE A CA    1 
ATOM   5665  C  C     . PHE A 1 2165 ? 68.640  117.003 137.468 1.00 29.40  ? 2165 PHE A C     1 
ATOM   5666  O  O     . PHE A 1 2165 ? 69.603  116.670 138.172 1.00 31.92  ? 2165 PHE A O     1 
ATOM   5667  C  CB    . PHE A 1 2165 ? 68.567  114.633 136.646 1.00 22.51  ? 2165 PHE A CB    1 
ATOM   5668  C  CG    . PHE A 1 2165 ? 68.117  113.650 135.602 1.00 25.25  ? 2165 PHE A CG    1 
ATOM   5669  C  CD1   . PHE A 1 2165 ? 68.874  113.433 134.462 1.00 23.31  ? 2165 PHE A CD1   1 
ATOM   5670  C  CD2   . PHE A 1 2165 ? 66.947  112.929 135.770 1.00 23.25  ? 2165 PHE A CD2   1 
ATOM   5671  C  CE1   . PHE A 1 2165 ? 68.467  112.523 133.506 1.00 18.95  ? 2165 PHE A CE1   1 
ATOM   5672  C  CE2   . PHE A 1 2165 ? 66.535  112.018 134.816 1.00 20.89  ? 2165 PHE A CE2   1 
ATOM   5673  C  CZ    . PHE A 1 2165 ? 67.296  111.815 133.683 1.00 19.17  ? 2165 PHE A CZ    1 
ATOM   5674  N  N     . PRO A 1 2166 ? 68.049  118.189 137.614 1.00 30.77  ? 2166 PRO A N     1 
ATOM   5675  C  CA    . PRO A 1 2166 ? 68.545  119.144 138.614 1.00 27.12  ? 2166 PRO A CA    1 
ATOM   5676  C  C     . PRO A 1 2166 ? 68.377  118.609 140.029 1.00 31.14  ? 2166 PRO A C     1 
ATOM   5677  O  O     . PRO A 1 2166 ? 67.381  117.961 140.354 1.00 33.05  ? 2166 PRO A O     1 
ATOM   5678  C  CB    . PRO A 1 2166 ? 67.680  120.388 138.372 1.00 26.73  ? 2166 PRO A CB    1 
ATOM   5679  C  CG    . PRO A 1 2166 ? 67.115  120.202 136.992 1.00 31.25  ? 2166 PRO A CG    1 
ATOM   5680  C  CD    . PRO A 1 2166 ? 66.897  118.730 136.877 1.00 28.33  ? 2166 PRO A CD    1 
ATOM   5681  N  N     . GLY A 1 2167 ? 69.368  118.890 140.873 1.00 33.56  ? 2167 GLY A N     1 
ATOM   5682  C  CA    . GLY A 1 2167 ? 69.304  118.530 142.273 1.00 36.11  ? 2167 GLY A CA    1 
ATOM   5683  C  C     . GLY A 1 2167 ? 69.570  117.075 142.585 1.00 41.01  ? 2167 GLY A C     1 
ATOM   5684  O  O     . GLY A 1 2167 ? 69.428  116.675 143.747 1.00 47.70  ? 2167 GLY A O     1 
ATOM   5685  N  N     . VAL A 1 2168 ? 69.947  116.270 141.597 1.00 39.99  ? 2168 VAL A N     1 
ATOM   5686  C  CA    . VAL A 1 2168 ? 70.193  114.846 141.791 1.00 39.73  ? 2168 VAL A CA    1 
ATOM   5687  C  C     . VAL A 1 2168 ? 71.691  114.602 141.684 1.00 40.94  ? 2168 VAL A C     1 
ATOM   5688  O  O     . VAL A 1 2168 ? 72.313  114.938 140.669 1.00 39.56  ? 2168 VAL A O     1 
ATOM   5689  C  CB    . VAL A 1 2168 ? 69.418  113.998 140.771 1.00 38.05  ? 2168 VAL A CB    1 
ATOM   5690  C  CG1   . VAL A 1 2168 ? 69.511  112.528 141.135 1.00 34.12  ? 2168 VAL A CG1   1 
ATOM   5691  C  CG2   . VAL A 1 2168 ? 67.967  114.447 140.701 1.00 35.07  ? 2168 VAL A CG2   1 
ATOM   5692  N  N     . GLN A 1 2169 ? 72.270  114.016 142.727 1.00 44.15  ? 2169 GLN A N     1 
ATOM   5693  C  CA    . GLN A 1 2169 ? 73.702  113.767 142.802 1.00 49.63  ? 2169 GLN A CA    1 
ATOM   5694  C  C     . GLN A 1 2169 ? 73.974  112.269 142.802 1.00 45.32  ? 2169 GLN A C     1 
ATOM   5695  O  O     . GLN A 1 2169 ? 73.234  111.493 143.415 1.00 43.63  ? 2169 GLN A O     1 
ATOM   5696  C  CB    . GLN A 1 2169 ? 74.304  114.406 144.056 1.00 55.76  ? 2169 GLN A CB    1 
ATOM   5697  C  CG    . GLN A 1 2169 ? 73.875  115.844 144.292 1.00 53.99  ? 2169 GLN A CG    1 
ATOM   5698  C  CD    . GLN A 1 2169 ? 74.054  116.715 143.065 1.00 60.85  ? 2169 GLN A CD    1 
ATOM   5699  O  OE1   . GLN A 1 2169 ? 73.094  117.288 142.549 1.00 64.65  ? 2169 GLN A OE1   1 
ATOM   5700  N  NE2   . GLN A 1 2169 ? 75.290  116.821 142.589 1.00 55.41  ? 2169 GLN A NE2   1 
ATOM   5701  N  N     . TYR A 1 2170 ? 75.038  111.870 142.113 1.00 44.18  ? 2170 TYR A N     1 
ATOM   5702  C  CA    . TYR A 1 2170 ? 75.460  110.479 142.055 1.00 43.40  ? 2170 TYR A CA    1 
ATOM   5703  C  C     . TYR A 1 2170 ? 76.701  110.273 142.914 1.00 45.01  ? 2170 TYR A C     1 
ATOM   5704  O  O     . TYR A 1 2170 ? 77.696  110.989 142.768 1.00 51.44  ? 2170 TYR A O     1 
ATOM   5705  C  CB    . TYR A 1 2170 ? 75.743  110.052 140.613 1.00 39.51  ? 2170 TYR A CB    1 
ATOM   5706  C  CG    . TYR A 1 2170 ? 76.562  108.785 140.485 1.00 37.04  ? 2170 TYR A CG    1 
ATOM   5707  C  CD1   . TYR A 1 2170 ? 75.958  107.537 140.545 1.00 28.83  ? 2170 TYR A CD1   1 
ATOM   5708  C  CD2   . TYR A 1 2170 ? 77.936  108.838 140.275 1.00 34.77  ? 2170 TYR A CD2   1 
ATOM   5709  C  CE1   . TYR A 1 2170 ? 76.699  106.377 140.422 1.00 33.97  ? 2170 TYR A CE1   1 
ATOM   5710  C  CE2   . TYR A 1 2170 ? 78.685  107.683 140.151 1.00 38.15  ? 2170 TYR A CE2   1 
ATOM   5711  C  CZ    . TYR A 1 2170 ? 78.061  106.456 140.224 1.00 40.54  ? 2170 TYR A CZ    1 
ATOM   5712  O  OH    . TYR A 1 2170 ? 78.803  105.304 140.099 1.00 29.95  ? 2170 TYR A OH    1 
ATOM   5713  N  N     . HIS A 1 2171 ? 76.634  109.289 143.808 1.00 46.68  ? 2171 HIS A N     1 
ATOM   5714  C  CA    . HIS A 1 2171 ? 77.759  108.940 144.667 1.00 48.63  ? 2171 HIS A CA    1 
ATOM   5715  C  C     . HIS A 1 2171 ? 78.027  107.451 144.527 1.00 47.98  ? 2171 HIS A C     1 
ATOM   5716  O  O     . HIS A 1 2171 ? 77.116  106.637 144.707 1.00 51.17  ? 2171 HIS A O     1 
ATOM   5717  C  CB    . HIS A 1 2171 ? 77.477  109.297 146.130 1.00 54.19  ? 2171 HIS A CB    1 
ATOM   5718  C  CG    . HIS A 1 2171 ? 76.866  110.650 146.316 1.00 61.34  ? 2171 HIS A CG    1 
ATOM   5719  N  ND1   . HIS A 1 2171 ? 75.504  110.859 146.308 1.00 64.28  ? 2171 HIS A ND1   1 
ATOM   5720  C  CD2   . HIS A 1 2171 ? 77.431  111.864 146.516 1.00 62.37  ? 2171 HIS A CD2   1 
ATOM   5721  C  CE1   . HIS A 1 2171 ? 75.256  112.143 146.496 1.00 62.27  ? 2171 HIS A CE1   1 
ATOM   5722  N  NE2   . HIS A 1 2171 ? 76.409  112.775 146.624 1.00 64.22  ? 2171 HIS A NE2   1 
ATOM   5723  N  N     . ARG A 1 2172 ? 79.268  107.097 144.205 1.00 44.79  ? 2172 ARG A N     1 
ATOM   5724  C  CA    . ARG A 1 2172 ? 79.638  105.692 144.132 1.00 44.64  ? 2172 ARG A CA    1 
ATOM   5725  C  C     . ARG A 1 2172 ? 79.603  105.064 145.519 1.00 49.95  ? 2172 ARG A C     1 
ATOM   5726  O  O     . ARG A 1 2172 ? 79.992  105.687 146.511 1.00 53.91  ? 2172 ARG A O     1 
ATOM   5727  C  CB    . ARG A 1 2172 ? 81.035  105.532 143.536 1.00 45.27  ? 2172 ARG A CB    1 
ATOM   5728  C  CG    . ARG A 1 2172 ? 81.264  106.237 142.216 1.00 42.57  ? 2172 ARG A CG    1 
ATOM   5729  C  CD    . ARG A 1 2172 ? 82.587  105.791 141.616 1.00 48.03  ? 2172 ARG A CD    1 
ATOM   5730  N  NE    . ARG A 1 2172 ? 83.648  105.770 142.616 1.00 48.90  ? 2172 ARG A NE    1 
ATOM   5731  C  CZ    . ARG A 1 2172 ? 84.292  104.676 143.003 1.00 46.29  ? 2172 ARG A CZ    1 
ATOM   5732  N  NH1   . ARG A 1 2172 ? 84.008  103.490 142.492 1.00 45.35  ? 2172 ARG A NH1   1 
ATOM   5733  N  NH2   . ARG A 1 2172 ? 85.243  104.776 143.927 1.00 43.11  ? 2172 ARG A NH2   1 
ATOM   5734  N  N     . GLY A 1 2173 ? 79.130  103.824 145.586 1.00 46.27  ? 2173 GLY A N     1 
ATOM   5735  C  CA    . GLY A 1 2173 ? 79.214  103.070 146.818 1.00 51.42  ? 2173 GLY A CA    1 
ATOM   5736  C  C     . GLY A 1 2173 ? 80.653  102.746 147.161 1.00 54.20  ? 2173 GLY A C     1 
ATOM   5737  O  O     . GLY A 1 2173 ? 81.389  102.221 146.320 1.00 53.28  ? 2173 GLY A O     1 
ATOM   5738  N  N     . GLU A 1 2174 ? 81.073  103.057 148.386 1.00 52.64  ? 2174 GLU A N     1 
ATOM   5739  C  CA    . GLU A 1 2174 ? 82.448  102.795 148.789 1.00 50.76  ? 2174 GLU A CA    1 
ATOM   5740  C  C     . GLU A 1 2174 ? 82.654  101.296 148.964 1.00 54.53  ? 2174 GLU A C     1 
ATOM   5741  O  O     . GLU A 1 2174 ? 82.328  100.735 150.015 1.00 60.07  ? 2174 GLU A O     1 
ATOM   5742  C  CB    . GLU A 1 2174 ? 82.783  103.548 150.080 1.00 50.98  ? 2174 GLU A CB    1 
ATOM   5743  C  CG    . GLU A 1 2174 ? 84.219  103.377 150.555 1.00 57.42  ? 2174 GLU A CG    1 
ATOM   5744  C  CD    . GLU A 1 2174 ? 85.231  103.982 149.599 1.00 63.89  ? 2174 GLU A CD    1 
ATOM   5745  O  OE1   . GLU A 1 2174 ? 84.871  104.924 148.861 1.00 66.92  ? 2174 GLU A OE1   1 
ATOM   5746  O  OE2   . GLU A 1 2174 ? 86.390  103.516 149.587 1.00 55.08  ? 2174 GLU A OE2   1 
ATOM   5747  N  N     . MET A 1 2175 ? 83.198  100.643 147.937 1.00 42.76  ? 2175 MET A N     1 
ATOM   5748  C  CA    . MET A 1 2175 ? 83.353  99.189  147.918 1.00 34.41  ? 2175 MET A CA    1 
ATOM   5749  C  C     . MET A 1 2175 ? 84.652  98.841  148.629 1.00 26.22  ? 2175 MET A C     1 
ATOM   5750  O  O     . MET A 1 2175 ? 85.661  98.527  148.001 1.00 28.48  ? 2175 MET A O     1 
ATOM   5751  C  CB    . MET A 1 2175 ? 83.345  98.667  146.487 1.00 35.15  ? 2175 MET A CB    1 
ATOM   5752  C  CG    . MET A 1 2175 ? 82.022  98.835  145.766 1.00 43.95  ? 2175 MET A CG    1 
ATOM   5753  S  SD    . MET A 1 2175 ? 82.062  98.142  144.103 1.00 57.62  ? 2175 MET A SD    1 
ATOM   5754  C  CE    . MET A 1 2175 ? 83.051  99.369  143.250 1.00 33.81  ? 2175 MET A CE    1 
ATOM   5755  N  N     . THR A 1 2176 ? 84.616  98.874  149.963 1.00 26.30  ? 2176 THR A N     1 
ATOM   5756  C  CA    . THR A 1 2176 ? 85.842  98.744  150.744 1.00 27.05  ? 2176 THR A CA    1 
ATOM   5757  C  C     . THR A 1 2176 ? 86.519  97.397  150.511 1.00 21.11  ? 2176 THR A C     1 
ATOM   5758  O  O     . THR A 1 2176 ? 87.628  97.338  149.966 1.00 26.84  ? 2176 THR A O     1 
ATOM   5759  C  CB    . THR A 1 2176 ? 85.538  98.942  152.230 1.00 33.51  ? 2176 THR A CB    1 
ATOM   5760  O  OG1   . THR A 1 2176 ? 84.612  97.940  152.669 1.00 37.26  ? 2176 THR A OG1   1 
ATOM   5761  C  CG2   . THR A 1 2176 ? 84.934  100.315 152.466 1.00 31.04  ? 2176 THR A CG2   1 
ATOM   5762  N  N     . ALA A 1 2177 ? 85.851  96.302  150.895 1.00 18.25  ? 2177 ALA A N     1 
ATOM   5763  C  CA    . ALA A 1 2177 ? 86.497  94.989  150.936 1.00 19.16  ? 2177 ALA A CA    1 
ATOM   5764  C  C     . ALA A 1 2177 ? 87.192  94.665  149.620 1.00 21.42  ? 2177 ALA A C     1 
ATOM   5765  O  O     . ALA A 1 2177 ? 88.315  94.140  149.608 1.00 23.83  ? 2177 ALA A O     1 
ATOM   5766  C  CB    . ALA A 1 2177 ? 85.468  93.913  151.282 1.00 16.53  ? 2177 ALA A CB    1 
ATOM   5767  N  N     . LEU A 1 2178 ? 86.549  94.996  148.500 1.00 16.49  ? 2178 LEU A N     1 
ATOM   5768  C  CA    . LEU A 1 2178 ? 87.204  94.853  147.207 1.00 16.38  ? 2178 LEU A CA    1 
ATOM   5769  C  C     . LEU A 1 2178 ? 88.464  95.707  147.142 1.00 15.10  ? 2178 LEU A C     1 
ATOM   5770  O  O     . LEU A 1 2178 ? 89.470  95.301  146.553 1.00 16.41  ? 2178 LEU A O     1 
ATOM   5771  C  CB    . LEU A 1 2178 ? 86.239  95.226  146.081 1.00 16.00  ? 2178 LEU A CB    1 
ATOM   5772  C  CG    . LEU A 1 2178 ? 86.800  95.125  144.661 1.00 10.91  ? 2178 LEU A CG    1 
ATOM   5773  C  CD1   . LEU A 1 2178 ? 87.314  93.721  144.377 1.00 10.73  ? 2178 LEU A CD1   1 
ATOM   5774  C  CD2   . LEU A 1 2178 ? 85.759  95.537  143.637 1.00 10.30  ? 2178 LEU A CD2   1 
ATOM   5775  N  N     . ARG A 1 2179 ? 88.435  96.893  147.758 1.00 14.68  ? 2179 ARG A N     1 
ATOM   5776  C  CA    . ARG A 1 2179 ? 89.601  97.769  147.688 1.00 14.89  ? 2179 ARG A CA    1 
ATOM   5777  C  C     . ARG A 1 2179 ? 90.761  97.245  148.529 1.00 17.70  ? 2179 ARG A C     1 
ATOM   5778  O  O     . ARG A 1 2179 ? 91.917  97.343  148.107 1.00 17.84  ? 2179 ARG A O     1 
ATOM   5779  C  CB    . ARG A 1 2179 ? 89.234  99.199  148.086 1.00 15.89  ? 2179 ARG A CB    1 
ATOM   5780  C  CG    . ARG A 1 2179 ? 88.235  99.850  147.146 1.00 17.57  ? 2179 ARG A CG    1 
ATOM   5781  C  CD    . ARG A 1 2179 ? 87.886  101.264 147.572 1.00 24.41  ? 2179 ARG A CD    1 
ATOM   5782  N  NE    . ARG A 1 2179 ? 88.936  102.205 147.200 1.00 29.02  ? 2179 ARG A NE    1 
ATOM   5783  C  CZ    . ARG A 1 2179 ? 88.758  103.242 146.394 1.00 33.47  ? 2179 ARG A CZ    1 
ATOM   5784  N  NH1   . ARG A 1 2179 ? 87.570  103.529 145.890 1.00 31.04  ? 2179 ARG A NH1   1 
ATOM   5785  N  NH2   . ARG A 1 2179 ? 89.799  104.010 146.085 1.00 29.43  ? 2179 ARG A NH2   1 
ATOM   5786  N  N     . GLU A 1 2180 ? 90.495  96.675  149.711 1.00 16.78  ? 2180 GLU A N     1 
ATOM   5787  C  CA    . GLU A 1 2180 ? 91.608  96.057  150.439 1.00 21.24  ? 2180 GLU A CA    1 
ATOM   5788  C  C     . GLU A 1 2180 ? 92.125  94.815  149.718 1.00 18.35  ? 2180 GLU A C     1 
ATOM   5789  O  O     . GLU A 1 2180 ? 93.332  94.538  149.733 1.00 19.59  ? 2180 GLU A O     1 
ATOM   5790  C  CB    . GLU A 1 2180 ? 91.278  95.716  151.901 1.00 26.89  ? 2180 GLU A CB    1 
ATOM   5791  C  CG    . GLU A 1 2180 ? 91.049  96.892  152.855 1.00 35.42  ? 2180 GLU A CG    1 
ATOM   5792  C  CD    . GLU A 1 2180 ? 89.659  97.445  152.816 1.00 44.11  ? 2180 GLU A CD    1 
ATOM   5793  O  OE1   . GLU A 1 2180 ? 88.840  96.871  152.092 1.00 34.86  ? 2180 GLU A OE1   1 
ATOM   5794  O  OE2   . GLU A 1 2180 ? 89.387  98.450  153.506 1.00 45.69  ? 2180 GLU A OE2   1 
ATOM   5795  N  N     . GLU A 1 2181 ? 91.235  94.050  149.080 1.00 15.92  ? 2181 GLU A N     1 
ATOM   5796  C  CA    . GLU A 1 2181 ? 91.710  92.904  148.307 1.00 13.74  ? 2181 GLU A CA    1 
ATOM   5797  C  C     . GLU A 1 2181 ? 92.602  93.351  147.153 1.00 14.82  ? 2181 GLU A C     1 
ATOM   5798  O  O     . GLU A 1 2181 ? 93.666  92.763  146.910 1.00 17.51  ? 2181 GLU A O     1 
ATOM   5799  C  CB    . GLU A 1 2181 ? 90.527  92.083  147.792 1.00 16.68  ? 2181 GLU A CB    1 
ATOM   5800  C  CG    . GLU A 1 2181 ? 89.786  91.287  148.866 1.00 19.75  ? 2181 GLU A CG    1 
ATOM   5801  C  CD    . GLU A 1 2181 ? 90.608  90.157  149.476 1.00 31.57  ? 2181 GLU A CD    1 
ATOM   5802  O  OE1   . GLU A 1 2181 ? 91.776  89.961  149.080 1.00 36.08  ? 2181 GLU A OE1   1 
ATOM   5803  O  OE2   . GLU A 1 2181 ? 90.076  89.458  150.363 1.00 37.15  ? 2181 GLU A OE2   1 
ATOM   5804  N  N     . LEU A 1 2182 ? 92.194  94.406  146.444 1.00 12.58  ? 2182 LEU A N     1 
ATOM   5805  C  CA    . LEU A 1 2182 ? 93.011  94.945  145.362 1.00 11.20  ? 2182 LEU A CA    1 
ATOM   5806  C  C     . LEU A 1 2182 ? 94.320  95.514  145.889 1.00 12.74  ? 2182 LEU A C     1 
ATOM   5807  O  O     . LEU A 1 2182 ? 95.355  95.412  145.226 1.00 13.87  ? 2182 LEU A O     1 
ATOM   5808  C  CB    . LEU A 1 2182 ? 92.230  96.012  144.596 1.00 9.62   ? 2182 LEU A CB    1 
ATOM   5809  C  CG    . LEU A 1 2182 ? 91.025  95.521  143.794 1.00 13.45  ? 2182 LEU A CG    1 
ATOM   5810  C  CD1   . LEU A 1 2182 ? 90.001  96.624  143.647 1.00 8.91   ? 2182 LEU A CD1   1 
ATOM   5811  C  CD2   . LEU A 1 2182 ? 91.465  95.025  142.430 1.00 8.04   ? 2182 LEU A CD2   1 
ATOM   5812  N  N     . LYS A 1 2183 ? 94.293  96.128  147.073 1.00 13.46  ? 2183 LYS A N     1 
ATOM   5813  C  CA    . LYS A 1 2183 ? 95.519  96.644  147.674 1.00 14.62  ? 2183 LYS A CA    1 
ATOM   5814  C  C     . LYS A 1 2183 ? 96.496  95.516  147.984 1.00 14.48  ? 2183 LYS A C     1 
ATOM   5815  O  O     . LYS A 1 2183 ? 97.699  95.635  147.722 1.00 15.46  ? 2183 LYS A O     1 
ATOM   5816  C  CB    . LYS A 1 2183 ? 95.178  97.429  148.940 1.00 14.32  ? 2183 LYS A CB    1 
ATOM   5817  C  CG    . LYS A 1 2183 ? 96.320  98.249  149.510 1.00 17.60  ? 2183 LYS A CG    1 
ATOM   5818  C  CD    . LYS A 1 2183 ? 95.923  98.898  150.829 1.00 23.60  ? 2183 LYS A CD    1 
ATOM   5819  C  CE    . LYS A 1 2183 ? 94.481  99.390  150.800 1.00 27.90  ? 2183 LYS A CE    1 
ATOM   5820  N  NZ    . LYS A 1 2183 ? 94.056  99.965  152.106 1.00 35.54  ? 2183 LYS A NZ    1 
ATOM   5821  N  N     . LYS A 1 2184 ? 95.994  94.410  148.537 1.00 14.11  ? 2184 LYS A N     1 
ATOM   5822  C  CA    . LYS A 1 2184 ? 96.852  93.258  148.802 1.00 14.93  ? 2184 LYS A CA    1 
ATOM   5823  C  C     . LYS A 1 2184 ? 97.419  92.688  147.506 1.00 13.94  ? 2184 LYS A C     1 
ATOM   5824  O  O     . LYS A 1 2184 ? 98.607  92.348  147.428 1.00 18.18  ? 2184 LYS A O     1 
ATOM   5825  C  CB    . LYS A 1 2184 ? 96.072  92.187  149.566 1.00 18.42  ? 2184 LYS A CB    1 
ATOM   5826  C  CG    . LYS A 1 2184 ? 95.776  92.542  151.013 1.00 24.25  ? 2184 LYS A CG    1 
ATOM   5827  C  CD    . LYS A 1 2184 ? 94.488  91.887  151.484 1.00 25.94  ? 2184 LYS A CD    1 
ATOM   5828  C  CE    . LYS A 1 2184 ? 94.392  91.883  153.001 1.00 31.91  ? 2184 LYS A CE    1 
ATOM   5829  N  NZ    . LYS A 1 2184 ? 93.875  93.176  153.528 1.00 29.67  ? 2184 LYS A NZ    1 
ATOM   5830  N  N     . VAL A 1 2185 ? 96.579  92.579  146.473 1.00 12.62  ? 2185 VAL A N     1 
ATOM   5831  C  CA    . VAL A 1 2185 ? 97.047  92.053  145.193 1.00 12.51  ? 2185 VAL A CA    1 
ATOM   5832  C  C     . VAL A 1 2185 ? 98.106  92.973  144.594 1.00 13.44  ? 2185 VAL A C     1 
ATOM   5833  O  O     . VAL A 1 2185 ? 99.108  92.510  144.034 1.00 16.97  ? 2185 VAL A O     1 
ATOM   5834  C  CB    . VAL A 1 2185 ? 95.861  91.839  144.233 1.00 14.64  ? 2185 VAL A CB    1 
ATOM   5835  C  CG1   . VAL A 1 2185 ? 96.359  91.533  142.830 1.00 11.47  ? 2185 VAL A CG1   1 
ATOM   5836  C  CG2   . VAL A 1 2185 ? 94.969  90.716  144.737 1.00 11.14  ? 2185 VAL A CG2   1 
ATOM   5837  N  N     . CYS A 1 2186 ? 97.906  94.288  144.709 1.00 12.55  ? 2186 CYS A N     1 
ATOM   5838  C  CA    . CYS A 1 2186 ? 98.894  95.249  144.230 1.00 10.36  ? 2186 CYS A CA    1 
ATOM   5839  C  C     . CYS A 1 2186 ? 100.205 95.106  144.989 1.00 11.48  ? 2186 CYS A C     1 
ATOM   5840  O  O     . CYS A 1 2186 ? 101.290 95.209  144.405 1.00 13.34  ? 2186 CYS A O     1 
ATOM   5841  C  CB    . CYS A 1 2186 ? 98.348  96.671  144.357 1.00 10.02  ? 2186 CYS A CB    1 
ATOM   5842  S  SG    . CYS A 1 2186 ? 97.177  97.142  143.065 1.00 8.73   ? 2186 CYS A SG    1 
ATOM   5843  N  N     . GLN A 1 2187 ? 100.121 94.879  146.300 1.00 15.08  ? 2187 GLN A N     1 
ATOM   5844  C  CA    . GLN A 1 2187 ? 101.328 94.667  147.089 1.00 14.62  ? 2187 GLN A CA    1 
ATOM   5845  C  C     . GLN A 1 2187 ? 102.072 93.416  146.636 1.00 16.83  ? 2187 GLN A C     1 
ATOM   5846  O  O     . GLN A 1 2187 ? 103.306 93.414  146.558 1.00 20.08  ? 2187 GLN A O     1 
ATOM   5847  C  CB    . GLN A 1 2187 ? 100.977 94.580  148.574 1.00 17.68  ? 2187 GLN A CB    1 
ATOM   5848  C  CG    . GLN A 1 2187 ? 102.166 94.288  149.474 1.00 25.14  ? 2187 GLN A CG    1 
ATOM   5849  C  CD    . GLN A 1 2187 ? 103.215 95.382  149.427 1.00 31.08  ? 2187 GLN A CD    1 
ATOM   5850  O  OE1   . GLN A 1 2187 ? 104.414 95.108  149.390 1.00 31.34  ? 2187 GLN A OE1   1 
ATOM   5851  N  NE2   . GLN A 1 2187 ? 102.766 96.633  149.429 1.00 31.84  ? 2187 GLN A NE2   1 
ATOM   5852  N  N     . GLU A 1 2188 ? 101.341 92.342  146.325 1.00 16.25  ? 2188 GLU A N     1 
ATOM   5853  C  CA    . GLU A 1 2188 ? 102.012 91.099  145.955 1.00 20.30  ? 2188 GLU A CA    1 
ATOM   5854  C  C     . GLU A 1 2188 ? 102.375 91.036  144.474 1.00 16.89  ? 2188 GLU A C     1 
ATOM   5855  O  O     . GLU A 1 2188 ? 103.008 90.063  144.050 1.00 18.06  ? 2188 GLU A O     1 
ATOM   5856  C  CB    . GLU A 1 2188 ? 101.155 89.894  146.363 1.00 21.41  ? 2188 GLU A CB    1 
ATOM   5857  C  CG    . GLU A 1 2188 ? 99.780  89.795  145.719 1.00 24.20  ? 2188 GLU A CG    1 
ATOM   5858  C  CD    . GLU A 1 2188 ? 99.793  89.102  144.370 1.00 33.93  ? 2188 GLU A CD    1 
ATOM   5859  O  OE1   . GLU A 1 2188 ? 100.763 88.372  144.079 1.00 38.19  ? 2188 GLU A OE1   1 
ATOM   5860  O  OE2   . GLU A 1 2188 ? 98.818  89.271  143.608 1.00 32.51  ? 2188 GLU A OE2   1 
ATOM   5861  N  N     . MET A 1 2189 ? 102.007 92.045  143.679 1.00 18.38  ? 2189 MET A N     1 
ATOM   5862  C  CA    . MET A 1 2189 ? 102.427 92.129  142.283 1.00 14.61  ? 2189 MET A CA    1 
ATOM   5863  C  C     . MET A 1 2189 ? 103.259 93.376  142.003 1.00 11.64  ? 2189 MET A C     1 
ATOM   5864  O  O     . MET A 1 2189 ? 103.437 93.746  140.838 1.00 14.77  ? 2189 MET A O     1 
ATOM   5865  C  CB    . MET A 1 2189 ? 101.223 92.088  141.342 1.00 12.80  ? 2189 MET A CB    1 
ATOM   5866  C  CG    . MET A 1 2189 ? 100.428 90.801  141.376 1.00 18.81  ? 2189 MET A CG    1 
ATOM   5867  S  SD    . MET A 1 2189 ? 99.032  90.833  140.235 1.00 24.62  ? 2189 MET A SD    1 
ATOM   5868  C  CE    . MET A 1 2189 ? 99.870  91.089  138.673 1.00 21.98  ? 2189 MET A CE    1 
ATOM   5869  N  N     . TYR A 1 2190 ? 103.760 94.035  143.048 1.00 12.38  ? 2190 TYR A N     1 
ATOM   5870  C  CA    . TYR A 1 2190 ? 104.635 95.203  142.920 1.00 10.63  ? 2190 TYR A CA    1 
ATOM   5871  C  C     . TYR A 1 2190 ? 103.948 96.354  142.191 1.00 8.74   ? 2190 TYR A C     1 
ATOM   5872  O  O     . TYR A 1 2190 ? 104.601 97.147  141.508 1.00 7.32   ? 2190 TYR A O     1 
ATOM   5873  C  CB    . TYR A 1 2190 ? 105.947 94.841  142.216 1.00 9.87   ? 2190 TYR A CB    1 
ATOM   5874  C  CG    . TYR A 1 2190 ? 106.585 93.577  142.735 1.00 11.45  ? 2190 TYR A CG    1 
ATOM   5875  C  CD1   . TYR A 1 2190 ? 107.301 93.573  143.923 1.00 10.55  ? 2190 TYR A CD1   1 
ATOM   5876  C  CD2   . TYR A 1 2190 ? 106.478 92.385  142.031 1.00 13.61  ? 2190 TYR A CD2   1 
ATOM   5877  C  CE1   . TYR A 1 2190 ? 107.882 92.417  144.398 1.00 12.29  ? 2190 TYR A CE1   1 
ATOM   5878  C  CE2   . TYR A 1 2190 ? 107.057 91.224  142.498 1.00 16.75  ? 2190 TYR A CE2   1 
ATOM   5879  C  CZ    . TYR A 1 2190 ? 107.760 91.246  143.682 1.00 20.06  ? 2190 TYR A CZ    1 
ATOM   5880  O  OH    . TYR A 1 2190 ? 108.341 90.091  144.152 1.00 25.73  ? 2190 TYR A OH    1 
ATOM   5881  N  N     . LEU A 1 2191 ? 102.631 96.458  142.325 1.00 10.05  ? 2191 LEU A N     1 
ATOM   5882  C  CA    . LEU A 1 2191 ? 101.865 97.510  141.675 1.00 6.04   ? 2191 LEU A CA    1 
ATOM   5883  C  C     . LEU A 1 2191 ? 101.515 98.607  142.672 1.00 6.10   ? 2191 LEU A C     1 
ATOM   5884  O  O     . LEU A 1 2191 ? 101.449 98.377  143.882 1.00 12.20  ? 2191 LEU A O     1 
ATOM   5885  C  CB    . LEU A 1 2191 ? 100.589 96.952  141.043 1.00 6.01   ? 2191 LEU A CB    1 
ATOM   5886  C  CG    . LEU A 1 2191 ? 100.776 96.045  139.825 1.00 6.42   ? 2191 LEU A CG    1 
ATOM   5887  C  CD1   . LEU A 1 2191 ? 99.457  95.852  139.096 1.00 6.65   ? 2191 LEU A CD1   1 
ATOM   5888  C  CD2   . LEU A 1 2191 ? 101.834 96.602  138.885 1.00 4.86   ? 2191 LEU A CD2   1 
ATOM   5889  N  N     . THR A 1 2192 ? 101.292 99.807  142.147 1.00 6.68   ? 2192 THR A N     1 
ATOM   5890  C  CA    . THR A 1 2192 ? 100.976 100.968 142.967 1.00 6.56   ? 2192 THR A CA    1 
ATOM   5891  C  C     . THR A 1 2192 ? 99.468  101.084 143.139 1.00 7.17   ? 2192 THR A C     1 
ATOM   5892  O  O     . THR A 1 2192 ? 98.724  101.118 142.154 1.00 6.68   ? 2192 THR A O     1 
ATOM   5893  C  CB    . THR A 1 2192 ? 101.535 102.244 142.336 1.00 6.75   ? 2192 THR A CB    1 
ATOM   5894  O  OG1   . THR A 1 2192 ? 102.964 102.166 142.281 1.00 6.12   ? 2192 THR A OG1   1 
ATOM   5895  C  CG2   . THR A 1 2192 ? 101.133 103.464 143.153 1.00 6.85   ? 2192 THR A CG2   1 
ATOM   5896  N  N     . TYR A 1 2193 ? 99.024  101.142 144.390 1.00 9.18   ? 2193 TYR A N     1 
ATOM   5897  C  CA    . TYR A 1 2193 ? 97.616  101.294 144.728 1.00 9.82   ? 2193 TYR A CA    1 
ATOM   5898  C  C     . TYR A 1 2193 ? 97.396  102.669 145.343 1.00 10.95  ? 2193 TYR A C     1 
ATOM   5899  O  O     . TYR A 1 2193 ? 98.139  103.078 146.241 1.00 14.16  ? 2193 TYR A O     1 
ATOM   5900  C  CB    . TYR A 1 2193 ? 97.159  100.195 145.692 1.00 8.99   ? 2193 TYR A CB    1 
ATOM   5901  C  CG    . TYR A 1 2193 ? 95.740  100.363 146.190 1.00 13.22  ? 2193 TYR A CG    1 
ATOM   5902  C  CD1   . TYR A 1 2193 ? 95.463  101.114 147.326 1.00 14.42  ? 2193 TYR A CD1   1 
ATOM   5903  C  CD2   . TYR A 1 2193 ? 94.676  99.774  145.520 1.00 11.58  ? 2193 TYR A CD2   1 
ATOM   5904  C  CE1   . TYR A 1 2193 ? 94.171  101.274 147.778 1.00 16.13  ? 2193 TYR A CE1   1 
ATOM   5905  C  CE2   . TYR A 1 2193 ? 93.379  99.928  145.967 1.00 13.27  ? 2193 TYR A CE2   1 
ATOM   5906  C  CZ    . TYR A 1 2193 ? 93.134  100.678 147.096 1.00 17.57  ? 2193 TYR A CZ    1 
ATOM   5907  O  OH    . TYR A 1 2193 ? 91.847  100.838 147.548 1.00 23.45  ? 2193 TYR A OH    1 
ATOM   5908  N  N     . GLY A 1 2194 ? 96.377  103.376 144.859 1.00 10.75  ? 2194 GLY A N     1 
ATOM   5909  C  CA    . GLY A 1 2194 ? 96.032  104.671 145.405 1.00 12.15  ? 2194 GLY A CA    1 
ATOM   5910  C  C     . GLY A 1 2194 ? 94.534  104.794 145.592 1.00 15.12  ? 2194 GLY A C     1 
ATOM   5911  O  O     . GLY A 1 2194 ? 93.748  104.021 145.040 1.00 17.38  ? 2194 GLY A O     1 
ATOM   5912  N  N     . ASP A 1 2195 ? 94.150  105.789 146.388 1.00 23.39  ? 2195 ASP A N     1 
ATOM   5913  C  CA    . ASP A 1 2195 ? 92.748  106.070 146.675 1.00 23.31  ? 2195 ASP A CA    1 
ATOM   5914  C  C     . ASP A 1 2195 ? 92.475  107.535 146.373 1.00 26.84  ? 2195 ASP A C     1 
ATOM   5915  O  O     . ASP A 1 2195 ? 93.093  108.419 146.974 1.00 30.87  ? 2195 ASP A O     1 
ATOM   5916  C  CB    . ASP A 1 2195 ? 92.407  105.747 148.133 1.00 19.38  ? 2195 ASP A CB    1 
ATOM   5917  C  CG    . ASP A 1 2195 ? 91.950  104.313 148.322 1.00 28.44  ? 2195 ASP A CG    1 
ATOM   5918  O  OD1   . ASP A 1 2195 ? 91.779  103.602 147.309 1.00 29.93  ? 2195 ASP A OD1   1 
ATOM   5919  O  OD2   . ASP A 1 2195 ? 91.759  103.897 149.483 1.00 32.80  ? 2195 ASP A OD2   1 
ATOM   5920  N  N     . GLY A 1 2196 ? 91.550  107.790 145.452 1.00 27.71  ? 2196 GLY A N     1 
ATOM   5921  C  CA    . GLY A 1 2196 ? 91.201  109.150 145.096 1.00 28.35  ? 2196 GLY A CA    1 
ATOM   5922  C  C     . GLY A 1 2196 ? 92.242  109.841 144.239 1.00 32.07  ? 2196 GLY A C     1 
ATOM   5923  O  O     . GLY A 1 2196 ? 92.484  109.438 143.098 1.00 33.64  ? 2196 GLY A O     1 
ATOM   5924  N  N     . GLU A 1 2197 ? 92.863  110.886 144.780 1.00 33.56  ? 2197 GLU A N     1 
ATOM   5925  C  CA    . GLU A 1 2197 ? 93.846  111.676 144.051 1.00 30.44  ? 2197 GLU A CA    1 
ATOM   5926  C  C     . GLU A 1 2197 ? 95.281  111.232 144.303 1.00 28.93  ? 2197 GLU A C     1 
ATOM   5927  O  O     . GLU A 1 2197 ? 96.208  111.870 143.794 1.00 28.87  ? 2197 GLU A O     1 
ATOM   5928  C  CB    . GLU A 1 2197 ? 93.699  113.159 144.409 1.00 37.95  ? 2197 GLU A CB    1 
ATOM   5929  C  CG    . GLU A 1 2197 ? 92.260  113.643 144.454 1.00 41.68  ? 2197 GLU A CG    1 
ATOM   5930  C  CD    . GLU A 1 2197 ? 91.536  113.440 143.138 1.00 45.45  ? 2197 GLU A CD    1 
ATOM   5931  O  OE1   . GLU A 1 2197 ? 90.565  112.655 143.106 1.00 49.12  ? 2197 GLU A OE1   1 
ATOM   5932  O  OE2   . GLU A 1 2197 ? 91.937  114.066 142.134 1.00 49.04  ? 2197 GLU A OE2   1 
ATOM   5933  N  N     . GLU A 1 2198 ? 95.489  110.164 145.069 1.00 26.37  ? 2198 GLU A N     1 
ATOM   5934  C  CA    . GLU A 1 2198 ? 96.836  109.674 145.314 1.00 23.66  ? 2198 GLU A CA    1 
ATOM   5935  C  C     . GLU A 1 2198 ? 97.411  109.038 144.049 1.00 21.62  ? 2198 GLU A C     1 
ATOM   5936  O  O     . GLU A 1 2198 ? 96.734  108.884 143.028 1.00 23.70  ? 2198 GLU A O     1 
ATOM   5937  C  CB    . GLU A 1 2198 ? 96.843  108.666 146.462 1.00 22.29  ? 2198 GLU A CB    1 
ATOM   5938  C  CG    . GLU A 1 2198 ? 96.127  109.137 147.714 1.00 24.51  ? 2198 GLU A CG    1 
ATOM   5939  C  CD    . GLU A 1 2198 ? 95.810  107.999 148.663 1.00 30.56  ? 2198 GLU A CD    1 
ATOM   5940  O  OE1   . GLU A 1 2198 ? 95.191  108.255 149.717 1.00 39.82  ? 2198 GLU A OE1   1 
ATOM   5941  O  OE2   . GLU A 1 2198 ? 96.181  106.846 148.355 1.00 26.55  ? 2198 GLU A OE2   1 
ATOM   5942  N  N     . VAL A 1 2199 ? 98.691  108.671 144.127 1.00 19.26  ? 2199 VAL A N     1 
ATOM   5943  C  CA    . VAL A 1 2199 ? 99.344  108.002 143.008 1.00 14.34  ? 2199 VAL A CA    1 
ATOM   5944  C  C     . VAL A 1 2199 ? 98.690  106.644 142.802 1.00 12.82  ? 2199 VAL A C     1 
ATOM   5945  O  O     . VAL A 1 2199 ? 98.653  105.810 143.714 1.00 14.71  ? 2199 VAL A O     1 
ATOM   5946  C  CB    . VAL A 1 2199 ? 100.850 107.873 143.260 1.00 16.38  ? 2199 VAL A CB    1 
ATOM   5947  C  CG1   . VAL A 1 2199 ? 101.526 107.180 142.088 1.00 11.84  ? 2199 VAL A CG1   1 
ATOM   5948  C  CG2   . VAL A 1 2199 ? 101.466 109.243 143.502 1.00 18.55  ? 2199 VAL A CG2   1 
ATOM   5949  N  N     . GLY A 1 2200 ? 98.171  106.415 141.598 1.00 10.37  ? 2200 GLY A N     1 
ATOM   5950  C  CA    . GLY A 1 2200 ? 97.452  105.198 141.295 1.00 9.71   ? 2200 GLY A CA    1 
ATOM   5951  C  C     . GLY A 1 2200 ? 95.961  105.252 141.544 1.00 8.23   ? 2200 GLY A C     1 
ATOM   5952  O  O     . GLY A 1 2200 ? 95.267  104.272 141.246 1.00 8.90   ? 2200 GLY A O     1 
ATOM   5953  N  N     . GLY A 1 2201 ? 95.446  106.361 142.079 1.00 12.77  ? 2201 GLY A N     1 
ATOM   5954  C  CA    . GLY A 1 2201 ? 94.024  106.442 142.372 1.00 11.00  ? 2201 GLY A CA    1 
ATOM   5955  C  C     . GLY A 1 2201 ? 93.155  106.342 141.133 1.00 9.42   ? 2201 GLY A C     1 
ATOM   5956  O  O     . GLY A 1 2201 ? 92.106  105.696 141.152 1.00 9.66   ? 2201 GLY A O     1 
ATOM   5957  N  N     . MET A 1 2202 ? 93.573  106.988 140.042 1.00 9.92   ? 2202 MET A N     1 
ATOM   5958  C  CA    . MET A 1 2202 ? 92.810  106.915 138.798 1.00 8.78   ? 2202 MET A CA    1 
ATOM   5959  C  C     . MET A 1 2202 ? 92.764  105.489 138.263 1.00 6.77   ? 2202 MET A C     1 
ATOM   5960  O  O     . MET A 1 2202 ? 91.719  105.026 137.789 1.00 7.81   ? 2202 MET A O     1 
ATOM   5961  C  CB    . MET A 1 2202 ? 93.413  107.860 137.759 1.00 11.15  ? 2202 MET A CB    1 
ATOM   5962  C  CG    . MET A 1 2202 ? 93.283  109.332 138.110 1.00 17.59  ? 2202 MET A CG    1 
ATOM   5963  S  SD    . MET A 1 2202 ? 94.350  110.389 137.112 1.00 49.02  ? 2202 MET A SD    1 
ATOM   5964  C  CE    . MET A 1 2202 ? 93.580  110.234 135.502 1.00 21.13  ? 2202 MET A CE    1 
ATOM   5965  N  N     . TRP A 1 2203 ? 93.890  104.778 138.330 1.00 5.46   ? 2203 TRP A N     1 
ATOM   5966  C  CA    . TRP A 1 2203 ? 93.926  103.394 137.871 1.00 4.12   ? 2203 TRP A CA    1 
ATOM   5967  C  C     . TRP A 1 2203 ? 93.037  102.506 138.736 1.00 4.20   ? 2203 TRP A C     1 
ATOM   5968  O  O     . TRP A 1 2203 ? 92.354  101.616 138.221 1.00 4.81   ? 2203 TRP A O     1 
ATOM   5969  C  CB    . TRP A 1 2203 ? 95.372  102.895 137.863 1.00 3.57   ? 2203 TRP A CB    1 
ATOM   5970  C  CG    . TRP A 1 2203 ? 95.539  101.464 137.462 1.00 2.88   ? 2203 TRP A CG    1 
ATOM   5971  C  CD1   . TRP A 1 2203 ? 95.569  100.969 136.191 1.00 1.92   ? 2203 TRP A CD1   1 
ATOM   5972  C  CD2   . TRP A 1 2203 ? 95.724  100.343 138.333 1.00 2.42   ? 2203 TRP A CD2   1 
ATOM   5973  N  NE1   . TRP A 1 2203 ? 95.748  99.608  136.217 1.00 2.10   ? 2203 TRP A NE1   1 
ATOM   5974  C  CE2   . TRP A 1 2203 ? 95.847  99.199  137.520 1.00 2.03   ? 2203 TRP A CE2   1 
ATOM   5975  C  CE3   . TRP A 1 2203 ? 95.791  100.194 139.721 1.00 2.34   ? 2203 TRP A CE3   1 
ATOM   5976  C  CZ2   . TRP A 1 2203 ? 96.036  97.925  138.048 1.00 1.84   ? 2203 TRP A CZ2   1 
ATOM   5977  C  CZ3   . TRP A 1 2203 ? 95.978  98.929  140.243 1.00 3.55   ? 2203 TRP A CZ3   1 
ATOM   5978  C  CH2   . TRP A 1 2203 ? 96.098  97.811  139.409 1.00 3.03   ? 2203 TRP A CH2   1 
ATOM   5979  N  N     . VAL A 1 2204 ? 93.025  102.743 140.050 1.00 3.99   ? 2204 VAL A N     1 
ATOM   5980  C  CA    . VAL A 1 2204 ? 92.143  101.998 140.946 1.00 5.83   ? 2204 VAL A CA    1 
ATOM   5981  C  C     . VAL A 1 2204 ? 90.678  102.289 140.632 1.00 5.88   ? 2204 VAL A C     1 
ATOM   5982  O  O     . VAL A 1 2204 ? 89.828  101.388 140.663 1.00 5.28   ? 2204 VAL A O     1 
ATOM   5983  C  CB    . VAL A 1 2204 ? 92.497  102.320 142.409 1.00 7.62   ? 2204 VAL A CB    1 
ATOM   5984  C  CG1   . VAL A 1 2204 ? 91.462  101.749 143.362 1.00 7.46   ? 2204 VAL A CG1   1 
ATOM   5985  C  CG2   . VAL A 1 2204 ? 93.875  101.773 142.740 1.00 6.16   ? 2204 VAL A CG2   1 
ATOM   5986  N  N     . GLU A 1 2205 ? 90.357  103.549 140.335 1.00 6.01   ? 2205 GLU A N     1 
ATOM   5987  C  CA    . GLU A 1 2205 ? 88.999  103.886 139.923 1.00 7.71   ? 2205 GLU A CA    1 
ATOM   5988  C  C     . GLU A 1 2205 ? 88.623  103.164 138.636 1.00 6.26   ? 2205 GLU A C     1 
ATOM   5989  O  O     . GLU A 1 2205 ? 87.491  102.693 138.489 1.00 6.30   ? 2205 GLU A O     1 
ATOM   5990  C  CB    . GLU A 1 2205 ? 88.856  105.398 139.754 1.00 8.66   ? 2205 GLU A CB    1 
ATOM   5991  C  CG    . GLU A 1 2205 ? 88.936  106.170 141.057 1.00 19.96  ? 2205 GLU A CG    1 
ATOM   5992  C  CD    . GLU A 1 2205 ? 87.755  105.889 141.962 1.00 29.68  ? 2205 GLU A CD    1 
ATOM   5993  O  OE1   . GLU A 1 2205 ? 86.655  105.626 141.433 1.00 28.85  ? 2205 GLU A OE1   1 
ATOM   5994  O  OE2   . GLU A 1 2205 ? 87.924  105.928 143.198 1.00 34.65  ? 2205 GLU A OE2   1 
ATOM   5995  N  N     . LYS A 1 2206 ? 89.561  103.072 137.692 1.00 5.63   ? 2206 LYS A N     1 
ATOM   5996  C  CA    . LYS A 1 2206 ? 89.300  102.333 136.461 1.00 4.47   ? 2206 LYS A CA    1 
ATOM   5997  C  C     . LYS A 1 2206 ? 89.090  100.849 136.744 1.00 4.28   ? 2206 LYS A C     1 
ATOM   5998  O  O     . LYS A 1 2206 ? 88.268  100.196 136.093 1.00 5.07   ? 2206 LYS A O     1 
ATOM   5999  C  CB    . LYS A 1 2206 ? 90.444  102.541 135.471 1.00 3.73   ? 2206 LYS A CB    1 
ATOM   6000  C  CG    . LYS A 1 2206 ? 90.407  103.891 134.784 1.00 4.57   ? 2206 LYS A CG    1 
ATOM   6001  C  CD    . LYS A 1 2206 ? 89.106  104.080 134.032 1.00 4.96   ? 2206 LYS A CD    1 
ATOM   6002  C  CE    . LYS A 1 2206 ? 88.913  105.528 133.621 1.00 5.32   ? 2206 LYS A CE    1 
ATOM   6003  N  NZ    . LYS A 1 2206 ? 87.726  105.696 132.739 1.00 3.78   ? 2206 LYS A NZ    1 
ATOM   6004  N  N     . VAL A 1 2207 ? 89.840  100.299 137.702 1.00 5.49   ? 2207 VAL A N     1 
ATOM   6005  C  CA    . VAL A 1 2207 ? 89.624  98.917  138.128 1.00 4.76   ? 2207 VAL A CA    1 
ATOM   6006  C  C     . VAL A 1 2207 ? 88.208  98.726  138.655 1.00 6.13   ? 2207 VAL A C     1 
ATOM   6007  O  O     . VAL A 1 2207 ? 87.514  97.771  138.282 1.00 6.24   ? 2207 VAL A O     1 
ATOM   6008  C  CB    . VAL A 1 2207 ? 90.672  98.512  139.180 1.00 5.62   ? 2207 VAL A CB    1 
ATOM   6009  C  CG1   . VAL A 1 2207 ? 90.391  97.114  139.686 1.00 3.61   ? 2207 VAL A CG1   1 
ATOM   6010  C  CG2   . VAL A 1 2207 ? 92.063  98.575  138.587 1.00 3.56   ? 2207 VAL A CG2   1 
ATOM   6011  N  N     . LEU A 1 2208 ? 87.761  99.622  139.535 1.00 5.05   ? 2208 LEU A N     1 
ATOM   6012  C  CA    . LEU A 1 2208 ? 86.397  99.522  140.051 1.00 5.23   ? 2208 LEU A CA    1 
ATOM   6013  C  C     . LEU A 1 2208 ? 85.377  99.643  138.927 1.00 4.72   ? 2208 LEU A C     1 
ATOM   6014  O  O     . LEU A 1 2208 ? 84.373  98.916  138.901 1.00 6.89   ? 2208 LEU A O     1 
ATOM   6015  C  CB    . LEU A 1 2208 ? 86.154  100.588 141.117 1.00 7.22   ? 2208 LEU A CB    1 
ATOM   6016  C  CG    . LEU A 1 2208 ? 87.051  100.483 142.348 1.00 8.62   ? 2208 LEU A CG    1 
ATOM   6017  C  CD1   . LEU A 1 2208 ? 86.852  101.678 143.258 1.00 19.16  ? 2208 LEU A CD1   1 
ATOM   6018  C  CD2   . LEU A 1 2208 ? 86.791  99.180  143.090 1.00 7.95   ? 2208 LEU A CD2   1 
ATOM   6019  N  N     . GLN A 1 2209 ? 85.621  100.562 137.989 1.00 4.39   ? 2209 GLN A N     1 
ATOM   6020  C  CA    . GLN A 1 2209 ? 84.724  100.729 136.853 1.00 4.70   ? 2209 GLN A CA    1 
ATOM   6021  C  C     . GLN A 1 2209 ? 84.621  99.448  136.039 1.00 4.60   ? 2209 GLN A C     1 
ATOM   6022  O  O     . GLN A 1 2209 ? 83.516  99.008  135.699 1.00 5.82   ? 2209 GLN A O     1 
ATOM   6023  C  CB    . GLN A 1 2209 ? 85.191  101.896 135.983 1.00 4.89   ? 2209 GLN A CB    1 
ATOM   6024  C  CG    . GLN A 1 2209 ? 84.979  103.261 136.629 1.00 5.16   ? 2209 GLN A CG    1 
ATOM   6025  C  CD    . GLN A 1 2209 ? 85.499  104.401 135.779 1.00 6.55   ? 2209 GLN A CD    1 
ATOM   6026  O  OE1   . GLN A 1 2209 ? 86.010  104.185 134.683 1.00 8.04   ? 2209 GLN A OE1   1 
ATOM   6027  N  NE2   . GLN A 1 2209 ? 85.365  105.624 136.278 1.00 9.90   ? 2209 GLN A NE2   1 
ATOM   6028  N  N     . LEU A 1 2210 ? 85.761  98.825  135.735 1.00 4.87   ? 2210 LEU A N     1 
ATOM   6029  C  CA    . LEU A 1 2210 ? 85.749  97.539  135.051 1.00 4.24   ? 2210 LEU A CA    1 
ATOM   6030  C  C     . LEU A 1 2210 ? 84.983  96.501  135.858 1.00 4.35   ? 2210 LEU A C     1 
ATOM   6031  O  O     . LEU A 1 2210 ? 84.273  95.662  135.291 1.00 3.99   ? 2210 LEU A O     1 
ATOM   6032  C  CB    . LEU A 1 2210 ? 87.178  97.067  134.793 1.00 3.83   ? 2210 LEU A CB    1 
ATOM   6033  C  CG    . LEU A 1 2210 ? 87.300  95.649  134.237 1.00 5.37   ? 2210 LEU A CG    1 
ATOM   6034  C  CD1   . LEU A 1 2210 ? 86.811  95.616  132.805 1.00 5.37   ? 2210 LEU A CD1   1 
ATOM   6035  C  CD2   . LEU A 1 2210 ? 88.725  95.147  134.334 1.00 2.77   ? 2210 LEU A CD2   1 
ATOM   6036  N  N     . TYR A 1 2211 ? 85.110  96.550  137.186 1.00 4.92   ? 2211 TYR A N     1 
ATOM   6037  C  CA    . TYR A 1 2211 ? 84.373  95.613  138.025 1.00 4.66   ? 2211 TYR A CA    1 
ATOM   6038  C  C     . TYR A 1 2211 ? 82.871  95.746  137.827 1.00 5.99   ? 2211 TYR A C     1 
ATOM   6039  O  O     . TYR A 1 2211 ? 82.182  94.741  137.619 1.00 6.60   ? 2211 TYR A O     1 
ATOM   6040  C  CB    . TYR A 1 2211 ? 84.718  95.810  139.499 1.00 5.05   ? 2211 TYR A CB    1 
ATOM   6041  C  CG    . TYR A 1 2211 ? 83.898  94.917  140.405 1.00 6.93   ? 2211 TYR A CG    1 
ATOM   6042  C  CD1   . TYR A 1 2211 ? 83.886  93.540  140.231 1.00 8.90   ? 2211 TYR A CD1   1 
ATOM   6043  C  CD2   . TYR A 1 2211 ? 83.107  95.455  141.411 1.00 9.62   ? 2211 TYR A CD2   1 
ATOM   6044  C  CE1   . TYR A 1 2211 ? 83.128  92.724  141.049 1.00 10.33  ? 2211 TYR A CE1   1 
ATOM   6045  C  CE2   . TYR A 1 2211 ? 82.349  94.646  142.235 1.00 10.38  ? 2211 TYR A CE2   1 
ATOM   6046  C  CZ    . TYR A 1 2211 ? 82.364  93.281  142.050 1.00 14.64  ? 2211 TYR A CZ    1 
ATOM   6047  O  OH    . TYR A 1 2211 ? 81.608  92.473  142.866 1.00 19.77  ? 2211 TYR A OH    1 
ATOM   6048  N  N     . GLN A 1 2212 ? 82.332  96.967  137.896 1.00 5.00   ? 2212 GLN A N     1 
ATOM   6049  C  CA    . GLN A 1 2212 ? 80.874  97.046  137.787 1.00 8.17   ? 2212 GLN A CA    1 
ATOM   6050  C  C     . GLN A 1 2212 ? 80.421  96.888  136.339 1.00 9.20   ? 2212 GLN A C     1 
ATOM   6051  O  O     . GLN A 1 2212 ? 79.247  96.600  136.083 1.00 10.46  ? 2212 GLN A O     1 
ATOM   6052  C  CB    . GLN A 1 2212 ? 80.262  98.321  138.386 1.00 15.45  ? 2212 GLN A CB    1 
ATOM   6053  C  CG    . GLN A 1 2212 ? 80.439  99.645  137.667 1.00 16.71  ? 2212 GLN A CG    1 
ATOM   6054  C  CD    . GLN A 1 2212 ? 81.603  100.466 138.146 1.00 19.45  ? 2212 GLN A CD    1 
ATOM   6055  O  OE1   . GLN A 1 2212 ? 82.226  100.152 139.153 1.00 24.72  ? 2212 GLN A OE1   1 
ATOM   6056  N  NE2   . GLN A 1 2212 ? 81.849  101.580 137.469 1.00 14.26  ? 2212 GLN A NE2   1 
ATOM   6057  N  N     . ILE A 1 2213 ? 81.326  97.077  135.374 1.00 8.57   ? 2213 ILE A N     1 
ATOM   6058  C  CA    . ILE A 1 2213 ? 80.992  96.699  134.002 1.00 7.49   ? 2213 ILE A CA    1 
ATOM   6059  C  C     . ILE A 1 2213 ? 80.867  95.183  133.883 1.00 8.52   ? 2213 ILE A C     1 
ATOM   6060  O  O     . ILE A 1 2213 ? 79.990  94.674  133.175 1.00 7.71   ? 2213 ILE A O     1 
ATOM   6061  C  CB    . ILE A 1 2213 ? 82.014  97.270  133.003 1.00 7.36   ? 2213 ILE A CB    1 
ATOM   6062  C  CG1   . ILE A 1 2213 ? 82.065  98.793  133.097 1.00 7.78   ? 2213 ILE A CG1   1 
ATOM   6063  C  CG2   . ILE A 1 2213 ? 81.656  96.872  131.582 1.00 7.16   ? 2213 ILE A CG2   1 
ATOM   6064  C  CD1   . ILE A 1 2213 ? 80.825  99.469  132.569 1.00 8.65   ? 2213 ILE A CD1   1 
ATOM   6065  N  N     . THR A 1 2214 ? 81.733  94.437  134.577 1.00 7.72   ? 2214 THR A N     1 
ATOM   6066  C  CA    . THR A 1 2214 ? 81.671  92.978  134.504 1.00 7.14   ? 2214 THR A CA    1 
ATOM   6067  C  C     . THR A 1 2214 ? 80.378  92.433  135.098 1.00 9.32   ? 2214 THR A C     1 
ATOM   6068  O  O     . THR A 1 2214 ? 79.964  91.319  134.761 1.00 10.17  ? 2214 THR A O     1 
ATOM   6069  C  CB    . THR A 1 2214 ? 82.872  92.351  135.215 1.00 4.88   ? 2214 THR A CB    1 
ATOM   6070  O  OG1   . THR A 1 2214 ? 82.988  92.888  136.539 1.00 7.90   ? 2214 THR A OG1   1 
ATOM   6071  C  CG2   . THR A 1 2214 ? 84.155  92.617  134.445 1.00 4.49   ? 2214 THR A CG2   1 
ATOM   6072  N  N     . GLN A 1 2215 ? 79.732  93.191  135.982 1.00 9.95   ? 2215 GLN A N     1 
ATOM   6073  C  CA    . GLN A 1 2215 ? 78.498  92.747  136.615 1.00 9.93   ? 2215 GLN A CA    1 
ATOM   6074  C  C     . GLN A 1 2215 ? 77.250  93.079  135.808 1.00 11.96  ? 2215 GLN A C     1 
ATOM   6075  O  O     . GLN A 1 2215 ? 76.157  92.647  136.187 1.00 21.78  ? 2215 GLN A O     1 
ATOM   6076  C  CB    . GLN A 1 2215 ? 78.369  93.361  138.014 1.00 10.71  ? 2215 GLN A CB    1 
ATOM   6077  C  CG    . GLN A 1 2215 ? 79.484  92.980  138.971 1.00 12.32  ? 2215 GLN A CG    1 
ATOM   6078  C  CD    . GLN A 1 2215 ? 79.523  93.868  140.199 1.00 18.27  ? 2215 GLN A CD    1 
ATOM   6079  O  OE1   . GLN A 1 2215 ? 79.781  95.067  140.105 1.00 24.38  ? 2215 GLN A OE1   1 
ATOM   6080  N  NE2   . GLN A 1 2215 ? 79.261  93.282  141.362 1.00 17.62  ? 2215 GLN A NE2   1 
ATOM   6081  N  N     . ILE A 1 2216 ? 77.378  93.829  134.715 1.00 11.44  ? 2216 ILE A N     1 
ATOM   6082  C  CA    . ILE A 1 2216 ? 76.213  94.263  133.952 1.00 13.56  ? 2216 ILE A CA    1 
ATOM   6083  C  C     . ILE A 1 2216 ? 76.303  93.746  132.521 1.00 12.89  ? 2216 ILE A C     1 
ATOM   6084  O  O     . ILE A 1 2216 ? 75.280  93.477  131.881 1.00 17.60  ? 2216 ILE A O     1 
ATOM   6085  C  CB    . ILE A 1 2216 ? 76.082  95.799  133.999 1.00 11.64  ? 2216 ILE A CB    1 
ATOM   6086  C  CG1   . ILE A 1 2216 ? 75.674  96.246  135.404 1.00 19.16  ? 2216 ILE A CG1   1 
ATOM   6087  C  CG2   . ILE A 1 2216 ? 75.073  96.303  132.979 1.00 16.76  ? 2216 ILE A CG2   1 
ATOM   6088  C  CD1   . ILE A 1 2216 ? 76.093  97.654  135.748 1.00 23.70  ? 2216 ILE A CD1   1 
ATOM   6089  N  N     . ASN A 1 2217 ? 77.521  93.565  132.020 1.00 9.66   ? 2217 ASN A N     1 
ATOM   6090  C  CA    . ASN A 1 2217 ? 77.739  93.118  130.652 1.00 9.02   ? 2217 ASN A CA    1 
ATOM   6091  C  C     . ASN A 1 2217 ? 78.487  91.794  130.640 1.00 7.96   ? 2217 ASN A C     1 
ATOM   6092  O  O     . ASN A 1 2217 ? 79.444  91.601  131.396 1.00 13.54  ? 2217 ASN A O     1 
ATOM   6093  C  CB    . ASN A 1 2217 ? 78.526  94.157  129.842 1.00 9.13   ? 2217 ASN A CB    1 
ATOM   6094  C  CG    . ASN A 1 2217 ? 77.980  95.560  130.002 1.00 12.24  ? 2217 ASN A CG    1 
ATOM   6095  O  OD1   . ASN A 1 2217 ? 78.011  96.132  131.090 1.00 20.28  ? 2217 ASN A OD1   1 
ATOM   6096  N  ND2   . ASN A 1 2217 ? 77.473  96.122  128.912 1.00 13.09  ? 2217 ASN A ND2   1 
ATOM   6097  N  N     . HIS A 1 2218 ? 78.037  90.881  129.780 1.00 7.17   ? 2218 HIS A N     1 
ATOM   6098  C  CA    . HIS A 1 2218 ? 78.783  89.670  129.473 1.00 5.05   ? 2218 HIS A CA    1 
ATOM   6099  C  C     . HIS A 1 2218 ? 79.792  89.881  128.353 1.00 5.57   ? 2218 HIS A C     1 
ATOM   6100  O  O     . HIS A 1 2218 ? 80.628  89.003  128.117 1.00 5.24   ? 2218 HIS A O     1 
ATOM   6101  C  CB    . HIS A 1 2218 ? 77.823  88.537  129.095 1.00 4.21   ? 2218 HIS A CB    1 
ATOM   6102  C  CG    . HIS A 1 2218 ? 76.980  88.836  127.894 1.00 5.50   ? 2218 HIS A CG    1 
ATOM   6103  N  ND1   . HIS A 1 2218 ? 75.740  89.430  127.986 1.00 8.23   ? 2218 HIS A ND1   1 
ATOM   6104  C  CD2   . HIS A 1 2218 ? 77.196  88.617  126.576 1.00 4.81   ? 2218 HIS A CD2   1 
ATOM   6105  C  CE1   . HIS A 1 2218 ? 75.231  89.570  126.775 1.00 7.63   ? 2218 HIS A CE1   1 
ATOM   6106  N  NE2   . HIS A 1 2218 ? 76.094  89.083  125.902 1.00 6.64   ? 2218 HIS A NE2   1 
ATOM   6107  N  N     . GLY A 1 2219 ? 79.731  91.020  127.669 1.00 5.14   ? 2219 GLY A N     1 
ATOM   6108  C  CA    . GLY A 1 2219 ? 80.693  91.381  126.648 1.00 4.66   ? 2219 GLY A CA    1 
ATOM   6109  C  C     . GLY A 1 2219 ? 81.148  92.814  126.824 1.00 5.62   ? 2219 GLY A C     1 
ATOM   6110  O  O     . GLY A 1 2219 ? 80.326  93.736  126.850 1.00 7.00   ? 2219 GLY A O     1 
ATOM   6111  N  N     . LEU A 1 2220 ? 82.455  93.021  126.950 1.00 3.69   ? 2220 LEU A N     1 
ATOM   6112  C  CA    . LEU A 1 2220 ? 82.969  94.322  127.345 1.00 4.03   ? 2220 LEU A CA    1 
ATOM   6113  C  C     . LEU A 1 2220 ? 84.375  94.512  126.797 1.00 5.10   ? 2220 LEU A C     1 
ATOM   6114  O  O     . LEU A 1 2220 ? 85.130  93.555  126.611 1.00 5.24   ? 2220 LEU A O     1 
ATOM   6115  C  CB    . LEU A 1 2220 ? 82.946  94.482  128.871 1.00 4.59   ? 2220 LEU A CB    1 
ATOM   6116  C  CG    . LEU A 1 2220 ? 83.965  93.695  129.699 1.00 4.39   ? 2220 LEU A CG    1 
ATOM   6117  C  CD1   . LEU A 1 2220 ? 84.043  94.249  131.097 1.00 6.02   ? 2220 LEU A CD1   1 
ATOM   6118  C  CD2   . LEU A 1 2220 ? 83.581  92.228  129.764 1.00 5.73   ? 2220 LEU A CD2   1 
ATOM   6119  N  N     . MET A 1 2221 ? 84.713  95.773  126.540 1.00 5.14   ? 2221 MET A N     1 
ATOM   6120  C  CA    . MET A 1 2221 ? 86.016  96.172  126.034 1.00 3.38   ? 2221 MET A CA    1 
ATOM   6121  C  C     . MET A 1 2221 ? 86.669  97.201  126.943 1.00 3.88   ? 2221 MET A C     1 
ATOM   6122  O  O     . MET A 1 2221 ? 86.003  98.089  127.491 1.00 5.31   ? 2221 MET A O     1 
ATOM   6123  C  CB    . MET A 1 2221 ? 85.933  96.744  124.613 1.00 4.79   ? 2221 MET A CB    1 
ATOM   6124  C  CG    . MET A 1 2221 ? 85.555  95.734  123.564 1.00 7.16   ? 2221 MET A CG    1 
ATOM   6125  S  SD    . MET A 1 2221 ? 85.457  96.397  121.895 1.00 20.37  ? 2221 MET A SD    1 
ATOM   6126  C  CE    . MET A 1 2221 ? 84.918  94.930  121.025 1.00 9.45   ? 2221 MET A CE    1 
ATOM   6127  N  N     . MET A 1 2222 ? 87.980  97.056  127.095 1.00 4.68   ? 2222 MET A N     1 
ATOM   6128  C  CA    . MET A 1 2222 ? 88.838  98.041  127.739 1.00 3.67   ? 2222 MET A CA    1 
ATOM   6129  C  C     . MET A 1 2222 ? 89.702  98.675  126.656 1.00 3.13   ? 2222 MET A C     1 
ATOM   6130  O  O     . MET A 1 2222 ? 90.616  98.034  126.126 1.00 4.20   ? 2222 MET A O     1 
ATOM   6131  C  CB    . MET A 1 2222 ? 89.684  97.373  128.817 1.00 3.58   ? 2222 MET A CB    1 
ATOM   6132  C  CG    . MET A 1 2222 ? 88.876  96.857  129.981 1.00 9.31   ? 2222 MET A CG    1 
ATOM   6133  S  SD    . MET A 1 2222 ? 89.922  96.125  131.242 1.00 33.57  ? 2222 MET A SD    1 
ATOM   6134  C  CE    . MET A 1 2222 ? 90.337  94.595  130.417 1.00 3.04   ? 2222 MET A CE    1 
ATOM   6135  N  N     . VAL A 1 2223 ? 89.416  99.930  126.330 1.00 3.74   ? 2223 VAL A N     1 
ATOM   6136  C  CA    . VAL A 1 2223 ? 90.023  100.609 125.191 1.00 2.73   ? 2223 VAL A CA    1 
ATOM   6137  C  C     . VAL A 1 2223 ? 90.922  101.718 125.710 1.00 3.33   ? 2223 VAL A C     1 
ATOM   6138  O  O     . VAL A 1 2223 ? 90.485  102.558 126.502 1.00 5.60   ? 2223 VAL A O     1 
ATOM   6139  C  CB    . VAL A 1 2223 ? 88.955  101.171 124.236 1.00 3.09   ? 2223 VAL A CB    1 
ATOM   6140  C  CG1   . VAL A 1 2223 ? 89.605  101.720 122.971 1.00 3.56   ? 2223 VAL A CG1   1 
ATOM   6141  C  CG2   . VAL A 1 2223 ? 87.934  100.097 123.903 1.00 4.26   ? 2223 VAL A CG2   1 
ATOM   6142  N  N     . GLY A 1 2224 ? 92.174  101.720 125.266 1.00 2.86   ? 2224 GLY A N     1 
ATOM   6143  C  CA    . GLY A 1 2224 ? 93.118  102.728 125.679 1.00 2.98   ? 2224 GLY A CA    1 
ATOM   6144  C  C     . GLY A 1 2224 ? 94.480  102.540 125.050 1.00 4.63   ? 2224 GLY A C     1 
ATOM   6145  O  O     . GLY A 1 2224 ? 94.889  101.422 124.727 1.00 5.96   ? 2224 GLY A O     1 
ATOM   6146  N  N     . PRO A 1 2225 ? 95.219  103.637 124.887 1.00 7.73   ? 2225 PRO A N     1 
ATOM   6147  C  CA    . PRO A 1 2225 ? 96.517  103.566 124.207 1.00 5.70   ? 2225 PRO A CA    1 
ATOM   6148  C  C     . PRO A 1 2225 ? 97.469  102.604 124.900 1.00 5.40   ? 2225 PRO A C     1 
ATOM   6149  O  O     . PRO A 1 2225 ? 97.333  102.291 126.085 1.00 5.29   ? 2225 PRO A O     1 
ATOM   6150  C  CB    . PRO A 1 2225 ? 97.035  105.009 124.274 1.00 7.61   ? 2225 PRO A CB    1 
ATOM   6151  C  CG    . PRO A 1 2225 ? 96.262  105.641 125.391 1.00 6.94   ? 2225 PRO A CG    1 
ATOM   6152  C  CD    . PRO A 1 2225 ? 94.910  105.005 125.332 1.00 5.56   ? 2225 PRO A CD    1 
ATOM   6153  N  N     . SER A 1 2226 ? 98.438  102.119 124.126 1.00 6.92   ? 2226 SER A N     1 
ATOM   6154  C  CA    . SER A 1 2226 ? 99.366  101.111 124.619 1.00 5.68   ? 2226 SER A CA    1 
ATOM   6155  C  C     . SER A 1 2226 ? 100.103 101.616 125.853 1.00 4.91   ? 2226 SER A C     1 
ATOM   6156  O  O     . SER A 1 2226 ? 100.686 102.704 125.844 1.00 7.17   ? 2226 SER A O     1 
ATOM   6157  C  CB    . SER A 1 2226 ? 100.357 100.733 123.520 1.00 6.41   ? 2226 SER A CB    1 
ATOM   6158  O  OG    . SER A 1 2226 ? 101.312 99.803  123.991 1.00 5.71   ? 2226 SER A OG    1 
ATOM   6159  N  N     . GLY A 1 2227 ? 100.073 100.818 126.916 1.00 3.80   ? 2227 GLY A N     1 
ATOM   6160  C  CA    . GLY A 1 2227 ? 100.679 101.209 128.169 1.00 2.99   ? 2227 GLY A CA    1 
ATOM   6161  C  C     . GLY A 1 2227 ? 99.792  102.005 129.095 1.00 3.32   ? 2227 GLY A C     1 
ATOM   6162  O  O     . GLY A 1 2227 ? 100.278 102.926 129.761 1.00 5.45   ? 2227 GLY A O     1 
ATOM   6163  N  N     . SER A 1 2228 ? 98.503  101.683 129.162 1.00 4.91   ? 2228 SER A N     1 
ATOM   6164  C  CA    . SER A 1 2228 ? 97.562  102.397 130.013 1.00 3.37   ? 2228 SER A CA    1 
ATOM   6165  C  C     . SER A 1 2228 ? 97.202  101.634 131.281 1.00 2.81   ? 2228 SER A C     1 
ATOM   6166  O  O     . SER A 1 2228 ? 96.271  102.039 131.984 1.00 4.49   ? 2228 SER A O     1 
ATOM   6167  C  CB    . SER A 1 2228 ? 96.287  102.722 129.228 1.00 3.10   ? 2228 SER A CB    1 
ATOM   6168  O  OG    . SER A 1 2228 ? 96.558  103.616 128.164 1.00 6.39   ? 2228 SER A OG    1 
ATOM   6169  N  N     . GLY A 1 2229 ? 97.906  100.549 131.589 1.00 1.70   ? 2229 GLY A N     1 
ATOM   6170  C  CA    . GLY A 1 2229 ? 97.587  99.746  132.753 1.00 1.60   ? 2229 GLY A CA    1 
ATOM   6171  C  C     . GLY A 1 2229 ? 96.378  98.854  132.602 1.00 1.23   ? 2229 GLY A C     1 
ATOM   6172  O  O     . GLY A 1 2229 ? 95.814  98.424  133.614 1.00 1.37   ? 2229 GLY A O     1 
ATOM   6173  N  N     . LYS A 1 2230 ? 95.960  98.565  131.370 1.00 1.69   ? 2230 LYS A N     1 
ATOM   6174  C  CA    . LYS A 1 2230 ? 94.737  97.802  131.141 1.00 1.40   ? 2230 LYS A CA    1 
ATOM   6175  C  C     . LYS A 1 2230 ? 94.904  96.338  131.546 1.00 1.97   ? 2230 LYS A C     1 
ATOM   6176  O  O     . LYS A 1 2230 ? 94.065  95.779  132.271 1.00 2.83   ? 2230 LYS A O     1 
ATOM   6177  C  CB    . LYS A 1 2230 ? 94.348  97.923  129.667 1.00 1.01   ? 2230 LYS A CB    1 
ATOM   6178  C  CG    . LYS A 1 2230 ? 94.204  99.363  129.199 1.00 1.97   ? 2230 LYS A CG    1 
ATOM   6179  C  CD    . LYS A 1 2230 ? 93.723  99.454  127.760 1.00 2.16   ? 2230 LYS A CD    1 
ATOM   6180  C  CE    . LYS A 1 2230 ? 94.699  98.781  126.804 1.00 2.03   ? 2230 LYS A CE    1 
ATOM   6181  N  NZ    . LYS A 1 2230 ? 96.010  99.482  126.738 1.00 2.60   ? 2230 LYS A NZ    1 
ATOM   6182  N  N     . SER A 1 2231 ? 95.985  95.701  131.083 1.00 2.00   ? 2231 SER A N     1 
ATOM   6183  C  CA    . SER A 1 2231 ? 96.207  94.289  131.383 1.00 1.78   ? 2231 SER A CA    1 
ATOM   6184  C  C     . SER A 1 2231 ? 96.363  94.071  132.879 1.00 2.31   ? 2231 SER A C     1 
ATOM   6185  O  O     . SER A 1 2231 ? 95.766  93.150  133.452 1.00 2.29   ? 2231 SER A O     1 
ATOM   6186  C  CB    . SER A 1 2231 ? 97.444  93.777  130.646 1.00 2.25   ? 2231 SER A CB    1 
ATOM   6187  O  OG    . SER A 1 2231 ? 97.351  94.000  129.255 1.00 5.28   ? 2231 SER A OG    1 
ATOM   6188  N  N     . MET A 1 2232 ? 97.172  94.913  133.526 1.00 2.27   ? 2232 MET A N     1 
ATOM   6189  C  CA    . MET A 1 2232 ? 97.319  94.830  134.972 1.00 2.44   ? 2232 MET A CA    1 
ATOM   6190  C  C     . MET A 1 2232 ? 95.985  95.059  135.661 1.00 1.93   ? 2232 MET A C     1 
ATOM   6191  O  O     . MET A 1 2232 ? 95.670  94.392  136.650 1.00 2.26   ? 2232 MET A O     1 
ATOM   6192  C  CB    . MET A 1 2232 ? 98.357  95.842  135.456 1.00 2.31   ? 2232 MET A CB    1 
ATOM   6193  C  CG    . MET A 1 2232 ? 99.794  95.423  135.204 1.00 4.54   ? 2232 MET A CG    1 
ATOM   6194  S  SD    . MET A 1 2232 ? 100.087 93.690  135.607 1.00 14.02  ? 2232 MET A SD    1 
ATOM   6195  C  CE    . MET A 1 2232 ? 101.827 93.731  136.024 1.00 15.35  ? 2232 MET A CE    1 
ATOM   6196  N  N     . ALA A 1 2233 ? 95.175  95.979  135.133 1.00 1.80   ? 2233 ALA A N     1 
ATOM   6197  C  CA    . ALA A 1 2233 ? 93.870  96.240  135.727 1.00 1.74   ? 2233 ALA A CA    1 
ATOM   6198  C  C     . ALA A 1 2233 ? 93.015  94.980  135.750 1.00 2.09   ? 2233 ALA A C     1 
ATOM   6199  O  O     . ALA A 1 2233 ? 92.517  94.576  136.809 1.00 2.47   ? 2233 ALA A O     1 
ATOM   6200  C  CB    . ALA A 1 2233 ? 93.159  97.359  134.969 1.00 1.66   ? 2233 ALA A CB    1 
ATOM   6201  N  N     . TRP A 1 2234 ? 92.851  94.322  134.597 1.00 2.23   ? 2234 TRP A N     1 
ATOM   6202  C  CA    . TRP A 1 2234 ? 91.948  93.173  134.599 1.00 1.71   ? 2234 TRP A CA    1 
ATOM   6203  C  C     . TRP A 1 2234 ? 92.557  91.974  135.318 1.00 1.84   ? 2234 TRP A C     1 
ATOM   6204  O  O     . TRP A 1 2234 ? 91.831  91.223  135.977 1.00 2.17   ? 2234 TRP A O     1 
ATOM   6205  C  CB    . TRP A 1 2234 ? 91.509  92.806  133.177 1.00 1.89   ? 2234 TRP A CB    1 
ATOM   6206  C  CG    . TRP A 1 2234 ? 92.535  92.180  132.281 1.00 1.99   ? 2234 TRP A CG    1 
ATOM   6207  C  CD1   . TRP A 1 2234 ? 93.206  92.785  131.264 1.00 1.64   ? 2234 TRP A CD1   1 
ATOM   6208  C  CD2   . TRP A 1 2234 ? 92.951  90.808  132.274 1.00 1.58   ? 2234 TRP A CD2   1 
ATOM   6209  N  NE1   . TRP A 1 2234 ? 94.043  91.889  130.646 1.00 2.16   ? 2234 TRP A NE1   1 
ATOM   6210  C  CE2   . TRP A 1 2234 ? 93.904  90.667  131.247 1.00 2.03   ? 2234 TRP A CE2   1 
ATOM   6211  C  CE3   . TRP A 1 2234 ? 92.623  89.691  133.047 1.00 1.32   ? 2234 TRP A CE3   1 
ATOM   6212  C  CZ2   . TRP A 1 2234 ? 94.532  89.454  130.973 1.00 2.81   ? 2234 TRP A CZ2   1 
ATOM   6213  C  CZ3   . TRP A 1 2234 ? 93.249  88.492  132.777 1.00 1.91   ? 2234 TRP A CZ3   1 
ATOM   6214  C  CH2   . TRP A 1 2234 ? 94.191  88.381  131.747 1.00 2.60   ? 2234 TRP A CH2   1 
ATOM   6215  N  N     . ARG A 1 2235 ? 93.879  91.788  135.235 1.00 1.81   ? 2235 ARG A N     1 
ATOM   6216  C  CA    . ARG A 1 2235 ? 94.506  90.680  135.950 1.00 1.80   ? 2235 ARG A CA    1 
ATOM   6217  C  C     . ARG A 1 2235 ? 94.370  90.846  137.460 1.00 3.00   ? 2235 ARG A C     1 
ATOM   6218  O  O     . ARG A 1 2235 ? 94.048  89.887  138.179 1.00 6.96   ? 2235 ARG A O     1 
ATOM   6219  C  CB    . ARG A 1 2235 ? 95.978  90.580  135.552 1.00 2.58   ? 2235 ARG A CB    1 
ATOM   6220  C  CG    . ARG A 1 2235 ? 96.202  90.040  134.150 1.00 4.55   ? 2235 ARG A CG    1 
ATOM   6221  C  CD    . ARG A 1 2235 ? 97.681  90.022  133.794 1.00 8.88   ? 2235 ARG A CD    1 
ATOM   6222  N  NE    . ARG A 1 2235 ? 97.963  89.244  132.593 1.00 17.24  ? 2235 ARG A NE    1 
ATOM   6223  C  CZ    . ARG A 1 2235 ? 97.827  87.928  132.491 1.00 17.85  ? 2235 ARG A CZ    1 
ATOM   6224  N  NH1   . ARG A 1 2235 ? 97.432  87.190  133.516 1.00 16.82  ? 2235 ARG A NH1   1 
ATOM   6225  N  NH2   . ARG A 1 2235 ? 98.102  87.336  131.333 1.00 14.40  ? 2235 ARG A NH2   1 
ATOM   6226  N  N     . VAL A 1 2236 ? 94.596  92.063  137.957 1.00 2.13   ? 2236 VAL A N     1 
ATOM   6227  C  CA    . VAL A 1 2236 ? 94.490  92.326  139.384 1.00 2.49   ? 2236 VAL A CA    1 
ATOM   6228  C  C     . VAL A 1 2236 ? 93.042  92.222  139.837 1.00 2.80   ? 2236 VAL A C     1 
ATOM   6229  O  O     . VAL A 1 2236 ? 92.760  91.735  140.936 1.00 3.57   ? 2236 VAL A O     1 
ATOM   6230  C  CB    . VAL A 1 2236 ? 95.102  93.701  139.704 1.00 3.59   ? 2236 VAL A CB    1 
ATOM   6231  C  CG1   . VAL A 1 2236 ? 94.707  94.170  141.093 1.00 3.79   ? 2236 VAL A CG1   1 
ATOM   6232  C  CG2   . VAL A 1 2236 ? 96.600  93.647  139.546 1.00 5.41   ? 2236 VAL A CG2   1 
ATOM   6233  N  N     . LEU A 1 2237 ? 92.099  92.665  138.999 1.00 2.41   ? 2237 LEU A N     1 
ATOM   6234  C  CA    . LEU A 1 2237 ? 90.692  92.483  139.336 1.00 2.18   ? 2237 LEU A CA    1 
ATOM   6235  C  C     . LEU A 1 2237 ? 90.339  91.004  139.429 1.00 2.71   ? 2237 LEU A C     1 
ATOM   6236  O  O     . LEU A 1 2237 ? 89.605  90.592  140.332 1.00 3.11   ? 2237 LEU A O     1 
ATOM   6237  C  CB    . LEU A 1 2237 ? 89.802  93.184  138.310 1.00 2.19   ? 2237 LEU A CB    1 
ATOM   6238  C  CG    . LEU A 1 2237 ? 88.295  93.005  138.526 1.00 2.86   ? 2237 LEU A CG    1 
ATOM   6239  C  CD1   . LEU A 1 2237 ? 87.876  93.526  139.893 1.00 2.45   ? 2237 LEU A CD1   1 
ATOM   6240  C  CD2   . LEU A 1 2237 ? 87.501  93.687  137.427 1.00 2.57   ? 2237 LEU A CD2   1 
ATOM   6241  N  N     . LEU A 1 2238 ? 90.858  90.189  138.507 1.00 2.81   ? 2238 LEU A N     1 
ATOM   6242  C  CA    . LEU A 1 2238 ? 90.600  88.752  138.553 1.00 2.55   ? 2238 LEU A CA    1 
ATOM   6243  C  C     . LEU A 1 2238 ? 91.131  88.139  139.843 1.00 4.20   ? 2238 LEU A C     1 
ATOM   6244  O  O     . LEU A 1 2238 ? 90.430  87.373  140.517 1.00 6.39   ? 2238 LEU A O     1 
ATOM   6245  C  CB    . LEU A 1 2238 ? 91.224  88.071  137.334 1.00 2.54   ? 2238 LEU A CB    1 
ATOM   6246  C  CG    . LEU A 1 2238 ? 90.829  86.616  137.070 1.00 2.10   ? 2238 LEU A CG    1 
ATOM   6247  C  CD1   . LEU A 1 2238 ? 89.328  86.492  136.876 1.00 2.25   ? 2238 LEU A CD1   1 
ATOM   6248  C  CD2   . LEU A 1 2238 ? 91.575  86.064  135.865 1.00 1.27   ? 2238 LEU A CD2   1 
ATOM   6249  N  N     . LYS A 1 2239 ? 92.371  88.476  140.210 1.00 3.86   ? 2239 LYS A N     1 
ATOM   6250  C  CA    . LYS A 1 2239 ? 92.939  87.931  141.444 1.00 5.24   ? 2239 LYS A CA    1 
ATOM   6251  C  C     . LYS A 1 2239 ? 92.174  88.412  142.675 1.00 5.64   ? 2239 LYS A C     1 
ATOM   6252  O  O     . LYS A 1 2239 ? 91.933  87.637  143.612 1.00 7.04   ? 2239 LYS A O     1 
ATOM   6253  C  CB    . LYS A 1 2239 ? 94.419  88.295  141.555 1.00 6.39   ? 2239 LYS A CB    1 
ATOM   6254  C  CG    . LYS A 1 2239 ? 95.317  87.512  140.616 1.00 12.04  ? 2239 LYS A CG    1 
ATOM   6255  C  CD    . LYS A 1 2239 ? 96.734  88.057  140.622 1.00 16.68  ? 2239 LYS A CD    1 
ATOM   6256  C  CE    . LYS A 1 2239 ? 97.669  87.162  139.826 1.00 19.08  ? 2239 LYS A CE    1 
ATOM   6257  N  NZ    . LYS A 1 2239 ? 98.623  87.949  139.000 1.00 25.03  ? 2239 LYS A NZ    1 
ATOM   6258  N  N     . ALA A 1 2240 ? 91.787  89.689  142.694 1.00 4.45   ? 2240 ALA A N     1 
ATOM   6259  C  CA    . ALA A 1 2240 ? 91.054  90.225  143.835 1.00 4.44   ? 2240 ALA A CA    1 
ATOM   6260  C  C     . ALA A 1 2240 ? 89.689  89.567  143.973 1.00 5.02   ? 2240 ALA A C     1 
ATOM   6261  O  O     . ALA A 1 2240 ? 89.242  89.289  145.089 1.00 7.65   ? 2240 ALA A O     1 
ATOM   6262  C  CB    . ALA A 1 2240 ? 90.910  91.739  143.706 1.00 4.77   ? 2240 ALA A CB    1 
ATOM   6263  N  N     . LEU A 1 2241 ? 89.005  89.324  142.853 1.00 5.04   ? 2241 LEU A N     1 
ATOM   6264  C  CA    . LEU A 1 2241 ? 87.735  88.609  142.909 1.00 4.89   ? 2241 LEU A CA    1 
ATOM   6265  C  C     . LEU A 1 2241 ? 87.932  87.176  143.382 1.00 6.74   ? 2241 LEU A C     1 
ATOM   6266  O  O     . LEU A 1 2241 ? 87.110  86.652  144.143 1.00 8.28   ? 2241 LEU A O     1 
ATOM   6267  C  CB    . LEU A 1 2241 ? 87.047  88.637  141.546 1.00 4.14   ? 2241 LEU A CB    1 
ATOM   6268  C  CG    . LEU A 1 2241 ? 86.612  90.026  141.086 1.00 4.17   ? 2241 LEU A CG    1 
ATOM   6269  C  CD1   . LEU A 1 2241 ? 86.063  89.990  139.669 1.00 3.00   ? 2241 LEU A CD1   1 
ATOM   6270  C  CD2   . LEU A 1 2241 ? 85.592  90.588  142.057 1.00 7.65   ? 2241 LEU A CD2   1 
ATOM   6271  N  N     . GLU A 1 2242 ? 89.016  86.530  142.947 1.00 7.64   ? 2242 GLU A N     1 
ATOM   6272  C  CA    . GLU A 1 2242 ? 89.306  85.183  143.427 1.00 9.19   ? 2242 GLU A CA    1 
ATOM   6273  C  C     . GLU A 1 2242 ? 89.478  85.165  144.940 1.00 10.02  ? 2242 GLU A C     1 
ATOM   6274  O  O     . GLU A 1 2242 ? 88.973  84.263  145.620 1.00 11.43  ? 2242 GLU A O     1 
ATOM   6275  C  CB    . GLU A 1 2242 ? 90.558  84.638  142.740 1.00 12.17  ? 2242 GLU A CB    1 
ATOM   6276  C  CG    . GLU A 1 2242 ? 90.935  83.232  143.174 1.00 13.34  ? 2242 GLU A CG    1 
ATOM   6277  C  CD    . GLU A 1 2242 ? 91.671  82.466  142.093 1.00 28.56  ? 2242 GLU A CD    1 
ATOM   6278  O  OE1   . GLU A 1 2242 ? 91.857  83.022  140.990 1.00 24.52  ? 2242 GLU A OE1   1 
ATOM   6279  O  OE2   . GLU A 1 2242 ? 92.064  81.308  142.347 1.00 36.83  ? 2242 GLU A OE2   1 
ATOM   6280  N  N     . ARG A 1 2243 ? 90.186  86.155  145.486 1.00 11.14  ? 2243 ARG A N     1 
ATOM   6281  C  CA    . ARG A 1 2243 ? 90.396  86.187  146.932 1.00 13.84  ? 2243 ARG A CA    1 
ATOM   6282  C  C     . ARG A 1 2243 ? 89.124  86.575  147.682 1.00 15.58  ? 2243 ARG A C     1 
ATOM   6283  O  O     . ARG A 1 2243 ? 88.823  86.005  148.737 1.00 22.63  ? 2243 ARG A O     1 
ATOM   6284  C  CB    . ARG A 1 2243 ? 91.538  87.140  147.280 1.00 11.23  ? 2243 ARG A CB    1 
ATOM   6285  C  CG    . ARG A 1 2243 ? 92.900  86.667  146.804 1.00 18.04  ? 2243 ARG A CG    1 
ATOM   6286  C  CD    . ARG A 1 2243 ? 93.991  87.652  147.178 1.00 26.65  ? 2243 ARG A CD    1 
ATOM   6287  N  NE    . ARG A 1 2243 ? 95.301  87.217  146.710 1.00 30.01  ? 2243 ARG A NE    1 
ATOM   6288  C  CZ    . ARG A 1 2243 ? 96.418  87.917  146.855 1.00 27.38  ? 2243 ARG A CZ    1 
ATOM   6289  N  NH1   . ARG A 1 2243 ? 96.422  89.096  147.454 1.00 26.43  ? 2243 ARG A NH1   1 
ATOM   6290  N  NH2   . ARG A 1 2243 ? 97.560  87.419  146.390 1.00 23.87  ? 2243 ARG A NH2   1 
ATOM   6291  N  N     . LEU A 1 2244 ? 88.366  87.540  147.158 1.00 13.03  ? 2244 LEU A N     1 
ATOM   6292  C  CA    . LEU A 1 2244 ? 87.211  88.074  147.871 1.00 13.14  ? 2244 LEU A CA    1 
ATOM   6293  C  C     . LEU A 1 2244 ? 86.023  87.121  147.847 1.00 16.10  ? 2244 LEU A C     1 
ATOM   6294  O  O     . LEU A 1 2244 ? 85.353  86.938  148.870 1.00 20.13  ? 2244 LEU A O     1 
ATOM   6295  C  CB    . LEU A 1 2244 ? 86.812  89.424  147.271 1.00 12.78  ? 2244 LEU A CB    1 
ATOM   6296  C  CG    . LEU A 1 2244 ? 85.675  90.189  147.951 1.00 17.85  ? 2244 LEU A CG    1 
ATOM   6297  C  CD1   . LEU A 1 2244 ? 86.179  90.940  149.170 1.00 17.82  ? 2244 LEU A CD1   1 
ATOM   6298  C  CD2   . LEU A 1 2244 ? 85.008  91.142  146.969 1.00 17.70  ? 2244 LEU A CD2   1 
ATOM   6299  N  N     . GLU A 1 2245 ? 85.743  86.507  146.698 1.00 14.69  ? 2245 GLU A N     1 
ATOM   6300  C  CA    . GLU A 1 2245 ? 84.536  85.711  146.531 1.00 12.10  ? 2245 GLU A CA    1 
ATOM   6301  C  C     . GLU A 1 2245 ? 84.761  84.219  146.724 1.00 14.47  ? 2245 GLU A C     1 
ATOM   6302  O  O     . GLU A 1 2245 ? 83.784  83.478  146.880 1.00 19.17  ? 2245 GLU A O     1 
ATOM   6303  C  CB    . GLU A 1 2245 ? 83.939  85.950  145.139 1.00 13.56  ? 2245 GLU A CB    1 
ATOM   6304  C  CG    . GLU A 1 2245 ? 83.437  87.367  144.918 1.00 16.81  ? 2245 GLU A CG    1 
ATOM   6305  C  CD    . GLU A 1 2245 ? 82.902  87.585  143.517 1.00 24.32  ? 2245 GLU A CD    1 
ATOM   6306  O  OE1   . GLU A 1 2245 ? 83.038  86.671  142.677 1.00 21.37  ? 2245 GLU A OE1   1 
ATOM   6307  O  OE2   . GLU A 1 2245 ? 82.345  88.672  143.255 1.00 25.61  ? 2245 GLU A OE2   1 
ATOM   6308  N  N     . GLY A 1 2246 ? 86.011  83.763  146.719 1.00 11.49  ? 2246 GLY A N     1 
ATOM   6309  C  CA    . GLY A 1 2246 ? 86.301  82.350  146.805 1.00 11.27  ? 2246 GLY A CA    1 
ATOM   6310  C  C     . GLY A 1 2246 ? 86.175  81.597  145.500 1.00 13.74  ? 2246 GLY A C     1 
ATOM   6311  O  O     . GLY A 1 2246 ? 86.396  80.380  145.484 1.00 18.62  ? 2246 GLY A O     1 
ATOM   6312  N  N     . VAL A 1 2247 ? 85.827  82.275  144.412 1.00 14.85  ? 2247 VAL A N     1 
ATOM   6313  C  CA    . VAL A 1 2247 ? 85.664  81.641  143.110 1.00 15.12  ? 2247 VAL A CA    1 
ATOM   6314  C  C     . VAL A 1 2247 ? 86.973  81.772  142.343 1.00 12.57  ? 2247 VAL A C     1 
ATOM   6315  O  O     . VAL A 1 2247 ? 87.484  82.881  142.156 1.00 12.91  ? 2247 VAL A O     1 
ATOM   6316  C  CB    . VAL A 1 2247 ? 84.502  82.270  142.328 1.00 13.35  ? 2247 VAL A CB    1 
ATOM   6317  C  CG1   . VAL A 1 2247 ? 84.380  81.635  140.951 1.00 10.66  ? 2247 VAL A CG1   1 
ATOM   6318  C  CG2   . VAL A 1 2247 ? 83.203  82.132  143.106 1.00 12.05  ? 2247 VAL A CG2   1 
ATOM   6319  N  N     . GLU A 1 2248 ? 87.516  80.641  141.903 1.00 12.97  ? 2248 GLU A N     1 
ATOM   6320  C  CA    . GLU A 1 2248 ? 88.752  80.654  141.134 1.00 13.52  ? 2248 GLU A CA    1 
ATOM   6321  C  C     . GLU A 1 2248 ? 88.539  81.356  139.798 1.00 11.89  ? 2248 GLU A C     1 
ATOM   6322  O  O     . GLU A 1 2248 ? 87.535  81.137  139.114 1.00 10.06  ? 2248 GLU A O     1 
ATOM   6323  C  CB    . GLU A 1 2248 ? 89.252  79.227  140.912 1.00 17.19  ? 2248 GLU A CB    1 
ATOM   6324  C  CG    . GLU A 1 2248 ? 90.388  79.104  139.911 1.00 21.70  ? 2248 GLU A CG    1 
ATOM   6325  C  CD    . GLU A 1 2248 ? 90.810  77.666  139.685 1.00 36.53  ? 2248 GLU A CD    1 
ATOM   6326  O  OE1   . GLU A 1 2248 ? 90.275  76.773  140.376 1.00 40.22  ? 2248 GLU A OE1   1 
ATOM   6327  O  OE2   . GLU A 1 2248 ? 91.676  77.427  138.818 1.00 40.34  ? 2248 GLU A OE2   1 
ATOM   6328  N  N     . GLY A 1 2249 ? 89.493  82.206  139.428 1.00 9.40   ? 2249 GLY A N     1 
ATOM   6329  C  CA    . GLY A 1 2249 ? 89.432  82.963  138.191 1.00 5.28   ? 2249 GLY A CA    1 
ATOM   6330  C  C     . GLY A 1 2249 ? 90.456  82.444  137.195 1.00 4.43   ? 2249 GLY A C     1 
ATOM   6331  O  O     . GLY A 1 2249 ? 91.639  82.315  137.516 1.00 7.28   ? 2249 GLY A O     1 
ATOM   6332  N  N     . VAL A 1 2250 ? 89.981  82.150  135.989 1.00 3.80   ? 2250 VAL A N     1 
ATOM   6333  C  CA    . VAL A 1 2250 ? 90.803  81.615  134.913 1.00 2.59   ? 2250 VAL A CA    1 
ATOM   6334  C  C     . VAL A 1 2250 ? 90.649  82.525  133.705 1.00 2.21   ? 2250 VAL A C     1 
ATOM   6335  O  O     . VAL A 1 2250 ? 89.523  82.820  133.283 1.00 2.71   ? 2250 VAL A O     1 
ATOM   6336  C  CB    . VAL A 1 2250 ? 90.409  80.168  134.565 1.00 2.53   ? 2250 VAL A CB    1 
ATOM   6337  C  CG1   . VAL A 1 2250 ? 91.178  79.683  133.344 1.00 2.59   ? 2250 VAL A CG1   1 
ATOM   6338  C  CG2   . VAL A 1 2250 ? 90.644  79.253  135.756 1.00 5.73   ? 2250 VAL A CG2   1 
ATOM   6339  N  N     . ALA A 1 2251 ? 91.775  82.963  133.152 1.00 1.99   ? 2251 ALA A N     1 
ATOM   6340  C  CA    . ALA A 1 2251 ? 91.796  83.855  132.003 1.00 1.35   ? 2251 ALA A CA    1 
ATOM   6341  C  C     . ALA A 1 2251 ? 92.394  83.132  130.807 1.00 1.87   ? 2251 ALA A C     1 
ATOM   6342  O  O     . ALA A 1 2251 ? 93.472  82.536  130.908 1.00 2.95   ? 2251 ALA A O     1 
ATOM   6343  C  CB    . ALA A 1 2251 ? 92.596  85.123  132.307 1.00 1.47   ? 2251 ALA A CB    1 
ATOM   6344  N  N     . HIS A 1 2252 ? 91.692  83.187  129.681 1.00 1.36   ? 2252 HIS A N     1 
ATOM   6345  C  CA    . HIS A 1 2252 ? 92.183  82.686  128.404 1.00 1.34   ? 2252 HIS A CA    1 
ATOM   6346  C  C     . HIS A 1 2252 ? 92.446  83.894  127.515 1.00 1.65   ? 2252 HIS A C     1 
ATOM   6347  O  O     . HIS A 1 2252 ? 91.506  84.572  127.085 1.00 2.34   ? 2252 HIS A O     1 
ATOM   6348  C  CB    . HIS A 1 2252 ? 91.179  81.731  127.762 1.00 1.46   ? 2252 HIS A CB    1 
ATOM   6349  C  CG    . HIS A 1 2252 ? 90.714  80.640  128.674 1.00 2.10   ? 2252 HIS A CG    1 
ATOM   6350  N  ND1   . HIS A 1 2252 ? 91.294  79.390  128.695 1.00 1.90   ? 2252 HIS A ND1   1 
ATOM   6351  C  CD2   . HIS A 1 2252 ? 89.722  80.609  129.595 1.00 2.02   ? 2252 HIS A CD2   1 
ATOM   6352  C  CE1   . HIS A 1 2252 ? 90.681  78.637  129.591 1.00 1.65   ? 2252 HIS A CE1   1 
ATOM   6353  N  NE2   . HIS A 1 2252 ? 89.723  79.353  130.151 1.00 2.11   ? 2252 HIS A NE2   1 
ATOM   6354  N  N     . ILE A 1 2253 ? 93.719  84.166  127.245 1.00 1.34   ? 2253 ILE A N     1 
ATOM   6355  C  CA    . ILE A 1 2253 ? 94.129  85.335  126.476 1.00 1.74   ? 2253 ILE A CA    1 
ATOM   6356  C  C     . ILE A 1 2253 ? 94.421  84.891  125.051 1.00 1.90   ? 2253 ILE A C     1 
ATOM   6357  O  O     . ILE A 1 2253 ? 95.323  84.079  124.816 1.00 2.35   ? 2253 ILE A O     1 
ATOM   6358  C  CB    . ILE A 1 2253 ? 95.351  86.027  127.100 1.00 2.09   ? 2253 ILE A CB    1 
ATOM   6359  C  CG1   . ILE A 1 2253 ? 95.023  86.564  128.497 1.00 2.04   ? 2253 ILE A CG1   1 
ATOM   6360  C  CG2   . ILE A 1 2253 ? 95.828  87.156  126.205 1.00 2.25   ? 2253 ILE A CG2   1 
ATOM   6361  C  CD1   . ILE A 1 2253 ? 95.283  85.586  129.620 1.00 3.81   ? 2253 ILE A CD1   1 
ATOM   6362  N  N     . ILE A 1 2254 ? 93.663  85.429  124.101 1.00 2.84   ? 2254 ILE A N     1 
ATOM   6363  C  CA    . ILE A 1 2254 ? 93.785  85.086  122.691 1.00 3.57   ? 2254 ILE A CA    1 
ATOM   6364  C  C     . ILE A 1 2254 ? 94.185  86.336  121.922 1.00 3.86   ? 2254 ILE A C     1 
ATOM   6365  O  O     . ILE A 1 2254 ? 93.639  87.419  122.164 1.00 4.47   ? 2254 ILE A O     1 
ATOM   6366  C  CB    . ILE A 1 2254 ? 92.472  84.502  122.136 1.00 3.24   ? 2254 ILE A CB    1 
ATOM   6367  C  CG1   . ILE A 1 2254 ? 92.119  83.200  122.856 1.00 3.37   ? 2254 ILE A CG1   1 
ATOM   6368  C  CG2   . ILE A 1 2254 ? 92.565  84.285  120.633 1.00 3.64   ? 2254 ILE A CG2   1 
ATOM   6369  C  CD1   . ILE A 1 2254 ? 90.807  82.601  122.413 1.00 3.09   ? 2254 ILE A CD1   1 
ATOM   6370  N  N     . ASP A 1 2255 ? 95.151  86.190  121.018 1.00 5.85   ? 2255 ASP A N     1 
ATOM   6371  C  CA    . ASP A 1 2255 ? 95.437  87.222  120.031 1.00 5.05   ? 2255 ASP A CA    1 
ATOM   6372  C  C     . ASP A 1 2255 ? 94.713  86.847  118.744 1.00 5.06   ? 2255 ASP A C     1 
ATOM   6373  O  O     . ASP A 1 2255 ? 95.237  86.065  117.941 1.00 7.13   ? 2255 ASP A O     1 
ATOM   6374  C  CB    . ASP A 1 2255 ? 96.943  87.360  119.797 1.00 4.52   ? 2255 ASP A CB    1 
ATOM   6375  C  CG    . ASP A 1 2255 ? 97.317  88.679  119.143 1.00 7.47   ? 2255 ASP A CG    1 
ATOM   6376  O  OD1   . ASP A 1 2255 ? 96.544  89.170  118.292 1.00 5.09   ? 2255 ASP A OD1   1 
ATOM   6377  O  OD2   . ASP A 1 2255 ? 98.389  89.225  119.477 1.00 9.45   ? 2255 ASP A OD2   1 
ATOM   6378  N  N     . PRO A 1 2256 ? 93.506  87.371  118.519 1.00 5.76   ? 2256 PRO A N     1 
ATOM   6379  C  CA    . PRO A 1 2256 ? 92.704  86.897  117.379 1.00 6.46   ? 2256 PRO A CA    1 
ATOM   6380  C  C     . PRO A 1 2256 ? 93.302  87.216  116.020 1.00 6.27   ? 2256 PRO A C     1 
ATOM   6381  O  O     . PRO A 1 2256 ? 93.005  86.510  115.048 1.00 11.44  ? 2256 PRO A O     1 
ATOM   6382  C  CB    . PRO A 1 2256 ? 91.357  87.603  117.590 1.00 4.71   ? 2256 PRO A CB    1 
ATOM   6383  C  CG    . PRO A 1 2256 ? 91.698  88.822  118.365 1.00 3.83   ? 2256 PRO A CG    1 
ATOM   6384  C  CD    . PRO A 1 2256 ? 92.812  88.421  119.283 1.00 3.87   ? 2256 PRO A CD    1 
ATOM   6385  N  N     . LYS A 1 2257 ? 94.131  88.251  115.912 1.00 5.13   ? 2257 LYS A N     1 
ATOM   6386  C  CA    . LYS A 1 2257 ? 94.756  88.594  114.641 1.00 5.92   ? 2257 LYS A CA    1 
ATOM   6387  C  C     . LYS A 1 2257 ? 96.151  88.004  114.483 1.00 4.39   ? 2257 LYS A C     1 
ATOM   6388  O  O     . LYS A 1 2257 ? 96.774  88.199  113.434 1.00 5.56   ? 2257 LYS A O     1 
ATOM   6389  C  CB    . LYS A 1 2257 ? 94.815  90.115  114.467 1.00 6.16   ? 2257 LYS A CB    1 
ATOM   6390  C  CG    . LYS A 1 2257 ? 93.454  90.769  114.295 1.00 6.16   ? 2257 LYS A CG    1 
ATOM   6391  C  CD    . LYS A 1 2257 ? 92.865  90.467  112.930 1.00 7.47   ? 2257 LYS A CD    1 
ATOM   6392  C  CE    . LYS A 1 2257 ? 93.626  91.181  111.827 1.00 8.74   ? 2257 LYS A CE    1 
ATOM   6393  N  NZ    . LYS A 1 2257 ? 93.085  92.543  111.570 1.00 6.08   ? 2257 LYS A NZ    1 
ATOM   6394  N  N     . ALA A 1 2258 ? 96.657  87.292  115.489 1.00 3.77   ? 2258 ALA A N     1 
ATOM   6395  C  CA    . ALA A 1 2258 ? 97.906  86.559  115.333 1.00 3.31   ? 2258 ALA A CA    1 
ATOM   6396  C  C     . ALA A 1 2258 ? 97.714  85.240  114.599 1.00 6.78   ? 2258 ALA A C     1 
ATOM   6397  O  O     . ALA A 1 2258 ? 98.706  84.599  114.238 1.00 8.03   ? 2258 ALA A O     1 
ATOM   6398  C  CB    . ALA A 1 2258 ? 98.545  86.301  116.699 1.00 2.74   ? 2258 ALA A CB    1 
ATOM   6399  N  N     . ILE A 1 2259 ? 96.467  84.827  114.375 1.00 6.76   ? 2259 ILE A N     1 
ATOM   6400  C  CA    . ILE A 1 2259 ? 96.139  83.600  113.666 1.00 5.75   ? 2259 ILE A CA    1 
ATOM   6401  C  C     . ILE A 1 2259 ? 95.072  83.921  112.628 1.00 7.10   ? 2259 ILE A C     1 
ATOM   6402  O  O     . ILE A 1 2259 ? 94.459  84.989  112.641 1.00 8.61   ? 2259 ILE A O     1 
ATOM   6403  C  CB    . ILE A 1 2259 ? 95.650  82.485  114.613 1.00 6.68   ? 2259 ILE A CB    1 
ATOM   6404  C  CG1   . ILE A 1 2259 ? 94.340  82.901  115.288 1.00 4.97   ? 2259 ILE A CG1   1 
ATOM   6405  C  CG2   . ILE A 1 2259 ? 96.710  82.156  115.653 1.00 4.38   ? 2259 ILE A CG2   1 
ATOM   6406  C  CD1   . ILE A 1 2259 ? 93.809  81.891  116.276 1.00 3.88   ? 2259 ILE A CD1   1 
ATOM   6407  N  N     . SER A 1 2260 ? 94.858  82.977  111.717 1.00 6.51   ? 2260 SER A N     1 
ATOM   6408  C  CA    . SER A 1 2260 ? 93.804  83.128  110.728 1.00 7.52   ? 2260 SER A CA    1 
ATOM   6409  C  C     . SER A 1 2260 ? 92.433  82.986  111.385 1.00 7.51   ? 2260 SER A C     1 
ATOM   6410  O  O     . SER A 1 2260 ? 92.286  82.411  112.467 1.00 6.89   ? 2260 SER A O     1 
ATOM   6411  C  CB    . SER A 1 2260 ? 93.962  82.097  109.611 1.00 8.15   ? 2260 SER A CB    1 
ATOM   6412  O  OG    . SER A 1 2260 ? 93.752  80.782  110.094 1.00 9.44   ? 2260 SER A OG    1 
ATOM   6413  N  N     . LYS A 1 2261 ? 91.417  83.533  110.712 1.00 7.68   ? 2261 LYS A N     1 
ATOM   6414  C  CA    . LYS A 1 2261 ? 90.052  83.429  111.220 1.00 7.15   ? 2261 LYS A CA    1 
ATOM   6415  C  C     . LYS A 1 2261 ? 89.584  81.981  111.261 1.00 6.34   ? 2261 LYS A C     1 
ATOM   6416  O  O     . LYS A 1 2261 ? 88.811  81.600  112.150 1.00 6.20   ? 2261 LYS A O     1 
ATOM   6417  C  CB    . LYS A 1 2261 ? 89.112  84.278  110.364 1.00 7.80   ? 2261 LYS A CB    1 
ATOM   6418  C  CG    . LYS A 1 2261 ? 87.683  84.335  110.871 1.00 10.10  ? 2261 LYS A CG    1 
ATOM   6419  C  CD    . LYS A 1 2261 ? 86.779  85.047  109.881 1.00 11.85  ? 2261 LYS A CD    1 
ATOM   6420  C  CE    . LYS A 1 2261 ? 85.333  85.025  110.340 1.00 13.16  ? 2261 LYS A CE    1 
ATOM   6421  N  NZ    . LYS A 1 2261 ? 84.433  85.689  109.360 1.00 18.83  ? 2261 LYS A NZ    1 
ATOM   6422  N  N     . ASP A 1 2262 ? 90.042  81.163  110.310 1.00 6.96   ? 2262 ASP A N     1 
ATOM   6423  C  CA    . ASP A 1 2262 ? 89.745  79.736  110.347 1.00 8.82   ? 2262 ASP A CA    1 
ATOM   6424  C  C     . ASP A 1 2262 ? 90.318  79.092  111.602 1.00 8.04   ? 2262 ASP A C     1 
ATOM   6425  O  O     . ASP A 1 2262 ? 89.676  78.236  112.220 1.00 6.98   ? 2262 ASP A O     1 
ATOM   6426  C  CB    . ASP A 1 2262 ? 90.295  79.055  109.094 1.00 12.57  ? 2262 ASP A CB    1 
ATOM   6427  C  CG    . ASP A 1 2262 ? 89.554  79.459  107.836 1.00 23.29  ? 2262 ASP A CG    1 
ATOM   6428  O  OD1   . ASP A 1 2262 ? 88.351  79.781  107.930 1.00 28.09  ? 2262 ASP A OD1   1 
ATOM   6429  O  OD2   . ASP A 1 2262 ? 90.175  79.456  106.753 1.00 22.22  ? 2262 ASP A OD2   1 
ATOM   6430  N  N     . HIS A 1 2263 ? 91.530  79.489  111.992 1.00 6.55   ? 2263 HIS A N     1 
ATOM   6431  C  CA    . HIS A 1 2263 ? 92.127  78.981  113.219 1.00 4.92   ? 2263 HIS A CA    1 
ATOM   6432  C  C     . HIS A 1 2263 ? 91.492  79.573  114.470 1.00 3.91   ? 2263 HIS A C     1 
ATOM   6433  O  O     . HIS A 1 2263 ? 91.609  78.978  115.546 1.00 4.43   ? 2263 HIS A O     1 
ATOM   6434  C  CB    . HIS A 1 2263 ? 93.632  79.258  113.228 1.00 6.13   ? 2263 HIS A CB    1 
ATOM   6435  C  CG    . HIS A 1 2263 ? 94.417  78.352  112.333 1.00 9.48   ? 2263 HIS A CG    1 
ATOM   6436  N  ND1   . HIS A 1 2263 ? 95.602  78.734  111.741 1.00 12.27  ? 2263 HIS A ND1   1 
ATOM   6437  C  CD2   . HIS A 1 2263 ? 94.187  77.081  111.927 1.00 9.34   ? 2263 HIS A CD2   1 
ATOM   6438  C  CE1   . HIS A 1 2263 ? 96.068  77.736  111.010 1.00 11.71  ? 2263 HIS A CE1   1 
ATOM   6439  N  NE2   . HIS A 1 2263 ? 95.228  76.722  111.106 1.00 12.55  ? 2263 HIS A NE2   1 
ATOM   6440  N  N     . LEU A 1 2264 ? 90.828  80.724  114.357 1.00 3.95   ? 2264 LEU A N     1 
ATOM   6441  C  CA    . LEU A 1 2264 ? 90.185  81.323  115.521 1.00 3.26   ? 2264 LEU A CA    1 
ATOM   6442  C  C     . LEU A 1 2264 ? 88.826  80.691  115.796 1.00 2.46   ? 2264 LEU A C     1 
ATOM   6443  O  O     . LEU A 1 2264 ? 88.525  80.326  116.937 1.00 2.53   ? 2264 LEU A O     1 
ATOM   6444  C  CB    . LEU A 1 2264 ? 90.034  82.833  115.328 1.00 3.57   ? 2264 LEU A CB    1 
ATOM   6445  C  CG    . LEU A 1 2264 ? 89.371  83.556  116.505 1.00 3.10   ? 2264 LEU A CG    1 
ATOM   6446  C  CD1   . LEU A 1 2264 ? 90.195  83.390  117.775 1.00 2.75   ? 2264 LEU A CD1   1 
ATOM   6447  C  CD2   . LEU A 1 2264 ? 89.137  85.027  116.197 1.00 3.25   ? 2264 LEU A CD2   1 
ATOM   6448  N  N     . TYR A 1 2265 ? 87.993  80.553  114.766 1.00 2.78   ? 2265 TYR A N     1 
ATOM   6449  C  CA    . TYR A 1 2265 ? 86.629  80.076  114.951 1.00 3.63   ? 2265 TYR A CA    1 
ATOM   6450  C  C     . TYR A 1 2265 ? 86.407  78.634  114.526 1.00 3.65   ? 2265 TYR A C     1 
ATOM   6451  O  O     . TYR A 1 2265 ? 85.540  77.969  115.094 1.00 3.44   ? 2265 TYR A O     1 
ATOM   6452  C  CB    . TYR A 1 2265 ? 85.641  80.973  114.195 1.00 2.18   ? 2265 TYR A CB    1 
ATOM   6453  C  CG    . TYR A 1 2265 ? 85.559  82.375  114.749 1.00 2.98   ? 2265 TYR A CG    1 
ATOM   6454  C  CD1   . TYR A 1 2265 ? 85.039  82.608  116.016 1.00 4.10   ? 2265 TYR A CD1   1 
ATOM   6455  C  CD2   . TYR A 1 2265 ? 85.996  83.465  114.010 1.00 3.48   ? 2265 TYR A CD2   1 
ATOM   6456  C  CE1   . TYR A 1 2265 ? 84.958  83.883  116.531 1.00 4.02   ? 2265 TYR A CE1   1 
ATOM   6457  C  CE2   . TYR A 1 2265 ? 85.918  84.746  114.518 1.00 3.78   ? 2265 TYR A CE2   1 
ATOM   6458  C  CZ    . TYR A 1 2265 ? 85.399  84.949  115.780 1.00 3.33   ? 2265 TYR A CZ    1 
ATOM   6459  O  OH    . TYR A 1 2265 ? 85.318  86.222  116.293 1.00 5.73   ? 2265 TYR A OH    1 
ATOM   6460  N  N     . GLY A 1 2266 ? 87.161  78.134  113.560 1.00 4.92   ? 2266 GLY A N     1 
ATOM   6461  C  CA    . GLY A 1 2266 ? 87.008  76.773  113.090 1.00 4.76   ? 2266 GLY A CA    1 
ATOM   6462  C  C     . GLY A 1 2266 ? 86.808  76.707  111.587 1.00 5.59   ? 2266 GLY A C     1 
ATOM   6463  O  O     . GLY A 1 2266 ? 86.688  77.714  110.892 1.00 10.22  ? 2266 GLY A O     1 
ATOM   6464  N  N     . THR A 1 2267 ? 86.775  75.471  111.100 1.00 5.95   ? 2267 THR A N     1 
ATOM   6465  C  CA    . THR A 1 2267 ? 86.694  75.201  109.674 1.00 9.00   ? 2267 THR A CA    1 
ATOM   6466  C  C     . THR A 1 2267 ? 85.754  74.034  109.408 1.00 9.75   ? 2267 THR A C     1 
ATOM   6467  O  O     . THR A 1 2267 ? 85.803  73.005  110.087 1.00 8.44   ? 2267 THR A O     1 
ATOM   6468  C  CB    . THR A 1 2267 ? 88.084  74.899  109.085 1.00 12.60  ? 2267 THR A CB    1 
ATOM   6469  O  OG1   . THR A 1 2267 ? 88.921  76.054  109.216 1.00 12.95  ? 2267 THR A OG1   1 
ATOM   6470  C  CG2   . THR A 1 2267 ? 87.982  74.526  107.615 1.00 15.12  ? 2267 THR A CG2   1 
ATOM   6471  N  N     . LEU A 1 2268 ? 84.901  74.203  108.403 1.00 11.90  ? 2268 LEU A N     1 
ATOM   6472  C  CA    . LEU A 1 2268 ? 84.053  73.131  107.900 1.00 15.49  ? 2268 LEU A CA    1 
ATOM   6473  C  C     . LEU A 1 2268 ? 84.729  72.528  106.675 1.00 19.05  ? 2268 LEU A C     1 
ATOM   6474  O  O     . LEU A 1 2268 ? 85.012  73.240  105.706 1.00 21.92  ? 2268 LEU A O     1 
ATOM   6475  C  CB    . LEU A 1 2268 ? 82.658  73.652  107.555 1.00 13.75  ? 2268 LEU A CB    1 
ATOM   6476  C  CG    . LEU A 1 2268 ? 81.523  72.627  107.526 1.00 18.22  ? 2268 LEU A CG    1 
ATOM   6477  C  CD1   . LEU A 1 2268 ? 81.583  71.720  108.746 1.00 16.59  ? 2268 LEU A CD1   1 
ATOM   6478  C  CD2   . LEU A 1 2268 ? 80.177  73.329  107.444 1.00 14.81  ? 2268 LEU A CD2   1 
ATOM   6479  N  N     . ASP A 1 2269 ? 84.995  71.228  106.727 1.00 24.16  ? 2269 ASP A N     1 
ATOM   6480  C  CA    . ASP A 1 2269 ? 85.736  70.576  105.655 1.00 29.30  ? 2269 ASP A CA    1 
ATOM   6481  C  C     . ASP A 1 2269 ? 84.924  70.608  104.363 1.00 28.65  ? 2269 ASP A C     1 
ATOM   6482  O  O     . ASP A 1 2269 ? 83.752  70.209  104.363 1.00 33.49  ? 2269 ASP A O     1 
ATOM   6483  C  CB    . ASP A 1 2269 ? 86.072  69.136  106.039 1.00 30.48  ? 2269 ASP A CB    1 
ATOM   6484  C  CG    . ASP A 1 2269 ? 86.843  68.407  104.955 1.00 41.23  ? 2269 ASP A CG    1 
ATOM   6485  O  OD1   . ASP A 1 2269 ? 88.088  68.355  105.043 1.00 43.18  ? 2269 ASP A OD1   1 
ATOM   6486  O  OD2   . ASP A 1 2269 ? 86.206  67.879  104.020 1.00 44.99  ? 2269 ASP A OD2   1 
ATOM   6487  N  N     . PRO A 1 2270 ? 85.497  71.085  103.255 1.00 29.69  ? 2270 PRO A N     1 
ATOM   6488  C  CA    . PRO A 1 2270 ? 84.718  71.171  102.007 1.00 36.10  ? 2270 PRO A CA    1 
ATOM   6489  C  C     . PRO A 1 2270 ? 84.191  69.833  101.515 1.00 41.73  ? 2270 PRO A C     1 
ATOM   6490  O  O     . PRO A 1 2270 ? 83.092  69.777  100.950 1.00 43.17  ? 2270 PRO A O     1 
ATOM   6491  C  CB    . PRO A 1 2270 ? 85.719  71.783  101.017 1.00 33.31  ? 2270 PRO A CB    1 
ATOM   6492  C  CG    . PRO A 1 2270 ? 86.702  72.512  101.873 1.00 28.55  ? 2270 PRO A CG    1 
ATOM   6493  C  CD    . PRO A 1 2270 ? 86.832  71.691  103.120 1.00 28.72  ? 2270 PRO A CD    1 
ATOM   6494  N  N     . ASN A 1 2271 ? 84.942  68.749  101.713 1.00 39.34  ? 2271 ASN A N     1 
ATOM   6495  C  CA    . ASN A 1 2271 ? 84.575  67.442  101.176 1.00 43.90  ? 2271 ASN A CA    1 
ATOM   6496  C  C     . ASN A 1 2271 ? 83.790  66.601  102.177 1.00 39.69  ? 2271 ASN A C     1 
ATOM   6497  O  O     . ASN A 1 2271 ? 82.653  66.206  101.904 1.00 46.23  ? 2271 ASN A O     1 
ATOM   6498  C  CB    . ASN A 1 2271 ? 85.835  66.693  100.722 1.00 49.83  ? 2271 ASN A CB    1 
ATOM   6499  C  CG    . ASN A 1 2271 ? 86.788  67.576  99.941  1.00 50.08  ? 2271 ASN A CG    1 
ATOM   6500  O  OD1   . ASN A 1 2271 ? 86.430  68.126  98.899  1.00 55.03  ? 2271 ASN A OD1   1 
ATOM   6501  N  ND2   . ASN A 1 2271 ? 88.009  67.717  100.442 1.00 47.52  ? 2271 ASN A ND2   1 
ATOM   6502  N  N     . THR A 1 2272 ? 84.378  66.319  103.339 1.00 36.84  ? 2272 THR A N     1 
ATOM   6503  C  CA    . THR A 1 2272 ? 83.742  65.449  104.320 1.00 38.83  ? 2272 THR A CA    1 
ATOM   6504  C  C     . THR A 1 2272 ? 82.729  66.172  105.197 1.00 32.48  ? 2272 THR A C     1 
ATOM   6505  O  O     . THR A 1 2272 ? 82.022  65.509  105.964 1.00 31.85  ? 2272 THR A O     1 
ATOM   6506  C  CB    . THR A 1 2272 ? 84.802  64.792  105.209 1.00 44.42  ? 2272 THR A CB    1 
ATOM   6507  O  OG1   . THR A 1 2272 ? 85.525  65.802  105.922 1.00 39.63  ? 2272 THR A OG1   1 
ATOM   6508  C  CG2   . THR A 1 2272 ? 85.774  63.981  104.366 1.00 47.30  ? 2272 THR A CG2   1 
ATOM   6509  N  N     . ARG A 1 2273 ? 82.649  67.501  105.108 1.00 32.59  ? 2273 ARG A N     1 
ATOM   6510  C  CA    . ARG A 1 2273 ? 81.749  68.308  105.935 1.00 28.58  ? 2273 ARG A CA    1 
ATOM   6511  C  C     . ARG A 1 2273 ? 82.021  68.109  107.424 1.00 30.06  ? 2273 ARG A C     1 
ATOM   6512  O  O     . ARG A 1 2273 ? 81.120  68.237  108.255 1.00 32.10  ? 2273 ARG A O     1 
ATOM   6513  C  CB    . ARG A 1 2273 ? 80.279  68.022  105.612 1.00 30.35  ? 2273 ARG A CB    1 
ATOM   6514  C  CG    . ARG A 1 2273 ? 79.916  68.194  104.144 1.00 34.10  ? 2273 ARG A CG    1 
ATOM   6515  C  CD    . ARG A 1 2273 ? 80.493  69.482  103.574 1.00 28.05  ? 2273 ARG A CD    1 
ATOM   6516  N  NE    . ARG A 1 2273 ? 79.707  70.649  103.953 1.00 25.30  ? 2273 ARG A NE    1 
ATOM   6517  C  CZ    . ARG A 1 2273 ? 80.082  71.904  103.747 1.00 23.93  ? 2273 ARG A CZ    1 
ATOM   6518  N  NH1   . ARG A 1 2273 ? 81.231  72.194  103.159 1.00 25.93  ? 2273 ARG A NH1   1 
ATOM   6519  N  NH2   . ARG A 1 2273 ? 79.284  72.893  104.140 1.00 19.00  ? 2273 ARG A NH2   1 
ATOM   6520  N  N     . GLU A 1 2274 ? 83.267  67.795  107.766 1.00 32.21  ? 2274 GLU A N     1 
ATOM   6521  C  CA    . GLU A 1 2274 ? 83.673  67.617  109.151 1.00 25.17  ? 2274 GLU A CA    1 
ATOM   6522  C  C     . GLU A 1 2274 ? 84.101  68.955  109.738 1.00 21.39  ? 2274 GLU A C     1 
ATOM   6523  O  O     . GLU A 1 2274 ? 84.831  69.721  109.103 1.00 19.56  ? 2274 GLU A O     1 
ATOM   6524  C  CB    . GLU A 1 2274 ? 84.816  66.604  109.251 1.00 27.30  ? 2274 GLU A CB    1 
ATOM   6525  C  CG    . GLU A 1 2274 ? 85.506  66.507  110.616 1.00 30.97  ? 2274 GLU A CG    1 
ATOM   6526  C  CD    . GLU A 1 2274 ? 84.572  66.122  111.757 1.00 42.02  ? 2274 GLU A CD    1 
ATOM   6527  O  OE1   . GLU A 1 2274 ? 84.766  65.030  112.331 1.00 43.19  ? 2274 GLU A OE1   1 
ATOM   6528  O  OE2   . GLU A 1 2274 ? 83.669  66.911  112.107 1.00 38.53  ? 2274 GLU A OE2   1 
ATOM   6529  N  N     . TRP A 1 2275 ? 83.642  69.231  110.954 1.00 18.34  ? 2275 TRP A N     1 
ATOM   6530  C  CA    . TRP A 1 2275 ? 83.913  70.495  111.623 1.00 14.07  ? 2275 TRP A CA    1 
ATOM   6531  C  C     . TRP A 1 2275 ? 85.118  70.364  112.543 1.00 14.14  ? 2275 TRP A C     1 
ATOM   6532  O  O     . TRP A 1 2275 ? 85.181  69.448  113.370 1.00 17.33  ? 2275 TRP A O     1 
ATOM   6533  C  CB    . TRP A 1 2275 ? 82.694  70.963  112.418 1.00 9.94   ? 2275 TRP A CB    1 
ATOM   6534  C  CG    . TRP A 1 2275 ? 82.976  72.159  113.269 1.00 8.19   ? 2275 TRP A CG    1 
ATOM   6535  C  CD1   . TRP A 1 2275 ? 83.153  72.179  114.620 1.00 6.54   ? 2275 TRP A CD1   1 
ATOM   6536  C  CD2   . TRP A 1 2275 ? 83.156  73.507  112.821 1.00 7.92   ? 2275 TRP A CD2   1 
ATOM   6537  N  NE1   . TRP A 1 2275 ? 83.409  73.458  115.046 1.00 5.31   ? 2275 TRP A NE1   1 
ATOM   6538  C  CE2   . TRP A 1 2275 ? 83.419  74.293  113.960 1.00 5.14   ? 2275 TRP A CE2   1 
ATOM   6539  C  CE3   . TRP A 1 2275 ? 83.113  74.127  111.569 1.00 6.44   ? 2275 TRP A CE3   1 
ATOM   6540  C  CZ2   . TRP A 1 2275 ? 83.636  75.667  113.884 1.00 4.15   ? 2275 TRP A CZ2   1 
ATOM   6541  C  CZ3   . TRP A 1 2275 ? 83.327  75.491  111.496 1.00 6.57   ? 2275 TRP A CZ3   1 
ATOM   6542  C  CH2   . TRP A 1 2275 ? 83.584  76.246  112.647 1.00 5.33   ? 2275 TRP A CH2   1 
ATOM   6543  N  N     . THR A 1 2276 ? 86.067  71.283  112.396 1.00 10.25  ? 2276 THR A N     1 
ATOM   6544  C  CA    . THR A 1 2276 ? 87.218  71.394  113.279 1.00 9.54   ? 2276 THR A CA    1 
ATOM   6545  C  C     . THR A 1 2276 ? 87.106  72.699  114.054 1.00 7.29   ? 2276 THR A C     1 
ATOM   6546  O  O     . THR A 1 2276 ? 86.957  73.768  113.453 1.00 6.63   ? 2276 THR A O     1 
ATOM   6547  C  CB    . THR A 1 2276 ? 88.529  71.356  112.491 1.00 11.04  ? 2276 THR A CB    1 
ATOM   6548  O  OG1   . THR A 1 2276 ? 88.664  70.086  111.842 1.00 20.62  ? 2276 THR A OG1   1 
ATOM   6549  C  CG2   . THR A 1 2276 ? 89.715  71.576  113.418 1.00 7.72   ? 2276 THR A CG2   1 
ATOM   6550  N  N     . ASP A 1 2277 ? 87.171  72.605  115.379 1.00 6.25   ? 2277 ASP A N     1 
ATOM   6551  C  CA    . ASP A 1 2277 ? 87.011  73.777  116.227 1.00 4.43   ? 2277 ASP A CA    1 
ATOM   6552  C  C     . ASP A 1 2277 ? 88.203  74.716  116.102 1.00 4.93   ? 2277 ASP A C     1 
ATOM   6553  O  O     . ASP A 1 2277 ? 89.347  74.281  115.947 1.00 4.82   ? 2277 ASP A O     1 
ATOM   6554  C  CB    . ASP A 1 2277 ? 86.839  73.358  117.687 1.00 4.79   ? 2277 ASP A CB    1 
ATOM   6555  C  CG    . ASP A 1 2277 ? 85.391  73.133  118.063 1.00 7.02   ? 2277 ASP A CG    1 
ATOM   6556  O  OD1   . ASP A 1 2277 ? 84.512  73.322  117.197 1.00 10.28  ? 2277 ASP A OD1   1 
ATOM   6557  O  OD2   . ASP A 1 2277 ? 85.132  72.766  119.228 1.00 8.07   ? 2277 ASP A OD2   1 
ATOM   6558  N  N     . GLY A 1 2278 ? 87.926  76.016  116.169 1.00 5.21   ? 2278 GLY A N     1 
ATOM   6559  C  CA    . GLY A 1 2278 ? 88.967  77.008  116.298 1.00 3.12   ? 2278 GLY A CA    1 
ATOM   6560  C  C     . GLY A 1 2278 ? 89.392  77.170  117.743 1.00 2.54   ? 2278 GLY A C     1 
ATOM   6561  O  O     . GLY A 1 2278 ? 88.937  76.465  118.641 1.00 3.12   ? 2278 GLY A O     1 
ATOM   6562  N  N     . LEU A 1 2279 ? 90.291  78.130  117.965 1.00 3.04   ? 2279 LEU A N     1 
ATOM   6563  C  CA    . LEU A 1 2279 ? 90.807  78.360  119.311 1.00 2.20   ? 2279 LEU A CA    1 
ATOM   6564  C  C     . LEU A 1 2279 ? 89.705  78.827  120.256 1.00 2.04   ? 2279 LEU A C     1 
ATOM   6565  O  O     . LEU A 1 2279 ? 89.482  78.231  121.319 1.00 2.13   ? 2279 LEU A O     1 
ATOM   6566  C  CB    . LEU A 1 2279 ? 91.941  79.383  119.254 1.00 2.50   ? 2279 LEU A CB    1 
ATOM   6567  C  CG    . LEU A 1 2279 ? 92.545  79.844  120.579 1.00 2.78   ? 2279 LEU A CG    1 
ATOM   6568  C  CD1   . LEU A 1 2279 ? 93.013  78.656  121.405 1.00 3.85   ? 2279 LEU A CD1   1 
ATOM   6569  C  CD2   . LEU A 1 2279 ? 93.683  80.808  120.314 1.00 2.59   ? 2279 LEU A CD2   1 
ATOM   6570  N  N     . PHE A 1 2280 ? 88.989  79.886  119.872 1.00 2.17   ? 2280 PHE A N     1 
ATOM   6571  C  CA    . PHE A 1 2280 ? 87.926  80.414  120.721 1.00 2.57   ? 2280 PHE A CA    1 
ATOM   6572  C  C     . PHE A 1 2280 ? 86.779  79.418  120.844 1.00 2.30   ? 2280 PHE A C     1 
ATOM   6573  O  O     . PHE A 1 2280 ? 86.217  79.238  121.933 1.00 2.02   ? 2280 PHE A O     1 
ATOM   6574  C  CB    . PHE A 1 2280 ? 87.442  81.754  120.163 1.00 2.15   ? 2280 PHE A CB    1 
ATOM   6575  C  CG    . PHE A 1 2280 ? 86.202  82.281  120.824 1.00 2.27   ? 2280 PHE A CG    1 
ATOM   6576  C  CD1   . PHE A 1 2280 ? 86.254  82.803  122.104 1.00 2.32   ? 2280 PHE A CD1   1 
ATOM   6577  C  CD2   . PHE A 1 2280 ? 84.992  82.280  120.155 1.00 1.74   ? 2280 PHE A CD2   1 
ATOM   6578  C  CE1   . PHE A 1 2280 ? 85.117  83.294  122.714 1.00 1.93   ? 2280 PHE A CE1   1 
ATOM   6579  C  CE2   . PHE A 1 2280 ? 83.852  82.772  120.760 1.00 1.94   ? 2280 PHE A CE2   1 
ATOM   6580  C  CZ    . PHE A 1 2280 ? 83.915  83.279  122.040 1.00 2.97   ? 2280 PHE A CZ    1 
ATOM   6581  N  N     . THR A 1 2281 ? 86.431  78.754  119.738 1.00 2.28   ? 2281 THR A N     1 
ATOM   6582  C  CA    . THR A 1 2281 ? 85.395  77.728  119.781 1.00 2.79   ? 2281 THR A CA    1 
ATOM   6583  C  C     . THR A 1 2281 ? 85.787  76.591  120.713 1.00 2.73   ? 2281 THR A C     1 
ATOM   6584  O  O     . THR A 1 2281 ? 84.971  76.133  121.520 1.00 3.29   ? 2281 THR A O     1 
ATOM   6585  C  CB    . THR A 1 2281 ? 85.120  77.196  118.375 1.00 4.08   ? 2281 THR A CB    1 
ATOM   6586  O  OG1   . THR A 1 2281 ? 85.032  78.292  117.457 1.00 4.41   ? 2281 THR A OG1   1 
ATOM   6587  C  CG2   . THR A 1 2281 ? 83.818  76.413  118.347 1.00 2.84   ? 2281 THR A CG2   1 
ATOM   6588  N  N     . HIS A 1 2282 ? 87.038  76.132  120.625 1.00 2.26   ? 2282 HIS A N     1 
ATOM   6589  C  CA    . HIS A 1 2282 ? 87.495  75.054  121.495 1.00 2.35   ? 2282 HIS A CA    1 
ATOM   6590  C  C     . HIS A 1 2282 ? 87.448  75.467  122.960 1.00 2.06   ? 2282 HIS A C     1 
ATOM   6591  O  O     . HIS A 1 2282 ? 86.997  74.695  123.812 1.00 2.59   ? 2282 HIS A O     1 
ATOM   6592  C  CB    . HIS A 1 2282 ? 88.909  74.624  121.107 1.00 3.12   ? 2282 HIS A CB    1 
ATOM   6593  C  CG    . HIS A 1 2282 ? 89.604  73.810  122.153 1.00 4.67   ? 2282 HIS A CG    1 
ATOM   6594  N  ND1   . HIS A 1 2282 ? 89.446  72.446  122.263 1.00 5.84   ? 2282 HIS A ND1   1 
ATOM   6595  C  CD2   . HIS A 1 2282 ? 90.465  74.169  123.135 1.00 3.89   ? 2282 HIS A CD2   1 
ATOM   6596  C  CE1   . HIS A 1 2282 ? 90.177  71.999  123.268 1.00 6.46   ? 2282 HIS A CE1   1 
ATOM   6597  N  NE2   . HIS A 1 2282 ? 90.804  73.024  123.815 1.00 7.36   ? 2282 HIS A NE2   1 
ATOM   6598  N  N     . VAL A 1 2283 ? 87.905  76.682  123.272 1.00 2.16   ? 2283 VAL A N     1 
ATOM   6599  C  CA    . VAL A 1 2283 ? 87.935  77.122  124.666 1.00 1.95   ? 2283 VAL A CA    1 
ATOM   6600  C  C     . VAL A 1 2283 ? 86.519  77.236  125.224 1.00 2.27   ? 2283 VAL A C     1 
ATOM   6601  O  O     . VAL A 1 2283 ? 86.230  76.772  126.337 1.00 2.72   ? 2283 VAL A O     1 
ATOM   6602  C  CB    . VAL A 1 2283 ? 88.706  78.448  124.796 1.00 2.08   ? 2283 VAL A CB    1 
ATOM   6603  C  CG1   . VAL A 1 2283 ? 88.503  79.051  126.178 1.00 1.68   ? 2283 VAL A CG1   1 
ATOM   6604  C  CG2   . VAL A 1 2283 ? 90.185  78.230  124.520 1.00 2.21   ? 2283 VAL A CG2   1 
ATOM   6605  N  N     . LEU A 1 2284 ? 85.609  77.845  124.457 1.00 2.10   ? 2284 LEU A N     1 
ATOM   6606  C  CA    . LEU A 1 2284 ? 84.245  78.004  124.951 1.00 2.20   ? 2284 LEU A CA    1 
ATOM   6607  C  C     . LEU A 1 2284 ? 83.543  76.657  125.076 1.00 2.52   ? 2284 LEU A C     1 
ATOM   6608  O  O     . LEU A 1 2284 ? 82.781  76.436  126.023 1.00 3.24   ? 2284 LEU A O     1 
ATOM   6609  C  CB    . LEU A 1 2284 ? 83.453  78.947  124.046 1.00 2.01   ? 2284 LEU A CB    1 
ATOM   6610  C  CG    . LEU A 1 2284 ? 81.950  79.052  124.321 1.00 2.16   ? 2284 LEU A CG    1 
ATOM   6611  C  CD1   . LEU A 1 2284 ? 81.699  79.563  125.732 1.00 3.53   ? 2284 LEU A CD1   1 
ATOM   6612  C  CD2   . LEU A 1 2284 ? 81.259  79.944  123.302 1.00 3.36   ? 2284 LEU A CD2   1 
ATOM   6613  N  N     . ARG A 1 2285 ? 83.785  75.741  124.133 1.00 1.91   ? 2285 ARG A N     1 
ATOM   6614  C  CA    . ARG A 1 2285 ? 83.198  74.410  124.231 1.00 3.40   ? 2285 ARG A CA    1 
ATOM   6615  C  C     . ARG A 1 2285 ? 83.740  73.656  125.438 1.00 4.39   ? 2285 ARG A C     1 
ATOM   6616  O  O     . ARG A 1 2285 ? 83.000  72.920  126.100 1.00 5.12   ? 2285 ARG A O     1 
ATOM   6617  C  CB    . ARG A 1 2285 ? 83.454  73.630  122.943 1.00 3.06   ? 2285 ARG A CB    1 
ATOM   6618  C  CG    . ARG A 1 2285 ? 82.663  72.341  122.829 1.00 4.33   ? 2285 ARG A CG    1 
ATOM   6619  C  CD    . ARG A 1 2285 ? 83.169  71.489  121.677 1.00 7.37   ? 2285 ARG A CD    1 
ATOM   6620  N  NE    . ARG A 1 2285 ? 82.989  72.151  120.390 1.00 8.52   ? 2285 ARG A NE    1 
ATOM   6621  C  CZ    . ARG A 1 2285 ? 81.828  72.269  119.761 1.00 7.64   ? 2285 ARG A CZ    1 
ATOM   6622  N  NH1   . ARG A 1 2285 ? 80.712  71.773  120.268 1.00 8.59   ? 2285 ARG A NH1   1 
ATOM   6623  N  NH2   . ARG A 1 2285 ? 81.787  72.900  118.591 1.00 7.65   ? 2285 ARG A NH2   1 
ATOM   6624  N  N     . LYS A 1 2286 ? 85.031  73.823  125.735 1.00 2.77   ? 2286 LYS A N     1 
ATOM   6625  C  CA    . LYS A 1 2286 ? 85.603  73.219  126.933 1.00 3.97   ? 2286 LYS A CA    1 
ATOM   6626  C  C     . LYS A 1 2286 ? 84.949  73.772  128.192 1.00 3.89   ? 2286 LYS A C     1 
ATOM   6627  O  O     . LYS A 1 2286 ? 84.677  73.025  129.139 1.00 4.27   ? 2286 LYS A O     1 
ATOM   6628  C  CB    . LYS A 1 2286 ? 87.113  73.457  126.967 1.00 5.06   ? 2286 LYS A CB    1 
ATOM   6629  C  CG    . LYS A 1 2286 ? 87.900  72.397  127.714 1.00 6.39   ? 2286 LYS A CG    1 
ATOM   6630  C  CD    . LYS A 1 2286 ? 89.333  72.848  127.947 1.00 11.57  ? 2286 LYS A CD    1 
ATOM   6631  C  CE    . LYS A 1 2286 ? 90.252  71.668  128.215 1.00 16.44  ? 2286 LYS A CE    1 
ATOM   6632  N  NZ    . LYS A 1 2286 ? 89.550  70.570  128.933 1.00 21.20  ? 2286 LYS A NZ    1 
ATOM   6633  N  N     . ILE A 1 2287 ? 84.699  75.082  128.224 1.00 2.80   ? 2287 ILE A N     1 
ATOM   6634  C  CA    . ILE A 1 2287 ? 84.029  75.670  129.382 1.00 3.23   ? 2287 ILE A CA    1 
ATOM   6635  C  C     . ILE A 1 2287 ? 82.603  75.141  129.510 1.00 4.02   ? 2287 ILE A C     1 
ATOM   6636  O  O     . ILE A 1 2287 ? 82.151  74.802  130.611 1.00 4.87   ? 2287 ILE A O     1 
ATOM   6637  C  CB    . ILE A 1 2287 ? 84.061  77.207  129.302 1.00 3.65   ? 2287 ILE A CB    1 
ATOM   6638  C  CG1   . ILE A 1 2287 ? 85.505  77.712  129.331 1.00 2.16   ? 2287 ILE A CG1   1 
ATOM   6639  C  CG2   . ILE A 1 2287 ? 83.262  77.812  130.443 1.00 2.50   ? 2287 ILE A CG2   1 
ATOM   6640  C  CD1   . ILE A 1 2287 ? 85.650  79.169  128.957 1.00 1.35   ? 2287 ILE A CD1   1 
ATOM   6641  N  N     . ILE A 1 2288 ? 81.875  75.059  128.394 1.00 3.99   ? 2288 ILE A N     1 
ATOM   6642  C  CA    . ILE A 1 2288 ? 80.486  74.604  128.434 1.00 4.56   ? 2288 ILE A CA    1 
ATOM   6643  C  C     . ILE A 1 2288 ? 80.401  73.147  128.874 1.00 6.15   ? 2288 ILE A C     1 
ATOM   6644  O  O     . ILE A 1 2288 ? 79.551  72.785  129.697 1.00 7.90   ? 2288 ILE A O     1 
ATOM   6645  C  CB    . ILE A 1 2288 ? 79.806  74.820  127.069 1.00 6.33   ? 2288 ILE A CB    1 
ATOM   6646  C  CG1   . ILE A 1 2288 ? 79.729  76.308  126.729 1.00 4.77   ? 2288 ILE A CG1   1 
ATOM   6647  C  CG2   . ILE A 1 2288 ? 78.419  74.196  127.053 1.00 4.45   ? 2288 ILE A CG2   1 
ATOM   6648  C  CD1   . ILE A 1 2288 ? 79.458  76.577  125.267 1.00 3.13   ? 2288 ILE A CD1   1 
ATOM   6649  N  N     . ASP A 1 2289 ? 81.270  72.290  128.334 1.00 7.32   ? 2289 ASP A N     1 
ATOM   6650  C  CA    . ASP A 1 2289 ? 81.218  70.870  128.672 1.00 7.22   ? 2289 ASP A CA    1 
ATOM   6651  C  C     . ASP A 1 2289 ? 81.484  70.646  130.154 1.00 8.79   ? 2289 ASP A C     1 
ATOM   6652  O  O     . ASP A 1 2289 ? 80.874  69.767  130.775 1.00 13.21  ? 2289 ASP A O     1 
ATOM   6653  C  CB    . ASP A 1 2289 ? 82.217  70.089  127.819 1.00 9.26   ? 2289 ASP A CB    1 
ATOM   6654  C  CG    . ASP A 1 2289 ? 81.803  70.013  126.362 1.00 18.86  ? 2289 ASP A CG    1 
ATOM   6655  O  OD1   . ASP A 1 2289 ? 80.589  70.108  126.082 1.00 20.86  ? 2289 ASP A OD1   1 
ATOM   6656  O  OD2   . ASP A 1 2289 ? 82.689  69.857  125.497 1.00 22.69  ? 2289 ASP A OD2   1 
ATOM   6657  N  N     . SER A 1 2290 ? 82.391  71.434  130.735 1.00 5.99   ? 2290 SER A N     1 
ATOM   6658  C  CA    . SER A 1 2290 ? 82.668  71.414  132.172 1.00 7.39   ? 2290 SER A CA    1 
ATOM   6659  C  C     . SER A 1 2290 ? 83.078  70.020  132.645 1.00 9.49   ? 2290 SER A C     1 
ATOM   6660  O  O     . SER A 1 2290 ? 82.589  69.510  133.656 1.00 9.00   ? 2290 SER A O     1 
ATOM   6661  C  CB    . SER A 1 2290 ? 81.470  71.933  132.968 1.00 8.13   ? 2290 SER A CB    1 
ATOM   6662  O  OG    . SER A 1 2290 ? 81.834  72.228  134.305 1.00 11.49  ? 2290 SER A OG    1 
ATOM   6663  N  N     . VAL A 1 2291 ? 83.989  69.399  131.895 1.00 9.77   ? 2291 VAL A N     1 
ATOM   6664  C  CA    . VAL A 1 2291 ? 84.528  68.107  132.305 1.00 10.79  ? 2291 VAL A CA    1 
ATOM   6665  C  C     . VAL A 1 2291 ? 85.317  68.249  133.600 1.00 12.91  ? 2291 VAL A C     1 
ATOM   6666  O  O     . VAL A 1 2291 ? 85.253  67.384  134.482 1.00 14.45  ? 2291 VAL A O     1 
ATOM   6667  C  CB    . VAL A 1 2291 ? 85.385  67.507  131.174 1.00 10.49  ? 2291 VAL A CB    1 
ATOM   6668  C  CG1   . VAL A 1 2291 ? 86.241  66.361  131.692 1.00 8.95   ? 2291 VAL A CG1   1 
ATOM   6669  C  CG2   . VAL A 1 2291 ? 84.499  67.041  130.029 1.00 11.53  ? 2291 VAL A CG2   1 
ATOM   6670  N  N     . ARG A 1 2292 ? 86.053  69.349  133.747 1.00 9.48   ? 2292 ARG A N     1 
ATOM   6671  C  CA    . ARG A 1 2292 ? 86.894  69.591  134.912 1.00 10.46  ? 2292 ARG A CA    1 
ATOM   6672  C  C     . ARG A 1 2292 ? 86.408  70.792  135.719 1.00 13.58  ? 2292 ARG A C     1 
ATOM   6673  O  O     . ARG A 1 2292 ? 87.212  71.543  136.275 1.00 13.12  ? 2292 ARG A O     1 
ATOM   6674  C  CB    . ARG A 1 2292 ? 88.350  69.769  134.484 1.00 12.42  ? 2292 ARG A CB    1 
ATOM   6675  C  CG    . ARG A 1 2292 ? 88.885  68.580  133.701 1.00 14.66  ? 2292 ARG A CG    1 
ATOM   6676  C  CD    . ARG A 1 2292 ? 90.265  68.841  133.119 1.00 14.43  ? 2292 ARG A CD    1 
ATOM   6677  N  NE    . ARG A 1 2292 ? 90.757  67.707  132.344 1.00 18.32  ? 2292 ARG A NE    1 
ATOM   6678  C  CZ    . ARG A 1 2292 ? 90.221  67.271  131.211 1.00 15.97  ? 2292 ARG A CZ    1 
ATOM   6679  N  NH1   . ARG A 1 2292 ? 89.187  67.881  130.652 1.00 15.97  ? 2292 ARG A NH1   1 
ATOM   6680  N  NH2   . ARG A 1 2292 ? 90.740  66.200  130.618 1.00 12.84  ? 2292 ARG A NH2   1 
ATOM   6681  N  N     . GLY A 1 2293 ? 85.094  70.978  135.791 1.00 10.70  ? 2293 GLY A N     1 
ATOM   6682  C  CA    . GLY A 1 2293 ? 84.510  72.027  136.611 1.00 9.65   ? 2293 GLY A CA    1 
ATOM   6683  C  C     . GLY A 1 2293 ? 84.773  73.445  136.151 1.00 12.05  ? 2293 GLY A C     1 
ATOM   6684  O  O     . GLY A 1 2293 ? 85.005  74.328  136.986 1.00 14.10  ? 2293 GLY A O     1 
ATOM   6685  N  N     . GLU A 1 2294 ? 84.741  73.689  134.839 1.00 10.74  ? 2294 GLU A N     1 
ATOM   6686  C  CA    . GLU A 1 2294 ? 84.907  75.050  134.336 1.00 7.73   ? 2294 GLU A CA    1 
ATOM   6687  C  C     . GLU A 1 2294 ? 83.710  75.933  134.666 1.00 7.33   ? 2294 GLU A C     1 
ATOM   6688  O  O     . GLU A 1 2294 ? 83.872  77.144  134.855 1.00 7.66   ? 2294 GLU A O     1 
ATOM   6689  C  CB    . GLU A 1 2294 ? 85.158  75.037  132.825 1.00 5.67   ? 2294 GLU A CB    1 
ATOM   6690  C  CG    . GLU A 1 2294 ? 86.469  74.385  132.370 1.00 6.90   ? 2294 GLU A CG    1 
ATOM   6691  C  CD    . GLU A 1 2294 ? 86.509  72.873  132.528 1.00 9.85   ? 2294 GLU A CD    1 
ATOM   6692  O  OE1   . GLU A 1 2294 ? 85.556  72.290  133.081 1.00 8.81   ? 2294 GLU A OE1   1 
ATOM   6693  O  OE2   . GLU A 1 2294 ? 87.508  72.266  132.091 1.00 12.55  ? 2294 GLU A OE2   1 
ATOM   6694  N  N     . LEU A 1 2295 ? 82.506  75.358  134.741 1.00 7.81   ? 2295 LEU A N     1 
ATOM   6695  C  CA    . LEU A 1 2295 ? 81.315  76.162  134.995 1.00 6.95   ? 2295 LEU A CA    1 
ATOM   6696  C  C     . LEU A 1 2295 ? 81.261  76.705  136.417 1.00 8.00   ? 2295 LEU A C     1 
ATOM   6697  O  O     . LEU A 1 2295 ? 80.507  77.649  136.675 1.00 8.62   ? 2295 LEU A O     1 
ATOM   6698  C  CB    . LEU A 1 2295 ? 80.051  75.350  134.710 1.00 8.61   ? 2295 LEU A CB    1 
ATOM   6699  C  CG    . LEU A 1 2295 ? 79.756  75.039  133.242 1.00 9.88   ? 2295 LEU A CG    1 
ATOM   6700  C  CD1   . LEU A 1 2295 ? 78.532  74.146  133.118 1.00 8.30   ? 2295 LEU A CD1   1 
ATOM   6701  C  CD2   . LEU A 1 2295 ? 79.577  76.320  132.449 1.00 5.14   ? 2295 LEU A CD2   1 
ATOM   6702  N  N     . GLN A 1 2296 ? 82.034  76.140  137.339 1.00 10.83  ? 2296 GLN A N     1 
ATOM   6703  C  CA    . GLN A 1 2296 ? 82.060  76.612  138.717 1.00 11.07  ? 2296 GLN A CA    1 
ATOM   6704  C  C     . GLN A 1 2296 ? 83.121  77.678  138.954 1.00 11.97  ? 2296 GLN A C     1 
ATOM   6705  O  O     . GLN A 1 2296 ? 83.237  78.177  140.078 1.00 19.34  ? 2296 GLN A O     1 
ATOM   6706  C  CB    . GLN A 1 2296 ? 82.285  75.439  139.678 1.00 10.97  ? 2296 GLN A CB    1 
ATOM   6707  C  CG    . GLN A 1 2296 ? 81.575  74.150  139.287 1.00 12.48  ? 2296 GLN A CG    1 
ATOM   6708  C  CD    . GLN A 1 2296 ? 80.120  74.369  138.917 1.00 15.23  ? 2296 GLN A CD    1 
ATOM   6709  O  OE1   . GLN A 1 2296 ? 79.687  74.018  137.819 1.00 14.19  ? 2296 GLN A OE1   1 
ATOM   6710  N  NE2   . GLN A 1 2296 ? 79.356  74.950  139.835 1.00 17.64  ? 2296 GLN A NE2   1 
ATOM   6711  N  N     . LYS A 1 2297 ? 83.889  78.037  137.932 1.00 11.15  ? 2297 LYS A N     1 
ATOM   6712  C  CA    . LYS A 1 2297 ? 84.929  79.046  138.036 1.00 7.56   ? 2297 LYS A CA    1 
ATOM   6713  C  C     . LYS A 1 2297 ? 84.552  80.276  137.222 1.00 4.70   ? 2297 LYS A C     1 
ATOM   6714  O  O     . LYS A 1 2297 ? 83.741  80.213  136.294 1.00 5.52   ? 2297 LYS A O     1 
ATOM   6715  C  CB    . LYS A 1 2297 ? 86.275  78.502  137.546 1.00 9.02   ? 2297 LYS A CB    1 
ATOM   6716  C  CG    . LYS A 1 2297 ? 86.698  77.194  138.185 1.00 15.06  ? 2297 LYS A CG    1 
ATOM   6717  C  CD    . LYS A 1 2297 ? 87.986  76.683  137.562 1.00 16.41  ? 2297 LYS A CD    1 
ATOM   6718  C  CE    . LYS A 1 2297 ? 88.351  75.307  138.090 1.00 21.06  ? 2297 LYS A CE    1 
ATOM   6719  N  NZ    . LYS A 1 2297 ? 89.634  74.822  137.514 1.00 21.57  ? 2297 LYS A NZ    1 
ATOM   6720  N  N     . ARG A 1 2298 ? 85.153  81.405  137.586 1.00 5.24   ? 2298 ARG A N     1 
ATOM   6721  C  CA    . ARG A 1 2298 ? 85.050  82.612  136.778 1.00 3.74   ? 2298 ARG A CA    1 
ATOM   6722  C  C     . ARG A 1 2298 ? 85.936  82.443  135.550 1.00 3.23   ? 2298 ARG A C     1 
ATOM   6723  O  O     . ARG A 1 2298 ? 87.116  82.105  135.676 1.00 3.28   ? 2298 ARG A O     1 
ATOM   6724  C  CB    . ARG A 1 2298 ? 85.462  83.837  137.591 1.00 3.80   ? 2298 ARG A CB    1 
ATOM   6725  C  CG    . ARG A 1 2298 ? 85.646  85.100  136.767 1.00 4.37   ? 2298 ARG A CG    1 
ATOM   6726  C  CD    . ARG A 1 2298 ? 85.785  86.327  137.654 1.00 3.46   ? 2298 ARG A CD    1 
ATOM   6727  N  NE    . ARG A 1 2298 ? 84.503  86.779  138.180 1.00 6.26   ? 2298 ARG A NE    1 
ATOM   6728  C  CZ    . ARG A 1 2298 ? 84.141  86.686  139.452 1.00 7.39   ? 2298 ARG A CZ    1 
ATOM   6729  N  NH1   . ARG A 1 2298 ? 84.941  86.156  140.362 1.00 5.00   ? 2298 ARG A NH1   1 
ATOM   6730  N  NH2   . ARG A 1 2298 ? 82.946  87.138  139.821 1.00 9.55   ? 2298 ARG A NH2   1 
ATOM   6731  N  N     . GLN A 1 2299 ? 85.366  82.648  134.367 1.00 2.54   ? 2299 GLN A N     1 
ATOM   6732  C  CA    . GLN A 1 2299 ? 86.063  82.418  133.105 1.00 1.95   ? 2299 GLN A CA    1 
ATOM   6733  C  C     . GLN A 1 2299 ? 86.083  83.720  132.316 1.00 1.74   ? 2299 GLN A C     1 
ATOM   6734  O  O     . GLN A 1 2299 ? 85.035  84.193  131.864 1.00 2.96   ? 2299 GLN A O     1 
ATOM   6735  C  CB    . GLN A 1 2299 ? 85.388  81.304  132.307 1.00 2.12   ? 2299 GLN A CB    1 
ATOM   6736  C  CG    . GLN A 1 2299 ? 85.338  79.963  133.024 1.00 2.35   ? 2299 GLN A CG    1 
ATOM   6737  C  CD    . GLN A 1 2299 ? 86.644  79.199  132.935 1.00 2.60   ? 2299 GLN A CD    1 
ATOM   6738  O  OE1   . GLN A 1 2299 ? 87.606  79.658  132.321 1.00 3.61   ? 2299 GLN A OE1   1 
ATOM   6739  N  NE2   . GLN A 1 2299 ? 86.683  78.026  133.553 1.00 3.90   ? 2299 GLN A NE2   1 
ATOM   6740  N  N     . TRP A 1 2300 ? 87.269  84.298  132.150 1.00 1.57   ? 2300 TRP A N     1 
ATOM   6741  C  CA    . TRP A 1 2300 ? 87.441  85.528  131.387 1.00 1.82   ? 2300 TRP A CA    1 
ATOM   6742  C  C     . TRP A 1 2300 ? 88.176  85.213  130.092 1.00 1.83   ? 2300 TRP A C     1 
ATOM   6743  O  O     . TRP A 1 2300 ? 89.336  84.791  130.121 1.00 2.17   ? 2300 TRP A O     1 
ATOM   6744  C  CB    . TRP A 1 2300 ? 88.202  86.577  132.197 1.00 1.95   ? 2300 TRP A CB    1 
ATOM   6745  C  CG    . TRP A 1 2300 ? 87.380  87.226  133.265 1.00 2.03   ? 2300 TRP A CG    1 
ATOM   6746  C  CD1   . TRP A 1 2300 ? 86.087  86.940  133.592 1.00 1.72   ? 2300 TRP A CD1   1 
ATOM   6747  C  CD2   . TRP A 1 2300 ? 87.792  88.279  134.143 1.00 2.55   ? 2300 TRP A CD2   1 
ATOM   6748  N  NE1   . TRP A 1 2300 ? 85.669  87.747  134.621 1.00 2.10   ? 2300 TRP A NE1   1 
ATOM   6749  C  CE2   . TRP A 1 2300 ? 86.697  88.580  134.977 1.00 2.43   ? 2300 TRP A CE2   1 
ATOM   6750  C  CE3   . TRP A 1 2300 ? 88.979  89.000  134.303 1.00 2.04   ? 2300 TRP A CE3   1 
ATOM   6751  C  CZ2   . TRP A 1 2300 ? 86.755  89.566  135.958 1.00 1.78   ? 2300 TRP A CZ2   1 
ATOM   6752  C  CZ3   . TRP A 1 2300 ? 89.034  89.978  135.277 1.00 1.98   ? 2300 TRP A CZ3   1 
ATOM   6753  C  CH2   . TRP A 1 2300 ? 87.930  90.252  136.093 1.00 2.35   ? 2300 TRP A CH2   1 
ATOM   6754  N  N     . ILE A 1 2301 ? 87.510  85.438  128.966 1.00 1.29   ? 2301 ILE A N     1 
ATOM   6755  C  CA    . ILE A 1 2301 ? 88.092  85.246  127.644 1.00 1.52   ? 2301 ILE A CA    1 
ATOM   6756  C  C     . ILE A 1 2301 ? 88.476  86.622  127.119 1.00 1.73   ? 2301 ILE A C     1 
ATOM   6757  O  O     . ILE A 1 2301 ? 87.607  87.423  126.752 1.00 2.26   ? 2301 ILE A O     1 
ATOM   6758  C  CB    . ILE A 1 2301 ? 87.125  84.530  126.693 1.00 1.92   ? 2301 ILE A CB    1 
ATOM   6759  C  CG1   . ILE A 1 2301 ? 86.709  83.179  127.280 1.00 1.97   ? 2301 ILE A CG1   1 
ATOM   6760  C  CG2   . ILE A 1 2301 ? 87.753  84.356  125.325 1.00 1.52   ? 2301 ILE A CG2   1 
ATOM   6761  C  CD1   . ILE A 1 2301 ? 85.599  82.494  126.520 1.00 1.96   ? 2301 ILE A CD1   1 
ATOM   6762  N  N     . VAL A 1 2302 ? 89.775  86.901  127.085 1.00 1.48   ? 2302 VAL A N     1 
ATOM   6763  C  CA    . VAL A 1 2302 ? 90.288  88.226  126.760 1.00 2.01   ? 2302 VAL A CA    1 
ATOM   6764  C  C     . VAL A 1 2302 ? 90.923  88.181  125.377 1.00 1.68   ? 2302 VAL A C     1 
ATOM   6765  O  O     . VAL A 1 2302 ? 91.930  87.494  125.169 1.00 1.77   ? 2302 VAL A O     1 
ATOM   6766  C  CB    . VAL A 1 2302 ? 91.298  88.706  127.813 1.00 1.99   ? 2302 VAL A CB    1 
ATOM   6767  C  CG1   . VAL A 1 2302 ? 91.732  90.134  127.520 1.00 1.82   ? 2302 VAL A CG1   1 
ATOM   6768  C  CG2   . VAL A 1 2302 ? 90.700  88.597  129.207 1.00 1.27   ? 2302 VAL A CG2   1 
ATOM   6769  N  N     . PHE A 1 2303 ? 90.342  88.923  124.435 1.00 1.78   ? 2303 PHE A N     1 
ATOM   6770  C  CA    . PHE A 1 2303 ? 90.935  89.105  123.111 1.00 2.03   ? 2303 PHE A CA    1 
ATOM   6771  C  C     . PHE A 1 2303 ? 91.903  90.276  123.203 1.00 2.56   ? 2303 PHE A C     1 
ATOM   6772  O  O     . PHE A 1 2303 ? 91.510  91.442  123.157 1.00 3.78   ? 2303 PHE A O     1 
ATOM   6773  C  CB    . PHE A 1 2303 ? 89.863  89.341  122.054 1.00 2.12   ? 2303 PHE A CB    1 
ATOM   6774  C  CG    . PHE A 1 2303 ? 89.022  88.133  121.757 1.00 2.18   ? 2303 PHE A CG    1 
ATOM   6775  C  CD1   . PHE A 1 2303 ? 89.434  87.202  120.818 1.00 3.52   ? 2303 PHE A CD1   1 
ATOM   6776  C  CD2   . PHE A 1 2303 ? 87.815  87.934  122.406 1.00 1.74   ? 2303 PHE A CD2   1 
ATOM   6777  C  CE1   . PHE A 1 2303 ? 88.663  86.090  120.540 1.00 3.34   ? 2303 PHE A CE1   1 
ATOM   6778  C  CE2   . PHE A 1 2303 ? 87.039  86.825  122.131 1.00 1.89   ? 2303 PHE A CE2   1 
ATOM   6779  C  CZ    . PHE A 1 2303 ? 87.464  85.902  121.197 1.00 2.04   ? 2303 PHE A CZ    1 
ATOM   6780  N  N     . ASP A 1 2304 ? 93.188  89.961  123.336 1.00 2.71   ? 2304 ASP A N     1 
ATOM   6781  C  CA    . ASP A 1 2304 ? 94.232  90.974  123.473 1.00 3.89   ? 2304 ASP A CA    1 
ATOM   6782  C  C     . ASP A 1 2304 ? 94.857  91.186  122.101 1.00 3.92   ? 2304 ASP A C     1 
ATOM   6783  O  O     . ASP A 1 2304 ? 95.829  90.531  121.724 1.00 5.19   ? 2304 ASP A O     1 
ATOM   6784  C  CB    . ASP A 1 2304 ? 95.265  90.541  124.508 1.00 5.13   ? 2304 ASP A CB    1 
ATOM   6785  C  CG    . ASP A 1 2304 ? 96.320  91.603  124.772 1.00 5.72   ? 2304 ASP A CG    1 
ATOM   6786  O  OD1   . ASP A 1 2304 ? 96.237  92.705  124.191 1.00 5.75   ? 2304 ASP A OD1   1 
ATOM   6787  O  OD2   . ASP A 1 2304 ? 97.241  91.329  125.569 1.00 7.02   ? 2304 ASP A OD2   1 
ATOM   6788  N  N     . GLY A 1 2305 ? 94.287  92.113  121.342 1.00 3.73   ? 2305 GLY A N     1 
ATOM   6789  C  CA    . GLY A 1 2305 ? 94.785  92.377  120.007 1.00 5.68   ? 2305 GLY A CA    1 
ATOM   6790  C  C     . GLY A 1 2305 ? 93.875  93.333  119.269 1.00 5.83   ? 2305 GLY A C     1 
ATOM   6791  O  O     . GLY A 1 2305 ? 92.980  93.948  119.851 1.00 7.28   ? 2305 GLY A O     1 
ATOM   6792  N  N     . ASP A 1 2306 ? 94.120  93.446  117.966 1.00 5.38   ? 2306 ASP A N     1 
ATOM   6793  C  CA    . ASP A 1 2306 ? 93.368  94.360  117.120 1.00 6.64   ? 2306 ASP A CA    1 
ATOM   6794  C  C     . ASP A 1 2306 ? 91.975  93.815  116.827 1.00 7.17   ? 2306 ASP A C     1 
ATOM   6795  O  O     . ASP A 1 2306 ? 91.774  92.607  116.677 1.00 8.97   ? 2306 ASP A O     1 
ATOM   6796  C  CB    . ASP A 1 2306 ? 94.113  94.609  115.809 1.00 8.46   ? 2306 ASP A CB    1 
ATOM   6797  C  CG    . ASP A 1 2306 ? 95.416  95.356  116.010 1.00 13.89  ? 2306 ASP A CG    1 
ATOM   6798  O  OD1   . ASP A 1 2306 ? 95.580  95.996  117.070 1.00 18.65  ? 2306 ASP A OD1   1 
ATOM   6799  O  OD2   . ASP A 1 2306 ? 96.278  95.303  115.108 1.00 13.74  ? 2306 ASP A OD2   1 
ATOM   6800  N  N     . VAL A 1 2307 ? 91.008  94.725  116.749 1.00 6.82   ? 2307 VAL A N     1 
ATOM   6801  C  CA    . VAL A 1 2307 ? 89.622  94.392  116.439 1.00 6.83   ? 2307 VAL A CA    1 
ATOM   6802  C  C     . VAL A 1 2307 ? 89.312  94.895  115.036 1.00 7.98   ? 2307 VAL A C     1 
ATOM   6803  O  O     . VAL A 1 2307 ? 89.523  96.075  114.731 1.00 11.92  ? 2307 VAL A O     1 
ATOM   6804  C  CB    . VAL A 1 2307 ? 88.649  94.992  117.466 1.00 5.43   ? 2307 VAL A CB    1 
ATOM   6805  C  CG1   . VAL A 1 2307 ? 87.234  95.013  116.910 1.00 6.74   ? 2307 VAL A CG1   1 
ATOM   6806  C  CG2   . VAL A 1 2307 ? 88.692  94.198  118.759 1.00 3.55   ? 2307 VAL A CG2   1 
ATOM   6807  N  N     . ASP A 1 2308 ? 88.818  94.006  114.187 1.00 6.61   ? 2308 ASP A N     1 
ATOM   6808  C  CA    . ASP A 1 2308 ? 88.338  94.352  112.860 1.00 8.21   ? 2308 ASP A CA    1 
ATOM   6809  C  C     . ASP A 1 2308 ? 87.021  93.638  112.598 1.00 8.78   ? 2308 ASP A C     1 
ATOM   6810  O  O     . ASP A 1 2308 ? 86.727  92.615  113.227 1.00 7.18   ? 2308 ASP A O     1 
ATOM   6811  C  CB    . ASP A 1 2308 ? 89.398  94.039  111.783 1.00 8.17   ? 2308 ASP A CB    1 
ATOM   6812  C  CG    . ASP A 1 2308 ? 89.568  92.543  111.468 1.00 11.96  ? 2308 ASP A CG    1 
ATOM   6813  O  OD1   . ASP A 1 2308 ? 88.687  91.704  111.729 1.00 14.10  ? 2308 ASP A OD1   1 
ATOM   6814  O  OD2   . ASP A 1 2308 ? 90.642  92.202  110.932 1.00 15.00  ? 2308 ASP A OD2   1 
ATOM   6815  N  N     . PRO A 1 2309 ? 86.185  94.172  111.703 1.00 11.16  ? 2309 PRO A N     1 
ATOM   6816  C  CA    . PRO A 1 2309 ? 84.858  93.566  111.492 1.00 9.99   ? 2309 PRO A CA    1 
ATOM   6817  C  C     . PRO A 1 2309 ? 84.900  92.144  110.960 1.00 11.40  ? 2309 PRO A C     1 
ATOM   6818  O  O     . PRO A 1 2309 ? 83.912  91.418  111.115 1.00 13.56  ? 2309 PRO A O     1 
ATOM   6819  C  CB    . PRO A 1 2309 ? 84.192  94.519  110.490 1.00 11.20  ? 2309 PRO A CB    1 
ATOM   6820  C  CG    . PRO A 1 2309 ? 85.318  95.237  109.833 1.00 11.90  ? 2309 PRO A CG    1 
ATOM   6821  C  CD    . PRO A 1 2309 ? 86.370  95.382  110.885 1.00 9.91   ? 2309 PRO A CD    1 
ATOM   6822  N  N     . GLU A 1 2310 ? 86.003  91.722  110.337 1.00 12.20  ? 2310 GLU A N     1 
ATOM   6823  C  CA    . GLU A 1 2310 ? 86.055  90.385  109.753 1.00 14.36  ? 2310 GLU A CA    1 
ATOM   6824  C  C     . GLU A 1 2310 ? 85.911  89.299  110.813 1.00 14.78  ? 2310 GLU A C     1 
ATOM   6825  O  O     . GLU A 1 2310 ? 85.174  88.326  110.615 1.00 21.01  ? 2310 GLU A O     1 
ATOM   6826  C  CB    . GLU A 1 2310 ? 87.356  90.203  108.973 1.00 21.26  ? 2310 GLU A CB    1 
ATOM   6827  C  CG    . GLU A 1 2310 ? 87.480  91.112  107.765 1.00 28.30  ? 2310 GLU A CG    1 
ATOM   6828  C  CD    . GLU A 1 2310 ? 87.222  90.387  106.460 1.00 48.12  ? 2310 GLU A CD    1 
ATOM   6829  O  OE1   . GLU A 1 2310 ? 86.914  89.177  106.502 1.00 55.13  ? 2310 GLU A OE1   1 
ATOM   6830  O  OE2   . GLU A 1 2310 ? 87.327  91.026  105.392 1.00 50.04  ? 2310 GLU A OE2   1 
ATOM   6831  N  N     . TRP A 1 2311 ? 86.600  89.444  111.944 1.00 9.56   ? 2311 TRP A N     1 
ATOM   6832  C  CA    . TRP A 1 2311 ? 86.572  88.414  112.975 1.00 6.79   ? 2311 TRP A CA    1 
ATOM   6833  C  C     . TRP A 1 2311 ? 85.630  88.729  114.128 1.00 6.23   ? 2311 TRP A C     1 
ATOM   6834  O  O     . TRP A 1 2311 ? 85.057  87.802  114.708 1.00 10.38  ? 2311 TRP A O     1 
ATOM   6835  C  CB    . TRP A 1 2311 ? 87.985  88.166  113.526 1.00 5.14   ? 2311 TRP A CB    1 
ATOM   6836  C  CG    . TRP A 1 2311 ? 88.486  89.211  114.486 1.00 5.35   ? 2311 TRP A CG    1 
ATOM   6837  C  CD1   . TRP A 1 2311 ? 89.260  90.292  114.187 1.00 4.04   ? 2311 TRP A CD1   1 
ATOM   6838  C  CD2   . TRP A 1 2311 ? 88.272  89.253  115.903 1.00 4.84   ? 2311 TRP A CD2   1 
ATOM   6839  N  NE1   . TRP A 1 2311 ? 89.527  91.015  115.321 1.00 5.99   ? 2311 TRP A NE1   1 
ATOM   6840  C  CE2   . TRP A 1 2311 ? 88.933  90.398  116.390 1.00 4.33   ? 2311 TRP A CE2   1 
ATOM   6841  C  CE3   . TRP A 1 2311 ? 87.580  88.440  116.804 1.00 3.75   ? 2311 TRP A CE3   1 
ATOM   6842  C  CZ2   . TRP A 1 2311 ? 88.921  90.750  117.736 1.00 3.61   ? 2311 TRP A CZ2   1 
ATOM   6843  C  CZ3   . TRP A 1 2311 ? 87.571  88.790  118.140 1.00 2.86   ? 2311 TRP A CZ3   1 
ATOM   6844  C  CH2   . TRP A 1 2311 ? 88.239  89.933  118.594 1.00 2.40   ? 2311 TRP A CH2   1 
ATOM   6845  N  N     . VAL A 1 2312 ? 85.446  90.002  114.477 1.00 4.53   ? 2312 VAL A N     1 
ATOM   6846  C  CA    . VAL A 1 2312 ? 84.669  90.307  115.674 1.00 4.99   ? 2312 VAL A CA    1 
ATOM   6847  C  C     . VAL A 1 2312 ? 83.169  90.212  115.401 1.00 6.82   ? 2312 VAL A C     1 
ATOM   6848  O  O     . VAL A 1 2312 ? 82.381  90.014  116.333 1.00 6.55   ? 2312 VAL A O     1 
ATOM   6849  C  CB    . VAL A 1 2312 ? 85.052  91.690  116.233 1.00 5.42   ? 2312 VAL A CB    1 
ATOM   6850  C  CG1   . VAL A 1 2312 ? 84.450  92.807  115.390 1.00 6.42   ? 2312 VAL A CG1   1 
ATOM   6851  C  CG2   . VAL A 1 2312 ? 84.639  91.811  117.693 1.00 3.40   ? 2312 VAL A CG2   1 
ATOM   6852  N  N     . GLU A 1 2313 ? 82.744  90.336  114.142 1.00 7.10   ? 2313 GLU A N     1 
ATOM   6853  C  CA    . GLU A 1 2313 ? 81.319  90.253  113.843 1.00 7.43   ? 2313 GLU A CA    1 
ATOM   6854  C  C     . GLU A 1 2313 ? 80.778  88.833  113.925 1.00 6.91   ? 2313 GLU A C     1 
ATOM   6855  O  O     . GLU A 1 2313 ? 79.556  88.658  113.945 1.00 8.37   ? 2313 GLU A O     1 
ATOM   6856  C  CB    . GLU A 1 2313 ? 81.022  90.842  112.464 1.00 10.06  ? 2313 GLU A CB    1 
ATOM   6857  C  CG    . GLU A 1 2313 ? 80.666  92.318  112.508 1.00 12.90  ? 2313 GLU A CG    1 
ATOM   6858  C  CD    . GLU A 1 2313 ? 81.094  93.067  111.265 1.00 24.95  ? 2313 GLU A CD    1 
ATOM   6859  O  OE1   . GLU A 1 2313 ? 81.433  92.410  110.258 1.00 26.93  ? 2313 GLU A OE1   1 
ATOM   6860  O  OE2   . GLU A 1 2313 ? 81.085  94.315  111.294 1.00 23.14  ? 2313 GLU A OE2   1 
ATOM   6861  N  N     . ASN A 1 2314 ? 81.646  87.820  113.971 1.00 6.86   ? 2314 ASN A N     1 
ATOM   6862  C  CA    . ASN A 1 2314 ? 81.196  86.478  114.314 1.00 5.79   ? 2314 ASN A CA    1 
ATOM   6863  C  C     . ASN A 1 2314 ? 80.710  86.386  115.753 1.00 4.98   ? 2314 ASN A C     1 
ATOM   6864  O  O     . ASN A 1 2314 ? 80.056  85.401  116.109 1.00 7.76   ? 2314 ASN A O     1 
ATOM   6865  C  CB    . ASN A 1 2314 ? 82.317  85.464  114.083 1.00 6.45   ? 2314 ASN A CB    1 
ATOM   6866  C  CG    . ASN A 1 2314 ? 82.550  85.178  112.614 1.00 8.66   ? 2314 ASN A CG    1 
ATOM   6867  O  OD1   . ASN A 1 2314 ? 82.562  86.087  111.786 1.00 13.25  ? 2314 ASN A OD1   1 
ATOM   6868  N  ND2   . ASN A 1 2314 ? 82.737  83.906  112.283 1.00 6.07   ? 2314 ASN A ND2   1 
ATOM   6869  N  N     . LEU A 1 2315 ? 81.017  87.385  116.579 1.00 4.50   ? 2315 LEU A N     1 
ATOM   6870  C  CA    . LEU A 1 2315 ? 80.583  87.442  117.965 1.00 4.62   ? 2315 LEU A CA    1 
ATOM   6871  C  C     . LEU A 1 2315 ? 79.366  88.335  118.160 1.00 5.64   ? 2315 LEU A C     1 
ATOM   6872  O  O     . LEU A 1 2315 ? 79.036  88.669  119.301 1.00 6.41   ? 2315 LEU A O     1 
ATOM   6873  C  CB    . LEU A 1 2315 ? 81.731  87.927  118.852 1.00 4.37   ? 2315 LEU A CB    1 
ATOM   6874  C  CG    . LEU A 1 2315 ? 83.023  87.113  118.776 1.00 3.78   ? 2315 LEU A CG    1 
ATOM   6875  C  CD1   . LEU A 1 2315 ? 84.110  87.739  119.633 1.00 2.61   ? 2315 LEU A CD1   1 
ATOM   6876  C  CD2   . LEU A 1 2315 ? 82.764  85.679  119.192 1.00 2.80   ? 2315 LEU A CD2   1 
ATOM   6877  N  N     . ASN A 1 2316 ? 78.704  88.745  117.075 1.00 5.38   ? 2316 ASN A N     1 
ATOM   6878  C  CA    . ASN A 1 2316 ? 77.530  89.603  117.205 1.00 5.02   ? 2316 ASN A CA    1 
ATOM   6879  C  C     . ASN A 1 2316 ? 76.429  88.917  118.002 1.00 4.60   ? 2316 ASN A C     1 
ATOM   6880  O  O     . ASN A 1 2316 ? 75.808  89.533  118.875 1.00 6.00   ? 2316 ASN A O     1 
ATOM   6881  C  CB    . ASN A 1 2316 ? 77.018  90.012  115.824 1.00 6.31   ? 2316 ASN A CB    1 
ATOM   6882  C  CG    . ASN A 1 2316 ? 77.670  91.280  115.312 1.00 8.71   ? 2316 ASN A CG    1 
ATOM   6883  O  OD1   . ASN A 1 2316 ? 78.472  91.904  116.006 1.00 13.19  ? 2316 ASN A OD1   1 
ATOM   6884  N  ND2   . ASN A 1 2316 ? 77.329  91.668  114.090 1.00 11.84  ? 2316 ASN A ND2   1 
ATOM   6885  N  N     . SER A 1 2317 ? 76.176  87.639  117.724 1.00 4.54   ? 2317 SER A N     1 
ATOM   6886  C  CA    . SER A 1 2317 ? 75.178  86.892  118.477 1.00 4.88   ? 2317 SER A CA    1 
ATOM   6887  C  C     . SER A 1 2317 ? 75.672  86.469  119.855 1.00 4.58   ? 2317 SER A C     1 
ATOM   6888  O  O     . SER A 1 2317 ? 74.861  86.035  120.679 1.00 5.13   ? 2317 SER A O     1 
ATOM   6889  C  CB    . SER A 1 2317 ? 74.732  85.661  117.683 1.00 5.05   ? 2317 SER A CB    1 
ATOM   6890  O  OG    . SER A 1 2317 ? 75.818  84.785  117.440 1.00 5.05   ? 2317 SER A OG    1 
ATOM   6891  N  N     . VAL A 1 2318 ? 76.972  86.578  120.121 1.00 4.74   ? 2318 VAL A N     1 
ATOM   6892  C  CA    . VAL A 1 2318 ? 77.516  86.274  121.441 1.00 4.76   ? 2318 VAL A CA    1 
ATOM   6893  C  C     . VAL A 1 2318 ? 77.400  87.471  122.377 1.00 4.29   ? 2318 VAL A C     1 
ATOM   6894  O  O     . VAL A 1 2318 ? 77.007  87.325  123.536 1.00 4.15   ? 2318 VAL A O     1 
ATOM   6895  C  CB    . VAL A 1 2318 ? 78.980  85.809  121.311 1.00 4.55   ? 2318 VAL A CB    1 
ATOM   6896  C  CG1   . VAL A 1 2318 ? 79.562  85.483  122.678 1.00 3.27   ? 2318 VAL A CG1   1 
ATOM   6897  C  CG2   . VAL A 1 2318 ? 79.081  84.615  120.381 1.00 3.23   ? 2318 VAL A CG2   1 
ATOM   6898  N  N     . LEU A 1 2319 ? 77.741  88.661  121.885 1.00 4.73   ? 2319 LEU A N     1 
ATOM   6899  C  CA    . LEU A 1 2319 ? 77.769  89.869  122.697 1.00 5.64   ? 2319 LEU A CA    1 
ATOM   6900  C  C     . LEU A 1 2319 ? 76.390  90.479  122.919 1.00 8.28   ? 2319 LEU A C     1 
ATOM   6901  O  O     . LEU A 1 2319 ? 76.243  91.318  123.813 1.00 9.40   ? 2319 LEU A O     1 
ATOM   6902  C  CB    . LEU A 1 2319 ? 78.691  90.903  122.045 1.00 6.28   ? 2319 LEU A CB    1 
ATOM   6903  C  CG    . LEU A 1 2319 ? 80.104  90.417  121.711 1.00 4.58   ? 2319 LEU A CG    1 
ATOM   6904  C  CD1   . LEU A 1 2319 ? 80.876  91.475  120.944 1.00 4.07   ? 2319 LEU A CD1   1 
ATOM   6905  C  CD2   . LEU A 1 2319 ? 80.848  90.029  122.977 1.00 2.51   ? 2319 LEU A CD2   1 
ATOM   6906  N  N     . ASP A 1 2320 ? 75.387  90.087  122.138 1.00 8.64   ? 2320 ASP A N     1 
ATOM   6907  C  CA    . ASP A 1 2320 ? 74.038  90.607  122.301 1.00 9.86   ? 2320 ASP A CA    1 
ATOM   6908  C  C     . ASP A 1 2320 ? 73.238  89.697  123.236 1.00 10.43  ? 2320 ASP A C     1 
ATOM   6909  O  O     . ASP A 1 2320 ? 73.789  88.831  123.920 1.00 8.85   ? 2320 ASP A O     1 
ATOM   6910  C  CB    . ASP A 1 2320 ? 73.376  90.803  120.934 1.00 6.95   ? 2320 ASP A CB    1 
ATOM   6911  C  CG    . ASP A 1 2320 ? 73.104  89.495  120.202 1.00 9.39   ? 2320 ASP A CG    1 
ATOM   6912  O  OD1   . ASP A 1 2320 ? 73.372  88.409  120.753 1.00 11.44  ? 2320 ASP A OD1   1 
ATOM   6913  O  OD2   . ASP A 1 2320 ? 72.614  89.560  119.055 1.00 10.20  ? 2320 ASP A OD2   1 
ATOM   6914  N  N     . ASP A 1 2321 ? 71.917  89.894  123.275 1.00 12.39  ? 2321 ASP A N     1 
ATOM   6915  C  CA    . ASP A 1 2321 ? 71.077  89.154  124.212 1.00 15.50  ? 2321 ASP A CA    1 
ATOM   6916  C  C     . ASP A 1 2321 ? 71.010  87.668  123.879 1.00 11.07  ? 2321 ASP A C     1 
ATOM   6917  O  O     . ASP A 1 2321 ? 70.646  86.861  124.742 1.00 12.88  ? 2321 ASP A O     1 
ATOM   6918  C  CB    . ASP A 1 2321 ? 69.669  89.748  124.233 1.00 20.17  ? 2321 ASP A CB    1 
ATOM   6919  C  CG    . ASP A 1 2321 ? 69.664  91.220  124.590 1.00 30.04  ? 2321 ASP A CG    1 
ATOM   6920  O  OD1   . ASP A 1 2321 ? 68.885  91.979  123.976 1.00 26.60  ? 2321 ASP A OD1   1 
ATOM   6921  O  OD2   . ASP A 1 2321 ? 70.439  91.617  125.486 1.00 33.08  ? 2321 ASP A OD2   1 
ATOM   6922  N  N     . ASN A 1 2322 ? 71.343  87.287  122.643 1.00 8.26   ? 2322 ASN A N     1 
ATOM   6923  C  CA    . ASN A 1 2322 ? 71.282  85.879  122.263 1.00 7.50   ? 2322 ASN A CA    1 
ATOM   6924  C  C     . ASN A 1 2322 ? 72.261  85.040  123.073 1.00 7.52   ? 2322 ASN A C     1 
ATOM   6925  O  O     . ASN A 1 2322 ? 71.937  83.917  123.479 1.00 8.07   ? 2322 ASN A O     1 
ATOM   6926  C  CB    . ASN A 1 2322 ? 71.554  85.723  120.766 1.00 7.97   ? 2322 ASN A CB    1 
ATOM   6927  C  CG    . ASN A 1 2322 ? 70.459  86.323  119.909 1.00 8.89   ? 2322 ASN A CG    1 
ATOM   6928  O  OD1   . ASN A 1 2322 ? 69.308  85.892  119.963 1.00 8.44   ? 2322 ASN A OD1   1 
ATOM   6929  N  ND2   . ASN A 1 2322 ? 70.813  87.322  119.110 1.00 6.64   ? 2322 ASN A ND2   1 
ATOM   6930  N  N     . LYS A 1 2323 ? 73.460  85.569  123.321 1.00 6.11   ? 2323 LYS A N     1 
ATOM   6931  C  CA    . LYS A 1 2323 ? 74.512  84.860  124.051 1.00 5.42   ? 2323 LYS A CA    1 
ATOM   6932  C  C     . LYS A 1 2323 ? 74.801  83.505  123.408 1.00 3.96   ? 2323 LYS A C     1 
ATOM   6933  O  O     . LYS A 1 2323 ? 74.985  82.490  124.083 1.00 5.01   ? 2323 LYS A O     1 
ATOM   6934  C  CB    . LYS A 1 2323 ? 74.142  84.699  125.527 1.00 6.11   ? 2323 LYS A CB    1 
ATOM   6935  C  CG    . LYS A 1 2323 ? 74.005  86.007  126.284 1.00 7.68   ? 2323 LYS A CG    1 
ATOM   6936  C  CD    . LYS A 1 2323 ? 73.519  85.766  127.704 1.00 11.13  ? 2323 LYS A CD    1 
ATOM   6937  C  CE    . LYS A 1 2323 ? 73.344  87.072  128.458 1.00 18.19  ? 2323 LYS A CE    1 
ATOM   6938  N  NZ    . LYS A 1 2323 ? 72.450  88.015  127.731 1.00 18.65  ? 2323 LYS A NZ    1 
ATOM   6939  N  N     . LEU A 1 2324 ? 74.835  83.498  122.079 1.00 3.86   ? 2324 LEU A N     1 
ATOM   6940  C  CA    . LEU A 1 2324 ? 74.992  82.275  121.305 1.00 3.77   ? 2324 LEU A CA    1 
ATOM   6941  C  C     . LEU A 1 2324 ? 76.076  82.469  120.258 1.00 3.86   ? 2324 LEU A C     1 
ATOM   6942  O  O     . LEU A 1 2324 ? 76.070  83.465  119.530 1.00 4.61   ? 2324 LEU A O     1 
ATOM   6943  C  CB    . LEU A 1 2324 ? 73.678  81.880  120.622 1.00 4.91   ? 2324 LEU A CB    1 
ATOM   6944  C  CG    . LEU A 1 2324 ? 72.625  81.144  121.449 1.00 5.59   ? 2324 LEU A CG    1 
ATOM   6945  C  CD1   . LEU A 1 2324 ? 71.308  81.097  120.695 1.00 8.93   ? 2324 LEU A CD1   1 
ATOM   6946  C  CD2   . LEU A 1 2324 ? 73.095  79.742  121.790 1.00 4.39   ? 2324 LEU A CD2   1 
ATOM   6947  N  N     . LEU A 1 2325 ? 76.998  81.518  120.182 1.00 3.34   ? 2325 LEU A N     1 
ATOM   6948  C  CA    . LEU A 1 2325 ? 77.944  81.432  119.078 1.00 3.31   ? 2325 LEU A CA    1 
ATOM   6949  C  C     . LEU A 1 2325 ? 77.360  80.468  118.056 1.00 3.81   ? 2325 LEU A C     1 
ATOM   6950  O  O     . LEU A 1 2325 ? 77.153  79.288  118.357 1.00 5.84   ? 2325 LEU A O     1 
ATOM   6951  C  CB    . LEU A 1 2325 ? 79.316  80.960  119.549 1.00 3.20   ? 2325 LEU A CB    1 
ATOM   6952  C  CG    . LEU A 1 2325 ? 80.304  80.761  118.397 1.00 4.07   ? 2325 LEU A CG    1 
ATOM   6953  C  CD1   . LEU A 1 2325 ? 80.717  82.097  117.793 1.00 3.62   ? 2325 LEU A CD1   1 
ATOM   6954  C  CD2   . LEU A 1 2325 ? 81.510  79.963  118.839 1.00 2.55   ? 2325 LEU A CD2   1 
ATOM   6955  N  N     . THR A 1 2326 ? 77.085  80.969  116.856 1.00 3.58   ? 2326 THR A N     1 
ATOM   6956  C  CA    . THR A 1 2326 ? 76.501  80.153  115.803 1.00 7.46   ? 2326 THR A CA    1 
ATOM   6957  C  C     . THR A 1 2326 ? 77.590  79.735  114.825 1.00 6.90   ? 2326 THR A C     1 
ATOM   6958  O  O     . THR A 1 2326 ? 78.371  80.570  114.359 1.00 8.52   ? 2326 THR A O     1 
ATOM   6959  C  CB    . THR A 1 2326 ? 75.397  80.914  115.071 1.00 5.96   ? 2326 THR A CB    1 
ATOM   6960  O  OG1   . THR A 1 2326 ? 75.956  82.063  114.426 1.00 7.12   ? 2326 THR A OG1   1 
ATOM   6961  C  CG2   . THR A 1 2326 ? 74.336  81.369  116.055 1.00 3.28   ? 2326 THR A CG2   1 
ATOM   6962  N  N     . LEU A 1 2327 ? 77.636  78.450  114.524 1.00 6.28   ? 2327 LEU A N     1 
ATOM   6963  C  CA    . LEU A 1 2327 ? 78.641  77.894  113.641 1.00 8.53   ? 2327 LEU A CA    1 
ATOM   6964  C  C     . LEU A 1 2327 ? 78.007  77.463  112.323 1.00 9.87   ? 2327 LEU A C     1 
ATOM   6965  O  O     . LEU A 1 2327 ? 76.829  77.095  112.288 1.00 10.02  ? 2327 LEU A O     1 
ATOM   6966  C  CB    . LEU A 1 2327 ? 79.331  76.695  114.301 1.00 9.98   ? 2327 LEU A CB    1 
ATOM   6967  C  CG    . LEU A 1 2327 ? 80.158  77.009  115.550 1.00 6.99   ? 2327 LEU A CG    1 
ATOM   6968  C  CD1   . LEU A 1 2327 ? 80.841  75.758  116.077 1.00 7.11   ? 2327 LEU A CD1   1 
ATOM   6969  C  CD2   . LEU A 1 2327 ? 81.178  78.098  115.260 1.00 5.02   ? 2327 LEU A CD2   1 
ATOM   6970  N  N     . PRO A 1 2328 ? 78.757  77.503  111.218 1.00 9.71   ? 2328 PRO A N     1 
ATOM   6971  C  CA    . PRO A 1 2328 ? 78.168  77.133  109.920 1.00 7.98   ? 2328 PRO A CA    1 
ATOM   6972  C  C     . PRO A 1 2328 ? 77.694  75.689  109.830 1.00 9.98   ? 2328 PRO A C     1 
ATOM   6973  O  O     . PRO A 1 2328 ? 77.005  75.348  108.862 1.00 11.54  ? 2328 PRO A O     1 
ATOM   6974  C  CB    . PRO A 1 2328 ? 79.305  77.419  108.926 1.00 7.88   ? 2328 PRO A CB    1 
ATOM   6975  C  CG    . PRO A 1 2328 ? 80.551  77.458  109.764 1.00 8.00   ? 2328 PRO A CG    1 
ATOM   6976  C  CD    . PRO A 1 2328 ? 80.108  78.064  111.058 1.00 9.06   ? 2328 PRO A CD    1 
ATOM   6977  N  N     . ASN A 1 2329 ? 78.021  74.832  110.796 1.00 9.66   ? 2329 ASN A N     1 
ATOM   6978  C  CA    . ASN A 1 2329 ? 77.496  73.471  110.795 1.00 8.68   ? 2329 ASN A CA    1 
ATOM   6979  C  C     . ASN A 1 2329 ? 76.148  73.356  111.499 1.00 9.01   ? 2329 ASN A C     1 
ATOM   6980  O  O     . ASN A 1 2329 ? 75.703  72.237  111.774 1.00 12.48  ? 2329 ASN A O     1 
ATOM   6981  C  CB    . ASN A 1 2329 ? 78.500  72.502  111.432 1.00 9.54   ? 2329 ASN A CB    1 
ATOM   6982  C  CG    . ASN A 1 2329 ? 78.750  72.792  112.904 1.00 12.63  ? 2329 ASN A CG    1 
ATOM   6983  O  OD1   . ASN A 1 2329 ? 78.256  73.775  113.452 1.00 13.68  ? 2329 ASN A OD1   1 
ATOM   6984  N  ND2   . ASN A 1 2329 ? 79.524  71.928  113.549 1.00 11.59  ? 2329 ASN A ND2   1 
ATOM   6985  N  N     . GLY A 1 2330 ? 75.494  74.477  111.794 1.00 10.16  ? 2330 GLY A N     1 
ATOM   6986  C  CA    . GLY A 1 2330 ? 74.222  74.470  112.482 1.00 10.28  ? 2330 GLY A CA    1 
ATOM   6987  C  C     . GLY A 1 2330 ? 74.308  74.387  113.990 1.00 13.33  ? 2330 GLY A C     1 
ATOM   6988  O  O     . GLY A 1 2330 ? 73.265  74.422  114.655 1.00 15.27  ? 2330 GLY A O     1 
ATOM   6989  N  N     . GLU A 1 2331 ? 75.509  74.280  114.549 1.00 12.99  ? 2331 GLU A N     1 
ATOM   6990  C  CA    . GLU A 1 2331 ? 75.674  74.190  115.992 1.00 10.23  ? 2331 GLU A CA    1 
ATOM   6991  C  C     . GLU A 1 2331 ? 75.652  75.576  116.622 1.00 9.87   ? 2331 GLU A C     1 
ATOM   6992  O  O     . GLU A 1 2331 ? 76.223  76.529  116.085 1.00 10.46  ? 2331 GLU A O     1 
ATOM   6993  C  CB    . GLU A 1 2331 ? 76.987  73.485  116.334 1.00 11.87  ? 2331 GLU A CB    1 
ATOM   6994  C  CG    . GLU A 1 2331 ? 76.921  72.588  117.553 1.00 15.34  ? 2331 GLU A CG    1 
ATOM   6995  C  CD    . GLU A 1 2331 ? 78.293  72.131  118.010 1.00 23.21  ? 2331 GLU A CD    1 
ATOM   6996  O  OE1   . GLU A 1 2331 ? 79.135  71.814  117.143 1.00 20.63  ? 2331 GLU A OE1   1 
ATOM   6997  O  OE2   . GLU A 1 2331 ? 78.530  72.088  119.235 1.00 25.50  ? 2331 GLU A OE2   1 
ATOM   6998  N  N     . ARG A 1 2332 ? 74.987  75.684  117.769 1.00 12.34  ? 2332 ARG A N     1 
ATOM   6999  C  CA    . ARG A 1 2332 ? 74.970  76.913  118.551 1.00 10.01  ? 2332 ARG A CA    1 
ATOM   7000  C  C     . ARG A 1 2332 ? 75.472  76.602  119.951 1.00 8.22   ? 2332 ARG A C     1 
ATOM   7001  O  O     . ARG A 1 2332 ? 75.006  75.649  120.583 1.00 9.45   ? 2332 ARG A O     1 
ATOM   7002  C  CB    . ARG A 1 2332 ? 73.570  77.529  118.612 1.00 10.53  ? 2332 ARG A CB    1 
ATOM   7003  C  CG    . ARG A 1 2332 ? 73.045  78.036  117.284 1.00 17.42  ? 2332 ARG A CG    1 
ATOM   7004  C  CD    . ARG A 1 2332 ? 71.650  78.607  117.449 1.00 17.71  ? 2332 ARG A CD    1 
ATOM   7005  N  NE    . ARG A 1 2332 ? 70.668  77.583  117.781 1.00 22.21  ? 2332 ARG A NE    1 
ATOM   7006  C  CZ    . ARG A 1 2332 ? 69.409  77.835  118.110 1.00 26.80  ? 2332 ARG A CZ    1 
ATOM   7007  N  NH1   . ARG A 1 2332 ? 68.938  79.071  118.145 1.00 20.98  ? 2332 ARG A NH1   1 
ATOM   7008  N  NH2   . ARG A 1 2332 ? 68.603  76.823  118.418 1.00 28.82  ? 2332 ARG A NH2   1 
ATOM   7009  N  N     . LEU A 1 2333 ? 76.415  77.405  120.430 1.00 6.57   ? 2333 LEU A N     1 
ATOM   7010  C  CA    . LEU A 1 2333 ? 76.987  77.254  121.761 1.00 4.90   ? 2333 LEU A CA    1 
ATOM   7011  C  C     . LEU A 1 2333 ? 76.502  78.405  122.631 1.00 4.32   ? 2333 LEU A C     1 
ATOM   7012  O  O     . LEU A 1 2333 ? 76.735  79.573  122.304 1.00 6.94   ? 2333 LEU A O     1 
ATOM   7013  C  CB    . LEU A 1 2333 ? 78.515  77.221  121.706 1.00 5.18   ? 2333 LEU A CB    1 
ATOM   7014  C  CG    . LEU A 1 2333 ? 79.187  75.964  121.141 1.00 6.56   ? 2333 LEU A CG    1 
ATOM   7015  C  CD1   . LEU A 1 2333 ? 79.156  75.941  119.618 1.00 8.86   ? 2333 LEU A CD1   1 
ATOM   7016  C  CD2   . LEU A 1 2333 ? 80.617  75.847  121.649 1.00 4.98   ? 2333 LEU A CD2   1 
ATOM   7017  N  N     . SER A 1 2334 ? 75.824  78.075  123.726 1.00 4.22   ? 2334 SER A N     1 
ATOM   7018  C  CA    . SER A 1 2334 ? 75.304  79.088  124.632 1.00 4.08   ? 2334 SER A CA    1 
ATOM   7019  C  C     . SER A 1 2334 ? 76.403  79.595  125.554 1.00 4.84   ? 2334 SER A C     1 
ATOM   7020  O  O     . SER A 1 2334 ? 77.220  78.819  126.057 1.00 5.60   ? 2334 SER A O     1 
ATOM   7021  C  CB    . SER A 1 2334 ? 74.148  78.525  125.459 1.00 5.24   ? 2334 SER A CB    1 
ATOM   7022  O  OG    . SER A 1 2334 ? 73.109  78.045  124.626 1.00 11.36  ? 2334 SER A OG    1 
ATOM   7023  N  N     . LEU A 1 2335 ? 76.420  80.903  125.774 1.00 5.51   ? 2335 LEU A N     1 
ATOM   7024  C  CA    . LEU A 1 2335 ? 77.402  81.495  126.672 1.00 3.55   ? 2335 LEU A CA    1 
ATOM   7025  C  C     . LEU A 1 2335 ? 76.974  81.268  128.116 1.00 5.05   ? 2335 LEU A C     1 
ATOM   7026  O  O     . LEU A 1 2335 ? 75.895  81.726  128.510 1.00 5.11   ? 2335 LEU A O     1 
ATOM   7027  C  CB    . LEU A 1 2335 ? 77.556  82.984  126.394 1.00 4.32   ? 2335 LEU A CB    1 
ATOM   7028  C  CG    . LEU A 1 2335 ? 78.882  83.610  126.832 1.00 5.24   ? 2335 LEU A CG    1 
ATOM   7029  C  CD1   . LEU A 1 2335 ? 80.041  83.023  126.041 1.00 3.12   ? 2335 LEU A CD1   1 
ATOM   7030  C  CD2   . LEU A 1 2335 ? 78.839  85.122  126.684 1.00 4.02   ? 2335 LEU A CD2   1 
ATOM   7031  N  N     . PRO A 1 2336 ? 77.771  80.571  128.928 1.00 4.74   ? 2336 PRO A N     1 
ATOM   7032  C  CA    . PRO A 1 2336 ? 77.381  80.355  130.318 1.00 3.55   ? 2336 PRO A CA    1 
ATOM   7033  C  C     . PRO A 1 2336 ? 77.453  81.650  131.106 1.00 3.45   ? 2336 PRO A C     1 
ATOM   7034  O  O     . PRO A 1 2336 ? 78.223  82.562  130.759 1.00 3.92   ? 2336 PRO A O     1 
ATOM   7035  C  CB    . PRO A 1 2336 ? 78.414  79.329  130.822 1.00 2.93   ? 2336 PRO A CB    1 
ATOM   7036  C  CG    . PRO A 1 2336 ? 79.109  78.814  129.595 1.00 3.20   ? 2336 PRO A CG    1 
ATOM   7037  C  CD    . PRO A 1 2336 ? 79.045  79.916  128.598 1.00 4.68   ? 2336 PRO A CD    1 
ATOM   7038  N  N     . PRO A 1 2337 ? 76.664  81.779  132.175 1.00 4.06   ? 2337 PRO A N     1 
ATOM   7039  C  CA    . PRO A 1 2337 ? 76.661  83.037  132.942 1.00 3.84   ? 2337 PRO A CA    1 
ATOM   7040  C  C     . PRO A 1 2337 ? 77.988  83.365  133.605 1.00 3.84   ? 2337 PRO A C     1 
ATOM   7041  O  O     . PRO A 1 2337 ? 78.218  84.532  133.944 1.00 5.39   ? 2337 PRO A O     1 
ATOM   7042  C  CB    . PRO A 1 2337 ? 75.557  82.807  133.983 1.00 4.08   ? 2337 PRO A CB    1 
ATOM   7043  C  CG    . PRO A 1 2337 ? 75.463  81.317  134.102 1.00 3.99   ? 2337 PRO A CG    1 
ATOM   7044  C  CD    . PRO A 1 2337 ? 75.693  80.811  132.711 1.00 3.37   ? 2337 PRO A CD    1 
ATOM   7045  N  N     . ASN A 1 2338 ? 78.865  82.384  133.805 1.00 3.33   ? 2338 ASN A N     1 
ATOM   7046  C  CA    . ASN A 1 2338 ? 80.151  82.625  134.448 1.00 2.65   ? 2338 ASN A CA    1 
ATOM   7047  C  C     . ASN A 1 2338 ? 81.228  83.084  133.473 1.00 2.82   ? 2338 ASN A C     1 
ATOM   7048  O  O     . ASN A 1 2338 ? 82.364  83.319  133.898 1.00 3.69   ? 2338 ASN A O     1 
ATOM   7049  C  CB    . ASN A 1 2338 ? 80.624  81.362  135.174 1.00 3.25   ? 2338 ASN A CB    1 
ATOM   7050  C  CG    . ASN A 1 2338 ? 81.032  80.257  134.218 1.00 3.83   ? 2338 ASN A CG    1 
ATOM   7051  O  OD1   . ASN A 1 2338 ? 80.269  79.875  133.333 1.00 4.67   ? 2338 ASN A OD1   1 
ATOM   7052  N  ND2   . ASN A 1 2338 ? 82.240  79.738  134.394 1.00 3.62   ? 2338 ASN A ND2   1 
ATOM   7053  N  N     . VAL A 1 2339 ? 80.905  83.221  132.191 1.00 2.06   ? 2339 VAL A N     1 
ATOM   7054  C  CA    . VAL A 1 2339 ? 81.882  83.550  131.161 1.00 2.00   ? 2339 VAL A CA    1 
ATOM   7055  C  C     . VAL A 1 2339 ? 81.736  85.017  130.786 1.00 2.04   ? 2339 VAL A C     1 
ATOM   7056  O  O     . VAL A 1 2339 ? 80.626  85.494  130.519 1.00 2.49   ? 2339 VAL A O     1 
ATOM   7057  C  CB    . VAL A 1 2339 ? 81.711  82.649  129.926 1.00 1.76   ? 2339 VAL A CB    1 
ATOM   7058  C  CG1   . VAL A 1 2339 ? 82.610  83.119  128.793 1.00 1.46   ? 2339 VAL A CG1   1 
ATOM   7059  C  CG2   . VAL A 1 2339 ? 82.009  81.205  130.285 1.00 1.87   ? 2339 VAL A CG2   1 
ATOM   7060  N  N     . ARG A 1 2340 ? 82.857  85.734  130.772 1.00 1.38   ? 2340 ARG A N     1 
ATOM   7061  C  CA    . ARG A 1 2340 ? 82.921  87.104  130.284 1.00 1.81   ? 2340 ARG A CA    1 
ATOM   7062  C  C     . ARG A 1 2340 ? 83.796  87.141  129.041 1.00 1.56   ? 2340 ARG A C     1 
ATOM   7063  O  O     . ARG A 1 2340 ? 84.898  86.582  129.038 1.00 1.58   ? 2340 ARG A O     1 
ATOM   7064  C  CB    . ARG A 1 2340 ? 83.484  88.053  131.347 1.00 1.91   ? 2340 ARG A CB    1 
ATOM   7065  C  CG    . ARG A 1 2340 ? 82.606  88.238  132.570 1.00 1.88   ? 2340 ARG A CG    1 
ATOM   7066  C  CD    . ARG A 1 2340 ? 81.250  88.815  132.200 1.00 2.68   ? 2340 ARG A CD    1 
ATOM   7067  N  NE    . ARG A 1 2340 ? 80.371  88.937  133.357 1.00 6.08   ? 2340 ARG A NE    1 
ATOM   7068  C  CZ    . ARG A 1 2340 ? 79.795  87.916  133.978 1.00 5.68   ? 2340 ARG A CZ    1 
ATOM   7069  N  NH1   . ARG A 1 2340 ? 79.962  86.671  133.565 1.00 2.88   ? 2340 ARG A NH1   1 
ATOM   7070  N  NH2   . ARG A 1 2340 ? 79.028  88.152  135.038 1.00 6.13   ? 2340 ARG A NH2   1 
ATOM   7071  N  N     . ILE A 1 2341 ? 83.307  87.792  127.991 1.00 1.80   ? 2341 ILE A N     1 
ATOM   7072  C  CA    . ILE A 1 2341 ? 84.082  88.018  126.778 1.00 1.80   ? 2341 ILE A CA    1 
ATOM   7073  C  C     . ILE A 1 2341 ? 84.687  89.411  126.866 1.00 2.08   ? 2341 ILE A C     1 
ATOM   7074  O  O     . ILE A 1 2341 ? 83.961  90.409  126.948 1.00 2.95   ? 2341 ILE A O     1 
ATOM   7075  C  CB    . ILE A 1 2341 ? 83.219  87.865  125.516 1.00 1.57   ? 2341 ILE A CB    1 
ATOM   7076  C  CG1   . ILE A 1 2341 ? 82.503  86.512  125.513 1.00 1.48   ? 2341 ILE A CG1   1 
ATOM   7077  C  CG2   . ILE A 1 2341 ? 84.072  88.022  124.266 1.00 1.49   ? 2341 ILE A CG2   1 
ATOM   7078  C  CD1   . ILE A 1 2341 ? 83.432  85.324  125.598 1.00 1.51   ? 2341 ILE A CD1   1 
ATOM   7079  N  N     . MET A 1 2342 ? 86.015  89.481  126.846 1.00 2.32   ? 2342 MET A N     1 
ATOM   7080  C  CA    . MET A 1 2342 ? 86.737  90.733  126.991 1.00 2.57   ? 2342 MET A CA    1 
ATOM   7081  C  C     . MET A 1 2342 ? 87.633  90.968  125.785 1.00 2.08   ? 2342 MET A C     1 
ATOM   7082  O  O     . MET A 1 2342 ? 88.139  90.026  125.169 1.00 3.64   ? 2342 MET A O     1 
ATOM   7083  C  CB    . MET A 1 2342 ? 87.580  90.747  128.272 1.00 2.52   ? 2342 MET A CB    1 
ATOM   7084  C  CG    . MET A 1 2342 ? 86.758  90.703  129.543 1.00 2.36   ? 2342 MET A CG    1 
ATOM   7085  S  SD    . MET A 1 2342 ? 87.745  90.649  131.047 1.00 16.65  ? 2342 MET A SD    1 
ATOM   7086  C  CE    . MET A 1 2342 ? 86.453  90.756  132.279 1.00 4.63   ? 2342 MET A CE    1 
ATOM   7087  N  N     . PHE A 1 2343 ? 87.814  92.242  125.448 1.00 2.08   ? 2343 PHE A N     1 
ATOM   7088  C  CA    . PHE A 1 2343 ? 88.680  92.659  124.349 1.00 2.71   ? 2343 PHE A CA    1 
ATOM   7089  C  C     . PHE A 1 2343 ? 89.662  93.675  124.922 1.00 3.29   ? 2343 PHE A C     1 
ATOM   7090  O  O     . PHE A 1 2343 ? 89.249  94.682  125.503 1.00 3.30   ? 2343 PHE A O     1 
ATOM   7091  C  CB    . PHE A 1 2343 ? 87.874  93.261  123.204 1.00 1.84   ? 2343 PHE A CB    1 
ATOM   7092  C  CG    . PHE A 1 2343 ? 86.820  92.347  122.649 1.00 2.74   ? 2343 PHE A CG    1 
ATOM   7093  C  CD1   . PHE A 1 2343 ? 85.552  92.318  123.206 1.00 3.98   ? 2343 PHE A CD1   1 
ATOM   7094  C  CD2   . PHE A 1 2343 ? 87.081  91.544  121.553 1.00 1.82   ? 2343 PHE A CD2   1 
ATOM   7095  C  CE1   . PHE A 1 2343 ? 84.573  91.492  122.696 1.00 2.38   ? 2343 PHE A CE1   1 
ATOM   7096  C  CE2   . PHE A 1 2343 ? 86.102  90.715  121.040 1.00 2.31   ? 2343 PHE A CE2   1 
ATOM   7097  C  CZ    . PHE A 1 2343 ? 84.847  90.690  121.612 1.00 2.08   ? 2343 PHE A CZ    1 
ATOM   7098  N  N     . GLU A 1 2344 ? 90.955  93.412  124.769 1.00 3.86   ? 2344 GLU A N     1 
ATOM   7099  C  CA    . GLU A 1 2344 ? 91.986  94.348  125.197 1.00 3.44   ? 2344 GLU A CA    1 
ATOM   7100  C  C     . GLU A 1 2344 ? 92.598  94.985  123.956 1.00 3.24   ? 2344 GLU A C     1 
ATOM   7101  O  O     . GLU A 1 2344 ? 93.389  94.351  123.249 1.00 4.86   ? 2344 GLU A O     1 
ATOM   7102  C  CB    . GLU A 1 2344 ? 93.040  93.645  126.046 1.00 6.20   ? 2344 GLU A CB    1 
ATOM   7103  C  CG    . GLU A 1 2344 ? 94.146  94.563  126.522 1.00 5.58   ? 2344 GLU A CG    1 
ATOM   7104  C  CD    . GLU A 1 2344 ? 95.158  93.857  127.390 1.00 4.58   ? 2344 GLU A CD    1 
ATOM   7105  O  OE1   . GLU A 1 2344 ? 94.760  93.292  128.430 1.00 2.81   ? 2344 GLU A OE1   1 
ATOM   7106  O  OE2   . GLU A 1 2344 ? 96.357  93.878  127.047 1.00 9.56   ? 2344 GLU A OE2   1 
ATOM   7107  N  N     . VAL A 1 2345 ? 92.231  96.240  123.689 1.00 3.07   ? 2345 VAL A N     1 
ATOM   7108  C  CA    . VAL A 1 2345 ? 92.608  96.920  122.457 1.00 4.21   ? 2345 VAL A CA    1 
ATOM   7109  C  C     . VAL A 1 2345 ? 93.225  98.270  122.792 1.00 3.80   ? 2345 VAL A C     1 
ATOM   7110  O  O     . VAL A 1 2345 ? 93.002  98.837  123.864 1.00 3.47   ? 2345 VAL A O     1 
ATOM   7111  C  CB    . VAL A 1 2345 ? 91.405  97.117  121.507 1.00 3.88   ? 2345 VAL A CB    1 
ATOM   7112  C  CG1   . VAL A 1 2345 ? 90.745  95.788  121.203 1.00 2.94   ? 2345 VAL A CG1   1 
ATOM   7113  C  CG2   . VAL A 1 2345 ? 90.405  98.095  122.103 1.00 3.00   ? 2345 VAL A CG2   1 
ATOM   7114  N  N     . GLN A 1 2346 ? 94.016  98.781  121.850 1.00 5.95   ? 2346 GLN A N     1 
ATOM   7115  C  CA    . GLN A 1 2346 ? 94.559  100.127 121.961 1.00 6.51   ? 2346 GLN A CA    1 
ATOM   7116  C  C     . GLN A 1 2346 ? 93.727  101.160 121.217 1.00 6.48   ? 2346 GLN A C     1 
ATOM   7117  O  O     . GLN A 1 2346 ? 93.833  102.354 121.517 1.00 7.00   ? 2346 GLN A O     1 
ATOM   7118  C  CB    . GLN A 1 2346 ? 96.002  100.167 121.448 1.00 5.06   ? 2346 GLN A CB    1 
ATOM   7119  C  CG    . GLN A 1 2346 ? 96.193  99.567  120.068 1.00 8.56   ? 2346 GLN A CG    1 
ATOM   7120  C  CD    . GLN A 1 2346 ? 97.568  99.854  119.498 1.00 13.93  ? 2346 GLN A CD    1 
ATOM   7121  O  OE1   . GLN A 1 2346 ? 98.312  100.681 120.026 1.00 11.59  ? 2346 GLN A OE1   1 
ATOM   7122  N  NE2   . GLN A 1 2346 ? 97.916  99.165  118.417 1.00 11.81  ? 2346 GLN A NE2   1 
ATOM   7123  N  N     . ASP A 1 2347 ? 92.906  100.729 120.263 1.00 6.64   ? 2347 ASP A N     1 
ATOM   7124  C  CA    . ASP A 1 2347 ? 92.062  101.633 119.496 1.00 7.00   ? 2347 ASP A CA    1 
ATOM   7125  C  C     . ASP A 1 2347 ? 90.916  100.830 118.898 1.00 7.87   ? 2347 ASP A C     1 
ATOM   7126  O  O     . ASP A 1 2347 ? 90.941  99.597  118.872 1.00 7.93   ? 2347 ASP A O     1 
ATOM   7127  C  CB    . ASP A 1 2347 ? 92.864  102.356 118.407 1.00 7.38   ? 2347 ASP A CB    1 
ATOM   7128  C  CG    . ASP A 1 2347 ? 93.491  101.400 117.407 1.00 11.77  ? 2347 ASP A CG    1 
ATOM   7129  O  OD1   . ASP A 1 2347 ? 92.758  100.847 116.560 1.00 13.68  ? 2347 ASP A OD1   1 
ATOM   7130  O  OD2   . ASP A 1 2347 ? 94.722  101.199 117.470 1.00 11.02  ? 2347 ASP A OD2   1 
ATOM   7131  N  N     . LEU A 1 2348 ? 89.901  101.551 118.419 1.00 8.91   ? 2348 LEU A N     1 
ATOM   7132  C  CA    . LEU A 1 2348 ? 88.760  100.932 117.756 1.00 9.52   ? 2348 LEU A CA    1 
ATOM   7133  C  C     . LEU A 1 2348 ? 88.422  101.649 116.456 1.00 11.51  ? 2348 LEU A C     1 
ATOM   7134  O  O     . LEU A 1 2348 ? 87.245  101.799 116.113 1.00 13.88  ? 2348 LEU A O     1 
ATOM   7135  C  CB    . LEU A 1 2348 ? 87.535  100.905 118.672 1.00 8.38   ? 2348 LEU A CB    1 
ATOM   7136  C  CG    . LEU A 1 2348 ? 87.529  99.837  119.766 1.00 8.58   ? 2348 LEU A CG    1 
ATOM   7137  C  CD1   . LEU A 1 2348 ? 86.255  99.925  120.587 1.00 9.92   ? 2348 LEU A CD1   1 
ATOM   7138  C  CD2   . LEU A 1 2348 ? 87.692  98.449  119.166 1.00 8.26   ? 2348 LEU A CD2   1 
ATOM   7139  N  N     . LYS A 1 2349 ? 89.442  102.094 115.719 1.00 12.58  ? 2349 LYS A N     1 
ATOM   7140  C  CA    . LYS A 1 2349 ? 89.220  102.867 114.504 1.00 14.06  ? 2349 LYS A CA    1 
ATOM   7141  C  C     . LYS A 1 2349 ? 88.717  102.023 113.341 1.00 14.03  ? 2349 LYS A C     1 
ATOM   7142  O  O     . LYS A 1 2349 ? 88.322  102.589 112.317 1.00 22.13  ? 2349 LYS A O     1 
ATOM   7143  C  CB    . LYS A 1 2349 ? 90.508  103.591 114.107 1.00 13.76  ? 2349 LYS A CB    1 
ATOM   7144  C  CG    . LYS A 1 2349 ? 91.720  102.687 113.986 1.00 15.81  ? 2349 LYS A CG    1 
ATOM   7145  C  CD    . LYS A 1 2349 ? 92.863  103.390 113.272 1.00 22.42  ? 2349 LYS A CD    1 
ATOM   7146  C  CE    . LYS A 1 2349 ? 92.441  103.881 111.897 1.00 28.08  ? 2349 LYS A CE    1 
ATOM   7147  N  NZ    . LYS A 1 2349 ? 93.603  104.368 111.103 1.00 31.95  ? 2349 LYS A NZ    1 
ATOM   7148  N  N     . TYR A 1 2350 ? 88.717  100.696 113.467 1.00 9.45   ? 2350 TYR A N     1 
ATOM   7149  C  CA    . TYR A 1 2350 ? 88.173  99.824  112.437 1.00 9.25   ? 2350 TYR A CA    1 
ATOM   7150  C  C     . TYR A 1 2350 ? 86.935  99.059  112.883 1.00 11.58  ? 2350 TYR A C     1 
ATOM   7151  O  O     . TYR A 1 2350 ? 86.298  98.409  112.048 1.00 14.12  ? 2350 TYR A O     1 
ATOM   7152  C  CB    . TYR A 1 2350 ? 89.241  98.830  111.957 1.00 9.50   ? 2350 TYR A CB    1 
ATOM   7153  C  CG    . TYR A 1 2350 ? 90.459  99.494  111.357 1.00 12.89  ? 2350 TYR A CG    1 
ATOM   7154  C  CD1   . TYR A 1 2350 ? 90.437  99.981  110.057 1.00 11.48  ? 2350 TYR A CD1   1 
ATOM   7155  C  CD2   . TYR A 1 2350 ? 91.629  99.638  112.091 1.00 12.21  ? 2350 TYR A CD2   1 
ATOM   7156  C  CE1   . TYR A 1 2350 ? 91.545  100.591 109.504 1.00 13.16  ? 2350 TYR A CE1   1 
ATOM   7157  C  CE2   . TYR A 1 2350 ? 92.743  100.247 111.545 1.00 13.47  ? 2350 TYR A CE2   1 
ATOM   7158  C  CZ    . TYR A 1 2350 ? 92.695  100.721 110.251 1.00 14.54  ? 2350 TYR A CZ    1 
ATOM   7159  O  OH    . TYR A 1 2350 ? 93.801  101.328 109.703 1.00 21.27  ? 2350 TYR A OH    1 
ATOM   7160  N  N     . ALA A 1 2351 ? 86.579  99.117  114.163 1.00 12.74  ? 2351 ALA A N     1 
ATOM   7161  C  CA    . ALA A 1 2351 ? 85.356  98.482  114.631 1.00 13.18  ? 2351 ALA A CA    1 
ATOM   7162  C  C     . ALA A 1 2351 ? 84.135  99.275  114.179 1.00 12.89  ? 2351 ALA A C     1 
ATOM   7163  O  O     . ALA A 1 2351 ? 84.174  100.501 114.048 1.00 17.92  ? 2351 ALA A O     1 
ATOM   7164  C  CB    . ALA A 1 2351 ? 85.369  98.355  116.154 1.00 11.04  ? 2351 ALA A CB    1 
ATOM   7165  N  N     . THR A 1 2352 ? 83.038  98.559  113.939 1.00 11.33  ? 2352 THR A N     1 
ATOM   7166  C  CA    . THR A 1 2352 ? 81.812  99.174  113.458 1.00 15.34  ? 2352 THR A CA    1 
ATOM   7167  C  C     . THR A 1 2352 ? 80.870  99.472  114.625 1.00 16.15  ? 2352 THR A C     1 
ATOM   7168  O  O     . THR A 1 2352 ? 81.187  99.239  115.793 1.00 12.93  ? 2352 THR A O     1 
ATOM   7169  C  CB    . THR A 1 2352 ? 81.137  98.277  112.422 1.00 17.91  ? 2352 THR A CB    1 
ATOM   7170  O  OG1   . THR A 1 2352 ? 80.803  97.021  113.022 1.00 23.06  ? 2352 THR A OG1   1 
ATOM   7171  C  CG2   . THR A 1 2352 ? 82.067  98.037  111.242 1.00 15.45  ? 2352 THR A CG2   1 
ATOM   7172  N  N     . LEU A 1 2353 ? 79.685  99.994  114.299 1.00 19.79  ? 2353 LEU A N     1 
ATOM   7173  C  CA    . LEU A 1 2353 ? 78.758  100.439 115.336 1.00 13.82  ? 2353 LEU A CA    1 
ATOM   7174  C  C     . LEU A 1 2353 ? 78.163  99.262  116.099 1.00 13.43  ? 2353 LEU A C     1 
ATOM   7175  O  O     . LEU A 1 2353 ? 77.902  99.365  117.303 1.00 13.69  ? 2353 LEU A O     1 
ATOM   7176  C  CB    . LEU A 1 2353 ? 77.657  101.303 114.715 1.00 15.74  ? 2353 LEU A CB    1 
ATOM   7177  C  CG    . LEU A 1 2353 ? 76.661  102.034 115.626 1.00 19.57  ? 2353 LEU A CG    1 
ATOM   7178  C  CD1   . LEU A 1 2353 ? 76.135  103.273 114.925 1.00 30.27  ? 2353 LEU A CD1   1 
ATOM   7179  C  CD2   . LEU A 1 2353 ? 75.491  101.144 116.034 1.00 19.56  ? 2353 LEU A CD2   1 
ATOM   7180  N  N     . ALA A 1 2354 ? 77.926  98.140  115.416 1.00 11.30  ? 2354 ALA A N     1 
ATOM   7181  C  CA    . ALA A 1 2354 ? 77.302  96.989  116.061 1.00 14.81  ? 2354 ALA A CA    1 
ATOM   7182  C  C     . ALA A 1 2354 ? 78.165  96.452  117.197 1.00 14.41  ? 2354 ALA A C     1 
ATOM   7183  O  O     . ALA A 1 2354 ? 77.687  96.245  118.321 1.00 16.31  ? 2354 ALA A O     1 
ATOM   7184  C  CB    . ALA A 1 2354 ? 77.039  95.897  115.023 1.00 13.63  ? 2354 ALA A CB    1 
ATOM   7185  N  N     . THR A 1 2355 ? 79.448  96.227  116.914 1.00 13.70  ? 2355 THR A N     1 
ATOM   7186  C  CA    . THR A 1 2355 ? 80.358  95.699  117.923 1.00 10.73  ? 2355 THR A CA    1 
ATOM   7187  C  C     . THR A 1 2355 ? 80.522  96.677  119.081 1.00 9.16   ? 2355 THR A C     1 
ATOM   7188  O  O     . THR A 1 2355 ? 80.538  96.274  120.250 1.00 10.48  ? 2355 THR A O     1 
ATOM   7189  C  CB    . THR A 1 2355 ? 81.707  95.380  117.282 1.00 9.26   ? 2355 THR A CB    1 
ATOM   7190  O  OG1   . THR A 1 2355 ? 81.514  94.455  116.205 1.00 12.06  ? 2355 THR A OG1   1 
ATOM   7191  C  CG2   . THR A 1 2355 ? 82.638  94.761  118.298 1.00 6.55   ? 2355 THR A CG2   1 
ATOM   7192  N  N     . VAL A 1 2356 ? 80.642  97.971  118.773 1.00 9.36   ? 2356 VAL A N     1 
ATOM   7193  C  CA    . VAL A 1 2356 ? 80.784  98.979  119.821 1.00 10.29  ? 2356 VAL A CA    1 
ATOM   7194  C  C     . VAL A 1 2356 ? 79.550  99.001  120.713 1.00 13.59  ? 2356 VAL A C     1 
ATOM   7195  O  O     . VAL A 1 2356 ? 79.655  99.065  121.944 1.00 16.12  ? 2356 VAL A O     1 
ATOM   7196  C  CB    . VAL A 1 2356 ? 81.060  100.361 119.199 1.00 12.30  ? 2356 VAL A CB    1 
ATOM   7197  C  CG1   . VAL A 1 2356 ? 80.970  101.452 120.256 1.00 11.26  ? 2356 VAL A CG1   1 
ATOM   7198  C  CG2   . VAL A 1 2356 ? 82.425  100.376 118.530 1.00 12.12  ? 2356 VAL A CG2   1 
ATOM   7199  N  N     . SER A 1 2357 ? 78.370  98.928  120.090 1.00 13.81  ? 2357 SER A N     1 
ATOM   7200  C  CA    . SER A 1 2357 ? 77.097  98.999  120.857 1.00 11.29  ? 2357 SER A CA    1 
ATOM   7201  C  C     . SER A 1 2357 ? 76.819  97.675  121.585 1.00 11.95  ? 2357 SER A C     1 
ATOM   7202  O  O     . SER A 1 2357 ? 75.958  97.677  122.491 1.00 13.66  ? 2357 SER A O     1 
ATOM   7203  C  CB    . SER A 1 2357 ? 75.951  99.360  119.948 1.00 9.86   ? 2357 SER A CB    1 
ATOM   7204  O  OG    . SER A 1 2357 ? 75.804  98.396  118.914 1.00 14.29  ? 2357 SER A OG    1 
ATOM   7205  N  N     . ARG A 1 2358 ? 77.514  96.596  121.214 1.00 10.36  ? 2358 ARG A N     1 
ATOM   7206  C  CA    . ARG A 1 2358 ? 77.221  95.267  121.814 1.00 10.50  ? 2358 ARG A CA    1 
ATOM   7207  C  C     . ARG A 1 2358 ? 78.161  94.974  122.993 1.00 11.68  ? 2358 ARG A C     1 
ATOM   7208  O  O     . ARG A 1 2358 ? 78.210  93.797  123.415 1.00 13.69  ? 2358 ARG A O     1 
ATOM   7209  C  CB    . ARG A 1 2358 ? 77.378  94.146  120.779 1.00 8.41   ? 2358 ARG A CB    1 
ATOM   7210  C  CG    . ARG A 1 2358 ? 76.170  93.855  119.901 1.00 8.10   ? 2358 ARG A CG    1 
ATOM   7211  C  CD    . ARG A 1 2358 ? 76.421  92.598  119.081 1.00 8.55   ? 2358 ARG A CD    1 
ATOM   7212  N  NE    . ARG A 1 2358 ? 75.275  92.164  118.273 1.00 11.52  ? 2358 ARG A NE    1 
ATOM   7213  C  CZ    . ARG A 1 2358 ? 74.729  92.856  117.282 1.00 9.38   ? 2358 ARG A CZ    1 
ATOM   7214  N  NH1   . ARG A 1 2358 ? 75.202  94.047  116.963 1.00 9.12   ? 2358 ARG A NH1   1 
ATOM   7215  N  NH2   . ARG A 1 2358 ? 73.711  92.351  116.609 1.00 8.43   ? 2358 ARG A NH2   1 
ATOM   7216  N  N     . CYS A 1 2359 ? 78.878  95.979  123.508 1.00 8.86   ? 2359 CYS A N     1 
ATOM   7217  C  CA    . CYS A 1 2359 ? 79.868  95.682  124.577 1.00 8.56   ? 2359 CYS A CA    1 
ATOM   7218  C  C     . CYS A 1 2359 ? 80.092  96.872  125.519 1.00 9.16   ? 2359 CYS A C     1 
ATOM   7219  O  O     . CYS A 1 2359 ? 80.342  97.987  125.009 1.00 13.38  ? 2359 CYS A O     1 
ATOM   7220  C  CB    . CYS A 1 2359 ? 81.224  95.322  123.980 1.00 7.18   ? 2359 CYS A CB    1 
ATOM   7221  S  SG    . CYS A 1 2359 ? 81.360  93.586  123.482 1.00 12.53  ? 2359 CYS A SG    1 
ATOM   7222  N  N     . GLY A 1 2360 ? 80.014  96.642  126.835 1.00 7.25   ? 2360 GLY A N     1 
ATOM   7223  C  CA    . GLY A 1 2360 ? 80.342  97.686  127.789 1.00 7.54   ? 2360 GLY A CA    1 
ATOM   7224  C  C     . GLY A 1 2360 ? 81.725  98.242  127.504 1.00 6.14   ? 2360 GLY A C     1 
ATOM   7225  O  O     . GLY A 1 2360 ? 82.553  97.592  126.866 1.00 5.85   ? 2360 GLY A O     1 
ATOM   7226  N  N     . MET A 1 2361 ? 81.972  99.465  127.957 1.00 7.02   ? 2361 MET A N     1 
ATOM   7227  C  CA    . MET A 1 2361 ? 83.207  100.165 127.632 1.00 5.27   ? 2361 MET A CA    1 
ATOM   7228  C  C     . MET A 1 2361 ? 83.869  100.695 128.893 1.00 4.87   ? 2361 MET A C     1 
ATOM   7229  O  O     . MET A 1 2361 ? 83.207  101.304 129.740 1.00 7.19   ? 2361 MET A O     1 
ATOM   7230  C  CB    . MET A 1 2361 ? 82.944  101.313 126.658 1.00 6.13   ? 2361 MET A CB    1 
ATOM   7231  C  CG    . MET A 1 2361 ? 82.518  100.866 125.279 1.00 8.65   ? 2361 MET A CG    1 
ATOM   7232  S  SD    . MET A 1 2361 ? 83.833  99.973  124.433 1.00 20.08  ? 2361 MET A SD    1 
ATOM   7233  C  CE    . MET A 1 2361 ? 83.269  100.078 122.740 1.00 14.26  ? 2361 MET A CE    1 
ATOM   7234  N  N     . VAL A 1 2362 ? 85.171  100.449 129.019 1.00 4.02   ? 2362 VAL A N     1 
ATOM   7235  C  CA    . VAL A 1 2362 ? 86.014  101.124 129.998 1.00 4.75   ? 2362 VAL A CA    1 
ATOM   7236  C  C     . VAL A 1 2362 ? 87.157  101.779 129.237 1.00 4.08   ? 2362 VAL A C     1 
ATOM   7237  O  O     . VAL A 1 2362 ? 87.936  101.091 128.563 1.00 3.68   ? 2362 VAL A O     1 
ATOM   7238  C  CB    . VAL A 1 2362 ? 86.547  100.165 131.075 1.00 3.26   ? 2362 VAL A CB    1 
ATOM   7239  C  CG1   . VAL A 1 2362 ? 87.287  100.946 132.151 1.00 2.97   ? 2362 VAL A CG1   1 
ATOM   7240  C  CG2   . VAL A 1 2362 ? 85.414  99.366  131.689 1.00 3.72   ? 2362 VAL A CG2   1 
ATOM   7241  N  N     . TRP A 1 2363 ? 87.261  103.100 129.345 1.00 3.76   ? 2363 TRP A N     1 
ATOM   7242  C  CA    . TRP A 1 2363 ? 88.294  103.849 128.646 1.00 2.95   ? 2363 TRP A CA    1 
ATOM   7243  C  C     . TRP A 1 2363 ? 89.481  104.086 129.570 1.00 2.76   ? 2363 TRP A C     1 
ATOM   7244  O  O     . TRP A 1 2363 ? 89.316  104.556 130.699 1.00 4.09   ? 2363 TRP A O     1 
ATOM   7245  C  CB    . TRP A 1 2363 ? 87.749  105.182 128.133 1.00 3.78   ? 2363 TRP A CB    1 
ATOM   7246  C  CG    . TRP A 1 2363 ? 88.821  106.173 127.782 1.00 4.16   ? 2363 TRP A CG    1 
ATOM   7247  C  CD1   . TRP A 1 2363 ? 89.232  107.235 128.534 1.00 4.48   ? 2363 TRP A CD1   1 
ATOM   7248  C  CD2   . TRP A 1 2363 ? 89.626  106.186 126.596 1.00 3.87   ? 2363 TRP A CD2   1 
ATOM   7249  N  NE1   . TRP A 1 2363 ? 90.237  107.911 127.889 1.00 4.87   ? 2363 TRP A NE1   1 
ATOM   7250  C  CE2   . TRP A 1 2363 ? 90.499  107.288 126.698 1.00 5.30   ? 2363 TRP A CE2   1 
ATOM   7251  C  CE3   . TRP A 1 2363 ? 89.693  105.376 125.459 1.00 3.88   ? 2363 TRP A CE3   1 
ATOM   7252  C  CZ2   . TRP A 1 2363 ? 91.426  107.600 125.705 1.00 5.53   ? 2363 TRP A CZ2   1 
ATOM   7253  C  CZ3   . TRP A 1 2363 ? 90.613  105.688 124.475 1.00 3.76   ? 2363 TRP A CZ3   1 
ATOM   7254  C  CH2   . TRP A 1 2363 ? 91.468  106.790 124.605 1.00 4.41   ? 2363 TRP A CH2   1 
ATOM   7255  N  N     . PHE A 1 2364 ? 90.671  103.754 129.086 1.00 2.53   ? 2364 PHE A N     1 
ATOM   7256  C  CA    . PHE A 1 2364 ? 91.920  103.992 129.791 1.00 3.01   ? 2364 PHE A CA    1 
ATOM   7257  C  C     . PHE A 1 2364 ? 92.691  105.078 129.057 1.00 4.13   ? 2364 PHE A C     1 
ATOM   7258  O  O     . PHE A 1 2364 ? 92.976  104.941 127.864 1.00 5.45   ? 2364 PHE A O     1 
ATOM   7259  C  CB    . PHE A 1 2364 ? 92.770  102.722 129.870 1.00 2.50   ? 2364 PHE A CB    1 
ATOM   7260  C  CG    . PHE A 1 2364 ? 92.230  101.677 130.801 1.00 1.80   ? 2364 PHE A CG    1 
ATOM   7261  C  CD1   . PHE A 1 2364 ? 91.061  100.995 130.503 1.00 1.82   ? 2364 PHE A CD1   1 
ATOM   7262  C  CD2   . PHE A 1 2364 ? 92.899  101.369 131.973 1.00 1.50   ? 2364 PHE A CD2   1 
ATOM   7263  C  CE1   . PHE A 1 2364 ? 90.572  100.031 131.358 1.00 1.80   ? 2364 PHE A CE1   1 
ATOM   7264  C  CE2   . PHE A 1 2364 ? 92.412  100.406 132.831 1.00 1.26   ? 2364 PHE A CE2   1 
ATOM   7265  C  CZ    . PHE A 1 2364 ? 91.247  99.738  132.523 1.00 2.29   ? 2364 PHE A CZ    1 
ATOM   7266  N  N     . SER A 1 2365 ? 93.022  106.150 129.762 1.00 5.53   ? 2365 SER A N     1 
ATOM   7267  C  CA    . SER A 1 2365 ? 93.836  107.213 129.199 1.00 6.35   ? 2365 SER A CA    1 
ATOM   7268  C  C     . SER A 1 2365 ? 95.298  106.983 129.555 1.00 9.59   ? 2365 SER A C     1 
ATOM   7269  O  O     . SER A 1 2365 ? 95.628  106.211 130.459 1.00 8.09   ? 2365 SER A O     1 
ATOM   7270  C  CB    . SER A 1 2365 ? 93.378  108.587 129.700 1.00 6.81   ? 2365 SER A CB    1 
ATOM   7271  O  OG    . SER A 1 2365 ? 93.609  108.726 131.089 1.00 11.93  ? 2365 SER A OG    1 
ATOM   7272  N  N     . GLU A 1 2366 ? 96.179  107.660 128.816 1.00 13.36  ? 2366 GLU A N     1 
ATOM   7273  C  CA    . GLU A 1 2366 ? 97.597  107.641 129.150 1.00 15.00  ? 2366 GLU A CA    1 
ATOM   7274  C  C     . GLU A 1 2366 ? 97.853  108.202 130.543 1.00 15.49  ? 2366 GLU A C     1 
ATOM   7275  O  O     . GLU A 1 2366 ? 98.827  107.808 131.192 1.00 20.00  ? 2366 GLU A O     1 
ATOM   7276  C  CB    . GLU A 1 2366 ? 98.385  108.421 128.090 1.00 23.84  ? 2366 GLU A CB    1 
ATOM   7277  C  CG    . GLU A 1 2366 ? 99.903  108.299 128.172 1.00 23.77  ? 2366 GLU A CG    1 
ATOM   7278  C  CD    . GLU A 1 2366 ? 100.525 109.259 129.169 1.00 34.91  ? 2366 GLU A CD    1 
ATOM   7279  O  OE1   . GLU A 1 2366 ? 99.945  110.342 129.395 1.00 31.41  ? 2366 GLU A OE1   1 
ATOM   7280  O  OE2   . GLU A 1 2366 ? 101.595 108.933 129.722 1.00 34.56  ? 2366 GLU A OE2   1 
ATOM   7281  N  N     . ASP A 1 2367 ? 96.985  109.097 131.021 1.00 14.15  ? 2367 ASP A N     1 
ATOM   7282  C  CA    . ASP A 1 2367 ? 97.133  109.659 132.357 1.00 15.85  ? 2367 ASP A CA    1 
ATOM   7283  C  C     . ASP A 1 2367 ? 96.762  108.669 133.453 1.00 13.27  ? 2367 ASP A C     1 
ATOM   7284  O  O     . ASP A 1 2367 ? 97.127  108.886 134.614 1.00 16.13  ? 2367 ASP A O     1 
ATOM   7285  C  CB    . ASP A 1 2367 ? 96.278  110.920 132.488 1.00 20.88  ? 2367 ASP A CB    1 
ATOM   7286  C  CG    . ASP A 1 2367 ? 96.796  112.065 131.641 1.00 35.89  ? 2367 ASP A CG    1 
ATOM   7287  O  OD1   . ASP A 1 2367 ? 98.021  112.125 131.406 1.00 39.35  ? 2367 ASP A OD1   1 
ATOM   7288  O  OD2   . ASP A 1 2367 ? 95.978  112.903 131.208 1.00 47.50  ? 2367 ASP A OD2   1 
ATOM   7289  N  N     . VAL A 1 2368 ? 96.039  107.597 133.117 1.00 11.17  ? 2368 VAL A N     1 
ATOM   7290  C  CA    . VAL A 1 2368 ? 95.650  106.610 134.122 1.00 10.90  ? 2368 VAL A CA    1 
ATOM   7291  C  C     . VAL A 1 2368 ? 96.881  105.963 134.741 1.00 10.28  ? 2368 VAL A C     1 
ATOM   7292  O  O     . VAL A 1 2368 ? 96.974  105.811 135.966 1.00 8.41   ? 2368 VAL A O     1 
ATOM   7293  C  CB    . VAL A 1 2368 ? 94.709  105.560 133.501 1.00 8.78   ? 2368 VAL A CB    1 
ATOM   7294  C  CG1   . VAL A 1 2368 ? 94.495  104.404 134.456 1.00 7.19   ? 2368 VAL A CG1   1 
ATOM   7295  C  CG2   . VAL A 1 2368 ? 93.379  106.195 133.132 1.00 10.42  ? 2368 VAL A CG2   1 
ATOM   7296  N  N     . LEU A 1 2369 ? 97.845  105.577 133.912 1.00 11.60  ? 2369 LEU A N     1 
ATOM   7297  C  CA    . LEU A 1 2369 ? 99.104  105.000 134.376 1.00 8.16   ? 2369 LEU A CA    1 
ATOM   7298  C  C     . LEU A 1 2369 ? 100.151 106.107 134.364 1.00 7.20   ? 2369 LEU A C     1 
ATOM   7299  O  O     . LEU A 1 2369 ? 100.651 106.492 133.304 1.00 12.30  ? 2369 LEU A O     1 
ATOM   7300  C  CB    . LEU A 1 2369 ? 99.516  103.824 133.498 1.00 6.02   ? 2369 LEU A CB    1 
ATOM   7301  C  CG    . LEU A 1 2369 ? 100.831 103.126 133.839 1.00 4.88   ? 2369 LEU A CG    1 
ATOM   7302  C  CD1   . LEU A 1 2369 ? 100.827 102.622 135.273 1.00 3.50   ? 2369 LEU A CD1   1 
ATOM   7303  C  CD2   . LEU A 1 2369 ? 101.080 101.994 132.864 1.00 3.88   ? 2369 LEU A CD2   1 
ATOM   7304  N  N     . SER A 1 2370 ? 100.482 106.619 135.545 1.00 6.69   ? 2370 SER A N     1 
ATOM   7305  C  CA    . SER A 1 2370 ? 101.461 107.686 135.643 1.00 9.03   ? 2370 SER A CA    1 
ATOM   7306  C  C     . SER A 1 2370 ? 102.877 107.121 135.577 1.00 8.47   ? 2370 SER A C     1 
ATOM   7307  O  O     . SER A 1 2370 ? 103.117 105.936 135.826 1.00 7.69   ? 2370 SER A O     1 
ATOM   7308  C  CB    . SER A 1 2370 ? 101.269 108.480 136.936 1.00 8.30   ? 2370 SER A CB    1 
ATOM   7309  O  OG    . SER A 1 2370 ? 101.699 107.739 138.064 1.00 9.93   ? 2370 SER A OG    1 
ATOM   7310  N  N     . THR A 1 2371 ? 103.823 107.994 135.226 1.00 7.68   ? 2371 THR A N     1 
ATOM   7311  C  CA    . THR A 1 2371 ? 105.219 107.576 135.143 1.00 8.61   ? 2371 THR A CA    1 
ATOM   7312  C  C     . THR A 1 2371 ? 105.772 107.203 136.513 1.00 10.17  ? 2371 THR A C     1 
ATOM   7313  O  O     . THR A 1 2371 ? 106.615 106.303 136.618 1.00 9.25   ? 2371 THR A O     1 
ATOM   7314  C  CB    . THR A 1 2371 ? 106.059 108.683 134.508 1.00 11.40  ? 2371 THR A CB    1 
ATOM   7315  O  OG1   . THR A 1 2371 ? 105.395 109.175 133.338 1.00 16.72  ? 2371 THR A OG1   1 
ATOM   7316  C  CG2   . THR A 1 2371 ? 107.425 108.153 134.111 1.00 10.13  ? 2371 THR A CG2   1 
ATOM   7317  N  N     . ASP A 1 2372 ? 105.309 107.877 137.568 1.00 10.70  ? 2372 ASP A N     1 
ATOM   7318  C  CA    . ASP A 1 2372 ? 105.728 107.517 138.918 1.00 10.94  ? 2372 ASP A CA    1 
ATOM   7319  C  C     . ASP A 1 2372 ? 105.285 106.104 139.272 1.00 8.39   ? 2372 ASP A C     1 
ATOM   7320  O  O     . ASP A 1 2372 ? 105.992 105.387 139.986 1.00 9.76   ? 2372 ASP A O     1 
ATOM   7321  C  CB    . ASP A 1 2372 ? 105.175 108.522 139.927 1.00 16.20  ? 2372 ASP A CB    1 
ATOM   7322  C  CG    . ASP A 1 2372 ? 106.060 109.742 140.074 1.00 44.51  ? 2372 ASP A CG    1 
ATOM   7323  O  OD1   . ASP A 1 2372 ? 107.159 109.612 140.654 1.00 42.07  ? 2372 ASP A OD1   1 
ATOM   7324  O  OD2   . ASP A 1 2372 ? 105.660 110.830 139.609 1.00 51.92  ? 2372 ASP A OD2   1 
ATOM   7325  N  N     . MET A 1 2373 ? 104.117 105.687 138.781 1.00 7.13   ? 2373 MET A N     1 
ATOM   7326  C  CA    . MET A 1 2373 ? 103.657 104.321 139.013 1.00 5.73   ? 2373 MET A CA    1 
ATOM   7327  C  C     . MET A 1 2373 ? 104.608 103.308 138.384 1.00 5.85   ? 2373 MET A C     1 
ATOM   7328  O  O     . MET A 1 2373 ? 104.962 102.299 139.008 1.00 5.18   ? 2373 MET A O     1 
ATOM   7329  C  CB    . MET A 1 2373 ? 102.245 104.163 138.450 1.00 5.13   ? 2373 MET A CB    1 
ATOM   7330  C  CG    . MET A 1 2373 ? 101.171 104.820 139.301 1.00 5.66   ? 2373 MET A CG    1 
ATOM   7331  S  SD    . MET A 1 2373 ? 99.584  104.967 138.459 1.00 4.86   ? 2373 MET A SD    1 
ATOM   7332  C  CE    . MET A 1 2373 ? 99.036  103.267 138.436 1.00 3.13   ? 2373 MET A CE    1 
ATOM   7333  N  N     . ILE A 1 2374 ? 105.047 103.576 137.152 1.00 7.06   ? 2374 ILE A N     1 
ATOM   7334  C  CA    . ILE A 1 2374 ? 105.982 102.689 136.468 1.00 5.73   ? 2374 ILE A CA    1 
ATOM   7335  C  C     . ILE A 1 2374 ? 107.323 102.664 137.190 1.00 6.40   ? 2374 ILE A C     1 
ATOM   7336  O  O     . ILE A 1 2374 ? 107.945 101.604 137.343 1.00 7.24   ? 2374 ILE A O     1 
ATOM   7337  C  CB    . ILE A 1 2374 ? 106.135 103.127 135.001 1.00 7.12   ? 2374 ILE A CB    1 
ATOM   7338  C  CG1   . ILE A 1 2374 ? 104.770 103.139 134.311 1.00 5.24   ? 2374 ILE A CG1   1 
ATOM   7339  C  CG2   . ILE A 1 2374 ? 107.098 102.208 134.268 1.00 5.73   ? 2374 ILE A CG2   1 
ATOM   7340  C  CD1   . ILE A 1 2374 ? 104.758 103.880 132.996 1.00 6.51   ? 2374 ILE A CD1   1 
ATOM   7341  N  N     . PHE A 1 2375 ? 107.797 103.832 137.633 1.00 6.19   ? 2375 PHE A N     1 
ATOM   7342  C  CA    . PHE A 1 2375 ? 109.052 103.892 138.375 1.00 6.60   ? 2375 PHE A CA    1 
ATOM   7343  C  C     . PHE A 1 2375 ? 108.960 103.107 139.677 1.00 7.27   ? 2375 PHE A C     1 
ATOM   7344  O  O     . PHE A 1 2375 ? 109.896 102.387 140.045 1.00 10.06  ? 2375 PHE A O     1 
ATOM   7345  C  CB    . PHE A 1 2375 ? 109.426 105.347 138.657 1.00 7.74   ? 2375 PHE A CB    1 
ATOM   7346  C  CG    . PHE A 1 2375 ? 109.866 106.107 137.442 1.00 7.56   ? 2375 PHE A CG    1 
ATOM   7347  C  CD1   . PHE A 1 2375 ? 110.233 105.440 136.285 1.00 7.75   ? 2375 PHE A CD1   1 
ATOM   7348  C  CD2   . PHE A 1 2375 ? 109.916 107.490 137.457 1.00 9.41   ? 2375 PHE A CD2   1 
ATOM   7349  C  CE1   . PHE A 1 2375 ? 110.640 106.139 135.167 1.00 9.17   ? 2375 PHE A CE1   1 
ATOM   7350  C  CE2   . PHE A 1 2375 ? 110.323 108.194 136.341 1.00 12.85  ? 2375 PHE A CE2   1 
ATOM   7351  C  CZ    . PHE A 1 2375 ? 110.686 107.517 135.196 1.00 11.59  ? 2375 PHE A CZ    1 
ATOM   7352  N  N     . ASN A 1 2376 ? 107.838 103.240 140.389 1.00 6.40   ? 2376 ASN A N     1 
ATOM   7353  C  CA    . ASN A 1 2376 ? 107.638 102.482 141.618 1.00 6.64   ? 2376 ASN A CA    1 
ATOM   7354  C  C     . ASN A 1 2376 ? 107.636 100.987 141.343 1.00 6.49   ? 2376 ASN A C     1 
ATOM   7355  O  O     . ASN A 1 2376 ? 108.227 100.211 142.099 1.00 7.85   ? 2376 ASN A O     1 
ATOM   7356  C  CB    . ASN A 1 2376 ? 106.330 102.900 142.290 1.00 7.24   ? 2376 ASN A CB    1 
ATOM   7357  C  CG    . ASN A 1 2376 ? 106.367 104.323 142.804 1.00 8.88   ? 2376 ASN A CG    1 
ATOM   7358  O  OD1   . ASN A 1 2376 ? 107.426 104.945 142.870 1.00 12.42  ? 2376 ASN A OD1   1 
ATOM   7359  N  ND2   . ASN A 1 2376 ? 105.204 104.850 143.169 1.00 7.31   ? 2376 ASN A ND2   1 
ATOM   7360  N  N     . ASN A 1 2377 ? 106.970 100.564 140.265 1.00 5.61   ? 2377 ASN A N     1 
ATOM   7361  C  CA    . ASN A 1 2377 ? 106.964 99.148  139.914 1.00 6.49   ? 2377 ASN A CA    1 
ATOM   7362  C  C     . ASN A 1 2377 ? 108.377 98.644  139.647 1.00 7.49   ? 2377 ASN A C     1 
ATOM   7363  O  O     . ASN A 1 2377 ? 108.791 97.603  140.174 1.00 7.49   ? 2377 ASN A O     1 
ATOM   7364  C  CB    . ASN A 1 2377 ? 106.070 98.915  138.696 1.00 6.14   ? 2377 ASN A CB    1 
ATOM   7365  C  CG    . ASN A 1 2377 ? 106.075 97.471  138.237 1.00 7.67   ? 2377 ASN A CG    1 
ATOM   7366  O  OD1   . ASN A 1 2377 ? 106.482 97.167  137.117 1.00 15.00  ? 2377 ASN A OD1   1 
ATOM   7367  N  ND2   . ASN A 1 2377 ? 105.619 96.574  139.102 1.00 6.86   ? 2377 ASN A ND2   1 
ATOM   7368  N  N     . PHE A 1 2378 ? 109.140 99.387  138.840 1.00 7.76   ? 2378 PHE A N     1 
ATOM   7369  C  CA    . PHE A 1 2378 ? 110.494 98.961  138.503 1.00 5.50   ? 2378 PHE A CA    1 
ATOM   7370  C  C     . PHE A 1 2378 ? 111.376 98.888  139.743 1.00 5.31   ? 2378 PHE A C     1 
ATOM   7371  O  O     . PHE A 1 2378 ? 112.126 97.921  139.924 1.00 5.87   ? 2378 PHE A O     1 
ATOM   7372  C  CB    . PHE A 1 2378 ? 111.100 99.906  137.465 1.00 4.63   ? 2378 PHE A CB    1 
ATOM   7373  C  CG    . PHE A 1 2378 ? 112.602 99.939  137.479 1.00 4.76   ? 2378 PHE A CG    1 
ATOM   7374  C  CD1   . PHE A 1 2378 ? 113.336 98.891  136.949 1.00 3.45   ? 2378 PHE A CD1   1 
ATOM   7375  C  CD2   . PHE A 1 2378 ? 113.279 101.020 138.019 1.00 3.75   ? 2378 PHE A CD2   1 
ATOM   7376  C  CE1   . PHE A 1 2378 ? 114.717 98.919  136.960 1.00 3.60   ? 2378 PHE A CE1   1 
ATOM   7377  C  CE2   . PHE A 1 2378 ? 114.660 101.053 138.033 1.00 4.39   ? 2378 PHE A CE2   1 
ATOM   7378  C  CZ    . PHE A 1 2378 ? 115.379 100.002 137.503 1.00 4.82   ? 2378 PHE A CZ    1 
ATOM   7379  N  N     . LEU A 1 2379 ? 111.286 99.891  140.619 1.00 5.79   ? 2379 LEU A N     1 
ATOM   7380  C  CA    . LEU A 1 2379 ? 112.121 99.891  141.814 1.00 7.55   ? 2379 LEU A CA    1 
ATOM   7381  C  C     . LEU A 1 2379 ? 111.702 98.804  142.797 1.00 8.75   ? 2379 LEU A C     1 
ATOM   7382  O  O     . LEU A 1 2379 ? 112.560 98.213  143.460 1.00 11.36  ? 2379 LEU A O     1 
ATOM   7383  C  CB    . LEU A 1 2379 ? 112.088 101.266 142.477 1.00 7.64   ? 2379 LEU A CB    1 
ATOM   7384  C  CG    . LEU A 1 2379 ? 112.938 102.317 141.759 1.00 8.97   ? 2379 LEU A CG    1 
ATOM   7385  C  CD1   . LEU A 1 2379 ? 112.853 103.662 142.455 1.00 9.81   ? 2379 LEU A CD1   1 
ATOM   7386  C  CD2   . LEU A 1 2379 ? 114.385 101.856 141.648 1.00 9.83   ? 2379 LEU A CD2   1 
ATOM   7387  N  N     . ALA A 1 2380 ? 110.402 98.515  142.900 1.00 7.45   ? 2380 ALA A N     1 
ATOM   7388  C  CA    . ALA A 1 2380 ? 109.955 97.430  143.766 1.00 8.14   ? 2380 ALA A CA    1 
ATOM   7389  C  C     . ALA A 1 2380 ? 110.466 96.083  143.273 1.00 10.18  ? 2380 ALA A C     1 
ATOM   7390  O  O     . ALA A 1 2380 ? 110.952 95.269  144.070 1.00 15.05  ? 2380 ALA A O     1 
ATOM   7391  C  CB    . ALA A 1 2380 ? 108.430 97.427  143.860 1.00 10.12  ? 2380 ALA A CB    1 
ATOM   7392  N  N     . ARG A 1 2381 ? 110.374 95.829  141.963 1.00 8.52   ? 2381 ARG A N     1 
ATOM   7393  C  CA    . ARG A 1 2381 ? 110.924 94.580  141.440 1.00 9.36   ? 2381 ARG A CA    1 
ATOM   7394  C  C     . ARG A 1 2381 ? 112.437 94.517  141.605 1.00 10.61  ? 2381 ARG A C     1 
ATOM   7395  O  O     . ARG A 1 2381 ? 112.982 93.437  141.860 1.00 12.09  ? 2381 ARG A O     1 
ATOM   7396  C  CB    . ARG A 1 2381 ? 110.538 94.380  139.973 1.00 9.48   ? 2381 ARG A CB    1 
ATOM   7397  C  CG    . ARG A 1 2381 ? 109.086 94.674  139.653 1.00 9.97   ? 2381 ARG A CG    1 
ATOM   7398  C  CD    . ARG A 1 2381 ? 108.758 94.337  138.210 1.00 9.74   ? 2381 ARG A CD    1 
ATOM   7399  N  NE    . ARG A 1 2381 ? 108.265 92.972  138.070 1.00 13.88  ? 2381 ARG A NE    1 
ATOM   7400  C  CZ    . ARG A 1 2381 ? 108.946 91.983  137.509 1.00 19.82  ? 2381 ARG A CZ    1 
ATOM   7401  N  NH1   . ARG A 1 2381 ? 110.160 92.171  137.019 1.00 27.26  ? 2381 ARG A NH1   1 
ATOM   7402  N  NH2   . ARG A 1 2381 ? 108.395 90.775  137.439 1.00 22.99  ? 2381 ARG A NH2   1 
ATOM   7403  N  N     . LEU A 1 2382 ? 113.132 95.647  141.458 1.00 8.53   ? 2382 LEU A N     1 
ATOM   7404  C  CA    . LEU A 1 2382 ? 114.574 95.650  141.688 1.00 10.19  ? 2382 LEU A CA    1 
ATOM   7405  C  C     . LEU A 1 2382 ? 114.906 95.323  143.140 1.00 13.88  ? 2382 LEU A C     1 
ATOM   7406  O  O     . LEU A 1 2382 ? 115.841 94.563  143.415 1.00 16.12  ? 2382 LEU A O     1 
ATOM   7407  C  CB    . LEU A 1 2382 ? 115.170 97.000  141.297 1.00 11.06  ? 2382 LEU A CB    1 
ATOM   7408  C  CG    . LEU A 1 2382 ? 116.699 97.048  141.315 1.00 13.81  ? 2382 LEU A CG    1 
ATOM   7409  C  CD1   . LEU A 1 2382 ? 117.276 96.080  140.295 1.00 10.47  ? 2382 LEU A CD1   1 
ATOM   7410  C  CD2   . LEU A 1 2382 ? 117.201 98.457  141.070 1.00 7.83   ? 2382 LEU A CD2   1 
ATOM   7411  N  N     . ARG A 1 2383 ? 114.149 95.887  144.081 1.00 11.85  ? 2383 ARG A N     1 
ATOM   7412  C  CA    . ARG A 1 2383 ? 114.405 95.678  145.500 1.00 10.67  ? 2383 ARG A CA    1 
ATOM   7413  C  C     . ARG A 1 2383 ? 113.950 94.313  145.997 1.00 13.87  ? 2383 ARG A C     1 
ATOM   7414  O  O     . ARG A 1 2383 ? 114.407 93.879  147.059 1.00 19.68  ? 2383 ARG A O     1 
ATOM   7415  C  CB    . ARG A 1 2383 ? 113.718 96.771  146.324 1.00 10.14  ? 2383 ARG A CB    1 
ATOM   7416  C  CG    . ARG A 1 2383 ? 114.362 98.138  146.196 1.00 10.48  ? 2383 ARG A CG    1 
ATOM   7417  C  CD    . ARG A 1 2383 ? 113.578 99.200  146.949 1.00 9.68   ? 2383 ARG A CD    1 
ATOM   7418  N  NE    . ARG A 1 2383 ? 114.381 100.389 147.203 1.00 15.09  ? 2383 ARG A NE    1 
ATOM   7419  C  CZ    . ARG A 1 2383 ? 114.108 101.594 146.721 1.00 15.43  ? 2383 ARG A CZ    1 
ATOM   7420  N  NH1   . ARG A 1 2383 ? 113.048 101.810 145.960 1.00 14.82  ? 2383 ARG A NH1   1 
ATOM   7421  N  NH2   . ARG A 1 2383 ? 114.920 102.607 147.008 1.00 9.32   ? 2383 ARG A NH2   1 
ATOM   7422  N  N     . SER A 1 2384 ? 113.070 93.631  145.271 1.00 15.44  ? 2384 SER A N     1 
ATOM   7423  C  CA    . SER A 1 2384 ? 112.554 92.346  145.727 1.00 16.36  ? 2384 SER A CA    1 
ATOM   7424  C  C     . SER A 1 2384 ? 113.045 91.161  144.913 1.00 19.83  ? 2384 SER A C     1 
ATOM   7425  O  O     . SER A 1 2384 ? 113.467 90.158  145.494 1.00 25.53  ? 2384 SER A O     1 
ATOM   7426  C  CB    . SER A 1 2384 ? 111.020 92.365  145.716 1.00 19.06  ? 2384 SER A CB    1 
ATOM   7427  O  OG    . SER A 1 2384 ? 110.491 91.116  146.125 1.00 30.87  ? 2384 SER A OG    1 
ATOM   7428  N  N     . ILE A 1 2385 ? 113.006 91.241  143.589 1.00 20.17  ? 2385 ILE A N     1 
ATOM   7429  C  CA    . ILE A 1 2385 ? 113.319 90.113  142.716 1.00 20.43  ? 2385 ILE A CA    1 
ATOM   7430  C  C     . ILE A 1 2385 ? 114.809 90.152  142.395 1.00 22.26  ? 2385 ILE A C     1 
ATOM   7431  O  O     . ILE A 1 2385 ? 115.280 91.147  141.824 1.00 22.57  ? 2385 ILE A O     1 
ATOM   7432  C  CB    . ILE A 1 2385 ? 112.479 90.145  141.431 1.00 19.85  ? 2385 ILE A CB    1 
ATOM   7433  C  CG1   . ILE A 1 2385 ? 110.997 90.313  141.769 1.00 15.48  ? 2385 ILE A CG1   1 
ATOM   7434  C  CG2   . ILE A 1 2385 ? 112.707 88.882  140.616 1.00 16.54  ? 2385 ILE A CG2   1 
ATOM   7435  C  CD1   . ILE A 1 2385 ? 110.107 90.459  140.555 1.00 17.29  ? 2385 ILE A CD1   1 
ATOM   7436  N  N     . PRO A 1 2386 ? 115.576 89.118  142.738 1.00 26.67  ? 2386 PRO A N     1 
ATOM   7437  C  CA    . PRO A 1 2386 ? 116.996 89.102  142.368 1.00 26.18  ? 2386 PRO A CA    1 
ATOM   7438  C  C     . PRO A 1 2386 ? 117.178 88.811  140.886 1.00 26.04  ? 2386 PRO A C     1 
ATOM   7439  O  O     . PRO A 1 2386 ? 116.461 87.996  140.300 1.00 34.05  ? 2386 PRO A O     1 
ATOM   7440  C  CB    . PRO A 1 2386 ? 117.582 87.979  143.235 1.00 26.52  ? 2386 PRO A CB    1 
ATOM   7441  C  CG    . PRO A 1 2386 ? 116.501 87.620  144.227 1.00 25.92  ? 2386 PRO A CG    1 
ATOM   7442  C  CD    . PRO A 1 2386 ? 115.211 87.956  143.561 1.00 21.47  ? 2386 PRO A CD    1 
ATOM   7443  N  N     . LEU A 1 2387 ? 118.152 89.492  140.279 1.00 25.09  ? 2387 LEU A N     1 
ATOM   7444  C  CA    . LEU A 1 2387 ? 118.410 89.317  138.854 1.00 26.86  ? 2387 LEU A CA    1 
ATOM   7445  C  C     . LEU A 1 2387 ? 119.163 88.028  138.549 1.00 31.67  ? 2387 LEU A C     1 
ATOM   7446  O  O     . LEU A 1 2387 ? 119.015 87.480  137.451 1.00 32.97  ? 2387 LEU A O     1 
ATOM   7447  C  CB    . LEU A 1 2387 ? 119.189 90.515  138.306 1.00 25.40  ? 2387 LEU A CB    1 
ATOM   7448  C  CG    . LEU A 1 2387 ? 118.496 91.876  138.377 1.00 21.41  ? 2387 LEU A CG    1 
ATOM   7449  C  CD1   . LEU A 1 2387 ? 119.506 93.000  138.217 1.00 17.43  ? 2387 LEU A CD1   1 
ATOM   7450  C  CD2   . LEU A 1 2387 ? 117.404 91.977  137.325 1.00 14.94  ? 2387 LEU A CD2   1 
ATOM   7451  N  N     . ASP A 1 2388 ? 119.976 87.537  139.489 1.00 38.72  ? 2388 ASP A N     1 
ATOM   7452  C  CA    . ASP A 1 2388 ? 120.790 86.356  139.216 1.00 40.18  ? 2388 ASP A CA    1 
ATOM   7453  C  C     . ASP A 1 2388 ? 119.923 85.131  138.948 1.00 46.18  ? 2388 ASP A C     1 
ATOM   7454  O  O     . ASP A 1 2388 ? 120.216 84.342  138.042 1.00 53.14  ? 2388 ASP A O     1 
ATOM   7455  C  CB    . ASP A 1 2388 ? 121.749 86.094  140.379 1.00 40.09  ? 2388 ASP A CB    1 
ATOM   7456  C  CG    . ASP A 1 2388 ? 121.031 85.924  141.702 1.00 48.79  ? 2388 ASP A CG    1 
ATOM   7457  O  OD1   . ASP A 1 2388 ? 120.368 86.883  142.147 1.00 48.36  ? 2388 ASP A OD1   1 
ATOM   7458  O  OD2   . ASP A 1 2388 ? 121.130 84.831  142.298 1.00 55.67  ? 2388 ASP A OD2   1 
ATOM   7459  N  N     . GLU A 1 2389 ? 118.854 84.958  139.718 1.00 43.15  ? 2389 GLU A N     1 
ATOM   7460  C  CA    . GLU A 1 2389 ? 117.949 83.830  139.528 1.00 54.89  ? 2389 GLU A CA    1 
ATOM   7461  C  C     . GLU A 1 2389 ? 116.594 84.110  140.169 1.00 51.90  ? 2389 GLU A C     1 
ATOM   7462  O  O     . GLU A 1 2389 ? 116.511 84.740  141.223 0.00 45.59  ? 2389 GLU A O     1 
ATOM   7463  C  CB    . GLU A 1 2389 ? 118.556 82.549  140.108 1.00 59.87  ? 2389 GLU A CB    1 
ATOM   7464  C  CG    . GLU A 1 2389 ? 117.668 81.312  140.004 1.00 58.97  ? 2389 GLU A CG    1 
ATOM   7465  C  CD    . GLU A 1 2389 ? 117.510 80.808  138.578 1.00 71.08  ? 2389 GLU A CD    1 
ATOM   7466  O  OE1   . GLU A 1 2389 ? 116.856 81.491  137.762 1.00 74.93  ? 2389 GLU A OE1   1 
ATOM   7467  O  OE2   . GLU A 1 2389 ? 118.045 79.721  138.273 1.00 80.20  ? 2389 GLU A OE2   1 
ATOM   7468  N  N     . SER A 1 2410 ? 120.797 87.629  149.712 1.00 39.46  ? 2410 SER A N     1 
ATOM   7469  C  CA    . SER A 1 2410 ? 121.539 87.393  148.479 1.00 37.20  ? 2410 SER A CA    1 
ATOM   7470  C  C     . SER A 1 2410 ? 122.415 88.592  148.133 1.00 39.84  ? 2410 SER A C     1 
ATOM   7471  O  O     . SER A 1 2410 ? 121.940 89.728  148.131 1.00 36.36  ? 2410 SER A O     1 
ATOM   7472  C  CB    . SER A 1 2410 ? 120.581 87.089  147.326 1.00 37.09  ? 2410 SER A CB    1 
ATOM   7473  O  OG    . SER A 1 2410 ? 121.280 86.959  146.101 1.00 41.01  ? 2410 SER A OG    1 
ATOM   7474  N  N     . PRO A 1 2411 ? 123.698 88.340  147.855 1.00 41.01  ? 2411 PRO A N     1 
ATOM   7475  C  CA    . PRO A 1 2411 ? 124.589 89.451  147.478 1.00 40.12  ? 2411 PRO A CA    1 
ATOM   7476  C  C     . PRO A 1 2411 ? 124.130 90.190  146.233 1.00 33.70  ? 2411 PRO A C     1 
ATOM   7477  O  O     . PRO A 1 2411 ? 124.258 91.419  146.161 1.00 34.38  ? 2411 PRO A O     1 
ATOM   7478  C  CB    . PRO A 1 2411 ? 125.941 88.754  147.269 1.00 39.67  ? 2411 PRO A CB    1 
ATOM   7479  C  CG    . PRO A 1 2411 ? 125.593 87.332  146.965 1.00 40.35  ? 2411 PRO A CG    1 
ATOM   7480  C  CD    . PRO A 1 2411 ? 124.375 87.034  147.786 1.00 36.89  ? 2411 PRO A CD    1 
ATOM   7481  N  N     . MET A 1 2412 ? 123.590 89.470  145.248 1.00 31.43  ? 2412 MET A N     1 
ATOM   7482  C  CA    . MET A 1 2412 ? 123.054 90.127  144.061 1.00 29.76  ? 2412 MET A CA    1 
ATOM   7483  C  C     . MET A 1 2412 ? 121.851 90.992  144.420 1.00 26.09  ? 2412 MET A C     1 
ATOM   7484  O  O     . MET A 1 2412 ? 121.724 92.126  143.940 1.00 22.09  ? 2412 MET A O     1 
ATOM   7485  C  CB    . MET A 1 2412 ? 122.674 89.078  143.015 1.00 24.67  ? 2412 MET A CB    1 
ATOM   7486  C  CG    . MET A 1 2412 ? 122.025 89.634  141.760 1.00 29.95  ? 2412 MET A CG    1 
ATOM   7487  S  SD    . MET A 1 2412 ? 123.229 90.452  140.695 1.00 37.81  ? 2412 MET A SD    1 
ATOM   7488  C  CE    . MET A 1 2412 ? 122.519 92.085  140.543 1.00 21.35  ? 2412 MET A CE    1 
ATOM   7489  N  N     . LEU A 1 2413 ? 120.966 90.474  145.275 1.00 27.52  ? 2413 LEU A N     1 
ATOM   7490  C  CA    . LEU A 1 2413 ? 119.834 91.263  145.746 1.00 26.09  ? 2413 LEU A CA    1 
ATOM   7491  C  C     . LEU A 1 2413 ? 120.297 92.460  146.565 1.00 23.40  ? 2413 LEU A C     1 
ATOM   7492  O  O     . LEU A 1 2413 ? 119.695 93.536  146.495 1.00 23.46  ? 2413 LEU A O     1 
ATOM   7493  C  CB    . LEU A 1 2413 ? 118.884 90.388  146.565 1.00 30.62  ? 2413 LEU A CB    1 
ATOM   7494  C  CG    . LEU A 1 2413 ? 117.450 90.905  146.702 1.00 26.81  ? 2413 LEU A CG    1 
ATOM   7495  C  CD1   . LEU A 1 2413 ? 116.945 91.470  145.381 1.00 21.59  ? 2413 LEU A CD1   1 
ATOM   7496  C  CD2   . LEU A 1 2413 ? 116.530 89.806  147.206 1.00 26.01  ? 2413 LEU A CD2   1 
ATOM   7497  N  N     . GLN A 1 2414 ? 121.360 92.292  147.355 1.00 23.80  ? 2414 GLN A N     1 
ATOM   7498  C  CA    . GLN A 1 2414 ? 121.911 93.420  148.101 1.00 23.90  ? 2414 GLN A CA    1 
ATOM   7499  C  C     . GLN A 1 2414 ? 122.429 94.500  147.158 1.00 25.78  ? 2414 GLN A C     1 
ATOM   7500  O  O     . GLN A 1 2414 ? 122.222 95.699  147.394 1.00 28.40  ? 2414 GLN A O     1 
ATOM   7501  C  CB    . GLN A 1 2414 ? 123.026 92.935  149.030 1.00 27.65  ? 2414 GLN A CB    1 
ATOM   7502  C  CG    . GLN A 1 2414 ? 123.410 93.893  150.159 1.00 33.19  ? 2414 GLN A CG    1 
ATOM   7503  C  CD    . GLN A 1 2414 ? 122.227 94.606  150.799 1.00 35.21  ? 2414 GLN A CD    1 
ATOM   7504  O  OE1   . GLN A 1 2414 ? 121.147 94.035  150.963 1.00 37.26  ? 2414 GLN A OE1   1 
ATOM   7505  N  NE2   . GLN A 1 2414 ? 122.431 95.867  151.163 1.00 38.27  ? 2414 GLN A NE2   1 
ATOM   7506  N  N     . ILE A 1 2415 ? 123.102 94.091  146.079 1.00 23.52  ? 2415 ILE A N     1 
ATOM   7507  C  CA    . ILE A 1 2415 ? 123.580 95.049  145.086 1.00 21.36  ? 2415 ILE A CA    1 
ATOM   7508  C  C     . ILE A 1 2415 ? 122.407 95.770  144.435 1.00 19.93  ? 2415 ILE A C     1 
ATOM   7509  O  O     . ILE A 1 2415 ? 122.442 96.991  144.239 1.00 21.41  ? 2415 ILE A O     1 
ATOM   7510  C  CB    . ILE A 1 2415 ? 124.462 94.338  144.043 1.00 26.01  ? 2415 ILE A CB    1 
ATOM   7511  C  CG1   . ILE A 1 2415 ? 125.808 93.952  144.658 1.00 27.12  ? 2415 ILE A CG1   1 
ATOM   7512  C  CG2   . ILE A 1 2415 ? 124.667 95.219  142.817 1.00 18.82  ? 2415 ILE A CG2   1 
ATOM   7513  C  CD1   . ILE A 1 2415 ? 126.733 93.239  143.699 1.00 22.08  ? 2415 ILE A CD1   1 
ATOM   7514  N  N     . GLN A 1 2416 ? 121.351 95.028  144.092 1.00 18.61  ? 2416 GLN A N     1 
ATOM   7515  C  CA    . GLN A 1 2416 ? 120.171 95.653  143.499 1.00 13.51  ? 2416 GLN A CA    1 
ATOM   7516  C  C     . GLN A 1 2416 ? 119.517 96.638  144.460 1.00 16.36  ? 2416 GLN A C     1 
ATOM   7517  O  O     . GLN A 1 2416 ? 119.058 97.707  144.045 1.00 15.19  ? 2416 GLN A O     1 
ATOM   7518  C  CB    . GLN A 1 2416 ? 119.162 94.591  143.063 1.00 14.23  ? 2416 GLN A CB    1 
ATOM   7519  C  CG    . GLN A 1 2416 ? 119.690 93.613  142.038 1.00 15.97  ? 2416 GLN A CG    1 
ATOM   7520  C  CD    . GLN A 1 2416 ? 118.794 92.405  141.868 1.00 15.64  ? 2416 GLN A CD    1 
ATOM   7521  O  OE1   . GLN A 1 2416 ? 119.265 91.304  141.590 1.00 22.26  ? 2416 GLN A OE1   1 
ATOM   7522  N  NE2   . GLN A 1 2416 ? 117.492 92.606  142.034 1.00 16.16  ? 2416 GLN A NE2   1 
ATOM   7523  N  N     . ARG A 1 2417 ? 119.450 96.290  145.745 1.00 19.90  ? 2417 ARG A N     1 
ATOM   7524  C  CA    . ARG A 1 2417 ? 118.843 97.184  146.726 1.00 16.89  ? 2417 ARG A CA    1 
ATOM   7525  C  C     . ARG A 1 2417 ? 119.659 98.461  146.887 1.00 18.81  ? 2417 ARG A C     1 
ATOM   7526  O  O     . ARG A 1 2417 ? 119.096 99.561  146.956 1.00 19.00  ? 2417 ARG A O     1 
ATOM   7527  C  CB    . ARG A 1 2417 ? 118.692 96.459  148.063 1.00 20.52  ? 2417 ARG A CB    1 
ATOM   7528  C  CG    . ARG A 1 2417 ? 117.617 95.384  148.046 1.00 21.82  ? 2417 ARG A CG    1 
ATOM   7529  C  CD    . ARG A 1 2417 ? 117.080 95.081  149.432 1.00 19.81  ? 2417 ARG A CD    1 
ATOM   7530  N  NE    . ARG A 1 2417 ? 115.930 94.187  149.371 1.00 27.74  ? 2417 ARG A NE    1 
ATOM   7531  C  CZ    . ARG A 1 2417 ? 115.817 93.060  150.061 1.00 26.62  ? 2417 ARG A CZ    1 
ATOM   7532  N  NH1   . ARG A 1 2417 ? 116.771 92.653  150.881 1.00 28.99  ? 2417 ARG A NH1   1 
ATOM   7533  N  NH2   . ARG A 1 2417 ? 114.721 92.320  149.920 1.00 25.98  ? 2417 ARG A NH2   1 
ATOM   7534  N  N     . ASP A 1 2418 ? 120.988 98.337  146.938 1.00 19.61  ? 2418 ASP A N     1 
ATOM   7535  C  CA    . ASP A 1 2418 ? 121.831 99.527  147.010 1.00 19.64  ? 2418 ASP A CA    1 
ATOM   7536  C  C     . ASP A 1 2418 ? 121.682 100.386 145.759 1.00 21.26  ? 2418 ASP A C     1 
ATOM   7537  O  O     . ASP A 1 2418 ? 121.614 101.619 145.846 1.00 20.22  ? 2418 ASP A O     1 
ATOM   7538  C  CB    . ASP A 1 2418 ? 123.290 99.125  147.220 1.00 29.68  ? 2418 ASP A CB    1 
ATOM   7539  C  CG    . ASP A 1 2418 ? 123.543 98.543  148.597 1.00 42.83  ? 2418 ASP A CG    1 
ATOM   7540  O  OD1   . ASP A 1 2418 ? 122.819 98.916  149.543 1.00 41.81  ? 2418 ASP A OD1   1 
ATOM   7541  O  OD2   . ASP A 1 2418 ? 124.468 97.716  148.733 1.00 46.29  ? 2418 ASP A OD2   1 
ATOM   7542  N  N     . ALA A 1 2419 ? 121.621 99.752  144.584 1.00 16.83  ? 2419 ALA A N     1 
ATOM   7543  C  CA    . ALA A 1 2419 ? 121.446 100.503 143.345 1.00 14.92  ? 2419 ALA A CA    1 
ATOM   7544  C  C     . ALA A 1 2419 ? 120.102 101.219 143.318 1.00 15.12  ? 2419 ALA A C     1 
ATOM   7545  O  O     . ALA A 1 2419 ? 120.006 102.355 142.842 1.00 16.19  ? 2419 ALA A O     1 
ATOM   7546  C  CB    . ALA A 1 2419 ? 121.584 99.572  142.141 1.00 12.02  ? 2419 ALA A CB    1 
ATOM   7547  N  N     . ALA A 1 2420 ? 119.049 100.564 143.812 1.00 14.68  ? 2420 ALA A N     1 
ATOM   7548  C  CA    . ALA A 1 2420 ? 117.746 101.213 143.901 1.00 12.74  ? 2420 ALA A CA    1 
ATOM   7549  C  C     . ALA A 1 2420 ? 117.789 102.400 144.854 1.00 13.95  ? 2420 ALA A C     1 
ATOM   7550  O  O     . ALA A 1 2420 ? 117.187 103.445 144.583 1.00 14.72  ? 2420 ALA A O     1 
ATOM   7551  C  CB    . ALA A 1 2420 ? 116.686 100.206 144.345 1.00 8.53   ? 2420 ALA A CB    1 
ATOM   7552  N  N     . THR A 1 2421 ? 118.494 102.254 145.978 1.00 11.67  ? 2421 THR A N     1 
ATOM   7553  C  CA    . THR A 1 2421 ? 118.646 103.373 146.902 1.00 12.07  ? 2421 THR A CA    1 
ATOM   7554  C  C     . THR A 1 2421 ? 119.350 104.545 146.229 1.00 14.38  ? 2421 THR A C     1 
ATOM   7555  O  O     . THR A 1 2421 ? 118.972 105.706 146.428 1.00 16.94  ? 2421 THR A O     1 
ATOM   7556  C  CB    . THR A 1 2421 ? 119.417 102.931 148.146 1.00 18.17  ? 2421 THR A CB    1 
ATOM   7557  O  OG1   . THR A 1 2421 ? 118.819 101.745 148.686 1.00 23.14  ? 2421 THR A OG1   1 
ATOM   7558  C  CG2   . THR A 1 2421 ? 119.398 104.026 149.202 1.00 16.39  ? 2421 THR A CG2   1 
ATOM   7559  N  N     . ILE A 1 2422 ? 120.378 104.259 145.429 1.00 14.93  ? 2422 ILE A N     1 
ATOM   7560  C  CA    . ILE A 1 2422 ? 121.085 105.322 144.718 1.00 15.76  ? 2422 ILE A CA    1 
ATOM   7561  C  C     . ILE A 1 2422 ? 120.184 105.976 143.673 1.00 16.07  ? 2422 ILE A C     1 
ATOM   7562  O  O     . ILE A 1 2422 ? 120.177 107.203 143.523 1.00 18.26  ? 2422 ILE A O     1 
ATOM   7563  C  CB    . ILE A 1 2422 ? 122.380 104.778 144.088 1.00 20.19  ? 2422 ILE A CB    1 
ATOM   7564  C  CG1   . ILE A 1 2422 ? 123.263 104.136 145.158 1.00 17.62  ? 2422 ILE A CG1   1 
ATOM   7565  C  CG2   . ILE A 1 2422 ? 123.133 105.886 143.366 1.00 19.44  ? 2422 ILE A CG2   1 
ATOM   7566  C  CD1   . ILE A 1 2422 ? 124.365 103.273 144.599 1.00 15.34  ? 2422 ILE A CD1   1 
ATOM   7567  N  N     . MET A 1 2423 ? 119.419 105.175 142.929 1.00 13.53  ? 2423 MET A N     1 
ATOM   7568  C  CA    . MET A 1 2423 ? 118.644 105.686 141.803 1.00 14.08  ? 2423 MET A CA    1 
ATOM   7569  C  C     . MET A 1 2423 ? 117.317 106.318 142.199 1.00 16.93  ? 2423 MET A C     1 
ATOM   7570  O  O     . MET A 1 2423 ? 116.726 107.024 141.375 1.00 18.52  ? 2423 MET A O     1 
ATOM   7571  C  CB    . MET A 1 2423 ? 118.375 104.568 140.794 1.00 14.63  ? 2423 MET A CB    1 
ATOM   7572  C  CG    . MET A 1 2423 ? 119.619 104.022 140.143 1.00 19.62  ? 2423 MET A CG    1 
ATOM   7573  S  SD    . MET A 1 2423 ? 119.273 102.850 138.826 1.00 39.51  ? 2423 MET A SD    1 
ATOM   7574  C  CE    . MET A 1 2423 ? 118.626 101.472 139.762 1.00 10.83  ? 2423 MET A CE    1 
ATOM   7575  N  N     . GLN A 1 2424 ? 116.832 106.078 143.415 1.00 18.96  ? 2424 GLN A N     1 
ATOM   7576  C  CA    . GLN A 1 2424 ? 115.531 106.610 143.818 1.00 16.15  ? 2424 GLN A CA    1 
ATOM   7577  C  C     . GLN A 1 2424 ? 115.389 108.121 143.653 1.00 18.96  ? 2424 GLN A C     1 
ATOM   7578  O  O     . GLN A 1 2424 ? 114.333 108.556 143.162 1.00 20.07  ? 2424 GLN A O     1 
ATOM   7579  C  CB    . GLN A 1 2424 ? 115.239 106.194 145.267 1.00 15.12  ? 2424 GLN A CB    1 
ATOM   7580  C  CG    . GLN A 1 2424 ? 113.860 106.594 145.761 1.00 16.77  ? 2424 GLN A CG    1 
ATOM   7581  C  CD    . GLN A 1 2424 ? 112.802 105.563 145.421 1.00 23.50  ? 2424 GLN A CD    1 
ATOM   7582  O  OE1   . GLN A 1 2424 ? 112.860 104.423 145.880 1.00 25.15  ? 2424 GLN A OE1   1 
ATOM   7583  N  NE2   . GLN A 1 2424 ? 111.827 105.960 144.613 1.00 24.38  ? 2424 GLN A NE2   1 
ATOM   7584  N  N     . PRO A 1 2425 ? 116.361 108.966 144.033 1.00 19.55  ? 2425 PRO A N     1 
ATOM   7585  C  CA    . PRO A 1 2425 ? 116.163 110.416 143.846 1.00 18.50  ? 2425 PRO A CA    1 
ATOM   7586  C  C     . PRO A 1 2425 ? 115.904 110.827 142.406 1.00 19.55  ? 2425 PRO A C     1 
ATOM   7587  O  O     . PRO A 1 2425 ? 115.144 111.773 142.167 1.00 24.64  ? 2425 PRO A O     1 
ATOM   7588  C  CB    . PRO A 1 2425 ? 117.473 111.015 144.377 1.00 19.73  ? 2425 PRO A CB    1 
ATOM   7589  C  CG    . PRO A 1 2425 ? 117.971 110.016 145.344 1.00 20.65  ? 2425 PRO A CG    1 
ATOM   7590  C  CD    . PRO A 1 2425 ? 117.608 108.685 144.767 1.00 16.69  ? 2425 PRO A CD    1 
ATOM   7591  N  N     . TYR A 1 2426 ? 116.518 110.151 141.436 1.00 22.06  ? 2426 TYR A N     1 
ATOM   7592  C  CA    . TYR A 1 2426 ? 116.306 110.492 140.035 1.00 17.06  ? 2426 TYR A CA    1 
ATOM   7593  C  C     . TYR A 1 2426 ? 115.005 109.937 139.472 1.00 17.63  ? 2426 TYR A C     1 
ATOM   7594  O  O     . TYR A 1 2426 ? 114.605 110.340 138.375 1.00 20.96  ? 2426 TYR A O     1 
ATOM   7595  C  CB    . TYR A 1 2426 ? 117.478 109.997 139.184 1.00 17.16  ? 2426 TYR A CB    1 
ATOM   7596  C  CG    . TYR A 1 2426 ? 118.833 110.430 139.691 1.00 16.89  ? 2426 TYR A CG    1 
ATOM   7597  C  CD1   . TYR A 1 2426 ? 119.337 111.687 139.388 1.00 13.97  ? 2426 TYR A CD1   1 
ATOM   7598  C  CD2   . TYR A 1 2426 ? 119.611 109.582 140.468 1.00 16.35  ? 2426 TYR A CD2   1 
ATOM   7599  C  CE1   . TYR A 1 2426 ? 120.574 112.090 139.846 1.00 17.12  ? 2426 TYR A CE1   1 
ATOM   7600  C  CE2   . TYR A 1 2426 ? 120.851 109.976 140.931 1.00 15.63  ? 2426 TYR A CE2   1 
ATOM   7601  C  CZ    . TYR A 1 2426 ? 121.327 111.231 140.617 1.00 19.36  ? 2426 TYR A CZ    1 
ATOM   7602  O  OH    . TYR A 1 2426 ? 122.561 111.631 141.073 1.00 24.43  ? 2426 TYR A OH    1 
ATOM   7603  N  N     . PHE A 1 2427 ? 114.336 109.032 140.187 1.00 19.19  ? 2427 PHE A N     1 
ATOM   7604  C  CA    . PHE A 1 2427 ? 113.102 108.416 139.716 1.00 18.71  ? 2427 PHE A CA    1 
ATOM   7605  C  C     . PHE A 1 2427 ? 111.870 108.967 140.428 1.00 22.32  ? 2427 PHE A C     1 
ATOM   7606  O  O     . PHE A 1 2427 ? 110.888 108.243 140.620 1.00 27.10  ? 2427 PHE A O     1 
ATOM   7607  C  CB    . PHE A 1 2427 ? 113.179 106.898 139.875 1.00 16.04  ? 2427 PHE A CB    1 
ATOM   7608  C  CG    . PHE A 1 2427 ? 113.919 106.210 138.763 1.00 13.41  ? 2427 PHE A CG    1 
ATOM   7609  C  CD1   . PHE A 1 2427 ? 113.332 106.042 137.522 1.00 11.01  ? 2427 PHE A CD1   1 
ATOM   7610  C  CD2   . PHE A 1 2427 ? 115.205 105.735 138.959 1.00 17.72  ? 2427 PHE A CD2   1 
ATOM   7611  C  CE1   . PHE A 1 2427 ? 114.010 105.411 136.498 1.00 10.46  ? 2427 PHE A CE1   1 
ATOM   7612  C  CE2   . PHE A 1 2427 ? 115.889 105.104 137.939 1.00 11.87  ? 2427 PHE A CE2   1 
ATOM   7613  C  CZ    . PHE A 1 2427 ? 115.290 104.941 136.706 1.00 9.08   ? 2427 PHE A CZ    1 
ATOM   7614  N  N     . THR A 1 2428 ? 111.904 110.238 140.824 1.00 25.66  ? 2428 THR A N     1 
ATOM   7615  C  CA    . THR A 1 2428 ? 110.782 110.874 141.496 1.00 29.19  ? 2428 THR A CA    1 
ATOM   7616  C  C     . THR A 1 2428 ? 109.927 111.646 140.493 1.00 33.24  ? 2428 THR A C     1 
ATOM   7617  O  O     . THR A 1 2428 ? 110.114 111.562 139.278 1.00 32.71  ? 2428 THR A O     1 
ATOM   7618  C  CB    . THR A 1 2428 ? 111.274 111.800 142.607 1.00 32.59  ? 2428 THR A CB    1 
ATOM   7619  O  OG1   . THR A 1 2428 ? 111.882 112.962 142.028 1.00 29.31  ? 2428 THR A OG1   1 
ATOM   7620  C  CG2   . THR A 1 2428 ? 112.284 111.090 143.491 1.00 24.92  ? 2428 THR A CG2   1 
ATOM   7621  N  N     . SER A 1 2429 ? 108.964 112.404 141.010 1.00 44.06  ? 2429 SER A N     1 
ATOM   7622  C  CA    . SER A 1 2429 ? 108.152 113.265 140.162 1.00 43.56  ? 2429 SER A CA    1 
ATOM   7623  C  C     . SER A 1 2429 ? 108.958 114.487 139.739 1.00 41.99  ? 2429 SER A C     1 
ATOM   7624  O  O     . SER A 1 2429 ? 109.644 115.103 140.560 1.00 45.24  ? 2429 SER A O     1 
ATOM   7625  C  CB    . SER A 1 2429 ? 106.884 113.694 140.897 1.00 47.10  ? 2429 SER A CB    1 
ATOM   7626  O  OG    . SER A 1 2429 ? 105.879 112.700 140.805 1.00 44.77  ? 2429 SER A OG    1 
ATOM   7627  N  N     . ASN A 1 2430 ? 108.872 114.835 138.453 1.00 38.49  ? 2430 ASN A N     1 
ATOM   7628  C  CA    . ASN A 1 2430 ? 109.631 115.946 137.877 1.00 38.36  ? 2430 ASN A CA    1 
ATOM   7629  C  C     . ASN A 1 2430 ? 111.131 115.776 138.101 1.00 37.24  ? 2430 ASN A C     1 
ATOM   7630  O  O     . ASN A 1 2430 ? 111.851 116.751 138.332 1.00 41.12  ? 2430 ASN A O     1 
ATOM   7631  C  CB    . ASN A 1 2430 ? 109.157 117.295 138.427 1.00 39.74  ? 2430 ASN A CB    1 
ATOM   7632  C  CG    . ASN A 1 2430 ? 107.939 117.826 137.698 1.00 48.29  ? 2430 ASN A CG    1 
ATOM   7633  O  OD1   . ASN A 1 2430 ? 107.757 117.575 136.507 1.00 51.47  ? 2430 ASN A OD1   1 
ATOM   7634  N  ND2   . ASN A 1 2430 ? 107.097 118.564 138.412 1.00 48.98  ? 2430 ASN A ND2   1 
ATOM   7635  N  N     . GLY A 1 2431 ? 111.609 114.536 138.035 1.00 34.21  ? 2431 GLY A N     1 
ATOM   7636  C  CA    . GLY A 1 2431 ? 113.008 114.235 138.236 1.00 25.85  ? 2431 GLY A CA    1 
ATOM   7637  C  C     . GLY A 1 2431 ? 113.789 114.231 136.937 1.00 22.96  ? 2431 GLY A C     1 
ATOM   7638  O  O     . GLY A 1 2431 ? 113.374 114.786 135.918 1.00 25.28  ? 2431 GLY A O     1 
ATOM   7639  N  N     . LEU A 1 2432 ? 114.954 113.584 136.988 1.00 21.75  ? 2432 LEU A N     1 
ATOM   7640  C  CA    . LEU A 1 2432 ? 115.845 113.559 135.833 1.00 18.40  ? 2432 LEU A CA    1 
ATOM   7641  C  C     . LEU A 1 2432 ? 115.227 112.779 134.677 1.00 16.59  ? 2432 LEU A C     1 
ATOM   7642  O  O     . LEU A 1 2432 ? 115.171 113.267 133.541 1.00 18.11  ? 2432 LEU A O     1 
ATOM   7643  C  CB    . LEU A 1 2432 ? 117.190 112.954 136.238 1.00 16.39  ? 2432 LEU A CB    1 
ATOM   7644  C  CG    . LEU A 1 2432 ? 118.228 112.721 135.141 1.00 15.78  ? 2432 LEU A CG    1 
ATOM   7645  C  CD1   . LEU A 1 2432 ? 118.742 114.053 134.623 1.00 16.86  ? 2432 LEU A CD1   1 
ATOM   7646  C  CD2   . LEU A 1 2432 ? 119.372 111.860 135.650 1.00 21.69  ? 2432 LEU A CD2   1 
ATOM   7647  N  N     . VAL A 1 2433 ? 114.743 111.565 134.954 1.00 15.67  ? 2433 VAL A N     1 
ATOM   7648  C  CA    . VAL A 1 2433 ? 114.235 110.700 133.893 1.00 12.66  ? 2433 VAL A CA    1 
ATOM   7649  C  C     . VAL A 1 2433 ? 112.967 111.280 133.279 1.00 14.38  ? 2433 VAL A C     1 
ATOM   7650  O  O     . VAL A 1 2433 ? 112.767 111.212 132.061 1.00 14.08  ? 2433 VAL A O     1 
ATOM   7651  C  CB    . VAL A 1 2433 ? 114.001 109.275 134.429 1.00 9.99   ? 2433 VAL A CB    1 
ATOM   7652  C  CG1   . VAL A 1 2433 ? 113.563 108.348 133.306 1.00 10.12  ? 2433 VAL A CG1   1 
ATOM   7653  C  CG2   . VAL A 1 2433 ? 115.250 108.748 135.114 1.00 9.25   ? 2433 VAL A CG2   1 
ATOM   7654  N  N     . THR A 1 2434 ? 112.085 111.848 134.105 1.00 18.74  ? 2434 THR A N     1 
ATOM   7655  C  CA    . THR A 1 2434 ? 110.833 112.396 133.589 1.00 18.81  ? 2434 THR A CA    1 
ATOM   7656  C  C     . THR A 1 2434 ? 111.090 113.580 132.662 1.00 16.56  ? 2434 THR A C     1 
ATOM   7657  O  O     . THR A 1 2434 ? 110.506 113.674 131.576 1.00 14.89  ? 2434 THR A O     1 
ATOM   7658  C  CB    . THR A 1 2434 ? 109.922 112.804 134.748 1.00 21.95  ? 2434 THR A CB    1 
ATOM   7659  O  OG1   . THR A 1 2434 ? 109.660 111.663 135.575 1.00 26.44  ? 2434 THR A OG1   1 
ATOM   7660  C  CG2   . THR A 1 2434 ? 108.603 113.347 134.223 1.00 24.37  ? 2434 THR A CG2   1 
ATOM   7661  N  N     . LYS A 1 2435 ? 111.967 114.498 133.078 1.00 16.16  ? 2435 LYS A N     1 
ATOM   7662  C  CA    . LYS A 1 2435 ? 112.312 115.632 132.226 1.00 16.22  ? 2435 LYS A CA    1 
ATOM   7663  C  C     . LYS A 1 2435 ? 113.007 115.169 130.953 1.00 16.47  ? 2435 LYS A C     1 
ATOM   7664  O  O     . LYS A 1 2435 ? 112.749 115.699 129.864 1.00 17.36  ? 2435 LYS A O     1 
ATOM   7665  C  CB    . LYS A 1 2435 ? 113.196 116.617 132.990 1.00 19.94  ? 2435 LYS A CB    1 
ATOM   7666  C  CG    . LYS A 1 2435 ? 112.498 117.321 134.139 1.00 24.63  ? 2435 LYS A CG    1 
ATOM   7667  C  CD    . LYS A 1 2435 ? 113.420 118.327 134.807 1.00 29.68  ? 2435 LYS A CD    1 
ATOM   7668  C  CE    . LYS A 1 2435 ? 112.749 118.981 136.003 1.00 41.22  ? 2435 LYS A CE    1 
ATOM   7669  N  NZ    . LYS A 1 2435 ? 111.611 119.850 135.597 1.00 39.94  ? 2435 LYS A NZ    1 
ATOM   7670  N  N     . ALA A 1 2436 ? 113.896 114.179 131.073 1.00 17.98  ? 2436 ALA A N     1 
ATOM   7671  C  CA    . ALA A 1 2436 ? 114.563 113.636 129.895 1.00 12.96  ? 2436 ALA A CA    1 
ATOM   7672  C  C     . ALA A 1 2436 ? 113.557 113.057 128.909 1.00 11.68  ? 2436 ALA A C     1 
ATOM   7673  O  O     . ALA A 1 2436 ? 113.662 113.286 127.701 1.00 14.03  ? 2436 ALA A O     1 
ATOM   7674  C  CB    . ALA A 1 2436 ? 115.576 112.572 130.315 1.00 10.15  ? 2436 ALA A CB    1 
ATOM   7675  N  N     . LEU A 1 2437 ? 112.577 112.302 129.408 1.00 9.85   ? 2437 LEU A N     1 
ATOM   7676  C  CA    . LEU A 1 2437 ? 111.562 111.716 128.537 1.00 11.55  ? 2437 LEU A CA    1 
ATOM   7677  C  C     . LEU A 1 2437 ? 110.701 112.793 127.888 1.00 14.50  ? 2437 LEU A C     1 
ATOM   7678  O  O     . LEU A 1 2437 ? 110.378 112.711 126.694 1.00 17.06  ? 2437 LEU A O     1 
ATOM   7679  C  CB    . LEU A 1 2437 ? 110.698 110.741 129.335 1.00 14.22  ? 2437 LEU A CB    1 
ATOM   7680  C  CG    . LEU A 1 2437 ? 109.728 109.855 128.556 1.00 19.24  ? 2437 LEU A CG    1 
ATOM   7681  C  CD1   . LEU A 1 2437 ? 110.467 109.065 127.487 1.00 22.37  ? 2437 LEU A CD1   1 
ATOM   7682  C  CD2   . LEU A 1 2437 ? 108.985 108.925 129.499 1.00 14.87  ? 2437 LEU A CD2   1 
ATOM   7683  N  N     . GLU A 1 2438 ? 110.318 113.812 128.662 1.00 15.82  ? 2438 GLU A N     1 
ATOM   7684  C  CA    . GLU A 1 2438 ? 109.515 114.897 128.111 1.00 16.94  ? 2438 GLU A CA    1 
ATOM   7685  C  C     . GLU A 1 2438 ? 110.263 115.619 126.998 1.00 18.51  ? 2438 GLU A C     1 
ATOM   7686  O  O     . GLU A 1 2438 ? 109.673 115.967 125.968 1.00 20.01  ? 2438 GLU A O     1 
ATOM   7687  C  CB    . GLU A 1 2438 ? 109.121 115.873 129.220 1.00 20.21  ? 2438 GLU A CB    1 
ATOM   7688  C  CG    . GLU A 1 2438 ? 107.812 116.600 128.965 1.00 25.29  ? 2438 GLU A CG    1 
ATOM   7689  C  CD    . GLU A 1 2438 ? 108.005 117.906 128.222 1.00 32.63  ? 2438 GLU A CD    1 
ATOM   7690  O  OE1   . GLU A 1 2438 ? 109.105 118.489 128.317 1.00 33.93  ? 2438 GLU A OE1   1 
ATOM   7691  O  OE2   . GLU A 1 2438 ? 107.056 118.350 127.542 1.00 42.96  ? 2438 GLU A OE2   1 
ATOM   7692  N  N     . HIS A 1 2439 ? 111.564 115.849 127.184 1.00 14.46  ? 2439 HIS A N     1 
ATOM   7693  C  CA    . HIS A 1 2439 ? 112.360 116.458 126.123 1.00 16.16  ? 2439 HIS A CA    1 
ATOM   7694  C  C     . HIS A 1 2439 ? 112.521 115.525 124.930 1.00 18.17  ? 2439 HIS A C     1 
ATOM   7695  O  O     . HIS A 1 2439 ? 112.512 115.983 123.781 1.00 19.02  ? 2439 HIS A O     1 
ATOM   7696  C  CB    . HIS A 1 2439 ? 113.729 116.864 126.661 1.00 18.02  ? 2439 HIS A CB    1 
ATOM   7697  C  CG    . HIS A 1 2439 ? 114.530 117.698 125.710 1.00 22.08  ? 2439 HIS A CG    1 
ATOM   7698  N  ND1   . HIS A 1 2439 ? 114.171 118.982 125.362 1.00 22.19  ? 2439 HIS A ND1   1 
ATOM   7699  C  CD2   . HIS A 1 2439 ? 115.674 117.432 125.036 1.00 20.97  ? 2439 HIS A CD2   1 
ATOM   7700  C  CE1   . HIS A 1 2439 ? 115.058 119.470 124.514 1.00 27.90  ? 2439 HIS A CE1   1 
ATOM   7701  N  NE2   . HIS A 1 2439 ? 115.980 118.550 124.299 1.00 24.08  ? 2439 HIS A NE2   1 
ATOM   7702  N  N     . ALA A 1 2440 ? 112.677 114.222 125.178 1.00 15.74  ? 2440 ALA A N     1 
ATOM   7703  C  CA    . ALA A 1 2440 ? 112.874 113.274 124.088 1.00 13.58  ? 2440 ALA A CA    1 
ATOM   7704  C  C     . ALA A 1 2440 ? 111.632 113.146 123.218 1.00 14.10  ? 2440 ALA A C     1 
ATOM   7705  O  O     . ALA A 1 2440 ? 111.747 112.865 122.020 1.00 17.59  ? 2440 ALA A O     1 
ATOM   7706  C  CB    . ALA A 1 2440 ? 113.274 111.908 124.646 1.00 10.94  ? 2440 ALA A CB    1 
ATOM   7707  N  N     . PHE A 1 2441 ? 110.443 113.337 123.796 1.00 15.71  ? 2441 PHE A N     1 
ATOM   7708  C  CA    . PHE A 1 2441 ? 109.236 113.297 122.971 1.00 17.85  ? 2441 PHE A CA    1 
ATOM   7709  C  C     . PHE A 1 2441 ? 109.223 114.399 121.918 1.00 19.21  ? 2441 PHE A C     1 
ATOM   7710  O  O     . PHE A 1 2441 ? 108.633 114.216 120.846 1.00 22.97  ? 2441 PHE A O     1 
ATOM   7711  C  CB    . PHE A 1 2441 ? 107.975 113.373 123.833 1.00 17.21  ? 2441 PHE A CB    1 
ATOM   7712  C  CG    . PHE A 1 2441 ? 107.492 112.034 124.316 1.00 18.60  ? 2441 PHE A CG    1 
ATOM   7713  C  CD1   . PHE A 1 2441 ? 106.648 111.271 123.526 1.00 17.78  ? 2441 PHE A CD1   1 
ATOM   7714  C  CD2   . PHE A 1 2441 ? 107.866 111.543 125.552 1.00 16.70  ? 2441 PHE A CD2   1 
ATOM   7715  C  CE1   . PHE A 1 2441 ? 106.196 110.040 123.955 1.00 18.79  ? 2441 PHE A CE1   1 
ATOM   7716  C  CE2   . PHE A 1 2441 ? 107.415 110.311 125.988 1.00 19.07  ? 2441 PHE A CE2   1 
ATOM   7717  C  CZ    . PHE A 1 2441 ? 106.580 109.559 125.188 1.00 19.22  ? 2441 PHE A CZ    1 
ATOM   7718  N  N     . GLN A 1 2442 ? 109.860 115.538 122.189 1.00 19.81  ? 2442 GLN A N     1 
ATOM   7719  C  CA    . GLN A 1 2442 ? 109.946 116.589 121.182 1.00 20.09  ? 2442 GLN A CA    1 
ATOM   7720  C  C     . GLN A 1 2442 ? 110.974 116.287 120.099 1.00 19.69  ? 2442 GLN A C     1 
ATOM   7721  O  O     . GLN A 1 2442 ? 110.880 116.851 119.003 1.00 24.72  ? 2442 GLN A O     1 
ATOM   7722  C  CB    . GLN A 1 2442 ? 110.269 117.933 121.839 1.00 26.58  ? 2442 GLN A CB    1 
ATOM   7723  C  CG    . GLN A 1 2442 ? 109.050 118.666 122.379 1.00 30.29  ? 2442 GLN A CG    1 
ATOM   7724  C  CD    . GLN A 1 2442 ? 108.562 118.106 123.699 1.00 33.94  ? 2442 GLN A CD    1 
ATOM   7725  O  OE1   . GLN A 1 2442 ? 109.107 118.420 124.757 1.00 34.91  ? 2442 GLN A OE1   1 
ATOM   7726  N  NE2   . GLN A 1 2442 ? 107.531 117.272 123.644 1.00 30.21  ? 2442 GLN A NE2   1 
ATOM   7727  N  N     . LEU A 1 2443 ? 111.943 115.419 120.373 1.00 22.53  ? 2443 LEU A N     1 
ATOM   7728  C  CA    . LEU A 1 2443 ? 112.941 115.069 119.376 1.00 18.05  ? 2443 LEU A CA    1 
ATOM   7729  C  C     . LEU A 1 2443 ? 112.329 114.180 118.294 1.00 18.57  ? 2443 LEU A C     1 
ATOM   7730  O  O     . LEU A 1 2443 ? 111.296 113.533 118.487 1.00 24.81  ? 2443 LEU A O     1 
ATOM   7731  C  CB    . LEU A 1 2443 ? 114.126 114.364 120.033 1.00 16.76  ? 2443 LEU A CB    1 
ATOM   7732  C  CG    . LEU A 1 2443 ? 114.852 115.167 121.112 1.00 21.08  ? 2443 LEU A CG    1 
ATOM   7733  C  CD1   . LEU A 1 2443 ? 115.917 114.326 121.800 1.00 18.66  ? 2443 LEU A CD1   1 
ATOM   7734  C  CD2   . LEU A 1 2443 ? 115.455 116.418 120.507 1.00 17.37  ? 2443 LEU A CD2   1 
ATOM   7735  N  N     . GLU A 1 2444 ? 112.982 114.156 117.136 1.00 16.70  ? 2444 GLU A N     1 
ATOM   7736  C  CA    . GLU A 1 2444 ? 112.610 113.257 116.053 1.00 18.61  ? 2444 GLU A CA    1 
ATOM   7737  C  C     . GLU A 1 2444 ? 113.313 111.916 116.218 1.00 15.95  ? 2444 GLU A C     1 
ATOM   7738  O  O     . GLU A 1 2444 ? 114.503 111.858 116.539 1.00 13.88  ? 2444 GLU A O     1 
ATOM   7739  C  CB    . GLU A 1 2444 ? 112.937 113.859 114.683 1.00 24.24  ? 2444 GLU A CB    1 
ATOM   7740  C  CG    . GLU A 1 2444 ? 112.105 115.084 114.300 1.00 36.05  ? 2444 GLU A CG    1 
ATOM   7741  C  CD    . GLU A 1 2444 ? 112.619 116.384 114.885 1.00 46.90  ? 2444 GLU A CD    1 
ATOM   7742  O  OE1   . GLU A 1 2444 ? 113.671 116.372 115.551 1.00 44.36  ? 2444 GLU A OE1   1 
ATOM   7743  O  OE2   . GLU A 1 2444 ? 111.965 117.427 114.672 1.00 53.18  ? 2444 GLU A OE2   1 
ATOM   7744  N  N     . HIS A 1 2445 ? 112.560 110.840 116.001 1.00 15.27  ? 2445 HIS A N     1 
ATOM   7745  C  CA    . HIS A 1 2445 ? 113.054 109.479 116.135 1.00 10.11  ? 2445 HIS A CA    1 
ATOM   7746  C  C     . HIS A 1 2445 ? 112.686 108.684 114.891 1.00 10.45  ? 2445 HIS A C     1 
ATOM   7747  O  O     . HIS A 1 2445 ? 111.693 108.976 114.220 1.00 10.31  ? 2445 HIS A O     1 
ATOM   7748  C  CB    . HIS A 1 2445 ? 112.485 108.796 117.385 1.00 9.61   ? 2445 HIS A CB    1 
ATOM   7749  C  CG    . HIS A 1 2445 ? 112.598 109.624 118.626 1.00 14.09  ? 2445 HIS A CG    1 
ATOM   7750  N  ND1   . HIS A 1 2445 ? 113.676 109.539 119.480 1.00 14.62  ? 2445 HIS A ND1   1 
ATOM   7751  C  CD2   . HIS A 1 2445 ? 111.777 110.565 119.148 1.00 12.59  ? 2445 HIS A CD2   1 
ATOM   7752  C  CE1   . HIS A 1 2445 ? 113.509 110.386 120.480 1.00 12.98  ? 2445 HIS A CE1   1 
ATOM   7753  N  NE2   . HIS A 1 2445 ? 112.367 111.023 120.301 1.00 14.17  ? 2445 HIS A NE2   1 
ATOM   7754  N  N     . ILE A 1 2446 ? 113.505 107.674 114.588 1.00 8.16   ? 2446 ILE A N     1 
ATOM   7755  C  CA    . ILE A 1 2446 ? 113.310 106.909 113.360 1.00 8.64   ? 2446 ILE A CA    1 
ATOM   7756  C  C     . ILE A 1 2446 ? 112.012 106.107 113.409 1.00 8.65   ? 2446 ILE A C     1 
ATOM   7757  O  O     . ILE A 1 2446 ? 111.416 105.818 112.364 1.00 9.52   ? 2446 ILE A O     1 
ATOM   7758  C  CB    . ILE A 1 2446 ? 114.543 106.025 113.085 1.00 9.07   ? 2446 ILE A CB    1 
ATOM   7759  C  CG1   . ILE A 1 2446 ? 114.683 105.771 111.583 1.00 7.96   ? 2446 ILE A CG1   1 
ATOM   7760  C  CG2   . ILE A 1 2446 ? 114.494 104.725 113.879 1.00 5.41   ? 2446 ILE A CG2   1 
ATOM   7761  C  CD1   . ILE A 1 2446 ? 114.828 107.030 110.762 1.00 9.86   ? 2446 ILE A CD1   1 
ATOM   7762  N  N     . MET A 1 2447 ? 111.553 105.734 114.600 1.00 10.72  ? 2447 MET A N     1 
ATOM   7763  C  CA    . MET A 1 2447 ? 110.226 105.172 114.798 1.00 9.52   ? 2447 MET A CA    1 
ATOM   7764  C  C     . MET A 1 2447 ? 109.432 106.064 115.742 1.00 11.32  ? 2447 MET A C     1 
ATOM   7765  O  O     . MET A 1 2447 ? 109.976 106.970 116.378 1.00 11.84  ? 2447 MET A O     1 
ATOM   7766  C  CB    . MET A 1 2447 ? 110.278 103.748 115.368 1.00 9.98   ? 2447 MET A CB    1 
ATOM   7767  C  CG    . MET A 1 2447 ? 111.107 102.764 114.575 1.00 12.54  ? 2447 MET A CG    1 
ATOM   7768  S  SD    . MET A 1 2447 ? 110.675 101.069 115.008 1.00 33.50  ? 2447 MET A SD    1 
ATOM   7769  C  CE    . MET A 1 2447 ? 111.570 100.165 113.754 1.00 4.33   ? 2447 MET A CE    1 
ATOM   7770  N  N     . ASP A 1 2448 ? 108.130 105.798 115.820 1.00 12.63  ? 2448 ASP A N     1 
ATOM   7771  C  CA    . ASP A 1 2448 ? 107.276 106.529 116.745 1.00 10.39  ? 2448 ASP A CA    1 
ATOM   7772  C  C     . ASP A 1 2448 ? 107.731 106.288 118.178 1.00 12.62  ? 2448 ASP A C     1 
ATOM   7773  O  O     . ASP A 1 2448 ? 108.088 105.166 118.549 1.00 14.91  ? 2448 ASP A O     1 
ATOM   7774  C  CB    . ASP A 1 2448 ? 105.819 106.108 116.567 1.00 11.08  ? 2448 ASP A CB    1 
ATOM   7775  C  CG    . ASP A 1 2448 ? 105.196 106.684 115.311 1.00 21.61  ? 2448 ASP A CG    1 
ATOM   7776  O  OD1   . ASP A 1 2448 ? 105.842 107.532 114.661 1.00 26.61  ? 2448 ASP A OD1   1 
ATOM   7777  O  OD2   . ASP A 1 2448 ? 104.059 106.291 114.976 1.00 25.98  ? 2448 ASP A OD2   1 
ATOM   7778  N  N     . LEU A 1 2449 ? 107.719 107.345 118.981 1.00 12.65  ? 2449 LEU A N     1 
ATOM   7779  C  CA    . LEU A 1 2449 ? 108.251 107.285 120.333 1.00 10.36  ? 2449 LEU A CA    1 
ATOM   7780  C  C     . LEU A 1 2449 ? 107.134 107.031 121.336 1.00 11.93  ? 2449 LEU A C     1 
ATOM   7781  O  O     . LEU A 1 2449 ? 106.112 107.723 121.335 1.00 14.28  ? 2449 LEU A O     1 
ATOM   7782  C  CB    . LEU A 1 2449 ? 108.975 108.584 120.686 1.00 12.75  ? 2449 LEU A CB    1 
ATOM   7783  C  CG    . LEU A 1 2449 ? 109.623 108.565 122.068 1.00 16.08  ? 2449 LEU A CG    1 
ATOM   7784  C  CD1   . LEU A 1 2449 ? 110.681 107.489 122.089 1.00 9.41   ? 2449 LEU A CD1   1 
ATOM   7785  C  CD2   . LEU A 1 2449 ? 110.216 109.907 122.436 1.00 15.13  ? 2449 LEU A CD2   1 
ATOM   7786  N  N     . THR A 1 2450 ? 107.338 106.034 122.193 1.00 8.42   ? 2450 THR A N     1 
ATOM   7787  C  CA    . THR A 1 2450 ? 106.402 105.710 123.258 1.00 6.48   ? 2450 THR A CA    1 
ATOM   7788  C  C     . THR A 1 2450 ? 107.151 105.643 124.581 1.00 6.31   ? 2450 THR A C     1 
ATOM   7789  O  O     . THR A 1 2450 ? 108.357 105.389 124.627 1.00 7.99   ? 2450 THR A O     1 
ATOM   7790  C  CB    . THR A 1 2450 ? 105.669 104.384 122.999 1.00 8.79   ? 2450 THR A CB    1 
ATOM   7791  O  OG1   . THR A 1 2450 ? 106.621 103.318 122.888 1.00 11.76  ? 2450 THR A OG1   1 
ATOM   7792  C  CG2   . THR A 1 2450 ? 104.846 104.465 121.720 1.00 9.95   ? 2450 THR A CG2   1 
ATOM   7793  N  N     . ARG A 1 2451 ? 106.411 105.882 125.665 1.00 6.48   ? 2451 ARG A N     1 
ATOM   7794  C  CA    . ARG A 1 2451 ? 107.019 105.948 126.991 1.00 6.48   ? 2451 ARG A CA    1 
ATOM   7795  C  C     . ARG A 1 2451 ? 107.597 104.600 127.411 1.00 6.28   ? 2451 ARG A C     1 
ATOM   7796  O  O     . ARG A 1 2451 ? 108.723 104.525 127.921 1.00 6.56   ? 2451 ARG A O     1 
ATOM   7797  C  CB    . ARG A 1 2451 ? 105.983 106.428 128.008 1.00 7.07   ? 2451 ARG A CB    1 
ATOM   7798  C  CG    . ARG A 1 2451 ? 106.413 106.277 129.454 1.00 8.62   ? 2451 ARG A CG    1 
ATOM   7799  C  CD    . ARG A 1 2451 ? 105.365 106.820 130.411 1.00 11.58  ? 2451 ARG A CD    1 
ATOM   7800  N  NE    . ARG A 1 2451 ? 104.068 106.180 130.225 1.00 11.91  ? 2451 ARG A NE    1 
ATOM   7801  C  CZ    . ARG A 1 2451 ? 102.992 106.441 130.955 1.00 12.72  ? 2451 ARG A CZ    1 
ATOM   7802  N  NH1   . ARG A 1 2451 ? 103.022 107.327 131.937 1.00 10.69  ? 2451 ARG A NH1   1 
ATOM   7803  N  NH2   . ARG A 1 2451 ? 101.859 105.796 130.695 1.00 10.00  ? 2451 ARG A NH2   1 
ATOM   7804  N  N     . LEU A 1 2452 ? 106.844 103.520 127.194 1.00 6.41   ? 2452 LEU A N     1 
ATOM   7805  C  CA    . LEU A 1 2452 ? 107.228 102.236 127.771 1.00 5.67   ? 2452 LEU A CA    1 
ATOM   7806  C  C     . LEU A 1 2452 ? 108.407 101.610 127.042 1.00 5.66   ? 2452 LEU A C     1 
ATOM   7807  O  O     . LEU A 1 2452 ? 109.178 100.863 127.647 1.00 4.92   ? 2452 LEU A O     1 
ATOM   7808  C  CB    . LEU A 1 2452 ? 106.038 101.282 127.796 1.00 6.06   ? 2452 LEU A CB    1 
ATOM   7809  C  CG    . LEU A 1 2452 ? 105.003 101.670 128.846 1.00 6.30   ? 2452 LEU A CG    1 
ATOM   7810  C  CD1   . LEU A 1 2452 ? 103.966 100.592 128.975 1.00 5.44   ? 2452 LEU A CD1   1 
ATOM   7811  C  CD2   . LEU A 1 2452 ? 105.691 101.899 130.176 1.00 5.58   ? 2452 LEU A CD2   1 
ATOM   7812  N  N     . ARG A 1 2453 ? 108.577 101.899 125.752 1.00 5.97   ? 2453 ARG A N     1 
ATOM   7813  C  CA    . ARG A 1 2453 ? 109.767 101.408 125.064 1.00 5.41   ? 2453 ARG A CA    1 
ATOM   7814  C  C     . ARG A 1 2453 ? 111.034 101.975 125.699 1.00 4.82   ? 2453 ARG A C     1 
ATOM   7815  O  O     . ARG A 1 2453 ? 111.962 101.226 126.041 1.00 5.75   ? 2453 ARG A O     1 
ATOM   7816  C  CB    . ARG A 1 2453 ? 109.694 101.755 123.576 1.00 4.87   ? 2453 ARG A CB    1 
ATOM   7817  C  CG    . ARG A 1 2453 ? 110.924 101.358 122.779 1.00 5.62   ? 2453 ARG A CG    1 
ATOM   7818  C  CD    . ARG A 1 2453 ? 110.713 101.530 121.279 1.00 4.46   ? 2453 ARG A CD    1 
ATOM   7819  N  NE    . ARG A 1 2453 ? 110.372 102.899 120.910 1.00 8.18   ? 2453 ARG A NE    1 
ATOM   7820  C  CZ    . ARG A 1 2453 ? 111.128 103.680 120.151 1.00 8.93   ? 2453 ARG A CZ    1 
ATOM   7821  N  NH1   . ARG A 1 2453 ? 112.294 103.271 119.684 1.00 8.21   ? 2453 ARG A NH1   1 
ATOM   7822  N  NH2   . ARG A 1 2453 ? 110.704 104.906 119.858 1.00 12.21  ? 2453 ARG A NH2   1 
ATOM   7823  N  N     . CYS A 1 2454 ? 111.070 103.295 125.899 1.00 4.66   ? 2454 CYS A N     1 
ATOM   7824  C  CA    . CYS A 1 2454 ? 112.213 103.929 126.548 1.00 4.31   ? 2454 CYS A CA    1 
ATOM   7825  C  C     . CYS A 1 2454 ? 112.387 103.432 127.975 1.00 4.57   ? 2454 CYS A C     1 
ATOM   7826  O  O     . CYS A 1 2454 ? 113.511 103.164 128.414 1.00 5.51   ? 2454 CYS A O     1 
ATOM   7827  C  CB    . CYS A 1 2454 ? 112.052 105.447 126.533 1.00 5.71   ? 2454 CYS A CB    1 
ATOM   7828  S  SG    . CYS A 1 2454 ? 112.095 106.181 124.898 1.00 24.76  ? 2454 CYS A SG    1 
ATOM   7829  N  N     . LEU A 1 2455 ? 111.286 103.320 128.724 1.00 4.21   ? 2455 LEU A N     1 
ATOM   7830  C  CA    . LEU A 1 2455 ? 111.402 102.890 130.113 1.00 3.34   ? 2455 LEU A CA    1 
ATOM   7831  C  C     . LEU A 1 2455 ? 111.894 101.451 130.214 1.00 3.03   ? 2455 LEU A C     1 
ATOM   7832  O  O     . LEU A 1 2455 ? 112.722 101.138 131.073 1.00 4.41   ? 2455 LEU A O     1 
ATOM   7833  C  CB    . LEU A 1 2455 ? 110.068 103.065 130.837 1.00 3.74   ? 2455 LEU A CB    1 
ATOM   7834  C  CG    . LEU A 1 2455 ? 109.645 104.523 131.032 1.00 5.08   ? 2455 LEU A CG    1 
ATOM   7835  C  CD1   . LEU A 1 2455 ? 108.415 104.618 131.917 1.00 7.29   ? 2455 LEU A CD1   1 
ATOM   7836  C  CD2   . LEU A 1 2455 ? 110.789 105.344 131.609 1.00 3.59   ? 2455 LEU A CD2   1 
ATOM   7837  N  N     . GLY A 1 2456 ? 111.408 100.564 129.344 1.00 2.76   ? 2456 GLY A N     1 
ATOM   7838  C  CA    . GLY A 1 2456 ? 111.892 99.196  129.345 1.00 3.47   ? 2456 GLY A CA    1 
ATOM   7839  C  C     . GLY A 1 2456 ? 113.359 99.099  128.980 1.00 5.59   ? 2456 GLY A C     1 
ATOM   7840  O  O     . GLY A 1 2456 ? 114.112 98.342  129.599 1.00 5.81   ? 2456 GLY A O     1 
ATOM   7841  N  N     . SER A 1 2457 ? 113.788 99.868  127.974 1.00 4.35   ? 2457 SER A N     1 
ATOM   7842  C  CA    . SER A 1 2457 ? 115.207 99.884  127.634 1.00 4.08   ? 2457 SER A CA    1 
ATOM   7843  C  C     . SER A 1 2457 ? 116.045 100.383 128.806 1.00 3.75   ? 2457 SER A C     1 
ATOM   7844  O  O     . SER A 1 2457 ? 117.086 99.799  129.130 1.00 4.29   ? 2457 SER A O     1 
ATOM   7845  C  CB    . SER A 1 2457 ? 115.442 100.749 126.397 1.00 3.82   ? 2457 SER A CB    1 
ATOM   7846  O  OG    . SER A 1 2457 ? 116.825 100.878 126.117 1.00 5.79   ? 2457 SER A OG    1 
ATOM   7847  N  N     . LEU A 1 2458 ? 115.589 101.450 129.467 1.00 3.56   ? 2458 LEU A N     1 
ATOM   7848  C  CA    . LEU A 1 2458 ? 116.320 101.995 130.606 1.00 3.66   ? 2458 LEU A CA    1 
ATOM   7849  C  C     . LEU A 1 2458 ? 116.399 100.991 131.749 1.00 3.72   ? 2458 LEU A C     1 
ATOM   7850  O  O     . LEU A 1 2458 ? 117.457 100.828 132.369 1.00 5.11   ? 2458 LEU A O     1 
ATOM   7851  C  CB    . LEU A 1 2458 ? 115.658 103.292 131.072 1.00 3.30   ? 2458 LEU A CB    1 
ATOM   7852  C  CG    . LEU A 1 2458 ? 116.203 103.952 132.340 1.00 4.70   ? 2458 LEU A CG    1 
ATOM   7853  C  CD1   . LEU A 1 2458 ? 117.605 104.484 132.108 1.00 3.84   ? 2458 LEU A CD1   1 
ATOM   7854  C  CD2   . LEU A 1 2458 ? 115.276 105.064 132.804 1.00 3.38   ? 2458 LEU A CD2   1 
ATOM   7855  N  N     . PHE A 1 2459 ? 115.292 100.304 132.041 1.00 3.68   ? 2459 PHE A N     1 
ATOM   7856  C  CA    . PHE A 1 2459 ? 115.283 99.344  133.141 1.00 3.87   ? 2459 PHE A CA    1 
ATOM   7857  C  C     . PHE A 1 2459 ? 116.168 98.143  132.833 1.00 5.02   ? 2459 PHE A C     1 
ATOM   7858  O  O     . PHE A 1 2459 ? 116.878 97.646  133.716 1.00 6.78   ? 2459 PHE A O     1 
ATOM   7859  C  CB    . PHE A 1 2459 ? 113.852 98.896  133.442 1.00 3.47   ? 2459 PHE A CB    1 
ATOM   7860  C  CG    . PHE A 1 2459 ? 112.925 100.022 133.815 1.00 3.06   ? 2459 PHE A CG    1 
ATOM   7861  C  CD1   . PHE A 1 2459 ? 113.414 101.180 134.398 1.00 3.33   ? 2459 PHE A CD1   1 
ATOM   7862  C  CD2   . PHE A 1 2459 ? 111.562 99.916  133.592 1.00 3.70   ? 2459 PHE A CD2   1 
ATOM   7863  C  CE1   . PHE A 1 2459 ? 112.564 102.213 134.740 1.00 3.77   ? 2459 PHE A CE1   1 
ATOM   7864  C  CE2   . PHE A 1 2459 ? 110.707 100.946 133.933 1.00 3.68   ? 2459 PHE A CE2   1 
ATOM   7865  C  CZ    . PHE A 1 2459 ? 111.208 102.096 134.508 1.00 4.08   ? 2459 PHE A CZ    1 
ATOM   7866  N  N     . SER A 1 2460 ? 116.143 97.664  131.586 1.00 6.12   ? 2460 SER A N     1 
ATOM   7867  C  CA    . SER A 1 2460 ? 117.036 96.578  131.197 1.00 5.08   ? 2460 SER A CA    1 
ATOM   7868  C  C     . SER A 1 2460 ? 118.495 97.000  131.319 1.00 6.04   ? 2460 SER A C     1 
ATOM   7869  O  O     . SER A 1 2460 ? 119.339 96.226  131.787 1.00 8.24   ? 2460 SER A O     1 
ATOM   7870  C  CB    . SER A 1 2460 ? 116.722 96.128  129.771 1.00 4.49   ? 2460 SER A CB    1 
ATOM   7871  O  OG    . SER A 1 2460 ? 115.400 95.628  129.673 1.00 10.79  ? 2460 SER A OG    1 
ATOM   7872  N  N     . MET A 1 2461 ? 118.808 98.231  130.911 1.00 6.30   ? 2461 MET A N     1 
ATOM   7873  C  CA    . MET A 1 2461 ? 120.180 98.715  131.016 1.00 5.72   ? 2461 MET A CA    1 
ATOM   7874  C  C     . MET A 1 2461 ? 120.614 98.832  132.474 1.00 6.33   ? 2461 MET A C     1 
ATOM   7875  O  O     . MET A 1 2461 ? 121.755 98.507  132.819 1.00 9.42   ? 2461 MET A O     1 
ATOM   7876  C  CB    . MET A 1 2461 ? 120.306 100.055 130.291 1.00 3.59   ? 2461 MET A CB    1 
ATOM   7877  C  CG    . MET A 1 2461 ? 120.248 99.917  128.774 1.00 5.56   ? 2461 MET A CG    1 
ATOM   7878  S  SD    . MET A 1 2461 ? 120.648 101.421 127.869 1.00 12.56  ? 2461 MET A SD    1 
ATOM   7879  C  CE    . MET A 1 2461 ? 122.408 101.516 128.155 1.00 6.78   ? 2461 MET A CE    1 
ATOM   7880  N  N     . LEU A 1 2462 ? 119.713 99.284  133.349 1.00 4.86   ? 2462 LEU A N     1 
ATOM   7881  C  CA    . LEU A 1 2462 ? 120.044 99.378  134.769 1.00 6.63   ? 2462 LEU A CA    1 
ATOM   7882  C  C     . LEU A 1 2462 ? 120.239 97.996  135.387 1.00 6.99   ? 2462 LEU A C     1 
ATOM   7883  O  O     . LEU A 1 2462 ? 121.112 97.805  136.246 1.00 10.83  ? 2462 LEU A O     1 
ATOM   7884  C  CB    . LEU A 1 2462 ? 118.954 100.159 135.502 1.00 5.09   ? 2462 LEU A CB    1 
ATOM   7885  C  CG    . LEU A 1 2462 ? 118.849 101.629 135.086 1.00 6.65   ? 2462 LEU A CG    1 
ATOM   7886  C  CD1   . LEU A 1 2462 ? 117.657 102.309 135.744 1.00 7.39   ? 2462 LEU A CD1   1 
ATOM   7887  C  CD2   . LEU A 1 2462 ? 120.142 102.379 135.378 1.00 6.72   ? 2462 LEU A CD2   1 
ATOM   7888  N  N     . HIS A 1 2463 ? 119.434 97.018  134.964 1.00 7.01   ? 2463 HIS A N     1 
ATOM   7889  C  CA    . HIS A 1 2463 ? 119.650 95.642  135.401 1.00 8.73   ? 2463 HIS A CA    1 
ATOM   7890  C  C     . HIS A 1 2463 ? 121.015 95.142  134.944 1.00 12.33  ? 2463 HIS A C     1 
ATOM   7891  O  O     . HIS A 1 2463 ? 121.714 94.436  135.684 1.00 14.97  ? 2463 HIS A O     1 
ATOM   7892  C  CB    . HIS A 1 2463 ? 118.541 94.743  134.855 1.00 11.50  ? 2463 HIS A CB    1 
ATOM   7893  C  CG    . HIS A 1 2463 ? 117.206 94.973  135.493 1.00 10.89  ? 2463 HIS A CG    1 
ATOM   7894  N  ND1   . HIS A 1 2463 ? 116.021 94.613  134.888 1.00 11.46  ? 2463 HIS A ND1   1 
ATOM   7895  C  CD2   . HIS A 1 2463 ? 116.868 95.534  136.678 1.00 9.79   ? 2463 HIS A CD2   1 
ATOM   7896  C  CE1   . HIS A 1 2463 ? 115.011 94.940  135.673 1.00 9.75   ? 2463 HIS A CE1   1 
ATOM   7897  N  NE2   . HIS A 1 2463 ? 115.498 95.500  136.766 1.00 10.05  ? 2463 HIS A NE2   1 
ATOM   7898  N  N     . GLN A 1 2464 ? 121.408 95.503  133.721 1.00 15.42  ? 2464 GLN A N     1 
ATOM   7899  C  CA    . GLN A 1 2464 ? 122.742 95.162  133.240 1.00 12.63  ? 2464 GLN A CA    1 
ATOM   7900  C  C     . GLN A 1 2464 ? 123.822 95.825  134.085 1.00 12.21  ? 2464 GLN A C     1 
ATOM   7901  O  O     . GLN A 1 2464 ? 124.879 95.236  134.322 1.00 17.13  ? 2464 GLN A O     1 
ATOM   7902  C  CB    . GLN A 1 2464 ? 122.892 95.556  131.772 1.00 13.03  ? 2464 GLN A CB    1 
ATOM   7903  C  CG    . GLN A 1 2464 ? 124.239 95.182  131.187 1.00 16.12  ? 2464 GLN A CG    1 
ATOM   7904  C  CD    . GLN A 1 2464 ? 124.583 93.727  131.422 1.00 17.00  ? 2464 GLN A CD    1 
ATOM   7905  O  OE1   . GLN A 1 2464 ? 123.787 92.834  131.131 1.00 22.37  ? 2464 GLN A OE1   1 
ATOM   7906  N  NE2   . GLN A 1 2464 ? 125.774 93.478  131.951 1.00 17.96  ? 2464 GLN A NE2   1 
ATOM   7907  N  N     . ALA A 1 2465 ? 123.584 97.059  134.531 1.00 9.82   ? 2465 ALA A N     1 
ATOM   7908  C  CA    . ALA A 1 2465 ? 124.541 97.721  135.416 1.00 10.39  ? 2465 ALA A CA    1 
ATOM   7909  C  C     . ALA A 1 2465 ? 124.680 96.972  136.737 1.00 15.40  ? 2465 ALA A C     1 
ATOM   7910  O  O     . ALA A 1 2465 ? 125.790 96.822  137.268 1.00 14.50  ? 2465 ALA A O     1 
ATOM   7911  C  CB    . ALA A 1 2465 ? 124.115 99.165  135.668 1.00 8.05   ? 2465 ALA A CB    1 
ATOM   7912  N  N     . CYS A 1 2466 ? 123.558 96.510  137.290 1.00 19.36  ? 2466 CYS A N     1 
ATOM   7913  C  CA    . CYS A 1 2466 ? 123.614 95.715  138.515 1.00 15.24  ? 2466 CYS A CA    1 
ATOM   7914  C  C     . CYS A 1 2466 ? 124.403 94.427  138.297 1.00 16.68  ? 2466 CYS A C     1 
ATOM   7915  O  O     . CYS A 1 2466 ? 125.223 94.035  139.140 1.00 18.71  ? 2466 CYS A O     1 
ATOM   7916  C  CB    . CYS A 1 2466 ? 122.200 95.407  139.007 1.00 16.70  ? 2466 CYS A CB    1 
ATOM   7917  S  SG    . CYS A 1 2466 ? 121.261 96.857  139.536 1.00 25.80  ? 2466 CYS A SG    1 
ATOM   7918  N  N     . ARG A 1 2467 ? 124.172 93.759  137.163 1.00 17.59  ? 2467 ARG A N     1 
ATOM   7919  C  CA    . ARG A 1 2467 ? 124.960 92.573  136.837 1.00 15.56  ? 2467 ARG A CA    1 
ATOM   7920  C  C     . ARG A 1 2467 ? 126.434 92.908  136.652 1.00 16.03  ? 2467 ARG A C     1 
ATOM   7921  O  O     . ARG A 1 2467 ? 127.300 92.093  136.984 1.00 20.71  ? 2467 ARG A O     1 
ATOM   7922  C  CB    . ARG A 1 2467 ? 124.413 91.891  135.584 1.00 15.37  ? 2467 ARG A CB    1 
ATOM   7923  C  CG    . ARG A 1 2467 ? 123.071 91.215  135.780 1.00 19.76  ? 2467 ARG A CG    1 
ATOM   7924  C  CD    . ARG A 1 2467 ? 122.529 90.699  134.462 1.00 23.30  ? 2467 ARG A CD    1 
ATOM   7925  N  NE    . ARG A 1 2467 ? 121.090 90.473  134.511 1.00 27.05  ? 2467 ARG A NE    1 
ATOM   7926  C  CZ    . ARG A 1 2467 ? 120.521 89.378  134.997 1.00 30.61  ? 2467 ARG A CZ    1 
ATOM   7927  N  NH1   . ARG A 1 2467 ? 121.242 88.382  135.485 1.00 22.09  ? 2467 ARG A NH1   1 
ATOM   7928  N  NH2   . ARG A 1 2467 ? 119.194 89.280  134.992 1.00 27.17  ? 2467 ARG A NH2   1 
ATOM   7929  N  N     . ASN A 1 2468 ? 126.739 94.088  136.110 1.00 15.99  ? 2468 ASN A N     1 
ATOM   7930  C  CA    . ASN A 1 2468 ? 128.128 94.514  135.974 1.00 16.71  ? 2468 ASN A CA    1 
ATOM   7931  C  C     . ASN A 1 2468 ? 128.787 94.660  137.336 1.00 18.66  ? 2468 ASN A C     1 
ATOM   7932  O  O     . ASN A 1 2468 ? 129.938 94.253  137.528 1.00 29.33  ? 2468 ASN A O     1 
ATOM   7933  C  CB    . ASN A 1 2468 ? 128.202 95.835  135.208 1.00 14.80  ? 2468 ASN A CB    1 
ATOM   7934  C  CG    . ASN A 1 2468 ? 127.852 95.683  133.742 1.00 17.19  ? 2468 ASN A CG    1 
ATOM   7935  O  OD1   . ASN A 1 2468 ? 127.730 94.570  133.232 1.00 14.20  ? 2468 ASN A OD1   1 
ATOM   7936  N  ND2   . ASN A 1 2468 ? 127.680 96.808  133.058 1.00 14.33  ? 2468 ASN A ND2   1 
ATOM   7937  N  N     . VAL A 1 2469 ? 128.070 95.248  138.295 1.00 18.92  ? 2469 VAL A N     1 
ATOM   7938  C  CA    . VAL A 1 2469 ? 128.604 95.376  139.649 1.00 14.93  ? 2469 VAL A CA    1 
ATOM   7939  C  C     . VAL A 1 2469 ? 128.828 93.999  140.265 1.00 19.72  ? 2469 VAL A C     1 
ATOM   7940  O  O     . VAL A 1 2469 ? 129.850 93.749  140.920 1.00 21.36  ? 2469 VAL A O     1 
ATOM   7941  C  CB    . VAL A 1 2469 ? 127.669 96.240  140.514 1.00 16.19  ? 2469 VAL A CB    1 
ATOM   7942  C  CG1   . VAL A 1 2469 ? 128.207 96.348  141.932 1.00 19.66  ? 2469 VAL A CG1   1 
ATOM   7943  C  CG2   . VAL A 1 2469 ? 127.507 97.616  139.895 1.00 13.39  ? 2469 VAL A CG2   1 
ATOM   7944  N  N     . ALA A 1 2470 ? 127.878 93.082  140.061 1.00 19.28  ? 2470 ALA A N     1 
ATOM   7945  C  CA    . ALA A 1 2470 ? 128.038 91.727  140.584 1.00 16.93  ? 2470 ALA A CA    1 
ATOM   7946  C  C     . ALA A 1 2470 ? 129.249 91.032  139.969 1.00 26.37  ? 2470 ALA A C     1 
ATOM   7947  O  O     . ALA A 1 2470 ? 130.013 90.357  140.670 1.00 32.24  ? 2470 ALA A O     1 
ATOM   7948  C  CB    . ALA A 1 2470 ? 126.770 90.914  140.335 1.00 17.13  ? 2470 ALA A CB    1 
ATOM   7949  N  N     . GLN A 1 2471 ? 129.442 91.187  138.659 1.00 27.78  ? 2471 GLN A N     1 
ATOM   7950  C  CA    . GLN A 1 2471 ? 130.567 90.540  137.994 1.00 30.81  ? 2471 GLN A CA    1 
ATOM   7951  C  C     . GLN A 1 2471 ? 131.892 91.168  138.412 1.00 33.41  ? 2471 GLN A C     1 
ATOM   7952  O  O     . GLN A 1 2471 ? 132.911 90.472  138.487 1.00 36.51  ? 2471 GLN A O     1 
ATOM   7953  C  CB    . GLN A 1 2471 ? 130.376 90.609  136.476 1.00 34.85  ? 2471 GLN A CB    1 
ATOM   7954  C  CG    . GLN A 1 2471 ? 131.356 89.783  135.655 1.00 35.83  ? 2471 GLN A CG    1 
ATOM   7955  C  CD    . GLN A 1 2471 ? 132.644 90.512  135.347 1.00 47.20  ? 2471 GLN A CD    1 
ATOM   7956  O  OE1   . GLN A 1 2471 ? 132.671 91.739  135.246 1.00 44.36  ? 2471 GLN A OE1   1 
ATOM   7957  N  NE2   . GLN A 1 2471 ? 133.721 89.756  135.176 1.00 52.42  ? 2471 GLN A NE2   1 
ATOM   7958  N  N     . TYR A 1 2472 ? 131.898 92.475  138.686 1.00 30.74  ? 2472 TYR A N     1 
ATOM   7959  C  CA    . TYR A 1 2472 ? 133.088 93.106  139.247 1.00 30.20  ? 2472 TYR A CA    1 
ATOM   7960  C  C     . TYR A 1 2472 ? 133.408 92.539  140.624 1.00 34.29  ? 2472 TYR A C     1 
ATOM   7961  O  O     . TYR A 1 2472 ? 134.575 92.283  140.942 1.00 37.14  ? 2472 TYR A O     1 
ATOM   7962  C  CB    . TYR A 1 2472 ? 132.900 94.625  139.306 1.00 25.72  ? 2472 TYR A CB    1 
ATOM   7963  C  CG    . TYR A 1 2472 ? 133.975 95.383  140.067 1.00 28.93  ? 2472 TYR A CG    1 
ATOM   7964  C  CD1   . TYR A 1 2472 ? 133.950 95.475  141.455 1.00 31.54  ? 2472 TYR A CD1   1 
ATOM   7965  C  CD2   . TYR A 1 2472 ? 135.022 95.998  139.393 1.00 29.41  ? 2472 TYR A CD2   1 
ATOM   7966  C  CE1   . TYR A 1 2472 ? 134.929 96.162  142.145 1.00 32.75  ? 2472 TYR A CE1   1 
ATOM   7967  C  CE2   . TYR A 1 2472 ? 136.006 96.687  140.076 1.00 32.58  ? 2472 TYR A CE2   1 
ATOM   7968  C  CZ    . TYR A 1 2472 ? 135.954 96.766  141.451 1.00 35.54  ? 2472 TYR A CZ    1 
ATOM   7969  O  OH    . TYR A 1 2472 ? 136.932 97.451  142.136 1.00 38.36  ? 2472 TYR A OH    1 
ATOM   7970  N  N     . ASN A 1 2473 ? 132.384 92.348  141.460 1.00 36.76  ? 2473 ASN A N     1 
ATOM   7971  C  CA    . ASN A 1 2473 ? 132.610 91.708  142.753 1.00 36.24  ? 2473 ASN A CA    1 
ATOM   7972  C  C     . ASN A 1 2473 ? 133.148 90.295  142.572 1.00 36.41  ? 2473 ASN A C     1 
ATOM   7973  O  O     . ASN A 1 2473 ? 133.968 89.825  143.369 1.00 37.20  ? 2473 ASN A O     1 
ATOM   7974  C  CB    . ASN A 1 2473 ? 131.322 91.692  143.575 1.00 25.50  ? 2473 ASN A CB    1 
ATOM   7975  C  CG    . ASN A 1 2473 ? 130.950 93.062  144.101 1.00 32.68  ? 2473 ASN A CG    1 
ATOM   7976  O  OD1   . ASN A 1 2473 ? 131.631 94.050  143.830 1.00 35.04  ? 2473 ASN A OD1   1 
ATOM   7977  N  ND2   . ASN A 1 2473 ? 129.869 93.127  144.868 1.00 32.77  ? 2473 ASN A ND2   1 
ATOM   7978  N  N     . ALA A 1 2474 ? 132.688 89.601  141.529 1.00 41.14  ? 2474 ALA A N     1 
ATOM   7979  C  CA    . ALA A 1 2474 ? 133.240 88.288  141.211 1.00 38.15  ? 2474 ALA A CA    1 
ATOM   7980  C  C     . ALA A 1 2474 ? 134.718 88.383  140.850 1.00 45.01  ? 2474 ALA A C     1 
ATOM   7981  O  O     . ALA A 1 2474 ? 135.520 87.533  141.255 1.00 48.20  ? 2474 ALA A O     1 
ATOM   7982  C  CB    . ALA A 1 2474 ? 132.448 87.645  140.073 1.00 30.56  ? 2474 ALA A CB    1 
ATOM   7983  N  N     . ASN A 1 2475 ? 135.099 89.410  140.083 1.00 43.18  ? 2475 ASN A N     1 
ATOM   7984  C  CA    . ASN A 1 2475 ? 136.502 89.591  139.725 1.00 40.22  ? 2475 ASN A CA    1 
ATOM   7985  C  C     . ASN A 1 2475 ? 137.368 89.972  140.918 1.00 42.20  ? 2475 ASN A C     1 
ATOM   7986  O  O     . ASN A 1 2475 ? 138.581 89.741  140.883 1.00 47.73  ? 2475 ASN A O     1 
ATOM   7987  C  CB    . ASN A 1 2475 ? 136.651 90.658  138.639 1.00 39.48  ? 2475 ASN A CB    1 
ATOM   7988  C  CG    . ASN A 1 2475 ? 135.871 90.331  137.387 1.00 43.16  ? 2475 ASN A CG    1 
ATOM   7989  O  OD1   . ASN A 1 2475 ? 135.321 89.238  137.248 1.00 41.73  ? 2475 ASN A OD1   1 
ATOM   7990  N  ND2   . ASN A 1 2475 ? 135.828 91.278  136.457 1.00 42.62  ? 2475 ASN A ND2   1 
ATOM   7991  N  N     . HIS A 1 2476 ? 136.784 90.550  141.964 1.00 40.77  ? 2476 HIS A N     1 
ATOM   7992  C  CA    . HIS A 1 2476 ? 137.522 90.979  143.152 1.00 47.38  ? 2476 HIS A CA    1 
ATOM   7993  C  C     . HIS A 1 2476 ? 136.869 90.382  144.391 1.00 52.95  ? 2476 HIS A C     1 
ATOM   7994  O  O     . HIS A 1 2476 ? 136.174 91.078  145.142 1.00 55.21  ? 2476 HIS A O     1 
ATOM   7995  C  CB    . HIS A 1 2476 ? 137.576 92.505  143.245 1.00 42.65  ? 2476 HIS A CB    1 
ATOM   7996  C  CG    . HIS A 1 2476 ? 138.146 93.168  142.030 1.00 39.91  ? 2476 HIS A CG    1 
ATOM   7997  N  ND1   . HIS A 1 2476 ? 137.474 93.228  140.828 1.00 40.92  ? 2476 HIS A ND1   1 
ATOM   7998  C  CD2   . HIS A 1 2476 ? 139.325 93.806  141.833 1.00 38.53  ? 2476 HIS A CD2   1 
ATOM   7999  C  CE1   . HIS A 1 2476 ? 138.214 93.870  139.942 1.00 41.29  ? 2476 HIS A CE1   1 
ATOM   8000  N  NE2   . HIS A 1 2476 ? 139.342 94.232  140.527 1.00 41.79  ? 2476 HIS A NE2   1 
ATOM   8001  N  N     . PRO A 1 2477 ? 137.064 89.083  144.631 1.00 50.38  ? 2477 PRO A N     1 
ATOM   8002  C  CA    . PRO A 1 2477 ? 136.509 88.474  145.851 1.00 53.73  ? 2477 PRO A CA    1 
ATOM   8003  C  C     . PRO A 1 2477 ? 137.095 89.044  147.129 1.00 63.86  ? 2477 PRO A C     1 
ATOM   8004  O  O     . PRO A 1 2477 ? 136.456 88.944  148.184 1.00 65.48  ? 2477 PRO A O     1 
ATOM   8005  C  CB    . PRO A 1 2477 ? 136.853 86.985  145.694 1.00 57.06  ? 2477 PRO A CB    1 
ATOM   8006  C  CG    . PRO A 1 2477 ? 137.187 86.805  144.242 1.00 46.49  ? 2477 PRO A CG    1 
ATOM   8007  C  CD    . PRO A 1 2477 ? 137.790 88.101  143.809 1.00 49.39  ? 2477 PRO A CD    1 
ATOM   8008  N  N     . ASP A 1 2478 ? 138.288 89.637  147.071 1.00 68.10  ? 2478 ASP A N     1 
ATOM   8009  C  CA    . ASP A 1 2478 ? 138.909 90.191  148.269 1.00 69.01  ? 2478 ASP A CA    1 
ATOM   8010  C  C     . ASP A 1 2478 ? 138.308 91.543  148.633 1.00 66.25  ? 2478 ASP A C     1 
ATOM   8011  O  O     . ASP A 1 2478 ? 137.948 91.778  149.792 1.00 67.38  ? 2478 ASP A O     1 
ATOM   8012  C  CB    . ASP A 1 2478 ? 140.420 90.312  148.065 1.00 69.25  ? 2478 ASP A CB    1 
ATOM   8013  C  CG    . ASP A 1 2478 ? 141.084 91.167  149.125 1.00 81.30  ? 2478 ASP A CG    1 
ATOM   8014  O  OD1   . ASP A 1 2478 ? 140.860 90.910  150.327 1.00 86.66  ? 2478 ASP A OD1   1 
ATOM   8015  O  OD2   . ASP A 1 2478 ? 141.830 92.099  148.757 1.00 81.13  ? 2478 ASP A OD2   1 
ATOM   8016  N  N     . PHE A 1 2479 ? 138.185 92.442  147.655 1.00 65.58  ? 2479 PHE A N     1 
ATOM   8017  C  CA    . PHE A 1 2479 ? 137.687 93.800  147.872 1.00 71.04  ? 2479 PHE A CA    1 
ATOM   8018  C  C     . PHE A 1 2479 ? 136.472 94.039  146.985 1.00 64.61  ? 2479 PHE A C     1 
ATOM   8019  O  O     . PHE A 1 2479 ? 136.607 94.502  145.841 1.00 58.03  ? 2479 PHE A O     1 
ATOM   8020  C  CB    . PHE A 1 2479 ? 138.775 94.835  147.592 1.00 71.75  ? 2479 PHE A CB    1 
ATOM   8021  C  CG    . PHE A 1 2479 ? 139.892 94.832  148.596 1.00 77.18  ? 2479 PHE A CG    1 
ATOM   8022  C  CD1   . PHE A 1 2479 ? 139.683 94.373  149.886 1.00 76.50  ? 2479 PHE A CD1   1 
ATOM   8023  C  CD2   . PHE A 1 2479 ? 141.152 95.291  148.251 1.00 75.21  ? 2479 PHE A CD2   1 
ATOM   8024  C  CE1   . PHE A 1 2479 ? 140.709 94.370  150.812 1.00 74.79  ? 2479 PHE A CE1   1 
ATOM   8025  C  CE2   . PHE A 1 2479 ? 142.183 95.291  149.172 1.00 74.29  ? 2479 PHE A CE2   1 
ATOM   8026  C  CZ    . PHE A 1 2479 ? 141.961 94.830  150.454 1.00 76.55  ? 2479 PHE A CZ    1 
ATOM   8027  N  N     . PRO A 1 2480 ? 135.269 93.736  147.465 1.00 61.13  ? 2480 PRO A N     1 
ATOM   8028  C  CA    . PRO A 1 2480 ? 134.064 94.064  146.697 1.00 53.84  ? 2480 PRO A CA    1 
ATOM   8029  C  C     . PRO A 1 2480 ? 133.856 95.568  146.615 1.00 51.13  ? 2480 PRO A C     1 
ATOM   8030  O  O     . PRO A 1 2480 ? 134.359 96.341  147.433 1.00 55.80  ? 2480 PRO A O     1 
ATOM   8031  C  CB    . PRO A 1 2480 ? 132.940 93.387  147.488 1.00 51.20  ? 2480 PRO A CB    1 
ATOM   8032  C  CG    . PRO A 1 2480 ? 133.473 93.278  148.877 1.00 57.24  ? 2480 PRO A CG    1 
ATOM   8033  C  CD    . PRO A 1 2480 ? 134.953 93.061  148.735 1.00 64.93  ? 2480 PRO A CD    1 
ATOM   8034  N  N     . MET A 1 2481 ? 133.110 95.976  145.590 1.00 45.99  ? 2481 MET A N     1 
ATOM   8035  C  CA    . MET A 1 2481 ? 132.855 97.393  145.358 1.00 41.18  ? 2481 MET A CA    1 
ATOM   8036  C  C     . MET A 1 2481 ? 132.175 98.027  146.565 1.00 43.43  ? 2481 MET A C     1 
ATOM   8037  O  O     . MET A 1 2481 ? 131.215 97.478  147.114 1.00 45.07  ? 2481 MET A O     1 
ATOM   8038  C  CB    . MET A 1 2481 ? 131.990 97.574  144.111 1.00 37.96  ? 2481 MET A CB    1 
ATOM   8039  C  CG    . MET A 1 2481 ? 131.768 99.023  143.715 1.00 32.99  ? 2481 MET A CG    1 
ATOM   8040  S  SD    . MET A 1 2481 ? 130.753 99.191  142.236 1.00 45.93  ? 2481 MET A SD    1 
ATOM   8041  C  CE    . MET A 1 2481 ? 131.896 98.630  140.978 1.00 30.59  ? 2481 MET A CE    1 
ATOM   8042  N  N     . GLN A 1 2482 ? 132.678 99.188  146.975 1.00 42.34  ? 2482 GLN A N     1 
ATOM   8043  C  CA    . GLN A 1 2482 ? 132.139 99.906  148.117 1.00 39.00  ? 2482 GLN A CA    1 
ATOM   8044  C  C     . GLN A 1 2482 ? 130.931 100.741 147.696 1.00 43.47  ? 2482 GLN A C     1 
ATOM   8045  O  O     . GLN A 1 2482 ? 130.590 100.844 146.516 1.00 47.12  ? 2482 GLN A O     1 
ATOM   8046  C  CB    . GLN A 1 2482 ? 133.218 100.776 148.759 1.00 44.58  ? 2482 GLN A CB    1 
ATOM   8047  C  CG    . GLN A 1 2482 ? 134.361 99.988  149.377 1.00 46.93  ? 2482 GLN A CG    1 
ATOM   8048  C  CD    . GLN A 1 2482 ? 133.877 98.809  150.201 1.00 43.41  ? 2482 GLN A CD    1 
ATOM   8049  O  OE1   . GLN A 1 2482 ? 133.138 98.976  151.170 1.00 37.24  ? 2482 GLN A OE1   1 
ATOM   8050  N  NE2   . GLN A 1 2482 ? 134.294 97.609  149.817 1.00 42.69  ? 2482 GLN A NE2   1 
ATOM   8051  N  N     . ILE A 1 2483 ? 130.271 101.346 148.686 1.00 47.26  ? 2483 ILE A N     1 
ATOM   8052  C  CA    . ILE A 1 2483 ? 129.047 102.096 148.423 1.00 38.72  ? 2483 ILE A CA    1 
ATOM   8053  C  C     . ILE A 1 2483 ? 129.342 103.356 147.618 1.00 38.27  ? 2483 ILE A C     1 
ATOM   8054  O  O     . ILE A 1 2483 ? 128.548 103.758 146.761 1.00 42.66  ? 2483 ILE A O     1 
ATOM   8055  C  CB    . ILE A 1 2483 ? 128.329 102.419 149.746 1.00 48.77  ? 2483 ILE A CB    1 
ATOM   8056  C  CG1   . ILE A 1 2483 ? 128.263 101.176 150.635 1.00 55.96  ? 2483 ILE A CG1   1 
ATOM   8057  C  CG2   . ILE A 1 2483 ? 126.930 102.948 149.479 1.00 47.20  ? 2483 ILE A CG2   1 
ATOM   8058  C  CD1   . ILE A 1 2483 ? 127.539 100.005 150.000 1.00 57.95  ? 2483 ILE A CD1   1 
ATOM   8059  N  N     . GLU A 1 2484 ? 130.479 104.005 147.882 1.00 38.25  ? 2484 GLU A N     1 
ATOM   8060  C  CA    . GLU A 1 2484 ? 130.813 105.241 147.177 1.00 32.97  ? 2484 GLU A CA    1 
ATOM   8061  C  C     . GLU A 1 2484 ? 131.136 104.969 145.711 1.00 31.69  ? 2484 GLU A C     1 
ATOM   8062  O  O     . GLU A 1 2484 ? 130.657 105.677 144.811 1.00 30.19  ? 2484 GLU A O     1 
ATOM   8063  C  CB    . GLU A 1 2484 ? 131.982 105.930 147.884 1.00 35.61  ? 2484 GLU A CB    1 
ATOM   8064  C  CG    . GLU A 1 2484 ? 132.296 107.340 147.410 1.00 41.86  ? 2484 GLU A CG    1 
ATOM   8065  C  CD    . GLU A 1 2484 ? 133.175 107.367 146.176 1.00 48.79  ? 2484 GLU A CD    1 
ATOM   8066  O  OE1   . GLU A 1 2484 ? 133.971 106.423 145.988 1.00 49.45  ? 2484 GLU A OE1   1 
ATOM   8067  O  OE2   . GLU A 1 2484 ? 133.075 108.338 145.399 1.00 43.95  ? 2484 GLU A OE2   1 
ATOM   8068  N  N     . GLN A 1 2485 ? 131.952 103.945 145.452 1.00 36.64  ? 2485 GLN A N     1 
ATOM   8069  C  CA    . GLN A 1 2485 ? 132.222 103.542 144.077 1.00 32.92  ? 2485 GLN A CA    1 
ATOM   8070  C  C     . GLN A 1 2485 ? 130.941 103.111 143.378 1.00 27.41  ? 2485 GLN A C     1 
ATOM   8071  O  O     . GLN A 1 2485 ? 130.733 103.421 142.199 1.00 25.73  ? 2485 GLN A O     1 
ATOM   8072  C  CB    . GLN A 1 2485 ? 133.254 102.415 144.050 1.00 33.08  ? 2485 GLN A CB    1 
ATOM   8073  C  CG    . GLN A 1 2485 ? 133.669 101.983 142.652 1.00 23.79  ? 2485 GLN A CG    1 
ATOM   8074  C  CD    . GLN A 1 2485 ? 134.734 100.905 142.664 1.00 34.27  ? 2485 GLN A CD    1 
ATOM   8075  O  OE1   . GLN A 1 2485 ? 135.206 100.470 141.614 1.00 34.17  ? 2485 GLN A OE1   1 
ATOM   8076  N  NE2   . GLN A 1 2485 ? 135.121 100.470 143.857 1.00 42.04  ? 2485 GLN A NE2   1 
ATOM   8077  N  N     . LEU A 1 2486 ? 130.070 102.400 144.097 1.00 27.02  ? 2486 LEU A N     1 
ATOM   8078  C  CA    . LEU A 1 2486 ? 128.790 101.997 143.528 1.00 23.79  ? 2486 LEU A CA    1 
ATOM   8079  C  C     . LEU A 1 2486 ? 127.952 103.208 143.141 1.00 19.46  ? 2486 LEU A C     1 
ATOM   8080  O  O     . LEU A 1 2486 ? 127.349 103.229 142.066 1.00 16.76  ? 2486 LEU A O     1 
ATOM   8081  C  CB    . LEU A 1 2486 ? 128.035 101.111 144.517 1.00 24.94  ? 2486 LEU A CB    1 
ATOM   8082  C  CG    . LEU A 1 2486 ? 126.719 100.509 144.025 1.00 24.03  ? 2486 LEU A CG    1 
ATOM   8083  C  CD1   . LEU A 1 2486 ? 126.934 99.743  142.736 1.00 19.70  ? 2486 LEU A CD1   1 
ATOM   8084  C  CD2   . LEU A 1 2486 ? 126.126 99.605  145.087 1.00 23.22  ? 2486 LEU A CD2   1 
ATOM   8085  N  N     . GLU A 1 2487 ? 127.908 104.227 144.000 1.00 19.93  ? 2487 GLU A N     1 
ATOM   8086  C  CA    . GLU A 1 2487 ? 127.131 105.426 143.696 1.00 23.32  ? 2487 GLU A CA    1 
ATOM   8087  C  C     . GLU A 1 2487 ? 127.681 106.141 142.468 1.00 20.48  ? 2487 GLU A C     1 
ATOM   8088  O  O     . GLU A 1 2487 ? 126.923 106.546 141.573 1.00 19.37  ? 2487 GLU A O     1 
ATOM   8089  C  CB    . GLU A 1 2487 ? 127.126 106.361 144.905 1.00 21.76  ? 2487 GLU A CB    1 
ATOM   8090  C  CG    . GLU A 1 2487 ? 126.441 107.694 144.663 1.00 33.74  ? 2487 GLU A CG    1 
ATOM   8091  C  CD    . GLU A 1 2487 ? 126.039 108.385 145.951 1.00 48.69  ? 2487 GLU A CD    1 
ATOM   8092  O  OE1   . GLU A 1 2487 ? 124.956 109.007 145.981 1.00 51.93  ? 2487 GLU A OE1   1 
ATOM   8093  O  OE2   . GLU A 1 2487 ? 126.806 108.306 146.934 1.00 51.70  ? 2487 GLU A OE2   1 
ATOM   8094  N  N     . ARG A 1 2488 ? 129.006 106.308 142.413 1.00 22.18  ? 2488 ARG A N     1 
ATOM   8095  C  CA    . ARG A 1 2488 ? 129.604 107.008 141.279 1.00 22.07  ? 2488 ARG A CA    1 
ATOM   8096  C  C     . ARG A 1 2488 ? 129.402 106.235 139.982 1.00 20.04  ? 2488 ARG A C     1 
ATOM   8097  O  O     . ARG A 1 2488 ? 129.201 106.835 138.921 1.00 18.77  ? 2488 ARG A O     1 
ATOM   8098  C  CB    . ARG A 1 2488 ? 131.088 107.269 141.532 1.00 23.50  ? 2488 ARG A CB    1 
ATOM   8099  C  CG    . ARG A 1 2488 ? 131.362 108.602 142.210 1.00 26.10  ? 2488 ARG A CG    1 
ATOM   8100  C  CD    . ARG A 1 2488 ? 132.850 108.892 142.319 1.00 29.85  ? 2488 ARG A CD    1 
ATOM   8101  N  NE    . ARG A 1 2488 ? 133.586 107.793 142.931 1.00 35.04  ? 2488 ARG A NE    1 
ATOM   8102  C  CZ    . ARG A 1 2488 ? 134.440 107.012 142.283 1.00 32.74  ? 2488 ARG A CZ    1 
ATOM   8103  N  NH1   . ARG A 1 2488 ? 134.688 107.179 140.994 1.00 34.99  ? 2488 ARG A NH1   1 
ATOM   8104  N  NH2   . ARG A 1 2488 ? 135.060 106.039 142.945 1.00 29.88  ? 2488 ARG A NH2   1 
ATOM   8105  N  N     . TYR A 1 2489 ? 129.452 104.902 140.044 1.00 15.80  ? 2489 TYR A N     1 
ATOM   8106  C  CA    . TYR A 1 2489 ? 129.154 104.103 138.861 1.00 12.08  ? 2489 TYR A CA    1 
ATOM   8107  C  C     . TYR A 1 2489 ? 127.692 104.235 138.452 1.00 13.08  ? 2489 TYR A C     1 
ATOM   8108  O  O     . TYR A 1 2489 ? 127.389 104.423 137.267 1.00 13.15  ? 2489 TYR A O     1 
ATOM   8109  C  CB    . TYR A 1 2489 ? 129.502 102.637 139.113 1.00 11.06  ? 2489 TYR A CB    1 
ATOM   8110  C  CG    . TYR A 1 2489 ? 129.230 101.740 137.927 1.00 12.96  ? 2489 TYR A CG    1 
ATOM   8111  C  CD1   . TYR A 1 2489 ? 129.823 101.983 136.696 1.00 10.07  ? 2489 TYR A CD1   1 
ATOM   8112  C  CD2   . TYR A 1 2489 ? 128.365 100.658 138.035 1.00 11.40  ? 2489 TYR A CD2   1 
ATOM   8113  C  CE1   . TYR A 1 2489 ? 129.573 101.168 135.608 1.00 11.48  ? 2489 TYR A CE1   1 
ATOM   8114  C  CE2   . TYR A 1 2489 ? 128.108 99.838  136.952 1.00 10.59  ? 2489 TYR A CE2   1 
ATOM   8115  C  CZ    . TYR A 1 2489 ? 128.714 100.098 135.742 1.00 12.27  ? 2489 TYR A CZ    1 
ATOM   8116  O  OH    . TYR A 1 2489 ? 128.461 99.285  134.662 1.00 18.04  ? 2489 TYR A OH    1 
ATOM   8117  N  N     . ILE A 1 2490 ? 126.776 104.145 139.419 1.00 13.55  ? 2490 ILE A N     1 
ATOM   8118  C  CA    . ILE A 1 2490 ? 125.354 104.055 139.107 1.00 9.97   ? 2490 ILE A CA    1 
ATOM   8119  C  C     . ILE A 1 2490 ? 124.831 105.369 138.541 1.00 9.82   ? 2490 ILE A C     1 
ATOM   8120  O  O     . ILE A 1 2490 ? 124.016 105.367 137.616 1.00 8.03   ? 2490 ILE A O     1 
ATOM   8121  C  CB    . ILE A 1 2490 ? 124.561 103.608 140.350 1.00 11.08  ? 2490 ILE A CB    1 
ATOM   8122  C  CG1   . ILE A 1 2490 ? 124.874 102.149 140.692 1.00 12.35  ? 2490 ILE A CG1   1 
ATOM   8123  C  CG2   . ILE A 1 2490 ? 123.078 103.776 140.129 1.00 9.97   ? 2490 ILE A CG2   1 
ATOM   8124  C  CD1   . ILE A 1 2490 ? 124.557 101.176 139.581 1.00 12.72  ? 2490 ILE A CD1   1 
ATOM   8125  N  N     . GLN A 1 2491 ? 125.279 106.508 139.074 1.00 9.82   ? 2491 GLN A N     1 
ATOM   8126  C  CA    . GLN A 1 2491 ? 124.782 107.786 138.559 1.00 9.88   ? 2491 GLN A CA    1 
ATOM   8127  C  C     . GLN A 1 2491 ? 125.185 107.990 137.098 1.00 11.36  ? 2491 GLN A C     1 
ATOM   8128  O  O     . GLN A 1 2491 ? 124.351 108.328 136.241 1.00 13.84  ? 2491 GLN A O     1 
ATOM   8129  C  CB    . GLN A 1 2491 ? 125.296 108.932 139.429 1.00 16.12  ? 2491 GLN A CB    1 
ATOM   8130  C  CG    . GLN A 1 2491 ? 124.740 108.930 140.842 1.00 19.93  ? 2491 GLN A CG    1 
ATOM   8131  C  CD    . GLN A 1 2491 ? 125.288 110.064 141.685 1.00 27.79  ? 2491 GLN A CD    1 
ATOM   8132  O  OE1   . GLN A 1 2491 ? 126.143 110.828 141.237 1.00 30.90  ? 2491 GLN A OE1   1 
ATOM   8133  N  NE2   . GLN A 1 2491 ? 124.797 110.179 142.912 1.00 28.36  ? 2491 GLN A NE2   1 
ATOM   8134  N  N     . ARG A 1 2492 ? 126.466 107.775 136.797 1.00 11.58  ? 2492 ARG A N     1 
ATOM   8135  C  CA    . ARG A 1 2492 ? 126.947 107.932 135.430 1.00 9.23   ? 2492 ARG A CA    1 
ATOM   8136  C  C     . ARG A 1 2492 ? 126.300 106.916 134.498 1.00 6.97   ? 2492 ARG A C     1 
ATOM   8137  O  O     . ARG A 1 2492 ? 125.944 107.247 133.359 1.00 7.05   ? 2492 ARG A O     1 
ATOM   8138  C  CB    . ARG A 1 2492 ? 128.468 107.808 135.400 1.00 10.65  ? 2492 ARG A CB    1 
ATOM   8139  C  CG    . ARG A 1 2492 ? 129.176 108.759 136.344 1.00 14.27  ? 2492 ARG A CG    1 
ATOM   8140  C  CD    . ARG A 1 2492 ? 130.684 108.659 136.206 1.00 14.68  ? 2492 ARG A CD    1 
ATOM   8141  N  NE    . ARG A 1 2492 ? 131.365 109.012 137.444 1.00 18.18  ? 2492 ARG A NE    1 
ATOM   8142  C  CZ    . ARG A 1 2492 ? 131.734 110.243 137.769 1.00 22.50  ? 2492 ARG A CZ    1 
ATOM   8143  N  NH1   . ARG A 1 2492 ? 131.504 111.267 136.964 1.00 29.07  ? 2492 ARG A NH1   1 
ATOM   8144  N  NH2   . ARG A 1 2492 ? 132.350 110.452 138.929 1.00 21.45  ? 2492 ARG A NH2   1 
ATOM   8145  N  N     . TYR A 1 2493 ? 126.136 105.672 134.958 1.00 5.65   ? 2493 TYR A N     1 
ATOM   8146  C  CA    . TYR A 1 2493 ? 125.476 104.679 134.122 1.00 5.85   ? 2493 TYR A CA    1 
ATOM   8147  C  C     . TYR A 1 2493 ? 124.012 105.026 133.902 1.00 6.17   ? 2493 TYR A C     1 
ATOM   8148  O  O     . TYR A 1 2493 ? 123.465 104.724 132.841 1.00 7.45   ? 2493 TYR A O     1 
ATOM   8149  C  CB    . TYR A 1 2493 ? 125.602 103.284 134.733 1.00 6.52   ? 2493 TYR A CB    1 
ATOM   8150  C  CG    . TYR A 1 2493 ? 125.261 102.176 133.759 1.00 9.13   ? 2493 TYR A CG    1 
ATOM   8151  C  CD1   . TYR A 1 2493 ? 123.941 101.831 133.500 1.00 7.50   ? 2493 TYR A CD1   1 
ATOM   8152  C  CD2   . TYR A 1 2493 ? 126.260 101.476 133.097 1.00 9.16   ? 2493 TYR A CD2   1 
ATOM   8153  C  CE1   . TYR A 1 2493 ? 123.627 100.829 132.610 1.00 6.28   ? 2493 TYR A CE1   1 
ATOM   8154  C  CE2   . TYR A 1 2493 ? 125.954 100.465 132.206 1.00 8.53   ? 2493 TYR A CE2   1 
ATOM   8155  C  CZ    . TYR A 1 2493 ? 124.635 100.145 131.968 1.00 11.32  ? 2493 TYR A CZ    1 
ATOM   8156  O  OH    . TYR A 1 2493 ? 124.321 99.140  131.082 1.00 16.05  ? 2493 TYR A OH    1 
ATOM   8157  N  N     . LEU A 1 2494 ? 123.358 105.643 134.886 1.00 6.53   ? 2494 LEU A N     1 
ATOM   8158  C  CA    . LEU A 1 2494 ? 121.986 106.092 134.689 1.00 5.75   ? 2494 LEU A CA    1 
ATOM   8159  C  C     . LEU A 1 2494 ? 121.916 107.150 133.600 1.00 5.12   ? 2494 LEU A C     1 
ATOM   8160  O  O     . LEU A 1 2494 ? 121.028 107.107 132.741 1.00 5.13   ? 2494 LEU A O     1 
ATOM   8161  C  CB    . LEU A 1 2494 ? 121.416 106.633 135.999 1.00 6.00   ? 2494 LEU A CB    1 
ATOM   8162  C  CG    . LEU A 1 2494 ? 120.105 107.410 135.877 1.00 7.14   ? 2494 LEU A CG    1 
ATOM   8163  C  CD1   . LEU A 1 2494 ? 118.932 106.469 135.644 1.00 6.18   ? 2494 LEU A CD1   1 
ATOM   8164  C  CD2   . LEU A 1 2494 ? 119.879 108.264 137.110 1.00 15.27  ? 2494 LEU A CD2   1 
ATOM   8165  N  N     . VAL A 1 2495 ? 122.852 108.100 133.612 1.00 5.66   ? 2495 VAL A N     1 
ATOM   8166  C  CA    . VAL A 1 2495 ? 122.894 109.103 132.545 1.00 5.50   ? 2495 VAL A CA    1 
ATOM   8167  C  C     . VAL A 1 2495 ? 123.101 108.428 131.190 1.00 6.20   ? 2495 VAL A C     1 
ATOM   8168  O  O     . VAL A 1 2495 ? 122.405 108.723 130.207 1.00 4.76   ? 2495 VAL A O     1 
ATOM   8169  C  CB    . VAL A 1 2495 ? 123.991 110.144 132.831 1.00 6.77   ? 2495 VAL A CB    1 
ATOM   8170  C  CG1   . VAL A 1 2495 ? 124.193 111.051 131.625 1.00 5.77   ? 2495 VAL A CG1   1 
ATOM   8171  C  CG2   . VAL A 1 2495 ? 123.639 110.958 134.065 1.00 7.84   ? 2495 VAL A CG2   1 
ATOM   8172  N  N     . TYR A 1 2496 ? 124.056 107.498 131.130 1.00 5.25   ? 2496 TYR A N     1 
ATOM   8173  C  CA    . TYR A 1 2496 ? 124.377 106.796 129.888 1.00 4.78   ? 2496 TYR A CA    1 
ATOM   8174  C  C     . TYR A 1 2496 ? 123.176 106.006 129.370 1.00 4.41   ? 2496 TYR A C     1 
ATOM   8175  O  O     . TYR A 1 2496 ? 122.854 106.040 128.173 1.00 4.79   ? 2496 TYR A O     1 
ATOM   8176  C  CB    . TYR A 1 2496 ? 125.584 105.889 130.152 1.00 5.21   ? 2496 TYR A CB    1 
ATOM   8177  C  CG    . TYR A 1 2496 ? 125.871 104.802 129.144 1.00 5.64   ? 2496 TYR A CG    1 
ATOM   8178  C  CD1   . TYR A 1 2496 ? 126.640 105.057 128.017 1.00 5.09   ? 2496 TYR A CD1   1 
ATOM   8179  C  CD2   . TYR A 1 2496 ? 125.412 103.507 129.344 1.00 7.00   ? 2496 TYR A CD2   1 
ATOM   8180  C  CE1   . TYR A 1 2496 ? 126.925 104.059 127.108 1.00 7.09   ? 2496 TYR A CE1   1 
ATOM   8181  C  CE2   . TYR A 1 2496 ? 125.689 102.504 128.437 1.00 6.41   ? 2496 TYR A CE2   1 
ATOM   8182  C  CZ    . TYR A 1 2496 ? 126.444 102.786 127.320 1.00 7.40   ? 2496 TYR A CZ    1 
ATOM   8183  O  OH    . TYR A 1 2496 ? 126.720 101.788 126.414 1.00 10.73  ? 2496 TYR A OH    1 
ATOM   8184  N  N     . ALA A 1 2497 ? 122.494 105.298 130.271 1.00 4.09   ? 2497 ALA A N     1 
ATOM   8185  C  CA    . ALA A 1 2497 ? 121.342 104.490 129.896 1.00 4.23   ? 2497 ALA A CA    1 
ATOM   8186  C  C     . ALA A 1 2497 ? 120.172 105.359 129.463 1.00 4.11   ? 2497 ALA A C     1 
ATOM   8187  O  O     . ALA A 1 2497 ? 119.452 105.005 128.526 1.00 3.91   ? 2497 ALA A O     1 
ATOM   8188  C  CB    . ALA A 1 2497 ? 120.941 103.582 131.057 1.00 4.62   ? 2497 ALA A CB    1 
ATOM   8189  N  N     . ILE A 1 2498 ? 119.961 106.494 130.131 1.00 3.63   ? 2498 ILE A N     1 
ATOM   8190  C  CA    . ILE A 1 2498 ? 118.918 107.423 129.705 1.00 4.55   ? 2498 ILE A CA    1 
ATOM   8191  C  C     . ILE A 1 2498 ? 119.199 107.901 128.289 1.00 5.17   ? 2498 ILE A C     1 
ATOM   8192  O  O     . ILE A 1 2498 ? 118.306 107.927 127.430 1.00 5.13   ? 2498 ILE A O     1 
ATOM   8193  C  CB    . ILE A 1 2498 ? 118.819 108.604 130.688 1.00 4.57   ? 2498 ILE A CB    1 
ATOM   8194  C  CG1   . ILE A 1 2498 ? 118.128 108.174 131.981 1.00 4.95   ? 2498 ILE A CG1   1 
ATOM   8195  C  CG2   . ILE A 1 2498 ? 118.075 109.768 130.052 1.00 4.46   ? 2498 ILE A CG2   1 
ATOM   8196  C  CD1   . ILE A 1 2498 ? 118.187 109.222 133.068 1.00 7.07   ? 2498 ILE A CD1   1 
ATOM   8197  N  N     . LEU A 1 2499 ? 120.456 108.262 128.020 1.00 4.25   ? 2499 LEU A N     1 
ATOM   8198  C  CA    . LEU A 1 2499 ? 120.829 108.714 126.684 1.00 5.04   ? 2499 LEU A CA    1 
ATOM   8199  C  C     . LEU A 1 2499 ? 120.532 107.648 125.637 1.00 4.84   ? 2499 LEU A C     1 
ATOM   8200  O  O     . LEU A 1 2499 ? 119.863 107.918 124.632 1.00 4.70   ? 2499 LEU A O     1 
ATOM   8201  C  CB    . LEU A 1 2499 ? 122.308 109.089 126.658 1.00 5.13   ? 2499 LEU A CB    1 
ATOM   8202  C  CG    . LEU A 1 2499 ? 122.643 110.476 127.194 1.00 8.51   ? 2499 LEU A CG    1 
ATOM   8203  C  CD1   . LEU A 1 2499 ? 124.137 110.612 127.361 1.00 10.33  ? 2499 LEU A CD1   1 
ATOM   8204  C  CD2   . LEU A 1 2499 ? 122.110 111.536 126.253 1.00 11.00  ? 2499 LEU A CD2   1 
ATOM   8205  N  N     . TRP A 1 2500 ? 121.007 106.423 125.863 1.00 3.47   ? 2500 TRP A N     1 
ATOM   8206  C  CA    . TRP A 1 2500 ? 120.848 105.391 124.843 1.00 3.48   ? 2500 TRP A CA    1 
ATOM   8207  C  C     . TRP A 1 2500 ? 119.430 104.839 124.755 1.00 4.83   ? 2500 TRP A C     1 
ATOM   8208  O  O     . TRP A 1 2500 ? 119.067 104.274 123.717 1.00 8.46   ? 2500 TRP A O     1 
ATOM   8209  C  CB    . TRP A 1 2500 ? 121.841 104.254 125.073 1.00 4.61   ? 2500 TRP A CB    1 
ATOM   8210  C  CG    . TRP A 1 2500 ? 123.214 104.608 124.609 1.00 5.14   ? 2500 TRP A CG    1 
ATOM   8211  C  CD1   . TRP A 1 2500 ? 124.293 104.897 125.386 1.00 3.94   ? 2500 TRP A CD1   1 
ATOM   8212  C  CD2   . TRP A 1 2500 ? 123.648 104.749 123.250 1.00 5.10   ? 2500 TRP A CD2   1 
ATOM   8213  N  NE1   . TRP A 1 2500 ? 125.379 105.189 124.599 1.00 7.27   ? 2500 TRP A NE1   1 
ATOM   8214  C  CE2   . TRP A 1 2500 ? 125.009 105.107 123.283 1.00 8.42   ? 2500 TRP A CE2   1 
ATOM   8215  C  CE3   . TRP A 1 2500 ? 123.020 104.598 122.011 1.00 4.52   ? 2500 TRP A CE3   1 
ATOM   8216  C  CZ2   . TRP A 1 2500 ? 125.753 105.317 122.124 1.00 7.58   ? 2500 TRP A CZ2   1 
ATOM   8217  C  CZ3   . TRP A 1 2500 ? 123.759 104.811 120.862 1.00 4.71   ? 2500 TRP A CZ3   1 
ATOM   8218  C  CH2   . TRP A 1 2500 ? 125.111 105.164 120.926 1.00 6.97   ? 2500 TRP A CH2   1 
ATOM   8219  N  N     . SER A 1 2501 ? 118.621 104.987 125.802 1.00 5.26   ? 2501 SER A N     1 
ATOM   8220  C  CA    . SER A 1 2501 ? 117.239 104.536 125.763 1.00 4.06   ? 2501 SER A CA    1 
ATOM   8221  C  C     . SER A 1 2501 ? 116.291 105.582 125.200 1.00 5.83   ? 2501 SER A C     1 
ATOM   8222  O  O     . SER A 1 2501 ? 115.205 105.224 124.733 1.00 6.94   ? 2501 SER A O     1 
ATOM   8223  C  CB    . SER A 1 2501 ? 116.772 104.137 127.166 1.00 3.79   ? 2501 SER A CB    1 
ATOM   8224  O  OG    . SER A 1 2501 ? 117.610 103.137 127.717 1.00 4.31   ? 2501 SER A OG    1 
ATOM   8225  N  N     . LEU A 1 2502 ? 116.668 106.861 125.232 1.00 4.90   ? 2502 LEU A N     1 
ATOM   8226  C  CA    . LEU A 1 2502 ? 115.794 107.907 124.728 1.00 4.96   ? 2502 LEU A CA    1 
ATOM   8227  C  C     . LEU A 1 2502 ? 116.236 108.492 123.396 1.00 7.67   ? 2502 LEU A C     1 
ATOM   8228  O  O     . LEU A 1 2502 ? 115.426 109.148 122.734 1.00 11.66  ? 2502 LEU A O     1 
ATOM   8229  C  CB    . LEU A 1 2502 ? 115.675 109.040 125.758 1.00 6.48   ? 2502 LEU A CB    1 
ATOM   8230  C  CG    . LEU A 1 2502 ? 114.622 108.918 126.863 1.00 7.51   ? 2502 LEU A CG    1 
ATOM   8231  C  CD1   . LEU A 1 2502 ? 114.744 107.614 127.636 1.00 4.72   ? 2502 LEU A CD1   1 
ATOM   8232  C  CD2   . LEU A 1 2502 ? 114.750 110.091 127.805 1.00 6.31   ? 2502 LEU A CD2   1 
ATOM   8233  N  N     . SER A 1 2503 ? 117.486 108.271 122.980 1.00 6.60   ? 2503 SER A N     1 
ATOM   8234  C  CA    . SER A 1 2503 ? 117.965 108.780 121.702 1.00 6.90   ? 2503 SER A CA    1 
ATOM   8235  C  C     . SER A 1 2503 ? 118.752 107.742 120.910 1.00 7.53   ? 2503 SER A C     1 
ATOM   8236  O  O     . SER A 1 2503 ? 119.282 108.070 119.843 1.00 9.65   ? 2503 SER A O     1 
ATOM   8237  C  CB    . SER A 1 2503 ? 118.826 110.031 121.907 1.00 8.91   ? 2503 SER A CB    1 
ATOM   8238  O  OG    . SER A 1 2503 ? 120.047 109.703 122.544 1.00 9.57   ? 2503 SER A OG    1 
ATOM   8239  N  N     . GLY A 1 2504 ? 118.845 106.504 121.399 1.00 6.31   ? 2504 GLY A N     1 
ATOM   8240  C  CA    . GLY A 1 2504 ? 119.517 105.461 120.645 1.00 5.79   ? 2504 GLY A CA    1 
ATOM   8241  C  C     . GLY A 1 2504 ? 118.815 105.105 119.353 1.00 5.19   ? 2504 GLY A C     1 
ATOM   8242  O  O     . GLY A 1 2504 ? 119.441 104.544 118.448 1.00 4.76   ? 2504 GLY A O     1 
ATOM   8243  N  N     . ASP A 1 2505 ? 117.527 105.424 119.246 1.00 4.36   ? 2505 ASP A N     1 
ATOM   8244  C  CA    . ASP A 1 2505 ? 116.749 105.224 118.035 1.00 4.67   ? 2505 ASP A CA    1 
ATOM   8245  C  C     . ASP A 1 2505 ? 116.690 106.474 117.164 1.00 7.74   ? 2505 ASP A C     1 
ATOM   8246  O  O     . ASP A 1 2505 ? 115.863 106.546 116.249 1.00 8.86   ? 2505 ASP A O     1 
ATOM   8247  C  CB    . ASP A 1 2505 ? 115.337 104.761 118.397 1.00 5.44   ? 2505 ASP A CB    1 
ATOM   8248  C  CG    . ASP A 1 2505 ? 114.485 105.880 118.964 1.00 10.87  ? 2505 ASP A CG    1 
ATOM   8249  O  OD1   . ASP A 1 2505 ? 115.030 106.730 119.699 1.00 9.98   ? 2505 ASP A OD1   1 
ATOM   8250  O  OD2   . ASP A 1 2505 ? 113.270 105.908 118.678 1.00 12.95  ? 2505 ASP A OD2   1 
ATOM   8251  N  N     . SER A 1 2506 ? 117.545 107.455 117.429 1.00 6.93   ? 2506 SER A N     1 
ATOM   8252  C  CA    . SER A 1 2506 ? 117.565 108.708 116.695 1.00 6.80   ? 2506 SER A CA    1 
ATOM   8253  C  C     . SER A 1 2506 ? 118.954 108.949 116.117 1.00 7.72   ? 2506 SER A C     1 
ATOM   8254  O  O     . SER A 1 2506 ? 119.934 108.297 116.488 1.00 9.31   ? 2506 SER A O     1 
ATOM   8255  C  CB    . SER A 1 2506 ? 117.150 109.881 117.592 1.00 8.45   ? 2506 SER A CB    1 
ATOM   8256  O  OG    . SER A 1 2506 ? 118.186 110.220 118.497 1.00 9.40   ? 2506 SER A OG    1 
ATOM   8257  N  N     . ARG A 1 2507 ? 119.021 109.903 115.194 1.00 8.62   ? 2507 ARG A N     1 
ATOM   8258  C  CA    . ARG A 1 2507 ? 120.270 110.253 114.538 1.00 9.21   ? 2507 ARG A CA    1 
ATOM   8259  C  C     . ARG A 1 2507 ? 121.173 111.043 115.488 1.00 12.42  ? 2507 ARG A C     1 
ATOM   8260  O  O     . ARG A 1 2507 ? 120.792 111.405 116.605 1.00 15.34  ? 2507 ARG A O     1 
ATOM   8261  C  CB    . ARG A 1 2507 ? 119.975 111.005 113.242 1.00 12.43  ? 2507 ARG A CB    1 
ATOM   8262  C  CG    . ARG A 1 2507 ? 119.425 112.413 113.417 1.00 21.06  ? 2507 ARG A CG    1 
ATOM   8263  C  CD    . ARG A 1 2507 ? 119.054 113.011 112.063 1.00 26.08  ? 2507 ARG A CD    1 
ATOM   8264  N  NE    . ARG A 1 2507 ? 118.357 114.287 112.178 1.00 38.74  ? 2507 ARG A NE    1 
ATOM   8265  C  CZ    . ARG A 1 2507 ? 117.040 114.411 112.277 1.00 43.64  ? 2507 ARG A CZ    1 
ATOM   8266  N  NH1   . ARG A 1 2507 ? 116.244 113.353 112.280 1.00 42.20  ? 2507 ARG A NH1   1 
ATOM   8267  N  NH2   . ARG A 1 2507 ? 116.507 115.625 112.370 1.00 42.07  ? 2507 ARG A NH2   1 
ATOM   8268  N  N     . LEU A 1 2508 ? 122.398 111.306 115.022 1.00 14.30  ? 2508 LEU A N     1 
ATOM   8269  C  CA    . LEU A 1 2508 ? 123.452 111.820 115.895 1.00 14.83  ? 2508 LEU A CA    1 
ATOM   8270  C  C     . LEU A 1 2508 ? 123.102 113.184 116.480 1.00 14.82  ? 2508 LEU A C     1 
ATOM   8271  O  O     . LEU A 1 2508 ? 123.372 113.448 117.659 1.00 15.63  ? 2508 LEU A O     1 
ATOM   8272  C  CB    . LEU A 1 2508 ? 124.769 111.893 115.121 1.00 18.96  ? 2508 LEU A CB    1 
ATOM   8273  C  CG    . LEU A 1 2508 ? 125.980 112.491 115.838 1.00 29.77  ? 2508 LEU A CG    1 
ATOM   8274  C  CD1   . LEU A 1 2508 ? 126.582 111.497 116.820 1.00 33.07  ? 2508 LEU A CD1   1 
ATOM   8275  C  CD2   . LEU A 1 2508 ? 127.016 112.954 114.823 1.00 25.52  ? 2508 LEU A CD2   1 
ATOM   8276  N  N     . LYS A 1 2509 ? 122.520 114.072 115.671 1.00 15.96  ? 2509 LYS A N     1 
ATOM   8277  C  CA    . LYS A 1 2509 ? 122.249 115.422 116.154 1.00 19.80  ? 2509 LYS A CA    1 
ATOM   8278  C  C     . LYS A 1 2509 ? 121.226 115.405 117.282 1.00 22.39  ? 2509 LYS A C     1 
ATOM   8279  O  O     . LYS A 1 2509 ? 121.354 116.155 118.255 1.00 24.79  ? 2509 LYS A O     1 
ATOM   8280  C  CB    . LYS A 1 2509 ? 121.779 116.313 115.004 1.00 24.93  ? 2509 LYS A CB    1 
ATOM   8281  C  CG    . LYS A 1 2509 ? 121.514 117.756 115.406 1.00 36.29  ? 2509 LYS A CG    1 
ATOM   8282  C  CD    . LYS A 1 2509 ? 121.193 118.621 114.199 1.00 46.61  ? 2509 LYS A CD    1 
ATOM   8283  C  CE    . LYS A 1 2509 ? 119.821 118.312 113.633 1.00 51.39  ? 2509 LYS A CE    1 
ATOM   8284  N  NZ    . LYS A 1 2509 ? 118.749 118.739 114.573 1.00 53.52  ? 2509 LYS A NZ    1 
ATOM   8285  N  N     . MET A 1 2510 ? 120.213 114.541 117.177 1.00 19.84  ? 2510 MET A N     1 
ATOM   8286  C  CA    . MET A 1 2510 ? 119.256 114.378 118.266 1.00 14.97  ? 2510 MET A CA    1 
ATOM   8287  C  C     . MET A 1 2510 ? 119.935 113.839 119.519 1.00 14.53  ? 2510 MET A C     1 
ATOM   8288  O  O     . MET A 1 2510 ? 119.574 114.212 120.641 1.00 16.58  ? 2510 MET A O     1 
ATOM   8289  C  CB    . MET A 1 2510 ? 118.123 113.448 117.834 1.00 16.11  ? 2510 MET A CB    1 
ATOM   8290  C  CG    . MET A 1 2510 ? 117.392 113.847 116.555 1.00 22.36  ? 2510 MET A CG    1 
ATOM   8291  S  SD    . MET A 1 2510 ? 116.194 115.184 116.749 1.00 37.97  ? 2510 MET A SD    1 
ATOM   8292  C  CE    . MET A 1 2510 ? 117.220 116.646 116.621 1.00 30.96  ? 2510 MET A CE    1 
ATOM   8293  N  N     . ARG A 1 2511 ? 120.900 112.935 119.347 1.00 12.17  ? 2511 ARG A N     1 
ATOM   8294  C  CA    . ARG A 1 2511 ? 121.631 112.418 120.496 1.00 12.56  ? 2511 ARG A CA    1 
ATOM   8295  C  C     . ARG A 1 2511 ? 122.406 113.528 121.192 1.00 16.81  ? 2511 ARG A C     1 
ATOM   8296  O  O     . ARG A 1 2511 ? 122.397 113.626 122.426 1.00 16.82  ? 2511 ARG A O     1 
ATOM   8297  C  CB    . ARG A 1 2511 ? 122.563 111.294 120.049 1.00 10.02  ? 2511 ARG A CB    1 
ATOM   8298  C  CG    . ARG A 1 2511 ? 121.821 110.083 119.516 1.00 9.25   ? 2511 ARG A CG    1 
ATOM   8299  C  CD    . ARG A 1 2511 ? 122.770 109.035 118.984 1.00 11.10  ? 2511 ARG A CD    1 
ATOM   8300  N  NE    . ARG A 1 2511 ? 122.047 107.849 118.546 1.00 8.01   ? 2511 ARG A NE    1 
ATOM   8301  C  CZ    . ARG A 1 2511 ? 122.604 106.814 117.935 1.00 7.02   ? 2511 ARG A CZ    1 
ATOM   8302  N  NH1   . ARG A 1 2511 ? 123.903 106.775 117.689 1.00 6.21   ? 2511 ARG A NH1   1 
ATOM   8303  N  NH2   . ARG A 1 2511 ? 121.838 105.797 117.553 1.00 5.80   ? 2511 ARG A NH2   1 
ATOM   8304  N  N     . ALA A 1 2512 ? 123.060 114.390 120.412 1.00 18.05  ? 2512 ALA A N     1 
ATOM   8305  C  CA    . ALA A 1 2512 ? 123.757 115.533 120.990 1.00 16.19  ? 2512 ALA A CA    1 
ATOM   8306  C  C     . ALA A 1 2512 ? 122.778 116.491 121.663 1.00 16.53  ? 2512 ALA A C     1 
ATOM   8307  O  O     . ALA A 1 2512 ? 123.090 117.079 122.705 1.00 20.02  ? 2512 ALA A O     1 
ATOM   8308  C  CB    . ALA A 1 2512 ? 124.565 116.249 119.910 1.00 16.49  ? 2512 ALA A CB    1 
ATOM   8309  N  N     . GLU A 1 2513 ? 121.589 116.660 121.080 1.00 16.09  ? 2513 GLU A N     1 
ATOM   8310  C  CA    . GLU A 1 2513 ? 120.571 117.526 121.672 1.00 19.31  ? 2513 GLU A CA    1 
ATOM   8311  C  C     . GLU A 1 2513 ? 120.113 117.007 123.032 1.00 20.33  ? 2513 GLU A C     1 
ATOM   8312  O  O     . GLU A 1 2513 ? 120.074 117.764 124.014 1.00 22.95  ? 2513 GLU A O     1 
ATOM   8313  C  CB    . GLU A 1 2513 ? 119.386 117.642 120.709 1.00 19.58  ? 2513 GLU A CB    1 
ATOM   8314  C  CG    . GLU A 1 2513 ? 118.226 118.548 121.146 1.00 29.91  ? 2513 GLU A CG    1 
ATOM   8315  C  CD    . GLU A 1 2513 ? 118.590 120.013 121.252 1.00 48.05  ? 2513 GLU A CD    1 
ATOM   8316  O  OE1   . GLU A 1 2513 ? 119.536 120.441 120.562 1.00 61.29  ? 2513 GLU A OE1   1 
ATOM   8317  O  OE2   . GLU A 1 2513 ? 117.912 120.746 122.003 1.00 49.44  ? 2513 GLU A OE2   1 
ATOM   8318  N  N     . LEU A 1 2514 ? 119.779 115.716 123.108 1.00 15.50  ? 2514 LEU A N     1 
ATOM   8319  C  CA    . LEU A 1 2514 ? 119.392 115.117 124.382 1.00 14.04  ? 2514 LEU A CA    1 
ATOM   8320  C  C     . LEU A 1 2514 ? 120.534 115.186 125.387 1.00 15.80  ? 2514 LEU A C     1 
ATOM   8321  O  O     . LEU A 1 2514 ? 120.309 115.448 126.576 1.00 17.08  ? 2514 LEU A O     1 
ATOM   8322  C  CB    . LEU A 1 2514 ? 118.944 113.667 124.180 1.00 14.47  ? 2514 LEU A CB    1 
ATOM   8323  C  CG    . LEU A 1 2514 ? 118.438 112.956 125.439 1.00 15.01  ? 2514 LEU A CG    1 
ATOM   8324  C  CD1   . LEU A 1 2514 ? 117.250 113.695 126.025 1.00 12.38  ? 2514 LEU A CD1   1 
ATOM   8325  C  CD2   . LEU A 1 2514 ? 118.087 111.508 125.154 1.00 10.11  ? 2514 LEU A CD2   1 
ATOM   8326  N  N     . GLY A 1 2515 ? 121.769 114.954 124.931 1.00 13.18  ? 2515 GLY A N     1 
ATOM   8327  C  CA    . GLY A 1 2515 ? 122.904 115.016 125.841 1.00 13.31  ? 2515 GLY A CA    1 
ATOM   8328  C  C     . GLY A 1 2515 ? 123.126 116.399 126.418 1.00 17.44  ? 2515 GLY A C     1 
ATOM   8329  O  O     . GLY A 1 2515 ? 123.384 116.554 127.615 1.00 18.29  ? 2515 GLY A O     1 
ATOM   8330  N  N     . GLU A 1 2516 ? 123.030 117.429 125.583 1.00 16.68  ? 2516 GLU A N     1 
ATOM   8331  C  CA    . GLU A 1 2516 ? 123.257 118.767 126.116 1.00 22.64  ? 2516 GLU A CA    1 
ATOM   8332  C  C     . GLU A 1 2516 ? 122.105 119.192 127.018 1.00 22.64  ? 2516 GLU A C     1 
ATOM   8333  O  O     . GLU A 1 2516 ? 122.319 119.909 127.997 1.00 22.43  ? 2516 GLU A O     1 
ATOM   8334  C  CB    . GLU A 1 2516 ? 123.490 119.772 124.992 1.00 23.84  ? 2516 GLU A CB    1 
ATOM   8335  C  CG    . GLU A 1 2516 ? 122.349 120.094 124.011 1.00 31.39  ? 2516 GLU A CG    1 
ATOM   8336  C  CD    . GLU A 1 2516 ? 122.824 121.077 122.943 1.00 45.22  ? 2516 GLU A CD    1 
ATOM   8337  O  OE1   . GLU A 1 2516 ? 124.022 121.440 122.991 1.00 47.02  ? 2516 GLU A OE1   1 
ATOM   8338  O  OE2   . GLU A 1 2516 ? 122.026 121.500 122.083 1.00 48.66  ? 2516 GLU A OE2   1 
ATOM   8339  N  N     . TYR A 1 2517 ? 120.875 118.760 126.711 1.00 18.23  ? 2517 TYR A N     1 
ATOM   8340  C  CA    . TYR A 1 2517 ? 119.777 119.030 127.632 1.00 18.74  ? 2517 TYR A CA    1 
ATOM   8341  C  C     . TYR A 1 2517 ? 120.017 118.363 128.984 1.00 18.77  ? 2517 TYR A C     1 
ATOM   8342  O  O     . TYR A 1 2517 ? 119.811 118.979 130.043 1.00 19.29  ? 2517 TYR A O     1 
ATOM   8343  C  CB    . TYR A 1 2517 ? 118.463 118.549 127.024 1.00 17.90  ? 2517 TYR A CB    1 
ATOM   8344  C  CG    . TYR A 1 2517 ? 117.289 118.683 127.951 1.00 22.27  ? 2517 TYR A CG    1 
ATOM   8345  C  CD1   . TYR A 1 2517 ? 116.799 119.934 128.295 1.00 22.07  ? 2517 TYR A CD1   1 
ATOM   8346  C  CD2   . TYR A 1 2517 ? 116.670 117.566 128.482 1.00 27.51  ? 2517 TYR A CD2   1 
ATOM   8347  C  CE1   . TYR A 1 2517 ? 115.723 120.070 129.138 1.00 22.26  ? 2517 TYR A CE1   1 
ATOM   8348  C  CE2   . TYR A 1 2517 ? 115.592 117.690 129.328 1.00 26.66  ? 2517 TYR A CE2   1 
ATOM   8349  C  CZ    . TYR A 1 2517 ? 115.122 118.949 129.652 1.00 23.63  ? 2517 TYR A CZ    1 
ATOM   8350  O  OH    . TYR A 1 2517 ? 114.049 119.113 130.492 1.00 23.96  ? 2517 TYR A OH    1 
ATOM   8351  N  N     . ILE A 1 2518 ? 120.473 117.106 128.966 1.00 17.59  ? 2518 ILE A N     1 
ATOM   8352  C  CA    . ILE A 1 2518 ? 120.773 116.412 130.216 1.00 18.08  ? 2518 ILE A CA    1 
ATOM   8353  C  C     . ILE A 1 2518 ? 121.847 117.165 130.982 1.00 19.21  ? 2518 ILE A C     1 
ATOM   8354  O  O     . ILE A 1 2518 ? 121.714 117.408 132.186 1.00 20.33  ? 2518 ILE A O     1 
ATOM   8355  C  CB    . ILE A 1 2518 ? 121.188 114.954 129.952 1.00 15.48  ? 2518 ILE A CB    1 
ATOM   8356  C  CG1   . ILE A 1 2518 ? 120.002 114.125 129.458 1.00 13.85  ? 2518 ILE A CG1   1 
ATOM   8357  C  CG2   . ILE A 1 2518 ? 121.789 114.327 131.211 1.00 13.59  ? 2518 ILE A CG2   1 
ATOM   8358  C  CD1   . ILE A 1 2518 ? 120.347 112.678 129.166 1.00 13.22  ? 2518 ILE A CD1   1 
ATOM   8359  N  N     . ARG A 1 2519 ? 122.912 117.567 130.286 1.00 19.80  ? 2519 ARG A N     1 
ATOM   8360  C  CA    . ARG A 1 2519 ? 123.968 118.356 130.909 1.00 22.87  ? 2519 ARG A CA    1 
ATOM   8361  C  C     . ARG A 1 2519 ? 123.405 119.600 131.580 1.00 23.75  ? 2519 ARG A C     1 
ATOM   8362  O  O     . ARG A 1 2519 ? 123.824 119.960 132.687 1.00 21.19  ? 2519 ARG A O     1 
ATOM   8363  C  CB    . ARG A 1 2519 ? 125.010 118.745 129.863 1.00 21.72  ? 2519 ARG A CB    1 
ATOM   8364  C  CG    . ARG A 1 2519 ? 126.226 119.458 130.421 1.00 25.52  ? 2519 ARG A CG    1 
ATOM   8365  C  CD    . ARG A 1 2519 ? 127.233 119.752 129.323 1.00 27.65  ? 2519 ARG A CD    1 
ATOM   8366  N  NE    . ARG A 1 2519 ? 127.890 118.547 128.832 1.00 26.64  ? 2519 ARG A NE    1 
ATOM   8367  C  CZ    . ARG A 1 2519 ? 128.897 117.941 129.444 1.00 26.66  ? 2519 ARG A CZ    1 
ATOM   8368  N  NH1   . ARG A 1 2519 ? 129.386 118.394 130.587 1.00 24.46  ? 2519 ARG A NH1   1 
ATOM   8369  N  NH2   . ARG A 1 2519 ? 129.432 116.855 128.894 1.00 29.16  ? 2519 ARG A NH2   1 
ATOM   8370  N  N     . ARG A 1 2520 ? 122.461 120.275 130.921 1.00 24.09  ? 2520 ARG A N     1 
ATOM   8371  C  CA    . ARG A 1 2520 ? 121.853 121.453 131.531 1.00 20.18  ? 2520 ARG A CA    1 
ATOM   8372  C  C     . ARG A 1 2520 ? 121.104 121.101 132.811 1.00 25.59  ? 2520 ARG A C     1 
ATOM   8373  O  O     . ARG A 1 2520 ? 121.220 121.810 133.816 1.00 33.33  ? 2520 ARG A O     1 
ATOM   8374  C  CB    . ARG A 1 2520 ? 120.915 122.156 130.550 1.00 20.31  ? 2520 ARG A CB    1 
ATOM   8375  C  CG    . ARG A 1 2520 ? 121.559 122.590 129.251 1.00 25.36  ? 2520 ARG A CG    1 
ATOM   8376  C  CD    . ARG A 1 2520 ? 120.785 123.739 128.626 1.00 25.87  ? 2520 ARG A CD    1 
ATOM   8377  N  NE    . ARG A 1 2520 ? 119.423 123.370 128.260 1.00 29.45  ? 2520 ARG A NE    1 
ATOM   8378  C  CZ    . ARG A 1 2520 ? 119.067 122.883 127.079 1.00 34.23  ? 2520 ARG A CZ    1 
ATOM   8379  N  NH1   . ARG A 1 2520 ? 119.953 122.686 126.117 1.00 31.64  ? 2520 ARG A NH1   1 
ATOM   8380  N  NH2   . ARG A 1 2520 ? 117.789 122.593 126.856 1.00 37.64  ? 2520 ARG A NH2   1 
ATOM   8381  N  N     . ILE A 1 2521 ? 120.327 120.015 132.802 1.00 22.98  ? 2521 ILE A N     1 
ATOM   8382  C  CA    . ILE A 1 2521 ? 119.445 119.771 133.942 1.00 21.77  ? 2521 ILE A CA    1 
ATOM   8383  C  C     . ILE A 1 2521 ? 119.985 118.784 134.975 1.00 24.88  ? 2521 ILE A C     1 
ATOM   8384  O  O     . ILE A 1 2521 ? 119.413 118.685 136.071 1.00 25.83  ? 2521 ILE A O     1 
ATOM   8385  C  CB    . ILE A 1 2521 ? 118.060 119.281 133.487 1.00 20.81  ? 2521 ILE A CB    1 
ATOM   8386  C  CG1   . ILE A 1 2521 ? 118.158 117.873 132.906 1.00 21.98  ? 2521 ILE A CG1   1 
ATOM   8387  C  CG2   . ILE A 1 2521 ? 117.453 120.249 132.480 1.00 24.96  ? 2521 ILE A CG2   1 
ATOM   8388  C  CD1   . ILE A 1 2521 ? 116.836 117.329 132.451 1.00 22.75  ? 2521 ILE A CD1   1 
ATOM   8389  N  N     . THR A 1 2522 ? 121.056 118.055 134.676 1.00 24.37  ? 2522 THR A N     1 
ATOM   8390  C  CA    . THR A 1 2522 ? 121.498 117.028 135.610 1.00 24.06  ? 2522 THR A CA    1 
ATOM   8391  C  C     . THR A 1 2522 ? 122.493 117.593 136.617 1.00 25.04  ? 2522 THR A C     1 
ATOM   8392  O  O     . THR A 1 2522 ? 123.179 118.588 136.369 1.00 22.93  ? 2522 THR A O     1 
ATOM   8393  C  CB    . THR A 1 2522 ? 122.135 115.838 134.886 1.00 23.55  ? 2522 THR A CB    1 
ATOM   8394  O  OG1   . THR A 1 2522 ? 122.311 114.762 135.814 1.00 21.24  ? 2522 THR A OG1   1 
ATOM   8395  C  CG2   . THR A 1 2522 ? 123.507 116.214 134.342 1.00 23.92  ? 2522 THR A CG2   1 
ATOM   8396  N  N     . THR A 1 2523 ? 122.546 116.945 137.780 1.00 27.29  ? 2523 THR A N     1 
ATOM   8397  C  CA    . THR A 1 2523 ? 123.575 117.200 138.776 1.00 27.35  ? 2523 THR A CA    1 
ATOM   8398  C  C     . THR A 1 2523 ? 124.662 116.135 138.779 1.00 27.90  ? 2523 THR A C     1 
ATOM   8399  O  O     . THR A 1 2523 ? 125.648 116.279 139.510 1.00 29.02  ? 2523 THR A O     1 
ATOM   8400  C  CB    . THR A 1 2523 ? 122.953 117.293 140.176 1.00 33.36  ? 2523 THR A CB    1 
ATOM   8401  O  OG1   . THR A 1 2523 ? 122.323 116.048 140.505 1.00 38.68  ? 2523 THR A OG1   1 
ATOM   8402  C  CG2   . THR A 1 2523 ? 121.918 118.405 140.227 1.00 31.59  ? 2523 THR A CG2   1 
ATOM   8403  N  N     . VAL A 1 2524 ? 124.502 115.079 137.990 1.00 27.32  ? 2524 VAL A N     1 
ATOM   8404  C  CA    . VAL A 1 2524 ? 125.508 114.014 137.908 1.00 27.11  ? 2524 VAL A CA    1 
ATOM   8405  C  C     . VAL A 1 2524 ? 126.771 114.567 137.259 1.00 25.66  ? 2524 VAL A C     1 
ATOM   8406  O  O     . VAL A 1 2524 ? 126.674 115.319 136.272 1.00 20.55  ? 2524 VAL A O     1 
ATOM   8407  C  CB    . VAL A 1 2524 ? 124.954 112.826 137.117 1.00 24.92  ? 2524 VAL A CB    1 
ATOM   8408  C  CG1   . VAL A 1 2524 ? 125.967 111.690 137.061 1.00 21.37  ? 2524 VAL A CG1   1 
ATOM   8409  C  CG2   . VAL A 1 2524 ? 123.645 112.349 137.725 1.00 20.78  ? 2524 VAL A CG2   1 
ATOM   8410  N  N     . PRO A 1 2525 ? 127.960 114.251 137.772 1.00 29.50  ? 2525 PRO A N     1 
ATOM   8411  C  CA    . PRO A 1 2525 ? 129.190 114.695 137.105 1.00 26.70  ? 2525 PRO A CA    1 
ATOM   8412  C  C     . PRO A 1 2525 ? 129.279 114.144 135.689 1.00 25.41  ? 2525 PRO A C     1 
ATOM   8413  O  O     . PRO A 1 2525 ? 128.894 113.004 135.417 1.00 24.72  ? 2525 PRO A O     1 
ATOM   8414  C  CB    . PRO A 1 2525 ? 130.301 114.138 138.001 1.00 23.01  ? 2525 PRO A CB    1 
ATOM   8415  C  CG    . PRO A 1 2525 ? 129.660 113.959 139.334 1.00 28.04  ? 2525 PRO A CG    1 
ATOM   8416  C  CD    . PRO A 1 2525 ? 128.232 113.592 139.061 1.00 26.31  ? 2525 PRO A CD    1 
ATOM   8417  N  N     . LEU A 1 2526 ? 129.794 114.967 134.787 1.00 26.26  ? 2526 LEU A N     1 
ATOM   8418  C  CA    . LEU A 1 2526 ? 129.818 114.698 133.359 1.00 24.85  ? 2526 LEU A CA    1 
ATOM   8419  C  C     . LEU A 1 2526 ? 131.202 114.986 132.804 1.00 32.47  ? 2526 LEU A C     1 
ATOM   8420  O  O     . LEU A 1 2526 ? 131.989 115.710 133.424 1.00 39.63  ? 2526 LEU A O     1 
ATOM   8421  C  CB    . LEU A 1 2526 ? 128.771 115.557 132.634 1.00 20.94  ? 2526 LEU A CB    1 
ATOM   8422  C  CG    . LEU A 1 2526 ? 127.314 115.243 132.969 1.00 18.73  ? 2526 LEU A CG    1 
ATOM   8423  C  CD1   . LEU A 1 2526 ? 126.396 116.050 132.086 1.00 17.74  ? 2526 LEU A CD1   1 
ATOM   8424  C  CD2   . LEU A 1 2526 ? 127.031 113.757 132.816 1.00 18.28  ? 2526 LEU A CD2   1 
ATOM   8425  N  N     . PRO A 1 2527 ? 131.541 114.417 131.645 1.00 35.01  ? 2527 PRO A N     1 
ATOM   8426  C  CA    . PRO A 1 2527 ? 132.839 114.722 131.031 1.00 34.63  ? 2527 PRO A CA    1 
ATOM   8427  C  C     . PRO A 1 2527 ? 132.980 116.210 130.743 1.00 37.80  ? 2527 PRO A C     1 
ATOM   8428  O  O     . PRO A 1 2527 ? 132.021 116.882 130.356 1.00 36.86  ? 2527 PRO A O     1 
ATOM   8429  C  CB    . PRO A 1 2527 ? 132.824 113.896 129.740 1.00 26.53  ? 2527 PRO A CB    1 
ATOM   8430  C  CG    . PRO A 1 2527 ? 131.865 112.794 130.012 1.00 23.44  ? 2527 PRO A CG    1 
ATOM   8431  C  CD    . PRO A 1 2527 ? 130.805 113.390 130.887 1.00 27.42  ? 2527 PRO A CD    1 
ATOM   8432  N  N     . THR A 1 2528 ? 134.195 116.719 130.932 1.00 41.34  ? 2528 THR A N     1 
ATOM   8433  C  CA    . THR A 1 2528 ? 134.482 118.142 130.810 1.00 46.30  ? 2528 THR A CA    1 
ATOM   8434  C  C     . THR A 1 2528 ? 134.986 118.531 129.425 1.00 51.04  ? 2528 THR A C     1 
ATOM   8435  O  O     . THR A 1 2528 ? 135.378 119.685 129.224 1.00 53.48  ? 2528 THR A O     1 
ATOM   8436  C  CB    . THR A 1 2528 ? 135.500 118.566 131.871 1.00 50.63  ? 2528 THR A CB    1 
ATOM   8437  O  OG1   . THR A 1 2528 ? 136.721 117.842 131.680 1.00 55.88  ? 2528 THR A OG1   1 
ATOM   8438  C  CG2   . THR A 1 2528 ? 134.962 118.284 133.266 1.00 41.54  ? 2528 THR A CG2   1 
ATOM   8439  N  N     . ALA A 1 2529 ? 134.996 117.601 128.476 1.00 50.24  ? 2529 ALA A N     1 
ATOM   8440  C  CA    . ALA A 1 2529 ? 135.449 117.924 127.132 1.00 51.43  ? 2529 ALA A CA    1 
ATOM   8441  C  C     . ALA A 1 2529 ? 134.502 118.938 126.493 1.00 55.83  ? 2529 ALA A C     1 
ATOM   8442  O  O     . ALA A 1 2529 ? 133.279 118.830 126.648 1.00 54.90  ? 2529 ALA A O     1 
ATOM   8443  C  CB    . ALA A 1 2529 ? 135.534 116.661 126.276 1.00 52.53  ? 2529 ALA A CB    1 
ATOM   8444  N  N     . PRO A 1 2530 ? 135.027 119.933 125.772 1.00 59.22  ? 2530 PRO A N     1 
ATOM   8445  C  CA    . PRO A 1 2530 ? 134.175 121.032 125.293 1.00 59.83  ? 2530 PRO A CA    1 
ATOM   8446  C  C     . PRO A 1 2530 ? 133.195 120.654 124.191 1.00 58.23  ? 2530 PRO A C     1 
ATOM   8447  O  O     . PRO A 1 2530 ? 132.010 120.992 124.278 1.00 59.34  ? 2530 PRO A O     1 
ATOM   8448  C  CB    . PRO A 1 2530 ? 135.197 122.062 124.795 1.00 59.47  ? 2530 PRO A CB    1 
ATOM   8449  C  CG    . PRO A 1 2530 ? 136.381 121.243 124.400 1.00 58.98  ? 2530 PRO A CG    1 
ATOM   8450  C  CD    . PRO A 1 2530 ? 136.440 120.125 125.403 1.00 57.59  ? 2530 PRO A CD    1 
ATOM   8451  N  N     . ASN A 1 2531 ? 133.662 119.955 123.151 1.00 56.97  ? 2531 ASN A N     1 
ATOM   8452  C  CA    . ASN A 1 2531 ? 132.859 119.757 121.949 1.00 55.59  ? 2531 ASN A CA    1 
ATOM   8453  C  C     . ASN A 1 2531 ? 132.631 118.284 121.624 1.00 50.09  ? 2531 ASN A C     1 
ATOM   8454  O  O     . ASN A 1 2531 ? 132.396 117.944 120.460 1.00 51.41  ? 2531 ASN A O     1 
ATOM   8455  C  CB    . ASN A 1 2531 ? 133.504 120.460 120.752 1.00 57.95  ? 2531 ASN A CB    1 
ATOM   8456  C  CG    . ASN A 1 2531 ? 133.906 121.888 121.063 1.00 70.75  ? 2531 ASN A CG    1 
ATOM   8457  O  OD1   . ASN A 1 2531 ? 135.086 122.236 121.024 1.00 75.29  ? 2531 ASN A OD1   1 
ATOM   8458  N  ND2   . ASN A 1 2531 ? 132.923 122.725 121.374 1.00 67.66  ? 2531 ASN A ND2   1 
ATOM   8459  N  N     . ILE A 1 2532 ? 132.690 117.406 122.616 1.00 45.09  ? 2532 ILE A N     1 
ATOM   8460  C  CA    . ILE A 1 2532 ? 132.455 115.978 122.424 1.00 37.14  ? 2532 ILE A CA    1 
ATOM   8461  C  C     . ILE A 1 2532 ? 131.148 115.614 123.120 1.00 29.12  ? 2532 ILE A C     1 
ATOM   8462  O  O     . ILE A 1 2532 ? 131.015 115.861 124.328 1.00 30.56  ? 2532 ILE A O     1 
ATOM   8463  C  CB    . ILE A 1 2532 ? 133.623 115.129 122.951 1.00 34.67  ? 2532 ILE A CB    1 
ATOM   8464  C  CG1   . ILE A 1 2532 ? 134.908 115.432 122.172 1.00 37.55  ? 2532 ILE A CG1   1 
ATOM   8465  C  CG2   . ILE A 1 2532 ? 133.285 113.651 122.867 1.00 27.90  ? 2532 ILE A CG2   1 
ATOM   8466  C  CD1   . ILE A 1 2532 ? 135.745 116.565 122.727 1.00 48.92  ? 2532 ILE A CD1   1 
ATOM   8467  N  N     . PRO A 1 2533 ? 130.170 115.048 122.412 1.00 23.17  ? 2533 PRO A N     1 
ATOM   8468  C  CA    . PRO A 1 2533 ? 128.892 114.713 123.050 1.00 21.56  ? 2533 PRO A CA    1 
ATOM   8469  C  C     . PRO A 1 2533 ? 129.060 113.652 124.127 1.00 18.81  ? 2533 PRO A C     1 
ATOM   8470  O  O     . PRO A 1 2533 ? 129.984 112.836 124.092 1.00 22.82  ? 2533 PRO A O     1 
ATOM   8471  C  CB    . PRO A 1 2533 ? 128.033 114.195 121.889 1.00 18.94  ? 2533 PRO A CB    1 
ATOM   8472  C  CG    . PRO A 1 2533 ? 128.994 113.856 120.801 1.00 18.07  ? 2533 PRO A CG    1 
ATOM   8473  C  CD    . PRO A 1 2533 ? 130.177 114.749 120.971 1.00 21.52  ? 2533 PRO A CD    1 
ATOM   8474  N  N     . ILE A 1 2534 ? 128.146 113.681 125.101 1.00 17.58  ? 2534 ILE A N     1 
ATOM   8475  C  CA    . ILE A 1 2534 ? 128.180 112.715 126.195 1.00 15.83  ? 2534 ILE A CA    1 
ATOM   8476  C  C     . ILE A 1 2534 ? 127.970 111.303 125.667 1.00 14.42  ? 2534 ILE A C     1 
ATOM   8477  O  O     . ILE A 1 2534 ? 128.473 110.330 126.244 1.00 13.63  ? 2534 ILE A O     1 
ATOM   8478  C  CB    . ILE A 1 2534 ? 127.129 113.091 127.257 1.00 16.53  ? 2534 ILE A CB    1 
ATOM   8479  C  CG1   . ILE A 1 2534 ? 127.410 114.490 127.801 1.00 19.66  ? 2534 ILE A CG1   1 
ATOM   8480  C  CG2   . ILE A 1 2534 ? 127.158 112.110 128.416 1.00 11.38  ? 2534 ILE A CG2   1 
ATOM   8481  C  CD1   . ILE A 1 2534 ? 126.284 115.054 128.631 1.00 22.36  ? 2534 ILE A CD1   1 
ATOM   8482  N  N     . ILE A 1 2535 ? 127.245 111.166 124.554 1.00 12.30  ? 2535 ILE A N     1 
ATOM   8483  C  CA    . ILE A 1 2535 ? 126.998 109.869 123.944 1.00 11.97  ? 2535 ILE A CA    1 
ATOM   8484  C  C     . ILE A 1 2535 ? 128.274 109.203 123.446 1.00 14.18  ? 2535 ILE A C     1 
ATOM   8485  O  O     . ILE A 1 2535 ? 128.258 108.013 123.121 1.00 14.39  ? 2535 ILE A O     1 
ATOM   8486  C  CB    . ILE A 1 2535 ? 125.978 110.021 122.793 1.00 14.62  ? 2535 ILE A CB    1 
ATOM   8487  C  CG1   . ILE A 1 2535 ? 125.237 108.706 122.549 1.00 13.84  ? 2535 ILE A CG1   1 
ATOM   8488  C  CG2   . ILE A 1 2535 ? 126.666 110.496 121.521 1.00 11.94  ? 2535 ILE A CG2   1 
ATOM   8489  C  CD1   . ILE A 1 2535 ? 124.134 108.433 123.539 1.00 8.44   ? 2535 ILE A CD1   1 
ATOM   8490  N  N     . ASP A 1 2536 ? 129.382 109.938 123.389 1.00 13.59  ? 2536 ASP A N     1 
ATOM   8491  C  CA    . ASP A 1 2536 ? 130.668 109.399 122.972 1.00 12.44  ? 2536 ASP A CA    1 
ATOM   8492  C  C     . ASP A 1 2536 ? 131.450 108.788 124.128 1.00 10.85  ? 2536 ASP A C     1 
ATOM   8493  O  O     . ASP A 1 2536 ? 132.621 108.438 123.953 1.00 10.33  ? 2536 ASP A O     1 
ATOM   8494  C  CB    . ASP A 1 2536 ? 131.505 110.494 122.305 1.00 15.40  ? 2536 ASP A CB    1 
ATOM   8495  C  CG    . ASP A 1 2536 ? 131.039 110.809 120.897 1.00 21.26  ? 2536 ASP A CG    1 
ATOM   8496  O  OD1   . ASP A 1 2536 ? 130.073 110.172 120.430 1.00 25.49  ? 2536 ASP A OD1   1 
ATOM   8497  O  OD2   . ASP A 1 2536 ? 131.638 111.699 120.258 1.00 23.86  ? 2536 ASP A OD2   1 
ATOM   8498  N  N     . TYR A 1 2537 ? 130.834 108.657 125.300 1.00 10.61  ? 2537 TYR A N     1 
ATOM   8499  C  CA    . TYR A 1 2537 ? 131.505 108.185 126.501 1.00 9.60   ? 2537 TYR A CA    1 
ATOM   8500  C  C     . TYR A 1 2537 ? 130.798 106.956 127.053 1.00 9.18   ? 2537 TYR A C     1 
ATOM   8501  O  O     . TYR A 1 2537 ? 129.573 106.831 126.965 1.00 10.51  ? 2537 TYR A O     1 
ATOM   8502  C  CB    . TYR A 1 2537 ? 131.533 109.274 127.581 1.00 10.52  ? 2537 TYR A CB    1 
ATOM   8503  C  CG    . TYR A 1 2537 ? 132.559 110.357 127.354 1.00 11.84  ? 2537 TYR A CG    1 
ATOM   8504  C  CD1   . TYR A 1 2537 ? 132.256 111.478 126.594 1.00 12.74  ? 2537 TYR A CD1   1 
ATOM   8505  C  CD2   . TYR A 1 2537 ? 133.824 110.270 127.918 1.00 13.97  ? 2537 TYR A CD2   1 
ATOM   8506  C  CE1   . TYR A 1 2537 ? 133.188 112.475 126.388 1.00 17.36  ? 2537 TYR A CE1   1 
ATOM   8507  C  CE2   . TYR A 1 2537 ? 134.764 111.262 127.718 1.00 13.57  ? 2537 TYR A CE2   1 
ATOM   8508  C  CZ    . TYR A 1 2537 ? 134.440 112.362 126.953 1.00 19.69  ? 2537 TYR A CZ    1 
ATOM   8509  O  OH    . TYR A 1 2537 ? 135.372 113.353 126.752 1.00 29.32  ? 2537 TYR A OH    1 
ATOM   8510  N  N     . GLU A 1 2538 ? 131.581 106.046 127.623 1.00 9.64   ? 2538 GLU A N     1 
ATOM   8511  C  CA    . GLU A 1 2538 ? 131.068 104.949 128.424 1.00 11.37  ? 2538 GLU A CA    1 
ATOM   8512  C  C     . GLU A 1 2538 ? 131.341 105.234 129.896 1.00 10.09  ? 2538 GLU A C     1 
ATOM   8513  O  O     . GLU A 1 2538 ? 132.066 106.169 130.255 1.00 11.17  ? 2538 GLU A O     1 
ATOM   8514  C  CB    . GLU A 1 2538 ? 131.705 103.619 128.019 1.00 10.63  ? 2538 GLU A CB    1 
ATOM   8515  C  CG    . GLU A 1 2538 ? 133.192 103.568 128.306 1.00 15.00  ? 2538 GLU A CG    1 
ATOM   8516  C  CD    . GLU A 1 2538 ? 133.843 102.281 127.859 1.00 26.28  ? 2538 GLU A CD    1 
ATOM   8517  O  OE1   . GLU A 1 2538 ? 133.140 101.419 127.298 1.00 27.34  ? 2538 GLU A OE1   1 
ATOM   8518  O  OE2   . GLU A 1 2538 ? 135.065 102.133 128.070 1.00 32.14  ? 2538 GLU A OE2   1 
ATOM   8519  N  N     . VAL A 1 2539 ? 130.768 104.395 130.753 1.00 8.52   ? 2539 VAL A N     1 
ATOM   8520  C  CA    . VAL A 1 2539 ? 130.990 104.454 132.190 1.00 9.37   ? 2539 VAL A CA    1 
ATOM   8521  C  C     . VAL A 1 2539 ? 131.808 103.231 132.571 1.00 10.44  ? 2539 VAL A C     1 
ATOM   8522  O  O     . VAL A 1 2539 ? 131.318 102.097 132.483 1.00 13.30  ? 2539 VAL A O     1 
ATOM   8523  C  CB    . VAL A 1 2539 ? 129.675 104.504 132.977 1.00 7.52   ? 2539 VAL A CB    1 
ATOM   8524  C  CG1   . VAL A 1 2539 ? 129.954 104.738 134.451 1.00 7.16   ? 2539 VAL A CG1   1 
ATOM   8525  C  CG2   . VAL A 1 2539 ? 128.766 105.588 132.419 1.00 5.57   ? 2539 VAL A CG2   1 
ATOM   8526  N  N     . SER A 1 2540 ? 133.049 103.452 132.991 1.00 12.71  ? 2540 SER A N     1 
ATOM   8527  C  CA    . SER A 1 2540 ? 133.868 102.357 133.480 1.00 15.80  ? 2540 SER A CA    1 
ATOM   8528  C  C     . SER A 1 2540 ? 133.339 101.874 134.826 1.00 15.16  ? 2540 SER A C     1 
ATOM   8529  O  O     . SER A 1 2540 ? 132.669 102.606 135.560 1.00 13.85  ? 2540 SER A O     1 
ATOM   8530  C  CB    . SER A 1 2540 ? 135.329 102.790 133.603 1.00 17.44  ? 2540 SER A CB    1 
ATOM   8531  O  OG    . SER A 1 2540 ? 135.466 103.870 134.509 1.00 25.79  ? 2540 SER A OG    1 
ATOM   8532  N  N     . ILE A 1 2541 ? 133.648 100.615 135.147 1.00 14.90  ? 2541 ILE A N     1 
ATOM   8533  C  CA    . ILE A 1 2541 ? 133.146 100.017 136.378 1.00 15.76  ? 2541 ILE A CA    1 
ATOM   8534  C  C     . ILE A 1 2541 ? 133.675 100.746 137.607 1.00 18.89  ? 2541 ILE A C     1 
ATOM   8535  O  O     . ILE A 1 2541 ? 133.086 100.645 138.688 1.00 21.66  ? 2541 ILE A O     1 
ATOM   8536  C  CB    . ILE A 1 2541 ? 133.494 98.513  136.416 1.00 17.66  ? 2541 ILE A CB    1 
ATOM   8537  C  CG1   . ILE A 1 2541 ? 132.683 97.800  137.500 1.00 21.83  ? 2541 ILE A CG1   1 
ATOM   8538  C  CG2   . ILE A 1 2541 ? 134.983 98.310  136.638 1.00 19.07  ? 2541 ILE A CG2   1 
ATOM   8539  C  CD1   . ILE A 1 2541 ? 131.193 97.785  137.238 1.00 15.11  ? 2541 ILE A CD1   1 
ATOM   8540  N  N     . SER A 1 2542 ? 134.765 101.500 137.464 1.00 20.93  ? 2542 SER A N     1 
ATOM   8541  C  CA    . SER A 1 2542 ? 135.288 102.338 138.535 1.00 22.14  ? 2542 SER A CA    1 
ATOM   8542  C  C     . SER A 1 2542 ? 134.532 103.658 138.677 1.00 21.56  ? 2542 SER A C     1 
ATOM   8543  O  O     . SER A 1 2542 ? 135.008 104.560 139.377 1.00 27.09  ? 2542 SER A O     1 
ATOM   8544  C  CB    . SER A 1 2542 ? 136.777 102.611 138.310 1.00 23.72  ? 2542 SER A CB    1 
ATOM   8545  O  OG    . SER A 1 2542 ? 136.976 103.483 137.211 1.00 23.68  ? 2542 SER A OG    1 
ATOM   8546  N  N     . GLY A 1 2543 ? 133.376 103.786 138.034 1.00 18.85  ? 2543 GLY A N     1 
ATOM   8547  C  CA    . GLY A 1 2543 ? 132.573 104.994 138.131 1.00 17.32  ? 2543 GLY A CA    1 
ATOM   8548  C  C     . GLY A 1 2543 ? 133.205 106.228 137.527 1.00 18.92  ? 2543 GLY A C     1 
ATOM   8549  O  O     . GLY A 1 2543 ? 133.130 107.311 138.122 1.00 20.09  ? 2543 GLY A O     1 
ATOM   8550  N  N     . GLU A 1 2544 ? 133.826 106.093 136.360 1.00 19.20  ? 2544 GLU A N     1 
ATOM   8551  C  CA    . GLU A 1 2544 ? 134.442 107.212 135.666 1.00 17.27  ? 2544 GLU A CA    1 
ATOM   8552  C  C     . GLU A 1 2544 ? 133.956 107.249 134.225 1.00 18.26  ? 2544 GLU A C     1 
ATOM   8553  O  O     . GLU A 1 2544 ? 133.711 106.210 133.605 1.00 16.56  ? 2544 GLU A O     1 
ATOM   8554  C  CB    . GLU A 1 2544 ? 135.976 107.120 135.692 1.00 16.75  ? 2544 GLU A CB    1 
ATOM   8555  C  CG    . GLU A 1 2544 ? 136.584 107.086 137.085 1.00 24.20  ? 2544 GLU A CG    1 
ATOM   8556  C  CD    . GLU A 1 2544 ? 136.158 108.263 137.941 1.00 32.04  ? 2544 GLU A CD    1 
ATOM   8557  O  OE1   . GLU A 1 2544 ? 136.154 109.402 137.429 1.00 28.95  ? 2544 GLU A OE1   1 
ATOM   8558  O  OE2   . GLU A 1 2544 ? 135.831 108.049 139.126 1.00 31.76  ? 2544 GLU A OE2   1 
ATOM   8559  N  N     . TRP A 1 2545 ? 133.820 108.461 133.694 1.00 17.58  ? 2545 TRP A N     1 
ATOM   8560  C  CA    . TRP A 1 2545 ? 133.489 108.639 132.287 1.00 17.78  ? 2545 TRP A CA    1 
ATOM   8561  C  C     . TRP A 1 2545 ? 134.741 108.410 131.451 1.00 18.35  ? 2545 TRP A C     1 
ATOM   8562  O  O     . TRP A 1 2545 ? 135.723 109.148 131.580 1.00 23.68  ? 2545 TRP A O     1 
ATOM   8563  C  CB    . TRP A 1 2545 ? 132.929 110.035 132.033 1.00 15.63  ? 2545 TRP A CB    1 
ATOM   8564  C  CG    . TRP A 1 2545 ? 131.545 110.246 132.558 1.00 16.69  ? 2545 TRP A CG    1 
ATOM   8565  C  CD1   . TRP A 1 2545 ? 131.191 110.935 133.680 1.00 15.88  ? 2545 TRP A CD1   1 
ATOM   8566  C  CD2   . TRP A 1 2545 ? 130.326 109.770 131.978 1.00 15.20  ? 2545 TRP A CD2   1 
ATOM   8567  N  NE1   . TRP A 1 2545 ? 129.827 110.916 133.836 1.00 15.51  ? 2545 TRP A NE1   1 
ATOM   8568  C  CE2   . TRP A 1 2545 ? 129.272 110.206 132.804 1.00 14.99  ? 2545 TRP A CE2   1 
ATOM   8569  C  CE3   . TRP A 1 2545 ? 130.023 109.015 130.841 1.00 13.14  ? 2545 TRP A CE3   1 
ATOM   8570  C  CZ2   . TRP A 1 2545 ? 127.938 109.914 132.529 1.00 11.62  ? 2545 TRP A CZ2   1 
ATOM   8571  C  CZ3   . TRP A 1 2545 ? 128.698 108.725 130.570 1.00 9.61   ? 2545 TRP A CZ3   1 
ATOM   8572  C  CH2   . TRP A 1 2545 ? 127.673 109.174 131.411 1.00 9.45   ? 2545 TRP A CH2   1 
ATOM   8573  N  N     . SER A 1 2546 ? 134.709 107.393 130.595 1.00 14.66  ? 2546 SER A N     1 
ATOM   8574  C  CA    . SER A 1 2546 ? 135.844 107.080 129.749 1.00 15.61  ? 2546 SER A CA    1 
ATOM   8575  C  C     . SER A 1 2546 ? 135.435 107.167 128.285 1.00 13.97  ? 2546 SER A C     1 
ATOM   8576  O  O     . SER A 1 2546 ? 134.404 106.598 127.901 1.00 15.63  ? 2546 SER A O     1 
ATOM   8577  C  CB    . SER A 1 2546 ? 136.399 105.681 130.065 1.00 17.28  ? 2546 SER A CB    1 
ATOM   8578  O  OG    . SER A 1 2546 ? 135.357 104.733 130.195 1.00 18.97  ? 2546 SER A OG    1 
ATOM   8579  N  N     . PRO A 1 2547 ? 136.193 107.874 127.449 1.00 12.89  ? 2547 PRO A N     1 
ATOM   8580  C  CA    . PRO A 1 2547 ? 135.798 108.016 126.044 1.00 10.94  ? 2547 PRO A CA    1 
ATOM   8581  C  C     . PRO A 1 2547 ? 135.742 106.672 125.333 1.00 10.51  ? 2547 PRO A C     1 
ATOM   8582  O  O     . PRO A 1 2547 ? 136.571 105.788 125.559 1.00 12.02  ? 2547 PRO A O     1 
ATOM   8583  C  CB    . PRO A 1 2547 ? 136.888 108.921 125.459 1.00 9.38   ? 2547 PRO A CB    1 
ATOM   8584  C  CG    . PRO A 1 2547 ? 138.054 108.755 126.374 1.00 11.26  ? 2547 PRO A CG    1 
ATOM   8585  C  CD    . PRO A 1 2547 ? 137.472 108.543 127.738 1.00 12.87  ? 2547 PRO A CD    1 
ATOM   8586  N  N     . TRP A 1 2548 ? 134.738 106.527 124.467 1.00 7.89   ? 2548 TRP A N     1 
ATOM   8587  C  CA    . TRP A 1 2548 ? 134.619 105.340 123.633 1.00 8.02   ? 2548 TRP A CA    1 
ATOM   8588  C  C     . TRP A 1 2548 ? 135.777 105.208 122.653 1.00 11.58  ? 2548 TRP A C     1 
ATOM   8589  O  O     . TRP A 1 2548 ? 136.103 104.088 122.244 1.00 10.85  ? 2548 TRP A O     1 
ATOM   8590  C  CB    . TRP A 1 2548 ? 133.292 105.380 122.877 1.00 7.57   ? 2548 TRP A CB    1 
ATOM   8591  C  CG    . TRP A 1 2548 ? 132.142 104.787 123.619 1.00 7.02   ? 2548 TRP A CG    1 
ATOM   8592  C  CD1   . TRP A 1 2548 ? 131.002 105.425 124.008 1.00 6.94   ? 2548 TRP A CD1   1 
ATOM   8593  C  CD2   . TRP A 1 2548 ? 131.991 103.420 124.012 1.00 7.68   ? 2548 TRP A CD2   1 
ATOM   8594  N  NE1   . TRP A 1 2548 ? 130.162 104.546 124.647 1.00 8.07   ? 2548 TRP A NE1   1 
ATOM   8595  C  CE2   . TRP A 1 2548 ? 130.746 103.307 124.659 1.00 8.63   ? 2548 TRP A CE2   1 
ATOM   8596  C  CE3   . TRP A 1 2548 ? 132.794 102.283 123.891 1.00 6.97   ? 2548 TRP A CE3   1 
ATOM   8597  C  CZ2   . TRP A 1 2548 ? 130.286 102.104 125.182 1.00 8.00   ? 2548 TRP A CZ2   1 
ATOM   8598  C  CZ3   . TRP A 1 2548 ? 132.335 101.092 124.407 1.00 9.22   ? 2548 TRP A CZ3   1 
ATOM   8599  C  CH2   . TRP A 1 2548 ? 131.096 101.011 125.049 1.00 9.15   ? 2548 TRP A CH2   1 
ATOM   8600  N  N     . GLN A 1 2549 ? 136.409 106.325 122.281 1.00 13.84  ? 2549 GLN A N     1 
ATOM   8601  C  CA    . GLN A 1 2549 ? 137.545 106.287 121.368 1.00 14.12  ? 2549 GLN A CA    1 
ATOM   8602  C  C     . GLN A 1 2549 ? 138.707 105.479 121.927 1.00 17.09  ? 2549 GLN A C     1 
ATOM   8603  O  O     . GLN A 1 2549 ? 139.544 105.001 121.154 1.00 20.82  ? 2549 GLN A O     1 
ATOM   8604  C  CB    . GLN A 1 2549 ? 138.002 107.712 121.047 1.00 16.94  ? 2549 GLN A CB    1 
ATOM   8605  C  CG    . GLN A 1 2549 ? 138.843 107.834 119.788 1.00 17.05  ? 2549 GLN A CG    1 
ATOM   8606  C  CD    . GLN A 1 2549 ? 138.052 107.543 118.529 1.00 25.22  ? 2549 GLN A CD    1 
ATOM   8607  O  OE1   . GLN A 1 2549 ? 137.060 108.210 118.237 1.00 35.08  ? 2549 GLN A OE1   1 
ATOM   8608  N  NE2   . GLN A 1 2549 ? 138.490 106.543 117.774 1.00 25.62  ? 2549 GLN A NE2   1 
ATOM   8609  N  N     . ALA A 1 2550 ? 138.777 105.313 123.250 1.00 15.95  ? 2550 ALA A N     1 
ATOM   8610  C  CA    . ALA A 1 2550 ? 139.815 104.483 123.846 1.00 12.37  ? 2550 ALA A CA    1 
ATOM   8611  C  C     . ALA A 1 2550 ? 139.666 103.014 123.472 1.00 17.10  ? 2550 ALA A C     1 
ATOM   8612  O  O     . ALA A 1 2550 ? 140.640 102.261 123.575 1.00 24.48  ? 2550 ALA A O     1 
ATOM   8613  C  CB    . ALA A 1 2550 ? 139.805 104.637 125.367 1.00 11.97  ? 2550 ALA A CB    1 
ATOM   8614  N  N     . LYS A 1 2551 ? 138.477 102.589 123.043 1.00 15.63  ? 2551 LYS A N     1 
ATOM   8615  C  CA    . LYS A 1 2551 ? 138.254 101.223 122.584 1.00 15.86  ? 2551 LYS A CA    1 
ATOM   8616  C  C     . LYS A 1 2551 ? 138.163 101.133 121.066 1.00 16.46  ? 2551 LYS A C     1 
ATOM   8617  O  O     . LYS A 1 2551 ? 137.562 100.193 120.538 1.00 19.51  ? 2551 LYS A O     1 
ATOM   8618  C  CB    . LYS A 1 2551 ? 136.997 100.636 123.226 1.00 15.60  ? 2551 LYS A CB    1 
ATOM   8619  C  CG    . LYS A 1 2551 ? 137.124 100.370 124.715 1.00 16.54  ? 2551 LYS A CG    1 
ATOM   8620  C  CD    . LYS A 1 2551 ? 135.917 99.608  125.236 1.00 21.64  ? 2551 LYS A CD    1 
ATOM   8621  C  CE    . LYS A 1 2551 ? 135.994 99.409  126.739 1.00 23.67  ? 2551 LYS A CE    1 
ATOM   8622  N  NZ    . LYS A 1 2551 ? 134.683 98.994  127.308 1.00 24.23  ? 2551 LYS A NZ    1 
ATOM   8623  N  N     . VAL A 1 2552 ? 138.746 102.092 120.354 1.00 17.25  ? 2552 VAL A N     1 
ATOM   8624  C  CA    . VAL A 1 2552 ? 138.748 102.085 118.894 1.00 17.86  ? 2552 VAL A CA    1 
ATOM   8625  C  C     . VAL A 1 2552 ? 140.197 102.197 118.430 1.00 20.48  ? 2552 VAL A C     1 
ATOM   8626  O  O     . VAL A 1 2552 ? 140.656 103.292 118.075 1.00 22.93  ? 2552 VAL A O     1 
ATOM   8627  C  CB    . VAL A 1 2552 ? 137.874 103.217 118.327 1.00 15.24  ? 2552 VAL A CB    1 
ATOM   8628  C  CG1   . VAL A 1 2552 ? 137.896 103.209 116.804 1.00 10.09  ? 2552 VAL A CG1   1 
ATOM   8629  C  CG2   . VAL A 1 2552 ? 136.448 103.100 118.841 1.00 13.60  ? 2552 VAL A CG2   1 
ATOM   8630  N  N     . PRO A 1 2553 ? 140.960 101.108 118.451 1.00 22.67  ? 2553 PRO A N     1 
ATOM   8631  C  CA    . PRO A 1 2553 ? 142.343 101.167 117.976 1.00 28.20  ? 2553 PRO A CA    1 
ATOM   8632  C  C     . PRO A 1 2553 ? 142.428 101.087 116.461 1.00 32.82  ? 2553 PRO A C     1 
ATOM   8633  O  O     . PRO A 1 2553 ? 141.576 100.498 115.792 1.00 31.60  ? 2553 PRO A O     1 
ATOM   8634  C  CB    . PRO A 1 2553 ? 142.984 99.936  118.626 1.00 27.39  ? 2553 PRO A CB    1 
ATOM   8635  C  CG    . PRO A 1 2553 ? 141.858 98.962  118.707 1.00 25.09  ? 2553 PRO A CG    1 
ATOM   8636  C  CD    . PRO A 1 2553 ? 140.624 99.782  119.001 1.00 23.78  ? 2553 PRO A CD    1 
ATOM   8637  N  N     . GLN A 1 2554 ? 143.480 101.699 115.921 1.00 32.57  ? 2554 GLN A N     1 
ATOM   8638  C  CA    . GLN A 1 2554 ? 143.779 101.601 114.494 1.00 28.49  ? 2554 GLN A CA    1 
ATOM   8639  C  C     . GLN A 1 2554 ? 144.383 100.227 114.239 1.00 31.23  ? 2554 GLN A C     1 
ATOM   8640  O  O     . GLN A 1 2554 ? 145.583 100.008 114.405 1.00 33.85  ? 2554 GLN A O     1 
ATOM   8641  C  CB    . GLN A 1 2554 ? 144.723 102.714 114.056 1.00 31.59  ? 2554 GLN A CB    1 
ATOM   8642  C  CG    . GLN A 1 2554 ? 145.005 102.721 112.562 1.00 38.31  ? 2554 GLN A CG    1 
ATOM   8643  C  CD    . GLN A 1 2554 ? 145.899 103.869 112.139 1.00 48.83  ? 2554 GLN A CD    1 
ATOM   8644  O  OE1   . GLN A 1 2554 ? 146.352 104.657 112.969 1.00 48.62  ? 2554 GLN A OE1   1 
ATOM   8645  N  NE2   . GLN A 1 2554 ? 146.162 103.966 110.841 1.00 39.38  ? 2554 GLN A NE2   1 
ATOM   8646  N  N     . ILE A 1 2555 ? 143.536 99.286  113.831 1.00 27.32  ? 2555 ILE A N     1 
ATOM   8647  C  CA    . ILE A 1 2555 ? 143.999 97.928  113.585 1.00 26.64  ? 2555 ILE A CA    1 
ATOM   8648  C  C     . ILE A 1 2555 ? 144.636 97.840  112.202 1.00 29.51  ? 2555 ILE A C     1 
ATOM   8649  O  O     . ILE A 1 2555 ? 144.349 98.629  111.297 1.00 28.36  ? 2555 ILE A O     1 
ATOM   8650  C  CB    . ILE A 1 2555 ? 142.852 96.912  113.727 1.00 31.06  ? 2555 ILE A CB    1 
ATOM   8651  C  CG1   . ILE A 1 2555 ? 141.793 97.153  112.650 1.00 22.68  ? 2555 ILE A CG1   1 
ATOM   8652  C  CG2   . ILE A 1 2555 ? 142.231 97.000  115.112 1.00 22.63  ? 2555 ILE A CG2   1 
ATOM   8653  C  CD1   . ILE A 1 2555 ? 140.780 96.039  112.535 1.00 17.06  ? 2555 ILE A CD1   1 
ATOM   8654  N  N     . GLU A 1 2556 ? 145.523 96.862  112.045 1.00 23.67  ? 2556 GLU A N     1 
ATOM   8655  C  CA    . GLU A 1 2556 ? 146.050 96.475  110.743 1.00 22.15  ? 2556 GLU A CA    1 
ATOM   8656  C  C     . GLU A 1 2556 ? 145.513 95.089  110.425 1.00 25.45  ? 2556 GLU A C     1 
ATOM   8657  O  O     . GLU A 1 2556 ? 145.748 94.140  111.181 1.00 33.86  ? 2556 GLU A O     1 
ATOM   8658  C  CB    . GLU A 1 2556 ? 147.579 96.491  110.730 1.00 18.40  ? 2556 GLU A CB    1 
ATOM   8659  C  CG    . GLU A 1 2556 ? 148.180 97.848  111.045 1.00 24.83  ? 2556 GLU A CG    1 
ATOM   8660  C  CD    . GLU A 1 2556 ? 147.710 98.927  110.088 1.00 31.02  ? 2556 GLU A CD    1 
ATOM   8661  O  OE1   . GLU A 1 2556 ? 147.862 98.746  108.862 1.00 35.74  ? 2556 GLU A OE1   1 
ATOM   8662  O  OE2   . GLU A 1 2556 ? 147.187 99.958  110.563 1.00 36.89  ? 2556 GLU A OE2   1 
ATOM   8663  N  N     . VAL A 1 2557 ? 144.799 94.976  109.316 1.00 22.49  ? 2557 VAL A N     1 
ATOM   8664  C  CA    . VAL A 1 2557 ? 144.085 93.749  108.992 1.00 22.10  ? 2557 VAL A CA    1 
ATOM   8665  C  C     . VAL A 1 2557 ? 145.020 92.790  108.269 1.00 25.78  ? 2557 VAL A C     1 
ATOM   8666  O  O     . VAL A 1 2557 ? 145.791 93.187  107.388 1.00 25.36  ? 2557 VAL A O     1 
ATOM   8667  C  CB    . VAL A 1 2557 ? 142.832 94.065  108.154 1.00 24.10  ? 2557 VAL A CB    1 
ATOM   8668  C  CG1   . VAL A 1 2557 ? 142.269 92.807  107.518 1.00 22.07  ? 2557 VAL A CG1   1 
ATOM   8669  C  CG2   . VAL A 1 2557 ? 141.778 94.733  109.021 1.00 19.78  ? 2557 VAL A CG2   1 
ATOM   8670  N  N     . GLU A 1 2558 ? 144.979 91.524  108.674 1.00 29.47  ? 2558 GLU A N     1 
ATOM   8671  C  CA    . GLU A 1 2558 ? 145.694 90.474  107.963 1.00 32.43  ? 2558 GLU A CA    1 
ATOM   8672  C  C     . GLU A 1 2558 ? 145.246 90.401  106.506 1.00 33.50  ? 2558 GLU A C     1 
ATOM   8673  O  O     . GLU A 1 2558 ? 144.060 90.534  106.190 1.00 30.32  ? 2558 GLU A O     1 
ATOM   8674  C  CB    . GLU A 1 2558 ? 145.485 89.142  108.685 1.00 32.57  ? 2558 GLU A CB    1 
ATOM   8675  C  CG    . GLU A 1 2558 ? 144.066 88.608  108.610 1.00 44.21  ? 2558 GLU A CG    1 
ATOM   8676  C  CD    . GLU A 1 2558 ? 143.180 89.206  109.694 1.00 47.35  ? 2558 GLU A CD    1 
ATOM   8677  O  OE1   . GLU A 1 2558 ? 143.575 90.230  110.291 1.00 43.10  ? 2558 GLU A OE1   1 
ATOM   8678  O  OE2   . GLU A 1 2558 ? 142.089 88.661  109.953 1.00 46.63  ? 2558 GLU A OE2   1 
ATOM   8679  N  N     . THR A 1 2559 ? 146.218 90.202  105.613 1.00 37.34  ? 2559 THR A N     1 
ATOM   8680  C  CA    . THR A 1 2559 ? 145.991 90.399  104.185 1.00 32.12  ? 2559 THR A CA    1 
ATOM   8681  C  C     . THR A 1 2559 ? 145.025 89.387  103.579 1.00 32.20  ? 2559 THR A C     1 
ATOM   8682  O  O     . THR A 1 2559 ? 144.455 89.660  102.518 1.00 32.72  ? 2559 THR A O     1 
ATOM   8683  C  CB    . THR A 1 2559 ? 147.324 90.355  103.432 1.00 33.36  ? 2559 THR A CB    1 
ATOM   8684  O  OG1   . THR A 1 2559 ? 147.115 90.708  102.059 1.00 27.11  ? 2559 THR A OG1   1 
ATOM   8685  C  CG2   . THR A 1 2559 ? 147.940 88.967  103.507 1.00 37.13  ? 2559 THR A CG2   1 
ATOM   8686  N  N     . HIS A 1 2560 ? 144.824 88.233  104.211 1.00 34.40  ? 2560 HIS A N     1 
ATOM   8687  C  CA    . HIS A 1 2560 ? 144.006 87.192  103.602 1.00 33.36  ? 2560 HIS A CA    1 
ATOM   8688  C  C     . HIS A 1 2560 ? 142.528 87.279  103.970 1.00 37.76  ? 2560 HIS A C     1 
ATOM   8689  O  O     . HIS A 1 2560 ? 141.709 86.620  103.320 1.00 44.81  ? 2560 HIS A O     1 
ATOM   8690  C  CB    . HIS A 1 2560 ? 144.562 85.809  103.960 1.00 40.04  ? 2560 HIS A CB    1 
ATOM   8691  C  CG    . HIS A 1 2560 ? 144.283 85.384  105.367 1.00 48.41  ? 2560 HIS A CG    1 
ATOM   8692  N  ND1   . HIS A 1 2560 ? 145.073 85.767  106.429 1.00 54.36  ? 2560 HIS A ND1   1 
ATOM   8693  C  CD2   . HIS A 1 2560 ? 143.319 84.586  105.883 1.00 49.23  ? 2560 HIS A CD2   1 
ATOM   8694  C  CE1   . HIS A 1 2560 ? 144.598 85.236  107.541 1.00 49.40  ? 2560 HIS A CE1   1 
ATOM   8695  N  NE2   . HIS A 1 2560 ? 143.535 84.514  107.237 1.00 45.79  ? 2560 HIS A NE2   1 
ATOM   8696  N  N     . LYS A 1 2561 ? 142.160 88.067  104.982 1.00 36.21  ? 2561 LYS A N     1 
ATOM   8697  C  CA    . LYS A 1 2561 ? 140.760 88.357  105.269 1.00 37.03  ? 2561 LYS A CA    1 
ATOM   8698  C  C     . LYS A 1 2561 ? 140.403 89.816  105.004 1.00 32.02  ? 2561 LYS A C     1 
ATOM   8699  O  O     . LYS A 1 2561 ? 139.654 90.418  105.780 1.00 30.90  ? 2561 LYS A O     1 
ATOM   8700  C  CB    . LYS A 1 2561 ? 140.398 87.977  106.707 1.00 40.08  ? 2561 LYS A CB    1 
ATOM   8701  C  CG    . LYS A 1 2561 ? 140.895 86.614  107.157 1.00 46.56  ? 2561 LYS A CG    1 
ATOM   8702  C  CD    . LYS A 1 2561 ? 140.550 86.367  108.618 1.00 45.16  ? 2561 LYS A CD    1 
ATOM   8703  C  CE    . LYS A 1 2561 ? 140.880 84.948  109.045 1.00 60.95  ? 2561 LYS A CE    1 
ATOM   8704  N  NZ    . LYS A 1 2561 ? 140.109 83.941  108.265 1.00 66.67  ? 2561 LYS A NZ    1 
ATOM   8705  N  N     . VAL A 1 2562 ? 140.929 90.397  103.927 1.00 31.73  ? 2562 VAL A N     1 
ATOM   8706  C  CA    . VAL A 1 2562 ? 140.610 91.776  103.575 1.00 27.01  ? 2562 VAL A CA    1 
ATOM   8707  C  C     . VAL A 1 2562 ? 139.165 91.847  103.100 1.00 26.15  ? 2562 VAL A C     1 
ATOM   8708  O  O     . VAL A 1 2562 ? 138.770 91.142  102.164 1.00 31.79  ? 2562 VAL A O     1 
ATOM   8709  C  CB    . VAL A 1 2562 ? 141.572 92.302  102.503 1.00 21.97  ? 2562 VAL A CB    1 
ATOM   8710  C  CG1   . VAL A 1 2562 ? 141.087 93.632  101.968 1.00 19.88  ? 2562 VAL A CG1   1 
ATOM   8711  C  CG2   . VAL A 1 2562 ? 142.971 92.437  103.069 1.00 23.76  ? 2562 VAL A CG2   1 
ATOM   8712  N  N     . ALA A 1 2563 ? 138.372 92.706  103.745 1.00 22.90  ? 2563 ALA A N     1 
ATOM   8713  C  CA    . ALA A 1 2563 ? 136.953 92.885  103.428 1.00 20.02  ? 2563 ALA A CA    1 
ATOM   8714  C  C     . ALA A 1 2563 ? 136.180 91.573  103.529 1.00 27.87  ? 2563 ALA A C     1 
ATOM   8715  O  O     . ALA A 1 2563 ? 135.229 91.340  102.777 1.00 27.93  ? 2563 ALA A O     1 
ATOM   8716  C  CB    . ALA A 1 2563 ? 136.762 93.515  102.045 1.00 13.82  ? 2563 ALA A CB    1 
ATOM   8717  N  N     . ALA A 1 2564 ? 136.583 90.709  104.455 1.00 28.68  ? 2564 ALA A N     1 
ATOM   8718  C  CA    . ALA A 1 2564 ? 135.873 89.461  104.668 1.00 28.40  ? 2564 ALA A CA    1 
ATOM   8719  C  C     . ALA A 1 2564 ? 134.517 89.735  105.318 1.00 32.30  ? 2564 ALA A C     1 
ATOM   8720  O  O     . ALA A 1 2564 ? 134.337 90.752  105.992 1.00 28.54  ? 2564 ALA A O     1 
ATOM   8721  C  CB    . ALA A 1 2564 ? 136.697 88.521  105.544 1.00 28.77  ? 2564 ALA A CB    1 
ATOM   8722  N  N     . PRO A 1 2565 ? 133.540 88.845  105.121 1.00 36.71  ? 2565 PRO A N     1 
ATOM   8723  C  CA    . PRO A 1 2565 ? 132.206 89.083  105.699 1.00 36.00  ? 2565 PRO A CA    1 
ATOM   8724  C  C     . PRO A 1 2565 ? 132.187 89.120  107.218 1.00 37.48  ? 2565 PRO A C     1 
ATOM   8725  O  O     . PRO A 1 2565 ? 131.224 89.640  107.794 1.00 37.62  ? 2565 PRO A O     1 
ATOM   8726  C  CB    . PRO A 1 2565 ? 131.377 87.909  105.157 1.00 25.61  ? 2565 PRO A CB    1 
ATOM   8727  C  CG    . PRO A 1 2565 ? 132.391 86.861  104.814 1.00 26.22  ? 2565 PRO A CG    1 
ATOM   8728  C  CD    . PRO A 1 2565 ? 133.558 87.632  104.287 1.00 31.19  ? 2565 PRO A CD    1 
ATOM   8729  N  N     . ASP A 1 2566 ? 133.243 88.601  107.851 1.00 33.69  ? 2566 ASP A N     1 
ATOM   8730  C  CA    . ASP A 1 2566 ? 133.285 88.528  109.337 1.00 34.21  ? 2566 ASP A CA    1 
ATOM   8731  C  C     . ASP A 1 2566 ? 134.117 89.684  109.899 1.00 29.19  ? 2566 ASP A C     1 
ATOM   8732  O  O     . ASP A 1 2566 ? 133.855 90.091  111.051 1.00 27.64  ? 2566 ASP A O     1 
ATOM   8733  C  CB    . ASP A 1 2566 ? 133.842 87.189  109.794 1.00 38.32  ? 2566 ASP A CB    1 
ATOM   8734  C  CG    . ASP A 1 2566 ? 133.805 86.942  111.294 1.00 41.67  ? 2566 ASP A CG    1 
ATOM   8735  O  OD1   . ASP A 1 2566 ? 132.689 86.872  111.845 1.00 42.47  ? 2566 ASP A OD1   1 
ATOM   8736  O  OD2   . ASP A 1 2566 ? 134.891 86.832  111.898 1.00 42.11  ? 2566 ASP A OD2   1 
ATOM   8737  N  N     . VAL A 1 2567 ? 135.081 90.189  109.125 1.00 25.74  ? 2567 VAL A N     1 
ATOM   8738  C  CA    . VAL A 1 2567 ? 135.998 91.254  109.636 1.00 19.94  ? 2567 VAL A CA    1 
ATOM   8739  C  C     . VAL A 1 2567 ? 135.210 92.550  109.883 1.00 19.59  ? 2567 VAL A C     1 
ATOM   8740  O  O     . VAL A 1 2567 ? 134.403 92.927  109.006 1.00 22.89  ? 2567 VAL A O     1 
ATOM   8741  C  CB    . VAL A 1 2567 ? 137.168 91.486  108.661 1.00 19.07  ? 2567 VAL A CB    1 
ATOM   8742  C  CG1   . VAL A 1 2567 ? 138.050 92.649  109.099 1.00 18.05  ? 2567 VAL A CG1   1 
ATOM   8743  C  CG2   . VAL A 1 2567 ? 137.999 90.223  108.469 1.00 28.55  ? 2567 VAL A CG2   1 
ATOM   8744  N  N     . VAL A 1 2568 ? 135.441 93.201  111.027 1.00 13.43  ? 2568 VAL A N     1 
ATOM   8745  C  CA    . VAL A 1 2568 ? 134.773 94.503  111.333 1.00 9.88   ? 2568 VAL A CA    1 
ATOM   8746  C  C     . VAL A 1 2568 ? 135.854 95.498  111.786 1.00 9.63   ? 2568 VAL A C     1 
ATOM   8747  O  O     . VAL A 1 2568 ? 136.583 95.178  112.748 1.00 11.71  ? 2568 VAL A O     1 
ATOM   8748  C  CB    . VAL A 1 2568 ? 133.679 94.353  112.407 1.00 11.81  ? 2568 VAL A CB    1 
ATOM   8749  C  CG1   . VAL A 1 2568 ? 132.983 95.678  112.691 1.00 7.09   ? 2568 VAL A CG1   1 
ATOM   8750  C  CG2   . VAL A 1 2568 ? 132.667 93.272  112.044 1.00 13.43  ? 2568 VAL A CG2   1 
ATOM   8751  N  N     . VAL A 1 2569 ? 135.950 96.651  111.119 1.00 7.47   ? 2569 VAL A N     1 
ATOM   8752  C  CA    . VAL A 1 2569 ? 136.942 97.692  111.522 1.00 6.89   ? 2569 VAL A CA    1 
ATOM   8753  C  C     . VAL A 1 2569 ? 136.361 98.473  112.712 1.00 7.75   ? 2569 VAL A C     1 
ATOM   8754  O  O     . VAL A 1 2569 ? 135.270 99.061  112.562 1.00 8.34   ? 2569 VAL A O     1 
ATOM   8755  C  CB    . VAL A 1 2569 ? 137.320 98.633  110.361 1.00 6.32   ? 2569 VAL A CB    1 
ATOM   8756  C  CG1   . VAL A 1 2569 ? 138.252 99.747  110.820 1.00 5.83   ? 2569 VAL A CG1   1 
ATOM   8757  C  CG2   . VAL A 1 2569 ? 137.935 97.872  109.194 1.00 4.90   ? 2569 VAL A CG2   1 
ATOM   8758  N  N     . PRO A 1 2570 ? 137.035 98.496  113.882 1.00 10.23  ? 2570 PRO A N     1 
ATOM   8759  C  CA    . PRO A 1 2570 ? 136.495 99.172  115.053 1.00 7.64   ? 2570 PRO A CA    1 
ATOM   8760  C  C     . PRO A 1 2570 ? 136.235 100.647 114.790 1.00 7.92   ? 2570 PRO A C     1 
ATOM   8761  O  O     . PRO A 1 2570 ? 137.132 101.331 114.258 1.00 7.88   ? 2570 PRO A O     1 
ATOM   8762  C  CB    . PRO A 1 2570 ? 137.588 98.960  116.115 1.00 8.70   ? 2570 PRO A CB    1 
ATOM   8763  C  CG    . PRO A 1 2570 ? 138.346 97.746  115.629 1.00 10.71  ? 2570 PRO A CG    1 
ATOM   8764  C  CD    . PRO A 1 2570 ? 138.317 97.858  114.116 1.00 8.72   ? 2570 PRO A CD    1 
ATOM   8765  N  N     . THR A 1 2571 ? 135.039 101.126 115.145 1.00 7.33   ? 2571 THR A N     1 
ATOM   8766  C  CA    . THR A 1 2571 ? 134.709 102.561 114.992 1.00 7.00   ? 2571 THR A CA    1 
ATOM   8767  C  C     . THR A 1 2571 ? 133.931 103.001 116.212 1.00 8.69   ? 2571 THR A C     1 
ATOM   8768  O  O     . THR A 1 2571 ? 133.415 102.118 116.933 1.00 10.90  ? 2571 THR A O     1 
ATOM   8769  C  CB    . THR A 1 2571 ? 133.913 102.802 113.709 1.00 11.19  ? 2571 THR A CB    1 
ATOM   8770  O  OG1   . THR A 1 2571 ? 132.674 102.124 113.894 1.00 11.43  ? 2571 THR A OG1   1 
ATOM   8771  C  CG2   . THR A 1 2571 ? 134.621 102.276 112.474 1.00 9.41   ? 2571 THR A CG2   1 
ATOM   8772  N  N     . LEU A 1 2572 ? 133.833 104.313 116.437 1.00 9.29   ? 2572 LEU A N     1 
ATOM   8773  C  CA    . LEU A 1 2572 ? 133.050 104.837 117.584 1.00 10.06  ? 2572 LEU A CA    1 
ATOM   8774  C  C     . LEU A 1 2572 ? 131.636 104.237 117.533 1.00 9.59   ? 2572 LEU A C     1 
ATOM   8775  O  O     . LEU A 1 2572 ? 131.171 103.722 118.572 1.00 8.79   ? 2572 LEU A O     1 
ATOM   8776  C  CB    . LEU A 1 2572 ? 133.018 106.363 117.523 1.00 12.35  ? 2572 LEU A CB    1 
ATOM   8777  C  CG    . LEU A 1 2572 ? 132.101 107.058 118.534 1.00 21.21  ? 2572 LEU A CG    1 
ATOM   8778  C  CD1   . LEU A 1 2572 ? 132.579 106.822 119.954 1.00 15.07  ? 2572 LEU A CD1   1 
ATOM   8779  C  CD2   . LEU A 1 2572 ? 132.001 108.545 118.243 1.00 24.87  ? 2572 LEU A CD2   1 
ATOM   8780  N  N     . ASP A 1 2573 ? 130.997 104.278 116.362 1.00 10.27  ? 2573 ASP A N     1 
ATOM   8781  C  CA    . ASP A 1 2573 ? 129.621 103.728 116.214 1.00 11.35  ? 2573 ASP A CA    1 
ATOM   8782  C  C     . ASP A 1 2573 ? 129.645 102.222 116.486 1.00 7.73   ? 2573 ASP A C     1 
ATOM   8783  O  O     . ASP A 1 2573 ? 128.762 101.743 117.228 1.00 5.79   ? 2573 ASP A O     1 
ATOM   8784  C  CB    . ASP A 1 2573 ? 129.041 104.049 114.845 1.00 14.78  ? 2573 ASP A CB    1 
ATOM   8785  C  CG    . ASP A 1 2573 ? 129.102 105.514 114.439 1.00 37.25  ? 2573 ASP A CG    1 
ATOM   8786  O  OD1   . ASP A 1 2573 ? 128.541 106.351 115.177 1.00 37.71  ? 2573 ASP A OD1   1 
ATOM   8787  O  OD2   . ASP A 1 2573 ? 129.706 105.805 113.385 1.00 52.00  ? 2573 ASP A OD2   1 
ATOM   8788  N  N     . THR A 1 2574 ? 130.625 101.510 115.922 1.00 7.33   ? 2574 THR A N     1 
ATOM   8789  C  CA    . THR A 1 2574 ? 130.695 100.041 116.084 1.00 7.26   ? 2574 THR A CA    1 
ATOM   8790  C  C     . THR A 1 2574 ? 130.828 99.697  117.552 1.00 6.10   ? 2574 THR A C     1 
ATOM   8791  O  O     . THR A 1 2574 ? 130.075 98.815  118.017 1.00 5.89   ? 2574 THR A O     1 
ATOM   8792  C  CB    . THR A 1 2574 ? 131.867 99.495  115.269 1.00 6.92   ? 2574 THR A CB    1 
ATOM   8793  O  OG1   . THR A 1 2574 ? 131.498 99.691  113.908 1.00 7.53   ? 2574 THR A OG1   1 
ATOM   8794  C  CG2   . THR A 1 2574 ? 132.124 98.022  115.528 1.00 9.78   ? 2574 THR A CG2   1 
ATOM   8795  N  N     . VAL A 1 2575 ? 131.734 100.369 118.268 1.00 6.13   ? 2575 VAL A N     1 
ATOM   8796  C  CA    . VAL A 1 2575 ? 131.988 100.018 119.699 1.00 6.93   ? 2575 VAL A CA    1 
ATOM   8797  C  C     . VAL A 1 2575 ? 130.746 100.373 120.535 1.00 6.43   ? 2575 VAL A C     1 
ATOM   8798  O  O     . VAL A 1 2575 ? 130.412 99.590  121.450 1.00 9.03   ? 2575 VAL A O     1 
ATOM   8799  C  CB    . VAL A 1 2575 ? 133.258 100.692 120.257 1.00 9.58   ? 2575 VAL A CB    1 
ATOM   8800  C  CG1   . VAL A 1 2575 ? 134.503 100.265 119.489 1.00 9.57   ? 2575 VAL A CG1   1 
ATOM   8801  C  CG2   . VAL A 1 2575 ? 133.140 102.211 120.292 1.00 9.44   ? 2575 VAL A CG2   1 
ATOM   8802  N  N     . ARG A 1 2576 ? 130.093 101.500 120.233 1.00 5.54   ? 2576 ARG A N     1 
ATOM   8803  C  CA    . ARG A 1 2576 ? 128.925 101.912 121.011 1.00 5.87   ? 2576 ARG A CA    1 
ATOM   8804  C  C     . ARG A 1 2576 ? 127.730 101.009 120.727 1.00 5.01   ? 2576 ARG A C     1 
ATOM   8805  O  O     . ARG A 1 2576 ? 127.039 100.553 121.651 1.00 5.11   ? 2576 ARG A O     1 
ATOM   8806  C  CB    . ARG A 1 2576 ? 128.582 103.371 120.713 1.00 7.76   ? 2576 ARG A CB    1 
ATOM   8807  C  CG    . ARG A 1 2576 ? 129.647 104.348 121.156 1.00 8.47   ? 2576 ARG A CG    1 
ATOM   8808  C  CD    . ARG A 1 2576 ? 129.234 105.786 120.914 1.00 13.87  ? 2576 ARG A CD    1 
ATOM   8809  N  NE    . ARG A 1 2576 ? 128.702 105.996 119.574 1.00 14.11  ? 2576 ARG A NE    1 
ATOM   8810  C  CZ    . ARG A 1 2576 ? 128.546 107.187 119.013 1.00 16.59  ? 2576 ARG A CZ    1 
ATOM   8811  N  NH1   . ARG A 1 2576 ? 128.882 108.298 119.647 1.00 18.70  ? 2576 ARG A NH1   1 
ATOM   8812  N  NH2   . ARG A 1 2576 ? 128.042 107.266 117.785 1.00 18.61  ? 2576 ARG A NH2   1 
ATOM   8813  N  N     . HIS A 1 2577 ? 127.479 100.730 119.446 1.00 6.32   ? 2577 HIS A N     1 
ATOM   8814  C  CA    . HIS A 1 2577 ? 126.360 99.879  119.069 1.00 5.02   ? 2577 HIS A CA    1 
ATOM   8815  C  C     . HIS A 1 2577 ? 126.558 98.461  119.579 1.00 5.18   ? 2577 HIS A C     1 
ATOM   8816  O  O     . HIS A 1 2577 ? 125.601 97.822  120.027 1.00 6.44   ? 2577 HIS A O     1 
ATOM   8817  C  CB    . HIS A 1 2577 ? 126.190 99.894  117.552 1.00 4.95   ? 2577 HIS A CB    1 
ATOM   8818  C  CG    . HIS A 1 2577 ? 125.690 101.199 117.016 1.00 6.64   ? 2577 HIS A CG    1 
ATOM   8819  N  ND1   . HIS A 1 2577 ? 125.729 101.518 115.676 1.00 7.65   ? 2577 HIS A ND1   1 
ATOM   8820  C  CD2   . HIS A 1 2577 ? 125.157 102.273 117.644 1.00 5.11   ? 2577 HIS A CD2   1 
ATOM   8821  C  CE1   . HIS A 1 2577 ? 125.229 102.728 115.500 1.00 6.62   ? 2577 HIS A CE1   1 
ATOM   8822  N  NE2   . HIS A 1 2577 ? 124.875 103.208 116.679 1.00 4.85   ? 2577 HIS A NE2   1 
ATOM   8823  N  N     . GLU A 1 2578 ? 127.792 97.954  119.528 1.00 5.09   ? 2578 GLU A N     1 
ATOM   8824  C  CA    . GLU A 1 2578 ? 128.063 96.617  120.041 1.00 5.49   ? 2578 GLU A CA    1 
ATOM   8825  C  C     . GLU A 1 2578 ? 127.813 96.541  121.540 1.00 4.96   ? 2578 GLU A C     1 
ATOM   8826  O  O     . GLU A 1 2578 ? 127.245 95.559  122.026 1.00 5.91   ? 2578 GLU A O     1 
ATOM   8827  C  CB    . GLU A 1 2578 ? 129.499 96.210  119.715 1.00 8.76   ? 2578 GLU A CB    1 
ATOM   8828  C  CG    . GLU A 1 2578 ? 129.731 94.710  119.715 1.00 10.23  ? 2578 GLU A CG    1 
ATOM   8829  C  CD    . GLU A 1 2578 ? 130.247 94.202  121.047 1.00 19.82  ? 2578 GLU A CD    1 
ATOM   8830  O  OE1   . GLU A 1 2578 ? 130.244 92.971  121.257 1.00 26.76  ? 2578 GLU A OE1   1 
ATOM   8831  O  OE2   . GLU A 1 2578 ? 130.653 95.034  121.885 1.00 22.18  ? 2578 GLU A OE2   1 
ATOM   8832  N  N     . ALA A 1 2579 ? 128.227 97.567  122.289 1.00 6.70   ? 2579 ALA A N     1 
ATOM   8833  C  CA    . ALA A 1 2579 ? 127.983 97.566  123.729 1.00 6.27   ? 2579 ALA A CA    1 
ATOM   8834  C  C     . ALA A 1 2579 ? 126.493 97.605  124.043 1.00 5.62   ? 2579 ALA A C     1 
ATOM   8835  O  O     . ALA A 1 2579 ? 126.013 96.860  124.908 1.00 4.33   ? 2579 ALA A O     1 
ATOM   8836  C  CB    . ALA A 1 2579 ? 128.696 98.747  124.382 1.00 5.55   ? 2579 ALA A CB    1 
ATOM   8837  N  N     . LEU A 1 2580 ? 125.742 98.470  123.355 1.00 5.84   ? 2580 LEU A N     1 
ATOM   8838  C  CA    . LEU A 1 2580 ? 124.303 98.541  123.602 1.00 4.78   ? 2580 LEU A CA    1 
ATOM   8839  C  C     . LEU A 1 2580 ? 123.611 97.234  123.226 1.00 5.52   ? 2580 LEU A C     1 
ATOM   8840  O  O     . LEU A 1 2580 ? 122.712 96.766  123.939 1.00 5.61   ? 2580 LEU A O     1 
ATOM   8841  C  CB    . LEU A 1 2580 ? 123.695 99.717  122.840 1.00 4.11   ? 2580 LEU A CB    1 
ATOM   8842  C  CG    . LEU A 1 2580 ? 122.193 99.938  123.020 1.00 5.84   ? 2580 LEU A CG    1 
ATOM   8843  C  CD1   . LEU A 1 2580 ? 121.876 100.362 124.445 1.00 5.50   ? 2580 LEU A CD1   1 
ATOM   8844  C  CD2   . LEU A 1 2580 ? 121.694 100.976 122.032 1.00 5.64   ? 2580 LEU A CD2   1 
ATOM   8845  N  N     . LEU A 1 2581 ? 124.018 96.632  122.105 1.00 5.57   ? 2581 LEU A N     1 
ATOM   8846  C  CA    . LEU A 1 2581 ? 123.455 95.353  121.695 1.00 4.43   ? 2581 LEU A CA    1 
ATOM   8847  C  C     . LEU A 1 2581 ? 123.773 94.262  122.706 1.00 5.11   ? 2581 LEU A C     1 
ATOM   8848  O  O     . LEU A 1 2581 ? 122.922 93.424  123.006 1.00 6.42   ? 2581 LEU A O     1 
ATOM   8849  C  CB    . LEU A 1 2581 ? 123.982 94.972  120.314 1.00 4.18   ? 2581 LEU A CB    1 
ATOM   8850  C  CG    . LEU A 1 2581 ? 123.332 95.669  119.121 1.00 5.67   ? 2581 LEU A CG    1 
ATOM   8851  C  CD1   . LEU A 1 2581 ? 123.780 95.012  117.834 1.00 6.94   ? 2581 LEU A CD1   1 
ATOM   8852  C  CD2   . LEU A 1 2581 ? 121.818 95.643  119.243 1.00 3.76   ? 2581 LEU A CD2   1 
ATOM   8853  N  N     . TYR A 1 2582 ? 124.999 94.251  123.231 1.00 5.26   ? 2582 TYR A N     1 
ATOM   8854  C  CA    . TYR A 1 2582 ? 125.363 93.294  124.269 1.00 6.37   ? 2582 TYR A CA    1 
ATOM   8855  C  C     . TYR A 1 2582 ? 124.477 93.468  125.495 1.00 7.56   ? 2582 TYR A C     1 
ATOM   8856  O  O     . TYR A 1 2582 ? 123.967 92.488  126.055 1.00 12.10  ? 2582 TYR A O     1 
ATOM   8857  C  CB    . TYR A 1 2582 ? 126.840 93.476  124.630 1.00 8.47   ? 2582 TYR A CB    1 
ATOM   8858  C  CG    . TYR A 1 2582 ? 127.428 92.407  125.523 1.00 17.52  ? 2582 TYR A CG    1 
ATOM   8859  C  CD1   . TYR A 1 2582 ? 127.293 92.474  126.902 1.00 16.04  ? 2582 TYR A CD1   1 
ATOM   8860  C  CD2   . TYR A 1 2582 ? 128.147 91.347  124.987 1.00 20.44  ? 2582 TYR A CD2   1 
ATOM   8861  C  CE1   . TYR A 1 2582 ? 127.836 91.505  127.723 1.00 21.22  ? 2582 TYR A CE1   1 
ATOM   8862  C  CE2   . TYR A 1 2582 ? 128.700 90.377  125.800 1.00 21.33  ? 2582 TYR A CE2   1 
ATOM   8863  C  CZ    . TYR A 1 2582 ? 128.538 90.459  127.166 1.00 32.94  ? 2582 TYR A CZ    1 
ATOM   8864  O  OH    . TYR A 1 2582 ? 129.084 89.492  127.980 1.00 45.05  ? 2582 TYR A OH    1 
ATOM   8865  N  N     . THR A 1 2583 ? 124.268 94.720  125.909 1.00 6.91   ? 2583 THR A N     1 
ATOM   8866  C  CA    . THR A 1 2583 ? 123.436 94.993  127.077 1.00 6.56   ? 2583 THR A CA    1 
ATOM   8867  C  C     . THR A 1 2583 ? 122.014 94.486  126.872 1.00 7.32   ? 2583 THR A C     1 
ATOM   8868  O  O     . THR A 1 2583 ? 121.446 93.825  127.749 1.00 11.16  ? 2583 THR A O     1 
ATOM   8869  C  CB    . THR A 1 2583 ? 123.440 96.492  127.380 1.00 9.55   ? 2583 THR A CB    1 
ATOM   8870  O  OG1   . THR A 1 2583 ? 124.694 96.859  127.968 1.00 10.82  ? 2583 THR A OG1   1 
ATOM   8871  C  CG2   . THR A 1 2583 ? 122.316 96.851  128.340 1.00 8.11   ? 2583 THR A CG2   1 
ATOM   8872  N  N     . TRP A 1 2584 ? 121.421 94.777  125.711 1.00 6.37   ? 2584 TRP A N     1 
ATOM   8873  C  CA    . TRP A 1 2584 ? 120.051 94.329  125.469 1.00 4.82   ? 2584 TRP A CA    1 
ATOM   8874  C  C     . TRP A 1 2584 ? 119.964 92.814  125.294 1.00 7.76   ? 2584 TRP A C     1 
ATOM   8875  O  O     . TRP A 1 2584 ? 119.008 92.187  125.764 1.00 8.91   ? 2584 TRP A O     1 
ATOM   8876  C  CB    . TRP A 1 2584 ? 119.453 95.043  124.258 1.00 5.57   ? 2584 TRP A CB    1 
ATOM   8877  C  CG    . TRP A 1 2584 ? 119.228 96.510  124.453 1.00 4.78   ? 2584 TRP A CG    1 
ATOM   8878  C  CD1   . TRP A 1 2584 ? 119.176 97.182  125.640 1.00 5.60   ? 2584 TRP A CD1   1 
ATOM   8879  C  CD2   . TRP A 1 2584 ? 118.954 97.478  123.433 1.00 4.71   ? 2584 TRP A CD2   1 
ATOM   8880  N  NE1   . TRP A 1 2584 ? 118.922 98.513  125.420 1.00 5.14   ? 2584 TRP A NE1   1 
ATOM   8881  C  CE2   . TRP A 1 2584 ? 118.778 98.721  124.074 1.00 5.26   ? 2584 TRP A CE2   1 
ATOM   8882  C  CE3   . TRP A 1 2584 ? 118.854 97.417  122.040 1.00 6.50   ? 2584 TRP A CE3   1 
ATOM   8883  C  CZ2   . TRP A 1 2584 ? 118.509 99.892  123.369 1.00 6.60   ? 2584 TRP A CZ2   1 
ATOM   8884  C  CZ3   . TRP A 1 2584 ? 118.588 98.582  121.342 1.00 4.68   ? 2584 TRP A CZ3   1 
ATOM   8885  C  CH2   . TRP A 1 2584 ? 118.417 99.802  122.007 1.00 6.05   ? 2584 TRP A CH2   1 
ATOM   8886  N  N     . LEU A 1 2585 ? 120.945 92.207  124.624 1.00 8.25   ? 2585 LEU A N     1 
ATOM   8887  C  CA    . LEU A 1 2585 ? 120.862 90.787  124.299 1.00 5.31   ? 2585 LEU A CA    1 
ATOM   8888  C  C     . LEU A 1 2585 ? 121.091 89.911  125.522 1.00 9.15   ? 2585 LEU A C     1 
ATOM   8889  O  O     . LEU A 1 2585 ? 120.395 88.905  125.706 1.00 8.40   ? 2585 LEU A O     1 
ATOM   8890  C  CB    . LEU A 1 2585 ? 121.868 90.440  123.203 1.00 5.66   ? 2585 LEU A CB    1 
ATOM   8891  C  CG    . LEU A 1 2585 ? 121.515 90.798  121.761 1.00 7.08   ? 2585 LEU A CG    1 
ATOM   8892  C  CD1   . LEU A 1 2585 ? 122.776 90.948  120.931 1.00 3.75   ? 2585 LEU A CD1   1 
ATOM   8893  C  CD2   . LEU A 1 2585 ? 120.612 89.732  121.173 1.00 5.53   ? 2585 LEU A CD2   1 
ATOM   8894  N  N     . ALA A 1 2586 ? 122.066 90.264  126.367 1.00 10.76  ? 2586 ALA A N     1 
ATOM   8895  C  CA    . ALA A 1 2586 ? 122.352 89.432  127.531 1.00 9.08   ? 2586 ALA A CA    1 
ATOM   8896  C  C     . ALA A 1 2586 ? 121.173 89.362  128.492 1.00 10.39  ? 2586 ALA A C     1 
ATOM   8897  O  O     . ALA A 1 2586 ? 121.103 88.433  129.304 1.00 11.92  ? 2586 ALA A O     1 
ATOM   8898  C  CB    . ALA A 1 2586 ? 123.594 89.945  128.258 1.00 9.86   ? 2586 ALA A CB    1 
ATOM   8899  N  N     . GLU A 1 2587 ? 120.250 90.315  128.415 1.00 10.19  ? 2587 GLU A N     1 
ATOM   8900  C  CA    . GLU A 1 2587 ? 119.011 90.274  129.178 1.00 9.00   ? 2587 GLU A CA    1 
ATOM   8901  C  C     . GLU A 1 2587 ? 117.907 89.507  128.464 1.00 9.00   ? 2587 GLU A C     1 
ATOM   8902  O  O     . GLU A 1 2587 ? 116.800 89.404  129.003 1.00 9.05   ? 2587 GLU A O     1 
ATOM   8903  C  CB    . GLU A 1 2587 ? 118.530 91.697  129.476 1.00 11.34  ? 2587 GLU A CB    1 
ATOM   8904  C  CG    . GLU A 1 2587 ? 119.447 92.488  130.390 1.00 17.82  ? 2587 GLU A CG    1 
ATOM   8905  C  CD    . GLU A 1 2587 ? 119.503 91.922  131.792 1.00 29.39  ? 2587 GLU A CD    1 
ATOM   8906  O  OE1   . GLU A 1 2587 ? 118.488 91.355  132.250 1.00 24.72  ? 2587 GLU A OE1   1 
ATOM   8907  O  OE2   . GLU A 1 2587 ? 120.560 92.050  132.441 1.00 27.97  ? 2587 GLU A OE2   1 
ATOM   8908  N  N     . HIS A 1 2588 ? 118.177 88.987  127.264 1.00 6.41   ? 2588 HIS A N     1 
ATOM   8909  C  CA    . HIS A 1 2588 ? 117.197 88.291  126.431 1.00 5.43   ? 2588 HIS A CA    1 
ATOM   8910  C  C     . HIS A 1 2588 ? 116.036 89.195  126.033 1.00 6.87   ? 2588 HIS A C     1 
ATOM   8911  O  O     . HIS A 1 2588 ? 114.970 88.711  125.638 1.00 8.75   ? 2588 HIS A O     1 
ATOM   8912  C  CB    . HIS A 1 2588 ? 116.682 87.022  127.119 1.00 4.60   ? 2588 HIS A CB    1 
ATOM   8913  C  CG    . HIS A 1 2588 ? 117.768 86.175  127.705 1.00 5.11   ? 2588 HIS A CG    1 
ATOM   8914  N  ND1   . HIS A 1 2588 ? 118.864 85.765  126.977 1.00 6.30   ? 2588 HIS A ND1   1 
ATOM   8915  C  CD2   . HIS A 1 2588 ? 117.937 85.676  128.952 1.00 4.97   ? 2588 HIS A CD2   1 
ATOM   8916  C  CE1   . HIS A 1 2588 ? 119.656 85.041  127.747 1.00 6.31   ? 2588 HIS A CE1   1 
ATOM   8917  N  NE2   . HIS A 1 2588 ? 119.116 84.972  128.951 1.00 7.44   ? 2588 HIS A NE2   1 
ATOM   8918  N  N     . LYS A 1 2589 ? 116.233 90.501  126.134 1.00 7.86   ? 2589 LYS A N     1 
ATOM   8919  C  CA    . LYS A 1 2589 ? 115.210 91.456  125.733 1.00 8.24   ? 2589 LYS A CA    1 
ATOM   8920  C  C     . LYS A 1 2589 ? 115.137 91.521  124.211 1.00 6.51   ? 2589 LYS A C     1 
ATOM   8921  O  O     . LYS A 1 2589 ? 116.172 91.679  123.553 1.00 6.94   ? 2589 LYS A O     1 
ATOM   8922  C  CB    . LYS A 1 2589 ? 115.534 92.833  126.313 1.00 9.03   ? 2589 LYS A CB    1 
ATOM   8923  C  CG    . LYS A 1 2589 ? 114.529 93.927  125.990 1.00 9.53   ? 2589 LYS A CG    1 
ATOM   8924  C  CD    . LYS A 1 2589 ? 113.412 93.983  127.016 1.00 11.43  ? 2589 LYS A CD    1 
ATOM   8925  C  CE    . LYS A 1 2589 ? 112.674 95.311  126.941 1.00 10.05  ? 2589 LYS A CE    1 
ATOM   8926  N  NZ    . LYS A 1 2589 ? 111.515 95.365  127.872 1.00 10.11  ? 2589 LYS A NZ    1 
ATOM   8927  N  N     . PRO A 1 2590 ? 113.952 91.388  123.616 1.00 6.43   ? 2590 PRO A N     1 
ATOM   8928  C  CA    . PRO A 1 2590 ? 113.845 91.530  122.158 1.00 5.40   ? 2590 PRO A CA    1 
ATOM   8929  C  C     . PRO A 1 2590 ? 114.239 92.935  121.729 1.00 4.48   ? 2590 PRO A C     1 
ATOM   8930  O  O     . PRO A 1 2590 ? 113.988 93.910  122.438 1.00 6.32   ? 2590 PRO A O     1 
ATOM   8931  C  CB    . PRO A 1 2590 ? 112.365 91.248  121.882 1.00 4.17   ? 2590 PRO A CB    1 
ATOM   8932  C  CG    . PRO A 1 2590 ? 111.679 91.554  123.172 1.00 4.00   ? 2590 PRO A CG    1 
ATOM   8933  C  CD    . PRO A 1 2590 ? 112.643 91.160  124.249 1.00 5.41   ? 2590 PRO A CD    1 
ATOM   8934  N  N     . LEU A 1 2591 ? 114.863 93.038  120.558 1.00 2.97   ? 2591 LEU A N     1 
ATOM   8935  C  CA    . LEU A 1 2591 ? 115.327 94.341  120.097 1.00 2.07   ? 2591 LEU A CA    1 
ATOM   8936  C  C     . LEU A 1 2591 ? 115.168 94.429  118.588 1.00 2.70   ? 2591 LEU A C     1 
ATOM   8937  O  O     . LEU A 1 2591 ? 115.002 93.418  117.907 1.00 1.97   ? 2591 LEU A O     1 
ATOM   8938  C  CB    . LEU A 1 2591 ? 116.783 94.601  120.514 1.00 3.94   ? 2591 LEU A CB    1 
ATOM   8939  C  CG    . LEU A 1 2591 ? 117.910 93.719  119.965 1.00 3.67   ? 2591 LEU A CG    1 
ATOM   8940  C  CD1   . LEU A 1 2591 ? 118.457 94.267  118.654 1.00 2.26   ? 2591 LEU A CD1   1 
ATOM   8941  C  CD2   . LEU A 1 2591 ? 119.023 93.556  120.987 1.00 3.97   ? 2591 LEU A CD2   1 
ATOM   8942  N  N     . VAL A 1 2592 ? 115.197 95.658  118.073 1.00 2.35   ? 2592 VAL A N     1 
ATOM   8943  C  CA    . VAL A 1 2592 ? 115.172 95.913  116.636 1.00 1.59   ? 2592 VAL A CA    1 
ATOM   8944  C  C     . VAL A 1 2592 ? 116.261 96.917  116.284 1.00 1.75   ? 2592 VAL A C     1 
ATOM   8945  O  O     . VAL A 1 2592 ? 116.406 97.948  116.951 1.00 1.86   ? 2592 VAL A O     1 
ATOM   8946  C  CB    . VAL A 1 2592 ? 113.796 96.414  116.152 1.00 1.46   ? 2592 VAL A CB    1 
ATOM   8947  C  CG1   . VAL A 1 2592 ? 113.877 96.858  114.705 1.00 1.79   ? 2592 VAL A CG1   1 
ATOM   8948  C  CG2   . VAL A 1 2592 ? 112.775 95.304  116.249 1.00 1.67   ? 2592 VAL A CG2   1 
ATOM   8949  N  N     . LEU A 1 2593 ? 117.025 96.602  115.243 1.00 1.48   ? 2593 LEU A N     1 
ATOM   8950  C  CA    . LEU A 1 2593 ? 117.985 97.518  114.646 1.00 1.57   ? 2593 LEU A CA    1 
ATOM   8951  C  C     . LEU A 1 2593 ? 117.364 98.104  113.386 1.00 1.70   ? 2593 LEU A C     1 
ATOM   8952  O  O     . LEU A 1 2593 ? 116.972 97.361  112.477 1.00 2.45   ? 2593 LEU A O     1 
ATOM   8953  C  CB    . LEU A 1 2593 ? 119.293 96.803  114.310 1.00 1.85   ? 2593 LEU A CB    1 
ATOM   8954  C  CG    . LEU A 1 2593 ? 119.982 96.022  115.427 1.00 2.47   ? 2593 LEU A CG    1 
ATOM   8955  C  CD1   . LEU A 1 2593 ? 119.691 94.539  115.290 1.00 2.89   ? 2593 LEU A CD1   1 
ATOM   8956  C  CD2   . LEU A 1 2593 ? 121.474 96.279  115.409 1.00 3.79   ? 2593 LEU A CD2   1 
ATOM   8957  N  N     . CYS A 1 2594 ? 117.275 99.427  113.330 1.00 2.15   ? 2594 CYS A N     1 
ATOM   8958  C  CA    . CYS A 1 2594 ? 116.727 100.119 112.177 1.00 2.21   ? 2594 CYS A CA    1 
ATOM   8959  C  C     . CYS A 1 2594 ? 117.804 100.991 111.551 1.00 2.60   ? 2594 CYS A C     1 
ATOM   8960  O  O     . CYS A 1 2594 ? 118.616 101.598 112.256 1.00 3.43   ? 2594 CYS A O     1 
ATOM   8961  C  CB    . CYS A 1 2594 ? 115.515 100.970 112.560 1.00 2.12   ? 2594 CYS A CB    1 
ATOM   8962  S  SG    . CYS A 1 2594 ? 114.585 101.580 111.141 1.00 3.09   ? 2594 CYS A SG    1 
ATOM   8963  N  N     . GLY A 1 2595 ? 117.811 101.052 110.218 1.00 2.25   ? 2595 GLY A N     1 
ATOM   8964  C  CA    . GLY A 1 2595 ? 118.816 101.866 109.510 1.00 1.97   ? 2595 GLY A CA    1 
ATOM   8965  C  C     . GLY A 1 2595 ? 118.714 101.681 108.010 1.00 3.08   ? 2595 GLY A C     1 
ATOM   8966  O  O     . GLY A 1 2595 ? 117.967 100.782 107.571 1.00 4.26   ? 2595 GLY A O     1 
ATOM   8967  N  N     . PRO A 1 2596 ? 119.432 102.486 107.197 1.00 4.93   ? 2596 PRO A N     1 
ATOM   8968  C  CA    . PRO A 1 2596 ? 119.421 102.312 105.752 1.00 4.34   ? 2596 PRO A CA    1 
ATOM   8969  C  C     . PRO A 1 2596 ? 120.064 100.981 105.383 1.00 3.56   ? 2596 PRO A C     1 
ATOM   8970  O  O     . PRO A 1 2596 ? 120.998 100.535 106.077 1.00 3.65   ? 2596 PRO A O     1 
ATOM   8971  C  CB    . PRO A 1 2596 ? 120.217 103.516 105.221 1.00 4.97   ? 2596 PRO A CB    1 
ATOM   8972  C  CG    . PRO A 1 2596 ? 120.333 104.453 106.404 1.00 4.88   ? 2596 PRO A CG    1 
ATOM   8973  C  CD    . PRO A 1 2596 ? 120.278 103.576 107.640 1.00 4.57   ? 2596 PRO A CD    1 
ATOM   8974  N  N     . PRO A 1 2597 ? 119.605 100.309 104.304 1.00 3.48   ? 2597 PRO A N     1 
ATOM   8975  C  CA    . PRO A 1 2597 ? 120.143 99.006  103.939 1.00 4.89   ? 2597 PRO A CA    1 
ATOM   8976  C  C     . PRO A 1 2597 ? 121.650 99.069  103.730 1.00 5.22   ? 2597 PRO A C     1 
ATOM   8977  O  O     . PRO A 1 2597 ? 122.116 99.908  102.937 1.00 7.49   ? 2597 PRO A O     1 
ATOM   8978  C  CB    . PRO A 1 2597 ? 119.387 98.654  102.646 1.00 5.18   ? 2597 PRO A CB    1 
ATOM   8979  C  CG    . PRO A 1 2597 ? 118.855 99.980  102.151 1.00 6.41   ? 2597 PRO A CG    1 
ATOM   8980  C  CD    . PRO A 1 2597 ? 118.569 100.783 103.406 1.00 5.52   ? 2597 PRO A CD    1 
ATOM   8981  N  N     . GLY A 1 2598 ? 122.396 98.196  104.414 1.00 3.22   ? 2598 GLY A N     1 
ATOM   8982  C  CA    . GLY A 1 2598 ? 123.868 98.198  104.305 1.00 3.33   ? 2598 GLY A CA    1 
ATOM   8983  C  C     . GLY A 1 2598 ? 124.498 99.102  105.346 1.00 2.99   ? 2598 GLY A C     1 
ATOM   8984  O  O     . GLY A 1 2598 ? 125.714 99.360  105.243 1.00 3.91   ? 2598 GLY A O     1 
ATOM   8985  N  N     . SER A 1 2599 ? 123.707 99.564  106.319 1.00 3.44   ? 2599 SER A N     1 
ATOM   8986  C  CA    . SER A 1 2599 ? 124.228 100.456 107.390 1.00 3.81   ? 2599 SER A CA    1 
ATOM   8987  C  C     . SER A 1 2599 ? 125.102 99.652  108.364 1.00 3.92   ? 2599 SER A C     1 
ATOM   8988  O  O     . SER A 1 2599 ? 125.817 100.282 109.170 1.00 3.30   ? 2599 SER A O     1 
ATOM   8989  C  CB    . SER A 1 2599 ? 123.108 101.161 108.113 1.00 2.75   ? 2599 SER A CB    1 
ATOM   8990  O  OG    . SER A 1 2599 ? 122.238 100.229 108.739 1.00 2.58   ? 2599 SER A OG    1 
ATOM   8991  N  N     . GLY A 1 2600 ? 125.047 98.318  108.288 1.00 2.71   ? 2600 GLY A N     1 
ATOM   8992  C  CA    . GLY A 1 2600 ? 125.881 97.470  109.161 1.00 3.37   ? 2600 GLY A CA    1 
ATOM   8993  C  C     . GLY A 1 2600 ? 125.086 96.918  110.329 1.00 3.65   ? 2600 GLY A C     1 
ATOM   8994  O  O     . GLY A 1 2600 ? 125.712 96.549  111.344 1.00 3.74   ? 2600 GLY A O     1 
ATOM   8995  N  N     . LYS A 1 2601 ? 123.758 96.867  110.198 1.00 3.81   ? 2601 LYS A N     1 
ATOM   8996  C  CA    . LYS A 1 2601 ? 122.888 96.356  111.291 1.00 3.31   ? 2601 LYS A CA    1 
ATOM   8997  C  C     . LYS A 1 2601 ? 123.211 94.875  111.557 1.00 4.76   ? 2601 LYS A C     1 
ATOM   8998  O  O     . LYS A 1 2601 ? 123.454 94.524  112.733 1.00 7.20   ? 2601 LYS A O     1 
ATOM   8999  C  CB    . LYS A 1 2601 ? 121.414 96.571  110.929 1.00 2.94   ? 2601 LYS A CB    1 
ATOM   9000  C  CG    . LYS A 1 2601 ? 120.984 98.031  110.869 1.00 2.70   ? 2601 LYS A CG    1 
ATOM   9001  C  CD    . LYS A 1 2601 ? 119.530 98.232  110.460 1.00 2.14   ? 2601 LYS A CD    1 
ATOM   9002  C  CE    . LYS A 1 2601 ? 119.263 97.824  109.046 1.00 2.17   ? 2601 LYS A CE    1 
ATOM   9003  N  NZ    . LYS A 1 2601 ? 120.035 98.623  108.091 1.00 2.28   ? 2601 LYS A NZ    1 
ATOM   9004  N  N     . THR A 1 2602 ? 123.230 94.048  110.507 1.00 4.50   ? 2602 THR A N     1 
ATOM   9005  C  CA    . THR A 1 2602 ? 123.528 92.606  110.665 1.00 5.06   ? 2602 THR A CA    1 
ATOM   9006  C  C     . THR A 1 2602 ? 124.950 92.444  111.159 1.00 4.44   ? 2602 THR A C     1 
ATOM   9007  O  O     . THR A 1 2602 ? 125.176 91.599  112.052 1.00 4.99   ? 2602 THR A O     1 
ATOM   9008  C  CB    . THR A 1 2602 ? 123.306 91.884  109.337 1.00 7.40   ? 2602 THR A CB    1 
ATOM   9009  O  OG1   . THR A 1 2602 ? 121.924 92.052  109.040 1.00 9.08   ? 2602 THR A OG1   1 
ATOM   9010  C  CG2   . THR A 1 2602 ? 123.642 90.405  109.418 1.00 5.16   ? 2602 THR A CG2   1 
ATOM   9011  N  N     . MET A 1 2603 ? 125.880 93.227  110.604 1.00 5.08   ? 2603 MET A N     1 
ATOM   9012  C  CA    . MET A 1 2603 ? 127.308 93.140  111.005 1.00 4.65   ? 2603 MET A CA    1 
ATOM   9013  C  C     . MET A 1 2603 ? 127.431 93.425  112.510 1.00 5.29   ? 2603 MET A C     1 
ATOM   9014  O  O     . MET A 1 2603 ? 128.107 92.640  113.208 1.00 6.72   ? 2603 MET A O     1 
ATOM   9015  C  CB    . MET A 1 2603 ? 128.149 94.159  110.229 1.00 3.82   ? 2603 MET A CB    1 
ATOM   9016  C  CG    . MET A 1 2603 ? 129.605 94.207  110.646 1.00 6.48   ? 2603 MET A CG    1 
ATOM   9017  S  SD    . MET A 1 2603 ? 130.470 95.629  109.949 1.00 5.37   ? 2603 MET A SD    1 
ATOM   9018  C  CE    . MET A 1 2603 ? 129.545 96.978  110.695 1.00 5.41   ? 2603 MET A CE    1 
ATOM   9019  N  N     . THR A 1 2604 ? 126.793 94.499  112.985 1.00 5.20   ? 2604 THR A N     1 
ATOM   9020  C  CA    . THR A 1 2604 ? 126.896 94.869  114.413 1.00 6.90   ? 2604 THR A CA    1 
ATOM   9021  C  C     . THR A 1 2604 ? 126.287 93.765  115.253 1.00 5.65   ? 2604 THR A C     1 
ATOM   9022  O  O     . THR A 1 2604 ? 126.905 93.396  116.275 1.00 6.36   ? 2604 THR A O     1 
ATOM   9023  C  CB    . THR A 1 2604 ? 126.224 96.218  114.667 1.00 9.09   ? 2604 THR A CB    1 
ATOM   9024  O  OG1   . THR A 1 2604 ? 126.866 97.133  113.785 1.00 13.25  ? 2604 THR A OG1   1 
ATOM   9025  C  CG2   . THR A 1 2604 ? 126.387 96.686  116.102 1.00 6.34   ? 2604 THR A CG2   1 
ATOM   9026  N  N     . LEU A 1 2605 ? 125.124 93.242  114.848 1.00 4.54   ? 2605 LEU A N     1 
ATOM   9027  C  CA    . LEU A 1 2605 ? 124.464 92.234  115.674 1.00 4.85   ? 2605 LEU A CA    1 
ATOM   9028  C  C     . LEU A 1 2605 ? 125.306 90.967  115.773 1.00 6.57   ? 2605 LEU A C     1 
ATOM   9029  O  O     . LEU A 1 2605 ? 125.431 90.382  116.854 1.00 7.59   ? 2605 LEU A O     1 
ATOM   9030  C  CB    . LEU A 1 2605 ? 123.068 91.911  115.139 1.00 6.03   ? 2605 LEU A CB    1 
ATOM   9031  C  CG    . LEU A 1 2605 ? 122.444 90.693  115.834 1.00 7.35   ? 2605 LEU A CG    1 
ATOM   9032  C  CD1   . LEU A 1 2605 ? 122.128 91.020  117.287 1.00 3.97   ? 2605 LEU A CD1   1 
ATOM   9033  C  CD2   . LEU A 1 2605 ? 121.198 90.201  115.128 1.00 4.98   ? 2605 LEU A CD2   1 
ATOM   9034  N  N     . PHE A 1 2606 ? 125.901 90.530  114.658 1.00 6.66   ? 2606 PHE A N     1 
ATOM   9035  C  CA    . PHE A 1 2606 ? 126.790 89.373  114.710 1.00 7.19   ? 2606 PHE A CA    1 
ATOM   9036  C  C     . PHE A 1 2606 ? 128.042 89.652  115.533 1.00 8.33   ? 2606 PHE A C     1 
ATOM   9037  O  O     . PHE A 1 2606 ? 128.512 88.766  116.256 1.00 10.12  ? 2606 PHE A O     1 
ATOM   9038  C  CB    . PHE A 1 2606 ? 127.164 88.916  113.298 1.00 8.38   ? 2606 PHE A CB    1 
ATOM   9039  C  CG    . PHE A 1 2606 ? 126.054 88.202  112.567 1.00 10.26  ? 2606 PHE A CG    1 
ATOM   9040  C  CD1   . PHE A 1 2606 ? 126.341 87.385  111.487 1.00 18.94  ? 2606 PHE A CD1   1 
ATOM   9041  C  CD2   . PHE A 1 2606 ? 124.739 88.299  112.990 1.00 9.72   ? 2606 PHE A CD2   1 
ATOM   9042  C  CE1   . PHE A 1 2606 ? 125.335 86.715  110.817 1.00 24.23  ? 2606 PHE A CE1   1 
ATOM   9043  C  CE2   . PHE A 1 2606 ? 123.730 87.625  112.326 1.00 9.80   ? 2606 PHE A CE2   1 
ATOM   9044  C  CZ    . PHE A 1 2606 ? 124.028 86.835  111.239 1.00 17.68  ? 2606 PHE A CZ    1 
ATOM   9045  N  N     . SER A 1 2607 ? 128.592 90.866  115.448 1.00 8.21   ? 2607 SER A N     1 
ATOM   9046  C  CA    . SER A 1 2607 ? 129.739 91.210  116.282 1.00 7.98   ? 2607 SER A CA    1 
ATOM   9047  C  C     . SER A 1 2607 ? 129.385 91.137  117.762 1.00 11.29  ? 2607 SER A C     1 
ATOM   9048  O  O     . SER A 1 2607 ? 130.171 90.631  118.573 1.00 13.74  ? 2607 SER A O     1 
ATOM   9049  C  CB    . SER A 1 2607 ? 130.250 92.604  115.918 1.00 7.88   ? 2607 SER A CB    1 
ATOM   9050  O  OG    . SER A 1 2607 ? 131.345 92.978  116.735 1.00 17.23  ? 2607 SER A OG    1 
ATOM   9051  N  N     . ALA A 1 2608 ? 128.207 91.641  118.134 1.00 8.94   ? 2608 ALA A N     1 
ATOM   9052  C  CA    . ALA A 1 2608 ? 127.771 91.562  119.525 1.00 8.00   ? 2608 ALA A CA    1 
ATOM   9053  C  C     . ALA A 1 2608 ? 127.532 90.118  119.951 1.00 10.02  ? 2608 ALA A C     1 
ATOM   9054  O  O     . ALA A 1 2608 ? 127.886 89.729  121.070 1.00 11.67  ? 2608 ALA A O     1 
ATOM   9055  C  CB    . ALA A 1 2608 ? 126.509 92.400  119.729 1.00 5.80   ? 2608 ALA A CB    1 
ATOM   9056  N  N     . LEU A 1 2609 ? 126.929 89.311  119.074 1.00 8.13   ? 2609 LEU A N     1 
ATOM   9057  C  CA    . LEU A 1 2609 ? 126.687 87.908  119.393 1.00 9.74   ? 2609 LEU A CA    1 
ATOM   9058  C  C     . LEU A 1 2609 ? 127.988 87.131  119.542 1.00 12.95  ? 2609 LEU A C     1 
ATOM   9059  O  O     . LEU A 1 2609 ? 128.035 86.142  120.281 1.00 15.23  ? 2609 LEU A O     1 
ATOM   9060  C  CB    . LEU A 1 2609 ? 125.808 87.270  118.318 1.00 8.42   ? 2609 LEU A CB    1 
ATOM   9061  C  CG    . LEU A 1 2609 ? 124.330 87.664  118.336 1.00 7.00   ? 2609 LEU A CG    1 
ATOM   9062  C  CD1   . LEU A 1 2609 ? 123.630 87.173  117.081 1.00 6.89   ? 2609 LEU A CD1   1 
ATOM   9063  C  CD2   . LEU A 1 2609 ? 123.649 87.121  119.582 1.00 8.36   ? 2609 LEU A CD2   1 
ATOM   9064  N  N     . ARG A 1 2610 ? 129.046 87.554  118.844 1.00 14.35  ? 2610 ARG A N     1 
ATOM   9065  C  CA    . ARG A 1 2610 ? 130.345 86.910  119.011 1.00 15.44  ? 2610 ARG A CA    1 
ATOM   9066  C  C     . ARG A 1 2610 ? 130.866 87.064  120.434 1.00 17.30  ? 2610 ARG A C     1 
ATOM   9067  O  O     . ARG A 1 2610 ? 131.631 86.218  120.910 1.00 27.45  ? 2610 ARG A O     1 
ATOM   9068  C  CB    . ARG A 1 2610 ? 131.349 87.484  118.012 1.00 15.62  ? 2610 ARG A CB    1 
ATOM   9069  C  CG    . ARG A 1 2610 ? 131.166 86.979  116.593 1.00 16.07  ? 2610 ARG A CG    1 
ATOM   9070  C  CD    . ARG A 1 2610 ? 132.353 87.342  115.719 1.00 20.34  ? 2610 ARG A CD    1 
ATOM   9071  N  NE    . ARG A 1 2610 ? 132.104 88.553  114.945 1.00 23.92  ? 2610 ARG A NE    1 
ATOM   9072  C  CZ    . ARG A 1 2610 ? 131.381 88.599  113.835 1.00 19.08  ? 2610 ARG A CZ    1 
ATOM   9073  N  NH1   . ARG A 1 2610 ? 130.819 87.513  113.329 1.00 22.41  ? 2610 ARG A NH1   1 
ATOM   9074  N  NH2   . ARG A 1 2610 ? 131.216 89.764  113.216 1.00 16.14  ? 2610 ARG A NH2   1 
ATOM   9075  N  N     . ALA A 1 2611 ? 130.465 88.129  121.126 1.00 15.33  ? 2611 ALA A N     1 
ATOM   9076  C  CA    . ALA A 1 2611 ? 130.820 88.325  122.525 1.00 16.74  ? 2611 ALA A CA    1 
ATOM   9077  C  C     . ALA A 1 2611 ? 129.874 87.610  123.479 1.00 18.29  ? 2611 ALA A C     1 
ATOM   9078  O  O     . ALA A 1 2611 ? 130.074 87.686  124.696 1.00 20.57  ? 2611 ALA A O     1 
ATOM   9079  C  CB    . ALA A 1 2611 ? 130.853 89.819  122.857 1.00 16.46  ? 2611 ALA A CB    1 
ATOM   9080  N  N     . LEU A 1 2612 ? 128.855 86.924  122.960 1.00 16.48  ? 2612 LEU A N     1 
ATOM   9081  C  CA    . LEU A 1 2612 ? 127.876 86.196  123.766 1.00 17.46  ? 2612 LEU A CA    1 
ATOM   9082  C  C     . LEU A 1 2612 ? 127.912 84.719  123.399 1.00 20.46  ? 2612 LEU A C     1 
ATOM   9083  O  O     . LEU A 1 2612 ? 127.210 84.281  122.474 1.00 22.71  ? 2612 LEU A O     1 
ATOM   9084  C  CB    . LEU A 1 2612 ? 126.472 86.765  123.574 1.00 15.82  ? 2612 LEU A CB    1 
ATOM   9085  C  CG    . LEU A 1 2612 ? 126.188 88.142  124.164 1.00 16.85  ? 2612 LEU A CG    1 
ATOM   9086  C  CD1   . LEU A 1 2612 ? 124.835 88.624  123.705 1.00 14.93  ? 2612 LEU A CD1   1 
ATOM   9087  C  CD2   . LEU A 1 2612 ? 126.215 88.045  125.677 1.00 19.54  ? 2612 LEU A CD2   1 
ATOM   9088  N  N     . PRO A 1 2613 ? 128.713 83.917  124.093 1.00 24.35  ? 2613 PRO A N     1 
ATOM   9089  C  CA    . PRO A 1 2613 ? 128.624 82.464  123.928 1.00 26.52  ? 2613 PRO A CA    1 
ATOM   9090  C  C     . PRO A 1 2613 ? 127.306 81.947  124.483 1.00 33.24  ? 2613 PRO A C     1 
ATOM   9091  O  O     . PRO A 1 2613 ? 126.575 82.646  125.188 1.00 39.58  ? 2613 PRO A O     1 
ATOM   9092  C  CB    . PRO A 1 2613 ? 129.822 81.940  124.723 1.00 27.32  ? 2613 PRO A CB    1 
ATOM   9093  C  CG    . PRO A 1 2613 ? 130.066 82.990  125.752 1.00 27.60  ? 2613 PRO A CG    1 
ATOM   9094  C  CD    . PRO A 1 2613 ? 129.721 84.300  125.096 1.00 26.23  ? 2613 PRO A CD    1 
ATOM   9095  N  N     . ASP A 1 2614 ? 127.001 80.698  124.133 1.00 28.92  ? 2614 ASP A N     1 
ATOM   9096  C  CA    . ASP A 1 2614 ? 125.742 80.040  124.471 1.00 31.73  ? 2614 ASP A CA    1 
ATOM   9097  C  C     . ASP A 1 2614 ? 124.541 80.712  123.817 1.00 25.49  ? 2614 ASP A C     1 
ATOM   9098  O  O     . ASP A 1 2614 ? 123.416 80.594  124.314 1.00 21.70  ? 2614 ASP A O     1 
ATOM   9099  C  CB    . ASP A 1 2614 ? 125.531 79.954  125.989 1.00 32.18  ? 2614 ASP A CB    1 
ATOM   9100  C  CG    . ASP A 1 2614 ? 126.789 79.548  126.731 1.00 43.87  ? 2614 ASP A CG    1 
ATOM   9101  O  OD1   . ASP A 1 2614 ? 127.457 78.589  126.291 1.00 47.14  ? 2614 ASP A OD1   1 
ATOM   9102  O  OD2   . ASP A 1 2614 ? 127.108 80.188  127.755 1.00 42.40  ? 2614 ASP A OD2   1 
ATOM   9103  N  N     . MET A 1 2615 ? 124.756 81.423  122.712 1.00 21.60  ? 2615 MET A N     1 
ATOM   9104  C  CA    . MET A 1 2615 ? 123.681 82.037  121.945 1.00 13.15  ? 2615 MET A CA    1 
ATOM   9105  C  C     . MET A 1 2615 ? 123.832 81.641  120.485 1.00 13.86  ? 2615 MET A C     1 
ATOM   9106  O  O     . MET A 1 2615 ? 124.852 81.942  119.858 1.00 20.16  ? 2615 MET A O     1 
ATOM   9107  C  CB    . MET A 1 2615 ? 123.690 83.563  122.087 1.00 17.43  ? 2615 MET A CB    1 
ATOM   9108  C  CG    . MET A 1 2615 ? 122.765 84.087  123.172 1.00 16.02  ? 2615 MET A CG    1 
ATOM   9109  S  SD    . MET A 1 2615 ? 122.455 85.857  123.035 1.00 39.82  ? 2615 MET A SD    1 
ATOM   9110  C  CE    . MET A 1 2615 ? 122.067 86.259  124.736 1.00 19.91  ? 2615 MET A CE    1 
ATOM   9111  N  N     . GLU A 1 2616 ? 122.817 80.972  119.951 1.00 12.93  ? 2616 GLU A N     1 
ATOM   9112  C  CA    . GLU A 1 2616 ? 122.797 80.535  118.561 1.00 10.54  ? 2616 GLU A CA    1 
ATOM   9113  C  C     . GLU A 1 2616 ? 121.813 81.391  117.778 1.00 7.86   ? 2616 GLU A C     1 
ATOM   9114  O  O     . GLU A 1 2616 ? 120.633 81.462  118.130 1.00 10.67  ? 2616 GLU A O     1 
ATOM   9115  C  CB    . GLU A 1 2616 ? 122.410 79.059  118.450 1.00 14.18  ? 2616 GLU A CB    1 
ATOM   9116  C  CG    . GLU A 1 2616 ? 122.447 78.524  117.027 1.00 22.62  ? 2616 GLU A CG    1 
ATOM   9117  C  CD    . GLU A 1 2616 ? 122.109 77.049  116.944 1.00 40.79  ? 2616 GLU A CD    1 
ATOM   9118  O  OE1   . GLU A 1 2616 ? 121.823 76.441  117.997 1.00 42.00  ? 2616 GLU A OE1   1 
ATOM   9119  O  OE2   . GLU A 1 2616 ? 122.125 76.498  115.823 1.00 39.81  ? 2616 GLU A OE2   1 
ATOM   9120  N  N     . VAL A 1 2617 ? 122.296 82.030  116.717 1.00 7.64   ? 2617 VAL A N     1 
ATOM   9121  C  CA    . VAL A 1 2617 ? 121.472 82.898  115.884 1.00 6.00   ? 2617 VAL A CA    1 
ATOM   9122  C  C     . VAL A 1 2617 ? 120.927 82.097  114.709 1.00 4.43   ? 2617 VAL A C     1 
ATOM   9123  O  O     . VAL A 1 2617 ? 121.625 81.254  114.131 1.00 7.41   ? 2617 VAL A O     1 
ATOM   9124  C  CB    . VAL A 1 2617 ? 122.262 84.137  115.413 1.00 4.79   ? 2617 VAL A CB    1 
ATOM   9125  C  CG1   . VAL A 1 2617 ? 123.323 83.763  114.386 1.00 6.88   ? 2617 VAL A CG1   1 
ATOM   9126  C  CG2   . VAL A 1 2617 ? 121.316 85.189  114.850 1.00 4.59   ? 2617 VAL A CG2   1 
ATOM   9127  N  N     . VAL A 1 2618 ? 119.657 82.329  114.385 1.00 4.75   ? 2618 VAL A N     1 
ATOM   9128  C  CA    . VAL A 1 2618 ? 119.000 81.727  113.231 1.00 5.17   ? 2618 VAL A CA    1 
ATOM   9129  C  C     . VAL A 1 2618 ? 118.333 82.849  112.451 1.00 5.21   ? 2618 VAL A C     1 
ATOM   9130  O  O     . VAL A 1 2618 ? 117.507 83.586  113.003 1.00 5.69   ? 2618 VAL A O     1 
ATOM   9131  C  CB    . VAL A 1 2618 ? 117.969 80.662  113.640 1.00 6.34   ? 2618 VAL A CB    1 
ATOM   9132  C  CG1   . VAL A 1 2618 ? 117.093 80.298  112.458 1.00 8.17   ? 2618 VAL A CG1   1 
ATOM   9133  C  CG2   . VAL A 1 2618 ? 118.668 79.432  114.194 1.00 6.73   ? 2618 VAL A CG2   1 
ATOM   9134  N  N     . GLY A 1 2619 ? 118.679 82.974  111.171 1.00 4.75   ? 2619 GLY A N     1 
ATOM   9135  C  CA    . GLY A 1 2619 ? 118.222 84.090  110.365 1.00 5.22   ? 2619 GLY A CA    1 
ATOM   9136  C  C     . GLY A 1 2619 ? 116.970 83.770  109.575 1.00 6.40   ? 2619 GLY A C     1 
ATOM   9137  O  O     . GLY A 1 2619 ? 116.946 82.826  108.782 1.00 8.86   ? 2619 GLY A O     1 
ATOM   9138  N  N     . LEU A 1 2620 ? 115.928 84.566  109.796 1.00 7.46   ? 2620 LEU A N     1 
ATOM   9139  C  CA    . LEU A 1 2620 ? 114.701 84.529  109.016 1.00 8.55   ? 2620 LEU A CA    1 
ATOM   9140  C  C     . LEU A 1 2620 ? 114.603 85.821  108.222 1.00 7.54   ? 2620 LEU A C     1 
ATOM   9141  O  O     . LEU A 1 2620 ? 114.896 86.901  108.748 1.00 8.15   ? 2620 LEU A O     1 
ATOM   9142  C  CB    . LEU A 1 2620 ? 113.473 84.371  109.915 1.00 7.14   ? 2620 LEU A CB    1 
ATOM   9143  C  CG    . LEU A 1 2620 ? 113.309 83.052  110.665 1.00 11.29  ? 2620 LEU A CG    1 
ATOM   9144  C  CD1   . LEU A 1 2620 ? 113.973 83.133  112.025 1.00 8.65   ? 2620 LEU A CD1   1 
ATOM   9145  C  CD2   . LEU A 1 2620 ? 111.838 82.713  110.808 1.00 9.27   ? 2620 LEU A CD2   1 
ATOM   9146  N  N     . ASN A 1 2621 ? 114.196 85.714  106.966 1.00 9.19   ? 2621 ASN A N     1 
ATOM   9147  C  CA    . ASN A 1 2621 ? 114.141 86.855  106.060 1.00 8.41   ? 2621 ASN A CA    1 
ATOM   9148  C  C     . ASN A 1 2621 ? 112.681 87.116  105.711 1.00 7.28   ? 2621 ASN A C     1 
ATOM   9149  O  O     . ASN A 1 2621 ? 112.061 86.351  104.968 1.00 10.29  ? 2621 ASN A O     1 
ATOM   9150  C  CB    . ASN A 1 2621 ? 114.990 86.588  104.825 1.00 10.71  ? 2621 ASN A CB    1 
ATOM   9151  C  CG    . ASN A 1 2621 ? 116.456 86.444  105.161 1.00 15.96  ? 2621 ASN A CG    1 
ATOM   9152  O  OD1   . ASN A 1 2621 ? 116.952 85.335  105.355 1.00 12.62  ? 2621 ASN A OD1   1 
ATOM   9153  N  ND2   . ASN A 1 2621 ? 117.160 87.567  105.234 1.00 16.11  ? 2621 ASN A ND2   1 
ATOM   9154  N  N     . PHE A 1 2622 ? 112.140 88.201  106.253 1.00 6.61   ? 2622 PHE A N     1 
ATOM   9155  C  CA    . PHE A 1 2622 ? 110.738 88.527  106.058 1.00 5.87   ? 2622 PHE A CA    1 
ATOM   9156  C  C     . PHE A 1 2622 ? 110.514 89.165  104.693 1.00 7.27   ? 2622 PHE A C     1 
ATOM   9157  O  O     . PHE A 1 2622 ? 111.333 89.945  104.201 1.00 8.44   ? 2622 PHE A O     1 
ATOM   9158  C  CB    . PHE A 1 2622 ? 110.245 89.472  107.156 1.00 5.35   ? 2622 PHE A CB    1 
ATOM   9159  C  CG    . PHE A 1 2622 ? 109.951 88.793  108.467 1.00 5.43   ? 2622 PHE A CG    1 
ATOM   9160  C  CD1   . PHE A 1 2622 ? 110.444 87.527  108.742 1.00 6.23   ? 2622 PHE A CD1   1 
ATOM   9161  C  CD2   . PHE A 1 2622 ? 109.180 89.427  109.427 1.00 5.42   ? 2622 PHE A CD2   1 
ATOM   9162  C  CE1   . PHE A 1 2622 ? 110.172 86.909  109.947 1.00 6.58   ? 2622 PHE A CE1   1 
ATOM   9163  C  CE2   . PHE A 1 2622 ? 108.906 88.813  110.634 1.00 5.37   ? 2622 PHE A CE2   1 
ATOM   9164  C  CZ    . PHE A 1 2622 ? 109.402 87.553  110.894 1.00 5.48   ? 2622 PHE A CZ    1 
ATOM   9165  N  N     . SER A 1 2623 ? 109.390 88.812  104.080 1.00 7.83   ? 2623 SER A N     1 
ATOM   9166  C  CA    . SER A 1 2623 ? 108.916 89.442  102.859 1.00 8.66   ? 2623 SER A CA    1 
ATOM   9167  C  C     . SER A 1 2623 ? 107.532 90.014  103.127 1.00 8.52   ? 2623 SER A C     1 
ATOM   9168  O  O     . SER A 1 2623 ? 107.024 89.956  104.250 1.00 8.03   ? 2623 SER A O     1 
ATOM   9169  C  CB    . SER A 1 2623 ? 108.890 88.447  101.692 1.00 11.97  ? 2623 SER A CB    1 
ATOM   9170  O  OG    . SER A 1 2623 ? 107.903 87.452  101.895 1.00 12.92  ? 2623 SER A OG    1 
ATOM   9171  N  N     . SER A 1 2624 ? 106.910 90.570  102.085 1.00 11.56  ? 2624 SER A N     1 
ATOM   9172  C  CA    . SER A 1 2624 ? 105.553 91.083  102.238 1.00 11.67  ? 2624 SER A CA    1 
ATOM   9173  C  C     . SER A 1 2624 ? 104.562 89.964  102.532 1.00 10.29  ? 2624 SER A C     1 
ATOM   9174  O  O     . SER A 1 2624 ? 103.527 90.205  103.163 1.00 13.02  ? 2624 SER A O     1 
ATOM   9175  C  CB    . SER A 1 2624 ? 105.134 91.853  100.985 1.00 13.03  ? 2624 SER A CB    1 
ATOM   9176  O  OG    . SER A 1 2624 ? 105.211 91.035  99.832  1.00 23.68  ? 2624 SER A OG    1 
ATOM   9177  N  N     . ALA A 1 2625 ? 104.865 88.741  102.103 1.00 11.22  ? 2625 ALA A N     1 
ATOM   9178  C  CA    . ALA A 1 2625 ? 103.985 87.597  102.289 1.00 13.54  ? 2625 ALA A CA    1 
ATOM   9179  C  C     . ALA A 1 2625 ? 104.337 86.773  103.521 1.00 14.43  ? 2625 ALA A C     1 
ATOM   9180  O  O     . ALA A 1 2625 ? 103.806 85.670  103.687 1.00 15.86  ? 2625 ALA A O     1 
ATOM   9181  C  CB    . ALA A 1 2625 ? 104.009 86.708  101.044 1.00 18.90  ? 2625 ALA A CB    1 
ATOM   9182  N  N     . THR A 1 2626 ? 105.219 87.275  104.382 1.00 11.25  ? 2626 THR A N     1 
ATOM   9183  C  CA    . THR A 1 2626 ? 105.639 86.515  105.552 1.00 10.87  ? 2626 THR A CA    1 
ATOM   9184  C  C     . THR A 1 2626 ? 104.492 86.375  106.545 1.00 9.45   ? 2626 THR A C     1 
ATOM   9185  O  O     . THR A 1 2626 ? 103.855 87.363  106.924 1.00 11.26  ? 2626 THR A O     1 
ATOM   9186  C  CB    . THR A 1 2626 ? 106.839 87.188  106.218 1.00 9.68   ? 2626 THR A CB    1 
ATOM   9187  O  OG1   . THR A 1 2626 ? 108.009 86.971  105.421 1.00 9.52   ? 2626 THR A OG1   1 
ATOM   9188  C  CG2   . THR A 1 2626 ? 107.070 86.624  107.614 1.00 7.34   ? 2626 THR A CG2   1 
ATOM   9189  N  N     . THR A 1 2627 ? 104.234 85.139  106.965 1.00 10.29  ? 2627 THR A N     1 
ATOM   9190  C  CA    . THR A 1 2627 ? 103.219 84.813  107.958 1.00 10.93  ? 2627 THR A CA    1 
ATOM   9191  C  C     . THR A 1 2627 ? 103.903 84.148  109.148 1.00 10.07  ? 2627 THR A C     1 
ATOM   9192  O  O     . THR A 1 2627 ? 105.096 83.831  109.068 1.00 10.99  ? 2627 THR A O     1 
ATOM   9193  C  CB    . THR A 1 2627 ? 102.150 83.898  107.351 1.00 11.92  ? 2627 THR A CB    1 
ATOM   9194  O  OG1   . THR A 1 2627 ? 102.713 82.607  107.089 1.00 13.18  ? 2627 THR A OG1   1 
ATOM   9195  C  CG2   . THR A 1 2627 ? 101.612 84.486  106.055 1.00 13.46  ? 2627 THR A CG2   1 
ATOM   9196  N  N     . PRO A 1 2628 ? 103.203 83.928  110.268 1.00 12.04  ? 2628 PRO A N     1 
ATOM   9197  C  CA    . PRO A 1 2628 ? 103.817 83.182  111.380 1.00 8.06   ? 2628 PRO A CA    1 
ATOM   9198  C  C     . PRO A 1 2628 ? 104.266 81.775  111.010 1.00 10.41  ? 2628 PRO A C     1 
ATOM   9199  O  O     . PRO A 1 2628 ? 105.001 81.157  111.792 1.00 10.68  ? 2628 PRO A O     1 
ATOM   9200  C  CB    . PRO A 1 2628 ? 102.703 83.149  112.432 1.00 6.55   ? 2628 PRO A CB    1 
ATOM   9201  C  CG    . PRO A 1 2628 ? 101.941 84.398  112.178 1.00 5.96   ? 2628 PRO A CG    1 
ATOM   9202  C  CD    . PRO A 1 2628 ? 101.938 84.564  110.681 1.00 8.23   ? 2628 PRO A CD    1 
ATOM   9203  N  N     . GLU A 1 2629 ? 103.844 81.250  109.856 1.00 12.96  ? 2629 GLU A N     1 
ATOM   9204  C  CA    . GLU A 1 2629 ? 104.248 79.907  109.455 1.00 14.04  ? 2629 GLU A CA    1 
ATOM   9205  C  C     . GLU A 1 2629 ? 105.757 79.796  109.274 1.00 13.79  ? 2629 GLU A C     1 
ATOM   9206  O  O     . GLU A 1 2629 ? 106.327 78.726  109.503 1.00 15.55  ? 2629 GLU A O     1 
ATOM   9207  C  CB    . GLU A 1 2629 ? 103.527 79.503  108.170 1.00 16.38  ? 2629 GLU A CB    1 
ATOM   9208  C  CG    . GLU A 1 2629 ? 103.225 78.017  108.075 1.00 27.96  ? 2629 GLU A CG    1 
ATOM   9209  C  CD    . GLU A 1 2629 ? 102.493 77.493  109.295 1.00 33.25  ? 2629 GLU A CD    1 
ATOM   9210  O  OE1   . GLU A 1 2629 ? 101.480 78.107  109.692 1.00 35.68  ? 2629 GLU A OE1   1 
ATOM   9211  O  OE2   . GLU A 1 2629 ? 102.932 76.470  109.860 1.00 27.99  ? 2629 GLU A OE2   1 
ATOM   9212  N  N     . LEU A 1 2630 ? 106.421 80.879  108.864 1.00 9.86   ? 2630 LEU A N     1 
ATOM   9213  C  CA    . LEU A 1 2630 ? 107.876 80.852  108.744 1.00 9.38   ? 2630 LEU A CA    1 
ATOM   9214  C  C     . LEU A 1 2630 ? 108.531 80.636  110.105 1.00 10.79  ? 2630 LEU A C     1 
ATOM   9215  O  O     . LEU A 1 2630 ? 109.439 79.804  110.253 1.00 14.18  ? 2630 LEU A O     1 
ATOM   9216  C  CB    . LEU A 1 2630 ? 108.362 82.152  108.099 1.00 11.70  ? 2630 LEU A CB    1 
ATOM   9217  C  CG    . LEU A 1 2630 ? 109.847 82.290  107.763 1.00 13.11  ? 2630 LEU A CG    1 
ATOM   9218  C  CD1   . LEU A 1 2630 ? 110.180 81.517  106.499 1.00 16.88  ? 2630 LEU A CD1   1 
ATOM   9219  C  CD2   . LEU A 1 2630 ? 110.224 83.755  107.611 1.00 7.32   ? 2630 LEU A CD2   1 
ATOM   9220  N  N     . LEU A 1 2631 ? 108.065 81.368  111.119 1.00 9.34   ? 2631 LEU A N     1 
ATOM   9221  C  CA    . LEU A 1 2631 ? 108.564 81.170  112.476 1.00 9.55   ? 2631 LEU A CA    1 
ATOM   9222  C  C     . LEU A 1 2631 ? 108.233 79.774  112.988 1.00 7.63   ? 2631 LEU A C     1 
ATOM   9223  O  O     . LEU A 1 2631 ? 109.038 79.157  113.694 1.00 8.63   ? 2631 LEU A O     1 
ATOM   9224  C  CB    . LEU A 1 2631 ? 107.987 82.236  113.409 1.00 9.71   ? 2631 LEU A CB    1 
ATOM   9225  C  CG    . LEU A 1 2631 ? 108.422 83.690  113.228 1.00 8.62   ? 2631 LEU A CG    1 
ATOM   9226  C  CD1   . LEU A 1 2631 ? 107.559 84.603  114.078 1.00 7.55   ? 2631 LEU A CD1   1 
ATOM   9227  C  CD2   . LEU A 1 2631 ? 109.884 83.855  113.599 1.00 9.91   ? 2631 LEU A CD2   1 
ATOM   9228  N  N     . LEU A 1 2632 ? 107.043 79.264  112.654 1.00 8.45   ? 2632 LEU A N     1 
ATOM   9229  C  CA    . LEU A 1 2632 ? 106.677 77.914  113.072 1.00 8.53   ? 2632 LEU A CA    1 
ATOM   9230  C  C     . LEU A 1 2632 ? 107.594 76.867  112.449 1.00 9.38   ? 2632 LEU A C     1 
ATOM   9231  O  O     . LEU A 1 2632 ? 107.997 75.913  113.120 1.00 9.73   ? 2632 LEU A O     1 
ATOM   9232  C  CB    . LEU A 1 2632 ? 105.217 77.630  112.721 1.00 12.24  ? 2632 LEU A CB    1 
ATOM   9233  C  CG    . LEU A 1 2632 ? 104.167 78.462  113.459 1.00 8.86   ? 2632 LEU A CG    1 
ATOM   9234  C  CD1   . LEU A 1 2632 ? 102.798 78.277  112.831 1.00 13.93  ? 2632 LEU A CD1   1 
ATOM   9235  C  CD2   . LEU A 1 2632 ? 104.134 78.075  114.928 1.00 4.91   ? 2632 LEU A CD2   1 
ATOM   9236  N  N     . LYS A 1 2633 ? 107.931 77.025  111.167 1.00 10.20  ? 2633 LYS A N     1 
ATOM   9237  C  CA    . LYS A 1 2633 ? 108.860 76.098  110.526 1.00 9.67   ? 2633 LYS A CA    1 
ATOM   9238  C  C     . LYS A 1 2633 ? 110.246 76.187  111.154 1.00 8.45   ? 2633 LYS A C     1 
ATOM   9239  O  O     . LYS A 1 2633 ? 110.922 75.166  111.341 1.00 9.89   ? 2633 LYS A O     1 
ATOM   9240  C  CB    . LYS A 1 2633 ? 108.932 76.375  109.024 1.00 12.55  ? 2633 LYS A CB    1 
ATOM   9241  C  CG    . LYS A 1 2633 ? 107.637 76.109  108.276 1.00 16.03  ? 2633 LYS A CG    1 
ATOM   9242  C  CD    . LYS A 1 2633 ? 107.066 74.742  108.607 1.00 26.19  ? 2633 LYS A CD    1 
ATOM   9243  C  CE    . LYS A 1 2633 ? 105.682 74.567  108.004 1.00 35.10  ? 2633 LYS A CE    1 
ATOM   9244  N  NZ    . LYS A 1 2633 ? 104.887 73.532  108.722 1.00 33.11  ? 2633 LYS A NZ    1 
ATOM   9245  N  N     . THR A 1 2634 ? 110.692 77.405  111.476 1.00 6.71   ? 2634 THR A N     1 
ATOM   9246  C  CA    . THR A 1 2634 ? 111.989 77.558  112.127 1.00 8.16   ? 2634 THR A CA    1 
ATOM   9247  C  C     . THR A 1 2634 ? 112.004 76.892  113.501 1.00 6.64   ? 2634 THR A C     1 
ATOM   9248  O  O     . THR A 1 2634 ? 112.988 76.240  113.871 1.00 6.00   ? 2634 THR A O     1 
ATOM   9249  C  CB    . THR A 1 2634 ? 112.352 79.038  112.232 1.00 8.04   ? 2634 THR A CB    1 
ATOM   9250  O  OG1   . THR A 1 2634 ? 112.458 79.592  110.916 1.00 10.47  ? 2634 THR A OG1   1 
ATOM   9251  C  CG2   . THR A 1 2634 ? 113.677 79.211  112.949 1.00 7.55   ? 2634 THR A CG2   1 
ATOM   9252  N  N     . PHE A 1 2635 ? 110.921 77.041  114.270 1.00 5.87   ? 2635 PHE A N     1 
ATOM   9253  C  CA    . PHE A 1 2635 ? 110.805 76.319  115.536 1.00 6.76   ? 2635 PHE A CA    1 
ATOM   9254  C  C     . PHE A 1 2635 ? 110.787 74.811  115.324 1.00 8.43   ? 2635 PHE A C     1 
ATOM   9255  O  O     . PHE A 1 2635 ? 111.380 74.063  116.109 1.00 10.01  ? 2635 PHE A O     1 
ATOM   9256  C  CB    . PHE A 1 2635 ? 109.555 76.761  116.298 1.00 6.46   ? 2635 PHE A CB    1 
ATOM   9257  C  CG    . PHE A 1 2635 ? 109.626 78.162  116.827 1.00 7.12   ? 2635 PHE A CG    1 
ATOM   9258  C  CD1   . PHE A 1 2635 ? 108.476 78.908  117.012 1.00 6.35   ? 2635 PHE A CD1   1 
ATOM   9259  C  CD2   . PHE A 1 2635 ? 110.840 78.710  117.198 1.00 5.65   ? 2635 PHE A CD2   1 
ATOM   9260  C  CE1   . PHE A 1 2635 ? 108.541 80.191  117.520 1.00 5.33   ? 2635 PHE A CE1   1 
ATOM   9261  C  CE2   . PHE A 1 2635 ? 110.909 79.986  117.711 1.00 6.50   ? 2635 PHE A CE2   1 
ATOM   9262  C  CZ    . PHE A 1 2635 ? 109.758 80.730  117.870 1.00 7.04   ? 2635 PHE A CZ    1 
ATOM   9263  N  N     . ASP A 1 2636 ? 110.101 74.343  114.281 1.00 10.36  ? 2636 ASP A N     1 
ATOM   9264  C  CA    . ASP A 1 2636 ? 110.069 72.911  114.008 1.00 9.52   ? 2636 ASP A CA    1 
ATOM   9265  C  C     . ASP A 1 2636 ? 111.469 72.376  113.745 1.00 9.40   ? 2636 ASP A C     1 
ATOM   9266  O  O     . ASP A 1 2636 ? 111.833 71.299  114.231 1.00 12.31  ? 2636 ASP A O     1 
ATOM   9267  C  CB    . ASP A 1 2636 ? 109.153 72.620  112.820 1.00 8.88   ? 2636 ASP A CB    1 
ATOM   9268  C  CG    . ASP A 1 2636 ? 107.686 72.642  113.194 1.00 22.61  ? 2636 ASP A CG    1 
ATOM   9269  O  OD1   . ASP A 1 2636 ? 107.349 72.218  114.320 1.00 30.57  ? 2636 ASP A OD1   1 
ATOM   9270  O  OD2   . ASP A 1 2636 ? 106.867 73.081  112.360 1.00 32.91  ? 2636 ASP A OD2   1 
ATOM   9271  N  N     . HIS A 1 2637 ? 112.269 73.114  112.974 1.00 7.63   ? 2637 HIS A N     1 
ATOM   9272  C  CA    . HIS A 1 2637 ? 113.620 72.648  112.677 1.00 9.34   ? 2637 HIS A CA    1 
ATOM   9273  C  C     . HIS A 1 2637 ? 114.539 72.749  113.891 1.00 9.97   ? 2637 HIS A C     1 
ATOM   9274  O  O     . HIS A 1 2637 ? 115.242 71.788  114.222 1.00 10.19  ? 2637 HIS A O     1 
ATOM   9275  C  CB    . HIS A 1 2637 ? 114.210 73.427  111.504 1.00 10.37  ? 2637 HIS A CB    1 
ATOM   9276  C  CG    . HIS A 1 2637 ? 115.591 72.986  111.132 1.00 14.17  ? 2637 HIS A CG    1 
ATOM   9277  N  ND1   . HIS A 1 2637 ? 116.724 73.544  111.685 1.00 13.54  ? 2637 HIS A ND1   1 
ATOM   9278  C  CD2   . HIS A 1 2637 ? 116.022 72.031  110.275 1.00 16.08  ? 2637 HIS A CD2   1 
ATOM   9279  C  CE1   . HIS A 1 2637 ? 117.793 72.957  111.178 1.00 19.07  ? 2637 HIS A CE1   1 
ATOM   9280  N  NE2   . HIS A 1 2637 ? 117.395 72.035  110.320 1.00 21.09  ? 2637 HIS A NE2   1 
ATOM   9281  N  N     . TYR A 1 2638 ? 114.550 73.898  114.568 1.00 9.82   ? 2638 TYR A N     1 
ATOM   9282  C  CA    . TYR A 1 2638 ? 115.556 74.178  115.586 1.00 8.74   ? 2638 TYR A CA    1 
ATOM   9283  C  C     . TYR A 1 2638 ? 115.093 73.910  117.011 1.00 9.24   ? 2638 TYR A C     1 
ATOM   9284  O  O     . TYR A 1 2638 ? 115.937 73.841  117.911 1.00 9.05   ? 2638 TYR A O     1 
ATOM   9285  C  CB    . TYR A 1 2638 ? 116.025 75.635  115.485 1.00 5.94   ? 2638 TYR A CB    1 
ATOM   9286  C  CG    . TYR A 1 2638 ? 116.770 75.960  114.212 1.00 9.07   ? 2638 TYR A CG    1 
ATOM   9287  C  CD1   . TYR A 1 2638 ? 118.139 75.745  114.114 1.00 11.84  ? 2638 TYR A CD1   1 
ATOM   9288  C  CD2   . TYR A 1 2638 ? 116.110 76.489  113.111 1.00 8.64   ? 2638 TYR A CD2   1 
ATOM   9289  C  CE1   . TYR A 1 2638 ? 118.827 76.042  112.954 1.00 11.80  ? 2638 TYR A CE1   1 
ATOM   9290  C  CE2   . TYR A 1 2638 ? 116.790 76.789  111.947 1.00 12.92  ? 2638 TYR A CE2   1 
ATOM   9291  C  CZ    . TYR A 1 2638 ? 118.148 76.564  111.875 1.00 14.37  ? 2638 TYR A CZ    1 
ATOM   9292  O  OH    . TYR A 1 2638 ? 118.830 76.861  110.717 1.00 21.17  ? 2638 TYR A OH    1 
ATOM   9293  N  N     . CYS A 1 2639 ? 113.795 73.756  117.247 1.00 8.84   ? 2639 CYS A N     1 
ATOM   9294  C  CA    . CYS A 1 2639 ? 113.275 73.602  118.595 1.00 7.83   ? 2639 CYS A CA    1 
ATOM   9295  C  C     . CYS A 1 2639 ? 112.398 72.362  118.673 1.00 9.69   ? 2639 CYS A C     1 
ATOM   9296  O  O     . CYS A 1 2639 ? 112.042 71.757  117.658 1.00 10.78  ? 2639 CYS A O     1 
ATOM   9297  C  CB    . CYS A 1 2639 ? 112.475 74.838  119.035 1.00 6.04   ? 2639 CYS A CB    1 
ATOM   9298  S  SG    . CYS A 1 2639 ? 113.426 76.373  119.079 1.00 7.54   ? 2639 CYS A SG    1 
ATOM   9299  N  N     . GLU A 1 2640 ? 112.056 71.987  119.901 1.00 9.82   ? 2640 GLU A N     1 
ATOM   9300  C  CA    . GLU A 1 2640 ? 111.186 70.853  120.161 1.00 12.41  ? 2640 GLU A CA    1 
ATOM   9301  C  C     . GLU A 1 2640 ? 110.129 71.239  121.184 1.00 9.15   ? 2640 GLU A C     1 
ATOM   9302  O  O     . GLU A 1 2640 ? 110.370 72.073  122.067 1.00 8.14   ? 2640 GLU A O     1 
ATOM   9303  C  CB    . GLU A 1 2640 ? 111.978 69.637  120.659 1.00 15.79  ? 2640 GLU A CB    1 
ATOM   9304  C  CG    . GLU A 1 2640 ? 112.940 69.936  121.794 1.00 22.23  ? 2640 GLU A CG    1 
ATOM   9305  C  CD    . GLU A 1 2640 ? 113.564 68.681  122.371 1.00 40.99  ? 2640 GLU A CD    1 
ATOM   9306  O  OE1   . GLU A 1 2640 ? 114.481 68.124  121.733 1.00 47.95  ? 2640 GLU A OE1   1 
ATOM   9307  O  OE2   . GLU A 1 2640 ? 113.135 68.250  123.462 1.00 47.06  ? 2640 GLU A OE2   1 
ATOM   9308  N  N     . TYR A 1 2641 ? 108.953 70.630  121.038 1.00 11.14  ? 2641 TYR A N     1 
ATOM   9309  C  CA    . TYR A 1 2641 ? 107.865 70.755  121.996 1.00 11.18  ? 2641 TYR A CA    1 
ATOM   9310  C  C     . TYR A 1 2641 ? 107.950 69.596  122.980 1.00 10.81  ? 2641 TYR A C     1 
ATOM   9311  O  O     . TYR A 1 2641 ? 108.187 68.453  122.577 1.00 16.24  ? 2641 TYR A O     1 
ATOM   9312  C  CB    . TYR A 1 2641 ? 106.509 70.728  121.288 1.00 9.77   ? 2641 TYR A CB    1 
ATOM   9313  C  CG    . TYR A 1 2641 ? 106.268 71.861  120.317 1.00 9.92   ? 2641 TYR A CG    1 
ATOM   9314  C  CD1   . TYR A 1 2641 ? 106.720 71.783  119.005 1.00 11.18  ? 2641 TYR A CD1   1 
ATOM   9315  C  CD2   . TYR A 1 2641 ? 105.575 73.000  120.704 1.00 8.00   ? 2641 TYR A CD2   1 
ATOM   9316  C  CE1   . TYR A 1 2641 ? 106.496 72.809  118.109 1.00 9.62   ? 2641 TYR A CE1   1 
ATOM   9317  C  CE2   . TYR A 1 2641 ? 105.347 74.033  119.813 1.00 7.91   ? 2641 TYR A CE2   1 
ATOM   9318  C  CZ    . TYR A 1 2641 ? 105.810 73.932  118.518 1.00 12.64  ? 2641 TYR A CZ    1 
ATOM   9319  O  OH    . TYR A 1 2641 ? 105.587 74.956  117.628 1.00 17.68  ? 2641 TYR A OH    1 
ATOM   9320  N  N     . ARG A 1 2642 ? 107.758 69.885  124.263 1.00 11.20  ? 2642 ARG A N     1 
ATOM   9321  C  CA    . ARG A 1 2642 ? 107.791 68.848  125.283 1.00 11.51  ? 2642 ARG A CA    1 
ATOM   9322  C  C     . ARG A 1 2642 ? 106.674 69.054  126.295 1.00 17.37  ? 2642 ARG A C     1 
ATOM   9323  O  O     . ARG A 1 2642 ? 106.337 70.188  126.654 1.00 16.07  ? 2642 ARG A O     1 
ATOM   9324  C  CB    . ARG A 1 2642 ? 109.160 68.796  125.985 1.00 15.17  ? 2642 ARG A CB    1 
ATOM   9325  C  CG    . ARG A 1 2642 ? 109.448 69.926  126.957 1.00 14.22  ? 2642 ARG A CG    1 
ATOM   9326  C  CD    . ARG A 1 2642 ? 110.661 69.590  127.816 1.00 15.70  ? 2642 ARG A CD    1 
ATOM   9327  N  NE    . ARG A 1 2642 ? 110.918 70.596  128.839 1.00 19.37  ? 2642 ARG A NE    1 
ATOM   9328  C  CZ    . ARG A 1 2642 ? 111.480 71.773  128.607 1.00 21.83  ? 2642 ARG A CZ    1 
ATOM   9329  N  NH1   . ARG A 1 2642 ? 111.890 72.117  127.397 1.00 22.58  ? 2642 ARG A NH1   1 
ATOM   9330  N  NH2   . ARG A 1 2642 ? 111.643 72.625  129.615 1.00 16.48  ? 2642 ARG A NH2   1 
ATOM   9331  N  N     . ARG A 1 2643 ? 106.090 67.938  126.729 1.00 23.12  ? 2643 ARG A N     1 
ATOM   9332  C  CA    . ARG A 1 2643 ? 105.062 67.928  127.761 1.00 19.42  ? 2643 ARG A CA    1 
ATOM   9333  C  C     . ARG A 1 2643 ? 105.713 68.120  129.125 1.00 19.66  ? 2643 ARG A C     1 
ATOM   9334  O  O     . ARG A 1 2643 ? 106.677 67.422  129.461 1.00 24.94  ? 2643 ARG A O     1 
ATOM   9335  C  CB    . ARG A 1 2643 ? 104.298 66.605  127.720 1.00 26.97  ? 2643 ARG A CB    1 
ATOM   9336  C  CG    . ARG A 1 2643 ? 103.550 66.326  126.423 1.00 28.97  ? 2643 ARG A CG    1 
ATOM   9337  C  CD    . ARG A 1 2643 ? 102.395 67.287  126.193 1.00 34.63  ? 2643 ARG A CD    1 
ATOM   9338  N  NE    . ARG A 1 2643 ? 101.372 67.124  127.221 1.00 44.64  ? 2643 ARG A NE    1 
ATOM   9339  C  CZ    . ARG A 1 2643 ? 100.415 68.004  127.481 1.00 43.58  ? 2643 ARG A CZ    1 
ATOM   9340  N  NH1   . ARG A 1 2643 ? 100.299 69.125  126.791 1.00 36.27  ? 2643 ARG A NH1   1 
ATOM   9341  N  NH2   . ARG A 1 2643 ? 99.544  67.746  128.453 1.00 37.03  ? 2643 ARG A NH2   1 
ATOM   9342  N  N     . THR A 1 2644 ? 105.195 69.058  129.909 1.00 16.43  ? 2644 THR A N     1 
ATOM   9343  C  CA    . THR A 1 2644 ? 105.590 69.288  131.286 1.00 20.18  ? 2644 THR A CA    1 
ATOM   9344  C  C     . THR A 1 2644 ? 104.331 69.406  132.133 1.00 22.79  ? 2644 THR A C     1 
ATOM   9345  O  O     . THR A 1 2644 ? 103.247 69.690  131.607 1.00 22.43  ? 2644 THR A O     1 
ATOM   9346  C  CB    . THR A 1 2644 ? 106.434 70.566  131.426 1.00 24.13  ? 2644 THR A CB    1 
ATOM   9347  O  OG1   . THR A 1 2644 ? 105.588 71.719  131.325 1.00 24.36  ? 2644 THR A OG1   1 
ATOM   9348  C  CG2   . THR A 1 2644 ? 107.516 70.634  130.356 1.00 16.73  ? 2644 THR A CG2   1 
ATOM   9349  N  N     . PRO A 1 2645 ? 104.429 69.189  133.447 1.00 30.57  ? 2645 PRO A N     1 
ATOM   9350  C  CA    . PRO A 1 2645 ? 103.236 69.332  134.300 1.00 29.05  ? 2645 PRO A CA    1 
ATOM   9351  C  C     . PRO A 1 2645 ? 102.588 70.705  134.227 1.00 27.47  ? 2645 PRO A C     1 
ATOM   9352  O  O     . PRO A 1 2645 ? 101.445 70.856  134.676 1.00 29.23  ? 2645 PRO A O     1 
ATOM   9353  C  CB    . PRO A 1 2645 ? 103.776 69.043  135.707 1.00 23.09  ? 2645 PRO A CB    1 
ATOM   9354  C  CG    . PRO A 1 2645 ? 104.965 68.179  135.475 1.00 23.92  ? 2645 PRO A CG    1 
ATOM   9355  C  CD    . PRO A 1 2645 ? 105.587 68.683  134.206 1.00 26.29  ? 2645 PRO A CD    1 
ATOM   9356  N  N     . ASN A 1 2646 ? 103.274 71.708  133.679 1.00 25.04  ? 2646 ASN A N     1 
ATOM   9357  C  CA    . ASN A 1 2646 ? 102.726 73.049  133.544 1.00 25.24  ? 2646 ASN A CA    1 
ATOM   9358  C  C     . ASN A 1 2646 ? 102.343 73.397  132.109 1.00 24.99  ? 2646 ASN A C     1 
ATOM   9359  O  O     . ASN A 1 2646 ? 101.976 74.546  131.842 1.00 34.25  ? 2646 ASN A O     1 
ATOM   9360  C  CB    . ASN A 1 2646 ? 103.721 74.077  134.087 1.00 27.85  ? 2646 ASN A CB    1 
ATOM   9361  C  CG    . ASN A 1 2646 ? 104.278 73.687  135.441 1.00 33.05  ? 2646 ASN A CG    1 
ATOM   9362  O  OD1   . ASN A 1 2646 ? 103.591 73.782  136.458 1.00 29.35  ? 2646 ASN A OD1   1 
ATOM   9363  N  ND2   . ASN A 1 2646 ? 105.529 73.241  135.461 1.00 36.11  ? 2646 ASN A ND2   1 
ATOM   9364  N  N     . GLY A 1 2647 ? 102.416 72.447  131.186 1.00 20.14  ? 2647 GLY A N     1 
ATOM   9365  C  CA    . GLY A 1 2647 ? 101.964 72.655  129.825 1.00 14.38  ? 2647 GLY A CA    1 
ATOM   9366  C  C     . GLY A 1 2647 ? 103.004 72.249  128.797 1.00 13.76  ? 2647 GLY A C     1 
ATOM   9367  O  O     . GLY A 1 2647 ? 103.961 71.531  129.080 1.00 17.37  ? 2647 GLY A O     1 
ATOM   9368  N  N     . VAL A 1 2648 ? 102.779 72.717  127.570 1.00 12.68  ? 2648 VAL A N     1 
ATOM   9369  C  CA    . VAL A 1 2648 ? 103.721 72.459  126.488 1.00 10.70  ? 2648 VAL A CA    1 
ATOM   9370  C  C     . VAL A 1 2648 ? 104.808 73.523  126.509 1.00 7.90   ? 2648 VAL A C     1 
ATOM   9371  O  O     . VAL A 1 2648 ? 104.520 74.725  126.583 1.00 6.59   ? 2648 VAL A O     1 
ATOM   9372  C  CB    . VAL A 1 2648 ? 102.998 72.432  125.134 1.00 10.92  ? 2648 VAL A CB    1 
ATOM   9373  C  CG1   . VAL A 1 2648 ? 103.992 72.194  124.008 1.00 7.72   ? 2648 VAL A CG1   1 
ATOM   9374  C  CG2   . VAL A 1 2648 ? 101.919 71.368  125.130 1.00 14.02  ? 2648 VAL A CG2   1 
ATOM   9375  N  N     . VAL A 1 2649 ? 106.063 73.089  126.452 1.00 8.37   ? 2649 VAL A N     1 
ATOM   9376  C  CA    . VAL A 1 2649 ? 107.208 73.990  126.438 1.00 6.57   ? 2649 VAL A CA    1 
ATOM   9377  C  C     . VAL A 1 2649 ? 107.954 73.799  125.126 1.00 7.63   ? 2649 VAL A C     1 
ATOM   9378  O  O     . VAL A 1 2649 ? 108.321 72.673  124.774 1.00 10.86  ? 2649 VAL A O     1 
ATOM   9379  C  CB    . VAL A 1 2649 ? 108.141 73.746  127.639 1.00 8.77   ? 2649 VAL A CB    1 
ATOM   9380  C  CG1   . VAL A 1 2649 ? 109.488 74.404  127.406 1.00 8.00   ? 2649 VAL A CG1   1 
ATOM   9381  C  CG2   . VAL A 1 2649 ? 107.505 74.266  128.917 1.00 8.02   ? 2649 VAL A CG2   1 
ATOM   9382  N  N     . LEU A 1 2650 ? 108.170 74.895  124.406 1.00 5.31   ? 2650 LEU A N     1 
ATOM   9383  C  CA    . LEU A 1 2650 ? 108.975 74.896  123.192 1.00 5.16   ? 2650 LEU A CA    1 
ATOM   9384  C  C     . LEU A 1 2650 ? 110.365 75.411  123.534 1.00 4.66   ? 2650 LEU A C     1 
ATOM   9385  O  O     . LEU A 1 2650 ? 110.519 76.570  123.937 1.00 3.78   ? 2650 LEU A O     1 
ATOM   9386  C  CB    . LEU A 1 2650 ? 108.335 75.760  122.107 1.00 5.46   ? 2650 LEU A CB    1 
ATOM   9387  C  CG    . LEU A 1 2650 ? 109.045 75.757  120.754 1.00 4.58   ? 2650 LEU A CG    1 
ATOM   9388  C  CD1   . LEU A 1 2650 ? 108.943 74.395  120.095 1.00 6.54   ? 2650 LEU A CD1   1 
ATOM   9389  C  CD2   . LEU A 1 2650 ? 108.467 76.835  119.857 1.00 4.17   ? 2650 LEU A CD2   1 
ATOM   9390  N  N     . ALA A 1 2651 ? 111.366 74.559  123.368 1.00 6.06   ? 2651 ALA A N     1 
ATOM   9391  C  CA    . ALA A 1 2651 ? 112.729 74.900  123.743 1.00 6.00   ? 2651 ALA A CA    1 
ATOM   9392  C  C     . ALA A 1 2651 ? 113.678 74.486  122.631 1.00 7.58   ? 2651 ALA A C     1 
ATOM   9393  O  O     . ALA A 1 2651 ? 113.416 73.515  121.914 1.00 10.26  ? 2651 ALA A O     1 
ATOM   9394  C  CB    . ALA A 1 2651 ? 113.136 74.225  125.059 1.00 7.15   ? 2651 ALA A CB    1 
ATOM   9395  N  N     . PRO A 1 2652 ? 114.796 75.196  122.470 1.00 8.08   ? 2652 PRO A N     1 
ATOM   9396  C  CA    . PRO A 1 2652 ? 115.773 74.805  121.449 1.00 8.43   ? 2652 PRO A CA    1 
ATOM   9397  C  C     . PRO A 1 2652 ? 116.303 73.401  121.697 1.00 11.13  ? 2652 PRO A C     1 
ATOM   9398  O  O     . PRO A 1 2652 ? 116.442 72.957  122.839 1.00 11.42  ? 2652 PRO A O     1 
ATOM   9399  C  CB    . PRO A 1 2652 ? 116.881 75.855  121.591 1.00 6.42   ? 2652 PRO A CB    1 
ATOM   9400  C  CG    . PRO A 1 2652 ? 116.233 77.009  122.273 1.00 5.47   ? 2652 PRO A CG    1 
ATOM   9401  C  CD    . PRO A 1 2652 ? 115.201 76.420  123.180 1.00 5.92   ? 2652 PRO A CD    1 
ATOM   9402  N  N     . VAL A 1 2653 ? 116.590 72.699  120.599 1.00 13.15  ? 2653 VAL A N     1 
ATOM   9403  C  CA    . VAL A 1 2653 ? 117.053 71.317  120.691 1.00 14.64  ? 2653 VAL A CA    1 
ATOM   9404  C  C     . VAL A 1 2653 ? 118.361 71.241  121.466 1.00 18.29  ? 2653 VAL A C     1 
ATOM   9405  O  O     . VAL A 1 2653 ? 118.534 70.381  122.338 1.00 19.39  ? 2653 VAL A O     1 
ATOM   9406  C  CB    . VAL A 1 2653 ? 117.185 70.709  119.282 1.00 16.85  ? 2653 VAL A CB    1 
ATOM   9407  C  CG1   . VAL A 1 2653 ? 118.123 69.512  119.298 1.00 23.04  ? 2653 VAL A CG1   1 
ATOM   9408  C  CG2   . VAL A 1 2653 ? 115.816 70.314  118.750 1.00 12.91  ? 2653 VAL A CG2   1 
ATOM   9409  N  N     . GLN A 1 2654 ? 119.296 72.143  121.175 1.00 18.73  ? 2654 GLN A N     1 
ATOM   9410  C  CA    . GLN A 1 2654 ? 120.562 72.178  121.891 1.00 21.46  ? 2654 GLN A CA    1 
ATOM   9411  C  C     . GLN A 1 2654 ? 120.343 72.709  123.303 1.00 19.58  ? 2654 GLN A C     1 
ATOM   9412  O  O     . GLN A 1 2654 ? 119.783 73.794  123.487 1.00 18.22  ? 2654 GLN A O     1 
ATOM   9413  C  CB    . GLN A 1 2654 ? 121.573 73.048  121.145 1.00 23.39  ? 2654 GLN A CB    1 
ATOM   9414  C  CG    . GLN A 1 2654 ? 121.976 72.502  119.784 1.00 37.80  ? 2654 GLN A CG    1 
ATOM   9415  C  CD    . GLN A 1 2654 ? 122.669 71.157  119.875 1.00 52.00  ? 2654 GLN A CD    1 
ATOM   9416  O  OE1   . GLN A 1 2654 ? 122.110 70.130  119.488 1.00 43.03  ? 2654 GLN A OE1   1 
ATOM   9417  N  NE2   . GLN A 1 2654 ? 123.893 71.155  120.390 1.00 50.54  ? 2654 GLN A NE2   1 
ATOM   9418  N  N     . LEU A 1 2655 ? 120.789 71.946  124.296 1.00 24.15  ? 2655 LEU A N     1 
ATOM   9419  C  CA    . LEU A 1 2655 ? 120.571 72.308  125.688 1.00 24.23  ? 2655 LEU A CA    1 
ATOM   9420  C  C     . LEU A 1 2655 ? 121.579 73.355  126.144 1.00 26.20  ? 2655 LEU A C     1 
ATOM   9421  O  O     . LEU A 1 2655 ? 122.714 73.412  125.662 1.00 26.94  ? 2655 LEU A O     1 
ATOM   9422  C  CB    . LEU A 1 2655 ? 120.663 71.074  126.589 1.00 28.83  ? 2655 LEU A CB    1 
ATOM   9423  C  CG    . LEU A 1 2655 ? 119.824 69.843  126.235 1.00 29.99  ? 2655 LEU A CG    1 
ATOM   9424  C  CD1   . LEU A 1 2655 ? 119.666 68.954  127.457 1.00 24.66  ? 2655 LEU A CD1   1 
ATOM   9425  C  CD2   . LEU A 1 2655 ? 118.457 70.239  125.692 1.00 26.37  ? 2655 LEU A CD2   1 
ATOM   9426  N  N     . GLY A 1 2656 ? 121.148 74.193  127.085 1.00 23.22  ? 2656 GLY A N     1 
ATOM   9427  C  CA    . GLY A 1 2656 ? 121.993 75.247  127.602 1.00 22.41  ? 2656 GLY A CA    1 
ATOM   9428  C  C     . GLY A 1 2656 ? 122.217 76.403  126.657 1.00 22.95  ? 2656 GLY A C     1 
ATOM   9429  O  O     . GLY A 1 2656 ? 123.001 77.303  126.978 1.00 30.80  ? 2656 GLY A O     1 
ATOM   9430  N  N     . LYS A 1 2657 ? 121.554 76.410  125.505 1.00 20.92  ? 2657 LYS A N     1 
ATOM   9431  C  CA    . LYS A 1 2657 ? 121.747 77.427  124.484 1.00 16.15  ? 2657 LYS A CA    1 
ATOM   9432  C  C     . LYS A 1 2657 ? 120.495 78.280  124.358 1.00 11.76  ? 2657 LYS A C     1 
ATOM   9433  O  O     . LYS A 1 2657 ? 119.376 77.760  124.308 1.00 10.37  ? 2657 LYS A O     1 
ATOM   9434  C  CB    . LYS A 1 2657 ? 122.077 76.792  123.129 1.00 19.14  ? 2657 LYS A CB    1 
ATOM   9435  C  CG    . LYS A 1 2657 ? 123.402 76.052  123.091 1.00 25.61  ? 2657 LYS A CG    1 
ATOM   9436  C  CD    . LYS A 1 2657 ? 124.564 77.023  123.068 1.00 31.17  ? 2657 LYS A CD    1 
ATOM   9437  C  CE    . LYS A 1 2657 ? 125.774 76.435  122.365 1.00 37.95  ? 2657 LYS A CE    1 
ATOM   9438  N  NZ    . LYS A 1 2657 ? 127.034 76.740  123.098 1.00 42.64  ? 2657 LYS A NZ    1 
ATOM   9439  N  N     . TRP A 1 2658 ? 120.692 79.593  124.308 1.00 11.25  ? 2658 TRP A N     1 
ATOM   9440  C  CA    . TRP A 1 2658 ? 119.622 80.529  123.998 1.00 5.75   ? 2658 TRP A CA    1 
ATOM   9441  C  C     . TRP A 1 2658 ? 119.615 80.803  122.499 1.00 6.63   ? 2658 TRP A C     1 
ATOM   9442  O  O     . TRP A 1 2658 ? 120.666 81.059  121.903 1.00 11.17  ? 2658 TRP A O     1 
ATOM   9443  C  CB    . TRP A 1 2658 ? 119.797 81.828  124.785 1.00 6.54   ? 2658 TRP A CB    1 
ATOM   9444  C  CG    . TRP A 1 2658 ? 119.095 81.851  126.102 1.00 5.33   ? 2658 TRP A CG    1 
ATOM   9445  C  CD1   . TRP A 1 2658 ? 119.508 81.272  127.265 1.00 4.50   ? 2658 TRP A CD1   1 
ATOM   9446  C  CD2   . TRP A 1 2658 ? 117.850 82.494  126.393 1.00 4.43   ? 2658 TRP A CD2   1 
ATOM   9447  N  NE1   . TRP A 1 2658 ? 118.595 81.513  128.263 1.00 5.18   ? 2658 TRP A NE1   1 
ATOM   9448  C  CE2   . TRP A 1 2658 ? 117.567 82.261  127.753 1.00 4.30   ? 2658 TRP A CE2   1 
ATOM   9449  C  CE3   . TRP A 1 2658 ? 116.945 83.244  125.635 1.00 4.00   ? 2658 TRP A CE3   1 
ATOM   9450  C  CZ2   . TRP A 1 2658 ? 116.418 82.749  128.370 1.00 3.39   ? 2658 TRP A CZ2   1 
ATOM   9451  C  CZ3   . TRP A 1 2658 ? 115.805 83.725  126.249 1.00 4.62   ? 2658 TRP A CZ3   1 
ATOM   9452  C  CH2   . TRP A 1 2658 ? 115.552 83.478  127.603 1.00 4.25   ? 2658 TRP A CH2   1 
ATOM   9453  N  N     . LEU A 1 2659 ? 118.432 80.752  121.895 1.00 5.60   ? 2659 LEU A N     1 
ATOM   9454  C  CA    . LEU A 1 2659 ? 118.287 80.874  120.451 1.00 4.77   ? 2659 LEU A CA    1 
ATOM   9455  C  C     . LEU A 1 2659 ? 117.735 82.251  120.102 1.00 3.43   ? 2659 LEU A C     1 
ATOM   9456  O  O     . LEU A 1 2659 ? 116.716 82.678  120.657 1.00 3.54   ? 2659 LEU A O     1 
ATOM   9457  C  CB    . LEU A 1 2659 ? 117.380 79.765  119.911 1.00 4.19   ? 2659 LEU A CB    1 
ATOM   9458  C  CG    . LEU A 1 2659 ? 117.213 79.572  118.401 1.00 6.02   ? 2659 LEU A CG    1 
ATOM   9459  C  CD1   . LEU A 1 2659 ? 116.863 78.125  118.104 1.00 5.97   ? 2659 LEU A CD1   1 
ATOM   9460  C  CD2   . LEU A 1 2659 ? 116.141 80.484  117.833 1.00 7.36   ? 2659 LEU A CD2   1 
ATOM   9461  N  N     . VAL A 1 2660 ? 118.410 82.938  119.183 1.00 3.54   ? 2660 VAL A N     1 
ATOM   9462  C  CA    . VAL A 1 2660 ? 118.026 84.269  118.723 1.00 3.52   ? 2660 VAL A CA    1 
ATOM   9463  C  C     . VAL A 1 2660 ? 117.447 84.144  117.324 1.00 3.64   ? 2660 VAL A C     1 
ATOM   9464  O  O     . VAL A 1 2660 ? 118.153 83.756  116.386 1.00 4.16   ? 2660 VAL A O     1 
ATOM   9465  C  CB    . VAL A 1 2660 ? 119.217 85.239  118.711 1.00 4.20   ? 2660 VAL A CB    1 
ATOM   9466  C  CG1   . VAL A 1 2660 ? 118.740 86.649  118.409 1.00 4.03   ? 2660 VAL A CG1   1 
ATOM   9467  C  CG2   . VAL A 1 2660 ? 119.971 85.195  120.017 1.00 3.41   ? 2660 VAL A CG2   1 
ATOM   9468  N  N     . LEU A 1 2661 ? 116.181 84.518  117.171 1.00 3.63   ? 2661 LEU A N     1 
ATOM   9469  C  CA    . LEU A 1 2661 ? 115.548 84.596  115.859 1.00 3.64   ? 2661 LEU A CA    1 
ATOM   9470  C  C     . LEU A 1 2661 ? 115.813 85.981  115.281 1.00 4.38   ? 2661 LEU A C     1 
ATOM   9471  O  O     . LEU A 1 2661 ? 115.217 86.967  115.722 1.00 5.10   ? 2661 LEU A O     1 
ATOM   9472  C  CB    . LEU A 1 2661 ? 114.051 84.332  115.966 1.00 5.56   ? 2661 LEU A CB    1 
ATOM   9473  C  CG    . LEU A 1 2661 ? 113.593 82.943  116.394 1.00 9.32   ? 2661 LEU A CG    1 
ATOM   9474  C  CD1   . LEU A 1 2661 ? 112.097 82.976  116.561 1.00 10.14  ? 2661 LEU A CD1   1 
ATOM   9475  C  CD2   . LEU A 1 2661 ? 113.993 81.898  115.372 1.00 8.42   ? 2661 LEU A CD2   1 
ATOM   9476  N  N     . PHE A 1 2662 ? 116.705 86.056  114.296 1.00 4.62   ? 2662 PHE A N     1 
ATOM   9477  C  CA    . PHE A 1 2662 ? 117.061 87.312  113.645 1.00 3.64   ? 2662 PHE A CA    1 
ATOM   9478  C  C     . PHE A 1 2662 ? 116.155 87.516  112.436 1.00 5.12   ? 2662 PHE A C     1 
ATOM   9479  O  O     . PHE A 1 2662 ? 116.367 86.901  111.389 1.00 7.09   ? 2662 PHE A O     1 
ATOM   9480  C  CB    . PHE A 1 2662 ? 118.528 87.307  113.223 1.00 4.31   ? 2662 PHE A CB    1 
ATOM   9481  C  CG    . PHE A 1 2662 ? 118.943 88.540  112.474 1.00 8.28   ? 2662 PHE A CG    1 
ATOM   9482  C  CD1   . PHE A 1 2662 ? 118.445 89.782  112.826 1.00 7.45   ? 2662 PHE A CD1   1 
ATOM   9483  C  CD2   . PHE A 1 2662 ? 119.802 88.450  111.391 1.00 8.40   ? 2662 PHE A CD2   1 
ATOM   9484  C  CE1   . PHE A 1 2662 ? 118.816 90.911  112.132 1.00 7.07   ? 2662 PHE A CE1   1 
ATOM   9485  C  CE2   . PHE A 1 2662 ? 120.171 89.578  110.688 1.00 11.68  ? 2662 PHE A CE2   1 
ATOM   9486  C  CZ    . PHE A 1 2662 ? 119.680 90.810  111.060 1.00 10.41  ? 2662 PHE A CZ    1 
ATOM   9487  N  N     . CYS A 1 2663 ? 115.163 88.392  112.573 1.00 5.40   ? 2663 CYS A N     1 
ATOM   9488  C  CA    . CYS A 1 2663 ? 114.275 88.748  111.473 1.00 6.05   ? 2663 CYS A CA    1 
ATOM   9489  C  C     . CYS A 1 2663 ? 114.841 89.977  110.771 1.00 7.55   ? 2663 CYS A C     1 
ATOM   9490  O  O     . CYS A 1 2663 ? 114.960 91.045  111.379 1.00 7.56   ? 2663 CYS A O     1 
ATOM   9491  C  CB    . CYS A 1 2663 ? 112.857 89.010  111.977 1.00 8.75   ? 2663 CYS A CB    1 
ATOM   9492  S  SG    . CYS A 1 2663 ? 112.220 87.740  113.096 1.00 11.89  ? 2663 CYS A SG    1 
ATOM   9493  N  N     . ASP A 1 2664 ? 115.181 89.827  109.492 1.00 8.73   ? 2664 ASP A N     1 
ATOM   9494  C  CA    . ASP A 1 2664 ? 115.941 90.846  108.778 1.00 8.83   ? 2664 ASP A CA    1 
ATOM   9495  C  C     . ASP A 1 2664 ? 115.076 91.950  108.184 1.00 12.67  ? 2664 ASP A C     1 
ATOM   9496  O  O     . ASP A 1 2664 ? 115.587 93.047  107.931 1.00 15.89  ? 2664 ASP A O     1 
ATOM   9497  C  CB    . ASP A 1 2664 ? 116.764 90.195  107.661 1.00 11.60  ? 2664 ASP A CB    1 
ATOM   9498  C  CG    . ASP A 1 2664 ? 117.900 91.078  107.179 1.00 23.50  ? 2664 ASP A CG    1 
ATOM   9499  O  OD1   . ASP A 1 2664 ? 118.169 92.116  107.819 1.00 24.55  ? 2664 ASP A OD1   1 
ATOM   9500  O  OD2   . ASP A 1 2664 ? 118.526 90.731  106.156 1.00 30.12  ? 2664 ASP A OD2   1 
ATOM   9501  N  N     . GLU A 1 2665 ? 113.795 91.693  107.939 1.00 8.45   ? 2665 GLU A N     1 
ATOM   9502  C  CA    . GLU A 1 2665 ? 112.895 92.651  107.299 1.00 7.45   ? 2665 GLU A CA    1 
ATOM   9503  C  C     . GLU A 1 2665 ? 111.562 92.705  108.035 1.00 8.30   ? 2665 GLU A C     1 
ATOM   9504  O  O     . GLU A 1 2665 ? 110.488 92.604  107.439 1.00 8.20   ? 2665 GLU A O     1 
ATOM   9505  C  CB    . GLU A 1 2665 ? 112.694 92.304  105.829 1.00 10.11  ? 2665 GLU A CB    1 
ATOM   9506  C  CG    . GLU A 1 2665 ? 113.978 92.221  105.016 1.00 13.11  ? 2665 GLU A CG    1 
ATOM   9507  C  CD    . GLU A 1 2665 ? 114.564 93.583  104.691 1.00 19.58  ? 2665 GLU A CD    1 
ATOM   9508  O  OE1   . GLU A 1 2665 ? 113.907 94.605  104.979 1.00 20.49  ? 2665 GLU A OE1   1 
ATOM   9509  O  OE2   . GLU A 1 2665 ? 115.688 93.632  104.151 1.00 23.89  ? 2665 GLU A OE2   1 
ATOM   9510  N  N     . ILE A 1 2666 ? 111.627 92.874  109.358 1.00 6.18   ? 2666 ILE A N     1 
ATOM   9511  C  CA    . ILE A 1 2666 ? 110.474 92.668  110.229 1.00 4.65   ? 2666 ILE A CA    1 
ATOM   9512  C  C     . ILE A 1 2666 ? 109.281 93.557  109.885 1.00 5.05   ? 2666 ILE A C     1 
ATOM   9513  O  O     . ILE A 1 2666 ? 108.144 93.209  110.219 1.00 5.85   ? 2666 ILE A O     1 
ATOM   9514  C  CB    . ILE A 1 2666 ? 110.903 92.862  111.701 1.00 5.23   ? 2666 ILE A CB    1 
ATOM   9515  C  CG1   . ILE A 1 2666 ? 109.922 92.162  112.646 1.00 4.58   ? 2666 ILE A CG1   1 
ATOM   9516  C  CG2   . ILE A 1 2666 ? 111.037 94.341  112.041 1.00 3.94   ? 2666 ILE A CG2   1 
ATOM   9517  C  CD1   . ILE A 1 2666 ? 110.474 91.928  114.032 1.00 5.55   ? 2666 ILE A CD1   1 
ATOM   9518  N  N     . ASN A 1 2667 ? 109.498 94.691  109.220 1.00 4.83   ? 2667 ASN A N     1 
ATOM   9519  C  CA    . ASN A 1 2667 ? 108.417 95.631  108.949 1.00 5.09   ? 2667 ASN A CA    1 
ATOM   9520  C  C     . ASN A 1 2667 ? 107.905 95.569  107.512 1.00 6.92   ? 2667 ASN A C     1 
ATOM   9521  O  O     . ASN A 1 2667 ? 107.055 96.382  107.135 1.00 7.92   ? 2667 ASN A O     1 
ATOM   9522  C  CB    . ASN A 1 2667 ? 108.863 97.054  109.296 1.00 4.49   ? 2667 ASN A CB    1 
ATOM   9523  C  CG    . ASN A 1 2667 ? 109.996 97.544  108.421 1.00 5.81   ? 2667 ASN A CG    1 
ATOM   9524  O  OD1   . ASN A 1 2667 ? 110.762 96.752  107.871 1.00 11.59  ? 2667 ASN A OD1   1 
ATOM   9525  N  ND2   . ASN A 1 2667 ? 110.125 98.859  108.307 1.00 5.44   ? 2667 ASN A ND2   1 
ATOM   9526  N  N     . LEU A 1 2668 ? 108.396 94.629  106.704 1.00 7.24   ? 2668 LEU A N     1 
ATOM   9527  C  CA    . LEU A 1 2668 ? 107.881 94.412  105.353 1.00 7.51   ? 2668 LEU A CA    1 
ATOM   9528  C  C     . LEU A 1 2668 ? 106.553 93.659  105.253 1.00 7.60   ? 2668 LEU A C     1 
ATOM   9529  O  O     . LEU A 1 2668 ? 105.753 93.993  104.369 1.00 9.28   ? 2668 LEU A O     1 
ATOM   9530  C  CB    . LEU A 1 2668 ? 108.914 93.686  104.486 1.00 10.96  ? 2668 LEU A CB    1 
ATOM   9531  C  CG    . LEU A 1 2668 ? 110.078 94.546  103.999 1.00 16.06  ? 2668 LEU A CG    1 
ATOM   9532  C  CD1   . LEU A 1 2668 ? 111.040 93.731  103.156 1.00 14.96  ? 2668 LEU A CD1   1 
ATOM   9533  C  CD2   . LEU A 1 2668 ? 109.535 95.716  103.205 1.00 15.17  ? 2668 LEU A CD2   1 
ATOM   9534  N  N     . PRO A 1 2669 ? 106.272 92.643  106.082 1.00 8.59   ? 2669 PRO A N     1 
ATOM   9535  C  CA    . PRO A 1 2669 ? 105.088 91.808  105.829 1.00 10.16  ? 2669 PRO A CA    1 
ATOM   9536  C  C     . PRO A 1 2669 ? 103.801 92.618  105.754 1.00 8.14   ? 2669 PRO A C     1 
ATOM   9537  O  O     . PRO A 1 2669 ? 103.630 93.622  106.449 1.00 7.13   ? 2669 PRO A O     1 
ATOM   9538  C  CB    . PRO A 1 2669 ? 105.080 90.839  107.015 1.00 7.31   ? 2669 PRO A CB    1 
ATOM   9539  C  CG    . PRO A 1 2669 ? 106.500 90.718  107.385 1.00 8.35   ? 2669 PRO A CG    1 
ATOM   9540  C  CD    . PRO A 1 2669 ? 107.079 92.086  107.185 1.00 6.98   ? 2669 PRO A CD    1 
ATOM   9541  N  N     . ASP A 1 2670 ? 102.901 92.162  104.883 1.00 9.18   ? 2670 ASP A N     1 
ATOM   9542  C  CA    . ASP A 1 2670 ? 101.758 92.959  104.458 1.00 9.09   ? 2670 ASP A CA    1 
ATOM   9543  C  C     . ASP A 1 2670 ? 100.895 93.393  105.634 1.00 9.11   ? 2670 ASP A C     1 
ATOM   9544  O  O     . ASP A 1 2670 ? 100.544 92.588  106.502 1.00 7.59   ? 2670 ASP A O     1 
ATOM   9545  C  CB    . ASP A 1 2670 ? 100.913 92.165  103.461 1.00 10.06  ? 2670 ASP A CB    1 
ATOM   9546  C  CG    . ASP A 1 2670 ? 101.507 92.158  102.066 1.00 17.16  ? 2670 ASP A CG    1 
ATOM   9547  O  OD1   . ASP A 1 2670 ? 102.167 93.151  101.695 1.00 21.75  ? 2670 ASP A OD1   1 
ATOM   9548  O  OD2   . ASP A 1 2670 ? 101.315 91.159  101.343 1.00 17.98  ? 2670 ASP A OD2   1 
ATOM   9549  N  N     . MET A 1 2671 ? 100.558 94.677  105.653 1.00 8.91   ? 2671 MET A N     1 
ATOM   9550  C  CA    . MET A 1 2671 ? 99.551  95.214  106.554 1.00 8.19   ? 2671 MET A CA    1 
ATOM   9551  C  C     . MET A 1 2671 ? 98.188  95.067  105.891 1.00 10.15  ? 2671 MET A C     1 
ATOM   9552  O  O     . MET A 1 2671 ? 97.990  95.533  104.764 1.00 14.82  ? 2671 MET A O     1 
ATOM   9553  C  CB    . MET A 1 2671 ? 99.840  96.680  106.874 1.00 10.61  ? 2671 MET A CB    1 
ATOM   9554  C  CG    . MET A 1 2671 ? 98.953  97.269  107.952 1.00 9.86   ? 2671 MET A CG    1 
ATOM   9555  S  SD    . MET A 1 2671 ? 99.768  98.531  108.947 1.00 25.19  ? 2671 MET A SD    1 
ATOM   9556  C  CE    . MET A 1 2671 ? 100.674 97.521  110.111 1.00 9.45   ? 2671 MET A CE    1 
ATOM   9557  N  N     . ASP A 1 2672 ? 97.254  94.418  106.581 1.00 9.44   ? 2672 ASP A N     1 
ATOM   9558  C  CA    . ASP A 1 2672 ? 95.918  94.251  106.033 1.00 8.17   ? 2672 ASP A CA    1 
ATOM   9559  C  C     . ASP A 1 2672 ? 95.190  95.596  106.007 1.00 11.75  ? 2672 ASP A C     1 
ATOM   9560  O  O     . ASP A 1 2672 ? 95.711  96.629  106.437 1.00 12.41  ? 2672 ASP A O     1 
ATOM   9561  C  CB    . ASP A 1 2672 ? 95.146  93.194  106.825 1.00 7.90   ? 2672 ASP A CB    1 
ATOM   9562  C  CG    . ASP A 1 2672 ? 94.908  93.589  108.277 1.00 11.28  ? 2672 ASP A CG    1 
ATOM   9563  O  OD1   . ASP A 1 2672 ? 95.355  94.673  108.705 1.00 13.49  ? 2672 ASP A OD1   1 
ATOM   9564  O  OD2   . ASP A 1 2672 ? 94.264  92.800  108.998 1.00 13.53  ? 2672 ASP A OD2   1 
ATOM   9565  N  N     . LYS A 1 2673 ? 93.958  95.580  105.498 1.00 11.31  ? 2673 LYS A N     1 
ATOM   9566  C  CA    . LYS A 1 2673 ? 93.184  96.810  105.385 1.00 12.01  ? 2673 LYS A CA    1 
ATOM   9567  C  C     . LYS A 1 2673 ? 92.793  97.388  106.738 1.00 12.06  ? 2673 LYS A C     1 
ATOM   9568  O  O     . LYS A 1 2673 ? 92.317  98.527  106.791 1.00 14.19  ? 2673 LYS A O     1 
ATOM   9569  C  CB    . LYS A 1 2673 ? 91.934  96.568  104.537 1.00 12.48  ? 2673 LYS A CB    1 
ATOM   9570  C  CG    . LYS A 1 2673 ? 91.021  95.482  105.070 1.00 16.95  ? 2673 LYS A CG    1 
ATOM   9571  C  CD    . LYS A 1 2673 ? 89.721  95.417  104.286 1.00 18.91  ? 2673 LYS A CD    1 
ATOM   9572  C  CE    . LYS A 1 2673 ? 89.949  94.885  102.882 1.00 25.71  ? 2673 LYS A CE    1 
ATOM   9573  N  NZ    . LYS A 1 2673 ? 88.666  94.626  102.173 1.00 31.59  ? 2673 LYS A NZ    1 
ATOM   9574  N  N     . TYR A 1 2674 ? 92.979  96.639  107.825 1.00 11.62  ? 2674 TYR A N     1 
ATOM   9575  C  CA    . TYR A 1 2674 ? 92.668  97.107  109.169 1.00 10.67  ? 2674 TYR A CA    1 
ATOM   9576  C  C     . TYR A 1 2674 ? 93.920  97.390  109.994 1.00 11.94  ? 2674 TYR A C     1 
ATOM   9577  O  O     . TYR A 1 2674 ? 93.868  97.351  111.227 1.00 11.67  ? 2674 TYR A O     1 
ATOM   9578  C  CB    . TYR A 1 2674 ? 91.774  96.094  109.882 1.00 10.31  ? 2674 TYR A CB    1 
ATOM   9579  C  CG    . TYR A 1 2674 ? 90.615  95.623  109.036 1.00 12.43  ? 2674 TYR A CG    1 
ATOM   9580  C  CD1   . TYR A 1 2674 ? 89.564  96.477  108.730 1.00 12.06  ? 2674 TYR A CD1   1 
ATOM   9581  C  CD2   . TYR A 1 2674 ? 90.576  94.329  108.536 1.00 10.97  ? 2674 TYR A CD2   1 
ATOM   9582  C  CE1   . TYR A 1 2674 ? 88.503  96.053  107.957 1.00 11.28  ? 2674 TYR A CE1   1 
ATOM   9583  C  CE2   . TYR A 1 2674 ? 89.518  93.897  107.764 1.00 12.73  ? 2674 TYR A CE2   1 
ATOM   9584  C  CZ    . TYR A 1 2674 ? 88.485  94.762  107.476 1.00 14.74  ? 2674 TYR A CZ    1 
ATOM   9585  O  OH    . TYR A 1 2674 ? 87.430  94.335  106.704 1.00 18.40  ? 2674 TYR A OH    1 
ATOM   9586  N  N     . GLY A 1 2675 ? 95.045  97.662  109.337 1.00 11.26  ? 2675 GLY A N     1 
ATOM   9587  C  CA    . GLY A 1 2675 ? 96.232  98.114  110.038 1.00 12.07  ? 2675 GLY A CA    1 
ATOM   9588  C  C     . GLY A 1 2675 ? 96.942  97.070  110.871 1.00 8.76   ? 2675 GLY A C     1 
ATOM   9589  O  O     . GLY A 1 2675 ? 97.637  97.424  111.828 1.00 8.33   ? 2675 GLY A O     1 
ATOM   9590  N  N     . THR A 1 2676 ? 96.791  95.790  110.539 1.00 7.43   ? 2676 THR A N     1 
ATOM   9591  C  CA    . THR A 1 2676 ? 97.371  94.708  111.324 1.00 7.82   ? 2676 THR A CA    1 
ATOM   9592  C  C     . THR A 1 2676 ? 98.332  93.892  110.472 1.00 7.51   ? 2676 THR A C     1 
ATOM   9593  O  O     . THR A 1 2676 ? 97.997  93.501  109.349 1.00 6.64   ? 2676 THR A O     1 
ATOM   9594  C  CB    . THR A 1 2676 ? 96.280  93.796  111.894 1.00 7.97   ? 2676 THR A CB    1 
ATOM   9595  O  OG1   . THR A 1 2676 ? 95.381  94.567  112.699 1.00 16.02  ? 2676 THR A OG1   1 
ATOM   9596  C  CG2   . THR A 1 2676 ? 96.896  92.696  112.746 1.00 6.00   ? 2676 THR A CG2   1 
ATOM   9597  N  N     . GLN A 1 2677 ? 99.524  93.641  111.009 1.00 7.43   ? 2677 GLN A N     1 
ATOM   9598  C  CA    . GLN A 1 2677 ? 100.449 92.657  110.463 1.00 5.67   ? 2677 GLN A CA    1 
ATOM   9599  C  C     . GLN A 1 2677 ? 100.371 91.409  111.334 1.00 4.48   ? 2677 GLN A C     1 
ATOM   9600  O  O     . GLN A 1 2677 ? 100.653 91.472  112.536 1.00 5.43   ? 2677 GLN A O     1 
ATOM   9601  C  CB    . GLN A 1 2677 ? 101.878 93.199  110.424 1.00 4.40   ? 2677 GLN A CB    1 
ATOM   9602  C  CG    . GLN A 1 2677 ? 102.109 94.307  109.410 1.00 5.22   ? 2677 GLN A CG    1 
ATOM   9603  C  CD    . GLN A 1 2677 ? 103.390 95.078  109.672 1.00 5.03   ? 2677 GLN A CD    1 
ATOM   9604  O  OE1   . GLN A 1 2677 ? 104.341 95.009  108.892 1.00 4.88   ? 2677 GLN A OE1   1 
ATOM   9605  N  NE2   . GLN A 1 2677 ? 103.426 95.810  110.778 1.00 5.68   ? 2677 GLN A NE2   1 
ATOM   9606  N  N     . ARG A 1 2678 ? 99.985  90.282  110.731 1.00 3.44   ? 2678 ARG A N     1 
ATOM   9607  C  CA    . ARG A 1 2678 ? 99.746  89.071  111.512 1.00 3.11   ? 2678 ARG A CA    1 
ATOM   9608  C  C     . ARG A 1 2678 ? 101.015 88.589  112.202 1.00 2.95   ? 2678 ARG A C     1 
ATOM   9609  O  O     . ARG A 1 2678 ? 100.981 88.195  113.375 1.00 3.11   ? 2678 ARG A O     1 
ATOM   9610  C  CB    . ARG A 1 2678 ? 99.172  87.970  110.619 1.00 4.22   ? 2678 ARG A CB    1 
ATOM   9611  C  CG    . ARG A 1 2678 ? 98.906  86.664  111.353 1.00 4.58   ? 2678 ARG A CG    1 
ATOM   9612  C  CD    . ARG A 1 2678 ? 98.337  85.601  110.429 1.00 6.23   ? 2678 ARG A CD    1 
ATOM   9613  N  NE    . ARG A 1 2678 ? 97.047  85.988  109.872 1.00 9.96   ? 2678 ARG A NE    1 
ATOM   9614  C  CZ    . ARG A 1 2678 ? 96.376  85.280  108.974 1.00 9.59   ? 2678 ARG A CZ    1 
ATOM   9615  N  NH1   . ARG A 1 2678 ? 96.844  84.133  108.509 1.00 11.43  ? 2678 ARG A NH1   1 
ATOM   9616  N  NH2   . ARG A 1 2678 ? 95.206  85.732  108.533 1.00 10.22  ? 2678 ARG A NH2   1 
ATOM   9617  N  N     . VAL A 1 2679 ? 102.147 88.610  111.494 1.00 3.15   ? 2679 VAL A N     1 
ATOM   9618  C  CA    . VAL A 1 2679 ? 103.390 88.137  112.092 1.00 3.06   ? 2679 VAL A CA    1 
ATOM   9619  C  C     . VAL A 1 2679 ? 103.835 89.057  113.225 1.00 2.12   ? 2679 VAL A C     1 
ATOM   9620  O  O     . VAL A 1 2679 ? 104.380 88.588  114.230 1.00 1.62   ? 2679 VAL A O     1 
ATOM   9621  C  CB    . VAL A 1 2679 ? 104.480 87.968  111.013 1.00 5.36   ? 2679 VAL A CB    1 
ATOM   9622  C  CG1   . VAL A 1 2679 ? 104.955 89.315  110.484 1.00 4.76   ? 2679 VAL A CG1   1 
ATOM   9623  C  CG2   . VAL A 1 2679 ? 105.648 87.158  111.558 1.00 3.59   ? 2679 VAL A CG2   1 
ATOM   9624  N  N     . ILE A 1 2680 ? 103.606 90.368  113.100 1.00 2.42   ? 2680 ILE A N     1 
ATOM   9625  C  CA    . ILE A 1 2680 ? 103.943 91.282  114.189 1.00 2.60   ? 2680 ILE A CA    1 
ATOM   9626  C  C     . ILE A 1 2680 ? 103.085 90.997  115.413 1.00 2.17   ? 2680 ILE A C     1 
ATOM   9627  O  O     . ILE A 1 2680 ? 103.581 90.998  116.545 1.00 2.44   ? 2680 ILE A O     1 
ATOM   9628  C  CB    . ILE A 1 2680 ? 103.810 92.746  113.733 1.00 3.27   ? 2680 ILE A CB    1 
ATOM   9629  C  CG1   . ILE A 1 2680 ? 104.765 93.031  112.576 1.00 3.58   ? 2680 ILE A CG1   1 
ATOM   9630  C  CG2   . ILE A 1 2680 ? 104.078 93.694  114.891 1.00 2.47   ? 2680 ILE A CG2   1 
ATOM   9631  C  CD1   . ILE A 1 2680 ? 106.214 92.744  112.895 1.00 5.04   ? 2680 ILE A CD1   1 
ATOM   9632  N  N     . SER A 1 2681 ? 101.787 90.755  115.213 1.00 1.94   ? 2681 SER A N     1 
ATOM   9633  C  CA    . SER A 1 2681 ? 100.927 90.392  116.334 1.00 2.96   ? 2681 SER A CA    1 
ATOM   9634  C  C     . SER A 1 2681 ? 101.390 89.092  116.979 1.00 2.35   ? 2681 SER A C     1 
ATOM   9635  O  O     . SER A 1 2681 ? 101.378 88.959  118.207 1.00 3.01   ? 2681 SER A O     1 
ATOM   9636  C  CB    . SER A 1 2681 ? 99.475  90.270  115.868 1.00 2.90   ? 2681 SER A CB    1 
ATOM   9637  O  OG    . SER A 1 2681 ? 98.982  91.512  115.401 1.00 9.32   ? 2681 SER A OG    1 
ATOM   9638  N  N     . PHE A 1 2682 ? 101.810 88.126  116.161 1.00 1.59   ? 2682 PHE A N     1 
ATOM   9639  C  CA    . PHE A 1 2682 ? 102.272 86.846  116.689 1.00 1.83   ? 2682 PHE A CA    1 
ATOM   9640  C  C     . PHE A 1 2682 ? 103.546 87.017  117.515 1.00 1.72   ? 2682 PHE A C     1 
ATOM   9641  O  O     . PHE A 1 2682 ? 103.685 86.428  118.597 1.00 1.68   ? 2682 PHE A O     1 
ATOM   9642  C  CB    . PHE A 1 2682 ? 102.492 85.877  115.528 1.00 2.03   ? 2682 PHE A CB    1 
ATOM   9643  C  CG    . PHE A 1 2682 ? 102.751 84.467  115.950 1.00 2.59   ? 2682 PHE A CG    1 
ATOM   9644  C  CD1   . PHE A 1 2682 ? 101.705 83.655  116.352 1.00 3.62   ? 2682 PHE A CD1   1 
ATOM   9645  C  CD2   . PHE A 1 2682 ? 104.030 83.945  115.935 1.00 3.53   ? 2682 PHE A CD2   1 
ATOM   9646  C  CE1   . PHE A 1 2682 ? 101.931 82.352  116.736 1.00 4.56   ? 2682 PHE A CE1   1 
ATOM   9647  C  CE2   . PHE A 1 2682 ? 104.262 82.643  116.322 1.00 2.67   ? 2682 PHE A CE2   1 
ATOM   9648  C  CZ    . PHE A 1 2682 ? 103.210 81.846  116.722 1.00 2.40   ? 2682 PHE A CZ    1 
ATOM   9649  N  N     . ILE A 1 2683 ? 104.483 87.832  117.023 1.00 1.31   ? 2683 ILE A N     1 
ATOM   9650  C  CA    . ILE A 1 2683 ? 105.722 88.082  117.756 1.00 1.65   ? 2683 ILE A CA    1 
ATOM   9651  C  C     . ILE A 1 2683 ? 105.438 88.850  119.041 1.00 2.21   ? 2683 ILE A C     1 
ATOM   9652  O  O     . ILE A 1 2683 ? 106.054 88.595  120.081 1.00 2.21   ? 2683 ILE A O     1 
ATOM   9653  C  CB    . ILE A 1 2683 ? 106.740 88.818  116.866 1.00 1.95   ? 2683 ILE A CB    1 
ATOM   9654  C  CG1   . ILE A 1 2683 ? 107.057 87.989  115.620 1.00 1.47   ? 2683 ILE A CG1   1 
ATOM   9655  C  CG2   . ILE A 1 2683 ? 108.013 89.120  117.643 1.00 1.19   ? 2683 ILE A CG2   1 
ATOM   9656  C  CD1   . ILE A 1 2683 ? 107.898 88.718  114.595 1.00 1.73   ? 2683 ILE A CD1   1 
ATOM   9657  N  N     . ARG A 1 2684 ? 104.507 89.807  118.989 1.00 2.27   ? 2684 ARG A N     1 
ATOM   9658  C  CA    . ARG A 1 2684 ? 104.103 90.505  120.204 1.00 2.22   ? 2684 ARG A CA    1 
ATOM   9659  C  C     . ARG A 1 2684 ? 103.520 89.535  121.219 1.00 2.65   ? 2684 ARG A C     1 
ATOM   9660  O  O     . ARG A 1 2684 ? 103.795 89.640  122.419 1.00 3.95   ? 2684 ARG A O     1 
ATOM   9661  C  CB    . ARG A 1 2684 ? 103.081 91.596  119.888 1.00 2.99   ? 2684 ARG A CB    1 
ATOM   9662  C  CG    . ARG A 1 2684 ? 102.539 92.257  121.145 1.00 5.09   ? 2684 ARG A CG    1 
ATOM   9663  C  CD    . ARG A 1 2684 ? 101.337 93.137  120.884 1.00 5.39   ? 2684 ARG A CD    1 
ATOM   9664  N  NE    . ARG A 1 2684 ? 100.826 93.695  122.130 1.00 11.28  ? 2684 ARG A NE    1 
ATOM   9665  C  CZ    . ARG A 1 2684 ? 99.605  93.487  122.605 1.00 9.03   ? 2684 ARG A CZ    1 
ATOM   9666  N  NH1   . ARG A 1 2684 ? 98.729  92.738  121.956 1.00 7.85   ? 2684 ARG A NH1   1 
ATOM   9667  N  NH2   . ARG A 1 2684 ? 99.256  94.043  123.762 1.00 6.09   ? 2684 ARG A NH2   1 
ATOM   9668  N  N     . GLN A 1 2685 ? 102.694 88.596  120.755 1.00 2.19   ? 2685 GLN A N     1 
ATOM   9669  C  CA    . GLN A 1 2685 ? 102.121 87.604  121.654 1.00 2.54   ? 2685 GLN A CA    1 
ATOM   9670  C  C     . GLN A 1 2685 ? 103.214 86.768  122.306 1.00 3.04   ? 2685 GLN A C     1 
ATOM   9671  O  O     . GLN A 1 2685 ? 103.198 86.547  123.523 1.00 3.03   ? 2685 GLN A O     1 
ATOM   9672  C  CB    . GLN A 1 2685 ? 101.135 86.717  120.892 1.00 2.33   ? 2685 GLN A CB    1 
ATOM   9673  C  CG    . GLN A 1 2685 ? 100.646 85.510  121.671 1.00 2.56   ? 2685 GLN A CG    1 
ATOM   9674  C  CD    . GLN A 1 2685 ? 99.705  84.640  120.861 1.00 3.27   ? 2685 GLN A CD    1 
ATOM   9675  O  OE1   . GLN A 1 2685 ? 100.062 84.147  119.792 1.00 3.95   ? 2685 GLN A OE1   1 
ATOM   9676  N  NE2   . GLN A 1 2685 ? 98.493  84.450  121.367 1.00 3.11   ? 2685 GLN A NE2   1 
ATOM   9677  N  N     . MET A 1 2686 ? 104.193 86.320  121.515 1.00 2.81   ? 2686 MET A N     1 
ATOM   9678  C  CA    . MET A 1 2686 ? 105.280 85.531  122.090 1.00 3.10   ? 2686 MET A CA    1 
ATOM   9679  C  C     . MET A 1 2686 ? 106.089 86.347  123.092 1.00 4.67   ? 2686 MET A C     1 
ATOM   9680  O  O     . MET A 1 2686 ? 106.464 85.841  124.155 1.00 5.31   ? 2686 MET A O     1 
ATOM   9681  C  CB    . MET A 1 2686 ? 106.199 84.981  120.999 1.00 2.83   ? 2686 MET A CB    1 
ATOM   9682  C  CG    . MET A 1 2686 ? 105.559 83.955  120.083 1.00 3.72   ? 2686 MET A CG    1 
ATOM   9683  S  SD    . MET A 1 2686 ? 106.729 83.303  118.874 1.00 12.39  ? 2686 MET A SD    1 
ATOM   9684  C  CE    . MET A 1 2686 ? 106.882 84.682  117.748 1.00 5.19   ? 2686 MET A CE    1 
ATOM   9685  N  N     . VAL A 1 2687 ? 106.362 87.612  122.775 1.00 4.19   ? 2687 VAL A N     1 
ATOM   9686  C  CA    . VAL A 1 2687 ? 107.214 88.430  123.630 1.00 5.10   ? 2687 VAL A CA    1 
ATOM   9687  C  C     . VAL A 1 2687 ? 106.511 88.780  124.937 1.00 6.73   ? 2687 VAL A C     1 
ATOM   9688  O  O     . VAL A 1 2687 ? 107.107 88.690  126.017 1.00 9.17   ? 2687 VAL A O     1 
ATOM   9689  C  CB    . VAL A 1 2687 ? 107.661 89.692  122.869 1.00 6.75   ? 2687 VAL A CB    1 
ATOM   9690  C  CG1   . VAL A 1 2687 ? 108.188 90.735  123.834 1.00 9.95   ? 2687 VAL A CG1   1 
ATOM   9691  C  CG2   . VAL A 1 2687 ? 108.714 89.339  121.829 1.00 4.62   ? 2687 VAL A CG2   1 
ATOM   9692  N  N     . GLU A 1 2688 ? 105.237 89.171  124.871 1.00 6.13   ? 2688 GLU A N     1 
ATOM   9693  C  CA    . GLU A 1 2688 ? 104.544 89.644  126.063 1.00 6.84   ? 2688 GLU A CA    1 
ATOM   9694  C  C     . GLU A 1 2688 ? 103.971 88.505  126.895 1.00 5.75   ? 2688 GLU A C     1 
ATOM   9695  O  O     . GLU A 1 2688 ? 104.121 88.508  128.122 1.00 7.80   ? 2688 GLU A O     1 
ATOM   9696  C  CB    . GLU A 1 2688 ? 103.428 90.614  125.670 1.00 6.00   ? 2688 GLU A CB    1 
ATOM   9697  C  CG    . GLU A 1 2688 ? 102.694 91.226  126.851 1.00 10.79  ? 2688 GLU A CG    1 
ATOM   9698  C  CD    . GLU A 1 2688 ? 101.633 92.219  126.426 1.00 12.32  ? 2688 GLU A CD    1 
ATOM   9699  O  OE1   . GLU A 1 2688 ? 101.457 92.414  125.205 1.00 18.16  ? 2688 GLU A OE1   1 
ATOM   9700  O  OE2   . GLU A 1 2688 ? 100.978 92.806  127.310 1.00 13.55  ? 2688 GLU A OE2   1 
ATOM   9701  N  N     . HIS A 1 2689 ? 103.317 87.532  126.263 1.00 4.06   ? 2689 HIS A N     1 
ATOM   9702  C  CA    . HIS A 1 2689 ? 102.696 86.427  126.977 1.00 4.99   ? 2689 HIS A CA    1 
ATOM   9703  C  C     . HIS A 1 2689 ? 103.627 85.238  127.154 1.00 4.32   ? 2689 HIS A C     1 
ATOM   9704  O  O     . HIS A 1 2689 ? 103.251 84.268  127.820 1.00 5.79   ? 2689 HIS A O     1 
ATOM   9705  C  CB    . HIS A 1 2689 ? 101.420 85.993  126.248 1.00 4.15   ? 2689 HIS A CB    1 
ATOM   9706  C  CG    . HIS A 1 2689 ? 100.387 87.072  126.155 1.00 4.95   ? 2689 HIS A CG    1 
ATOM   9707  N  ND1   . HIS A 1 2689 ? 100.231 88.036  127.127 1.00 6.99   ? 2689 HIS A ND1   1 
ATOM   9708  C  CD2   . HIS A 1 2689 ? 99.476  87.355  125.195 1.00 6.45   ? 2689 HIS A CD2   1 
ATOM   9709  C  CE1   . HIS A 1 2689 ? 99.257  88.857  126.778 1.00 6.28   ? 2689 HIS A CE1   1 
ATOM   9710  N  NE2   . HIS A 1 2689 ? 98.784  88.468  125.608 1.00 7.42   ? 2689 HIS A NE2   1 
ATOM   9711  N  N     . GLY A 1 2690 ? 104.827 85.285  126.582 1.00 4.53   ? 2690 GLY A N     1 
ATOM   9712  C  CA    . GLY A 1 2690 ? 105.774 84.203  126.750 1.00 4.44   ? 2690 GLY A CA    1 
ATOM   9713  C  C     . GLY A 1 2690 ? 105.453 82.946  125.978 1.00 4.19   ? 2690 GLY A C     1 
ATOM   9714  O  O     . GLY A 1 2690 ? 105.993 81.884  126.294 1.00 7.35   ? 2690 GLY A O     1 
ATOM   9715  N  N     . GLY A 1 2691 ? 104.590 83.030  124.971 1.00 2.72   ? 2691 GLY A N     1 
ATOM   9716  C  CA    . GLY A 1 2691 ? 104.241 81.848  124.207 1.00 3.07   ? 2691 GLY A CA    1 
ATOM   9717  C  C     . GLY A 1 2691 ? 103.227 82.170  123.128 1.00 2.77   ? 2691 GLY A C     1 
ATOM   9718  O  O     . GLY A 1 2691 ? 103.041 83.328  122.752 1.00 3.02   ? 2691 GLY A O     1 
ATOM   9719  N  N     . PHE A 1 2692 ? 102.574 81.119  122.645 1.00 2.42   ? 2692 PHE A N     1 
ATOM   9720  C  CA    . PHE A 1 2692 ? 101.595 81.236  121.571 1.00 2.52   ? 2692 PHE A CA    1 
ATOM   9721  C  C     . PHE A 1 2692 ? 100.643 80.050  121.661 1.00 2.65   ? 2692 PHE A C     1 
ATOM   9722  O  O     . PHE A 1 2692 ? 100.666 79.284  122.626 1.00 3.34   ? 2692 PHE A O     1 
ATOM   9723  C  CB    . PHE A 1 2692 ? 102.277 81.308  120.200 1.00 3.17   ? 2692 PHE A CB    1 
ATOM   9724  C  CG    . PHE A 1 2692 ? 103.019 80.056  119.824 1.00 3.01   ? 2692 PHE A CG    1 
ATOM   9725  C  CD1   . PHE A 1 2692 ? 104.307 79.834  120.283 1.00 3.23   ? 2692 PHE A CD1   1 
ATOM   9726  C  CD2   . PHE A 1 2692 ? 102.432 79.105  119.006 1.00 2.51   ? 2692 PHE A CD2   1 
ATOM   9727  C  CE1   . PHE A 1 2692 ? 104.989 78.682  119.942 1.00 4.45   ? 2692 PHE A CE1   1 
ATOM   9728  C  CE2   . PHE A 1 2692 ? 103.110 77.954  118.660 1.00 3.42   ? 2692 PHE A CE2   1 
ATOM   9729  C  CZ    . PHE A 1 2692 ? 104.390 77.742  119.127 1.00 3.37   ? 2692 PHE A CZ    1 
ATOM   9730  N  N     . TYR A 1 2693 ? 99.790  79.911  120.652 1.00 3.16   ? 2693 TYR A N     1 
ATOM   9731  C  CA    . TYR A 1 2693 ? 98.843  78.807  120.585 1.00 3.19   ? 2693 TYR A CA    1 
ATOM   9732  C  C     . TYR A 1 2693 ? 99.180  77.888  119.419 1.00 5.59   ? 2693 TYR A C     1 
ATOM   9733  O  O     . TYR A 1 2693 ? 99.213  78.325  118.264 1.00 7.30   ? 2693 TYR A O     1 
ATOM   9734  C  CB    . TYR A 1 2693 ? 97.409  79.320  120.448 1.00 3.05   ? 2693 TYR A CB    1 
ATOM   9735  C  CG    . TYR A 1 2693 ? 96.779  79.741  121.755 1.00 2.88   ? 2693 TYR A CG    1 
ATOM   9736  C  CD1   . TYR A 1 2693 ? 96.315  78.795  122.658 1.00 2.74   ? 2693 TYR A CD1   1 
ATOM   9737  C  CD2   . TYR A 1 2693 ? 96.644  81.082  122.083 1.00 3.19   ? 2693 TYR A CD2   1 
ATOM   9738  C  CE1   . TYR A 1 2693 ? 95.736  79.172  123.853 1.00 3.06   ? 2693 TYR A CE1   1 
ATOM   9739  C  CE2   . TYR A 1 2693 ? 96.064  81.470  123.275 1.00 3.38   ? 2693 TYR A CE2   1 
ATOM   9740  C  CZ    . TYR A 1 2693 ? 95.614  80.511  124.156 1.00 3.83   ? 2693 TYR A CZ    1 
ATOM   9741  O  OH    . TYR A 1 2693 ? 95.038  80.893  125.345 1.00 2.83   ? 2693 TYR A OH    1 
ATOM   9742  N  N     . ARG A 1 2694 ? 99.431  76.620  119.729 1.00 7.39   ? 2694 ARG A N     1 
ATOM   9743  C  CA    . ARG A 1 2694 ? 99.508  75.576  118.719 1.00 7.85   ? 2694 ARG A CA    1 
ATOM   9744  C  C     . ARG A 1 2694 ? 98.091  75.261  118.258 1.00 8.86   ? 2694 ARG A C     1 
ATOM   9745  O  O     . ARG A 1 2694 ? 97.250  74.833  119.060 1.00 12.27  ? 2694 ARG A O     1 
ATOM   9746  C  CB    . ARG A 1 2694 ? 100.193 74.334  119.285 1.00 8.51   ? 2694 ARG A CB    1 
ATOM   9747  C  CG    . ARG A 1 2694 ? 100.683 73.355  118.233 1.00 12.24  ? 2694 ARG A CG    1 
ATOM   9748  C  CD    . ARG A 1 2694 ? 100.650 71.923  118.742 1.00 12.24  ? 2694 ARG A CD    1 
ATOM   9749  N  NE    . ARG A 1 2694 ? 101.853 71.560  119.480 1.00 12.22  ? 2694 ARG A NE    1 
ATOM   9750  C  CZ    . ARG A 1 2694 ? 101.857 70.852  120.602 1.00 11.41  ? 2694 ARG A CZ    1 
ATOM   9751  N  NH1   . ARG A 1 2694 ? 100.735 70.404  121.140 1.00 10.18  ? 2694 ARG A NH1   1 
ATOM   9752  N  NH2   . ARG A 1 2694 ? 103.016 70.582  121.194 1.00 14.59  ? 2694 ARG A NH2   1 
ATOM   9753  N  N     . THR A 1 2695 ? 97.826  75.492  116.971 1.00 8.98   ? 2695 THR A N     1 
ATOM   9754  C  CA    . THR A 1 2695 ? 96.477  75.416  116.426 1.00 10.06  ? 2695 THR A CA    1 
ATOM   9755  C  C     . THR A 1 2695 ? 96.057  74.004  116.043 1.00 12.66  ? 2695 THR A C     1 
ATOM   9756  O  O     . THR A 1 2695 ? 94.876  73.791  115.750 1.00 17.00  ? 2695 THR A O     1 
ATOM   9757  C  CB    . THR A 1 2695 ? 96.351  76.330  115.204 1.00 12.05  ? 2695 THR A CB    1 
ATOM   9758  O  OG1   . THR A 1 2695 ? 97.301  75.934  114.207 1.00 19.17  ? 2695 THR A OG1   1 
ATOM   9759  C  CG2   . THR A 1 2695 ? 96.606  77.778  115.592 1.00 9.14   ? 2695 THR A CG2   1 
ATOM   9760  N  N     . SER A 1 2696 ? 96.982  73.042  116.026 1.00 14.88  ? 2696 SER A N     1 
ATOM   9761  C  CA    . SER A 1 2696 ? 96.598  71.666  115.724 1.00 16.53  ? 2696 SER A CA    1 
ATOM   9762  C  C     . SER A 1 2696 ? 95.675  71.106  116.799 1.00 16.91  ? 2696 SER A C     1 
ATOM   9763  O  O     . SER A 1 2696 ? 94.697  70.417  116.489 1.00 22.11  ? 2696 SER A O     1 
ATOM   9764  C  CB    . SER A 1 2696 ? 97.841  70.791  115.569 1.00 21.53  ? 2696 SER A CB    1 
ATOM   9765  O  OG    . SER A 1 2696 ? 98.481  70.586  116.815 1.00 21.41  ? 2696 SER A OG    1 
ATOM   9766  N  N     . ASP A 1 2697 ? 95.969  71.394  118.069 1.00 11.91  ? 2697 ASP A N     1 
ATOM   9767  C  CA    . ASP A 1 2697 ? 95.118  70.974  119.174 1.00 14.51  ? 2697 ASP A CA    1 
ATOM   9768  C  C     . ASP A 1 2697 ? 94.722  72.138  120.075 1.00 14.91  ? 2697 ASP A C     1 
ATOM   9769  O  O     . ASP A 1 2697 ? 94.234  71.904  121.187 1.00 13.74  ? 2697 ASP A O     1 
ATOM   9770  C  CB    . ASP A 1 2697 ? 95.806  69.881  120.000 1.00 16.56  ? 2697 ASP A CB    1 
ATOM   9771  C  CG    . ASP A 1 2697 ? 97.057  70.375  120.691 1.00 17.50  ? 2697 ASP A CG    1 
ATOM   9772  O  OD1   . ASP A 1 2697 ? 97.864  71.061  120.033 1.00 17.37  ? 2697 ASP A OD1   1 
ATOM   9773  O  OD2   . ASP A 1 2697 ? 97.236  70.071  121.889 1.00 19.82  ? 2697 ASP A OD2   1 
ATOM   9774  N  N     . GLN A 1 2698 ? 94.924  73.379  119.624 1.00 11.81  ? 2698 GLN A N     1 
ATOM   9775  C  CA    . GLN A 1 2698 ? 94.475  74.576  120.341 1.00 12.58  ? 2698 GLN A CA    1 
ATOM   9776  C  C     . GLN A 1 2698 ? 95.084  74.661  121.738 1.00 9.22   ? 2698 GLN A C     1 
ATOM   9777  O  O     . GLN A 1 2698 ? 94.406  75.008  122.707 1.00 11.98  ? 2698 GLN A O     1 
ATOM   9778  C  CB    . GLN A 1 2698 ? 92.946  74.636  120.421 1.00 8.99   ? 2698 GLN A CB    1 
ATOM   9779  C  CG    . GLN A 1 2698 ? 92.238  74.965  119.114 1.00 6.74   ? 2698 GLN A CG    1 
ATOM   9780  C  CD    . GLN A 1 2698 ? 92.320  73.844  118.099 1.00 14.96  ? 2698 GLN A CD    1 
ATOM   9781  O  OE1   . GLN A 1 2698 ? 91.850  72.733  118.345 1.00 20.70  ? 2698 GLN A OE1   1 
ATOM   9782  N  NE2   . GLN A 1 2698 ? 92.917  74.129  116.949 1.00 19.06  ? 2698 GLN A NE2   1 
ATOM   9783  N  N     . THR A 1 2699 ? 96.371  74.347  121.853 1.00 8.90   ? 2699 THR A N     1 
ATOM   9784  C  CA    . THR A 1 2699 ? 97.022  74.286  123.155 1.00 8.75   ? 2699 THR A CA    1 
ATOM   9785  C  C     . THR A 1 2699 ? 98.018  75.428  123.319 1.00 5.64   ? 2699 THR A C     1 
ATOM   9786  O  O     . THR A 1 2699 ? 98.647  75.871  122.357 1.00 4.27   ? 2699 THR A O     1 
ATOM   9787  C  CB    . THR A 1 2699 ? 97.728  72.938  123.362 1.00 11.62  ? 2699 THR A CB    1 
ATOM   9788  O  OG1   . THR A 1 2699 ? 98.103  72.799  124.738 1.00 14.44  ? 2699 THR A OG1   1 
ATOM   9789  C  CG2   . THR A 1 2699 ? 98.969  72.829  122.492 1.00 11.47  ? 2699 THR A CG2   1 
ATOM   9790  N  N     . TRP A 1 2700 ? 98.148  75.917  124.548 1.00 4.91   ? 2700 TRP A N     1 
ATOM   9791  C  CA    . TRP A 1 2700 ? 99.093  76.992  124.817 1.00 3.99   ? 2700 TRP A CA    1 
ATOM   9792  C  C     . TRP A 1 2700 ? 100.501 76.427  124.941 1.00 4.05   ? 2700 TRP A C     1 
ATOM   9793  O  O     . TRP A 1 2700 ? 100.728 75.452  125.665 1.00 5.82   ? 2700 TRP A O     1 
ATOM   9794  C  CB    . TRP A 1 2700 ? 98.715  77.750  126.088 1.00 3.44   ? 2700 TRP A CB    1 
ATOM   9795  C  CG    . TRP A 1 2700 ? 99.686  78.842  126.415 1.00 4.36   ? 2700 TRP A CG    1 
ATOM   9796  C  CD1   . TRP A 1 2700 ? 100.675 78.808  127.353 1.00 3.03   ? 2700 TRP A CD1   1 
ATOM   9797  C  CD2   . TRP A 1 2700 ? 99.768  80.130  125.792 1.00 2.72   ? 2700 TRP A CD2   1 
ATOM   9798  N  NE1   . TRP A 1 2700 ? 101.365 79.995  127.356 1.00 2.45   ? 2700 TRP A NE1   1 
ATOM   9799  C  CE2   . TRP A 1 2700 ? 100.828 80.824  126.407 1.00 2.47   ? 2700 TRP A CE2   1 
ATOM   9800  C  CE3   . TRP A 1 2700 ? 99.046  80.764  124.777 1.00 1.85   ? 2700 TRP A CE3   1 
ATOM   9801  C  CZ2   . TRP A 1 2700 ? 101.183 82.120  126.041 1.00 2.76   ? 2700 TRP A CZ2   1 
ATOM   9802  C  CZ3   . TRP A 1 2700 ? 99.401  82.050  124.414 1.00 2.21   ? 2700 TRP A CZ3   1 
ATOM   9803  C  CH2   . TRP A 1 2700 ? 100.459 82.714  125.044 1.00 2.61   ? 2700 TRP A CH2   1 
ATOM   9804  N  N     . VAL A 1 2701 ? 101.445 77.040  124.233 1.00 3.29   ? 2701 VAL A N     1 
ATOM   9805  C  CA    . VAL A 1 2701 ? 102.844 76.635  124.237 1.00 3.70   ? 2701 VAL A CA    1 
ATOM   9806  C  C     . VAL A 1 2701 ? 103.663 77.791  124.790 1.00 3.40   ? 2701 VAL A C     1 
ATOM   9807  O  O     . VAL A 1 2701 ? 103.528 78.930  124.328 1.00 3.92   ? 2701 VAL A O     1 
ATOM   9808  C  CB    . VAL A 1 2701 ? 103.326 76.250  122.826 1.00 4.49   ? 2701 VAL A CB    1 
ATOM   9809  C  CG1   . VAL A 1 2701 ? 104.814 75.946  122.838 1.00 3.64   ? 2701 VAL A CG1   1 
ATOM   9810  C  CG2   . VAL A 1 2701 ? 102.529 75.072  122.291 1.00 5.15   ? 2701 VAL A CG2   1 
ATOM   9811  N  N     . LYS A 1 2702 ? 104.507 77.497  125.775 1.00 4.13   ? 2702 LYS A N     1 
ATOM   9812  C  CA    . LYS A 1 2702 ? 105.361 78.489  126.413 1.00 3.73   ? 2702 LYS A CA    1 
ATOM   9813  C  C     . LYS A 1 2702 ? 106.769 78.401  125.838 1.00 2.94   ? 2702 LYS A C     1 
ATOM   9814  O  O     . LYS A 1 2702 ? 107.346 77.313  125.761 1.00 3.83   ? 2702 LYS A O     1 
ATOM   9815  C  CB    . LYS A 1 2702 ? 105.397 78.273  127.927 1.00 4.77   ? 2702 LYS A CB    1 
ATOM   9816  C  CG    . LYS A 1 2702 ? 106.200 79.310  128.692 1.00 9.66   ? 2702 LYS A CG    1 
ATOM   9817  C  CD    . LYS A 1 2702 ? 106.132 79.056  130.189 1.00 15.10  ? 2702 LYS A CD    1 
ATOM   9818  C  CE    . LYS A 1 2702 ? 106.946 80.078  130.964 1.00 22.26  ? 2702 LYS A CE    1 
ATOM   9819  N  NZ    . LYS A 1 2702 ? 106.887 79.838  132.432 1.00 27.62  ? 2702 LYS A NZ    1 
ATOM   9820  N  N     . LEU A 1 2703 ? 107.313 79.545  125.434 1.00 3.70   ? 2703 LEU A N     1 
ATOM   9821  C  CA    . LEU A 1 2703 ? 108.676 79.603  124.930 1.00 4.91   ? 2703 LEU A CA    1 
ATOM   9822  C  C     . LEU A 1 2703 ? 109.681 79.473  126.069 1.00 4.35   ? 2703 LEU A C     1 
ATOM   9823  O  O     . LEU A 1 2703 ? 109.455 79.951  127.183 1.00 5.26   ? 2703 LEU A O     1 
ATOM   9824  C  CB    . LEU A 1 2703 ? 108.920 80.914  124.182 1.00 4.26   ? 2703 LEU A CB    1 
ATOM   9825  C  CG    . LEU A 1 2703 ? 108.179 81.144  122.866 1.00 5.72   ? 2703 LEU A CG    1 
ATOM   9826  C  CD1   . LEU A 1 2703 ? 108.540 82.502  122.295 1.00 8.36   ? 2703 LEU A CD1   1 
ATOM   9827  C  CD2   . LEU A 1 2703 ? 108.508 80.044  121.871 1.00 5.31   ? 2703 LEU A CD2   1 
ATOM   9828  N  N     . GLU A 1 2704 ? 110.802 78.816  125.777 1.00 4.41   ? 2704 GLU A N     1 
ATOM   9829  C  CA    . GLU A 1 2704 ? 111.912 78.740  126.716 1.00 4.60   ? 2704 GLU A CA    1 
ATOM   9830  C  C     . GLU A 1 2704 ? 113.211 78.943  125.954 1.00 3.93   ? 2704 GLU A C     1 
ATOM   9831  O  O     . GLU A 1 2704 ? 113.427 78.311  124.917 1.00 4.08   ? 2704 GLU A O     1 
ATOM   9832  C  CB    . GLU A 1 2704 ? 111.932 77.396  127.455 1.00 7.87   ? 2704 GLU A CB    1 
ATOM   9833  C  CG    . GLU A 1 2704 ? 113.009 77.295  128.524 1.00 13.16  ? 2704 GLU A CG    1 
ATOM   9834  C  CD    . GLU A 1 2704 ? 113.519 75.879  128.712 1.00 24.46  ? 2704 GLU A CD    1 
ATOM   9835  O  OE1   . GLU A 1 2704 ? 114.730 75.651  128.514 1.00 25.64  ? 2704 GLU A OE1   1 
ATOM   9836  O  OE2   . GLU A 1 2704 ? 112.709 74.994  129.059 1.00 28.43  ? 2704 GLU A OE2   1 
ATOM   9837  N  N     . ARG A 1 2705 ? 114.064 79.831  126.470 1.00 5.06   ? 2705 ARG A N     1 
ATOM   9838  C  CA    . ARG A 1 2705 ? 115.386 80.100  125.899 1.00 3.76   ? 2705 ARG A CA    1 
ATOM   9839  C  C     . ARG A 1 2705 ? 115.304 80.521  124.431 1.00 3.64   ? 2705 ARG A C     1 
ATOM   9840  O  O     . ARG A 1 2705 ? 116.118 80.108  123.603 1.00 4.73   ? 2705 ARG A O     1 
ATOM   9841  C  CB    . ARG A 1 2705 ? 116.316 78.895  126.067 1.00 4.55   ? 2705 ARG A CB    1 
ATOM   9842  C  CG    . ARG A 1 2705 ? 116.679 78.587  127.512 1.00 4.97   ? 2705 ARG A CG    1 
ATOM   9843  C  CD    . ARG A 1 2705 ? 117.582 77.367  127.623 1.00 10.28  ? 2705 ARG A CD    1 
ATOM   9844  N  NE    . ARG A 1 2705 ? 116.930 76.146  127.166 1.00 10.48  ? 2705 ARG A NE    1 
ATOM   9845  C  CZ    . ARG A 1 2705 ? 117.352 75.406  126.150 1.00 9.79   ? 2705 ARG A CZ    1 
ATOM   9846  N  NH1   . ARG A 1 2705 ? 118.426 75.737  125.453 1.00 12.64  ? 2705 ARG A NH1   1 
ATOM   9847  N  NH2   . ARG A 1 2705 ? 116.679 74.306  125.825 1.00 10.98  ? 2705 ARG A NH2   1 
ATOM   9848  N  N     . ILE A 1 2706 ? 114.317 81.352  124.105 1.00 3.87   ? 2706 ILE A N     1 
ATOM   9849  C  CA    . ILE A 1 2706 ? 114.135 81.881  122.756 1.00 3.31   ? 2706 ILE A CA    1 
ATOM   9850  C  C     . ILE A 1 2706 ? 113.886 83.380  122.867 1.00 3.67   ? 2706 ILE A C     1 
ATOM   9851  O  O     . ILE A 1 2706 ? 112.962 83.805  123.569 1.00 6.40   ? 2706 ILE A O     1 
ATOM   9852  C  CB    . ILE A 1 2706 ? 112.973 81.193  122.018 1.00 3.86   ? 2706 ILE A CB    1 
ATOM   9853  C  CG1   . ILE A 1 2706 ? 113.290 79.716  121.772 1.00 4.16   ? 2706 ILE A CG1   1 
ATOM   9854  C  CG2   . ILE A 1 2706 ? 112.674 81.903  120.706 1.00 4.00   ? 2706 ILE A CG2   1 
ATOM   9855  C  CD1   . ILE A 1 2706 ? 112.095 78.900  121.331 1.00 4.13   ? 2706 ILE A CD1   1 
ATOM   9856  N  N     . GLN A 1 2707 ? 114.705 84.177  122.184 1.00 3.58   ? 2707 GLN A N     1 
ATOM   9857  C  CA    . GLN A 1 2707 ? 114.540 85.625  122.150 1.00 4.40   ? 2707 GLN A CA    1 
ATOM   9858  C  C     . GLN A 1 2707 ? 114.432 86.107  120.709 1.00 3.44   ? 2707 GLN A C     1 
ATOM   9859  O  O     . GLN A 1 2707 ? 114.585 85.337  119.757 1.00 3.08   ? 2707 GLN A O     1 
ATOM   9860  C  CB    . GLN A 1 2707 ? 115.692 86.339  122.869 1.00 3.92   ? 2707 GLN A CB    1 
ATOM   9861  C  CG    . GLN A 1 2707 ? 117.077 85.887  122.459 1.00 3.53   ? 2707 GLN A CG    1 
ATOM   9862  C  CD    . GLN A 1 2707 ? 118.158 86.481  123.339 1.00 4.58   ? 2707 GLN A CD    1 
ATOM   9863  O  OE1   . GLN A 1 2707 ? 118.856 85.763  124.054 1.00 7.66   ? 2707 GLN A OE1   1 
ATOM   9864  N  NE2   . GLN A 1 2707 ? 118.307 87.798  123.287 1.00 4.40   ? 2707 GLN A NE2   1 
ATOM   9865  N  N     . PHE A 1 2708 ? 114.167 87.405  120.551 1.00 4.78   ? 2708 PHE A N     1 
ATOM   9866  C  CA    . PHE A 1 2708 ? 113.841 87.969  119.249 1.00 3.65   ? 2708 PHE A CA    1 
ATOM   9867  C  C     . PHE A 1 2708 ? 114.650 89.227  118.967 1.00 3.80   ? 2708 PHE A C     1 
ATOM   9868  O  O     . PHE A 1 2708 ? 114.653 90.182  119.756 1.00 6.58   ? 2708 PHE A O     1 
ATOM   9869  C  CB    . PHE A 1 2708 ? 112.345 88.286  119.148 1.00 4.11   ? 2708 PHE A CB    1 
ATOM   9870  C  CG    . PHE A 1 2708 ? 111.461 87.113  119.453 1.00 7.75   ? 2708 PHE A CG    1 
ATOM   9871  C  CD1   . PHE A 1 2708 ? 111.055 86.855  120.751 1.00 7.34   ? 2708 PHE A CD1   1 
ATOM   9872  C  CD2   . PHE A 1 2708 ? 111.052 86.257  118.446 1.00 8.83   ? 2708 PHE A CD2   1 
ATOM   9873  C  CE1   . PHE A 1 2708 ? 110.248 85.773  121.037 1.00 8.36   ? 2708 PHE A CE1   1 
ATOM   9874  C  CE2   . PHE A 1 2708 ? 110.245 85.173  118.726 1.00 6.62   ? 2708 PHE A CE2   1 
ATOM   9875  C  CZ    . PHE A 1 2708 ? 109.843 84.930  120.023 1.00 7.67   ? 2708 PHE A CZ    1 
ATOM   9876  N  N     . VAL A 1 2709 ? 115.322 89.220  117.818 1.00 2.56   ? 2709 VAL A N     1 
ATOM   9877  C  CA    . VAL A 1 2709 ? 116.000 90.389  117.276 1.00 2.43   ? 2709 VAL A CA    1 
ATOM   9878  C  C     . VAL A 1 2709 ? 115.504 90.602  115.854 1.00 2.59   ? 2709 VAL A C     1 
ATOM   9879  O  O     . VAL A 1 2709 ? 115.492 89.665  115.048 1.00 3.28   ? 2709 VAL A O     1 
ATOM   9880  C  CB    . VAL A 1 2709 ? 117.532 90.233  117.297 1.00 2.60   ? 2709 VAL A CB    1 
ATOM   9881  C  CG1   . VAL A 1 2709 ? 118.182 91.362  116.522 1.00 2.07   ? 2709 VAL A CG1   1 
ATOM   9882  C  CG2   . VAL A 1 2709 ? 118.039 90.209  118.724 1.00 3.41   ? 2709 VAL A CG2   1 
ATOM   9883  N  N     . GLY A 1 2710 ? 115.089 91.825  115.551 1.00 2.78   ? 2710 GLY A N     1 
ATOM   9884  C  CA    . GLY A 1 2710 ? 114.632 92.193  114.227 1.00 2.07   ? 2710 GLY A CA    1 
ATOM   9885  C  C     . GLY A 1 2710 ? 115.539 93.244  113.620 1.00 2.28   ? 2710 GLY A C     1 
ATOM   9886  O  O     . GLY A 1 2710 ? 116.185 94.012  114.333 1.00 2.08   ? 2710 GLY A O     1 
ATOM   9887  N  N     . ALA A 1 2711 ? 115.603 93.260  112.294 1.00 4.45   ? 2711 ALA A N     1 
ATOM   9888  C  CA    . ALA A 1 2711 ? 116.271 94.321  111.557 1.00 2.51   ? 2711 ALA A CA    1 
ATOM   9889  C  C     . ALA A 1 2711 ? 115.284 94.902  110.561 1.00 3.54   ? 2711 ALA A C     1 
ATOM   9890  O  O     . ALA A 1 2711 ? 114.385 94.206  110.082 1.00 7.08   ? 2711 ALA A O     1 
ATOM   9891  C  CB    . ALA A 1 2711 ? 117.522 93.821  110.828 1.00 3.94   ? 2711 ALA A CB    1 
ATOM   9892  N  N     . CYS A 1 2712 ? 115.439 96.188  110.268 1.00 3.46   ? 2712 CYS A N     1 
ATOM   9893  C  CA    . CYS A 1 2712 ? 114.508 96.814  109.339 1.00 3.59   ? 2712 CYS A CA    1 
ATOM   9894  C  C     . CYS A 1 2712 ? 115.088 98.121  108.824 1.00 3.26   ? 2712 CYS A C     1 
ATOM   9895  O  O     . CYS A 1 2712 ? 116.014 98.689  109.407 1.00 2.64   ? 2712 CYS A O     1 
ATOM   9896  C  CB    . CYS A 1 2712 ? 113.147 97.066  109.995 1.00 2.67   ? 2712 CYS A CB    1 
ATOM   9897  S  SG    . CYS A 1 2712 ? 113.208 98.200  111.388 1.00 3.73   ? 2712 CYS A SG    1 
ATOM   9898  N  N     . ASN A 1 2713 ? 114.528 98.575  107.717 1.00 4.62   ? 2713 ASN A N     1 
ATOM   9899  C  CA    . ASN A 1 2713 ? 114.700 99.905  107.163 1.00 5.27   ? 2713 ASN A CA    1 
ATOM   9900  C  C     . ASN A 1 2713 ? 113.679 100.853 107.778 1.00 7.31   ? 2713 ASN A C     1 
ATOM   9901  O  O     . ASN A 1 2713 ? 112.694 100.410 108.377 1.00 7.54   ? 2713 ASN A O     1 
ATOM   9902  C  CB    . ASN A 1 2713 ? 114.546 99.858  105.644 1.00 6.89   ? 2713 ASN A CB    1 
ATOM   9903  C  CG    . ASN A 1 2713 ? 115.671 99.097  104.967 1.00 7.07   ? 2713 ASN A CG    1 
ATOM   9904  O  OD1   . ASN A 1 2713 ? 115.562 98.708  103.806 1.00 11.45  ? 2713 ASN A OD1   1 
ATOM   9905  N  ND2   . ASN A 1 2713 ? 116.764 98.887  105.692 1.00 3.70   ? 2713 ASN A ND2   1 
ATOM   9906  N  N     . PRO A 1 2714 ? 113.894 102.164 107.674 1.00 7.70   ? 2714 PRO A N     1 
ATOM   9907  C  CA    . PRO A 1 2714 ? 112.933 103.104 108.242 1.00 8.26   ? 2714 PRO A CA    1 
ATOM   9908  C  C     . PRO A 1 2714 ? 111.556 102.897 107.642 1.00 9.48   ? 2714 PRO A C     1 
ATOM   9909  O  O     . PRO A 1 2714 ? 111.422 102.553 106.454 1.00 14.46  ? 2714 PRO A O     1 
ATOM   9910  C  CB    . PRO A 1 2714 ? 113.513 104.472 107.859 1.00 11.88  ? 2714 PRO A CB    1 
ATOM   9911  C  CG    . PRO A 1 2714 ? 114.971 104.235 107.791 1.00 9.77   ? 2714 PRO A CG    1 
ATOM   9912  C  CD    . PRO A 1 2714 ? 115.130 102.842 107.241 1.00 7.13   ? 2714 PRO A CD    1 
ATOM   9913  N  N     . PRO A 1 2715 ? 110.498 103.086 108.437 1.00 10.49  ? 2715 PRO A N     1 
ATOM   9914  C  CA    . PRO A 1 2715 ? 109.139 102.854 107.919 1.00 10.95  ? 2715 PRO A CA    1 
ATOM   9915  C  C     . PRO A 1 2715 ? 108.758 103.778 106.779 1.00 13.04  ? 2715 PRO A C     1 
ATOM   9916  O  O     . PRO A 1 2715 ? 107.834 103.454 106.023 1.00 20.74  ? 2715 PRO A O     1 
ATOM   9917  C  CB    . PRO A 1 2715 ? 108.249 103.089 109.148 1.00 10.30  ? 2715 PRO A CB    1 
ATOM   9918  C  CG    . PRO A 1 2715 ? 109.073 103.934 110.059 1.00 8.60   ? 2715 PRO A CG    1 
ATOM   9919  C  CD    . PRO A 1 2715 ? 110.485 103.494 109.850 1.00 9.99   ? 2715 PRO A CD    1 
ATOM   9920  N  N     . THR A 1 2716 ? 109.435 104.917 106.629 1.00 13.61  ? 2716 THR A N     1 
ATOM   9921  C  CA    . THR A 1 2716 ? 109.153 105.823 105.524 1.00 17.76  ? 2716 THR A CA    1 
ATOM   9922  C  C     . THR A 1 2716 ? 109.658 105.296 104.188 1.00 18.41  ? 2716 THR A C     1 
ATOM   9923  O  O     . THR A 1 2716 ? 109.289 105.849 103.146 1.00 26.08  ? 2716 THR A O     1 
ATOM   9924  C  CB    . THR A 1 2716 ? 109.768 107.196 105.803 1.00 20.27  ? 2716 THR A CB    1 
ATOM   9925  O  OG1   . THR A 1 2716 ? 111.176 107.055 106.025 1.00 21.09  ? 2716 THR A OG1   1 
ATOM   9926  C  CG2   . THR A 1 2716 ? 109.129 107.824 107.032 1.00 14.28  ? 2716 THR A CG2   1 
ATOM   9927  N  N     . ASP A 1 2717 ? 110.487 104.255 104.190 1.00 15.51  ? 2717 ASP A N     1 
ATOM   9928  C  CA    . ASP A 1 2717 ? 110.938 103.657 102.946 1.00 19.07  ? 2717 ASP A CA    1 
ATOM   9929  C  C     . ASP A 1 2717 ? 109.778 102.946 102.250 1.00 18.68  ? 2717 ASP A C     1 
ATOM   9930  O  O     . ASP A 1 2717 ? 108.851 102.466 102.907 1.00 16.00  ? 2717 ASP A O     1 
ATOM   9931  C  CB    . ASP A 1 2717 ? 112.073 102.669 103.208 1.00 20.15  ? 2717 ASP A CB    1 
ATOM   9932  C  CG    . ASP A 1 2717 ? 113.313 103.340 103.762 1.00 23.83  ? 2717 ASP A CG    1 
ATOM   9933  O  OD1   . ASP A 1 2717 ? 113.288 104.573 103.955 1.00 23.90  ? 2717 ASP A OD1   1 
ATOM   9934  O  OD2   . ASP A 1 2717 ? 114.316 102.636 104.000 1.00 29.85  ? 2717 ASP A OD2   1 
ATOM   9935  N  N     . PRO A 1 2718 ? 109.797 102.883 100.918 1.00 19.57  ? 2718 PRO A N     1 
ATOM   9936  C  CA    . PRO A 1 2718 ? 108.711 102.204 100.200 1.00 21.47  ? 2718 PRO A CA    1 
ATOM   9937  C  C     . PRO A 1 2718 ? 108.613 100.736 100.587 1.00 18.51  ? 2718 PRO A C     1 
ATOM   9938  O  O     . PRO A 1 2718 ? 109.621 100.043 100.738 1.00 20.93  ? 2718 PRO A O     1 
ATOM   9939  C  CB    . PRO A 1 2718 ? 109.098 102.378 98.726  1.00 21.09  ? 2718 PRO A CB    1 
ATOM   9940  C  CG    . PRO A 1 2718 ? 110.572 102.630 98.750  1.00 21.41  ? 2718 PRO A CG    1 
ATOM   9941  C  CD    . PRO A 1 2718 ? 110.805 103.428 99.995  1.00 18.94  ? 2718 PRO A CD    1 
ATOM   9942  N  N     . GLY A 1 2719 ? 107.376 100.265 100.746 1.00 15.77  ? 2719 GLY A N     1 
ATOM   9943  C  CA    . GLY A 1 2719 ? 107.119 98.913  101.187 1.00 13.05  ? 2719 GLY A CA    1 
ATOM   9944  C  C     . GLY A 1 2719 ? 107.228 98.696  102.680 1.00 13.58  ? 2719 GLY A C     1 
ATOM   9945  O  O     . GLY A 1 2719 ? 106.873 97.611  103.158 1.00 14.42  ? 2719 GLY A O     1 
ATOM   9946  N  N     . ARG A 1 2720 ? 107.696 99.686  103.432 1.00 10.22  ? 2720 ARG A N     1 
ATOM   9947  C  CA    . ARG A 1 2720 ? 107.896 99.563  104.869 1.00 10.16  ? 2720 ARG A CA    1 
ATOM   9948  C  C     . ARG A 1 2720 ? 106.685 100.129 105.598 1.00 11.69  ? 2720 ARG A C     1 
ATOM   9949  O  O     . ARG A 1 2720 ? 106.194 101.208 105.251 1.00 14.86  ? 2720 ARG A O     1 
ATOM   9950  C  CB    . ARG A 1 2720 ? 109.168 100.292 105.312 1.00 11.02  ? 2720 ARG A CB    1 
ATOM   9951  C  CG    . ARG A 1 2720 ? 110.472 99.503  105.165 1.00 10.81  ? 2720 ARG A CG    1 
ATOM   9952  C  CD    . ARG A 1 2720 ? 110.734 99.031  103.743 1.00 12.57  ? 2720 ARG A CD    1 
ATOM   9953  N  NE    . ARG A 1 2720 ? 111.938 98.214  103.654 1.00 16.31  ? 2720 ARG A NE    1 
ATOM   9954  C  CZ    . ARG A 1 2720 ? 112.355 97.610  102.550 1.00 16.82  ? 2720 ARG A CZ    1 
ATOM   9955  N  NH1   . ARG A 1 2720 ? 111.688 97.712  101.412 1.00 18.66  ? 2720 ARG A NH1   1 
ATOM   9956  N  NH2   . ARG A 1 2720 ? 113.468 96.884  102.588 1.00 15.12  ? 2720 ARG A NH2   1 
ATOM   9957  N  N     . LYS A 1 2721 ? 106.204 99.399  106.600 1.00 11.48  ? 2721 LYS A N     1 
ATOM   9958  C  CA    . LYS A 1 2721 ? 105.078 99.863  107.392 1.00 11.79  ? 2721 LYS A CA    1 
ATOM   9959  C  C     . LYS A 1 2721 ? 105.527 100.198 108.810 1.00 8.91   ? 2721 LYS A C     1 
ATOM   9960  O  O     . LYS A 1 2721 ? 106.449 99.569  109.339 1.00 8.93   ? 2721 LYS A O     1 
ATOM   9961  C  CB    . LYS A 1 2721 ? 103.963 98.811  107.460 1.00 11.10  ? 2721 LYS A CB    1 
ATOM   9962  C  CG    . LYS A 1 2721 ? 102.996 98.829  106.285 1.00 13.52  ? 2721 LYS A CG    1 
ATOM   9963  C  CD    . LYS A 1 2721 ? 103.617 98.224  105.038 1.00 14.04  ? 2721 LYS A CD    1 
ATOM   9964  C  CE    . LYS A 1 2721 ? 103.805 96.725  105.195 1.00 9.54   ? 2721 LYS A CE    1 
ATOM   9965  N  NZ    . LYS A 1 2721 ? 104.335 96.098  103.954 1.00 8.44   ? 2721 LYS A NZ    1 
ATOM   9966  N  N     . PRO A 1 2722 ? 104.908 101.191 109.448 1.00 10.58  ? 2722 PRO A N     1 
ATOM   9967  C  CA    . PRO A 1 2722 ? 105.221 101.463 110.855 1.00 9.41   ? 2722 PRO A CA    1 
ATOM   9968  C  C     . PRO A 1 2722 ? 104.841 100.283 111.736 1.00 6.15   ? 2722 PRO A C     1 
ATOM   9969  O  O     . PRO A 1 2722 ? 103.814 99.633  111.530 1.00 7.89   ? 2722 PRO A O     1 
ATOM   9970  C  CB    . PRO A 1 2722 ? 104.379 102.703 111.175 1.00 8.10   ? 2722 PRO A CB    1 
ATOM   9971  C  CG    . PRO A 1 2722 ? 103.294 102.706 110.149 1.00 7.24   ? 2722 PRO A CG    1 
ATOM   9972  C  CD    . PRO A 1 2722 ? 103.909 102.130 108.911 1.00 8.97   ? 2722 PRO A CD    1 
ATOM   9973  N  N     . LEU A 1 2723 ? 105.684 100.008 112.725 1.00 5.97   ? 2723 LEU A N     1 
ATOM   9974  C  CA    . LEU A 1 2723 ? 105.416 98.930  113.662 1.00 4.14   ? 2723 LEU A CA    1 
ATOM   9975  C  C     . LEU A 1 2723 ? 104.378 99.363  114.690 1.00 5.66   ? 2723 LEU A C     1 
ATOM   9976  O  O     . LEU A 1 2723 ? 104.284 100.538 115.053 1.00 7.01   ? 2723 LEU A O     1 
ATOM   9977  C  CB    . LEU A 1 2723 ? 106.701 98.494  114.364 1.00 4.55   ? 2723 LEU A CB    1 
ATOM   9978  C  CG    . LEU A 1 2723 ? 107.688 97.684  113.520 1.00 3.96   ? 2723 LEU A CG    1 
ATOM   9979  C  CD1   . LEU A 1 2723 ? 108.947 97.374  114.313 1.00 5.42   ? 2723 LEU A CD1   1 
ATOM   9980  C  CD2   . LEU A 1 2723 ? 107.040 96.406  113.011 1.00 3.95   ? 2723 LEU A CD2   1 
ATOM   9981  N  N     . SER A 1 2724 ? 103.590 98.395  115.152 1.00 6.60   ? 2724 SER A N     1 
ATOM   9982  C  CA    . SER A 1 2724 ? 102.565 98.677  116.146 1.00 5.05   ? 2724 SER A CA    1 
ATOM   9983  C  C     . SER A 1 2724 ? 103.198 99.134  117.455 1.00 5.09   ? 2724 SER A C     1 
ATOM   9984  O  O     . SER A 1 2724 ? 104.245 98.629  117.868 1.00 6.02   ? 2724 SER A O     1 
ATOM   9985  C  CB    . SER A 1 2724 ? 101.701 97.437  116.380 1.00 6.02   ? 2724 SER A CB    1 
ATOM   9986  O  OG    . SER A 1 2724 ? 100.778 97.646  117.434 1.00 13.46  ? 2724 SER A OG    1 
ATOM   9987  N  N     . HIS A 1 2725 ? 102.550 100.102 118.109 1.00 6.44   ? 2725 HIS A N     1 
ATOM   9988  C  CA    . HIS A 1 2725 ? 103.053 100.612 119.381 1.00 7.90   ? 2725 HIS A CA    1 
ATOM   9989  C  C     . HIS A 1 2725 ? 103.040 99.537  120.461 1.00 5.46   ? 2725 HIS A C     1 
ATOM   9990  O  O     . HIS A 1 2725 ? 103.937 99.502  121.314 1.00 4.80   ? 2725 HIS A O     1 
ATOM   9991  C  CB    . HIS A 1 2725 ? 102.226 101.819 119.824 1.00 11.60  ? 2725 HIS A CB    1 
ATOM   9992  C  CG    . HIS A 1 2725 ? 102.443 103.042 118.988 1.00 16.24  ? 2725 HIS A CG    1 
ATOM   9993  N  ND1   . HIS A 1 2725 ? 102.268 104.318 119.477 1.00 20.07  ? 2725 HIS A ND1   1 
ATOM   9994  C  CD2   . HIS A 1 2725 ? 102.826 103.183 117.697 1.00 15.77  ? 2725 HIS A CD2   1 
ATOM   9995  C  CE1   . HIS A 1 2725 ? 102.529 105.193 118.522 1.00 15.66  ? 2725 HIS A CE1   1 
ATOM   9996  N  NE2   . HIS A 1 2725 ? 102.870 104.530 117.432 1.00 17.38  ? 2725 HIS A NE2   1 
ATOM   9997  N  N     . ARG A 1 2726 ? 102.032 98.662  120.441 1.00 4.21   ? 2726 ARG A N     1 
ATOM   9998  C  CA    . ARG A 1 2726 ? 101.990 97.552  121.386 1.00 5.66   ? 2726 ARG A CA    1 
ATOM   9999  C  C     . ARG A 1 2726 ? 103.179 96.621  121.189 1.00 4.52   ? 2726 ARG A C     1 
ATOM   10000 O  O     . ARG A 1 2726 ? 103.666 96.010  122.147 1.00 7.00   ? 2726 ARG A O     1 
ATOM   10001 C  CB    . ARG A 1 2726 ? 100.678 96.788  121.227 1.00 4.78   ? 2726 ARG A CB    1 
ATOM   10002 C  CG    . ARG A 1 2726 ? 99.441  97.609  121.526 1.00 5.35   ? 2726 ARG A CG    1 
ATOM   10003 C  CD    . ARG A 1 2726 ? 98.197  96.749  121.455 1.00 5.63   ? 2726 ARG A CD    1 
ATOM   10004 N  NE    . ARG A 1 2726 ? 97.616  96.525  122.771 1.00 3.80   ? 2726 ARG A NE    1 
ATOM   10005 C  CZ    . ARG A 1 2726 ? 96.533  95.796  122.996 1.00 3.68   ? 2726 ARG A CZ    1 
ATOM   10006 N  NH1   . ARG A 1 2726 ? 95.883  95.202  122.009 1.00 6.32   ? 2726 ARG A NH1   1 
ATOM   10007 N  NH2   . ARG A 1 2726 ? 96.094  95.657  124.242 1.00 3.34   ? 2726 ARG A NH2   1 
ATOM   10008 N  N     . PHE A 1 2727 ? 103.651 96.490  119.949 1.00 3.70   ? 2727 PHE A N     1 
ATOM   10009 C  CA    . PHE A 1 2727 ? 104.869 95.728  119.701 1.00 3.99   ? 2727 PHE A CA    1 
ATOM   10010 C  C     . PHE A 1 2727 ? 106.103 96.513  120.129 1.00 3.82   ? 2727 PHE A C     1 
ATOM   10011 O  O     . PHE A 1 2727 ? 107.054 95.938  120.670 1.00 4.29   ? 2727 PHE A O     1 
ATOM   10012 C  CB    . PHE A 1 2727 ? 104.943 95.337  118.222 1.00 3.84   ? 2727 PHE A CB    1 
ATOM   10013 C  CG    . PHE A 1 2727 ? 106.232 94.666  117.825 1.00 3.80   ? 2727 PHE A CG    1 
ATOM   10014 C  CD1   . PHE A 1 2727 ? 106.318 93.285  117.776 1.00 3.20   ? 2727 PHE A CD1   1 
ATOM   10015 C  CD2   . PHE A 1 2727 ? 107.339 95.413  117.450 1.00 4.16   ? 2727 PHE A CD2   1 
ATOM   10016 C  CE1   . PHE A 1 2727 ? 107.492 92.663  117.402 1.00 4.06   ? 2727 PHE A CE1   1 
ATOM   10017 C  CE2   . PHE A 1 2727 ? 108.516 94.796  117.076 1.00 3.59   ? 2727 PHE A CE2   1 
ATOM   10018 C  CZ    . PHE A 1 2727 ? 108.592 93.419  117.049 1.00 2.78   ? 2727 PHE A CZ    1 
ATOM   10019 N  N     . LEU A 1 2728 ? 106.103 97.829  119.901 1.00 3.14   ? 2728 LEU A N     1 
ATOM   10020 C  CA    . LEU A 1 2728 ? 107.296 98.626  120.167 1.00 3.58   ? 2728 LEU A CA    1 
ATOM   10021 C  C     . LEU A 1 2728 ? 107.552 98.815  121.657 1.00 3.97   ? 2728 LEU A C     1 
ATOM   10022 O  O     . LEU A 1 2728 ? 108.701 99.036  122.054 1.00 4.10   ? 2728 LEU A O     1 
ATOM   10023 C  CB    . LEU A 1 2728 ? 107.189 99.985  119.474 1.00 4.39   ? 2728 LEU A CB    1 
ATOM   10024 C  CG    . LEU A 1 2728 ? 107.203 99.963  117.945 1.00 4.84   ? 2728 LEU A CG    1 
ATOM   10025 C  CD1   . LEU A 1 2728 ? 107.079 101.368 117.384 1.00 4.91   ? 2728 LEU A CD1   1 
ATOM   10026 C  CD2   . LEU A 1 2728 ? 108.472 99.295  117.444 1.00 3.30   ? 2728 LEU A CD2   1 
ATOM   10027 N  N     . ARG A 1 2729 ? 106.513 98.740  122.496 1.00 5.49   ? 2729 ARG A N     1 
ATOM   10028 C  CA    . ARG A 1 2729 ? 106.727 98.962  123.925 1.00 4.12   ? 2729 ARG A CA    1 
ATOM   10029 C  C     . ARG A 1 2729 ? 107.642 97.908  124.535 1.00 5.33   ? 2729 ARG A C     1 
ATOM   10030 O  O     . ARG A 1 2729 ? 108.355 98.191  125.505 1.00 6.75   ? 2729 ARG A O     1 
ATOM   10031 C  CB    . ARG A 1 2729 ? 105.392 99.001  124.675 1.00 5.93   ? 2729 ARG A CB    1 
ATOM   10032 C  CG    . ARG A 1 2729 ? 104.611 97.698  124.682 1.00 6.69   ? 2729 ARG A CG    1 
ATOM   10033 C  CD    . ARG A 1 2729 ? 103.294 97.873  125.422 1.00 8.47   ? 2729 ARG A CD    1 
ATOM   10034 N  NE    . ARG A 1 2729 ? 103.466 98.076  126.855 1.00 9.21   ? 2729 ARG A NE    1 
ATOM   10035 C  CZ    . ARG A 1 2729 ? 103.539 97.097  127.747 1.00 7.57   ? 2729 ARG A CZ    1 
ATOM   10036 N  NH1   . ARG A 1 2729 ? 103.379 95.834  127.398 1.00 15.36  ? 2729 ARG A NH1   1 
ATOM   10037 N  NH2   . ARG A 1 2729 ? 103.755 97.395  129.025 1.00 9.31   ? 2729 ARG A NH2   1 
ATOM   10038 N  N     . HIS A 1 2730 ? 107.642 96.695  123.987 1.00 4.08   ? 2730 HIS A N     1 
ATOM   10039 C  CA    . HIS A 1 2730 ? 108.523 95.630  124.445 1.00 4.89   ? 2730 HIS A CA    1 
ATOM   10040 C  C     . HIS A 1 2730 ? 109.890 95.656  123.781 1.00 4.17   ? 2730 HIS A C     1 
ATOM   10041 O  O     . HIS A 1 2730 ? 110.816 95.008  124.277 1.00 5.36   ? 2730 HIS A O     1 
ATOM   10042 C  CB    . HIS A 1 2730 ? 107.884 94.262  124.191 1.00 5.41   ? 2730 HIS A CB    1 
ATOM   10043 C  CG    . HIS A 1 2730 ? 106.541 94.088  124.824 1.00 6.49   ? 2730 HIS A CG    1 
ATOM   10044 N  ND1   . HIS A 1 2730 ? 106.386 93.695  126.135 1.00 10.70  ? 2730 HIS A ND1   1 
ATOM   10045 C  CD2   . HIS A 1 2730 ? 105.292 94.241  124.325 1.00 5.19   ? 2730 HIS A CD2   1 
ATOM   10046 C  CE1   . HIS A 1 2730 ? 105.098 93.616  126.418 1.00 8.31   ? 2730 HIS A CE1   1 
ATOM   10047 N  NE2   . HIS A 1 2730 ? 104.413 93.945  125.337 1.00 7.80   ? 2730 HIS A NE2   1 
ATOM   10048 N  N     . VAL A 1 2731 ? 110.042 96.381  122.679 1.00 3.71   ? 2731 VAL A N     1 
ATOM   10049 C  CA    . VAL A 1 2731 ? 111.209 96.206  121.820 1.00 3.81   ? 2731 VAL A CA    1 
ATOM   10050 C  C     . VAL A 1 2731 ? 112.028 97.487  121.732 1.00 3.20   ? 2731 VAL A C     1 
ATOM   10051 O  O     . VAL A 1 2731 ? 111.628 98.431  121.035 1.00 3.75   ? 2731 VAL A O     1 
ATOM   10052 C  CB    . VAL A 1 2731 ? 110.786 95.738  120.420 1.00 4.49   ? 2731 VAL A CB    1 
ATOM   10053 C  CG1   . VAL A 1 2731 ? 112.002 95.496  119.580 1.00 3.17   ? 2731 VAL A CG1   1 
ATOM   10054 C  CG2   . VAL A 1 2731 ? 109.945 94.475  120.512 1.00 4.08   ? 2731 VAL A CG2   1 
ATOM   10055 N  N     . PRO A 1 2732 ? 113.167 97.571  122.418 1.00 3.57   ? 2732 PRO A N     1 
ATOM   10056 C  CA    . PRO A 1 2732 ? 114.085 98.689  122.187 1.00 4.00   ? 2732 PRO A CA    1 
ATOM   10057 C  C     . PRO A 1 2732 ? 114.547 98.737  120.737 1.00 3.74   ? 2732 PRO A C     1 
ATOM   10058 O  O     . PRO A 1 2732 ? 114.839 97.708  120.121 1.00 4.33   ? 2732 PRO A O     1 
ATOM   10059 C  CB    . PRO A 1 2732 ? 115.244 98.386  123.140 1.00 4.06   ? 2732 PRO A CB    1 
ATOM   10060 C  CG    . PRO A 1 2732 ? 114.589 97.667  124.265 1.00 5.33   ? 2732 PRO A CG    1 
ATOM   10061 C  CD    . PRO A 1 2732 ? 113.551 96.791  123.607 1.00 5.76   ? 2732 PRO A CD    1 
ATOM   10062 N  N     . VAL A 1 2733 ? 114.624 99.950  120.198 1.00 3.25   ? 2733 VAL A N     1 
ATOM   10063 C  CA    . VAL A 1 2733 ? 115.023 100.188 118.817 1.00 3.08   ? 2733 VAL A CA    1 
ATOM   10064 C  C     . VAL A 1 2733 ? 116.328 100.969 118.827 1.00 2.77   ? 2733 VAL A C     1 
ATOM   10065 O  O     . VAL A 1 2733 ? 116.447 101.979 119.529 1.00 3.80   ? 2733 VAL A O     1 
ATOM   10066 C  CB    . VAL A 1 2733 ? 113.937 100.947 118.032 1.00 2.64   ? 2733 VAL A CB    1 
ATOM   10067 C  CG1   . VAL A 1 2733 ? 114.440 101.320 116.644 1.00 2.40   ? 2733 VAL A CG1   1 
ATOM   10068 C  CG2   . VAL A 1 2733 ? 112.670 100.116 117.942 1.00 2.26   ? 2733 VAL A CG2   1 
ATOM   10069 N  N     . VAL A 1 2734 ? 117.304 100.494 118.061 1.00 1.94   ? 2734 VAL A N     1 
ATOM   10070 C  CA    . VAL A 1 2734 ? 118.589 101.167 117.912 1.00 2.26   ? 2734 VAL A CA    1 
ATOM   10071 C  C     . VAL A 1 2734 ? 118.739 101.606 116.461 1.00 2.43   ? 2734 VAL A C     1 
ATOM   10072 O  O     . VAL A 1 2734 ? 118.547 100.807 115.536 1.00 2.21   ? 2734 VAL A O     1 
ATOM   10073 C  CB    . VAL A 1 2734 ? 119.756 100.269 118.369 1.00 3.53   ? 2734 VAL A CB    1 
ATOM   10074 C  CG1   . VAL A 1 2734 ? 119.845 98.995  117.542 1.00 3.18   ? 2734 VAL A CG1   1 
ATOM   10075 C  CG2   . VAL A 1 2734 ? 121.065 101.033 118.310 1.00 3.03   ? 2734 VAL A CG2   1 
ATOM   10076 N  N     . TYR A 1 2735 ? 119.057 102.883 116.263 1.00 3.52   ? 2735 TYR A N     1 
ATOM   10077 C  CA    . TYR A 1 2735 ? 119.212 103.459 114.933 1.00 3.14   ? 2735 TYR A CA    1 
ATOM   10078 C  C     . TYR A 1 2735 ? 120.661 103.313 114.490 1.00 3.47   ? 2735 TYR A C     1 
ATOM   10079 O  O     . TYR A 1 2735 ? 121.579 103.732 115.203 1.00 4.14   ? 2735 TYR A O     1 
ATOM   10080 C  CB    . TYR A 1 2735 ? 118.798 104.929 114.910 1.00 3.63   ? 2735 TYR A CB    1 
ATOM   10081 C  CG    . TYR A 1 2735 ? 118.939 105.563 113.546 1.00 5.52   ? 2735 TYR A CG    1 
ATOM   10082 C  CD1   . TYR A 1 2735 ? 118.333 104.998 112.431 1.00 4.58   ? 2735 TYR A CD1   1 
ATOM   10083 C  CD2   . TYR A 1 2735 ? 119.694 106.714 113.367 1.00 5.82   ? 2735 TYR A CD2   1 
ATOM   10084 C  CE1   . TYR A 1 2735 ? 118.464 105.569 111.180 1.00 5.49   ? 2735 TYR A CE1   1 
ATOM   10085 C  CE2   . TYR A 1 2735 ? 119.831 107.292 112.119 1.00 6.72   ? 2735 TYR A CE2   1 
ATOM   10086 C  CZ    . TYR A 1 2735 ? 119.213 106.715 111.030 1.00 9.00   ? 2735 TYR A CZ    1 
ATOM   10087 O  OH    . TYR A 1 2735 ? 119.345 107.286 109.785 1.00 14.27  ? 2735 TYR A OH    1 
ATOM   10088 N  N     . VAL A 1 2736 ? 120.860 102.727 113.317 1.00 3.06   ? 2736 VAL A N     1 
ATOM   10089 C  CA    . VAL A 1 2736 ? 122.186 102.490 112.765 1.00 3.95   ? 2736 VAL A CA    1 
ATOM   10090 C  C     . VAL A 1 2736 ? 122.225 103.163 111.399 1.00 4.12   ? 2736 VAL A C     1 
ATOM   10091 O  O     . VAL A 1 2736 ? 121.722 102.622 110.410 1.00 3.04   ? 2736 VAL A O     1 
ATOM   10092 C  CB    . VAL A 1 2736 ? 122.503 100.995 112.673 1.00 4.58   ? 2736 VAL A CB    1 
ATOM   10093 C  CG1   . VAL A 1 2736 ? 123.895 100.775 112.100 1.00 3.39   ? 2736 VAL A CG1   1 
ATOM   10094 C  CG2   . VAL A 1 2736 ? 122.361 100.354 114.042 1.00 4.54   ? 2736 VAL A CG2   1 
ATOM   10095 N  N     . ASP A 1 2737 ? 122.822 104.348 111.342 1.00 4.42   ? 2737 ASP A N     1 
ATOM   10096 C  CA    . ASP A 1 2737 ? 122.915 105.112 110.110 1.00 5.66   ? 2737 ASP A CA    1 
ATOM   10097 C  C     . ASP A 1 2737 ? 124.128 104.670 109.294 1.00 5.19   ? 2737 ASP A C     1 
ATOM   10098 O  O     . ASP A 1 2737 ? 124.957 103.874 109.741 1.00 4.95   ? 2737 ASP A O     1 
ATOM   10099 C  CB    . ASP A 1 2737 ? 122.991 106.608 110.419 1.00 6.74   ? 2737 ASP A CB    1 
ATOM   10100 C  CG    . ASP A 1 2737 ? 122.536 107.470 109.259 1.00 11.57  ? 2737 ASP A CG    1 
ATOM   10101 O  OD1   . ASP A 1 2737 ? 122.074 106.908 108.243 1.00 9.31   ? 2737 ASP A OD1   1 
ATOM   10102 O  OD2   . ASP A 1 2737 ? 122.641 108.710 109.362 1.00 24.01  ? 2737 ASP A OD2   1 
ATOM   10103 N  N     . TYR A 1 2738 ? 124.235 105.192 108.069 1.00 6.18   ? 2738 TYR A N     1 
ATOM   10104 C  CA    . TYR A 1 2738 ? 125.422 104.874 107.227 1.00 6.91   ? 2738 TYR A CA    1 
ATOM   10105 C  C     . TYR A 1 2738 ? 126.659 105.496 107.871 1.00 10.02  ? 2738 TYR A C     1 
ATOM   10106 O  O     . TYR A 1 2738 ? 126.565 106.621 108.409 1.00 8.56   ? 2738 TYR A O     1 
ATOM   10107 C  CB    . TYR A 1 2738 ? 125.251 105.392 105.796 1.00 4.82   ? 2738 TYR A CB    1 
ATOM   10108 C  CG    . TYR A 1 2738 ? 124.349 104.555 104.900 1.00 5.50   ? 2738 TYR A CG    1 
ATOM   10109 C  CD1   . TYR A 1 2738 ? 124.217 103.184 105.088 1.00 5.32   ? 2738 TYR A CD1   1 
ATOM   10110 C  CD2   . TYR A 1 2738 ? 123.640 105.138 103.857 1.00 6.95   ? 2738 TYR A CD2   1 
ATOM   10111 C  CE1   . TYR A 1 2738 ? 123.401 102.420 104.271 1.00 4.32   ? 2738 TYR A CE1   1 
ATOM   10112 C  CE2   . TYR A 1 2738 ? 122.821 104.385 103.033 1.00 6.24   ? 2738 TYR A CE2   1 
ATOM   10113 C  CZ    . TYR A 1 2738 ? 122.702 103.023 103.240 1.00 6.35   ? 2738 TYR A CZ    1 
ATOM   10114 O  OH    . TYR A 1 2738 ? 121.892 102.286 102.425 1.00 7.38   ? 2738 TYR A OH    1 
ATOM   10115 N  N     . PRO A 1 2739 ? 127.829 104.818 107.848 1.00 13.36  ? 2739 PRO A N     1 
ATOM   10116 C  CA    . PRO A 1 2739 ? 129.051 105.405 108.380 1.00 8.87   ? 2739 PRO A CA    1 
ATOM   10117 C  C     . PRO A 1 2739 ? 129.362 106.699 107.643 1.00 10.75  ? 2739 PRO A C     1 
ATOM   10118 O  O     . PRO A 1 2739 ? 129.208 106.741 106.406 1.00 12.18  ? 2739 PRO A O     1 
ATOM   10119 C  CB    . PRO A 1 2739 ? 130.115 104.323 108.136 1.00 6.65   ? 2739 PRO A CB    1 
ATOM   10120 C  CG    . PRO A 1 2739 ? 129.317 103.048 107.972 1.00 6.18   ? 2739 PRO A CG    1 
ATOM   10121 C  CD    . PRO A 1 2739 ? 128.008 103.474 107.328 1.00 8.17   ? 2739 PRO A CD    1 
ATOM   10122 N  N     . GLY A 1 2740 ? 129.786 107.732 108.378 1.00 11.80  ? 2740 GLY A N     1 
ATOM   10123 C  CA    . GLY A 1 2740 ? 130.090 109.039 107.762 1.00 11.19  ? 2740 GLY A CA    1 
ATOM   10124 C  C     . GLY A 1 2740 ? 131.365 108.983 106.941 1.00 12.59  ? 2740 GLY A C     1 
ATOM   10125 O  O     . GLY A 1 2740 ? 132.062 107.949 107.001 1.00 13.09  ? 2740 GLY A O     1 
ATOM   10126 N  N     . PRO A 1 2741 ? 131.710 110.040 106.171 1.00 14.22  ? 2741 PRO A N     1 
ATOM   10127 C  CA    . PRO A 1 2741 ? 132.895 110.013 105.298 1.00 11.18  ? 2741 PRO A CA    1 
ATOM   10128 C  C     . PRO A 1 2741 ? 134.179 109.693 106.043 1.00 12.35  ? 2741 PRO A C     1 
ATOM   10129 O  O     . PRO A 1 2741 ? 135.035 108.977 105.511 1.00 10.52  ? 2741 PRO A O     1 
ATOM   10130 C  CB    . PRO A 1 2741 ? 132.914 111.426 104.698 1.00 16.05  ? 2741 PRO A CB    1 
ATOM   10131 C  CG    . PRO A 1 2741 ? 131.496 111.893 104.792 1.00 20.33  ? 2741 PRO A CG    1 
ATOM   10132 C  CD    . PRO A 1 2741 ? 130.982 111.316 106.076 1.00 15.98  ? 2741 PRO A CD    1 
ATOM   10133 N  N     . ALA A 1 2742 ? 134.330 110.193 107.272 1.00 10.88  ? 2742 ALA A N     1 
ATOM   10134 C  CA    . ALA A 1 2742 ? 135.520 109.874 108.054 1.00 9.95   ? 2742 ALA A CA    1 
ATOM   10135 C  C     . ALA A 1 2742 ? 135.538 108.406 108.465 1.00 9.25   ? 2742 ALA A C     1 
ATOM   10136 O  O     . ALA A 1 2742 ? 136.583 107.750 108.395 1.00 8.91   ? 2742 ALA A O     1 
ATOM   10137 C  CB    . ALA A 1 2742 ? 135.598 110.778 109.283 1.00 9.20   ? 2742 ALA A CB    1 
ATOM   10138 N  N     . SER A 1 2743 ? 134.392 107.873 108.895 1.00 11.51  ? 2743 SER A N     1 
ATOM   10139 C  CA    . SER A 1 2743 ? 134.325 106.464 109.269 1.00 8.23   ? 2743 SER A CA    1 
ATOM   10140 C  C     . SER A 1 2743 ? 134.551 105.559 108.062 1.00 9.00   ? 2743 SER A C     1 
ATOM   10141 O  O     . SER A 1 2743 ? 135.273 104.556 108.155 1.00 8.97   ? 2743 SER A O     1 
ATOM   10142 C  CB    . SER A 1 2743 ? 132.977 106.164 109.925 1.00 6.90   ? 2743 SER A CB    1 
ATOM   10143 O  OG    . SER A 1 2743 ? 132.908 104.820 110.366 1.00 13.70  ? 2743 SER A OG    1 
ATOM   10144 N  N     . LEU A 1 2744 ? 133.937 105.897 106.925 1.00 7.48   ? 2744 LEU A N     1 
ATOM   10145 C  CA    . LEU A 1 2744 ? 134.158 105.132 105.703 1.00 6.79   ? 2744 LEU A CA    1 
ATOM   10146 C  C     . LEU A 1 2744 ? 135.626 105.166 105.310 1.00 5.69   ? 2744 LEU A C     1 
ATOM   10147 O  O     . LEU A 1 2744 ? 136.213 104.132 104.960 1.00 5.06   ? 2744 LEU A O     1 
ATOM   10148 C  CB    . LEU A 1 2744 ? 133.298 105.698 104.571 1.00 7.01   ? 2744 LEU A CB    1 
ATOM   10149 C  CG    . LEU A 1 2744 ? 131.778 105.534 104.638 1.00 8.88   ? 2744 LEU A CG    1 
ATOM   10150 C  CD1   . LEU A 1 2744 ? 131.115 106.206 103.443 1.00 8.48   ? 2744 LEU A CD1   1 
ATOM   10151 C  CD2   . LEU A 1 2744 ? 131.379 104.079 104.723 1.00 6.66   ? 2744 LEU A CD2   1 
ATOM   10152 N  N     . THR A 1 2745 ? 136.236 106.352 105.377 1.00 7.67   ? 2745 THR A N     1 
ATOM   10153 C  CA    . THR A 1 2745 ? 137.652 106.488 105.068 1.00 7.15   ? 2745 THR A CA    1 
ATOM   10154 C  C     . THR A 1 2745 ? 138.498 105.626 105.988 1.00 5.84   ? 2745 THR A C     1 
ATOM   10155 O  O     . THR A 1 2745 ? 139.398 104.926 105.525 1.00 6.20   ? 2745 THR A O     1 
ATOM   10156 C  CB    . THR A 1 2745 ? 138.076 107.953 105.168 1.00 6.47   ? 2745 THR A CB    1 
ATOM   10157 O  OG1   . THR A 1 2745 ? 137.380 108.723 104.179 1.00 9.21   ? 2745 THR A OG1   1 
ATOM   10158 C  CG2   . THR A 1 2745 ? 139.576 108.096 104.965 1.00 5.90   ? 2745 THR A CG2   1 
ATOM   10159 N  N     . GLN A 1 2746 ? 138.188 105.646 107.285 1.00 6.81   ? 2746 GLN A N     1 
ATOM   10160 C  CA    . GLN A 1 2746 ? 138.981 104.859 108.265 1.00 6.71   ? 2746 GLN A CA    1 
ATOM   10161 C  C     . GLN A 1 2746 ? 138.802 103.356 107.989 1.00 6.69   ? 2746 GLN A C     1 
ATOM   10162 O  O     . GLN A 1 2746 ? 139.829 102.658 107.838 1.00 8.55   ? 2746 GLN A O     1 
ATOM   10163 C  CB    . GLN A 1 2746 ? 138.559 105.233 109.686 1.00 12.51  ? 2746 GLN A CB    1 
ATOM   10164 C  CG    . GLN A 1 2746 ? 139.285 104.454 110.777 1.00 17.60  ? 2746 GLN A CG    1 
ATOM   10165 C  CD    . GLN A 1 2746 ? 138.535 103.223 111.235 1.00 24.12  ? 2746 GLN A CD    1 
ATOM   10166 O  OE1   . GLN A 1 2746 ? 137.429 102.930 110.768 1.00 25.00  ? 2746 GLN A OE1   1 
ATOM   10167 N  NE2   . GLN A 1 2746 ? 139.127 102.495 112.171 1.00 27.53  ? 2746 GLN A NE2   1 
ATOM   10168 N  N     . ILE A 1 2747 ? 137.555 102.883 107.906 1.00 5.56   ? 2747 ILE A N     1 
ATOM   10169 C  CA    . ILE A 1 2747 ? 137.288 101.422 107.731 1.00 5.21   ? 2747 ILE A CA    1 
ATOM   10170 C  C     . ILE A 1 2747 ? 137.918 100.911 106.424 1.00 5.60   ? 2747 ILE A C     1 
ATOM   10171 O  O     . ILE A 1 2747 ? 138.713 99.945  106.491 1.00 4.12   ? 2747 ILE A O     1 
ATOM   10172 C  CB    . ILE A 1 2747 ? 135.770 101.163 107.764 1.00 5.11   ? 2747 ILE A CB    1 
ATOM   10173 C  CG1   . ILE A 1 2747 ? 135.174 101.535 109.122 1.00 11.37  ? 2747 ILE A CG1   1 
ATOM   10174 C  CG2   . ILE A 1 2747 ? 135.447 99.720  107.380 1.00 4.36   ? 2747 ILE A CG2   1 
ATOM   10175 C  CD1   . ILE A 1 2747 ? 133.659 101.626 109.136 1.00 7.09   ? 2747 ILE A CD1   1 
ATOM   10176 N  N     . TYR A 1 2748 ? 137.595 101.535 105.289 1.00 5.45   ? 2748 TYR A N     1 
ATOM   10177 C  CA    . TYR A 1 2748 ? 138.093 101.022 103.981 1.00 3.59   ? 2748 TYR A CA    1 
ATOM   10178 C  C     . TYR A 1 2748 ? 139.560 101.418 103.804 1.00 4.21   ? 2748 TYR A C     1 
ATOM   10179 O  O     . TYR A 1 2748 ? 140.264 100.762 103.007 1.00 5.27   ? 2748 TYR A O     1 
ATOM   10180 C  CB    . TYR A 1 2748 ? 137.122 101.463 102.880 1.00 4.69   ? 2748 TYR A CB    1 
ATOM   10181 C  CG    . TYR A 1 2748 ? 135.781 100.757 103.026 1.00 3.75   ? 2748 TYR A CG    1 
ATOM   10182 C  CD1   . TYR A 1 2748 ? 135.566 99.506  102.462 1.00 2.97   ? 2748 TYR A CD1   1 
ATOM   10183 C  CD2   . TYR A 1 2748 ? 134.742 101.327 103.753 1.00 3.37   ? 2748 TYR A CD2   1 
ATOM   10184 C  CE1   . TYR A 1 2748 ? 134.358 98.846  102.607 1.00 3.37   ? 2748 TYR A CE1   1 
ATOM   10185 C  CE2   . TYR A 1 2748 ? 133.527 100.680 103.900 1.00 4.19   ? 2748 TYR A CE2   1 
ATOM   10186 C  CZ    . TYR A 1 2748 ? 133.334 99.436  103.326 1.00 3.89   ? 2748 TYR A CZ    1 
ATOM   10187 O  OH    . TYR A 1 2748 ? 132.139 98.795  103.468 1.00 4.61   ? 2748 TYR A OH    1 
ATOM   10188 N  N     . GLY A 1 2749 ? 140.013 102.452 104.519 1.00 4.70   ? 2749 GLY A N     1 
ATOM   10189 C  CA    . GLY A 1 2749 ? 141.447 102.795 104.473 1.00 4.05   ? 2749 GLY A CA    1 
ATOM   10190 C  C     . GLY A 1 2749 ? 142.248 101.653 105.064 1.00 5.19   ? 2749 GLY A C     1 
ATOM   10191 O  O     . GLY A 1 2749 ? 143.301 101.308 104.490 1.00 6.64   ? 2749 GLY A O     1 
ATOM   10192 N  N     . THR A 1 2750 ? 141.759 101.073 106.165 1.00 4.95   ? 2750 THR A N     1 
ATOM   10193 C  CA    . THR A 1 2750 ? 142.434 99.914  106.786 1.00 5.96   ? 2750 THR A CA    1 
ATOM   10194 C  C     . THR A 1 2750 ? 142.383 98.752  105.820 1.00 5.72   ? 2750 THR A C     1 
ATOM   10195 O  O     . THR A 1 2750 ? 143.406 98.045  105.688 1.00 6.32   ? 2750 THR A O     1 
ATOM   10196 C  CB    . THR A 1 2750 ? 141.751 99.579  108.111 1.00 5.64   ? 2750 THR A CB    1 
ATOM   10197 O  OG1   . THR A 1 2750 ? 141.877 100.755 108.904 1.00 12.34  ? 2750 THR A OG1   1 
ATOM   10198 C  CG2   . THR A 1 2750 ? 142.397 98.400  108.816 1.00 6.92   ? 2750 THR A CG2   1 
ATOM   10199 N  N     . PHE A 1 2751 ? 141.239 98.564  105.155 1.00 7.28   ? 2751 PHE A N     1 
ATOM   10200 C  CA    . PHE A 1 2751 ? 141.094 97.468  104.159 1.00 5.98   ? 2751 PHE A CA    1 
ATOM   10201 C  C     . PHE A 1 2751 ? 142.133 97.648  103.055 1.00 7.69   ? 2751 PHE A C     1 
ATOM   10202 O  O     . PHE A 1 2751 ? 142.812 96.661  102.695 1.00 9.04   ? 2751 PHE A O     1 
ATOM   10203 C  CB    . PHE A 1 2751 ? 139.683 97.481  103.565 1.00 4.95   ? 2751 PHE A CB    1 
ATOM   10204 C  CG    . PHE A 1 2751 ? 138.571 97.077  104.522 1.00 5.88   ? 2751 PHE A CG    1 
ATOM   10205 C  CD1   . PHE A 1 2751 ? 138.804 96.167  105.546 1.00 8.58   ? 2751 PHE A CD1   1 
ATOM   10206 C  CD2   . PHE A 1 2751 ? 137.291 97.604  104.389 1.00 6.92   ? 2751 PHE A CD2   1 
ATOM   10207 C  CE1   . PHE A 1 2751 ? 137.786 95.798  106.411 1.00 9.60   ? 2751 PHE A CE1   1 
ATOM   10208 C  CE2   . PHE A 1 2751 ? 136.277 97.232  105.257 1.00 7.38   ? 2751 PHE A CE2   1 
ATOM   10209 C  CZ    . PHE A 1 2751 ? 136.527 96.332  106.266 1.00 7.07   ? 2751 PHE A CZ    1 
ATOM   10210 N  N     . ASN A 1 2752 ? 142.263 98.872  102.536 1.00 4.76   ? 2752 ASN A N     1 
ATOM   10211 C  CA    . ASN A 1 2752 ? 143.202 99.123  101.406 1.00 6.27   ? 2752 ASN A CA    1 
ATOM   10212 C  C     . ASN A 1 2752 ? 144.642 98.883  101.875 1.00 8.87   ? 2752 ASN A C     1 
ATOM   10213 O  O     . ASN A 1 2752 ? 145.399 98.214  101.137 1.00 11.39  ? 2752 ASN A O     1 
ATOM   10214 C  CB    . ASN A 1 2752 ? 142.993 100.506 100.795 1.00 4.00   ? 2752 ASN A CB    1 
ATOM   10215 C  CG    . ASN A 1 2752 ? 141.724 100.579 99.979  1.00 4.80   ? 2752 ASN A CG    1 
ATOM   10216 O  OD1   . ASN A 1 2752 ? 141.419 101.623 99.394  1.00 9.03   ? 2752 ASN A OD1   1 
ATOM   10217 N  ND2   . ASN A 1 2752 ? 140.978 99.485  99.919  1.00 4.67   ? 2752 ASN A ND2   1 
ATOM   10218 N  N     . ARG A 1 2753 ? 145.001 99.395  103.056 1.00 8.81   ? 2753 ARG A N     1 
ATOM   10219 C  CA    . ARG A 1 2753 ? 146.347 99.182  103.572 1.00 11.65  ? 2753 ARG A CA    1 
ATOM   10220 C  C     . ARG A 1 2753 ? 146.639 97.697  103.727 1.00 11.47  ? 2753 ARG A C     1 
ATOM   10221 O  O     . ARG A 1 2753 ? 147.754 97.242  103.448 1.00 13.36  ? 2753 ARG A O     1 
ATOM   10222 C  CB    . ARG A 1 2753 ? 146.515 99.901  104.911 1.00 11.61  ? 2753 ARG A CB    1 
ATOM   10223 C  CG    . ARG A 1 2753 ? 146.812 101.383 104.794 1.00 19.56  ? 2753 ARG A CG    1 
ATOM   10224 C  CD    . ARG A 1 2753 ? 147.276 101.960 106.121 1.00 19.95  ? 2753 ARG A CD    1 
ATOM   10225 N  NE    . ARG A 1 2753 ? 146.509 101.433 107.244 1.00 15.35  ? 2753 ARG A NE    1 
ATOM   10226 C  CZ    . ARG A 1 2753 ? 145.379 101.961 107.695 1.00 15.81  ? 2753 ARG A CZ    1 
ATOM   10227 N  NH1   . ARG A 1 2753 ? 144.843 103.032 107.132 1.00 9.09   ? 2753 ARG A NH1   1 
ATOM   10228 N  NH2   . ARG A 1 2753 ? 144.771 101.399 108.735 1.00 15.83  ? 2753 ARG A NH2   1 
ATOM   10229 N  N     . ALA A 1 2754 ? 145.646 96.926  104.176 1.00 9.04   ? 2754 ALA A N     1 
ATOM   10230 C  CA    . ALA A 1 2754 ? 145.831 95.484  104.282 1.00 10.88  ? 2754 ALA A CA    1 
ATOM   10231 C  C     . ALA A 1 2754 ? 145.975 94.835  102.910 1.00 15.44  ? 2754 ALA A C     1 
ATOM   10232 O  O     . ALA A 1 2754 ? 146.824 93.957  102.717 1.00 18.82  ? 2754 ALA A O     1 
ATOM   10233 C  CB    . ALA A 1 2754 ? 144.662 94.869  105.048 1.00 13.87  ? 2754 ALA A CB    1 
ATOM   10234 N  N     . MET A 1 2755 ? 145.159 95.260  101.943 1.00 16.35  ? 2755 MET A N     1 
ATOM   10235 C  CA    . MET A 1 2755 ? 145.119 94.603  100.640 1.00 13.87  ? 2755 MET A CA    1 
ATOM   10236 C  C     . MET A 1 2755 ? 146.331 94.947  99.780  1.00 16.86  ? 2755 MET A C     1 
ATOM   10237 O  O     . MET A 1 2755 ? 146.858 94.078  99.078  1.00 21.98  ? 2755 MET A O     1 
ATOM   10238 C  CB    . MET A 1 2755 ? 143.821 94.972  99.918  1.00 12.64  ? 2755 MET A CB    1 
ATOM   10239 C  CG    . MET A 1 2755 ? 143.884 94.890  98.402  1.00 13.27  ? 2755 MET A CG    1 
ATOM   10240 S  SD    . MET A 1 2755 ? 142.494 95.731  97.623  1.00 16.96  ? 2755 MET A SD    1 
ATOM   10241 C  CE    . MET A 1 2755 ? 143.177 97.367  97.378  1.00 9.55   ? 2755 MET A CE    1 
ATOM   10242 N  N     . LEU A 1 2756 ? 146.796 96.193  99.823  1.00 14.32  ? 2756 LEU A N     1 
ATOM   10243 C  CA    . LEU A 1 2756 ? 147.910 96.618  98.987  1.00 16.17  ? 2756 LEU A CA    1 
ATOM   10244 C  C     . LEU A 1 2756 ? 149.267 96.257  99.573  1.00 20.89  ? 2756 LEU A C     1 
ATOM   10245 O  O     . LEU A 1 2756 ? 150.289 96.726  99.061  1.00 23.29  ? 2756 LEU A O     1 
ATOM   10246 C  CB    . LEU A 1 2756 ? 147.828 98.124  98.726  1.00 13.49  ? 2756 LEU A CB    1 
ATOM   10247 C  CG    . LEU A 1 2756 ? 146.748 98.561  97.732  1.00 16.76  ? 2756 LEU A CG    1 
ATOM   10248 C  CD1   . LEU A 1 2756 ? 146.979 99.982  97.246  1.00 17.14  ? 2756 LEU A CD1   1 
ATOM   10249 C  CD2   . LEU A 1 2756 ? 146.712 97.607  96.553  1.00 15.23  ? 2756 LEU A CD2   1 
ATOM   10250 N  N     . ARG A 1 2757 ? 149.306 95.444  100.629 1.00 23.18  ? 2757 ARG A N     1 
ATOM   10251 C  CA    . ARG A 1 2757 ? 150.556 94.818  101.034 1.00 20.13  ? 2757 ARG A CA    1 
ATOM   10252 C  C     . ARG A 1 2757 ? 150.929 93.650  100.134 1.00 24.06  ? 2757 ARG A C     1 
ATOM   10253 O  O     . ARG A 1 2757 ? 152.047 93.135  100.245 1.00 26.31  ? 2757 ARG A O     1 
ATOM   10254 C  CB    . ARG A 1 2757 ? 150.478 94.345  102.489 1.00 17.20  ? 2757 ARG A CB    1 
ATOM   10255 C  CG    . ARG A 1 2757 ? 150.440 95.472  103.507 1.00 16.67  ? 2757 ARG A CG    1 
ATOM   10256 C  CD    . ARG A 1 2757 ? 150.760 94.972  104.906 1.00 18.70  ? 2757 ARG A CD    1 
ATOM   10257 N  NE    . ARG A 1 2757 ? 149.623 94.315  105.538 1.00 23.73  ? 2757 ARG A NE    1 
ATOM   10258 C  CZ    . ARG A 1 2757 ? 148.724 94.933  106.292 1.00 22.52  ? 2757 ARG A CZ    1 
ATOM   10259 N  NH1   . ARG A 1 2757 ? 148.797 96.233  106.530 1.00 19.64  ? 2757 ARG A NH1   1 
ATOM   10260 N  NH2   . ARG A 1 2757 ? 147.730 94.229  106.824 1.00 24.93  ? 2757 ARG A NH2   1 
ATOM   10261 N  N     . LEU A 1 2758 ? 150.018 93.220  99.257  1.00 24.70  ? 2758 LEU A N     1 
ATOM   10262 C  CA    . LEU A 1 2758 ? 150.359 92.216  98.255  1.00 25.15  ? 2758 LEU A CA    1 
ATOM   10263 C  C     . LEU A 1 2758 ? 151.439 92.737  97.315  1.00 26.14  ? 2758 LEU A C     1 
ATOM   10264 O  O     . LEU A 1 2758 ? 152.411 92.035  97.014  1.00 33.40  ? 2758 LEU A O     1 
ATOM   10265 C  CB    . LEU A 1 2758 ? 149.108 91.817  97.471  1.00 24.14  ? 2758 LEU A CB    1 
ATOM   10266 C  CG    . LEU A 1 2758 ? 147.989 91.117  98.244  1.00 28.17  ? 2758 LEU A CG    1 
ATOM   10267 C  CD1   . LEU A 1 2758 ? 146.799 90.851  97.335  1.00 21.71  ? 2758 LEU A CD1   1 
ATOM   10268 C  CD2   . LEU A 1 2758 ? 148.489 89.824  98.868  1.00 23.64  ? 2758 LEU A CD2   1 
ATOM   10269 N  N     . ILE A 1 2759 ? 151.283 93.969  96.844  1.00 25.40  ? 2759 ILE A N     1 
ATOM   10270 C  CA    . ILE A 1 2759 ? 152.288 94.621  96.009  1.00 26.89  ? 2759 ILE A CA    1 
ATOM   10271 C  C     . ILE A 1 2759 ? 152.932 95.735  96.825  1.00 28.02  ? 2759 ILE A C     1 
ATOM   10272 O  O     . ILE A 1 2759 ? 152.314 96.792  97.017  1.00 33.17  ? 2759 ILE A O     1 
ATOM   10273 C  CB    . ILE A 1 2759 ? 151.673 95.168  94.711  1.00 28.30  ? 2759 ILE A CB    1 
ATOM   10274 C  CG1   . ILE A 1 2759 ? 150.764 94.121  94.065  1.00 27.92  ? 2759 ILE A CG1   1 
ATOM   10275 C  CG2   . ILE A 1 2759 ? 152.766 95.591  93.742  1.00 28.06  ? 2759 ILE A CG2   1 
ATOM   10276 C  CD1   . ILE A 1 2759 ? 151.488 92.879  93.615  1.00 31.13  ? 2759 ILE A CD1   1 
ATOM   10277 N  N     . PRO A 1 2760 ? 154.152 95.543  97.333  1.00 30.36  ? 2760 PRO A N     1 
ATOM   10278 C  CA    . PRO A 1 2760 ? 154.790 96.604  98.129  1.00 33.73  ? 2760 PRO A CA    1 
ATOM   10279 C  C     . PRO A 1 2760 ? 154.947 97.917  97.383  1.00 32.69  ? 2760 PRO A C     1 
ATOM   10280 O  O     . PRO A 1 2760 ? 154.778 98.986  97.986  1.00 38.40  ? 2760 PRO A O     1 
ATOM   10281 C  CB    . PRO A 1 2760 ? 156.151 95.992  98.484  1.00 40.05  ? 2760 PRO A CB    1 
ATOM   10282 C  CG    . PRO A 1 2760 ? 155.892 94.523  98.502  1.00 35.39  ? 2760 PRO A CG    1 
ATOM   10283 C  CD    . PRO A 1 2760 ? 154.920 94.286  97.376  1.00 32.26  ? 2760 PRO A CD    1 
ATOM   10284 N  N     . SER A 1 2761 ? 155.231 97.870  96.080  1.00 26.01  ? 2761 SER A N     1 
ATOM   10285 C  CA    . SER A 1 2761 ? 155.465 99.081  95.302  1.00 27.55  ? 2761 SER A CA    1 
ATOM   10286 C  C     . SER A 1 2761 ? 154.232 99.967  95.205  1.00 27.47  ? 2761 SER A C     1 
ATOM   10287 O  O     . SER A 1 2761 ? 154.353 101.124 94.789  1.00 29.59  ? 2761 SER A O     1 
ATOM   10288 C  CB    . SER A 1 2761 ? 155.948 98.714  93.897  1.00 36.11  ? 2761 SER A CB    1 
ATOM   10289 O  OG    . SER A 1 2761 ? 154.927 98.067  93.158  1.00 38.57  ? 2761 SER A OG    1 
ATOM   10290 N  N     . LEU A 1 2762 ? 153.059 99.457  95.574  1.00 29.45  ? 2762 LEU A N     1 
ATOM   10291 C  CA    . LEU A 1 2762 ? 151.823 100.224 95.554  1.00 28.84  ? 2762 LEU A CA    1 
ATOM   10292 C  C     . LEU A 1 2762 ? 151.405 100.688 96.944  1.00 30.12  ? 2762 LEU A C     1 
ATOM   10293 O  O     . LEU A 1 2762 ? 150.319 101.262 97.095  1.00 29.14  ? 2762 LEU A O     1 
ATOM   10294 C  CB    . LEU A 1 2762 ? 150.711 99.391  94.912  1.00 30.90  ? 2762 LEU A CB    1 
ATOM   10295 C  CG    . LEU A 1 2762 ? 150.861 99.152  93.407  1.00 27.74  ? 2762 LEU A CG    1 
ATOM   10296 C  CD1   . LEU A 1 2762 ? 149.683 98.365  92.854  1.00 18.96  ? 2762 LEU A CD1   1 
ATOM   10297 C  CD2   . LEU A 1 2762 ? 151.019 100.473 92.669  1.00 21.97  ? 2762 LEU A CD2   1 
ATOM   10298 N  N     . ARG A 1 2763 ? 152.251 100.473 97.960  1.00 33.78  ? 2763 ARG A N     1 
ATOM   10299 C  CA    . ARG A 1 2763 ? 151.864 100.783 99.335  1.00 28.60  ? 2763 ARG A CA    1 
ATOM   10300 C  C     . ARG A 1 2763 ? 151.488 102.250 99.505  1.00 26.14  ? 2763 ARG A C     1 
ATOM   10301 O  O     . ARG A 1 2763 ? 150.430 102.557 100.071 1.00 26.50  ? 2763 ARG A O     1 
ATOM   10302 C  CB    . ARG A 1 2763 ? 152.994 100.415 100.296 1.00 31.08  ? 2763 ARG A CB    1 
ATOM   10303 C  CG    . ARG A 1 2763 ? 152.691 100.726 101.755 1.00 37.51  ? 2763 ARG A CG    1 
ATOM   10304 C  CD    . ARG A 1 2763 ? 153.927 101.218 102.497 1.00 37.81  ? 2763 ARG A CD    1 
ATOM   10305 N  NE    . ARG A 1 2763 ? 154.415 102.495 101.987 1.00 41.32  ? 2763 ARG A NE    1 
ATOM   10306 C  CZ    . ARG A 1 2763 ? 153.804 103.659 102.159 1.00 46.25  ? 2763 ARG A CZ    1 
ATOM   10307 N  NH1   . ARG A 1 2763 ? 152.674 103.754 102.842 1.00 38.91  ? 2763 ARG A NH1   1 
ATOM   10308 N  NH2   . ARG A 1 2763 ? 154.343 104.758 101.639 1.00 44.27  ? 2763 ARG A NH2   1 
ATOM   10309 N  N     . THR A 1 2764 ? 152.311 103.162 98.983  1.00 25.59  ? 2764 THR A N     1 
ATOM   10310 C  CA    . THR A 1 2764 ? 152.049 104.592 99.094  1.00 28.30  ? 2764 THR A CA    1 
ATOM   10311 C  C     . THR A 1 2764 ? 150.725 105.008 98.467  1.00 24.18  ? 2764 THR A C     1 
ATOM   10312 O  O     . THR A 1 2764 ? 150.331 106.169 98.613  1.00 25.60  ? 2764 THR A O     1 
ATOM   10313 C  CB    . THR A 1 2764 ? 153.184 105.385 98.444  1.00 33.85  ? 2764 THR A CB    1 
ATOM   10314 O  OG1   . THR A 1 2764 ? 152.922 106.788 98.569  1.00 40.01  ? 2764 THR A OG1   1 
ATOM   10315 C  CG2   . THR A 1 2764 ? 153.298 105.030 96.971  1.00 29.63  ? 2764 THR A CG2   1 
ATOM   10316 N  N     . TYR A 1 2765 ? 150.034 104.102 97.778  1.00 19.59  ? 2765 TYR A N     1 
ATOM   10317 C  CA    . TYR A 1 2765 ? 148.756 104.414 97.159  1.00 17.02  ? 2765 TYR A CA    1 
ATOM   10318 C  C     . TYR A 1 2765 ? 147.567 103.959 97.995  1.00 14.85  ? 2765 TYR A C     1 
ATOM   10319 O  O     . TYR A 1 2765 ? 146.445 103.920 97.481  1.00 14.11  ? 2765 TYR A O     1 
ATOM   10320 C  CB    . TYR A 1 2765 ? 148.688 103.802 95.759  1.00 19.95  ? 2765 TYR A CB    1 
ATOM   10321 C  CG    . TYR A 1 2765 ? 149.710 104.370 94.801  1.00 20.73  ? 2765 TYR A CG    1 
ATOM   10322 C  CD1   . TYR A 1 2765 ? 149.526 105.620 94.227  1.00 19.08  ? 2765 TYR A CD1   1 
ATOM   10323 C  CD2   . TYR A 1 2765 ? 150.855 103.658 94.469  1.00 23.39  ? 2765 TYR A CD2   1 
ATOM   10324 C  CE1   . TYR A 1 2765 ? 150.453 106.148 93.350  1.00 20.40  ? 2765 TYR A CE1   1 
ATOM   10325 C  CE2   . TYR A 1 2765 ? 151.789 104.179 93.591  1.00 18.22  ? 2765 TYR A CE2   1 
ATOM   10326 C  CZ    . TYR A 1 2765 ? 151.581 105.424 93.035  1.00 22.00  ? 2765 TYR A CZ    1 
ATOM   10327 O  OH    . TYR A 1 2765 ? 152.504 105.951 92.162  1.00 25.49  ? 2765 TYR A OH    1 
ATOM   10328 N  N     . ALA A 1 2766 ? 147.783 103.608 99.266  1.00 18.49  ? 2766 ALA A N     1 
ATOM   10329 C  CA    . ALA A 1 2766 ? 146.658 103.244 100.125 1.00 12.36  ? 2766 ALA A CA    1 
ATOM   10330 C  C     . ALA A 1 2766 ? 145.706 104.418 100.327 1.00 13.16  ? 2766 ALA A C     1 
ATOM   10331 O  O     . ALA A 1 2766 ? 144.495 104.293 100.108 1.00 12.79  ? 2766 ALA A O     1 
ATOM   10332 C  CB    . ALA A 1 2766 ? 147.167 102.738 101.474 1.00 14.96  ? 2766 ALA A CB    1 
ATOM   10333 N  N     . GLU A 1 2767 ? 146.237 105.567 100.749 1.00 13.26  ? 2767 GLU A N     1 
ATOM   10334 C  CA    . GLU A 1 2767 ? 145.382 106.711 101.063 1.00 12.60  ? 2767 GLU A CA    1 
ATOM   10335 C  C     . GLU A 1 2767 ? 144.638 107.266 99.854  1.00 10.09  ? 2767 GLU A C     1 
ATOM   10336 O  O     . GLU A 1 2767 ? 143.420 107.495 99.965  1.00 8.54   ? 2767 GLU A O     1 
ATOM   10337 C  CB    . GLU A 1 2767 ? 146.209 107.798 101.759 1.00 13.94  ? 2767 GLU A CB    1 
ATOM   10338 C  CG    . GLU A 1 2767 ? 146.334 107.630 103.269 1.00 18.29  ? 2767 GLU A CG    1 
ATOM   10339 C  CD    . GLU A 1 2767 ? 145.015 107.826 104.000 1.00 31.88  ? 2767 GLU A CD    1 
ATOM   10340 O  OE1   . GLU A 1 2767 ? 144.143 106.933 103.926 1.00 27.38  ? 2767 GLU A OE1   1 
ATOM   10341 O  OE2   . GLU A 1 2767 ? 144.848 108.881 104.648 1.00 27.24  ? 2767 GLU A OE2   1 
ATOM   10342 N  N     . PRO A 1 2768 ? 145.271 107.524 98.701  1.00 12.37  ? 2768 PRO A N     1 
ATOM   10343 C  CA    . PRO A 1 2768 ? 144.491 108.044 97.564  1.00 10.90  ? 2768 PRO A CA    1 
ATOM   10344 C  C     . PRO A 1 2768 ? 143.402 107.096 97.101  1.00 9.00   ? 2768 PRO A C     1 
ATOM   10345 O  O     . PRO A 1 2768 ? 142.247 107.523 96.957  1.00 12.57  ? 2768 PRO A O     1 
ATOM   10346 C  CB    . PRO A 1 2768 ? 145.551 108.264 96.475  1.00 9.37   ? 2768 PRO A CB    1 
ATOM   10347 C  CG    . PRO A 1 2768 ? 146.715 107.441 96.887  1.00 13.08  ? 2768 PRO A CG    1 
ATOM   10348 C  CD    . PRO A 1 2768 ? 146.707 107.451 98.378  1.00 12.97  ? 2768 PRO A CD    1 
ATOM   10349 N  N     . LEU A 1 2769 ? 143.727 105.813 96.908  1.00 6.72   ? 2769 LEU A N     1 
ATOM   10350 C  CA    . LEU A 1 2769 ? 142.744 104.855 96.412  1.00 7.44   ? 2769 LEU A CA    1 
ATOM   10351 C  C     . LEU A 1 2769 ? 141.490 104.869 97.271  1.00 6.67   ? 2769 LEU A C     1 
ATOM   10352 O  O     . LEU A 1 2769 ? 140.383 105.104 96.768  1.00 6.10   ? 2769 LEU A O     1 
ATOM   10353 C  CB    . LEU A 1 2769 ? 143.356 103.454 96.385  1.00 8.90   ? 2769 LEU A CB    1 
ATOM   10354 C  CG    . LEU A 1 2769 ? 142.507 102.310 95.828  1.00 5.94   ? 2769 LEU A CG    1 
ATOM   10355 C  CD1   . LEU A 1 2769 ? 142.384 102.419 94.317  1.00 5.01   ? 2769 LEU A CD1   1 
ATOM   10356 C  CD2   . LEU A 1 2769 ? 143.088 100.965 96.231  1.00 6.28   ? 2769 LEU A CD2   1 
ATOM   10357 N  N     . THR A 1 2770 ? 141.658 104.689 98.586  1.00 6.39   ? 2770 THR A N     1 
ATOM   10358 C  CA    . THR A 1 2770 ? 140.521 104.766 99.494  1.00 6.53   ? 2770 THR A CA    1 
ATOM   10359 C  C     . THR A 1 2770 ? 139.751 106.056 99.281  1.00 3.93   ? 2770 THR A C     1 
ATOM   10360 O  O     . THR A 1 2770 ? 138.538 106.028 99.028  1.00 3.21   ? 2770 THR A O     1 
ATOM   10361 C  CB    . THR A 1 2770 ? 140.992 104.668 100.946 1.00 6.59   ? 2770 THR A CB    1 
ATOM   10362 O  OG1   . THR A 1 2770 ? 141.720 103.449 101.138 1.00 5.71   ? 2770 THR A OG1   1 
ATOM   10363 C  CG2   . THR A 1 2770 ? 139.805 104.710 101.898 1.00 4.09   ? 2770 THR A CG2   1 
ATOM   10364 N  N     . ALA A 1 2771 ? 140.457 107.192 99.302  1.00 4.16   ? 2771 ALA A N     1 
ATOM   10365 C  CA    . ALA A 1 2771 ? 139.799 108.470 99.074  1.00 5.39   ? 2771 ALA A CA    1 
ATOM   10366 C  C     . ALA A 1 2771 ? 138.995 108.427 97.787  1.00 5.38   ? 2771 ALA A C     1 
ATOM   10367 O  O     . ALA A 1 2771 ? 137.787 108.704 97.792  1.00 5.45   ? 2771 ALA A O     1 
ATOM   10368 C  CB    . ALA A 1 2771 ? 140.831 109.595 99.032  1.00 5.86   ? 2771 ALA A CB    1 
ATOM   10369 N  N     . ALA A 1 2772 ? 139.628 107.983 96.698  1.00 3.97   ? 2772 ALA A N     1 
ATOM   10370 C  CA    . ALA A 1 2772 ? 138.923 107.893 95.428  1.00 4.32   ? 2772 ALA A CA    1 
ATOM   10371 C  C     . ALA A 1 2772 ? 137.641 107.098 95.589  1.00 3.79   ? 2772 ALA A C     1 
ATOM   10372 O  O     . ALA A 1 2772 ? 136.547 107.616 95.317  1.00 5.28   ? 2772 ALA A O     1 
ATOM   10373 C  CB    . ALA A 1 2772 ? 139.824 107.256 94.374  1.00 4.37   ? 2772 ALA A CB    1 
ATOM   10374 N  N     . MET A 1 2773 ? 137.747 105.885 96.144  1.00 2.82   ? 2773 MET A N     1 
ATOM   10375 C  CA    . MET A 1 2773 ? 136.560 105.068 96.348  1.00 3.03   ? 2773 MET A CA    1 
ATOM   10376 C  C     . MET A 1 2773 ? 135.491 105.878 97.055  1.00 3.56   ? 2773 MET A C     1 
ATOM   10377 O  O     . MET A 1 2773 ? 134.401 106.102 96.508  1.00 4.89   ? 2773 MET A O     1 
ATOM   10378 C  CB    . MET A 1 2773 ? 136.901 103.823 97.167  1.00 2.88   ? 2773 MET A CB    1 
ATOM   10379 C  CG    . MET A 1 2773 ? 137.800 102.819 96.487  1.00 4.26   ? 2773 MET A CG    1 
ATOM   10380 S  SD    . MET A 1 2773 ? 138.114 101.418 97.577  1.00 9.64   ? 2773 MET A SD    1 
ATOM   10381 C  CE    . MET A 1 2773 ? 139.252 100.464 96.588  1.00 5.22   ? 2773 MET A CE    1 
ATOM   10382 N  N     . VAL A 1 2774 ? 135.848 106.444 98.212  1.00 3.93   ? 2774 VAL A N     1 
ATOM   10383 C  CA    . VAL A 1 2774 ? 134.865 107.158 99.014  1.00 4.07   ? 2774 VAL A CA    1 
ATOM   10384 C  C     . VAL A 1 2774 ? 134.204 108.229 98.167  1.00 3.97   ? 2774 VAL A C     1 
ATOM   10385 O  O     . VAL A 1 2774 ? 132.977 108.233 97.991  1.00 5.41   ? 2774 VAL A O     1 
ATOM   10386 C  CB    . VAL A 1 2774 ? 135.524 107.754 100.271 1.00 4.87   ? 2774 VAL A CB    1 
ATOM   10387 C  CG1   . VAL A 1 2774 ? 134.545 108.650 101.013 1.00 5.31   ? 2774 VAL A CG1   1 
ATOM   10388 C  CG2   . VAL A 1 2774 ? 136.036 106.647 101.180 1.00 3.62   ? 2774 VAL A CG2   1 
ATOM   10389 N  N     . GLU A 1 2775 ? 135.022 109.061 97.513  1.00 3.51   ? 2775 GLU A N     1 
ATOM   10390 C  CA    . GLU A 1 2775 ? 134.454 110.156 96.741  1.00 5.74   ? 2775 GLU A CA    1 
ATOM   10391 C  C     . GLU A 1 2775 ? 133.472 109.615 95.721  1.00 5.90   ? 2775 GLU A C     1 
ATOM   10392 O  O     . GLU A 1 2775 ? 132.286 109.972 95.735  1.00 6.54   ? 2775 GLU A O     1 
ATOM   10393 C  CB    . GLU A 1 2775 ? 135.555 110.964 96.055  1.00 8.02   ? 2775 GLU A CB    1 
ATOM   10394 C  CG    . GLU A 1 2775 ? 135.015 112.156 95.278  1.00 12.32  ? 2775 GLU A CG    1 
ATOM   10395 C  CD    . GLU A 1 2775 ? 136.103 112.993 94.644  1.00 18.97  ? 2775 GLU A CD    1 
ATOM   10396 O  OE1   . GLU A 1 2775 ? 137.288 112.642 94.799  1.00 21.44  ? 2775 GLU A OE1   1 
ATOM   10397 O  OE2   . GLU A 1 2775 ? 135.773 114.003 93.988  1.00 28.91  ? 2775 GLU A OE2   1 
ATOM   10398 N  N     . PHE A 1 2776 ? 133.920 108.650 94.911  1.00 3.95   ? 2776 PHE A N     1 
ATOM   10399 C  CA    . PHE A 1 2776 ? 133.036 108.143 93.875  1.00 5.05   ? 2776 PHE A CA    1 
ATOM   10400 C  C     . PHE A 1 2776 ? 131.784 107.564 94.502  1.00 5.15   ? 2776 PHE A C     1 
ATOM   10401 O  O     . PHE A 1 2776 ? 130.665 107.933 94.119  1.00 6.36   ? 2776 PHE A O     1 
ATOM   10402 C  CB    . PHE A 1 2776 ? 133.748 107.099 93.017  1.00 5.17   ? 2776 PHE A CB    1 
ATOM   10403 C  CG    . PHE A 1 2776 ? 132.924 106.619 91.861  1.00 5.67   ? 2776 PHE A CG    1 
ATOM   10404 C  CD1   . PHE A 1 2776 ? 132.790 107.398 90.725  1.00 5.75   ? 2776 PHE A CD1   1 
ATOM   10405 C  CD2   . PHE A 1 2776 ? 132.267 105.403 91.915  1.00 4.96   ? 2776 PHE A CD2   1 
ATOM   10406 C  CE1   . PHE A 1 2776 ? 132.023 106.970 89.661  1.00 6.19   ? 2776 PHE A CE1   1 
ATOM   10407 C  CE2   . PHE A 1 2776 ? 131.500 104.968 90.853  1.00 4.79   ? 2776 PHE A CE2   1 
ATOM   10408 C  CZ    . PHE A 1 2776 ? 131.378 105.753 89.724  1.00 5.90   ? 2776 PHE A CZ    1 
ATOM   10409 N  N     . TYR A 1 2777 ? 131.957 106.746 95.547  1.00 4.14   ? 2777 TYR A N     1 
ATOM   10410 C  CA    . TYR A 1 2777 ? 130.797 106.157 96.197  1.00 5.58   ? 2777 TYR A CA    1 
ATOM   10411 C  C     . TYR A 1 2777 ? 129.844 107.249 96.642  1.00 5.92   ? 2777 TYR A C     1 
ATOM   10412 O  O     . TYR A 1 2777 ? 128.658 107.232 96.286  1.00 6.40   ? 2777 TYR A O     1 
ATOM   10413 C  CB    . TYR A 1 2777 ? 131.232 105.300 97.386  1.00 4.63   ? 2777 TYR A CB    1 
ATOM   10414 C  CG    . TYR A 1 2777 ? 130.132 105.073 98.396  1.00 6.58   ? 2777 TYR A CG    1 
ATOM   10415 C  CD1   . TYR A 1 2777 ? 129.103 104.178 98.135  1.00 6.42   ? 2777 TYR A CD1   1 
ATOM   10416 C  CD2   . TYR A 1 2777 ? 130.109 105.765 99.599  1.00 6.62   ? 2777 TYR A CD2   1 
ATOM   10417 C  CE1   . TYR A 1 2777 ? 128.090 103.968 99.049  1.00 5.81   ? 2777 TYR A CE1   1 
ATOM   10418 C  CE2   . TYR A 1 2777 ? 129.097 105.566 100.517 1.00 6.36   ? 2777 TYR A CE2   1 
ATOM   10419 C  CZ    . TYR A 1 2777 ? 128.092 104.664 100.238 1.00 6.66   ? 2777 TYR A CZ    1 
ATOM   10420 O  OH    . TYR A 1 2777 ? 127.083 104.458 101.149 1.00 10.47  ? 2777 TYR A OH    1 
ATOM   10421 N  N     . THR A 1 2778 ? 130.374 108.265 97.330  1.00 5.17   ? 2778 THR A N     1 
ATOM   10422 C  CA    . THR A 1 2778 ? 129.519 109.339 97.811  1.00 8.36   ? 2778 THR A CA    1 
ATOM   10423 C  C     . THR A 1 2778 ? 128.786 109.986 96.650  1.00 8.13   ? 2778 THR A C     1 
ATOM   10424 O  O     . THR A 1 2778 ? 127.554 110.110 96.675  1.00 8.11   ? 2778 THR A O     1 
ATOM   10425 C  CB    . THR A 1 2778 ? 130.349 110.369 98.577  1.00 10.08  ? 2778 THR A CB    1 
ATOM   10426 O  OG1   . THR A 1 2778 ? 131.082 109.713 99.618  1.00 6.44   ? 2778 THR A OG1   1 
ATOM   10427 C  CG2   . THR A 1 2778 ? 129.449 111.421 99.197  1.00 12.87  ? 2778 THR A CG2   1 
ATOM   10428 N  N     . MET A 1 2779 ? 129.518 110.310 95.579  1.00 9.19   ? 2779 MET A N     1 
ATOM   10429 C  CA    . MET A 1 2779 ? 128.879 110.934 94.429  1.00 7.51   ? 2779 MET A CA    1 
ATOM   10430 C  C     . MET A 1 2779 ? 127.796 110.028 93.871  1.00 9.48   ? 2779 MET A C     1 
ATOM   10431 O  O     . MET A 1 2779 ? 126.669 110.476 93.619  1.00 10.55  ? 2779 MET A O     1 
ATOM   10432 C  CB    . MET A 1 2779 ? 129.923 111.262 93.364  1.00 8.30   ? 2779 MET A CB    1 
ATOM   10433 C  CG    . MET A 1 2779 ? 130.923 112.320 93.792  1.00 13.14  ? 2779 MET A CG    1 
ATOM   10434 S  SD    . MET A 1 2779 ? 132.417 112.304 92.788  1.00 26.45  ? 2779 MET A SD    1 
ATOM   10435 C  CE    . MET A 1 2779 ? 131.711 112.312 91.145  1.00 15.06  ? 2779 MET A CE    1 
ATOM   10436 N  N     . SER A 1 2780 ? 128.095 108.733 93.747  1.00 7.60   ? 2780 SER A N     1 
ATOM   10437 C  CA    . SER A 1 2780 ? 127.086 107.805 93.261  1.00 7.59   ? 2780 SER A CA    1 
ATOM   10438 C  C     . SER A 1 2780 ? 125.879 107.806 94.184  1.00 9.21   ? 2780 SER A C     1 
ATOM   10439 O  O     . SER A 1 2780 ? 124.736 107.919 93.723  1.00 10.26  ? 2780 SER A O     1 
ATOM   10440 C  CB    . SER A 1 2780 ? 127.678 106.403 93.139  1.00 8.45   ? 2780 SER A CB    1 
ATOM   10441 O  OG    . SER A 1 2780 ? 128.838 106.411 92.325  1.00 8.00   ? 2780 SER A OG    1 
ATOM   10442 N  N     . GLN A 1 2781 ? 126.123 107.763 95.497  1.00 10.74  ? 2781 GLN A N     1 
ATOM   10443 C  CA    . GLN A 1 2781 ? 125.018 107.714 96.444  1.00 9.27   ? 2781 GLN A CA    1 
ATOM   10444 C  C     . GLN A 1 2781 ? 124.196 108.993 96.390  1.00 12.49  ? 2781 GLN A C     1 
ATOM   10445 O  O     . GLN A 1 2781 ? 123.026 108.995 96.789  1.00 17.37  ? 2781 GLN A O     1 
ATOM   10446 C  CB    . GLN A 1 2781 ? 125.556 107.452 97.851  1.00 9.79   ? 2781 GLN A CB    1 
ATOM   10447 C  CG    . GLN A 1 2781 ? 124.496 107.216 98.909  1.00 12.48  ? 2781 GLN A CG    1 
ATOM   10448 C  CD    . GLN A 1 2781 ? 125.094 106.899 100.264 1.00 18.73  ? 2781 GLN A CD    1 
ATOM   10449 O  OE1   . GLN A 1 2781 ? 124.759 105.889 100.882 1.00 13.57  ? 2781 GLN A OE1   1 
ATOM   10450 N  NE2   . GLN A 1 2781 ? 125.990 107.760 100.731 1.00 20.01  ? 2781 GLN A NE2   1 
ATOM   10451 N  N     . GLU A 1 2782 ? 124.778 110.081 95.880  1.00 11.02  ? 2782 GLU A N     1 
ATOM   10452 C  CA    . GLU A 1 2782 ? 124.001 111.302 95.708  1.00 13.50  ? 2782 GLU A CA    1 
ATOM   10453 C  C     . GLU A 1 2782 ? 123.328 111.335 94.342  1.00 15.91  ? 2782 GLU A C     1 
ATOM   10454 O  O     . GLU A 1 2782 ? 122.227 111.879 94.200  1.00 18.76  ? 2782 GLU A O     1 
ATOM   10455 C  CB    . GLU A 1 2782 ? 124.893 112.528 95.899  1.00 19.25  ? 2782 GLU A CB    1 
ATOM   10456 C  CG    . GLU A 1 2782 ? 124.121 113.817 96.126  1.00 30.45  ? 2782 GLU A CG    1 
ATOM   10457 C  CD    . GLU A 1 2782 ? 124.966 114.900 96.765  1.00 49.66  ? 2782 GLU A CD    1 
ATOM   10458 O  OE1   . GLU A 1 2782 ? 125.195 115.940 96.113  1.00 48.41  ? 2782 GLU A OE1   1 
ATOM   10459 O  OE2   . GLU A 1 2782 ? 125.400 114.712 97.921  1.00 57.13  ? 2782 GLU A OE2   1 
ATOM   10460 N  N     . ARG A 1 2783 ? 123.971 110.754 93.327  1.00 13.85  ? 2783 ARG A N     1 
ATOM   10461 C  CA    . ARG A 1 2783 ? 123.475 110.916 91.965  1.00 9.97   ? 2783 ARG A CA    1 
ATOM   10462 C  C     . ARG A 1 2783 ? 122.273 110.017 91.698  1.00 11.38  ? 2783 ARG A C     1 
ATOM   10463 O  O     . ARG A 1 2783 ? 121.372 110.387 90.937  1.00 13.58  ? 2783 ARG A O     1 
ATOM   10464 C  CB    . ARG A 1 2783 ? 124.599 110.635 90.969  1.00 11.30  ? 2783 ARG A CB    1 
ATOM   10465 C  CG    . ARG A 1 2783 ? 124.173 110.613 89.513  1.00 13.75  ? 2783 ARG A CG    1 
ATOM   10466 C  CD    . ARG A 1 2783 ? 123.944 112.015 88.974  1.00 11.43  ? 2783 ARG A CD    1 
ATOM   10467 N  NE    . ARG A 1 2783 ? 123.722 112.021 87.532  1.00 18.09  ? 2783 ARG A NE    1 
ATOM   10468 C  CZ    . ARG A 1 2783 ? 122.629 111.566 86.934  1.00 24.93  ? 2783 ARG A CZ    1 
ATOM   10469 N  NH1   . ARG A 1 2783 ? 121.612 111.078 87.626  1.00 23.35  ? 2783 ARG A NH1   1 
ATOM   10470 N  NH2   . ARG A 1 2783 ? 122.550 111.609 85.607  1.00 22.31  ? 2783 ARG A NH2   1 
ATOM   10471 N  N     . PHE A 1 2784 ? 122.232 108.844 92.325  1.00 10.61  ? 2784 PHE A N     1 
ATOM   10472 C  CA    . PHE A 1 2784 ? 121.194 107.853 92.075  1.00 11.44  ? 2784 PHE A CA    1 
ATOM   10473 C  C     . PHE A 1 2784 ? 120.530 107.483 93.392  1.00 13.43  ? 2784 PHE A C     1 
ATOM   10474 O  O     . PHE A 1 2784 ? 121.195 106.989 94.309  1.00 17.42  ? 2784 PHE A O     1 
ATOM   10475 C  CB    . PHE A 1 2784 ? 121.779 106.613 91.398  1.00 10.49  ? 2784 PHE A CB    1 
ATOM   10476 C  CG    . PHE A 1 2784 ? 122.641 106.926 90.212  1.00 11.07  ? 2784 PHE A CG    1 
ATOM   10477 C  CD1   . PHE A 1 2784 ? 122.084 107.419 89.045  1.00 11.53  ? 2784 PHE A CD1   1 
ATOM   10478 C  CD2   . PHE A 1 2784 ? 124.010 106.730 90.264  1.00 10.61  ? 2784 PHE A CD2   1 
ATOM   10479 C  CE1   . PHE A 1 2784 ? 122.876 107.708 87.953  1.00 10.95  ? 2784 PHE A CE1   1 
ATOM   10480 C  CE2   . PHE A 1 2784 ? 124.807 107.017 89.173  1.00 11.22  ? 2784 PHE A CE2   1 
ATOM   10481 C  CZ    . PHE A 1 2784 ? 124.238 107.505 88.015  1.00 9.92   ? 2784 PHE A CZ    1 
ATOM   10482 N  N     . THR A 1 2785 ? 119.223 107.714 93.481  1.00 14.50  ? 2785 THR A N     1 
ATOM   10483 C  CA    . THR A 1 2785 ? 118.451 107.440 94.682  1.00 18.30  ? 2785 THR A CA    1 
ATOM   10484 C  C     . THR A 1 2785 ? 117.230 106.604 94.321  1.00 17.04  ? 2785 THR A C     1 
ATOM   10485 O  O     . THR A 1 2785 ? 116.936 106.363 93.148  1.00 17.24  ? 2785 THR A O     1 
ATOM   10486 C  CB    . THR A 1 2785 ? 118.015 108.736 95.382  1.00 20.70  ? 2785 THR A CB    1 
ATOM   10487 O  OG1   . THR A 1 2785 ? 117.126 109.468 94.529  1.00 22.63  ? 2785 THR A OG1   1 
ATOM   10488 C  CG2   . THR A 1 2785 ? 119.223 109.602 95.712  1.00 18.52  ? 2785 THR A CG2   1 
ATOM   10489 N  N     . GLN A 1 2786 ? 116.511 106.165 95.357  1.00 21.01  ? 2786 GLN A N     1 
ATOM   10490 C  CA    . GLN A 1 2786 ? 115.317 105.351 95.153  1.00 19.53  ? 2786 GLN A CA    1 
ATOM   10491 C  C     . GLN A 1 2786 ? 114.201 106.115 94.453  1.00 23.18  ? 2786 GLN A C     1 
ATOM   10492 O  O     . GLN A 1 2786 ? 113.274 105.486 93.931  1.00 24.02  ? 2786 GLN A O     1 
ATOM   10493 C  CB    . GLN A 1 2786 ? 114.812 104.809 96.491  1.00 22.44  ? 2786 GLN A CB    1 
ATOM   10494 C  CG    . GLN A 1 2786 ? 115.619 103.644 97.034  1.00 24.79  ? 2786 GLN A CG    1 
ATOM   10495 C  CD    . GLN A 1 2786 ? 114.889 102.890 98.128  1.00 33.18  ? 2786 GLN A CD    1 
ATOM   10496 O  OE1   . GLN A 1 2786 ? 115.286 102.925 99.293  1.00 39.66  ? 2786 GLN A OE1   1 
ATOM   10497 N  NE2   . GLN A 1 2786 ? 113.817 102.201 97.757  1.00 25.16  ? 2786 GLN A NE2   1 
ATOM   10498 N  N     . ASP A 1 2787 ? 114.262 107.449 94.437  1.00 26.24  ? 2787 ASP A N     1 
ATOM   10499 C  CA    . ASP A 1 2787 ? 113.240 108.228 93.745  1.00 22.38  ? 2787 ASP A CA    1 
ATOM   10500 C  C     . ASP A 1 2787 ? 113.243 107.936 92.250  1.00 22.37  ? 2787 ASP A C     1 
ATOM   10501 O  O     . ASP A 1 2787 ? 112.179 107.831 91.628  1.00 23.12  ? 2787 ASP A O     1 
ATOM   10502 C  CB    . ASP A 1 2787 ? 113.454 109.720 94.002  1.00 27.50  ? 2787 ASP A CB    1 
ATOM   10503 C  CG    . ASP A 1 2787 ? 113.486 110.060 95.479  1.00 46.07  ? 2787 ASP A CG    1 
ATOM   10504 O  OD1   . ASP A 1 2787 ? 112.407 110.095 96.107  1.00 52.34  ? 2787 ASP A OD1   1 
ATOM   10505 O  OD2   . ASP A 1 2787 ? 114.591 110.292 96.013  1.00 43.78  ? 2787 ASP A OD2   1 
ATOM   10506 N  N     . THR A 1 2788 ? 114.429 107.804 91.655  1.00 20.25  ? 2788 THR A N     1 
ATOM   10507 C  CA    . THR A 1 2788 ? 114.518 107.510 90.228  1.00 18.89  ? 2788 THR A CA    1 
ATOM   10508 C  C     . THR A 1 2788 ? 114.133 106.062 89.943  1.00 20.29  ? 2788 THR A C     1 
ATOM   10509 O  O     . THR A 1 2788 ? 113.179 105.792 89.205  1.00 24.24  ? 2788 THR A O     1 
ATOM   10510 C  CB    . THR A 1 2788 ? 115.930 107.802 89.719  1.00 19.80  ? 2788 THR A CB    1 
ATOM   10511 O  OG1   . THR A 1 2788 ? 116.241 109.185 89.933  1.00 23.57  ? 2788 THR A OG1   1 
ATOM   10512 C  CG2   . THR A 1 2788 ? 116.034 107.490 88.236  1.00 17.44  ? 2788 THR A CG2   1 
ATOM   10513 N  N     . GLN A 1 2789 ? 114.869 105.116 90.519  1.00 17.66  ? 2789 GLN A N     1 
ATOM   10514 C  CA    . GLN A 1 2789 ? 114.599 103.700 90.339  1.00 16.45  ? 2789 GLN A CA    1 
ATOM   10515 C  C     . GLN A 1 2789 ? 114.583 102.997 91.687  1.00 17.10  ? 2789 GLN A C     1 
ATOM   10516 O  O     . GLN A 1 2789 ? 115.334 103.367 92.595  1.00 17.54  ? 2789 GLN A O     1 
ATOM   10517 C  CB    . GLN A 1 2789 ? 115.645 103.045 89.426  1.00 10.79  ? 2789 GLN A CB    1 
ATOM   10518 C  CG    . GLN A 1 2789 ? 115.665 103.600 88.012  1.00 9.49   ? 2789 GLN A CG    1 
ATOM   10519 C  CD    . GLN A 1 2789 ? 114.507 103.098 87.170  1.00 12.94  ? 2789 GLN A CD    1 
ATOM   10520 O  OE1   . GLN A 1 2789 ? 113.810 102.157 87.549  1.00 15.21  ? 2789 GLN A OE1   1 
ATOM   10521 N  NE2   . GLN A 1 2789 ? 114.295 103.728 86.022  1.00 12.65  ? 2789 GLN A NE2   1 
ATOM   10522 N  N     . PRO A 1 2790 ? 113.738 101.974 91.843  1.00 21.16  ? 2790 PRO A N     1 
ATOM   10523 C  CA    . PRO A 1 2790 ? 113.619 101.313 93.152  1.00 19.40  ? 2790 PRO A CA    1 
ATOM   10524 C  C     . PRO A 1 2790 ? 114.856 100.540 93.574  1.00 17.55  ? 2790 PRO A C     1 
ATOM   10525 O  O     . PRO A 1 2790 ? 114.959 100.179 94.751  1.00 20.11  ? 2790 PRO A O     1 
ATOM   10526 C  CB    . PRO A 1 2790 ? 112.417 100.380 92.962  1.00 23.97  ? 2790 PRO A CB    1 
ATOM   10527 C  CG    . PRO A 1 2790 ? 112.412 100.093 91.500  1.00 23.55  ? 2790 PRO A CG    1 
ATOM   10528 C  CD    . PRO A 1 2790 ? 112.822 101.386 90.850  1.00 20.69  ? 2790 PRO A CD    1 
ATOM   10529 N  N     . HIS A 1 2791 ? 115.787 100.260 92.662  1.00 14.04  ? 2791 HIS A N     1 
ATOM   10530 C  CA    . HIS A 1 2791 ? 116.985 99.496  92.984  1.00 13.66  ? 2791 HIS A CA    1 
ATOM   10531 C  C     . HIS A 1 2791 ? 118.233 100.365 93.080  1.00 12.32  ? 2791 HIS A C     1 
ATOM   10532 O  O     . HIS A 1 2791 ? 119.346 99.831  93.114  1.00 14.60  ? 2791 HIS A O     1 
ATOM   10533 C  CB    . HIS A 1 2791 ? 117.195 98.384  91.953  1.00 12.14  ? 2791 HIS A CB    1 
ATOM   10534 C  CG    . HIS A 1 2791 ? 117.460 98.883  90.567  1.00 9.55   ? 2791 HIS A CG    1 
ATOM   10535 N  ND1   . HIS A 1 2791 ? 116.467 99.383  89.753  1.00 12.60  ? 2791 HIS A ND1   1 
ATOM   10536 C  CD2   . HIS A 1 2791 ? 118.606 98.951  89.848  1.00 7.39   ? 2791 HIS A CD2   1 
ATOM   10537 C  CE1   . HIS A 1 2791 ? 116.990 99.742  88.594  1.00 8.69   ? 2791 HIS A CE1   1 
ATOM   10538 N  NE2   . HIS A 1 2791 ? 118.286 99.490  88.626  1.00 6.40   ? 2791 HIS A NE2   1 
ATOM   10539 N  N     . TYR A 1 2792 ? 118.077 101.687 93.125  1.00 12.17  ? 2792 TYR A N     1 
ATOM   10540 C  CA    . TYR A 1 2792 ? 119.217 102.601 93.232  1.00 12.91  ? 2792 TYR A CA    1 
ATOM   10541 C  C     . TYR A 1 2792 ? 119.567 102.817 94.706  1.00 15.03  ? 2792 TYR A C     1 
ATOM   10542 O  O     . TYR A 1 2792 ? 119.380 103.890 95.282  1.00 18.89  ? 2792 TYR A O     1 
ATOM   10543 C  CB    . TYR A 1 2792 ? 118.912 103.918 92.530  1.00 11.70  ? 2792 TYR A CB    1 
ATOM   10544 C  CG    . TYR A 1 2792 ? 118.983 103.867 91.019  1.00 10.68  ? 2792 TYR A CG    1 
ATOM   10545 C  CD1   . TYR A 1 2792 ? 119.179 102.666 90.348  1.00 9.79   ? 2792 TYR A CD1   1 
ATOM   10546 C  CD2   . TYR A 1 2792 ? 118.851 105.024 90.262  1.00 10.30  ? 2792 TYR A CD2   1 
ATOM   10547 C  CE1   . TYR A 1 2792 ? 119.245 102.621 88.968  1.00 7.30   ? 2792 TYR A CE1   1 
ATOM   10548 C  CE2   . TYR A 1 2792 ? 118.915 104.989 88.884  1.00 10.98  ? 2792 TYR A CE2   1 
ATOM   10549 C  CZ    . TYR A 1 2792 ? 119.113 103.786 88.241  1.00 10.23  ? 2792 TYR A CZ    1 
ATOM   10550 O  OH    . TYR A 1 2792 ? 119.176 103.749 86.868  1.00 8.07   ? 2792 TYR A OH    1 
ATOM   10551 N  N     . ILE A 1 2793 ? 120.086 101.756 95.318  1.00 12.87  ? 2793 ILE A N     1 
ATOM   10552 C  CA    . ILE A 1 2793 ? 120.540 101.781 96.704  1.00 11.11  ? 2793 ILE A CA    1 
ATOM   10553 C  C     . ILE A 1 2793 ? 122.039 101.526 96.714  1.00 11.04  ? 2793 ILE A C     1 
ATOM   10554 O  O     . ILE A 1 2793 ? 122.506 100.502 96.201  1.00 17.85  ? 2793 ILE A O     1 
ATOM   10555 C  CB    . ILE A 1 2793 ? 119.805 100.748 97.574  1.00 18.54  ? 2793 ILE A CB    1 
ATOM   10556 C  CG1   . ILE A 1 2793 ? 118.314 101.075 97.674  1.00 17.16  ? 2793 ILE A CG1   1 
ATOM   10557 C  CG2   . ILE A 1 2793 ? 120.434 100.673 98.957  1.00 19.62  ? 2793 ILE A CG2   1 
ATOM   10558 C  CD1   . ILE A 1 2793 ? 117.472 100.424 96.610  1.00 18.10  ? 2793 ILE A CD1   1 
ATOM   10559 N  N     . TYR A 1 2794 ? 122.791 102.453 97.298  1.00 8.15   ? 2794 TYR A N     1 
ATOM   10560 C  CA    . TYR A 1 2794 ? 124.233 102.323 97.441  1.00 6.47   ? 2794 TYR A CA    1 
ATOM   10561 C  C     . TYR A 1 2794 ? 124.598 102.430 98.913  1.00 9.70   ? 2794 TYR A C     1 
ATOM   10562 O  O     . TYR A 1 2794 ? 124.168 103.363 99.599  1.00 13.40  ? 2794 TYR A O     1 
ATOM   10563 C  CB    . TYR A 1 2794 ? 124.963 103.379 96.609  1.00 8.09   ? 2794 TYR A CB    1 
ATOM   10564 C  CG    . TYR A 1 2794 ? 124.703 103.224 95.129  1.00 10.91  ? 2794 TYR A CG    1 
ATOM   10565 C  CD1   . TYR A 1 2794 ? 125.382 102.270 94.384  1.00 9.97   ? 2794 TYR A CD1   1 
ATOM   10566 C  CD2   . TYR A 1 2794 ? 123.764 104.015 94.481  1.00 10.10  ? 2794 TYR A CD2   1 
ATOM   10567 C  CE1   . TYR A 1 2794 ? 125.142 102.115 93.034  1.00 10.86  ? 2794 TYR A CE1   1 
ATOM   10568 C  CE2   . TYR A 1 2794 ? 123.518 103.868 93.131  1.00 10.37  ? 2794 TYR A CE2   1 
ATOM   10569 C  CZ    . TYR A 1 2794 ? 124.210 102.917 92.413  1.00 12.97  ? 2794 TYR A CZ    1 
ATOM   10570 O  OH    . TYR A 1 2794 ? 123.969 102.764 91.069  1.00 14.71  ? 2794 TYR A OH    1 
ATOM   10571 N  N     . SER A 1 2795 ? 125.379 101.462 99.399  1.00 5.99   ? 2795 SER A N     1 
ATOM   10572 C  CA    . SER A 1 2795 ? 125.755 101.432 100.836 1.00 5.01   ? 2795 SER A CA    1 
ATOM   10573 C  C     . SER A 1 2795 ? 127.212 100.969 100.975 1.00 6.87   ? 2795 SER A C     1 
ATOM   10574 O  O     . SER A 1 2795 ? 127.834 100.664 99.933  1.00 6.66   ? 2795 SER A O     1 
ATOM   10575 C  CB    . SER A 1 2795 ? 124.821 100.533 101.601 1.00 4.59   ? 2795 SER A CB    1 
ATOM   10576 O  OG    . SER A 1 2795 ? 124.945 99.184  101.171 1.00 5.80   ? 2795 SER A OG    1 
ATOM   10577 N  N     . PRO A 1 2796 ? 127.786 100.895 102.198 1.00 7.05   ? 2796 PRO A N     1 
ATOM   10578 C  CA    . PRO A 1 2796 ? 129.139 100.381 102.370 1.00 6.05   ? 2796 PRO A CA    1 
ATOM   10579 C  C     . PRO A 1 2796 ? 129.303 98.979  101.796 1.00 4.21   ? 2796 PRO A C     1 
ATOM   10580 O  O     . PRO A 1 2796 ? 130.452 98.533  101.620 1.00 5.37   ? 2796 PRO A O     1 
ATOM   10581 C  CB    . PRO A 1 2796 ? 129.331 100.415 103.895 1.00 5.52   ? 2796 PRO A CB    1 
ATOM   10582 C  CG    . PRO A 1 2796 ? 128.396 101.508 104.351 1.00 6.23   ? 2796 PRO A CG    1 
ATOM   10583 C  CD    . PRO A 1 2796 ? 127.190 101.361 103.441 1.00 4.33   ? 2796 PRO A CD    1 
ATOM   10584 N  N     . ARG A 1 2797 ? 128.190 98.293  101.519 1.00 5.22   ? 2797 ARG A N     1 
ATOM   10585 C  CA    . ARG A 1 2797 ? 128.266 96.949  100.886 1.00 6.83   ? 2797 ARG A CA    1 
ATOM   10586 C  C     . ARG A 1 2797 ? 128.983 97.078  99.532  1.00 7.42   ? 2797 ARG A C     1 
ATOM   10587 O  O     . ARG A 1 2797 ? 129.826 96.207  99.228  1.00 7.56   ? 2797 ARG A O     1 
ATOM   10588 C  CB    . ARG A 1 2797 ? 126.867 96.336  100.753 1.00 8.36   ? 2797 ARG A CB    1 
ATOM   10589 C  CG    . ARG A 1 2797 ? 126.295 95.917  102.099 1.00 9.38   ? 2797 ARG A CG    1 
ATOM   10590 C  CD    . ARG A 1 2797 ? 125.063 95.041  101.949 1.00 12.50  ? 2797 ARG A CD    1 
ATOM   10591 N  NE    . ARG A 1 2797 ? 123.903 95.782  101.445 1.00 17.01  ? 2797 ARG A NE    1 
ATOM   10592 C  CZ    . ARG A 1 2797 ? 122.746 95.877  102.086 1.00 15.15  ? 2797 ARG A CZ    1 
ATOM   10593 N  NH1   . ARG A 1 2797 ? 122.518 95.132  103.153 1.00 11.14  ? 2797 ARG A NH1   1 
ATOM   10594 N  NH2   . ARG A 1 2797 ? 121.820 96.713  101.655 1.00 12.77  ? 2797 ARG A NH2   1 
ATOM   10595 N  N     . GLU A 1 2798 ? 128.670 98.125  98.763  1.00 7.60   ? 2798 GLU A N     1 
ATOM   10596 C  CA    . GLU A 1 2798 ? 129.368 98.361  97.472  1.00 5.71   ? 2798 GLU A CA    1 
ATOM   10597 C  C     . GLU A 1 2798 ? 130.864 98.577  97.750  1.00 4.91   ? 2798 GLU A C     1 
ATOM   10598 O  O     . GLU A 1 2798 ? 131.692 98.016  97.002  1.00 5.47   ? 2798 GLU A O     1 
ATOM   10599 C  CB    . GLU A 1 2798 ? 128.769 99.563  96.741  1.00 6.78   ? 2798 GLU A CB    1 
ATOM   10600 C  CG    . GLU A 1 2798 ? 127.435 99.263  96.063  1.00 8.04   ? 2798 GLU A CG    1 
ATOM   10601 C  CD    . GLU A 1 2798 ? 126.355 98.718  96.980  1.00 14.83  ? 2798 GLU A CD    1 
ATOM   10602 O  OE1   . GLU A 1 2798 ? 125.989 99.416  97.948  1.00 13.93  ? 2798 GLU A OE1   1 
ATOM   10603 O  OE2   . GLU A 1 2798 ? 125.883 97.590  96.726  1.00 21.87  ? 2798 GLU A OE2   1 
ATOM   10604 N  N     . MET A 1 2799 ? 131.188 99.352  98.789  1.00 5.51   ? 2799 MET A N     1 
ATOM   10605 C  CA    . MET A 1 2799 ? 132.607 99.616  99.147  1.00 4.52   ? 2799 MET A CA    1 
ATOM   10606 C  C     . MET A 1 2799 ? 133.299 98.290  99.498  1.00 5.11   ? 2799 MET A C     1 
ATOM   10607 O  O     . MET A 1 2799 ? 134.454 98.090  99.064  1.00 5.19   ? 2799 MET A O     1 
ATOM   10608 C  CB    . MET A 1 2799 ? 132.699 100.575 100.340 1.00 4.08   ? 2799 MET A CB    1 
ATOM   10609 C  CG    . MET A 1 2799 ? 132.241 101.987 100.036 1.00 6.30   ? 2799 MET A CG    1 
ATOM   10610 S  SD    . MET A 1 2799 ? 133.381 102.864 98.946  1.00 12.26  ? 2799 MET A SD    1 
ATOM   10611 C  CE    . MET A 1 2799 ? 134.861 102.879 99.967  1.00 4.25   ? 2799 MET A CE    1 
ATOM   10612 N  N     . THR A 1 2800 ? 132.619 97.424  100.255 1.00 3.55   ? 2800 THR A N     1 
ATOM   10613 C  CA    . THR A 1 2800 ? 133.200 96.119  100.638 1.00 3.47   ? 2800 THR A CA    1 
ATOM   10614 C  C     . THR A 1 2800 ? 133.417 95.292  99.389  1.00 5.44   ? 2800 THR A C     1 
ATOM   10615 O  O     . THR A 1 2800 ? 134.508 94.696  99.259  1.00 4.98   ? 2800 THR A O     1 
ATOM   10616 C  CB    . THR A 1 2800 ? 132.277 95.419  101.634 1.00 5.84   ? 2800 THR A CB    1 
ATOM   10617 O  OG1   . THR A 1 2800 ? 132.220 96.285  102.762 1.00 6.97   ? 2800 THR A OG1   1 
ATOM   10618 C  CG2   . THR A 1 2800 ? 132.798 94.056  102.053 1.00 8.86   ? 2800 THR A CG2   1 
ATOM   10619 N  N     . ARG A 1 2801 ? 132.424 95.260  98.495  1.00 4.66   ? 2801 ARG A N     1 
ATOM   10620 C  CA    . ARG A 1 2801 ? 132.545 94.500  97.223  1.00 4.43   ? 2801 ARG A CA    1 
ATOM   10621 C  C     . ARG A 1 2801 ? 133.692 95.096  96.394  1.00 4.71   ? 2801 ARG A C     1 
ATOM   10622 O  O     . ARG A 1 2801 ? 134.460 94.310  95.797  1.00 3.80   ? 2801 ARG A O     1 
ATOM   10623 C  CB    . ARG A 1 2801 ? 131.208 94.532  96.473  1.00 5.81   ? 2801 ARG A CB    1 
ATOM   10624 C  CG    . ARG A 1 2801 ? 130.104 93.767  97.189  1.00 13.06  ? 2801 ARG A CG    1 
ATOM   10625 C  CD    . ARG A 1 2801 ? 128.715 94.131  96.687  1.00 19.19  ? 2801 ARG A CD    1 
ATOM   10626 N  NE    . ARG A 1 2801 ? 127.661 93.392  97.391  1.00 30.40  ? 2801 ARG A NE    1 
ATOM   10627 C  CZ    . ARG A 1 2801 ? 126.360 93.558  97.193  1.00 26.58  ? 2801 ARG A CZ    1 
ATOM   10628 N  NH1   . ARG A 1 2801 ? 125.922 94.608  96.522  1.00 19.70  ? 2801 ARG A NH1   1 
ATOM   10629 N  NH2   . ARG A 1 2801 ? 125.499 92.678  97.673  1.00 22.66  ? 2801 ARG A NH2   1 
ATOM   10630 N  N     . TRP A 1 2802 ? 133.804 96.427  96.367  1.00 4.21   ? 2802 TRP A N     1 
ATOM   10631 C  CA    . TRP A 1 2802 ? 134.885 97.082  95.637  1.00 3.90   ? 2802 TRP A CA    1 
ATOM   10632 C  C     . TRP A 1 2802 ? 136.242 96.608  96.138  1.00 3.87   ? 2802 TRP A C     1 
ATOM   10633 O  O     . TRP A 1 2802 ? 137.110 96.202  95.350  1.00 5.30   ? 2802 TRP A O     1 
ATOM   10634 C  CB    . TRP A 1 2802 ? 134.745 98.595  95.805  1.00 3.54   ? 2802 TRP A CB    1 
ATOM   10635 C  CG    . TRP A 1 2802 ? 135.282 99.430  94.695  1.00 3.44   ? 2802 TRP A CG    1 
ATOM   10636 C  CD1   . TRP A 1 2802 ? 136.146 99.047  93.714  1.00 3.42   ? 2802 TRP A CD1   1 
ATOM   10637 C  CD2   . TRP A 1 2802 ? 134.985 100.810 94.453  1.00 4.05   ? 2802 TRP A CD2   1 
ATOM   10638 N  NE1   . TRP A 1 2802 ? 136.405 100.103 92.874  1.00 2.70   ? 2802 TRP A NE1   1 
ATOM   10639 C  CE2   . TRP A 1 2802 ? 135.703 101.197 93.307  1.00 3.30   ? 2802 TRP A CE2   1 
ATOM   10640 C  CE3   . TRP A 1 2802 ? 134.180 101.754 95.097  1.00 3.80   ? 2802 TRP A CE3   1 
ATOM   10641 C  CZ2   . TRP A 1 2802 ? 135.640 102.487 92.790  1.00 3.46   ? 2802 TRP A CZ2   1 
ATOM   10642 C  CZ3   . TRP A 1 2802 ? 134.119 103.034 94.582  1.00 3.27   ? 2802 TRP A CZ3   1 
ATOM   10643 C  CH2   . TRP A 1 2802 ? 134.845 103.390 93.442  1.00 3.20   ? 2802 TRP A CH2   1 
ATOM   10644 N  N     . VAL A 1 2803 ? 136.433 96.645  97.458  1.00 4.52   ? 2803 VAL A N     1 
ATOM   10645 C  CA    . VAL A 1 2803 ? 137.694 96.206  98.046  1.00 4.86   ? 2803 VAL A CA    1 
ATOM   10646 C  C     . VAL A 1 2803 ? 137.938 94.733  97.745  1.00 5.08   ? 2803 VAL A C     1 
ATOM   10647 O  O     . VAL A 1 2803 ? 139.047 94.340  97.365  1.00 6.43   ? 2803 VAL A O     1 
ATOM   10648 C  CB    . VAL A 1 2803 ? 137.706 96.487  99.560  1.00 5.61   ? 2803 VAL A CB    1 
ATOM   10649 C  CG1   . VAL A 1 2803 ? 138.930 95.866  100.202 1.00 7.84   ? 2803 VAL A CG1   1 
ATOM   10650 C  CG2   . VAL A 1 2803 ? 137.676 97.981  99.820  1.00 5.52   ? 2803 VAL A CG2   1 
ATOM   10651 N  N     . ARG A 1 2804 ? 136.907 93.898  97.901  1.00 4.81   ? 2804 ARG A N     1 
ATOM   10652 C  CA    . ARG A 1 2804 ? 137.057 92.470  97.642  1.00 7.71   ? 2804 ARG A CA    1 
ATOM   10653 C  C     . ARG A 1 2804 ? 137.402 92.196  96.183  1.00 8.93   ? 2804 ARG A C     1 
ATOM   10654 O  O     . ARG A 1 2804 ? 138.259 91.356  95.891  1.00 12.28  ? 2804 ARG A O     1 
ATOM   10655 C  CB    . ARG A 1 2804 ? 135.778 91.731  98.038  1.00 10.65  ? 2804 ARG A CB    1 
ATOM   10656 C  CG    . ARG A 1 2804 ? 135.976 90.255  98.339  1.00 24.98  ? 2804 ARG A CG    1 
ATOM   10657 C  CD    . ARG A 1 2804 ? 136.878 90.032  99.541  1.00 27.34  ? 2804 ARG A CD    1 
ATOM   10658 N  NE    . ARG A 1 2804 ? 137.590 88.764  99.446  1.00 31.68  ? 2804 ARG A NE    1 
ATOM   10659 C  CZ    . ARG A 1 2804 ? 138.430 88.303  100.363 1.00 34.83  ? 2804 ARG A CZ    1 
ATOM   10660 N  NH1   . ARG A 1 2804 ? 138.685 88.980  101.470 1.00 31.20  ? 2804 ARG A NH1   1 
ATOM   10661 N  NH2   . ARG A 1 2804 ? 139.026 87.130  100.166 1.00 41.60  ? 2804 ARG A NH2   1 
ATOM   10662 N  N     . GLY A 1 2805 ? 136.743 92.890  95.255  1.00 7.05   ? 2805 GLY A N     1 
ATOM   10663 C  CA    . GLY A 1 2805 ? 137.010 92.668  93.845  1.00 5.82   ? 2805 GLY A CA    1 
ATOM   10664 C  C     . GLY A 1 2805 ? 138.404 93.098  93.441  1.00 7.08   ? 2805 GLY A C     1 
ATOM   10665 O  O     . GLY A 1 2805 ? 139.065 92.421  92.649  1.00 15.57  ? 2805 GLY A O     1 
ATOM   10666 N  N     . ILE A 1 2806 ? 138.871 94.231  93.969  1.00 5.49   ? 2806 ILE A N     1 
ATOM   10667 C  CA    . ILE A 1 2806 ? 140.245 94.639  93.693  1.00 7.18   ? 2806 ILE A CA    1 
ATOM   10668 C  C     . ILE A 1 2806 ? 141.230 93.650  94.307  1.00 10.59  ? 2806 ILE A C     1 
ATOM   10669 O  O     . ILE A 1 2806 ? 142.244 93.300  93.690  1.00 11.58  ? 2806 ILE A O     1 
ATOM   10670 C  CB    . ILE A 1 2806 ? 140.489 96.077  94.183  1.00 4.83   ? 2806 ILE A CB    1 
ATOM   10671 C  CG1   . ILE A 1 2806 ? 139.585 97.046  93.420  1.00 4.99   ? 2806 ILE A CG1   1 
ATOM   10672 C  CG2   . ILE A 1 2806 ? 141.951 96.460  94.016  1.00 3.18   ? 2806 ILE A CG2   1 
ATOM   10673 C  CD1   . ILE A 1 2806 ? 139.858 98.496  93.709  1.00 4.11   ? 2806 ILE A CD1   1 
ATOM   10674 N  N     . PHE A 1 2807 ? 140.944 93.174  95.521  1.00 10.88  ? 2807 PHE A N     1 
ATOM   10675 C  CA    . PHE A 1 2807 ? 141.839 92.235  96.191  1.00 9.99   ? 2807 PHE A CA    1 
ATOM   10676 C  C     . PHE A 1 2807 ? 141.937 90.913  95.437  1.00 14.04  ? 2807 PHE A C     1 
ATOM   10677 O  O     . PHE A 1 2807 ? 143.026 90.340  95.317  1.00 17.35  ? 2807 PHE A O     1 
ATOM   10678 C  CB    . PHE A 1 2807 ? 141.364 92.014  97.627  1.00 9.66   ? 2807 PHE A CB    1 
ATOM   10679 C  CG    . PHE A 1 2807 ? 142.079 90.908  98.342  1.00 13.72  ? 2807 PHE A CG    1 
ATOM   10680 C  CD1   . PHE A 1 2807 ? 143.356 91.097  98.837  1.00 18.08  ? 2807 PHE A CD1   1 
ATOM   10681 C  CD2   . PHE A 1 2807 ? 141.460 89.686  98.543  1.00 19.29  ? 2807 PHE A CD2   1 
ATOM   10682 C  CE1   . PHE A 1 2807 ? 144.012 90.080  99.500  1.00 20.30  ? 2807 PHE A CE1   1 
ATOM   10683 C  CE2   . PHE A 1 2807 ? 142.108 88.668  99.210  1.00 18.84  ? 2807 PHE A CE2   1 
ATOM   10684 C  CZ    . PHE A 1 2807 ? 143.387 88.864  99.687  1.00 18.27  ? 2807 PHE A CZ    1 
ATOM   10685 N  N     . GLU A 1 2808 ? 140.810 90.408  94.928  1.00 15.04  ? 2808 GLU A N     1 
ATOM   10686 C  CA    . GLU A 1 2808 ? 140.837 89.161  94.169  1.00 16.39  ? 2808 GLU A CA    1 
ATOM   10687 C  C     . GLU A 1 2808 ? 141.627 89.307  92.875  1.00 18.15  ? 2808 GLU A C     1 
ATOM   10688 O  O     . GLU A 1 2808 ? 142.296 88.359  92.449  1.00 23.85  ? 2808 GLU A O     1 
ATOM   10689 C  CB    . GLU A 1 2808 ? 139.414 88.689  93.871  1.00 12.97  ? 2808 GLU A CB    1 
ATOM   10690 C  CG    . GLU A 1 2808 ? 138.607 88.327  95.106  1.00 22.88  ? 2808 GLU A CG    1 
ATOM   10691 C  CD    . GLU A 1 2808 ? 137.112 88.359  94.855  1.00 35.62  ? 2808 GLU A CD    1 
ATOM   10692 O  OE1   . GLU A 1 2808 ? 136.707 88.627  93.705  1.00 28.80  ? 2808 GLU A OE1   1 
ATOM   10693 O  OE2   . GLU A 1 2808 ? 136.343 88.115  95.808  1.00 34.11  ? 2808 GLU A OE2   1 
ATOM   10694 N  N     . ALA A 1 2809 ? 141.562 90.476  92.240  1.00 13.33  ? 2809 ALA A N     1 
ATOM   10695 C  CA    . ALA A 1 2809 ? 142.341 90.735  91.037  1.00 11.64  ? 2809 ALA A CA    1 
ATOM   10696 C  C     . ALA A 1 2809 ? 143.790 91.093  91.335  1.00 14.42  ? 2809 ALA A C     1 
ATOM   10697 O  O     . ALA A 1 2809 ? 144.524 91.451  90.408  1.00 23.06  ? 2809 ALA A O     1 
ATOM   10698 C  CB    . ALA A 1 2809 ? 141.692 91.856  90.222  1.00 11.84  ? 2809 ALA A CB    1 
ATOM   10699 N  N     . LEU A 1 2810 ? 144.218 91.011  92.597  1.00 13.81  ? 2810 LEU A N     1 
ATOM   10700 C  CA    . LEU A 1 2810 ? 145.583 91.341  92.980  1.00 13.50  ? 2810 LEU A CA    1 
ATOM   10701 C  C     . LEU A 1 2810 ? 146.359 90.175  93.575  1.00 20.54  ? 2810 LEU A C     1 
ATOM   10702 O  O     . LEU A 1 2810 ? 147.592 90.238  93.615  1.00 24.68  ? 2810 LEU A O     1 
ATOM   10703 C  CB    . LEU A 1 2810 ? 145.584 92.497  93.992  1.00 14.68  ? 2810 LEU A CB    1 
ATOM   10704 C  CG    . LEU A 1 2810 ? 145.430 93.913  93.436  1.00 12.49  ? 2810 LEU A CG    1 
ATOM   10705 C  CD1   . LEU A 1 2810 ? 145.351 94.914  94.572  1.00 12.21  ? 2810 LEU A CD1   1 
ATOM   10706 C  CD2   . LEU A 1 2810 ? 146.572 94.257  92.497  1.00 13.66  ? 2810 LEU A CD2   1 
ATOM   10707 N  N     . ARG A 1 2811 ? 145.678 89.126  94.041  1.00 19.22  ? 2811 ARG A N     1 
ATOM   10708 C  CA    . ARG A 1 2811 ? 146.365 88.043  94.745  1.00 24.11  ? 2811 ARG A CA    1 
ATOM   10709 C  C     . ARG A 1 2811 ? 147.409 87.324  93.897  1.00 29.16  ? 2811 ARG A C     1 
ATOM   10710 O  O     . ARG A 1 2811 ? 148.559 87.204  94.354  1.00 35.46  ? 2811 ARG A O     1 
ATOM   10711 C  CB    . ARG A 1 2811 ? 145.334 87.056  95.302  1.00 25.29  ? 2811 ARG A CB    1 
ATOM   10712 C  CG    . ARG A 1 2811 ? 144.496 87.594  96.440  1.00 23.48  ? 2811 ARG A CG    1 
ATOM   10713 C  CD    . ARG A 1 2811 ? 143.484 86.558  96.893  1.00 31.99  ? 2811 ARG A CD    1 
ATOM   10714 N  NE    . ARG A 1 2811 ? 142.457 86.324  95.885  1.00 31.16  ? 2811 ARG A NE    1 
ATOM   10715 C  CZ    . ARG A 1 2811 ? 141.515 85.396  95.977  1.00 36.01  ? 2811 ARG A CZ    1 
ATOM   10716 N  NH1   . ARG A 1 2811 ? 141.436 84.594  97.026  1.00 36.51  ? 2811 ARG A NH1   1 
ATOM   10717 N  NH2   . ARG A 1 2811 ? 140.629 85.271  94.994  1.00 43.57  ? 2811 ARG A NH2   1 
ATOM   10718 N  N     . PRO A 1 2812 ? 147.111 86.830  92.692  1.00 25.06  ? 2812 PRO A N     1 
ATOM   10719 C  CA    . PRO A 1 2812 ? 148.119 86.084  91.932  1.00 26.51  ? 2812 PRO A CA    1 
ATOM   10720 C  C     . PRO A 1 2812 ? 149.112 86.948  91.171  1.00 28.18  ? 2812 PRO A C     1 
ATOM   10721 O  O     . PRO A 1 2812 ? 149.827 86.421  90.315  1.00 42.14  ? 2812 PRO A O     1 
ATOM   10722 C  CB    . PRO A 1 2812 ? 147.258 85.265  90.960  1.00 33.32  ? 2812 PRO A CB    1 
ATOM   10723 C  CG    . PRO A 1 2812 ? 146.125 86.156  90.672  1.00 26.72  ? 2812 PRO A CG    1 
ATOM   10724 C  CD    . PRO A 1 2812 ? 145.826 86.873  91.965  1.00 23.13  ? 2812 PRO A CD    1 
ATOM   10725 N  N     . LEU A 1 2813 ? 149.178 88.245  91.451  1.00 24.74  ? 2813 LEU A N     1 
ATOM   10726 C  CA    . LEU A 1 2813 ? 150.064 89.158  90.741  1.00 28.67  ? 2813 LEU A CA    1 
ATOM   10727 C  C     . LEU A 1 2813 ? 151.315 89.396  91.575  1.00 37.30  ? 2813 LEU A C     1 
ATOM   10728 O  O     . LEU A 1 2813 ? 151.223 89.796  92.741  1.00 37.72  ? 2813 LEU A O     1 
ATOM   10729 C  CB    . LEU A 1 2813 ? 149.355 90.480  90.447  1.00 30.57  ? 2813 LEU A CB    1 
ATOM   10730 C  CG    . LEU A 1 2813 ? 148.176 90.415  89.476  1.00 24.00  ? 2813 LEU A CG    1 
ATOM   10731 C  CD1   . LEU A 1 2813 ? 147.803 91.805  88.993  1.00 16.68  ? 2813 LEU A CD1   1 
ATOM   10732 C  CD2   . LEU A 1 2813 ? 148.492 89.503  88.301  1.00 27.85  ? 2813 LEU A CD2   1 
ATOM   10733 N  N     . GLU A 1 2814 ? 152.482 89.142  90.980  1.00 41.27  ? 2814 GLU A N     1 
ATOM   10734 C  CA    . GLU A 1 2814 ? 153.736 89.437  91.665  1.00 50.09  ? 2814 GLU A CA    1 
ATOM   10735 C  C     . GLU A 1 2814 ? 154.003 90.936  91.704  1.00 43.28  ? 2814 GLU A C     1 
ATOM   10736 O  O     . GLU A 1 2814 ? 154.532 91.453  92.694  1.00 39.79  ? 2814 GLU A O     1 
ATOM   10737 C  CB    . GLU A 1 2814 ? 154.892 88.701  90.989  1.00 49.36  ? 2814 GLU A CB    1 
ATOM   10738 C  CG    . GLU A 1 2814 ? 154.889 87.192  91.197  1.00 57.36  ? 2814 GLU A CG    1 
ATOM   10739 C  CD    . GLU A 1 2814 ? 154.942 86.799  92.663  1.00 70.56  ? 2814 GLU A CD    1 
ATOM   10740 O  OE1   . GLU A 1 2814 ? 153.873 86.721  93.305  1.00 68.87  ? 2814 GLU A OE1   1 
ATOM   10741 O  OE2   . GLU A 1 2814 ? 156.058 86.567  93.175  1.00 78.04  ? 2814 GLU A OE2   1 
ATOM   10742 N  N     . THR A 1 2815 ? 153.644 91.649  90.639  1.00 36.16  ? 2815 THR A N     1 
ATOM   10743 C  CA    . THR A 1 2815 ? 153.845 93.088  90.577  1.00 35.36  ? 2815 THR A CA    1 
ATOM   10744 C  C     . THR A 1 2815 ? 152.791 93.696  89.666  1.00 29.60  ? 2815 THR A C     1 
ATOM   10745 O  O     . THR A 1 2815 ? 152.168 93.006  88.854  1.00 28.49  ? 2815 THR A O     1 
ATOM   10746 C  CB    . THR A 1 2815 ? 155.253 93.447  90.083  1.00 34.03  ? 2815 THR A CB    1 
ATOM   10747 O  OG1   . THR A 1 2815 ? 155.538 94.815  90.401  1.00 32.34  ? 2815 THR A OG1   1 
ATOM   10748 C  CG2   . THR A 1 2815 ? 155.362 93.247  88.579  1.00 31.57  ? 2815 THR A CG2   1 
ATOM   10749 N  N     . LEU A 1 2816 ? 152.591 95.007  89.818  1.00 24.16  ? 2816 LEU A N     1 
ATOM   10750 C  CA    . LEU A 1 2816 ? 151.611 95.729  89.022  1.00 20.07  ? 2816 LEU A CA    1 
ATOM   10751 C  C     . LEU A 1 2816 ? 151.943 97.209  89.044  1.00 23.50  ? 2816 LEU A C     1 
ATOM   10752 O  O     . LEU A 1 2816 ? 152.211 97.751  90.125  1.00 28.33  ? 2816 LEU A O     1 
ATOM   10753 C  CB    . LEU A 1 2816 ? 150.190 95.503  89.551  1.00 21.06  ? 2816 LEU A CB    1 
ATOM   10754 C  CG    . LEU A 1 2816 ? 149.042 95.899  88.620  1.00 16.73  ? 2816 LEU A CG    1 
ATOM   10755 C  CD1   . LEU A 1 2816 ? 148.911 94.919  87.466  1.00 9.74   ? 2816 LEU A CD1   1 
ATOM   10756 C  CD2   . LEU A 1 2816 ? 147.741 95.993  89.397  1.00 11.54  ? 2816 LEU A CD2   1 
ATOM   10757 N  N     . PRO A 1 2817 ? 151.939 97.886  87.900  1.00 22.95  ? 2817 PRO A N     1 
ATOM   10758 C  CA    . PRO A 1 2817 ? 152.098 99.343  87.905  1.00 22.42  ? 2817 PRO A CA    1 
ATOM   10759 C  C     . PRO A 1 2817 ? 150.859 100.015 88.476  1.00 18.86  ? 2817 PRO A C     1 
ATOM   10760 O  O     . PRO A 1 2817 ? 149.805 99.400  88.654  1.00 23.23  ? 2817 PRO A O     1 
ATOM   10761 C  CB    . PRO A 1 2817 ? 152.299 99.691  86.428  1.00 24.24  ? 2817 PRO A CB    1 
ATOM   10762 C  CG    . PRO A 1 2817 ? 151.666 98.563  85.683  1.00 26.94  ? 2817 PRO A CG    1 
ATOM   10763 C  CD    . PRO A 1 2817 ? 151.820 97.338  86.538  1.00 19.50  ? 2817 PRO A CD    1 
ATOM   10764 N  N     . VAL A 1 2818 ? 151.002 101.307 88.776  1.00 16.14  ? 2818 VAL A N     1 
ATOM   10765 C  CA    . VAL A 1 2818 ? 149.885 102.047 89.353  1.00 16.56  ? 2818 VAL A CA    1 
ATOM   10766 C  C     . VAL A 1 2818 ? 148.732 102.144 88.361  1.00 16.35  ? 2818 VAL A C     1 
ATOM   10767 O  O     . VAL A 1 2818 ? 147.560 102.107 88.757  1.00 14.47  ? 2818 VAL A O     1 
ATOM   10768 C  CB    . VAL A 1 2818 ? 150.351 103.435 89.839  1.00 20.55  ? 2818 VAL A CB    1 
ATOM   10769 C  CG1   . VAL A 1 2818 ? 150.791 104.310 88.672  1.00 17.22  ? 2818 VAL A CG1   1 
ATOM   10770 C  CG2   . VAL A 1 2818 ? 149.251 104.114 90.643  1.00 17.81  ? 2818 VAL A CG2   1 
ATOM   10771 N  N     . GLU A 1 2819 ? 149.034 102.247 87.063  1.00 17.23  ? 2819 GLU A N     1 
ATOM   10772 C  CA    . GLU A 1 2819 ? 147.978 102.314 86.059  1.00 13.10  ? 2819 GLU A CA    1 
ATOM   10773 C  C     . GLU A 1 2819 ? 147.162 101.027 86.025  1.00 12.34  ? 2819 GLU A C     1 
ATOM   10774 O  O     . GLU A 1 2819 ? 145.946 101.063 85.809  1.00 10.77  ? 2819 GLU A O     1 
ATOM   10775 C  CB    . GLU A 1 2819 ? 148.577 102.614 84.684  1.00 16.57  ? 2819 GLU A CB    1 
ATOM   10776 C  CG    . GLU A 1 2819 ? 149.192 104.004 84.556  1.00 25.63  ? 2819 GLU A CG    1 
ATOM   10777 C  CD    . GLU A 1 2819 ? 150.606 104.082 85.100  1.00 32.07  ? 2819 GLU A CD    1 
ATOM   10778 O  OE1   . GLU A 1 2819 ? 151.144 103.039 85.526  1.00 25.09  ? 2819 GLU A OE1   1 
ATOM   10779 O  OE2   . GLU A 1 2819 ? 151.181 105.191 85.102  1.00 44.08  ? 2819 GLU A OE2   1 
ATOM   10780 N  N     . GLY A 1 2820 ? 147.808 99.880  86.241  1.00 10.05  ? 2820 GLY A N     1 
ATOM   10781 C  CA    . GLY A 1 2820 ? 147.066 98.630  86.305  1.00 8.99   ? 2820 GLY A CA    1 
ATOM   10782 C  C     . GLY A 1 2820 ? 146.117 98.573  87.487  1.00 8.38   ? 2820 GLY A C     1 
ATOM   10783 O  O     . GLY A 1 2820 ? 144.977 98.114  87.363  1.00 8.64   ? 2820 GLY A O     1 
ATOM   10784 N  N     . LEU A 1 2821 ? 146.574 99.041  88.651  1.00 10.02  ? 2821 LEU A N     1 
ATOM   10785 C  CA    . LEU A 1 2821 ? 145.701 99.093  89.819  1.00 7.16   ? 2821 LEU A CA    1 
ATOM   10786 C  C     . LEU A 1 2821 ? 144.533 100.041 89.584  1.00 6.27   ? 2821 LEU A C     1 
ATOM   10787 O  O     . LEU A 1 2821 ? 143.396 99.748  89.972  1.00 7.84   ? 2821 LEU A O     1 
ATOM   10788 C  CB    . LEU A 1 2821 ? 146.500 99.513  91.052  1.00 9.39   ? 2821 LEU A CB    1 
ATOM   10789 C  CG    . LEU A 1 2821 ? 145.715 99.645  92.357  1.00 10.38  ? 2821 LEU A CG    1 
ATOM   10790 C  CD1   . LEU A 1 2821 ? 145.106 98.311  92.748  1.00 6.34   ? 2821 LEU A CD1   1 
ATOM   10791 C  CD2   . LEU A 1 2821 ? 146.618 100.159 93.460  1.00 14.04  ? 2821 LEU A CD2   1 
ATOM   10792 N  N     . ILE A 1 2822 ? 144.796 101.183 88.946  1.00 5.13   ? 2822 ILE A N     1 
ATOM   10793 C  CA    . ILE A 1 2822 ? 143.720 102.112 88.619  1.00 5.27   ? 2822 ILE A CA    1 
ATOM   10794 C  C     . ILE A 1 2822 ? 142.740 101.487 87.633  1.00 7.84   ? 2822 ILE A C     1 
ATOM   10795 O  O     . ILE A 1 2822 ? 141.529 101.717 87.722  1.00 7.79   ? 2822 ILE A O     1 
ATOM   10796 C  CB    . ILE A 1 2822 ? 144.305 103.433 88.087  1.00 9.40   ? 2822 ILE A CB    1 
ATOM   10797 C  CG1   . ILE A 1 2822 ? 145.223 104.055 89.135  1.00 11.98  ? 2822 ILE A CG1   1 
ATOM   10798 C  CG2   . ILE A 1 2822 ? 143.206 104.405 87.753  1.00 6.95   ? 2822 ILE A CG2   1 
ATOM   10799 C  CD1   . ILE A 1 2822 ? 144.514 104.385 90.418  1.00 11.83  ? 2822 ILE A CD1   1 
ATOM   10800 N  N     . ARG A 1 2823 ? 143.237 100.695 86.680  1.00 7.94   ? 2823 ARG A N     1 
ATOM   10801 C  CA    . ARG A 1 2823 ? 142.346 99.992  85.762  1.00 7.27   ? 2823 ARG A CA    1 
ATOM   10802 C  C     . ARG A 1 2823 ? 141.459 98.998  86.501  1.00 5.43   ? 2823 ARG A C     1 
ATOM   10803 O  O     . ARG A 1 2823 ? 140.260 98.900  86.219  1.00 6.00   ? 2823 ARG A O     1 
ATOM   10804 C  CB    . ARG A 1 2823 ? 143.154 99.285  84.674  1.00 8.79   ? 2823 ARG A CB    1 
ATOM   10805 C  CG    . ARG A 1 2823 ? 142.317 98.856  83.482  1.00 8.42   ? 2823 ARG A CG    1 
ATOM   10806 C  CD    . ARG A 1 2823 ? 143.177 98.390  82.317  1.00 11.42  ? 2823 ARG A CD    1 
ATOM   10807 N  NE    . ARG A 1 2823 ? 142.383 98.157  81.116  1.00 15.87  ? 2823 ARG A NE    1 
ATOM   10808 C  CZ    . ARG A 1 2823 ? 141.830 99.109  80.377  1.00 16.48  ? 2823 ARG A CZ    1 
ATOM   10809 N  NH1   . ARG A 1 2823 ? 141.983 100.390 80.669  1.00 16.27  ? 2823 ARG A NH1   1 
ATOM   10810 N  NH2   . ARG A 1 2823 ? 141.107 98.767  79.314  1.00 12.37  ? 2823 ARG A NH2   1 
ATOM   10811 N  N     . ILE A 1 2824 ? 142.032 98.250  87.446  1.00 4.20   ? 2824 ILE A N     1 
ATOM   10812 C  CA    . ILE A 1 2824 ? 141.227 97.332  88.253  1.00 4.73   ? 2824 ILE A CA    1 
ATOM   10813 C  C     . ILE A 1 2824 ? 140.169 98.099  89.038  1.00 4.82   ? 2824 ILE A C     1 
ATOM   10814 O  O     . ILE A 1 2824 ? 139.007 97.681  89.121  1.00 4.55   ? 2824 ILE A O     1 
ATOM   10815 C  CB    . ILE A 1 2824 ? 142.127 96.500  89.187  1.00 5.81   ? 2824 ILE A CB    1 
ATOM   10816 C  CG1   . ILE A 1 2824 ? 143.191 95.749  88.387  1.00 6.58   ? 2824 ILE A CG1   1 
ATOM   10817 C  CG2   . ILE A 1 2824 ? 141.292 95.537  90.020  1.00 6.32   ? 2824 ILE A CG2   1 
ATOM   10818 C  CD1   . ILE A 1 2824 ? 144.193 95.013  89.244  1.00 9.87   ? 2824 ILE A CD1   1 
ATOM   10819 N  N     . TRP A 1 2825 ? 140.560 99.229  89.630  1.00 5.02   ? 2825 TRP A N     1 
ATOM   10820 C  CA    . TRP A 1 2825 ? 139.632 100.048 90.405  1.00 3.62   ? 2825 TRP A CA    1 
ATOM   10821 C  C     . TRP A 1 2825 ? 138.478 100.554 89.543  1.00 4.65   ? 2825 TRP A C     1 
ATOM   10822 O  O     . TRP A 1 2825 ? 137.307 100.478 89.938  1.00 4.63   ? 2825 TRP A O     1 
ATOM   10823 C  CB    . TRP A 1 2825 ? 140.416 101.198 91.045  1.00 3.66   ? 2825 TRP A CB    1 
ATOM   10824 C  CG    . TRP A 1 2825 ? 139.613 102.234 91.754  1.00 4.54   ? 2825 TRP A CG    1 
ATOM   10825 C  CD1   . TRP A 1 2825 ? 139.195 102.204 93.051  1.00 3.91   ? 2825 TRP A CD1   1 
ATOM   10826 C  CD2   . TRP A 1 2825 ? 139.201 103.501 91.228  1.00 5.55   ? 2825 TRP A CD2   1 
ATOM   10827 N  NE1   . TRP A 1 2825 ? 138.514 103.357 93.354  1.00 3.49   ? 2825 TRP A NE1   1 
ATOM   10828 C  CE2   . TRP A 1 2825 ? 138.503 104.170 92.252  1.00 4.05   ? 2825 TRP A CE2   1 
ATOM   10829 C  CE3   . TRP A 1 2825 ? 139.338 104.126 89.986  1.00 5.44   ? 2825 TRP A CE3   1 
ATOM   10830 C  CZ2   . TRP A 1 2825 ? 137.942 105.431 92.071  1.00 5.93   ? 2825 TRP A CZ2   1 
ATOM   10831 C  CZ3   . TRP A 1 2825 ? 138.784 105.379 89.810  1.00 6.80   ? 2825 TRP A CZ3   1 
ATOM   10832 C  CH2   . TRP A 1 2825 ? 138.092 106.018 90.846  1.00 7.94   ? 2825 TRP A CH2   1 
ATOM   10833 N  N     . ALA A 1 2826 ? 138.791 101.048 88.343  1.00 5.38   ? 2826 ALA A N     1 
ATOM   10834 C  CA    . ALA A 1 2826 ? 137.750 101.528 87.438  1.00 4.05   ? 2826 ALA A CA    1 
ATOM   10835 C  C     . ALA A 1 2826 ? 136.842 100.394 86.979  1.00 3.66   ? 2826 ALA A C     1 
ATOM   10836 O  O     . ALA A 1 2826 ? 135.623 100.574 86.872  1.00 3.86   ? 2826 ALA A O     1 
ATOM   10837 C  CB    . ALA A 1 2826 ? 138.379 102.225 86.235  1.00 4.58   ? 2826 ALA A CB    1 
ATOM   10838 N  N     . HIS A 1 2827 ? 137.418 99.227  86.682  1.00 3.60   ? 2827 HIS A N     1 
ATOM   10839 C  CA    . HIS A 1 2827 ? 136.608 98.092  86.253  1.00 3.96   ? 2827 HIS A CA    1 
ATOM   10840 C  C     . HIS A 1 2827 ? 135.653 97.653  87.355  1.00 3.89   ? 2827 HIS A C     1 
ATOM   10841 O  O     . HIS A 1 2827 ? 134.477 97.370  87.093  1.00 3.10   ? 2827 HIS A O     1 
ATOM   10842 C  CB    . HIS A 1 2827 ? 137.515 96.937  85.830  1.00 3.36   ? 2827 HIS A CB    1 
ATOM   10843 C  CG    . HIS A 1 2827 ? 136.778 95.669  85.533  1.00 3.54   ? 2827 HIS A CG    1 
ATOM   10844 N  ND1   . HIS A 1 2827 ? 136.745 94.606  86.409  1.00 4.79   ? 2827 HIS A ND1   1 
ATOM   10845 C  CD2   . HIS A 1 2827 ? 136.050 95.292  84.456  1.00 3.31   ? 2827 HIS A CD2   1 
ATOM   10846 C  CE1   . HIS A 1 2827 ? 136.024 93.631  85.885  1.00 6.30   ? 2827 HIS A CE1   1 
ATOM   10847 N  NE2   . HIS A 1 2827 ? 135.592 94.021  84.700  1.00 4.22   ? 2827 HIS A NE2   1 
ATOM   10848 N  N     . GLU A 1 2828 ? 136.139 97.598  88.598  1.00 4.14   ? 2828 GLU A N     1 
ATOM   10849 C  CA    . GLU A 1 2828 ? 135.270 97.235  89.712  1.00 4.22   ? 2828 GLU A CA    1 
ATOM   10850 C  C     . GLU A 1 2828 ? 134.175 98.273  89.919  1.00 3.19   ? 2828 GLU A C     1 
ATOM   10851 O  O     . GLU A 1 2828 ? 133.029 97.920  90.220  1.00 4.17   ? 2828 GLU A O     1 
ATOM   10852 C  CB    . GLU A 1 2828 ? 136.093 97.051  90.988  1.00 5.53   ? 2828 GLU A CB    1 
ATOM   10853 C  CG    . GLU A 1 2828 ? 137.084 95.897  90.935  1.00 6.04   ? 2828 GLU A CG    1 
ATOM   10854 C  CD    . GLU A 1 2828 ? 136.410 94.538  90.864  1.00 14.03  ? 2828 GLU A CD    1 
ATOM   10855 O  OE1   . GLU A 1 2828 ? 135.215 94.440  91.212  1.00 15.20  ? 2828 GLU A OE1   1 
ATOM   10856 O  OE2   . GLU A 1 2828 ? 137.078 93.565  90.454  1.00 15.18  ? 2828 GLU A OE2   1 
ATOM   10857 N  N     . ALA A 1 2829 ? 134.505 99.559  89.761  1.00 2.39   ? 2829 ALA A N     1 
ATOM   10858 C  CA    . ALA A 1 2829 ? 133.480 100.593 89.866  1.00 2.97   ? 2829 ALA A CA    1 
ATOM   10859 C  C     . ALA A 1 2829 ? 132.417 100.434 88.786  1.00 3.45   ? 2829 ALA A C     1 
ATOM   10860 O  O     . ALA A 1 2829 ? 131.221 100.583 89.057  1.00 3.18   ? 2829 ALA A O     1 
ATOM   10861 C  CB    . ALA A 1 2829 ? 134.112 101.977 89.783  1.00 2.82   ? 2829 ALA A CB    1 
ATOM   10862 N  N     . LEU A 1 2830 ? 132.835 100.142 87.553  1.00 3.16   ? 2830 LEU A N     1 
ATOM   10863 C  CA    . LEU A 1 2830 ? 131.871 99.924  86.477  1.00 3.57   ? 2830 LEU A CA    1 
ATOM   10864 C  C     . LEU A 1 2830 ? 130.983 98.723  86.773  1.00 3.68   ? 2830 LEU A C     1 
ATOM   10865 O  O     . LEU A 1 2830 ? 129.772 98.755  86.524  1.00 4.14   ? 2830 LEU A O     1 
ATOM   10866 C  CB    . LEU A 1 2830 ? 132.597 99.738  85.144  1.00 5.84   ? 2830 LEU A CB    1 
ATOM   10867 C  CG    . LEU A 1 2830 ? 133.290 100.962 84.549  1.00 7.14   ? 2830 LEU A CG    1 
ATOM   10868 C  CD1   . LEU A 1 2830 ? 134.359 100.541 83.561  1.00 6.80   ? 2830 LEU A CD1   1 
ATOM   10869 C  CD2   . LEU A 1 2830 ? 132.268 101.864 83.878  1.00 7.51   ? 2830 LEU A CD2   1 
ATOM   10870 N  N     . ARG A 1 2831 ? 131.572 97.648  87.299  1.00 2.99   ? 2831 ARG A N     1 
ATOM   10871 C  CA    . ARG A 1 2831 ? 130.785 96.460  87.613  1.00 3.61   ? 2831 ARG A CA    1 
ATOM   10872 C  C     . ARG A 1 2831 ? 129.779 96.731  88.725  1.00 4.85   ? 2831 ARG A C     1 
ATOM   10873 O  O     . ARG A 1 2831 ? 128.633 96.272  88.659  1.00 6.52   ? 2831 ARG A O     1 
ATOM   10874 C  CB    . ARG A 1 2831 ? 131.709 95.301  87.991  1.00 5.37   ? 2831 ARG A CB    1 
ATOM   10875 C  CG    . ARG A 1 2831 ? 132.626 94.834  86.867  1.00 5.04   ? 2831 ARG A CG    1 
ATOM   10876 C  CD    . ARG A 1 2831 ? 131.881 94.006  85.822  1.00 5.13   ? 2831 ARG A CD    1 
ATOM   10877 N  NE    . ARG A 1 2831 ? 131.095 94.823  84.905  1.00 5.95   ? 2831 ARG A NE    1 
ATOM   10878 C  CZ    . ARG A 1 2831 ? 131.604 95.629  83.983  1.00 5.38   ? 2831 ARG A CZ    1 
ATOM   10879 N  NH1   . ARG A 1 2831 ? 132.910 95.730  83.796  1.00 5.28   ? 2831 ARG A NH1   1 
ATOM   10880 N  NH2   . ARG A 1 2831 ? 130.781 96.349  83.227  1.00 5.63   ? 2831 ARG A NH2   1 
ATOM   10881 N  N     . LEU A 1 2832 ? 130.183 97.476  89.753  1.00 4.45   ? 2832 LEU A N     1 
ATOM   10882 C  CA    . LEU A 1 2832 ? 129.331 97.665  90.921  1.00 3.99   ? 2832 LEU A CA    1 
ATOM   10883 C  C     . LEU A 1 2832 ? 128.282 98.754  90.745  1.00 4.95   ? 2832 LEU A C     1 
ATOM   10884 O  O     . LEU A 1 2832 ? 127.162 98.608  91.249  1.00 9.10   ? 2832 LEU A O     1 
ATOM   10885 C  CB    . LEU A 1 2832 ? 130.184 97.996  92.145  1.00 5.05   ? 2832 LEU A CB    1 
ATOM   10886 C  CG    . LEU A 1 2832 ? 131.008 96.841  92.706  1.00 6.98   ? 2832 LEU A CG    1 
ATOM   10887 C  CD1   . LEU A 1 2832 ? 131.882 97.350  93.822  1.00 3.62   ? 2832 LEU A CD1   1 
ATOM   10888 C  CD2   . LEU A 1 2832 ? 130.104 95.725  93.193  1.00 9.23   ? 2832 LEU A CD2   1 
ATOM   10889 N  N     . PHE A 1 2833 ? 128.609 99.839  90.052  1.00 4.24   ? 2833 PHE A N     1 
ATOM   10890 C  CA    . PHE A 1 2833 ? 127.739 101.005 89.973  1.00 4.85   ? 2833 PHE A CA    1 
ATOM   10891 C  C     . PHE A 1 2833 ? 126.987 101.119 88.658  1.00 5.86   ? 2833 PHE A C     1 
ATOM   10892 O  O     . PHE A 1 2833 ? 125.774 101.338 88.665  1.00 8.91   ? 2833 PHE A O     1 
ATOM   10893 C  CB    . PHE A 1 2833 ? 128.559 102.280 90.196  1.00 6.78   ? 2833 PHE A CB    1 
ATOM   10894 C  CG    . PHE A 1 2833 ? 129.184 102.369 91.559  1.00 5.36   ? 2833 PHE A CG    1 
ATOM   10895 C  CD1   . PHE A 1 2833 ? 128.484 102.914 92.622  1.00 4.73   ? 2833 PHE A CD1   1 
ATOM   10896 C  CD2   . PHE A 1 2833 ? 130.466 101.898 91.781  1.00 4.41   ? 2833 PHE A CD2   1 
ATOM   10897 C  CE1   . PHE A 1 2833 ? 129.054 102.995 93.876  1.00 4.53   ? 2833 PHE A CE1   1 
ATOM   10898 C  CE2   . PHE A 1 2833 ? 131.042 101.975 93.032  1.00 4.67   ? 2833 PHE A CE2   1 
ATOM   10899 C  CZ    . PHE A 1 2833 ? 130.334 102.525 94.082  1.00 5.57   ? 2833 PHE A CZ    1 
ATOM   10900 N  N     . GLN A 1 2834 ? 127.676 100.969 87.527  1.00 4.74   ? 2834 GLN A N     1 
ATOM   10901 C  CA    . GLN A 1 2834 ? 127.060 101.193 86.225  1.00 4.94   ? 2834 GLN A CA    1 
ATOM   10902 C  C     . GLN A 1 2834 ? 126.151 100.053 85.780  1.00 4.13   ? 2834 GLN A C     1 
ATOM   10903 O  O     . GLN A 1 2834 ? 125.208 100.297 85.021  1.00 6.70   ? 2834 GLN A O     1 
ATOM   10904 C  CB    . GLN A 1 2834 ? 128.142 101.420 85.170  1.00 4.47   ? 2834 GLN A CB    1 
ATOM   10905 C  CG    . GLN A 1 2834 ? 127.664 102.171 83.942  1.00 5.98   ? 2834 GLN A CG    1 
ATOM   10906 C  CD    . GLN A 1 2834 ? 128.682 102.155 82.822  1.00 9.41   ? 2834 GLN A CD    1 
ATOM   10907 O  OE1   . GLN A 1 2834 ? 129.069 101.093 82.336  1.00 9.16   ? 2834 GLN A OE1   1 
ATOM   10908 N  NE2   . GLN A 1 2834 ? 129.125 103.335 82.407  1.00 9.47   ? 2834 GLN A NE2   1 
ATOM   10909 N  N     . ASP A 1 2835 ? 126.408 98.823  86.229  1.00 4.10   ? 2835 ASP A N     1 
ATOM   10910 C  CA    . ASP A 1 2835 ? 125.703 97.667  85.683  1.00 3.79   ? 2835 ASP A CA    1 
ATOM   10911 C  C     . ASP A 1 2835 ? 124.222 97.645  86.039  1.00 3.47   ? 2835 ASP A C     1 
ATOM   10912 O  O     . ASP A 1 2835 ? 123.448 96.964  85.359  1.00 3.44   ? 2835 ASP A O     1 
ATOM   10913 C  CB    . ASP A 1 2835 ? 126.368 96.375  86.159  1.00 4.21   ? 2835 ASP A CB    1 
ATOM   10914 C  CG    . ASP A 1 2835 ? 127.678 96.099  85.450  1.00 5.74   ? 2835 ASP A CG    1 
ATOM   10915 O  OD1   . ASP A 1 2835 ? 128.073 96.913  84.590  1.00 4.80   ? 2835 ASP A OD1   1 
ATOM   10916 O  OD2   . ASP A 1 2835 ? 128.314 95.068  85.752  1.00 5.73   ? 2835 ASP A OD2   1 
ATOM   10917 N  N     . ARG A 1 2836 ? 123.808 98.363  87.081  1.00 3.73   ? 2836 ARG A N     1 
ATOM   10918 C  CA    . ARG A 1 2836 ? 122.407 98.392  87.477  1.00 3.30   ? 2836 ARG A CA    1 
ATOM   10919 C  C     . ARG A 1 2836 ? 121.631 99.551  86.865  1.00 5.19   ? 2836 ARG A C     1 
ATOM   10920 O  O     . ARG A 1 2836 ? 120.408 99.609  87.030  1.00 6.24   ? 2836 ARG A O     1 
ATOM   10921 C  CB    . ARG A 1 2836 ? 122.291 98.461  89.003  1.00 4.15   ? 2836 ARG A CB    1 
ATOM   10922 C  CG    . ARG A 1 2836 ? 122.638 99.821  89.584  1.00 5.66   ? 2836 ARG A CG    1 
ATOM   10923 C  CD    . ARG A 1 2836 ? 122.548 99.816  91.098  1.00 8.72   ? 2836 ARG A CD    1 
ATOM   10924 N  NE    . ARG A 1 2836 ? 123.587 98.997  91.709  1.00 10.65  ? 2836 ARG A NE    1 
ATOM   10925 C  CZ    . ARG A 1 2836 ? 123.607 98.648  92.988  1.00 10.79  ? 2836 ARG A CZ    1 
ATOM   10926 N  NH1   . ARG A 1 2836 ? 122.653 99.027  93.822  1.00 12.21  ? 2836 ARG A NH1   1 
ATOM   10927 N  NH2   . ARG A 1 2836 ? 124.609 97.900  93.440  1.00 11.33  ? 2836 ARG A NH2   1 
ATOM   10928 N  N     . LEU A 1 2837 ? 122.300 100.463 86.167  1.00 3.91   ? 2837 LEU A N     1 
ATOM   10929 C  CA    . LEU A 1 2837 ? 121.638 101.659 85.664  1.00 5.00   ? 2837 LEU A CA    1 
ATOM   10930 C  C     . LEU A 1 2837 ? 120.719 101.336 84.493  1.00 7.50   ? 2837 LEU A C     1 
ATOM   10931 O  O     . LEU A 1 2837 ? 120.998 100.448 83.682  1.00 10.51  ? 2837 LEU A O     1 
ATOM   10932 C  CB    . LEU A 1 2837 ? 122.673 102.703 85.255  1.00 8.39   ? 2837 LEU A CB    1 
ATOM   10933 C  CG    . LEU A 1 2837 ? 123.514 103.205 86.427  1.00 7.26   ? 2837 LEU A CG    1 
ATOM   10934 C  CD1   . LEU A 1 2837 ? 124.552 104.208 85.967  1.00 5.66   ? 2837 LEU A CD1   1 
ATOM   10935 C  CD2   . LEU A 1 2837 ? 122.598 103.819 87.474  1.00 8.16   ? 2837 LEU A CD2   1 
ATOM   10936 N  N     . VAL A 1 2838 ? 119.614 102.071 84.413  1.00 8.89   ? 2838 VAL A N     1 
ATOM   10937 C  CA    . VAL A 1 2838 ? 118.602 101.846 83.386  1.00 10.85  ? 2838 VAL A CA    1 
ATOM   10938 C  C     . VAL A 1 2838 ? 118.845 102.721 82.164  1.00 14.45  ? 2838 VAL A C     1 
ATOM   10939 O  O     . VAL A 1 2838 ? 118.787 102.248 81.026  1.00 16.01  ? 2838 VAL A O     1 
ATOM   10940 C  CB    . VAL A 1 2838 ? 117.198 102.091 83.979  1.00 10.06  ? 2838 VAL A CB    1 
ATOM   10941 C  CG1   . VAL A 1 2838 ? 116.125 101.872 82.924  1.00 9.28   ? 2838 VAL A CG1   1 
ATOM   10942 C  CG2   . VAL A 1 2838 ? 116.969 101.201 85.191  1.00 6.04   ? 2838 VAL A CG2   1 
ATOM   10943 N  N     . GLU A 1 2839 ? 119.123 104.001 82.378  1.00 16.34  ? 2839 GLU A N     1 
ATOM   10944 C  CA    . GLU A 1 2839 ? 119.203 104.969 81.296  1.00 22.50  ? 2839 GLU A CA    1 
ATOM   10945 C  C     . GLU A 1 2839 ? 120.638 105.132 80.803  1.00 19.26  ? 2839 GLU A C     1 
ATOM   10946 O  O     . GLU A 1 2839 ? 121.606 104.874 81.522  1.00 18.04  ? 2839 GLU A O     1 
ATOM   10947 C  CB    . GLU A 1 2839 ? 118.649 106.322 81.748  1.00 23.69  ? 2839 GLU A CB    1 
ATOM   10948 C  CG    . GLU A 1 2839 ? 117.267 106.277 82.407  1.00 27.22  ? 2839 GLU A CG    1 
ATOM   10949 C  CD    . GLU A 1 2839 ? 116.142 105.820 81.481  1.00 40.17  ? 2839 GLU A CD    1 
ATOM   10950 O  OE1   . GLU A 1 2839 ? 116.404 105.446 80.318  1.00 33.88  ? 2839 GLU A OE1   1 
ATOM   10951 O  OE2   . GLU A 1 2839 ? 114.977 105.836 81.930  1.00 47.09  ? 2839 GLU A OE2   1 
ATOM   10952 N  N     . ASP A 1 2840 ? 120.760 105.570 79.547  1.00 23.79  ? 2840 ASP A N     1 
ATOM   10953 C  CA    . ASP A 1 2840 ? 122.076 105.757 78.946  1.00 20.63  ? 2840 ASP A CA    1 
ATOM   10954 C  C     . ASP A 1 2840 ? 122.816 106.944 79.548  1.00 22.55  ? 2840 ASP A C     1 
ATOM   10955 O  O     . ASP A 1 2840 ? 124.043 106.896 79.692  1.00 22.54  ? 2840 ASP A O     1 
ATOM   10956 C  CB    . ASP A 1 2840 ? 121.944 105.931 77.433  1.00 25.93  ? 2840 ASP A CB    1 
ATOM   10957 C  CG    . ASP A 1 2840 ? 121.503 104.660 76.737  1.00 39.97  ? 2840 ASP A CG    1 
ATOM   10958 O  OD1   . ASP A 1 2840 ? 121.815 103.563 77.245  1.00 42.86  ? 2840 ASP A OD1   1 
ATOM   10959 O  OD2   . ASP A 1 2840 ? 120.846 104.757 75.678  1.00 50.00  ? 2840 ASP A OD2   1 
ATOM   10960 N  N     . GLU A 1 2841 ? 122.100 108.018 79.896  1.00 22.63  ? 2841 GLU A N     1 
ATOM   10961 C  CA    . GLU A 1 2841 ? 122.767 109.179 80.475  1.00 22.70  ? 2841 GLU A CA    1 
ATOM   10962 C  C     . GLU A 1 2841 ? 123.334 108.872 81.856  1.00 19.41  ? 2841 GLU A C     1 
ATOM   10963 O  O     . GLU A 1 2841 ? 124.382 109.410 82.223  1.00 19.60  ? 2841 GLU A O     1 
ATOM   10964 C  CB    . GLU A 1 2841 ? 121.814 110.377 80.531  1.00 23.50  ? 2841 GLU A CB    1 
ATOM   10965 C  CG    . GLU A 1 2841 ? 120.662 110.257 81.519  1.00 32.37  ? 2841 GLU A CG    1 
ATOM   10966 C  CD    . GLU A 1 2841 ? 119.469 109.516 80.945  1.00 43.60  ? 2841 GLU A CD    1 
ATOM   10967 O  OE1   . GLU A 1 2841 ? 119.624 108.839 79.907  1.00 33.26  ? 2841 GLU A OE1   1 
ATOM   10968 O  OE2   . GLU A 1 2841 ? 118.371 109.614 81.534  1.00 41.85  ? 2841 GLU A OE2   1 
ATOM   10969 N  N     . GLU A 1 2842 ? 122.672 108.004 82.626  1.00 14.74  ? 2842 GLU A N     1 
ATOM   10970 C  CA    . GLU A 1 2842 ? 123.219 107.601 83.918  1.00 13.43  ? 2842 GLU A CA    1 
ATOM   10971 C  C     . GLU A 1 2842 ? 124.531 106.844 83.751  1.00 10.74  ? 2842 GLU A C     1 
ATOM   10972 O  O     . GLU A 1 2842 ? 125.503 107.099 84.475  1.00 9.39   ? 2842 GLU A O     1 
ATOM   10973 C  CB    . GLU A 1 2842 ? 122.197 106.750 84.671  1.00 15.01  ? 2842 GLU A CB    1 
ATOM   10974 C  CG    . GLU A 1 2842 ? 120.918 107.489 85.026  1.00 16.25  ? 2842 GLU A CG    1 
ATOM   10975 C  CD    . GLU A 1 2842 ? 119.763 106.551 85.308  1.00 19.36  ? 2842 GLU A CD    1 
ATOM   10976 O  OE1   . GLU A 1 2842 ? 119.932 105.326 85.131  1.00 17.60  ? 2842 GLU A OE1   1 
ATOM   10977 O  OE2   . GLU A 1 2842 ? 118.685 107.037 85.711  1.00 25.13  ? 2842 GLU A OE2   1 
ATOM   10978 N  N     . ARG A 1 2843 ? 124.577 105.910 82.798  1.00 9.94   ? 2843 ARG A N     1 
ATOM   10979 C  CA    . ARG A 1 2843 ? 125.807 105.171 82.535  1.00 9.75   ? 2843 ARG A CA    1 
ATOM   10980 C  C     . ARG A 1 2843 ? 126.902 106.096 82.019  1.00 10.22  ? 2843 ARG A C     1 
ATOM   10981 O  O     . ARG A 1 2843 ? 128.074 105.947 82.383  1.00 8.95   ? 2843 ARG A O     1 
ATOM   10982 C  CB    . ARG A 1 2843 ? 125.530 104.043 81.541  1.00 10.19  ? 2843 ARG A CB    1 
ATOM   10983 C  CG    . ARG A 1 2843 ? 124.433 103.091 81.994  1.00 11.80  ? 2843 ARG A CG    1 
ATOM   10984 C  CD    . ARG A 1 2843 ? 124.352 101.857 81.110  1.00 16.94  ? 2843 ARG A CD    1 
ATOM   10985 N  NE    . ARG A 1 2843 ? 123.450 102.056 79.982  1.00 17.99  ? 2843 ARG A NE    1 
ATOM   10986 C  CZ    . ARG A 1 2843 ? 122.230 101.543 79.899  1.00 18.19  ? 2843 ARG A CZ    1 
ATOM   10987 N  NH1   . ARG A 1 2843 ? 121.730 100.789 80.863  1.00 13.84  ? 2843 ARG A NH1   1 
ATOM   10988 N  NH2   . ARG A 1 2843 ? 121.493 101.795 78.821  1.00 22.06  ? 2843 ARG A NH2   1 
ATOM   10989 N  N     . ARG A 1 2844 ? 126.535 107.059 81.171  1.00 11.04  ? 2844 ARG A N     1 
ATOM   10990 C  CA    . ARG A 1 2844 ? 127.496 108.049 80.695  1.00 12.79  ? 2844 ARG A CA    1 
ATOM   10991 C  C     . ARG A 1 2844 ? 128.066 108.861 81.853  1.00 12.07  ? 2844 ARG A C     1 
ATOM   10992 O  O     . ARG A 1 2844 ? 129.277 109.105 81.920  1.00 10.53  ? 2844 ARG A O     1 
ATOM   10993 C  CB    . ARG A 1 2844 ? 126.822 108.957 79.662  1.00 18.90  ? 2844 ARG A CB    1 
ATOM   10994 C  CG    . ARG A 1 2844 ? 127.739 109.931 78.930  1.00 21.08  ? 2844 ARG A CG    1 
ATOM   10995 C  CD    . ARG A 1 2844 ? 127.832 111.259 79.672  1.00 32.62  ? 2844 ARG A CD    1 
ATOM   10996 N  NE    . ARG A 1 2844 ? 126.532 111.908 79.774  1.00 39.35  ? 2844 ARG A NE    1 
ATOM   10997 C  CZ    . ARG A 1 2844 ? 126.251 112.896 80.613  1.00 45.66  ? 2844 ARG A CZ    1 
ATOM   10998 N  NH1   . ARG A 1 2844 ? 127.160 113.377 81.445  1.00 37.85  ? 2844 ARG A NH1   1 
ATOM   10999 N  NH2   . ARG A 1 2844 ? 125.024 113.411 80.621  1.00 45.17  ? 2844 ARG A NH2   1 
ATOM   11000 N  N     . TRP A 1 2845 ? 127.200 109.294 82.772  1.00 12.82  ? 2845 TRP A N     1 
ATOM   11001 C  CA    . TRP A 1 2845 ? 127.655 110.062 83.926  1.00 12.40  ? 2845 TRP A CA    1 
ATOM   11002 C  C     . TRP A 1 2845 ? 128.597 109.240 84.793  1.00 11.49  ? 2845 TRP A C     1 
ATOM   11003 O  O     . TRP A 1 2845 ? 129.636 109.740 85.240  1.00 13.84  ? 2845 TRP A O     1 
ATOM   11004 C  CB    . TRP A 1 2845 ? 126.452 110.538 84.742  1.00 12.80  ? 2845 TRP A CB    1 
ATOM   11005 C  CG    . TRP A 1 2845 ? 126.815 111.331 85.963  1.00 14.10  ? 2845 TRP A CG    1 
ATOM   11006 C  CD1   . TRP A 1 2845 ? 126.892 112.689 86.062  1.00 17.88  ? 2845 TRP A CD1   1 
ATOM   11007 C  CD2   . TRP A 1 2845 ? 127.144 110.816 87.260  1.00 14.72  ? 2845 TRP A CD2   1 
ATOM   11008 N  NE1   . TRP A 1 2845 ? 127.251 113.052 87.336  1.00 15.38  ? 2845 TRP A NE1   1 
ATOM   11009 C  CE2   . TRP A 1 2845 ? 127.410 111.921 88.092  1.00 13.97  ? 2845 TRP A CE2   1 
ATOM   11010 C  CE3   . TRP A 1 2845 ? 127.240 109.529 87.798  1.00 12.94  ? 2845 TRP A CE3   1 
ATOM   11011 C  CZ2   . TRP A 1 2845 ? 127.770 111.779 89.430  1.00 13.84  ? 2845 TRP A CZ2   1 
ATOM   11012 C  CZ3   . TRP A 1 2845 ? 127.597 109.391 89.127  1.00 15.91  ? 2845 TRP A CZ3   1 
ATOM   11013 C  CH2   . TRP A 1 2845 ? 127.858 110.510 89.927  1.00 16.19  ? 2845 TRP A CH2   1 
ATOM   11014 N  N     . THR A 1 2846 ? 128.248 107.975 85.043  1.00 9.04   ? 2846 THR A N     1 
ATOM   11015 C  CA    . THR A 1 2846 ? 129.120 107.112 85.835  1.00 10.37  ? 2846 THR A CA    1 
ATOM   11016 C  C     . THR A 1 2846 ? 130.472 106.928 85.160  1.00 8.74   ? 2846 THR A C     1 
ATOM   11017 O  O     . THR A 1 2846 ? 131.521 107.024 85.811  1.00 7.74   ? 2846 THR A O     1 
ATOM   11018 C  CB    . THR A 1 2846 ? 128.452 105.756 86.067  1.00 8.94   ? 2846 THR A CB    1 
ATOM   11019 O  OG1   . THR A 1 2846 ? 127.264 105.933 86.848  1.00 9.87   ? 2846 THR A OG1   1 
ATOM   11020 C  CG2   . THR A 1 2846 ? 129.399 104.811 86.793  1.00 6.09   ? 2846 THR A CG2   1 
ATOM   11021 N  N     . ASP A 1 2847 ? 130.466 106.679 83.849  1.00 9.97   ? 2847 ASP A N     1 
ATOM   11022 C  CA    . ASP A 1 2847 ? 131.711 106.474 83.118  1.00 11.75  ? 2847 ASP A CA    1 
ATOM   11023 C  C     . ASP A 1 2847 ? 132.589 107.719 83.153  1.00 13.71  ? 2847 ASP A C     1 
ATOM   11024 O  O     . ASP A 1 2847 ? 133.805 107.623 83.350  1.00 15.47  ? 2847 ASP A O     1 
ATOM   11025 C  CB    . ASP A 1 2847 ? 131.395 106.070 81.678  1.00 12.64  ? 2847 ASP A CB    1 
ATOM   11026 C  CG    . ASP A 1 2847 ? 132.630 105.704 80.889  1.00 30.27  ? 2847 ASP A CG    1 
ATOM   11027 O  OD1   . ASP A 1 2847 ? 133.186 104.609 81.121  1.00 28.29  ? 2847 ASP A OD1   1 
ATOM   11028 O  OD2   . ASP A 1 2847 ? 133.047 106.515 80.037  1.00 33.71  ? 2847 ASP A OD2   1 
ATOM   11029 N  N     . GLU A 1 2848 ? 131.990 108.898 82.969  1.00 15.01  ? 2848 GLU A N     1 
ATOM   11030 C  CA    . GLU A 1 2848 ? 132.767 110.134 82.992  1.00 14.79  ? 2848 GLU A CA    1 
ATOM   11031 C  C     . GLU A 1 2848 ? 133.314 110.428 84.385  1.00 16.29  ? 2848 GLU A C     1 
ATOM   11032 O  O     . GLU A 1 2848 ? 134.477 110.825 84.535  1.00 19.82  ? 2848 GLU A O     1 
ATOM   11033 C  CB    . GLU A 1 2848 ? 131.912 111.300 82.496  1.00 20.28  ? 2848 GLU A CB    1 
ATOM   11034 C  CG    . GLU A 1 2848 ? 132.646 112.631 82.442  1.00 39.98  ? 2848 GLU A CG    1 
ATOM   11035 C  CD    . GLU A 1 2848 ? 133.778 112.639 81.431  1.00 53.46  ? 2848 GLU A CD    1 
ATOM   11036 O  OE1   . GLU A 1 2848 ? 133.716 111.861 80.455  1.00 54.46  ? 2848 GLU A OE1   1 
ATOM   11037 O  OE2   . GLU A 1 2848 ? 134.732 113.423 81.614  1.00 53.38  ? 2848 GLU A OE2   1 
ATOM   11038 N  N     . ASN A 1 2849 ? 132.496 110.240 85.420  1.00 15.39  ? 2849 ASN A N     1 
ATOM   11039 C  CA    . ASN A 1 2849 ? 132.936 110.576 86.765  1.00 13.31  ? 2849 ASN A CA    1 
ATOM   11040 C  C     . ASN A 1 2849 ? 133.928 109.568 87.325  1.00 13.77  ? 2849 ASN A C     1 
ATOM   11041 O  O     . ASN A 1 2849 ? 134.708 109.923 88.214  1.00 14.49  ? 2849 ASN A O     1 
ATOM   11042 C  CB    . ASN A 1 2849 ? 131.723 110.719 87.681  1.00 12.97  ? 2849 ASN A CB    1 
ATOM   11043 C  CG    . ASN A 1 2849 ? 131.010 112.041 87.479  1.00 22.53  ? 2849 ASN A CG    1 
ATOM   11044 O  OD1   . ASN A 1 2849 ? 131.373 113.055 88.074  1.00 25.46  ? 2849 ASN A OD1   1 
ATOM   11045 N  ND2   . ASN A 1 2849 ? 130.014 112.045 86.604  1.00 22.08  ? 2849 ASN A ND2   1 
ATOM   11046 N  N     . ILE A 1 2850 ? 133.941 108.337 86.807  1.00 12.02  ? 2850 ILE A N     1 
ATOM   11047 C  CA    . ILE A 1 2850 ? 135.039 107.424 87.117  1.00 11.21  ? 2850 ILE A CA    1 
ATOM   11048 C  C     . ILE A 1 2850 ? 136.365 108.034 86.682  1.00 16.53  ? 2850 ILE A C     1 
ATOM   11049 O  O     . ILE A 1 2850 ? 137.325 108.096 87.459  1.00 15.32  ? 2850 ILE A O     1 
ATOM   11050 C  CB    . ILE A 1 2850 ? 134.802 106.052 86.459  1.00 12.18  ? 2850 ILE A CB    1 
ATOM   11051 C  CG1   . ILE A 1 2850 ? 133.784 105.247 87.266  1.00 8.70   ? 2850 ILE A CG1   1 
ATOM   11052 C  CG2   . ILE A 1 2850 ? 136.113 105.297 86.292  1.00 11.50  ? 2850 ILE A CG2   1 
ATOM   11053 C  CD1   . ILE A 1 2850 ? 133.353 103.965 86.611  1.00 8.13   ? 2850 ILE A CD1   1 
ATOM   11054 N  N     . ASP A 1 2851 ? 136.425 108.519 85.437  1.00 19.59  ? 2851 ASP A N     1 
ATOM   11055 C  CA    . ASP A 1 2851 ? 137.628 109.186 84.951  1.00 21.58  ? 2851 ASP A CA    1 
ATOM   11056 C  C     . ASP A 1 2851 ? 137.951 110.412 85.794  1.00 20.34  ? 2851 ASP A C     1 
ATOM   11057 O  O     . ASP A 1 2851 ? 139.116 110.655 86.136  1.00 22.76  ? 2851 ASP A O     1 
ATOM   11058 C  CB    . ASP A 1 2851 ? 137.446 109.597 83.488  1.00 24.48  ? 2851 ASP A CB    1 
ATOM   11059 C  CG    . ASP A 1 2851 ? 137.158 108.421 82.575  1.00 29.93  ? 2851 ASP A CG    1 
ATOM   11060 O  OD1   . ASP A 1 2851 ? 138.003 107.510 82.484  1.00 35.44  ? 2851 ASP A OD1   1 
ATOM   11061 O  OD2   . ASP A 1 2851 ? 136.083 108.412 81.941  1.00 32.74  ? 2851 ASP A OD2   1 
ATOM   11062 N  N     . THR A 1 2852 ? 136.926 111.198 86.130  1.00 16.39  ? 2852 THR A N     1 
ATOM   11063 C  CA    . THR A 1 2852 ? 137.141 112.426 86.890  1.00 17.83  ? 2852 THR A CA    1 
ATOM   11064 C  C     . THR A 1 2852 ? 137.771 112.135 88.250  1.00 20.44  ? 2852 THR A C     1 
ATOM   11065 O  O     . THR A 1 2852 ? 138.796 112.725 88.610  1.00 17.98  ? 2852 THR A O     1 
ATOM   11066 C  CB    . THR A 1 2852 ? 135.818 113.175 87.062  1.00 21.78  ? 2852 THR A CB    1 
ATOM   11067 O  OG1   . THR A 1 2852 ? 135.288 113.514 85.774  1.00 25.91  ? 2852 THR A OG1   1 
ATOM   11068 C  CG2   . THR A 1 2852 ? 136.029 114.447 87.864  1.00 21.06  ? 2852 THR A CG2   1 
ATOM   11069 N  N     . VAL A 1 2853 ? 137.173 111.219 89.016  1.00 18.70  ? 2853 VAL A N     1 
ATOM   11070 C  CA    . VAL A 1 2853 ? 137.707 110.876 90.333  1.00 15.24  ? 2853 VAL A CA    1 
ATOM   11071 C  C     . VAL A 1 2853 ? 139.092 110.255 90.203  1.00 16.29  ? 2853 VAL A C     1 
ATOM   11072 O  O     . VAL A 1 2853 ? 140.010 110.571 90.976  1.00 20.25  ? 2853 VAL A O     1 
ATOM   11073 C  CB    . VAL A 1 2853 ? 136.731 109.944 91.077  1.00 12.30  ? 2853 VAL A CB    1 
ATOM   11074 C  CG1   . VAL A 1 2853 ? 137.388 109.354 92.315  1.00 10.30  ? 2853 VAL A CG1   1 
ATOM   11075 C  CG2   . VAL A 1 2853 ? 135.462 110.694 91.449  1.00 8.65   ? 2853 VAL A CG2   1 
ATOM   11076 N  N     . ALA A 1 2854 ? 139.268 109.367 89.217  1.00 16.18  ? 2854 ALA A N     1 
ATOM   11077 C  CA    . ALA A 1 2854 ? 140.551 108.705 89.025  1.00 15.53  ? 2854 ALA A CA    1 
ATOM   11078 C  C     . ALA A 1 2854 ? 141.666 109.712 88.788  1.00 22.70  ? 2854 ALA A C     1 
ATOM   11079 O  O     . ALA A 1 2854 ? 142.747 109.602 89.378  1.00 25.41  ? 2854 ALA A O     1 
ATOM   11080 C  CB    . ALA A 1 2854 ? 140.459 107.726 87.858  1.00 15.21  ? 2854 ALA A CB    1 
ATOM   11081 N  N     . LEU A 1 2855 ? 141.425 110.701 87.928  1.00 24.65  ? 2855 LEU A N     1 
ATOM   11082 C  CA    . LEU A 1 2855 ? 142.471 111.675 87.644  1.00 25.71  ? 2855 LEU A CA    1 
ATOM   11083 C  C     . LEU A 1 2855 ? 142.560 112.742 88.727  1.00 26.67  ? 2855 LEU A C     1 
ATOM   11084 O  O     . LEU A 1 2855 ? 143.568 113.454 88.807  1.00 37.42  ? 2855 LEU A O     1 
ATOM   11085 C  CB    . LEU A 1 2855 ? 142.250 112.308 86.270  1.00 25.80  ? 2855 LEU A CB    1 
ATOM   11086 C  CG    . LEU A 1 2855 ? 142.774 111.520 85.061  1.00 37.69  ? 2855 LEU A CG    1 
ATOM   11087 C  CD1   . LEU A 1 2855 ? 144.290 111.406 85.134  1.00 32.41  ? 2855 LEU A CD1   1 
ATOM   11088 C  CD2   . LEU A 1 2855 ? 142.143 110.137 84.939  1.00 32.32  ? 2855 LEU A CD2   1 
ATOM   11089 N  N     . LYS A 1 2856 ? 141.530 112.875 89.566  1.00 22.19  ? 2856 LYS A N     1 
ATOM   11090 C  CA    . LYS A 1 2856 ? 141.643 113.791 90.694  1.00 17.53  ? 2856 LYS A CA    1 
ATOM   11091 C  C     . LYS A 1 2856 ? 142.560 113.229 91.774  1.00 20.46  ? 2856 LYS A C     1 
ATOM   11092 O  O     . LYS A 1 2856 ? 143.438 113.939 92.278  1.00 21.97  ? 2856 LYS A O     1 
ATOM   11093 C  CB    . LYS A 1 2856 ? 140.265 114.103 91.276  1.00 18.86  ? 2856 LYS A CB    1 
ATOM   11094 C  CG    . LYS A 1 2856 ? 140.333 114.806 92.625  1.00 17.29  ? 2856 LYS A CG    1 
ATOM   11095 C  CD    . LYS A 1 2856 ? 138.967 114.943 93.271  1.00 21.21  ? 2856 LYS A CD    1 
ATOM   11096 C  CE    . LYS A 1 2856 ? 139.087 115.488 94.685  1.00 24.39  ? 2856 LYS A CE    1 
ATOM   11097 N  NZ    . LYS A 1 2856 ? 137.757 115.699 95.319  1.00 25.91  ? 2856 LYS A NZ    1 
ATOM   11098 N  N     . HIS A 1 2857 ? 142.382 111.957 92.140  1.00 22.16  ? 2857 HIS A N     1 
ATOM   11099 C  CA    . HIS A 1 2857 ? 143.198 111.391 93.211  1.00 17.38  ? 2857 HIS A CA    1 
ATOM   11100 C  C     . HIS A 1 2857 ? 144.479 110.725 92.728  1.00 19.58  ? 2857 HIS A C     1 
ATOM   11101 O  O     . HIS A 1 2857 ? 145.354 110.441 93.554  1.00 18.38  ? 2857 HIS A O     1 
ATOM   11102 C  CB    . HIS A 1 2857 ? 142.395 110.379 94.035  1.00 14.46  ? 2857 HIS A CB    1 
ATOM   11103 C  CG    . HIS A 1 2857 ? 141.173 110.954 94.677  1.00 15.08  ? 2857 HIS A CG    1 
ATOM   11104 N  ND1   . HIS A 1 2857 ? 141.206 111.577 95.905  1.00 13.47  ? 2857 HIS A ND1   1 
ATOM   11105 C  CD2   . HIS A 1 2857 ? 139.885 110.999 94.266  1.00 12.32  ? 2857 HIS A CD2   1 
ATOM   11106 C  CE1   . HIS A 1 2857 ? 139.991 111.982 96.224  1.00 14.66  ? 2857 HIS A CE1   1 
ATOM   11107 N  NE2   . HIS A 1 2857 ? 139.170 111.642 95.246  1.00 14.27  ? 2857 HIS A NE2   1 
ATOM   11108 N  N     . PHE A 1 2858 ? 144.623 110.466 91.431  1.00 21.22  ? 2858 PHE A N     1 
ATOM   11109 C  CA    . PHE A 1 2858 ? 145.824 109.830 90.887  1.00 20.70  ? 2858 PHE A CA    1 
ATOM   11110 C  C     . PHE A 1 2858 ? 146.346 110.623 89.696  1.00 31.03  ? 2858 PHE A C     1 
ATOM   11111 O  O     . PHE A 1 2858 ? 146.182 110.210 88.540  1.00 33.67  ? 2858 PHE A O     1 
ATOM   11112 C  CB    . PHE A 1 2858 ? 145.546 108.378 90.497  1.00 15.15  ? 2858 PHE A CB    1 
ATOM   11113 C  CG    . PHE A 1 2858 ? 145.355 107.465 91.670  1.00 16.07  ? 2858 PHE A CG    1 
ATOM   11114 C  CD1   . PHE A 1 2858 ? 146.433 106.807 92.237  1.00 14.47  ? 2858 PHE A CD1   1 
ATOM   11115 C  CD2   . PHE A 1 2858 ? 144.098 107.278 92.218  1.00 11.82  ? 2858 PHE A CD2   1 
ATOM   11116 C  CE1   . PHE A 1 2858 ? 146.256 105.968 93.317  1.00 8.03   ? 2858 PHE A CE1   1 
ATOM   11117 C  CE2   . PHE A 1 2858 ? 143.916 106.442 93.298  1.00 8.42   ? 2858 PHE A CE2   1 
ATOM   11118 C  CZ    . PHE A 1 2858 ? 144.996 105.787 93.848  1.00 7.50   ? 2858 PHE A CZ    1 
ATOM   11119 N  N     . PRO A 1 2859 ? 146.982 111.776 89.940  1.00 37.99  ? 2859 PRO A N     1 
ATOM   11120 C  CA    . PRO A 1 2859 ? 147.670 112.473 88.846  1.00 39.51  ? 2859 PRO A CA    1 
ATOM   11121 C  C     . PRO A 1 2859 ? 148.958 111.768 88.452  1.00 39.06  ? 2859 PRO A C     1 
ATOM   11122 O  O     . PRO A 1 2859 ? 149.293 110.718 89.010  1.00 43.37  ? 2859 PRO A O     1 
ATOM   11123 C  CB    . PRO A 1 2859 ? 147.956 113.861 89.435  1.00 35.54  ? 2859 PRO A CB    1 
ATOM   11124 C  CG    . PRO A 1 2859 ? 147.003 114.006 90.573  1.00 25.81  ? 2859 PRO A CG    1 
ATOM   11125 C  CD    . PRO A 1 2859 ? 146.870 112.625 91.137  1.00 27.43  ? 2859 PRO A CD    1 
ATOM   11126 N  N     . ASN A 1 2860 ? 149.684 112.345 87.493  1.00 34.52  ? 2860 ASN A N     1 
ATOM   11127 C  CA    . ASN A 1 2860 ? 151.007 111.857 87.092  1.00 41.59  ? 2860 ASN A CA    1 
ATOM   11128 C  C     . ASN A 1 2860 ? 150.961 110.398 86.643  1.00 45.29  ? 2860 ASN A C     1 
ATOM   11129 O  O     . ASN A 1 2860 ? 151.880 109.619 86.903  1.00 44.18  ? 2860 ASN A O     1 
ATOM   11130 C  CB    . ASN A 1 2860 ? 152.026 112.047 88.219  1.00 41.49  ? 2860 ASN A CB    1 
ATOM   11131 C  CG    . ASN A 1 2860 ? 151.871 113.378 88.927  1.00 45.05  ? 2860 ASN A CG    1 
ATOM   11132 O  OD1   . ASN A 1 2860 ? 151.990 114.439 88.314  1.00 44.14  ? 2860 ASN A OD1   1 
ATOM   11133 N  ND2   . ASN A 1 2860 ? 151.601 113.328 90.226  1.00 42.58  ? 2860 ASN A ND2   1 
ATOM   11134 N  N     . ILE A 1 2861 ? 149.878 110.023 85.963  1.00 47.07  ? 2861 ILE A N     1 
ATOM   11135 C  CA    . ILE A 1 2861 ? 149.738 108.696 85.381  1.00 46.11  ? 2861 ILE A CA    1 
ATOM   11136 C  C     . ILE A 1 2861 ? 149.383 108.858 83.911  1.00 50.09  ? 2861 ILE A C     1 
ATOM   11137 O  O     . ILE A 1 2861 ? 149.000 109.937 83.453  1.00 54.64  ? 2861 ILE A O     1 
ATOM   11138 C  CB    . ILE A 1 2861 ? 148.671 107.839 86.092  1.00 42.34  ? 2861 ILE A CB    1 
ATOM   11139 C  CG1   . ILE A 1 2861 ? 147.287 108.462 85.912  1.00 44.62  ? 2861 ILE A CG1   1 
ATOM   11140 C  CG2   . ILE A 1 2861 ? 148.999 107.687 87.568  1.00 37.59  ? 2861 ILE A CG2   1 
ATOM   11141 C  CD1   . ILE A 1 2861 ? 146.164 107.556 86.334  1.00 34.30  ? 2861 ILE A CD1   1 
ATOM   11142 N  N     . ASP A 1 2862 ? 149.516 107.763 83.167  1.00 48.61  ? 2862 ASP A N     1 
ATOM   11143 C  CA    . ASP A 1 2862 ? 149.151 107.754 81.756  1.00 47.18  ? 2862 ASP A CA    1 
ATOM   11144 C  C     . ASP A 1 2862 ? 147.659 107.446 81.676  1.00 46.77  ? 2862 ASP A C     1 
ATOM   11145 O  O     . ASP A 1 2862 ? 147.220 106.360 82.065  1.00 43.78  ? 2862 ASP A O     1 
ATOM   11146 C  CB    . ASP A 1 2862 ? 149.997 106.735 80.993  1.00 40.11  ? 2862 ASP A CB    1 
ATOM   11147 C  CG    . ASP A 1 2862 ? 149.521 106.499 79.559  1.00 52.23  ? 2862 ASP A CG    1 
ATOM   11148 O  OD1   . ASP A 1 2862 ? 148.540 107.125 79.103  1.00 51.55  ? 2862 ASP A OD1   1 
ATOM   11149 O  OD2   . ASP A 1 2862 ? 150.158 105.679 78.867  1.00 58.55  ? 2862 ASP A OD2   1 
ATOM   11150 N  N     . ARG A 1 2863 ? 146.883 108.411 81.177  1.00 47.22  ? 2863 ARG A N     1 
ATOM   11151 C  CA    . ARG A 1 2863 ? 145.432 108.258 81.127  1.00 44.40  ? 2863 ARG A CA    1 
ATOM   11152 C  C     . ARG A 1 2863 ? 145.018 107.082 80.250  1.00 45.06  ? 2863 ARG A C     1 
ATOM   11153 O  O     . ARG A 1 2863 ? 144.079 106.353 80.585  1.00 42.46  ? 2863 ARG A O     1 
ATOM   11154 C  CB    . ARG A 1 2863 ? 144.789 109.548 80.618  1.00 47.20  ? 2863 ARG A CB    1 
ATOM   11155 C  CG    . ARG A 1 2863 ? 143.267 109.532 80.604  1.00 47.66  ? 2863 ARG A CG    1 
ATOM   11156 C  CD    . ARG A 1 2863 ? 142.710 110.880 80.167  1.00 52.93  ? 2863 ARG A CD    1 
ATOM   11157 N  NE    . ARG A 1 2863 ? 141.256 110.870 80.058  1.00 54.46  ? 2863 ARG A NE    1 
ATOM   11158 C  CZ    . ARG A 1 2863 ? 140.424 111.114 81.062  1.00 51.46  ? 2863 ARG A CZ    1 
ATOM   11159 N  NH1   . ARG A 1 2863 ? 140.868 111.424 82.268  1.00 46.96  ? 2863 ARG A NH1   1 
ATOM   11160 N  NH2   . ARG A 1 2863 ? 139.113 111.055 80.847  1.00 53.53  ? 2863 ARG A NH2   1 
ATOM   11161 N  N     . GLU A 1 2864 ? 145.692 106.894 79.113  1.00 42.77  ? 2864 GLU A N     1 
ATOM   11162 C  CA    . GLU A 1 2864 ? 145.238 105.903 78.141  1.00 42.18  ? 2864 GLU A CA    1 
ATOM   11163 C  C     . GLU A 1 2864 ? 145.403 104.479 78.663  1.00 42.94  ? 2864 GLU A C     1 
ATOM   11164 O  O     . GLU A 1 2864 ? 144.510 103.643 78.486  1.00 43.56  ? 2864 GLU A O     1 
ATOM   11165 C  CB    . GLU A 1 2864 ? 145.986 106.092 76.820  1.00 51.73  ? 2864 GLU A CB    1 
ATOM   11166 C  CG    . GLU A 1 2864 ? 145.786 104.972 75.810  1.00 52.14  ? 2864 GLU A CG    1 
ATOM   11167 C  CD    . GLU A 1 2864 ? 146.917 103.962 75.825  1.00 59.39  ? 2864 GLU A CD    1 
ATOM   11168 O  OE1   . GLU A 1 2864 ? 146.681 102.799 75.437  1.00 59.63  ? 2864 GLU A OE1   1 
ATOM   11169 O  OE2   . GLU A 1 2864 ? 148.041 104.334 76.221  1.00 57.71  ? 2864 GLU A OE2   1 
ATOM   11170 N  N     . LYS A 1 2865 ? 146.530 104.182 79.315  1.00 36.45  ? 2865 LYS A N     1 
ATOM   11171 C  CA    . LYS A 1 2865 ? 146.778 102.820 79.777  1.00 34.52  ? 2865 LYS A CA    1 
ATOM   11172 C  C     . LYS A 1 2865 ? 145.926 102.439 80.980  1.00 40.36  ? 2865 LYS A C     1 
ATOM   11173 O  O     . LYS A 1 2865 ? 145.895 101.260 81.350  1.00 36.65  ? 2865 LYS A O     1 
ATOM   11174 C  CB    . LYS A 1 2865 ? 148.256 102.633 80.123  1.00 36.31  ? 2865 LYS A CB    1 
ATOM   11175 C  CG    . LYS A 1 2865 ? 149.191 102.687 78.929  1.00 46.25  ? 2865 LYS A CG    1 
ATOM   11176 C  CD    . LYS A 1 2865 ? 150.633 102.463 79.356  1.00 49.91  ? 2865 LYS A CD    1 
ATOM   11177 C  CE    . LYS A 1 2865 ? 151.581 102.537 78.172  1.00 52.75  ? 2865 LYS A CE    1 
ATOM   11178 N  NZ    . LYS A 1 2865 ? 152.997 102.331 78.584  1.00 51.43  ? 2865 LYS A NZ    1 
ATOM   11179 N  N     . ALA A 1 2866 ? 145.239 103.397 81.598  1.00 35.95  ? 2866 ALA A N     1 
ATOM   11180 C  CA    . ALA A 1 2866 ? 144.432 103.116 82.777  1.00 25.48  ? 2866 ALA A CA    1 
ATOM   11181 C  C     . ALA A 1 2866 ? 142.941 103.318 82.555  1.00 29.84  ? 2866 ALA A C     1 
ATOM   11182 O  O     . ALA A 1 2866 ? 142.138 102.732 83.286  1.00 32.67  ? 2866 ALA A O     1 
ATOM   11183 C  CB    . ALA A 1 2866 ? 144.887 103.988 83.951  1.00 24.60  ? 2866 ALA A CB    1 
ATOM   11184 N  N     . MET A 1 2867 ? 142.548 104.132 81.575  1.00 31.60  ? 2867 MET A N     1 
ATOM   11185 C  CA    . MET A 1 2867 ? 141.145 104.464 81.357  1.00 27.44  ? 2867 MET A CA    1 
ATOM   11186 C  C     . MET A 1 2867 ? 140.729 104.260 79.906  1.00 29.91  ? 2867 MET A C     1 
ATOM   11187 O  O     . MET A 1 2867 ? 139.811 104.930 79.423  1.00 37.84  ? 2867 MET A O     1 
ATOM   11188 C  CB    . MET A 1 2867 ? 140.848 105.897 81.797  1.00 35.51  ? 2867 MET A CB    1 
ATOM   11189 C  CG    . MET A 1 2867 ? 141.135 106.149 83.260  1.00 31.34  ? 2867 MET A CG    1 
ATOM   11190 S  SD    . MET A 1 2867 ? 139.703 105.739 84.270  1.00 38.23  ? 2867 MET A SD    1 
ATOM   11191 C  CE    . MET A 1 2867 ? 140.501 104.970 85.663  1.00 20.76  ? 2867 MET A CE    1 
ATOM   11192 N  N     . SER A 1 2868 ? 141.396 103.354 79.193  1.00 26.32  ? 2868 SER A N     1 
ATOM   11193 C  CA    . SER A 1 2868 ? 140.913 102.951 77.878  1.00 27.85  ? 2868 SER A CA    1 
ATOM   11194 C  C     . SER A 1 2868 ? 139.515 102.371 78.036  1.00 27.14  ? 2868 SER A C     1 
ATOM   11195 O  O     . SER A 1 2868 ? 139.345 101.320 78.662  1.00 27.03  ? 2868 SER A O     1 
ATOM   11196 C  CB    . SER A 1 2868 ? 141.861 101.942 77.230  1.00 33.31  ? 2868 SER A CB    1 
ATOM   11197 O  OG    . SER A 1 2868 ? 143.132 102.519 76.985  1.00 37.83  ? 2868 SER A OG    1 
ATOM   11198 N  N     . ARG A 1 2869 ? 138.519 103.046 77.464  1.00 28.32  ? 2869 ARG A N     1 
ATOM   11199 C  CA    . ARG A 1 2869 ? 137.125 102.812 77.837  1.00 31.39  ? 2869 ARG A CA    1 
ATOM   11200 C  C     . ARG A 1 2869 ? 136.662 101.361 77.739  1.00 40.41  ? 2869 ARG A C     1 
ATOM   11201 O  O     . ARG A 1 2869 ? 135.905 100.932 78.626  1.00 45.45  ? 2869 ARG A O     1 
ATOM   11202 C  CB    . ARG A 1 2869 ? 136.214 103.730 77.010  1.00 34.59  ? 2869 ARG A CB    1 
ATOM   11203 C  CG    . ARG A 1 2869 ? 136.184 105.191 77.479  1.00 42.62  ? 2869 ARG A CG    1 
ATOM   11204 C  CD    . ARG A 1 2869 ? 135.745 105.357 78.944  1.00 46.11  ? 2869 ARG A CD    1 
ATOM   11205 N  NE    . ARG A 1 2869 ? 136.793 105.049 79.913  1.00 43.07  ? 2869 ARG A NE    1 
ATOM   11206 C  CZ    . ARG A 1 2869 ? 136.615 104.998 81.227  1.00 35.83  ? 2869 ARG A CZ    1 
ATOM   11207 N  NH1   . ARG A 1 2869 ? 135.434 105.220 81.775  1.00 25.58  ? 2869 ARG A NH1   1 
ATOM   11208 N  NH2   . ARG A 1 2869 ? 137.651 104.714 82.011  1.00 34.05  ? 2869 ARG A NH2   1 
ATOM   11209 N  N     . PRO A 1 2870 ? 137.040 100.562 76.730  1.00 32.70  ? 2870 PRO A N     1 
ATOM   11210 C  CA    . PRO A 1 2870 ? 136.667 99.141  76.781  1.00 27.88  ? 2870 PRO A CA    1 
ATOM   11211 C  C     . PRO A 1 2870 ? 137.453 98.403  77.854  1.00 20.19  ? 2870 PRO A C     1 
ATOM   11212 O  O     . PRO A 1 2870 ? 138.425 97.700  77.560  1.00 23.74  ? 2870 PRO A O     1 
ATOM   11213 C  CB    . PRO A 1 2870 ? 136.998 98.635  75.372  1.00 24.76  ? 2870 PRO A CB    1 
ATOM   11214 C  CG    . PRO A 1 2870 ? 138.047 99.559  74.880  1.00 27.62  ? 2870 PRO A CG    1 
ATOM   11215 C  CD    . PRO A 1 2870 ? 137.712 100.901 75.461  1.00 26.31  ? 2870 PRO A CD    1 
ATOM   11216 N  N     . ILE A 1 2871 ? 137.031 98.566  79.105  1.00 15.73  ? 2871 ILE A N     1 
ATOM   11217 C  CA    . ILE A 1 2871 ? 137.713 97.982  80.255  1.00 14.57  ? 2871 ILE A CA    1 
ATOM   11218 C  C     . ILE A 1 2871 ? 137.142 96.587  80.476  1.00 11.00  ? 2871 ILE A C     1 
ATOM   11219 O  O     . ILE A 1 2871 ? 136.056 96.434  81.040  1.00 10.20  ? 2871 ILE A O     1 
ATOM   11220 C  CB    . ILE A 1 2871 ? 137.542 98.849  81.507  1.00 13.32  ? 2871 ILE A CB    1 
ATOM   11221 C  CG1   . ILE A 1 2871 ? 137.757 100.324 81.169  1.00 19.45  ? 2871 ILE A CG1   1 
ATOM   11222 C  CG2   . ILE A 1 2871 ? 138.501 98.397  82.599  1.00 9.63   ? 2871 ILE A CG2   1 
ATOM   11223 C  CD1   . ILE A 1 2871 ? 137.733 101.235 82.366  1.00 21.06  ? 2871 ILE A CD1   1 
ATOM   11224 N  N     . LEU A 1 2872 ? 137.872 95.568  80.037  1.00 10.43  ? 2872 LEU A N     1 
ATOM   11225 C  CA    . LEU A 1 2872 ? 137.412 94.190  80.121  1.00 8.67   ? 2872 LEU A CA    1 
ATOM   11226 C  C     . LEU A 1 2872 ? 138.453 93.344  80.838  1.00 6.86   ? 2872 LEU A C     1 
ATOM   11227 O  O     . LEU A 1 2872 ? 139.640 93.388  80.499  1.00 6.66   ? 2872 LEU A O     1 
ATOM   11228 C  CB    . LEU A 1 2872 ? 137.122 93.629  78.727  1.00 12.79  ? 2872 LEU A CB    1 
ATOM   11229 C  CG    . LEU A 1 2872 ? 136.167 94.516  77.923  1.00 15.43  ? 2872 LEU A CG    1 
ATOM   11230 C  CD1   . LEU A 1 2872 ? 136.113 94.114  76.456  1.00 13.36  ? 2872 LEU A CD1   1 
ATOM   11231 C  CD2   . LEU A 1 2872 ? 134.780 94.520  78.549  1.00 11.46  ? 2872 LEU A CD2   1 
ATOM   11232 N  N     . TYR A 1 2873 ? 138.002 92.581  81.828  1.00 7.04   ? 2873 TYR A N     1 
ATOM   11233 C  CA    . TYR A 1 2873 ? 138.844 91.676  82.594  1.00 6.88   ? 2873 TYR A CA    1 
ATOM   11234 C  C     . TYR A 1 2873 ? 138.289 90.265  82.477  1.00 5.78   ? 2873 TYR A C     1 
ATOM   11235 O  O     . TYR A 1 2873 ? 137.070 90.070  82.443  1.00 6.89   ? 2873 TYR A O     1 
ATOM   11236 C  CB    . TYR A 1 2873 ? 138.907 92.098  84.066  1.00 4.74   ? 2873 TYR A CB    1 
ATOM   11237 C  CG    . TYR A 1 2873 ? 139.949 93.148  84.369  1.00 4.64   ? 2873 TYR A CG    1 
ATOM   11238 C  CD1   . TYR A 1 2873 ? 139.733 94.482  84.049  1.00 5.07   ? 2873 TYR A CD1   1 
ATOM   11239 C  CD2   . TYR A 1 2873 ? 141.143 92.809  84.988  1.00 4.28   ? 2873 TYR A CD2   1 
ATOM   11240 C  CE1   . TYR A 1 2873 ? 140.682 95.446  84.328  1.00 4.83   ? 2873 TYR A CE1   1 
ATOM   11241 C  CE2   . TYR A 1 2873 ? 142.095 93.765  85.276  1.00 4.12   ? 2873 TYR A CE2   1 
ATOM   11242 C  CZ    . TYR A 1 2873 ? 141.861 95.081  84.941  1.00 4.99   ? 2873 TYR A CZ    1 
ATOM   11243 O  OH    . TYR A 1 2873 ? 142.809 96.035  85.222  1.00 7.55   ? 2873 TYR A OH    1 
ATOM   11244 N  N     . SER A 1 2874 ? 139.182 89.282  82.412  1.00 6.93   ? 2874 SER A N     1 
ATOM   11245 C  CA    . SER A 1 2874 ? 138.754 87.898  82.270  1.00 6.55   ? 2874 SER A CA    1 
ATOM   11246 C  C     . SER A 1 2874 ? 139.864 86.972  82.738  1.00 6.60   ? 2874 SER A C     1 
ATOM   11247 O  O     . SER A 1 2874 ? 141.036 87.352  82.801  1.00 8.13   ? 2874 SER A O     1 
ATOM   11248 C  CB    . SER A 1 2874 ? 138.368 87.577  80.821  1.00 5.77   ? 2874 SER A CB    1 
ATOM   11249 O  OG    . SER A 1 2874 ? 137.782 86.291  80.720  1.00 8.34   ? 2874 SER A OG    1 
ATOM   11250 N  N     . ASN A 1 2875 ? 139.470 85.742  83.069  1.00 7.35   ? 2875 ASN A N     1 
ATOM   11251 C  CA    . ASN A 1 2875 ? 140.397 84.649  83.326  1.00 11.03  ? 2875 ASN A CA    1 
ATOM   11252 C  C     . ASN A 1 2875 ? 140.228 83.522  82.313  1.00 13.07  ? 2875 ASN A C     1 
ATOM   11253 O  O     . ASN A 1 2875 ? 140.578 82.373  82.599  1.00 18.07  ? 2875 ASN A O     1 
ATOM   11254 C  CB    . ASN A 1 2875 ? 140.223 84.119  84.749  1.00 10.94  ? 2875 ASN A CB    1 
ATOM   11255 C  CG    . ASN A 1 2875 ? 138.779 83.797  85.081  1.00 13.17  ? 2875 ASN A CG    1 
ATOM   11256 O  OD1   . ASN A 1 2875 ? 137.895 83.903  84.232  1.00 14.14  ? 2875 ASN A OD1   1 
ATOM   11257 N  ND2   . ASN A 1 2875 ? 138.535 83.397  86.322  1.00 14.86  ? 2875 ASN A ND2   1 
ATOM   11258 N  N     . TRP A 1 2876 ? 139.680 83.831  81.139  1.00 10.43  ? 2876 TRP A N     1 
ATOM   11259 C  CA    . TRP A 1 2876 ? 139.459 82.834  80.101  1.00 12.29  ? 2876 TRP A CA    1 
ATOM   11260 C  C     . TRP A 1 2876 ? 140.675 82.634  79.210  1.00 17.86  ? 2876 TRP A C     1 
ATOM   11261 O  O     . TRP A 1 2876 ? 140.889 81.525  78.707  1.00 17.39  ? 2876 TRP A O     1 
ATOM   11262 C  CB    . TRP A 1 2876 ? 138.260 83.235  79.238  1.00 7.98   ? 2876 TRP A CB    1 
ATOM   11263 C  CG    . TRP A 1 2876 ? 136.934 83.040  79.905  1.00 9.78   ? 2876 TRP A CG    1 
ATOM   11264 C  CD1   . TRP A 1 2876 ? 136.684 82.339  81.048  1.00 10.52  ? 2876 TRP A CD1   1 
ATOM   11265 C  CD2   . TRP A 1 2876 ? 135.671 83.555  79.467  1.00 7.61   ? 2876 TRP A CD2   1 
ATOM   11266 N  NE1   . TRP A 1 2876 ? 135.345 82.386  81.349  1.00 6.00   ? 2876 TRP A NE1   1 
ATOM   11267 C  CE2   . TRP A 1 2876 ? 134.701 83.126  80.393  1.00 6.10   ? 2876 TRP A CE2   1 
ATOM   11268 C  CE3   . TRP A 1 2876 ? 135.268 84.338  78.381  1.00 7.22   ? 2876 TRP A CE3   1 
ATOM   11269 C  CZ2   . TRP A 1 2876 ? 133.353 83.453  80.267  1.00 6.11   ? 2876 TRP A CZ2   1 
ATOM   11270 C  CZ3   . TRP A 1 2876 ? 133.929 84.661  78.258  1.00 7.52   ? 2876 TRP A CZ3   1 
ATOM   11271 C  CH2   . TRP A 1 2876 ? 132.988 84.219  79.195  1.00 7.36   ? 2876 TRP A CH2   1 
ATOM   11272 N  N     . LEU A 1 2877 ? 141.473 83.679  79.001  1.00 15.33  ? 2877 LEU A N     1 
ATOM   11273 C  CA    . LEU A 1 2877 ? 142.668 83.602  78.172  1.00 15.20  ? 2877 LEU A CA    1 
ATOM   11274 C  C     . LEU A 1 2877 ? 143.938 83.404  78.984  1.00 18.42  ? 2877 LEU A C     1 
ATOM   11275 O  O     . LEU A 1 2877 ? 145.027 83.355  78.403  1.00 20.83  ? 2877 LEU A O     1 
ATOM   11276 C  CB    . LEU A 1 2877 ? 142.801 84.866  77.314  1.00 16.50  ? 2877 LEU A CB    1 
ATOM   11277 C  CG    . LEU A 1 2877 ? 141.631 85.250  76.407  1.00 16.05  ? 2877 LEU A CG    1 
ATOM   11278 C  CD1   . LEU A 1 2877 ? 142.115 86.144  75.281  1.00 20.31  ? 2877 LEU A CD1   1 
ATOM   11279 C  CD2   . LEU A 1 2877 ? 140.951 84.016  75.843  1.00 11.79  ? 2877 LEU A CD2   1 
ATOM   11280 N  N     . SER A 1 2878 ? 143.828 83.287  80.303  1.00 22.05  ? 2878 SER A N     1 
ATOM   11281 C  CA    . SER A 1 2878 ? 144.991 83.125  81.163  1.00 18.02  ? 2878 SER A CA    1 
ATOM   11282 C  C     . SER A 1 2878 ? 144.529 82.543  82.490  1.00 23.04  ? 2878 SER A C     1 
ATOM   11283 O  O     . SER A 1 2878 ? 143.336 82.519  82.800  1.00 25.60  ? 2878 SER A O     1 
ATOM   11284 C  CB    . SER A 1 2878 ? 145.722 84.453  81.371  1.00 20.41  ? 2878 SER A CB    1 
ATOM   11285 O  OG    . SER A 1 2878 ? 144.830 85.444  81.848  1.00 27.07  ? 2878 SER A OG    1 
ATOM   11286 N  N     . LYS A 1 2879 ? 145.499 82.069  83.274  1.00 25.14  ? 2879 LYS A N     1 
ATOM   11287 C  CA    . LYS A 1 2879 ? 145.180 81.516  84.586  1.00 26.83  ? 2879 LYS A CA    1 
ATOM   11288 C  C     . LYS A 1 2879 ? 144.663 82.593  85.533  1.00 25.53  ? 2879 LYS A C     1 
ATOM   11289 O  O     . LYS A 1 2879 ? 143.801 82.326  86.378  1.00 24.48  ? 2879 LYS A O     1 
ATOM   11290 C  CB    . LYS A 1 2879 ? 146.408 80.814  85.170  1.00 29.22  ? 2879 LYS A CB    1 
ATOM   11291 C  CG    . LYS A 1 2879 ? 147.557 81.742  85.529  1.00 39.85  ? 2879 LYS A CG    1 
ATOM   11292 C  CD    . LYS A 1 2879 ? 148.744 80.974  86.081  1.00 46.90  ? 2879 LYS A CD    1 
ATOM   11293 C  CE    . LYS A 1 2879 ? 149.901 81.908  86.397  1.00 55.29  ? 2879 LYS A CE    1 
ATOM   11294 N  NZ    . LYS A 1 2879 ? 149.575 82.828  87.521  1.00 50.52  ? 2879 LYS A NZ    1 
ATOM   11295 N  N     . ASP A 1 2880 ? 145.171 83.815  85.405  1.00 22.59  ? 2880 ASP A N     1 
ATOM   11296 C  CA    . ASP A 1 2880 ? 144.816 84.900  86.306  1.00 20.01  ? 2880 ASP A CA    1 
ATOM   11297 C  C     . ASP A 1 2880 ? 143.757 85.808  85.687  1.00 15.63  ? 2880 ASP A C     1 
ATOM   11298 O  O     . ASP A 1 2880 ? 143.580 85.865  84.468  1.00 14.67  ? 2880 ASP A O     1 
ATOM   11299 C  CB    . ASP A 1 2880 ? 146.053 85.719  86.674  1.00 25.96  ? 2880 ASP A CB    1 
ATOM   11300 C  CG    . ASP A 1 2880 ? 147.101 84.898  87.395  1.00 33.67  ? 2880 ASP A CG    1 
ATOM   11301 O  OD1   . ASP A 1 2880 ? 146.758 83.809  87.901  1.00 32.17  ? 2880 ASP A OD1   1 
ATOM   11302 O  OD2   . ASP A 1 2880 ? 148.267 85.341  87.456  1.00 39.10  ? 2880 ASP A OD2   1 
ATOM   11303 N  N     . TYR A 1 2881 ? 143.051 86.524  86.558  1.00 15.57  ? 2881 TYR A N     1 
ATOM   11304 C  CA    . TYR A 1 2881 ? 142.022 87.476  86.147  1.00 9.92   ? 2881 TYR A CA    1 
ATOM   11305 C  C     . TYR A 1 2881 ? 142.714 88.780  85.768  1.00 9.84   ? 2881 TYR A C     1 
ATOM   11306 O  O     . TYR A 1 2881 ? 142.996 89.623  86.622  1.00 14.14  ? 2881 TYR A O     1 
ATOM   11307 C  CB    . TYR A 1 2881 ? 141.008 87.666  87.269  1.00 11.55  ? 2881 TYR A CB    1 
ATOM   11308 C  CG    . TYR A 1 2881 ? 139.786 88.468  86.895  1.00 8.79   ? 2881 TYR A CG    1 
ATOM   11309 C  CD1   . TYR A 1 2881 ? 138.828 87.946  86.038  1.00 7.68   ? 2881 TYR A CD1   1 
ATOM   11310 C  CD2   . TYR A 1 2881 ? 139.569 89.732  87.428  1.00 6.35   ? 2881 TYR A CD2   1 
ATOM   11311 C  CE1   . TYR A 1 2881 ? 137.705 88.669  85.699  1.00 6.84   ? 2881 TYR A CE1   1 
ATOM   11312 C  CE2   . TYR A 1 2881 ? 138.444 90.461  87.100  1.00 6.58   ? 2881 TYR A CE2   1 
ATOM   11313 C  CZ    . TYR A 1 2881 ? 137.515 89.922  86.235  1.00 7.57   ? 2881 TYR A CZ    1 
ATOM   11314 O  OH    . TYR A 1 2881 ? 136.394 90.640  85.898  1.00 9.65   ? 2881 TYR A OH    1 
ATOM   11315 N  N     . ILE A 1 2882 ? 142.987 88.946  84.478  1.00 9.24   ? 2882 ILE A N     1 
ATOM   11316 C  CA    . ILE A 1 2882 ? 143.793 90.057  83.974  1.00 8.48   ? 2882 ILE A CA    1 
ATOM   11317 C  C     . ILE A 1 2882 ? 143.006 90.754  82.872  1.00 6.77   ? 2882 ILE A C     1 
ATOM   11318 O  O     . ILE A 1 2882 ? 142.022 90.204  82.354  1.00 8.86   ? 2882 ILE A O     1 
ATOM   11319 C  CB    . ILE A 1 2882 ? 145.168 89.572  83.454  1.00 9.90   ? 2882 ILE A CB    1 
ATOM   11320 C  CG1   . ILE A 1 2882 ? 144.994 88.662  82.238  1.00 8.01   ? 2882 ILE A CG1   1 
ATOM   11321 C  CG2   . ILE A 1 2882 ? 145.945 88.868  84.554  1.00 10.95  ? 2882 ILE A CG2   1 
ATOM   11322 C  CD1   . ILE A 1 2882 ? 146.299 88.279  81.579  1.00 10.10  ? 2882 ILE A CD1   1 
ATOM   11323 N  N     . PRO A 1 2883 ? 143.398 91.978  82.502  1.00 5.76   ? 2883 PRO A N     1 
ATOM   11324 C  CA    . PRO A 1 2883 ? 142.712 92.652  81.392  1.00 7.00   ? 2883 PRO A CA    1 
ATOM   11325 C  C     . PRO A 1 2883 ? 142.834 91.856  80.101  1.00 8.64   ? 2883 PRO A C     1 
ATOM   11326 O  O     . PRO A 1 2883 ? 143.862 91.233  79.825  1.00 8.28   ? 2883 PRO A O     1 
ATOM   11327 C  CB    . PRO A 1 2883 ? 143.431 94.003  81.298  1.00 7.73   ? 2883 PRO A CB    1 
ATOM   11328 C  CG    . PRO A 1 2883 ? 144.755 93.771  81.936  1.00 5.85   ? 2883 PRO A CG    1 
ATOM   11329 C  CD    . PRO A 1 2883 ? 144.474 92.821  83.055  1.00 5.67   ? 2883 PRO A CD    1 
ATOM   11330 N  N     . VAL A 1 2884 ? 141.765 91.879  79.309  1.00 9.48   ? 2884 VAL A N     1 
ATOM   11331 C  CA    . VAL A 1 2884 ? 141.648 91.059  78.111  1.00 8.65   ? 2884 VAL A CA    1 
ATOM   11332 C  C     . VAL A 1 2884 ? 141.238 91.938  76.936  1.00 10.32  ? 2884 VAL A C     1 
ATOM   11333 O  O     . VAL A 1 2884 ? 140.367 92.805  77.068  1.00 9.73   ? 2884 VAL A O     1 
ATOM   11334 C  CB    . VAL A 1 2884 ? 140.648 89.898  78.324  1.00 8.91   ? 2884 VAL A CB    1 
ATOM   11335 C  CG1   . VAL A 1 2884 ? 139.280 90.425  78.735  1.00 6.82   ? 2884 VAL A CG1   1 
ATOM   11336 C  CG2   . VAL A 1 2884 ? 140.544 89.040  77.074  1.00 8.82   ? 2884 VAL A CG2   1 
ATOM   11337 N  N     . ASP A 1 2885 ? 141.889 91.728  75.794  1.00 14.02  ? 2885 ASP A N     1 
ATOM   11338 C  CA    . ASP A 1 2885 ? 141.567 92.482  74.590  1.00 15.75  ? 2885 ASP A CA    1 
ATOM   11339 C  C     . ASP A 1 2885 ? 140.199 92.070  74.060  1.00 11.66  ? 2885 ASP A C     1 
ATOM   11340 O  O     . ASP A 1 2885 ? 139.813 90.900  74.130  1.00 10.74  ? 2885 ASP A O     1 
ATOM   11341 C  CB    . ASP A 1 2885 ? 142.639 92.257  73.522  1.00 19.37  ? 2885 ASP A CB    1 
ATOM   11342 C  CG    . ASP A 1 2885 ? 142.557 93.259  72.380  1.00 26.63  ? 2885 ASP A CG    1 
ATOM   11343 O  OD1   . ASP A 1 2885 ? 141.439 93.597  71.941  1.00 24.88  ? 2885 ASP A OD1   1 
ATOM   11344 O  OD2   . ASP A 1 2885 ? 143.625 93.711  71.918  1.00 44.83  ? 2885 ASP A OD2   1 
ATOM   11345 N  N     . GLN A 1 2886 ? 139.462 93.047  73.525  1.00 10.33  ? 2886 GLN A N     1 
ATOM   11346 C  CA    . GLN A 1 2886 ? 138.109 92.778  73.048  1.00 11.20  ? 2886 GLN A CA    1 
ATOM   11347 C  C     . GLN A 1 2886 ? 138.111 91.840  71.845  1.00 15.22  ? 2886 GLN A C     1 
ATOM   11348 O  O     . GLN A 1 2886 ? 137.238 90.973  71.732  1.00 13.86  ? 2886 GLN A O     1 
ATOM   11349 C  CB    . GLN A 1 2886 ? 137.398 94.087  72.710  1.00 11.36  ? 2886 GLN A CB    1 
ATOM   11350 C  CG    . GLN A 1 2886 ? 135.925 93.913  72.382  1.00 12.77  ? 2886 GLN A CG    1 
ATOM   11351 C  CD    . GLN A 1 2886 ? 135.206 95.231  72.189  1.00 17.06  ? 2886 GLN A CD    1 
ATOM   11352 O  OE1   . GLN A 1 2886 ? 135.555 96.018  71.310  1.00 20.07  ? 2886 GLN A OE1   1 
ATOM   11353 N  NE2   . GLN A 1 2886 ? 134.193 95.478  73.011  1.00 16.35  ? 2886 GLN A NE2   1 
ATOM   11354 N  N     . GLU A 1 2887 ? 139.072 91.998  70.932  1.00 16.64  ? 2887 GLU A N     1 
ATOM   11355 C  CA    . GLU A 1 2887 ? 139.109 91.141  69.749  1.00 15.41  ? 2887 GLU A CA    1 
ATOM   11356 C  C     . GLU A 1 2887 ? 139.507 89.712  70.104  1.00 14.92  ? 2887 GLU A C     1 
ATOM   11357 O  O     . GLU A 1 2887 ? 138.922 88.750  69.589  1.00 15.07  ? 2887 GLU A O     1 
ATOM   11358 C  CB    . GLU A 1 2887 ? 140.066 91.723  68.709  1.00 15.58  ? 2887 GLU A CB    1 
ATOM   11359 C  CG    . GLU A 1 2887 ? 139.617 93.054  68.128  1.00 19.55  ? 2887 GLU A CG    1 
ATOM   11360 C  CD    . GLU A 1 2887 ? 138.134 93.083  67.808  1.00 27.46  ? 2887 GLU A CD    1 
ATOM   11361 O  OE1   . GLU A 1 2887 ? 137.675 92.223  67.026  1.00 27.89  ? 2887 GLU A OE1   1 
ATOM   11362 O  OE2   . GLU A 1 2887 ? 137.428 93.966  68.337  1.00 20.51  ? 2887 GLU A OE2   1 
ATOM   11363 N  N     . GLU A 1 2888 ? 140.507 89.554  70.975  1.00 14.30  ? 2888 GLU A N     1 
ATOM   11364 C  CA    . GLU A 1 2888 ? 140.892 88.220  71.423  1.00 15.51  ? 2888 GLU A CA    1 
ATOM   11365 C  C     . GLU A 1 2888 ? 139.754 87.550  72.180  1.00 14.88  ? 2888 GLU A C     1 
ATOM   11366 O  O     . GLU A 1 2888 ? 139.496 86.352  72.003  1.00 16.25  ? 2888 GLU A O     1 
ATOM   11367 C  CB    . GLU A 1 2888 ? 142.145 88.304  72.293  1.00 16.03  ? 2888 GLU A CB    1 
ATOM   11368 C  CG    . GLU A 1 2888 ? 143.391 88.740  71.541  1.00 28.82  ? 2888 GLU A CG    1 
ATOM   11369 C  CD    . GLU A 1 2888 ? 144.609 88.832  72.437  1.00 46.26  ? 2888 GLU A CD    1 
ATOM   11370 O  OE1   . GLU A 1 2888 ? 144.457 88.677  73.666  1.00 47.17  ? 2888 GLU A OE1   1 
ATOM   11371 O  OE2   . GLU A 1 2888 ? 145.719 89.061  71.911  1.00 47.57  ? 2888 GLU A OE2   1 
ATOM   11372 N  N     . LEU A 1 2889 ? 139.057 88.313  73.025  1.00 11.17  ? 2889 LEU A N     1 
ATOM   11373 C  CA    . LEU A 1 2889 ? 137.895 87.775  73.721  1.00 9.99   ? 2889 LEU A CA    1 
ATOM   11374 C  C     . LEU A 1 2889 ? 136.804 87.378  72.738  1.00 11.47  ? 2889 LEU A C     1 
ATOM   11375 O  O     . LEU A 1 2889 ? 136.132 86.361  72.927  1.00 13.73  ? 2889 LEU A O     1 
ATOM   11376 C  CB    . LEU A 1 2889 ? 137.363 88.794  74.728  1.00 9.20   ? 2889 LEU A CB    1 
ATOM   11377 C  CG    . LEU A 1 2889 ? 136.151 88.360  75.555  1.00 7.75   ? 2889 LEU A CG    1 
ATOM   11378 C  CD1   . LEU A 1 2889 ? 136.562 87.394  76.655  1.00 6.39   ? 2889 LEU A CD1   1 
ATOM   11379 C  CD2   . LEU A 1 2889 ? 135.433 89.567  76.135  1.00 7.80   ? 2889 LEU A CD2   1 
ATOM   11380 N  N     . ARG A 1 2890 ? 136.607 88.173  71.684  1.00 11.94  ? 2890 ARG A N     1 
ATOM   11381 C  CA    . ARG A 1 2890 ? 135.610 87.835  70.675  1.00 12.35  ? 2890 ARG A CA    1 
ATOM   11382 C  C     . ARG A 1 2890 ? 135.954 86.525  69.979  1.00 13.81  ? 2890 ARG A C     1 
ATOM   11383 O  O     . ARG A 1 2890 ? 135.084 85.664  69.787  1.00 13.89  ? 2890 ARG A O     1 
ATOM   11384 C  CB    . ARG A 1 2890 ? 135.492 88.972  69.659  1.00 13.15  ? 2890 ARG A CB    1 
ATOM   11385 C  CG    . ARG A 1 2890 ? 134.196 88.974  68.868  1.00 13.27  ? 2890 ARG A CG    1 
ATOM   11386 C  CD    . ARG A 1 2890 ? 134.277 89.914  67.678  1.00 16.78  ? 2890 ARG A CD    1 
ATOM   11387 N  NE    . ARG A 1 2890 ? 134.739 91.241  68.065  1.00 22.52  ? 2890 ARG A NE    1 
ATOM   11388 C  CZ    . ARG A 1 2890 ? 133.943 92.227  68.457  1.00 22.77  ? 2890 ARG A CZ    1 
ATOM   11389 N  NH1   . ARG A 1 2890 ? 132.631 92.070  68.525  1.00 21.41  ? 2890 ARG A NH1   1 
ATOM   11390 N  NH2   . ARG A 1 2890 ? 134.477 93.398  68.789  1.00 17.43  ? 2890 ARG A NH2   1 
ATOM   11391 N  N     . ASP A 1 2891 ? 137.223 86.354  69.602  1.00 12.56  ? 2891 ASP A N     1 
ATOM   11392 C  CA    . ASP A 1 2891 ? 137.649 85.103  68.981  1.00 15.37  ? 2891 ASP A CA    1 
ATOM   11393 C  C     . ASP A 1 2891 ? 137.444 83.924  69.924  1.00 15.55  ? 2891 ASP A C     1 
ATOM   11394 O  O     . ASP A 1 2891 ? 136.944 82.866  69.515  1.00 18.54  ? 2891 ASP A O     1 
ATOM   11395 C  CB    . ASP A 1 2891 ? 139.114 85.199  68.557  1.00 19.60  ? 2891 ASP A CB    1 
ATOM   11396 C  CG    . ASP A 1 2891 ? 139.352 86.276  67.518  1.00 26.74  ? 2891 ASP A CG    1 
ATOM   11397 O  OD1   . ASP A 1 2891 ? 138.409 86.599  66.768  1.00 27.53  ? 2891 ASP A OD1   1 
ATOM   11398 O  OD2   . ASP A 1 2891 ? 140.483 86.803  67.454  1.00 28.06  ? 2891 ASP A OD2   1 
ATOM   11399 N  N     . TYR A 1 2892 ? 137.817 84.092  71.195  1.00 12.35  ? 2892 TYR A N     1 
ATOM   11400 C  CA    . TYR A 1 2892 ? 137.658 83.013  72.165  1.00 9.82   ? 2892 TYR A CA    1 
ATOM   11401 C  C     . TYR A 1 2892 ? 136.190 82.657  72.366  1.00 9.34   ? 2892 TYR A C     1 
ATOM   11402 O  O     . TYR A 1 2892 ? 135.839 81.475  72.458  1.00 8.78   ? 2892 TYR A O     1 
ATOM   11403 C  CB    . TYR A 1 2892 ? 138.298 83.405  73.494  1.00 10.84  ? 2892 TYR A CB    1 
ATOM   11404 C  CG    . TYR A 1 2892 ? 138.147 82.361  74.575  1.00 10.17  ? 2892 TYR A CG    1 
ATOM   11405 C  CD1   . TYR A 1 2892 ? 138.983 81.254  74.619  1.00 9.46   ? 2892 TYR A CD1   1 
ATOM   11406 C  CD2   . TYR A 1 2892 ? 137.168 82.482  75.551  1.00 8.98   ? 2892 TYR A CD2   1 
ATOM   11407 C  CE1   . TYR A 1 2892 ? 138.848 80.297  75.605  1.00 9.23   ? 2892 TYR A CE1   1 
ATOM   11408 C  CE2   . TYR A 1 2892 ? 137.024 81.530  76.538  1.00 8.28   ? 2892 TYR A CE2   1 
ATOM   11409 C  CZ    . TYR A 1 2892 ? 137.867 80.441  76.563  1.00 10.01  ? 2892 TYR A CZ    1 
ATOM   11410 O  OH    . TYR A 1 2892 ? 137.726 79.492  77.548  1.00 13.85  ? 2892 TYR A OH    1 
ATOM   11411 N  N     . VAL A 1 2893 ? 135.319 83.664  72.447  1.00 9.30   ? 2893 VAL A N     1 
ATOM   11412 C  CA    . VAL A 1 2893 ? 133.901 83.403  72.668  1.00 11.04  ? 2893 VAL A CA    1 
ATOM   11413 C  C     . VAL A 1 2893 ? 133.285 82.726  71.451  1.00 11.26  ? 2893 VAL A C     1 
ATOM   11414 O  O     . VAL A 1 2893 ? 132.430 81.846  71.589  1.00 10.94  ? 2893 VAL A O     1 
ATOM   11415 C  CB    . VAL A 1 2893 ? 133.166 84.704  73.042  1.00 9.77   ? 2893 VAL A CB    1 
ATOM   11416 C  CG1   . VAL A 1 2893 ? 131.665 84.475  73.096  1.00 9.62   ? 2893 VAL A CG1   1 
ATOM   11417 C  CG2   . VAL A 1 2893 ? 133.651 85.207  74.390  1.00 7.62   ? 2893 VAL A CG2   1 
ATOM   11418 N  N     . LYS A 1 2894 ? 133.709 83.108  70.243  1.00 12.23  ? 2894 LYS A N     1 
ATOM   11419 C  CA    . LYS A 1 2894 ? 133.242 82.392  69.058  1.00 12.01  ? 2894 LYS A CA    1 
ATOM   11420 C  C     . LYS A 1 2894 ? 133.685 80.933  69.085  1.00 12.31  ? 2894 LYS A C     1 
ATOM   11421 O  O     . LYS A 1 2894 ? 132.889 80.026  68.803  1.00 13.28  ? 2894 LYS A O     1 
ATOM   11422 C  CB    . LYS A 1 2894 ? 133.745 83.075  67.787  1.00 16.50  ? 2894 LYS A CB    1 
ATOM   11423 C  CG    . LYS A 1 2894 ? 133.111 84.423  67.503  1.00 22.03  ? 2894 LYS A CG    1 
ATOM   11424 C  CD    . LYS A 1 2894 ? 133.629 84.995  66.197  1.00 23.44  ? 2894 LYS A CD    1 
ATOM   11425 C  CE    . LYS A 1 2894 ? 133.017 86.352  65.897  1.00 25.83  ? 2894 LYS A CE    1 
ATOM   11426 N  NZ    . LYS A 1 2894 ? 133.541 86.917  64.623  1.00 36.22  ? 2894 LYS A NZ    1 
ATOM   11427 N  N     . ALA A 1 2895 ? 134.949 80.688  69.442  1.00 11.14  ? 2895 ALA A N     1 
ATOM   11428 C  CA    . ALA A 1 2895 ? 135.442 79.315  69.506  1.00 10.44  ? 2895 ALA A CA    1 
ATOM   11429 C  C     . ALA A 1 2895 ? 134.676 78.499  70.540  1.00 13.31  ? 2895 ALA A C     1 
ATOM   11430 O  O     . ALA A 1 2895 ? 134.355 77.328  70.306  1.00 14.03  ? 2895 ALA A O     1 
ATOM   11431 C  CB    . ALA A 1 2895 ? 136.938 79.307  69.815  1.00 11.64  ? 2895 ALA A CB    1 
ATOM   11432 N  N     . ARG A 1 2896 ? 134.376 79.101  71.693  1.00 13.61  ? 2896 ARG A N     1 
ATOM   11433 C  CA    . ARG A 1 2896 ? 133.650 78.382  72.736  1.00 10.73  ? 2896 ARG A CA    1 
ATOM   11434 C  C     . ARG A 1 2896 ? 132.195 78.149  72.348  1.00 7.95   ? 2896 ARG A C     1 
ATOM   11435 O  O     . ARG A 1 2896 ? 131.634 77.088  72.642  1.00 11.92  ? 2896 ARG A O     1 
ATOM   11436 C  CB    . ARG A 1 2896 ? 133.740 79.140  74.060  1.00 10.36  ? 2896 ARG A CB    1 
ATOM   11437 C  CG    . ARG A 1 2896 ? 135.149 79.250  74.617  1.00 7.93   ? 2896 ARG A CG    1 
ATOM   11438 C  CD    . ARG A 1 2896 ? 135.876 77.917  74.558  1.00 13.21  ? 2896 ARG A CD    1 
ATOM   11439 N  NE    . ARG A 1 2896 ? 135.251 76.908  75.405  1.00 16.46  ? 2896 ARG A NE    1 
ATOM   11440 C  CZ    . ARG A 1 2896 ? 135.431 75.601  75.268  1.00 16.08  ? 2896 ARG A CZ    1 
ATOM   11441 N  NH1   . ARG A 1 2896 ? 136.204 75.106  74.316  1.00 13.02  ? 2896 ARG A NH1   1 
ATOM   11442 N  NH2   . ARG A 1 2896 ? 134.819 74.771  76.107  1.00 15.13  ? 2896 ARG A NH2   1 
ATOM   11443 N  N     . LEU A 1 2897 ? 131.563 79.126  71.693  1.00 6.27   ? 2897 LEU A N     1 
ATOM   11444 C  CA    . LEU A 1 2897 ? 130.192 78.939  71.235  1.00 9.17   ? 2897 LEU A CA    1 
ATOM   11445 C  C     . LEU A 1 2897 ? 130.102 77.872  70.155  1.00 10.09  ? 2897 LEU A C     1 
ATOM   11446 O  O     . LEU A 1 2897 ? 129.068 77.210  70.031  1.00 9.78   ? 2897 LEU A O     1 
ATOM   11447 C  CB    . LEU A 1 2897 ? 129.613 80.257  70.724  1.00 7.61   ? 2897 LEU A CB    1 
ATOM   11448 C  CG    . LEU A 1 2897 ? 128.927 81.135  71.769  1.00 7.58   ? 2897 LEU A CG    1 
ATOM   11449 C  CD1   . LEU A 1 2897 ? 128.519 82.459  71.160  1.00 7.71   ? 2897 LEU A CD1   1 
ATOM   11450 C  CD2   . LEU A 1 2897 ? 127.716 80.423  72.349  1.00 5.56   ? 2897 LEU A CD2   1 
ATOM   11451 N  N     . LYS A 1 2898 ? 131.166 77.691  69.370  1.00 12.51  ? 2898 LYS A N     1 
ATOM   11452 C  CA    . LYS A 1 2898 ? 131.174 76.600  68.400  1.00 13.60  ? 2898 LYS A CA    1 
ATOM   11453 C  C     . LYS A 1 2898 ? 130.985 75.252  69.089  1.00 15.52  ? 2898 LYS A C     1 
ATOM   11454 O  O     . LYS A 1 2898 ? 130.186 74.421  68.640  1.00 18.85  ? 2898 LYS A O     1 
ATOM   11455 C  CB    . LYS A 1 2898 ? 132.477 76.620  67.601  1.00 18.91  ? 2898 LYS A CB    1 
ATOM   11456 C  CG    . LYS A 1 2898 ? 132.539 75.589  66.489  1.00 28.44  ? 2898 LYS A CG    1 
ATOM   11457 C  CD    . LYS A 1 2898 ? 133.822 75.721  65.687  1.00 34.22  ? 2898 LYS A CD    1 
ATOM   11458 C  CE    . LYS A 1 2898 ? 133.888 74.683  64.579  1.00 49.30  ? 2898 LYS A CE    1 
ATOM   11459 N  NZ    . LYS A 1 2898 ? 135.141 74.798  63.785  1.00 47.69  ? 2898 LYS A NZ    1 
ATOM   11460 N  N     . VAL A 1 2899 ? 131.707 75.022  70.187  1.00 14.27  ? 2899 VAL A N     1 
ATOM   11461 C  CA    . VAL A 1 2899 ? 131.540 73.796  70.962  1.00 14.90  ? 2899 VAL A CA    1 
ATOM   11462 C  C     . VAL A 1 2899 ? 130.193 73.788  71.679  1.00 15.30  ? 2899 VAL A C     1 
ATOM   11463 O  O     . VAL A 1 2899 ? 129.547 72.739  71.814  1.00 18.13  ? 2899 VAL A O     1 
ATOM   11464 C  CB    . VAL A 1 2899 ? 132.714 73.640  71.946  1.00 13.19  ? 2899 VAL A CB    1 
ATOM   11465 C  CG1   . VAL A 1 2899 ? 132.594 72.350  72.724  1.00 14.78  ? 2899 VAL A CG1   1 
ATOM   11466 C  CG2   . VAL A 1 2899 ? 134.038 73.696  71.201  1.00 13.93  ? 2899 VAL A CG2   1 
ATOM   11467 N  N     . PHE A 1 2900 ? 129.756 74.955  72.161  1.00 11.20  ? 2900 PHE A N     1 
ATOM   11468 C  CA    . PHE A 1 2900 ? 128.499 75.040  72.898  1.00 10.63  ? 2900 PHE A CA    1 
ATOM   11469 C  C     . PHE A 1 2900 ? 127.315 74.645  72.025  1.00 13.09  ? 2900 PHE A C     1 
ATOM   11470 O  O     . PHE A 1 2900 ? 126.355 74.033  72.508  1.00 13.65  ? 2900 PHE A O     1 
ATOM   11471 C  CB    . PHE A 1 2900 ? 128.313 76.453  73.452  1.00 7.98   ? 2900 PHE A CB    1 
ATOM   11472 C  CG    . PHE A 1 2900 ? 127.060 76.629  74.261  1.00 6.55   ? 2900 PHE A CG    1 
ATOM   11473 C  CD1   . PHE A 1 2900 ? 126.940 76.047  75.512  1.00 6.38   ? 2900 PHE A CD1   1 
ATOM   11474 C  CD2   . PHE A 1 2900 ? 126.004 77.381  73.774  1.00 5.55   ? 2900 PHE A CD2   1 
ATOM   11475 C  CE1   . PHE A 1 2900 ? 125.788 76.208  76.260  1.00 7.49   ? 2900 PHE A CE1   1 
ATOM   11476 C  CE2   . PHE A 1 2900 ? 124.851 77.546  74.517  1.00 6.80   ? 2900 PHE A CE2   1 
ATOM   11477 C  CZ    . PHE A 1 2900 ? 124.742 76.959  75.762  1.00 5.30   ? 2900 PHE A CZ    1 
ATOM   11478 N  N     . TYR A 1 2901 ? 127.362 74.994  70.738  1.00 12.52  ? 2901 TYR A N     1 
ATOM   11479 C  CA    . TYR A 1 2901 ? 126.278 74.630  69.833  1.00 14.75  ? 2901 TYR A CA    1 
ATOM   11480 C  C     . TYR A 1 2901 ? 126.144 73.118  69.710  1.00 19.62  ? 2901 TYR A C     1 
ATOM   11481 O  O     . TYR A 1 2901 ? 125.028 72.586  69.679  1.00 20.75  ? 2901 TYR A O     1 
ATOM   11482 C  CB    . TYR A 1 2901 ? 126.497 75.257  68.455  1.00 15.13  ? 2901 TYR A CB    1 
ATOM   11483 C  CG    . TYR A 1 2901 ? 126.542 76.767  68.458  1.00 17.17  ? 2901 TYR A CG    1 
ATOM   11484 C  CD1   . TYR A 1 2901 ? 125.840 77.502  69.404  1.00 10.61  ? 2901 TYR A CD1   1 
ATOM   11485 C  CD2   . TYR A 1 2901 ? 127.280 77.459  67.506  1.00 12.85  ? 2901 TYR A CD2   1 
ATOM   11486 C  CE1   . TYR A 1 2901 ? 125.879 78.882  69.408  1.00 10.69  ? 2901 TYR A CE1   1 
ATOM   11487 C  CE2   . TYR A 1 2901 ? 127.324 78.839  67.502  1.00 10.19  ? 2901 TYR A CE2   1 
ATOM   11488 C  CZ    . TYR A 1 2901 ? 126.622 79.546  68.455  1.00 11.79  ? 2901 TYR A CZ    1 
ATOM   11489 O  OH    . TYR A 1 2901 ? 126.662 80.921  68.453  1.00 13.78  ? 2901 TYR A OH    1 
ATOM   11490 N  N     . GLU A 1 2902 ? 127.270 72.406  69.640  1.00 23.95  ? 2902 GLU A N     1 
ATOM   11491 C  CA    . GLU A 1 2902 ? 127.223 70.967  69.425  1.00 23.21  ? 2902 GLU A CA    1 
ATOM   11492 C  C     . GLU A 1 2902 ? 127.052 70.170  70.713  1.00 23.53  ? 2902 GLU A C     1 
ATOM   11493 O  O     . GLU A 1 2902 ? 126.623 69.014  70.648  1.00 32.97  ? 2902 GLU A O     1 
ATOM   11494 C  CB    . GLU A 1 2902 ? 128.485 70.497  68.696  1.00 25.24  ? 2902 GLU A CB    1 
ATOM   11495 C  CG    . GLU A 1 2902 ? 129.768 70.660  69.489  1.00 29.92  ? 2902 GLU A CG    1 
ATOM   11496 C  CD    . GLU A 1 2902 ? 130.995 70.244  68.704  1.00 40.61  ? 2902 GLU A CD    1 
ATOM   11497 O  OE1   . GLU A 1 2902 ? 130.844 69.848  67.529  1.00 47.31  ? 2902 GLU A OE1   1 
ATOM   11498 O  OE2   . GLU A 1 2902 ? 132.111 70.313  69.261  1.00 37.60  ? 2902 GLU A OE2   1 
ATOM   11499 N  N     . GLU A 1 2903 ? 127.370 70.741  71.876  1.00 22.63  ? 2903 GLU A N     1 
ATOM   11500 C  CA    . GLU A 1 2903 ? 127.250 69.971  73.111  1.00 22.69  ? 2903 GLU A CA    1 
ATOM   11501 C  C     . GLU A 1 2903 ? 125.954 70.217  73.876  1.00 24.60  ? 2903 GLU A C     1 
ATOM   11502 O  O     . GLU A 1 2903 ? 125.328 69.254  74.327  1.00 32.36  ? 2903 GLU A O     1 
ATOM   11503 C  CB    . GLU A 1 2903 ? 128.441 70.238  74.038  1.00 25.92  ? 2903 GLU A CB    1 
ATOM   11504 C  CG    . GLU A 1 2903 ? 129.766 69.712  73.518  1.00 31.22  ? 2903 GLU A CG    1 
ATOM   11505 C  CD    . GLU A 1 2903 ? 130.916 70.001  74.463  1.00 38.59  ? 2903 GLU A CD    1 
ATOM   11506 O  OE1   . GLU A 1 2903 ? 130.701 70.716  75.464  1.00 31.97  ? 2903 GLU A OE1   1 
ATOM   11507 O  OE2   . GLU A 1 2903 ? 132.035 69.508  74.208  1.00 44.46  ? 2903 GLU A OE2   1 
ATOM   11508 N  N     . GLU A 1 2904 ? 125.523 71.468  74.044  1.00 23.25  ? 2904 GLU A N     1 
ATOM   11509 C  CA    . GLU A 1 2904 ? 124.359 71.763  74.874  1.00 21.27  ? 2904 GLU A CA    1 
ATOM   11510 C  C     . GLU A 1 2904 ? 123.170 72.286  74.077  1.00 22.89  ? 2904 GLU A C     1 
ATOM   11511 O  O     . GLU A 1 2904 ? 122.087 71.699  74.138  1.00 32.56  ? 2904 GLU A O     1 
ATOM   11512 C  CB    . GLU A 1 2904 ? 124.731 72.761  75.981  1.00 16.71  ? 2904 GLU A CB    1 
ATOM   11513 C  CG    . GLU A 1 2904 ? 125.663 72.202  77.044  1.00 21.11  ? 2904 GLU A CG    1 
ATOM   11514 C  CD    . GLU A 1 2904 ? 125.013 71.120  77.881  1.00 32.34  ? 2904 GLU A CD    1 
ATOM   11515 O  OE1   . GLU A 1 2904 ? 123.941 71.383  78.467  1.00 33.95  ? 2904 GLU A OE1   1 
ATOM   11516 O  OE2   . GLU A 1 2904 ? 125.572 70.006  77.955  1.00 35.37  ? 2904 GLU A OE2   1 
ATOM   11517 N  N     . LEU A 1 2905 ? 123.333 73.376  73.329  1.00 21.04  ? 2905 LEU A N     1 
ATOM   11518 C  CA    . LEU A 1 2905 ? 122.200 74.026  72.675  1.00 22.55  ? 2905 LEU A CA    1 
ATOM   11519 C  C     . LEU A 1 2905 ? 122.629 74.514  71.300  1.00 17.88  ? 2905 LEU A C     1 
ATOM   11520 O  O     . LEU A 1 2905 ? 123.508 75.374  71.191  1.00 20.82  ? 2905 LEU A O     1 
ATOM   11521 C  CB    . LEU A 1 2905 ? 121.668 75.185  73.519  1.00 23.37  ? 2905 LEU A CB    1 
ATOM   11522 C  CG    . LEU A 1 2905 ? 120.171 75.460  73.383  1.00 23.14  ? 2905 LEU A CG    1 
ATOM   11523 C  CD1   . LEU A 1 2905 ? 119.381 74.179  73.586  1.00 25.18  ? 2905 LEU A CD1   1 
ATOM   11524 C  CD2   . LEU A 1 2905 ? 119.724 76.532  74.363  1.00 20.29  ? 2905 LEU A CD2   1 
ATOM   11525 N  N     . ASP A 1 2906 ? 121.995 73.983  70.256  1.00 20.47  ? 2906 ASP A N     1 
ATOM   11526 C  CA    . ASP A 1 2906 ? 122.309 74.360  68.878  1.00 20.60  ? 2906 ASP A CA    1 
ATOM   11527 C  C     . ASP A 1 2906 ? 121.434 75.531  68.426  1.00 23.41  ? 2906 ASP A C     1 
ATOM   11528 O  O     . ASP A 1 2906 ? 120.622 75.430  67.507  1.00 24.04  ? 2906 ASP A O     1 
ATOM   11529 C  CB    . ASP A 1 2906 ? 122.149 73.158  67.955  1.00 21.36  ? 2906 ASP A CB    1 
ATOM   11530 C  CG    . ASP A 1 2906 ? 123.097 73.202  66.773  1.00 29.43  ? 2906 ASP A CG    1 
ATOM   11531 O  OD1   . ASP A 1 2906 ? 123.825 72.211  66.556  1.00 34.41  ? 2906 ASP A OD1   1 
ATOM   11532 O  OD2   . ASP A 1 2906 ? 123.115 74.227  66.061  1.00 28.75  ? 2906 ASP A OD2   1 
ATOM   11533 N  N     . VAL A 1 2907 ? 121.617 76.659  69.098  1.00 19.87  ? 2907 VAL A N     1 
ATOM   11534 C  CA    . VAL A 1 2907 ? 120.963 77.912  68.750  1.00 15.75  ? 2907 VAL A CA    1 
ATOM   11535 C  C     . VAL A 1 2907 ? 122.042 78.928  68.400  1.00 18.37  ? 2907 VAL A C     1 
ATOM   11536 O  O     . VAL A 1 2907 ? 122.679 79.503  69.283  1.00 20.17  ? 2907 VAL A O     1 
ATOM   11537 C  CB    . VAL A 1 2907 ? 120.069 78.424  69.894  1.00 17.27  ? 2907 VAL A CB    1 
ATOM   11538 C  CG1   . VAL A 1 2907 ? 119.304 79.660  69.453  1.00 14.71  ? 2907 VAL A CG1   1 
ATOM   11539 C  CG2   . VAL A 1 2907 ? 119.107 77.336  70.346  1.00 18.57  ? 2907 VAL A CG2   1 
ATOM   11540 N  N     . PRO A 1 2908 ? 122.290 79.162  67.111  1.00 19.80  ? 2908 PRO A N     1 
ATOM   11541 C  CA    . PRO A 1 2908 ? 123.328 80.125  66.722  1.00 16.25  ? 2908 PRO A CA    1 
ATOM   11542 C  C     . PRO A 1 2908 ? 123.019 81.520  67.243  1.00 17.95  ? 2908 PRO A C     1 
ATOM   11543 O  O     . PRO A 1 2908 ? 121.867 81.958  67.258  1.00 24.34  ? 2908 PRO A O     1 
ATOM   11544 C  CB    . PRO A 1 2908 ? 123.301 80.077  65.190  1.00 19.14  ? 2908 PRO A CB    1 
ATOM   11545 C  CG    . PRO A 1 2908 ? 122.673 78.759  64.859  1.00 20.47  ? 2908 PRO A CG    1 
ATOM   11546 C  CD    . PRO A 1 2908 ? 121.670 78.514  65.944  1.00 18.89  ? 2908 PRO A CD    1 
ATOM   11547 N  N     . LEU A 1 2909 ? 124.066 82.219  67.672  1.00 15.33  ? 2909 LEU A N     1 
ATOM   11548 C  CA    . LEU A 1 2909 ? 123.934 83.546  68.254  1.00 13.53  ? 2909 LEU A CA    1 
ATOM   11549 C  C     . LEU A 1 2909 ? 124.825 84.531  67.515  1.00 14.07  ? 2909 LEU A C     1 
ATOM   11550 O  O     . LEU A 1 2909 ? 125.981 84.226  67.205  1.00 15.88  ? 2909 LEU A O     1 
ATOM   11551 C  CB    . LEU A 1 2909 ? 124.296 83.542  69.744  1.00 14.08  ? 2909 LEU A CB    1 
ATOM   11552 C  CG    . LEU A 1 2909 ? 123.539 82.567  70.646  1.00 15.72  ? 2909 LEU A CG    1 
ATOM   11553 C  CD1   . LEU A 1 2909 ? 124.258 82.408  71.975  1.00 16.14  ? 2909 LEU A CD1   1 
ATOM   11554 C  CD2   . LEU A 1 2909 ? 122.108 83.033  70.859  1.00 12.56  ? 2909 LEU A CD2   1 
ATOM   11555 N  N     . VAL A 1 2910 ? 124.282 85.711  67.239  1.00 13.43  ? 2910 VAL A N     1 
ATOM   11556 C  CA    . VAL A 1 2910 ? 125.056 86.816  66.689  1.00 14.46  ? 2910 VAL A CA    1 
ATOM   11557 C  C     . VAL A 1 2910 ? 125.775 87.504  67.841  1.00 14.28  ? 2910 VAL A C     1 
ATOM   11558 O  O     . VAL A 1 2910 ? 125.159 87.834  68.862  1.00 18.20  ? 2910 VAL A O     1 
ATOM   11559 C  CB    . VAL A 1 2910 ? 124.152 87.799  65.927  1.00 16.22  ? 2910 VAL A CB    1 
ATOM   11560 C  CG1   . VAL A 1 2910 ? 124.961 88.983  65.431  1.00 13.47  ? 2910 VAL A CG1   1 
ATOM   11561 C  CG2   . VAL A 1 2910 ? 123.459 87.096  64.772  1.00 13.07  ? 2910 VAL A CG2   1 
ATOM   11562 N  N     . LEU A 1 2911 ? 127.077 87.716  67.683  1.00 14.27  ? 2911 LEU A N     1 
ATOM   11563 C  CA    . LEU A 1 2911 ? 127.937 88.111  68.791  1.00 17.81  ? 2911 LEU A CA    1 
ATOM   11564 C  C     . LEU A 1 2911 ? 128.316 89.582  68.664  1.00 18.34  ? 2911 LEU A C     1 
ATOM   11565 O  O     . LEU A 1 2911 ? 129.014 89.968  67.721  1.00 26.99  ? 2911 LEU A O     1 
ATOM   11566 C  CB    . LEU A 1 2911 ? 129.185 87.232  68.810  1.00 17.27  ? 2911 LEU A CB    1 
ATOM   11567 C  CG    . LEU A 1 2911 ? 128.990 85.885  69.503  1.00 26.60  ? 2911 LEU A CG    1 
ATOM   11568 C  CD1   . LEU A 1 2911 ? 130.315 85.185  69.715  1.00 20.99  ? 2911 LEU A CD1   1 
ATOM   11569 C  CD2   . LEU A 1 2911 ? 128.264 86.071  70.821  1.00 23.08  ? 2911 LEU A CD2   1 
ATOM   11570 N  N     . PHE A 1 2912 ? 127.877 90.396  69.620  1.00 12.70  ? 2912 PHE A N     1 
ATOM   11571 C  CA    . PHE A 1 2912 ? 128.217 91.811  69.643  1.00 12.41  ? 2912 PHE A CA    1 
ATOM   11572 C  C     . PHE A 1 2912 ? 128.833 92.175  70.989  1.00 11.70  ? 2912 PHE A C     1 
ATOM   11573 O  O     . PHE A 1 2912 ? 128.915 91.353  71.906  1.00 14.02  ? 2912 PHE A O     1 
ATOM   11574 C  CB    . PHE A 1 2912 ? 127.000 92.695  69.317  1.00 9.36   ? 2912 PHE A CB    1 
ATOM   11575 C  CG    . PHE A 1 2912 ? 125.776 92.406  70.143  1.00 11.88  ? 2912 PHE A CG    1 
ATOM   11576 C  CD1   . PHE A 1 2912 ? 124.889 91.412  69.762  1.00 10.86  ? 2912 PHE A CD1   1 
ATOM   11577 C  CD2   . PHE A 1 2912 ? 125.495 93.145  71.278  1.00 10.46  ? 2912 PHE A CD2   1 
ATOM   11578 C  CE1   . PHE A 1 2912 ? 123.754 91.152  70.506  1.00 6.91   ? 2912 PHE A CE1   1 
ATOM   11579 C  CE2   . PHE A 1 2912 ? 124.364 92.886  72.028  1.00 8.75   ? 2912 PHE A CE2   1 
ATOM   11580 C  CZ    . PHE A 1 2912 ? 123.491 91.891  71.640  1.00 8.21   ? 2912 PHE A CZ    1 
ATOM   11581 N  N     . ASN A 1 2913 ? 129.284 93.429  71.085  1.00 9.49   ? 2913 ASN A N     1 
ATOM   11582 C  CA    . ASN A 1 2913 ? 130.118 93.854  72.208  1.00 10.07  ? 2913 ASN A CA    1 
ATOM   11583 C  C     . ASN A 1 2913 ? 129.378 93.736  73.535  1.00 11.60  ? 2913 ASN A C     1 
ATOM   11584 O  O     . ASN A 1 2913 ? 129.947 93.284  74.541  1.00 11.92  ? 2913 ASN A O     1 
ATOM   11585 C  CB    . ASN A 1 2913 ? 130.583 95.292  71.984  1.00 12.67  ? 2913 ASN A CB    1 
ATOM   11586 C  CG    . ASN A 1 2913 ? 131.693 95.393  70.956  1.00 14.71  ? 2913 ASN A CG    1 
ATOM   11587 O  OD1   . ASN A 1 2913 ? 132.206 94.382  70.478  1.00 14.75  ? 2913 ASN A OD1   1 
ATOM   11588 N  ND2   . ASN A 1 2913 ? 132.065 96.619  70.608  1.00 13.73  ? 2913 ASN A ND2   1 
ATOM   11589 N  N     . GLU A 1 2914 ? 128.108 94.150  73.559  1.00 10.97  ? 2914 GLU A N     1 
ATOM   11590 C  CA    . GLU A 1 2914 ? 127.321 94.045  74.780  1.00 11.58  ? 2914 GLU A CA    1 
ATOM   11591 C  C     . GLU A 1 2914 ? 127.201 92.600  75.241  1.00 10.10  ? 2914 GLU A C     1 
ATOM   11592 O  O     . GLU A 1 2914 ? 127.185 92.339  76.445  1.00 11.13  ? 2914 GLU A O     1 
ATOM   11593 C  CB    . GLU A 1 2914 ? 125.939 94.660  74.570  1.00 12.43  ? 2914 GLU A CB    1 
ATOM   11594 C  CG    . GLU A 1 2914 ? 125.961 96.164  74.359  1.00 20.40  ? 2914 GLU A CG    1 
ATOM   11595 C  CD    . GLU A 1 2914 ? 124.580 96.745  74.134  1.00 32.62  ? 2914 GLU A CD    1 
ATOM   11596 O  OE1   . GLU A 1 2914 ? 123.613 95.963  74.017  1.00 27.37  ? 2914 GLU A OE1   1 
ATOM   11597 O  OE2   . GLU A 1 2914 ? 124.461 97.987  74.073  1.00 36.88  ? 2914 GLU A OE2   1 
ATOM   11598 N  N     . VAL A 1 2915 ? 127.134 91.650  74.304  1.00 7.44   ? 2915 VAL A N     1 
ATOM   11599 C  CA    . VAL A 1 2915 ? 127.103 90.239  74.679  1.00 8.08   ? 2915 VAL A CA    1 
ATOM   11600 C  C     . VAL A 1 2915 ? 128.393 89.842  75.386  1.00 5.56   ? 2915 VAL A C     1 
ATOM   11601 O  O     . VAL A 1 2915 ? 128.369 89.111  76.382  1.00 6.44   ? 2915 VAL A O     1 
ATOM   11602 C  CB    . VAL A 1 2915 ? 126.839 89.358  73.445  1.00 9.82   ? 2915 VAL A CB    1 
ATOM   11603 C  CG1   . VAL A 1 2915 ? 127.243 87.921  73.721  1.00 8.36   ? 2915 VAL A CG1   1 
ATOM   11604 C  CG2   . VAL A 1 2915 ? 125.379 89.416  73.064  1.00 7.94   ? 2915 VAL A CG2   1 
ATOM   11605 N  N     . LEU A 1 2916 ? 129.538 90.303  74.878  1.00 6.05   ? 2916 LEU A N     1 
ATOM   11606 C  CA    . LEU A 1 2916 ? 130.810 89.989  75.521  1.00 6.88   ? 2916 LEU A CA    1 
ATOM   11607 C  C     . LEU A 1 2916 ? 130.872 90.562  76.931  1.00 6.70   ? 2916 LEU A C     1 
ATOM   11608 O  O     . LEU A 1 2916 ? 131.280 89.873  77.879  1.00 8.30   ? 2916 LEU A O     1 
ATOM   11609 C  CB    . LEU A 1 2916 ? 131.966 90.522  74.675  1.00 6.77   ? 2916 LEU A CB    1 
ATOM   11610 C  CG    . LEU A 1 2916 ? 132.079 89.952  73.263  1.00 8.32   ? 2916 LEU A CG    1 
ATOM   11611 C  CD1   . LEU A 1 2916 ? 133.232 90.598  72.513  1.00 9.73   ? 2916 LEU A CD1   1 
ATOM   11612 C  CD2   . LEU A 1 2916 ? 132.250 88.448  73.330  1.00 8.31   ? 2916 LEU A CD2   1 
ATOM   11613 N  N     . ASP A 1 2917 ? 130.456 91.820  77.095  1.00 5.74   ? 2917 ASP A N     1 
ATOM   11614 C  CA    . ASP A 1 2917 ? 130.453 92.407  78.432  1.00 6.82   ? 2917 ASP A CA    1 
ATOM   11615 C  C     . ASP A 1 2917 ? 129.500 91.653  79.356  1.00 4.88   ? 2917 ASP A C     1 
ATOM   11616 O  O     . ASP A 1 2917 ? 129.822 91.397  80.524  1.00 3.68   ? 2917 ASP A O     1 
ATOM   11617 C  CB    . ASP A 1 2917 ? 130.082 93.887  78.356  1.00 10.56  ? 2917 ASP A CB    1 
ATOM   11618 C  CG    . ASP A 1 2917 ? 130.600 94.677  79.540  1.00 18.33  ? 2917 ASP A CG    1 
ATOM   11619 O  OD1   . ASP A 1 2917 ? 130.031 94.543  80.642  1.00 14.49  ? 2917 ASP A OD1   1 
ATOM   11620 O  OD2   . ASP A 1 2917 ? 131.578 95.435  79.370  1.00 19.84  ? 2917 ASP A OD2   1 
ATOM   11621 N  N     . HIS A 1 2918 ? 128.330 91.271  78.838  1.00 4.10   ? 2918 HIS A N     1 
ATOM   11622 C  CA    . HIS A 1 2918 ? 127.338 90.569  79.644  1.00 4.72   ? 2918 HIS A CA    1 
ATOM   11623 C  C     . HIS A 1 2918 ? 127.845 89.203  80.086  1.00 3.84   ? 2918 HIS A C     1 
ATOM   11624 O  O     . HIS A 1 2918 ? 127.643 88.806  81.239  1.00 4.44   ? 2918 HIS A O     1 
ATOM   11625 C  CB    . HIS A 1 2918 ? 126.039 90.425  78.854  1.00 5.93   ? 2918 HIS A CB    1 
ATOM   11626 C  CG    . HIS A 1 2918 ? 125.301 91.712  78.664  1.00 8.00   ? 2918 HIS A CG    1 
ATOM   11627 N  ND1   . HIS A 1 2918 ? 125.633 92.867  79.339  1.00 10.80  ? 2918 HIS A ND1   1 
ATOM   11628 C  CD2   . HIS A 1 2918 ? 124.253 92.031  77.868  1.00 8.39   ? 2918 HIS A CD2   1 
ATOM   11629 C  CE1   . HIS A 1 2918 ? 124.820 93.840  78.970  1.00 12.49  ? 2918 HIS A CE1   1 
ATOM   11630 N  NE2   . HIS A 1 2918 ? 123.972 93.359  78.079  1.00 13.22  ? 2918 HIS A NE2   1 
ATOM   11631 N  N     . VAL A 1 2919 ? 128.493 88.462  79.184  1.00 3.06   ? 2919 VAL A N     1 
ATOM   11632 C  CA    . VAL A 1 2919 ? 128.997 87.146  79.562  1.00 3.76   ? 2919 VAL A CA    1 
ATOM   11633 C  C     . VAL A 1 2919 ? 130.150 87.281  80.548  1.00 3.76   ? 2919 VAL A C     1 
ATOM   11634 O  O     . VAL A 1 2919 ? 130.295 86.448  81.449  1.00 4.25   ? 2919 VAL A O     1 
ATOM   11635 C  CB    . VAL A 1 2919 ? 129.388 86.307  78.327  1.00 3.39   ? 2919 VAL A CB    1 
ATOM   11636 C  CG1   . VAL A 1 2919 ? 128.179 86.083  77.429  1.00 2.86   ? 2919 VAL A CG1   1 
ATOM   11637 C  CG2   . VAL A 1 2919 ? 130.530 86.937  77.553  1.00 3.68   ? 2919 VAL A CG2   1 
ATOM   11638 N  N     . LEU A 1 2920 ? 130.973 88.329  80.420  1.00 3.90   ? 2920 LEU A N     1 
ATOM   11639 C  CA    . LEU A 1 2920 ? 131.996 88.569  81.436  1.00 3.52   ? 2920 LEU A CA    1 
ATOM   11640 C  C     . LEU A 1 2920 ? 131.368 88.827  82.803  1.00 3.09   ? 2920 LEU A C     1 
ATOM   11641 O  O     . LEU A 1 2920 ? 131.830 88.294  83.821  1.00 2.72   ? 2920 LEU A O     1 
ATOM   11642 C  CB    . LEU A 1 2920 ? 132.888 89.739  81.022  1.00 3.68   ? 2920 LEU A CB    1 
ATOM   11643 C  CG    . LEU A 1 2920 ? 133.904 89.464  79.912  1.00 6.44   ? 2920 LEU A CG    1 
ATOM   11644 C  CD1   . LEU A 1 2920 ? 134.788 90.677  79.676  1.00 7.64   ? 2920 LEU A CD1   1 
ATOM   11645 C  CD2   . LEU A 1 2920 ? 134.746 88.242  80.245  1.00 3.86   ? 2920 LEU A CD2   1 
ATOM   11646 N  N     . ARG A 1 2921 ? 130.305 89.637  82.845  1.00 3.12   ? 2921 ARG A N     1 
ATOM   11647 C  CA    . ARG A 1 2921 ? 129.630 89.909  84.114  1.00 4.13   ? 2921 ARG A CA    1 
ATOM   11648 C  C     . ARG A 1 2921 ? 129.025 88.639  84.708  1.00 3.83   ? 2921 ARG A C     1 
ATOM   11649 O  O     . ARG A 1 2921 ? 129.133 88.389  85.919  1.00 6.01   ? 2921 ARG A O     1 
ATOM   11650 C  CB    . ARG A 1 2921 ? 128.548 90.968  83.910  1.00 4.59   ? 2921 ARG A CB    1 
ATOM   11651 C  CG    . ARG A 1 2921 ? 129.058 92.313  83.420  1.00 4.03   ? 2921 ARG A CG    1 
ATOM   11652 C  CD    . ARG A 1 2921 ? 127.897 93.199  83.007  1.00 5.00   ? 2921 ARG A CD    1 
ATOM   11653 N  NE    . ARG A 1 2921 ? 128.323 94.411  82.320  1.00 7.26   ? 2921 ARG A NE    1 
ATOM   11654 C  CZ    . ARG A 1 2921 ? 127.502 95.379  81.938  1.00 10.41  ? 2921 ARG A CZ    1 
ATOM   11655 N  NH1   . ARG A 1 2921 ? 126.200 95.309  82.161  1.00 7.56   ? 2921 ARG A NH1   1 
ATOM   11656 N  NH2   . ARG A 1 2921 ? 127.999 96.444  81.315  1.00 10.55  ? 2921 ARG A NH2   1 
ATOM   11657 N  N     . ILE A 1 2922 ? 128.380 87.825  83.869  1.00 3.20   ? 2922 ILE A N     1 
ATOM   11658 C  CA    . ILE A 1 2922 ? 127.761 86.594  84.350  1.00 3.97   ? 2922 ILE A CA    1 
ATOM   11659 C  C     . ILE A 1 2922 ? 128.823 85.627  84.861  1.00 4.33   ? 2922 ILE A C     1 
ATOM   11660 O  O     . ILE A 1 2922 ? 128.619 84.940  85.868  1.00 4.34   ? 2922 ILE A O     1 
ATOM   11661 C  CB    . ILE A 1 2922 ? 126.891 85.963  83.246  1.00 2.99   ? 2922 ILE A CB    1 
ATOM   11662 C  CG1   . ILE A 1 2922 ? 125.749 86.905  82.864  1.00 3.41   ? 2922 ILE A CG1   1 
ATOM   11663 C  CG2   . ILE A 1 2922 ? 126.317 84.638  83.708  1.00 2.61   ? 2922 ILE A CG2   1 
ATOM   11664 C  CD1   . ILE A 1 2922 ? 124.960 86.456  81.654  1.00 3.04   ? 2922 ILE A CD1   1 
ATOM   11665 N  N     . ASP A 1 2923 ? 129.971 85.557  84.180  1.00 4.06   ? 2923 ASP A N     1 
ATOM   11666 C  CA    . ASP A 1 2923 ? 131.075 84.739  84.670  1.00 5.24   ? 2923 ASP A CA    1 
ATOM   11667 C  C     . ASP A 1 2923 ? 131.577 85.229  86.022  1.00 5.09   ? 2923 ASP A C     1 
ATOM   11668 O  O     . ASP A 1 2923 ? 131.829 84.417  86.926  1.00 5.77   ? 2923 ASP A O     1 
ATOM   11669 C  CB    . ASP A 1 2923 ? 132.211 84.731  83.647  1.00 4.15   ? 2923 ASP A CB    1 
ATOM   11670 C  CG    . ASP A 1 2923 ? 133.379 83.869  84.077  1.00 8.57   ? 2923 ASP A CG    1 
ATOM   11671 O  OD1   . ASP A 1 2923 ? 133.223 82.632  84.123  1.00 10.36  ? 2923 ASP A OD1   1 
ATOM   11672 O  OD2   . ASP A 1 2923 ? 134.457 84.428  84.369  1.00 12.04  ? 2923 ASP A OD2   1 
ATOM   11673 N  N     . ARG A 1 2924 ? 131.717 86.548  86.181  1.00 5.30   ? 2924 ARG A N     1 
ATOM   11674 C  CA    . ARG A 1 2924 ? 132.123 87.096  87.471  1.00 4.81   ? 2924 ARG A CA    1 
ATOM   11675 C  C     . ARG A 1 2924 ? 131.169 86.664  88.574  1.00 5.15   ? 2924 ARG A C     1 
ATOM   11676 O  O     . ARG A 1 2924 ? 131.604 86.244  89.653  1.00 7.67   ? 2924 ARG A O     1 
ATOM   11677 C  CB    . ARG A 1 2924 ? 132.188 88.620  87.410  1.00 4.34   ? 2924 ARG A CB    1 
ATOM   11678 C  CG    . ARG A 1 2924 ? 133.410 89.180  86.723  1.00 7.43   ? 2924 ARG A CG    1 
ATOM   11679 C  CD    . ARG A 1 2924 ? 133.333 90.693  86.681  1.00 6.55   ? 2924 ARG A CD    1 
ATOM   11680 N  NE    . ARG A 1 2924 ? 132.852 91.231  87.949  1.00 11.50  ? 2924 ARG A NE    1 
ATOM   11681 C  CZ    . ARG A 1 2924 ? 133.571 91.992  88.762  1.00 12.68  ? 2924 ARG A CZ    1 
ATOM   11682 N  NH1   . ARG A 1 2924 ? 134.821 92.318  88.480  1.00 11.79  ? 2924 ARG A NH1   1 
ATOM   11683 N  NH2   . ARG A 1 2924 ? 133.023 92.431  89.891  1.00 12.59  ? 2924 ARG A NH2   1 
ATOM   11684 N  N     . ILE A 1 2925 ? 129.863 86.757  88.322  1.00 5.13   ? 2925 ILE A N     1 
ATOM   11685 C  CA    . ILE A 1 2925 ? 128.901 86.395  89.360  1.00 6.00   ? 2925 ILE A CA    1 
ATOM   11686 C  C     . ILE A 1 2925 ? 128.923 84.892  89.628  1.00 5.68   ? 2925 ILE A C     1 
ATOM   11687 O  O     . ILE A 1 2925 ? 128.799 84.456  90.779  1.00 5.46   ? 2925 ILE A O     1 
ATOM   11688 C  CB    . ILE A 1 2925 ? 127.492 86.892  88.995  1.00 7.59   ? 2925 ILE A CB    1 
ATOM   11689 C  CG1   . ILE A 1 2925 ? 127.541 88.381  88.659  1.00 5.69   ? 2925 ILE A CG1   1 
ATOM   11690 C  CG2   . ILE A 1 2925 ? 126.527 86.638  90.141  1.00 2.84   ? 2925 ILE A CG2   1 
ATOM   11691 C  CD1   . ILE A 1 2925 ? 128.182 89.227  89.736  1.00 5.15   ? 2925 ILE A CD1   1 
ATOM   11692 N  N     . PHE A 1 2926 ? 129.083 84.075  88.584  1.00 6.92   ? 2926 PHE A N     1 
ATOM   11693 C  CA    . PHE A 1 2926 ? 129.158 82.632  88.785  1.00 5.43   ? 2926 PHE A CA    1 
ATOM   11694 C  C     . PHE A 1 2926 ? 130.420 82.191  89.514  1.00 7.56   ? 2926 PHE A C     1 
ATOM   11695 O  O     . PHE A 1 2926 ? 130.431 81.090  90.073  1.00 9.50   ? 2926 PHE A O     1 
ATOM   11696 C  CB    . PHE A 1 2926 ? 129.062 81.890  87.449  1.00 4.72   ? 2926 PHE A CB    1 
ATOM   11697 C  CG    . PHE A 1 2926 ? 127.672 81.814  86.888  1.00 5.98   ? 2926 PHE A CG    1 
ATOM   11698 C  CD1   . PHE A 1 2926 ? 126.571 82.086  87.683  1.00 3.78   ? 2926 PHE A CD1   1 
ATOM   11699 C  CD2   . PHE A 1 2926 ? 127.465 81.448  85.568  1.00 3.32   ? 2926 PHE A CD2   1 
ATOM   11700 C  CE1   . PHE A 1 2926 ? 125.293 82.007  87.167  1.00 3.72   ? 2926 PHE A CE1   1 
ATOM   11701 C  CE2   . PHE A 1 2926 ? 126.190 81.368  85.048  1.00 2.55   ? 2926 PHE A CE2   1 
ATOM   11702 C  CZ    . PHE A 1 2926 ? 125.102 81.648  85.848  1.00 2.58   ? 2926 PHE A CZ    1 
ATOM   11703 N  N     . ARG A 1 2927 ? 131.478 83.003  89.525  1.00 9.97   ? 2927 ARG A N     1 
ATOM   11704 C  CA    . ARG A 1 2927 ? 132.678 82.669  90.284  1.00 10.18  ? 2927 ARG A CA    1 
ATOM   11705 C  C     . ARG A 1 2927 ? 132.663 83.218  91.708  1.00 12.84  ? 2927 ARG A C     1 
ATOM   11706 O  O     . ARG A 1 2927 ? 133.733 83.418  92.290  1.00 19.98  ? 2927 ARG A O     1 
ATOM   11707 C  CB    . ARG A 1 2927 ? 133.930 83.161  89.556  1.00 10.58  ? 2927 ARG A CB    1 
ATOM   11708 C  CG    . ARG A 1 2927 ? 134.148 82.528  88.199  1.00 11.40  ? 2927 ARG A CG    1 
ATOM   11709 C  CD    . ARG A 1 2927 ? 135.462 82.973  87.595  1.00 12.04  ? 2927 ARG A CD    1 
ATOM   11710 N  NE    . ARG A 1 2927 ? 135.354 84.307  87.021  1.00 12.77  ? 2927 ARG A NE    1 
ATOM   11711 C  CZ    . ARG A 1 2927 ? 135.939 85.385  87.522  1.00 15.17  ? 2927 ARG A CZ    1 
ATOM   11712 N  NH1   . ARG A 1 2927 ? 136.696 85.320  88.605  1.00 14.74  ? 2927 ARG A NH1   1 
ATOM   11713 N  NH2   . ARG A 1 2927 ? 135.756 86.559  86.925  1.00 10.53  ? 2927 ARG A NH2   1 
ATOM   11714 N  N     . GLN A 1 2928 ? 131.485 83.462  92.283  1.00 13.98  ? 2928 GLN A N     1 
ATOM   11715 C  CA    . GLN A 1 2928 ? 131.398 83.952  93.649  1.00 12.16  ? 2928 GLN A CA    1 
ATOM   11716 C  C     . GLN A 1 2928 ? 130.462 83.080  94.477  1.00 12.55  ? 2928 GLN A C     1 
ATOM   11717 O  O     . GLN A 1 2928 ? 129.415 82.656  93.980  1.00 11.07  ? 2928 GLN A O     1 
ATOM   11718 C  CB    . GLN A 1 2928 ? 130.898 85.404  93.684  1.00 12.20  ? 2928 GLN A CB    1 
ATOM   11719 C  CG    . GLN A 1 2928 ? 131.845 86.406  93.047  1.00 19.45  ? 2928 GLN A CG    1 
ATOM   11720 C  CD    . GLN A 1 2928 ? 133.179 86.477  93.761  1.00 31.02  ? 2928 GLN A CD    1 
ATOM   11721 O  OE1   . GLN A 1 2928 ? 134.202 86.036  93.239  1.00 29.39  ? 2928 GLN A OE1   1 
ATOM   11722 N  NE2   . GLN A 1 2928 ? 133.175 87.033  94.967  1.00 30.79  ? 2928 GLN A NE2   1 
ATOM   11723 N  N     . PRO A 1 2929 ? 130.803 82.800  95.736  1.00 18.52  ? 2929 PRO A N     1 
ATOM   11724 C  CA    . PRO A 1 2929 ? 129.885 82.040  96.593  1.00 14.23  ? 2929 PRO A CA    1 
ATOM   11725 C  C     . PRO A 1 2929 ? 128.580 82.795  96.802  1.00 11.09  ? 2929 PRO A C     1 
ATOM   11726 O  O     . PRO A 1 2929 ? 128.569 84.016  96.972  1.00 12.86  ? 2929 PRO A O     1 
ATOM   11727 C  CB    . PRO A 1 2929 ? 130.668 81.885  97.902  1.00 13.32  ? 2929 PRO A CB    1 
ATOM   11728 C  CG    . PRO A 1 2929 ? 131.637 83.025  97.894  1.00 16.16  ? 2929 PRO A CG    1 
ATOM   11729 C  CD    . PRO A 1 2929 ? 132.025 83.200  96.454  1.00 17.40  ? 2929 PRO A CD    1 
ATOM   11730 N  N     . GLN A 1 2930 ? 127.474 82.046  96.802  1.00 9.58   ? 2930 GLN A N     1 
ATOM   11731 C  CA    . GLN A 1 2930 ? 126.130 82.628  96.809  1.00 8.77   ? 2930 GLN A CA    1 
ATOM   11732 C  C     . GLN A 1 2930 ? 125.979 83.660  95.696  1.00 8.68   ? 2930 GLN A C     1 
ATOM   11733 O  O     . GLN A 1 2930 ? 125.376 84.720  95.876  1.00 9.31   ? 2930 GLN A O     1 
ATOM   11734 C  CB    . GLN A 1 2930 ? 125.789 83.237  98.171  1.00 9.20   ? 2930 GLN A CB    1 
ATOM   11735 C  CG    . GLN A 1 2930 ? 125.063 82.291  99.110  1.00 12.89  ? 2930 GLN A CG    1 
ATOM   11736 C  CD    . GLN A 1 2930 ? 124.681 82.948  100.422 1.00 15.35  ? 2930 GLN A CD    1 
ATOM   11737 O  OE1   . GLN A 1 2930 ? 125.540 83.420  101.166 1.00 22.00  ? 2930 GLN A OE1   1 
ATOM   11738 N  NE2   . GLN A 1 2930 ? 123.386 82.981  100.713 1.00 11.58  ? 2930 GLN A NE2   1 
ATOM   11739 N  N     . GLY A 1 2931 ? 126.535 83.345  94.529  1.00 7.21   ? 2931 GLY A N     1 
ATOM   11740 C  CA    . GLY A 1 2931 ? 126.490 84.265  93.414  1.00 3.65   ? 2931 GLY A CA    1 
ATOM   11741 C  C     . GLY A 1 2931 ? 125.169 84.184  92.684  1.00 3.17   ? 2931 GLY A C     1 
ATOM   11742 O  O     . GLY A 1 2931 ? 124.930 83.258  91.904  1.00 2.95   ? 2931 GLY A O     1 
ATOM   11743 N  N     . HIS A 1 2932 ? 124.302 85.158  92.933  1.00 3.06   ? 2932 HIS A N     1 
ATOM   11744 C  CA    . HIS A 1 2932 ? 122.956 85.181  92.389  1.00 2.35   ? 2932 HIS A CA    1 
ATOM   11745 C  C     . HIS A 1 2932 ? 122.814 86.357  91.434  1.00 1.96   ? 2932 HIS A C     1 
ATOM   11746 O  O     . HIS A 1 2932 ? 123.356 87.437  91.681  1.00 2.26   ? 2932 HIS A O     1 
ATOM   11747 C  CB    . HIS A 1 2932 ? 121.924 85.277  93.513  1.00 2.85   ? 2932 HIS A CB    1 
ATOM   11748 C  CG    . HIS A 1 2932 ? 122.030 84.173  94.518  1.00 4.92   ? 2932 HIS A CG    1 
ATOM   11749 N  ND1   . HIS A 1 2932 ? 122.285 82.867  94.162  1.00 4.51   ? 2932 HIS A ND1   1 
ATOM   11750 C  CD2   . HIS A 1 2932 ? 121.939 84.184  95.869  1.00 6.43   ? 2932 HIS A CD2   1 
ATOM   11751 C  CE1   . HIS A 1 2932 ? 122.334 82.118  95.249  1.00 4.00   ? 2932 HIS A CE1   1 
ATOM   11752 N  NE2   . HIS A 1 2932 ? 122.126 82.893  96.299  1.00 5.97   ? 2932 HIS A NE2   1 
ATOM   11753 N  N     . LEU A 1 2933 ? 122.084 86.144  90.344  1.00 2.36   ? 2933 LEU A N     1 
ATOM   11754 C  CA    . LEU A 1 2933 ? 121.944 87.135  89.287  1.00 2.24   ? 2933 LEU A CA    1 
ATOM   11755 C  C     . LEU A 1 2933 ? 120.492 87.561  89.152  1.00 2.32   ? 2933 LEU A C     1 
ATOM   11756 O  O     . LEU A 1 2933 ? 119.584 86.726  89.219  1.00 2.88   ? 2933 LEU A O     1 
ATOM   11757 C  CB    . LEU A 1 2933 ? 122.452 86.590  87.951  1.00 2.48   ? 2933 LEU A CB    1 
ATOM   11758 C  CG    . LEU A 1 2933 ? 123.923 86.859  87.648  1.00 4.08   ? 2933 LEU A CG    1 
ATOM   11759 C  CD1   . LEU A 1 2933 ? 124.343 86.154  86.374  1.00 7.46   ? 2933 LEU A CD1   1 
ATOM   11760 C  CD2   . LEU A 1 2933 ? 124.154 88.354  87.539  1.00 3.71   ? 2933 LEU A CD2   1 
ATOM   11761 N  N     . LEU A 1 2934 ? 120.281 88.859  88.959  1.00 2.93   ? 2934 LEU A N     1 
ATOM   11762 C  CA    . LEU A 1 2934 ? 118.979 89.421  88.618  1.00 3.28   ? 2934 LEU A CA    1 
ATOM   11763 C  C     . LEU A 1 2934 ? 119.139 90.101  87.263  1.00 3.02   ? 2934 LEU A C     1 
ATOM   11764 O  O     . LEU A 1 2934 ? 119.545 91.264  87.189  1.00 3.59   ? 2934 LEU A O     1 
ATOM   11765 C  CB    . LEU A 1 2934 ? 118.498 90.397  89.688  1.00 4.06   ? 2934 LEU A CB    1 
ATOM   11766 C  CG    . LEU A 1 2934 ? 117.176 91.115  89.411  1.00 5.39   ? 2934 LEU A CG    1 
ATOM   11767 C  CD1   . LEU A 1 2934 ? 116.073 90.121  89.085  1.00 5.42   ? 2934 LEU A CD1   1 
ATOM   11768 C  CD2   . LEU A 1 2934 ? 116.791 91.990  90.592  1.00 6.61   ? 2934 LEU A CD2   1 
ATOM   11769 N  N     . LEU A 1 2935 ? 118.836 89.371  86.195  1.00 3.00   ? 2935 LEU A N     1 
ATOM   11770 C  CA    . LEU A 1 2935 ? 118.962 89.875  84.835  1.00 3.27   ? 2935 LEU A CA    1 
ATOM   11771 C  C     . LEU A 1 2935 ? 117.644 90.520  84.431  1.00 3.78   ? 2935 LEU A C     1 
ATOM   11772 O  O     . LEU A 1 2935 ? 116.624 89.833  84.317  1.00 7.15   ? 2935 LEU A O     1 
ATOM   11773 C  CB    . LEU A 1 2935 ? 119.327 88.748  83.869  1.00 4.81   ? 2935 LEU A CB    1 
ATOM   11774 C  CG    . LEU A 1 2935 ? 120.658 88.029  84.098  1.00 5.49   ? 2935 LEU A CG    1 
ATOM   11775 C  CD1   . LEU A 1 2935 ? 121.048 87.221  82.871  1.00 3.42   ? 2935 LEU A CD1   1 
ATOM   11776 C  CD2   . LEU A 1 2935 ? 121.754 89.018  84.458  1.00 4.55   ? 2935 LEU A CD2   1 
ATOM   11777 N  N     . ILE A 1 2936 ? 117.663 91.832  84.216  1.00 3.26   ? 2936 ILE A N     1 
ATOM   11778 C  CA    . ILE A 1 2936 ? 116.465 92.583  83.860  1.00 5.43   ? 2936 ILE A CA    1 
ATOM   11779 C  C     . ILE A 1 2936 ? 116.622 93.064  82.427  1.00 5.52   ? 2936 ILE A C     1 
ATOM   11780 O  O     . ILE A 1 2936 ? 117.557 93.812  82.118  1.00 5.83   ? 2936 ILE A O     1 
ATOM   11781 C  CB    . ILE A 1 2936 ? 116.225 93.763  84.813  1.00 6.12   ? 2936 ILE A CB    1 
ATOM   11782 C  CG1   . ILE A 1 2936 ? 116.165 93.270  86.260  1.00 5.96   ? 2936 ILE A CG1   1 
ATOM   11783 C  CG2   . ILE A 1 2936 ? 114.944 94.493  84.440  1.00 5.41   ? 2936 ILE A CG2   1 
ATOM   11784 C  CD1   . ILE A 1 2936 ? 115.938 94.368  87.269  1.00 9.38   ? 2936 ILE A CD1   1 
ATOM   11785 N  N     . GLY A 1 2937 ? 115.709 92.647  81.560  1.00 6.24   ? 2937 GLY A N     1 
ATOM   11786 C  CA    . GLY A 1 2937 ? 115.784 93.031  80.163  1.00 6.64   ? 2937 GLY A CA    1 
ATOM   11787 C  C     . GLY A 1 2937 ? 114.578 92.523  79.407  1.00 9.87   ? 2937 GLY A C     1 
ATOM   11788 O  O     . GLY A 1 2937 ? 113.774 91.737  79.919  1.00 13.69  ? 2937 GLY A O     1 
ATOM   11789 N  N     . VAL A 1 2938 ? 114.466 92.995  78.164  1.00 10.53  ? 2938 VAL A N     1 
ATOM   11790 C  CA    . VAL A 1 2938 ? 113.341 92.624  77.318  1.00 11.51  ? 2938 VAL A CA    1 
ATOM   11791 C  C     . VAL A 1 2938 ? 113.424 91.140  76.964  1.00 10.56  ? 2938 VAL A C     1 
ATOM   11792 O  O     . VAL A 1 2938 ? 114.513 90.568  76.826  1.00 14.01  ? 2938 VAL A O     1 
ATOM   11793 C  CB    . VAL A 1 2938 ? 113.325 93.505  76.056  1.00 13.42  ? 2938 VAL A CB    1 
ATOM   11794 C  CG1   . VAL A 1 2938 ? 112.117 93.200  75.185  1.00 12.91  ? 2938 VAL A CG1   1 
ATOM   11795 C  CG2   . VAL A 1 2938 ? 113.345 94.974  76.445  1.00 14.63  ? 2938 VAL A CG2   1 
ATOM   11796 N  N     . SER A 1 2939 ? 112.260 90.507  76.832  1.00 7.88   ? 2939 SER A N     1 
ATOM   11797 C  CA    . SER A 1 2939 ? 112.214 89.105  76.438  1.00 8.84   ? 2939 SER A CA    1 
ATOM   11798 C  C     . SER A 1 2939 ? 112.803 88.926  75.045  1.00 8.23   ? 2939 SER A C     1 
ATOM   11799 O  O     . SER A 1 2939 ? 112.648 89.783  74.170  1.00 9.24   ? 2939 SER A O     1 
ATOM   11800 C  CB    . SER A 1 2939 ? 110.776 88.588  76.472  1.00 12.32  ? 2939 SER A CB    1 
ATOM   11801 O  OG    . SER A 1 2939 ? 110.215 88.720  77.766  1.00 21.82  ? 2939 SER A OG    1 
ATOM   11802 N  N     . GLY A 1 2940 ? 113.485 87.803  74.842  1.00 7.95   ? 2940 GLY A N     1 
ATOM   11803 C  CA    . GLY A 1 2940 ? 114.161 87.535  73.593  1.00 6.63   ? 2940 GLY A CA    1 
ATOM   11804 C  C     . GLY A 1 2940 ? 115.532 88.157  73.461  1.00 7.27   ? 2940 GLY A C     1 
ATOM   11805 O  O     . GLY A 1 2940 ? 116.125 88.079  72.379  1.00 8.43   ? 2940 GLY A O     1 
ATOM   11806 N  N     . ALA A 1 2941 ? 116.055 88.769  74.523  1.00 7.99   ? 2941 ALA A N     1 
ATOM   11807 C  CA    . ALA A 1 2941 ? 117.368 89.398  74.482  1.00 7.39   ? 2941 ALA A CA    1 
ATOM   11808 C  C     . ALA A 1 2941 ? 118.511 88.404  74.622  1.00 8.62   ? 2941 ALA A C     1 
ATOM   11809 O  O     . ALA A 1 2941 ? 119.672 88.797  74.467  1.00 9.84   ? 2941 ALA A O     1 
ATOM   11810 C  CB    . ALA A 1 2941 ? 117.481 90.450  75.587  1.00 7.89   ? 2941 ALA A CB    1 
ATOM   11811 N  N     . GLY A 1 2942 ? 118.217 87.141  74.911  1.00 7.71   ? 2942 GLY A N     1 
ATOM   11812 C  CA    . GLY A 1 2942 ? 119.255 86.155  75.117  1.00 6.43   ? 2942 GLY A CA    1 
ATOM   11813 C  C     . GLY A 1 2942 ? 119.761 86.042  76.535  1.00 4.15   ? 2942 GLY A C     1 
ATOM   11814 O  O     . GLY A 1 2942 ? 120.851 85.499  76.742  1.00 5.16   ? 2942 GLY A O     1 
ATOM   11815 N  N     . LYS A 1 2943 ? 119.010 86.541  77.520  1.00 5.37   ? 2943 LYS A N     1 
ATOM   11816 C  CA    . LYS A 1 2943 ? 119.448 86.451  78.910  1.00 4.78   ? 2943 LYS A CA    1 
ATOM   11817 C  C     . LYS A 1 2943 ? 119.602 84.998  79.342  1.00 4.59   ? 2943 LYS A C     1 
ATOM   11818 O  O     . LYS A 1 2943 ? 120.640 84.604  79.887  1.00 4.68   ? 2943 LYS A O     1 
ATOM   11819 C  CB    . LYS A 1 2943 ? 118.456 87.178  79.820  1.00 2.87   ? 2943 LYS A CB    1 
ATOM   11820 C  CG    . LYS A 1 2943 ? 118.420 88.685  79.631  1.00 5.24   ? 2943 LYS A CG    1 
ATOM   11821 C  CD    . LYS A 1 2943 ? 117.504 89.350  80.650  1.00 4.80   ? 2943 LYS A CD    1 
ATOM   11822 C  CE    . LYS A 1 2943 ? 116.097 88.774  80.595  1.00 6.51   ? 2943 LYS A CE    1 
ATOM   11823 N  NZ    . LYS A 1 2943 ? 115.499 88.877  79.236  1.00 7.33   ? 2943 LYS A NZ    1 
ATOM   11824 N  N     . THR A 1 2944 ? 118.575 84.181  79.095  1.00 3.53   ? 2944 THR A N     1 
ATOM   11825 C  CA    . THR A 1 2944 ? 118.635 82.775  79.480  1.00 4.31   ? 2944 THR A CA    1 
ATOM   11826 C  C     . THR A 1 2944 ? 119.717 82.033  78.707  1.00 4.74   ? 2944 THR A C     1 
ATOM   11827 O  O     . THR A 1 2944 ? 120.451 81.222  79.282  1.00 4.49   ? 2944 THR A O     1 
ATOM   11828 C  CB    . THR A 1 2944 ? 117.275 82.112  79.264  1.00 5.62   ? 2944 THR A CB    1 
ATOM   11829 O  OG1   . THR A 1 2944 ? 116.248 82.924  79.844  1.00 9.86   ? 2944 THR A OG1   1 
ATOM   11830 C  CG2   . THR A 1 2944 ? 117.246 80.735  79.909  1.00 6.09   ? 2944 THR A CG2   1 
ATOM   11831 N  N     . THR A 1 2945 ? 119.829 82.293  77.402  1.00 5.27   ? 2945 THR A N     1 
ATOM   11832 C  CA    . THR A 1 2945 ? 120.831 81.603  76.596  1.00 4.63   ? 2945 THR A CA    1 
ATOM   11833 C  C     . THR A 1 2945 ? 122.243 81.975  77.026  1.00 4.04   ? 2945 THR A C     1 
ATOM   11834 O  O     . THR A 1 2945 ? 123.116 81.106  77.131  1.00 5.40   ? 2945 THR A O     1 
ATOM   11835 C  CB    . THR A 1 2945 ? 120.625 81.917  75.116  1.00 6.16   ? 2945 THR A CB    1 
ATOM   11836 O  OG1   . THR A 1 2945 ? 119.280 81.596  74.741  1.00 8.43   ? 2945 THR A OG1   1 
ATOM   11837 C  CG2   . THR A 1 2945 ? 121.589 81.114  74.259  1.00 5.76   ? 2945 THR A CG2   1 
ATOM   11838 N  N     . LEU A 1 2946 ? 122.491 83.263  77.276  1.00 2.79   ? 2946 LEU A N     1 
ATOM   11839 C  CA    . LEU A 1 2946 ? 123.808 83.676  77.748  1.00 2.66   ? 2946 LEU A CA    1 
ATOM   11840 C  C     . LEU A 1 2946 ? 124.107 83.092  79.122  1.00 2.97   ? 2946 LEU A C     1 
ATOM   11841 O  O     . LEU A 1 2946 ? 125.241 82.680  79.393  1.00 3.22   ? 2946 LEU A O     1 
ATOM   11842 C  CB    . LEU A 1 2946 ? 123.911 85.201  77.776  1.00 3.90   ? 2946 LEU A CB    1 
ATOM   11843 C  CG    . LEU A 1 2946 ? 124.015 85.902  76.419  1.00 3.20   ? 2946 LEU A CG    1 
ATOM   11844 C  CD1   . LEU A 1 2946 ? 124.381 87.367  76.595  1.00 5.01   ? 2946 LEU A CD1   1 
ATOM   11845 C  CD2   . LEU A 1 2946 ? 125.022 85.198  75.522  1.00 4.18   ? 2946 LEU A CD2   1 
ATOM   11846 N  N     . SER A 1 2947 ? 123.103 83.045  80.003  1.00 2.96   ? 2947 SER A N     1 
ATOM   11847 C  CA    . SER A 1 2947 ? 123.304 82.440  81.314  1.00 3.23   ? 2947 SER A CA    1 
ATOM   11848 C  C     . SER A 1 2947 ? 123.671 80.966  81.190  1.00 2.81   ? 2947 SER A C     1 
ATOM   11849 O  O     . SER A 1 2947 ? 124.597 80.491  81.857  1.00 2.74   ? 2947 SER A O     1 
ATOM   11850 C  CB    . SER A 1 2947 ? 122.049 82.612  82.170  1.00 2.04   ? 2947 SER A CB    1 
ATOM   11851 O  OG    . SER A 1 2947 ? 121.757 83.982  82.374  1.00 4.42   ? 2947 SER A OG    1 
ATOM   11852 N  N     . ARG A 1 2948 ? 122.964 80.231  80.328  1.00 2.86   ? 2948 ARG A N     1 
ATOM   11853 C  CA    . ARG A 1 2948 ? 123.270 78.817  80.131  1.00 3.95   ? 2948 ARG A CA    1 
ATOM   11854 C  C     . ARG A 1 2948 ? 124.654 78.629  79.522  1.00 3.49   ? 2948 ARG A C     1 
ATOM   11855 O  O     . ARG A 1 2948 ? 125.390 77.713  79.906  1.00 4.62   ? 2948 ARG A O     1 
ATOM   11856 C  CB    . ARG A 1 2948 ? 122.202 78.165  79.252  1.00 3.93   ? 2948 ARG A CB    1 
ATOM   11857 C  CG    . ARG A 1 2948 ? 120.821 78.140  79.878  1.00 7.49   ? 2948 ARG A CG    1 
ATOM   11858 C  CD    . ARG A 1 2948 ? 119.748 77.767  78.869  1.00 12.66  ? 2948 ARG A CD    1 
ATOM   11859 N  NE    . ARG A 1 2948 ? 119.839 76.375  78.448  1.00 18.57  ? 2948 ARG A NE    1 
ATOM   11860 C  CZ    . ARG A 1 2948 ? 118.909 75.746  77.743  1.00 29.99  ? 2948 ARG A CZ    1 
ATOM   11861 N  NH1   . ARG A 1 2948 ? 117.797 76.356  77.366  1.00 25.02  ? 2948 ARG A NH1   1 
ATOM   11862 N  NH2   . ARG A 1 2948 ? 119.097 74.472  77.411  1.00 28.70  ? 2948 ARG A NH2   1 
ATOM   11863 N  N     . PHE A 1 2949 ? 125.025 79.486  78.570  1.00 2.71   ? 2949 PHE A N     1 
ATOM   11864 C  CA    . PHE A 1 2949 ? 126.341 79.379  77.949  1.00 3.29   ? 2949 PHE A CA    1 
ATOM   11865 C  C     . PHE A 1 2949 ? 127.450 79.624  78.964  1.00 3.48   ? 2949 PHE A C     1 
ATOM   11866 O  O     . PHE A 1 2949 ? 128.438 78.884  79.011  1.00 4.09   ? 2949 PHE A O     1 
ATOM   11867 C  CB    . PHE A 1 2949 ? 126.449 80.359  76.780  1.00 2.34   ? 2949 PHE A CB    1 
ATOM   11868 C  CG    . PHE A 1 2949 ? 127.848 80.542  76.273  1.00 2.69   ? 2949 PHE A CG    1 
ATOM   11869 C  CD1   . PHE A 1 2949 ? 128.517 79.498  75.656  1.00 3.58   ? 2949 PHE A CD1   1 
ATOM   11870 C  CD2   . PHE A 1 2949 ? 128.497 81.756  76.417  1.00 2.72   ? 2949 PHE A CD2   1 
ATOM   11871 C  CE1   . PHE A 1 2949 ? 129.805 79.662  75.190  1.00 3.77   ? 2949 PHE A CE1   1 
ATOM   11872 C  CE2   . PHE A 1 2949 ? 129.786 81.926  75.953  1.00 4.17   ? 2949 PHE A CE2   1 
ATOM   11873 C  CZ    . PHE A 1 2949 ? 130.441 80.878  75.338  1.00 4.32   ? 2949 PHE A CZ    1 
ATOM   11874 N  N     . VAL A 1 2950 ? 127.297 80.656  79.797  1.00 3.13   ? 2950 VAL A N     1 
ATOM   11875 C  CA    . VAL A 1 2950 ? 128.315 80.946  80.803  1.00 2.87   ? 2950 VAL A CA    1 
ATOM   11876 C  C     . VAL A 1 2950 ? 128.362 79.842  81.853  1.00 3.14   ? 2950 VAL A C     1 
ATOM   11877 O  O     . VAL A 1 2950 ? 129.438 79.483  82.346  1.00 4.81   ? 2950 VAL A O     1 
ATOM   11878 C  CB    . VAL A 1 2950 ? 128.067 82.328  81.434  1.00 3.40   ? 2950 VAL A CB    1 
ATOM   11879 C  CG1   . VAL A 1 2950 ? 129.046 82.580  82.566  1.00 3.58   ? 2950 VAL A CG1   1 
ATOM   11880 C  CG2   . VAL A 1 2950 ? 128.190 83.417  80.381  1.00 1.85   ? 2950 VAL A CG2   1 
ATOM   11881 N  N     . ALA A 1 2951 ? 127.203 79.278  82.205  1.00 2.33   ? 2951 ALA A N     1 
ATOM   11882 C  CA    . ALA A 1 2951 ? 127.182 78.155  83.137  1.00 3.25   ? 2951 ALA A CA    1 
ATOM   11883 C  C     . ALA A 1 2951 ? 127.918 76.952  82.563  1.00 5.10   ? 2951 ALA A C     1 
ATOM   11884 O  O     . ALA A 1 2951 ? 128.642 76.255  83.283  1.00 6.16   ? 2951 ALA A O     1 
ATOM   11885 C  CB    . ALA A 1 2951 ? 125.740 77.789  83.486  1.00 2.63   ? 2951 ALA A CB    1 
ATOM   11886 N  N     . TRP A 1 2952 ? 127.742 76.692  81.265  1.00 4.79   ? 2952 TRP A N     1 
ATOM   11887 C  CA    . TRP A 1 2952 ? 128.485 75.618  80.617  1.00 4.80   ? 2952 TRP A CA    1 
ATOM   11888 C  C     . TRP A 1 2952 ? 129.979 75.917  80.567  1.00 6.49   ? 2952 TRP A C     1 
ATOM   11889 O  O     . TRP A 1 2952 ? 130.796 74.996  80.674  1.00 8.07   ? 2952 TRP A O     1 
ATOM   11890 C  CB    . TRP A 1 2952 ? 127.931 75.371  79.213  1.00 6.10   ? 2952 TRP A CB    1 
ATOM   11891 C  CG    . TRP A 1 2952 ? 128.837 74.566  78.331  1.00 8.71   ? 2952 TRP A CG    1 
ATOM   11892 C  CD1   . TRP A 1 2952 ? 128.911 73.206  78.257  1.00 10.52  ? 2952 TRP A CD1   1 
ATOM   11893 C  CD2   . TRP A 1 2952 ? 129.777 75.071  77.376  1.00 7.37   ? 2952 TRP A CD2   1 
ATOM   11894 N  NE1   . TRP A 1 2952 ? 129.851 72.833  77.328  1.00 11.40  ? 2952 TRP A NE1   1 
ATOM   11895 C  CE2   . TRP A 1 2952 ? 130.397 73.959  76.772  1.00 9.27   ? 2952 TRP A CE2   1 
ATOM   11896 C  CE3   . TRP A 1 2952 ? 130.160 76.355  76.978  1.00 7.48   ? 2952 TRP A CE3   1 
ATOM   11897 C  CZ2   . TRP A 1 2952 ? 131.375 74.093  75.789  1.00 10.02  ? 2952 TRP A CZ2   1 
ATOM   11898 C  CZ3   . TRP A 1 2952 ? 131.133 76.484  76.002  1.00 7.96   ? 2952 TRP A CZ3   1 
ATOM   11899 C  CH2   . TRP A 1 2952 ? 131.730 75.360  75.420  1.00 9.84   ? 2952 TRP A CH2   1 
ATOM   11900 N  N     . MET A 1 2953 ? 130.355 77.189  80.404  1.00 5.27   ? 2953 MET A N     1 
ATOM   11901 C  CA    . MET A 1 2953 ? 131.768 77.554  80.455  1.00 6.45   ? 2953 MET A CA    1 
ATOM   11902 C  C     . MET A 1 2953 ? 132.375 77.298  81.828  1.00 9.11   ? 2953 MET A C     1 
ATOM   11903 O  O     . MET A 1 2953 ? 133.590 77.096  81.938  1.00 12.52  ? 2953 MET A O     1 
ATOM   11904 C  CB    . MET A 1 2953 ? 131.956 79.024  80.078  1.00 7.38   ? 2953 MET A CB    1 
ATOM   11905 C  CG    . MET A 1 2953 ? 131.469 79.395  78.693  1.00 6.64   ? 2953 MET A CG    1 
ATOM   11906 S  SD    . MET A 1 2953 ? 132.747 79.144  77.453  1.00 27.60  ? 2953 MET A SD    1 
ATOM   11907 C  CE    . MET A 1 2953 ? 133.847 80.505  77.833  1.00 9.82   ? 2953 MET A CE    1 
ATOM   11908 N  N     . ASN A 1 2954 ? 131.559 77.302  82.879  1.00 8.55   ? 2954 ASN A N     1 
ATOM   11909 C  CA    . ASN A 1 2954 ? 132.045 77.180  84.246  1.00 7.54   ? 2954 ASN A CA    1 
ATOM   11910 C  C     . ASN A 1 2954 ? 131.765 75.815  84.856  1.00 9.25   ? 2954 ASN A C     1 
ATOM   11911 O  O     . ASN A 1 2954 ? 131.981 75.630  86.058  1.00 14.89  ? 2954 ASN A O     1 
ATOM   11912 C  CB    . ASN A 1 2954 ? 131.426 78.273  85.115  1.00 9.41   ? 2954 ASN A CB    1 
ATOM   11913 C  CG    . ASN A 1 2954 ? 132.010 79.634  84.831  1.00 9.87   ? 2954 ASN A CG    1 
ATOM   11914 O  OD1   . ASN A 1 2954 ? 131.324 80.521  84.323  1.00 8.52   ? 2954 ASN A OD1   1 
ATOM   11915 N  ND2   . ASN A 1 2954 ? 133.283 79.813  85.157  1.00 13.53  ? 2954 ASN A ND2   1 
ATOM   11916 N  N     . GLY A 1 2955 ? 131.297 74.856  84.063  1.00 6.85   ? 2955 GLY A N     1 
ATOM   11917 C  CA    . GLY A 1 2955 ? 130.971 73.554  84.606  1.00 6.32   ? 2955 GLY A CA    1 
ATOM   11918 C  C     . GLY A 1 2955 ? 129.737 73.524  85.474  1.00 8.24   ? 2955 GLY A C     1 
ATOM   11919 O  O     . GLY A 1 2955 ? 129.616 72.647  86.333  1.00 11.74  ? 2955 GLY A O     1 
ATOM   11920 N  N     . LEU A 1 2956 ? 128.814 74.462  85.279  1.00 8.10   ? 2956 LEU A N     1 
ATOM   11921 C  CA    . LEU A 1 2956 ? 127.583 74.514  86.055  1.00 6.06   ? 2956 LEU A CA    1 
ATOM   11922 C  C     . LEU A 1 2956 ? 126.461 73.830  85.287  1.00 7.37   ? 2956 LEU A C     1 
ATOM   11923 O  O     . LEU A 1 2956 ? 126.216 74.147  84.119  1.00 8.40   ? 2956 LEU A O     1 
ATOM   11924 C  CB    . LEU A 1 2956 ? 127.195 75.960  86.371  1.00 6.41   ? 2956 LEU A CB    1 
ATOM   11925 C  CG    . LEU A 1 2956 ? 127.778 76.653  87.606  1.00 6.00   ? 2956 LEU A CG    1 
ATOM   11926 C  CD1   . LEU A 1 2956 ? 129.296 76.650  87.598  1.00 9.88   ? 2956 LEU A CD1   1 
ATOM   11927 C  CD2   . LEU A 1 2956 ? 127.246 78.077  87.717  1.00 3.61   ? 2956 LEU A CD2   1 
ATOM   11928 N  N     . SER A 1 2957 ? 125.785 72.892  85.943  1.00 7.12   ? 2957 SER A N     1 
ATOM   11929 C  CA    . SER A 1 2957 ? 124.612 72.272  85.349  1.00 7.46   ? 2957 SER A CA    1 
ATOM   11930 C  C     . SER A 1 2957 ? 123.429 73.228  85.421  1.00 7.33   ? 2957 SER A C     1 
ATOM   11931 O  O     . SER A 1 2957 ? 123.147 73.812  86.469  1.00 7.91   ? 2957 SER A O     1 
ATOM   11932 C  CB    . SER A 1 2957 ? 124.280 70.963  86.063  1.00 9.16   ? 2957 SER A CB    1 
ATOM   11933 O  OG    . SER A 1 2957 ? 125.362 70.052  85.986  1.00 15.58  ? 2957 SER A OG    1 
ATOM   11934 N  N     . VAL A 1 2958 ? 122.739 73.392  84.300  1.00 7.54   ? 2958 VAL A N     1 
ATOM   11935 C  CA    . VAL A 1 2958 ? 121.625 74.328  84.207  1.00 7.62   ? 2958 VAL A CA    1 
ATOM   11936 C  C     . VAL A 1 2958 ? 120.353 73.615  84.645  1.00 8.26   ? 2958 VAL A C     1 
ATOM   11937 O  O     . VAL A 1 2958 ? 120.022 72.544  84.126  1.00 12.24  ? 2958 VAL A O     1 
ATOM   11938 C  CB    . VAL A 1 2958 ? 121.483 74.885  82.783  1.00 7.48   ? 2958 VAL A CB    1 
ATOM   11939 C  CG1   . VAL A 1 2958 ? 120.144 75.589  82.619  1.00 7.28   ? 2958 VAL A CG1   1 
ATOM   11940 C  CG2   . VAL A 1 2958 ? 122.631 75.828  82.466  1.00 5.38   ? 2958 VAL A CG2   1 
ATOM   11941 N  N     . TYR A 1 2959 ? 119.643 74.204  85.604  1.00 8.06   ? 2959 TYR A N     1 
ATOM   11942 C  CA    . TYR A 1 2959 ? 118.358 73.692  86.055  1.00 8.27   ? 2959 TYR A CA    1 
ATOM   11943 C  C     . TYR A 1 2959 ? 117.276 74.736  85.826  1.00 8.57   ? 2959 TYR A C     1 
ATOM   11944 O  O     . TYR A 1 2959 ? 117.395 75.877  86.285  1.00 7.99   ? 2959 TYR A O     1 
ATOM   11945 C  CB    . TYR A 1 2959 ? 118.399 73.285  87.531  1.00 7.50   ? 2959 TYR A CB    1 
ATOM   11946 C  CG    . TYR A 1 2959 ? 117.164 72.533  87.978  1.00 13.53  ? 2959 TYR A CG    1 
ATOM   11947 C  CD1   . TYR A 1 2959 ? 116.011 73.211  88.357  1.00 12.70  ? 2959 TYR A CD1   1 
ATOM   11948 C  CD2   . TYR A 1 2959 ? 117.134 71.146  87.975  1.00 12.61  ? 2959 TYR A CD2   1 
ATOM   11949 C  CE1   . TYR A 1 2959 ? 114.878 72.530  88.753  1.00 13.94  ? 2959 TYR A CE1   1 
ATOM   11950 C  CE2   . TYR A 1 2959 ? 116.003 70.457  88.367  1.00 16.12  ? 2959 TYR A CE2   1 
ATOM   11951 C  CZ    . TYR A 1 2959 ? 114.880 71.154  88.756  1.00 19.93  ? 2959 TYR A CZ    1 
ATOM   11952 O  OH    . TYR A 1 2959 ? 113.753 70.468  89.146  1.00 23.40  ? 2959 TYR A OH    1 
ATOM   11953 N  N     . GLN A 1 2960 ? 116.219 74.330  85.130  1.00 9.23   ? 2960 GLN A N     1 
ATOM   11954 C  CA    . GLN A 1 2960 ? 115.044 75.158  84.906  1.00 12.81  ? 2960 GLN A CA    1 
ATOM   11955 C  C     . GLN A 1 2960 ? 113.813 74.335  85.242  1.00 15.19  ? 2960 GLN A C     1 
ATOM   11956 O  O     . GLN A 1 2960 ? 113.693 73.188  84.800  1.00 22.83  ? 2960 GLN A O     1 
ATOM   11957 C  CB    . GLN A 1 2960 ? 114.980 75.649  83.455  1.00 12.60  ? 2960 GLN A CB    1 
ATOM   11958 C  CG    . GLN A 1 2960 ? 116.167 76.498  83.031  1.00 13.49  ? 2960 GLN A CG    1 
ATOM   11959 C  CD    . GLN A 1 2960 ? 116.073 76.954  81.588  1.00 18.00  ? 2960 GLN A CD    1 
ATOM   11960 O  OE1   . GLN A 1 2960 ? 115.166 77.698  81.218  1.00 22.88  ? 2960 GLN A OE1   1 
ATOM   11961 N  NE2   . GLN A 1 2960 ? 117.012 76.505  80.764  1.00 18.75  ? 2960 GLN A NE2   1 
ATOM   11962 N  N     . ILE A 1 2961 ? 112.903 74.912  86.027  1.00 15.68  ? 2961 ILE A N     1 
ATOM   11963 C  CA    . ILE A 1 2961 ? 111.665 74.216  86.350  1.00 19.10  ? 2961 ILE A CA    1 
ATOM   11964 C  C     . ILE A 1 2961 ? 110.782 74.154  85.111  1.00 23.05  ? 2961 ILE A C     1 
ATOM   11965 O  O     . ILE A 1 2961 ? 110.701 75.111  84.328  1.00 26.77  ? 2961 ILE A O     1 
ATOM   11966 C  CB    . ILE A 1 2961 ? 110.954 74.890  87.538  1.00 17.79  ? 2961 ILE A CB    1 
ATOM   11967 C  CG1   . ILE A 1 2961 ? 110.337 76.231  87.134  1.00 21.04  ? 2961 ILE A CG1   1 
ATOM   11968 C  CG2   . ILE A 1 2961 ? 111.911 75.059  88.706  1.00 16.19  ? 2961 ILE A CG2   1 
ATOM   11969 C  CD1   . ILE A 1 2961 ? 109.511 76.873  88.226  1.00 25.90  ? 2961 ILE A CD1   1 
ATOM   11970 N  N     . LYS A 1 2962 ? 110.142 73.004  84.907  1.00 26.14  ? 2962 LYS A N     1 
ATOM   11971 C  CA    . LYS A 1 2962 ? 109.349 72.757  83.705  1.00 25.41  ? 2962 LYS A CA    1 
ATOM   11972 C  C     . LYS A 1 2962 ? 107.897 73.112  84.015  1.00 26.70  ? 2962 LYS A C     1 
ATOM   11973 O  O     . LYS A 1 2962 ? 107.081 72.270  84.389  1.00 28.64  ? 2962 LYS A O     1 
ATOM   11974 C  CB    . LYS A 1 2962 ? 109.507 71.311  83.249  1.00 27.16  ? 2962 LYS A CB    1 
ATOM   11975 C  CG    . LYS A 1 2962 ? 110.946 70.933  82.934  1.00 29.27  ? 2962 LYS A CG    1 
ATOM   11976 C  CD    . LYS A 1 2962 ? 111.479 71.720  81.747  1.00 33.65  ? 2962 LYS A CD    1 
ATOM   11977 C  CE    . LYS A 1 2962 ? 112.858 71.231  81.332  1.00 36.03  ? 2962 LYS A CE    1 
ATOM   11978 N  NZ    . LYS A 1 2962 ? 113.895 71.559  82.348  1.00 21.32  ? 2962 LYS A NZ    1 
ATOM   11979 N  N     . VAL A 1 2963 ? 107.584 74.397  83.852  1.00 22.86  ? 2963 VAL A N     1 
ATOM   11980 C  CA    . VAL A 1 2963 ? 106.260 74.900  84.188  1.00 26.71  ? 2963 VAL A CA    1 
ATOM   11981 C  C     . VAL A 1 2963 ? 105.245 74.431  83.155  1.00 27.46  ? 2963 VAL A C     1 
ATOM   11982 O  O     . VAL A 1 2963 ? 105.473 74.523  81.941  1.00 23.62  ? 2963 VAL A O     1 
ATOM   11983 C  CB    . VAL A 1 2963 ? 106.281 76.435  84.286  1.00 31.30  ? 2963 VAL A CB    1 
ATOM   11984 C  CG1   . VAL A 1 2963 ? 104.881 76.973  84.532  1.00 31.30  ? 2963 VAL A CG1   1 
ATOM   11985 C  CG2   . VAL A 1 2963 ? 107.225 76.882  85.384  1.00 29.80  ? 2963 VAL A CG2   1 
ATOM   11986 N  N     . HIS A 1 2964 ? 104.114 73.922  83.639  1.00 28.09  ? 2964 HIS A N     1 
ATOM   11987 C  CA    . HIS A 1 2964 ? 102.968 73.616  82.798  1.00 30.02  ? 2964 HIS A CA    1 
ATOM   11988 C  C     . HIS A 1 2964 ? 101.738 74.256  83.429  1.00 31.57  ? 2964 HIS A C     1 
ATOM   11989 O  O     . HIS A 1 2964 ? 101.830 74.956  84.442  1.00 32.02  ? 2964 HIS A O     1 
ATOM   11990 C  CB    . HIS A 1 2964 ? 102.800 72.103  82.606  1.00 29.46  ? 2964 HIS A CB    1 
ATOM   11991 C  CG    . HIS A 1 2964 ? 102.878 71.315  83.876  1.00 26.63  ? 2964 HIS A CG    1 
ATOM   11992 N  ND1   . HIS A 1 2964 ? 101.768 71.014  84.636  1.00 30.94  ? 2964 HIS A ND1   1 
ATOM   11993 C  CD2   . HIS A 1 2964 ? 103.933 70.759  84.516  1.00 25.91  ? 2964 HIS A CD2   1 
ATOM   11994 C  CE1   . HIS A 1 2964 ? 102.137 70.309  85.690  1.00 33.27  ? 2964 HIS A CE1   1 
ATOM   11995 N  NE2   . HIS A 1 2964 ? 103.446 70.141  85.642  1.00 34.47  ? 2964 HIS A NE2   1 
ATOM   11996 N  N     . ARG A 1 2965 ? 100.573 74.020  82.821  1.00 33.85  ? 2965 ARG A N     1 
ATOM   11997 C  CA    . ARG A 1 2965 ? 99.354  74.659  83.308  1.00 40.00  ? 2965 ARG A CA    1 
ATOM   11998 C  C     . ARG A 1 2965 ? 98.940  74.128  84.675  1.00 37.24  ? 2965 ARG A C     1 
ATOM   11999 O  O     . ARG A 1 2965 ? 98.323  74.858  85.459  1.00 37.05  ? 2965 ARG A O     1 
ATOM   12000 C  CB    . ARG A 1 2965 ? 98.217  74.472  82.304  1.00 41.60  ? 2965 ARG A CB    1 
ATOM   12001 C  CG    . ARG A 1 2965 ? 97.965  73.030  81.901  1.00 48.33  ? 2965 ARG A CG    1 
ATOM   12002 C  CD    . ARG A 1 2965 ? 96.793  72.937  80.937  1.00 48.95  ? 2965 ARG A CD    1 
ATOM   12003 N  NE    . ARG A 1 2965 ? 95.593  73.550  81.493  1.00 48.72  ? 2965 ARG A NE    1 
ATOM   12004 C  CZ    . ARG A 1 2965 ? 94.991  74.617  80.986  1.00 49.76  ? 2965 ARG A CZ    1 
ATOM   12005 N  NH1   . ARG A 1 2965 ? 95.454  75.224  79.906  1.00 46.90  ? 2965 ARG A NH1   1 
ATOM   12006 N  NH2   . ARG A 1 2965 ? 93.899  75.090  81.581  1.00 41.59  ? 2965 ARG A NH2   1 
ATOM   12007 N  N     . LYS A 1 2966 ? 99.266  72.872  84.980  1.00 37.61  ? 2966 LYS A N     1 
ATOM   12008 C  CA    . LYS A 1 2966 ? 98.911  72.254  86.250  1.00 36.47  ? 2966 LYS A CA    1 
ATOM   12009 C  C     . LYS A 1 2966 ? 100.056 72.293  87.259  1.00 36.25  ? 2966 LYS A C     1 
ATOM   12010 O  O     . LYS A 1 2966 ? 100.026 71.554  88.249  1.00 40.56  ? 2966 LYS A O     1 
ATOM   12011 C  CB    . LYS A 1 2966 ? 98.454  70.811  86.026  1.00 43.14  ? 2966 LYS A CB    1 
ATOM   12012 C  CG    . LYS A 1 2966 ? 97.224  70.623  85.125  1.00 42.60  ? 2966 LYS A CG    1 
ATOM   12013 C  CD    . LYS A 1 2966 ? 95.909  71.089  85.761  1.00 44.09  ? 2966 LYS A CD    1 
ATOM   12014 C  CE    . LYS A 1 2966 ? 95.551  72.525  85.392  1.00 47.95  ? 2966 LYS A CE    1 
ATOM   12015 N  NZ    . LYS A 1 2966 ? 94.219  72.931  85.925  1.00 49.93  ? 2966 LYS A NZ    1 
ATOM   12016 N  N     . TYR A 1 2967 ? 101.066 73.127  87.024  1.00 37.55  ? 2967 TYR A N     1 
ATOM   12017 C  CA    . TYR A 1 2967 ? 102.204 73.236  87.929  1.00 29.16  ? 2967 TYR A CA    1 
ATOM   12018 C  C     . TYR A 1 2967 ? 101.787 74.034  89.161  1.00 31.78  ? 2967 TYR A C     1 
ATOM   12019 O  O     . TYR A 1 2967 ? 101.321 75.171  89.040  1.00 36.18  ? 2967 TYR A O     1 
ATOM   12020 C  CB    . TYR A 1 2967 ? 103.376 73.906  87.214  1.00 25.19  ? 2967 TYR A CB    1 
ATOM   12021 C  CG    . TYR A 1 2967 ? 104.712 73.796  87.917  1.00 25.21  ? 2967 TYR A CG    1 
ATOM   12022 C  CD1   . TYR A 1 2967 ? 105.102 74.732  88.866  1.00 21.73  ? 2967 TYR A CD1   1 
ATOM   12023 C  CD2   . TYR A 1 2967 ? 105.596 72.771  87.607  1.00 23.72  ? 2967 TYR A CD2   1 
ATOM   12024 C  CE1   . TYR A 1 2967 ? 106.328 74.638  89.501  1.00 18.04  ? 2967 TYR A CE1   1 
ATOM   12025 C  CE2   . TYR A 1 2967 ? 106.823 72.671  88.234  1.00 21.52  ? 2967 TYR A CE2   1 
ATOM   12026 C  CZ    . TYR A 1 2967 ? 107.184 73.606  89.180  1.00 18.58  ? 2967 TYR A CZ    1 
ATOM   12027 O  OH    . TYR A 1 2967 ? 108.406 73.505  89.803  1.00 16.91  ? 2967 TYR A OH    1 
ATOM   12028 N  N     . THR A 1 2968 ? 101.954 73.444  90.340  1.00 32.49  ? 2968 THR A N     1 
ATOM   12029 C  CA    . THR A 1 2968 ? 101.493 74.031  91.592  1.00 29.68  ? 2968 THR A CA    1 
ATOM   12030 C  C     . THR A 1 2968 ? 102.673 74.282  92.527  1.00 25.30  ? 2968 THR A C     1 
ATOM   12031 O  O     . THR A 1 2968 ? 103.836 74.071  92.175  1.00 23.24  ? 2968 THR A O     1 
ATOM   12032 C  CB    . THR A 1 2968 ? 100.458 73.131  92.274  1.00 34.37  ? 2968 THR A CB    1 
ATOM   12033 O  OG1   . THR A 1 2968 ? 101.106 71.964  92.796  1.00 32.00  ? 2968 THR A OG1   1 
ATOM   12034 C  CG2   . THR A 1 2968 ? 99.381  72.708  91.286  1.00 38.54  ? 2968 THR A CG2   1 
ATOM   12035 N  N     . GLY A 1 2969 ? 102.351 74.743  93.738  1.00 26.83  ? 2969 GLY A N     1 
ATOM   12036 C  CA    . GLY A 1 2969 ? 103.378 74.991  94.735  1.00 23.13  ? 2969 GLY A CA    1 
ATOM   12037 C  C     . GLY A 1 2969 ? 104.094 73.736  95.186  1.00 24.72  ? 2969 GLY A C     1 
ATOM   12038 O  O     . GLY A 1 2969 ? 105.289 73.776  95.489  1.00 23.88  ? 2969 GLY A O     1 
ATOM   12039 N  N     . GLU A 1 2970 ? 103.379 72.611  95.247  1.00 24.59  ? 2970 GLU A N     1 
ATOM   12040 C  CA    . GLU A 1 2970 ? 104.013 71.350  95.618  1.00 23.98  ? 2970 GLU A CA    1 
ATOM   12041 C  C     . GLU A 1 2970 ? 105.047 70.926  94.582  1.00 24.09  ? 2970 GLU A C     1 
ATOM   12042 O  O     . GLU A 1 2970 ? 106.105 70.391  94.936  1.00 25.64  ? 2970 GLU A O     1 
ATOM   12043 C  CB    . GLU A 1 2970 ? 102.961 70.252  95.809  1.00 26.45  ? 2970 GLU A CB    1 
ATOM   12044 C  CG    . GLU A 1 2970 ? 101.892 70.523  96.874  1.00 35.40  ? 2970 GLU A CG    1 
ATOM   12045 C  CD    . GLU A 1 2970 ? 100.944 71.653  96.517  1.00 44.18  ? 2970 GLU A CD    1 
ATOM   12046 O  OE1   . GLU A 1 2970 ? 100.990 72.703  97.191  1.00 40.43  ? 2970 GLU A OE1   1 
ATOM   12047 O  OE2   . GLU A 1 2970 ? 100.153 71.490  95.564  1.00 45.59  ? 2970 GLU A OE2   1 
ATOM   12048 N  N     . ASP A 1 2971 ? 104.758 71.149  93.298  1.00 22.70  ? 2971 ASP A N     1 
ATOM   12049 C  CA    . ASP A 1 2971 ? 105.734 70.837  92.257  1.00 22.32  ? 2971 ASP A CA    1 
ATOM   12050 C  C     . ASP A 1 2971 ? 106.989 71.686  92.408  1.00 17.47  ? 2971 ASP A C     1 
ATOM   12051 O  O     . ASP A 1 2971 ? 108.110 71.187  92.248  1.00 18.33  ? 2971 ASP A O     1 
ATOM   12052 C  CB    . ASP A 1 2971 ? 105.113 71.038  90.875  1.00 24.55  ? 2971 ASP A CB    1 
ATOM   12053 C  CG    . ASP A 1 2971 ? 103.889 70.175  90.655  1.00 32.03  ? 2971 ASP A CG    1 
ATOM   12054 O  OD1   . ASP A 1 2971 ? 102.920 70.306  91.432  1.00 34.57  ? 2971 ASP A OD1   1 
ATOM   12055 O  OD2   . ASP A 1 2971 ? 103.894 69.365  89.705  1.00 37.76  ? 2971 ASP A OD2   1 
ATOM   12056 N  N     . PHE A 1 2972 ? 106.822 72.974  92.713  1.00 14.76  ? 2972 PHE A N     1 
ATOM   12057 C  CA    . PHE A 1 2972 ? 107.977 73.833  92.947  1.00 14.73  ? 2972 PHE A CA    1 
ATOM   12058 C  C     . PHE A 1 2972 ? 108.757 73.390  94.174  1.00 12.36  ? 2972 PHE A C     1 
ATOM   12059 O  O     . PHE A 1 2972 ? 109.989 73.458  94.190  1.00 9.23   ? 2972 PHE A O     1 
ATOM   12060 C  CB    . PHE A 1 2972 ? 107.530 75.281  93.100  1.00 15.87  ? 2972 PHE A CB    1 
ATOM   12061 C  CG    . PHE A 1 2972 ? 108.659 76.267  93.142  1.00 15.29  ? 2972 PHE A CG    1 
ATOM   12062 C  CD1   . PHE A 1 2972 ? 109.477 76.453  92.043  1.00 13.03  ? 2972 PHE A CD1   1 
ATOM   12063 C  CD2   . PHE A 1 2972 ? 108.894 77.017  94.283  1.00 14.96  ? 2972 PHE A CD2   1 
ATOM   12064 C  CE1   . PHE A 1 2972 ? 110.512 77.366  92.082  1.00 14.78  ? 2972 PHE A CE1   1 
ATOM   12065 C  CE2   . PHE A 1 2972 ? 109.925 77.931  94.325  1.00 13.69  ? 2972 PHE A CE2   1 
ATOM   12066 C  CZ    . PHE A 1 2972 ? 110.735 78.104  93.224  1.00 13.56  ? 2972 PHE A CZ    1 
ATOM   12067 N  N     . ASP A 1 2973 ? 108.057 72.955  95.223  1.00 14.49  ? 2973 ASP A N     1 
ATOM   12068 C  CA    . ASP A 1 2973 ? 108.747 72.458  96.408  1.00 12.70  ? 2973 ASP A CA    1 
ATOM   12069 C  C     . ASP A 1 2973 ? 109.555 71.207  96.088  1.00 10.87  ? 2973 ASP A C     1 
ATOM   12070 O  O     . ASP A 1 2973 ? 110.687 71.053  96.558  1.00 8.63   ? 2973 ASP A O     1 
ATOM   12071 C  CB    . ASP A 1 2973 ? 107.743 72.185  97.527  1.00 17.58  ? 2973 ASP A CB    1 
ATOM   12072 C  CG    . ASP A 1 2973 ? 107.380 73.437  98.299  1.00 26.52  ? 2973 ASP A CG    1 
ATOM   12073 O  OD1   . ASP A 1 2973 ? 107.892 74.520  97.949  1.00 29.21  ? 2973 ASP A OD1   1 
ATOM   12074 O  OD2   . ASP A 1 2973 ? 106.584 73.339  99.257  1.00 26.05  ? 2973 ASP A OD2   1 
ATOM   12075 N  N     . GLU A 1 2974 ? 108.991 70.304  95.283  1.00 13.95  ? 2974 GLU A N     1 
ATOM   12076 C  CA    . GLU A 1 2974 ? 109.729 69.111  94.878  1.00 14.99  ? 2974 GLU A CA    1 
ATOM   12077 C  C     . GLU A 1 2974 ? 110.940 69.470  94.023  1.00 13.55  ? 2974 GLU A C     1 
ATOM   12078 O  O     . GLU A 1 2974 ? 112.017 68.882  94.178  1.00 14.01  ? 2974 GLU A O     1 
ATOM   12079 C  CB    . GLU A 1 2974 ? 108.805 68.149  94.129  1.00 14.80  ? 2974 GLU A CB    1 
ATOM   12080 C  CG    . GLU A 1 2974 ? 109.486 66.867  93.671  1.00 25.26  ? 2974 GLU A CG    1 
ATOM   12081 C  CD    . GLU A 1 2974 ? 109.976 66.012  94.826  1.00 37.22  ? 2974 GLU A CD    1 
ATOM   12082 O  OE1   . GLU A 1 2974 ? 109.389 66.095  95.925  1.00 33.73  ? 2974 GLU A OE1   1 
ATOM   12083 O  OE2   . GLU A 1 2974 ? 110.955 65.261  94.636  1.00 32.15  ? 2974 GLU A OE2   1 
ATOM   12084 N  N     . ASP A 1 2975 ? 110.781 70.432  93.110  1.00 10.56  ? 2975 ASP A N     1 
ATOM   12085 C  CA    . ASP A 1 2975 ? 111.910 70.877  92.297  1.00 12.07  ? 2975 ASP A CA    1 
ATOM   12086 C  C     . ASP A 1 2975 ? 112.999 71.502  93.162  1.00 11.54  ? 2975 ASP A C     1 
ATOM   12087 O  O     . ASP A 1 2975 ? 114.195 71.274  92.937  1.00 12.96  ? 2975 ASP A O     1 
ATOM   12088 C  CB    . ASP A 1 2975 ? 111.431 71.869  91.238  1.00 13.39  ? 2975 ASP A CB    1 
ATOM   12089 C  CG    . ASP A 1 2975 ? 110.877 71.183  90.006  1.00 26.07  ? 2975 ASP A CG    1 
ATOM   12090 O  OD1   . ASP A 1 2975 ? 111.108 69.966  89.850  1.00 30.30  ? 2975 ASP A OD1   1 
ATOM   12091 O  OD2   . ASP A 1 2975 ? 110.208 71.858  89.197  1.00 27.21  ? 2975 ASP A OD2   1 
ATOM   12092 N  N     . LEU A 1 2976 ? 112.598 72.302  94.153  1.00 8.15   ? 2976 LEU A N     1 
ATOM   12093 C  CA    . LEU A 1 2976 ? 113.553 72.882  95.088  1.00 7.34   ? 2976 LEU A CA    1 
ATOM   12094 C  C     . LEU A 1 2976 ? 114.280 71.798  95.868  1.00 7.56   ? 2976 LEU A C     1 
ATOM   12095 O  O     . LEU A 1 2976 ? 115.496 71.877  96.066  1.00 7.11   ? 2976 LEU A O     1 
ATOM   12096 C  CB    . LEU A 1 2976 ? 112.837 73.835  96.044  1.00 7.10   ? 2976 LEU A CB    1 
ATOM   12097 C  CG    . LEU A 1 2976 ? 112.496 75.239  95.546  1.00 7.15   ? 2976 LEU A CG    1 
ATOM   12098 C  CD1   . LEU A 1 2976 ? 111.778 76.017  96.637  1.00 12.11  ? 2976 LEU A CD1   1 
ATOM   12099 C  CD2   . LEU A 1 2976 ? 113.746 75.972  95.092  1.00 8.94   ? 2976 LEU A CD2   1 
ATOM   12100 N  N     . ARG A 1 2977 ? 113.551 70.776  96.321  1.00 7.93   ? 2977 ARG A N     1 
ATOM   12101 C  CA    . ARG A 1 2977 ? 114.194 69.673  97.027  1.00 7.54   ? 2977 ARG A CA    1 
ATOM   12102 C  C     . ARG A 1 2977 ? 115.198 68.961  96.133  1.00 6.72   ? 2977 ARG A C     1 
ATOM   12103 O  O     . ARG A 1 2977 ? 116.300 68.628  96.574  1.00 5.87   ? 2977 ARG A O     1 
ATOM   12104 C  CB    . ARG A 1 2977 ? 113.147 68.688  97.547  1.00 8.88   ? 2977 ARG A CB    1 
ATOM   12105 C  CG    . ARG A 1 2977 ? 112.395 69.170  98.773  1.00 8.39   ? 2977 ARG A CG    1 
ATOM   12106 C  CD    . ARG A 1 2977 ? 111.259 68.229  99.136  1.00 9.39   ? 2977 ARG A CD    1 
ATOM   12107 N  NE    . ARG A 1 2977 ? 110.143 68.938  99.749  1.00 13.79  ? 2977 ARG A NE    1 
ATOM   12108 C  CZ    . ARG A 1 2977 ? 108.923 69.005  99.233  1.00 13.82  ? 2977 ARG A CZ    1 
ATOM   12109 N  NH1   . ARG A 1 2977 ? 108.622 68.408  98.092  1.00 12.66  ? 2977 ARG A NH1   1 
ATOM   12110 N  NH2   . ARG A 1 2977 ? 107.982 69.687  99.879  1.00 19.70  ? 2977 ARG A NH2   1 
ATOM   12111 N  N     . THR A 1 2978 ? 114.839 68.732  94.869  1.00 8.12   ? 2978 THR A N     1 
ATOM   12112 C  CA    . THR A 1 2978 ? 115.754 68.067  93.946  1.00 9.60   ? 2978 THR A CA    1 
ATOM   12113 C  C     . THR A 1 2978 ? 117.025 68.887  93.742  1.00 7.87   ? 2978 THR A C     1 
ATOM   12114 O  O     . THR A 1 2978 ? 118.145 68.362  93.839  1.00 9.07   ? 2978 THR A O     1 
ATOM   12115 C  CB    . THR A 1 2978 ? 115.054 67.816  92.609  1.00 10.95  ? 2978 THR A CB    1 
ATOM   12116 O  OG1   . THR A 1 2978 ? 113.992 66.872  92.793  1.00 22.93  ? 2978 THR A OG1   1 
ATOM   12117 C  CG2   . THR A 1 2978 ? 116.035 67.273  91.583  1.00 10.97  ? 2978 THR A CG2   1 
ATOM   12118 N  N     . VAL A 1 2979 ? 116.870 70.185  93.470  1.00 6.26   ? 2979 VAL A N     1 
ATOM   12119 C  CA    . VAL A 1 2979 ? 118.038 71.015  93.187  1.00 6.14   ? 2979 VAL A CA    1 
ATOM   12120 C  C     . VAL A 1 2979 ? 118.897 71.169  94.437  1.00 6.01   ? 2979 VAL A C     1 
ATOM   12121 O  O     . VAL A 1 2979 ? 120.131 71.196  94.356  1.00 8.24   ? 2979 VAL A O     1 
ATOM   12122 C  CB    . VAL A 1 2979 ? 117.615 72.375  92.592  1.00 9.45   ? 2979 VAL A CB    1 
ATOM   12123 C  CG1   . VAL A 1 2979 ? 116.863 73.225  93.601  1.00 10.10  ? 2979 VAL A CG1   1 
ATOM   12124 C  CG2   . VAL A 1 2979 ? 118.822 73.119  92.039  1.00 10.71  ? 2979 VAL A CG2   1 
ATOM   12125 N  N     . LEU A 1 2980 ? 118.270 71.240  95.615  1.00 5.86   ? 2980 LEU A N     1 
ATOM   12126 C  CA    . LEU A 1 2980 ? 119.042 71.368  96.846  1.00 4.71   ? 2980 LEU A CA    1 
ATOM   12127 C  C     . LEU A 1 2980 ? 119.753 70.067  97.192  1.00 5.25   ? 2980 LEU A C     1 
ATOM   12128 O  O     . LEU A 1 2980 ? 120.870 70.092  97.716  1.00 7.03   ? 2980 LEU A O     1 
ATOM   12129 C  CB    . LEU A 1 2980 ? 118.141 71.816  97.996  1.00 6.12   ? 2980 LEU A CB    1 
ATOM   12130 C  CG    . LEU A 1 2980 ? 117.638 73.260  97.921  1.00 5.68   ? 2980 LEU A CG    1 
ATOM   12131 C  CD1   . LEU A 1 2980 ? 116.895 73.641  99.190  1.00 6.70   ? 2980 LEU A CD1   1 
ATOM   12132 C  CD2   . LEU A 1 2980 ? 118.780 74.224  97.654  1.00 4.84   ? 2980 LEU A CD2   1 
ATOM   12133 N  N     . ARG A 1 2981 ? 119.129 68.920  96.911  1.00 6.46   ? 2981 ARG A N     1 
ATOM   12134 C  CA    . ARG A 1 2981 ? 119.819 67.648  97.099  1.00 6.15   ? 2981 ARG A CA    1 
ATOM   12135 C  C     . ARG A 1 2981 ? 121.031 67.547  96.186  1.00 6.72   ? 2981 ARG A C     1 
ATOM   12136 O  O     . ARG A 1 2981 ? 122.093 67.073  96.603  1.00 8.13   ? 2981 ARG A O     1 
ATOM   12137 C  CB    . ARG A 1 2981 ? 118.867 66.478  96.846  1.00 8.02   ? 2981 ARG A CB    1 
ATOM   12138 C  CG    . ARG A 1 2981 ? 117.801 66.272  97.907  1.00 9.98   ? 2981 ARG A CG    1 
ATOM   12139 C  CD    . ARG A 1 2981 ? 116.756 65.273  97.423  1.00 10.13  ? 2981 ARG A CD    1 
ATOM   12140 N  NE    . ARG A 1 2981 ? 115.661 65.088  98.368  1.00 12.53  ? 2981 ARG A NE    1 
ATOM   12141 C  CZ    . ARG A 1 2981 ? 115.770 64.482  99.544  1.00 14.27  ? 2981 ARG A CZ    1 
ATOM   12142 N  NH1   . ARG A 1 2981 ? 116.917 63.965  99.953  1.00 11.92  ? 2981 ARG A NH1   1 
ATOM   12143 N  NH2   . ARG A 1 2981 ? 114.698 64.385  100.325 1.00 14.47  ? 2981 ARG A NH2   1 
ATOM   12144 N  N     . ARG A 1 2982 ? 120.894 67.984  94.933  1.00 6.71   ? 2982 ARG A N     1 
ATOM   12145 C  CA    . ARG A 1 2982 ? 122.038 67.917  94.028  1.00 6.69   ? 2982 ARG A CA    1 
ATOM   12146 C  C     . ARG A 1 2982 ? 123.138 68.896  94.431  1.00 8.00   ? 2982 ARG A C     1 
ATOM   12147 O  O     . ARG A 1 2982 ? 124.326 68.562  94.356  1.00 10.09  ? 2982 ARG A O     1 
ATOM   12148 C  CB    . ARG A 1 2982 ? 121.595 68.159  92.587  1.00 6.43   ? 2982 ARG A CB    1 
ATOM   12149 C  CG    . ARG A 1 2982 ? 120.765 67.033  92.001  1.00 8.50   ? 2982 ARG A CG    1 
ATOM   12150 C  CD    . ARG A 1 2982 ? 120.174 67.427  90.665  1.00 10.56  ? 2982 ARG A CD    1 
ATOM   12151 N  NE    . ARG A 1 2982 ? 121.199 67.812  89.702  1.00 12.91  ? 2982 ARG A NE    1 
ATOM   12152 C  CZ    . ARG A 1 2982 ? 120.947 68.312  88.500  1.00 12.08  ? 2982 ARG A CZ    1 
ATOM   12153 N  NH1   . ARG A 1 2982 ? 119.709 68.502  88.077  1.00 9.59   ? 2982 ARG A NH1   1 
ATOM   12154 N  NH2   . ARG A 1 2982 ? 121.963 68.630  87.704  1.00 12.90  ? 2982 ARG A NH2   1 
ATOM   12155 N  N     . SER A 1 2983 ? 122.771 70.103  94.863  1.00 7.11   ? 2983 SER A N     1 
ATOM   12156 C  CA    . SER A 1 2983 ? 123.763 71.124  95.181  1.00 6.53   ? 2983 SER A CA    1 
ATOM   12157 C  C     . SER A 1 2983 ? 124.431 70.935  96.537  1.00 7.05   ? 2983 SER A C     1 
ATOM   12158 O  O     . SER A 1 2983 ? 125.631 71.207  96.661  1.00 6.87   ? 2983 SER A O     1 
ATOM   12159 C  CB    . SER A 1 2983 ? 123.120 72.513  95.131  1.00 6.32   ? 2983 SER A CB    1 
ATOM   12160 O  OG    . SER A 1 2983 ? 123.896 73.465  95.836  1.00 10.90  ? 2983 SER A OG    1 
ATOM   12161 N  N     . GLY A 1 2984 ? 123.699 70.476  97.549  1.00 7.05   ? 2984 GLY A N     1 
ATOM   12162 C  CA    . GLY A 1 2984 ? 124.225 70.410  98.898  1.00 7.17   ? 2984 GLY A CA    1 
ATOM   12163 C  C     . GLY A 1 2984 ? 124.735 69.047  99.314  1.00 9.28   ? 2984 GLY A C     1 
ATOM   12164 O  O     . GLY A 1 2984 ? 125.604 68.946  100.185 1.00 9.87   ? 2984 GLY A O     1 
ATOM   12165 N  N     . CYS A 1 2985 ? 124.203 67.988  98.707  1.00 8.83   ? 2985 CYS A N     1 
ATOM   12166 C  CA    . CYS A 1 2985 ? 124.635 66.630  99.012  1.00 11.89  ? 2985 CYS A CA    1 
ATOM   12167 C  C     . CYS A 1 2985 ? 125.648 66.094  98.011  1.00 13.75  ? 2985 CYS A C     1 
ATOM   12168 O  O     . CYS A 1 2985 ? 126.643 65.483  98.411  1.00 14.61  ? 2985 CYS A O     1 
ATOM   12169 C  CB    . CYS A 1 2985 ? 123.430 65.686  99.063  1.00 10.16  ? 2985 CYS A CB    1 
ATOM   12170 S  SG    . CYS A 1 2985 ? 122.130 66.180  100.213 1.00 15.25  ? 2985 CYS A SG    1 
ATOM   12171 N  N     . LYS A 1 2986 ? 125.419 66.313  96.719  1.00 13.00  ? 2986 LYS A N     1 
ATOM   12172 C  CA    . LYS A 1 2986 ? 126.287 65.792  95.672  1.00 9.40   ? 2986 LYS A CA    1 
ATOM   12173 C  C     . LYS A 1 2986 ? 127.395 66.759  95.276  1.00 9.78   ? 2986 LYS A C     1 
ATOM   12174 O  O     . LYS A 1 2986 ? 128.171 66.444  94.368  1.00 13.86  ? 2986 LYS A O     1 
ATOM   12175 C  CB    . LYS A 1 2986 ? 125.456 65.428  94.438  1.00 12.09  ? 2986 LYS A CB    1 
ATOM   12176 C  CG    . LYS A 1 2986 ? 124.441 64.325  94.687  1.00 13.19  ? 2986 LYS A CG    1 
ATOM   12177 C  CD    . LYS A 1 2986 ? 125.128 62.999  94.960  1.00 20.89  ? 2986 LYS A CD    1 
ATOM   12178 C  CE    . LYS A 1 2986 ? 124.119 61.875  95.121  1.00 31.20  ? 2986 LYS A CE    1 
ATOM   12179 N  NZ    . LYS A 1 2986 ? 124.782 60.578  95.426  1.00 37.80  ? 2986 LYS A NZ    1 
ATOM   12180 N  N     . ASN A 1 2987 ? 127.481 67.921  95.928  1.00 12.43  ? 2987 ASN A N     1 
ATOM   12181 C  CA    . ASN A 1 2987 ? 128.528 68.910  95.658  1.00 11.69  ? 2987 ASN A CA    1 
ATOM   12182 C  C     . ASN A 1 2987 ? 128.520 69.344  94.193  1.00 11.51  ? 2987 ASN A C     1 
ATOM   12183 O  O     . ASN A 1 2987 ? 129.567 69.602  93.595  1.00 13.89  ? 2987 ASN A O     1 
ATOM   12184 C  CB    . ASN A 1 2987 ? 129.905 68.381  96.065  1.00 11.89  ? 2987 ASN A CB    1 
ATOM   12185 C  CG    . ASN A 1 2987 ? 130.911 69.490  96.298  1.00 14.45  ? 2987 ASN A CG    1 
ATOM   12186 O  OD1   . ASN A 1 2987 ? 130.644 70.444  97.027  1.00 17.30  ? 2987 ASN A OD1   1 
ATOM   12187 N  ND2   . ASN A 1 2987 ? 132.078 69.368  95.678  1.00 16.70  ? 2987 ASN A ND2   1 
ATOM   12188 N  N     . GLU A 1 2988 ? 127.329 69.424  93.609  1.00 7.46   ? 2988 GLU A N     1 
ATOM   12189 C  CA    . GLU A 1 2988 ? 127.165 69.769  92.204  1.00 8.99   ? 2988 GLU A CA    1 
ATOM   12190 C  C     . GLU A 1 2988 ? 126.888 71.262  92.081  1.00 7.95   ? 2988 GLU A C     1 
ATOM   12191 O  O     . GLU A 1 2988 ? 125.991 71.788  92.750  1.00 9.54   ? 2988 GLU A O     1 
ATOM   12192 C  CB    . GLU A 1 2988 ? 126.034 68.957  91.575  1.00 9.06   ? 2988 GLU A CB    1 
ATOM   12193 C  CG    . GLU A 1 2988 ? 125.767 69.284  90.116  1.00 12.33  ? 2988 GLU A CG    1 
ATOM   12194 C  CD    . GLU A 1 2988 ? 124.589 68.514  89.557  1.00 21.39  ? 2988 GLU A CD    1 
ATOM   12195 O  OE1   . GLU A 1 2988 ? 123.957 67.755  90.320  1.00 23.71  ? 2988 GLU A OE1   1 
ATOM   12196 O  OE2   . GLU A 1 2988 ? 124.294 68.667  88.354  1.00 21.55  ? 2988 GLU A OE2   1 
ATOM   12197 N  N     . LYS A 1 2989 ? 127.656 71.937  91.232  1.00 9.15   ? 2989 LYS A N     1 
ATOM   12198 C  CA    . LYS A 1 2989 ? 127.439 73.354  90.969  1.00 6.96   ? 2989 LYS A CA    1 
ATOM   12199 C  C     . LYS A 1 2989 ? 126.297 73.502  89.973  1.00 5.42   ? 2989 LYS A C     1 
ATOM   12200 O  O     . LYS A 1 2989 ? 126.399 73.045  88.830  1.00 7.27   ? 2989 LYS A O     1 
ATOM   12201 C  CB    . LYS A 1 2989 ? 128.717 73.999  90.440  1.00 8.61   ? 2989 LYS A CB    1 
ATOM   12202 C  CG    . LYS A 1 2989 ? 129.842 74.052  91.460  1.00 10.37  ? 2989 LYS A CG    1 
ATOM   12203 C  CD    . LYS A 1 2989 ? 131.032 74.844  90.945  1.00 13.44  ? 2989 LYS A CD    1 
ATOM   12204 C  CE    . LYS A 1 2989 ? 131.801 74.066  89.893  1.00 18.49  ? 2989 LYS A CE    1 
ATOM   12205 N  NZ    . LYS A 1 2989 ? 133.029 74.786  89.462  1.00 28.86  ? 2989 LYS A NZ    1 
ATOM   12206 N  N     . ILE A 1 2990 ? 125.212 74.140  90.403  1.00 5.02   ? 2990 ILE A N     1 
ATOM   12207 C  CA    . ILE A 1 2990 ? 123.990 74.238  89.615  1.00 5.77   ? 2990 ILE A CA    1 
ATOM   12208 C  C     . ILE A 1 2990 ? 123.625 75.703  89.437  1.00 5.23   ? 2990 ILE A C     1 
ATOM   12209 O  O     . ILE A 1 2990 ? 123.517 76.448  90.420  1.00 3.54   ? 2990 ILE A O     1 
ATOM   12210 C  CB    . ILE A 1 2990 ? 122.828 73.468  90.268  1.00 5.53   ? 2990 ILE A CB    1 
ATOM   12211 C  CG1   . ILE A 1 2990 ? 123.067 71.961  90.172  1.00 7.57   ? 2990 ILE A CG1   1 
ATOM   12212 C  CG2   . ILE A 1 2990 ? 121.502 73.853  89.626  1.00 5.78   ? 2990 ILE A CG2   1 
ATOM   12213 C  CD1   . ILE A 1 2990 ? 121.914 71.134  90.680  1.00 10.33  ? 2990 ILE A CD1   1 
ATOM   12214 N  N     . ALA A 1 2991 ? 123.431 76.104  88.184  1.00 5.86   ? 2991 ALA A N     1 
ATOM   12215 C  CA    . ALA A 1 2991 ? 122.829 77.385  87.841  1.00 4.77   ? 2991 ALA A CA    1 
ATOM   12216 C  C     . ALA A 1 2991 ? 121.327 77.165  87.710  1.00 5.40   ? 2991 ALA A C     1 
ATOM   12217 O  O     . ALA A 1 2991 ? 120.858 76.591  86.722  1.00 6.68   ? 2991 ALA A O     1 
ATOM   12218 C  CB    . ALA A 1 2991 ? 123.424 77.945  86.551  1.00 2.93   ? 2991 ALA A CB    1 
ATOM   12219 N  N     . PHE A 1 2992 ? 120.582 77.597  88.721  1.00 3.46   ? 2992 PHE A N     1 
ATOM   12220 C  CA    . PHE A 1 2992 ? 119.126 77.507  88.731  1.00 4.66   ? 2992 PHE A CA    1 
ATOM   12221 C  C     . PHE A 1 2992 ? 118.596 78.756  88.039  1.00 4.60   ? 2992 PHE A C     1 
ATOM   12222 O  O     . PHE A 1 2992 ? 118.518 79.828  88.640  1.00 6.70   ? 2992 PHE A O     1 
ATOM   12223 C  CB    . PHE A 1 2992 ? 118.612 77.382  90.161  1.00 5.71   ? 2992 PHE A CB    1 
ATOM   12224 C  CG    . PHE A 1 2992 ? 117.120 77.250  90.269  1.00 7.73   ? 2992 PHE A CG    1 
ATOM   12225 C  CD1   . PHE A 1 2992 ? 116.378 76.707  89.234  1.00 9.36   ? 2992 PHE A CD1   1 
ATOM   12226 C  CD2   . PHE A 1 2992 ? 116.460 77.666  91.413  1.00 9.14   ? 2992 PHE A CD2   1 
ATOM   12227 C  CE1   . PHE A 1 2992 ? 115.008 76.587  89.336  1.00 12.12  ? 2992 PHE A CE1   1 
ATOM   12228 C  CE2   . PHE A 1 2992 ? 115.090 77.547  91.521  1.00 11.48  ? 2992 PHE A CE2   1 
ATOM   12229 C  CZ    . PHE A 1 2992 ? 114.362 77.006  90.482  1.00 16.05  ? 2992 PHE A CZ    1 
ATOM   12230 N  N     . ILE A 1 2993 ? 118.241 78.621  86.766  1.00 5.61   ? 2993 ILE A N     1 
ATOM   12231 C  CA    . ILE A 1 2993 ? 117.804 79.755  85.961  1.00 5.89   ? 2993 ILE A CA    1 
ATOM   12232 C  C     . ILE A 1 2993 ? 116.283 79.765  85.933  1.00 8.27   ? 2993 ILE A C     1 
ATOM   12233 O  O     . ILE A 1 2993 ? 115.655 78.795  85.495  1.00 13.10  ? 2993 ILE A O     1 
ATOM   12234 C  CB    . ILE A 1 2993 ? 118.384 79.685  84.541  1.00 5.34   ? 2993 ILE A CB    1 
ATOM   12235 C  CG1   . ILE A 1 2993 ? 119.899 79.483  84.602  1.00 3.37   ? 2993 ILE A CG1   1 
ATOM   12236 C  CG2   . ILE A 1 2993 ? 118.036 80.944  83.761  1.00 6.02   ? 2993 ILE A CG2   1 
ATOM   12237 C  CD1   . ILE A 1 2993 ? 120.559 79.384  83.249  1.00 3.82   ? 2993 ILE A CD1   1 
ATOM   12238 N  N     . MET A 1 2994 ? 115.687 80.859  86.403  1.00 8.62   ? 2994 MET A N     1 
ATOM   12239 C  CA    . MET A 1 2994 ? 114.238 80.945  86.508  1.00 11.79  ? 2994 MET A CA    1 
ATOM   12240 C  C     . MET A 1 2994 ? 113.769 82.332  86.094  1.00 11.75  ? 2994 MET A C     1 
ATOM   12241 O  O     . MET A 1 2994 ? 114.437 83.334  86.371  1.00 13.12  ? 2994 MET A O     1 
ATOM   12242 C  CB    . MET A 1 2994 ? 113.780 80.602  87.932  1.00 15.95  ? 2994 MET A CB    1 
ATOM   12243 C  CG    . MET A 1 2994 ? 112.277 80.608  88.137  1.00 32.75  ? 2994 MET A CG    1 
ATOM   12244 S  SD    . MET A 1 2994 ? 111.807 80.163  89.820  1.00 62.64  ? 2994 MET A SD    1 
ATOM   12245 C  CE    . MET A 1 2994 ? 112.313 81.618  90.722  1.00 36.27  ? 2994 MET A CE    1 
ATOM   12246 N  N     . ASP A 1 2995 ? 112.632 82.377  85.409  1.00 17.07  ? 2995 ASP A N     1 
ATOM   12247 C  CA    . ASP A 1 2995 ? 112.053 83.616  84.916  1.00 17.88  ? 2995 ASP A CA    1 
ATOM   12248 C  C     . ASP A 1 2995 ? 110.862 84.032  85.774  1.00 17.88  ? 2995 ASP A C     1 
ATOM   12249 O  O     . ASP A 1 2995 ? 110.325 83.250  86.561  1.00 21.89  ? 2995 ASP A O     1 
ATOM   12250 C  CB    . ASP A 1 2995 ? 111.620 83.460  83.458  1.00 17.85  ? 2995 ASP A CB    1 
ATOM   12251 C  CG    . ASP A 1 2995 ? 111.542 84.786  82.728  1.00 24.80  ? 2995 ASP A CG    1 
ATOM   12252 O  OD1   . ASP A 1 2995 ? 112.590 85.270  82.254  1.00 20.57  ? 2995 ASP A OD1   1 
ATOM   12253 O  OD2   . ASP A 1 2995 ? 110.430 85.345  82.627  1.00 26.31  ? 2995 ASP A OD2   1 
ATOM   12254 N  N     . GLU A 1 2996 ? 110.458 85.295  85.614  1.00 22.63  ? 2996 GLU A N     1 
ATOM   12255 C  CA    . GLU A 1 2996 ? 109.274 85.786  86.312  1.00 27.39  ? 2996 GLU A CA    1 
ATOM   12256 C  C     . GLU A 1 2996 ? 108.018 85.055  85.860  1.00 25.79  ? 2996 GLU A C     1 
ATOM   12257 O  O     . GLU A 1 2996 ? 107.067 84.915  86.637  1.00 28.49  ? 2996 GLU A O     1 
ATOM   12258 C  CB    . GLU A 1 2996 ? 109.118 87.290  86.093  1.00 26.64  ? 2996 GLU A CB    1 
ATOM   12259 C  CG    . GLU A 1 2996 ? 109.305 87.728  84.650  1.00 23.01  ? 2996 GLU A CG    1 
ATOM   12260 C  CD    . GLU A 1 2996 ? 108.859 89.157  84.410  1.00 31.41  ? 2996 GLU A CD    1 
ATOM   12261 O  OE1   . GLU A 1 2996 ? 108.502 89.844  85.391  1.00 37.19  ? 2996 GLU A OE1   1 
ATOM   12262 O  OE2   . GLU A 1 2996 ? 108.865 89.594  83.241  1.00 24.81  ? 2996 GLU A OE2   1 
ATOM   12263 N  N     . SER A 1 2997 ? 107.993 84.587  84.609  1.00 24.55  ? 2997 SER A N     1 
ATOM   12264 C  CA    . SER A 1 2997 ? 106.848 83.825  84.125  1.00 30.44  ? 2997 SER A CA    1 
ATOM   12265 C  C     . SER A 1 2997 ? 106.720 82.488  84.844  1.00 30.86  ? 2997 SER A C     1 
ATOM   12266 O  O     . SER A 1 2997 ? 105.611 81.958  84.969  1.00 37.86  ? 2997 SER A O     1 
ATOM   12267 C  CB    . SER A 1 2997 ? 106.960 83.611  82.616  1.00 32.65  ? 2997 SER A CB    1 
ATOM   12268 O  OG    . SER A 1 2997 ? 108.066 82.785  82.298  1.00 41.36  ? 2997 SER A OG    1 
ATOM   12269 N  N     . ASN A 1 2998 ? 107.836 81.931  85.319  1.00 31.45  ? 2998 ASN A N     1 
ATOM   12270 C  CA    . ASN A 1 2998 ? 107.797 80.701  86.099  1.00 30.84  ? 2998 ASN A CA    1 
ATOM   12271 C  C     . ASN A 1 2998 ? 107.120 80.885  87.450  1.00 32.44  ? 2998 ASN A C     1 
ATOM   12272 O  O     . ASN A 1 2998 ? 106.718 79.891  88.062  1.00 41.89  ? 2998 ASN A O     1 
ATOM   12273 C  CB    . ASN A 1 2998 ? 109.215 80.166  86.309  1.00 28.32  ? 2998 ASN A CB    1 
ATOM   12274 C  CG    . ASN A 1 2998 ? 109.844 79.657  85.028  1.00 29.20  ? 2998 ASN A CG    1 
ATOM   12275 O  OD1   . ASN A 1 2998 ? 109.220 79.670  83.968  1.00 31.02  ? 2998 ASN A OD1   1 
ATOM   12276 N  ND2   . ASN A 1 2998 ? 111.090 79.207  85.120  1.00 28.01  ? 2998 ASN A ND2   1 
ATOM   12277 N  N     . VAL A 1 2999 ? 106.990 82.122  87.926  1.00 30.80  ? 2999 VAL A N     1 
ATOM   12278 C  CA    . VAL A 1 2999 ? 106.370 82.409  89.218  1.00 34.03  ? 2999 VAL A CA    1 
ATOM   12279 C  C     . VAL A 1 2999 ? 104.857 82.400  89.013  1.00 40.47  ? 2999 VAL A C     1 
ATOM   12280 O  O     . VAL A 1 2999 ? 104.271 83.390  88.572  1.00 45.71  ? 2999 VAL A O     1 
ATOM   12281 C  CB    . VAL A 1 2999 ? 106.853 83.739  89.799  1.00 34.06  ? 2999 VAL A CB    1 
ATOM   12282 C  CG1   . VAL A 1 2999 ? 106.137 84.034  91.105  1.00 37.16  ? 2999 VAL A CG1   1 
ATOM   12283 C  CG2   . VAL A 1 2999 ? 108.360 83.713  90.002  1.00 31.54  ? 2999 VAL A CG2   1 
ATOM   12284 N  N     . LEU A 1 3000 ? 104.221 81.272  89.324  1.00 40.97  ? 3000 LEU A N     1 
ATOM   12285 C  CA    . LEU A 1 3000 ? 102.772 81.161  89.242  1.00 41.23  ? 3000 LEU A CA    1 
ATOM   12286 C  C     . LEU A 1 3000 ? 102.070 81.528  90.543  1.00 45.93  ? 3000 LEU A C     1 
ATOM   12287 O  O     . LEU A 1 3000 ? 100.837 81.615  90.559  1.00 57.70  ? 3000 LEU A O     1 
ATOM   12288 C  CB    . LEU A 1 3000 ? 102.370 79.738  88.838  1.00 40.57  ? 3000 LEU A CB    1 
ATOM   12289 C  CG    . LEU A 1 3000 ? 103.102 79.120  87.644  1.00 39.77  ? 3000 LEU A CG    1 
ATOM   12290 C  CD1   . LEU A 1 3000 ? 102.506 77.767  87.294  1.00 36.93  ? 3000 LEU A CD1   1 
ATOM   12291 C  CD2   . LEU A 1 3000 ? 103.061 80.051  86.443  1.00 40.79  ? 3000 LEU A CD2   1 
ATOM   12292 N  N     . ASP A 1 3001 ? 102.816 81.744  91.625  1.00 38.40  ? 3001 ASP A N     1 
ATOM   12293 C  CA    . ASP A 1 3001 ? 102.216 82.052  92.915  1.00 44.24  ? 3001 ASP A CA    1 
ATOM   12294 C  C     . ASP A 1 3001 ? 103.240 82.780  93.776  1.00 44.54  ? 3001 ASP A C     1 
ATOM   12295 O  O     . ASP A 1 3001 ? 104.448 82.698  93.541  1.00 46.57  ? 3001 ASP A O     1 
ATOM   12296 C  CB    . ASP A 1 3001 ? 101.720 80.776  93.612  1.00 42.44  ? 3001 ASP A CB    1 
ATOM   12297 C  CG    . ASP A 1 3001 ? 100.880 81.064  94.844  1.00 54.81  ? 3001 ASP A CG    1 
ATOM   12298 O  OD1   . ASP A 1 3001 ? 100.694 82.250  95.186  1.00 50.12  ? 3001 ASP A OD1   1 
ATOM   12299 O  OD2   . ASP A 1 3001 ? 100.404 80.095  95.472  1.00 58.82  ? 3001 ASP A OD2   1 
ATOM   12300 N  N     . SER A 1 3002 ? 102.738 83.490  94.790  1.00 43.12  ? 3002 SER A N     1 
ATOM   12301 C  CA    . SER A 1 3002 ? 103.612 84.238  95.688  1.00 44.72  ? 3002 SER A CA    1 
ATOM   12302 C  C     . SER A 1 3002 ? 104.408 83.332  96.619  1.00 42.22  ? 3002 SER A C     1 
ATOM   12303 O  O     . SER A 1 3002 ? 105.472 83.740  97.102  1.00 45.76  ? 3002 SER A O     1 
ATOM   12304 C  CB    . SER A 1 3002 ? 102.791 85.234  96.508  1.00 44.66  ? 3002 SER A CB    1 
ATOM   12305 O  OG    . SER A 1 3002 ? 101.894 84.562  97.375  1.00 42.58  ? 3002 SER A OG    1 
ATOM   12306 N  N     . GLY A 1 3003 ? 103.918 82.120  96.889  1.00 33.21  ? 3003 GLY A N     1 
ATOM   12307 C  CA    . GLY A 1 3003 ? 104.681 81.170  97.680  1.00 33.03  ? 3003 GLY A CA    1 
ATOM   12308 C  C     . GLY A 1 3003 ? 105.985 80.759  97.034  1.00 28.38  ? 3003 GLY A C     1 
ATOM   12309 O  O     . GLY A 1 3003 ? 106.963 80.491  97.745  1.00 21.46  ? 3003 GLY A O     1 
ATOM   12310 N  N     . PHE A 1 3004 ? 106.016 80.698  95.700  1.00 27.84  ? 3004 PHE A N     1 
ATOM   12311 C  CA    . PHE A 1 3004 ? 107.267 80.467  94.989  1.00 25.29  ? 3004 PHE A CA    1 
ATOM   12312 C  C     . PHE A 1 3004 ? 108.305 81.489  95.424  1.00 22.30  ? 3004 PHE A C     1 
ATOM   12313 O  O     . PHE A 1 3004 ? 109.438 81.145  95.782  1.00 20.63  ? 3004 PHE A O     1 
ATOM   12314 C  CB    . PHE A 1 3004 ? 107.044 80.588  93.481  1.00 27.03  ? 3004 PHE A CB    1 
ATOM   12315 C  CG    . PHE A 1 3004 ? 106.180 79.513  92.896  1.00 26.57  ? 3004 PHE A CG    1 
ATOM   12316 C  CD1   . PHE A 1 3004 ? 105.887 78.365  93.601  1.00 28.88  ? 3004 PHE A CD1   1 
ATOM   12317 C  CD2   . PHE A 1 3004 ? 105.658 79.660  91.625  1.00 35.67  ? 3004 PHE A CD2   1 
ATOM   12318 C  CE1   . PHE A 1 3004 ? 105.073 77.397  93.053  1.00 26.29  ? 3004 PHE A CE1   1 
ATOM   12319 C  CE2   . PHE A 1 3004 ? 104.857 78.685  91.070  1.00 36.28  ? 3004 PHE A CE2   1 
ATOM   12320 C  CZ    . PHE A 1 3004 ? 104.569 77.550  91.784  1.00 28.72  ? 3004 PHE A CZ    1 
ATOM   12321 N  N     . LEU A 1 3005 ? 107.910 82.763  95.415  1.00 24.56  ? 3005 LEU A N     1 
ATOM   12322 C  CA    . LEU A 1 3005 ? 108.805 83.852  95.779  1.00 24.66  ? 3005 LEU A CA    1 
ATOM   12323 C  C     . LEU A 1 3005 ? 109.143 83.830  97.261  1.00 21.61  ? 3005 LEU A C     1 
ATOM   12324 O  O     . LEU A 1 3005 ? 110.257 84.198  97.641  1.00 23.58  ? 3005 LEU A O     1 
ATOM   12325 C  CB    . LEU A 1 3005 ? 108.160 85.181  95.399  1.00 32.29  ? 3005 LEU A CB    1 
ATOM   12326 C  CG    . LEU A 1 3005 ? 107.993 85.358  93.893  1.00 40.96  ? 3005 LEU A CG    1 
ATOM   12327 C  CD1   . LEU A 1 3005 ? 107.223 86.619  93.598  1.00 42.61  ? 3005 LEU A CD1   1 
ATOM   12328 C  CD2   . LEU A 1 3005 ? 109.347 85.383  93.206  1.00 38.25  ? 3005 LEU A CD2   1 
ATOM   12329 N  N     . GLU A 1 3006 ? 108.201 83.415  98.109  1.00 21.97  ? 3006 GLU A N     1 
ATOM   12330 C  CA    . GLU A 1 3006 ? 108.509 83.291  99.530  1.00 19.72  ? 3006 GLU A CA    1 
ATOM   12331 C  C     . GLU A 1 3006 ? 109.594 82.247  99.769  1.00 17.25  ? 3006 GLU A C     1 
ATOM   12332 O  O     . GLU A 1 3006 ? 110.502 82.463  100.580 1.00 17.89  ? 3006 GLU A O     1 
ATOM   12333 C  CB    . GLU A 1 3006 ? 107.246 82.947  100.318 1.00 25.09  ? 3006 GLU A CB    1 
ATOM   12334 C  CG    . GLU A 1 3006 ? 107.297 83.379  101.773 1.00 24.17  ? 3006 GLU A CG    1 
ATOM   12335 C  CD    . GLU A 1 3006 ? 105.973 83.191  102.483 1.00 39.66  ? 3006 GLU A CD    1 
ATOM   12336 O  OE1   . GLU A 1 3006 ? 105.022 82.693  101.846 1.00 49.84  ? 3006 GLU A OE1   1 
ATOM   12337 O  OE2   . GLU A 1 3006 ? 105.883 83.540  103.679 1.00 31.51  ? 3006 GLU A OE2   1 
ATOM   12338 N  N     . ARG A 1 3007 ? 109.511 81.107  99.079  1.00 16.30  ? 3007 ARG A N     1 
ATOM   12339 C  CA    . ARG A 1 3007 ? 110.564 80.100  99.185  1.00 14.38  ? 3007 ARG A CA    1 
ATOM   12340 C  C     . ARG A 1 3007 ? 111.881 80.619  98.616  1.00 13.28  ? 3007 ARG A C     1 
ATOM   12341 O  O     . ARG A 1 3007 ? 112.952 80.417  99.208  1.00 13.35  ? 3007 ARG A O     1 
ATOM   12342 C  CB    . ARG A 1 3007 ? 110.141 78.823  98.459  1.00 17.04  ? 3007 ARG A CB    1 
ATOM   12343 C  CG    . ARG A 1 3007 ? 108.882 78.164  99.003  1.00 13.84  ? 3007 ARG A CG    1 
ATOM   12344 C  CD    . ARG A 1 3007 ? 109.097 77.519  100.361 1.00 21.24  ? 3007 ARG A CD    1 
ATOM   12345 N  NE    . ARG A 1 3007 ? 108.353 76.270  100.478 1.00 24.76  ? 3007 ARG A NE    1 
ATOM   12346 C  CZ    . ARG A 1 3007 ? 108.336 75.503  101.560 1.00 22.88  ? 3007 ARG A CZ    1 
ATOM   12347 N  NH1   . ARG A 1 3007 ? 108.998 75.837  102.655 1.00 20.88  ? 3007 ARG A NH1   1 
ATOM   12348 N  NH2   . ARG A 1 3007 ? 107.631 74.375  101.544 1.00 26.72  ? 3007 ARG A NH2   1 
ATOM   12349 N  N     . MET A 1 3008 ? 111.813 81.294  97.463  1.00 12.99  ? 3008 MET A N     1 
ATOM   12350 C  CA    . MET A 1 3008 ? 113.015 81.777  96.794  1.00 14.30  ? 3008 MET A CA    1 
ATOM   12351 C  C     . MET A 1 3008 ? 113.734 82.837  97.616  1.00 12.88  ? 3008 MET A C     1 
ATOM   12352 O  O     . MET A 1 3008 ? 114.964 82.890  97.605  1.00 13.61  ? 3008 MET A O     1 
ATOM   12353 C  CB    . MET A 1 3008 ? 112.655 82.332  95.416  1.00 14.73  ? 3008 MET A CB    1 
ATOM   12354 C  CG    . MET A 1 3008 ? 112.365 81.267  94.372  1.00 19.03  ? 3008 MET A CG    1 
ATOM   12355 S  SD    . MET A 1 3008 ? 113.547 79.907  94.363  1.00 36.88  ? 3008 MET A SD    1 
ATOM   12356 C  CE    . MET A 1 3008 ? 114.946 80.688  93.566  1.00 13.34  ? 3008 MET A CE    1 
ATOM   12357 N  N     . ASN A 1 3009 ? 112.988 83.694  98.317  1.00 13.09  ? 3009 ASN A N     1 
ATOM   12358 C  CA    . ASN A 1 3009 ? 113.604 84.715  99.158  1.00 13.42  ? 3009 ASN A CA    1 
ATOM   12359 C  C     . ASN A 1 3009 ? 114.481 84.084  100.232 1.00 12.65  ? 3009 ASN A C     1 
ATOM   12360 O  O     . ASN A 1 3009 ? 115.646 84.469  100.406 1.00 13.59  ? 3009 ASN A O     1 
ATOM   12361 C  CB    . ASN A 1 3009 ? 112.513 85.576  99.794  1.00 14.02  ? 3009 ASN A CB    1 
ATOM   12362 C  CG    . ASN A 1 3009 ? 113.052 86.845  100.414 1.00 16.75  ? 3009 ASN A CG    1 
ATOM   12363 O  OD1   . ASN A 1 3009 ? 113.519 87.740  99.714  1.00 21.08  ? 3009 ASN A OD1   1 
ATOM   12364 N  ND2   . ASN A 1 3009 ? 112.991 86.930  101.737 1.00 12.59  ? 3009 ASN A ND2   1 
ATOM   12365 N  N     . THR A 1 3010 ? 113.937 83.103  100.955 1.00 12.74  ? 3010 THR A N     1 
ATOM   12366 C  CA    . THR A 1 3010 ? 114.708 82.417  101.984 1.00 12.65  ? 3010 THR A CA    1 
ATOM   12367 C  C     . THR A 1 3010 ? 115.892 81.673  101.382 1.00 11.48  ? 3010 THR A C     1 
ATOM   12368 O  O     . THR A 1 3010 ? 116.994 81.698  101.942 1.00 10.23  ? 3010 THR A O     1 
ATOM   12369 C  CB    . THR A 1 3010 ? 113.810 81.456  102.761 1.00 11.51  ? 3010 THR A CB    1 
ATOM   12370 O  OG1   . THR A 1 3010 ? 112.558 82.092  103.043 1.00 21.40  ? 3010 THR A OG1   1 
ATOM   12371 C  CG2   . THR A 1 3010 ? 114.470 81.054  104.070 1.00 12.47  ? 3010 THR A CG2   1 
ATOM   12372 N  N     . LEU A 1 3011 ? 115.686 81.005  100.242 1.00 11.82  ? 3011 LEU A N     1 
ATOM   12373 C  CA    . LEU A 1 3011 ? 116.787 80.265  99.630  1.00 10.06  ? 3011 LEU A CA    1 
ATOM   12374 C  C     . LEU A 1 3011 ? 117.909 81.201  99.191  1.00 11.13  ? 3011 LEU A C     1 
ATOM   12375 O  O     . LEU A 1 3011 ? 119.092 80.882  99.355  1.00 12.06  ? 3011 LEU A O     1 
ATOM   12376 C  CB    . LEU A 1 3011 ? 116.276 79.436  98.451  1.00 10.63  ? 3011 LEU A CB    1 
ATOM   12377 C  CG    . LEU A 1 3011 ? 117.335 78.613  97.715  1.00 8.74   ? 3011 LEU A CG    1 
ATOM   12378 C  CD1   . LEU A 1 3011 ? 118.109 77.738  98.688  1.00 9.11   ? 3011 LEU A CD1   1 
ATOM   12379 C  CD2   . LEU A 1 3011 ? 116.693 77.767  96.629  1.00 8.86   ? 3011 LEU A CD2   1 
ATOM   12380 N  N     . LEU A 1 3012 ? 117.559 82.360  98.627  1.00 10.02  ? 3012 LEU A N     1 
ATOM   12381 C  CA    . LEU A 1 3012 ? 118.570 83.330  98.218  1.00 9.03   ? 3012 LEU A CA    1 
ATOM   12382 C  C     . LEU A 1 3012 ? 119.319 83.886  99.419  1.00 8.81   ? 3012 LEU A C     1 
ATOM   12383 O  O     . LEU A 1 3012 ? 120.549 84.009  99.389  1.00 9.86   ? 3012 LEU A O     1 
ATOM   12384 C  CB    . LEU A 1 3012 ? 117.925 84.474  97.435  1.00 11.22  ? 3012 LEU A CB    1 
ATOM   12385 C  CG    . LEU A 1 3012 ? 117.348 84.218  96.042  1.00 10.11  ? 3012 LEU A CG    1 
ATOM   12386 C  CD1   . LEU A 1 3012 ? 116.440 85.367  95.630  1.00 13.18  ? 3012 LEU A CD1   1 
ATOM   12387 C  CD2   . LEU A 1 3012 ? 118.442 83.992  95.014  1.00 6.05   ? 3012 LEU A CD2   1 
ATOM   12388 N  N     . ALA A 1 3013 ? 118.595 84.235  100.483 1.00 11.86  ? 3013 ALA A N     1 
ATOM   12389 C  CA    . ALA A 1 3013 ? 119.233 84.918  101.602 1.00 11.13  ? 3013 ALA A CA    1 
ATOM   12390 C  C     . ALA A 1 3013 ? 120.080 83.975  102.452 1.00 11.66  ? 3013 ALA A C     1 
ATOM   12391 O  O     . ALA A 1 3013 ? 121.192 84.334  102.852 1.00 12.29  ? 3013 ALA A O     1 
ATOM   12392 C  CB    . ALA A 1 3013 ? 118.177 85.607  102.458 1.00 9.82   ? 3013 ALA A CB    1 
ATOM   12393 N  N     . ASN A 1 3014 ? 119.582 82.771  102.738 1.00 12.79  ? 3014 ASN A N     1 
ATOM   12394 C  CA    . ASN A 1 3014 ? 120.243 81.884  103.685 1.00 13.90  ? 3014 ASN A CA    1 
ATOM   12395 C  C     . ASN A 1 3014 ? 120.754 80.587  103.075 1.00 15.33  ? 3014 ASN A C     1 
ATOM   12396 O  O     . ASN A 1 3014 ? 121.514 79.873  103.738 1.00 14.88  ? 3014 ASN A O     1 
ATOM   12397 C  CB    . ASN A 1 3014 ? 119.293 81.546  104.845 1.00 12.11  ? 3014 ASN A CB    1 
ATOM   12398 C  CG    . ASN A 1 3014 ? 118.745 82.782  105.528 1.00 19.59  ? 3014 ASN A CG    1 
ATOM   12399 O  OD1   . ASN A 1 3014 ? 119.498 83.586  106.077 1.00 20.05  ? 3014 ASN A OD1   1 
ATOM   12400 N  ND2   . ASN A 1 3014 ? 117.427 82.939  105.499 1.00 17.22  ? 3014 ASN A ND2   1 
ATOM   12401 N  N     . GLY A 1 3015 ? 120.368 80.261  101.844 1.00 14.92  ? 3015 GLY A N     1 
ATOM   12402 C  CA    . GLY A 1 3015 ? 120.758 78.983  101.283 1.00 10.60  ? 3015 GLY A CA    1 
ATOM   12403 C  C     . GLY A 1 3015 ? 120.057 77.798  101.901 1.00 11.00  ? 3015 GLY A C     1 
ATOM   12404 O  O     . GLY A 1 3015 ? 120.543 76.671  101.785 1.00 13.75  ? 3015 GLY A O     1 
ATOM   12405 N  N     . GLU A 1 3016 ? 118.927 78.023  102.565 1.00 13.91  ? 3016 GLU A N     1 
ATOM   12406 C  CA    . GLU A 1 3016 ? 118.180 76.952  103.205 1.00 13.29  ? 3016 GLU A CA    1 
ATOM   12407 C  C     . GLU A 1 3016 ? 116.722 77.372  103.305 1.00 15.57  ? 3016 GLU A C     1 
ATOM   12408 O  O     . GLU A 1 3016 ? 116.411 78.561  103.410 1.00 14.83  ? 3016 GLU A O     1 
ATOM   12409 C  CB    . GLU A 1 3016 ? 118.741 76.625  104.594 1.00 14.68  ? 3016 GLU A CB    1 
ATOM   12410 C  CG    . GLU A 1 3016 ? 118.591 77.754  105.602 1.00 20.75  ? 3016 GLU A CG    1 
ATOM   12411 C  CD    . GLU A 1 3016 ? 119.210 77.429  106.946 1.00 29.38  ? 3016 GLU A CD    1 
ATOM   12412 O  OE1   . GLU A 1 3016 ? 119.781 76.328  107.090 1.00 40.47  ? 3016 GLU A OE1   1 
ATOM   12413 O  OE2   . GLU A 1 3016 ? 119.127 78.277  107.859 1.00 35.61  ? 3016 GLU A OE2   1 
ATOM   12414 N  N     . VAL A 1 3017 ? 115.835 76.384  103.260 1.00 13.83  ? 3017 VAL A N     1 
ATOM   12415 C  CA    . VAL A 1 3017 ? 114.403 76.616  103.426 1.00 10.93  ? 3017 VAL A CA    1 
ATOM   12416 C  C     . VAL A 1 3017 ? 113.949 75.852  104.664 1.00 16.26  ? 3017 VAL A C     1 
ATOM   12417 O  O     . VAL A 1 3017 ? 114.035 74.616  104.692 1.00 21.27  ? 3017 VAL A O     1 
ATOM   12418 C  CB    . VAL A 1 3017 ? 113.617 76.196  102.175 1.00 13.33  ? 3017 VAL A CB    1 
ATOM   12419 C  CG1   . VAL A 1 3017 ? 112.155 76.570  102.321 1.00 17.00  ? 3017 VAL A CG1   1 
ATOM   12420 C  CG2   . VAL A 1 3017 ? 114.214 76.840  100.932 1.00 9.49   ? 3017 VAL A CG2   1 
ATOM   12421 N  N     . PRO A 1 3018 ? 113.481 76.543  105.710 1.00 20.29  ? 3018 PRO A N     1 
ATOM   12422 C  CA    . PRO A 1 3018 ? 113.228 75.856  106.992 1.00 18.08  ? 3018 PRO A CA    1 
ATOM   12423 C  C     . PRO A 1 3018 ? 112.249 74.697  106.903 1.00 17.48  ? 3018 PRO A C     1 
ATOM   12424 O  O     . PRO A 1 3018 ? 112.465 73.664  107.548 1.00 21.76  ? 3018 PRO A O     1 
ATOM   12425 C  CB    . PRO A 1 3018 ? 112.685 76.979  107.893 1.00 19.98  ? 3018 PRO A CB    1 
ATOM   12426 C  CG    . PRO A 1 3018 ? 112.365 78.126  106.975 1.00 24.58  ? 3018 PRO A CG    1 
ATOM   12427 C  CD    . PRO A 1 3018 ? 113.274 77.996  105.803 1.00 23.13  ? 3018 PRO A CD    1 
ATOM   12428 N  N     . GLY A 1 3019 ? 111.177 74.832  106.125 1.00 15.90  ? 3019 GLY A N     1 
ATOM   12429 C  CA    . GLY A 1 3019 ? 110.158 73.804  106.041 1.00 21.24  ? 3019 GLY A CA    1 
ATOM   12430 C  C     . GLY A 1 3019 ? 110.138 72.977  104.777 1.00 21.41  ? 3019 GLY A C     1 
ATOM   12431 O  O     . GLY A 1 3019 ? 109.185 72.212  104.575 1.00 24.12  ? 3019 GLY A O     1 
ATOM   12432 N  N     . LEU A 1 3020 ? 111.147 73.093  103.911 1.00 12.87  ? 3020 LEU A N     1 
ATOM   12433 C  CA    . LEU A 1 3020 ? 111.111 72.383  102.636 1.00 12.71  ? 3020 LEU A CA    1 
ATOM   12434 C  C     . LEU A 1 3020 ? 111.227 70.875  102.829 1.00 11.33  ? 3020 LEU A C     1 
ATOM   12435 O  O     . LEU A 1 3020 ? 110.505 70.105  102.185 1.00 11.09  ? 3020 LEU A O     1 
ATOM   12436 C  CB    . LEU A 1 3020 ? 112.223 72.895  101.722 1.00 12.40  ? 3020 LEU A CB    1 
ATOM   12437 C  CG    . LEU A 1 3020 ? 112.152 72.444  100.264 1.00 8.52   ? 3020 LEU A CG    1 
ATOM   12438 C  CD1   . LEU A 1 3020 ? 110.872 72.938  99.610  1.00 9.99   ? 3020 LEU A CD1   1 
ATOM   12439 C  CD2   . LEU A 1 3020 ? 113.367 72.927  99.499  1.00 7.81   ? 3020 LEU A CD2   1 
ATOM   12440 N  N     . PHE A 1 3021 ? 112.125 70.434  103.706 1.00 10.65  ? 3021 PHE A N     1 
ATOM   12441 C  CA    . PHE A 1 3021 ? 112.355 69.014  103.955 1.00 10.17  ? 3021 PHE A CA    1 
ATOM   12442 C  C     . PHE A 1 3021 ? 111.649 68.625  105.249 1.00 14.07  ? 3021 PHE A C     1 
ATOM   12443 O  O     . PHE A 1 3021 ? 112.036 69.072  106.334 1.00 15.73  ? 3021 PHE A O     1 
ATOM   12444 C  CB    . PHE A 1 3021 ? 113.850 68.711  104.031 1.00 8.45   ? 3021 PHE A CB    1 
ATOM   12445 C  CG    . PHE A 1 3021 ? 114.577 68.906  102.730 1.00 9.03   ? 3021 PHE A CG    1 
ATOM   12446 C  CD1   . PHE A 1 3021 ? 114.679 67.871  101.816 1.00 7.06   ? 3021 PHE A CD1   1 
ATOM   12447 C  CD2   . PHE A 1 3021 ? 115.165 70.123  102.426 1.00 8.30   ? 3021 PHE A CD2   1 
ATOM   12448 C  CE1   . PHE A 1 3021 ? 115.349 68.046  100.621 1.00 7.83   ? 3021 PHE A CE1   1 
ATOM   12449 C  CE2   . PHE A 1 3021 ? 115.838 70.304  101.232 1.00 7.91   ? 3021 PHE A CE2   1 
ATOM   12450 C  CZ    . PHE A 1 3021 ? 115.930 69.265  100.329 1.00 7.42   ? 3021 PHE A CZ    1 
ATOM   12451 N  N     . GLU A 1 3022 ? 110.617 67.791  105.134 1.00 16.21  ? 3022 GLU A N     1 
ATOM   12452 C  CA    . GLU A 1 3022 ? 109.838 67.362  106.286 1.00 19.20  ? 3022 GLU A CA    1 
ATOM   12453 C  C     . GLU A 1 3022 ? 109.495 65.886  106.153 1.00 20.05  ? 3022 GLU A C     1 
ATOM   12454 O  O     . GLU A 1 3022 ? 109.342 65.365  105.045 1.00 20.85  ? 3022 GLU A O     1 
ATOM   12455 C  CB    . GLU A 1 3022 ? 108.553 68.188  106.431 1.00 19.57  ? 3022 GLU A CB    1 
ATOM   12456 C  CG    . GLU A 1 3022 ? 108.695 69.410  107.322 1.00 26.93  ? 3022 GLU A CG    1 
ATOM   12457 C  CD    . GLU A 1 3022 ? 107.677 70.486  107.001 1.00 38.45  ? 3022 GLU A CD    1 
ATOM   12458 O  OE1   . GLU A 1 3022 ? 106.887 70.294  106.053 1.00 34.40  ? 3022 GLU A OE1   1 
ATOM   12459 O  OE2   . GLU A 1 3022 ? 107.667 71.524  107.695 1.00 41.72  ? 3022 GLU A OE2   1 
ATOM   12460 N  N     . GLY A 1 3023 ? 109.373 65.220  107.297 1.00 18.04  ? 3023 GLY A N     1 
ATOM   12461 C  CA    . GLY A 1 3023 ? 108.964 63.823  107.300 1.00 15.68  ? 3023 GLY A CA    1 
ATOM   12462 C  C     . GLY A 1 3023 ? 110.022 62.924  106.691 1.00 18.31  ? 3023 GLY A C     1 
ATOM   12463 O  O     . GLY A 1 3023 ? 111.205 62.987  107.046 1.00 18.28  ? 3023 GLY A O     1 
ATOM   12464 N  N     . ASP A 1 3024 ? 109.591 62.065  105.762 1.00 18.94  ? 3024 ASP A N     1 
ATOM   12465 C  CA    . ASP A 1 3024 ? 110.515 61.142  105.110 1.00 16.33  ? 3024 ASP A CA    1 
ATOM   12466 C  C     . ASP A 1 3024 ? 111.551 61.880  104.274 1.00 15.73  ? 3024 ASP A C     1 
ATOM   12467 O  O     . ASP A 1 3024 ? 112.681 61.398  104.119 1.00 14.55  ? 3024 ASP A O     1 
ATOM   12468 C  CB    . ASP A 1 3024 ? 109.740 60.155  104.237 1.00 16.83  ? 3024 ASP A CB    1 
ATOM   12469 C  CG    . ASP A 1 3024 ? 108.974 59.132  105.052 1.00 23.19  ? 3024 ASP A CG    1 
ATOM   12470 O  OD1   . ASP A 1 3024 ? 109.291 58.962  106.247 1.00 28.16  ? 3024 ASP A OD1   1 
ATOM   12471 O  OD2   . ASP A 1 3024 ? 108.051 58.501  104.496 1.00 22.47  ? 3024 ASP A OD2   1 
ATOM   12472 N  N     . GLU A 1 3025 ? 111.184 63.042  103.728 1.00 15.14  ? 3025 GLU A N     1 
ATOM   12473 C  CA    . GLU A 1 3025 ? 112.133 63.825  102.946 1.00 13.92  ? 3025 GLU A CA    1 
ATOM   12474 C  C     . GLU A 1 3025 ? 113.316 64.260  103.797 1.00 13.51  ? 3025 GLU A C     1 
ATOM   12475 O  O     . GLU A 1 3025 ? 114.462 64.232  103.337 1.00 13.51  ? 3025 GLU A O     1 
ATOM   12476 C  CB    . GLU A 1 3025 ? 111.435 65.041  102.335 1.00 14.00  ? 3025 GLU A CB    1 
ATOM   12477 C  CG    . GLU A 1 3025 ? 110.174 64.709  101.557 1.00 18.92  ? 3025 GLU A CG    1 
ATOM   12478 C  CD    . GLU A 1 3025 ? 110.440 64.477  100.083 1.00 27.25  ? 3025 GLU A CD    1 
ATOM   12479 O  OE1   . GLU A 1 3025 ? 111.535 63.981  99.743  1.00 29.20  ? 3025 GLU A OE1   1 
ATOM   12480 O  OE2   . GLU A 1 3025 ? 109.554 64.791  99.262  1.00 38.63  ? 3025 GLU A OE2   1 
ATOM   12481 N  N     . TYR A 1 3026 ? 113.061 64.660  105.046 1.00 11.35  ? 3026 TYR A N     1 
ATOM   12482 C  CA    . TYR A 1 3026 ? 114.154 65.063  105.924 1.00 10.03  ? 3026 TYR A CA    1 
ATOM   12483 C  C     . TYR A 1 3026 ? 115.064 63.887  106.258 1.00 11.41  ? 3026 TYR A C     1 
ATOM   12484 O  O     . TYR A 1 3026 ? 116.286 64.048  106.323 1.00 11.69  ? 3026 TYR A O     1 
ATOM   12485 C  CB    . TYR A 1 3026 ? 113.607 65.699  107.201 1.00 10.58  ? 3026 TYR A CB    1 
ATOM   12486 C  CG    . TYR A 1 3026 ? 114.669 66.386  108.032 1.00 9.69   ? 3026 TYR A CG    1 
ATOM   12487 C  CD1   . TYR A 1 3026 ? 115.096 67.671  107.724 1.00 9.54   ? 3026 TYR A CD1   1 
ATOM   12488 C  CD2   . TYR A 1 3026 ? 115.246 65.748  109.123 1.00 9.70   ? 3026 TYR A CD2   1 
ATOM   12489 C  CE1   . TYR A 1 3026 ? 116.067 68.302  108.479 1.00 13.36  ? 3026 TYR A CE1   1 
ATOM   12490 C  CE2   . TYR A 1 3026 ? 116.217 66.372  109.884 1.00 9.44   ? 3026 TYR A CE2   1 
ATOM   12491 C  CZ    . TYR A 1 3026 ? 116.624 67.648  109.557 1.00 14.42  ? 3026 TYR A CZ    1 
ATOM   12492 O  OH    . TYR A 1 3026 ? 117.591 68.272  110.312 1.00 19.98  ? 3026 TYR A OH    1 
ATOM   12493 N  N     . ALA A 1 3027 ? 114.494 62.700  106.480 1.00 11.14  ? 3027 ALA A N     1 
ATOM   12494 C  CA    . ALA A 1 3027 ? 115.321 61.529  106.761 1.00 13.02  ? 3027 ALA A CA    1 
ATOM   12495 C  C     . ALA A 1 3027 ? 116.180 61.152  105.558 1.00 11.28  ? 3027 ALA A C     1 
ATOM   12496 O  O     . ALA A 1 3027 ? 117.370 60.837  105.707 1.00 11.82  ? 3027 ALA A O     1 
ATOM   12497 C  CB    . ALA A 1 3027 ? 114.441 60.354  107.184 1.00 13.53  ? 3027 ALA A CB    1 
ATOM   12498 N  N     . THR A 1 3028 ? 115.594 61.179  104.358 1.00 10.70  ? 3028 THR A N     1 
ATOM   12499 C  CA    . THR A 1 3028 ? 116.370 60.910  103.152 1.00 12.44  ? 3028 THR A CA    1 
ATOM   12500 C  C     . THR A 1 3028 ? 117.465 61.955  102.966 1.00 12.02  ? 3028 THR A C     1 
ATOM   12501 O  O     . THR A 1 3028 ? 118.594 61.623  102.583 1.00 11.07  ? 3028 THR A O     1 
ATOM   12502 C  CB    . THR A 1 3028 ? 115.448 60.869  101.933 1.00 13.77  ? 3028 THR A CB    1 
ATOM   12503 O  OG1   . THR A 1 3028 ? 114.474 59.832  102.105 1.00 15.74  ? 3028 THR A OG1   1 
ATOM   12504 C  CG2   . THR A 1 3028 ? 116.242 60.599  100.665 1.00 17.27  ? 3028 THR A CG2   1 
ATOM   12505 N  N     . LEU A 1 3029 ? 117.147 63.223  103.241 1.00 10.83  ? 3029 LEU A N     1 
ATOM   12506 C  CA    . LEU A 1 3029 ? 118.149 64.278  103.167 1.00 11.43  ? 3029 LEU A CA    1 
ATOM   12507 C  C     . LEU A 1 3029 ? 119.275 64.037  104.160 1.00 10.55  ? 3029 LEU A C     1 
ATOM   12508 O  O     . LEU A 1 3029 ? 120.445 64.266  103.846 1.00 11.61  ? 3029 LEU A O     1 
ATOM   12509 C  CB    . LEU A 1 3029 ? 117.501 65.640  103.422 1.00 10.59  ? 3029 LEU A CB    1 
ATOM   12510 C  CG    . LEU A 1 3029 ? 118.450 66.842  103.417 1.00 7.34   ? 3029 LEU A CG    1 
ATOM   12511 C  CD1   . LEU A 1 3029 ? 119.032 67.059  102.032 1.00 7.12   ? 3029 LEU A CD1   1 
ATOM   12512 C  CD2   . LEU A 1 3029 ? 117.749 68.096  103.910 1.00 8.01   ? 3029 LEU A CD2   1 
ATOM   12513 N  N     . MET A 1 3030 ? 118.938 63.593  105.372 1.00 9.36   ? 3030 MET A N     1 
ATOM   12514 C  CA    . MET A 1 3030 ? 119.968 63.312  106.365 1.00 10.47  ? 3030 MET A CA    1 
ATOM   12515 C  C     . MET A 1 3030 ? 120.876 62.179  105.909 1.00 11.37  ? 3030 MET A C     1 
ATOM   12516 O  O     . MET A 1 3030 ? 122.101 62.260  106.051 1.00 13.08  ? 3030 MET A O     1 
ATOM   12517 C  CB    . MET A 1 3030 ? 119.333 62.984  107.716 1.00 10.47  ? 3030 MET A CB    1 
ATOM   12518 C  CG    . MET A 1 3030 ? 118.592 64.136  108.407 1.00 13.49  ? 3030 MET A CG    1 
ATOM   12519 S  SD    . MET A 1 3030 ? 119.577 65.521  109.036 1.00 19.66  ? 3030 MET A SD    1 
ATOM   12520 C  CE    . MET A 1 3030 ? 119.946 66.479  107.565 1.00 11.88  ? 3030 MET A CE    1 
ATOM   12521 N  N     . THR A 1 3031 ? 120.291 61.118  105.350 1.00 11.65  ? 3031 THR A N     1 
ATOM   12522 C  CA    . THR A 1 3031 ? 121.101 60.016  104.837 1.00 14.01  ? 3031 THR A CA    1 
ATOM   12523 C  C     . THR A 1 3031 ? 122.026 60.485  103.716 1.00 15.69  ? 3031 THR A C     1 
ATOM   12524 O  O     . THR A 1 3031 ? 123.224 60.161  103.702 1.00 17.91  ? 3031 THR A O     1 
ATOM   12525 C  CB    . THR A 1 3031 ? 120.191 58.889  104.347 1.00 16.30  ? 3031 THR A CB    1 
ATOM   12526 O  OG1   . THR A 1 3031 ? 119.316 58.485  105.408 1.00 16.33  ? 3031 THR A OG1   1 
ATOM   12527 C  CG2   . THR A 1 3031 ? 121.012 57.693  103.894 1.00 16.21  ? 3031 THR A CG2   1 
ATOM   12528 N  N     . GLN A 1 3032 ? 121.488 61.268  102.776 1.00 13.24  ? 3032 GLN A N     1 
ATOM   12529 C  CA    . GLN A 1 3032 ? 122.292 61.743  101.657 1.00 13.72  ? 3032 GLN A CA    1 
ATOM   12530 C  C     . GLN A 1 3032 ? 123.380 62.706  102.114 1.00 16.17  ? 3032 GLN A C     1 
ATOM   12531 O  O     . GLN A 1 3032 ? 124.496 62.672  101.587 1.00 17.01  ? 3032 GLN A O     1 
ATOM   12532 C  CB    . GLN A 1 3032 ? 121.394 62.400  100.611 1.00 15.76  ? 3032 GLN A CB    1 
ATOM   12533 C  CG    . GLN A 1 3032 ? 120.432 61.431  99.944  1.00 14.85  ? 3032 GLN A CG    1 
ATOM   12534 C  CD    . GLN A 1 3032 ? 119.516 62.108  98.947  1.00 20.39  ? 3032 GLN A CD    1 
ATOM   12535 O  OE1   . GLN A 1 3032 ? 119.554 63.327  98.780  1.00 27.32  ? 3032 GLN A OE1   1 
ATOM   12536 N  NE2   . GLN A 1 3032 ? 118.675 61.321  98.287  1.00 26.49  ? 3032 GLN A NE2   1 
ATOM   12537 N  N     . CYS A 1 3033 ? 123.086 63.558  103.097 1.00 14.81  ? 3033 CYS A N     1 
ATOM   12538 C  CA    . CYS A 1 3033 ? 124.101 64.465  103.617 1.00 13.83  ? 3033 CYS A CA    1 
ATOM   12539 C  C     . CYS A 1 3033 ? 125.184 63.702  104.367 1.00 12.34  ? 3033 CYS A C     1 
ATOM   12540 O  O     . CYS A 1 3033 ? 126.360 64.068  104.302 1.00 14.53  ? 3033 CYS A O     1 
ATOM   12541 C  CB    . CYS A 1 3033 ? 123.458 65.515  104.519 1.00 11.94  ? 3033 CYS A CB    1 
ATOM   12542 S  SG    . CYS A 1 3033 ? 122.401 66.695  103.661 1.00 26.66  ? 3033 CYS A SG    1 
ATOM   12543 N  N     . LYS A 1 3034 ? 124.810 62.638  105.082 1.00 15.48  ? 3034 LYS A N     1 
ATOM   12544 C  CA    . LYS A 1 3034 ? 125.811 61.793  105.725 1.00 17.41  ? 3034 LYS A CA    1 
ATOM   12545 C  C     . LYS A 1 3034 ? 126.746 61.167  104.698 1.00 17.90  ? 3034 LYS A C     1 
ATOM   12546 O  O     . LYS A 1 3034 ? 127.976 61.226  104.845 1.00 18.78  ? 3034 LYS A O     1 
ATOM   12547 C  CB    . LYS A 1 3034 ? 125.120 60.708  106.553 1.00 20.56  ? 3034 LYS A CB    1 
ATOM   12548 C  CG    . LYS A 1 3034 ? 126.065 59.774  107.291 1.00 22.13  ? 3034 LYS A CG    1 
ATOM   12549 C  CD    . LYS A 1 3034 ? 126.808 60.489  108.403 1.00 31.34  ? 3034 LYS A CD    1 
ATOM   12550 C  CE    . LYS A 1 3034 ? 127.772 59.548  109.109 1.00 37.64  ? 3034 LYS A CE    1 
ATOM   12551 N  NZ    . LYS A 1 3034 ? 127.057 58.465  109.839 1.00 42.78  ? 3034 LYS A NZ    1 
ATOM   12552 N  N     . GLU A 1 3035 ? 126.182 60.576  103.640 1.00 18.34  ? 3035 GLU A N     1 
ATOM   12553 C  CA    . GLU A 1 3035 ? 127.025 59.907  102.652 1.00 20.25  ? 3035 GLU A CA    1 
ATOM   12554 C  C     . GLU A 1 3035 ? 127.822 60.913  101.826 1.00 25.05  ? 3035 GLU A C     1 
ATOM   12555 O  O     . GLU A 1 3035 ? 128.882 60.577  101.285 1.00 30.30  ? 3035 GLU A O     1 
ATOM   12556 C  CB    . GLU A 1 3035 ? 126.184 58.999  101.751 1.00 21.26  ? 3035 GLU A CB    1 
ATOM   12557 C  CG    . GLU A 1 3035 ? 125.116 59.697  100.930 1.00 23.56  ? 3035 GLU A CG    1 
ATOM   12558 C  CD    . GLU A 1 3035 ? 125.641 60.243  99.615  1.00 38.58  ? 3035 GLU A CD    1 
ATOM   12559 O  OE1   . GLU A 1 3035 ? 126.708 59.777  99.160  1.00 36.48  ? 3035 GLU A OE1   1 
ATOM   12560 O  OE2   . GLU A 1 3035 ? 124.988 61.138  99.036  1.00 33.99  ? 3035 GLU A OE2   1 
ATOM   12561 N  N     . GLY A 1 3036 ? 127.327 62.148  101.703 1.00 21.24  ? 3036 GLY A N     1 
ATOM   12562 C  CA    . GLY A 1 3036 ? 128.084 63.172  101.006 1.00 19.30  ? 3036 GLY A CA    1 
ATOM   12563 C  C     . GLY A 1 3036 ? 129.174 63.802  101.844 1.00 21.31  ? 3036 GLY A C     1 
ATOM   12564 O  O     . GLY A 1 3036 ? 130.212 64.203  101.311 1.00 24.52  ? 3036 GLY A O     1 
ATOM   12565 N  N     . ALA A 1 3037 ? 128.959 63.903  103.158 1.00 18.37  ? 3037 ALA A N     1 
ATOM   12566 C  CA    . ALA A 1 3037 ? 129.981 64.454  104.037 1.00 17.88  ? 3037 ALA A CA    1 
ATOM   12567 C  C     . ALA A 1 3037 ? 131.085 63.440  104.298 1.00 32.20  ? 3037 ALA A C     1 
ATOM   12568 O  O     . ALA A 1 3037 ? 132.246 63.819  104.494 1.00 36.79  ? 3037 ALA A O     1 
ATOM   12569 C  CB    . ALA A 1 3037 ? 129.351 64.918  105.350 1.00 16.09  ? 3037 ALA A CB    1 
ATOM   12570 N  N     . GLN A 1 3038 ? 130.748 62.146  104.309 1.00 31.75  ? 3038 GLN A N     1 
ATOM   12571 C  CA    . GLN A 1 3038 ? 131.799 61.143  104.444 1.00 32.66  ? 3038 GLN A CA    1 
ATOM   12572 C  C     . GLN A 1 3038 ? 132.708 61.127  103.220 1.00 34.28  ? 3038 GLN A C     1 
ATOM   12573 O  O     . GLN A 1 3038 ? 133.898 60.815  103.339 1.00 35.56  ? 3038 GLN A O     1 
ATOM   12574 C  CB    . GLN A 1 3038 ? 131.192 59.759  104.696 1.00 32.12  ? 3038 GLN A CB    1 
ATOM   12575 C  CG    . GLN A 1 3038 ? 130.582 59.083  103.480 1.00 37.66  ? 3038 GLN A CG    1 
ATOM   12576 C  CD    . GLN A 1 3038 ? 131.563 58.174  102.764 1.00 46.08  ? 3038 GLN A CD    1 
ATOM   12577 O  OE1   . GLN A 1 3038 ? 132.587 57.783  103.324 1.00 39.80  ? 3038 GLN A OE1   1 
ATOM   12578 N  NE2   . GLN A 1 3038 ? 131.254 57.835  101.517 1.00 40.18  ? 3038 GLN A NE2   1 
ATOM   12579 N  N     . LYS A 1 3039 ? 132.172 61.462  102.043 1.00 32.51  ? 3039 LYS A N     1 
ATOM   12580 C  CA    . LYS A 1 3039 ? 132.996 61.565  100.845 1.00 33.29  ? 3039 LYS A CA    1 
ATOM   12581 C  C     . LYS A 1 3039 ? 133.918 62.776  100.881 1.00 40.65  ? 3039 LYS A C     1 
ATOM   12582 O  O     . LYS A 1 3039 ? 134.942 62.781  100.190 1.00 45.00  ? 3039 LYS A O     1 
ATOM   12583 C  CB    . LYS A 1 3039 ? 132.112 61.625  99.598  1.00 31.25  ? 3039 LYS A CB    1 
ATOM   12584 C  CG    . LYS A 1 3039 ? 131.557 60.278  99.162  1.00 40.93  ? 3039 LYS A CG    1 
ATOM   12585 C  CD    . LYS A 1 3039 ? 130.393 60.435  98.194  1.00 38.32  ? 3039 LYS A CD    1 
ATOM   12586 C  CE    . LYS A 1 3039 ? 130.667 61.508  97.150  1.00 42.18  ? 3039 LYS A CE    1 
ATOM   12587 N  NZ    . LYS A 1 3039 ? 131.854 61.185  96.310  1.00 40.47  ? 3039 LYS A NZ    1 
ATOM   12588 N  N     . GLU A 1 3040 ? 133.578 63.798  101.664 1.00 42.37  ? 3040 GLU A N     1 
ATOM   12589 C  CA    . GLU A 1 3040 ? 134.396 64.996  101.781 1.00 37.41  ? 3040 GLU A CA    1 
ATOM   12590 C  C     . GLU A 1 3040 ? 135.462 64.877  102.864 1.00 46.23  ? 3040 GLU A C     1 
ATOM   12591 O  O     . GLU A 1 3040 ? 136.293 65.782  102.999 1.00 54.71  ? 3040 GLU A O     1 
ATOM   12592 C  CB    . GLU A 1 3040 ? 133.501 66.211  102.062 1.00 37.45  ? 3040 GLU A CB    1 
ATOM   12593 C  CG    . GLU A 1 3040 ? 134.119 67.558  101.714 1.00 43.37  ? 3040 GLU A CG    1 
ATOM   12594 C  CD    . GLU A 1 3040 ? 133.086 68.663  101.614 1.00 39.86  ? 3040 GLU A CD    1 
ATOM   12595 O  OE1   . GLU A 1 3040 ? 132.289 68.647  100.653 1.00 36.04  ? 3040 GLU A OE1   1 
ATOM   12596 O  OE2   . GLU A 1 3040 ? 133.071 69.548  102.496 1.00 29.72  ? 3040 GLU A OE2   1 
ATOM   12597 N  N     . GLY A 1 3041 ? 135.468 63.785  103.623 1.00 37.89  ? 3041 GLY A N     1 
ATOM   12598 C  CA    . GLY A 1 3041 ? 136.445 63.596  104.674 1.00 41.93  ? 3041 GLY A CA    1 
ATOM   12599 C  C     . GLY A 1 3041 ? 136.091 64.217  106.005 1.00 50.20  ? 3041 GLY A C     1 
ATOM   12600 O  O     . GLY A 1 3041 ? 136.987 64.419  106.833 1.00 55.08  ? 3041 GLY A O     1 
ATOM   12601 N  N     . LEU A 1 3042 ? 134.821 64.526  106.240 1.00 47.57  ? 3042 LEU A N     1 
ATOM   12602 C  CA    . LEU A 1 3042 ? 134.384 65.153  107.477 1.00 48.97  ? 3042 LEU A CA    1 
ATOM   12603 C  C     . LEU A 1 3042 ? 133.712 64.132  108.387 1.00 55.89  ? 3042 LEU A C     1 
ATOM   12604 O  O     . LEU A 1 3042 ? 133.019 63.221  107.928 1.00 50.57  ? 3042 LEU A O     1 
ATOM   12605 C  CB    . LEU A 1 3042 ? 133.423 66.308  107.191 1.00 38.75  ? 3042 LEU A CB    1 
ATOM   12606 C  CG    . LEU A 1 3042 ? 133.862 67.267  106.083 1.00 42.47  ? 3042 LEU A CG    1 
ATOM   12607 C  CD1   . LEU A 1 3042 ? 132.694 68.116  105.617 1.00 34.17  ? 3042 LEU A CD1   1 
ATOM   12608 C  CD2   . LEU A 1 3042 ? 135.010 68.144  106.558 1.00 41.16  ? 3042 LEU A CD2   1 
ATOM   12609 N  N     . MET A 1 3043 ? 133.925 64.299  109.691 1.00 55.02  ? 3043 MET A N     1 
ATOM   12610 C  CA    . MET A 1 3043 ? 133.359 63.414  110.708 1.00 56.62  ? 3043 MET A CA    1 
ATOM   12611 C  C     . MET A 1 3043 ? 132.126 64.100  111.285 1.00 56.31  ? 3043 MET A C     1 
ATOM   12612 O  O     . MET A 1 3043 ? 132.207 64.856  112.253 1.00 60.75  ? 3043 MET A O     1 
ATOM   12613 C  CB    . MET A 1 3043 ? 134.387 63.101  111.788 1.00 59.41  ? 3043 MET A CB    1 
ATOM   12614 C  CG    . MET A 1 3043 ? 135.570 62.280  111.306 1.00 65.39  ? 3043 MET A CG    1 
ATOM   12615 S  SD    . MET A 1 3043 ? 136.720 61.888  112.637 1.00 94.53  ? 3043 MET A SD    1 
ATOM   12616 C  CE    . MET A 1 3043 ? 137.510 63.477  112.878 1.00 76.32  ? 3043 MET A CE    1 
ATOM   12617 N  N     . LEU A 1 3044 ? 130.972 63.831  110.679 1.00 45.87  ? 3044 LEU A N     1 
ATOM   12618 C  CA    . LEU A 1 3044 ? 129.712 64.431  111.095 1.00 42.72  ? 3044 LEU A CA    1 
ATOM   12619 C  C     . LEU A 1 3044 ? 128.665 63.339  111.245 1.00 42.01  ? 3044 LEU A C     1 
ATOM   12620 O  O     . LEU A 1 3044 ? 128.472 62.531  110.331 1.00 34.07  ? 3044 LEU A O     1 
ATOM   12621 C  CB    . LEU A 1 3044 ? 129.244 65.480  110.082 1.00 33.73  ? 3044 LEU A CB    1 
ATOM   12622 C  CG    . LEU A 1 3044 ? 130.125 66.711  109.867 1.00 35.15  ? 3044 LEU A CG    1 
ATOM   12623 C  CD1   . LEU A 1 3044 ? 129.539 67.601  108.781 1.00 25.24  ? 3044 LEU A CD1   1 
ATOM   12624 C  CD2   . LEU A 1 3044 ? 130.297 67.486  111.160 1.00 36.14  ? 3044 LEU A CD2   1 
ATOM   12625 N  N     . ASP A 1 3045 ? 127.991 63.316  112.395 1.00 41.87  ? 3045 ASP A N     1 
ATOM   12626 C  CA    . ASP A 1 3045 ? 126.957 62.320  112.648 1.00 39.81  ? 3045 ASP A CA    1 
ATOM   12627 C  C     . ASP A 1 3045 ? 125.669 62.979  113.122 1.00 34.16  ? 3045 ASP A C     1 
ATOM   12628 O  O     . ASP A 1 3045 ? 124.573 62.469  112.869 1.00 34.27  ? 3045 ASP A O     1 
ATOM   12629 C  CB    . ASP A 1 3045 ? 127.441 61.297  113.678 1.00 48.94  ? 3045 ASP A CB    1 
ATOM   12630 C  CG    . ASP A 1 3045 ? 126.422 60.204  113.936 1.00 53.94  ? 3045 ASP A CG    1 
ATOM   12631 O  OD1   . ASP A 1 3045 ? 126.094 59.460  112.988 1.00 54.53  ? 3045 ASP A OD1   1 
ATOM   12632 O  OD2   . ASP A 1 3045 ? 125.948 60.090  115.086 1.00 51.55  ? 3045 ASP A OD2   1 
ATOM   12633 N  N     . SER A 1 3046 ? 125.791 64.111  113.810 1.00 28.56  ? 3046 SER A N     1 
ATOM   12634 C  CA    . SER A 1 3046 ? 124.622 64.814  114.316 1.00 21.70  ? 3046 SER A CA    1 
ATOM   12635 C  C     . SER A 1 3046 ? 123.811 65.410  113.171 1.00 21.37  ? 3046 SER A C     1 
ATOM   12636 O  O     . SER A 1 3046 ? 124.355 65.850  112.155 1.00 25.48  ? 3046 SER A O     1 
ATOM   12637 C  CB    . SER A 1 3046 ? 125.040 65.915  115.289 1.00 23.14  ? 3046 SER A CB    1 
ATOM   12638 O  OG    . SER A 1 3046 ? 123.963 66.795  115.557 1.00 20.11  ? 3046 SER A OG    1 
ATOM   12639 N  N     . HIS A 1 3047 ? 122.488 65.418  113.346 1.00 19.52  ? 3047 HIS A N     1 
ATOM   12640 C  CA    . HIS A 1 3047 ? 121.610 65.968  112.319 1.00 16.54  ? 3047 HIS A CA    1 
ATOM   12641 C  C     . HIS A 1 3047 ? 121.806 67.471  112.165 1.00 16.85  ? 3047 HIS A C     1 
ATOM   12642 O  O     . HIS A 1 3047 ? 121.738 67.998  111.050 1.00 20.50  ? 3047 HIS A O     1 
ATOM   12643 C  CB    . HIS A 1 3047 ? 120.152 65.644  112.644 1.00 15.21  ? 3047 HIS A CB    1 
ATOM   12644 C  CG    . HIS A 1 3047 ? 119.727 64.276  112.210 1.00 18.54  ? 3047 HIS A CG    1 
ATOM   12645 N  ND1   . HIS A 1 3047 ? 118.410 63.869  112.212 1.00 18.93  ? 3047 HIS A ND1   1 
ATOM   12646 C  CD2   . HIS A 1 3047 ? 120.445 63.222  111.756 1.00 18.86  ? 3047 HIS A CD2   1 
ATOM   12647 C  CE1   . HIS A 1 3047 ? 118.336 62.623  111.780 1.00 18.88  ? 3047 HIS A CE1   1 
ATOM   12648 N  NE2   . HIS A 1 3047 ? 119.557 62.207  111.496 1.00 18.39  ? 3047 HIS A NE2   1 
ATOM   12649 N  N     . GLU A 1 3048 ? 122.044 68.178  113.273 1.00 19.88  ? 3048 GLU A N     1 
ATOM   12650 C  CA    . GLU A 1 3048 ? 122.257 69.621  113.202 1.00 17.49  ? 3048 GLU A CA    1 
ATOM   12651 C  C     . GLU A 1 3048 ? 123.527 69.960  112.430 1.00 16.76  ? 3048 GLU A C     1 
ATOM   12652 O  O     . GLU A 1 3048 ? 123.514 70.832  111.551 1.00 18.42  ? 3048 GLU A O     1 
ATOM   12653 C  CB    . GLU A 1 3048 ? 122.314 70.204  114.614 1.00 16.82  ? 3048 GLU A CB    1 
ATOM   12654 C  CG    . GLU A 1 3048 ? 122.490 71.713  114.672 1.00 28.78  ? 3048 GLU A CG    1 
ATOM   12655 C  CD    . GLU A 1 3048 ? 121.306 72.467  114.097 1.00 37.87  ? 3048 GLU A CD    1 
ATOM   12656 O  OE1   . GLU A 1 3048 ? 120.184 71.916  114.103 1.00 45.60  ? 3048 GLU A OE1   1 
ATOM   12657 O  OE2   . GLU A 1 3048 ? 121.496 73.612  113.639 1.00 30.70  ? 3048 GLU A OE2   1 
ATOM   12658 N  N     . GLU A 1 3049 ? 124.633 69.280  112.742 1.00 16.38  ? 3049 GLU A N     1 
ATOM   12659 C  CA    . GLU A 1 3049 ? 125.892 69.538  112.049 1.00 20.18  ? 3049 GLU A CA    1 
ATOM   12660 C  C     . GLU A 1 3049 ? 125.792 69.177  110.573 1.00 17.13  ? 3049 GLU A C     1 
ATOM   12661 O  O     . GLU A 1 3049 ? 126.306 69.897  109.708 1.00 16.46  ? 3049 GLU A O     1 
ATOM   12662 C  CB    . GLU A 1 3049 ? 127.019 68.753  112.719 1.00 26.07  ? 3049 GLU A CB    1 
ATOM   12663 C  CG    . GLU A 1 3049 ? 127.704 69.492  113.855 1.00 37.30  ? 3049 GLU A CG    1 
ATOM   12664 C  CD    . GLU A 1 3049 ? 128.511 68.567  114.745 1.00 54.19  ? 3049 GLU A CD    1 
ATOM   12665 O  OE1   . GLU A 1 3049 ? 129.349 67.808  114.216 1.00 57.18  ? 3049 GLU A OE1   1 
ATOM   12666 O  OE2   . GLU A 1 3049 ? 128.304 68.596  115.976 1.00 54.37  ? 3049 GLU A OE2   1 
ATOM   12667 N  N     . LEU A 1 3050 ? 125.135 68.057  110.270 1.00 16.42  ? 3050 LEU A N     1 
ATOM   12668 C  CA    . LEU A 1 3050 ? 124.954 67.644  108.883 1.00 14.48  ? 3050 LEU A CA    1 
ATOM   12669 C  C     . LEU A 1 3050 ? 124.088 68.634  108.113 1.00 12.10  ? 3050 LEU A C     1 
ATOM   12670 O  O     . LEU A 1 3050 ? 124.371 68.942  106.950 1.00 11.73  ? 3050 LEU A O     1 
ATOM   12671 C  CB    . LEU A 1 3050 ? 124.366 66.234  108.852 1.00 17.72  ? 3050 LEU A CB    1 
ATOM   12672 C  CG    . LEU A 1 3050 ? 125.422 65.169  109.157 1.00 23.38  ? 3050 LEU A CG    1 
ATOM   12673 C  CD1   . LEU A 1 3050 ? 124.838 63.775  109.288 1.00 20.98  ? 3050 LEU A CD1   1 
ATOM   12674 C  CD2   . LEU A 1 3050 ? 126.444 65.188  108.037 1.00 21.73  ? 3050 LEU A CD2   1 
ATOM   12675 N  N     . TYR A 1 3051 ? 123.035 69.156  108.747 1.00 12.85  ? 3051 TYR A N     1 
ATOM   12676 C  CA    . TYR A 1 3051 ? 122.211 70.168  108.093 1.00 8.22   ? 3051 TYR A CA    1 
ATOM   12677 C  C     . TYR A 1 3051 ? 122.991 71.459  107.869 1.00 11.39  ? 3051 TYR A C     1 
ATOM   12678 O  O     . TYR A 1 3051 ? 122.825 72.117  106.836 1.00 11.39  ? 3051 TYR A O     1 
ATOM   12679 C  CB    . TYR A 1 3051 ? 120.950 70.440  108.912 1.00 9.15   ? 3051 TYR A CB    1 
ATOM   12680 C  CG    . TYR A 1 3051 ? 119.893 71.207  108.149 1.00 12.21  ? 3051 TYR A CG    1 
ATOM   12681 C  CD1   . TYR A 1 3051 ? 119.020 70.556  107.288 1.00 11.87  ? 3051 TYR A CD1   1 
ATOM   12682 C  CD2   . TYR A 1 3051 ? 119.778 72.586  108.278 1.00 15.21  ? 3051 TYR A CD2   1 
ATOM   12683 C  CE1   . TYR A 1 3051 ? 118.055 71.254  106.585 1.00 13.64  ? 3051 TYR A CE1   1 
ATOM   12684 C  CE2   . TYR A 1 3051 ? 118.817 73.292  107.580 1.00 17.80  ? 3051 TYR A CE2   1 
ATOM   12685 C  CZ    . TYR A 1 3051 ? 117.959 72.622  106.735 1.00 20.24  ? 3051 TYR A CZ    1 
ATOM   12686 O  OH    . TYR A 1 3051 ? 117.001 73.321  106.038 1.00 21.09  ? 3051 TYR A OH    1 
ATOM   12687 N  N     . LYS A 1 3052 ? 123.837 71.846  108.829 1.00 12.66  ? 3052 LYS A N     1 
ATOM   12688 C  CA    . LYS A 1 3052 ? 124.677 73.026  108.635 1.00 9.40   ? 3052 LYS A CA    1 
ATOM   12689 C  C     . LYS A 1 3052 ? 125.642 72.832  107.470 1.00 9.53   ? 3052 LYS A C     1 
ATOM   12690 O  O     . LYS A 1 3052 ? 125.845 73.746  106.660 1.00 12.03  ? 3052 LYS A O     1 
ATOM   12691 C  CB    . LYS A 1 3052 ? 125.448 73.344  109.916 1.00 14.28  ? 3052 LYS A CB    1 
ATOM   12692 C  CG    . LYS A 1 3052 ? 124.589 73.852  111.060 1.00 16.75  ? 3052 LYS A CG    1 
ATOM   12693 C  CD    . LYS A 1 3052 ? 125.440 74.177  112.277 1.00 23.36  ? 3052 LYS A CD    1 
ATOM   12694 C  CE    . LYS A 1 3052 ? 124.588 74.664  113.437 1.00 33.69  ? 3052 LYS A CE    1 
ATOM   12695 N  NZ    . LYS A 1 3052 ? 125.411 74.973  114.639 1.00 34.34  ? 3052 LYS A NZ    1 
ATOM   12696 N  N     . TRP A 1 3053 ? 126.249 71.647  107.374 1.00 8.52   ? 3053 TRP A N     1 
ATOM   12697 C  CA    . TRP A 1 3053 ? 127.134 71.357  106.250 1.00 6.80   ? 3053 TRP A CA    1 
ATOM   12698 C  C     . TRP A 1 3053 ? 126.375 71.390  104.930 1.00 6.75   ? 3053 TRP A C     1 
ATOM   12699 O  O     . TRP A 1 3053 ? 126.887 71.890  103.921 1.00 6.98   ? 3053 TRP A O     1 
ATOM   12700 C  CB    . TRP A 1 3053 ? 127.810 70.001  106.450 1.00 6.63   ? 3053 TRP A CB    1 
ATOM   12701 C  CG    . TRP A 1 3053 ? 128.519 69.500  105.229 1.00 8.26   ? 3053 TRP A CG    1 
ATOM   12702 C  CD1   . TRP A 1 3053 ? 129.794 69.790  104.846 1.00 7.95   ? 3053 TRP A CD1   1 
ATOM   12703 C  CD2   . TRP A 1 3053 ? 127.992 68.614  104.234 1.00 8.60   ? 3053 TRP A CD2   1 
ATOM   12704 N  NE1   . TRP A 1 3053 ? 130.094 69.144  103.672 1.00 10.48  ? 3053 TRP A NE1   1 
ATOM   12705 C  CE2   . TRP A 1 3053 ? 129.005 68.414  103.276 1.00 9.68   ? 3053 TRP A CE2   1 
ATOM   12706 C  CE3   . TRP A 1 3053 ? 126.762 67.973  104.058 1.00 7.05   ? 3053 TRP A CE3   1 
ATOM   12707 C  CZ2   . TRP A 1 3053 ? 128.826 67.601  102.159 1.00 10.02  ? 3053 TRP A CZ2   1 
ATOM   12708 C  CZ3   . TRP A 1 3053 ? 126.587 67.166  102.949 1.00 9.39   ? 3053 TRP A CZ3   1 
ATOM   12709 C  CH2   . TRP A 1 3053 ? 127.613 66.987  102.014 1.00 10.53  ? 3053 TRP A CH2   1 
ATOM   12710 N  N     . PHE A 1 3054 ? 125.153 70.854  104.919 1.00 6.21   ? 3054 PHE A N     1 
ATOM   12711 C  CA    . PHE A 1 3054 ? 124.326 70.894  103.717 1.00 5.42   ? 3054 PHE A CA    1 
ATOM   12712 C  C     . PHE A 1 3054 ? 124.009 72.330  103.316 1.00 6.01   ? 3054 PHE A C     1 
ATOM   12713 O  O     . PHE A 1 3054 ? 124.049 72.677  102.129 1.00 6.05   ? 3054 PHE A O     1 
ATOM   12714 C  CB    . PHE A 1 3054 ? 123.045 70.096  103.961 1.00 4.79   ? 3054 PHE A CB    1 
ATOM   12715 C  CG    . PHE A 1 3054 ? 121.989 70.286  102.913 1.00 3.96   ? 3054 PHE A CG    1 
ATOM   12716 C  CD1   . PHE A 1 3054 ? 122.070 69.621  101.702 1.00 5.41   ? 3054 PHE A CD1   1 
ATOM   12717 C  CD2   . PHE A 1 3054 ? 120.897 71.104  103.149 1.00 4.45   ? 3054 PHE A CD2   1 
ATOM   12718 C  CE1   . PHE A 1 3054 ? 121.095 69.783  100.741 1.00 4.98   ? 3054 PHE A CE1   1 
ATOM   12719 C  CE2   . PHE A 1 3054 ? 119.917 71.270  102.190 1.00 5.36   ? 3054 PHE A CE2   1 
ATOM   12720 C  CZ    . PHE A 1 3054 ? 120.017 70.609  100.984 1.00 4.37   ? 3054 PHE A CZ    1 
ATOM   12721 N  N     . THR A 1 3055 ? 123.695 73.178  104.297 1.00 4.58   ? 3055 THR A N     1 
ATOM   12722 C  CA    . THR A 1 3055 ? 123.431 74.585  104.014 1.00 6.24   ? 3055 THR A CA    1 
ATOM   12723 C  C     . THR A 1 3055 ? 124.666 75.274  103.447 1.00 5.86   ? 3055 THR A C     1 
ATOM   12724 O  O     . THR A 1 3055 ? 124.565 76.071  102.508 1.00 5.64   ? 3055 THR A O     1 
ATOM   12725 C  CB    . THR A 1 3055 ? 122.954 75.294  105.282 1.00 7.35   ? 3055 THR A CB    1 
ATOM   12726 O  OG1   . THR A 1 3055 ? 121.787 74.636  105.789 1.00 11.37  ? 3055 THR A OG1   1 
ATOM   12727 C  CG2   . THR A 1 3055 ? 122.621 76.748  104.990 1.00 9.24   ? 3055 THR A CG2   1 
ATOM   12728 N  N     . SER A 1 3056 ? 125.842 74.977  104.004 1.00 4.94   ? 3056 SER A N     1 
ATOM   12729 C  CA    . SER A 1 3056 ? 127.073 75.571  103.489 1.00 4.67   ? 3056 SER A CA    1 
ATOM   12730 C  C     . SER A 1 3056 ? 127.356 75.114  102.061 1.00 4.92   ? 3056 SER A C     1 
ATOM   12731 O  O     . SER A 1 3056 ? 127.799 75.908  101.219 1.00 4.82   ? 3056 SER A O     1 
ATOM   12732 C  CB    . SER A 1 3056 ? 128.245 75.230  104.409 1.00 6.51   ? 3056 SER A CB    1 
ATOM   12733 O  OG    . SER A 1 3056 ? 128.501 73.837  104.418 1.00 7.82   ? 3056 SER A OG    1 
ATOM   12734 N  N     . GLN A 1 3057 ? 127.112 73.833  101.771 1.00 5.40   ? 3057 GLN A N     1 
ATOM   12735 C  CA    . GLN A 1 3057 ? 127.301 73.333  100.413 1.00 5.29   ? 3057 GLN A CA    1 
ATOM   12736 C  C     . GLN A 1 3057 ? 126.334 73.996  99.439  1.00 4.33   ? 3057 GLN A C     1 
ATOM   12737 O  O     . GLN A 1 3057 ? 126.716 74.344  98.315  1.00 4.65   ? 3057 GLN A O     1 
ATOM   12738 C  CB    . GLN A 1 3057 ? 127.139 71.814  100.383 1.00 6.29   ? 3057 GLN A CB    1 
ATOM   12739 C  CG    . GLN A 1 3057 ? 128.225 71.058  101.126 1.00 6.93   ? 3057 GLN A CG    1 
ATOM   12740 C  CD    . GLN A 1 3057 ? 129.522 70.988  100.347 1.00 10.31  ? 3057 GLN A CD    1 
ATOM   12741 O  OE1   . GLN A 1 3057 ? 130.550 71.502  100.784 1.00 13.70  ? 3057 GLN A OE1   1 
ATOM   12742 N  NE2   . GLN A 1 3057 ? 129.481 70.345  99.186  1.00 12.07  ? 3057 GLN A NE2   1 
ATOM   12743 N  N     . VAL A 1 3058 ? 125.077 74.177  99.851  1.00 3.60   ? 3058 VAL A N     1 
ATOM   12744 C  CA    . VAL A 1 3058 ? 124.113 74.887  99.013  1.00 3.56   ? 3058 VAL A CA    1 
ATOM   12745 C  C     . VAL A 1 3058 ? 124.570 76.321  98.780  1.00 4.79   ? 3058 VAL A C     1 
ATOM   12746 O  O     . VAL A 1 3058 ? 124.455 76.855  97.669  1.00 5.00   ? 3058 VAL A O     1 
ATOM   12747 C  CB    . VAL A 1 3058 ? 122.709 74.837  99.647  1.00 4.74   ? 3058 VAL A CB    1 
ATOM   12748 C  CG1   . VAL A 1 3058 ? 121.770 75.798  98.936  1.00 4.01   ? 3058 VAL A CG1   1 
ATOM   12749 C  CG2   . VAL A 1 3058 ? 122.156 73.421  99.602  1.00 4.77   ? 3058 VAL A CG2   1 
ATOM   12750 N  N     . ILE A 1 3059 ? 125.097 76.964  99.823  1.00 4.83   ? 3059 ILE A N     1 
ATOM   12751 C  CA    . ILE A 1 3059 ? 125.585 78.334  99.703  1.00 4.79   ? 3059 ILE A CA    1 
ATOM   12752 C  C     . ILE A 1 3059 ? 126.707 78.417  98.677  1.00 5.21   ? 3059 ILE A C     1 
ATOM   12753 O  O     . ILE A 1 3059 ? 126.717 79.304  97.816  1.00 5.98   ? 3059 ILE A O     1 
ATOM   12754 C  CB    . ILE A 1 3059 ? 126.035 78.854  101.083 1.00 5.90   ? 3059 ILE A CB    1 
ATOM   12755 C  CG1   . ILE A 1 3059 ? 124.824 79.293  101.910 1.00 6.49   ? 3059 ILE A CG1   1 
ATOM   12756 C  CG2   . ILE A 1 3059 ? 127.060 79.975  100.943 1.00 7.86   ? 3059 ILE A CG2   1 
ATOM   12757 C  CD1   . ILE A 1 3059 ? 125.185 79.885  103.252 1.00 6.07   ? 3059 ILE A CD1   1 
ATOM   12758 N  N     . ARG A 1 3060 ? 127.662 77.489  98.742  1.00 5.01   ? 3060 ARG A N     1 
ATOM   12759 C  CA    . ARG A 1 3060 ? 128.815 77.569  97.853  1.00 6.40   ? 3060 ARG A CA    1 
ATOM   12760 C  C     . ARG A 1 3060 ? 128.534 77.055  96.443  1.00 7.17   ? 3060 ARG A C     1 
ATOM   12761 O  O     . ARG A 1 3060 ? 129.261 77.424  95.515  1.00 8.68   ? 3060 ARG A O     1 
ATOM   12762 C  CB    . ARG A 1 3060 ? 130.003 76.804  98.442  1.00 6.16   ? 3060 ARG A CB    1 
ATOM   12763 C  CG    . ARG A 1 3060 ? 129.782 75.314  98.595  1.00 11.23  ? 3060 ARG A CG    1 
ATOM   12764 C  CD    . ARG A 1 3060 ? 130.959 74.659  99.296  1.00 17.11  ? 3060 ARG A CD    1 
ATOM   12765 N  NE    . ARG A 1 3060 ? 132.191 74.806  98.529  1.00 28.26  ? 3060 ARG A NE    1 
ATOM   12766 C  CZ    . ARG A 1 3060 ? 132.608 73.948  97.609  1.00 27.51  ? 3060 ARG A CZ    1 
ATOM   12767 N  NH1   . ARG A 1 3060 ? 131.915 72.861  97.312  1.00 20.63  ? 3060 ARG A NH1   1 
ATOM   12768 N  NH2   . ARG A 1 3060 ? 133.748 74.188  96.968  1.00 29.27  ? 3060 ARG A NH2   1 
ATOM   12769 N  N     . ASN A 1 3061 ? 127.506 76.227  96.252  1.00 6.13   ? 3061 ASN A N     1 
ATOM   12770 C  CA    . ASN A 1 3061 ? 127.309 75.545  94.977  1.00 5.42   ? 3061 ASN A CA    1 
ATOM   12771 C  C     . ASN A 1 3061 ? 126.167 76.086  94.129  1.00 5.39   ? 3061 ASN A C     1 
ATOM   12772 O  O     . ASN A 1 3061 ? 126.259 76.033  92.902  1.00 6.48   ? 3061 ASN A O     1 
ATOM   12773 C  CB    . ASN A 1 3061 ? 127.072 74.047  95.206  1.00 5.75   ? 3061 ASN A CB    1 
ATOM   12774 C  CG    . ASN A 1 3061 ? 128.330 73.316  95.627  1.00 7.02   ? 3061 ASN A CG    1 
ATOM   12775 O  OD1   . ASN A 1 3061 ? 129.412 73.568  95.100  1.00 9.75   ? 3061 ASN A OD1   1 
ATOM   12776 N  ND2   . ASN A 1 3061 ? 128.192 72.398  96.574  1.00 6.77   ? 3061 ASN A ND2   1 
ATOM   12777 N  N     . LEU A 1 3062 ? 125.097 76.595  94.732  1.00 4.55   ? 3062 LEU A N     1 
ATOM   12778 C  CA    . LEU A 1 3062 ? 123.902 76.965  93.982  1.00 3.42   ? 3062 LEU A CA    1 
ATOM   12779 C  C     . LEU A 1 3062 ? 123.969 78.429  93.567  1.00 3.36   ? 3062 LEU A C     1 
ATOM   12780 O  O     . LEU A 1 3062 ? 124.267 79.301  94.389  1.00 4.91   ? 3062 LEU A O     1 
ATOM   12781 C  CB    . LEU A 1 3062 ? 122.643 76.709  94.812  1.00 3.85   ? 3062 LEU A CB    1 
ATOM   12782 C  CG    . LEU A 1 3062 ? 121.310 77.060  94.144  1.00 5.05   ? 3062 LEU A CG    1 
ATOM   12783 C  CD1   . LEU A 1 3062 ? 121.164 76.350  92.804  1.00 6.22   ? 3062 LEU A CD1   1 
ATOM   12784 C  CD2   . LEU A 1 3062 ? 120.127 76.759  95.057  1.00 3.69   ? 3062 LEU A CD2   1 
ATOM   12785 N  N     . HIS A 1 3063 ? 123.695 78.695  92.290  1.00 4.61   ? 3063 HIS A N     1 
ATOM   12786 C  CA    . HIS A 1 3063 ? 123.664 80.048  91.748  1.00 2.72   ? 3063 HIS A CA    1 
ATOM   12787 C  C     . HIS A 1 3063 ? 122.311 80.273  91.092  1.00 2.18   ? 3063 HIS A C     1 
ATOM   12788 O  O     . HIS A 1 3063 ? 122.015 79.664  90.061  1.00 3.66   ? 3063 HIS A O     1 
ATOM   12789 C  CB    . HIS A 1 3063 ? 124.786 80.258  90.730  1.00 2.46   ? 3063 HIS A CB    1 
ATOM   12790 C  CG    . HIS A 1 3063 ? 126.159 80.147  91.310  1.00 3.40   ? 3063 HIS A CG    1 
ATOM   12791 N  ND1   . HIS A 1 3063 ? 126.875 81.241  91.744  1.00 4.88   ? 3063 HIS A ND1   1 
ATOM   12792 C  CD2   . HIS A 1 3063 ? 126.948 79.070  91.531  1.00 3.45   ? 3063 HIS A CD2   1 
ATOM   12793 C  CE1   . HIS A 1 3063 ? 128.047 80.843  92.203  1.00 6.59   ? 3063 HIS A CE1   1 
ATOM   12794 N  NE2   . HIS A 1 3063 ? 128.116 79.530  92.087  1.00 4.38   ? 3063 HIS A NE2   1 
ATOM   12795 N  N     . VAL A 1 3064 ? 121.499 81.145  91.676  1.00 3.02   ? 3064 VAL A N     1 
ATOM   12796 C  CA    . VAL A 1 3064 ? 120.160 81.421  91.168  1.00 3.15   ? 3064 VAL A CA    1 
ATOM   12797 C  C     . VAL A 1 3064 ? 120.238 82.604  90.213  1.00 2.83   ? 3064 VAL A C     1 
ATOM   12798 O  O     . VAL A 1 3064 ? 120.766 83.665  90.564  1.00 2.79   ? 3064 VAL A O     1 
ATOM   12799 C  CB    . VAL A 1 3064 ? 119.169 81.693  92.310  1.00 4.49   ? 3064 VAL A CB    1 
ATOM   12800 C  CG1   . VAL A 1 3064 ? 117.871 82.266  91.762  1.00 2.61   ? 3064 VAL A CG1   1 
ATOM   12801 C  CG2   . VAL A 1 3064 ? 118.904 80.415  93.086  1.00 3.36   ? 3064 VAL A CG2   1 
ATOM   12802 N  N     . VAL A 1 3065 ? 119.718 82.420  89.003  1.00 2.76   ? 3065 VAL A N     1 
ATOM   12803 C  CA    . VAL A 1 3065 ? 119.676 83.462  87.985  1.00 2.70   ? 3065 VAL A CA    1 
ATOM   12804 C  C     . VAL A 1 3065 ? 118.216 83.805  87.726  1.00 3.05   ? 3065 VAL A C     1 
ATOM   12805 O  O     . VAL A 1 3065 ? 117.491 83.032  87.087  1.00 4.99   ? 3065 VAL A O     1 
ATOM   12806 C  CB    . VAL A 1 3065 ? 120.376 83.021  86.691  1.00 2.53   ? 3065 VAL A CB    1 
ATOM   12807 C  CG1   . VAL A 1 3065 ? 120.343 84.140  85.661  1.00 2.45   ? 3065 VAL A CG1   1 
ATOM   12808 C  CG2   . VAL A 1 3065 ? 121.804 82.596  86.980  1.00 2.30   ? 3065 VAL A CG2   1 
ATOM   12809 N  N     . PHE A 1 3066 ? 117.793 84.969  88.208  1.00 2.35   ? 3066 PHE A N     1 
ATOM   12810 C  CA    . PHE A 1 3066 ? 116.442 85.473  88.004  1.00 4.20   ? 3066 PHE A CA    1 
ATOM   12811 C  C     . PHE A 1 3066 ? 116.404 86.350  86.763  1.00 5.73   ? 3066 PHE A C     1 
ATOM   12812 O  O     . PHE A 1 3066 ? 117.182 87.303  86.647  1.00 6.65   ? 3066 PHE A O     1 
ATOM   12813 C  CB    . PHE A 1 3066 ? 115.962 86.267  89.221  1.00 7.40   ? 3066 PHE A CB    1 
ATOM   12814 C  CG    . PHE A 1 3066 ? 114.482 86.185  89.452  1.00 14.28  ? 3066 PHE A CG    1 
ATOM   12815 C  CD1   . PHE A 1 3066 ? 113.920 85.097  90.095  1.00 16.07  ? 3066 PHE A CD1   1 
ATOM   12816 C  CD2   . PHE A 1 3066 ? 113.649 87.204  89.018  1.00 15.09  ? 3066 PHE A CD2   1 
ATOM   12817 C  CE1   . PHE A 1 3066 ? 112.555 85.029  90.303  1.00 26.86  ? 3066 PHE A CE1   1 
ATOM   12818 C  CE2   . PHE A 1 3066 ? 112.286 87.141  89.223  1.00 22.70  ? 3066 PHE A CE2   1 
ATOM   12819 C  CZ    . PHE A 1 3066 ? 111.738 86.052  89.867  1.00 28.75  ? 3066 PHE A CZ    1 
ATOM   12820 N  N     . THR A 1 3067 ? 115.503 86.028  85.841  1.00 8.29   ? 3067 THR A N     1 
ATOM   12821 C  CA    . THR A 1 3067 ? 115.301 86.826  84.640  1.00 8.63   ? 3067 THR A CA    1 
ATOM   12822 C  C     . THR A 1 3067 ? 113.896 87.411  84.648  1.00 11.44  ? 3067 THR A C     1 
ATOM   12823 O  O     . THR A 1 3067 ? 112.924 86.709  84.944  1.00 14.71  ? 3067 THR A O     1 
ATOM   12824 C  CB    . THR A 1 3067 ? 115.522 85.995  83.370  1.00 9.85   ? 3067 THR A CB    1 
ATOM   12825 O  OG1   . THR A 1 3067 ? 114.689 84.831  83.405  1.00 17.11  ? 3067 THR A OG1   1 
ATOM   12826 C  CG2   . THR A 1 3067 ? 116.978 85.568  83.261  1.00 6.20   ? 3067 THR A CG2   1 
ATOM   12827 N  N     . MET A 1 3068 ? 113.793 88.700  84.333  1.00 11.79  ? 3068 MET A N     1 
ATOM   12828 C  CA    . MET A 1 3068 ? 112.500 89.370  84.336  1.00 15.96  ? 3068 MET A CA    1 
ATOM   12829 C  C     . MET A 1 3068 ? 112.546 90.575  83.408  1.00 16.75  ? 3068 MET A C     1 
ATOM   12830 O  O     . MET A 1 3068 ? 113.611 91.148  83.162  1.00 13.28  ? 3068 MET A O     1 
ATOM   12831 C  CB    . MET A 1 3068 ? 112.096 89.806  85.748  1.00 16.24  ? 3068 MET A CB    1 
ATOM   12832 C  CG    . MET A 1 3068 ? 113.117 90.681  86.446  1.00 14.73  ? 3068 MET A CG    1 
ATOM   12833 S  SD    . MET A 1 3068 ? 112.610 91.103  88.122  1.00 32.39  ? 3068 MET A SD    1 
ATOM   12834 C  CE    . MET A 1 3068 ? 111.045 91.916  87.808  1.00 32.90  ? 3068 MET A CE    1 
ATOM   12835 N  N     . ASN A 1 3069 ? 111.371 90.947  82.897  1.00 20.12  ? 3069 ASN A N     1 
ATOM   12836 C  CA    . ASN A 1 3069 ? 111.221 92.096  82.019  1.00 18.84  ? 3069 ASN A CA    1 
ATOM   12837 C  C     . ASN A 1 3069 ? 111.220 93.396  82.823  1.00 18.66  ? 3069 ASN A C     1 
ATOM   12838 O  O     . ASN A 1 3069 ? 110.817 93.413  83.989  1.00 24.79  ? 3069 ASN A O     1 
ATOM   12839 C  CB    . ASN A 1 3069 ? 109.928 91.986  81.219  1.00 18.14  ? 3069 ASN A CB    1 
ATOM   12840 C  CG    . ASN A 1 3069 ? 110.113 91.245  79.910  1.00 16.61  ? 3069 ASN A CG    1 
ATOM   12841 O  OD1   . ASN A 1 3069 ? 110.261 91.857  78.853  1.00 21.51  ? 3069 ASN A OD1   1 
ATOM   12842 N  ND2   . ASN A 1 3069 ? 110.103 89.920  79.974  1.00 20.58  ? 3069 ASN A ND2   1 
ATOM   12843 N  N     . PRO A 1 3070 ? 111.671 94.498  82.221  1.00 21.40  ? 3070 PRO A N     1 
ATOM   12844 C  CA    . PRO A 1 3070 ? 111.644 95.794  82.919  1.00 23.91  ? 3070 PRO A CA    1 
ATOM   12845 C  C     . PRO A 1 3070 ? 110.218 96.314  83.041  1.00 29.68  ? 3070 PRO A C     1 
ATOM   12846 O  O     . PRO A 1 3070 ? 109.515 96.475  82.042  1.00 33.50  ? 3070 PRO A O     1 
ATOM   12847 C  CB    . PRO A 1 3070 ? 112.500 96.699  82.024  1.00 18.16  ? 3070 PRO A CB    1 
ATOM   12848 C  CG    . PRO A 1 3070 ? 113.266 95.768  81.130  1.00 13.44  ? 3070 PRO A CG    1 
ATOM   12849 C  CD    . PRO A 1 3070 ? 112.375 94.586  80.933  1.00 14.82  ? 3070 PRO A CD    1 
ATOM   12850 N  N     . SER A 1 3071 ? 109.797 96.577  84.276  1.00 36.41  ? 3071 SER A N     1 
ATOM   12851 C  CA    . SER A 1 3071 ? 108.483 97.147  84.557  1.00 38.33  ? 3071 SER A CA    1 
ATOM   12852 C  C     . SER A 1 3071 ? 108.585 97.946  85.846  1.00 44.29  ? 3071 SER A C     1 
ATOM   12853 O  O     . SER A 1 3071 ? 108.902 97.381  86.896  1.00 45.77  ? 3071 SER A O     1 
ATOM   12854 C  CB    . SER A 1 3071 ? 107.414 96.058  84.678  1.00 35.16  ? 3071 SER A CB    1 
ATOM   12855 O  OG    . SER A 1 3071 ? 107.373 95.247  83.517  1.00 41.22  ? 3071 SER A OG    1 
ATOM   12856 N  N     . SER A 1 3072 ? 108.316 99.252  85.766  1.00 50.81  ? 3072 SER A N     1 
ATOM   12857 C  CA    . SER A 1 3072 ? 108.515 100.124 86.921  1.00 51.25  ? 3072 SER A CA    1 
ATOM   12858 C  C     . SER A 1 3072 ? 107.642 99.698  88.095  1.00 47.31  ? 3072 SER A C     1 
ATOM   12859 O  O     . SER A 1 3072 ? 108.142 99.455  89.200  1.00 46.18  ? 3072 SER A O     1 
ATOM   12860 C  CB    . SER A 1 3072 ? 108.228 101.575 86.534  1.00 55.13  ? 3072 SER A CB    1 
ATOM   12861 O  OG    . SER A 1 3072 ? 109.099 102.011 85.506  1.00 63.88  ? 3072 SER A OG    1 
ATOM   12862 N  N     . GLU A 1 3073 ? 106.331 99.585  87.870  1.00 48.68  ? 3073 GLU A N     1 
ATOM   12863 C  CA    . GLU A 1 3073 ? 105.445 99.100  88.923  1.00 54.24  ? 3073 GLU A CA    1 
ATOM   12864 C  C     . GLU A 1 3073 ? 105.784 97.664  89.297  1.00 48.08  ? 3073 GLU A C     1 
ATOM   12865 O  O     . GLU A 1 3073 ? 105.798 97.306  90.482  1.00 49.59  ? 3073 GLU A O     1 
ATOM   12866 C  CB    . GLU A 1 3073 ? 103.987 99.208  88.476  1.00 57.19  ? 3073 GLU A CB    1 
ATOM   12867 C  CG    . GLU A 1 3073 ? 102.989 98.643  89.475  1.00 64.06  ? 3073 GLU A CG    1 
ATOM   12868 C  CD    . GLU A 1 3073 ? 101.557 98.739  88.987  1.00 79.32  ? 3073 GLU A CD    1 
ATOM   12869 O  OE1   . GLU A 1 3073 ? 101.249 98.156  87.926  1.00 79.29  ? 3073 GLU A OE1   1 
ATOM   12870 O  OE2   . GLU A 1 3073 ? 100.738 99.395  89.665  1.00 83.17  ? 3073 GLU A OE2   1 
ATOM   12871 N  N     . GLY A 1 3074 ? 106.068 96.831  88.294  1.00 45.71  ? 3074 GLY A N     1 
ATOM   12872 C  CA    . GLY A 1 3074 ? 106.447 95.458  88.569  1.00 42.93  ? 3074 GLY A CA    1 
ATOM   12873 C  C     . GLY A 1 3074 ? 107.708 95.358  89.402  1.00 40.90  ? 3074 GLY A C     1 
ATOM   12874 O  O     . GLY A 1 3074 ? 107.774 94.574  90.346  1.00 37.98  ? 3074 GLY A O     1 
ATOM   12875 N  N     . LEU A 1 3075 ? 108.719 96.169  89.080  1.00 40.44  ? 3075 LEU A N     1 
ATOM   12876 C  CA    . LEU A 1 3075 ? 109.972 96.125  89.830  1.00 36.66  ? 3075 LEU A CA    1 
ATOM   12877 C  C     . LEU A 1 3075 ? 109.789 96.661  91.247  1.00 39.09  ? 3075 LEU A C     1 
ATOM   12878 O  O     . LEU A 1 3075 ? 110.351 96.112  92.206  1.00 36.94  ? 3075 LEU A O     1 
ATOM   12879 C  CB    . LEU A 1 3075 ? 111.049 96.914  89.084  1.00 42.13  ? 3075 LEU A CB    1 
ATOM   12880 C  CG    . LEU A 1 3075 ? 112.501 96.761  89.530  1.00 36.05  ? 3075 LEU A CG    1 
ATOM   12881 C  CD1   . LEU A 1 3075 ? 112.983 95.361  89.205  1.00 24.42  ? 3075 LEU A CD1   1 
ATOM   12882 C  CD2   . LEU A 1 3075 ? 113.380 97.798  88.854  1.00 29.84  ? 3075 LEU A CD2   1 
ATOM   12883 N  N     . LYS A 1 3076 ? 109.010 97.737  91.399  1.00 41.73  ? 3076 LYS A N     1 
ATOM   12884 C  CA    . LYS A 1 3076 ? 108.765 98.287  92.729  1.00 36.94  ? 3076 LYS A CA    1 
ATOM   12885 C  C     . LYS A 1 3076 ? 108.021 97.293  93.614  1.00 36.01  ? 3076 LYS A C     1 
ATOM   12886 O  O     . LYS A 1 3076 ? 108.353 97.135  94.794  1.00 36.50  ? 3076 LYS A O     1 
ATOM   12887 C  CB    . LYS A 1 3076 ? 107.994 99.602  92.622  1.00 40.12  ? 3076 LYS A CB    1 
ATOM   12888 C  CG    . LYS A 1 3076 ? 108.799 100.736 92.006  1.00 38.13  ? 3076 LYS A CG    1 
ATOM   12889 C  CD    . LYS A 1 3076 ? 107.999 102.025 91.949  1.00 39.71  ? 3076 LYS A CD    1 
ATOM   12890 C  CE    . LYS A 1 3076 ? 108.809 103.143 91.314  1.00 41.23  ? 3076 LYS A CE    1 
ATOM   12891 N  NZ    . LYS A 1 3076 ? 108.037 104.414 91.240  1.00 54.21  ? 3076 LYS A NZ    1 
ATOM   12892 N  N     . ASP A 1 3077 ? 107.009 96.614  93.065  1.00 37.02  ? 3077 ASP A N     1 
ATOM   12893 C  CA    . ASP A 1 3077 ? 106.337 95.567  93.829  1.00 40.70  ? 3077 ASP A CA    1 
ATOM   12894 C  C     . ASP A 1 3077 ? 107.253 94.372  94.061  1.00 39.63  ? 3077 ASP A C     1 
ATOM   12895 O  O     . ASP A 1 3077 ? 107.153 93.703  95.098  1.00 41.13  ? 3077 ASP A O     1 
ATOM   12896 C  CB    . ASP A 1 3077 ? 105.061 95.128  93.111  1.00 47.38  ? 3077 ASP A CB    1 
ATOM   12897 C  CG    . ASP A 1 3077 ? 103.993 96.203  93.112  1.00 59.37  ? 3077 ASP A CG    1 
ATOM   12898 O  OD1   . ASP A 1 3077 ? 103.970 97.020  94.056  1.00 57.55  ? 3077 ASP A OD1   1 
ATOM   12899 O  OD2   . ASP A 1 3077 ? 103.176 96.232  92.168  1.00 63.10  ? 3077 ASP A OD2   1 
ATOM   12900 N  N     . ARG A 1 3078 ? 108.147 94.097  93.109  1.00 41.38  ? 3078 ARG A N     1 
ATOM   12901 C  CA    . ARG A 1 3078 ? 109.082 92.988  93.226  1.00 37.57  ? 3078 ARG A CA    1 
ATOM   12902 C  C     . ARG A 1 3078 ? 110.014 93.195  94.409  1.00 30.95  ? 3078 ARG A C     1 
ATOM   12903 O  O     . ARG A 1 3078 ? 110.376 92.234  95.096  1.00 30.06  ? 3078 ARG A O     1 
ATOM   12904 C  CB    . ARG A 1 3078 ? 109.901 92.886  91.939  1.00 37.24  ? 3078 ARG A CB    1 
ATOM   12905 C  CG    . ARG A 1 3078 ? 110.925 91.777  91.904  1.00 37.44  ? 3078 ARG A CG    1 
ATOM   12906 C  CD    . ARG A 1 3078 ? 110.204 90.451  91.913  1.00 36.55  ? 3078 ARG A CD    1 
ATOM   12907 N  NE    . ARG A 1 3078 ? 109.447 90.337  90.670  1.00 44.41  ? 3078 ARG A NE    1 
ATOM   12908 C  CZ    . ARG A 1 3078 ? 108.518 89.426  90.423  1.00 46.42  ? 3078 ARG A CZ    1 
ATOM   12909 N  NH1   . ARG A 1 3078 ? 108.201 88.505  91.314  1.00 48.12  ? 3078 ARG A NH1   1 
ATOM   12910 N  NH2   . ARG A 1 3078 ? 107.890 89.440  89.251  1.00 40.26  ? 3078 ARG A NH2   1 
ATOM   12911 N  N     . ALA A 1 3079 ? 110.416 94.448  94.643  1.00 31.46  ? 3079 ALA A N     1 
ATOM   12912 C  CA    . ALA A 1 3079 ? 111.311 94.755  95.754  1.00 26.24  ? 3079 ALA A CA    1 
ATOM   12913 C  C     . ALA A 1 3079 ? 110.692 94.372  97.093  1.00 31.36  ? 3079 ALA A C     1 
ATOM   12914 O  O     . ALA A 1 3079 ? 111.369 93.807  97.959  1.00 27.83  ? 3079 ALA A O     1 
ATOM   12915 C  CB    . ALA A 1 3079 ? 111.679 96.238  95.738  1.00 22.80  ? 3079 ALA A CB    1 
ATOM   12916 N  N     . ALA A 1 3080 ? 109.407 94.675  97.285  1.00 37.69  ? 3080 ALA A N     1 
ATOM   12917 C  CA    . ALA A 1 3080 ? 108.743 94.298  98.527  1.00 28.90  ? 3080 ALA A CA    1 
ATOM   12918 C  C     . ALA A 1 3080 ? 108.452 92.804  98.579  1.00 24.03  ? 3080 ALA A C     1 
ATOM   12919 O  O     . ALA A 1 3080 ? 108.584 92.181  99.638  1.00 21.70  ? 3080 ALA A O     1 
ATOM   12920 C  CB    . ALA A 1 3080 ? 107.450 95.096  98.698  1.00 25.76  ? 3080 ALA A CB    1 
ATOM   12921 N  N     . THR A 1 3081 ? 108.053 92.214  97.449  1.00 29.46  ? 3081 THR A N     1 
ATOM   12922 C  CA    . THR A 1 3081 ? 107.666 90.807  97.450  1.00 30.57  ? 3081 THR A CA    1 
ATOM   12923 C  C     . THR A 1 3081 ? 108.852 89.897  97.758  1.00 32.30  ? 3081 THR A C     1 
ATOM   12924 O  O     . THR A 1 3081 ? 108.718 88.933  98.521  1.00 33.24  ? 3081 THR A O     1 
ATOM   12925 C  CB    . THR A 1 3081 ? 107.038 90.437  96.108  1.00 34.66  ? 3081 THR A CB    1 
ATOM   12926 O  OG1   . THR A 1 3081 ? 105.877 91.248  95.886  1.00 35.23  ? 3081 THR A OG1   1 
ATOM   12927 C  CG2   . THR A 1 3081 ? 106.616 88.984  96.112  1.00 35.31  ? 3081 THR A CG2   1 
ATOM   12928 N  N     . SER A 1 3082 ? 110.016 90.180  97.174  1.00 27.85  ? 3082 SER A N     1 
ATOM   12929 C  CA    . SER A 1 3082 ? 111.233 89.397  97.398  1.00 20.40  ? 3082 SER A CA    1 
ATOM   12930 C  C     . SER A 1 3082 ? 112.389 90.355  97.651  1.00 20.30  ? 3082 SER A C     1 
ATOM   12931 O  O     . SER A 1 3082 ? 113.163 90.669  96.737  1.00 21.24  ? 3082 SER A O     1 
ATOM   12932 C  CB    . SER A 1 3082 ? 111.525 88.474  96.214  1.00 27.16  ? 3082 SER A CB    1 
ATOM   12933 O  OG    . SER A 1 3082 ? 112.713 87.732  96.429  1.00 25.39  ? 3082 SER A OG    1 
ATOM   12934 N  N     . PRO A 1 3083 ? 112.527 90.852  98.884  1.00 21.18  ? 3083 PRO A N     1 
ATOM   12935 C  CA    . PRO A 1 3083 ? 113.610 91.810  99.171  1.00 17.16  ? 3083 PRO A CA    1 
ATOM   12936 C  C     . PRO A 1 3083 ? 115.004 91.267  98.905  1.00 13.27  ? 3083 PRO A C     1 
ATOM   12937 O  O     . PRO A 1 3083 ? 115.860 92.014  98.411  1.00 14.46  ? 3083 PRO A O     1 
ATOM   12938 C  CB    . PRO A 1 3083 ? 113.404 92.134  100.659 1.00 14.22  ? 3083 PRO A CB    1 
ATOM   12939 C  CG    . PRO A 1 3083 ? 112.552 91.025  101.190 1.00 12.37  ? 3083 PRO A CG    1 
ATOM   12940 C  CD    . PRO A 1 3083 ? 111.678 90.604  100.059 1.00 14.70  ? 3083 PRO A CD    1 
ATOM   12941 N  N     . ALA A 1 3084 ? 115.257 89.988  99.201  1.00 13.67  ? 3084 ALA A N     1 
ATOM   12942 C  CA    . ALA A 1 3084 ? 116.585 89.420  98.990  1.00 12.05  ? 3084 ALA A CA    1 
ATOM   12943 C  C     . ALA A 1 3084 ? 117.042 89.550  97.546  1.00 12.65  ? 3084 ALA A C     1 
ATOM   12944 O  O     . ALA A 1 3084 ? 118.235 89.769  97.303  1.00 11.54  ? 3084 ALA A O     1 
ATOM   12945 C  CB    . ALA A 1 3084 ? 116.613 87.950  99.410  1.00 12.66  ? 3084 ALA A CB    1 
ATOM   12946 N  N     . LEU A 1 3085 ? 116.112 89.466  96.593  1.00 14.55  ? 3085 LEU A N     1 
ATOM   12947 C  CA    . LEU A 1 3085 ? 116.445 89.588  95.181  1.00 12.91  ? 3085 LEU A CA    1 
ATOM   12948 C  C     . LEU A 1 3085 ? 117.151 90.900  94.869  1.00 14.03  ? 3085 LEU A C     1 
ATOM   12949 O  O     . LEU A 1 3085 ? 117.892 90.972  93.883  1.00 14.48  ? 3085 LEU A O     1 
ATOM   12950 C  CB    . LEU A 1 3085 ? 115.170 89.456  94.344  1.00 15.85  ? 3085 LEU A CB    1 
ATOM   12951 C  CG    . LEU A 1 3085 ? 115.267 89.486  92.819  1.00 20.35  ? 3085 LEU A CG    1 
ATOM   12952 C  CD1   . LEU A 1 3085 ? 116.088 88.313  92.313  1.00 20.93  ? 3085 LEU A CD1   1 
ATOM   12953 C  CD2   . LEU A 1 3085 ? 113.880 89.482  92.195  1.00 18.94  ? 3085 LEU A CD2   1 
ATOM   12954 N  N     . PHE A 1 3086 ? 116.951 91.933  95.687  1.00 14.07  ? 3086 PHE A N     1 
ATOM   12955 C  CA    . PHE A 1 3086 ? 117.588 93.224  95.473  1.00 13.65  ? 3086 PHE A CA    1 
ATOM   12956 C  C     . PHE A 1 3086 ? 118.738 93.507  96.427  1.00 14.30  ? 3086 PHE A C     1 
ATOM   12957 O  O     . PHE A 1 3086 ? 119.355 94.572  96.323  1.00 18.72  ? 3086 PHE A O     1 
ATOM   12958 C  CB    . PHE A 1 3086 ? 116.545 94.341  95.565  1.00 14.50  ? 3086 PHE A CB    1 
ATOM   12959 C  CG    . PHE A 1 3086 ? 115.548 94.317  94.450  1.00 19.51  ? 3086 PHE A CG    1 
ATOM   12960 C  CD1   . PHE A 1 3086 ? 114.417 93.526  94.530  1.00 21.46  ? 3086 PHE A CD1   1 
ATOM   12961 C  CD2   . PHE A 1 3086 ? 115.743 95.086  93.316  1.00 16.77  ? 3086 PHE A CD2   1 
ATOM   12962 C  CE1   . PHE A 1 3086 ? 113.506 93.498  93.500  1.00 25.04  ? 3086 PHE A CE1   1 
ATOM   12963 C  CE2   . PHE A 1 3086 ? 114.830 95.065  92.287  1.00 19.41  ? 3086 PHE A CE2   1 
ATOM   12964 C  CZ    . PHE A 1 3086 ? 113.708 94.272  92.382  1.00 23.99  ? 3086 PHE A CZ    1 
ATOM   12965 N  N     . ASN A 1 3087 ? 119.054 92.596  97.350  1.00 11.50  ? 3087 ASN A N     1 
ATOM   12966 C  CA    . ASN A 1 3087 ? 120.218 92.784  98.206  1.00 13.84  ? 3087 ASN A CA    1 
ATOM   12967 C  C     . ASN A 1 3087 ? 121.093 91.547  98.347  1.00 15.45  ? 3087 ASN A C     1 
ATOM   12968 O  O     . ASN A 1 3087 ? 122.180 91.651  98.925  1.00 20.24  ? 3087 ASN A O     1 
ATOM   12969 C  CB    . ASN A 1 3087 ? 119.796 93.289  99.600  1.00 15.51  ? 3087 ASN A CB    1 
ATOM   12970 C  CG    . ASN A 1 3087 ? 118.932 92.298  100.365 1.00 16.96  ? 3087 ASN A CG    1 
ATOM   12971 O  OD1   . ASN A 1 3087 ? 118.949 91.098  100.109 1.00 15.69  ? 3087 ASN A OD1   1 
ATOM   12972 N  ND2   . ASN A 1 3087 ? 118.167 92.811  101.321 1.00 18.06  ? 3087 ASN A ND2   1 
ATOM   12973 N  N     . ARG A 1 3088 ? 120.665 90.391  97.841  1.00 12.56  ? 3088 ARG A N     1 
ATOM   12974 C  CA    . ARG A 1 3088 ? 121.513 89.213  97.769  1.00 12.38  ? 3088 ARG A CA    1 
ATOM   12975 C  C     . ARG A 1 3088 ? 121.873 88.832  96.340  1.00 10.49  ? 3088 ARG A C     1 
ATOM   12976 O  O     . ARG A 1 3088 ? 122.744 87.977  96.145  1.00 8.83   ? 3088 ARG A O     1 
ATOM   12977 C  CB    . ARG A 1 3088 ? 120.836 88.018  98.458  1.00 11.34  ? 3088 ARG A CB    1 
ATOM   12978 C  CG    . ARG A 1 3088 ? 120.376 88.277  99.880  1.00 12.65  ? 3088 ARG A CG    1 
ATOM   12979 C  CD    . ARG A 1 3088 ? 121.510 88.770  100.758 1.00 18.02  ? 3088 ARG A CD    1 
ATOM   12980 N  NE    . ARG A 1 3088 ? 121.522 88.093  102.049 1.00 28.80  ? 3088 ARG A NE    1 
ATOM   12981 C  CZ    . ARG A 1 3088 ? 120.856 88.508  103.118 1.00 27.67  ? 3088 ARG A CZ    1 
ATOM   12982 N  NH1   . ARG A 1 3088 ? 120.114 89.603  103.088 1.00 24.18  ? 3088 ARG A NH1   1 
ATOM   12983 N  NH2   . ARG A 1 3088 ? 120.934 87.806  104.245 1.00 24.25  ? 3088 ARG A NH2   1 
ATOM   12984 N  N     . CYS A 1 3089 ? 121.230 89.435  95.343  1.00 11.15  ? 3089 CYS A N     1 
ATOM   12985 C  CA    . CYS A 1 3089 ? 121.524 89.188  93.940  1.00 6.27   ? 3089 CYS A CA    1 
ATOM   12986 C  C     . CYS A 1 3089 ? 122.157 90.426  93.320  1.00 4.93   ? 3089 CYS A C     1 
ATOM   12987 O  O     . CYS A 1 3089 ? 121.754 91.555  93.614  1.00 6.93   ? 3089 CYS A O     1 
ATOM   12988 C  CB    . CYS A 1 3089 ? 120.259 88.822  93.156  1.00 3.84   ? 3089 CYS A CB    1 
ATOM   12989 S  SG    . CYS A 1 3089 ? 119.220 87.554  93.903  1.00 16.95  ? 3089 CYS A SG    1 
ATOM   12990 N  N     . VAL A 1 3090 ? 123.148 90.207  92.463  1.00 3.72   ? 3090 VAL A N     1 
ATOM   12991 C  CA    . VAL A 1 3090 ? 123.726 91.287  91.672  1.00 5.43   ? 3090 VAL A CA    1 
ATOM   12992 C  C     . VAL A 1 3090 ? 122.781 91.575  90.514  1.00 3.22   ? 3090 VAL A C     1 
ATOM   12993 O  O     . VAL A 1 3090 ? 122.407 90.667  89.763  1.00 3.86   ? 3090 VAL A O     1 
ATOM   12994 C  CB    . VAL A 1 3090 ? 125.129 90.918  91.171  1.00 5.42   ? 3090 VAL A CB    1 
ATOM   12995 C  CG1   . VAL A 1 3090 ? 125.612 91.930  90.143  1.00 4.13   ? 3090 VAL A CG1   1 
ATOM   12996 C  CG2   . VAL A 1 3090 ? 126.097 90.826  92.338  1.00 3.48   ? 3090 VAL A CG2   1 
ATOM   12997 N  N     . LEU A 1 3091 ? 122.373 92.833  90.380  1.00 2.87   ? 3091 LEU A N     1 
ATOM   12998 C  CA    . LEU A 1 3091 ? 121.398 93.228  89.373  1.00 3.33   ? 3091 LEU A CA    1 
ATOM   12999 C  C     . LEU A 1 3091 ? 122.134 93.680  88.119  1.00 3.96   ? 3091 LEU A C     1 
ATOM   13000 O  O     . LEU A 1 3091 ? 123.065 94.489  88.195  1.00 4.32   ? 3091 LEU A O     1 
ATOM   13001 C  CB    . LEU A 1 3091 ? 120.488 94.335  89.909  1.00 3.99   ? 3091 LEU A CB    1 
ATOM   13002 C  CG    . LEU A 1 3091 ? 119.191 94.674  89.163  1.00 5.47   ? 3091 LEU A CG    1 
ATOM   13003 C  CD1   . LEU A 1 3091 ? 118.242 95.405  90.095  1.00 7.77   ? 3091 LEU A CD1   1 
ATOM   13004 C  CD2   . LEU A 1 3091 ? 119.436 95.515  87.915  1.00 4.20   ? 3091 LEU A CD2   1 
ATOM   13005 N  N     . ASN A 1 3092 ? 121.722 93.151  86.971  1.00 4.12   ? 3092 ASN A N     1 
ATOM   13006 C  CA    . ASN A 1 3092 ? 122.289 93.521  85.681  1.00 3.62   ? 3092 ASN A CA    1 
ATOM   13007 C  C     . ASN A 1 3092 ? 121.152 93.950  84.767  1.00 4.29   ? 3092 ASN A C     1 
ATOM   13008 O  O     . ASN A 1 3092 ? 120.285 93.139  84.418  1.00 4.48   ? 3092 ASN A O     1 
ATOM   13009 C  CB    . ASN A 1 3092 ? 123.082 92.365  85.079  1.00 4.36   ? 3092 ASN A CB    1 
ATOM   13010 C  CG    . ASN A 1 3092 ? 124.463 92.243  85.679  1.00 7.59   ? 3092 ASN A CG    1 
ATOM   13011 O  OD1   . ASN A 1 3092 ? 124.652 91.590  86.705  1.00 7.32   ? 3092 ASN A OD1   1 
ATOM   13012 N  ND2   . ASN A 1 3092 ? 125.436 92.886  85.052  1.00 9.42   ? 3092 ASN A ND2   1 
ATOM   13013 N  N     . TRP A 1 3093 ? 121.157 95.225  84.389  1.00 4.67   ? 3093 TRP A N     1 
ATOM   13014 C  CA    . TRP A 1 3093 ? 120.138 95.789  83.509  1.00 4.72   ? 3093 TRP A CA    1 
ATOM   13015 C  C     . TRP A 1 3093 ? 120.599 95.616  82.069  1.00 5.12   ? 3093 TRP A C     1 
ATOM   13016 O  O     . TRP A 1 3093 ? 121.227 96.498  81.481  1.00 8.45   ? 3093 TRP A O     1 
ATOM   13017 C  CB    . TRP A 1 3093 ? 119.888 97.254  83.842  1.00 5.29   ? 3093 TRP A CB    1 
ATOM   13018 C  CG    . TRP A 1 3093 ? 118.558 97.745  83.375  1.00 6.85   ? 3093 TRP A CG    1 
ATOM   13019 C  CD1   . TRP A 1 3093 ? 118.247 98.209  82.131  1.00 5.70   ? 3093 TRP A CD1   1 
ATOM   13020 C  CD2   . TRP A 1 3093 ? 117.354 97.826  84.146  1.00 6.21   ? 3093 TRP A CD2   1 
ATOM   13021 N  NE1   . TRP A 1 3093 ? 116.924 98.571  82.079  1.00 7.07   ? 3093 TRP A NE1   1 
ATOM   13022 C  CE2   . TRP A 1 3093 ? 116.353 98.345  83.303  1.00 6.69   ? 3093 TRP A CE2   1 
ATOM   13023 C  CE3   . TRP A 1 3093 ? 117.026 97.508  85.467  1.00 4.97   ? 3093 TRP A CE3   1 
ATOM   13024 C  CZ2   . TRP A 1 3093 ? 115.047 98.555  83.738  1.00 5.72   ? 3093 TRP A CZ2   1 
ATOM   13025 C  CZ3   . TRP A 1 3093 ? 115.729 97.717  85.897  1.00 7.74   ? 3093 TRP A CZ3   1 
ATOM   13026 C  CH2   . TRP A 1 3093 ? 114.756 98.235  85.035  1.00 6.23   ? 3093 TRP A CH2   1 
ATOM   13027 N  N     . PHE A 1 3094 ? 120.288 94.454  81.494  1.00 4.20   ? 3094 PHE A N     1 
ATOM   13028 C  CA    . PHE A 1 3094 ? 120.582 94.238  80.083  1.00 5.75   ? 3094 PHE A CA    1 
ATOM   13029 C  C     . PHE A 1 3094 ? 119.658 95.077  79.210  1.00 7.10   ? 3094 PHE A C     1 
ATOM   13030 O  O     . PHE A 1 3094 ? 120.059 95.542  78.136  1.00 9.71   ? 3094 PHE A O     1 
ATOM   13031 C  CB    . PHE A 1 3094 ? 120.450 92.754  79.738  1.00 6.52   ? 3094 PHE A CB    1 
ATOM   13032 C  CG    . PHE A 1 3094 ? 121.532 91.890  80.330  1.00 8.85   ? 3094 PHE A CG    1 
ATOM   13033 C  CD1   . PHE A 1 3094 ? 122.609 92.454  80.997  1.00 8.26   ? 3094 PHE A CD1   1 
ATOM   13034 C  CD2   . PHE A 1 3094 ? 121.473 90.512  80.215  1.00 8.47   ? 3094 PHE A CD2   1 
ATOM   13035 C  CE1   . PHE A 1 3094 ? 123.601 91.660  81.542  1.00 7.38   ? 3094 PHE A CE1   1 
ATOM   13036 C  CE2   . PHE A 1 3094 ? 122.463 89.713  80.754  1.00 8.95   ? 3094 PHE A CE2   1 
ATOM   13037 C  CZ    . PHE A 1 3094 ? 123.528 90.288  81.418  1.00 9.43   ? 3094 PHE A CZ    1 
ATOM   13038 N  N     . GLY A 1 3095 ? 118.422 95.283  79.659  1.00 6.24   ? 3095 GLY A N     1 
ATOM   13039 C  CA    . GLY A 1 3095 ? 117.437 96.105  78.989  1.00 6.68   ? 3095 GLY A CA    1 
ATOM   13040 C  C     . GLY A 1 3095 ? 117.119 95.597  77.596  1.00 10.98  ? 3095 GLY A C     1 
ATOM   13041 O  O     . GLY A 1 3095 ? 117.016 94.392  77.342  1.00 11.09  ? 3095 GLY A O     1 
ATOM   13042 N  N     . ASP A 1 3096 ? 116.958 96.540  76.677  1.00 11.64  ? 3096 ASP A N     1 
ATOM   13043 C  CA    . ASP A 1 3096 ? 116.742 96.241  75.271  1.00 11.75  ? 3096 ASP A CA    1 
ATOM   13044 C  C     . ASP A 1 3096 ? 118.048 96.404  74.505  1.00 11.17  ? 3096 ASP A C     1 
ATOM   13045 O  O     . ASP A 1 3096 ? 118.984 97.065  74.961  1.00 15.44  ? 3096 ASP A O     1 
ATOM   13046 C  CB    . ASP A 1 3096 ? 115.663 97.154  74.681  1.00 15.18  ? 3096 ASP A CB    1 
ATOM   13047 C  CG    . ASP A 1 3096 ? 115.046 96.590  73.415  1.00 21.51  ? 3096 ASP A CG    1 
ATOM   13048 O  OD1   . ASP A 1 3096 ? 115.649 95.682  72.804  1.00 19.76  ? 3096 ASP A OD1   1 
ATOM   13049 O  OD2   . ASP A 1 3096 ? 113.953 97.054  73.031  1.00 23.54  ? 3096 ASP A OD2   1 
ATOM   13050 N  N     . TRP A 1 3097 ? 118.109 95.777  73.331  1.00 10.79  ? 3097 TRP A N     1 
ATOM   13051 C  CA    . TRP A 1 3097 ? 119.272 95.946  72.473  1.00 11.16  ? 3097 TRP A CA    1 
ATOM   13052 C  C     . TRP A 1 3097 ? 119.377 97.398  72.029  1.00 14.11  ? 3097 TRP A C     1 
ATOM   13053 O  O     . TRP A 1 3097 ? 118.403 97.988  71.551  1.00 17.48  ? 3097 TRP A O     1 
ATOM   13054 C  CB    . TRP A 1 3097 ? 119.188 95.025  71.256  1.00 9.25   ? 3097 TRP A CB    1 
ATOM   13055 C  CG    . TRP A 1 3097 ? 119.460 93.581  71.557  1.00 9.11   ? 3097 TRP A CG    1 
ATOM   13056 C  CD1   . TRP A 1 3097 ? 119.615 93.014  72.787  1.00 7.61   ? 3097 TRP A CD1   1 
ATOM   13057 C  CD2   . TRP A 1 3097 ? 119.624 92.524  70.604  1.00 9.33   ? 3097 TRP A CD2   1 
ATOM   13058 N  NE1   . TRP A 1 3097 ? 119.855 91.667  72.661  1.00 7.74   ? 3097 TRP A NE1   1 
ATOM   13059 C  CE2   . TRP A 1 3097 ? 119.866 91.342  71.330  1.00 7.66   ? 3097 TRP A CE2   1 
ATOM   13060 C  CE3   . TRP A 1 3097 ? 119.584 92.462  69.208  1.00 7.77   ? 3097 TRP A CE3   1 
ATOM   13061 C  CZ2   . TRP A 1 3097 ? 120.069 90.112  70.708  1.00 7.97   ? 3097 TRP A CZ2   1 
ATOM   13062 C  CZ3   . TRP A 1 3097 ? 119.785 91.241  68.592  1.00 7.25   ? 3097 TRP A CZ3   1 
ATOM   13063 C  CH2   . TRP A 1 3097 ? 120.025 90.083  69.341  1.00 6.81   ? 3097 TRP A CH2   1 
ATOM   13064 N  N     . SER A 1 3098 ? 120.562 97.974  72.192  1.00 15.26  ? 3098 SER A N     1 
ATOM   13065 C  CA    . SER A 1 3098 ? 120.775 99.365  71.839  1.00 16.32  ? 3098 SER A CA    1 
ATOM   13066 C  C     . SER A 1 3098 ? 120.878 99.518  70.324  1.00 13.30  ? 3098 SER A C     1 
ATOM   13067 O  O     . SER A 1 3098 ? 120.885 98.543  69.568  1.00 11.89  ? 3098 SER A O     1 
ATOM   13068 C  CB    . SER A 1 3098 ? 122.037 99.901  72.512  1.00 17.28  ? 3098 SER A CB    1 
ATOM   13069 O  OG    . SER A 1 3098 ? 123.184 99.194  72.077  1.00 22.87  ? 3098 SER A OG    1 
ATOM   13070 N  N     . THR A 1 3099 ? 120.948 100.775 69.884  1.00 13.88  ? 3099 THR A N     1 
ATOM   13071 C  CA    . THR A 1 3099 ? 121.225 101.048 68.478  1.00 12.40  ? 3099 THR A CA    1 
ATOM   13072 C  C     . THR A 1 3099 ? 122.554 100.430 68.062  1.00 13.94  ? 3099 THR A C     1 
ATOM   13073 O  O     . THR A 1 3099 ? 122.686 99.904  66.950  1.00 14.20  ? 3099 THR A O     1 
ATOM   13074 C  CB    . THR A 1 3099 ? 121.219 102.558 68.233  1.00 13.75  ? 3099 THR A CB    1 
ATOM   13075 O  OG1   . THR A 1 3099 ? 119.920 103.083 68.535  1.00 18.07  ? 3099 THR A OG1   1 
ATOM   13076 C  CG2   . THR A 1 3099 ? 121.555 102.873 66.789  1.00 15.71  ? 3099 THR A CG2   1 
ATOM   13077 N  N     . GLU A 1 3100 ? 123.545 100.463 68.958  1.00 15.45  ? 3100 GLU A N     1 
ATOM   13078 C  CA    . GLU A 1 3100 ? 124.815 99.793  68.700  1.00 15.20  ? 3100 GLU A CA    1 
ATOM   13079 C  C     . GLU A 1 3100 ? 124.619 98.301  68.469  1.00 14.04  ? 3100 GLU A C     1 
ATOM   13080 O  O     . GLU A 1 3100 ? 125.156 97.738  67.507  1.00 14.06  ? 3100 GLU A O     1 
ATOM   13081 C  CB    . GLU A 1 3100 ? 125.770 100.015 69.873  1.00 22.29  ? 3100 GLU A CB    1 
ATOM   13082 C  CG    . GLU A 1 3100 ? 127.141 99.387  69.684  1.00 29.44  ? 3100 GLU A CG    1 
ATOM   13083 C  CD    . GLU A 1 3100 ? 127.911 100.016 68.548  1.00 42.17  ? 3100 GLU A CD    1 
ATOM   13084 O  OE1   . GLU A 1 3100 ? 127.642 101.191 68.241  1.00 45.32  ? 3100 GLU A OE1   1 
ATOM   13085 O  OE2   . GLU A 1 3100 ? 128.773 99.340  67.953  1.00 43.34  ? 3100 GLU A OE2   1 
ATOM   13086 N  N     . ALA A 1 3101 ? 123.863 97.642  69.351  1.00 12.66  ? 3101 ALA A N     1 
ATOM   13087 C  CA    . ALA A 1 3101 ? 123.662 96.203  69.227  1.00 10.03  ? 3101 ALA A CA    1 
ATOM   13088 C  C     . ALA A 1 3101 ? 122.931 95.858  67.938  1.00 9.65   ? 3101 ALA A C     1 
ATOM   13089 O  O     . ALA A 1 3101 ? 123.321 94.927  67.226  1.00 8.16   ? 3101 ALA A O     1 
ATOM   13090 C  CB    . ALA A 1 3101 ? 122.895 95.675  70.439  1.00 12.33  ? 3101 ALA A CB    1 
ATOM   13091 N  N     . LEU A 1 3102 ? 121.872 96.606  67.619  1.00 9.28   ? 3102 LEU A N     1 
ATOM   13092 C  CA    . LEU A 1 3102 ? 121.128 96.357  66.389  1.00 5.10   ? 3102 LEU A CA    1 
ATOM   13093 C  C     . LEU A 1 3102 ? 122.020 96.536  65.168  1.00 7.26   ? 3102 LEU A C     1 
ATOM   13094 O  O     . LEU A 1 3102 ? 122.003 95.711  64.246  1.00 6.91   ? 3102 LEU A O     1 
ATOM   13095 C  CB    . LEU A 1 3102 ? 119.927 97.299  66.316  1.00 4.94   ? 3102 LEU A CB    1 
ATOM   13096 C  CG    . LEU A 1 3102 ? 118.786 97.066  67.308  1.00 7.36   ? 3102 LEU A CG    1 
ATOM   13097 C  CD1   . LEU A 1 3102 ? 117.795 98.216  67.248  1.00 8.85   ? 3102 LEU A CD1   1 
ATOM   13098 C  CD2   . LEU A 1 3102 ? 118.088 95.743  67.049  1.00 4.76   ? 3102 LEU A CD2   1 
ATOM   13099 N  N     . TYR A 1 3103 ? 122.826 97.601  65.161  1.00 8.11   ? 3103 TYR A N     1 
ATOM   13100 C  CA    . TYR A 1 3103 ? 123.715 97.861  64.035  1.00 9.12   ? 3103 TYR A CA    1 
ATOM   13101 C  C     . TYR A 1 3103 ? 124.743 96.750  63.865  1.00 8.83   ? 3103 TYR A C     1 
ATOM   13102 O  O     . TYR A 1 3103 ? 124.983 96.282  62.746  1.00 10.83  ? 3103 TYR A O     1 
ATOM   13103 C  CB    . TYR A 1 3103 ? 124.412 99.204  64.240  1.00 12.88  ? 3103 TYR A CB    1 
ATOM   13104 C  CG    . TYR A 1 3103 ? 125.275 99.638  63.085  1.00 16.37  ? 3103 TYR A CG    1 
ATOM   13105 C  CD1   . TYR A 1 3103 ? 124.744 100.378 62.041  1.00 19.55  ? 3103 TYR A CD1   1 
ATOM   13106 C  CD2   . TYR A 1 3103 ? 126.622 99.306  63.038  1.00 17.99  ? 3103 TYR A CD2   1 
ATOM   13107 C  CE1   . TYR A 1 3103 ? 125.530 100.784 60.990  1.00 20.93  ? 3103 TYR A CE1   1 
ATOM   13108 C  CE2   . TYR A 1 3103 ? 127.416 99.701  61.986  1.00 22.29  ? 3103 TYR A CE2   1 
ATOM   13109 C  CZ    . TYR A 1 3103 ? 126.867 100.441 60.965  1.00 25.63  ? 3103 TYR A CZ    1 
ATOM   13110 O  OH    . TYR A 1 3103 ? 127.659 100.834 59.912  1.00 33.39  ? 3103 TYR A OH    1 
ATOM   13111 N  N     . GLN A 1 3104 ? 125.366 96.319  64.964  1.00 11.31  ? 3104 GLN A N     1 
ATOM   13112 C  CA    . GLN A 1 3104 ? 126.395 95.288  64.870  1.00 11.29  ? 3104 GLN A CA    1 
ATOM   13113 C  C     . GLN A 1 3104 ? 125.800 93.946  64.465  1.00 10.16  ? 3104 GLN A C     1 
ATOM   13114 O  O     . GLN A 1 3104 ? 126.412 93.197  63.690  1.00 10.53  ? 3104 GLN A O     1 
ATOM   13115 C  CB    . GLN A 1 3104 ? 127.147 95.176  66.194  1.00 10.33  ? 3104 GLN A CB    1 
ATOM   13116 C  CG    . GLN A 1 3104 ? 127.988 96.398  66.514  1.00 15.63  ? 3104 GLN A CG    1 
ATOM   13117 C  CD    . GLN A 1 3104 ? 128.724 96.281  67.832  1.00 22.57  ? 3104 GLN A CD    1 
ATOM   13118 O  OE1   . GLN A 1 3104 ? 128.571 95.302  68.559  1.00 28.84  ? 3104 GLN A OE1   1 
ATOM   13119 N  NE2   . GLN A 1 3104 ? 129.537 97.281  68.143  1.00 21.73  ? 3104 GLN A NE2   1 
ATOM   13120 N  N     . VAL A 1 3105 ? 124.608 93.624  64.975  1.00 7.90   ? 3105 VAL A N     1 
ATOM   13121 C  CA    . VAL A 1 3105 ? 123.939 92.394  64.565  1.00 7.64   ? 3105 VAL A CA    1 
ATOM   13122 C  C     . VAL A 1 3105 ? 123.629 92.434  63.077  1.00 9.68   ? 3105 VAL A C     1 
ATOM   13123 O  O     . VAL A 1 3105 ? 123.853 91.454  62.358  1.00 13.95  ? 3105 VAL A O     1 
ATOM   13124 C  CB    . VAL A 1 3105 ? 122.668 92.166  65.404  1.00 7.14   ? 3105 VAL A CB    1 
ATOM   13125 C  CG1   . VAL A 1 3105 ? 121.858 91.021  64.829  1.00 7.16   ? 3105 VAL A CG1   1 
ATOM   13126 C  CG2   . VAL A 1 3105 ? 123.036 91.867  66.841  1.00 8.63   ? 3105 VAL A CG2   1 
ATOM   13127 N  N     . GLY A 1 3106 ? 123.120 93.568  62.590  1.00 7.93   ? 3106 GLY A N     1 
ATOM   13128 C  CA    . GLY A 1 3106 ? 122.872 93.700  61.164  1.00 7.55   ? 3106 GLY A CA    1 
ATOM   13129 C  C     . GLY A 1 3106 ? 124.129 93.532  60.332  1.00 9.61   ? 3106 GLY A C     1 
ATOM   13130 O  O     . GLY A 1 3106 ? 124.127 92.814  59.330  1.00 13.52  ? 3106 GLY A O     1 
ATOM   13131 N  N     . LYS A 1 3107 ? 125.222 94.181  60.742  1.00 9.16   ? 3107 LYS A N     1 
ATOM   13132 C  CA    . LYS A 1 3107 ? 126.481 94.044  60.014  1.00 9.90   ? 3107 LYS A CA    1 
ATOM   13133 C  C     . LYS A 1 3107 ? 126.943 92.594  59.960  1.00 14.57  ? 3107 LYS A C     1 
ATOM   13134 O  O     . LYS A 1 3107 ? 127.268 92.078  58.885  1.00 20.10  ? 3107 LYS A O     1 
ATOM   13135 C  CB    . LYS A 1 3107 ? 127.563 94.921  60.642  1.00 13.77  ? 3107 LYS A CB    1 
ATOM   13136 C  CG    . LYS A 1 3107 ? 127.276 96.398  60.588  1.00 21.29  ? 3107 LYS A CG    1 
ATOM   13137 C  CD    . LYS A 1 3107 ? 127.241 96.860  59.145  1.00 24.18  ? 3107 LYS A CD    1 
ATOM   13138 C  CE    . LYS A 1 3107 ? 128.626 96.857  58.508  1.00 28.44  ? 3107 LYS A CE    1 
ATOM   13139 N  NZ    . LYS A 1 3107 ? 128.604 97.385  57.111  1.00 28.79  ? 3107 LYS A NZ    1 
ATOM   13140 N  N     . GLU A 1 3108 ? 126.978 91.913  61.104  1.00 13.47  ? 3108 GLU A N     1 
ATOM   13141 C  CA    . GLU A 1 3108 ? 127.500 90.552  61.091  1.00 17.92  ? 3108 GLU A CA    1 
ATOM   13142 C  C     . GLU A 1 3108 ? 126.574 89.597  60.351  1.00 18.46  ? 3108 GLU A C     1 
ATOM   13143 O  O     . GLU A 1 3108 ? 127.044 88.683  59.665  1.00 22.97  ? 3108 GLU A O     1 
ATOM   13144 C  CB    . GLU A 1 3108 ? 127.763 90.063  62.510  1.00 21.60  ? 3108 GLU A CB    1 
ATOM   13145 C  CG    . GLU A 1 3108 ? 128.891 90.808  63.184  1.00 27.55  ? 3108 GLU A CG    1 
ATOM   13146 C  CD    . GLU A 1 3108 ? 129.139 90.335  64.597  1.00 39.55  ? 3108 GLU A CD    1 
ATOM   13147 O  OE1   . GLU A 1 3108 ? 128.351 89.510  65.099  1.00 34.21  ? 3108 GLU A OE1   1 
ATOM   13148 O  OE2   . GLU A 1 3108 ? 130.131 90.794  65.211  1.00 39.20  ? 3108 GLU A OE2   1 
ATOM   13149 N  N     . PHE A 1 3109 ? 125.258 89.791  60.460  1.00 17.06  ? 3109 PHE A N     1 
ATOM   13150 C  CA    . PHE A 1 3109 ? 124.337 88.863  59.819  1.00 18.53  ? 3109 PHE A CA    1 
ATOM   13151 C  C     . PHE A 1 3109 ? 124.259 89.086  58.310  1.00 18.63  ? 3109 PHE A C     1 
ATOM   13152 O  O     . PHE A 1 3109 ? 124.031 88.130  57.559  1.00 27.19  ? 3109 PHE A O     1 
ATOM   13153 C  CB    . PHE A 1 3109 ? 122.954 88.982  60.454  1.00 13.89  ? 3109 PHE A CB    1 
ATOM   13154 C  CG    . PHE A 1 3109 ? 122.016 87.880  60.069  1.00 14.51  ? 3109 PHE A CG    1 
ATOM   13155 C  CD1   . PHE A 1 3109 ? 121.215 87.992  58.948  1.00 12.56  ? 3109 PHE A CD1   1 
ATOM   13156 C  CD2   . PHE A 1 3109 ? 121.929 86.731  60.838  1.00 13.60  ? 3109 PHE A CD2   1 
ATOM   13157 C  CE1   . PHE A 1 3109 ? 120.351 86.973  58.592  1.00 12.02  ? 3109 PHE A CE1   1 
ATOM   13158 C  CE2   . PHE A 1 3109 ? 121.064 85.711  60.491  1.00 13.53  ? 3109 PHE A CE2   1 
ATOM   13159 C  CZ    . PHE A 1 3109 ? 120.276 85.832  59.365  1.00 13.23  ? 3109 PHE A CZ    1 
ATOM   13160 N  N     . THR A 1 3110 ? 124.431 90.325  57.842  1.00 17.36  ? 3110 THR A N     1 
ATOM   13161 C  CA    . THR A 1 3110 ? 124.372 90.625  56.418  1.00 19.12  ? 3110 THR A CA    1 
ATOM   13162 C  C     . THR A 1 3110 ? 125.730 90.498  55.734  1.00 22.39  ? 3110 THR A C     1 
ATOM   13163 O  O     . THR A 1 3110 ? 125.912 91.029  54.633  1.00 25.68  ? 3110 THR A O     1 
ATOM   13164 C  CB    . THR A 1 3110 ? 123.805 92.029  56.194  1.00 18.70  ? 3110 THR A CB    1 
ATOM   13165 O  OG1   . THR A 1 3110 ? 124.617 92.991  56.877  1.00 24.29  ? 3110 THR A OG1   1 
ATOM   13166 C  CG2   . THR A 1 3110 ? 122.385 92.116  56.735  1.00 15.59  ? 3110 THR A CG2   1 
ATOM   13167 N  N     . SER A 1 3111 ? 126.690 89.821  56.369  1.00 22.03  ? 3111 SER A N     1 
ATOM   13168 C  CA    . SER A 1 3111 ? 127.999 89.638  55.753  1.00 25.34  ? 3111 SER A CA    1 
ATOM   13169 C  C     . SER A 1 3111 ? 127.906 88.778  54.498  1.00 28.10  ? 3111 SER A C     1 
ATOM   13170 O  O     . SER A 1 3111 ? 128.539 89.081  53.480  1.00 24.54  ? 3111 SER A O     1 
ATOM   13171 C  CB    . SER A 1 3111 ? 128.967 89.019  56.761  1.00 26.42  ? 3111 SER A CB    1 
ATOM   13172 O  OG    . SER A 1 3111 ? 129.069 89.824  57.922  1.00 29.75  ? 3111 SER A OG    1 
ATOM   13173 N  N     . LYS A 1 3112 ? 127.121 87.698  54.554  1.00 28.10  ? 3112 LYS A N     1 
ATOM   13174 C  CA    . LYS A 1 3112 ? 126.930 86.854  53.379  1.00 28.70  ? 3112 LYS A CA    1 
ATOM   13175 C  C     . LYS A 1 3112 ? 126.195 87.595  52.271  1.00 31.88  ? 3112 LYS A C     1 
ATOM   13176 O  O     . LYS A 1 3112 ? 126.312 87.231  51.095  1.00 33.48  ? 3112 LYS A O     1 
ATOM   13177 C  CB    . LYS A 1 3112 ? 126.164 85.589  53.765  1.00 38.35  ? 3112 LYS A CB    1 
ATOM   13178 C  CG    . LYS A 1 3112 ? 124.884 85.863  54.541  1.00 43.95  ? 3112 LYS A CG    1 
ATOM   13179 C  CD    . LYS A 1 3112 ? 124.247 84.580  55.047  1.00 54.85  ? 3112 LYS A CD    1 
ATOM   13180 C  CE    . LYS A 1 3112 ? 123.024 84.876  55.901  1.00 48.78  ? 3112 LYS A CE    1 
ATOM   13181 N  NZ    . LYS A 1 3112 ? 122.400 83.635  56.436  1.00 46.84  ? 3112 LYS A NZ    1 
ATOM   13182 N  N     . MET A 1 3113 ? 125.433 88.625  52.627  1.00 30.99  ? 3113 MET A N     1 
ATOM   13183 C  CA    . MET A 1 3113 ? 124.674 89.391  51.650  1.00 28.61  ? 3113 MET A CA    1 
ATOM   13184 C  C     . MET A 1 3113 ? 125.608 90.107  50.681  1.00 31.18  ? 3113 MET A C     1 
ATOM   13185 O  O     . MET A 1 3113 ? 126.704 90.544  51.044  1.00 34.67  ? 3113 MET A O     1 
ATOM   13186 C  CB    . MET A 1 3113 ? 123.788 90.409  52.365  1.00 25.32  ? 3113 MET A CB    1 
ATOM   13187 C  CG    . MET A 1 3113 ? 122.585 89.813  53.071  1.00 23.70  ? 3113 MET A CG    1 
ATOM   13188 S  SD    . MET A 1 3113 ? 121.412 91.087  53.561  1.00 37.60  ? 3113 MET A SD    1 
ATOM   13189 C  CE    . MET A 1 3113 ? 120.050 90.742  52.466  1.00 11.88  ? 3113 MET A CE    1 
ATOM   13190 N  N     . ASP A 1 3114 ? 125.163 90.223  49.430  1.00 34.09  ? 3114 ASP A N     1 
ATOM   13191 C  CA    . ASP A 1 3114 ? 125.899 90.960  48.405  1.00 34.59  ? 3114 ASP A CA    1 
ATOM   13192 C  C     . ASP A 1 3114 ? 125.255 92.341  48.318  1.00 32.37  ? 3114 ASP A C     1 
ATOM   13193 O  O     . ASP A 1 3114 ? 124.403 92.616  47.473  1.00 37.66  ? 3114 ASP A O     1 
ATOM   13194 C  CB    . ASP A 1 3114 ? 125.871 90.204  47.074  1.00 41.17  ? 3114 ASP A CB    1 
ATOM   13195 C  CG    . ASP A 1 3114 ? 126.627 90.921  45.955  1.00 51.18  ? 3114 ASP A CG    1 
ATOM   13196 O  OD1   . ASP A 1 3114 ? 126.642 92.169  45.901  1.00 46.32  ? 3114 ASP A OD1   1 
ATOM   13197 O  OD2   . ASP A 1 3114 ? 127.219 90.215  45.112  1.00 56.32  ? 3114 ASP A OD2   1 
ATOM   13198 N  N     . LEU A 1 3115 ? 125.672 93.220  49.230  1.00 29.39  ? 3115 LEU A N     1 
ATOM   13199 C  CA    . LEU A 1 3115 ? 125.128 94.568  49.339  1.00 25.91  ? 3115 LEU A CA    1 
ATOM   13200 C  C     . LEU A 1 3115 ? 126.081 95.625  48.793  1.00 30.15  ? 3115 LEU A C     1 
ATOM   13201 O  O     . LEU A 1 3115 ? 125.898 96.817  49.060  1.00 32.78  ? 3115 LEU A O     1 
ATOM   13202 C  CB    . LEU A 1 3115 ? 124.776 94.877  50.795  1.00 22.65  ? 3115 LEU A CB    1 
ATOM   13203 C  CG    . LEU A 1 3115 ? 123.801 93.913  51.471  1.00 27.09  ? 3115 LEU A CG    1 
ATOM   13204 C  CD1   . LEU A 1 3115 ? 123.556 94.318  52.915  1.00 19.86  ? 3115 LEU A CD1   1 
ATOM   13205 C  CD2   . LEU A 1 3115 ? 122.492 93.844  50.699  1.00 24.51  ? 3115 LEU A CD2   1 
ATOM   13206 N  N     . GLU A 1 3116 ? 127.095 95.214  48.036  1.00 35.19  ? 3116 GLU A N     1 
ATOM   13207 C  CA    . GLU A 1 3116 ? 128.102 96.143  47.541  1.00 37.24  ? 3116 GLU A CA    1 
ATOM   13208 C  C     . GLU A 1 3116 ? 127.596 96.838  46.282  1.00 36.22  ? 3116 GLU A C     1 
ATOM   13209 O  O     . GLU A 1 3116 ? 127.390 96.193  45.249  1.00 42.52  ? 3116 GLU A O     1 
ATOM   13210 C  CB    . GLU A 1 3116 ? 129.412 95.407  47.261  1.00 38.39  ? 3116 GLU A CB    1 
ATOM   13211 C  CG    . GLU A 1 3116 ? 130.153 94.857  48.491  1.00 40.89  ? 3116 GLU A CG    1 
ATOM   13212 C  CD    . GLU A 1 3116 ? 130.513 95.899  49.552  1.00 49.22  ? 3116 GLU A CD    1 
ATOM   13213 O  OE1   . GLU A 1 3116 ? 131.181 95.515  50.535  1.00 45.72  ? 3116 GLU A OE1   1 
ATOM   13214 O  OE2   . GLU A 1 3116 ? 130.178 97.094  49.407  1.00 48.21  ? 3116 GLU A OE2   1 
ATOM   13215 N  N     . LYS A 1 3117 ? 127.397 98.152  46.370  1.00 35.57  ? 3117 LYS A N     1 
ATOM   13216 C  CA    . LYS A 1 3117 ? 127.022 98.980  45.225  1.00 37.36  ? 3117 LYS A CA    1 
ATOM   13217 C  C     . LYS A 1 3117 ? 128.048 100.097 45.103  1.00 42.80  ? 3117 LYS A C     1 
ATOM   13218 O  O     . LYS A 1 3117 ? 127.915 101.151 45.741  1.00 42.25  ? 3117 LYS A O     1 
ATOM   13219 C  CB    . LYS A 1 3117 ? 125.608 99.536  45.371  1.00 33.77  ? 3117 LYS A CB    1 
ATOM   13220 C  CG    . LYS A 1 3117 ? 125.123 100.288 44.141  1.00 36.60  ? 3117 LYS A CG    1 
ATOM   13221 C  CD    . LYS A 1 3117 ? 123.614 100.470 44.142  1.00 30.24  ? 3117 LYS A CD    1 
ATOM   13222 C  CE    . LYS A 1 3117 ? 123.162 101.366 45.279  1.00 32.63  ? 3117 LYS A CE    1 
ATOM   13223 N  NZ    . LYS A 1 3117 ? 121.686 101.566 45.278  1.00 37.14  ? 3117 LYS A NZ    1 
ATOM   13224 N  N     . PRO A 1 3118 ? 129.095 99.898  44.298  1.00 45.53  ? 3118 PRO A N     1 
ATOM   13225 C  CA    . PRO A 1 3118 ? 130.125 100.942 44.159  1.00 47.94  ? 3118 PRO A CA    1 
ATOM   13226 C  C     . PRO A 1 3118 ? 129.606 102.238 43.564  1.00 47.08  ? 3118 PRO A C     1 
ATOM   13227 O  O     . PRO A 1 3118 ? 130.238 103.285 43.755  1.00 46.20  ? 3118 PRO A O     1 
ATOM   13228 C  CB    . PRO A 1 3118 ? 131.168 100.284 43.245  1.00 43.90  ? 3118 PRO A CB    1 
ATOM   13229 C  CG    . PRO A 1 3118 ? 130.412 99.221  42.512  1.00 45.36  ? 3118 PRO A CG    1 
ATOM   13230 C  CD    . PRO A 1 3118 ? 129.406 98.704  43.495  1.00 44.73  ? 3118 PRO A CD    1 
ATOM   13231 N  N     . ASN A 1 3119 ? 128.481 102.208 42.854  1.00 47.83  ? 3119 ASN A N     1 
ATOM   13232 C  CA    . ASN A 1 3119 ? 127.910 103.398 42.241  1.00 42.54  ? 3119 ASN A CA    1 
ATOM   13233 C  C     . ASN A 1 3119 ? 126.909 104.106 43.146  1.00 46.49  ? 3119 ASN A C     1 
ATOM   13234 O  O     . ASN A 1 3119 ? 126.215 105.017 42.685  1.00 48.83  ? 3119 ASN A O     1 
ATOM   13235 C  CB    . ASN A 1 3119 ? 127.248 103.038 40.907  1.00 46.50  ? 3119 ASN A CB    1 
ATOM   13236 C  CG    . ASN A 1 3119 ? 126.141 102.012 41.059  1.00 46.69  ? 3119 ASN A CG    1 
ATOM   13237 O  OD1   . ASN A 1 3119 ? 125.076 102.303 41.603  1.00 43.18  ? 3119 ASN A OD1   1 
ATOM   13238 N  ND2   . ASN A 1 3119 ? 126.389 100.800 40.576  1.00 53.06  ? 3119 ASN A ND2   1 
ATOM   13239 N  N     . TYR A 1 3120 ? 126.808 103.701 44.409  1.00 40.62  ? 3120 TYR A N     1 
ATOM   13240 C  CA    . TYR A 1 3120 ? 125.886 104.340 45.337  1.00 35.70  ? 3120 TYR A CA    1 
ATOM   13241 C  C     . TYR A 1 3120 ? 126.342 105.760 45.655  1.00 36.34  ? 3120 TYR A C     1 
ATOM   13242 O  O     . TYR A 1 3120 ? 127.534 106.021 45.840  1.00 41.45  ? 3120 TYR A O     1 
ATOM   13243 C  CB    . TYR A 1 3120 ? 125.781 103.514 46.620  1.00 34.34  ? 3120 TYR A CB    1 
ATOM   13244 C  CG    . TYR A 1 3120 ? 125.057 104.197 47.758  1.00 30.62  ? 3120 TYR A CG    1 
ATOM   13245 C  CD1   . TYR A 1 3120 ? 123.670 104.258 47.788  1.00 29.75  ? 3120 TYR A CD1   1 
ATOM   13246 C  CD2   . TYR A 1 3120 ? 125.760 104.768 48.810  1.00 26.82  ? 3120 TYR A CD2   1 
ATOM   13247 C  CE1   . TYR A 1 3120 ? 123.005 104.877 48.828  1.00 26.23  ? 3120 TYR A CE1   1 
ATOM   13248 C  CE2   . TYR A 1 3120 ? 125.103 105.389 49.855  1.00 25.38  ? 3120 TYR A CE2   1 
ATOM   13249 C  CZ    . TYR A 1 3120 ? 123.726 105.440 49.859  1.00 25.82  ? 3120 TYR A CZ    1 
ATOM   13250 O  OH    . TYR A 1 3120 ? 123.067 106.057 50.897  1.00 28.79  ? 3120 TYR A OH    1 
ATOM   13251 N  N     . ILE A 1 3121 ? 125.383 106.682 45.720  1.00 30.43  ? 3121 ILE A N     1 
ATOM   13252 C  CA    . ILE A 1 3121 ? 125.644 108.083 46.036  1.00 35.78  ? 3121 ILE A CA    1 
ATOM   13253 C  C     . ILE A 1 3121 ? 125.118 108.364 47.435  1.00 34.82  ? 3121 ILE A C     1 
ATOM   13254 O  O     . ILE A 1 3121 ? 123.952 108.080 47.735  1.00 37.65  ? 3121 ILE A O     1 
ATOM   13255 C  CB    . ILE A 1 3121 ? 124.998 109.041 45.017  1.00 41.35  ? 3121 ILE A CB    1 
ATOM   13256 C  CG1   . ILE A 1 3121 ? 125.574 108.847 43.611  1.00 38.36  ? 3121 ILE A CG1   1 
ATOM   13257 C  CG2   . ILE A 1 3121 ? 125.168 110.487 45.462  1.00 37.89  ? 3121 ILE A CG2   1 
ATOM   13258 C  CD1   . ILE A 1 3121 ? 124.851 107.812 42.781  1.00 39.44  ? 3121 ILE A CD1   1 
ATOM   13259 N  N     . VAL A 1 3122 ? 125.973 108.920 48.287  1.00 35.91  ? 3122 VAL A N     1 
ATOM   13260 C  CA    . VAL A 1 3122 ? 125.570 109.319 49.632  1.00 36.40  ? 3122 VAL A CA    1 
ATOM   13261 C  C     . VAL A 1 3122 ? 124.689 110.558 49.531  1.00 43.60  ? 3122 VAL A C     1 
ATOM   13262 O  O     . VAL A 1 3122 ? 125.106 111.569 48.947  1.00 51.97  ? 3122 VAL A O     1 
ATOM   13263 C  CB    . VAL A 1 3122 ? 126.790 109.583 50.528  1.00 37.87  ? 3122 VAL A CB    1 
ATOM   13264 C  CG1   . VAL A 1 3122 ? 126.344 110.099 51.888  1.00 46.65  ? 3122 VAL A CG1   1 
ATOM   13265 C  CG2   . VAL A 1 3122 ? 127.620 108.321 50.678  1.00 35.54  ? 3122 VAL A CG2   1 
ATOM   13266 N  N     . PRO A 1 3123 ? 123.474 110.528 50.073  1.00 41.93  ? 3123 PRO A N     1 
ATOM   13267 C  CA    . PRO A 1 3123 ? 122.628 111.725 50.051  1.00 44.87  ? 3123 PRO A CA    1 
ATOM   13268 C  C     . PRO A 1 3123 ? 123.203 112.828 50.925  1.00 55.76  ? 3123 PRO A C     1 
ATOM   13269 O  O     . PRO A 1 3123 ? 123.932 112.585 51.890  1.00 60.68  ? 3123 PRO A O     1 
ATOM   13270 C  CB    . PRO A 1 3123 ? 121.289 111.221 50.601  1.00 45.91  ? 3123 PRO A CB    1 
ATOM   13271 C  CG    . PRO A 1 3123 ? 121.656 110.041 51.439  1.00 37.38  ? 3123 PRO A CG    1 
ATOM   13272 C  CD    . PRO A 1 3123 ? 122.812 109.393 50.735  1.00 36.27  ? 3123 PRO A CD    1 
ATOM   13273 N  N     . ASP A 1 3124 ? 122.869 114.069 50.559  1.00 60.23  ? 3124 ASP A N     1 
ATOM   13274 C  CA    . ASP A 1 3124 ? 123.324 115.215 51.340  1.00 64.63  ? 3124 ASP A CA    1 
ATOM   13275 C  C     . ASP A 1 3124 ? 122.780 115.161 52.762  1.00 65.34  ? 3124 ASP A C     1 
ATOM   13276 O  O     . ASP A 1 3124 ? 123.508 115.427 53.725  1.00 66.93  ? 3124 ASP A O     1 
ATOM   13277 C  CB    . ASP A 1 3124 ? 122.912 116.516 50.654  1.00 65.09  ? 3124 ASP A CB    1 
ATOM   13278 C  CG    . ASP A 1 3124 ? 123.459 116.630 49.245  1.00 71.04  ? 3124 ASP A CG    1 
ATOM   13279 O  OD1   . ASP A 1 3124 ? 124.697 116.609 49.083  1.00 71.36  ? 3124 ASP A OD1   1 
ATOM   13280 O  OD2   . ASP A 1 3124 ? 122.651 116.742 48.299  1.00 78.06  ? 3124 ASP A OD2   1 
ATOM   13281 N  N     . TYR A 1 3125 ? 121.504 114.819 52.913  1.00 64.21  ? 3125 TYR A N     1 
ATOM   13282 C  CA    . TYR A 1 3125 ? 120.889 114.600 54.219  1.00 64.89  ? 3125 TYR A CA    1 
ATOM   13283 C  C     . TYR A 1 3125 ? 120.703 113.095 54.376  1.00 62.89  ? 3125 TYR A C     1 
ATOM   13284 O  O     . TYR A 1 3125 ? 119.751 112.517 53.845  1.00 53.65  ? 3125 TYR A O     1 
ATOM   13285 C  CB    . TYR A 1 3125 ? 119.569 115.358 54.343  1.00 64.15  ? 3125 TYR A CB    1 
ATOM   13286 C  CG    . TYR A 1 3125 ? 118.762 115.006 55.576  1.00 69.45  ? 3125 TYR A CG    1 
ATOM   13287 C  CD1   . TYR A 1 3125 ? 119.000 115.643 56.787  1.00 62.93  ? 3125 TYR A CD1   1 
ATOM   13288 C  CD2   . TYR A 1 3125 ? 117.749 114.056 55.525  1.00 68.94  ? 3125 TYR A CD2   1 
ATOM   13289 C  CE1   . TYR A 1 3125 ? 118.265 115.330 57.916  1.00 68.19  ? 3125 TYR A CE1   1 
ATOM   13290 C  CE2   . TYR A 1 3125 ? 117.009 113.738 56.647  1.00 68.17  ? 3125 TYR A CE2   1 
ATOM   13291 C  CZ    . TYR A 1 3125 ? 117.271 114.378 57.840  1.00 72.23  ? 3125 TYR A CZ    1 
ATOM   13292 O  OH    . TYR A 1 3125 ? 116.535 114.065 58.959  1.00 73.27  ? 3125 TYR A OH    1 
ATOM   13293 N  N     . MET A 1 3126 ? 121.629 112.461 55.090  1.00 59.30  ? 3126 MET A N     1 
ATOM   13294 C  CA    . MET A 1 3126 ? 121.559 111.027 55.328  1.00 55.98  ? 3126 MET A CA    1 
ATOM   13295 C  C     . MET A 1 3126 ? 120.628 110.753 56.500  1.00 54.84  ? 3126 MET A C     1 
ATOM   13296 O  O     . MET A 1 3126 ? 120.835 111.318 57.583  1.00 46.61  ? 3126 MET A O     1 
ATOM   13297 C  CB    . MET A 1 3126 ? 122.940 110.462 55.614  1.00 48.83  ? 3126 MET A CB    1 
ATOM   13298 C  CG    . MET A 1 3126 ? 122.984 108.947 55.733  1.00 46.51  ? 3126 MET A CG    1 
ATOM   13299 S  SD    . MET A 1 3126 ? 123.140 108.120 54.139  1.00 61.60  ? 3126 MET A SD    1 
ATOM   13300 C  CE    . MET A 1 3126 ? 122.294 106.580 54.476  1.00 32.33  ? 3126 MET A CE    1 
ATOM   13301 N  N     . PRO A 1 3127 ? 119.604 109.912 56.340  1.00 48.37  ? 3127 PRO A N     1 
ATOM   13302 C  CA    . PRO A 1 3127 ? 118.710 109.618 57.468  1.00 43.12  ? 3127 PRO A CA    1 
ATOM   13303 C  C     . PRO A 1 3127 ? 119.397 108.764 58.521  1.00 45.31  ? 3127 PRO A C     1 
ATOM   13304 O  O     . PRO A 1 3127 ? 119.097 107.575 58.672  1.00 39.04  ? 3127 PRO A O     1 
ATOM   13305 C  CB    . PRO A 1 3127 ? 117.545 108.881 56.801  1.00 33.60  ? 3127 PRO A CB    1 
ATOM   13306 C  CG    . PRO A 1 3127 ? 118.177 108.192 55.639  1.00 30.52  ? 3127 PRO A CG    1 
ATOM   13307 C  CD    . PRO A 1 3127 ? 119.270 109.114 55.147  1.00 33.59  ? 3127 PRO A CD    1 
ATOM   13308 N  N     . VAL A 1 3128 ? 120.321 109.374 59.256  1.00 48.10  ? 3128 VAL A N     1 
ATOM   13309 C  CA    . VAL A 1 3128 ? 121.179 108.644 60.181  1.00 46.95  ? 3128 VAL A CA    1 
ATOM   13310 C  C     . VAL A 1 3128 ? 120.406 108.322 61.452  1.00 44.66  ? 3128 VAL A C     1 
ATOM   13311 O  O     . VAL A 1 3128 ? 119.836 109.213 62.093  1.00 39.25  ? 3128 VAL A O     1 
ATOM   13312 C  CB    . VAL A 1 3128 ? 122.446 109.455 60.497  1.00 48.34  ? 3128 VAL A CB    1 
ATOM   13313 C  CG1   . VAL A 1 3128 ? 123.284 108.740 61.536  1.00 42.08  ? 3128 VAL A CG1   1 
ATOM   13314 C  CG2   . VAL A 1 3128 ? 123.253 109.696 59.235  1.00 51.79  ? 3128 VAL A CG2   1 
ATOM   13315 N  N     . VAL A 1 3129 ? 120.387 107.043 61.818  1.00 41.68  ? 3129 VAL A N     1 
ATOM   13316 C  CA    . VAL A 1 3129 ? 119.885 106.622 63.118  1.00 36.18  ? 3129 VAL A CA    1 
ATOM   13317 C  C     . VAL A 1 3129 ? 120.974 106.035 64.004  1.00 31.56  ? 3129 VAL A C     1 
ATOM   13318 O  O     . VAL A 1 3129 ? 120.741 105.861 65.212  1.00 29.00  ? 3129 VAL A O     1 
ATOM   13319 C  CB    . VAL A 1 3129 ? 118.721 105.619 62.971  1.00 32.08  ? 3129 VAL A CB    1 
ATOM   13320 C  CG1   . VAL A 1 3129 ? 117.567 106.256 62.214  1.00 28.93  ? 3129 VAL A CG1   1 
ATOM   13321 C  CG2   . VAL A 1 3129 ? 119.191 104.355 62.273  1.00 17.38  ? 3129 VAL A CG2   1 
ATOM   13322 N  N     . TYR A 1 3130 ? 122.147 105.723 63.460  1.00 33.23  ? 3130 TYR A N     1 
ATOM   13323 C  CA    . TYR A 1 3130 ? 123.265 105.183 64.222  1.00 29.61  ? 3130 TYR A CA    1 
ATOM   13324 C  C     . TYR A 1 3130 ? 124.295 106.288 64.427  1.00 36.25  ? 3130 TYR A C     1 
ATOM   13325 O  O     . TYR A 1 3130 ? 124.833 106.824 63.453  1.00 38.87  ? 3130 TYR A O     1 
ATOM   13326 C  CB    . TYR A 1 3130 ? 123.887 103.995 63.491  1.00 25.46  ? 3130 TYR A CB    1 
ATOM   13327 C  CG    . TYR A 1 3130 ? 125.094 103.413 64.181  1.00 27.93  ? 3130 TYR A CG    1 
ATOM   13328 C  CD1   . TYR A 1 3130 ? 125.128 103.278 65.559  1.00 27.56  ? 3130 TYR A CD1   1 
ATOM   13329 C  CD2   . TYR A 1 3130 ? 126.202 103.004 63.455  1.00 25.18  ? 3130 TYR A CD2   1 
ATOM   13330 C  CE1   . TYR A 1 3130 ? 126.227 102.750 66.192  1.00 26.60  ? 3130 TYR A CE1   1 
ATOM   13331 C  CE2   . TYR A 1 3130 ? 127.307 102.472 64.080  1.00 25.46  ? 3130 TYR A CE2   1 
ATOM   13332 C  CZ    . TYR A 1 3130 ? 127.315 102.346 65.449  1.00 29.75  ? 3130 TYR A CZ    1 
ATOM   13333 O  OH    . TYR A 1 3130 ? 128.419 101.816 66.077  1.00 31.01  ? 3130 TYR A OH    1 
ATOM   13334 N  N     . ASP A 1 3131 ? 124.581 106.611 65.692  1.00 40.41  ? 3131 ASP A N     1 
ATOM   13335 C  CA    . ASP A 1 3131 ? 125.420 107.769 65.989  1.00 46.09  ? 3131 ASP A CA    1 
ATOM   13336 C  C     . ASP A 1 3131 ? 126.829 107.610 65.427  1.00 43.24  ? 3131 ASP A C     1 
ATOM   13337 O  O     . ASP A 1 3131 ? 127.363 108.538 64.807  1.00 40.77  ? 3131 ASP A O     1 
ATOM   13338 C  CB    . ASP A 1 3131 ? 125.466 108.010 67.498  1.00 47.95  ? 3131 ASP A CB    1 
ATOM   13339 C  CG    . ASP A 1 3131 ? 124.120 108.423 68.062  1.00 60.23  ? 3131 ASP A CG    1 
ATOM   13340 O  OD1   . ASP A 1 3131 ? 123.938 108.336 69.295  1.00 62.38  ? 3131 ASP A OD1   1 
ATOM   13341 O  OD2   . ASP A 1 3131 ? 123.243 108.833 67.273  1.00 58.06  ? 3131 ASP A OD2   1 
ATOM   13342 N  N     . LYS A 1 3132 ? 127.449 106.447 65.627  1.00 36.89  ? 3132 LYS A N     1 
ATOM   13343 C  CA    . LYS A 1 3132 ? 128.799 106.203 65.135  1.00 38.02  ? 3132 LYS A CA    1 
ATOM   13344 C  C     . LYS A 1 3132 ? 128.824 105.566 63.748  1.00 34.15  ? 3132 LYS A C     1 
ATOM   13345 O  O     . LYS A 1 3132 ? 129.780 104.855 63.419  1.00 36.35  ? 3132 LYS A O     1 
ATOM   13346 C  CB    . LYS A 1 3132 ? 129.590 105.353 66.133  1.00 38.64  ? 3132 LYS A CB    1 
ATOM   13347 C  CG    . LYS A 1 3132 ? 129.418 105.783 67.583  1.00 45.05  ? 3132 LYS A CG    1 
ATOM   13348 C  CD    . LYS A 1 3132 ? 130.273 104.948 68.524  1.00 51.70  ? 3132 LYS A CD    1 
ATOM   13349 C  CE    . LYS A 1 3132 ? 129.749 103.533 68.656  1.00 53.74  ? 3132 LYS A CE    1 
ATOM   13350 N  NZ    . LYS A 1 3132 ? 128.559 103.485 69.551  1.00 49.57  ? 3132 LYS A NZ    1 
ATOM   13351 N  N     . LEU A 1 3133 ? 127.799 105.799 62.937  1.00 35.65  ? 3133 LEU A N     1 
ATOM   13352 C  CA    . LEU A 1 3133 ? 127.860 105.424 61.529  1.00 33.41  ? 3133 LEU A CA    1 
ATOM   13353 C  C     . LEU A 1 3133 ? 128.927 106.260 60.830  1.00 36.34  ? 3133 LEU A C     1 
ATOM   13354 O  O     . LEU A 1 3133 ? 129.021 107.467 61.084  1.00 43.53  ? 3133 LEU A O     1 
ATOM   13355 C  CB    . LEU A 1 3133 ? 126.499 105.633 60.864  1.00 30.80  ? 3133 LEU A CB    1 
ATOM   13356 C  CG    . LEU A 1 3133 ? 126.323 105.237 59.395  1.00 30.18  ? 3133 LEU A CG    1 
ATOM   13357 C  CD1   . LEU A 1 3133 ? 126.473 103.738 59.199  1.00 26.84  ? 3133 LEU A CD1   1 
ATOM   13358 C  CD2   . LEU A 1 3133 ? 124.977 105.712 58.873  1.00 30.40  ? 3133 LEU A CD2   1 
ATOM   13359 N  N     . PRO A 1 3134 ? 129.756 105.664 59.973  1.00 32.83  ? 3134 PRO A N     1 
ATOM   13360 C  CA    . PRO A 1 3134 ? 130.786 106.445 59.280  1.00 41.56  ? 3134 PRO A CA    1 
ATOM   13361 C  C     . PRO A 1 3134 ? 130.186 107.591 58.479  1.00 50.67  ? 3134 PRO A C     1 
ATOM   13362 O  O     . PRO A 1 3134 ? 129.106 107.474 57.895  1.00 49.71  ? 3134 PRO A O     1 
ATOM   13363 C  CB    . PRO A 1 3134 ? 131.445 105.410 58.367  1.00 39.72  ? 3134 PRO A CB    1 
ATOM   13364 C  CG    . PRO A 1 3134 ? 131.359 104.158 59.173  1.00 37.06  ? 3134 PRO A CG    1 
ATOM   13365 C  CD    . PRO A 1 3134 ? 129.975 104.217 59.794  1.00 36.00  ? 3134 PRO A CD    1 
ATOM   13366 N  N     . GLN A 1 3135 ? 130.903 108.716 58.471  1.00 56.36  ? 3135 GLN A N     1 
ATOM   13367 C  CA    . GLN A 1 3135 ? 130.409 109.912 57.789  1.00 55.75  ? 3135 GLN A CA    1 
ATOM   13368 C  C     . GLN A 1 3135 ? 130.202 109.707 56.292  1.00 59.52  ? 3135 GLN A C     1 
ATOM   13369 O  O     . GLN A 1 3135 ? 129.193 110.207 55.766  1.00 60.17  ? 3135 GLN A O     1 
ATOM   13370 C  CB    . GLN A 1 3135 ? 131.347 111.092 58.072  1.00 63.47  ? 3135 GLN A CB    1 
ATOM   13371 C  CG    . GLN A 1 3135 ? 131.455 111.465 59.542  1.00 71.01  ? 3135 GLN A CG    1 
ATOM   13372 C  CD    . GLN A 1 3135 ? 130.117 111.836 60.150  1.00 73.42  ? 3135 GLN A CD    1 
ATOM   13373 O  OE1   . GLN A 1 3135 ? 129.430 112.735 59.665  1.00 75.83  ? 3135 GLN A OE1   1 
ATOM   13374 N  NE2   . GLN A 1 3135 ? 129.740 111.145 61.220  1.00 68.61  ? 3135 GLN A NE2   1 
ATOM   13375 N  N     . PRO A 1 3136 ? 131.114 109.087 55.542  1.00 60.56  ? 3136 PRO A N     1 
ATOM   13376 C  CA    . PRO A 1 3136 ? 130.793 108.671 54.169  1.00 51.29  ? 3136 PRO A CA    1 
ATOM   13377 C  C     . PRO A 1 3136 ? 130.288 107.239 54.125  1.00 50.32  ? 3136 PRO A C     1 
ATOM   13378 O  O     . PRO A 1 3136 ? 131.062 106.317 53.824  1.00 53.56  ? 3136 PRO A O     1 
ATOM   13379 C  CB    . PRO A 1 3136 ? 132.135 108.814 53.439  1.00 49.47  ? 3136 PRO A CB    1 
ATOM   13380 C  CG    . PRO A 1 3136 ? 133.170 108.595 54.505  1.00 59.99  ? 3136 PRO A CG    1 
ATOM   13381 C  CD    . PRO A 1 3136 ? 132.527 108.805 55.861  1.00 58.12  ? 3136 PRO A CD    1 
ATOM   13382 N  N     . PRO A 1 3137 ? 129.010 106.997 54.424  1.00 45.46  ? 3137 PRO A N     1 
ATOM   13383 C  CA    . PRO A 1 3137 ? 128.537 105.613 54.521  1.00 38.67  ? 3137 PRO A CA    1 
ATOM   13384 C  C     . PRO A 1 3137 ? 128.575 104.906 53.175  1.00 34.26  ? 3137 PRO A C     1 
ATOM   13385 O  O     . PRO A 1 3137 ? 128.383 105.514 52.120  1.00 42.06  ? 3137 PRO A O     1 
ATOM   13386 C  CB    . PRO A 1 3137 ? 127.100 105.765 55.027  1.00 39.14  ? 3137 PRO A CB    1 
ATOM   13387 C  CG    . PRO A 1 3137 ? 126.666 107.064 54.469  1.00 41.85  ? 3137 PRO A CG    1 
ATOM   13388 C  CD    . PRO A 1 3137 ? 127.886 107.950 54.424  1.00 46.33  ? 3137 PRO A CD    1 
ATOM   13389 N  N     . SER A 1 3138 ? 128.830 103.603 53.223  1.00 30.09  ? 3138 SER A N     1 
ATOM   13390 C  CA    . SER A 1 3138 ? 128.739 102.759 52.045  1.00 27.49  ? 3138 SER A CA    1 
ATOM   13391 C  C     . SER A 1 3138 ? 127.307 102.256 51.875  1.00 25.61  ? 3138 SER A C     1 
ATOM   13392 O  O     . SER A 1 3138 ? 126.436 102.488 52.717  1.00 28.93  ? 3138 SER A O     1 
ATOM   13393 C  CB    . SER A 1 3138 ? 129.717 101.588 52.144  1.00 27.60  ? 3138 SER A CB    1 
ATOM   13394 O  OG    . SER A 1 3138 ? 129.331 100.686 53.165  1.00 30.94  ? 3138 SER A OG    1 
ATOM   13395 N  N     . HIS A 1 3139 ? 127.065 101.565 50.759  1.00 25.07  ? 3139 HIS A N     1 
ATOM   13396 C  CA    . HIS A 1 3139 ? 125.724 101.053 50.489  1.00 21.19  ? 3139 HIS A CA    1 
ATOM   13397 C  C     . HIS A 1 3139 ? 125.299 100.032 51.537  1.00 21.36  ? 3139 HIS A C     1 
ATOM   13398 O  O     . HIS A 1 3139 ? 124.154 100.050 52.004  1.00 24.32  ? 3139 HIS A O     1 
ATOM   13399 C  CB    . HIS A 1 3139 ? 125.663 100.445 49.089  1.00 22.78  ? 3139 HIS A CB    1 
ATOM   13400 C  CG    . HIS A 1 3139 ? 124.335 99.843  48.752  1.00 21.83  ? 3139 HIS A CG    1 
ATOM   13401 N  ND1   . HIS A 1 3139 ? 124.150 98.486  48.595  1.00 16.51  ? 3139 HIS A ND1   1 
ATOM   13402 C  CD2   . HIS A 1 3139 ? 123.123 100.413 48.555  1.00 20.62  ? 3139 HIS A CD2   1 
ATOM   13403 C  CE1   . HIS A 1 3139 ? 122.883 98.247  48.308  1.00 22.80  ? 3139 HIS A CE1   1 
ATOM   13404 N  NE2   . HIS A 1 3139 ? 122.238 99.399  48.278  1.00 21.34  ? 3139 HIS A NE2   1 
ATOM   13405 N  N     . ARG A 1 3140 ? 126.208 99.132  51.920  1.00 19.84  ? 3140 ARG A N     1 
ATOM   13406 C  CA    . ARG A 1 3140 ? 125.906 98.166  52.972  1.00 19.14  ? 3140 ARG A CA    1 
ATOM   13407 C  C     . ARG A 1 3140 ? 125.645 98.865  54.301  1.00 17.69  ? 3140 ARG A C     1 
ATOM   13408 O  O     . ARG A 1 3140 ? 124.750 98.469  55.062  1.00 20.39  ? 3140 ARG A O     1 
ATOM   13409 C  CB    . ARG A 1 3140 ? 127.057 97.169  53.104  1.00 20.95  ? 3140 ARG A CB    1 
ATOM   13410 C  CG    . ARG A 1 3140 ? 126.795 96.016  54.053  1.00 21.55  ? 3140 ARG A CG    1 
ATOM   13411 C  CD    . ARG A 1 3140 ? 128.062 95.205  54.282  1.00 22.93  ? 3140 ARG A CD    1 
ATOM   13412 N  NE    . ARG A 1 3140 ? 128.451 94.439  53.103  1.00 24.04  ? 3140 ARG A NE    1 
ATOM   13413 C  CZ    . ARG A 1 3140 ? 127.867 93.316  52.711  1.00 23.56  ? 3140 ARG A CZ    1 
ATOM   13414 N  NH1   . ARG A 1 3140 ? 126.859 92.788  53.385  1.00 23.35  ? 3140 ARG A NH1   1 
ATOM   13415 N  NH2   . ARG A 1 3140 ? 128.307 92.704  51.614  1.00 25.95  ? 3140 ARG A NH2   1 
ATOM   13416 N  N     . GLU A 1 3141 ? 126.431 99.902  54.600  1.00 19.96  ? 3141 GLU A N     1 
ATOM   13417 C  CA    . GLU A 1 3141 ? 126.222 100.654 55.830  1.00 21.85  ? 3141 GLU A CA    1 
ATOM   13418 C  C     . GLU A 1 3141 ? 124.858 101.332 55.832  1.00 18.10  ? 3141 GLU A C     1 
ATOM   13419 O  O     . GLU A 1 3141 ? 124.152 101.320 56.848  1.00 18.02  ? 3141 GLU A O     1 
ATOM   13420 C  CB    . GLU A 1 3141 ? 127.347 101.670 56.024  1.00 24.19  ? 3141 GLU A CB    1 
ATOM   13421 C  CG    . GLU A 1 3141 ? 128.698 101.020 56.286  1.00 25.94  ? 3141 GLU A CG    1 
ATOM   13422 C  CD    . GLU A 1 3141 ? 129.818 102.025 56.460  1.00 43.21  ? 3141 GLU A CD    1 
ATOM   13423 O  OE1   . GLU A 1 3141 ? 129.575 103.230 56.255  1.00 46.43  ? 3141 GLU A OE1   1 
ATOM   13424 O  OE2   . GLU A 1 3141 ? 130.946 101.609 56.796  1.00 49.82  ? 3141 GLU A OE2   1 
ATOM   13425 N  N     . ALA A 1 3142 ? 124.461 101.903 54.693  1.00 17.34  ? 3142 ALA A N     1 
ATOM   13426 C  CA    . ALA A 1 3142 ? 123.129 102.486 54.581  1.00 13.58  ? 3142 ALA A CA    1 
ATOM   13427 C  C     . ALA A 1 3142 ? 122.048 101.426 54.751  1.00 14.05  ? 3142 ALA A C     1 
ATOM   13428 O  O     . ALA A 1 3142 ? 121.015 101.680 55.381  1.00 13.68  ? 3142 ALA A O     1 
ATOM   13429 C  CB    . ALA A 1 3142 ? 122.980 103.197 53.237  1.00 16.90  ? 3142 ALA A CB    1 
ATOM   13430 N  N     . ILE A 1 3143 ? 122.271 100.229 54.202  1.00 11.17  ? 3143 ILE A N     1 
ATOM   13431 C  CA    . ILE A 1 3143 ? 121.284 99.156  54.308  1.00 10.92  ? 3143 ILE A CA    1 
ATOM   13432 C  C     . ILE A 1 3143 ? 121.064 98.776  55.769  1.00 11.31  ? 3143 ILE A C     1 
ATOM   13433 O  O     . ILE A 1 3143 ? 119.925 98.677  56.243  1.00 11.75  ? 3143 ILE A O     1 
ATOM   13434 C  CB    . ILE A 1 3143 ? 121.724 97.940  53.472  1.00 13.44  ? 3143 ILE A CB    1 
ATOM   13435 C  CG1   . ILE A 1 3143 ? 121.545 98.208  51.975  1.00 14.75  ? 3143 ILE A CG1   1 
ATOM   13436 C  CG2   . ILE A 1 3143 ? 120.946 96.700  53.885  1.00 9.61   ? 3143 ILE A CG2   1 
ATOM   13437 C  CD1   . ILE A 1 3143 ? 120.115 98.131  51.495  1.00 13.56  ? 3143 ILE A CD1   1 
ATOM   13438 N  N     . VAL A 1 3144 ? 122.155 98.561  56.507  1.00 10.74  ? 3144 VAL A N     1 
ATOM   13439 C  CA    . VAL A 1 3144 ? 122.020 98.147  57.903  1.00 9.47   ? 3144 VAL A CA    1 
ATOM   13440 C  C     . VAL A 1 3144 ? 121.455 99.284  58.752  1.00 9.12   ? 3144 VAL A C     1 
ATOM   13441 O  O     . VAL A 1 3144 ? 120.663 99.054  59.679  1.00 8.61   ? 3144 VAL A O     1 
ATOM   13442 C  CB    . VAL A 1 3144 ? 123.367 97.634  58.445  1.00 9.80   ? 3144 VAL A CB    1 
ATOM   13443 C  CG1   . VAL A 1 3144 ? 123.254 97.275  59.919  1.00 8.11   ? 3144 VAL A CG1   1 
ATOM   13444 C  CG2   . VAL A 1 3144 ? 123.841 96.436  57.637  1.00 12.29  ? 3144 VAL A CG2   1 
ATOM   13445 N  N     . ASN A 1 3145 ? 121.843 100.528 58.450  1.00 8.96   ? 3145 ASN A N     1 
ATOM   13446 C  CA    . ASN A 1 3145 ? 121.266 101.671 59.150  1.00 8.77   ? 3145 ASN A CA    1 
ATOM   13447 C  C     . ASN A 1 3145 ? 119.759 101.742 58.935  1.00 8.33   ? 3145 ASN A C     1 
ATOM   13448 O  O     . ASN A 1 3145 ? 118.999 102.013 59.872  1.00 7.15   ? 3145 ASN A O     1 
ATOM   13449 C  CB    . ASN A 1 3145 ? 121.940 102.961 58.679  1.00 8.75   ? 3145 ASN A CB    1 
ATOM   13450 C  CG    . ASN A 1 3145 ? 121.634 104.141 59.576  1.00 18.33  ? 3145 ASN A CG    1 
ATOM   13451 O  OD1   . ASN A 1 3145 ? 122.011 104.158 60.746  1.00 25.98  ? 3145 ASN A OD1   1 
ATOM   13452 N  ND2   . ASN A 1 3145 ? 120.947 105.137 59.030  1.00 25.91  ? 3145 ASN A ND2   1 
ATOM   13453 N  N     . SER A 1 3146 ? 119.309 101.493 57.703  1.00 7.88   ? 3146 SER A N     1 
ATOM   13454 C  CA    . SER A 1 3146 ? 117.878 101.483 57.424  1.00 5.68   ? 3146 SER A CA    1 
ATOM   13455 C  C     . SER A 1 3146 ? 117.184 100.329 58.135  1.00 5.52   ? 3146 SER A C     1 
ATOM   13456 O  O     . SER A 1 3146 ? 116.035 100.463 58.563  1.00 5.73   ? 3146 SER A O     1 
ATOM   13457 C  CB    . SER A 1 3146 ? 117.639 101.408 55.918  1.00 10.30  ? 3146 SER A CB    1 
ATOM   13458 O  OG    . SER A 1 3146 ? 118.239 102.504 55.250  1.00 13.26  ? 3146 SER A OG    1 
ATOM   13459 N  N     . CYS A 1 3147 ? 117.858 99.183  58.257  1.00 6.26   ? 3147 CYS A N     1 
ATOM   13460 C  CA    . CYS A 1 3147 ? 117.285 98.074  59.019  1.00 4.59   ? 3147 CYS A CA    1 
ATOM   13461 C  C     . CYS A 1 3147 ? 117.067 98.466  60.478  1.00 5.30   ? 3147 CYS A C     1 
ATOM   13462 O  O     . CYS A 1 3147 ? 116.010 98.180  61.064  1.00 5.84   ? 3147 CYS A O     1 
ATOM   13463 C  CB    . CYS A 1 3147 ? 118.193 96.848  58.925  1.00 4.36   ? 3147 CYS A CB    1 
ATOM   13464 S  SG    . CYS A 1 3147 ? 118.281 96.097  57.284  1.00 10.19  ? 3147 CYS A SG    1 
ATOM   13465 N  N     . VAL A 1 3148 ? 118.057 99.130  61.077  1.00 4.57   ? 3148 VAL A N     1 
ATOM   13466 C  CA    . VAL A 1 3148 ? 117.909 99.599  62.454  1.00 4.17   ? 3148 VAL A CA    1 
ATOM   13467 C  C     . VAL A 1 3148 ? 116.770 100.608 62.555  1.00 5.33   ? 3148 VAL A C     1 
ATOM   13468 O  O     . VAL A 1 3148 ? 115.976 100.581 63.507  1.00 6.13   ? 3148 VAL A O     1 
ATOM   13469 C  CB    . VAL A 1 3148 ? 119.238 100.183 62.967  1.00 5.32   ? 3148 VAL A CB    1 
ATOM   13470 C  CG1   . VAL A 1 3148 ? 119.064 100.745 64.368  1.00 7.04   ? 3148 VAL A CG1   1 
ATOM   13471 C  CG2   . VAL A 1 3148 ? 120.319 99.115  62.951  1.00 4.82   ? 3148 VAL A CG2   1 
ATOM   13472 N  N     . PHE A 1 3149 ? 116.677 101.519 61.581  1.00 4.74   ? 3149 PHE A N     1 
ATOM   13473 C  CA    . PHE A 1 3149 ? 115.572 102.474 61.572  1.00 6.31   ? 3149 PHE A CA    1 
ATOM   13474 C  C     . PHE A 1 3149 ? 114.229 101.761 61.508  1.00 6.08   ? 3149 PHE A C     1 
ATOM   13475 O  O     . PHE A 1 3149 ? 113.272 102.165 62.176  1.00 6.69   ? 3149 PHE A O     1 
ATOM   13476 C  CB    . PHE A 1 3149 ? 115.698 103.440 60.394  1.00 6.73   ? 3149 PHE A CB    1 
ATOM   13477 C  CG    . PHE A 1 3149 ? 114.480 104.302 60.195  1.00 7.91   ? 3149 PHE A CG    1 
ATOM   13478 C  CD1   . PHE A 1 3149 ? 114.321 105.473 60.915  1.00 8.90   ? 3149 PHE A CD1   1 
ATOM   13479 C  CD2   . PHE A 1 3149 ? 113.479 103.923 59.314  1.00 6.71   ? 3149 PHE A CD2   1 
ATOM   13480 C  CE1   . PHE A 1 3149 ? 113.200 106.262 60.743  1.00 11.27  ? 3149 PHE A CE1   1 
ATOM   13481 C  CE2   . PHE A 1 3149 ? 112.352 104.705 59.146  1.00 6.76   ? 3149 PHE A CE2   1 
ATOM   13482 C  CZ    . PHE A 1 3149 ? 112.215 105.877 59.858  1.00 8.24   ? 3149 PHE A CZ    1 
ATOM   13483 N  N     . VAL A 1 3150 ? 114.132 100.722 60.678  1.00 5.29   ? 3150 VAL A N     1 
ATOM   13484 C  CA    . VAL A 1 3150 ? 112.899 99.950  60.581  1.00 5.01   ? 3150 VAL A CA    1 
ATOM   13485 C  C     . VAL A 1 3150 ? 112.551 99.345  61.931  1.00 6.74   ? 3150 VAL A C     1 
ATOM   13486 O  O     . VAL A 1 3150 ? 111.387 99.353  62.351  1.00 5.94   ? 3150 VAL A O     1 
ATOM   13487 C  CB    . VAL A 1 3150 ? 113.025 98.869  59.490  1.00 3.56   ? 3150 VAL A CB    1 
ATOM   13488 C  CG1   . VAL A 1 3150 ? 111.883 97.878  59.593  1.00 2.70   ? 3150 VAL A CG1   1 
ATOM   13489 C  CG2   . VAL A 1 3150 ? 113.041 99.509  58.111  1.00 3.68   ? 3150 VAL A CG2   1 
ATOM   13490 N  N     . HIS A 1 3151 ? 113.553 98.816  62.636  1.00 6.52   ? 3151 HIS A N     1 
ATOM   13491 C  CA    . HIS A 1 3151 ? 113.278 98.241  63.950  1.00 4.96   ? 3151 HIS A CA    1 
ATOM   13492 C  C     . HIS A 1 3151 ? 112.765 99.297  64.927  1.00 6.88   ? 3151 HIS A C     1 
ATOM   13493 O  O     . HIS A 1 3151 ? 111.828 99.039  65.693  1.00 8.22   ? 3151 HIS A O     1 
ATOM   13494 C  CB    . HIS A 1 3151 ? 114.520 97.557  64.514  1.00 5.18   ? 3151 HIS A CB    1 
ATOM   13495 C  CG    . HIS A 1 3151 ? 114.272 96.849  65.809  1.00 5.85   ? 3151 HIS A CG    1 
ATOM   13496 N  ND1   . HIS A 1 3151 ? 113.677 95.607  65.874  1.00 5.48   ? 3151 HIS A ND1   1 
ATOM   13497 C  CD2   . HIS A 1 3151 ? 114.514 97.217  67.089  1.00 6.08   ? 3151 HIS A CD2   1 
ATOM   13498 C  CE1   . HIS A 1 3151 ? 113.576 95.235  67.137  1.00 4.88   ? 3151 HIS A CE1   1 
ATOM   13499 N  NE2   . HIS A 1 3151 ? 114.077 96.194  67.895  1.00 5.90   ? 3151 HIS A NE2   1 
ATOM   13500 N  N     . GLN A 1 3152 ? 113.364 100.491 64.918  1.00 8.03   ? 3152 GLN A N     1 
ATOM   13501 C  CA    . GLN A 1 3152 ? 112.931 101.540 65.846  1.00 8.49   ? 3152 GLN A CA    1 
ATOM   13502 C  C     . GLN A 1 3152 ? 111.563 102.108 65.472  1.00 11.01  ? 3152 GLN A C     1 
ATOM   13503 O  O     . GLN A 1 3152 ? 110.825 102.605 66.342  1.00 13.20  ? 3152 GLN A O     1 
ATOM   13504 C  CB    . GLN A 1 3152 ? 113.974 102.656 65.899  1.00 9.49   ? 3152 GLN A CB    1 
ATOM   13505 C  CG    . GLN A 1 3152 ? 115.399 102.162 66.087  1.00 9.75   ? 3152 GLN A CG    1 
ATOM   13506 C  CD    . GLN A 1 3152 ? 116.291 103.179 66.767  1.00 19.41  ? 3152 GLN A CD    1 
ATOM   13507 O  OE1   . GLN A 1 3152 ? 117.008 102.858 67.714  1.00 19.45  ? 3152 GLN A OE1   1 
ATOM   13508 N  NE2   . GLN A 1 3152 ? 116.257 104.414 66.281  1.00 22.25  ? 3152 GLN A NE2   1 
ATOM   13509 N  N     . THR A 1 3153 ? 111.212 102.051 64.186  1.00 9.37   ? 3153 THR A N     1 
ATOM   13510 C  CA    . THR A 1 3153 ? 109.916 102.549 63.746  1.00 10.06  ? 3153 THR A CA    1 
ATOM   13511 C  C     . THR A 1 3153 ? 108.779 101.751 64.373  1.00 9.92   ? 3153 THR A C     1 
ATOM   13512 O  O     . THR A 1 3153 ? 107.699 102.296 64.620  1.00 10.62  ? 3153 THR A O     1 
ATOM   13513 C  CB    . THR A 1 3153 ? 109.845 102.510 62.216  1.00 8.51   ? 3153 THR A CB    1 
ATOM   13514 O  OG1   . THR A 1 3153 ? 110.770 103.460 61.674  1.00 8.80   ? 3153 THR A OG1   1 
ATOM   13515 C  CG2   . THR A 1 3153 ? 108.459 102.867 61.722  1.00 10.04  ? 3153 THR A CG2   1 
ATOM   13516 N  N     . LEU A 1 3154 ? 109.012 100.471 64.673  1.00 9.18   ? 3154 LEU A N     1 
ATOM   13517 C  CA    . LEU A 1 3154 ? 107.984 99.676  65.336  1.00 9.21   ? 3154 LEU A CA    1 
ATOM   13518 C  C     . LEU A 1 3154 ? 107.771 100.124 66.776  1.00 11.96  ? 3154 LEU A C     1 
ATOM   13519 O  O     . LEU A 1 3154 ? 106.637 100.126 67.265  1.00 14.26  ? 3154 LEU A O     1 
ATOM   13520 C  CB    . LEU A 1 3154 ? 108.338 98.192  65.285  1.00 7.00   ? 3154 LEU A CB    1 
ATOM   13521 C  CG    . LEU A 1 3154 ? 107.869 97.443  64.038  1.00 5.43   ? 3154 LEU A CG    1 
ATOM   13522 C  CD1   . LEU A 1 3154 ? 106.352 97.457  63.962  1.00 5.47   ? 3154 LEU A CD1   1 
ATOM   13523 C  CD2   . LEU A 1 3154 ? 108.480 98.006  62.765  1.00 4.12   ? 3154 LEU A CD2   1 
ATOM   13524 N  N     . HIS A 1 3155 ? 108.845 100.501 67.474  1.00 12.90  ? 3155 HIS A N     1 
ATOM   13525 C  CA    . HIS A 1 3155 ? 108.678 101.087 68.800  1.00 12.42  ? 3155 HIS A CA    1 
ATOM   13526 C  C     . HIS A 1 3155 ? 107.892 102.388 68.720  1.00 14.28  ? 3155 HIS A C     1 
ATOM   13527 O  O     . HIS A 1 3155 ? 107.001 102.639 69.543  1.00 16.27  ? 3155 HIS A O     1 
ATOM   13528 C  CB    . HIS A 1 3155 ? 110.039 101.320 69.455  1.00 12.28  ? 3155 HIS A CB    1 
ATOM   13529 C  CG    . HIS A 1 3155 ? 110.723 100.062 69.893  1.00 14.56  ? 3155 HIS A CG    1 
ATOM   13530 N  ND1   . HIS A 1 3155 ? 111.912 99.631  69.345  1.00 13.52  ? 3155 HIS A ND1   1 
ATOM   13531 C  CD2   . HIS A 1 3155 ? 110.387 99.146  70.831  1.00 13.24  ? 3155 HIS A CD2   1 
ATOM   13532 C  CE1   . HIS A 1 3155 ? 112.277 98.502  69.925  1.00 15.05  ? 3155 HIS A CE1   1 
ATOM   13533 N  NE2   . HIS A 1 3155 ? 111.369 98.186  70.830  1.00 13.95  ? 3155 HIS A NE2   1 
ATOM   13534 N  N     . GLN A 1 3156 ? 108.199 103.222 67.723  1.00 16.07  ? 3156 GLN A N     1 
ATOM   13535 C  CA    . GLN A 1 3156 ? 107.439 104.460 67.553  1.00 16.65  ? 3156 GLN A CA    1 
ATOM   13536 C  C     . GLN A 1 3156 ? 105.960 104.175 67.291  1.00 18.89  ? 3156 GLN A C     1 
ATOM   13537 O  O     . GLN A 1 3156 ? 105.079 104.839 67.852  1.00 20.37  ? 3156 GLN A O     1 
ATOM   13538 C  CB    . GLN A 1 3156 ? 108.034 105.300 66.423  1.00 17.59  ? 3156 GLN A CB    1 
ATOM   13539 C  CG    . GLN A 1 3156 ? 109.328 106.007 66.792  1.00 19.26  ? 3156 GLN A CG    1 
ATOM   13540 C  CD    . GLN A 1 3156 ? 110.389 105.889 65.716  1.00 26.41  ? 3156 GLN A CD    1 
ATOM   13541 O  OE1   . GLN A 1 3156 ? 110.080 105.680 64.544  1.00 21.88  ? 3156 GLN A OE1   1 
ATOM   13542 N  NE2   . GLN A 1 3156 ? 111.650 106.022 66.111  1.00 26.73  ? 3156 GLN A NE2   1 
ATOM   13543 N  N     . ALA A 1 3157 ? 105.670 103.185 66.444  1.00 17.30  ? 3157 ALA A N     1 
ATOM   13544 C  CA    . ALA A 1 3157 ? 104.284 102.847 66.133  1.00 17.27  ? 3157 ALA A CA    1 
ATOM   13545 C  C     . ALA A 1 3157 ? 103.555 102.290 67.351  1.00 22.04  ? 3157 ALA A C     1 
ATOM   13546 O  O     . ALA A 1 3157 ? 102.387 102.624 67.589  1.00 29.70  ? 3157 ALA A O     1 
ATOM   13547 C  CB    . ALA A 1 3157 ? 104.235 101.850 64.976  1.00 13.86  ? 3157 ALA A CB    1 
ATOM   13548 N  N     . ASN A 1 3158 ? 104.219 101.428 68.124  1.00 21.19  ? 3158 ASN A N     1 
ATOM   13549 C  CA    . ASN A 1 3158 ? 103.602 100.917 69.342  1.00 21.56  ? 3158 ASN A CA    1 
ATOM   13550 C  C     . ASN A 1 3158 ? 103.311 102.046 70.317  1.00 23.09  ? 3158 ASN A C     1 
ATOM   13551 O  O     . ASN A 1 3158 ? 102.265 102.051 70.972  1.00 28.52  ? 3158 ASN A O     1 
ATOM   13552 C  CB    . ASN A 1 3158 ? 104.491 99.857  69.993  1.00 19.39  ? 3158 ASN A CB    1 
ATOM   13553 C  CG    . ASN A 1 3158 ? 104.235 98.468  69.446  1.00 19.65  ? 3158 ASN A CG    1 
ATOM   13554 O  OD1   . ASN A 1 3158 ? 103.486 98.295  68.485  1.00 24.35  ? 3158 ASN A OD1   1 
ATOM   13555 N  ND2   . ASN A 1 3158 ? 104.836 97.465  70.073  1.00 20.23  ? 3158 ASN A ND2   1 
ATOM   13556 N  N     . ALA A 1 3159 ? 104.217 103.022 70.414  1.00 26.92  ? 3159 ALA A N     1 
ATOM   13557 C  CA    . ALA A 1 3159 ? 103.942 104.195 71.236  1.00 26.42  ? 3159 ALA A CA    1 
ATOM   13558 C  C     . ALA A 1 3159 ? 102.723 104.955 70.726  1.00 27.76  ? 3159 ALA A C     1 
ATOM   13559 O  O     . ALA A 1 3159 ? 101.884 105.403 71.520  1.00 34.30  ? 3159 ALA A O     1 
ATOM   13560 C  CB    . ALA A 1 3159 ? 105.168 105.107 71.276  1.00 22.44  ? 3159 ALA A CB    1 
ATOM   13561 N  N     . ARG A 1 3160 ? 102.606 105.115 69.403  1.00 28.55  ? 3160 ARG A N     1 
ATOM   13562 C  CA    . ARG A 1 3160 ? 101.484 105.877 68.861  1.00 31.97  ? 3160 ARG A CA    1 
ATOM   13563 C  C     . ARG A 1 3160 ? 100.156 105.184 69.144  1.00 36.48  ? 3160 ARG A C     1 
ATOM   13564 O  O     . ARG A 1 3160 ? 99.164  105.841 69.479  1.00 45.18  ? 3160 ARG A O     1 
ATOM   13565 C  CB    . ARG A 1 3160 ? 101.643 106.106 67.356  1.00 38.57  ? 3160 ARG A CB    1 
ATOM   13566 C  CG    . ARG A 1 3160 ? 100.537 107.006 66.805  1.00 48.36  ? 3160 ARG A CG    1 
ATOM   13567 C  CD    . ARG A 1 3160 ? 100.627 107.297 65.313  1.00 51.92  ? 3160 ARG A CD    1 
ATOM   13568 N  NE    . ARG A 1 3160 ? 100.395 106.121 64.484  1.00 52.43  ? 3160 ARG A NE    1 
ATOM   13569 C  CZ    . ARG A 1 3160 ? 100.585 106.085 63.172  1.00 56.61  ? 3160 ARG A CZ    1 
ATOM   13570 N  NH1   . ARG A 1 3160 ? 101.036 107.137 62.509  1.00 50.48  ? 3160 ARG A NH1   1 
ATOM   13571 N  NH2   . ARG A 1 3160 ? 100.301 104.970 62.506  1.00 55.71  ? 3160 ARG A NH2   1 
ATOM   13572 N  N     . LEU A 1 3161 ? 100.107 103.858 68.999  1.00 33.71  ? 3161 LEU A N     1 
ATOM   13573 C  CA    . LEU A 1 3161 ? 98.873  103.146 69.331  1.00 33.39  ? 3161 LEU A CA    1 
ATOM   13574 C  C     . LEU A 1 3161 ? 98.626  103.113 70.836  1.00 38.46  ? 3161 LEU A C     1 
ATOM   13575 O  O     . LEU A 1 3161 ? 97.472  103.081 71.276  1.00 40.11  ? 3161 LEU A O     1 
ATOM   13576 C  CB    . LEU A 1 3161 ? 98.875  101.728 68.757  1.00 31.12  ? 3161 LEU A CB    1 
ATOM   13577 C  CG    . LEU A 1 3161 ? 98.572  101.540 67.266  1.00 37.80  ? 3161 LEU A CG    1 
ATOM   13578 C  CD1   . LEU A 1 3161 ? 99.688  102.018 66.372  1.00 35.87  ? 3161 LEU A CD1   1 
ATOM   13579 C  CD2   . LEU A 1 3161 ? 98.238  100.083 66.975  1.00 39.65  ? 3161 LEU A CD2   1 
ATOM   13580 N  N     . ALA A 1 3162 ? 99.690  103.116 71.642  1.00 37.23  ? 3162 ALA A N     1 
ATOM   13581 C  CA    . ALA A 1 3162 ? 99.510  103.104 73.088  1.00 38.08  ? 3162 ALA A CA    1 
ATOM   13582 C  C     . ALA A 1 3162 ? 98.914  104.414 73.583  1.00 46.84  ? 3162 ALA A C     1 
ATOM   13583 O  O     . ALA A 1 3162 ? 98.041  104.412 74.460  1.00 48.55  ? 3162 ALA A O     1 
ATOM   13584 C  CB    . ALA A 1 3162 ? 100.842 102.820 73.782  1.00 32.25  ? 3162 ALA A CB    1 
ATOM   13585 N  N     . LYS A 1 3163 ? 99.368  105.545 73.036  1.00 45.55  ? 3163 LYS A N     1 
ATOM   13586 C  CA    . LYS A 1 3163 ? 98.837  106.831 73.478  1.00 44.57  ? 3163 LYS A CA    1 
ATOM   13587 C  C     . LYS A 1 3163 ? 97.384  107.035 73.063  1.00 50.09  ? 3163 LYS A C     1 
ATOM   13588 O  O     . LYS A 1 3163 ? 96.702  107.883 73.645  1.00 59.45  ? 3163 LYS A O     1 
ATOM   13589 C  CB    . LYS A 1 3163 ? 99.696  107.980 72.944  1.00 43.40  ? 3163 LYS A CB    1 
ATOM   13590 C  CG    . LYS A 1 3163 ? 99.622  108.173 71.442  1.00 48.82  ? 3163 LYS A CG    1 
ATOM   13591 C  CD    . LYS A 1 3163 ? 100.510 109.317 70.984  1.00 48.43  ? 3163 LYS A CD    1 
ATOM   13592 C  CE    . LYS A 1 3163 ? 100.464 109.477 69.474  1.00 47.62  ? 3163 LYS A CE    1 
ATOM   13593 N  NZ    . LYS A 1 3163 ? 99.121  109.914 69.001  1.00 49.42  ? 3163 LYS A NZ    1 
ATOM   13594 N  N     . ARG A 1 3164 ? 96.897  106.281 72.078  1.00 48.79  ? 3164 ARG A N     1 
ATOM   13595 C  CA    . ARG A 1 3164 ? 95.514  106.372 71.629  1.00 50.67  ? 3164 ARG A CA    1 
ATOM   13596 C  C     . ARG A 1 3164 ? 94.620  105.314 72.263  1.00 49.57  ? 3164 ARG A C     1 
ATOM   13597 O  O     . ARG A 1 3164 ? 93.458  105.181 71.866  1.00 46.83  ? 3164 ARG A O     1 
ATOM   13598 C  CB    . ARG A 1 3164 ? 95.442  106.262 70.105  1.00 49.91  ? 3164 ARG A CB    1 
ATOM   13599 C  CG    . ARG A 1 3164 ? 96.296  107.273 69.361  1.00 55.14  ? 3164 ARG A CG    1 
ATOM   13600 C  CD    . ARG A 1 3164 ? 95.803  107.462 67.936  1.00 67.04  ? 3164 ARG A CD    1 
ATOM   13601 N  NE    . ARG A 1 3164 ? 95.268  106.226 67.377  1.00 77.19  ? 3164 ARG A NE    1 
ATOM   13602 C  CZ    . ARG A 1 3164 ? 95.747  105.622 66.299  1.00 77.45  ? 3164 ARG A CZ    1 
ATOM   13603 N  NH1   . ARG A 1 3164 ? 96.778  106.114 65.632  1.00 68.87  ? 3164 ARG A NH1   1 
ATOM   13604 N  NH2   . ARG A 1 3164 ? 95.178  104.496 65.878  1.00 64.36  ? 3164 ARG A NH2   1 
ATOM   13605 N  N     . GLY A 1 3165 ? 95.131  104.560 73.233  1.00 53.10  ? 3165 GLY A N     1 
ATOM   13606 C  CA    . GLY A 1 3165 ? 94.364  103.510 73.866  1.00 50.52  ? 3165 GLY A CA    1 
ATOM   13607 C  C     . GLY A 1 3165 ? 94.316  102.202 73.108  1.00 47.12  ? 3165 GLY A C     1 
ATOM   13608 O  O     . GLY A 1 3165 ? 93.606  101.284 73.539  1.00 49.41  ? 3165 GLY A O     1 
ATOM   13609 N  N     . GLY A 1 3166 ? 95.040  102.084 72.001  1.00 50.20  ? 3166 GLY A N     1 
ATOM   13610 C  CA    . GLY A 1 3166 ? 95.050  100.852 71.243  1.00 45.15  ? 3166 GLY A CA    1 
ATOM   13611 C  C     . GLY A 1 3166 ? 95.839  99.756  71.933  1.00 41.83  ? 3166 GLY A C     1 
ATOM   13612 O  O     . GLY A 1 3166 ? 96.575  99.974  72.897  1.00 38.96  ? 3166 GLY A O     1 
ATOM   13613 N  N     . ARG A 1 3167 ? 95.674  98.543  71.417  1.00 44.41  ? 3167 ARG A N     1 
ATOM   13614 C  CA    . ARG A 1 3167 ? 96.325  97.359  71.960  1.00 42.06  ? 3167 ARG A CA    1 
ATOM   13615 C  C     . ARG A 1 3167 ? 97.605  97.094  71.177  1.00 34.52  ? 3167 ARG A C     1 
ATOM   13616 O  O     . ARG A 1 3167 ? 97.568  96.934  69.953  1.00 35.54  ? 3167 ARG A O     1 
ATOM   13617 C  CB    . ARG A 1 3167 ? 95.389  96.154  71.897  1.00 41.88  ? 3167 ARG A CB    1 
ATOM   13618 C  CG    . ARG A 1 3167 ? 95.651  95.101  72.955  1.00 37.32  ? 3167 ARG A CG    1 
ATOM   13619 C  CD    . ARG A 1 3167 ? 94.514  94.098  73.001  1.00 38.07  ? 3167 ARG A CD    1 
ATOM   13620 N  NE    . ARG A 1 3167 ? 93.559  94.421  74.054  1.00 45.76  ? 3167 ARG A NE    1 
ATOM   13621 C  CZ    . ARG A 1 3167 ? 92.328  94.864  73.838  1.00 48.89  ? 3167 ARG A CZ    1 
ATOM   13622 N  NH1   . ARG A 1 3167 ? 91.871  95.066  72.613  1.00 42.33  ? 3167 ARG A NH1   1 
ATOM   13623 N  NH2   . ARG A 1 3167 ? 91.537  95.115  74.878  1.00 45.23  ? 3167 ARG A NH2   1 
ATOM   13624 N  N     . THR A 1 3168 ? 98.731  97.049  71.884  1.00 29.90  ? 3168 THR A N     1 
ATOM   13625 C  CA    . THR A 1 3168 ? 100.038 96.873  71.271  1.00 28.12  ? 3168 THR A CA    1 
ATOM   13626 C  C     . THR A 1 3168 ? 100.687 95.590  71.772  1.00 23.58  ? 3168 THR A C     1 
ATOM   13627 O  O     . THR A 1 3168 ? 100.418 95.131  72.887  1.00 26.74  ? 3168 THR A O     1 
ATOM   13628 C  CB    . THR A 1 3168 ? 100.962 98.061  71.570  1.00 28.48  ? 3168 THR A CB    1 
ATOM   13629 O  OG1   . THR A 1 3168 ? 101.229 98.121  72.976  1.00 29.84  ? 3168 THR A OG1   1 
ATOM   13630 C  CG2   . THR A 1 3168 ? 100.315 99.363  71.129  1.00 31.26  ? 3168 THR A CG2   1 
ATOM   13631 N  N     . MET A 1 3169 ? 101.545 95.018  70.935  1.00 20.68  ? 3169 MET A N     1 
ATOM   13632 C  CA    . MET A 1 3169 ? 102.334 93.848  71.287  1.00 19.12  ? 3169 MET A CA    1 
ATOM   13633 C  C     . MET A 1 3169 ? 103.798 94.246  71.409  1.00 16.01  ? 3169 MET A C     1 
ATOM   13634 O  O     . MET A 1 3169 ? 104.281 95.108  70.668  1.00 16.11  ? 3169 MET A O     1 
ATOM   13635 C  CB    . MET A 1 3169 ? 102.171 92.734  70.249  1.00 17.88  ? 3169 MET A CB    1 
ATOM   13636 C  CG    . MET A 1 3169 ? 100.756 92.186  70.154  1.00 18.10  ? 3169 MET A CG    1 
ATOM   13637 S  SD    . MET A 1 3169 ? 100.336 91.121  71.547  1.00 32.24  ? 3169 MET A SD    1 
ATOM   13638 C  CE    . MET A 1 3169 ? 98.590  91.464  71.736  1.00 28.61  ? 3169 MET A CE    1 
ATOM   13639 N  N     . ALA A 1 3170 ? 104.495 93.620  72.354  1.00 15.90  ? 3170 ALA A N     1 
ATOM   13640 C  CA    . ALA A 1 3170 ? 105.864 94.009  72.663  1.00 12.96  ? 3170 ALA A CA    1 
ATOM   13641 C  C     . ALA A 1 3170 ? 106.787 93.774  71.474  1.00 9.93   ? 3170 ALA A C     1 
ATOM   13642 O  O     . ALA A 1 3170 ? 106.725 92.736  70.810  1.00 10.66  ? 3170 ALA A O     1 
ATOM   13643 C  CB    . ALA A 1 3170 ? 106.370 93.235  73.880  1.00 15.42  ? 3170 ALA A CB    1 
ATOM   13644 N  N     . ILE A 1 3171 ? 107.647 94.753  71.210  1.00 10.64  ? 3171 ILE A N     1 
ATOM   13645 C  CA    . ILE A 1 3171 ? 108.686 94.643  70.193  1.00 7.78   ? 3171 ILE A CA    1 
ATOM   13646 C  C     . ILE A 1 3171 ? 109.950 94.134  70.867  1.00 8.72   ? 3171 ILE A C     1 
ATOM   13647 O  O     . ILE A 1 3171 ? 110.408 94.706  71.864  1.00 15.83  ? 3171 ILE A O     1 
ATOM   13648 C  CB    . ILE A 1 3171 ? 108.934 95.986  69.489  1.00 12.93  ? 3171 ILE A CB    1 
ATOM   13649 C  CG1   . ILE A 1 3171 ? 107.647 96.495  68.838  1.00 13.72  ? 3171 ILE A CG1   1 
ATOM   13650 C  CG2   . ILE A 1 3171 ? 110.041 95.847  68.463  1.00 9.88   ? 3171 ILE A CG2   1 
ATOM   13651 C  CD1   . ILE A 1 3171 ? 107.011 95.507  67.884  1.00 10.52  ? 3171 ILE A CD1   1 
ATOM   13652 N  N     . THR A 1 3172 ? 110.514 93.061  70.324  1.00 6.65   ? 3172 THR A N     1 
ATOM   13653 C  CA    . THR A 1 3172 ? 111.642 92.366  70.929  1.00 7.15   ? 3172 THR A CA    1 
ATOM   13654 C  C     . THR A 1 3172 ? 112.777 92.249  69.918  1.00 5.14   ? 3172 THR A C     1 
ATOM   13655 O  O     . THR A 1 3172 ? 112.544 92.378  68.710  1.00 5.04   ? 3172 THR A O     1 
ATOM   13656 C  CB    . THR A 1 3172 ? 111.216 90.978  71.419  1.00 5.95   ? 3172 THR A CB    1 
ATOM   13657 O  OG1   . THR A 1 3172 ? 111.035 90.107  70.296  1.00 8.81   ? 3172 THR A OG1   1 
ATOM   13658 C  CG2   . THR A 1 3172 ? 109.917 91.059  72.203  1.00 7.03   ? 3172 THR A CG2   1 
ATOM   13659 N  N     . PRO A 1 3173 ? 114.016 92.023  70.365  1.00 7.42   ? 3173 PRO A N     1 
ATOM   13660 C  CA    . PRO A 1 3173 ? 115.105 91.805  69.398  1.00 6.42   ? 3173 PRO A CA    1 
ATOM   13661 C  C     . PRO A 1 3173 ? 114.913 90.568  68.540  1.00 3.30   ? 3173 PRO A C     1 
ATOM   13662 O  O     . PRO A 1 3173 ? 115.546 90.454  67.482  1.00 3.83   ? 3173 PRO A O     1 
ATOM   13663 C  CB    . PRO A 1 3173 ? 116.351 91.690  70.288  1.00 5.84   ? 3173 PRO A CB    1 
ATOM   13664 C  CG    . PRO A 1 3173 ? 115.958 92.284  71.591  1.00 6.08   ? 3173 PRO A CG    1 
ATOM   13665 C  CD    . PRO A 1 3173 ? 114.504 92.018  71.753  1.00 6.23   ? 3173 PRO A CD    1 
ATOM   13666 N  N     . ARG A 1 3174 ? 114.067 89.626  68.965  1.00 3.54   ? 3174 ARG A N     1 
ATOM   13667 C  CA    . ARG A 1 3174 ? 113.755 88.492  68.105  1.00 4.53   ? 3174 ARG A CA    1 
ATOM   13668 C  C     . ARG A 1 3174 ? 112.996 88.932  66.861  1.00 4.40   ? 3174 ARG A C     1 
ATOM   13669 O  O     . ARG A 1 3174 ? 113.128 88.308  65.803  1.00 4.64   ? 3174 ARG A O     1 
ATOM   13670 C  CB    . ARG A 1 3174 ? 112.964 87.440  68.878  1.00 5.12   ? 3174 ARG A CB    1 
ATOM   13671 C  CG    . ARG A 1 3174 ? 113.747 86.796  70.007  1.00 7.68   ? 3174 ARG A CG    1 
ATOM   13672 C  CD    . ARG A 1 3174 ? 113.088 85.508  70.448  1.00 9.46   ? 3174 ARG A CD    1 
ATOM   13673 N  NE    . ARG A 1 3174 ? 113.028 84.542  69.358  1.00 8.85   ? 3174 ARG A NE    1 
ATOM   13674 C  CZ    . ARG A 1 3174 ? 112.500 83.331  69.459  1.00 12.43  ? 3174 ARG A CZ    1 
ATOM   13675 N  NH1   . ARG A 1 3174 ? 111.951 82.910  70.585  1.00 9.21   ? 3174 ARG A NH1   1 
ATOM   13676 N  NH2   . ARG A 1 3174 ? 112.518 82.524  68.402  1.00 12.50  ? 3174 ARG A NH2   1 
ATOM   13677 N  N     . HIS A 1 3175 ? 112.215 90.011  66.959  1.00 3.81   ? 3175 HIS A N     1 
ATOM   13678 C  CA    . HIS A 1 3175 ? 111.635 90.608  65.761  1.00 2.88   ? 3175 HIS A CA    1 
ATOM   13679 C  C     . HIS A 1 3175 ? 112.723 91.082  64.806  1.00 2.97   ? 3175 HIS A C     1 
ATOM   13680 O  O     . HIS A 1 3175 ? 112.621 90.880  63.592  1.00 2.77   ? 3175 HIS A O     1 
ATOM   13681 C  CB    . HIS A 1 3175 ? 110.713 91.769  66.137  1.00 3.98   ? 3175 HIS A CB    1 
ATOM   13682 C  CG    . HIS A 1 3175 ? 109.517 91.363  66.940  1.00 5.32   ? 3175 HIS A CG    1 
ATOM   13683 N  ND1   . HIS A 1 3175 ? 109.560 91.188  68.306  1.00 5.50   ? 3175 HIS A ND1   1 
ATOM   13684 C  CD2   . HIS A 1 3175 ? 108.236 91.122  66.571  1.00 6.58   ? 3175 HIS A CD2   1 
ATOM   13685 C  CE1   . HIS A 1 3175 ? 108.362 90.842  68.742  1.00 7.06   ? 3175 HIS A CE1   1 
ATOM   13686 N  NE2   . HIS A 1 3175 ? 107.541 90.795  67.709  1.00 11.28  ? 3175 HIS A NE2   1 
ATOM   13687 N  N     . TYR A 1 3176 ? 113.778 91.704  65.337  1.00 2.43   ? 3176 TYR A N     1 
ATOM   13688 C  CA    . TYR A 1 3176 ? 114.884 92.149  64.494  1.00 2.40   ? 3176 TYR A CA    1 
ATOM   13689 C  C     . TYR A 1 3176 ? 115.622 90.967  63.873  1.00 2.49   ? 3176 TYR A C     1 
ATOM   13690 O  O     . TYR A 1 3176 ? 116.040 91.029  62.709  1.00 2.21   ? 3176 TYR A O     1 
ATOM   13691 C  CB    . TYR A 1 3176 ? 115.841 93.015  65.312  1.00 3.02   ? 3176 TYR A CB    1 
ATOM   13692 C  CG    . TYR A 1 3176 ? 116.919 93.689  64.498  1.00 2.63   ? 3176 TYR A CG    1 
ATOM   13693 C  CD1   . TYR A 1 3176 ? 116.631 94.799  63.716  1.00 2.55   ? 3176 TYR A CD1   1 
ATOM   13694 C  CD2   . TYR A 1 3176 ? 118.228 93.225  64.520  1.00 1.98   ? 3176 TYR A CD2   1 
ATOM   13695 C  CE1   . TYR A 1 3176 ? 117.612 95.423  62.973  1.00 2.88   ? 3176 TYR A CE1   1 
ATOM   13696 C  CE2   . TYR A 1 3176 ? 119.218 93.845  63.781  1.00 2.73   ? 3176 TYR A CE2   1 
ATOM   13697 C  CZ    . TYR A 1 3176 ? 118.904 94.944  63.009  1.00 2.59   ? 3176 TYR A CZ    1 
ATOM   13698 O  OH    . TYR A 1 3176 ? 119.882 95.565  62.270  1.00 2.88   ? 3176 TYR A OH    1 
ATOM   13699 N  N     . LEU A 1 3177 ? 115.809 89.891  64.640  1.00 2.53   ? 3177 LEU A N     1 
ATOM   13700 C  CA    . LEU A 1 3177 ? 116.461 88.703  64.096  1.00 3.26   ? 3177 LEU A CA    1 
ATOM   13701 C  C     . LEU A 1 3177 ? 115.625 88.074  62.989  1.00 4.54   ? 3177 LEU A C     1 
ATOM   13702 O  O     . LEU A 1 3177 ? 116.163 87.656  61.957  1.00 5.70   ? 3177 LEU A O     1 
ATOM   13703 C  CB    . LEU A 1 3177 ? 116.731 87.692  65.208  1.00 4.41   ? 3177 LEU A CB    1 
ATOM   13704 C  CG    . LEU A 1 3177 ? 117.821 88.087  66.204  1.00 6.06   ? 3177 LEU A CG    1 
ATOM   13705 C  CD1   . LEU A 1 3177 ? 117.622 87.353  67.514  1.00 6.50   ? 3177 LEU A CD1   1 
ATOM   13706 C  CD2   . LEU A 1 3177 ? 119.200 87.806  65.630  1.00 4.70   ? 3177 LEU A CD2   1 
ATOM   13707 N  N     . ASP A 1 3178 ? 114.307 88.002  63.183  1.00 3.28   ? 3178 ASP A N     1 
ATOM   13708 C  CA    . ASP A 1 3178 ? 113.428 87.533  62.118  1.00 3.76   ? 3178 ASP A CA    1 
ATOM   13709 C  C     . ASP A 1 3178 ? 113.519 88.440  60.900  1.00 3.80   ? 3178 ASP A C     1 
ATOM   13710 O  O     . ASP A 1 3178 ? 113.533 87.963  59.761  1.00 4.32   ? 3178 ASP A O     1 
ATOM   13711 C  CB    . ASP A 1 3178 ? 111.986 87.459  62.617  1.00 4.63   ? 3178 ASP A CB    1 
ATOM   13712 C  CG    . ASP A 1 3178 ? 111.704 86.198  63.399  1.00 12.25  ? 3178 ASP A CG    1 
ATOM   13713 O  OD1   . ASP A 1 3178 ? 112.653 85.429  63.658  1.00 13.61  ? 3178 ASP A OD1   1 
ATOM   13714 O  OD2   . ASP A 1 3178 ? 110.527 85.975  63.750  1.00 18.29  ? 3178 ASP A OD2   1 
ATOM   13715 N  N     . PHE A 1 3179 ? 113.578 89.753  61.127  1.00 3.36   ? 3179 PHE A N     1 
ATOM   13716 C  CA    . PHE A 1 3179 ? 113.679 90.708  60.030  1.00 2.51   ? 3179 PHE A CA    1 
ATOM   13717 C  C     . PHE A 1 3179 ? 114.936 90.461  59.204  1.00 2.83   ? 3179 PHE A C     1 
ATOM   13718 O  O     . PHE A 1 3179 ? 114.873 90.361  57.975  1.00 3.69   ? 3179 PHE A O     1 
ATOM   13719 C  CB    . PHE A 1 3179 ? 113.653 92.132  60.593  1.00 2.46   ? 3179 PHE A CB    1 
ATOM   13720 C  CG    . PHE A 1 3179 ? 113.996 93.203  59.594  1.00 2.21   ? 3179 PHE A CG    1 
ATOM   13721 C  CD1   . PHE A 1 3179 ? 113.541 93.138  58.286  1.00 2.82   ? 3179 PHE A CD1   1 
ATOM   13722 C  CD2   . PHE A 1 3179 ? 114.770 94.287  59.971  1.00 2.15   ? 3179 PHE A CD2   1 
ATOM   13723 C  CE1   . PHE A 1 3179 ? 113.861 94.125  57.377  1.00 3.37   ? 3179 PHE A CE1   1 
ATOM   13724 C  CE2   . PHE A 1 3179 ? 115.088 95.278  59.067  1.00 2.65   ? 3179 PHE A CE2   1 
ATOM   13725 C  CZ    . PHE A 1 3179 ? 114.634 95.198  57.768  1.00 2.94   ? 3179 PHE A CZ    1 
ATOM   13726 N  N     . ILE A 1 3180 ? 116.089 90.343  59.866  1.00 2.83   ? 3180 ILE A N     1 
ATOM   13727 C  CA    . ILE A 1 3180 ? 117.333 90.158  59.121  1.00 3.26   ? 3180 ILE A CA    1 
ATOM   13728 C  C     . ILE A 1 3180 ? 117.388 88.776  58.471  1.00 3.93   ? 3180 ILE A C     1 
ATOM   13729 O  O     . ILE A 1 3180 ? 117.912 88.630  57.358  1.00 4.79   ? 3180 ILE A O     1 
ATOM   13730 C  CB    . ILE A 1 3180 ? 118.559 90.419  60.017  1.00 6.63   ? 3180 ILE A CB    1 
ATOM   13731 C  CG1   . ILE A 1 3180 ? 118.561 89.495  61.233  1.00 6.70   ? 3180 ILE A CG1   1 
ATOM   13732 C  CG2   . ILE A 1 3180 ? 118.596 91.878  60.452  1.00 3.47   ? 3180 ILE A CG2   1 
ATOM   13733 C  CD1   . ILE A 1 3180 ? 119.661 89.791  62.219  1.00 6.65   ? 3180 ILE A CD1   1 
ATOM   13734 N  N     . ASN A 1 3181 ? 116.857 87.745  59.137  1.00 4.93   ? 3181 ASN A N     1 
ATOM   13735 C  CA    . ASN A 1 3181 ? 116.815 86.415  58.534  1.00 6.31   ? 3181 ASN A CA    1 
ATOM   13736 C  C     . ASN A 1 3181 ? 115.971 86.418  57.266  1.00 5.45   ? 3181 ASN A C     1 
ATOM   13737 O  O     . ASN A 1 3181 ? 116.385 85.889  56.226  1.00 6.21   ? 3181 ASN A O     1 
ATOM   13738 C  CB    . ASN A 1 3181 ? 116.266 85.403  59.541  1.00 7.37   ? 3181 ASN A CB    1 
ATOM   13739 C  CG    . ASN A 1 3181 ? 117.344 84.817  60.429  1.00 13.95  ? 3181 ASN A CG    1 
ATOM   13740 O  OD1   . ASN A 1 3181 ? 117.985 83.828  60.074  1.00 25.00  ? 3181 ASN A OD1   1 
ATOM   13741 N  ND2   . ASN A 1 3181 ? 117.554 85.428  61.589  1.00 12.87  ? 3181 ASN A ND2   1 
ATOM   13742 N  N     . HIS A 1 3182 ? 114.781 87.021  57.335  1.00 4.00   ? 3182 HIS A N     1 
ATOM   13743 C  CA    . HIS A 1 3182 ? 113.929 87.123  56.158  1.00 4.89   ? 3182 HIS A CA    1 
ATOM   13744 C  C     . HIS A 1 3182 ? 114.594 87.956  55.075  1.00 5.31   ? 3182 HIS A C     1 
ATOM   13745 O  O     . HIS A 1 3182 ? 114.462 87.654  53.888  1.00 7.14   ? 3182 HIS A O     1 
ATOM   13746 C  CB    . HIS A 1 3182 ? 112.581 87.732  56.532  1.00 3.83   ? 3182 HIS A CB    1 
ATOM   13747 C  CG    . HIS A 1 3182 ? 111.638 86.777  57.195  1.00 5.32   ? 3182 HIS A CG    1 
ATOM   13748 N  ND1   . HIS A 1 3182 ? 110.813 87.151  58.233  1.00 4.34   ? 3182 HIS A ND1   1 
ATOM   13749 C  CD2   . HIS A 1 3182 ? 111.373 85.471  56.956  1.00 8.27   ? 3182 HIS A CD2   1 
ATOM   13750 C  CE1   . HIS A 1 3182 ? 110.089 86.114  58.614  1.00 6.33   ? 3182 HIS A CE1   1 
ATOM   13751 N  NE2   . HIS A 1 3182 ? 110.408 85.082  57.853  1.00 7.59   ? 3182 HIS A NE2   1 
ATOM   13752 N  N     . TYR A 1 3183 ? 115.299 89.021  55.462  1.00 3.80   ? 3183 TYR A N     1 
ATOM   13753 C  CA    . TYR A 1 3183 ? 115.993 89.844  54.478  1.00 4.67   ? 3183 TYR A CA    1 
ATOM   13754 C  C     . TYR A 1 3183 ? 117.033 89.029  53.724  1.00 6.04   ? 3183 TYR A C     1 
ATOM   13755 O  O     . TYR A 1 3183 ? 117.078 89.052  52.489  1.00 8.01   ? 3183 TYR A O     1 
ATOM   13756 C  CB    . TYR A 1 3183 ? 116.633 91.050  55.168  1.00 3.76   ? 3183 TYR A CB    1 
ATOM   13757 C  CG    . TYR A 1 3183 ? 117.242 92.061  54.222  1.00 5.41   ? 3183 TYR A CG    1 
ATOM   13758 C  CD1   . TYR A 1 3183 ? 116.794 92.182  52.912  1.00 6.23   ? 3183 TYR A CD1   1 
ATOM   13759 C  CD2   . TYR A 1 3183 ? 118.264 92.901  54.643  1.00 6.24   ? 3183 TYR A CD2   1 
ATOM   13760 C  CE1   . TYR A 1 3183 ? 117.355 93.103  52.048  1.00 6.39   ? 3183 TYR A CE1   1 
ATOM   13761 C  CE2   . TYR A 1 3183 ? 118.826 93.827  53.788  1.00 9.18   ? 3183 TYR A CE2   1 
ATOM   13762 C  CZ    . TYR A 1 3183 ? 118.368 93.924  52.492  1.00 8.73   ? 3183 TYR A CZ    1 
ATOM   13763 O  OH    . TYR A 1 3183 ? 118.928 94.846  51.638  1.00 12.64  ? 3183 TYR A OH    1 
ATOM   13764 N  N     . ALA A 1 3184 ? 117.858 88.274  54.452  1.00 5.31   ? 3184 ALA A N     1 
ATOM   13765 C  CA    . ALA A 1 3184 ? 118.867 87.446  53.799  1.00 8.31   ? 3184 ALA A CA    1 
ATOM   13766 C  C     . ALA A 1 3184 ? 118.220 86.402  52.894  1.00 8.49   ? 3184 ALA A C     1 
ATOM   13767 O  O     . ALA A 1 3184 ? 118.625 86.227  51.736  1.00 11.77  ? 3184 ALA A O     1 
ATOM   13768 C  CB    . ALA A 1 3184 ? 119.757 86.779  54.848  1.00 12.09  ? 3184 ALA A CB    1 
ATOM   13769 N  N     . ASN A 1 3185 ? 117.196 85.709  53.402  1.00 6.71   ? 3185 ASN A N     1 
ATOM   13770 C  CA    . ASN A 1 3185 ? 116.566 84.643  52.628  1.00 8.21   ? 3185 ASN A CA    1 
ATOM   13771 C  C     . ASN A 1 3185 ? 115.895 85.187  51.372  1.00 12.04  ? 3185 ASN A C     1 
ATOM   13772 O  O     . ASN A 1 3185 ? 116.057 84.631  50.281  1.00 17.09  ? 3185 ASN A O     1 
ATOM   13773 C  CB    . ASN A 1 3185 ? 115.559 83.886  53.496  1.00 8.86   ? 3185 ASN A CB    1 
ATOM   13774 C  CG    . ASN A 1 3185 ? 116.197 83.258  54.720  1.00 9.55   ? 3185 ASN A CG    1 
ATOM   13775 O  OD1   . ASN A 1 3185 ? 117.418 83.277  54.877  1.00 14.71  ? 3185 ASN A OD1   1 
ATOM   13776 N  ND2   . ASN A 1 3185 ? 115.373 82.696  55.595  1.00 9.99   ? 3185 ASN A ND2   1 
ATOM   13777 N  N     . LEU A 1 3186 ? 115.138 86.279  51.506  1.00 10.35  ? 3186 LEU A N     1 
ATOM   13778 C  CA    . LEU A 1 3186 ? 114.442 86.853  50.361  1.00 10.40  ? 3186 LEU A CA    1 
ATOM   13779 C  C     . LEU A 1 3186 ? 115.420 87.438  49.353  1.00 12.45  ? 3186 LEU A C     1 
ATOM   13780 O  O     . LEU A 1 3186 ? 115.203 87.328  48.142  1.00 19.61  ? 3186 LEU A O     1 
ATOM   13781 C  CB    . LEU A 1 3186 ? 113.449 87.918  50.830  1.00 9.13   ? 3186 LEU A CB    1 
ATOM   13782 C  CG    . LEU A 1 3186 ? 112.202 87.408  51.555  1.00 11.04  ? 3186 LEU A CG    1 
ATOM   13783 C  CD1   . LEU A 1 3186 ? 111.354 88.566  52.056  1.00 10.49  ? 3186 LEU A CD1   1 
ATOM   13784 C  CD2   . LEU A 1 3186 ? 111.388 86.500  50.646  1.00 12.70  ? 3186 LEU A CD2   1 
ATOM   13785 N  N     . PHE A 1 3187 ? 116.502 88.060  49.826  1.00 11.04  ? 3187 PHE A N     1 
ATOM   13786 C  CA    . PHE A 1 3187 ? 117.510 88.587  48.915  1.00 14.39  ? 3187 PHE A CA    1 
ATOM   13787 C  C     . PHE A 1 3187 ? 118.138 87.467  48.098  1.00 18.74  ? 3187 PHE A C     1 
ATOM   13788 O  O     . PHE A 1 3187 ? 118.232 87.557  46.867  1.00 21.93  ? 3187 PHE A O     1 
ATOM   13789 C  CB    . PHE A 1 3187 ? 118.572 89.334  49.717  1.00 14.34  ? 3187 PHE A CB    1 
ATOM   13790 C  CG    . PHE A 1 3187 ? 119.541 90.114  48.881  1.00 18.45  ? 3187 PHE A CG    1 
ATOM   13791 C  CD1   . PHE A 1 3187 ? 119.193 91.352  48.371  1.00 19.98  ? 3187 PHE A CD1   1 
ATOM   13792 C  CD2   . PHE A 1 3187 ? 120.807 89.618  48.622  1.00 18.30  ? 3187 PHE A CD2   1 
ATOM   13793 C  CE1   . PHE A 1 3187 ? 120.087 92.077  47.611  1.00 23.90  ? 3187 PHE A CE1   1 
ATOM   13794 C  CE2   . PHE A 1 3187 ? 121.702 90.338  47.861  1.00 21.11  ? 3187 PHE A CE2   1 
ATOM   13795 C  CZ    . PHE A 1 3187 ? 121.342 91.569  47.358  1.00 23.26  ? 3187 PHE A CZ    1 
ATOM   13796 N  N     . HIS A 1 3188 ? 118.558 86.391  48.771  1.00 15.95  ? 3188 HIS A N     1 
ATOM   13797 C  CA    . HIS A 1 3188 ? 119.149 85.265  48.055  1.00 19.88  ? 3188 HIS A CA    1 
ATOM   13798 C  C     . HIS A 1 3188 ? 118.152 84.647  47.082  1.00 23.28  ? 3188 HIS A C     1 
ATOM   13799 O  O     . HIS A 1 3188 ? 118.500 84.346  45.933  1.00 27.41  ? 3188 HIS A O     1 
ATOM   13800 C  CB    . HIS A 1 3188 ? 119.651 84.217  49.048  1.00 19.60  ? 3188 HIS A CB    1 
ATOM   13801 C  CG    . HIS A 1 3188 ? 120.001 82.906  48.416  1.00 29.22  ? 3188 HIS A CG    1 
ATOM   13802 N  ND1   . HIS A 1 3188 ? 121.068 82.756  47.557  1.00 33.44  ? 3188 HIS A ND1   1 
ATOM   13803 C  CD2   . HIS A 1 3188 ? 119.423 81.685  48.514  1.00 30.99  ? 3188 HIS A CD2   1 
ATOM   13804 C  CE1   . HIS A 1 3188 ? 121.134 81.500  47.155  1.00 31.71  ? 3188 HIS A CE1   1 
ATOM   13805 N  NE2   . HIS A 1 3188 ? 120.148 80.829  47.721  1.00 32.09  ? 3188 HIS A NE2   1 
ATOM   13806 N  N     . GLU A 1 3189 ? 116.903 84.466  47.521  1.00 21.81  ? 3189 GLU A N     1 
ATOM   13807 C  CA    . GLU A 1 3189 ? 115.885 83.862  46.668  1.00 22.14  ? 3189 GLU A CA    1 
ATOM   13808 C  C     . GLU A 1 3189 ? 115.633 84.704  45.424  1.00 25.10  ? 3189 GLU A C     1 
ATOM   13809 O  O     . GLU A 1 3189 ? 115.595 84.179  44.306  1.00 33.41  ? 3189 GLU A O     1 
ATOM   13810 C  CB    . GLU A 1 3189 ? 114.590 83.674  47.461  1.00 22.56  ? 3189 GLU A CB    1 
ATOM   13811 C  CG    . GLU A 1 3189 ? 113.479 82.976  46.693  1.00 34.99  ? 3189 GLU A CG    1 
ATOM   13812 C  CD    . GLU A 1 3189 ? 112.111 83.205  47.310  1.00 37.20  ? 3189 GLU A CD    1 
ATOM   13813 O  OE1   . GLU A 1 3189 ? 111.960 82.983  48.530  1.00 33.43  ? 3189 GLU A OE1   1 
ATOM   13814 O  OE2   . GLU A 1 3189 ? 111.187 83.615  46.576  1.00 36.77  ? 3189 GLU A OE2   1 
ATOM   13815 N  N     . LYS A 1 3190 ? 115.465 86.016  45.597  1.00 21.94  ? 3190 LYS A N     1 
ATOM   13816 C  CA    . LYS A 1 3190 ? 115.172 86.878  44.459  1.00 22.94  ? 3190 LYS A CA    1 
ATOM   13817 C  C     . LYS A 1 3190 ? 116.357 86.950  43.505  1.00 23.77  ? 3190 LYS A C     1 
ATOM   13818 O  O     . LYS A 1 3190 ? 116.175 86.924  42.282  1.00 30.37  ? 3190 LYS A O     1 
ATOM   13819 C  CB    . LYS A 1 3190 ? 114.776 88.272  44.945  1.00 22.52  ? 3190 LYS A CB    1 
ATOM   13820 C  CG    . LYS A 1 3190 ? 113.406 88.331  45.611  1.00 21.06  ? 3190 LYS A CG    1 
ATOM   13821 C  CD    . LYS A 1 3190 ? 112.299 87.868  44.676  1.00 25.77  ? 3190 LYS A CD    1 
ATOM   13822 C  CE    . LYS A 1 3190 ? 110.930 87.975  45.332  1.00 25.87  ? 3190 LYS A CE    1 
ATOM   13823 N  NZ    . LYS A 1 3190 ? 109.832 87.921  44.329  1.00 32.56  ? 3190 LYS A NZ    1 
ATOM   13824 N  N     . ARG A 1 3191 ? 117.579 87.028  44.044  1.00 26.33  ? 3191 ARG A N     1 
ATOM   13825 C  CA    . ARG A 1 3191 ? 118.765 87.043  43.193  1.00 27.31  ? 3191 ARG A CA    1 
ATOM   13826 C  C     . ARG A 1 3191 ? 118.866 85.760  42.375  1.00 26.80  ? 3191 ARG A C     1 
ATOM   13827 O  O     . ARG A 1 3191 ? 119.129 85.801  41.164  1.00 28.76  ? 3191 ARG A O     1 
ATOM   13828 C  CB    . ARG A 1 3191 ? 120.009 87.244  44.063  1.00 30.52  ? 3191 ARG A CB    1 
ATOM   13829 C  CG    . ARG A 1 3191 ? 121.339 87.338  43.331  1.00 41.41  ? 3191 ARG A CG    1 
ATOM   13830 C  CD    . ARG A 1 3191 ? 121.423 88.567  42.450  1.00 51.60  ? 3191 ARG A CD    1 
ATOM   13831 N  NE    . ARG A 1 3191 ? 121.276 89.815  43.190  1.00 49.19  ? 3191 ARG A NE    1 
ATOM   13832 C  CZ    . ARG A 1 3191 ? 122.264 90.436  43.819  1.00 48.93  ? 3191 ARG A CZ    1 
ATOM   13833 N  NH1   . ARG A 1 3191 ? 123.480 89.920  43.876  1.00 49.43  ? 3191 ARG A NH1   1 
ATOM   13834 N  NH2   . ARG A 1 3191 ? 122.024 91.602  44.410  1.00 43.58  ? 3191 ARG A NH2   1 
ATOM   13835 N  N     . SER A 1 3192 ? 118.630 84.611  43.016  1.00 26.91  ? 3192 SER A N     1 
ATOM   13836 C  CA    . SER A 1 3192 ? 118.701 83.333  42.316  1.00 29.35  ? 3192 SER A CA    1 
ATOM   13837 C  C     . SER A 1 3192 ? 117.632 83.231  41.234  1.00 31.81  ? 3192 SER A C     1 
ATOM   13838 O  O     . SER A 1 3192 ? 117.916 82.820  40.101  1.00 34.13  ? 3192 SER A O     1 
ATOM   13839 C  CB    . SER A 1 3192 ? 118.565 82.188  43.319  1.00 28.85  ? 3192 SER A CB    1 
ATOM   13840 O  OG    . SER A 1 3192 ? 118.597 80.934  42.663  1.00 40.01  ? 3192 SER A OG    1 
ATOM   13841 N  N     . GLU A 1 3193 ? 116.392 83.604  41.566  1.00 29.87  ? 3193 GLU A N     1 
ATOM   13842 C  CA    . GLU A 1 3193 ? 115.318 83.532  40.581  1.00 29.08  ? 3193 GLU A CA    1 
ATOM   13843 C  C     . GLU A 1 3193 ? 115.590 84.451  39.400  1.00 29.92  ? 3193 GLU A C     1 
ATOM   13844 O  O     . GLU A 1 3193 ? 115.343 84.080  38.248  1.00 37.43  ? 3193 GLU A O     1 
ATOM   13845 C  CB    . GLU A 1 3193 ? 113.972 83.873  41.223  1.00 26.43  ? 3193 GLU A CB    1 
ATOM   13846 C  CG    . GLU A 1 3193 ? 113.575 82.987  42.390  1.00 35.35  ? 3193 GLU A CG    1 
ATOM   13847 C  CD    . GLU A 1 3193 ? 112.123 83.172  42.785  1.00 50.31  ? 3193 GLU A CD    1 
ATOM   13848 O  OE1   . GLU A 1 3193 ? 111.665 84.333  42.834  1.00 44.48  ? 3193 GLU A OE1   1 
ATOM   13849 O  OE2   . GLU A 1 3193 ? 111.441 82.159  43.046  1.00 58.78  ? 3193 GLU A OE2   1 
ATOM   13850 N  N     . LEU A 1 3194 ? 116.101 85.656  39.663  1.00 29.20  ? 3194 LEU A N     1 
ATOM   13851 C  CA    . LEU A 1 3194 ? 116.347 86.594  38.575  1.00 25.53  ? 3194 LEU A CA    1 
ATOM   13852 C  C     . LEU A 1 3194 ? 117.486 86.123  37.677  1.00 33.54  ? 3194 LEU A C     1 
ATOM   13853 O  O     . LEU A 1 3194 ? 117.389 86.226  36.448  1.00 42.85  ? 3194 LEU A O     1 
ATOM   13854 C  CB    . LEU A 1 3194 ? 116.620 87.988  39.135  1.00 27.28  ? 3194 LEU A CB    1 
ATOM   13855 C  CG    . LEU A 1 3194 ? 116.506 89.116  38.110  1.00 36.19  ? 3194 LEU A CG    1 
ATOM   13856 C  CD1   . LEU A 1 3194 ? 115.153 89.058  37.427  1.00 41.06  ? 3194 LEU A CD1   1 
ATOM   13857 C  CD2   . LEU A 1 3194 ? 116.679 90.455  38.790  1.00 38.41  ? 3194 LEU A CD2   1 
ATOM   13858 N  N     . GLU A 1 3195 ? 118.569 85.593  38.260  1.00 35.94  ? 3195 GLU A N     1 
ATOM   13859 C  CA    . GLU A 1 3195 ? 119.625 85.027  37.420  1.00 35.00  ? 3195 GLU A CA    1 
ATOM   13860 C  C     . GLU A 1 3195 ? 119.119 83.847  36.600  1.00 35.94  ? 3195 GLU A C     1 
ATOM   13861 O  O     . GLU A 1 3195 ? 119.475 83.709  35.424  1.00 42.26  ? 3195 GLU A O     1 
ATOM   13862 C  CB    . GLU A 1 3195 ? 120.835 84.600  38.251  1.00 36.31  ? 3195 GLU A CB    1 
ATOM   13863 C  CG    . GLU A 1 3195 ? 121.820 85.708  38.580  1.00 42.45  ? 3195 GLU A CG    1 
ATOM   13864 C  CD    . GLU A 1 3195 ? 122.405 85.575  39.968  1.00 49.76  ? 3195 GLU A CD    1 
ATOM   13865 O  OE1   . GLU A 1 3195 ? 122.430 84.444  40.495  1.00 49.98  ? 3195 GLU A OE1   1 
ATOM   13866 O  OE2   . GLU A 1 3195 ? 122.876 86.591  40.515  1.00 47.51  ? 3195 GLU A OE2   1 
ATOM   13867 N  N     . GLU A 1 3196 ? 118.305 82.975  37.200  1.00 35.59  ? 3196 GLU A N     1 
ATOM   13868 C  CA    . GLU A 1 3196 ? 117.778 81.836  36.453  1.00 37.65  ? 3196 GLU A CA    1 
ATOM   13869 C  C     . GLU A 1 3196 ? 116.890 82.296  35.300  1.00 37.15  ? 3196 GLU A C     1 
ATOM   13870 O  O     . GLU A 1 3196 ? 116.990 81.778  34.177  1.00 42.86  ? 3196 GLU A O     1 
ATOM   13871 C  CB    . GLU A 1 3196 ? 117.011 80.908  37.394  1.00 38.20  ? 3196 GLU A CB    1 
ATOM   13872 C  CG    . GLU A 1 3196 ? 116.483 79.644  36.738  1.00 44.75  ? 3196 GLU A CG    1 
ATOM   13873 C  CD    . GLU A 1 3196 ? 115.775 78.733  37.722  1.00 59.00  ? 3196 GLU A CD    1 
ATOM   13874 O  OE1   . GLU A 1 3196 ? 115.681 79.101  38.911  1.00 67.00  ? 3196 GLU A OE1   1 
ATOM   13875 O  OE2   . GLU A 1 3196 ? 115.315 77.648  37.306  1.00 67.84  ? 3196 GLU A OE2   1 
ATOM   13876 N  N     . GLN A 1 3197 ? 116.026 83.281  35.558  1.00 34.26  ? 3197 GLN A N     1 
ATOM   13877 C  CA    . GLN A 1 3197 ? 115.161 83.806  34.509  1.00 37.13  ? 3197 GLN A CA    1 
ATOM   13878 C  C     . GLN A 1 3197 ? 115.977 84.438  33.390  1.00 37.64  ? 3197 GLN A C     1 
ATOM   13879 O  O     . GLN A 1 3197 ? 115.687 84.227  32.207  1.00 44.92  ? 3197 GLN A O     1 
ATOM   13880 C  CB    . GLN A 1 3197 ? 114.176 84.817  35.100  1.00 39.36  ? 3197 GLN A CB    1 
ATOM   13881 C  CG    . GLN A 1 3197 ? 113.598 85.795  34.088  1.00 50.42  ? 3197 GLN A CG    1 
ATOM   13882 C  CD    . GLN A 1 3197 ? 112.682 86.824  34.722  1.00 57.21  ? 3197 GLN A CD    1 
ATOM   13883 O  OE1   . GLN A 1 3197 ? 113.104 87.935  35.044  1.00 57.41  ? 3197 GLN A OE1   1 
ATOM   13884 N  NE2   . GLN A 1 3197 ? 111.417 86.460  34.900  1.00 60.29  ? 3197 GLN A NE2   1 
ATOM   13885 N  N     . GLN A 1 3198 ? 117.011 85.207  33.743  1.00 34.52  ? 3198 GLN A N     1 
ATOM   13886 C  CA    . GLN A 1 3198 ? 117.849 85.820  32.717  1.00 39.64  ? 3198 GLN A CA    1 
ATOM   13887 C  C     . GLN A 1 3198 ? 118.608 84.772  31.914  1.00 43.01  ? 3198 GLN A C     1 
ATOM   13888 O  O     . GLN A 1 3198 ? 118.776 84.922  30.699  1.00 47.49  ? 3198 GLN A O     1 
ATOM   13889 C  CB    . GLN A 1 3198 ? 118.813 86.823  33.346  1.00 39.80  ? 3198 GLN A CB    1 
ATOM   13890 C  CG    . GLN A 1 3198 ? 119.675 87.537  32.321  1.00 42.66  ? 3198 GLN A CG    1 
ATOM   13891 C  CD    . GLN A 1 3198 ? 118.852 88.338  31.335  1.00 48.76  ? 3198 GLN A CD    1 
ATOM   13892 O  OE1   . GLN A 1 3198 ? 118.680 87.937  30.184  1.00 58.27  ? 3198 GLN A OE1   1 
ATOM   13893 N  NE2   . GLN A 1 3198 ? 118.325 89.466  31.782  1.00 48.78  ? 3198 GLN A NE2   1 
ATOM   13894 N  N     . MET A 1 3199 ? 119.080 83.710  32.569  1.00 37.26  ? 3199 MET A N     1 
ATOM   13895 C  CA    . MET A 1 3199 ? 119.758 82.639  31.847  1.00 41.18  ? 3199 MET A CA    1 
ATOM   13896 C  C     . MET A 1 3199 ? 118.825 81.996  30.830  1.00 44.80  ? 3199 MET A C     1 
ATOM   13897 O  O     . MET A 1 3199 ? 119.194 81.798  29.663  1.00 48.80  ? 3199 MET A O     1 
ATOM   13898 C  CB    . MET A 1 3199 ? 120.283 81.595  32.833  1.00 42.20  ? 3199 MET A CB    1 
ATOM   13899 C  CG    . MET A 1 3199 ? 121.077 80.471  32.187  1.00 53.72  ? 3199 MET A CG    1 
ATOM   13900 S  SD    . MET A 1 3199 ? 121.102 78.972  33.189  1.00 86.99  ? 3199 MET A SD    1 
ATOM   13901 C  CE    . MET A 1 3199 ? 121.911 79.568  34.672  1.00 70.85  ? 3199 MET A CE    1 
ATOM   13902 N  N     . HIS A 1 3200 ? 117.599 81.677  31.254  1.00 44.85  ? 3200 HIS A N     1 
ATOM   13903 C  CA    . HIS A 1 3200 ? 116.643 81.073  30.329  1.00 45.62  ? 3200 HIS A CA    1 
ATOM   13904 C  C     . HIS A 1 3200 ? 116.304 82.019  29.182  1.00 43.70  ? 3200 HIS A C     1 
ATOM   13905 O  O     . HIS A 1 3200 ? 116.214 81.593  28.024  1.00 46.43  ? 3200 HIS A O     1 
ATOM   13906 C  CB    . HIS A 1 3200 ? 115.378 80.645  31.075  1.00 41.04  ? 3200 HIS A CB    1 
ATOM   13907 C  CG    . HIS A 1 3200 ? 115.621 79.621  32.140  1.00 44.85  ? 3200 HIS A CG    1 
ATOM   13908 N  ND1   . HIS A 1 3200 ? 114.601 79.062  32.880  1.00 51.67  ? 3200 HIS A ND1   1 
ATOM   13909 C  CD2   . HIS A 1 3200 ? 116.764 79.046  32.582  1.00 48.27  ? 3200 HIS A CD2   1 
ATOM   13910 C  CE1   . HIS A 1 3200 ? 115.107 78.191  33.735  1.00 52.94  ? 3200 HIS A CE1   1 
ATOM   13911 N  NE2   . HIS A 1 3200 ? 116.418 78.163  33.575  1.00 55.00  ? 3200 HIS A NE2   1 
ATOM   13912 N  N     . LEU A 1 3201 ? 116.123 83.308  29.481  1.00 38.07  ? 3201 LEU A N     1 
ATOM   13913 C  CA    . LEU A 1 3201 ? 115.801 84.270  28.429  1.00 42.54  ? 3201 LEU A CA    1 
ATOM   13914 C  C     . LEU A 1 3201 ? 116.943 84.408  27.429  1.00 45.93  ? 3201 LEU A C     1 
ATOM   13915 O  O     . LEU A 1 3201 ? 116.709 84.469  26.216  1.00 50.44  ? 3201 LEU A O     1 
ATOM   13916 C  CB    . LEU A 1 3201 ? 115.462 85.628  29.042  1.00 46.07  ? 3201 LEU A CB    1 
ATOM   13917 C  CG    . LEU A 1 3201 ? 114.163 85.702  29.843  1.00 50.27  ? 3201 LEU A CG    1 
ATOM   13918 C  CD1   . LEU A 1 3201 ? 113.841 87.142  30.180  1.00 51.78  ? 3201 LEU A CD1   1 
ATOM   13919 C  CD2   . LEU A 1 3201 ? 113.017 85.054  29.081  1.00 46.67  ? 3201 LEU A CD2   1 
ATOM   13920 N  N     . ASN A 1 3202 ? 118.184 84.470  27.918  1.00 48.06  ? 3202 ASN A N     1 
ATOM   13921 C  CA    . ASN A 1 3202 ? 119.327 84.586  27.019  1.00 46.50  ? 3202 ASN A CA    1 
ATOM   13922 C  C     . ASN A 1 3202 ? 119.465 83.351  26.141  1.00 45.98  ? 3202 ASN A C     1 
ATOM   13923 O  O     . ASN A 1 3202 ? 119.748 83.461  24.941  1.00 48.01  ? 3202 ASN A O     1 
ATOM   13924 C  CB    . ASN A 1 3202 ? 120.606 84.821  27.823  1.00 51.22  ? 3202 ASN A CB    1 
ATOM   13925 C  CG    . ASN A 1 3202 ? 120.781 86.270  28.231  1.00 57.88  ? 3202 ASN A CG    1 
ATOM   13926 O  OD1   . ASN A 1 3202 ? 121.784 86.638  28.842  1.00 68.82  ? 3202 ASN A OD1   1 
ATOM   13927 N  ND2   . ASN A 1 3202 ? 119.803 87.103  27.893  1.00 55.13  ? 3202 ASN A ND2   1 
ATOM   13928 N  N     . VAL A 1 3203 ? 119.266 82.162  26.719  1.00 45.70  ? 3203 VAL A N     1 
ATOM   13929 C  CA    . VAL A 1 3203 ? 119.360 80.940  25.924  1.00 44.35  ? 3203 VAL A CA    1 
ATOM   13930 C  C     . VAL A 1 3203 ? 118.258 80.906  24.869  1.00 46.50  ? 3203 VAL A C     1 
ATOM   13931 O  O     . VAL A 1 3203 ? 118.497 80.538  23.711  1.00 48.45  ? 3203 VAL A O     1 
ATOM   13932 C  CB    . VAL A 1 3203 ? 119.322 79.702  26.839  1.00 39.66  ? 3203 VAL A CB    1 
ATOM   13933 C  CG1   . VAL A 1 3203 ? 119.182 78.433  26.016  1.00 40.91  ? 3203 VAL A CG1   1 
ATOM   13934 C  CG2   . VAL A 1 3203 ? 120.576 79.642  27.697  1.00 44.36  ? 3203 VAL A CG2   1 
ATOM   13935 N  N     . GLY A 1 3204 ? 117.041 81.309  25.242  1.00 44.00  ? 3204 GLY A N     1 
ATOM   13936 C  CA    . GLY A 1 3204 ? 115.965 81.363  24.266  1.00 40.00  ? 3204 GLY A CA    1 
ATOM   13937 C  C     . GLY A 1 3204 ? 116.243 82.340  23.139  1.00 45.74  ? 3204 GLY A C     1 
ATOM   13938 O  O     . GLY A 1 3204 ? 115.996 82.041  21.967  1.00 54.34  ? 3204 GLY A O     1 
ATOM   13939 N  N     . LEU A 1 3205 ? 116.769 83.519  23.477  1.00 45.27  ? 3205 LEU A N     1 
ATOM   13940 C  CA    . LEU A 1 3205 ? 117.052 84.521  22.456  1.00 47.94  ? 3205 LEU A CA    1 
ATOM   13941 C  C     . LEU A 1 3205 ? 118.158 84.059  21.515  1.00 48.46  ? 3205 LEU A C     1 
ATOM   13942 O  O     . LEU A 1 3205 ? 118.062 84.249  20.294  1.00 51.29  ? 3205 LEU A O     1 
ATOM   13943 C  CB    . LEU A 1 3205 ? 117.422 85.847  23.116  1.00 48.43  ? 3205 LEU A CB    1 
ATOM   13944 C  CG    . LEU A 1 3205 ? 116.222 86.659  23.602  1.00 51.01  ? 3205 LEU A CG    1 
ATOM   13945 C  CD1   . LEU A 1 3205 ? 116.651 87.751  24.573  1.00 54.57  ? 3205 LEU A CD1   1 
ATOM   13946 C  CD2   . LEU A 1 3205 ? 115.459 87.235  22.425  1.00 58.58  ? 3205 LEU A CD2   1 
ATOM   13947 N  N     . ARG A 1 3206 ? 119.215 83.447  22.058  1.00 48.80  ? 3206 ARG A N     1 
ATOM   13948 C  CA    . ARG A 1 3206 ? 120.276 82.957  21.187  1.00 50.95  ? 3206 ARG A CA    1 
ATOM   13949 C  C     . ARG A 1 3206 ? 119.788 81.805  20.318  1.00 54.37  ? 3206 ARG A C     1 
ATOM   13950 O  O     . ARG A 1 3206 ? 120.216 81.682  19.167  1.00 58.20  ? 3206 ARG A O     1 
ATOM   13951 C  CB    . ARG A 1 3206 ? 121.506 82.541  21.999  1.00 50.43  ? 3206 ARG A CB    1 
ATOM   13952 C  CG    . ARG A 1 3206 ? 121.323 81.323  22.880  1.00 52.40  ? 3206 ARG A CG    1 
ATOM   13953 C  CD    . ARG A 1 3206 ? 122.589 80.989  23.652  1.00 58.50  ? 3206 ARG A CD    1 
ATOM   13954 N  NE    . ARG A 1 3206 ? 122.946 82.033  24.605  1.00 67.23  ? 3206 ARG A NE    1 
ATOM   13955 C  CZ    . ARG A 1 3206 ? 123.973 82.860  24.462  1.00 67.05  ? 3206 ARG A CZ    1 
ATOM   13956 N  NH1   . ARG A 1 3206 ? 124.772 82.793  23.410  1.00 66.42  ? 3206 ARG A NH1   1 
ATOM   13957 N  NH2   . ARG A 1 3206 ? 124.203 83.775  25.398  1.00 61.57  ? 3206 ARG A NH2   1 
ATOM   13958 N  N     . LYS A 1 3207 ? 118.879 80.969  20.830  1.00 52.59  ? 3207 LYS A N     1 
ATOM   13959 C  CA    . LYS A 1 3207 ? 118.316 79.914  19.993  1.00 55.74  ? 3207 LYS A CA    1 
ATOM   13960 C  C     . LYS A 1 3207 ? 117.445 80.484  18.879  1.00 55.28  ? 3207 LYS A C     1 
ATOM   13961 O  O     . LYS A 1 3207 ? 117.458 79.970  17.757  1.00 59.05  ? 3207 LYS A O     1 
ATOM   13962 C  CB    . LYS A 1 3207 ? 117.532 78.917  20.843  1.00 48.68  ? 3207 LYS A CB    1 
ATOM   13963 C  CG    . LYS A 1 3207 ? 118.423 77.998  21.655  1.00 53.76  ? 3207 LYS A CG    1 
ATOM   13964 C  CD    . LYS A 1 3207 ? 118.487 76.620  21.018  1.00 62.43  ? 3207 LYS A CD    1 
ATOM   13965 C  CE    . LYS A 1 3207 ? 119.545 75.752  21.673  1.00 68.85  ? 3207 LYS A CE    1 
ATOM   13966 N  NZ    . LYS A 1 3207 ? 119.357 74.314  21.340  1.00 74.09  ? 3207 LYS A NZ    1 
ATOM   13967 N  N     . ILE A 1 3208 ? 116.682 81.542  19.164  1.00 49.99  ? 3208 ILE A N     1 
ATOM   13968 C  CA    . ILE A 1 3208 ? 115.897 82.180  18.106  1.00 49.86  ? 3208 ILE A CA    1 
ATOM   13969 C  C     . ILE A 1 3208 ? 116.813 82.770  17.039  1.00 56.78  ? 3208 ILE A C     1 
ATOM   13970 O  O     . ILE A 1 3208 ? 116.559 82.634  15.833  1.00 65.32  ? 3208 ILE A O     1 
ATOM   13971 C  CB    . ILE A 1 3208 ? 114.953 83.244  18.697  1.00 52.73  ? 3208 ILE A CB    1 
ATOM   13972 C  CG1   . ILE A 1 3208 ? 113.949 82.599  19.653  1.00 53.57  ? 3208 ILE A CG1   1 
ATOM   13973 C  CG2   . ILE A 1 3208 ? 114.224 83.988  17.588  1.00 50.40  ? 3208 ILE A CG2   1 
ATOM   13974 C  CD1   . ILE A 1 3208 ? 112.996 83.586  20.289  1.00 54.71  ? 3208 ILE A CD1   1 
ATOM   13975 N  N     . LYS A 1 3209 ? 117.891 83.436  17.461  1.00 56.88  ? 3209 LYS A N     1 
ATOM   13976 C  CA    . LYS A 1 3209 ? 118.835 83.994  16.495  1.00 56.44  ? 3209 LYS A CA    1 
ATOM   13977 C  C     . LYS A 1 3209 ? 119.491 82.894  15.666  1.00 61.59  ? 3209 LYS A C     1 
ATOM   13978 O  O     . LYS A 1 3209 ? 119.663 83.036  14.446  1.00 63.23  ? 3209 LYS A O     1 
ATOM   13979 C  CB    . LYS A 1 3209 ? 119.893 84.827  17.219  1.00 59.08  ? 3209 LYS A CB    1 
ATOM   13980 C  CG    . LYS A 1 3209 ? 120.846 85.564  16.295  1.00 64.59  ? 3209 LYS A CG    1 
ATOM   13981 C  CD    . LYS A 1 3209 ? 121.447 86.781  16.981  1.00 64.17  ? 3209 LYS A CD    1 
ATOM   13982 C  CE    . LYS A 1 3209 ? 120.365 87.681  17.559  1.00 68.17  ? 3209 LYS A CE    1 
ATOM   13983 N  NZ    . LYS A 1 3209 ? 119.509 88.278  16.497  1.00 62.39  ? 3209 LYS A NZ    1 
ATOM   13984 N  N     . GLU A 1 3210 ? 119.858 81.784  16.311  1.00 59.40  ? 3210 GLU A N     1 
ATOM   13985 C  CA    . GLU A 1 3210 ? 120.428 80.657  15.585  1.00 61.65  ? 3210 GLU A CA    1 
ATOM   13986 C  C     . GLU A 1 3210 ? 119.426 80.080  14.596  1.00 62.89  ? 3210 GLU A C     1 
ATOM   13987 O  O     . GLU A 1 3210 ? 119.802 79.678  13.493  1.00 67.38  ? 3210 GLU A O     1 
ATOM   13988 C  CB    . GLU A 1 3210 ? 120.897 79.582  16.565  1.00 62.83  ? 3210 GLU A CB    1 
ATOM   13989 C  CG    . GLU A 1 3210 ? 122.208 79.906  17.259  1.00 69.73  ? 3210 GLU A CG    1 
ATOM   13990 C  CD    . GLU A 1 3210 ? 122.520 78.946  18.390  1.00 81.46  ? 3210 GLU A CD    1 
ATOM   13991 O  OE1   . GLU A 1 3210 ? 121.702 78.036  18.641  1.00 77.46  ? 3210 GLU A OE1   1 
ATOM   13992 O  OE2   . GLU A 1 3210 ? 123.582 79.102  19.028  1.00 79.68  ? 3210 GLU A OE2   1 
ATOM   13993 N  N     . THR A 1 3211 ? 118.148 80.025  14.974  1.00 59.47  ? 3211 THR A N     1 
ATOM   13994 C  CA    . THR A 1 3211 ? 117.119 79.541  14.058  1.00 64.60  ? 3211 THR A CA    1 
ATOM   13995 C  C     . THR A 1 3211 ? 116.989 80.456  12.845  1.00 65.51  ? 3211 THR A C     1 
ATOM   13996 O  O     . THR A 1 3211 ? 116.806 79.983  11.716  1.00 66.47  ? 3211 THR A O     1 
ATOM   13997 C  CB    . THR A 1 3211 ? 115.782 79.422  14.792  1.00 64.76  ? 3211 THR A CB    1 
ATOM   13998 O  OG1   . THR A 1 3211 ? 115.858 78.362  15.754  1.00 68.44  ? 3211 THR A OG1   1 
ATOM   13999 C  CG2   . THR A 1 3211 ? 114.655 79.123  13.817  1.00 64.77  ? 3211 THR A CG2   1 
ATOM   14000 N  N     . VAL A 1 3212 ? 117.078 81.770  13.060  1.00 62.13  ? 3212 VAL A N     1 
ATOM   14001 C  CA    . VAL A 1 3212 ? 117.049 82.704  11.935  1.00 63.77  ? 3212 VAL A CA    1 
ATOM   14002 C  C     . VAL A 1 3212 ? 118.240 82.464  11.012  1.00 68.48  ? 3212 VAL A C     1 
ATOM   14003 O  O     . VAL A 1 3212 ? 118.103 82.455  9.780   1.00 71.66  ? 3212 VAL A O     1 
ATOM   14004 C  CB    . VAL A 1 3212 ? 117.006 84.158  12.440  1.00 61.62  ? 3212 VAL A CB    1 
ATOM   14005 C  CG1   . VAL A 1 3212 ? 117.017 85.126  11.269  1.00 60.87  ? 3212 VAL A CG1   1 
ATOM   14006 C  CG2   . VAL A 1 3212 ? 115.772 84.383  13.296  1.00 58.84  ? 3212 VAL A CG2   1 
ATOM   14007 N  N     . ASP A 1 3213 ? 119.425 82.260  11.590  1.00 67.75  ? 3213 ASP A N     1 
ATOM   14008 C  CA    . ASP A 1 3213 ? 120.594 81.960  10.765  1.00 69.38  ? 3213 ASP A CA    1 
ATOM   14009 C  C     . ASP A 1 3213 ? 120.411 80.651  10.000  1.00 71.76  ? 3213 ASP A C     1 
ATOM   14010 O  O     . ASP A 1 3213 ? 120.795 80.545  8.826   1.00 78.20  ? 3213 ASP A O     1 
ATOM   14011 C  CB    . ASP A 1 3213 ? 121.851 81.908  11.632  1.00 75.83  ? 3213 ASP A CB    1 
ATOM   14012 C  CG    . ASP A 1 3213 ? 122.080 83.193  12.404  1.00 75.30  ? 3213 ASP A CG    1 
ATOM   14013 O  OD1   . ASP A 1 3213 ? 121.925 84.280  11.809  1.00 72.82  ? 3213 ASP A OD1   1 
ATOM   14014 O  OD2   . ASP A 1 3213 ? 122.417 83.116  13.604  1.00 74.78  ? 3213 ASP A OD2   1 
ATOM   14015 N  N     . GLN A 1 3214 ? 119.826 79.643  10.654  1.00 71.49  ? 3214 GLN A N     1 
ATOM   14016 C  CA    . GLN A 1 3214 ? 119.598 78.358  10.001  1.00 70.72  ? 3214 GLN A CA    1 
ATOM   14017 C  C     . GLN A 1 3214 ? 118.642 78.499  8.827   1.00 75.05  ? 3214 GLN A C     1 
ATOM   14018 O  O     . GLN A 1 3214 ? 118.875 77.922  7.760   1.00 82.41  ? 3214 GLN A O     1 
ATOM   14019 C  CB    . GLN A 1 3214 ? 119.049 77.337  11.001  1.00 71.20  ? 3214 GLN A CB    1 
ATOM   14020 C  CG    . GLN A 1 3214 ? 119.974 76.987  12.158  1.00 78.71  ? 3214 GLN A CG    1 
ATOM   14021 C  CD    . GLN A 1 3214 ? 121.442 77.099  11.804  1.00 81.63  ? 3214 GLN A CD    1 
ATOM   14022 O  OE1   . GLN A 1 3214 ? 121.958 76.326  11.001  1.00 80.41  ? 3214 GLN A OE1   1 
ATOM   14023 N  NE2   . GLN A 1 3214 ? 122.124 78.066  12.408  1.00 76.75  ? 3214 GLN A NE2   1 
ATOM   14024 N  N     . VAL A 1 3215 ? 117.555 79.255  9.001   1.00 74.52  ? 3215 VAL A N     1 
ATOM   14025 C  CA    . VAL A 1 3215 ? 116.610 79.403  7.898   1.00 75.41  ? 3215 VAL A CA    1 
ATOM   14026 C  C     . VAL A 1 3215 ? 117.226 80.223  6.773   1.00 78.80  ? 3215 VAL A C     1 
ATOM   14027 O  O     . VAL A 1 3215 ? 116.952 79.968  5.594   1.00 81.60  ? 3215 VAL A O     1 
ATOM   14028 C  CB    . VAL A 1 3215 ? 115.268 79.997  8.373   1.00 70.37  ? 3215 VAL A CB    1 
ATOM   14029 C  CG1   . VAL A 1 3215 ? 114.675 79.139  9.468   1.00 76.30  ? 3215 VAL A CG1   1 
ATOM   14030 C  CG2   . VAL A 1 3215 ? 115.414 81.436  8.829   1.00 68.60  ? 3215 VAL A CG2   1 
ATOM   14031 N  N     . GLU A 1 3216 ? 118.080 81.198  7.100   1.00 77.76  ? 3216 GLU A N     1 
ATOM   14032 C  CA    . GLU A 1 3216 ? 118.774 81.936  6.048   1.00 80.44  ? 3216 GLU A CA    1 
ATOM   14033 C  C     . GLU A 1 3216 ? 119.671 81.011  5.232   1.00 83.33  ? 3216 GLU A C     1 
ATOM   14034 O  O     . GLU A 1 3216 ? 119.620 81.004  3.993   1.00 87.34  ? 3216 GLU A O     1 
ATOM   14035 C  CB    . GLU A 1 3216 ? 119.585 83.081  6.657   1.00 82.00  ? 3216 GLU A CB    1 
ATOM   14036 C  CG    . GLU A 1 3216 ? 120.029 84.135  5.650   1.00 83.72  ? 3216 GLU A CG    1 
ATOM   14037 C  CD    . GLU A 1 3216 ? 121.344 83.788  4.977   1.00 90.03  ? 3216 GLU A CD    1 
ATOM   14038 O  OE1   . GLU A 1 3216 ? 122.344 83.577  5.695   1.00 92.53  ? 3216 GLU A OE1   1 
ATOM   14039 O  OE2   . GLU A 1 3216 ? 121.376 83.725  3.730   1.00 86.54  ? 3216 GLU A OE2   1 
ATOM   14040 N  N     . GLU A 1 3217 ? 120.487 80.197  5.909   1.00 81.90  ? 3217 GLU A N     1 
ATOM   14041 C  CA    . GLU A 1 3217 ? 121.392 79.325  5.167   1.00 83.09  ? 3217 GLU A CA    1 
ATOM   14042 C  C     . GLU A 1 3217 ? 120.638 78.205  4.460   1.00 85.19  ? 3217 GLU A C     1 
ATOM   14043 O  O     . GLU A 1 3217 ? 121.119 77.678  3.451   1.00 89.34  ? 3217 GLU A O     1 
ATOM   14044 C  CB    . GLU A 1 3217 ? 122.467 78.739  6.083   1.00 82.06  ? 3217 GLU A CB    1 
ATOM   14045 C  CG    . GLU A 1 3217 ? 121.997 77.615  6.983   1.00 83.29  ? 3217 GLU A CG    1 
ATOM   14046 C  CD    . GLU A 1 3217 ? 123.120 77.054  7.832   1.00 93.55  ? 3217 GLU A CD    1 
ATOM   14047 O  OE1   . GLU A 1 3217 ? 124.228 77.629  7.810   1.00 98.07  ? 3217 GLU A OE1   1 
ATOM   14048 O  OE2   . GLU A 1 3217 ? 122.903 76.022  8.498   1.00 90.91  ? 3217 GLU A OE2   1 
ATOM   14049 N  N     . VAL A 1 3472 ? 111.425 75.274  5.079   1.00 78.88  ? 3472 VAL A N     1 
ATOM   14050 C  CA    . VAL A 1 3472 ? 111.690 76.710  5.101   1.00 75.53  ? 3472 VAL A CA    1 
ATOM   14051 C  C     . VAL A 1 3472 ? 110.414 77.478  5.420   1.00 77.58  ? 3472 VAL A C     1 
ATOM   14052 O  O     . VAL A 1 3472 ? 110.402 78.373  6.273   1.00 77.82  ? 3472 VAL A O     1 
ATOM   14053 C  CB    . VAL A 1 3472 ? 112.298 77.164  3.761   1.00 75.29  ? 3472 VAL A CB    1 
ATOM   14054 C  CG1   . VAL A 1 3472 ? 112.136 78.667  3.583   1.00 74.24  ? 3472 VAL A CG1   1 
ATOM   14055 C  CG2   . VAL A 1 3472 ? 113.761 76.774  3.681   1.00 80.20  ? 3472 VAL A CG2   1 
ATOM   14056 N  N     . ASN A 1 3473 ? 109.316 77.129  4.744   1.00 81.10  ? 3473 ASN A N     1 
ATOM   14057 C  CA    . ASN A 1 3473 ? 108.049 77.815  4.981   1.00 79.26  ? 3473 ASN A CA    1 
ATOM   14058 C  C     . ASN A 1 3473 ? 107.566 77.603  6.411   1.00 78.94  ? 3473 ASN A C     1 
ATOM   14059 O  O     . ASN A 1 3473 ? 107.126 78.548  7.078   1.00 77.96  ? 3473 ASN A O     1 
ATOM   14060 C  CB    . ASN A 1 3473 ? 106.998 77.334  3.979   1.00 74.20  ? 3473 ASN A CB    1 
ATOM   14061 C  CG    . ASN A 1 3473 ? 107.405 77.587  2.541   1.00 81.63  ? 3473 ASN A CG    1 
ATOM   14062 O  OD1   . ASN A 1 3473 ? 108.463 78.157  2.273   1.00 80.99  ? 3473 ASN A OD1   1 
ATOM   14063 N  ND2   . ASN A 1 3473 ? 106.563 77.163  1.605   1.00 84.30  ? 3473 ASN A ND2   1 
ATOM   14064 N  N     . ARG A 1 3474 ? 107.651 76.364  6.903   1.00 77.44  ? 3474 ARG A N     1 
ATOM   14065 C  CA    . ARG A 1 3474 ? 107.176 76.073  8.252   1.00 73.95  ? 3474 ARG A CA    1 
ATOM   14066 C  C     . ARG A 1 3474 ? 107.995 76.814  9.301   1.00 74.84  ? 3474 ARG A C     1 
ATOM   14067 O  O     . ARG A 1 3474 ? 107.438 77.366  10.258  1.00 73.88  ? 3474 ARG A O     1 
ATOM   14068 C  CB    . ARG A 1 3474 ? 107.210 74.566  8.509   1.00 69.95  ? 3474 ARG A CB    1 
ATOM   14069 C  CG    . ARG A 1 3474 ? 106.647 74.163  9.861   1.00 71.66  ? 3474 ARG A CG    1 
ATOM   14070 C  CD    . ARG A 1 3474 ? 106.640 72.654  10.036  1.00 72.80  ? 3474 ARG A CD    1 
ATOM   14071 N  NE    . ARG A 1 3474 ? 107.987 72.097  10.050  1.00 82.32  ? 3474 ARG A NE    1 
ATOM   14072 C  CZ    . ARG A 1 3474 ? 108.261 70.801  10.004  1.00 86.24  ? 3474 ARG A CZ    1 
ATOM   14073 N  NH1   . ARG A 1 3474 ? 107.301 69.893  9.944   1.00 84.41  ? 3474 ARG A NH1   1 
ATOM   14074 N  NH2   . ARG A 1 3474 ? 109.531 70.405  10.019  1.00 87.64  ? 3474 ARG A NH2   1 
ATOM   14075 N  N     . SER A 1 3475 ? 109.318 76.856  9.134   1.00 76.05  ? 3475 SER A N     1 
ATOM   14076 C  CA    . SER A 1 3475 ? 110.145 77.524  10.131  1.00 73.60  ? 3475 SER A CA    1 
ATOM   14077 C  C     . SER A 1 3475 ? 110.019 79.039  10.038  1.00 72.38  ? 3475 SER A C     1 
ATOM   14078 O  O     . SER A 1 3475 ? 110.119 79.729  11.059  1.00 76.19  ? 3475 SER A O     1 
ATOM   14079 C  CB    . SER A 1 3475 ? 111.603 77.093  9.985   1.00 74.82  ? 3475 SER A CB    1 
ATOM   14080 O  OG    . SER A 1 3475 ? 112.404 77.715  10.973  1.00 86.07  ? 3475 SER A OG    1 
ATOM   14081 N  N     . THR A 1 3476 ? 109.788 79.578  8.837   1.00 71.96  ? 3476 THR A N     1 
ATOM   14082 C  CA    . THR A 1 3476 ? 109.496 81.002  8.719   1.00 70.45  ? 3476 THR A CA    1 
ATOM   14083 C  C     . THR A 1 3476 ? 108.187 81.348  9.417   1.00 70.78  ? 3476 THR A C     1 
ATOM   14084 O  O     . THR A 1 3476 ? 108.089 82.376  10.098  1.00 69.04  ? 3476 THR A O     1 
ATOM   14085 C  CB    . THR A 1 3476 ? 109.446 81.410  7.246   1.00 72.98  ? 3476 THR A CB    1 
ATOM   14086 O  OG1   . THR A 1 3476 ? 110.670 81.032  6.602   1.00 73.94  ? 3476 THR A OG1   1 
ATOM   14087 C  CG2   . THR A 1 3476 ? 109.256 82.913  7.113   1.00 72.12  ? 3476 THR A CG2   1 
ATOM   14088 N  N     . ALA A 1 3477 ? 107.171 80.493  9.266   1.00 74.55  ? 3477 ALA A N     1 
ATOM   14089 C  CA    . ALA A 1 3477 ? 105.920 80.702  9.987   1.00 74.99  ? 3477 ALA A CA    1 
ATOM   14090 C  C     . ALA A 1 3477 ? 106.133 80.618  11.493  1.00 72.21  ? 3477 ALA A C     1 
ATOM   14091 O  O     . ALA A 1 3477 ? 105.538 81.388  12.256  1.00 69.49  ? 3477 ALA A O     1 
ATOM   14092 C  CB    . ALA A 1 3477 ? 104.875 79.683  9.533   1.00 73.31  ? 3477 ALA A CB    1 
ATOM   14093 N  N     . LEU A 1 3478 ? 106.975 79.684  11.940  1.00 69.97  ? 3478 LEU A N     1 
ATOM   14094 C  CA    . LEU A 1 3478 ? 107.269 79.568  13.366  1.00 64.63  ? 3478 LEU A CA    1 
ATOM   14095 C  C     . LEU A 1 3478 ? 107.965 80.818  13.893  1.00 65.29  ? 3478 LEU A C     1 
ATOM   14096 O  O     . LEU A 1 3478 ? 107.638 81.307  14.981  1.00 68.02  ? 3478 LEU A O     1 
ATOM   14097 C  CB    . LEU A 1 3478 ? 108.125 78.329  13.625  1.00 62.31  ? 3478 LEU A CB    1 
ATOM   14098 C  CG    . LEU A 1 3478 ? 108.451 78.027  15.089  1.00 62.49  ? 3478 LEU A CG    1 
ATOM   14099 C  CD1   . LEU A 1 3478 ? 107.230 77.474  15.807  1.00 60.49  ? 3478 LEU A CD1   1 
ATOM   14100 C  CD2   . LEU A 1 3478 ? 109.621 77.061  15.191  1.00 62.03  ? 3478 LEU A CD2   1 
ATOM   14101 N  N     . LEU A 1 3479 ? 108.932 81.346  13.138  1.00 62.73  ? 3479 LEU A N     1 
ATOM   14102 C  CA    . LEU A 1 3479 ? 109.607 82.574  13.548  1.00 59.44  ? 3479 LEU A CA    1 
ATOM   14103 C  C     . LEU A 1 3479 ? 108.645 83.754  13.572  1.00 63.52  ? 3479 LEU A C     1 
ATOM   14104 O  O     . LEU A 1 3479 ? 108.721 84.607  14.465  1.00 66.95  ? 3479 LEU A O     1 
ATOM   14105 C  CB    . LEU A 1 3479 ? 110.790 82.864  12.625  1.00 60.22  ? 3479 LEU A CB    1 
ATOM   14106 C  CG    . LEU A 1 3479 ? 111.966 81.899  12.748  1.00 61.50  ? 3479 LEU A CG    1 
ATOM   14107 C  CD1   . LEU A 1 3479 ? 113.023 82.201  11.700  1.00 63.86  ? 3479 LEU A CD1   1 
ATOM   14108 C  CD2   . LEU A 1 3479 ? 112.550 81.992  14.147  1.00 57.97  ? 3479 LEU A CD2   1 
ATOM   14109 N  N     . LYS A 1 3480 ? 107.741 83.828  12.593  1.00 67.02  ? 3480 LYS A N     1 
ATOM   14110 C  CA    . LYS A 1 3480 ? 106.712 84.862  12.620  1.00 68.24  ? 3480 LYS A CA    1 
ATOM   14111 C  C     . LYS A 1 3480 ? 105.813 84.712  13.840  1.00 65.37  ? 3480 LYS A C     1 
ATOM   14112 O  O     . LYS A 1 3480 ? 105.349 85.712  14.399  1.00 63.85  ? 3480 LYS A O     1 
ATOM   14113 C  CB    . LYS A 1 3480 ? 105.890 84.812  11.331  1.00 71.45  ? 3480 LYS A CB    1 
ATOM   14114 C  CG    . LYS A 1 3480 ? 104.873 85.935  11.178  1.00 74.49  ? 3480 LYS A CG    1 
ATOM   14115 C  CD    . LYS A 1 3480 ? 103.469 85.470  11.537  1.00 75.66  ? 3480 LYS A CD    1 
ATOM   14116 C  CE    . LYS A 1 3480 ? 102.936 84.484  10.511  1.00 76.75  ? 3480 LYS A CE    1 
ATOM   14117 N  NZ    . LYS A 1 3480 ? 101.562 84.020  10.847  1.00 82.56  ? 3480 LYS A NZ    1 
ATOM   14118 N  N     . SER A 1 3481 ? 105.560 83.473  14.266  1.00 65.06  ? 3481 SER A N     1 
ATOM   14119 C  CA    . SER A 1 3481 ? 104.744 83.241  15.452  1.00 64.54  ? 3481 SER A CA    1 
ATOM   14120 C  C     . SER A 1 3481 ? 105.500 83.572  16.734  1.00 63.99  ? 3481 SER A C     1 
ATOM   14121 O  O     . SER A 1 3481 ? 104.879 83.916  17.746  1.00 63.14  ? 3481 SER A O     1 
ATOM   14122 C  CB    . SER A 1 3481 ? 104.263 81.790  15.473  1.00 64.39  ? 3481 SER A CB    1 
ATOM   14123 O  OG    . SER A 1 3481 ? 103.432 81.539  16.592  1.00 69.97  ? 3481 SER A OG    1 
ATOM   14124 N  N     . LEU A 1 3482 ? 106.828 83.473  16.715  1.00 64.79  ? 3482 LEU A N     1 
ATOM   14125 C  CA    . LEU A 1 3482 ? 107.649 83.698  17.898  1.00 61.32  ? 3482 LEU A CA    1 
ATOM   14126 C  C     . LEU A 1 3482 ? 108.165 85.128  18.014  1.00 63.81  ? 3482 LEU A C     1 
ATOM   14127 O  O     . LEU A 1 3482 ? 108.966 85.407  18.912  1.00 70.28  ? 3482 LEU A O     1 
ATOM   14128 C  CB    . LEU A 1 3482 ? 108.836 82.729  17.907  1.00 60.46  ? 3482 LEU A CB    1 
ATOM   14129 C  CG    . LEU A 1 3482 ? 108.528 81.256  18.181  1.00 61.58  ? 3482 LEU A CG    1 
ATOM   14130 C  CD1   . LEU A 1 3482 ? 109.814 80.468  18.377  1.00 58.40  ? 3482 LEU A CD1   1 
ATOM   14131 C  CD2   . LEU A 1 3482 ? 107.619 81.111  19.391  1.00 61.43  ? 3482 LEU A CD2   1 
ATOM   14132 N  N     . SER A 1 3483 ? 107.740 86.032  17.128  1.00 63.31  ? 3483 SER A N     1 
ATOM   14133 C  CA    . SER A 1 3483 ? 108.249 87.401  17.161  1.00 68.25  ? 3483 SER A CA    1 
ATOM   14134 C  C     . SER A 1 3483 ? 107.868 88.111  18.456  1.00 73.23  ? 3483 SER A C     1 
ATOM   14135 O  O     . SER A 1 3483 ? 108.695 88.811  19.056  1.00 75.33  ? 3483 SER A O     1 
ATOM   14136 C  CB    . SER A 1 3483 ? 107.733 88.180  15.951  1.00 73.89  ? 3483 SER A CB    1 
ATOM   14137 O  OG    . SER A 1 3483 ? 108.143 89.535  16.004  1.00 80.67  ? 3483 SER A OG    1 
ATOM   14138 N  N     . ALA A 1 3484 ? 106.619 87.948  18.900  1.00 68.33  ? 3484 ALA A N     1 
ATOM   14139 C  CA    . ALA A 1 3484 ? 106.176 88.607  20.125  1.00 68.63  ? 3484 ALA A CA    1 
ATOM   14140 C  C     . ALA A 1 3484 ? 106.946 88.097  21.337  1.00 68.74  ? 3484 ALA A C     1 
ATOM   14141 O  O     . ALA A 1 3484 ? 107.343 88.883  22.207  1.00 69.14  ? 3484 ALA A O     1 
ATOM   14142 C  CB    . ALA A 1 3484 ? 104.674 88.402  20.318  1.00 65.89  ? 3484 ALA A CB    1 
ATOM   14143 N  N     . GLU A 1 3485 ? 107.164 86.781  21.411  1.00 66.83  ? 3485 GLU A N     1 
ATOM   14144 C  CA    . GLU A 1 3485 ? 107.941 86.221  22.511  1.00 63.52  ? 3485 GLU A CA    1 
ATOM   14145 C  C     . GLU A 1 3485 ? 109.369 86.746  22.495  1.00 63.15  ? 3485 GLU A C     1 
ATOM   14146 O  O     . GLU A 1 3485 ? 109.930 87.070  23.548  1.00 68.75  ? 3485 GLU A O     1 
ATOM   14147 C  CB    . GLU A 1 3485 ? 107.929 84.694  22.442  1.00 64.47  ? 3485 GLU A CB    1 
ATOM   14148 C  CG    . GLU A 1 3485 ? 106.640 84.056  22.935  1.00 68.50  ? 3485 GLU A CG    1 
ATOM   14149 C  CD    . GLU A 1 3485 ? 105.523 84.118  21.911  1.00 73.96  ? 3485 GLU A CD    1 
ATOM   14150 O  OE1   . GLU A 1 3485 ? 105.781 84.551  20.768  1.00 72.21  ? 3485 GLU A OE1   1 
ATOM   14151 O  OE2   . GLU A 1 3485 ? 104.384 83.735  22.252  1.00 78.20  ? 3485 GLU A OE2   1 
ATOM   14152 N  N     . ARG A 1 3486 ? 109.972 86.842  21.308  1.00 60.45  ? 3486 ARG A N     1 
ATOM   14153 C  CA    . ARG A 1 3486 ? 111.328 87.374  21.207  1.00 67.13  ? 3486 ARG A CA    1 
ATOM   14154 C  C     . ARG A 1 3486 ? 111.391 88.822  21.677  1.00 67.66  ? 3486 ARG A C     1 
ATOM   14155 O  O     . ARG A 1 3486 ? 112.307 89.203  22.418  1.00 68.06  ? 3486 ARG A O     1 
ATOM   14156 C  CB    . ARG A 1 3486 ? 111.827 87.243  19.767  1.00 66.12  ? 3486 ARG A CB    1 
ATOM   14157 C  CG    . ARG A 1 3486 ? 113.279 87.639  19.560  1.00 67.53  ? 3486 ARG A CG    1 
ATOM   14158 C  CD    . ARG A 1 3486 ? 113.603 87.812  18.080  1.00 69.90  ? 3486 ARG A CD    1 
ATOM   14159 N  NE    . ARG A 1 3486 ? 112.572 88.541  17.351  1.00 79.37  ? 3486 ARG A NE    1 
ATOM   14160 C  CZ    . ARG A 1 3486 ? 112.308 89.833  17.500  1.00 78.16  ? 3486 ARG A CZ    1 
ATOM   14161 N  NH1   . ARG A 1 3486 ? 113.001 90.590  18.334  1.00 77.45  ? 3486 ARG A NH1   1 
ATOM   14162 N  NH2   . ARG A 1 3486 ? 111.327 90.381  16.788  1.00 78.89  ? 3486 ARG A NH2   1 
ATOM   14163 N  N     . GLU A 1 3487 ? 110.417 89.641  21.268  1.00 67.95  ? 3487 GLU A N     1 
ATOM   14164 C  CA    . GLU A 1 3487 ? 110.394 91.038  21.695  1.00 71.42  ? 3487 GLU A CA    1 
ATOM   14165 C  C     . GLU A 1 3487 ? 110.234 91.150  23.207  1.00 70.04  ? 3487 GLU A C     1 
ATOM   14166 O  O     . GLU A 1 3487 ? 110.936 91.935  23.861  1.00 66.42  ? 3487 GLU A O     1 
ATOM   14167 C  CB    . GLU A 1 3487 ? 109.265 91.782  20.980  1.00 72.50  ? 3487 GLU A CB    1 
ATOM   14168 C  CG    . GLU A 1 3487 ? 109.513 92.044  19.498  1.00 77.51  ? 3487 GLU A CG    1 
ATOM   14169 C  CD    . GLU A 1 3487 ? 110.493 93.175  19.245  1.00 83.17  ? 3487 GLU A CD    1 
ATOM   14170 O  OE1   . GLU A 1 3487 ? 111.681 93.037  19.605  1.00 83.00  ? 3487 GLU A OE1   1 
ATOM   14171 O  OE2   . GLU A 1 3487 ? 110.073 94.208  18.681  1.00 81.68  ? 3487 GLU A OE2   1 
ATOM   14172 N  N     . ARG A 1 3488 ? 109.320 90.362  23.779  1.00 67.70  ? 3488 ARG A N     1 
ATOM   14173 C  CA    . ARG A 1 3488 ? 109.109 90.394  25.222  1.00 61.87  ? 3488 ARG A CA    1 
ATOM   14174 C  C     . ARG A 1 3488 ? 110.359 89.954  25.972  1.00 65.72  ? 3488 ARG A C     1 
ATOM   14175 O  O     . ARG A 1 3488 ? 110.711 90.537  27.005  1.00 68.35  ? 3488 ARG A O     1 
ATOM   14176 C  CB    . ARG A 1 3488 ? 107.917 89.513  25.593  1.00 59.88  ? 3488 ARG A CB    1 
ATOM   14177 C  CG    . ARG A 1 3488 ? 107.589 89.496  27.076  1.00 64.67  ? 3488 ARG A CG    1 
ATOM   14178 C  CD    . ARG A 1 3488 ? 106.885 88.208  27.478  1.00 66.86  ? 3488 ARG A CD    1 
ATOM   14179 N  NE    . ARG A 1 3488 ? 105.869 87.808  26.512  1.00 66.95  ? 3488 ARG A NE    1 
ATOM   14180 C  CZ    . ARG A 1 3488 ? 105.934 86.715  25.764  1.00 68.68  ? 3488 ARG A CZ    1 
ATOM   14181 N  NH1   . ARG A 1 3488 ? 106.957 85.881  25.846  1.00 69.16  ? 3488 ARG A NH1   1 
ATOM   14182 N  NH2   . ARG A 1 3488 ? 104.947 86.452  24.912  1.00 68.96  ? 3488 ARG A NH2   1 
ATOM   14183 N  N     . TRP A 1 3489 ? 111.043 88.924  25.469  1.00 59.55  ? 3489 TRP A N     1 
ATOM   14184 C  CA    . TRP A 1 3489 ? 112.254 88.452  26.132  1.00 57.54  ? 3489 TRP A CA    1 
ATOM   14185 C  C     . TRP A 1 3489 ? 113.375 89.480  26.052  1.00 61.97  ? 3489 TRP A C     1 
ATOM   14186 O  O     . TRP A 1 3489 ? 114.106 89.672  27.030  1.00 67.36  ? 3489 TRP A O     1 
ATOM   14187 C  CB    . TRP A 1 3489 ? 112.690 87.111  25.543  1.00 56.44  ? 3489 TRP A CB    1 
ATOM   14188 C  CG    . TRP A 1 3489 ? 111.655 86.037  25.701  1.00 57.79  ? 3489 TRP A CG    1 
ATOM   14189 C  CD1   . TRP A 1 3489 ? 110.555 86.073  26.509  1.00 56.80  ? 3489 TRP A CD1   1 
ATOM   14190 C  CD2   . TRP A 1 3489 ? 111.618 84.771  25.032  1.00 57.29  ? 3489 TRP A CD2   1 
ATOM   14191 N  NE1   . TRP A 1 3489 ? 109.839 84.908  26.387  1.00 56.99  ? 3489 TRP A NE1   1 
ATOM   14192 C  CE2   . TRP A 1 3489 ? 110.470 84.092  25.486  1.00 60.05  ? 3489 TRP A CE2   1 
ATOM   14193 C  CE3   . TRP A 1 3489 ? 112.445 84.145  24.095  1.00 54.81  ? 3489 TRP A CE3   1 
ATOM   14194 C  CZ2   . TRP A 1 3489 ? 110.128 82.820  25.035  1.00 59.16  ? 3489 TRP A CZ2   1 
ATOM   14195 C  CZ3   . TRP A 1 3489 ? 112.104 82.884  23.649  1.00 57.32  ? 3489 TRP A CZ3   1 
ATOM   14196 C  CH2   . TRP A 1 3489 ? 110.956 82.234  24.119  1.00 60.48  ? 3489 TRP A CH2   1 
ATOM   14197 N  N     . GLU A 1 3490 ? 113.530 90.159  24.909  1.00 63.70  ? 3490 GLU A N     1 
ATOM   14198 C  CA    . GLU A 1 3490 ? 114.537 91.217  24.851  1.00 65.92  ? 3490 GLU A CA    1 
ATOM   14199 C  C     . GLU A 1 3490 ? 114.206 92.351  25.815  1.00 65.31  ? 3490 GLU A C     1 
ATOM   14200 O  O     . GLU A 1 3490 ? 115.101 92.877  26.488  1.00 63.25  ? 3490 GLU A O     1 
ATOM   14201 C  CB    . GLU A 1 3490 ? 114.707 91.761  23.429  1.00 64.77  ? 3490 GLU A CB    1 
ATOM   14202 C  CG    . GLU A 1 3490 ? 115.214 90.752  22.412  1.00 71.06  ? 3490 GLU A CG    1 
ATOM   14203 C  CD    . GLU A 1 3490 ? 114.643 90.966  21.022  1.00 79.08  ? 3490 GLU A CD    1 
ATOM   14204 O  OE1   . GLU A 1 3490 ? 113.415 91.125  20.889  1.00 78.68  ? 3490 GLU A OE1   1 
ATOM   14205 O  OE2   . GLU A 1 3490 ? 115.432 90.973  20.055  1.00 77.20  ? 3490 GLU A OE2   1 
ATOM   14206 N  N     . LYS A 1 3491 ? 112.931 92.735  25.907  1.00 65.36  ? 3491 LYS A N     1 
ATOM   14207 C  CA    . LYS A 1 3491 ? 112.557 93.796  26.840  1.00 66.63  ? 3491 LYS A CA    1 
ATOM   14208 C  C     . LYS A 1 3491 ? 112.835 93.392  28.287  1.00 64.70  ? 3491 LYS A C     1 
ATOM   14209 O  O     . LYS A 1 3491 ? 113.384 94.180  29.072  1.00 67.04  ? 3491 LYS A O     1 
ATOM   14210 C  CB    . LYS A 1 3491 ? 111.084 94.158  26.653  1.00 66.77  ? 3491 LYS A CB    1 
ATOM   14211 C  CG    . LYS A 1 3491 ? 110.596 95.281  27.551  1.00 73.65  ? 3491 LYS A CG    1 
ATOM   14212 C  CD    . LYS A 1 3491 ? 109.171 95.679  27.204  1.00 77.74  ? 3491 LYS A CD    1 
ATOM   14213 C  CE    . LYS A 1 3491 ? 108.180 94.608  27.630  1.00 74.87  ? 3491 LYS A CE    1 
ATOM   14214 N  NZ    . LYS A 1 3491 ? 108.081 94.499  29.112  1.00 67.61  ? 3491 LYS A NZ    1 
ATOM   14215 N  N     . THR A 1 3492 ? 112.469 92.162  28.656  1.00 63.72  ? 3492 THR A N     1 
ATOM   14216 C  CA    . THR A 1 3492 ? 112.699 91.704  30.022  1.00 59.54  ? 3492 THR A CA    1 
ATOM   14217 C  C     . THR A 1 3492 ? 114.190 91.604  30.326  1.00 58.93  ? 3492 THR A C     1 
ATOM   14218 O  O     . THR A 1 3492 ? 114.628 91.948  31.430  1.00 63.68  ? 3492 THR A O     1 
ATOM   14219 C  CB    . THR A 1 3492 ? 112.008 90.360  30.251  1.00 56.69  ? 3492 THR A CB    1 
ATOM   14220 O  OG1   . THR A 1 3492 ? 110.610 90.489  29.965  1.00 60.88  ? 3492 THR A OG1   1 
ATOM   14221 C  CG2   . THR A 1 3492 ? 112.169 89.922  31.698  1.00 55.75  ? 3492 THR A CG2   1 
ATOM   14222 N  N     . SER A 1 3493 ? 114.987 91.140  29.358  1.00 56.79  ? 3493 SER A N     1 
ATOM   14223 C  CA    . SER A 1 3493 ? 116.434 91.114  29.539  1.00 59.89  ? 3493 SER A CA    1 
ATOM   14224 C  C     . SER A 1 3493 ? 117.006 92.518  29.669  1.00 64.52  ? 3493 SER A C     1 
ATOM   14225 O  O     . SER A 1 3493 ? 118.024 92.713  30.342  1.00 63.63  ? 3493 SER A O     1 
ATOM   14226 C  CB    . SER A 1 3493 ? 117.094 90.376  28.374  1.00 57.25  ? 3493 SER A CB    1 
ATOM   14227 O  OG    . SER A 1 3493 ? 118.507 90.430  28.469  1.00 61.58  ? 3493 SER A OG    1 
ATOM   14228 N  N     . GLU A 1 3494 ? 116.382 93.503  29.020  1.00 65.36  ? 3494 GLU A N     1 
ATOM   14229 C  CA    . GLU A 1 3494 ? 116.827 94.883  29.184  1.00 65.64  ? 3494 GLU A CA    1 
ATOM   14230 C  C     . GLU A 1 3494 ? 116.534 95.396  30.590  1.00 65.95  ? 3494 GLU A C     1 
ATOM   14231 O  O     . GLU A 1 3494 ? 117.360 96.099  31.184  1.00 66.45  ? 3494 GLU A O     1 
ATOM   14232 C  CB    . GLU A 1 3494 ? 116.166 95.777  28.134  1.00 69.43  ? 3494 GLU A CB    1 
ATOM   14233 C  CG    . GLU A 1 3494 ? 116.428 97.270  28.309  1.00 73.61  ? 3494 GLU A CG    1 
ATOM   14234 C  CD    . GLU A 1 3494 ? 117.871 97.660  28.033  1.00 81.00  ? 3494 GLU A CD    1 
ATOM   14235 O  OE1   . GLU A 1 3494 ? 118.758 97.310  28.841  1.00 86.61  ? 3494 GLU A OE1   1 
ATOM   14236 O  OE2   . GLU A 1 3494 ? 118.120 98.318  27.001  1.00 84.96  ? 3494 GLU A OE2   1 
ATOM   14237 N  N     . THR A 1 3495 ? 115.370 95.049  31.142  1.00 62.92  ? 3495 THR A N     1 
ATOM   14238 C  CA    . THR A 1 3495 ? 115.014 95.470  32.500  1.00 60.05  ? 3495 THR A CA    1 
ATOM   14239 C  C     . THR A 1 3495 ? 115.837 94.771  33.590  1.00 59.56  ? 3495 THR A C     1 
ATOM   14240 O  O     . THR A 1 3495 ? 115.599 95.013  34.787  1.00 61.37  ? 3495 THR A O     1 
ATOM   14241 C  CB    . THR A 1 3495 ? 113.523 95.236  32.761  1.00 58.99  ? 3495 THR A CB    1 
ATOM   14242 O  OG1   . THR A 1 3495 ? 113.269 93.830  32.885  1.00 60.10  ? 3495 THR A OG1   1 
ATOM   14243 C  CG2   . THR A 1 3495 ? 112.679 95.817  31.640  1.00 62.98  ? 3495 THR A CG2   1 
ATOM   14244 N  N     . PHE A 1 3496 ? 116.795 93.928  33.195  1.00 56.34  ? 3496 PHE A N     1 
ATOM   14245 C  CA    . PHE A 1 3496 ? 117.531 93.103  34.148  1.00 51.16  ? 3496 PHE A CA    1 
ATOM   14246 C  C     . PHE A 1 3496 ? 118.333 93.953  35.124  1.00 50.58  ? 3496 PHE A C     1 
ATOM   14247 O  O     . PHE A 1 3496 ? 118.350 93.673  36.328  1.00 49.79  ? 3496 PHE A O     1 
ATOM   14248 C  CB    . PHE A 1 3496 ? 118.457 92.154  33.393  1.00 49.78  ? 3496 PHE A CB    1 
ATOM   14249 C  CG    . PHE A 1 3496 ? 119.279 91.266  34.278  1.00 48.66  ? 3496 PHE A CG    1 
ATOM   14250 C  CD1   . PHE A 1 3496 ? 118.676 90.493  35.253  1.00 46.85  ? 3496 PHE A CD1   1 
ATOM   14251 C  CD2   . PHE A 1 3496 ? 120.656 91.205  34.137  1.00 48.34  ? 3496 PHE A CD2   1 
ATOM   14252 C  CE1   . PHE A 1 3496 ? 119.426 89.670  36.064  1.00 41.33  ? 3496 PHE A CE1   1 
ATOM   14253 C  CE2   . PHE A 1 3496 ? 121.413 90.386  34.951  1.00 43.29  ? 3496 PHE A CE2   1 
ATOM   14254 C  CZ    . PHE A 1 3496 ? 120.797 89.619  35.916  1.00 40.58  ? 3496 PHE A CZ    1 
ATOM   14255 N  N     . LYS A 1 3497 ? 119.016 94.985  34.623  1.00 51.29  ? 3497 LYS A N     1 
ATOM   14256 C  CA    . LYS A 1 3497 ? 119.866 95.800  35.487  1.00 48.10  ? 3497 LYS A CA    1 
ATOM   14257 C  C     . LYS A 1 3497 ? 119.042 96.602  36.486  1.00 45.26  ? 3497 LYS A C     1 
ATOM   14258 O  O     . LYS A 1 3497 ? 119.436 96.745  37.649  1.00 48.68  ? 3497 LYS A O     1 
ATOM   14259 C  CB    . LYS A 1 3497 ? 120.746 96.726  34.645  1.00 51.18  ? 3497 LYS A CB    1 
ATOM   14260 C  CG    . LYS A 1 3497 ? 122.006 96.069  34.083  1.00 53.01  ? 3497 LYS A CG    1 
ATOM   14261 C  CD    . LYS A 1 3497 ? 121.700 95.114  32.938  1.00 59.92  ? 3497 LYS A CD    1 
ATOM   14262 C  CE    . LYS A 1 3497 ? 122.975 94.543  32.339  1.00 60.72  ? 3497 LYS A CE    1 
ATOM   14263 N  NZ    . LYS A 1 3497 ? 122.688 93.518  31.298  1.00 60.45  ? 3497 LYS A NZ    1 
ATOM   14264 N  N     . ASN A 1 3498 ? 117.899 97.141  36.054  1.00 47.42  ? 3498 ASN A N     1 
ATOM   14265 C  CA    . ASN A 1 3498 ? 117.035 97.864  36.981  1.00 44.62  ? 3498 ASN A CA    1 
ATOM   14266 C  C     . ASN A 1 3498 ? 116.485 96.934  38.056  1.00 42.04  ? 3498 ASN A C     1 
ATOM   14267 O  O     . ASN A 1 3498 ? 116.432 97.299  39.241  1.00 40.46  ? 3498 ASN A O     1 
ATOM   14268 C  CB    . ASN A 1 3498 ? 115.896 98.542  36.219  1.00 46.23  ? 3498 ASN A CB    1 
ATOM   14269 C  CG    . ASN A 1 3498 ? 115.243 99.654  37.016  1.00 55.10  ? 3498 ASN A CG    1 
ATOM   14270 O  OD1   . ASN A 1 3498 ? 114.330 99.415  37.806  1.00 56.67  ? 3498 ASN A OD1   1 
ATOM   14271 N  ND2   . ASN A 1 3498 ? 115.710 100.880 36.812  1.00 60.35  ? 3498 ASN A ND2   1 
ATOM   14272 N  N     . GLN A 1 3499 ? 116.077 95.721  37.664  1.00 40.11  ? 3499 GLN A N     1 
ATOM   14273 C  CA    . GLN A 1 3499 ? 115.633 94.751  38.661  1.00 41.00  ? 3499 GLN A CA    1 
ATOM   14274 C  C     . GLN A 1 3499 ? 116.753 94.426  39.646  1.00 40.01  ? 3499 GLN A C     1 
ATOM   14275 O  O     . GLN A 1 3499 ? 116.526 94.381  40.864  1.00 36.34  ? 3499 GLN A O     1 
ATOM   14276 C  CB    . GLN A 1 3499 ? 115.133 93.482  37.972  1.00 41.87  ? 3499 GLN A CB    1 
ATOM   14277 C  CG    . GLN A 1 3499 ? 113.885 93.662  37.118  1.00 54.38  ? 3499 GLN A CG    1 
ATOM   14278 C  CD    . GLN A 1 3499 ? 112.678 94.101  37.921  1.00 63.09  ? 3499 GLN A CD    1 
ATOM   14279 O  OE1   . GLN A 1 3499 ? 112.122 93.329  38.703  1.00 62.48  ? 3499 GLN A OE1   1 
ATOM   14280 N  NE2   . GLN A 1 3499 ? 112.270 95.351  37.738  1.00 58.92  ? 3499 GLN A NE2   1 
ATOM   14281 N  N     . MET A 1 3500 ? 117.970 94.210  39.134  1.00 39.15  ? 3500 MET A N     1 
ATOM   14282 C  CA    . MET A 1 3500 ? 119.124 93.957  39.992  1.00 35.02  ? 3500 MET A CA    1 
ATOM   14283 C  C     . MET A 1 3500 ? 119.337 95.090  40.983  1.00 35.17  ? 3500 MET A C     1 
ATOM   14284 O  O     . MET A 1 3500 ? 119.608 94.851  42.165  1.00 35.48  ? 3500 MET A O     1 
ATOM   14285 C  CB    . MET A 1 3500 ? 120.380 93.777  39.139  1.00 40.86  ? 3500 MET A CB    1 
ATOM   14286 C  CG    . MET A 1 3500 ? 120.703 92.354  38.727  1.00 42.21  ? 3500 MET A CG    1 
ATOM   14287 S  SD    . MET A 1 3500 ? 120.802 91.222  40.122  1.00 57.26  ? 3500 MET A SD    1 
ATOM   14288 C  CE    . MET A 1 3500 ? 120.033 89.768  39.426  1.00 39.13  ? 3500 MET A CE    1 
ATOM   14289 N  N     . SER A 1 3501 ? 119.242 96.334  40.511  1.00 33.36  ? 3501 SER A N     1 
ATOM   14290 C  CA    . SER A 1 3501 ? 119.455 97.476  41.392  1.00 31.39  ? 3501 SER A CA    1 
ATOM   14291 C  C     . SER A 1 3501 ? 118.389 97.560  42.477  1.00 27.20  ? 3501 SER A C     1 
ATOM   14292 O  O     . SER A 1 3501 ? 118.709 97.861  43.632  1.00 37.63  ? 3501 SER A O     1 
ATOM   14293 C  CB    . SER A 1 3501 ? 119.494 98.768  40.578  1.00 35.12  ? 3501 SER A CB    1 
ATOM   14294 O  OG    . SER A 1 3501 ? 118.208 99.108  40.093  1.00 41.89  ? 3501 SER A OG    1 
ATOM   14295 N  N     . THR A 1 3502 ? 117.129 97.294  42.136  1.00 26.74  ? 3502 THR A N     1 
ATOM   14296 C  CA    . THR A 1 3502 ? 116.043 97.440  43.100  1.00 27.86  ? 3502 THR A CA    1 
ATOM   14297 C  C     . THR A 1 3502 ? 115.861 96.225  44.006  1.00 26.11  ? 3502 THR A C     1 
ATOM   14298 O  O     . THR A 1 3502 ? 115.047 96.289  44.938  1.00 22.41  ? 3502 THR A O     1 
ATOM   14299 C  CB    . THR A 1 3502 ? 114.727 97.731  42.374  1.00 28.68  ? 3502 THR A CB    1 
ATOM   14300 O  OG1   . THR A 1 3502 ? 114.530 96.767  41.333  1.00 33.88  ? 3502 THR A OG1   1 
ATOM   14301 C  CG2   . THR A 1 3502 ? 114.756 99.126  41.768  1.00 30.49  ? 3502 THR A CG2   1 
ATOM   14302 N  N     . ILE A 1 3503 ? 116.575 95.124  43.740  1.00 25.24  ? 3503 ILE A N     1 
ATOM   14303 C  CA    . ILE A 1 3503 ? 116.426 93.917  44.555  1.00 22.06  ? 3503 ILE A CA    1 
ATOM   14304 C  C     . ILE A 1 3503 ? 116.662 94.211  46.034  1.00 20.36  ? 3503 ILE A C     1 
ATOM   14305 O  O     . ILE A 1 3503 ? 115.888 93.772  46.894  1.00 17.06  ? 3503 ILE A O     1 
ATOM   14306 C  CB    . ILE A 1 3503 ? 117.366 92.805  44.050  1.00 26.42  ? 3503 ILE A CB    1 
ATOM   14307 C  CG1   . ILE A 1 3503 ? 116.770 92.098  42.833  1.00 27.77  ? 3503 ILE A CG1   1 
ATOM   14308 C  CG2   . ILE A 1 3503 ? 117.655 91.794  45.147  1.00 24.74  ? 3503 ILE A CG2   1 
ATOM   14309 C  CD1   . ILE A 1 3503 ? 117.665 91.025  42.256  1.00 34.40  ? 3503 ILE A CD1   1 
ATOM   14310 N  N     . ALA A 1 3504 ? 117.732 94.940  46.358  1.00 20.13  ? 3504 ALA A N     1 
ATOM   14311 C  CA    . ALA A 1 3504 ? 118.102 95.132  47.760  1.00 14.48  ? 3504 ALA A CA    1 
ATOM   14312 C  C     . ALA A 1 3504 ? 117.005 95.859  48.532  1.00 14.32  ? 3504 ALA A C     1 
ATOM   14313 O  O     . ALA A 1 3504 ? 116.556 95.393  49.588  1.00 15.58  ? 3504 ALA A O     1 
ATOM   14314 C  CB    . ALA A 1 3504 ? 119.423 95.894  47.853  1.00 16.94  ? 3504 ALA A CB    1 
ATOM   14315 N  N     . GLY A 1 3505 ? 116.549 96.998  48.008  1.00 13.48  ? 3505 GLY A N     1 
ATOM   14316 C  CA    . GLY A 1 3505 ? 115.507 97.747  48.689  1.00 10.90  ? 3505 GLY A CA    1 
ATOM   14317 C  C     . GLY A 1 3505 ? 114.184 97.007  48.735  1.00 9.26   ? 3505 GLY A C     1 
ATOM   14318 O  O     . GLY A 1 3505 ? 113.487 97.028  49.757  1.00 11.24  ? 3505 GLY A O     1 
ATOM   14319 N  N     . ASP A 1 3506 ? 113.815 96.346  47.633  1.00 10.22  ? 3506 ASP A N     1 
ATOM   14320 C  CA    . ASP A 1 3506 ? 112.557 95.608  47.609  1.00 12.93  ? 3506 ASP A CA    1 
ATOM   14321 C  C     . ASP A 1 3506 ? 112.561 94.498  48.651  1.00 9.79   ? 3506 ASP A C     1 
ATOM   14322 O  O     . ASP A 1 3506 ? 111.584 94.315  49.386  1.00 7.93   ? 3506 ASP A O     1 
ATOM   14323 C  CB    . ASP A 1 3506 ? 112.315 95.041  46.211  1.00 16.83  ? 3506 ASP A CB    1 
ATOM   14324 C  CG    . ASP A 1 3506 ? 111.852 96.096  45.227  1.00 27.55  ? 3506 ASP A CG    1 
ATOM   14325 O  OD1   . ASP A 1 3506 ? 111.896 95.832  44.007  1.00 31.86  ? 3506 ASP A OD1   1 
ATOM   14326 O  OD2   . ASP A 1 3506 ? 111.446 97.189  45.673  1.00 29.19  ? 3506 ASP A OD2   1 
ATOM   14327 N  N     . CYS A 1 3507 ? 113.668 93.757  48.739  1.00 8.77   ? 3507 CYS A N     1 
ATOM   14328 C  CA    . CYS A 1 3507 ? 113.767 92.682  49.718  1.00 8.08   ? 3507 CYS A CA    1 
ATOM   14329 C  C     . CYS A 1 3507 ? 113.779 93.225  51.139  1.00 7.87   ? 3507 CYS A C     1 
ATOM   14330 O  O     . CYS A 1 3507 ? 113.191 92.619  52.039  1.00 7.89   ? 3507 CYS A O     1 
ATOM   14331 C  CB    . CYS A 1 3507 ? 115.013 91.840  49.449  1.00 11.28  ? 3507 CYS A CB    1 
ATOM   14332 S  SG    . CYS A 1 3507 ? 114.907 90.839  47.950  1.00 16.65  ? 3507 CYS A SG    1 
ATOM   14333 N  N     . LEU A 1 3508 ? 114.441 94.363  51.366  1.00 6.41   ? 3508 LEU A N     1 
ATOM   14334 C  CA    . LEU A 1 3508 ? 114.438 94.952  52.702  1.00 5.28   ? 3508 LEU A CA    1 
ATOM   14335 C  C     . LEU A 1 3508 ? 113.020 95.314  53.133  1.00 5.85   ? 3508 LEU A C     1 
ATOM   14336 O  O     . LEU A 1 3508 ? 112.588 94.974  54.243  1.00 4.30   ? 3508 LEU A O     1 
ATOM   14337 C  CB    . LEU A 1 3508 ? 115.356 96.177  52.733  1.00 7.11   ? 3508 LEU A CB    1 
ATOM   14338 C  CG    . LEU A 1 3508 ? 115.680 96.843  54.076  1.00 5.43   ? 3508 LEU A CG    1 
ATOM   14339 C  CD1   . LEU A 1 3508 ? 117.037 97.520  53.995  1.00 8.35   ? 3508 LEU A CD1   1 
ATOM   14340 C  CD2   . LEU A 1 3508 ? 114.618 97.853  54.486  1.00 5.05   ? 3508 LEU A CD2   1 
ATOM   14341 N  N     . LEU A 1 3509 ? 112.273 95.991  52.255  1.00 5.38   ? 3509 LEU A N     1 
ATOM   14342 C  CA    . LEU A 1 3509 ? 110.900 96.363  52.589  1.00 5.52   ? 3509 LEU A CA    1 
ATOM   14343 C  C     . LEU A 1 3509 ? 110.025 95.132  52.796  1.00 4.99   ? 3509 LEU A C     1 
ATOM   14344 O  O     . LEU A 1 3509 ? 109.218 95.082  53.735  1.00 4.37   ? 3509 LEU A O     1 
ATOM   14345 C  CB    . LEU A 1 3509 ? 110.313 97.253  51.494  1.00 6.40   ? 3509 LEU A CB    1 
ATOM   14346 C  CG    . LEU A 1 3509 ? 110.964 98.619  51.294  1.00 7.92   ? 3509 LEU A CG    1 
ATOM   14347 C  CD1   . LEU A 1 3509 ? 110.394 99.307  50.066  1.00 7.44   ? 3509 LEU A CD1   1 
ATOM   14348 C  CD2   . LEU A 1 3509 ? 110.774 99.482  52.529  1.00 7.47   ? 3509 LEU A CD2   1 
ATOM   14349 N  N     . SER A 1 3510 ? 110.168 94.129  51.926  1.00 5.57   ? 3510 SER A N     1 
ATOM   14350 C  CA    . SER A 1 3510 ? 109.359 92.923  52.045  1.00 4.79   ? 3510 SER A CA    1 
ATOM   14351 C  C     . SER A 1 3510 ? 109.646 92.192  53.349  1.00 5.46   ? 3510 SER A C     1 
ATOM   14352 O  O     . SER A 1 3510 ? 108.719 91.747  54.036  1.00 5.46   ? 3510 SER A O     1 
ATOM   14353 C  CB    . SER A 1 3510 ? 109.614 92.011  50.846  1.00 6.92   ? 3510 SER A CB    1 
ATOM   14354 O  OG    . SER A 1 3510 ? 109.382 92.700  49.632  1.00 9.08   ? 3510 SER A OG    1 
ATOM   14355 N  N     . ALA A 1 3511 ? 110.924 92.065  53.710  1.00 5.65   ? 3511 ALA A N     1 
ATOM   14356 C  CA    . ALA A 1 3511 ? 111.284 91.408  54.960  1.00 3.35   ? 3511 ALA A CA    1 
ATOM   14357 C  C     . ALA A 1 3511 ? 110.764 92.183  56.160  1.00 3.54   ? 3511 ALA A C     1 
ATOM   14358 O  O     . ALA A 1 3511 ? 110.299 91.586  57.137  1.00 4.21   ? 3511 ALA A O     1 
ATOM   14359 C  CB    . ALA A 1 3511 ? 112.798 91.241  55.047  1.00 3.46   ? 3511 ALA A CB    1 
ATOM   14360 N  N     . ALA A 1 3512 ? 110.848 93.515  56.117  1.00 3.66   ? 3512 ALA A N     1 
ATOM   14361 C  CA    . ALA A 1 3512 ? 110.311 94.310  57.215  1.00 2.59   ? 3512 ALA A CA    1 
ATOM   14362 C  C     . ALA A 1 3512 ? 108.814 94.079  57.373  1.00 3.22   ? 3512 ALA A C     1 
ATOM   14363 O  O     . ALA A 1 3512 ? 108.318 93.903  58.495  1.00 3.20   ? 3512 ALA A O     1 
ATOM   14364 C  CB    . ALA A 1 3512 ? 110.611 95.789  56.983  1.00 2.51   ? 3512 ALA A CB    1 
ATOM   14365 N  N     . PHE A 1 3513 ? 108.081 94.056  56.257  1.00 3.65   ? 3513 PHE A N     1 
ATOM   14366 C  CA    . PHE A 1 3513 ? 106.644 93.809  56.326  1.00 3.72   ? 3513 PHE A CA    1 
ATOM   14367 C  C     . PHE A 1 3513 ? 106.345 92.418  56.876  1.00 3.69   ? 3513 PHE A C     1 
ATOM   14368 O  O     . PHE A 1 3513 ? 105.431 92.249  57.690  1.00 4.13   ? 3513 PHE A O     1 
ATOM   14369 C  CB    . PHE A 1 3513 ? 106.009 93.990  54.948  1.00 3.33   ? 3513 PHE A CB    1 
ATOM   14370 C  CG    . PHE A 1 3513 ? 104.518 94.157  54.990  1.00 5.05   ? 3513 PHE A CG    1 
ATOM   14371 C  CD1   . PHE A 1 3513 ? 103.953 95.412  55.143  1.00 5.33   ? 3513 PHE A CD1   1 
ATOM   14372 C  CD2   . PHE A 1 3513 ? 103.681 93.061  54.877  1.00 5.68   ? 3513 PHE A CD2   1 
ATOM   14373 C  CE1   . PHE A 1 3513 ? 102.582 95.568  55.185  1.00 7.65   ? 3513 PHE A CE1   1 
ATOM   14374 C  CE2   . PHE A 1 3513 ? 102.310 93.211  54.917  1.00 8.79   ? 3513 PHE A CE2   1 
ATOM   14375 C  CZ    . PHE A 1 3513 ? 101.760 94.467  55.071  1.00 9.10   ? 3513 PHE A CZ    1 
ATOM   14376 N  N     . ILE A 1 3514 ? 107.103 91.411  56.438  1.00 3.55   ? 3514 ILE A N     1 
ATOM   14377 C  CA    . ILE A 1 3514 ? 106.894 90.051  56.932  1.00 3.97   ? 3514 ILE A CA    1 
ATOM   14378 C  C     . ILE A 1 3514 ? 107.149 89.969  58.432  1.00 4.90   ? 3514 ILE A C     1 
ATOM   14379 O  O     . ILE A 1 3514 ? 106.378 89.347  59.173  1.00 6.63   ? 3514 ILE A O     1 
ATOM   14380 C  CB    . ILE A 1 3514 ? 107.773 89.056  56.152  1.00 6.99   ? 3514 ILE A CB    1 
ATOM   14381 C  CG1   . ILE A 1 3514 ? 107.399 89.059  54.671  1.00 9.49   ? 3514 ILE A CG1   1 
ATOM   14382 C  CG2   . ILE A 1 3514 ? 107.661 87.671  56.736  1.00 7.88   ? 3514 ILE A CG2   1 
ATOM   14383 C  CD1   . ILE A 1 3514 ? 105.954 88.694  54.423  1.00 9.59   ? 3514 ILE A CD1   1 
ATOM   14384 N  N     . ALA A 1 3515 ? 108.228 90.592  58.905  1.00 3.61   ? 3515 ALA A N     1 
ATOM   14385 C  CA    . ALA A 1 3515 ? 108.585 90.467  60.313  1.00 3.16   ? 3515 ALA A CA    1 
ATOM   14386 C  C     . ALA A 1 3515 ? 107.641 91.242  61.220  1.00 3.15   ? 3515 ALA A C     1 
ATOM   14387 O  O     . ALA A 1 3515 ? 107.260 90.746  62.286  1.00 2.97   ? 3515 ALA A O     1 
ATOM   14388 C  CB    . ALA A 1 3515 ? 110.020 90.940  60.543  1.00 2.89   ? 3515 ALA A CB    1 
ATOM   14389 N  N     . TYR A 1 3516 ? 107.250 92.453  60.827  1.00 3.09   ? 3516 TYR A N     1 
ATOM   14390 C  CA    . TYR A 1 3516 ? 106.683 93.389  61.787  1.00 3.90   ? 3516 TYR A CA    1 
ATOM   14391 C  C     . TYR A 1 3516 ? 105.201 93.675  61.602  1.00 4.08   ? 3516 TYR A C     1 
ATOM   14392 O  O     . TYR A 1 3516 ? 104.534 94.027  62.576  1.00 8.29   ? 3516 TYR A O     1 
ATOM   14393 C  CB    . TYR A 1 3516 ? 107.444 94.717  61.728  1.00 3.06   ? 3516 TYR A CB    1 
ATOM   14394 C  CG    . TYR A 1 3516 ? 108.902 94.608  62.111  1.00 2.70   ? 3516 TYR A CG    1 
ATOM   14395 C  CD1   . TYR A 1 3516 ? 109.285 94.404  63.429  1.00 2.22   ? 3516 TYR A CD1   1 
ATOM   14396 C  CD2   . TYR A 1 3516 ? 109.898 94.733  61.152  1.00 2.82   ? 3516 TYR A CD2   1 
ATOM   14397 C  CE1   . TYR A 1 3516 ? 110.617 94.315  63.778  1.00 2.58   ? 3516 TYR A CE1   1 
ATOM   14398 C  CE2   . TYR A 1 3516 ? 111.232 94.645  61.493  1.00 2.95   ? 3516 TYR A CE2   1 
ATOM   14399 C  CZ    . TYR A 1 3516 ? 111.586 94.436  62.807  1.00 2.80   ? 3516 TYR A CZ    1 
ATOM   14400 O  OH    . TYR A 1 3516 ? 112.914 94.348  63.151  1.00 2.83   ? 3516 TYR A OH    1 
ATOM   14401 N  N     . ALA A 1 3517 ? 104.668 93.535  60.391  1.00 3.66   ? 3517 ALA A N     1 
ATOM   14402 C  CA    . ALA A 1 3517 ? 103.342 94.055  60.079  1.00 5.22   ? 3517 ALA A CA    1 
ATOM   14403 C  C     . ALA A 1 3517 ? 102.207 93.083  60.382  1.00 5.12   ? 3517 ALA A C     1 
ATOM   14404 O  O     . ALA A 1 3517 ? 101.047 93.427  60.133  1.00 8.54   ? 3517 ALA A O     1 
ATOM   14405 C  CB    . ALA A 1 3517 ? 103.278 94.467  58.606  1.00 3.98   ? 3517 ALA A CB    1 
ATOM   14406 N  N     . GLY A 1 3518 ? 102.501 91.892  60.905  1.00 5.13   ? 3518 GLY A N     1 
ATOM   14407 C  CA    . GLY A 1 3518 ? 101.463 90.881  61.042  1.00 4.38   ? 3518 GLY A CA    1 
ATOM   14408 C  C     . GLY A 1 3518 ? 100.355 91.266  62.006  1.00 5.29   ? 3518 GLY A C     1 
ATOM   14409 O  O     . GLY A 1 3518 ? 99.172  91.085  61.707  1.00 6.24   ? 3518 GLY A O     1 
ATOM   14410 N  N     . TYR A 1 3519 ? 100.718 91.801  63.174  1.00 6.55   ? 3519 TYR A N     1 
ATOM   14411 C  CA    . TYR A 1 3519 ? 99.715  92.077  64.200  1.00 6.75   ? 3519 TYR A CA    1 
ATOM   14412 C  C     . TYR A 1 3519 ? 98.822  93.257  63.837  1.00 6.87   ? 3519 TYR A C     1 
ATOM   14413 O  O     . TYR A 1 3519 ? 97.649  93.284  64.224  1.00 7.73   ? 3519 TYR A O     1 
ATOM   14414 C  CB    . TYR A 1 3519 ? 100.391 92.333  65.547  1.00 10.72  ? 3519 TYR A CB    1 
ATOM   14415 C  CG    . TYR A 1 3519 ? 99.412  92.581  66.671  1.00 12.35  ? 3519 TYR A CG    1 
ATOM   14416 C  CD1   . TYR A 1 3519 ? 98.633  91.552  67.182  1.00 10.96  ? 3519 TYR A CD1   1 
ATOM   14417 C  CD2   . TYR A 1 3519 ? 99.256  93.851  67.213  1.00 12.62  ? 3519 TYR A CD2   1 
ATOM   14418 C  CE1   . TYR A 1 3519 ? 97.733  91.778  68.205  1.00 16.51  ? 3519 TYR A CE1   1 
ATOM   14419 C  CE2   . TYR A 1 3519 ? 98.359  94.085  68.237  1.00 17.76  ? 3519 TYR A CE2   1 
ATOM   14420 C  CZ    . TYR A 1 3519 ? 97.600  93.046  68.728  1.00 20.87  ? 3519 TYR A CZ    1 
ATOM   14421 O  OH    . TYR A 1 3519 ? 96.705  93.274  69.747  1.00 30.88  ? 3519 TYR A OH    1 
ATOM   14422 N  N     . PHE A 1 3520 ? 99.347  94.231  63.103  1.00 7.53   ? 3520 PHE A N     1 
ATOM   14423 C  CA    . PHE A 1 3520 ? 98.632  95.476  62.878  1.00 9.04   ? 3520 PHE A CA    1 
ATOM   14424 C  C     . PHE A 1 3520 ? 97.583  95.324  61.778  1.00 9.81   ? 3520 PHE A C     1 
ATOM   14425 O  O     . PHE A 1 3520 ? 97.596  94.374  60.991  1.00 8.64   ? 3520 PHE A O     1 
ATOM   14426 C  CB    . PHE A 1 3520 ? 99.614  96.589  62.523  1.00 8.15   ? 3520 PHE A CB    1 
ATOM   14427 C  CG    . PHE A 1 3520 ? 100.716 96.761  63.528  1.00 12.41  ? 3520 PHE A CG    1 
ATOM   14428 C  CD1   . PHE A 1 3520 ? 100.484 97.422  64.723  1.00 11.43  ? 3520 PHE A CD1   1 
ATOM   14429 C  CD2   . PHE A 1 3520 ? 101.978 96.246  63.288  1.00 8.69   ? 3520 PHE A CD2   1 
ATOM   14430 C  CE1   . PHE A 1 3520 ? 101.494 97.578  65.650  1.00 12.83  ? 3520 PHE A CE1   1 
ATOM   14431 C  CE2   . PHE A 1 3520 ? 102.990 96.398  64.211  1.00 11.38  ? 3520 PHE A CE2   1 
ATOM   14432 C  CZ    . PHE A 1 3520 ? 102.748 97.064  65.393  1.00 14.13  ? 3520 PHE A CZ    1 
ATOM   14433 N  N     . ASP A 1 3521 ? 96.662  96.286  61.739  1.00 11.77  ? 3521 ASP A N     1 
ATOM   14434 C  CA    . ASP A 1 3521 ? 95.603  96.312  60.744  1.00 10.40  ? 3521 ASP A CA    1 
ATOM   14435 C  C     . ASP A 1 3521 ? 96.098  96.977  59.459  1.00 10.04  ? 3521 ASP A C     1 
ATOM   14436 O  O     . ASP A 1 3521 ? 97.265  97.350  59.332  1.00 11.59  ? 3521 ASP A O     1 
ATOM   14437 C  CB    . ASP A 1 3521 ? 94.362  97.010  61.304  1.00 9.97   ? 3521 ASP A CB    1 
ATOM   14438 C  CG    . ASP A 1 3521 ? 94.636  98.438  61.754  1.00 21.25  ? 3521 ASP A CG    1 
ATOM   14439 O  OD1   . ASP A 1 3521 ? 95.767  98.933  61.566  1.00 23.90  ? 3521 ASP A OD1   1 
ATOM   14440 O  OD2   . ASP A 1 3521 ? 93.709  99.070  62.302  1.00 24.60  ? 3521 ASP A OD2   1 
ATOM   14441 N  N     . GLN A 1 3522 ? 95.187  97.138  58.496  1.00 10.47  ? 3522 GLN A N     1 
ATOM   14442 C  CA    . GLN A 1 3522 ? 95.569  97.611  57.167  1.00 11.20  ? 3522 GLN A CA    1 
ATOM   14443 C  C     . GLN A 1 3522 ? 96.186  99.005  57.221  1.00 12.89  ? 3522 GLN A C     1 
ATOM   14444 O  O     . GLN A 1 3522 ? 97.222  99.264  56.595  1.00 13.17  ? 3522 GLN A O     1 
ATOM   14445 C  CB    . GLN A 1 3522 ? 94.349  97.599  56.246  1.00 10.61  ? 3522 GLN A CB    1 
ATOM   14446 C  CG    . GLN A 1 3522 ? 94.540  98.350  54.939  1.00 17.97  ? 3522 GLN A CG    1 
ATOM   14447 C  CD    . GLN A 1 3522 ? 93.461  98.031  53.923  1.00 23.01  ? 3522 GLN A CD    1 
ATOM   14448 O  OE1   . GLN A 1 3522 ? 92.345  97.656  54.283  1.00 25.64  ? 3522 GLN A OE1   1 
ATOM   14449 N  NE2   . GLN A 1 3522 ? 93.790  98.171  52.645  1.00 27.33  ? 3522 GLN A NE2   1 
ATOM   14450 N  N     . GLN A 1 3523 ? 95.558  99.917  57.967  1.00 12.23  ? 3523 GLN A N     1 
ATOM   14451 C  CA    . GLN A 1 3523 ? 96.042  101.294 58.022  1.00 13.81  ? 3523 GLN A CA    1 
ATOM   14452 C  C     . GLN A 1 3523 ? 97.446  101.366 58.608  1.00 12.77  ? 3523 GLN A C     1 
ATOM   14453 O  O     . GLN A 1 3523 ? 98.317  102.061 58.071  1.00 13.40  ? 3523 GLN A O     1 
ATOM   14454 C  CB    . GLN A 1 3523 ? 95.071  102.154 58.832  1.00 16.66  ? 3523 GLN A CB    1 
ATOM   14455 C  CG    . GLN A 1 3523 ? 95.408  103.647 58.919  1.00 16.85  ? 3523 GLN A CG    1 
ATOM   14456 C  CD    . GLN A 1 3523 ? 95.678  104.297 57.570  1.00 34.87  ? 3523 GLN A CD    1 
ATOM   14457 O  OE1   . GLN A 1 3523 ? 96.780  104.194 57.032  1.00 35.24  ? 3523 GLN A OE1   1 
ATOM   14458 N  NE2   . GLN A 1 3523 ? 94.657  104.926 56.994  1.00 35.59  ? 3523 GLN A NE2   1 
ATOM   14459 N  N     . MET A 1 3524 ? 97.692  100.641 59.700  1.00 12.53  ? 3524 MET A N     1 
ATOM   14460 C  CA    . MET A 1 3524 ? 99.007  100.689 60.330  1.00 11.90  ? 3524 MET A CA    1 
ATOM   14461 C  C     . MET A 1 3524 ? 100.057 99.977  59.482  1.00 10.29  ? 3524 MET A C     1 
ATOM   14462 O  O     . MET A 1 3524 ? 101.220 100.396 59.446  1.00 12.77  ? 3524 MET A O     1 
ATOM   14463 C  CB    . MET A 1 3524 ? 98.937  100.091 61.733  1.00 13.95  ? 3524 MET A CB    1 
ATOM   14464 C  CG    . MET A 1 3524 ? 100.249 100.159 62.478  1.00 18.50  ? 3524 MET A CG    1 
ATOM   14465 S  SD    . MET A 1 3524 ? 100.571 101.834 63.048  1.00 36.65  ? 3524 MET A SD    1 
ATOM   14466 C  CE    . MET A 1 3524 ? 102.011 102.243 62.074  1.00 18.68  ? 3524 MET A CE    1 
ATOM   14467 N  N     . ARG A 1 3525 ? 99.668  98.902  58.792  1.00 8.62   ? 3525 ARG A N     1 
ATOM   14468 C  CA    . ARG A 1 3525 ? 100.590 98.238  57.874  1.00 9.81   ? 3525 ARG A CA    1 
ATOM   14469 C  C     . ARG A 1 3525 ? 101.020 99.188  56.765  1.00 10.60  ? 3525 ARG A C     1 
ATOM   14470 O  O     . ARG A 1 3525 ? 102.213 99.296  56.444  1.00 12.05  ? 3525 ARG A O     1 
ATOM   14471 C  CB    . ARG A 1 3525 ? 99.933  96.986  57.291  1.00 8.28   ? 3525 ARG A CB    1 
ATOM   14472 C  CG    . ARG A 1 3525 ? 99.746  95.858  58.294  1.00 6.45   ? 3525 ARG A CG    1 
ATOM   14473 C  CD    . ARG A 1 3525 ? 99.206  94.596  57.647  1.00 6.41   ? 3525 ARG A CD    1 
ATOM   14474 N  NE    . ARG A 1 3525 ? 98.992  93.545  58.634  1.00 6.60   ? 3525 ARG A NE    1 
ATOM   14475 C  CZ    . ARG A 1 3525 ? 98.565  92.323  58.351  1.00 5.57   ? 3525 ARG A CZ    1 
ATOM   14476 N  NH1   . ARG A 1 3525 ? 98.301  91.952  57.109  1.00 6.10   ? 3525 ARG A NH1   1 
ATOM   14477 N  NH2   . ARG A 1 3525 ? 98.398  91.449  59.339  1.00 5.38   ? 3525 ARG A NH2   1 
ATOM   14478 N  N     . GLN A 1 3526 ? 100.055 99.902  56.180  1.00 10.60  ? 3526 GLN A N     1 
ATOM   14479 C  CA    . GLN A 1 3526 ? 100.381 100.877 55.148  1.00 11.06  ? 3526 GLN A CA    1 
ATOM   14480 C  C     . GLN A 1 3526 ? 101.254 101.993 55.705  1.00 11.85  ? 3526 GLN A C     1 
ATOM   14481 O  O     . GLN A 1 3526 ? 102.191 102.445 55.040  1.00 10.88  ? 3526 GLN A O     1 
ATOM   14482 C  CB    . GLN A 1 3526 ? 99.101  101.448 54.538  1.00 14.87  ? 3526 GLN A CB    1 
ATOM   14483 C  CG    . GLN A 1 3526 ? 99.340  102.349 53.341  1.00 14.53  ? 3526 GLN A CG    1 
ATOM   14484 C  CD    . GLN A 1 3526 ? 100.257 101.717 52.314  1.00 16.53  ? 3526 GLN A CD    1 
ATOM   14485 O  OE1   . GLN A 1 3526 ? 99.996  100.619 51.824  1.00 21.41  ? 3526 GLN A OE1   1 
ATOM   14486 N  NE2   . GLN A 1 3526 ? 101.341 102.408 51.983  1.00 15.61  ? 3526 GLN A NE2   1 
ATOM   14487 N  N     . ASN A 1 3527 ? 100.961 102.452 56.926  1.00 11.35  ? 3527 ASN A N     1 
ATOM   14488 C  CA    . ASN A 1 3527 ? 101.759 103.514 57.532  1.00 10.59  ? 3527 ASN A CA    1 
ATOM   14489 C  C     . ASN A 1 3527 ? 103.207 103.081 57.734  1.00 11.29  ? 3527 ASN A C     1 
ATOM   14490 O  O     . ASN A 1 3527 ? 104.137 103.827 57.401  1.00 12.23  ? 3527 ASN A O     1 
ATOM   14491 C  CB    . ASN A 1 3527 ? 101.139 103.939 58.863  1.00 17.04  ? 3527 ASN A CB    1 
ATOM   14492 C  CG    . ASN A 1 3527 ? 100.033 104.961 58.691  1.00 26.78  ? 3527 ASN A CG    1 
ATOM   14493 O  OD1   . ASN A 1 3527 ? 100.257 106.054 58.172  1.00 42.50  ? 3527 ASN A OD1   1 
ATOM   14494 N  ND2   . ASN A 1 3527 ? 98.830  104.609 59.127  1.00 19.98  ? 3527 ASN A ND2   1 
ATOM   14495 N  N     . LEU A 1 3528 ? 103.418 101.880 58.281  1.00 8.16   ? 3528 LEU A N     1 
ATOM   14496 C  CA    . LEU A 1 3528 ? 104.778 101.389 58.487  1.00 7.01   ? 3528 LEU A CA    1 
ATOM   14497 C  C     . LEU A 1 3528 ? 105.510 101.212 57.164  1.00 6.14   ? 3528 LEU A C     1 
ATOM   14498 O  O     . LEU A 1 3528 ? 106.687 101.579 57.044  1.00 6.32   ? 3528 LEU A O     1 
ATOM   14499 C  CB    . LEU A 1 3528 ? 104.763 100.070 59.261  1.00 7.31   ? 3528 LEU A CB    1 
ATOM   14500 C  CG    . LEU A 1 3528 ? 104.467 100.108 60.761  1.00 6.20   ? 3528 LEU A CG    1 
ATOM   14501 C  CD1   . LEU A 1 3528 ? 104.165 98.722  61.287  1.00 7.15   ? 3528 LEU A CD1   1 
ATOM   14502 C  CD2   . LEU A 1 3528 ? 105.629 100.711 61.523  1.00 5.37   ? 3528 LEU A CD2   1 
ATOM   14503 N  N     . PHE A 1 3529 ? 104.836 100.647 56.158  1.00 6.43   ? 3529 PHE A N     1 
ATOM   14504 C  CA    . PHE A 1 3529 ? 105.498 100.450 54.873  1.00 6.71   ? 3529 PHE A CA    1 
ATOM   14505 C  C     . PHE A 1 3529 ? 105.843 101.783 54.221  1.00 8.82   ? 3529 PHE A C     1 
ATOM   14506 O  O     . PHE A 1 3529 ? 106.917 101.930 53.626  1.00 10.11  ? 3529 PHE A O     1 
ATOM   14507 C  CB    . PHE A 1 3529 ? 104.627 99.599  53.951  1.00 6.28   ? 3529 PHE A CB    1 
ATOM   14508 C  CG    . PHE A 1 3529 ? 105.396 98.934  52.847  1.00 7.48   ? 3529 PHE A CG    1 
ATOM   14509 C  CD1   . PHE A 1 3529 ? 105.561 99.560  51.624  1.00 5.49   ? 3529 PHE A CD1   1 
ATOM   14510 C  CD2   . PHE A 1 3529 ? 105.979 97.693  53.044  1.00 5.82   ? 3529 PHE A CD2   1 
ATOM   14511 C  CE1   . PHE A 1 3529 ? 106.276 98.951  50.610  1.00 5.70   ? 3529 PHE A CE1   1 
ATOM   14512 C  CE2   . PHE A 1 3529 ? 106.697 97.081  52.036  1.00 5.15   ? 3529 PHE A CE2   1 
ATOM   14513 C  CZ    . PHE A 1 3529 ? 106.843 97.710  50.817  1.00 7.59   ? 3529 PHE A CZ    1 
ATOM   14514 N  N     . THR A 1 3530 ? 104.951 102.770 54.331  1.00 9.32   ? 3530 THR A N     1 
ATOM   14515 C  CA    . THR A 1 3530 ? 105.234 104.095 53.790  1.00 10.66  ? 3530 THR A CA    1 
ATOM   14516 C  C     . THR A 1 3530 ? 106.406 104.747 54.512  1.00 10.66  ? 3530 THR A C     1 
ATOM   14517 O  O     . THR A 1 3530 ? 107.255 105.382 53.878  1.00 12.40  ? 3530 THR A O     1 
ATOM   14518 C  CB    . THR A 1 3530 ? 103.986 104.975 53.880  1.00 14.32  ? 3530 THR A CB    1 
ATOM   14519 O  OG1   . THR A 1 3530 ? 102.924 104.378 53.126  1.00 15.33  ? 3530 THR A OG1   1 
ATOM   14520 C  CG2   . THR A 1 3530 ? 104.267 106.363 53.327  1.00 20.95  ? 3530 THR A CG2   1 
ATOM   14521 N  N     . THR A 1 3531 ? 106.469 104.602 55.838  1.00 9.19   ? 3531 THR A N     1 
ATOM   14522 C  CA    . THR A 1 3531 ? 107.591 105.152 56.593  1.00 7.72   ? 3531 THR A CA    1 
ATOM   14523 C  C     . THR A 1 3531 ? 108.909 104.516 56.162  1.00 9.75   ? 3531 THR A C     1 
ATOM   14524 O  O     . THR A 1 3531 ? 109.910 105.213 55.946  1.00 12.92  ? 3531 THR A O     1 
ATOM   14525 C  CB    . THR A 1 3531 ? 107.359 104.948 58.091  1.00 8.38   ? 3531 THR A CB    1 
ATOM   14526 O  OG1   . THR A 1 3531 ? 106.081 105.485 58.456  1.00 14.32  ? 3531 THR A OG1   1 
ATOM   14527 C  CG2   . THR A 1 3531 ? 108.445 105.636 58.903  1.00 8.65   ? 3531 THR A CG2   1 
ATOM   14528 N  N     . TRP A 1 3532 ? 108.923 103.187 56.021  1.00 8.11   ? 3532 TRP A N     1 
ATOM   14529 C  CA    . TRP A 1 3532 ? 110.144 102.506 55.597  1.00 6.47   ? 3532 TRP A CA    1 
ATOM   14530 C  C     . TRP A 1 3532 ? 110.546 102.917 54.185  1.00 8.18   ? 3532 TRP A C     1 
ATOM   14531 O  O     . TRP A 1 3532 ? 111.732 103.134 53.906  1.00 11.11  ? 3532 TRP A O     1 
ATOM   14532 C  CB    . TRP A 1 3532 ? 109.964 100.990 55.683  1.00 5.57   ? 3532 TRP A CB    1 
ATOM   14533 C  CG    . TRP A 1 3532 ? 109.514 100.497 57.023  1.00 3.86   ? 3532 TRP A CG    1 
ATOM   14534 C  CD1   . TRP A 1 3532 ? 109.772 101.065 58.236  1.00 4.05   ? 3532 TRP A CD1   1 
ATOM   14535 C  CD2   . TRP A 1 3532 ? 108.731 99.328  57.286  1.00 3.24   ? 3532 TRP A CD2   1 
ATOM   14536 N  NE1   . TRP A 1 3532 ? 109.195 100.324 59.238  1.00 4.04   ? 3532 TRP A NE1   1 
ATOM   14537 C  CE2   . TRP A 1 3532 ? 108.549 99.252  58.680  1.00 3.47   ? 3532 TRP A CE2   1 
ATOM   14538 C  CE3   . TRP A 1 3532 ? 108.161 98.340  56.477  1.00 3.26   ? 3532 TRP A CE3   1 
ATOM   14539 C  CZ2   . TRP A 1 3532 ? 107.825 98.227  59.284  1.00 3.56   ? 3532 TRP A CZ2   1 
ATOM   14540 C  CZ3   . TRP A 1 3532 ? 107.443 97.324  57.078  1.00 3.46   ? 3532 TRP A CZ3   1 
ATOM   14541 C  CH2   . TRP A 1 3532 ? 107.281 97.274  58.467  1.00 3.68   ? 3532 TRP A CH2   1 
ATOM   14542 N  N     . SER A 1 3533 ? 109.571 103.026 53.278  1.00 10.51  ? 3533 SER A N     1 
ATOM   14543 C  CA    . SER A 1 3533 ? 109.873 103.434 51.910  1.00 11.80  ? 3533 SER A CA    1 
ATOM   14544 C  C     . SER A 1 3533 ? 110.418 104.854 51.866  1.00 14.74  ? 3533 SER A C     1 
ATOM   14545 O  O     . SER A 1 3533 ? 111.370 105.139 51.131  1.00 14.60  ? 3533 SER A O     1 
ATOM   14546 C  CB    . SER A 1 3533 ? 108.624 103.310 51.039  1.00 9.08   ? 3533 SER A CB    1 
ATOM   14547 O  OG    . SER A 1 3533 ? 108.184 101.965 50.968  1.00 15.76  ? 3533 SER A OG    1 
ATOM   14548 N  N     . HIS A 1 3534 ? 109.831 105.760 52.652  1.00 12.94  ? 3534 HIS A N     1 
ATOM   14549 C  CA    . HIS A 1 3534 ? 110.339 107.125 52.711  1.00 14.18  ? 3534 HIS A CA    1 
ATOM   14550 C  C     . HIS A 1 3534 ? 111.765 107.156 53.239  1.00 14.56  ? 3534 HIS A C     1 
ATOM   14551 O  O     . HIS A 1 3534 ? 112.617 107.876 52.703  1.00 18.36  ? 3534 HIS A O     1 
ATOM   14552 C  CB    . HIS A 1 3534 ? 109.426 107.990 53.579  1.00 14.98  ? 3534 HIS A CB    1 
ATOM   14553 C  CG    . HIS A 1 3534 ? 108.156 108.397 52.901  1.00 27.54  ? 3534 HIS A CG    1 
ATOM   14554 N  ND1   . HIS A 1 3534 ? 107.112 108.996 53.573  1.00 30.37  ? 3534 HIS A ND1   1 
ATOM   14555 C  CD2   . HIS A 1 3534 ? 107.761 108.292 51.610  1.00 27.56  ? 3534 HIS A CD2   1 
ATOM   14556 C  CE1   . HIS A 1 3534 ? 106.130 109.243 52.725  1.00 27.77  ? 3534 HIS A CE1   1 
ATOM   14557 N  NE2   . HIS A 1 3534 ? 106.497 108.824 51.528  1.00 31.88  ? 3534 HIS A NE2   1 
ATOM   14558 N  N     . HIS A 1 3535 ? 112.050 106.373 54.283  1.00 14.94  ? 3535 HIS A N     1 
ATOM   14559 C  CA    . HIS A 1 3535 ? 113.410 106.332 54.811  1.00 12.19  ? 3535 HIS A CA    1 
ATOM   14560 C  C     . HIS A 1 3535 ? 114.390 105.805 53.771  1.00 12.78  ? 3535 HIS A C     1 
ATOM   14561 O  O     . HIS A 1 3535 ? 115.506 106.323 53.644  1.00 17.07  ? 3535 HIS A O     1 
ATOM   14562 C  CB    . HIS A 1 3535 ? 113.467 105.477 56.072  1.00 9.58   ? 3535 HIS A CB    1 
ATOM   14563 C  CG    . HIS A 1 3535 ? 114.802 105.498 56.747  1.00 10.78  ? 3535 HIS A CG    1 
ATOM   14564 N  ND1   . HIS A 1 3535 ? 115.127 106.414 57.725  1.00 13.52  ? 3535 HIS A ND1   1 
ATOM   14565 C  CD2   . HIS A 1 3535 ? 115.892 104.710 56.593  1.00 9.84   ? 3535 HIS A CD2   1 
ATOM   14566 C  CE1   . HIS A 1 3535 ? 116.361 106.191 58.141  1.00 16.57  ? 3535 HIS A CE1   1 
ATOM   14567 N  NE2   . HIS A 1 3535 ? 116.848 105.164 57.469  1.00 12.82  ? 3535 HIS A NE2   1 
ATOM   14568 N  N     . LEU A 1 3536 ? 113.998 104.768 53.027  1.00 10.91  ? 3536 LEU A N     1 
ATOM   14569 C  CA    . LEU A 1 3536 ? 114.856 104.279 51.951  1.00 12.37  ? 3536 LEU A CA    1 
ATOM   14570 C  C     . LEU A 1 3536 ? 115.068 105.350 50.889  1.00 14.83  ? 3536 LEU A C     1 
ATOM   14571 O  O     . LEU A 1 3536 ? 116.152 105.447 50.302  1.00 16.84  ? 3536 LEU A O     1 
ATOM   14572 C  CB    . LEU A 1 3536 ? 114.264 103.017 51.326  1.00 12.93  ? 3536 LEU A CB    1 
ATOM   14573 C  CG    . LEU A 1 3536 ? 114.266 101.751 52.182  1.00 12.26  ? 3536 LEU A CG    1 
ATOM   14574 C  CD1   . LEU A 1 3536 ? 114.042 100.531 51.310  1.00 11.04  ? 3536 LEU A CD1   1 
ATOM   14575 C  CD2   . LEU A 1 3536 ? 115.565 101.625 52.957  1.00 12.14  ? 3536 LEU A CD2   1 
ATOM   14576 N  N     . GLN A 1 3537 ? 114.038 106.156 50.622  1.00 15.36  ? 3537 GLN A N     1 
ATOM   14577 C  CA    . GLN A 1 3537 ? 114.186 107.257 49.675  1.00 17.59  ? 3537 GLN A CA    1 
ATOM   14578 C  C     . GLN A 1 3537 ? 115.208 108.277 50.166  1.00 19.34  ? 3537 GLN A C     1 
ATOM   14579 O  O     . GLN A 1 3537 ? 116.047 108.746 49.388  1.00 19.26  ? 3537 GLN A O     1 
ATOM   14580 C  CB    . GLN A 1 3537 ? 112.835 107.928 49.430  1.00 19.87  ? 3537 GLN A CB    1 
ATOM   14581 C  CG    . GLN A 1 3537 ? 111.840 107.067 48.676  1.00 24.34  ? 3537 GLN A CG    1 
ATOM   14582 C  CD    . GLN A 1 3537 ? 110.502 107.753 48.484  1.00 30.23  ? 3537 GLN A CD    1 
ATOM   14583 O  OE1   . GLN A 1 3537 ? 110.281 108.857 48.982  1.00 29.55  ? 3537 GLN A OE1   1 
ATOM   14584 N  NE2   . GLN A 1 3537 ? 109.601 107.101 47.758  1.00 31.98  ? 3537 GLN A NE2   1 
ATOM   14585 N  N     . GLN A 1 3538 ? 115.154 108.635 51.452  1.00 16.37  ? 3538 GLN A N     1 
ATOM   14586 C  CA    . GLN A 1 3538 ? 116.134 109.575 51.987  1.00 17.10  ? 3538 GLN A CA    1 
ATOM   14587 C  C     . GLN A 1 3538 ? 117.542 108.995 52.021  1.00 19.84  ? 3538 GLN A C     1 
ATOM   14588 O  O     . GLN A 1 3538 ? 118.511 109.761 52.026  1.00 29.15  ? 3538 GLN A O     1 
ATOM   14589 C  CB    . GLN A 1 3538 ? 115.743 110.037 53.393  1.00 22.26  ? 3538 GLN A CB    1 
ATOM   14590 C  CG    . GLN A 1 3538 ? 114.262 110.282 53.597  1.00 21.44  ? 3538 GLN A CG    1 
ATOM   14591 C  CD    . GLN A 1 3538 ? 113.931 110.661 55.026  1.00 33.62  ? 3538 GLN A CD    1 
ATOM   14592 O  OE1   . GLN A 1 3538 ? 113.204 109.948 55.717  1.00 33.24  ? 3538 GLN A OE1   1 
ATOM   14593 N  NE2   . GLN A 1 3538 ? 114.464 111.789 55.478  1.00 38.53  ? 3538 GLN A NE2   1 
ATOM   14594 N  N     . ALA A 1 3539 ? 117.678 107.672 52.044  1.00 21.58  ? 3539 ALA A N     1 
ATOM   14595 C  CA    . ALA A 1 3539 ? 118.977 107.017 52.089  1.00 20.58  ? 3539 ALA A CA    1 
ATOM   14596 C  C     . ALA A 1 3539 ? 119.495 106.634 50.709  1.00 22.08  ? 3539 ALA A C     1 
ATOM   14597 O  O     . ALA A 1 3539 ? 120.530 105.966 50.615  1.00 29.50  ? 3539 ALA A O     1 
ATOM   14598 C  CB    . ALA A 1 3539 ? 118.911 105.775 52.981  1.00 14.24  ? 3539 ALA A CB    1 
ATOM   14599 N  N     . ASN A 1 3540 ? 118.793 107.030 49.644  1.00 18.03  ? 3540 ASN A N     1 
ATOM   14600 C  CA    . ASN A 1 3540 ? 119.170 106.706 48.267  1.00 20.97  ? 3540 ASN A CA    1 
ATOM   14601 C  C     . ASN A 1 3540 ? 119.211 105.198 48.030  1.00 22.03  ? 3540 ASN A C     1 
ATOM   14602 O  O     . ASN A 1 3540 ? 120.005 104.706 47.225  1.00 28.98  ? 3540 ASN A O     1 
ATOM   14603 C  CB    . ASN A 1 3540 ? 120.509 107.344 47.885  1.00 25.54  ? 3540 ASN A CB    1 
ATOM   14604 C  CG    . ASN A 1 3540 ? 120.395 108.834 47.637  1.00 27.63  ? 3540 ASN A CG    1 
ATOM   14605 O  OD1   . ASN A 1 3540 ? 119.476 109.488 48.128  1.00 29.54  ? 3540 ASN A OD1   1 
ATOM   14606 N  ND2   . ASN A 1 3540 ? 121.333 109.380 46.872  1.00 31.01  ? 3540 ASN A ND2   1 
ATOM   14607 N  N     . ILE A 1 3541 ? 118.359 104.456 48.729  1.00 18.62  ? 3541 ILE A N     1 
ATOM   14608 C  CA    . ILE A 1 3541 ? 118.243 103.015 48.542  1.00 19.69  ? 3541 ILE A CA    1 
ATOM   14609 C  C     . ILE A 1 3541 ? 117.185 102.750 47.481  1.00 20.14  ? 3541 ILE A C     1 
ATOM   14610 O  O     . ILE A 1 3541 ? 116.062 103.263 47.568  1.00 22.57  ? 3541 ILE A O     1 
ATOM   14611 C  CB    . ILE A 1 3541 ? 117.897 102.313 49.865  1.00 18.05  ? 3541 ILE A CB    1 
ATOM   14612 C  CG1   . ILE A 1 3541 ? 118.884 102.729 50.957  1.00 17.37  ? 3541 ILE A CG1   1 
ATOM   14613 C  CG2   . ILE A 1 3541 ? 117.890 100.802 49.685  1.00 14.57  ? 3541 ILE A CG2   1 
ATOM   14614 C  CD1   . ILE A 1 3541 ? 120.230 102.043 50.863  1.00 19.28  ? 3541 ILE A CD1   1 
ATOM   14615 N  N     . GLN A 1 3542 ? 117.539 101.951 46.480  1.00 21.89  ? 3542 GLN A N     1 
ATOM   14616 C  CA    . GLN A 1 3542 ? 116.681 101.760 45.319  1.00 23.49  ? 3542 GLN A CA    1 
ATOM   14617 C  C     . GLN A 1 3542 ? 115.627 100.695 45.593  1.00 24.28  ? 3542 GLN A C     1 
ATOM   14618 O  O     . GLN A 1 3542 ? 115.943 99.598  46.063  1.00 22.61  ? 3542 GLN A O     1 
ATOM   14619 C  CB    . GLN A 1 3542 ? 117.519 101.372 44.102  1.00 26.92  ? 3542 GLN A CB    1 
ATOM   14620 C  CG    . GLN A 1 3542 ? 118.415 102.489 43.588  1.00 30.83  ? 3542 GLN A CG    1 
ATOM   14621 C  CD    . GLN A 1 3542 ? 117.741 103.846 43.639  1.00 38.24  ? 3542 GLN A CD    1 
ATOM   14622 O  OE1   . GLN A 1 3542 ? 118.153 104.728 44.393  1.00 36.91  ? 3542 GLN A OE1   1 
ATOM   14623 N  NE2   . GLN A 1 3542 ? 116.701 104.022 42.832  1.00 38.41  ? 3542 GLN A NE2   1 
ATOM   14624 N  N     . PHE A 1 3543 ? 114.373 101.023 45.292  1.00 24.38  ? 3543 PHE A N     1 
ATOM   14625 C  CA    . PHE A 1 3543 ? 113.272 100.079 45.413  1.00 23.23  ? 3543 PHE A CA    1 
ATOM   14626 C  C     . PHE A 1 3543 ? 112.179 100.494 44.439  1.00 27.63  ? 3543 PHE A C     1 
ATOM   14627 O  O     . PHE A 1 3543 ? 112.170 101.618 43.932  1.00 26.65  ? 3543 PHE A O     1 
ATOM   14628 C  CB    . PHE A 1 3543 ? 112.733 100.014 46.847  1.00 15.85  ? 3543 PHE A CB    1 
ATOM   14629 C  CG    . PHE A 1 3543 ? 112.092 101.290 47.317  1.00 17.19  ? 3543 PHE A CG    1 
ATOM   14630 C  CD1   . PHE A 1 3543 ? 112.863 102.323 47.823  1.00 18.24  ? 3543 PHE A CD1   1 
ATOM   14631 C  CD2   . PHE A 1 3543 ? 110.718 101.453 47.260  1.00 17.25  ? 3543 PHE A CD2   1 
ATOM   14632 C  CE1   . PHE A 1 3543 ? 112.276 103.494 48.259  1.00 17.66  ? 3543 PHE A CE1   1 
ATOM   14633 C  CE2   . PHE A 1 3543 ? 110.126 102.622 47.695  1.00 19.39  ? 3543 PHE A CE2   1 
ATOM   14634 C  CZ    . PHE A 1 3543 ? 110.906 103.644 48.194  1.00 19.15  ? 3543 PHE A CZ    1 
ATOM   14635 N  N     . ARG A 1 3544 ? 111.259 99.570  44.184  1.00 28.96  ? 3544 ARG A N     1 
ATOM   14636 C  CA    . ARG A 1 3544 ? 110.159 99.806  43.259  1.00 29.58  ? 3544 ARG A CA    1 
ATOM   14637 C  C     . ARG A 1 3544 ? 108.894 100.175 44.021  1.00 33.70  ? 3544 ARG A C     1 
ATOM   14638 O  O     . ARG A 1 3544 ? 108.600 99.606  45.076  1.00 40.50  ? 3544 ARG A O     1 
ATOM   14639 C  CB    . ARG A 1 3544 ? 109.896 98.578  42.387  1.00 30.89  ? 3544 ARG A CB    1 
ATOM   14640 C  CG    . ARG A 1 3544 ? 111.024 98.231  41.433  1.00 32.92  ? 3544 ARG A CG    1 
ATOM   14641 C  CD    . ARG A 1 3544 ? 110.662 97.018  40.594  1.00 41.53  ? 3544 ARG A CD    1 
ATOM   14642 N  NE    . ARG A 1 3544 ? 110.559 95.800  41.388  1.00 49.76  ? 3544 ARG A NE    1 
ATOM   14643 C  CZ    . ARG A 1 3544 ? 110.117 94.641  40.920  1.00 51.25  ? 3544 ARG A CZ    1 
ATOM   14644 N  NH1   . ARG A 1 3544 ? 109.705 94.513  39.669  1.00 56.10  ? 3544 ARG A NH1   1 
ATOM   14645 N  NH2   . ARG A 1 3544 ? 110.081 93.586  41.728  1.00 43.74  ? 3544 ARG A NH2   1 
ATOM   14646 N  N     . THR A 1 3545 ? 108.147 101.135 43.477  1.00 37.11  ? 3545 THR A N     1 
ATOM   14647 C  CA    . THR A 1 3545 ? 106.890 101.583 44.060  1.00 42.31  ? 3545 THR A CA    1 
ATOM   14648 C  C     . THR A 1 3545 ? 105.676 101.105 43.272  1.00 45.82  ? 3545 THR A C     1 
ATOM   14649 O  O     . THR A 1 3545 ? 104.543 101.432 43.640  1.00 49.27  ? 3545 THR A O     1 
ATOM   14650 C  CB    . THR A 1 3545 ? 106.870 103.110 44.167  1.00 41.40  ? 3545 THR A CB    1 
ATOM   14651 O  OG1   . THR A 1 3545 ? 106.981 103.684 42.858  1.00 49.40  ? 3545 THR A OG1   1 
ATOM   14652 C  CG2   . THR A 1 3545 ? 108.023 103.599 45.026  1.00 31.07  ? 3545 THR A CG2   1 
ATOM   14653 N  N     . ASP A 1 3546 ? 105.882 100.340 42.201  1.00 45.03  ? 3546 ASP A N     1 
ATOM   14654 C  CA    . ASP A 1 3546 ? 104.794 99.895  41.338  1.00 50.31  ? 3546 ASP A CA    1 
ATOM   14655 C  C     . ASP A 1 3546 ? 104.243 98.528  41.719  1.00 54.28  ? 3546 ASP A C     1 
ATOM   14656 O  O     . ASP A 1 3546 ? 103.021 98.357  41.784  1.00 56.80  ? 3546 ASP A O     1 
ATOM   14657 C  CB    . ASP A 1 3546 ? 105.257 99.866  39.877  1.00 48.74  ? 3546 ASP A CB    1 
ATOM   14658 C  CG    . ASP A 1 3546 ? 106.589 99.163  39.702  1.00 53.62  ? 3546 ASP A CG    1 
ATOM   14659 O  OD1   . ASP A 1 3546 ? 107.152 98.693  40.712  1.00 55.96  ? 3546 ASP A OD1   1 
ATOM   14660 O  OD2   . ASP A 1 3546 ? 107.073 99.081  38.553  1.00 52.80  ? 3546 ASP A OD2   1 
ATOM   14661 N  N     . ILE A 1 3547 ? 105.109 97.552  41.969  1.00 47.30  ? 3547 ILE A N     1 
ATOM   14662 C  CA    . ILE A 1 3547 ? 104.669 96.194  42.269  1.00 48.65  ? 3547 ILE A CA    1 
ATOM   14663 C  C     . ILE A 1 3547 ? 104.087 96.146  43.676  1.00 44.29  ? 3547 ILE A C     1 
ATOM   14664 O  O     . ILE A 1 3547 ? 104.600 96.784  44.604  1.00 40.60  ? 3547 ILE A O     1 
ATOM   14665 C  CB    . ILE A 1 3547 ? 105.833 95.199  42.098  1.00 50.96  ? 3547 ILE A CB    1 
ATOM   14666 C  CG1   . ILE A 1 3547 ? 105.359 93.764  42.342  1.00 39.82  ? 3547 ILE A CG1   1 
ATOM   14667 C  CG2   . ILE A 1 3547 ? 106.996 95.557  43.016  1.00 45.41  ? 3547 ILE A CG2   1 
ATOM   14668 C  CD1   . ILE A 1 3547 ? 106.390 92.715  41.992  1.00 34.04  ? 3547 ILE A CD1   1 
ATOM   14669 N  N     . ALA A 1 3548 ? 102.997 95.401  43.832  1.00 36.56  ? 3548 ALA A N     1 
ATOM   14670 C  CA    . ALA A 1 3548 ? 102.364 95.241  45.129  1.00 32.01  ? 3548 ALA A CA    1 
ATOM   14671 C  C     . ALA A 1 3548 ? 103.144 94.250  45.990  1.00 27.58  ? 3548 ALA A C     1 
ATOM   14672 O  O     . ALA A 1 3548 ? 103.922 93.431  45.494  1.00 24.79  ? 3548 ALA A O     1 
ATOM   14673 C  CB    . ALA A 1 3548 ? 100.917 94.773  44.969  1.00 32.02  ? 3548 ALA A CB    1 
ATOM   14674 N  N     . ARG A 1 3549 ? 102.928 94.344  47.303  1.00 25.19  ? 3549 ARG A N     1 
ATOM   14675 C  CA    . ARG A 1 3549 ? 103.607 93.451  48.238  1.00 21.43  ? 3549 ARG A CA    1 
ATOM   14676 C  C     . ARG A 1 3549 ? 103.201 92.000  48.008  1.00 17.72  ? 3549 ARG A C     1 
ATOM   14677 O  O     . ARG A 1 3549 ? 104.050 91.099  47.982  1.00 22.96  ? 3549 ARG A O     1 
ATOM   14678 C  CB    . ARG A 1 3549 ? 103.293 93.870  49.674  1.00 21.36  ? 3549 ARG A CB    1 
ATOM   14679 C  CG    . ARG A 1 3549 ? 103.899 95.196  50.089  1.00 15.18  ? 3549 ARG A CG    1 
ATOM   14680 C  CD    . ARG A 1 3549 ? 103.703 95.439  51.575  1.00 10.49  ? 3549 ARG A CD    1 
ATOM   14681 N  NE    . ARG A 1 3549 ? 102.298 95.595  51.930  1.00 10.85  ? 3549 ARG A NE    1 
ATOM   14682 C  CZ    . ARG A 1 3549 ? 101.652 96.753  51.938  1.00 12.93  ? 3549 ARG A CZ    1 
ATOM   14683 N  NH1   . ARG A 1 3549 ? 102.254 97.883  51.607  1.00 13.89  ? 3549 ARG A NH1   1 
ATOM   14684 N  NH2   . ARG A 1 3549 ? 100.370 96.778  52.289  1.00 10.80  ? 3549 ARG A NH2   1 
ATOM   14685 N  N     . THR A 1 3550 ? 101.898 91.757  47.846  1.00 17.78  ? 3550 THR A N     1 
ATOM   14686 C  CA    . THR A 1 3550 ? 101.412 90.393  47.664  1.00 21.10  ? 3550 THR A CA    1 
ATOM   14687 C  C     . THR A 1 3550 ? 101.909 89.801  46.352  1.00 19.75  ? 3550 THR A C     1 
ATOM   14688 O  O     . THR A 1 3550 ? 102.267 88.619  46.295  1.00 17.44  ? 3550 THR A O     1 
ATOM   14689 C  CB    . THR A 1 3550 ? 99.885  90.370  47.718  1.00 19.94  ? 3550 THR A CB    1 
ATOM   14690 O  OG1   . THR A 1 3550 ? 99.357  91.283  46.747  1.00 20.05  ? 3550 THR A OG1   1 
ATOM   14691 C  CG2   . THR A 1 3550 ? 99.401  90.777  49.098  1.00 14.97  ? 3550 THR A CG2   1 
ATOM   14692 N  N     . GLU A 1 3551 ? 101.933 90.606  45.289  1.00 23.55  ? 3551 GLU A N     1 
ATOM   14693 C  CA    . GLU A 1 3551 ? 102.456 90.132  44.013  1.00 20.77  ? 3551 GLU A CA    1 
ATOM   14694 C  C     . GLU A 1 3551 ? 103.953 89.866  44.100  1.00 19.58  ? 3551 GLU A C     1 
ATOM   14695 O  O     . GLU A 1 3551 ? 104.469 88.957  43.439  1.00 19.72  ? 3551 GLU A O     1 
ATOM   14696 C  CB    . GLU A 1 3551 ? 102.155 91.149  42.913  1.00 25.36  ? 3551 GLU A CB    1 
ATOM   14697 C  CG    . GLU A 1 3551 ? 100.683 91.499  42.776  1.00 27.52  ? 3551 GLU A CG    1 
ATOM   14698 C  CD    . GLU A 1 3551 ? 99.964  90.614  41.779  1.00 39.68  ? 3551 GLU A CD    1 
ATOM   14699 O  OE1   . GLU A 1 3551 ? 98.741  90.791  41.599  1.00 44.63  ? 3551 GLU A OE1   1 
ATOM   14700 O  OE2   . GLU A 1 3551 ? 100.621 89.741  41.174  1.00 43.09  ? 3551 GLU A OE2   1 
ATOM   14701 N  N     . TYR A 1 3552 ? 104.666 90.651  44.909  1.00 20.14  ? 3552 TYR A N     1 
ATOM   14702 C  CA    . TYR A 1 3552 ? 106.112 90.503  45.014  1.00 18.64  ? 3552 TYR A CA    1 
ATOM   14703 C  C     . TYR A 1 3552 ? 106.517 89.288  45.838  1.00 19.60  ? 3552 TYR A C     1 
ATOM   14704 O  O     . TYR A 1 3552 ? 107.492 88.612  45.492  1.00 20.87  ? 3552 TYR A O     1 
ATOM   14705 C  CB    . TYR A 1 3552 ? 106.723 91.768  45.617  1.00 20.72  ? 3552 TYR A CB    1 
ATOM   14706 C  CG    . TYR A 1 3552 ? 108.232 91.768  45.642  1.00 25.73  ? 3552 TYR A CG    1 
ATOM   14707 C  CD1   . TYR A 1 3552 ? 108.963 92.116  44.515  1.00 29.24  ? 3552 TYR A CD1   1 
ATOM   14708 C  CD2   . TYR A 1 3552 ? 108.927 91.426  46.794  1.00 20.54  ? 3552 TYR A CD2   1 
ATOM   14709 C  CE1   . TYR A 1 3552 ? 110.342 92.120  44.533  1.00 26.89  ? 3552 TYR A CE1   1 
ATOM   14710 C  CE2   . TYR A 1 3552 ? 110.306 91.428  46.822  1.00 20.33  ? 3552 TYR A CE2   1 
ATOM   14711 C  CZ    . TYR A 1 3552 ? 111.008 91.776  45.688  1.00 26.54  ? 3552 TYR A CZ    1 
ATOM   14712 O  OH    . TYR A 1 3552 ? 112.381 91.779  45.709  1.00 26.41  ? 3552 TYR A OH    1 
ATOM   14713 N  N     . LEU A 1 3553 ? 105.798 88.991  46.919  1.00 18.46  ? 3553 LEU A N     1 
ATOM   14714 C  CA    . LEU A 1 3553 ? 106.177 87.896  47.803  1.00 17.73  ? 3553 LEU A CA    1 
ATOM   14715 C  C     . LEU A 1 3553 ? 105.361 86.629  47.590  1.00 16.32  ? 3553 LEU A C     1 
ATOM   14716 O  O     . LEU A 1 3553 ? 105.496 85.686  48.375  1.00 13.93  ? 3553 LEU A O     1 
ATOM   14717 C  CB    . LEU A 1 3553 ? 106.074 88.333  49.265  1.00 14.84  ? 3553 LEU A CB    1 
ATOM   14718 C  CG    . LEU A 1 3553 ? 107.153 89.321  49.707  1.00 16.15  ? 3553 LEU A CG    1 
ATOM   14719 C  CD1   . LEU A 1 3553 ? 106.903 89.773  51.127  1.00 12.36  ? 3553 LEU A CD1   1 
ATOM   14720 C  CD2   . LEU A 1 3553 ? 108.531 88.693  49.574  1.00 14.33  ? 3553 LEU A CD2   1 
ATOM   14721 N  N     . SER A 1 3554 ? 104.524 86.577  46.558  1.00 16.69  ? 3554 SER A N     1 
ATOM   14722 C  CA    . SER A 1 3554 ? 103.788 85.364  46.244  1.00 16.98  ? 3554 SER A CA    1 
ATOM   14723 C  C     . SER A 1 3554 ? 103.540 85.312  44.745  1.00 20.18  ? 3554 SER A C     1 
ATOM   14724 O  O     . SER A 1 3554 ? 103.393 86.347  44.090  1.00 21.88  ? 3554 SER A O     1 
ATOM   14725 C  CB    . SER A 1 3554 ? 102.463 85.291  47.012  1.00 14.72  ? 3554 SER A CB    1 
ATOM   14726 O  OG    . SER A 1 3554 ? 101.505 86.179  46.466  1.00 15.42  ? 3554 SER A OG    1 
ATOM   14727 N  N     . ASN A 1 3555 ? 103.496 84.098  44.208  1.00 20.67  ? 3555 ASN A N     1 
ATOM   14728 C  CA    . ASN A 1 3555 ? 103.220 83.886  42.797  1.00 20.05  ? 3555 ASN A CA    1 
ATOM   14729 C  C     . ASN A 1 3555 ? 101.741 83.573  42.596  1.00 19.17  ? 3555 ASN A C     1 
ATOM   14730 O  O     . ASN A 1 3555 ? 100.998 83.311  43.544  1.00 19.55  ? 3555 ASN A O     1 
ATOM   14731 C  CB    . ASN A 1 3555 ? 104.094 82.761  42.231  1.00 19.32  ? 3555 ASN A CB    1 
ATOM   14732 C  CG    . ASN A 1 3555 ? 104.029 81.496  43.060  1.00 23.82  ? 3555 ASN A CG    1 
ATOM   14733 O  OD1   . ASN A 1 3555 ? 103.033 80.775  43.032  1.00 25.72  ? 3555 ASN A OD1   1 
ATOM   14734 N  ND2   . ASN A 1 3555 ? 105.094 81.216  43.802  1.00 22.19  ? 3555 ASN A ND2   1 
ATOM   14735 N  N     . ALA A 1 3556 ? 101.317 83.609  41.331  1.00 21.75  ? 3556 ALA A N     1 
ATOM   14736 C  CA    . ALA A 1 3556 ? 99.909  83.393  41.018  1.00 19.55  ? 3556 ALA A CA    1 
ATOM   14737 C  C     . ALA A 1 3556 ? 99.460  81.975  41.346  1.00 21.41  ? 3556 ALA A C     1 
ATOM   14738 O  O     . ALA A 1 3556 ? 98.293  81.765  41.696  1.00 21.95  ? 3556 ALA A O     1 
ATOM   14739 C  CB    . ALA A 1 3556 ? 99.646  83.709  39.547  1.00 18.57  ? 3556 ALA A CB    1 
ATOM   14740 N  N     . ASP A 1 3557 ? 100.357 80.993  41.234  1.00 19.57  ? 3557 ASP A N     1 
ATOM   14741 C  CA    . ASP A 1 3557 ? 99.994  79.617  41.563  1.00 21.95  ? 3557 ASP A CA    1 
ATOM   14742 C  C     . ASP A 1 3557 ? 99.666  79.477  43.045  1.00 25.36  ? 3557 ASP A C     1 
ATOM   14743 O  O     . ASP A 1 3557 ? 98.667  78.848  43.420  1.00 28.20  ? 3557 ASP A O     1 
ATOM   14744 C  CB    . ASP A 1 3557 ? 101.128 78.670  41.172  1.00 27.04  ? 3557 ASP A CB    1 
ATOM   14745 C  CG    . ASP A 1 3557 ? 101.281 78.534  39.672  1.00 35.81  ? 3557 ASP A CG    1 
ATOM   14746 O  OD1   . ASP A 1 3557 ? 100.261 78.623  38.960  1.00 35.97  ? 3557 ASP A OD1   1 
ATOM   14747 O  OD2   . ASP A 1 3557 ? 102.423 78.338  39.205  1.00 40.13  ? 3557 ASP A OD2   1 
ATOM   14748 N  N     . GLU A 1 3558 ? 100.504 80.062  43.905  1.00 21.67  ? 3558 GLU A N     1 
ATOM   14749 C  CA    . GLU A 1 3558 ? 100.250 80.012  45.341  1.00 20.39  ? 3558 GLU A CA    1 
ATOM   14750 C  C     . GLU A 1 3558 ? 98.957  80.731  45.697  1.00 18.08  ? 3558 GLU A C     1 
ATOM   14751 O  O     . GLU A 1 3558 ? 98.192  80.259  46.542  1.00 18.57  ? 3558 GLU A O     1 
ATOM   14752 C  CB    . GLU A 1 3558 ? 101.427 80.614  46.107  1.00 20.34  ? 3558 GLU A CB    1 
ATOM   14753 C  CG    . GLU A 1 3558 ? 102.709 79.808  46.009  1.00 30.80  ? 3558 GLU A CG    1 
ATOM   14754 C  CD    . GLU A 1 3558 ? 103.856 80.448  46.763  1.00 38.49  ? 3558 GLU A CD    1 
ATOM   14755 O  OE1   . GLU A 1 3558 ? 103.685 81.582  47.255  1.00 32.10  ? 3558 GLU A OE1   1 
ATOM   14756 O  OE2   . GLU A 1 3558 ? 104.928 79.816  46.863  1.00 44.33  ? 3558 GLU A OE2   1 
ATOM   14757 N  N     . ARG A 1 3559 ? 98.699  81.878  45.068  1.00 16.14  ? 3559 ARG A N     1 
ATOM   14758 C  CA    . ARG A 1 3559 ? 97.463  82.606  45.339  1.00 15.70  ? 3559 ARG A CA    1 
ATOM   14759 C  C     . ARG A 1 3559 ? 96.241  81.816  44.884  1.00 18.72  ? 3559 ARG A C     1 
ATOM   14760 O  O     . ARG A 1 3559 ? 95.217  81.793  45.578  1.00 18.27  ? 3559 ARG A O     1 
ATOM   14761 C  CB    . ARG A 1 3559 ? 97.513  83.979  44.672  1.00 13.63  ? 3559 ARG A CB    1 
ATOM   14762 C  CG    . ARG A 1 3559 ? 98.520  84.916  45.315  1.00 14.19  ? 3559 ARG A CG    1 
ATOM   14763 C  CD    . ARG A 1 3559 ? 98.480  86.303  44.704  1.00 16.27  ? 3559 ARG A CD    1 
ATOM   14764 N  NE    . ARG A 1 3559 ? 98.792  86.279  43.280  1.00 20.11  ? 3559 ARG A NE    1 
ATOM   14765 C  CZ    . ARG A 1 3559 ? 99.909  86.760  42.754  1.00 19.86  ? 3559 ARG A CZ    1 
ATOM   14766 N  NH1   . ARG A 1 3559 ? 100.860 87.283  43.510  1.00 18.50  ? 3559 ARG A NH1   1 
ATOM   14767 N  NH2   . ARG A 1 3559 ? 100.080 86.710  41.436  1.00 24.44  ? 3559 ARG A NH2   1 
ATOM   14768 N  N     . LEU A 1 3560 ? 96.328  81.159  43.725  1.00 19.61  ? 3560 LEU A N     1 
ATOM   14769 C  CA    . LEU A 1 3560 ? 95.222  80.325  43.262  1.00 17.58  ? 3560 LEU A CA    1 
ATOM   14770 C  C     . LEU A 1 3560 ? 94.971  79.163  44.215  1.00 19.35  ? 3560 LEU A C     1 
ATOM   14771 O  O     . LEU A 1 3560 ? 93.816  78.839  44.522  1.00 21.85  ? 3560 LEU A O     1 
ATOM   14772 C  CB    . LEU A 1 3560 ? 95.508  79.811  41.852  1.00 25.05  ? 3560 LEU A CB    1 
ATOM   14773 C  CG    . LEU A 1 3560 ? 94.290  79.475  40.990  1.00 24.41  ? 3560 LEU A CG    1 
ATOM   14774 C  CD1   . LEU A 1 3560 ? 93.561  80.742  40.569  1.00 23.11  ? 3560 LEU A CD1   1 
ATOM   14775 C  CD2   . LEU A 1 3560 ? 94.702  78.658  39.777  1.00 29.63  ? 3560 LEU A CD2   1 
ATOM   14776 N  N     . ARG A 1 3561 ? 96.039  78.519  44.691  1.00 18.29  ? 3561 ARG A N     1 
ATOM   14777 C  CA    . ARG A 1 3561 ? 95.870  77.428  45.648  1.00 20.08  ? 3561 ARG A CA    1 
ATOM   14778 C  C     . ARG A 1 3561 ? 95.295  77.936  46.966  1.00 21.15  ? 3561 ARG A C     1 
ATOM   14779 O  O     . ARG A 1 3561 ? 94.475  77.259  47.598  1.00 24.30  ? 3561 ARG A O     1 
ATOM   14780 C  CB    . ARG A 1 3561 ? 97.203  76.715  45.873  1.00 22.67  ? 3561 ARG A CB    1 
ATOM   14781 C  CG    . ARG A 1 3561 ? 97.173  75.675  46.981  1.00 24.40  ? 3561 ARG A CG    1 
ATOM   14782 C  CD    . ARG A 1 3561 ? 98.507  74.960  47.108  1.00 34.07  ? 3561 ARG A CD    1 
ATOM   14783 N  NE    . ARG A 1 3561 ? 99.461  75.715  47.911  1.00 35.67  ? 3561 ARG A NE    1 
ATOM   14784 C  CZ    . ARG A 1 3561 ? 100.430 76.469  47.410  1.00 39.12  ? 3561 ARG A CZ    1 
ATOM   14785 N  NH1   . ARG A 1 3561 ? 100.606 76.590  46.105  1.00 39.08  ? 3561 ARG A NH1   1 
ATOM   14786 N  NH2   . ARG A 1 3561 ? 101.244 77.115  48.240  1.00 37.24  ? 3561 ARG A NH2   1 
ATOM   14787 N  N     . TRP A 1 3562 ? 95.716  79.127  47.397  1.00 19.55  ? 3562 TRP A N     1 
ATOM   14788 C  CA    . TRP A 1 3562 ? 95.168  79.725  48.609  1.00 17.63  ? 3562 TRP A CA    1 
ATOM   14789 C  C     . TRP A 1 3562 ? 93.677  79.990  48.454  1.00 20.69  ? 3562 TRP A C     1 
ATOM   14790 O  O     . TRP A 1 3562 ? 92.895  79.759  49.383  1.00 22.42  ? 3562 TRP A O     1 
ATOM   14791 C  CB    . TRP A 1 3562 ? 95.914  81.021  48.927  1.00 14.25  ? 3562 TRP A CB    1 
ATOM   14792 C  CG    . TRP A 1 3562 ? 97.317  80.806  49.406  1.00 12.69  ? 3562 TRP A CG    1 
ATOM   14793 C  CD1   . TRP A 1 3562 ? 97.860  79.638  49.854  1.00 14.68  ? 3562 TRP A CD1   1 
ATOM   14794 C  CD2   . TRP A 1 3562 ? 98.367  81.779  49.449  1.00 12.17  ? 3562 TRP A CD2   1 
ATOM   14795 N  NE1   . TRP A 1 3562 ? 99.178  79.827  50.190  1.00 13.93  ? 3562 TRP A NE1   1 
ATOM   14796 C  CE2   . TRP A 1 3562 ? 99.514  81.133  49.949  1.00 13.80  ? 3562 TRP A CE2   1 
ATOM   14797 C  CE3   . TRP A 1 3562 ? 98.447  83.136  49.120  1.00 11.44  ? 3562 TRP A CE3   1 
ATOM   14798 C  CZ2   . TRP A 1 3562 ? 100.726 81.796  50.129  1.00 12.50  ? 3562 TRP A CZ2   1 
ATOM   14799 C  CZ3   . TRP A 1 3562 ? 99.651  83.793  49.300  1.00 10.90  ? 3562 TRP A CZ3   1 
ATOM   14800 C  CH2   . TRP A 1 3562 ? 100.774 83.122  49.800  1.00 10.96  ? 3562 TRP A CH2   1 
ATOM   14801 N  N     . GLN A 1 3563 ? 93.269  80.479  47.281  1.00 22.25  ? 3563 GLN A N     1 
ATOM   14802 C  CA    . GLN A 1 3563 ? 91.847  80.640  46.995  1.00 22.95  ? 3563 GLN A CA    1 
ATOM   14803 C  C     . GLN A 1 3563 ? 91.129  79.298  47.026  1.00 23.25  ? 3563 GLN A C     1 
ATOM   14804 O  O     . GLN A 1 3563 ? 89.991  79.205  47.502  1.00 20.43  ? 3563 GLN A O     1 
ATOM   14805 C  CB    . GLN A 1 3563 ? 91.656  81.324  45.642  1.00 21.22  ? 3563 GLN A CB    1 
ATOM   14806 C  CG    . GLN A 1 3563 ? 92.202  82.738  45.592  1.00 33.81  ? 3563 GLN A CG    1 
ATOM   14807 C  CD    . GLN A 1 3563 ? 91.443  83.678  46.504  1.00 44.41  ? 3563 GLN A CD    1 
ATOM   14808 O  OE1   . GLN A 1 3563 ? 90.221  83.592  46.624  1.00 50.47  ? 3563 GLN A OE1   1 
ATOM   14809 N  NE2   . GLN A 1 3563 ? 92.166  84.576  47.163  1.00 44.78  ? 3563 GLN A NE2   1 
ATOM   14810 N  N     . ALA A 1 3564 ? 91.777  78.246  46.519  1.00 23.82  ? 3564 ALA A N     1 
ATOM   14811 C  CA    . ALA A 1 3564 ? 91.211  76.906  46.633  1.00 20.94  ? 3564 ALA A CA    1 
ATOM   14812 C  C     . ALA A 1 3564 ? 91.075  76.481  48.089  1.00 26.83  ? 3564 ALA A C     1 
ATOM   14813 O  O     . ALA A 1 3564 ? 90.092  75.827  48.456  1.00 34.71  ? 3564 ALA A O     1 
ATOM   14814 C  CB    . ALA A 1 3564 ? 92.068  75.903  45.861  1.00 22.10  ? 3564 ALA A CB    1 
ATOM   14815 N  N     . SER A 1 3565 ? 92.045  76.843  48.932  1.00 27.03  ? 3565 SER A N     1 
ATOM   14816 C  CA    . SER A 1 3565 ? 92.009  76.550  50.360  1.00 19.32  ? 3565 SER A CA    1 
ATOM   14817 C  C     . SER A 1 3565 ? 91.086  77.485  51.138  1.00 20.67  ? 3565 SER A C     1 
ATOM   14818 O  O     . SER A 1 3565 ? 91.189  77.545  52.370  1.00 23.19  ? 3565 SER A O     1 
ATOM   14819 C  CB    . SER A 1 3565 ? 93.422  76.608  50.948  1.00 19.76  ? 3565 SER A CB    1 
ATOM   14820 O  OG    . SER A 1 3565 ? 94.239  75.575  50.424  1.00 23.90  ? 3565 SER A OG    1 
ATOM   14821 N  N     . SER A 1 3566 ? 90.219  78.223  50.441  1.00 23.68  ? 3566 SER A N     1 
ATOM   14822 C  CA    . SER A 1 3566 ? 89.215  79.101  51.043  1.00 20.20  ? 3566 SER A CA    1 
ATOM   14823 C  C     . SER A 1 3566 ? 89.837  80.307  51.744  1.00 21.24  ? 3566 SER A C     1 
ATOM   14824 O  O     . SER A 1 3566 ? 89.305  80.792  52.744  1.00 23.36  ? 3566 SER A O     1 
ATOM   14825 C  CB    . SER A 1 3566 ? 88.303  78.338  52.011  1.00 18.74  ? 3566 SER A CB    1 
ATOM   14826 O  OG    . SER A 1 3566 ? 88.937  78.137  53.262  1.00 25.47  ? 3566 SER A OG    1 
ATOM   14827 N  N     . LEU A 1 3567 ? 90.960  80.800  51.235  1.00 19.57  ? 3567 LEU A N     1 
ATOM   14828 C  CA    . LEU A 1 3567 ? 91.485  82.075  51.712  1.00 18.99  ? 3567 LEU A CA    1 
ATOM   14829 C  C     . LEU A 1 3567 ? 90.700  83.216  51.076  1.00 27.23  ? 3567 LEU A C     1 
ATOM   14830 O  O     . LEU A 1 3567 ? 90.564  83.256  49.849  1.00 26.34  ? 3567 LEU A O     1 
ATOM   14831 C  CB    . LEU A 1 3567 ? 92.968  82.215  51.383  1.00 17.25  ? 3567 LEU A CB    1 
ATOM   14832 C  CG    . LEU A 1 3567 ? 93.648  83.478  51.917  1.00 15.92  ? 3567 LEU A CG    1 
ATOM   14833 C  CD1   . LEU A 1 3567 ? 94.000  83.319  53.389  1.00 16.49  ? 3567 LEU A CD1   1 
ATOM   14834 C  CD2   . LEU A 1 3567 ? 94.883  83.816  51.099  1.00 10.20  ? 3567 LEU A CD2   1 
ATOM   14835 N  N     . PRO A 1 3568 ? 90.159  84.142  51.867  1.00 27.10  ? 3568 PRO A N     1 
ATOM   14836 C  CA    . PRO A 1 3568 ? 89.357  85.229  51.291  1.00 23.83  ? 3568 PRO A CA    1 
ATOM   14837 C  C     . PRO A 1 3568 ? 90.170  86.076  50.323  1.00 27.22  ? 3568 PRO A C     1 
ATOM   14838 O  O     . PRO A 1 3568 ? 91.362  86.315  50.524  1.00 30.49  ? 3568 PRO A O     1 
ATOM   14839 C  CB    . PRO A 1 3568 ? 88.924  86.038  52.518  1.00 22.28  ? 3568 PRO A CB    1 
ATOM   14840 C  CG    . PRO A 1 3568 ? 89.002  85.073  53.653  1.00 24.05  ? 3568 PRO A CG    1 
ATOM   14841 C  CD    . PRO A 1 3568 ? 90.162  84.179  53.339  1.00 23.08  ? 3568 PRO A CD    1 
ATOM   14842 N  N     . ALA A 1 3569 ? 89.505  86.534  49.261  1.00 27.07  ? 3569 ALA A N     1 
ATOM   14843 C  CA    . ALA A 1 3569 ? 90.141  87.363  48.238  1.00 30.81  ? 3569 ALA A CA    1 
ATOM   14844 C  C     . ALA A 1 3569 ? 90.294  88.777  48.792  1.00 32.79  ? 3569 ALA A C     1 
ATOM   14845 O  O     . ALA A 1 3569 ? 89.469  89.667  48.570  1.00 39.24  ? 3569 ALA A O     1 
ATOM   14846 C  CB    . ALA A 1 3569 ? 89.332  87.345  46.948  1.00 34.11  ? 3569 ALA A CB    1 
ATOM   14847 N  N     . ASP A 1 3570 ? 91.381  88.978  49.531  1.00 28.43  ? 3570 ASP A N     1 
ATOM   14848 C  CA    . ASP A 1 3570 ? 91.663  90.259  50.159  1.00 20.95  ? 3570 ASP A CA    1 
ATOM   14849 C  C     . ASP A 1 3570 ? 93.171  90.436  50.246  1.00 19.67  ? 3570 ASP A C     1 
ATOM   14850 O  O     . ASP A 1 3570 ? 93.904  89.464  50.443  1.00 19.97  ? 3570 ASP A O     1 
ATOM   14851 C  CB    . ASP A 1 3570 ? 91.028  90.348  51.552  1.00 20.62  ? 3570 ASP A CB    1 
ATOM   14852 C  CG    . ASP A 1 3570 ? 91.332  91.656  52.252  1.00 26.09  ? 3570 ASP A CG    1 
ATOM   14853 O  OD1   . ASP A 1 3570 ? 91.177  92.722  51.620  1.00 29.32  ? 3570 ASP A OD1   1 
ATOM   14854 O  OD2   . ASP A 1 3570 ? 91.726  91.619  53.436  1.00 26.20  ? 3570 ASP A OD2   1 
ATOM   14855 N  N     . ASP A 1 3571 ? 93.625  91.682  50.091  1.00 18.23  ? 3571 ASP A N     1 
ATOM   14856 C  CA    . ASP A 1 3571 ? 95.058  91.956  50.133  1.00 18.10  ? 3571 ASP A CA    1 
ATOM   14857 C  C     . ASP A 1 3571 ? 95.645  91.640  51.503  1.00 14.82  ? 3571 ASP A C     1 
ATOM   14858 O  O     . ASP A 1 3571 ? 96.733  91.061  51.601  1.00 13.42  ? 3571 ASP A O     1 
ATOM   14859 C  CB    . ASP A 1 3571 ? 95.324  93.413  49.757  1.00 20.11  ? 3571 ASP A CB    1 
ATOM   14860 C  CG    . ASP A 1 3571 ? 95.485  93.608  48.263  1.00 31.64  ? 3571 ASP A CG    1 
ATOM   14861 O  OD1   . ASP A 1 3571 ? 95.379  92.610  47.519  1.00 34.19  ? 3571 ASP A OD1   1 
ATOM   14862 O  OD2   . ASP A 1 3571 ? 95.716  94.757  47.833  1.00 33.11  ? 3571 ASP A OD2   1 
ATOM   14863 N  N     . LEU A 1 3572 ? 94.941  92.015  52.574  1.00 12.59  ? 3572 LEU A N     1 
ATOM   14864 C  CA    . LEU A 1 3572 ? 95.426  91.712  53.916  1.00 11.34  ? 3572 LEU A CA    1 
ATOM   14865 C  C     . LEU A 1 3572 ? 95.436  90.208  54.169  1.00 10.04  ? 3572 LEU A C     1 
ATOM   14866 O  O     . LEU A 1 3572 ? 96.353  89.689  54.815  1.00 7.67   ? 3572 LEU A O     1 
ATOM   14867 C  CB    . LEU A 1 3572 ? 94.576  92.443  54.958  1.00 11.51  ? 3572 LEU A CB    1 
ATOM   14868 C  CG    . LEU A 1 3572 ? 95.021  92.414  56.424  1.00 10.13  ? 3572 LEU A CG    1 
ATOM   14869 C  CD1   . LEU A 1 3572 ? 94.618  93.703  57.116  1.00 10.08  ? 3572 LEU A CD1   1 
ATOM   14870 C  CD2   . LEU A 1 3572 ? 94.430  91.223  57.167  1.00 7.57   ? 3572 LEU A CD2   1 
ATOM   14871 N  N     . CYS A 1 3573 ? 94.428  89.493  53.666  1.00 10.20  ? 3573 CYS A N     1 
ATOM   14872 C  CA    . CYS A 1 3573 ? 94.413  88.040  53.805  1.00 9.51   ? 3573 CYS A CA    1 
ATOM   14873 C  C     . CYS A 1 3573 ? 95.567  87.398  53.043  1.00 9.69   ? 3573 CYS A C     1 
ATOM   14874 O  O     . CYS A 1 3573 ? 96.181  86.438  53.522  1.00 9.16   ? 3573 CYS A O     1 
ATOM   14875 C  CB    . CYS A 1 3573 ? 93.073  87.482  53.328  1.00 13.89  ? 3573 CYS A CB    1 
ATOM   14876 S  SG    . CYS A 1 3573 ? 91.695  87.795  54.456  1.00 26.30  ? 3573 CYS A SG    1 
ATOM   14877 N  N     . THR A 1 3574 ? 95.874  87.911  51.848  1.00 10.16  ? 3574 THR A N     1 
ATOM   14878 C  CA    . THR A 1 3574 ? 97.009  87.388  51.094  1.00 7.60   ? 3574 THR A CA    1 
ATOM   14879 C  C     . THR A 1 3574 ? 98.325  87.676  51.810  1.00 7.39   ? 3574 THR A C     1 
ATOM   14880 O  O     . THR A 1 3574 ? 99.225  86.828  51.831  1.00 10.70  ? 3574 THR A O     1 
ATOM   14881 C  CB    . THR A 1 3574 ? 97.021  87.978  49.683  1.00 9.24   ? 3574 THR A CB    1 
ATOM   14882 O  OG1   . THR A 1 3574 ? 95.761  87.722  49.050  1.00 14.01  ? 3574 THR A OG1   1 
ATOM   14883 C  CG2   . THR A 1 3574 ? 98.124  87.343  48.853  1.00 8.03   ? 3574 THR A CG2   1 
ATOM   14884 N  N     . GLU A 1 3575 ? 98.451  88.865  52.404  1.00 7.11   ? 3575 GLU A N     1 
ATOM   14885 C  CA    . GLU A 1 3575 ? 99.628  89.173  53.211  1.00 7.86   ? 3575 GLU A CA    1 
ATOM   14886 C  C     . GLU A 1 3575 ? 99.746  88.218  54.391  1.00 6.85   ? 3575 GLU A C     1 
ATOM   14887 O  O     . GLU A 1 3575 ? 100.846 87.759  54.727  1.00 7.28   ? 3575 GLU A O     1 
ATOM   14888 C  CB    . GLU A 1 3575 ? 99.558  90.619  53.703  1.00 9.01   ? 3575 GLU A CB    1 
ATOM   14889 C  CG    . GLU A 1 3575 ? 99.764  91.665  52.626  1.00 11.73  ? 3575 GLU A CG    1 
ATOM   14890 C  CD    . GLU A 1 3575 ? 99.385  93.058  53.090  1.00 15.39  ? 3575 GLU A CD    1 
ATOM   14891 O  OE1   . GLU A 1 3575 ? 98.871  93.190  54.220  1.00 17.34  ? 3575 GLU A OE1   1 
ATOM   14892 O  OE2   . GLU A 1 3575 ? 99.602  94.021  52.326  1.00 18.60  ? 3575 GLU A OE2   1 
ATOM   14893 N  N     . ASN A 1 3576 ? 98.620  87.918  55.039  1.00 6.07   ? 3576 ASN A N     1 
ATOM   14894 C  CA    . ASN A 1 3576 ? 98.621  86.968  56.144  1.00 5.63   ? 3576 ASN A CA    1 
ATOM   14895 C  C     . ASN A 1 3576 ? 99.051  85.583  55.680  1.00 6.70   ? 3576 ASN A C     1 
ATOM   14896 O  O     . ASN A 1 3576 ? 99.793  84.890  56.382  1.00 7.04   ? 3576 ASN A O     1 
ATOM   14897 C  CB    . ASN A 1 3576 ? 97.235  86.919  56.786  1.00 5.86   ? 3576 ASN A CB    1 
ATOM   14898 C  CG    . ASN A 1 3576 ? 96.921  88.164  57.589  1.00 5.12   ? 3576 ASN A CG    1 
ATOM   14899 O  OD1   . ASN A 1 3576 ? 97.728  89.088  57.662  1.00 6.27   ? 3576 ASN A OD1   1 
ATOM   14900 N  ND2   . ASN A 1 3576 ? 95.742  88.195  58.197  1.00 5.09   ? 3576 ASN A ND2   1 
ATOM   14901 N  N     . ALA A 1 3577 ? 98.587  85.160  54.503  1.00 6.33   ? 3577 ALA A N     1 
ATOM   14902 C  CA    . ALA A 1 3577 ? 99.009  83.873  53.956  1.00 6.11   ? 3577 ALA A CA    1 
ATOM   14903 C  C     . ALA A 1 3577 ? 100.507 83.857  53.667  1.00 6.58   ? 3577 ALA A C     1 
ATOM   14904 O  O     . ALA A 1 3577 ? 101.189 82.857  53.922  1.00 7.37   ? 3577 ALA A O     1 
ATOM   14905 C  CB    . ALA A 1 3577 ? 98.215  83.553  52.691  1.00 6.18   ? 3577 ALA A CB    1 
ATOM   14906 N  N     . ILE A 1 3578 ? 101.036 84.958  53.129  1.00 5.27   ? 3578 ILE A N     1 
ATOM   14907 C  CA    . ILE A 1 3578 ? 102.473 85.043  52.880  1.00 6.03   ? 3578 ILE A CA    1 
ATOM   14908 C  C     . ILE A 1 3578 ? 103.248 84.944  54.190  1.00 6.44   ? 3578 ILE A C     1 
ATOM   14909 O  O     . ILE A 1 3578 ? 104.289 84.277  54.265  1.00 6.56   ? 3578 ILE A O     1 
ATOM   14910 C  CB    . ILE A 1 3578 ? 102.812 86.334  52.112  1.00 7.43   ? 3578 ILE A CB    1 
ATOM   14911 C  CG1   . ILE A 1 3578 ? 102.138 86.326  50.739  1.00 7.65   ? 3578 ILE A CG1   1 
ATOM   14912 C  CG2   . ILE A 1 3578 ? 104.316 86.494  51.966  1.00 9.18   ? 3578 ILE A CG2   1 
ATOM   14913 C  CD1   . ILE A 1 3578 ? 102.326 87.601  49.957  1.00 9.75   ? 3578 ILE A CD1   1 
ATOM   14914 N  N     . MET A 1 3579 ? 102.756 85.604  55.242  1.00 5.54   ? 3579 MET A N     1 
ATOM   14915 C  CA    . MET A 1 3579 ? 103.393 85.473  56.549  1.00 5.03   ? 3579 MET A CA    1 
ATOM   14916 C  C     . MET A 1 3579 ? 103.315 84.041  57.067  1.00 5.20   ? 3579 MET A C     1 
ATOM   14917 O  O     . MET A 1 3579 ? 104.282 83.528  57.643  1.00 6.67   ? 3579 MET A O     1 
ATOM   14918 C  CB    . MET A 1 3579 ? 102.773 86.443  57.557  1.00 5.08   ? 3579 MET A CB    1 
ATOM   14919 C  CG    . MET A 1 3579 ? 103.102 87.902  57.298  1.00 6.14   ? 3579 MET A CG    1 
ATOM   14920 S  SD    . MET A 1 3579 ? 101.819 89.053  57.819  1.00 10.86  ? 3579 MET A SD    1 
ATOM   14921 C  CE    . MET A 1 3579 ? 102.580 90.610  57.365  1.00 8.47   ? 3579 MET A CE    1 
ATOM   14922 N  N     . LEU A 1 3580 ? 102.174 83.380  56.872  1.00 5.26   ? 3580 LEU A N     1 
ATOM   14923 C  CA    . LEU A 1 3580 ? 102.020 81.994  57.300  1.00 5.91   ? 3580 LEU A CA    1 
ATOM   14924 C  C     . LEU A 1 3580 ? 102.877 81.040  56.482  1.00 6.45   ? 3580 LEU A C     1 
ATOM   14925 O  O     . LEU A 1 3580 ? 103.085 79.898  56.901  1.00 10.07  ? 3580 LEU A O     1 
ATOM   14926 C  CB    . LEU A 1 3580 ? 100.554 81.578  57.201  1.00 5.39   ? 3580 LEU A CB    1 
ATOM   14927 C  CG    . LEU A 1 3580 ? 99.587  82.285  58.147  1.00 6.44   ? 3580 LEU A CG    1 
ATOM   14928 C  CD1   . LEU A 1 3580 ? 98.161  81.959  57.765  1.00 8.14   ? 3580 LEU A CD1   1 
ATOM   14929 C  CD2   . LEU A 1 3580 ? 99.864  81.893  59.585  1.00 4.48   ? 3580 LEU A CD2   1 
ATOM   14930 N  N     . LYS A 1 3581 ? 103.346 81.472  55.315  1.00 7.44   ? 3581 LYS A N     1 
ATOM   14931 C  CA    . LYS A 1 3581 ? 104.214 80.635  54.497  1.00 8.34   ? 3581 LYS A CA    1 
ATOM   14932 C  C     . LYS A 1 3581 ? 105.697 80.861  54.784  1.00 9.91   ? 3581 LYS A C     1 
ATOM   14933 O  O     . LYS A 1 3581 ? 106.467 79.897  54.838  1.00 10.20  ? 3581 LYS A O     1 
ATOM   14934 C  CB    . LYS A 1 3581 ? 103.931 80.883  53.013  1.00 8.62   ? 3581 LYS A CB    1 
ATOM   14935 C  CG    . LYS A 1 3581 ? 104.883 80.168  52.073  1.00 12.36  ? 3581 LYS A CG    1 
ATOM   14936 C  CD    . LYS A 1 3581 ? 105.254 81.044  50.892  1.00 18.79  ? 3581 LYS A CD    1 
ATOM   14937 C  CE    . LYS A 1 3581 ? 106.097 80.279  49.886  1.00 29.86  ? 3581 LYS A CE    1 
ATOM   14938 N  NZ    . LYS A 1 3581 ? 106.569 81.153  48.778  1.00 24.41  ? 3581 LYS A NZ    1 
ATOM   14939 N  N     . ARG A 1 3582 ? 106.115 82.113  54.982  1.00 8.45   ? 3582 ARG A N     1 
ATOM   14940 C  CA    . ARG A 1 3582 ? 107.529 82.463  55.064  1.00 8.91   ? 3582 ARG A CA    1 
ATOM   14941 C  C     . ARG A 1 3582 ? 108.013 82.696  56.493  1.00 8.28   ? 3582 ARG A C     1 
ATOM   14942 O  O     . ARG A 1 3582 ? 109.089 83.272  56.685  1.00 11.08  ? 3582 ARG A O     1 
ATOM   14943 C  CB    . ARG A 1 3582 ? 107.813 83.706  54.219  1.00 8.76   ? 3582 ARG A CB    1 
ATOM   14944 C  CG    . ARG A 1 3582 ? 107.529 83.553  52.738  1.00 11.11  ? 3582 ARG A CG    1 
ATOM   14945 C  CD    . ARG A 1 3582 ? 107.738 84.876  52.013  1.00 11.56  ? 3582 ARG A CD    1 
ATOM   14946 N  NE    . ARG A 1 3582 ? 107.608 84.759  50.565  1.00 20.28  ? 3582 ARG A NE    1 
ATOM   14947 C  CZ    . ARG A 1 3582 ? 108.445 84.091  49.782  1.00 20.23  ? 3582 ARG A CZ    1 
ATOM   14948 N  NH1   . ARG A 1 3582 ? 109.517 83.487  50.267  1.00 16.51  ? 3582 ARG A NH1   1 
ATOM   14949 N  NH2   . ARG A 1 3582 ? 108.205 84.036  48.475  1.00 22.11  ? 3582 ARG A NH2   1 
ATOM   14950 N  N     . PHE A 1 3583 ? 107.245 82.275  57.494  1.00 6.93   ? 3583 PHE A N     1 
ATOM   14951 C  CA    . PHE A 1 3583 ? 107.550 82.622  58.876  1.00 6.26   ? 3583 PHE A CA    1 
ATOM   14952 C  C     . PHE A 1 3583 ? 108.857 81.989  59.343  1.00 7.38   ? 3583 PHE A C     1 
ATOM   14953 O  O     . PHE A 1 3583 ? 109.214 80.876  58.948  1.00 10.26  ? 3583 PHE A O     1 
ATOM   14954 C  CB    . PHE A 1 3583 ? 106.411 82.182  59.797  1.00 6.79   ? 3583 PHE A CB    1 
ATOM   14955 C  CG    . PHE A 1 3583 ? 106.196 80.696  59.827  1.00 6.40   ? 3583 PHE A CG    1 
ATOM   14956 C  CD1   . PHE A 1 3583 ? 105.342 80.091  58.924  1.00 6.63   ? 3583 PHE A CD1   1 
ATOM   14957 C  CD2   . PHE A 1 3583 ? 106.843 79.905  60.763  1.00 6.50   ? 3583 PHE A CD2   1 
ATOM   14958 C  CE1   . PHE A 1 3583 ? 105.141 78.728  58.948  1.00 8.15   ? 3583 PHE A CE1   1 
ATOM   14959 C  CE2   . PHE A 1 3583 ? 106.646 78.543  60.790  1.00 6.99   ? 3583 PHE A CE2   1 
ATOM   14960 C  CZ    . PHE A 1 3583 ? 105.795 77.954  59.882  1.00 7.64   ? 3583 PHE A CZ    1 
ATOM   14961 N  N     . ASN A 1 3584 ? 109.574 82.720  60.197  1.00 7.00   ? 3584 ASN A N     1 
ATOM   14962 C  CA    . ASN A 1 3584 ? 110.700 82.168  60.944  1.00 9.39   ? 3584 ASN A CA    1 
ATOM   14963 C  C     . ASN A 1 3584 ? 110.251 81.662  62.310  1.00 9.57   ? 3584 ASN A C     1 
ATOM   14964 O  O     . ASN A 1 3584 ? 110.398 80.477  62.619  1.00 14.28  ? 3584 ASN A O     1 
ATOM   14965 C  CB    . ASN A 1 3584 ? 111.810 83.217  61.103  1.00 8.10   ? 3584 ASN A CB    1 
ATOM   14966 C  CG    . ASN A 1 3584 ? 112.436 83.610  59.781  1.00 13.32  ? 3584 ASN A CG    1 
ATOM   14967 O  OD1   . ASN A 1 3584 ? 112.581 82.785  58.880  1.00 15.29  ? 3584 ASN A OD1   1 
ATOM   14968 N  ND2   . ASN A 1 3584 ? 112.826 84.874  59.665  1.00 10.35  ? 3584 ASN A ND2   1 
ATOM   14969 N  N     . ARG A 1 3585 ? 109.702 82.549  63.136  1.00 8.28   ? 3585 ARG A N     1 
ATOM   14970 C  CA    . ARG A 1 3585 ? 109.037 82.125  64.357  1.00 7.88   ? 3585 ARG A CA    1 
ATOM   14971 C  C     . ARG A 1 3585 ? 107.666 81.547  64.029  1.00 6.30   ? 3585 ARG A C     1 
ATOM   14972 O  O     . ARG A 1 3585 ? 107.007 81.960  63.072  1.00 6.99   ? 3585 ARG A O     1 
ATOM   14973 C  CB    . ARG A 1 3585 ? 108.896 83.296  65.327  1.00 6.19   ? 3585 ARG A CB    1 
ATOM   14974 C  CG    . ARG A 1 3585 ? 110.201 83.738  65.964  1.00 8.68   ? 3585 ARG A CG    1 
ATOM   14975 C  CD    . ARG A 1 3585 ? 109.992 84.975  66.816  1.00 7.73   ? 3585 ARG A CD    1 
ATOM   14976 N  NE    . ARG A 1 3585 ? 109.561 86.109  66.007  1.00 6.08   ? 3585 ARG A NE    1 
ATOM   14977 C  CZ    . ARG A 1 3585 ? 109.232 87.297  66.492  1.00 5.96   ? 3585 ARG A CZ    1 
ATOM   14978 N  NH1   . ARG A 1 3585 ? 109.266 87.548  67.791  1.00 6.53   ? 3585 ARG A NH1   1 
ATOM   14979 N  NH2   . ARG A 1 3585 ? 108.857 88.259  65.654  1.00 5.29   ? 3585 ARG A NH2   1 
ATOM   14980 N  N     . TYR A 1 3586 ? 107.241 80.580  64.835  1.00 6.18   ? 3586 TYR A N     1 
ATOM   14981 C  CA    . TYR A 1 3586 ? 105.978 79.909  64.576  1.00 6.91   ? 3586 TYR A CA    1 
ATOM   14982 C  C     . TYR A 1 3586 ? 104.826 80.906  64.679  1.00 6.27   ? 3586 TYR A C     1 
ATOM   14983 O  O     . TYR A 1 3586 ? 104.788 81.721  65.608  1.00 6.40   ? 3586 TYR A O     1 
ATOM   14984 C  CB    . TYR A 1 3586 ? 105.776 78.754  65.555  1.00 6.62   ? 3586 TYR A CB    1 
ATOM   14985 C  CG    . TYR A 1 3586 ? 106.709 77.591  65.314  1.00 8.22   ? 3586 TYR A CG    1 
ATOM   14986 C  CD1   . TYR A 1 3586 ? 106.613 76.827  64.158  1.00 7.73   ? 3586 TYR A CD1   1 
ATOM   14987 C  CD2   . TYR A 1 3586 ? 107.687 77.256  66.241  1.00 7.73   ? 3586 TYR A CD2   1 
ATOM   14988 C  CE1   . TYR A 1 3586 ? 107.464 75.764  63.934  1.00 8.43   ? 3586 TYR A CE1   1 
ATOM   14989 C  CE2   . TYR A 1 3586 ? 108.541 76.194  66.025  1.00 7.29   ? 3586 TYR A CE2   1 
ATOM   14990 C  CZ    . TYR A 1 3586 ? 108.425 75.451  64.870  1.00 8.80   ? 3586 TYR A CZ    1 
ATOM   14991 O  OH    . TYR A 1 3586 ? 109.275 74.393  64.650  1.00 12.18  ? 3586 TYR A OH    1 
ATOM   14992 N  N     . PRO A 1 3587 ? 103.877 80.874  63.746  1.00 5.91   ? 3587 PRO A N     1 
ATOM   14993 C  CA    . PRO A 1 3587 ? 102.860 81.929  63.695  1.00 5.18   ? 3587 PRO A CA    1 
ATOM   14994 C  C     . PRO A 1 3587 ? 101.817 81.781  64.791  1.00 6.21   ? 3587 PRO A C     1 
ATOM   14995 O  O     . PRO A 1 3587 ? 101.440 80.672  65.174  1.00 6.09   ? 3587 PRO A O     1 
ATOM   14996 C  CB    . PRO A 1 3587 ? 102.230 81.749  62.307  1.00 5.62   ? 3587 PRO A CB    1 
ATOM   14997 C  CG    . PRO A 1 3587 ? 103.163 80.834  61.560  1.00 6.86   ? 3587 PRO A CG    1 
ATOM   14998 C  CD    . PRO A 1 3587 ? 103.757 79.953  62.607  1.00 5.30   ? 3587 PRO A CD    1 
ATOM   14999 N  N     . LEU A 1 3588 ? 101.352 82.922  65.291  1.00 6.11   ? 3588 LEU A N     1 
ATOM   15000 C  CA    . LEU A 1 3588 ? 100.175 82.999  66.145  1.00 6.26   ? 3588 LEU A CA    1 
ATOM   15001 C  C     . LEU A 1 3588 ? 99.084  83.717  65.361  1.00 5.57   ? 3588 LEU A C     1 
ATOM   15002 O  O     . LEU A 1 3588 ? 99.263  84.872  64.961  1.00 4.32   ? 3588 LEU A O     1 
ATOM   15003 C  CB    . LEU A 1 3588 ? 100.490 83.729  67.453  1.00 6.36   ? 3588 LEU A CB    1 
ATOM   15004 C  CG    . LEU A 1 3588 ? 99.575  83.485  68.658  1.00 6.40   ? 3588 LEU A CG    1 
ATOM   15005 C  CD1   . LEU A 1 3588 ? 100.297 83.842  69.946  1.00 7.20   ? 3588 LEU A CD1   1 
ATOM   15006 C  CD2   . LEU A 1 3588 ? 98.275  84.273  68.550  1.00 4.91   ? 3588 LEU A CD2   1 
ATOM   15007 N  N     . ILE A 1 3589 ? 97.962  83.036  65.140  1.00 5.82   ? 3589 ILE A N     1 
ATOM   15008 C  CA    . ILE A 1 3589 ? 96.883  83.546  64.299  1.00 6.05   ? 3589 ILE A CA    1 
ATOM   15009 C  C     . ILE A 1 3589 ? 95.781  84.125  65.172  1.00 6.35   ? 3589 ILE A C     1 
ATOM   15010 O  O     . ILE A 1 3589 ? 95.320  83.478  66.120  1.00 8.45   ? 3589 ILE A O     1 
ATOM   15011 C  CB    . ILE A 1 3589 ? 96.327  82.451  63.373  1.00 6.85   ? 3589 ILE A CB    1 
ATOM   15012 C  CG1   . ILE A 1 3589 ? 97.394  81.997  62.377  1.00 7.46   ? 3589 ILE A CG1   1 
ATOM   15013 C  CG2   . ILE A 1 3589 ? 95.089  82.945  62.653  1.00 7.29   ? 3589 ILE A CG2   1 
ATOM   15014 C  CD1   . ILE A 1 3589 ? 97.046  80.718  61.647  1.00 9.99   ? 3589 ILE A CD1   1 
ATOM   15015 N  N     . ILE A 1 3590 ? 95.363  85.345  64.852  1.00 7.00   ? 3590 ILE A N     1 
ATOM   15016 C  CA    . ILE A 1 3590 ? 94.227  86.001  65.486  1.00 8.99   ? 3590 ILE A CA    1 
ATOM   15017 C  C     . ILE A 1 3590 ? 93.145  86.152  64.426  1.00 11.15  ? 3590 ILE A C     1 
ATOM   15018 O  O     . ILE A 1 3590 ? 93.295  86.935  63.480  1.00 10.94  ? 3590 ILE A O     1 
ATOM   15019 C  CB    . ILE A 1 3590 ? 94.618  87.359  66.085  1.00 9.74   ? 3590 ILE A CB    1 
ATOM   15020 C  CG1   . ILE A 1 3590 ? 95.727  87.184  67.124  1.00 10.87  ? 3590 ILE A CG1   1 
ATOM   15021 C  CG2   . ILE A 1 3590 ? 93.410  88.047  66.693  1.00 12.77  ? 3590 ILE A CG2   1 
ATOM   15022 C  CD1   . ILE A 1 3590 ? 96.270  88.487  67.658  1.00 11.22  ? 3590 ILE A CD1   1 
ATOM   15023 N  N     . ASP A 1 3591 ? 92.055  85.402  64.573  1.00 13.54  ? 3591 ASP A N     1 
ATOM   15024 C  CA    . ASP A 1 3591 ? 90.950  85.433  63.617  1.00 16.99  ? 3591 ASP A CA    1 
ATOM   15025 C  C     . ASP A 1 3591 ? 89.640  85.200  64.359  1.00 16.82  ? 3591 ASP A C     1 
ATOM   15026 O  O     . ASP A 1 3591 ? 89.263  84.046  64.617  1.00 20.57  ? 3591 ASP A O     1 
ATOM   15027 C  CB    . ASP A 1 3591 ? 91.145  84.394  62.515  1.00 18.38  ? 3591 ASP A CB    1 
ATOM   15028 C  CG    . ASP A 1 3591 ? 90.183  84.581  61.360  1.00 25.29  ? 3591 ASP A CG    1 
ATOM   15029 O  OD1   . ASP A 1 3591 ? 89.562  85.661  61.268  1.00 25.76  ? 3591 ASP A OD1   1 
ATOM   15030 O  OD2   . ASP A 1 3591 ? 90.048  83.648  60.543  1.00 26.50  ? 3591 ASP A OD2   1 
ATOM   15031 N  N     . PRO A 1 3592 ? 88.921  86.265  64.720  1.00 18.54  ? 3592 PRO A N     1 
ATOM   15032 C  CA    . PRO A 1 3592 ? 87.613  86.068  65.365  1.00 20.29  ? 3592 PRO A CA    1 
ATOM   15033 C  C     . PRO A 1 3592 ? 86.615  85.339  64.482  1.00 21.18  ? 3592 PRO A C     1 
ATOM   15034 O  O     . PRO A 1 3592 ? 85.818  84.540  64.991  1.00 22.53  ? 3592 PRO A O     1 
ATOM   15035 C  CB    . PRO A 1 3592 ? 87.156  87.499  65.682  1.00 18.42  ? 3592 PRO A CB    1 
ATOM   15036 C  CG    . PRO A 1 3592 ? 87.982  88.381  64.811  1.00 21.32  ? 3592 PRO A CG    1 
ATOM   15037 C  CD    . PRO A 1 3592 ? 89.280  87.686  64.593  1.00 19.54  ? 3592 PRO A CD    1 
ATOM   15038 N  N     . SER A 1 3593 ? 86.648  85.576  63.168  1.00 21.91  ? 3593 SER A N     1 
ATOM   15039 C  CA    . SER A 1 3593 ? 85.767  84.845  62.263  1.00 26.75  ? 3593 SER A CA    1 
ATOM   15040 C  C     . SER A 1 3593 ? 86.218  83.401  62.096  1.00 27.59  ? 3593 SER A C     1 
ATOM   15041 O  O     . SER A 1 3593 ? 85.398  82.520  61.809  1.00 29.69  ? 3593 SER A O     1 
ATOM   15042 C  CB    . SER A 1 3593 ? 85.704  85.550  60.907  1.00 25.72  ? 3593 SER A CB    1 
ATOM   15043 O  OG    . SER A 1 3593 ? 86.859  85.272  60.141  1.00 31.82  ? 3593 SER A OG    1 
ATOM   15044 N  N     . GLY A 1 3594 ? 87.509  83.144  62.259  1.00 27.64  ? 3594 GLY A N     1 
ATOM   15045 C  CA    . GLY A 1 3594 ? 88.018  81.796  62.292  1.00 25.79  ? 3594 GLY A CA    1 
ATOM   15046 C  C     . GLY A 1 3594 ? 88.287  81.158  60.947  1.00 27.71  ? 3594 GLY A C     1 
ATOM   15047 O  O     . GLY A 1 3594 ? 88.689  79.988  60.911  1.00 33.86  ? 3594 GLY A O     1 
ATOM   15048 N  N     . GLN A 1 3595 ? 88.104  81.887  59.842  1.00 29.65  ? 3595 GLN A N     1 
ATOM   15049 C  CA    . GLN A 1 3595 ? 88.361  81.325  58.516  1.00 28.14  ? 3595 GLN A CA    1 
ATOM   15050 C  C     . GLN A 1 3595 ? 89.834  80.979  58.323  1.00 25.87  ? 3595 GLN A C     1 
ATOM   15051 O  O     . GLN A 1 3595 ? 90.174  80.154  57.465  1.00 27.23  ? 3595 GLN A O     1 
ATOM   15052 C  CB    . GLN A 1 3595 ? 87.906  82.308  57.437  1.00 34.42  ? 3595 GLN A CB    1 
ATOM   15053 C  CG    . GLN A 1 3595 ? 86.650  83.089  57.797  1.00 43.49  ? 3595 GLN A CG    1 
ATOM   15054 C  CD    . GLN A 1 3595 ? 85.951  83.654  56.584  1.00 53.49  ? 3595 GLN A CD    1 
ATOM   15055 O  OE1   . GLN A 1 3595 ? 86.507  84.488  55.865  1.00 49.96  ? 3595 GLN A OE1   1 
ATOM   15056 N  NE2   . GLN A 1 3595 ? 84.711  83.235  56.369  1.00 52.61  ? 3595 GLN A NE2   1 
ATOM   15057 N  N     . ALA A 1 3596 ? 90.721  81.613  59.094  1.00 25.83  ? 3596 ALA A N     1 
ATOM   15058 C  CA    . ALA A 1 3596 ? 92.135  81.258  59.048  1.00 17.14  ? 3596 ALA A CA    1 
ATOM   15059 C  C     . ALA A 1 3596 ? 92.350  79.812  59.472  1.00 19.64  ? 3596 ALA A C     1 
ATOM   15060 O  O     . ALA A 1 3596 ? 93.250  79.134  58.961  1.00 20.99  ? 3596 ALA A O     1 
ATOM   15061 C  CB    . ALA A 1 3596 ? 92.937  82.203  59.940  1.00 13.40  ? 3596 ALA A CB    1 
ATOM   15062 N  N     . THR A 1 3597 ? 91.536  79.328  60.412  1.00 19.75  ? 3597 THR A N     1 
ATOM   15063 C  CA    . THR A 1 3597 ? 91.642  77.942  60.852  1.00 24.27  ? 3597 THR A CA    1 
ATOM   15064 C  C     . THR A 1 3597 ? 91.356  76.980  59.706  1.00 27.63  ? 3597 THR A C     1 
ATOM   15065 O  O     . THR A 1 3597 ? 92.146  76.066  59.432  1.00 29.53  ? 3597 THR A O     1 
ATOM   15066 C  CB    . THR A 1 3597 ? 90.682  77.698  62.016  1.00 33.23  ? 3597 THR A CB    1 
ATOM   15067 O  OG1   . THR A 1 3597 ? 91.017  78.565  63.108  1.00 33.29  ? 3597 THR A OG1   1 
ATOM   15068 C  CG2   . THR A 1 3597 ? 90.745  76.257  62.477  1.00 35.00  ? 3597 THR A CG2   1 
ATOM   15069 N  N     . GLU A 1 3598 ? 90.234  77.183  59.009  1.00 25.26  ? 3598 GLU A N     1 
ATOM   15070 C  CA    . GLU A 1 3598 ? 89.954  76.359  57.838  1.00 25.16  ? 3598 GLU A CA    1 
ATOM   15071 C  C     . GLU A 1 3598 ? 91.012  76.529  56.754  1.00 24.14  ? 3598 GLU A C     1 
ATOM   15072 O  O     . GLU A 1 3598 ? 91.349  75.561  56.066  1.00 29.04  ? 3598 GLU A O     1 
ATOM   15073 C  CB    . GLU A 1 3598 ? 88.547  76.621  57.282  1.00 32.36  ? 3598 GLU A CB    1 
ATOM   15074 C  CG    . GLU A 1 3598 ? 87.375  76.157  58.177  1.00 46.20  ? 3598 GLU A CG    1 
ATOM   15075 C  CD    . GLU A 1 3598 ? 86.967  77.103  59.279  1.00 46.66  ? 3598 GLU A CD    1 
ATOM   15076 O  OE1   . GLU A 1 3598 ? 87.528  78.205  59.374  1.00 48.09  ? 3598 GLU A OE1   1 
ATOM   15077 O  OE2   . GLU A 1 3598 ? 86.071  76.730  60.061  1.00 49.31  ? 3598 GLU A OE2   1 
ATOM   15078 N  N     . PHE A 1 3599 ? 91.549  77.739  56.576  1.00 20.69  ? 3599 PHE A N     1 
ATOM   15079 C  CA    . PHE A 1 3599 ? 92.584  77.905  55.558  1.00 18.47  ? 3599 PHE A CA    1 
ATOM   15080 C  C     . PHE A 1 3599 ? 93.810  77.061  55.885  1.00 17.88  ? 3599 PHE A C     1 
ATOM   15081 O  O     . PHE A 1 3599 ? 94.369  76.399  55.003  1.00 17.89  ? 3599 PHE A O     1 
ATOM   15082 C  CB    . PHE A 1 3599 ? 92.982  79.373  55.415  1.00 17.16  ? 3599 PHE A CB    1 
ATOM   15083 C  CG    . PHE A 1 3599 ? 94.242  79.578  54.611  1.00 16.49  ? 3599 PHE A CG    1 
ATOM   15084 C  CD1   . PHE A 1 3599 ? 94.212  79.478  53.229  1.00 16.18  ? 3599 PHE A CD1   1 
ATOM   15085 C  CD2   . PHE A 1 3599 ? 95.452  79.858  55.227  1.00 14.44  ? 3599 PHE A CD2   1 
ATOM   15086 C  CE1   . PHE A 1 3599 ? 95.360  79.655  52.479  1.00 15.98  ? 3599 PHE A CE1   1 
ATOM   15087 C  CE2   . PHE A 1 3599 ? 96.602  80.040  54.481  1.00 11.58  ? 3599 PHE A CE2   1 
ATOM   15088 C  CZ    . PHE A 1 3599 ? 96.556  79.938  53.107  1.00 13.41  ? 3599 PHE A CZ    1 
ATOM   15089 N  N     . ILE A 1 3600 ? 94.234  77.067  57.152  1.00 18.59  ? 3600 ILE A N     1 
ATOM   15090 C  CA    . ILE A 1 3600 ? 95.392  76.274  57.562  1.00 18.20  ? 3600 ILE A CA    1 
ATOM   15091 C  C     . ILE A 1 3600 ? 95.109  74.785  57.401  1.00 19.29  ? 3600 ILE A C     1 
ATOM   15092 O  O     . ILE A 1 3600 ? 95.946  74.029  56.885  1.00 20.63  ? 3600 ILE A O     1 
ATOM   15093 C  CB    . ILE A 1 3600 ? 95.787  76.620  59.010  1.00 18.55  ? 3600 ILE A CB    1 
ATOM   15094 C  CG1   . ILE A 1 3600 ? 96.415  78.011  59.083  1.00 15.36  ? 3600 ILE A CG1   1 
ATOM   15095 C  CG2   . ILE A 1 3600 ? 96.744  75.582  59.572  1.00 16.32  ? 3600 ILE A CG2   1 
ATOM   15096 C  CD1   . ILE A 1 3600 ? 97.626  78.179  58.199  1.00 14.57  ? 3600 ILE A CD1   1 
ATOM   15097 N  N     . MET A 1 3601 ? 93.929  74.341  57.840  1.00 19.73  ? 3601 MET A N     1 
ATOM   15098 C  CA    . MET A 1 3601 ? 93.588  72.925  57.745  1.00 20.99  ? 3601 MET A CA    1 
ATOM   15099 C  C     . MET A 1 3601 ? 93.529  72.469  56.293  1.00 22.97  ? 3601 MET A C     1 
ATOM   15100 O  O     . MET A 1 3601 ? 93.948  71.352  55.966  1.00 25.78  ? 3601 MET A O     1 
ATOM   15101 C  CB    . MET A 1 3601 ? 92.256  72.662  58.445  1.00 20.75  ? 3601 MET A CB    1 
ATOM   15102 C  CG    . MET A 1 3601 ? 92.291  72.878  59.949  1.00 25.21  ? 3601 MET A CG    1 
ATOM   15103 S  SD    . MET A 1 3601 ? 93.643  72.018  60.772  1.00 36.74  ? 3601 MET A SD    1 
ATOM   15104 C  CE    . MET A 1 3601 ? 92.890  70.423  61.081  1.00 20.95  ? 3601 MET A CE    1 
ATOM   15105 N  N     . ASN A 1 3602 ? 93.009  73.322  55.408  1.00 21.42  ? 3602 ASN A N     1 
ATOM   15106 C  CA    . ASN A 1 3602 ? 92.942  72.983  53.993  1.00 22.09  ? 3602 ASN A CA    1 
ATOM   15107 C  C     . ASN A 1 3602 ? 94.329  72.959  53.370  1.00 21.33  ? 3602 ASN A C     1 
ATOM   15108 O  O     . ASN A 1 3602 ? 94.631  72.089  52.545  1.00 28.36  ? 3602 ASN A O     1 
ATOM   15109 C  CB    . ASN A 1 3602 ? 92.041  73.979  53.265  1.00 22.75  ? 3602 ASN A CB    1 
ATOM   15110 C  CG    . ASN A 1 3602 ? 90.575  73.785  53.596  1.00 28.28  ? 3602 ASN A CG    1 
ATOM   15111 O  OD1   . ASN A 1 3602 ? 90.176  72.745  54.116  1.00 34.81  ? 3602 ASN A OD1   1 
ATOM   15112 N  ND2   . ASN A 1 3602 ? 89.764  74.795  53.303  1.00 27.09  ? 3602 ASN A ND2   1 
ATOM   15113 N  N     . GLU A 1 3603 ? 95.187  73.907  53.751  1.00 18.61  ? 3603 GLU A N     1 
ATOM   15114 C  CA    . GLU A 1 3603 ? 96.549  73.940  53.244  1.00 20.23  ? 3603 GLU A CA    1 
ATOM   15115 C  C     . GLU A 1 3603 ? 97.387  72.769  53.736  1.00 20.78  ? 3603 GLU A C     1 
ATOM   15116 O  O     . GLU A 1 3603 ? 98.373  72.419  53.079  1.00 19.07  ? 3603 GLU A O     1 
ATOM   15117 C  CB    . GLU A 1 3603 ? 97.220  75.255  53.644  1.00 19.11  ? 3603 GLU A CB    1 
ATOM   15118 C  CG    . GLU A 1 3603 ? 96.999  76.389  52.661  1.00 21.44  ? 3603 GLU A CG    1 
ATOM   15119 C  CD    . GLU A 1 3603 ? 97.662  76.142  51.323  1.00 30.98  ? 3603 GLU A CD    1 
ATOM   15120 O  OE1   . GLU A 1 3603 ? 98.866  75.812  51.307  1.00 34.68  ? 3603 GLU A OE1   1 
ATOM   15121 O  OE2   . GLU A 1 3603 ? 96.980  76.279  50.287  1.00 28.17  ? 3603 GLU A OE2   1 
ATOM   15122 N  N     . TYR A 1 3604 ? 97.025  72.156  54.867  1.00 21.70  ? 3604 TYR A N     1 
ATOM   15123 C  CA    . TYR A 1 3604 ? 97.839  71.087  55.432  1.00 20.98  ? 3604 TYR A CA    1 
ATOM   15124 C  C     . TYR A 1 3604 ? 97.088  69.762  55.549  1.00 26.31  ? 3604 TYR A C     1 
ATOM   15125 O  O     . TYR A 1 3604 ? 97.452  68.931  56.387  1.00 30.84  ? 3604 TYR A O     1 
ATOM   15126 C  CB    . TYR A 1 3604 ? 98.390  71.505  56.798  1.00 19.11  ? 3604 TYR A CB    1 
ATOM   15127 C  CG    . TYR A 1 3604 ? 99.484  72.546  56.722  1.00 20.02  ? 3604 TYR A CG    1 
ATOM   15128 C  CD1   . TYR A 1 3604 ? 99.179  73.898  56.641  1.00 17.71  ? 3604 TYR A CD1   1 
ATOM   15129 C  CD2   . TYR A 1 3604 ? 100.823 72.177  56.734  1.00 18.71  ? 3604 TYR A CD2   1 
ATOM   15130 C  CE1   . TYR A 1 3604 ? 100.174 74.853  56.571  1.00 17.62  ? 3604 TYR A CE1   1 
ATOM   15131 C  CE2   . TYR A 1 3604 ? 101.826 73.126  56.667  1.00 16.03  ? 3604 TYR A CE2   1 
ATOM   15132 C  CZ    . TYR A 1 3604 ? 101.496 74.462  56.584  1.00 20.00  ? 3604 TYR A CZ    1 
ATOM   15133 O  OH    . TYR A 1 3604 ? 102.491 75.408  56.515  1.00 25.09  ? 3604 TYR A OH    1 
ATOM   15134 N  N     . LYS A 1 3605 ? 96.049  69.537  54.736  1.00 28.11  ? 3605 LYS A N     1 
ATOM   15135 C  CA    . LYS A 1 3605 ? 95.402  68.226  54.743  1.00 25.68  ? 3605 LYS A CA    1 
ATOM   15136 C  C     . LYS A 1 3605 ? 96.346  67.136  54.251  1.00 31.43  ? 3605 LYS A C     1 
ATOM   15137 O  O     . LYS A 1 3605 ? 96.395  66.045  54.830  1.00 35.43  ? 3605 LYS A O     1 
ATOM   15138 C  CB    . LYS A 1 3605 ? 94.133  68.224  53.889  1.00 26.47  ? 3605 LYS A CB    1 
ATOM   15139 C  CG    . LYS A 1 3605 ? 92.835  68.305  54.679  1.00 32.29  ? 3605 LYS A CG    1 
ATOM   15140 C  CD    . LYS A 1 3605 ? 91.634  68.494  53.760  1.00 37.37  ? 3605 LYS A CD    1 
ATOM   15141 C  CE    . LYS A 1 3605 ? 91.479  69.924  53.299  1.00 34.10  ? 3605 LYS A CE    1 
ATOM   15142 N  NZ    . LYS A 1 3605 ? 90.413  70.067  52.270  1.00 41.26  ? 3605 LYS A NZ    1 
ATOM   15143 N  N     . ASP A 1 3606 ? 97.093  67.409  53.178  1.00 28.33  ? 3606 ASP A N     1 
ATOM   15144 C  CA    . ASP A 1 3606 ? 97.957  66.386  52.595  1.00 33.33  ? 3606 ASP A CA    1 
ATOM   15145 C  C     . ASP A 1 3606 ? 99.046  65.946  53.563  1.00 36.25  ? 3606 ASP A C     1 
ATOM   15146 O  O     . ASP A 1 3606 ? 99.520  64.807  53.489  1.00 37.17  ? 3606 ASP A O     1 
ATOM   15147 C  CB    . ASP A 1 3606 ? 98.571  66.898  51.290  1.00 42.70  ? 3606 ASP A CB    1 
ATOM   15148 C  CG    . ASP A 1 3606 ? 99.359  68.184  51.475  1.00 44.56  ? 3606 ASP A CG    1 
ATOM   15149 O  OD1   . ASP A 1 3606 ? 99.388  68.720  52.602  1.00 40.13  ? 3606 ASP A OD1   1 
ATOM   15150 O  OD2   . ASP A 1 3606 ? 99.952  68.662  50.484  1.00 48.38  ? 3606 ASP A OD2   1 
ATOM   15151 N  N     . ARG A 1 3607 ? 99.451  66.827  54.474  1.00 37.37  ? 3607 ARG A N     1 
ATOM   15152 C  CA    . ARG A 1 3607 ? 100.473 66.524  55.463  1.00 31.06  ? 3607 ARG A CA    1 
ATOM   15153 C  C     . ARG A 1 3607 ? 99.884  66.112  56.807  1.00 30.41  ? 3607 ARG A C     1 
ATOM   15154 O  O     . ARG A 1 3607 ? 100.627 65.992  57.787  1.00 30.88  ? 3607 ARG A O     1 
ATOM   15155 C  CB    . ARG A 1 3607 ? 101.412 67.722  55.617  1.00 28.23  ? 3607 ARG A CB    1 
ATOM   15156 C  CG    . ARG A 1 3607 ? 102.414 67.826  54.474  1.00 31.59  ? 3607 ARG A CG    1 
ATOM   15157 C  CD    . ARG A 1 3607 ? 103.144 69.157  54.440  1.00 36.52  ? 3607 ARG A CD    1 
ATOM   15158 N  NE    . ARG A 1 3607 ? 102.269 70.242  54.013  1.00 40.88  ? 3607 ARG A NE    1 
ATOM   15159 C  CZ    . ARG A 1 3607 ? 102.653 71.503  53.872  1.00 39.38  ? 3607 ARG A CZ    1 
ATOM   15160 N  NH1   . ARG A 1 3607 ? 103.896 71.880  54.122  1.00 35.97  ? 3607 ARG A NH1   1 
ATOM   15161 N  NH2   . ARG A 1 3607 ? 101.767 72.409  53.466  1.00 28.64  ? 3607 ARG A NH2   1 
ATOM   15162 N  N     . LYS A 1 3608 ? 98.570  65.886  56.868  1.00 31.48  ? 3608 LYS A N     1 
ATOM   15163 C  CA    . LYS A 1 3608 ? 97.899  65.308  58.034  1.00 30.32  ? 3608 LYS A CA    1 
ATOM   15164 C  C     . LYS A 1 3608 ? 98.059  66.193  59.273  1.00 24.97  ? 3608 LYS A C     1 
ATOM   15165 O  O     . LYS A 1 3608 ? 98.649  65.802  60.282  1.00 30.33  ? 3608 LYS A O     1 
ATOM   15166 C  CB    . LYS A 1 3608 ? 98.406  63.886  58.301  1.00 37.62  ? 3608 LYS A CB    1 
ATOM   15167 C  CG    . LYS A 1 3608 ? 98.093  62.900  57.188  1.00 41.31  ? 3608 LYS A CG    1 
ATOM   15168 C  CD    . LYS A 1 3608 ? 98.562  61.500  57.546  1.00 55.84  ? 3608 LYS A CD    1 
ATOM   15169 C  CE    . LYS A 1 3608 ? 100.080 61.410  57.534  1.00 54.35  ? 3608 LYS A CE    1 
ATOM   15170 N  NZ    . LYS A 1 3608 ? 100.637 61.598  56.167  1.00 49.73  ? 3608 LYS A NZ    1 
ATOM   15171 N  N     . ILE A 1 3609 ? 97.517  67.402  59.176  1.00 20.93  ? 3609 ILE A N     1 
ATOM   15172 C  CA    . ILE A 1 3609 ? 97.524  68.333  60.298  1.00 21.07  ? 3609 ILE A CA    1 
ATOM   15173 C  C     . ILE A 1 3609 ? 96.447  67.928  61.296  1.00 22.30  ? 3609 ILE A C     1 
ATOM   15174 O  O     . ILE A 1 3609 ? 95.362  67.471  60.918  1.00 24.55  ? 3609 ILE A O     1 
ATOM   15175 C  CB    . ILE A 1 3609 ? 97.327  69.778  59.804  1.00 19.08  ? 3609 ILE A CB    1 
ATOM   15176 C  CG1   . ILE A 1 3609 ? 97.428  70.762  60.972  1.00 14.13  ? 3609 ILE A CG1   1 
ATOM   15177 C  CG2   . ILE A 1 3609 ? 95.998  69.926  59.077  1.00 16.26  ? 3609 ILE A CG2   1 
ATOM   15178 C  CD1   . ILE A 1 3609 ? 97.541  72.201  60.544  1.00 14.19  ? 3609 ILE A CD1   1 
ATOM   15179 N  N     . THR A 1 3610 ? 96.755  68.077  62.582  1.00 20.09  ? 3610 THR A N     1 
ATOM   15180 C  CA    . THR A 1 3610 ? 95.842  67.732  63.663  1.00 19.11  ? 3610 THR A CA    1 
ATOM   15181 C  C     . THR A 1 3610 ? 95.421  68.999  64.393  1.00 17.66  ? 3610 THR A C     1 
ATOM   15182 O  O     . THR A 1 3610 ? 96.269  69.822  64.754  1.00 15.50  ? 3610 THR A O     1 
ATOM   15183 C  CB    . THR A 1 3610 ? 96.498  66.752  64.642  1.00 20.95  ? 3610 THR A CB    1 
ATOM   15184 O  OG1   . THR A 1 3610 ? 96.840  65.542  63.955  1.00 28.37  ? 3610 THR A OG1   1 
ATOM   15185 C  CG2   . THR A 1 3610 ? 95.560  66.430  65.794  1.00 24.11  ? 3610 THR A CG2   1 
ATOM   15186 N  N     . ARG A 1 3611 ? 94.116  69.154  64.608  1.00 19.24  ? 3611 ARG A N     1 
ATOM   15187 C  CA    . ARG A 1 3611 ? 93.590  70.251  65.408  1.00 18.05  ? 3611 ARG A CA    1 
ATOM   15188 C  C     . ARG A 1 3611 ? 93.552  69.838  66.873  1.00 19.49  ? 3611 ARG A C     1 
ATOM   15189 O  O     . ARG A 1 3611 ? 93.089  68.742  67.204  1.00 26.98  ? 3611 ARG A O     1 
ATOM   15190 C  CB    . ARG A 1 3611 ? 92.186  70.652  64.952  1.00 24.00  ? 3611 ARG A CB    1 
ATOM   15191 C  CG    . ARG A 1 3611 ? 91.648  71.872  65.692  1.00 25.97  ? 3611 ARG A CG    1 
ATOM   15192 C  CD    . ARG A 1 3611 ? 90.261  72.295  65.228  1.00 35.42  ? 3611 ARG A CD    1 
ATOM   15193 N  NE    . ARG A 1 3611 ? 90.216  72.744  63.842  1.00 41.64  ? 3611 ARG A NE    1 
ATOM   15194 C  CZ    . ARG A 1 3611 ? 89.585  72.099  62.870  1.00 48.45  ? 3611 ARG A CZ    1 
ATOM   15195 N  NH1   . ARG A 1 3611 ? 88.961  70.955  63.092  1.00 47.45  ? 3611 ARG A NH1   1 
ATOM   15196 N  NH2   . ARG A 1 3611 ? 89.573  72.620  61.647  1.00 47.07  ? 3611 ARG A NH2   1 
ATOM   15197 N  N     . THR A 1 3612 ? 94.039  70.716  67.745  1.00 16.85  ? 3612 THR A N     1 
ATOM   15198 C  CA    . THR A 1 3612 ? 93.975  70.493  69.181  1.00 20.09  ? 3612 THR A CA    1 
ATOM   15199 C  C     . THR A 1 3612 ? 93.891  71.848  69.871  1.00 16.27  ? 3612 THR A C     1 
ATOM   15200 O  O     . THR A 1 3612 ? 93.889  72.898  69.223  1.00 15.53  ? 3612 THR A O     1 
ATOM   15201 C  CB    . THR A 1 3612 ? 95.177  69.678  69.674  1.00 23.32  ? 3612 THR A CB    1 
ATOM   15202 O  OG1   . THR A 1 3612 ? 94.997  69.344  71.056  1.00 24.64  ? 3612 THR A OG1   1 
ATOM   15203 C  CG2   . THR A 1 3612 ? 96.463  70.468  69.512  1.00 14.34  ? 3612 THR A CG2   1 
ATOM   15204 N  N     . SER A 1 3613 ? 93.807  71.820  71.198  1.00 16.78  ? 3613 SER A N     1 
ATOM   15205 C  CA    . SER A 1 3613 ? 93.709  73.036  71.988  1.00 16.37  ? 3613 SER A CA    1 
ATOM   15206 C  C     . SER A 1 3613 ? 94.558  72.890  73.242  1.00 20.12  ? 3613 SER A C     1 
ATOM   15207 O  O     . SER A 1 3613 ? 94.833  71.780  73.703  1.00 22.26  ? 3613 SER A O     1 
ATOM   15208 C  CB    . SER A 1 3613 ? 92.254  73.349  72.362  1.00 15.68  ? 3613 SER A CB    1 
ATOM   15209 O  OG    . SER A 1 3613 ? 92.190  74.271  73.435  1.00 21.17  ? 3613 SER A OG    1 
ATOM   15210 N  N     . PHE A 1 3614 ? 94.976  74.034  73.790  1.00 20.33  ? 3614 PHE A N     1 
ATOM   15211 C  CA    . PHE A 1 3614 ? 95.742  74.019  75.031  1.00 17.60  ? 3614 PHE A CA    1 
ATOM   15212 C  C     . PHE A 1 3614 ? 94.926  73.455  76.186  1.00 22.67  ? 3614 PHE A C     1 
ATOM   15213 O  O     . PHE A 1 3614 ? 95.494  72.904  77.136  1.00 27.46  ? 3614 PHE A O     1 
ATOM   15214 C  CB    . PHE A 1 3614 ? 96.229  75.428  75.375  1.00 17.44  ? 3614 PHE A CB    1 
ATOM   15215 C  CG    . PHE A 1 3614 ? 97.371  75.903  74.525  1.00 18.66  ? 3614 PHE A CG    1 
ATOM   15216 C  CD1   . PHE A 1 3614 ? 98.642  75.384  74.697  1.00 15.82  ? 3614 PHE A CD1   1 
ATOM   15217 C  CD2   . PHE A 1 3614 ? 97.179  76.887  73.571  1.00 16.25  ? 3614 PHE A CD2   1 
ATOM   15218 C  CE1   . PHE A 1 3614 ? 99.696  75.824  73.921  1.00 11.39  ? 3614 PHE A CE1   1 
ATOM   15219 C  CE2   . PHE A 1 3614 ? 98.231  77.334  72.793  1.00 13.64  ? 3614 PHE A CE2   1 
ATOM   15220 C  CZ    . PHE A 1 3614 ? 99.491  76.800  72.968  1.00 11.83  ? 3614 PHE A CZ    1 
ATOM   15221 N  N     . LEU A 1 3615 ? 93.603  73.583  76.126  1.00 25.03  ? 3615 LEU A N     1 
ATOM   15222 C  CA    . LEU A 1 3615 ? 92.725  73.096  77.180  1.00 28.76  ? 3615 LEU A CA    1 
ATOM   15223 C  C     . LEU A 1 3615 ? 92.363  71.625  77.026  1.00 32.52  ? 3615 LEU A C     1 
ATOM   15224 O  O     . LEU A 1 3615 ? 91.768  71.052  77.945  1.00 35.45  ? 3615 LEU A O     1 
ATOM   15225 C  CB    . LEU A 1 3615 ? 91.443  73.934  77.223  1.00 28.64  ? 3615 LEU A CB    1 
ATOM   15226 C  CG    . LEU A 1 3615 ? 91.642  75.442  77.386  1.00 31.57  ? 3615 LEU A CG    1 
ATOM   15227 C  CD1   . LEU A 1 3615 ? 90.376  76.193  77.014  1.00 27.65  ? 3615 LEU A CD1   1 
ATOM   15228 C  CD2   . LEU A 1 3615 ? 92.068  75.775  78.807  1.00 29.89  ? 3615 LEU A CD2   1 
ATOM   15229 N  N     . ASP A 1 3616 ? 92.701  71.006  75.899  1.00 27.07  ? 3616 ASP A N     1 
ATOM   15230 C  CA    . ASP A 1 3616 ? 92.416  69.593  75.708  1.00 27.82  ? 3616 ASP A CA    1 
ATOM   15231 C  C     . ASP A 1 3616 ? 93.330  68.737  76.579  1.00 38.93  ? 3616 ASP A C     1 
ATOM   15232 O  O     . ASP A 1 3616 ? 94.480  69.092  76.852  1.00 38.91  ? 3616 ASP A O     1 
ATOM   15233 C  CB    . ASP A 1 3616 ? 92.583  69.207  74.238  1.00 28.77  ? 3616 ASP A CB    1 
ATOM   15234 C  CG    . ASP A 1 3616 ? 91.368  69.558  73.403  1.00 38.35  ? 3616 ASP A CG    1 
ATOM   15235 O  OD1   . ASP A 1 3616 ? 90.346  69.975  73.986  1.00 41.99  ? 3616 ASP A OD1   1 
ATOM   15236 O  OD2   . ASP A 1 3616 ? 91.436  69.417  72.164  1.00 37.59  ? 3616 ASP A OD2   1 
ATOM   15237 N  N     . ASP A 1 3617 ? 92.798  67.595  77.021  1.00 44.12  ? 3617 ASP A N     1 
ATOM   15238 C  CA    . ASP A 1 3617 ? 93.582  66.688  77.852  1.00 43.58  ? 3617 ASP A CA    1 
ATOM   15239 C  C     . ASP A 1 3617 ? 94.685  66.001  77.056  1.00 39.54  ? 3617 ASP A C     1 
ATOM   15240 O  O     . ASP A 1 3617 ? 95.771  65.755  77.591  1.00 42.96  ? 3617 ASP A O     1 
ATOM   15241 C  CB    . ASP A 1 3617 ? 92.668  65.646  78.497  1.00 49.83  ? 3617 ASP A CB    1 
ATOM   15242 C  CG    . ASP A 1 3617 ? 93.388  64.797  79.526  1.00 62.49  ? 3617 ASP A CG    1 
ATOM   15243 O  OD1   . ASP A 1 3617 ? 93.524  65.249  80.682  1.00 64.69  ? 3617 ASP A OD1   1 
ATOM   15244 O  OD2   . ASP A 1 3617 ? 93.817  63.676  79.179  1.00 68.43  ? 3617 ASP A OD2   1 
ATOM   15245 N  N     . ALA A 1 3618 ? 94.429  65.687  75.789  1.00 36.30  ? 3618 ALA A N     1 
ATOM   15246 C  CA    . ALA A 1 3618 ? 95.376  64.965  74.950  1.00 34.15  ? 3618 ALA A CA    1 
ATOM   15247 C  C     . ALA A 1 3618 ? 96.417  65.874  74.309  1.00 30.63  ? 3618 ALA A C     1 
ATOM   15248 O  O     . ALA A 1 3618 ? 97.323  65.368  73.634  1.00 32.06  ? 3618 ALA A O     1 
ATOM   15249 C  CB    . ALA A 1 3618 ? 94.628  64.190  73.862  1.00 31.94  ? 3618 ALA A CB    1 
ATOM   15250 N  N     . PHE A 1 3619 ? 96.324  67.191  74.532  1.00 30.87  ? 3619 PHE A N     1 
ATOM   15251 C  CA    . PHE A 1 3619 ? 97.191  68.141  73.838  1.00 24.42  ? 3619 PHE A CA    1 
ATOM   15252 C  C     . PHE A 1 3619 ? 98.656  67.747  73.946  1.00 21.30  ? 3619 PHE A C     1 
ATOM   15253 O  O     . PHE A 1 3619 ? 99.341  67.607  72.925  1.00 22.21  ? 3619 PHE A O     1 
ATOM   15254 C  CB    . PHE A 1 3619 ? 96.983  69.546  74.403  1.00 22.08  ? 3619 PHE A CB    1 
ATOM   15255 C  CG    . PHE A 1 3619 ? 98.108  70.495  74.095  1.00 21.32  ? 3619 PHE A CG    1 
ATOM   15256 C  CD1   . PHE A 1 3619 ? 98.288  70.991  72.816  1.00 20.32  ? 3619 PHE A CD1   1 
ATOM   15257 C  CD2   . PHE A 1 3619 ? 98.989  70.885  75.090  1.00 16.98  ? 3619 PHE A CD2   1 
ATOM   15258 C  CE1   . PHE A 1 3619 ? 99.327  71.860  72.535  1.00 16.57  ? 3619 PHE A CE1   1 
ATOM   15259 C  CE2   . PHE A 1 3619 ? 100.029 71.753  74.816  1.00 20.02  ? 3619 PHE A CE2   1 
ATOM   15260 C  CZ    . PHE A 1 3619 ? 100.197 72.241  73.536  1.00 16.09  ? 3619 PHE A CZ    1 
ATOM   15261 N  N     . ARG A 1 3620 ? 99.135  67.510  75.171  1.00 22.36  ? 3620 ARG A N     1 
ATOM   15262 C  CA    . ARG A 1 3620 ? 100.525 67.112  75.356  1.00 21.81  ? 3620 ARG A CA    1 
ATOM   15263 C  C     . ARG A 1 3620 ? 100.864 65.924  74.472  1.00 21.70  ? 3620 ARG A C     1 
ATOM   15264 O  O     . ARG A 1 3620 ? 101.781 66.001  73.642  1.00 23.28  ? 3620 ARG A O     1 
ATOM   15265 C  CB    . ARG A 1 3620 ? 100.777 66.767  76.824  1.00 24.60  ? 3620 ARG A CB    1 
ATOM   15266 C  CG    . ARG A 1 3620 ? 102.211 66.388  77.144  1.00 31.52  ? 3620 ARG A CG    1 
ATOM   15267 C  CD    . ARG A 1 3620 ? 103.145 67.564  76.940  1.00 32.51  ? 3620 ARG A CD    1 
ATOM   15268 N  NE    . ARG A 1 3620 ? 102.771 68.680  77.800  1.00 40.20  ? 3620 ARG A NE    1 
ATOM   15269 C  CZ    . ARG A 1 3620 ? 103.149 68.808  79.064  1.00 42.90  ? 3620 ARG A CZ    1 
ATOM   15270 N  NH1   . ARG A 1 3620 ? 103.929 67.911  79.645  1.00 40.32  ? 3620 ARG A NH1   1 
ATOM   15271 N  NH2   . ARG A 1 3620 ? 102.732 69.859  79.764  1.00 39.27  ? 3620 ARG A NH2   1 
ATOM   15272 N  N     . LYS A 1 3621 ? 100.070 64.852  74.573  1.00 21.92  ? 3621 LYS A N     1 
ATOM   15273 C  CA    . LYS A 1 3621 ? 100.278 63.694  73.715  1.00 21.61  ? 3621 LYS A CA    1 
ATOM   15274 C  C     . LYS A 1 3621 ? 100.301 64.110  72.254  1.00 18.88  ? 3621 LYS A C     1 
ATOM   15275 O  O     . LYS A 1 3621 ? 101.266 63.820  71.535  1.00 20.66  ? 3621 LYS A O     1 
ATOM   15276 C  CB    . LYS A 1 3621 ? 99.186  62.653  73.975  1.00 22.23  ? 3621 LYS A CB    1 
ATOM   15277 C  CG    . LYS A 1 3621 ? 99.379  61.315  73.268  1.00 26.05  ? 3621 LYS A CG    1 
ATOM   15278 C  CD    . LYS A 1 3621 ? 98.699  61.289  71.906  1.00 32.59  ? 3621 LYS A CD    1 
ATOM   15279 C  CE    . LYS A 1 3621 ? 98.831  59.930  71.242  1.00 40.19  ? 3621 LYS A CE    1 
ATOM   15280 N  NZ    . LYS A 1 3621 ? 98.197  59.914  69.895  1.00 47.62  ? 3621 LYS A NZ    1 
ATOM   15281 N  N     . ASN A 1 3622 ? 99.273  64.847  71.818  1.00 17.30  ? 3622 ASN A N     1 
ATOM   15282 C  CA    . ASN A 1 3622 ? 99.237  65.311  70.438  1.00 18.05  ? 3622 ASN A CA    1 
ATOM   15283 C  C     . ASN A 1 3622 ? 100.522 66.042  70.091  1.00 15.53  ? 3622 ASN A C     1 
ATOM   15284 O  O     . ASN A 1 3622 ? 101.190 65.706  69.104  1.00 16.15  ? 3622 ASN A O     1 
ATOM   15285 C  CB    . ASN A 1 3622 ? 98.025  66.216  70.218  1.00 18.84  ? 3622 ASN A CB    1 
ATOM   15286 C  CG    . ASN A 1 3622 ? 96.711  65.469  70.330  1.00 25.13  ? 3622 ASN A CG    1 
ATOM   15287 O  OD1   . ASN A 1 3622 ? 96.679  64.240  70.304  1.00 32.06  ? 3622 ASN A OD1   1 
ATOM   15288 N  ND2   . ASN A 1 3622 ? 95.618  66.211  70.460  1.00 28.79  ? 3622 ASN A ND2   1 
ATOM   15289 N  N     . LEU A 1 3623 ? 100.926 66.985  70.946  1.00 14.98  ? 3623 LEU A N     1 
ATOM   15290 C  CA    . LEU A 1 3623 ? 102.152 67.728  70.690  1.00 12.28  ? 3623 LEU A CA    1 
ATOM   15291 C  C     . LEU A 1 3623 ? 103.328 66.779  70.537  1.00 14.79  ? 3623 LEU A C     1 
ATOM   15292 O  O     . LEU A 1 3623 ? 104.070 66.854  69.549  1.00 13.21  ? 3623 LEU A O     1 
ATOM   15293 C  CB    . LEU A 1 3623 ? 102.396 68.730  71.815  1.00 11.88  ? 3623 LEU A CB    1 
ATOM   15294 C  CG    . LEU A 1 3623 ? 103.749 69.436  71.828  1.00 14.04  ? 3623 LEU A CG    1 
ATOM   15295 C  CD1   . LEU A 1 3623 ? 103.918 70.290  70.583  1.00 9.19   ? 3623 LEU A CD1   1 
ATOM   15296 C  CD2   . LEU A 1 3623 ? 103.867 70.276  73.082  1.00 11.16  ? 3623 LEU A CD2   1 
ATOM   15297 N  N     . GLU A 1 3624 ? 103.463 65.828  71.468  1.00 17.78  ? 3624 GLU A N     1 
ATOM   15298 C  CA    . GLU A 1 3624 ? 104.541 64.853  71.367  1.00 19.23  ? 3624 GLU A CA    1 
ATOM   15299 C  C     . GLU A 1 3624 ? 104.507 64.157  70.016  1.00 17.24  ? 3624 GLU A C     1 
ATOM   15300 O  O     . GLU A 1 3624 ? 105.523 64.105  69.310  1.00 17.97  ? 3624 GLU A O     1 
ATOM   15301 C  CB    . GLU A 1 3624 ? 104.438 63.834  72.501  1.00 23.36  ? 3624 GLU A CB    1 
ATOM   15302 C  CG    . GLU A 1 3624 ? 105.406 62.671  72.376  1.00 35.66  ? 3624 GLU A CG    1 
ATOM   15303 C  CD    . GLU A 1 3624 ? 105.349 61.734  73.566  1.00 48.46  ? 3624 GLU A CD    1 
ATOM   15304 O  OE1   . GLU A 1 3624 ? 104.757 60.642  73.437  1.00 47.87  ? 3624 GLU A OE1   1 
ATOM   15305 O  OE2   . GLU A 1 3624 ? 105.893 62.091  74.631  1.00 53.01  ? 3624 GLU A OE2   1 
ATOM   15306 N  N     . SER A 1 3625 ? 103.327 63.681  69.609  1.00 16.40  ? 3625 SER A N     1 
ATOM   15307 C  CA    . SER A 1 3625 ? 103.217 63.024  68.314  1.00 15.74  ? 3625 SER A CA    1 
ATOM   15308 C  C     . SER A 1 3625 ? 103.657 63.961  67.202  1.00 17.25  ? 3625 SER A C     1 
ATOM   15309 O  O     . SER A 1 3625 ? 104.487 63.593  66.360  1.00 17.08  ? 3625 SER A O     1 
ATOM   15310 C  CB    . SER A 1 3625 ? 101.783 62.545  68.088  1.00 18.71  ? 3625 SER A CB    1 
ATOM   15311 O  OG    . SER A 1 3625 ? 101.638 61.941  66.816  1.00 27.06  ? 3625 SER A OG    1 
ATOM   15312 N  N     . ALA A 1 3626 ? 103.169 65.206  67.232  1.00 14.21  ? 3626 ALA A N     1 
ATOM   15313 C  CA    . ALA A 1 3626 ? 103.529 66.157  66.190  1.00 12.06  ? 3626 ALA A CA    1 
ATOM   15314 C  C     . ALA A 1 3626 ? 105.032 66.382  66.160  1.00 14.60  ? 3626 ALA A C     1 
ATOM   15315 O  O     . ALA A 1 3626 ? 105.616 66.596  65.091  1.00 16.00  ? 3626 ALA A O     1 
ATOM   15316 C  CB    . ALA A 1 3626 ? 102.786 67.476  66.401  1.00 9.24   ? 3626 ALA A CB    1 
ATOM   15317 N  N     . LEU A 1 3627 ? 105.681 66.310  67.324  1.00 12.86  ? 3627 LEU A N     1 
ATOM   15318 C  CA    . LEU A 1 3627 ? 107.122 66.515  67.362  1.00 11.01  ? 3627 LEU A CA    1 
ATOM   15319 C  C     . LEU A 1 3627 ? 107.864 65.290  66.846  1.00 17.16  ? 3627 LEU A C     1 
ATOM   15320 O  O     . LEU A 1 3627 ? 108.926 65.416  66.225  1.00 18.75  ? 3627 LEU A O     1 
ATOM   15321 C  CB    . LEU A 1 3627 ? 107.567 66.861  68.782  1.00 13.50  ? 3627 LEU A CB    1 
ATOM   15322 C  CG    . LEU A 1 3627 ? 107.109 68.224  69.304  1.00 11.64  ? 3627 LEU A CG    1 
ATOM   15323 C  CD1   . LEU A 1 3627 ? 107.135 68.251  70.825  1.00 12.74  ? 3627 LEU A CD1   1 
ATOM   15324 C  CD2   . LEU A 1 3627 ? 107.955 69.345  68.724  1.00 7.71   ? 3627 LEU A CD2   1 
ATOM   15325 N  N     . ARG A 1 3628 ? 107.322 64.095  67.089  1.00 17.41  ? 3628 ARG A N     1 
ATOM   15326 C  CA    . ARG A 1 3628 ? 108.076 62.883  66.783  1.00 16.42  ? 3628 ARG A CA    1 
ATOM   15327 C  C     . ARG A 1 3628 ? 107.945 62.505  65.313  1.00 17.66  ? 3628 ARG A C     1 
ATOM   15328 O  O     . ARG A 1 3628 ? 108.927 62.112  64.673  1.00 23.68  ? 3628 ARG A O     1 
ATOM   15329 C  CB    . ARG A 1 3628 ? 107.618 61.736  67.684  1.00 19.59  ? 3628 ARG A CB    1 
ATOM   15330 C  CG    . ARG A 1 3628 ? 108.311 60.414  67.395  1.00 23.65  ? 3628 ARG A CG    1 
ATOM   15331 C  CD    . ARG A 1 3628 ? 107.890 59.335  68.377  1.00 23.46  ? 3628 ARG A CD    1 
ATOM   15332 N  NE    . ARG A 1 3628 ? 108.500 59.526  69.687  1.00 26.77  ? 3628 ARG A NE    1 
ATOM   15333 C  CZ    . ARG A 1 3628 ? 107.831 59.866  70.781  1.00 26.39  ? 3628 ARG A CZ    1 
ATOM   15334 N  NH1   . ARG A 1 3628 ? 106.521 60.042  70.762  1.00 25.31  ? 3628 ARG A NH1   1 
ATOM   15335 N  NH2   . ARG A 1 3628 ? 108.494 60.029  71.922  1.00 27.62  ? 3628 ARG A NH2   1 
ATOM   15336 N  N     . PHE A 1 3629 ? 106.742 62.618  64.760  1.00 17.57  ? 3629 PHE A N     1 
ATOM   15337 C  CA    . PHE A 1 3629 ? 106.484 62.232  63.380  1.00 17.57  ? 3629 PHE A CA    1 
ATOM   15338 C  C     . PHE A 1 3629 ? 106.592 63.396  62.406  1.00 18.12  ? 3629 PHE A C     1 
ATOM   15339 O  O     . PHE A 1 3629 ? 106.440 63.189  61.198  1.00 23.07  ? 3629 PHE A O     1 
ATOM   15340 C  CB    . PHE A 1 3629 ? 105.098 61.589  63.271  1.00 16.51  ? 3629 PHE A CB    1 
ATOM   15341 C  CG    . PHE A 1 3629 ? 104.883 60.456  64.231  1.00 18.47  ? 3629 PHE A CG    1 
ATOM   15342 C  CD1   . PHE A 1 3629 ? 105.783 59.406  64.296  1.00 23.38  ? 3629 PHE A CD1   1 
ATOM   15343 C  CD2   . PHE A 1 3629 ? 103.788 60.447  65.077  1.00 19.35  ? 3629 PHE A CD2   1 
ATOM   15344 C  CE1   . PHE A 1 3629 ? 105.591 58.363  65.183  1.00 26.71  ? 3629 PHE A CE1   1 
ATOM   15345 C  CE2   . PHE A 1 3629 ? 103.590 59.408  65.966  1.00 23.57  ? 3629 PHE A CE2   1 
ATOM   15346 C  CZ    . PHE A 1 3629 ? 104.493 58.365  66.019  1.00 25.22  ? 3629 PHE A CZ    1 
ATOM   15347 N  N     . GLY A 1 3630 ? 106.854 64.603  62.896  1.00 17.84  ? 3630 GLY A N     1 
ATOM   15348 C  CA    . GLY A 1 3630 ? 106.969 65.763  62.030  1.00 17.87  ? 3630 GLY A CA    1 
ATOM   15349 C  C     . GLY A 1 3630 ? 105.692 66.132  61.308  1.00 15.57  ? 3630 GLY A C     1 
ATOM   15350 O  O     . GLY A 1 3630 ? 105.732 66.469  60.119  1.00 17.53  ? 3630 GLY A O     1 
ATOM   15351 N  N     . ASN A 1 3631 ? 104.565 66.076  61.993  1.00 13.02  ? 3631 ASN A N     1 
ATOM   15352 C  CA    . ASN A 1 3631 ? 103.324 66.453  61.343  1.00 16.18  ? 3631 ASN A CA    1 
ATOM   15353 C  C     . ASN A 1 3631 ? 102.917 67.865  61.745  1.00 17.07  ? 3631 ASN A C     1 
ATOM   15354 O  O     . ASN A 1 3631 ? 103.217 68.312  62.856  1.00 14.45  ? 3631 ASN A O     1 
ATOM   15355 C  CB    . ASN A 1 3631 ? 102.199 65.479  61.709  1.00 17.40  ? 3631 ASN A CB    1 
ATOM   15356 C  CG    . ASN A 1 3631 ? 102.568 64.034  61.439  1.00 20.63  ? 3631 ASN A CG    1 
ATOM   15357 O  OD1   . ASN A 1 3631 ? 102.460 63.180  62.319  1.00 23.70  ? 3631 ASN A OD1   1 
ATOM   15358 N  ND2   . ASN A 1 3631 ? 103.005 63.753  60.218  1.00 19.31  ? 3631 ASN A ND2   1 
ATOM   15359 N  N     . PRO A 1 3632 ? 102.250 68.595  60.854  1.00 17.28  ? 3632 PRO A N     1 
ATOM   15360 C  CA    . PRO A 1 3632 ? 101.717 69.907  61.235  1.00 11.81  ? 3632 PRO A CA    1 
ATOM   15361 C  C     . PRO A 1 3632 ? 100.695 69.780  62.354  1.00 13.58  ? 3632 PRO A C     1 
ATOM   15362 O  O     . PRO A 1 3632 ? 99.914  68.829  62.406  1.00 18.67  ? 3632 PRO A O     1 
ATOM   15363 C  CB    . PRO A 1 3632 ? 101.081 70.426  59.939  1.00 11.64  ? 3632 PRO A CB    1 
ATOM   15364 C  CG    . PRO A 1 3632 ? 100.892 69.219  59.082  1.00 16.24  ? 3632 PRO A CG    1 
ATOM   15365 C  CD    . PRO A 1 3632 ? 102.001 68.285  59.437  1.00 16.47  ? 3632 PRO A CD    1 
ATOM   15366 N  N     . LEU A 1 3633 ? 100.713 70.754  63.259  1.00 10.02  ? 3633 LEU A N     1 
ATOM   15367 C  CA    . LEU A 1 3633 ? 99.823  70.776  64.410  1.00 8.29   ? 3633 LEU A CA    1 
ATOM   15368 C  C     . LEU A 1 3633 ? 99.191  72.153  64.515  1.00 8.69   ? 3633 LEU A C     1 
ATOM   15369 O  O     . LEU A 1 3633 ? 99.865  73.166  64.304  1.00 10.14  ? 3633 LEU A O     1 
ATOM   15370 C  CB    . LEU A 1 3633 ? 100.578 70.435  65.700  1.00 10.27  ? 3633 LEU A CB    1 
ATOM   15371 C  CG    . LEU A 1 3633 ? 99.741  70.273  66.970  1.00 10.47  ? 3633 LEU A CG    1 
ATOM   15372 C  CD1   . LEU A 1 3633 ? 98.806  69.081  66.850  1.00 11.36  ? 3633 LEU A CD1   1 
ATOM   15373 C  CD2   . LEU A 1 3633 ? 100.638 70.136  68.189  1.00 9.49   ? 3633 LEU A CD2   1 
ATOM   15374 N  N     . LEU A 1 3634 ? 97.899  72.187  64.822  1.00 10.18  ? 3634 LEU A N     1 
ATOM   15375 C  CA    . LEU A 1 3634 ? 97.163  73.429  65.016  1.00 8.45   ? 3634 LEU A CA    1 
ATOM   15376 C  C     . LEU A 1 3634 ? 96.581  73.428  66.422  1.00 10.71  ? 3634 LEU A C     1 
ATOM   15377 O  O     . LEU A 1 3634 ? 95.739  72.585  66.748  1.00 13.38  ? 3634 LEU A O     1 
ATOM   15378 C  CB    . LEU A 1 3634 ? 96.061  73.582  63.968  1.00 10.92  ? 3634 LEU A CB    1 
ATOM   15379 C  CG    . LEU A 1 3634 ? 95.053  74.709  64.198  1.00 13.41  ? 3634 LEU A CG    1 
ATOM   15380 C  CD1   . LEU A 1 3634 ? 95.750  76.055  64.218  1.00 7.67   ? 3634 LEU A CD1   1 
ATOM   15381 C  CD2   . LEU A 1 3634 ? 93.977  74.685  63.130  1.00 19.14  ? 3634 LEU A CD2   1 
ATOM   15382 N  N     . VAL A 1 3635 ? 97.026  74.370  67.248  1.00 9.09   ? 3635 VAL A N     1 
ATOM   15383 C  CA    . VAL A 1 3635 ? 96.627  74.446  68.647  1.00 10.95  ? 3635 VAL A CA    1 
ATOM   15384 C  C     . VAL A 1 3635 ? 95.787  75.702  68.828  1.00 10.08  ? 3635 VAL A C     1 
ATOM   15385 O  O     . VAL A 1 3635 ? 96.256  76.818  68.567  1.00 11.27  ? 3635 VAL A O     1 
ATOM   15386 C  CB    . VAL A 1 3635 ? 97.844  74.455  69.584  1.00 8.61   ? 3635 VAL A CB    1 
ATOM   15387 C  CG1   . VAL A 1 3635 ? 97.392  74.482  71.030  1.00 9.57   ? 3635 VAL A CG1   1 
ATOM   15388 C  CG2   . VAL A 1 3635 ? 98.742  73.259  69.308  1.00 10.08  ? 3635 VAL A CG2   1 
ATOM   15389 N  N     . GLN A 1 3636 ? 94.552  75.522  69.281  1.00 11.66  ? 3636 GLN A N     1 
ATOM   15390 C  CA    . GLN A 1 3636 ? 93.622  76.618  69.497  1.00 14.35  ? 3636 GLN A CA    1 
ATOM   15391 C  C     . GLN A 1 3636 ? 93.661  77.071  70.952  1.00 14.71  ? 3636 GLN A C     1 
ATOM   15392 O  O     . GLN A 1 3636 ? 94.297  76.452  71.809  1.00 16.18  ? 3636 GLN A O     1 
ATOM   15393 C  CB    . GLN A 1 3636 ? 92.202  76.201  69.100  1.00 18.82  ? 3636 GLN A CB    1 
ATOM   15394 C  CG    . GLN A 1 3636 ? 92.078  75.737  67.658  1.00 23.46  ? 3636 GLN A CG    1 
ATOM   15395 C  CD    . GLN A 1 3636 ? 90.648  75.417  67.269  1.00 34.96  ? 3636 GLN A CD    1 
ATOM   15396 O  OE1   . GLN A 1 3636 ? 89.996  74.579  67.891  1.00 40.85  ? 3636 GLN A OE1   1 
ATOM   15397 N  NE2   . GLN A 1 3636 ? 90.154  76.086  66.234  1.00 36.72  ? 3636 GLN A NE2   1 
ATOM   15398 N  N     . ASP A 1 3637 ? 92.966  78.180  71.218  1.00 17.39  ? 3637 ASP A N     1 
ATOM   15399 C  CA    . ASP A 1 3637 ? 92.871  78.763  72.558  1.00 20.00  ? 3637 ASP A CA    1 
ATOM   15400 C  C     . ASP A 1 3637 ? 94.254  79.105  73.112  1.00 21.54  ? 3637 ASP A C     1 
ATOM   15401 O  O     . ASP A 1 3637 ? 94.635  78.684  74.206  1.00 22.76  ? 3637 ASP A O     1 
ATOM   15402 C  CB    . ASP A 1 3637 ? 92.110  77.837  73.510  1.00 22.92  ? 3637 ASP A CB    1 
ATOM   15403 C  CG    . ASP A 1 3637 ? 90.782  77.379  72.939  1.00 30.39  ? 3637 ASP A CG    1 
ATOM   15404 O  OD1   . ASP A 1 3637 ? 89.928  78.243  72.652  1.00 33.00  ? 3637 ASP A OD1   1 
ATOM   15405 O  OD2   . ASP A 1 3637 ? 90.593  76.155  72.779  1.00 29.83  ? 3637 ASP A OD2   1 
ATOM   15406 N  N     . VAL A 1 3638 ? 95.012  79.886  72.338  1.00 19.64  ? 3638 VAL A N     1 
ATOM   15407 C  CA    . VAL A 1 3638 ? 96.345  80.301  72.763  1.00 17.06  ? 3638 VAL A CA    1 
ATOM   15408 C  C     . VAL A 1 3638 ? 96.303  81.278  73.928  1.00 17.11  ? 3638 VAL A C     1 
ATOM   15409 O  O     . VAL A 1 3638 ? 97.341  81.538  74.547  1.00 22.24  ? 3638 VAL A O     1 
ATOM   15410 C  CB    . VAL A 1 3638 ? 97.116  80.900  71.567  1.00 13.24  ? 3638 VAL A CB    1 
ATOM   15411 C  CG1   . VAL A 1 3638 ? 96.617  82.294  71.248  1.00 11.87  ? 3638 VAL A CG1   1 
ATOM   15412 C  CG2   . VAL A 1 3638 ? 98.621  80.894  71.825  1.00 10.39  ? 3638 VAL A CG2   1 
ATOM   15413 N  N     . GLU A 1 3639 ? 95.126  81.820  74.255  1.00 19.04  ? 3639 GLU A N     1 
ATOM   15414 C  CA    . GLU A 1 3639 ? 94.987  82.628  75.461  1.00 24.00  ? 3639 GLU A CA    1 
ATOM   15415 C  C     . GLU A 1 3639 ? 95.264  81.817  76.720  1.00 24.55  ? 3639 GLU A C     1 
ATOM   15416 O  O     . GLU A 1 3639 ? 95.601  82.395  77.759  1.00 30.55  ? 3639 GLU A O     1 
ATOM   15417 C  CB    . GLU A 1 3639 ? 93.586  83.241  75.533  1.00 22.21  ? 3639 GLU A CB    1 
ATOM   15418 C  CG    . GLU A 1 3639 ? 92.447  82.246  75.343  1.00 25.95  ? 3639 GLU A CG    1 
ATOM   15419 C  CD    . GLU A 1 3639 ? 92.080  82.030  73.884  1.00 30.59  ? 3639 GLU A CD    1 
ATOM   15420 O  OE1   . GLU A 1 3639 ? 92.977  82.118  73.020  1.00 27.59  ? 3639 GLU A OE1   1 
ATOM   15421 O  OE2   . GLU A 1 3639 ? 90.892  81.771  73.603  1.00 35.02  ? 3639 GLU A OE2   1 
ATOM   15422 N  N     . SER A 1 3640 ? 95.128  80.495  76.645  1.00 19.22  ? 3640 SER A N     1 
ATOM   15423 C  CA    . SER A 1 3640 ? 95.474  79.576  77.728  1.00 18.43  ? 3640 SER A CA    1 
ATOM   15424 C  C     . SER A 1 3640 ? 96.798  78.878  77.452  1.00 20.32  ? 3640 SER A C     1 
ATOM   15425 O  O     . SER A 1 3640 ? 96.944  77.679  77.703  1.00 23.26  ? 3640 SER A O     1 
ATOM   15426 C  CB    . SER A 1 3640 ? 94.360  78.556  77.935  1.00 25.91  ? 3640 SER A CB    1 
ATOM   15427 O  OG    . SER A 1 3640 ? 93.153  79.191  78.321  1.00 35.98  ? 3640 SER A OG    1 
ATOM   15428 N  N     . TYR A 1 3641 ? 97.765  79.621  76.914  1.00 18.71  ? 3641 TYR A N     1 
ATOM   15429 C  CA    . TYR A 1 3641 ? 99.024  79.045  76.459  1.00 15.26  ? 3641 TYR A CA    1 
ATOM   15430 C  C     . TYR A 1 3641 ? 99.717  78.265  77.570  1.00 19.20  ? 3641 TYR A C     1 
ATOM   15431 O  O     . TYR A 1 3641 ? 99.872  78.755  78.692  1.00 26.02  ? 3641 TYR A O     1 
ATOM   15432 C  CB    . TYR A 1 3641 ? 99.939  80.157  75.941  1.00 13.06  ? 3641 TYR A CB    1 
ATOM   15433 C  CG    . TYR A 1 3641 ? 101.364 79.729  75.674  1.00 13.68  ? 3641 TYR A CG    1 
ATOM   15434 C  CD1   . TYR A 1 3641 ? 101.696 79.032  74.520  1.00 12.10  ? 3641 TYR A CD1   1 
ATOM   15435 C  CD2   . TYR A 1 3641 ? 102.380 80.034  76.571  1.00 11.40  ? 3641 TYR A CD2   1 
ATOM   15436 C  CE1   . TYR A 1 3641 ? 102.998 78.643  74.272  1.00 11.74  ? 3641 TYR A CE1   1 
ATOM   15437 C  CE2   . TYR A 1 3641 ? 103.683 79.650  76.330  1.00 12.83  ? 3641 TYR A CE2   1 
ATOM   15438 C  CZ    . TYR A 1 3641 ? 103.987 78.955  75.180  1.00 14.05  ? 3641 TYR A CZ    1 
ATOM   15439 O  OH    . TYR A 1 3641 ? 105.285 78.571  74.937  1.00 13.57  ? 3641 TYR A OH    1 
ATOM   15440 N  N     . ASP A 1 3642 ? 100.131 77.043  77.245  1.00 17.26  ? 3642 ASP A N     1 
ATOM   15441 C  CA    . ASP A 1 3642 ? 100.855 76.194  78.179  1.00 16.56  ? 3642 ASP A CA    1 
ATOM   15442 C  C     . ASP A 1 3642 ? 102.350 76.384  77.958  1.00 17.11  ? 3642 ASP A C     1 
ATOM   15443 O  O     . ASP A 1 3642 ? 102.831 76.151  76.841  1.00 13.26  ? 3642 ASP A O     1 
ATOM   15444 C  CB    . ASP A 1 3642 ? 100.467 74.736  77.978  1.00 19.24  ? 3642 ASP A CB    1 
ATOM   15445 C  CG    . ASP A 1 3642 ? 100.792 73.865  79.174  1.00 28.12  ? 3642 ASP A CG    1 
ATOM   15446 O  OD1   . ASP A 1 3642 ? 101.379 74.373  80.148  1.00 29.82  ? 3642 ASP A OD1   1 
ATOM   15447 O  OD2   . ASP A 1 3642 ? 100.456 72.663  79.139  1.00 33.21  ? 3642 ASP A OD2   1 
ATOM   15448 N  N     . PRO A 1 3643 ? 103.117 76.811  78.971  1.00 20.99  ? 3643 PRO A N     1 
ATOM   15449 C  CA    . PRO A 1 3643 ? 104.535 77.136  78.747  1.00 16.67  ? 3643 PRO A CA    1 
ATOM   15450 C  C     . PRO A 1 3643 ? 105.403 75.955  78.337  1.00 16.73  ? 3643 PRO A C     1 
ATOM   15451 O  O     . PRO A 1 3643 ? 106.609 76.119  78.128  1.00 19.31  ? 3643 PRO A O     1 
ATOM   15452 C  CB    . PRO A 1 3643 ? 104.982 77.698  80.104  1.00 16.13  ? 3643 PRO A CB    1 
ATOM   15453 C  CG    . PRO A 1 3643 ? 103.723 78.134  80.773  1.00 19.12  ? 3643 PRO A CG    1 
ATOM   15454 C  CD    . PRO A 1 3643 ? 102.682 77.160  80.333  1.00 16.71  ? 3643 PRO A CD    1 
ATOM   15455 N  N     . VAL A 1 3644 ? 104.813 74.763  78.213  1.00 18.13  ? 3644 VAL A N     1 
ATOM   15456 C  CA    . VAL A 1 3644 ? 105.585 73.595  77.806  1.00 14.98  ? 3644 VAL A CA    1 
ATOM   15457 C  C     . VAL A 1 3644 ? 106.097 73.731  76.375  1.00 18.30  ? 3644 VAL A C     1 
ATOM   15458 O  O     . VAL A 1 3644 ? 107.046 73.037  75.991  1.00 20.85  ? 3644 VAL A O     1 
ATOM   15459 C  CB    . VAL A 1 3644 ? 104.745 72.315  77.986  1.00 19.60  ? 3644 VAL A CB    1 
ATOM   15460 C  CG1   . VAL A 1 3644 ? 103.691 72.195  76.894  1.00 19.25  ? 3644 VAL A CG1   1 
ATOM   15461 C  CG2   . VAL A 1 3644 ? 105.638 71.083  78.037  1.00 22.46  ? 3644 VAL A CG2   1 
ATOM   15462 N  N     . LEU A 1 3645 ? 105.504 74.619  75.575  1.00 14.14  ? 3645 LEU A N     1 
ATOM   15463 C  CA    . LEU A 1 3645 ? 106.009 74.923  74.241  1.00 13.61  ? 3645 LEU A CA    1 
ATOM   15464 C  C     . LEU A 1 3645 ? 107.205 75.862  74.246  1.00 13.48  ? 3645 LEU A C     1 
ATOM   15465 O  O     . LEU A 1 3645 ? 107.750 76.133  73.172  1.00 14.50  ? 3645 LEU A O     1 
ATOM   15466 C  CB    . LEU A 1 3645 ? 104.909 75.536  73.368  1.00 13.89  ? 3645 LEU A CB    1 
ATOM   15467 C  CG    . LEU A 1 3645 ? 103.807 74.629  72.833  1.00 11.89  ? 3645 LEU A CG    1 
ATOM   15468 C  CD1   . LEU A 1 3645 ? 102.753 75.454  72.119  1.00 12.03  ? 3645 LEU A CD1   1 
ATOM   15469 C  CD2   . LEU A 1 3645 ? 104.413 73.616  71.888  1.00 10.82  ? 3645 LEU A CD2   1 
ATOM   15470 N  N     . ASN A 1 3646 ? 107.614 76.372  75.409  1.00 12.74  ? 3646 ASN A N     1 
ATOM   15471 C  CA    . ASN A 1 3646 ? 108.707 77.343  75.443  1.00 12.13  ? 3646 ASN A CA    1 
ATOM   15472 C  C     . ASN A 1 3646 ? 109.974 76.834  74.765  1.00 13.07  ? 3646 ASN A C     1 
ATOM   15473 O  O     . ASN A 1 3646 ? 110.536 77.571  73.936  1.00 12.23  ? 3646 ASN A O     1 
ATOM   15474 C  CB    . ASN A 1 3646 ? 108.971 77.771  76.891  1.00 11.39  ? 3646 ASN A CB    1 
ATOM   15475 C  CG    . ASN A 1 3646 ? 107.965 78.789  77.390  1.00 13.53  ? 3646 ASN A CG    1 
ATOM   15476 O  OD1   . ASN A 1 3646 ? 107.085 79.224  76.648  1.00 19.72  ? 3646 ASN A OD1   1 
ATOM   15477 N  ND2   . ASN A 1 3646 ? 108.090 79.174  78.654  1.00 13.90  ? 3646 ASN A ND2   1 
ATOM   15478 N  N     . PRO A 1 3647 ? 110.478 75.626  75.045  1.00 13.51  ? 3647 PRO A N     1 
ATOM   15479 C  CA    . PRO A 1 3647 ? 111.616 75.129  74.252  1.00 12.81  ? 3647 PRO A CA    1 
ATOM   15480 C  C     . PRO A 1 3647 ? 111.288 74.931  72.782  1.00 11.62  ? 3647 PRO A C     1 
ATOM   15481 O  O     . PRO A 1 3647 ? 112.164 75.124  71.930  1.00 12.48  ? 3647 PRO A O     1 
ATOM   15482 C  CB    . PRO A 1 3647 ? 111.966 73.801  74.938  1.00 13.45  ? 3647 PRO A CB    1 
ATOM   15483 C  CG    . PRO A 1 3647 ? 110.702 73.382  75.597  1.00 16.15  ? 3647 PRO A CG    1 
ATOM   15484 C  CD    . PRO A 1 3647 ? 110.089 74.654  76.084  1.00 12.11  ? 3647 PRO A CD    1 
ATOM   15485 N  N     . VAL A 1 3648 ? 110.052 74.545  72.460  1.00 12.53  ? 3648 VAL A N     1 
ATOM   15486 C  CA    . VAL A 1 3648 ? 109.686 74.301  71.067  1.00 10.79  ? 3648 VAL A CA    1 
ATOM   15487 C  C     . VAL A 1 3648 ? 109.644 75.608  70.284  1.00 9.87   ? 3648 VAL A C     1 
ATOM   15488 O  O     . VAL A 1 3648 ? 110.174 75.696  69.170  1.00 10.10  ? 3648 VAL A O     1 
ATOM   15489 C  CB    . VAL A 1 3648 ? 108.344 73.551  70.994  1.00 11.15  ? 3648 VAL A CB    1 
ATOM   15490 C  CG1   . VAL A 1 3648 ? 107.897 73.399  69.549  1.00 7.80   ? 3648 VAL A CG1   1 
ATOM   15491 C  CG2   . VAL A 1 3648 ? 108.458 72.194  71.668  1.00 10.18  ? 3648 VAL A CG2   1 
ATOM   15492 N  N     . LEU A 1 3649 ? 109.019 76.643  70.851  1.00 10.02  ? 3649 LEU A N     1 
ATOM   15493 C  CA    . LEU A 1 3649 ? 108.949 77.926  70.160  1.00 7.77   ? 3649 LEU A CA    1 
ATOM   15494 C  C     . LEU A 1 3649 ? 110.310 78.605  70.096  1.00 10.68  ? 3649 LEU A C     1 
ATOM   15495 O  O     . LEU A 1 3649 ? 110.593 79.331  69.136  1.00 14.45  ? 3649 LEU A O     1 
ATOM   15496 C  CB    . LEU A 1 3649 ? 107.927 78.840  70.839  1.00 8.52   ? 3649 LEU A CB    1 
ATOM   15497 C  CG    . LEU A 1 3649 ? 106.532 78.265  71.100  1.00 11.11  ? 3649 LEU A CG    1 
ATOM   15498 C  CD1   . LEU A 1 3649 ? 105.568 79.365  71.514  1.00 8.01   ? 3649 LEU A CD1   1 
ATOM   15499 C  CD2   . LEU A 1 3649 ? 106.008 77.528  69.875  1.00 8.86   ? 3649 LEU A CD2   1 
ATOM   15500 N  N     . ASN A 1 3650 ? 111.160 78.385  71.096  1.00 9.95   ? 3650 ASN A N     1 
ATOM   15501 C  CA    . ASN A 1 3650 ? 112.516 78.913  71.101  1.00 7.87   ? 3650 ASN A CA    1 
ATOM   15502 C  C     . ASN A 1 3650 ? 113.464 78.098  70.232  1.00 10.28  ? 3650 ASN A C     1 
ATOM   15503 O  O     . ASN A 1 3650 ? 114.606 78.520  70.022  1.00 15.15  ? 3650 ASN A O     1 
ATOM   15504 C  CB    . ASN A 1 3650 ? 113.058 78.971  72.532  1.00 12.57  ? 3650 ASN A CB    1 
ATOM   15505 C  CG    . ASN A 1 3650 ? 112.343 79.992  73.391  1.00 14.96  ? 3650 ASN A CG    1 
ATOM   15506 O  OD1   . ASN A 1 3650 ? 112.243 79.833  74.607  1.00 19.19  ? 3650 ASN A OD1   1 
ATOM   15507 N  ND2   . ASN A 1 3650 ? 111.837 81.043  72.765  1.00 16.38  ? 3650 ASN A ND2   1 
ATOM   15508 N  N     . ARG A 1 3651 ? 113.016 76.944  69.730  1.00 10.47  ? 3651 ARG A N     1 
ATOM   15509 C  CA    . ARG A 1 3651 ? 113.836 76.047  68.921  1.00 12.24  ? 3651 ARG A CA    1 
ATOM   15510 C  C     . ARG A 1 3651 ? 115.116 75.647  69.646  1.00 14.48  ? 3651 ARG A C     1 
ATOM   15511 O  O     . ARG A 1 3651 ? 116.195 75.627  69.045  1.00 17.10  ? 3651 ARG A O     1 
ATOM   15512 C  CB    . ARG A 1 3651 ? 114.167 76.689  67.570  1.00 14.02  ? 3651 ARG A CB    1 
ATOM   15513 C  CG    . ARG A 1 3651 ? 113.082 76.522  66.516  1.00 17.32  ? 3651 ARG A CG    1 
ATOM   15514 C  CD    . ARG A 1 3651 ? 113.441 77.254  65.231  1.00 18.14  ? 3651 ARG A CD    1 
ATOM   15515 N  NE    . ARG A 1 3651 ? 112.324 78.036  64.715  1.00 19.75  ? 3651 ARG A NE    1 
ATOM   15516 C  CZ    . ARG A 1 3651 ? 111.313 77.532  64.021  1.00 17.09  ? 3651 ARG A CZ    1 
ATOM   15517 N  NH1   . ARG A 1 3651 ? 111.258 76.246  63.714  1.00 17.42  ? 3651 ARG A NH1   1 
ATOM   15518 N  NH2   . ARG A 1 3651 ? 110.335 78.339  63.621  1.00 11.38  ? 3651 ARG A NH2   1 
ATOM   15519 N  N     . GLU A 1 3652 ? 115.007 75.326  70.935  1.00 14.66  ? 3652 GLU A N     1 
ATOM   15520 C  CA    . GLU A 1 3652 ? 116.153 74.884  71.729  1.00 17.86  ? 3652 GLU A CA    1 
ATOM   15521 C  C     . GLU A 1 3652 ? 116.369 73.397  71.483  1.00 18.54  ? 3652 GLU A C     1 
ATOM   15522 O  O     . GLU A 1 3652 ? 115.934 72.544  72.257  1.00 22.84  ? 3652 GLU A O     1 
ATOM   15523 C  CB    . GLU A 1 3652 ? 115.935 75.171  73.209  1.00 16.81  ? 3652 GLU A CB    1 
ATOM   15524 C  CG    . GLU A 1 3652 ? 115.466 76.577  73.521  1.00 13.91  ? 3652 GLU A CG    1 
ATOM   15525 C  CD    . GLU A 1 3652 ? 114.972 76.717  74.947  1.00 24.48  ? 3652 GLU A CD    1 
ATOM   15526 O  OE1   . GLU A 1 3652 ? 115.321 75.857  75.783  1.00 32.37  ? 3652 GLU A OE1   1 
ATOM   15527 O  OE2   . GLU A 1 3652 ? 114.237 77.684  75.235  1.00 21.33  ? 3652 GLU A OE2   1 
ATOM   15528 N  N     . VAL A 1 3653 ? 117.065 73.083  70.399  1.00 19.93  ? 3653 VAL A N     1 
ATOM   15529 C  CA    . VAL A 1 3653 ? 117.327 71.703  70.013  1.00 22.95  ? 3653 VAL A CA    1 
ATOM   15530 C  C     . VAL A 1 3653 ? 118.749 71.340  70.409  1.00 27.07  ? 3653 VAL A C     1 
ATOM   15531 O  O     . VAL A 1 3653 ? 119.660 72.176  70.392  1.00 27.99  ? 3653 VAL A O     1 
ATOM   15532 C  CB    . VAL A 1 3653 ? 117.096 71.486  68.502  1.00 21.54  ? 3653 VAL A CB    1 
ATOM   15533 C  CG1   . VAL A 1 3653 ? 115.646 71.756  68.149  1.00 24.29  ? 3653 VAL A CG1   1 
ATOM   15534 C  CG2   . VAL A 1 3653 ? 118.020 72.375  67.683  1.00 22.29  ? 3653 VAL A CG2   1 
ATOM   15535 N  N     . ARG A 1 3654 ? 118.940 70.079  70.788  1.00 27.82  ? 3654 ARG A N     1 
ATOM   15536 C  CA    . ARG A 1 3654 ? 120.251 69.549  71.147  1.00 29.43  ? 3654 ARG A CA    1 
ATOM   15537 C  C     . ARG A 1 3654 ? 120.618 68.478  70.130  1.00 28.02  ? 3654 ARG A C     1 
ATOM   15538 O  O     . ARG A 1 3654 ? 119.935 67.455  70.027  1.00 31.60  ? 3654 ARG A O     1 
ATOM   15539 C  CB    . ARG A 1 3654 ? 120.245 68.987  72.568  1.00 30.64  ? 3654 ARG A CB    1 
ATOM   15540 C  CG    . ARG A 1 3654 ? 121.514 68.247  72.952  1.00 33.52  ? 3654 ARG A CG    1 
ATOM   15541 C  CD    . ARG A 1 3654 ? 121.549 67.956  74.443  1.00 35.70  ? 3654 ARG A CD    1 
ATOM   15542 N  NE    . ARG A 1 3654 ? 120.231 67.614  74.964  1.00 48.45  ? 3654 ARG A NE    1 
ATOM   15543 C  CZ    . ARG A 1 3654 ? 119.882 66.406  75.385  1.00 53.41  ? 3654 ARG A CZ    1 
ATOM   15544 N  NH1   . ARG A 1 3654 ? 120.732 65.392  75.359  1.00 51.06  ? 3654 ARG A NH1   1 
ATOM   15545 N  NH2   . ARG A 1 3654 ? 118.649 66.209  75.843  1.00 50.10  ? 3654 ARG A NH2   1 
ATOM   15546 N  N     . ARG A 1 3655 ? 121.679 68.718  69.367  1.00 29.47  ? 3655 ARG A N     1 
ATOM   15547 C  CA    . ARG A 1 3655 ? 122.140 67.777  68.349  1.00 31.85  ? 3655 ARG A CA    1 
ATOM   15548 C  C     . ARG A 1 3655 ? 123.351 67.036  68.902  1.00 39.48  ? 3655 ARG A C     1 
ATOM   15549 O  O     . ARG A 1 3655 ? 124.445 67.597  69.010  1.00 39.88  ? 3655 ARG A O     1 
ATOM   15550 C  CB    . ARG A 1 3655 ? 122.449 68.498  67.043  1.00 27.03  ? 3655 ARG A CB    1 
ATOM   15551 C  CG    . ARG A 1 3655 ? 121.197 68.905  66.286  1.00 30.71  ? 3655 ARG A CG    1 
ATOM   15552 C  CD    . ARG A 1 3655 ? 121.484 69.865  65.147  1.00 34.07  ? 3655 ARG A CD    1 
ATOM   15553 N  NE    . ARG A 1 3655 ? 120.282 70.119  64.361  1.00 33.18  ? 3655 ARG A NE    1 
ATOM   15554 C  CZ    . ARG A 1 3655 ? 119.689 71.300  64.257  1.00 36.88  ? 3655 ARG A CZ    1 
ATOM   15555 N  NH1   . ARG A 1 3655 ? 120.160 72.368  64.879  1.00 42.60  ? 3655 ARG A NH1   1 
ATOM   15556 N  NH2   . ARG A 1 3655 ? 118.592 71.411  63.513  1.00 34.77  ? 3655 ARG A NH2   1 
ATOM   15557 N  N     . THR A 1 3656 ? 123.148 65.767  69.250  1.00 45.06  ? 3656 THR A N     1 
ATOM   15558 C  CA    . THR A 1 3656 ? 124.185 64.942  69.854  1.00 50.33  ? 3656 THR A CA    1 
ATOM   15559 C  C     . THR A 1 3656 ? 123.988 63.500  69.414  1.00 51.30  ? 3656 THR A C     1 
ATOM   15560 O  O     . THR A 1 3656 ? 122.852 63.022  69.340  1.00 47.15  ? 3656 THR A O     1 
ATOM   15561 C  CB    . THR A 1 3656 ? 124.152 65.042  71.386  1.00 50.83  ? 3656 THR A CB    1 
ATOM   15562 O  OG1   . THR A 1 3656 ? 124.295 66.412  71.780  1.00 47.68  ? 3656 THR A OG1   1 
ATOM   15563 C  CG2   . THR A 1 3656 ? 125.278 64.227  72.006  1.00 50.51  ? 3656 THR A CG2   1 
ATOM   15564 N  N     . GLY A 1 3657 ? 125.091 62.821  69.111  1.00 53.34  ? 3657 GLY A N     1 
ATOM   15565 C  CA    . GLY A 1 3657 ? 125.041 61.428  68.703  1.00 43.74  ? 3657 GLY A CA    1 
ATOM   15566 C  C     . GLY A 1 3657 ? 124.214 61.185  67.461  1.00 44.37  ? 3657 GLY A C     1 
ATOM   15567 O  O     . GLY A 1 3657 ? 123.528 60.159  67.368  1.00 46.21  ? 3657 GLY A O     1 
ATOM   15568 N  N     . GLY A 1 3658 ? 124.259 62.106  66.500  1.00 43.62  ? 3658 GLY A N     1 
ATOM   15569 C  CA    . GLY A 1 3658 ? 123.425 61.995  65.323  1.00 39.71  ? 3658 GLY A CA    1 
ATOM   15570 C  C     . GLY A 1 3658 ? 121.944 62.145  65.579  1.00 39.19  ? 3658 GLY A C     1 
ATOM   15571 O  O     . GLY A 1 3658 ? 121.143 61.814  64.701  1.00 39.86  ? 3658 GLY A O     1 
ATOM   15572 N  N     . ARG A 1 3659 ? 121.554 62.634  66.754  1.00 37.70  ? 3659 ARG A N     1 
ATOM   15573 C  CA    . ARG A 1 3659 ? 120.154 62.768  67.125  1.00 32.41  ? 3659 ARG A CA    1 
ATOM   15574 C  C     . ARG A 1 3659 ? 119.833 64.218  67.458  1.00 31.12  ? 3659 ARG A C     1 
ATOM   15575 O  O     . ARG A 1 3659 ? 120.604 64.892  68.149  1.00 31.61  ? 3659 ARG A O     1 
ATOM   15576 C  CB    . ARG A 1 3659 ? 119.813 61.880  68.323  1.00 30.33  ? 3659 ARG A CB    1 
ATOM   15577 C  CG    . ARG A 1 3659 ? 119.664 60.406  68.011  1.00 32.24  ? 3659 ARG A CG    1 
ATOM   15578 C  CD    . ARG A 1 3659 ? 119.582 59.603  69.298  1.00 32.89  ? 3659 ARG A CD    1 
ATOM   15579 N  NE    . ARG A 1 3659 ? 118.292 59.768  69.957  1.00 26.36  ? 3659 ARG A NE    1 
ATOM   15580 C  CZ    . ARG A 1 3659 ? 118.128 59.885  71.268  1.00 24.82  ? 3659 ARG A CZ    1 
ATOM   15581 N  NH1   . ARG A 1 3659 ? 119.158 59.866  72.097  1.00 23.13  ? 3659 ARG A NH1   1 
ATOM   15582 N  NH2   . ARG A 1 3659 ? 116.900 60.026  71.758  1.00 21.84  ? 3659 ARG A NH2   1 
ATOM   15583 N  N     . VAL A 1 3660 ? 118.689 64.686  66.969  1.00 27.19  ? 3660 VAL A N     1 
ATOM   15584 C  CA    . VAL A 1 3660 ? 118.179 66.020  67.266  1.00 23.32  ? 3660 VAL A CA    1 
ATOM   15585 C  C     . VAL A 1 3660 ? 117.081 65.860  68.309  1.00 20.27  ? 3660 VAL A C     1 
ATOM   15586 O  O     . VAL A 1 3660 ? 116.030 65.274  68.030  1.00 24.67  ? 3660 VAL A O     1 
ATOM   15587 C  CB    . VAL A 1 3660 ? 117.653 66.718  66.004  1.00 20.15  ? 3660 VAL A CB    1 
ATOM   15588 C  CG1   . VAL A 1 3660 ? 117.214 68.139  66.325  1.00 22.25  ? 3660 VAL A CG1   1 
ATOM   15589 C  CG2   . VAL A 1 3660 ? 118.705 66.702  64.907  1.00 21.95  ? 3660 VAL A CG2   1 
ATOM   15590 N  N     . LEU A 1 3661 ? 117.313 66.380  69.511  1.00 19.14  ? 3661 LEU A N     1 
ATOM   15591 C  CA    . LEU A 1 3661 ? 116.411 66.188  70.638  1.00 23.13  ? 3661 LEU A CA    1 
ATOM   15592 C  C     . LEU A 1 3661 ? 115.789 67.516  71.044  1.00 22.39  ? 3661 LEU A C     1 
ATOM   15593 O  O     . LEU A 1 3661 ? 116.476 68.543  71.093  1.00 26.35  ? 3661 LEU A O     1 
ATOM   15594 C  CB    . LEU A 1 3661 ? 117.143 65.575  71.835  1.00 29.40  ? 3661 LEU A CB    1 
ATOM   15595 C  CG    . LEU A 1 3661 ? 117.222 64.048  71.939  1.00 26.77  ? 3661 LEU A CG    1 
ATOM   15596 C  CD1   . LEU A 1 3661 ? 115.858 63.445  72.214  1.00 29.08  ? 3661 LEU A CD1   1 
ATOM   15597 C  CD2   . LEU A 1 3661 ? 117.831 63.436  70.700  1.00 24.06  ? 3661 LEU A CD2   1 
ATOM   15598 N  N     . ILE A 1 3662 ? 114.490 67.487  71.329  1.00 25.12  ? 3662 ILE A N     1 
ATOM   15599 C  CA    . ILE A 1 3662 ? 113.771 68.599  71.936  1.00 21.12  ? 3662 ILE A CA    1 
ATOM   15600 C  C     . ILE A 1 3662 ? 113.298 68.145  73.311  1.00 20.87  ? 3662 ILE A C     1 
ATOM   15601 O  O     . ILE A 1 3662 ? 112.762 67.040  73.458  1.00 26.89  ? 3662 ILE A O     1 
ATOM   15602 C  CB    . ILE A 1 3662 ? 112.599 69.077  71.052  1.00 23.03  ? 3662 ILE A CB    1 
ATOM   15603 C  CG1   . ILE A 1 3662 ? 112.050 70.418  71.550  1.00 20.00  ? 3662 ILE A CG1   1 
ATOM   15604 C  CG2   . ILE A 1 3662 ? 111.503 68.020  70.930  1.00 21.35  ? 3662 ILE A CG2   1 
ATOM   15605 C  CD1   . ILE A 1 3662 ? 113.018 71.564  71.419  1.00 19.01  ? 3662 ILE A CD1   1 
ATOM   15606 N  N     . THR A 1 3663 ? 113.545 68.968  74.324  1.00 22.77  ? 3663 THR A N     1 
ATOM   15607 C  CA    . THR A 1 3663 ? 113.204 68.619  75.699  1.00 30.12  ? 3663 THR A CA    1 
ATOM   15608 C  C     . THR A 1 3663 ? 111.811 69.152  76.008  1.00 29.30  ? 3663 THR A C     1 
ATOM   15609 O  O     . THR A 1 3663 ? 111.641 70.344  76.282  1.00 32.14  ? 3663 THR A O     1 
ATOM   15610 C  CB    . THR A 1 3663 ? 114.237 69.178  76.673  1.00 35.04  ? 3663 THR A CB    1 
ATOM   15611 O  OG1   . THR A 1 3663 ? 115.539 68.698  76.317  1.00 41.37  ? 3663 THR A OG1   1 
ATOM   15612 C  CG2   . THR A 1 3663 ? 113.915 68.744  78.095  1.00 34.61  ? 3663 THR A CG2   1 
ATOM   15613 N  N     . LEU A 1 3664 ? 110.814 68.272  75.964  1.00 28.54  ? 3664 LEU A N     1 
ATOM   15614 C  CA    . LEU A 1 3664 ? 109.432 68.620  76.271  1.00 26.29  ? 3664 LEU A CA    1 
ATOM   15615 C  C     . LEU A 1 3664 ? 109.167 68.153  77.698  1.00 34.04  ? 3664 LEU A C     1 
ATOM   15616 O  O     . LEU A 1 3664 ? 109.234 66.955  77.993  1.00 42.70  ? 3664 LEU A O     1 
ATOM   15617 C  CB    . LEU A 1 3664 ? 108.473 67.975  75.276  1.00 22.64  ? 3664 LEU A CB    1 
ATOM   15618 C  CG    . LEU A 1 3664 ? 107.017 68.422  75.381  1.00 28.25  ? 3664 LEU A CG    1 
ATOM   15619 C  CD1   . LEU A 1 3664 ? 106.898 69.850  74.886  1.00 28.38  ? 3664 LEU A CD1   1 
ATOM   15620 C  CD2   . LEU A 1 3664 ? 106.105 67.495  74.593  1.00 25.81  ? 3664 LEU A CD2   1 
ATOM   15621 N  N     . GLY A 1 3665 ? 108.870 69.102  78.579  1.00 37.49  ? 3665 GLY A N     1 
ATOM   15622 C  CA    . GLY A 1 3665 ? 108.733 68.766  79.987  1.00 36.89  ? 3665 GLY A CA    1 
ATOM   15623 C  C     . GLY A 1 3665 ? 110.025 68.169  80.507  1.00 38.99  ? 3665 GLY A C     1 
ATOM   15624 O  O     . GLY A 1 3665 ? 111.108 68.742  80.349  1.00 41.81  ? 3665 GLY A O     1 
ATOM   15625 N  N     . ASP A 1 3666 ? 109.918 67.000  81.129  1.00 45.08  ? 3666 ASP A N     1 
ATOM   15626 C  CA    . ASP A 1 3666 ? 111.078 66.268  81.615  1.00 48.77  ? 3666 ASP A CA    1 
ATOM   15627 C  C     . ASP A 1 3666 ? 111.534 65.174  80.658  1.00 51.05  ? 3666 ASP A C     1 
ATOM   15628 O  O     . ASP A 1 3666 ? 112.437 64.407  81.007  1.00 55.85  ? 3666 ASP A O     1 
ATOM   15629 C  CB    . ASP A 1 3666 ? 110.776 65.656  82.986  1.00 56.08  ? 3666 ASP A CB    1 
ATOM   15630 C  CG    . ASP A 1 3666 ? 109.651 64.640  82.935  1.00 63.71  ? 3666 ASP A CG    1 
ATOM   15631 O  OD1   . ASP A 1 3666 ? 108.552 64.993  82.458  1.00 59.89  ? 3666 ASP A OD1   1 
ATOM   15632 O  OD2   . ASP A 1 3666 ? 109.865 63.490  83.370  1.00 72.13  ? 3666 ASP A OD2   1 
ATOM   15633 N  N     . GLN A 1 3667 ? 110.942 65.082  79.470  1.00 46.38  ? 3667 GLN A N     1 
ATOM   15634 C  CA    . GLN A 1 3667 ? 111.204 63.985  78.548  1.00 42.60  ? 3667 GLN A CA    1 
ATOM   15635 C  C     . GLN A 1 3667 ? 111.775 64.527  77.245  1.00 41.20  ? 3667 GLN A C     1 
ATOM   15636 O  O     . GLN A 1 3667 ? 111.278 65.522  76.711  1.00 41.68  ? 3667 GLN A O     1 
ATOM   15637 C  CB    . GLN A 1 3667 ? 109.923 63.186  78.285  1.00 49.91  ? 3667 GLN A CB    1 
ATOM   15638 C  CG    . GLN A 1 3667 ? 109.961 62.314  77.043  1.00 51.73  ? 3667 GLN A CG    1 
ATOM   15639 C  CD    . GLN A 1 3667 ? 108.589 62.134  76.427  1.00 57.30  ? 3667 GLN A CD    1 
ATOM   15640 O  OE1   . GLN A 1 3667 ? 107.731 63.010  76.534  1.00 58.12  ? 3667 GLN A OE1   1 
ATOM   15641 N  NE2   . GLN A 1 3667 ? 108.375 60.995  75.779  1.00 57.12  ? 3667 GLN A NE2   1 
ATOM   15642 N  N     . ASP A 1 3668 ? 112.813 63.871  76.737  1.00 40.86  ? 3668 ASP A N     1 
ATOM   15643 C  CA    . ASP A 1 3668 ? 113.424 64.259  75.474  1.00 37.36  ? 3668 ASP A CA    1 
ATOM   15644 C  C     . ASP A 1 3668 ? 112.812 63.475  74.316  1.00 35.99  ? 3668 ASP A C     1 
ATOM   15645 O  O     . ASP A 1 3668 ? 112.540 62.277  74.431  1.00 41.61  ? 3668 ASP A O     1 
ATOM   15646 C  CB    . ASP A 1 3668 ? 114.942 64.064  75.531  1.00 42.03  ? 3668 ASP A CB    1 
ATOM   15647 C  CG    . ASP A 1 3668 ? 115.348 62.640  75.880  1.00 59.38  ? 3668 ASP A CG    1 
ATOM   15648 O  OD1   . ASP A 1 3668 ? 114.469 61.809  76.188  1.00 66.80  ? 3668 ASP A OD1   1 
ATOM   15649 O  OD2   . ASP A 1 3668 ? 116.563 62.350  75.846  1.00 59.57  ? 3668 ASP A OD2   1 
ATOM   15650 N  N     . ILE A 1 3669 ? 112.574 64.170  73.204  1.00 27.15  ? 3669 ILE A N     1 
ATOM   15651 C  CA    . ILE A 1 3669 ? 111.882 63.612  72.049  1.00 22.56  ? 3669 ILE A CA    1 
ATOM   15652 C  C     . ILE A 1 3669 ? 112.713 63.874  70.801  1.00 22.84  ? 3669 ILE A C     1 
ATOM   15653 O  O     . ILE A 1 3669 ? 113.244 64.975  70.618  1.00 21.70  ? 3669 ILE A O     1 
ATOM   15654 C  CB    . ILE A 1 3669 ? 110.468 64.213  71.889  1.00 23.58  ? 3669 ILE A CB    1 
ATOM   15655 C  CG1   . ILE A 1 3669 ? 109.682 64.101  73.197  1.00 31.87  ? 3669 ILE A CG1   1 
ATOM   15656 C  CG2   . ILE A 1 3669 ? 109.716 63.532  70.755  1.00 22.96  ? 3669 ILE A CG2   1 
ATOM   15657 C  CD1   . ILE A 1 3669 ? 108.327 64.763  73.149  1.00 32.73  ? 3669 ILE A CD1   1 
ATOM   15658 N  N     . ASP A 1 3670 ? 112.825 62.863  69.943  1.00 24.10  ? 3670 ASP A N     1 
ATOM   15659 C  CA    . ASP A 1 3670 ? 113.491 63.035  68.659  1.00 21.31  ? 3670 ASP A CA    1 
ATOM   15660 C  C     . ASP A 1 3670 ? 112.653 63.945  67.768  1.00 20.13  ? 3670 ASP A C     1 
ATOM   15661 O  O     . ASP A 1 3670 ? 111.567 63.559  67.323  1.00 22.25  ? 3670 ASP A O     1 
ATOM   15662 C  CB    . ASP A 1 3670 ? 113.712 61.681  67.989  1.00 24.48  ? 3670 ASP A CB    1 
ATOM   15663 C  CG    . ASP A 1 3670 ? 114.736 60.831  68.714  1.00 33.05  ? 3670 ASP A CG    1 
ATOM   15664 O  OD1   . ASP A 1 3670 ? 115.648 61.405  69.345  1.00 32.38  ? 3670 ASP A OD1   1 
ATOM   15665 O  OD2   . ASP A 1 3670 ? 114.628 59.588  68.655  1.00 39.77  ? 3670 ASP A OD2   1 
ATOM   15666 N  N     . LEU A 1 3671 ? 113.154 65.149  67.508  1.00 22.25  ? 3671 LEU A N     1 
ATOM   15667 C  CA    . LEU A 1 3671 ? 112.419 66.147  66.741  1.00 20.10  ? 3671 LEU A CA    1 
ATOM   15668 C  C     . LEU A 1 3671 ? 112.591 65.885  65.249  1.00 22.49  ? 3671 LEU A C     1 
ATOM   15669 O  O     . LEU A 1 3671 ? 113.719 65.834  64.747  1.00 27.00  ? 3671 LEU A O     1 
ATOM   15670 C  CB    . LEU A 1 3671 ? 112.892 67.557  67.091  1.00 19.39  ? 3671 LEU A CB    1 
ATOM   15671 C  CG    . LEU A 1 3671 ? 112.262 68.672  66.255  1.00 18.57  ? 3671 LEU A CG    1 
ATOM   15672 C  CD1   . LEU A 1 3671 ? 110.758 68.717  66.463  1.00 18.17  ? 3671 LEU A CD1   1 
ATOM   15673 C  CD2   . LEU A 1 3671 ? 112.888 70.014  66.585  1.00 18.70  ? 3671 LEU A CD2   1 
ATOM   15674 N  N     . SER A 1 3672 ? 111.474 65.722  64.548  1.00 19.39  ? 3672 SER A N     1 
ATOM   15675 C  CA    . SER A 1 3672 ? 111.510 65.567  63.102  1.00 20.69  ? 3672 SER A CA    1 
ATOM   15676 C  C     . SER A 1 3672 ? 111.528 66.939  62.429  1.00 21.91  ? 3672 SER A C     1 
ATOM   15677 O  O     . SER A 1 3672 ? 110.833 67.857  62.872  1.00 24.31  ? 3672 SER A O     1 
ATOM   15678 C  CB    . SER A 1 3672 ? 110.308 64.763  62.617  1.00 21.13  ? 3672 SER A CB    1 
ATOM   15679 O  OG    . SER A 1 3672 ? 110.137 64.892  61.216  1.00 25.49  ? 3672 SER A OG    1 
ATOM   15680 N  N     . PRO A 1 3673 ? 112.318 67.106  61.363  1.00 23.00  ? 3673 PRO A N     1 
ATOM   15681 C  CA    . PRO A 1 3673 ? 112.425 68.430  60.728  1.00 22.81  ? 3673 PRO A CA    1 
ATOM   15682 C  C     . PRO A 1 3673 ? 111.137 68.919  60.087  1.00 23.15  ? 3673 PRO A C     1 
ATOM   15683 O  O     . PRO A 1 3673 ? 111.016 70.124  59.832  1.00 23.34  ? 3673 PRO A O     1 
ATOM   15684 C  CB    . PRO A 1 3673 ? 113.526 68.225  59.680  1.00 24.53  ? 3673 PRO A CB    1 
ATOM   15685 C  CG    . PRO A 1 3673 ? 113.472 66.766  59.370  1.00 25.73  ? 3673 PRO A CG    1 
ATOM   15686 C  CD    . PRO A 1 3673 ? 113.133 66.094  60.671  1.00 25.32  ? 3673 PRO A CD    1 
ATOM   15687 N  N     . SER A 1 3674 ? 110.176 68.039  59.821  1.00 22.72  ? 3674 SER A N     1 
ATOM   15688 C  CA    . SER A 1 3674 ? 108.939 68.423  59.155  1.00 19.41  ? 3674 SER A CA    1 
ATOM   15689 C  C     . SER A 1 3674 ? 107.874 68.933  60.118  1.00 20.96  ? 3674 SER A C     1 
ATOM   15690 O  O     . SER A 1 3674 ? 106.774 69.277  59.674  1.00 20.52  ? 3674 SER A O     1 
ATOM   15691 C  CB    . SER A 1 3674 ? 108.385 67.240  58.353  1.00 19.96  ? 3674 SER A CB    1 
ATOM   15692 O  OG    . SER A 1 3674 ? 108.407 66.048  59.118  1.00 28.65  ? 3674 SER A OG    1 
ATOM   15693 N  N     . PHE A 1 3675 ? 108.168 68.988  61.414  1.00 17.86  ? 3675 PHE A N     1 
ATOM   15694 C  CA    . PHE A 1 3675 ? 107.200 69.487  62.381  1.00 13.42  ? 3675 PHE A CA    1 
ATOM   15695 C  C     . PHE A 1 3675 ? 106.975 70.984  62.207  1.00 12.66  ? 3675 PHE A C     1 
ATOM   15696 O  O     . PHE A 1 3675 ? 107.907 71.744  61.930  1.00 14.46  ? 3675 PHE A O     1 
ATOM   15697 C  CB    . PHE A 1 3675 ? 107.665 69.187  63.808  1.00 10.77  ? 3675 PHE A CB    1 
ATOM   15698 C  CG    . PHE A 1 3675 ? 106.971 70.009  64.861  1.00 8.56   ? 3675 PHE A CG    1 
ATOM   15699 C  CD1   . PHE A 1 3675 ? 105.748 69.613  65.374  1.00 8.17   ? 3675 PHE A CD1   1 
ATOM   15700 C  CD2   . PHE A 1 3675 ? 107.551 71.169  65.350  1.00 8.04   ? 3675 PHE A CD2   1 
ATOM   15701 C  CE1   . PHE A 1 3675 ? 105.110 70.363  66.341  1.00 7.27   ? 3675 PHE A CE1   1 
ATOM   15702 C  CE2   . PHE A 1 3675 ? 106.916 71.924  66.316  1.00 7.78   ? 3675 PHE A CE2   1 
ATOM   15703 C  CZ    . PHE A 1 3675 ? 105.695 71.519  66.813  1.00 6.33   ? 3675 PHE A CZ    1 
ATOM   15704 N  N     . VAL A 1 3676 ? 105.724 71.402  62.376  1.00 9.33   ? 3676 VAL A N     1 
ATOM   15705 C  CA    . VAL A 1 3676 ? 105.351 72.812  62.374  1.00 7.59   ? 3676 VAL A CA    1 
ATOM   15706 C  C     . VAL A 1 3676 ? 104.117 72.964  63.252  1.00 7.82   ? 3676 VAL A C     1 
ATOM   15707 O  O     . VAL A 1 3676 ? 103.294 72.050  63.347  1.00 9.15   ? 3676 VAL A O     1 
ATOM   15708 C  CB    . VAL A 1 3676 ? 105.113 73.331  60.937  1.00 7.73   ? 3676 VAL A CB    1 
ATOM   15709 C  CG1   . VAL A 1 3676 ? 103.939 72.619  60.291  1.00 7.71   ? 3676 VAL A CG1   1 
ATOM   15710 C  CG2   . VAL A 1 3676 ? 104.895 74.830  60.937  1.00 9.17   ? 3676 VAL A CG2   1 
ATOM   15711 N  N     . ILE A 1 3677 ? 104.000 74.111  63.917  1.00 6.90   ? 3677 ILE A N     1 
ATOM   15712 C  CA    . ILE A 1 3677 ? 102.921 74.358  64.865  1.00 6.33   ? 3677 ILE A CA    1 
ATOM   15713 C  C     . ILE A 1 3677 ? 102.324 75.734  64.604  1.00 7.60   ? 3677 ILE A C     1 
ATOM   15714 O  O     . ILE A 1 3677 ? 103.049 76.705  64.361  1.00 9.01   ? 3677 ILE A O     1 
ATOM   15715 C  CB    . ILE A 1 3677 ? 103.410 74.229  66.326  1.00 6.61   ? 3677 ILE A CB    1 
ATOM   15716 C  CG1   . ILE A 1 3677 ? 102.279 74.540  67.309  1.00 6.58   ? 3677 ILE A CG1   1 
ATOM   15717 C  CG2   . ILE A 1 3677 ? 104.627 75.110  66.578  1.00 4.75   ? 3677 ILE A CG2   1 
ATOM   15718 C  CD1   . ILE A 1 3677 ? 102.514 73.991  68.694  1.00 6.78   ? 3677 ILE A CD1   1 
ATOM   15719 N  N     . PHE A 1 3678 ? 100.995 75.809  64.639  1.00 6.62   ? 3678 PHE A N     1 
ATOM   15720 C  CA    . PHE A 1 3678 ? 100.258 77.051  64.458  1.00 6.01   ? 3678 PHE A CA    1 
ATOM   15721 C  C     . PHE A 1 3678 ? 99.369  77.289  65.669  1.00 6.74   ? 3678 PHE A C     1 
ATOM   15722 O  O     . PHE A 1 3678 ? 98.469  76.490  65.945  1.00 10.60  ? 3678 PHE A O     1 
ATOM   15723 C  CB    . PHE A 1 3678 ? 99.400  77.006  63.188  1.00 6.64   ? 3678 PHE A CB    1 
ATOM   15724 C  CG    . PHE A 1 3678 ? 100.185 76.809  61.924  1.00 7.15   ? 3678 PHE A CG    1 
ATOM   15725 C  CD1   . PHE A 1 3678 ? 100.463 75.535  61.456  1.00 7.98   ? 3678 PHE A CD1   1 
ATOM   15726 C  CD2   . PHE A 1 3678 ? 100.631 77.897  61.193  1.00 7.47   ? 3678 PHE A CD2   1 
ATOM   15727 C  CE1   . PHE A 1 3678 ? 101.179 75.351  60.289  1.00 8.70   ? 3678 PHE A CE1   1 
ATOM   15728 C  CE2   . PHE A 1 3678 ? 101.347 77.720  60.025  1.00 8.57   ? 3678 PHE A CE2   1 
ATOM   15729 C  CZ    . PHE A 1 3678 ? 101.622 76.445  59.573  1.00 9.26   ? 3678 PHE A CZ    1 
ATOM   15730 N  N     . LEU A 1 3679 ? 99.603  78.391  66.376  1.00 6.19   ? 3679 LEU A N     1 
ATOM   15731 C  CA    . LEU A 1 3679 ? 98.779  78.780  67.512  1.00 9.77   ? 3679 LEU A CA    1 
ATOM   15732 C  C     . LEU A 1 3679 ? 97.699  79.752  67.056  1.00 7.75   ? 3679 LEU A C     1 
ATOM   15733 O  O     . LEU A 1 3679 ? 97.969  80.675  66.283  1.00 8.62   ? 3679 LEU A O     1 
ATOM   15734 C  CB    . LEU A 1 3679 ? 99.626  79.415  68.617  1.00 9.83   ? 3679 LEU A CB    1 
ATOM   15735 C  CG    . LEU A 1 3679 ? 100.894 78.667  69.034  1.00 9.61   ? 3679 LEU A CG    1 
ATOM   15736 C  CD1   . LEU A 1 3679 ? 101.582 79.370  70.193  1.00 9.50   ? 3679 LEU A CD1   1 
ATOM   15737 C  CD2   . LEU A 1 3679 ? 100.571 77.225  69.395  1.00 8.91   ? 3679 LEU A CD2   1 
ATOM   15738 N  N     . SER A 1 3680 ? 96.473  79.537  67.530  1.00 8.41   ? 3680 SER A N     1 
ATOM   15739 C  CA    . SER A 1 3680 ? 95.340  80.329  67.076  1.00 8.16   ? 3680 SER A CA    1 
ATOM   15740 C  C     . SER A 1 3680 ? 94.493  80.777  68.258  1.00 10.04  ? 3680 SER A C     1 
ATOM   15741 O  O     . SER A 1 3680 ? 94.454  80.121  69.302  1.00 12.23  ? 3680 SER A O     1 
ATOM   15742 C  CB    . SER A 1 3680 ? 94.467  79.547  66.085  1.00 11.10  ? 3680 SER A CB    1 
ATOM   15743 O  OG    . SER A 1 3680 ? 94.121  78.276  66.605  1.00 17.39  ? 3680 SER A OG    1 
ATOM   15744 N  N     . THR A 1 3681 ? 93.818  81.910  68.077  1.00 9.99   ? 3681 THR A N     1 
ATOM   15745 C  CA    . THR A 1 3681 ? 92.841  82.411  69.031  1.00 10.37  ? 3681 THR A CA    1 
ATOM   15746 C  C     . THR A 1 3681 ? 91.708  83.087  68.274  1.00 12.30  ? 3681 THR A C     1 
ATOM   15747 O  O     . THR A 1 3681 ? 91.896  83.590  67.163  1.00 12.35  ? 3681 THR A O     1 
ATOM   15748 C  CB    . THR A 1 3681 ? 93.461  83.400  70.029  1.00 13.19  ? 3681 THR A CB    1 
ATOM   15749 O  OG1   . THR A 1 3681 ? 92.446  83.893  70.912  1.00 17.71  ? 3681 THR A OG1   1 
ATOM   15750 C  CG2   . THR A 1 3681 ? 94.107  84.570  69.300  1.00 10.89  ? 3681 THR A CG2   1 
ATOM   15751 N  N     . ARG A 1 3682 ? 90.525  83.088  68.883  1.00 18.43  ? 3682 ARG A N     1 
ATOM   15752 C  CA    . ARG A 1 3682 ? 89.362  83.757  68.319  1.00 18.22  ? 3682 ARG A CA    1 
ATOM   15753 C  C     . ARG A 1 3682 ? 89.033  85.068  69.019  1.00 18.80  ? 3682 ARG A C     1 
ATOM   15754 O  O     . ARG A 1 3682 ? 88.042  85.712  68.664  1.00 22.97  ? 3682 ARG A O     1 
ATOM   15755 C  CB    . ARG A 1 3682 ? 88.142  82.834  68.362  1.00 13.55  ? 3682 ARG A CB    1 
ATOM   15756 C  CG    . ARG A 1 3682 ? 88.212  81.661  67.401  1.00 17.70  ? 3682 ARG A CG    1 
ATOM   15757 C  CD    . ARG A 1 3682 ? 86.922  80.864  67.429  1.00 18.37  ? 3682 ARG A CD    1 
ATOM   15758 N  NE    . ARG A 1 3682 ? 86.733  80.182  68.703  1.00 20.11  ? 3682 ARG A NE    1 
ATOM   15759 C  CZ    . ARG A 1 3682 ? 85.854  80.552  69.624  1.00 22.07  ? 3682 ARG A CZ    1 
ATOM   15760 N  NH1   . ARG A 1 3682 ? 85.061  81.595  69.443  1.00 17.08  ? 3682 ARG A NH1   1 
ATOM   15761 N  NH2   . ARG A 1 3682 ? 85.770  79.859  70.756  1.00 22.95  ? 3682 ARG A NH2   1 
ATOM   15762 N  N     . ASP A 1 3683 ? 89.837  85.481  69.998  1.00 16.26  ? 3683 ASP A N     1 
ATOM   15763 C  CA    . ASP A 1 3683 ? 89.600  86.731  70.701  1.00 19.02  ? 3683 ASP A CA    1 
ATOM   15764 C  C     . ASP A 1 3683 ? 90.588  87.776  70.210  1.00 22.43  ? 3683 ASP A C     1 
ATOM   15765 O  O     . ASP A 1 3683 ? 91.785  87.673  70.516  1.00 24.82  ? 3683 ASP A O     1 
ATOM   15766 C  CB    . ASP A 1 3683 ? 89.737  86.536  72.209  1.00 19.00  ? 3683 ASP A CB    1 
ATOM   15767 C  CG    . ASP A 1 3683 ? 89.311  87.759  72.996  1.00 32.10  ? 3683 ASP A CG    1 
ATOM   15768 O  OD1   . ASP A 1 3683 ? 88.199  88.269  72.746  1.00 39.26  ? 3683 ASP A OD1   1 
ATOM   15769 O  OD2   . ASP A 1 3683 ? 90.087  88.211  73.863  1.00 38.84  ? 3683 ASP A OD2   1 
ATOM   15770 N  N     . PRO A 1 3684 ? 90.153  88.786  69.450  1.00 21.81  ? 3684 PRO A N     1 
ATOM   15771 C  CA    . PRO A 1 3684 ? 91.095  89.813  68.979  1.00 23.53  ? 3684 PRO A CA    1 
ATOM   15772 C  C     . PRO A 1 3684 ? 91.595  90.740  70.075  1.00 27.40  ? 3684 PRO A C     1 
ATOM   15773 O  O     . PRO A 1 3684 ? 92.610  91.417  69.867  1.00 31.46  ? 3684 PRO A O     1 
ATOM   15774 C  CB    . PRO A 1 3684 ? 90.278  90.582  67.935  1.00 22.75  ? 3684 PRO A CB    1 
ATOM   15775 C  CG    . PRO A 1 3684 ? 88.864  90.402  68.373  1.00 23.99  ? 3684 PRO A CG    1 
ATOM   15776 C  CD    . PRO A 1 3684 ? 88.787  89.015  68.950  1.00 21.17  ? 3684 PRO A CD    1 
ATOM   15777 N  N     . THR A 1 3685 ? 90.925  90.793  71.224  1.00 28.39  ? 3685 THR A N     1 
ATOM   15778 C  CA    . THR A 1 3685 ? 91.270  91.723  72.290  1.00 28.28  ? 3685 THR A CA    1 
ATOM   15779 C  C     . THR A 1 3685 ? 92.133  91.101  73.380  1.00 30.14  ? 3685 THR A C     1 
ATOM   15780 O  O     . THR A 1 3685 ? 92.410  91.767  74.382  1.00 41.44  ? 3685 THR A O     1 
ATOM   15781 C  CB    . THR A 1 3685 ? 89.997  92.300  72.919  1.00 35.16  ? 3685 THR A CB    1 
ATOM   15782 O  OG1   . THR A 1 3685 ? 89.466  91.369  73.871  1.00 35.18  ? 3685 THR A OG1   1 
ATOM   15783 C  CG2   . THR A 1 3685 ? 88.951  92.575  71.849  1.00 31.32  ? 3685 THR A CG2   1 
ATOM   15784 N  N     . VAL A 1 3686 ? 92.562  89.854  73.218  1.00 26.75  ? 3686 VAL A N     1 
ATOM   15785 C  CA    . VAL A 1 3686 ? 93.349  89.185  74.248  1.00 29.10  ? 3686 VAL A CA    1 
ATOM   15786 C  C     . VAL A 1 3686 ? 94.755  89.769  74.273  1.00 27.94  ? 3686 VAL A C     1 
ATOM   15787 O  O     . VAL A 1 3686 ? 95.357  90.044  73.227  1.00 29.65  ? 3686 VAL A O     1 
ATOM   15788 C  CB    . VAL A 1 3686 ? 93.364  87.661  74.019  1.00 31.13  ? 3686 VAL A CB    1 
ATOM   15789 C  CG1   . VAL A 1 3686 ? 94.051  87.308  72.710  1.00 23.94  ? 3686 VAL A CG1   1 
ATOM   15790 C  CG2   . VAL A 1 3686 ? 94.033  86.951  75.188  1.00 31.21  ? 3686 VAL A CG2   1 
ATOM   15791 N  N     . GLU A 1 3687 ? 95.273  89.989  75.478  1.00 35.42  ? 3687 GLU A N     1 
ATOM   15792 C  CA    . GLU A 1 3687 ? 96.610  90.531  75.676  1.00 30.92  ? 3687 GLU A CA    1 
ATOM   15793 C  C     . GLU A 1 3687 ? 97.590  89.391  75.915  1.00 25.54  ? 3687 GLU A C     1 
ATOM   15794 O  O     . GLU A 1 3687 ? 97.347  88.524  76.761  1.00 33.65  ? 3687 GLU A O     1 
ATOM   15795 C  CB    . GLU A 1 3687 ? 96.636  91.503  76.857  1.00 36.23  ? 3687 GLU A CB    1 
ATOM   15796 C  CG    . GLU A 1 3687 ? 95.465  92.470  76.897  1.00 43.22  ? 3687 GLU A CG    1 
ATOM   15797 C  CD    . GLU A 1 3687 ? 95.815  93.828  76.323  1.00 51.88  ? 3687 GLU A CD    1 
ATOM   15798 O  OE1   . GLU A 1 3687 ? 96.900  93.956  75.717  1.00 46.67  ? 3687 GLU A OE1   1 
ATOM   15799 O  OE2   . GLU A 1 3687 ? 95.006  94.767  76.477  1.00 53.14  ? 3687 GLU A OE2   1 
ATOM   15800 N  N     . PHE A 1 3688 ? 98.691  89.395  75.172  1.00 20.00  ? 3688 PHE A N     1 
ATOM   15801 C  CA    . PHE A 1 3688 ? 99.706  88.377  75.362  1.00 19.24  ? 3688 PHE A CA    1 
ATOM   15802 C  C     . PHE A 1 3688 ? 100.904 88.945  76.115  1.00 23.17  ? 3688 PHE A C     1 
ATOM   15803 O  O     . PHE A 1 3688 ? 101.291 90.098  75.903  1.00 23.88  ? 3688 PHE A O     1 
ATOM   15804 C  CB    . PHE A 1 3688 ? 100.184 87.801  74.024  1.00 18.21  ? 3688 PHE A CB    1 
ATOM   15805 C  CG    . PHE A 1 3688 ? 99.103  87.126  73.234  1.00 15.68  ? 3688 PHE A CG    1 
ATOM   15806 C  CD1   . PHE A 1 3688 ? 98.714  85.834  73.538  1.00 15.52  ? 3688 PHE A CD1   1 
ATOM   15807 C  CD2   . PHE A 1 3688 ? 98.482  87.779  72.184  1.00 13.59  ? 3688 PHE A CD2   1 
ATOM   15808 C  CE1   . PHE A 1 3688 ? 97.723  85.208  72.815  1.00 14.32  ? 3688 PHE A CE1   1 
ATOM   15809 C  CE2   . PHE A 1 3688 ? 97.490  87.156  71.455  1.00 14.09  ? 3688 PHE A CE2   1 
ATOM   15810 C  CZ    . PHE A 1 3688 ? 97.111  85.868  71.771  1.00 12.72  ? 3688 PHE A CZ    1 
ATOM   15811 N  N     . PRO A 1 3689 ? 101.507 88.161  77.004  1.00 25.30  ? 3689 PRO A N     1 
ATOM   15812 C  CA    . PRO A 1 3689 ? 102.705 88.619  77.711  1.00 19.28  ? 3689 PRO A CA    1 
ATOM   15813 C  C     . PRO A 1 3689 ? 103.867 88.796  76.751  1.00 16.88  ? 3689 PRO A C     1 
ATOM   15814 O  O     . PRO A 1 3689 ? 103.920 88.138  75.701  1.00 17.15  ? 3689 PRO A O     1 
ATOM   15815 C  CB    . PRO A 1 3689 ? 102.971 87.489  78.717  1.00 21.38  ? 3689 PRO A CB    1 
ATOM   15816 C  CG    . PRO A 1 3689 ? 102.348 86.287  78.087  1.00 19.69  ? 3689 PRO A CG    1 
ATOM   15817 C  CD    . PRO A 1 3689 ? 101.110 86.805  77.417  1.00 20.23  ? 3689 PRO A CD    1 
ATOM   15818 N  N     . PRO A 1 3690 ? 104.809 89.687  77.069  1.00 18.39  ? 3690 PRO A N     1 
ATOM   15819 C  CA    . PRO A 1 3690 ? 105.928 89.936  76.144  1.00 16.80  ? 3690 PRO A CA    1 
ATOM   15820 C  C     . PRO A 1 3690 ? 106.752 88.700  75.828  1.00 13.01  ? 3690 PRO A C     1 
ATOM   15821 O  O     . PRO A 1 3690 ? 107.264 88.579  74.707  1.00 13.51  ? 3690 PRO A O     1 
ATOM   15822 C  CB    . PRO A 1 3690 ? 106.758 90.992  76.888  1.00 18.49  ? 3690 PRO A CB    1 
ATOM   15823 C  CG    . PRO A 1 3690 ? 105.775 91.675  77.781  1.00 19.15  ? 3690 PRO A CG    1 
ATOM   15824 C  CD    . PRO A 1 3690 ? 104.845 90.589  78.233  1.00 18.24  ? 3690 PRO A CD    1 
ATOM   15825 N  N     . ASP A 1 3691 ? 106.898 87.777  76.783  1.00 14.41  ? 3691 ASP A N     1 
ATOM   15826 C  CA    . ASP A 1 3691 ? 107.665 86.564  76.520  1.00 17.58  ? 3691 ASP A CA    1 
ATOM   15827 C  C     . ASP A 1 3691 ? 107.012 85.720  75.430  1.00 14.46  ? 3691 ASP A C     1 
ATOM   15828 O  O     . ASP A 1 3691 ? 107.701 85.185  74.555  1.00 12.13  ? 3691 ASP A O     1 
ATOM   15829 C  CB    . ASP A 1 3691 ? 107.846 85.761  77.812  1.00 18.69  ? 3691 ASP A CB    1 
ATOM   15830 C  CG    . ASP A 1 3691 ? 106.532 85.278  78.403  1.00 31.10  ? 3691 ASP A CG    1 
ATOM   15831 O  OD1   . ASP A 1 3691 ? 105.460 85.592  77.844  1.00 30.08  ? 3691 ASP A OD1   1 
ATOM   15832 O  OD2   . ASP A 1 3691 ? 106.572 84.577  79.435  1.00 45.82  ? 3691 ASP A OD2   1 
ATOM   15833 N  N     . LEU A 1 3692 ? 105.683 85.597  75.461  1.00 14.39  ? 3692 LEU A N     1 
ATOM   15834 C  CA    . LEU A 1 3692 ? 104.987 84.892  74.391  1.00 11.37  ? 3692 LEU A CA    1 
ATOM   15835 C  C     . LEU A 1 3692 ? 105.044 85.667  73.082  1.00 9.43   ? 3692 LEU A C     1 
ATOM   15836 O  O     . LEU A 1 3692 ? 105.108 85.060  72.007  1.00 10.61  ? 3692 LEU A O     1 
ATOM   15837 C  CB    . LEU A 1 3692 ? 103.535 84.626  74.788  1.00 14.75  ? 3692 LEU A CB    1 
ATOM   15838 C  CG    . LEU A 1 3692 ? 102.746 83.690  73.869  1.00 12.09  ? 3692 LEU A CG    1 
ATOM   15839 C  CD1   . LEU A 1 3692 ? 103.459 82.356  73.718  1.00 9.28   ? 3692 LEU A CD1   1 
ATOM   15840 C  CD2   . LEU A 1 3692 ? 101.332 83.488  74.387  1.00 11.36  ? 3692 LEU A CD2   1 
ATOM   15841 N  N     . CYS A 1 3693 ? 105.023 87.000  73.151  1.00 10.21  ? 3693 CYS A N     1 
ATOM   15842 C  CA    . CYS A 1 3693 ? 105.105 87.807  71.938  1.00 8.46   ? 3693 CYS A CA    1 
ATOM   15843 C  C     . CYS A 1 3693 ? 106.457 87.658  71.256  1.00 10.30  ? 3693 CYS A C     1 
ATOM   15844 O  O     . CYS A 1 3693 ? 106.543 87.753  70.026  1.00 11.37  ? 3693 CYS A O     1 
ATOM   15845 C  CB    . CYS A 1 3693 ? 104.839 89.276  72.266  1.00 9.34   ? 3693 CYS A CB    1 
ATOM   15846 S  SG    . CYS A 1 3693 ? 103.188 89.606  72.913  1.00 22.86  ? 3693 CYS A SG    1 
ATOM   15847 N  N     . SER A 1 3694 ? 107.518 87.428  72.031  1.00 8.89   ? 3694 SER A N     1 
ATOM   15848 C  CA    . SER A 1 3694 ? 108.851 87.294  71.458  1.00 6.98   ? 3694 SER A CA    1 
ATOM   15849 C  C     . SER A 1 3694 ? 109.063 85.968  70.738  1.00 8.81   ? 3694 SER A C     1 
ATOM   15850 O  O     . SER A 1 3694 ? 109.960 85.879  69.894  1.00 9.25   ? 3694 SER A O     1 
ATOM   15851 C  CB    . SER A 1 3694 ? 109.910 87.454  72.551  1.00 9.04   ? 3694 SER A CB    1 
ATOM   15852 O  OG    . SER A 1 3694 ? 109.762 86.466  73.556  1.00 13.91  ? 3694 SER A OG    1 
ATOM   15853 N  N     . ARG A 1 3695 ? 108.267 84.945  71.040  1.00 7.82   ? 3695 ARG A N     1 
ATOM   15854 C  CA    . ARG A 1 3695 ? 108.474 83.612  70.489  1.00 7.96   ? 3695 ARG A CA    1 
ATOM   15855 C  C     . ARG A 1 3695 ? 107.573 83.293  69.305  1.00 8.18   ? 3695 ARG A C     1 
ATOM   15856 O  O     . ARG A 1 3695 ? 107.730 82.228  68.699  1.00 8.18   ? 3695 ARG A O     1 
ATOM   15857 C  CB    . ARG A 1 3695 ? 108.267 82.554  71.578  1.00 8.88   ? 3695 ARG A CB    1 
ATOM   15858 C  CG    . ARG A 1 3695 ? 108.943 82.874  72.894  1.00 12.85  ? 3695 ARG A CG    1 
ATOM   15859 C  CD    . ARG A 1 3695 ? 108.598 81.844  73.955  1.00 11.07  ? 3695 ARG A CD    1 
ATOM   15860 N  NE    . ARG A 1 3695 ? 108.903 82.326  75.297  1.00 15.06  ? 3695 ARG A NE    1 
ATOM   15861 C  CZ    . ARG A 1 3695 ? 109.746 81.737  76.132  1.00 16.14  ? 3695 ARG A CZ    1 
ATOM   15862 N  NH1   . ARG A 1 3695 ? 110.392 80.632  75.797  1.00 16.32  ? 3695 ARG A NH1   1 
ATOM   15863 N  NH2   . ARG A 1 3695 ? 109.947 82.269  77.334  1.00 16.30  ? 3695 ARG A NH2   1 
ATOM   15864 N  N     . VAL A 1 3696 ? 106.639 84.177  68.952  1.00 8.59   ? 3696 VAL A N     1 
ATOM   15865 C  CA    . VAL A 1 3696 ? 105.649 83.885  67.924  1.00 7.21   ? 3696 VAL A CA    1 
ATOM   15866 C  C     . VAL A 1 3696 ? 105.655 84.987  66.875  1.00 6.22   ? 3696 VAL A C     1 
ATOM   15867 O  O     . VAL A 1 3696 ? 106.134 86.099  67.105  1.00 10.56  ? 3696 VAL A O     1 
ATOM   15868 C  CB    . VAL A 1 3696 ? 104.224 83.726  68.506  1.00 8.01   ? 3696 VAL A CB    1 
ATOM   15869 C  CG1   . VAL A 1 3696 ? 104.198 82.646  69.576  1.00 7.58   ? 3696 VAL A CG1   1 
ATOM   15870 C  CG2   . VAL A 1 3696 ? 103.722 85.052  69.056  1.00 5.67   ? 3696 VAL A CG2   1 
ATOM   15871 N  N     . THR A 1 3697 ? 105.116 84.655  65.706  1.00 5.67   ? 3697 THR A N     1 
ATOM   15872 C  CA    . THR A 1 3697 ? 104.888 85.611  64.628  1.00 6.01   ? 3697 THR A CA    1 
ATOM   15873 C  C     . THR A 1 3697 ? 103.393 85.901  64.577  1.00 4.63   ? 3697 THR A C     1 
ATOM   15874 O  O     . THR A 1 3697 ? 102.598 85.023  64.228  1.00 5.16   ? 3697 THR A O     1 
ATOM   15875 C  CB    . THR A 1 3697 ? 105.384 85.070  63.290  1.00 6.74   ? 3697 THR A CB    1 
ATOM   15876 O  OG1   . THR A 1 3697 ? 106.804 84.886  63.341  1.00 10.97  ? 3697 THR A OG1   1 
ATOM   15877 C  CG2   . THR A 1 3697 ? 105.041 86.037  62.172  1.00 7.24   ? 3697 THR A CG2   1 
ATOM   15878 N  N     . PHE A 1 3698 ? 103.012 87.126  64.923  1.00 4.53   ? 3698 PHE A N     1 
ATOM   15879 C  CA    . PHE A 1 3698 ? 101.600 87.477  64.954  1.00 5.91   ? 3698 PHE A CA    1 
ATOM   15880 C  C     . PHE A 1 3698 ? 101.057 87.612  63.537  1.00 5.69   ? 3698 PHE A C     1 
ATOM   15881 O  O     . PHE A 1 3698 ? 101.679 88.242  62.678  1.00 6.43   ? 3698 PHE A O     1 
ATOM   15882 C  CB    . PHE A 1 3698 ? 101.391 88.771  65.735  1.00 5.36   ? 3698 PHE A CB    1 
ATOM   15883 C  CG    . PHE A 1 3698 ? 101.412 88.583  67.222  1.00 7.76   ? 3698 PHE A CG    1 
ATOM   15884 C  CD1   . PHE A 1 3698 ? 100.382 87.915  67.861  1.00 6.35   ? 3698 PHE A CD1   1 
ATOM   15885 C  CD2   . PHE A 1 3698 ? 102.463 89.068  67.981  1.00 9.08   ? 3698 PHE A CD2   1 
ATOM   15886 C  CE1   . PHE A 1 3698 ? 100.398 87.735  69.229  1.00 7.67   ? 3698 PHE A CE1   1 
ATOM   15887 C  CE2   . PHE A 1 3698 ? 102.484 88.891  69.350  1.00 7.43   ? 3698 PHE A CE2   1 
ATOM   15888 C  CZ    . PHE A 1 3698 ? 101.450 88.223  69.975  1.00 8.67   ? 3698 PHE A CZ    1 
ATOM   15889 N  N     . VAL A 1 3699 ? 99.903  86.998  63.292  1.00 5.17   ? 3699 VAL A N     1 
ATOM   15890 C  CA    . VAL A 1 3699 ? 99.222  87.049  62.002  1.00 5.44   ? 3699 VAL A CA    1 
ATOM   15891 C  C     . VAL A 1 3699 ? 97.763  87.364  62.307  1.00 5.26   ? 3699 VAL A C     1 
ATOM   15892 O  O     . VAL A 1 3699 ? 96.986  86.467  62.652  1.00 6.30   ? 3699 VAL A O     1 
ATOM   15893 C  CB    . VAL A 1 3699 ? 99.356  85.742  61.212  1.00 5.28   ? 3699 VAL A CB    1 
ATOM   15894 C  CG1   . VAL A 1 3699 ? 98.648  85.858  59.877  1.00 3.84   ? 3699 VAL A CG1   1 
ATOM   15895 C  CG2   . VAL A 1 3699 ? 100.821 85.381  61.009  1.00 4.20   ? 3699 VAL A CG2   1 
ATOM   15896 N  N     . ASN A 1 3700 ? 97.385  88.633  62.183  1.00 6.27   ? 3700 ASN A N     1 
ATOM   15897 C  CA    . ASN A 1 3700 ? 96.071  89.105  62.598  1.00 8.33   ? 3700 ASN A CA    1 
ATOM   15898 C  C     . ASN A 1 3700 ? 95.138  89.173  61.397  1.00 7.93   ? 3700 ASN A C     1 
ATOM   15899 O  O     . ASN A 1 3700 ? 95.478  89.774  60.372  1.00 7.51   ? 3700 ASN A O     1 
ATOM   15900 C  CB    . ASN A 1 3700 ? 96.173  90.478  63.264  1.00 7.88   ? 3700 ASN A CB    1 
ATOM   15901 C  CG    . ASN A 1 3700 ? 94.956  90.812  64.104  1.00 11.35  ? 3700 ASN A CG    1 
ATOM   15902 O  OD1   . ASN A 1 3700 ? 93.946  90.111  64.062  1.00 12.54  ? 3700 ASN A OD1   1 
ATOM   15903 N  ND2   . ASN A 1 3700 ? 95.049  91.887  64.876  1.00 10.88  ? 3700 ASN A ND2   1 
ATOM   15904 N  N     . PHE A 1 3701 ? 93.964  88.561  61.530  1.00 8.98   ? 3701 PHE A N     1 
ATOM   15905 C  CA    . PHE A 1 3701 ? 92.947  88.556  60.479  1.00 8.24   ? 3701 PHE A CA    1 
ATOM   15906 C  C     . PHE A 1 3701 ? 91.847  89.529  60.889  1.00 12.97  ? 3701 PHE A C     1 
ATOM   15907 O  O     . PHE A 1 3701 ? 90.870  89.155  61.539  1.00 17.39  ? 3701 PHE A O     1 
ATOM   15908 C  CB    . PHE A 1 3701 ? 92.402  87.150  60.257  1.00 9.87   ? 3701 PHE A CB    1 
ATOM   15909 C  CG    . PHE A 1 3701 ? 93.322  86.263  59.473  1.00 8.11   ? 3701 PHE A CG    1 
ATOM   15910 C  CD1   . PHE A 1 3701 ? 94.438  85.703  60.070  1.00 6.43   ? 3701 PHE A CD1   1 
ATOM   15911 C  CD2   . PHE A 1 3701 ? 93.073  85.991  58.139  1.00 7.69   ? 3701 PHE A CD2   1 
ATOM   15912 C  CE1   . PHE A 1 3701 ? 95.286  84.888  59.354  1.00 7.48   ? 3701 PHE A CE1   1 
ATOM   15913 C  CE2   . PHE A 1 3701 ? 93.920  85.175  57.418  1.00 7.35   ? 3701 PHE A CE2   1 
ATOM   15914 C  CZ    . PHE A 1 3701 ? 95.027  84.624  58.027  1.00 6.95   ? 3701 PHE A CZ    1 
ATOM   15915 N  N     . THR A 1 3702 ? 92.012  90.789  60.505  1.00 15.55  ? 3702 THR A N     1 
ATOM   15916 C  CA    . THR A 1 3702 ? 91.035  91.827  60.795  1.00 13.86  ? 3702 THR A CA    1 
ATOM   15917 C  C     . THR A 1 3702 ? 90.205  92.131  59.556  1.00 14.97  ? 3702 THR A C     1 
ATOM   15918 O  O     . THR A 1 3702 ? 90.667  91.983  58.422  1.00 16.04  ? 3702 THR A O     1 
ATOM   15919 C  CB    . THR A 1 3702 ? 91.715  93.106  61.289  1.00 16.16  ? 3702 THR A CB    1 
ATOM   15920 O  OG1   . THR A 1 3702 ? 92.394  93.742  60.200  1.00 15.32  ? 3702 THR A OG1   1 
ATOM   15921 C  CG2   . THR A 1 3702 ? 92.711  92.788  62.390  1.00 11.39  ? 3702 THR A CG2   1 
ATOM   15922 N  N     . VAL A 1 3703 ? 88.963  92.556  59.786  1.00 18.19  ? 3703 VAL A N     1 
ATOM   15923 C  CA    . VAL A 1 3703 ? 88.061  92.868  58.686  1.00 12.90  ? 3703 VAL A CA    1 
ATOM   15924 C  C     . VAL A 1 3703 ? 88.443  94.212  58.082  1.00 11.54  ? 3703 VAL A C     1 
ATOM   15925 O  O     . VAL A 1 3703 ? 88.522  95.228  58.784  1.00 12.50  ? 3703 VAL A O     1 
ATOM   15926 C  CB    . VAL A 1 3703 ? 86.603  92.868  59.169  1.00 15.38  ? 3703 VAL A CB    1 
ATOM   15927 C  CG1   . VAL A 1 3703 ? 85.678  93.369  58.069  1.00 12.30  ? 3703 VAL A CG1   1 
ATOM   15928 C  CG2   . VAL A 1 3703 ? 86.195  91.476  59.624  1.00 15.74  ? 3703 VAL A CG2   1 
ATOM   15929 N  N     . THR A 1 3704 ? 88.684  94.221  56.778  1.00 12.82  ? 3704 THR A N     1 
ATOM   15930 C  CA    . THR A 1 3704 ? 88.939  95.447  56.039  1.00 13.17  ? 3704 THR A CA    1 
ATOM   15931 C  C     . THR A 1 3704 ? 87.665  95.903  55.339  1.00 12.66  ? 3704 THR A C     1 
ATOM   15932 O  O     . THR A 1 3704 ? 86.766  95.109  55.053  1.00 11.45  ? 3704 THR A O     1 
ATOM   15933 C  CB    . THR A 1 3704 ? 90.063  95.251  55.017  1.00 15.72  ? 3704 THR A CB    1 
ATOM   15934 O  OG1   . THR A 1 3704 ? 89.576  94.490  53.906  1.00 15.36  ? 3704 THR A OG1   1 
ATOM   15935 C  CG2   . THR A 1 3704 ? 91.236  94.522  55.651  1.00 13.18  ? 3704 THR A CG2   1 
ATOM   15936 N  N     . ARG A 1 3705 ? 87.595  97.210  55.074  1.00 12.02  ? 3705 ARG A N     1 
ATOM   15937 C  CA    . ARG A 1 3705 ? 86.396  97.773  54.462  1.00 12.69  ? 3705 ARG A CA    1 
ATOM   15938 C  C     . ARG A 1 3705 ? 86.162  97.200  53.070  1.00 12.25  ? 3705 ARG A C     1 
ATOM   15939 O  O     . ARG A 1 3705 ? 85.025  96.872  52.709  1.00 12.87  ? 3705 ARG A O     1 
ATOM   15940 C  CB    . ARG A 1 3705 ? 86.501  99.297  54.409  1.00 14.84  ? 3705 ARG A CB    1 
ATOM   15941 C  CG    . ARG A 1 3705 ? 86.312  99.968  55.758  1.00 20.52  ? 3705 ARG A CG    1 
ATOM   15942 C  CD    . ARG A 1 3705 ? 86.581  101.462 55.696  1.00 25.48  ? 3705 ARG A CD    1 
ATOM   15943 N  NE    . ARG A 1 3705 ? 86.213  102.133 56.938  1.00 24.39  ? 3705 ARG A NE    1 
ATOM   15944 C  CZ    . ARG A 1 3705 ? 84.967  102.367 57.329  1.00 25.00  ? 3705 ARG A CZ    1 
ATOM   15945 N  NH1   . ARG A 1 3705 ? 83.930  102.000 56.594  1.00 15.67  ? 3705 ARG A NH1   1 
ATOM   15946 N  NH2   . ARG A 1 3705 ? 84.756  102.987 58.487  1.00 21.95  ? 3705 ARG A NH2   1 
ATOM   15947 N  N     . SER A 1 3706 ? 87.227  97.068  52.275  1.00 10.99  ? 3706 SER A N     1 
ATOM   15948 C  CA    . SER A 1 3706 ? 87.080  96.549  50.918  1.00 12.28  ? 3706 SER A CA    1 
ATOM   15949 C  C     . SER A 1 3706 ? 86.619  95.097  50.919  1.00 12.82  ? 3706 SER A C     1 
ATOM   15950 O  O     . SER A 1 3706 ? 85.756  94.712  50.120  1.00 12.18  ? 3706 SER A O     1 
ATOM   15951 C  CB    . SER A 1 3706 ? 88.398  96.690  50.157  1.00 18.20  ? 3706 SER A CB    1 
ATOM   15952 O  OG    . SER A 1 3706 ? 89.413  95.896  50.744  1.00 21.88  ? 3706 SER A OG    1 
ATOM   15953 N  N     . SER A 1 3707 ? 87.190  94.270  51.799  1.00 11.78  ? 3707 SER A N     1 
ATOM   15954 C  CA    . SER A 1 3707 ? 86.808  92.861  51.838  1.00 13.79  ? 3707 SER A CA    1 
ATOM   15955 C  C     . SER A 1 3707 ? 85.351  92.694  52.249  1.00 11.42  ? 3707 SER A C     1 
ATOM   15956 O  O     . SER A 1 3707 ? 84.620  91.895  51.652  1.00 12.21  ? 3707 SER A O     1 
ATOM   15957 C  CB    . SER A 1 3707 ? 87.726  92.092  52.787  1.00 14.88  ? 3707 SER A CB    1 
ATOM   15958 O  OG    . SER A 1 3707 ? 87.636  92.595  54.108  1.00 20.55  ? 3707 SER A OG    1 
ATOM   15959 N  N     . LEU A 1 3708 ? 84.910  93.442  53.262  1.00 10.44  ? 3708 LEU A N     1 
ATOM   15960 C  CA    . LEU A 1 3708 ? 83.512  93.375  53.672  1.00 8.94   ? 3708 LEU A CA    1 
ATOM   15961 C  C     . LEU A 1 3708 ? 82.587  93.899  52.581  1.00 8.51   ? 3708 LEU A C     1 
ATOM   15962 O  O     . LEU A 1 3708 ? 81.497  93.354  52.370  1.00 7.93   ? 3708 LEU A O     1 
ATOM   15963 C  CB    . LEU A 1 3708 ? 83.301  94.158  54.964  1.00 9.54   ? 3708 LEU A CB    1 
ATOM   15964 C  CG    . LEU A 1 3708 ? 81.897  93.996  55.544  1.00 8.39   ? 3708 LEU A CG    1 
ATOM   15965 C  CD1   . LEU A 1 3708 ? 81.519  92.526  55.661  1.00 9.21   ? 3708 LEU A CD1   1 
ATOM   15966 C  CD2   . LEU A 1 3708 ? 81.792  94.690  56.875  1.00 9.46   ? 3708 LEU A CD2   1 
ATOM   15967 N  N     . GLN A 1 3709 ? 82.994  94.969  51.894  1.00 8.91   ? 3709 GLN A N     1 
ATOM   15968 C  CA    . GLN A 1 3709 ? 82.191  95.482  50.791  1.00 9.54   ? 3709 GLN A CA    1 
ATOM   15969 C  C     . GLN A 1 3709 ? 82.039  94.436  49.697  1.00 9.82   ? 3709 GLN A C     1 
ATOM   15970 O  O     . GLN A 1 3709 ? 80.943  94.244  49.160  1.00 13.67  ? 3709 GLN A O     1 
ATOM   15971 C  CB    . GLN A 1 3709 ? 82.822  96.755  50.229  1.00 10.23  ? 3709 GLN A CB    1 
ATOM   15972 C  CG    . GLN A 1 3709 ? 82.446  98.020  50.975  1.00 11.13  ? 3709 GLN A CG    1 
ATOM   15973 C  CD    . GLN A 1 3709 ? 83.509  99.093  50.867  1.00 17.12  ? 3709 GLN A CD    1 
ATOM   15974 O  OE1   . GLN A 1 3709 ? 84.412  99.007  50.034  1.00 24.95  ? 3709 GLN A OE1   1 
ATOM   15975 N  NE2   . GLN A 1 3709 ? 83.408  100.113 51.710  1.00 19.29  ? 3709 GLN A NE2   1 
ATOM   15976 N  N     . SER A 1 3710 ? 83.129  93.743  49.361  1.00 10.41  ? 3710 SER A N     1 
ATOM   15977 C  CA    . SER A 1 3710 ? 83.056  92.679  48.366  1.00 10.80  ? 3710 SER A CA    1 
ATOM   15978 C  C     . SER A 1 3710 ? 82.154  91.545  48.837  1.00 11.87  ? 3710 SER A C     1 
ATOM   15979 O  O     . SER A 1 3710 ? 81.359  91.011  48.055  1.00 14.70  ? 3710 SER A O     1 
ATOM   15980 C  CB    . SER A 1 3710 ? 84.457  92.154  48.054  1.00 12.10  ? 3710 SER A CB    1 
ATOM   15981 O  OG    . SER A 1 3710 ? 85.254  93.157  47.451  1.00 23.51  ? 3710 SER A OG    1 
ATOM   15982 N  N     . GLN A 1 3711 ? 82.264  91.164  50.112  1.00 10.17  ? 3711 GLN A N     1 
ATOM   15983 C  CA    . GLN A 1 3711 ? 81.419  90.102  50.650  1.00 10.37  ? 3711 GLN A CA    1 
ATOM   15984 C  C     . GLN A 1 3711 ? 79.944  90.465  50.538  1.00 10.60  ? 3711 GLN A C     1 
ATOM   15985 O  O     . GLN A 1 3711 ? 79.125  89.663  50.074  1.00 15.35  ? 3711 GLN A O     1 
ATOM   15986 C  CB    . GLN A 1 3711 ? 81.788  89.826  52.108  1.00 11.93  ? 3711 GLN A CB    1 
ATOM   15987 C  CG    . GLN A 1 3711 ? 83.092  89.077  52.305  1.00 17.23  ? 3711 GLN A CG    1 
ATOM   15988 C  CD    . GLN A 1 3711 ? 83.469  88.952  53.769  1.00 25.43  ? 3711 GLN A CD    1 
ATOM   15989 O  OE1   . GLN A 1 3711 ? 84.581  89.297  54.167  1.00 26.33  ? 3711 GLN A OE1   1 
ATOM   15990 N  NE2   . GLN A 1 3711 ? 82.539  88.460  54.579  1.00 24.97  ? 3711 GLN A NE2   1 
ATOM   15991 N  N     . CYS A 1 3712 ? 79.589  91.683  50.953  1.00 10.02  ? 3712 CYS A N     1 
ATOM   15992 C  CA    . CYS A 1 3712 ? 78.188  92.092  50.934  1.00 10.96  ? 3712 CYS A CA    1 
ATOM   15993 C  C     . CYS A 1 3712 ? 77.679  92.265  49.509  1.00 13.06  ? 3712 CYS A C     1 
ATOM   15994 O  O     . CYS A 1 3712 ? 76.525  91.932  49.213  1.00 15.39  ? 3712 CYS A O     1 
ATOM   15995 C  CB    . CYS A 1 3712 ? 78.008  93.377  51.738  1.00 9.13   ? 3712 CYS A CB    1 
ATOM   15996 S  SG    . CYS A 1 3712 ? 78.473  93.218  53.479  1.00 14.68  ? 3712 CYS A SG    1 
ATOM   15997 N  N     . LEU A 1 3713 ? 78.523  92.781  48.610  1.00 11.51  ? 3713 LEU A N     1 
ATOM   15998 C  CA    . LEU A 1 3713 ? 78.134  92.897  47.210  1.00 11.80  ? 3713 LEU A CA    1 
ATOM   15999 C  C     . LEU A 1 3713 ? 77.875  91.528  46.599  1.00 11.92  ? 3713 LEU A C     1 
ATOM   16000 O  O     . LEU A 1 3713 ? 76.880  91.334  45.891  1.00 12.93  ? 3713 LEU A O     1 
ATOM   16001 C  CB    . LEU A 1 3713 ? 79.217  93.637  46.426  1.00 12.76  ? 3713 LEU A CB    1 
ATOM   16002 C  CG    . LEU A 1 3713 ? 79.022  93.713  44.911  1.00 12.09  ? 3713 LEU A CG    1 
ATOM   16003 C  CD1   . LEU A 1 3713 ? 77.854  94.620  44.565  1.00 13.71  ? 3713 LEU A CD1   1 
ATOM   16004 C  CD2   . LEU A 1 3713 ? 80.296  94.178  44.225  1.00 18.65  ? 3713 LEU A CD2   1 
ATOM   16005 N  N     . ASN A 1 3714 ? 78.752  90.560  46.872  1.00 12.88  ? 3714 ASN A N     1 
ATOM   16006 C  CA    . ASN A 1 3714 ? 78.543  89.209  46.367  1.00 17.13  ? 3714 ASN A CA    1 
ATOM   16007 C  C     . ASN A 1 3714 ? 77.278  88.595  46.951  1.00 15.74  ? 3714 ASN A C     1 
ATOM   16008 O  O     . ASN A 1 3714 ? 76.527  87.913  46.244  1.00 16.11  ? 3714 ASN A O     1 
ATOM   16009 C  CB    . ASN A 1 3714 ? 79.759  88.339  46.683  1.00 17.30  ? 3714 ASN A CB    1 
ATOM   16010 C  CG    . ASN A 1 3714 ? 80.964  88.692  45.834  1.00 22.50  ? 3714 ASN A CG    1 
ATOM   16011 O  OD1   . ASN A 1 3714 ? 80.867  89.486  44.898  1.00 26.94  ? 3714 ASN A OD1   1 
ATOM   16012 N  ND2   . ASN A 1 3714 ? 82.109  88.106  46.159  1.00 23.85  ? 3714 ASN A ND2   1 
ATOM   16013 N  N     . GLU A 1 3715 ? 77.023  88.827  48.241  1.00 16.10  ? 3715 GLU A N     1 
ATOM   16014 C  CA    . GLU A 1 3715 ? 75.842  88.247  48.872  1.00 19.06  ? 3715 GLU A CA    1 
ATOM   16015 C  C     . GLU A 1 3715 ? 74.556  88.832  48.295  1.00 16.91  ? 3715 GLU A C     1 
ATOM   16016 O  O     . GLU A 1 3715 ? 73.604  88.094  48.014  1.00 19.26  ? 3715 GLU A O     1 
ATOM   16017 C  CB    . GLU A 1 3715 ? 75.903  88.459  50.384  1.00 17.98  ? 3715 GLU A CB    1 
ATOM   16018 C  CG    . GLU A 1 3715 ? 74.750  87.831  51.144  1.00 26.80  ? 3715 GLU A CG    1 
ATOM   16019 C  CD    . GLU A 1 3715 ? 74.755  86.316  51.058  1.00 39.20  ? 3715 GLU A CD    1 
ATOM   16020 O  OE1   . GLU A 1 3715 ? 75.842  85.730  50.871  1.00 44.68  ? 3715 GLU A OE1   1 
ATOM   16021 O  OE2   . GLU A 1 3715 ? 73.671  85.709  51.176  1.00 40.74  ? 3715 GLU A OE2   1 
ATOM   16022 N  N     . VAL A 1 3716 ? 74.508  90.154  48.105  1.00 12.30  ? 3716 VAL A N     1 
ATOM   16023 C  CA    . VAL A 1 3716 ? 73.309  90.756  47.528  1.00 14.04  ? 3716 VAL A CA    1 
ATOM   16024 C  C     . VAL A 1 3716 ? 73.168  90.373  46.061  1.00 18.48  ? 3716 VAL A C     1 
ATOM   16025 O  O     . VAL A 1 3716 ? 72.049  90.254  45.553  1.00 18.93  ? 3716 VAL A O     1 
ATOM   16026 C  CB    . VAL A 1 3716 ? 73.301  92.286  47.718  1.00 12.14  ? 3716 VAL A CB    1 
ATOM   16027 C  CG1   . VAL A 1 3716 ? 74.446  92.943  46.974  1.00 12.42  ? 3716 VAL A CG1   1 
ATOM   16028 C  CG2   . VAL A 1 3716 ? 71.967  92.871  47.275  1.00 13.60  ? 3716 VAL A CG2   1 
ATOM   16029 N  N     . LEU A 1 3717 ? 74.283  90.173  45.352  1.00 16.06  ? 3717 LEU A N     1 
ATOM   16030 C  CA    . LEU A 1 3717 ? 74.195  89.689  43.980  1.00 17.33  ? 3717 LEU A CA    1 
ATOM   16031 C  C     . LEU A 1 3717 ? 73.615  88.282  43.938  1.00 21.17  ? 3717 LEU A C     1 
ATOM   16032 O  O     . LEU A 1 3717 ? 72.791  87.966  43.073  1.00 20.20  ? 3717 LEU A O     1 
ATOM   16033 C  CB    . LEU A 1 3717 ? 75.574  89.730  43.324  1.00 19.56  ? 3717 LEU A CB    1 
ATOM   16034 C  CG    . LEU A 1 3717 ? 75.642  89.314  41.856  1.00 29.22  ? 3717 LEU A CG    1 
ATOM   16035 C  CD1   . LEU A 1 3717 ? 74.815  90.266  41.007  1.00 27.99  ? 3717 LEU A CD1   1 
ATOM   16036 C  CD2   . LEU A 1 3717 ? 77.083  89.279  41.377  1.00 31.81  ? 3717 LEU A CD2   1 
ATOM   16037 N  N     . LYS A 1 3718 ? 74.033  87.424  44.870  1.00 20.22  ? 3718 LYS A N     1 
ATOM   16038 C  CA    . LYS A 1 3718 ? 73.484  86.075  44.946  1.00 20.99  ? 3718 LYS A CA    1 
ATOM   16039 C  C     . LYS A 1 3718 ? 71.996  86.099  45.274  1.00 25.10  ? 3718 LYS A C     1 
ATOM   16040 O  O     . LYS A 1 3718 ? 71.210  85.346  44.688  1.00 25.22  ? 3718 LYS A O     1 
ATOM   16041 C  CB    . LYS A 1 3718 ? 74.248  85.261  45.989  1.00 23.71  ? 3718 LYS A CB    1 
ATOM   16042 C  CG    . LYS A 1 3718 ? 73.847  83.799  46.063  1.00 32.40  ? 3718 LYS A CG    1 
ATOM   16043 C  CD    . LYS A 1 3718 ? 74.605  83.082  47.168  1.00 38.83  ? 3718 LYS A CD    1 
ATOM   16044 C  CE    . LYS A 1 3718 ? 76.055  82.848  46.781  1.00 44.18  ? 3718 LYS A CE    1 
ATOM   16045 N  NZ    . LYS A 1 3718 ? 76.779  82.044  47.804  1.00 50.83  ? 3718 LYS A NZ    1 
ATOM   16046 N  N     . ALA A 1 3719 ? 71.592  86.958  46.212  1.00 21.95  ? 3719 ALA A N     1 
ATOM   16047 C  CA    . ALA A 1 3719 ? 70.195  86.984  46.636  1.00 19.00  ? 3719 ALA A CA    1 
ATOM   16048 C  C     . ALA A 1 3719 ? 69.290  87.599  45.573  1.00 22.78  ? 3719 ALA A C     1 
ATOM   16049 O  O     . ALA A 1 3719 ? 68.212  87.067  45.284  1.00 29.68  ? 3719 ALA A O     1 
ATOM   16050 C  CB    . ALA A 1 3719 ? 70.062  87.742  47.956  1.00 20.64  ? 3719 ALA A CB    1 
ATOM   16051 N  N     . GLU A 1 3720 ? 69.708  88.717  44.981  1.00 23.47  ? 3720 GLU A N     1 
ATOM   16052 C  CA    . GLU A 1 3720 ? 68.868  89.490  44.074  1.00 21.13  ? 3720 GLU A CA    1 
ATOM   16053 C  C     . GLU A 1 3720 ? 68.992  89.039  42.624  1.00 27.85  ? 3720 GLU A C     1 
ATOM   16054 O  O     . GLU A 1 3720 ? 67.990  88.995  41.903  1.00 34.69  ? 3720 GLU A O     1 
ATOM   16055 C  CB    . GLU A 1 3720 ? 69.220  90.976  44.179  1.00 20.69  ? 3720 GLU A CB    1 
ATOM   16056 C  CG    . GLU A 1 3720 ? 68.754  91.639  45.464  1.00 23.53  ? 3720 GLU A CG    1 
ATOM   16057 C  CD    . GLU A 1 3720 ? 67.246  91.684  45.583  1.00 33.36  ? 3720 GLU A CD    1 
ATOM   16058 O  OE1   . GLU A 1 3720 ? 66.617  92.491  44.867  1.00 31.91  ? 3720 GLU A OE1   1 
ATOM   16059 O  OE2   . GLU A 1 3720 ? 66.689  90.910  46.390  1.00 27.84  ? 3720 GLU A OE2   1 
ATOM   16060 N  N     . ARG A 1 3721 ? 70.202  88.703  42.179  1.00 29.31  ? 3721 ARG A N     1 
ATOM   16061 C  CA    . ARG A 1 3721 ? 70.470  88.332  40.790  1.00 25.04  ? 3721 ARG A CA    1 
ATOM   16062 C  C     . ARG A 1 3721 ? 71.216  87.005  40.772  1.00 27.02  ? 3721 ARG A C     1 
ATOM   16063 O  O     . ARG A 1 3721 ? 72.409  86.953  40.448  1.00 32.53  ? 3721 ARG A O     1 
ATOM   16064 C  CB    . ARG A 1 3721 ? 71.277  89.421  40.081  1.00 24.25  ? 3721 ARG A CB    1 
ATOM   16065 C  CG    . ARG A 1 3721 ? 70.695  90.823  40.203  1.00 23.31  ? 3721 ARG A CG    1 
ATOM   16066 C  CD    . ARG A 1 3721 ? 69.321  90.921  39.562  1.00 27.25  ? 3721 ARG A CD    1 
ATOM   16067 N  NE    . ARG A 1 3721 ? 69.379  90.748  38.116  1.00 36.77  ? 3721 ARG A NE    1 
ATOM   16068 C  CZ    . ARG A 1 3721 ? 69.770  91.686  37.263  1.00 41.20  ? 3721 ARG A CZ    1 
ATOM   16069 N  NH1   . ARG A 1 3721 ? 70.136  92.888  37.677  1.00 36.87  ? 3721 ARG A NH1   1 
ATOM   16070 N  NH2   . ARG A 1 3721 ? 69.790  91.413  35.962  1.00 41.80  ? 3721 ARG A NH2   1 
ATOM   16071 N  N     . PRO A 1 3722 ? 70.541  85.906  41.130  1.00 27.22  ? 3722 PRO A N     1 
ATOM   16072 C  CA    . PRO A 1 3722 ? 71.253  84.619  41.234  1.00 29.28  ? 3722 PRO A CA    1 
ATOM   16073 C  C     . PRO A 1 3722 ? 71.916  84.182  39.940  1.00 28.46  ? 3722 PRO A C     1 
ATOM   16074 O  O     . PRO A 1 3722 ? 73.013  83.610  39.975  1.00 34.61  ? 3722 PRO A O     1 
ATOM   16075 C  CB    . PRO A 1 3722 ? 70.145  83.646  41.666  1.00 28.19  ? 3722 PRO A CB    1 
ATOM   16076 C  CG    . PRO A 1 3722 ? 68.875  84.295  41.226  1.00 26.53  ? 3722 PRO A CG    1 
ATOM   16077 C  CD    . PRO A 1 3722 ? 69.099  85.764  41.391  1.00 24.65  ? 3722 PRO A CD    1 
ATOM   16078 N  N     . ASP A 1 3723 ? 71.281  84.440  38.795  1.00 28.05  ? 3723 ASP A N     1 
ATOM   16079 C  CA    . ASP A 1 3723 ? 71.898  84.097  37.518  1.00 31.08  ? 3723 ASP A CA    1 
ATOM   16080 C  C     . ASP A 1 3723 ? 73.180  84.891  37.294  1.00 33.76  ? 3723 ASP A C     1 
ATOM   16081 O  O     . ASP A 1 3723 ? 74.191  84.338  36.845  1.00 39.08  ? 3723 ASP A O     1 
ATOM   16082 C  CB    . ASP A 1 3723 ? 70.904  84.326  36.377  1.00 32.08  ? 3723 ASP A CB    1 
ATOM   16083 C  CG    . ASP A 1 3723 ? 70.549  85.790  36.192  1.00 40.63  ? 3723 ASP A CG    1 
ATOM   16084 O  OD1   . ASP A 1 3723 ? 70.150  86.436  37.184  1.00 35.09  ? 3723 ASP A OD1   1 
ATOM   16085 O  OD2   . ASP A 1 3723 ? 70.667  86.293  35.055  1.00 48.59  ? 3723 ASP A OD2   1 
ATOM   16086 N  N     . VAL A 1 3724 ? 73.162  86.185  37.620  1.00 28.39  ? 3724 VAL A N     1 
ATOM   16087 C  CA    . VAL A 1 3724 ? 74.350  87.013  37.447  1.00 29.87  ? 3724 VAL A CA    1 
ATOM   16088 C  C     . VAL A 1 3724 ? 75.465  86.548  38.376  1.00 37.88  ? 3724 VAL A C     1 
ATOM   16089 O  O     . VAL A 1 3724 ? 76.633  86.485  37.979  1.00 38.19  ? 3724 VAL A O     1 
ATOM   16090 C  CB    . VAL A 1 3724 ? 74.006  88.497  37.670  1.00 29.78  ? 3724 VAL A CB    1 
ATOM   16091 C  CG1   . VAL A 1 3724 ? 75.249  89.359  37.519  1.00 29.56  ? 3724 VAL A CG1   1 
ATOM   16092 C  CG2   . VAL A 1 3724 ? 72.918  88.941  36.705  1.00 29.89  ? 3724 VAL A CG2   1 
ATOM   16093 N  N     . ASP A 1 3725 ? 75.125  86.216  39.624  1.00 33.47  ? 3725 ASP A N     1 
ATOM   16094 C  CA    . ASP A 1 3725 ? 76.135  85.743  40.567  1.00 31.33  ? 3725 ASP A CA    1 
ATOM   16095 C  C     . ASP A 1 3725 ? 76.738  84.417  40.119  1.00 37.65  ? 3725 ASP A C     1 
ATOM   16096 O  O     . ASP A 1 3725 ? 77.955  84.216  40.214  1.00 43.04  ? 3725 ASP A O     1 
ATOM   16097 C  CB    . ASP A 1 3725 ? 75.527  85.611  41.962  1.00 29.17  ? 3725 ASP A CB    1 
ATOM   16098 C  CG    . ASP A 1 3725 ? 76.578  85.536  43.051  1.00 37.40  ? 3725 ASP A CG    1 
ATOM   16099 O  OD1   . ASP A 1 3725 ? 77.308  86.530  43.247  1.00 35.45  ? 3725 ASP A OD1   1 
ATOM   16100 O  OD2   . ASP A 1 3725 ? 76.676  84.480  43.711  1.00 42.30  ? 3725 ASP A OD2   1 
ATOM   16101 N  N     . GLU A 1 3726 ? 75.900  83.493  39.639  1.00 41.63  ? 3726 GLU A N     1 
ATOM   16102 C  CA    . GLU A 1 3726 ? 76.413  82.218  39.147  1.00 42.89  ? 3726 GLU A CA    1 
ATOM   16103 C  C     . GLU A 1 3726 ? 77.317  82.419  37.938  1.00 41.27  ? 3726 GLU A C     1 
ATOM   16104 O  O     . GLU A 1 3726 ? 78.388  81.803  37.841  1.00 44.03  ? 3726 GLU A O     1 
ATOM   16105 C  CB    . GLU A 1 3726 ? 75.253  81.285  38.801  1.00 42.90  ? 3726 GLU A CB    1 
ATOM   16106 C  CG    . GLU A 1 3726 ? 75.689  79.898  38.363  1.00 55.06  ? 3726 GLU A CG    1 
ATOM   16107 C  CD    . GLU A 1 3726 ? 74.517  78.974  38.098  1.00 68.19  ? 3726 GLU A CD    1 
ATOM   16108 O  OE1   . GLU A 1 3726 ? 73.360  79.422  38.238  1.00 73.25  ? 3726 GLU A OE1   1 
ATOM   16109 O  OE2   . GLU A 1 3726 ? 74.755  77.799  37.746  1.00 71.40  ? 3726 GLU A OE2   1 
ATOM   16110 N  N     . LYS A 1 3727 ? 76.902  83.282  37.006  1.00 35.93  ? 3727 LYS A N     1 
ATOM   16111 C  CA    . LYS A 1 3727 ? 77.731  83.577  35.844  1.00 37.40  ? 3727 LYS A CA    1 
ATOM   16112 C  C     . LYS A 1 3727 ? 79.060  84.187  36.266  1.00 38.51  ? 3727 LYS A C     1 
ATOM   16113 O  O     . LYS A 1 3727 ? 80.111  83.846  35.715  1.00 41.81  ? 3727 LYS A O     1 
ATOM   16114 C  CB    . LYS A 1 3727 ? 76.982  84.514  34.896  1.00 37.92  ? 3727 LYS A CB    1 
ATOM   16115 C  CG    . LYS A 1 3727 ? 77.864  85.248  33.901  1.00 44.46  ? 3727 LYS A CG    1 
ATOM   16116 C  CD    . LYS A 1 3727 ? 77.062  86.277  33.120  1.00 49.92  ? 3727 LYS A CD    1 
ATOM   16117 C  CE    . LYS A 1 3727 ? 76.062  85.616  32.187  1.00 54.43  ? 3727 LYS A CE    1 
ATOM   16118 N  NZ    . LYS A 1 3727 ? 76.731  84.780  31.153  1.00 60.46  ? 3727 LYS A NZ    1 
ATOM   16119 N  N     . ARG A 1 3728 ? 79.031  85.083  37.254  1.00 36.64  ? 3728 ARG A N     1 
ATOM   16120 C  CA    . ARG A 1 3728 ? 80.257  85.693  37.755  1.00 37.40  ? 3728 ARG A CA    1 
ATOM   16121 C  C     . ARG A 1 3728 ? 81.187  84.648  38.360  1.00 36.37  ? 3728 ARG A C     1 
ATOM   16122 O  O     . ARG A 1 3728 ? 82.396  84.653  38.103  1.00 36.88  ? 3728 ARG A O     1 
ATOM   16123 C  CB    . ARG A 1 3728 ? 79.905  86.773  38.780  1.00 36.87  ? 3728 ARG A CB    1 
ATOM   16124 C  CG    . ARG A 1 3728 ? 81.082  87.572  39.306  1.00 38.54  ? 3728 ARG A CG    1 
ATOM   16125 C  CD    . ARG A 1 3728 ? 80.982  87.772  40.813  1.00 36.56  ? 3728 ARG A CD    1 
ATOM   16126 N  NE    . ARG A 1 3728 ? 81.464  86.615  41.559  1.00 46.73  ? 3728 ARG A NE    1 
ATOM   16127 C  CZ    . ARG A 1 3728 ? 80.883  86.129  42.647  1.00 43.00  ? 3728 ARG A CZ    1 
ATOM   16128 N  NH1   . ARG A 1 3728 ? 79.788  86.676  43.149  1.00 41.05  ? 3728 ARG A NH1   1 
ATOM   16129 N  NH2   . ARG A 1 3728 ? 81.413  85.066  43.246  1.00 41.52  ? 3728 ARG A NH2   1 
ATOM   16130 N  N     . SER A 1 3729 ? 80.640  83.743  39.174  1.00 37.61  ? 3729 SER A N     1 
ATOM   16131 C  CA    . SER A 1 3729 ? 81.473  82.707  39.776  1.00 38.79  ? 3729 SER A CA    1 
ATOM   16132 C  C     . SER A 1 3729 ? 82.114  81.828  38.706  1.00 40.72  ? 3729 SER A C     1 
ATOM   16133 O  O     . SER A 1 3729 ? 83.324  81.551  38.755  1.00 42.19  ? 3729 SER A O     1 
ATOM   16134 C  CB    . SER A 1 3729 ? 80.642  81.863  40.742  1.00 45.15  ? 3729 SER A CB    1 
ATOM   16135 O  OG    . SER A 1 3729 ? 80.176  82.646  41.827  1.00 43.64  ? 3729 SER A OG    1 
ATOM   16136 N  N     . ASP A 1 3730 ? 81.321  81.406  37.714  1.00 40.09  ? 3730 ASP A N     1 
ATOM   16137 C  CA    . ASP A 1 3730 ? 81.875  80.613  36.621  1.00 42.24  ? 3730 ASP A CA    1 
ATOM   16138 C  C     . ASP A 1 3730 ? 82.944  81.392  35.864  1.00 39.26  ? 3730 ASP A C     1 
ATOM   16139 O  O     . ASP A 1 3730 ? 83.956  80.822  35.443  1.00 39.83  ? 3730 ASP A O     1 
ATOM   16140 C  CB    . ASP A 1 3730 ? 80.766  80.152  35.671  1.00 42.90  ? 3730 ASP A CB    1 
ATOM   16141 C  CG    . ASP A 1 3730 ? 79.613  79.470  36.393  1.00 50.10  ? 3730 ASP A CG    1 
ATOM   16142 O  OD1   . ASP A 1 3730 ? 79.873  78.667  37.315  1.00 54.80  ? 3730 ASP A OD1   1 
ATOM   16143 O  OD2   . ASP A 1 3730 ? 78.445  79.726  36.030  1.00 51.50  ? 3730 ASP A OD2   1 
ATOM   16144 N  N     . LEU A 1 3731 ? 82.749  82.700  35.695  1.00 35.68  ? 3731 LEU A N     1 
ATOM   16145 C  CA    . LEU A 1 3731 ? 83.716  83.490  34.943  1.00 33.35  ? 3731 LEU A CA    1 
ATOM   16146 C  C     . LEU A 1 3731 ? 85.040  83.618  35.685  1.00 36.76  ? 3731 LEU A C     1 
ATOM   16147 O  O     . LEU A 1 3731 ? 86.108  83.486  35.078  1.00 40.75  ? 3731 LEU A O     1 
ATOM   16148 C  CB    . LEU A 1 3731 ? 83.137  84.866  34.646  1.00 38.10  ? 3731 LEU A CB    1 
ATOM   16149 C  CG    . LEU A 1 3731 ? 82.094  84.974  33.539  1.00 39.10  ? 3731 LEU A CG    1 
ATOM   16150 C  CD1   . LEU A 1 3731 ? 81.694  86.419  33.433  1.00 39.89  ? 3731 LEU A CD1   1 
ATOM   16151 C  CD2   . LEU A 1 3731 ? 82.590  84.437  32.200  1.00 40.69  ? 3731 LEU A CD2   1 
ATOM   16152 N  N     . LEU A 1 3732 ? 84.996  83.905  36.990  1.00 32.97  ? 3732 LEU A N     1 
ATOM   16153 C  CA    . LEU A 1 3732 ? 86.239  83.965  37.760  1.00 34.45  ? 3732 LEU A CA    1 
ATOM   16154 C  C     . LEU A 1 3732 ? 86.956  82.624  37.767  1.00 35.45  ? 3732 LEU A C     1 
ATOM   16155 O  O     . LEU A 1 3732 ? 88.188  82.577  37.662  1.00 37.02  ? 3732 LEU A O     1 
ATOM   16156 C  CB    . LEU A 1 3732 ? 86.000  84.454  39.192  1.00 36.28  ? 3732 LEU A CB    1 
ATOM   16157 C  CG    . LEU A 1 3732 ? 85.798  85.943  39.505  1.00 37.62  ? 3732 LEU A CG    1 
ATOM   16158 C  CD1   . LEU A 1 3732 ? 84.488  86.493  39.036  1.00 38.78  ? 3732 LEU A CD1   1 
ATOM   16159 C  CD2   . LEU A 1 3732 ? 85.926  86.157  41.007  1.00 42.87  ? 3732 LEU A CD2   1 
ATOM   16160 N  N     . LYS A 1 3733 ? 86.214  81.519  37.879  1.00 33.47  ? 3733 LYS A N     1 
ATOM   16161 C  CA    . LYS A 1 3733 ? 86.871  80.217  37.800  1.00 34.77  ? 3733 LYS A CA    1 
ATOM   16162 C  C     . LYS A 1 3733 ? 87.527  80.019  36.434  1.00 35.09  ? 3733 LYS A C     1 
ATOM   16163 O  O     . LYS A 1 3733 ? 88.675  79.551  36.336  1.00 33.84  ? 3733 LYS A O     1 
ATOM   16164 C  CB    . LYS A 1 3733 ? 85.868  79.102  38.094  1.00 36.11  ? 3733 LYS A CB    1 
ATOM   16165 C  CG    . LYS A 1 3733 ? 86.478  77.711  38.075  1.00 43.27  ? 3733 LYS A CG    1 
ATOM   16166 C  CD    . LYS A 1 3733 ? 85.478  76.656  38.513  1.00 48.17  ? 3733 LYS A CD    1 
ATOM   16167 C  CE    . LYS A 1 3733 ? 84.416  76.437  37.452  1.00 56.29  ? 3733 LYS A CE    1 
ATOM   16168 N  NZ    . LYS A 1 3733 ? 84.993  75.801  36.236  1.00 60.67  ? 3733 LYS A NZ    1 
ATOM   16169 N  N     . LEU A 1 3734 ? 86.817  80.398  35.365  1.00 32.61  ? 3734 LEU A N     1 
ATOM   16170 C  CA    . LEU A 1 3734 ? 87.355  80.251  34.017  1.00 35.72  ? 3734 LEU A CA    1 
ATOM   16171 C  C     . LEU A 1 3734 ? 88.621  81.075  33.829  1.00 33.45  ? 3734 LEU A C     1 
ATOM   16172 O  O     . LEU A 1 3734 ? 89.606  80.584  33.273  1.00 35.35  ? 3734 LEU A O     1 
ATOM   16173 C  CB    . LEU A 1 3734 ? 86.303  80.650  32.980  1.00 37.31  ? 3734 LEU A CB    1 
ATOM   16174 C  CG    . LEU A 1 3734 ? 85.217  79.625  32.640  1.00 40.20  ? 3734 LEU A CG    1 
ATOM   16175 C  CD1   . LEU A 1 3734 ? 84.460  80.037  31.388  1.00 38.02  ? 3734 LEU A CD1   1 
ATOM   16176 C  CD2   . LEU A 1 3734 ? 85.812  78.241  32.473  1.00 41.21  ? 3734 LEU A CD2   1 
ATOM   16177 N  N     . GLN A 1 3735 ? 88.620  82.327  34.289  1.00 30.82  ? 3735 GLN A N     1 
ATOM   16178 C  CA    . GLN A 1 3735 ? 89.799  83.171  34.104  1.00 33.01  ? 3735 GLN A CA    1 
ATOM   16179 C  C     . GLN A 1 3735 ? 90.958  82.720  34.984  1.00 32.54  ? 3735 GLN A C     1 
ATOM   16180 O  O     . GLN A 1 3735 ? 92.121  82.843  34.586  1.00 35.28  ? 3735 GLN A O     1 
ATOM   16181 C  CB    . GLN A 1 3735 ? 89.468  84.641  34.359  1.00 37.22  ? 3735 GLN A CB    1 
ATOM   16182 C  CG    . GLN A 1 3735 ? 88.538  85.255  33.328  1.00 46.17  ? 3735 GLN A CG    1 
ATOM   16183 C  CD    . GLN A 1 3735 ? 88.230  86.708  33.617  1.00 46.21  ? 3735 GLN A CD    1 
ATOM   16184 O  OE1   . GLN A 1 3735 ? 88.649  87.252  34.638  1.00 47.29  ? 3735 GLN A OE1   1 
ATOM   16185 N  NE2   . GLN A 1 3735 ? 87.519  87.354  32.702  1.00 47.02  ? 3735 GLN A NE2   1 
ATOM   16186 N  N     . GLY A 1 3736 ? 90.672  82.207  36.182  1.00 30.91  ? 3736 GLY A N     1 
ATOM   16187 C  CA    . GLY A 1 3736 ? 91.743  81.657  36.997  1.00 27.88  ? 3736 GLY A CA    1 
ATOM   16188 C  C     . GLY A 1 3736 ? 92.440  80.498  36.314  1.00 32.36  ? 3736 GLY A C     1 
ATOM   16189 O  O     . GLY A 1 3736 ? 93.672  80.472  36.201  1.00 33.68  ? 3736 GLY A O     1 
ATOM   16190 N  N     . GLU A 1 3737 ? 91.660  79.538  35.805  1.00 32.70  ? 3737 GLU A N     1 
ATOM   16191 C  CA    . GLU A 1 3737 ? 92.296  78.427  35.102  1.00 32.61  ? 3737 GLU A CA    1 
ATOM   16192 C  C     . GLU A 1 3737 ? 92.901  78.877  33.775  1.00 30.35  ? 3737 GLU A C     1 
ATOM   16193 O  O     . GLU A 1 3737 ? 93.875  78.279  33.308  1.00 32.81  ? 3737 GLU A O     1 
ATOM   16194 C  CB    . GLU A 1 3737 ? 91.309  77.279  34.890  1.00 34.11  ? 3737 GLU A CB    1 
ATOM   16195 C  CG    . GLU A 1 3737 ? 90.034  77.646  34.173  1.00 37.11  ? 3737 GLU A CG    1 
ATOM   16196 C  CD    . GLU A 1 3737 ? 88.958  76.597  34.351  1.00 48.10  ? 3737 GLU A CD    1 
ATOM   16197 O  OE1   . GLU A 1 3737 ? 88.891  75.991  35.441  1.00 45.52  ? 3737 GLU A OE1   1 
ATOM   16198 O  OE2   . GLU A 1 3737 ? 88.185  76.370  33.398  1.00 51.53  ? 3737 GLU A OE2   1 
ATOM   16199 N  N     . PHE A 1 3738 ? 92.372  79.945  33.176  1.00 30.45  ? 3738 PHE A N     1 
ATOM   16200 C  CA    . PHE A 1 3738 ? 92.915  80.448  31.919  1.00 28.72  ? 3738 PHE A CA    1 
ATOM   16201 C  C     . PHE A 1 3738 ? 94.292  81.065  32.129  1.00 32.41  ? 3738 PHE A C     1 
ATOM   16202 O  O     . PHE A 1 3738 ? 95.223  80.817  31.354  1.00 34.67  ? 3738 PHE A O     1 
ATOM   16203 C  CB    . PHE A 1 3738 ? 91.952  81.473  31.322  1.00 30.69  ? 3738 PHE A CB    1 
ATOM   16204 C  CG    . PHE A 1 3738 ? 90.826  80.863  30.540  1.00 37.90  ? 3738 PHE A CG    1 
ATOM   16205 C  CD1   . PHE A 1 3738 ? 90.807  79.506  30.268  1.00 39.20  ? 3738 PHE A CD1   1 
ATOM   16206 C  CD2   . PHE A 1 3738 ? 89.764  81.643  30.114  1.00 39.64  ? 3738 PHE A CD2   1 
ATOM   16207 C  CE1   . PHE A 1 3738 ? 89.762  78.942  29.561  1.00 38.84  ? 3738 PHE A CE1   1 
ATOM   16208 C  CE2   . PHE A 1 3738 ? 88.716  81.084  29.412  1.00 39.71  ? 3738 PHE A CE2   1 
ATOM   16209 C  CZ    . PHE A 1 3738 ? 88.715  79.733  29.134  1.00 40.89  ? 3738 PHE A CZ    1 
ATOM   16210 N  N     . GLN A 1 3739 ? 94.433  81.885  33.173  1.00 33.14  ? 3739 GLN A N     1 
ATOM   16211 C  CA    . GLN A 1 3739 ? 95.738  82.440  33.512  1.00 29.95  ? 3739 GLN A CA    1 
ATOM   16212 C  C     . GLN A 1 3739 ? 96.703  81.340  33.930  1.00 26.88  ? 3739 GLN A C     1 
ATOM   16213 O  O     . GLN A 1 3739 ? 97.894  81.389  33.596  1.00 26.51  ? 3739 GLN A O     1 
ATOM   16214 C  CB    . GLN A 1 3739 ? 95.594  83.489  34.616  1.00 32.22  ? 3739 GLN A CB    1 
ATOM   16215 C  CG    . GLN A 1 3739 ? 94.777  84.707  34.211  1.00 31.47  ? 3739 GLN A CG    1 
ATOM   16216 C  CD    . GLN A 1 3739 ? 95.467  85.554  33.157  1.00 43.49  ? 3739 GLN A CD    1 
ATOM   16217 O  OE1   . GLN A 1 3739 ? 96.688  85.509  33.008  1.00 43.19  ? 3739 GLN A OE1   1 
ATOM   16218 N  NE2   . GLN A 1 3739 ? 94.684  86.331  32.418  1.00 41.93  ? 3739 GLN A NE2   1 
ATOM   16219 N  N     . LEU A 1 3740 ? 96.207  80.337  34.663  1.00 26.30  ? 3740 LEU A N     1 
ATOM   16220 C  CA    . LEU A 1 3740 ? 97.025  79.168  34.970  1.00 25.92  ? 3740 LEU A CA    1 
ATOM   16221 C  C     . LEU A 1 3740 ? 97.570  78.529  33.698  1.00 33.28  ? 3740 LEU A C     1 
ATOM   16222 O  O     . LEU A 1 3740 ? 98.775  78.274  33.578  1.00 36.22  ? 3740 LEU A O     1 
ATOM   16223 C  CB    . LEU A 1 3740 ? 96.200  78.158  35.769  1.00 27.83  ? 3740 LEU A CB    1 
ATOM   16224 C  CG    . LEU A 1 3740 ? 96.895  76.873  36.223  1.00 31.72  ? 3740 LEU A CG    1 
ATOM   16225 C  CD1   . LEU A 1 3740 ? 98.026  77.182  37.184  1.00 31.56  ? 3740 LEU A CD1   1 
ATOM   16226 C  CD2   . LEU A 1 3740 ? 95.893  75.924  36.859  1.00 32.60  ? 3740 LEU A CD2   1 
ATOM   16227 N  N     . ARG A 1 3741 ? 96.686  78.275  32.729  1.00 29.17  ? 3741 ARG A N     1 
ATOM   16228 C  CA    . ARG A 1 3741 ? 97.091  77.632  31.484  1.00 30.11  ? 3741 ARG A CA    1 
ATOM   16229 C  C     . ARG A 1 3741 ? 98.085  78.491  30.714  1.00 31.41  ? 3741 ARG A C     1 
ATOM   16230 O  O     . ARG A 1 3741 ? 99.046  77.972  30.140  1.00 36.18  ? 3741 ARG A O     1 
ATOM   16231 C  CB    . ARG A 1 3741 ? 95.861  77.337  30.627  1.00 34.25  ? 3741 ARG A CB    1 
ATOM   16232 C  CG    . ARG A 1 3741 ? 96.067  76.270  29.560  1.00 37.50  ? 3741 ARG A CG    1 
ATOM   16233 C  CD    . ARG A 1 3741 ? 96.538  74.956  30.163  1.00 43.58  ? 3741 ARG A CD    1 
ATOM   16234 N  NE    . ARG A 1 3741 ? 97.166  74.089  29.173  1.00 46.19  ? 3741 ARG A NE    1 
ATOM   16235 C  CZ    . ARG A 1 3741 ? 98.476  73.945  29.022  1.00 46.78  ? 3741 ARG A CZ    1 
ATOM   16236 N  NH1   . ARG A 1 3741 ? 99.336  74.607  29.776  1.00 45.37  ? 3741 ARG A NH1   1 
ATOM   16237 N  NH2   . ARG A 1 3741 ? 98.933  73.113  28.090  1.00 43.46  ? 3741 ARG A NH2   1 
ATOM   16238 N  N     . LEU A 1 3742 ? 97.864  79.808  30.679  1.00 28.73  ? 3742 LEU A N     1 
ATOM   16239 C  CA    . LEU A 1 3742 ? 98.795  80.693  29.985  1.00 26.71  ? 3742 LEU A CA    1 
ATOM   16240 C  C     . LEU A 1 3742 ? 100.175 80.663  30.633  1.00 31.33  ? 3742 LEU A C     1 
ATOM   16241 O  O     . LEU A 1 3742 ? 101.198 80.642  29.936  1.00 34.36  ? 3742 LEU A O     1 
ATOM   16242 C  CB    . LEU A 1 3742 ? 98.246  82.118  29.955  1.00 25.34  ? 3742 LEU A CB    1 
ATOM   16243 C  CG    . LEU A 1 3742 ? 97.153  82.410  28.926  1.00 34.17  ? 3742 LEU A CG    1 
ATOM   16244 C  CD1   . LEU A 1 3742 ? 97.000  83.908  28.722  1.00 35.53  ? 3742 LEU A CD1   1 
ATOM   16245 C  CD2   . LEU A 1 3742 ? 97.461  81.717  27.606  1.00 35.05  ? 3742 LEU A CD2   1 
ATOM   16246 N  N     . ARG A 1 3743 ? 100.223 80.663  31.968  1.00 30.51  ? 3743 ARG A N     1 
ATOM   16247 C  CA    . ARG A 1 3743 ? 101.506 80.580  32.657  1.00 30.24  ? 3743 ARG A CA    1 
ATOM   16248 C  C     . ARG A 1 3743 ? 102.211 79.264  32.350  1.00 33.93  ? 3743 ARG A C     1 
ATOM   16249 O  O     . ARG A 1 3743 ? 103.420 79.246  32.076  1.00 36.96  ? 3743 ARG A O     1 
ATOM   16250 C  CB    . ARG A 1 3743 ? 101.301 80.741  34.162  1.00 29.21  ? 3743 ARG A CB    1 
ATOM   16251 C  CG    . ARG A 1 3743 ? 101.241 82.184  34.627  1.00 28.79  ? 3743 ARG A CG    1 
ATOM   16252 C  CD    . ARG A 1 3743 ? 101.010 82.263  36.125  1.00 33.29  ? 3743 ARG A CD    1 
ATOM   16253 N  NE    . ARG A 1 3743 ? 99.597  82.436  36.443  1.00 28.36  ? 3743 ARG A NE    1 
ATOM   16254 C  CZ    . ARG A 1 3743 ? 98.846  81.519  37.038  1.00 27.62  ? 3743 ARG A CZ    1 
ATOM   16255 N  NH1   . ARG A 1 3743 ? 99.342  80.347  37.399  1.00 25.42  ? 3743 ARG A NH1   1 
ATOM   16256 N  NH2   . ARG A 1 3743 ? 97.566  81.786  37.279  1.00 28.12  ? 3743 ARG A NH2   1 
ATOM   16257 N  N     . GLN A 1 3744 ? 101.470 78.152  32.385  1.00 33.19  ? 3744 GLN A N     1 
ATOM   16258 C  CA    . GLN A 1 3744 ? 102.072 76.862  32.057  1.00 35.28  ? 3744 GLN A CA    1 
ATOM   16259 C  C     . GLN A 1 3744 ? 102.571 76.832  30.619  1.00 37.78  ? 3744 GLN A C     1 
ATOM   16260 O  O     . GLN A 1 3744 ? 103.630 76.263  30.339  1.00 43.30  ? 3744 GLN A O     1 
ATOM   16261 C  CB    . GLN A 1 3744 ? 101.083 75.721  32.302  1.00 35.50  ? 3744 GLN A CB    1 
ATOM   16262 C  CG    . GLN A 1 3744 ? 100.389 75.750  33.647  1.00 40.21  ? 3744 GLN A CG    1 
ATOM   16263 C  CD    . GLN A 1 3744 ? 99.644  74.464  33.942  1.00 45.18  ? 3744 GLN A CD    1 
ATOM   16264 O  OE1   . GLN A 1 3744 ? 98.687  74.115  33.251  1.00 48.01  ? 3744 GLN A OE1   1 
ATOM   16265 N  NE2   . GLN A 1 3744 ? 100.080 73.751  34.973  1.00 45.26  ? 3744 GLN A NE2   1 
ATOM   16266 N  N     . LEU A 1 3745 ? 101.821 77.430  29.692  1.00 34.91  ? 3745 LEU A N     1 
ATOM   16267 C  CA    . LEU A 1 3745 ? 102.244 77.447  28.295  1.00 40.64  ? 3745 LEU A CA    1 
ATOM   16268 C  C     . LEU A 1 3745 ? 103.512 78.270  28.105  1.00 39.37  ? 3745 LEU A C     1 
ATOM   16269 O  O     . LEU A 1 3745 ? 104.413 77.865  27.361  1.00 42.63  ? 3745 LEU A O     1 
ATOM   16270 C  CB    . LEU A 1 3745 ? 101.118 77.979  27.409  1.00 37.95  ? 3745 LEU A CB    1 
ATOM   16271 C  CG    . LEU A 1 3745 ? 99.917  77.047  27.250  1.00 39.81  ? 3745 LEU A CG    1 
ATOM   16272 C  CD1   . LEU A 1 3745 ? 98.798  77.735  26.492  1.00 40.11  ? 3745 LEU A CD1   1 
ATOM   16273 C  CD2   . LEU A 1 3745 ? 100.329 75.762  26.553  1.00 42.17  ? 3745 LEU A CD2   1 
ATOM   16274 N  N     . GLU A 1 3746 ? 103.601 79.429  28.762  1.00 40.43  ? 3746 GLU A N     1 
ATOM   16275 C  CA    . GLU A 1 3746 ? 104.822 80.227  28.675  1.00 43.10  ? 3746 GLU A CA    1 
ATOM   16276 C  C     . GLU A 1 3746 ? 106.015 79.470  29.250  1.00 44.18  ? 3746 GLU A C     1 
ATOM   16277 O  O     . GLU A 1 3746 ? 107.099 79.445  28.648  1.00 49.29  ? 3746 GLU A O     1 
ATOM   16278 C  CB    . GLU A 1 3746 ? 104.632 81.561  29.396  1.00 43.29  ? 3746 GLU A CB    1 
ATOM   16279 C  CG    . GLU A 1 3746 ? 105.837 82.489  29.328  1.00 54.99  ? 3746 GLU A CG    1 
ATOM   16280 C  CD    . GLU A 1 3746 ? 106.145 82.960  27.919  1.00 67.86  ? 3746 GLU A CD    1 
ATOM   16281 O  OE1   . GLU A 1 3746 ? 105.217 83.000  27.084  1.00 68.41  ? 3746 GLU A OE1   1 
ATOM   16282 O  OE2   . GLU A 1 3746 ? 107.318 83.292  27.647  1.00 73.69  ? 3746 GLU A OE2   1 
ATOM   16283 N  N     . LYS A 1 3747 ? 105.827 78.834  30.411  1.00 41.44  ? 3747 LYS A N     1 
ATOM   16284 C  CA    . LYS A 1 3747 ? 106.911 78.065  31.014  1.00 43.73  ? 3747 LYS A CA    1 
ATOM   16285 C  C     . LYS A 1 3747 ? 107.329 76.906  30.119  1.00 45.24  ? 3747 LYS A C     1 
ATOM   16286 O  O     . LYS A 1 3747 ? 108.524 76.626  29.968  1.00 47.52  ? 3747 LYS A O     1 
ATOM   16287 C  CB    . LYS A 1 3747 ? 106.487 77.556  32.391  1.00 44.33  ? 3747 LYS A CB    1 
ATOM   16288 C  CG    . LYS A 1 3747 ? 106.305 78.652  33.427  1.00 50.62  ? 3747 LYS A CG    1 
ATOM   16289 C  CD    . LYS A 1 3747 ? 105.911 78.077  34.777  1.00 59.90  ? 3747 LYS A CD    1 
ATOM   16290 C  CE    . LYS A 1 3747 ? 105.708 79.178  35.805  1.00 58.02  ? 3747 LYS A CE    1 
ATOM   16291 N  NZ    . LYS A 1 3747 ? 105.309 78.633  37.131  1.00 62.10  ? 3747 LYS A NZ    1 
ATOM   16292 N  N     . SER A 1 3748 ? 106.356 76.220  29.515  1.00 46.95  ? 3748 SER A N     1 
ATOM   16293 C  CA    . SER A 1 3748 ? 106.660 75.093  28.641  1.00 42.65  ? 3748 SER A CA    1 
ATOM   16294 C  C     . SER A 1 3748 ? 107.395 75.544  27.387  1.00 41.57  ? 3748 SER A C     1 
ATOM   16295 O  O     . SER A 1 3748 ? 108.327 74.872  26.940  1.00 46.27  ? 3748 SER A O     1 
ATOM   16296 C  CB    . SER A 1 3748 ? 105.374 74.353  28.274  1.00 41.46  ? 3748 SER A CB    1 
ATOM   16297 O  OG    . SER A 1 3748 ? 104.700 73.901  29.435  1.00 43.97  ? 3748 SER A OG    1 
ATOM   16298 N  N     . LEU A 1 3749 ? 106.986 76.673  26.802  1.00 37.04  ? 3749 LEU A N     1 
ATOM   16299 C  CA    . LEU A 1 3749 ? 107.696 77.205  25.643  1.00 40.84  ? 3749 LEU A CA    1 
ATOM   16300 C  C     . LEU A 1 3749 ? 109.141 77.537  25.992  1.00 42.51  ? 3749 LEU A C     1 
ATOM   16301 O  O     . LEU A 1 3749 ? 110.073 77.158  25.264  1.00 44.93  ? 3749 LEU A O     1 
ATOM   16302 C  CB    . LEU A 1 3749 ? 106.972 78.446  25.119  1.00 44.93  ? 3749 LEU A CB    1 
ATOM   16303 C  CG    . LEU A 1 3749 ? 107.513 79.133  23.863  1.00 47.60  ? 3749 LEU A CG    1 
ATOM   16304 C  CD1   . LEU A 1 3749 ? 107.444 78.204  22.669  1.00 49.82  ? 3749 LEU A CD1   1 
ATOM   16305 C  CD2   . LEU A 1 3749 ? 106.750 80.417  23.587  1.00 54.66  ? 3749 LEU A CD2   1 
ATOM   16306 N  N     . LEU A 1 3750 ? 109.347 78.227  27.117  1.00 48.15  ? 3750 LEU A N     1 
ATOM   16307 C  CA    . LEU A 1 3750 ? 110.704 78.581  27.516  1.00 45.89  ? 3750 LEU A CA    1 
ATOM   16308 C  C     . LEU A 1 3750 ? 111.546 77.338  27.774  1.00 45.19  ? 3750 LEU A C     1 
ATOM   16309 O  O     . LEU A 1 3750 ? 112.693 77.256  27.321  1.00 47.88  ? 3750 LEU A O     1 
ATOM   16310 C  CB    . LEU A 1 3750 ? 110.671 79.480  28.751  1.00 44.83  ? 3750 LEU A CB    1 
ATOM   16311 C  CG    . LEU A 1 3750 ? 111.852 80.439  28.900  1.00 44.74  ? 3750 LEU A CG    1 
ATOM   16312 C  CD1   . LEU A 1 3750 ? 112.098 81.197  27.606  1.00 46.55  ? 3750 LEU A CD1   1 
ATOM   16313 C  CD2   . LEU A 1 3750 ? 111.599 81.403  30.042  1.00 44.43  ? 3750 LEU A CD2   1 
ATOM   16314 N  N     . GLN A 1 3751 ? 110.988 76.347  28.474  1.00 47.43  ? 3751 GLN A N     1 
ATOM   16315 C  CA    . GLN A 1 3751 ? 111.756 75.145  28.779  1.00 53.71  ? 3751 GLN A CA    1 
ATOM   16316 C  C     . GLN A 1 3751 ? 112.017 74.308  27.532  1.00 57.62  ? 3751 GLN A C     1 
ATOM   16317 O  O     . GLN A 1 3751 ? 113.072 73.672  27.428  1.00 62.52  ? 3751 GLN A O     1 
ATOM   16318 C  CB    . GLN A 1 3751 ? 111.044 74.322  29.857  1.00 49.98  ? 3751 GLN A CB    1 
ATOM   16319 C  CG    . GLN A 1 3751 ? 110.014 73.332  29.345  1.00 57.15  ? 3751 GLN A CG    1 
ATOM   16320 C  CD    . GLN A 1 3751 ? 109.626 72.305  30.389  1.00 66.61  ? 3751 GLN A CD    1 
ATOM   16321 O  OE1   . GLN A 1 3751 ? 109.386 72.642  31.548  1.00 70.63  ? 3751 GLN A OE1   1 
ATOM   16322 N  NE2   . GLN A 1 3751 ? 109.565 71.042  29.983  1.00 66.34  ? 3751 GLN A NE2   1 
ATOM   16323 N  N     . ALA A 1 3752 ? 111.085 74.297  26.576  1.00 53.72  ? 3752 ALA A N     1 
ATOM   16324 C  CA    . ALA A 1 3752 ? 111.320 73.594  25.321  1.00 51.24  ? 3752 ALA A CA    1 
ATOM   16325 C  C     . ALA A 1 3752 ? 112.450 74.245  24.543  1.00 51.42  ? 3752 ALA A C     1 
ATOM   16326 O  O     . ALA A 1 3752 ? 113.255 73.553  23.908  1.00 56.42  ? 3752 ALA A O     1 
ATOM   16327 C  CB    . ALA A 1 3752 ? 110.040 73.557  24.488  1.00 47.63  ? 3752 ALA A CB    1 
ATOM   16328 N  N     . LEU A 1 3753 ? 112.525 75.577  24.574  1.00 50.01  ? 3753 LEU A N     1 
ATOM   16329 C  CA    . LEU A 1 3753 ? 113.681 76.235  23.975  1.00 50.17  ? 3753 LEU A CA    1 
ATOM   16330 C  C     . LEU A 1 3753 ? 114.962 75.948  24.752  1.00 55.14  ? 3753 LEU A C     1 
ATOM   16331 O  O     . LEU A 1 3753 ? 116.036 75.839  24.149  1.00 62.11  ? 3753 LEU A O     1 
ATOM   16332 C  CB    . LEU A 1 3753 ? 113.449 77.742  23.867  1.00 46.63  ? 3753 LEU A CB    1 
ATOM   16333 C  CG    . LEU A 1 3753 ? 112.972 78.227  22.496  1.00 47.44  ? 3753 LEU A CG    1 
ATOM   16334 C  CD1   . LEU A 1 3753 ? 111.630 77.616  22.129  1.00 48.75  ? 3753 LEU A CD1   1 
ATOM   16335 C  CD2   . LEU A 1 3753 ? 112.914 79.742  22.441  1.00 45.66  ? 3753 LEU A CD2   1 
ATOM   16336 N  N     . ASN A 1 3754 ? 114.880 75.831  26.078  1.00 53.50  ? 3754 ASN A N     1 
ATOM   16337 C  CA    . ASN A 1 3754 ? 116.067 75.636  26.903  1.00 54.05  ? 3754 ASN A CA    1 
ATOM   16338 C  C     . ASN A 1 3754 ? 116.579 74.200  26.919  1.00 61.33  ? 3754 ASN A C     1 
ATOM   16339 O  O     . ASN A 1 3754 ? 117.746 73.986  27.262  1.00 67.01  ? 3754 ASN A O     1 
ATOM   16340 C  CB    . ASN A 1 3754 ? 115.801 76.078  28.348  1.00 53.82  ? 3754 ASN A CB    1 
ATOM   16341 C  CG    . ASN A 1 3754 ? 115.571 77.572  28.475  1.00 49.73  ? 3754 ASN A CG    1 
ATOM   16342 O  OD1   . ASN A 1 3754 ? 114.582 78.012  29.059  1.00 56.07  ? 3754 ASN A OD1   1 
ATOM   16343 N  ND2   . ASN A 1 3754 ? 116.485 78.360  27.926  1.00 44.50  ? 3754 ASN A ND2   1 
ATOM   16344 N  N     . GLU A 1 3755 ? 115.753 73.217  26.564  1.00 64.58  ? 3755 GLU A N     1 
ATOM   16345 C  CA    . GLU A 1 3755 ? 116.140 71.814  26.657  1.00 68.28  ? 3755 GLU A CA    1 
ATOM   16346 C  C     . GLU A 1 3755 ? 116.350 71.157  25.299  1.00 71.08  ? 3755 GLU A C     1 
ATOM   16347 O  O     . GLU A 1 3755 ? 116.377 69.924  25.218  1.00 77.07  ? 3755 GLU A O     1 
ATOM   16348 C  CB    . GLU A 1 3755 ? 115.103 71.026  27.461  1.00 68.87  ? 3755 GLU A CB    1 
ATOM   16349 C  CG    . GLU A 1 3755 ? 114.852 71.565  28.859  1.00 72.23  ? 3755 GLU A CG    1 
ATOM   16350 C  CD    . GLU A 1 3755 ? 113.502 71.150  29.408  1.00 80.64  ? 3755 GLU A CD    1 
ATOM   16351 O  OE1   . GLU A 1 3755 ? 112.684 70.611  28.633  1.00 79.19  ? 3755 GLU A OE1   1 
ATOM   16352 O  OE2   . GLU A 1 3755 ? 113.258 71.361  30.614  1.00 79.78  ? 3755 GLU A OE2   1 
ATOM   16353 N  N     . VAL A 1 3756 ? 116.500 71.938  24.234  1.00 65.70  ? 3756 VAL A N     1 
ATOM   16354 C  CA    . VAL A 1 3756 ? 116.773 71.403  22.905  1.00 68.29  ? 3756 VAL A CA    1 
ATOM   16355 C  C     . VAL A 1 3756 ? 118.252 71.587  22.597  1.00 74.37  ? 3756 VAL A C     1 
ATOM   16356 O  O     . VAL A 1 3756 ? 118.825 72.656  22.842  1.00 75.32  ? 3756 VAL A O     1 
ATOM   16357 C  CB    . VAL A 1 3756 ? 115.883 72.068  21.835  1.00 65.51  ? 3756 VAL A CB    1 
ATOM   16358 C  CG1   . VAL A 1 3756 ? 116.057 73.581  21.837  1.00 63.10  ? 3756 VAL A CG1   1 
ATOM   16359 C  CG2   . VAL A 1 3756 ? 116.178 71.490  20.458  1.00 65.52  ? 3756 VAL A CG2   1 
ATOM   16360 N  N     . LYS A 1 3757 ? 118.881 70.532  22.090  1.00 74.54  ? 3757 LYS A N     1 
ATOM   16361 C  CA    . LYS A 1 3757 ? 120.291 70.558  21.733  1.00 73.95  ? 3757 LYS A CA    1 
ATOM   16362 C  C     . LYS A 1 3757 ? 120.455 70.789  20.235  1.00 74.33  ? 3757 LYS A C     1 
ATOM   16363 O  O     . LYS A 1 3757 ? 119.549 70.536  19.438  1.00 72.65  ? 3757 LYS A O     1 
ATOM   16364 C  CB    . LYS A 1 3757 ? 120.981 69.255  22.145  1.00 72.69  ? 3757 LYS A CB    1 
ATOM   16365 C  CG    . LYS A 1 3757 ? 121.008 69.017  23.646  1.00 77.13  ? 3757 LYS A CG    1 
ATOM   16366 C  CD    . LYS A 1 3757 ? 121.754 67.739  23.990  1.00 75.20  ? 3757 LYS A CD    1 
ATOM   16367 C  CE    . LYS A 1 3757 ? 120.969 66.510  23.565  1.00 78.73  ? 3757 LYS A CE    1 
ATOM   16368 N  NZ    . LYS A 1 3757 ? 119.706 66.365  24.339  1.00 73.49  ? 3757 LYS A NZ    1 
ATOM   16369 N  N     . GLY A 1 3758 ? 121.637 71.273  19.861  1.00 77.49  ? 3758 GLY A N     1 
ATOM   16370 C  CA    . GLY A 1 3758 ? 121.913 71.590  18.474  1.00 78.52  ? 3758 GLY A CA    1 
ATOM   16371 C  C     . GLY A 1 3758 ? 121.079 72.745  17.962  1.00 79.21  ? 3758 GLY A C     1 
ATOM   16372 O  O     . GLY A 1 3758 ? 121.115 73.844  18.524  1.00 75.41  ? 3758 GLY A O     1 
ATOM   16373 N  N     . ARG A 1 3759 ? 120.323 72.510  16.894  1.00 80.26  ? 3759 ARG A N     1 
ATOM   16374 C  CA    . ARG A 1 3759 ? 119.459 73.519  16.306  1.00 80.91  ? 3759 ARG A CA    1 
ATOM   16375 C  C     . ARG A 1 3759 ? 118.005 73.076  16.403  1.00 80.75  ? 3759 ARG A C     1 
ATOM   16376 O  O     . ARG A 1 3759 ? 117.699 71.882  16.474  1.00 78.74  ? 3759 ARG A O     1 
ATOM   16377 C  CB    . ARG A 1 3759 ? 119.831 73.787  14.841  1.00 78.45  ? 3759 ARG A CB    1 
ATOM   16378 C  CG    . ARG A 1 3759 ? 121.319 73.985  14.609  1.00 74.34  ? 3759 ARG A CG    1 
ATOM   16379 C  CD    . ARG A 1 3759 ? 121.666 73.878  13.134  1.00 81.05  ? 3759 ARG A CD    1 
ATOM   16380 N  NE    . ARG A 1 3759 ? 121.717 72.493  12.681  1.00 84.03  ? 3759 ARG A NE    1 
ATOM   16381 C  CZ    . ARG A 1 3759 ? 121.958 72.124  11.430  1.00 82.33  ? 3759 ARG A CZ    1 
ATOM   16382 N  NH1   . ARG A 1 3759 ? 122.174 73.014  10.476  1.00 79.94  ? 3759 ARG A NH1   1 
ATOM   16383 N  NH2   . ARG A 1 3759 ? 121.980 70.828  11.130  1.00 79.70  ? 3759 ARG A NH2   1 
ATOM   16384 N  N     . ILE A 1 3760 ? 117.107 74.063  16.413  1.00 80.71  ? 3760 ILE A N     1 
ATOM   16385 C  CA    . ILE A 1 3760 ? 115.682 73.771  16.528  1.00 81.52  ? 3760 ILE A CA    1 
ATOM   16386 C  C     . ILE A 1 3760 ? 115.182 73.033  15.291  1.00 83.86  ? 3760 ILE A C     1 
ATOM   16387 O  O     . ILE A 1 3760 ? 114.391 72.087  15.394  1.00 83.76  ? 3760 ILE A O     1 
ATOM   16388 C  CB    . ILE A 1 3760 ? 114.893 75.070  16.777  1.00 78.57  ? 3760 ILE A CB    1 
ATOM   16389 C  CG1   . ILE A 1 3760 ? 115.296 75.685  18.119  1.00 73.08  ? 3760 ILE A CG1   1 
ATOM   16390 C  CG2   . ILE A 1 3760 ? 113.395 74.807  16.740  1.00 78.60  ? 3760 ILE A CG2   1 
ATOM   16391 C  CD1   . ILE A 1 3760 ? 114.596 76.990  18.431  1.00 64.31  ? 3760 ILE A CD1   1 
ATOM   16392 N  N     . LEU A 1 3761 ? 115.638 73.443  14.105  1.00 81.50  ? 3761 LEU A N     1 
ATOM   16393 C  CA    . LEU A 1 3761 ? 115.170 72.826  12.868  1.00 79.61  ? 3761 LEU A CA    1 
ATOM   16394 C  C     . LEU A 1 3761 ? 115.621 71.378  12.723  1.00 84.36  ? 3761 LEU A C     1 
ATOM   16395 O  O     . LEU A 1 3761 ? 115.019 70.636  11.940  1.00 86.61  ? 3761 LEU A O     1 
ATOM   16396 C  CB    . LEU A 1 3761 ? 115.649 73.631  11.658  1.00 79.07  ? 3761 LEU A CB    1 
ATOM   16397 C  CG    . LEU A 1 3761 ? 114.917 74.939  11.353  1.00 75.89  ? 3761 LEU A CG    1 
ATOM   16398 C  CD1   . LEU A 1 3761 ? 115.557 76.094  12.101  1.00 73.84  ? 3761 LEU A CD1   1 
ATOM   16399 C  CD2   . LEU A 1 3761 ? 114.899 75.208  9.857   1.00 81.29  ? 3761 LEU A CD2   1 
ATOM   16400 N  N     . ASP A 1 3762 ? 116.662 70.962  13.448  1.00 86.19  ? 3762 ASP A N     1 
ATOM   16401 C  CA    . ASP A 1 3762 ? 117.150 69.592  13.318  1.00 86.26  ? 3762 ASP A CA    1 
ATOM   16402 C  C     . ASP A 1 3762 ? 116.099 68.581  13.763  1.00 87.21  ? 3762 ASP A C     1 
ATOM   16403 O  O     . ASP A 1 3762 ? 115.922 67.540  13.120  1.00 88.44  ? 3762 ASP A O     1 
ATOM   16404 C  CB    . ASP A 1 3762 ? 118.439 69.412  14.118  1.00 83.30  ? 3762 ASP A CB    1 
ATOM   16405 C  CG    . ASP A 1 3762 ? 119.621 70.117  13.483  1.00 86.81  ? 3762 ASP A CG    1 
ATOM   16406 O  OD1   . ASP A 1 3762 ? 119.747 70.066  12.242  1.00 86.07  ? 3762 ASP A OD1   1 
ATOM   16407 O  OD2   . ASP A 1 3762 ? 120.429 70.712  14.226  1.00 88.19  ? 3762 ASP A OD2   1 
ATOM   16408 N  N     . ASP A 1 3763 ? 115.395 68.866  14.855  1.00 85.82  ? 3763 ASP A N     1 
ATOM   16409 C  CA    . ASP A 1 3763 ? 114.372 67.976  15.392  1.00 85.39  ? 3763 ASP A CA    1 
ATOM   16410 C  C     . ASP A 1 3763 ? 113.005 68.579  15.093  1.00 82.17  ? 3763 ASP A C     1 
ATOM   16411 O  O     . ASP A 1 3763 ? 112.657 69.639  15.625  1.00 80.22  ? 3763 ASP A O     1 
ATOM   16412 C  CB    . ASP A 1 3763 ? 114.566 67.762  16.891  1.00 83.45  ? 3763 ASP A CB    1 
ATOM   16413 C  CG    . ASP A 1 3763 ? 113.550 66.805  17.480  1.00 85.56  ? 3763 ASP A CG    1 
ATOM   16414 O  OD1   . ASP A 1 3763 ? 113.445 65.665  16.981  1.00 85.39  ? 3763 ASP A OD1   1 
ATOM   16415 O  OD2   . ASP A 1 3763 ? 112.857 67.191  18.445  1.00 82.69  ? 3763 ASP A OD2   1 
ATOM   16416 N  N     . ASP A 1 3764 ? 112.231 67.903  14.240  1.00 83.43  ? 3764 ASP A N     1 
ATOM   16417 C  CA    . ASP A 1 3764 ? 110.900 68.386  13.894  1.00 81.60  ? 3764 ASP A CA    1 
ATOM   16418 C  C     . ASP A 1 3764 ? 109.916 68.247  15.049  1.00 79.30  ? 3764 ASP A C     1 
ATOM   16419 O  O     . ASP A 1 3764 ? 108.899 68.950  15.068  1.00 80.58  ? 3764 ASP A O     1 
ATOM   16420 C  CB    . ASP A 1 3764 ? 110.373 67.640  12.667  1.00 84.40  ? 3764 ASP A CB    1 
ATOM   16421 C  CG    . ASP A 1 3764 ? 111.118 68.007  11.399  1.00 90.05  ? 3764 ASP A CG    1 
ATOM   16422 O  OD1   . ASP A 1 3764 ? 112.082 68.797  11.482  1.00 91.33  ? 3764 ASP A OD1   1 
ATOM   16423 O  OD2   . ASP A 1 3764 ? 110.741 67.506  10.319  1.00 85.57  ? 3764 ASP A OD2   1 
ATOM   16424 N  N     . THR A 1 3765 ? 110.194 67.358  16.006  1.00 77.27  ? 3765 THR A N     1 
ATOM   16425 C  CA    . THR A 1 3765 ? 109.328 67.233  17.173  1.00 75.33  ? 3765 THR A CA    1 
ATOM   16426 C  C     . THR A 1 3765 ? 109.311 68.525  17.980  1.00 70.99  ? 3765 THR A C     1 
ATOM   16427 O  O     . THR A 1 3765 ? 108.256 68.952  18.463  1.00 69.61  ? 3765 THR A O     1 
ATOM   16428 C  CB    . THR A 1 3765 ? 109.783 66.060  18.043  1.00 74.96  ? 3765 THR A CB    1 
ATOM   16429 O  OG1   . THR A 1 3765 ? 109.780 64.857  17.264  1.00 77.02  ? 3765 THR A OG1   1 
ATOM   16430 C  CG2   . THR A 1 3765 ? 108.855 65.884  19.235  1.00 69.63  ? 3765 THR A CG2   1 
ATOM   16431 N  N     . ILE A 1 3766 ? 110.474 69.163  18.130  1.00 69.08  ? 3766 ILE A N     1 
ATOM   16432 C  CA    . ILE A 1 3766 ? 110.541 70.444  18.827  1.00 68.38  ? 3766 ILE A CA    1 
ATOM   16433 C  C     . ILE A 1 3766 ? 109.700 71.488  18.103  1.00 68.43  ? 3766 ILE A C     1 
ATOM   16434 O  O     . ILE A 1 3766 ? 108.970 72.263  18.732  1.00 69.19  ? 3766 ILE A O     1 
ATOM   16435 C  CB    . ILE A 1 3766 ? 112.007 70.895  18.974  1.00 70.28  ? 3766 ILE A CB    1 
ATOM   16436 C  CG1   . ILE A 1 3766 ? 112.725 70.044  20.022  1.00 70.64  ? 3766 ILE A CG1   1 
ATOM   16437 C  CG2   . ILE A 1 3766 ? 112.086 72.370  19.341  1.00 65.91  ? 3766 ILE A CG2   1 
ATOM   16438 C  CD1   . ILE A 1 3766 ? 112.149 70.175  21.414  1.00 70.36  ? 3766 ILE A CD1   1 
ATOM   16439 N  N     . ILE A 1 3767 ? 109.785 71.519  16.771  1.00 66.93  ? 3767 ILE A N     1 
ATOM   16440 C  CA    . ILE A 1 3767 ? 109.005 72.479  15.993  1.00 67.68  ? 3767 ILE A CA    1 
ATOM   16441 C  C     . ILE A 1 3767 ? 107.513 72.237  16.185  1.00 65.09  ? 3767 ILE A C     1 
ATOM   16442 O  O     . ILE A 1 3767 ? 106.733 73.182  16.363  1.00 67.05  ? 3767 ILE A O     1 
ATOM   16443 C  CB    . ILE A 1 3767 ? 109.403 72.409  14.507  1.00 69.52  ? 3767 ILE A CB    1 
ATOM   16444 C  CG1   . ILE A 1 3767 ? 110.896 72.698  14.340  1.00 73.97  ? 3767 ILE A CG1   1 
ATOM   16445 C  CG2   . ILE A 1 3767 ? 108.574 73.383  13.685  1.00 63.99  ? 3767 ILE A CG2   1 
ATOM   16446 C  CD1   . ILE A 1 3767 ? 111.355 72.725  12.898  1.00 79.44  ? 3767 ILE A CD1   1 
ATOM   16447 N  N     . THR A 1 3768 ? 107.091 70.970  16.144  1.00 63.67  ? 3768 THR A N     1 
ATOM   16448 C  CA    . THR A 1 3768 ? 105.678 70.658  16.336  1.00 65.84  ? 3768 THR A CA    1 
ATOM   16449 C  C     . THR A 1 3768 ? 105.207 71.065  17.727  1.00 66.63  ? 3768 THR A C     1 
ATOM   16450 O  O     . THR A 1 3768 ? 104.108 71.612  17.882  1.00 69.48  ? 3768 THR A O     1 
ATOM   16451 C  CB    . THR A 1 3768 ? 105.425 69.168  16.103  1.00 65.80  ? 3768 THR A CB    1 
ATOM   16452 O  OG1   . THR A 1 3768 ? 106.293 68.396  16.941  1.00 68.42  ? 3768 THR A OG1   1 
ATOM   16453 C  CG2   . THR A 1 3768 ? 105.676 68.807  14.646  1.00 66.41  ? 3768 THR A CG2   1 
ATOM   16454 N  N     . THR A 1 3769 ? 106.025 70.807  18.752  1.00 64.25  ? 3769 THR A N     1 
ATOM   16455 C  CA    . THR A 1 3769 ? 105.654 71.211  20.105  1.00 63.51  ? 3769 THR A CA    1 
ATOM   16456 C  C     . THR A 1 3769 ? 105.537 72.726  20.214  1.00 60.44  ? 3769 THR A C     1 
ATOM   16457 O  O     . THR A 1 3769 ? 104.611 73.238  20.853  1.00 61.46  ? 3769 THR A O     1 
ATOM   16458 C  CB    . THR A 1 3769 ? 106.668 70.681  21.120  1.00 62.40  ? 3769 THR A CB    1 
ATOM   16459 O  OG1   . THR A 1 3769 ? 107.984 71.125  20.766  1.00 67.13  ? 3769 THR A OG1   1 
ATOM   16460 C  CG2   . THR A 1 3769 ? 106.634 69.160  21.170  1.00 62.56  ? 3769 THR A CG2   1 
ATOM   16461 N  N     . LEU A 1 3770 ? 106.467 73.460  19.597  1.00 55.19  ? 3770 LEU A N     1 
ATOM   16462 C  CA    . LEU A 1 3770 ? 106.399 74.918  19.637  1.00 60.77  ? 3770 LEU A CA    1 
ATOM   16463 C  C     . LEU A 1 3770 ? 105.136 75.426  18.954  1.00 63.59  ? 3770 LEU A C     1 
ATOM   16464 O  O     . LEU A 1 3770 ? 104.462 76.332  19.465  1.00 59.87  ? 3770 LEU A O     1 
ATOM   16465 C  CB    . LEU A 1 3770 ? 107.639 75.524  18.978  1.00 56.63  ? 3770 LEU A CB    1 
ATOM   16466 C  CG    . LEU A 1 3770 ? 108.998 75.248  19.627  1.00 54.84  ? 3770 LEU A CG    1 
ATOM   16467 C  CD1   . LEU A 1 3770 ? 110.075 76.153  19.042  1.00 53.57  ? 3770 LEU A CD1   1 
ATOM   16468 C  CD2   . LEU A 1 3770 ? 108.934 75.368  21.139  1.00 55.15  ? 3770 LEU A CD2   1 
ATOM   16469 N  N     . GLU A 1 3771 ? 104.798 74.850  17.797  1.00 63.89  ? 3771 GLU A N     1 
ATOM   16470 C  CA    . GLU A 1 3771 ? 103.585 75.259  17.095  1.00 61.91  ? 3771 GLU A CA    1 
ATOM   16471 C  C     . GLU A 1 3771 ? 102.342 74.969  17.925  1.00 59.69  ? 3771 GLU A C     1 
ATOM   16472 O  O     . GLU A 1 3771 ? 101.432 75.804  18.004  1.00 62.71  ? 3771 GLU A O     1 
ATOM   16473 C  CB    . GLU A 1 3771 ? 103.496 74.559  15.739  1.00 64.10  ? 3771 GLU A CB    1 
ATOM   16474 C  CG    . GLU A 1 3771 ? 104.617 74.907  14.777  1.00 63.35  ? 3771 GLU A CG    1 
ATOM   16475 C  CD    . GLU A 1 3771 ? 104.670 73.972  13.586  1.00 69.92  ? 3771 GLU A CD    1 
ATOM   16476 O  OE1   . GLU A 1 3771 ? 104.687 72.740  13.794  1.00 73.40  ? 3771 GLU A OE1   1 
ATOM   16477 O  OE2   . GLU A 1 3771 ? 104.691 74.468  12.440  1.00 72.17  ? 3771 GLU A OE2   1 
ATOM   16478 N  N     . ASN A 1 3772 ? 102.285 73.791  18.553  1.00 54.98  ? 3772 ASN A N     1 
ATOM   16479 C  CA    . ASN A 1 3772 ? 101.134 73.455  19.386  1.00 56.86  ? 3772 ASN A CA    1 
ATOM   16480 C  C     . ASN A 1 3772 ? 101.013 74.406  20.570  1.00 57.40  ? 3772 ASN A C     1 
ATOM   16481 O  O     . ASN A 1 3772 ? 99.910  74.858  20.904  1.00 58.07  ? 3772 ASN A O     1 
ATOM   16482 C  CB    . ASN A 1 3772 ? 101.234 72.008  19.868  1.00 60.11  ? 3772 ASN A CB    1 
ATOM   16483 C  CG    . ASN A 1 3772 ? 101.259 71.013  18.725  1.00 61.38  ? 3772 ASN A CG    1 
ATOM   16484 O  OD1   . ASN A 1 3772 ? 101.252 71.393  17.554  1.00 63.51  ? 3772 ASN A OD1   1 
ATOM   16485 N  ND2   . ASN A 1 3772 ? 101.287 69.728  19.060  1.00 55.96  ? 3772 ASN A ND2   1 
ATOM   16486 N  N     . LEU A 1 3773 ? 102.139 74.721  21.218  1.00 57.01  ? 3773 LEU A N     1 
ATOM   16487 C  CA    . LEU A 1 3773 ? 102.105 75.639  22.351  1.00 51.82  ? 3773 LEU A CA    1 
ATOM   16488 C  C     . LEU A 1 3773 ? 101.627 77.022  21.929  1.00 53.71  ? 3773 LEU A C     1 
ATOM   16489 O  O     . LEU A 1 3773 ? 100.800 77.634  22.614  1.00 56.11  ? 3773 LEU A O     1 
ATOM   16490 C  CB    . LEU A 1 3773 ? 103.484 75.724  23.006  1.00 50.16  ? 3773 LEU A CB    1 
ATOM   16491 C  CG    . LEU A 1 3773 ? 103.999 74.457  23.692  1.00 48.62  ? 3773 LEU A CG    1 
ATOM   16492 C  CD1   . LEU A 1 3773 ? 105.379 74.689  24.286  1.00 43.86  ? 3773 LEU A CD1   1 
ATOM   16493 C  CD2   . LEU A 1 3773 ? 103.025 73.986  24.759  1.00 51.02  ? 3773 LEU A CD2   1 
ATOM   16494 N  N     . LYS A 1 3774 ? 102.128 77.529  20.799  1.00 50.13  ? 3774 LYS A N     1 
ATOM   16495 C  CA    . LYS A 1 3774 ? 101.698 78.847  20.337  1.00 53.22  ? 3774 LYS A CA    1 
ATOM   16496 C  C     . LYS A 1 3774 ? 100.218 78.853  19.970  1.00 52.90  ? 3774 LYS A C     1 
ATOM   16497 O  O     . LYS A 1 3774 ? 99.495  79.807  20.289  1.00 57.52  ? 3774 LYS A O     1 
ATOM   16498 C  CB    . LYS A 1 3774 ? 102.549 79.296  19.150  1.00 57.97  ? 3774 LYS A CB    1 
ATOM   16499 C  CG    . LYS A 1 3774 ? 103.910 79.852  19.541  1.00 59.89  ? 3774 LYS A CG    1 
ATOM   16500 C  CD    . LYS A 1 3774 ? 103.774 81.135  20.351  1.00 59.48  ? 3774 LYS A CD    1 
ATOM   16501 C  CE    . LYS A 1 3774 ? 102.893 82.156  19.646  1.00 57.40  ? 3774 LYS A CE    1 
ATOM   16502 N  NZ    . LYS A 1 3774 ? 102.882 83.470  20.344  1.00 68.01  ? 3774 LYS A NZ    1 
ATOM   16503 N  N     . ARG A 1 3775 ? 99.750  77.797  19.299  1.00 51.15  ? 3775 ARG A N     1 
ATOM   16504 C  CA    . ARG A 1 3775 ? 98.340  77.708  18.932  1.00 55.24  ? 3775 ARG A CA    1 
ATOM   16505 C  C     . ARG A 1 3775 ? 97.455  77.707  20.172  1.00 54.25  ? 3775 ARG A C     1 
ATOM   16506 O  O     . ARG A 1 3775 ? 96.459  78.444  20.248  1.00 54.65  ? 3775 ARG A O     1 
ATOM   16507 C  CB    . ARG A 1 3775 ? 98.108  76.442  18.107  1.00 57.89  ? 3775 ARG A CB    1 
ATOM   16508 C  CG    . ARG A 1 3775 ? 96.703  76.284  17.558  1.00 62.76  ? 3775 ARG A CG    1 
ATOM   16509 C  CD    . ARG A 1 3775 ? 96.587  75.000  16.750  1.00 62.00  ? 3775 ARG A CD    1 
ATOM   16510 N  NE    . ARG A 1 3775 ? 97.445  75.009  15.572  1.00 75.48  ? 3775 ARG A NE    1 
ATOM   16511 C  CZ    . ARG A 1 3775 ? 98.498  74.219  15.409  1.00 72.82  ? 3775 ARG A CZ    1 
ATOM   16512 N  NH1   . ARG A 1 3775 ? 98.855  73.344  16.335  1.00 67.53  ? 3775 ARG A NH1   1 
ATOM   16513 N  NH2   . ARG A 1 3775 ? 99.212  74.311  14.291  1.00 71.45  ? 3775 ARG A NH2   1 
ATOM   16514 N  N     . GLU A 1 3776 ? 97.810  76.881  21.161  1.00 51.41  ? 3776 GLU A N     1 
ATOM   16515 C  CA    . GLU A 1 3776 ? 97.021  76.812  22.383  1.00 49.98  ? 3776 GLU A CA    1 
ATOM   16516 C  C     . GLU A 1 3776 ? 97.052  78.137  23.132  1.00 49.47  ? 3776 GLU A C     1 
ATOM   16517 O  O     . GLU A 1 3776 ? 96.031  78.568  23.676  1.00 52.37  ? 3776 GLU A O     1 
ATOM   16518 C  CB    . GLU A 1 3776 ? 97.519  75.673  23.272  1.00 43.88  ? 3776 GLU A CB    1 
ATOM   16519 C  CG    . GLU A 1 3776 ? 96.674  75.454  24.517  1.00 49.56  ? 3776 GLU A CG    1 
ATOM   16520 C  CD    . GLU A 1 3776 ? 97.147  74.279  25.347  1.00 56.10  ? 3776 GLU A CD    1 
ATOM   16521 O  OE1   . GLU A 1 3776 ? 98.153  73.645  24.966  1.00 58.62  ? 3776 GLU A OE1   1 
ATOM   16522 O  OE2   . GLU A 1 3776 ? 96.510  73.986  26.381  1.00 53.90  ? 3776 GLU A OE2   1 
ATOM   16523 N  N     . ALA A 1 3777 ? 98.209  78.803  23.165  1.00 44.78  ? 3777 ALA A N     1 
ATOM   16524 C  CA    . ALA A 1 3777 ? 98.291  80.102  23.822  1.00 46.85  ? 3777 ALA A CA    1 
ATOM   16525 C  C     . ALA A 1 3777 ? 97.376  81.117  23.152  1.00 51.14  ? 3777 ALA A C     1 
ATOM   16526 O  O     . ALA A 1 3777 ? 96.651  81.853  23.832  1.00 53.72  ? 3777 ALA A O     1 
ATOM   16527 C  CB    . ALA A 1 3777 ? 99.737  80.599  23.825  1.00 41.63  ? 3777 ALA A CB    1 
ATOM   16528 N  N     . ALA A 1 3778 ? 97.378  81.156  21.817  1.00 51.42  ? 3778 ALA A N     1 
ATOM   16529 C  CA    . ALA A 1 3778 ? 96.529  82.110  21.107  1.00 48.93  ? 3778 ALA A CA    1 
ATOM   16530 C  C     . ALA A 1 3778 ? 95.050  81.841  21.362  1.00 48.68  ? 3778 ALA A C     1 
ATOM   16531 O  O     . ALA A 1 3778 ? 94.271  82.774  21.604  1.00 52.63  ? 3778 ALA A O     1 
ATOM   16532 C  CB    . ALA A 1 3778 ? 96.833  82.068  19.610  1.00 50.28  ? 3778 ALA A CB    1 
ATOM   16533 N  N     . GLU A 1 3779 ? 94.640  80.570  21.329  1.00 47.14  ? 3779 GLU A N     1 
ATOM   16534 C  CA    . GLU A 1 3779 ? 93.220  80.272  21.505  1.00 49.62  ? 3779 GLU A CA    1 
ATOM   16535 C  C     . GLU A 1 3779 ? 92.764  80.457  22.955  1.00 50.19  ? 3779 GLU A C     1 
ATOM   16536 O  O     . GLU A 1 3779 ? 91.642  80.935  23.198  1.00 53.02  ? 3779 GLU A O     1 
ATOM   16537 C  CB    . GLU A 1 3779 ? 92.927  78.870  20.958  1.00 49.95  ? 3779 GLU A CB    1 
ATOM   16538 C  CG    . GLU A 1 3779 ? 93.687  77.727  21.608  1.00 51.61  ? 3779 GLU A CG    1 
ATOM   16539 C  CD    . GLU A 1 3779 ? 92.983  77.148  22.804  1.00 56.89  ? 3779 GLU A CD    1 
ATOM   16540 O  OE1   . GLU A 1 3779 ? 91.760  77.342  22.905  1.00 62.37  ? 3779 GLU A OE1   1 
ATOM   16541 O  OE2   . GLU A 1 3779 ? 93.645  76.489  23.632  1.00 54.36  ? 3779 GLU A OE2   1 
ATOM   16542 N  N     . VAL A 1 3780 ? 93.622  80.141  23.930  1.00 48.57  ? 3780 VAL A N     1 
ATOM   16543 C  CA    . VAL A 1 3780 ? 93.298  80.456  25.319  1.00 48.89  ? 3780 VAL A CA    1 
ATOM   16544 C  C     . VAL A 1 3780 ? 93.202  81.964  25.514  1.00 45.49  ? 3780 VAL A C     1 
ATOM   16545 O  O     . VAL A 1 3780 ? 92.326  82.453  26.236  1.00 45.66  ? 3780 VAL A O     1 
ATOM   16546 C  CB    . VAL A 1 3780 ? 94.322  79.819  26.277  1.00 42.64  ? 3780 VAL A CB    1 
ATOM   16547 C  CG1   . VAL A 1 3780 ? 94.057  80.261  27.705  1.00 39.80  ? 3780 VAL A CG1   1 
ATOM   16548 C  CG2   . VAL A 1 3780 ? 94.244  78.307  26.197  1.00 44.15  ? 3780 VAL A CG2   1 
ATOM   16549 N  N     . THR A 1 3781 ? 94.081  82.731  24.862  1.00 41.78  ? 3781 THR A N     1 
ATOM   16550 C  CA    . THR A 1 3781 ? 93.981  84.185  24.939  1.00 45.16  ? 3781 THR A CA    1 
ATOM   16551 C  C     . THR A 1 3781 ? 92.651  84.675  24.379  1.00 47.42  ? 3781 THR A C     1 
ATOM   16552 O  O     . THR A 1 3781 ? 92.014  85.562  24.961  1.00 53.70  ? 3781 THR A O     1 
ATOM   16553 C  CB    . THR A 1 3781 ? 95.148  84.831  24.192  1.00 45.95  ? 3781 THR A CB    1 
ATOM   16554 O  OG1   . THR A 1 3781 ? 96.380  84.239  24.624  1.00 44.88  ? 3781 THR A OG1   1 
ATOM   16555 C  CG2   . THR A 1 3781 ? 95.192  86.327  24.463  1.00 44.74  ? 3781 THR A CG2   1 
ATOM   16556 N  N     . ARG A 1 3782 ? 92.223  84.111  23.246  1.00 49.19  ? 3782 ARG A N     1 
ATOM   16557 C  CA    . ARG A 1 3782 ? 90.916  84.452  22.686  1.00 47.38  ? 3782 ARG A CA    1 
ATOM   16558 C  C     . ARG A 1 3782 ? 89.801  84.215  23.700  1.00 47.87  ? 3782 ARG A C     1 
ATOM   16559 O  O     . ARG A 1 3782 ? 88.940  85.088  23.916  1.00 51.42  ? 3782 ARG A O     1 
ATOM   16560 C  CB    . ARG A 1 3782 ? 90.671  83.640  21.416  1.00 51.66  ? 3782 ARG A CB    1 
ATOM   16561 C  CG    . ARG A 1 3782 ? 89.365  83.952  20.711  1.00 59.71  ? 3782 ARG A CG    1 
ATOM   16562 C  CD    . ARG A 1 3782 ? 89.216  83.105  19.460  1.00 62.40  ? 3782 ARG A CD    1 
ATOM   16563 N  NE    . ARG A 1 3782 ? 89.157  81.684  19.779  1.00 68.48  ? 3782 ARG A NE    1 
ATOM   16564 C  CZ    . ARG A 1 3782 ? 88.061  81.043  20.162  1.00 72.94  ? 3782 ARG A CZ    1 
ATOM   16565 N  NH1   . ARG A 1 3782 ? 86.902  81.669  20.285  1.00 72.39  ? 3782 ARG A NH1   1 
ATOM   16566 N  NH2   . ARG A 1 3782 ? 88.130  79.742  20.430  1.00 68.44  ? 3782 ARG A NH2   1 
ATOM   16567 N  N     . LYS A 1 3783 ? 89.802  83.041  24.341  1.00 44.81  ? 3783 LYS A N     1 
ATOM   16568 C  CA    . LYS A 1 3783 ? 88.850  82.828  25.429  1.00 46.51  ? 3783 LYS A CA    1 
ATOM   16569 C  C     . LYS A 1 3783 ? 89.011  83.878  26.523  1.00 47.19  ? 3783 LYS A C     1 
ATOM   16570 O  O     . LYS A 1 3783 ? 88.038  84.231  27.197  1.00 53.22  ? 3783 LYS A O     1 
ATOM   16571 C  CB    . LYS A 1 3783 ? 88.979  81.430  26.033  1.00 44.49  ? 3783 LYS A CB    1 
ATOM   16572 C  CG    . LYS A 1 3783 ? 88.608  80.274  25.132  1.00 47.75  ? 3783 LYS A CG    1 
ATOM   16573 C  CD    . LYS A 1 3783 ? 89.126  78.976  25.725  1.00 46.36  ? 3783 LYS A CD    1 
ATOM   16574 C  CE    . LYS A 1 3783 ? 89.454  77.961  24.665  1.00 51.81  ? 3783 LYS A CE    1 
ATOM   16575 N  NZ    . LYS A 1 3783 ? 90.224  76.813  25.224  1.00 58.03  ? 3783 LYS A NZ    1 
ATOM   16576 N  N     . VAL A 1 3784 ? 90.232  84.377  26.727  1.00 41.71  ? 3784 VAL A N     1 
ATOM   16577 C  CA    . VAL A 1 3784 ? 90.439  85.395  27.756  1.00 46.00  ? 3784 VAL A CA    1 
ATOM   16578 C  C     . VAL A 1 3784 ? 89.683  86.675  27.413  1.00 46.82  ? 3784 VAL A C     1 
ATOM   16579 O  O     . VAL A 1 3784 ? 89.015  87.254  28.275  1.00 53.37  ? 3784 VAL A O     1 
ATOM   16580 C  CB    . VAL A 1 3784 ? 91.940  85.662  27.983  1.00 48.50  ? 3784 VAL A CB    1 
ATOM   16581 C  CG1   . VAL A 1 3784 ? 92.129  86.857  28.903  1.00 47.22  ? 3784 VAL A CG1   1 
ATOM   16582 C  CG2   . VAL A 1 3784 ? 92.603  84.444  28.590  1.00 39.01  ? 3784 VAL A CG2   1 
ATOM   16583 N  N     . GLU A 1 3785 ? 89.767  87.143  26.160  1.00 43.79  ? 3785 GLU A N     1 
ATOM   16584 C  CA    . GLU A 1 3785 ? 88.987  88.346  25.836  1.00 50.26  ? 3785 GLU A CA    1 
ATOM   16585 C  C     . GLU A 1 3785 ? 87.487  88.076  25.925  1.00 51.62  ? 3785 GLU A C     1 
ATOM   16586 O  O     . GLU A 1 3785 ? 86.714  88.959  26.331  1.00 50.89  ? 3785 GLU A O     1 
ATOM   16587 C  CB    . GLU A 1 3785 ? 89.298  88.977  24.467  1.00 53.44  ? 3785 GLU A CB    1 
ATOM   16588 C  CG    . GLU A 1 3785 ? 90.675  89.614  24.262  1.00 60.23  ? 3785 GLU A CG    1 
ATOM   16589 C  CD    . GLU A 1 3785 ? 91.739  88.642  23.872  1.00 66.95  ? 3785 GLU A CD    1 
ATOM   16590 O  OE1   . GLU A 1 3785 ? 91.393  87.472  23.684  1.00 63.42  ? 3785 GLU A OE1   1 
ATOM   16591 O  OE2   . GLU A 1 3785 ? 92.916  89.043  23.758  1.00 68.01  ? 3785 GLU A OE2   1 
ATOM   16592 N  N     . GLU A 1 3786 ? 87.048  86.876  25.534  1.00 49.19  ? 3786 GLU A N     1 
ATOM   16593 C  CA    . GLU A 1 3786 ? 85.624  86.565  25.662  1.00 46.94  ? 3786 GLU A CA    1 
ATOM   16594 C  C     . GLU A 1 3786 ? 85.173  86.637  27.121  1.00 51.35  ? 3786 GLU A C     1 
ATOM   16595 O  O     . GLU A 1 3786 ? 84.143  87.249  27.448  1.00 55.76  ? 3786 GLU A O     1 
ATOM   16596 C  CB    . GLU A 1 3786 ? 85.330  85.188  25.065  1.00 49.84  ? 3786 GLU A CB    1 
ATOM   16597 C  CG    . GLU A 1 3786 ? 85.756  85.050  23.612  1.00 50.22  ? 3786 GLU A CG    1 
ATOM   16598 C  CD    . GLU A 1 3786 ? 85.980  83.609  23.197  1.00 60.35  ? 3786 GLU A CD    1 
ATOM   16599 O  OE1   . GLU A 1 3786 ? 85.796  82.707  24.040  1.00 66.18  ? 3786 GLU A OE1   1 
ATOM   16600 O  OE2   . GLU A 1 3786 ? 86.340  83.380  22.023  1.00 60.23  ? 3786 GLU A OE2   1 
ATOM   16601 N  N     . THR A 1 3787 ? 85.953  86.037  28.020  1.00 47.11  ? 3787 THR A N     1 
ATOM   16602 C  CA    . THR A 1 3787 ? 85.626  86.104  29.439  1.00 43.63  ? 3787 THR A CA    1 
ATOM   16603 C  C     . THR A 1 3787 ? 85.695  87.538  29.950  1.00 48.62  ? 3787 THR A C     1 
ATOM   16604 O  O     . THR A 1 3787 ? 84.925  87.923  30.834  1.00 53.22  ? 3787 THR A O     1 
ATOM   16605 C  CB    . THR A 1 3787 ? 86.558  85.193  30.238  1.00 44.02  ? 3787 THR A CB    1 
ATOM   16606 O  OG1   . THR A 1 3787 ? 87.922  85.545  29.973  1.00 47.62  ? 3787 THR A OG1   1 
ATOM   16607 C  CG2   . THR A 1 3787 ? 86.326  83.736  29.865  1.00 41.66  ? 3787 THR A CG2   1 
ATOM   16608 N  N     . ASP A 1 3788 ? 86.598  88.348  29.392  1.00 49.17  ? 3788 ASP A N     1 
ATOM   16609 C  CA    . ASP A 1 3788 ? 86.687  89.748  29.795  1.00 48.11  ? 3788 ASP A CA    1 
ATOM   16610 C  C     . ASP A 1 3788 ? 85.415  90.512  29.447  1.00 48.54  ? 3788 ASP A C     1 
ATOM   16611 O  O     . ASP A 1 3788 ? 84.920  91.312  30.248  1.00 53.02  ? 3788 ASP A O     1 
ATOM   16612 C  CB    . ASP A 1 3788 ? 87.907  90.406  29.148  1.00 51.25  ? 3788 ASP A CB    1 
ATOM   16613 C  CG    . ASP A 1 3788 ? 89.214  89.845  29.669  1.00 62.06  ? 3788 ASP A CG    1 
ATOM   16614 O  OD1   . ASP A 1 3788 ? 89.171  88.975  30.564  1.00 60.03  ? 3788 ASP A OD1   1 
ATOM   16615 O  OD2   . ASP A 1 3788 ? 90.283  90.270  29.183  1.00 72.47  ? 3788 ASP A OD2   1 
ATOM   16616 N  N     . ILE A 1 3789 ? 84.870  90.289  28.249  1.00 49.67  ? 3789 ILE A N     1 
ATOM   16617 C  CA    . ILE A 1 3789 ? 83.649  91.012  27.883  1.00 49.16  ? 3789 ILE A CA    1 
ATOM   16618 C  C     . ILE A 1 3789 ? 82.471  90.526  28.721  1.00 48.40  ? 3789 ILE A C     1 
ATOM   16619 O  O     . ILE A 1 3789 ? 81.587  91.312  29.101  1.00 48.94  ? 3789 ILE A O     1 
ATOM   16620 C  CB    . ILE A 1 3789 ? 83.359  90.909  26.372  1.00 52.17  ? 3789 ILE A CB    1 
ATOM   16621 C  CG1   . ILE A 1 3789 ? 82.834  89.525  25.984  1.00 49.35  ? 3789 ILE A CG1   1 
ATOM   16622 C  CG2   . ILE A 1 3789 ? 84.596  91.263  25.570  1.00 46.56  ? 3789 ILE A CG2   1 
ATOM   16623 C  CD1   . ILE A 1 3789 ? 82.705  89.317  24.498  1.00 54.18  ? 3789 ILE A CD1   1 
ATOM   16624 N  N     . VAL A 1 3790 ? 82.429  89.227  29.029  1.00 49.96  ? 3790 VAL A N     1 
ATOM   16625 C  CA    . VAL A 1 3790 ? 81.320  88.756  29.855  1.00 50.23  ? 3790 VAL A CA    1 
ATOM   16626 C  C     . VAL A 1 3790 ? 81.457  89.305  31.278  1.00 48.54  ? 3790 VAL A C     1 
ATOM   16627 O  O     . VAL A 1 3790 ? 80.458  89.602  31.948  1.00 44.97  ? 3790 VAL A O     1 
ATOM   16628 C  CB    . VAL A 1 3790 ? 81.223  87.221  29.815  1.00 48.40  ? 3790 VAL A CB    1 
ATOM   16629 C  CG1   . VAL A 1 3790 ? 79.973  86.759  30.549  1.00 49.66  ? 3790 VAL A CG1   1 
ATOM   16630 C  CG2   . VAL A 1 3790 ? 81.198  86.740  28.378  1.00 43.81  ? 3790 VAL A CG2   1 
ATOM   16631 N  N     . MET A 1 3791 ? 82.698  89.486  31.751  1.00 48.53  ? 3791 MET A N     1 
ATOM   16632 C  CA    . MET A 1 3791 ? 82.909  90.206  33.008  1.00 43.37  ? 3791 MET A CA    1 
ATOM   16633 C  C     . MET A 1 3791 ? 82.484  91.661  32.911  1.00 44.51  ? 3791 MET A C     1 
ATOM   16634 O  O     . MET A 1 3791 ? 82.052  92.246  33.904  1.00 47.84  ? 3791 MET A O     1 
ATOM   16635 C  CB    . MET A 1 3791 ? 84.367  90.132  33.459  1.00 46.04  ? 3791 MET A CB    1 
ATOM   16636 C  CG    . MET A 1 3791 ? 84.850  88.771  33.852  1.00 52.97  ? 3791 MET A CG    1 
ATOM   16637 S  SD    . MET A 1 3791 ? 83.845  88.238  35.248  1.00 64.34  ? 3791 MET A SD    1 
ATOM   16638 C  CE    . MET A 1 3791 ? 84.413  89.372  36.515  1.00 56.88  ? 3791 MET A CE    1 
ATOM   16639 N  N     . GLN A 1 3792 ? 82.644  92.279  31.745  1.00 45.75  ? 3792 GLN A N     1 
ATOM   16640 C  CA    . GLN A 1 3792 ? 82.145  93.642  31.588  1.00 47.71  ? 3792 GLN A CA    1 
ATOM   16641 C  C     . GLN A 1 3792 ? 80.629  93.683  31.754  1.00 46.18  ? 3792 GLN A C     1 
ATOM   16642 O  O     . GLN A 1 3792 ? 80.086  94.583  32.412  1.00 42.52  ? 3792 GLN A O     1 
ATOM   16643 C  CB    . GLN A 1 3792 ? 82.580  94.203  30.235  1.00 46.98  ? 3792 GLN A CB    1 
ATOM   16644 C  CG    . GLN A 1 3792 ? 84.078  94.451  30.158  1.00 52.36  ? 3792 GLN A CG    1 
ATOM   16645 C  CD    . GLN A 1 3792 ? 84.549  94.863  28.778  1.00 60.91  ? 3792 GLN A CD    1 
ATOM   16646 O  OE1   . GLN A 1 3792 ? 83.749  95.233  27.918  1.00 63.33  ? 3792 GLN A OE1   1 
ATOM   16647 N  NE2   . GLN A 1 3792 ? 85.859  94.803  28.560  1.00 57.71  ? 3792 GLN A NE2   1 
ATOM   16648 N  N     . GLU A 1 3793 ? 79.935  92.694  31.188  1.00 48.98  ? 3793 GLU A N     1 
ATOM   16649 C  CA    . GLU A 1 3793 ? 78.491  92.586  31.399  1.00 45.94  ? 3793 GLU A CA    1 
ATOM   16650 C  C     . GLU A 1 3793 ? 78.157  92.398  32.879  1.00 43.78  ? 3793 GLU A C     1 
ATOM   16651 O  O     . GLU A 1 3793 ? 77.268  93.069  33.423  1.00 44.86  ? 3793 GLU A O     1 
ATOM   16652 C  CB    . GLU A 1 3793 ? 77.921  91.433  30.572  1.00 49.57  ? 3793 GLU A CB    1 
ATOM   16653 C  CG    . GLU A 1 3793 ? 77.828  91.714  29.083  1.00 56.92  ? 3793 GLU A CG    1 
ATOM   16654 C  CD    . GLU A 1 3793 ? 77.864  90.450  28.247  1.00 67.37  ? 3793 GLU A CD    1 
ATOM   16655 O  OE1   . GLU A 1 3793 ? 76.988  89.578  28.438  1.00 72.07  ? 3793 GLU A OE1   1 
ATOM   16656 O  OE2   . GLU A 1 3793 ? 78.770  90.329  27.398  1.00 60.30  ? 3793 GLU A OE2   1 
ATOM   16657 N  N     . VAL A 1 3794 ? 78.874  91.494  33.550  1.00 47.80  ? 3794 VAL A N     1 
ATOM   16658 C  CA    . VAL A 1 3794 ? 78.621  91.243  34.969  1.00 43.18  ? 3794 VAL A CA    1 
ATOM   16659 C  C     . VAL A 1 3794 ? 78.876  92.504  35.788  1.00 43.39  ? 3794 VAL A C     1 
ATOM   16660 O  O     . VAL A 1 3794 ? 78.133  92.822  36.724  1.00 44.37  ? 3794 VAL A O     1 
ATOM   16661 C  CB    . VAL A 1 3794 ? 79.477  90.065  35.467  1.00 42.68  ? 3794 VAL A CB    1 
ATOM   16662 C  CG1   . VAL A 1 3794 ? 79.321  89.887  36.971  1.00 34.12  ? 3794 VAL A CG1   1 
ATOM   16663 C  CG2   . VAL A 1 3794 ? 79.091  88.789  34.742  1.00 42.09  ? 3794 VAL A CG2   1 
ATOM   16664 N  N     . GLU A 1 3795 ? 79.940  93.233  35.452  1.00 45.03  ? 3795 GLU A N     1 
ATOM   16665 C  CA    . GLU A 1 3795 ? 80.314  94.431  36.194  1.00 41.82  ? 3795 GLU A CA    1 
ATOM   16666 C  C     . GLU A 1 3795 ? 79.271  95.528  36.028  1.00 40.64  ? 3795 GLU A C     1 
ATOM   16667 O  O     . GLU A 1 3795 ? 78.908  96.207  36.996  1.00 42.45  ? 3795 GLU A O     1 
ATOM   16668 C  CB    . GLU A 1 3795 ? 81.689  94.911  35.723  1.00 45.18  ? 3795 GLU A CB    1 
ATOM   16669 C  CG    . GLU A 1 3795 ? 82.238  96.131  36.445  1.00 53.01  ? 3795 GLU A CG    1 
ATOM   16670 C  CD    . GLU A 1 3795 ? 82.534  95.867  37.908  1.00 61.70  ? 3795 GLU A CD    1 
ATOM   16671 O  OE1   . GLU A 1 3795 ? 82.793  94.699  38.267  1.00 62.80  ? 3795 GLU A OE1   1 
ATOM   16672 O  OE2   . GLU A 1 3795 ? 82.514  96.832  38.701  1.00 67.96  ? 3795 GLU A OE2   1 
ATOM   16673 N  N     . THR A 1 3796 ? 78.776  95.725  34.801  1.00 42.62  ? 3796 THR A N     1 
ATOM   16674 C  CA    . THR A 1 3796 ? 77.758  96.752  34.608  1.00 38.85  ? 3796 THR A CA    1 
ATOM   16675 C  C     . THR A 1 3796 ? 76.431  96.340  35.232  1.00 42.85  ? 3796 THR A C     1 
ATOM   16676 O  O     . THR A 1 3796 ? 75.615  97.204  35.576  1.00 42.89  ? 3796 THR A O     1 
ATOM   16677 C  CB    . THR A 1 3796 ? 77.584  97.084  33.122  1.00 38.05  ? 3796 THR A CB    1 
ATOM   16678 O  OG1   . THR A 1 3796 ? 76.708  98.211  32.985  1.00 41.65  ? 3796 THR A OG1   1 
ATOM   16679 C  CG2   . THR A 1 3796 ? 76.993  95.916  32.361  1.00 39.33  ? 3796 THR A CG2   1 
ATOM   16680 N  N     . VAL A 1 3797 ? 76.191  95.035  35.390  1.00 43.36  ? 3797 VAL A N     1 
ATOM   16681 C  CA    . VAL A 1 3797 ? 75.018  94.607  36.148  1.00 36.82  ? 3797 VAL A CA    1 
ATOM   16682 C  C     . VAL A 1 3797 ? 75.196  94.885  37.640  1.00 37.18  ? 3797 VAL A C     1 
ATOM   16683 O  O     . VAL A 1 3797 ? 74.281  95.386  38.303  1.00 36.34  ? 3797 VAL A O     1 
ATOM   16684 C  CB    . VAL A 1 3797 ? 74.717  93.121  35.881  1.00 45.43  ? 3797 VAL A CB    1 
ATOM   16685 C  CG1   . VAL A 1 3797 ? 73.646  92.619  36.835  1.00 36.01  ? 3797 VAL A CG1   1 
ATOM   16686 C  CG2   . VAL A 1 3797 ? 74.272  92.925  34.443  1.00 45.31  ? 3797 VAL A CG2   1 
ATOM   16687 N  N     . SER A 1 3798 ? 76.371  94.572  38.189  1.00 41.27  ? 3798 SER A N     1 
ATOM   16688 C  CA    . SER A 1 3798 ? 76.609  94.673  39.625  1.00 36.96  ? 3798 SER A CA    1 
ATOM   16689 C  C     . SER A 1 3798 ? 76.948  96.086  40.085  1.00 31.78  ? 3798 SER A C     1 
ATOM   16690 O  O     . SER A 1 3798 ? 77.052  96.314  41.295  1.00 30.00  ? 3798 SER A O     1 
ATOM   16691 C  CB    . SER A 1 3798 ? 77.733  93.720  40.039  1.00 34.91  ? 3798 SER A CB    1 
ATOM   16692 O  OG    . SER A 1 3798 ? 79.004  94.324  39.875  1.00 39.58  ? 3798 SER A OG    1 
ATOM   16693 N  N     . GLN A 1 3799 ? 77.136  97.025  39.155  1.00 36.40  ? 3799 GLN A N     1 
ATOM   16694 C  CA    . GLN A 1 3799 ? 77.381  98.417  39.528  1.00 34.67  ? 3799 GLN A CA    1 
ATOM   16695 C  C     . GLN A 1 3799 ? 76.255  98.990  40.383  1.00 30.39  ? 3799 GLN A C     1 
ATOM   16696 O  O     . GLN A 1 3799 ? 76.483  99.922  41.163  1.00 30.50  ? 3799 GLN A O     1 
ATOM   16697 C  CB    . GLN A 1 3799 ? 77.570  99.254  38.260  1.00 40.46  ? 3799 GLN A CB    1 
ATOM   16698 C  CG    . GLN A 1 3799 ? 77.909  100.721 38.480  1.00 51.30  ? 3799 GLN A CG    1 
ATOM   16699 C  CD    . GLN A 1 3799 ? 79.269  100.928 39.112  1.00 58.99  ? 3799 GLN A CD    1 
ATOM   16700 O  OE1   . GLN A 1 3799 ? 79.438  101.776 39.988  1.00 56.74  ? 3799 GLN A OE1   1 
ATOM   16701 N  NE2   . GLN A 1 3799 ? 80.244  100.135 38.685  1.00 54.70  ? 3799 GLN A NE2   1 
ATOM   16702 N  N     . GLN A 1 3800 ? 75.044  98.441  40.264  1.00 31.72  ? 3800 GLN A N     1 
ATOM   16703 C  CA    . GLN A 1 3800 ? 73.889  99.028  40.934  1.00 25.40  ? 3800 GLN A CA    1 
ATOM   16704 C  C     . GLN A 1 3800 ? 73.893  98.765  42.437  1.00 24.64  ? 3800 GLN A C     1 
ATOM   16705 O  O     . GLN A 1 3800 ? 73.290  99.531  43.197  1.00 26.50  ? 3800 GLN A O     1 
ATOM   16706 C  CB    . GLN A 1 3800 ? 72.604  98.490  40.303  1.00 27.73  ? 3800 GLN A CB    1 
ATOM   16707 C  CG    . GLN A 1 3800 ? 71.365  99.316  40.590  1.00 32.62  ? 3800 GLN A CG    1 
ATOM   16708 C  CD    . GLN A 1 3800 ? 70.092  98.606  40.178  1.00 37.50  ? 3800 GLN A CD    1 
ATOM   16709 O  OE1   . GLN A 1 3800 ? 70.112  97.426  39.826  1.00 39.48  ? 3800 GLN A OE1   1 
ATOM   16710 N  NE2   . GLN A 1 3800 ? 68.975  99.322  40.218  1.00 36.62  ? 3800 GLN A NE2   1 
ATOM   16711 N  N     . TYR A 1 3801 ? 74.557  97.702  42.886  1.00 22.27  ? 3801 TYR A N     1 
ATOM   16712 C  CA    . TYR A 1 3801 ? 74.504  97.293  44.285  1.00 13.95  ? 3801 TYR A CA    1 
ATOM   16713 C  C     . TYR A 1 3801 ? 75.701  97.756  45.109  1.00 16.52  ? 3801 TYR A C     1 
ATOM   16714 O  O     . TYR A 1 3801 ? 75.801  97.381  46.282  1.00 17.41  ? 3801 TYR A O     1 
ATOM   16715 C  CB    . TYR A 1 3801 ? 74.375  95.769  44.383  1.00 16.17  ? 3801 TYR A CB    1 
ATOM   16716 C  CG    . TYR A 1 3801 ? 73.147  95.209  43.701  1.00 19.50  ? 3801 TYR A CG    1 
ATOM   16717 C  CD1   . TYR A 1 3801 ? 71.944  95.096  44.385  1.00 20.61  ? 3801 TYR A CD1   1 
ATOM   16718 C  CD2   . TYR A 1 3801 ? 73.188  94.795  42.377  1.00 21.56  ? 3801 TYR A CD2   1 
ATOM   16719 C  CE1   . TYR A 1 3801 ? 70.817  94.586  43.771  1.00 22.20  ? 3801 TYR A CE1   1 
ATOM   16720 C  CE2   . TYR A 1 3801 ? 72.066  94.284  41.753  1.00 25.88  ? 3801 TYR A CE2   1 
ATOM   16721 C  CZ    . TYR A 1 3801 ? 70.883  94.182  42.455  1.00 29.92  ? 3801 TYR A CZ    1 
ATOM   16722 O  OH    . TYR A 1 3801 ? 69.763  93.674  41.840  1.00 30.75  ? 3801 TYR A OH    1 
ATOM   16723 N  N     . LEU A 1 3802 ? 76.608  98.546  44.535  1.00 17.88  ? 3802 LEU A N     1 
ATOM   16724 C  CA    . LEU A 1 3802 ? 77.742  99.052  45.308  1.00 16.98  ? 3802 LEU A CA    1 
ATOM   16725 C  C     . LEU A 1 3802 ? 77.334  99.931  46.486  1.00 13.53  ? 3802 LEU A C     1 
ATOM   16726 O  O     . LEU A 1 3802 ? 77.920  99.771  47.573  1.00 13.75  ? 3802 LEU A O     1 
ATOM   16727 C  CB    . LEU A 1 3802 ? 78.718  99.785  44.382  1.00 19.19  ? 3802 LEU A CB    1 
ATOM   16728 C  CG    . LEU A 1 3802 ? 79.345  98.945  43.270  1.00 30.19  ? 3802 LEU A CG    1 
ATOM   16729 C  CD1   . LEU A 1 3802 ? 80.202  99.812  42.368  1.00 30.60  ? 3802 LEU A CD1   1 
ATOM   16730 C  CD2   . LEU A 1 3802 ? 80.167  97.815  43.863  1.00 24.52  ? 3802 LEU A CD2   1 
ATOM   16731 N  N     . PRO A 1 3803 ? 76.397  100.881 46.356  1.00 16.54  ? 3803 PRO A N     1 
ATOM   16732 C  CA    . PRO A 1 3803 ? 76.033  101.692 47.531  1.00 12.53  ? 3803 PRO A CA    1 
ATOM   16733 C  C     . PRO A 1 3803 ? 75.526  100.873 48.704  1.00 11.27  ? 3803 PRO A C     1 
ATOM   16734 O  O     . PRO A 1 3803 ? 75.805  101.226 49.857  1.00 13.36  ? 3803 PRO A O     1 
ATOM   16735 C  CB    . PRO A 1 3803 ? 74.947  102.629 46.983  1.00 12.18  ? 3803 PRO A CB    1 
ATOM   16736 C  CG    . PRO A 1 3803 ? 75.253  102.732 45.536  1.00 11.35  ? 3803 PRO A CG    1 
ATOM   16737 C  CD    . PRO A 1 3803 ? 75.695  101.355 45.148  1.00 14.55  ? 3803 PRO A CD    1 
ATOM   16738 N  N     . LEU A 1 3804 ? 74.798  99.784  48.450  1.00 11.18  ? 3804 LEU A N     1 
ATOM   16739 C  CA    . LEU A 1 3804 ? 74.340  98.940  49.548  1.00 11.63  ? 3804 LEU A CA    1 
ATOM   16740 C  C     . LEU A 1 3804 ? 75.512  98.283  50.267  1.00 10.43  ? 3804 LEU A C     1 
ATOM   16741 O  O     . LEU A 1 3804 ? 75.519  98.198  51.499  1.00 11.35  ? 3804 LEU A O     1 
ATOM   16742 C  CB    . LEU A 1 3804 ? 73.362  97.885  49.033  1.00 12.08  ? 3804 LEU A CB    1 
ATOM   16743 C  CG    . LEU A 1 3804 ? 72.850  96.913  50.096  1.00 12.10  ? 3804 LEU A CG    1 
ATOM   16744 C  CD1   . LEU A 1 3804 ? 71.934  97.632  51.074  1.00 10.76  ? 3804 LEU A CD1   1 
ATOM   16745 C  CD2   . LEU A 1 3804 ? 72.135  95.740  49.454  1.00 11.34  ? 3804 LEU A CD2   1 
ATOM   16746 N  N     . SER A 1 3805 ? 76.515  97.816  49.519  1.00 9.35   ? 3805 SER A N     1 
ATOM   16747 C  CA    . SER A 1 3805 ? 77.692  97.222  50.148  1.00 9.59   ? 3805 SER A CA    1 
ATOM   16748 C  C     . SER A 1 3805 ? 78.481  98.261  50.938  1.00 9.26   ? 3805 SER A C     1 
ATOM   16749 O  O     . SER A 1 3805 ? 79.006  97.964  52.020  1.00 8.99   ? 3805 SER A O     1 
ATOM   16750 C  CB    . SER A 1 3805 ? 78.577  96.563  49.090  1.00 10.60  ? 3805 SER A CB    1 
ATOM   16751 O  OG    . SER A 1 3805 ? 79.094  97.524  48.186  1.00 12.64  ? 3805 SER A OG    1 
ATOM   16752 N  N     . THR A 1 3806 ? 78.583  99.483  50.408  1.00 7.01   ? 3806 THR A N     1 
ATOM   16753 C  CA    . THR A 1 3806 ? 79.252  100.551 51.145  1.00 9.30   ? 3806 THR A CA    1 
ATOM   16754 C  C     . THR A 1 3806 ? 78.521  100.858 52.447  1.00 10.15  ? 3806 THR A C     1 
ATOM   16755 O  O     . THR A 1 3806 ? 79.151  101.027 53.500  1.00 10.65  ? 3806 THR A O     1 
ATOM   16756 C  CB    . THR A 1 3806 ? 79.350  101.806 50.278  1.00 11.89  ? 3806 THR A CB    1 
ATOM   16757 O  OG1   . THR A 1 3806 ? 79.958  101.477 49.023  1.00 15.61  ? 3806 THR A OG1   1 
ATOM   16758 C  CG2   . THR A 1 3806 ? 80.183  102.871 50.974  1.00 9.87   ? 3806 THR A CG2   1 
ATOM   16759 N  N     . ALA A 1 3807 ? 77.189  100.928 52.393  1.00 6.70   ? 3807 ALA A N     1 
ATOM   16760 C  CA    . ALA A 1 3807 ? 76.406  101.138 53.605  1.00 8.39   ? 3807 ALA A CA    1 
ATOM   16761 C  C     . ALA A 1 3807 ? 76.589  99.986  54.583  1.00 8.28   ? 3807 ALA A C     1 
ATOM   16762 O  O     . ALA A 1 3807 ? 76.661  100.199 55.797  1.00 9.16   ? 3807 ALA A O     1 
ATOM   16763 C  CB    . ALA A 1 3807 ? 74.929  101.318 53.253  1.00 9.56   ? 3807 ALA A CB    1 
ATOM   16764 N  N     . CYS A 1 3808 ? 76.663  98.756  54.070  1.00 6.34   ? 3808 CYS A N     1 
ATOM   16765 C  CA    . CYS A 1 3808 ? 76.886  97.597  54.927  1.00 7.03   ? 3808 CYS A CA    1 
ATOM   16766 C  C     . CYS A 1 3808 ? 78.211  97.712  55.670  1.00 7.90   ? 3808 CYS A C     1 
ATOM   16767 O  O     . CYS A 1 3808 ? 78.279  97.499  56.888  1.00 10.24  ? 3808 CYS A O     1 
ATOM   16768 C  CB    . CYS A 1 3808 ? 76.854  96.320  54.087  1.00 5.32   ? 3808 CYS A CB    1 
ATOM   16769 S  SG    . CYS A 1 3808 ? 75.211  95.726  53.640  1.00 14.13  ? 3808 CYS A SG    1 
ATOM   16770 N  N     . SER A 1 3809 ? 79.279  98.054  54.945  1.00 7.83   ? 3809 SER A N     1 
ATOM   16771 C  CA    . SER A 1 3809 ? 80.588  98.185  55.578  1.00 9.01   ? 3809 SER A CA    1 
ATOM   16772 C  C     . SER A 1 3809 ? 80.595  99.315  56.600  1.00 7.93   ? 3809 SER A C     1 
ATOM   16773 O  O     . SER A 1 3809 ? 81.151  99.168  57.697  1.00 8.08   ? 3809 SER A O     1 
ATOM   16774 C  CB    . SER A 1 3809 ? 81.668  98.410  54.519  1.00 8.73   ? 3809 SER A CB    1 
ATOM   16775 O  OG    . SER A 1 3809 ? 81.498  99.656  53.867  1.00 14.37  ? 3809 SER A OG    1 
ATOM   16776 N  N     . SER A 1 3810 ? 79.974  100.449 56.261  1.00 6.93   ? 3810 SER A N     1 
ATOM   16777 C  CA    . SER A 1 3810 ? 79.921  101.567 57.198  1.00 8.07   ? 3810 SER A CA    1 
ATOM   16778 C  C     . SER A 1 3810 ? 79.154  101.195 58.462  1.00 7.92   ? 3810 SER A C     1 
ATOM   16779 O  O     . SER A 1 3810 ? 79.578  101.531 59.574  1.00 9.15   ? 3810 SER A O     1 
ATOM   16780 C  CB    . SER A 1 3810 ? 79.290  102.787 56.525  1.00 9.27   ? 3810 SER A CB    1 
ATOM   16781 O  OG    . SER A 1 3810 ? 79.870  103.029 55.256  1.00 14.76  ? 3810 SER A OG    1 
ATOM   16782 N  N     . ILE A 1 3811 ? 78.028  100.495 58.311  1.00 6.05   ? 3811 ILE A N     1 
ATOM   16783 C  CA    . ILE A 1 3811 ? 77.230  100.097 59.468  1.00 6.27   ? 3811 ILE A CA    1 
ATOM   16784 C  C     . ILE A 1 3811 ? 78.016  99.133  60.347  1.00 7.22   ? 3811 ILE A C     1 
ATOM   16785 O  O     . ILE A 1 3811 ? 78.028  99.256  61.578  1.00 9.77   ? 3811 ILE A O     1 
ATOM   16786 C  CB    . ILE A 1 3811 ? 75.894  99.483  59.011  1.00 6.22   ? 3811 ILE A CB    1 
ATOM   16787 C  CG1   . ILE A 1 3811 ? 74.971  100.571 58.460  1.00 6.67   ? 3811 ILE A CG1   1 
ATOM   16788 C  CG2   . ILE A 1 3811 ? 75.221  98.742  60.158  1.00 7.55   ? 3811 ILE A CG2   1 
ATOM   16789 C  CD1   . ILE A 1 3811 ? 73.697  100.037 57.849  1.00 4.80   ? 3811 ILE A CD1   1 
ATOM   16790 N  N     . TYR A 1 3812 ? 78.686  98.158  59.728  1.00 7.70   ? 3812 TYR A N     1 
ATOM   16791 C  CA    . TYR A 1 3812 ? 79.462  97.201  60.509  1.00 7.17   ? 3812 TYR A CA    1 
ATOM   16792 C  C     . TYR A 1 3812 ? 80.592  97.884  61.267  1.00 8.14   ? 3812 TYR A C     1 
ATOM   16793 O  O     . TYR A 1 3812 ? 80.842  97.572  62.438  1.00 10.21  ? 3812 TYR A O     1 
ATOM   16794 C  CB    . TYR A 1 3812 ? 80.025  96.107  59.609  1.00 7.98   ? 3812 TYR A CB    1 
ATOM   16795 C  CG    . TYR A 1 3812 ? 81.018  95.229  60.326  1.00 11.29  ? 3812 TYR A CG    1 
ATOM   16796 C  CD1   . TYR A 1 3812 ? 80.593  94.265  61.226  1.00 11.06  ? 3812 TYR A CD1   1 
ATOM   16797 C  CD2   . TYR A 1 3812 ? 82.384  95.384  60.127  1.00 9.03   ? 3812 TYR A CD2   1 
ATOM   16798 C  CE1   . TYR A 1 3812 ? 81.497  93.473  61.895  1.00 10.92  ? 3812 TYR A CE1   1 
ATOM   16799 C  CE2   . TYR A 1 3812 ? 83.294  94.591  60.786  1.00 9.70   ? 3812 TYR A CE2   1 
ATOM   16800 C  CZ    . TYR A 1 3812 ? 82.846  93.635  61.669  1.00 11.96  ? 3812 TYR A CZ    1 
ATOM   16801 O  OH    . TYR A 1 3812 ? 83.752  92.840  62.332  1.00 14.31  ? 3812 TYR A OH    1 
ATOM   16802 N  N     . PHE A 1 3813 ? 81.300  98.808  60.616  1.00 7.54   ? 3813 PHE A N     1 
ATOM   16803 C  CA    . PHE A 1 3813 ? 82.394  99.480  61.306  1.00 9.03   ? 3813 PHE A CA    1 
ATOM   16804 C  C     . PHE A 1 3813 ? 81.892  100.435 62.383  1.00 11.34  ? 3813 PHE A C     1 
ATOM   16805 O  O     . PHE A 1 3813 ? 82.571  100.612 63.401  1.00 13.23  ? 3813 PHE A O     1 
ATOM   16806 C  CB    . PHE A 1 3813 ? 83.288  100.195 60.294  1.00 10.63  ? 3813 PHE A CB    1 
ATOM   16807 C  CG    . PHE A 1 3813 ? 84.342  99.303  59.700  1.00 12.79  ? 3813 PHE A CG    1 
ATOM   16808 C  CD1   . PHE A 1 3813 ? 84.069  98.538  58.578  1.00 13.82  ? 3813 PHE A CD1   1 
ATOM   16809 C  CD2   . PHE A 1 3813 ? 85.597  99.212  60.277  1.00 19.83  ? 3813 PHE A CD2   1 
ATOM   16810 C  CE1   . PHE A 1 3813 ? 85.030  97.706  58.038  1.00 12.39  ? 3813 PHE A CE1   1 
ATOM   16811 C  CE2   . PHE A 1 3813 ? 86.565  98.384  59.739  1.00 24.06  ? 3813 PHE A CE2   1 
ATOM   16812 C  CZ    . PHE A 1 3813 ? 86.281  97.630  58.617  1.00 16.84  ? 3813 PHE A CZ    1 
ATOM   16813 N  N     . THR A 1 3814 ? 80.706  101.022 62.205  1.00 9.48   ? 3814 THR A N     1 
ATOM   16814 C  CA    . THR A 1 3814 ? 80.090  101.779 63.290  1.00 9.53   ? 3814 THR A CA    1 
ATOM   16815 C  C     . THR A 1 3814 ? 79.768  100.876 64.477  1.00 7.83   ? 3814 THR A C     1 
ATOM   16816 O  O     . THR A 1 3814 ? 80.011  101.246 65.634  1.00 10.18  ? 3814 THR A O     1 
ATOM   16817 C  CB    . THR A 1 3814 ? 78.829  102.481 62.785  1.00 9.98   ? 3814 THR A CB    1 
ATOM   16818 O  OG1   . THR A 1 3814 ? 79.189  103.476 61.819  1.00 11.98  ? 3814 THR A OG1   1 
ATOM   16819 C  CG2   . THR A 1 3814 ? 78.082  103.141 63.931  1.00 7.78   ? 3814 THR A CG2   1 
ATOM   16820 N  N     . MET A 1 3815 ? 79.232  99.683  64.210  1.00 7.11   ? 3815 MET A N     1 
ATOM   16821 C  CA    . MET A 1 3815 ? 78.953  98.746  65.295  1.00 9.58   ? 3815 MET A CA    1 
ATOM   16822 C  C     . MET A 1 3815 ? 80.233  98.335  66.013  1.00 9.32   ? 3815 MET A C     1 
ATOM   16823 O  O     . MET A 1 3815 ? 80.245  98.193  67.241  1.00 11.37  ? 3815 MET A O     1 
ATOM   16824 C  CB    . MET A 1 3815 ? 78.206  97.519  64.767  1.00 8.08   ? 3815 MET A CB    1 
ATOM   16825 C  CG    . MET A 1 3815 ? 76.879  97.838  64.093  1.00 6.89   ? 3815 MET A CG    1 
ATOM   16826 S  SD    . MET A 1 3815 ? 76.101  96.412  63.309  1.00 19.35  ? 3815 MET A SD    1 
ATOM   16827 C  CE    . MET A 1 3815 ? 76.496  95.118  64.481  1.00 7.07   ? 3815 MET A CE    1 
ATOM   16828 N  N     . GLU A 1 3816 ? 81.317  98.127  65.264  1.00 9.82   ? 3816 GLU A N     1 
ATOM   16829 C  CA    . GLU A 1 3816 ? 82.597  97.822  65.898  1.00 9.62   ? 3816 GLU A CA    1 
ATOM   16830 C  C     . GLU A 1 3816 ? 83.101  98.986  66.746  1.00 10.62  ? 3816 GLU A C     1 
ATOM   16831 O  O     . GLU A 1 3816 ? 83.609  98.767  67.852  1.00 14.41  ? 3816 GLU A O     1 
ATOM   16832 C  CB    . GLU A 1 3816 ? 83.638  97.441  64.845  1.00 12.51  ? 3816 GLU A CB    1 
ATOM   16833 C  CG    . GLU A 1 3816 ? 83.343  96.141  64.107  1.00 16.19  ? 3816 GLU A CG    1 
ATOM   16834 C  CD    . GLU A 1 3816 ? 83.420  94.912  64.999  1.00 29.78  ? 3816 GLU A CD    1 
ATOM   16835 O  OE1   . GLU A 1 3816 ? 84.226  94.908  65.954  1.00 36.18  ? 3816 GLU A OE1   1 
ATOM   16836 O  OE2   . GLU A 1 3816 ? 82.678  93.944  64.736  1.00 26.58  ? 3816 GLU A OE2   1 
ATOM   16837 N  N     . SER A 1 3817 ? 82.967  100.221 66.258  1.00 10.86  ? 3817 SER A N     1 
ATOM   16838 C  CA    . SER A 1 3817 ? 83.379  101.386 67.033  1.00 10.76  ? 3817 SER A CA    1 
ATOM   16839 C  C     . SER A 1 3817 ? 82.483  101.638 68.238  1.00 10.90  ? 3817 SER A C     1 
ATOM   16840 O  O     . SER A 1 3817 ? 82.880  102.386 69.138  1.00 13.87  ? 3817 SER A O     1 
ATOM   16841 C  CB    . SER A 1 3817 ? 83.404  102.636 66.148  1.00 12.51  ? 3817 SER A CB    1 
ATOM   16842 O  OG    . SER A 1 3817 ? 82.127  103.247 66.083  1.00 18.82  ? 3817 SER A OG    1 
ATOM   16843 N  N     . LEU A 1 3818 ? 81.290  101.040 68.268  1.00 10.24  ? 3818 LEU A N     1 
ATOM   16844 C  CA    . LEU A 1 3818 ? 80.397  101.205 69.411  1.00 9.62   ? 3818 LEU A CA    1 
ATOM   16845 C  C     . LEU A 1 3818 ? 80.994  100.688 70.715  1.00 11.24  ? 3818 LEU A C     1 
ATOM   16846 O  O     . LEU A 1 3818 ? 80.516  101.069 71.788  1.00 10.57  ? 3818 LEU A O     1 
ATOM   16847 C  CB    . LEU A 1 3818 ? 79.063  100.502 69.153  1.00 8.03   ? 3818 LEU A CB    1 
ATOM   16848 C  CG    . LEU A 1 3818 ? 78.027  101.259 68.322  1.00 9.19   ? 3818 LEU A CG    1 
ATOM   16849 C  CD1   . LEU A 1 3818 ? 76.941  100.316 67.834  1.00 4.74   ? 3818 LEU A CD1   1 
ATOM   16850 C  CD2   . LEU A 1 3818 ? 77.425  102.397 69.128  1.00 9.25   ? 3818 LEU A CD2   1 
ATOM   16851 N  N     . LYS A 1 3819 ? 82.015  99.828  70.657  1.00 11.46  ? 3819 LYS A N     1 
ATOM   16852 C  CA    . LYS A 1 3819 ? 82.640  99.349  71.885  1.00 10.34  ? 3819 LYS A CA    1 
ATOM   16853 C  C     . LYS A 1 3819 ? 83.388  100.452 72.623  1.00 13.23  ? 3819 LYS A C     1 
ATOM   16854 O  O     . LYS A 1 3819 ? 83.691  100.291 73.810  1.00 12.92  ? 3819 LYS A O     1 
ATOM   16855 C  CB    . LYS A 1 3819 ? 83.602  98.197  71.587  1.00 10.28  ? 3819 LYS A CB    1 
ATOM   16856 C  CG    . LYS A 1 3819 ? 84.886  98.622  70.894  1.00 10.49  ? 3819 LYS A CG    1 
ATOM   16857 C  CD    . LYS A 1 3819 ? 85.944  97.534  70.975  1.00 8.99   ? 3819 LYS A CD    1 
ATOM   16858 C  CE    . LYS A 1 3819 ? 85.615  96.368  70.061  1.00 12.38  ? 3819 LYS A CE    1 
ATOM   16859 N  NZ    . LYS A 1 3819 ? 85.717  96.748  68.626  1.00 13.73  ? 3819 LYS A NZ    1 
ATOM   16860 N  N     . GLN A 1 3820 ? 83.695  101.563 71.949  1.00 15.28  ? 3820 GLN A N     1 
ATOM   16861 C  CA    . GLN A 1 3820 ? 84.420  102.654 72.587  1.00 14.74  ? 3820 GLN A CA    1 
ATOM   16862 C  C     . GLN A 1 3820 ? 83.574  103.402 73.609  1.00 13.97  ? 3820 GLN A C     1 
ATOM   16863 O  O     . GLN A 1 3820 ? 84.133  104.019 74.522  1.00 26.90  ? 3820 GLN A O     1 
ATOM   16864 C  CB    . GLN A 1 3820 ? 84.934  103.634 71.530  1.00 16.64  ? 3820 GLN A CB    1 
ATOM   16865 C  CG    . GLN A 1 3820 ? 85.847  103.009 70.489  1.00 17.10  ? 3820 GLN A CG    1 
ATOM   16866 C  CD    . GLN A 1 3820 ? 87.028  102.291 71.109  1.00 27.57  ? 3820 GLN A CD    1 
ATOM   16867 O  OE1   . GLN A 1 3820 ? 87.287  101.125 70.813  1.00 31.96  ? 3820 GLN A OE1   1 
ATOM   16868 N  NE2   . GLN A 1 3820 ? 87.755  102.987 71.976  1.00 30.55  ? 3820 GLN A NE2   1 
ATOM   16869 N  N     . ILE A 1 3821 ? 82.249  103.362 73.484  1.00 12.97  ? 3821 ILE A N     1 
ATOM   16870 C  CA    . ILE A 1 3821 ? 81.382  104.111 74.385  1.00 16.02  ? 3821 ILE A CA    1 
ATOM   16871 C  C     . ILE A 1 3821 ? 80.864  103.268 75.547  1.00 14.38  ? 3821 ILE A C     1 
ATOM   16872 O  O     . ILE A 1 3821 ? 80.449  103.836 76.569  1.00 18.49  ? 3821 ILE A O     1 
ATOM   16873 C  CB    . ILE A 1 3821 ? 80.203  104.741 73.615  1.00 14.04  ? 3821 ILE A CB    1 
ATOM   16874 C  CG1   . ILE A 1 3821 ? 79.221  103.665 73.153  1.00 13.40  ? 3821 ILE A CG1   1 
ATOM   16875 C  CG2   . ILE A 1 3821 ? 80.716  105.526 72.422  1.00 14.07  ? 3821 ILE A CG2   1 
ATOM   16876 C  CD1   . ILE A 1 3821 ? 77.931  104.222 72.594  1.00 13.04  ? 3821 ILE A CD1   1 
ATOM   16877 N  N     . HIS A 1 3822 ? 80.873  101.943 75.426  1.00 11.10  ? 3822 HIS A N     1 
ATOM   16878 C  CA    . HIS A 1 3822 ? 80.471  101.070 76.519  1.00 9.23   ? 3822 HIS A CA    1 
ATOM   16879 C  C     . HIS A 1 3822 ? 81.103  99.703  76.305  1.00 10.07  ? 3822 HIS A C     1 
ATOM   16880 O  O     . HIS A 1 3822 ? 81.153  99.209  75.177  1.00 13.68  ? 3822 HIS A O     1 
ATOM   16881 C  CB    . HIS A 1 3822 ? 78.946  100.945 76.612  1.00 8.98   ? 3822 HIS A CB    1 
ATOM   16882 C  CG    . HIS A 1 3822 ? 78.453  100.576 77.977  1.00 9.68   ? 3822 HIS A CG    1 
ATOM   16883 N  ND1   . HIS A 1 3822 ? 78.590  99.309  78.501  1.00 9.46   ? 3822 HIS A ND1   1 
ATOM   16884 C  CD2   . HIS A 1 3822 ? 77.822  101.309 78.925  1.00 12.16  ? 3822 HIS A CD2   1 
ATOM   16885 C  CE1   . HIS A 1 3822 ? 78.068  99.277  79.713  1.00 11.22  ? 3822 HIS A CE1   1 
ATOM   16886 N  NE2   . HIS A 1 3822 ? 77.594  100.477 79.994  1.00 14.97  ? 3822 HIS A NE2   1 
ATOM   16887 N  N     . PHE A 1 3823 ? 81.583  99.102  77.396  1.00 9.87   ? 3823 PHE A N     1 
ATOM   16888 C  CA    . PHE A 1 3823 ? 82.219  97.793  77.309  1.00 8.67   ? 3823 PHE A CA    1 
ATOM   16889 C  C     . PHE A 1 3823 ? 81.246  96.700  76.887  1.00 8.14   ? 3823 PHE A C     1 
ATOM   16890 O  O     . PHE A 1 3823 ? 81.677  95.678  76.343  1.00 9.65   ? 3823 PHE A O     1 
ATOM   16891 C  CB    . PHE A 1 3823 ? 82.866  97.436  78.652  1.00 13.38  ? 3823 PHE A CB    1 
ATOM   16892 C  CG    . PHE A 1 3823 ? 81.894  97.362  79.800  1.00 12.46  ? 3823 PHE A CG    1 
ATOM   16893 C  CD1   . PHE A 1 3823 ? 81.177  96.203  80.052  1.00 11.19  ? 3823 PHE A CD1   1 
ATOM   16894 C  CD2   . PHE A 1 3823 ? 81.703  98.454  80.630  1.00 12.44  ? 3823 PHE A CD2   1 
ATOM   16895 C  CE1   . PHE A 1 3823 ? 80.284  96.139  81.103  1.00 10.23  ? 3823 PHE A CE1   1 
ATOM   16896 C  CE2   . PHE A 1 3823 ? 80.814  98.393  81.685  1.00 12.66  ? 3823 PHE A CE2   1 
ATOM   16897 C  CZ    . PHE A 1 3823 ? 80.104  97.234  81.922  1.00 10.26  ? 3823 PHE A CZ    1 
ATOM   16898 N  N     . LEU A 1 3824 ? 79.948  96.890  77.123  1.00 7.59   ? 3824 LEU A N     1 
ATOM   16899 C  CA    . LEU A 1 3824 ? 78.961  95.871  76.793  1.00 7.46   ? 3824 LEU A CA    1 
ATOM   16900 C  C     . LEU A 1 3824 ? 78.682  95.780  75.298  1.00 7.51   ? 3824 LEU A C     1 
ATOM   16901 O  O     . LEU A 1 3824 ? 78.149  94.764  74.842  1.00 6.39   ? 3824 LEU A O     1 
ATOM   16902 C  CB    . LEU A 1 3824 ? 77.658  96.146  77.549  1.00 7.50   ? 3824 LEU A CB    1 
ATOM   16903 C  CG    . LEU A 1 3824 ? 76.602  95.039  77.578  1.00 6.67   ? 3824 LEU A CG    1 
ATOM   16904 C  CD1   . LEU A 1 3824 ? 77.103  93.844  78.368  1.00 8.44   ? 3824 LEU A CD1   1 
ATOM   16905 C  CD2   . LEU A 1 3824 ? 75.298  95.558  78.157  1.00 6.99   ? 3824 LEU A CD2   1 
ATOM   16906 N  N     . TYR A 1 3825 ? 79.045  96.802  74.525  1.00 8.39   ? 3825 TYR A N     1 
ATOM   16907 C  CA    . TYR A 1 3825 ? 78.705  96.851  73.102  1.00 6.52   ? 3825 TYR A CA    1 
ATOM   16908 C  C     . TYR A 1 3825 ? 79.763  96.100  72.292  1.00 6.30   ? 3825 TYR A C     1 
ATOM   16909 O  O     . TYR A 1 3825 ? 80.565  96.673  71.553  1.00 10.51  ? 3825 TYR A O     1 
ATOM   16910 C  CB    . TYR A 1 3825 ? 78.556  98.294  72.635  1.00 6.78   ? 3825 TYR A CB    1 
ATOM   16911 C  CG    . TYR A 1 3825 ? 77.541  99.106  73.415  1.00 8.06   ? 3825 TYR A CG    1 
ATOM   16912 C  CD1   . TYR A 1 3825 ? 76.598  98.490  74.230  1.00 7.18   ? 3825 TYR A CD1   1 
ATOM   16913 C  CD2   . TYR A 1 3825 ? 77.525  100.492 73.332  1.00 6.98   ? 3825 TYR A CD2   1 
ATOM   16914 C  CE1   . TYR A 1 3825 ? 75.678  99.228  74.942  1.00 6.67   ? 3825 TYR A CE1   1 
ATOM   16915 C  CE2   . TYR A 1 3825 ? 76.603  101.238 74.039  1.00 9.33   ? 3825 TYR A CE2   1 
ATOM   16916 C  CZ    . TYR A 1 3825 ? 75.682  100.601 74.842  1.00 8.58   ? 3825 TYR A CZ    1 
ATOM   16917 O  OH    . TYR A 1 3825 ? 74.763  101.339 75.550  1.00 9.29   ? 3825 TYR A OH    1 
ATOM   16918 N  N     . GLN A 1 3826 ? 79.745  94.779  72.447  1.00 6.12   ? 3826 GLN A N     1 
ATOM   16919 C  CA    . GLN A 1 3826 ? 80.618  93.884  71.699  1.00 5.68   ? 3826 GLN A CA    1 
ATOM   16920 C  C     . GLN A 1 3826 ? 79.796  93.186  70.624  1.00 5.87   ? 3826 GLN A C     1 
ATOM   16921 O  O     . GLN A 1 3826 ? 78.786  92.542  70.928  1.00 7.13   ? 3826 GLN A O     1 
ATOM   16922 C  CB    . GLN A 1 3826 ? 81.277  92.860  72.623  1.00 7.08   ? 3826 GLN A CB    1 
ATOM   16923 C  CG    . GLN A 1 3826 ? 82.006  93.466  73.810  1.00 6.31   ? 3826 GLN A CG    1 
ATOM   16924 C  CD    . GLN A 1 3826 ? 83.022  94.512  73.398  1.00 8.66   ? 3826 GLN A CD    1 
ATOM   16925 O  OE1   . GLN A 1 3826 ? 83.935  94.235  72.622  1.00 10.67  ? 3826 GLN A OE1   1 
ATOM   16926 N  NE2   . GLN A 1 3826 ? 82.871  95.722  73.922  1.00 9.50   ? 3826 GLN A NE2   1 
ATOM   16927 N  N     . TYR A 1 3827 ? 80.230  93.314  69.372  1.00 7.20   ? 3827 TYR A N     1 
ATOM   16928 C  CA    . TYR A 1 3827 ? 79.506  92.754  68.240  1.00 6.75   ? 3827 TYR A CA    1 
ATOM   16929 C  C     . TYR A 1 3827 ? 80.494  92.102  67.288  1.00 12.85  ? 3827 TYR A C     1 
ATOM   16930 O  O     . TYR A 1 3827 ? 81.496  92.717  66.916  1.00 18.57  ? 3827 TYR A O     1 
ATOM   16931 C  CB    . TYR A 1 3827 ? 78.703  93.837  67.512  1.00 6.57   ? 3827 TYR A CB    1 
ATOM   16932 C  CG    . TYR A 1 3827 ? 77.757  94.587  68.418  1.00 6.68   ? 3827 TYR A CG    1 
ATOM   16933 C  CD1   . TYR A 1 3827 ? 76.649  93.960  68.970  1.00 6.01   ? 3827 TYR A CD1   1 
ATOM   16934 C  CD2   . TYR A 1 3827 ? 77.980  95.920  68.733  1.00 6.25   ? 3827 TYR A CD2   1 
ATOM   16935 C  CE1   . TYR A 1 3827 ? 75.786  94.642  69.804  1.00 6.56   ? 3827 TYR A CE1   1 
ATOM   16936 C  CE2   . TYR A 1 3827 ? 77.123  96.610  69.566  1.00 5.58   ? 3827 TYR A CE2   1 
ATOM   16937 C  CZ    . TYR A 1 3827 ? 76.028  95.966  70.099  1.00 5.51   ? 3827 TYR A CZ    1 
ATOM   16938 O  OH    . TYR A 1 3827 ? 75.169  96.647  70.929  1.00 7.41   ? 3827 TYR A OH    1 
ATOM   16939 N  N     . SER A 1 3828 ? 80.216  90.861  66.909  1.00 13.61  ? 3828 SER A N     1 
ATOM   16940 C  CA    . SER A 1 3828 ? 81.042  90.150  65.949  1.00 10.95  ? 3828 SER A CA    1 
ATOM   16941 C  C     . SER A 1 3828 ? 80.589  90.456  64.523  1.00 11.19  ? 3828 SER A C     1 
ATOM   16942 O  O     . SER A 1 3828 ? 79.554  91.084  64.290  1.00 11.55  ? 3828 SER A O     1 
ATOM   16943 C  CB    . SER A 1 3828 ? 80.995  88.646  66.214  1.00 12.32  ? 3828 SER A CB    1 
ATOM   16944 O  OG    . SER A 1 3828 ? 79.709  88.122  65.940  1.00 8.98   ? 3828 SER A OG    1 
ATOM   16945 N  N     . LEU A 1 3829 ? 81.391  90.003  63.557  1.00 11.07  ? 3829 LEU A N     1 
ATOM   16946 C  CA    . LEU A 1 3829 ? 80.993  90.122  62.159  1.00 7.01   ? 3829 LEU A CA    1 
ATOM   16947 C  C     . LEU A 1 3829 ? 79.807  89.222  61.841  1.00 6.58   ? 3829 LEU A C     1 
ATOM   16948 O  O     . LEU A 1 3829 ? 78.974  89.571  60.997  1.00 8.25   ? 3829 LEU A O     1 
ATOM   16949 C  CB    . LEU A 1 3829 ? 82.175  89.797  61.243  1.00 9.45   ? 3829 LEU A CB    1 
ATOM   16950 C  CG    . LEU A 1 3829 ? 81.916  89.787  59.734  1.00 9.84   ? 3829 LEU A CG    1 
ATOM   16951 C  CD1   . LEU A 1 3829 ? 81.430  91.144  59.251  1.00 7.57   ? 3829 LEU A CD1   1 
ATOM   16952 C  CD2   . LEU A 1 3829 ? 83.165  89.364  58.978  1.00 13.99  ? 3829 LEU A CD2   1 
ATOM   16953 N  N     . GLN A 1 3830 ? 79.710  88.072  62.512  1.00 8.49   ? 3830 GLN A N     1 
ATOM   16954 C  CA    . GLN A 1 3830 ? 78.594  87.167  62.267  1.00 9.89   ? 3830 GLN A CA    1 
ATOM   16955 C  C     . GLN A 1 3830 ? 77.264  87.795  62.659  1.00 9.76   ? 3830 GLN A C     1 
ATOM   16956 O  O     . GLN A 1 3830 ? 76.238  87.497  62.045  1.00 10.61  ? 3830 GLN A O     1 
ATOM   16957 C  CB    . GLN A 1 3830 ? 78.804  85.852  63.017  1.00 10.04  ? 3830 GLN A CB    1 
ATOM   16958 C  CG    . GLN A 1 3830 ? 77.871  84.737  62.570  1.00 12.51  ? 3830 GLN A CG    1 
ATOM   16959 C  CD    . GLN A 1 3830 ? 77.794  84.615  61.060  1.00 20.68  ? 3830 GLN A CD    1 
ATOM   16960 O  OE1   . GLN A 1 3830 ? 78.802  84.380  60.393  1.00 20.74  ? 3830 GLN A OE1   1 
ATOM   16961 N  NE2   . GLN A 1 3830 ? 76.596  84.781  60.513  1.00 17.57  ? 3830 GLN A NE2   1 
ATOM   16962 N  N     . PHE A 1 3831 ? 77.257  88.670  63.667  1.00 8.26   ? 3831 PHE A N     1 
ATOM   16963 C  CA    . PHE A 1 3831 ? 76.021  89.344  64.059  1.00 8.15   ? 3831 PHE A CA    1 
ATOM   16964 C  C     . PHE A 1 3831 ? 75.520  90.259  62.945  1.00 8.19   ? 3831 PHE A C     1 
ATOM   16965 O  O     . PHE A 1 3831 ? 74.335  90.233  62.580  1.00 9.36   ? 3831 PHE A O     1 
ATOM   16966 C  CB    . PHE A 1 3831 ? 76.256  90.127  65.352  1.00 7.92   ? 3831 PHE A CB    1 
ATOM   16967 C  CG    . PHE A 1 3831 ? 75.044  90.849  65.860  1.00 9.65   ? 3831 PHE A CG    1 
ATOM   16968 C  CD1   . PHE A 1 3831 ? 73.897  90.152  66.199  1.00 16.88  ? 3831 PHE A CD1   1 
ATOM   16969 C  CD2   . PHE A 1 3831 ? 75.055  92.224  66.013  1.00 10.04  ? 3831 PHE A CD2   1 
ATOM   16970 C  CE1   . PHE A 1 3831 ? 72.781  90.815  66.672  1.00 16.35  ? 3831 PHE A CE1   1 
ATOM   16971 C  CE2   . PHE A 1 3831 ? 73.942  92.892  66.487  1.00 9.00   ? 3831 PHE A CE2   1 
ATOM   16972 C  CZ    . PHE A 1 3831 ? 72.804  92.187  66.816  1.00 9.00   ? 3831 PHE A CZ    1 
ATOM   16973 N  N     . PHE A 1 3832 ? 76.419  91.067  62.378  1.00 7.12   ? 3832 PHE A N     1 
ATOM   16974 C  CA    . PHE A 1 3832 ? 76.034  91.925  61.264  1.00 7.10   ? 3832 PHE A CA    1 
ATOM   16975 C  C     . PHE A 1 3832 ? 75.658  91.102  60.039  1.00 8.19   ? 3832 PHE A C     1 
ATOM   16976 O  O     . PHE A 1 3832 ? 74.757  91.482  59.284  1.00 9.22   ? 3832 PHE A O     1 
ATOM   16977 C  CB    . PHE A 1 3832 ? 77.159  92.904  60.930  1.00 6.72   ? 3832 PHE A CB    1 
ATOM   16978 C  CG    . PHE A 1 3832 ? 76.967  93.609  59.621  1.00 9.32   ? 3832 PHE A CG    1 
ATOM   16979 C  CD1   . PHE A 1 3832 ? 76.155  94.726  59.538  1.00 8.78   ? 3832 PHE A CD1   1 
ATOM   16980 C  CD2   . PHE A 1 3832 ? 77.594  93.154  58.472  1.00 7.89   ? 3832 PHE A CD2   1 
ATOM   16981 C  CE1   . PHE A 1 3832 ? 75.968  95.373  58.337  1.00 8.67   ? 3832 PHE A CE1   1 
ATOM   16982 C  CE2   . PHE A 1 3832 ? 77.411  93.798  57.269  1.00 7.19   ? 3832 PHE A CE2   1 
ATOM   16983 C  CZ    . PHE A 1 3832 ? 76.597  94.908  57.202  1.00 8.83   ? 3832 PHE A CZ    1 
ATOM   16984 N  N     . LEU A 1 3833 ? 76.345  89.979  59.815  1.00 8.14   ? 3833 LEU A N     1 
ATOM   16985 C  CA    . LEU A 1 3833 ? 75.978  89.117  58.697  1.00 7.94   ? 3833 LEU A CA    1 
ATOM   16986 C  C     . LEU A 1 3833 ? 74.603  88.492  58.898  1.00 9.72   ? 3833 LEU A C     1 
ATOM   16987 O  O     . LEU A 1 3833 ? 73.864  88.307  57.927  1.00 14.98  ? 3833 LEU A O     1 
ATOM   16988 C  CB    . LEU A 1 3833 ? 77.037  88.033  58.492  1.00 9.78   ? 3833 LEU A CB    1 
ATOM   16989 C  CG    . LEU A 1 3833 ? 78.396  88.529  57.996  1.00 9.03   ? 3833 LEU A CG    1 
ATOM   16990 C  CD1   . LEU A 1 3833 ? 79.390  87.382  57.902  1.00 9.88   ? 3833 LEU A CD1   1 
ATOM   16991 C  CD2   . LEU A 1 3833 ? 78.254  89.235  56.657  1.00 7.39   ? 3833 LEU A CD2   1 
ATOM   16992 N  N     . ASP A 1 3834 ? 74.245  88.166  60.141  1.00 8.78   ? 3834 ASP A N     1 
ATOM   16993 C  CA    . ASP A 1 3834 ? 72.893  87.697  60.426  1.00 10.49  ? 3834 ASP A CA    1 
ATOM   16994 C  C     . ASP A 1 3834 ? 71.869  88.787  60.149  1.00 12.99  ? 3834 ASP A C     1 
ATOM   16995 O  O     . ASP A 1 3834 ? 70.797  88.515  59.599  1.00 13.44  ? 3834 ASP A O     1 
ATOM   16996 C  CB    . ASP A 1 3834 ? 72.791  87.225  61.877  1.00 14.55  ? 3834 ASP A CB    1 
ATOM   16997 C  CG    . ASP A 1 3834 ? 73.657  86.015  62.161  1.00 23.61  ? 3834 ASP A CG    1 
ATOM   16998 O  OD1   . ASP A 1 3834 ? 74.206  85.434  61.202  1.00 22.55  ? 3834 ASP A OD1   1 
ATOM   16999 O  OD2   . ASP A 1 3834 ? 73.790  85.645  63.346  1.00 23.52  ? 3834 ASP A OD2   1 
ATOM   17000 N  N     . ILE A 1 3835 ? 72.183  90.030  60.525  1.00 10.70  ? 3835 ILE A N     1 
ATOM   17001 C  CA    . ILE A 1 3835 ? 71.293  91.147  60.207  1.00 8.47   ? 3835 ILE A CA    1 
ATOM   17002 C  C     . ILE A 1 3835 ? 71.116  91.273  58.696  1.00 10.11  ? 3835 ILE A C     1 
ATOM   17003 O  O     . ILE A 1 3835 ? 69.999  91.454  58.192  1.00 12.18  ? 3835 ILE A O     1 
ATOM   17004 C  CB    . ILE A 1 3835 ? 71.834  92.452  60.821  1.00 9.08   ? 3835 ILE A CB    1 
ATOM   17005 C  CG1   . ILE A 1 3835 ? 71.643  92.454  62.337  1.00 9.52   ? 3835 ILE A CG1   1 
ATOM   17006 C  CG2   . ILE A 1 3835 ? 71.160  93.664  60.193  1.00 6.78   ? 3835 ILE A CG2   1 
ATOM   17007 C  CD1   . ILE A 1 3835 ? 72.415  93.546  63.045  1.00 8.13   ? 3835 ILE A CD1   1 
ATOM   17008 N  N     . TYR A 1 3836 ? 72.220  91.176  57.955  1.00 10.02  ? 3836 TYR A N     1 
ATOM   17009 C  CA    . TYR A 1 3836 ? 72.180  91.315  56.503  1.00 9.09   ? 3836 TYR A CA    1 
ATOM   17010 C  C     . TYR A 1 3836 ? 71.376  90.188  55.863  1.00 10.62  ? 3836 TYR A C     1 
ATOM   17011 O  O     . TYR A 1 3836 ? 70.589  90.424  54.939  1.00 13.04  ? 3836 TYR A O     1 
ATOM   17012 C  CB    . TYR A 1 3836 ? 73.610  91.348  55.966  1.00 10.05  ? 3836 TYR A CB    1 
ATOM   17013 C  CG    . TYR A 1 3836 ? 73.751  91.786  54.530  1.00 12.21  ? 3836 TYR A CG    1 
ATOM   17014 C  CD1   . TYR A 1 3836 ? 72.905  92.743  53.988  1.00 14.25  ? 3836 TYR A CD1   1 
ATOM   17015 C  CD2   . TYR A 1 3836 ? 74.757  91.269  53.727  1.00 9.28   ? 3836 TYR A CD2   1 
ATOM   17016 C  CE1   . TYR A 1 3836 ? 73.044  93.154  52.678  1.00 13.04  ? 3836 TYR A CE1   1 
ATOM   17017 C  CE2   . TYR A 1 3836 ? 74.904  91.675  52.418  1.00 10.21  ? 3836 TYR A CE2   1 
ATOM   17018 C  CZ    . TYR A 1 3836 ? 74.046  92.618  51.900  1.00 12.31  ? 3836 TYR A CZ    1 
ATOM   17019 O  OH    . TYR A 1 3836 ? 74.191  93.025  50.598  1.00 12.71  ? 3836 TYR A OH    1 
ATOM   17020 N  N     . HIS A 1 3837 ? 71.559  88.957  56.346  1.00 10.82  ? 3837 HIS A N     1 
ATOM   17021 C  CA    . HIS A 1 3837 ? 70.776  87.828  55.854  1.00 12.77  ? 3837 HIS A CA    1 
ATOM   17022 C  C     . HIS A 1 3837 ? 69.295  88.009  56.165  1.00 15.39  ? 3837 HIS A C     1 
ATOM   17023 O  O     . HIS A 1 3837 ? 68.435  87.687  55.337  1.00 19.31  ? 3837 HIS A O     1 
ATOM   17024 C  CB    . HIS A 1 3837 ? 71.305  86.530  56.465  1.00 13.75  ? 3837 HIS A CB    1 
ATOM   17025 C  CG    . HIS A 1 3837 ? 70.531  85.310  56.074  1.00 23.76  ? 3837 HIS A CG    1 
ATOM   17026 N  ND1   . HIS A 1 3837 ? 70.912  84.489  55.034  1.00 30.44  ? 3837 HIS A ND1   1 
ATOM   17027 C  CD2   . HIS A 1 3837 ? 69.404  84.764  56.589  1.00 25.86  ? 3837 HIS A CD2   1 
ATOM   17028 C  CE1   . HIS A 1 3837 ? 70.051  83.494  54.922  1.00 31.08  ? 3837 HIS A CE1   1 
ATOM   17029 N  NE2   . HIS A 1 3837 ? 69.126  83.638  55.853  1.00 30.63  ? 3837 HIS A NE2   1 
ATOM   17030 N  N     . ASN A 1 3838 ? 68.982  88.514  57.362  1.00 14.27  ? 3838 ASN A N     1 
ATOM   17031 C  CA    . ASN A 1 3838 ? 67.602  88.834  57.709  1.00 14.31  ? 3838 ASN A CA    1 
ATOM   17032 C  C     . ASN A 1 3838 ? 67.003  89.821  56.719  1.00 17.89  ? 3838 ASN A C     1 
ATOM   17033 O  O     . ASN A 1 3838 ? 65.865  89.651  56.266  1.00 20.89  ? 3838 ASN A O     1 
ATOM   17034 C  CB    . ASN A 1 3838 ? 67.548  89.406  59.127  1.00 18.70  ? 3838 ASN A CB    1 
ATOM   17035 C  CG    . ASN A 1 3838 ? 66.137  89.726  59.580  1.00 19.55  ? 3838 ASN A CG    1 
ATOM   17036 O  OD1   . ASN A 1 3838 ? 65.785  90.889  59.768  1.00 18.86  ? 3838 ASN A OD1   1 
ATOM   17037 N  ND2   . ASN A 1 3838 ? 65.332  88.694  59.787  1.00 21.11  ? 3838 ASN A ND2   1 
ATOM   17038 N  N     . VAL A 1 3839 ? 67.760  90.862  56.374  1.00 17.05  ? 3839 VAL A N     1 
ATOM   17039 C  CA    . VAL A 1 3839 ? 67.260  91.870  55.446  1.00 14.87  ? 3839 VAL A CA    1 
ATOM   17040 C  C     . VAL A 1 3839 ? 67.095  91.287  54.045  1.00 16.35  ? 3839 VAL A C     1 
ATOM   17041 O  O     . VAL A 1 3839 ? 66.163  91.647  53.315  1.00 21.51  ? 3839 VAL A O     1 
ATOM   17042 C  CB    . VAL A 1 3839 ? 68.190  93.097  55.450  1.00 13.70  ? 3839 VAL A CB    1 
ATOM   17043 C  CG1   . VAL A 1 3839 ? 67.752  94.107  54.407  1.00 15.07  ? 3839 VAL A CG1   1 
ATOM   17044 C  CG2   . VAL A 1 3839 ? 68.203  93.730  56.829  1.00 14.09  ? 3839 VAL A CG2   1 
ATOM   17045 N  N     . LEU A 1 3840 ? 67.985  90.378  53.646  1.00 19.20  ? 3840 LEU A N     1 
ATOM   17046 C  CA    . LEU A 1 3840 ? 67.987  89.922  52.259  1.00 16.23  ? 3840 LEU A CA    1 
ATOM   17047 C  C     . LEU A 1 3840 ? 66.977  88.808  51.999  1.00 23.22  ? 3840 LEU A C     1 
ATOM   17048 O  O     . LEU A 1 3840 ? 66.246  88.857  51.004  1.00 32.70  ? 3840 LEU A O     1 
ATOM   17049 C  CB    . LEU A 1 3840 ? 69.387  89.460  51.857  1.00 13.94  ? 3840 LEU A CB    1 
ATOM   17050 C  CG    . LEU A 1 3840 ? 70.443  90.553  51.697  1.00 15.30  ? 3840 LEU A CG    1 
ATOM   17051 C  CD1   . LEU A 1 3840 ? 71.800  89.941  51.398  1.00 12.18  ? 3840 LEU A CD1   1 
ATOM   17052 C  CD2   . LEU A 1 3840 ? 70.036  91.527  50.604  1.00 15.43  ? 3840 LEU A CD2   1 
ATOM   17053 N  N     . TYR A 1 3841 ? 66.917  87.799  52.867  1.00 24.14  ? 3841 TYR A N     1 
ATOM   17054 C  CA    . TYR A 1 3841 ? 66.199  86.569  52.551  1.00 24.35  ? 3841 TYR A CA    1 
ATOM   17055 C  C     . TYR A 1 3841 ? 64.873  86.403  53.276  1.00 32.90  ? 3841 TYR A C     1 
ATOM   17056 O  O     . TYR A 1 3841 ? 63.951  85.813  52.710  1.00 38.82  ? 3841 TYR A O     1 
ATOM   17057 C  CB    . TYR A 1 3841 ? 67.081  85.352  52.852  1.00 25.29  ? 3841 TYR A CB    1 
ATOM   17058 C  CG    . TYR A 1 3841 ? 68.281  85.245  51.944  1.00 29.45  ? 3841 TYR A CG    1 
ATOM   17059 C  CD1   . TYR A 1 3841 ? 68.146  84.801  50.635  1.00 26.81  ? 3841 TYR A CD1   1 
ATOM   17060 C  CD2   . TYR A 1 3841 ? 69.544  85.606  52.385  1.00 22.53  ? 3841 TYR A CD2   1 
ATOM   17061 C  CE1   . TYR A 1 3841 ? 69.239  84.705  49.798  1.00 29.15  ? 3841 TYR A CE1   1 
ATOM   17062 C  CE2   . TYR A 1 3841 ? 70.642  85.514  51.557  1.00 24.94  ? 3841 TYR A CE2   1 
ATOM   17063 C  CZ    . TYR A 1 3841 ? 70.485  85.064  50.263  1.00 34.11  ? 3841 TYR A CZ    1 
ATOM   17064 O  OH    . TYR A 1 3841 ? 71.578  84.972  49.432  1.00 38.40  ? 3841 TYR A OH    1 
ATOM   17065 N  N     . GLU A 1 3842 ? 64.747  86.897  54.503  1.00 26.89  ? 3842 GLU A N     1 
ATOM   17066 C  CA    . GLU A 1 3842 ? 63.525  86.749  55.286  1.00 29.15  ? 3842 GLU A CA    1 
ATOM   17067 C  C     . GLU A 1 3842 ? 62.907  88.107  55.616  1.00 29.10  ? 3842 GLU A C     1 
ATOM   17068 O  O     . GLU A 1 3842 ? 62.434  88.351  56.727  1.00 32.51  ? 3842 GLU A O     1 
ATOM   17069 C  CB    . GLU A 1 3842 ? 63.795  85.924  56.542  1.00 29.93  ? 3842 GLU A CB    1 
ATOM   17070 C  CG    . GLU A 1 3842 ? 64.738  86.562  57.541  1.00 32.20  ? 3842 GLU A CG    1 
ATOM   17071 C  CD    . GLU A 1 3842 ? 65.017  85.668  58.731  1.00 43.53  ? 3842 GLU A CD    1 
ATOM   17072 O  OE1   . GLU A 1 3842 ? 64.489  84.537  58.763  1.00 48.24  ? 3842 GLU A OE1   1 
ATOM   17073 O  OE2   . GLU A 1 3842 ? 65.764  86.096  59.636  1.00 41.83  ? 3842 GLU A OE2   1 
ATOM   17074 N  N     . ASN A 1 3843 ? 62.884  88.995  54.622  1.00 27.08  ? 3843 ASN A N     1 
ATOM   17075 C  CA    . ASN A 1 3843 ? 62.312  90.323  54.770  1.00 29.39  ? 3843 ASN A CA    1 
ATOM   17076 C  C     . ASN A 1 3843 ? 60.861  90.293  54.319  1.00 35.80  ? 3843 ASN A C     1 
ATOM   17077 O  O     . ASN A 1 3843 ? 60.598  90.007  53.140  1.00 36.99  ? 3843 ASN A O     1 
ATOM   17078 C  CB    . ASN A 1 3843 ? 63.104  91.330  53.943  1.00 27.37  ? 3843 ASN A CB    1 
ATOM   17079 C  CG    . ASN A 1 3843 ? 62.648  92.760  54.151  1.00 29.72  ? 3843 ASN A CG    1 
ATOM   17080 O  OD1   . ASN A 1 3843 ? 61.684  93.028  54.867  1.00 34.30  ? 3843 ASN A OD1   1 
ATOM   17081 N  ND2   . ASN A 1 3843 ? 63.349  93.694  53.519  1.00 25.02  ? 3843 ASN A ND2   1 
ATOM   17082 N  N     . PRO A 1 3844 ? 59.896  90.570  55.201  1.00 39.04  ? 3844 PRO A N     1 
ATOM   17083 C  CA    . PRO A 1 3844 ? 58.486  90.543  54.777  1.00 36.49  ? 3844 PRO A CA    1 
ATOM   17084 C  C     . PRO A 1 3844 ? 58.128  91.607  53.753  1.00 34.61  ? 3844 PRO A C     1 
ATOM   17085 O  O     . PRO A 1 3844 ? 57.108  91.460  53.069  1.00 41.40  ? 3844 PRO A O     1 
ATOM   17086 C  CB    . PRO A 1 3844 ? 57.715  90.753  56.091  1.00 40.13  ? 3844 PRO A CB    1 
ATOM   17087 C  CG    . PRO A 1 3844 ? 58.721  90.518  57.187  1.00 39.26  ? 3844 PRO A CG    1 
ATOM   17088 C  CD    . PRO A 1 3844 ? 60.037  90.929  56.620  1.00 35.81  ? 3844 PRO A CD    1 
ATOM   17089 N  N     . ASN A 1 3845 ? 58.924  92.666  53.621  1.00 33.15  ? 3845 ASN A N     1 
ATOM   17090 C  CA    . ASN A 1 3845 ? 58.616  93.746  52.692  1.00 31.49  ? 3845 ASN A CA    1 
ATOM   17091 C  C     . ASN A 1 3845 ? 59.004  93.428  51.253  1.00 32.43  ? 3845 ASN A C     1 
ATOM   17092 O  O     . ASN A 1 3845 ? 58.700  94.224  50.358  1.00 32.48  ? 3845 ASN A O     1 
ATOM   17093 C  CB    . ASN A 1 3845 ? 59.307  95.036  53.141  1.00 32.08  ? 3845 ASN A CB    1 
ATOM   17094 C  CG    . ASN A 1 3845 ? 59.111  95.320  54.616  1.00 36.67  ? 3845 ASN A CG    1 
ATOM   17095 O  OD1   . ASN A 1 3845 ? 57.993  95.257  55.129  1.00 39.28  ? 3845 ASN A OD1   1 
ATOM   17096 N  ND2   . ASN A 1 3845 ? 60.198  95.636  55.308  1.00 33.53  ? 3845 ASN A ND2   1 
ATOM   17097 N  N     . LEU A 1 3846 ? 59.664  92.295  51.009  1.00 32.17  ? 3846 LEU A N     1 
ATOM   17098 C  CA    . LEU A 1 3846 ? 60.028  91.862  49.666  1.00 37.25  ? 3846 LEU A CA    1 
ATOM   17099 C  C     . LEU A 1 3846 ? 59.134  90.732  49.167  1.00 44.43  ? 3846 LEU A C     1 
ATOM   17100 O  O     . LEU A 1 3846 ? 59.488  90.045  48.203  1.00 47.98  ? 3846 LEU A O     1 
ATOM   17101 C  CB    . LEU A 1 3846 ? 61.493  91.426  49.628  1.00 35.02  ? 3846 LEU A CB    1 
ATOM   17102 C  CG    . LEU A 1 3846 ? 62.555  92.462  49.997  1.00 32.90  ? 3846 LEU A CG    1 
ATOM   17103 C  CD1   . LEU A 1 3846 ? 63.880  91.773  50.274  1.00 24.98  ? 3846 LEU A CD1   1 
ATOM   17104 C  CD2   . LEU A 1 3846 ? 62.707  93.494  48.893  1.00 25.65  ? 3846 LEU A CD2   1 
ATOM   17105 N  N     . LYS A 1 3847 ? 57.983  90.523  49.812  1.00 43.83  ? 3847 LYS A N     1 
ATOM   17106 C  CA    . LYS A 1 3847 ? 57.169  89.346  49.527  1.00 50.68  ? 3847 LYS A CA    1 
ATOM   17107 C  C     . LYS A 1 3847 ? 56.626  89.361  48.102  1.00 55.50  ? 3847 LYS A C     1 
ATOM   17108 O  O     . LYS A 1 3847 ? 56.676  88.342  47.402  1.00 59.63  ? 3847 LYS A O     1 
ATOM   17109 C  CB    . LYS A 1 3847 ? 56.023  89.252  50.533  1.00 51.93  ? 3847 LYS A CB    1 
ATOM   17110 C  CG    . LYS A 1 3847 ? 55.206  87.976  50.428  1.00 52.07  ? 3847 LYS A CG    1 
ATOM   17111 C  CD    . LYS A 1 3847 ? 56.026  86.768  50.849  1.00 55.00  ? 3847 LYS A CD    1 
ATOM   17112 C  CE    . LYS A 1 3847 ? 56.454  86.877  52.304  1.00 63.54  ? 3847 LYS A CE    1 
ATOM   17113 N  NZ    . LYS A 1 3847 ? 57.263  85.705  52.737  1.00 68.02  ? 3847 LYS A NZ    1 
ATOM   17114 N  N     . GLY A 1 3848 ? 56.107  90.500  47.653  1.00 50.54  ? 3848 GLY A N     1 
ATOM   17115 C  CA    . GLY A 1 3848 ? 55.465  90.558  46.354  1.00 48.45  ? 3848 GLY A CA    1 
ATOM   17116 C  C     . GLY A 1 3848 ? 56.112  91.507  45.366  1.00 49.46  ? 3848 GLY A C     1 
ATOM   17117 O  O     . GLY A 1 3848 ? 55.630  91.660  44.240  1.00 54.09  ? 3848 GLY A O     1 
ATOM   17118 N  N     . VAL A 1 3849 ? 57.201  92.149  45.772  1.00 49.69  ? 3849 VAL A N     1 
ATOM   17119 C  CA    . VAL A 1 3849 ? 57.869  93.127  44.921  1.00 48.41  ? 3849 VAL A CA    1 
ATOM   17120 C  C     . VAL A 1 3849 ? 58.858  92.408  44.013  1.00 48.76  ? 3849 VAL A C     1 
ATOM   17121 O  O     . VAL A 1 3849 ? 59.671  91.599  44.476  1.00 45.72  ? 3849 VAL A O     1 
ATOM   17122 C  CB    . VAL A 1 3849 ? 58.568  94.198  45.771  1.00 46.22  ? 3849 VAL A CB    1 
ATOM   17123 C  CG1   . VAL A 1 3849 ? 59.510  95.015  44.915  1.00 37.77  ? 3849 VAL A CG1   1 
ATOM   17124 C  CG2   . VAL A 1 3849 ? 57.539  95.094  46.446  1.00 51.42  ? 3849 VAL A CG2   1 
ATOM   17125 N  N     . THR A 1 3850 ? 58.791  92.701  42.714  1.00 47.86  ? 3850 THR A N     1 
ATOM   17126 C  CA    . THR A 1 3850 ? 59.646  92.058  41.725  1.00 44.13  ? 3850 THR A CA    1 
ATOM   17127 C  C     . THR A 1 3850 ? 60.630  93.001  41.050  1.00 42.28  ? 3850 THR A C     1 
ATOM   17128 O  O     . THR A 1 3850 ? 61.676  92.544  40.586  1.00 40.66  ? 3850 THR A O     1 
ATOM   17129 C  CB    . THR A 1 3850 ? 58.796  91.382  40.641  1.00 44.59  ? 3850 THR A CB    1 
ATOM   17130 O  OG1   . THR A 1 3850 ? 57.763  92.278  40.213  1.00 46.87  ? 3850 THR A OG1   1 
ATOM   17131 C  CG2   . THR A 1 3850 ? 58.165  90.106  41.178  1.00 42.84  ? 3850 THR A CG2   1 
ATOM   17132 N  N     . ASP A 1 3851 ? 60.322  94.294  40.975  1.00 38.13  ? 3851 ASP A N     1 
ATOM   17133 C  CA    . ASP A 1 3851 ? 61.226  95.241  40.335  1.00 32.65  ? 3851 ASP A CA    1 
ATOM   17134 C  C     . ASP A 1 3851 ? 62.517  95.358  41.136  1.00 35.99  ? 3851 ASP A C     1 
ATOM   17135 O  O     . ASP A 1 3851 ? 62.488  95.570  42.352  1.00 37.24  ? 3851 ASP A O     1 
ATOM   17136 C  CB    . ASP A 1 3851 ? 60.555  96.607  40.200  1.00 37.09  ? 3851 ASP A CB    1 
ATOM   17137 C  CG    . ASP A 1 3851 ? 61.530  97.698  39.803  1.00 42.69  ? 3851 ASP A CG    1 
ATOM   17138 O  OD1   . ASP A 1 3851 ? 62.247  97.520  38.796  1.00 42.23  ? 3851 ASP A OD1   1 
ATOM   17139 O  OD2   . ASP A 1 3851 ? 61.579  98.736  40.496  1.00 42.66  ? 3851 ASP A OD2   1 
ATOM   17140 N  N     . HIS A 1 3852 ? 63.653  95.231  40.445  1.00 34.39  ? 3852 HIS A N     1 
ATOM   17141 C  CA    . HIS A 1 3852 ? 64.940  95.168  41.132  1.00 28.46  ? 3852 HIS A CA    1 
ATOM   17142 C  C     . HIS A 1 3852 ? 65.256  96.467  41.865  1.00 28.39  ? 3852 HIS A C     1 
ATOM   17143 O  O     . HIS A 1 3852 ? 65.803  96.441  42.973  1.00 31.33  ? 3852 HIS A O     1 
ATOM   17144 C  CB    . HIS A 1 3852 ? 66.049  94.829  40.137  1.00 35.48  ? 3852 HIS A CB    1 
ATOM   17145 C  CG    . HIS A 1 3852 ? 65.915  93.469  39.525  1.00 38.34  ? 3852 HIS A CG    1 
ATOM   17146 N  ND1   . HIS A 1 3852 ? 65.239  92.439  40.143  1.00 36.15  ? 3852 HIS A ND1   1 
ATOM   17147 C  CD2   . HIS A 1 3852 ? 66.372  92.969  38.353  1.00 34.89  ? 3852 HIS A CD2   1 
ATOM   17148 C  CE1   . HIS A 1 3852 ? 65.285  91.364  39.378  1.00 32.98  ? 3852 HIS A CE1   1 
ATOM   17149 N  NE2   . HIS A 1 3852 ? 65.966  91.659  38.285  1.00 36.27  ? 3852 HIS A NE2   1 
ATOM   17150 N  N     . THR A 1 3853 ? 64.937  97.613  41.259  1.00 26.79  ? 3853 THR A N     1 
ATOM   17151 C  CA    . THR A 1 3853 ? 65.227  98.891  41.903  1.00 28.91  ? 3853 THR A CA    1 
ATOM   17152 C  C     . THR A 1 3853 ? 64.448  99.047  43.205  1.00 29.65  ? 3853 THR A C     1 
ATOM   17153 O  O     . THR A 1 3853 ? 65.007  99.461  44.230  1.00 30.13  ? 3853 THR A O     1 
ATOM   17154 C  CB    . THR A 1 3853 ? 64.910  100.042 40.948  1.00 32.24  ? 3853 THR A CB    1 
ATOM   17155 O  OG1   . THR A 1 3853 ? 65.754  99.952  39.793  1.00 41.89  ? 3853 THR A OG1   1 
ATOM   17156 C  CG2   . THR A 1 3853 ? 65.138  101.382 41.629  1.00 36.06  ? 3853 THR A CG2   1 
ATOM   17157 N  N     . GLN A 1 3854 ? 63.157  98.710  43.187  1.00 28.08  ? 3854 GLN A N     1 
ATOM   17158 C  CA    . GLN A 1 3854 ? 62.348  98.846  44.392  1.00 34.47  ? 3854 GLN A CA    1 
ATOM   17159 C  C     . GLN A 1 3854 ? 62.769  97.832  45.450  1.00 29.07  ? 3854 GLN A C     1 
ATOM   17160 O  O     . GLN A 1 3854 ? 62.781  98.145  46.647  1.00 28.84  ? 3854 GLN A O     1 
ATOM   17161 C  CB    . GLN A 1 3854 ? 60.866  98.703  44.046  1.00 37.57  ? 3854 GLN A CB    1 
ATOM   17162 C  CG    . GLN A 1 3854 ? 59.955  98.486  45.240  1.00 45.20  ? 3854 GLN A CG    1 
ATOM   17163 C  CD    . GLN A 1 3854 ? 58.497  98.356  44.845  1.00 53.61  ? 3854 GLN A CD    1 
ATOM   17164 O  OE1   . GLN A 1 3854 ? 58.175  98.142  43.676  1.00 50.92  ? 3854 GLN A OE1   1 
ATOM   17165 N  NE2   . GLN A 1 3854 ? 57.605  98.485  45.821  1.00 55.19  ? 3854 GLN A NE2   1 
ATOM   17166 N  N     . ARG A 1 3855 ? 63.137  96.617  45.028  1.00 26.12  ? 3855 ARG A N     1 
ATOM   17167 C  CA    . ARG A 1 3855 ? 63.672  95.640  45.971  1.00 20.79  ? 3855 ARG A CA    1 
ATOM   17168 C  C     . ARG A 1 3855 ? 64.948  96.151  46.625  1.00 22.22  ? 3855 ARG A C     1 
ATOM   17169 O  O     . ARG A 1 3855 ? 65.140  95.991  47.834  1.00 24.51  ? 3855 ARG A O     1 
ATOM   17170 C  CB    . ARG A 1 3855 ? 63.937  94.306  45.273  1.00 20.08  ? 3855 ARG A CB    1 
ATOM   17171 C  CG    . ARG A 1 3855 ? 62.700  93.601  44.755  1.00 24.21  ? 3855 ARG A CG    1 
ATOM   17172 C  CD    . ARG A 1 3855 ? 62.996  92.162  44.370  1.00 27.72  ? 3855 ARG A CD    1 
ATOM   17173 N  NE    . ARG A 1 3855 ? 63.678  91.438  45.435  1.00 25.41  ? 3855 ARG A NE    1 
ATOM   17174 C  CZ    . ARG A 1 3855 ? 63.179  90.378  46.057  1.00 28.84  ? 3855 ARG A CZ    1 
ATOM   17175 N  NH1   . ARG A 1 3855 ? 61.989  89.892  45.745  1.00 31.51  ? 3855 ARG A NH1   1 
ATOM   17176 N  NH2   . ARG A 1 3855 ? 63.892  89.792  47.014  1.00 34.23  ? 3855 ARG A NH2   1 
ATOM   17177 N  N     . LEU A 1 3856 ? 65.834  96.766  45.839  1.00 19.48  ? 3856 LEU A N     1 
ATOM   17178 C  CA    . LEU A 1 3856 ? 67.071  97.304  46.395  1.00 19.57  ? 3856 LEU A CA    1 
ATOM   17179 C  C     . LEU A 1 3856 ? 66.794  98.437  47.374  1.00 21.42  ? 3856 LEU A C     1 
ATOM   17180 O  O     . LEU A 1 3856 ? 67.440  98.530  48.423  1.00 22.64  ? 3856 LEU A O     1 
ATOM   17181 C  CB    . LEU A 1 3856 ? 67.990  97.778  45.270  1.00 18.76  ? 3856 LEU A CB    1 
ATOM   17182 C  CG    . LEU A 1 3856 ? 69.386  98.238  45.692  1.00 17.16  ? 3856 LEU A CG    1 
ATOM   17183 C  CD1   . LEU A 1 3856 ? 70.073  97.177  46.535  1.00 16.87  ? 3856 LEU A CD1   1 
ATOM   17184 C  CD2   . LEU A 1 3856 ? 70.224  98.582  44.470  1.00 23.34  ? 3856 LEU A CD2   1 
ATOM   17185 N  N     . SER A 1 3857 ? 65.842  99.315  47.046  1.00 20.33  ? 3857 SER A N     1 
ATOM   17186 C  CA    . SER A 1 3857 ? 65.493  100.394 47.968  1.00 20.53  ? 3857 SER A CA    1 
ATOM   17187 C  C     . SER A 1 3857 ? 64.925  99.845  49.273  1.00 16.46  ? 3857 SER A C     1 
ATOM   17188 O  O     . SER A 1 3857 ? 65.282  100.310 50.366  1.00 17.15  ? 3857 SER A O     1 
ATOM   17189 C  CB    . SER A 1 3857 ? 64.498  101.348 47.307  1.00 25.00  ? 3857 SER A CB    1 
ATOM   17190 O  OG    . SER A 1 3857 ? 63.243  100.719 47.110  1.00 25.02  ? 3857 SER A OG    1 
ATOM   17191 N  N     . ILE A 1 3858 ? 64.042  98.847  49.176  1.00 16.52  ? 3858 ILE A N     1 
ATOM   17192 C  CA    . ILE A 1 3858 ? 63.469  98.229  50.369  1.00 16.99  ? 3858 ILE A CA    1 
ATOM   17193 C  C     . ILE A 1 3858 ? 64.559  97.569  51.203  1.00 18.12  ? 3858 ILE A C     1 
ATOM   17194 O  O     . ILE A 1 3858 ? 64.566  97.671  52.436  1.00 18.33  ? 3858 ILE A O     1 
ATOM   17195 C  CB    . ILE A 1 3858 ? 62.371  97.226  49.970  1.00 18.25  ? 3858 ILE A CB    1 
ATOM   17196 C  CG1   . ILE A 1 3858 ? 61.158  97.960  49.395  1.00 19.75  ? 3858 ILE A CG1   1 
ATOM   17197 C  CG2   . ILE A 1 3858 ? 61.968  96.369  51.154  1.00 20.12  ? 3858 ILE A CG2   1 
ATOM   17198 C  CD1   . ILE A 1 3858 ? 60.210  97.063  48.633  1.00 28.57  ? 3858 ILE A CD1   1 
ATOM   17199 N  N     . ILE A 1 3859 ? 65.492  96.878  50.544  1.00 17.36  ? 3859 ILE A N     1 
ATOM   17200 C  CA    . ILE A 1 3859 ? 66.592  96.229  51.250  1.00 15.74  ? 3859 ILE A CA    1 
ATOM   17201 C  C     . ILE A 1 3859 ? 67.458  97.264  51.956  1.00 12.80  ? 3859 ILE A C     1 
ATOM   17202 O  O     . ILE A 1 3859 ? 67.872  97.068  53.103  1.00 15.75  ? 3859 ILE A O     1 
ATOM   17203 C  CB    . ILE A 1 3859 ? 67.413  95.366  50.273  1.00 14.74  ? 3859 ILE A CB    1 
ATOM   17204 C  CG1   . ILE A 1 3859 ? 66.666  94.071  49.951  1.00 16.44  ? 3859 ILE A CG1   1 
ATOM   17205 C  CG2   . ILE A 1 3859 ? 68.787  95.059  50.839  1.00 15.53  ? 3859 ILE A CG2   1 
ATOM   17206 C  CD1   . ILE A 1 3859 ? 67.176  93.363  48.719  1.00 12.42  ? 3859 ILE A CD1   1 
ATOM   17207 N  N     . THR A 1 3860 ? 67.744  98.381  51.283  1.00 12.45  ? 3860 THR A N     1 
ATOM   17208 C  CA    . THR A 1 3860 ? 68.558  99.428  51.893  1.00 14.90  ? 3860 THR A CA    1 
ATOM   17209 C  C     . THR A 1 3860 ? 67.879  100.009 53.128  1.00 15.54  ? 3860 THR A C     1 
ATOM   17210 O  O     . THR A 1 3860 ? 68.528  100.225 54.158  1.00 15.33  ? 3860 THR A O     1 
ATOM   17211 C  CB    . THR A 1 3860 ? 68.845  100.530 50.874  1.00 16.85  ? 3860 THR A CB    1 
ATOM   17212 O  OG1   . THR A 1 3860 ? 69.406  99.952  49.689  1.00 20.81  ? 3860 THR A OG1   1 
ATOM   17213 C  CG2   . THR A 1 3860 ? 69.820  101.546 51.448  1.00 14.13  ? 3860 THR A CG2   1 
ATOM   17214 N  N     . LYS A 1 3861 ? 66.573  100.272 53.041  1.00 14.80  ? 3861 LYS A N     1 
ATOM   17215 C  CA    . LYS A 1 3861 ? 65.843  100.797 54.194  1.00 14.41  ? 3861 LYS A CA    1 
ATOM   17216 C  C     . LYS A 1 3861 ? 65.829  99.790  55.344  1.00 16.65  ? 3861 LYS A C     1 
ATOM   17217 O  O     . LYS A 1 3861 ? 66.116  100.133 56.504  1.00 14.84  ? 3861 LYS A O     1 
ATOM   17218 C  CB    . LYS A 1 3861 ? 64.420  101.161 53.768  1.00 15.14  ? 3861 LYS A CB    1 
ATOM   17219 C  CG    . LYS A 1 3861 ? 63.547  101.764 54.852  1.00 17.43  ? 3861 LYS A CG    1 
ATOM   17220 C  CD    . LYS A 1 3861 ? 62.197  102.174 54.277  1.00 21.23  ? 3861 LYS A CD    1 
ATOM   17221 C  CE    . LYS A 1 3861 ? 61.240  102.645 55.359  1.00 31.87  ? 3861 LYS A CE    1 
ATOM   17222 N  NZ    . LYS A 1 3861 ? 61.704  103.906 56.000  1.00 30.80  ? 3861 LYS A NZ    1 
ATOM   17223 N  N     . ASP A 1 3862 ? 65.516  98.531  55.031  1.00 15.83  ? 3862 ASP A N     1 
ATOM   17224 C  CA    . ASP A 1 3862 ? 65.395  97.514  56.065  1.00 12.40  ? 3862 ASP A CA    1 
ATOM   17225 C  C     . ASP A 1 3862 ? 66.739  97.183  56.694  1.00 12.09  ? 3862 ASP A C     1 
ATOM   17226 O  O     . ASP A 1 3862 ? 66.783  96.775  57.856  1.00 15.70  ? 3862 ASP A O     1 
ATOM   17227 C  CB    . ASP A 1 3862 ? 64.746  96.257  55.490  1.00 17.75  ? 3862 ASP A CB    1 
ATOM   17228 C  CG    . ASP A 1 3862 ? 63.287  96.469  55.138  1.00 36.68  ? 3862 ASP A CG    1 
ATOM   17229 O  OD1   . ASP A 1 3862 ? 62.632  97.308  55.791  1.00 37.63  ? 3862 ASP A OD1   1 
ATOM   17230 O  OD2   . ASP A 1 3862 ? 62.793  95.799  54.209  1.00 46.45  ? 3862 ASP A OD2   1 
ATOM   17231 N  N     . LEU A 1 3863 ? 67.840  97.359  55.961  1.00 10.66  ? 3863 LEU A N     1 
ATOM   17232 C  CA    . LEU A 1 3863 ? 69.154  97.145  56.555  1.00 9.62   ? 3863 LEU A CA    1 
ATOM   17233 C  C     . LEU A 1 3863 ? 69.372  98.083  57.731  1.00 8.34   ? 3863 LEU A C     1 
ATOM   17234 O  O     . LEU A 1 3863 ? 69.702  97.644  58.839  1.00 8.65   ? 3863 LEU A O     1 
ATOM   17235 C  CB    . LEU A 1 3863 ? 70.245  97.342  55.503  1.00 9.25   ? 3863 LEU A CB    1 
ATOM   17236 C  CG    . LEU A 1 3863 ? 71.683  97.287  56.023  1.00 10.33  ? 3863 LEU A CG    1 
ATOM   17237 C  CD1   . LEU A 1 3863 ? 72.049  95.874  56.455  1.00 8.26   ? 3863 LEU A CD1   1 
ATOM   17238 C  CD2   . LEU A 1 3863 ? 72.655  97.808  54.977  1.00 7.31   ? 3863 LEU A CD2   1 
ATOM   17239 N  N     . PHE A 1 3864 ? 69.159  99.383  57.512  1.00 8.19   ? 3864 PHE A N     1 
ATOM   17240 C  CA    . PHE A 1 3864 ? 69.301  100.352 58.590  1.00 7.67   ? 3864 PHE A CA    1 
ATOM   17241 C  C     . PHE A 1 3864 ? 68.320  100.062 59.717  1.00 7.56   ? 3864 PHE A C     1 
ATOM   17242 O  O     . PHE A 1 3864 ? 68.694  100.086 60.899  1.00 5.72   ? 3864 PHE A O     1 
ATOM   17243 C  CB    . PHE A 1 3864 ? 69.089  101.767 58.050  1.00 7.65   ? 3864 PHE A CB    1 
ATOM   17244 C  CG    . PHE A 1 3864 ? 70.274  102.321 57.313  1.00 7.82   ? 3864 PHE A CG    1 
ATOM   17245 C  CD1   . PHE A 1 3864 ? 71.286  102.978 57.993  1.00 7.60   ? 3864 PHE A CD1   1 
ATOM   17246 C  CD2   . PHE A 1 3864 ? 70.373  102.190 55.938  1.00 8.81   ? 3864 PHE A CD2   1 
ATOM   17247 C  CE1   . PHE A 1 3864 ? 72.376  103.491 57.314  1.00 9.95   ? 3864 PHE A CE1   1 
ATOM   17248 C  CE2   . PHE A 1 3864 ? 71.460  102.700 55.254  1.00 8.04   ? 3864 PHE A CE2   1 
ATOM   17249 C  CZ    . PHE A 1 3864 ? 72.463  103.351 55.944  1.00 8.68   ? 3864 PHE A CZ    1 
ATOM   17250 N  N     . GLN A 1 3865 ? 67.062  99.766  59.371  1.00 8.45   ? 3865 GLN A N     1 
ATOM   17251 C  CA    . GLN A 1 3865 ? 66.053  99.556  60.406  1.00 6.60   ? 3865 GLN A CA    1 
ATOM   17252 C  C     . GLN A 1 3865 ? 66.394  98.356  61.288  1.00 5.80   ? 3865 GLN A C     1 
ATOM   17253 O  O     . GLN A 1 3865 ? 66.383  98.453  62.522  1.00 6.09   ? 3865 GLN A O     1 
ATOM   17254 C  CB    . GLN A 1 3865 ? 64.674  99.387  59.770  1.00 7.47   ? 3865 GLN A CB    1 
ATOM   17255 C  CG    . GLN A 1 3865 ? 63.541  99.328  60.779  1.00 9.65   ? 3865 GLN A CG    1 
ATOM   17256 C  CD    . GLN A 1 3865 ? 63.357  100.638 61.520  1.00 9.36   ? 3865 GLN A CD    1 
ATOM   17257 O  OE1   . GLN A 1 3865 ? 62.824  101.604 60.975  1.00 12.78  ? 3865 GLN A OE1   1 
ATOM   17258 N  NE2   . GLN A 1 3865 ? 63.804  100.679 62.769  1.00 7.24   ? 3865 GLN A NE2   1 
ATOM   17259 N  N     . VAL A 1 3866 ? 66.711  97.215  60.671  1.00 4.89   ? 3866 VAL A N     1 
ATOM   17260 C  CA    . VAL A 1 3866 ? 66.997  96.002  61.428  1.00 6.19   ? 3866 VAL A CA    1 
ATOM   17261 C  C     . VAL A 1 3866 ? 68.306  96.139  62.194  1.00 5.01   ? 3866 VAL A C     1 
ATOM   17262 O  O     . VAL A 1 3866 ? 68.430  95.651  63.325  1.00 4.92   ? 3866 VAL A O     1 
ATOM   17263 C  CB    . VAL A 1 3866 ? 67.007  94.780  60.491  1.00 6.04   ? 3866 VAL A CB    1 
ATOM   17264 C  CG1   . VAL A 1 3866 ? 67.414  93.525  61.246  1.00 6.34   ? 3866 VAL A CG1   1 
ATOM   17265 C  CG2   . VAL A 1 3866 ? 65.638  94.592  59.858  1.00 5.77   ? 3866 VAL A CG2   1 
ATOM   17266 N  N     . ALA A 1 3867 ? 69.307  96.795  61.597  1.00 3.84   ? 3867 ALA A N     1 
ATOM   17267 C  CA    . ALA A 1 3867 ? 70.557  97.022  62.309  1.00 4.02   ? 3867 ALA A CA    1 
ATOM   17268 C  C     . ALA A 1 3867 ? 70.312  97.815  63.583  1.00 5.12   ? 3867 ALA A C     1 
ATOM   17269 O  O     . ALA A 1 3867 ? 70.771  97.429  64.666  1.00 5.89   ? 3867 ALA A O     1 
ATOM   17270 C  CB    . ALA A 1 3867 ? 71.555  97.742  61.402  1.00 4.41   ? 3867 ALA A CB    1 
ATOM   17271 N  N     . PHE A 1 3868 ? 69.558  98.915  63.479  1.00 4.38   ? 3868 PHE A N     1 
ATOM   17272 C  CA    . PHE A 1 3868 ? 69.246  99.687  64.675  1.00 3.73   ? 3868 PHE A CA    1 
ATOM   17273 C  C     . PHE A 1 3868 ? 68.469  98.858  65.684  1.00 4.49   ? 3868 PHE A C     1 
ATOM   17274 O  O     . PHE A 1 3868 ? 68.782  98.879  66.877  1.00 4.54   ? 3868 PHE A O     1 
ATOM   17275 C  CB    . PHE A 1 3868 ? 68.460  100.947 64.329  1.00 3.43   ? 3868 PHE A CB    1 
ATOM   17276 C  CG    . PHE A 1 3868 ? 68.112  101.779 65.530  1.00 3.68   ? 3868 PHE A CG    1 
ATOM   17277 C  CD1   . PHE A 1 3868 ? 69.066  102.578 66.135  1.00 4.32   ? 3868 PHE A CD1   1 
ATOM   17278 C  CD2   . PHE A 1 3868 ? 66.836  101.744 66.067  1.00 3.49   ? 3868 PHE A CD2   1 
ATOM   17279 C  CE1   . PHE A 1 3868 ? 68.752  103.334 67.247  1.00 4.40   ? 3868 PHE A CE1   1 
ATOM   17280 C  CE2   . PHE A 1 3868 ? 66.516  102.499 67.178  1.00 4.64   ? 3868 PHE A CE2   1 
ATOM   17281 C  CZ    . PHE A 1 3868 ? 67.475  103.294 67.768  1.00 5.45   ? 3868 PHE A CZ    1 
ATOM   17282 N  N     . ASN A 1 3869 ? 67.456  98.118  65.229  1.00 4.62   ? 3869 ASN A N     1 
ATOM   17283 C  CA    . ASN A 1 3869 ? 66.632  97.358  66.164  1.00 4.63   ? 3869 ASN A CA    1 
ATOM   17284 C  C     . ASN A 1 3869 ? 67.472  96.357  66.947  1.00 6.95   ? 3869 ASN A C     1 
ATOM   17285 O  O     . ASN A 1 3869 ? 67.477  96.363  68.187  1.00 9.54   ? 3869 ASN A O     1 
ATOM   17286 C  CB    . ASN A 1 3869 ? 65.510  96.645  65.409  1.00 4.77   ? 3869 ASN A CB    1 
ATOM   17287 C  CG    . ASN A 1 3869 ? 64.404  97.587  64.987  1.00 8.22   ? 3869 ASN A CG    1 
ATOM   17288 O  OD1   . ASN A 1 3869 ? 64.395  98.759  65.360  1.00 10.16  ? 3869 ASN A OD1   1 
ATOM   17289 N  ND2   . ASN A 1 3869 ? 63.462  97.078  64.202  1.00 7.88   ? 3869 ASN A ND2   1 
ATOM   17290 N  N     . ARG A 1 3870 ? 68.232  95.521  66.238  1.00 5.17   ? 3870 ARG A N     1 
ATOM   17291 C  CA    . ARG A 1 3870 ? 68.987  94.467  66.901  1.00 5.30   ? 3870 ARG A CA    1 
ATOM   17292 C  C     . ARG A 1 3870 ? 70.138  95.011  67.737  1.00 5.91   ? 3870 ARG A C     1 
ATOM   17293 O  O     . ARG A 1 3870 ? 70.432  94.454  68.800  1.00 9.71   ? 3870 ARG A O     1 
ATOM   17294 C  CB    . ARG A 1 3870 ? 69.506  93.460  65.875  1.00 6.73   ? 3870 ARG A CB    1 
ATOM   17295 C  CG    . ARG A 1 3870 ? 68.407  92.792  65.069  1.00 7.11   ? 3870 ARG A CG    1 
ATOM   17296 C  CD    . ARG A 1 3870 ? 68.899  91.506  64.434  1.00 9.88   ? 3870 ARG A CD    1 
ATOM   17297 N  NE    . ARG A 1 3870 ? 67.836  90.799  63.731  1.00 15.54  ? 3870 ARG A NE    1 
ATOM   17298 C  CZ    . ARG A 1 3870 ? 67.984  89.619  63.146  1.00 18.36  ? 3870 ARG A CZ    1 
ATOM   17299 N  NH1   . ARG A 1 3870 ? 69.144  88.984  63.155  1.00 14.79  ? 3870 ARG A NH1   1 
ATOM   17300 N  NH2   . ARG A 1 3870 ? 66.941  89.060  62.539  1.00 22.64  ? 3870 ARG A NH2   1 
ATOM   17301 N  N     . VAL A 1 3871 ? 70.805  96.079  67.293  1.00 4.93   ? 3871 VAL A N     1 
ATOM   17302 C  CA    . VAL A 1 3871 ? 71.899  96.618  68.091  1.00 5.37   ? 3871 VAL A CA    1 
ATOM   17303 C  C     . VAL A 1 3871 ? 71.364  97.334  69.328  1.00 5.44   ? 3871 VAL A C     1 
ATOM   17304 O  O     . VAL A 1 3871 ? 71.884  97.155  70.435  1.00 5.35   ? 3871 VAL A O     1 
ATOM   17305 C  CB    . VAL A 1 3871 ? 72.787  97.533  67.229  1.00 4.29   ? 3871 VAL A CB    1 
ATOM   17306 C  CG1   . VAL A 1 3871 ? 73.768  98.293  68.095  1.00 3.88   ? 3871 VAL A CG1   1 
ATOM   17307 C  CG2   . VAL A 1 3871 ? 73.527  96.716  66.182  1.00 4.61   ? 3871 VAL A CG2   1 
ATOM   17308 N  N     . ALA A 1 3872 ? 70.304  98.136  69.170  1.00 5.21   ? 3872 ALA A N     1 
ATOM   17309 C  CA    . ALA A 1 3872 ? 69.774  98.918  70.278  1.00 4.52   ? 3872 ALA A CA    1 
ATOM   17310 C  C     . ALA A 1 3872 ? 69.030  98.068  71.297  1.00 5.74   ? 3872 ALA A C     1 
ATOM   17311 O  O     . ALA A 1 3872 ? 68.885  98.499  72.446  1.00 4.72   ? 3872 ALA A O     1 
ATOM   17312 C  CB    . ALA A 1 3872 ? 68.852  100.020 69.751  1.00 4.48   ? 3872 ALA A CB    1 
ATOM   17313 N  N     . ARG A 1 3873 ? 68.545  96.881  70.915  1.00 8.45   ? 3873 ARG A N     1 
ATOM   17314 C  CA    . ARG A 1 3873 ? 68.007  95.982  71.933  1.00 6.72   ? 3873 ARG A CA    1 
ATOM   17315 C  C     . ARG A 1 3873 ? 69.074  95.578  72.944  1.00 6.76   ? 3873 ARG A C     1 
ATOM   17316 O  O     . ARG A 1 3873 ? 68.745  95.230  74.083  1.00 6.66   ? 3873 ARG A O     1 
ATOM   17317 C  CB    . ARG A 1 3873 ? 67.385  94.745  71.287  1.00 9.47   ? 3873 ARG A CB    1 
ATOM   17318 C  CG    . ARG A 1 3873 ? 66.048  95.006  70.613  1.00 16.59  ? 3873 ARG A CG    1 
ATOM   17319 C  CD    . ARG A 1 3873 ? 65.082  95.695  71.565  1.00 19.56  ? 3873 ARG A CD    1 
ATOM   17320 N  NE    . ARG A 1 3873 ? 63.701  95.610  71.107  1.00 27.16  ? 3873 ARG A NE    1 
ATOM   17321 C  CZ    . ARG A 1 3873 ? 62.672  96.177  71.723  1.00 26.53  ? 3873 ARG A CZ    1 
ATOM   17322 N  NH1   . ARG A 1 3873 ? 62.833  96.888  72.827  1.00 21.62  ? 3873 ARG A NH1   1 
ATOM   17323 N  NH2   . ARG A 1 3873 ? 61.450  96.026  71.218  1.00 26.07  ? 3873 ARG A NH2   1 
ATOM   17324 N  N     . GLY A 1 3874 ? 70.346  95.620  72.553  1.00 4.43   ? 3874 GLY A N     1 
ATOM   17325 C  CA    . GLY A 1 3874 ? 71.432  95.324  73.466  1.00 3.61   ? 3874 GLY A CA    1 
ATOM   17326 C  C     . GLY A 1 3874 ? 72.235  96.544  73.870  1.00 4.47   ? 3874 GLY A C     1 
ATOM   17327 O  O     . GLY A 1 3874 ? 73.429  96.438  74.163  1.00 6.33   ? 3874 GLY A O     1 
ATOM   17328 N  N     . MET A 1 3875 ? 71.591  97.708  73.892  1.00 5.91   ? 3875 MET A N     1 
ATOM   17329 C  CA    . MET A 1 3875 ? 72.236  98.954  74.280  1.00 4.32   ? 3875 MET A CA    1 
ATOM   17330 C  C     . MET A 1 3875 ? 71.426  99.639  75.369  1.00 4.13   ? 3875 MET A C     1 
ATOM   17331 O  O     . MET A 1 3875 ? 70.212  99.449  75.475  1.00 4.43   ? 3875 MET A O     1 
ATOM   17332 C  CB    . MET A 1 3875 ? 72.390  99.917  73.093  1.00 4.40   ? 3875 MET A CB    1 
ATOM   17333 C  CG    . MET A 1 3875 ? 73.345  99.456  72.012  1.00 6.42   ? 3875 MET A CG    1 
ATOM   17334 S  SD    . MET A 1 3875 ? 73.389  100.612 70.628  1.00 14.83  ? 3875 MET A SD    1 
ATOM   17335 C  CE    . MET A 1 3875 ? 74.236  102.004 71.364  1.00 7.74   ? 3875 MET A CE    1 
ATOM   17336 N  N     . LEU A 1 3876 ? 72.115  100.432 76.185  1.00 5.83   ? 3876 LEU A N     1 
ATOM   17337 C  CA    . LEU A 1 3876 ? 71.422  101.328 77.098  1.00 6.69   ? 3876 LEU A CA    1 
ATOM   17338 C  C     . LEU A 1 3876 ? 70.631  102.355 76.300  1.00 7.95   ? 3876 LEU A C     1 
ATOM   17339 O  O     . LEU A 1 3876 ? 71.099  102.862 75.277  1.00 7.57   ? 3876 LEU A O     1 
ATOM   17340 C  CB    . LEU A 1 3876 ? 72.414  102.027 78.027  1.00 8.30   ? 3876 LEU A CB    1 
ATOM   17341 C  CG    . LEU A 1 3876 ? 73.163  101.144 79.026  1.00 9.96   ? 3876 LEU A CG    1 
ATOM   17342 C  CD1   . LEU A 1 3876 ? 74.202  101.953 79.785  1.00 10.22  ? 3876 LEU A CD1   1 
ATOM   17343 C  CD2   . LEU A 1 3876 ? 72.193  100.474 79.987  1.00 9.07   ? 3876 LEU A CD2   1 
ATOM   17344 N  N     . HIS A 1 3877 ? 69.419  102.655 76.775  1.00 7.23   ? 3877 HIS A N     1 
ATOM   17345 C  CA    . HIS A 1 3877 ? 68.525  103.543 76.038  1.00 7.59   ? 3877 HIS A CA    1 
ATOM   17346 C  C     . HIS A 1 3877 ? 69.169  104.896 75.765  1.00 8.15   ? 3877 HIS A C     1 
ATOM   17347 O  O     . HIS A 1 3877 ? 68.993  105.458 74.676  1.00 8.28   ? 3877 HIS A O     1 
ATOM   17348 C  CB    . HIS A 1 3877 ? 67.218  103.719 76.812  1.00 7.64   ? 3877 HIS A CB    1 
ATOM   17349 C  CG    . HIS A 1 3877 ? 66.159  104.452 76.052  1.00 8.77   ? 3877 HIS A CG    1 
ATOM   17350 N  ND1   . HIS A 1 3877 ? 65.998  105.819 76.129  1.00 8.65   ? 3877 HIS A ND1   1 
ATOM   17351 C  CD2   . HIS A 1 3877 ? 65.204  104.008 75.201  1.00 11.66  ? 3877 HIS A CD2   1 
ATOM   17352 C  CE1   . HIS A 1 3877 ? 64.991  106.185 75.357  1.00 10.95  ? 3877 HIS A CE1   1 
ATOM   17353 N  NE2   . HIS A 1 3877 ? 64.492  105.106 74.783  1.00 13.38  ? 3877 HIS A NE2   1 
ATOM   17354 N  N     . GLN A 1 3878 ? 69.938  105.418 76.725  1.00 8.52   ? 3878 GLN A N     1 
ATOM   17355 C  CA    . GLN A 1 3878 ? 70.561  106.728 76.565  1.00 10.92  ? 3878 GLN A CA    1 
ATOM   17356 C  C     . GLN A 1 3878 ? 71.468  106.784 75.342  1.00 11.39  ? 3878 GLN A C     1 
ATOM   17357 O  O     . GLN A 1 3878 ? 71.617  107.848 74.730  1.00 13.74  ? 3878 GLN A O     1 
ATOM   17358 C  CB    . GLN A 1 3878 ? 71.347  107.088 77.827  1.00 12.00  ? 3878 GLN A CB    1 
ATOM   17359 C  CG    . GLN A 1 3878 ? 72.532  106.174 78.101  1.00 15.53  ? 3878 GLN A CG    1 
ATOM   17360 C  CD    . GLN A 1 3878 ? 73.254  106.517 79.388  1.00 25.72  ? 3878 GLN A CD    1 
ATOM   17361 O  OE1   . GLN A 1 3878 ? 72.908  107.479 80.071  1.00 35.15  ? 3878 GLN A OE1   1 
ATOM   17362 N  NE2   . GLN A 1 3878 ? 74.268  105.728 79.724  1.00 25.29  ? 3878 GLN A NE2   1 
ATOM   17363 N  N     . ASP A 1 3879 ? 72.075  105.661 74.967  1.00 9.34   ? 3879 ASP A N     1 
ATOM   17364 C  CA    . ASP A 1 3879 ? 72.967  105.610 73.819  1.00 9.42   ? 3879 ASP A CA    1 
ATOM   17365 C  C     . ASP A 1 3879 ? 72.234  105.419 72.497  1.00 9.73   ? 3879 ASP A C     1 
ATOM   17366 O  O     . ASP A 1 3879 ? 72.834  105.655 71.441  1.00 10.07  ? 3879 ASP A O     1 
ATOM   17367 C  CB    . ASP A 1 3879 ? 73.993  104.488 74.000  1.00 8.45   ? 3879 ASP A CB    1 
ATOM   17368 C  CG    . ASP A 1 3879 ? 74.918  104.730 75.172  1.00 16.19  ? 3879 ASP A CG    1 
ATOM   17369 O  OD1   . ASP A 1 3879 ? 75.547  105.806 75.218  1.00 20.76  ? 3879 ASP A OD1   1 
ATOM   17370 O  OD2   . ASP A 1 3879 ? 75.021  103.844 76.046  1.00 19.23  ? 3879 ASP A OD2   1 
ATOM   17371 N  N     . HIS A 1 3880 ? 70.952  105.034 72.532  1.00 6.64   ? 3880 HIS A N     1 
ATOM   17372 C  CA    . HIS A 1 3880 ? 70.244  104.691 71.300  1.00 6.31   ? 3880 HIS A CA    1 
ATOM   17373 C  C     . HIS A 1 3880 ? 70.336  105.811 70.274  1.00 7.60   ? 3880 HIS A C     1 
ATOM   17374 O  O     . HIS A 1 3880 ? 70.774  105.585 69.137  1.00 7.24   ? 3880 HIS A O     1 
ATOM   17375 C  CB    . HIS A 1 3880 ? 68.781  104.371 71.603  1.00 5.49   ? 3880 HIS A CB    1 
ATOM   17376 C  CG    . HIS A 1 3880 ? 68.582  103.081 72.336  1.00 6.66   ? 3880 HIS A CG    1 
ATOM   17377 N  ND1   . HIS A 1 3880 ? 67.334  102.554 72.586  1.00 5.41   ? 3880 HIS A ND1   1 
ATOM   17378 C  CD2   . HIS A 1 3880 ? 69.472  102.206 72.859  1.00 4.81   ? 3880 HIS A CD2   1 
ATOM   17379 C  CE1   . HIS A 1 3880 ? 67.463  101.414 73.241  1.00 6.41   ? 3880 HIS A CE1   1 
ATOM   17380 N  NE2   . HIS A 1 3880 ? 68.750  101.181 73.420  1.00 5.25   ? 3880 HIS A NE2   1 
ATOM   17381 N  N     . ILE A 1 3881 ? 69.989  107.036 70.678  1.00 7.71   ? 3881 ILE A N     1 
ATOM   17382 C  CA    . ILE A 1 3881 ? 70.012  108.165 69.755  1.00 9.03   ? 3881 ILE A CA    1 
ATOM   17383 C  C     . ILE A 1 3881 ? 71.378  108.290 69.101  1.00 7.88   ? 3881 ILE A C     1 
ATOM   17384 O  O     . ILE A 1 3881 ? 71.471  108.458 67.877  1.00 9.11   ? 3881 ILE A O     1 
ATOM   17385 C  CB    . ILE A 1 3881 ? 69.587  109.464 70.478  1.00 8.94   ? 3881 ILE A CB    1 
ATOM   17386 C  CG1   . ILE A 1 3881 ? 69.439  110.619 69.482  1.00 8.54   ? 3881 ILE A CG1   1 
ATOM   17387 C  CG2   . ILE A 1 3881 ? 70.538  109.819 71.621  1.00 7.64   ? 3881 ILE A CG2   1 
ATOM   17388 C  CD1   . ILE A 1 3881 ? 68.466  110.343 68.362  1.00 6.60   ? 3881 ILE A CD1   1 
ATOM   17389 N  N     . THR A 1 3882 ? 72.455  108.138 69.881  1.00 6.99   ? 3882 THR A N     1 
ATOM   17390 C  CA    . THR A 1 3882 ? 73.792  108.233 69.310  1.00 7.23   ? 3882 THR A CA    1 
ATOM   17391 C  C     . THR A 1 3882 ? 73.943  107.267 68.146  1.00 6.10   ? 3882 THR A C     1 
ATOM   17392 O  O     . THR A 1 3882 ? 74.270  107.677 67.024  1.00 7.60   ? 3882 THR A O     1 
ATOM   17393 C  CB    . THR A 1 3882 ? 74.846  107.957 70.382  1.00 9.32   ? 3882 THR A CB    1 
ATOM   17394 O  OG1   . THR A 1 3882 ? 74.721  108.918 71.437  1.00 14.60  ? 3882 THR A OG1   1 
ATOM   17395 C  CG2   . THR A 1 3882 ? 76.239  108.051 69.788  1.00 7.55   ? 3882 THR A CG2   1 
ATOM   17396 N  N     . PHE A 1 3883 ? 73.622  105.989 68.376  1.00 5.62   ? 3883 PHE A N     1 
ATOM   17397 C  CA    . PHE A 1 3883 ? 73.672  105.022 67.287  1.00 5.14   ? 3883 PHE A CA    1 
ATOM   17398 C  C     . PHE A 1 3883 ? 72.801  105.478 66.130  1.00 5.11   ? 3883 PHE A C     1 
ATOM   17399 O  O     . PHE A 1 3883 ? 73.266  105.552 64.984  1.00 6.25   ? 3883 PHE A O     1 
ATOM   17400 C  CB    . PHE A 1 3883 ? 73.233  103.642 67.774  1.00 4.63   ? 3883 PHE A CB    1 
ATOM   17401 C  CG    . PHE A 1 3883 ? 73.431  102.556 66.758  1.00 3.64   ? 3883 PHE A CG    1 
ATOM   17402 C  CD1   . PHE A 1 3883 ? 74.587  102.503 65.997  1.00 4.20   ? 3883 PHE A CD1   1 
ATOM   17403 C  CD2   . PHE A 1 3883 ? 72.451  101.603 66.543  1.00 4.13   ? 3883 PHE A CD2   1 
ATOM   17404 C  CE1   . PHE A 1 3883 ? 74.769  101.510 65.054  1.00 4.06   ? 3883 PHE A CE1   1 
ATOM   17405 C  CE2   . PHE A 1 3883 ? 72.627  100.608 65.600  1.00 3.50   ? 3883 PHE A CE2   1 
ATOM   17406 C  CZ    . PHE A 1 3883 ? 73.788  100.561 64.856  1.00 3.15   ? 3883 PHE A CZ    1 
ATOM   17407 N  N     . ALA A 1 3884 ? 71.553  105.856 66.425  1.00 5.38   ? 3884 ALA A N     1 
ATOM   17408 C  CA    . ALA A 1 3884 ? 70.666  106.335 65.374  1.00 5.09   ? 3884 ALA A CA    1 
ATOM   17409 C  C     . ALA A 1 3884 ? 71.315  107.480 64.618  1.00 5.65   ? 3884 ALA A C     1 
ATOM   17410 O  O     . ALA A 1 3884 ? 71.352  107.474 63.380  1.00 6.65   ? 3884 ALA A O     1 
ATOM   17411 C  CB    . ALA A 1 3884 ? 69.326  106.765 65.968  1.00 5.41   ? 3884 ALA A CB    1 
ATOM   17412 N  N     . MET A 1 3885 ? 71.908  108.426 65.354  1.00 4.94   ? 3885 MET A N     1 
ATOM   17413 C  CA    . MET A 1 3885 ? 72.575  109.553 64.715  1.00 5.53   ? 3885 MET A CA    1 
ATOM   17414 C  C     . MET A 1 3885 ? 73.566  109.056 63.677  1.00 9.50   ? 3885 MET A C     1 
ATOM   17415 O  O     . MET A 1 3885 ? 73.484  109.422 62.496  1.00 13.27  ? 3885 MET A O     1 
ATOM   17416 C  CB    . MET A 1 3885 ? 73.279  110.405 65.772  1.00 8.11   ? 3885 MET A CB    1 
ATOM   17417 C  CG    . MET A 1 3885 ? 72.366  111.336 66.551  1.00 10.99  ? 3885 MET A CG    1 
ATOM   17418 S  SD    . MET A 1 3885 ? 71.440  112.466 65.500  1.00 21.97  ? 3885 MET A SD    1 
ATOM   17419 C  CE    . MET A 1 3885 ? 72.747  113.581 64.994  1.00 15.74  ? 3885 MET A CE    1 
ATOM   17420 N  N     . LEU A 1 3886 ? 74.448  108.137 64.082  1.00 6.91   ? 3886 LEU A N     1 
ATOM   17421 C  CA    . LEU A 1 3886 ? 75.455  107.640 63.156  1.00 7.49   ? 3886 LEU A CA    1 
ATOM   17422 C  C     . LEU A 1 3886 ? 74.798  107.001 61.945  1.00 9.63   ? 3886 LEU A C     1 
ATOM   17423 O  O     . LEU A 1 3886 ? 75.170  107.301 60.802  1.00 16.95  ? 3886 LEU A O     1 
ATOM   17424 C  CB    . LEU A 1 3886 ? 76.379  106.654 63.864  1.00 7.94   ? 3886 LEU A CB    1 
ATOM   17425 C  CG    . LEU A 1 3886 ? 77.154  107.248 65.040  1.00 8.07   ? 3886 LEU A CG    1 
ATOM   17426 C  CD1   . LEU A 1 3886 ? 77.736  106.148 65.900  1.00 10.34  ? 3886 LEU A CD1   1 
ATOM   17427 C  CD2   . LEU A 1 3886 ? 78.246  108.183 64.546  1.00 7.38   ? 3886 LEU A CD2   1 
ATOM   17428 N  N     . LEU A 1 3887 ? 73.769  106.179 62.172  1.00 6.51   ? 3887 LEU A N     1 
ATOM   17429 C  CA    . LEU A 1 3887 ? 73.089  105.554 61.047  1.00 7.91   ? 3887 LEU A CA    1 
ATOM   17430 C  C     . LEU A 1 3887 ? 72.550  106.614 60.103  1.00 9.36   ? 3887 LEU A C     1 
ATOM   17431 O  O     . LEU A 1 3887 ? 72.771  106.541 58.886  1.00 11.49  ? 3887 LEU A O     1 
ATOM   17432 C  CB    . LEU A 1 3887 ? 71.970  104.640 61.543  1.00 5.90   ? 3887 LEU A CB    1 
ATOM   17433 C  CG    . LEU A 1 3887 ? 72.429  103.417 62.340  1.00 4.97   ? 3887 LEU A CG    1 
ATOM   17434 C  CD1   . LEU A 1 3887 ? 71.239  102.589 62.784  1.00 4.69   ? 3887 LEU A CD1   1 
ATOM   17435 C  CD2   . LEU A 1 3887 ? 73.396  102.574 61.524  1.00 4.56   ? 3887 LEU A CD2   1 
ATOM   17436 N  N     . ALA A 1 3888 ? 71.914  107.652 60.657  1.00 9.27   ? 3888 ALA A N     1 
ATOM   17437 C  CA    . ALA A 1 3888 ? 71.417  108.730 59.814  1.00 9.99   ? 3888 ALA A CA    1 
ATOM   17438 C  C     . ALA A 1 3888 ? 72.547  109.319 58.988  1.00 9.78   ? 3888 ALA A C     1 
ATOM   17439 O  O     . ALA A 1 3888 ? 72.430  109.446 57.762  1.00 14.84  ? 3888 ALA A O     1 
ATOM   17440 C  CB    . ALA A 1 3888 ? 70.752  109.807 60.670  1.00 11.45  ? 3888 ALA A CB    1 
ATOM   17441 N  N     . ARG A 1 3889 ? 73.682  109.600 59.633  1.00 9.42   ? 3889 ARG A N     1 
ATOM   17442 C  CA    . ARG A 1 3889 ? 74.811  110.168 58.909  1.00 11.84  ? 3889 ARG A CA    1 
ATOM   17443 C  C     . ARG A 1 3889 ? 75.262  109.228 57.803  1.00 13.52  ? 3889 ARG A C     1 
ATOM   17444 O  O     . ARG A 1 3889 ? 75.536  109.667 56.679  1.00 18.04  ? 3889 ARG A O     1 
ATOM   17445 C  CB    . ARG A 1 3889 ? 75.953  110.471 59.877  1.00 12.78  ? 3889 ARG A CB    1 
ATOM   17446 C  CG    . ARG A 1 3889 ? 75.639  111.605 60.841  1.00 17.50  ? 3889 ARG A CG    1 
ATOM   17447 C  CD    . ARG A 1 3889 ? 76.866  112.437 61.169  1.00 23.54  ? 3889 ARG A CD    1 
ATOM   17448 N  NE    . ARG A 1 3889 ? 77.618  112.819 59.980  1.00 30.83  ? 3889 ARG A NE    1 
ATOM   17449 C  CZ    . ARG A 1 3889 ? 78.892  113.185 59.988  1.00 31.37  ? 3889 ARG A CZ    1 
ATOM   17450 N  NH1   . ARG A 1 3889 ? 79.591  113.229 61.111  1.00 25.68  ? 3889 ARG A NH1   1 
ATOM   17451 N  NH2   . ARG A 1 3889 ? 79.479  113.517 58.842  1.00 31.26  ? 3889 ARG A NH2   1 
ATOM   17452 N  N     . ILE A 1 3890 ? 75.291  107.922 58.084  1.00 11.58  ? 3890 ILE A N     1 
ATOM   17453 C  CA    . ILE A 1 3890 ? 75.633  106.967 57.038  1.00 12.60  ? 3890 ILE A CA    1 
ATOM   17454 C  C     . ILE A 1 3890 ? 74.607  107.036 55.918  1.00 13.23  ? 3890 ILE A C     1 
ATOM   17455 O  O     . ILE A 1 3890 ? 74.962  107.149 54.737  1.00 16.65  ? 3890 ILE A O     1 
ATOM   17456 C  CB    . ILE A 1 3890 ? 75.753  105.547 57.621  1.00 11.33  ? 3890 ILE A CB    1 
ATOM   17457 C  CG1   . ILE A 1 3890 ? 76.910  105.479 58.618  1.00 10.28  ? 3890 ILE A CG1   1 
ATOM   17458 C  CG2   . ILE A 1 3890 ? 75.954  104.532 56.509  1.00 8.51   ? 3890 ILE A CG2   1 
ATOM   17459 C  CD1   . ILE A 1 3890 ? 77.038  104.145 59.319  1.00 7.31   ? 3890 ILE A CD1   1 
ATOM   17460 N  N     . LYS A 1 3891 ? 73.319  107.031 56.272  1.00 12.62  ? 3891 LYS A N     1 
ATOM   17461 C  CA    . LYS A 1 3891 ? 72.291  107.163 55.247  1.00 15.22  ? 3891 LYS A CA    1 
ATOM   17462 C  C     . LYS A 1 3891 ? 72.359  108.535 54.597  1.00 21.72  ? 3891 LYS A C     1 
ATOM   17463 O  O     . LYS A 1 3891 ? 71.904  108.720 53.462  1.00 23.73  ? 3891 LYS A O     1 
ATOM   17464 C  CB    . LYS A 1 3891 ? 70.905  106.916 55.841  1.00 15.57  ? 3891 LYS A CB    1 
ATOM   17465 C  CG    . LYS A 1 3891 ? 69.843  106.620 54.793  1.00 14.98  ? 3891 LYS A CG    1 
ATOM   17466 C  CD    . LYS A 1 3891 ? 68.456  107.000 55.274  1.00 20.67  ? 3891 LYS A CD    1 
ATOM   17467 C  CE    . LYS A 1 3891 ? 67.402  106.669 54.229  1.00 21.56  ? 3891 LYS A CE    1 
ATOM   17468 N  NZ    . LYS A 1 3891 ? 66.033  106.638 54.812  1.00 16.82  ? 3891 LYS A NZ    1 
ATOM   17469 N  N     . LEU A 1 3892 ? 72.932  109.512 55.302  1.00 20.64  ? 3892 LEU A N     1 
ATOM   17470 C  CA    . LEU A 1 3892 ? 73.098  110.832 54.712  1.00 21.34  ? 3892 LEU A CA    1 
ATOM   17471 C  C     . LEU A 1 3892 ? 74.194  110.813 53.655  1.00 28.10  ? 3892 LEU A C     1 
ATOM   17472 O  O     . LEU A 1 3892 ? 74.142  111.573 52.681  1.00 37.04  ? 3892 LEU A O     1 
ATOM   17473 C  CB    . LEU A 1 3892 ? 73.400  111.857 55.804  1.00 22.78  ? 3892 LEU A CB    1 
ATOM   17474 C  CG    . LEU A 1 3892 ? 73.402  113.322 55.374  1.00 26.39  ? 3892 LEU A CG    1 
ATOM   17475 C  CD1   . LEU A 1 3892 ? 72.152  113.619 54.564  1.00 25.25  ? 3892 LEU A CD1   1 
ATOM   17476 C  CD2   . LEU A 1 3892 ? 73.481  114.233 56.583  1.00 24.64  ? 3892 LEU A CD2   1 
ATOM   17477 N  N     . LYS A 1 3893 ? 75.196  109.944 53.827  1.00 29.33  ? 3893 LYS A N     1 
ATOM   17478 C  CA    . LYS A 1 3893 ? 76.260  109.849 52.833  1.00 26.69  ? 3893 LYS A CA    1 
ATOM   17479 C  C     . LYS A 1 3893 ? 75.807  109.087 51.595  1.00 30.26  ? 3893 LYS A C     1 
ATOM   17480 O  O     . LYS A 1 3893 ? 76.337  109.311 50.501  1.00 37.80  ? 3893 LYS A O     1 
ATOM   17481 C  CB    . LYS A 1 3893 ? 77.497  109.189 53.442  1.00 28.32  ? 3893 LYS A CB    1 
ATOM   17482 C  CG    . LYS A 1 3893 ? 78.209  110.046 54.474  1.00 33.73  ? 3893 LYS A CG    1 
ATOM   17483 C  CD    . LYS A 1 3893 ? 79.343  109.283 55.136  1.00 40.46  ? 3893 LYS A CD    1 
ATOM   17484 C  CE    . LYS A 1 3893 ? 80.495  109.063 54.168  1.00 41.98  ? 3893 LYS A CE    1 
ATOM   17485 N  NZ    . LYS A 1 3893 ? 81.662  108.418 54.830  1.00 45.11  ? 3893 LYS A NZ    1 
ATOM   17486 N  N     . GLY A 1 3894 ? 74.836  108.189 51.742  1.00 30.67  ? 3894 GLY A N     1 
ATOM   17487 C  CA    . GLY A 1 3894 ? 74.351  107.397 50.633  1.00 29.98  ? 3894 GLY A CA    1 
ATOM   17488 C  C     . GLY A 1 3894 ? 73.378  108.089 49.710  1.00 40.23  ? 3894 GLY A C     1 
ATOM   17489 O  O     . GLY A 1 3894 ? 72.943  107.488 48.724  1.00 45.04  ? 3894 GLY A O     1 
ATOM   17490 N  N     . THR A 1 3895 ? 73.018  109.337 49.996  1.00 46.79  ? 3895 THR A N     1 
ATOM   17491 C  CA    . THR A 1 3895 ? 72.100  110.093 49.154  1.00 50.27  ? 3895 THR A CA    1 
ATOM   17492 C  C     . THR A 1 3895 ? 72.905  110.925 48.162  1.00 54.22  ? 3895 THR A C     1 
ATOM   17493 O  O     . THR A 1 3895 ? 73.733  111.750 48.563  1.00 51.38  ? 3895 THR A O     1 
ATOM   17494 C  CB    . THR A 1 3895 ? 71.197  110.990 50.000  1.00 49.68  ? 3895 THR A CB    1 
ATOM   17495 O  OG1   . THR A 1 3895 ? 70.460  110.187 50.930  1.00 46.14  ? 3895 THR A OG1   1 
ATOM   17496 C  CG2   . THR A 1 3895 ? 70.220  111.741 49.110  1.00 52.41  ? 3895 THR A CG2   1 
ATOM   17497 N  N     . VAL A 1 3896 ? 72.661  110.705 46.869  1.00 63.11  ? 3896 VAL A N     1 
ATOM   17498 C  CA    . VAL A 1 3896 ? 73.414  111.410 45.837  1.00 62.24  ? 3896 VAL A CA    1 
ATOM   17499 C  C     . VAL A 1 3896 ? 73.033  112.885 45.803  1.00 59.72  ? 3896 VAL A C     1 
ATOM   17500 O  O     . VAL A 1 3896 ? 73.890  113.758 45.622  1.00 59.81  ? 3896 VAL A O     1 
ATOM   17501 C  CB    . VAL A 1 3896 ? 73.199  110.736 44.469  1.00 61.94  ? 3896 VAL A CB    1 
ATOM   17502 C  CG1   . VAL A 1 3896 ? 74.006  111.445 43.391  1.00 62.56  ? 3896 VAL A CG1   1 
ATOM   17503 C  CG2   . VAL A 1 3896 ? 73.571  109.264 44.541  1.00 55.35  ? 3896 VAL A CG2   1 
ATOM   17504 N  N     . GLY A 1 3897 ? 71.751  113.189 45.986  1.00 58.08  ? 3897 GLY A N     1 
ATOM   17505 C  CA    . GLY A 1 3897 ? 71.263  114.548 45.887  1.00 59.90  ? 3897 GLY A CA    1 
ATOM   17506 C  C     . GLY A 1 3897 ? 71.511  115.430 47.087  1.00 57.41  ? 3897 GLY A C     1 
ATOM   17507 O  O     . GLY A 1 3897 ? 71.130  116.603 47.068  1.00 53.22  ? 3897 GLY A O     1 
ATOM   17508 N  N     . GLU A 1 3898 ? 72.140  114.904 48.140  1.00 57.31  ? 3898 GLU A N     1 
ATOM   17509 C  CA    . GLU A 1 3898 ? 72.382  115.732 49.308  1.00 49.30  ? 3898 GLU A CA    1 
ATOM   17510 C  C     . GLU A 1 3898 ? 73.848  116.150 49.375  1.00 46.65  ? 3898 GLU A C     1 
ATOM   17511 O  O     . GLU A 1 3898 ? 74.734  115.404 48.947  1.00 47.07  ? 3898 GLU A O     1 
ATOM   17512 C  CB    . GLU A 1 3898 ? 72.010  114.978 50.588  1.00 46.58  ? 3898 GLU A CB    1 
ATOM   17513 C  CG    . GLU A 1 3898 ? 70.513  114.891 50.859  1.00 44.05  ? 3898 GLU A CG    1 
ATOM   17514 C  CD    . GLU A 1 3898 ? 69.956  116.128 51.532  1.00 44.54  ? 3898 GLU A CD    1 
ATOM   17515 O  OE1   . GLU A 1 3898 ? 70.749  116.931 52.062  1.00 48.33  ? 3898 GLU A OE1   1 
ATOM   17516 O  OE2   . GLU A 1 3898 ? 68.718  116.291 51.538  1.00 47.02  ? 3898 GLU A OE2   1 
ATOM   17517 N  N     . PRO A 1 3899 ? 74.134  117.336 49.906  1.00 42.39  ? 3899 PRO A N     1 
ATOM   17518 C  CA    . PRO A 1 3899 ? 75.529  117.772 50.048  1.00 41.73  ? 3899 PRO A CA    1 
ATOM   17519 C  C     . PRO A 1 3899 ? 76.243  117.005 51.153  1.00 43.90  ? 3899 PRO A C     1 
ATOM   17520 O  O     . PRO A 1 3899 ? 75.701  116.093 51.777  1.00 45.88  ? 3899 PRO A O     1 
ATOM   17521 C  CB    . PRO A 1 3899 ? 75.415  119.263 50.386  1.00 38.22  ? 3899 PRO A CB    1 
ATOM   17522 C  CG    . PRO A 1 3899 ? 74.008  119.644 50.040  1.00 41.11  ? 3899 PRO A CG    1 
ATOM   17523 C  CD    . PRO A 1 3899 ? 73.184  118.413 50.219  1.00 39.41  ? 3899 PRO A CD    1 
ATOM   17524 N  N     . THR A 1 3900 ? 77.497  117.396 51.390  1.00 45.34  ? 3900 THR A N     1 
ATOM   17525 C  CA    . THR A 1 3900 ? 78.326  116.658 52.338  1.00 44.76  ? 3900 THR A CA    1 
ATOM   17526 C  C     . THR A 1 3900 ? 78.001  117.027 53.781  1.00 43.72  ? 3900 THR A C     1 
ATOM   17527 O  O     . THR A 1 3900 ? 77.984  116.154 54.657  1.00 40.45  ? 3900 THR A O     1 
ATOM   17528 C  CB    . THR A 1 3900 ? 79.806  116.903 52.047  1.00 44.14  ? 3900 THR A CB    1 
ATOM   17529 O  OG1   . THR A 1 3900 ? 80.101  118.297 52.199  1.00 46.07  ? 3900 THR A OG1   1 
ATOM   17530 C  CG2   . THR A 1 3900 ? 80.150  116.466 50.631  1.00 44.31  ? 3900 THR A CG2   1 
ATOM   17531 N  N     . TYR A 1 3901 ? 77.748  118.311 54.049  1.00 42.28  ? 3901 TYR A N     1 
ATOM   17532 C  CA    . TYR A 1 3901 ? 77.522  118.804 55.411  1.00 38.50  ? 3901 TYR A CA    1 
ATOM   17533 C  C     . TYR A 1 3901 ? 78.705  118.505 56.327  1.00 42.11  ? 3901 TYR A C     1 
ATOM   17534 O  O     . TYR A 1 3901 ? 78.538  118.303 57.532  1.00 45.90  ? 3901 TYR A O     1 
ATOM   17535 C  CB    . TYR A 1 3901 ? 76.226  118.240 55.998  1.00 35.04  ? 3901 TYR A CB    1 
ATOM   17536 C  CG    . TYR A 1 3901 ? 75.015  118.463 55.124  1.00 36.14  ? 3901 TYR A CG    1 
ATOM   17537 C  CD1   . TYR A 1 3901 ? 74.286  117.393 54.624  1.00 31.69  ? 3901 TYR A CD1   1 
ATOM   17538 C  CD2   . TYR A 1 3901 ? 74.569  119.748 54.845  1.00 34.74  ? 3901 TYR A CD2   1 
ATOM   17539 C  CE1   . TYR A 1 3901 ? 73.177  117.600 53.827  1.00 34.19  ? 3901 TYR A CE1   1 
ATOM   17540 C  CE2   . TYR A 1 3901 ? 73.454  119.965 54.064  1.00 28.12  ? 3901 TYR A CE2   1 
ATOM   17541 C  CZ    . TYR A 1 3901 ? 72.759  118.889 53.560  1.00 34.82  ? 3901 TYR A CZ    1 
ATOM   17542 O  OH    . TYR A 1 3901 ? 71.645  119.106 52.783  1.00 41.19  ? 3901 TYR A OH    1 
ATOM   17543 N  N     . ASP A 1 3902 ? 79.912  118.473 55.757  1.00 43.92  ? 3902 ASP A N     1 
ATOM   17544 C  CA    . ASP A 1 3902 ? 81.097  118.165 56.550  1.00 44.37  ? 3902 ASP A CA    1 
ATOM   17545 C  C     . ASP A 1 3902 ? 81.393  119.263 57.562  1.00 40.36  ? 3902 ASP A C     1 
ATOM   17546 O  O     . ASP A 1 3902 ? 81.715  118.975 58.719  1.00 40.88  ? 3902 ASP A O     1 
ATOM   17547 C  CB    . ASP A 1 3902 ? 82.298  117.940 55.632  1.00 51.30  ? 3902 ASP A CB    1 
ATOM   17548 C  CG    . ASP A 1 3902 ? 82.199  116.644 54.855  1.00 55.82  ? 3902 ASP A CG    1 
ATOM   17549 O  OD1   . ASP A 1 3902 ? 81.235  115.884 55.087  1.00 53.67  ? 3902 ASP A OD1   1 
ATOM   17550 O  OD2   . ASP A 1 3902 ? 83.084  116.383 54.014  1.00 61.60  ? 3902 ASP A OD2   1 
ATOM   17551 N  N     . ALA A 1 3903 ? 81.297  120.529 57.147  1.00 42.26  ? 3903 ALA A N     1 
ATOM   17552 C  CA    . ALA A 1 3903 ? 81.574  121.627 58.068  1.00 40.69  ? 3903 ALA A CA    1 
ATOM   17553 C  C     . ALA A 1 3903 ? 80.512  121.723 59.158  1.00 37.60  ? 3903 ALA A C     1 
ATOM   17554 O  O     . ALA A 1 3903 ? 80.833  121.989 60.324  1.00 37.00  ? 3903 ALA A O     1 
ATOM   17555 C  CB    . ALA A 1 3903 ? 81.677  122.945 57.301  1.00 37.21  ? 3903 ALA A CB    1 
ATOM   17556 N  N     . GLU A 1 3904 ? 79.243  121.519 58.800  1.00 37.13  ? 3904 GLU A N     1 
ATOM   17557 C  CA    . GLU A 1 3904 ? 78.177  121.607 59.792  1.00 35.89  ? 3904 GLU A CA    1 
ATOM   17558 C  C     . GLU A 1 3904 ? 78.289  120.507 60.844  1.00 34.71  ? 3904 GLU A C     1 
ATOM   17559 O  O     . GLU A 1 3904 ? 78.145  120.777 62.042  1.00 34.18  ? 3904 GLU A O     1 
ATOM   17560 C  CB    . GLU A 1 3904 ? 76.812  121.587 59.104  1.00 34.00  ? 3904 GLU A CB    1 
ATOM   17561 C  CG    . GLU A 1 3904 ? 76.518  122.827 58.257  1.00 39.29  ? 3904 GLU A CG    1 
ATOM   17562 C  CD    . GLU A 1 3904 ? 77.128  122.774 56.871  1.00 48.32  ? 3904 GLU A CD    1 
ATOM   17563 O  OE1   . GLU A 1 3904 ? 77.738  121.744 56.525  1.00 52.83  ? 3904 GLU A OE1   1 
ATOM   17564 O  OE2   . GLU A 1 3904 ? 76.992  123.766 56.123  1.00 44.28  ? 3904 GLU A OE2   1 
ATOM   17565 N  N     . PHE A 1 3905 ? 78.559  119.266 60.431  1.00 32.83  ? 3905 PHE A N     1 
ATOM   17566 C  CA    . PHE A 1 3905 ? 78.808  118.218 61.419  1.00 30.70  ? 3905 PHE A CA    1 
ATOM   17567 C  C     . PHE A 1 3905 ? 80.113  118.439 62.171  1.00 33.87  ? 3905 PHE A C     1 
ATOM   17568 O  O     . PHE A 1 3905 ? 80.217  118.071 63.347  1.00 34.22  ? 3905 PHE A O     1 
ATOM   17569 C  CB    . PHE A 1 3905 ? 78.817  116.839 60.762  1.00 30.40  ? 3905 PHE A CB    1 
ATOM   17570 C  CG    . PHE A 1 3905 ? 77.456  116.324 60.404  1.00 29.49  ? 3905 PHE A CG    1 
ATOM   17571 C  CD1   . PHE A 1 3905 ? 76.481  116.183 61.378  1.00 26.72  ? 3905 PHE A CD1   1 
ATOM   17572 C  CD2   . PHE A 1 3905 ? 77.157  115.954 59.105  1.00 32.27  ? 3905 PHE A CD2   1 
ATOM   17573 C  CE1   . PHE A 1 3905 ? 75.229  115.698 61.060  1.00 29.86  ? 3905 PHE A CE1   1 
ATOM   17574 C  CE2   . PHE A 1 3905 ? 75.908  115.468 58.782  1.00 26.17  ? 3905 PHE A CE2   1 
ATOM   17575 C  CZ    . PHE A 1 3905 ? 74.943  115.337 59.762  1.00 27.37  ? 3905 PHE A CZ    1 
ATOM   17576 N  N     . GLN A 1 3906 ? 81.119  119.019 61.516  1.00 35.53  ? 3906 GLN A N     1 
ATOM   17577 C  CA    . GLN A 1 3906 ? 82.400  119.242 62.174  1.00 37.36  ? 3906 GLN A CA    1 
ATOM   17578 C  C     . GLN A 1 3906 ? 82.269  120.262 63.295  1.00 35.35  ? 3906 GLN A C     1 
ATOM   17579 O  O     . GLN A 1 3906 ? 82.907  120.126 64.345  1.00 38.69  ? 3906 GLN A O     1 
ATOM   17580 C  CB    . GLN A 1 3906 ? 83.441  119.691 61.148  1.00 38.38  ? 3906 GLN A CB    1 
ATOM   17581 C  CG    . GLN A 1 3906 ? 84.832  119.955 61.712  1.00 42.57  ? 3906 GLN A CG    1 
ATOM   17582 C  CD    . GLN A 1 3906 ? 85.467  118.738 62.373  1.00 56.49  ? 3906 GLN A CD    1 
ATOM   17583 O  OE1   . GLN A 1 3906 ? 84.956  117.620 62.288  1.00 52.44  ? 3906 GLN A OE1   1 
ATOM   17584 N  NE2   . GLN A 1 3906 ? 86.592  118.958 63.038  1.00 56.82  ? 3906 GLN A NE2   1 
ATOM   17585 N  N     . HIS A 1 3907 ? 81.460  121.301 63.084  1.00 31.98  ? 3907 HIS A N     1 
ATOM   17586 C  CA    . HIS A 1 3907 ? 81.156  122.240 64.158  1.00 35.20  ? 3907 HIS A CA    1 
ATOM   17587 C  C     . HIS A 1 3907 ? 80.143  121.667 65.143  1.00 37.37  ? 3907 HIS A C     1 
ATOM   17588 O  O     . HIS A 1 3907 ? 80.119  122.080 66.308  1.00 38.08  ? 3907 HIS A O     1 
ATOM   17589 C  CB    . HIS A 1 3907 ? 80.656  123.561 63.575  1.00 38.32  ? 3907 HIS A CB    1 
ATOM   17590 C  CG    . HIS A 1 3907 ? 80.492  124.650 64.589  1.00 44.19  ? 3907 HIS A CG    1 
ATOM   17591 N  ND1   . HIS A 1 3907 ? 79.310  124.867 65.263  1.00 42.16  ? 3907 HIS A ND1   1 
ATOM   17592 C  CD2   . HIS A 1 3907 ? 81.360  125.584 65.042  1.00 46.68  ? 3907 HIS A CD2   1 
ATOM   17593 C  CE1   . HIS A 1 3907 ? 79.457  125.889 66.088  1.00 44.77  ? 3907 HIS A CE1   1 
ATOM   17594 N  NE2   . HIS A 1 3907 ? 80.692  126.341 65.974  1.00 48.77  ? 3907 HIS A NE2   1 
ATOM   17595 N  N     . PHE A 1 3908 ? 79.298  120.734 64.694  1.00 32.83  ? 3908 PHE A N     1 
ATOM   17596 C  CA    . PHE A 1 3908 ? 78.422  120.013 65.613  1.00 28.55  ? 3908 PHE A CA    1 
ATOM   17597 C  C     . PHE A 1 3908 ? 79.227  119.286 66.681  1.00 28.25  ? 3908 PHE A C     1 
ATOM   17598 O  O     . PHE A 1 3908 ? 78.954  119.423 67.879  1.00 27.25  ? 3908 PHE A O     1 
ATOM   17599 C  CB    . PHE A 1 3908 ? 77.549  119.029 64.834  1.00 29.51  ? 3908 PHE A CB    1 
ATOM   17600 C  CG    . PHE A 1 3908 ? 76.587  118.252 65.688  1.00 27.34  ? 3908 PHE A CG    1 
ATOM   17601 C  CD1   . PHE A 1 3908 ? 76.645  116.870 65.738  1.00 30.47  ? 3908 PHE A CD1   1 
ATOM   17602 C  CD2   . PHE A 1 3908 ? 75.634  118.900 66.447  1.00 22.91  ? 3908 PHE A CD2   1 
ATOM   17603 C  CE1   . PHE A 1 3908 ? 75.759  116.153 66.520  1.00 33.01  ? 3908 PHE A CE1   1 
ATOM   17604 C  CE2   . PHE A 1 3908 ? 74.748  118.191 67.235  1.00 23.67  ? 3908 PHE A CE2   1 
ATOM   17605 C  CZ    . PHE A 1 3908 ? 74.808  116.815 67.267  1.00 28.08  ? 3908 PHE A CZ    1 
ATOM   17606 N  N     . LEU A 1 3909 ? 80.223  118.511 66.266  1.00 31.29  ? 3909 LEU A N     1 
ATOM   17607 C  CA    . LEU A 1 3909 ? 81.175  117.942 67.201  1.00 32.31  ? 3909 LEU A CA    1 
ATOM   17608 C  C     . LEU A 1 3909 ? 82.233  118.984 67.551  1.00 43.77  ? 3909 LEU A C     1 
ATOM   17609 O  O     . LEU A 1 3909 ? 82.305  120.057 66.947  1.00 48.03  ? 3909 LEU A O     1 
ATOM   17610 C  CB    . LEU A 1 3909 ? 81.819  116.688 66.614  1.00 37.37  ? 3909 LEU A CB    1 
ATOM   17611 C  CG    . LEU A 1 3909 ? 80.849  115.561 66.255  1.00 34.12  ? 3909 LEU A CG    1 
ATOM   17612 C  CD1   . LEU A 1 3909 ? 81.607  114.311 65.845  1.00 37.03  ? 3909 LEU A CD1   1 
ATOM   17613 C  CD2   . LEU A 1 3909 ? 79.906  115.269 67.412  1.00 28.85  ? 3909 LEU A CD2   1 
ATOM   17614 N  N     . ARG A 1 3910 ? 83.059  118.658 68.546  1.00 46.08  ? 3910 ARG A N     1 
ATOM   17615 C  CA    . ARG A 1 3910 ? 84.084  119.580 69.027  1.00 59.79  ? 3910 ARG A CA    1 
ATOM   17616 C  C     . ARG A 1 3910 ? 83.469  120.942 69.327  1.00 63.85  ? 3910 ARG A C     1 
ATOM   17617 O  O     . ARG A 1 3910 ? 82.782  121.110 70.340  1.00 68.52  ? 3910 ARG A O     1 
ATOM   17618 C  CB    . ARG A 1 3910 ? 85.223  119.705 68.008  1.00 59.35  ? 3910 ARG A CB    1 
ATOM   17619 C  CG    . ARG A 1 3910 ? 85.948  118.393 67.739  1.00 56.94  ? 3910 ARG A CG    1 
ATOM   17620 C  CD    . ARG A 1 3910 ? 86.879  118.473 66.536  1.00 58.56  ? 3910 ARG A CD    1 
ATOM   17621 N  NE    . ARG A 1 3910 ? 87.742  119.647 66.582  1.00 77.75  ? 3910 ARG A NE    1 
ATOM   17622 C  CZ    . ARG A 1 3910 ? 88.694  119.914 65.698  1.00 74.95  ? 3910 ARG A CZ    1 
ATOM   17623 N  NH1   . ARG A 1 3910 ? 88.964  119.088 64.702  1.00 71.24  ? 3910 ARG A NH1   1 
ATOM   17624 N  NH2   . ARG A 1 3910 ? 89.401  121.033 65.825  1.00 68.18  ? 3910 ARG A NH2   1 
ATOM   17625 N  N     . GLY A 1 3911 ? 83.708  121.919 68.454  1.00 58.10  ? 3911 GLY A N     1 
ATOM   17626 C  CA    . GLY A 1 3911 ? 83.063  123.212 68.570  1.00 57.32  ? 3911 GLY A CA    1 
ATOM   17627 C  C     . GLY A 1 3911 ? 83.620  124.073 69.684  1.00 63.91  ? 3911 GLY A C     1 
ATOM   17628 O  O     . GLY A 1 3911 ? 83.982  125.232 69.463  1.00 67.25  ? 3911 GLY A O     1 
ATOM   17629 N  N     . ASN A 1 3912 ? 83.689  123.511 70.893  1.00 68.59  ? 3912 ASN A N     1 
ATOM   17630 C  CA    . ASN A 1 3912 ? 84.261  124.230 72.025  1.00 68.15  ? 3912 ASN A CA    1 
ATOM   17631 C  C     . ASN A 1 3912 ? 85.741  124.528 71.830  1.00 73.95  ? 3912 ASN A C     1 
ATOM   17632 O  O     . ASN A 1 3912 ? 86.287  125.386 72.533  1.00 78.95  ? 3912 ASN A O     1 
ATOM   17633 C  CB    . ASN A 1 3912 ? 84.047  123.430 73.312  1.00 71.58  ? 3912 ASN A CB    1 
ATOM   17634 C  CG    . ASN A 1 3912 ? 84.521  121.994 73.191  1.00 78.94  ? 3912 ASN A CG    1 
ATOM   17635 O  OD1   . ASN A 1 3912 ? 85.012  121.574 72.144  1.00 77.80  ? 3912 ASN A OD1   1 
ATOM   17636 N  ND2   . ASN A 1 3912 ? 84.371  121.230 74.267  1.00 75.98  ? 3912 ASN A ND2   1 
ATOM   17637 N  N     . GLU A 1 3913 ? 86.402  123.843 70.895  1.00 73.12  ? 3913 GLU A N     1 
ATOM   17638 C  CA    . GLU A 1 3913 ? 87.806  124.110 70.609  1.00 75.71  ? 3913 GLU A CA    1 
ATOM   17639 C  C     . GLU A 1 3913 ? 88.030  125.476 69.976  1.00 76.68  ? 3913 GLU A C     1 
ATOM   17640 O  O     . GLU A 1 3913 ? 89.180  125.924 69.908  1.00 80.85  ? 3913 GLU A O     1 
ATOM   17641 C  CB    . GLU A 1 3913 ? 88.373  123.019 69.698  1.00 74.18  ? 3913 GLU A CB    1 
ATOM   17642 C  CG    . GLU A 1 3913 ? 88.112  121.606 70.190  1.00 68.91  ? 3913 GLU A CG    1 
ATOM   17643 C  CD    . GLU A 1 3913 ? 88.848  120.563 69.375  1.00 73.97  ? 3913 GLU A CD    1 
ATOM   17644 O  OE1   . GLU A 1 3913 ? 89.578  120.947 68.438  1.00 74.71  ? 3913 GLU A OE1   1 
ATOM   17645 O  OE2   . GLU A 1 3913 ? 88.695  119.359 69.670  1.00 75.26  ? 3913 GLU A OE2   1 
ATOM   17646 N  N     . ILE A 1 3914 ? 86.974  126.144 69.515  1.00 71.51  ? 3914 ILE A N     1 
ATOM   17647 C  CA    . ILE A 1 3914 ? 87.094  127.489 68.964  1.00 70.18  ? 3914 ILE A CA    1 
ATOM   17648 C  C     . ILE A 1 3914 ? 87.307  128.459 70.117  1.00 74.86  ? 3914 ILE A C     1 
ATOM   17649 O  O     . ILE A 1 3914 ? 86.358  128.832 70.816  1.00 75.24  ? 3914 ILE A O     1 
ATOM   17650 C  CB    . ILE A 1 3914 ? 85.855  127.870 68.134  1.00 70.52  ? 3914 ILE A CB    1 
ATOM   17651 C  CG1   . ILE A 1 3914 ? 85.662  126.887 66.978  1.00 64.29  ? 3914 ILE A CG1   1 
ATOM   17652 C  CG2   . ILE A 1 3914 ? 85.982  129.292 67.606  1.00 69.67  ? 3914 ILE A CG2   1 
ATOM   17653 C  CD1   . ILE A 1 3914 ? 86.817  126.858 66.002  1.00 69.25  ? 3914 ILE A CD1   1 
ATOM   17654 N  N     . VAL A 1 3915 ? 88.558  128.869 70.325  1.00 79.12  ? 3915 VAL A N     1 
ATOM   17655 C  CA    . VAL A 1 3915 ? 88.895  129.711 71.467  1.00 83.96  ? 3915 VAL A CA    1 
ATOM   17656 C  C     . VAL A 1 3915 ? 88.391  131.126 71.226  1.00 84.81  ? 3915 VAL A C     1 
ATOM   17657 O  O     . VAL A 1 3915 ? 88.628  131.717 70.164  1.00 78.92  ? 3915 VAL A O     1 
ATOM   17658 C  CB    . VAL A 1 3915 ? 90.410  129.692 71.719  1.00 82.89  ? 3915 VAL A CB    1 
ATOM   17659 C  CG1   . VAL A 1 3915 ? 90.772  130.633 72.859  1.00 78.75  ? 3915 VAL A CG1   1 
ATOM   17660 C  CG2   . VAL A 1 3915 ? 90.879  128.277 72.018  1.00 75.01  ? 3915 VAL A CG2   1 
ATOM   17661 N  N     . LEU A 1 3916 ? 87.690  131.677 72.214  1.00 84.45  ? 3916 LEU A N     1 
ATOM   17662 C  CA    . LEU A 1 3916 ? 87.157  133.030 72.152  1.00 86.33  ? 3916 LEU A CA    1 
ATOM   17663 C  C     . LEU A 1 3916 ? 87.816  133.874 73.232  1.00 92.46  ? 3916 LEU A C     1 
ATOM   17664 O  O     . LEU A 1 3916 ? 87.869  133.467 74.398  1.00 91.22  ? 3916 LEU A O     1 
ATOM   17665 C  CB    . LEU A 1 3916 ? 85.637  133.032 72.333  1.00 81.50  ? 3916 LEU A CB    1 
ATOM   17666 C  CG    . LEU A 1 3916 ? 84.838  132.129 71.391  1.00 77.90  ? 3916 LEU A CG    1 
ATOM   17667 C  CD1   . LEU A 1 3916 ? 83.347  132.280 71.647  1.00 69.75  ? 3916 LEU A CD1   1 
ATOM   17668 C  CD2   . LEU A 1 3916 ? 85.172  132.437 69.940  1.00 78.22  ? 3916 LEU A CD2   1 
ATOM   17669 N  N     . SER A 1 3917 ? 88.315  135.045 72.844  1.00 95.48  ? 3917 SER A N     1 
ATOM   17670 C  CA    . SER A 1 3917 ? 88.948  135.952 73.787  1.00 96.14  ? 3917 SER A CA    1 
ATOM   17671 C  C     . SER A 1 3917 ? 87.889  136.782 74.509  1.00 99.52  ? 3917 SER A C     1 
ATOM   17672 O  O     . SER A 1 3917 ? 86.688  136.682 74.239  1.00 97.22  ? 3917 SER A O     1 
ATOM   17673 C  CB    . SER A 1 3917 ? 89.956  136.845 73.067  1.00 92.23  ? 3917 SER A CB    1 
ATOM   17674 O  OG    . SER A 1 3917 ? 90.940  136.072 72.403  1.00 88.10  ? 3917 SER A OG    1 
ATOM   17675 N  N     . ALA A 1 3918 ? 88.342  137.612 75.452  1.00 98.87  ? 3918 ALA A N     1 
ATOM   17676 C  CA    . ALA A 1 3918 ? 87.420  138.473 76.186  1.00 95.92  ? 3918 ALA A CA    1 
ATOM   17677 C  C     . ALA A 1 3918 ? 86.737  139.467 75.254  1.00 96.09  ? 3918 ALA A C     1 
ATOM   17678 O  O     . ALA A 1 3918 ? 85.522  139.681 75.336  1.00 91.43  ? 3918 ALA A O     1 
ATOM   17679 C  CB    . ALA A 1 3918 ? 88.163  139.202 77.306  1.00 87.68  ? 3918 ALA A CB    1 
ATOM   17680 N  N     . GLY A 1 3919 ? 87.508  140.086 74.356  1.00 95.62  ? 3919 GLY A N     1 
ATOM   17681 C  CA    . GLY A 1 3919 ? 86.931  140.999 73.386  1.00 93.10  ? 3919 GLY A CA    1 
ATOM   17682 C  C     . GLY A 1 3919 ? 86.236  140.323 72.226  1.00 93.21  ? 3919 GLY A C     1 
ATOM   17683 O  O     . GLY A 1 3919 ? 85.407  140.954 71.563  1.00 87.13  ? 3919 GLY A O     1 
ATOM   17684 N  N     . SER A 1 3920 ? 86.557  139.054 71.963  1.00 96.60  ? 3920 SER A N     1 
ATOM   17685 C  CA    . SER A 1 3920 ? 85.919  138.338 70.864  1.00 94.71  ? 3920 SER A CA    1 
ATOM   17686 C  C     . SER A 1 3920 ? 84.437  138.104 71.126  1.00 89.50  ? 3920 SER A C     1 
ATOM   17687 O  O     . SER A 1 3920 ? 83.626  138.179 70.196  1.00 84.77  ? 3920 SER A O     1 
ATOM   17688 C  CB    . SER A 1 3920 ? 86.631  137.008 70.618  1.00 89.81  ? 3920 SER A CB    1 
ATOM   17689 O  OG    . SER A 1 3920 ? 88.018  137.203 70.406  1.00 91.66  ? 3920 SER A OG    1 
ATOM   17690 N  N     . THR A 1 3921 ? 84.065  137.819 72.374  1.00 87.55  ? 3921 THR A N     1 
ATOM   17691 C  CA    . THR A 1 3921 ? 82.676  137.558 72.715  1.00 83.38  ? 3921 THR A CA    1 
ATOM   17692 C  C     . THR A 1 3921 ? 82.043  138.825 73.264  1.00 78.31  ? 3921 THR A C     1 
ATOM   17693 O  O     . THR A 1 3921 ? 82.416  139.266 74.362  1.00 76.13  ? 3921 THR A O     1 
ATOM   17694 C  CB    . THR A 1 3921 ? 82.573  136.428 73.739  1.00 79.56  ? 3921 THR A CB    1 
ATOM   17695 O  OG1   . THR A 1 3921 ? 83.138  135.230 73.191  1.00 78.49  ? 3921 THR A OG1   1 
ATOM   17696 C  CG2   . THR A 1 3921 ? 81.119  136.177 74.108  1.00 70.84  ? 3921 THR A CG2   1 
ATOM   17697 N  N     . PRO A 1 3922 ? 81.101  139.440 72.562  1.00 76.66  ? 3922 PRO A N     1 
ATOM   17698 C  CA    . PRO A 1 3922 ? 80.424  140.630 73.081  1.00 76.10  ? 3922 PRO A CA    1 
ATOM   17699 C  C     . PRO A 1 3922 ? 79.295  140.234 74.027  1.00 74.20  ? 3922 PRO A C     1 
ATOM   17700 O  O     . PRO A 1 3922 ? 79.077  139.061 74.323  1.00 70.42  ? 3922 PRO A O     1 
ATOM   17701 C  CB    . PRO A 1 3922 ? 79.892  141.300 71.815  1.00 74.85  ? 3922 PRO A CB    1 
ATOM   17702 C  CG    . PRO A 1 3922 ? 79.613  140.157 70.898  1.00 72.36  ? 3922 PRO A CG    1 
ATOM   17703 C  CD    . PRO A 1 3922 ? 80.655  139.103 71.198  1.00 75.11  ? 3922 PRO A CD    1 
ATOM   17704 N  N     . ARG A 1 3923 ? 78.572  141.245 74.501  1.00 78.15  ? 3923 ARG A N     1 
ATOM   17705 C  CA    . ARG A 1 3923 ? 77.433  141.050 75.394  1.00 78.13  ? 3923 ARG A CA    1 
ATOM   17706 C  C     . ARG A 1 3923 ? 76.160  141.308 74.596  1.00 78.11  ? 3923 ARG A C     1 
ATOM   17707 O  O     . ARG A 1 3923 ? 75.809  142.458 74.319  1.00 77.06  ? 3923 ARG A O     1 
ATOM   17708 C  CB    . ARG A 1 3923 ? 77.526  141.969 76.607  1.00 79.66  ? 3923 ARG A CB    1 
ATOM   17709 C  CG    . ARG A 1 3923 ? 76.330  141.879 77.540  1.00 74.76  ? 3923 ARG A CG    1 
ATOM   17710 C  CD    . ARG A 1 3923 ? 76.393  142.941 78.625  1.00 78.87  ? 3923 ARG A CD    1 
ATOM   17711 N  NE    . ARG A 1 3923 ? 76.395  144.288 78.067  1.00 91.34  ? 3923 ARG A NE    1 
ATOM   17712 C  CZ    . ARG A 1 3923 ? 76.402  145.399 78.792  1.00 93.88  ? 3923 ARG A CZ    1 
ATOM   17713 N  NH1   . ARG A 1 3923 ? 76.408  145.362 80.114  1.00 89.39  ? 3923 ARG A NH1   1 
ATOM   17714 N  NH2   . ARG A 1 3923 ? 76.403  146.576 78.174  1.00 92.92  ? 3923 ARG A NH2   1 
ATOM   17715 N  N     . ILE A 1 3924 ? 75.471  140.235 74.224  1.00 75.17  ? 3924 ILE A N     1 
ATOM   17716 C  CA    . ILE A 1 3924 ? 74.215  140.334 73.491  1.00 73.68  ? 3924 ILE A CA    1 
ATOM   17717 C  C     . ILE A 1 3924 ? 73.072  140.388 74.494  1.00 69.85  ? 3924 ILE A C     1 
ATOM   17718 O  O     . ILE A 1 3924 ? 72.983  139.545 75.395  1.00 65.67  ? 3924 ILE A O     1 
ATOM   17719 C  CB    . ILE A 1 3924 ? 74.042  139.152 72.522  1.00 72.38  ? 3924 ILE A CB    1 
ATOM   17720 C  CG1   . ILE A 1 3924 ? 75.183  139.113 71.503  1.00 70.88  ? 3924 ILE A CG1   1 
ATOM   17721 C  CG2   . ILE A 1 3924 ? 72.704  139.248 71.806  1.00 63.39  ? 3924 ILE A CG2   1 
ATOM   17722 C  CD1   . ILE A 1 3924 ? 76.302  138.156 71.865  1.00 69.65  ? 3924 ILE A CD1   1 
ATOM   17723 N  N     . GLN A 1 3925 ? 72.201  141.382 74.344  1.00 74.02  ? 3925 GLN A N     1 
ATOM   17724 C  CA    . GLN A 1 3925 ? 71.063  141.518 75.242  1.00 75.00  ? 3925 GLN A CA    1 
ATOM   17725 C  C     . GLN A 1 3925 ? 70.077  140.378 75.016  1.00 66.89  ? 3925 GLN A C     1 
ATOM   17726 O  O     . GLN A 1 3925 ? 69.675  140.105 73.881  1.00 61.75  ? 3925 GLN A O     1 
ATOM   17727 C  CB    . GLN A 1 3925 ? 70.378  142.867 75.027  1.00 71.90  ? 3925 GLN A CB    1 
ATOM   17728 C  CG    . GLN A 1 3925 ? 69.178  143.109 75.927  1.00 74.20  ? 3925 GLN A CG    1 
ATOM   17729 C  CD    . GLN A 1 3925 ? 68.379  144.330 75.515  1.00 84.15  ? 3925 GLN A CD    1 
ATOM   17730 O  OE1   . GLN A 1 3925 ? 68.695  144.987 74.523  1.00 86.81  ? 3925 GLN A OE1   1 
ATOM   17731 N  NE2   . GLN A 1 3925 ? 67.337  144.641 76.277  1.00 87.53  ? 3925 GLN A NE2   1 
ATOM   17732 N  N     . GLY A 1 3926 ? 69.687  139.714 76.102  1.00 62.88  ? 3926 GLY A N     1 
ATOM   17733 C  CA    . GLY A 1 3926 ? 68.766  138.601 76.042  1.00 60.94  ? 3926 GLY A CA    1 
ATOM   17734 C  C     . GLY A 1 3926 ? 69.408  137.231 76.104  1.00 55.03  ? 3926 GLY A C     1 
ATOM   17735 O  O     . GLY A 1 3926 ? 68.685  136.234 76.221  1.00 49.58  ? 3926 GLY A O     1 
ATOM   17736 N  N     . LEU A 1 3927 ? 70.735  137.149 76.031  1.00 55.73  ? 3927 LEU A N     1 
ATOM   17737 C  CA    . LEU A 1 3927 ? 71.444  135.879 76.075  1.00 53.90  ? 3927 LEU A CA    1 
ATOM   17738 C  C     . LEU A 1 3927 ? 72.456  135.883 77.211  1.00 54.99  ? 3927 LEU A C     1 
ATOM   17739 O  O     . LEU A 1 3927 ? 72.989  136.931 77.590  1.00 57.15  ? 3927 LEU A O     1 
ATOM   17740 C  CB    . LEU A 1 3927 ? 72.163  135.588 74.751  1.00 53.26  ? 3927 LEU A CB    1 
ATOM   17741 C  CG    . LEU A 1 3927 ? 71.386  135.811 73.454  1.00 56.50  ? 3927 LEU A CG    1 
ATOM   17742 C  CD1   . LEU A 1 3927 ? 72.309  135.667 72.255  1.00 60.00  ? 3927 LEU A CD1   1 
ATOM   17743 C  CD2   . LEU A 1 3927 ? 70.217  134.851 73.351  1.00 46.78  ? 3927 LEU A CD2   1 
ATOM   17744 N  N     . THR A 1 3928 ? 72.717  134.696 77.752  1.00 54.37  ? 3928 THR A N     1 
ATOM   17745 C  CA    . THR A 1 3928 ? 73.700  134.534 78.811  1.00 52.85  ? 3928 THR A CA    1 
ATOM   17746 C  C     . THR A 1 3928 ? 75.106  134.484 78.216  1.00 57.12  ? 3928 THR A C     1 
ATOM   17747 O  O     . THR A 1 3928 ? 75.297  134.508 76.997  1.00 58.21  ? 3928 THR A O     1 
ATOM   17748 C  CB    . THR A 1 3928 ? 73.403  133.279 79.627  1.00 51.29  ? 3928 THR A CB    1 
ATOM   17749 O  OG1   . THR A 1 3928 ? 73.492  132.125 78.782  1.00 58.65  ? 3928 THR A OG1   1 
ATOM   17750 C  CG2   . THR A 1 3928 ? 72.008  133.353 80.228  1.00 50.79  ? 3928 THR A CG2   1 
ATOM   17751 N  N     . VAL A 1 3929 ? 76.109  134.420 79.095  1.00 59.22  ? 3929 VAL A N     1 
ATOM   17752 C  CA    . VAL A 1 3929 ? 77.498  134.375 78.641  1.00 62.56  ? 3929 VAL A CA    1 
ATOM   17753 C  C     . VAL A 1 3929 ? 77.754  133.105 77.838  1.00 60.68  ? 3929 VAL A C     1 
ATOM   17754 O  O     . VAL A 1 3929 ? 78.365  133.141 76.762  1.00 60.67  ? 3929 VAL A O     1 
ATOM   17755 C  CB    . VAL A 1 3929 ? 78.458  134.490 79.838  1.00 64.90  ? 3929 VAL A CB    1 
ATOM   17756 C  CG1   . VAL A 1 3929 ? 79.898  134.309 79.385  1.00 56.87  ? 3929 VAL A CG1   1 
ATOM   17757 C  CG2   . VAL A 1 3929 ? 78.276  135.829 80.537  1.00 60.71  ? 3929 VAL A CG2   1 
ATOM   17758 N  N     . GLU A 1 3930 ? 77.287  131.962 78.348  1.00 62.72  ? 3930 GLU A N     1 
ATOM   17759 C  CA    . GLU A 1 3930 ? 77.452  130.706 77.623  1.00 58.99  ? 3930 GLU A CA    1 
ATOM   17760 C  C     . GLU A 1 3930 ? 76.724  130.749 76.286  1.00 55.58  ? 3930 GLU A C     1 
ATOM   17761 O  O     . GLU A 1 3930 ? 77.273  130.339 75.255  1.00 51.61  ? 3930 GLU A O     1 
ATOM   17762 C  CB    . GLU A 1 3930 ? 76.952  129.529 78.466  1.00 56.33  ? 3930 GLU A CB    1 
ATOM   17763 C  CG    . GLU A 1 3930 ? 77.591  129.372 79.852  1.00 66.65  ? 3930 GLU A CG    1 
ATOM   17764 C  CD    . GLU A 1 3930 ? 77.137  130.411 80.870  1.00 75.71  ? 3930 GLU A CD    1 
ATOM   17765 O  OE1   . GLU A 1 3930 ? 76.495  131.410 80.483  1.00 68.47  ? 3930 GLU A OE1   1 
ATOM   17766 O  OE2   . GLU A 1 3930 ? 77.428  130.222 82.070  1.00 79.21  ? 3930 GLU A OE2   1 
ATOM   17767 N  N     . GLN A 1 3931 ? 75.491  131.259 76.284  1.00 54.33  ? 3931 GLN A N     1 
ATOM   17768 C  CA    . GLN A 1 3931 ? 74.755  131.404 75.033  1.00 52.34  ? 3931 GLN A CA    1 
ATOM   17769 C  C     . GLN A 1 3931 ? 75.464  132.363 74.087  1.00 57.38  ? 3931 GLN A C     1 
ATOM   17770 O  O     . GLN A 1 3931 ? 75.523  132.117 72.879  1.00 60.06  ? 3931 GLN A O     1 
ATOM   17771 C  CB    . GLN A 1 3931 ? 73.330  131.880 75.311  1.00 47.81  ? 3931 GLN A CB    1 
ATOM   17772 C  CG    . GLN A 1 3931 ? 72.379  130.775 75.735  1.00 43.46  ? 3931 GLN A CG    1 
ATOM   17773 C  CD    . GLN A 1 3931 ? 70.958  131.269 75.907  1.00 49.66  ? 3931 GLN A CD    1 
ATOM   17774 O  OE1   . GLN A 1 3931 ? 70.702  132.472 75.895  1.00 56.38  ? 3931 GLN A OE1   1 
ATOM   17775 N  NE2   . GLN A 1 3931 ? 70.022  130.339 76.064  1.00 42.91  ? 3931 GLN A NE2   1 
ATOM   17776 N  N     . ALA A 1 3932 ? 76.007  133.463 74.617  1.00 62.33  ? 3932 ALA A N     1 
ATOM   17777 C  CA    . ALA A 1 3932 ? 76.705  134.423 73.768  1.00 62.76  ? 3932 ALA A CA    1 
ATOM   17778 C  C     . ALA A 1 3932 ? 77.925  133.794 73.107  1.00 61.25  ? 3932 ALA A C     1 
ATOM   17779 O  O     . ALA A 1 3932 ? 78.153  133.977 71.904  1.00 62.63  ? 3932 ALA A O     1 
ATOM   17780 C  CB    . ALA A 1 3932 ? 77.110  135.650 74.583  1.00 65.85  ? 3932 ALA A CB    1 
ATOM   17781 N  N     . GLU A 1 3933 ? 78.721  133.044 73.874  1.00 55.49  ? 3933 GLU A N     1 
ATOM   17782 C  CA    . GLU A 1 3933 ? 79.868  132.366 73.280  1.00 59.11  ? 3933 GLU A CA    1 
ATOM   17783 C  C     . GLU A 1 3933 ? 79.433  131.304 72.279  1.00 59.22  ? 3933 GLU A C     1 
ATOM   17784 O  O     . GLU A 1 3933 ? 80.118  131.086 71.272  1.00 60.80  ? 3933 GLU A O     1 
ATOM   17785 C  CB    . GLU A 1 3933 ? 80.754  131.749 74.363  1.00 56.91  ? 3933 GLU A CB    1 
ATOM   17786 C  CG    . GLU A 1 3933 ? 81.253  132.735 75.407  1.00 64.80  ? 3933 GLU A CG    1 
ATOM   17787 C  CD    . GLU A 1 3933 ? 81.468  132.093 76.764  1.00 68.54  ? 3933 GLU A CD    1 
ATOM   17788 O  OE1   . GLU A 1 3933 ? 80.540  131.428 77.268  1.00 68.72  ? 3933 GLU A OE1   1 
ATOM   17789 O  OE2   . GLU A 1 3933 ? 82.570  132.254 77.329  1.00 66.65  ? 3933 GLU A OE2   1 
ATOM   17790 N  N     . ALA A 1 3934 ? 78.305  130.635 72.532  1.00 56.55  ? 3934 ALA A N     1 
ATOM   17791 C  CA    . ALA A 1 3934 ? 77.787  129.680 71.558  1.00 53.03  ? 3934 ALA A CA    1 
ATOM   17792 C  C     . ALA A 1 3934 ? 77.417  130.372 70.251  1.00 52.72  ? 3934 ALA A C     1 
ATOM   17793 O  O     . ALA A 1 3934 ? 77.703  129.854 69.165  1.00 52.33  ? 3934 ALA A O     1 
ATOM   17794 C  CB    . ALA A 1 3934 ? 76.584  128.940 72.138  1.00 48.11  ? 3934 ALA A CB    1 
ATOM   17795 N  N     . VAL A 1 3935 ? 76.782  131.544 70.336  1.00 52.74  ? 3935 VAL A N     1 
ATOM   17796 C  CA    . VAL A 1 3935 ? 76.468  132.313 69.132  1.00 55.28  ? 3935 VAL A CA    1 
ATOM   17797 C  C     . VAL A 1 3935 ? 77.743  132.720 68.406  1.00 56.61  ? 3935 VAL A C     1 
ATOM   17798 O  O     . VAL A 1 3935 ? 77.824  132.639 67.175  1.00 56.76  ? 3935 VAL A O     1 
ATOM   17799 C  CB    . VAL A 1 3935 ? 75.600  133.540 69.473  1.00 54.25  ? 3935 VAL A CB    1 
ATOM   17800 C  CG1   . VAL A 1 3935 ? 75.093  134.192 68.204  1.00 49.77  ? 3935 VAL A CG1   1 
ATOM   17801 C  CG2   . VAL A 1 3935 ? 74.413  133.130 70.308  1.00 53.00  ? 3935 VAL A CG2   1 
ATOM   17802 N  N     . VAL A 1 3936 ? 78.752  133.170 69.154  1.00 57.59  ? 3936 VAL A N     1 
ATOM   17803 C  CA    . VAL A 1 3936 ? 80.003  133.595 68.526  1.00 58.21  ? 3936 VAL A CA    1 
ATOM   17804 C  C     . VAL A 1 3936 ? 80.656  132.429 67.792  1.00 59.22  ? 3936 VAL A C     1 
ATOM   17805 O  O     . VAL A 1 3936 ? 81.118  132.571 66.654  1.00 58.65  ? 3936 VAL A O     1 
ATOM   17806 C  CB    . VAL A 1 3936 ? 80.953  134.212 69.569  1.00 64.32  ? 3936 VAL A CB    1 
ATOM   17807 C  CG1   . VAL A 1 3936 ? 82.276  134.579 68.921  1.00 65.20  ? 3936 VAL A CG1   1 
ATOM   17808 C  CG2   . VAL A 1 3936 ? 80.323  135.445 70.190  1.00 61.42  ? 3936 VAL A CG2   1 
ATOM   17809 N  N     . ARG A 1 3937 ? 80.704  131.257 68.432  1.00 58.29  ? 3937 ARG A N     1 
ATOM   17810 C  CA    . ARG A 1 3937 ? 81.299  130.093 67.780  1.00 51.01  ? 3937 ARG A CA    1 
ATOM   17811 C  C     . ARG A 1 3937 ? 80.490  129.650 66.566  1.00 52.50  ? 3937 ARG A C     1 
ATOM   17812 O  O     . ARG A 1 3937 ? 81.065  129.306 65.526  1.00 55.45  ? 3937 ARG A O     1 
ATOM   17813 C  CB    . ARG A 1 3937 ? 81.453  128.938 68.770  1.00 50.77  ? 3937 ARG A CB    1 
ATOM   17814 C  CG    . ARG A 1 3937 ? 82.506  129.169 69.839  1.00 55.86  ? 3937 ARG A CG    1 
ATOM   17815 C  CD    . ARG A 1 3937 ? 82.622  127.967 70.762  1.00 60.34  ? 3937 ARG A CD    1 
ATOM   17816 N  NE    . ARG A 1 3937 ? 83.666  128.144 71.764  1.00 62.68  ? 3937 ARG A NE    1 
ATOM   17817 C  CZ    . ARG A 1 3937 ? 83.472  128.668 72.966  1.00 64.07  ? 3937 ARG A CZ    1 
ATOM   17818 N  NH1   . ARG A 1 3937 ? 82.274  129.064 73.362  1.00 63.85  ? 3937 ARG A NH1   1 
ATOM   17819 N  NH2   . ARG A 1 3937 ? 84.506  128.792 73.794  1.00 62.35  ? 3937 ARG A NH2   1 
ATOM   17820 N  N     . LEU A 1 3938 ? 79.159  129.642 66.674  1.00 51.17  ? 3938 LEU A N     1 
ATOM   17821 C  CA    . LEU A 1 3938 ? 78.330  129.249 65.542  1.00 48.30  ? 3938 LEU A CA    1 
ATOM   17822 C  C     . LEU A 1 3938 ? 78.429  130.239 64.390  1.00 49.92  ? 3938 LEU A C     1 
ATOM   17823 O  O     . LEU A 1 3938 ? 78.222  129.852 63.235  1.00 51.82  ? 3938 LEU A O     1 
ATOM   17824 C  CB    . LEU A 1 3938 ? 76.873  129.091 65.986  1.00 46.24  ? 3938 LEU A CB    1 
ATOM   17825 C  CG    . LEU A 1 3938 ? 75.890  128.518 64.961  1.00 42.76  ? 3938 LEU A CG    1 
ATOM   17826 C  CD1   . LEU A 1 3938 ? 76.284  127.101 64.581  1.00 40.90  ? 3938 LEU A CD1   1 
ATOM   17827 C  CD2   . LEU A 1 3938 ? 74.469  128.548 65.499  1.00 36.95  ? 3938 LEU A CD2   1 
ATOM   17828 N  N     . SER A 1 3939 ? 78.760  131.500 64.676  1.00 54.50  ? 3939 SER A N     1 
ATOM   17829 C  CA    . SER A 1 3939 ? 78.911  132.504 63.630  1.00 56.28  ? 3939 SER A CA    1 
ATOM   17830 C  C     . SER A 1 3939 ? 80.105  132.244 62.722  1.00 58.24  ? 3939 SER A C     1 
ATOM   17831 O  O     . SER A 1 3939 ? 80.224  132.907 61.686  1.00 58.37  ? 3939 SER A O     1 
ATOM   17832 C  CB    . SER A 1 3939 ? 79.033  133.895 64.254  1.00 48.95  ? 3939 SER A CB    1 
ATOM   17833 O  OG    . SER A 1 3939 ? 80.318  134.087 64.818  1.00 56.99  ? 3939 SER A OG    1 
ATOM   17834 N  N     . CYS A 1 3940 ? 80.990  131.311 63.084  1.00 55.17  ? 3940 CYS A N     1 
ATOM   17835 C  CA    . CYS A 1 3940 ? 82.138  131.008 62.235  1.00 54.25  ? 3940 CYS A CA    1 
ATOM   17836 C  C     . CYS A 1 3940 ? 81.710  130.457 60.881  1.00 61.02  ? 3940 CYS A C     1 
ATOM   17837 O  O     . CYS A 1 3940 ? 82.452  130.580 59.900  1.00 64.22  ? 3940 CYS A O     1 
ATOM   17838 C  CB    . CYS A 1 3940 ? 83.066  130.020 62.943  1.00 54.94  ? 3940 CYS A CB    1 
ATOM   17839 S  SG    . CYS A 1 3940 ? 84.673  129.796 62.147  1.00 89.52  ? 3940 CYS A SG    1 
ATOM   17840 N  N     . LEU A 1 3941 ? 80.530  129.846 60.805  1.00 58.37  ? 3941 LEU A N     1 
ATOM   17841 C  CA    . LEU A 1 3941 ? 80.034  129.352 59.533  1.00 58.71  ? 3941 LEU A CA    1 
ATOM   17842 C  C     . LEU A 1 3941 ? 79.673  130.512 58.607  1.00 58.05  ? 3941 LEU A C     1 
ATOM   17843 O  O     . LEU A 1 3941 ? 79.283  131.588 59.068  1.00 60.31  ? 3941 LEU A O     1 
ATOM   17844 C  CB    . LEU A 1 3941 ? 78.804  128.473 59.731  1.00 59.95  ? 3941 LEU A CB    1 
ATOM   17845 C  CG    . LEU A 1 3941 ? 78.923  127.157 60.495  1.00 57.97  ? 3941 LEU A CG    1 
ATOM   17846 C  CD1   . LEU A 1 3941 ? 77.750  126.274 60.115  1.00 49.51  ? 3941 LEU A CD1   1 
ATOM   17847 C  CD2   . LEU A 1 3941 ? 80.243  126.464 60.198  1.00 54.01  ? 3941 LEU A CD2   1 
ATOM   17848 N  N     . PRO A 1 3942 ? 79.807  130.320 57.293  1.00 62.14  ? 3942 PRO A N     1 
ATOM   17849 C  CA    . PRO A 1 3942 ? 79.281  131.321 56.354  1.00 61.80  ? 3942 PRO A CA    1 
ATOM   17850 C  C     . PRO A 1 3942 ? 77.784  131.536 56.486  1.00 58.15  ? 3942 PRO A C     1 
ATOM   17851 O  O     . PRO A 1 3942 ? 77.304  132.654 56.260  1.00 59.21  ? 3942 PRO A O     1 
ATOM   17852 C  CB    . PRO A 1 3942 ? 79.649  130.735 54.985  1.00 59.44  ? 3942 PRO A CB    1 
ATOM   17853 C  CG    . PRO A 1 3942 ? 80.856  129.901 55.256  1.00 52.63  ? 3942 PRO A CG    1 
ATOM   17854 C  CD    . PRO A 1 3942 ? 80.619  129.296 56.613  1.00 57.99  ? 3942 PRO A CD    1 
ATOM   17855 N  N     . ALA A 1 3943 ? 77.028  130.495 56.844  1.00 56.51  ? 3943 ALA A N     1 
ATOM   17856 C  CA    . ALA A 1 3943 ? 75.578  130.626 56.936  1.00 58.03  ? 3943 ALA A CA    1 
ATOM   17857 C  C     . ALA A 1 3943 ? 75.152  131.397 58.178  1.00 52.87  ? 3943 ALA A C     1 
ATOM   17858 O  O     . ALA A 1 3943 ? 74.108  132.058 58.167  1.00 55.16  ? 3943 ALA A O     1 
ATOM   17859 C  CB    . ALA A 1 3943 ? 74.922  129.244 56.921  1.00 48.58  ? 3943 ALA A CB    1 
ATOM   17860 N  N     . PHE A 1 3944 ? 75.935  131.326 59.254  1.00 51.79  ? 3944 PHE A N     1 
ATOM   17861 C  CA    . PHE A 1 3944 ? 75.614  132.006 60.503  1.00 58.89  ? 3944 PHE A CA    1 
ATOM   17862 C  C     . PHE A 1 3944 ? 76.494  133.227 60.747  1.00 60.31  ? 3944 PHE A C     1 
ATOM   17863 O  O     . PHE A 1 3944 ? 76.608  133.680 61.888  1.00 58.86  ? 3944 PHE A O     1 
ATOM   17864 C  CB    . PHE A 1 3944 ? 75.727  131.039 61.682  1.00 54.53  ? 3944 PHE A CB    1 
ATOM   17865 C  CG    . PHE A 1 3944 ? 74.769  129.883 61.621  1.00 53.46  ? 3944 PHE A CG    1 
ATOM   17866 C  CD1   . PHE A 1 3944 ? 73.449  130.040 62.007  1.00 49.78  ? 3944 PHE A CD1   1 
ATOM   17867 C  CD2   . PHE A 1 3944 ? 75.191  128.639 61.184  1.00 51.00  ? 3944 PHE A CD2   1 
ATOM   17868 C  CE1   . PHE A 1 3944 ? 72.566  128.978 61.957  1.00 46.11  ? 3944 PHE A CE1   1 
ATOM   17869 C  CE2   . PHE A 1 3944 ? 74.313  127.573 61.130  1.00 44.45  ? 3944 PHE A CE2   1 
ATOM   17870 C  CZ    . PHE A 1 3944 ? 72.999  127.743 61.517  1.00 38.53  ? 3944 PHE A CZ    1 
ATOM   17871 N  N     . LYS A 1 3945 ? 77.120  133.771 59.700  1.00 60.62  ? 3945 LYS A N     1 
ATOM   17872 C  CA    . LYS A 1 3945 ? 78.035  134.892 59.897  1.00 63.27  ? 3945 LYS A CA    1 
ATOM   17873 C  C     . LYS A 1 3945 ? 77.312  136.109 60.467  1.00 65.97  ? 3945 LYS A C     1 
ATOM   17874 O  O     . LYS A 1 3945 ? 77.831  136.780 61.368  1.00 62.20  ? 3945 LYS A O     1 
ATOM   17875 C  CB    . LYS A 1 3945 ? 78.750  135.230 58.585  1.00 65.26  ? 3945 LYS A CB    1 
ATOM   17876 C  CG    . LYS A 1 3945 ? 77.864  135.776 57.476  1.00 67.44  ? 3945 LYS A CG    1 
ATOM   17877 C  CD    . LYS A 1 3945 ? 78.670  136.065 56.222  1.00 65.20  ? 3945 LYS A CD    1 
ATOM   17878 C  CE    . LYS A 1 3945 ? 77.781  136.572 55.099  1.00 70.36  ? 3945 LYS A CE    1 
ATOM   17879 N  NZ    . LYS A 1 3945 ? 77.203  137.908 55.410  1.00 66.74  ? 3945 LYS A NZ    1 
ATOM   17880 N  N     . ASP A 1 3946 ? 76.121  136.411 59.962  1.00 64.57  ? 3946 ASP A N     1 
ATOM   17881 C  CA    . ASP A 1 3946 ? 75.282  137.474 60.520  1.00 66.01  ? 3946 ASP A CA    1 
ATOM   17882 C  C     . ASP A 1 3946 ? 74.256  136.921 61.506  1.00 65.93  ? 3946 ASP A C     1 
ATOM   17883 O  O     . ASP A 1 3946 ? 73.060  137.197 61.416  1.00 63.52  ? 3946 ASP A O     1 
ATOM   17884 C  CB    . ASP A 1 3946 ? 74.612  138.259 59.394  1.00 69.02  ? 3946 ASP A CB    1 
ATOM   17885 C  CG    . ASP A 1 3946 ? 73.675  137.408 58.548  1.00 77.08  ? 3946 ASP A CG    1 
ATOM   17886 O  OD1   . ASP A 1 3946 ? 73.564  136.189 58.798  1.00 75.92  ? 3946 ASP A OD1   1 
ATOM   17887 O  OD2   . ASP A 1 3946 ? 73.044  137.967 57.627  1.00 78.05  ? 3946 ASP A OD2   1 
ATOM   17888 N  N     . LEU A 1 3947 ? 74.723  136.140 62.482  1.00 62.20  ? 3947 LEU A N     1 
ATOM   17889 C  CA    . LEU A 1 3947 ? 73.807  135.529 63.439  1.00 55.66  ? 3947 LEU A CA    1 
ATOM   17890 C  C     . LEU A 1 3947 ? 73.438  136.491 64.561  1.00 60.63  ? 3947 LEU A C     1 
ATOM   17891 O  O     . LEU A 1 3947 ? 72.276  136.543 64.976  1.00 60.40  ? 3947 LEU A O     1 
ATOM   17892 C  CB    . LEU A 1 3947 ? 74.419  134.249 64.008  1.00 53.72  ? 3947 LEU A CB    1 
ATOM   17893 C  CG    . LEU A 1 3947 ? 73.552  133.394 64.930  1.00 47.37  ? 3947 LEU A CG    1 
ATOM   17894 C  CD1   . LEU A 1 3947 ? 72.266  132.985 64.234  1.00 47.47  ? 3947 LEU A CD1   1 
ATOM   17895 C  CD2   . LEU A 1 3947 ? 74.328  132.167 65.366  1.00 46.82  ? 3947 LEU A CD2   1 
ATOM   17896 N  N     . ILE A 1 3948 ? 74.411  137.256 65.065  1.00 57.96  ? 3948 ILE A N     1 
ATOM   17897 C  CA    . ILE A 1 3948 ? 74.128  138.213 66.131  1.00 57.77  ? 3948 ILE A CA    1 
ATOM   17898 C  C     . ILE A 1 3948 ? 73.130  139.261 65.658  1.00 61.01  ? 3948 ILE A C     1 
ATOM   17899 O  O     . ILE A 1 3948 ? 72.175  139.599 66.370  1.00 60.59  ? 3948 ILE A O     1 
ATOM   17900 C  CB    . ILE A 1 3948 ? 75.433  138.861 66.630  1.00 61.96  ? 3948 ILE A CB    1 
ATOM   17901 C  CG1   . ILE A 1 3948 ? 76.348  137.808 67.258  1.00 58.47  ? 3948 ILE A CG1   1 
ATOM   17902 C  CG2   . ILE A 1 3948 ? 75.136  139.976 67.621  1.00 66.16  ? 3948 ILE A CG2   1 
ATOM   17903 C  CD1   . ILE A 1 3948 ? 77.746  138.307 67.539  1.00 51.38  ? 3948 ILE A CD1   1 
ATOM   17904 N  N     . ALA A 1 3949 ? 73.334  139.792 64.449  1.00 62.88  ? 3949 ALA A N     1 
ATOM   17905 C  CA    . ALA A 1 3949 ? 72.416  140.791 63.913  1.00 64.22  ? 3949 ALA A CA    1 
ATOM   17906 C  C     . ALA A 1 3949 ? 71.022  140.211 63.709  1.00 65.37  ? 3949 ALA A C     1 
ATOM   17907 O  O     . ALA A 1 3949 ? 70.018  140.872 63.997  1.00 66.44  ? 3949 ALA A O     1 
ATOM   17908 C  CB    . ALA A 1 3949 ? 72.961  141.354 62.601  1.00 60.58  ? 3949 ALA A CB    1 
ATOM   17909 N  N     . LYS A 1 3950 ? 70.941  138.976 63.208  1.00 65.84  ? 3950 LYS A N     1 
ATOM   17910 C  CA    . LYS A 1 3950 ? 69.640  138.351 62.988  1.00 66.13  ? 3950 LYS A CA    1 
ATOM   17911 C  C     . LYS A 1 3950 ? 68.909  138.106 64.303  1.00 64.69  ? 3950 LYS A C     1 
ATOM   17912 O  O     . LYS A 1 3950 ? 67.689  138.292 64.384  1.00 58.69  ? 3950 LYS A O     1 
ATOM   17913 C  CB    . LYS A 1 3950 ? 69.810  137.045 62.213  1.00 61.46  ? 3950 LYS A CB    1 
ATOM   17914 C  CG    . LYS A 1 3950 ? 69.461  137.146 60.737  1.00 61.38  ? 3950 LYS A CG    1 
ATOM   17915 C  CD    . LYS A 1 3950 ? 69.963  135.935 59.968  1.00 66.20  ? 3950 LYS A CD    1 
ATOM   17916 C  CE    . LYS A 1 3950 ? 69.643  136.049 58.487  1.00 71.93  ? 3950 LYS A CE    1 
ATOM   17917 N  NZ    . LYS A 1 3950 ? 70.201  137.294 57.893  1.00 70.38  ? 3950 LYS A NZ    1 
ATOM   17918 N  N     . VAL A 1 3951 ? 69.633  137.680 65.341  1.00 62.69  ? 3951 VAL A N     1 
ATOM   17919 C  CA    . VAL A 1 3951 ? 69.010  137.481 66.647  1.00 57.57  ? 3951 VAL A CA    1 
ATOM   17920 C  C     . VAL A 1 3951 ? 68.546  138.810 67.229  1.00 63.97  ? 3951 VAL A C     1 
ATOM   17921 O  O     . VAL A 1 3951 ? 67.436  138.914 67.766  1.00 67.52  ? 3951 VAL A O     1 
ATOM   17922 C  CB    . VAL A 1 3951 ? 69.974  136.750 67.598  1.00 51.03  ? 3951 VAL A CB    1 
ATOM   17923 C  CG1   . VAL A 1 3951 ? 69.387  136.681 68.997  1.00 53.12  ? 3951 VAL A CG1   1 
ATOM   17924 C  CG2   . VAL A 1 3951 ? 70.260  135.349 67.086  1.00 53.79  ? 3951 VAL A CG2   1 
ATOM   17925 N  N     . GLN A 1 3952 ? 69.382  139.848 67.134  1.00 64.32  ? 3952 GLN A N     1 
ATOM   17926 C  CA    . GLN A 1 3952 ? 69.018  141.146 67.694  1.00 60.68  ? 3952 GLN A CA    1 
ATOM   17927 C  C     . GLN A 1 3952 ? 67.818  141.748 66.973  1.00 61.73  ? 3952 GLN A C     1 
ATOM   17928 O  O     . GLN A 1 3952 ? 66.945  142.351 67.608  1.00 62.80  ? 3952 GLN A O     1 
ATOM   17929 C  CB    . GLN A 1 3952 ? 70.215  142.096 67.634  1.00 58.54  ? 3952 GLN A CB    1 
ATOM   17930 C  CG    . GLN A 1 3952 ? 71.203  141.915 68.775  1.00 58.55  ? 3952 GLN A CG    1 
ATOM   17931 C  CD    . GLN A 1 3952 ? 72.549  142.550 68.488  1.00 64.41  ? 3952 GLN A CD    1 
ATOM   17932 O  OE1   . GLN A 1 3952 ? 72.811  142.998 67.371  1.00 69.84  ? 3952 GLN A OE1   1 
ATOM   17933 N  NE2   . GLN A 1 3952 ? 73.411  142.592 69.497  1.00 56.36  ? 3952 GLN A NE2   1 
ATOM   17934 N  N     . ALA A 1 3953 ? 67.756  141.597 65.649  1.00 63.30  ? 3953 ALA A N     1 
ATOM   17935 C  CA    . ALA A 1 3953 ? 66.641  142.134 64.878  1.00 63.88  ? 3953 ALA A CA    1 
ATOM   17936 C  C     . ALA A 1 3953 ? 65.332  141.401 65.137  1.00 68.20  ? 3953 ALA A C     1 
ATOM   17937 O  O     . ALA A 1 3953 ? 64.271  141.923 64.779  1.00 70.62  ? 3953 ALA A O     1 
ATOM   17938 C  CB    . ALA A 1 3953 ? 66.969  142.092 63.385  1.00 56.86  ? 3953 ALA A CB    1 
ATOM   17939 N  N     . ASP A 1 3954 ? 65.376  140.216 65.741  1.00 71.28  ? 3954 ASP A N     1 
ATOM   17940 C  CA    . ASP A 1 3954 ? 64.178  139.434 66.039  1.00 73.41  ? 3954 ASP A CA    1 
ATOM   17941 C  C     . ASP A 1 3954 ? 63.838  139.632 67.512  1.00 72.63  ? 3954 ASP A C     1 
ATOM   17942 O  O     . ASP A 1 3954 ? 64.492  139.069 68.393  1.00 69.34  ? 3954 ASP A O     1 
ATOM   17943 C  CB    . ASP A 1 3954 ? 64.396  137.962 65.706  1.00 70.58  ? 3954 ASP A CB    1 
ATOM   17944 C  CG    . ASP A 1 3954 ? 63.119  137.148 65.791  1.00 71.25  ? 3954 ASP A CG    1 
ATOM   17945 O  OD1   . ASP A 1 3954 ? 62.034  137.752 65.927  1.00 71.21  ? 3954 ASP A OD1   1 
ATOM   17946 O  OD2   . ASP A 1 3954 ? 63.200  135.904 65.723  1.00 74.75  ? 3954 ASP A OD2   1 
ATOM   17947 N  N     . GLU A 1 3955 ? 62.810  140.441 67.777  1.00 75.69  ? 3955 GLU A N     1 
ATOM   17948 C  CA    . GLU A 1 3955 ? 62.385  140.663 69.155  1.00 78.46  ? 3955 GLU A CA    1 
ATOM   17949 C  C     . GLU A 1 3955 ? 61.601  139.476 69.701  1.00 73.51  ? 3955 GLU A C     1 
ATOM   17950 O  O     . GLU A 1 3955 ? 61.603  139.241 70.915  1.00 70.81  ? 3955 GLU A O     1 
ATOM   17951 C  CB    . GLU A 1 3955 ? 61.555  141.946 69.256  1.00 80.02  ? 3955 GLU A CB    1 
ATOM   17952 C  CG    . GLU A 1 3955 ? 60.405  142.045 68.264  1.00 78.92  ? 3955 GLU A CG    1 
ATOM   17953 C  CD    . GLU A 1 3955 ? 60.838  142.573 66.908  1.00 81.14  ? 3955 GLU A CD    1 
ATOM   17954 O  OE1   . GLU A 1 3955 ? 62.036  142.890 66.746  1.00 78.14  ? 3955 GLU A OE1   1 
ATOM   17955 O  OE2   . GLU A 1 3955 ? 59.981  142.669 66.005  1.00 81.35  ? 3955 GLU A OE2   1 
ATOM   17956 N  N     . GLN A 1 3956 ? 60.928  138.720 68.830  1.00 71.02  ? 3956 GLN A N     1 
ATOM   17957 C  CA    . GLN A 1 3956 ? 60.231  137.514 69.259  1.00 68.48  ? 3956 GLN A CA    1 
ATOM   17958 C  C     . GLN A 1 3956 ? 61.185  136.396 69.655  1.00 59.51  ? 3956 GLN A C     1 
ATOM   17959 O  O     . GLN A 1 3956 ? 60.756  135.451 70.329  1.00 53.35  ? 3956 GLN A O     1 
ATOM   17960 C  CB    . GLN A 1 3956 ? 59.297  137.012 68.152  1.00 70.01  ? 3956 GLN A CB    1 
ATOM   17961 C  CG    . GLN A 1 3956 ? 58.034  137.840 67.935  1.00 72.27  ? 3956 GLN A CG    1 
ATOM   17962 C  CD    . GLN A 1 3956 ? 58.315  139.229 67.395  1.00 79.94  ? 3956 GLN A CD    1 
ATOM   17963 O  OE1   . GLN A 1 3956 ? 59.078  139.396 66.443  1.00 77.81  ? 3956 GLN A OE1   1 
ATOM   17964 N  NE2   . GLN A 1 3956 ? 57.687  140.233 67.994  1.00 80.61  ? 3956 GLN A NE2   1 
ATOM   17965 N  N     . PHE A 1 3957 ? 62.461  136.492 69.266  1.00 55.63  ? 3957 PHE A N     1 
ATOM   17966 C  CA    . PHE A 1 3957 ? 63.422  135.427 69.535  1.00 55.18  ? 3957 PHE A CA    1 
ATOM   17967 C  C     . PHE A 1 3957 ? 63.480  135.072 71.014  1.00 53.50  ? 3957 PHE A C     1 
ATOM   17968 O  O     . PHE A 1 3957 ? 63.546  133.887 71.363  1.00 51.32  ? 3957 PHE A O     1 
ATOM   17969 C  CB    . PHE A 1 3957 ? 64.806  135.842 69.036  1.00 55.45  ? 3957 PHE A CB    1 
ATOM   17970 C  CG    . PHE A 1 3957 ? 65.804  134.725 69.018  1.00 48.47  ? 3957 PHE A CG    1 
ATOM   17971 C  CD1   . PHE A 1 3957 ? 65.883  133.865 67.936  1.00 47.10  ? 3957 PHE A CD1   1 
ATOM   17972 C  CD2   . PHE A 1 3957 ? 66.667  134.536 70.083  1.00 38.74  ? 3957 PHE A CD2   1 
ATOM   17973 C  CE1   . PHE A 1 3957 ? 66.804  132.837 67.918  1.00 46.82  ? 3957 PHE A CE1   1 
ATOM   17974 C  CE2   . PHE A 1 3957 ? 67.586  133.511 70.072  1.00 39.96  ? 3957 PHE A CE2   1 
ATOM   17975 C  CZ    . PHE A 1 3957 ? 67.658  132.662 68.988  1.00 42.09  ? 3957 PHE A CZ    1 
ATOM   17976 N  N     . GLY A 1 3958 ? 63.437  136.077 71.892  1.00 48.84  ? 3958 GLY A N     1 
ATOM   17977 C  CA    . GLY A 1 3958 ? 63.448  135.804 73.318  1.00 43.79  ? 3958 GLY A CA    1 
ATOM   17978 C  C     . GLY A 1 3958 ? 62.332  134.875 73.746  1.00 45.77  ? 3958 GLY A C     1 
ATOM   17979 O  O     . GLY A 1 3958 ? 62.557  133.956 74.540  1.00 43.03  ? 3958 GLY A O     1 
ATOM   17980 N  N     . ILE A 1 3959 ? 61.126  135.081 73.210  1.00 47.91  ? 3959 ILE A N     1 
ATOM   17981 C  CA    . ILE A 1 3959 ? 60.027  134.164 73.492  1.00 44.39  ? 3959 ILE A CA    1 
ATOM   17982 C  C     . ILE A 1 3959 ? 60.410  132.746 73.095  1.00 44.70  ? 3959 ILE A C     1 
ATOM   17983 O  O     . ILE A 1 3959 ? 60.231  131.799 73.872  1.00 49.75  ? 3959 ILE A O     1 
ATOM   17984 C  CB    . ILE A 1 3959 ? 58.747  134.627 72.774  1.00 48.09  ? 3959 ILE A CB    1 
ATOM   17985 C  CG1   . ILE A 1 3959 ? 58.314  136.004 73.282  1.00 52.70  ? 3959 ILE A CG1   1 
ATOM   17986 C  CG2   . ILE A 1 3959 ? 57.631  133.610 72.961  1.00 45.53  ? 3959 ILE A CG2   1 
ATOM   17987 C  CD1   . ILE A 1 3959 ? 58.094  136.063 74.777  1.00 46.13  ? 3959 ILE A CD1   1 
ATOM   17988 N  N     . TRP A 1 3960 ? 60.976  132.579 71.896  1.00 39.79  ? 3960 TRP A N     1 
ATOM   17989 C  CA    . TRP A 1 3960 ? 61.390  131.251 71.463  1.00 36.68  ? 3960 TRP A CA    1 
ATOM   17990 C  C     . TRP A 1 3960 ? 62.482  130.692 72.363  1.00 33.36  ? 3960 TRP A C     1 
ATOM   17991 O  O     . TRP A 1 3960 ? 62.606  129.470 72.501  1.00 33.41  ? 3960 TRP A O     1 
ATOM   17992 C  CB    . TRP A 1 3960 ? 61.866  131.292 70.010  1.00 38.56  ? 3960 TRP A CB    1 
ATOM   17993 C  CG    . TRP A 1 3960 ? 62.495  130.013 69.557  1.00 35.83  ? 3960 TRP A CG    1 
ATOM   17994 C  CD1   . TRP A 1 3960 ? 61.852  128.922 69.052  1.00 30.37  ? 3960 TRP A CD1   1 
ATOM   17995 C  CD2   . TRP A 1 3960 ? 63.888  129.682 69.581  1.00 34.65  ? 3960 TRP A CD2   1 
ATOM   17996 N  NE1   . TRP A 1 3960 ? 62.758  127.936 68.751  1.00 30.51  ? 3960 TRP A NE1   1 
ATOM   17997 C  CE2   . TRP A 1 3960 ? 64.015  128.376 69.070  1.00 33.50  ? 3960 TRP A CE2   1 
ATOM   17998 C  CE3   . TRP A 1 3960 ? 65.041  130.363 69.984  1.00 29.57  ? 3960 TRP A CE3   1 
ATOM   17999 C  CZ2   . TRP A 1 3960 ? 65.247  127.739 68.947  1.00 31.68  ? 3960 TRP A CZ2   1 
ATOM   18000 C  CZ3   . TRP A 1 3960 ? 66.262  129.727 69.863  1.00 33.76  ? 3960 TRP A CZ3   1 
ATOM   18001 C  CH2   . TRP A 1 3960 ? 66.356  128.430 69.349  1.00 32.35  ? 3960 TRP A CH2   1 
ATOM   18002 N  N     . LEU A 1 3961 ? 63.273  131.566 72.990  1.00 38.52  ? 3961 LEU A N     1 
ATOM   18003 C  CA    . LEU A 1 3961 ? 64.313  131.100 73.896  1.00 36.17  ? 3961 LEU A CA    1 
ATOM   18004 C  C     . LEU A 1 3961 ? 63.740  130.540 75.189  1.00 39.78  ? 3961 LEU A C     1 
ATOM   18005 O  O     . LEU A 1 3961 ? 64.451  129.834 75.912  1.00 41.67  ? 3961 LEU A O     1 
ATOM   18006 C  CB    . LEU A 1 3961 ? 65.289  132.234 74.209  1.00 35.57  ? 3961 LEU A CB    1 
ATOM   18007 C  CG    . LEU A 1 3961 ? 66.695  131.794 74.622  1.00 43.39  ? 3961 LEU A CG    1 
ATOM   18008 C  CD1   . LEU A 1 3961 ? 67.342  130.970 73.519  1.00 41.67  ? 3961 LEU A CD1   1 
ATOM   18009 C  CD2   . LEU A 1 3961 ? 67.558  132.990 74.988  1.00 42.16  ? 3961 LEU A CD2   1 
ATOM   18010 N  N     . ASP A 1 3962 ? 62.475  130.833 75.498  1.00 38.72  ? 3962 ASP A N     1 
ATOM   18011 C  CA    . ASP A 1 3962 ? 61.856  130.375 76.736  1.00 39.55  ? 3962 ASP A CA    1 
ATOM   18012 C  C     . ASP A 1 3962 ? 60.662  129.463 76.481  1.00 43.08  ? 3962 ASP A C     1 
ATOM   18013 O  O     . ASP A 1 3962 ? 59.834  129.266 77.375  1.00 48.01  ? 3962 ASP A O     1 
ATOM   18014 C  CB    . ASP A 1 3962 ? 61.443  131.568 77.599  1.00 44.88  ? 3962 ASP A CB    1 
ATOM   18015 C  CG    . ASP A 1 3962 ? 62.602  132.499 77.897  1.00 51.37  ? 3962 ASP A CG    1 
ATOM   18016 O  OD1   . ASP A 1 3962 ? 63.589  132.042 78.511  1.00 47.31  ? 3962 ASP A OD1   1 
ATOM   18017 O  OD2   . ASP A 1 3962 ? 62.527  133.686 77.517  1.00 51.47  ? 3962 ASP A OD2   1 
ATOM   18018 N  N     . SER A 1 3963 ? 60.555  128.902 75.280  1.00 38.37  ? 3963 SER A N     1 
ATOM   18019 C  CA    . SER A 1 3963 ? 59.474  127.979 74.979  1.00 35.41  ? 3963 SER A CA    1 
ATOM   18020 C  C     . SER A 1 3963 ? 59.813  126.576 75.476  1.00 38.14  ? 3963 SER A C     1 
ATOM   18021 O  O     . SER A 1 3963 ? 60.980  126.204 75.626  1.00 38.35  ? 3963 SER A O     1 
ATOM   18022 C  CB    . SER A 1 3963 ? 59.186  127.958 73.478  1.00 37.10  ? 3963 SER A CB    1 
ATOM   18023 O  OG    . SER A 1 3963 ? 60.320  127.532 72.747  1.00 38.16  ? 3963 SER A OG    1 
ATOM   18024 N  N     . SER A 1 3964 ? 58.763  125.796 75.742  1.00 38.12  ? 3964 SER A N     1 
ATOM   18025 C  CA    . SER A 1 3964 ? 58.953  124.449 76.271  1.00 32.78  ? 3964 SER A CA    1 
ATOM   18026 C  C     . SER A 1 3964 ? 59.632  123.538 75.255  1.00 33.31  ? 3964 SER A C     1 
ATOM   18027 O  O     . SER A 1 3964 ? 60.516  122.751 75.613  1.00 33.01  ? 3964 SER A O     1 
ATOM   18028 C  CB    . SER A 1 3964 ? 57.610  123.863 76.704  1.00 31.24  ? 3964 SER A CB    1 
ATOM   18029 O  OG    . SER A 1 3964 ? 56.729  123.738 75.601  1.00 31.94  ? 3964 SER A OG    1 
ATOM   18030 N  N     . SER A 1 3965 ? 59.238  123.628 73.987  1.00 31.55  ? 3965 SER A N     1 
ATOM   18031 C  CA    . SER A 1 3965 ? 59.779  122.782 72.923  1.00 29.45  ? 3965 SER A CA    1 
ATOM   18032 C  C     . SER A 1 3965 ? 60.211  123.654 71.751  1.00 29.43  ? 3965 SER A C     1 
ATOM   18033 O  O     . SER A 1 3965 ? 59.583  123.645 70.686  1.00 33.78  ? 3965 SER A O     1 
ATOM   18034 C  CB    . SER A 1 3965 ? 58.752  121.740 72.480  1.00 35.66  ? 3965 SER A CB    1 
ATOM   18035 O  OG    . SER A 1 3965 ? 58.329  120.942 73.571  1.00 38.57  ? 3965 SER A OG    1 
ATOM   18036 N  N     . PRO A 1 3966 ? 61.287  124.429 71.916  1.00 27.78  ? 3966 PRO A N     1 
ATOM   18037 C  CA    . PRO A 1 3966 ? 61.748  125.283 70.811  1.00 30.06  ? 3966 PRO A CA    1 
ATOM   18038 C  C     . PRO A 1 3966 ? 62.223  124.514 69.588  1.00 29.59  ? 3966 PRO A C     1 
ATOM   18039 O  O     . PRO A 1 3966 ? 62.184  125.068 68.481  1.00 32.80  ? 3966 PRO A O     1 
ATOM   18040 C  CB    . PRO A 1 3966 ? 62.881  126.095 71.452  1.00 27.88  ? 3966 PRO A CB    1 
ATOM   18041 C  CG    . PRO A 1 3966 ? 63.389  125.223 72.534  1.00 24.47  ? 3966 PRO A CG    1 
ATOM   18042 C  CD    . PRO A 1 3966 ? 62.184  124.510 73.082  1.00 26.89  ? 3966 PRO A CD    1 
ATOM   18043 N  N     . GLU A 1 3967 ? 62.651  123.255 69.742  1.00 28.72  ? 3967 GLU A N     1 
ATOM   18044 C  CA    . GLU A 1 3967 ? 63.107  122.481 68.590  1.00 26.83  ? 3967 GLU A CA    1 
ATOM   18045 C  C     . GLU A 1 3967 ? 62.002  122.300 67.559  1.00 27.16  ? 3967 GLU A C     1 
ATOM   18046 O  O     . GLU A 1 3967 ? 62.289  122.119 66.371  1.00 33.08  ? 3967 GLU A O     1 
ATOM   18047 C  CB    . GLU A 1 3967 ? 63.639  121.114 69.033  1.00 20.67  ? 3967 GLU A CB    1 
ATOM   18048 C  CG    . GLU A 1 3967 ? 62.592  120.164 69.602  1.00 26.04  ? 3967 GLU A CG    1 
ATOM   18049 C  CD    . GLU A 1 3967 ? 62.186  120.504 71.024  1.00 28.44  ? 3967 GLU A CD    1 
ATOM   18050 O  OE1   . GLU A 1 3967 ? 62.796  121.416 71.620  1.00 28.42  ? 3967 GLU A OE1   1 
ATOM   18051 O  OE2   . GLU A 1 3967 ? 61.254  119.858 71.545  1.00 30.57  ? 3967 GLU A OE2   1 
ATOM   18052 N  N     . GLN A 1 3968 ? 60.743  122.349 67.989  1.00 28.82  ? 3968 GLN A N     1 
ATOM   18053 C  CA    . GLN A 1 3968 ? 59.628  122.230 67.062  1.00 31.77  ? 3968 GLN A CA    1 
ATOM   18054 C  C     . GLN A 1 3968 ? 59.394  123.502 66.261  1.00 34.08  ? 3968 GLN A C     1 
ATOM   18055 O  O     . GLN A 1 3968 ? 58.777  123.438 65.192  1.00 39.03  ? 3968 GLN A O     1 
ATOM   18056 C  CB    . GLN A 1 3968 ? 58.356  121.859 67.826  1.00 32.82  ? 3968 GLN A CB    1 
ATOM   18057 C  CG    . GLN A 1 3968 ? 58.393  120.474 68.450  1.00 36.73  ? 3968 GLN A CG    1 
ATOM   18058 C  CD    . GLN A 1 3968 ? 57.126  120.143 69.212  1.00 51.53  ? 3968 GLN A CD    1 
ATOM   18059 O  OE1   . GLN A 1 3968 ? 56.227  120.974 69.336  1.00 55.70  ? 3968 GLN A OE1   1 
ATOM   18060 N  NE2   . GLN A 1 3968 ? 57.049  118.922 69.729  1.00 52.41  ? 3968 GLN A NE2   1 
ATOM   18061 N  N     . THR A 1 3969 ? 59.868  124.649 66.744  1.00 31.14  ? 3969 THR A N     1 
ATOM   18062 C  CA    . THR A 1 3969 ? 59.630  125.936 66.098  1.00 32.59  ? 3969 THR A CA    1 
ATOM   18063 C  C     . THR A 1 3969 ? 60.910  126.754 66.021  1.00 36.37  ? 3969 THR A C     1 
ATOM   18064 O  O     . THR A 1 3969 ? 60.927  127.942 66.353  1.00 41.16  ? 3969 THR A O     1 
ATOM   18065 C  CB    . THR A 1 3969 ? 58.545  126.729 66.826  1.00 40.70  ? 3969 THR A CB    1 
ATOM   18066 O  OG1   . THR A 1 3969 ? 58.933  126.934 68.191  1.00 34.93  ? 3969 THR A OG1   1 
ATOM   18067 C  CG2   . THR A 1 3969 ? 57.208  125.998 66.781  1.00 42.46  ? 3969 THR A CG2   1 
ATOM   18068 N  N     . VAL A 1 3970 ? 62.004  126.138 65.582  1.00 35.95  ? 3970 VAL A N     1 
ATOM   18069 C  CA    . VAL A 1 3970 ? 63.272  126.853 65.460  1.00 37.59  ? 3970 VAL A CA    1 
ATOM   18070 C  C     . VAL A 1 3970 ? 63.129  127.903 64.366  1.00 42.70  ? 3970 VAL A C     1 
ATOM   18071 O  O     . VAL A 1 3970 ? 62.842  127.561 63.210  1.00 44.74  ? 3970 VAL A O     1 
ATOM   18072 C  CB    . VAL A 1 3970 ? 64.437  125.898 65.158  1.00 30.98  ? 3970 VAL A CB    1 
ATOM   18073 C  CG1   . VAL A 1 3970 ? 65.755  126.653 65.166  1.00 27.77  ? 3970 VAL A CG1   1 
ATOM   18074 C  CG2   . VAL A 1 3970 ? 64.465  124.756 66.155  1.00 27.36  ? 3970 VAL A CG2   1 
ATOM   18075 N  N     . PRO A 1 3971 ? 63.316  129.182 64.679  1.00 48.25  ? 3971 PRO A N     1 
ATOM   18076 C  CA    . PRO A 1 3971 ? 63.147  130.220 63.660  1.00 48.52  ? 3971 PRO A CA    1 
ATOM   18077 C  C     . PRO A 1 3971 ? 64.304  130.243 62.672  1.00 51.55  ? 3971 PRO A C     1 
ATOM   18078 O  O     . PRO A 1 3971 ? 65.418  129.804 62.965  1.00 50.12  ? 3971 PRO A O     1 
ATOM   18079 C  CB    . PRO A 1 3971 ? 63.081  131.510 64.484  1.00 47.25  ? 3971 PRO A CB    1 
ATOM   18080 C  CG    . PRO A 1 3971 ? 63.893  131.199 65.698  1.00 40.64  ? 3971 PRO A CG    1 
ATOM   18081 C  CD    . PRO A 1 3971 ? 63.648  129.747 65.998  1.00 36.43  ? 3971 PRO A CD    1 
ATOM   18082 N  N     . TYR A 1 3972 ? 64.016  130.771 61.481  1.00 55.47  ? 3972 TYR A N     1 
ATOM   18083 C  CA    . TYR A 1 3972 ? 64.962  130.797 60.365  1.00 52.61  ? 3972 TYR A CA    1 
ATOM   18084 C  C     . TYR A 1 3972 ? 66.023  131.860 60.641  1.00 55.48  ? 3972 TYR A C     1 
ATOM   18085 O  O     . TYR A 1 3972 ? 65.843  133.054 60.390  1.00 64.00  ? 3972 TYR A O     1 
ATOM   18086 C  CB    . TYR A 1 3972 ? 64.216  131.062 59.062  1.00 52.04  ? 3972 TYR A CB    1 
ATOM   18087 C  CG    . TYR A 1 3972 ? 65.074  131.041 57.817  1.00 61.33  ? 3972 TYR A CG    1 
ATOM   18088 C  CD1   . TYR A 1 3972 ? 65.518  129.841 57.279  1.00 56.15  ? 3972 TYR A CD1   1 
ATOM   18089 C  CD2   . TYR A 1 3972 ? 65.423  132.219 57.170  1.00 68.44  ? 3972 TYR A CD2   1 
ATOM   18090 C  CE1   . TYR A 1 3972 ? 66.295  129.814 56.137  1.00 59.05  ? 3972 TYR A CE1   1 
ATOM   18091 C  CE2   . TYR A 1 3972 ? 66.201  132.202 56.027  1.00 69.35  ? 3972 TYR A CE2   1 
ATOM   18092 C  CZ    . TYR A 1 3972 ? 66.633  130.997 55.516  1.00 66.56  ? 3972 TYR A CZ    1 
ATOM   18093 O  OH    . TYR A 1 3972 ? 67.407  130.975 54.379  1.00 71.41  ? 3972 TYR A OH    1 
ATOM   18094 N  N     . LEU A 1 3973 ? 67.159  131.410 61.175  1.00 50.97  ? 3973 LEU A N     1 
ATOM   18095 C  CA    . LEU A 1 3973 ? 68.233  132.296 61.608  1.00 50.25  ? 3973 LEU A CA    1 
ATOM   18096 C  C     . LEU A 1 3973 ? 69.519  132.140 60.806  1.00 53.20  ? 3973 LEU A C     1 
ATOM   18097 O  O     . LEU A 1 3973 ? 70.501  132.827 61.106  1.00 57.87  ? 3973 LEU A O     1 
ATOM   18098 C  CB    . LEU A 1 3973 ? 68.534  132.075 63.095  1.00 47.44  ? 3973 LEU A CB    1 
ATOM   18099 C  CG    . LEU A 1 3973 ? 67.826  132.962 64.123  1.00 50.32  ? 3973 LEU A CG    1 
ATOM   18100 C  CD1   . LEU A 1 3973 ? 68.340  134.383 64.034  1.00 53.68  ? 3973 LEU A CD1   1 
ATOM   18101 C  CD2   . LEU A 1 3973 ? 66.331  132.947 63.913  1.00 56.00  ? 3973 LEU A CD2   1 
ATOM   18102 N  N     . TRP A 1 3974 ? 69.550  131.265 59.806  1.00 52.31  ? 3974 TRP A N     1 
ATOM   18103 C  CA    . TRP A 1 3974 ? 70.737  131.077 58.983  1.00 52.04  ? 3974 TRP A CA    1 
ATOM   18104 C  C     . TRP A 1 3974 ? 70.514  131.700 57.612  1.00 57.09  ? 3974 TRP A C     1 
ATOM   18105 O  O     . TRP A 1 3974 ? 69.432  131.565 57.030  1.00 58.73  ? 3974 TRP A O     1 
ATOM   18106 C  CB    . TRP A 1 3974 ? 71.088  129.594 58.844  1.00 47.73  ? 3974 TRP A CB    1 
ATOM   18107 C  CG    . TRP A 1 3974 ? 70.049  128.777 58.144  1.00 44.22  ? 3974 TRP A CG    1 
ATOM   18108 C  CD1   . TRP A 1 3974 ? 69.995  128.487 56.813  1.00 43.31  ? 3974 TRP A CD1   1 
ATOM   18109 C  CD2   . TRP A 1 3974 ? 68.916  128.134 58.741  1.00 47.35  ? 3974 TRP A CD2   1 
ATOM   18110 N  NE1   . TRP A 1 3974 ? 68.897  127.707 56.541  1.00 45.30  ? 3974 TRP A NE1   1 
ATOM   18111 C  CE2   . TRP A 1 3974 ? 68.219  127.476 57.709  1.00 51.28  ? 3974 TRP A CE2   1 
ATOM   18112 C  CE3   . TRP A 1 3974 ? 68.424  128.053 60.047  1.00 39.79  ? 3974 TRP A CE3   1 
ATOM   18113 C  CZ2   . TRP A 1 3974 ? 67.055  126.747 57.942  1.00 45.61  ? 3974 TRP A CZ2   1 
ATOM   18114 C  CZ3   . TRP A 1 3974 ? 67.268  127.329 60.276  1.00 42.03  ? 3974 TRP A CZ3   1 
ATOM   18115 C  CH2   . TRP A 1 3974 ? 66.597  126.686 59.229  1.00 40.78  ? 3974 TRP A CH2   1 
ATOM   18116 N  N     . SER A 1 3975 ? 71.537  132.382 57.104  1.00 59.52  ? 3975 SER A N     1 
ATOM   18117 C  CA    . SER A 1 3975 ? 71.468  133.039 55.805  1.00 65.43  ? 3975 SER A CA    1 
ATOM   18118 C  C     . SER A 1 3975 ? 72.053  132.115 54.744  1.00 62.51  ? 3975 SER A C     1 
ATOM   18119 O  O     . SER A 1 3975 ? 73.190  131.651 54.876  1.00 65.51  ? 3975 SER A O     1 
ATOM   18120 C  CB    . SER A 1 3975 ? 72.218  134.370 55.833  1.00 66.44  ? 3975 SER A CB    1 
ATOM   18121 O  OG    . SER A 1 3975 ? 73.576  134.184 56.192  1.00 67.33  ? 3975 SER A OG    1 
ATOM   18122 N  N     . GLU A 1 3976 ? 71.275  131.848 53.698  1.00 68.02  ? 3976 GLU A N     1 
ATOM   18123 C  CA    . GLU A 1 3976 ? 71.702  130.976 52.615  1.00 71.80  ? 3976 GLU A CA    1 
ATOM   18124 C  C     . GLU A 1 3976 ? 71.086  131.450 51.307  1.00 76.26  ? 3976 GLU A C     1 
ATOM   18125 O  O     . GLU A 1 3976 ? 69.922  131.857 51.270  1.00 74.59  ? 3976 GLU A O     1 
ATOM   18126 C  CB    . GLU A 1 3976 ? 71.322  129.516 52.898  1.00 70.49  ? 3976 GLU A CB    1 
ATOM   18127 C  CG    . GLU A 1 3976 ? 69.827  129.258 52.975  1.00 66.98  ? 3976 GLU A CG    1 
ATOM   18128 C  CD    . GLU A 1 3976 ? 69.503  127.819 53.314  1.00 67.73  ? 3976 GLU A CD    1 
ATOM   18129 O  OE1   . GLU A 1 3976 ? 70.450  127.028 53.510  1.00 65.53  ? 3976 GLU A OE1   1 
ATOM   18130 O  OE2   . GLU A 1 3976 ? 68.303  127.480 53.386  1.00 66.98  ? 3976 GLU A OE2   1 
ATOM   18131 N  N     . GLU A 1 3977 ? 71.885  131.413 50.239  1.00 80.74  ? 3977 GLU A N     1 
ATOM   18132 C  CA    . GLU A 1 3977 ? 71.399  131.847 48.933  1.00 83.88  ? 3977 GLU A CA    1 
ATOM   18133 C  C     . GLU A 1 3977 ? 70.368  130.872 48.378  1.00 82.28  ? 3977 GLU A C     1 
ATOM   18134 O  O     . GLU A 1 3977 ? 69.294  131.281 47.920  1.00 84.20  ? 3977 GLU A O     1 
ATOM   18135 C  CB    . GLU A 1 3977 ? 72.569  132.010 47.960  1.00 82.54  ? 3977 GLU A CB    1 
ATOM   18136 C  CG    . GLU A 1 3977 ? 73.595  133.066 48.363  1.00 88.41  ? 3977 GLU A CG    1 
ATOM   18137 C  CD    . GLU A 1 3977 ? 74.548  132.594 49.448  1.00 91.56  ? 3977 GLU A CD    1 
ATOM   18138 O  OE1   . GLU A 1 3977 ? 74.445  131.422 49.869  1.00 85.40  ? 3977 GLU A OE1   1 
ATOM   18139 O  OE2   . GLU A 1 3977 ? 75.399  133.398 49.882  1.00 95.60  ? 3977 GLU A OE2   1 
ATOM   18140 N  N     . THR A 1 3978 ? 70.675  129.578 48.410  1.00 79.14  ? 3978 THR A N     1 
ATOM   18141 C  CA    . THR A 1 3978 ? 69.708  128.600 47.935  1.00 79.48  ? 3978 THR A CA    1 
ATOM   18142 C  C     . THR A 1 3978 ? 68.995  127.943 49.112  1.00 76.94  ? 3978 THR A C     1 
ATOM   18143 O  O     . THR A 1 3978 ? 69.598  127.754 50.175  1.00 74.37  ? 3978 THR A O     1 
ATOM   18144 C  CB    . THR A 1 3978 ? 70.391  127.529 47.078  1.00 77.75  ? 3978 THR A CB    1 
ATOM   18145 O  OG1   . THR A 1 3978 ? 69.406  126.654 46.513  1.00 71.38  ? 3978 THR A OG1   1 
ATOM   18146 C  CG2   . THR A 1 3978 ? 71.389  126.716 47.898  1.00 74.94  ? 3978 THR A CG2   1 
ATOM   18147 N  N     . PRO A 1 3979 ? 67.711  127.618 48.972  1.00 75.34  ? 3979 PRO A N     1 
ATOM   18148 C  CA    . PRO A 1 3979 ? 66.992  126.974 50.079  1.00 71.51  ? 3979 PRO A CA    1 
ATOM   18149 C  C     . PRO A 1 3979 ? 67.611  125.629 50.433  1.00 66.87  ? 3979 PRO A C     1 
ATOM   18150 O  O     . PRO A 1 3979 ? 67.911  124.813 49.558  1.00 65.22  ? 3979 PRO A O     1 
ATOM   18151 C  CB    . PRO A 1 3979 ? 65.567  126.818 49.536  1.00 66.42  ? 3979 PRO A CB    1 
ATOM   18152 C  CG    . PRO A 1 3979 ? 65.460  127.837 48.449  1.00 68.88  ? 3979 PRO A CG    1 
ATOM   18153 C  CD    . PRO A 1 3979 ? 66.823  127.914 47.836  1.00 71.46  ? 3979 PRO A CD    1 
ATOM   18154 N  N     . ALA A 1 3980 ? 67.802  125.406 51.729  1.00 67.31  ? 3980 ALA A N     1 
ATOM   18155 C  CA    . ALA A 1 3980 ? 68.369  124.152 52.195  1.00 57.14  ? 3980 ALA A CA    1 
ATOM   18156 C  C     . ALA A 1 3980 ? 67.358  123.021 52.058  1.00 50.21  ? 3980 ALA A C     1 
ATOM   18157 O  O     . ALA A 1 3980 ? 66.143  123.232 52.095  1.00 48.31  ? 3980 ALA A O     1 
ATOM   18158 C  CB    . ALA A 1 3980 ? 68.821  124.271 53.650  1.00 46.25  ? 3980 ALA A CB    1 
ATOM   18159 N  N     . THR A 1 3981 ? 67.877  121.808 51.895  1.00 45.53  ? 3981 THR A N     1 
ATOM   18160 C  CA    . THR A 1 3981 ? 67.032  120.631 51.887  1.00 42.51  ? 3981 THR A CA    1 
ATOM   18161 C  C     . THR A 1 3981 ? 66.442  120.414 53.278  1.00 38.67  ? 3981 THR A C     1 
ATOM   18162 O  O     . THR A 1 3981 ? 66.960  120.937 54.268  1.00 35.29  ? 3981 THR A O     1 
ATOM   18163 C  CB    . THR A 1 3981 ? 67.833  119.406 51.454  1.00 38.63  ? 3981 THR A CB    1 
ATOM   18164 O  OG1   . THR A 1 3981 ? 68.824  119.105 52.444  1.00 41.63  ? 3981 THR A OG1   1 
ATOM   18165 C  CG2   . THR A 1 3981 ? 68.519  119.665 50.122  1.00 36.45  ? 3981 THR A CG2   1 
ATOM   18166 N  N     . PRO A 1 3982 ? 65.336  119.668 53.376  1.00 35.39  ? 3982 PRO A N     1 
ATOM   18167 C  CA    . PRO A 1 3982 ? 64.768  119.386 54.705  1.00 36.73  ? 3982 PRO A CA    1 
ATOM   18168 C  C     . PRO A 1 3982 ? 65.776  118.795 55.676  1.00 33.38  ? 3982 PRO A C     1 
ATOM   18169 O  O     . PRO A 1 3982 ? 65.749  119.122 56.868  1.00 33.77  ? 3982 PRO A O     1 
ATOM   18170 C  CB    . PRO A 1 3982 ? 63.640  118.400 54.385  1.00 32.10  ? 3982 PRO A CB    1 
ATOM   18171 C  CG    . PRO A 1 3982 ? 63.184  118.801 53.027  1.00 32.56  ? 3982 PRO A CG    1 
ATOM   18172 C  CD    . PRO A 1 3982 ? 64.406  119.303 52.292  1.00 34.02  ? 3982 PRO A CD    1 
ATOM   18173 N  N     . ILE A 1 3983 ? 66.677  117.939 55.194  1.00 31.28  ? 3983 ILE A N     1 
ATOM   18174 C  CA    . ILE A 1 3983 ? 67.736  117.417 56.051  1.00 31.20  ? 3983 ILE A CA    1 
ATOM   18175 C  C     . ILE A 1 3983 ? 68.745  118.519 56.370  1.00 28.98  ? 3983 ILE A C     1 
ATOM   18176 O  O     . ILE A 1 3983 ? 69.254  118.617 57.497  1.00 26.90  ? 3983 ILE A O     1 
ATOM   18177 C  CB    . ILE A 1 3983 ? 68.393  116.198 55.376  1.00 31.61  ? 3983 ILE A CB    1 
ATOM   18178 C  CG1   . ILE A 1 3983 ? 67.441  115.005 55.402  1.00 31.73  ? 3983 ILE A CG1   1 
ATOM   18179 C  CG2   . ILE A 1 3983 ? 69.635  115.774 56.119  1.00 23.48  ? 3983 ILE A CG2   1 
ATOM   18180 C  CD1   . ILE A 1 3983 ? 67.786  113.928 54.400  1.00 26.79  ? 3983 ILE A CD1   1 
ATOM   18181 N  N     . GLY A 1 3984 ? 69.056  119.365 55.382  1.00 30.88  ? 3984 GLY A N     1 
ATOM   18182 C  CA    . GLY A 1 3984 ? 69.901  120.521 55.648  1.00 29.22  ? 3984 GLY A CA    1 
ATOM   18183 C  C     . GLY A 1 3984 ? 69.265  121.485 56.628  1.00 31.34  ? 3984 GLY A C     1 
ATOM   18184 O  O     . GLY A 1 3984 ? 69.937  122.025 57.514  1.00 26.87  ? 3984 GLY A O     1 
ATOM   18185 N  N     . GLN A 1 3985 ? 67.957  121.706 56.490  1.00 30.51  ? 3985 GLN A N     1 
ATOM   18186 C  CA    . GLN A 1 3985 ? 67.236  122.488 57.484  1.00 31.25  ? 3985 GLN A CA    1 
ATOM   18187 C  C     . GLN A 1 3985 ? 67.324  121.831 58.853  1.00 28.56  ? 3985 GLN A C     1 
ATOM   18188 O  O     . GLN A 1 3985 ? 67.450  122.518 59.869  1.00 30.42  ? 3985 GLN A O     1 
ATOM   18189 C  CB    . GLN A 1 3985 ? 65.777  122.662 57.062  1.00 33.88  ? 3985 GLN A CB    1 
ATOM   18190 C  CG    . GLN A 1 3985 ? 65.506  123.933 56.277  1.00 38.76  ? 3985 GLN A CG    1 
ATOM   18191 C  CD    . GLN A 1 3985 ? 64.321  123.797 55.341  1.00 53.29  ? 3985 GLN A CD    1 
ATOM   18192 O  OE1   . GLN A 1 3985 ? 63.315  123.173 55.682  1.00 47.65  ? 3985 GLN A OE1   1 
ATOM   18193 N  NE2   . GLN A 1 3985 ? 64.433  124.380 54.154  1.00 56.45  ? 3985 GLN A NE2   1 
ATOM   18194 N  N     . ALA A 1 3986 ? 67.264  120.498 58.896  1.00 27.75  ? 3986 ALA A N     1 
ATOM   18195 C  CA    . ALA A 1 3986 ? 67.380  119.788 60.164  1.00 21.28  ? 3986 ALA A CA    1 
ATOM   18196 C  C     . ALA A 1 3986 ? 68.730  120.043 60.822  1.00 21.02  ? 3986 ALA A C     1 
ATOM   18197 O  O     . ALA A 1 3986 ? 68.801  120.280 62.031  1.00 20.68  ? 3986 ALA A O     1 
ATOM   18198 C  CB    . ALA A 1 3986 ? 67.160  118.291 59.951  1.00 20.26  ? 3986 ALA A CB    1 
ATOM   18199 N  N     . ILE A 1 3987 ? 69.814  120.006 60.042  1.00 19.95  ? 3987 ILE A N     1 
ATOM   18200 C  CA    . ILE A 1 3987 ? 71.126  120.298 60.624  1.00 21.17  ? 3987 ILE A CA    1 
ATOM   18201 C  C     . ILE A 1 3987 ? 71.218  121.755 61.069  1.00 24.41  ? 3987 ILE A C     1 
ATOM   18202 O  O     . ILE A 1 3987 ? 71.827  122.059 62.103  1.00 23.15  ? 3987 ILE A O     1 
ATOM   18203 C  CB    . ILE A 1 3987 ? 72.280  119.930 59.671  1.00 24.09  ? 3987 ILE A CB    1 
ATOM   18204 C  CG1   . ILE A 1 3987 ? 72.350  118.423 59.449  1.00 27.09  ? 3987 ILE A CG1   1 
ATOM   18205 C  CG2   . ILE A 1 3987 ? 73.609  120.437 60.198  1.00 25.07  ? 3987 ILE A CG2   1 
ATOM   18206 C  CD1   . ILE A 1 3987 ? 73.359  118.031 58.407  1.00 26.40  ? 3987 ILE A CD1   1 
ATOM   18207 N  N     . HIS A 1 3988 ? 70.640  122.680 60.302  1.00 26.82  ? 3988 HIS A N     1 
ATOM   18208 C  CA    . HIS A 1 3988 ? 70.681  124.081 60.719  1.00 24.71  ? 3988 HIS A CA    1 
ATOM   18209 C  C     . HIS A 1 3988 ? 69.932  124.292 62.033  1.00 24.37  ? 3988 HIS A C     1 
ATOM   18210 O  O     . HIS A 1 3988 ? 70.420  124.992 62.932  1.00 25.70  ? 3988 HIS A O     1 
ATOM   18211 C  CB    . HIS A 1 3988 ? 70.120  124.979 59.618  1.00 28.43  ? 3988 HIS A CB    1 
ATOM   18212 C  CG    . HIS A 1 3988 ? 71.049  125.159 58.457  1.00 35.54  ? 3988 HIS A CG    1 
ATOM   18213 N  ND1   . HIS A 1 3988 ? 72.285  125.755 58.581  1.00 37.59  ? 3988 HIS A ND1   1 
ATOM   18214 C  CD2   . HIS A 1 3988 ? 70.921  124.827 57.151  1.00 38.03  ? 3988 HIS A CD2   1 
ATOM   18215 C  CE1   . HIS A 1 3988 ? 72.881  125.777 57.402  1.00 35.99  ? 3988 HIS A CE1   1 
ATOM   18216 N  NE2   . HIS A 1 3988 ? 72.074  125.221 56.517  1.00 32.32  ? 3988 HIS A NE2   1 
ATOM   18217 N  N     . ARG A 1 3989 ? 68.751  123.682 62.170  1.00 23.61  ? 3989 ARG A N     1 
ATOM   18218 C  CA    . ARG A 1 3989 ? 68.026  123.743 63.435  1.00 23.44  ? 3989 ARG A CA    1 
ATOM   18219 C  C     . ARG A 1 3989 ? 68.797  123.061 64.556  1.00 21.21  ? 3989 ARG A C     1 
ATOM   18220 O  O     . ARG A 1 3989 ? 68.760  123.521 65.699  1.00 22.96  ? 3989 ARG A O     1 
ATOM   18221 C  CB    . ARG A 1 3989 ? 66.639  123.110 63.293  1.00 21.03  ? 3989 ARG A CB    1 
ATOM   18222 C  CG    . ARG A 1 3989 ? 65.848  123.584 62.091  1.00 24.05  ? 3989 ARG A CG    1 
ATOM   18223 C  CD    . ARG A 1 3989 ? 64.368  123.699 62.389  1.00 25.80  ? 3989 ARG A CD    1 
ATOM   18224 N  NE    . ARG A 1 3989 ? 63.646  124.317 61.284  1.00 32.92  ? 3989 ARG A NE    1 
ATOM   18225 C  CZ    . ARG A 1 3989 ? 63.102  123.646 60.278  1.00 35.07  ? 3989 ARG A CZ    1 
ATOM   18226 N  NH1   . ARG A 1 3989 ? 63.179  122.328 60.204  1.00 32.27  ? 3989 ARG A NH1   1 
ATOM   18227 N  NH2   . ARG A 1 3989 ? 62.465  124.316 59.322  1.00 38.18  ? 3989 ARG A NH2   1 
ATOM   18228 N  N     . LEU A 1 3990 ? 69.493  121.963 64.252  1.00 15.73  ? 3990 LEU A N     1 
ATOM   18229 C  CA    . LEU A 1 3990 ? 70.305  121.291 65.259  1.00 16.51  ? 3990 LEU A CA    1 
ATOM   18230 C  C     . LEU A 1 3990 ? 71.415  122.203 65.763  1.00 22.49  ? 3990 LEU A C     1 
ATOM   18231 O  O     . LEU A 1 3990 ? 71.674  122.272 66.971  1.00 25.92  ? 3990 LEU A O     1 
ATOM   18232 C  CB    . LEU A 1 3990 ? 70.884  120.004 64.671  1.00 17.83  ? 3990 LEU A CB    1 
ATOM   18233 C  CG    . LEU A 1 3990 ? 71.679  119.058 65.570  1.00 19.81  ? 3990 LEU A CG    1 
ATOM   18234 C  CD1   . LEU A 1 3990 ? 70.792  118.494 66.666  1.00 17.18  ? 3990 LEU A CD1   1 
ATOM   18235 C  CD2   . LEU A 1 3990 ? 72.286  117.939 64.740  1.00 22.17  ? 3990 LEU A CD2   1 
ATOM   18236 N  N     . LEU A 1 3991 ? 72.072  122.915 64.847  1.00 26.32  ? 3991 LEU A N     1 
ATOM   18237 C  CA    . LEU A 1 3991 ? 73.109  123.866 65.232  1.00 20.75  ? 3991 LEU A CA    1 
ATOM   18238 C  C     . LEU A 1 3991 ? 72.534  124.993 66.076  1.00 24.59  ? 3991 LEU A C     1 
ATOM   18239 O  O     . LEU A 1 3991 ? 73.112  125.370 67.105  1.00 24.70  ? 3991 LEU A O     1 
ATOM   18240 C  CB    . LEU A 1 3991 ? 73.787  124.424 63.983  1.00 24.29  ? 3991 LEU A CB    1 
ATOM   18241 C  CG    . LEU A 1 3991 ? 74.648  123.424 63.214  1.00 24.78  ? 3991 LEU A CG    1 
ATOM   18242 C  CD1   . LEU A 1 3991 ? 75.001  123.976 61.843  1.00 29.80  ? 3991 LEU A CD1   1 
ATOM   18243 C  CD2   . LEU A 1 3991 ? 75.894  123.077 64.010  1.00 26.40  ? 3991 LEU A CD2   1 
ATOM   18244 N  N     . LEU A 1 3992 ? 71.387  125.536 65.662  1.00 20.72  ? 3992 LEU A N     1 
ATOM   18245 C  CA    . LEU A 1 3992 ? 70.768  126.618 66.421  1.00 24.58  ? 3992 LEU A CA    1 
ATOM   18246 C  C     . LEU A 1 3992 ? 70.373  126.153 67.817  1.00 23.96  ? 3992 LEU A C     1 
ATOM   18247 O  O     . LEU A 1 3992 ? 70.525  126.895 68.794  1.00 25.62  ? 3992 LEU A O     1 
ATOM   18248 C  CB    . LEU A 1 3992 ? 69.554  127.158 65.666  1.00 25.05  ? 3992 LEU A CB    1 
ATOM   18249 C  CG    . LEU A 1 3992 ? 69.872  128.102 64.504  1.00 26.92  ? 3992 LEU A CG    1 
ATOM   18250 C  CD1   . LEU A 1 3992 ? 68.631  128.372 63.669  1.00 32.30  ? 3992 LEU A CD1   1 
ATOM   18251 C  CD2   . LEU A 1 3992 ? 70.468  129.402 65.020  1.00 26.75  ? 3992 LEU A CD2   1 
ATOM   18252 N  N     . ILE A 1 3993 ? 69.873  124.922 67.931  1.00 23.31  ? 3993 ILE A N     1 
ATOM   18253 C  CA    . ILE A 1 3993 ? 69.441  124.409 69.224  1.00 21.29  ? 3993 ILE A CA    1 
ATOM   18254 C  C     . ILE A 1 3993 ? 70.642  124.153 70.125  1.00 20.94  ? 3993 ILE A C     1 
ATOM   18255 O  O     . ILE A 1 3993 ? 70.626  124.492 71.313  1.00 24.43  ? 3993 ILE A O     1 
ATOM   18256 C  CB    . ILE A 1 3993 ? 68.587  123.144 69.033  1.00 21.05  ? 3993 ILE A CB    1 
ATOM   18257 C  CG1   . ILE A 1 3993 ? 67.232  123.525 68.438  1.00 19.75  ? 3993 ILE A CG1   1 
ATOM   18258 C  CG2   . ILE A 1 3993 ? 68.412  122.405 70.349  1.00 16.18  ? 3993 ILE A CG2   1 
ATOM   18259 C  CD1   . ILE A 1 3993 ? 66.447  124.475 69.291  1.00 20.24  ? 3993 ILE A CD1   1 
ATOM   18260 N  N     . GLN A 1 3994 ? 71.707  123.561 69.576  1.00 19.16  ? 3994 GLN A N     1 
ATOM   18261 C  CA    . GLN A 1 3994 ? 72.922  123.366 70.359  1.00 18.74  ? 3994 GLN A CA    1 
ATOM   18262 C  C     . GLN A 1 3994 ? 73.478  124.697 70.844  1.00 25.03  ? 3994 GLN A C     1 
ATOM   18263 O  O     . GLN A 1 3994 ? 73.969  124.800 71.974  1.00 24.75  ? 3994 GLN A O     1 
ATOM   18264 C  CB    . GLN A 1 3994 ? 73.966  122.619 69.530  1.00 19.99  ? 3994 GLN A CB    1 
ATOM   18265 C  CG    . GLN A 1 3994 ? 75.338  122.521 70.176  1.00 19.28  ? 3994 GLN A CG    1 
ATOM   18266 C  CD    . GLN A 1 3994 ? 76.330  121.761 69.319  1.00 24.51  ? 3994 GLN A CD    1 
ATOM   18267 O  OE1   . GLN A 1 3994 ? 76.632  122.163 68.195  1.00 27.81  ? 3994 GLN A OE1   1 
ATOM   18268 N  NE2   . GLN A 1 3994 ? 76.840  120.653 69.843  1.00 26.51  ? 3994 GLN A NE2   1 
ATOM   18269 N  N     . ALA A 1 3995 ? 73.406  125.731 70.003  1.00 29.17  ? 3995 ALA A N     1 
ATOM   18270 C  CA    . ALA A 1 3995 ? 73.886  127.045 70.411  1.00 26.19  ? 3995 ALA A CA    1 
ATOM   18271 C  C     . ALA A 1 3995 ? 73.006  127.655 71.498  1.00 29.51  ? 3995 ALA A C     1 
ATOM   18272 O  O     . ALA A 1 3995 ? 73.516  128.253 72.452  1.00 32.36  ? 3995 ALA A O     1 
ATOM   18273 C  CB    . ALA A 1 3995 ? 73.964  127.974 69.200  1.00 25.99  ? 3995 ALA A CB    1 
ATOM   18274 N  N     . PHE A 1 3996 ? 71.686  127.512 71.380  1.00 27.95  ? 3996 PHE A N     1 
ATOM   18275 C  CA    . PHE A 1 3996 ? 70.772  128.278 72.219  1.00 26.29  ? 3996 PHE A CA    1 
ATOM   18276 C  C     . PHE A 1 3996 ? 70.090  127.452 73.303  1.00 29.50  ? 3996 PHE A C     1 
ATOM   18277 O  O     . PHE A 1 3996 ? 69.990  127.910 74.445  1.00 33.48  ? 3996 PHE A O     1 
ATOM   18278 C  CB    . PHE A 1 3996 ? 69.710  128.952 71.348  1.00 29.91  ? 3996 PHE A CB    1 
ATOM   18279 C  CG    . PHE A 1 3996 ? 70.202  130.186 70.650  1.00 34.82  ? 3996 PHE A CG    1 
ATOM   18280 C  CD1   . PHE A 1 3996 ? 70.634  130.125 69.335  1.00 35.80  ? 3996 PHE A CD1   1 
ATOM   18281 C  CD2   . PHE A 1 3996 ? 70.259  131.400 71.312  1.00 39.91  ? 3996 PHE A CD2   1 
ATOM   18282 C  CE1   . PHE A 1 3996 ? 71.096  131.254 68.689  1.00 38.49  ? 3996 PHE A CE1   1 
ATOM   18283 C  CE2   . PHE A 1 3996 ? 70.724  132.532 70.671  1.00 45.67  ? 3996 PHE A CE2   1 
ATOM   18284 C  CZ    . PHE A 1 3996 ? 71.139  132.459 69.357  1.00 44.97  ? 3996 PHE A CZ    1 
ATOM   18285 N  N     . ARG A 1 3997 ? 69.619  126.248 72.985  1.00 21.22  ? 3997 ARG A N     1 
ATOM   18286 C  CA    . ARG A 1 3997 ? 68.879  125.411 73.930  1.00 18.10  ? 3997 ARG A CA    1 
ATOM   18287 C  C     . ARG A 1 3997 ? 69.514  124.027 73.990  1.00 17.16  ? 3997 ARG A C     1 
ATOM   18288 O  O     . ARG A 1 3997 ? 68.968  123.054 73.457  1.00 22.45  ? 3997 ARG A O     1 
ATOM   18289 C  CB    . ARG A 1 3997 ? 67.404  125.320 73.539  1.00 20.84  ? 3997 ARG A CB    1 
ATOM   18290 C  CG    . ARG A 1 3997 ? 66.638  126.625 73.689  1.00 28.04  ? 3997 ARG A CG    1 
ATOM   18291 C  CD    . ARG A 1 3997 ? 66.726  127.157 75.111  1.00 24.85  ? 3997 ARG A CD    1 
ATOM   18292 N  NE    . ARG A 1 3997 ? 66.112  126.248 76.072  1.00 27.26  ? 3997 ARG A NE    1 
ATOM   18293 C  CZ    . ARG A 1 3997 ? 64.805  126.062 76.204  1.00 26.93  ? 3997 ARG A CZ    1 
ATOM   18294 N  NH1   . ARG A 1 3997 ? 63.933  126.729 75.467  1.00 22.83  ? 3997 ARG A NH1   1 
ATOM   18295 N  NH2   . ARG A 1 3997 ? 64.363  125.187 77.103  1.00 31.19  ? 3997 ARG A NH2   1 
ATOM   18296 N  N     . PRO A 1 3998 ? 70.680  123.906 74.631  1.00 19.31  ? 3998 PRO A N     1 
ATOM   18297 C  CA    . PRO A 1 3998 ? 71.337  122.592 74.713  1.00 18.24  ? 3998 PRO A CA    1 
ATOM   18298 C  C     . PRO A 1 3998 ? 70.510  121.537 75.427  1.00 18.52  ? 3998 PRO A C     1 
ATOM   18299 O  O     . PRO A 1 3998 ? 70.618  120.353 75.083  1.00 20.03  ? 3998 PRO A O     1 
ATOM   18300 C  CB    . PRO A 1 3998 ? 72.636  122.896 75.472  1.00 16.47  ? 3998 PRO A CB    1 
ATOM   18301 C  CG    . PRO A 1 3998 ? 72.354  124.153 76.223  1.00 17.57  ? 3998 PRO A CG    1 
ATOM   18302 C  CD    . PRO A 1 3998 ? 71.429  124.947 75.354  1.00 20.18  ? 3998 PRO A CD    1 
ATOM   18303 N  N     . ASP A 1 3999 ? 69.684  121.925 76.402  1.00 19.19  ? 3999 ASP A N     1 
ATOM   18304 C  CA    . ASP A 1 3999 ? 68.859  120.961 77.120  1.00 16.70  ? 3999 ASP A CA    1 
ATOM   18305 C  C     . ASP A 1 3999 ? 67.883  120.234 76.205  1.00 14.60  ? 3999 ASP A C     1 
ATOM   18306 O  O     . ASP A 1 3999 ? 67.463  119.119 76.526  1.00 16.80  ? 3999 ASP A O     1 
ATOM   18307 C  CB    . ASP A 1 3999 ? 68.092  121.660 78.243  1.00 17.34  ? 3999 ASP A CB    1 
ATOM   18308 C  CG    . ASP A 1 3999 ? 67.413  122.933 77.777  1.00 21.93  ? 3999 ASP A CG    1 
ATOM   18309 O  OD1   . ASP A 1 3999 ? 68.114  123.827 77.260  1.00 24.09  ? 3999 ASP A OD1   1 
ATOM   18310 O  OD2   . ASP A 1 3999 ? 66.178  123.040 77.929  1.00 24.95  ? 3999 ASP A OD2   1 
ATOM   18311 N  N     . ARG A 1 4000 ? 67.514  120.838 75.077  1.00 13.68  ? 4000 ARG A N     1 
ATOM   18312 C  CA    . ARG A 1 4000 ? 66.631  120.217 74.104  1.00 16.27  ? 4000 ARG A CA    1 
ATOM   18313 C  C     . ARG A 1 4000 ? 67.392  119.574 72.949  1.00 11.04  ? 4000 ARG A C     1 
ATOM   18314 O  O     . ARG A 1 4000 ? 66.764  119.056 72.017  1.00 13.48  ? 4000 ARG A O     1 
ATOM   18315 C  CB    . ARG A 1 4000 ? 65.637  121.247 73.575  1.00 14.89  ? 4000 ARG A CB    1 
ATOM   18316 C  CG    . ARG A 1 4000 ? 64.831  121.961 74.644  1.00 19.14  ? 4000 ARG A CG    1 
ATOM   18317 C  CD    . ARG A 1 4000 ? 64.022  120.968 75.456  1.00 20.55  ? 4000 ARG A CD    1 
ATOM   18318 N  NE    . ARG A 1 4000 ? 63.056  120.274 74.614  1.00 22.20  ? 4000 ARG A NE    1 
ATOM   18319 C  CZ    . ARG A 1 4000 ? 62.274  119.285 75.023  1.00 25.81  ? 4000 ARG A CZ    1 
ATOM   18320 N  NH1   . ARG A 1 4000 ? 62.315  118.841 76.268  1.00 34.39  ? 4000 ARG A NH1   1 
ATOM   18321 N  NH2   . ARG A 1 4000 ? 61.428  118.728 74.161  1.00 20.42  ? 4000 ARG A NH2   1 
ATOM   18322 N  N     . LEU A 1 4001 ? 68.729  119.583 73.005  1.00 12.21  ? 4001 LEU A N     1 
ATOM   18323 C  CA    . LEU A 1 4001 ? 69.533  119.044 71.912  1.00 13.68  ? 4001 LEU A CA    1 
ATOM   18324 C  C     . LEU A 1 4001 ? 69.097  117.633 71.544  1.00 11.20  ? 4001 LEU A C     1 
ATOM   18325 O  O     . LEU A 1 4001 ? 68.821  117.351 70.370  1.00 11.11  ? 4001 LEU A O     1 
ATOM   18326 C  CB    . LEU A 1 4001 ? 71.013  119.055 72.293  1.00 14.24  ? 4001 LEU A CB    1 
ATOM   18327 C  CG    . LEU A 1 4001 ? 71.988  118.647 71.187  1.00 16.42  ? 4001 LEU A CG    1 
ATOM   18328 C  CD1   . LEU A 1 4001 ? 71.817  119.539 69.967  1.00 16.22  ? 4001 LEU A CD1   1 
ATOM   18329 C  CD2   . LEU A 1 4001 ? 73.425  118.663 71.682  1.00 17.30  ? 4001 LEU A CD2   1 
ATOM   18330 N  N     . LEU A 1 4002 ? 68.990  116.750 72.542  1.00 10.27  ? 4002 LEU A N     1 
ATOM   18331 C  CA    . LEU A 1 4002 ? 68.544  115.384 72.290  1.00 8.94   ? 4002 LEU A CA    1 
ATOM   18332 C  C     . LEU A 1 4002 ? 67.251  115.371 71.491  1.00 8.76   ? 4002 LEU A C     1 
ATOM   18333 O  O     . LEU A 1 4002 ? 67.157  114.692 70.461  1.00 12.04  ? 4002 LEU A O     1 
ATOM   18334 C  CB    . LEU A 1 4002 ? 68.355  114.639 73.610  1.00 10.30  ? 4002 LEU A CB    1 
ATOM   18335 C  CG    . LEU A 1 4002 ? 69.596  114.312 74.438  1.00 10.94  ? 4002 LEU A CG    1 
ATOM   18336 C  CD1   . LEU A 1 4002 ? 69.195  113.533 75.676  1.00 10.56  ? 4002 LEU A CD1   1 
ATOM   18337 C  CD2   . LEU A 1 4002 ? 70.608  113.532 73.615  1.00 9.06   ? 4002 LEU A CD2   1 
ATOM   18338 N  N     . ALA A 1 4003 ? 66.258  116.153 71.927  1.00 8.68   ? 4003 ALA A N     1 
ATOM   18339 C  CA    . ALA A 1 4003 ? 65.002  116.223 71.191  1.00 9.68   ? 4003 ALA A CA    1 
ATOM   18340 C  C     . ALA A 1 4003 ? 65.251  116.593 69.738  1.00 12.65  ? 4003 ALA A C     1 
ATOM   18341 O  O     . ALA A 1 4003 ? 64.819  115.877 68.824  1.00 13.71  ? 4003 ALA A O     1 
ATOM   18342 C  CB    . ALA A 1 4003 ? 64.059  117.228 71.851  1.00 9.77   ? 4003 ALA A CB    1 
ATOM   18343 N  N     . MET A 1 4004 ? 66.009  117.668 69.506  1.00 11.95  ? 4004 MET A N     1 
ATOM   18344 C  CA    . MET A 1 4004 ? 66.326  118.049 68.137  1.00 13.19  ? 4004 MET A CA    1 
ATOM   18345 C  C     . MET A 1 4004 ? 67.059  116.930 67.416  1.00 11.01  ? 4004 MET A C     1 
ATOM   18346 O  O     . MET A 1 4004 ? 66.745  116.634 66.256  1.00 10.15  ? 4004 MET A O     1 
ATOM   18347 C  CB    . MET A 1 4004 ? 67.154  119.332 68.120  1.00 14.40  ? 4004 MET A CB    1 
ATOM   18348 C  CG    . MET A 1 4004 ? 67.358  119.898 66.731  1.00 12.62  ? 4004 MET A CG    1 
ATOM   18349 S  SD    . MET A 1 4004 ? 65.871  120.674 66.079  1.00 29.02  ? 4004 MET A SD    1 
ATOM   18350 C  CE    . MET A 1 4004 ? 65.717  119.824 64.512  1.00 18.96  ? 4004 MET A CE    1 
ATOM   18351 N  N     . ALA A 1 4005 ? 67.998  116.269 68.101  1.00 9.32   ? 4005 ALA A N     1 
ATOM   18352 C  CA    . ALA A 1 4005 ? 68.687  115.140 67.491  1.00 8.88   ? 4005 ALA A CA    1 
ATOM   18353 C  C     . ALA A 1 4005 ? 67.690  114.090 67.030  1.00 9.73   ? 4005 ALA A C     1 
ATOM   18354 O  O     . ALA A 1 4005 ? 67.778  113.598 65.897  1.00 9.46   ? 4005 ALA A O     1 
ATOM   18355 C  CB    . ALA A 1 4005 ? 69.691  114.539 68.474  1.00 8.30   ? 4005 ALA A CB    1 
ATOM   18356 N  N     . HIS A 1 4006 ? 66.697  113.782 67.871  1.00 10.12  ? 4006 HIS A N     1 
ATOM   18357 C  CA    . HIS A 1 4006 ? 65.672  112.829 67.465  1.00 9.40   ? 4006 HIS A CA    1 
ATOM   18358 C  C     . HIS A 1 4006 ? 64.975  113.304 66.201  1.00 9.37   ? 4006 HIS A C     1 
ATOM   18359 O  O     . HIS A 1 4006 ? 64.819  112.536 65.243  1.00 12.84  ? 4006 HIS A O     1 
ATOM   18360 C  CB    . HIS A 1 4006 ? 64.667  112.621 68.597  1.00 7.59   ? 4006 HIS A CB    1 
ATOM   18361 C  CG    . HIS A 1 4006 ? 65.101  111.607 69.609  1.00 11.53  ? 4006 HIS A CG    1 
ATOM   18362 N  ND1   . HIS A 1 4006 ? 65.923  111.920 70.670  1.00 14.88  ? 4006 HIS A ND1   1 
ATOM   18363 C  CD2   . HIS A 1 4006 ? 64.831  110.285 69.719  1.00 11.87  ? 4006 HIS A CD2   1 
ATOM   18364 C  CE1   . HIS A 1 4006 ? 66.140  110.834 71.391  1.00 15.14  ? 4006 HIS A CE1   1 
ATOM   18365 N  NE2   . HIS A 1 4006 ? 65.488  109.829 70.836  1.00 14.07  ? 4006 HIS A NE2   1 
ATOM   18366 N  N     . MET A 1 4007 ? 64.611  114.590 66.156  1.00 10.81  ? 4007 MET A N     1 
ATOM   18367 C  CA    . MET A 1 4007 ? 64.001  115.137 64.952  1.00 14.31  ? 4007 MET A CA    1 
ATOM   18368 C  C     . MET A 1 4007 ? 64.910  114.932 63.751  1.00 13.28  ? 4007 MET A C     1 
ATOM   18369 O  O     . MET A 1 4007 ? 64.451  114.516 62.680  1.00 15.70  ? 4007 MET A O     1 
ATOM   18370 C  CB    . MET A 1 4007 ? 63.689  116.620 65.146  1.00 16.68  ? 4007 MET A CB    1 
ATOM   18371 C  CG    . MET A 1 4007 ? 62.433  116.888 65.953  1.00 18.13  ? 4007 MET A CG    1 
ATOM   18372 S  SD    . MET A 1 4007 ? 62.246  118.631 66.367  1.00 39.38  ? 4007 MET A SD    1 
ATOM   18373 C  CE    . MET A 1 4007 ? 61.655  119.286 64.809  1.00 27.04  ? 4007 MET A CE    1 
ATOM   18374 N  N     . PHE A 1 4008 ? 66.213  115.170 63.929  1.00 12.49  ? 4008 PHE A N     1 
ATOM   18375 C  CA    . PHE A 1 4008 ? 67.156  114.933 62.843  1.00 12.25  ? 4008 PHE A CA    1 
ATOM   18376 C  C     . PHE A 1 4008 ? 67.058  113.497 62.356  1.00 11.44  ? 4008 PHE A C     1 
ATOM   18377 O  O     . PHE A 1 4008 ? 66.929  113.249 61.150  1.00 14.68  ? 4008 PHE A O     1 
ATOM   18378 C  CB    . PHE A 1 4008 ? 68.577  115.260 63.306  1.00 13.37  ? 4008 PHE A CB    1 
ATOM   18379 C  CG    . PHE A 1 4008 ? 69.645  114.875 62.322  1.00 12.86  ? 4008 PHE A CG    1 
ATOM   18380 C  CD1   . PHE A 1 4008 ? 69.982  115.722 61.280  1.00 16.07  ? 4008 PHE A CD1   1 
ATOM   18381 C  CD2   . PHE A 1 4008 ? 70.324  113.676 62.448  1.00 14.70  ? 4008 PHE A CD2   1 
ATOM   18382 C  CE1   . PHE A 1 4008 ? 70.967  115.372 60.377  1.00 17.16  ? 4008 PHE A CE1   1 
ATOM   18383 C  CE2   . PHE A 1 4008 ? 71.311  113.322 61.549  1.00 16.08  ? 4008 PHE A CE2   1 
ATOM   18384 C  CZ    . PHE A 1 4008 ? 71.634  114.172 60.513  1.00 15.96  ? 4008 PHE A CZ    1 
ATOM   18385 N  N     . VAL A 1 4009 ? 67.052  112.539 63.287  1.00 10.93  ? 4009 VAL A N     1 
ATOM   18386 C  CA    . VAL A 1 4009 ? 66.888  111.143 62.899  1.00 11.49  ? 4009 VAL A CA    1 
ATOM   18387 C  C     . VAL A 1 4009 ? 65.557  110.955 62.189  1.00 12.41  ? 4009 VAL A C     1 
ATOM   18388 O  O     . VAL A 1 4009 ? 65.484  110.314 61.132  1.00 13.10  ? 4009 VAL A O     1 
ATOM   18389 C  CB    . VAL A 1 4009 ? 67.018  110.227 64.131  1.00 10.88  ? 4009 VAL A CB    1 
ATOM   18390 C  CG1   . VAL A 1 4009 ? 66.634  108.800 63.781  1.00 7.49   ? 4009 VAL A CG1   1 
ATOM   18391 C  CG2   . VAL A 1 4009 ? 68.435  110.282 64.680  1.00 7.40   ? 4009 VAL A CG2   1 
ATOM   18392 N  N     . SER A 1 4010 ? 64.493  111.558 62.729  1.00 13.62  ? 4010 SER A N     1 
ATOM   18393 C  CA    . SER A 1 4010 ? 63.179  111.434 62.108  1.00 14.83  ? 4010 SER A CA    1 
ATOM   18394 C  C     . SER A 1 4010 ? 63.184  112.007 60.699  1.00 17.87  ? 4010 SER A C     1 
ATOM   18395 O  O     . SER A 1 4010 ? 62.390  111.589 59.847  1.00 25.24  ? 4010 SER A O     1 
ATOM   18396 C  CB    . SER A 1 4010 ? 62.123  112.127 62.968  1.00 16.85  ? 4010 SER A CB    1 
ATOM   18397 O  OG    . SER A 1 4010 ? 60.818  111.839 62.499  1.00 29.15  ? 4010 SER A OG    1 
ATOM   18398 N  N     . THR A 1 4011 ? 64.073  112.965 60.431  1.00 17.14  ? 4011 THR A N     1 
ATOM   18399 C  CA    . THR A 1 4011 ? 64.145  113.527 59.088  1.00 20.21  ? 4011 THR A CA    1 
ATOM   18400 C  C     . THR A 1 4011 ? 64.885  112.586 58.144  1.00 23.93  ? 4011 THR A C     1 
ATOM   18401 O  O     . THR A 1 4011 ? 64.549  112.491 56.958  1.00 22.93  ? 4011 THR A O     1 
ATOM   18402 C  CB    . THR A 1 4011 ? 64.816  114.900 59.132  1.00 21.43  ? 4011 THR A CB    1 
ATOM   18403 O  OG1   . THR A 1 4011 ? 64.075  115.761 60.005  1.00 25.80  ? 4011 THR A OG1   1 
ATOM   18404 C  CG2   . THR A 1 4011 ? 64.835  115.525 57.752  1.00 25.14  ? 4011 THR A CG2   1 
ATOM   18405 N  N     . ASN A 1 4012 ? 65.885  111.865 58.659  1.00 20.84  ? 4012 ASN A N     1 
ATOM   18406 C  CA    . ASN A 1 4012 ? 66.730  111.050 57.793  1.00 17.06  ? 4012 ASN A CA    1 
ATOM   18407 C  C     . ASN A 1 4012 ? 66.197  109.631 57.639  1.00 14.63  ? 4012 ASN A C     1 
ATOM   18408 O  O     . ASN A 1 4012 ? 66.213  109.078 56.534  1.00 15.83  ? 4012 ASN A O     1 
ATOM   18409 C  CB    . ASN A 1 4012 ? 68.158  111.024 58.335  1.00 18.27  ? 4012 ASN A CB    1 
ATOM   18410 C  CG    . ASN A 1 4012 ? 69.025  112.115 57.744  1.00 20.88  ? 4012 ASN A CG    1 
ATOM   18411 O  OD1   . ASN A 1 4012 ? 69.343  112.095 56.556  1.00 29.44  ? 4012 ASN A OD1   1 
ATOM   18412 N  ND2   . ASN A 1 4012 ? 69.401  113.083 58.569  1.00 18.34  ? 4012 ASN A ND2   1 
ATOM   18413 N  N     . LEU A 1 4013 ? 65.721  109.028 58.727  1.00 17.03  ? 4013 LEU A N     1 
ATOM   18414 C  CA    . LEU A 1 4013 ? 65.376  107.615 58.738  1.00 14.26  ? 4013 LEU A CA    1 
ATOM   18415 C  C     . LEU A 1 4013 ? 63.889  107.333 58.889  1.00 16.04  ? 4013 LEU A C     1 
ATOM   18416 O  O     . LEU A 1 4013 ? 63.500  106.160 58.871  1.00 21.43  ? 4013 LEU A O     1 
ATOM   18417 C  CB    . LEU A 1 4013 ? 66.141  106.899 59.862  1.00 9.35   ? 4013 LEU A CB    1 
ATOM   18418 C  CG    . LEU A 1 4013 ? 67.664  106.924 59.724  1.00 8.27   ? 4013 LEU A CG    1 
ATOM   18419 C  CD1   . LEU A 1 4013 ? 68.336  106.635 61.051  1.00 8.10   ? 4013 LEU A CD1   1 
ATOM   18420 C  CD2   . LEU A 1 4013 ? 68.115  105.924 58.674  1.00 9.06   ? 4013 LEU A CD2   1 
ATOM   18421 N  N     . GLY A 1 4014 ? 63.054  108.350 59.033  1.00 16.98  ? 4014 GLY A N     1 
ATOM   18422 C  CA    . GLY A 1 4014 ? 61.628  108.153 59.163  1.00 19.06  ? 4014 GLY A CA    1 
ATOM   18423 C  C     . GLY A 1 4014 ? 61.147  108.375 60.590  1.00 20.49  ? 4014 GLY A C     1 
ATOM   18424 O  O     . GLY A 1 4014 ? 61.910  108.322 61.558  1.00 17.66  ? 4014 GLY A O     1 
ATOM   18425 N  N     . GLU A 1 4015 ? 59.842  108.633 60.706  1.00 26.73  ? 4015 GLU A N     1 
ATOM   18426 C  CA    . GLU A 1 4015 ? 59.250  108.920 62.009  1.00 24.75  ? 4015 GLU A CA    1 
ATOM   18427 C  C     . GLU A 1 4015 ? 59.308  107.709 62.933  1.00 23.10  ? 4015 GLU A C     1 
ATOM   18428 O  O     . GLU A 1 4015 ? 59.567  107.847 64.134  1.00 21.44  ? 4015 GLU A O     1 
ATOM   18429 C  CB    . GLU A 1 4015 ? 57.805  109.388 61.836  1.00 30.57  ? 4015 GLU A CB    1 
ATOM   18430 C  CG    . GLU A 1 4015 ? 57.659  110.740 61.157  1.00 42.69  ? 4015 GLU A CG    1 
ATOM   18431 C  CD    . GLU A 1 4015 ? 57.581  110.631 59.645  1.00 53.47  ? 4015 GLU A CD    1 
ATOM   18432 O  OE1   . GLU A 1 4015 ? 56.526  110.983 59.076  1.00 61.03  ? 4015 GLU A OE1   1 
ATOM   18433 O  OE2   . GLU A 1 4015 ? 58.575  110.198 59.026  1.00 44.50  ? 4015 GLU A OE2   1 
ATOM   18434 N  N     . SER A 1 4016 ? 59.066  106.514 62.394  1.00 20.04  ? 4016 SER A N     1 
ATOM   18435 C  CA    . SER A 1 4016 ? 58.940  105.303 63.192  1.00 19.92  ? 4016 SER A CA    1 
ATOM   18436 C  C     . SER A 1 4016 ? 60.237  104.503 63.273  1.00 19.03  ? 4016 SER A C     1 
ATOM   18437 O  O     . SER A 1 4016 ? 60.202  103.324 63.642  1.00 22.10  ? 4016 SER A O     1 
ATOM   18438 C  CB    . SER A 1 4016 ? 57.818  104.423 62.636  1.00 23.40  ? 4016 SER A CB    1 
ATOM   18439 O  OG    . SER A 1 4016 ? 57.697  103.222 63.377  1.00 31.86  ? 4016 SER A OG    1 
ATOM   18440 N  N     . PHE A 1 4017 ? 61.374  105.111 62.927  1.00 16.51  ? 4017 PHE A N     1 
ATOM   18441 C  CA    . PHE A 1 4017 ? 62.638  104.382 62.942  1.00 13.60  ? 4017 PHE A CA    1 
ATOM   18442 C  C     . PHE A 1 4017 ? 63.013  103.940 64.352  1.00 12.63  ? 4017 PHE A C     1 
ATOM   18443 O  O     . PHE A 1 4017 ? 63.479  102.813 64.554  1.00 9.03   ? 4017 PHE A O     1 
ATOM   18444 C  CB    . PHE A 1 4017 ? 63.743  105.247 62.337  1.00 10.84  ? 4017 PHE A CB    1 
ATOM   18445 C  CG    . PHE A 1 4017 ? 65.072  104.556 62.238  1.00 10.20  ? 4017 PHE A CG    1 
ATOM   18446 C  CD1   . PHE A 1 4017 ? 65.358  103.735 61.161  1.00 8.48   ? 4017 PHE A CD1   1 
ATOM   18447 C  CD2   . PHE A 1 4017 ? 66.035  104.730 63.217  1.00 8.21   ? 4017 PHE A CD2   1 
ATOM   18448 C  CE1   . PHE A 1 4017 ? 66.578  103.100 61.061  1.00 7.12   ? 4017 PHE A CE1   1 
ATOM   18449 C  CE2   . PHE A 1 4017 ? 67.256  104.094 63.125  1.00 6.16   ? 4017 PHE A CE2   1 
ATOM   18450 C  CZ    . PHE A 1 4017 ? 67.529  103.281 62.042  1.00 5.89   ? 4017 PHE A CZ    1 
ATOM   18451 N  N     . MET A 1 4018 ? 62.820  104.813 65.339  1.00 15.66  ? 4018 MET A N     1 
ATOM   18452 C  CA    . MET A 1 4018 ? 63.202  104.548 66.719  1.00 11.77  ? 4018 MET A CA    1 
ATOM   18453 C  C     . MET A 1 4018 ? 62.034  104.075 67.578  1.00 18.16  ? 4018 MET A C     1 
ATOM   18454 O  O     . MET A 1 4018 ? 62.183  103.960 68.798  1.00 20.57  ? 4018 MET A O     1 
ATOM   18455 C  CB    . MET A 1 4018 ? 63.826  105.801 67.335  1.00 10.06  ? 4018 MET A CB    1 
ATOM   18456 C  CG    . MET A 1 4018 ? 65.110  106.257 66.661  1.00 11.72  ? 4018 MET A CG    1 
ATOM   18457 S  SD    . MET A 1 4018 ? 65.981  107.524 67.603  1.00 16.03  ? 4018 MET A SD    1 
ATOM   18458 C  CE    . MET A 1 4018 ? 66.793  106.535 68.854  1.00 7.64   ? 4018 MET A CE    1 
ATOM   18459 N  N     . SER A 1 4019 ? 60.880  103.793 66.970  1.00 19.10  ? 4019 SER A N     1 
ATOM   18460 C  CA    . SER A 1 4019 ? 59.671  103.520 67.741  1.00 19.83  ? 4019 SER A CA    1 
ATOM   18461 C  C     . SER A 1 4019 ? 59.680  102.148 68.405  1.00 25.71  ? 4019 SER A C     1 
ATOM   18462 O  O     . SER A 1 4019 ? 58.956  101.951 69.387  1.00 29.78  ? 4019 SER A O     1 
ATOM   18463 C  CB    . SER A 1 4019 ? 58.441  103.652 66.842  1.00 23.51  ? 4019 SER A CB    1 
ATOM   18464 O  OG    . SER A 1 4019 ? 58.188  105.010 66.525  1.00 27.78  ? 4019 SER A OG    1 
ATOM   18465 N  N     . ILE A 1 4020 ? 60.469  101.199 67.897  1.00 24.35  ? 4020 ILE A N     1 
ATOM   18466 C  CA    . ILE A 1 4020 ? 60.470  99.853  68.465  1.00 20.88  ? 4020 ILE A CA    1 
ATOM   18467 C  C     . ILE A 1 4020 ? 61.015  99.867  69.889  1.00 21.54  ? 4020 ILE A C     1 
ATOM   18468 O  O     . ILE A 1 4020 ? 60.553  99.111  70.752  1.00 23.16  ? 4020 ILE A O     1 
ATOM   18469 C  CB    . ILE A 1 4020 ? 61.262  98.891  67.561  1.00 23.17  ? 4020 ILE A CB    1 
ATOM   18470 C  CG1   . ILE A 1 4020 ? 60.648  98.850  66.161  1.00 24.69  ? 4020 ILE A CG1   1 
ATOM   18471 C  CG2   . ILE A 1 4020 ? 61.296  97.492  68.157  1.00 22.81  ? 4020 ILE A CG2   1 
ATOM   18472 C  CD1   . ILE A 1 4020 ? 59.217  98.359  66.136  1.00 21.71  ? 4020 ILE A CD1   1 
ATOM   18473 N  N     . MET A 1 4021 ? 61.999  100.727 70.160  1.00 21.88  ? 4021 MET A N     1 
ATOM   18474 C  CA    . MET A 1 4021 ? 62.611  100.761 71.485  1.00 21.48  ? 4021 MET A CA    1 
ATOM   18475 C  C     . MET A 1 4021 ? 61.618  101.187 72.559  1.00 24.63  ? 4021 MET A C     1 
ATOM   18476 O  O     . MET A 1 4021 ? 61.788  100.839 73.733  1.00 29.67  ? 4021 MET A O     1 
ATOM   18477 C  CB    . MET A 1 4021 ? 63.821  101.694 71.477  1.00 21.70  ? 4021 MET A CB    1 
ATOM   18478 C  CG    . MET A 1 4021 ? 64.997  101.165 70.676  1.00 21.86  ? 4021 MET A CG    1 
ATOM   18479 S  SD    . MET A 1 4021 ? 65.383  99.447  71.063  1.00 22.64  ? 4021 MET A SD    1 
ATOM   18480 C  CE    . MET A 1 4021 ? 65.329  98.714  69.430  1.00 12.14  ? 4021 MET A CE    1 
ATOM   18481 N  N     . GLU A 1 4022 ? 60.580  101.937 72.183  1.00 27.50  ? 4022 GLU A N     1 
ATOM   18482 C  CA    . GLU A 1 4022 ? 59.561  102.324 73.153  1.00 24.59  ? 4022 GLU A CA    1 
ATOM   18483 C  C     . GLU A 1 4022 ? 58.641  101.159 73.496  1.00 21.81  ? 4022 GLU A C     1 
ATOM   18484 O  O     . GLU A 1 4022 ? 57.988  101.176 74.546  1.00 26.08  ? 4022 GLU A O     1 
ATOM   18485 C  CB    . GLU A 1 4022 ? 58.746  103.501 72.618  1.00 25.52  ? 4022 GLU A CB    1 
ATOM   18486 C  CG    . GLU A 1 4022 ? 59.560  104.758 72.355  1.00 26.76  ? 4022 GLU A CG    1 
ATOM   18487 C  CD    . GLU A 1 4022 ? 60.495  105.101 73.498  1.00 35.14  ? 4022 GLU A CD    1 
ATOM   18488 O  OE1   . GLU A 1 4022 ? 60.011  105.619 74.527  1.00 33.64  ? 4022 GLU A OE1   1 
ATOM   18489 O  OE2   . GLU A 1 4022 ? 61.712  104.855 73.369  1.00 31.52  ? 4022 GLU A OE2   1 
ATOM   18490 N  N     . GLN A 1 4023 ? 58.572  100.149 72.630  1.00 22.46  ? 4023 GLN A N     1 
ATOM   18491 C  CA    . GLN A 1 4023 ? 57.729  98.988  72.854  1.00 23.38  ? 4023 GLN A CA    1 
ATOM   18492 C  C     . GLN A 1 4023 ? 58.421  98.009  73.804  1.00 23.77  ? 4023 GLN A C     1 
ATOM   18493 O  O     . GLN A 1 4023 ? 59.651  97.986  73.892  1.00 25.92  ? 4023 GLN A O     1 
ATOM   18494 C  CB    . GLN A 1 4023 ? 57.429  98.291  71.529  1.00 28.02  ? 4023 GLN A CB    1 
ATOM   18495 C  CG    . GLN A 1 4023 ? 56.307  98.920  70.704  1.00 32.09  ? 4023 GLN A CG    1 
ATOM   18496 C  CD    . GLN A 1 4023 ? 55.018  99.123  71.478  1.00 37.68  ? 4023 GLN A CD    1 
ATOM   18497 O  OE1   . GLN A 1 4023 ? 54.635  98.296  72.303  1.00 35.99  ? 4023 GLN A OE1   1 
ATOM   18498 N  NE2   . GLN A 1 4023 ? 54.340  100.234 71.212  1.00 34.34  ? 4023 GLN A NE2   1 
ATOM   18499 N  N     . PRO A 1 4024 ? 57.655  97.198  74.534  1.00 22.65  ? 4024 PRO A N     1 
ATOM   18500 C  CA    . PRO A 1 4024 ? 58.275  96.151  75.352  1.00 22.23  ? 4024 PRO A CA    1 
ATOM   18501 C  C     . PRO A 1 4024 ? 58.977  95.116  74.486  1.00 24.06  ? 4024 PRO A C     1 
ATOM   18502 O  O     . PRO A 1 4024 ? 58.596  94.870  73.339  1.00 28.96  ? 4024 PRO A O     1 
ATOM   18503 C  CB    . PRO A 1 4024 ? 57.090  95.538  76.110  1.00 18.71  ? 4024 PRO A CB    1 
ATOM   18504 C  CG    . PRO A 1 4024 ? 55.885  95.926  75.318  1.00 18.96  ? 4024 PRO A CG    1 
ATOM   18505 C  CD    . PRO A 1 4024 ? 56.202  97.272  74.754  1.00 23.53  ? 4024 PRO A CD    1 
ATOM   18506 N  N     . LEU A 1 4025 ? 60.022  94.515  75.049  1.00 21.70  ? 4025 LEU A N     1 
ATOM   18507 C  CA    . LEU A 1 4025 ? 60.803  93.523  74.324  1.00 22.11  ? 4025 LEU A CA    1 
ATOM   18508 C  C     . LEU A 1 4025 ? 59.946  92.310  73.987  1.00 28.44  ? 4025 LEU A C     1 
ATOM   18509 O  O     . LEU A 1 4025 ? 59.528  91.565  74.879  1.00 30.70  ? 4025 LEU A O     1 
ATOM   18510 C  CB    . LEU A 1 4025 ? 62.017  93.104  75.152  1.00 20.39  ? 4025 LEU A CB    1 
ATOM   18511 C  CG    . LEU A 1 4025 ? 62.997  92.149  74.469  1.00 20.07  ? 4025 LEU A CG    1 
ATOM   18512 C  CD1   . LEU A 1 4025 ? 63.581  92.784  73.219  1.00 21.34  ? 4025 LEU A CD1   1 
ATOM   18513 C  CD2   . LEU A 1 4025 ? 64.100  91.731  75.427  1.00 17.35  ? 4025 LEU A CD2   1 
ATOM   18514 N  N     . ASP A 1 4026 ? 59.684  92.114  72.694  1.00 33.76  ? 4026 ASP A N     1 
ATOM   18515 C  CA    . ASP A 1 4026 ? 58.932  90.953  72.221  1.00 34.90  ? 4026 ASP A CA    1 
ATOM   18516 C  C     . ASP A 1 4026 ? 59.908  89.783  72.123  1.00 33.46  ? 4026 ASP A C     1 
ATOM   18517 O  O     . ASP A 1 4026 ? 60.441  89.450  71.062  1.00 36.18  ? 4026 ASP A O     1 
ATOM   18518 C  CB    . ASP A 1 4026 ? 58.250  91.256  70.893  1.00 40.45  ? 4026 ASP A CB    1 
ATOM   18519 C  CG    . ASP A 1 4026 ? 57.561  90.045  70.301  1.00 48.91  ? 4026 ASP A CG    1 
ATOM   18520 O  OD1   . ASP A 1 4026 ? 56.472  89.678  70.791  1.00 55.53  ? 4026 ASP A OD1   1 
ATOM   18521 O  OD2   . ASP A 1 4026 ? 58.104  89.465  69.340  1.00 49.24  ? 4026 ASP A OD2   1 
ATOM   18522 N  N     . LEU A 1 4027 ? 60.143  89.154  73.276  1.00 29.16  ? 4027 LEU A N     1 
ATOM   18523 C  CA    . LEU A 1 4027 ? 61.200  88.156  73.389  1.00 25.38  ? 4027 LEU A CA    1 
ATOM   18524 C  C     . LEU A 1 4027 ? 60.843  86.858  72.673  1.00 29.97  ? 4027 LEU A C     1 
ATOM   18525 O  O     . LEU A 1 4027 ? 61.741  86.124  72.243  1.00 34.03  ? 4027 LEU A O     1 
ATOM   18526 C  CB    . LEU A 1 4027 ? 61.491  87.890  74.866  1.00 22.52  ? 4027 LEU A CB    1 
ATOM   18527 C  CG    . LEU A 1 4027 ? 62.614  86.922  75.233  1.00 30.03  ? 4027 LEU A CG    1 
ATOM   18528 C  CD1   . LEU A 1 4027 ? 63.949  87.450  74.736  1.00 26.12  ? 4027 LEU A CD1   1 
ATOM   18529 C  CD2   . LEU A 1 4027 ? 62.642  86.697  76.735  1.00 29.00  ? 4027 LEU A CD2   1 
ATOM   18530 N  N     . THR A 1 4028 ? 59.548  86.562  72.533  1.00 33.66  ? 4028 THR A N     1 
ATOM   18531 C  CA    . THR A 1 4028 ? 59.129  85.283  71.968  1.00 33.63  ? 4028 THR A CA    1 
ATOM   18532 C  C     . THR A 1 4028 ? 59.628  85.119  70.537  1.00 33.10  ? 4028 THR A C     1 
ATOM   18533 O  O     . THR A 1 4028 ? 60.274  84.118  70.202  1.00 32.82  ? 4028 THR A O     1 
ATOM   18534 C  CB    . THR A 1 4028 ? 57.604  85.164  72.018  1.00 32.37  ? 4028 THR A CB    1 
ATOM   18535 O  OG1   . THR A 1 4028 ? 57.182  84.929  73.367  1.00 42.28  ? 4028 THR A OG1   1 
ATOM   18536 C  CG2   . THR A 1 4028 ? 57.128  84.016  71.141  1.00 31.25  ? 4028 THR A CG2   1 
ATOM   18537 N  N     . HIS A 1 4029 ? 59.344  86.103  69.680  1.00 32.13  ? 4029 HIS A N     1 
ATOM   18538 C  CA    . HIS A 1 4029 ? 59.743  86.008  68.279  1.00 33.25  ? 4029 HIS A CA    1 
ATOM   18539 C  C     . HIS A 1 4029 ? 61.259  86.014  68.133  1.00 32.71  ? 4029 HIS A C     1 
ATOM   18540 O  O     . HIS A 1 4029 ? 61.812  85.287  67.299  1.00 33.77  ? 4029 HIS A O     1 
ATOM   18541 C  CB    . HIS A 1 4029 ? 59.121  87.153  67.480  1.00 39.33  ? 4029 HIS A CB    1 
ATOM   18542 C  CG    . HIS A 1 4029 ? 59.524  87.175  66.039  1.00 45.21  ? 4029 HIS A CG    1 
ATOM   18543 N  ND1   . HIS A 1 4029 ? 60.065  88.290  65.435  1.00 46.13  ? 4029 HIS A ND1   1 
ATOM   18544 C  CD2   . HIS A 1 4029 ? 59.460  86.222  65.080  1.00 45.60  ? 4029 HIS A CD2   1 
ATOM   18545 C  CE1   . HIS A 1 4029 ? 60.320  88.021  64.167  1.00 46.86  ? 4029 HIS A CE1   1 
ATOM   18546 N  NE2   . HIS A 1 4029 ? 59.962  86.773  63.926  1.00 51.00  ? 4029 HIS A NE2   1 
ATOM   18547 N  N     . ILE A 1 4030 ? 61.946  86.831  68.933  1.00 33.63  ? 4030 ILE A N     1 
ATOM   18548 C  CA    . ILE A 1 4030 ? 63.401  86.918  68.838  1.00 29.99  ? 4030 ILE A CA    1 
ATOM   18549 C  C     . ILE A 1 4030 ? 64.039  85.584  69.205  1.00 25.93  ? 4030 ILE A C     1 
ATOM   18550 O  O     . ILE A 1 4030 ? 64.956  85.107  68.527  1.00 27.06  ? 4030 ILE A O     1 
ATOM   18551 C  CB    . ILE A 1 4030 ? 63.929  88.059  69.725  1.00 24.61  ? 4030 ILE A CB    1 
ATOM   18552 C  CG1   . ILE A 1 4030 ? 63.247  89.378  69.360  1.00 21.22  ? 4030 ILE A CG1   1 
ATOM   18553 C  CG2   . ILE A 1 4030 ? 65.433  88.178  69.586  1.00 21.78  ? 4030 ILE A CG2   1 
ATOM   18554 C  CD1   . ILE A 1 4030 ? 63.632  90.532  70.256  1.00 22.04  ? 4030 ILE A CD1   1 
ATOM   18555 N  N     . VAL A 1 4031 ? 63.563  84.962  70.286  1.00 26.11  ? 4031 VAL A N     1 
ATOM   18556 C  CA    . VAL A 1 4031 ? 64.110  83.670  70.693  1.00 26.69  ? 4031 VAL A CA    1 
ATOM   18557 C  C     . VAL A 1 4031 ? 63.767  82.596  69.668  1.00 28.61  ? 4031 VAL A C     1 
ATOM   18558 O  O     . VAL A 1 4031 ? 64.604  81.750  69.331  1.00 27.53  ? 4031 VAL A O     1 
ATOM   18559 C  CB    . VAL A 1 4031 ? 63.609  83.295  72.101  1.00 25.28  ? 4031 VAL A CB    1 
ATOM   18560 C  CG1   . VAL A 1 4031 ? 63.916  81.838  72.410  1.00 21.15  ? 4031 VAL A CG1   1 
ATOM   18561 C  CG2   . VAL A 1 4031 ? 64.245  84.199  73.141  1.00 18.62  ? 4031 VAL A CG2   1 
ATOM   18562 N  N     . GLY A 1 4032 ? 62.539  82.619  69.143  1.00 29.03  ? 4032 GLY A N     1 
ATOM   18563 C  CA    . GLY A 1 4032 ? 62.113  81.566  68.240  1.00 28.45  ? 4032 GLY A CA    1 
ATOM   18564 C  C     . GLY A 1 4032 ? 62.755  81.623  66.868  1.00 33.38  ? 4032 GLY A C     1 
ATOM   18565 O  O     . GLY A 1 4032 ? 63.009  80.581  66.258  1.00 39.39  ? 4032 GLY A O     1 
ATOM   18566 N  N     . THR A 1 4033 ? 63.026  82.823  66.362  1.00 31.10  ? 4033 THR A N     1 
ATOM   18567 C  CA    . THR A 1 4033 ? 63.458  82.976  64.977  1.00 30.85  ? 4033 THR A CA    1 
ATOM   18568 C  C     . THR A 1 4033 ? 64.828  83.614  64.821  1.00 32.49  ? 4033 THR A C     1 
ATOM   18569 O  O     . THR A 1 4033 ? 65.597  83.198  63.951  1.00 41.15  ? 4033 THR A O     1 
ATOM   18570 C  CB    . THR A 1 4033 ? 62.431  83.808  64.193  1.00 40.34  ? 4033 THR A CB    1 
ATOM   18571 O  OG1   . THR A 1 4033 ? 62.344  85.121  64.762  1.00 40.22  ? 4033 THR A OG1   1 
ATOM   18572 C  CG2   . THR A 1 4033 ? 61.061  83.150  64.238  1.00 40.58  ? 4033 THR A CG2   1 
ATOM   18573 N  N     . GLU A 1 4034 ? 65.161  84.616  65.634  1.00 29.58  ? 4034 GLU A N     1 
ATOM   18574 C  CA    . GLU A 1 4034 ? 66.379  85.385  65.414  1.00 27.71  ? 4034 GLU A CA    1 
ATOM   18575 C  C     . GLU A 1 4034 ? 67.599  84.818  66.126  1.00 30.25  ? 4034 GLU A C     1 
ATOM   18576 O  O     . GLU A 1 4034 ? 68.726  85.172  65.763  1.00 34.64  ? 4034 GLU A O     1 
ATOM   18577 C  CB    . GLU A 1 4034 ? 66.177  86.836  65.858  1.00 23.70  ? 4034 GLU A CB    1 
ATOM   18578 C  CG    . GLU A 1 4034 ? 65.168  87.612  65.032  1.00 28.87  ? 4034 GLU A CG    1 
ATOM   18579 C  CD    . GLU A 1 4034 ? 65.003  89.040  65.513  1.00 29.67  ? 4034 GLU A CD    1 
ATOM   18580 O  OE1   . GLU A 1 4034 ? 65.596  89.391  66.553  1.00 27.21  ? 4034 GLU A OE1   1 
ATOM   18581 O  OE2   . GLU A 1 4034 ? 64.278  89.813  64.851  1.00 32.36  ? 4034 GLU A OE2   1 
ATOM   18582 N  N     . VAL A 1 4035 ? 67.413  83.956  67.121  1.00 31.31  ? 4035 VAL A N     1 
ATOM   18583 C  CA    . VAL A 1 4035 ? 68.514  83.438  67.924  1.00 23.79  ? 4035 VAL A CA    1 
ATOM   18584 C  C     . VAL A 1 4035 ? 68.772  81.989  67.541  1.00 23.98  ? 4035 VAL A C     1 
ATOM   18585 O  O     . VAL A 1 4035 ? 67.864  81.151  67.597  1.00 28.91  ? 4035 VAL A O     1 
ATOM   18586 C  CB    . VAL A 1 4035 ? 68.214  83.565  69.427  1.00 17.91  ? 4035 VAL A CB    1 
ATOM   18587 C  CG1   . VAL A 1 4035 ? 69.218  82.760  70.234  1.00 19.16  ? 4035 VAL A CG1   1 
ATOM   18588 C  CG2   . VAL A 1 4035 ? 68.233  85.025  69.849  1.00 18.26  ? 4035 VAL A CG2   1 
ATOM   18589 N  N     . LYS A 1 4036 ? 70.009  81.694  67.152  1.00 19.05  ? 4036 LYS A N     1 
ATOM   18590 C  CA    . LYS A 1 4036 ? 70.413  80.330  66.862  1.00 23.20  ? 4036 LYS A CA    1 
ATOM   18591 C  C     . LYS A 1 4036 ? 70.628  79.555  68.161  1.00 21.03  ? 4036 LYS A C     1 
ATOM   18592 O  O     . LYS A 1 4036 ? 70.942  80.145  69.197  1.00 20.93  ? 4036 LYS A O     1 
ATOM   18593 C  CB    . LYS A 1 4036 ? 71.696  80.319  66.036  1.00 21.92  ? 4036 LYS A CB    1 
ATOM   18594 C  CG    . LYS A 1 4036 ? 71.616  81.020  64.677  1.00 22.86  ? 4036 LYS A CG    1 
ATOM   18595 C  CD    . LYS A 1 4036 ? 70.768  80.263  63.656  1.00 31.20  ? 4036 LYS A CD    1 
ATOM   18596 C  CE    . LYS A 1 4036 ? 69.320  80.741  63.627  1.00 42.47  ? 4036 LYS A CE    1 
ATOM   18597 N  NZ    . LYS A 1 4036 ? 68.534  80.071  62.555  1.00 56.15  ? 4036 LYS A NZ    1 
ATOM   18598 N  N     . PRO A 1 4037 ? 70.452  78.230  68.134  1.00 21.40  ? 4037 PRO A N     1 
ATOM   18599 C  CA    . PRO A 1 4037 ? 70.726  77.437  69.345  1.00 18.63  ? 4037 PRO A CA    1 
ATOM   18600 C  C     . PRO A 1 4037 ? 72.160  77.552  69.830  1.00 16.19  ? 4037 PRO A C     1 
ATOM   18601 O  O     . PRO A 1 4037 ? 72.400  77.491  71.042  1.00 15.80  ? 4037 PRO A O     1 
ATOM   18602 C  CB    . PRO A 1 4037 ? 70.383  76.002  68.914  1.00 19.01  ? 4037 PRO A CB    1 
ATOM   18603 C  CG    . PRO A 1 4037 ? 70.373  76.025  67.420  1.00 19.69  ? 4037 PRO A CG    1 
ATOM   18604 C  CD    . PRO A 1 4037 ? 69.945  77.401  67.028  1.00 20.36  ? 4037 PRO A CD    1 
ATOM   18605 N  N     . ASN A 1 4038 ? 73.123  77.713  68.922  1.00 18.86  ? 4038 ASN A N     1 
ATOM   18606 C  CA    . ASN A 1 4038 ? 74.509  77.917  69.326  1.00 18.50  ? 4038 ASN A CA    1 
ATOM   18607 C  C     . ASN A 1 4038 ? 74.745  79.269  69.983  1.00 17.19  ? 4038 ASN A C     1 
ATOM   18608 O  O     . ASN A 1 4038 ? 75.724  79.413  70.722  1.00 17.66  ? 4038 ASN A O     1 
ATOM   18609 C  CB    . ASN A 1 4038 ? 75.438  77.771  68.120  1.00 23.71  ? 4038 ASN A CB    1 
ATOM   18610 C  CG    . ASN A 1 4038 ? 76.851  77.406  68.519  1.00 31.57  ? 4038 ASN A CG    1 
ATOM   18611 O  OD1   . ASN A 1 4038 ? 77.150  76.244  68.786  1.00 32.17  ? 4038 ASN A OD1   1 
ATOM   18612 N  ND2   . ASN A 1 4038 ? 77.731  78.400  68.559  1.00 40.44  ? 4038 ASN A ND2   1 
ATOM   18613 N  N     . THR A 1 4039 ? 73.885  80.256  69.737  1.00 13.97  ? 4039 THR A N     1 
ATOM   18614 C  CA    . THR A 1 4039 ? 74.094  81.594  70.266  1.00 12.09  ? 4039 THR A CA    1 
ATOM   18615 C  C     . THR A 1 4039 ? 73.415  81.726  71.618  1.00 11.47  ? 4039 THR A C     1 
ATOM   18616 O  O     . THR A 1 4039 ? 72.180  81.622  71.692  1.00 10.92  ? 4039 THR A O     1 
ATOM   18617 C  CB    . THR A 1 4039 ? 73.551  82.641  69.301  1.00 12.15  ? 4039 THR A CB    1 
ATOM   18618 O  OG1   . THR A 1 4039 ? 74.288  82.587  68.073  1.00 18.23  ? 4039 THR A OG1   1 
ATOM   18619 C  CG2   . THR A 1 4039 ? 73.671  84.032  69.897  1.00 6.92   ? 4039 THR A CG2   1 
ATOM   18620 N  N     . PRO A 1 4040 ? 74.158  81.945  72.700  1.00 8.30   ? 4040 PRO A N     1 
ATOM   18621 C  CA    . PRO A 1 4040 ? 73.513  82.205  73.990  1.00 5.63   ? 4040 PRO A CA    1 
ATOM   18622 C  C     . PRO A 1 4040 ? 72.790  83.541  73.983  1.00 6.20   ? 4040 PRO A C     1 
ATOM   18623 O  O     . PRO A 1 4040 ? 73.205  84.500  73.328  1.00 5.59   ? 4040 PRO A O     1 
ATOM   18624 C  CB    . PRO A 1 4040 ? 74.684  82.210  74.980  1.00 4.88   ? 4040 PRO A CB    1 
ATOM   18625 C  CG    . PRO A 1 4040 ? 75.874  82.556  74.153  1.00 6.05   ? 4040 PRO A CG    1 
ATOM   18626 C  CD    . PRO A 1 4040 ? 75.627  81.952  72.801  1.00 7.36   ? 4040 PRO A CD    1 
ATOM   18627 N  N     . VAL A 1 4041 ? 71.688  83.591  74.719  1.00 6.72   ? 4041 VAL A N     1 
ATOM   18628 C  CA    . VAL A 1 4041 ? 70.914  84.812  74.901  1.00 5.43   ? 4041 VAL A CA    1 
ATOM   18629 C  C     . VAL A 1 4041 ? 71.400  85.462  76.187  1.00 4.99   ? 4041 VAL A C     1 
ATOM   18630 O  O     . VAL A 1 4041 ? 71.029  85.039  77.286  1.00 5.22   ? 4041 VAL A O     1 
ATOM   18631 C  CB    . VAL A 1 4041 ? 69.407  84.527  74.954  1.00 6.10   ? 4041 VAL A CB    1 
ATOM   18632 C  CG1   . VAL A 1 4041 ? 68.630  85.819  75.143  1.00 6.10   ? 4041 VAL A CG1   1 
ATOM   18633 C  CG2   . VAL A 1 4041 ? 68.957  83.806  73.695  1.00 5.91   ? 4041 VAL A CG2   1 
ATOM   18634 N  N     . LEU A 1 4042 ? 72.253  86.475  76.060  1.00 4.88   ? 4042 LEU A N     1 
ATOM   18635 C  CA    . LEU A 1 4042 ? 72.763  87.204  77.213  1.00 5.23   ? 4042 LEU A CA    1 
ATOM   18636 C  C     . LEU A 1 4042 ? 71.727  88.253  77.589  1.00 5.73   ? 4042 LEU A C     1 
ATOM   18637 O  O     . LEU A 1 4042 ? 71.310  89.050  76.745  1.00 7.29   ? 4042 LEU A O     1 
ATOM   18638 C  CB    . LEU A 1 4042 ? 74.109  87.849  76.896  1.00 5.37   ? 4042 LEU A CB    1 
ATOM   18639 C  CG    . LEU A 1 4042 ? 75.139  86.987  76.164  1.00 7.60   ? 4042 LEU A CG    1 
ATOM   18640 C  CD1   . LEU A 1 4042 ? 76.438  87.751  75.994  1.00 9.08   ? 4042 LEU A CD1   1 
ATOM   18641 C  CD2   . LEU A 1 4042 ? 75.379  85.682  76.901  1.00 6.82   ? 4042 LEU A CD2   1 
ATOM   18642 N  N     . MET A 1 4043 ? 71.290  88.238  78.840  1.00 7.06   ? 4043 MET A N     1 
ATOM   18643 C  CA    . MET A 1 4043 ? 70.366  89.240  79.356  1.00 8.09   ? 4043 MET A CA    1 
ATOM   18644 C  C     . MET A 1 4043 ? 71.096  90.009  80.451  1.00 9.25   ? 4043 MET A C     1 
ATOM   18645 O  O     . MET A 1 4043 ? 71.246  89.533  81.579  1.00 8.86   ? 4043 MET A O     1 
ATOM   18646 C  CB    . MET A 1 4043 ? 69.078  88.603  79.853  1.00 9.21   ? 4043 MET A CB    1 
ATOM   18647 C  CG    . MET A 1 4043 ? 68.258  88.003  78.728  1.00 13.79  ? 4043 MET A CG    1 
ATOM   18648 S  SD    . MET A 1 4043 ? 66.731  87.236  79.275  1.00 45.84  ? 4043 MET A SD    1 
ATOM   18649 C  CE    . MET A 1 4043 ? 66.123  86.586  77.724  1.00 25.41  ? 4043 MET A CE    1 
ATOM   18650 N  N     . CYS A 1 4044 ? 71.560  91.203  80.097  1.00 10.02  ? 4044 CYS A N     1 
ATOM   18651 C  CA    . CYS A 1 4044 ? 72.313  92.047  81.008  1.00 9.06   ? 4044 CYS A CA    1 
ATOM   18652 C  C     . CYS A 1 4044 ? 71.387  93.111  81.578  1.00 7.35   ? 4044 CYS A C     1 
ATOM   18653 O  O     . CYS A 1 4044 ? 70.725  93.835  80.828  1.00 8.39   ? 4044 CYS A O     1 
ATOM   18654 C  CB    . CYS A 1 4044 ? 73.498  92.691  80.288  1.00 13.56  ? 4044 CYS A CB    1 
ATOM   18655 S  SG    . CYS A 1 4044 ? 74.474  91.529  79.305  1.00 17.24  ? 4044 CYS A SG    1 
ATOM   18656 N  N     . SER A 1 4045 ? 71.330  93.189  82.900  1.00 9.53   ? 4045 SER A N     1 
ATOM   18657 C  CA    . SER A 1 4045 ? 70.405  94.082  83.576  1.00 10.03  ? 4045 SER A CA    1 
ATOM   18658 C  C     . SER A 1 4045 ? 71.167  95.057  84.458  1.00 11.51  ? 4045 SER A C     1 
ATOM   18659 O  O     . SER A 1 4045 ? 72.208  94.725  85.031  1.00 13.58  ? 4045 SER A O     1 
ATOM   18660 C  CB    . SER A 1 4045 ? 69.388  93.301  84.417  1.00 11.60  ? 4045 SER A CB    1 
ATOM   18661 O  OG    . SER A 1 4045 ? 70.036  92.498  85.387  1.00 15.03  ? 4045 SER A OG    1 
ATOM   18662 N  N     . VAL A 1 4046 ? 70.633  96.270  84.554  1.00 11.89  ? 4046 VAL A N     1 
ATOM   18663 C  CA    . VAL A 1 4046 ? 71.140  97.284  85.472  1.00 17.54  ? 4046 VAL A CA    1 
ATOM   18664 C  C     . VAL A 1 4046 ? 70.754  96.849  86.882  1.00 19.74  ? 4046 VAL A C     1 
ATOM   18665 O  O     . VAL A 1 4046 ? 69.859  96.005  87.034  1.00 18.69  ? 4046 VAL A O     1 
ATOM   18666 C  CB    . VAL A 1 4046 ? 70.584  98.675  85.126  1.00 15.40  ? 4046 VAL A CB    1 
ATOM   18667 C  CG1   . VAL A 1 4046 ? 70.924  99.035  83.688  1.00 11.49  ? 4046 VAL A CG1   1 
ATOM   18668 C  CG2   . VAL A 1 4046 ? 69.082  98.716  85.351  1.00 15.82  ? 4046 VAL A CG2   1 
ATOM   18669 N  N     . PRO A 1 4047 ? 71.402  97.362  87.929  1.00 24.82  ? 4047 PRO A N     1 
ATOM   18670 C  CA    . PRO A 1 4047 ? 71.048  96.936  89.289  1.00 24.16  ? 4047 PRO A CA    1 
ATOM   18671 C  C     . PRO A 1 4047 ? 69.573  97.170  89.585  1.00 25.96  ? 4047 PRO A C     1 
ATOM   18672 O  O     . PRO A 1 4047 ? 68.998  98.196  89.215  1.00 31.45  ? 4047 PRO A O     1 
ATOM   18673 C  CB    . PRO A 1 4047 ? 71.944  97.808  90.173  1.00 24.85  ? 4047 PRO A CB    1 
ATOM   18674 C  CG    . PRO A 1 4047 ? 73.133  98.076  89.324  1.00 25.76  ? 4047 PRO A CG    1 
ATOM   18675 C  CD    . PRO A 1 4047 ? 72.598  98.225  87.924  1.00 24.99  ? 4047 PRO A CD    1 
ATOM   18676 N  N     . GLY A 1 4048 ? 68.965  96.199  90.263  1.00 26.09  ? 4048 GLY A N     1 
ATOM   18677 C  CA    . GLY A 1 4048 ? 67.555  96.242  90.575  1.00 27.38  ? 4048 GLY A CA    1 
ATOM   18678 C  C     . GLY A 1 4048 ? 66.647  95.574  89.567  1.00 23.66  ? 4048 GLY A C     1 
ATOM   18679 O  O     . GLY A 1 4048 ? 65.445  95.446  89.830  1.00 27.28  ? 4048 GLY A O     1 
ATOM   18680 N  N     . TYR A 1 4049 ? 67.175  95.145  88.425  1.00 20.59  ? 4049 TYR A N     1 
ATOM   18681 C  CA    . TYR A 1 4049 ? 66.393  94.470  87.401  1.00 22.65  ? 4049 TYR A CA    1 
ATOM   18682 C  C     . TYR A 1 4049 ? 66.957  93.077  87.164  1.00 29.05  ? 4049 TYR A C     1 
ATOM   18683 O  O     . TYR A 1 4049 ? 68.163  92.852  87.304  1.00 27.86  ? 4049 TYR A O     1 
ATOM   18684 C  CB    . TYR A 1 4049 ? 66.373  95.278  86.095  1.00 18.39  ? 4049 TYR A CB    1 
ATOM   18685 C  CG    . TYR A 1 4049 ? 65.469  96.491  86.160  1.00 19.55  ? 4049 TYR A CG    1 
ATOM   18686 C  CD1   . TYR A 1 4049 ? 65.770  97.564  86.989  1.00 19.22  ? 4049 TYR A CD1   1 
ATOM   18687 C  CD2   . TYR A 1 4049 ? 64.307  96.555  85.403  1.00 16.74  ? 4049 TYR A CD2   1 
ATOM   18688 C  CE1   . TYR A 1 4049 ? 64.943  98.667  87.059  1.00 16.42  ? 4049 TYR A CE1   1 
ATOM   18689 C  CE2   . TYR A 1 4049 ? 63.475  97.656  85.465  1.00 15.15  ? 4049 TYR A CE2   1 
ATOM   18690 C  CZ    . TYR A 1 4049 ? 63.797  98.708  86.295  1.00 18.22  ? 4049 TYR A CZ    1 
ATOM   18691 O  OH    . TYR A 1 4049 ? 62.971  99.806  86.363  1.00 24.22  ? 4049 TYR A OH    1 
ATOM   18692 N  N     . ASP A 1 4050 ? 66.074  92.141  86.825  1.00 26.35  ? 4050 ASP A N     1 
ATOM   18693 C  CA    . ASP A 1 4050 ? 66.459  90.753  86.611  1.00 25.36  ? 4050 ASP A CA    1 
ATOM   18694 C  C     . ASP A 1 4050 ? 65.527  90.146  85.576  1.00 22.32  ? 4050 ASP A C     1 
ATOM   18695 O  O     . ASP A 1 4050 ? 64.304  90.188  85.740  1.00 24.44  ? 4050 ASP A O     1 
ATOM   18696 C  CB    . ASP A 1 4050 ? 66.406  89.957  87.920  1.00 25.51  ? 4050 ASP A CB    1 
ATOM   18697 C  CG    . ASP A 1 4050 ? 66.471  88.459  87.696  1.00 33.05  ? 4050 ASP A CG    1 
ATOM   18698 O  OD1   . ASP A 1 4050 ? 67.468  87.985  87.112  1.00 25.95  ? 4050 ASP A OD1   1 
ATOM   18699 O  OD2   . ASP A 1 4050 ? 65.524  87.755  88.106  1.00 35.22  ? 4050 ASP A OD2   1 
ATOM   18700 N  N     . ALA A 1 4051 ? 66.106  89.588  84.515  1.00 19.81  ? 4051 ALA A N     1 
ATOM   18701 C  CA    . ALA A 1 4051 ? 65.347  89.055  83.393  1.00 19.52  ? 4051 ALA A CA    1 
ATOM   18702 C  C     . ALA A 1 4051 ? 65.065  87.563  83.519  1.00 21.50  ? 4051 ALA A C     1 
ATOM   18703 O  O     . ALA A 1 4051 ? 64.536  86.965  82.577  1.00 25.21  ? 4051 ALA A O     1 
ATOM   18704 C  CB    . ALA A 1 4051 ? 66.082  89.339  82.083  1.00 15.29  ? 4051 ALA A CB    1 
ATOM   18705 N  N     . SER A 1 4052 ? 65.413  86.947  84.652  1.00 18.67  ? 4052 SER A N     1 
ATOM   18706 C  CA    . SER A 1 4052 ? 65.141  85.524  84.833  1.00 22.52  ? 4052 SER A CA    1 
ATOM   18707 C  C     . SER A 1 4052 ? 63.644  85.241  84.814  1.00 26.06  ? 4052 SER A C     1 
ATOM   18708 O  O     . SER A 1 4052 ? 63.197  84.246  84.229  1.00 26.04  ? 4052 SER A O     1 
ATOM   18709 C  CB    . SER A 1 4052 ? 65.764  85.033  86.139  1.00 24.97  ? 4052 SER A CB    1 
ATOM   18710 O  OG    . SER A 1 4052 ? 67.098  85.493  86.270  1.00 27.81  ? 4052 SER A OG    1 
ATOM   18711 N  N     . GLY A 1 4053 ? 62.853  86.105  85.455  1.00 27.73  ? 4053 GLY A N     1 
ATOM   18712 C  CA    . GLY A 1 4053 ? 61.411  85.949  85.411  1.00 24.10  ? 4053 GLY A CA    1 
ATOM   18713 C  C     . GLY A 1 4053 ? 60.849  86.056  84.009  1.00 25.97  ? 4053 GLY A C     1 
ATOM   18714 O  O     . GLY A 1 4053 ? 59.885  85.366  83.669  1.00 31.56  ? 4053 GLY A O     1 
ATOM   18715 N  N     . HIS A 1 4054 ? 61.442  86.916  83.176  1.00 24.23  ? 4054 HIS A N     1 
ATOM   18716 C  CA    . HIS A 1 4054 ? 61.021  87.000  81.782  1.00 26.45  ? 4054 HIS A CA    1 
ATOM   18717 C  C     . HIS A 1 4054 ? 61.238  85.675  81.063  1.00 28.59  ? 4054 HIS A C     1 
ATOM   18718 O  O     . HIS A 1 4054 ? 60.368  85.217  80.315  1.00 33.76  ? 4054 HIS A O     1 
ATOM   18719 C  CB    . HIS A 1 4054 ? 61.774  88.125  81.071  1.00 27.41  ? 4054 HIS A CB    1 
ATOM   18720 C  CG    . HIS A 1 4054 ? 61.366  89.497  81.508  1.00 33.98  ? 4054 HIS A CG    1 
ATOM   18721 N  ND1   . HIS A 1 4054 ? 62.273  90.444  81.929  1.00 36.29  ? 4054 HIS A ND1   1 
ATOM   18722 C  CD2   . HIS A 1 4054 ? 60.147  90.082  81.588  1.00 39.75  ? 4054 HIS A CD2   1 
ATOM   18723 C  CE1   . HIS A 1 4054 ? 61.632  91.553  82.251  1.00 39.58  ? 4054 HIS A CE1   1 
ATOM   18724 N  NE2   . HIS A 1 4054 ? 60.340  91.360  82.053  1.00 45.10  ? 4054 HIS A NE2   1 
ATOM   18725 N  N     . VAL A 1 4055 ? 62.390  85.039  81.290  1.00 25.97  ? 4055 VAL A N     1 
ATOM   18726 C  CA    . VAL A 1 4055 ? 62.664  83.747  80.666  1.00 26.33  ? 4055 VAL A CA    1 
ATOM   18727 C  C     . VAL A 1 4055 ? 61.699  82.688  81.179  1.00 26.15  ? 4055 VAL A C     1 
ATOM   18728 O  O     . VAL A 1 4055 ? 61.219  81.843  80.414  1.00 26.60  ? 4055 VAL A O     1 
ATOM   18729 C  CB    . VAL A 1 4055 ? 64.127  83.337  80.906  1.00 18.63  ? 4055 VAL A CB    1 
ATOM   18730 C  CG1   . VAL A 1 4055 ? 64.453  82.063  80.146  1.00 12.29  ? 4055 VAL A CG1   1 
ATOM   18731 C  CG2   . VAL A 1 4055 ? 65.064  84.453  80.507  1.00 15.61  ? 4055 VAL A CG2   1 
ATOM   18732 N  N     . GLU A 1 4056 ? 61.416  82.699  82.484  1.00 28.08  ? 4056 GLU A N     1 
ATOM   18733 C  CA    . GLU A 1 4056 ? 60.489  81.719  83.043  1.00 30.57  ? 4056 GLU A CA    1 
ATOM   18734 C  C     . GLU A 1 4056 ? 59.091  81.880  82.454  1.00 34.67  ? 4056 GLU A C     1 
ATOM   18735 O  O     . GLU A 1 4056 ? 58.445  80.892  82.084  1.00 33.44  ? 4056 GLU A O     1 
ATOM   18736 C  CB    . GLU A 1 4056 ? 60.456  81.845  84.566  1.00 33.83  ? 4056 GLU A CB    1 
ATOM   18737 C  CG    . GLU A 1 4056 ? 61.763  81.448  85.235  1.00 37.41  ? 4056 GLU A CG    1 
ATOM   18738 C  CD    . GLU A 1 4056 ? 61.721  81.597  86.742  1.00 46.91  ? 4056 GLU A CD    1 
ATOM   18739 O  OE1   . GLU A 1 4056 ? 60.717  82.129  87.262  1.00 48.89  ? 4056 GLU A OE1   1 
ATOM   18740 O  OE2   . GLU A 1 4056 ? 62.694  81.185  87.407  1.00 45.28  ? 4056 GLU A OE2   1 
ATOM   18741 N  N     . ASP A 1 4057 ? 58.614  83.123  82.342  1.00 32.37  ? 4057 ASP A N     1 
ATOM   18742 C  CA    . ASP A 1 4057 ? 57.308  83.362  81.736  1.00 33.79  ? 4057 ASP A CA    1 
ATOM   18743 C  C     . ASP A 1 4057 ? 57.301  82.972  80.263  1.00 36.72  ? 4057 ASP A C     1 
ATOM   18744 O  O     . ASP A 1 4057 ? 56.310  82.424  79.766  1.00 39.46  ? 4057 ASP A O     1 
ATOM   18745 C  CB    . ASP A 1 4057 ? 56.906  84.827  81.909  1.00 38.62  ? 4057 ASP A CB    1 
ATOM   18746 C  CG    . ASP A 1 4057 ? 56.876  85.255  83.363  1.00 44.55  ? 4057 ASP A CG    1 
ATOM   18747 O  OD1   . ASP A 1 4057 ? 57.245  84.437  84.232  1.00 40.47  ? 4057 ASP A OD1   1 
ATOM   18748 O  OD2   . ASP A 1 4057 ? 56.485  86.409  83.637  1.00 45.81  ? 4057 ASP A OD2   1 
ATOM   18749 N  N     . LEU A 1 4058 ? 58.392  83.252  79.546  1.00 36.31  ? 4058 LEU A N     1 
ATOM   18750 C  CA    . LEU A 1 4058 ? 58.482  82.848  78.147  1.00 33.60  ? 4058 LEU A CA    1 
ATOM   18751 C  C     . LEU A 1 4058 ? 58.397  81.334  78.005  1.00 36.07  ? 4058 LEU A C     1 
ATOM   18752 O  O     . LEU A 1 4058 ? 57.677  80.822  77.140  1.00 39.46  ? 4058 LEU A O     1 
ATOM   18753 C  CB    . LEU A 1 4058 ? 59.782  83.373  77.537  1.00 27.80  ? 4058 LEU A CB    1 
ATOM   18754 C  CG    . LEU A 1 4058 ? 60.198  82.794  76.184  1.00 32.51  ? 4058 LEU A CG    1 
ATOM   18755 C  CD1   . LEU A 1 4058 ? 59.236  83.225  75.095  1.00 29.08  ? 4058 LEU A CD1   1 
ATOM   18756 C  CD2   . LEU A 1 4058 ? 61.621  83.208  75.841  1.00 25.84  ? 4058 LEU A CD2   1 
ATOM   18757 N  N     . ALA A 1 4059 ? 59.121  80.602  78.854  1.00 31.55  ? 4059 ALA A N     1 
ATOM   18758 C  CA    . ALA A 1 4059 ? 59.061  79.145  78.814  1.00 32.70  ? 4059 ALA A CA    1 
ATOM   18759 C  C     . ALA A 1 4059 ? 57.665  78.644  79.156  1.00 42.48  ? 4059 ALA A C     1 
ATOM   18760 O  O     . ALA A 1 4059 ? 57.193  77.656  78.581  1.00 39.29  ? 4059 ALA A O     1 
ATOM   18761 C  CB    . ALA A 1 4059 ? 60.097  78.551  79.767  1.00 27.55  ? 4059 ALA A CB    1 
ATOM   18762 N  N     . ALA A 1 4060 ? 56.992  79.307  80.100  1.00 42.50  ? 4060 ALA A N     1 
ATOM   18763 C  CA    . ALA A 1 4060 ? 55.621  78.929  80.430  1.00 40.55  ? 4060 ALA A CA    1 
ATOM   18764 C  C     . ALA A 1 4060 ? 54.689  79.124  79.239  1.00 42.80  ? 4060 ALA A C     1 
ATOM   18765 O  O     . ALA A 1 4060 ? 53.853  78.261  78.949  1.00 45.36  ? 4060 ALA A O     1 
ATOM   18766 C  CB    . ALA A 1 4060 ? 55.130  79.732  81.634  1.00 33.98  ? 4060 ALA A CB    1 
ATOM   18767 N  N     . GLU A 1 4061 ? 54.813  80.256  78.539  1.00 39.25  ? 4061 GLU A N     1 
ATOM   18768 C  CA    . GLU A 1 4061 ? 53.959  80.504  77.379  1.00 45.49  ? 4061 GLU A CA    1 
ATOM   18769 C  C     . GLU A 1 4061 ? 54.240  79.514  76.255  1.00 48.49  ? 4061 GLU A C     1 
ATOM   18770 O  O     . GLU A 1 4061 ? 53.308  78.983  75.640  1.00 54.41  ? 4061 GLU A O     1 
ATOM   18771 C  CB    . GLU A 1 4061 ? 54.128  81.939  76.878  1.00 50.35  ? 4061 GLU A CB    1 
ATOM   18772 C  CG    . GLU A 1 4061 ? 53.944  83.009  77.937  1.00 53.01  ? 4061 GLU A CG    1 
ATOM   18773 C  CD    . GLU A 1 4061 ? 54.781  84.244  77.667  1.00 59.10  ? 4061 GLU A CD    1 
ATOM   18774 O  OE1   . GLU A 1 4061 ? 55.481  84.275  76.633  1.00 57.68  ? 4061 GLU A OE1   1 
ATOM   18775 O  OE2   . GLU A 1 4061 ? 54.740  85.184  78.488  1.00 55.81  ? 4061 GLU A OE2   1 
ATOM   18776 N  N     . GLN A 1 4062 ? 55.517  79.251  75.969  1.00 46.61  ? 4062 GLN A N     1 
ATOM   18777 C  CA    . GLN A 1 4062 ? 55.859  78.313  74.905  1.00 47.14  ? 4062 GLN A CA    1 
ATOM   18778 C  C     . GLN A 1 4062 ? 55.600  76.862  75.287  1.00 48.57  ? 4062 GLN A C     1 
ATOM   18779 O  O     . GLN A 1 4062 ? 55.735  75.986  74.426  1.00 50.83  ? 4062 GLN A O     1 
ATOM   18780 C  CB    . GLN A 1 4062 ? 57.324  78.479  74.494  1.00 47.63  ? 4062 GLN A CB    1 
ATOM   18781 C  CG    . GLN A 1 4062 ? 57.732  79.906  74.176  1.00 44.13  ? 4062 GLN A CG    1 
ATOM   18782 C  CD    . GLN A 1 4062 ? 57.406  80.301  72.751  1.00 51.40  ? 4062 GLN A CD    1 
ATOM   18783 O  OE1   . GLN A 1 4062 ? 56.283  80.702  72.446  1.00 52.93  ? 4062 GLN A OE1   1 
ATOM   18784 N  NE2   . GLN A 1 4062 ? 58.391  80.188  71.867  1.00 46.76  ? 4062 GLN A NE2   1 
ATOM   18785 N  N     . ASN A 1 4063 ? 55.242  76.593  76.544  1.00 48.96  ? 4063 ASN A N     1 
ATOM   18786 C  CA    . ASN A 1 4063 ? 55.032  75.230  77.038  1.00 49.93  ? 4063 ASN A CA    1 
ATOM   18787 C  C     . ASN A 1 4063 ? 56.284  74.378  76.846  1.00 50.77  ? 4063 ASN A C     1 
ATOM   18788 O  O     . ASN A 1 4063 ? 56.208  73.177  76.580  1.00 55.34  ? 4063 ASN A O     1 
ATOM   18789 C  CB    . ASN A 1 4063 ? 53.818  74.574  76.375  1.00 51.17  ? 4063 ASN A CB    1 
ATOM   18790 C  CG    . ASN A 1 4063 ? 52.524  74.872  77.105  1.00 61.05  ? 4063 ASN A CG    1 
ATOM   18791 O  OD1   . ASN A 1 4063 ? 51.695  75.649  76.632  1.00 59.90  ? 4063 ASN A OD1   1 
ATOM   18792 N  ND2   . ASN A 1 4063 ? 52.345  74.253  78.267  1.00 67.61  ? 4063 ASN A ND2   1 
ATOM   18793 N  N     . THR A 1 4064 ? 57.446  75.008  76.983  1.00 44.58  ? 4064 THR A N     1 
ATOM   18794 C  CA    . THR A 1 4064 ? 58.729  74.332  76.879  1.00 39.41  ? 4064 THR A CA    1 
ATOM   18795 C  C     . THR A 1 4064 ? 59.364  74.228  78.260  1.00 39.62  ? 4064 THR A C     1 
ATOM   18796 O  O     . THR A 1 4064 ? 59.264  75.152  79.074  1.00 37.51  ? 4064 THR A O     1 
ATOM   18797 C  CB    . THR A 1 4064 ? 59.665  75.063  75.904  1.00 36.63  ? 4064 THR A CB    1 
ATOM   18798 O  OG1   . THR A 1 4064 ? 60.873  74.310  75.734  1.00 34.06  ? 4064 THR A OG1   1 
ATOM   18799 C  CG2   . THR A 1 4064 ? 59.997  76.467  76.395  1.00 33.56  ? 4064 THR A CG2   1 
ATOM   18800 N  N     . GLN A 1 4065 ? 59.986  73.085  78.530  1.00 39.16  ? 4065 GLN A N     1 
ATOM   18801 C  CA    . GLN A 1 4065 ? 60.620  72.857  79.818  1.00 38.40  ? 4065 GLN A CA    1 
ATOM   18802 C  C     . GLN A 1 4065 ? 61.963  73.572  79.875  1.00 33.40  ? 4065 GLN A C     1 
ATOM   18803 O  O     . GLN A 1 4065 ? 62.686  73.647  78.878  1.00 29.08  ? 4065 GLN A O     1 
ATOM   18804 C  CB    . GLN A 1 4065 ? 60.805  71.360  80.063  1.00 39.68  ? 4065 GLN A CB    1 
ATOM   18805 C  CG    . GLN A 1 4065 ? 59.529  70.546  79.927  1.00 48.17  ? 4065 GLN A CG    1 
ATOM   18806 C  CD    . GLN A 1 4065 ? 58.540  70.823  81.041  1.00 59.69  ? 4065 GLN A CD    1 
ATOM   18807 O  OE1   . GLN A 1 4065 ? 58.717  70.369  82.171  1.00 71.07  ? 4065 GLN A OE1   1 
ATOM   18808 N  NE2   . GLN A 1 4065 ? 57.489  71.571  80.726  1.00 49.62  ? 4065 GLN A NE2   1 
ATOM   18809 N  N     . ILE A 1 4066 ? 62.288  74.112  81.047  1.00 26.72  ? 4066 ILE A N     1 
ATOM   18810 C  CA    . ILE A 1 4066 ? 63.529  74.851  81.245  1.00 21.48  ? 4066 ILE A CA    1 
ATOM   18811 C  C     . ILE A 1 4066 ? 64.113  74.481  82.601  1.00 23.53  ? 4066 ILE A C     1 
ATOM   18812 O  O     . ILE A 1 4066 ? 63.384  74.323  83.586  1.00 31.71  ? 4066 ILE A O     1 
ATOM   18813 C  CB    . ILE A 1 4066 ? 63.308  76.375  81.132  1.00 21.49  ? 4066 ILE A CB    1 
ATOM   18814 C  CG1   . ILE A 1 4066 ? 64.626  77.127  81.331  1.00 16.88  ? 4066 ILE A CG1   1 
ATOM   18815 C  CG2   . ILE A 1 4066 ? 62.260  76.847  82.130  1.00 20.93  ? 4066 ILE A CG2   1 
ATOM   18816 C  CD1   . ILE A 1 4066 ? 64.673  78.465  80.639  1.00 15.09  ? 4066 ILE A CD1   1 
ATOM   18817 N  N     . THR A 1 4067 ? 65.432  74.324  82.643  1.00 21.09  ? 4067 THR A N     1 
ATOM   18818 C  CA    . THR A 1 4067 ? 66.164  74.121  83.888  1.00 19.72  ? 4067 THR A CA    1 
ATOM   18819 C  C     . THR A 1 4067 ? 66.903  75.409  84.224  1.00 16.69  ? 4067 THR A C     1 
ATOM   18820 O  O     . THR A 1 4067 ? 67.685  75.908  83.408  1.00 15.26  ? 4067 THR A O     1 
ATOM   18821 C  CB    . THR A 1 4067 ? 67.144  72.952  83.774  1.00 22.23  ? 4067 THR A CB    1 
ATOM   18822 O  OG1   . THR A 1 4067 ? 66.414  71.725  83.649  1.00 32.88  ? 4067 THR A OG1   1 
ATOM   18823 C  CG2   . THR A 1 4067 ? 68.039  72.880  85.002  1.00 18.46  ? 4067 THR A CG2   1 
ATOM   18824 N  N     . SER A 1 4068 ? 66.661  75.938  85.420  1.00 15.46  ? 4068 SER A N     1 
ATOM   18825 C  CA    . SER A 1 4068 ? 67.255  77.190  85.869  1.00 11.28  ? 4068 SER A CA    1 
ATOM   18826 C  C     . SER A 1 4068 ? 68.242  76.906  86.993  1.00 11.70  ? 4068 SER A C     1 
ATOM   18827 O  O     . SER A 1 4068 ? 67.901  76.225  87.965  1.00 18.79  ? 4068 SER A O     1 
ATOM   18828 C  CB    . SER A 1 4068 ? 66.178  78.165  86.345  1.00 12.00  ? 4068 SER A CB    1 
ATOM   18829 O  OG    . SER A 1 4068 ? 65.173  78.329  85.361  1.00 28.05  ? 4068 SER A OG    1 
ATOM   18830 N  N     . ILE A 1 4069 ? 69.460  77.427  86.857  1.00 9.50   ? 4069 ILE A N     1 
ATOM   18831 C  CA    . ILE A 1 4069 ? 70.538  77.156  87.801  1.00 9.51   ? 4069 ILE A CA    1 
ATOM   18832 C  C     . ILE A 1 4069 ? 71.228  78.461  88.175  1.00 7.91   ? 4069 ILE A C     1 
ATOM   18833 O  O     . ILE A 1 4069 ? 71.541  79.279  87.302  1.00 8.85   ? 4069 ILE A O     1 
ATOM   18834 C  CB    . ILE A 1 4069 ? 71.559  76.150  87.233  1.00 10.67  ? 4069 ILE A CB    1 
ATOM   18835 C  CG1   . ILE A 1 4069 ? 70.862  74.850  86.828  1.00 13.17  ? 4069 ILE A CG1   1 
ATOM   18836 C  CG2   . ILE A 1 4069 ? 72.659  75.869  88.240  1.00 9.98   ? 4069 ILE A CG2   1 
ATOM   18837 C  CD1   . ILE A 1 4069 ? 71.757  73.879  86.108  1.00 14.28  ? 4069 ILE A CD1   1 
ATOM   18838 N  N     . ALA A 1 4070 ? 71.454  78.652  89.472  1.00 10.32  ? 4070 ALA A N     1 
ATOM   18839 C  CA    . ALA A 1 4070 ? 72.353  79.689  89.950  1.00 8.65   ? 4070 ALA A CA    1 
ATOM   18840 C  C     . ALA A 1 4070 ? 73.795  79.202  89.861  1.00 12.26  ? 4070 ALA A C     1 
ATOM   18841 O  O     . ALA A 1 4070 ? 74.095  78.032  90.114  1.00 15.95  ? 4070 ALA A O     1 
ATOM   18842 C  CB    . ALA A 1 4070 ? 72.012  80.079  91.385  1.00 11.59  ? 4070 ALA A CB    1 
ATOM   18843 N  N     . ILE A 1 4071 ? 74.693  80.120  89.517  1.00 10.82  ? 4071 ILE A N     1 
ATOM   18844 C  CA    . ILE A 1 4071 ? 76.016  79.756  89.021  1.00 17.19  ? 4071 ILE A CA    1 
ATOM   18845 C  C     . ILE A 1 4071 ? 77.045  79.752  90.149  1.00 24.33  ? 4071 ILE A C     1 
ATOM   18846 O  O     . ILE A 1 4071 ? 78.105  79.124  90.036  1.00 25.22  ? 4071 ILE A O     1 
ATOM   18847 C  CB    . ILE A 1 4071 ? 76.408  80.706  87.870  1.00 11.72  ? 4071 ILE A CB    1 
ATOM   18848 C  CG1   . ILE A 1 4071 ? 75.581  80.372  86.628  1.00 11.81  ? 4071 ILE A CG1   1 
ATOM   18849 C  CG2   . ILE A 1 4071 ? 77.878  80.611  87.513  1.00 9.14   ? 4071 ILE A CG2   1 
ATOM   18850 C  CD1   . ILE A 1 4071 ? 75.564  78.893  86.298  1.00 10.04  ? 4071 ILE A CD1   1 
ATOM   18851 N  N     . GLY A 1 4072 ? 76.710  80.395  91.271  1.00 14.67  ? 4072 GLY A N     1 
ATOM   18852 C  CA    . GLY A 1 4072 ? 77.710  80.658  92.297  1.00 12.08  ? 4072 GLY A CA    1 
ATOM   18853 C  C     . GLY A 1 4072 ? 78.398  79.413  92.834  1.00 14.93  ? 4072 GLY A C     1 
ATOM   18854 O  O     . GLY A 1 4072 ? 79.618  79.399  93.012  1.00 15.87  ? 4072 GLY A O     1 
ATOM   18855 N  N     . SER A 1 4073 ? 77.634  78.359  93.103  1.00 17.32  ? 4073 SER A N     1 
ATOM   18856 C  CA    . SER A 1 4073 ? 78.198  77.162  93.712  1.00 15.89  ? 4073 SER A CA    1 
ATOM   18857 C  C     . SER A 1 4073 ? 78.946  76.317  92.686  1.00 21.63  ? 4073 SER A C     1 
ATOM   18858 O  O     . SER A 1 4073 ? 78.675  76.374  91.483  1.00 20.76  ? 4073 SER A O     1 
ATOM   18859 C  CB    . SER A 1 4073 ? 77.100  76.327  94.371  1.00 15.34  ? 4073 SER A CB    1 
ATOM   18860 O  OG    . SER A 1 4073 ? 77.600  75.077  94.813  1.00 23.97  ? 4073 SER A OG    1 
ATOM   18861 N  N     . ALA A 1 4074 ? 79.910  75.531  93.178  1.00 20.53  ? 4074 ALA A N     1 
ATOM   18862 C  CA    . ALA A 1 4074 ? 80.603  74.575  92.317  1.00 19.88  ? 4074 ALA A CA    1 
ATOM   18863 C  C     . ALA A 1 4074 ? 79.661  73.468  91.862  1.00 23.89  ? 4074 ALA A C     1 
ATOM   18864 O  O     . ALA A 1 4074 ? 79.704  73.038  90.699  1.00 30.38  ? 4074 ALA A O     1 
ATOM   18865 C  CB    . ALA A 1 4074 ? 81.812  73.990  93.045  1.00 14.54  ? 4074 ALA A CB    1 
ATOM   18866 N  N     . GLU A 1 4075 ? 78.808  72.988  92.770  1.00 21.10  ? 4075 GLU A N     1 
ATOM   18867 C  CA    . GLU A 1 4075 ? 77.716  72.116  92.361  1.00 27.40  ? 4075 GLU A CA    1 
ATOM   18868 C  C     . GLU A 1 4075 ? 76.841  72.799  91.322  1.00 27.03  ? 4075 GLU A C     1 
ATOM   18869 O  O     . GLU A 1 4075 ? 76.284  72.133  90.443  1.00 29.40  ? 4075 GLU A O     1 
ATOM   18870 C  CB    . GLU A 1 4075 ? 76.891  71.702  93.580  1.00 28.45  ? 4075 GLU A CB    1 
ATOM   18871 C  CG    . GLU A 1 4075 ? 75.745  70.751  93.274  1.00 37.55  ? 4075 GLU A CG    1 
ATOM   18872 C  CD    . GLU A 1 4075 ? 76.217  69.401  92.769  1.00 47.54  ? 4075 GLU A CD    1 
ATOM   18873 O  OE1   . GLU A 1 4075 ? 77.356  69.004  93.095  1.00 48.17  ? 4075 GLU A OE1   1 
ATOM   18874 O  OE2   . GLU A 1 4075 ? 75.448  68.736  92.044  1.00 46.59  ? 4075 GLU A OE2   1 
ATOM   18875 N  N     . GLY A 1 4076 ? 76.726  74.127  91.394  1.00 20.63  ? 4076 GLY A N     1 
ATOM   18876 C  CA    . GLY A 1 4076 ? 76.064  74.861  90.331  1.00 16.58  ? 4076 GLY A CA    1 
ATOM   18877 C  C     . GLY A 1 4076 ? 76.762  74.703  88.994  1.00 17.29  ? 4076 GLY A C     1 
ATOM   18878 O  O     . GLY A 1 4076 ? 76.111  74.527  87.964  1.00 18.39  ? 4076 GLY A O     1 
ATOM   18879 N  N     . PHE A 1 4077 ? 78.097  74.754  88.993  1.00 20.27  ? 4077 PHE A N     1 
ATOM   18880 C  CA    . PHE A 1 4077 ? 78.850  74.541  87.759  1.00 16.44  ? 4077 PHE A CA    1 
ATOM   18881 C  C     . PHE A 1 4077 ? 78.607  73.142  87.206  1.00 19.39  ? 4077 PHE A C     1 
ATOM   18882 O  O     . PHE A 1 4077 ? 78.387  72.963  85.999  1.00 23.66  ? 4077 PHE A O     1 
ATOM   18883 C  CB    . PHE A 1 4077 ? 80.343  74.755  88.011  1.00 11.33  ? 4077 PHE A CB    1 
ATOM   18884 C  CG    . PHE A 1 4077 ? 80.713  76.173  88.330  1.00 14.27  ? 4077 PHE A CG    1 
ATOM   18885 C  CD1   . PHE A 1 4077 ? 80.303  77.213  87.515  1.00 12.86  ? 4077 PHE A CD1   1 
ATOM   18886 C  CD2   . PHE A 1 4077 ? 81.477  76.464  89.448  1.00 18.92  ? 4077 PHE A CD2   1 
ATOM   18887 C  CE1   . PHE A 1 4077 ? 80.649  78.515  87.811  1.00 13.95  ? 4077 PHE A CE1   1 
ATOM   18888 C  CE2   . PHE A 1 4077 ? 81.823  77.765  89.749  1.00 14.68  ? 4077 PHE A CE2   1 
ATOM   18889 C  CZ    . PHE A 1 4077 ? 81.409  78.791  88.930  1.00 14.38  ? 4077 PHE A CZ    1 
ATOM   18890 N  N     . ASN A 1 4078 ? 78.650  72.134  88.080  1.00 18.84  ? 4078 ASN A N     1 
ATOM   18891 C  CA    . ASN A 1 4078 ? 78.438  70.760  87.631  1.00 19.63  ? 4078 ASN A CA    1 
ATOM   18892 C  C     . ASN A 1 4078 ? 77.035  70.573  87.064  1.00 19.63  ? 4078 ASN A C     1 
ATOM   18893 O  O     . ASN A 1 4078 ? 76.860  69.964  85.999  1.00 22.50  ? 4078 ASN A O     1 
ATOM   18894 C  CB    . ASN A 1 4078 ? 78.687  69.788  88.783  1.00 28.16  ? 4078 ASN A CB    1 
ATOM   18895 C  CG    . ASN A 1 4078 ? 80.144  69.734  89.196  1.00 34.12  ? 4078 ASN A CG    1 
ATOM   18896 O  OD1   . ASN A 1 4078 ? 81.041  69.916  88.374  1.00 36.56  ? 4078 ASN A OD1   1 
ATOM   18897 N  ND2   . ASN A 1 4078 ? 80.386  69.483  90.477  1.00 32.24  ? 4078 ASN A ND2   1 
ATOM   18898 N  N     . GLN A 1 4079 ? 76.022  71.099  87.760  1.00 20.71  ? 4079 GLN A N     1 
ATOM   18899 C  CA    . GLN A 1 4079 ? 74.654  70.990  87.270  1.00 19.35  ? 4079 GLN A CA    1 
ATOM   18900 C  C     . GLN A 1 4079 ? 74.473  71.749  85.964  1.00 18.29  ? 4079 GLN A C     1 
ATOM   18901 O  O     . GLN A 1 4079 ? 73.732  71.303  85.085  1.00 21.97  ? 4079 GLN A O     1 
ATOM   18902 C  CB    . GLN A 1 4079 ? 73.666  71.493  88.323  1.00 19.02  ? 4079 GLN A CB    1 
ATOM   18903 C  CG    . GLN A 1 4079 ? 73.602  70.642  89.579  1.00 28.38  ? 4079 GLN A CG    1 
ATOM   18904 C  CD    . GLN A 1 4079 ? 73.178  71.437  90.797  1.00 38.82  ? 4079 GLN A CD    1 
ATOM   18905 O  OE1   . GLN A 1 4079 ? 73.178  72.667  90.782  1.00 33.28  ? 4079 GLN A OE1   1 
ATOM   18906 N  NE2   . GLN A 1 4079 ? 72.799  70.734  91.859  1.00 36.86  ? 4079 GLN A NE2   1 
ATOM   18907 N  N     . ALA A 1 4080 ? 75.129  72.902  85.820  1.00 16.84  ? 4080 ALA A N     1 
ATOM   18908 C  CA    . ALA A 1 4080 ? 75.044  73.647  84.569  1.00 15.53  ? 4080 ALA A CA    1 
ATOM   18909 C  C     . ALA A 1 4080 ? 75.624  72.841  83.417  1.00 16.07  ? 4080 ALA A C     1 
ATOM   18910 O  O     . ALA A 1 4080 ? 75.034  72.770  82.333  1.00 18.57  ? 4080 ALA A O     1 
ATOM   18911 C  CB    . ALA A 1 4080 ? 75.762  74.990  84.707  1.00 9.53   ? 4080 ALA A CB    1 
ATOM   18912 N  N     . ASP A 1 4081 ? 76.780  72.210  83.642  1.00 16.93  ? 4081 ASP A N     1 
ATOM   18913 C  CA    . ASP A 1 4081 ? 77.377  71.385  82.596  1.00 18.85  ? 4081 ASP A CA    1 
ATOM   18914 C  C     . ASP A 1 4081 ? 76.464  70.226  82.215  1.00 20.74  ? 4081 ASP A C     1 
ATOM   18915 O  O     . ASP A 1 4081 ? 76.214  69.988  81.024  1.00 18.96  ? 4081 ASP A O     1 
ATOM   18916 C  CB    . ASP A 1 4081 ? 78.742  70.868  83.049  1.00 21.54  ? 4081 ASP A CB    1 
ATOM   18917 C  CG    . ASP A 1 4081 ? 79.465  70.100  81.959  1.00 31.16  ? 4081 ASP A CG    1 
ATOM   18918 O  OD1   . ASP A 1 4081 ? 79.600  68.865  82.089  1.00 34.40  ? 4081 ASP A OD1   1 
ATOM   18919 O  OD2   . ASP A 1 4081 ? 79.897  70.731  80.972  1.00 28.75  ? 4081 ASP A OD2   1 
ATOM   18920 N  N     . LYS A 1 4082 ? 75.941  69.501  83.211  1.00 16.71  ? 4082 LYS A N     1 
ATOM   18921 C  CA    . LYS A 1 4082 ? 75.068  68.369  82.906  1.00 17.49  ? 4082 LYS A CA    1 
ATOM   18922 C  C     . LYS A 1 4082 ? 73.790  68.821  82.206  1.00 20.23  ? 4082 LYS A C     1 
ATOM   18923 O  O     . LYS A 1 4082 ? 73.336  68.176  81.253  1.00 19.83  ? 4082 LYS A O     1 
ATOM   18924 C  CB    . LYS A 1 4082 ? 74.730  67.583  84.174  1.00 21.35  ? 4082 LYS A CB    1 
ATOM   18925 C  CG    . LYS A 1 4082 ? 75.926  67.183  85.019  1.00 25.16  ? 4082 LYS A CG    1 
ATOM   18926 C  CD    . LYS A 1 4082 ? 75.481  66.711  86.396  1.00 24.45  ? 4082 LYS A CD    1 
ATOM   18927 C  CE    . LYS A 1 4082 ? 76.659  66.539  87.340  1.00 30.57  ? 4082 LYS A CE    1 
ATOM   18928 N  NZ    . LYS A 1 4082 ? 76.504  67.363  88.569  1.00 29.14  ? 4082 LYS A NZ    1 
ATOM   18929 N  N     . ALA A 1 4083 ? 73.193  69.922  82.667  1.00 20.94  ? 4083 ALA A N     1 
ATOM   18930 C  CA    . ALA A 1 4083 ? 71.958  70.411  82.068  1.00 18.26  ? 4083 ALA A CA    1 
ATOM   18931 C  C     . ALA A 1 4083 ? 72.177  70.853  80.629  1.00 17.53  ? 4083 ALA A C     1 
ATOM   18932 O  O     . ALA A 1 4083 ? 71.341  70.582  79.763  1.00 17.66  ? 4083 ALA A O     1 
ATOM   18933 C  CB    . ALA A 1 4083 ? 71.388  71.558  82.902  1.00 12.84  ? 4083 ALA A CB    1 
ATOM   18934 N  N     . ILE A 1 4084 ? 73.291  71.533  80.353  1.00 12.92  ? 4084 ILE A N     1 
ATOM   18935 C  CA    . ILE A 1 4084 ? 73.586  71.942  78.983  1.00 13.53  ? 4084 ILE A CA    1 
ATOM   18936 C  C     . ILE A 1 4084 ? 73.800  70.721  78.098  1.00 17.42  ? 4084 ILE A C     1 
ATOM   18937 O  O     . ILE A 1 4084 ? 73.288  70.652  76.972  1.00 19.76  ? 4084 ILE A O     1 
ATOM   18938 C  CB    . ILE A 1 4084 ? 74.802  72.886  78.962  1.00 16.81  ? 4084 ILE A CB    1 
ATOM   18939 C  CG1   . ILE A 1 4084 ? 74.404  74.271  79.477  1.00 12.35  ? 4084 ILE A CG1   1 
ATOM   18940 C  CG2   . ILE A 1 4084 ? 75.387  72.984  77.562  1.00 13.88  ? 4084 ILE A CG2   1 
ATOM   18941 C  CD1   . ILE A 1 4084 ? 75.575  75.185  79.739  1.00 11.04  ? 4084 ILE A CD1   1 
ATOM   18942 N  N     . ASN A 1 4085 ? 74.554  69.734  78.595  1.00 19.90  ? 4085 ASN A N     1 
ATOM   18943 C  CA    . ASN A 1 4085 ? 74.809  68.533  77.805  1.00 16.33  ? 4085 ASN A CA    1 
ATOM   18944 C  C     . ASN A 1 4085 ? 73.517  67.778  77.513  1.00 17.58  ? 4085 ASN A C     1 
ATOM   18945 O  O     . ASN A 1 4085 ? 73.350  67.216  76.424  1.00 22.55  ? 4085 ASN A O     1 
ATOM   18946 C  CB    . ASN A 1 4085 ? 75.807  67.631  78.531  1.00 16.37  ? 4085 ASN A CB    1 
ATOM   18947 C  CG    . ASN A 1 4085 ? 77.200  68.227  78.578  1.00 19.16  ? 4085 ASN A CG    1 
ATOM   18948 O  OD1   . ASN A 1 4085 ? 77.509  69.169  77.850  1.00 27.86  ? 4085 ASN A OD1   1 
ATOM   18949 N  ND2   . ASN A 1 4085 ? 78.048  67.681  79.441  1.00 17.90  ? 4085 ASN A ND2   1 
ATOM   18950 N  N     . THR A 1 4086 ? 72.596  67.745  78.477  1.00 17.84  ? 4086 THR A N     1 
ATOM   18951 C  CA    . THR A 1 4086 ? 71.312  67.090  78.248  1.00 19.53  ? 4086 THR A CA    1 
ATOM   18952 C  C     . THR A 1 4086 ? 70.441  67.893  77.288  1.00 19.14  ? 4086 THR A C     1 
ATOM   18953 O  O     . THR A 1 4086 ? 69.753  67.318  76.436  1.00 20.17  ? 4086 THR A O     1 
ATOM   18954 C  CB    . THR A 1 4086 ? 70.587  66.879  79.577  1.00 19.16  ? 4086 THR A CB    1 
ATOM   18955 O  OG1   . THR A 1 4086 ? 71.479  66.269  80.519  1.00 19.11  ? 4086 THR A OG1   1 
ATOM   18956 C  CG2   . THR A 1 4086 ? 69.374  65.983  79.387  1.00 21.83  ? 4086 THR A CG2   1 
ATOM   18957 N  N     . ALA A 1 4087 ? 70.460  69.222  77.408  1.00 21.15  ? 4087 ALA A N     1 
ATOM   18958 C  CA    . ALA A 1 4087 ? 69.544  70.057  76.641  1.00 19.40  ? 4087 ALA A CA    1 
ATOM   18959 C  C     . ALA A 1 4087 ? 69.949  70.166  75.180  1.00 18.92  ? 4087 ALA A C     1 
ATOM   18960 O  O     . ALA A 1 4087 ? 69.078  70.270  74.308  1.00 20.61  ? 4087 ALA A O     1 
ATOM   18961 C  CB    . ALA A 1 4087 ? 69.461  71.447  77.266  1.00 17.86  ? 4087 ALA A CB    1 
ATOM   18962 N  N     . VAL A 1 4088 ? 71.251  70.157  74.886  1.00 16.53  ? 4088 VAL A N     1 
ATOM   18963 C  CA    . VAL A 1 4088 ? 71.687  70.276  73.498  1.00 18.76  ? 4088 VAL A CA    1 
ATOM   18964 C  C     . VAL A 1 4088 ? 71.255  69.098  72.640  1.00 26.16  ? 4088 VAL A C     1 
ATOM   18965 O  O     . VAL A 1 4088 ? 71.243  69.213  71.409  1.00 32.87  ? 4088 VAL A O     1 
ATOM   18966 C  CB    . VAL A 1 4088 ? 73.217  70.446  73.408  1.00 20.52  ? 4088 VAL A CB    1 
ATOM   18967 C  CG1   . VAL A 1 4088 ? 73.639  71.743  74.074  1.00 14.12  ? 4088 VAL A CG1   1 
ATOM   18968 C  CG2   . VAL A 1 4088 ? 73.925  69.258  74.032  1.00 18.62  ? 4088 VAL A CG2   1 
ATOM   18969 N  N     . LYS A 1 4089 ? 70.900  67.970  73.251  1.00 27.24  ? 4089 LYS A N     1 
ATOM   18970 C  CA    . LYS A 1 4089 ? 70.458  66.791  72.519  1.00 25.35  ? 4089 LYS A CA    1 
ATOM   18971 C  C     . LYS A 1 4089 ? 68.945  66.612  72.526  1.00 25.52  ? 4089 LYS A C     1 
ATOM   18972 O  O     . LYS A 1 4089 ? 68.453  65.625  71.971  1.00 38.52  ? 4089 LYS A O     1 
ATOM   18973 C  CB    . LYS A 1 4089 ? 71.123  65.537  73.094  1.00 26.23  ? 4089 LYS A CB    1 
ATOM   18974 C  CG    . LYS A 1 4089 ? 72.626  65.483  72.890  1.00 30.61  ? 4089 LYS A CG    1 
ATOM   18975 C  CD    . LYS A 1 4089 ? 73.189  64.140  73.321  1.00 36.42  ? 4089 LYS A CD    1 
ATOM   18976 C  CE    . LYS A 1 4089 ? 73.210  64.011  74.835  1.00 40.68  ? 4089 LYS A CE    1 
ATOM   18977 N  NZ    . LYS A 1 4089 ? 73.852  62.741  75.273  1.00 53.76  ? 4089 LYS A NZ    1 
ATOM   18978 N  N     . SER A 1 4090 ? 68.195  67.531  73.136  1.00 22.06  ? 4090 SER A N     1 
ATOM   18979 C  CA    . SER A 1 4090 ? 66.753  67.362  73.250  1.00 24.61  ? 4090 SER A CA    1 
ATOM   18980 C  C     . SER A 1 4090 ? 65.946  68.627  72.991  1.00 29.62  ? 4090 SER A C     1 
ATOM   18981 O  O     . SER A 1 4090 ? 64.717  68.576  73.091  1.00 29.69  ? 4090 SER A O     1 
ATOM   18982 C  CB    . SER A 1 4090 ? 66.394  66.819  74.644  1.00 20.32  ? 4090 SER A CB    1 
ATOM   18983 O  OG    . SER A 1 4090 ? 66.747  67.745  75.656  1.00 21.24  ? 4090 SER A OG    1 
ATOM   18984 N  N     . GLY A 1 4091 ? 66.581  69.750  72.666  1.00 24.87  ? 4091 GLY A N     1 
ATOM   18985 C  CA    . GLY A 1 4091 ? 65.854  70.994  72.517  1.00 21.35  ? 4091 GLY A CA    1 
ATOM   18986 C  C     . GLY A 1 4091 ? 65.434  71.631  73.820  1.00 23.38  ? 4091 GLY A C     1 
ATOM   18987 O  O     . GLY A 1 4091 ? 64.688  72.616  73.802  1.00 23.73  ? 4091 GLY A O     1 
ATOM   18988 N  N     . ARG A 1 4092 ? 65.890  71.094  74.946  1.00 26.70  ? 4092 ARG A N     1 
ATOM   18989 C  CA    . ARG A 1 4092 ? 65.550  71.619  76.259  1.00 24.09  ? 4092 ARG A CA    1 
ATOM   18990 C  C     . ARG A 1 4092 ? 66.186  72.992  76.462  1.00 21.04  ? 4092 ARG A C     1 
ATOM   18991 O  O     . ARG A 1 4092 ? 67.212  73.320  75.862  1.00 22.27  ? 4092 ARG A O     1 
ATOM   18992 C  CB    . ARG A 1 4092 ? 66.018  70.631  77.331  1.00 28.10  ? 4092 ARG A CB    1 
ATOM   18993 C  CG    . ARG A 1 4092 ? 65.724  71.001  78.767  1.00 31.86  ? 4092 ARG A CG    1 
ATOM   18994 C  CD    . ARG A 1 4092 ? 64.252  70.911  79.086  1.00 37.52  ? 4092 ARG A CD    1 
ATOM   18995 N  NE    . ARG A 1 4092 ? 63.997  71.214  80.489  1.00 37.29  ? 4092 ARG A NE    1 
ATOM   18996 C  CZ    . ARG A 1 4092 ? 63.973  70.310  81.458  1.00 38.87  ? 4092 ARG A CZ    1 
ATOM   18997 N  NH1   . ARG A 1 4092 ? 64.185  69.027  81.211  1.00 45.63  ? 4092 ARG A NH1   1 
ATOM   18998 N  NH2   . ARG A 1 4092 ? 63.730  70.701  82.705  1.00 33.07  ? 4092 ARG A NH2   1 
ATOM   18999 N  N     . TRP A 1 4093 ? 65.559  73.804  77.309  1.00 18.92  ? 4093 TRP A N     1 
ATOM   19000 C  CA    . TRP A 1 4093 ? 66.035  75.151  77.593  1.00 16.80  ? 4093 TRP A CA    1 
ATOM   19001 C  C     . TRP A 1 4093 ? 66.811  75.183  78.903  1.00 16.19  ? 4093 TRP A C     1 
ATOM   19002 O  O     . TRP A 1 4093 ? 66.405  74.573  79.898  1.00 18.71  ? 4093 TRP A O     1 
ATOM   19003 C  CB    . TRP A 1 4093 ? 64.873  76.146  77.657  1.00 13.43  ? 4093 TRP A CB    1 
ATOM   19004 C  CG    . TRP A 1 4093 ? 64.380  76.595  76.315  1.00 16.68  ? 4093 TRP A CG    1 
ATOM   19005 C  CD1   . TRP A 1 4093 ? 64.687  76.049  75.104  1.00 17.24  ? 4093 TRP A CD1   1 
ATOM   19006 C  CD2   . TRP A 1 4093 ? 63.503  77.696  76.049  1.00 17.84  ? 4093 TRP A CD2   1 
ATOM   19007 N  NE1   . TRP A 1 4093 ? 64.048  76.735  74.100  1.00 14.10  ? 4093 TRP A NE1   1 
ATOM   19008 C  CE2   . TRP A 1 4093 ? 63.316  77.752  74.654  1.00 11.80  ? 4093 TRP A CE2   1 
ATOM   19009 C  CE3   . TRP A 1 4093 ? 62.855  78.637  76.855  1.00 21.44  ? 4093 TRP A CE3   1 
ATOM   19010 C  CZ2   . TRP A 1 4093 ? 62.509  78.711  74.048  1.00 15.73  ? 4093 TRP A CZ2   1 
ATOM   19011 C  CZ3   . TRP A 1 4093 ? 62.054  79.588  76.251  1.00 19.21  ? 4093 TRP A CZ3   1 
ATOM   19012 C  CH2   . TRP A 1 4093 ? 61.888  79.619  74.861  1.00 16.42  ? 4093 TRP A CH2   1 
ATOM   19013 N  N     . VAL A 1 4094 ? 67.928  75.906  78.897  1.00 12.07  ? 4094 VAL A N     1 
ATOM   19014 C  CA    . VAL A 1 4094 ? 68.776  76.071  80.071  1.00 11.32  ? 4094 VAL A CA    1 
ATOM   19015 C  C     . VAL A 1 4094 ? 68.877  77.559  80.367  1.00 7.90   ? 4094 VAL A C     1 
ATOM   19016 O  O     . VAL A 1 4094 ? 69.057  78.361  79.447  1.00 6.17   ? 4094 VAL A O     1 
ATOM   19017 C  CB    . VAL A 1 4094 ? 70.179  75.468  79.856  1.00 10.54  ? 4094 VAL A CB    1 
ATOM   19018 C  CG1   . VAL A 1 4094 ? 71.080  75.764  81.043  1.00 7.48   ? 4094 VAL A CG1   1 
ATOM   19019 C  CG2   . VAL A 1 4094 ? 70.090  73.979  79.623  1.00 11.24  ? 4094 VAL A CG2   1 
ATOM   19020 N  N     . MET A 1 4095 ? 68.738  77.929  81.637  1.00 9.67   ? 4095 MET A N     1 
ATOM   19021 C  CA    . MET A 1 4095 ? 68.976  79.295  82.082  1.00 6.11   ? 4095 MET A CA    1 
ATOM   19022 C  C     . MET A 1 4095 ? 69.973  79.276  83.230  1.00 5.16   ? 4095 MET A C     1 
ATOM   19023 O  O     . MET A 1 4095 ? 69.823  78.498  84.178  1.00 6.17   ? 4095 MET A O     1 
ATOM   19024 C  CB    . MET A 1 4095 ? 67.680  79.986  82.515  1.00 7.21   ? 4095 MET A CB    1 
ATOM   19025 C  CG    . MET A 1 4095 ? 67.884  81.435  82.936  1.00 9.34   ? 4095 MET A CG    1 
ATOM   19026 S  SD    . MET A 1 4095 ? 66.371  82.282  83.425  1.00 23.04  ? 4095 MET A SD    1 
ATOM   19027 C  CE    . MET A 1 4095 ? 66.025  81.501  84.995  1.00 20.68  ? 4095 MET A CE    1 
ATOM   19028 N  N     . LEU A 1 4096 ? 70.994  80.121  83.129  1.00 5.21   ? 4096 LEU A N     1 
ATOM   19029 C  CA    . LEU A 1 4096 ? 72.026  80.254  84.148  1.00 4.30   ? 4096 LEU A CA    1 
ATOM   19030 C  C     . LEU A 1 4096 ? 72.011  81.689  84.650  1.00 5.30   ? 4096 LEU A C     1 
ATOM   19031 O  O     . LEU A 1 4096 ? 72.217  82.625  83.870  1.00 4.79   ? 4096 LEU A O     1 
ATOM   19032 C  CB    . LEU A 1 4096 ? 73.398  79.876  83.586  1.00 4.23   ? 4096 LEU A CB    1 
ATOM   19033 C  CG    . LEU A 1 4096 ? 73.444  78.518  82.878  1.00 5.93   ? 4096 LEU A CG    1 
ATOM   19034 C  CD1   . LEU A 1 4096 ? 74.838  78.212  82.360  1.00 5.15   ? 4096 LEU A CD1   1 
ATOM   19035 C  CD2   . LEU A 1 4096 ? 72.964  77.413  83.808  1.00 6.40   ? 4096 LEU A CD2   1 
ATOM   19036 N  N     . LYS A 1 4097 ? 71.768  81.858  85.945  1.00 6.05   ? 4097 LYS A N     1 
ATOM   19037 C  CA    . LYS A 1 4097 ? 71.587  83.174  86.536  1.00 5.78   ? 4097 LYS A CA    1 
ATOM   19038 C  C     . LYS A 1 4097 ? 72.871  83.657  87.196  1.00 5.95   ? 4097 LYS A C     1 
ATOM   19039 O  O     . LYS A 1 4097 ? 73.654  82.866  87.729  1.00 6.62   ? 4097 LYS A O     1 
ATOM   19040 C  CB    . LYS A 1 4097 ? 70.455  83.161  87.565  1.00 7.59   ? 4097 LYS A CB    1 
ATOM   19041 C  CG    . LYS A 1 4097 ? 69.246  82.344  87.153  1.00 10.12  ? 4097 LYS A CG    1 
ATOM   19042 C  CD    . LYS A 1 4097 ? 68.195  82.341  88.249  1.00 12.75  ? 4097 LYS A CD    1 
ATOM   19043 C  CE    . LYS A 1 4097 ? 67.475  81.006  88.319  1.00 16.31  ? 4097 LYS A CE    1 
ATOM   19044 N  NZ    . LYS A 1 4097 ? 66.540  80.940  89.474  1.00 24.89  ? 4097 LYS A NZ    1 
ATOM   19045 N  N     . ASN A 1 4098 ? 73.072  84.977  87.155  1.00 6.25   ? 4098 ASN A N     1 
ATOM   19046 C  CA    . ASN A 1 4098 ? 74.206  85.634  87.808  1.00 6.74   ? 4098 ASN A CA    1 
ATOM   19047 C  C     . ASN A 1 4098 ? 75.538  85.062  87.328  1.00 7.45   ? 4098 ASN A C     1 
ATOM   19048 O  O     . ASN A 1 4098 ? 76.435  84.775  88.123  1.00 9.12   ? 4098 ASN A O     1 
ATOM   19049 C  CB    . ASN A 1 4098 ? 74.090  85.545  89.331  1.00 5.94   ? 4098 ASN A CB    1 
ATOM   19050 C  CG    . ASN A 1 4098 ? 72.716  85.942  89.835  1.00 7.19   ? 4098 ASN A CG    1 
ATOM   19051 O  OD1   . ASN A 1 4098 ? 72.295  87.088  89.685  1.00 10.98  ? 4098 ASN A OD1   1 
ATOM   19052 N  ND2   . ASN A 1 4098 ? 72.008  84.992  90.435  1.00 6.43   ? 4098 ASN A ND2   1 
ATOM   19053 N  N     . VAL A 1 4099 ? 75.669  84.895  86.009  1.00 6.79   ? 4099 VAL A N     1 
ATOM   19054 C  CA    . VAL A 1 4099 ? 76.901  84.357  85.448  1.00 7.32   ? 4099 VAL A CA    1 
ATOM   19055 C  C     . VAL A 1 4099 ? 78.052  85.346  85.560  1.00 8.21   ? 4099 VAL A C     1 
ATOM   19056 O  O     . VAL A 1 4099 ? 79.215  84.955  85.417  1.00 8.95   ? 4099 VAL A O     1 
ATOM   19057 C  CB    . VAL A 1 4099 ? 76.686  83.936  83.982  1.00 5.80   ? 4099 VAL A CB    1 
ATOM   19058 C  CG1   . VAL A 1 4099 ? 75.524  82.963  83.879  1.00 4.79   ? 4099 VAL A CG1   1 
ATOM   19059 C  CG2   . VAL A 1 4099 ? 76.447  85.156  83.105  1.00 6.53   ? 4099 VAL A CG2   1 
ATOM   19060 N  N     . HIS A 1 4100 ? 77.761  86.622  85.825  1.00 7.37   ? 4100 HIS A N     1 
ATOM   19061 C  CA    . HIS A 1 4100 ? 78.812  87.615  86.009  1.00 8.32   ? 4100 HIS A CA    1 
ATOM   19062 C  C     . HIS A 1 4100 ? 79.660  87.346  87.245  1.00 9.38   ? 4100 HIS A C     1 
ATOM   19063 O  O     . HIS A 1 4100 ? 80.740  87.933  87.374  1.00 12.35  ? 4100 HIS A O     1 
ATOM   19064 C  CB    . HIS A 1 4100 ? 78.201  89.016  86.092  1.00 9.82   ? 4100 HIS A CB    1 
ATOM   19065 C  CG    . HIS A 1 4100 ? 77.342  89.231  87.300  1.00 9.38   ? 4100 HIS A CG    1 
ATOM   19066 N  ND1   . HIS A 1 4100 ? 76.051  88.756  87.389  1.00 9.53   ? 4100 HIS A ND1   1 
ATOM   19067 C  CD2   . HIS A 1 4100 ? 77.589  89.871  88.467  1.00 11.94  ? 4100 HIS A CD2   1 
ATOM   19068 C  CE1   . HIS A 1 4100 ? 75.540  89.094  88.559  1.00 10.59  ? 4100 HIS A CE1   1 
ATOM   19069 N  NE2   . HIS A 1 4100 ? 76.453  89.771  89.232  1.00 14.09  ? 4100 HIS A NE2   1 
ATOM   19070 N  N     . LEU A 1 4101 ? 79.202  86.482  88.149  1.00 8.69   ? 4101 LEU A N     1 
ATOM   19071 C  CA    . LEU A 1 4101 ? 79.975  86.126  89.330  1.00 10.45  ? 4101 LEU A CA    1 
ATOM   19072 C  C     . LEU A 1 4101 ? 81.053  85.087  89.043  1.00 14.15  ? 4101 LEU A C     1 
ATOM   19073 O  O     . LEU A 1 4101 ? 81.902  84.849  89.907  1.00 16.32  ? 4101 LEU A O     1 
ATOM   19074 C  CB    . LEU A 1 4101 ? 79.040  85.611  90.427  1.00 11.83  ? 4101 LEU A CB    1 
ATOM   19075 C  CG    . LEU A 1 4101 ? 77.954  86.577  90.908  1.00 12.30  ? 4101 LEU A CG    1 
ATOM   19076 C  CD1   . LEU A 1 4101 ? 77.061  85.912  91.943  1.00 10.96  ? 4101 LEU A CD1   1 
ATOM   19077 C  CD2   . LEU A 1 4101 ? 78.570  87.849  91.467  1.00 12.94  ? 4101 LEU A CD2   1 
ATOM   19078 N  N     . ALA A 1 4102 ? 81.039  84.466  87.864  1.00 11.60  ? 4102 ALA A N     1 
ATOM   19079 C  CA    . ALA A 1 4102 ? 82.030  83.461  87.476  1.00 11.41  ? 4102 ALA A CA    1 
ATOM   19080 C  C     . ALA A 1 4102 ? 82.544  83.755  86.070  1.00 15.17  ? 4102 ALA A C     1 
ATOM   19081 O  O     . ALA A 1 4102 ? 82.167  83.083  85.103  1.00 15.35  ? 4102 ALA A O     1 
ATOM   19082 C  CB    . ALA A 1 4102 ? 81.438  82.054  87.558  1.00 9.06   ? 4102 ALA A CB    1 
ATOM   19083 N  N     . PRO A 1 4103 ? 83.413  84.761  85.920  1.00 15.13  ? 4103 PRO A N     1 
ATOM   19084 C  CA    . PRO A 1 4103 ? 83.930  85.071  84.574  1.00 14.26  ? 4103 PRO A CA    1 
ATOM   19085 C  C     . PRO A 1 4103 ? 84.881  84.016  84.033  1.00 16.53  ? 4103 PRO A C     1 
ATOM   19086 O  O     . PRO A 1 4103 ? 84.834  83.697  82.835  1.00 18.28  ? 4103 PRO A O     1 
ATOM   19087 C  CB    . PRO A 1 4103 ? 84.634  86.421  84.773  1.00 15.77  ? 4103 PRO A CB    1 
ATOM   19088 C  CG    . PRO A 1 4103 ? 84.951  86.474  86.231  1.00 16.35  ? 4103 PRO A CG    1 
ATOM   19089 C  CD    . PRO A 1 4103 ? 83.837  85.755  86.921  1.00 12.67  ? 4103 PRO A CD    1 
ATOM   19090 N  N     . GLY A 1 4104 ? 85.762  83.479  84.882  1.00 13.81  ? 4104 GLY A N     1 
ATOM   19091 C  CA    . GLY A 1 4104 ? 86.675  82.443  84.427  1.00 14.04  ? 4104 GLY A CA    1 
ATOM   19092 C  C     . GLY A 1 4104 ? 85.947  81.218  83.913  1.00 17.51  ? 4104 GLY A C     1 
ATOM   19093 O  O     . GLY A 1 4104 ? 86.346  80.620  82.911  1.00 22.95  ? 4104 GLY A O     1 
ATOM   19094 N  N     . TRP A 1 4105 ? 84.869  80.826  84.593  1.00 11.60  ? 4105 TRP A N     1 
ATOM   19095 C  CA    . TRP A 1 4105 ? 84.023  79.758  84.079  1.00 10.81  ? 4105 TRP A CA    1 
ATOM   19096 C  C     . TRP A 1 4105 ? 83.254  80.206  82.843  1.00 12.14  ? 4105 TRP A C     1 
ATOM   19097 O  O     . TRP A 1 4105 ? 82.933  79.380  81.982  1.00 15.58  ? 4105 TRP A O     1 
ATOM   19098 C  CB    . TRP A 1 4105 ? 83.066  79.279  85.172  1.00 9.15   ? 4105 TRP A CB    1 
ATOM   19099 C  CG    . TRP A 1 4105 ? 81.915  78.471  84.662  1.00 8.95   ? 4105 TRP A CG    1 
ATOM   19100 C  CD1   . TRP A 1 4105 ? 81.901  77.130  84.413  1.00 9.06   ? 4105 TRP A CD1   1 
ATOM   19101 C  CD2   . TRP A 1 4105 ? 80.605  78.952  84.347  1.00 8.61   ? 4105 TRP A CD2   1 
ATOM   19102 N  NE1   . TRP A 1 4105 ? 80.663  76.747  83.956  1.00 9.06   ? 4105 TRP A NE1   1 
ATOM   19103 C  CE2   . TRP A 1 4105 ? 79.849  77.848  83.908  1.00 8.27   ? 4105 TRP A CE2   1 
ATOM   19104 C  CE3   . TRP A 1 4105 ? 79.997  80.210  84.392  1.00 9.29   ? 4105 TRP A CE3   1 
ATOM   19105 C  CZ2   . TRP A 1 4105 ? 78.519  77.964  83.516  1.00 10.24  ? 4105 TRP A CZ2   1 
ATOM   19106 C  CZ3   . TRP A 1 4105 ? 78.677  80.323  84.003  1.00 10.82  ? 4105 TRP A CZ3   1 
ATOM   19107 C  CH2   . TRP A 1 4105 ? 77.953  79.207  83.571  1.00 10.28  ? 4105 TRP A CH2   1 
ATOM   19108 N  N     . LEU A 1 4106 ? 82.958  81.504  82.733  1.00 12.54  ? 4106 LEU A N     1 
ATOM   19109 C  CA    . LEU A 1 4106 ? 82.239  82.009  81.567  1.00 12.67  ? 4106 LEU A CA    1 
ATOM   19110 C  C     . LEU A 1 4106 ? 83.066  81.865  80.295  1.00 17.26  ? 4106 LEU A C     1 
ATOM   19111 O  O     . LEU A 1 4106 ? 82.524  81.565  79.224  1.00 22.14  ? 4106 LEU A O     1 
ATOM   19112 C  CB    . LEU A 1 4106 ? 81.841  83.469  81.784  1.00 12.49  ? 4106 LEU A CB    1 
ATOM   19113 C  CG    . LEU A 1 4106 ? 80.433  83.721  82.325  1.00 8.95   ? 4106 LEU A CG    1 
ATOM   19114 C  CD1   . LEU A 1 4106 ? 80.126  85.208  82.333  1.00 7.32   ? 4106 LEU A CD1   1 
ATOM   19115 C  CD2   . LEU A 1 4106 ? 79.397  82.957  81.516  1.00 7.68   ? 4106 LEU A CD2   1 
ATOM   19116 N  N     . MET A 1 4107 ? 84.379  82.094  80.384  1.00 17.82  ? 4107 MET A N     1 
ATOM   19117 C  CA    . MET A 1 4107 ? 85.233  81.920  79.209  1.00 20.74  ? 4107 MET A CA    1 
ATOM   19118 C  C     . MET A 1 4107 ? 85.220  80.471  78.728  1.00 20.68  ? 4107 MET A C     1 
ATOM   19119 O  O     . MET A 1 4107 ? 85.110  80.198  77.523  1.00 26.47  ? 4107 MET A O     1 
ATOM   19120 C  CB    . MET A 1 4107 ? 86.661  82.370  79.521  1.00 24.61  ? 4107 MET A CB    1 
ATOM   19121 C  CG    . MET A 1 4107 ? 86.760  83.699  80.247  1.00 26.62  ? 4107 MET A CG    1 
ATOM   19122 S  SD    . MET A 1 4107 ? 88.354  83.935  81.056  1.00 58.78  ? 4107 MET A SD    1 
ATOM   19123 C  CE    . MET A 1 4107 ? 87.928  85.142  82.309  1.00 28.32  ? 4107 MET A CE    1 
ATOM   19124 N  N     . GLN A 1 4108 ? 85.324  79.524  79.662  1.00 19.17  ? 4108 GLN A N     1 
ATOM   19125 C  CA    . GLN A 1 4108 ? 85.281  78.115  79.286  1.00 22.79  ? 4108 GLN A CA    1 
ATOM   19126 C  C     . GLN A 1 4108 ? 83.902  77.727  78.771  1.00 23.13  ? 4108 GLN A C     1 
ATOM   19127 O  O     . GLN A 1 4108 ? 83.779  76.860  77.901  1.00 21.72  ? 4108 GLN A O     1 
ATOM   19128 C  CB    . GLN A 1 4108 ? 85.686  77.242  80.475  1.00 24.58  ? 4108 GLN A CB    1 
ATOM   19129 C  CG    . GLN A 1 4108 ? 86.966  77.673  81.208  1.00 28.97  ? 4108 GLN A CG    1 
ATOM   19130 C  CD    . GLN A 1 4108 ? 88.164  77.956  80.298  1.00 44.54  ? 4108 GLN A CD    1 
ATOM   19131 O  OE1   . GLN A 1 4108 ? 88.189  77.583  79.124  1.00 38.63  ? 4108 GLN A OE1   1 
ATOM   19132 N  NE2   . GLN A 1 4108 ? 89.167  78.626  80.853  1.00 46.92  ? 4108 GLN A NE2   1 
ATOM   19133 N  N     . LEU A 1 4109 ? 82.852  78.369  79.288  1.00 22.50  ? 4109 LEU A N     1 
ATOM   19134 C  CA    . LEU A 1 4109 ? 81.513  78.142  78.755  1.00 20.04  ? 4109 LEU A CA    1 
ATOM   19135 C  C     . LEU A 1 4109 ? 81.412  78.612  77.310  1.00 17.68  ? 4109 LEU A C     1 
ATOM   19136 O  O     . LEU A 1 4109 ? 80.803  77.940  76.471  1.00 16.74  ? 4109 LEU A O     1 
ATOM   19137 C  CB    . LEU A 1 4109 ? 80.473  78.848  79.623  1.00 17.37  ? 4109 LEU A CB    1 
ATOM   19138 C  CG    . LEU A 1 4109 ? 79.029  78.753  79.127  1.00 17.47  ? 4109 LEU A CG    1 
ATOM   19139 C  CD1   . LEU A 1 4109 ? 78.493  77.348  79.327  1.00 12.78  ? 4109 LEU A CD1   1 
ATOM   19140 C  CD2   . LEU A 1 4109 ? 78.146  79.773  79.827  1.00 13.10  ? 4109 LEU A CD2   1 
ATOM   19141 N  N     . GLU A 1 4110 ? 82.000  79.770  77.003  1.00 17.13  ? 4110 GLU A N     1 
ATOM   19142 C  CA    . GLU A 1 4110 ? 82.025  80.247  75.623  1.00 19.55  ? 4110 GLU A CA    1 
ATOM   19143 C  C     . GLU A 1 4110 ? 82.777  79.276  74.722  1.00 20.54  ? 4110 GLU A C     1 
ATOM   19144 O  O     . GLU A 1 4110 ? 82.321  78.959  73.615  1.00 21.55  ? 4110 GLU A O     1 
ATOM   19145 C  CB    . GLU A 1 4110 ? 82.655  81.640  75.562  1.00 17.29  ? 4110 GLU A CB    1 
ATOM   19146 C  CG    . GLU A 1 4110 ? 82.498  82.352  74.224  1.00 21.93  ? 4110 GLU A CG    1 
ATOM   19147 C  CD    . GLU A 1 4110 ? 83.560  81.954  73.214  1.00 25.94  ? 4110 GLU A CD    1 
ATOM   19148 O  OE1   . GLU A 1 4110 ? 84.759  81.994  73.562  1.00 29.05  ? 4110 GLU A OE1   1 
ATOM   19149 O  OE2   . GLU A 1 4110 ? 83.196  81.597  72.074  1.00 22.01  ? 4110 GLU A OE2   1 
ATOM   19150 N  N     . LYS A 1 4111 ? 83.931  78.789  75.185  1.00 20.09  ? 4111 LYS A N     1 
ATOM   19151 C  CA    . LYS A 1 4111 ? 84.694  77.829  74.390  1.00 22.87  ? 4111 LYS A CA    1 
ATOM   19152 C  C     . LYS A 1 4111 ? 83.913  76.537  74.175  1.00 18.39  ? 4111 LYS A C     1 
ATOM   19153 O  O     . LYS A 1 4111 ? 83.963  75.946  73.090  1.00 21.44  ? 4111 LYS A O     1 
ATOM   19154 C  CB    . LYS A 1 4111 ? 86.043  77.546  75.051  1.00 24.80  ? 4111 LYS A CB    1 
ATOM   19155 C  CG    . LYS A 1 4111 ? 87.076  78.636  74.816  1.00 24.78  ? 4111 LYS A CG    1 
ATOM   19156 C  CD    . LYS A 1 4111 ? 87.990  78.816  76.014  1.00 32.00  ? 4111 LYS A CD    1 
ATOM   19157 C  CE    . LYS A 1 4111 ? 89.200  79.662  75.653  1.00 31.10  ? 4111 LYS A CE    1 
ATOM   19158 N  NZ    . LYS A 1 4111 ? 88.808  80.987  75.099  1.00 29.86  ? 4111 LYS A NZ    1 
ATOM   19159 N  N     . LYS A 1 4112 ? 83.191  76.079  75.200  1.00 19.70  ? 4112 LYS A N     1 
ATOM   19160 C  CA    . LYS A 1 4112 ? 82.352  74.893  75.058  1.00 20.59  ? 4112 LYS A CA    1 
ATOM   19161 C  C     . LYS A 1 4112 ? 81.225  75.124  74.058  1.00 20.30  ? 4112 LYS A C     1 
ATOM   19162 O  O     . LYS A 1 4112 ? 80.927  74.250  73.236  1.00 23.50  ? 4112 LYS A O     1 
ATOM   19163 C  CB    . LYS A 1 4112 ? 81.785  74.493  76.420  1.00 20.30  ? 4112 LYS A CB    1 
ATOM   19164 C  CG    . LYS A 1 4112 ? 80.698  73.434  76.366  1.00 17.20  ? 4112 LYS A CG    1 
ATOM   19165 C  CD    . LYS A 1 4112 ? 80.146  73.149  77.752  1.00 19.97  ? 4112 LYS A CD    1 
ATOM   19166 C  CE    . LYS A 1 4112 ? 79.097  72.051  77.718  1.00 23.43  ? 4112 LYS A CE    1 
ATOM   19167 N  NZ    . LYS A 1 4112 ? 78.631  71.689  79.084  1.00 21.05  ? 4112 LYS A NZ    1 
ATOM   19168 N  N     . LEU A 1 4113 ? 80.587  76.295  74.117  1.00 23.43  ? 4113 LEU A N     1 
ATOM   19169 C  CA    . LEU A 1 4113 ? 79.479  76.590  73.215  1.00 19.84  ? 4113 LEU A CA    1 
ATOM   19170 C  C     . LEU A 1 4113 ? 79.939  76.713  71.770  1.00 25.97  ? 4113 LEU A C     1 
ATOM   19171 O  O     . LEU A 1 4113 ? 79.181  76.375  70.853  1.00 29.30  ? 4113 LEU A O     1 
ATOM   19172 C  CB    . LEU A 1 4113 ? 78.769  77.872  73.647  1.00 17.23  ? 4113 LEU A CB    1 
ATOM   19173 C  CG    . LEU A 1 4113 ? 77.999  77.842  74.967  1.00 19.43  ? 4113 LEU A CG    1 
ATOM   19174 C  CD1   . LEU A 1 4113 ? 77.600  79.252  75.372  1.00 16.65  ? 4113 LEU A CD1   1 
ATOM   19175 C  CD2   . LEU A 1 4113 ? 76.779  76.944  74.854  1.00 19.56  ? 4113 LEU A CD2   1 
ATOM   19176 N  N     . HIS A 1 4114 ? 81.158  77.210  71.543  1.00 25.70  ? 4114 HIS A N     1 
ATOM   19177 C  CA    . HIS A 1 4114 ? 81.627  77.395  70.173  1.00 23.31  ? 4114 HIS A CA    1 
ATOM   19178 C  C     . HIS A 1 4114 ? 81.690  76.072  69.417  1.00 28.83  ? 4114 HIS A C     1 
ATOM   19179 O  O     . HIS A 1 4114 ? 81.261  75.990  68.260  1.00 32.94  ? 4114 HIS A O     1 
ATOM   19180 C  CB    . HIS A 1 4114 ? 82.994  78.078  70.169  1.00 22.94  ? 4114 HIS A CB    1 
ATOM   19181 C  CG    . HIS A 1 4114 ? 83.515  78.368  68.796  1.00 27.76  ? 4114 HIS A CG    1 
ATOM   19182 N  ND1   . HIS A 1 4114 ? 83.161  79.497  68.090  1.00 26.44  ? 4114 HIS A ND1   1 
ATOM   19183 C  CD2   . HIS A 1 4114 ? 84.359  77.674  67.997  1.00 23.77  ? 4114 HIS A CD2   1 
ATOM   19184 C  CE1   . HIS A 1 4114 ? 83.766  79.487  66.916  1.00 24.23  ? 4114 HIS A CE1   1 
ATOM   19185 N  NE2   . HIS A 1 4114 ? 84.500  78.392  66.835  1.00 22.88  ? 4114 HIS A NE2   1 
ATOM   19186 N  N     . SER A 1 4115 ? 82.218  75.025  70.051  1.00 28.88  ? 4115 SER A N     1 
ATOM   19187 C  CA    . SER A 1 4115 ? 82.343  73.710  69.421  1.00 32.16  ? 4115 SER A CA    1 
ATOM   19188 C  C     . SER A 1 4115 ? 81.163  72.849  69.864  1.00 36.18  ? 4115 SER A C     1 
ATOM   19189 O  O     . SER A 1 4115 ? 81.274  71.988  70.737  1.00 42.54  ? 4115 SER A O     1 
ATOM   19190 C  CB    . SER A 1 4115 ? 83.682  73.071  69.775  1.00 36.02  ? 4115 SER A CB    1 
ATOM   19191 O  OG    . SER A 1 4115 ? 83.834  72.950  71.179  1.00 33.50  ? 4115 SER A OG    1 
ATOM   19192 N  N     . LEU A 1 4116 ? 80.014  73.090  69.234  1.00 36.50  ? 4116 LEU A N     1 
ATOM   19193 C  CA    . LEU A 1 4116 ? 78.773  72.438  69.630  1.00 37.12  ? 4116 LEU A CA    1 
ATOM   19194 C  C     . LEU A 1 4116 ? 77.737  72.615  68.530  1.00 40.14  ? 4116 LEU A C     1 
ATOM   19195 O  O     . LEU A 1 4116 ? 77.648  73.685  67.925  1.00 45.18  ? 4116 LEU A O     1 
ATOM   19196 C  CB    . LEU A 1 4116 ? 78.253  73.021  70.950  1.00 37.48  ? 4116 LEU A CB    1 
ATOM   19197 C  CG    . LEU A 1 4116 ? 76.989  72.424  71.564  1.00 40.04  ? 4116 LEU A CG    1 
ATOM   19198 C  CD1   . LEU A 1 4116 ? 77.193  70.963  71.928  1.00 39.19  ? 4116 LEU A CD1   1 
ATOM   19199 C  CD2   . LEU A 1 4116 ? 76.598  73.238  72.782  1.00 31.92  ? 4116 LEU A CD2   1 
ATOM   19200 N  N     . GLN A 1 4117 ? 76.964  71.559  68.275  1.00 42.27  ? 4117 GLN A N     1 
ATOM   19201 C  CA    . GLN A 1 4117 ? 75.865  71.580  67.308  1.00 42.08  ? 4117 GLN A CA    1 
ATOM   19202 C  C     . GLN A 1 4117 ? 74.611  71.070  68.006  1.00 35.82  ? 4117 GLN A C     1 
ATOM   19203 O  O     . GLN A 1 4117 ? 74.239  69.897  67.868  1.00 39.59  ? 4117 GLN A O     1 
ATOM   19204 C  CB    . GLN A 1 4117 ? 76.187  70.745  66.066  1.00 45.70  ? 4117 GLN A CB    1 
ATOM   19205 C  CG    . GLN A 1 4117 ? 77.206  71.364  65.113  1.00 50.50  ? 4117 GLN A CG    1 
ATOM   19206 C  CD    . GLN A 1 4117 ? 78.618  71.372  65.666  1.00 59.17  ? 4117 GLN A CD    1 
ATOM   19207 O  OE1   . GLN A 1 4117 ? 79.227  72.430  65.828  1.00 56.82  ? 4117 GLN A OE1   1 
ATOM   19208 N  NE2   . GLN A 1 4117 ? 79.145  70.190  65.961  1.00 51.51  ? 4117 GLN A NE2   1 
ATOM   19209 N  N     . PRO A 1 4118 ? 73.933  71.926  68.760  1.00 35.39  ? 4118 PRO A N     1 
ATOM   19210 C  CA    . PRO A 1 4118 ? 72.794  71.487  69.572  1.00 28.10  ? 4118 PRO A CA    1 
ATOM   19211 C  C     . PRO A 1 4118 ? 71.533  71.313  68.731  1.00 23.43  ? 4118 PRO A C     1 
ATOM   19212 O  O     . PRO A 1 4118 ? 71.492  71.625  67.543  1.00 26.12  ? 4118 PRO A O     1 
ATOM   19213 C  CB    . PRO A 1 4118 ? 72.633  72.622  70.584  1.00 23.78  ? 4118 PRO A CB    1 
ATOM   19214 C  CG    . PRO A 1 4118 ? 73.158  73.824  69.885  1.00 24.89  ? 4118 PRO A CG    1 
ATOM   19215 C  CD    . PRO A 1 4118 ? 74.226  73.359  68.936  1.00 30.96  ? 4118 PRO A CD    1 
ATOM   19216 N  N     . HIS A 1 4119 ? 70.494  70.794  69.383  1.00 22.99  ? 4119 HIS A N     1 
ATOM   19217 C  CA    . HIS A 1 4119 ? 69.187  70.666  68.753  1.00 25.70  ? 4119 HIS A CA    1 
ATOM   19218 C  C     . HIS A 1 4119 ? 68.648  72.055  68.427  1.00 26.79  ? 4119 HIS A C     1 
ATOM   19219 O  O     . HIS A 1 4119 ? 68.881  73.017  69.165  1.00 27.06  ? 4119 HIS A O     1 
ATOM   19220 C  CB    . HIS A 1 4119 ? 68.235  69.913  69.690  1.00 24.01  ? 4119 HIS A CB    1 
ATOM   19221 C  CG    . HIS A 1 4119 ? 66.898  69.590  69.092  1.00 27.38  ? 4119 HIS A CG    1 
ATOM   19222 N  ND1   . HIS A 1 4119 ? 65.899  68.970  69.812  1.00 33.54  ? 4119 HIS A ND1   1 
ATOM   19223 C  CD2   . HIS A 1 4119 ? 66.410  69.755  67.840  1.00 35.85  ? 4119 HIS A CD2   1 
ATOM   19224 C  CE1   . HIS A 1 4119 ? 64.843  68.795  69.038  1.00 30.88  ? 4119 HIS A CE1   1 
ATOM   19225 N  NE2   . HIS A 1 4119 ? 65.127  69.263  67.836  1.00 42.43  ? 4119 HIS A NE2   1 
ATOM   19226 N  N     . ALA A 1 4120 ? 67.932  72.161  67.305  1.00 25.23  ? 4120 ALA A N     1 
ATOM   19227 C  CA    . ALA A 1 4120 ? 67.458  73.455  66.824  1.00 23.51  ? 4120 ALA A CA    1 
ATOM   19228 C  C     . ALA A 1 4120 ? 66.579  74.180  67.836  1.00 26.03  ? 4120 ALA A C     1 
ATOM   19229 O  O     . ALA A 1 4120 ? 66.507  75.413  67.803  1.00 27.34  ? 4120 ALA A O     1 
ATOM   19230 C  CB    . ALA A 1 4120 ? 66.695  73.278  65.511  1.00 22.13  ? 4120 ALA A CB    1 
ATOM   19231 N  N     . CYS A 1 4121 ? 65.912  73.453  68.732  1.00 25.75  ? 4121 CYS A N     1 
ATOM   19232 C  CA    . CYS A 1 4121 ? 65.061  74.075  69.737  1.00 22.65  ? 4121 CYS A CA    1 
ATOM   19233 C  C     . CYS A 1 4121 ? 65.801  74.415  71.025  1.00 19.67  ? 4121 CYS A C     1 
ATOM   19234 O  O     . CYS A 1 4121 ? 65.215  75.057  71.903  1.00 19.69  ? 4121 CYS A O     1 
ATOM   19235 C  CB    . CYS A 1 4121 ? 63.872  73.163  70.060  1.00 25.96  ? 4121 CYS A CB    1 
ATOM   19236 S  SG    . CYS A 1 4121 ? 62.726  72.917  68.685  1.00 56.84  ? 4121 CYS A SG    1 
ATOM   19237 N  N     . PHE A 1 4122 ? 67.061  74.007  71.160  1.00 17.95  ? 4122 PHE A N     1 
ATOM   19238 C  CA    . PHE A 1 4122 ? 67.822  74.304  72.366  1.00 16.25  ? 4122 PHE A CA    1 
ATOM   19239 C  C     . PHE A 1 4122 ? 68.074  75.801  72.493  1.00 15.24  ? 4122 PHE A C     1 
ATOM   19240 O  O     . PHE A 1 4122 ? 68.438  76.472  71.523  1.00 15.09  ? 4122 PHE A O     1 
ATOM   19241 C  CB    . PHE A 1 4122 ? 69.152  73.550  72.355  1.00 13.10  ? 4122 PHE A CB    1 
ATOM   19242 C  CG    . PHE A 1 4122 ? 70.172  74.099  73.315  1.00 13.08  ? 4122 PHE A CG    1 
ATOM   19243 C  CD1   . PHE A 1 4122 ? 70.104  73.798  74.664  1.00 11.51  ? 4122 PHE A CD1   1 
ATOM   19244 C  CD2   . PHE A 1 4122 ? 71.200  74.913  72.867  1.00 13.01  ? 4122 PHE A CD2   1 
ATOM   19245 C  CE1   . PHE A 1 4122 ? 71.038  74.300  75.549  1.00 9.18   ? 4122 PHE A CE1   1 
ATOM   19246 C  CE2   . PHE A 1 4122 ? 72.136  75.418  73.748  1.00 9.52   ? 4122 PHE A CE2   1 
ATOM   19247 C  CZ    . PHE A 1 4122 ? 72.055  75.111  75.090  1.00 9.63   ? 4122 PHE A CZ    1 
ATOM   19248 N  N     . ARG A 1 4123 ? 67.878  76.325  73.701  1.00 12.14  ? 4123 ARG A N     1 
ATOM   19249 C  CA    . ARG A 1 4123 ? 68.168  77.721  73.997  1.00 9.64   ? 4123 ARG A CA    1 
ATOM   19250 C  C     . ARG A 1 4123 ? 68.863  77.821  75.345  1.00 8.05   ? 4123 ARG A C     1 
ATOM   19251 O  O     . ARG A 1 4123 ? 68.394  77.248  76.335  1.00 9.55   ? 4123 ARG A O     1 
ATOM   19252 C  CB    . ARG A 1 4123 ? 66.893  78.573  73.995  1.00 10.06  ? 4123 ARG A CB    1 
ATOM   19253 C  CG    . ARG A 1 4123 ? 66.259  78.752  72.625  1.00 13.09  ? 4123 ARG A CG    1 
ATOM   19254 C  CD    . ARG A 1 4123 ? 67.180  79.528  71.692  1.00 14.20  ? 4123 ARG A CD    1 
ATOM   19255 N  NE    . ARG A 1 4123 ? 66.614  79.687  70.358  1.00 19.87  ? 4123 ARG A NE    1 
ATOM   19256 C  CZ    . ARG A 1 4123 ? 66.544  78.725  69.448  1.00 18.78  ? 4123 ARG A CZ    1 
ATOM   19257 N  NH1   . ARG A 1 4123 ? 67.015  77.512  69.686  1.00 17.62  ? 4123 ARG A NH1   1 
ATOM   19258 N  NH2   . ARG A 1 4123 ? 65.993  78.989  68.267  1.00 20.33  ? 4123 ARG A NH2   1 
ATOM   19259 N  N     . LEU A 1 4124 ? 69.968  78.560  75.375  1.00 7.39   ? 4124 LEU A N     1 
ATOM   19260 C  CA    . LEU A 1 4124 ? 70.706  78.851  76.596  1.00 6.54   ? 4124 LEU A CA    1 
ATOM   19261 C  C     . LEU A 1 4124 ? 70.570  80.336  76.901  1.00 5.14   ? 4124 LEU A C     1 
ATOM   19262 O  O     . LEU A 1 4124 ? 70.894  81.178  76.059  1.00 7.15   ? 4124 LEU A O     1 
ATOM   19263 C  CB    . LEU A 1 4124 ? 72.178  78.465  76.457  1.00 4.83   ? 4124 LEU A CB    1 
ATOM   19264 C  CG    . LEU A 1 4124 ? 73.083  78.866  77.625  1.00 6.16   ? 4124 LEU A CG    1 
ATOM   19265 C  CD1   . LEU A 1 4124 ? 72.739  78.079  78.873  1.00 5.81   ? 4124 LEU A CD1   1 
ATOM   19266 C  CD2   . LEU A 1 4124 ? 74.545  78.685  77.263  1.00 6.79   ? 4124 LEU A CD2   1 
ATOM   19267 N  N     . PHE A 1 4125 ? 70.091  80.650  78.099  1.00 3.74   ? 4125 PHE A N     1 
ATOM   19268 C  CA    . PHE A 1 4125 ? 69.927  82.018  78.569  1.00 5.65   ? 4125 PHE A CA    1 
ATOM   19269 C  C     . PHE A 1 4125 ? 70.951  82.263  79.666  1.00 4.34   ? 4125 PHE A C     1 
ATOM   19270 O  O     . PHE A 1 4125 ? 71.109  81.431  80.565  1.00 4.43   ? 4125 PHE A O     1 
ATOM   19271 C  CB    . PHE A 1 4125 ? 68.511  82.255  79.093  1.00 5.02   ? 4125 PHE A CB    1 
ATOM   19272 C  CG    . PHE A 1 4125 ? 67.441  82.077  78.056  1.00 6.45   ? 4125 PHE A CG    1 
ATOM   19273 C  CD1   . PHE A 1 4125 ? 66.913  80.823  77.794  1.00 5.53   ? 4125 PHE A CD1   1 
ATOM   19274 C  CD2   . PHE A 1 4125 ? 66.959  83.163  77.345  1.00 5.86   ? 4125 PHE A CD2   1 
ATOM   19275 C  CE1   . PHE A 1 4125 ? 65.929  80.656  76.841  1.00 6.97   ? 4125 PHE A CE1   1 
ATOM   19276 C  CE2   . PHE A 1 4125 ? 65.973  83.002  76.391  1.00 7.01   ? 4125 PHE A CE2   1 
ATOM   19277 C  CZ    . PHE A 1 4125 ? 65.458  81.747  76.139  1.00 9.40   ? 4125 PHE A CZ    1 
ATOM   19278 N  N     . LEU A 1 4126 ? 71.659  83.382  79.580  1.00 4.81   ? 4126 LEU A N     1 
ATOM   19279 C  CA    . LEU A 1 4126 ? 72.634  83.770  80.590  1.00 4.98   ? 4126 LEU A CA    1 
ATOM   19280 C  C     . LEU A 1 4126 ? 72.212  85.107  81.179  1.00 6.26   ? 4126 LEU A C     1 
ATOM   19281 O  O     . LEU A 1 4126 ? 72.363  86.149  80.533  1.00 8.55   ? 4126 LEU A O     1 
ATOM   19282 C  CB    . LEU A 1 4126 ? 74.041  83.851  79.998  1.00 5.11   ? 4126 LEU A CB    1 
ATOM   19283 C  CG    . LEU A 1 4126 ? 74.553  82.573  79.326  1.00 5.35   ? 4126 LEU A CG    1 
ATOM   19284 C  CD1   . LEU A 1 4126 ? 75.999  82.730  78.889  1.00 3.84   ? 4126 LEU A CD1   1 
ATOM   19285 C  CD2   . LEU A 1 4126 ? 74.397  81.375  80.250  1.00 3.72   ? 4126 LEU A CD2   1 
ATOM   19286 N  N     . THR A 1 4127 ? 71.671  85.071  82.392  1.00 6.90   ? 4127 THR A N     1 
ATOM   19287 C  CA    . THR A 1 4127 ? 71.243  86.269  83.100  1.00 5.77   ? 4127 THR A CA    1 
ATOM   19288 C  C     . THR A 1 4127 ? 72.431  86.836  83.863  1.00 6.48   ? 4127 THR A C     1 
ATOM   19289 O  O     . THR A 1 4127 ? 73.137  86.097  84.557  1.00 8.60   ? 4127 THR A O     1 
ATOM   19290 C  CB    . THR A 1 4127 ? 70.093  85.952  84.058  1.00 9.20   ? 4127 THR A CB    1 
ATOM   19291 O  OG1   . THR A 1 4127 ? 68.895  85.716  83.308  1.00 12.44  ? 4127 THR A OG1   1 
ATOM   19292 C  CG2   . THR A 1 4127 ? 69.860  87.103  85.021  1.00 13.35  ? 4127 THR A CG2   1 
ATOM   19293 N  N     . MET A 1 4128 ? 72.658  88.141  83.729  1.00 8.25   ? 4128 MET A N     1 
ATOM   19294 C  CA    . MET A 1 4128 ? 73.805  88.758  84.374  1.00 8.54   ? 4128 MET A CA    1 
ATOM   19295 C  C     . MET A 1 4128 ? 73.531  90.235  84.601  1.00 10.07  ? 4128 MET A C     1 
ATOM   19296 O  O     . MET A 1 4128 ? 72.662  90.836  83.964  1.00 9.86   ? 4128 MET A O     1 
ATOM   19297 C  CB    . MET A 1 4128 ? 75.079  88.581  83.538  1.00 9.99   ? 4128 MET A CB    1 
ATOM   19298 C  CG    . MET A 1 4128 ? 75.101  89.419  82.268  1.00 12.76  ? 4128 MET A CG    1 
ATOM   19299 S  SD    . MET A 1 4128 ? 76.413  88.952  81.124  1.00 32.05  ? 4128 MET A SD    1 
ATOM   19300 C  CE    . MET A 1 4128 ? 75.674  87.533  80.322  1.00 8.92   ? 4128 MET A CE    1 
ATOM   19301 N  N     . GLU A 1 4129 ? 74.279  90.809  85.536  1.00 11.85  ? 4129 GLU A N     1 
ATOM   19302 C  CA    . GLU A 1 4129 ? 74.321  92.250  85.688  1.00 13.21  ? 4129 GLU A CA    1 
ATOM   19303 C  C     . GLU A 1 4129 ? 75.252  92.850  84.639  1.00 12.81  ? 4129 GLU A C     1 
ATOM   19304 O  O     . GLU A 1 4129 ? 76.108  92.168  84.069  1.00 17.84  ? 4129 GLU A O     1 
ATOM   19305 C  CB    . GLU A 1 4129 ? 74.792  92.633  87.091  1.00 17.63  ? 4129 GLU A CB    1 
ATOM   19306 C  CG    . GLU A 1 4129 ? 73.857  92.199  88.206  1.00 20.62  ? 4129 GLU A CG    1 
ATOM   19307 C  CD    . GLU A 1 4129 ? 74.210  92.831  89.538  1.00 34.61  ? 4129 GLU A CD    1 
ATOM   19308 O  OE1   . GLU A 1 4129 ? 75.394  93.173  89.740  1.00 32.37  ? 4129 GLU A OE1   1 
ATOM   19309 O  OE2   . GLU A 1 4129 ? 73.305  92.984  90.385  1.00 33.86  ? 4129 GLU A OE2   1 
ATOM   19310 N  N     . ILE A 1 4130 ? 75.077  94.143  84.382  1.00 12.53  ? 4130 ILE A N     1 
ATOM   19311 C  CA    . ILE A 1 4130 ? 75.969  94.839  83.462  1.00 16.69  ? 4130 ILE A CA    1 
ATOM   19312 C  C     . ILE A 1 4130 ? 77.291  95.051  84.185  1.00 18.85  ? 4130 ILE A C     1 
ATOM   19313 O  O     . ILE A 1 4130 ? 77.437  95.983  84.983  1.00 21.79  ? 4130 ILE A O     1 
ATOM   19314 C  CB    . ILE A 1 4130 ? 75.360  96.166  82.975  1.00 14.56  ? 4130 ILE A CB    1 
ATOM   19315 C  CG1   . ILE A 1 4130 ? 74.054  95.899  82.222  1.00 10.03  ? 4130 ILE A CG1   1 
ATOM   19316 C  CG2   . ILE A 1 4130 ? 76.345  96.913  82.088  1.00 12.44  ? 4130 ILE A CG2   1 
ATOM   19317 C  CD1   . ILE A 1 4130 ? 73.445  97.128  81.587  1.00 12.38  ? 4130 ILE A CD1   1 
ATOM   19318 N  N     . ASN A 1 4131 ? 78.260  94.178  83.913  1.00 16.78  ? 4131 ASN A N     1 
ATOM   19319 C  CA    . ASN A 1 4131 ? 79.492  94.112  84.681  1.00 15.33  ? 4131 ASN A CA    1 
ATOM   19320 C  C     . ASN A 1 4131 ? 80.682  94.060  83.730  1.00 16.17  ? 4131 ASN A C     1 
ATOM   19321 O  O     . ASN A 1 4131 ? 80.677  93.267  82.773  1.00 19.56  ? 4131 ASN A O     1 
ATOM   19322 C  CB    . ASN A 1 4131 ? 79.483  92.882  85.601  1.00 17.92  ? 4131 ASN A CB    1 
ATOM   19323 C  CG    . ASN A 1 4131 ? 80.439  93.015  86.768  1.00 24.51  ? 4131 ASN A CG    1 
ATOM   19324 O  OD1   . ASN A 1 4131 ? 81.634  93.245  86.587  1.00 31.68  ? 4131 ASN A OD1   1 
ATOM   19325 N  ND2   . ASN A 1 4131 ? 79.915  92.868  87.979  1.00 20.77  ? 4131 ASN A ND2   1 
ATOM   19326 N  N     . PRO A 1 4132 ? 81.711  94.882  83.949  1.00 15.25  ? 4132 PRO A N     1 
ATOM   19327 C  CA    . PRO A 1 4132 ? 82.902  94.814  83.085  1.00 14.83  ? 4132 PRO A CA    1 
ATOM   19328 C  C     . PRO A 1 4132 ? 83.654  93.498  83.183  1.00 20.33  ? 4132 PRO A C     1 
ATOM   19329 O  O     . PRO A 1 4132 ? 84.447  93.190  82.285  1.00 20.43  ? 4132 PRO A O     1 
ATOM   19330 C  CB    . PRO A 1 4132 ? 83.761  95.988  83.577  1.00 14.77  ? 4132 PRO A CB    1 
ATOM   19331 C  CG    . PRO A 1 4132 ? 83.266  96.276  84.958  1.00 15.51  ? 4132 PRO A CG    1 
ATOM   19332 C  CD    . PRO A 1 4132 ? 81.804  95.965  84.941  1.00 15.39  ? 4132 PRO A CD    1 
ATOM   19333 N  N     . LYS A 1 4133 ? 83.435  92.712  84.240  1.00 23.21  ? 4133 LYS A N     1 
ATOM   19334 C  CA    . LYS A 1 4133 ? 84.148  91.449  84.392  1.00 22.87  ? 4133 LYS A CA    1 
ATOM   19335 C  C     . LYS A 1 4133 ? 83.648  90.376  83.433  1.00 23.50  ? 4133 LYS A C     1 
ATOM   19336 O  O     . LYS A 1 4133 ? 84.301  89.337  83.295  1.00 27.24  ? 4133 LYS A O     1 
ATOM   19337 C  CB    . LYS A 1 4133 ? 84.032  90.950  85.833  1.00 28.95  ? 4133 LYS A CB    1 
ATOM   19338 C  CG    . LYS A 1 4133 ? 84.611  91.903  86.865  1.00 33.78  ? 4133 LYS A CG    1 
ATOM   19339 C  CD    . LYS A 1 4133 ? 86.115  92.042  86.703  1.00 40.20  ? 4133 LYS A CD    1 
ATOM   19340 C  CE    . LYS A 1 4133 ? 86.718  92.859  87.833  1.00 54.28  ? 4133 LYS A CE    1 
ATOM   19341 N  NZ    . LYS A 1 4133 ? 86.312  94.290  87.758  1.00 56.64  ? 4133 LYS A NZ    1 
ATOM   19342 N  N     . VAL A 1 4134 ? 82.515  90.598  82.780  1.00 19.73  ? 4134 VAL A N     1 
ATOM   19343 C  CA    . VAL A 1 4134 ? 81.999  89.624  81.811  1.00 19.06  ? 4134 VAL A CA    1 
ATOM   19344 C  C     . VAL A 1 4134 ? 82.946  89.559  80.617  1.00 18.41  ? 4134 VAL A C     1 
ATOM   19345 O  O     . VAL A 1 4134 ? 83.309  90.610  80.061  1.00 19.41  ? 4134 VAL A O     1 
ATOM   19346 C  CB    . VAL A 1 4134 ? 80.583  90.005  81.377  1.00 15.93  ? 4134 VAL A CB    1 
ATOM   19347 C  CG1   . VAL A 1 4134 ? 80.157  89.201  80.158  1.00 11.84  ? 4134 VAL A CG1   1 
ATOM   19348 C  CG2   . VAL A 1 4134 ? 79.607  89.801  82.526  1.00 14.91  ? 4134 VAL A CG2   1 
ATOM   19349 N  N     . PRO A 1 4135 ? 83.378  88.369  80.195  1.00 18.17  ? 4135 PRO A N     1 
ATOM   19350 C  CA    . PRO A 1 4135 ? 84.368  88.283  79.114  1.00 16.65  ? 4135 PRO A CA    1 
ATOM   19351 C  C     . PRO A 1 4135 ? 83.831  88.827  77.797  1.00 16.68  ? 4135 PRO A C     1 
ATOM   19352 O  O     . PRO A 1 4135 ? 82.643  88.717  77.487  1.00 14.34  ? 4135 PRO A O     1 
ATOM   19353 C  CB    . PRO A 1 4135 ? 84.663  86.780  79.018  1.00 18.97  ? 4135 PRO A CB    1 
ATOM   19354 C  CG    . PRO A 1 4135 ? 84.138  86.190  80.292  1.00 18.02  ? 4135 PRO A CG    1 
ATOM   19355 C  CD    . PRO A 1 4135 ? 82.985  87.042  80.693  1.00 13.61  ? 4135 PRO A CD    1 
ATOM   19356 N  N     . VAL A 1 4136 ? 84.739  89.418  77.018  1.00 18.66  ? 4136 VAL A N     1 
ATOM   19357 C  CA    . VAL A 1 4136 ? 84.370  89.993  75.727  1.00 15.07  ? 4136 VAL A CA    1 
ATOM   19358 C  C     . VAL A 1 4136 ? 83.992  88.897  74.738  1.00 10.95  ? 4136 VAL A C     1 
ATOM   19359 O  O     . VAL A 1 4136 ? 83.080  89.069  73.919  1.00 10.98  ? 4136 VAL A O     1 
ATOM   19360 C  CB    . VAL A 1 4136 ? 85.518  90.870  75.194  1.00 17.84  ? 4136 VAL A CB    1 
ATOM   19361 C  CG1   . VAL A 1 4136 ? 85.211  91.371  73.791  1.00 14.72  ? 4136 VAL A CG1   1 
ATOM   19362 C  CG2   . VAL A 1 4136 ? 85.773  92.036  76.135  1.00 21.18  ? 4136 VAL A CG2   1 
ATOM   19363 N  N     . ASN A 1 4137 ? 84.688  87.758  74.789  1.00 11.78  ? 4137 ASN A N     1 
ATOM   19364 C  CA    . ASN A 1 4137 ? 84.406  86.675  73.851  1.00 15.93  ? 4137 ASN A CA    1 
ATOM   19365 C  C     . ASN A 1 4137 ? 82.989  86.140  74.024  1.00 12.64  ? 4137 ASN A C     1 
ATOM   19366 O  O     . ASN A 1 4137 ? 82.301  85.853  73.037  1.00 12.45  ? 4137 ASN A O     1 
ATOM   19367 C  CB    . ASN A 1 4137 ? 85.447  85.559  74.005  1.00 18.57  ? 4137 ASN A CB    1 
ATOM   19368 C  CG    . ASN A 1 4137 ? 85.415  84.892  75.376  1.00 30.76  ? 4137 ASN A CG    1 
ATOM   19369 O  OD1   . ASN A 1 4137 ? 84.543  85.159  76.202  1.00 31.45  ? 4137 ASN A OD1   1 
ATOM   19370 N  ND2   . ASN A 1 4137 ? 86.379  84.011  75.618  1.00 30.93  ? 4137 ASN A ND2   1 
ATOM   19371 N  N     . LEU A 1 4138 ? 82.534  86.002  75.272  1.00 12.84  ? 4138 LEU A N     1 
ATOM   19372 C  CA    . LEU A 1 4138 ? 81.157  85.586  75.514  1.00 10.68  ? 4138 LEU A CA    1 
ATOM   19373 C  C     . LEU A 1 4138 ? 80.170  86.619  74.988  1.00 10.94  ? 4138 LEU A C     1 
ATOM   19374 O  O     . LEU A 1 4138 ? 79.133  86.264  74.415  1.00 11.89  ? 4138 LEU A O     1 
ATOM   19375 C  CB    . LEU A 1 4138 ? 80.934  85.346  77.006  1.00 13.94  ? 4138 LEU A CB    1 
ATOM   19376 C  CG    . LEU A 1 4138 ? 79.497  84.990  77.393  1.00 10.06  ? 4138 LEU A CG    1 
ATOM   19377 C  CD1   . LEU A 1 4138 ? 79.252  83.498  77.228  1.00 7.93   ? 4138 LEU A CD1   1 
ATOM   19378 C  CD2   . LEU A 1 4138 ? 79.186  85.443  78.806  1.00 7.92   ? 4138 LEU A CD2   1 
ATOM   19379 N  N     . LEU A 1 4139 ? 80.473  87.906  75.180  1.00 8.38   ? 4139 LEU A N     1 
ATOM   19380 C  CA    . LEU A 1 4139 ? 79.593  88.959  74.686  1.00 7.89   ? 4139 LEU A CA    1 
ATOM   19381 C  C     . LEU A 1 4139 ? 79.469  88.909  73.169  1.00 8.93   ? 4139 LEU A C     1 
ATOM   19382 O  O     . LEU A 1 4139 ? 78.371  89.063  72.622  1.00 9.50   ? 4139 LEU A O     1 
ATOM   19383 C  CB    . LEU A 1 4139 ? 80.108  90.326  75.138  1.00 8.09   ? 4139 LEU A CB    1 
ATOM   19384 C  CG    . LEU A 1 4139 ? 80.013  90.627  76.635  1.00 10.90  ? 4139 LEU A CG    1 
ATOM   19385 C  CD1   . LEU A 1 4139 ? 80.694  91.947  76.961  1.00 7.54   ? 4139 LEU A CD1   1 
ATOM   19386 C  CD2   . LEU A 1 4139 ? 78.563  90.642  77.089  1.00 10.15  ? 4139 LEU A CD2   1 
ATOM   19387 N  N     . ARG A 1 4140 ? 80.587  88.698  72.472  1.00 8.51   ? 4140 ARG A N     1 
ATOM   19388 C  CA    . ARG A 1 4140 ? 80.543  88.600  71.017  1.00 9.08   ? 4140 ARG A CA    1 
ATOM   19389 C  C     . ARG A 1 4140 ? 79.816  87.339  70.567  1.00 8.51   ? 4140 ARG A C     1 
ATOM   19390 O  O     . ARG A 1 4140 ? 79.078  87.363  69.574  1.00 8.43   ? 4140 ARG A O     1 
ATOM   19391 C  CB    . ARG A 1 4140 ? 81.958  88.636  70.443  1.00 12.49  ? 4140 ARG A CB    1 
ATOM   19392 C  CG    . ARG A 1 4140 ? 82.733  89.897  70.782  1.00 11.20  ? 4140 ARG A CG    1 
ATOM   19393 C  CD    . ARG A 1 4140 ? 84.152  89.827  70.248  1.00 15.32  ? 4140 ARG A CD    1 
ATOM   19394 N  NE    . ARG A 1 4140 ? 84.213  89.119  68.975  1.00 22.88  ? 4140 ARG A NE    1 
ATOM   19395 C  CZ    . ARG A 1 4140 ? 84.387  89.706  67.800  1.00 20.07  ? 4140 ARG A CZ    1 
ATOM   19396 N  NH1   . ARG A 1 4140 ? 84.535  91.017  67.697  1.00 19.06  ? 4140 ARG A NH1   1 
ATOM   19397 N  NH2   . ARG A 1 4140 ? 84.408  88.961  66.699  1.00 18.87  ? 4140 ARG A NH2   1 
ATOM   19398 N  N     . ALA A 1 4141 ? 80.016  86.226  71.278  1.00 8.86   ? 4141 ALA A N     1 
ATOM   19399 C  CA    . ALA A 1 4141 ? 79.410  84.963  70.868  1.00 8.44   ? 4141 ALA A CA    1 
ATOM   19400 C  C     . ALA A 1 4141 ? 77.889  85.019  70.945  1.00 9.82   ? 4141 ALA A C     1 
ATOM   19401 O  O     . ALA A 1 4141 ? 77.197  84.519  70.050  1.00 13.83  ? 4141 ALA A O     1 
ATOM   19402 C  CB    . ALA A 1 4141 ? 79.946  83.821  71.730  1.00 8.74   ? 4141 ALA A CB    1 
ATOM   19403 N  N     . GLY A 1 4142 ? 77.348  85.619  72.005  1.00 5.89   ? 4142 GLY A N     1 
ATOM   19404 C  CA    . GLY A 1 4142 ? 75.920  85.666  72.217  1.00 7.07   ? 4142 GLY A CA    1 
ATOM   19405 C  C     . GLY A 1 4142 ? 75.291  86.973  71.753  1.00 5.92   ? 4142 GLY A C     1 
ATOM   19406 O  O     . GLY A 1 4142 ? 75.959  87.917  71.341  1.00 7.37   ? 4142 GLY A O     1 
ATOM   19407 N  N     . ARG A 1 4143 ? 73.964  87.006  71.829  1.00 4.49   ? 4143 ARG A N     1 
ATOM   19408 C  CA    . ARG A 1 4143 ? 73.196  88.207  71.533  1.00 5.70   ? 4143 ARG A CA    1 
ATOM   19409 C  C     . ARG A 1 4143 ? 72.752  88.851  72.838  1.00 5.18   ? 4143 ARG A C     1 
ATOM   19410 O  O     . ARG A 1 4143 ? 72.191  88.178  73.710  1.00 6.85   ? 4143 ARG A O     1 
ATOM   19411 C  CB    . ARG A 1 4143 ? 71.984  87.902  70.652  1.00 6.40   ? 4143 ARG A CB    1 
ATOM   19412 C  CG    . ARG A 1 4143 ? 71.219  89.155  70.256  1.00 11.19  ? 4143 ARG A CG    1 
ATOM   19413 C  CD    . ARG A 1 4143 ? 70.076  88.866  69.305  1.00 15.32  ? 4143 ARG A CD    1 
ATOM   19414 N  NE    . ARG A 1 4143 ? 69.341  90.082  68.981  1.00 19.31  ? 4143 ARG A NE    1 
ATOM   19415 C  CZ    . ARG A 1 4143 ? 68.304  90.135  68.157  1.00 21.35  ? 4143 ARG A CZ    1 
ATOM   19416 N  NH1   . ARG A 1 4143 ? 67.873  89.060  67.519  1.00 19.98  ? 4143 ARG A NH1   1 
ATOM   19417 N  NH2   . ARG A 1 4143 ? 67.686  91.297  67.966  1.00 18.50  ? 4143 ARG A NH2   1 
ATOM   19418 N  N     . ILE A 1 4144 ? 72.999  90.151  72.959  1.00 4.18   ? 4144 ILE A N     1 
ATOM   19419 C  CA    . ILE A 1 4144 ? 72.853  90.883  74.211  1.00 5.53   ? 4144 ILE A CA    1 
ATOM   19420 C  C     . ILE A 1 4144 ? 71.508  91.594  74.223  1.00 6.07   ? 4144 ILE A C     1 
ATOM   19421 O  O     . ILE A 1 4144 ? 71.100  92.188  73.217  1.00 6.01   ? 4144 ILE A O     1 
ATOM   19422 C  CB    . ILE A 1 4144 ? 74.007  91.885  74.396  1.00 6.70   ? 4144 ILE A CB    1 
ATOM   19423 C  CG1   . ILE A 1 4144 ? 75.351  91.162  74.283  1.00 7.35   ? 4144 ILE A CG1   1 
ATOM   19424 C  CG2   . ILE A 1 4144 ? 73.888  92.603  75.731  1.00 6.17   ? 4144 ILE A CG2   1 
ATOM   19425 C  CD1   . ILE A 1 4144 ? 76.518  92.075  73.994  1.00 8.79   ? 4144 ILE A CD1   1 
ATOM   19426 N  N     . PHE A 1 4145 ? 70.812  91.515  75.354  1.00 7.37   ? 4145 PHE A N     1 
ATOM   19427 C  CA    . PHE A 1 4145 ? 69.588  92.267  75.591  1.00 6.52   ? 4145 PHE A CA    1 
ATOM   19428 C  C     . PHE A 1 4145 ? 69.735  93.022  76.901  1.00 4.88   ? 4145 PHE A C     1 
ATOM   19429 O  O     . PHE A 1 4145 ? 70.016  92.417  77.942  1.00 6.58   ? 4145 PHE A O     1 
ATOM   19430 C  CB    . PHE A 1 4145 ? 68.366  91.346  75.636  1.00 7.03   ? 4145 PHE A CB    1 
ATOM   19431 C  CG    . PHE A 1 4145 ? 68.113  90.623  74.349  1.00 8.36   ? 4145 PHE A CG    1 
ATOM   19432 C  CD1   . PHE A 1 4145 ? 67.400  91.228  73.329  1.00 12.82  ? 4145 PHE A CD1   1 
ATOM   19433 C  CD2   . PHE A 1 4145 ? 68.600  89.342  74.154  1.00 7.80   ? 4145 PHE A CD2   1 
ATOM   19434 C  CE1   . PHE A 1 4145 ? 67.172  90.566  72.141  1.00 15.71  ? 4145 PHE A CE1   1 
ATOM   19435 C  CE2   . PHE A 1 4145 ? 68.375  88.676  72.970  1.00 9.77   ? 4145 PHE A CE2   1 
ATOM   19436 C  CZ    . PHE A 1 4145 ? 67.661  89.288  71.962  1.00 14.63  ? 4145 PHE A CZ    1 
ATOM   19437 N  N     . VAL A 1 4146 ? 69.538  94.335  76.849  1.00 5.22   ? 4146 VAL A N     1 
ATOM   19438 C  CA    . VAL A 1 4146 ? 69.699  95.205  78.007  1.00 6.50   ? 4146 VAL A CA    1 
ATOM   19439 C  C     . VAL A 1 4146 ? 68.341  95.400  78.663  1.00 5.51   ? 4146 VAL A C     1 
ATOM   19440 O  O     . VAL A 1 4146 ? 67.379  95.823  78.009  1.00 8.21   ? 4146 VAL A O     1 
ATOM   19441 C  CB    . VAL A 1 4146 ? 70.319  96.555  77.608  1.00 4.03   ? 4146 VAL A CB    1 
ATOM   19442 C  CG1   . VAL A 1 4146 ? 70.110  97.585  78.709  1.00 5.89   ? 4146 VAL A CG1   1 
ATOM   19443 C  CG2   . VAL A 1 4146 ? 71.797  96.386  77.310  1.00 4.22   ? 4146 VAL A CG2   1 
ATOM   19444 N  N     . PHE A 1 4147 ? 68.262  95.090  79.952  1.00 5.58   ? 4147 PHE A N     1 
ATOM   19445 C  CA    . PHE A 1 4147 ? 67.053  95.282  80.741  1.00 7.88   ? 4147 PHE A CA    1 
ATOM   19446 C  C     . PHE A 1 4147 ? 67.294  96.414  81.729  1.00 7.28   ? 4147 PHE A C     1 
ATOM   19447 O  O     . PHE A 1 4147 ? 68.228  96.352  82.536  1.00 8.31   ? 4147 PHE A O     1 
ATOM   19448 C  CB    . PHE A 1 4147 ? 66.655  93.993  81.459  1.00 8.26   ? 4147 PHE A CB    1 
ATOM   19449 C  CG    . PHE A 1 4147 ? 66.157  92.922  80.533  1.00 9.77   ? 4147 PHE A CG    1 
ATOM   19450 C  CD1   . PHE A 1 4147 ? 67.043  92.071  79.893  1.00 9.07   ? 4147 PHE A CD1   1 
ATOM   19451 C  CD2   . PHE A 1 4147 ? 64.801  92.771  80.295  1.00 10.79  ? 4147 PHE A CD2   1 
ATOM   19452 C  CE1   . PHE A 1 4147 ? 66.586  91.090  79.036  1.00 9.05   ? 4147 PHE A CE1   1 
ATOM   19453 C  CE2   . PHE A 1 4147 ? 64.338  91.789  79.441  1.00 13.95  ? 4147 PHE A CE2   1 
ATOM   19454 C  CZ    . PHE A 1 4147 ? 65.231  90.947  78.811  1.00 11.81  ? 4147 PHE A CZ    1 
ATOM   19455 N  N     . GLU A 1 4148 ? 66.454  97.436  81.662  1.00 10.15  ? 4148 GLU A N     1 
ATOM   19456 C  CA    . GLU A 1 4148 ? 66.645  98.659  82.426  1.00 10.38  ? 4148 GLU A CA    1 
ATOM   19457 C  C     . GLU A 1 4148 ? 65.280  99.289  82.642  1.00 11.66  ? 4148 GLU A C     1 
ATOM   19458 O  O     . GLU A 1 4148 ? 64.274  98.809  82.104  1.00 13.61  ? 4148 GLU A O     1 
ATOM   19459 C  CB    . GLU A 1 4148 ? 67.594  99.620  81.698  1.00 10.71  ? 4148 GLU A CB    1 
ATOM   19460 C  CG    . GLU A 1 4148 ? 67.045  100.190 80.404  1.00 13.15  ? 4148 GLU A CG    1 
ATOM   19461 C  CD    . GLU A 1 4148 ? 68.088  100.974 79.632  1.00 17.00  ? 4148 GLU A CD    1 
ATOM   19462 O  OE1   . GLU A 1 4148 ? 68.703  101.887 80.223  1.00 12.05  ? 4148 GLU A OE1   1 
ATOM   19463 O  OE2   . GLU A 1 4148 ? 68.294  100.678 78.436  1.00 15.98  ? 4148 GLU A OE2   1 
ATOM   19464 N  N     . PRO A 1 4149 ? 65.200  100.349 83.446  1.00 15.19  ? 4149 PRO A N     1 
ATOM   19465 C  CA    . PRO A 1 4149 ? 63.926  101.059 83.605  1.00 15.23  ? 4149 PRO A CA    1 
ATOM   19466 C  C     . PRO A 1 4149 ? 63.391  101.539 82.269  1.00 14.42  ? 4149 PRO A C     1 
ATOM   19467 O  O     . PRO A 1 4149 ? 64.163  101.956 81.392  1.00 15.78  ? 4149 PRO A O     1 
ATOM   19468 C  CB    . PRO A 1 4149 ? 64.292  102.240 84.514  1.00 18.81  ? 4149 PRO A CB    1 
ATOM   19469 C  CG    . PRO A 1 4149 ? 65.412  101.732 85.329  1.00 16.46  ? 4149 PRO A CG    1 
ATOM   19470 C  CD    . PRO A 1 4149 ? 66.185  100.776 84.459  1.00 15.89  ? 4149 PRO A CD    1 
ATOM   19471 N  N     . PRO A 1 4150 ? 62.075  101.477 82.073  1.00 14.53  ? 4150 PRO A N     1 
ATOM   19472 C  CA    . PRO A 1 4150 ? 61.506  101.926 80.806  1.00 16.93  ? 4150 PRO A CA    1 
ATOM   19473 C  C     . PRO A 1 4150 ? 61.778  103.395 80.585  1.00 17.27  ? 4150 PRO A C     1 
ATOM   19474 O  O     . PRO A 1 4150 ? 61.924  104.173 81.548  1.00 17.14  ? 4150 PRO A O     1 
ATOM   19475 C  CB    . PRO A 1 4150 ? 60.006  101.646 80.976  1.00 16.40  ? 4150 PRO A CB    1 
ATOM   19476 C  CG    . PRO A 1 4150 ? 59.925  100.597 82.027  1.00 11.75  ? 4150 PRO A CG    1 
ATOM   19477 C  CD    . PRO A 1 4150 ? 61.076  100.844 82.948  1.00 12.12  ? 4150 PRO A CD    1 
ATOM   19478 N  N     . PRO A 1 4151 ? 61.874  103.830 79.325  1.00 20.04  ? 4151 PRO A N     1 
ATOM   19479 C  CA    . PRO A 1 4151 ? 62.224  105.233 79.052  1.00 18.97  ? 4151 PRO A CA    1 
ATOM   19480 C  C     . PRO A 1 4151 ? 61.261  106.246 79.651  1.00 21.05  ? 4151 PRO A C     1 
ATOM   19481 O  O     . PRO A 1 4151 ? 61.697  107.340 80.030  1.00 28.79  ? 4151 PRO A O     1 
ATOM   19482 C  CB    . PRO A 1 4151 ? 62.229  105.306 77.516  1.00 17.77  ? 4151 PRO A CB    1 
ATOM   19483 C  CG    . PRO A 1 4151 ? 61.599  104.031 77.038  1.00 20.78  ? 4151 PRO A CG    1 
ATOM   19484 C  CD    . PRO A 1 4151 ? 61.831  103.015 78.100  1.00 16.39  ? 4151 PRO A CD    1 
ATOM   19485 N  N     . GLY A 1 4152 ? 59.977  105.926 79.756  1.00 14.17  ? 4152 GLY A N     1 
ATOM   19486 C  CA    . GLY A 1 4152 ? 59.029  106.892 80.263  1.00 9.39   ? 4152 GLY A CA    1 
ATOM   19487 C  C     . GLY A 1 4152 ? 57.790  106.237 80.831  1.00 7.75   ? 4152 GLY A C     1 
ATOM   19488 O  O     . GLY A 1 4152 ? 57.704  105.012 80.942  1.00 10.98  ? 4152 GLY A O     1 
ATOM   19489 N  N     . VAL A 1 4153 ? 56.825  107.086 81.196  1.00 9.46   ? 4153 VAL A N     1 
ATOM   19490 C  CA    . VAL A 1 4153 ? 55.585  106.607 81.802  1.00 8.75   ? 4153 VAL A CA    1 
ATOM   19491 C  C     . VAL A 1 4153 ? 54.824  105.712 80.832  1.00 5.75   ? 4153 VAL A C     1 
ATOM   19492 O  O     . VAL A 1 4153 ? 54.303  104.657 81.215  1.00 6.55   ? 4153 VAL A O     1 
ATOM   19493 C  CB    . VAL A 1 4153 ? 54.724  107.798 82.267  1.00 6.56   ? 4153 VAL A CB    1 
ATOM   19494 C  CG1   . VAL A 1 4153 ? 53.323  107.334 82.643  1.00 7.67   ? 4153 VAL A CG1   1 
ATOM   19495 C  CG2   . VAL A 1 4153 ? 55.385  108.512 83.432  1.00 3.99   ? 4153 VAL A CG2   1 
ATOM   19496 N  N     . LYS A 1 4154 ? 54.741  106.124 79.565  1.00 8.51   ? 4154 LYS A N     1 
ATOM   19497 C  CA    . LYS A 1 4154 ? 54.033  105.330 78.565  1.00 8.24   ? 4154 LYS A CA    1 
ATOM   19498 C  C     . LYS A 1 4154 ? 54.670  103.957 78.400  1.00 7.35   ? 4154 LYS A C     1 
ATOM   19499 O  O     . LYS A 1 4154 ? 53.978  102.933 78.411  1.00 6.74   ? 4154 LYS A O     1 
ATOM   19500 C  CB    . LYS A 1 4154 ? 54.008  106.081 77.232  1.00 8.85   ? 4154 LYS A CB    1 
ATOM   19501 C  CG    . LYS A 1 4154 ? 53.336  105.331 76.097  1.00 11.43  ? 4154 LYS A CG    1 
ATOM   19502 C  CD    . LYS A 1 4154 ? 53.330  106.163 74.824  1.00 17.02  ? 4154 LYS A CD    1 
ATOM   19503 C  CE    . LYS A 1 4154 ? 52.508  105.501 73.731  1.00 20.48  ? 4154 LYS A CE    1 
ATOM   19504 N  NZ    . LYS A 1 4154 ? 52.364  106.378 72.537  1.00 15.68  ? 4154 LYS A NZ    1 
ATOM   19505 N  N     . ALA A 1 4155 ? 55.997  103.919 78.258  1.00 6.47   ? 4155 ALA A N     1 
ATOM   19506 C  CA    . ALA A 1 4155 ? 56.692  102.644 78.119  1.00 7.48   ? 4155 ALA A CA    1 
ATOM   19507 C  C     . ALA A 1 4155 ? 56.549  101.797 79.377  1.00 9.20   ? 4155 ALA A C     1 
ATOM   19508 O  O     . ALA A 1 4155 ? 56.370  100.576 79.295  1.00 14.20  ? 4155 ALA A O     1 
ATOM   19509 C  CB    . ALA A 1 4155 ? 58.165  102.886 77.795  1.00 10.92  ? 4155 ALA A CB    1 
ATOM   19510 N  N     . ASN A 1 4156 ? 56.624  102.429 80.551  1.00 6.95   ? 4156 ASN A N     1 
ATOM   19511 C  CA    . ASN A 1 4156 ? 56.480  101.698 81.806  1.00 6.65   ? 4156 ASN A CA    1 
ATOM   19512 C  C     . ASN A 1 4156 ? 55.111  101.037 81.901  1.00 6.21   ? 4156 ASN A C     1 
ATOM   19513 O  O     . ASN A 1 4156 ? 54.997  99.854  82.247  1.00 7.56   ? 4156 ASN A O     1 
ATOM   19514 C  CB    . ASN A 1 4156 ? 56.707  102.647 82.985  1.00 5.42   ? 4156 ASN A CB    1 
ATOM   19515 C  CG    . ASN A 1 4156 ? 56.954  101.917 84.291  1.00 5.33   ? 4156 ASN A CG    1 
ATOM   19516 O  OD1   . ASN A 1 4156 ? 56.124  101.131 84.746  1.00 5.30   ? 4156 ASN A OD1   1 
ATOM   19517 N  ND2   . ASN A 1 4156 ? 58.101  102.181 84.905  1.00 5.52   ? 4156 ASN A ND2   1 
ATOM   19518 N  N     . MET A 1 4157 ? 54.056  101.785 81.578  1.00 5.48   ? 4157 MET A N     1 
ATOM   19519 C  CA    . MET A 1 4157 ? 52.710  101.235 81.685  1.00 5.80   ? 4157 MET A CA    1 
ATOM   19520 C  C     . MET A 1 4157 ? 52.452  100.192 80.606  1.00 9.36   ? 4157 MET A C     1 
ATOM   19521 O  O     . MET A 1 4157 ? 51.736  99.213  80.843  1.00 11.82  ? 4157 MET A O     1 
ATOM   19522 C  CB    . MET A 1 4157 ? 51.679  102.359 81.623  1.00 3.95   ? 4157 MET A CB    1 
ATOM   19523 C  CG    . MET A 1 4157 ? 51.548  103.117 82.935  1.00 4.84   ? 4157 MET A CG    1 
ATOM   19524 S  SD    . MET A 1 4157 ? 50.395  104.497 82.861  1.00 8.23   ? 4157 MET A SD    1 
ATOM   19525 C  CE    . MET A 1 4157 ? 48.854  103.644 83.160  1.00 2.92   ? 4157 MET A CE    1 
ATOM   19526 N  N     . LEU A 1 4158 ? 53.031  100.373 79.415  1.00 10.71  ? 4158 LEU A N     1 
ATOM   19527 C  CA    . LEU A 1 4158 ? 52.908  99.349  78.384  1.00 10.25  ? 4158 LEU A CA    1 
ATOM   19528 C  C     . LEU A 1 4158 ? 53.583  98.054  78.816  1.00 12.93  ? 4158 LEU A C     1 
ATOM   19529 O  O     . LEU A 1 4158 ? 53.034  96.964  78.620  1.00 16.26  ? 4158 LEU A O     1 
ATOM   19530 C  CB    . LEU A 1 4158 ? 53.495  99.851  77.065  1.00 11.08  ? 4158 LEU A CB    1 
ATOM   19531 C  CG    . LEU A 1 4158 ? 52.648  100.867 76.297  1.00 11.42  ? 4158 LEU A CG    1 
ATOM   19532 C  CD1   . LEU A 1 4158 ? 53.428  101.441 75.127  1.00 15.64  ? 4158 LEU A CD1   1 
ATOM   19533 C  CD2   . LEU A 1 4158 ? 51.354  100.232 75.819  1.00 13.39  ? 4158 LEU A CD2   1 
ATOM   19534 N  N     . ARG A 1 4159 ? 54.769  98.154  79.423  1.00 9.28   ? 4159 ARG A N     1 
ATOM   19535 C  CA    . ARG A 1 4159 ? 55.437  96.963  79.936  1.00 11.01  ? 4159 ARG A CA    1 
ATOM   19536 C  C     . ARG A 1 4159 ? 54.619  96.309  81.042  1.00 14.14  ? 4159 ARG A C     1 
ATOM   19537 O  O     . ARG A 1 4159 ? 54.532  95.077  81.116  1.00 17.83  ? 4159 ARG A O     1 
ATOM   19538 C  CB    . ARG A 1 4159 ? 56.837  97.318  80.437  1.00 13.07  ? 4159 ARG A CB    1 
ATOM   19539 C  CG    . ARG A 1 4159 ? 57.606  96.143  81.016  1.00 19.84  ? 4159 ARG A CG    1 
ATOM   19540 C  CD    . ARG A 1 4159 ? 59.015  96.542  81.427  1.00 29.45  ? 4159 ARG A CD    1 
ATOM   19541 N  NE    . ARG A 1 4159 ? 59.659  97.389  80.429  1.00 37.29  ? 4159 ARG A NE    1 
ATOM   19542 C  CZ    . ARG A 1 4159 ? 60.946  97.711  80.439  1.00 34.59  ? 4159 ARG A CZ    1 
ATOM   19543 N  NH1   . ARG A 1 4159 ? 61.761  97.275  81.386  1.00 24.47  ? 4159 ARG A NH1   1 
ATOM   19544 N  NH2   . ARG A 1 4159 ? 61.427  98.491  79.475  1.00 22.50  ? 4159 ARG A NH2   1 
ATOM   19545 N  N     . THR A 1 4160 ? 54.012  97.119  81.914  1.00 12.99  ? 4160 THR A N     1 
ATOM   19546 C  CA    . THR A 1 4160 ? 53.173  96.567  82.974  1.00 12.17  ? 4160 THR A CA    1 
ATOM   19547 C  C     . THR A 1 4160 ? 51.984  95.806  82.400  1.00 15.58  ? 4160 THR A C     1 
ATOM   19548 O  O     . THR A 1 4160 ? 51.713  94.666  82.794  1.00 18.35  ? 4160 THR A O     1 
ATOM   19549 C  CB    . THR A 1 4160 ? 52.692  97.683  83.901  1.00 8.63   ? 4160 THR A CB    1 
ATOM   19550 O  OG1   . THR A 1 4160 ? 53.795  98.185  84.665  1.00 7.23   ? 4160 THR A OG1   1 
ATOM   19551 C  CG2   . THR A 1 4160 ? 51.616  97.162  84.843  1.00 8.04   ? 4160 THR A CG2   1 
ATOM   19552 N  N     . PHE A 1 4161 ? 51.262  96.422  81.461  1.00 16.53  ? 4161 PHE A N     1 
ATOM   19553 C  CA    . PHE A 1 4161 ? 50.092  95.766  80.884  1.00 16.29  ? 4161 PHE A CA    1 
ATOM   19554 C  C     . PHE A 1 4161 ? 50.477  94.561  80.034  1.00 19.78  ? 4161 PHE A C     1 
ATOM   19555 O  O     . PHE A 1 4161 ? 49.668  93.641  79.870  1.00 28.08  ? 4161 PHE A O     1 
ATOM   19556 C  CB    . PHE A 1 4161 ? 49.271  96.763  80.065  1.00 13.33  ? 4161 PHE A CB    1 
ATOM   19557 C  CG    . PHE A 1 4161 ? 48.441  97.699  80.902  1.00 14.21  ? 4161 PHE A CG    1 
ATOM   19558 C  CD1   . PHE A 1 4161 ? 47.382  97.218  81.653  1.00 16.74  ? 4161 PHE A CD1   1 
ATOM   19559 C  CD2   . PHE A 1 4161 ? 48.715  99.055  80.937  1.00 14.58  ? 4161 PHE A CD2   1 
ATOM   19560 C  CE1   . PHE A 1 4161 ? 46.616  98.070  82.426  1.00 16.84  ? 4161 PHE A CE1   1 
ATOM   19561 C  CE2   . PHE A 1 4161 ? 47.952  99.913  81.707  1.00 14.41  ? 4161 PHE A CE2   1 
ATOM   19562 C  CZ    . PHE A 1 4161 ? 46.901  99.420  82.451  1.00 13.02  ? 4161 PHE A CZ    1 
ATOM   19563 N  N     . SER A 1 4162 ? 51.694  94.542  79.489  1.00 17.23  ? 4162 SER A N     1 
ATOM   19564 C  CA    . SER A 1 4162 ? 52.152  93.361  78.767  1.00 17.42  ? 4162 SER A CA    1 
ATOM   19565 C  C     . SER A 1 4162 ? 52.546  92.232  79.711  1.00 20.72  ? 4162 SER A C     1 
ATOM   19566 O  O     . SER A 1 4162 ? 52.362  91.058  79.374  1.00 28.28  ? 4162 SER A O     1 
ATOM   19567 C  CB    . SER A 1 4162 ? 53.328  93.720  77.858  1.00 19.63  ? 4162 SER A CB    1 
ATOM   19568 O  OG    . SER A 1 4162 ? 54.469  94.080  78.617  1.00 21.71  ? 4162 SER A OG    1 
ATOM   19569 N  N     . SER A 1 4163 ? 53.084  92.562  80.887  1.00 20.04  ? 4163 SER A N     1 
ATOM   19570 C  CA    . SER A 1 4163 ? 53.549  91.532  81.809  1.00 21.69  ? 4163 SER A CA    1 
ATOM   19571 C  C     . SER A 1 4163 ? 52.403  90.820  82.519  1.00 21.47  ? 4163 SER A C     1 
ATOM   19572 O  O     . SER A 1 4163 ? 52.525  89.633  82.840  1.00 26.05  ? 4163 SER A O     1 
ATOM   19573 C  CB    . SER A 1 4163 ? 54.500  92.140  82.841  1.00 22.67  ? 4163 SER A CB    1 
ATOM   19574 O  OG    . SER A 1 4163 ? 53.852  93.143  83.604  1.00 29.98  ? 4163 SER A OG    1 
ATOM   19575 N  N     . ILE A 1 4164 ? 51.297  91.513  82.774  1.00 22.62  ? 4164 ILE A N     1 
ATOM   19576 C  CA    . ILE A 1 4164 ? 50.174  90.931  83.507  1.00 24.41  ? 4164 ILE A CA    1 
ATOM   19577 C  C     . ILE A 1 4164 ? 49.200  90.274  82.536  1.00 24.93  ? 4164 ILE A C     1 
ATOM   19578 O  O     . ILE A 1 4164 ? 48.790  90.899  81.547  1.00 28.31  ? 4164 ILE A O     1 
ATOM   19579 C  CB    . ILE A 1 4164 ? 49.473  91.985  84.379  1.00 25.57  ? 4164 ILE A CB    1 
ATOM   19580 C  CG1   . ILE A 1 4164 ? 50.487  92.656  85.310  1.00 21.38  ? 4164 ILE A CG1   1 
ATOM   19581 C  CG2   . ILE A 1 4164 ? 48.341  91.357  85.172  1.00 22.20  ? 4164 ILE A CG2   1 
ATOM   19582 C  CD1   . ILE A 1 4164 ? 49.936  93.833  86.077  1.00 18.23  ? 4164 ILE A CD1   1 
ATOM   19583 N  N     . PRO A 1 4165 ? 48.818  89.018  82.772  1.00 27.56  ? 4165 PRO A N     1 
ATOM   19584 C  CA    . PRO A 1 4165 ? 47.909  88.330  81.847  1.00 30.35  ? 4165 PRO A CA    1 
ATOM   19585 C  C     . PRO A 1 4165 ? 46.548  89.006  81.767  1.00 27.75  ? 4165 PRO A C     1 
ATOM   19586 O  O     . PRO A 1 4165 ? 46.091  89.656  82.709  1.00 27.73  ? 4165 PRO A O     1 
ATOM   19587 C  CB    . PRO A 1 4165 ? 47.793  86.924  82.448  1.00 26.76  ? 4165 PRO A CB    1 
ATOM   19588 C  CG    . PRO A 1 4165 ? 49.051  86.746  83.226  1.00 26.87  ? 4165 PRO A CG    1 
ATOM   19589 C  CD    . PRO A 1 4165 ? 49.376  88.103  83.782  1.00 28.27  ? 4165 PRO A CD    1 
ATOM   19590 N  N     . VAL A 1 4166 ? 45.905  88.849  80.607  1.00 30.78  ? 4166 VAL A N     1 
ATOM   19591 C  CA    . VAL A 1 4166 ? 44.583  89.432  80.396  1.00 33.69  ? 4166 VAL A CA    1 
ATOM   19592 C  C     . VAL A 1 4166 ? 43.560  88.800  81.333  1.00 32.81  ? 4166 VAL A C     1 
ATOM   19593 O  O     . VAL A 1 4166 ? 42.734  89.499  81.933  1.00 34.64  ? 4166 VAL A O     1 
ATOM   19594 C  CB    . VAL A 1 4166 ? 44.171  89.285  78.920  1.00 30.83  ? 4166 VAL A CB    1 
ATOM   19595 C  CG1   . VAL A 1 4166 ? 42.680  89.538  78.749  1.00 33.78  ? 4166 VAL A CG1   1 
ATOM   19596 C  CG2   . VAL A 1 4166 ? 44.984  90.227  78.046  1.00 21.69  ? 4166 VAL A CG2   1 
ATOM   19597 N  N     . SER A 1 4167 ? 43.596  87.472  81.474  1.00 30.06  ? 4167 SER A N     1 
ATOM   19598 C  CA    . SER A 1 4167 ? 42.661  86.793  82.365  1.00 33.46  ? 4167 SER A CA    1 
ATOM   19599 C  C     . SER A 1 4167 ? 42.845  87.231  83.812  1.00 36.71  ? 4167 SER A C     1 
ATOM   19600 O  O     . SER A 1 4167 ? 41.884  87.222  84.591  1.00 39.60  ? 4167 SER A O     1 
ATOM   19601 C  CB    . SER A 1 4167 ? 42.825  85.278  82.242  1.00 39.90  ? 4167 SER A CB    1 
ATOM   19602 O  OG    . SER A 1 4167 ? 44.187  84.903  82.355  1.00 39.66  ? 4167 SER A OG    1 
ATOM   19603 N  N     . ARG A 1 4168 ? 44.070  87.603  84.190  1.00 34.84  ? 4168 ARG A N     1 
ATOM   19604 C  CA    . ARG A 1 4168 ? 44.310  88.151  85.521  1.00 29.21  ? 4168 ARG A CA    1 
ATOM   19605 C  C     . ARG A 1 4168 ? 43.489  89.413  85.757  1.00 31.80  ? 4168 ARG A C     1 
ATOM   19606 O  O     . ARG A 1 4168 ? 42.838  89.555  86.799  1.00 35.32  ? 4168 ARG A O     1 
ATOM   19607 C  CB    . ARG A 1 4168 ? 45.801  88.448  85.691  1.00 29.57  ? 4168 ARG A CB    1 
ATOM   19608 C  CG    . ARG A 1 4168 ? 46.197  89.035  87.035  1.00 26.04  ? 4168 ARG A CG    1 
ATOM   19609 C  CD    . ARG A 1 4168 ? 46.136  88.011  88.149  1.00 23.93  ? 4168 ARG A CD    1 
ATOM   19610 N  NE    . ARG A 1 4168 ? 46.563  88.589  89.418  1.00 27.94  ? 4168 ARG A NE    1 
ATOM   19611 C  CZ    . ARG A 1 4168 ? 47.821  88.634  89.835  1.00 24.01  ? 4168 ARG A CZ    1 
ATOM   19612 N  NH1   . ARG A 1 4168 ? 48.809  88.141  89.106  1.00 25.88  ? 4168 ARG A NH1   1 
ATOM   19613 N  NH2   . ARG A 1 4168 ? 48.096  89.192  91.011  1.00 17.93  ? 4168 ARG A NH2   1 
ATOM   19614 N  N     . ILE A 1 4169 ? 43.498  90.334  84.794  1.00 31.89  ? 4169 ILE A N     1 
ATOM   19615 C  CA    . ILE A 1 4169 ? 42.852  91.630  84.970  1.00 29.60  ? 4169 ILE A CA    1 
ATOM   19616 C  C     . ILE A 1 4169 ? 41.345  91.584  84.730  1.00 29.25  ? 4169 ILE A C     1 
ATOM   19617 O  O     . ILE A 1 4169 ? 40.607  92.385  85.323  1.00 29.54  ? 4169 ILE A O     1 
ATOM   19618 C  CB    . ILE A 1 4169 ? 43.533  92.659  84.046  1.00 23.20  ? 4169 ILE A CB    1 
ATOM   19619 C  CG1   . ILE A 1 4169 ? 45.006  92.809  84.429  1.00 22.06  ? 4169 ILE A CG1   1 
ATOM   19620 C  CG2   . ILE A 1 4169 ? 42.853  94.013  84.118  1.00 22.68  ? 4169 ILE A CG2   1 
ATOM   19621 C  CD1   . ILE A 1 4169 ? 45.826  93.596  83.431  1.00 24.98  ? 4169 ILE A CD1   1 
ATOM   19622 N  N     . CYS A 1 4170 ? 40.861  90.646  83.918  1.00 31.51  ? 4170 CYS A N     1 
ATOM   19623 C  CA    . CYS A 1 4170 ? 39.465  90.608  83.485  1.00 35.20  ? 4170 CYS A CA    1 
ATOM   19624 C  C     . CYS A 1 4170 ? 38.624  89.632  84.299  1.00 42.68  ? 4170 CYS A C     1 
ATOM   19625 O  O     . CYS A 1 4170 ? 37.777  88.926  83.745  1.00 50.19  ? 4170 CYS A O     1 
ATOM   19626 C  CB    . CYS A 1 4170 ? 39.386  90.268  82.000  1.00 40.92  ? 4170 CYS A CB    1 
ATOM   19627 S  SG    . CYS A 1 4170 ? 40.232  91.444  80.919  1.00 59.09  ? 4170 CYS A SG    1 
ATOM   19628 N  N     . LYS A 1 4171 ? 38.829  89.564  85.612  1.00 41.47  ? 4171 LYS A N     1 
ATOM   19629 C  CA    . LYS A 1 4171 ? 38.059  88.656  86.452  1.00 39.66  ? 4171 LYS A CA    1 
ATOM   19630 C  C     . LYS A 1 4171 ? 36.667  89.239  86.708  1.00 49.58  ? 4171 LYS A C     1 
ATOM   19631 O  O     . LYS A 1 4171 ? 36.256  90.227  86.092  1.00 51.43  ? 4171 LYS A O     1 
ATOM   19632 C  CB    . LYS A 1 4171 ? 38.814  88.355  87.743  1.00 38.61  ? 4171 LYS A CB    1 
ATOM   19633 C  CG    . LYS A 1 4171 ? 39.495  86.995  87.731  1.00 37.10  ? 4171 LYS A CG    1 
ATOM   19634 C  CD    . LYS A 1 4171 ? 40.503  86.851  88.855  1.00 36.98  ? 4171 LYS A CD    1 
ATOM   19635 C  CE    . LYS A 1 4171 ? 39.854  87.060  90.212  1.00 41.94  ? 4171 LYS A CE    1 
ATOM   19636 N  NZ    . LYS A 1 4171 ? 38.849  86.005  90.516  1.00 30.57  ? 4171 LYS A NZ    1 
ATOM   19637 N  N     . SER A 1 4172 ? 35.924  88.618  87.628  1.00 50.97  ? 4172 SER A N     1 
ATOM   19638 C  CA    . SER A 1 4172 ? 34.497  88.911  87.772  1.00 50.29  ? 4172 SER A CA    1 
ATOM   19639 C  C     . SER A 1 4172 ? 34.194  90.376  88.068  1.00 50.22  ? 4172 SER A C     1 
ATOM   19640 O  O     . SER A 1 4172 ? 33.307  90.940  87.404  1.00 54.32  ? 4172 SER A O     1 
ATOM   19641 C  CB    . SER A 1 4172 ? 33.892  87.990  88.838  1.00 58.75  ? 4172 SER A CB    1 
ATOM   19642 O  OG    . SER A 1 4172 ? 34.091  86.627  88.506  1.00 65.98  ? 4172 SER A OG    1 
ATOM   19643 N  N     . PRO A 1 4173 ? 34.848  91.047  89.021  1.00 48.88  ? 4173 PRO A N     1 
ATOM   19644 C  CA    . PRO A 1 4173 ? 34.553  92.475  89.231  1.00 38.74  ? 4173 PRO A CA    1 
ATOM   19645 C  C     . PRO A 1 4173 ? 35.043  93.302  88.051  1.00 35.50  ? 4173 PRO A C     1 
ATOM   19646 O  O     . PRO A 1 4173 ? 36.237  93.323  87.747  1.00 38.74  ? 4173 PRO A O     1 
ATOM   19647 C  CB    . PRO A 1 4173 ? 35.316  92.815  90.518  1.00 31.20  ? 4173 PRO A CB    1 
ATOM   19648 C  CG    . PRO A 1 4173 ? 35.598  91.508  91.162  1.00 37.74  ? 4173 PRO A CG    1 
ATOM   19649 C  CD    . PRO A 1 4173 ? 35.786  90.545  90.039  1.00 41.98  ? 4173 PRO A CD    1 
ATOM   19650 N  N     . ASN A 1 4174 ? 34.108  93.981  87.383  1.00 31.06  ? 4174 ASN A N     1 
ATOM   19651 C  CA    . ASN A 1 4174 ? 34.464  94.821  86.246  1.00 32.54  ? 4174 ASN A CA    1 
ATOM   19652 C  C     . ASN A 1 4174 ? 35.375  95.973  86.643  1.00 27.95  ? 4174 ASN A C     1 
ATOM   19653 O  O     . ASN A 1 4174 ? 36.175  96.428  85.819  1.00 26.73  ? 4174 ASN A O     1 
ATOM   19654 C  CB    . ASN A 1 4174 ? 33.201  95.365  85.577  1.00 34.94  ? 4174 ASN A CB    1 
ATOM   19655 C  CG    . ASN A 1 4174 ? 32.428  94.295  84.836  1.00 37.45  ? 4174 ASN A CG    1 
ATOM   19656 O  OD1   . ASN A 1 4174 ? 32.862  93.146  84.750  1.00 35.97  ? 4174 ASN A OD1   1 
ATOM   19657 N  ND2   . ASN A 1 4174 ? 31.274  94.666  84.294  1.00 37.34  ? 4174 ASN A ND2   1 
ATOM   19658 N  N     . GLU A 1 4175 ? 35.272  96.450  87.884  1.00 26.90  ? 4175 GLU A N     1 
ATOM   19659 C  CA    . GLU A 1 4175 ? 36.092  97.555  88.358  1.00 21.30  ? 4175 GLU A CA    1 
ATOM   19660 C  C     . GLU A 1 4175 ? 37.564  97.181  88.486  1.00 18.19  ? 4175 GLU A C     1 
ATOM   19661 O  O     . GLU A 1 4175 ? 38.417  98.078  88.444  1.00 18.41  ? 4175 GLU A O     1 
ATOM   19662 C  CB    . GLU A 1 4175 ? 35.559  98.048  89.708  1.00 20.95  ? 4175 GLU A CB    1 
ATOM   19663 C  CG    . GLU A 1 4175 ? 34.198  98.743  89.657  1.00 26.51  ? 4175 GLU A CG    1 
ATOM   19664 C  CD    . GLU A 1 4175 ? 33.039  97.792  89.403  1.00 33.61  ? 4175 GLU A CD    1 
ATOM   19665 O  OE1   . GLU A 1 4175 ? 33.263  96.564  89.356  1.00 37.07  ? 4175 GLU A OE1   1 
ATOM   19666 O  OE2   . GLU A 1 4175 ? 31.898  98.276  89.252  1.00 32.87  ? 4175 GLU A OE2   1 
ATOM   19667 N  N     . ARG A 1 4176 ? 37.874  95.883  88.602  1.00 15.85  ? 4176 ARG A N     1 
ATOM   19668 C  CA    . ARG A 1 4176 ? 39.248  95.434  88.812  1.00 13.80  ? 4176 ARG A CA    1 
ATOM   19669 C  C     . ARG A 1 4176 ? 40.210  96.046  87.807  1.00 12.64  ? 4176 ARG A C     1 
ATOM   19670 O  O     . ARG A 1 4176 ? 41.277  96.540  88.195  1.00 10.64  ? 4176 ARG A O     1 
ATOM   19671 C  CB    . ARG A 1 4176 ? 39.323  93.909  88.726  1.00 16.54  ? 4176 ARG A CB    1 
ATOM   19672 C  CG    . ARG A 1 4176 ? 40.715  93.347  88.979  1.00 19.83  ? 4176 ARG A CG    1 
ATOM   19673 C  CD    . ARG A 1 4176 ? 40.746  91.828  88.894  1.00 21.03  ? 4176 ARG A CD    1 
ATOM   19674 N  NE    . ARG A 1 4176 ? 39.642  91.201  89.609  1.00 33.83  ? 4176 ARG A NE    1 
ATOM   19675 C  CZ    . ARG A 1 4176 ? 39.778  90.519  90.738  1.00 27.74  ? 4176 ARG A CZ    1 
ATOM   19676 N  NH1   . ARG A 1 4176 ? 40.961  90.349  91.305  1.00 25.17  ? 4176 ARG A NH1   1 
ATOM   19677 N  NH2   . ARG A 1 4176 ? 38.701  89.991  91.311  1.00 28.04  ? 4176 ARG A NH2   1 
ATOM   19678 N  N     . ALA A 1 4177 ? 39.842  96.040  86.523  1.00 12.65  ? 4177 ALA A N     1 
ATOM   19679 C  CA    . ALA A 1 4177 ? 40.719  96.587  85.495  1.00 12.38  ? 4177 ALA A CA    1 
ATOM   19680 C  C     . ALA A 1 4177 ? 41.177  97.992  85.856  1.00 9.77   ? 4177 ALA A C     1 
ATOM   19681 O  O     . ALA A 1 4177 ? 42.381  98.278  85.847  1.00 9.72   ? 4177 ALA A O     1 
ATOM   19682 C  CB    . ALA A 1 4177 ? 40.009  96.584  84.141  1.00 13.25  ? 4177 ALA A CB    1 
ATOM   19683 N  N     . ARG A 1 4178 ? 40.236  98.862  86.241  1.00 6.99   ? 4178 ARG A N     1 
ATOM   19684 C  CA    . ARG A 1 4178 ? 40.615  100.227 86.585  1.00 7.30   ? 4178 ARG A CA    1 
ATOM   19685 C  C     . ARG A 1 4178 ? 41.650  100.233 87.699  1.00 7.50   ? 4178 ARG A C     1 
ATOM   19686 O  O     . ARG A 1 4178 ? 42.682  100.909 87.587  1.00 8.24   ? 4178 ARG A O     1 
ATOM   19687 C  CB    . ARG A 1 4178 ? 39.386  101.040 86.988  1.00 8.76   ? 4178 ARG A CB    1 
ATOM   19688 C  CG    . ARG A 1 4178 ? 39.634  102.542 87.009  1.00 9.83   ? 4178 ARG A CG    1 
ATOM   19689 C  CD    . ARG A 1 4178 ? 38.380  103.315 87.376  1.00 17.39  ? 4178 ARG A CD    1 
ATOM   19690 N  NE    . ARG A 1 4178 ? 37.450  103.425 86.259  1.00 22.16  ? 4178 ARG A NE    1 
ATOM   19691 C  CZ    . ARG A 1 4178 ? 37.452  104.415 85.376  1.00 21.04  ? 4178 ARG A CZ    1 
ATOM   19692 N  NH1   . ARG A 1 4178 ? 38.316  105.412 85.457  1.00 20.91  ? 4178 ARG A NH1   1 
ATOM   19693 N  NH2   . ARG A 1 4178 ? 36.561  104.405 84.389  1.00 29.18  ? 4178 ARG A NH2   1 
ATOM   19694 N  N     . LEU A 1 4179 ? 41.421  99.435  88.749  1.00 6.25   ? 4179 LEU A N     1 
ATOM   19695 C  CA    . LEU A 1 4179 ? 42.404  99.334  89.821  1.00 6.81   ? 4179 LEU A CA    1 
ATOM   19696 C  C     . LEU A 1 4179 ? 43.778  99.015  89.260  1.00 7.06   ? 4179 LEU A C     1 
ATOM   19697 O  O     . LEU A 1 4179 ? 44.750  99.733  89.534  1.00 8.64   ? 4179 LEU A O     1 
ATOM   19698 C  CB    . LEU A 1 4179 ? 41.985  98.267  90.833  1.00 7.94   ? 4179 LEU A CB    1 
ATOM   19699 C  CG    . LEU A 1 4179 ? 40.680  98.465  91.602  1.00 10.37  ? 4179 LEU A CG    1 
ATOM   19700 C  CD1   . LEU A 1 4179 ? 40.461  97.310  92.563  1.00 8.83   ? 4179 LEU A CD1   1 
ATOM   19701 C  CD2   . LEU A 1 4179 ? 40.697  99.784  92.345  1.00 7.65   ? 4179 LEU A CD2   1 
ATOM   19702 N  N     . TYR A 1 4180 ? 43.863  97.986  88.413  1.00 6.90   ? 4180 TYR A N     1 
ATOM   19703 C  CA    . TYR A 1 4180 ? 45.147  97.638  87.821  1.00 6.66   ? 4180 TYR A CA    1 
ATOM   19704 C  C     . TYR A 1 4180 ? 45.733  98.827  87.079  1.00 5.95   ? 4180 TYR A C     1 
ATOM   19705 O  O     . TYR A 1 4180 ? 46.892  99.198  87.313  1.00 7.08   ? 4180 TYR A O     1 
ATOM   19706 C  CB    . TYR A 1 4180 ? 44.993  96.435  86.892  1.00 8.78   ? 4180 TYR A CB    1 
ATOM   19707 C  CG    . TYR A 1 4180 ? 45.205  95.115  87.592  1.00 12.80  ? 4180 TYR A CG    1 
ATOM   19708 C  CD1   . TYR A 1 4180 ? 44.212  94.563  88.389  1.00 13.00  ? 4180 TYR A CD1   1 
ATOM   19709 C  CD2   . TYR A 1 4180 ? 46.401  94.423  87.460  1.00 13.83  ? 4180 TYR A CD2   1 
ATOM   19710 C  CE1   . TYR A 1 4180 ? 44.404  93.359  89.035  1.00 15.04  ? 4180 TYR A CE1   1 
ATOM   19711 C  CE2   . TYR A 1 4180 ? 46.602  93.218  88.100  1.00 16.87  ? 4180 TYR A CE2   1 
ATOM   19712 C  CZ    . TYR A 1 4180 ? 45.600  92.690  88.887  1.00 17.56  ? 4180 TYR A CZ    1 
ATOM   19713 O  OH    . TYR A 1 4180 ? 45.796  91.489  89.526  1.00 19.30  ? 4180 TYR A OH    1 
ATOM   19714 N  N     . PHE A 1 4181 ? 44.922  99.481  86.240  1.00 4.49   ? 4181 PHE A N     1 
ATOM   19715 C  CA    . PHE A 1 4181 ? 45.394  100.677 85.558  1.00 5.05   ? 4181 PHE A CA    1 
ATOM   19716 C  C     . PHE A 1 4181 ? 45.954  101.670 86.560  1.00 4.14   ? 4181 PHE A C     1 
ATOM   19717 O  O     . PHE A 1 4181 ? 47.100  102.119 86.428  1.00 3.73   ? 4181 PHE A O     1 
ATOM   19718 C  CB    . PHE A 1 4181 ? 44.261  101.310 84.751  1.00 5.15   ? 4181 PHE A CB    1 
ATOM   19719 C  CG    . PHE A 1 4181 ? 44.617  102.640 84.150  1.00 6.71   ? 4181 PHE A CG    1 
ATOM   19720 C  CD1   . PHE A 1 4181 ? 45.199  102.716 82.898  1.00 7.34   ? 4181 PHE A CD1   1 
ATOM   19721 C  CD2   . PHE A 1 4181 ? 44.373  103.816 84.842  1.00 6.28   ? 4181 PHE A CD2   1 
ATOM   19722 C  CE1   . PHE A 1 4181 ? 45.525  103.937 82.347  1.00 8.89   ? 4181 PHE A CE1   1 
ATOM   19723 C  CE2   . PHE A 1 4181 ? 44.703  105.038 84.298  1.00 6.27   ? 4181 PHE A CE2   1 
ATOM   19724 C  CZ    . PHE A 1 4181 ? 45.280  105.099 83.051  1.00 7.42   ? 4181 PHE A CZ    1 
ATOM   19725 N  N     . LEU A 1 4182 ? 45.181  101.964 87.610  1.00 3.85   ? 4182 LEU A N     1 
ATOM   19726 C  CA    . LEU A 1 4182 ? 45.658  102.875 88.639  1.00 4.14   ? 4182 LEU A CA    1 
ATOM   19727 C  C     . LEU A 1 4182 ? 47.009  102.420 89.162  1.00 3.50   ? 4182 LEU A C     1 
ATOM   19728 O  O     . LEU A 1 4182 ? 47.987  103.179 89.119  1.00 3.80   ? 4182 LEU A O     1 
ATOM   19729 C  CB    . LEU A 1 4182 ? 44.636  102.962 89.769  1.00 5.54   ? 4182 LEU A CB    1 
ATOM   19730 C  CG    . LEU A 1 4182 ? 43.355  103.744 89.473  1.00 11.27  ? 4182 LEU A CG    1 
ATOM   19731 C  CD1   . LEU A 1 4182 ? 42.286  103.436 90.510  1.00 9.39   ? 4182 LEU A CD1   1 
ATOM   19732 C  CD2   . LEU A 1 4182 ? 43.638  105.237 89.412  1.00 5.90   ? 4182 LEU A CD2   1 
ATOM   19733 N  N     . LEU A 1 4183 ? 47.100  101.148 89.565  1.00 3.71   ? 4183 LEU A N     1 
ATOM   19734 C  CA    . LEU A 1 4183 ? 48.369  100.614 90.038  1.00 3.13   ? 4183 LEU A CA    1 
ATOM   19735 C  C     . LEU A 1 4183 ? 49.467  100.873 89.023  1.00 3.05   ? 4183 LEU A C     1 
ATOM   19736 O  O     . LEU A 1 4183 ? 50.497  101.477 89.355  1.00 3.12   ? 4183 LEU A O     1 
ATOM   19737 C  CB    . LEU A 1 4183 ? 48.236  99.119  90.321  1.00 6.15   ? 4183 LEU A CB    1 
ATOM   19738 C  CG    . LEU A 1 4183 ? 49.460  98.429  90.921  1.00 6.33   ? 4183 LEU A CG    1 
ATOM   19739 C  CD1   . LEU A 1 4183 ? 49.999  99.216  92.102  1.00 5.80   ? 4183 LEU A CD1   1 
ATOM   19740 C  CD2   . LEU A 1 4183 ? 49.114  97.010  91.330  1.00 6.90   ? 4183 LEU A CD2   1 
ATOM   19741 N  N     . ALA A 1 4184 ? 49.223  100.504 87.760  1.00 3.03   ? 4184 ALA A N     1 
ATOM   19742 C  CA    . ALA A 1 4184 ? 50.228  100.725 86.731  1.00 3.27   ? 4184 ALA A CA    1 
ATOM   19743 C  C     . ALA A 1 4184 ? 50.663  102.179 86.720  1.00 2.82   ? 4184 ALA A C     1 
ATOM   19744 O  O     . ALA A 1 4184 ? 51.856  102.477 86.879  1.00 3.12   ? 4184 ALA A O     1 
ATOM   19745 C  CB    . ALA A 1 4184 ? 49.687  100.312 85.363  1.00 3.39   ? 4184 ALA A CB    1 
ATOM   19746 N  N     . TRP A 1 4185 ? 49.696  103.100 86.642  1.00 2.15   ? 4185 TRP A N     1 
ATOM   19747 C  CA    . TRP A 1 4185 ? 50.043  104.513 86.647  1.00 2.02   ? 4185 TRP A CA    1 
ATOM   19748 C  C     . TRP A 1 4185 ? 50.895  104.838 87.860  1.00 2.01   ? 4185 TRP A C     1 
ATOM   19749 O  O     . TRP A 1 4185 ? 52.027  105.322 87.719  1.00 2.22   ? 4185 TRP A O     1 
ATOM   19750 C  CB    . TRP A 1 4185 ? 48.778  105.371 86.624  1.00 2.75   ? 4185 TRP A CB    1 
ATOM   19751 C  CG    . TRP A 1 4185 ? 49.051  106.836 86.783  1.00 3.51   ? 4185 TRP A CG    1 
ATOM   19752 C  CD1   . TRP A 1 4185 ? 49.041  107.550 87.945  1.00 2.59   ? 4185 TRP A CD1   1 
ATOM   19753 C  CD2   . TRP A 1 4185 ? 49.388  107.764 85.746  1.00 3.41   ? 4185 TRP A CD2   1 
ATOM   19754 N  NE1   . TRP A 1 4185 ? 49.343  108.866 87.696  1.00 4.02   ? 4185 TRP A NE1   1 
ATOM   19755 C  CE2   . TRP A 1 4185 ? 49.561  109.024 86.353  1.00 4.07   ? 4185 TRP A CE2   1 
ATOM   19756 C  CE3   . TRP A 1 4185 ? 49.556  107.653 84.362  1.00 2.72   ? 4185 TRP A CE3   1 
ATOM   19757 C  CZ2   . TRP A 1 4185 ? 49.895  110.163 85.625  1.00 3.75   ? 4185 TRP A CZ2   1 
ATOM   19758 C  CZ3   . TRP A 1 4185 ? 49.888  108.785 83.642  1.00 4.56   ? 4185 TRP A CZ3   1 
ATOM   19759 C  CH2   . TRP A 1 4185 ? 50.054  110.024 84.274  1.00 4.25   ? 4185 TRP A CH2   1 
ATOM   19760 N  N     . PHE A 1 4186 ? 50.414  104.462 89.049  1.00 1.82   ? 4186 PHE A N     1 
ATOM   19761 C  CA    . PHE A 1 4186 ? 51.180  104.712 90.259  1.00 1.43   ? 4186 PHE A CA    1 
ATOM   19762 C  C     . PHE A 1 4186 ? 52.586  104.163 90.114  1.00 1.49   ? 4186 PHE A C     1 
ATOM   19763 O  O     . PHE A 1 4186 ? 53.567  104.915 90.214  1.00 1.98   ? 4186 PHE A O     1 
ATOM   19764 C  CB    . PHE A 1 4186 ? 50.464  104.091 91.460  1.00 1.88   ? 4186 PHE A CB    1 
ATOM   19765 C  CG    . PHE A 1 4186 ? 51.295  104.039 92.709  1.00 2.45   ? 4186 PHE A CG    1 
ATOM   19766 C  CD1   . PHE A 1 4186 ? 51.365  105.128 93.559  1.00 2.36   ? 4186 PHE A CD1   1 
ATOM   19767 C  CD2   . PHE A 1 4186 ? 51.993  102.888 93.042  1.00 2.23   ? 4186 PHE A CD2   1 
ATOM   19768 C  CE1   . PHE A 1 4186 ? 52.126  105.076 94.708  1.00 2.92   ? 4186 PHE A CE1   1 
ATOM   19769 C  CE2   . PHE A 1 4186 ? 52.755  102.832 94.188  1.00 2.29   ? 4186 PHE A CE2   1 
ATOM   19770 C  CZ    . PHE A 1 4186 ? 52.820  103.924 95.023  1.00 2.52   ? 4186 PHE A CZ    1 
ATOM   19771 N  N     . HIS A 1 4187 ? 52.697  102.883 89.748  1.00 2.05   ? 4187 HIS A N     1 
ATOM   19772 C  CA    . HIS A 1 4187 ? 54.013  102.277 89.620  1.00 2.20   ? 4187 HIS A CA    1 
ATOM   19773 C  C     . HIS A 1 4187 ? 54.867  103.077 88.653  1.00 2.41   ? 4187 HIS A C     1 
ATOM   19774 O  O     . HIS A 1 4187 ? 55.973  103.511 89.005  1.00 3.31   ? 4187 HIS A O     1 
ATOM   19775 C  CB    . HIS A 1 4187 ? 53.877  100.825 89.167  1.00 2.22   ? 4187 HIS A CB    1 
ATOM   19776 C  CG    . HIS A 1 4187 ? 55.177  100.087 89.090  1.00 3.49   ? 4187 HIS A CG    1 
ATOM   19777 N  ND1   . HIS A 1 4187 ? 55.813  99.579  90.201  1.00 4.13   ? 4187 HIS A ND1   1 
ATOM   19778 C  CD2   . HIS A 1 4187 ? 55.956  99.763  88.031  1.00 3.69   ? 4187 HIS A CD2   1 
ATOM   19779 C  CE1   . HIS A 1 4187 ? 56.930  98.979  89.832  1.00 5.53   ? 4187 HIS A CE1   1 
ATOM   19780 N  NE2   . HIS A 1 4187 ? 57.040  99.076  88.519  1.00 5.40   ? 4187 HIS A NE2   1 
ATOM   19781 N  N     . ALA A 1 4188 ? 54.319  103.377 87.470  1.00 1.58   ? 4188 ALA A N     1 
ATOM   19782 C  CA    . ALA A 1 4188 ? 55.081  104.137 86.491  1.00 1.88   ? 4188 ALA A CA    1 
ATOM   19783 C  C     . ALA A 1 4188 ? 55.584  105.430 87.105  1.00 2.72   ? 4188 ALA A C     1 
ATOM   19784 O  O     . ALA A 1 4188 ? 56.798  105.681 87.132  1.00 2.58   ? 4188 ALA A O     1 
ATOM   19785 C  CB    . ALA A 1 4188 ? 54.228  104.418 85.254  1.00 2.85   ? 4188 ALA A CB    1 
ATOM   19786 N  N     . ILE A 1 4189 ? 54.676  106.203 87.711  1.00 2.43   ? 4189 ILE A N     1 
ATOM   19787 C  CA    . ILE A 1 4189 ? 55.073  107.485 88.278  1.00 2.37   ? 4189 ILE A CA    1 
ATOM   19788 C  C     . ILE A 1 4189 ? 56.203  107.272 89.266  1.00 2.94   ? 4189 ILE A C     1 
ATOM   19789 O  O     . ILE A 1 4189 ? 57.264  107.905 89.167  1.00 3.52   ? 4189 ILE A O     1 
ATOM   19790 C  CB    . ILE A 1 4189 ? 53.869  108.185 88.935  1.00 2.62   ? 4189 ILE A CB    1 
ATOM   19791 C  CG1   . ILE A 1 4189 ? 52.751  108.416 87.914  1.00 2.84   ? 4189 ILE A CG1   1 
ATOM   19792 C  CG2   . ILE A 1 4189 ? 54.297  109.503 89.563  1.00 3.97   ? 4189 ILE A CG2   1 
ATOM   19793 C  CD1   . ILE A 1 4189 ? 53.216  109.023 86.610  1.00 3.12   ? 4189 ILE A CD1   1 
ATOM   19794 N  N     . ILE A 1 4190 ? 56.035  106.297 90.162  1.00 2.53   ? 4190 ILE A N     1 
ATOM   19795 C  CA    . ILE A 1 4190 ? 57.046  106.056 91.182  1.00 3.05   ? 4190 ILE A CA    1 
ATOM   19796 C  C     . ILE A 1 4190 ? 58.383  105.768 90.521  1.00 3.67   ? 4190 ILE A C     1 
ATOM   19797 O  O     . ILE A 1 4190 ? 59.390  106.430 90.805  1.00 5.08   ? 4190 ILE A O     1 
ATOM   19798 C  CB    . ILE A 1 4190 ? 56.601  104.910 92.110  1.00 2.92   ? 4190 ILE A CB    1 
ATOM   19799 C  CG1   . ILE A 1 4190 ? 55.319  105.285 92.858  1.00 2.48   ? 4190 ILE A CG1   1 
ATOM   19800 C  CG2   . ILE A 1 4190 ? 57.686  104.578 93.102  1.00 4.04   ? 4190 ILE A CG2   1 
ATOM   19801 C  CD1   . ILE A 1 4190 ? 55.284  106.706 93.363  1.00 3.06   ? 4190 ILE A CD1   1 
ATOM   19802 N  N     . GLN A 1 4191 ? 58.392  104.842 89.557  1.00 3.56   ? 4191 GLN A N     1 
ATOM   19803 C  CA    . GLN A 1 4191 ? 59.648  104.498 88.905  1.00 5.01   ? 4191 GLN A CA    1 
ATOM   19804 C  C     . GLN A 1 4191 ? 60.207  105.697 88.159  1.00 5.15   ? 4191 GLN A C     1 
ATOM   19805 O  O     . GLN A 1 4191 ? 61.418  105.950 88.193  1.00 6.68   ? 4191 GLN A O     1 
ATOM   19806 C  CB    . GLN A 1 4191 ? 59.451  103.311 87.964  1.00 7.27   ? 4191 GLN A CB    1 
ATOM   19807 C  CG    . GLN A 1 4191 ? 59.318  101.979 88.685  1.00 6.97   ? 4191 GLN A CG    1 
ATOM   19808 C  CD    . GLN A 1 4191 ? 59.673  100.797 87.806  1.00 13.16  ? 4191 GLN A CD    1 
ATOM   19809 O  OE1   . GLN A 1 4191 ? 59.106  100.614 86.730  1.00 17.02  ? 4191 GLN A OE1   1 
ATOM   19810 N  NE2   . GLN A 1 4191 ? 60.617  99.983  88.265  1.00 13.60  ? 4191 GLN A NE2   1 
ATOM   19811 N  N     . GLU A 1 4192 ? 59.332  106.477 87.521  1.00 5.41   ? 4192 GLU A N     1 
ATOM   19812 C  CA    . GLU A 1 4192 ? 59.820  107.603 86.740  1.00 5.96   ? 4192 GLU A CA    1 
ATOM   19813 C  C     . GLU A 1 4192 ? 60.366  108.703 87.637  1.00 6.33   ? 4192 GLU A C     1 
ATOM   19814 O  O     . GLU A 1 4192 ? 61.088  109.585 87.160  1.00 11.19  ? 4192 GLU A O     1 
ATOM   19815 C  CB    . GLU A 1 4192 ? 58.713  108.133 85.833  1.00 5.19   ? 4192 GLU A CB    1 
ATOM   19816 C  CG    . GLU A 1 4192 ? 58.625  107.412 84.499  1.00 6.79   ? 4192 GLU A CG    1 
ATOM   19817 C  CD    . GLU A 1 4192 ? 59.782  107.746 83.580  1.00 21.70  ? 4192 GLU A CD    1 
ATOM   19818 O  OE1   . GLU A 1 4192 ? 59.905  108.923 83.181  1.00 25.71  ? 4192 GLU A OE1   1 
ATOM   19819 O  OE2   . GLU A 1 4192 ? 60.570  106.833 83.257  1.00 20.81  ? 4192 GLU A OE2   1 
ATOM   19820 N  N     . ARG A 1 4193 ? 60.051  108.664 88.934  1.00 5.18   ? 4193 ARG A N     1 
ATOM   19821 C  CA    . ARG A 1 4193 ? 60.631  109.655 89.828  1.00 5.53   ? 4193 ARG A CA    1 
ATOM   19822 C  C     . ARG A 1 4193 ? 62.045  109.276 90.250  1.00 8.70   ? 4193 ARG A C     1 
ATOM   19823 O  O     . ARG A 1 4193 ? 62.747  110.106 90.835  1.00 9.31   ? 4193 ARG A O     1 
ATOM   19824 C  CB    . ARG A 1 4193 ? 59.728  109.859 91.046  1.00 4.88   ? 4193 ARG A CB    1 
ATOM   19825 C  CG    . ARG A 1 4193 ? 58.427  110.580 90.705  1.00 5.12   ? 4193 ARG A CG    1 
ATOM   19826 C  CD    . ARG A 1 4193 ? 57.681  111.066 91.938  1.00 5.13   ? 4193 ARG A CD    1 
ATOM   19827 N  NE    . ARG A 1 4193 ? 58.481  111.982 92.741  1.00 6.75   ? 4193 ARG A NE    1 
ATOM   19828 C  CZ    . ARG A 1 4193 ? 58.166  113.250 92.966  1.00 4.59   ? 4193 ARG A CZ    1 
ATOM   19829 N  NH1   . ARG A 1 4193 ? 57.071  113.792 92.457  1.00 3.69   ? 4193 ARG A NH1   1 
ATOM   19830 N  NH2   . ARG A 1 4193 ? 58.970  113.995 93.718  1.00 6.26   ? 4193 ARG A NH2   1 
ATOM   19831 N  N     . LEU A 1 4194 ? 62.480  108.046 89.956  1.00 8.27   ? 4194 LEU A N     1 
ATOM   19832 C  CA    . LEU A 1 4194 ? 63.848  107.652 90.277  1.00 8.84   ? 4194 LEU A CA    1 
ATOM   19833 C  C     . LEU A 1 4194 ? 64.862  108.295 89.339  1.00 10.61  ? 4194 LEU A C     1 
ATOM   19834 O  O     . LEU A 1 4194 ? 66.004  108.542 89.743  1.00 12.79  ? 4194 LEU A O     1 
ATOM   19835 C  CB    . LEU A 1 4194 ? 63.983  106.130 90.237  1.00 10.13  ? 4194 LEU A CB    1 
ATOM   19836 C  CG    . LEU A 1 4194 ? 63.068  105.350 91.182  1.00 11.00  ? 4194 LEU A CG    1 
ATOM   19837 C  CD1   . LEU A 1 4194 ? 63.215  103.855 90.962  1.00 12.05  ? 4194 LEU A CD1   1 
ATOM   19838 C  CD2   . LEU A 1 4194 ? 63.377  105.712 92.625  1.00 10.17  ? 4194 LEU A CD2   1 
ATOM   19839 N  N     . ARG A 1 4195 ? 64.470  108.576 88.094  1.00 11.65  ? 4195 ARG A N     1 
ATOM   19840 C  CA    . ARG A 1 4195 ? 65.404  109.165 87.137  1.00 15.20  ? 4195 ARG A CA    1 
ATOM   19841 C  C     . ARG A 1 4195 ? 65.904  110.518 87.622  1.00 14.89  ? 4195 ARG A C     1 
ATOM   19842 O  O     . ARG A 1 4195 ? 67.088  110.844 87.476  1.00 21.63  ? 4195 ARG A O     1 
ATOM   19843 C  CB    . ARG A 1 4195 ? 64.739  109.297 85.769  1.00 13.50  ? 4195 ARG A CB    1 
ATOM   19844 C  CG    . ARG A 1 4195 ? 64.339  107.971 85.153  1.00 20.61  ? 4195 ARG A CG    1 
ATOM   19845 C  CD    . ARG A 1 4195 ? 63.608  108.166 83.833  1.00 22.38  ? 4195 ARG A CD    1 
ATOM   19846 N  NE    . ARG A 1 4195 ? 63.429  106.916 83.100  1.00 28.45  ? 4195 ARG A NE    1 
ATOM   19847 C  CZ    . ARG A 1 4195 ? 64.413  106.158 82.633  1.00 24.19  ? 4195 ARG A CZ    1 
ATOM   19848 N  NH1   . ARG A 1 4195 ? 65.681  106.515 82.752  1.00 23.58  ? 4195 ARG A NH1   1 
ATOM   19849 N  NH2   . ARG A 1 4195 ? 64.115  105.017 82.019  1.00 22.58  ? 4195 ARG A NH2   1 
ATOM   19850 N  N     . TYR A 1 4196 ? 65.014  111.319 88.200  1.00 14.44  ? 4196 TYR A N     1 
ATOM   19851 C  CA    . TYR A 1 4196 ? 65.391  112.577 88.839  1.00 13.23  ? 4196 TYR A CA    1 
ATOM   19852 C  C     . TYR A 1 4196 ? 65.849  112.292 90.270  1.00 19.38  ? 4196 TYR A C     1 
ATOM   19853 O  O     . TYR A 1 4196 ? 65.159  112.562 91.253  1.00 14.77  ? 4196 TYR A O     1 
ATOM   19854 C  CB    . TYR A 1 4196 ? 64.227  113.561 88.790  1.00 10.73  ? 4196 TYR A CB    1 
ATOM   19855 C  CG    . TYR A 1 4196 ? 63.539  113.604 87.439  1.00 12.78  ? 4196 TYR A CG    1 
ATOM   19856 C  CD1   . TYR A 1 4196 ? 62.589  112.651 87.087  1.00 10.91  ? 4196 TYR A CD1   1 
ATOM   19857 C  CD2   . TYR A 1 4196 ? 63.862  114.577 86.506  1.00 13.67  ? 4196 TYR A CD2   1 
ATOM   19858 C  CE1   . TYR A 1 4196 ? 61.972  112.677 85.853  1.00 11.38  ? 4196 TYR A CE1   1 
ATOM   19859 C  CE2   . TYR A 1 4196 ? 63.247  114.611 85.270  1.00 16.98  ? 4196 TYR A CE2   1 
ATOM   19860 C  CZ    . TYR A 1 4196 ? 62.303  113.660 84.948  1.00 15.82  ? 4196 TYR A CZ    1 
ATOM   19861 O  OH    . TYR A 1 4196 ? 61.688  113.690 83.718  1.00 15.66  ? 4196 TYR A OH    1 
ATOM   19862 N  N     . ALA A 1 4197 ? 67.055  111.732 90.351  1.00 28.32  ? 4197 ALA A N     1 
ATOM   19863 C  CA    . ALA A 1 4197 ? 67.495  111.019 91.548  1.00 23.63  ? 4197 ALA A CA    1 
ATOM   19864 C  C     . ALA A 1 4197 ? 67.399  111.816 92.845  1.00 24.00  ? 4197 ALA A C     1 
ATOM   19865 O  O     . ALA A 1 4197 ? 66.949  111.239 93.848  1.00 26.40  ? 4197 ALA A O     1 
ATOM   19866 C  CB    . ALA A 1 4197 ? 68.928  110.503 91.336  1.00 26.41  ? 4197 ALA A CB    1 
ATOM   19867 N  N     . PRO A 1 4198 ? 67.804  113.090 92.924  1.00 26.17  ? 4198 PRO A N     1 
ATOM   19868 C  CA    . PRO A 1 4198 ? 67.653  113.790 94.212  1.00 18.96  ? 4198 PRO A CA    1 
ATOM   19869 C  C     . PRO A 1 4198 ? 66.264  114.363 94.431  1.00 16.02  ? 4198 PRO A C     1 
ATOM   19870 O  O     . PRO A 1 4198 ? 65.841  114.517 95.583  1.00 16.18  ? 4198 PRO A O     1 
ATOM   19871 C  CB    . PRO A 1 4198 ? 68.713  114.897 94.135  1.00 18.80  ? 4198 PRO A CB    1 
ATOM   19872 C  CG    . PRO A 1 4198 ? 68.864  115.156 92.688  1.00 29.18  ? 4198 PRO A CG    1 
ATOM   19873 C  CD    . PRO A 1 4198 ? 68.680  113.837 92.002  1.00 26.64  ? 4198 PRO A CD    1 
ATOM   19874 N  N     . LEU A 1 4199 ? 65.538  114.682 93.359  1.00 17.48  ? 4199 LEU A N     1 
ATOM   19875 C  CA    . LEU A 1 4199 ? 64.288  115.423 93.485  1.00 15.32  ? 4199 LEU A CA    1 
ATOM   19876 C  C     . LEU A 1 4199 ? 63.058  114.522 93.510  1.00 13.03  ? 4199 LEU A C     1 
ATOM   19877 O  O     . LEU A 1 4199 ? 62.159  114.735 94.331  1.00 9.82   ? 4199 LEU A O     1 
ATOM   19878 C  CB    . LEU A 1 4199 ? 64.166  116.437 92.345  1.00 14.09  ? 4199 LEU A CB    1 
ATOM   19879 C  CG    . LEU A 1 4199 ? 63.360  117.698 92.660  1.00 13.19  ? 4199 LEU A CG    1 
ATOM   19880 C  CD1   . LEU A 1 4199 ? 63.902  118.380 93.904  1.00 16.12  ? 4199 LEU A CD1   1 
ATOM   19881 C  CD2   . LEU A 1 4199 ? 63.371  118.653 91.480  1.00 13.29  ? 4199 LEU A CD2   1 
ATOM   19882 N  N     . GLY A 1 4200 ? 62.988  113.529 92.621  1.00 9.43   ? 4200 GLY A N     1 
ATOM   19883 C  CA    . GLY A 1 4200 ? 61.840  112.636 92.617  1.00 6.77   ? 4200 GLY A CA    1 
ATOM   19884 C  C     . GLY A 1 4200 ? 61.702  111.864 93.915  1.00 7.74   ? 4200 GLY A C     1 
ATOM   19885 O  O     . GLY A 1 4200 ? 60.600  111.711 94.446  1.00 6.78   ? 4200 GLY A O     1 
ATOM   19886 N  N     . TRP A 1 4201 ? 62.818  111.362 94.435  1.00 7.99   ? 4201 TRP A N     1 
ATOM   19887 C  CA    . TRP A 1 4201 ? 62.887  110.799 95.773  1.00 9.06   ? 4201 TRP A CA    1 
ATOM   19888 C  C     . TRP A 1 4201 ? 64.177  111.276 96.420  1.00 11.41  ? 4201 TRP A C     1 
ATOM   19889 O  O     . TRP A 1 4201 ? 65.139  111.615 95.730  1.00 17.30  ? 4201 TRP A O     1 
ATOM   19890 C  CB    . TRP A 1 4201 ? 62.833  109.264 95.759  1.00 9.76   ? 4201 TRP A CB    1 
ATOM   19891 C  CG    . TRP A 1 4201 ? 61.584  108.713 95.150  1.00 5.85   ? 4201 TRP A CG    1 
ATOM   19892 C  CD1   . TRP A 1 4201 ? 61.396  108.354 93.848  1.00 5.82   ? 4201 TRP A CD1   1 
ATOM   19893 C  CD2   . TRP A 1 4201 ? 60.344  108.463 95.819  1.00 5.78   ? 4201 TRP A CD2   1 
ATOM   19894 N  NE1   . TRP A 1 4201 ? 60.116  107.892 93.665  1.00 4.57   ? 4201 TRP A NE1   1 
ATOM   19895 C  CE2   . TRP A 1 4201 ? 59.449  107.950 94.861  1.00 5.61   ? 4201 TRP A CE2   1 
ATOM   19896 C  CE3   . TRP A 1 4201 ? 59.904  108.622 97.137  1.00 5.52   ? 4201 TRP A CE3   1 
ATOM   19897 C  CZ2   . TRP A 1 4201 ? 58.141  107.594 95.177  1.00 5.07   ? 4201 TRP A CZ2   1 
ATOM   19898 C  CZ3   . TRP A 1 4201 ? 58.605  108.269 97.448  1.00 6.31   ? 4201 TRP A CZ3   1 
ATOM   19899 C  CH2   . TRP A 1 4201 ? 57.738  107.761 96.473  1.00 6.21   ? 4201 TRP A CH2   1 
ATOM   19900 N  N     . SER A 1 4202 ? 64.185  111.322 97.752  1.00 11.70  ? 4202 SER A N     1 
ATOM   19901 C  CA    . SER A 1 4202 ? 65.402  111.718 98.453  1.00 13.85  ? 4202 SER A CA    1 
ATOM   19902 C  C     . SER A 1 4202 ? 66.513  110.697 98.255  1.00 14.35  ? 4202 SER A C     1 
ATOM   19903 O  O     . SER A 1 4202 ? 67.697  111.044 98.326  1.00 24.05  ? 4202 SER A O     1 
ATOM   19904 C  CB    . SER A 1 4202 ? 65.118  111.911 99.942  1.00 15.77  ? 4202 SER A CB    1 
ATOM   19905 O  OG    . SER A 1 4202 ? 64.956  110.665 100.595 1.00 19.54  ? 4202 SER A OG    1 
ATOM   19906 N  N     . LYS A 1 4203 ? 66.154  109.440 98.003  1.00 14.86  ? 4203 LYS A N     1 
ATOM   19907 C  CA    . LYS A 1 4203 ? 67.121  108.366 97.849  1.00 15.51  ? 4203 LYS A CA    1 
ATOM   19908 C  C     . LYS A 1 4203 ? 66.701  107.487 96.680  1.00 15.74  ? 4203 LYS A C     1 
ATOM   19909 O  O     . LYS A 1 4203 ? 65.518  107.404 96.341  1.00 17.41  ? 4203 LYS A O     1 
ATOM   19910 C  CB    . LYS A 1 4203 ? 67.232  107.541 99.142  1.00 18.16  ? 4203 LYS A CB    1 
ATOM   19911 C  CG    . LYS A 1 4203 ? 68.310  106.471 99.138  1.00 25.29  ? 4203 LYS A CG    1 
ATOM   19912 C  CD    . LYS A 1 4203 ? 68.290  105.676 100.434 1.00 30.63  ? 4203 LYS A CD    1 
ATOM   19913 C  CE    . LYS A 1 4203 ? 68.852  106.496 101.586 1.00 34.17  ? 4203 LYS A CE    1 
ATOM   19914 N  NZ    . LYS A 1 4203 ? 68.953  105.704 102.842 1.00 32.33  ? 4203 LYS A NZ    1 
ATOM   19915 N  N     . LYS A 1 4204 ? 67.682  106.839 96.058  1.00 16.26  ? 4204 LYS A N     1 
ATOM   19916 C  CA    . LYS A 1 4204 ? 67.412  105.904 94.973  1.00 20.24  ? 4204 LYS A CA    1 
ATOM   19917 C  C     . LYS A 1 4204 ? 66.916  104.585 95.553  1.00 20.24  ? 4204 LYS A C     1 
ATOM   19918 O  O     . LYS A 1 4204 ? 67.713  103.773 96.034  1.00 26.68  ? 4204 LYS A O     1 
ATOM   19919 C  CB    . LYS A 1 4204 ? 68.667  105.684 94.132  1.00 23.74  ? 4204 LYS A CB    1 
ATOM   19920 C  CG    . LYS A 1 4204 ? 68.500  104.677 92.999  1.00 32.19  ? 4204 LYS A CG    1 
ATOM   19921 C  CD    . LYS A 1 4204 ? 67.339  105.026 92.082  1.00 31.10  ? 4204 LYS A CD    1 
ATOM   19922 C  CE    . LYS A 1 4204 ? 67.522  106.396 91.452  1.00 29.76  ? 4204 LYS A CE    1 
ATOM   19923 N  NZ    . LYS A 1 4204 ? 68.701  106.436 90.545  1.00 32.23  ? 4204 LYS A NZ    1 
ATOM   19924 N  N     . TYR A 1 4205 ? 65.604  104.371 95.508  1.00 17.14  ? 4205 TYR A N     1 
ATOM   19925 C  CA    . TYR A 1 4205 ? 65.001  103.141 95.992  1.00 16.20  ? 4205 TYR A CA    1 
ATOM   19926 C  C     . TYR A 1 4205 ? 64.797  102.188 94.825  1.00 16.62  ? 4205 TYR A C     1 
ATOM   19927 O  O     . TYR A 1 4205 ? 64.692  102.608 93.669  1.00 22.43  ? 4205 TYR A O     1 
ATOM   19928 C  CB    . TYR A 1 4205 ? 63.659  103.395 96.679  1.00 11.89  ? 4205 TYR A CB    1 
ATOM   19929 C  CG    . TYR A 1 4205 ? 63.742  104.327 97.859  1.00 11.22  ? 4205 TYR A CG    1 
ATOM   19930 C  CD1   . TYR A 1 4205 ? 64.170  103.876 99.101  1.00 10.53  ? 4205 TYR A CD1   1 
ATOM   19931 C  CD2   . TYR A 1 4205 ? 63.364  105.654 97.738  1.00 11.26  ? 4205 TYR A CD2   1 
ATOM   19932 C  CE1   . TYR A 1 4205 ? 64.238  104.731 100.184 1.00 11.59  ? 4205 TYR A CE1   1 
ATOM   19933 C  CE2   . TYR A 1 4205 ? 63.426  106.511 98.810  1.00 12.62  ? 4205 TYR A CE2   1 
ATOM   19934 C  CZ    . TYR A 1 4205 ? 63.862  106.049 100.032 1.00 16.27  ? 4205 TYR A CZ    1 
ATOM   19935 O  OH    . TYR A 1 4205 ? 63.923  106.910 101.102 1.00 17.96  ? 4205 TYR A OH    1 
ATOM   19936 N  N     . GLU A 1 4206 ? 64.745  100.898 95.134  1.00 19.16  ? 4206 GLU A N     1 
ATOM   19937 C  CA    . GLU A 1 4206 ? 64.624  99.875  94.100  1.00 19.80  ? 4206 GLU A CA    1 
ATOM   19938 C  C     . GLU A 1 4206 ? 63.167  99.444  93.930  1.00 16.05  ? 4206 GLU A C     1 
ATOM   19939 O  O     . GLU A 1 4206 ? 62.806  98.280  94.105  1.00 19.64  ? 4206 GLU A O     1 
ATOM   19940 C  CB    . GLU A 1 4206 ? 65.526  98.689  94.423  1.00 18.39  ? 4206 GLU A CB    1 
ATOM   19941 C  CG    . GLU A 1 4206 ? 67.003  99.035  94.376  1.00 22.23  ? 4206 GLU A CG    1 
ATOM   19942 C  CD    . GLU A 1 4206 ? 67.473  99.389  92.980  1.00 42.89  ? 4206 GLU A CD    1 
ATOM   19943 O  OE1   . GLU A 1 4206 ? 66.920  98.840  92.008  1.00 46.99  ? 4206 GLU A OE1   1 
ATOM   19944 O  OE2   . GLU A 1 4206 ? 68.396  100.220 92.855  1.00 50.43  ? 4206 GLU A OE2   1 
ATOM   19945 N  N     . PHE A 1 4207 ? 62.323  100.416 93.587  1.00 12.68  ? 4207 PHE A N     1 
ATOM   19946 C  CA    . PHE A 1 4207 ? 60.952  100.118 93.191  1.00 12.05  ? 4207 PHE A CA    1 
ATOM   19947 C  C     . PHE A 1 4207 ? 60.969  99.283  91.919  1.00 13.76  ? 4207 PHE A C     1 
ATOM   19948 O  O     . PHE A 1 4207 ? 61.329  99.785  90.850  1.00 14.84  ? 4207 PHE A O     1 
ATOM   19949 C  CB    . PHE A 1 4207 ? 60.153  101.403 92.966  1.00 8.25   ? 4207 PHE A CB    1 
ATOM   19950 C  CG    . PHE A 1 4207 ? 60.148  102.338 94.140  1.00 8.69   ? 4207 PHE A CG    1 
ATOM   19951 C  CD1   . PHE A 1 4207 ? 59.512  101.991 95.320  1.00 9.39   ? 4207 PHE A CD1   1 
ATOM   19952 C  CD2   . PHE A 1 4207 ? 60.772  103.573 94.059  1.00 8.76   ? 4207 PHE A CD2   1 
ATOM   19953 C  CE1   . PHE A 1 4207 ? 59.498  102.856 96.395  1.00 8.06   ? 4207 PHE A CE1   1 
ATOM   19954 C  CE2   . PHE A 1 4207 ? 60.758  104.444 95.129  1.00 7.85   ? 4207 PHE A CE2   1 
ATOM   19955 C  CZ    . PHE A 1 4207 ? 60.124  104.085 96.300  1.00 8.87   ? 4207 PHE A CZ    1 
ATOM   19956 N  N     . GLY A 1 4208 ? 60.582  98.015  92.014  1.00 9.84   ? 4208 GLY A N     1 
ATOM   19957 C  CA    . GLY A 1 4208 ? 60.710  97.131  90.874  1.00 8.72   ? 4208 GLY A CA    1 
ATOM   19958 C  C     . GLY A 1 4208 ? 59.532  96.213  90.631  1.00 8.07   ? 4208 GLY A C     1 
ATOM   19959 O  O     . GLY A 1 4208 ? 58.414  96.482  91.079  1.00 11.22  ? 4208 GLY A O     1 
ATOM   19960 N  N     . GLU A 1 4209 ? 59.785  95.116  89.914  1.00 10.37  ? 4209 GLU A N     1 
ATOM   19961 C  CA    . GLU A 1 4209 ? 58.711  94.204  89.537  1.00 12.13  ? 4209 GLU A CA    1 
ATOM   19962 C  C     . GLU A 1 4209 ? 58.145  93.462  90.740  1.00 11.02  ? 4209 GLU A C     1 
ATOM   19963 O  O     . GLU A 1 4209 ? 56.953  93.138  90.758  1.00 10.47  ? 4209 GLU A O     1 
ATOM   19964 C  CB    . GLU A 1 4209 ? 59.215  93.214  88.485  1.00 14.65  ? 4209 GLU A CB    1 
ATOM   19965 C  CG    . GLU A 1 4209 ? 58.160  92.246  87.973  1.00 20.60  ? 4209 GLU A CG    1 
ATOM   19966 C  CD    . GLU A 1 4209 ? 57.042  92.941  87.217  1.00 25.68  ? 4209 GLU A CD    1 
ATOM   19967 O  OE1   . GLU A 1 4209 ? 57.283  94.030  86.655  1.00 24.87  ? 4209 GLU A OE1   1 
ATOM   19968 O  OE2   . GLU A 1 4209 ? 55.918  92.397  87.186  1.00 26.96  ? 4209 GLU A OE2   1 
ATOM   19969 N  N     . SER A 1 4210 ? 58.976  93.175  91.746  1.00 10.91  ? 4210 SER A N     1 
ATOM   19970 C  CA    . SER A 1 4210 ? 58.480  92.488  92.934  1.00 10.90  ? 4210 SER A CA    1 
ATOM   19971 C  C     . SER A 1 4210 ? 57.437  93.327  93.661  1.00 9.82   ? 4210 SER A C     1 
ATOM   19972 O  O     . SER A 1 4210 ? 56.410  92.803  94.112  1.00 10.49  ? 4210 SER A O     1 
ATOM   19973 C  CB    . SER A 1 4210 ? 59.642  92.143  93.866  1.00 11.23  ? 4210 SER A CB    1 
ATOM   19974 O  OG    . SER A 1 4210 ? 60.263  93.313  94.365  1.00 14.64  ? 4210 SER A OG    1 
ATOM   19975 N  N     . ASP A 1 4211 ? 57.678  94.636  93.777  1.00 9.91   ? 4211 ASP A N     1 
ATOM   19976 C  CA    . ASP A 1 4211 ? 56.701  95.520  94.404  1.00 9.03   ? 4211 ASP A CA    1 
ATOM   19977 C  C     . ASP A 1 4211 ? 55.397  95.546  93.617  1.00 7.21   ? 4211 ASP A C     1 
ATOM   19978 O  O     . ASP A 1 4211 ? 54.309  95.502  94.202  1.00 5.88   ? 4211 ASP A O     1 
ATOM   19979 C  CB    . ASP A 1 4211 ? 57.276  96.931  94.533  1.00 8.37   ? 4211 ASP A CB    1 
ATOM   19980 C  CG    . ASP A 1 4211 ? 58.367  97.023  95.579  1.00 14.28  ? 4211 ASP A CG    1 
ATOM   19981 O  OD1   . ASP A 1 4211 ? 58.649  96.002  96.239  1.00 19.86  ? 4211 ASP A OD1   1 
ATOM   19982 O  OD2   . ASP A 1 4211 ? 58.945  98.118  95.742  1.00 18.17  ? 4211 ASP A OD2   1 
ATOM   19983 N  N     . LEU A 1 4212 ? 55.488  95.617  92.288  1.00 7.10   ? 4212 LEU A N     1 
ATOM   19984 C  CA    . LEU A 1 4212 ? 54.285  95.634  91.462  1.00 6.19   ? 4212 LEU A CA    1 
ATOM   19985 C  C     . LEU A 1 4212 ? 53.503  94.333  91.595  1.00 6.67   ? 4212 LEU A C     1 
ATOM   19986 O  O     . LEU A 1 4212 ? 52.271  94.349  91.690  1.00 5.17   ? 4212 LEU A O     1 
ATOM   19987 C  CB    . LEU A 1 4212 ? 54.660  95.895  90.004  1.00 6.17   ? 4212 LEU A CB    1 
ATOM   19988 C  CG    . LEU A 1 4212 ? 53.519  95.918  88.988  1.00 7.19   ? 4212 LEU A CG    1 
ATOM   19989 C  CD1   . LEU A 1 4212 ? 52.540  97.033  89.310  1.00 6.28   ? 4212 LEU A CD1   1 
ATOM   19990 C  CD2   . LEU A 1 4212 ? 54.063  96.067  87.578  1.00 8.40   ? 4212 LEU A CD2   1 
ATOM   19991 N  N     . ARG A 1 4213 ? 54.202  93.196  91.608  1.00 8.09   ? 4213 ARG A N     1 
ATOM   19992 C  CA    . ARG A 1 4213 ? 53.528  91.911  91.765  1.00 8.33   ? 4213 ARG A CA    1 
ATOM   19993 C  C     . ARG A 1 4213 ? 52.865  91.796  93.132  1.00 8.88   ? 4213 ARG A C     1 
ATOM   19994 O  O     . ARG A 1 4213 ? 51.737  91.301  93.240  1.00 11.02  ? 4213 ARG A O     1 
ATOM   19995 C  CB    . ARG A 1 4213 ? 54.519  90.767  91.551  1.00 11.40  ? 4213 ARG A CB    1 
ATOM   19996 C  CG    . ARG A 1 4213 ? 55.000  90.624  90.118  1.00 12.79  ? 4213 ARG A CG    1 
ATOM   19997 C  CD    . ARG A 1 4213 ? 55.884  89.398  89.954  1.00 24.13  ? 4213 ARG A CD    1 
ATOM   19998 N  NE    . ARG A 1 4213 ? 57.301  89.733  90.016  1.00 23.80  ? 4213 ARG A NE    1 
ATOM   19999 C  CZ    . ARG A 1 4213 ? 58.109  89.392  91.010  1.00 25.96  ? 4213 ARG A CZ    1 
ATOM   20000 N  NH1   . ARG A 1 4213 ? 57.672  88.702  92.051  1.00 21.99  ? 4213 ARG A NH1   1 
ATOM   20001 N  NH2   . ARG A 1 4213 ? 59.389  89.751  90.959  1.00 27.01  ? 4213 ARG A NH2   1 
ATOM   20002 N  N     . SER A 1 4214 ? 53.549  92.247  94.188  1.00 6.98   ? 4214 SER A N     1 
ATOM   20003 C  CA    . SER A 1 4214 ? 52.951  92.217  95.518  1.00 5.97   ? 4214 SER A CA    1 
ATOM   20004 C  C     . SER A 1 4214 ? 51.717  93.107  95.585  1.00 5.93   ? 4214 SER A C     1 
ATOM   20005 O  O     . SER A 1 4214 ? 50.703  92.734  96.189  1.00 7.48   ? 4214 SER A O     1 
ATOM   20006 C  CB    . SER A 1 4214 ? 53.980  92.643  96.566  1.00 8.54   ? 4214 SER A CB    1 
ATOM   20007 O  OG    . SER A 1 4214 ? 55.076  91.746  96.598  1.00 13.76  ? 4214 SER A OG    1 
ATOM   20008 N  N     . ALA A 1 4215 ? 51.784  94.291  94.972  1.00 5.92   ? 4215 ALA A N     1 
ATOM   20009 C  CA    . ALA A 1 4215 ? 50.627  95.179  94.948  1.00 6.61   ? 4215 ALA A CA    1 
ATOM   20010 C  C     . ALA A 1 4215 ? 49.468  94.555  94.180  1.00 6.07   ? 4215 ALA A C     1 
ATOM   20011 O  O     . ALA A 1 4215 ? 48.308  94.679  94.587  1.00 7.20   ? 4215 ALA A O     1 
ATOM   20012 C  CB    . ALA A 1 4215 ? 51.015  96.528  94.344  1.00 4.72   ? 4215 ALA A CB    1 
ATOM   20013 N  N     . CYS A 1 4216 ? 49.763  93.878  93.067  1.00 6.51   ? 4216 CYS A N     1 
ATOM   20014 C  CA    . CYS A 1 4216 ? 48.712  93.197  92.316  1.00 6.84   ? 4216 CYS A CA    1 
ATOM   20015 C  C     . CYS A 1 4216 ? 48.074  92.087  93.142  1.00 7.93   ? 4216 CYS A C     1 
ATOM   20016 O  O     . CYS A 1 4216 ? 46.847  91.927  93.138  1.00 9.85   ? 4216 CYS A O     1 
ATOM   20017 C  CB    . CYS A 1 4216 ? 49.275  92.632  91.011  1.00 9.19   ? 4216 CYS A CB    1 
ATOM   20018 S  SG    . CYS A 1 4216 ? 49.757  93.869  89.787  1.00 9.12   ? 4216 CYS A SG    1 
ATOM   20019 N  N     . ASP A 1 4217 ? 48.893  91.306  93.853  1.00 7.89   ? 4217 ASP A N     1 
ATOM   20020 C  CA    . ASP A 1 4217 ? 48.349  90.245  94.696  1.00 7.49   ? 4217 ASP A CA    1 
ATOM   20021 C  C     . ASP A 1 4217 ? 47.479  90.816  95.807  1.00 5.85   ? 4217 ASP A C     1 
ATOM   20022 O  O     . ASP A 1 4217 ? 46.415  90.268  96.112  1.00 8.26   ? 4217 ASP A O     1 
ATOM   20023 C  CB    . ASP A 1 4217 ? 49.475  89.393  95.284  1.00 8.35   ? 4217 ASP A CB    1 
ATOM   20024 C  CG    . ASP A 1 4217 ? 50.287  88.679  94.222  1.00 22.29  ? 4217 ASP A CG    1 
ATOM   20025 O  OD1   . ASP A 1 4217 ? 49.682  87.991  93.373  1.00 29.71  ? 4217 ASP A OD1   1 
ATOM   20026 O  OD2   . ASP A 1 4217 ? 51.531  88.781  94.251  1.00 25.52  ? 4217 ASP A OD2   1 
ATOM   20027 N  N     . THR A 1 4218 ? 47.916  91.914  96.427  1.00 5.19   ? 4218 THR A N     1 
ATOM   20028 C  CA    . THR A 1 4218 ? 47.107  92.554  97.461  1.00 4.99   ? 4218 THR A CA    1 
ATOM   20029 C  C     . THR A 1 4218 ? 45.787  93.068  96.899  1.00 4.42   ? 4218 THR A C     1 
ATOM   20030 O  O     . THR A 1 4218 ? 44.727  92.899  97.519  1.00 4.55   ? 4218 THR A O     1 
ATOM   20031 C  CB    . THR A 1 4218 ? 47.895  93.692  98.108  1.00 3.97   ? 4218 THR A CB    1 
ATOM   20032 O  OG1   . THR A 1 4218 ? 48.988  93.150  98.859  1.00 9.15   ? 4218 THR A OG1   1 
ATOM   20033 C  CG2   . THR A 1 4218 ? 47.007  94.518  99.019  1.00 3.33   ? 4218 THR A CG2   1 
ATOM   20034 N  N     . VAL A 1 4219 ? 45.835  93.701  95.724  1.00 4.89   ? 4219 VAL A N     1 
ATOM   20035 C  CA    . VAL A 1 4219 ? 44.618  94.204  95.095  1.00 6.44   ? 4219 VAL A CA    1 
ATOM   20036 C  C     . VAL A 1 4219 ? 43.651  93.058  94.839  1.00 8.50   ? 4219 VAL A C     1 
ATOM   20037 O  O     . VAL A 1 4219 ? 42.464  93.138  95.172  1.00 11.37  ? 4219 VAL A O     1 
ATOM   20038 C  CB    . VAL A 1 4219 ? 44.958  94.961  93.798  1.00 5.97   ? 4219 VAL A CB    1 
ATOM   20039 C  CG1   . VAL A 1 4219 ? 43.737  95.053  92.895  1.00 8.46   ? 4219 VAL A CG1   1 
ATOM   20040 C  CG2   . VAL A 1 4219 ? 45.491  96.346  94.118  1.00 4.17   ? 4219 VAL A CG2   1 
ATOM   20041 N  N     . ASP A 1 4220 ? 44.155  91.960  94.269  1.00 7.32   ? 4220 ASP A N     1 
ATOM   20042 C  CA    . ASP A 1 4220 ? 43.302  90.808  93.996  1.00 9.87   ? 4220 ASP A CA    1 
ATOM   20043 C  C     . ASP A 1 4220 ? 42.716  90.241  95.282  1.00 12.11  ? 4220 ASP A C     1 
ATOM   20044 O  O     . ASP A 1 4220 ? 41.512  89.972  95.364  1.00 16.12  ? 4220 ASP A O     1 
ATOM   20045 C  CB    . ASP A 1 4220 ? 44.095  89.735  93.251  1.00 11.69  ? 4220 ASP A CB    1 
ATOM   20046 C  CG    . ASP A 1 4220 ? 44.313  90.080  91.796  1.00 18.59  ? 4220 ASP A CG    1 
ATOM   20047 O  OD1   . ASP A 1 4220 ? 43.413  90.691  91.184  1.00 25.00  ? 4220 ASP A OD1   1 
ATOM   20048 O  OD2   . ASP A 1 4220 ? 45.386  89.735  91.260  1.00 21.48  ? 4220 ASP A OD2   1 
ATOM   20049 N  N     . THR A 1 4221 ? 43.557  90.067  96.305  1.00 9.57   ? 4221 THR A N     1 
ATOM   20050 C  CA    . THR A 1 4221 ? 43.107  89.466  97.556  1.00 7.31   ? 4221 THR A CA    1 
ATOM   20051 C  C     . THR A 1 4221 ? 41.990  90.282  98.189  1.00 9.76   ? 4221 THR A C     1 
ATOM   20052 O  O     . THR A 1 4221 ? 40.920  89.751  98.508  1.00 15.44  ? 4221 THR A O     1 
ATOM   20053 C  CB    . THR A 1 4221 ? 44.284  89.330  98.523  1.00 7.78   ? 4221 THR A CB    1 
ATOM   20054 O  OG1   . THR A 1 4221 ? 45.213  88.361  98.021  1.00 9.65   ? 4221 THR A OG1   1 
ATOM   20055 C  CG2   . THR A 1 4221 ? 43.801  88.901  99.901  1.00 7.05   ? 4221 THR A CG2   1 
ATOM   20056 N  N     . TRP A 1 4222 ? 42.208  91.587  98.357  1.00 8.34   ? 4222 TRP A N     1 
ATOM   20057 C  CA    . TRP A 1 4222 ? 41.211  92.389  99.054  1.00 10.02  ? 4222 TRP A CA    1 
ATOM   20058 C  C     . TRP A 1 4222 ? 39.991  92.682  98.190  1.00 14.46  ? 4222 TRP A C     1 
ATOM   20059 O  O     . TRP A 1 4222 ? 38.886  92.830  98.726  1.00 16.67  ? 4222 TRP A O     1 
ATOM   20060 C  CB    . TRP A 1 4222 ? 41.849  93.675  99.576  1.00 6.78   ? 4222 TRP A CB    1 
ATOM   20061 C  CG    . TRP A 1 4222 ? 42.829  93.387  100.669 1.00 6.18   ? 4222 TRP A CG    1 
ATOM   20062 C  CD1   . TRP A 1 4222 ? 44.163  93.147  100.530 1.00 4.85   ? 4222 TRP A CD1   1 
ATOM   20063 C  CD2   . TRP A 1 4222 ? 42.542  93.262  102.067 1.00 4.84   ? 4222 TRP A CD2   1 
ATOM   20064 N  NE1   . TRP A 1 4222 ? 44.729  92.898  101.755 1.00 4.34   ? 4222 TRP A NE1   1 
ATOM   20065 C  CE2   . TRP A 1 4222 ? 43.755  92.965  102.717 1.00 4.49   ? 4222 TRP A CE2   1 
ATOM   20066 C  CE3   . TRP A 1 4222 ? 41.379  93.384  102.834 1.00 4.30   ? 4222 TRP A CE3   1 
ATOM   20067 C  CZ2   . TRP A 1 4222 ? 43.841  92.786  104.096 1.00 4.78   ? 4222 TRP A CZ2   1 
ATOM   20068 C  CZ3   . TRP A 1 4222 ? 41.466  93.207  104.203 1.00 5.49   ? 4222 TRP A CZ3   1 
ATOM   20069 C  CH2   . TRP A 1 4222 ? 42.688  92.911  104.820 1.00 6.65   ? 4222 TRP A CH2   1 
ATOM   20070 N  N     . LEU A 1 4223 ? 40.149  92.743  96.864  1.00 13.55  ? 4223 LEU A N     1 
ATOM   20071 C  CA    . LEU A 1 4223 ? 38.986  92.886  95.998  1.00 14.48  ? 4223 LEU A CA    1 
ATOM   20072 C  C     . LEU A 1 4223 ? 38.106  91.644  96.046  1.00 20.26  ? 4223 LEU A C     1 
ATOM   20073 O  O     . LEU A 1 4223 ? 36.876  91.752  96.094  1.00 24.96  ? 4223 LEU A O     1 
ATOM   20074 C  CB    . LEU A 1 4223 ? 39.434  93.173  94.569  1.00 17.34  ? 4223 LEU A CB    1 
ATOM   20075 C  CG    . LEU A 1 4223 ? 38.310  93.452  93.576  1.00 26.06  ? 4223 LEU A CG    1 
ATOM   20076 C  CD1   . LEU A 1 4223 ? 37.424  94.580  94.078  1.00 21.61  ? 4223 LEU A CD1   1 
ATOM   20077 C  CD2   . LEU A 1 4223 ? 38.897  93.783  92.223  1.00 21.41  ? 4223 LEU A CD2   1 
ATOM   20078 N  N     . ASP A 1 4224 ? 38.715  90.455  96.030  1.00 19.12  ? 4224 ASP A N     1 
ATOM   20079 C  CA    . ASP A 1 4224 ? 37.933  89.230  96.157  1.00 21.95  ? 4224 ASP A CA    1 
ATOM   20080 C  C     . ASP A 1 4224 ? 37.312  89.116  97.543  1.00 23.69  ? 4224 ASP A C     1 
ATOM   20081 O  O     . ASP A 1 4224 ? 36.197  88.601  97.688  1.00 32.04  ? 4224 ASP A O     1 
ATOM   20082 C  CB    . ASP A 1 4224 ? 38.805  88.013  95.851  1.00 24.45  ? 4224 ASP A CB    1 
ATOM   20083 C  CG    . ASP A 1 4224 ? 39.412  88.068  94.461  1.00 30.61  ? 4224 ASP A CG    1 
ATOM   20084 O  OD1   . ASP A 1 4224 ? 39.056  88.986  93.693  1.00 33.21  ? 4224 ASP A OD1   1 
ATOM   20085 O  OD2   . ASP A 1 4224 ? 40.245  87.195  94.138  1.00 31.64  ? 4224 ASP A OD2   1 
ATOM   20086 N  N     . ASP A 1 4225 ? 38.019  89.585  98.574  1.00 26.77  ? 4225 ASP A N     1 
ATOM   20087 C  CA    . ASP A 1 4225 ? 37.453  89.581  99.918  1.00 26.56  ? 4225 ASP A CA    1 
ATOM   20088 C  C     . ASP A 1 4225 ? 36.227  90.481  100.005 1.00 28.34  ? 4225 ASP A C     1 
ATOM   20089 O  O     . ASP A 1 4225 ? 35.217  90.109  100.614 1.00 36.52  ? 4225 ASP A O     1 
ATOM   20090 C  CB    . ASP A 1 4225 ? 38.510  90.013  100.934 1.00 27.79  ? 4225 ASP A CB    1 
ATOM   20091 C  CG    . ASP A 1 4225 ? 38.026  89.895  102.364 1.00 39.30  ? 4225 ASP A CG    1 
ATOM   20092 O  OD1   . ASP A 1 4225 ? 37.936  88.757  102.870 1.00 53.45  ? 4225 ASP A OD1   1 
ATOM   20093 O  OD2   . ASP A 1 4225 ? 37.734  90.940  102.982 1.00 35.97  ? 4225 ASP A OD2   1 
ATOM   20094 N  N     . THR A 1 4226 ? 36.292  91.668  99.400  1.00 27.75  ? 4226 THR A N     1 
ATOM   20095 C  CA    . THR A 1 4226 ? 35.152  92.578  99.444  1.00 30.85  ? 4226 THR A CA    1 
ATOM   20096 C  C     . THR A 1 4226 ? 34.081  92.171  98.437  1.00 37.01  ? 4226 THR A C     1 
ATOM   20097 O  O     . THR A 1 4226 ? 32.935  91.898  98.808  1.00 44.61  ? 4226 THR A O     1 
ATOM   20098 C  CB    . THR A 1 4226 ? 35.610  94.015  99.190  1.00 27.73  ? 4226 THR A CB    1 
ATOM   20099 O  OG1   . THR A 1 4226 ? 36.553  94.403  100.197 1.00 32.65  ? 4226 THR A OG1   1 
ATOM   20100 C  CG2   . THR A 1 4226 ? 34.420  94.954  99.235  1.00 29.97  ? 4226 THR A CG2   1 
ATOM   20101 N  N     . ALA A 1 4227 ? 34.437  92.128  97.155  1.00 32.93  ? 4227 ALA A N     1 
ATOM   20102 C  CA    . ALA A 1 4227 ? 33.509  91.709  96.105  1.00 35.80  ? 4227 ALA A CA    1 
ATOM   20103 C  C     . ALA A 1 4227 ? 33.498  90.187  96.070  1.00 40.31  ? 4227 ALA A C     1 
ATOM   20104 O  O     . ALA A 1 4227 ? 34.266  89.550  95.347  1.00 43.25  ? 4227 ALA A O     1 
ATOM   20105 C  CB    . ALA A 1 4227 ? 33.908  92.300  94.759  1.00 37.50  ? 4227 ALA A CB    1 
ATOM   20106 N  N     . LYS A 1 4228 ? 32.609  89.594  96.868  1.00 45.17  ? 4228 LYS A N     1 
ATOM   20107 C  CA    . LYS A 1 4228 ? 32.544  88.141  97.022  1.00 46.40  ? 4228 LYS A CA    1 
ATOM   20108 C  C     . LYS A 1 4228 ? 31.856  87.540  95.800  1.00 47.34  ? 4228 LYS A C     1 
ATOM   20109 O  O     . LYS A 1 4228 ? 30.677  87.175  95.818  1.00 51.53  ? 4228 LYS A O     1 
ATOM   20110 C  CB    . LYS A 1 4228 ? 31.825  87.774  98.314  1.00 43.31  ? 4228 LYS A CB    1 
ATOM   20111 C  CG    . LYS A 1 4228 ? 32.550  88.225  99.571  1.00 46.91  ? 4228 LYS A CG    1 
ATOM   20112 C  CD    . LYS A 1 4228 ? 31.816  87.779  100.823 1.00 53.64  ? 4228 LYS A CD    1 
ATOM   20113 C  CE    . LYS A 1 4228 ? 30.519  88.551  101.002 1.00 60.51  ? 4228 LYS A CE    1 
ATOM   20114 N  NZ    . LYS A 1 4228 ? 30.765  89.997  101.262 1.00 50.59  ? 4228 LYS A NZ    1 
ATOM   20115 N  N     . GLY A 1 4229 ? 32.620  87.433  94.718  1.00 44.90  ? 4229 GLY A N     1 
ATOM   20116 C  CA    . GLY A 1 4229 ? 32.112  86.830  93.494  1.00 49.22  ? 4229 GLY A CA    1 
ATOM   20117 C  C     . GLY A 1 4229 ? 30.961  87.581  92.862  1.00 52.20  ? 4229 GLY A C     1 
ATOM   20118 O  O     . GLY A 1 4229 ? 30.009  86.958  92.376  1.00 52.40  ? 4229 GLY A O     1 
ATOM   20119 N  N     . ARG A 1 4230 ? 31.025  88.909  92.855  1.00 54.90  ? 4230 ARG A N     1 
ATOM   20120 C  CA    . ARG A 1 4230 ? 29.988  89.741  92.267  1.00 50.49  ? 4230 ARG A CA    1 
ATOM   20121 C  C     . ARG A 1 4230 ? 30.489  90.362  90.969  1.00 50.89  ? 4230 ARG A C     1 
ATOM   20122 O  O     . ARG A 1 4230 ? 31.679  90.648  90.816  1.00 54.68  ? 4230 ARG A O     1 
ATOM   20123 C  CB    . ARG A 1 4230 ? 29.546  90.839  93.239  1.00 47.39  ? 4230 ARG A CB    1 
ATOM   20124 C  CG    . ARG A 1 4230 ? 28.507  90.383  94.251  1.00 46.45  ? 4230 ARG A CG    1 
ATOM   20125 C  CD    . ARG A 1 4230 ? 27.740  91.563  94.831  1.00 47.21  ? 4230 ARG A CD    1 
ATOM   20126 N  NE    . ARG A 1 4230 ? 28.606  92.489  95.553  1.00 52.07  ? 4230 ARG A NE    1 
ATOM   20127 C  CZ    . ARG A 1 4230 ? 29.187  92.229  96.717  1.00 58.86  ? 4230 ARG A CZ    1 
ATOM   20128 N  NH1   . ARG A 1 4230 ? 29.000  91.078  97.343  1.00 56.23  ? 4230 ARG A NH1   1 
ATOM   20129 N  NH2   . ARG A 1 4230 ? 29.970  93.150  97.271  1.00 53.15  ? 4230 ARG A NH2   1 
ATOM   20130 N  N     . GLN A 1 4231 ? 29.561  90.562  90.031  1.00 51.52  ? 4231 GLN A N     1 
ATOM   20131 C  CA    . GLN A 1 4231 ? 29.931  91.100  88.726  1.00 47.18  ? 4231 GLN A CA    1 
ATOM   20132 C  C     . GLN A 1 4231 ? 30.422  92.538  88.831  1.00 45.86  ? 4231 GLN A C     1 
ATOM   20133 O  O     . GLN A 1 4231 ? 31.397  92.916  88.173  1.00 47.24  ? 4231 GLN A O     1 
ATOM   20134 C  CB    . GLN A 1 4231 ? 28.745  91.007  87.764  1.00 46.04  ? 4231 GLN A CB    1 
ATOM   20135 C  CG    . GLN A 1 4231 ? 29.111  91.123  86.287  1.00 51.92  ? 4231 GLN A CG    1 
ATOM   20136 C  CD    . GLN A 1 4231 ? 30.317  90.287  85.892  1.00 47.39  ? 4231 GLN A CD    1 
ATOM   20137 O  OE1   . GLN A 1 4231 ? 31.180  90.743  85.142  1.00 47.99  ? 4231 GLN A OE1   1 
ATOM   20138 N  NE2   . GLN A 1 4231 ? 30.363  89.045  86.364  1.00 45.81  ? 4231 GLN A NE2   1 
ATOM   20139 N  N     . ASN A 1 4232 ? 29.762  93.354  89.650  1.00 46.85  ? 4232 ASN A N     1 
ATOM   20140 C  CA    . ASN A 1 4232 ? 30.114  94.762  89.790  1.00 40.41  ? 4232 ASN A CA    1 
ATOM   20141 C  C     . ASN A 1 4232 ? 30.171  95.114  91.267  1.00 43.35  ? 4232 ASN A C     1 
ATOM   20142 O  O     . ASN A 1 4232 ? 29.263  94.763  92.026  1.00 53.95  ? 4232 ASN A O     1 
ATOM   20143 C  CB    . ASN A 1 4232 ? 29.110  95.660  89.061  1.00 40.99  ? 4232 ASN A CB    1 
ATOM   20144 C  CG    . ASN A 1 4232 ? 29.177  95.505  87.555  1.00 49.07  ? 4232 ASN A CG    1 
ATOM   20145 O  OD1   . ASN A 1 4232 ? 30.137  95.939  86.918  1.00 48.58  ? 4232 ASN A OD1   1 
ATOM   20146 N  ND2   . ASN A 1 4232 ? 28.156  94.883  86.978  1.00 49.72  ? 4232 ASN A ND2   1 
ATOM   20147 N  N     . ILE A 1 4233 ? 31.235  95.799  91.668  1.00 41.95  ? 4233 ILE A N     1 
ATOM   20148 C  CA    . ILE A 1 4233 ? 31.400  96.289  93.030  1.00 35.65  ? 4233 ILE A CA    1 
ATOM   20149 C  C     . ILE A 1 4233 ? 31.283  97.806  93.018  1.00 35.24  ? 4233 ILE A C     1 
ATOM   20150 O  O     . ILE A 1 4233 ? 31.843  98.479  92.143  1.00 42.42  ? 4233 ILE A O     1 
ATOM   20151 C  CB    . ILE A 1 4233 ? 32.745  95.831  93.631  1.00 35.92  ? 4233 ILE A CB    1 
ATOM   20152 C  CG1   . ILE A 1 4233 ? 32.905  96.352  95.061  1.00 31.01  ? 4233 ILE A CG1   1 
ATOM   20153 C  CG2   . ILE A 1 4233 ? 33.915  96.250  92.748  1.00 28.99  ? 4233 ILE A CG2   1 
ATOM   20154 C  CD1   . ILE A 1 4233 ? 34.191  95.919  95.724  1.00 30.27  ? 4233 ILE A CD1   1 
ATOM   20155 N  N     . SER A 1 4234 ? 30.528  98.344  93.968  1.00 35.20  ? 4234 SER A N     1 
ATOM   20156 C  CA    . SER A 1 4234 ? 30.369  99.787  94.047  1.00 34.60  ? 4234 SER A CA    1 
ATOM   20157 C  C     . SER A 1 4234 ? 31.712  100.436 94.375  1.00 34.52  ? 4234 SER A C     1 
ATOM   20158 O  O     . SER A 1 4234 ? 32.461  99.921  95.214  1.00 34.04  ? 4234 SER A O     1 
ATOM   20159 C  CB    . SER A 1 4234 ? 29.327  100.155 95.104  1.00 33.96  ? 4234 SER A CB    1 
ATOM   20160 O  OG    . SER A 1 4234 ? 29.310  101.550 95.339  1.00 38.02  ? 4234 SER A OG    1 
ATOM   20161 N  N     . PRO A 1 4235 ? 32.057  101.551 93.722  1.00 33.45  ? 4235 PRO A N     1 
ATOM   20162 C  CA    . PRO A 1 4235 ? 33.392  102.140 93.936  1.00 29.87  ? 4235 PRO A CA    1 
ATOM   20163 C  C     . PRO A 1 4235 ? 33.677  102.511 95.381  1.00 25.95  ? 4235 PRO A C     1 
ATOM   20164 O  O     . PRO A 1 4235 ? 34.816  102.357 95.839  1.00 26.15  ? 4235 PRO A O     1 
ATOM   20165 C  CB    . PRO A 1 4235 ? 33.374  103.373 93.022  1.00 26.44  ? 4235 PRO A CB    1 
ATOM   20166 C  CG    . PRO A 1 4235 ? 32.364  103.047 91.972  1.00 30.33  ? 4235 PRO A CG    1 
ATOM   20167 C  CD    . PRO A 1 4235 ? 31.300  102.261 92.678  1.00 32.93  ? 4235 PRO A CD    1 
ATOM   20168 N  N     . ASP A 1 4236 ? 32.676  102.996 96.119  1.00 32.31  ? 4236 ASP A N     1 
ATOM   20169 C  CA    . ASP A 1 4236 ? 32.888  103.330 97.522  1.00 31.87  ? 4236 ASP A CA    1 
ATOM   20170 C  C     . ASP A 1 4236 ? 33.041  102.098 98.404  1.00 30.03  ? 4236 ASP A C     1 
ATOM   20171 O  O     . ASP A 1 4236 ? 33.491  102.230 99.547  1.00 32.19  ? 4236 ASP A O     1 
ATOM   20172 C  CB    . ASP A 1 4236 ? 31.741  104.200 98.039  1.00 34.60  ? 4236 ASP A CB    1 
ATOM   20173 C  CG    . ASP A 1 4236 ? 30.382  103.679 97.624  1.00 44.00  ? 4236 ASP A CG    1 
ATOM   20174 O  OD1   . ASP A 1 4236 ? 30.322  102.885 96.664  1.00 44.43  ? 4236 ASP A OD1   1 
ATOM   20175 O  OD2   . ASP A 1 4236 ? 29.376  104.064 98.255  1.00 46.73  ? 4236 ASP A OD2   1 
ATOM   20176 N  N     . LYS A 1 4237 ? 32.682  100.915 97.908  1.00 28.97  ? 4237 LYS A N     1 
ATOM   20177 C  CA    . LYS A 1 4237 ? 32.879  99.675  98.646  1.00 26.49  ? 4237 LYS A CA    1 
ATOM   20178 C  C     . LYS A 1 4237 ? 34.253  99.062  98.420  1.00 25.60  ? 4237 LYS A C     1 
ATOM   20179 O  O     . LYS A 1 4237 ? 34.610  98.109  99.120  1.00 28.08  ? 4237 LYS A O     1 
ATOM   20180 C  CB    . LYS A 1 4237 ? 31.798  98.655  98.269  1.00 26.52  ? 4237 LYS A CB    1 
ATOM   20181 C  CG    . LYS A 1 4237 ? 30.360  99.085  98.561  1.00 29.41  ? 4237 LYS A CG    1 
ATOM   20182 C  CD    . LYS A 1 4237 ? 30.040  99.098  100.055 1.00 31.64  ? 4237 LYS A CD    1 
ATOM   20183 C  CE    . LYS A 1 4237 ? 30.191  100.482 100.673 1.00 41.62  ? 4237 LYS A CE    1 
ATOM   20184 N  NZ    . LYS A 1 4237 ? 29.770  100.499 102.101 1.00 50.37  ? 4237 LYS A NZ    1 
ATOM   20185 N  N     . ILE A 1 4238 ? 35.023  99.579  97.468  1.00 20.75  ? 4238 ILE A N     1 
ATOM   20186 C  CA    . ILE A 1 4238 ? 36.381  99.074  97.244  1.00 17.61  ? 4238 ILE A CA    1 
ATOM   20187 C  C     . ILE A 1 4238 ? 37.227  99.348  98.481  1.00 19.05  ? 4238 ILE A C     1 
ATOM   20188 O  O     . ILE A 1 4238 ? 37.212  100.480 99.004  1.00 21.56  ? 4238 ILE A O     1 
ATOM   20189 C  CB    . ILE A 1 4238 ? 36.998  99.728  95.995  1.00 15.50  ? 4238 ILE A CB    1 
ATOM   20190 C  CG1   . ILE A 1 4238 ? 36.198  99.342  94.749  1.00 19.25  ? 4238 ILE A CG1   1 
ATOM   20191 C  CG2   . ILE A 1 4238 ? 38.464  99.348  95.847  1.00 10.41  ? 4238 ILE A CG2   1 
ATOM   20192 C  CD1   . ILE A 1 4238 ? 36.682  99.999  93.480  1.00 16.18  ? 4238 ILE A CD1   1 
ATOM   20193 N  N     . PRO A 1 4239 ? 37.972  98.367  99.000  1.00 14.86  ? 4239 PRO A N     1 
ATOM   20194 C  CA    . PRO A 1 4239 ? 38.774  98.613  100.205 1.00 13.48  ? 4239 PRO A CA    1 
ATOM   20195 C  C     . PRO A 1 4239 ? 39.948  99.539  99.937  1.00 10.47  ? 4239 PRO A C     1 
ATOM   20196 O  O     . PRO A 1 4239 ? 41.099  99.097  99.856  1.00 8.14   ? 4239 PRO A O     1 
ATOM   20197 C  CB    . PRO A 1 4239 ? 39.236  97.207  100.606 1.00 10.07  ? 4239 PRO A CB    1 
ATOM   20198 C  CG    . PRO A 1 4239 ? 39.270  96.456  99.319  1.00 11.10  ? 4239 PRO A CG    1 
ATOM   20199 C  CD    . PRO A 1 4239 ? 38.109  96.982  98.517  1.00 14.76  ? 4239 PRO A CD    1 
ATOM   20200 N  N     . TRP A 1 4240 ? 39.657  100.833 99.792  1.00 9.59   ? 4240 TRP A N     1 
ATOM   20201 C  CA    . TRP A 1 4240 ? 40.710  101.810 99.537  1.00 8.13   ? 4240 TRP A CA    1 
ATOM   20202 C  C     . TRP A 1 4240 ? 41.669  101.910 100.714 1.00 7.40   ? 4240 TRP A C     1 
ATOM   20203 O  O     . TRP A 1 4240 ? 42.883  102.037 100.521 1.00 5.06   ? 4240 TRP A O     1 
ATOM   20204 C  CB    . TRP A 1 4240 ? 40.097  103.176 99.231  1.00 9.49   ? 4240 TRP A CB    1 
ATOM   20205 C  CG    . TRP A 1 4240 ? 39.201  103.171 98.039  1.00 8.78   ? 4240 TRP A CG    1 
ATOM   20206 C  CD1   . TRP A 1 4240 ? 37.849  103.342 98.029  1.00 9.25   ? 4240 TRP A CD1   1 
ATOM   20207 C  CD2   . TRP A 1 4240 ? 39.592  102.987 96.675  1.00 9.30   ? 4240 TRP A CD2   1 
ATOM   20208 N  NE1   . TRP A 1 4240 ? 37.372  103.275 96.744  1.00 10.79  ? 4240 TRP A NE1   1 
ATOM   20209 C  CE2   . TRP A 1 4240 ? 38.423  103.058 95.893  1.00 10.57  ? 4240 TRP A CE2   1 
ATOM   20210 C  CE3   . TRP A 1 4240 ? 40.818  102.770 96.038  1.00 7.16   ? 4240 TRP A CE3   1 
ATOM   20211 C  CZ2   . TRP A 1 4240 ? 38.443  102.919 94.509  1.00 11.72  ? 4240 TRP A CZ2   1 
ATOM   20212 C  CZ3   . TRP A 1 4240 ? 40.835  102.632 94.665  1.00 7.26   ? 4240 TRP A CZ3   1 
ATOM   20213 C  CH2   . TRP A 1 4240 ? 39.656  102.709 93.914  1.00 9.18   ? 4240 TRP A CH2   1 
ATOM   20214 N  N     . SER A 1 4241 ? 41.143  101.861 101.940 1.00 10.11  ? 4241 SER A N     1 
ATOM   20215 C  CA    . SER A 1 4241 ? 41.998  101.959 103.118 1.00 7.80   ? 4241 SER A CA    1 
ATOM   20216 C  C     . SER A 1 4241 ? 42.980  100.796 103.181 1.00 5.29   ? 4241 SER A C     1 
ATOM   20217 O  O     . SER A 1 4241 ? 44.166  100.987 103.465 1.00 5.80   ? 4241 SER A O     1 
ATOM   20218 C  CB    . SER A 1 4241 ? 41.142  102.010 104.384 1.00 10.46  ? 4241 SER A CB    1 
ATOM   20219 O  OG    . SER A 1 4241 ? 41.953  102.077 105.543 1.00 17.89  ? 4241 SER A OG    1 
ATOM   20220 N  N     . ALA A 1 4242 ? 42.500  99.581  102.910 1.00 4.18   ? 4242 ALA A N     1 
ATOM   20221 C  CA    . ALA A 1 4242 ? 43.370  98.410  102.952 1.00 3.69   ? 4242 ALA A CA    1 
ATOM   20222 C  C     . ALA A 1 4242 ? 44.510  98.535  101.950 1.00 4.43   ? 4242 ALA A C     1 
ATOM   20223 O  O     . ALA A 1 4242 ? 45.685  98.375  102.304 1.00 4.15   ? 4242 ALA A O     1 
ATOM   20224 C  CB    . ALA A 1 4242 ? 42.555  97.144  102.683 1.00 3.61   ? 4242 ALA A CB    1 
ATOM   20225 N  N     . LEU A 1 4243 ? 44.178  98.831  100.691 1.00 4.05   ? 4243 LEU A N     1 
ATOM   20226 C  CA    . LEU A 1 4243 ? 45.198  98.937  99.654  1.00 3.98   ? 4243 LEU A CA    1 
ATOM   20227 C  C     . LEU A 1 4243 ? 46.175  100.063 99.963  1.00 4.95   ? 4243 LEU A C     1 
ATOM   20228 O  O     . LEU A 1 4243 ? 47.396  99.890  99.857  1.00 6.81   ? 4243 LEU A O     1 
ATOM   20229 C  CB    . LEU A 1 4243 ? 44.538  99.160  98.293  1.00 4.83   ? 4243 LEU A CB    1 
ATOM   20230 C  CG    . LEU A 1 4243 ? 43.559  98.092  97.802  1.00 6.35   ? 4243 LEU A CG    1 
ATOM   20231 C  CD1   . LEU A 1 4243 ? 43.004  98.467  96.436  1.00 5.32   ? 4243 LEU A CD1   1 
ATOM   20232 C  CD2   . LEU A 1 4243 ? 44.220  96.723  97.762  1.00 4.78   ? 4243 LEU A CD2   1 
ATOM   20233 N  N     . LYS A 1 4244 ? 45.651  101.226 100.358 1.00 5.19   ? 4244 LYS A N     1 
ATOM   20234 C  CA    . LYS A 1 4244 ? 46.508  102.376 100.618 1.00 5.50   ? 4244 LYS A CA    1 
ATOM   20235 C  C     . LYS A 1 4244 ? 47.450  102.114 101.783 1.00 4.46   ? 4244 LYS A C     1 
ATOM   20236 O  O     . LYS A 1 4244 ? 48.644  102.408 101.693 1.00 5.43   ? 4244 LYS A O     1 
ATOM   20237 C  CB    . LYS A 1 4244 ? 45.660  103.619 100.886 1.00 8.50   ? 4244 LYS A CB    1 
ATOM   20238 C  CG    . LYS A 1 4244 ? 45.152  104.308 99.633  1.00 8.00   ? 4244 LYS A CG    1 
ATOM   20239 C  CD    . LYS A 1 4244 ? 44.372  105.565 99.981  1.00 8.08   ? 4244 LYS A CD    1 
ATOM   20240 C  CE    . LYS A 1 4244 ? 43.201  105.249 100.895 1.00 8.67   ? 4244 LYS A CE    1 
ATOM   20241 N  NZ    . LYS A 1 4244 ? 42.332  106.433 101.119 1.00 16.11  ? 4244 LYS A NZ    1 
ATOM   20242 N  N     . THR A 1 4245 ? 46.939  101.556 102.884 1.00 4.52   ? 4245 THR A N     1 
ATOM   20243 C  CA    . THR A 1 4245 ? 47.797  101.269 104.028 1.00 3.81   ? 4245 THR A CA    1 
ATOM   20244 C  C     . THR A 1 4245 ? 48.833  100.202 103.694 1.00 4.35   ? 4245 THR A C     1 
ATOM   20245 O  O     . THR A 1 4245 ? 50.008  100.337 104.057 1.00 4.65   ? 4245 THR A O     1 
ATOM   20246 C  CB    . THR A 1 4245 ? 46.953  100.835 105.225 1.00 5.46   ? 4245 THR A CB    1 
ATOM   20247 O  OG1   . THR A 1 4245 ? 45.880  101.765 105.420 1.00 8.46   ? 4245 THR A OG1   1 
ATOM   20248 C  CG2   . THR A 1 4245 ? 47.804  100.775 106.483 1.00 4.65   ? 4245 THR A CG2   1 
ATOM   20249 N  N     . LEU A 1 4246 ? 48.419  99.135  103.005 1.00 3.72   ? 4246 LEU A N     1 
ATOM   20250 C  CA    . LEU A 1 4246 ? 49.352  98.061  102.694 1.00 4.33   ? 4246 LEU A CA    1 
ATOM   20251 C  C     . LEU A 1 4246 ? 50.450  98.527  101.749 1.00 4.79   ? 4246 LEU A C     1 
ATOM   20252 O  O     . LEU A 1 4246 ? 51.600  98.093  101.879 1.00 5.80   ? 4246 LEU A O     1 
ATOM   20253 C  CB    . LEU A 1 4246 ? 48.597  96.868  102.110 1.00 5.24   ? 4246 LEU A CB    1 
ATOM   20254 C  CG    . LEU A 1 4246 ? 47.926  95.995  103.175 1.00 5.63   ? 4246 LEU A CG    1 
ATOM   20255 C  CD1   . LEU A 1 4246 ? 47.176  94.839  102.552 1.00 4.78   ? 4246 LEU A CD1   1 
ATOM   20256 C  CD2   . LEU A 1 4246 ? 48.944  95.488  104.178 1.00 2.40   ? 4246 LEU A CD2   1 
ATOM   20257 N  N     . MET A 1 4247 ? 50.125  99.407  100.798 1.00 3.82   ? 4247 MET A N     1 
ATOM   20258 C  CA    . MET A 1 4247 ? 51.158  99.967  99.935  1.00 4.07   ? 4247 MET A CA    1 
ATOM   20259 C  C     . MET A 1 4247 ? 51.965  101.057 100.633 1.00 5.01   ? 4247 MET A C     1 
ATOM   20260 O  O     . MET A 1 4247 ? 53.112  101.313 100.256 1.00 6.88   ? 4247 MET A O     1 
ATOM   20261 C  CB    . MET A 1 4247 ? 50.534  100.506 98.648  1.00 4.92   ? 4247 MET A CB    1 
ATOM   20262 C  CG    . MET A 1 4247 ? 50.340  99.445  97.577  1.00 6.25   ? 4247 MET A CG    1 
ATOM   20263 S  SD    . MET A 1 4247 ? 48.997  99.823  96.440  1.00 15.70  ? 4247 MET A SD    1 
ATOM   20264 C  CE    . MET A 1 4247 ? 49.841  100.902 95.288  1.00 10.92  ? 4247 MET A CE    1 
ATOM   20265 N  N     . ALA A 1 4248 ? 51.395  101.719 101.634 1.00 3.96   ? 4248 ALA A N     1 
ATOM   20266 C  CA    . ALA A 1 4248 ? 52.145  102.732 102.360 1.00 4.21   ? 4248 ALA A CA    1 
ATOM   20267 C  C     . ALA A 1 4248 ? 53.173  102.118 103.296 1.00 5.88   ? 4248 ALA A C     1 
ATOM   20268 O  O     . ALA A 1 4248 ? 54.258  102.683 103.473 1.00 6.05   ? 4248 ALA A O     1 
ATOM   20269 C  CB    . ALA A 1 4248 ? 51.187  103.626 103.147 1.00 7.89   ? 4248 ALA A CB    1 
ATOM   20270 N  N     . GLN A 1 4249 ? 52.858  100.975 103.897 1.00 5.07   ? 4249 GLN A N     1 
ATOM   20271 C  CA    . GLN A 1 4249 ? 53.705  100.386 104.925 1.00 4.38   ? 4249 GLN A CA    1 
ATOM   20272 C  C     . GLN A 1 4249 ? 54.521  99.197  104.445 1.00 6.25   ? 4249 GLN A C     1 
ATOM   20273 O  O     . GLN A 1 4249 ? 55.632  98.988  104.935 1.00 5.87   ? 4249 GLN A O     1 
ATOM   20274 C  CB    . GLN A 1 4249 ? 52.850  99.960  106.124 1.00 5.53   ? 4249 GLN A CB    1 
ATOM   20275 C  CG    . GLN A 1 4249 ? 51.967  101.073 106.669 1.00 5.40   ? 4249 GLN A CG    1 
ATOM   20276 C  CD    . GLN A 1 4249 ? 52.766  102.244 107.207 1.00 7.99   ? 4249 GLN A CD    1 
ATOM   20277 O  OE1   . GLN A 1 4249 ? 53.476  102.121 108.204 1.00 10.89  ? 4249 GLN A OE1   1 
ATOM   20278 N  NE2   . GLN A 1 4249 ? 52.658  103.388 106.542 1.00 6.21   ? 4249 GLN A NE2   1 
ATOM   20279 N  N     . SER A 1 4250 ? 54.011  98.408  103.499 1.00 7.75   ? 4250 SER A N     1 
ATOM   20280 C  CA    . SER A 1 4250 ? 54.688  97.183  103.085 1.00 5.66   ? 4250 SER A CA    1 
ATOM   20281 C  C     . SER A 1 4250 ? 55.113  97.180  101.622 1.00 10.22  ? 4250 SER A C     1 
ATOM   20282 O  O     . SER A 1 4250 ? 56.287  96.952  101.321 1.00 14.27  ? 4250 SER A O     1 
ATOM   20283 C  CB    . SER A 1 4250 ? 53.788  95.977  103.364 1.00 7.06   ? 4250 SER A CB    1 
ATOM   20284 O  OG    . SER A 1 4250 ? 53.453  95.915  104.737 1.00 6.56   ? 4250 SER A OG    1 
ATOM   20285 N  N     . ILE A 1 4251 ? 54.184  97.426  100.705 1.00 10.25  ? 4251 ILE A N     1 
ATOM   20286 C  CA    . ILE A 1 4251 ? 54.455  97.318  99.276  1.00 9.28   ? 4251 ILE A CA    1 
ATOM   20287 C  C     . ILE A 1 4251 ? 54.814  98.699  98.749  1.00 18.11  ? 4251 ILE A C     1 
ATOM   20288 O  O     . ILE A 1 4251 ? 53.941  99.564  98.640  1.00 26.58  ? 4251 ILE A O     1 
ATOM   20289 C  CB    . ILE A 1 4251 ? 53.243  96.746  98.528  1.00 9.20   ? 4251 ILE A CB    1 
ATOM   20290 C  CG1   . ILE A 1 4251 ? 52.922  95.346  99.037  1.00 9.22   ? 4251 ILE A CG1   1 
ATOM   20291 C  CG2   . ILE A 1 4251 ? 53.514  96.703  97.039  1.00 7.96   ? 4251 ILE A CG2   1 
ATOM   20292 C  CD1   . ILE A 1 4251 ? 51.603  94.829  98.558  1.00 6.92   ? 4251 ILE A CD1   1 
ATOM   20293 N  N     . TYR A 1 4252 ? 56.086  98.883  98.380  1.00 10.60  ? 4252 TYR A N     1 
ATOM   20294 C  CA    . TYR A 1 4252 ? 56.709  100.169 98.060  1.00 10.18  ? 4252 TYR A CA    1 
ATOM   20295 C  C     . TYR A 1 4252 ? 57.001  100.940 99.342  1.00 9.40   ? 4252 TYR A C     1 
ATOM   20296 O  O     . TYR A 1 4252 ? 57.631  102.001 99.303  1.00 15.05  ? 4252 TYR A O     1 
ATOM   20297 C  CB    . TYR A 1 4252 ? 55.836  101.040 97.143  1.00 5.96   ? 4252 TYR A CB    1 
ATOM   20298 C  CG    . TYR A 1 4252 ? 55.515  100.465 95.781  1.00 6.46   ? 4252 TYR A CG    1 
ATOM   20299 C  CD1   . TYR A 1 4252 ? 56.363  100.661 94.700  1.00 6.39   ? 4252 TYR A CD1   1 
ATOM   20300 C  CD2   . TYR A 1 4252 ? 54.337  99.761  95.570  1.00 6.84   ? 4252 TYR A CD2   1 
ATOM   20301 C  CE1   . TYR A 1 4252 ? 56.057  100.146 93.453  1.00 8.54   ? 4252 TYR A CE1   1 
ATOM   20302 C  CE2   . TYR A 1 4252 ? 54.025  99.243  94.331  1.00 5.63   ? 4252 TYR A CE2   1 
ATOM   20303 C  CZ    . TYR A 1 4252 ? 54.886  99.438  93.276  1.00 6.06   ? 4252 TYR A CZ    1 
ATOM   20304 O  OH    . TYR A 1 4252 ? 54.572  98.921  92.041  1.00 10.63  ? 4252 TYR A OH    1 
ATOM   20305 N  N     . GLY A 1 4253 ? 56.560  100.410 100.486 1.00 10.96  ? 4253 GLY A N     1 
ATOM   20306 C  CA    . GLY A 1 4253 ? 56.701  101.136 101.735 1.00 5.52   ? 4253 GLY A CA    1 
ATOM   20307 C  C     . GLY A 1 4253 ? 57.846  100.665 102.603 1.00 7.71   ? 4253 GLY A C     1 
ATOM   20308 O  O     . GLY A 1 4253 ? 58.442  101.467 103.329 1.00 8.59   ? 4253 GLY A O     1 
ATOM   20309 N  N     . GLY A 1 4254 ? 58.173  99.372  102.549 1.00 5.56   ? 4254 GLY A N     1 
ATOM   20310 C  CA    . GLY A 1 4254 ? 59.259  98.854  103.361 1.00 5.40   ? 4254 GLY A CA    1 
ATOM   20311 C  C     . GLY A 1 4254 ? 60.628  99.336  102.939 1.00 7.01   ? 4254 GLY A C     1 
ATOM   20312 O  O     . GLY A 1 4254 ? 61.550  99.349  103.760 1.00 10.52  ? 4254 GLY A O     1 
ATOM   20313 N  N     . ARG A 1 4255 ? 60.782  99.736  101.678 1.00 7.51   ? 4255 ARG A N     1 
ATOM   20314 C  CA    . ARG A 1 4255 ? 62.052  100.266 101.204 1.00 7.40   ? 4255 ARG A CA    1 
ATOM   20315 C  C     . ARG A 1 4255 ? 62.306  101.688 101.686 1.00 9.39   ? 4255 ARG A C     1 
ATOM   20316 O  O     . ARG A 1 4255 ? 63.464  102.116 101.724 1.00 15.06  ? 4255 ARG A O     1 
ATOM   20317 C  CB    . ARG A 1 4255 ? 62.095  100.226 99.675  1.00 9.36   ? 4255 ARG A CB    1 
ATOM   20318 C  CG    . ARG A 1 4255 ? 61.648  98.907  99.067  1.00 13.69  ? 4255 ARG A CG    1 
ATOM   20319 C  CD    . ARG A 1 4255 ? 61.630  98.991  97.547  1.00 15.32  ? 4255 ARG A CD    1 
ATOM   20320 N  NE    . ARG A 1 4255 ? 61.445  97.692  96.909  1.00 15.79  ? 4255 ARG A NE    1 
ATOM   20321 C  CZ    . ARG A 1 4255 ? 62.350  96.723  96.894  1.00 14.95  ? 4255 ARG A CZ    1 
ATOM   20322 N  NH1   . ARG A 1 4255 ? 63.536  96.873  97.462  1.00 15.30  ? 4255 ARG A NH1   1 
ATOM   20323 N  NH2   . ARG A 1 4255 ? 62.063  95.577  96.284  1.00 13.51  ? 4255 ARG A NH2   1 
ATOM   20324 N  N     . VAL A 1 4256 ? 61.259  102.419 102.060 1.00 8.01   ? 4256 VAL A N     1 
ATOM   20325 C  CA    . VAL A 1 4256 ? 61.391  103.821 102.441 1.00 9.75   ? 4256 VAL A CA    1 
ATOM   20326 C  C     . VAL A 1 4256 ? 62.040  103.913 103.815 1.00 10.90  ? 4256 VAL A C     1 
ATOM   20327 O  O     . VAL A 1 4256 ? 61.546  103.334 104.789 1.00 11.74  ? 4256 VAL A O     1 
ATOM   20328 C  CB    . VAL A 1 4256 ? 60.020  104.517 102.437 1.00 10.90  ? 4256 VAL A CB    1 
ATOM   20329 C  CG1   . VAL A 1 4256 ? 60.177  105.990 102.766 1.00 11.13  ? 4256 VAL A CG1   1 
ATOM   20330 C  CG2   . VAL A 1 4256 ? 59.322  104.334 101.102 1.00 7.96   ? 4256 VAL A CG2   1 
ATOM   20331 N  N     . ASP A 1 4257 ? 63.146  104.656 103.900 1.00 13.19  ? 4257 ASP A N     1 
ATOM   20332 C  CA    . ASP A 1 4257 ? 63.836  104.891 105.163 1.00 17.81  ? 4257 ASP A CA    1 
ATOM   20333 C  C     . ASP A 1 4257 ? 63.867  106.371 105.533 1.00 20.61  ? 4257 ASP A C     1 
ATOM   20334 O  O     . ASP A 1 4257 ? 64.604  106.764 106.442 1.00 25.84  ? 4257 ASP A O     1 
ATOM   20335 C  CB    . ASP A 1 4257 ? 65.257  104.323 105.111 1.00 18.13  ? 4257 ASP A CB    1 
ATOM   20336 C  CG    . ASP A 1 4257 ? 66.048  104.824 103.916 1.00 22.15  ? 4257 ASP A CG    1 
ATOM   20337 O  OD1   . ASP A 1 4257 ? 66.239  106.052 103.790 1.00 22.02  ? 4257 ASP A OD1   1 
ATOM   20338 O  OD2   . ASP A 1 4257 ? 66.480  103.985 103.098 1.00 23.66  ? 4257 ASP A OD2   1 
ATOM   20339 N  N     . ASN A 1 4258 ? 63.079  107.197 104.849 1.00 19.69  ? 4258 ASN A N     1 
ATOM   20340 C  CA    . ASN A 1 4258 ? 63.033  108.631 105.091 1.00 18.44  ? 4258 ASN A CA    1 
ATOM   20341 C  C     . ASN A 1 4258 ? 61.581  109.025 105.311 1.00 16.61  ? 4258 ASN A C     1 
ATOM   20342 O  O     . ASN A 1 4258 ? 60.689  108.561 104.595 1.00 17.74  ? 4258 ASN A O     1 
ATOM   20343 C  CB    . ASN A 1 4258 ? 63.654  109.406 103.902 1.00 14.28  ? 4258 ASN A CB    1 
ATOM   20344 C  CG    . ASN A 1 4258 ? 63.553  110.927 104.043 1.00 21.59  ? 4258 ASN A CG    1 
ATOM   20345 O  OD1   . ASN A 1 4258 ? 62.666  111.463 104.708 1.00 31.76  ? 4258 ASN A OD1   1 
ATOM   20346 N  ND2   . ASN A 1 4258 ? 64.479  111.627 103.399 1.00 19.74  ? 4258 ASN A ND2   1 
ATOM   20347 N  N     . GLU A 1 4259 ? 61.347  109.888 106.302 1.00 16.90  ? 4259 GLU A N     1 
ATOM   20348 C  CA    . GLU A 1 4259 ? 59.979  110.286 106.618 1.00 15.53  ? 4259 GLU A CA    1 
ATOM   20349 C  C     . GLU A 1 4259 ? 59.369  111.147 105.518 1.00 12.75  ? 4259 GLU A C     1 
ATOM   20350 O  O     . GLU A 1 4259 ? 58.153  111.102 105.305 1.00 9.02   ? 4259 GLU A O     1 
ATOM   20351 C  CB    . GLU A 1 4259 ? 59.934  111.020 107.961 1.00 19.20  ? 4259 GLU A CB    1 
ATOM   20352 C  CG    . GLU A 1 4259 ? 60.365  112.477 107.907 1.00 26.58  ? 4259 GLU A CG    1 
ATOM   20353 C  CD    . GLU A 1 4259 ? 60.473  113.108 109.280 1.00 42.03  ? 4259 GLU A CD    1 
ATOM   20354 O  OE1   . GLU A 1 4259 ? 61.587  113.123 109.843 1.00 36.41  ? 4259 GLU A OE1   1 
ATOM   20355 O  OE2   . GLU A 1 4259 ? 59.443  113.591 109.795 1.00 52.93  ? 4259 GLU A OE2   1 
ATOM   20356 N  N     . PHE A 1 4260 ? 60.183  111.932 104.812 1.00 13.26  ? 4260 PHE A N     1 
ATOM   20357 C  CA    . PHE A 1 4260 ? 59.650  112.793 103.762 1.00 12.94  ? 4260 PHE A CA    1 
ATOM   20358 C  C     . PHE A 1 4260 ? 59.338  112.004 102.496 1.00 9.88   ? 4260 PHE A C     1 
ATOM   20359 O  O     . PHE A 1 4260 ? 58.343  112.279 101.817 1.00 9.01   ? 4260 PHE A O     1 
ATOM   20360 C  CB    . PHE A 1 4260 ? 60.630  113.929 103.482 1.00 13.53  ? 4260 PHE A CB    1 
ATOM   20361 C  CG    . PHE A 1 4260 ? 60.904  114.781 104.683 1.00 14.95  ? 4260 PHE A CG    1 
ATOM   20362 C  CD1   . PHE A 1 4260 ? 60.051  115.815 105.024 1.00 13.50  ? 4260 PHE A CD1   1 
ATOM   20363 C  CD2   . PHE A 1 4260 ? 61.997  114.525 105.493 1.00 15.78  ? 4260 PHE A CD2   1 
ATOM   20364 C  CE1   . PHE A 1 4260 ? 60.292  116.591 106.137 1.00 14.65  ? 4260 PHE A CE1   1 
ATOM   20365 C  CE2   . PHE A 1 4260 ? 62.242  115.296 106.609 1.00 16.91  ? 4260 PHE A CE2   1 
ATOM   20366 C  CZ    . PHE A 1 4260 ? 61.388  116.331 106.930 1.00 18.83  ? 4260 PHE A CZ    1 
ATOM   20367 N  N     . ASP A 1 4261 ? 60.162  111.006 102.176 1.00 11.26  ? 4261 ASP A N     1 
ATOM   20368 C  CA    . ASP A 1 4261 ? 59.824  110.104 101.082 1.00 8.65   ? 4261 ASP A CA    1 
ATOM   20369 C  C     . ASP A 1 4261 ? 58.591  109.276 101.423 1.00 7.57   ? 4261 ASP A C     1 
ATOM   20370 O  O     . ASP A 1 4261 ? 57.762  108.994 100.550 1.00 7.79   ? 4261 ASP A O     1 
ATOM   20371 C  CB    . ASP A 1 4261 ? 61.016  109.208 100.760 1.00 8.33   ? 4261 ASP A CB    1 
ATOM   20372 C  CG    . ASP A 1 4261 ? 62.075  109.927 99.953  1.00 14.03  ? 4261 ASP A CG    1 
ATOM   20373 O  OD1   . ASP A 1 4261 ? 61.844  111.094 99.575  1.00 15.17  ? 4261 ASP A OD1   1 
ATOM   20374 O  OD2   . ASP A 1 4261 ? 63.146  109.337 99.710  1.00 14.92  ? 4261 ASP A OD2   1 
ATOM   20375 N  N     . GLN A 1 4262 ? 58.451  108.888 102.693 1.00 6.76   ? 4262 GLN A N     1 
ATOM   20376 C  CA    . GLN A 1 4262 ? 57.227  108.229 103.135 1.00 6.26   ? 4262 GLN A CA    1 
ATOM   20377 C  C     . GLN A 1 4262 ? 56.024  109.150 102.989 1.00 6.33   ? 4262 GLN A C     1 
ATOM   20378 O  O     . GLN A 1 4262 ? 54.938  108.709 102.596 1.00 6.20   ? 4262 GLN A O     1 
ATOM   20379 C  CB    . GLN A 1 4262 ? 57.375  107.759 104.582 1.00 5.40   ? 4262 GLN A CB    1 
ATOM   20380 C  CG    . GLN A 1 4262 ? 56.178  106.983 105.109 1.00 6.43   ? 4262 GLN A CG    1 
ATOM   20381 C  CD    . GLN A 1 4262 ? 55.946  105.683 104.366 1.00 8.90   ? 4262 GLN A CD    1 
ATOM   20382 O  OE1   . GLN A 1 4262 ? 54.863  105.441 103.833 1.00 6.88   ? 4262 GLN A OE1   1 
ATOM   20383 N  NE2   . GLN A 1 4262 ? 56.967  104.835 104.328 1.00 9.21   ? 4262 GLN A NE2   1 
ATOM   20384 N  N     . ARG A 1 4263 ? 56.196  110.435 103.307 1.00 6.00   ? 4263 ARG A N     1 
ATOM   20385 C  CA    . ARG A 1 4263 ? 55.105  111.388 103.146 1.00 6.32   ? 4263 ARG A CA    1 
ATOM   20386 C  C     . ARG A 1 4263 ? 54.733  111.542 101.678 1.00 7.46   ? 4263 ARG A C     1 
ATOM   20387 O  O     . ARG A 1 4263 ? 53.553  111.645 101.339 1.00 8.45   ? 4263 ARG A O     1 
ATOM   20388 C  CB    . ARG A 1 4263 ? 55.491  112.739 103.750 1.00 10.03  ? 4263 ARG A CB    1 
ATOM   20389 C  CG    . ARG A 1 4263 ? 54.509  113.858 103.442 1.00 13.55  ? 4263 ARG A CG    1 
ATOM   20390 C  CD    . ARG A 1 4263 ? 54.965  115.183 104.031 1.00 19.48  ? 4263 ARG A CD    1 
ATOM   20391 N  NE    . ARG A 1 4263 ? 56.187  115.668 103.404 1.00 20.26  ? 4263 ARG A NE    1 
ATOM   20392 C  CZ    . ARG A 1 4263 ? 56.843  116.756 103.782 1.00 22.66  ? 4263 ARG A CZ    1 
ATOM   20393 N  NH1   . ARG A 1 4263 ? 56.445  117.478 104.816 1.00 18.42  ? 4263 ARG A NH1   1 
ATOM   20394 N  NH2   . ARG A 1 4263 ? 57.924  117.131 103.104 1.00 18.22  ? 4263 ARG A NH2   1 
ATOM   20395 N  N     . LEU A 1 4264 ? 55.730  111.553 100.792 1.00 6.74   ? 4264 LEU A N     1 
ATOM   20396 C  CA    . LEU A 1 4264 ? 55.461  111.640 99.359  1.00 5.59   ? 4264 LEU A CA    1 
ATOM   20397 C  C     . LEU A 1 4264 ? 54.734  110.398 98.847  1.00 6.02   ? 4264 LEU A C     1 
ATOM   20398 O  O     . LEU A 1 4264 ? 53.828  110.494 98.005  1.00 6.15   ? 4264 LEU A O     1 
ATOM   20399 C  CB    . LEU A 1 4264 ? 56.773  111.849 98.604  1.00 8.27   ? 4264 LEU A CB    1 
ATOM   20400 C  CG    . LEU A 1 4264 ? 56.688  112.017 97.091  1.00 7.14   ? 4264 LEU A CG    1 
ATOM   20401 C  CD1   . LEU A 1 4264 ? 55.840  113.230 96.762  1.00 5.65   ? 4264 LEU A CD1   1 
ATOM   20402 C  CD2   . LEU A 1 4264 ? 58.080  112.156 96.504  1.00 6.59   ? 4264 LEU A CD2   1 
ATOM   20403 N  N     . LEU A 1 4265 ? 55.137  109.218 99.321  1.00 6.57   ? 4265 LEU A N     1 
ATOM   20404 C  CA    . LEU A 1 4265 ? 54.463  107.993 98.908  1.00 5.12   ? 4265 LEU A CA    1 
ATOM   20405 C  C     . LEU A 1 4265 ? 53.022  107.968 99.407  1.00 6.04   ? 4265 LEU A C     1 
ATOM   20406 O  O     . LEU A 1 4265 ? 52.100  107.610 98.660  1.00 7.36   ? 4265 LEU A O     1 
ATOM   20407 C  CB    . LEU A 1 4265 ? 55.243  106.779 99.412  1.00 5.72   ? 4265 LEU A CB    1 
ATOM   20408 C  CG    . LEU A 1 4265 ? 54.661  105.410 99.075  1.00 6.38   ? 4265 LEU A CG    1 
ATOM   20409 C  CD1   . LEU A 1 4265 ? 54.695  105.209 97.577  1.00 5.22   ? 4265 LEU A CD1   1 
ATOM   20410 C  CD2   . LEU A 1 4265 ? 55.437  104.312 99.777  1.00 5.51   ? 4265 LEU A CD2   1 
ATOM   20411 N  N     . ASN A 1 4266 ? 52.810  108.362 100.666 1.00 5.61   ? 4266 ASN A N     1 
ATOM   20412 C  CA    . ASN A 1 4266 ? 51.457  108.546 101.181 1.00 7.49   ? 4266 ASN A CA    1 
ATOM   20413 C  C     . ASN A 1 4266 ? 50.690  109.566 100.350 1.00 8.12   ? 4266 ASN A C     1 
ATOM   20414 O  O     . ASN A 1 4266 ? 49.484  109.421 100.128 1.00 10.18  ? 4266 ASN A O     1 
ATOM   20415 C  CB    . ASN A 1 4266 ? 51.515  108.985 102.648 1.00 10.46  ? 4266 ASN A CB    1 
ATOM   20416 C  CG    . ASN A 1 4266 ? 51.912  107.858 103.592 1.00 10.31  ? 4266 ASN A CG    1 
ATOM   20417 O  OD1   . ASN A 1 4266 ? 51.438  106.730 103.470 1.00 17.93  ? 4266 ASN A OD1   1 
ATOM   20418 N  ND2   . ASN A 1 4266 ? 52.804  108.160 104.530 1.00 9.55   ? 4266 ASN A ND2   1 
ATOM   20419 N  N     . THR A 1 4267 ? 51.376  110.608 99.886  1.00 6.68   ? 4267 THR A N     1 
ATOM   20420 C  CA    . THR A 1 4267 ? 50.738  111.629 99.068  1.00 6.72   ? 4267 THR A CA    1 
ATOM   20421 C  C     . THR A 1 4267 ? 50.176  111.025 97.789  1.00 6.47   ? 4267 THR A C     1 
ATOM   20422 O  O     . THR A 1 4267 ? 48.992  111.199 97.463  1.00 7.12   ? 4267 THR A O     1 
ATOM   20423 C  CB    . THR A 1 4267 ? 51.768  112.711 98.744  1.00 10.03  ? 4267 THR A CB    1 
ATOM   20424 O  OG1   . THR A 1 4267 ? 52.219  113.333 99.955  1.00 11.34  ? 4267 THR A OG1   1 
ATOM   20425 C  CG2   . THR A 1 4267 ? 51.187  113.735 97.830  1.00 8.68   ? 4267 THR A CG2   1 
ATOM   20426 N  N     . PHE A 1 4268 ? 51.019  110.292 97.062  1.00 6.61   ? 4268 PHE A N     1 
ATOM   20427 C  CA    . PHE A 1 4268 ? 50.582  109.711 95.798  1.00 4.86   ? 4268 PHE A CA    1 
ATOM   20428 C  C     . PHE A 1 4268 ? 49.479  108.689 96.028  1.00 6.61   ? 4268 PHE A C     1 
ATOM   20429 O  O     . PHE A 1 4268 ? 48.503  108.637 95.270  1.00 7.52   ? 4268 PHE A O     1 
ATOM   20430 C  CB    . PHE A 1 4268 ? 51.759  109.080 95.061  1.00 5.19   ? 4268 PHE A CB    1 
ATOM   20431 C  CG    . PHE A 1 4268 ? 52.586  110.071 94.292  1.00 9.81   ? 4268 PHE A CG    1 
ATOM   20432 C  CD1   . PHE A 1 4268 ? 52.155  110.578 93.072  1.00 11.64  ? 4268 PHE A CD1   1 
ATOM   20433 C  CD2   . PHE A 1 4268 ? 53.805  110.488 94.791  1.00 8.77   ? 4268 PHE A CD2   1 
ATOM   20434 C  CE1   . PHE A 1 4268 ? 52.929  111.496 92.374  1.00 12.23  ? 4268 PHE A CE1   1 
ATOM   20435 C  CE2   . PHE A 1 4268 ? 54.578  111.394 94.099  1.00 7.87   ? 4268 PHE A CE2   1 
ATOM   20436 C  CZ    . PHE A 1 4268 ? 54.141  111.901 92.890  1.00 9.75   ? 4268 PHE A CZ    1 
ATOM   20437 N  N     . LEU A 1 4269 ? 49.610  107.873 97.079  1.00 6.97   ? 4269 LEU A N     1 
ATOM   20438 C  CA    . LEU A 1 4269 ? 48.574  106.886 97.367  1.00 7.13   ? 4269 LEU A CA    1 
ATOM   20439 C  C     . LEU A 1 4269 ? 47.239  107.549 97.685  1.00 7.94   ? 4269 LEU A C     1 
ATOM   20440 O  O     . LEU A 1 4269 ? 46.194  107.119 97.186  1.00 7.29   ? 4269 LEU A O     1 
ATOM   20441 C  CB    . LEU A 1 4269 ? 49.014  105.986 98.519  1.00 6.54   ? 4269 LEU A CB    1 
ATOM   20442 C  CG    . LEU A 1 4269 ? 50.124  105.006 98.144  1.00 6.59   ? 4269 LEU A CG    1 
ATOM   20443 C  CD1   . LEU A 1 4269 ? 50.696  104.343 99.385  1.00 4.95   ? 4269 LEU A CD1   1 
ATOM   20444 C  CD2   . LEU A 1 4269 ? 49.617  103.974 97.143  1.00 4.73   ? 4269 LEU A CD2   1 
ATOM   20445 N  N     . GLU A 1 4270 ? 47.248  108.602 98.507  1.00 7.85   ? 4270 GLU A N     1 
ATOM   20446 C  CA    . GLU A 1 4270 ? 45.998  109.286 98.823  1.00 9.23   ? 4270 GLU A CA    1 
ATOM   20447 C  C     . GLU A 1 4270 ? 45.389  109.935 97.590  1.00 8.46   ? 4270 GLU A C     1 
ATOM   20448 O  O     . GLU A 1 4270 ? 44.167  109.907 97.412  1.00 10.11  ? 4270 GLU A O     1 
ATOM   20449 C  CB    . GLU A 1 4270 ? 46.212  110.322 99.926  1.00 11.85  ? 4270 GLU A CB    1 
ATOM   20450 C  CG    . GLU A 1 4270 ? 46.576  109.723 101.270 1.00 18.33  ? 4270 GLU A CG    1 
ATOM   20451 C  CD    . GLU A 1 4270 ? 45.435  108.915 101.859 1.00 25.21  ? 4270 GLU A CD    1 
ATOM   20452 O  OE1   . GLU A 1 4270 ? 44.264  109.271 101.606 1.00 22.83  ? 4270 GLU A OE1   1 
ATOM   20453 O  OE2   . GLU A 1 4270 ? 45.704  107.923 102.568 1.00 28.82  ? 4270 GLU A OE2   1 
ATOM   20454 N  N     . ARG A 1 4271 ? 46.213  110.531 96.727  1.00 9.61   ? 4271 ARG A N     1 
ATOM   20455 C  CA    . ARG A 1 4271 ? 45.635  111.193 95.564  1.00 9.61   ? 4271 ARG A CA    1 
ATOM   20456 C  C     . ARG A 1 4271 ? 45.095  110.189 94.552  1.00 9.92   ? 4271 ARG A C     1 
ATOM   20457 O  O     . ARG A 1 4271 ? 44.090  110.464 93.886  1.00 11.81  ? 4271 ARG A O     1 
ATOM   20458 C  CB    . ARG A 1 4271 ? 46.659  112.100 94.888  1.00 10.25  ? 4271 ARG A CB    1 
ATOM   20459 C  CG    . ARG A 1 4271 ? 46.016  113.162 94.010  1.00 15.09  ? 4271 ARG A CG    1 
ATOM   20460 C  CD    . ARG A 1 4271 ? 47.013  113.849 93.099  1.00 24.00  ? 4271 ARG A CD    1 
ATOM   20461 N  NE    . ARG A 1 4271 ? 47.412  112.967 92.009  1.00 20.94  ? 4271 ARG A NE    1 
ATOM   20462 C  CZ    . ARG A 1 4271 ? 48.666  112.719 91.660  1.00 23.92  ? 4271 ARG A CZ    1 
ATOM   20463 N  NH1   . ARG A 1 4271 ? 49.683  113.297 92.277  1.00 20.76  ? 4271 ARG A NH1   1 
ATOM   20464 N  NH2   . ARG A 1 4271 ? 48.906  111.873 90.661  1.00 29.03  ? 4271 ARG A NH2   1 
ATOM   20465 N  N     . LEU A 1 4272 ? 45.734  109.027 94.422  1.00 7.06   ? 4272 LEU A N     1 
ATOM   20466 C  CA    . LEU A 1 4272 ? 45.437  108.100 93.336  1.00 7.98   ? 4272 LEU A CA    1 
ATOM   20467 C  C     . LEU A 1 4272 ? 44.394  107.043 93.682  1.00 8.61   ? 4272 LEU A C     1 
ATOM   20468 O  O     . LEU A 1 4272 ? 43.609  106.659 92.810  1.00 9.39   ? 4272 LEU A O     1 
ATOM   20469 C  CB    . LEU A 1 4272 ? 46.725  107.410 92.874  1.00 7.41   ? 4272 LEU A CB    1 
ATOM   20470 C  CG    . LEU A 1 4272 ? 47.761  108.305 92.194  1.00 6.50   ? 4272 LEU A CG    1 
ATOM   20471 C  CD1   . LEU A 1 4272 ? 49.057  107.548 91.960  1.00 4.93   ? 4272 LEU A CD1   1 
ATOM   20472 C  CD2   . LEU A 1 4272 ? 47.204  108.829 90.882  1.00 9.26   ? 4272 LEU A CD2   1 
ATOM   20473 N  N     . PHE A 1 4273 ? 44.357  106.554 94.919  1.00 9.68   ? 4273 PHE A N     1 
ATOM   20474 C  CA    . PHE A 1 4273 ? 43.486  105.438 95.291  1.00 9.06   ? 4273 PHE A CA    1 
ATOM   20475 C  C     . PHE A 1 4273 ? 42.346  105.953 96.167  1.00 10.06  ? 4273 PHE A C     1 
ATOM   20476 O  O     . PHE A 1 4273 ? 42.406  105.909 97.396  1.00 11.45  ? 4273 PHE A O     1 
ATOM   20477 C  CB    . PHE A 1 4273 ? 44.291  104.339 96.000  1.00 7.96   ? 4273 PHE A CB    1 
ATOM   20478 C  CG    . PHE A 1 4273 ? 45.258  103.621 95.104  1.00 6.62   ? 4273 PHE A CG    1 
ATOM   20479 C  CD1   . PHE A 1 4273 ? 44.858  102.506 94.385  1.00 6.77   ? 4273 PHE A CD1   1 
ATOM   20480 C  CD2   . PHE A 1 4273 ? 46.566  104.058 94.979  1.00 7.16   ? 4273 PHE A CD2   1 
ATOM   20481 C  CE1   . PHE A 1 4273 ? 45.744  101.840 93.558  1.00 4.45   ? 4273 PHE A CE1   1 
ATOM   20482 C  CE2   . PHE A 1 4273 ? 47.457  103.396 94.152  1.00 8.86   ? 4273 PHE A CE2   1 
ATOM   20483 C  CZ    . PHE A 1 4273 ? 47.045  102.286 93.442  1.00 5.69   ? 4273 PHE A CZ    1 
ATOM   20484 N  N     . THR A 1 4274 ? 41.286  106.433 95.514  1.00 10.54  ? 4274 THR A N     1 
ATOM   20485 C  CA    . THR A 1 4274 ? 40.056  106.848 96.178  1.00 9.94   ? 4274 THR A CA    1 
ATOM   20486 C  C     . THR A 1 4274 ? 38.871  106.437 95.316  1.00 12.25  ? 4274 THR A C     1 
ATOM   20487 O  O     . THR A 1 4274 ? 39.029  105.933 94.201  1.00 16.96  ? 4274 THR A O     1 
ATOM   20488 C  CB    . THR A 1 4274 ? 40.000  108.364 96.429  1.00 14.26  ? 4274 THR A CB    1 
ATOM   20489 O  OG1   . THR A 1 4274 ? 39.878  109.055 95.179  1.00 18.99  ? 4274 THR A OG1   1 
ATOM   20490 C  CG2   . THR A 1 4274 ? 41.225  108.862 97.173  1.00 11.98  ? 4274 THR A CG2   1 
ATOM   20491 N  N     . THR A 1 4275 ? 37.667  106.666 95.846  1.00 14.69  ? 4275 THR A N     1 
ATOM   20492 C  CA    . THR A 1 4275 ? 36.461  106.518 95.039  1.00 15.71  ? 4275 THR A CA    1 
ATOM   20493 C  C     . THR A 1 4275 ? 36.450  107.499 93.874  1.00 20.39  ? 4275 THR A C     1 
ATOM   20494 O  O     . THR A 1 4275 ? 35.934  107.177 92.797  1.00 26.89  ? 4275 THR A O     1 
ATOM   20495 C  CB    . THR A 1 4275 ? 35.220  106.719 95.910  1.00 17.40  ? 4275 THR A CB    1 
ATOM   20496 O  OG1   . THR A 1 4275 ? 35.393  106.035 97.157  1.00 18.98  ? 4275 THR A OG1   1 
ATOM   20497 C  CG2   . THR A 1 4275 ? 33.978  106.191 95.211  1.00 22.28  ? 4275 THR A CG2   1 
ATOM   20498 N  N     . ARG A 1 4276 ? 37.033  108.686 94.067  1.00 19.00  ? 4276 ARG A N     1 
ATOM   20499 C  CA    . ARG A 1 4276 ? 37.026  109.713 93.033  1.00 22.74  ? 4276 ARG A CA    1 
ATOM   20500 C  C     . ARG A 1 4276 ? 37.722  109.250 91.760  1.00 20.74  ? 4276 ARG A C     1 
ATOM   20501 O  O     . ARG A 1 4276 ? 37.477  109.818 90.690  1.00 23.38  ? 4276 ARG A O     1 
ATOM   20502 C  CB    . ARG A 1 4276 ? 37.701  110.985 93.550  1.00 22.48  ? 4276 ARG A CB    1 
ATOM   20503 C  CG    . ARG A 1 4276 ? 37.003  111.669 94.724  1.00 33.06  ? 4276 ARG A CG    1 
ATOM   20504 C  CD    . ARG A 1 4276 ? 35.628  112.224 94.377  1.00 44.14  ? 4276 ARG A CD    1 
ATOM   20505 N  NE    . ARG A 1 4276 ? 34.582  111.217 94.518  1.00 47.57  ? 4276 ARG A NE    1 
ATOM   20506 C  CZ    . ARG A 1 4276 ? 33.346  111.345 94.055  1.00 49.24  ? 4276 ARG A CZ    1 
ATOM   20507 N  NH1   . ARG A 1 4276 ? 32.960  112.434 93.410  1.00 44.91  ? 4276 ARG A NH1   1 
ATOM   20508 N  NH2   . ARG A 1 4276 ? 32.477  110.357 94.244  1.00 43.52  ? 4276 ARG A NH2   1 
ATOM   20509 N  N     . SER A 1 4277 ? 38.586  108.236 91.855  1.00 17.15  ? 4277 SER A N     1 
ATOM   20510 C  CA    . SER A 1 4277 ? 39.253  107.699 90.675  1.00 16.64  ? 4277 SER A CA    1 
ATOM   20511 C  C     . SER A 1 4277 ? 38.273  107.080 89.689  1.00 20.07  ? 4277 SER A C     1 
ATOM   20512 O  O     . SER A 1 4277 ? 38.621  106.902 88.516  1.00 23.28  ? 4277 SER A O     1 
ATOM   20513 C  CB    . SER A 1 4277 ? 40.294  106.657 91.088  1.00 15.57  ? 4277 SER A CB    1 
ATOM   20514 O  OG    . SER A 1 4277 ? 41.426  107.268 91.680  1.00 17.02  ? 4277 SER A OG    1 
ATOM   20515 N  N     . PHE A 1 4278 ? 37.063  106.746 90.130  1.00 19.07  ? 4278 PHE A N     1 
ATOM   20516 C  CA    . PHE A 1 4278 ? 36.067  106.142 89.257  1.00 22.57  ? 4278 PHE A CA    1 
ATOM   20517 C  C     . PHE A 1 4278 ? 35.111  107.160 88.651  1.00 28.84  ? 4278 PHE A C     1 
ATOM   20518 O  O     . PHE A 1 4278 ? 34.158  106.766 87.972  1.00 32.53  ? 4278 PHE A O     1 
ATOM   20519 C  CB    . PHE A 1 4278 ? 35.283  105.071 90.019  1.00 21.73  ? 4278 PHE A CB    1 
ATOM   20520 C  CG    . PHE A 1 4278 ? 36.003  103.760 90.115  1.00 18.08  ? 4278 PHE A CG    1 
ATOM   20521 C  CD1   . PHE A 1 4278 ? 37.128  103.629 90.911  1.00 18.39  ? 4278 PHE A CD1   1 
ATOM   20522 C  CD2   . PHE A 1 4278 ? 35.569  102.663 89.393  1.00 17.31  ? 4278 PHE A CD2   1 
ATOM   20523 C  CE1   . PHE A 1 4278 ? 37.799  102.427 90.993  1.00 14.60  ? 4278 PHE A CE1   1 
ATOM   20524 C  CE2   . PHE A 1 4278 ? 36.238  101.461 89.470  1.00 16.17  ? 4278 PHE A CE2   1 
ATOM   20525 C  CZ    . PHE A 1 4278 ? 37.353  101.342 90.271  1.00 17.79  ? 4278 PHE A CZ    1 
ATOM   20526 N  N     . ASP A 1 4279 ? 35.341  108.450 88.878  1.00 28.92  ? 4279 ASP A N     1 
ATOM   20527 C  CA    . ASP A 1 4279 ? 34.523  109.486 88.274  1.00 35.62  ? 4279 ASP A CA    1 
ATOM   20528 C  C     . ASP A 1 4279 ? 34.935  109.717 86.824  1.00 46.65  ? 4279 ASP A C     1 
ATOM   20529 O  O     . ASP A 1 4279 ? 35.969  109.232 86.355  1.00 46.09  ? 4279 ASP A O     1 
ATOM   20530 C  CB    . ASP A 1 4279 ? 34.640  110.792 89.058  1.00 39.24  ? 4279 ASP A CB    1 
ATOM   20531 C  CG    . ASP A 1 4279 ? 34.147  110.662 90.481  1.00 40.32  ? 4279 ASP A CG    1 
ATOM   20532 O  OD1   . ASP A 1 4279 ? 33.363  109.730 90.759  1.00 47.19  ? 4279 ASP A OD1   1 
ATOM   20533 O  OD2   . ASP A 1 4279 ? 34.546  111.493 91.321  1.00 32.15  ? 4279 ASP A OD2   1 
ATOM   20534 N  N     . SER A 1 4280 ? 34.101  110.474 86.109  1.00 48.70  ? 4280 SER A N     1 
ATOM   20535 C  CA    . SER A 1 4280 ? 34.397  110.783 84.714  1.00 49.69  ? 4280 SER A CA    1 
ATOM   20536 C  C     . SER A 1 4280 ? 35.493  111.836 84.598  1.00 53.73  ? 4280 SER A C     1 
ATOM   20537 O  O     . SER A 1 4280 ? 36.294  111.802 83.657  1.00 54.31  ? 4280 SER A O     1 
ATOM   20538 C  CB    . SER A 1 4280 ? 33.128  111.248 84.001  1.00 58.52  ? 4280 SER A CB    1 
ATOM   20539 O  OG    . SER A 1 4280 ? 32.104  110.275 84.096  1.00 64.54  ? 4280 SER A OG    1 
ATOM   20540 N  N     . GLU A 1 4281 ? 35.547  112.777 85.542  1.00 52.19  ? 4281 GLU A N     1 
ATOM   20541 C  CA    . GLU A 1 4281 ? 36.474  113.901 85.479  1.00 50.99  ? 4281 GLU A CA    1 
ATOM   20542 C  C     . GLU A 1 4281 ? 37.641  113.759 86.452  1.00 47.39  ? 4281 GLU A C     1 
ATOM   20543 O  O     . GLU A 1 4281 ? 38.222  114.766 86.871  1.00 42.72  ? 4281 GLU A O     1 
ATOM   20544 C  CB    . GLU A 1 4281 ? 35.735  115.216 85.730  1.00 55.98  ? 4281 GLU A CB    1 
ATOM   20545 C  CG    . GLU A 1 4281 ? 34.742  115.601 84.642  1.00 66.22  ? 4281 GLU A CG    1 
ATOM   20546 C  CD    . GLU A 1 4281 ? 33.399  114.913 84.795  1.00 73.67  ? 4281 GLU A CD    1 
ATOM   20547 O  OE1   . GLU A 1 4281 ? 33.213  114.178 85.788  1.00 72.68  ? 4281 GLU A OE1   1 
ATOM   20548 O  OE2   . GLU A 1 4281 ? 32.529  115.108 83.921  1.00 65.27  ? 4281 GLU A OE2   1 
ATOM   20549 N  N     . PHE A 1 4282 ? 37.994  112.532 86.828  1.00 44.43  ? 4282 PHE A N     1 
ATOM   20550 C  CA    . PHE A 1 4282 ? 39.182  112.320 87.642  1.00 29.09  ? 4282 PHE A CA    1 
ATOM   20551 C  C     . PHE A 1 4282 ? 40.425  112.747 86.871  1.00 26.86  ? 4282 PHE A C     1 
ATOM   20552 O  O     . PHE A 1 4282 ? 40.504  112.586 85.651  1.00 29.37  ? 4282 PHE A O     1 
ATOM   20553 C  CB    . PHE A 1 4282 ? 39.295  110.855 88.061  1.00 27.45  ? 4282 PHE A CB    1 
ATOM   20554 C  CG    . PHE A 1 4282 ? 40.434  110.581 89.000  1.00 19.85  ? 4282 PHE A CG    1 
ATOM   20555 C  CD1   . PHE A 1 4282 ? 40.518  111.234 90.218  1.00 19.51  ? 4282 PHE A CD1   1 
ATOM   20556 C  CD2   . PHE A 1 4282 ? 41.427  109.679 88.659  1.00 19.58  ? 4282 PHE A CD2   1 
ATOM   20557 C  CE1   . PHE A 1 4282 ? 41.567  110.986 91.082  1.00 17.73  ? 4282 PHE A CE1   1 
ATOM   20558 C  CE2   . PHE A 1 4282 ? 42.479  109.426 89.519  1.00 24.33  ? 4282 PHE A CE2   1 
ATOM   20559 C  CZ    . PHE A 1 4282 ? 42.548  110.081 90.731  1.00 19.76  ? 4282 PHE A CZ    1 
ATOM   20560 N  N     . LYS A 1 4283 ? 41.398  113.304 87.589  1.00 26.58  ? 4283 LYS A N     1 
ATOM   20561 C  CA    . LYS A 1 4283 ? 42.563  113.928 86.969  1.00 23.95  ? 4283 LYS A CA    1 
ATOM   20562 C  C     . LYS A 1 4283 ? 43.823  113.268 87.513  1.00 24.91  ? 4283 LYS A C     1 
ATOM   20563 O  O     . LYS A 1 4283 ? 44.186  113.482 88.674  1.00 30.51  ? 4283 LYS A O     1 
ATOM   20564 C  CB    . LYS A 1 4283 ? 42.567  115.433 87.237  1.00 27.53  ? 4283 LYS A CB    1 
ATOM   20565 C  CG    . LYS A 1 4283 ? 41.809  116.233 86.192  1.00 34.78  ? 4283 LYS A CG    1 
ATOM   20566 C  CD    . LYS A 1 4283 ? 41.789  117.715 86.516  1.00 46.50  ? 4283 LYS A CD    1 
ATOM   20567 C  CE    . LYS A 1 4283 ? 41.136  118.506 85.394  1.00 46.63  ? 4283 LYS A CE    1 
ATOM   20568 N  NZ    . LYS A 1 4283 ? 41.516  119.944 85.429  1.00 46.66  ? 4283 LYS A NZ    1 
ATOM   20569 N  N     . LEU A 1 4284 ? 44.485  112.465 86.676  1.00 25.12  ? 4284 LEU A N     1 
ATOM   20570 C  CA    . LEU A 1 4284 ? 45.722  111.813 87.097  1.00 19.44  ? 4284 LEU A CA    1 
ATOM   20571 C  C     . LEU A 1 4284 ? 46.822  112.832 87.364  1.00 22.32  ? 4284 LEU A C     1 
ATOM   20572 O  O     . LEU A 1 4284 ? 47.567  112.714 88.344  1.00 20.79  ? 4284 LEU A O     1 
ATOM   20573 C  CB    . LEU A 1 4284 ? 46.172  110.807 86.038  1.00 12.03  ? 4284 LEU A CB    1 
ATOM   20574 C  CG    . LEU A 1 4284 ? 45.311  109.556 85.855  1.00 13.09  ? 4284 LEU A CG    1 
ATOM   20575 C  CD1   . LEU A 1 4284 ? 45.376  109.071 84.415  1.00 11.23  ? 4284 LEU A CD1   1 
ATOM   20576 C  CD2   . LEU A 1 4284 ? 45.744  108.458 86.814  1.00 10.59  ? 4284 LEU A CD2   1 
ATOM   20577 N  N     . ALA A 1 4285 ? 46.939  113.838 86.501  1.00 24.51  ? 4285 ALA A N     1 
ATOM   20578 C  CA    . ALA A 1 4285 ? 47.935  114.888 86.644  1.00 23.56  ? 4285 ALA A CA    1 
ATOM   20579 C  C     . ALA A 1 4285 ? 47.293  116.219 86.288  1.00 29.21  ? 4285 ALA A C     1 
ATOM   20580 O  O     . ALA A 1 4285 ? 46.350  116.274 85.495  1.00 32.67  ? 4285 ALA A O     1 
ATOM   20581 C  CB    . ALA A 1 4285 ? 49.160  114.627 85.759  1.00 20.60  ? 4285 ALA A CB    1 
ATOM   20582 N  N     . CYS A 1 4286 ? 47.804  117.294 86.885  1.00 35.42  ? 4286 CYS A N     1 
ATOM   20583 C  CA    . CYS A 1 4286 ? 47.231  118.624 86.727  1.00 44.59  ? 4286 CYS A CA    1 
ATOM   20584 C  C     . CYS A 1 4286 ? 48.291  119.600 86.236  1.00 41.96  ? 4286 CYS A C     1 
ATOM   20585 O  O     . CYS A 1 4286 ? 49.377  119.688 86.819  1.00 41.73  ? 4286 CYS A O     1 
ATOM   20586 C  CB    . CYS A 1 4286 ? 46.629  119.119 88.044  1.00 49.20  ? 4286 CYS A CB    1 
ATOM   20587 S  SG    . CYS A 1 4286 ? 45.203  118.166 88.614  1.00 67.49  ? 4286 CYS A SG    1 
ATOM   20588 N  N     . LYS A 1 4287 ? 47.965  120.332 85.168  1.00 47.05  ? 4287 LYS A N     1 
ATOM   20589 C  CA    . LYS A 1 4287 ? 48.798  121.414 84.639  1.00 57.26  ? 4287 LYS A CA    1 
ATOM   20590 C  C     . LYS A 1 4287 ? 50.206  120.919 84.299  1.00 50.29  ? 4287 LYS A C     1 
ATOM   20591 O  O     . LYS A 1 4287 ? 51.210  121.373 84.852  1.00 48.48  ? 4287 LYS A O     1 
ATOM   20592 C  CB    . LYS A 1 4287 ? 48.845  122.594 85.617  1.00 62.46  ? 4287 LYS A CB    1 
ATOM   20593 C  CG    . LYS A 1 4287 ? 47.775  123.657 85.384  1.00 64.21  ? 4287 LYS A CG    1 
ATOM   20594 C  CD    . LYS A 1 4287 ? 46.366  123.083 85.451  1.00 63.79  ? 4287 LYS A CD    1 
ATOM   20595 C  CE    . LYS A 1 4287 ? 46.025  122.603 86.852  1.00 60.60  ? 4287 LYS A CE    1 
ATOM   20596 N  NZ    . LYS A 1 4287 ? 44.656  122.020 86.917  1.00 61.17  ? 4287 LYS A NZ    1 
ATOM   20597 N  N     . VAL A 1 4288 ? 50.260  119.968 83.366  1.00 46.25  ? 4288 VAL A N     1 
ATOM   20598 C  CA    . VAL A 1 4288 ? 51.546  119.428 82.935  1.00 41.22  ? 4288 VAL A CA    1 
ATOM   20599 C  C     . VAL A 1 4288 ? 52.317  120.458 82.114  1.00 49.42  ? 4288 VAL A C     1 
ATOM   20600 O  O     . VAL A 1 4288 ? 53.525  120.643 82.300  1.00 43.94  ? 4288 VAL A O     1 
ATOM   20601 C  CB    . VAL A 1 4288 ? 51.345  118.106 82.169  1.00 33.43  ? 4288 VAL A CB    1 
ATOM   20602 C  CG1   . VAL A 1 4288 ? 50.748  117.058 83.088  1.00 28.63  ? 4288 VAL A CG1   1 
ATOM   20603 C  CG2   . VAL A 1 4288 ? 50.431  118.308 80.970  1.00 41.18  ? 4288 VAL A CG2   1 
ATOM   20604 N  N     . ASP A 1 4289 ? 51.634  121.147 81.199  1.00 56.30  ? 4289 ASP A N     1 
ATOM   20605 C  CA    . ASP A 1 4289 ? 52.260  122.143 80.339  1.00 56.52  ? 4289 ASP A CA    1 
ATOM   20606 C  C     . ASP A 1 4289 ? 51.710  123.546 80.577  1.00 60.33  ? 4289 ASP A C     1 
ATOM   20607 O  O     . ASP A 1 4289 ? 51.711  124.374 79.661  1.00 67.20  ? 4289 ASP A O     1 
ATOM   20608 C  CB    . ASP A 1 4289 ? 52.104  121.747 78.869  1.00 58.41  ? 4289 ASP A CB    1 
ATOM   20609 C  CG    . ASP A 1 4289 ? 50.651  121.639 78.439  1.00 63.95  ? 4289 ASP A CG    1 
ATOM   20610 O  OD1   . ASP A 1 4289 ? 49.753  121.819 79.288  1.00 63.50  ? 4289 ASP A OD1   1 
ATOM   20611 O  OD2   . ASP A 1 4289 ? 50.406  121.370 77.244  1.00 65.58  ? 4289 ASP A OD2   1 
ATOM   20612 N  N     . GLY A 1 4290 ? 51.243  123.827 81.787  1.00 61.60  ? 4290 GLY A N     1 
ATOM   20613 C  CA    . GLY A 1 4290 ? 50.654  125.110 82.129  1.00 64.86  ? 4290 GLY A CA    1 
ATOM   20614 C  C     . GLY A 1 4290 ? 49.153  125.180 81.943  1.00 75.09  ? 4290 GLY A C     1 
ATOM   20615 O  O     . GLY A 1 4290 ? 48.450  125.747 82.782  1.00 79.64  ? 4290 GLY A O     1 
ATOM   20616 N  N     . HIS A 1 4291 ? 48.645  124.611 80.851  1.00 76.64  ? 4291 HIS A N     1 
ATOM   20617 C  CA    . HIS A 1 4291 ? 47.218  124.638 80.554  1.00 77.39  ? 4291 HIS A CA    1 
ATOM   20618 C  C     . HIS A 1 4291 ? 46.595  123.252 80.529  1.00 74.41  ? 4291 HIS A C     1 
ATOM   20619 O  O     . HIS A 1 4291 ? 45.602  123.011 81.225  1.00 74.08  ? 4291 HIS A O     1 
ATOM   20620 C  CB    . HIS A 1 4291 ? 46.975  125.345 79.211  1.00 79.66  ? 4291 HIS A CB    1 
ATOM   20621 C  CG    . HIS A 1 4291 ? 47.361  126.791 79.212  1.00 85.22  ? 4291 HIS A CG    1 
ATOM   20622 N  ND1   . HIS A 1 4291 ? 48.635  127.222 78.910  1.00 85.53  ? 4291 HIS A ND1   1 
ATOM   20623 C  CD2   . HIS A 1 4291 ? 46.641  127.907 79.480  1.00 84.02  ? 4291 HIS A CD2   1 
ATOM   20624 C  CE1   . HIS A 1 4291 ? 48.683  128.540 78.990  1.00 86.26  ? 4291 HIS A CE1   1 
ATOM   20625 N  NE2   . HIS A 1 4291 ? 47.486  128.980 79.335  1.00 86.27  ? 4291 HIS A NE2   1 
ATOM   20626 N  N     . LYS A 1 4292 ? 47.151  122.329 79.748  1.00 67.59  ? 4292 LYS A N     1 
ATOM   20627 C  CA    . LYS A 1 4292 ? 46.572  121.003 79.613  1.00 57.86  ? 4292 LYS A CA    1 
ATOM   20628 C  C     . LYS A 1 4292 ? 46.972  120.113 80.787  1.00 54.34  ? 4292 LYS A C     1 
ATOM   20629 O  O     . LYS A 1 4292 ? 47.882  120.420 81.562  1.00 55.56  ? 4292 LYS A O     1 
ATOM   20630 C  CB    . LYS A 1 4292 ? 46.999  120.361 78.293  1.00 60.62  ? 4292 LYS A CB    1 
ATOM   20631 C  CG    . LYS A 1 4292 ? 46.760  121.230 77.070  1.00 73.65  ? 4292 LYS A CG    1 
ATOM   20632 C  CD    . LYS A 1 4292 ? 47.259  120.546 75.807  1.00 70.37  ? 4292 LYS A CD    1 
ATOM   20633 C  CE    . LYS A 1 4292 ? 47.331  121.519 74.643  1.00 71.51  ? 4292 LYS A CE    1 
ATOM   20634 N  NZ    . LYS A 1 4292 ? 48.255  122.652 74.925  1.00 72.94  ? 4292 LYS A NZ    1 
ATOM   20635 N  N     . ASP A 1 4293 ? 46.270  118.989 80.910  1.00 53.03  ? 4293 ASP A N     1 
ATOM   20636 C  CA    . ASP A 1 4293 ? 46.525  118.029 81.974  1.00 44.00  ? 4293 ASP A CA    1 
ATOM   20637 C  C     . ASP A 1 4293 ? 46.010  116.661 81.541  1.00 36.19  ? 4293 ASP A C     1 
ATOM   20638 O  O     . ASP A 1 4293 ? 45.307  116.529 80.537  1.00 35.36  ? 4293 ASP A O     1 
ATOM   20639 C  CB    . ASP A 1 4293 ? 45.922  118.510 83.305  1.00 45.06  ? 4293 ASP A CB    1 
ATOM   20640 C  CG    . ASP A 1 4293 ? 44.398  118.574 83.297  1.00 44.43  ? 4293 ASP A CG    1 
ATOM   20641 O  OD1   . ASP A 1 4293 ? 43.735  117.889 82.493  1.00 44.73  ? 4293 ASP A OD1   1 
ATOM   20642 O  OD2   . ASP A 1 4293 ? 43.857  119.346 84.114  1.00 46.63  ? 4293 ASP A OD2   1 
ATOM   20643 N  N     . ILE A 1 4294 ? 46.371  115.643 82.317  1.00 31.45  ? 4294 ILE A N     1 
ATOM   20644 C  CA    . ILE A 1 4294 ? 46.133  114.249 81.958  1.00 25.33  ? 4294 ILE A CA    1 
ATOM   20645 C  C     . ILE A 1 4294 ? 44.858  113.776 82.642  1.00 23.76  ? 4294 ILE A C     1 
ATOM   20646 O  O     . ILE A 1 4294 ? 44.775  113.754 83.876  1.00 23.18  ? 4294 ILE A O     1 
ATOM   20647 C  CB    . ILE A 1 4294 ? 47.329  113.364 82.340  1.00 18.95  ? 4294 ILE A CB    1 
ATOM   20648 C  CG1   . ILE A 1 4294 ? 48.624  113.960 81.782  1.00 23.53  ? 4294 ILE A CG1   1 
ATOM   20649 C  CG2   . ILE A 1 4294 ? 47.128  111.944 81.836  1.00 12.43  ? 4294 ILE A CG2   1 
ATOM   20650 C  CD1   . ILE A 1 4294 ? 49.863  113.161 82.113  1.00 17.68  ? 4294 ILE A CD1   1 
ATOM   20651 N  N     . GLN A 1 4295 ? 43.866  113.398 81.843  1.00 27.08  ? 4295 GLN A N     1 
ATOM   20652 C  CA    . GLN A 1 4295 ? 42.579  112.940 82.344  1.00 21.48  ? 4295 GLN A CA    1 
ATOM   20653 C  C     . GLN A 1 4295 ? 42.602  111.447 82.656  1.00 17.57  ? 4295 GLN A C     1 
ATOM   20654 O  O     . GLN A 1 4295 ? 43.415  110.683 82.129  1.00 18.82  ? 4295 GLN A O     1 
ATOM   20655 C  CB    . GLN A 1 4295 ? 41.469  113.235 81.332  1.00 23.86  ? 4295 GLN A CB    1 
ATOM   20656 C  CG    . GLN A 1 4295 ? 41.273  114.708 80.983  1.00 26.34  ? 4295 GLN A CG    1 
ATOM   20657 C  CD    . GLN A 1 4295 ? 41.258  115.625 82.196  1.00 39.13  ? 4295 GLN A CD    1 
ATOM   20658 O  OE1   . GLN A 1 4295 ? 40.795  115.249 83.274  1.00 40.00  ? 4295 GLN A OE1   1 
ATOM   20659 N  NE2   . GLN A 1 4295 ? 41.761  116.840 82.020  1.00 40.21  ? 4295 GLN A NE2   1 
ATOM   20660 N  N     . MET A 1 4296 ? 41.689  111.043 83.530  1.00 21.43  ? 4296 MET A N     1 
ATOM   20661 C  CA    . MET A 1 4296 ? 41.462  109.631 83.809  1.00 20.45  ? 4296 MET A CA    1 
ATOM   20662 C  C     . MET A 1 4296 ? 40.655  109.013 82.675  1.00 20.46  ? 4296 MET A C     1 
ATOM   20663 O  O     . MET A 1 4296 ? 39.568  109.510 82.362  1.00 32.08  ? 4296 MET A O     1 
ATOM   20664 C  CB    . MET A 1 4296 ? 40.722  109.467 85.128  1.00 24.54  ? 4296 MET A CB    1 
ATOM   20665 C  CG    . MET A 1 4296 ? 40.529  108.035 85.595  1.00 20.67  ? 4296 MET A CG    1 
ATOM   20666 S  SD    . MET A 1 4296 ? 42.033  107.249 86.196  1.00 23.24  ? 4296 MET A SD    1 
ATOM   20667 C  CE    . MET A 1 4296 ? 41.604  105.528 85.973  1.00 16.81  ? 4296 MET A CE    1 
ATOM   20668 N  N     . PRO A 1 4297 ? 41.143  107.953 82.032  1.00 18.79  ? 4297 PRO A N     1 
ATOM   20669 C  CA    . PRO A 1 4297 ? 40.369  107.330 80.952  1.00 23.20  ? 4297 PRO A CA    1 
ATOM   20670 C  C     . PRO A 1 4297 ? 39.034  106.803 81.455  1.00 30.55  ? 4297 PRO A C     1 
ATOM   20671 O  O     . PRO A 1 4297 ? 38.927  106.288 82.570  1.00 33.30  ? 4297 PRO A O     1 
ATOM   20672 C  CB    . PRO A 1 4297 ? 41.277  106.191 80.472  1.00 16.79  ? 4297 PRO A CB    1 
ATOM   20673 C  CG    . PRO A 1 4297 ? 42.219  105.945 81.600  1.00 17.31  ? 4297 PRO A CG    1 
ATOM   20674 C  CD    . PRO A 1 4297 ? 42.425  107.269 82.264  1.00 17.66  ? 4297 PRO A CD    1 
ATOM   20675 N  N     . ASP A 1 4298 ? 38.011  106.940 80.618  1.00 34.84  ? 4298 ASP A N     1 
ATOM   20676 C  CA    . ASP A 1 4298 ? 36.672  106.448 80.940  1.00 39.04  ? 4298 ASP A CA    1 
ATOM   20677 C  C     . ASP A 1 4298 ? 36.486  105.006 80.477  1.00 38.32  ? 4298 ASP A C     1 
ATOM   20678 O  O     . ASP A 1 4298 ? 35.544  104.675 79.759  1.00 42.52  ? 4298 ASP A O     1 
ATOM   20679 C  CB    . ASP A 1 4298 ? 35.622  107.363 80.325  1.00 40.77  ? 4298 ASP A CB    1 
ATOM   20680 C  CG    . ASP A 1 4298 ? 35.576  108.725 80.989  1.00 50.42  ? 4298 ASP A CG    1 
ATOM   20681 O  OD1   . ASP A 1 4298 ? 35.894  108.810 82.194  1.00 53.59  ? 4298 ASP A OD1   1 
ATOM   20682 O  OD2   . ASP A 1 4298 ? 35.225  109.711 80.307  1.00 51.52  ? 4298 ASP A OD2   1 
ATOM   20683 N  N     . GLY A 1 4299 ? 37.400  104.137 80.892  1.00 30.31  ? 4299 GLY A N     1 
ATOM   20684 C  CA    . GLY A 1 4299 ? 37.356  102.734 80.534  1.00 32.22  ? 4299 GLY A CA    1 
ATOM   20685 C  C     . GLY A 1 4299 ? 36.880  101.867 81.684  1.00 34.85  ? 4299 GLY A C     1 
ATOM   20686 O  O     . GLY A 1 4299 ? 37.021  102.224 82.851  1.00 35.35  ? 4299 GLY A O     1 
ATOM   20687 N  N     . ILE A 1 4300 ? 36.297  100.720 81.339  1.00 29.95  ? 4300 ILE A N     1 
ATOM   20688 C  CA    . ILE A 1 4300 ? 35.836  99.764  82.339  1.00 26.42  ? 4300 ILE A CA    1 
ATOM   20689 C  C     . ILE A 1 4300 ? 36.360  98.373  82.003  1.00 30.42  ? 4300 ILE A C     1 
ATOM   20690 O  O     . ILE A 1 4300 ? 36.123  97.414  82.746  1.00 36.85  ? 4300 ILE A O     1 
ATOM   20691 C  CB    . ILE A 1 4300 ? 34.300  99.766  82.456  1.00 32.23  ? 4300 ILE A CB    1 
ATOM   20692 C  CG1   . ILE A 1 4300 ? 33.656  99.320  81.143  1.00 38.92  ? 4300 ILE A CG1   1 
ATOM   20693 C  CG2   . ILE A 1 4300 ? 33.792  101.142 82.875  1.00 34.24  ? 4300 ILE A CG2   1 
ATOM   20694 C  CD1   . ILE A 1 4300 ? 32.145  99.306  81.183  1.00 37.16  ? 4300 ILE A CD1   1 
ATOM   20695 N  N     . ARG A 1 4301 ? 37.074  98.250  80.887  1.00 28.86  ? 4301 ARG A N     1 
ATOM   20696 C  CA    . ARG A 1 4301 ? 37.755  97.015  80.533  1.00 26.30  ? 4301 ARG A CA    1 
ATOM   20697 C  C     . ARG A 1 4301 ? 39.220  97.303  80.230  1.00 21.03  ? 4301 ARG A C     1 
ATOM   20698 O  O     . ARG A 1 4301 ? 39.606  98.440  79.948  1.00 22.54  ? 4301 ARG A O     1 
ATOM   20699 C  CB    . ARG A 1 4301 ? 37.098  96.311  79.334  1.00 38.64  ? 4301 ARG A CB    1 
ATOM   20700 C  CG    . ARG A 1 4301 ? 35.667  95.858  79.584  1.00 39.82  ? 4301 ARG A CG    1 
ATOM   20701 C  CD    . ARG A 1 4301 ? 34.967  95.430  78.299  1.00 48.23  ? 4301 ARG A CD    1 
ATOM   20702 N  NE    . ARG A 1 4301 ? 34.749  96.529  77.368  1.00 58.34  ? 4301 ARG A NE    1 
ATOM   20703 C  CZ    . ARG A 1 4301 ? 35.260  96.582  76.145  1.00 61.44  ? 4301 ARG A CZ    1 
ATOM   20704 N  NH1   . ARG A 1 4301 ? 36.027  95.613  75.674  1.00 56.57  ? 4301 ARG A NH1   1 
ATOM   20705 N  NH2   . ARG A 1 4301 ? 34.995  97.635  75.376  1.00 58.27  ? 4301 ARG A NH2   1 
ATOM   20706 N  N     . ARG A 1 4302 ? 40.033  96.244  80.289  1.00 20.54  ? 4302 ARG A N     1 
ATOM   20707 C  CA    . ARG A 1 4302 ? 41.481  96.404  80.179  1.00 21.25  ? 4302 ARG A CA    1 
ATOM   20708 C  C     . ARG A 1 4302 ? 41.886  96.988  78.831  1.00 23.19  ? 4302 ARG A C     1 
ATOM   20709 O  O     . ARG A 1 4302 ? 42.755  97.865  78.765  1.00 23.28  ? 4302 ARG A O     1 
ATOM   20710 C  CB    . ARG A 1 4302 ? 42.172  95.059  80.402  1.00 20.72  ? 4302 ARG A CB    1 
ATOM   20711 C  CG    . ARG A 1 4302 ? 43.643  95.054  80.021  1.00 19.07  ? 4302 ARG A CG    1 
ATOM   20712 C  CD    . ARG A 1 4302 ? 44.250  93.669  80.162  1.00 21.75  ? 4302 ARG A CD    1 
ATOM   20713 N  NE    . ARG A 1 4302 ? 45.588  93.596  79.586  1.00 25.66  ? 4302 ARG A NE    1 
ATOM   20714 C  CZ    . ARG A 1 4302 ? 45.851  93.622  78.286  1.00 24.27  ? 4302 ARG A CZ    1 
ATOM   20715 N  NH1   . ARG A 1 4302 ? 44.885  93.700  77.386  1.00 23.22  ? 4302 ARG A NH1   1 
ATOM   20716 N  NH2   . ARG A 1 4302 ? 47.116  93.561  77.879  1.00 19.86  ? 4302 ARG A NH2   1 
ATOM   20717 N  N     . GLU A 1 4303 ? 41.264  96.518  77.746  1.00 27.39  ? 4303 GLU A N     1 
ATOM   20718 C  CA    . GLU A 1 4303 ? 41.668  96.946  76.410  1.00 25.88  ? 4303 GLU A CA    1 
ATOM   20719 C  C     . GLU A 1 4303 ? 41.476  98.446  76.207  1.00 27.91  ? 4303 GLU A C     1 
ATOM   20720 O  O     . GLU A 1 4303 ? 42.277  99.083  75.511  1.00 27.51  ? 4303 GLU A O     1 
ATOM   20721 C  CB    . GLU A 1 4303 ? 40.911  96.124  75.360  1.00 29.42  ? 4303 GLU A CB    1 
ATOM   20722 C  CG    . GLU A 1 4303 ? 39.388  96.250  75.387  1.00 39.79  ? 4303 GLU A CG    1 
ATOM   20723 C  CD    . GLU A 1 4303 ? 38.862  97.425  74.587  1.00 52.25  ? 4303 GLU A CD    1 
ATOM   20724 O  OE1   . GLU A 1 4303 ? 39.596  97.929  73.714  1.00 46.89  ? 4303 GLU A OE1   1 
ATOM   20725 O  OE2   . GLU A 1 4303 ? 37.708  97.839  74.827  1.00 54.86  ? 4303 GLU A OE2   1 
ATOM   20726 N  N     . GLU A 1 4304 ? 40.449  99.033  76.825  1.00 26.61  ? 4304 GLU A N     1 
ATOM   20727 C  CA    . GLU A 1 4304 ? 40.288  100.483 76.762  1.00 25.27  ? 4304 GLU A CA    1 
ATOM   20728 C  C     . GLU A 1 4304 ? 41.454  101.200 77.436  1.00 24.48  ? 4304 GLU A C     1 
ATOM   20729 O  O     . GLU A 1 4304 ? 41.967  102.196 76.912  1.00 26.64  ? 4304 GLU A O     1 
ATOM   20730 C  CB    . GLU A 1 4304 ? 38.961  100.892 77.399  1.00 33.22  ? 4304 GLU A CB    1 
ATOM   20731 C  CG    . GLU A 1 4304 ? 37.769  100.774 76.464  1.00 41.55  ? 4304 GLU A CG    1 
ATOM   20732 C  CD    . GLU A 1 4304 ? 36.501  100.350 77.178  1.00 50.35  ? 4304 GLU A CD    1 
ATOM   20733 O  OE1   . GLU A 1 4304 ? 36.230  100.873 78.278  1.00 45.50  ? 4304 GLU A OE1   1 
ATOM   20734 O  OE2   . GLU A 1 4304 ? 35.771  99.495  76.638  1.00 53.98  ? 4304 GLU A OE2   1 
ATOM   20735 N  N     . PHE A 1 4305 ? 41.889  100.706 78.598  1.00 23.12  ? 4305 PHE A N     1 
ATOM   20736 C  CA    . PHE A 1 4305 ? 43.029  101.315 79.277  1.00 15.92  ? 4305 PHE A CA    1 
ATOM   20737 C  C     . PHE A 1 4305 ? 44.307  101.156 78.464  1.00 18.33  ? 4305 PHE A C     1 
ATOM   20738 O  O     . PHE A 1 4305 ? 45.138  102.071 78.418  1.00 23.10  ? 4305 PHE A O     1 
ATOM   20739 C  CB    . PHE A 1 4305 ? 43.204  100.713 80.672  1.00 13.01  ? 4305 PHE A CB    1 
ATOM   20740 C  CG    . PHE A 1 4305 ? 42.073  101.016 81.612  1.00 13.78  ? 4305 PHE A CG    1 
ATOM   20741 C  CD1   . PHE A 1 4305 ? 41.877  102.301 82.089  1.00 15.62  ? 4305 PHE A CD1   1 
ATOM   20742 C  CD2   . PHE A 1 4305 ? 41.218  100.013 82.034  1.00 14.43  ? 4305 PHE A CD2   1 
ATOM   20743 C  CE1   . PHE A 1 4305 ? 40.841  102.581 82.958  1.00 14.74  ? 4305 PHE A CE1   1 
ATOM   20744 C  CE2   . PHE A 1 4305 ? 40.182  100.288 82.902  1.00 12.63  ? 4305 PHE A CE2   1 
ATOM   20745 C  CZ    . PHE A 1 4305 ? 39.994  101.573 83.365  1.00 13.32  ? 4305 PHE A CZ    1 
ATOM   20746 N  N     . VAL A 1 4306 ? 44.488  99.998  77.825  1.00 17.40  ? 4306 VAL A N     1 
ATOM   20747 C  CA    . VAL A 1 4306 ? 45.669  99.790  76.991  1.00 17.92  ? 4306 VAL A CA    1 
ATOM   20748 C  C     . VAL A 1 4306 ? 45.662  100.751 75.809  1.00 19.64  ? 4306 VAL A C     1 
ATOM   20749 O  O     . VAL A 1 4306 ? 46.703  101.306 75.437  1.00 19.31  ? 4306 VAL A O     1 
ATOM   20750 C  CB    . VAL A 1 4306 ? 45.759  98.323  76.531  1.00 22.49  ? 4306 VAL A CB    1 
ATOM   20751 C  CG1   . VAL A 1 4306 ? 47.048  98.091  75.759  1.00 19.93  ? 4306 VAL A CG1   1 
ATOM   20752 C  CG2   . VAL A 1 4306 ? 45.694  97.389  77.727  1.00 22.53  ? 4306 VAL A CG2   1 
ATOM   20753 N  N     . GLN A 1 4307 ? 44.491  100.965 75.201  1.00 22.90  ? 4307 GLN A N     1 
ATOM   20754 C  CA    . GLN A 1 4307 ? 44.399  101.947 74.124  1.00 19.48  ? 4307 GLN A CA    1 
ATOM   20755 C  C     . GLN A 1 4307 ? 44.720  103.349 74.626  1.00 17.75  ? 4307 GLN A C     1 
ATOM   20756 O  O     . GLN A 1 4307 ? 45.431  104.107 73.956  1.00 17.13  ? 4307 GLN A O     1 
ATOM   20757 C  CB    . GLN A 1 4307 ? 43.008  101.923 73.489  1.00 25.91  ? 4307 GLN A CB    1 
ATOM   20758 C  CG    . GLN A 1 4307 ? 42.844  100.911 72.371  1.00 36.66  ? 4307 GLN A CG    1 
ATOM   20759 C  CD    . GLN A 1 4307 ? 41.425  100.394 72.267  1.00 46.11  ? 4307 GLN A CD    1 
ATOM   20760 O  OE1   . GLN A 1 4307 ? 40.689  100.369 73.252  1.00 43.39  ? 4307 GLN A OE1   1 
ATOM   20761 N  NE2   . GLN A 1 4307 ? 41.033  99.976  71.069  1.00 45.23  ? 4307 GLN A NE2   1 
ATOM   20762 N  N     . TRP A 1 4308 ? 44.205  103.711 75.805  1.00 14.45  ? 4308 TRP A N     1 
ATOM   20763 C  CA    . TRP A 1 4308 ? 44.479  105.036 76.353  1.00 12.57  ? 4308 TRP A CA    1 
ATOM   20764 C  C     . TRP A 1 4308 ? 45.969  105.235 76.598  1.00 14.20  ? 4308 TRP A C     1 
ATOM   20765 O  O     . TRP A 1 4308 ? 46.519  106.301 76.297  1.00 15.36  ? 4308 TRP A O     1 
ATOM   20766 C  CB    . TRP A 1 4308 ? 43.690  105.249 77.646  1.00 12.67  ? 4308 TRP A CB    1 
ATOM   20767 C  CG    . TRP A 1 4308 ? 43.945  106.581 78.297  1.00 12.54  ? 4308 TRP A CG    1 
ATOM   20768 C  CD1   . TRP A 1 4308 ? 43.225  107.727 78.126  1.00 13.63  ? 4308 TRP A CD1   1 
ATOM   20769 C  CD2   . TRP A 1 4308 ? 44.992  106.901 79.222  1.00 12.42  ? 4308 TRP A CD2   1 
ATOM   20770 N  NE1   . TRP A 1 4308 ? 43.758  108.739 78.887  1.00 14.97  ? 4308 TRP A NE1   1 
ATOM   20771 C  CE2   . TRP A 1 4308 ? 44.844  108.257 79.569  1.00 15.31  ? 4308 TRP A CE2   1 
ATOM   20772 C  CE3   . TRP A 1 4308 ? 46.041  106.171 79.790  1.00 8.38   ? 4308 TRP A CE3   1 
ATOM   20773 C  CZ2   . TRP A 1 4308 ? 45.704  108.899 80.457  1.00 11.99  ? 4308 TRP A CZ2   1 
ATOM   20774 C  CZ3   . TRP A 1 4308 ? 46.893  106.809 80.669  1.00 7.69   ? 4308 TRP A CZ3   1 
ATOM   20775 C  CH2   . TRP A 1 4308 ? 46.720  108.159 80.996  1.00 9.27   ? 4308 TRP A CH2   1 
ATOM   20776 N  N     . VAL A 1 4309 ? 46.638  104.222 77.153  1.00 12.23  ? 4309 VAL A N     1 
ATOM   20777 C  CA    . VAL A 1 4309 ? 48.083  104.306 77.356  1.00 14.14  ? 4309 VAL A CA    1 
ATOM   20778 C  C     . VAL A 1 4309 ? 48.802  104.426 76.019  1.00 14.63  ? 4309 VAL A C     1 
ATOM   20779 O  O     . VAL A 1 4309 ? 49.740  105.218 75.869  1.00 13.67  ? 4309 VAL A O     1 
ATOM   20780 C  CB    . VAL A 1 4309 ? 48.584  103.095 78.165  1.00 12.77  ? 4309 VAL A CB    1 
ATOM   20781 C  CG1   . VAL A 1 4309 ? 50.103  103.098 78.246  1.00 7.55   ? 4309 VAL A CG1   1 
ATOM   20782 C  CG2   . VAL A 1 4309 ? 47.981  103.105 79.559  1.00 9.02   ? 4309 VAL A CG2   1 
ATOM   20783 N  N     . GLU A 1 4310 ? 48.374  103.642 75.025  1.00 19.58  ? 4310 GLU A N     1 
ATOM   20784 C  CA    . GLU A 1 4310 ? 48.985  103.695 73.702  1.00 17.38  ? 4310 GLU A CA    1 
ATOM   20785 C  C     . GLU A 1 4310 ? 48.765  105.033 73.008  1.00 16.92  ? 4310 GLU A C     1 
ATOM   20786 O  O     . GLU A 1 4310 ? 49.573  105.412 72.154  1.00 22.03  ? 4310 GLU A O     1 
ATOM   20787 C  CB    . GLU A 1 4310 ? 48.439  102.562 72.829  1.00 20.99  ? 4310 GLU A CB    1 
ATOM   20788 C  CG    . GLU A 1 4310 ? 49.249  101.267 72.862  1.00 22.26  ? 4310 GLU A CG    1 
ATOM   20789 C  CD    . GLU A 1 4310 ? 50.672  101.414 72.339  1.00 42.25  ? 4310 GLU A CD    1 
ATOM   20790 O  OE1   . GLU A 1 4310 ? 51.021  102.484 71.796  1.00 42.06  ? 4310 GLU A OE1   1 
ATOM   20791 O  OE2   . GLU A 1 4310 ? 51.447  100.444 72.470  1.00 44.32  ? 4310 GLU A OE2   1 
ATOM   20792 N  N     . LEU A 1 4311 ? 47.700  105.755 73.350  1.00 16.92  ? 4311 LEU A N     1 
ATOM   20793 C  CA    . LEU A 1 4311 ? 47.415  107.049 72.746  1.00 16.44  ? 4311 LEU A CA    1 
ATOM   20794 C  C     . LEU A 1 4311 ? 48.039  108.211 73.504  1.00 20.16  ? 4311 LEU A C     1 
ATOM   20795 O  O     . LEU A 1 4311 ? 47.825  109.366 73.122  1.00 25.14  ? 4311 LEU A O     1 
ATOM   20796 C  CB    . LEU A 1 4311 ? 45.902  107.263 72.635  1.00 18.76  ? 4311 LEU A CB    1 
ATOM   20797 C  CG    . LEU A 1 4311 ? 45.168  106.415 71.594  1.00 22.21  ? 4311 LEU A CG    1 
ATOM   20798 C  CD1   . LEU A 1 4311 ? 43.816  107.025 71.267  1.00 18.78  ? 4311 LEU A CD1   1 
ATOM   20799 C  CD2   . LEU A 1 4311 ? 46.008  106.260 70.335  1.00 16.82  ? 4311 LEU A CD2   1 
ATOM   20800 N  N     . LEU A 1 4312 ? 48.790  107.941 74.565  1.00 19.47  ? 4312 LEU A N     1 
ATOM   20801 C  CA    . LEU A 1 4312 ? 49.487  109.010 75.260  1.00 15.66  ? 4312 LEU A CA    1 
ATOM   20802 C  C     . LEU A 1 4312 ? 50.554  109.607 74.345  1.00 23.40  ? 4312 LEU A C     1 
ATOM   20803 O  O     . LEU A 1 4312 ? 51.220  108.873 73.605  1.00 22.95  ? 4312 LEU A O     1 
ATOM   20804 C  CB    . LEU A 1 4312 ? 50.122  108.489 76.550  1.00 16.45  ? 4312 LEU A CB    1 
ATOM   20805 C  CG    . LEU A 1 4312 ? 49.148  108.248 77.706  1.00 13.03  ? 4312 LEU A CG    1 
ATOM   20806 C  CD1   . LEU A 1 4312 ? 49.832  107.500 78.831  1.00 7.85   ? 4312 LEU A CD1   1 
ATOM   20807 C  CD2   . LEU A 1 4312 ? 48.572  109.563 78.207  1.00 12.80  ? 4312 LEU A CD2   1 
ATOM   20808 N  N     . PRO A 1 4313 ? 50.742  110.923 74.365  1.00 28.87  ? 4313 PRO A N     1 
ATOM   20809 C  CA    . PRO A 1 4313 ? 51.683  111.553 73.433  1.00 24.10  ? 4313 PRO A CA    1 
ATOM   20810 C  C     . PRO A 1 4313 ? 53.126  111.229 73.788  1.00 24.84  ? 4313 PRO A C     1 
ATOM   20811 O  O     . PRO A 1 4313 ? 53.430  110.585 74.794  1.00 28.78  ? 4313 PRO A O     1 
ATOM   20812 C  CB    . PRO A 1 4313 ? 51.391  113.046 73.593  1.00 21.97  ? 4313 PRO A CB    1 
ATOM   20813 C  CG    . PRO A 1 4313 ? 50.848  113.165 74.978  1.00 21.49  ? 4313 PRO A CG    1 
ATOM   20814 C  CD    . PRO A 1 4313 ? 50.051  111.914 75.207  1.00 21.62  ? 4313 PRO A CD    1 
ATOM   20815 N  N     . ASP A 1 4314 ? 54.030  111.694 72.925  1.00 24.70  ? 4314 ASP A N     1 
ATOM   20816 C  CA    . ASP A 1 4314 ? 55.465  111.561 73.139  1.00 26.21  ? 4314 ASP A CA    1 
ATOM   20817 C  C     . ASP A 1 4314 ? 56.089  112.846 73.675  1.00 27.55  ? 4314 ASP A C     1 
ATOM   20818 O  O     . ASP A 1 4314 ? 57.239  113.167 73.347  1.00 34.20  ? 4314 ASP A O     1 
ATOM   20819 C  CB    . ASP A 1 4314 ? 56.145  111.124 71.838  1.00 34.38  ? 4314 ASP A CB    1 
ATOM   20820 C  CG    . ASP A 1 4314 ? 57.562  110.625 72.054  1.00 39.09  ? 4314 ASP A CG    1 
ATOM   20821 O  OD1   . ASP A 1 4314 ? 57.885  110.222 73.191  1.00 40.97  ? 4314 ASP A OD1   1 
ATOM   20822 O  OD2   . ASP A 1 4314 ? 58.352  110.637 71.087  1.00 39.77  ? 4314 ASP A OD2   1 
ATOM   20823 N  N     . THR A 1 4315 ? 55.351  113.596 74.488  1.00 24.75  ? 4315 THR A N     1 
ATOM   20824 C  CA    . THR A 1 4315 ? 55.793  114.874 75.032  1.00 24.22  ? 4315 THR A CA    1 
ATOM   20825 C  C     . THR A 1 4315 ? 55.821  114.835 76.555  1.00 22.91  ? 4315 THR A C     1 
ATOM   20826 O  O     . THR A 1 4315 ? 55.359  115.760 77.227  1.00 30.31  ? 4315 THR A O     1 
ATOM   20827 C  CB    . THR A 1 4315 ? 54.898  116.012 74.545  1.00 33.70  ? 4315 THR A CB    1 
ATOM   20828 O  OG1   . THR A 1 4315 ? 53.617  115.917 75.180  1.00 38.05  ? 4315 THR A OG1   1 
ATOM   20829 C  CG2   . THR A 1 4315 ? 54.714  115.941 73.037  1.00 30.72  ? 4315 THR A CG2   1 
ATOM   20830 N  N     . GLN A 1 4316 ? 56.356  113.754 77.116  1.00 20.63  ? 4316 GLN A N     1 
ATOM   20831 C  CA    . GLN A 1 4316 ? 56.383  113.601 78.564  1.00 14.89  ? 4316 GLN A CA    1 
ATOM   20832 C  C     . GLN A 1 4316 ? 57.325  114.616 79.198  1.00 16.90  ? 4316 GLN A C     1 
ATOM   20833 O  O     . GLN A 1 4316 ? 58.428  114.865 78.702  1.00 18.16  ? 4316 GLN A O     1 
ATOM   20834 C  CB    . GLN A 1 4316 ? 56.809  112.185 78.948  1.00 14.62  ? 4316 GLN A CB    1 
ATOM   20835 C  CG    . GLN A 1 4316 ? 56.839  111.941 80.451  1.00 10.95  ? 4316 GLN A CG    1 
ATOM   20836 C  CD    . GLN A 1 4316 ? 57.434  110.598 80.821  1.00 14.47  ? 4316 GLN A CD    1 
ATOM   20837 O  OE1   . GLN A 1 4316 ? 57.046  109.564 80.280  1.00 17.74  ? 4316 GLN A OE1   1 
ATOM   20838 N  NE2   . GLN A 1 4316 ? 58.377  110.606 81.755  1.00 11.41  ? 4316 GLN A NE2   1 
ATOM   20839 N  N     . THR A 1 4317 ? 56.881  115.200 80.299  1.00 16.84  ? 4317 THR A N     1 
ATOM   20840 C  CA    . THR A 1 4317 ? 57.641  116.158 81.083  1.00 13.84  ? 4317 THR A CA    1 
ATOM   20841 C  C     . THR A 1 4317 ? 57.638  115.704 82.533  1.00 11.75  ? 4317 THR A C     1 
ATOM   20842 O  O     . THR A 1 4317 ? 56.764  114.935 82.947  1.00 11.51  ? 4317 THR A O     1 
ATOM   20843 C  CB    . THR A 1 4317 ? 57.043  117.569 80.973  1.00 17.86  ? 4317 THR A CB    1 
ATOM   20844 O  OG1   . THR A 1 4317 ? 55.664  117.540 81.361  1.00 16.00  ? 4317 THR A OG1   1 
ATOM   20845 C  CG2   . THR A 1 4317 ? 57.153  118.087 79.546  1.00 15.45  ? 4317 THR A CG2   1 
ATOM   20846 N  N     . PRO A 1 4318 ? 58.610  116.152 83.332  1.00 14.60  ? 4318 PRO A N     1 
ATOM   20847 C  CA    . PRO A 1 4318 ? 58.594  115.799 84.762  1.00 13.05  ? 4318 PRO A CA    1 
ATOM   20848 C  C     . PRO A 1 4318 ? 57.353  116.289 85.489  1.00 8.57   ? 4318 PRO A C     1 
ATOM   20849 O  O     . PRO A 1 4318 ? 57.048  115.776 86.573  1.00 10.35  ? 4318 PRO A O     1 
ATOM   20850 C  CB    . PRO A 1 4318 ? 59.868  116.461 85.310  1.00 13.40  ? 4318 PRO A CB    1 
ATOM   20851 C  CG    . PRO A 1 4318 ? 60.323  117.410 84.247  1.00 13.18  ? 4318 PRO A CG    1 
ATOM   20852 C  CD    . PRO A 1 4318 ? 59.846  116.852 82.951  1.00 11.57  ? 4318 PRO A CD    1 
ATOM   20853 N  N     . SER A 1 4319 ? 56.625  117.257 84.927  1.00 8.93   ? 4319 SER A N     1 
ATOM   20854 C  CA    . SER A 1 4319 ? 55.350  117.670 85.500  1.00 12.18  ? 4319 SER A CA    1 
ATOM   20855 C  C     . SER A 1 4319 ? 54.324  116.544 85.500  1.00 12.87  ? 4319 SER A C     1 
ATOM   20856 O  O     . SER A 1 4319 ? 53.354  116.608 86.262  1.00 16.22  ? 4319 SER A O     1 
ATOM   20857 C  CB    . SER A 1 4319 ? 54.797  118.874 84.740  1.00 16.82  ? 4319 SER A CB    1 
ATOM   20858 O  OG    . SER A 1 4319 ? 54.605  118.563 83.372  1.00 20.73  ? 4319 SER A OG    1 
ATOM   20859 N  N     . TRP A 1 4320 ? 54.511  115.523 84.660  1.00 10.32  ? 4320 TRP A N     1 
ATOM   20860 C  CA    . TRP A 1 4320 ? 53.662  114.340 84.734  1.00 11.59  ? 4320 TRP A CA    1 
ATOM   20861 C  C     . TRP A 1 4320 ? 53.797  113.650 86.083  1.00 11.23  ? 4320 TRP A C     1 
ATOM   20862 O  O     . TRP A 1 4320 ? 52.840  113.038 86.570  1.00 10.23  ? 4320 TRP A O     1 
ATOM   20863 C  CB    . TRP A 1 4320 ? 54.017  113.359 83.617  1.00 13.03  ? 4320 TRP A CB    1 
ATOM   20864 C  CG    . TRP A 1 4320 ? 53.611  113.798 82.246  1.00 13.14  ? 4320 TRP A CG    1 
ATOM   20865 C  CD1   . TRP A 1 4320 ? 53.540  115.076 81.776  1.00 13.54  ? 4320 TRP A CD1   1 
ATOM   20866 C  CD2   . TRP A 1 4320 ? 53.217  112.950 81.163  1.00 17.08  ? 4320 TRP A CD2   1 
ATOM   20867 N  NE1   . TRP A 1 4320 ? 53.128  115.076 80.466  1.00 16.80  ? 4320 TRP A NE1   1 
ATOM   20868 C  CE2   . TRP A 1 4320 ? 52.922  113.782 80.067  1.00 17.90  ? 4320 TRP A CE2   1 
ATOM   20869 C  CE3   . TRP A 1 4320 ? 53.084  111.567 81.016  1.00 17.37  ? 4320 TRP A CE3   1 
ATOM   20870 C  CZ2   . TRP A 1 4320 ? 52.503  113.276 78.840  1.00 18.88  ? 4320 TRP A CZ2   1 
ATOM   20871 C  CZ3   . TRP A 1 4320 ? 52.668  111.069 79.798  1.00 16.16  ? 4320 TRP A CZ3   1 
ATOM   20872 C  CH2   . TRP A 1 4320 ? 52.381  111.919 78.727  1.00 18.80  ? 4320 TRP A CH2   1 
ATOM   20873 N  N     . LEU A 1 4321 ? 54.974  113.737 86.695  1.00 10.04  ? 4321 LEU A N     1 
ATOM   20874 C  CA    . LEU A 1 4321 ? 55.269  113.074 87.955  1.00 6.42   ? 4321 LEU A CA    1 
ATOM   20875 C  C     . LEU A 1 4321 ? 55.024  113.966 89.163  1.00 8.01   ? 4321 LEU A C     1 
ATOM   20876 O  O     . LEU A 1 4321 ? 55.272  113.535 90.293  1.00 12.82  ? 4321 LEU A O     1 
ATOM   20877 C  CB    . LEU A 1 4321 ? 56.724  112.600 87.958  1.00 6.10   ? 4321 LEU A CB    1 
ATOM   20878 C  CG    . LEU A 1 4321 ? 57.192  111.985 86.639  1.00 5.77   ? 4321 LEU A CG    1 
ATOM   20879 C  CD1   . LEU A 1 4321 ? 58.675  111.669 86.689  1.00 5.11   ? 4321 LEU A CD1   1 
ATOM   20880 C  CD2   . LEU A 1 4321 ? 56.382  110.747 86.306  1.00 5.86   ? 4321 LEU A CD2   1 
ATOM   20881 N  N     . GLY A 1 4322 ? 54.548  115.190 88.954  1.00 7.41   ? 4322 GLY A N     1 
ATOM   20882 C  CA    . GLY A 1 4322 ? 54.430  116.161 90.017  1.00 10.18  ? 4322 GLY A CA    1 
ATOM   20883 C  C     . GLY A 1 4322 ? 55.664  117.007 90.236  1.00 7.38   ? 4322 GLY A C     1 
ATOM   20884 O  O     . GLY A 1 4322 ? 55.624  117.930 91.059  1.00 8.16   ? 4322 GLY A O     1 
ATOM   20885 N  N     . LEU A 1 4323 ? 56.753  116.723 89.532  1.00 7.37   ? 4323 LEU A N     1 
ATOM   20886 C  CA    . LEU A 1 4323 ? 57.982  117.488 89.636  1.00 7.53   ? 4323 LEU A CA    1 
ATOM   20887 C  C     . LEU A 1 4323 ? 57.899  118.755 88.791  1.00 7.62   ? 4323 LEU A C     1 
ATOM   20888 O  O     . LEU A 1 4323 ? 57.094  118.841 87.862  1.00 9.65   ? 4323 LEU A O     1 
ATOM   20889 C  CB    . LEU A 1 4323 ? 59.163  116.634 89.185  1.00 7.66   ? 4323 LEU A CB    1 
ATOM   20890 C  CG    . LEU A 1 4323 ? 59.630  115.543 90.150  1.00 7.34   ? 4323 LEU A CG    1 
ATOM   20891 C  CD1   . LEU A 1 4323 ? 60.573  114.579 89.450  1.00 6.83   ? 4323 LEU A CD1   1 
ATOM   20892 C  CD2   . LEU A 1 4323 ? 60.290  116.153 91.374  1.00 6.67   ? 4323 LEU A CD2   1 
ATOM   20893 N  N     . PRO A 1 4324 ? 58.711  119.764 89.100  1.00 10.72  ? 4324 PRO A N     1 
ATOM   20894 C  CA    . PRO A 1 4324 ? 58.797  120.928 88.212  1.00 10.96  ? 4324 PRO A CA    1 
ATOM   20895 C  C     . PRO A 1 4324 ? 59.392  120.549 86.865  1.00 11.74  ? 4324 PRO A C     1 
ATOM   20896 O  O     . PRO A 1 4324 ? 60.190  119.616 86.750  1.00 10.43  ? 4324 PRO A O     1 
ATOM   20897 C  CB    . PRO A 1 4324 ? 59.707  121.897 88.976  1.00 8.77   ? 4324 PRO A CB    1 
ATOM   20898 C  CG    . PRO A 1 4324 ? 60.483  121.037 89.910  1.00 8.61   ? 4324 PRO A CG    1 
ATOM   20899 C  CD    . PRO A 1 4324 ? 59.568  119.913 90.290  1.00 9.25   ? 4324 PRO A CD    1 
ATOM   20900 N  N     . ASN A 1 4325 ? 58.985  121.290 85.831  1.00 12.63  ? 4325 ASN A N     1 
ATOM   20901 C  CA    . ASN A 1 4325 ? 59.422  120.986 84.473  1.00 14.65  ? 4325 ASN A CA    1 
ATOM   20902 C  C     . ASN A 1 4325 ? 60.923  121.152 84.284  1.00 18.27  ? 4325 ASN A C     1 
ATOM   20903 O  O     . ASN A 1 4325 ? 61.498  120.499 83.406  1.00 18.60  ? 4325 ASN A O     1 
ATOM   20904 C  CB    . ASN A 1 4325 ? 58.671  121.865 83.472  1.00 16.34  ? 4325 ASN A CB    1 
ATOM   20905 C  CG    . ASN A 1 4325 ? 57.434  121.190 82.922  1.00 17.42  ? 4325 ASN A CG    1 
ATOM   20906 O  OD1   . ASN A 1 4325 ? 57.234  119.993 83.115  1.00 15.60  ? 4325 ASN A OD1   1 
ATOM   20907 N  ND2   . ASN A 1 4325 ? 56.591  121.956 82.242  1.00 23.16  ? 4325 ASN A ND2   1 
ATOM   20908 N  N     . ASN A 1 4326 ? 61.572  121.998 85.081  1.00 15.01  ? 4326 ASN A N     1 
ATOM   20909 C  CA    . ASN A 1 4326 ? 63.010  122.203 84.965  1.00 14.55  ? 4326 ASN A CA    1 
ATOM   20910 C  C     . ASN A 1 4326 ? 63.830  121.097 85.618  1.00 15.34  ? 4326 ASN A C     1 
ATOM   20911 O  O     . ASN A 1 4326 ? 65.054  121.073 85.442  1.00 20.78  ? 4326 ASN A O     1 
ATOM   20912 C  CB    . ASN A 1 4326 ? 63.394  123.568 85.554  1.00 17.22  ? 4326 ASN A CB    1 
ATOM   20913 C  CG    . ASN A 1 4326 ? 63.094  123.682 87.043  1.00 20.59  ? 4326 ASN A CG    1 
ATOM   20914 O  OD1   . ASN A 1 4326 ? 62.702  122.716 87.696  1.00 24.76  ? 4326 ASN A OD1   1 
ATOM   20915 N  ND2   . ASN A 1 4326 ? 63.281  124.879 87.585  1.00 21.47  ? 4326 ASN A ND2   1 
ATOM   20916 N  N     . ALA A 1 4327 ? 63.188  120.175 86.342  1.00 11.49  ? 4327 ALA A N     1 
ATOM   20917 C  CA    . ALA A 1 4327 ? 63.911  119.116 87.039  1.00 12.59  ? 4327 ALA A CA    1 
ATOM   20918 C  C     . ALA A 1 4327 ? 64.704  118.226 86.093  1.00 14.15  ? 4327 ALA A C     1 
ATOM   20919 O  O     . ALA A 1 4327 ? 65.657  117.573 86.530  1.00 15.67  ? 4327 ALA A O     1 
ATOM   20920 C  CB    . ALA A 1 4327 ? 62.938  118.263 87.854  1.00 12.26  ? 4327 ALA A CB    1 
ATOM   20921 N  N     . GLU A 1 4328 ? 64.334  118.182 84.815  1.00 16.38  ? 4328 GLU A N     1 
ATOM   20922 C  CA    . GLU A 1 4328 ? 65.071  117.421 83.818  1.00 16.10  ? 4328 GLU A CA    1 
ATOM   20923 C  C     . GLU A 1 4328 ? 66.136  118.242 83.105  1.00 16.17  ? 4328 GLU A C     1 
ATOM   20924 O  O     . GLU A 1 4328 ? 67.091  117.654 82.580  1.00 17.50  ? 4328 GLU A O     1 
ATOM   20925 C  CB    . GLU A 1 4328 ? 64.105  116.836 82.779  1.00 15.93  ? 4328 GLU A CB    1 
ATOM   20926 C  CG    . GLU A 1 4328 ? 63.686  117.818 81.697  1.00 16.72  ? 4328 GLU A CG    1 
ATOM   20927 C  CD    . GLU A 1 4328 ? 62.551  117.298 80.837  1.00 24.55  ? 4328 GLU A CD    1 
ATOM   20928 O  OE1   . GLU A 1 4328 ? 62.501  116.075 80.589  1.00 25.48  ? 4328 GLU A OE1   1 
ATOM   20929 O  OE2   . GLU A 1 4328 ? 61.708  118.114 80.409  1.00 25.12  ? 4328 GLU A OE2   1 
ATOM   20930 N  N     . ARG A 1 4329 ? 66.011  119.577 83.116  1.00 15.66  ? 4329 ARG A N     1 
ATOM   20931 C  CA    . ARG A 1 4329 ? 66.828  120.434 82.258  1.00 18.43  ? 4329 ARG A CA    1 
ATOM   20932 C  C     . ARG A 1 4329 ? 68.298  120.042 82.306  1.00 17.91  ? 4329 ARG A C     1 
ATOM   20933 O  O     . ARG A 1 4329 ? 68.853  119.551 81.312  1.00 20.52  ? 4329 ARG A O     1 
ATOM   20934 C  CB    . ARG A 1 4329 ? 66.660  121.896 82.673  1.00 15.76  ? 4329 ARG A CB    1 
ATOM   20935 C  CG    . ARG A 1 4329 ? 66.761  122.892 81.531  1.00 20.10  ? 4329 ARG A CG    1 
ATOM   20936 C  CD    . ARG A 1 4329 ? 66.922  124.309 82.065  1.00 24.98  ? 4329 ARG A CD    1 
ATOM   20937 N  NE    . ARG A 1 4329 ? 66.988  125.307 81.003  1.00 28.66  ? 4329 ARG A NE    1 
ATOM   20938 C  CZ    . ARG A 1 4329 ? 65.959  125.682 80.256  1.00 30.70  ? 4329 ARG A CZ    1 
ATOM   20939 N  NH1   . ARG A 1 4329 ? 64.751  125.172 80.433  1.00 28.44  ? 4329 ARG A NH1   1 
ATOM   20940 N  NH2   . ARG A 1 4329 ? 66.145  126.598 79.310  1.00 29.44  ? 4329 ARG A NH2   1 
ATOM   20941 N  N     . VAL A 1 4330 ? 68.923  120.185 83.477  1.00 14.72  ? 4330 VAL A N     1 
ATOM   20942 C  CA    . VAL A 1 4330 ? 70.350  119.908 83.599  1.00 15.77  ? 4330 VAL A CA    1 
ATOM   20943 C  C     . VAL A 1 4330 ? 70.655  118.502 83.109  1.00 16.45  ? 4330 VAL A C     1 
ATOM   20944 O  O     . VAL A 1 4330 ? 71.540  118.304 82.264  1.00 18.94  ? 4330 VAL A O     1 
ATOM   20945 C  CB    . VAL A 1 4330 ? 70.812  120.115 85.054  1.00 14.22  ? 4330 VAL A CB    1 
ATOM   20946 C  CG1   . VAL A 1 4330 ? 72.205  119.542 85.258  1.00 10.26  ? 4330 VAL A CG1   1 
ATOM   20947 C  CG2   . VAL A 1 4330 ? 70.774  121.590 85.419  1.00 13.26  ? 4330 VAL A CG2   1 
ATOM   20948 N  N     . LEU A 1 4331 ? 69.877  117.517 83.572  1.00 16.59  ? 4331 LEU A N     1 
ATOM   20949 C  CA    . LEU A 1 4331 ? 70.095  116.143 83.134  1.00 17.60  ? 4331 LEU A CA    1 
ATOM   20950 C  C     . LEU A 1 4331 ? 70.101  116.060 81.618  1.00 16.91  ? 4331 LEU A C     1 
ATOM   20951 O  O     . LEU A 1 4331 ? 71.082  115.594 81.020  1.00 16.26  ? 4331 LEU A O     1 
ATOM   20952 C  CB    . LEU A 1 4331 ? 69.020  115.226 83.718  1.00 20.90  ? 4331 LEU A CB    1 
ATOM   20953 C  CG    . LEU A 1 4331 ? 69.145  113.734 83.401  1.00 29.81  ? 4331 LEU A CG    1 
ATOM   20954 C  CD1   . LEU A 1 4331 ? 70.429  113.159 83.977  1.00 29.06  ? 4331 LEU A CD1   1 
ATOM   20955 C  CD2   . LEU A 1 4331 ? 67.933  112.968 83.912  1.00 30.81  ? 4331 LEU A CD2   1 
ATOM   20956 N  N     . LEU A 1 4332 ? 69.055  116.593 80.977  1.00 15.61  ? 4332 LEU A N     1 
ATOM   20957 C  CA    . LEU A 1 4332 ? 69.003  116.568 79.522  1.00 14.50  ? 4332 LEU A CA    1 
ATOM   20958 C  C     . LEU A 1 4332 ? 70.261  117.182 78.933  1.00 14.44  ? 4332 LEU A C     1 
ATOM   20959 O  O     . LEU A 1 4332 ? 70.931  116.556 78.100  1.00 15.41  ? 4332 LEU A O     1 
ATOM   20960 C  CB    . LEU A 1 4332 ? 67.761  117.304 79.023  1.00 12.59  ? 4332 LEU A CB    1 
ATOM   20961 C  CG    . LEU A 1 4332 ? 66.406  116.612 79.174  1.00 14.09  ? 4332 LEU A CG    1 
ATOM   20962 C  CD1   . LEU A 1 4332 ? 65.319  117.431 78.497  1.00 14.54  ? 4332 LEU A CD1   1 
ATOM   20963 C  CD2   . LEU A 1 4332 ? 66.454  115.208 78.599  1.00 10.99  ? 4332 LEU A CD2   1 
ATOM   20964 N  N     . THR A 1 4333 ? 70.639  118.370 79.421  1.00 15.33  ? 4333 THR A N     1 
ATOM   20965 C  CA    . THR A 1 4333 ? 71.840  119.022 78.915  1.00 15.79  ? 4333 THR A CA    1 
ATOM   20966 C  C     . THR A 1 4333 ? 73.026  118.076 78.984  1.00 15.66  ? 4333 THR A C     1 
ATOM   20967 O  O     . THR A 1 4333 ? 73.683  117.819 77.965  1.00 15.28  ? 4333 THR A O     1 
ATOM   20968 C  CB    . THR A 1 4333 ? 72.124  120.298 79.708  1.00 16.38  ? 4333 THR A CB    1 
ATOM   20969 O  OG1   . THR A 1 4333 ? 70.974  121.153 79.671  1.00 20.19  ? 4333 THR A OG1   1 
ATOM   20970 C  CG2   . THR A 1 4333 ? 73.314  121.037 79.120  1.00 14.82  ? 4333 THR A CG2   1 
ATOM   20971 N  N     . THR A 1 4334 ? 73.254  117.474 80.156  1.00 14.00  ? 4334 THR A N     1 
ATOM   20972 C  CA    . THR A 1 4334 ? 74.383  116.566 80.298  1.00 13.84  ? 4334 THR A CA    1 
ATOM   20973 C  C     . THR A 1 4334 ? 74.312  115.465 79.255  1.00 13.22  ? 4334 THR A C     1 
ATOM   20974 O  O     . THR A 1 4334 ? 75.271  115.250 78.501  1.00 14.70  ? 4334 THR A O     1 
ATOM   20975 C  CB    . THR A 1 4334 ? 74.415  115.973 81.707  1.00 14.06  ? 4334 THR A CB    1 
ATOM   20976 O  OG1   . THR A 1 4334 ? 74.352  117.029 82.673  1.00 18.97  ? 4334 THR A OG1   1 
ATOM   20977 C  CG2   . THR A 1 4334 ? 75.692  115.175 81.919  1.00 11.11  ? 4334 THR A CG2   1 
ATOM   20978 N  N     . GLN A 1 4335 ? 73.146  114.824 79.132  1.00 13.87  ? 4335 GLN A N     1 
ATOM   20979 C  CA    . GLN A 1 4335 ? 73.019  113.736 78.173  1.00 14.13  ? 4335 GLN A CA    1 
ATOM   20980 C  C     . GLN A 1 4335 ? 73.332  114.225 76.770  1.00 11.93  ? 4335 GLN A C     1 
ATOM   20981 O  O     . GLN A 1 4335 ? 74.087  113.573 76.037  1.00 13.98  ? 4335 GLN A O     1 
ATOM   20982 C  CB    . GLN A 1 4335 ? 71.620  113.127 78.244  1.00 17.30  ? 4335 GLN A CB    1 
ATOM   20983 C  CG    . GLN A 1 4335 ? 71.349  112.358 79.525  1.00 18.64  ? 4335 GLN A CG    1 
ATOM   20984 C  CD    . GLN A 1 4335 ? 70.669  111.025 79.276  1.00 37.49  ? 4335 GLN A CD    1 
ATOM   20985 O  OE1   . GLN A 1 4335 ? 70.190  110.755 78.174  1.00 40.46  ? 4335 GLN A OE1   1 
ATOM   20986 N  NE2   . GLN A 1 4335 ? 70.624  110.184 80.302  1.00 38.22  ? 4335 GLN A NE2   1 
ATOM   20987 N  N     . GLY A 1 4336 ? 72.823  115.407 76.407  1.00 12.14  ? 4336 GLY A N     1 
ATOM   20988 C  CA    . GLY A 1 4336 ? 73.155  115.959 75.108  1.00 10.99  ? 4336 GLY A CA    1 
ATOM   20989 C  C     . GLY A 1 4336 ? 74.652  116.065 74.917  1.00 15.04  ? 4336 GLY A C     1 
ATOM   20990 O  O     . GLY A 1 4336 ? 75.206  115.513 73.960  1.00 16.38  ? 4336 GLY A O     1 
ATOM   20991 N  N     . VAL A 1 4337 ? 75.338  116.688 75.879  1.00 14.46  ? 4337 VAL A N     1 
ATOM   20992 C  CA    . VAL A 1 4337 ? 76.790  116.781 75.798  1.00 13.28  ? 4337 VAL A CA    1 
ATOM   20993 C  C     . VAL A 1 4337 ? 77.387  115.385 75.738  1.00 15.18  ? 4337 VAL A C     1 
ATOM   20994 O  O     . VAL A 1 4337 ? 78.262  115.101 74.908  1.00 14.94  ? 4337 VAL A O     1 
ATOM   20995 C  CB    . VAL A 1 4337 ? 77.345  117.590 76.985  1.00 14.48  ? 4337 VAL A CB    1 
ATOM   20996 C  CG1   . VAL A 1 4337 ? 78.864  117.541 76.999  1.00 13.96  ? 4337 VAL A CG1   1 
ATOM   20997 C  CG2   . VAL A 1 4337 ? 76.852  119.027 76.923  1.00 14.09  ? 4337 VAL A CG2   1 
ATOM   20998 N  N     . ASP A 1 4338 ? 76.869  114.477 76.571  1.00 15.94  ? 4338 ASP A N     1 
ATOM   20999 C  CA    . ASP A 1 4338 ? 77.337  113.099 76.548  1.00 16.27  ? 4338 ASP A CA    1 
ATOM   21000 C  C     . ASP A 1 4338 ? 77.255  112.528 75.142  1.00 16.50  ? 4338 ASP A C     1 
ATOM   21001 O  O     . ASP A 1 4338 ? 78.247  111.996 74.623  1.00 16.24  ? 4338 ASP A O     1 
ATOM   21002 C  CB    . ASP A 1 4338 ? 76.521  112.257 77.529  1.00 19.82  ? 4338 ASP A CB    1 
ATOM   21003 C  CG    . ASP A 1 4338 ? 76.983  110.817 77.591  1.00 32.02  ? 4338 ASP A CG    1 
ATOM   21004 O  OD1   . ASP A 1 4338 ? 76.145  109.919 77.366  1.00 36.92  ? 4338 ASP A OD1   1 
ATOM   21005 O  OD2   . ASP A 1 4338 ? 78.179  110.583 77.862  1.00 29.47  ? 4338 ASP A OD2   1 
ATOM   21006 N  N     . MET A 1 4339 ? 76.105  112.705 74.481  1.00 16.17  ? 4339 MET A N     1 
ATOM   21007 C  CA    . MET A 1 4339 ? 75.965  112.196 73.123  1.00 17.51  ? 4339 MET A CA    1 
ATOM   21008 C  C     . MET A 1 4339 ? 77.084  112.721 72.242  1.00 21.04  ? 4339 MET A C     1 
ATOM   21009 O  O     . MET A 1 4339 ? 77.787  111.938 71.587  1.00 24.07  ? 4339 MET A O     1 
ATOM   21010 C  CB    . MET A 1 4339 ? 74.599  112.577 72.551  1.00 16.91  ? 4339 MET A CB    1 
ATOM   21011 C  CG    . MET A 1 4339 ? 74.477  112.358 71.051  1.00 17.85  ? 4339 MET A CG    1 
ATOM   21012 S  SD    . MET A 1 4339 ? 72.861  112.823 70.401  1.00 40.30  ? 4339 MET A SD    1 
ATOM   21013 C  CE    . MET A 1 4339 ? 72.987  114.609 70.426  1.00 15.67  ? 4339 MET A CE    1 
ATOM   21014 N  N     . ILE A 1 4340 ? 77.329  114.034 72.296  1.00 20.78  ? 4340 ILE A N     1 
ATOM   21015 C  CA    . ILE A 1 4340 ? 78.383  114.626 71.480  1.00 19.96  ? 4340 ILE A CA    1 
ATOM   21016 C  C     . ILE A 1 4340 ? 79.694  113.902 71.733  1.00 18.96  ? 4340 ILE A C     1 
ATOM   21017 O  O     . ILE A 1 4340 ? 80.336  113.397 70.802  1.00 22.00  ? 4340 ILE A O     1 
ATOM   21018 C  CB    . ILE A 1 4340 ? 78.511  116.131 71.774  1.00 24.26  ? 4340 ILE A CB    1 
ATOM   21019 C  CG1   . ILE A 1 4340 ? 77.191  116.849 71.494  1.00 20.25  ? 4340 ILE A CG1   1 
ATOM   21020 C  CG2   . ILE A 1 4340 ? 79.633  116.740 70.947  1.00 23.99  ? 4340 ILE A CG2   1 
ATOM   21021 C  CD1   . ILE A 1 4340 ? 76.755  116.765 70.063  1.00 17.79  ? 4340 ILE A CD1   1 
ATOM   21022 N  N     . SER A 1 4341 ? 80.056  113.753 73.012  1.00 17.57  ? 4341 SER A N     1 
ATOM   21023 C  CA    . SER A 1 4341 ? 81.317  113.103 73.340  1.00 18.99  ? 4341 SER A CA    1 
ATOM   21024 C  C     . SER A 1 4341 ? 81.370  111.712 72.737  1.00 20.77  ? 4341 SER A C     1 
ATOM   21025 O  O     . SER A 1 4341 ? 82.344  111.358 72.059  1.00 24.85  ? 4341 SER A O     1 
ATOM   21026 C  CB    . SER A 1 4341 ? 81.503  113.043 74.856  1.00 20.51  ? 4341 SER A CB    1 
ATOM   21027 O  OG    . SER A 1 4341 ? 81.608  114.343 75.408  1.00 31.40  ? 4341 SER A OG    1 
ATOM   21028 N  N     . LYS A 1 4342 ? 80.295  110.938 72.903  1.00 19.53  ? 4342 LYS A N     1 
ATOM   21029 C  CA    . LYS A 1 4342 ? 80.292  109.587 72.363  1.00 18.39  ? 4342 LYS A CA    1 
ATOM   21030 C  C     . LYS A 1 4342 ? 80.458  109.620 70.853  1.00 19.20  ? 4342 LYS A C     1 
ATOM   21031 O  O     . LYS A 1 4342 ? 81.279  108.880 70.296  1.00 20.00  ? 4342 LYS A O     1 
ATOM   21032 C  CB    . LYS A 1 4342 ? 79.012  108.863 72.774  1.00 16.74  ? 4342 LYS A CB    1 
ATOM   21033 C  CG    . LYS A 1 4342 ? 79.120  108.218 74.146  1.00 17.57  ? 4342 LYS A CG    1 
ATOM   21034 C  CD    . LYS A 1 4342 ? 77.804  108.221 74.894  1.00 20.22  ? 4342 LYS A CD    1 
ATOM   21035 C  CE    . LYS A 1 4342 ? 77.965  107.575 76.260  1.00 21.80  ? 4342 LYS A CE    1 
ATOM   21036 N  NZ    . LYS A 1 4342 ? 76.652  107.325 76.916  1.00 21.48  ? 4342 LYS A NZ    1 
ATOM   21037 N  N     . MET A 1 4343 ? 79.739  110.527 70.184  1.00 19.24  ? 4343 MET A N     1 
ATOM   21038 C  CA    . MET A 1 4343 ? 79.937  110.700 68.751  1.00 18.00  ? 4343 MET A CA    1 
ATOM   21039 C  C     . MET A 1 4343 ? 81.395  111.004 68.449  1.00 24.80  ? 4343 MET A C     1 
ATOM   21040 O  O     . MET A 1 4343 ? 82.022  110.333 67.619  1.00 34.99  ? 4343 MET A O     1 
ATOM   21041 C  CB    . MET A 1 4343 ? 79.031  111.818 68.237  1.00 20.10  ? 4343 MET A CB    1 
ATOM   21042 C  CG    . MET A 1 4343 ? 77.650  111.362 67.802  1.00 18.25  ? 4343 MET A CG    1 
ATOM   21043 S  SD    . MET A 1 4343 ? 76.590  112.759 67.383  1.00 38.76  ? 4343 MET A SD    1 
ATOM   21044 C  CE    . MET A 1 4343 ? 77.044  113.033 65.675  1.00 30.13  ? 4343 MET A CE    1 
ATOM   21045 N  N     . LEU A 1 4344 ? 81.973  111.964 69.176  1.00 25.36  ? 4344 LEU A N     1 
ATOM   21046 C  CA    . LEU A 1 4344 ? 83.353  112.350 68.919  1.00 26.50  ? 4344 LEU A CA    1 
ATOM   21047 C  C     . LEU A 1 4344 ? 84.305  111.201 69.216  1.00 27.08  ? 4344 LEU A C     1 
ATOM   21048 O  O     . LEU A 1 4344 ? 85.405  111.136 68.657  1.00 35.99  ? 4344 LEU A O     1 
ATOM   21049 C  CB    . LEU A 1 4344 ? 83.714  113.580 69.750  1.00 29.53  ? 4344 LEU A CB    1 
ATOM   21050 C  CG    . LEU A 1 4344 ? 84.912  114.404 69.276  1.00 29.87  ? 4344 LEU A CG    1 
ATOM   21051 C  CD1   . LEU A 1 4344 ? 84.879  114.585 67.765  1.00 32.75  ? 4344 LEU A CD1   1 
ATOM   21052 C  CD2   . LEU A 1 4344 ? 84.933  115.747 69.981  1.00 41.82  ? 4344 LEU A CD2   1 
ATOM   21053 N  N     . LYS A 1 4345 ? 83.896  110.279 70.091  1.00 26.39  ? 4345 LYS A N     1 
ATOM   21054 C  CA    . LYS A 1 4345 ? 84.791  109.186 70.448  1.00 26.52  ? 4345 LYS A CA    1 
ATOM   21055 C  C     . LYS A 1 4345 ? 84.729  108.069 69.412  1.00 31.30  ? 4345 LYS A C     1 
ATOM   21056 O  O     . LYS A 1 4345 ? 85.619  107.212 69.358  1.00 34.48  ? 4345 LYS A O     1 
ATOM   21057 C  CB    . LYS A 1 4345 ? 84.451  108.677 71.850  1.00 25.91  ? 4345 LYS A CB    1 
ATOM   21058 C  CG    . LYS A 1 4345 ? 85.334  107.547 72.357  1.00 29.36  ? 4345 LYS A CG    1 
ATOM   21059 C  CD    . LYS A 1 4345 ? 84.882  107.058 73.720  1.00 35.21  ? 4345 LYS A CD    1 
ATOM   21060 C  CE    . LYS A 1 4345 ? 84.719  108.214 74.693  1.00 42.63  ? 4345 LYS A CE    1 
ATOM   21061 N  NZ    . LYS A 1 4345 ? 84.163  107.768 76.000  1.00 41.67  ? 4345 LYS A NZ    1 
ATOM   21062 N  N     . MET A 1 4346 ? 83.702  108.077 68.557  1.00 28.88  ? 4346 MET A N     1 
ATOM   21063 C  CA    . MET A 1 4346 ? 83.581  107.006 67.575  1.00 27.88  ? 4346 MET A CA    1 
ATOM   21064 C  C     . MET A 1 4346 ? 84.068  107.405 66.187  1.00 37.23  ? 4346 MET A C     1 
ATOM   21065 O  O     . MET A 1 4346 ? 83.845  106.650 65.234  1.00 43.83  ? 4346 MET A O     1 
ATOM   21066 C  CB    . MET A 1 4346 ? 82.136  106.511 67.519  1.00 22.83  ? 4346 MET A CB    1 
ATOM   21067 C  CG    . MET A 1 4346 ? 81.762  105.670 68.731  1.00 21.76  ? 4346 MET A CG    1 
ATOM   21068 S  SD    . MET A 1 4346 ? 80.251  104.713 68.535  1.00 27.82  ? 4346 MET A SD    1 
ATOM   21069 C  CE    . MET A 1 4346 ? 79.047  105.865 69.180  1.00 14.52  ? 4346 MET A CE    1 
ATOM   21070 N  N     . GLN A 1 4347 ? 84.720  108.554 66.048  1.00 40.58  ? 4347 GLN A N     1 
ATOM   21071 C  CA    . GLN A 1 4347 ? 85.359  108.918 64.788  1.00 47.44  ? 4347 GLN A CA    1 
ATOM   21072 C  C     . GLN A 1 4347 ? 86.870  108.739 64.878  1.00 51.74  ? 4347 GLN A C     1 
ATOM   21073 O  O     . GLN A 1 4347 ? 87.538  109.406 65.668  1.00 60.75  ? 4347 GLN A O     1 
ATOM   21074 C  CB    . GLN A 1 4347 ? 85.025  110.359 64.399  1.00 45.83  ? 4347 GLN A CB    1 
ATOM   21075 C  CG    . GLN A 1 4347 ? 83.569  110.588 64.040  1.00 51.62  ? 4347 GLN A CG    1 
ATOM   21076 C  CD    . GLN A 1 4347 ? 83.285  112.028 63.669  1.00 56.75  ? 4347 GLN A CD    1 
ATOM   21077 O  OE1   . GLN A 1 4347 ? 84.163  112.887 63.749  1.00 56.86  ? 4347 GLN A OE1   1 
ATOM   21078 N  NE2   . GLN A 1 4347 ? 82.055  112.298 63.249  1.00 57.98  ? 4347 GLN A NE2   1 
ATOM   21079 N  N     . PRO A 1 4374 ? 110.666 118.348 86.990  1.00 73.70  ? 4374 PRO A N     1 
ATOM   21080 C  CA    . PRO A 1 4374 ? 109.361 117.930 86.467  1.00 80.32  ? 4374 PRO A CA    1 
ATOM   21081 C  C     . PRO A 1 4374 ? 108.319 119.043 86.535  1.00 82.28  ? 4374 PRO A C     1 
ATOM   21082 O  O     . PRO A 1 4374 ? 108.326 119.834 87.477  1.00 83.69  ? 4374 PRO A O     1 
ATOM   21083 C  CB    . PRO A 1 4374 ? 108.971 116.763 87.382  1.00 82.04  ? 4374 PRO A CB    1 
ATOM   21084 C  CG    . PRO A 1 4374 ? 110.256 116.290 87.978  1.00 82.09  ? 4374 PRO A CG    1 
ATOM   21085 C  CD    . PRO A 1 4374 ? 111.102 117.514 88.121  1.00 79.86  ? 4374 PRO A CD    1 
ATOM   21086 N  N     . ALA A 1 4375 ? 107.435 119.099 85.536  1.00 80.43  ? 4375 ALA A N     1 
ATOM   21087 C  CA    . ALA A 1 4375 ? 106.395 120.123 85.525  1.00 85.02  ? 4375 ALA A CA    1 
ATOM   21088 C  C     . ALA A 1 4375 ? 105.375 119.902 86.633  1.00 84.87  ? 4375 ALA A C     1 
ATOM   21089 O  O     . ALA A 1 4375 ? 104.885 120.873 87.226  1.00 78.46  ? 4375 ALA A O     1 
ATOM   21090 C  CB    . ALA A 1 4375 ? 105.702 120.154 84.163  1.00 79.10  ? 4375 ALA A CB    1 
ATOM   21091 N  N     . TRP A 1 4376 ? 105.039 118.641 86.922  1.00 85.52  ? 4376 TRP A N     1 
ATOM   21092 C  CA    . TRP A 1 4376 ? 104.092 118.356 87.995  1.00 83.01  ? 4376 TRP A CA    1 
ATOM   21093 C  C     . TRP A 1 4376 ? 104.620 118.850 89.334  1.00 79.30  ? 4376 TRP A C     1 
ATOM   21094 O  O     . TRP A 1 4376 ? 103.859 119.369 90.157  1.00 77.98  ? 4376 TRP A O     1 
ATOM   21095 C  CB    . TRP A 1 4376 ? 103.782 116.857 88.046  1.00 75.71  ? 4376 TRP A CB    1 
ATOM   21096 C  CG    . TRP A 1 4376 ? 104.893 116.003 88.598  1.00 83.75  ? 4376 TRP A CG    1 
ATOM   21097 C  CD1   . TRP A 1 4376 ? 105.823 115.308 87.881  1.00 84.23  ? 4376 TRP A CD1   1 
ATOM   21098 C  CD2   . TRP A 1 4376 ? 105.174 115.737 89.980  1.00 86.80  ? 4376 TRP A CD2   1 
ATOM   21099 N  NE1   . TRP A 1 4376 ? 106.672 114.638 88.728  1.00 84.40  ? 4376 TRP A NE1   1 
ATOM   21100 C  CE2   . TRP A 1 4376 ? 106.295 114.885 90.022  1.00 86.68  ? 4376 TRP A CE2   1 
ATOM   21101 C  CE3   . TRP A 1 4376 ? 104.591 116.145 91.184  1.00 84.11  ? 4376 TRP A CE3   1 
ATOM   21102 C  CZ2   . TRP A 1 4376 ? 106.843 114.432 91.220  1.00 86.29  ? 4376 TRP A CZ2   1 
ATOM   21103 C  CZ3   . TRP A 1 4376 ? 105.139 115.696 92.371  1.00 79.76  ? 4376 TRP A CZ3   1 
ATOM   21104 C  CH2   . TRP A 1 4376 ? 106.252 114.847 92.380  1.00 81.78  ? 4376 TRP A CH2   1 
ATOM   21105 N  N     . MET A 1 4377 ? 105.927 118.710 89.562  1.00 77.33  ? 4377 MET A N     1 
ATOM   21106 C  CA    . MET A 1 4377 ? 106.517 119.155 90.820  1.00 80.57  ? 4377 MET A CA    1 
ATOM   21107 C  C     . MET A 1 4377 ? 106.359 120.661 90.997  1.00 78.15  ? 4377 MET A C     1 
ATOM   21108 O  O     . MET A 1 4377 ? 105.927 121.128 92.058  1.00 75.58  ? 4377 MET A O     1 
ATOM   21109 C  CB    . MET A 1 4377 ? 107.989 118.740 90.856  1.00 79.78  ? 4377 MET A CB    1 
ATOM   21110 C  CG    . MET A 1 4377 ? 108.745 119.051 92.135  1.00 79.88  ? 4377 MET A CG    1 
ATOM   21111 S  SD    . MET A 1 4377 ? 110.425 118.398 92.009  1.00 88.66  ? 4377 MET A SD    1 
ATOM   21112 C  CE    . MET A 1 4377 ? 111.155 118.954 93.544  1.00 71.29  ? 4377 MET A CE    1 
ATOM   21113 N  N     . ARG A 1 4378 ? 106.665 121.433 89.951  1.00 77.77  ? 4378 ARG A N     1 
ATOM   21114 C  CA    . ARG A 1 4378 ? 106.550 122.886 90.038  1.00 75.23  ? 4378 ARG A CA    1 
ATOM   21115 C  C     . ARG A 1 4378 ? 105.097 123.328 90.171  1.00 73.33  ? 4378 ARG A C     1 
ATOM   21116 O  O     . ARG A 1 4378 ? 104.786 124.230 90.962  1.00 68.01  ? 4378 ARG A O     1 
ATOM   21117 C  CB    . ARG A 1 4378 ? 107.200 123.543 88.818  1.00 73.65  ? 4378 ARG A CB    1 
ATOM   21118 C  CG    . ARG A 1 4378 ? 108.698 123.816 88.954  1.00 76.11  ? 4378 ARG A CG    1 
ATOM   21119 C  CD    . ARG A 1 4378 ? 109.502 122.546 89.191  1.00 80.67  ? 4378 ARG A CD    1 
ATOM   21120 N  NE    . ARG A 1 4378 ? 110.908 122.828 89.456  1.00 87.40  ? 4378 ARG A NE    1 
ATOM   21121 C  CZ    . ARG A 1 4378 ? 111.821 121.903 89.719  1.00 84.29  ? 4378 ARG A CZ    1 
ATOM   21122 N  NH1   . ARG A 1 4378 ? 111.511 120.618 89.760  1.00 79.95  ? 4378 ARG A NH1   1 
ATOM   21123 N  NH2   . ARG A 1 4378 ? 113.077 122.277 89.946  1.00 76.99  ? 4378 ARG A NH2   1 
ATOM   21124 N  N     . THR A 1 4379 ? 104.190 122.718 89.401  1.00 75.04  ? 4379 THR A N     1 
ATOM   21125 C  CA    . THR A 1 4379 ? 102.793 123.132 89.480  1.00 73.52  ? 4379 THR A CA    1 
ATOM   21126 C  C     . THR A 1 4379 ? 102.186 122.767 90.832  1.00 71.50  ? 4379 THR A C     1 
ATOM   21127 O  O     . THR A 1 4379 ? 101.369 123.521 91.372  1.00 72.72  ? 4379 THR A O     1 
ATOM   21128 C  CB    . THR A 1 4379 ? 101.981 122.540 88.322  1.00 75.20  ? 4379 THR A CB    1 
ATOM   21129 O  OG1   . THR A 1 4379 ? 100.702 123.185 88.257  1.00 87.54  ? 4379 THR A OG1   1 
ATOM   21130 C  CG2   . THR A 1 4379 ? 101.771 121.045 88.483  1.00 70.28  ? 4379 THR A CG2   1 
ATOM   21131 N  N     . LEU A 1 4380 ? 102.601 121.639 91.417  1.00 66.79  ? 4380 LEU A N     1 
ATOM   21132 C  CA    . LEU A 1 4380 ? 102.125 121.290 92.750  1.00 62.38  ? 4380 LEU A CA    1 
ATOM   21133 C  C     . LEU A 1 4380 ? 102.715 122.220 93.800  1.00 62.32  ? 4380 LEU A C     1 
ATOM   21134 O  O     . LEU A 1 4380 ? 102.040 122.567 94.774  1.00 65.30  ? 4380 LEU A O     1 
ATOM   21135 C  CB    . LEU A 1 4380 ? 102.460 119.833 93.066  1.00 66.72  ? 4380 LEU A CB    1 
ATOM   21136 C  CG    . LEU A 1 4380 ? 101.931 119.291 94.396  1.00 62.97  ? 4380 LEU A CG    1 
ATOM   21137 C  CD1   . LEU A 1 4380 ? 100.469 119.666 94.591  1.00 62.67  ? 4380 LEU A CD1   1 
ATOM   21138 C  CD2   . LEU A 1 4380 ? 102.111 117.786 94.467  1.00 61.22  ? 4380 LEU A CD2   1 
ATOM   21139 N  N     . HIS A 1 4381 ? 103.970 122.640 93.618  1.00 64.57  ? 4381 HIS A N     1 
ATOM   21140 C  CA    . HIS A 1 4381 ? 104.551 123.636 94.512  1.00 68.61  ? 4381 HIS A CA    1 
ATOM   21141 C  C     . HIS A 1 4381 ? 103.735 124.922 94.488  1.00 65.03  ? 4381 HIS A C     1 
ATOM   21142 O  O     . HIS A 1 4381 ? 103.388 125.474 95.540  1.00 65.18  ? 4381 HIS A O     1 
ATOM   21143 C  CB    . HIS A 1 4381 ? 106.002 123.911 94.110  1.00 67.92  ? 4381 HIS A CB    1 
ATOM   21144 C  CG    . HIS A 1 4381 ? 106.676 124.961 94.939  1.00 69.44  ? 4381 HIS A CG    1 
ATOM   21145 N  ND1   . HIS A 1 4381 ? 107.801 125.634 94.514  1.00 71.53  ? 4381 HIS A ND1   1 
ATOM   21146 C  CD2   . HIS A 1 4381 ? 106.394 125.444 96.173  1.00 69.62  ? 4381 HIS A CD2   1 
ATOM   21147 C  CE1   . HIS A 1 4381 ? 108.178 126.492 95.445  1.00 70.45  ? 4381 HIS A CE1   1 
ATOM   21148 N  NE2   . HIS A 1 4381 ? 107.341 126.396 96.462  1.00 68.14  ? 4381 HIS A NE2   1 
ATOM   21149 N  N     . THR A 1 4382 ? 103.408 125.403 93.287  1.00 65.44  ? 4382 THR A N     1 
ATOM   21150 C  CA    . THR A 1 4382 ? 102.621 126.628 93.171  1.00 65.31  ? 4382 THR A CA    1 
ATOM   21151 C  C     . THR A 1 4382 ? 101.235 126.457 93.784  1.00 66.73  ? 4382 THR A C     1 
ATOM   21152 O  O     . THR A 1 4382 ? 100.756 127.338 94.510  1.00 66.41  ? 4382 THR A O     1 
ATOM   21153 C  CB    . THR A 1 4382 ? 102.506 127.046 91.705  1.00 67.10  ? 4382 THR A CB    1 
ATOM   21154 O  OG1   . THR A 1 4382 ? 101.937 125.974 90.943  1.00 66.68  ? 4382 THR A OG1   1 
ATOM   21155 C  CG2   . THR A 1 4382 ? 103.876 127.393 91.141  1.00 64.60  ? 4382 THR A CG2   1 
ATOM   21156 N  N     . THR A 1 4383 ? 100.579 125.326 93.507  1.00 63.19  ? 4383 THR A N     1 
ATOM   21157 C  CA    . THR A 1 4383 ? 99.240  125.093 94.039  1.00 61.58  ? 4383 THR A CA    1 
ATOM   21158 C  C     . THR A 1 4383 ? 99.251  125.029 95.561  1.00 59.19  ? 4383 THR A C     1 
ATOM   21159 O  O     . THR A 1 4383 ? 98.377  125.606 96.220  1.00 63.54  ? 4383 THR A O     1 
ATOM   21160 C  CB    . THR A 1 4383 ? 98.663  123.805 93.452  1.00 57.58  ? 4383 THR A CB    1 
ATOM   21161 O  OG1   . THR A 1 4383 ? 98.608  123.912 92.024  1.00 56.21  ? 4383 THR A OG1   1 
ATOM   21162 C  CG2   . THR A 1 4383 ? 97.263  123.556 93.985  1.00 55.70  ? 4383 THR A CG2   1 
ATOM   21163 N  N     . ALA A 1 4384 ? 100.237 124.341 96.140  1.00 61.25  ? 4384 ALA A N     1 
ATOM   21164 C  CA    . ALA A 1 4384 ? 100.308 124.229 97.592  1.00 60.79  ? 4384 ALA A CA    1 
ATOM   21165 C  C     . ALA A 1 4384 ? 100.641 125.568 98.238  1.00 58.94  ? 4384 ALA A C     1 
ATOM   21166 O  O     . ALA A 1 4384 ? 100.114 125.891 99.309  1.00 59.43  ? 4384 ALA A O     1 
ATOM   21167 C  CB    . ALA A 1 4384 ? 101.332 123.165 97.985  1.00 61.10  ? 4384 ALA A CB    1 
ATOM   21168 N  N     . SER A 1 4385 ? 101.509 126.364 97.606  1.00 62.82  ? 4385 SER A N     1 
ATOM   21169 C  CA    . SER A 1 4385 ? 101.791 127.697 98.129  1.00 65.71  ? 4385 SER A CA    1 
ATOM   21170 C  C     . SER A 1 4385 ? 100.538 128.565 98.112  1.00 68.25  ? 4385 SER A C     1 
ATOM   21171 O  O     . SER A 1 4385 ? 100.235 129.265 99.088  1.00 70.62  ? 4385 SER A O     1 
ATOM   21172 C  CB    . SER A 1 4385 ? 102.914 128.350 97.322  1.00 65.78  ? 4385 SER A CB    1 
ATOM   21173 O  OG    . SER A 1 4385 ? 104.080 127.545 97.328  1.00 66.04  ? 4385 SER A OG    1 
ATOM   21174 N  N     . ASN A 1 4386 ? 99.784  128.519 97.010  1.00 65.27  ? 4386 ASN A N     1 
ATOM   21175 C  CA    . ASN A 1 4386 ? 98.536  129.271 96.944  1.00 63.46  ? 4386 ASN A CA    1 
ATOM   21176 C  C     . ASN A 1 4386 ? 97.555  128.800 98.008  1.00 63.73  ? 4386 ASN A C     1 
ATOM   21177 O  O     . ASN A 1 4386 ? 96.879  129.617 98.643  1.00 64.92  ? 4386 ASN A O     1 
ATOM   21178 C  CB    . ASN A 1 4386 ? 97.917  129.152 95.551  1.00 63.70  ? 4386 ASN A CB    1 
ATOM   21179 C  CG    . ASN A 1 4386 ? 98.838  129.658 94.460  1.00 70.15  ? 4386 ASN A CG    1 
ATOM   21180 O  OD1   . ASN A 1 4386 ? 99.937  130.141 94.733  1.00 73.51  ? 4386 ASN A OD1   1 
ATOM   21181 N  ND2   . ASN A 1 4386 ? 98.393  129.549 93.214  1.00 64.68  ? 4386 ASN A ND2   1 
ATOM   21182 N  N     . TRP A 1 4387 ? 97.467  127.485 98.221  1.00 60.43  ? 4387 TRP A N     1 
ATOM   21183 C  CA    . TRP A 1 4387 ? 96.569  126.961 99.245  1.00 55.57  ? 4387 TRP A CA    1 
ATOM   21184 C  C     . TRP A 1 4387 ? 96.979  127.448 100.631 1.00 57.35  ? 4387 TRP A C     1 
ATOM   21185 O  O     . TRP A 1 4387 ? 96.129  127.810 101.450 1.00 60.43  ? 4387 TRP A O     1 
ATOM   21186 C  CB    . TRP A 1 4387 ? 96.542  125.434 99.194  1.00 53.52  ? 4387 TRP A CB    1 
ATOM   21187 C  CG    . TRP A 1 4387 ? 95.671  124.887 98.105  1.00 52.77  ? 4387 TRP A CG    1 
ATOM   21188 C  CD1   . TRP A 1 4387 ? 94.646  125.531 97.477  1.00 53.95  ? 4387 TRP A CD1   1 
ATOM   21189 C  CD2   . TRP A 1 4387 ? 95.725  123.572 97.538  1.00 53.02  ? 4387 TRP A CD2   1 
ATOM   21190 N  NE1   . TRP A 1 4387 ? 94.069  124.706 96.543  1.00 51.72  ? 4387 TRP A NE1   1 
ATOM   21191 C  CE2   . TRP A 1 4387 ? 94.713  123.497 96.561  1.00 52.59  ? 4387 TRP A CE2   1 
ATOM   21192 C  CE3   . TRP A 1 4387 ? 96.536  122.455 97.756  1.00 53.88  ? 4387 TRP A CE3   1 
ATOM   21193 C  CZ2   . TRP A 1 4387 ? 94.489  122.349 95.805  1.00 55.00  ? 4387 TRP A CZ2   1 
ATOM   21194 C  CZ3   . TRP A 1 4387 ? 96.313  121.316 97.004  1.00 57.89  ? 4387 TRP A CZ3   1 
ATOM   21195 C  CH2   . TRP A 1 4387 ? 95.298  121.272 96.040  1.00 58.81  ? 4387 TRP A CH2   1 
ATOM   21196 N  N     . LEU A 1 4388 ? 98.286  127.470 100.907 1.00 60.77  ? 4388 LEU A N     1 
ATOM   21197 C  CA    . LEU A 1 4388 ? 98.763  128.007 102.178 1.00 60.20  ? 4388 LEU A CA    1 
ATOM   21198 C  C     . LEU A 1 4388 ? 98.385  129.473 102.336 1.00 62.80  ? 4388 LEU A C     1 
ATOM   21199 O  O     . LEU A 1 4388 ? 98.022  129.913 103.433 1.00 60.48  ? 4388 LEU A O     1 
ATOM   21200 C  CB    . LEU A 1 4388 ? 100.276 127.829 102.300 1.00 61.38  ? 4388 LEU A CB    1 
ATOM   21201 C  CG    . LEU A 1 4388 ? 100.790 126.397 102.435 1.00 58.77  ? 4388 LEU A CG    1 
ATOM   21202 C  CD1   . LEU A 1 4388 ? 102.307 126.367 102.393 1.00 57.87  ? 4388 LEU A CD1   1 
ATOM   21203 C  CD2   . LEU A 1 4388 ? 100.284 125.805 103.737 1.00 54.45  ? 4388 LEU A CD2   1 
ATOM   21204 N  N     . HIS A 1 4389 ? 98.477  130.250 101.255 1.00 65.63  ? 4389 HIS A N     1 
ATOM   21205 C  CA    . HIS A 1 4389 ? 98.045  131.645 101.324 1.00 67.75  ? 4389 HIS A CA    1 
ATOM   21206 C  C     . HIS A 1 4389 ? 96.551  131.752 101.620 1.00 63.22  ? 4389 HIS A C     1 
ATOM   21207 O  O     . HIS A 1 4389 ? 96.131  132.577 102.440 1.00 61.30  ? 4389 HIS A O     1 
ATOM   21208 C  CB    . HIS A 1 4389 ? 98.394  132.382 100.030 1.00 70.23  ? 4389 HIS A CB    1 
ATOM   21209 C  CG    . HIS A 1 4389 ? 99.796  132.152 99.560  1.00 75.87  ? 4389 HIS A CG    1 
ATOM   21210 N  ND1   . HIS A 1 4389 ? 100.140 132.132 98.225  1.00 80.63  ? 4389 HIS A ND1   1 
ATOM   21211 C  CD2   . HIS A 1 4389 ? 100.945 131.950 100.247 1.00 75.66  ? 4389 HIS A CD2   1 
ATOM   21212 C  CE1   . HIS A 1 4389 ? 101.439 131.918 98.110  1.00 81.36  ? 4389 HIS A CE1   1 
ATOM   21213 N  NE2   . HIS A 1 4389 ? 101.951 131.803 99.323  1.00 84.65  ? 4389 HIS A NE2   1 
ATOM   21214 N  N     . LEU A 1 4390 ? 95.732  130.926 100.966 1.00 60.28  ? 4390 LEU A N     1 
ATOM   21215 C  CA    . LEU A 1 4390 ? 94.286  131.011 101.165 1.00 59.21  ? 4390 LEU A CA    1 
ATOM   21216 C  C     . LEU A 1 4390 ? 93.876  130.476 102.533 1.00 58.79  ? 4390 LEU A C     1 
ATOM   21217 O  O     . LEU A 1 4390 ? 93.025  131.066 103.209 1.00 58.62  ? 4390 LEU A O     1 
ATOM   21218 C  CB    . LEU A 1 4390 ? 93.548  130.261 100.054 1.00 55.97  ? 4390 LEU A CB    1 
ATOM   21219 C  CG    . LEU A 1 4390 ? 93.929  130.565 98.605  1.00 65.69  ? 4390 LEU A CG    1 
ATOM   21220 C  CD1   . LEU A 1 4390 ? 93.153  129.670 97.649  1.00 64.43  ? 4390 LEU A CD1   1 
ATOM   21221 C  CD2   . LEU A 1 4390 ? 93.699  132.033 98.279  1.00 64.35  ? 4390 LEU A CD2   1 
ATOM   21222 N  N     . ILE A 1 4391 ? 94.461  129.358 102.953 1.00 58.83  ? 4391 ILE A N     1 
ATOM   21223 C  CA    . ILE A 1 4391 ? 94.026  128.719 104.202 1.00 55.87  ? 4391 ILE A CA    1 
ATOM   21224 C  C     . ILE A 1 4391 ? 94.411  129.598 105.387 1.00 57.21  ? 4391 ILE A C     1 
ATOM   21225 O  O     . ILE A 1 4391 ? 95.576  130.031 105.486 1.00 57.81  ? 4391 ILE A O     1 
ATOM   21226 C  CB    . ILE A 1 4391 ? 94.642  127.315 104.335 1.00 55.51  ? 4391 ILE A CB    1 
ATOM   21227 C  CG1   . ILE A 1 4391 ? 94.073  126.379 103.267 1.00 52.70  ? 4391 ILE A CG1   1 
ATOM   21228 C  CG2   . ILE A 1 4391 ? 94.394  126.752 105.723 1.00 52.64  ? 4391 ILE A CG2   1 
ATOM   21229 C  CD1   . ILE A 1 4391 ? 94.371  124.915 103.508 1.00 50.35  ? 4391 ILE A CD1   1 
ATOM   21230 N  N     . PRO A 1 4392 ? 93.490  129.897 106.302 1.00 57.55  ? 4392 PRO A N     1 
ATOM   21231 C  CA    . PRO A 1 4392 ? 93.846  130.685 107.485 1.00 57.63  ? 4392 PRO A CA    1 
ATOM   21232 C  C     . PRO A 1 4392 ? 94.790  129.916 108.398 1.00 58.12  ? 4392 PRO A C     1 
ATOM   21233 O  O     . PRO A 1 4392 ? 94.863  128.685 108.369 1.00 60.53  ? 4392 PRO A O     1 
ATOM   21234 C  CB    . PRO A 1 4392 ? 92.493  130.939 108.161 1.00 56.95  ? 4392 PRO A CB    1 
ATOM   21235 C  CG    . PRO A 1 4392 ? 91.483  130.753 107.065 1.00 53.91  ? 4392 PRO A CG    1 
ATOM   21236 C  CD    . PRO A 1 4392 ? 92.043  129.637 106.239 1.00 56.78  ? 4392 PRO A CD    1 
ATOM   21237 N  N     . GLN A 1 4393 ? 95.523  130.663 109.225 1.00 60.76  ? 4393 GLN A N     1 
ATOM   21238 C  CA    . GLN A 1 4393 ? 96.665  130.122 109.952 1.00 59.00  ? 4393 GLN A CA    1 
ATOM   21239 C  C     . GLN A 1 4393 ? 96.475  130.149 111.467 1.00 62.49  ? 4393 GLN A C     1 
ATOM   21240 O  O     . GLN A 1 4393 ? 97.386  129.787 112.213 1.00 65.55  ? 4393 GLN A O     1 
ATOM   21241 C  CB    . GLN A 1 4393 ? 97.935  130.880 109.570 1.00 52.82  ? 4393 GLN A CB    1 
ATOM   21242 C  CG    . GLN A 1 4393 ? 98.009  131.254 108.099 1.00 55.85  ? 4393 GLN A CG    1 
ATOM   21243 C  CD    . GLN A 1 4393 ? 99.260  132.035 107.757 1.00 62.01  ? 4393 GLN A CD    1 
ATOM   21244 O  OE1   . GLN A 1 4393 ? 100.090 132.312 108.623 1.00 63.33  ? 4393 GLN A OE1   1 
ATOM   21245 N  NE2   . GLN A 1 4393 ? 99.402  132.398 106.487 1.00 59.88  ? 4393 GLN A NE2   1 
ATOM   21246 N  N     . THR A 1 4394 ? 95.305  130.571 111.946 1.00 64.12  ? 4394 THR A N     1 
ATOM   21247 C  CA    . THR A 1 4394 ? 95.082  130.702 113.380 1.00 68.73  ? 4394 THR A CA    1 
ATOM   21248 C  C     . THR A 1 4394 ? 93.711  130.161 113.755 1.00 66.81  ? 4394 THR A C     1 
ATOM   21249 O  O     . THR A 1 4394 ? 92.722  130.400 113.060 1.00 70.87  ? 4394 THR A O     1 
ATOM   21250 C  CB    . THR A 1 4394 ? 95.186  132.165 113.848 1.00 73.04  ? 4394 THR A CB    1 
ATOM   21251 O  OG1   . THR A 1 4394 ? 94.264  132.974 113.107 1.00 75.47  ? 4394 THR A OG1   1 
ATOM   21252 C  CG2   . THR A 1 4394 ? 96.599  132.701 113.659 1.00 61.73  ? 4394 THR A CG2   1 
ATOM   21253 N  N     . LEU A 1 4395 ? 93.667  129.410 114.857 1.00 58.81  ? 4395 LEU A N     1 
ATOM   21254 C  CA    . LEU A 1 4395 ? 92.406  129.056 115.500 1.00 63.50  ? 4395 LEU A CA    1 
ATOM   21255 C  C     . LEU A 1 4395 ? 92.637  128.699 116.964 1.00 65.51  ? 4395 LEU A C     1 
ATOM   21256 O  O     . LEU A 1 4395 ? 93.119  127.605 117.274 1.00 59.09  ? 4395 LEU A O     1 
ATOM   21257 C  CB    . LEU A 1 4395 ? 91.715  127.905 114.766 1.00 62.79  ? 4395 LEU A CB    1 
ATOM   21258 C  CG    . LEU A 1 4395 ? 90.343  127.540 115.336 1.00 60.64  ? 4395 LEU A CG    1 
ATOM   21259 C  CD1   . LEU A 1 4395 ? 89.397  128.722 115.219 1.00 57.29  ? 4395 LEU A CD1   1 
ATOM   21260 C  CD2   . LEU A 1 4395 ? 89.764  126.336 114.620 1.00 54.05  ? 4395 LEU A CD2   1 
ATOM   21261 N  N     . SER A 1 4396 ? 92.296  129.614 117.869 1.00 65.99  ? 4396 SER A N     1 
ATOM   21262 C  CA    . SER A 1 4396 ? 92.545  129.397 119.289 1.00 60.10  ? 4396 SER A CA    1 
ATOM   21263 C  C     . SER A 1 4396 ? 91.392  128.633 119.928 1.00 66.70  ? 4396 SER A C     1 
ATOM   21264 O  O     . SER A 1 4396 ? 90.222  128.874 119.616 1.00 69.44  ? 4396 SER A O     1 
ATOM   21265 C  CB    . SER A 1 4396 ? 92.752  130.734 119.998 1.00 61.93  ? 4396 SER A CB    1 
ATOM   21266 O  OG    . SER A 1 4396 ? 91.631  131.582 119.821 1.00 72.92  ? 4396 SER A OG    1 
ATOM   21267 N  N     . HIS A 1 4397 ? 91.726  127.710 120.826 1.00 66.59  ? 4397 HIS A N     1 
ATOM   21268 C  CA    . HIS A 1 4397 ? 90.716  126.915 121.508 1.00 66.59  ? 4397 HIS A CA    1 
ATOM   21269 C  C     . HIS A 1 4397 ? 89.927  127.765 122.498 1.00 69.48  ? 4397 HIS A C     1 
ATOM   21270 O  O     . HIS A 1 4397 ? 90.407  128.783 123.003 1.00 69.50  ? 4397 HIS A O     1 
ATOM   21271 C  CB    . HIS A 1 4397 ? 91.365  125.740 122.240 1.00 64.73  ? 4397 HIS A CB    1 
ATOM   21272 C  CG    . HIS A 1 4397 ? 91.785  124.622 121.339 1.00 69.93  ? 4397 HIS A CG    1 
ATOM   21273 N  ND1   . HIS A 1 4397 ? 91.673  123.296 121.697 1.00 67.35  ? 4397 HIS A ND1   1 
ATOM   21274 C  CD2   . HIS A 1 4397 ? 92.318  124.632 120.094 1.00 72.09  ? 4397 HIS A CD2   1 
ATOM   21275 C  CE1   . HIS A 1 4397 ? 92.119  122.537 120.712 1.00 66.81  ? 4397 HIS A CE1   1 
ATOM   21276 N  NE2   . HIS A 1 4397 ? 92.516  123.323 119.728 1.00 73.31  ? 4397 HIS A NE2   1 
ATOM   21277 N  N     . LEU A 1 4398 ? 88.699  127.332 122.773 1.00 69.16  ? 4398 LEU A N     1 
ATOM   21278 C  CA    . LEU A 1 4398 ? 87.871  128.005 123.764 1.00 66.20  ? 4398 LEU A CA    1 
ATOM   21279 C  C     . LEU A 1 4398 ? 88.346  127.664 125.172 1.00 68.55  ? 4398 LEU A C     1 
ATOM   21280 O  O     . LEU A 1 4398 ? 88.768  126.538 125.447 1.00 70.11  ? 4398 LEU A O     1 
ATOM   21281 C  CB    . LEU A 1 4398 ? 86.405  127.609 123.591 1.00 63.10  ? 4398 LEU A CB    1 
ATOM   21282 C  CG    . LEU A 1 4398 ? 85.776  127.861 122.218 1.00 63.36  ? 4398 LEU A CG    1 
ATOM   21283 C  CD1   . LEU A 1 4398 ? 84.267  127.679 122.278 1.00 56.85  ? 4398 LEU A CD1   1 
ATOM   21284 C  CD2   . LEU A 1 4398 ? 86.131  129.249 121.706 1.00 57.27  ? 4398 LEU A CD2   1 
ATOM   21285 N  N     . LYS A 1 4399 ? 88.273  128.647 126.066 1.00 68.13  ? 4399 LYS A N     1 
ATOM   21286 C  CA    . LYS A 1 4399 ? 88.721  128.480 127.443 1.00 60.25  ? 4399 LYS A CA    1 
ATOM   21287 C  C     . LYS A 1 4399 ? 87.579  127.924 128.285 1.00 59.49  ? 4399 LYS A C     1 
ATOM   21288 O  O     . LYS A 1 4399 ? 86.507  128.535 128.369 1.00 57.67  ? 4399 LYS A O     1 
ATOM   21289 C  CB    . LYS A 1 4399 ? 89.213  129.809 128.015 1.00 58.83  ? 4399 LYS A CB    1 
ATOM   21290 C  CG    . LYS A 1 4399 ? 89.715  129.717 129.447 1.00 58.13  ? 4399 LYS A CG    1 
ATOM   21291 C  CD    . LYS A 1 4399 ? 89.632  131.061 130.149 1.00 60.33  ? 4399 LYS A CD    1 
ATOM   21292 C  CE    . LYS A 1 4399 ? 88.191  131.525 130.282 1.00 65.03  ? 4399 LYS A CE    1 
ATOM   21293 N  NZ    . LYS A 1 4399 ? 88.090  132.832 130.988 1.00 68.24  ? 4399 LYS A NZ    1 
ATOM   21294 N  N     . ARG A 1 4400 ? 87.811  126.773 128.911 1.00 61.84  ? 4400 ARG A N     1 
ATOM   21295 C  CA    . ARG A 1 4400 ? 86.786  126.148 129.734 1.00 60.50  ? 4400 ARG A CA    1 
ATOM   21296 C  C     . ARG A 1 4400 ? 86.640  126.893 131.055 1.00 63.95  ? 4400 ARG A C     1 
ATOM   21297 O  O     . ARG A 1 4400 ? 87.633  127.224 131.710 1.00 66.08  ? 4400 ARG A O     1 
ATOM   21298 C  CB    . ARG A 1 4400 ? 87.129  124.681 129.986 1.00 53.74  ? 4400 ARG A CB    1 
ATOM   21299 C  CG    . ARG A 1 4400 ? 87.360  123.880 128.717 1.00 53.80  ? 4400 ARG A CG    1 
ATOM   21300 C  CD    . ARG A 1 4400 ? 87.407  122.385 128.991 1.00 57.38  ? 4400 ARG A CD    1 
ATOM   21301 N  NE    . ARG A 1 4400 ? 86.130  121.875 129.477 1.00 59.50  ? 4400 ARG A NE    1 
ATOM   21302 C  CZ    . ARG A 1 4400 ? 85.832  120.587 129.585 1.00 51.45  ? 4400 ARG A CZ    1 
ATOM   21303 N  NH1   . ARG A 1 4400 ? 86.693  119.646 129.236 1.00 42.35  ? 4400 ARG A NH1   1 
ATOM   21304 N  NH2   . ARG A 1 4400 ? 84.638  120.235 130.052 1.00 46.83  ? 4400 ARG A NH2   1 
ATOM   21305 N  N     . THR A 1 4401 ? 85.395  127.155 131.445 1.00 62.85  ? 4401 THR A N     1 
ATOM   21306 C  CA    . THR A 1 4401 ? 85.078  127.848 132.683 1.00 66.25  ? 4401 THR A CA    1 
ATOM   21307 C  C     . THR A 1 4401 ? 83.975  127.078 133.396 1.00 67.86  ? 4401 THR A C     1 
ATOM   21308 O  O     . THR A 1 4401 ? 83.170  126.395 132.757 1.00 65.51  ? 4401 THR A O     1 
ATOM   21309 C  CB    . THR A 1 4401 ? 84.645  129.305 132.406 1.00 65.55  ? 4401 THR A CB    1 
ATOM   21310 O  OG1   . THR A 1 4401 ? 85.682  129.979 131.683 1.00 63.10  ? 4401 THR A OG1   1 
ATOM   21311 C  CG2   . THR A 1 4401 ? 84.386  130.066 133.700 1.00 60.69  ? 4401 THR A CG2   1 
ATOM   21312 N  N     . VAL A 1 4402 ? 83.947  127.188 134.728 1.00 73.81  ? 4402 VAL A N     1 
ATOM   21313 C  CA    . VAL A 1 4402 ? 82.986  126.427 135.524 1.00 72.00  ? 4402 VAL A CA    1 
ATOM   21314 C  C     . VAL A 1 4402 ? 81.558  126.743 135.095 1.00 64.99  ? 4402 VAL A C     1 
ATOM   21315 O  O     . VAL A 1 4402 ? 80.700  125.854 135.045 1.00 62.06  ? 4402 VAL A O     1 
ATOM   21316 C  CB    . VAL A 1 4402 ? 83.203  126.697 137.026 1.00 73.48  ? 4402 VAL A CB    1 
ATOM   21317 C  CG1   . VAL A 1 4402 ? 84.449  125.979 137.518 1.00 71.03  ? 4402 VAL A CG1   1 
ATOM   21318 C  CG2   . VAL A 1 4402 ? 83.309  128.192 137.292 1.00 71.29  ? 4402 VAL A CG2   1 
ATOM   21319 N  N     . GLU A 1 4403 ? 81.279  128.008 134.782 1.00 64.13  ? 4403 GLU A N     1 
ATOM   21320 C  CA    . GLU A 1 4403 ? 79.966  128.392 134.284 1.00 65.20  ? 4403 GLU A CA    1 
ATOM   21321 C  C     . GLU A 1 4403 ? 79.834  128.244 132.773 1.00 63.01  ? 4403 GLU A C     1 
ATOM   21322 O  O     . GLU A 1 4403 ? 78.708  128.237 132.263 1.00 59.14  ? 4403 GLU A O     1 
ATOM   21323 C  CB    . GLU A 1 4403 ? 79.645  129.833 134.699 1.00 63.55  ? 4403 GLU A CB    1 
ATOM   21324 C  CG    . GLU A 1 4403 ? 80.622  130.884 134.188 1.00 68.22  ? 4403 GLU A CG    1 
ATOM   21325 C  CD    . GLU A 1 4403 ? 80.251  131.423 132.821 1.00 73.90  ? 4403 GLU A CD    1 
ATOM   21326 O  OE1   . GLU A 1 4403 ? 79.079  131.269 132.416 1.00 73.09  ? 4403 GLU A OE1   1 
ATOM   21327 O  OE2   . GLU A 1 4403 ? 81.130  132.008 132.154 1.00 74.14  ? 4403 GLU A OE2   1 
ATOM   21328 N  N     . ASN A 1 4404 ? 80.949  128.121 132.049 1.00 61.26  ? 4404 ASN A N     1 
ATOM   21329 C  CA    . ASN A 1 4404 ? 80.871  127.880 130.612 1.00 57.18  ? 4404 ASN A CA    1 
ATOM   21330 C  C     . ASN A 1 4404 ? 80.492  126.438 130.302 1.00 59.02  ? 4404 ASN A C     1 
ATOM   21331 O  O     . ASN A 1 4404 ? 79.893  126.168 129.256 1.00 62.13  ? 4404 ASN A O     1 
ATOM   21332 C  CB    . ASN A 1 4404 ? 82.199  128.231 129.940 1.00 55.96  ? 4404 ASN A CB    1 
ATOM   21333 C  CG    . ASN A 1 4404 ? 82.314  129.705 129.608 1.00 59.28  ? 4404 ASN A CG    1 
ATOM   21334 O  OD1   . ASN A 1 4404 ? 81.379  130.476 129.822 1.00 58.80  ? 4404 ASN A OD1   1 
ATOM   21335 N  ND2   . ASN A 1 4404 ? 83.466  130.105 129.083 1.00 58.57  ? 4404 ASN A ND2   1 
ATOM   21336 N  N     . ILE A 1 4405 ? 80.837  125.501 131.190 1.00 59.17  ? 4405 ILE A N     1 
ATOM   21337 C  CA    . ILE A 1 4405 ? 80.515  124.098 130.950 1.00 56.70  ? 4405 ILE A CA    1 
ATOM   21338 C  C     . ILE A 1 4405 ? 79.005  123.883 130.958 1.00 56.15  ? 4405 ILE A C     1 
ATOM   21339 O  O     . ILE A 1 4405 ? 78.492  122.993 130.269 1.00 58.59  ? 4405 ILE A O     1 
ATOM   21340 C  CB    . ILE A 1 4405 ? 81.223  123.204 131.987 1.00 55.19  ? 4405 ILE A CB    1 
ATOM   21341 C  CG1   . ILE A 1 4405 ? 82.737  123.424 131.949 1.00 60.35  ? 4405 ILE A CG1   1 
ATOM   21342 C  CG2   . ILE A 1 4405 ? 80.935  121.739 131.721 1.00 47.20  ? 4405 ILE A CG2   1 
ATOM   21343 C  CD1   . ILE A 1 4405 ? 83.334  123.405 130.558 1.00 59.57  ? 4405 ILE A CD1   1 
ATOM   21344 N  N     . LYS A 1 4406 ? 78.269  124.694 131.720 1.00 55.98  ? 4406 LYS A N     1 
ATOM   21345 C  CA    . LYS A 1 4406 ? 76.821  124.549 131.808 1.00 57.49  ? 4406 LYS A CA    1 
ATOM   21346 C  C     . LYS A 1 4406 ? 76.096  125.069 130.573 1.00 58.11  ? 4406 LYS A C     1 
ATOM   21347 O  O     . LYS A 1 4406 ? 74.886  124.851 130.452 1.00 53.63  ? 4406 LYS A O     1 
ATOM   21348 C  CB    . LYS A 1 4406 ? 76.302  125.271 133.053 1.00 55.50  ? 4406 LYS A CB    1 
ATOM   21349 C  CG    . LYS A 1 4406 ? 76.855  124.721 134.358 1.00 60.01  ? 4406 LYS A CG    1 
ATOM   21350 C  CD    . LYS A 1 4406 ? 76.357  123.312 134.630 1.00 58.20  ? 4406 LYS A CD    1 
ATOM   21351 C  CE    . LYS A 1 4406 ? 76.854  122.804 135.974 1.00 54.08  ? 4406 LYS A CE    1 
ATOM   21352 N  NZ    . LYS A 1 4406 ? 76.413  121.408 136.239 1.00 45.26  ? 4406 LYS A NZ    1 
ATOM   21353 N  N     . ASP A 1 4407 ? 76.795  125.746 129.663 1.00 57.49  ? 4407 ASP A N     1 
ATOM   21354 C  CA    . ASP A 1 4407 ? 76.162  126.334 128.489 1.00 59.01  ? 4407 ASP A CA    1 
ATOM   21355 C  C     . ASP A 1 4407 ? 76.234  125.358 127.322 1.00 56.32  ? 4407 ASP A C     1 
ATOM   21356 O  O     . ASP A 1 4407 ? 77.341  125.033 126.871 1.00 55.76  ? 4407 ASP A O     1 
ATOM   21357 C  CB    . ASP A 1 4407 ? 76.842  127.642 128.117 1.00 60.01  ? 4407 ASP A CB    1 
ATOM   21358 C  CG    . ASP A 1 4407 ? 76.103  128.405 127.033 1.00 60.25  ? 4407 ASP A CG    1 
ATOM   21359 O  OD1   . ASP A 1 4407 ? 75.008  127.966 126.623 1.00 56.95  ? 4407 ASP A OD1   1 
ATOM   21360 O  OD2   . ASP A 1 4407 ? 76.621  129.451 126.588 1.00 63.01  ? 4407 ASP A OD2   1 
ATOM   21361 N  N     . PRO A 1 4408 ? 75.100  124.864 126.812 1.00 54.94  ? 4408 PRO A N     1 
ATOM   21362 C  CA    . PRO A 1 4408 ? 75.155  123.945 125.659 1.00 53.47  ? 4408 PRO A CA    1 
ATOM   21363 C  C     . PRO A 1 4408 ? 75.793  124.555 124.424 1.00 50.82  ? 4408 PRO A C     1 
ATOM   21364 O  O     . PRO A 1 4408 ? 76.507  123.861 123.685 1.00 47.23  ? 4408 PRO A O     1 
ATOM   21365 C  CB    . PRO A 1 4408 ? 73.676  123.603 125.418 1.00 49.28  ? 4408 PRO A CB    1 
ATOM   21366 C  CG    . PRO A 1 4408 ? 72.909  124.707 126.090 1.00 45.05  ? 4408 PRO A CG    1 
ATOM   21367 C  CD    . PRO A 1 4408 ? 73.723  125.087 127.280 1.00 49.96  ? 4408 PRO A CD    1 
ATOM   21368 N  N     . LEU A 1 4409 ? 75.546  125.845 124.179 1.00 52.28  ? 4409 LEU A N     1 
ATOM   21369 C  CA    . LEU A 1 4409 ? 76.153  126.510 123.032 1.00 52.52  ? 4409 LEU A CA    1 
ATOM   21370 C  C     . LEU A 1 4409 ? 77.669  126.494 123.139 1.00 55.35  ? 4409 LEU A C     1 
ATOM   21371 O  O     . LEU A 1 4409 ? 78.367  126.222 122.154 1.00 57.78  ? 4409 LEU A O     1 
ATOM   21372 C  CB    . LEU A 1 4409 ? 75.637  127.945 122.924 1.00 49.05  ? 4409 LEU A CB    1 
ATOM   21373 C  CG    . LEU A 1 4409 ? 74.461  128.199 121.978 1.00 51.18  ? 4409 LEU A CG    1 
ATOM   21374 C  CD1   . LEU A 1 4409 ? 74.068  129.668 121.997 1.00 47.36  ? 4409 LEU A CD1   1 
ATOM   21375 C  CD2   . LEU A 1 4409 ? 74.797  127.750 120.564 1.00 48.25  ? 4409 LEU A CD2   1 
ATOM   21376 N  N     . PHE A 1 4410 ? 78.197  126.768 124.334 1.00 53.23  ? 4410 PHE A N     1 
ATOM   21377 C  CA    . PHE A 1 4410 ? 79.641  126.735 124.526 1.00 52.02  ? 4410 PHE A CA    1 
ATOM   21378 C  C     . PHE A 1 4410 ? 80.192  125.329 124.335 1.00 53.63  ? 4410 PHE A C     1 
ATOM   21379 O  O     . PHE A 1 4410 ? 81.282  125.159 123.788 1.00 54.55  ? 4410 PHE A O     1 
ATOM   21380 C  CB    . PHE A 1 4410 ? 80.009  127.275 125.908 1.00 57.32  ? 4410 PHE A CB    1 
ATOM   21381 C  CG    . PHE A 1 4410 ? 81.468  127.605 126.058 1.00 56.83  ? 4410 PHE A CG    1 
ATOM   21382 C  CD1   . PHE A 1 4410 ? 82.382  126.626 126.412 1.00 55.71  ? 4410 PHE A CD1   1 
ATOM   21383 C  CD2   . PHE A 1 4410 ? 81.928  128.889 125.823 1.00 55.63  ? 4410 PHE A CD2   1 
ATOM   21384 C  CE1   . PHE A 1 4410 ? 83.723  126.925 126.544 1.00 54.22  ? 4410 PHE A CE1   1 
ATOM   21385 C  CE2   . PHE A 1 4410 ? 83.268  129.194 125.952 1.00 52.04  ? 4410 PHE A CE2   1 
ATOM   21386 C  CZ    . PHE A 1 4410 ? 84.166  128.211 126.313 1.00 53.79  ? 4410 PHE A CZ    1 
ATOM   21387 N  N     . ARG A 1 4411 ? 79.454  124.308 124.776 1.00 48.03  ? 4411 ARG A N     1 
ATOM   21388 C  CA    . ARG A 1 4411 ? 79.915  122.933 124.602 1.00 50.88  ? 4411 ARG A CA    1 
ATOM   21389 C  C     . ARG A 1 4411 ? 80.008  122.565 123.123 1.00 53.51  ? 4411 ARG A C     1 
ATOM   21390 O  O     . ARG A 1 4411 ? 81.027  122.027 122.659 1.00 56.15  ? 4411 ARG A O     1 
ATOM   21391 C  CB    . ARG A 1 4411 ? 78.977  121.981 125.345 1.00 46.86  ? 4411 ARG A CB    1 
ATOM   21392 C  CG    . ARG A 1 4411 ? 78.935  122.224 126.847 1.00 42.20  ? 4411 ARG A CG    1 
ATOM   21393 C  CD    . ARG A 1 4411 ? 78.132  121.164 127.581 1.00 43.73  ? 4411 ARG A CD    1 
ATOM   21394 N  NE    . ARG A 1 4411 ? 76.710  121.238 127.268 1.00 46.46  ? 4411 ARG A NE    1 
ATOM   21395 C  CZ    . ARG A 1 4411 ? 75.753  121.387 128.174 1.00 45.35  ? 4411 ARG A CZ    1 
ATOM   21396 N  NH1   . ARG A 1 4411 ? 76.031  121.491 129.463 1.00 40.52  ? 4411 ARG A NH1   1 
ATOM   21397 N  NH2   . ARG A 1 4411 ? 74.484  121.432 127.777 1.00 45.95  ? 4411 ARG A NH2   1 
ATOM   21398 N  N     . PHE A 1 4412 ? 78.949  122.859 122.363 1.00 52.64  ? 4412 PHE A N     1 
ATOM   21399 C  CA    . PHE A 1 4412 ? 78.971  122.560 120.935 1.00 52.28  ? 4412 PHE A CA    1 
ATOM   21400 C  C     . PHE A 1 4412 ? 80.066  123.346 120.225 1.00 52.53  ? 4412 PHE A C     1 
ATOM   21401 O  O     . PHE A 1 4412 ? 80.794  122.796 119.387 1.00 53.26  ? 4412 PHE A O     1 
ATOM   21402 C  CB    . PHE A 1 4412 ? 77.611  122.859 120.306 1.00 49.88  ? 4412 PHE A CB    1 
ATOM   21403 C  CG    . PHE A 1 4412 ? 77.677  123.109 118.828 1.00 50.56  ? 4412 PHE A CG    1 
ATOM   21404 C  CD1   . PHE A 1 4412 ? 77.811  122.052 117.946 1.00 46.26  ? 4412 PHE A CD1   1 
ATOM   21405 C  CD2   . PHE A 1 4412 ? 77.617  124.396 118.321 1.00 47.58  ? 4412 PHE A CD2   1 
ATOM   21406 C  CE1   . PHE A 1 4412 ? 77.879  122.269 116.587 1.00 44.22  ? 4412 PHE A CE1   1 
ATOM   21407 C  CE2   . PHE A 1 4412 ? 77.688  124.620 116.963 1.00 44.25  ? 4412 PHE A CE2   1 
ATOM   21408 C  CZ    . PHE A 1 4412 ? 77.818  123.554 116.096 1.00 44.67  ? 4412 PHE A CZ    1 
ATOM   21409 N  N     . PHE A 1 4413 ? 80.203  124.635 120.547 1.00 41.33  ? 4413 PHE A N     1 
ATOM   21410 C  CA    . PHE A 1 4413 ? 81.221  125.446 119.893 1.00 47.09  ? 4413 PHE A CA    1 
ATOM   21411 C  C     . PHE A 1 4413 ? 82.623  125.010 120.296 1.00 55.71  ? 4413 PHE A C     1 
ATOM   21412 O  O     . PHE A 1 4413 ? 83.559  125.137 119.502 1.00 60.02  ? 4413 PHE A O     1 
ATOM   21413 C  CB    . PHE A 1 4413 ? 80.995  126.922 120.214 1.00 50.14  ? 4413 PHE A CB    1 
ATOM   21414 C  CG    . PHE A 1 4413 ? 79.982  127.583 119.322 1.00 52.59  ? 4413 PHE A CG    1 
ATOM   21415 C  CD1   . PHE A 1 4413 ? 79.962  127.323 117.962 1.00 53.83  ? 4413 PHE A CD1   1 
ATOM   21416 C  CD2   . PHE A 1 4413 ? 79.045  128.459 119.845 1.00 52.89  ? 4413 PHE A CD2   1 
ATOM   21417 C  CE1   . PHE A 1 4413 ? 79.028  127.926 117.141 1.00 49.34  ? 4413 PHE A CE1   1 
ATOM   21418 C  CE2   . PHE A 1 4413 ? 78.110  129.066 119.028 1.00 51.98  ? 4413 PHE A CE2   1 
ATOM   21419 C  CZ    . PHE A 1 4413 ? 78.102  128.800 117.675 1.00 50.61  ? 4413 PHE A CZ    1 
ATOM   21420 N  N     . GLU A 1 4414 ? 82.788  124.485 121.512 1.00 54.91  ? 4414 GLU A N     1 
ATOM   21421 C  CA    . GLU A 1 4414 ? 84.076  123.944 121.924 1.00 54.30  ? 4414 GLU A CA    1 
ATOM   21422 C  C     . GLU A 1 4414 ? 84.440  122.717 121.106 1.00 51.58  ? 4414 GLU A C     1 
ATOM   21423 O  O     . GLU A 1 4414 ? 85.580  122.591 120.644 1.00 56.20  ? 4414 GLU A O     1 
ATOM   21424 C  CB    . GLU A 1 4414 ? 84.051  123.604 123.412 1.00 53.32  ? 4414 GLU A CB    1 
ATOM   21425 C  CG    . GLU A 1 4414 ? 85.379  123.104 123.947 1.00 57.43  ? 4414 GLU A CG    1 
ATOM   21426 C  CD    . GLU A 1 4414 ? 85.341  122.821 125.432 1.00 63.45  ? 4414 GLU A CD    1 
ATOM   21427 O  OE1   . GLU A 1 4414 ? 84.267  122.995 126.046 1.00 65.18  ? 4414 GLU A OE1   1 
ATOM   21428 O  OE2   . GLU A 1 4414 ? 86.384  122.416 125.984 1.00 66.80  ? 4414 GLU A OE2   1 
ATOM   21429 N  N     . ARG A 1 4415 ? 83.486  121.800 120.916 1.00 49.82  ? 4415 ARG A N     1 
ATOM   21430 C  CA    . ARG A 1 4415 ? 83.737  120.672 120.020 1.00 48.69  ? 4415 ARG A CA    1 
ATOM   21431 C  C     . ARG A 1 4415 ? 84.117  121.164 118.629 1.00 54.34  ? 4415 ARG A C     1 
ATOM   21432 O  O     . ARG A 1 4415 ? 85.088  120.683 118.023 1.00 59.42  ? 4415 ARG A O     1 
ATOM   21433 C  CB    . ARG A 1 4415 ? 82.509  119.766 119.938 1.00 45.56  ? 4415 ARG A CB    1 
ATOM   21434 C  CG    . ARG A 1 4415 ? 82.284  118.873 121.136 1.00 44.69  ? 4415 ARG A CG    1 
ATOM   21435 C  CD    . ARG A 1 4415 ? 81.274  117.794 120.787 1.00 37.24  ? 4415 ARG A CD    1 
ATOM   21436 N  NE    . ARG A 1 4415 ? 81.380  117.388 119.391 1.00 42.24  ? 4415 ARG A NE    1 
ATOM   21437 C  CZ    . ARG A 1 4415 ? 80.756  116.345 118.861 1.00 43.42  ? 4415 ARG A CZ    1 
ATOM   21438 N  NH1   . ARG A 1 4415 ? 79.955  115.579 119.583 1.00 36.08  ? 4415 ARG A NH1   1 
ATOM   21439 N  NH2   . ARG A 1 4415 ? 80.939  116.064 117.574 1.00 42.12  ? 4415 ARG A NH2   1 
ATOM   21440 N  N     . GLU A 1 4416 ? 83.353  122.132 118.114 1.00 53.93  ? 4416 GLU A N     1 
ATOM   21441 C  CA    . GLU A 1 4416 ? 83.598  122.674 116.781 1.00 53.68  ? 4416 GLU A CA    1 
ATOM   21442 C  C     . GLU A 1 4416 ? 85.019  123.209 116.659 1.00 52.81  ? 4416 GLU A C     1 
ATOM   21443 O  O     . GLU A 1 4416 ? 85.761  122.835 115.744 1.00 57.62  ? 4416 GLU A O     1 
ATOM   21444 C  CB    . GLU A 1 4416 ? 82.586  123.783 116.488 1.00 56.74  ? 4416 GLU A CB    1 
ATOM   21445 C  CG    . GLU A 1 4416 ? 81.274  123.318 115.877 1.00 53.80  ? 4416 GLU A CG    1 
ATOM   21446 C  CD    . GLU A 1 4416 ? 81.458  122.309 114.766 1.00 55.88  ? 4416 GLU A CD    1 
ATOM   21447 O  OE1   . GLU A 1 4416 ? 82.281  122.566 113.866 1.00 58.73  ? 4416 GLU A OE1   1 
ATOM   21448 O  OE2   . GLU A 1 4416 ? 80.781  121.261 114.793 1.00 56.47  ? 4416 GLU A OE2   1 
ATOM   21449 N  N     . VAL A 1 4417 ? 85.417  124.077 117.591 1.00 51.17  ? 4417 VAL A N     1 
ATOM   21450 C  CA    . VAL A 1 4417 ? 86.720  124.727 117.510 1.00 53.78  ? 4417 VAL A CA    1 
ATOM   21451 C  C     . VAL A 1 4417 ? 87.840  123.716 117.713 1.00 54.80  ? 4417 VAL A C     1 
ATOM   21452 O  O     . VAL A 1 4417 ? 88.883  123.796 117.058 1.00 49.51  ? 4417 VAL A O     1 
ATOM   21453 C  CB    . VAL A 1 4417 ? 86.804  125.884 118.523 1.00 53.93  ? 4417 VAL A CB    1 
ATOM   21454 C  CG1   . VAL A 1 4417 ? 88.194  126.497 118.520 1.00 56.22  ? 4417 VAL A CG1   1 
ATOM   21455 C  CG2   . VAL A 1 4417 ? 85.767  126.946 118.194 1.00 53.31  ? 4417 VAL A CG2   1 
ATOM   21456 N  N     . LYS A 1 4418 ? 87.645  122.742 118.606 1.00 55.86  ? 4418 LYS A N     1 
ATOM   21457 C  CA    . LYS A 1 4418 ? 88.680  121.740 118.837 1.00 55.62  ? 4418 LYS A CA    1 
ATOM   21458 C  C     . LYS A 1 4418 ? 88.949  120.926 117.576 1.00 55.30  ? 4418 LYS A C     1 
ATOM   21459 O  O     . LYS A 1 4418 ? 90.103  120.804 117.133 1.00 57.35  ? 4418 LYS A O     1 
ATOM   21460 C  CB    . LYS A 1 4418 ? 88.270  120.830 119.997 1.00 54.97  ? 4418 LYS A CB    1 
ATOM   21461 C  CG    . LYS A 1 4418 ? 89.433  120.321 120.832 1.00 61.98  ? 4418 LYS A CG    1 
ATOM   21462 C  CD    . LYS A 1 4418 ? 88.945  119.579 122.067 1.00 59.72  ? 4418 LYS A CD    1 
ATOM   21463 C  CE    . LYS A 1 4418 ? 87.975  120.427 122.877 1.00 58.34  ? 4418 LYS A CE    1 
ATOM   21464 N  NZ    . LYS A 1 4418 ? 87.421  119.683 124.041 1.00 55.73  ? 4418 LYS A NZ    1 
ATOM   21465 N  N     . MET A 1 4419 ? 87.893  120.372 116.971 1.00 54.92  ? 4419 MET A N     1 
ATOM   21466 C  CA    . MET A 1 4419 ? 88.111  119.562 115.775 1.00 54.39  ? 4419 MET A CA    1 
ATOM   21467 C  C     . MET A 1 4419 ? 88.610  120.418 114.616 1.00 50.38  ? 4419 MET A C     1 
ATOM   21468 O  O     . MET A 1 4419 ? 89.460  119.974 113.831 1.00 54.46  ? 4419 MET A O     1 
ATOM   21469 C  CB    . MET A 1 4419 ? 86.838  118.809 115.383 1.00 50.08  ? 4419 MET A CB    1 
ATOM   21470 C  CG    . MET A 1 4419 ? 85.616  119.672 115.154 1.00 55.30  ? 4419 MET A CG    1 
ATOM   21471 S  SD    . MET A 1 4419 ? 84.157  118.678 114.791 1.00 76.04  ? 4419 MET A SD    1 
ATOM   21472 C  CE    . MET A 1 4419 ? 84.833  117.517 113.605 1.00 53.56  ? 4419 MET A CE    1 
ATOM   21473 N  N     . GLY A 1 4420 ? 88.112  121.653 114.503 1.00 42.26  ? 4420 GLY A N     1 
ATOM   21474 C  CA    . GLY A 1 4420 ? 88.581  122.532 113.447 1.00 47.02  ? 4420 GLY A CA    1 
ATOM   21475 C  C     . GLY A 1 4420 ? 90.051  122.871 113.580 1.00 49.35  ? 4420 GLY A C     1 
ATOM   21476 O  O     . GLY A 1 4420 ? 90.780  122.893 112.589 1.00 48.13  ? 4420 GLY A O     1 
ATOM   21477 N  N     . ALA A 1 4421 ? 90.509  123.135 114.806 1.00 53.52  ? 4421 ALA A N     1 
ATOM   21478 C  CA    . ALA A 1 4421 ? 91.917  123.439 115.025 1.00 48.01  ? 4421 ALA A CA    1 
ATOM   21479 C  C     . ALA A 1 4421 ? 92.793  122.228 114.741 1.00 48.07  ? 4421 ALA A C     1 
ATOM   21480 O  O     . ALA A 1 4421 ? 93.869  122.362 114.144 1.00 48.45  ? 4421 ALA A O     1 
ATOM   21481 C  CB    . ALA A 1 4421 ? 92.132  123.937 116.453 1.00 51.14  ? 4421 ALA A CB    1 
ATOM   21482 N  N     . LYS A 1 4422 ? 92.353  121.038 115.160 1.00 47.31  ? 4422 LYS A N     1 
ATOM   21483 C  CA    . LYS A 1 4422 ? 93.125  119.834 114.865 1.00 47.21  ? 4422 LYS A CA    1 
ATOM   21484 C  C     . LYS A 1 4422 ? 93.260  119.631 113.358 1.00 48.66  ? 4422 LYS A C     1 
ATOM   21485 O  O     . LYS A 1 4422 ? 94.366  119.404 112.841 1.00 53.73  ? 4422 LYS A O     1 
ATOM   21486 C  CB    . LYS A 1 4422 ? 92.469  118.624 115.536 1.00 52.17  ? 4422 LYS A CB    1 
ATOM   21487 C  CG    . LYS A 1 4422 ? 93.179  117.291 115.330 1.00 53.22  ? 4422 LYS A CG    1 
ATOM   21488 C  CD    . LYS A 1 4422 ? 92.590  116.505 114.167 1.00 63.57  ? 4422 LYS A CD    1 
ATOM   21489 C  CE    . LYS A 1 4422 ? 91.201  115.986 114.500 1.00 64.47  ? 4422 LYS A CE    1 
ATOM   21490 N  NZ    . LYS A 1 4422 ? 90.613  115.207 113.376 1.00 62.65  ? 4422 LYS A NZ    1 
ATOM   21491 N  N     . LEU A 1 4423 ? 92.143  119.742 112.632 1.00 49.75  ? 4423 LEU A N     1 
ATOM   21492 C  CA    . LEU A 1 4423 ? 92.181  119.572 111.183 1.00 49.08  ? 4423 LEU A CA    1 
ATOM   21493 C  C     . LEU A 1 4423 ? 93.027  120.655 110.522 1.00 42.08  ? 4423 LEU A C     1 
ATOM   21494 O  O     . LEU A 1 4423 ? 93.766  120.380 109.569 1.00 41.83  ? 4423 LEU A O     1 
ATOM   21495 C  CB    . LEU A 1 4423 ? 90.760  119.576 110.620 1.00 47.40  ? 4423 LEU A CB    1 
ATOM   21496 C  CG    . LEU A 1 4423 ? 90.597  119.391 109.110 1.00 47.14  ? 4423 LEU A CG    1 
ATOM   21497 C  CD1   . LEU A 1 4423 ? 91.414  118.206 108.618 1.00 50.45  ? 4423 LEU A CD1   1 
ATOM   21498 C  CD2   . LEU A 1 4423 ? 89.130  119.221 108.749 1.00 47.20  ? 4423 LEU A CD2   1 
ATOM   21499 N  N     . LEU A 1 4424 ? 92.927  121.893 111.012 1.00 39.57  ? 4424 LEU A N     1 
ATOM   21500 C  CA    . LEU A 1 4424 ? 93.705  122.992 110.453 1.00 39.87  ? 4424 LEU A CA    1 
ATOM   21501 C  C     . LEU A 1 4424 ? 95.197  122.740 110.607 1.00 45.55  ? 4424 LEU A C     1 
ATOM   21502 O  O     . LEU A 1 4424 ? 95.969  122.914 109.657 1.00 45.82  ? 4424 LEU A O     1 
ATOM   21503 C  CB    . LEU A 1 4424 ? 93.313  124.301 111.139 1.00 39.85  ? 4424 LEU A CB    1 
ATOM   21504 C  CG    . LEU A 1 4424 ? 94.017  125.577 110.676 1.00 41.29  ? 4424 LEU A CG    1 
ATOM   21505 C  CD1   . LEU A 1 4424 ? 94.090  125.635 109.159 1.00 37.20  ? 4424 LEU A CD1   1 
ATOM   21506 C  CD2   . LEU A 1 4424 ? 93.339  126.812 111.243 1.00 49.40  ? 4424 LEU A CD2   1 
ATOM   21507 N  N     . GLN A 1 4425 ? 95.622  122.336 111.807 1.00 50.77  ? 4425 GLN A N     1 
ATOM   21508 C  CA    . GLN A 1 4425 ? 97.035  122.051 112.024 1.00 48.62  ? 4425 GLN A CA    1 
ATOM   21509 C  C     . GLN A 1 4425 ? 97.509  120.916 111.129 1.00 46.59  ? 4425 GLN A C     1 
ATOM   21510 O  O     . GLN A 1 4425 ? 98.579  121.007 110.513 1.00 41.86  ? 4425 GLN A O     1 
ATOM   21511 C  CB    . GLN A 1 4425 ? 97.292  121.722 113.495 1.00 50.44  ? 4425 GLN A CB    1 
ATOM   21512 C  CG    . GLN A 1 4425 ? 97.003  122.871 114.450 1.00 62.73  ? 4425 GLN A CG    1 
ATOM   21513 C  CD    . GLN A 1 4425 ? 96.842  122.411 115.885 1.00 69.52  ? 4425 GLN A CD    1 
ATOM   21514 O  OE1   . GLN A 1 4425 ? 95.799  122.623 116.504 1.00 63.28  ? 4425 GLN A OE1   1 
ATOM   21515 N  NE2   . GLN A 1 4425 ? 97.877  121.776 116.423 1.00 67.38  ? 4425 GLN A NE2   1 
ATOM   21516 N  N     . ASP A 1 4426 ? 96.715  119.843 111.025 1.00 48.70  ? 4426 ASP A N     1 
ATOM   21517 C  CA    . ASP A 1 4426 ? 97.118  118.725 110.177 1.00 44.64  ? 4426 ASP A CA    1 
ATOM   21518 C  C     . ASP A 1 4426 ? 97.261  119.152 108.719 1.00 42.37  ? 4426 ASP A C     1 
ATOM   21519 O  O     . ASP A 1 4426 ? 98.266  118.836 108.069 1.00 44.86  ? 4426 ASP A O     1 
ATOM   21520 C  CB    . ASP A 1 4426 ? 96.117  117.577 110.303 1.00 51.74  ? 4426 ASP A CB    1 
ATOM   21521 C  CG    . ASP A 1 4426 ? 95.992  117.068 111.723 1.00 59.51  ? 4426 ASP A CG    1 
ATOM   21522 O  OD1   . ASP A 1 4426 ? 96.923  117.298 112.523 1.00 59.14  ? 4426 ASP A OD1   1 
ATOM   21523 O  OD2   . ASP A 1 4426 ? 94.965  116.433 112.038 1.00 63.19  ? 4426 ASP A OD2   1 
ATOM   21524 N  N     . VAL A 1 4427 ? 96.278  119.888 108.195 1.00 39.47  ? 4427 VAL A N     1 
ATOM   21525 C  CA    . VAL A 1 4427 ? 96.311  120.284 106.789 1.00 39.42  ? 4427 VAL A CA    1 
ATOM   21526 C  C     . VAL A 1 4427 ? 97.467  121.239 106.521 1.00 42.19  ? 4427 VAL A C     1 
ATOM   21527 O  O     . VAL A 1 4427 ? 98.165  121.117 105.505 1.00 46.85  ? 4427 VAL A O     1 
ATOM   21528 C  CB    . VAL A 1 4427 ? 94.961  120.894 106.371 1.00 38.90  ? 4427 VAL A CB    1 
ATOM   21529 C  CG1   . VAL A 1 4427 ? 95.047  121.460 104.965 1.00 31.14  ? 4427 VAL A CG1   1 
ATOM   21530 C  CG2   . VAL A 1 4427 ? 93.865  119.846 106.443 1.00 41.19  ? 4427 VAL A CG2   1 
ATOM   21531 N  N     . ARG A 1 4428 ? 97.686  122.212 107.411 1.00 41.36  ? 4428 ARG A N     1 
ATOM   21532 C  CA    . ARG A 1 4428 ? 98.776  123.158 107.203 1.00 44.19  ? 4428 ARG A CA    1 
ATOM   21533 C  C     . ARG A 1 4428 ? 100.129 122.461 107.252 1.00 44.20  ? 4428 ARG A C     1 
ATOM   21534 O  O     . ARG A 1 4428 ? 101.010 122.749 106.432 1.00 41.79  ? 4428 ARG A O     1 
ATOM   21535 C  CB    . ARG A 1 4428 ? 98.711  124.284 108.233 1.00 47.24  ? 4428 ARG A CB    1 
ATOM   21536 C  CG    . ARG A 1 4428 ? 97.526  125.215 108.050 1.00 45.32  ? 4428 ARG A CG    1 
ATOM   21537 C  CD    . ARG A 1 4428 ? 97.683  126.482 108.876 1.00 51.09  ? 4428 ARG A CD    1 
ATOM   21538 N  NE    . ARG A 1 4428 ? 98.829  127.276 108.450 1.00 54.62  ? 4428 ARG A NE    1 
ATOM   21539 C  CZ    . ARG A 1 4428 ? 98.885  127.973 107.323 1.00 50.41  ? 4428 ARG A CZ    1 
ATOM   21540 N  NH1   . ARG A 1 4428 ? 97.862  128.017 106.485 1.00 51.04  ? 4428 ARG A NH1   1 
ATOM   21541 N  NH2   . ARG A 1 4428 ? 99.993  128.649 107.033 1.00 46.99  ? 4428 ARG A NH2   1 
ATOM   21542 N  N     . GLN A 1 4429 ? 100.316 121.538 108.200 1.00 45.90  ? 4429 GLN A N     1 
ATOM   21543 C  CA    . GLN A 1 4429 ? 101.573 120.799 108.257 1.00 49.12  ? 4429 GLN A CA    1 
ATOM   21544 C  C     . GLN A 1 4429 ? 101.772 119.959 107.002 1.00 48.81  ? 4429 GLN A C     1 
ATOM   21545 O  O     . GLN A 1 4429 ? 102.881 119.897 106.456 1.00 49.86  ? 4429 GLN A O     1 
ATOM   21546 C  CB    . GLN A 1 4429 ? 101.610 119.919 109.507 1.00 48.71  ? 4429 GLN A CB    1 
ATOM   21547 C  CG    . GLN A 1 4429 ? 102.915 119.164 109.690 1.00 55.72  ? 4429 GLN A CG    1 
ATOM   21548 C  CD    . GLN A 1 4429 ? 104.104 120.090 109.853 1.00 61.74  ? 4429 GLN A CD    1 
ATOM   21549 O  OE1   . GLN A 1 4429 ? 104.903 120.263 108.932 1.00 60.32  ? 4429 GLN A OE1   1 
ATOM   21550 N  NE2   . GLN A 1 4429 ? 104.228 120.693 111.030 1.00 59.63  ? 4429 GLN A NE2   1 
ATOM   21551 N  N     . ASP A 1 4430 ? 100.704 119.314 106.522 1.00 45.41  ? 4430 ASP A N     1 
ATOM   21552 C  CA    . ASP A 1 4430 ? 100.812 118.500 105.315 1.00 44.18  ? 4430 ASP A CA    1 
ATOM   21553 C  C     . ASP A 1 4430 ? 101.194 119.349 104.110 1.00 46.12  ? 4430 ASP A C     1 
ATOM   21554 O  O     . ASP A 1 4430 ? 102.062 118.964 103.316 1.00 49.72  ? 4430 ASP A O     1 
ATOM   21555 C  CB    . ASP A 1 4430 ? 99.492  117.777 105.057 1.00 43.61  ? 4430 ASP A CB    1 
ATOM   21556 C  CG    . ASP A 1 4430 ? 99.304  116.577 105.955 1.00 52.19  ? 4430 ASP A CG    1 
ATOM   21557 O  OD1   . ASP A 1 4430 ? 100.233 115.750 106.037 1.00 54.88  ? 4430 ASP A OD1   1 
ATOM   21558 O  OD2   . ASP A 1 4430 ? 98.227  116.454 106.572 1.00 56.36  ? 4430 ASP A OD2   1 
ATOM   21559 N  N     . LEU A 1 4431 ? 100.558 120.511 103.958 1.00 47.70  ? 4431 LEU A N     1 
ATOM   21560 C  CA    . LEU A 1 4431 ? 100.850 121.365 102.813 1.00 49.77  ? 4431 LEU A CA    1 
ATOM   21561 C  C     . LEU A 1 4431 ? 102.253 121.955 102.904 1.00 52.86  ? 4431 LEU A C     1 
ATOM   21562 O  O     . LEU A 1 4431 ? 102.936 122.101 101.885 1.00 52.09  ? 4431 LEU A O     1 
ATOM   21563 C  CB    . LEU A 1 4431 ? 99.798  122.467 102.701 1.00 51.73  ? 4431 LEU A CB    1 
ATOM   21564 C  CG    . LEU A 1 4431 ? 98.530  122.083 101.937 1.00 49.05  ? 4431 LEU A CG    1 
ATOM   21565 C  CD1   . LEU A 1 4431 ? 97.546  123.240 101.912 1.00 49.58  ? 4431 LEU A CD1   1 
ATOM   21566 C  CD2   . LEU A 1 4431 ? 98.869  121.629 100.526 1.00 47.22  ? 4431 LEU A CD2   1 
ATOM   21567 N  N     . ALA A 1 4432 ? 102.703 122.296 104.115 1.00 52.28  ? 4432 ALA A N     1 
ATOM   21568 C  CA    . ALA A 1 4432 ? 104.074 122.769 104.282 1.00 47.17  ? 4432 ALA A CA    1 
ATOM   21569 C  C     . ALA A 1 4432 ? 105.077 121.682 103.918 1.00 52.87  ? 4432 ALA A C     1 
ATOM   21570 O  O     . ALA A 1 4432 ? 106.097 121.956 103.272 1.00 56.43  ? 4432 ALA A O     1 
ATOM   21571 C  CB    . ALA A 1 4432 ? 104.295 123.249 105.716 1.00 46.58  ? 4432 ALA A CB    1 
ATOM   21572 N  N     . ASP A 1 4433 ? 104.804 120.438 104.323 1.00 53.78  ? 4433 ASP A N     1 
ATOM   21573 C  CA    . ASP A 1 4433 ? 105.680 119.332 103.948 1.00 53.14  ? 4433 ASP A CA    1 
ATOM   21574 C  C     . ASP A 1 4433 ? 105.697 119.129 102.438 1.00 51.11  ? 4433 ASP A C     1 
ATOM   21575 O  O     . ASP A 1 4433 ? 106.752 118.862 101.853 1.00 54.31  ? 4433 ASP A O     1 
ATOM   21576 C  CB    . ASP A 1 4433 ? 105.242 118.052 104.659 1.00 54.11  ? 4433 ASP A CB    1 
ATOM   21577 C  CG    . ASP A 1 4433 ? 105.517 118.090 106.149 1.00 61.28  ? 4433 ASP A CG    1 
ATOM   21578 O  OD1   . ASP A 1 4433 ? 104.899 117.296 106.890 1.00 62.45  ? 4433 ASP A OD1   1 
ATOM   21579 O  OD2   . ASP A 1 4433 ? 106.350 118.914 106.581 1.00 61.08  ? 4433 ASP A OD2   1 
ATOM   21580 N  N     . VAL A 1 4434 ? 104.536 119.252 101.791 1.00 48.40  ? 4434 VAL A N     1 
ATOM   21581 C  CA    . VAL A 1 4434 ? 104.479 119.125 100.335 1.00 50.40  ? 4434 VAL A CA    1 
ATOM   21582 C  C     . VAL A 1 4434 ? 105.298 120.224 99.669  1.00 57.47  ? 4434 VAL A C     1 
ATOM   21583 O  O     . VAL A 1 4434 ? 106.040 119.972 98.711  1.00 59.87  ? 4434 VAL A O     1 
ATOM   21584 C  CB    . VAL A 1 4434 ? 103.016 119.136 99.853  1.00 53.67  ? 4434 VAL A CB    1 
ATOM   21585 C  CG1   . VAL A 1 4434 ? 102.952 119.326 98.345  1.00 53.16  ? 4434 VAL A CG1   1 
ATOM   21586 C  CG2   . VAL A 1 4434 ? 102.326 117.848 100.249 1.00 50.87  ? 4434 VAL A CG2   1 
ATOM   21587 N  N     . VAL A 1 4435 ? 105.178 121.459 100.164 1.00 60.37  ? 4435 VAL A N     1 
ATOM   21588 C  CA    . VAL A 1 4435 ? 105.949 122.568 99.605  1.00 60.77  ? 4435 VAL A CA    1 
ATOM   21589 C  C     . VAL A 1 4435 ? 107.441 122.308 99.760  1.00 64.50  ? 4435 VAL A C     1 
ATOM   21590 O  O     . VAL A 1 4435 ? 108.227 122.506 98.825  1.00 68.33  ? 4435 VAL A O     1 
ATOM   21591 C  CB    . VAL A 1 4435 ? 105.540 123.896 100.269 1.00 57.93  ? 4435 VAL A CB    1 
ATOM   21592 C  CG1   . VAL A 1 4435 ? 106.558 124.983 99.958  1.00 61.51  ? 4435 VAL A CG1   1 
ATOM   21593 C  CG2   . VAL A 1 4435 ? 104.161 124.319 99.806  1.00 60.49  ? 4435 VAL A CG2   1 
ATOM   21594 N  N     . GLN A 1 4436 ? 107.854 121.853 100.946 1.00 62.89  ? 4436 GLN A N     1 
ATOM   21595 C  CA    . GLN A 1 4436 ? 109.269 121.587 101.181 1.00 60.57  ? 4436 GLN A CA    1 
ATOM   21596 C  C     . GLN A 1 4436 ? 109.776 120.444 100.309 1.00 62.44  ? 4436 GLN A C     1 
ATOM   21597 O  O     . GLN A 1 4436 ? 110.936 120.457 99.881  1.00 64.37  ? 4436 GLN A O     1 
ATOM   21598 C  CB    . GLN A 1 4436 ? 109.503 121.289 102.662 1.00 57.47  ? 4436 GLN A CB    1 
ATOM   21599 C  CG    . GLN A 1 4436 ? 110.961 121.109 103.044 1.00 66.35  ? 4436 GLN A CG    1 
ATOM   21600 C  CD    . GLN A 1 4436 ? 111.148 120.884 104.531 1.00 70.03  ? 4436 GLN A CD    1 
ATOM   21601 O  OE1   . GLN A 1 4436 ? 110.179 120.825 105.288 1.00 65.15  ? 4436 GLN A OE1   1 
ATOM   21602 N  NE2   . GLN A 1 4436 ? 112.399 120.758 104.958 1.00 69.07  ? 4436 GLN A NE2   1 
ATOM   21603 N  N     . VAL A 1 4437 ? 108.927 119.449 100.038 1.00 60.45  ? 4437 VAL A N     1 
ATOM   21604 C  CA    . VAL A 1 4437 ? 109.297 118.383 99.110  1.00 60.04  ? 4437 VAL A CA    1 
ATOM   21605 C  C     . VAL A 1 4437 ? 109.490 118.946 97.708  1.00 61.86  ? 4437 VAL A C     1 
ATOM   21606 O  O     . VAL A 1 4437 ? 110.475 118.642 97.024  1.00 62.19  ? 4437 VAL A O     1 
ATOM   21607 C  CB    . VAL A 1 4437 ? 108.235 117.267 99.122  1.00 56.16  ? 4437 VAL A CB    1 
ATOM   21608 C  CG1   . VAL A 1 4437 ? 108.330 116.433 97.855  1.00 49.86  ? 4437 VAL A CG1   1 
ATOM   21609 C  CG2   . VAL A 1 4437 ? 108.394 116.388 100.347 1.00 52.22  ? 4437 VAL A CG2   1 
ATOM   21610 N  N     . CYS A 1 4438 ? 108.554 119.787 97.263  1.00 66.99  ? 4438 CYS A N     1 
ATOM   21611 C  CA    . CYS A 1 4438 ? 108.604 120.318 95.906  1.00 67.65  ? 4438 CYS A CA    1 
ATOM   21612 C  C     . CYS A 1 4438 ? 109.751 121.301 95.705  1.00 69.86  ? 4438 CYS A C     1 
ATOM   21613 O  O     . CYS A 1 4438 ? 110.026 121.689 94.565  1.00 74.33  ? 4438 CYS A O     1 
ATOM   21614 C  CB    . CYS A 1 4438 ? 107.274 120.981 95.553  1.00 69.24  ? 4438 CYS A CB    1 
ATOM   21615 S  SG    . CYS A 1 4438 ? 105.864 119.850 95.517  1.00 79.41  ? 4438 CYS A SG    1 
ATOM   21616 N  N     . GLU A 1 4439 ? 110.406 121.730 96.779  1.00 69.49  ? 4439 GLU A N     1 
ATOM   21617 C  CA    . GLU A 1 4439 ? 111.622 122.523 96.675  1.00 67.78  ? 4439 GLU A CA    1 
ATOM   21618 C  C     . GLU A 1 4439 ? 112.884 121.684 96.827  1.00 68.83  ? 4439 GLU A C     1 
ATOM   21619 O  O     . GLU A 1 4439 ? 113.985 122.244 96.844  1.00 72.90  ? 4439 GLU A O     1 
ATOM   21620 C  CB    . GLU A 1 4439 ? 111.615 123.645 97.718  1.00 67.47  ? 4439 GLU A CB    1 
ATOM   21621 C  CG    . GLU A 1 4439 ? 110.818 124.869 97.297  1.00 68.08  ? 4439 GLU A CG    1 
ATOM   21622 C  CD    . GLU A 1 4439 ? 110.744 125.921 98.384  1.00 74.03  ? 4439 GLU A CD    1 
ATOM   21623 O  OE1   . GLU A 1 4439 ? 111.285 125.680 99.484  1.00 79.19  ? 4439 GLU A OE1   1 
ATOM   21624 O  OE2   . GLU A 1 4439 ? 110.147 126.990 98.139  1.00 72.68  ? 4439 GLU A OE2   1 
ATOM   21625 N  N     . GLY A 1 4440 ? 112.750 120.366 96.934  1.00 68.17  ? 4440 GLY A N     1 
ATOM   21626 C  CA    . GLY A 1 4440 ? 113.901 119.491 97.081  1.00 64.16  ? 4440 GLY A CA    1 
ATOM   21627 C  C     . GLY A 1 4440 ? 114.675 119.684 98.367  1.00 71.02  ? 4440 GLY A C     1 
ATOM   21628 O  O     . GLY A 1 4440 ? 115.912 119.658 98.350  1.00 75.86  ? 4440 GLY A O     1 
ATOM   21629 N  N     . LYS A 1 4441 ? 113.976 119.877 99.488  1.00 70.08  ? 4441 LYS A N     1 
ATOM   21630 C  CA    . LYS A 1 4441 ? 114.628 120.082 100.773 1.00 67.78  ? 4441 LYS A CA    1 
ATOM   21631 C  C     . LYS A 1 4441 ? 114.386 118.964 101.775 1.00 67.15  ? 4441 LYS A C     1 
ATOM   21632 O  O     . LYS A 1 4441 ? 115.180 118.818 102.710 1.00 67.45  ? 4441 LYS A O     1 
ATOM   21633 C  CB    . LYS A 1 4441 ? 114.178 121.413 101.394 1.00 70.37  ? 4441 LYS A CB    1 
ATOM   21634 C  CG    . LYS A 1 4441 ? 114.479 122.629 100.533 1.00 70.35  ? 4441 LYS A CG    1 
ATOM   21635 C  CD    . LYS A 1 4441 ? 113.977 123.908 101.182 1.00 70.87  ? 4441 LYS A CD    1 
ATOM   21636 C  CE    . LYS A 1 4441 ? 114.399 125.131 100.385 1.00 78.85  ? 4441 LYS A CE    1 
ATOM   21637 N  NZ    . LYS A 1 4441 ? 113.886 126.393 100.988 1.00 78.56  ? 4441 LYS A NZ    1 
ATOM   21638 N  N     . LYS A 1 4442 ? 113.324 118.178 101.613 1.00 60.56  ? 4442 LYS A N     1 
ATOM   21639 C  CA    . LYS A 1 4442 ? 113.052 117.051 102.493 1.00 61.38  ? 4442 LYS A CA    1 
ATOM   21640 C  C     . LYS A 1 4442 ? 112.687 115.827 101.663 1.00 59.49  ? 4442 LYS A C     1 
ATOM   21641 O  O     . LYS A 1 4442 ? 112.102 115.938 100.583 1.00 56.13  ? 4442 LYS A O     1 
ATOM   21642 C  CB    . LYS A 1 4442 ? 111.936 117.375 103.501 1.00 59.91  ? 4442 LYS A CB    1 
ATOM   21643 C  CG    . LYS A 1 4442 ? 110.557 117.537 102.895 1.00 57.40  ? 4442 LYS A CG    1 
ATOM   21644 C  CD    . LYS A 1 4442 ? 109.479 117.528 103.968 1.00 57.77  ? 4442 LYS A CD    1 
ATOM   21645 C  CE    . LYS A 1 4442 ? 109.539 116.261 104.805 1.00 59.90  ? 4442 LYS A CE    1 
ATOM   21646 N  NZ    . LYS A 1 4442 ? 108.448 116.212 105.817 1.00 52.59  ? 4442 LYS A NZ    1 
ATOM   21647 N  N     . LYS A 1 4443 ? 113.050 114.658 102.184 1.00 60.19  ? 4443 LYS A N     1 
ATOM   21648 C  CA    . LYS A 1 4443 ? 112.887 113.404 101.460 1.00 52.25  ? 4443 LYS A CA    1 
ATOM   21649 C  C     . LYS A 1 4443 ? 111.429 112.958 101.469 1.00 51.86  ? 4443 LYS A C     1 
ATOM   21650 O  O     . LYS A 1 4443 ? 110.703 113.171 102.444 1.00 54.68  ? 4443 LYS A O     1 
ATOM   21651 C  CB    . LYS A 1 4443 ? 113.791 112.332 102.076 1.00 52.68  ? 4443 LYS A CB    1 
ATOM   21652 C  CG    . LYS A 1 4443 ? 113.757 110.963 101.408 1.00 57.77  ? 4443 LYS A CG    1 
ATOM   21653 C  CD    . LYS A 1 4443 ? 112.802 110.014 102.114 1.00 53.60  ? 4443 LYS A CD    1 
ATOM   21654 C  CE    . LYS A 1 4443 ? 113.340 109.605 103.475 1.00 49.98  ? 4443 LYS A CE    1 
ATOM   21655 N  NZ    . LYS A 1 4443 ? 112.426 108.660 104.173 1.00 41.21  ? 4443 LYS A NZ    1 
ATOM   21656 N  N     . GLN A 1 4444 ? 111.004 112.336 100.369 1.00 49.10  ? 4444 GLN A N     1 
ATOM   21657 C  CA    . GLN A 1 4444 ? 109.622 111.892 100.229 1.00 48.09  ? 4444 GLN A CA    1 
ATOM   21658 C  C     . GLN A 1 4444 ? 109.395 110.604 101.011 1.00 43.60  ? 4444 GLN A C     1 
ATOM   21659 O  O     . GLN A 1 4444 ? 109.997 109.569 100.706 1.00 47.86  ? 4444 GLN A O     1 
ATOM   21660 C  CB    . GLN A 1 4444 ? 109.283 111.677 98.756  1.00 51.15  ? 4444 GLN A CB    1 
ATOM   21661 C  CG    . GLN A 1 4444 ? 109.272 112.939 97.917  1.00 63.61  ? 4444 GLN A CG    1 
ATOM   21662 C  CD    . GLN A 1 4444 ? 108.947 112.662 96.462  1.00 71.28  ? 4444 GLN A CD    1 
ATOM   21663 O  OE1   . GLN A 1 4444 ? 108.792 111.510 96.057  1.00 64.80  ? 4444 GLN A OE1   1 
ATOM   21664 N  NE2   . GLN A 1 4444 ? 108.843 113.721 95.667  1.00 71.01  ? 4444 GLN A NE2   1 
ATOM   21665 N  N     . THR A 1 4445 ? 108.517 110.662 102.009 1.00 38.93  ? 4445 THR A N     1 
ATOM   21666 C  CA    . THR A 1 4445 ? 108.132 109.482 102.763 1.00 31.51  ? 4445 THR A CA    1 
ATOM   21667 C  C     . THR A 1 4445 ? 106.967 108.778 102.066 1.00 30.05  ? 4445 THR A C     1 
ATOM   21668 O  O     . THR A 1 4445 ? 106.444 109.244 101.051 1.00 32.83  ? 4445 THR A O     1 
ATOM   21669 C  CB    . THR A 1 4445 ? 107.769 109.858 104.198 1.00 27.97  ? 4445 THR A CB    1 
ATOM   21670 O  OG1   . THR A 1 4445 ? 106.452 110.422 104.229 1.00 30.09  ? 4445 THR A OG1   1 
ATOM   21671 C  CG2   . THR A 1 4445 ? 108.761 110.870 104.750 1.00 31.75  ? 4445 THR A CG2   1 
ATOM   21672 N  N     . ASN A 1 4446 ? 106.560 107.631 102.614 1.00 27.48  ? 4446 ASN A N     1 
ATOM   21673 C  CA    . ASN A 1 4446 ? 105.436 106.895 102.043 1.00 27.51  ? 4446 ASN A CA    1 
ATOM   21674 C  C     . ASN A 1 4446 ? 104.146 107.700 102.141 1.00 28.92  ? 4446 ASN A C     1 
ATOM   21675 O  O     . ASN A 1 4446 ? 103.386 107.804 101.169 1.00 30.22  ? 4446 ASN A O     1 
ATOM   21676 C  CB    . ASN A 1 4446 ? 105.281 105.548 102.749 1.00 22.12  ? 4446 ASN A CB    1 
ATOM   21677 C  CG    . ASN A 1 4446 ? 106.325 104.543 102.318 1.00 26.47  ? 4446 ASN A CG    1 
ATOM   21678 O  OD1   . ASN A 1 4446 ? 106.805 104.581 101.187 1.00 31.65  ? 4446 ASN A OD1   1 
ATOM   21679 N  ND2   . ASN A 1 4446 ? 106.684 103.637 103.220 1.00 17.31  ? 4446 ASN A ND2   1 
ATOM   21680 N  N     . TYR A 1 4447 ? 103.884 108.280 103.314 1.00 28.16  ? 4447 TYR A N     1 
ATOM   21681 C  CA    . TYR A 1 4447 ? 102.681 109.084 103.488 1.00 32.67  ? 4447 TYR A CA    1 
ATOM   21682 C  C     . TYR A 1 4447 ? 102.730 110.331 102.614 1.00 36.69  ? 4447 TYR A C     1 
ATOM   21683 O  O     . TYR A 1 4447 ? 101.718 110.718 102.015 1.00 37.38  ? 4447 TYR A O     1 
ATOM   21684 C  CB    . TYR A 1 4447 ? 102.509 109.447 104.964 1.00 36.50  ? 4447 TYR A CB    1 
ATOM   21685 C  CG    . TYR A 1 4447 ? 101.536 110.572 105.230 1.00 40.79  ? 4447 TYR A CG    1 
ATOM   21686 C  CD1   . TYR A 1 4447 ? 101.958 111.895 105.266 1.00 41.95  ? 4447 TYR A CD1   1 
ATOM   21687 C  CD2   . TYR A 1 4447 ? 100.190 110.307 105.441 1.00 45.89  ? 4447 TYR A CD2   1 
ATOM   21688 C  CE1   . TYR A 1 4447 ? 101.067 112.918 105.506 1.00 44.72  ? 4447 TYR A CE1   1 
ATOM   21689 C  CE2   . TYR A 1 4447 ? 99.292  111.324 105.682 1.00 51.74  ? 4447 TYR A CE2   1 
ATOM   21690 C  CZ    . TYR A 1 4447 ? 99.734  112.627 105.714 1.00 51.79  ? 4447 TYR A CZ    1 
ATOM   21691 O  OH    . TYR A 1 4447 ? 98.836  113.639 105.955 1.00 58.85  ? 4447 TYR A OH    1 
ATOM   21692 N  N     . LEU A 1 4448 ? 103.898 110.972 102.530 1.00 36.10  ? 4448 LEU A N     1 
ATOM   21693 C  CA    . LEU A 1 4448 ? 104.054 112.103 101.623 1.00 34.97  ? 4448 LEU A CA    1 
ATOM   21694 C  C     . LEU A 1 4448 ? 103.862 111.674 100.176 1.00 35.24  ? 4448 LEU A C     1 
ATOM   21695 O  O     . LEU A 1 4448 ? 103.279 112.413 99.378  1.00 40.81  ? 4448 LEU A O     1 
ATOM   21696 C  CB    . LEU A 1 4448 ? 105.423 112.755 101.811 1.00 33.88  ? 4448 LEU A CB    1 
ATOM   21697 C  CG    . LEU A 1 4448 ? 105.667 113.454 103.148 1.00 43.51  ? 4448 LEU A CG    1 
ATOM   21698 C  CD1   . LEU A 1 4448 ? 107.105 113.935 103.245 1.00 44.27  ? 4448 LEU A CD1   1 
ATOM   21699 C  CD2   . LEU A 1 4448 ? 104.698 114.613 103.324 1.00 39.38  ? 4448 LEU A CD2   1 
ATOM   21700 N  N     . ARG A 1 4449 ? 104.347 110.483 99.817  1.00 34.31  ? 4449 ARG A N     1 
ATOM   21701 C  CA    . ARG A 1 4449 ? 104.146 109.982 98.461  1.00 33.97  ? 4449 ARG A CA    1 
ATOM   21702 C  C     . ARG A 1 4449 ? 102.662 109.822 98.152  1.00 34.01  ? 4449 ARG A C     1 
ATOM   21703 O  O     . ARG A 1 4449 ? 102.188 110.235 97.087  1.00 35.54  ? 4449 ARG A O     1 
ATOM   21704 C  CB    . ARG A 1 4449 ? 104.881 108.653 98.283  1.00 33.81  ? 4449 ARG A CB    1 
ATOM   21705 C  CG    . ARG A 1 4449 ? 106.252 108.777 97.641  1.00 35.58  ? 4449 ARG A CG    1 
ATOM   21706 C  CD    . ARG A 1 4449 ? 106.796 107.412 97.232  1.00 34.07  ? 4449 ARG A CD    1 
ATOM   21707 N  NE    . ARG A 1 4449 ? 107.371 106.667 98.349  1.00 33.51  ? 4449 ARG A NE    1 
ATOM   21708 C  CZ    . ARG A 1 4449 ? 108.409 107.061 99.077  1.00 36.66  ? 4449 ARG A CZ    1 
ATOM   21709 N  NH1   . ARG A 1 4449 ? 109.064 108.178 98.806  1.00 42.14  ? 4449 ARG A NH1   1 
ATOM   21710 N  NH2   . ARG A 1 4449 ? 108.809 106.305 100.095 1.00 26.55  ? 4449 ARG A NH2   1 
ATOM   21711 N  N     . THR A 1 4450 ? 101.910 109.237 99.087  1.00 33.75  ? 4450 THR A N     1 
ATOM   21712 C  CA    . THR A 1 4450 ? 100.474 109.062 98.887  1.00 38.17  ? 4450 THR A CA    1 
ATOM   21713 C  C     . THR A 1 4450 ? 99.764  110.408 98.780  1.00 43.18  ? 4450 THR A C     1 
ATOM   21714 O  O     . THR A 1 4450 ? 98.900  110.605 97.915  1.00 41.46  ? 4450 THR A O     1 
ATOM   21715 C  CB    . THR A 1 4450 ? 99.887  108.231 100.031 1.00 33.25  ? 4450 THR A CB    1 
ATOM   21716 O  OG1   . THR A 1 4450 ? 100.336 106.875 99.919  1.00 42.31  ? 4450 THR A OG1   1 
ATOM   21717 C  CG2   . THR A 1 4450 ? 98.366  108.258 99.994  1.00 37.86  ? 4450 THR A CG2   1 
ATOM   21718 N  N     . LEU A 1 4451 ? 100.120 111.351 99.656  1.00 39.21  ? 4451 LEU A N     1 
ATOM   21719 C  CA    . LEU A 1 4451 ? 99.474  112.659 99.641  1.00 38.29  ? 4451 LEU A CA    1 
ATOM   21720 C  C     . LEU A 1 4451 ? 99.778  113.413 98.350  1.00 44.71  ? 4451 LEU A C     1 
ATOM   21721 O  O     . LEU A 1 4451 ? 98.890  114.052 97.772  1.00 48.54  ? 4451 LEU A O     1 
ATOM   21722 C  CB    . LEU A 1 4451 ? 99.911  113.465 100.864 1.00 37.31  ? 4451 LEU A CB    1 
ATOM   21723 C  CG    . LEU A 1 4451 ? 99.464  114.922 100.968 1.00 39.93  ? 4451 LEU A CG    1 
ATOM   21724 C  CD1   . LEU A 1 4451 ? 97.976  114.999 101.237 1.00 46.58  ? 4451 LEU A CD1   1 
ATOM   21725 C  CD2   . LEU A 1 4451 ? 100.231 115.617 102.076 1.00 47.80  ? 4451 LEU A CD2   1 
ATOM   21726 N  N     . ILE A 1 4452 ? 101.025 113.345 97.880  1.00 41.38  ? 4452 ILE A N     1 
ATOM   21727 C  CA    . ILE A 1 4452 ? 101.389 113.985 96.620  1.00 42.25  ? 4452 ILE A CA    1 
ATOM   21728 C  C     . ILE A 1 4452 ? 100.655 113.338 95.455  1.00 41.00  ? 4452 ILE A C     1 
ATOM   21729 O  O     . ILE A 1 4452 ? 100.197 114.028 94.538  1.00 46.96  ? 4452 ILE A O     1 
ATOM   21730 C  CB    . ILE A 1 4452 ? 102.916 113.952 96.424  1.00 43.23  ? 4452 ILE A CB    1 
ATOM   21731 C  CG1   . ILE A 1 4452 ? 103.609 114.817 97.478  1.00 43.82  ? 4452 ILE A CG1   1 
ATOM   21732 C  CG2   . ILE A 1 4452 ? 103.292 114.395 95.022  1.00 46.27  ? 4452 ILE A CG2   1 
ATOM   21733 C  CD1   . ILE A 1 4452 ? 105.115 114.786 97.393  1.00 48.76  ? 4452 ILE A CD1   1 
ATOM   21734 N  N     . ASN A 1 4453 ? 100.537 112.008 95.462  1.00 43.91  ? 4453 ASN A N     1 
ATOM   21735 C  CA    . ASN A 1 4453 ? 99.769  111.333 94.419  1.00 47.22  ? 4453 ASN A CA    1 
ATOM   21736 C  C     . ASN A 1 4453 ? 98.330  111.836 94.397  1.00 50.56  ? 4453 ASN A C     1 
ATOM   21737 O  O     . ASN A 1 4453 ? 97.797  112.191 93.337  1.00 52.72  ? 4453 ASN A O     1 
ATOM   21738 C  CB    . ASN A 1 4453 ? 99.816  109.819 94.642  1.00 49.47  ? 4453 ASN A CB    1 
ATOM   21739 C  CG    . ASN A 1 4453 ? 99.219  109.034 93.488  1.00 61.17  ? 4453 ASN A CG    1 
ATOM   21740 O  OD1   . ASN A 1 4453 ? 98.735  109.606 92.512  1.00 64.92  ? 4453 ASN A OD1   1 
ATOM   21741 N  ND2   . ASN A 1 4453 ? 99.250  107.711 93.598  1.00 67.78  ? 4453 ASN A ND2   1 
ATOM   21742 N  N     . GLU A 1 4454 ? 97.696  111.899 95.571  1.00 49.64  ? 4454 GLU A N     1 
ATOM   21743 C  CA    . GLU A 1 4454 ? 96.315  112.366 95.644  1.00 48.98  ? 4454 GLU A CA    1 
ATOM   21744 C  C     . GLU A 1 4454 ? 96.187  113.804 95.156  1.00 46.32  ? 4454 GLU A C     1 
ATOM   21745 O  O     . GLU A 1 4454 ? 95.239  114.142 94.438  1.00 50.60  ? 4454 GLU A O     1 
ATOM   21746 C  CB    . GLU A 1 4454 ? 95.789  112.237 97.073  1.00 48.60  ? 4454 GLU A CB    1 
ATOM   21747 C  CG    . GLU A 1 4454 ? 95.346  110.834 97.448  1.00 50.13  ? 4454 GLU A CG    1 
ATOM   21748 C  CD    . GLU A 1 4454 ? 95.278  110.625 98.947  1.00 61.34  ? 4454 GLU A CD    1 
ATOM   21749 O  OE1   . GLU A 1 4454 ? 95.994  111.338 99.681  1.00 57.19  ? 4454 GLU A OE1   1 
ATOM   21750 O  OE2   . GLU A 1 4454 ? 94.509  109.748 99.392  1.00 66.38  ? 4454 GLU A OE2   1 
ATOM   21751 N  N     . LEU A 1 4455 ? 97.131  114.667 95.539  1.00 41.62  ? 4455 LEU A N     1 
ATOM   21752 C  CA    . LEU A 1 4455 ? 97.076  116.061 95.106  1.00 47.47  ? 4455 LEU A CA    1 
ATOM   21753 C  C     . LEU A 1 4455 ? 97.261  116.186 93.598  1.00 54.15  ? 4455 LEU A C     1 
ATOM   21754 O  O     . LEU A 1 4455 ? 96.591  117.000 92.951  1.00 57.89  ? 4455 LEU A O     1 
ATOM   21755 C  CB    . LEU A 1 4455 ? 98.129  116.883 95.849  1.00 48.42  ? 4455 LEU A CB    1 
ATOM   21756 C  CG    . LEU A 1 4455 ? 97.870  117.110 97.340  1.00 50.07  ? 4455 LEU A CG    1 
ATOM   21757 C  CD1   . LEU A 1 4455 ? 98.922  118.032 97.937  1.00 50.53  ? 4455 LEU A CD1   1 
ATOM   21758 C  CD2   . LEU A 1 4455 ? 96.471  117.662 97.567  1.00 50.06  ? 4455 LEU A CD2   1 
ATOM   21759 N  N     . VAL A 1 4456 ? 98.170  115.397 93.020  1.00 54.20  ? 4456 VAL A N     1 
ATOM   21760 C  CA    . VAL A 1 4456 ? 98.397  115.457 91.578  1.00 52.62  ? 4456 VAL A CA    1 
ATOM   21761 C  C     . VAL A 1 4456 ? 97.163  114.989 90.819  1.00 58.17  ? 4456 VAL A C     1 
ATOM   21762 O  O     . VAL A 1 4456 ? 96.753  115.613 89.833  1.00 62.48  ? 4456 VAL A O     1 
ATOM   21763 C  CB    . VAL A 1 4456 ? 99.647  114.645 91.192  1.00 51.99  ? 4456 VAL A CB    1 
ATOM   21764 C  CG1   . VAL A 1 4456 ? 99.777  114.563 89.680  1.00 54.46  ? 4456 VAL A CG1   1 
ATOM   21765 C  CG2   . VAL A 1 4456 ? 100.892 115.287 91.779  1.00 51.84  ? 4456 VAL A CG2   1 
ATOM   21766 N  N     . LYS A 1 4457 ? 96.541  113.894 91.262  1.00 58.25  ? 4457 LYS A N     1 
ATOM   21767 C  CA    . LYS A 1 4457 ? 95.302  113.467 90.622  1.00 59.23  ? 4457 LYS A CA    1 
ATOM   21768 C  C     . LYS A 1 4457 ? 94.105  114.328 91.006  1.00 58.80  ? 4457 LYS A C     1 
ATOM   21769 O  O     . LYS A 1 4457 ? 93.012  114.111 90.472  1.00 57.64  ? 4457 LYS A O     1 
ATOM   21770 C  CB    . LYS A 1 4457 ? 95.005  111.997 90.934  1.00 59.43  ? 4457 LYS A CB    1 
ATOM   21771 C  CG    . LYS A 1 4457 ? 96.228  111.099 90.939  1.00 62.57  ? 4457 LYS A CG    1 
ATOM   21772 C  CD    . LYS A 1 4457 ? 96.718  110.843 89.522  1.00 76.98  ? 4457 LYS A CD    1 
ATOM   21773 C  CE    . LYS A 1 4457 ? 97.612  109.616 89.453  1.00 75.05  ? 4457 LYS A CE    1 
ATOM   21774 N  NZ    . LYS A 1 4457 ? 98.897  109.822 90.176  1.00 67.72  ? 4457 LYS A NZ    1 
ATOM   21775 N  N     . GLY A 1 4458 ? 94.279  115.290 91.910  1.00 55.94  ? 4458 GLY A N     1 
ATOM   21776 C  CA    . GLY A 1 4458 ? 93.202  116.185 92.279  1.00 53.06  ? 4458 GLY A CA    1 
ATOM   21777 C  C     . GLY A 1 4458 ? 92.163  115.595 93.200  1.00 53.33  ? 4458 GLY A C     1 
ATOM   21778 O  O     . GLY A 1 4458 ? 91.076  116.170 93.331  1.00 56.21  ? 4458 GLY A O     1 
ATOM   21779 N  N     . ILE A 1 4459 ? 92.455  114.473 93.839  1.00 51.86  ? 4459 ILE A N     1 
ATOM   21780 C  CA    . ILE A 1 4459 ? 91.521  113.817 94.745  1.00 54.89  ? 4459 ILE A CA    1 
ATOM   21781 C  C     . ILE A 1 4459 ? 91.721  114.375 96.145  1.00 57.41  ? 4459 ILE A C     1 
ATOM   21782 O  O     . ILE A 1 4459 ? 92.855  114.602 96.583  1.00 54.32  ? 4459 ILE A O     1 
ATOM   21783 C  CB    . ILE A 1 4459 ? 91.718  112.289 94.715  1.00 53.25  ? 4459 ILE A CB    1 
ATOM   21784 C  CG1   . ILE A 1 4459 ? 91.532  111.757 93.293  1.00 51.99  ? 4459 ILE A CG1   1 
ATOM   21785 C  CG2   . ILE A 1 4459 ? 90.751  111.601 95.666  1.00 51.31  ? 4459 ILE A CG2   1 
ATOM   21786 C  CD1   . ILE A 1 4459 ? 91.791  110.274 93.158  1.00 52.64  ? 4459 ILE A CD1   1 
ATOM   21787 N  N     . LEU A 1 4460 ? 90.618  114.612 96.845  1.00 55.92  ? 4460 LEU A N     1 
ATOM   21788 C  CA    . LEU A 1 4460 ? 90.698  115.076 98.221  1.00 50.53  ? 4460 LEU A CA    1 
ATOM   21789 C  C     . LEU A 1 4460 ? 91.354  114.003 99.085  1.00 52.76  ? 4460 LEU A C     1 
ATOM   21790 O  O     . LEU A 1 4460 ? 90.898  112.851 99.085  1.00 51.92  ? 4460 LEU A O     1 
ATOM   21791 C  CB    . LEU A 1 4460 ? 89.305  115.408 98.755  1.00 50.43  ? 4460 LEU A CB    1 
ATOM   21792 C  CG    . LEU A 1 4460 ? 89.175  115.624 100.265 1.00 45.93  ? 4460 LEU A CG    1 
ATOM   21793 C  CD1   . LEU A 1 4460 ? 89.938  116.862 100.700 1.00 45.22  ? 4460 LEU A CD1   1 
ATOM   21794 C  CD2   . LEU A 1 4460 ? 87.713  115.723 100.670 1.00 44.11  ? 4460 LEU A CD2   1 
ATOM   21795 N  N     . PRO A 1 4461 ? 92.423  114.328 99.812  1.00 54.76  ? 4461 PRO A N     1 
ATOM   21796 C  CA    . PRO A 1 4461 ? 93.078  113.318 100.652 1.00 49.43  ? 4461 PRO A CA    1 
ATOM   21797 C  C     . PRO A 1 4461 ? 92.131  112.766 101.706 1.00 53.30  ? 4461 PRO A C     1 
ATOM   21798 O  O     . PRO A 1 4461 ? 91.298  113.487 102.261 1.00 56.32  ? 4461 PRO A O     1 
ATOM   21799 C  CB    . PRO A 1 4461 ? 94.240  114.089 101.286 1.00 45.49  ? 4461 PRO A CB    1 
ATOM   21800 C  CG    . PRO A 1 4461 ? 94.512  115.200 100.325 1.00 43.36  ? 4461 PRO A CG    1 
ATOM   21801 C  CD    . PRO A 1 4461 ? 93.169  115.597 99.793  1.00 48.43  ? 4461 PRO A CD    1 
ATOM   21802 N  N     . ARG A 1 4462 ? 92.265  111.465 101.976 1.00 55.53  ? 4462 ARG A N     1 
ATOM   21803 C  CA    . ARG A 1 4462 ? 91.406  110.820 102.963 1.00 57.60  ? 4462 ARG A CA    1 
ATOM   21804 C  C     . ARG A 1 4462 ? 91.675  111.343 104.368 1.00 57.39  ? 4462 ARG A C     1 
ATOM   21805 O  O     . ARG A 1 4462 ? 90.740  111.481 105.166 1.00 58.69  ? 4462 ARG A O     1 
ATOM   21806 C  CB    . ARG A 1 4462 ? 91.594  109.304 102.908 1.00 58.84  ? 4462 ARG A CB    1 
ATOM   21807 C  CG    . ARG A 1 4462 ? 90.766  108.535 103.924 1.00 65.10  ? 4462 ARG A CG    1 
ATOM   21808 C  CD    . ARG A 1 4462 ? 89.280  108.694 103.646 1.00 72.33  ? 4462 ARG A CD    1 
ATOM   21809 N  NE    . ARG A 1 4462 ? 88.892  108.094 102.375 1.00 81.36  ? 4462 ARG A NE    1 
ATOM   21810 C  CZ    . ARG A 1 4462 ? 87.722  108.287 101.782 1.00 83.25  ? 4462 ARG A CZ    1 
ATOM   21811 N  NH1   . ARG A 1 4462 ? 86.795  109.064 102.319 1.00 76.93  ? 4462 ARG A NH1   1 
ATOM   21812 N  NH2   . ARG A 1 4462 ? 87.476  107.688 100.621 1.00 79.69  ? 4462 ARG A NH2   1 
ATOM   21813 N  N     . SER A 1 4463 ? 92.938  111.636 104.690 1.00 56.24  ? 4463 SER A N     1 
ATOM   21814 C  CA    . SER A 1 4463 ? 93.256  112.209 105.993 1.00 52.67  ? 4463 SER A CA    1 
ATOM   21815 C  C     . SER A 1 4463 ? 92.620  113.583 106.162 1.00 58.46  ? 4463 SER A C     1 
ATOM   21816 O  O     . SER A 1 4463 ? 92.168  113.935 107.258 1.00 56.72  ? 4463 SER A O     1 
ATOM   21817 C  CB    . SER A 1 4463 ? 94.772  112.294 106.172 1.00 47.96  ? 4463 SER A CB    1 
ATOM   21818 O  OG    . SER A 1 4463 ? 95.388  111.047 105.905 1.00 53.18  ? 4463 SER A OG    1 
ATOM   21819 N  N     . TRP A 1 4464 ? 92.580  114.374 105.087 1.00 54.11  ? 4464 TRP A N     1 
ATOM   21820 C  CA    . TRP A 1 4464 ? 91.997  115.709 105.162 1.00 45.59  ? 4464 TRP A CA    1 
ATOM   21821 C  C     . TRP A 1 4464 ? 90.492  115.658 105.394 1.00 47.85  ? 4464 TRP A C     1 
ATOM   21822 O  O     . TRP A 1 4464 ? 89.947  116.517 106.096 1.00 51.02  ? 4464 TRP A O     1 
ATOM   21823 C  CB    . TRP A 1 4464 ? 92.308  116.486 103.883 1.00 44.01  ? 4464 TRP A CB    1 
ATOM   21824 C  CG    . TRP A 1 4464 ? 93.726  116.962 103.798 1.00 43.61  ? 4464 TRP A CG    1 
ATOM   21825 C  CD1   . TRP A 1 4464 ? 94.769  116.575 104.588 1.00 40.66  ? 4464 TRP A CD1   1 
ATOM   21826 C  CD2   . TRP A 1 4464 ? 94.261  117.902 102.860 1.00 38.52  ? 4464 TRP A CD2   1 
ATOM   21827 N  NE1   . TRP A 1 4464 ? 95.918  117.223 104.206 1.00 40.36  ? 4464 TRP A NE1   1 
ATOM   21828 C  CE2   . TRP A 1 4464 ? 95.633  118.043 103.146 1.00 38.98  ? 4464 TRP A CE2   1 
ATOM   21829 C  CE3   . TRP A 1 4464 ? 93.712  118.641 101.807 1.00 37.49  ? 4464 TRP A CE3   1 
ATOM   21830 C  CZ2   . TRP A 1 4464 ? 96.463  118.893 102.419 1.00 40.19  ? 4464 TRP A CZ2   1 
ATOM   21831 C  CZ3   . TRP A 1 4464 ? 94.538  119.484 101.087 1.00 36.55  ? 4464 TRP A CZ3   1 
ATOM   21832 C  CH2   . TRP A 1 4464 ? 95.898  119.603 101.396 1.00 40.10  ? 4464 TRP A CH2   1 
ATOM   21833 N  N     . SER A 1 4465 ? 89.809  114.672 104.820 1.00 51.73  ? 4465 SER A N     1 
ATOM   21834 C  CA    . SER A 1 4465 ? 88.355  114.575 104.919 1.00 53.82  ? 4465 SER A CA    1 
ATOM   21835 C  C     . SER A 1 4465 ? 87.975  114.104 106.317 1.00 54.55  ? 4465 SER A C     1 
ATOM   21836 O  O     . SER A 1 4465 ? 87.974  112.906 106.606 1.00 56.70  ? 4465 SER A O     1 
ATOM   21837 C  CB    . SER A 1 4465 ? 87.813  113.627 103.855 1.00 53.88  ? 4465 SER A CB    1 
ATOM   21838 O  OG    . SER A 1 4465 ? 88.388  112.339 103.980 1.00 61.04  ? 4465 SER A OG    1 
ATOM   21839 N  N     . HIS A 1 4466 ? 87.647  115.054 107.195 1.00 52.93  ? 4466 HIS A N     1 
ATOM   21840 C  CA    . HIS A 1 4466 ? 87.188  114.744 108.540 1.00 53.96  ? 4466 HIS A CA    1 
ATOM   21841 C  C     . HIS A 1 4466 ? 85.747  115.148 108.806 1.00 53.59  ? 4466 HIS A C     1 
ATOM   21842 O  O     . HIS A 1 4466 ? 85.126  114.581 109.712 1.00 53.93  ? 4466 HIS A O     1 
ATOM   21843 C  CB    . HIS A 1 4466 ? 88.090  115.416 109.588 1.00 56.53  ? 4466 HIS A CB    1 
ATOM   21844 C  CG    . HIS A 1 4466 ? 89.420  114.751 109.753 1.00 60.23  ? 4466 HIS A CG    1 
ATOM   21845 N  ND1   . HIS A 1 4466 ? 90.518  115.399 110.275 1.00 65.49  ? 4466 HIS A ND1   1 
ATOM   21846 C  CD2   . HIS A 1 4466 ? 89.829  113.493 109.463 1.00 59.49  ? 4466 HIS A CD2   1 
ATOM   21847 C  CE1   . HIS A 1 4466 ? 91.546  114.570 110.300 1.00 68.95  ? 4466 HIS A CE1   1 
ATOM   21848 N  NE2   . HIS A 1 4466 ? 91.155  113.407 109.813 1.00 63.27  ? 4466 HIS A NE2   1 
ATOM   21849 N  N     . TYR A 1 4467 ? 85.200  116.099 108.055 1.00 53.20  ? 4467 TYR A N     1 
ATOM   21850 C  CA    . TYR A 1 4467 ? 83.800  116.475 108.157 1.00 50.08  ? 4467 TYR A CA    1 
ATOM   21851 C  C     . TYR A 1 4467 ? 83.063  116.005 106.911 1.00 49.87  ? 4467 TYR A C     1 
ATOM   21852 O  O     . TYR A 1 4467 ? 83.624  115.980 105.811 1.00 51.51  ? 4467 TYR A O     1 
ATOM   21853 C  CB    . TYR A 1 4467 ? 83.635  117.991 108.338 1.00 44.33  ? 4467 TYR A CB    1 
ATOM   21854 C  CG    . TYR A 1 4467 ? 84.326  118.835 107.289 1.00 43.58  ? 4467 TYR A CG    1 
ATOM   21855 C  CD1   . TYR A 1 4467 ? 83.676  119.187 106.113 1.00 42.71  ? 4467 TYR A CD1   1 
ATOM   21856 C  CD2   . TYR A 1 4467 ? 85.627  119.281 107.475 1.00 39.65  ? 4467 TYR A CD2   1 
ATOM   21857 C  CE1   . TYR A 1 4467 ? 84.303  119.961 105.155 1.00 39.73  ? 4467 TYR A CE1   1 
ATOM   21858 C  CE2   . TYR A 1 4467 ? 86.262  120.055 106.522 1.00 37.39  ? 4467 TYR A CE2   1 
ATOM   21859 C  CZ    . TYR A 1 4467 ? 85.595  120.390 105.364 1.00 39.34  ? 4467 TYR A CZ    1 
ATOM   21860 O  OH    . TYR A 1 4467 ? 86.222  121.159 104.410 1.00 41.26  ? 4467 TYR A OH    1 
ATOM   21861 N  N     . THR A 1 4468 ? 81.801  115.624 107.096 1.00 50.50  ? 4468 THR A N     1 
ATOM   21862 C  CA    . THR A 1 4468 ? 81.036  115.030 106.008 1.00 48.71  ? 4468 THR A CA    1 
ATOM   21863 C  C     . THR A 1 4468 ? 80.836  116.025 104.869 1.00 49.51  ? 4468 THR A C     1 
ATOM   21864 O  O     . THR A 1 4468 ? 80.578  117.212 105.085 1.00 46.80  ? 4468 THR A O     1 
ATOM   21865 C  CB    . THR A 1 4468 ? 79.691  114.510 106.529 1.00 50.72  ? 4468 THR A CB    1 
ATOM   21866 O  OG1   . THR A 1 4468 ? 79.017  113.784 105.492 1.00 64.47  ? 4468 THR A OG1   1 
ATOM   21867 C  CG2   . THR A 1 4468 ? 78.811  115.641 107.035 1.00 47.57  ? 4468 THR A CG2   1 
ATOM   21868 N  N     . VAL A 1 4469 ? 80.991  115.528 103.643 1.00 50.59  ? 4469 VAL A N     1 
ATOM   21869 C  CA    . VAL A 1 4469 ? 80.924  116.361 102.441 1.00 51.45  ? 4469 VAL A CA    1 
ATOM   21870 C  C     . VAL A 1 4469 ? 80.125  115.634 101.377 1.00 54.01  ? 4469 VAL A C     1 
ATOM   21871 O  O     . VAL A 1 4469 ? 80.012  114.401 101.387 1.00 54.68  ? 4469 VAL A O     1 
ATOM   21872 C  CB    . VAL A 1 4469 ? 82.333  116.691 101.897 1.00 49.18  ? 4469 VAL A CB    1 
ATOM   21873 C  CG1   . VAL A 1 4469 ? 83.067  117.626 102.841 1.00 49.75  ? 4469 VAL A CG1   1 
ATOM   21874 C  CG2   . VAL A 1 4469 ? 83.129  115.415 101.678 1.00 52.46  ? 4469 VAL A CG2   1 
ATOM   21875 N  N     . PRO A 1 4470 ? 79.539  116.383 100.440 1.00 53.23  ? 4470 PRO A N     1 
ATOM   21876 C  CA    . PRO A 1 4470 ? 78.847  115.730 99.324  1.00 50.26  ? 4470 PRO A CA    1 
ATOM   21877 C  C     . PRO A 1 4470 ? 79.815  114.921 98.473  1.00 54.60  ? 4470 PRO A C     1 
ATOM   21878 O  O     . PRO A 1 4470 ? 80.979  115.288 98.302  1.00 56.49  ? 4470 PRO A O     1 
ATOM   21879 C  CB    . PRO A 1 4470 ? 78.239  116.903 98.548  1.00 40.56  ? 4470 PRO A CB    1 
ATOM   21880 C  CG    . PRO A 1 4470 ? 79.126  118.050 98.852  1.00 41.21  ? 4470 PRO A CG    1 
ATOM   21881 C  CD    . PRO A 1 4470 ? 79.579  117.849 100.275 1.00 48.00  ? 4470 PRO A CD    1 
ATOM   21882 N  N     . ALA A 1 4471 ? 79.317  113.806 97.942  1.00 59.64  ? 4471 ALA A N     1 
ATOM   21883 C  CA    . ALA A 1 4471 ? 80.161  112.870 97.212  1.00 58.22  ? 4471 ALA A CA    1 
ATOM   21884 C  C     . ALA A 1 4471 ? 80.693  113.498 95.928  1.00 57.89  ? 4471 ALA A C     1 
ATOM   21885 O  O     . ALA A 1 4471 ? 80.055  114.359 95.316  1.00 61.06  ? 4471 ALA A O     1 
ATOM   21886 C  CB    . ALA A 1 4471 ? 79.383  111.593 96.891  1.00 55.09  ? 4471 ALA A CB    1 
ATOM   21887 N  N     . GLY A 1 4472 ? 81.882  113.056 95.526  1.00 53.54  ? 4472 GLY A N     1 
ATOM   21888 C  CA    . GLY A 1 4472 ? 82.517  113.591 94.339  1.00 59.42  ? 4472 GLY A CA    1 
ATOM   21889 C  C     . GLY A 1 4472 ? 82.980  115.023 94.462  1.00 61.75  ? 4472 GLY A C     1 
ATOM   21890 O  O     . GLY A 1 4472 ? 82.862  115.789 93.500  1.00 55.18  ? 4472 GLY A O     1 
ATOM   21891 N  N     . MET A 1 4473 ? 83.500  115.413 95.623  1.00 60.96  ? 4473 MET A N     1 
ATOM   21892 C  CA    . MET A 1 4473 ? 83.951  116.779 95.854  1.00 59.95  ? 4473 MET A CA    1 
ATOM   21893 C  C     . MET A 1 4473 ? 85.469  116.845 95.737  1.00 56.85  ? 4473 MET A C     1 
ATOM   21894 O  O     . MET A 1 4473 ? 86.185  116.176 96.488  1.00 59.38  ? 4473 MET A O     1 
ATOM   21895 C  CB    . MET A 1 4473 ? 83.490  117.261 97.230  1.00 55.71  ? 4473 MET A CB    1 
ATOM   21896 C  CG    . MET A 1 4473 ? 83.991  118.635 97.635  1.00 54.49  ? 4473 MET A CG    1 
ATOM   21897 S  SD    . MET A 1 4473 ? 83.538  119.020 99.336  1.00 71.35  ? 4473 MET A SD    1 
ATOM   21898 C  CE    . MET A 1 4473 ? 83.921  120.765 99.406  1.00 52.53  ? 4473 MET A CE    1 
ATOM   21899 N  N     . THR A 1 4474 ? 85.954  117.655 94.800  1.00 52.62  ? 4474 THR A N     1 
ATOM   21900 C  CA    . THR A 1 4474 ? 87.377  117.748 94.514  1.00 57.31  ? 4474 THR A CA    1 
ATOM   21901 C  C     . THR A 1 4474 ? 88.090  118.600 95.565  1.00 55.58  ? 4474 THR A C     1 
ATOM   21902 O  O     . THR A 1 4474 ? 87.468  119.259 96.400  1.00 56.70  ? 4474 THR A O     1 
ATOM   21903 C  CB    . THR A 1 4474 ? 87.606  118.315 93.112  1.00 59.25  ? 4474 THR A CB    1 
ATOM   21904 O  OG1   . THR A 1 4474 ? 89.002  118.257 92.790  1.00 66.04  ? 4474 THR A OG1   1 
ATOM   21905 C  CG2   . THR A 1 4474 ? 87.126  119.751 93.031  1.00 50.13  ? 4474 THR A CG2   1 
ATOM   21906 N  N     . VAL A 1 4475 ? 89.424  118.574 95.513  1.00 53.47  ? 4475 VAL A N     1 
ATOM   21907 C  CA    . VAL A 1 4475 ? 90.220  119.198 96.566  1.00 51.03  ? 4475 VAL A CA    1 
ATOM   21908 C  C     . VAL A 1 4475 ? 90.308  120.709 96.366  1.00 46.98  ? 4475 VAL A C     1 
ATOM   21909 O  O     . VAL A 1 4475 ? 90.446  121.466 97.335  1.00 48.50  ? 4475 VAL A O     1 
ATOM   21910 C  CB    . VAL A 1 4475 ? 91.614  118.543 96.638  1.00 53.35  ? 4475 VAL A CB    1 
ATOM   21911 C  CG1   . VAL A 1 4475 ? 92.469  118.942 95.442  1.00 52.74  ? 4475 VAL A CG1   1 
ATOM   21912 C  CG2   . VAL A 1 4475 ? 92.308  118.900 97.946  1.00 47.86  ? 4475 VAL A CG2   1 
ATOM   21913 N  N     . ILE A 1 4476 ? 90.222  121.175 95.117  1.00 46.58  ? 4476 ILE A N     1 
ATOM   21914 C  CA    . ILE A 1 4476 ? 90.380  122.604 94.855  1.00 49.70  ? 4476 ILE A CA    1 
ATOM   21915 C  C     . ILE A 1 4476 ? 89.221  123.394 95.455  1.00 48.31  ? 4476 ILE A C     1 
ATOM   21916 O  O     . ILE A 1 4476 ? 89.404  124.521 95.932  1.00 45.86  ? 4476 ILE A O     1 
ATOM   21917 C  CB    . ILE A 1 4476 ? 90.545  122.865 93.344  1.00 48.75  ? 4476 ILE A CB    1 
ATOM   21918 C  CG1   . ILE A 1 4476 ? 91.019  124.299 93.096  1.00 47.04  ? 4476 ILE A CG1   1 
ATOM   21919 C  CG2   . ILE A 1 4476 ? 89.258  122.586 92.582  1.00 50.06  ? 4476 ILE A CG2   1 
ATOM   21920 C  CD1   . ILE A 1 4476 ? 92.409  124.583 93.619  1.00 50.66  ? 4476 ILE A CD1   1 
ATOM   21921 N  N     . GLN A 1 4477 ? 88.015  122.823 95.445  1.00 48.50  ? 4477 GLN A N     1 
ATOM   21922 C  CA    . GLN A 1 4477 ? 86.883  123.466 96.103  1.00 52.71  ? 4477 GLN A CA    1 
ATOM   21923 C  C     . GLN A 1 4477 ? 86.816  123.110 97.583  1.00 49.24  ? 4477 GLN A C     1 
ATOM   21924 O  O     . GLN A 1 4477 ? 86.283  123.891 98.384  1.00 48.54  ? 4477 GLN A O     1 
ATOM   21925 C  CB    . GLN A 1 4477 ? 85.581  123.085 95.395  1.00 57.84  ? 4477 GLN A CB    1 
ATOM   21926 C  CG    . GLN A 1 4477 ? 85.224  121.611 95.476  1.00 53.85  ? 4477 GLN A CG    1 
ATOM   21927 C  CD    . GLN A 1 4477 ? 83.961  121.276 94.707  1.00 57.75  ? 4477 GLN A CD    1 
ATOM   21928 O  OE1   . GLN A 1 4477 ? 83.559  120.116 94.627  1.00 61.93  ? 4477 GLN A OE1   1 
ATOM   21929 N  NE2   . GLN A 1 4477 ? 83.322  122.295 94.146  1.00 54.31  ? 4477 GLN A NE2   1 
ATOM   21930 N  N     . TRP A 1 4478 ? 87.357  121.949 97.961  1.00 47.18  ? 4478 TRP A N     1 
ATOM   21931 C  CA    . TRP A 1 4478 ? 87.419  121.594 99.373  1.00 41.01  ? 4478 TRP A CA    1 
ATOM   21932 C  C     . TRP A 1 4478 ? 88.287  122.580 100.139 1.00 40.53  ? 4478 TRP A C     1 
ATOM   21933 O  O     . TRP A 1 4478 ? 88.003  122.894 101.299 1.00 40.88  ? 4478 TRP A O     1 
ATOM   21934 C  CB    . TRP A 1 4478 ? 87.962  120.176 99.550  1.00 38.48  ? 4478 TRP A CB    1 
ATOM   21935 C  CG    . TRP A 1 4478 ? 87.997  119.750 100.988 1.00 41.20  ? 4478 TRP A CG    1 
ATOM   21936 C  CD1   . TRP A 1 4478 ? 86.991  119.150 101.687 1.00 37.07  ? 4478 TRP A CD1   1 
ATOM   21937 C  CD2   . TRP A 1 4478 ? 89.068  119.949 101.920 1.00 41.17  ? 4478 TRP A CD2   1 
ATOM   21938 N  NE1   . TRP A 1 4478 ? 87.381  118.931 102.985 1.00 37.54  ? 4478 TRP A NE1   1 
ATOM   21939 C  CE2   . TRP A 1 4478 ? 88.651  119.416 103.155 1.00 34.29  ? 4478 TRP A CE2   1 
ATOM   21940 C  CE3   . TRP A 1 4478 ? 90.344  120.512 101.825 1.00 41.75  ? 4478 TRP A CE3   1 
ATOM   21941 C  CZ2   . TRP A 1 4478 ? 89.463  119.430 104.286 1.00 38.07  ? 4478 TRP A CZ2   1 
ATOM   21942 C  CZ3   . TRP A 1 4478 ? 91.148  120.527 102.950 1.00 39.93  ? 4478 TRP A CZ3   1 
ATOM   21943 C  CH2   . TRP A 1 4478 ? 90.705  119.988 104.164 1.00 40.98  ? 4478 TRP A CH2   1 
ATOM   21944 N  N     . VAL A 1 4479 ? 89.360  123.065 99.511  1.00 42.26  ? 4479 VAL A N     1 
ATOM   21945 C  CA    . VAL A 1 4479 ? 90.229  124.036 100.172 1.00 40.53  ? 4479 VAL A CA    1 
ATOM   21946 C  C     . VAL A 1 4479 ? 89.466  125.322 100.467 1.00 44.27  ? 4479 VAL A C     1 
ATOM   21947 O  O     . VAL A 1 4479 ? 89.566  125.879 101.565 1.00 48.55  ? 4479 VAL A O     1 
ATOM   21948 C  CB    . VAL A 1 4479 ? 91.483  124.302 99.319  1.00 42.61  ? 4479 VAL A CB    1 
ATOM   21949 C  CG1   . VAL A 1 4479 ? 92.192  125.558 99.800  1.00 45.23  ? 4479 VAL A CG1   1 
ATOM   21950 C  CG2   . VAL A 1 4479 ? 92.420  123.107 99.368  1.00 39.86  ? 4479 VAL A CG2   1 
ATOM   21951 N  N     . SER A 1 4480 ? 88.686  125.809 99.498  1.00 41.62  ? 4480 SER A N     1 
ATOM   21952 C  CA    . SER A 1 4480 ? 87.896  127.016 99.724  1.00 39.18  ? 4480 SER A CA    1 
ATOM   21953 C  C     . SER A 1 4480 ? 86.837  126.796 100.799 1.00 43.49  ? 4480 SER A C     1 
ATOM   21954 O  O     . SER A 1 4480 ? 86.623  127.664 101.658 1.00 52.64  ? 4480 SER A O     1 
ATOM   21955 C  CB    . SER A 1 4480 ? 87.247  127.470 98.417  1.00 38.88  ? 4480 SER A CB    1 
ATOM   21956 O  OG    . SER A 1 4480 ? 86.649  126.379 97.739  1.00 45.12  ? 4480 SER A OG    1 
ATOM   21957 N  N     . ASP A 1 4481 ? 86.163  125.644 100.765 1.00 36.70  ? 4481 ASP A N     1 
ATOM   21958 C  CA    . ASP A 1 4481 ? 85.163  125.351 101.788 1.00 41.62  ? 4481 ASP A CA    1 
ATOM   21959 C  C     . ASP A 1 4481 ? 85.792  125.306 103.176 1.00 42.79  ? 4481 ASP A C     1 
ATOM   21960 O  O     . ASP A 1 4481 ? 85.256  125.883 104.131 1.00 40.81  ? 4481 ASP A O     1 
ATOM   21961 C  CB    . ASP A 1 4481 ? 84.463  124.030 101.470 1.00 41.67  ? 4481 ASP A CB    1 
ATOM   21962 C  CG    . ASP A 1 4481 ? 83.059  123.963 102.035 1.00 45.02  ? 4481 ASP A CG    1 
ATOM   21963 O  OD1   . ASP A 1 4481 ? 82.917  123.930 103.275 1.00 50.44  ? 4481 ASP A OD1   1 
ATOM   21964 O  OD2   . ASP A 1 4481 ? 82.097  123.944 101.238 1.00 48.54  ? 4481 ASP A OD2   1 
ATOM   21965 N  N     . PHE A 1 4482 ? 86.941  124.639 103.300 1.00 39.12  ? 4482 PHE A N     1 
ATOM   21966 C  CA    . PHE A 1 4482 ? 87.627  124.550 104.583 1.00 36.40  ? 4482 PHE A CA    1 
ATOM   21967 C  C     . PHE A 1 4482 ? 88.113  125.918 105.042 1.00 40.70  ? 4482 PHE A C     1 
ATOM   21968 O  O     . PHE A 1 4482 ? 88.085  126.220 106.238 1.00 45.69  ? 4482 PHE A O     1 
ATOM   21969 C  CB    . PHE A 1 4482 ? 88.789  123.562 104.480 1.00 37.82  ? 4482 PHE A CB    1 
ATOM   21970 C  CG    . PHE A 1 4482 ? 89.600  123.441 105.737 1.00 39.23  ? 4482 PHE A CG    1 
ATOM   21971 C  CD1   . PHE A 1 4482 ? 89.075  122.821 106.858 1.00 38.21  ? 4482 PHE A CD1   1 
ATOM   21972 C  CD2   . PHE A 1 4482 ? 90.893  123.934 105.794 1.00 37.62  ? 4482 PHE A CD2   1 
ATOM   21973 C  CE1   . PHE A 1 4482 ? 89.821  122.704 108.013 1.00 38.78  ? 4482 PHE A CE1   1 
ATOM   21974 C  CE2   . PHE A 1 4482 ? 91.643  123.819 106.946 1.00 37.62  ? 4482 PHE A CE2   1 
ATOM   21975 C  CZ    . PHE A 1 4482 ? 91.106  123.202 108.057 1.00 37.89  ? 4482 PHE A CZ    1 
ATOM   21976 N  N     . SER A 1 4483 ? 88.559  126.758 104.105 1.00 39.23  ? 4483 SER A N     1 
ATOM   21977 C  CA    . SER A 1 4483 ? 88.966  128.114 104.459 1.00 45.18  ? 4483 SER A CA    1 
ATOM   21978 C  C     . SER A 1 4483 ? 87.796  128.910 105.022 1.00 44.81  ? 4483 SER A C     1 
ATOM   21979 O  O     . SER A 1 4483 ? 87.941  129.609 106.033 1.00 40.32  ? 4483 SER A O     1 
ATOM   21980 C  CB    . SER A 1 4483 ? 89.555  128.817 103.236 1.00 46.28  ? 4483 SER A CB    1 
ATOM   21981 O  OG    . SER A 1 4483 ? 90.257  129.989 103.608 1.00 55.63  ? 4483 SER A OG    1 
ATOM   21982 N  N     . GLU A 1 4484 ? 86.625  128.812 104.386 1.00 40.23  ? 4484 GLU A N     1 
ATOM   21983 C  CA    . GLU A 1 4484 ? 85.449  129.508 104.905 1.00 40.39  ? 4484 GLU A CA    1 
ATOM   21984 C  C     . GLU A 1 4484 ? 85.061  128.986 106.285 1.00 42.40  ? 4484 GLU A C     1 
ATOM   21985 O  O     . GLU A 1 4484 ? 84.716  129.767 107.184 1.00 45.52  ? 4484 GLU A O     1 
ATOM   21986 C  CB    . GLU A 1 4484 ? 84.278  129.366 103.929 1.00 42.38  ? 4484 GLU A CB    1 
ATOM   21987 C  CG    . GLU A 1 4484 ? 84.480  129.965 102.525 1.00 49.01  ? 4484 GLU A CG    1 
ATOM   21988 C  CD    . GLU A 1 4484 ? 85.318  131.244 102.472 1.00 60.21  ? 4484 GLU A CD    1 
ATOM   21989 O  OE1   . GLU A 1 4484 ? 85.298  132.051 103.428 1.00 60.13  ? 4484 GLU A OE1   1 
ATOM   21990 O  OE2   . GLU A 1 4484 ? 86.009  131.442 101.450 1.00 59.34  ? 4484 GLU A OE2   1 
ATOM   21991 N  N     . ARG A 1 4485 ? 85.112  127.663 106.471 1.00 35.88  ? 4485 ARG A N     1 
ATOM   21992 C  CA    . ARG A 1 4485 ? 84.786  127.088 107.773 1.00 36.54  ? 4485 ARG A CA    1 
ATOM   21993 C  C     . ARG A 1 4485 ? 85.757  127.563 108.846 1.00 41.84  ? 4485 ARG A C     1 
ATOM   21994 O  O     . ARG A 1 4485 ? 85.348  127.867 109.972 1.00 43.16  ? 4485 ARG A O     1 
ATOM   21995 C  CB    . ARG A 1 4485 ? 84.780  125.561 107.690 1.00 38.59  ? 4485 ARG A CB    1 
ATOM   21996 C  CG    . ARG A 1 4485 ? 83.786  124.995 106.691 1.00 34.04  ? 4485 ARG A CG    1 
ATOM   21997 C  CD    . ARG A 1 4485 ? 83.821  123.477 106.666 1.00 37.26  ? 4485 ARG A CD    1 
ATOM   21998 N  NE    . ARG A 1 4485 ? 82.840  122.927 105.738 1.00 40.31  ? 4485 ARG A NE    1 
ATOM   21999 C  CZ    . ARG A 1 4485 ? 81.838  122.134 106.087 1.00 40.69  ? 4485 ARG A CZ    1 
ATOM   22000 N  NH1   . ARG A 1 4485 ? 81.649  121.772 107.346 1.00 40.36  ? 4485 ARG A NH1   1 
ATOM   22001 N  NH2   . ARG A 1 4485 ? 81.005  121.689 105.151 1.00 45.71  ? 4485 ARG A NH2   1 
ATOM   22002 N  N     . ILE A 1 4486 ? 87.048  127.639 108.516 1.00 41.75  ? 4486 ILE A N     1 
ATOM   22003 C  CA    . ILE A 1 4486 ? 88.035  128.116 109.481 1.00 43.33  ? 4486 ILE A CA    1 
ATOM   22004 C  C     . ILE A 1 4486 ? 87.812  129.589 109.798 1.00 43.92  ? 4486 ILE A C     1 
ATOM   22005 O  O     . ILE A 1 4486 ? 87.978  130.018 110.944 1.00 52.97  ? 4486 ILE A O     1 
ATOM   22006 C  CB    . ILE A 1 4486 ? 89.463  127.850 108.970 1.00 46.92  ? 4486 ILE A CB    1 
ATOM   22007 C  CG1   . ILE A 1 4486 ? 89.716  126.347 108.859 1.00 39.86  ? 4486 ILE A CG1   1 
ATOM   22008 C  CG2   . ILE A 1 4486 ? 90.487  128.489 109.889 1.00 43.55  ? 4486 ILE A CG2   1 
ATOM   22009 C  CD1   . ILE A 1 4486 ? 89.443  125.590 110.139 1.00 37.41  ? 4486 ILE A CD1   1 
ATOM   22010 N  N     . LYS A 1 4487 ? 87.445  130.391 108.794 1.00 39.06  ? 4487 LYS A N     1 
ATOM   22011 C  CA    . LYS A 1 4487 ? 87.139  131.794 109.063 1.00 43.54  ? 4487 LYS A CA    1 
ATOM   22012 C  C     . LYS A 1 4487 ? 85.972  131.923 110.034 1.00 50.18  ? 4487 LYS A C     1 
ATOM   22013 O  O     . LYS A 1 4487 ? 86.032  132.707 110.993 1.00 50.93  ? 4487 LYS A O     1 
ATOM   22014 C  CB    . LYS A 1 4487 ? 86.833  132.531 107.759 1.00 41.91  ? 4487 LYS A CB    1 
ATOM   22015 C  CG    . LYS A 1 4487 ? 88.014  132.654 106.812 1.00 46.54  ? 4487 LYS A CG    1 
ATOM   22016 C  CD    . LYS A 1 4487 ? 87.628  133.410 105.551 1.00 46.49  ? 4487 LYS A CD    1 
ATOM   22017 C  CE    . LYS A 1 4487 ? 88.827  133.616 104.639 1.00 50.92  ? 4487 LYS A CE    1 
ATOM   22018 N  NZ    . LYS A 1 4487 ? 89.329  132.330 104.081 1.00 53.35  ? 4487 LYS A NZ    1 
ATOM   22019 N  N     . GLN A 1 4488 ? 84.908  131.148 109.812 1.00 45.81  ? 4488 GLN A N     1 
ATOM   22020 C  CA    . GLN A 1 4488 ? 83.778  131.181 110.737 1.00 43.06  ? 4488 GLN A CA    1 
ATOM   22021 C  C     . GLN A 1 4488 ? 84.185  130.711 112.128 1.00 50.69  ? 4488 GLN A C     1 
ATOM   22022 O  O     . GLN A 1 4488 ? 83.735  131.270 113.137 1.00 55.82  ? 4488 GLN A O     1 
ATOM   22023 C  CB    . GLN A 1 4488 ? 82.624  130.333 110.205 1.00 45.12  ? 4488 GLN A CB    1 
ATOM   22024 C  CG    . GLN A 1 4488 ? 81.346  130.505 111.008 1.00 45.77  ? 4488 GLN A CG    1 
ATOM   22025 C  CD    . GLN A 1 4488 ? 80.148  129.861 110.351 1.00 38.79  ? 4488 GLN A CD    1 
ATOM   22026 O  OE1   . GLN A 1 4488 ? 79.341  130.538 109.718 1.00 45.63  ? 4488 GLN A OE1   1 
ATOM   22027 N  NE2   . GLN A 1 4488 ? 80.024  128.547 110.496 1.00 37.40  ? 4488 GLN A NE2   1 
ATOM   22028 N  N     . LEU A 1 4489 ? 85.028  129.679 112.203 1.00 50.74  ? 4489 LEU A N     1 
ATOM   22029 C  CA    . LEU A 1 4489 ? 85.488  129.193 113.499 1.00 48.35  ? 4489 LEU A CA    1 
ATOM   22030 C  C     . LEU A 1 4489 ? 86.293  130.259 114.232 1.00 54.06  ? 4489 LEU A C     1 
ATOM   22031 O  O     . LEU A 1 4489 ? 86.168  130.410 115.452 1.00 59.90  ? 4489 LEU A O     1 
ATOM   22032 C  CB    . LEU A 1 4489 ? 86.314  127.920 113.320 1.00 47.08  ? 4489 LEU A CB    1 
ATOM   22033 C  CG    . LEU A 1 4489 ? 85.525  126.644 113.019 1.00 48.15  ? 4489 LEU A CG    1 
ATOM   22034 C  CD1   . LEU A 1 4489 ? 86.430  125.583 112.414 1.00 46.54  ? 4489 LEU A CD1   1 
ATOM   22035 C  CD2   . LEU A 1 4489 ? 84.843  126.123 114.275 1.00 50.80  ? 4489 LEU A CD2   1 
ATOM   22036 N  N     . GLN A 1 4490 ? 87.130  131.003 113.505 1.00 49.93  ? 4490 GLN A N     1 
ATOM   22037 C  CA    . GLN A 1 4490 ? 87.876  132.091 114.129 1.00 53.66  ? 4490 GLN A CA    1 
ATOM   22038 C  C     . GLN A 1 4490 ? 86.950  133.191 114.622 1.00 58.88  ? 4490 GLN A C     1 
ATOM   22039 O  O     . GLN A 1 4490 ? 87.165  133.745 115.705 1.00 62.54  ? 4490 GLN A O     1 
ATOM   22040 C  CB    . GLN A 1 4490 ? 88.910  132.668 113.165 1.00 54.41  ? 4490 GLN A CB    1 
ATOM   22041 C  CG    . GLN A 1 4490 ? 89.951  131.681 112.715 1.00 56.13  ? 4490 GLN A CG    1 
ATOM   22042 C  CD    . GLN A 1 4490 ? 90.738  132.172 111.524 1.00 53.65  ? 4490 GLN A CD    1 
ATOM   22043 O  OE1   . GLN A 1 4490 ? 90.425  133.207 110.938 1.00 47.32  ? 4490 GLN A OE1   1 
ATOM   22044 N  NE2   . GLN A 1 4490 ? 91.789  131.443 111.175 1.00 62.02  ? 4490 GLN A NE2   1 
ATOM   22045 N  N     . ASN A 1 4491 ? 85.925  133.537 113.840 1.00 56.28  ? 4491 ASN A N     1 
ATOM   22046 C  CA    . ASN A 1 4491 ? 84.971  134.536 114.317 1.00 54.50  ? 4491 ASN A CA    1 
ATOM   22047 C  C     . ASN A 1 4491 ? 84.274  134.066 115.589 1.00 56.58  ? 4491 ASN A C     1 
ATOM   22048 O  O     . ASN A 1 4491 ? 84.120  134.837 116.546 1.00 60.04  ? 4491 ASN A O     1 
ATOM   22049 C  CB    . ASN A 1 4491 ? 83.943  134.872 113.235 1.00 51.89  ? 4491 ASN A CB    1 
ATOM   22050 C  CG    . ASN A 1 4491 ? 84.568  135.516 112.013 1.00 56.51  ? 4491 ASN A CG    1 
ATOM   22051 O  OD1   . ASN A 1 4491 ? 84.561  134.948 110.923 1.00 63.40  ? 4491 ASN A OD1   1 
ATOM   22052 N  ND2   . ASN A 1 4491 ? 85.115  136.712 112.193 1.00 59.64  ? 4491 ASN A ND2   1 
ATOM   22053 N  N     . ILE A 1 4492 ? 83.866  132.795 115.625 1.00 55.79  ? 4492 ILE A N     1 
ATOM   22054 C  CA    . ILE A 1 4492 ? 83.195  132.255 116.806 1.00 53.99  ? 4492 ILE A CA    1 
ATOM   22055 C  C     . ILE A 1 4492 ? 84.128  132.277 118.012 1.00 60.36  ? 4492 ILE A C     1 
ATOM   22056 O  O     . ILE A 1 4492 ? 83.731  132.672 119.117 1.00 62.79  ? 4492 ILE A O     1 
ATOM   22057 C  CB    . ILE A 1 4492 ? 82.674  130.836 116.517 1.00 54.01  ? 4492 ILE A CB    1 
ATOM   22058 C  CG1   . ILE A 1 4492 ? 81.592  130.877 115.436 1.00 50.60  ? 4492 ILE A CG1   1 
ATOM   22059 C  CG2   . ILE A 1 4492 ? 82.141  130.191 117.788 1.00 51.38  ? 4492 ILE A CG2   1 
ATOM   22060 C  CD1   . ILE A 1 4492 ? 81.202  129.515 114.910 1.00 43.34  ? 4492 ILE A CD1   1 
ATOM   22061 N  N     . SER A 1 4493 ? 85.380  131.855 117.823 1.00 63.33  ? 4493 SER A N     1 
ATOM   22062 C  CA    . SER A 1 4493 ? 86.329  131.817 118.931 1.00 63.77  ? 4493 SER A CA    1 
ATOM   22063 C  C     . SER A 1 4493 ? 86.662  133.219 119.429 1.00 70.32  ? 4493 SER A C     1 
ATOM   22064 O  O     . SER A 1 4493 ? 86.812  133.434 120.636 1.00 72.69  ? 4493 SER A O     1 
ATOM   22065 C  CB    . SER A 1 4493 ? 87.600  131.081 118.509 1.00 61.42  ? 4493 SER A CB    1 
ATOM   22066 O  OG    . SER A 1 4493 ? 88.533  131.022 119.574 1.00 64.94  ? 4493 SER A OG    1 
ATOM   22067 N  N     . LEU A 1 4494 ? 86.792  134.182 118.514 1.00 64.26  ? 4494 LEU A N     1 
ATOM   22068 C  CA    . LEU A 1 4494 ? 87.051  135.560 118.915 1.00 67.95  ? 4494 LEU A CA    1 
ATOM   22069 C  C     . LEU A 1 4494 ? 85.873  136.136 119.689 1.00 72.04  ? 4494 LEU A C     1 
ATOM   22070 O  O     . LEU A 1 4494 ? 86.064  136.852 120.679 1.00 73.63  ? 4494 LEU A O     1 
ATOM   22071 C  CB    . LEU A 1 4494 ? 87.360  136.414 117.685 1.00 68.66  ? 4494 LEU A CB    1 
ATOM   22072 C  CG    . LEU A 1 4494 ? 87.574  137.913 117.904 1.00 70.76  ? 4494 LEU A CG    1 
ATOM   22073 C  CD1   . LEU A 1 4494 ? 88.618  138.160 118.983 1.00 75.23  ? 4494 LEU A CD1   1 
ATOM   22074 C  CD2   . LEU A 1 4494 ? 87.970  138.592 116.602 1.00 61.39  ? 4494 LEU A CD2   1 
ATOM   22075 N  N     . ALA A 1 4495 ? 84.646  135.839 119.251 1.00 71.44  ? 4495 ALA A N     1 
ATOM   22076 C  CA    . ALA A 1 4495 ? 83.474  136.288 119.994 1.00 72.54  ? 4495 ALA A CA    1 
ATOM   22077 C  C     . ALA A 1 4495 ? 83.428  135.661 121.382 1.00 74.35  ? 4495 ALA A C     1 
ATOM   22078 O  O     . ALA A 1 4495 ? 83.091  136.332 122.364 1.00 79.75  ? 4495 ALA A O     1 
ATOM   22079 C  CB    . ALA A 1 4495 ? 82.200  135.963 119.214 1.00 74.22  ? 4495 ALA A CB    1 
ATOM   22080 N  N     . ALA A 1 4496 ? 83.759  134.370 121.481 1.00 74.11  ? 4496 ALA A N     1 
ATOM   22081 C  CA    . ALA A 1 4496 ? 83.733  133.697 122.777 1.00 74.52  ? 4496 ALA A CA    1 
ATOM   22082 C  C     . ALA A 1 4496 ? 84.798  134.247 123.718 1.00 76.21  ? 4496 ALA A C     1 
ATOM   22083 O  O     . ALA A 1 4496 ? 84.531  134.468 124.905 1.00 76.22  ? 4496 ALA A O     1 
ATOM   22084 C  CB    . ALA A 1 4496 ? 83.914  132.191 122.589 1.00 68.16  ? 4496 ALA A CB    1 
ATOM   22085 N  N     . ALA A 1 4497 ? 86.012  134.470 123.211 1.00 78.63  ? 4497 ALA A N     1 
ATOM   22086 C  CA    . ALA A 1 4497 ? 87.101  134.928 124.068 1.00 76.74  ? 4497 ALA A CA    1 
ATOM   22087 C  C     . ALA A 1 4497 ? 86.935  136.397 124.439 1.00 78.18  ? 4497 ALA A C     1 
ATOM   22088 O  O     . ALA A 1 4497 ? 87.147  136.783 125.595 1.00 78.32  ? 4497 ALA A O     1 
ATOM   22089 C  CB    . ALA A 1 4497 ? 88.445  134.694 123.378 1.00 72.40  ? 4497 ALA A CB    1 
ATOM   22090 N  N     . SER A 1 4498 ? 86.554  137.230 123.474 1.00 79.02  ? 4498 SER A N     1 
ATOM   22091 C  CA    . SER A 1 4498 ? 86.414  138.671 123.685 1.00 77.75  ? 4498 SER A CA    1 
ATOM   22092 C  C     . SER A 1 4498 ? 84.938  138.974 123.923 1.00 77.55  ? 4498 SER A C     1 
ATOM   22093 O  O     . SER A 1 4498 ? 84.197  139.314 123.001 1.00 78.70  ? 4498 SER A O     1 
ATOM   22094 C  CB    . SER A 1 4498 ? 86.967  139.449 122.497 1.00 77.03  ? 4498 SER A CB    1 
ATOM   22095 O  OG    . SER A 1 4498 ? 88.323  139.117 122.255 1.00 80.63  ? 4498 SER A OG    1 
ATOM   22096 N  N     . GLY A 1 4499 ? 84.512  138.848 125.177 1.00 76.60  ? 4499 GLY A N     1 
ATOM   22097 C  CA    . GLY A 1 4499 ? 83.138  139.137 125.534 1.00 79.14  ? 4499 GLY A CA    1 
ATOM   22098 C  C     . GLY A 1 4499 ? 82.482  138.048 126.357 1.00 84.48  ? 4499 GLY A C     1 
ATOM   22099 O  O     . GLY A 1 4499 ? 81.453  138.281 126.999 1.00 84.32  ? 4499 GLY A O     1 
ATOM   22100 N  N     . GLY A 1 4500 ? 83.064  136.853 126.345 1.00 81.68  ? 4500 GLY A N     1 
ATOM   22101 C  CA    . GLY A 1 4500 ? 82.525  135.727 127.082 1.00 79.17  ? 4500 GLY A CA    1 
ATOM   22102 C  C     . GLY A 1 4500 ? 81.653  134.841 126.213 1.00 83.15  ? 4500 GLY A C     1 
ATOM   22103 O  O     . GLY A 1 4500 ? 81.439  135.083 125.021 1.00 82.17  ? 4500 GLY A O     1 
ATOM   22104 N  N     . ALA A 1 4501 ? 81.140  133.782 126.845 1.00 81.49  ? 4501 ALA A N     1 
ATOM   22105 C  CA    . ALA A 1 4501 ? 80.278  132.837 126.146 1.00 74.51  ? 4501 ALA A CA    1 
ATOM   22106 C  C     . ALA A 1 4501 ? 78.949  133.456 125.734 1.00 77.69  ? 4501 ALA A C     1 
ATOM   22107 O  O     . ALA A 1 4501 ? 78.316  132.962 124.794 1.00 80.55  ? 4501 ALA A O     1 
ATOM   22108 C  CB    . ALA A 1 4501 ? 80.026  131.608 127.020 1.00 68.55  ? 4501 ALA A CB    1 
ATOM   22109 N  N     . LYS A 1 4502 ? 78.518  134.526 126.406 1.00 78.71  ? 4502 LYS A N     1 
ATOM   22110 C  CA    . LYS A 1 4502 ? 77.243  135.155 126.081 1.00 78.41  ? 4502 LYS A CA    1 
ATOM   22111 C  C     . LYS A 1 4502 ? 77.223  135.743 124.676 1.00 78.33  ? 4502 LYS A C     1 
ATOM   22112 O  O     . LYS A 1 4502 ? 76.139  135.980 124.133 1.00 71.65  ? 4502 LYS A O     1 
ATOM   22113 C  CB    . LYS A 1 4502 ? 76.918  136.240 127.109 1.00 82.61  ? 4502 LYS A CB    1 
ATOM   22114 C  CG    . LYS A 1 4502 ? 77.921  137.382 127.145 1.00 83.27  ? 4502 LYS A CG    1 
ATOM   22115 C  CD    . LYS A 1 4502 ? 77.407  138.542 127.980 1.00 82.88  ? 4502 LYS A CD    1 
ATOM   22116 C  CE    . LYS A 1 4502 ? 78.354  139.729 127.917 1.00 86.20  ? 4502 LYS A CE    1 
ATOM   22117 N  NZ    . LYS A 1 4502 ? 77.845  140.888 128.703 1.00 79.98  ? 4502 LYS A NZ    1 
ATOM   22118 N  N     . GLU A 1 4503 ? 78.390  135.983 124.078 1.00 79.94  ? 4503 GLU A N     1 
ATOM   22119 C  CA    . GLU A 1 4503 ? 78.455  136.458 122.703 1.00 76.71  ? 4503 GLU A CA    1 
ATOM   22120 C  C     . GLU A 1 4503 ? 78.220  135.352 121.683 1.00 70.64  ? 4503 GLU A C     1 
ATOM   22121 O  O     . GLU A 1 4503 ? 78.028  135.655 120.500 1.00 69.70  ? 4503 GLU A O     1 
ATOM   22122 C  CB    . GLU A 1 4503 ? 79.810  137.119 122.439 1.00 77.30  ? 4503 GLU A CB    1 
ATOM   22123 C  CG    . GLU A 1 4503 ? 80.275  138.051 123.547 1.00 82.85  ? 4503 GLU A CG    1 
ATOM   22124 C  CD    . GLU A 1 4503 ? 79.547  139.383 123.541 1.00 92.57  ? 4503 GLU A CD    1 
ATOM   22125 O  OE1   . GLU A 1 4503 ? 78.791  139.650 122.583 1.00 94.02  ? 4503 GLU A OE1   1 
ATOM   22126 O  OE2   . GLU A 1 4503 ? 79.732  140.164 124.498 1.00 89.87  ? 4503 GLU A OE2   1 
ATOM   22127 N  N     . LEU A 1 4504 ? 78.233  134.085 122.106 1.00 64.34  ? 4504 LEU A N     1 
ATOM   22128 C  CA    . LEU A 1 4504 ? 77.964  132.993 121.177 1.00 64.46  ? 4504 LEU A CA    1 
ATOM   22129 C  C     . LEU A 1 4504 ? 76.516  132.998 120.706 1.00 65.30  ? 4504 LEU A C     1 
ATOM   22130 O  O     . LEU A 1 4504 ? 76.223  132.528 119.601 1.00 65.57  ? 4504 LEU A O     1 
ATOM   22131 C  CB    . LEU A 1 4504 ? 78.305  131.653 121.830 1.00 66.00  ? 4504 LEU A CB    1 
ATOM   22132 C  CG    . LEU A 1 4504 ? 79.768  131.446 122.227 1.00 64.17  ? 4504 LEU A CG    1 
ATOM   22133 C  CD1   . LEU A 1 4504 ? 79.958  130.089 122.886 1.00 58.83  ? 4504 LEU A CD1   1 
ATOM   22134 C  CD2   . LEU A 1 4504 ? 80.667  131.582 121.010 1.00 58.87  ? 4504 LEU A CD2   1 
ATOM   22135 N  N     . LYS A 1 4505 ? 75.602  133.519 121.526 1.00 61.41  ? 4505 LYS A N     1 
ATOM   22136 C  CA    . LYS A 1 4505 ? 74.188  133.532 121.172 1.00 56.73  ? 4505 LYS A CA    1 
ATOM   22137 C  C     . LYS A 1 4505 ? 73.862  134.604 120.138 1.00 60.71  ? 4505 LYS A C     1 
ATOM   22138 O  O     . LYS A 1 4505 ? 72.924  134.434 119.351 1.00 60.53  ? 4505 LYS A O     1 
ATOM   22139 C  CB    . LYS A 1 4505 ? 73.348  133.725 122.439 1.00 49.64  ? 4505 LYS A CB    1 
ATOM   22140 C  CG    . LYS A 1 4505 ? 71.841  133.706 122.234 1.00 49.32  ? 4505 LYS A CG    1 
ATOM   22141 C  CD    . LYS A 1 4505 ? 71.267  135.113 122.191 1.00 49.92  ? 4505 LYS A CD    1 
ATOM   22142 C  CE    . LYS A 1 4505 ? 69.948  135.146 121.445 1.00 51.32  ? 4505 LYS A CE    1 
ATOM   22143 N  NZ    . LYS A 1 4505 ? 69.476  136.539 121.217 1.00 58.06  ? 4505 LYS A NZ    1 
ATOM   22144 N  N     . ASN A 1 4506 ? 74.622  135.697 120.114 1.00 60.18  ? 4506 ASN A N     1 
ATOM   22145 C  CA    . ASN A 1 4506 ? 74.326  136.818 119.232 1.00 61.68  ? 4506 ASN A CA    1 
ATOM   22146 C  C     . ASN A 1 4506 ? 74.880  136.627 117.825 1.00 58.17  ? 4506 ASN A C     1 
ATOM   22147 O  O     . ASN A 1 4506 ? 74.304  137.156 116.868 1.00 57.97  ? 4506 ASN A O     1 
ATOM   22148 C  CB    . ASN A 1 4506 ? 74.890  138.111 119.839 1.00 66.68  ? 4506 ASN A CB    1 
ATOM   22149 C  CG    . ASN A 1 4506 ? 74.389  139.369 119.144 1.00 73.93  ? 4506 ASN A CG    1 
ATOM   22150 O  OD1   . ASN A 1 4506 ? 73.611  139.310 118.193 1.00 76.94  ? 4506 ASN A OD1   1 
ATOM   22151 N  ND2   . ASN A 1 4506 ? 74.842  140.521 119.624 1.00 68.63  ? 4506 ASN A ND2   1 
ATOM   22152 N  N     . ILE A 1 4507 ? 75.962  135.863 117.671 1.00 55.95  ? 4507 ILE A N     1 
ATOM   22153 C  CA    . ILE A 1 4507 ? 76.622  135.754 116.376 1.00 55.95  ? 4507 ILE A CA    1 
ATOM   22154 C  C     . ILE A 1 4507 ? 75.765  134.945 115.410 1.00 53.38  ? 4507 ILE A C     1 
ATOM   22155 O  O     . ILE A 1 4507 ? 75.164  133.925 115.776 1.00 46.88  ? 4507 ILE A O     1 
ATOM   22156 C  CB    . ILE A 1 4507 ? 78.026  135.142 116.540 1.00 53.86  ? 4507 ILE A CB    1 
ATOM   22157 C  CG1   . ILE A 1 4507 ? 78.823  135.269 115.238 1.00 55.75  ? 4507 ILE A CG1   1 
ATOM   22158 C  CG2   . ILE A 1 4507 ? 77.953  133.694 117.012 1.00 48.06  ? 4507 ILE A CG2   1 
ATOM   22159 C  CD1   . ILE A 1 4507 ? 79.138  136.695 114.850 1.00 58.72  ? 4507 ILE A CD1   1 
ATOM   22160 N  N     . HIS A 1 4508 ? 75.675  135.425 114.171 1.00 51.49  ? 4508 HIS A N     1 
ATOM   22161 C  CA    . HIS A 1 4508 ? 75.005  134.685 113.112 1.00 46.00  ? 4508 HIS A CA    1 
ATOM   22162 C  C     . HIS A 1 4508 ? 75.895  133.546 112.636 1.00 44.77  ? 4508 HIS A C     1 
ATOM   22163 O  O     . HIS A 1 4508 ? 77.116  133.696 112.529 1.00 50.37  ? 4508 HIS A O     1 
ATOM   22164 C  CB    . HIS A 1 4508 ? 74.661  135.610 111.946 1.00 42.08  ? 4508 HIS A CB    1 
ATOM   22165 C  CG    . HIS A 1 4508 ? 73.773  136.754 112.325 1.00 44.78  ? 4508 HIS A CG    1 
ATOM   22166 N  ND1   . HIS A 1 4508 ? 72.984  136.741 113.455 1.00 43.22  ? 4508 HIS A ND1   1 
ATOM   22167 C  CD2   . HIS A 1 4508 ? 73.556  137.950 111.729 1.00 44.45  ? 4508 HIS A CD2   1 
ATOM   22168 C  CE1   . HIS A 1 4508 ? 72.315  137.877 113.536 1.00 47.35  ? 4508 HIS A CE1   1 
ATOM   22169 N  NE2   . HIS A 1 4508 ? 72.644  138.628 112.501 1.00 47.16  ? 4508 HIS A NE2   1 
ATOM   22170 N  N     . VAL A 1 4509 ? 75.280  132.403 112.350 1.00 36.10  ? 4509 VAL A N     1 
ATOM   22171 C  CA    . VAL A 1 4509 ? 76.003  131.176 112.043 1.00 36.86  ? 4509 VAL A CA    1 
ATOM   22172 C  C     . VAL A 1 4509 ? 75.549  130.653 110.689 1.00 34.57  ? 4509 VAL A C     1 
ATOM   22173 O  O     . VAL A 1 4509 ? 74.345  130.516 110.443 1.00 34.93  ? 4509 VAL A O     1 
ATOM   22174 C  CB    . VAL A 1 4509 ? 75.790  130.111 113.134 1.00 39.44  ? 4509 VAL A CB    1 
ATOM   22175 C  CG1   . VAL A 1 4509 ? 76.459  128.817 112.736 1.00 30.37  ? 4509 VAL A CG1   1 
ATOM   22176 C  CG2   . VAL A 1 4509 ? 76.322  130.603 114.470 1.00 47.51  ? 4509 VAL A CG2   1 
ATOM   22177 N  N     . CYS A 1 4510 ? 76.510  130.359 109.816 1.00 34.78  ? 4510 CYS A N     1 
ATOM   22178 C  CA    . CYS A 1 4510 ? 76.228  129.636 108.580 1.00 31.88  ? 4510 CYS A CA    1 
ATOM   22179 C  C     . CYS A 1 4510 ? 76.217  128.146 108.898 1.00 32.20  ? 4510 CYS A C     1 
ATOM   22180 O  O     . CYS A 1 4510 ? 77.261  127.562 109.209 1.00 32.21  ? 4510 CYS A O     1 
ATOM   22181 C  CB    . CYS A 1 4510 ? 77.259  129.969 107.506 1.00 26.13  ? 4510 CYS A CB    1 
ATOM   22182 S  SG    . CYS A 1 4510 ? 77.281  128.826 106.107 1.00 45.75  ? 4510 CYS A SG    1 
ATOM   22183 N  N     . LEU A 1 4511 ? 75.033  127.532 108.828 1.00 29.91  ? 4511 LEU A N     1 
ATOM   22184 C  CA    . LEU A 1 4511 ? 74.888  126.139 109.239 1.00 29.89  ? 4511 LEU A CA    1 
ATOM   22185 C  C     . LEU A 1 4511 ? 75.732  125.204 108.383 1.00 29.66  ? 4511 LEU A C     1 
ATOM   22186 O  O     . LEU A 1 4511 ? 76.215  124.179 108.877 1.00 31.66  ? 4511 LEU A O     1 
ATOM   22187 C  CB    . LEU A 1 4511 ? 73.417  125.729 109.183 1.00 28.73  ? 4511 LEU A CB    1 
ATOM   22188 C  CG    . LEU A 1 4511 ? 72.616  125.946 110.468 1.00 28.76  ? 4511 LEU A CG    1 
ATOM   22189 C  CD1   . LEU A 1 4511 ? 71.173  125.505 110.283 1.00 28.46  ? 4511 LEU A CD1   1 
ATOM   22190 C  CD2   . LEU A 1 4511 ? 73.260  125.222 111.638 1.00 32.42  ? 4511 LEU A CD2   1 
ATOM   22191 N  N     . GLY A 1 4512 ? 75.915  125.533 107.103 1.00 28.74  ? 4512 GLY A N     1 
ATOM   22192 C  CA    . GLY A 1 4512 ? 76.727  124.688 106.244 1.00 31.58  ? 4512 GLY A CA    1 
ATOM   22193 C  C     . GLY A 1 4512 ? 78.186  124.658 106.655 1.00 34.76  ? 4512 GLY A C     1 
ATOM   22194 O  O     . GLY A 1 4512 ? 78.847  123.621 106.558 1.00 36.72  ? 4512 GLY A O     1 
ATOM   22195 N  N     . GLY A 1 4513 ? 78.710  125.796 107.115 1.00 34.10  ? 4513 GLY A N     1 
ATOM   22196 C  CA    . GLY A 1 4513 ? 80.095  125.846 107.546 1.00 30.68  ? 4513 GLY A CA    1 
ATOM   22197 C  C     . GLY A 1 4513 ? 80.375  124.994 108.767 1.00 32.85  ? 4513 GLY A C     1 
ATOM   22198 O  O     . GLY A 1 4513 ? 81.496  124.508 108.944 1.00 39.64  ? 4513 GLY A O     1 
ATOM   22199 N  N     . LEU A 1 4514 ? 79.375  124.805 109.623 1.00 31.28  ? 4514 LEU A N     1 
ATOM   22200 C  CA    . LEU A 1 4514 ? 79.550  123.985 110.813 1.00 38.28  ? 4514 LEU A CA    1 
ATOM   22201 C  C     . LEU A 1 4514 ? 79.770  122.527 110.431 1.00 41.32  ? 4514 LEU A C     1 
ATOM   22202 O  O     . LEU A 1 4514 ? 79.209  122.032 109.450 1.00 43.59  ? 4514 LEU A O     1 
ATOM   22203 C  CB    . LEU A 1 4514 ? 78.332  124.105 111.723 1.00 38.90  ? 4514 LEU A CB    1 
ATOM   22204 C  CG    . LEU A 1 4514 ? 78.087  125.476 112.349 1.00 38.74  ? 4514 LEU A CG    1 
ATOM   22205 C  CD1   . LEU A 1 4514 ? 76.931  125.390 113.319 1.00 35.34  ? 4514 LEU A CD1   1 
ATOM   22206 C  CD2   . LEU A 1 4514 ? 79.340  125.989 113.041 1.00 35.33  ? 4514 LEU A CD2   1 
ATOM   22207 N  N     . PHE A 1 4515 ? 80.598  121.837 111.217 1.00 44.00  ? 4515 PHE A N     1 
ATOM   22208 C  CA    . PHE A 1 4515 ? 80.876  120.434 110.930 1.00 42.52  ? 4515 PHE A CA    1 
ATOM   22209 C  C     . PHE A 1 4515 ? 79.680  119.553 111.276 1.00 45.16  ? 4515 PHE A C     1 
ATOM   22210 O  O     . PHE A 1 4515 ? 79.414  118.561 110.587 1.00 48.94  ? 4515 PHE A O     1 
ATOM   22211 C  CB    . PHE A 1 4515 ? 82.124  119.978 111.685 1.00 45.54  ? 4515 PHE A CB    1 
ATOM   22212 C  CG    . PHE A 1 4515 ? 83.372  120.727 111.302 1.00 50.82  ? 4515 PHE A CG    1 
ATOM   22213 C  CD1   . PHE A 1 4515 ? 83.626  121.052 109.981 1.00 48.09  ? 4515 PHE A CD1   1 
ATOM   22214 C  CD2   . PHE A 1 4515 ? 84.301  121.089 112.262 1.00 48.30  ? 4515 PHE A CD2   1 
ATOM   22215 C  CE1   . PHE A 1 4515 ? 84.772  121.740 109.630 1.00 48.42  ? 4515 PHE A CE1   1 
ATOM   22216 C  CE2   . PHE A 1 4515 ? 85.448  121.774 111.918 1.00 48.90  ? 4515 PHE A CE2   1 
ATOM   22217 C  CZ    . PHE A 1 4515 ? 85.686  122.099 110.600 1.00 49.87  ? 4515 PHE A CZ    1 
ATOM   22218 N  N     . VAL A 1 4516 ? 78.952  119.893 112.336 1.00 45.35  ? 4516 VAL A N     1 
ATOM   22219 C  CA    . VAL A 1 4516 ? 77.760  119.146 112.737 1.00 42.91  ? 4516 VAL A CA    1 
ATOM   22220 C  C     . VAL A 1 4516 ? 76.615  120.110 113.052 1.00 42.25  ? 4516 VAL A C     1 
ATOM   22221 O  O     . VAL A 1 4516 ? 76.402  120.491 114.212 1.00 42.58  ? 4516 VAL A O     1 
ATOM   22222 C  CB    . VAL A 1 4516 ? 78.091  118.171 113.886 1.00 41.60  ? 4516 VAL A CB    1 
ATOM   22223 C  CG1   . VAL A 1 4516 ? 78.605  118.890 115.137 1.00 46.04  ? 4516 VAL A CG1   1 
ATOM   22224 C  CG2   . VAL A 1 4516 ? 76.879  117.307 114.216 1.00 43.51  ? 4516 VAL A CG2   1 
ATOM   22225 N  N     . PRO A 1 4517 ? 75.860  120.545 112.039 1.00 43.97  ? 4517 PRO A N     1 
ATOM   22226 C  CA    . PRO A 1 4517 ? 74.749  121.481 112.296 1.00 42.31  ? 4517 PRO A CA    1 
ATOM   22227 C  C     . PRO A 1 4517 ? 73.642  120.911 113.173 1.00 40.69  ? 4517 PRO A C     1 
ATOM   22228 O  O     . PRO A 1 4517 ? 72.944  121.682 113.849 1.00 40.34  ? 4517 PRO A O     1 
ATOM   22229 C  CB    . PRO A 1 4517 ? 74.242  121.812 110.885 1.00 37.12  ? 4517 PRO A CB    1 
ATOM   22230 C  CG    . PRO A 1 4517 ? 74.706  120.679 110.034 1.00 38.55  ? 4517 PRO A CG    1 
ATOM   22231 C  CD    . PRO A 1 4517 ? 76.014  120.244 110.607 1.00 39.48  ? 4517 PRO A CD    1 
ATOM   22232 N  N     . GLU A 1 4518 ? 73.449  119.586 113.174 1.00 38.68  ? 4518 GLU A N     1 
ATOM   22233 C  CA    . GLU A 1 4518 ? 72.449  118.989 114.054 1.00 41.45  ? 4518 GLU A CA    1 
ATOM   22234 C  C     . GLU A 1 4518 ? 72.739  119.332 115.507 1.00 44.62  ? 4518 GLU A C     1 
ATOM   22235 O  O     . GLU A 1 4518 ? 71.826  119.659 116.278 1.00 45.54  ? 4518 GLU A O     1 
ATOM   22236 C  CB    . GLU A 1 4518 ? 72.415  117.469 113.885 1.00 50.40  ? 4518 GLU A CB    1 
ATOM   22237 C  CG    . GLU A 1 4518 ? 71.949  116.956 112.537 1.00 47.16  ? 4518 GLU A CG    1 
ATOM   22238 C  CD    . GLU A 1 4518 ? 73.065  116.917 111.514 1.00 49.78  ? 4518 GLU A CD    1 
ATOM   22239 O  OE1   . GLU A 1 4518 ? 74.216  117.243 111.874 1.00 44.55  ? 4518 GLU A OE1   1 
ATOM   22240 O  OE2   . GLU A 1 4518 ? 72.798  116.529 110.359 1.00 51.28  ? 4518 GLU A OE2   1 
ATOM   22241 N  N     . ALA A 1 4519 ? 74.013  119.254 115.897 1.00 42.94  ? 4519 ALA A N     1 
ATOM   22242 C  CA    . ALA A 1 4519 ? 74.397  119.599 117.256 1.00 36.03  ? 4519 ALA A CA    1 
ATOM   22243 C  C     . ALA A 1 4519 ? 74.149  121.070 117.552 1.00 40.25  ? 4519 ALA A C     1 
ATOM   22244 O  O     . ALA A 1 4519 ? 73.783  121.411 118.677 1.00 47.88  ? 4519 ALA A O     1 
ATOM   22245 C  CB    . ALA A 1 4519 ? 75.863  119.241 117.496 1.00 37.36  ? 4519 ALA A CB    1 
ATOM   22246 N  N     . TYR A 1 4520 ? 74.331  121.955 116.567 1.00 36.49  ? 4520 TYR A N     1 
ATOM   22247 C  CA    . TYR A 1 4520 ? 74.020  123.365 116.786 1.00 34.95  ? 4520 TYR A CA    1 
ATOM   22248 C  C     . TYR A 1 4520 ? 72.530  123.571 117.028 1.00 36.39  ? 4520 TYR A C     1 
ATOM   22249 O  O     . TYR A 1 4520 ? 72.136  124.333 117.921 1.00 39.06  ? 4520 TYR A O     1 
ATOM   22250 C  CB    . TYR A 1 4520 ? 74.478  124.206 115.597 1.00 36.16  ? 4520 TYR A CB    1 
ATOM   22251 C  CG    . TYR A 1 4520 ? 74.114  125.671 115.712 1.00 38.74  ? 4520 TYR A CG    1 
ATOM   22252 C  CD1   . TYR A 1 4520 ? 74.867  126.532 116.500 1.00 38.10  ? 4520 TYR A CD1   1 
ATOM   22253 C  CD2   . TYR A 1 4520 ? 73.020  126.193 115.036 1.00 34.66  ? 4520 TYR A CD2   1 
ATOM   22254 C  CE1   . TYR A 1 4520 ? 74.541  127.870 116.611 1.00 32.80  ? 4520 TYR A CE1   1 
ATOM   22255 C  CE2   . TYR A 1 4520 ? 72.686  127.530 115.140 1.00 36.71  ? 4520 TYR A CE2   1 
ATOM   22256 C  CZ    . TYR A 1 4520 ? 73.450  128.363 115.930 1.00 38.49  ? 4520 TYR A CZ    1 
ATOM   22257 O  OH    . TYR A 1 4520 ? 73.123  129.695 116.038 1.00 41.81  ? 4520 TYR A OH    1 
ATOM   22258 N  N     . ILE A 1 4521 ? 71.687  122.908 116.233 1.00 36.34  ? 4521 ILE A N     1 
ATOM   22259 C  CA    . ILE A 1 4521 ? 70.243  123.036 116.416 1.00 34.32  ? 4521 ILE A CA    1 
ATOM   22260 C  C     . ILE A 1 4521 ? 69.841  122.529 117.797 1.00 36.23  ? 4521 ILE A C     1 
ATOM   22261 O  O     . ILE A 1 4521 ? 69.075  123.176 118.526 1.00 37.30  ? 4521 ILE A O     1 
ATOM   22262 C  CB    . ILE A 1 4521 ? 69.493  122.288 115.299 1.00 36.61  ? 4521 ILE A CB    1 
ATOM   22263 C  CG1   . ILE A 1 4521 ? 69.821  122.898 113.935 1.00 31.25  ? 4521 ILE A CG1   1 
ATOM   22264 C  CG2   . ILE A 1 4521 ? 67.993  122.317 115.548 1.00 31.79  ? 4521 ILE A CG2   1 
ATOM   22265 C  CD1   . ILE A 1 4521 ? 69.516  124.372 113.836 1.00 28.45  ? 4521 ILE A CD1   1 
ATOM   22266 N  N     . THR A 1 4522 ? 70.371  121.364 118.180 1.00 38.81  ? 4522 THR A N     1 
ATOM   22267 C  CA    . THR A 1 4522 ? 70.048  120.800 119.487 1.00 42.20  ? 4522 THR A CA    1 
ATOM   22268 C  C     . THR A 1 4522 ? 70.576  121.679 120.614 1.00 40.15  ? 4522 THR A C     1 
ATOM   22269 O  O     . THR A 1 4522 ? 69.929  121.815 121.657 1.00 39.87  ? 4522 THR A O     1 
ATOM   22270 C  CB    . THR A 1 4522 ? 70.611  119.384 119.600 1.00 43.65  ? 4522 THR A CB    1 
ATOM   22271 O  OG1   . THR A 1 4522 ? 70.011  118.551 118.601 1.00 45.22  ? 4522 THR A OG1   1 
ATOM   22272 C  CG2   . THR A 1 4522 ? 70.311  118.799 120.973 1.00 44.57  ? 4522 THR A CG2   1 
ATOM   22273 N  N     . ALA A 1 4523 ? 71.752  122.282 120.427 1.00 39.45  ? 4523 ALA A N     1 
ATOM   22274 C  CA    . ALA A 1 4523 ? 72.309  123.167 121.442 1.00 39.74  ? 4523 ALA A CA    1 
ATOM   22275 C  C     . ALA A 1 4523 ? 71.452  124.410 121.622 1.00 39.14  ? 4523 ALA A C     1 
ATOM   22276 O  O     . ALA A 1 4523 ? 71.240  124.861 122.751 1.00 44.93  ? 4523 ALA A O     1 
ATOM   22277 C  CB    . ALA A 1 4523 ? 73.743  123.550 121.075 1.00 35.72  ? 4523 ALA A CB    1 
ATOM   22278 N  N     . THR A 1 4524 ? 70.957  124.985 120.524 1.00 41.03  ? 4524 THR A N     1 
ATOM   22279 C  CA    . THR A 1 4524 ? 70.053  126.126 120.641 1.00 37.50  ? 4524 THR A CA    1 
ATOM   22280 C  C     . THR A 1 4524 ? 68.763  125.732 121.352 1.00 37.16  ? 4524 THR A C     1 
ATOM   22281 O  O     . THR A 1 4524 ? 68.260  126.476 122.208 1.00 40.21  ? 4524 THR A O     1 
ATOM   22282 C  CB    . THR A 1 4524 ? 69.748  126.703 119.259 1.00 35.54  ? 4524 THR A CB    1 
ATOM   22283 O  OG1   . THR A 1 4524 ? 69.344  125.649 118.376 1.00 42.45  ? 4524 THR A OG1   1 
ATOM   22284 C  CG2   . THR A 1 4524 ? 70.978  127.392 118.688 1.00 32.66  ? 4524 THR A CG2   1 
ATOM   22285 N  N     . ARG A 1 4525 ? 68.217  124.560 121.015 1.00 37.75  ? 4525 ARG A N     1 
ATOM   22286 C  CA    . ARG A 1 4525 ? 67.009  124.089 121.687 1.00 39.84  ? 4525 ARG A CA    1 
ATOM   22287 C  C     . ARG A 1 4525 ? 67.248  123.895 123.181 1.00 44.39  ? 4525 ARG A C     1 
ATOM   22288 O  O     . ARG A 1 4525 ? 66.420  124.293 124.009 1.00 47.21  ? 4525 ARG A O     1 
ATOM   22289 C  CB    . ARG A 1 4525 ? 66.532  122.788 121.041 1.00 41.71  ? 4525 ARG A CB    1 
ATOM   22290 C  CG    . ARG A 1 4525 ? 65.150  122.336 121.475 1.00 45.14  ? 4525 ARG A CG    1 
ATOM   22291 C  CD    . ARG A 1 4525 ? 64.901  120.895 121.064 1.00 50.15  ? 4525 ARG A CD    1 
ATOM   22292 N  NE    . ARG A 1 4525 ? 63.482  120.560 121.062 1.00 58.66  ? 4525 ARG A NE    1 
ATOM   22293 C  CZ    . ARG A 1 4525 ? 62.883  119.847 120.117 1.00 60.20  ? 4525 ARG A CZ    1 
ATOM   22294 N  NH1   . ARG A 1 4525 ? 63.553  119.376 119.078 1.00 56.67  ? 4525 ARG A NH1   1 
ATOM   22295 N  NH2   . ARG A 1 4525 ? 61.580  119.601 120.218 1.00 59.93  ? 4525 ARG A NH2   1 
ATOM   22296 N  N     . GLN A 1 4526 ? 68.382  123.290 123.541 1.00 45.39  ? 4526 GLN A N     1 
ATOM   22297 C  CA    . GLN A 1 4526 ? 68.723  123.085 124.944 1.00 43.09  ? 4526 GLN A CA    1 
ATOM   22298 C  C     . GLN A 1 4526 ? 68.932  124.412 125.661 1.00 43.80  ? 4526 GLN A C     1 
ATOM   22299 O  O     . GLN A 1 4526 ? 68.539  124.566 126.821 1.00 52.82  ? 4526 GLN A O     1 
ATOM   22300 C  CB    . GLN A 1 4526 ? 69.973  122.208 125.048 1.00 44.61  ? 4526 GLN A CB    1 
ATOM   22301 C  CG    . GLN A 1 4526 ? 70.543  122.063 126.451 1.00 47.52  ? 4526 GLN A CG    1 
ATOM   22302 C  CD    . GLN A 1 4526 ? 69.567  121.428 127.418 1.00 52.30  ? 4526 GLN A CD    1 
ATOM   22303 O  OE1   . GLN A 1 4526 ? 69.131  120.294 127.223 1.00 46.00  ? 4526 GLN A OE1   1 
ATOM   22304 N  NE2   . GLN A 1 4526 ? 69.222  122.157 128.473 1.00 60.11  ? 4526 GLN A NE2   1 
ATOM   22305 N  N     . TYR A 1 4527 ? 69.554  125.380 124.986 1.00 38.52  ? 4527 TYR A N     1 
ATOM   22306 C  CA    . TYR A 1 4527 ? 69.735  126.710 125.558 1.00 43.04  ? 4527 TYR A CA    1 
ATOM   22307 C  C     . TYR A 1 4527 ? 68.395  127.352 125.890 1.00 48.82  ? 4527 TYR A C     1 
ATOM   22308 O  O     . TYR A 1 4527 ? 68.199  127.880 126.993 1.00 53.53  ? 4527 TYR A O     1 
ATOM   22309 C  CB    . TYR A 1 4527 ? 70.523  127.581 124.579 1.00 43.15  ? 4527 TYR A CB    1 
ATOM   22310 C  CG    . TYR A 1 4527 ? 70.815  128.983 125.064 1.00 46.84  ? 4527 TYR A CG    1 
ATOM   22311 C  CD1   . TYR A 1 4527 ? 71.802  129.224 126.011 1.00 50.51  ? 4527 TYR A CD1   1 
ATOM   22312 C  CD2   . TYR A 1 4527 ? 70.106  130.068 124.567 1.00 42.69  ? 4527 TYR A CD2   1 
ATOM   22313 C  CE1   . TYR A 1 4527 ? 72.071  130.507 126.449 1.00 49.08  ? 4527 TYR A CE1   1 
ATOM   22314 C  CE2   . TYR A 1 4527 ? 70.367  131.352 124.999 1.00 43.09  ? 4527 TYR A CE2   1 
ATOM   22315 C  CZ    . TYR A 1 4527 ? 71.350  131.567 125.940 1.00 46.15  ? 4527 TYR A CZ    1 
ATOM   22316 O  OH    . TYR A 1 4527 ? 71.611  132.847 126.372 1.00 52.95  ? 4527 TYR A OH    1 
ATOM   22317 N  N     . VAL A 1 4528 ? 67.453  127.308 124.947 1.00 48.73  ? 4528 VAL A N     1 
ATOM   22318 C  CA    . VAL A 1 4528 ? 66.155  127.931 125.188 1.00 48.06  ? 4528 VAL A CA    1 
ATOM   22319 C  C     . VAL A 1 4528 ? 65.394  127.184 126.278 1.00 52.00  ? 4528 VAL A C     1 
ATOM   22320 O  O     . VAL A 1 4528 ? 64.731  127.800 127.122 1.00 57.45  ? 4528 VAL A O     1 
ATOM   22321 C  CB    . VAL A 1 4528 ? 65.345  128.019 123.884 1.00 47.13  ? 4528 VAL A CB    1 
ATOM   22322 C  CG1   . VAL A 1 4528 ? 64.000  128.675 124.147 1.00 41.87  ? 4528 VAL A CG1   1 
ATOM   22323 C  CG2   . VAL A 1 4528 ? 66.118  128.802 122.839 1.00 42.52  ? 4528 VAL A CG2   1 
ATOM   22324 N  N     . ALA A 1 4529 ? 65.477  125.851 126.286 1.00 51.07  ? 4529 ALA A N     1 
ATOM   22325 C  CA    . ALA A 1 4529 ? 64.790  125.079 127.318 1.00 56.08  ? 4529 ALA A CA    1 
ATOM   22326 C  C     . ALA A 1 4529 ? 65.375  125.338 128.700 1.00 63.91  ? 4529 ALA A C     1 
ATOM   22327 O  O     . ALA A 1 4529 ? 64.631  125.387 129.686 1.00 68.90  ? 4529 ALA A O     1 
ATOM   22328 C  CB    . ALA A 1 4529 ? 64.849  123.589 126.988 1.00 58.86  ? 4529 ALA A CB    1 
ATOM   22329 N  N     . GLN A 1 4530 ? 66.695  125.504 128.793 1.00 59.72  ? 4530 GLN A N     1 
ATOM   22330 C  CA    . GLN A 1 4530 ? 67.338  125.775 130.071 1.00 58.71  ? 4530 GLN A CA    1 
ATOM   22331 C  C     . GLN A 1 4530 ? 67.075  127.196 130.547 1.00 63.29  ? 4530 GLN A C     1 
ATOM   22332 O  O     . GLN A 1 4530 ? 67.014  127.437 131.758 1.00 69.72  ? 4530 GLN A O     1 
ATOM   22333 C  CB    . GLN A 1 4530 ? 68.842  125.526 129.956 1.00 57.29  ? 4530 GLN A CB    1 
ATOM   22334 C  CG    . GLN A 1 4530 ? 69.580  125.478 131.281 1.00 63.15  ? 4530 GLN A CG    1 
ATOM   22335 C  CD    . GLN A 1 4530 ? 70.898  124.736 131.178 1.00 65.83  ? 4530 GLN A CD    1 
ATOM   22336 O  OE1   . GLN A 1 4530 ? 71.246  124.211 130.121 1.00 57.92  ? 4530 GLN A OE1   1 
ATOM   22337 N  NE2   . GLN A 1 4530 ? 71.640  124.691 132.279 1.00 63.60  ? 4530 GLN A NE2   1 
ATOM   22338 N  N     . ALA A 1 4531 ? 66.922  128.144 129.619 1.00 61.56  ? 4531 ALA A N     1 
ATOM   22339 C  CA    . ALA A 1 4531 ? 66.611  129.514 130.013 1.00 61.94  ? 4531 ALA A CA    1 
ATOM   22340 C  C     . ALA A 1 4531 ? 65.251  129.597 130.696 1.00 63.72  ? 4531 ALA A C     1 
ATOM   22341 O  O     . ALA A 1 4531 ? 65.085  130.331 131.677 1.00 62.27  ? 4531 ALA A O     1 
ATOM   22342 C  CB    . ALA A 1 4531 ? 66.658  130.435 128.794 1.00 54.93  ? 4531 ALA A CB    1 
ATOM   22343 N  N     . ASN A 1 4532 ? 64.268  128.852 130.194 1.00 67.57  ? 4532 ASN A N     1 
ATOM   22344 C  CA    . ASN A 1 4532 ? 62.918  128.860 130.739 1.00 67.38  ? 4532 ASN A CA    1 
ATOM   22345 C  C     . ASN A 1 4532 ? 62.623  127.640 131.605 1.00 68.44  ? 4532 ASN A C     1 
ATOM   22346 O  O     . ASN A 1 4532 ? 61.465  127.430 131.981 1.00 69.01  ? 4532 ASN A O     1 
ATOM   22347 C  CB    . ASN A 1 4532 ? 61.896  128.954 129.606 1.00 67.98  ? 4532 ASN A CB    1 
ATOM   22348 C  CG    . ASN A 1 4532 ? 62.211  130.069 128.629 1.00 66.55  ? 4532 ASN A CG    1 
ATOM   22349 O  OD1   . ASN A 1 4532 ? 62.360  129.835 127.430 1.00 63.71  ? 4532 ASN A OD1   1 
ATOM   22350 N  ND2   . ASN A 1 4532 ? 62.317  131.291 129.139 1.00 63.81  ? 4532 ASN A ND2   1 
ATOM   22351 N  N     . SER A 1 4533 ? 63.641  126.837 131.924 1.00 67.99  ? 4533 SER A N     1 
ATOM   22352 C  CA    . SER A 1 4533 ? 63.484  125.641 132.756 1.00 71.34  ? 4533 SER A CA    1 
ATOM   22353 C  C     . SER A 1 4533 ? 62.457  124.677 132.166 1.00 75.32  ? 4533 SER A C     1 
ATOM   22354 O  O     . SER A 1 4533 ? 61.648  124.085 132.885 1.00 75.91  ? 4533 SER A O     1 
ATOM   22355 C  CB    . SER A 1 4533 ? 63.118  126.012 134.196 1.00 70.87  ? 4533 SER A CB    1 
ATOM   22356 O  OG    . SER A 1 4533 ? 63.088  124.864 135.027 1.00 71.20  ? 4533 SER A OG    1 
ATOM   22357 N  N     . TRP A 1 4534 ? 62.488  124.517 130.848 1.00 73.54  ? 4534 TRP A N     1 
ATOM   22358 C  CA    . TRP A 1 4534 ? 61.601  123.608 130.139 1.00 73.37  ? 4534 TRP A CA    1 
ATOM   22359 C  C     . TRP A 1 4534 ? 62.376  122.392 129.645 1.00 71.86  ? 4534 TRP A C     1 
ATOM   22360 O  O     . TRP A 1 4534 ? 63.589  122.271 129.838 1.00 67.75  ? 4534 TRP A O     1 
ATOM   22361 C  CB    . TRP A 1 4534 ? 60.921  124.314 128.960 1.00 72.75  ? 4534 TRP A CB    1 
ATOM   22362 C  CG    . TRP A 1 4534 ? 59.922  125.353 129.365 1.00 75.73  ? 4534 TRP A CG    1 
ATOM   22363 C  CD1   . TRP A 1 4534 ? 59.176  125.374 130.506 1.00 75.89  ? 4534 TRP A CD1   1 
ATOM   22364 C  CD2   . TRP A 1 4534 ? 59.553  126.521 128.622 1.00 72.81  ? 4534 TRP A CD2   1 
ATOM   22365 N  NE1   . TRP A 1 4534 ? 58.369  126.485 130.523 1.00 73.32  ? 4534 TRP A NE1   1 
ATOM   22366 C  CE2   . TRP A 1 4534 ? 58.581  127.206 129.378 1.00 72.14  ? 4534 TRP A CE2   1 
ATOM   22367 C  CE3   . TRP A 1 4534 ? 59.951  127.055 127.394 1.00 71.59  ? 4534 TRP A CE3   1 
ATOM   22368 C  CZ2   . TRP A 1 4534 ? 58.002  128.397 128.945 1.00 75.18  ? 4534 TRP A CZ2   1 
ATOM   22369 C  CZ3   . TRP A 1 4534 ? 59.376  128.237 126.966 1.00 74.04  ? 4534 TRP A CZ3   1 
ATOM   22370 C  CH2   . TRP A 1 4534 ? 58.412  128.895 127.739 1.00 74.05  ? 4534 TRP A CH2   1 
ATOM   22371 N  N     . SER A 1 4535 ? 61.651  121.484 129.003 1.00 73.12  ? 4535 SER A N     1 
ATOM   22372 C  CA    . SER A 1 4535 ? 62.246  120.313 128.380 1.00 71.25  ? 4535 SER A CA    1 
ATOM   22373 C  C     . SER A 1 4535 ? 62.425  120.543 126.883 1.00 72.00  ? 4535 SER A C     1 
ATOM   22374 O  O     . SER A 1 4535 ? 61.796  121.418 126.283 1.00 71.76  ? 4535 SER A O     1 
ATOM   22375 C  CB    . SER A 1 4535 ? 61.384  119.073 128.623 1.00 73.71  ? 4535 SER A CB    1 
ATOM   22376 O  OG    . SER A 1 4535 ? 61.860  117.967 127.876 1.00 76.14  ? 4535 SER A OG    1 
ATOM   22377 N  N     . LEU A 1 4536 ? 63.309  119.742 126.282 1.00 70.16  ? 4536 LEU A N     1 
ATOM   22378 C  CA    . LEU A 1 4536 ? 63.548  119.856 124.846 1.00 68.46  ? 4536 LEU A CA    1 
ATOM   22379 C  C     . LEU A 1 4536 ? 62.293  119.521 124.051 1.00 69.71  ? 4536 LEU A C     1 
ATOM   22380 O  O     . LEU A 1 4536 ? 61.985  120.183 123.053 1.00 69.72  ? 4536 LEU A O     1 
ATOM   22381 C  CB    . LEU A 1 4536 ? 64.703  118.947 124.424 1.00 65.73  ? 4536 LEU A CB    1 
ATOM   22382 C  CG    . LEU A 1 4536 ? 66.086  119.206 125.026 1.00 57.80  ? 4536 LEU A CG    1 
ATOM   22383 C  CD1   . LEU A 1 4536 ? 66.293  118.382 126.289 1.00 61.02  ? 4536 LEU A CD1   1 
ATOM   22384 C  CD2   . LEU A 1 4536 ? 67.177  118.919 124.006 1.00 49.64  ? 4536 LEU A CD2   1 
ATOM   22385 N  N     . GLU A 1 4537 ? 61.554  118.495 124.479 1.00 71.46  ? 4537 GLU A N     1 
ATOM   22386 C  CA    . GLU A 1 4537 ? 60.348  118.080 123.776 1.00 70.95  ? 4537 GLU A CA    1 
ATOM   22387 C  C     . GLU A 1 4537 ? 59.207  119.080 123.912 1.00 71.78  ? 4537 GLU A C     1 
ATOM   22388 O  O     . GLU A 1 4537 ? 58.241  118.995 123.147 1.00 73.18  ? 4537 GLU A O     1 
ATOM   22389 C  CB    . GLU A 1 4537 ? 59.895  116.710 124.284 1.00 70.18  ? 4537 GLU A CB    1 
ATOM   22390 C  CG    . GLU A 1 4537 ? 60.944  115.621 124.135 1.00 68.45  ? 4537 GLU A CG    1 
ATOM   22391 C  CD    . GLU A 1 4537 ? 60.503  114.303 124.737 1.00 62.71  ? 4537 GLU A CD    1 
ATOM   22392 O  OE1   . GLU A 1 4537 ? 59.458  113.771 124.306 1.00 65.76  ? 4537 GLU A OE1   1 
ATOM   22393 O  OE2   . GLU A 1 4537 ? 61.200  113.800 125.643 1.00 55.57  ? 4537 GLU A OE2   1 
ATOM   22394 N  N     . GLU A 1 4538 ? 59.292  120.015 124.854 1.00 69.74  ? 4538 GLU A N     1 
ATOM   22395 C  CA    . GLU A 1 4538 ? 58.259  121.023 125.042 1.00 72.67  ? 4538 GLU A CA    1 
ATOM   22396 C  C     . GLU A 1 4538 ? 58.474  122.262 124.183 1.00 69.85  ? 4538 GLU A C     1 
ATOM   22397 O  O     . GLU A 1 4538 ? 57.653  123.183 124.235 1.00 67.14  ? 4538 GLU A O     1 
ATOM   22398 C  CB    . GLU A 1 4538 ? 58.178  121.431 126.517 1.00 75.29  ? 4538 GLU A CB    1 
ATOM   22399 C  CG    . GLU A 1 4538 ? 58.022  120.267 127.481 1.00 80.10  ? 4538 GLU A CG    1 
ATOM   22400 C  CD    . GLU A 1 4538 ? 58.252  120.674 128.923 1.00 83.47  ? 4538 GLU A CD    1 
ATOM   22401 O  OE1   . GLU A 1 4538 ? 58.557  121.861 129.165 1.00 77.89  ? 4538 GLU A OE1   1 
ATOM   22402 O  OE2   . GLU A 1 4538 ? 58.127  119.809 129.814 1.00 85.92  ? 4538 GLU A OE2   1 
ATOM   22403 N  N     . LEU A 1 4539 ? 59.549  122.310 123.401 1.00 67.25  ? 4539 LEU A N     1 
ATOM   22404 C  CA    . LEU A 1 4539 ? 59.853  123.447 122.542 1.00 59.85  ? 4539 LEU A CA    1 
ATOM   22405 C  C     . LEU A 1 4539 ? 59.586  123.078 121.091 1.00 57.20  ? 4539 LEU A C     1 
ATOM   22406 O  O     . LEU A 1 4539 ? 60.013  122.015 120.626 1.00 60.01  ? 4539 LEU A O     1 
ATOM   22407 C  CB    . LEU A 1 4539 ? 61.303  123.901 122.709 1.00 52.46  ? 4539 LEU A CB    1 
ATOM   22408 C  CG    . LEU A 1 4539 ? 61.704  124.530 124.039 1.00 53.13  ? 4539 LEU A CG    1 
ATOM   22409 C  CD1   . LEU A 1 4539 ? 63.192  124.805 124.037 1.00 53.56  ? 4539 LEU A CD1   1 
ATOM   22410 C  CD2   . LEU A 1 4539 ? 60.923  125.810 124.267 1.00 53.51  ? 4539 LEU A CD2   1 
ATOM   22411 N  N     . CYS A 1 4540 ? 58.882  123.954 120.386 1.00 53.62  ? 4540 CYS A N     1 
ATOM   22412 C  CA    . CYS A 1 4540 ? 58.696  123.853 118.949 1.00 48.91  ? 4540 CYS A CA    1 
ATOM   22413 C  C     . CYS A 1 4540 ? 59.442  124.994 118.271 1.00 51.23  ? 4540 CYS A C     1 
ATOM   22414 O  O     . CYS A 1 4540 ? 59.600  126.080 118.846 1.00 53.45  ? 4540 CYS A O     1 
ATOM   22415 C  CB    . CYS A 1 4540 ? 57.211  123.882 118.574 1.00 51.87  ? 4540 CYS A CB    1 
ATOM   22416 S  SG    . CYS A 1 4540 ? 56.350  125.414 118.983 1.00 73.30  ? 4540 CYS A SG    1 
ATOM   22417 N  N     . LEU A 1 4541 ? 59.910  124.736 117.053 1.00 46.36  ? 4541 LEU A N     1 
ATOM   22418 C  CA    . LEU A 1 4541 ? 60.750  125.686 116.340 1.00 40.97  ? 4541 LEU A CA    1 
ATOM   22419 C  C     . LEU A 1 4541 ? 59.920  126.496 115.353 1.00 40.82  ? 4541 LEU A C     1 
ATOM   22420 O  O     . LEU A 1 4541 ? 59.186  125.935 114.534 1.00 48.44  ? 4541 LEU A O     1 
ATOM   22421 C  CB    . LEU A 1 4541 ? 61.874  124.954 115.608 1.00 40.48  ? 4541 LEU A CB    1 
ATOM   22422 C  CG    . LEU A 1 4541 ? 62.841  125.821 114.802 1.00 39.13  ? 4541 LEU A CG    1 
ATOM   22423 C  CD1   . LEU A 1 4541 ? 63.433  126.908 115.683 1.00 39.02  ? 4541 LEU A CD1   1 
ATOM   22424 C  CD2   . LEU A 1 4541 ? 63.938  124.970 114.182 1.00 33.05  ? 4541 LEU A CD2   1 
ATOM   22425 N  N     . GLU A 1 4542 ? 60.039  127.817 115.436 1.00 38.87  ? 4542 GLU A N     1 
ATOM   22426 C  CA    . GLU A 1 4542 ? 59.425  128.741 114.499 1.00 36.21  ? 4542 GLU A CA    1 
ATOM   22427 C  C     . GLU A 1 4542 ? 60.519  129.382 113.660 1.00 37.05  ? 4542 GLU A C     1 
ATOM   22428 O  O     . GLU A 1 4542 ? 61.609  129.679 114.164 1.00 34.97  ? 4542 GLU A O     1 
ATOM   22429 C  CB    . GLU A 1 4542 ? 58.621  129.818 115.232 1.00 41.12  ? 4542 GLU A CB    1 
ATOM   22430 C  CG    . GLU A 1 4542 ? 57.345  129.313 115.890 1.00 48.02  ? 4542 GLU A CG    1 
ATOM   22431 C  CD    . GLU A 1 4542 ? 56.385  128.670 114.908 1.00 59.35  ? 4542 GLU A CD    1 
ATOM   22432 O  OE1   . GLU A 1 4542 ? 55.557  129.399 114.321 1.00 55.25  ? 4542 GLU A OE1   1 
ATOM   22433 O  OE2   . GLU A 1 4542 ? 56.451  127.436 114.728 1.00 56.23  ? 4542 GLU A OE2   1 
ATOM   22434 N  N     . VAL A 1 4543 ? 60.231  129.588 112.380 1.00 36.18  ? 4543 VAL A N     1 
ATOM   22435 C  CA    . VAL A 1 4543 ? 61.207  130.082 111.419 1.00 29.59  ? 4543 VAL A CA    1 
ATOM   22436 C  C     . VAL A 1 4543 ? 60.732  131.430 110.898 1.00 32.54  ? 4543 VAL A C     1 
ATOM   22437 O  O     . VAL A 1 4543 ? 59.582  131.564 110.461 1.00 38.04  ? 4543 VAL A O     1 
ATOM   22438 C  CB    . VAL A 1 4543 ? 61.410  129.084 110.267 1.00 29.93  ? 4543 VAL A CB    1 
ATOM   22439 C  CG1   . VAL A 1 4543 ? 62.061  129.766 109.078 1.00 27.07  ? 4543 VAL A CG1   1 
ATOM   22440 C  CG2   . VAL A 1 4543 ? 62.242  127.901 110.734 1.00 29.83  ? 4543 VAL A CG2   1 
ATOM   22441 N  N     . ASN A 1 4544 ? 61.613  132.426 110.948 1.00 32.26  ? 4544 ASN A N     1 
ATOM   22442 C  CA    . ASN A 1 4544 ? 61.334  133.741 110.387 1.00 31.53  ? 4544 ASN A CA    1 
ATOM   22443 C  C     . ASN A 1 4544 ? 62.391  134.061 109.342 1.00 32.53  ? 4544 ASN A C     1 
ATOM   22444 O  O     . ASN A 1 4544 ? 63.586  133.970 109.622 1.00 33.83  ? 4544 ASN A O     1 
ATOM   22445 C  CB    . ASN A 1 4544 ? 61.320  134.818 111.477 1.00 35.06  ? 4544 ASN A CB    1 
ATOM   22446 C  CG    . ASN A 1 4544 ? 61.134  136.214 110.916 1.00 42.96  ? 4544 ASN A CG    1 
ATOM   22447 O  OD1   . ASN A 1 4544 ? 60.168  136.486 110.205 1.00 41.64  ? 4544 ASN A OD1   1 
ATOM   22448 N  ND2   . ASN A 1 4544 ? 62.064  137.107 111.234 1.00 44.82  ? 4544 ASN A ND2   1 
ATOM   22449 N  N     . VAL A 1 4545 ? 61.962  134.433 108.142 1.00 34.57  ? 4545 VAL A N     1 
ATOM   22450 C  CA    . VAL A 1 4545 ? 62.877  134.775 107.060 1.00 38.09  ? 4545 VAL A CA    1 
ATOM   22451 C  C     . VAL A 1 4545 ? 62.892  136.288 106.915 1.00 43.02  ? 4545 VAL A C     1 
ATOM   22452 O  O     . VAL A 1 4545 ? 61.844  136.905 106.692 1.00 45.85  ? 4545 VAL A O     1 
ATOM   22453 C  CB    . VAL A 1 4545 ? 62.474  134.090 105.743 1.00 41.70  ? 4545 VAL A CB    1 
ATOM   22454 C  CG1   . VAL A 1 4545 ? 63.242  134.687 104.576 1.00 40.40  ? 4545 VAL A CG1   1 
ATOM   22455 C  CG2   . VAL A 1 4545 ? 62.717  132.591 105.836 1.00 30.35  ? 4545 VAL A CG2   1 
ATOM   22456 N  N     . THR A 1 4546 ? 64.074  136.887 107.043 1.00 46.43  ? 4546 THR A N     1 
ATOM   22457 C  CA    . THR A 1 4546 ? 64.199  138.335 106.984 1.00 50.03  ? 4546 THR A CA    1 
ATOM   22458 C  C     . THR A 1 4546 ? 64.644  138.774 105.595 1.00 59.46  ? 4546 THR A C     1 
ATOM   22459 O  O     . THR A 1 4546 ? 65.348  138.049 104.887 1.00 59.48  ? 4546 THR A O     1 
ATOM   22460 C  CB    . THR A 1 4546 ? 65.192  138.846 108.028 1.00 49.24  ? 4546 THR A CB    1 
ATOM   22461 O  OG1   . THR A 1 4546 ? 66.491  138.309 107.755 1.00 54.32  ? 4546 THR A OG1   1 
ATOM   22462 C  CG2   . THR A 1 4546 ? 64.761  138.425 109.424 1.00 46.04  ? 4546 THR A CG2   1 
ATOM   22463 N  N     . THR A 1 4547 ? 64.215  139.978 105.210 1.00 66.98  ? 4547 THR A N     1 
ATOM   22464 C  CA    . THR A 1 4547 ? 64.611  140.528 103.917 1.00 71.98  ? 4547 THR A CA    1 
ATOM   22465 C  C     . THR A 1 4547 ? 66.114  140.773 103.859 1.00 71.57  ? 4547 THR A C     1 
ATOM   22466 O  O     . THR A 1 4547 ? 66.753  140.507 102.834 1.00 74.09  ? 4547 THR A O     1 
ATOM   22467 C  CB    . THR A 1 4547 ? 63.844  141.822 103.641 1.00 72.68  ? 4547 THR A CB    1 
ATOM   22468 O  OG1   . THR A 1 4547 ? 62.440  141.593 103.814 1.00 75.71  ? 4547 THR A OG1   1 
ATOM   22469 C  CG2   . THR A 1 4547 ? 64.102  142.303 102.221 1.00 65.60  ? 4547 THR A CG2   1 
ATOM   22470 N  N     . SER A 1 4548 ? 66.694  141.278 104.945 1.00 69.23  ? 4548 SER A N     1 
ATOM   22471 C  CA    . SER A 1 4548 ? 68.122  141.548 105.008 1.00 72.91  ? 4548 SER A CA    1 
ATOM   22472 C  C     . SER A 1 4548 ? 68.669  141.051 106.337 1.00 73.21  ? 4548 SER A C     1 
ATOM   22473 O  O     . SER A 1 4548 ? 67.938  140.910 107.321 1.00 71.91  ? 4548 SER A O     1 
ATOM   22474 C  CB    . SER A 1 4548 ? 68.424  143.043 104.835 1.00 75.68  ? 4548 SER A CB    1 
ATOM   22475 O  OG    . SER A 1 4548 ? 67.953  143.790 105.943 1.00 76.69  ? 4548 SER A OG    1 
ATOM   22476 N  N     . GLN A 1 4549 ? 69.972  140.784 106.354 1.00 72.45  ? 4549 GLN A N     1 
ATOM   22477 C  CA    . GLN A 1 4549 ? 70.636  140.333 107.564 1.00 66.24  ? 4549 GLN A CA    1 
ATOM   22478 C  C     . GLN A 1 4549 ? 70.819  141.493 108.541 1.00 73.89  ? 4549 GLN A C     1 
ATOM   22479 O  O     . GLN A 1 4549 ? 70.632  142.666 108.205 1.00 75.56  ? 4549 GLN A O     1 
ATOM   22480 C  CB    . GLN A 1 4549 ? 71.988  139.700 107.234 1.00 59.86  ? 4549 GLN A CB    1 
ATOM   22481 C  CG    . GLN A 1 4549 ? 71.904  138.431 106.402 1.00 55.94  ? 4549 GLN A CG    1 
ATOM   22482 C  CD    . GLN A 1 4549 ? 71.931  138.704 104.912 1.00 64.07  ? 4549 GLN A CD    1 
ATOM   22483 O  OE1   . GLN A 1 4549 ? 71.818  139.849 104.476 1.00 70.37  ? 4549 GLN A OE1   1 
ATOM   22484 N  NE2   . GLN A 1 4549 ? 72.089  137.649 104.120 1.00 57.44  ? 4549 GLN A NE2   1 
ATOM   22485 N  N     . GLY A 1 4550 ? 71.192  141.149 109.771 1.00 70.92  ? 4550 GLY A N     1 
ATOM   22486 C  CA    . GLY A 1 4550 ? 71.410  142.145 110.801 1.00 74.18  ? 4550 GLY A CA    1 
ATOM   22487 C  C     . GLY A 1 4550 ? 70.126  142.738 111.343 1.00 82.86  ? 4550 GLY A C     1 
ATOM   22488 O  O     . GLY A 1 4550 ? 69.897  143.946 111.232 1.00 82.33  ? 4550 GLY A O     1 
ATOM   22489 N  N     . ALA A 1 4551 ? 69.282  141.898 111.930 1.00 86.45  ? 4551 ALA A N     1 
ATOM   22490 C  CA    . ALA A 1 4551 ? 68.017  142.319 112.511 1.00 83.23  ? 4551 ALA A CA    1 
ATOM   22491 C  C     . ALA A 1 4551 ? 68.048  142.111 114.019 1.00 82.91  ? 4551 ALA A C     1 
ATOM   22492 O  O     . ALA A 1 4551 ? 69.021  141.604 114.584 1.00 80.76  ? 4551 ALA A O     1 
ATOM   22493 C  CB    . ALA A 1 4551 ? 66.841  141.556 111.888 1.00 72.21  ? 4551 ALA A CB    1 
ATOM   22494 N  N     . THR A 1 4552 ? 66.962  142.515 114.673 1.00 85.69  ? 4552 THR A N     1 
ATOM   22495 C  CA    . THR A 1 4552 ? 66.855  142.371 116.120 1.00 85.44  ? 4552 THR A CA    1 
ATOM   22496 C  C     . THR A 1 4552 ? 66.676  140.902 116.481 1.00 79.20  ? 4552 THR A C     1 
ATOM   22497 O  O     . THR A 1 4552 ? 65.724  140.255 116.030 1.00 76.97  ? 4552 THR A O     1 
ATOM   22498 C  CB    . THR A 1 4552 ? 65.688  143.199 116.651 1.00 84.78  ? 4552 THR A CB    1 
ATOM   22499 O  OG1   . THR A 1 4552 ? 64.463  142.727 116.077 1.00 83.49  ? 4552 THR A OG1   1 
ATOM   22500 C  CG2   . THR A 1 4552 ? 65.874  144.668 116.300 1.00 79.85  ? 4552 THR A CG2   1 
ATOM   22501 N  N     . LEU A 1 4553 ? 67.588  140.376 117.293 1.00 76.43  ? 4553 LEU A N     1 
ATOM   22502 C  CA    . LEU A 1 4553 ? 67.554  138.983 117.718 1.00 72.70  ? 4553 LEU A CA    1 
ATOM   22503 C  C     . LEU A 1 4553 ? 66.961  138.900 119.119 1.00 73.95  ? 4553 LEU A C     1 
ATOM   22504 O  O     . LEU A 1 4553 ? 67.500  139.488 120.062 1.00 75.11  ? 4553 LEU A O     1 
ATOM   22505 C  CB    . LEU A 1 4553 ? 68.953  138.368 117.691 1.00 69.80  ? 4553 LEU A CB    1 
ATOM   22506 C  CG    . LEU A 1 4553 ? 69.434  137.809 116.351 1.00 68.24  ? 4553 LEU A CG    1 
ATOM   22507 C  CD1   . LEU A 1 4553 ? 70.702  136.992 116.539 1.00 59.18  ? 4553 LEU A CD1   1 
ATOM   22508 C  CD2   . LEU A 1 4553 ? 68.347  136.971 115.696 1.00 56.15  ? 4553 LEU A CD2   1 
ATOM   22509 N  N     . ASP A 1 4554 ? 65.856  138.171 119.249 1.00 70.93  ? 4554 ASP A N     1 
ATOM   22510 C  CA    . ASP A 1 4554 ? 65.249  137.954 120.551 1.00 65.52  ? 4554 ASP A CA    1 
ATOM   22511 C  C     . ASP A 1 4554 ? 66.115  137.004 121.377 1.00 64.19  ? 4554 ASP A C     1 
ATOM   22512 O  O     . ASP A 1 4554 ? 66.997  136.314 120.858 1.00 65.28  ? 4554 ASP A O     1 
ATOM   22513 C  CB    . ASP A 1 4554 ? 63.834  137.394 120.389 1.00 65.21  ? 4554 ASP A CB    1 
ATOM   22514 C  CG    . ASP A 1 4554 ? 63.044  137.397 121.687 1.00 73.07  ? 4554 ASP A CG    1 
ATOM   22515 O  OD1   . ASP A 1 4554 ? 63.596  137.811 122.728 1.00 74.36  ? 4554 ASP A OD1   1 
ATOM   22516 O  OD2   . ASP A 1 4554 ? 61.865  136.985 121.664 1.00 75.88  ? 4554 ASP A OD2   1 
ATOM   22517 N  N     . ALA A 1 4555 ? 65.856  136.981 122.687 1.00 66.03  ? 4555 ALA A N     1 
ATOM   22518 C  CA    . ALA A 1 4555 ? 66.622  136.117 123.579 1.00 61.37  ? 4555 ALA A CA    1 
ATOM   22519 C  C     . ALA A 1 4555 ? 66.447  134.647 123.215 1.00 61.27  ? 4555 ALA A C     1 
ATOM   22520 O  O     . ALA A 1 4555 ? 67.342  133.829 123.459 1.00 58.72  ? 4555 ALA A O     1 
ATOM   22521 C  CB    . ALA A 1 4555 ? 66.212  136.364 125.030 1.00 52.94  ? 4555 ALA A CB    1 
ATOM   22522 N  N     . CYS A 1 4556 ? 65.302  134.293 122.633 1.00 62.01  ? 4556 CYS A N     1 
ATOM   22523 C  CA    . CYS A 1 4556 ? 65.016  132.926 122.221 1.00 58.39  ? 4556 CYS A CA    1 
ATOM   22524 C  C     . CYS A 1 4556 ? 65.195  132.716 120.720 1.00 54.71  ? 4556 CYS A C     1 
ATOM   22525 O  O     . CYS A 1 4556 ? 64.772  131.683 120.191 1.00 45.64  ? 4556 CYS A O     1 
ATOM   22526 C  CB    . CYS A 1 4556 ? 63.599  132.535 122.643 1.00 54.46  ? 4556 CYS A CB    1 
ATOM   22527 S  SG    . CYS A 1 4556 ? 62.344  133.787 122.287 1.00 77.18  ? 4556 CYS A SG    1 
ATOM   22528 N  N     . SER A 1 4557 ? 65.814  133.669 120.026 1.00 53.48  ? 4557 SER A N     1 
ATOM   22529 C  CA    . SER A 1 4557 ? 65.985  133.601 118.583 1.00 44.38  ? 4557 SER A CA    1 
ATOM   22530 C  C     . SER A 1 4557 ? 67.464  133.551 118.226 1.00 49.04  ? 4557 SER A C     1 
ATOM   22531 O  O     . SER A 1 4557 ? 68.297  134.203 118.861 1.00 56.70  ? 4557 SER A O     1 
ATOM   22532 C  CB    . SER A 1 4557 ? 65.325  134.798 117.889 1.00 49.06  ? 4557 SER A CB    1 
ATOM   22533 O  OG    . SER A 1 4557 ? 63.918  134.639 117.825 1.00 56.41  ? 4557 SER A OG    1 
ATOM   22534 N  N     . PHE A 1 4558 ? 67.780  132.770 117.196 1.00 40.80  ? 4558 PHE A N     1 
ATOM   22535 C  CA    . PHE A 1 4558 ? 69.144  132.614 116.713 1.00 39.46  ? 4558 PHE A CA    1 
ATOM   22536 C  C     . PHE A 1 4558 ? 69.186  132.870 115.214 1.00 35.35  ? 4558 PHE A C     1 
ATOM   22537 O  O     . PHE A 1 4558 ? 68.280  132.464 114.481 1.00 37.10  ? 4558 PHE A O     1 
ATOM   22538 C  CB    . PHE A 1 4558 ? 69.692  131.214 117.020 1.00 32.05  ? 4558 PHE A CB    1 
ATOM   22539 C  CG    . PHE A 1 4558 ? 69.562  130.815 118.462 1.00 37.78  ? 4558 PHE A CG    1 
ATOM   22540 C  CD1   . PHE A 1 4558 ? 70.596  131.046 119.353 1.00 40.09  ? 4558 PHE A CD1   1 
ATOM   22541 C  CD2   . PHE A 1 4558 ? 68.409  130.204 118.924 1.00 41.44  ? 4558 PHE A CD2   1 
ATOM   22542 C  CE1   . PHE A 1 4558 ? 70.480  130.678 120.680 1.00 41.51  ? 4558 PHE A CE1   1 
ATOM   22543 C  CE2   . PHE A 1 4558 ? 68.287  129.835 120.249 1.00 40.43  ? 4558 PHE A CE2   1 
ATOM   22544 C  CZ    . PHE A 1 4558 ? 69.324  130.072 121.128 1.00 39.87  ? 4558 PHE A CZ    1 
ATOM   22545 N  N     . GLY A 1 4559 ? 70.245  133.537 114.761 1.00 38.66  ? 4559 GLY A N     1 
ATOM   22546 C  CA    . GLY A 1 4559 ? 70.397  133.889 113.360 1.00 36.90  ? 4559 GLY A CA    1 
ATOM   22547 C  C     . GLY A 1 4559 ? 71.199  132.839 112.612 1.00 31.13  ? 4559 GLY A C     1 
ATOM   22548 O  O     . GLY A 1 4559 ? 72.243  132.385 113.085 1.00 37.41  ? 4559 GLY A O     1 
ATOM   22549 N  N     . VAL A 1 4560 ? 70.695  132.461 111.439 1.00 29.26  ? 4560 VAL A N     1 
ATOM   22550 C  CA    . VAL A 1 4560 ? 71.322  131.459 110.588 1.00 27.54  ? 4560 VAL A CA    1 
ATOM   22551 C  C     . VAL A 1 4560 ? 71.433  132.023 109.178 1.00 25.94  ? 4560 VAL A C     1 
ATOM   22552 O  O     . VAL A 1 4560 ? 70.488  132.636 108.668 1.00 32.66  ? 4560 VAL A O     1 
ATOM   22553 C  CB    . VAL A 1 4560 ? 70.525  130.136 110.593 1.00 26.82  ? 4560 VAL A CB    1 
ATOM   22554 C  CG1   . VAL A 1 4560 ? 70.939  129.245 109.432 1.00 27.67  ? 4560 VAL A CG1   1 
ATOM   22555 C  CG2   . VAL A 1 4560 ? 70.708  129.412 111.918 1.00 28.25  ? 4560 VAL A CG2   1 
ATOM   22556 N  N     . THR A 1 4561 ? 72.593  131.829 108.555 1.00 26.40  ? 4561 THR A N     1 
ATOM   22557 C  CA    . THR A 1 4561 ? 72.843  132.276 107.194 1.00 31.38  ? 4561 THR A CA    1 
ATOM   22558 C  C     . THR A 1 4561 ? 73.193  131.084 106.313 1.00 29.29  ? 4561 THR A C     1 
ATOM   22559 O  O     . THR A 1 4561 ? 73.585  130.018 106.796 1.00 28.93  ? 4561 THR A O     1 
ATOM   22560 C  CB    . THR A 1 4561 ? 73.978  133.310 107.138 1.00 31.58  ? 4561 THR A CB    1 
ATOM   22561 O  OG1   . THR A 1 4561 ? 75.242  132.641 107.236 1.00 31.24  ? 4561 THR A OG1   1 
ATOM   22562 C  CG2   . THR A 1 4561 ? 73.852  134.312 108.275 1.00 34.72  ? 4561 THR A CG2   1 
ATOM   22563 N  N     . GLY A 1 4562 ? 73.036  131.273 105.004 1.00 27.49  ? 4562 GLY A N     1 
ATOM   22564 C  CA    . GLY A 1 4562 ? 73.417  130.272 104.032 1.00 24.82  ? 4562 GLY A CA    1 
ATOM   22565 C  C     . GLY A 1 4562 ? 72.344  129.274 103.655 1.00 28.20  ? 4562 GLY A C     1 
ATOM   22566 O  O     . GLY A 1 4562 ? 72.588  128.434 102.779 1.00 30.25  ? 4562 GLY A O     1 
ATOM   22567 N  N     . LEU A 1 4563 ? 71.171  129.330 104.281 1.00 26.81  ? 4563 LEU A N     1 
ATOM   22568 C  CA    . LEU A 1 4563 ? 70.093  128.417 103.923 1.00 21.82  ? 4563 LEU A CA    1 
ATOM   22569 C  C     . LEU A 1 4563 ? 69.586  128.728 102.520 1.00 24.30  ? 4563 LEU A C     1 
ATOM   22570 O  O     . LEU A 1 4563 ? 69.316  129.886 102.187 1.00 25.65  ? 4563 LEU A O     1 
ATOM   22571 C  CB    . LEU A 1 4563 ? 68.954  128.516 104.936 1.00 23.10  ? 4563 LEU A CB    1 
ATOM   22572 C  CG    . LEU A 1 4563 ? 69.259  128.027 106.353 1.00 23.02  ? 4563 LEU A CG    1 
ATOM   22573 C  CD1   . LEU A 1 4563 ? 67.993  127.995 107.194 1.00 22.26  ? 4563 LEU A CD1   1 
ATOM   22574 C  CD2   . LEU A 1 4563 ? 69.919  126.658 106.320 1.00 18.39  ? 4563 LEU A CD2   1 
ATOM   22575 N  N     . LYS A 1 4564 ? 69.458  127.692 101.698 1.00 22.80  ? 4564 LYS A N     1 
ATOM   22576 C  CA    . LYS A 1 4564 ? 69.033  127.828 100.311 1.00 20.90  ? 4564 LYS A CA    1 
ATOM   22577 C  C     . LYS A 1 4564 ? 67.712  127.095 100.127 1.00 17.93  ? 4564 LYS A C     1 
ATOM   22578 O  O     . LYS A 1 4564 ? 67.638  125.882 100.345 1.00 17.31  ? 4564 LYS A O     1 
ATOM   22579 C  CB    . LYS A 1 4564 ? 70.093  127.275 99.359  1.00 20.57  ? 4564 LYS A CB    1 
ATOM   22580 C  CG    . LYS A 1 4564 ? 71.402  128.049 99.363  1.00 27.89  ? 4564 LYS A CG    1 
ATOM   22581 C  CD    . LYS A 1 4564 ? 71.205  129.476 98.884  1.00 31.47  ? 4564 LYS A CD    1 
ATOM   22582 C  CE    . LYS A 1 4564 ? 72.537  130.179 98.678  1.00 32.49  ? 4564 LYS A CE    1 
ATOM   22583 N  NZ    . LYS A 1 4564 ? 73.323  130.273 99.938  1.00 34.23  ? 4564 LYS A NZ    1 
ATOM   22584 N  N     . LEU A 1 4565 ? 66.679  127.828 99.730  1.00 16.67  ? 4565 LEU A N     1 
ATOM   22585 C  CA    . LEU A 1 4565 ? 65.361  127.259 99.502  1.00 15.57  ? 4565 LEU A CA    1 
ATOM   22586 C  C     . LEU A 1 4565 ? 65.294  126.682 98.094  1.00 17.58  ? 4565 LEU A C     1 
ATOM   22587 O  O     . LEU A 1 4565 ? 65.464  127.409 97.110  1.00 20.19  ? 4565 LEU A O     1 
ATOM   22588 C  CB    . LEU A 1 4565 ? 64.291  128.332 99.700  1.00 15.46  ? 4565 LEU A CB    1 
ATOM   22589 C  CG    . LEU A 1 4565 ? 62.820  127.959 99.542  1.00 15.82  ? 4565 LEU A CG    1 
ATOM   22590 C  CD1   . LEU A 1 4565 ? 62.461  126.775 100.421 1.00 13.72  ? 4565 LEU A CD1   1 
ATOM   22591 C  CD2   . LEU A 1 4565 ? 61.968  129.165 99.883  1.00 18.89  ? 4565 LEU A CD2   1 
ATOM   22592 N  N     . GLN A 1 4566 ? 65.068  125.374 98.001  1.00 14.46  ? 4566 GLN A N     1 
ATOM   22593 C  CA    . GLN A 1 4566 ? 65.002  124.670 96.728  1.00 15.25  ? 4566 GLN A CA    1 
ATOM   22594 C  C     . GLN A 1 4566 ? 63.540  124.458 96.356  1.00 14.66  ? 4566 GLN A C     1 
ATOM   22595 O  O     . GLN A 1 4566 ? 62.800  123.785 97.086  1.00 11.99  ? 4566 GLN A O     1 
ATOM   22596 C  CB    . GLN A 1 4566 ? 65.728  123.328 96.809  1.00 14.13  ? 4566 GLN A CB    1 
ATOM   22597 C  CG    . GLN A 1 4566 ? 67.071  123.387 97.512  1.00 17.10  ? 4566 GLN A CG    1 
ATOM   22598 C  CD    . GLN A 1 4566 ? 68.104  124.185 96.744  1.00 23.92  ? 4566 GLN A CD    1 
ATOM   22599 O  OE1   . GLN A 1 4566 ? 68.599  125.204 97.223  1.00 20.05  ? 4566 GLN A OE1   1 
ATOM   22600 N  NE2   . GLN A 1 4566 ? 68.439  123.721 95.546  1.00 29.51  ? 4566 GLN A NE2   1 
ATOM   22601 N  N     . GLY A 1 4567 ? 63.137  125.023 95.218  1.00 15.54  ? 4567 GLY A N     1 
ATOM   22602 C  CA    . GLY A 1 4567 ? 61.802  124.844 94.691  1.00 15.42  ? 4567 GLY A CA    1 
ATOM   22603 C  C     . GLY A 1 4567 ? 60.781  125.875 95.110  1.00 16.84  ? 4567 GLY A C     1 
ATOM   22604 O  O     . GLY A 1 4567 ? 59.627  125.785 94.675  1.00 17.21  ? 4567 GLY A O     1 
ATOM   22605 N  N     . ALA A 1 4568 ? 61.155  126.855 95.931  1.00 19.49  ? 4568 ALA A N     1 
ATOM   22606 C  CA    . ALA A 1 4568 ? 60.189  127.814 96.448  1.00 17.26  ? 4568 ALA A CA    1 
ATOM   22607 C  C     . ALA A 1 4568 ? 60.823  129.193 96.544  1.00 19.81  ? 4568 ALA A C     1 
ATOM   22608 O  O     . ALA A 1 4568 ? 62.039  129.357 96.413  1.00 28.87  ? 4568 ALA A O     1 
ATOM   22609 C  CB    . ALA A 1 4568 ? 59.650  127.383 97.816  1.00 17.27  ? 4568 ALA A CB    1 
ATOM   22610 N  N     . THR A 1 4569 ? 59.970  130.190 96.769  1.00 22.17  ? 4569 THR A N     1 
ATOM   22611 C  CA    . THR A 1 4569 ? 60.394  131.542 97.102  1.00 26.45  ? 4569 THR A CA    1 
ATOM   22612 C  C     . THR A 1 4569 ? 59.704  131.979 98.386  1.00 26.48  ? 4569 THR A C     1 
ATOM   22613 O  O     . THR A 1 4569 ? 58.552  131.618 98.643  1.00 25.05  ? 4569 THR A O     1 
ATOM   22614 C  CB    . THR A 1 4569 ? 60.075  132.539 95.978  1.00 26.21  ? 4569 THR A CB    1 
ATOM   22615 O  OG1   . THR A 1 4569 ? 58.716  132.373 95.556  1.00 26.35  ? 4569 THR A OG1   1 
ATOM   22616 C  CG2   . THR A 1 4569 ? 61.008  132.331 94.793  1.00 26.74  ? 4569 THR A CG2   1 
ATOM   22617 N  N     . CYS A 1 4570 ? 60.415  132.758 99.195  1.00 33.03  ? 4570 CYS A N     1 
ATOM   22618 C  CA    . CYS A 1 4570 ? 59.921  133.190 100.496 1.00 28.85  ? 4570 CYS A CA    1 
ATOM   22619 C  C     . CYS A 1 4570 ? 59.849  134.711 100.530 1.00 30.73  ? 4570 CYS A C     1 
ATOM   22620 O  O     . CYS A 1 4570 ? 60.879  135.389 100.451 1.00 42.05  ? 4570 CYS A O     1 
ATOM   22621 C  CB    . CYS A 1 4570 ? 60.813  132.666 101.621 1.00 28.71  ? 4570 CYS A CB    1 
ATOM   22622 S  SG    . CYS A 1 4570 ? 60.131  132.900 103.277 1.00 44.83  ? 4570 CYS A SG    1 
ATOM   22623 N  N     . ASN A 1 4571 ? 58.633  135.235 100.651 1.00 30.57  ? 4571 ASN A N     1 
ATOM   22624 C  CA    . ASN A 1 4571 ? 58.378  136.664 100.779 1.00 38.32  ? 4571 ASN A CA    1 
ATOM   22625 C  C     . ASN A 1 4571 ? 57.576  136.876 102.051 1.00 41.76  ? 4571 ASN A C     1 
ATOM   22626 O  O     . ASN A 1 4571 ? 56.486  136.314 102.188 1.00 41.27  ? 4571 ASN A O     1 
ATOM   22627 C  CB    . ASN A 1 4571 ? 57.601  137.194 99.571  1.00 39.85  ? 4571 ASN A CB    1 
ATOM   22628 C  CG    . ASN A 1 4571 ? 58.496  137.539 98.404  1.00 42.63  ? 4571 ASN A CG    1 
ATOM   22629 O  OD1   . ASN A 1 4571 ? 58.998  136.655 97.710  1.00 38.54  ? 4571 ASN A OD1   1 
ATOM   22630 N  ND2   . ASN A 1 4571 ? 58.691  138.830 98.170  1.00 44.08  ? 4571 ASN A ND2   1 
ATOM   22631 N  N     . ASN A 1 4572 ? 58.100  137.691 102.968 1.00 44.08  ? 4572 ASN A N     1 
ATOM   22632 C  CA    . ASN A 1 4572 ? 57.420  137.999 104.231 1.00 47.61  ? 4572 ASN A CA    1 
ATOM   22633 C  C     . ASN A 1 4572 ? 57.133  136.735 105.041 1.00 43.88  ? 4572 ASN A C     1 
ATOM   22634 O  O     . ASN A 1 4572 ? 56.058  136.588 105.626 1.00 40.72  ? 4572 ASN A O     1 
ATOM   22635 C  CB    . ASN A 1 4572 ? 56.123  138.776 103.987 1.00 52.25  ? 4572 ASN A CB    1 
ATOM   22636 C  CG    . ASN A 1 4572 ? 56.367  140.199 103.530 1.00 54.94  ? 4572 ASN A CG    1 
ATOM   22637 O  OD1   . ASN A 1 4572 ? 57.277  140.874 104.013 1.00 53.59  ? 4572 ASN A OD1   1 
ATOM   22638 N  ND2   . ASN A 1 4572 ? 55.552  140.664 102.590 1.00 52.83  ? 4572 ASN A ND2   1 
ATOM   22639 N  N     . ASN A 1 4573 ? 58.107  135.819 105.089 1.00 42.94  ? 4573 ASN A N     1 
ATOM   22640 C  CA    . ASN A 1 4573 ? 57.912  134.499 105.694 1.00 40.78  ? 4573 ASN A CA    1 
ATOM   22641 C  C     . ASN A 1 4573 ? 56.709  133.788 105.079 1.00 41.06  ? 4573 ASN A C     1 
ATOM   22642 O  O     . ASN A 1 4573 ? 55.920  133.145 105.776 1.00 42.11  ? 4573 ASN A O     1 
ATOM   22643 C  CB    . ASN A 1 4573 ? 57.771  134.596 107.216 1.00 34.14  ? 4573 ASN A CB    1 
ATOM   22644 C  CG    . ASN A 1 4573 ? 58.317  133.382 107.932 1.00 38.15  ? 4573 ASN A CG    1 
ATOM   22645 O  OD1   . ASN A 1 4573 ? 59.244  132.732 107.452 1.00 35.17  ? 4573 ASN A OD1   1 
ATOM   22646 N  ND2   . ASN A 1 4573 ? 57.751  133.073 109.093 1.00 41.99  ? 4573 ASN A ND2   1 
ATOM   22647 N  N     . LYS A 1 4574 ? 56.574  133.913 103.762 1.00 42.71  ? 4574 LYS A N     1 
ATOM   22648 C  CA    . LYS A 1 4574 ? 55.436  133.418 103.001 1.00 39.57  ? 4574 LYS A CA    1 
ATOM   22649 C  C     . LYS A 1 4574 ? 55.991  132.623 101.829 1.00 33.42  ? 4574 LYS A C     1 
ATOM   22650 O  O     . LYS A 1 4574 ? 56.630  133.201 100.948 1.00 34.85  ? 4574 LYS A O     1 
ATOM   22651 C  CB    . LYS A 1 4574 ? 54.581  134.585 102.488 1.00 47.11  ? 4574 LYS A CB    1 
ATOM   22652 C  CG    . LYS A 1 4574 ? 53.955  135.494 103.556 1.00 49.78  ? 4574 LYS A CG    1 
ATOM   22653 C  CD    . LYS A 1 4574 ? 52.971  134.790 104.452 1.00 51.82  ? 4574 LYS A CD    1 
ATOM   22654 C  CE    . LYS A 1 4574 ? 51.751  134.398 103.660 1.00 50.90  ? 4574 LYS A CE    1 
ATOM   22655 N  NZ    . LYS A 1 4574 ? 51.010  135.591 103.149 1.00 64.94  ? 4574 LYS A NZ    1 
ATOM   22656 N  N     . LEU A 1 4575 ? 55.766  131.310 101.813 1.00 36.95  ? 4575 LEU A N     1 
ATOM   22657 C  CA    . LEU A 1 4575 ? 56.286  130.504 100.713 1.00 28.78  ? 4575 LEU A CA    1 
ATOM   22658 C  C     . LEU A 1 4575 ? 55.327  130.470 99.532  1.00 27.77  ? 4575 LEU A C     1 
ATOM   22659 O  O     . LEU A 1 4575 ? 54.104  130.438 99.695  1.00 33.18  ? 4575 LEU A O     1 
ATOM   22660 C  CB    . LEU A 1 4575 ? 56.590  129.069 101.142 1.00 19.79  ? 4575 LEU A CB    1 
ATOM   22661 C  CG    . LEU A 1 4575 ? 57.691  128.780 102.156 1.00 22.87  ? 4575 LEU A CG    1 
ATOM   22662 C  CD1   . LEU A 1 4575 ? 57.925  127.281 102.212 1.00 20.57  ? 4575 LEU A CD1   1 
ATOM   22663 C  CD2   . LEU A 1 4575 ? 58.969  129.512 101.802 1.00 21.93  ? 4575 LEU A CD2   1 
ATOM   22664 N  N     . SER A 1 4576 ? 55.907  130.477 98.336  1.00 24.91  ? 4576 SER A N     1 
ATOM   22665 C  CA    . SER A 1 4576 ? 55.183  130.282 97.092  1.00 25.92  ? 4576 SER A CA    1 
ATOM   22666 C  C     . SER A 1 4576 ? 55.986  129.351 96.196  1.00 23.18  ? 4576 SER A C     1 
ATOM   22667 O  O     . SER A 1 4576 ? 57.221  129.326 96.248  1.00 22.86  ? 4576 SER A O     1 
ATOM   22668 C  CB    . SER A 1 4576 ? 54.923  131.613 96.373  1.00 28.39  ? 4576 SER A CB    1 
ATOM   22669 O  OG    . SER A 1 4576 ? 56.133  132.182 95.910  1.00 33.52  ? 4576 SER A OG    1 
ATOM   22670 N  N     . LEU A 1 4577 ? 55.274  128.576 95.379  1.00 29.18  ? 4577 LEU A N     1 
ATOM   22671 C  CA    . LEU A 1 4577 ? 55.934  127.678 94.441  1.00 23.34  ? 4577 LEU A CA    1 
ATOM   22672 C  C     . LEU A 1 4577 ? 56.733  128.487 93.427  1.00 22.10  ? 4577 LEU A C     1 
ATOM   22673 O  O     . LEU A 1 4577 ? 56.282  129.529 92.945  1.00 24.25  ? 4577 LEU A O     1 
ATOM   22674 C  CB    . LEU A 1 4577 ? 54.909  126.801 93.716  1.00 27.16  ? 4577 LEU A CB    1 
ATOM   22675 C  CG    . LEU A 1 4577 ? 54.294  125.602 94.448  1.00 25.13  ? 4577 LEU A CG    1 
ATOM   22676 C  CD1   . LEU A 1 4577 ? 53.207  124.957 93.599  1.00 27.67  ? 4577 LEU A CD1   1 
ATOM   22677 C  CD2   . LEU A 1 4577 ? 55.332  124.573 94.836  1.00 16.95  ? 4577 LEU A CD2   1 
ATOM   22678 N  N     . SER A 1 4578 ? 57.929  128.004 93.107  1.00 18.30  ? 4578 SER A N     1 
ATOM   22679 C  CA    . SER A 1 4578 ? 58.828  128.702 92.204  1.00 20.51  ? 4578 SER A CA    1 
ATOM   22680 C  C     . SER A 1 4578 ? 59.381  127.738 91.167  1.00 26.16  ? 4578 SER A C     1 
ATOM   22681 O  O     . SER A 1 4578 ? 59.573  126.549 91.437  1.00 30.66  ? 4578 SER A O     1 
ATOM   22682 C  CB    . SER A 1 4578 ? 59.986  129.360 92.966  1.00 25.53  ? 4578 SER A CB    1 
ATOM   22683 O  OG    . SER A 1 4578 ? 61.001  129.791 92.078  1.00 24.23  ? 4578 SER A OG    1 
ATOM   22684 N  N     . ASN A 1 4579 ? 59.639  128.268 89.974  1.00 26.89  ? 4579 ASN A N     1 
ATOM   22685 C  CA    . ASN A 1 4579 ? 60.285  127.516 88.909  1.00 25.95  ? 4579 ASN A CA    1 
ATOM   22686 C  C     . ASN A 1 4579 ? 61.802  127.629 88.950  1.00 27.61  ? 4579 ASN A C     1 
ATOM   22687 O  O     . ASN A 1 4579 ? 62.477  127.037 88.101  1.00 29.32  ? 4579 ASN A O     1 
ATOM   22688 C  CB    . ASN A 1 4579 ? 59.768  127.983 87.544  1.00 28.58  ? 4579 ASN A CB    1 
ATOM   22689 C  CG    . ASN A 1 4579 ? 58.355  127.511 87.265  1.00 40.95  ? 4579 ASN A CG    1 
ATOM   22690 O  OD1   . ASN A 1 4579 ? 57.915  126.489 87.792  1.00 35.48  ? 4579 ASN A OD1   1 
ATOM   22691 N  ND2   . ASN A 1 4579 ? 57.635  128.254 86.433  1.00 50.31  ? 4579 ASN A ND2   1 
ATOM   22692 N  N     . ALA A 1 4580 ? 62.351  128.369 89.909  1.00 27.29  ? 4580 ALA A N     1 
ATOM   22693 C  CA    . ALA A 1 4580 ? 63.791  128.482 90.059  1.00 23.93  ? 4580 ALA A CA    1 
ATOM   22694 C  C     . ALA A 1 4580 ? 64.338  127.302 90.856  1.00 26.98  ? 4580 ALA A C     1 
ATOM   22695 O  O     . ALA A 1 4580 ? 63.615  126.622 91.589  1.00 32.49  ? 4580 ALA A O     1 
ATOM   22696 C  CB    . ALA A 1 4580 ? 64.161  129.798 90.743  1.00 19.06  ? 4580 ALA A CB    1 
ATOM   22697 N  N     . ILE A 1 4581 ? 65.639  127.065 90.706  1.00 28.52  ? 4581 ILE A N     1 
ATOM   22698 C  CA    . ILE A 1 4581 ? 66.273  125.926 91.365  1.00 29.47  ? 4581 ILE A CA    1 
ATOM   22699 C  C     . ILE A 1 4581 ? 66.562  126.242 92.828  1.00 29.76  ? 4581 ILE A C     1 
ATOM   22700 O  O     . ILE A 1 4581 ? 66.076  125.559 93.737  1.00 31.29  ? 4581 ILE A O     1 
ATOM   22701 C  CB    . ILE A 1 4581 ? 67.553  125.514 90.616  1.00 29.04  ? 4581 ILE A CB    1 
ATOM   22702 C  CG1   . ILE A 1 4581 ? 67.223  125.129 89.172  1.00 27.55  ? 4581 ILE A CG1   1 
ATOM   22703 C  CG2   . ILE A 1 4581 ? 68.245  124.367 91.334  1.00 27.65  ? 4581 ILE A CG2   1 
ATOM   22704 C  CD1   . ILE A 1 4581 ? 66.276  123.956 89.055  1.00 26.40  ? 4581 ILE A CD1   1 
ATOM   22705 N  N     . SER A 1 4582 ? 67.357  127.280 93.076  1.00 30.88  ? 4582 SER A N     1 
ATOM   22706 C  CA    . SER A 1 4582 ? 67.746  127.660 94.426  1.00 28.82  ? 4582 SER A CA    1 
ATOM   22707 C  C     . SER A 1 4582 ? 67.493  129.145 94.626  1.00 32.25  ? 4582 SER A C     1 
ATOM   22708 O  O     . SER A 1 4582 ? 67.760  129.950 93.728  1.00 35.98  ? 4582 SER A O     1 
ATOM   22709 C  CB    . SER A 1 4582 ? 69.220  127.337 94.690  1.00 25.34  ? 4582 SER A CB    1 
ATOM   22710 O  OG    . SER A 1 4582 ? 69.458  125.943 94.616  1.00 32.21  ? 4582 SER A OG    1 
ATOM   22711 N  N     . THR A 1 4583 ? 66.980  129.503 95.800  1.00 29.61  ? 4583 THR A N     1 
ATOM   22712 C  CA    . THR A 1 4583 ? 66.766  130.893 96.182  1.00 29.05  ? 4583 THR A CA    1 
ATOM   22713 C  C     . THR A 1 4583 ? 67.439  131.125 97.526  1.00 30.43  ? 4583 THR A C     1 
ATOM   22714 O  O     . THR A 1 4583 ? 67.211  130.368 98.475  1.00 29.67  ? 4583 THR A O     1 
ATOM   22715 C  CB    . THR A 1 4583 ? 65.274  131.223 96.256  1.00 33.24  ? 4583 THR A CB    1 
ATOM   22716 O  OG1   . THR A 1 4583 ? 64.737  131.316 94.931  1.00 38.74  ? 4583 THR A OG1   1 
ATOM   22717 C  CG2   . THR A 1 4583 ? 65.059  132.545 96.969  1.00 31.64  ? 4583 THR A CG2   1 
ATOM   22718 N  N     . ALA A 1 4584 ? 68.271  132.158 97.606  1.00 40.07  ? 4584 ALA A N     1 
ATOM   22719 C  CA    . ALA A 1 4584 ? 69.003  132.441 98.832  1.00 33.98  ? 4584 ALA A CA    1 
ATOM   22720 C  C     . ALA A 1 4584 ? 68.066  132.996 99.898  1.00 36.58  ? 4584 ALA A C     1 
ATOM   22721 O  O     . ALA A 1 4584 ? 67.277  133.907 99.632  1.00 37.86  ? 4584 ALA A O     1 
ATOM   22722 C  CB    . ALA A 1 4584 ? 70.137  133.427 98.559  1.00 36.19  ? 4584 ALA A CB    1 
ATOM   22723 N  N     . LEU A 1 4585 ? 68.153  132.439 101.104 1.00 31.56  ? 4585 LEU A N     1 
ATOM   22724 C  CA    . LEU A 1 4585 ? 67.456  132.997 102.254 1.00 35.12  ? 4585 LEU A CA    1 
ATOM   22725 C  C     . LEU A 1 4585 ? 68.411  133.907 103.014 1.00 40.27  ? 4585 LEU A C     1 
ATOM   22726 O  O     . LEU A 1 4585 ? 69.421  133.420 103.540 1.00 41.95  ? 4585 LEU A O     1 
ATOM   22727 C  CB    . LEU A 1 4585 ? 66.944  131.893 103.165 1.00 33.31  ? 4585 LEU A CB    1 
ATOM   22728 C  CG    . LEU A 1 4585 ? 66.041  130.834 102.527 1.00 29.22  ? 4585 LEU A CG    1 
ATOM   22729 C  CD1   . LEU A 1 4585 ? 65.771  129.699 103.502 1.00 24.50  ? 4585 LEU A CD1   1 
ATOM   22730 C  CD2   . LEU A 1 4585 ? 64.738  131.453 102.051 1.00 27.81  ? 4585 LEU A CD2   1 
ATOM   22731 N  N     . PRO A 1 4586 ? 68.148  135.218 103.086 1.00 46.44  ? 4586 PRO A N     1 
ATOM   22732 C  CA    . PRO A 1 4586 ? 69.131  136.146 103.669 1.00 45.55  ? 4586 PRO A CA    1 
ATOM   22733 C  C     . PRO A 1 4586 ? 69.504  135.823 105.107 1.00 42.14  ? 4586 PRO A C     1 
ATOM   22734 O  O     . PRO A 1 4586 ? 70.680  135.591 105.407 1.00 47.58  ? 4586 PRO A O     1 
ATOM   22735 C  CB    . PRO A 1 4586 ? 68.427  137.506 103.571 1.00 51.48  ? 4586 PRO A CB    1 
ATOM   22736 C  CG    . PRO A 1 4586 ? 67.424  137.338 102.475 1.00 49.14  ? 4586 PRO A CG    1 
ATOM   22737 C  CD    . PRO A 1 4586 ? 66.963  135.918 102.563 1.00 41.98  ? 4586 PRO A CD    1 
ATOM   22738 N  N     . LEU A 1 4587 ? 68.521  135.798 106.003 1.00 38.34  ? 4587 LEU A N     1 
ATOM   22739 C  CA    . LEU A 1 4587 ? 68.776  135.463 107.400 1.00 33.46  ? 4587 LEU A CA    1 
ATOM   22740 C  C     . LEU A 1 4587 ? 67.545  134.774 107.962 1.00 33.45  ? 4587 LEU A C     1 
ATOM   22741 O  O     . LEU A 1 4587 ? 66.429  135.300 107.859 1.00 37.34  ? 4587 LEU A O     1 
ATOM   22742 C  CB    . LEU A 1 4587 ? 69.136  136.709 108.218 1.00 40.98  ? 4587 LEU A CB    1 
ATOM   22743 C  CG    . LEU A 1 4587 ? 69.609  136.534 109.667 1.00 38.37  ? 4587 LEU A CG    1 
ATOM   22744 C  CD1   . LEU A 1 4587 ? 70.500  137.694 110.065 1.00 46.54  ? 4587 LEU A CD1   1 
ATOM   22745 C  CD2   . LEU A 1 4587 ? 68.445  136.428 110.642 1.00 39.70  ? 4587 LEU A CD2   1 
ATOM   22746 N  N     . THR A 1 4588 ? 67.751  133.602 108.553 1.00 32.96  ? 4588 THR A N     1 
ATOM   22747 C  CA    . THR A 1 4588 ? 66.677  132.821 109.144 1.00 32.07  ? 4588 THR A CA    1 
ATOM   22748 C  C     . THR A 1 4588 ? 66.796  132.890 110.661 1.00 29.88  ? 4588 THR A C     1 
ATOM   22749 O  O     . THR A 1 4588 ? 67.819  132.493 111.229 1.00 27.40  ? 4588 THR A O     1 
ATOM   22750 C  CB    . THR A 1 4588 ? 66.730  131.371 108.662 1.00 30.62  ? 4588 THR A CB    1 
ATOM   22751 O  OG1   . THR A 1 4588 ? 66.625  131.340 107.233 1.00 34.08  ? 4588 THR A OG1   1 
ATOM   22752 C  CG2   . THR A 1 4588 ? 65.586  130.576 109.254 1.00 29.78  ? 4588 THR A CG2   1 
ATOM   22753 N  N     . GLN A 1 4589 ? 65.759  133.407 111.306 1.00 30.76  ? 4589 GLN A N     1 
ATOM   22754 C  CA    . GLN A 1 4589 ? 65.662  133.429 112.755 1.00 30.76  ? 4589 GLN A CA    1 
ATOM   22755 C  C     . GLN A 1 4589 ? 64.959  132.157 113.207 1.00 28.30  ? 4589 GLN A C     1 
ATOM   22756 O  O     . GLN A 1 4589 ? 63.784  131.939 112.883 1.00 36.10  ? 4589 GLN A O     1 
ATOM   22757 C  CB    . GLN A 1 4589 ? 64.903  134.667 113.230 1.00 33.72  ? 4589 GLN A CB    1 
ATOM   22758 C  CG    . GLN A 1 4589 ? 65.236  135.933 112.460 1.00 39.44  ? 4589 GLN A CG    1 
ATOM   22759 C  CD    . GLN A 1 4589 ? 65.063  137.184 113.296 1.00 52.42  ? 4589 GLN A CD    1 
ATOM   22760 O  OE1   . GLN A 1 4589 ? 64.525  137.137 114.402 1.00 58.10  ? 4589 GLN A OE1   1 
ATOM   22761 N  NE2   . GLN A 1 4589 ? 65.519  138.315 112.769 1.00 60.54  ? 4589 GLN A NE2   1 
ATOM   22762 N  N     . LEU A 1 4590 ? 65.692  131.313 113.926 1.00 22.44  ? 4590 LEU A N     1 
ATOM   22763 C  CA    . LEU A 1 4590 ? 65.150  130.105 114.541 1.00 27.08  ? 4590 LEU A CA    1 
ATOM   22764 C  C     . LEU A 1 4590 ? 64.771  130.467 115.969 1.00 33.08  ? 4590 LEU A C     1 
ATOM   22765 O  O     . LEU A 1 4590 ? 65.623  130.871 116.764 1.00 41.07  ? 4590 LEU A O     1 
ATOM   22766 C  CB    . LEU A 1 4590 ? 66.172  128.975 114.497 1.00 27.36  ? 4590 LEU A CB    1 
ATOM   22767 C  CG    . LEU A 1 4590 ? 66.743  128.621 113.123 1.00 28.62  ? 4590 LEU A CG    1 
ATOM   22768 C  CD1   . LEU A 1 4590 ? 67.598  127.374 113.210 1.00 31.49  ? 4590 LEU A CD1   1 
ATOM   22769 C  CD2   . LEU A 1 4590 ? 65.620  128.421 112.123 1.00 24.83  ? 4590 LEU A CD2   1 
ATOM   22770 N  N     . ARG A 1 4591 ? 63.488  130.348 116.292 1.00 33.54  ? 4591 ARG A N     1 
ATOM   22771 C  CA    . ARG A 1 4591 ? 62.970  130.719 117.600 1.00 35.74  ? 4591 ARG A CA    1 
ATOM   22772 C  C     . ARG A 1 4591 ? 62.336  129.500 118.253 1.00 39.13  ? 4591 ARG A C     1 
ATOM   22773 O  O     . ARG A 1 4591 ? 61.428  128.889 117.685 1.00 43.02  ? 4591 ARG A O     1 
ATOM   22774 C  CB    . ARG A 1 4591 ? 61.950  131.852 117.471 1.00 38.09  ? 4591 ARG A CB    1 
ATOM   22775 C  CG    . ARG A 1 4591 ? 61.329  132.300 118.779 1.00 44.94  ? 4591 ARG A CG    1 
ATOM   22776 C  CD    . ARG A 1 4591 ? 60.713  133.684 118.640 1.00 51.04  ? 4591 ARG A CD    1 
ATOM   22777 N  NE    . ARG A 1 4591 ? 60.081  133.873 117.339 1.00 57.83  ? 4591 ARG A NE    1 
ATOM   22778 C  CZ    . ARG A 1 4591 ? 58.872  133.430 117.020 1.00 59.17  ? 4591 ARG A CZ    1 
ATOM   22779 N  NH1   . ARG A 1 4591 ? 58.125  132.769 117.889 1.00 55.79  ? 4591 ARG A NH1   1 
ATOM   22780 N  NH2   . ARG A 1 4591 ? 58.401  133.657 115.797 1.00 55.35  ? 4591 ARG A NH2   1 
ATOM   22781 N  N     . TRP A 1 4592 ? 62.808  129.151 119.443 1.00 39.01  ? 4592 TRP A N     1 
ATOM   22782 C  CA    . TRP A 1 4592 ? 62.285  128.008 120.178 1.00 42.51  ? 4592 TRP A CA    1 
ATOM   22783 C  C     . TRP A 1 4592 ? 61.239  128.514 121.161 1.00 45.01  ? 4592 TRP A C     1 
ATOM   22784 O  O     . TRP A 1 4592 ? 61.561  129.292 122.065 1.00 52.20  ? 4592 TRP A O     1 
ATOM   22785 C  CB    . TRP A 1 4592 ? 63.408  127.273 120.907 1.00 42.75  ? 4592 TRP A CB    1 
ATOM   22786 C  CG    . TRP A 1 4592 ? 64.402  126.638 119.986 1.00 42.86  ? 4592 TRP A CG    1 
ATOM   22787 C  CD1   . TRP A 1 4592 ? 65.629  127.126 119.646 1.00 38.06  ? 4592 TRP A CD1   1 
ATOM   22788 C  CD2   . TRP A 1 4592 ? 64.253  125.400 119.281 1.00 46.51  ? 4592 TRP A CD2   1 
ATOM   22789 N  NE1   . TRP A 1 4592 ? 66.256  126.269 118.776 1.00 38.41  ? 4592 TRP A NE1   1 
ATOM   22790 C  CE2   . TRP A 1 4592 ? 65.432  125.201 118.535 1.00 43.05  ? 4592 TRP A CE2   1 
ATOM   22791 C  CE3   . TRP A 1 4592 ? 63.240  124.440 119.209 1.00 45.24  ? 4592 TRP A CE3   1 
ATOM   22792 C  CZ2   . TRP A 1 4592 ? 65.625  124.083 117.728 1.00 41.58  ? 4592 TRP A CZ2   1 
ATOM   22793 C  CZ3   . TRP A 1 4592 ? 63.433  123.331 118.407 1.00 45.07  ? 4592 TRP A CZ3   1 
ATOM   22794 C  CH2   . TRP A 1 4592 ? 64.616  123.162 117.677 1.00 45.11  ? 4592 TRP A CH2   1 
ATOM   22795 N  N     . VAL A 1 4593 ? 59.990  128.080 120.986 1.00 44.60  ? 4593 VAL A N     1 
ATOM   22796 C  CA    . VAL A 1 4593 ? 58.892  128.579 121.802 1.00 50.88  ? 4593 VAL A CA    1 
ATOM   22797 C  C     . VAL A 1 4593 ? 58.149  127.408 122.427 1.00 59.87  ? 4593 VAL A C     1 
ATOM   22798 O  O     . VAL A 1 4593 ? 58.213  126.272 121.953 1.00 58.41  ? 4593 VAL A O     1 
ATOM   22799 C  CB    . VAL A 1 4593 ? 57.915  129.465 120.997 1.00 51.44  ? 4593 VAL A CB    1 
ATOM   22800 C  CG1   . VAL A 1 4593 ? 58.615  130.721 120.513 1.00 50.28  ? 4593 VAL A CG1   1 
ATOM   22801 C  CG2   . VAL A 1 4593 ? 57.339  128.694 119.826 1.00 43.55  ? 4593 VAL A CG2   1 
ATOM   22802 N  N     . LYS A 1 4594 ? 57.443  127.702 123.516 1.00 64.01  ? 4594 LYS A N     1 
ATOM   22803 C  CA    . LYS A 1 4594 ? 56.671  126.677 124.205 1.00 67.76  ? 4594 LYS A CA    1 
ATOM   22804 C  C     . LYS A 1 4594 ? 55.614  126.103 123.270 1.00 68.61  ? 4594 LYS A C     1 
ATOM   22805 O  O     . LYS A 1 4594 ? 54.867  126.845 122.625 1.00 69.65  ? 4594 LYS A O     1 
ATOM   22806 C  CB    . LYS A 1 4594 ? 56.015  127.265 125.454 1.00 72.70  ? 4594 LYS A CB    1 
ATOM   22807 C  CG    . LYS A 1 4594 ? 55.455  126.230 126.415 1.00 71.52  ? 4594 LYS A CG    1 
ATOM   22808 C  CD    . LYS A 1 4594 ? 56.545  125.294 126.911 1.00 74.27  ? 4594 LYS A CD    1 
ATOM   22809 C  CE    . LYS A 1 4594 ? 55.957  124.106 127.653 1.00 77.00  ? 4594 LYS A CE    1 
ATOM   22810 N  NZ    . LYS A 1 4594 ? 55.143  123.238 126.758 1.00 80.44  ? 4594 LYS A NZ    1 
ATOM   22811 N  N     . GLN A 1 4595 ? 55.555  124.776 123.196 1.00 69.57  ? 4595 GLN A N     1 
ATOM   22812 C  CA    . GLN A 1 4595 ? 54.655  124.112 122.264 1.00 72.16  ? 4595 GLN A CA    1 
ATOM   22813 C  C     . GLN A 1 4595 ? 53.228  124.144 122.795 1.00 81.94  ? 4595 GLN A C     1 
ATOM   22814 O  O     . GLN A 1 4595 ? 52.971  123.752 123.937 1.00 80.95  ? 4595 GLN A O     1 
ATOM   22815 C  CB    . GLN A 1 4595 ? 55.104  122.671 122.026 1.00 68.13  ? 4595 GLN A CB    1 
ATOM   22816 C  CG    . GLN A 1 4595 ? 54.393  121.983 120.872 1.00 72.27  ? 4595 GLN A CG    1 
ATOM   22817 C  CD    . GLN A 1 4595 ? 54.899  120.575 120.633 1.00 76.42  ? 4595 GLN A CD    1 
ATOM   22818 O  OE1   . GLN A 1 4595 ? 55.776  120.088 121.346 1.00 70.65  ? 4595 GLN A OE1   1 
ATOM   22819 N  NE2   . GLN A 1 4595 ? 54.348  119.912 119.623 1.00 73.78  ? 4595 GLN A NE2   1 
ATOM   22820 N  N     . THR A 1 4596 ? 52.301  124.611 121.960 1.00 86.35  ? 4596 THR A N     1 
ATOM   22821 C  CA    . THR A 1 4596 ? 50.891  124.691 122.315 1.00 89.67  ? 4596 THR A CA    1 
ATOM   22822 C  C     . THR A 1 4596 ? 50.064  123.587 121.667 1.00 89.38  ? 4596 THR A C     1 
ATOM   22823 O  O     . THR A 1 4596 ? 48.832  123.648 121.721 1.00 89.56  ? 4596 THR A O     1 
ATOM   22824 C  CB    . THR A 1 4596 ? 50.325  126.060 121.931 1.00 86.98  ? 4596 THR A CB    1 
ATOM   22825 O  OG1   . THR A 1 4596 ? 50.419  126.239 120.513 1.00 88.76  ? 4596 THR A OG1   1 
ATOM   22826 C  CG2   . THR A 1 4596 ? 51.098  127.169 122.629 1.00 75.71  ? 4596 THR A CG2   1 
ATOM   22827 N  N     . ASN A 1 4597 ? 50.722  122.617 121.027 1.00 87.60  ? 4597 ASN A N     1 
ATOM   22828 C  CA    . ASN A 1 4597 ? 50.118  121.418 120.424 1.00 92.31  ? 4597 ASN A CA    1 
ATOM   22829 C  C     . ASN A 1 4597 ? 48.745  121.693 119.809 1.00 95.49  ? 4597 ASN A C     1 
ATOM   22830 O  O     . ASN A 1 4597 ? 47.775  120.960 120.015 1.00 93.24  ? 4597 ASN A O     1 
ATOM   22831 C  CB    . ASN A 1 4597 ? 50.081  120.248 121.425 1.00 89.63  ? 4597 ASN A CB    1 
ATOM   22832 C  CG    . ASN A 1 4597 ? 49.209  120.506 122.654 1.00 91.96  ? 4597 ASN A CG    1 
ATOM   22833 O  OD1   . ASN A 1 4597 ? 48.301  121.332 122.649 1.00 92.07  ? 4597 ASN A OD1   1 
ATOM   22834 N  ND2   . ASN A 1 4597 ? 49.497  119.777 123.726 1.00 90.81  ? 4597 ASN A ND2   1 
ATOM   22835 N  N     . THR A 1 4598 ? 48.679  122.762 119.014 1.00 95.87  ? 4598 THR A N     1 
ATOM   22836 C  CA    . THR A 1 4598 ? 47.466  123.143 118.301 1.00 95.84  ? 4598 THR A CA    1 
ATOM   22837 C  C     . THR A 1 4598 ? 47.432  122.586 116.882 1.00 97.45  ? 4598 THR A C     1 
ATOM   22838 O  O     . THR A 1 4598 ? 46.762  123.152 116.010 1.00 92.82  ? 4598 THR A O     1 
ATOM   22839 C  CB    . THR A 1 4598 ? 47.317  124.665 118.273 1.00 96.04  ? 4598 THR A CB    1 
ATOM   22840 O  OG1   . THR A 1 4598 ? 48.563  125.263 117.892 1.00 97.61  ? 4598 THR A OG1   1 
ATOM   22841 C  CG2   . THR A 1 4598 ? 46.902  125.188 119.639 1.00 87.75  ? 4598 THR A CG2   1 
ATOM   22842 N  N     . GLU A 1 4599 ? 48.150  121.486 116.637 1.00 98.55  ? 4599 GLU A N     1 
ATOM   22843 C  CA    . GLU A 1 4599 ? 48.224  120.852 115.325 1.00 96.97  ? 4599 GLU A CA    1 
ATOM   22844 C  C     . GLU A 1 4599 ? 48.719  121.826 114.264 1.00 97.15  ? 4599 GLU A C     1 
ATOM   22845 O  O     . GLU A 1 4599 ? 49.369  122.827 114.583 1.00 98.19  ? 4599 GLU A O     1 
ATOM   22846 C  CB    . GLU A 1 4599 ? 46.863  120.276 114.922 1.00 95.11  ? 4599 GLU A CB    1 
ATOM   22847 C  CG    . GLU A 1 4599 ? 46.292  119.275 115.912 1.00 94.11  ? 4599 GLU A CG    1 
ATOM   22848 C  CD    . GLU A 1 4599 ? 44.914  118.785 115.512 1.00 103.61 ? 4599 GLU A CD    1 
ATOM   22849 O  OE1   . GLU A 1 4599 ? 44.788  118.186 114.423 1.00 108.40 ? 4599 GLU A OE1   1 
ATOM   22850 O  OE2   . GLU A 1 4599 ? 43.958  118.999 116.286 1.00 101.83 ? 4599 GLU A OE2   1 
ATOM   22851 N  N     . LYS A 1 4600 ? 48.423  121.538 113.001 1.00 91.92  ? 4600 LYS A N     1 
ATOM   22852 C  CA    . LYS A 1 4600 ? 48.813  122.406 111.902 1.00 85.05  ? 4600 LYS A CA    1 
ATOM   22853 C  C     . LYS A 1 4600 ? 47.735  123.468 111.689 1.00 85.68  ? 4600 LYS A C     1 
ATOM   22854 O  O     . LYS A 1 4600 ? 46.812  123.620 112.493 1.00 90.33  ? 4600 LYS A O     1 
ATOM   22855 C  CB    . LYS A 1 4600 ? 49.068  121.580 110.643 1.00 87.31  ? 4600 LYS A CB    1 
ATOM   22856 C  CG    . LYS A 1 4600 ? 50.188  120.563 110.790 1.00 90.05  ? 4600 LYS A CG    1 
ATOM   22857 C  CD    . LYS A 1 4600 ? 51.471  121.216 111.281 1.00 80.38  ? 4600 LYS A CD    1 
ATOM   22858 C  CE    . LYS A 1 4600 ? 52.587  120.194 111.432 1.00 68.83  ? 4600 LYS A CE    1 
ATOM   22859 N  NZ    . LYS A 1 4600 ? 53.871  120.827 111.841 1.00 62.35  ? 4600 LYS A NZ    1 
ATOM   22860 N  N     . LYS A 1 4601 ? 47.843  124.221 110.592 1.00 81.78  ? 4601 LYS A N     1 
ATOM   22861 C  CA    . LYS A 1 4601 ? 46.896  125.288 110.291 1.00 80.26  ? 4601 LYS A CA    1 
ATOM   22862 C  C     . LYS A 1 4601 ? 46.249  125.095 108.923 1.00 78.38  ? 4601 LYS A C     1 
ATOM   22863 O  O     . LYS A 1 4601 ? 45.686  126.046 108.370 1.00 77.21  ? 4601 LYS A O     1 
ATOM   22864 C  CB    . LYS A 1 4601 ? 47.588  126.653 110.368 1.00 74.52  ? 4601 LYS A CB    1 
ATOM   22865 C  CG    . LYS A 1 4601 ? 46.668  127.818 110.706 1.00 79.80  ? 4601 LYS A CG    1 
ATOM   22866 C  CD    . LYS A 1 4601 ? 47.397  129.148 110.587 1.00 85.80  ? 4601 LYS A CD    1 
ATOM   22867 C  CE    . LYS A 1 4601 ? 48.657  129.166 111.439 1.00 82.00  ? 4601 LYS A CE    1 
ATOM   22868 N  NZ    . LYS A 1 4601 ? 49.364  130.474 111.362 1.00 77.00  ? 4601 LYS A NZ    1 
ATOM   22869 N  N     . ALA A 1 4602 ? 46.338  123.889 108.359 1.00 73.64  ? 4602 ALA A N     1 
ATOM   22870 C  CA    . ALA A 1 4602 ? 45.846  123.519 107.034 1.00 69.88  ? 4602 ALA A CA    1 
ATOM   22871 C  C     . ALA A 1 4602 ? 46.580  124.257 105.924 1.00 71.36  ? 4602 ALA A C     1 
ATOM   22872 O  O     . ALA A 1 4602 ? 46.282  124.034 104.744 1.00 66.10  ? 4602 ALA A O     1 
ATOM   22873 C  CB    . ALA A 1 4602 ? 44.334  123.743 106.876 1.00 63.48  ? 4602 ALA A CB    1 
ATOM   22874 N  N     . SER A 1 4603 ? 47.532  125.127 106.260 1.00 66.61  ? 4603 SER A N     1 
ATOM   22875 C  CA    . SER A 1 4603 ? 48.324  125.872 105.292 1.00 55.52  ? 4603 SER A CA    1 
ATOM   22876 C  C     . SER A 1 4603 ? 49.792  125.884 105.699 1.00 47.88  ? 4603 SER A C     1 
ATOM   22877 O  O     . SER A 1 4603 ? 50.505  126.856 105.448 1.00 46.38  ? 4603 SER A O     1 
ATOM   22878 C  CB    . SER A 1 4603 ? 47.799  127.300 105.140 1.00 54.04  ? 4603 SER A CB    1 
ATOM   22879 O  OG    . SER A 1 4603 ? 47.557  127.893 106.403 1.00 63.05  ? 4603 SER A OG    1 
ATOM   22880 N  N     . VAL A 1 4604 ? 50.251  124.816 106.346 1.00 42.63  ? 4604 VAL A N     1 
ATOM   22881 C  CA    . VAL A 1 4604 ? 51.609  124.725 106.866 1.00 34.43  ? 4604 VAL A CA    1 
ATOM   22882 C  C     . VAL A 1 4604 ? 52.280  123.499 106.267 1.00 33.12  ? 4604 VAL A C     1 
ATOM   22883 O  O     . VAL A 1 4604 ? 51.715  122.399 106.287 1.00 38.45  ? 4604 VAL A O     1 
ATOM   22884 C  CB    . VAL A 1 4604 ? 51.624  124.666 108.405 1.00 38.50  ? 4604 VAL A CB    1 
ATOM   22885 C  CG1   . VAL A 1 4604 ? 52.998  124.257 108.911 1.00 31.37  ? 4604 VAL A CG1   1 
ATOM   22886 C  CG2   . VAL A 1 4604 ? 51.226  126.013 108.984 1.00 38.56  ? 4604 VAL A CG2   1 
ATOM   22887 N  N     . VAL A 1 4605 ? 53.483  123.693 105.737 1.00 27.48  ? 4605 VAL A N     1 
ATOM   22888 C  CA    . VAL A 1 4605 ? 54.297  122.626 105.174 1.00 23.87  ? 4605 VAL A CA    1 
ATOM   22889 C  C     . VAL A 1 4605 ? 55.544  122.464 106.030 1.00 20.94  ? 4605 VAL A C     1 
ATOM   22890 O  O     . VAL A 1 4605 ? 56.126  123.450 106.501 1.00 22.38  ? 4605 VAL A O     1 
ATOM   22891 C  CB    . VAL A 1 4605 ? 54.667  122.895 103.699 1.00 22.35  ? 4605 VAL A CB    1 
ATOM   22892 C  CG1   . VAL A 1 4605 ? 53.416  122.967 102.852 1.00 20.68  ? 4605 VAL A CG1   1 
ATOM   22893 C  CG2   . VAL A 1 4605 ? 55.476  124.178 103.560 1.00 29.31  ? 4605 VAL A CG2   1 
ATOM   22894 N  N     . THR A 1 4606 ? 55.925  121.210 106.262 1.00 21.25  ? 4606 THR A N     1 
ATOM   22895 C  CA    . THR A 1 4606 ? 57.156  120.881 106.969 1.00 17.23  ? 4606 THR A CA    1 
ATOM   22896 C  C     . THR A 1 4606 ? 58.235  120.591 105.932 1.00 15.30  ? 4606 THR A C     1 
ATOM   22897 O  O     . THR A 1 4606 ? 58.209  119.549 105.269 1.00 17.92  ? 4606 THR A O     1 
ATOM   22898 C  CB    . THR A 1 4606 ? 56.954  119.686 107.896 1.00 19.34  ? 4606 THR A CB    1 
ATOM   22899 O  OG1   . THR A 1 4606 ? 55.943  119.994 108.864 1.00 29.01  ? 4606 THR A OG1   1 
ATOM   22900 C  CG2   . THR A 1 4606 ? 58.249  119.360 108.621 1.00 17.33  ? 4606 THR A CG2   1 
ATOM   22901 N  N     . LEU A 1 4607 ? 59.172  121.506 105.797 1.00 15.07  ? 4607 LEU A N     1 
ATOM   22902 C  CA    . LEU A 1 4607 ? 60.265  121.387 104.844 1.00 13.45  ? 4607 LEU A CA    1 
ATOM   22903 C  C     . LEU A 1 4607 ? 61.499  120.822 105.524 1.00 12.54  ? 4607 LEU A C     1 
ATOM   22904 O  O     . LEU A 1 4607 ? 61.924  121.342 106.569 1.00 16.65  ? 4607 LEU A O     1 
ATOM   22905 C  CB    . LEU A 1 4607 ? 60.593  122.743 104.226 1.00 11.28  ? 4607 LEU A CB    1 
ATOM   22906 C  CG    . LEU A 1 4607 ? 59.590  123.301 103.216 1.00 12.31  ? 4607 LEU A CG    1 
ATOM   22907 C  CD1   . LEU A 1 4607 ? 60.223  124.425 102.413 1.00 13.55  ? 4607 LEU A CD1   1 
ATOM   22908 C  CD2   . LEU A 1 4607 ? 59.071  122.203 102.298 1.00 10.18  ? 4607 LEU A CD2   1 
ATOM   22909 N  N     . PRO A 1 4608 ? 62.074  119.754 104.979 1.00 11.61  ? 4608 PRO A N     1 
ATOM   22910 C  CA    . PRO A 1 4608 ? 63.354  119.262 105.490 1.00 13.91  ? 4608 PRO A CA    1 
ATOM   22911 C  C     . PRO A 1 4608 ? 64.482  120.230 105.177 1.00 11.91  ? 4608 PRO A C     1 
ATOM   22912 O  O     . PRO A 1 4608 ? 64.436  120.978 104.198 1.00 11.20  ? 4608 PRO A O     1 
ATOM   22913 C  CB    . PRO A 1 4608 ? 63.544  117.936 104.746 1.00 10.16  ? 4608 PRO A CB    1 
ATOM   22914 C  CG    . PRO A 1 4608 ? 62.771  118.106 103.481 1.00 8.21   ? 4608 PRO A CG    1 
ATOM   22915 C  CD    . PRO A 1 4608 ? 61.597  118.980 103.819 1.00 10.74  ? 4608 PRO A CD    1 
ATOM   22916 N  N     . VAL A 1 4609 ? 65.508  120.209 106.023 1.00 11.27  ? 4609 VAL A N     1 
ATOM   22917 C  CA    . VAL A 1 4609 ? 66.741  120.944 105.778 1.00 15.61  ? 4609 VAL A CA    1 
ATOM   22918 C  C     . VAL A 1 4609 ? 67.853  119.916 105.634 1.00 16.82  ? 4609 VAL A C     1 
ATOM   22919 O  O     . VAL A 1 4609 ? 68.243  119.269 106.612 1.00 18.25  ? 4609 VAL A O     1 
ATOM   22920 C  CB    . VAL A 1 4609 ? 67.049  121.945 106.899 1.00 15.48  ? 4609 VAL A CB    1 
ATOM   22921 C  CG1   . VAL A 1 4609 ? 68.294  122.747 106.561 1.00 17.11  ? 4609 VAL A CG1   1 
ATOM   22922 C  CG2   . VAL A 1 4609 ? 65.868  122.868 107.115 1.00 15.27  ? 4609 VAL A CG2   1 
ATOM   22923 N  N     . TYR A 1 4610 ? 68.354  119.755 104.417 1.00 14.21  ? 4610 TYR A N     1 
ATOM   22924 C  CA    . TYR A 1 4610 ? 69.463  118.855 104.148 1.00 13.96  ? 4610 TYR A CA    1 
ATOM   22925 C  C     . TYR A 1 4610 ? 70.777  119.624 104.168 1.00 16.47  ? 4610 TYR A C     1 
ATOM   22926 O  O     . TYR A 1 4610 ? 70.818  120.839 103.965 1.00 20.94  ? 4610 TYR A O     1 
ATOM   22927 C  CB    . TYR A 1 4610 ? 69.278  118.149 102.803 1.00 15.63  ? 4610 TYR A CB    1 
ATOM   22928 C  CG    . TYR A 1 4610 ? 68.068  117.244 102.753 1.00 12.29  ? 4610 TYR A CG    1 
ATOM   22929 C  CD1   . TYR A 1 4610 ? 68.079  116.003 103.376 1.00 12.71  ? 4610 TYR A CD1   1 
ATOM   22930 C  CD2   . TYR A 1 4610 ? 66.915  117.631 102.083 1.00 9.82   ? 4610 TYR A CD2   1 
ATOM   22931 C  CE1   . TYR A 1 4610 ? 66.976  115.173 103.333 1.00 13.59  ? 4610 TYR A CE1   1 
ATOM   22932 C  CE2   . TYR A 1 4610 ? 65.808  116.807 102.033 1.00 8.29   ? 4610 TYR A CE2   1 
ATOM   22933 C  CZ    . TYR A 1 4610 ? 65.843  115.579 102.660 1.00 10.64  ? 4610 TYR A CZ    1 
ATOM   22934 O  OH    . TYR A 1 4610 ? 64.743  114.756 102.615 1.00 13.01  ? 4610 TYR A OH    1 
ATOM   22935 N  N     . LEU A 1 4611 ? 71.862  118.894 104.431 1.00 18.71  ? 4611 LEU A N     1 
ATOM   22936 C  CA    . LEU A 1 4611 ? 73.167  119.535 104.547 1.00 20.64  ? 4611 LEU A CA    1 
ATOM   22937 C  C     . LEU A 1 4611 ? 73.640  120.074 103.202 1.00 26.93  ? 4611 LEU A C     1 
ATOM   22938 O  O     . LEU A 1 4611 ? 74.174  121.186 103.121 1.00 32.20  ? 4611 LEU A O     1 
ATOM   22939 C  CB    . LEU A 1 4611 ? 74.186  118.553 105.121 1.00 20.99  ? 4611 LEU A CB    1 
ATOM   22940 C  CG    . LEU A 1 4611 ? 75.591  119.125 105.299 1.00 26.33  ? 4611 LEU A CG    1 
ATOM   22941 C  CD1   . LEU A 1 4611 ? 75.560  120.309 106.254 1.00 28.99  ? 4611 LEU A CD1   1 
ATOM   22942 C  CD2   . LEU A 1 4611 ? 76.537  118.059 105.798 1.00 33.33  ? 4611 LEU A CD2   1 
ATOM   22943 N  N     . ASN A 1 4612 ? 73.452  119.302 102.135 1.00 22.73  ? 4612 ASN A N     1 
ATOM   22944 C  CA    . ASN A 1 4612 ? 73.922  119.686 100.811 1.00 22.28  ? 4612 ASN A CA    1 
ATOM   22945 C  C     . ASN A 1 4612 ? 72.924  119.181 99.774  1.00 24.53  ? 4612 ASN A C     1 
ATOM   22946 O  O     . ASN A 1 4612 ? 71.871  118.629 100.110 1.00 24.26  ? 4612 ASN A O     1 
ATOM   22947 C  CB    . ASN A 1 4612 ? 75.343  119.158 100.570 1.00 23.16  ? 4612 ASN A CB    1 
ATOM   22948 C  CG    . ASN A 1 4612 ? 75.473  117.679 100.871 1.00 24.86  ? 4612 ASN A CG    1 
ATOM   22949 O  OD1   . ASN A 1 4612 ? 74.924  116.839 100.160 1.00 31.61  ? 4612 ASN A OD1   1 
ATOM   22950 N  ND2   . ASN A 1 4612 ? 76.203  117.353 101.931 1.00 26.72  ? 4612 ASN A ND2   1 
ATOM   22951 N  N     . PHE A 1 4613 ? 73.270  119.368 98.497  1.00 22.54  ? 4613 PHE A N     1 
ATOM   22952 C  CA    . PHE A 1 4613 ? 72.358  119.055 97.403  1.00 21.57  ? 4613 PHE A CA    1 
ATOM   22953 C  C     . PHE A 1 4613 ? 72.044  117.569 97.295  1.00 20.98  ? 4613 PHE A C     1 
ATOM   22954 O  O     . PHE A 1 4613 ? 70.991  117.213 96.756  1.00 23.52  ? 4613 PHE A O     1 
ATOM   22955 C  CB    . PHE A 1 4613 ? 72.934  119.558 96.077  1.00 21.93  ? 4613 PHE A CB    1 
ATOM   22956 C  CG    . PHE A 1 4613 ? 74.234  118.908 95.691  1.00 25.72  ? 4613 PHE A CG    1 
ATOM   22957 C  CD1   . PHE A 1 4613 ? 75.429  119.323 96.256  1.00 28.41  ? 4613 PHE A CD1   1 
ATOM   22958 C  CD2   . PHE A 1 4613 ? 74.260  117.882 94.762  1.00 26.16  ? 4613 PHE A CD2   1 
ATOM   22959 C  CE1   . PHE A 1 4613 ? 76.623  118.726 95.902  1.00 32.34  ? 4613 PHE A CE1   1 
ATOM   22960 C  CE2   . PHE A 1 4613 ? 75.451  117.281 94.405  1.00 28.49  ? 4613 PHE A CE2   1 
ATOM   22961 C  CZ    . PHE A 1 4613 ? 76.634  117.704 94.976  1.00 35.80  ? 4613 PHE A CZ    1 
ATOM   22962 N  N     . THR A 1 4614 ? 72.925  116.694 97.786  1.00 21.46  ? 4614 THR A N     1 
ATOM   22963 C  CA    . THR A 1 4614 ? 72.666  115.261 97.702  1.00 20.48  ? 4614 THR A CA    1 
ATOM   22964 C  C     . THR A 1 4614 ? 71.476  114.834 98.550  1.00 21.17  ? 4614 THR A C     1 
ATOM   22965 O  O     . THR A 1 4614 ? 70.915  113.761 98.307  1.00 28.06  ? 4614 THR A O     1 
ATOM   22966 C  CB    . THR A 1 4614 ? 73.908  114.470 98.118  1.00 18.76  ? 4614 THR A CB    1 
ATOM   22967 O  OG1   . THR A 1 4614 ? 74.067  114.538 99.541  1.00 26.31  ? 4614 THR A OG1   1 
ATOM   22968 C  CG2   . THR A 1 4614 ? 75.150  115.031 97.444  1.00 20.70  ? 4614 THR A CG2   1 
ATOM   22969 N  N     . ARG A 1 4615 ? 71.085  115.647 99.535  1.00 19.87  ? 4615 ARG A N     1 
ATOM   22970 C  CA    . ARG A 1 4615 ? 69.931  115.375 100.395 1.00 15.90  ? 4615 ARG A CA    1 
ATOM   22971 C  C     . ARG A 1 4615 ? 70.065  114.043 101.128 1.00 14.79  ? 4615 ARG A C     1 
ATOM   22972 O  O     . ARG A 1 4615 ? 69.065  113.413 101.479 1.00 17.07  ? 4615 ARG A O     1 
ATOM   22973 C  CB    . ARG A 1 4615 ? 68.622  115.419 99.600  1.00 11.78  ? 4615 ARG A CB    1 
ATOM   22974 C  CG    . ARG A 1 4615 ? 68.347  116.758 98.943  1.00 12.71  ? 4615 ARG A CG    1 
ATOM   22975 C  CD    . ARG A 1 4615 ? 66.919  116.848 98.436  1.00 11.80  ? 4615 ARG A CD    1 
ATOM   22976 N  NE    . ARG A 1 4615 ? 66.680  118.096 97.721  1.00 14.49  ? 4615 ARG A NE    1 
ATOM   22977 C  CZ    . ARG A 1 4615 ? 65.494  118.493 97.281  1.00 12.31  ? 4615 ARG A CZ    1 
ATOM   22978 N  NH1   . ARG A 1 4615 ? 64.408  117.762 97.464  1.00 7.99   ? 4615 ARG A NH1   1 
ATOM   22979 N  NH2   . ARG A 1 4615 ? 65.396  119.656 96.643  1.00 15.62  ? 4615 ARG A NH2   1 
ATOM   22980 N  N     . ALA A 1 4616 ? 71.300  113.605 101.363 1.00 15.66  ? 4616 ALA A N     1 
ATOM   22981 C  CA    . ALA A 1 4616 ? 71.556  112.352 102.058 1.00 16.26  ? 4616 ALA A CA    1 
ATOM   22982 C  C     . ALA A 1 4616 ? 71.596  112.502 103.573 1.00 20.24  ? 4616 ALA A C     1 
ATOM   22983 O  O     . ALA A 1 4616 ? 71.594  111.487 104.278 1.00 27.55  ? 4616 ALA A O     1 
ATOM   22984 C  CB    . ALA A 1 4616 ? 72.874  111.740 101.574 1.00 15.88  ? 4616 ALA A CB    1 
ATOM   22985 N  N     . ASP A 1 4617 ? 71.630  113.729 104.089 1.00 20.06  ? 4617 ASP A N     1 
ATOM   22986 C  CA    . ASP A 1 4617 ? 71.745  113.977 105.523 1.00 23.30  ? 4617 ASP A CA    1 
ATOM   22987 C  C     . ASP A 1 4617 ? 70.707  115.014 105.928 1.00 22.36  ? 4617 ASP A C     1 
ATOM   22988 O  O     . ASP A 1 4617 ? 70.758  116.160 105.471 1.00 20.40  ? 4617 ASP A O     1 
ATOM   22989 C  CB    . ASP A 1 4617 ? 73.153  114.448 105.889 1.00 21.80  ? 4617 ASP A CB    1 
ATOM   22990 C  CG    . ASP A 1 4617 ? 74.235  113.610 105.239 1.00 28.45  ? 4617 ASP A CG    1 
ATOM   22991 O  OD1   . ASP A 1 4617 ? 74.515  112.502 105.744 1.00 31.56  ? 4617 ASP A OD1   1 
ATOM   22992 O  OD2   . ASP A 1 4617 ? 74.806  114.058 104.223 1.00 30.26  ? 4617 ASP A OD2   1 
ATOM   22993 N  N     . LEU A 1 4618 ? 69.772  114.613 106.785 1.00 23.30  ? 4618 LEU A N     1 
ATOM   22994 C  CA    . LEU A 1 4618 ? 68.781  115.538 107.315 1.00 21.81  ? 4618 LEU A CA    1 
ATOM   22995 C  C     . LEU A 1 4618 ? 69.357  116.292 108.506 1.00 25.18  ? 4618 LEU A C     1 
ATOM   22996 O  O     . LEU A 1 4618 ? 69.918  115.686 109.423 1.00 33.09  ? 4618 LEU A O     1 
ATOM   22997 C  CB    . LEU A 1 4618 ? 67.515  114.787 107.725 1.00 22.65  ? 4618 LEU A CB    1 
ATOM   22998 C  CG    . LEU A 1 4618 ? 66.366  115.662 108.226 1.00 22.87  ? 4618 LEU A CG    1 
ATOM   22999 C  CD1   . LEU A 1 4618 ? 65.796  116.485 107.088 1.00 16.17  ? 4618 LEU A CD1   1 
ATOM   23000 C  CD2   . LEU A 1 4618 ? 65.283  114.814 108.872 1.00 27.91  ? 4618 LEU A CD2   1 
ATOM   23001 N  N     . ILE A 1 4619 ? 69.216  117.616 108.490 1.00 23.31  ? 4619 ILE A N     1 
ATOM   23002 C  CA    . ILE A 1 4619 ? 69.709  118.447 109.582 1.00 25.34  ? 4619 ILE A CA    1 
ATOM   23003 C  C     . ILE A 1 4619 ? 68.583  118.630 110.589 1.00 23.43  ? 4619 ILE A C     1 
ATOM   23004 O  O     . ILE A 1 4619 ? 68.703  118.231 111.753 1.00 29.73  ? 4619 ILE A O     1 
ATOM   23005 C  CB    . ILE A 1 4619 ? 70.218  119.809 109.074 1.00 27.12  ? 4619 ILE A CB    1 
ATOM   23006 C  CG1   . ILE A 1 4619 ? 71.181  119.622 107.901 1.00 24.35  ? 4619 ILE A CG1   1 
ATOM   23007 C  CG2   . ILE A 1 4619 ? 70.906  120.566 110.195 1.00 26.53  ? 4619 ILE A CG2   1 
ATOM   23008 C  CD1   . ILE A 1 4619 ? 72.332  118.700 108.191 1.00 23.28  ? 4619 ILE A CD1   1 
ATOM   23009 N  N     . PHE A 1 4620 ? 67.483  119.227 110.143 1.00 19.22  ? 4620 PHE A N     1 
ATOM   23010 C  CA    . PHE A 1 4620 ? 66.303  119.433 110.974 1.00 19.00  ? 4620 PHE A CA    1 
ATOM   23011 C  C     . PHE A 1 4620 ? 65.119  119.720 110.055 1.00 18.49  ? 4620 PHE A C     1 
ATOM   23012 O  O     . PHE A 1 4620 ? 65.195  119.531 108.836 1.00 22.73  ? 4620 PHE A O     1 
ATOM   23013 C  CB    . PHE A 1 4620 ? 66.540  120.545 112.006 1.00 19.08  ? 4620 PHE A CB    1 
ATOM   23014 C  CG    . PHE A 1 4620 ? 66.736  121.914 111.409 1.00 18.16  ? 4620 PHE A CG    1 
ATOM   23015 C  CD1   . PHE A 1 4620 ? 67.919  122.245 110.768 1.00 22.24  ? 4620 PHE A CD1   1 
ATOM   23016 C  CD2   . PHE A 1 4620 ? 65.750  122.878 111.517 1.00 17.93  ? 4620 PHE A CD2   1 
ATOM   23017 C  CE1   . PHE A 1 4620 ? 68.106  123.504 110.228 1.00 19.77  ? 4620 PHE A CE1   1 
ATOM   23018 C  CE2   . PHE A 1 4620 ? 65.933  124.140 110.983 1.00 18.03  ? 4620 PHE A CE2   1 
ATOM   23019 C  CZ    . PHE A 1 4620 ? 67.112  124.452 110.336 1.00 17.28  ? 4620 PHE A CZ    1 
ATOM   23020 N  N     . THR A 1 4621 ? 64.010  120.156 110.645 1.00 17.39  ? 4621 THR A N     1 
ATOM   23021 C  CA    . THR A 1 4621 ? 62.793  120.444 109.904 1.00 16.55  ? 4621 THR A CA    1 
ATOM   23022 C  C     . THR A 1 4621 ? 62.313  121.846 110.244 1.00 20.61  ? 4621 THR A C     1 
ATOM   23023 O  O     . THR A 1 4621 ? 62.477  122.318 111.372 1.00 23.24  ? 4621 THR A O     1 
ATOM   23024 C  CB    . THR A 1 4621 ? 61.682  119.429 110.217 1.00 19.40  ? 4621 THR A CB    1 
ATOM   23025 O  OG1   . THR A 1 4621 ? 61.364  119.480 111.613 1.00 27.36  ? 4621 THR A OG1   1 
ATOM   23026 C  CG2   . THR A 1 4621 ? 62.131  118.023 109.864 1.00 16.45  ? 4621 THR A CG2   1 
ATOM   23027 N  N     . VAL A 1 4622 ? 61.699  122.500 109.254 1.00 18.48  ? 4622 VAL A N     1 
ATOM   23028 C  CA    . VAL A 1 4622 ? 61.152  123.874 109.461 1.00 20.30  ? 4622 VAL A CA    1 
ATOM   23029 C  C     . VAL A 1 4622 ? 59.685  123.878 109.007 1.00 20.57  ? 4622 VAL A C     1 
ATOM   23030 O  O     . VAL A 1 4622 ? 59.374  123.195 108.005 1.00 20.01  ? 4622 VAL A O     1 
ATOM   23031 C  CB    . VAL A 1 4622 ? 61.974  124.919 108.684 1.00 23.51  ? 4622 VAL A CB    1 
ATOM   23032 C  CG1   . VAL A 1 4622 ? 63.399  125.026 109.211 1.00 22.96  ? 4622 VAL A CG1   1 
ATOM   23033 C  CG2   . VAL A 1 4622 ? 61.982  124.632 107.188 1.00 20.31  ? 4622 VAL A CG2   1 
ATOM   23034 N  N     . ASP A 1 4623 ? 58.823  124.609 109.717 1.00 27.38  ? 4623 ASP A N     1 
ATOM   23035 C  CA    . ASP A 1 4623 ? 57.391  124.714 109.320 1.00 26.19  ? 4623 ASP A CA    1 
ATOM   23036 C  C     . ASP A 1 4623 ? 57.165  126.076 108.658 1.00 24.57  ? 4623 ASP A C     1 
ATOM   23037 O  O     . ASP A 1 4623 ? 57.558  127.099 109.259 1.00 30.68  ? 4623 ASP A O     1 
ATOM   23038 C  CB    . ASP A 1 4623 ? 56.467  124.470 110.501 1.00 31.20  ? 4623 ASP A CB    1 
ATOM   23039 C  CG    . ASP A 1 4623 ? 56.545  123.077 111.109 1.00 39.45  ? 4623 ASP A CG    1 
ATOM   23040 O  OD1   . ASP A 1 4623 ? 56.287  122.103 110.372 1.00 41.04  ? 4623 ASP A OD1   1 
ATOM   23041 O  OD2   . ASP A 1 4623 ? 56.862  122.980 112.313 1.00 52.03  ? 4623 ASP A OD2   1 
ATOM   23042 N  N     . PHE A 1 4624 ? 56.567  126.084 107.464 1.00 22.77  ? 4624 PHE A N     1 
ATOM   23043 C  CA    . PHE A 1 4624 ? 56.339  127.356 106.728 1.00 25.09  ? 4624 PHE A CA    1 
ATOM   23044 C  C     . PHE A 1 4624 ? 54.873  127.462 106.331 1.00 30.51  ? 4624 PHE A C     1 
ATOM   23045 O  O     . PHE A 1 4624 ? 54.289  126.451 105.882 1.00 32.97  ? 4624 PHE A O     1 
ATOM   23046 C  CB    . PHE A 1 4624 ? 57.217  127.422 105.476 1.00 22.77  ? 4624 PHE A CB    1 
ATOM   23047 C  CG    . PHE A 1 4624 ? 58.607  128.007 105.678 1.00 20.37  ? 4624 PHE A CG    1 
ATOM   23048 C  CD1   . PHE A 1 4624 ? 58.830  129.373 105.548 1.00 26.07  ? 4624 PHE A CD1   1 
ATOM   23049 C  CD2   . PHE A 1 4624 ? 59.689  127.189 105.983 1.00 21.63  ? 4624 PHE A CD2   1 
ATOM   23050 C  CE1   . PHE A 1 4624 ? 60.096  129.904 105.725 1.00 28.53  ? 4624 PHE A CE1   1 
ATOM   23051 C  CE2   . PHE A 1 4624 ? 60.954  127.727 106.159 1.00 23.39  ? 4624 PHE A CE2   1 
ATOM   23052 C  CZ    . PHE A 1 4624 ? 61.155  129.081 106.028 1.00 22.79  ? 4624 PHE A CZ    1 
ATOM   23053 N  N     . GLU A 1 4625 ? 54.290  128.653 106.488 1.00 31.74  ? 4625 GLU A N     1 
ATOM   23054 C  CA    . GLU A 1 4625 ? 52.888  128.865 106.044 1.00 38.57  ? 4625 GLU A CA    1 
ATOM   23055 C  C     . GLU A 1 4625 ? 52.890  129.009 104.514 1.00 38.92  ? 4625 GLU A C     1 
ATOM   23056 O  O     . GLU A 1 4625 ? 53.907  129.491 103.968 1.00 41.43  ? 4625 GLU A O     1 
ATOM   23057 C  CB    . GLU A 1 4625 ? 52.289  130.083 106.748 1.00 37.59  ? 4625 GLU A CB    1 
ATOM   23058 C  CG    . GLU A 1 4625 ? 50.787  130.238 106.524 1.00 46.67  ? 4625 GLU A CG    1 
ATOM   23059 C  CD    . GLU A 1 4625 ? 50.401  130.982 105.259 1.00 52.66  ? 4625 GLU A CD    1 
ATOM   23060 O  OE1   . GLU A 1 4625 ? 51.311  131.426 104.529 1.00 53.42  ? 4625 GLU A OE1   1 
ATOM   23061 O  OE2   . GLU A 1 4625 ? 49.186  131.118 105.004 1.00 55.29  ? 4625 GLU A OE2   1 
ATOM   23062 N  N     . ILE A 1 4626 ? 51.799  128.610 103.855 1.00 40.62  ? 4626 ILE A N     1 
ATOM   23063 C  CA    . ILE A 1 4626 ? 51.744  128.652 102.362 1.00 41.87  ? 4626 ILE A CA    1 
ATOM   23064 C  C     . ILE A 1 4626 ? 50.811  129.794 101.929 1.00 43.68  ? 4626 ILE A C     1 
ATOM   23065 O  O     . ILE A 1 4626 ? 49.702  129.901 102.496 1.00 49.72  ? 4626 ILE A O     1 
ATOM   23066 C  CB    . ILE A 1 4626 ? 51.300  127.284 101.814 1.00 47.90  ? 4626 ILE A CB    1 
ATOM   23067 C  CG1   . ILE A 1 4626 ? 49.848  126.975 102.174 1.00 50.75  ? 4626 ILE A CG1   1 
ATOM   23068 C  CG2   . ILE A 1 4626 ? 52.246  126.186 102.297 1.00 39.14  ? 4626 ILE A CG2   1 
ATOM   23069 C  CD1   . ILE A 1 4626 ? 49.480  125.507 102.060 1.00 42.72  ? 4626 ILE A CD1   1 
ATOM   23070 N  N     . ALA A 1 4627 ? 51.250  130.617 100.972 1.00 43.36  ? 4627 ALA A N     1 
ATOM   23071 C  CA    . ALA A 1 4627 ? 50.443  131.785 100.540 1.00 50.32  ? 4627 ALA A CA    1 
ATOM   23072 C  C     . ALA A 1 4627 ? 49.472  131.380 99.430  1.00 58.94  ? 4627 ALA A C     1 
ATOM   23073 O  O     . ALA A 1 4627 ? 49.438  130.186 99.066  1.00 59.34  ? 4627 ALA A O     1 
ATOM   23074 C  CB    . ALA A 1 4627 ? 51.358  132.901 100.086 1.00 48.92  ? 4627 ALA A CB    1 
ATOM   23075 N  N     . THR A 1 4628 ? 48.690  132.341 98.927  1.00 64.94  ? 4628 THR A N     1 
ATOM   23076 C  CA    . THR A 1 4628 ? 47.749  132.065 97.818  1.00 68.75  ? 4628 THR A CA    1 
ATOM   23077 C  C     . THR A 1 4628 ? 47.010  130.773 98.094  1.00 68.38  ? 4628 THR A C     1 
ATOM   23078 O  O     . THR A 1 4628 ? 46.501  130.612 99.225  1.00 64.30  ? 4628 THR A O     1 
ATOM   23079 C  CB    . THR A 1 4628 ? 48.513  132.007 96.495  1.00 64.52  ? 4628 THR A CB    1 
ATOM   23080 O  OG1   . THR A 1 4628 ? 49.317  130.833 96.560  1.00 59.83  ? 4628 THR A OG1   1 
ATOM   23081 C  CG2   . THR A 1 4628 ? 49.392  133.226 96.279  1.00 60.55  ? 4628 THR A CG2   1 
ATOM   23082 N  N     . LYS A 1 4629 ? 46.949  129.883 97.100  1.00 64.61  ? 4629 LYS A N     1 
ATOM   23083 C  CA    . LYS A 1 4629 ? 46.264  128.575 97.269  1.00 65.79  ? 4629 LYS A CA    1 
ATOM   23084 C  C     . LYS A 1 4629 ? 47.308  127.452 97.186  1.00 63.55  ? 4629 LYS A C     1 
ATOM   23085 O  O     . LYS A 1 4629 ? 46.959  126.350 96.708  1.00 65.36  ? 4629 LYS A O     1 
ATOM   23086 C  CB    . LYS A 1 4629 ? 45.183  128.402 96.197  1.00 73.88  ? 4629 LYS A CB    1 
ATOM   23087 C  CG    . LYS A 1 4629 ? 45.687  128.490 94.764  1.00 77.18  ? 4629 LYS A CG    1 
ATOM   23088 C  CD    . LYS A 1 4629 ? 44.584  128.278 93.735  1.00 76.06  ? 4629 LYS A CD    1 
ATOM   23089 C  CE    . LYS A 1 4629 ? 43.470  129.265 93.889  1.00 76.68  ? 4629 LYS A CE    1 
ATOM   23090 N  NZ    . LYS A 1 4629 ? 42.407  129.035 92.908  1.00 82.09  ? 4629 LYS A NZ    1 
ATOM   23091 N  N     . GLU A 1 4630 ? 48.536  127.725 97.638  1.00 55.83  ? 4630 GLU A N     1 
ATOM   23092 C  CA    . GLU A 1 4630 ? 49.619  126.712 97.561  1.00 48.36  ? 4630 GLU A CA    1 
ATOM   23093 C  C     . GLU A 1 4630 ? 49.087  125.368 98.076  1.00 44.22  ? 4630 GLU A C     1 
ATOM   23094 O  O     . GLU A 1 4630 ? 48.510  125.346 99.184  1.00 42.22  ? 4630 GLU A O     1 
ATOM   23095 C  CB    . GLU A 1 4630 ? 50.829  127.131 98.396  1.00 49.80  ? 4630 GLU A CB    1 
ATOM   23096 C  CG    . GLU A 1 4630 ? 51.484  128.413 97.897  1.00 54.23  ? 4630 GLU A CG    1 
ATOM   23097 C  CD    . GLU A 1 4630 ? 51.736  128.396 96.403  1.00 60.19  ? 4630 GLU A CD    1 
ATOM   23098 O  OE1   . GLU A 1 4630 ? 52.523  127.543 95.946  1.00 54.23  ? 4630 GLU A OE1   1 
ATOM   23099 O  OE2   . GLU A 1 4630 ? 51.134  129.229 95.694  1.00 68.17  ? 4630 GLU A OE2   1 
ATOM   23100 N  N     . ASP A 1 4631 ? 49.272  124.299 97.299  1.00 42.98  ? 4631 ASP A N     1 
ATOM   23101 C  CA    . ASP A 1 4631 ? 48.846  122.948 97.755  1.00 36.78  ? 4631 ASP A CA    1 
ATOM   23102 C  C     . ASP A 1 4631 ? 50.008  122.305 98.515  1.00 27.31  ? 4631 ASP A C     1 
ATOM   23103 O  O     . ASP A 1 4631 ? 51.065  122.069 97.892  1.00 27.37  ? 4631 ASP A O     1 
ATOM   23104 C  CB    . ASP A 1 4631 ? 48.380  122.087 96.592  1.00 39.59  ? 4631 ASP A CB    1 
ATOM   23105 C  CG    . ASP A 1 4631 ? 47.840  120.715 96.971  1.00 45.97  ? 4631 ASP A CG    1 
ATOM   23106 O  OD1   . ASP A 1 4631 ? 47.773  120.425 98.184  1.00 41.75  ? 4631 ASP A OD1   1 
ATOM   23107 O  OD2   . ASP A 1 4631 ? 47.496  119.946 96.049  1.00 49.55  ? 4631 ASP A OD2   1 
ATOM   23108 N  N     . PRO A 1 4632 ? 49.874  122.018 99.827  1.00 25.82  ? 4632 PRO A N     1 
ATOM   23109 C  CA    . PRO A 1 4632 ? 50.932  121.332 100.551 1.00 25.83  ? 4632 PRO A CA    1 
ATOM   23110 C  C     . PRO A 1 4632 ? 51.304  120.100 99.749  1.00 22.26  ? 4632 PRO A C     1 
ATOM   23111 O  O     . PRO A 1 4632 ? 52.493  119.727 99.719  1.00 21.78  ? 4632 PRO A O     1 
ATOM   23112 C  CB    . PRO A 1 4632 ? 50.302  120.996 101.910 1.00 26.93  ? 4632 PRO A CB    1 
ATOM   23113 C  CG    . PRO A 1 4632 ? 48.820  121.242 101.709 1.00 27.26  ? 4632 PRO A CG    1 
ATOM   23114 C  CD    . PRO A 1 4632 ? 48.715  122.317 100.640 1.00 25.62  ? 4632 PRO A CD    1 
ATOM   23115 N  N     . ARG A 1 4633 ? 50.311  119.489 99.093  1.00 28.10  ? 4633 ARG A N     1 
ATOM   23116 C  CA    . ARG A 1 4633 ? 50.570  118.312 98.277  1.00 24.48  ? 4633 ARG A CA    1 
ATOM   23117 C  C     . ARG A 1 4633 ? 51.509  118.605 97.116  1.00 20.48  ? 4633 ARG A C     1 
ATOM   23118 O  O     . ARG A 1 4633 ? 52.390  117.792 96.809  1.00 19.47  ? 4633 ARG A O     1 
ATOM   23119 C  CB    . ARG A 1 4633 ? 49.235  117.732 97.797  1.00 30.00  ? 4633 ARG A CB    1 
ATOM   23120 C  CG    . ARG A 1 4633 ? 49.367  116.432 97.008  1.00 38.25  ? 4633 ARG A CG    1 
ATOM   23121 C  CD    . ARG A 1 4633 ? 48.028  115.841 96.638  1.00 47.90  ? 4633 ARG A CD    1 
ATOM   23122 N  NE    . ARG A 1 4633 ? 47.205  116.639 95.748  1.00 50.54  ? 4633 ARG A NE    1 
ATOM   23123 C  CZ    . ARG A 1 4633 ? 46.055  117.173 96.137  1.00 53.28  ? 4633 ARG A CZ    1 
ATOM   23124 N  NH1   . ARG A 1 4633 ? 45.604  117.011 97.372  1.00 42.03  ? 4633 ARG A NH1   1 
ATOM   23125 N  NH2   . ARG A 1 4633 ? 45.342  117.893 95.275  1.00 60.13  ? 4633 ARG A NH2   1 
ATOM   23126 N  N     . SER A 1 4634 ? 51.352  119.760 96.472  1.00 17.05  ? 4634 SER A N     1 
ATOM   23127 C  CA    . SER A 1 4634 ? 52.246  120.123 95.379  1.00 16.43  ? 4634 SER A CA    1 
ATOM   23128 C  C     . SER A 1 4634 ? 53.667  120.389 95.872  1.00 14.27  ? 4634 SER A C     1 
ATOM   23129 O  O     . SER A 1 4634 ? 54.637  120.013 95.205  1.00 14.82  ? 4634 SER A O     1 
ATOM   23130 C  CB    . SER A 1 4634 ? 51.689  121.335 94.645  1.00 21.41  ? 4634 SER A CB    1 
ATOM   23131 O  OG    . SER A 1 4634 ? 51.675  122.461 95.498  1.00 27.19  ? 4634 SER A OG    1 
ATOM   23132 N  N     . PHE A 1 4635 ? 53.813  121.049 97.025  1.00 14.33  ? 4635 PHE A N     1 
ATOM   23133 C  CA    . PHE A 1 4635 ? 55.139  121.234 97.613  1.00 13.27  ? 4635 PHE A CA    1 
ATOM   23134 C  C     . PHE A 1 4635 ? 55.801  119.897 97.920  1.00 11.33  ? 4635 PHE A C     1 
ATOM   23135 O  O     . PHE A 1 4635 ? 57.007  119.726 97.695  1.00 10.80  ? 4635 PHE A O     1 
ATOM   23136 C  CB    . PHE A 1 4635 ? 55.032  122.085 98.878  1.00 14.94  ? 4635 PHE A CB    1 
ATOM   23137 C  CG    . PHE A 1 4635 ? 54.957  123.561 98.611  1.00 17.86  ? 4635 PHE A CG    1 
ATOM   23138 C  CD1   . PHE A 1 4635 ? 53.763  124.154 98.248  1.00 16.36  ? 4635 PHE A CD1   1 
ATOM   23139 C  CD2   . PHE A 1 4635 ? 56.071  124.365 98.788  1.00 20.66  ? 4635 PHE A CD2   1 
ATOM   23140 C  CE1   . PHE A 1 4635 ? 53.687  125.513 98.017  1.00 22.19  ? 4635 PHE A CE1   1 
ATOM   23141 C  CE2   . PHE A 1 4635 ? 56.000  125.726 98.565  1.00 17.41  ? 4635 PHE A CE2   1 
ATOM   23142 C  CZ    . PHE A 1 4635 ? 54.806  126.300 98.178  1.00 20.39  ? 4635 PHE A CZ    1 
ATOM   23143 N  N     . TYR A 1 4636 ? 55.035  118.938 98.440  1.00 13.34  ? 4636 TYR A N     1 
ATOM   23144 C  CA    . TYR A 1 4636 ? 55.600  117.616 98.691  1.00 13.61  ? 4636 TYR A CA    1 
ATOM   23145 C  C     . TYR A 1 4636 ? 56.016  116.932 97.392  1.00 11.05  ? 4636 TYR A C     1 
ATOM   23146 O  O     . TYR A 1 4636 ? 57.057  116.266 97.344  1.00 11.10  ? 4636 TYR A O     1 
ATOM   23147 C  CB    . TYR A 1 4636 ? 54.606  116.749 99.463  1.00 15.71  ? 4636 TYR A CB    1 
ATOM   23148 C  CG    . TYR A 1 4636 ? 54.125  117.361 100.762 1.00 16.54  ? 4636 TYR A CG    1 
ATOM   23149 C  CD1   . TYR A 1 4636 ? 54.909  118.274 101.456 1.00 17.36  ? 4636 TYR A CD1   1 
ATOM   23150 C  CD2   . TYR A 1 4636 ? 52.891  117.019 101.299 1.00 20.02  ? 4636 TYR A CD2   1 
ATOM   23151 C  CE1   . TYR A 1 4636 ? 54.476  118.835 102.643 1.00 21.68  ? 4636 TYR A CE1   1 
ATOM   23152 C  CE2   . TYR A 1 4636 ? 52.451  117.574 102.488 1.00 21.79  ? 4636 TYR A CE2   1 
ATOM   23153 C  CZ    . TYR A 1 4636 ? 53.248  118.480 103.155 1.00 25.01  ? 4636 TYR A CZ    1 
ATOM   23154 O  OH    . TYR A 1 4636 ? 52.817  119.036 104.337 1.00 29.08  ? 4636 TYR A OH    1 
ATOM   23155 N  N     . GLU A 1 4637 ? 55.220  117.085 96.329  1.00 11.04  ? 4637 GLU A N     1 
ATOM   23156 C  CA    . GLU A 1 4637 ? 55.517  116.398 95.073  1.00 11.32  ? 4637 GLU A CA    1 
ATOM   23157 C  C     . GLU A 1 4637 ? 56.657  117.048 94.291  1.00 8.34   ? 4637 GLU A C     1 
ATOM   23158 O  O     . GLU A 1 4637 ? 57.345  116.360 93.528  1.00 12.38  ? 4637 GLU A O     1 
ATOM   23159 C  CB    . GLU A 1 4637 ? 54.264  116.335 94.200  1.00 11.15  ? 4637 GLU A CB    1 
ATOM   23160 C  CG    . GLU A 1 4637 ? 53.193  115.380 94.703  1.00 13.93  ? 4637 GLU A CG    1 
ATOM   23161 C  CD    . GLU A 1 4637 ? 52.117  115.124 93.666  1.00 26.07  ? 4637 GLU A CD    1 
ATOM   23162 O  OE1   . GLU A 1 4637 ? 52.207  115.703 92.563  1.00 28.65  ? 4637 GLU A OE1   1 
ATOM   23163 O  OE2   . GLU A 1 4637 ? 51.172  114.360 93.957  1.00 32.69  ? 4637 GLU A OE2   1 
ATOM   23164 N  N     . ARG A 1 4638 ? 56.871  118.351 94.451  1.00 8.60   ? 4638 ARG A N     1 
ATOM   23165 C  CA    . ARG A 1 4638 ? 57.922  119.045 93.718  1.00 9.03   ? 4638 ARG A CA    1 
ATOM   23166 C  C     . ARG A 1 4638 ? 59.274  118.977 94.415  1.00 9.75   ? 4638 ARG A C     1 
ATOM   23167 O  O     . ARG A 1 4638 ? 60.246  119.546 93.908  1.00 10.82  ? 4638 ARG A O     1 
ATOM   23168 C  CB    . ARG A 1 4638 ? 57.527  120.506 93.480  1.00 7.27   ? 4638 ARG A CB    1 
ATOM   23169 C  CG    . ARG A 1 4638 ? 56.380  120.657 92.496  1.00 7.76   ? 4638 ARG A CG    1 
ATOM   23170 C  CD    . ARG A 1 4638 ? 55.913  122.090 92.372  1.00 13.15  ? 4638 ARG A CD    1 
ATOM   23171 N  NE    . ARG A 1 4638 ? 57.001  122.981 91.992  1.00 21.08  ? 4638 ARG A NE    1 
ATOM   23172 C  CZ    . ARG A 1 4638 ? 57.011  123.723 90.893  1.00 17.95  ? 4638 ARG A CZ    1 
ATOM   23173 N  NH1   . ARG A 1 4638 ? 56.001  123.709 90.040  1.00 13.92  ? 4638 ARG A NH1   1 
ATOM   23174 N  NH2   . ARG A 1 4638 ? 58.063  124.497 90.644  1.00 21.72  ? 4638 ARG A NH2   1 
ATOM   23175 N  N     . GLY A 1 4639 ? 59.359  118.289 95.548  1.00 7.72   ? 4639 GLY A N     1 
ATOM   23176 C  CA    . GLY A 1 4639 ? 60.618  118.155 96.258  1.00 7.69   ? 4639 GLY A CA    1 
ATOM   23177 C  C     . GLY A 1 4639 ? 61.151  119.456 96.814  1.00 8.66   ? 4639 GLY A C     1 
ATOM   23178 O  O     . GLY A 1 4639 ? 62.365  119.694 96.768  1.00 12.20  ? 4639 GLY A O     1 
ATOM   23179 N  N     . VAL A 1 4640 ? 60.270  120.309 97.333  1.00 6.89   ? 4640 VAL A N     1 
ATOM   23180 C  CA    . VAL A 1 4640 ? 60.697  121.569 97.927  1.00 8.46   ? 4640 VAL A CA    1 
ATOM   23181 C  C     . VAL A 1 4640 ? 61.463  121.280 99.209  1.00 10.17  ? 4640 VAL A C     1 
ATOM   23182 O  O     . VAL A 1 4640 ? 61.000  120.517 100.067 1.00 11.88  ? 4640 VAL A O     1 
ATOM   23183 C  CB    . VAL A 1 4640 ? 59.483  122.471 98.191  1.00 9.06   ? 4640 VAL A CB    1 
ATOM   23184 C  CG1   . VAL A 1 4640 ? 59.922  123.798 98.787  1.00 12.02  ? 4640 VAL A CG1   1 
ATOM   23185 C  CG2   . VAL A 1 4640 ? 58.694  122.675 96.911  1.00 11.11  ? 4640 VAL A CG2   1 
ATOM   23186 N  N     . ALA A 1 4641 ? 62.640  121.884 99.350  1.00 11.58  ? 4641 ALA A N     1 
ATOM   23187 C  CA    . ALA A 1 4641 ? 63.493  121.573 100.489 1.00 10.66  ? 4641 ALA A CA    1 
ATOM   23188 C  C     . ALA A 1 4641 ? 64.341  122.784 100.848 1.00 10.94  ? 4641 ALA A C     1 
ATOM   23189 O  O     . ALA A 1 4641 ? 64.203  123.863 100.271 1.00 9.92   ? 4641 ALA A O     1 
ATOM   23190 C  CB    . ALA A 1 4641 ? 64.382  120.357 100.205 1.00 8.41   ? 4641 ALA A CB    1 
ATOM   23191 N  N     . VAL A 1 4642 ? 65.220  122.590 101.828 1.00 10.53  ? 4642 VAL A N     1 
ATOM   23192 C  CA    . VAL A 1 4642 ? 66.173  123.604 102.263 1.00 9.39   ? 4642 VAL A CA    1 
ATOM   23193 C  C     . VAL A 1 4642 ? 67.542  122.946 102.371 1.00 12.50  ? 4642 VAL A C     1 
ATOM   23194 O  O     . VAL A 1 4642 ? 67.659  121.829 102.887 1.00 12.45  ? 4642 VAL A O     1 
ATOM   23195 C  CB    . VAL A 1 4642 ? 65.760  124.242 103.603 1.00 10.65  ? 4642 VAL A CB    1 
ATOM   23196 C  CG1   . VAL A 1 4642 ? 66.836  125.202 104.096 1.00 15.16  ? 4642 VAL A CG1   1 
ATOM   23197 C  CG2   . VAL A 1 4642 ? 64.428  124.965 103.464 1.00 9.33   ? 4642 VAL A CG2   1 
ATOM   23198 N  N     . LEU A 1 4643 ? 68.567  123.629 101.872 1.00 15.08  ? 4643 LEU A N     1 
ATOM   23199 C  CA    . LEU A 1 4643 ? 69.939  123.148 101.918 1.00 15.42  ? 4643 LEU A CA    1 
ATOM   23200 C  C     . LEU A 1 4643 ? 70.780  124.057 102.802 1.00 20.21  ? 4643 LEU A C     1 
ATOM   23201 O  O     . LEU A 1 4643 ? 70.600  125.279 102.801 1.00 19.70  ? 4643 LEU A O     1 
ATOM   23202 C  CB    . LEU A 1 4643 ? 70.548  123.088 100.515 1.00 16.57  ? 4643 LEU A CB    1 
ATOM   23203 C  CG    . LEU A 1 4643 ? 69.817  122.230 99.483  1.00 18.12  ? 4643 LEU A CG    1 
ATOM   23204 C  CD1   . LEU A 1 4643 ? 70.628  122.137 98.202  1.00 16.84  ? 4643 LEU A CD1   1 
ATOM   23205 C  CD2   . LEU A 1 4643 ? 69.513  120.847 100.037 1.00 14.98  ? 4643 LEU A CD2   1 
ATOM   23206 N  N     . CYS A 1 4644 ? 71.699  123.456 103.562 1.00 22.10  ? 4644 CYS A N     1 
ATOM   23207 C  CA    . CYS A 1 4644 ? 72.629  124.258 104.349 1.00 21.94  ? 4644 CYS A CA    1 
ATOM   23208 C  C     . CYS A 1 4644 ? 73.644  124.965 103.460 1.00 22.90  ? 4644 CYS A C     1 
ATOM   23209 O  O     . CYS A 1 4644 ? 74.065  126.084 103.772 1.00 28.72  ? 4644 CYS A O     1 
ATOM   23210 C  CB    . CYS A 1 4644 ? 73.339  123.383 105.382 1.00 25.90  ? 4644 CYS A CB    1 
ATOM   23211 S  SG    . CYS A 1 4644 ? 72.288  122.849 106.750 1.00 37.65  ? 4644 CYS A SG    1 
ATOM   23212 N  N     . THR A 1 4645 ? 74.045  124.333 102.361 1.00 23.54  ? 4645 THR A N     1 
ATOM   23213 C  CA    . THR A 1 4645 ? 74.913  124.965 101.373 1.00 27.94  ? 4645 THR A CA    1 
ATOM   23214 C  C     . THR A 1 4645 ? 74.299  124.868 99.982  1.00 29.64  ? 4645 THR A C     1 
ATOM   23215 O  O     . THR A 1 4645 ? 73.733  123.839 99.614  1.00 31.22  ? 4645 THR A O     1 
ATOM   23216 C  CB    . THR A 1 4645 ? 76.318  124.330 101.348 1.00 35.50  ? 4645 THR A CB    1 
ATOM   23217 O  OG1   . THR A 1 4645 ? 76.217  122.945 100.993 1.00 31.90  ? 4645 THR A OG1   1 
ATOM   23218 C  CG2   . THR A 1 4645 ? 76.996  124.463 102.698 1.00 35.99  ? 4645 THR A CG2   1 
HETATM 23219 P  PB    . ADP B 2 .    ? 69.481  95.289  115.277 1.00 2.40   ? 4701 ADP A PB    1 
HETATM 23220 O  O1B   . ADP B 2 .    ? 70.965  95.397  115.527 1.00 4.81   ? 4701 ADP A O1B   1 
HETATM 23221 O  O2B   . ADP B 2 .    ? 68.931  96.453  114.491 1.00 7.18   ? 4701 ADP A O2B   1 
HETATM 23222 O  O3B   . ADP B 2 .    ? 69.085  93.951  114.699 1.00 3.95   ? 4701 ADP A O3B   1 
HETATM 23223 P  PA    . ADP B 2 .    ? 68.504  94.237  117.834 1.00 3.35   ? 4701 ADP A PA    1 
HETATM 23224 O  O1A   . ADP B 2 .    ? 67.399  93.363  117.340 1.00 3.74   ? 4701 ADP A O1A   1 
HETATM 23225 O  O2A   . ADP B 2 .    ? 69.795  93.592  118.213 1.00 11.36  ? 4701 ADP A O2A   1 
HETATM 23226 O  O3A   . ADP B 2 .    ? 68.790  95.364  116.731 1.00 5.50   ? 4701 ADP A O3A   1 
HETATM 23227 O  "O5'" . ADP B 2 .    ? 67.983  95.130  119.060 1.00 6.24   ? 4701 ADP A "O5'" 1 
HETATM 23228 C  "C5'" . ADP B 2 .    ? 68.907  96.088  119.634 1.00 5.81   ? 4701 ADP A "C5'" 1 
HETATM 23229 C  "C4'" . ADP B 2 .    ? 68.419  96.501  121.001 1.00 6.53   ? 4701 ADP A "C4'" 1 
HETATM 23230 O  "O4'" . ADP B 2 .    ? 67.117  97.128  120.868 1.00 10.17  ? 4701 ADP A "O4'" 1 
HETATM 23231 C  "C3'" . ADP B 2 .    ? 68.225  95.367  122.018 1.00 7.05   ? 4701 ADP A "C3'" 1 
HETATM 23232 O  "O3'" . ADP B 2 .    ? 68.584  95.797  123.324 1.00 14.05  ? 4701 ADP A "O3'" 1 
HETATM 23233 C  "C2'" . ADP B 2 .    ? 66.720  95.107  121.927 1.00 5.89   ? 4701 ADP A "C2'" 1 
HETATM 23234 O  "O2'" . ADP B 2 .    ? 66.189  94.452  123.058 1.00 10.00  ? 4701 ADP A "O2'" 1 
HETATM 23235 C  "C1'" . ADP B 2 .    ? 66.222  96.538  121.781 1.00 7.78   ? 4701 ADP A "C1'" 1 
HETATM 23236 N  N9    . ADP B 2 .    ? 64.872  96.646  121.244 1.00 5.66   ? 4701 ADP A N9    1 
HETATM 23237 C  C8    . ADP B 2 .    ? 64.514  96.646  119.919 1.00 4.21   ? 4701 ADP A C8    1 
HETATM 23238 N  N7    . ADP B 2 .    ? 63.223  96.761  119.730 1.00 3.12   ? 4701 ADP A N7    1 
HETATM 23239 C  C5    . ADP B 2 .    ? 62.694  96.847  121.009 1.00 2.97   ? 4701 ADP A C5    1 
HETATM 23240 C  C6    . ADP B 2 .    ? 61.375  96.984  121.480 1.00 2.67   ? 4701 ADP A C6    1 
HETATM 23241 N  N6    . ADP B 2 .    ? 60.311  97.062  120.685 1.00 2.88   ? 4701 ADP A N6    1 
HETATM 23242 N  N1    . ADP B 2 .    ? 61.193  97.038  122.820 1.00 3.68   ? 4701 ADP A N1    1 
HETATM 23243 C  C2    . ADP B 2 .    ? 62.267  96.958  123.614 1.00 4.71   ? 4701 ADP A C2    1 
HETATM 23244 N  N3    . ADP B 2 .    ? 63.550  96.829  123.286 1.00 4.54   ? 4701 ADP A N3    1 
HETATM 23245 C  C4    . ADP B 2 .    ? 63.701  96.779  121.952 1.00 4.40   ? 4701 ADP A C4    1 
HETATM 23246 P  PG    . ATP C 3 .    ? 98.966  97.169  126.232 1.00 2.56   ? 4702 ATP A PG    1 
HETATM 23247 O  O1G   . ATP C 3 .    ? 98.249  98.372  125.674 1.00 4.26   ? 4702 ATP A O1G   1 
HETATM 23248 O  O2G   . ATP C 3 .    ? 98.116  95.923  126.214 1.00 5.40   ? 4702 ATP A O2G   1 
HETATM 23249 O  O3G   . ATP C 3 .    ? 100.321 96.958  125.606 1.00 5.13   ? 4702 ATP A O3G   1 
HETATM 23250 P  PB    . ATP C 3 .    ? 98.259  97.917  128.982 1.00 1.32   ? 4702 ATP A PB    1 
HETATM 23251 O  O1B   . ATP C 3 .    ? 97.739  99.287  128.702 1.00 2.58   ? 4702 ATP A O1B   1 
HETATM 23252 O  O2B   . ATP C 3 .    ? 97.301  96.797  129.214 1.00 1.80   ? 4702 ATP A O2B   1 
HETATM 23253 O  O3B   . ATP C 3 .    ? 99.240  97.496  127.789 1.00 3.54   ? 4702 ATP A O3B   1 
HETATM 23254 P  PA    . ATP C 3 .    ? 99.750  96.892  131.285 1.00 3.38   ? 4702 ATP A PA    1 
HETATM 23255 O  O1A   . ATP C 3 .    ? 99.909  95.582  130.591 1.00 8.29   ? 4702 ATP A O1A   1 
HETATM 23256 O  O2A   . ATP C 3 .    ? 98.847  96.957  132.472 1.00 1.69   ? 4702 ATP A O2A   1 
HETATM 23257 O  O3A   . ATP C 3 .    ? 99.280  97.988  130.213 1.00 3.30   ? 4702 ATP A O3A   1 
HETATM 23258 O  "O5'" . ATP C 3 .    ? 101.199 97.448  131.684 1.00 9.75   ? 4702 ATP A "O5'" 1 
HETATM 23259 C  "C5'" . ATP C 3 .    ? 101.301 98.578  132.584 1.00 4.43   ? 4702 ATP A "C5'" 1 
HETATM 23260 C  "C4'" . ATP C 3 .    ? 102.747 98.771  132.966 1.00 5.51   ? 4702 ATP A "C4'" 1 
HETATM 23261 O  "O4'" . ATP C 3 .    ? 102.811 99.542  134.190 1.00 8.64   ? 4702 ATP A "O4'" 1 
HETATM 23262 C  "C3'" . ATP C 3 .    ? 103.513 97.495  133.319 1.00 7.92   ? 4702 ATP A "C3'" 1 
HETATM 23263 O  "O3'" . ATP C 3 .    ? 104.915 97.724  133.322 1.00 20.13  ? 4702 ATP A "O3'" 1 
HETATM 23264 C  "C2'" . ATP C 3 .    ? 102.988 97.242  134.733 1.00 6.66   ? 4702 ATP A "C2'" 1 
HETATM 23265 O  "O2'" . ATP C 3 .    ? 103.831 96.416  135.508 1.00 15.86  ? 4702 ATP A "O2'" 1 
HETATM 23266 C  "C1'" . ATP C 3 .    ? 102.906 98.663  135.290 1.00 5.56   ? 4702 ATP A "C1'" 1 
HETATM 23267 N  N9    . ATP C 3 .    ? 101.746 98.878  136.141 1.00 4.42   ? 4702 ATP A N9    1 
HETATM 23268 C  C8    . ATP C 3 .    ? 100.469 98.417  135.945 1.00 3.13   ? 4702 ATP A C8    1 
HETATM 23269 N  N7    . ATP C 3 .    ? 99.650  98.771  136.909 1.00 3.16   ? 4702 ATP A N7    1 
HETATM 23270 C  C5    . ATP C 3 .    ? 100.442 99.492  137.793 1.00 3.23   ? 4702 ATP A C5    1 
HETATM 23271 C  C6    . ATP C 3 .    ? 100.165 100.131 139.016 1.00 3.71   ? 4702 ATP A C6    1 
HETATM 23272 N  N6    . ATP C 3 .    ? 98.964  100.152 139.584 1.00 2.79   ? 4702 ATP A N6    1 
HETATM 23273 N  N1    . ATP C 3 .    ? 101.193 100.760 139.634 1.00 4.50   ? 4702 ATP A N1    1 
HETATM 23274 C  C2    . ATP C 3 .    ? 102.402 100.734 139.058 1.00 4.05   ? 4702 ATP A C2    1 
HETATM 23275 N  N3    . ATP C 3 .    ? 102.779 100.167 137.915 1.00 6.11   ? 4702 ATP A N3    1 
HETATM 23276 C  C4    . ATP C 3 .    ? 101.738 99.557  137.328 1.00 3.88   ? 4702 ATP A C4    1 
HETATM 23277 P  PB    . ADP D 2 .    ? 122.667 96.106  107.127 1.00 1.41   ? 4703 ADP A PB    1 
HETATM 23278 O  O1B   . ADP D 2 .    ? 122.571 95.100  108.245 1.00 4.99   ? 4703 ADP A O1B   1 
HETATM 23279 O  O2B   . ADP D 2 .    ? 121.787 95.762  105.952 1.00 5.33   ? 4703 ADP A O2B   1 
HETATM 23280 O  O3B   . ADP D 2 .    ? 122.477 97.525  107.604 1.00 3.47   ? 4703 ADP A O3B   1 
HETATM 23281 P  PA    . ADP D 2 .    ? 125.142 94.768  106.283 1.00 4.93   ? 4703 ADP A PA    1 
HETATM 23282 O  O1A   . ADP D 2 .    ? 125.664 94.245  107.580 1.00 4.12   ? 4703 ADP A O1A   1 
HETATM 23283 O  O2A   . ADP D 2 .    ? 124.420 93.818  105.385 1.00 9.09   ? 4703 ADP A O2A   1 
HETATM 23284 O  O3A   . ADP D 2 .    ? 124.184 96.018  106.584 1.00 6.50   ? 4703 ADP A O3A   1 
HETATM 23285 O  "O5'" . ADP D 2 .    ? 126.332 95.471  105.469 1.00 7.17   ? 4703 ADP A "O5'" 1 
HETATM 23286 C  "C5'" . ADP D 2 .    ? 127.064 96.553  106.096 1.00 6.42   ? 4703 ADP A "C5'" 1 
HETATM 23287 C  "C4'" . ADP D 2 .    ? 128.149 97.028  105.163 1.00 6.51   ? 4703 ADP A "C4'" 1 
HETATM 23288 O  "O4'" . ADP D 2 .    ? 128.925 98.054  105.835 1.00 7.94   ? 4703 ADP A "O4'" 1 
HETATM 23289 C  "C3'" . ADP D 2 .    ? 129.171 95.971  104.727 1.00 8.13   ? 4703 ADP A "C3'" 1 
HETATM 23290 O  "O3'" . ADP D 2 .    ? 129.669 96.248  103.426 1.00 10.80  ? 4703 ADP A "O3'" 1 
HETATM 23291 C  "C2'" . ADP D 2 .    ? 130.273 96.158  105.771 1.00 7.57   ? 4703 ADP A "C2'" 1 
HETATM 23292 O  "O2'" . ADP D 2 .    ? 131.519 95.631  105.369 1.00 19.90  ? 4703 ADP A "O2'" 1 
HETATM 23293 C  "C1'" . ADP D 2 .    ? 130.283 97.678  105.873 1.00 6.53   ? 4703 ADP A "C1'" 1 
HETATM 23294 N  N9    . ADP D 2 .    ? 130.859 98.185  107.111 1.00 5.62   ? 4703 ADP A N9    1 
HETATM 23295 C  C8    . ADP D 2 .    ? 130.393 99.244  107.848 1.00 4.60   ? 4703 ADP A C8    1 
HETATM 23296 N  N7    . ADP D 2 .    ? 131.105 99.486  108.919 1.00 6.19   ? 4703 ADP A N7    1 
HETATM 23297 C  C5    . ADP D 2 .    ? 132.112 98.534  108.883 1.00 5.40   ? 4703 ADP A C5    1 
HETATM 23298 C  C6    . ADP D 2 .    ? 133.192 98.270  109.746 1.00 3.87   ? 4703 ADP A C6    1 
HETATM 23299 N  N6    . ADP D 2 .    ? 133.441 98.969  110.850 1.00 3.70   ? 4703 ADP A N6    1 
HETATM 23300 N  N1    . ADP D 2 .    ? 134.015 97.246  109.422 1.00 7.21   ? 4703 ADP A N1    1 
HETATM 23301 C  C2    . ADP D 2 .    ? 133.756 96.547  108.310 1.00 5.91   ? 4703 ADP A C2    1 
HETATM 23302 N  N3    . ADP D 2 .    ? 132.775 96.705  107.427 1.00 4.94   ? 4703 ADP A N3    1 
HETATM 23303 C  C4    . ADP D 2 .    ? 131.975 97.726  107.771 1.00 5.55   ? 4703 ADP A C4    1 
HETATM 23304 P  PB    . ADP E 2 .    ? 115.515 85.950  77.058  1.00 6.43   ? 4704 ADP A PB    1 
HETATM 23305 O  O1B   . ADP E 2 .    ? 115.668 87.422  76.770  1.00 8.14   ? 4704 ADP A O1B   1 
HETATM 23306 O  O2B   . ADP E 2 .    ? 116.357 85.490  78.221  1.00 7.96   ? 4704 ADP A O2B   1 
HETATM 23307 O  O3B   . ADP E 2 .    ? 114.072 85.528  77.180  1.00 10.11  ? 4704 ADP A O3B   1 
HETATM 23308 P  PA    . ADP E 2 .    ? 116.613 83.675  75.555  1.00 6.27   ? 4704 ADP A PA    1 
HETATM 23309 O  O1A   . ADP E 2 .    ? 117.974 83.561  76.156  1.00 5.55   ? 4704 ADP A O1A   1 
HETATM 23310 O  O2A   . ADP E 2 .    ? 115.555 82.730  76.019  1.00 16.03  ? 4704 ADP A O2A   1 
HETATM 23311 O  O3A   . ADP E 2 .    ? 116.090 85.176  75.764  1.00 9.59   ? 4704 ADP A O3A   1 
HETATM 23312 O  "O5'" . ADP E 2 .    ? 116.720 83.610  73.957  1.00 10.25  ? 4704 ADP A "O5'" 1 
HETATM 23313 C  "C5'" . ADP E 2 .    ? 115.489 83.413  73.219  1.00 11.52  ? 4704 ADP A "C5'" 1 
HETATM 23314 C  "C4'" . ADP E 2 .    ? 115.713 83.727  71.760  1.00 11.64  ? 4704 ADP A "C4'" 1 
HETATM 23315 O  "O4'" . ADP E 2 .    ? 116.197 85.085  71.618  1.00 10.99  ? 4704 ADP A "O4'" 1 
HETATM 23316 C  "C3'" . ADP E 2 .    ? 116.771 82.902  71.024  1.00 12.05  ? 4704 ADP A "C3'" 1 
HETATM 23317 O  "O3'" . ADP E 2 .    ? 116.294 81.609  70.671  1.00 22.99  ? 4704 ADP A "O3'" 1 
HETATM 23318 C  "C2'" . ADP E 2 .    ? 117.017 83.798  69.808  1.00 11.87  ? 4704 ADP A "C2'" 1 
HETATM 23319 O  "O2'" . ADP E 2 .    ? 116.016 83.647  68.826  1.00 15.26  ? 4704 ADP A "O2'" 1 
HETATM 23320 C  "C1'" . ADP E 2 .    ? 116.957 85.192  70.433  1.00 9.37   ? 4704 ADP A "C1'" 1 
HETATM 23321 N  N9    . ADP E 2 .    ? 118.263 85.748  70.769  1.00 8.74   ? 4704 ADP A N9    1 
HETATM 23322 C  C8    . ADP E 2 .    ? 118.577 86.467  71.895  1.00 9.52   ? 4704 ADP A C8    1 
HETATM 23323 N  N7    . ADP E 2 .    ? 119.825 86.859  71.931  1.00 10.54  ? 4704 ADP A N7    1 
HETATM 23324 C  C5    . ADP E 2 .    ? 120.368 86.385  70.746  1.00 9.28   ? 4704 ADP A C5    1 
HETATM 23325 C  C6    . ADP E 2 .    ? 121.660 86.480  70.195  1.00 9.17   ? 4704 ADP A C6    1 
HETATM 23326 N  N6    . ADP E 2 .    ? 122.673 87.105  70.788  1.00 8.11   ? 4704 ADP A N6    1 
HETATM 23327 N  N1    . ADP E 2 .    ? 121.870 85.896  68.991  1.00 10.37  ? 4704 ADP A N1    1 
HETATM 23328 C  C2    . ADP E 2 .    ? 120.846 85.268  68.400  1.00 9.42   ? 4704 ADP A C2    1 
HETATM 23329 N  N3    . ADP E 2 .    ? 119.595 85.116  68.823  1.00 9.06   ? 4704 ADP A N3    1 
HETATM 23330 C  C4    . ADP E 2 .    ? 119.414 85.703  70.017  1.00 7.89   ? 4704 ADP A C4    1 
HETATM 23331 MG MG    . MG  F 4 .    ? 70.288  92.222  114.716 1.00 7.25   ? 4705 MG  A MG    1 
HETATM 23332 MG MG    . MG  G 4 .    ? 98.121  94.749  127.717 1.00 2.65   ? 4706 MG  A MG    1 
HETATM 23333 O  O     . HOH H 5 .    ? 124.953 103.847 89.520  1.00 19.06  ? 4801 HOH A O     1 
HETATM 23334 O  O     . HOH H 5 .    ? 117.004 88.507  70.425  1.00 11.81  ? 4802 HOH A O     1 
HETATM 23335 O  O     . HOH H 5 .    ? 73.388  133.990 59.079  1.00 61.75  ? 4803 HOH A O     1 
HETATM 23336 O  O     . HOH H 5 .    ? 136.347 86.687  65.935  1.00 26.16  ? 4804 HOH A O     1 
HETATM 23337 O  O     . HOH H 5 .    ? 56.941  65.543  116.928 1.00 14.02  ? 4805 HOH A O     1 
HETATM 23338 O  O     . HOH H 5 .    ? 60.697  101.173 63.941  1.00 16.94  ? 4806 HOH A O     1 
HETATM 23339 O  O     . HOH H 5 .    ? 54.367  106.980 135.732 1.00 29.81  ? 4807 HOH A O     1 
HETATM 23340 O  O     . HOH H 5 .    ? 135.196 100.643 146.085 1.00 42.40  ? 4808 HOH A O     1 
HETATM 23341 O  O     . HOH H 5 .    ? 62.888  101.285 66.081  1.00 17.60  ? 4809 HOH A O     1 
HETATM 23342 O  O     . HOH H 5 .    ? 154.654 92.591  94.621  1.00 32.42  ? 4810 HOH A O     1 
HETATM 23343 O  O     . HOH H 5 .    ? 35.817  89.620  93.728  1.00 40.14  ? 4811 HOH A O     1 
HETATM 23344 O  O     . HOH H 5 .    ? 74.245  55.927  108.346 1.00 44.94  ? 4812 HOH A O     1 
HETATM 23345 O  O     . HOH H 5 .    ? 58.566  99.986  76.383  1.00 23.68  ? 4813 HOH A O     1 
HETATM 23346 O  O     . HOH H 5 .    ? 127.072 94.816  89.418  1.00 8.91   ? 4814 HOH A O     1 
HETATM 23347 O  O     . HOH H 5 .    ? 56.118  108.417 78.558  1.00 7.40   ? 4815 HOH A O     1 
HETATM 23348 O  O     . HOH H 5 .    ? 53.304  99.577  136.078 1.00 18.03  ? 4816 HOH A O     1 
HETATM 23349 O  O     . HOH H 5 .    ? 61.183  113.263 99.700  1.00 9.59   ? 4817 HOH A O     1 
HETATM 23350 O  O     . HOH H 5 .    ? 109.387 105.399 143.929 1.00 23.64  ? 4818 HOH A O     1 
HETATM 23351 O  O     . HOH H 5 .    ? 52.193  103.732 122.185 1.00 33.47  ? 4819 HOH A O     1 
HETATM 23352 O  O     . HOH H 5 .    ? 60.919  135.631 97.050  1.00 31.61  ? 4820 HOH A O     1 
HETATM 23353 O  O     . HOH H 5 .    ? 67.436  72.701  80.678  1.00 29.50  ? 4821 HOH A O     1 
HETATM 23354 O  O     . HOH H 5 .    ? 56.204  80.610  129.480 1.00 8.48   ? 4822 HOH A O     1 
HETATM 23355 O  O     . HOH H 5 .    ? 100.097 94.566  128.454 1.00 3.86   ? 4823 HOH A O     1 
HETATM 23356 O  O     . HOH H 5 .    ? 75.321  95.179  73.997  1.00 9.73   ? 4824 HOH A O     1 
HETATM 23357 O  O     . HOH H 5 .    ? 60.133  101.857 105.799 1.00 6.39   ? 4825 HOH A O     1 
HETATM 23358 O  O     . HOH H 5 .    ? 49.727  103.951 126.295 1.00 21.52  ? 4826 HOH A O     1 
HETATM 23359 O  O     . HOH H 5 .    ? 78.414  95.939  98.587  1.00 31.02  ? 4827 HOH A O     1 
HETATM 23360 O  O     . HOH H 5 .    ? 62.864  73.539  76.544  1.00 31.91  ? 4828 HOH A O     1 
HETATM 23361 O  O     . HOH H 5 .    ? 50.443  64.091  123.005 1.00 8.50   ? 4829 HOH A O     1 
HETATM 23362 O  O     . HOH H 5 .    ? 113.421 71.879  108.618 1.00 16.94  ? 4830 HOH A O     1 
HETATM 23363 O  O     . HOH H 5 .    ? 66.771  135.646 98.228  1.00 38.18  ? 4831 HOH A O     1 
HETATM 23364 O  O     . HOH H 5 .    ? 44.291  113.709 90.952  1.00 21.18  ? 4832 HOH A O     1 
HETATM 23365 O  O     . HOH H 5 .    ? 60.326  51.970  120.881 1.00 33.49  ? 4833 HOH A O     1 
HETATM 23366 O  O     . HOH H 5 .    ? 111.421 108.003 143.652 1.00 21.54  ? 4834 HOH A O     1 
HETATM 23367 O  O     . HOH H 5 .    ? 119.616 123.223 134.654 1.00 38.20  ? 4835 HOH A O     1 
HETATM 23368 O  O     . HOH H 5 .    ? 110.374 94.094  78.344  1.00 19.38  ? 4836 HOH A O     1 
HETATM 23369 O  O     . HOH H 5 .    ? 139.085 106.699 78.150  1.00 38.02  ? 4837 HOH A O     1 
HETATM 23370 O  O     . HOH H 5 .    ? 85.910  86.566  68.598  1.00 22.69  ? 4838 HOH A O     1 
HETATM 23371 O  O     . HOH H 5 .    ? 42.792  108.506 100.016 1.00 19.62  ? 4839 HOH A O     1 
HETATM 23372 O  O     . HOH H 5 .    ? 62.519  104.826 70.900  1.00 24.14  ? 4840 HOH A O     1 
HETATM 23373 O  O     . HOH H 5 .    ? 116.828 92.268  133.552 1.00 20.81  ? 4841 HOH A O     1 
HETATM 23374 O  O     . HOH H 5 .    ? 149.198 109.131 90.676  1.00 21.14  ? 4842 HOH A O     1 
HETATM 23375 O  O     . HOH H 5 .    ? 146.376 101.103 76.965  1.00 44.29  ? 4843 HOH A O     1 
HETATM 23376 O  O     . HOH H 5 .    ? 81.422  67.418  112.089 1.00 24.58  ? 4844 HOH A O     1 
HETATM 23377 O  O     . HOH H 5 .    ? 84.861  70.391  124.945 1.00 5.04   ? 4845 HOH A O     1 
HETATM 23378 O  O     . HOH H 5 .    ? 84.976  85.080  150.179 1.00 26.72  ? 4846 HOH A O     1 
HETATM 23379 O  O     . HOH H 5 .    ? 82.344  91.933  108.196 1.00 14.08  ? 4847 HOH A O     1 
HETATM 23380 O  O     . HOH H 5 .    ? 61.727  62.216  111.575 1.00 20.00  ? 4848 HOH A O     1 
HETATM 23381 O  O     . HOH H 5 .    ? 133.830 94.188  93.037  1.00 13.39  ? 4849 HOH A O     1 
HETATM 23382 O  O     . HOH H 5 .    ? 119.536 109.566 109.494 1.00 13.52  ? 4850 HOH A O     1 
HETATM 23383 O  O     . HOH H 5 .    ? 115.843 79.763  68.523  1.00 17.51  ? 4851 HOH A O     1 
HETATM 23384 O  O     . HOH H 5 .    ? 100.621 80.792  79.480  1.00 27.56  ? 4852 HOH A O     1 
HETATM 23385 O  O     . HOH H 5 .    ? 58.648  95.687  101.492 1.00 8.39   ? 4853 HOH A O     1 
HETATM 23386 O  O     . HOH H 5 .    ? 37.402  108.544 84.679  1.00 38.81  ? 4854 HOH A O     1 
HETATM 23387 O  O     . HOH H 5 .    ? 67.111  92.520  105.617 1.00 9.50   ? 4855 HOH A O     1 
HETATM 23388 O  O     . HOH H 5 .    ? 140.316 100.229 113.872 1.00 19.03  ? 4856 HOH A O     1 
HETATM 23389 O  O     . HOH H 5 .    ? 60.773  96.871  117.397 1.00 4.14   ? 4857 HOH A O     1 
HETATM 23390 O  O     . HOH H 5 .    ? 86.987  51.867  144.716 1.00 42.84  ? 4858 HOH A O     1 
HETATM 23391 O  O     . HOH H 5 .    ? 62.855  88.628  86.651  1.00 23.77  ? 4859 HOH A O     1 
HETATM 23392 O  O     . HOH H 5 .    ? 103.120 77.653  56.321  1.00 15.29  ? 4860 HOH A O     1 
HETATM 23393 O  O     . HOH H 5 .    ? 111.702 76.708  82.974  1.00 23.32  ? 4861 HOH A O     1 
HETATM 23394 O  O     . HOH H 5 .    ? 109.415 108.602 113.981 1.00 9.48   ? 4862 HOH A O     1 
HETATM 23395 O  O     . HOH H 5 .    ? 75.513  113.181 51.717  1.00 39.60  ? 4863 HOH A O     1 
HETATM 23396 O  O     . HOH H 5 .    ? 81.251  97.155  69.059  1.00 7.97   ? 4864 HOH A O     1 
HETATM 23397 O  O     . HOH H 5 .    ? 99.720  66.993  63.817  1.00 21.48  ? 4865 HOH A O     1 
HETATM 23398 O  O     . HOH H 5 .    ? 122.061 101.005 150.223 1.00 35.25  ? 4866 HOH A O     1 
HETATM 23399 O  O     . HOH H 5 .    ? 86.971  81.540  108.565 1.00 15.29  ? 4867 HOH A O     1 
HETATM 23400 O  O     . HOH H 5 .    ? 135.418 98.331  71.495  1.00 21.25  ? 4868 HOH A O     1 
HETATM 23401 O  O     . HOH H 5 .    ? 57.474  60.375  140.685 1.00 33.58  ? 4869 HOH A O     1 
HETATM 23402 O  O     . HOH H 5 .    ? 117.943 79.995  73.712  1.00 19.05  ? 4870 HOH A O     1 
HETATM 23403 O  O     . HOH H 5 .    ? 134.335 93.074  136.175 1.00 39.40  ? 4871 HOH A O     1 
HETATM 23404 O  O     . HOH H 5 .    ? 129.008 98.716  50.598  1.00 27.68  ? 4872 HOH A O     1 
HETATM 23405 O  O     . HOH H 5 .    ? 96.812  86.334  77.341  1.00 29.29  ? 4873 HOH A O     1 
HETATM 23406 O  O     . HOH H 5 .    ? 85.168  102.370 115.230 1.00 21.05  ? 4874 HOH A O     1 
HETATM 23407 O  O     . HOH H 5 .    ? 142.224 105.916 104.765 1.00 14.12  ? 4875 HOH A O     1 
HETATM 23408 O  O     . HOH H 5 .    ? 99.354  89.562  121.569 1.00 7.10   ? 4876 HOH A O     1 
HETATM 23409 O  O     . HOH H 5 .    ? 65.730  129.170 77.741  1.00 32.22  ? 4877 HOH A O     1 
HETATM 23410 O  O     . HOH H 5 .    ? 138.410 93.737  112.658 1.00 22.14  ? 4878 HOH A O     1 
HETATM 23411 O  O     . HOH H 5 .    ? 109.244 73.642  61.749  1.00 24.13  ? 4879 HOH A O     1 
HETATM 23412 O  O     . HOH H 5 .    ? 60.624  102.368 61.007  1.00 13.14  ? 4880 HOH A O     1 
HETATM 23413 O  O     . HOH H 5 .    ? 63.025  62.537  138.941 1.00 35.73  ? 4881 HOH A O     1 
HETATM 23414 O  O     . HOH H 5 .    ? 111.499 112.987 104.627 1.00 49.74  ? 4882 HOH A O     1 
HETATM 23415 O  O     . HOH H 5 .    ? 131.704 91.521  120.161 1.00 14.85  ? 4883 HOH A O     1 
HETATM 23416 O  O     . HOH H 5 .    ? 97.588  67.216  77.665  1.00 33.12  ? 4884 HOH A O     1 
HETATM 23417 O  O     . HOH H 5 .    ? 126.511 79.675  94.908  1.00 4.45   ? 4885 HOH A O     1 
HETATM 23418 O  O     . HOH H 5 .    ? 116.820 109.943 92.265  1.00 25.45  ? 4886 HOH A O     1 
HETATM 23419 O  O     . HOH H 5 .    ? 98.486  92.963  126.681 1.00 3.98   ? 4887 HOH A O     1 
HETATM 23420 O  O     . HOH H 5 .    ? 126.045 94.341  44.781  1.00 44.19  ? 4888 HOH A O     1 
HETATM 23421 O  O     . HOH H 5 .    ? 52.217  59.488  126.671 1.00 21.00  ? 4889 HOH A O     1 
HETATM 23422 O  O     . HOH H 5 .    ? 27.669  93.138  91.491  1.00 49.79  ? 4890 HOH A O     1 
HETATM 23423 O  O     . HOH H 5 .    ? 52.094  63.945  132.626 1.00 23.66  ? 4891 HOH A O     1 
HETATM 23424 O  O     . HOH H 5 .    ? 126.178 84.456  126.616 1.00 30.74  ? 4892 HOH A O     1 
HETATM 23425 O  O     . HOH H 5 .    ? 124.178 86.561  97.334  1.00 10.52  ? 4893 HOH A O     1 
HETATM 23426 O  O     . HOH H 5 .    ? 63.196  75.699  85.470  1.00 31.56  ? 4894 HOH A O     1 
HETATM 23427 O  O     . HOH H 5 .    ? 58.095  109.570 128.403 1.00 24.20  ? 4895 HOH A O     1 
HETATM 23428 O  O     . HOH H 5 .    ? 101.799 94.791  74.747  1.00 27.18  ? 4896 HOH A O     1 
HETATM 23429 O  O     . HOH H 5 .    ? 133.070 90.455  102.581 1.00 25.56  ? 4897 HOH A O     1 
HETATM 23430 O  O     . HOH H 5 .    ? 44.466  84.430  104.780 1.00 13.49  ? 4898 HOH A O     1 
HETATM 23431 O  O     . HOH H 5 .    ? 59.679  129.904 66.070  1.00 39.12  ? 4899 HOH A O     1 
HETATM 23432 O  O     . HOH H 5 .    ? 89.199  79.790  54.901  1.00 25.62  ? 4900 HOH A O     1 
HETATM 23433 O  O     . HOH H 5 .    ? 132.528 81.284  82.337  1.00 15.82  ? 4901 HOH A O     1 
HETATM 23434 O  O     . HOH H 5 .    ? 150.056 88.985  94.638  1.00 33.13  ? 4902 HOH A O     1 
HETATM 23435 O  O     . HOH H 5 .    ? 59.903  101.367 108.166 1.00 5.26   ? 4903 HOH A O     1 
HETATM 23436 O  O     . HOH H 5 .    ? 90.301  91.047  55.208  1.00 15.65  ? 4904 HOH A O     1 
HETATM 23437 O  O     . HOH H 5 .    ? 60.627  104.373 112.934 1.00 14.63  ? 4905 HOH A O     1 
HETATM 23438 O  O     . HOH H 5 .    ? 113.612 97.315  39.244  1.00 43.86  ? 4906 HOH A O     1 
HETATM 23439 O  O     . HOH H 5 .    ? 119.108 118.493 138.390 1.00 43.98  ? 4907 HOH A O     1 
HETATM 23440 O  O     . HOH H 5 .    ? 53.852  100.749 85.201  1.00 3.10   ? 4908 HOH A O     1 
HETATM 23441 O  O     . HOH H 5 .    ? 102.327 52.825  135.561 1.00 32.73  ? 4909 HOH A O     1 
HETATM 23442 O  O     . HOH H 5 .    ? 108.825 85.268  104.023 1.00 14.88  ? 4910 HOH A O     1 
HETATM 23443 O  O     . HOH H 5 .    ? 98.171  95.828  75.084  1.00 45.22  ? 4911 HOH A O     1 
HETATM 23444 O  O     . HOH H 5 .    ? 123.898 70.875  70.827  1.00 25.09  ? 4912 HOH A O     1 
HETATM 23445 O  O     . HOH H 5 .    ? 59.677  68.006  112.741 1.00 22.10  ? 4913 HOH A O     1 
HETATM 23446 O  O     . HOH H 5 .    ? 37.818  110.870 118.168 1.00 34.79  ? 4914 HOH A O     1 
HETATM 23447 O  O     . HOH H 5 .    ? 129.690 90.906  111.832 1.00 10.92  ? 4915 HOH A O     1 
HETATM 23448 O  O     . HOH H 5 .    ? 50.716  118.511 88.361  1.00 37.98  ? 4916 HOH A O     1 
HETATM 23449 O  O     . HOH H 5 .    ? 80.141  56.385  110.226 1.00 34.62  ? 4917 HOH A O     1 
HETATM 23450 O  O     . HOH H 5 .    ? 117.946 71.430  114.669 1.00 21.07  ? 4918 HOH A O     1 
HETATM 23451 O  O     . HOH H 5 .    ? 38.340  92.949  85.663  1.00 22.72  ? 4919 HOH A O     1 
HETATM 23452 O  O     . HOH H 5 .    ? 145.121 105.481 109.359 1.00 27.72  ? 4920 HOH A O     1 
HETATM 23453 O  O     . HOH H 5 .    ? 70.121  74.925  118.948 1.00 25.09  ? 4921 HOH A O     1 
HETATM 23454 O  O     . HOH H 5 .    ? 74.881  77.589  92.298  1.00 15.40  ? 4922 HOH A O     1 
HETATM 23455 O  O     . HOH H 5 .    ? 65.328  105.990 117.690 1.00 11.77  ? 4923 HOH A O     1 
HETATM 23456 O  O     . HOH H 5 .    ? 67.152  94.610  43.619  1.00 22.13  ? 4924 HOH A O     1 
HETATM 23457 O  O     . HOH H 5 .    ? 50.540  58.583  129.550 1.00 32.57  ? 4925 HOH A O     1 
HETATM 23458 O  O     . HOH H 5 .    ? 41.814  109.440 93.876  1.00 17.14  ? 4926 HOH A O     1 
HETATM 23459 O  O     . HOH H 5 .    ? 61.012  121.773 93.686  1.00 9.40   ? 4927 HOH A O     1 
HETATM 23460 O  O     . HOH H 5 .    ? 42.647  83.077  140.372 1.00 24.39  ? 4928 HOH A O     1 
HETATM 23461 O  O     . HOH H 5 .    ? 89.731  82.097  71.566  1.00 23.11  ? 4929 HOH A O     1 
HETATM 23462 O  O     . HOH H 5 .    ? 101.242 50.868  127.853 1.00 27.42  ? 4930 HOH A O     1 
HETATM 23463 O  O     . HOH H 5 .    ? 62.392  72.561  73.226  1.00 29.68  ? 4931 HOH A O     1 
HETATM 23464 O  O     . HOH H 5 .    ? 43.928  87.855  108.633 1.00 8.48   ? 4932 HOH A O     1 
HETATM 23465 O  O     . HOH H 5 .    ? 77.342  90.665  70.891  1.00 6.25   ? 4933 HOH A O     1 
HETATM 23466 O  O     . HOH H 5 .    ? 112.602 96.902  106.387 1.00 7.99   ? 4934 HOH A O     1 
HETATM 23467 O  O     . HOH H 5 .    ? 126.650 85.444  100.635 1.00 19.85  ? 4935 HOH A O     1 
HETATM 23468 O  O     . HOH H 5 .    ? 66.362  93.856  103.643 1.00 12.62  ? 4936 HOH A O     1 
HETATM 23469 O  O     . HOH H 5 .    ? 64.497  54.224  134.640 1.00 40.16  ? 4937 HOH A O     1 
HETATM 23470 O  O     . HOH H 5 .    ? 51.824  100.757 117.998 1.00 14.34  ? 4938 HOH A O     1 
HETATM 23471 O  O     . HOH H 5 .    ? 80.104  59.288  131.040 1.00 18.77  ? 4939 HOH A O     1 
HETATM 23472 O  O     . HOH H 5 .    ? 114.611 104.730 46.398  1.00 22.15  ? 4940 HOH A O     1 
HETATM 23473 O  O     . HOH H 5 .    ? 60.816  107.078 66.000  1.00 17.07  ? 4941 HOH A O     1 
HETATM 23474 O  O     . HOH H 5 .    ? 69.289  71.889  128.453 1.00 10.13  ? 4942 HOH A O     1 
HETATM 23475 O  O     . HOH H 5 .    ? 46.798  76.856  116.750 1.00 4.16   ? 4943 HOH A O     1 
HETATM 23476 O  O     . HOH H 5 .    ? 78.263  104.441 77.280  1.00 21.64  ? 4944 HOH A O     1 
HETATM 23477 O  O     . HOH H 5 .    ? 104.507 83.635  49.058  1.00 21.88  ? 4945 HOH A O     1 
HETATM 23478 O  O     . HOH H 5 .    ? 33.940  98.677  77.992  1.00 50.10  ? 4946 HOH A O     1 
HETATM 23479 O  O     . HOH H 5 .    ? 63.121  126.810 60.969  1.00 43.06  ? 4947 HOH A O     1 
HETATM 23480 O  O     . HOH H 5 .    ? 122.336 91.909  101.286 1.00 19.98  ? 4948 HOH A O     1 
HETATM 23481 O  O     . HOH H 5 .    ? 92.870  94.381  51.840  1.00 22.25  ? 4949 HOH A O     1 
HETATM 23482 O  O     . HOH H 5 .    ? 49.321  69.735  132.914 1.00 9.83   ? 4950 HOH A O     1 
HETATM 23483 O  O     . HOH H 5 .    ? 62.001  123.310 77.388  1.00 26.60  ? 4951 HOH A O     1 
HETATM 23484 O  O     . HOH H 5 .    ? 91.512  100.732 149.903 1.00 28.35  ? 4952 HOH A O     1 
HETATM 23485 O  O     . HOH H 5 .    ? 126.073 71.877  65.845  1.00 26.82  ? 4953 HOH A O     1 
HETATM 23486 O  O     . HOH H 5 .    ? 69.480  106.249 122.672 1.00 16.75  ? 4954 HOH A O     1 
HETATM 23487 O  O     . HOH H 5 .    ? 105.604 82.710  105.895 1.00 15.98  ? 4955 HOH A O     1 
HETATM 23488 O  O     . HOH H 5 .    ? 82.618  101.920 54.605  1.00 12.75  ? 4956 HOH A O     1 
HETATM 23489 O  O     . HOH H 5 .    ? 71.555  96.804  125.859 1.00 13.18  ? 4957 HOH A O     1 
HETATM 23490 O  O     . HOH H 5 .    ? 75.792  70.565  119.995 1.00 14.94  ? 4958 HOH A O     1 
HETATM 23491 O  O     . HOH H 5 .    ? 107.328 72.443  103.096 1.00 27.75  ? 4959 HOH A O     1 
HETATM 23492 O  O     . HOH H 5 .    ? 116.948 67.973  74.533  1.00 36.52  ? 4960 HOH A O     1 
HETATM 23493 O  O     . HOH H 5 .    ? 81.515  105.785 77.442  1.00 34.35  ? 4961 HOH A O     1 
HETATM 23494 O  O     . HOH H 5 .    ? 65.035  99.629  90.772  1.00 22.40  ? 4962 HOH A O     1 
HETATM 23495 O  O     . HOH H 5 .    ? 109.768 97.031  100.165 1.00 23.91  ? 4963 HOH A O     1 
HETATM 23496 O  O     . HOH H 5 .    ? 113.976 85.796  80.381  1.00 16.67  ? 4964 HOH A O     1 
HETATM 23497 O  O     . HOH H 5 .    ? 48.130  91.860  101.088 1.00 6.42   ? 4965 HOH A O     1 
HETATM 23498 O  O     . HOH H 5 .    ? 59.160  70.577  115.513 1.00 17.47  ? 4966 HOH A O     1 
HETATM 23499 O  O     . HOH H 5 .    ? 116.581 90.024  131.688 1.00 23.46  ? 4967 HOH A O     1 
HETATM 23500 O  O     . HOH H 5 .    ? 87.360  70.318  130.708 1.00 9.34   ? 4968 HOH A O     1 
HETATM 23501 O  O     . HOH H 5 .    ? 90.471  53.468  116.453 1.00 31.45  ? 4969 HOH A O     1 
HETATM 23502 O  O     . HOH H 5 .    ? 48.047  106.666 125.421 1.00 45.07  ? 4970 HOH A O     1 
HETATM 23503 O  O     . HOH H 5 .    ? 117.678 67.290  88.467  1.00 15.57  ? 4971 HOH A O     1 
HETATM 23504 O  O     . HOH H 5 .    ? 121.268 64.022  97.255  1.00 16.15  ? 4972 HOH A O     1 
HETATM 23505 O  O     . HOH H 5 .    ? 122.542 85.329  99.575  1.00 17.34  ? 4973 HOH A O     1 
HETATM 23506 O  O     . HOH H 5 .    ? 115.807 94.066  101.795 1.00 27.37  ? 4974 HOH A O     1 
HETATM 23507 O  O     . HOH H 5 .    ? 77.992  70.988  129.391 1.00 16.58  ? 4975 HOH A O     1 
HETATM 23508 O  O     . HOH H 5 .    ? 130.428 73.099  103.195 1.00 9.69   ? 4976 HOH A O     1 
HETATM 23509 O  O     . HOH H 5 .    ? 94.272  48.448  140.059 1.00 34.46  ? 4977 HOH A O     1 
HETATM 23510 O  O     . HOH H 5 .    ? 115.239 105.712 64.539  1.00 26.71  ? 4978 HOH A O     1 
HETATM 23511 O  O     . HOH H 5 .    ? 60.606  120.214 80.787  1.00 21.34  ? 4979 HOH A O     1 
HETATM 23512 O  O     . HOH H 5 .    ? 110.415 72.606  131.679 1.00 28.77  ? 4980 HOH A O     1 
HETATM 23513 O  O     . HOH H 5 .    ? 137.110 108.172 141.156 1.00 39.53  ? 4981 HOH A O     1 
HETATM 23514 O  O     . HOH H 5 .    ? 55.186  109.824 76.247  1.00 25.08  ? 4982 HOH A O     1 
HETATM 23515 O  O     . HOH H 5 .    ? 82.408  92.842  80.108  1.00 16.25  ? 4983 HOH A O     1 
HETATM 23516 O  O     . HOH H 5 .    ? 85.319  74.138  139.366 1.00 13.79  ? 4984 HOH A O     1 
HETATM 23517 O  O     . HOH H 5 .    ? 84.582  103.414 140.154 1.00 20.79  ? 4985 HOH A O     1 
HETATM 23518 O  O     . HOH H 5 .    ? 83.825  86.623  66.741  1.00 14.76  ? 4986 HOH A O     1 
HETATM 23519 O  O     . HOH H 5 .    ? 110.181 71.019  86.937  1.00 22.67  ? 4987 HOH A O     1 
HETATM 23520 O  O     . HOH H 5 .    ? 70.319  123.454 79.975  1.00 25.94  ? 4988 HOH A O     1 
HETATM 23521 O  O     . HOH H 5 .    ? 80.379  92.358  97.325  1.00 27.30  ? 4989 HOH A O     1 
HETATM 23522 O  O     . HOH H 5 .    ? 100.668 74.528  53.118  1.00 26.39  ? 4990 HOH A O     1 
HETATM 23523 O  O     . HOH H 5 .    ? 130.197 105.897 50.576  1.00 38.33  ? 4991 HOH A O     1 
HETATM 23524 O  O     . HOH H 5 .    ? 53.122  102.463 98.133  1.00 11.53  ? 4992 HOH A O     1 
HETATM 23525 O  O     . HOH H 5 .    ? 74.031  69.214  113.199 1.00 11.82  ? 4993 HOH A O     1 
HETATM 23526 O  O     . HOH H 5 .    ? 117.561 87.500  109.376 1.00 10.39  ? 4994 HOH A O     1 
HETATM 23527 O  O     . HOH H 5 .    ? 95.542  86.457  134.831 1.00 13.03  ? 4995 HOH A O     1 
HETATM 23528 O  O     . HOH H 5 .    ? 129.103 85.888  112.822 1.00 23.71  ? 4996 HOH A O     1 
HETATM 23529 O  O     . HOH H 5 .    ? 104.216 73.254  98.778  1.00 33.49  ? 4997 HOH A O     1 
HETATM 23530 O  O     . HOH H 5 .    ? 87.971  45.685  111.802 1.00 38.48  ? 4998 HOH A O     1 
HETATM 23531 O  O     . HOH H 5 .    ? 119.979 100.425 46.557  1.00 28.06  ? 4999 HOH A O     1 
HETATM 23532 O  O     . HOH H 5 .    ? 136.889 110.614 102.752 1.00 18.49  ? 5000 HOH A O     1 
HETATM 23533 O  O     . HOH H 5 .    ? 127.888 68.541  98.933  1.00 14.36  ? 5001 HOH A O     1 
HETATM 23534 O  O     . HOH H 5 .    ? 66.626  76.658  65.731  1.00 27.83  ? 5002 HOH A O     1 
HETATM 23535 O  O     . HOH H 5 .    ? 73.727  72.962  118.975 1.00 12.32  ? 5003 HOH A O     1 
HETATM 23536 O  O     . HOH H 5 .    ? 116.654 100.295 148.031 1.00 15.75  ? 5004 HOH A O     1 
HETATM 23537 O  O     . HOH H 5 .    ? 113.635 83.566  105.993 1.00 11.24  ? 5005 HOH A O     1 
HETATM 23538 O  O     . HOH H 5 .    ? 87.215  69.951  109.485 1.00 20.32  ? 5006 HOH A O     1 
HETATM 23539 O  O     . HOH H 5 .    ? 154.779 97.101  90.688  1.00 40.86  ? 5007 HOH A O     1 
HETATM 23540 O  O     . HOH H 5 .    ? 32.898  90.174  115.457 1.00 29.66  ? 5008 HOH A O     1 
HETATM 23541 O  O     . HOH H 5 .    ? 137.752 88.934  66.678  1.00 15.78  ? 5009 HOH A O     1 
HETATM 23542 O  O     . HOH H 5 .    ? 79.749  71.807  124.565 1.00 21.42  ? 5010 HOH A O     1 
HETATM 23543 O  O     . HOH H 5 .    ? 67.803  111.059 77.850  1.00 39.06  ? 5011 HOH A O     1 
HETATM 23544 O  O     . HOH H 5 .    ? 35.660  98.875  135.165 1.00 32.44  ? 5012 HOH A O     1 
HETATM 23545 O  O     . HOH H 5 .    ? 83.620  44.111  124.035 1.00 32.55  ? 5013 HOH A O     1 
HETATM 23546 O  O     . HOH H 5 .    ? 144.035 91.606  87.568  1.00 9.54   ? 5014 HOH A O     1 
HETATM 23547 O  O     . HOH H 5 .    ? 82.308  91.445  44.813  1.00 17.23  ? 5015 HOH A O     1 
HETATM 23548 O  O     . HOH H 5 .    ? 112.066 103.954 44.609  1.00 17.50  ? 5016 HOH A O     1 
HETATM 23549 O  O     . HOH H 5 .    ? 126.781 83.427  119.907 1.00 13.65  ? 5017 HOH A O     1 
HETATM 23550 O  O     . HOH H 5 .    ? 59.290  86.499  94.671  1.00 14.07  ? 5018 HOH A O     1 
HETATM 23551 O  O     . HOH H 5 .    ? 95.591  102.149 111.141 1.00 22.68  ? 5019 HOH A O     1 
HETATM 23552 O  O     . HOH H 5 .    ? 49.412  90.770  107.701 1.00 1.47   ? 5020 HOH A O     1 
HETATM 23553 O  O     . HOH H 5 .    ? 139.504 112.759 83.788  1.00 35.20  ? 5021 HOH A O     1 
HETATM 23554 O  O     . HOH H 5 .    ? 54.262  56.977  126.830 1.00 15.22  ? 5022 HOH A O     1 
HETATM 23555 O  O     . HOH H 5 .    ? 113.121 85.617  95.281  1.00 30.05  ? 5023 HOH A O     1 
HETATM 23556 O  O     . HOH H 5 .    ? 38.473  77.649  126.683 1.00 25.47  ? 5024 HOH A O     1 
HETATM 23557 O  O     . HOH H 5 .    ? 60.341  117.669 70.960  1.00 31.02  ? 5025 HOH A O     1 
HETATM 23558 O  O     . HOH H 5 .    ? 134.104 70.720  95.870  1.00 36.38  ? 5026 HOH A O     1 
HETATM 23559 O  O     . HOH H 5 .    ? 102.359 96.268  112.929 1.00 6.35   ? 5027 HOH A O     1 
HETATM 23560 O  O     . HOH H 5 .    ? 65.813  132.375 93.007  1.00 36.53  ? 5028 HOH A O     1 
HETATM 23561 O  O     . HOH H 5 .    ? 128.615 87.113  65.509  1.00 24.93  ? 5029 HOH A O     1 
HETATM 23562 O  O     . HOH H 5 .    ? 74.407  100.575 135.615 1.00 18.22  ? 5030 HOH A O     1 
HETATM 23563 O  O     . HOH H 5 .    ? 88.900  72.945  59.317  1.00 42.02  ? 5031 HOH A O     1 
HETATM 23564 O  O     . HOH H 5 .    ? 46.929  73.736  137.523 1.00 20.16  ? 5032 HOH A O     1 
HETATM 23565 O  O     . HOH H 5 .    ? 73.768  53.220  132.462 1.00 35.38  ? 5033 HOH A O     1 
HETATM 23566 O  O     . HOH H 5 .    ? 120.024 93.145  92.927  1.00 11.60  ? 5034 HOH A O     1 
HETATM 23567 O  O     . HOH H 5 .    ? 127.142 89.676  136.627 1.00 20.90  ? 5035 HOH A O     1 
HETATM 23568 O  O     . HOH H 5 .    ? 104.490 51.534  133.459 1.00 33.19  ? 5036 HOH A O     1 
HETATM 23569 O  O     . HOH H 5 .    ? 98.652  84.102  32.606  1.00 32.38  ? 5037 HOH A O     1 
HETATM 23570 O  O     . HOH H 5 .    ? 103.374 92.319  63.894  1.00 7.85   ? 5038 HOH A O     1 
HETATM 23571 O  O     . HOH H 5 .    ? 70.471  94.980  38.909  1.00 32.12  ? 5039 HOH A O     1 
HETATM 23572 O  O     . HOH H 5 .    ? 126.569 94.095  94.214  1.00 19.67  ? 5040 HOH A O     1 
HETATM 23573 O  O     . HOH H 5 .    ? 75.054  88.283  112.673 1.00 16.38  ? 5041 HOH A O     1 
HETATM 23574 O  O     . HOH H 5 .    ? 120.395 74.361  102.596 1.00 15.33  ? 5042 HOH A O     1 
HETATM 23575 O  O     . HOH H 5 .    ? 114.852 82.646  82.300  1.00 15.59  ? 5043 HOH A O     1 
HETATM 23576 O  O     . HOH H 5 .    ? 61.107  87.365  121.716 1.00 8.63   ? 5044 HOH A O     1 
HETATM 23577 O  O     . HOH H 5 .    ? 126.095 110.028 99.796  1.00 15.91  ? 5045 HOH A O     1 
HETATM 23578 O  O     . HOH H 5 .    ? 56.576  94.011  72.237  1.00 24.91  ? 5046 HOH A O     1 
HETATM 23579 O  O     . HOH H 5 .    ? 96.508  55.557  146.929 1.00 29.18  ? 5047 HOH A O     1 
HETATM 23580 O  O     . HOH H 5 .    ? 67.801  99.101  75.799  1.00 8.69   ? 5048 HOH A O     1 
HETATM 23581 O  O     . HOH H 5 .    ? 64.854  134.048 100.023 1.00 37.89  ? 5049 HOH A O     1 
HETATM 23582 O  O     . HOH H 5 .    ? 98.480  96.395  115.021 1.00 15.34  ? 5050 HOH A O     1 
HETATM 23583 O  O     . HOH H 5 .    ? 96.363  83.282  41.539  1.00 19.11  ? 5051 HOH A O     1 
HETATM 23584 O  O     . HOH H 5 .    ? 85.852  107.564 132.187 1.00 9.49   ? 5052 HOH A O     1 
HETATM 23585 O  O     . HOH H 5 .    ? 105.139 74.499  111.328 1.00 25.78  ? 5053 HOH A O     1 
HETATM 23586 O  O     . HOH H 5 .    ? 67.190  107.879 76.767  1.00 11.05  ? 5054 HOH A O     1 
HETATM 23587 O  O     . HOH H 5 .    ? 104.107 60.106  70.270  1.00 30.20  ? 5055 HOH A O     1 
HETATM 23588 O  O     . HOH H 5 .    ? 47.927  102.336 135.946 1.00 24.62  ? 5056 HOH A O     1 
HETATM 23589 O  O     . HOH H 5 .    ? 53.823  75.187  136.394 1.00 14.46  ? 5057 HOH A O     1 
HETATM 23590 O  O     . HOH H 5 .    ? 34.414  84.741  124.505 1.00 22.21  ? 5058 HOH A O     1 
HETATM 23591 O  O     . HOH H 5 .    ? 95.929  98.439  116.976 1.00 9.84   ? 5059 HOH A O     1 
HETATM 23592 O  O     . HOH H 5 .    ? 82.462  59.116  144.619 1.00 42.86  ? 5060 HOH A O     1 
HETATM 23593 O  O     . HOH H 5 .    ? 37.190  98.638  85.367  1.00 14.31  ? 5061 HOH A O     1 
HETATM 23594 O  O     . HOH H 5 .    ? 93.547  104.794 121.819 1.00 5.29   ? 5062 HOH A O     1 
HETATM 23595 O  O     . HOH H 5 .    ? 71.784  95.231  135.909 1.00 19.46  ? 5063 HOH A O     1 
HETATM 23596 O  O     . HOH H 5 .    ? 74.372  49.060  138.501 1.00 46.70  ? 5064 HOH A O     1 
HETATM 23597 O  O     . HOH H 5 .    ? 119.522 95.161  128.570 1.00 11.19  ? 5065 HOH A O     1 
HETATM 23598 O  O     . HOH H 5 .    ? 107.722 72.487  26.608  1.00 49.35  ? 5066 HOH A O     1 
HETATM 23599 O  O     . HOH H 5 .    ? 100.256 92.022  129.553 1.00 22.10  ? 5067 HOH A O     1 
HETATM 23600 O  O     . HOH H 5 .    ? 53.722  92.688  86.042  1.00 27.62  ? 5068 HOH A O     1 
HETATM 23601 O  O     . HOH H 5 .    ? 87.869  107.020 119.862 1.00 12.35  ? 5069 HOH A O     1 
HETATM 23602 O  O     . HOH H 5 .    ? 95.042  91.687  70.689  1.00 29.12  ? 5070 HOH A O     1 
HETATM 23603 O  O     . HOH H 5 .    ? 63.640  95.195  62.589  1.00 14.57  ? 5071 HOH A O     1 
HETATM 23604 O  O     . HOH H 5 .    ? 70.940  73.531  90.130  1.00 20.24  ? 5072 HOH A O     1 
HETATM 23605 O  O     . HOH H 5 .    ? 59.442  125.151 112.188 1.00 27.29  ? 5073 HOH A O     1 
HETATM 23606 O  O     . HOH H 5 .    ? 151.887 89.607  96.895  1.00 36.97  ? 5074 HOH A O     1 
HETATM 23607 O  O     . HOH H 5 .    ? 60.538  106.354 115.599 1.00 21.95  ? 5075 HOH A O     1 
HETATM 23608 O  O     . HOH H 5 .    ? 97.696  85.370  123.537 1.00 4.33   ? 5076 HOH A O     1 
HETATM 23609 O  O     . HOH H 5 .    ? 147.883 104.042 109.043 1.00 28.82  ? 5077 HOH A O     1 
HETATM 23610 O  O     . HOH H 5 .    ? 112.767 68.200  88.853  1.00 27.00  ? 5078 HOH A O     1 
HETATM 23611 O  O     . HOH H 5 .    ? 138.708 108.992 108.779 1.00 10.53  ? 5079 HOH A O     1 
HETATM 23612 O  O     . HOH H 5 .    ? 123.533 79.206  71.605  1.00 15.04  ? 5080 HOH A O     1 
HETATM 23613 O  O     . HOH H 5 .    ? 130.892 88.797  66.574  1.00 32.09  ? 5081 HOH A O     1 
HETATM 23614 O  O     . HOH H 5 .    ? 45.765  94.783  75.320  1.00 34.46  ? 5082 HOH A O     1 
HETATM 23615 O  O     . HOH H 5 .    ? 89.851  98.483  115.289 1.00 6.73   ? 5083 HOH A O     1 
HETATM 23616 O  O     . HOH H 5 .    ? 71.055  121.518 52.529  1.00 34.01  ? 5084 HOH A O     1 
HETATM 23617 O  O     . HOH H 5 .    ? 126.053 76.125  107.391 1.00 14.19  ? 5085 HOH A O     1 
HETATM 23618 O  O     . HOH H 5 .    ? 70.728  93.127  87.703  1.00 18.32  ? 5086 HOH A O     1 
HETATM 23619 O  O     . HOH H 5 .    ? 110.309 67.172  122.896 1.00 21.38  ? 5087 HOH A O     1 
HETATM 23620 O  O     . HOH H 5 .    ? 53.256  129.649 94.368  1.00 31.28  ? 5088 HOH A O     1 
HETATM 23621 O  O     . HOH H 5 .    ? 53.869  83.410  122.602 1.00 1.69   ? 5089 HOH A O     1 
HETATM 23622 O  O     . HOH H 5 .    ? 46.924  84.636  145.184 1.00 24.56  ? 5090 HOH A O     1 
HETATM 23623 O  O     . HOH H 5 .    ? 72.882  119.390 75.537  1.00 16.14  ? 5091 HOH A O     1 
HETATM 23624 O  O     . HOH H 5 .    ? 110.517 80.652  102.891 1.00 21.97  ? 5092 HOH A O     1 
HETATM 23625 O  O     . HOH H 5 .    ? 142.099 108.157 101.987 1.00 12.77  ? 5093 HOH A O     1 
HETATM 23626 O  O     . HOH H 5 .    ? 113.021 108.447 57.715  1.00 17.00  ? 5094 HOH A O     1 
HETATM 23627 O  O     . HOH H 5 .    ? 65.141  102.668 79.196  1.00 15.52  ? 5095 HOH A O     1 
HETATM 23628 O  O     . HOH H 5 .    ? 142.605 103.941 107.807 1.00 8.84   ? 5096 HOH A O     1 
HETATM 23629 O  O     . HOH H 5 .    ? 111.027 71.743  124.465 1.00 14.15  ? 5097 HOH A O     1 
HETATM 23630 O  O     . HOH H 5 .    ? 102.005 104.283 128.544 1.00 11.05  ? 5098 HOH A O     1 
HETATM 23631 O  O     . HOH H 5 .    ? 76.257  77.144  127.661 1.00 3.72   ? 5099 HOH A O     1 
HETATM 23632 O  O     . HOH H 5 .    ? 58.434  107.350 59.069  1.00 36.90  ? 5100 HOH A O     1 
HETATM 23633 O  O     . HOH H 5 .    ? 108.710 86.953  126.873 1.00 11.71  ? 5101 HOH A O     1 
HETATM 23634 O  O     . HOH H 5 .    ? 81.049  89.842  141.446 1.00 16.19  ? 5102 HOH A O     1 
HETATM 23635 O  O     . HOH H 5 .    ? 124.712 95.682  89.674  1.00 4.84   ? 5103 HOH A O     1 
HETATM 23636 O  O     . HOH H 5 .    ? 114.911 71.286  74.180  1.00 26.79  ? 5104 HOH A O     1 
HETATM 23637 O  O     . HOH H 5 .    ? 81.031  98.587  150.199 1.00 39.79  ? 5105 HOH A O     1 
HETATM 23638 O  O     . HOH H 5 .    ? 80.785  91.922  117.001 1.00 5.93   ? 5106 HOH A O     1 
HETATM 23639 O  O     . HOH H 5 .    ? 87.137  49.311  137.449 1.00 36.86  ? 5107 HOH A O     1 
HETATM 23640 O  O     . HOH H 5 .    ? 62.941  80.598  129.641 1.00 16.92  ? 5108 HOH A O     1 
HETATM 23641 O  O     . HOH H 5 .    ? 59.613  112.829 82.579  1.00 10.35  ? 5109 HOH A O     1 
HETATM 23642 O  O     . HOH H 5 .    ? 136.675 76.039  72.024  1.00 20.48  ? 5110 HOH A O     1 
HETATM 23643 O  O     . HOH H 5 .    ? 90.548  72.352  68.939  1.00 34.51  ? 5111 HOH A O     1 
HETATM 23644 O  O     . HOH H 5 .    ? 105.518 88.538  66.908  1.00 9.41   ? 5112 HOH A O     1 
HETATM 23645 O  O     . HOH H 5 .    ? 54.032  89.776  98.277  1.00 12.55  ? 5113 HOH A O     1 
HETATM 23646 O  O     . HOH H 5 .    ? 85.191  101.914 112.218 1.00 15.42  ? 5114 HOH A O     1 
HETATM 23647 O  O     . HOH H 5 .    ? 46.362  81.881  105.873 1.00 11.21  ? 5115 HOH A O     1 
HETATM 23648 O  O     . HOH H 5 .    ? 59.592  81.086  95.494  1.00 24.99  ? 5116 HOH A O     1 
HETATM 23649 O  O     . HOH H 5 .    ? 107.672 103.162 120.595 1.00 5.94   ? 5117 HOH A O     1 
HETATM 23650 O  O     . HOH H 5 .    ? 56.481  108.543 74.457  1.00 22.42  ? 5118 HOH A O     1 
HETATM 23651 O  O     . HOH H 5 .    ? 63.275  105.240 86.630  1.00 17.45  ? 5119 HOH A O     1 
HETATM 23652 O  O     . HOH H 5 .    ? 50.350  74.026  116.883 1.00 9.72   ? 5120 HOH A O     1 
HETATM 23653 O  O     . HOH H 5 .    ? 124.086 114.339 86.588  1.00 21.56  ? 5121 HOH A O     1 
HETATM 23654 O  O     . HOH H 5 .    ? 99.224  97.127  68.051  1.00 36.69  ? 5122 HOH A O     1 
HETATM 23655 O  O     . HOH H 5 .    ? 62.105  133.120 114.361 1.00 34.84  ? 5123 HOH A O     1 
HETATM 23656 O  O     . HOH H 5 .    ? 70.990  100.291 47.746  1.00 20.12  ? 5124 HOH A O     1 
HETATM 23657 O  O     . HOH H 5 .    ? 85.793  75.768  71.350  1.00 25.43  ? 5125 HOH A O     1 
HETATM 23658 O  O     . HOH H 5 .    ? 115.307 63.931  64.232  1.00 23.31  ? 5126 HOH A O     1 
HETATM 23659 O  O     . HOH H 5 .    ? 118.442 98.545  46.055  1.00 22.73  ? 5127 HOH A O     1 
HETATM 23660 O  O     . HOH H 5 .    ? 131.865 94.847  135.997 1.00 23.38  ? 5128 HOH A O     1 
HETATM 23661 O  O     . HOH H 5 .    ? 111.763 80.426  65.335  1.00 19.16  ? 5129 HOH A O     1 
HETATM 23662 O  O     . HOH H 5 .    ? 92.053  50.073  114.732 1.00 37.62  ? 5130 HOH A O     1 
HETATM 23663 O  O     . HOH H 5 .    ? 47.008  91.790  122.228 1.00 11.07  ? 5131 HOH A O     1 
HETATM 23664 O  O     . HOH H 5 .    ? 60.357  74.476  123.386 1.00 6.02   ? 5132 HOH A O     1 
HETATM 23665 O  O     . HOH H 5 .    ? 31.123  101.959 126.420 1.00 31.08  ? 5133 HOH A O     1 
HETATM 23666 O  O     . HOH H 5 .    ? 65.706  92.877  67.927  1.00 17.39  ? 5134 HOH A O     1 
HETATM 23667 O  O     . HOH H 5 .    ? 50.359  97.163  145.599 1.00 29.51  ? 5135 HOH A O     1 
HETATM 23668 O  O     . HOH H 5 .    ? 69.868  131.655 105.302 1.00 32.53  ? 5136 HOH A O     1 
HETATM 23669 O  O     . HOH H 5 .    ? 81.613  68.874  123.424 1.00 26.15  ? 5137 HOH A O     1 
HETATM 23670 O  O     . HOH H 5 .    ? 99.361  105.433 146.118 1.00 15.34  ? 5138 HOH A O     1 
HETATM 23671 O  O     . HOH H 5 .    ? 127.365 98.592  82.828  1.00 7.64   ? 5139 HOH A O     1 
HETATM 23672 O  O     . HOH H 5 .    ? 42.659  111.942 97.544  1.00 10.98  ? 5140 HOH A O     1 
HETATM 23673 O  O     . HOH H 5 .    ? 143.950 115.957 88.973  1.00 23.97  ? 5141 HOH A O     1 
HETATM 23674 O  O     . HOH H 5 .    ? 139.360 84.903  88.191  1.00 18.76  ? 5142 HOH A O     1 
HETATM 23675 O  O     . HOH H 5 .    ? 116.597 78.315  24.198  1.00 51.27  ? 5143 HOH A O     1 
HETATM 23676 O  O     . HOH H 5 .    ? 123.133 123.478 133.912 1.00 27.76  ? 5144 HOH A O     1 
HETATM 23677 O  O     . HOH H 5 .    ? 75.271  71.016  113.959 1.00 15.32  ? 5145 HOH A O     1 
HETATM 23678 O  O     . HOH H 5 .    ? 62.956  121.472 95.053  1.00 12.55  ? 5146 HOH A O     1 
HETATM 23679 O  O     . HOH H 5 .    ? 63.701  97.280  89.612  1.00 16.38  ? 5147 HOH A O     1 
HETATM 23680 O  O     . HOH H 5 .    ? 54.866  104.993 108.359 1.00 13.10  ? 5148 HOH A O     1 
HETATM 23681 O  O     . HOH H 5 .    ? 76.888  133.041 109.130 1.00 40.06  ? 5149 HOH A O     1 
HETATM 23682 O  O     . HOH H 5 .    ? 108.564 106.584 62.713  1.00 22.82  ? 5150 HOH A O     1 
HETATM 23683 O  O     . HOH H 5 .    ? 99.945  74.051  127.638 1.00 13.31  ? 5151 HOH A O     1 
HETATM 23684 O  O     . HOH H 5 .    ? 33.681  88.751  123.670 1.00 23.68  ? 5152 HOH A O     1 
HETATM 23685 O  O     . HOH H 5 .    ? 131.753 72.446  94.807  1.00 15.60  ? 5153 HOH A O     1 
HETATM 23686 O  O     . HOH H 5 .    ? 72.424  93.257  110.652 1.00 14.60  ? 5154 HOH A O     1 
HETATM 23687 O  O     . HOH H 5 .    ? 87.275  68.056  112.960 1.00 33.59  ? 5155 HOH A O     1 
HETATM 23688 O  O     . HOH H 5 .    ? 79.146  92.899  80.770  1.00 22.85  ? 5156 HOH A O     1 
HETATM 23689 O  O     . HOH H 5 .    ? 45.253  74.448  134.818 1.00 19.31  ? 5157 HOH A O     1 
HETATM 23690 O  O     . HOH H 5 .    ? 96.490  106.411 138.396 1.00 8.44   ? 5158 HOH A O     1 
HETATM 23691 O  O     . HOH H 5 .    ? 107.123 98.999  133.279 1.00 11.10  ? 5159 HOH A O     1 
HETATM 23692 O  O     . HOH H 5 .    ? 108.367 79.067  57.362  1.00 5.45   ? 5160 HOH A O     1 
HETATM 23693 O  O     . HOH H 5 .    ? 59.943  95.605  132.580 1.00 18.43  ? 5161 HOH A O     1 
HETATM 23694 O  O     . HOH H 5 .    ? 74.186  108.711 73.923  1.00 19.11  ? 5162 HOH A O     1 
HETATM 23695 O  O     . HOH H 5 .    ? 53.561  118.893 92.211  1.00 12.21  ? 5163 HOH A O     1 
HETATM 23696 O  O     . HOH H 5 .    ? 143.605 107.546 88.132  1.00 27.82  ? 5164 HOH A O     1 
HETATM 23697 O  O     . HOH H 5 .    ? 73.159  76.003  123.091 1.00 11.10  ? 5165 HOH A O     1 
HETATM 23698 O  O     . HOH H 5 .    ? 111.396 81.536  56.992  1.00 9.31   ? 5166 HOH A O     1 
HETATM 23699 O  O     . HOH H 5 .    ? 69.682  133.705 77.891  1.00 44.49  ? 5167 HOH A O     1 
HETATM 23700 O  O     . HOH H 5 .    ? 102.000 75.875  127.844 1.00 5.82   ? 5168 HOH A O     1 
HETATM 23701 O  O     . HOH H 5 .    ? 111.808 84.576  103.141 1.00 15.54  ? 5169 HOH A O     1 
HETATM 23702 O  O     . HOH H 5 .    ? 126.637 96.516  92.631  1.00 12.88  ? 5170 HOH A O     1 
HETATM 23703 O  O     . HOH H 5 .    ? 62.435  96.132  131.774 1.00 21.21  ? 5171 HOH A O     1 
HETATM 23704 O  O     . HOH H 5 .    ? 72.009  93.363  114.371 1.00 5.06   ? 5172 HOH A O     1 
HETATM 23705 O  O     . HOH H 5 .    ? 72.800  54.061  126.704 1.00 28.32  ? 5173 HOH A O     1 
HETATM 23706 O  O     . HOH H 5 .    ? 123.944 96.307  95.335  1.00 18.19  ? 5174 HOH A O     1 
HETATM 23707 O  O     . HOH H 5 .    ? 78.047  83.855  116.490 1.00 5.17   ? 5175 HOH A O     1 
HETATM 23708 O  O     . HOH H 5 .    ? 63.728  119.752 58.316  1.00 34.36  ? 5176 HOH A O     1 
HETATM 23709 O  O     . HOH H 5 .    ? 125.783 73.549  81.662  1.00 14.50  ? 5177 HOH A O     1 
HETATM 23710 O  O     . HOH H 5 .    ? 86.441  53.335  134.826 1.00 30.84  ? 5178 HOH A O     1 
HETATM 23711 O  O     . HOH H 5 .    ? 106.832 101.604 48.817  1.00 20.81  ? 5179 HOH A O     1 
HETATM 23712 O  O     . HOH H 5 .    ? 63.997  87.783  50.392  1.00 36.05  ? 5180 HOH A O     1 
HETATM 23713 O  O     . HOH H 5 .    ? 58.987  84.392  123.997 1.00 19.97  ? 5181 HOH A O     1 
HETATM 23714 O  O     . HOH H 5 .    ? 98.702  95.509  50.437  1.00 19.27  ? 5182 HOH A O     1 
HETATM 23715 O  O     . HOH H 5 .    ? 116.482 91.154  102.326 1.00 17.97  ? 5183 HOH A O     1 
HETATM 23716 O  O     . HOH H 5 .    ? 80.046  101.009 129.430 1.00 18.43  ? 5184 HOH A O     1 
HETATM 23717 O  O     . HOH H 5 .    ? 65.754  63.979  102.390 1.00 22.23  ? 5185 HOH A O     1 
HETATM 23718 O  O     . HOH H 5 .    ? 61.827  107.286 117.307 1.00 14.55  ? 5186 HOH A O     1 
HETATM 23719 O  O     . HOH H 5 .    ? 61.346  90.009  141.850 1.00 20.04  ? 5187 HOH A O     1 
HETATM 23720 O  O     . HOH H 5 .    ? 70.934  91.891  116.657 1.00 7.58   ? 5188 HOH A O     1 
HETATM 23721 O  O     . HOH H 5 .    ? 52.879  101.376 120.039 1.00 15.33  ? 5189 HOH A O     1 
HETATM 23722 O  O     . HOH H 5 .    ? 57.499  100.667 63.602  1.00 30.50  ? 5190 HOH A O     1 
HETATM 23723 O  O     . HOH H 5 .    ? 129.913 117.506 135.198 1.00 26.22  ? 5191 HOH A O     1 
HETATM 23724 O  O     . HOH H 5 .    ? 92.952  72.831  114.333 1.00 18.23  ? 5192 HOH A O     1 
HETATM 23725 O  O     . HOH H 5 .    ? 103.309 65.303  58.184  1.00 20.60  ? 5193 HOH A O     1 
HETATM 23726 O  O     . HOH H 5 .    ? 111.011 59.845  70.165  1.00 18.91  ? 5194 HOH A O     1 
HETATM 23727 O  O     . HOH H 5 .    ? 91.728  66.838  135.434 1.00 22.21  ? 5195 HOH A O     1 
HETATM 23728 O  O     . HOH H 5 .    ? 127.437 105.863 103.280 1.00 11.63  ? 5196 HOH A O     1 
HETATM 23729 O  O     . HOH H 5 .    ? 80.834  116.590 74.411  1.00 22.23  ? 5197 HOH A O     1 
HETATM 23730 O  O     . HOH H 5 .    ? 44.116  113.038 79.302  1.00 16.93  ? 5198 HOH A O     1 
HETATM 23731 O  O     . HOH H 5 .    ? 79.769  73.957  84.061  1.00 21.69  ? 5199 HOH A O     1 
HETATM 23732 O  O     . HOH H 5 .    ? 109.606 72.650  117.340 1.00 16.31  ? 5200 HOH A O     1 
HETATM 23733 O  O     . HOH H 5 .    ? 108.830 80.389  67.261  1.00 8.11   ? 5201 HOH A O     1 
HETATM 23734 O  O     . HOH H 5 .    ? 120.221 97.266  99.706  1.00 21.29  ? 5202 HOH A O     1 
HETATM 23735 O  O     . HOH H 5 .    ? 134.841 90.265  83.730  1.00 4.79   ? 5203 HOH A O     1 
HETATM 23736 O  O     . HOH H 5 .    ? 61.745  109.952 81.691  1.00 22.42  ? 5204 HOH A O     1 
HETATM 23737 O  O     . HOH H 5 .    ? 74.725  93.192  108.030 1.00 17.20  ? 5205 HOH A O     1 
HETATM 23738 O  O     . HOH H 5 .    ? 106.571 87.776  42.513  1.00 27.11  ? 5206 HOH A O     1 
HETATM 23739 O  O     . HOH H 5 .    ? 53.620  122.304 84.784  1.00 41.29  ? 5207 HOH A O     1 
HETATM 23740 O  O     . HOH H 5 .    ? 37.363  88.769  127.545 1.00 18.77  ? 5208 HOH A O     1 
HETATM 23741 O  O     . HOH H 5 .    ? 58.412  119.401 99.840  1.00 13.16  ? 5209 HOH A O     1 
HETATM 23742 O  O     . HOH H 5 .    ? 85.696  102.917 60.894  1.00 20.36  ? 5210 HOH A O     1 
HETATM 23743 O  O     . HOH H 5 .    ? 129.940 108.132 145.188 1.00 31.80  ? 5211 HOH A O     1 
HETATM 23744 O  O     . HOH H 5 .    ? 79.067  68.080  127.789 1.00 21.69  ? 5212 HOH A O     1 
HETATM 23745 O  O     . HOH H 5 .    ? 154.423 104.571 91.104  1.00 23.77  ? 5213 HOH A O     1 
HETATM 23746 O  O     . HOH H 5 .    ? 55.023  85.978  129.020 1.00 9.27   ? 5214 HOH A O     1 
HETATM 23747 O  O     . HOH H 5 .    ? 54.419  79.429  135.621 1.00 10.60  ? 5215 HOH A O     1 
HETATM 23748 O  O     . HOH H 5 .    ? 68.231  107.526 73.312  1.00 10.05  ? 5216 HOH A O     1 
HETATM 23749 O  O     . HOH H 5 .    ? 127.712 106.339 125.024 1.00 7.23   ? 5217 HOH A O     1 
HETATM 23750 O  O     . HOH H 5 .    ? 138.602 95.534  70.036  1.00 18.03  ? 5218 HOH A O     1 
HETATM 23751 O  O     . HOH H 5 .    ? 111.610 96.781  74.109  1.00 21.36  ? 5219 HOH A O     1 
HETATM 23752 O  O     . HOH H 5 .    ? 98.010  98.959  51.656  1.00 23.15  ? 5220 HOH A O     1 
HETATM 23753 O  O     . HOH H 5 .    ? 62.400  103.567 111.366 1.00 13.83  ? 5221 HOH A O     1 
HETATM 23754 O  O     . HOH H 5 .    ? 35.893  109.134 119.560 1.00 34.23  ? 5222 HOH A O     1 
HETATM 23755 O  O     . HOH H 5 .    ? 133.743 75.504  78.357  1.00 10.94  ? 5223 HOH A O     1 
HETATM 23756 O  O     . HOH H 5 .    ? 74.539  77.925  113.201 1.00 12.24  ? 5224 HOH A O     1 
HETATM 23757 O  O     . HOH H 5 .    ? 60.713  138.397 108.525 1.00 42.09  ? 5225 HOH A O     1 
HETATM 23758 O  O     . HOH H 5 .    ? 73.242  53.614  118.680 1.00 35.45  ? 5226 HOH A O     1 
HETATM 23759 O  O     . HOH H 5 .    ? 136.284 114.660 128.811 1.00 41.13  ? 5227 HOH A O     1 
HETATM 23760 O  O     . HOH H 5 .    ? 79.151  82.308  102.357 1.00 11.38  ? 5228 HOH A O     1 
HETATM 23761 O  O     . HOH H 5 .    ? 72.372  134.128 116.144 1.00 45.32  ? 5229 HOH A O     1 
HETATM 23762 O  O     . HOH H 5 .    ? 135.619 95.410  115.157 1.00 14.52  ? 5230 HOH A O     1 
HETATM 23763 O  O     . HOH H 5 .    ? 63.928  92.221  88.300  1.00 26.05  ? 5231 HOH A O     1 
HETATM 23764 O  O     . HOH H 5 .    ? 71.829  90.832  114.418 1.00 10.77  ? 5232 HOH A O     1 
HETATM 23765 O  O     . HOH H 5 .    ? 59.469  123.268 92.778  1.00 9.75   ? 5233 HOH A O     1 
HETATM 23766 O  O     . HOH H 5 .    ? 68.501  93.870  125.728 1.00 21.30  ? 5234 HOH A O     1 
HETATM 23767 O  O     . HOH H 5 .    ? 49.511  75.897  134.241 1.00 15.32  ? 5235 HOH A O     1 
HETATM 23768 O  O     . HOH H 5 .    ? 81.089  70.819  136.369 1.00 16.56  ? 5236 HOH A O     1 
HETATM 23769 O  O     . HOH H 5 .    ? 73.559  109.527 78.593  1.00 27.91  ? 5237 HOH A O     1 
HETATM 23770 O  O     . HOH H 5 .    ? 65.000  73.465  133.311 1.00 19.62  ? 5238 HOH A O     1 
HETATM 23771 O  O     . HOH H 5 .    ? 56.131  102.131 71.197  1.00 37.85  ? 5239 HOH A O     1 
HETATM 23772 O  O     . HOH H 5 .    ? 55.185  68.557  105.075 1.00 24.46  ? 5240 HOH A O     1 
HETATM 23773 O  O     . HOH H 5 .    ? 34.453  105.105 83.018  1.00 37.80  ? 5241 HOH A O     1 
HETATM 23774 O  O     . HOH H 5 .    ? 52.872  100.918 112.493 1.00 4.92   ? 5242 HOH A O     1 
HETATM 23775 O  O     . HOH H 5 .    ? 105.667 95.089  101.947 1.00 21.06  ? 5243 HOH A O     1 
HETATM 23776 O  O     . HOH H 5 .    ? 128.132 83.633  100.918 1.00 25.73  ? 5244 HOH A O     1 
HETATM 23777 O  O     . HOH H 5 .    ? 125.613 98.078  89.213  1.00 3.80   ? 5245 HOH A O     1 
HETATM 23778 O  O     . HOH H 5 .    ? 39.775  82.016  111.905 1.00 14.27  ? 5246 HOH A O     1 
HETATM 23779 O  O     . HOH H 5 .    ? 88.307  84.243  77.366  1.00 38.45  ? 5247 HOH A O     1 
HETATM 23780 O  O     . HOH H 5 .    ? 38.653  101.985 73.521  1.00 36.27  ? 5248 HOH A O     1 
HETATM 23781 O  O     . HOH H 5 .    ? 132.439 92.457  105.416 1.00 31.23  ? 5249 HOH A O     1 
HETATM 23782 O  O     . HOH H 5 .    ? 121.589 81.000  98.575  1.00 6.83   ? 5250 HOH A O     1 
HETATM 23783 O  O     . HOH H 5 .    ? 64.332  83.040  119.365 1.00 10.76  ? 5251 HOH A O     1 
HETATM 23784 O  O     . HOH H 5 .    ? 48.907  63.122  133.777 1.00 30.46  ? 5252 HOH A O     1 
HETATM 23785 O  O     . HOH H 5 .    ? 118.478 79.781  130.227 1.00 15.37  ? 5253 HOH A O     1 
HETATM 23786 O  O     . HOH H 5 .    ? 103.168 87.344  41.676  1.00 21.73  ? 5254 HOH A O     1 
HETATM 23787 O  O     . HOH H 5 .    ? 128.787 106.665 48.051  1.00 38.90  ? 5255 HOH A O     1 
HETATM 23788 O  O     . HOH H 5 .    ? 137.394 87.659  89.562  1.00 12.99  ? 5256 HOH A O     1 
HETATM 23789 O  O     . HOH H 5 .    ? 63.719  74.447  135.639 1.00 20.59  ? 5257 HOH A O     1 
HETATM 23790 O  O     . HOH H 5 .    ? 75.846  75.569  124.500 1.00 8.84   ? 5258 HOH A O     1 
HETATM 23791 O  O     . HOH H 5 .    ? 148.860 105.683 100.747 1.00 17.20  ? 5259 HOH A O     1 
HETATM 23792 O  O     . HOH H 5 .    ? 90.145  106.863 136.761 1.00 10.66  ? 5260 HOH A O     1 
HETATM 23793 O  O     . HOH H 5 .    ? 108.289 85.029  61.176  1.00 9.69   ? 5261 HOH A O     1 
HETATM 23794 O  O     . HOH H 5 .    ? 80.561  90.199  102.365 1.00 22.05  ? 5262 HOH A O     1 
HETATM 23795 O  O     . HOH H 5 .    ? 130.245 101.088 110.819 1.00 4.20   ? 5263 HOH A O     1 
HETATM 23796 O  O     . HOH H 5 .    ? 70.699  63.255  107.457 1.00 22.33  ? 5264 HOH A O     1 
HETATM 23797 O  O     . HOH H 5 .    ? 104.430 110.335 137.248 1.00 14.89  ? 5265 HOH A O     1 
HETATM 23798 O  O     . HOH H 5 .    ? 113.736 85.538  66.053  1.00 8.66   ? 5266 HOH A O     1 
HETATM 23799 O  O     . HOH H 5 .    ? 114.251 79.601  82.788  1.00 17.60  ? 5267 HOH A O     1 
HETATM 23800 O  O     . HOH H 5 .    ? 138.823 109.281 102.050 1.00 5.83   ? 5268 HOH A O     1 
HETATM 23801 O  O     . HOH H 5 .    ? 126.409 117.831 126.777 1.00 30.75  ? 5269 HOH A O     1 
HETATM 23802 O  O     . HOH H 5 .    ? 101.484 99.965  112.711 1.00 7.53   ? 5270 HOH A O     1 
HETATM 23803 O  O     . HOH H 5 .    ? 58.202  132.128 92.985  1.00 24.86  ? 5271 HOH A O     1 
HETATM 23804 O  O     . HOH H 5 .    ? 62.454  120.089 78.835  1.00 32.73  ? 5272 HOH A O     1 
HETATM 23805 O  O     . HOH H 5 .    ? 67.162  80.037  119.833 1.00 13.16  ? 5273 HOH A O     1 
HETATM 23806 O  O     . HOH H 5 .    ? 125.861 69.184  83.549  1.00 25.51  ? 5274 HOH A O     1 
HETATM 23807 O  O     . HOH H 5 .    ? 118.867 109.246 90.140  1.00 21.30  ? 5275 HOH A O     1 
HETATM 23808 O  O     . HOH H 5 .    ? 85.698  63.447  130.278 1.00 16.58  ? 5276 HOH A O     1 
HETATM 23809 O  O     . HOH H 5 .    ? 140.442 96.003  80.442  1.00 13.40  ? 5277 HOH A O     1 
HETATM 23810 O  O     . HOH H 5 .    ? 34.144  96.601  130.259 1.00 27.21  ? 5278 HOH A O     1 
HETATM 23811 O  O     . HOH H 5 .    ? 82.364  76.799  106.209 1.00 16.32  ? 5279 HOH A O     1 
HETATM 23812 O  O     . HOH H 5 .    ? 71.324  93.147  122.713 1.00 14.88  ? 5280 HOH A O     1 
HETATM 23813 O  O     . HOH H 5 .    ? 70.964  79.526  72.740  1.00 8.97   ? 5281 HOH A O     1 
HETATM 23814 O  O     . HOH H 5 .    ? 136.725 97.719  120.925 1.00 26.16  ? 5282 HOH A O     1 
HETATM 23815 O  O     . HOH H 5 .    ? 75.704  43.633  131.422 1.00 40.10  ? 5283 HOH A O     1 
HETATM 23816 O  O     . HOH H 5 .    ? 38.091  93.832  102.268 1.00 20.35  ? 5284 HOH A O     1 
HETATM 23817 O  O     . HOH H 5 .    ? 69.229  86.598  60.520  1.00 20.29  ? 5285 HOH A O     1 
HETATM 23818 O  O     . HOH H 5 .    ? 71.058  71.292  109.824 1.00 12.79  ? 5286 HOH A O     1 
HETATM 23819 O  O     . HOH H 5 .    ? 106.121 68.869  97.360  1.00 24.93  ? 5287 HOH A O     1 
HETATM 23820 O  O     . HOH H 5 .    ? 55.279  102.028 137.158 1.00 17.34  ? 5288 HOH A O     1 
HETATM 23821 O  O     . HOH H 5 .    ? 136.049 85.696  82.630  1.00 9.93   ? 5289 HOH A O     1 
HETATM 23822 O  O     . HOH H 5 .    ? 62.874  98.451  117.506 1.00 4.96   ? 5290 HOH A O     1 
HETATM 23823 O  O     . HOH H 5 .    ? 130.698 99.341  81.202  1.00 12.07  ? 5291 HOH A O     1 
HETATM 23824 O  O     . HOH H 5 .    ? 76.715  73.633  120.757 1.00 15.43  ? 5292 HOH A O     1 
HETATM 23825 O  O     . HOH H 5 .    ? 127.568 97.779  130.595 1.00 23.16  ? 5293 HOH A O     1 
HETATM 23826 O  O     . HOH H 5 .    ? 51.962  92.731  121.368 1.00 7.67   ? 5294 HOH A O     1 
HETATM 23827 O  O     . HOH H 5 .    ? 57.428  94.717  98.210  1.00 10.42  ? 5295 HOH A O     1 
HETATM 23828 O  O     . HOH H 5 .    ? 59.470  63.027  139.739 1.00 32.39  ? 5296 HOH A O     1 
HETATM 23829 O  O     . HOH H 5 .    ? 74.795  103.626 50.370  1.00 21.07  ? 5297 HOH A O     1 
HETATM 23830 O  O     . HOH H 5 .    ? 43.467  80.501  137.683 1.00 15.42  ? 5298 HOH A O     1 
HETATM 23831 O  O     . HOH H 5 .    ? 106.052 97.544  130.349 1.00 9.06   ? 5299 HOH A O     1 
HETATM 23832 O  O     . HOH H 5 .    ? 53.831  71.471  127.301 1.00 9.58   ? 5300 HOH A O     1 
HETATM 23833 O  O     . HOH H 5 .    ? 119.064 99.719  74.885  1.00 20.47  ? 5301 HOH A O     1 
HETATM 23834 O  O     . HOH H 5 .    ? 134.386 98.571  79.361  1.00 21.15  ? 5302 HOH A O     1 
HETATM 23835 O  O     . HOH H 5 .    ? 104.458 99.980  142.052 1.00 6.87   ? 5303 HOH A O     1 
HETATM 23836 O  O     . HOH H 5 .    ? 116.833 73.566  103.397 1.00 20.70  ? 5304 HOH A O     1 
HETATM 23837 O  O     . HOH H 5 .    ? 43.983  77.759  114.222 1.00 7.42   ? 5305 HOH A O     1 
HETATM 23838 O  O     . HOH H 5 .    ? 84.766  76.543  107.145 1.00 11.75  ? 5306 HOH A O     1 
HETATM 23839 O  O     . HOH H 5 .    ? 122.557 92.878  95.780  1.00 14.33  ? 5307 HOH A O     1 
HETATM 23840 O  O     . HOH H 5 .    ? 106.510 74.824  115.134 1.00 12.32  ? 5308 HOH A O     1 
HETATM 23841 O  O     . HOH H 5 .    ? 105.863 63.285  137.446 1.00 28.98  ? 5309 HOH A O     1 
HETATM 23842 O  O     . HOH H 5 .    ? 114.064 82.554  78.218  1.00 18.31  ? 5310 HOH A O     1 
HETATM 23843 O  O     . HOH H 5 .    ? 43.268  102.360 107.842 1.00 18.88  ? 5311 HOH A O     1 
HETATM 23844 O  O     . HOH H 5 .    ? 95.459  92.840  60.570  1.00 9.01   ? 5312 HOH A O     1 
HETATM 23845 O  O     . HOH H 5 .    ? 74.094  83.204  64.370  1.00 33.48  ? 5313 HOH A O     1 
HETATM 23846 O  O     . HOH H 5 .    ? 53.860  90.843  120.224 1.00 8.85   ? 5314 HOH A O     1 
HETATM 23847 O  O     . HOH H 5 .    ? 72.487  134.199 104.029 1.00 30.03  ? 5315 HOH A O     1 
HETATM 23848 O  O     . HOH H 5 .    ? 106.583 76.634  96.989  1.00 22.71  ? 5316 HOH A O     1 
HETATM 23849 O  O     . HOH H 5 .    ? 59.457  104.414 83.385  1.00 12.09  ? 5317 HOH A O     1 
HETATM 23850 O  O     . HOH H 5 .    ? 70.919  76.540  91.010  1.00 14.61  ? 5318 HOH A O     1 
HETATM 23851 O  O     . HOH H 5 .    ? 69.912  91.633  120.696 1.00 13.55  ? 5319 HOH A O     1 
HETATM 23852 O  O     . HOH H 5 .    ? 101.909 95.221  124.350 1.00 4.80   ? 5320 HOH A O     1 
HETATM 23853 O  O     . HOH H 5 .    ? 128.146 105.696 89.849  1.00 13.40  ? 5321 HOH A O     1 
HETATM 23854 O  O     . HOH H 5 .    ? 75.218  73.426  108.377 1.00 8.15   ? 5322 HOH A O     1 
HETATM 23855 O  O     . HOH H 5 .    ? 111.725 118.399 129.390 1.00 20.59  ? 5323 HOH A O     1 
HETATM 23856 O  O     . HOH H 5 .    ? 135.965 96.340  68.692  1.00 19.81  ? 5324 HOH A O     1 
HETATM 23857 O  O     . HOH H 5 .    ? 130.807 93.927  67.927  1.00 21.92  ? 5325 HOH A O     1 
HETATM 23858 O  O     . HOH H 5 .    ? 131.724 97.419  122.433 1.00 13.79  ? 5326 HOH A O     1 
HETATM 23859 O  O     . HOH H 5 .    ? 56.179  103.130 74.759  1.00 14.97  ? 5327 HOH A O     1 
HETATM 23860 O  O     . HOH H 5 .    ? 102.583 89.700  99.497  1.00 17.15  ? 5328 HOH A O     1 
HETATM 23861 O  O     . HOH H 5 .    ? 122.732 81.004  111.711 1.00 19.98  ? 5329 HOH A O     1 
HETATM 23862 O  O     . HOH H 5 .    ? 145.351 95.498  85.857  1.00 6.84   ? 5330 HOH A O     1 
HETATM 23863 O  O     . HOH H 5 .    ? 148.147 99.373  113.985 1.00 32.21  ? 5331 HOH A O     1 
HETATM 23864 O  O     . HOH H 5 .    ? 40.801  114.515 89.899  1.00 29.32  ? 5332 HOH A O     1 
HETATM 23865 O  O     . HOH H 5 .    ? 66.172  56.385  125.213 1.00 25.58  ? 5333 HOH A O     1 
HETATM 23866 O  O     . HOH H 5 .    ? 127.609 92.778  86.944  1.00 5.90   ? 5334 HOH A O     1 
HETATM 23867 O  O     . HOH H 5 .    ? 58.495  76.521  114.777 1.00 5.32   ? 5335 HOH A O     1 
HETATM 23868 O  O     . HOH H 5 .    ? 72.401  102.050 43.375  1.00 31.70  ? 5336 HOH A O     1 
HETATM 23869 O  O     . HOH H 5 .    ? 53.845  82.950  138.637 1.00 18.69  ? 5337 HOH A O     1 
HETATM 23870 O  O     . HOH H 5 .    ? 153.504 102.983 86.793  1.00 22.49  ? 5338 HOH A O     1 
HETATM 23871 O  O     . HOH H 5 .    ? 113.153 83.382  31.991  1.00 43.66  ? 5339 HOH A O     1 
HETATM 23872 O  O     . HOH H 5 .    ? 87.439  53.134  111.918 1.00 37.55  ? 5340 HOH A O     1 
HETATM 23873 O  O     . HOH H 5 .    ? 75.067  93.733  113.355 1.00 11.26  ? 5341 HOH A O     1 
HETATM 23874 O  O     . HOH H 5 .    ? 104.534 106.660 145.030 1.00 25.98  ? 5342 HOH A O     1 
HETATM 23875 O  O     . HOH H 5 .    ? 118.555 74.195  118.370 1.00 11.67  ? 5343 HOH A O     1 
HETATM 23876 O  O     . HOH H 5 .    ? 77.314  66.429  109.435 1.00 20.43  ? 5344 HOH A O     1 
HETATM 23877 O  O     . HOH H 5 .    ? 100.505 109.581 132.306 1.00 15.54  ? 5345 HOH A O     1 
HETATM 23878 O  O     . HOH H 5 .    ? 129.451 114.690 88.987  1.00 26.45  ? 5346 HOH A O     1 
HETATM 23879 O  O     . HOH H 5 .    ? 56.399  80.145  109.386 1.00 4.63   ? 5347 HOH A O     1 
HETATM 23880 O  O     . HOH H 5 .    ? 104.551 89.801  61.086  1.00 5.12   ? 5348 HOH A O     1 
HETATM 23881 O  O     . HOH H 5 .    ? 65.755  102.950 50.474  1.00 20.80  ? 5349 HOH A O     1 
HETATM 23882 O  O     . HOH H 5 .    ? 91.693  97.250  117.804 1.00 6.66   ? 5350 HOH A O     1 
HETATM 23883 O  O     . HOH H 5 .    ? 56.443  106.551 117.681 1.00 9.75   ? 5351 HOH A O     1 
HETATM 23884 O  O     . HOH H 5 .    ? 97.094  80.962  111.561 1.00 13.78  ? 5352 HOH A O     1 
HETATM 23885 O  O     . HOH H 5 .    ? 67.566  120.362 86.086  1.00 13.54  ? 5353 HOH A O     1 
HETATM 23886 O  O     . HOH H 5 .    ? 123.375 79.422  96.923  1.00 3.66   ? 5354 HOH A O     1 
HETATM 23887 O  O     . HOH H 5 .    ? 52.108  61.749  125.197 1.00 20.81  ? 5355 HOH A O     1 
HETATM 23888 O  O     . HOH H 5 .    ? 37.094  88.893  112.616 1.00 37.03  ? 5356 HOH A O     1 
HETATM 23889 O  O     . HOH H 5 .    ? 113.363 95.432  70.375  1.00 13.35  ? 5357 HOH A O     1 
HETATM 23890 O  O     . HOH H 5 .    ? 95.650  90.821  127.839 1.00 2.98   ? 5358 HOH A O     1 
HETATM 23891 O  O     . HOH H 5 .    ? 51.821  77.292  103.721 1.00 23.79  ? 5359 HOH A O     1 
HETATM 23892 O  O     . HOH H 5 .    ? 43.743  106.556 115.329 1.00 12.88  ? 5360 HOH A O     1 
HETATM 23893 O  O     . HOH H 5 .    ? 61.108  90.174  122.621 1.00 13.70  ? 5361 HOH A O     1 
HETATM 23894 O  O     . HOH H 5 .    ? 67.595  108.410 82.777  1.00 28.23  ? 5362 HOH A O     1 
HETATM 23895 O  O     . HOH H 5 .    ? 113.401 94.091  42.607  1.00 32.66  ? 5363 HOH A O     1 
HETATM 23896 O  O     . HOH H 5 .    ? 50.524  79.097  110.646 1.00 8.21   ? 5364 HOH A O     1 
HETATM 23897 O  O     . HOH H 5 .    ? 110.975 80.755  114.671 1.00 10.82  ? 5365 HOH A O     1 
HETATM 23898 O  O     . HOH H 5 .    ? 81.600  78.908  142.090 1.00 18.82  ? 5366 HOH A O     1 
HETATM 23899 O  O     . HOH H 5 .    ? 41.928  72.079  128.012 1.00 12.60  ? 5367 HOH A O     1 
HETATM 23900 O  O     . HOH H 5 .    ? 55.624  106.522 125.752 1.00 22.35  ? 5368 HOH A O     1 
HETATM 23901 O  O     . HOH H 5 .    ? 93.184  78.748  126.880 1.00 2.68   ? 5369 HOH A O     1 
HETATM 23902 O  O     . HOH H 5 .    ? 121.675 74.595  79.310  1.00 18.34  ? 5370 HOH A O     1 
HETATM 23903 O  O     . HOH H 5 .    ? 48.120  80.149  141.438 1.00 21.74  ? 5371 HOH A O     1 
HETATM 23904 O  O     . HOH H 5 .    ? 52.341  65.350  134.280 1.00 15.61  ? 5372 HOH A O     1 
HETATM 23905 O  O     . HOH H 5 .    ? 50.738  89.109  101.137 1.00 4.43   ? 5373 HOH A O     1 
HETATM 23906 O  O     . HOH H 5 .    ? 105.693 112.130 106.179 1.00 32.38  ? 5374 HOH A O     1 
HETATM 23907 O  O     . HOH H 5 .    ? 66.724  56.401  133.001 1.00 36.24  ? 5375 HOH A O     1 
HETATM 23908 O  O     . HOH H 5 .    ? 95.264  97.370  113.540 1.00 14.47  ? 5376 HOH A O     1 
HETATM 23909 O  O     . HOH H 5 .    ? 64.241  120.241 61.553  1.00 34.70  ? 5377 HOH A O     1 
HETATM 23910 O  O     . HOH H 5 .    ? 63.014  93.050  96.161  1.00 15.69  ? 5378 HOH A O     1 
HETATM 23911 O  O     . HOH H 5 .    ? 111.668 87.724  81.595  1.00 17.47  ? 5379 HOH A O     1 
HETATM 23912 O  O     . HOH H 5 .    ? 96.697  102.981 117.964 1.00 16.59  ? 5380 HOH A O     1 
HETATM 23913 O  O     . HOH H 5 .    ? 120.037 93.957  108.678 1.00 9.17   ? 5381 HOH A O     1 
HETATM 23914 O  O     . HOH H 5 .    ? 111.904 68.608  113.955 1.00 18.85  ? 5382 HOH A O     1 
HETATM 23915 O  O     . HOH H 5 .    ? 84.490  97.186  129.546 1.00 12.74  ? 5383 HOH A O     1 
HETATM 23916 O  O     . HOH H 5 .    ? 98.031  64.372  77.028  1.00 20.92  ? 5384 HOH A O     1 
HETATM 23917 O  O     . HOH H 5 .    ? 65.461  104.948 79.669  1.00 21.85  ? 5385 HOH A O     1 
HETATM 23918 O  O     . HOH H 5 .    ? 102.214 88.856  105.112 1.00 11.65  ? 5386 HOH A O     1 
HETATM 23919 O  O     . HOH H 5 .    ? 104.958 95.540  146.252 1.00 20.49  ? 5387 HOH A O     1 
HETATM 23920 O  O     . HOH H 5 .    ? 78.612  73.077  96.337  1.00 12.82  ? 5388 HOH A O     1 
HETATM 23921 O  O     . HOH H 5 .    ? 123.473 99.363  83.159  1.00 4.40   ? 5389 HOH A O     1 
HETATM 23922 O  O     . HOH H 5 .    ? 78.609  105.035 53.936  1.00 20.98  ? 5390 HOH A O     1 
HETATM 23923 O  O     . HOH H 5 .    ? 66.976  86.036  62.062  1.00 28.07  ? 5391 HOH A O     1 
HETATM 23924 O  O     . HOH H 5 .    ? 96.052  102.711 54.880  1.00 20.91  ? 5392 HOH A O     1 
HETATM 23925 O  O     . HOH H 5 .    ? 35.992  87.054  126.515 1.00 28.23  ? 5393 HOH A O     1 
HETATM 23926 O  O     . HOH H 5 .    ? 57.786  90.704  122.271 1.00 9.82   ? 5394 HOH A O     1 
HETATM 23927 O  O     . HOH H 5 .    ? 47.320  93.103  118.791 1.00 3.69   ? 5395 HOH A O     1 
HETATM 23928 O  O     . HOH H 5 .    ? 111.144 73.657  67.663  1.00 13.90  ? 5396 HOH A O     1 
HETATM 23929 O  O     . HOH H 5 .    ? 117.572 88.924  102.414 1.00 22.82  ? 5397 HOH A O     1 
HETATM 23930 O  O     . HOH H 5 .    ? 106.671 87.192  98.917  1.00 35.48  ? 5398 HOH A O     1 
HETATM 23931 O  O     . HOH H 5 .    ? 58.240  75.712  81.527  1.00 38.34  ? 5399 HOH A O     1 
HETATM 23932 O  O     . HOH H 5 .    ? 82.572  126.464 110.492 1.00 43.32  ? 5400 HOH A O     1 
HETATM 23933 O  O     . HOH H 5 .    ? 111.712 67.632  91.105  1.00 20.04  ? 5401 HOH A O     1 
HETATM 23934 O  O     . HOH H 5 .    ? 123.752 97.489  81.302  1.00 13.24  ? 5402 HOH A O     1 
HETATM 23935 O  O     . HOH H 5 .    ? 96.225  60.140  123.628 1.00 16.10  ? 5403 HOH A O     1 
HETATM 23936 O  O     . HOH H 5 .    ? 52.237  82.973  97.851  1.00 16.14  ? 5404 HOH A O     1 
HETATM 23937 O  O     . HOH H 5 .    ? 109.796 65.454  140.983 1.00 35.19  ? 5405 HOH A O     1 
HETATM 23938 O  O     . HOH H 5 .    ? 55.826  110.617 106.627 1.00 9.01   ? 5406 HOH A O     1 
HETATM 23939 O  O     . HOH H 5 .    ? 41.286  88.231  109.173 1.00 16.36  ? 5407 HOH A O     1 
HETATM 23940 O  O     . HOH H 5 .    ? 79.215  94.848  96.564  1.00 35.15  ? 5408 HOH A O     1 
HETATM 23941 O  O     . HOH H 5 .    ? 113.640 80.670  34.855  1.00 44.00  ? 5409 HOH A O     1 
HETATM 23942 O  O     . HOH H 5 .    ? 130.956 75.806  94.126  1.00 8.86   ? 5410 HOH A O     1 
HETATM 23943 O  O     . HOH H 5 .    ? 126.318 102.310 123.606 1.00 5.37   ? 5411 HOH A O     1 
HETATM 23944 O  O     . HOH H 5 .    ? 44.924  104.128 104.451 1.00 16.14  ? 5412 HOH A O     1 
HETATM 23945 O  O     . HOH H 5 .    ? 91.302  90.320  64.701  1.00 19.35  ? 5413 HOH A O     1 
HETATM 23946 O  O     . HOH H 5 .    ? 112.872 95.878  130.672 1.00 8.19   ? 5414 HOH A O     1 
HETATM 23947 O  O     . HOH H 5 .    ? 85.530  64.931  120.421 1.00 35.00  ? 5415 HOH A O     1 
HETATM 23948 O  O     . HOH H 5 .    ? 65.454  75.444  125.379 1.00 10.68  ? 5416 HOH A O     1 
HETATM 23949 O  O     . HOH H 5 .    ? 113.982 102.442 121.665 1.00 7.21   ? 5417 HOH A O     1 
HETATM 23950 O  O     . HOH H 5 .    ? 60.463  136.239 103.772 1.00 37.62  ? 5418 HOH A O     1 
HETATM 23951 O  O     . HOH H 5 .    ? 44.838  76.013  119.587 1.00 7.32   ? 5419 HOH A O     1 
HETATM 23952 O  O     . HOH H 5 .    ? 106.988 97.485  45.736  1.00 45.97  ? 5420 HOH A O     1 
HETATM 23953 O  O     . HOH H 5 .    ? 127.654 100.155 107.040 1.00 10.51  ? 5421 HOH A O     1 
HETATM 23954 O  O     . HOH H 5 .    ? 74.685  93.566  123.776 1.00 9.87   ? 5422 HOH A O     1 
HETATM 23955 O  O     . HOH H 5 .    ? 116.628 89.345  121.780 1.00 5.28   ? 5423 HOH A O     1 
HETATM 23956 O  O     . HOH H 5 .    ? 139.776 115.057 87.568  1.00 26.44  ? 5424 HOH A O     1 
HETATM 23957 O  O     . HOH H 5 .    ? 71.403  70.247  86.058  1.00 17.70  ? 5425 HOH A O     1 
HETATM 23958 O  O     . HOH H 5 .    ? 73.753  127.222 106.241 1.00 28.05  ? 5426 HOH A O     1 
HETATM 23959 O  O     . HOH H 5 .    ? 61.727  111.384 124.468 1.00 24.48  ? 5427 HOH A O     1 
HETATM 23960 O  O     . HOH H 5 .    ? 121.794 70.651  76.934  1.00 36.25  ? 5428 HOH A O     1 
HETATM 23961 O  O     . HOH H 5 .    ? 38.892  112.717 83.441  1.00 43.27  ? 5429 HOH A O     1 
HETATM 23962 O  O     . HOH H 5 .    ? 50.186  105.696 105.677 1.00 19.67  ? 5430 HOH A O     1 
HETATM 23963 O  O     . HOH H 5 .    ? 84.760  83.971  67.454  1.00 18.12  ? 5431 HOH A O     1 
HETATM 23964 O  O     . HOH H 5 .    ? 121.850 102.135 74.906  1.00 44.14  ? 5432 HOH A O     1 
HETATM 23965 O  O     . HOH H 5 .    ? 75.296  106.870 119.671 1.00 15.63  ? 5433 HOH A O     1 
HETATM 23966 O  O     . HOH H 5 .    ? 130.315 98.129  53.036  1.00 36.54  ? 5434 HOH A O     1 
HETATM 23967 O  O     . HOH H 5 .    ? 106.929 113.423 137.125 1.00 40.81  ? 5435 HOH A O     1 
HETATM 23968 O  O     . HOH H 5 .    ? 109.062 67.798  102.544 1.00 16.45  ? 5436 HOH A O     1 
HETATM 23969 O  O     . HOH H 5 .    ? 121.778 85.099  34.877  1.00 38.41  ? 5437 HOH A O     1 
HETATM 23970 O  O     . HOH H 5 .    ? 81.964  71.539  73.356  1.00 32.95  ? 5438 HOH A O     1 
HETATM 23971 O  O     . HOH H 5 .    ? 82.607  121.068 125.010 1.00 44.45  ? 5439 HOH A O     1 
HETATM 23972 O  O     . HOH H 5 .    ? 33.892  106.269 99.446  1.00 28.62  ? 5440 HOH A O     1 
HETATM 23973 O  O     . HOH H 5 .    ? 114.799 91.024  139.122 1.00 25.03  ? 5441 HOH A O     1 
HETATM 23974 O  O     . HOH H 5 .    ? 74.475  105.067 53.012  1.00 18.59  ? 5442 HOH A O     1 
HETATM 23975 O  O     . HOH H 5 .    ? 154.535 102.069 97.795  1.00 33.83  ? 5443 HOH A O     1 
HETATM 23976 O  O     . HOH H 5 .    ? 154.537 105.863 94.009  1.00 37.04  ? 5444 HOH A O     1 
HETATM 23977 O  O     . HOH H 5 .    ? 48.079  97.454  85.551  1.00 20.56  ? 5445 HOH A O     1 
HETATM 23978 O  O     . HOH H 5 .    ? 69.320  86.249  88.168  1.00 12.07  ? 5446 HOH A O     1 
HETATM 23979 O  O     . HOH H 5 .    ? 70.519  102.232 118.268 1.00 9.40   ? 5447 HOH A O     1 
HETATM 23980 O  O     . HOH H 5 .    ? 122.411 85.795  105.401 1.00 32.72  ? 5448 HOH A O     1 
HETATM 23981 O  O     . HOH H 5 .    ? 116.773 81.978  50.403  1.00 19.29  ? 5449 HOH A O     1 
HETATM 23982 O  O     . HOH H 5 .    ? 89.198  95.341  61.449  1.00 20.74  ? 5450 HOH A O     1 
HETATM 23983 O  O     . HOH H 5 .    ? 122.473 80.174  106.300 1.00 20.54  ? 5451 HOH A O     1 
HETATM 23984 O  O     . HOH H 5 .    ? 51.601  90.068  141.689 1.00 30.60  ? 5452 HOH A O     1 
HETATM 23985 O  O     . HOH H 5 .    ? 74.888  91.260  93.763  1.00 25.44  ? 5453 HOH A O     1 
HETATM 23986 O  O     . HOH H 5 .    ? 114.759 100.282 101.686 1.00 23.34  ? 5454 HOH A O     1 
HETATM 23987 O  O     . HOH H 5 .    ? 69.024  110.633 100.711 1.00 24.03  ? 5455 HOH A O     1 
HETATM 23988 O  O     . HOH H 5 .    ? 128.194 100.790 79.735  1.00 12.08  ? 5456 HOH A O     1 
HETATM 23989 O  O     . HOH H 5 .    ? 126.802 91.422  66.353  1.00 22.84  ? 5457 HOH A O     1 
HETATM 23990 O  O     . HOH H 5 .    ? 134.936 92.944  82.242  1.00 5.16   ? 5458 HOH A O     1 
HETATM 23991 O  O     . HOH H 5 .    ? 108.548 107.110 141.555 1.00 12.46  ? 5459 HOH A O     1 
HETATM 23992 O  O     . HOH H 5 .    ? 76.915  73.583  129.935 1.00 15.99  ? 5460 HOH A O     1 
HETATM 23993 O  O     . HOH H 5 .    ? 88.966  106.103 147.688 1.00 24.86  ? 5461 HOH A O     1 
HETATM 23994 O  O     . HOH H 5 .    ? 97.173  73.632  112.681 1.00 23.89  ? 5462 HOH A O     1 
HETATM 23995 O  O     . HOH H 5 .    ? 82.779  97.107  121.641 1.00 16.32  ? 5463 HOH A O     1 
HETATM 23996 O  O     . HOH H 5 .    ? 127.280 99.783  111.464 1.00 6.05   ? 5464 HOH A O     1 
HETATM 23997 O  O     . HOH H 5 .    ? 128.228 69.588  77.304  1.00 31.14  ? 5465 HOH A O     1 
HETATM 23998 O  O     . HOH H 5 .    ? 89.020  41.968  128.223 1.00 26.90  ? 5466 HOH A O     1 
HETATM 23999 O  O     . HOH H 5 .    ? 66.976  77.394  121.398 1.00 19.46  ? 5467 HOH A O     1 
HETATM 24000 O  O     . HOH H 5 .    ? 62.294  80.641  119.695 1.00 8.19   ? 5468 HOH A O     1 
HETATM 24001 O  O     . HOH H 5 .    ? 97.229  95.309  54.912  1.00 13.69  ? 5469 HOH A O     1 
HETATM 24002 O  O     . HOH H 5 .    ? 137.319 110.697 99.656  1.00 6.16   ? 5470 HOH A O     1 
HETATM 24003 O  O     . HOH H 5 .    ? 118.641 83.454  57.408  1.00 17.65  ? 5471 HOH A O     1 
HETATM 24004 O  O     . HOH H 5 .    ? 104.295 64.027  75.807  1.00 34.49  ? 5472 HOH A O     1 
HETATM 24005 O  O     . HOH H 5 .    ? 126.501 98.947  127.720 1.00 14.20  ? 5473 HOH A O     1 
HETATM 24006 O  O     . HOH H 5 .    ? 109.123 85.463  124.846 1.00 10.47  ? 5474 HOH A O     1 
HETATM 24007 O  O     . HOH H 5 .    ? 87.011  71.563  121.270 1.00 4.81   ? 5475 HOH A O     1 
HETATM 24008 O  O     . HOH H 5 .    ? 69.856  88.489  90.033  1.00 12.86  ? 5476 HOH A O     1 
HETATM 24009 O  O     . HOH H 5 .    ? 53.445  79.764  139.925 1.00 17.67  ? 5477 HOH A O     1 
HETATM 24010 O  O     . HOH H 5 .    ? 67.242  111.621 103.145 1.00 23.26  ? 5478 HOH A O     1 
HETATM 24011 O  O     . HOH H 5 .    ? 126.374 92.485  103.934 1.00 10.48  ? 5479 HOH A O     1 
HETATM 24012 O  O     . HOH H 5 .    ? 45.115  89.393  131.626 1.00 15.23  ? 5480 HOH A O     1 
HETATM 24013 O  O     . HOH H 5 .    ? 124.396 112.681 83.224  1.00 31.20  ? 5481 HOH A O     1 
HETATM 24014 O  O     . HOH H 5 .    ? 83.133  95.671  113.694 1.00 18.01  ? 5482 HOH A O     1 
HETATM 24015 O  O     . HOH H 5 .    ? 77.817  85.297  130.510 1.00 3.44   ? 5483 HOH A O     1 
HETATM 24016 O  O     . HOH H 5 .    ? 115.409 99.305  79.871  1.00 16.33  ? 5484 HOH A O     1 
HETATM 24017 O  O     . HOH H 5 .    ? 134.434 86.295  90.484  1.00 16.29  ? 5485 HOH A O     1 
HETATM 24018 O  O     . HOH H 5 .    ? 94.559  89.482  70.296  1.00 22.94  ? 5486 HOH A O     1 
HETATM 24019 O  O     . HOH H 5 .    ? 74.880  72.157  126.932 1.00 26.68  ? 5487 HOH A O     1 
HETATM 24020 O  O     . HOH H 5 .    ? 93.184  98.400  115.311 1.00 13.50  ? 5488 HOH A O     1 
HETATM 24021 O  O     . HOH H 5 .    ? 72.167  81.581  124.969 1.00 8.81   ? 5489 HOH A O     1 
HETATM 24022 O  O     . HOH H 5 .    ? 90.272  72.485  132.303 1.00 22.46  ? 5490 HOH A O     1 
HETATM 24023 O  O     . HOH H 5 .    ? 74.347  119.803 82.466  1.00 19.99  ? 5491 HOH A O     1 
HETATM 24024 O  O     . HOH H 5 .    ? 64.521  77.811  128.669 1.00 13.51  ? 5492 HOH A O     1 
HETATM 24025 O  O     . HOH H 5 .    ? 66.145  94.687  74.911  1.00 17.87  ? 5493 HOH A O     1 
HETATM 24026 O  O     . HOH H 5 .    ? 87.572  77.475  71.386  1.00 23.60  ? 5494 HOH A O     1 
HETATM 24027 O  O     . HOH H 5 .    ? 43.204  72.755  123.773 1.00 18.72  ? 5495 HOH A O     1 
HETATM 24028 O  O     . HOH H 5 .    ? 108.509 100.135 111.124 1.00 9.00   ? 5496 HOH A O     1 
HETATM 24029 O  O     . HOH H 5 .    ? 99.679  70.483  129.141 1.00 24.55  ? 5497 HOH A O     1 
HETATM 24030 O  O     . HOH H 5 .    ? 129.567 77.247  92.753  1.00 13.69  ? 5498 HOH A O     1 
HETATM 24031 O  O     . HOH H 5 .    ? 134.219 110.534 135.777 1.00 16.65  ? 5499 HOH A O     1 
HETATM 24032 O  O     . HOH H 5 .    ? 126.048 103.609 112.290 1.00 11.54  ? 5500 HOH A O     1 
HETATM 24033 O  O     . HOH H 5 .    ? 80.369  127.046 73.119  1.00 46.91  ? 5501 HOH A O     1 
HETATM 24034 O  O     . HOH H 5 .    ? 36.061  101.038 85.893  1.00 20.15  ? 5502 HOH A O     1 
HETATM 24035 O  O     . HOH H 5 .    ? 105.250 103.128 114.702 1.00 11.29  ? 5503 HOH A O     1 
HETATM 24036 O  O     . HOH H 5 .    ? 114.641 107.961 97.539  1.00 32.88  ? 5504 HOH A O     1 
HETATM 24037 O  O     . HOH H 5 .    ? 133.112 91.143  115.153 1.00 15.22  ? 5505 HOH A O     1 
HETATM 24038 O  O     . HOH H 5 .    ? 47.521  64.996  126.414 1.00 17.79  ? 5506 HOH A O     1 
HETATM 24039 O  O     . HOH H 5 .    ? 60.757  94.095  99.395  1.00 5.26   ? 5507 HOH A O     1 
HETATM 24040 O  O     . HOH H 5 .    ? 97.019  98.478  64.016  1.00 16.04  ? 5508 HOH A O     1 
HETATM 24041 O  O     . HOH H 5 .    ? 107.881 101.615 113.335 1.00 6.43   ? 5509 HOH A O     1 
HETATM 24042 O  O     . HOH H 5 .    ? 56.825  93.716  120.291 1.00 10.20  ? 5510 HOH A O     1 
HETATM 24043 O  O     . HOH H 5 .    ? 122.112 92.307  105.804 1.00 13.14  ? 5511 HOH A O     1 
HETATM 24044 O  O     . HOH H 5 .    ? 75.458  63.816  77.286  1.00 35.37  ? 5512 HOH A O     1 
HETATM 24045 O  O     . HOH H 5 .    ? 43.906  75.212  122.578 1.00 10.14  ? 5513 HOH A O     1 
HETATM 24046 O  O     . HOH H 5 .    ? 130.570 103.789 111.488 1.00 15.64  ? 5514 HOH A O     1 
HETATM 24047 O  O     . HOH H 5 .    ? 144.363 83.387  89.273  1.00 22.77  ? 5515 HOH A O     1 
HETATM 24048 O  O     . HOH H 5 .    ? 134.859 108.648 122.290 1.00 17.91  ? 5516 HOH A O     1 
HETATM 24049 O  O     . HOH H 5 .    ? 142.081 100.499 111.678 1.00 22.08  ? 5517 HOH A O     1 
HETATM 24050 O  O     . HOH H 5 .    ? 113.643 69.979  116.216 1.00 11.56  ? 5518 HOH A O     1 
HETATM 24051 O  O     . HOH H 5 .    ? 66.404  117.058 74.965  1.00 10.46  ? 5519 HOH A O     1 
HETATM 24052 O  O     . HOH H 5 .    ? 132.594 94.089  74.934  1.00 11.31  ? 5520 HOH A O     1 
HETATM 24053 O  O     . HOH H 5 .    ? 79.833  69.111  133.414 1.00 15.04  ? 5521 HOH A O     1 
HETATM 24054 O  O     . HOH H 5 .    ? 90.778  92.178  120.561 1.00 3.08   ? 5522 HOH A O     1 
HETATM 24055 O  O     . HOH H 5 .    ? 103.372 88.469  141.782 1.00 26.45  ? 5523 HOH A O     1 
HETATM 24056 O  O     . HOH H 5 .    ? 80.921  97.200  32.933  1.00 38.47  ? 5524 HOH A O     1 
HETATM 24057 O  O     . HOH H 5 .    ? 72.912  66.620  131.935 1.00 20.68  ? 5525 HOH A O     1 
HETATM 24058 O  O     . HOH H 5 .    ? 135.770 91.992  113.527 1.00 20.76  ? 5526 HOH A O     1 
HETATM 24059 O  O     . HOH H 5 .    ? 74.197  94.346  100.559 1.00 30.35  ? 5527 HOH A O     1 
HETATM 24060 O  O     . HOH H 5 .    ? 98.552  81.980  118.872 1.00 3.27   ? 5528 HOH A O     1 
HETATM 24061 O  O     . HOH H 5 .    ? 61.482  123.014 63.847  1.00 32.56  ? 5529 HOH A O     1 
HETATM 24062 O  O     . HOH H 5 .    ? 68.562  83.200  120.148 1.00 8.17   ? 5530 HOH A O     1 
HETATM 24063 O  O     . HOH H 5 .    ? 122.670 60.949  111.488 1.00 33.29  ? 5531 HOH A O     1 
HETATM 24064 O  O     . HOH H 5 .    ? 116.311 103.398 110.513 1.00 10.84  ? 5532 HOH A O     1 
HETATM 24065 O  O     . HOH H 5 .    ? 104.955 91.373  69.121  1.00 15.02  ? 5533 HOH A O     1 
HETATM 24066 O  O     . HOH H 5 .    ? 49.478  75.764  138.451 1.00 14.47  ? 5534 HOH A O     1 
HETATM 24067 O  O     . HOH H 5 .    ? 103.810 110.042 94.811  1.00 34.19  ? 5535 HOH A O     1 
HETATM 24068 O  O     . HOH H 5 .    ? 60.693  95.301  126.674 1.00 13.39  ? 5536 HOH A O     1 
HETATM 24069 O  O     . HOH H 5 .    ? 65.505  107.699 72.657  1.00 18.33  ? 5537 HOH A O     1 
HETATM 24070 O  O     . HOH H 5 .    ? 65.938  101.310 100.681 1.00 10.25  ? 5538 HOH A O     1 
HETATM 24071 O  O     . HOH H 5 .    ? 60.470  114.142 80.580  1.00 14.26  ? 5539 HOH A O     1 
HETATM 24072 O  O     . HOH H 5 .    ? 134.674 78.625  87.282  1.00 17.50  ? 5540 HOH A O     1 
HETATM 24073 O  O     . HOH H 5 .    ? 61.931  102.725 58.533  1.00 19.29  ? 5541 HOH A O     1 
HETATM 24074 O  O     . HOH H 5 .    ? 119.170 96.769  105.953 1.00 5.67   ? 5542 HOH A O     1 
HETATM 24075 O  O     . HOH H 5 .    ? 73.464  81.402  127.150 1.00 10.89  ? 5543 HOH A O     1 
HETATM 24076 O  O     . HOH H 5 .    ? 65.821  90.630  42.926  1.00 26.85  ? 5544 HOH A O     1 
HETATM 24077 O  O     . HOH H 5 .    ? 69.395  90.067  83.617  1.00 8.73   ? 5545 HOH A O     1 
HETATM 24078 O  O     . HOH H 5 .    ? 89.803  99.563  106.104 1.00 21.08  ? 5546 HOH A O     1 
HETATM 24079 O  O     . HOH H 5 .    ? 87.871  70.334  116.869 1.00 9.22   ? 5547 HOH A O     1 
HETATM 24080 O  O     . HOH H 5 .    ? 110.240 95.514  146.773 1.00 15.78  ? 5548 HOH A O     1 
HETATM 24081 O  O     . HOH H 5 .    ? 96.427  69.928  51.983  1.00 25.19  ? 5549 HOH A O     1 
HETATM 24082 O  O     . HOH H 5 .    ? 67.152  74.181  133.593 1.00 20.26  ? 5550 HOH A O     1 
HETATM 24083 O  O     . HOH H 5 .    ? 102.549 106.823 59.598  1.00 32.37  ? 5551 HOH A O     1 
HETATM 24084 O  O     . HOH H 5 .    ? 35.902  97.641  101.568 1.00 27.33  ? 5552 HOH A O     1 
HETATM 24085 O  O     . HOH H 5 .    ? 32.376  95.629  105.870 1.00 32.57  ? 5553 HOH A O     1 
HETATM 24086 O  O     . HOH H 5 .    ? 70.189  92.332  112.651 1.00 8.25   ? 5554 HOH A O     1 
HETATM 24087 O  O     . HOH H 5 .    ? 72.000  94.015  98.749  1.00 23.42  ? 5555 HOH A O     1 
HETATM 24088 O  O     . HOH H 5 .    ? 111.583 106.927 101.934 1.00 36.89  ? 5556 HOH A O     1 
HETATM 24089 O  O     . HOH H 5 .    ? 87.220  54.138  132.885 1.00 25.60  ? 5557 HOH A O     1 
HETATM 24090 O  O     . HOH H 5 .    ? 96.313  75.440  126.623 1.00 6.55   ? 5558 HOH A O     1 
HETATM 24091 O  O     . HOH H 5 .    ? 52.419  86.788  123.204 1.00 7.46   ? 5559 HOH A O     1 
HETATM 24092 O  O     . HOH H 5 .    ? 118.927 72.387  116.573 1.00 18.21  ? 5560 HOH A O     1 
HETATM 24093 O  O     . HOH H 5 .    ? 36.953  94.406  127.812 1.00 26.56  ? 5561 HOH A O     1 
HETATM 24094 O  O     . HOH H 5 .    ? 100.980 66.216  135.574 1.00 18.12  ? 5562 HOH A O     1 
HETATM 24095 O  O     . HOH H 5 .    ? 69.627  72.340  131.663 1.00 16.98  ? 5563 HOH A O     1 
HETATM 24096 O  O     . HOH H 5 .    ? 63.690  114.625 97.393  1.00 16.62  ? 5564 HOH A O     1 
HETATM 24097 O  O     . HOH H 5 .    ? 101.981 88.696  108.545 1.00 4.22   ? 5565 HOH A O     1 
HETATM 24098 O  O     . HOH H 5 .    ? 40.778  102.194 135.580 1.00 21.47  ? 5566 HOH A O     1 
HETATM 24099 O  O     . HOH H 5 .    ? 129.166 101.005 48.259  1.00 31.45  ? 5567 HOH A O     1 
HETATM 24100 O  O     . HOH H 5 .    ? 116.080 105.820 85.416  1.00 22.39  ? 5568 HOH A O     1 
HETATM 24101 O  O     . HOH H 5 .    ? 114.544 100.051 68.436  1.00 17.08  ? 5569 HOH A O     1 
HETATM 24102 O  O     . HOH H 5 .    ? 65.728  95.040  135.198 1.00 18.45  ? 5570 HOH A O     1 
HETATM 24103 O  O     . HOH H 5 .    ? 77.527  98.957  124.450 1.00 22.68  ? 5571 HOH A O     1 
HETATM 24104 O  O     . HOH H 5 .    ? 137.417 111.178 105.562 1.00 10.95  ? 5572 HOH A O     1 
HETATM 24105 O  O     . HOH H 5 .    ? 59.897  84.516  106.437 1.00 3.85   ? 5573 HOH A O     1 
HETATM 24106 O  O     . HOH H 5 .    ? 46.253  104.923 131.268 1.00 31.13  ? 5574 HOH A O     1 
HETATM 24107 O  O     . HOH H 5 .    ? 77.376  82.039  68.720  1.00 26.51  ? 5575 HOH A O     1 
HETATM 24108 O  O     . HOH H 5 .    ? 111.072 83.264  52.610  1.00 13.10  ? 5576 HOH A O     1 
HETATM 24109 O  O     . HOH H 5 .    ? 112.595 104.865 63.560  1.00 17.05  ? 5577 HOH A O     1 
HETATM 24110 O  O     . HOH H 5 .    ? 103.438 101.633 124.305 1.00 15.48  ? 5578 HOH A O     1 
HETATM 24111 O  O     . HOH H 5 .    ? 132.502 96.072  76.780  1.00 28.65  ? 5579 HOH A O     1 
HETATM 24112 O  O     . HOH H 5 .    ? 95.313  64.768  129.364 1.00 18.43  ? 5580 HOH A O     1 
HETATM 24113 O  O     . HOH H 5 .    ? 82.810  87.480  136.031 1.00 3.57   ? 5581 HOH A O     1 
HETATM 24114 O  O     . HOH H 5 .    ? 47.075  95.137  121.207 1.00 6.63   ? 5582 HOH A O     1 
HETATM 24115 O  O     . HOH H 5 .    ? 73.282  84.817  58.605  1.00 17.62  ? 5583 HOH A O     1 
HETATM 24116 O  O     . HOH H 5 .    ? 73.045  100.936 120.606 1.00 10.65  ? 5584 HOH A O     1 
HETATM 24117 O  O     . HOH H 5 .    ? 53.033  112.039 70.304  1.00 22.11  ? 5585 HOH A O     1 
HETATM 24118 O  O     . HOH H 5 .    ? 103.904 107.031 125.038 1.00 11.29  ? 5586 HOH A O     1 
HETATM 24119 O  O     . HOH H 5 .    ? 131.157 102.345 80.707  1.00 19.19  ? 5587 HOH A O     1 
HETATM 24120 O  O     . HOH H 5 .    ? 61.036  63.493  114.759 1.00 14.48  ? 5588 HOH A O     1 
HETATM 24121 O  O     . HOH H 5 .    ? 99.051  88.249  136.219 1.00 21.40  ? 5589 HOH A O     1 
HETATM 24122 O  O     . HOH H 5 .    ? 117.761 105.966 107.847 1.00 11.96  ? 5590 HOH A O     1 
HETATM 24123 O  O     . HOH H 5 .    ? 95.182  87.805  110.980 1.00 7.56   ? 5591 HOH A O     1 
HETATM 24124 O  O     . HOH H 5 .    ? 73.199  88.604  116.139 1.00 13.46  ? 5592 HOH A O     1 
HETATM 24125 O  O     . HOH H 5 .    ? 57.367  127.846 111.982 1.00 33.58  ? 5593 HOH A O     1 
HETATM 24126 O  O     . HOH H 5 .    ? 64.059  99.437  79.040  1.00 17.93  ? 5594 HOH A O     1 
HETATM 24127 O  O     . HOH H 5 .    ? 119.744 83.006  53.287  1.00 21.68  ? 5595 HOH A O     1 
HETATM 24128 O  O     . HOH H 5 .    ? 54.390  133.706 99.291  1.00 38.01  ? 5596 HOH A O     1 
HETATM 24129 O  O     . HOH H 5 .    ? 122.297 88.192  73.594  1.00 8.50   ? 5597 HOH A O     1 
HETATM 24130 O  O     . HOH H 5 .    ? 109.012 101.505 144.494 1.00 13.27  ? 5598 HOH A O     1 
HETATM 24131 O  O     . HOH H 5 .    ? 145.644 96.943  107.459 1.00 13.33  ? 5599 HOH A O     1 
HETATM 24132 O  O     . HOH H 5 .    ? 137.334 99.710  139.903 1.00 34.75  ? 5600 HOH A O     1 
HETATM 24133 O  O     . HOH H 5 .    ? 94.015  97.194  119.107 1.00 7.06   ? 5601 HOH A O     1 
HETATM 24134 O  O     . HOH H 5 .    ? 65.312  83.337  92.674  1.00 17.08  ? 5602 HOH A O     1 
HETATM 24135 O  O     . HOH H 5 .    ? 74.890  116.177 137.690 1.00 26.15  ? 5603 HOH A O     1 
HETATM 24136 O  O     . HOH H 5 .    ? 111.182 98.370  125.340 1.00 5.27   ? 5604 HOH A O     1 
HETATM 24137 O  O     . HOH H 5 .    ? 112.805 83.242  75.542  1.00 13.57  ? 5605 HOH A O     1 
HETATM 24138 O  O     . HOH H 5 .    ? 103.153 110.666 134.235 1.00 14.95  ? 5606 HOH A O     1 
HETATM 24139 O  O     . HOH H 5 .    ? 74.160  91.306  70.641  1.00 6.52   ? 5607 HOH A O     1 
HETATM 24140 O  O     . HOH H 5 .    ? 90.790  105.049 143.636 1.00 17.47  ? 5608 HOH A O     1 
HETATM 24141 O  O     . HOH H 5 .    ? 58.525  103.378 142.647 1.00 31.72  ? 5609 HOH A O     1 
HETATM 24142 O  O     . HOH H 5 .    ? 64.905  83.431  89.568  1.00 23.75  ? 5610 HOH A O     1 
HETATM 24143 O  O     . HOH H 5 .    ? 132.152 92.929  81.625  1.00 7.10   ? 5611 HOH A O     1 
HETATM 24144 O  O     . HOH H 5 .    ? 79.515  59.544  128.080 1.00 20.53  ? 5612 HOH A O     1 
HETATM 24145 O  O     . HOH H 5 .    ? 86.287  80.527  110.939 1.00 11.35  ? 5613 HOH A O     1 
HETATM 24146 O  O     . HOH H 5 .    ? 29.160  98.720  127.108 1.00 37.78  ? 5614 HOH A O     1 
HETATM 24147 O  O     . HOH H 5 .    ? 115.928 76.945  130.744 1.00 25.79  ? 5615 HOH A O     1 
HETATM 24148 O  O     . HOH H 5 .    ? 77.792  89.668  68.517  1.00 5.51   ? 5616 HOH A O     1 
HETATM 24149 O  O     . HOH H 5 .    ? 117.521 103.249 101.022 1.00 26.23  ? 5617 HOH A O     1 
HETATM 24150 O  O     . HOH H 5 .    ? 71.229  132.171 101.734 1.00 32.21  ? 5618 HOH A O     1 
HETATM 24151 O  O     . HOH H 5 .    ? 69.068  57.453  117.704 1.00 25.81  ? 5619 HOH A O     1 
HETATM 24152 O  O     . HOH H 5 .    ? 57.613  58.656  118.271 1.00 11.78  ? 5620 HOH A O     1 
HETATM 24153 O  O     . HOH H 5 .    ? 81.888  91.375  100.085 1.00 19.96  ? 5621 HOH A O     1 
HETATM 24154 O  O     . HOH H 5 .    ? 123.534 71.544  82.288  1.00 8.47   ? 5622 HOH A O     1 
HETATM 24155 O  O     . HOH H 5 .    ? 112.385 100.159 100.073 1.00 20.06  ? 5623 HOH A O     1 
HETATM 24156 O  O     . HOH H 5 .    ? 84.274  78.188  109.462 1.00 13.48  ? 5624 HOH A O     1 
HETATM 24157 O  O     . HOH H 5 .    ? 118.387 86.318  107.607 1.00 16.52  ? 5625 HOH A O     1 
HETATM 24158 O  O     . HOH H 5 .    ? 83.350  84.500  70.764  1.00 13.20  ? 5626 HOH A O     1 
HETATM 24159 O  O     . HOH H 5 .    ? 59.704  68.806  95.320  1.00 34.36  ? 5627 HOH A O     1 
HETATM 24160 O  O     . HOH H 5 .    ? 62.095  108.752 77.590  1.00 25.31  ? 5628 HOH A O     1 
HETATM 24161 O  O     . HOH H 5 .    ? 115.447 69.328  112.803 1.00 17.53  ? 5629 HOH A O     1 
HETATM 24162 O  O     . HOH H 5 .    ? 92.933  64.085  128.133 1.00 21.02  ? 5630 HOH A O     1 
HETATM 24163 O  O     . HOH H 5 .    ? 75.582  84.223  129.844 1.00 7.00   ? 5631 HOH A O     1 
HETATM 24164 O  O     . HOH H 5 .    ? 100.858 95.930  103.112 1.00 10.79  ? 5632 HOH A O     1 
HETATM 24165 O  O     . HOH H 5 .    ? 50.551  86.098  91.428  1.00 50.21  ? 5633 HOH A O     1 
HETATM 24166 O  O     . HOH H 5 .    ? 112.986 95.919  138.086 1.00 7.80   ? 5634 HOH A O     1 
HETATM 24167 O  O     . HOH H 5 .    ? 124.366 75.070  79.596  1.00 9.60   ? 5635 HOH A O     1 
HETATM 24168 O  O     . HOH H 5 .    ? 83.506  94.014  77.763  1.00 17.80  ? 5636 HOH A O     1 
HETATM 24169 O  O     . HOH H 5 .    ? 48.169  106.823 101.649 1.00 13.08  ? 5637 HOH A O     1 
HETATM 24170 O  O     . HOH H 5 .    ? 115.637 80.130  74.797  1.00 19.55  ? 5638 HOH A O     1 
HETATM 24171 O  O     . HOH H 5 .    ? 119.374 93.454  76.039  1.00 8.05   ? 5639 HOH A O     1 
HETATM 24172 O  O     . HOH H 5 .    ? 110.630 72.800  109.773 1.00 10.34  ? 5640 HOH A O     1 
HETATM 24173 O  O     . HOH H 5 .    ? 130.293 64.537  94.318  1.00 22.79  ? 5641 HOH A O     1 
HETATM 24174 O  O     . HOH H 5 .    ? 104.193 103.516 126.135 1.00 7.73   ? 5642 HOH A O     1 
HETATM 24175 O  O     . HOH H 5 .    ? 61.753  124.822 90.388  1.00 17.47  ? 5643 HOH A O     1 
HETATM 24176 O  O     . HOH H 5 .    ? 90.080  98.285  134.990 1.00 16.38  ? 5644 HOH A O     1 
HETATM 24177 O  O     . HOH H 5 .    ? 129.806 89.458  50.949  1.00 27.14  ? 5645 HOH A O     1 
HETATM 24178 O  O     . HOH H 5 .    ? 40.697  79.397  115.698 1.00 12.78  ? 5646 HOH A O     1 
HETATM 24179 O  O     . HOH H 5 .    ? 94.192  82.388  134.561 1.00 2.97   ? 5647 HOH A O     1 
HETATM 24180 O  O     . HOH H 5 .    ? 81.961  103.091 59.352  1.00 13.14  ? 5648 HOH A O     1 
HETATM 24181 O  O     . HOH H 5 .    ? 89.024  73.216  134.833 1.00 18.04  ? 5649 HOH A O     1 
HETATM 24182 O  O     . HOH H 5 .    ? 97.014  94.609  119.115 1.00 10.82  ? 5650 HOH A O     1 
HETATM 24183 O  O     . HOH H 5 .    ? 57.020  121.489 79.456  1.00 27.55  ? 5651 HOH A O     1 
HETATM 24184 O  O     . HOH H 5 .    ? 125.557 109.059 107.309 1.00 25.37  ? 5652 HOH A O     1 
HETATM 24185 O  O     . HOH H 5 .    ? 77.359  92.433  126.929 1.00 10.13  ? 5653 HOH A O     1 
HETATM 24186 O  O     . HOH H 5 .    ? 64.038  80.538  126.074 1.00 18.67  ? 5654 HOH A O     1 
HETATM 24187 O  O     . HOH H 5 .    ? 107.168 75.979  104.848 1.00 28.37  ? 5655 HOH A O     1 
HETATM 24188 O  O     . HOH H 5 .    ? 71.584  52.896  121.641 1.00 36.35  ? 5656 HOH A O     1 
HETATM 24189 O  O     . HOH H 5 .    ? 61.055  97.264  87.491  1.00 14.22  ? 5657 HOH A O     1 
HETATM 24190 O  O     . HOH H 5 .    ? 75.627  121.709 98.480  1.00 21.86  ? 5658 HOH A O     1 
HETATM 24191 O  O     . HOH H 5 .    ? 67.245  77.396  124.134 1.00 21.68  ? 5659 HOH A O     1 
HETATM 24192 O  O     . HOH H 5 .    ? 122.200 75.750  108.515 1.00 20.16  ? 5660 HOH A O     1 
HETATM 24193 O  O     . HOH H 5 .    ? 71.659  109.100 121.036 1.00 22.18  ? 5661 HOH A O     1 
HETATM 24194 O  O     . HOH H 5 .    ? 70.431  72.480  97.554  1.00 14.22  ? 5662 HOH A O     1 
HETATM 24195 O  O     . HOH H 5 .    ? 57.872  114.930 100.829 1.00 18.26  ? 5663 HOH A O     1 
HETATM 24196 O  O     . HOH H 5 .    ? 114.571 94.559  132.414 1.00 10.04  ? 5664 HOH A O     1 
HETATM 24197 O  O     . HOH H 5 .    ? 90.684  89.347  110.658 1.00 10.82  ? 5665 HOH A O     1 
HETATM 24198 O  O     . HOH H 5 .    ? 52.842  84.782  124.985 1.00 3.87   ? 5666 HOH A O     1 
HETATM 24199 O  O     . HOH H 5 .    ? 85.307  98.592  75.463  1.00 17.32  ? 5667 HOH A O     1 
HETATM 24200 O  O     . HOH H 5 .    ? 85.263  70.217  129.194 1.00 8.92   ? 5668 HOH A O     1 
HETATM 24201 O  O     . HOH H 5 .    ? 65.145  80.442  122.639 1.00 15.73  ? 5669 HOH A O     1 
HETATM 24202 O  O     . HOH H 5 .    ? 113.568 118.141 117.808 1.00 27.71  ? 5670 HOH A O     1 
HETATM 24203 O  O     . HOH H 5 .    ? 63.523  111.499 108.480 1.00 44.25  ? 5671 HOH A O     1 
HETATM 24204 O  O     . HOH H 5 .    ? 93.688  76.679  124.929 1.00 11.17  ? 5672 HOH A O     1 
HETATM 24205 O  O     . HOH H 5 .    ? 92.223  81.857  64.896  1.00 15.54  ? 5673 HOH A O     1 
HETATM 24206 O  O     . HOH H 5 .    ? 100.253 93.478  132.516 1.00 8.39   ? 5674 HOH A O     1 
HETATM 24207 O  O     . HOH H 5 .    ? 119.874 104.607 56.329  1.00 13.80  ? 5675 HOH A O     1 
HETATM 24208 O  O     . HOH H 5 .    ? 77.843  116.302 117.622 1.00 30.47  ? 5676 HOH A O     1 
HETATM 24209 O  O     . HOH H 5 .    ? 108.925 68.866  118.768 1.00 9.84   ? 5677 HOH A O     1 
HETATM 24210 O  O     . HOH H 5 .    ? 81.031  96.034  108.788 1.00 25.25  ? 5678 HOH A O     1 
HETATM 24211 O  O     . HOH H 5 .    ? 39.752  98.979  103.505 1.00 9.82   ? 5679 HOH A O     1 
HETATM 24212 O  O     . HOH H 5 .    ? 135.826 81.464  84.481  1.00 15.21  ? 5680 HOH A O     1 
HETATM 24213 O  O     . HOH H 5 .    ? 53.731  97.668  124.514 1.00 5.93   ? 5681 HOH A O     1 
HETATM 24214 O  O     . HOH H 5 .    ? 104.547 100.850 102.920 1.00 16.17  ? 5682 HOH A O     1 
HETATM 24215 O  O     . HOH H 5 .    ? 120.435 81.431  40.090  1.00 35.34  ? 5683 HOH A O     1 
HETATM 24216 O  O     . HOH H 5 .    ? 104.905 68.122  57.817  1.00 22.61  ? 5684 HOH A O     1 
HETATM 24217 O  O     . HOH H 5 .    ? 67.854  128.798 90.089  1.00 30.62  ? 5685 HOH A O     1 
HETATM 24218 O  O     . HOH H 5 .    ? 34.762  106.728 85.157  1.00 38.15  ? 5686 HOH A O     1 
HETATM 24219 O  O     . HOH H 5 .    ? 61.804  93.711  91.822  1.00 13.58  ? 5687 HOH A O     1 
HETATM 24220 O  O     . HOH H 5 .    ? 124.342 57.557  104.212 1.00 23.79  ? 5688 HOH A O     1 
HETATM 24221 O  O     . HOH H 5 .    ? 35.309  104.253 100.494 1.00 24.24  ? 5689 HOH A O     1 
HETATM 24222 O  O     . HOH H 5 .    ? 119.200 74.338  129.202 1.00 22.45  ? 5690 HOH A O     1 
HETATM 24223 O  O     . HOH H 5 .    ? 88.430  77.855  68.793  1.00 22.73  ? 5691 HOH A O     1 
HETATM 24224 O  O     . HOH H 5 .    ? 79.546  83.196  114.196 1.00 6.97   ? 5692 HOH A O     1 
HETATM 24225 O  O     . HOH H 5 .    ? 94.824  100.204 107.254 1.00 23.85  ? 5693 HOH A O     1 
HETATM 24226 O  O     . HOH H 5 .    ? 92.590  67.406  70.451  1.00 28.64  ? 5694 HOH A O     1 
HETATM 24227 O  O     . HOH H 5 .    ? 65.785  100.306 97.757  1.00 12.41  ? 5695 HOH A O     1 
HETATM 24228 O  O     . HOH H 5 .    ? 63.929  128.186 93.991  1.00 29.39  ? 5696 HOH A O     1 
HETATM 24229 O  O     . HOH H 5 .    ? 122.975 119.964 119.834 1.00 25.26  ? 5697 HOH A O     1 
HETATM 24230 O  O     . HOH H 5 .    ? 74.487  55.744  129.900 1.00 25.38  ? 5698 HOH A O     1 
HETATM 24231 O  O     . HOH H 5 .    ? 56.363  94.710  84.006  1.00 23.64  ? 5699 HOH A O     1 
HETATM 24232 O  O     . HOH H 5 .    ? 57.985  131.222 75.591  1.00 40.54  ? 5700 HOH A O     1 
HETATM 24233 O  O     . HOH H 5 .    ? 60.906  100.725 117.846 1.00 7.11   ? 5701 HOH A O     1 
HETATM 24234 O  O     . HOH H 5 .    ? 124.236 87.649  48.506  1.00 26.18  ? 5702 HOH A O     1 
HETATM 24235 O  O     . HOH H 5 .    ? 94.056  78.559  108.276 1.00 17.26  ? 5703 HOH A O     1 
HETATM 24236 O  O     . HOH H 5 .    ? 85.408  96.206  47.673  1.00 15.99  ? 5704 HOH A O     1 
HETATM 24237 O  O     . HOH H 5 .    ? 96.903  99.249  106.201 1.00 22.72  ? 5705 HOH A O     1 
HETATM 24238 O  O     . HOH H 5 .    ? 52.910  73.323  115.284 1.00 7.03   ? 5706 HOH A O     1 
HETATM 24239 O  O     . HOH H 5 .    ? 75.156  97.418  86.023  1.00 18.30  ? 5707 HOH A O     1 
HETATM 24240 O  O     . HOH H 5 .    ? 36.522  102.216 108.326 1.00 28.27  ? 5708 HOH A O     1 
HETATM 24241 O  O     . HOH H 5 .    ? 62.317  99.672  57.422  1.00 24.76  ? 5709 HOH A O     1 
HETATM 24242 O  O     . HOH H 5 .    ? 42.075  98.392  139.067 1.00 20.91  ? 5710 HOH A O     1 
HETATM 24243 O  O     . HOH H 5 .    ? 139.004 104.862 75.268  1.00 39.08  ? 5711 HOH A O     1 
HETATM 24244 O  O     . HOH H 5 .    ? 143.183 110.140 102.648 1.00 25.65  ? 5712 HOH A O     1 
HETATM 24245 O  O     . HOH H 5 .    ? 97.643  88.609  122.896 1.00 5.98   ? 5713 HOH A O     1 
HETATM 24246 O  O     . HOH H 5 .    ? 130.735 79.563  94.245  1.00 19.36  ? 5714 HOH A O     1 
HETATM 24247 O  O     . HOH H 5 .    ? 77.810  78.955  134.545 1.00 6.35   ? 5715 HOH A O     1 
HETATM 24248 O  O     . HOH H 5 .    ? 85.725  78.373  141.797 1.00 18.72  ? 5716 HOH A O     1 
HETATM 24249 O  O     . HOH H 5 .    ? 134.567 87.442  84.207  1.00 4.70   ? 5717 HOH A O     1 
HETATM 24250 O  O     . HOH H 5 .    ? 86.333  108.032 135.001 1.00 18.49  ? 5718 HOH A O     1 
HETATM 24251 O  O     . HOH H 5 .    ? 102.518 81.632  39.420  1.00 27.48  ? 5719 HOH A O     1 
HETATM 24252 O  O     . HOH H 5 .    ? 67.370  80.825  92.243  1.00 15.84  ? 5720 HOH A O     1 
HETATM 24253 O  O     . HOH H 5 .    ? 29.255  96.933  96.151  1.00 46.02  ? 5721 HOH A O     1 
HETATM 24254 O  O     . HOH H 5 .    ? 81.355  84.644  141.478 1.00 17.75  ? 5722 HOH A O     1 
HETATM 24255 O  O     . HOH H 5 .    ? 70.410  77.146  122.556 1.00 22.45  ? 5723 HOH A O     1 
HETATM 24256 O  O     . HOH H 5 .    ? 90.072  71.126  116.720 1.00 19.33  ? 5724 HOH A O     1 
HETATM 24257 O  O     . HOH H 5 .    ? 53.474  118.075 79.541  1.00 34.99  ? 5725 HOH A O     1 
HETATM 24258 O  O     . HOH H 5 .    ? 66.140  136.805 74.958  1.00 45.86  ? 5726 HOH A O     1 
HETATM 24259 O  O     . HOH H 5 .    ? 83.015  65.615  133.971 1.00 19.01  ? 5727 HOH A O     1 
HETATM 24260 O  O     . HOH H 5 .    ? 116.484 93.324  131.538 1.00 12.73  ? 5728 HOH A O     1 
HETATM 24261 O  O     . HOH H 5 .    ? 108.376 98.911  135.784 1.00 10.60  ? 5729 HOH A O     1 
HETATM 24262 O  O     . HOH H 5 .    ? 70.022  104.342 79.416  1.00 12.75  ? 5730 HOH A O     1 
HETATM 24263 O  O     . HOH H 5 .    ? 102.179 95.524  68.151  1.00 22.71  ? 5731 HOH A O     1 
HETATM 24264 O  O     . HOH H 5 .    ? 93.802  97.780  64.898  1.00 25.86  ? 5732 HOH A O     1 
HETATM 24265 O  O     . HOH H 5 .    ? 98.727  95.674  117.997 1.00 20.90  ? 5733 HOH A O     1 
HETATM 24266 O  O     . HOH H 5 .    ? 93.246  90.160  108.360 1.00 15.73  ? 5734 HOH A O     1 
HETATM 24267 O  O     . HOH H 5 .    ? 57.996  53.082  133.615 1.00 29.17  ? 5735 HOH A O     1 
HETATM 24268 O  O     . HOH H 5 .    ? 51.584  92.133  100.893 1.00 11.63  ? 5736 HOH A O     1 
HETATM 24269 O  O     . HOH H 5 .    ? 103.567 81.331  128.692 1.00 8.62   ? 5737 HOH A O     1 
HETATM 24270 O  O     . HOH H 5 .    ? 64.064  68.448  135.954 1.00 17.68  ? 5738 HOH A O     1 
HETATM 24271 O  O     . HOH H 5 .    ? 131.629 78.656  91.104  1.00 13.64  ? 5739 HOH A O     1 
HETATM 24272 O  O     . HOH H 5 .    ? 114.190 90.663  128.833 1.00 12.53  ? 5740 HOH A O     1 
HETATM 24273 O  O     . HOH H 5 .    ? 118.153 65.469  93.600  1.00 7.92   ? 5741 HOH A O     1 
HETATM 24274 O  O     . HOH H 5 .    ? 54.427  88.901  94.413  1.00 17.75  ? 5742 HOH A O     1 
HETATM 24275 O  O     . HOH H 5 .    ? 72.905  99.754  46.066  1.00 17.93  ? 5743 HOH A O     1 
HETATM 24276 O  O     . HOH H 5 .    ? 30.368  98.261  130.659 1.00 44.30  ? 5744 HOH A O     1 
HETATM 24277 O  O     . HOH H 5 .    ? 144.282 106.677 106.816 1.00 22.66  ? 5745 HOH A O     1 
HETATM 24278 O  O     . HOH H 5 .    ? 150.365 107.950 100.909 1.00 29.62  ? 5746 HOH A O     1 
HETATM 24279 O  O     . HOH H 5 .    ? 108.911 72.006  78.473  1.00 24.07  ? 5747 HOH A O     1 
HETATM 24280 O  O     . HOH H 5 .    ? 69.441  86.098  62.976  1.00 31.02  ? 5748 HOH A O     1 
HETATM 24281 O  O     . HOH H 5 .    ? 72.751  93.960  70.483  1.00 6.54   ? 5749 HOH A O     1 
HETATM 24282 O  O     . HOH H 5 .    ? 126.537 79.571  119.814 1.00 29.15  ? 5750 HOH A O     1 
HETATM 24283 O  O     . HOH H 5 .    ? 69.161  104.276 114.646 1.00 22.54  ? 5751 HOH A O     1 
HETATM 24284 O  O     . HOH H 5 .    ? 43.432  91.806  128.009 1.00 6.16   ? 5752 HOH A O     1 
HETATM 24285 O  O     . HOH H 5 .    ? 77.254  120.874 52.764  1.00 38.81  ? 5753 HOH A O     1 
HETATM 24286 O  O     . HOH H 5 .    ? 143.843 112.168 96.983  1.00 21.73  ? 5754 HOH A O     1 
HETATM 24287 O  O     . HOH H 5 .    ? 76.493  100.529 82.687  1.00 12.28  ? 5755 HOH A O     1 
HETATM 24288 O  O     . HOH H 5 .    ? 58.087  135.386 111.916 1.00 40.25  ? 5756 HOH A O     1 
HETATM 24289 O  O     . HOH H 5 .    ? 102.266 94.145  131.514 1.00 11.79  ? 5757 HOH A O     1 
HETATM 24290 O  O     . HOH H 5 .    ? 130.208 111.477 117.731 1.00 27.63  ? 5758 HOH A O     1 
HETATM 24291 O  O     . HOH H 5 .    ? 111.306 106.672 109.581 1.00 12.17  ? 5759 HOH A O     1 
HETATM 24292 O  O     . HOH H 5 .    ? 62.382  95.365  88.617  1.00 15.40  ? 5760 HOH A O     1 
HETATM 24293 O  O     . HOH H 5 .    ? 96.393  91.014  109.883 1.00 8.37   ? 5761 HOH A O     1 
HETATM 24294 O  O     . HOH H 5 .    ? 76.362  86.772  134.161 1.00 12.22  ? 5762 HOH A O     1 
HETATM 24295 O  O     . HOH H 5 .    ? 124.919 113.091 123.791 1.00 14.72  ? 5763 HOH A O     1 
HETATM 24296 O  O     . HOH H 5 .    ? 113.386 85.825  125.631 1.00 13.57  ? 5764 HOH A O     1 
HETATM 24297 O  O     . HOH H 5 .    ? 127.712 70.547  87.643  1.00 12.93  ? 5765 HOH A O     1 
HETATM 24298 O  O     . HOH H 5 .    ? 131.819 97.993  77.986  1.00 18.32  ? 5766 HOH A O     1 
HETATM 24299 O  O     . HOH H 5 .    ? 125.013 87.804  94.316  1.00 4.25   ? 5767 HOH A O     1 
HETATM 24300 O  O     . HOH H 5 .    ? 85.732  46.607  137.001 1.00 37.25  ? 5768 HOH A O     1 
HETATM 24301 O  O     . HOH H 5 .    ? 133.454 113.396 137.408 1.00 22.74  ? 5769 HOH A O     1 
HETATM 24302 O  O     . HOH H 5 .    ? 90.873  79.911  70.143  1.00 17.30  ? 5770 HOH A O     1 
HETATM 24303 O  O     . HOH H 5 .    ? 126.126 114.816 89.375  1.00 24.63  ? 5771 HOH A O     1 
HETATM 24304 O  O     . HOH H 5 .    ? 98.729  103.272 121.310 1.00 16.91  ? 5772 HOH A O     1 
HETATM 24305 O  O     . HOH H 5 .    ? 63.247  107.270 55.431  1.00 24.54  ? 5773 HOH A O     1 
HETATM 24306 O  O     . HOH H 5 .    ? 125.636 116.062 123.719 1.00 17.52  ? 5774 HOH A O     1 
HETATM 24307 O  O     . HOH H 5 .    ? 81.816  84.891  136.303 1.00 6.87   ? 5775 HOH A O     1 
HETATM 24308 O  O     . HOH H 5 .    ? 74.137  127.967 75.296  1.00 36.13  ? 5776 HOH A O     1 
HETATM 24309 O  O     . HOH H 5 .    ? 115.994 104.993 121.847 1.00 7.95   ? 5777 HOH A O     1 
HETATM 24310 O  O     . HOH H 5 .    ? 60.777  106.378 69.659  1.00 26.27  ? 5778 HOH A O     1 
HETATM 24311 O  O     . HOH H 5 .    ? 103.126 92.269  75.203  1.00 23.32  ? 5779 HOH A O     1 
HETATM 24312 O  O     . HOH H 5 .    ? 116.142 104.710 148.638 1.00 13.62  ? 5780 HOH A O     1 
HETATM 24313 O  O     . HOH H 5 .    ? 116.351 94.848  98.962  1.00 18.80  ? 5781 HOH A O     1 
HETATM 24314 O  O     . HOH H 5 .    ? 104.966 104.045 106.126 1.00 16.16  ? 5782 HOH A O     1 
HETATM 24315 O  O     . HOH H 5 .    ? 96.807  87.654  136.718 1.00 15.86  ? 5783 HOH A O     1 
HETATM 24316 O  O     . HOH H 5 .    ? 81.491  96.313  47.008  1.00 15.87  ? 5784 HOH A O     1 
HETATM 24317 O  O     . HOH H 5 .    ? 113.804 81.585  38.161  1.00 38.38  ? 5785 HOH A O     1 
HETATM 24318 O  O     . HOH H 5 .    ? 65.633  55.744  131.028 1.00 35.40  ? 5786 HOH A O     1 
HETATM 24319 O  O     . HOH H 5 .    ? 80.123  102.593 123.771 1.00 14.06  ? 5787 HOH A O     1 
HETATM 24320 O  O     . HOH H 5 .    ? 56.228  75.723  116.720 1.00 6.30   ? 5788 HOH A O     1 
HETATM 24321 O  O     . HOH H 5 .    ? 99.305  68.527  118.736 1.00 18.89  ? 5789 HOH A O     1 
HETATM 24322 O  O     . HOH H 5 .    ? 118.075 79.090  76.337  1.00 12.96  ? 5790 HOH A O     1 
HETATM 24323 O  O     . HOH H 5 .    ? 96.346  91.860  116.898 1.00 11.70  ? 5791 HOH A O     1 
HETATM 24324 O  O     . HOH H 5 .    ? 67.231  72.617  117.596 1.00 16.33  ? 5792 HOH A O     1 
HETATM 24325 O  O     . HOH H 5 .    ? 42.615  103.831 114.025 1.00 19.01  ? 5793 HOH A O     1 
HETATM 24326 O  O     . HOH H 5 .    ? 109.029 82.846  126.953 1.00 11.43  ? 5794 HOH A O     1 
HETATM 24327 O  O     . HOH H 5 .    ? 113.717 80.941  129.165 1.00 6.14   ? 5795 HOH A O     1 
HETATM 24328 O  O     . HOH H 5 .    ? 89.856  98.473  52.959  1.00 21.84  ? 5796 HOH A O     1 
HETATM 24329 O  O     . HOH H 5 .    ? 86.285  99.231  109.230 1.00 12.71  ? 5797 HOH A O     1 
HETATM 24330 O  O     . HOH H 5 .    ? 71.462  90.440  90.388  1.00 19.85  ? 5798 HOH A O     1 
HETATM 24331 O  O     . HOH H 5 .    ? 56.504  88.608  121.346 1.00 5.89   ? 5799 HOH A O     1 
HETATM 24332 O  O     . HOH H 5 .    ? 62.600  93.669  69.196  1.00 42.95  ? 5800 HOH A O     1 
HETATM 24333 O  O     . HOH H 5 .    ? 89.515  71.330  119.546 1.00 18.06  ? 5801 HOH A O     1 
HETATM 24334 O  O     . HOH H 5 .    ? 58.490  96.769  87.417  1.00 11.60  ? 5802 HOH A O     1 
HETATM 24335 O  O     . HOH H 5 .    ? 92.025  95.333  113.377 1.00 10.75  ? 5803 HOH A O     1 
HETATM 24336 O  O     . HOH H 5 .    ? 116.683 62.666  66.234  1.00 27.96  ? 5804 HOH A O     1 
HETATM 24337 O  O     . HOH H 5 .    ? 60.724  106.656 56.352  1.00 32.03  ? 5805 HOH A O     1 
HETATM 24338 O  O     . HOH H 5 .    ? 119.811 88.168  131.933 1.00 22.59  ? 5806 HOH A O     1 
HETATM 24339 O  O     . HOH H 5 .    ? 90.990  110.756 128.594 1.00 11.02  ? 5807 HOH A O     1 
HETATM 24340 O  O     . HOH H 5 .    ? 90.688  107.077 131.348 1.00 4.51   ? 5808 HOH A O     1 
HETATM 24341 O  O     . HOH H 5 .    ? 72.053  83.750  66.551  1.00 20.37  ? 5809 HOH A O     1 
HETATM 24342 O  O     . HOH H 5 .    ? 137.722 104.516 113.788 1.00 20.64  ? 5810 HOH A O     1 
HETATM 24343 O  O     . HOH H 5 .    ? 118.550 69.472  85.549  1.00 17.41  ? 5811 HOH A O     1 
HETATM 24344 O  O     . HOH H 5 .    ? 87.963  85.088  140.265 1.00 5.79   ? 5812 HOH A O     1 
HETATM 24345 O  O     . HOH H 5 .    ? 147.810 113.884 85.820  1.00 45.57  ? 5813 HOH A O     1 
HETATM 24346 O  O     . HOH H 5 .    ? 46.722  70.706  134.935 1.00 22.02  ? 5814 HOH A O     1 
HETATM 24347 O  O     . HOH H 5 .    ? 76.446  89.731  135.878 1.00 14.67  ? 5815 HOH A O     1 
HETATM 24348 O  O     . HOH H 5 .    ? 128.967 64.347  96.997  1.00 18.88  ? 5816 HOH A O     1 
HETATM 24349 O  O     . HOH H 5 .    ? 49.904  118.718 104.660 1.00 32.64  ? 5817 HOH A O     1 
HETATM 24350 O  O     . HOH H 5 .    ? 39.885  71.932  124.099 1.00 27.39  ? 5818 HOH A O     1 
HETATM 24351 O  O     . HOH H 5 .    ? 135.768 106.080 115.085 1.00 15.61  ? 5819 HOH A O     1 
HETATM 24352 O  O     . HOH H 5 .    ? 69.729  117.565 75.456  1.00 11.06  ? 5820 HOH A O     1 
HETATM 24353 O  O     . HOH H 5 .    ? 75.187  90.848  130.545 1.00 10.77  ? 5821 HOH A O     1 
HETATM 24354 O  O     . HOH H 5 .    ? 112.958 88.221  123.116 1.00 5.99   ? 5822 HOH A O     1 
HETATM 24355 O  O     . HOH H 5 .    ? 109.535 97.552  97.928  1.00 24.60  ? 5823 HOH A O     1 
HETATM 24356 O  O     . HOH H 5 .    ? 114.138 110.861 48.616  1.00 21.83  ? 5824 HOH A O     1 
HETATM 24357 O  O     . HOH H 5 .    ? 126.710 107.687 111.158 1.00 15.42  ? 5825 HOH A O     1 
HETATM 24358 O  O     . HOH H 5 .    ? 124.548 99.530  126.719 1.00 14.46  ? 5826 HOH A O     1 
HETATM 24359 O  O     . HOH H 5 .    ? 57.477  98.474  77.539  1.00 21.72  ? 5827 HOH A O     1 
HETATM 24360 O  O     . HOH H 5 .    ? 92.753  99.733  58.877  1.00 14.18  ? 5828 HOH A O     1 
HETATM 24361 O  O     . HOH H 5 .    ? 130.974 99.515  127.943 1.00 24.52  ? 5829 HOH A O     1 
HETATM 24362 O  O     . HOH H 5 .    ? 96.105  83.659  119.423 1.00 3.88   ? 5830 HOH A O     1 
HETATM 24363 O  O     . HOH H 5 .    ? 131.456 99.439  66.715  1.00 41.63  ? 5831 HOH A O     1 
HETATM 24364 O  O     . HOH H 5 .    ? 39.733  110.692 79.657  1.00 22.33  ? 5832 HOH A O     1 
HETATM 24365 O  O     . HOH H 5 .    ? 108.195 109.954 117.674 1.00 17.72  ? 5833 HOH A O     1 
HETATM 24366 O  O     . HOH H 5 .    ? 115.676 113.794 144.261 1.00 29.14  ? 5834 HOH A O     1 
HETATM 24367 O  O     . HOH H 5 .    ? 73.040  118.293 139.764 1.00 38.75  ? 5835 HOH A O     1 
HETATM 24368 O  O     . HOH H 5 .    ? 79.581  111.488 121.584 1.00 19.27  ? 5836 HOH A O     1 
HETATM 24369 O  O     . HOH H 5 .    ? 34.476  89.856  113.317 1.00 46.28  ? 5837 HOH A O     1 
HETATM 24370 O  O     . HOH H 5 .    ? 96.017  95.192  65.795  1.00 17.50  ? 5838 HOH A O     1 
HETATM 24371 O  O     . HOH H 5 .    ? 75.322  100.529 112.033 1.00 19.69  ? 5839 HOH A O     1 
HETATM 24372 O  O     . HOH H 5 .    ? 81.987  63.018  113.610 1.00 35.19  ? 5840 HOH A O     1 
HETATM 24373 O  O     . HOH H 5 .    ? 101.062 100.609 146.476 1.00 14.78  ? 5841 HOH A O     1 
HETATM 24374 O  O     . HOH H 5 .    ? 74.012  74.001  93.296  1.00 27.17  ? 5842 HOH A O     1 
HETATM 24375 O  O     . HOH H 5 .    ? 110.535 78.305  60.604  1.00 15.84  ? 5843 HOH A O     1 
HETATM 24376 O  O     . HOH H 5 .    ? 95.578  87.951  150.057 1.00 28.93  ? 5844 HOH A O     1 
HETATM 24377 O  O     . HOH H 5 .    ? 79.800  94.575  64.388  1.00 17.14  ? 5845 HOH A O     1 
HETATM 24378 O  O     . HOH H 5 .    ? 86.441  87.884  151.463 1.00 29.23  ? 5846 HOH A O     1 
HETATM 24379 O  O     . HOH H 5 .    ? 105.108 91.117  129.133 1.00 16.87  ? 5847 HOH A O     1 
HETATM 24380 O  O     . HOH H 5 .    ? 56.902  68.775  115.107 1.00 25.77  ? 5848 HOH A O     1 
HETATM 24381 O  O     . HOH H 5 .    ? 142.474 79.759  76.924  1.00 16.62  ? 5849 HOH A O     1 
HETATM 24382 O  O     . HOH H 5 .    ? 82.207  126.729 103.964 1.00 39.30  ? 5850 HOH A O     1 
HETATM 24383 O  O     . HOH H 5 .    ? 111.035 110.240 51.499  1.00 22.58  ? 5851 HOH A O     1 
HETATM 24384 O  O     . HOH H 5 .    ? 72.569  53.905  124.371 1.00 27.31  ? 5852 HOH A O     1 
HETATM 24385 O  O     . HOH H 5 .    ? 71.377  83.088  128.544 1.00 29.29  ? 5853 HOH A O     1 
HETATM 24386 O  O     . HOH H 5 .    ? 58.011  84.496  127.119 1.00 19.52  ? 5854 HOH A O     1 
HETATM 24387 O  O     . HOH H 5 .    ? 121.253 84.849  51.884  1.00 30.20  ? 5855 HOH A O     1 
HETATM 24388 O  O     . HOH H 5 .    ? 82.212  82.098  114.582 1.00 7.94   ? 5856 HOH A O     1 
HETATM 24389 O  O     . HOH H 5 .    ? 67.564  78.073  90.268  1.00 14.26  ? 5857 HOH A O     1 
HETATM 24390 O  O     . HOH H 5 .    ? 84.489  80.948  64.162  1.00 30.89  ? 5858 HOH A O     1 
HETATM 24391 O  O     . HOH H 5 .    ? 49.299  90.945  88.250  1.00 33.04  ? 5859 HOH A O     1 
HETATM 24392 O  O     . HOH H 5 .    ? 118.429 104.586 77.986  1.00 25.73  ? 5860 HOH A O     1 
HETATM 24393 O  O     . HOH H 5 .    ? 44.190  97.780  73.645  1.00 34.94  ? 5861 HOH A O     1 
HETATM 24394 O  O     . HOH H 5 .    ? 77.453  108.573 132.926 1.00 28.79  ? 5862 HOH A O     1 
HETATM 24395 O  O     . HOH H 5 .    ? 58.399  94.932  138.050 1.00 18.97  ? 5863 HOH A O     1 
HETATM 24396 O  O     . HOH H 5 .    ? 130.119 108.871 91.247  1.00 15.27  ? 5864 HOH A O     1 
HETATM 24397 O  O     . HOH H 5 .    ? 68.747  119.851 96.492  1.00 22.37  ? 5865 HOH A O     1 
HETATM 24398 O  O     . HOH H 5 .    ? 83.899  78.901  144.820 1.00 22.47  ? 5866 HOH A O     1 
HETATM 24399 O  O     . HOH H 5 .    ? 76.056  70.111  103.801 1.00 18.69  ? 5867 HOH A O     1 
HETATM 24400 O  O     . HOH H 5 .    ? 63.396  95.935  92.361  1.00 15.15  ? 5868 HOH A O     1 
HETATM 24401 O  O     . HOH H 5 .    ? 72.425  123.709 53.971  1.00 31.39  ? 5869 HOH A O     1 
HETATM 24402 O  O     . HOH H 5 .    ? 119.182 97.490  95.730  1.00 27.24  ? 5870 HOH A O     1 
HETATM 24403 O  O     . HOH H 5 .    ? 98.296  90.823  108.070 1.00 13.22  ? 5871 HOH A O     1 
HETATM 24404 O  O     . HOH H 5 .    ? 36.271  80.423  125.074 1.00 28.44  ? 5872 HOH A O     1 
HETATM 24405 O  O     . HOH H 5 .    ? 86.061  86.163  70.849  1.00 15.60  ? 5873 HOH A O     1 
HETATM 24406 O  O     . HOH H 5 .    ? 123.388 94.575  92.580  1.00 8.04   ? 5874 HOH A O     1 
HETATM 24407 O  O     . HOH H 5 .    ? 76.544  132.044 104.618 1.00 26.90  ? 5875 HOH A O     1 
HETATM 24408 O  O     . HOH H 5 .    ? 110.322 93.019  126.464 1.00 12.63  ? 5876 HOH A O     1 
HETATM 24409 O  O     . HOH H 5 .    ? 57.922  123.634 80.159  1.00 26.15  ? 5877 HOH A O     1 
HETATM 24410 O  O     . HOH H 5 .    ? 118.620 105.840 67.426  1.00 24.74  ? 5878 HOH A O     1 
HETATM 24411 O  O     . HOH H 5 .    ? 105.672 85.764  59.057  1.00 12.48  ? 5879 HOH A O     1 
HETATM 24412 O  O     . HOH H 5 .    ? 107.148 104.903 113.143 1.00 15.00  ? 5880 HOH A O     1 
HETATM 24413 O  O     . HOH H 5 .    ? 112.587 87.228  79.139  1.00 12.93  ? 5881 HOH A O     1 
HETATM 24414 O  O     . HOH H 5 .    ? 103.478 105.378 99.425  1.00 36.48  ? 5882 HOH A O     1 
HETATM 24415 O  O     . HOH H 5 .    ? 136.728 82.231  66.601  1.00 24.05  ? 5883 HOH A O     1 
HETATM 24416 O  O     . HOH H 5 .    ? 80.848  43.551  130.219 1.00 25.77  ? 5884 HOH A O     1 
HETATM 24417 O  O     . HOH H 5 .    ? 74.150  64.922  80.600  1.00 29.01  ? 5885 HOH A O     1 
HETATM 24418 O  O     . HOH H 5 .    ? 59.549  110.130 66.069  1.00 22.59  ? 5886 HOH A O     1 
HETATM 24419 O  O     . HOH H 5 .    ? 118.452 73.924  80.282  1.00 22.75  ? 5887 HOH A O     1 
HETATM 24420 O  O     . HOH H 5 .    ? 99.772  104.926 55.442  1.00 25.63  ? 5888 HOH A O     1 
HETATM 24421 O  O     . HOH H 5 .    ? 68.328  109.548 85.078  1.00 22.62  ? 5889 HOH A O     1 
HETATM 24422 O  O     . HOH H 5 .    ? 37.922  91.394  112.651 1.00 29.18  ? 5890 HOH A O     1 
HETATM 24423 O  O     . HOH H 5 .    ? 61.853  71.418  95.264  1.00 16.54  ? 5891 HOH A O     1 
HETATM 24424 O  O     . HOH H 5 .    ? 71.256  73.009  93.484  1.00 25.95  ? 5892 HOH A O     1 
HETATM 24425 O  O     . HOH H 5 .    ? 69.394  66.937  102.329 1.00 19.60  ? 5893 HOH A O     1 
HETATM 24426 O  O     . HOH H 5 .    ? 81.659  104.968 63.670  1.00 20.98  ? 5894 HOH A O     1 
HETATM 24427 O  O     . HOH H 5 .    ? 110.183 105.461 141.802 1.00 15.45  ? 5895 HOH A O     1 
HETATM 24428 O  O     . HOH H 5 .    ? 106.131 82.940  46.167  1.00 26.22  ? 5896 HOH A O     1 
HETATM 24429 O  O     . HOH H 5 .    ? 132.831 115.304 119.099 1.00 39.15  ? 5897 HOH A O     1 
HETATM 24430 O  O     . HOH H 5 .    ? 84.032  101.504 76.535  1.00 12.10  ? 5898 HOH A O     1 
HETATM 24431 O  O     . HOH H 5 .    ? 90.123  105.370 117.008 1.00 13.71  ? 5899 HOH A O     1 
HETATM 24432 O  O     . HOH H 5 .    ? 102.470 93.026  98.708  1.00 23.95  ? 5900 HOH A O     1 
HETATM 24433 O  O     . HOH H 5 .    ? 121.701 93.959  76.179  1.00 14.00  ? 5901 HOH A O     1 
HETATM 24434 O  O     . HOH H 5 .    ? 101.994 103.581 123.284 1.00 19.70  ? 5902 HOH A O     1 
HETATM 24435 O  O     . HOH H 5 .    ? 78.193  46.253  117.482 1.00 29.35  ? 5903 HOH A O     1 
HETATM 24436 O  O     . HOH H 5 .    ? 88.661  109.210 131.788 1.00 12.60  ? 5904 HOH A O     1 
HETATM 24437 O  O     . HOH H 5 .    ? 58.199  100.362 143.383 1.00 31.57  ? 5905 HOH A O     1 
HETATM 24438 O  O     . HOH H 5 .    ? 51.794  72.806  133.987 1.00 6.52   ? 5906 HOH A O     1 
HETATM 24439 O  O     . HOH H 5 .    ? 132.913 97.600  81.440  1.00 17.26  ? 5907 HOH A O     1 
HETATM 24440 O  O     . HOH H 5 .    ? 80.065  122.079 69.486  1.00 39.84  ? 5908 HOH A O     1 
HETATM 24441 O  O     . HOH H 5 .    ? 99.814  65.501  66.436  1.00 19.39  ? 5909 HOH A O     1 
HETATM 24442 O  O     . HOH H 5 .    ? 73.674  83.006  42.849  1.00 33.69  ? 5910 HOH A O     1 
HETATM 24443 O  O     . HOH H 5 .    ? 116.442 99.493  76.960  1.00 20.17  ? 5911 HOH A O     1 
HETATM 24444 O  O     . HOH H 5 .    ? 140.885 96.950  75.993  1.00 32.33  ? 5912 HOH A O     1 
HETATM 24445 O  O     . HOH H 5 .    ? 96.459  103.668 120.847 1.00 13.10  ? 5913 HOH A O     1 
HETATM 24446 O  O     . HOH H 5 .    ? 111.904 109.365 111.240 1.00 18.38  ? 5914 HOH A O     1 
HETATM 24447 O  O     . HOH H 5 .    ? 37.503  106.296 99.292  1.00 16.14  ? 5915 HOH A O     1 
HETATM 24448 O  O     . HOH H 5 .    ? 128.925 73.692  65.999  1.00 26.84  ? 5916 HOH A O     1 
HETATM 24449 O  O     . HOH H 5 .    ? 117.022 103.966 103.927 1.00 20.03  ? 5917 HOH A O     1 
HETATM 24450 O  O     . HOH H 5 .    ? 121.405 75.208  111.081 1.00 24.80  ? 5918 HOH A O     1 
HETATM 24451 O  O     . HOH H 5 .    ? 87.969  78.616  45.341  1.00 29.58  ? 5919 HOH A O     1 
HETATM 24452 O  O     . HOH H 5 .    ? 56.610  123.149 85.730  1.00 14.53  ? 5920 HOH A O     1 
HETATM 24453 O  O     . HOH H 5 .    ? 84.999  112.320 73.127  1.00 27.65  ? 5921 HOH A O     1 
HETATM 24454 O  O     . HOH H 5 .    ? 70.653  89.843  86.687  1.00 22.89  ? 5922 HOH A O     1 
HETATM 24455 O  O     . HOH H 5 .    ? 76.208  104.102 143.338 1.00 30.91  ? 5923 HOH A O     1 
HETATM 24456 O  O     . HOH H 5 .    ? 107.598 98.377  128.424 1.00 9.94   ? 5924 HOH A O     1 
HETATM 24457 O  O     . HOH H 5 .    ? 138.525 102.271 99.972  1.00 9.02   ? 5925 HOH A O     1 
HETATM 24458 O  O     . HOH H 5 .    ? 56.253  127.472 75.594  1.00 41.91  ? 5926 HOH A O     1 
HETATM 24459 O  O     . HOH H 5 .    ? 81.809  61.578  139.239 1.00 32.61  ? 5927 HOH A O     1 
HETATM 24460 O  O     . HOH H 5 .    ? 95.605  82.150  128.476 1.00 2.28   ? 5928 HOH A O     1 
HETATM 24461 O  O     . HOH H 5 .    ? 121.705 120.754 137.879 1.00 37.45  ? 5929 HOH A O     1 
HETATM 24462 O  O     . HOH H 5 .    ? 77.736  93.549  111.556 1.00 18.71  ? 5930 HOH A O     1 
HETATM 24463 O  O     . HOH H 5 .    ? 101.898 88.863  130.143 1.00 18.81  ? 5931 HOH A O     1 
HETATM 24464 O  O     . HOH H 5 .    ? 130.808 80.091  66.606  1.00 16.50  ? 5932 HOH A O     1 
HETATM 24465 O  O     . HOH H 5 .    ? 79.376  101.899 111.967 1.00 19.90  ? 5933 HOH A O     1 
HETATM 24466 O  O     . HOH H 5 .    ? 118.134 121.212 137.140 1.00 36.76  ? 5934 HOH A O     1 
HETATM 24467 O  O     . HOH H 5 .    ? 133.260 114.952 95.385  1.00 43.36  ? 5935 HOH A O     1 
HETATM 24468 O  O     . HOH H 5 .    ? 105.965 82.014  75.962  1.00 19.96  ? 5936 HOH A O     1 
HETATM 24469 O  O     . HOH H 5 .    ? 97.808  97.679  54.080  1.00 13.55  ? 5937 HOH A O     1 
HETATM 24470 O  O     . HOH H 5 .    ? 69.455  111.602 106.905 1.00 32.37  ? 5938 HOH A O     1 
HETATM 24471 O  O     . HOH H 5 .    ? 35.425  109.090 122.692 1.00 25.98  ? 5939 HOH A O     1 
HETATM 24472 O  O     . HOH H 5 .    ? 52.750  104.864 126.194 1.00 31.85  ? 5940 HOH A O     1 
HETATM 24473 O  O     . HOH H 5 .    ? 155.350 96.816  88.133  1.00 33.12  ? 5941 HOH A O     1 
HETATM 24474 O  O     . HOH H 5 .    ? 53.267  78.278  105.254 1.00 23.19  ? 5942 HOH A O     1 
HETATM 24475 O  O     . HOH H 5 .    ? 85.696  66.434  137.327 1.00 25.11  ? 5943 HOH A O     1 
HETATM 24476 O  O     . HOH H 5 .    ? 68.978  84.374  125.225 1.00 27.93  ? 5944 HOH A O     1 
HETATM 24477 O  O     . HOH H 5 .    ? 150.882 98.260  105.664 1.00 29.50  ? 5945 HOH A O     1 
HETATM 24478 O  O     . HOH H 5 .    ? 120.576 94.197  45.026  1.00 27.84  ? 5946 HOH A O     1 
HETATM 24479 O  O     . HOH H 5 .    ? 51.093  115.969 88.183  1.00 23.31  ? 5947 HOH A O     1 
HETATM 24480 O  O     . HOH H 5 .    ? 93.138  111.955 130.700 1.00 20.71  ? 5948 HOH A O     1 
HETATM 24481 O  O     . HOH H 5 .    ? 60.951  114.066 97.036  1.00 9.20   ? 5949 HOH A O     1 
HETATM 24482 O  O     . HOH H 5 .    ? 129.317 62.292  107.353 1.00 34.26  ? 5950 HOH A O     1 
HETATM 24483 O  O     . HOH H 5 .    ? 64.899  122.835 93.087  1.00 18.19  ? 5951 HOH A O     1 
HETATM 24484 O  O     . HOH H 5 .    ? 105.529 65.542  131.553 1.00 27.21  ? 5952 HOH A O     1 
HETATM 24485 O  O     . HOH H 5 .    ? 144.075 97.753  78.624  1.00 17.54  ? 5953 HOH A O     1 
HETATM 24486 O  O     . HOH H 5 .    ? 132.418 109.773 110.212 1.00 12.50  ? 5954 HOH A O     1 
HETATM 24487 O  O     . HOH H 5 .    ? 52.901  99.994  123.401 1.00 6.45   ? 5955 HOH A O     1 
HETATM 24488 O  O     . HOH H 5 .    ? 82.342  101.329 79.324  1.00 13.49  ? 5956 HOH A O     1 
HETATM 24489 O  O     . HOH H 5 .    ? 93.859  85.297  143.877 1.00 26.34  ? 5957 HOH A O     1 
HETATM 24490 O  O     . HOH H 5 .    ? 114.116 71.716  105.617 1.00 15.10  ? 5958 HOH A O     1 
HETATM 24491 O  O     . HOH H 5 .    ? 59.959  127.300 62.272  1.00 42.13  ? 5959 HOH A O     1 
HETATM 24492 O  O     . HOH H 5 .    ? 99.356  92.365  74.881  1.00 32.74  ? 5960 HOH A O     1 
HETATM 24493 O  O     . HOH H 5 .    ? 144.987 104.012 103.784 1.00 11.90  ? 5961 HOH A O     1 
HETATM 24494 O  O     . HOH H 5 .    ? 153.903 101.920 89.466  1.00 18.44  ? 5962 HOH A O     1 
HETATM 24495 O  O     . HOH H 5 .    ? 89.255  64.505  125.303 1.00 30.76  ? 5963 HOH A O     1 
HETATM 24496 O  O     . HOH H 5 .    ? 61.284  115.224 58.909  1.00 29.37  ? 5964 HOH A O     1 
HETATM 24497 O  O     . HOH H 5 .    ? 75.465  88.307  93.638  1.00 17.45  ? 5965 HOH A O     1 
HETATM 24498 O  O     . HOH H 5 .    ? 42.066  111.239 78.473  1.00 20.57  ? 5966 HOH A O     1 
HETATM 24499 O  O     . HOH H 5 .    ? 122.506 105.823 68.334  1.00 35.03  ? 5967 HOH A O     1 
HETATM 24500 O  O     . HOH H 5 .    ? 106.482 115.658 126.008 1.00 26.01  ? 5968 HOH A O     1 
HETATM 24501 O  O     . HOH H 5 .    ? 38.683  89.161  107.803 1.00 28.51  ? 5969 HOH A O     1 
HETATM 24502 O  O     . HOH H 5 .    ? 52.261  99.822  109.797 1.00 7.34   ? 5970 HOH A O     1 
HETATM 24503 O  O     . HOH H 5 .    ? 35.808  101.058 101.649 1.00 19.58  ? 5971 HOH A O     1 
HETATM 24504 O  O     . HOH H 5 .    ? 93.391  42.361  132.657 1.00 40.74  ? 5972 HOH A O     1 
HETATM 24505 O  O     . HOH H 5 .    ? 133.322 71.288  99.515  1.00 27.79  ? 5973 HOH A O     1 
HETATM 24506 O  O     . HOH H 5 .    ? 78.631  108.066 119.540 1.00 19.30  ? 5974 HOH A O     1 
HETATM 24507 O  O     . HOH H 5 .    ? 100.502 93.979  114.268 1.00 4.71   ? 5975 HOH A O     1 
HETATM 24508 O  O     . HOH H 5 .    ? 40.688  86.709  98.467  1.00 23.65  ? 5976 HOH A O     1 
HETATM 24509 O  O     . HOH H 5 .    ? 79.276  119.392 107.654 1.00 41.31  ? 5977 HOH A O     1 
HETATM 24510 O  O     . HOH H 5 .    ? 122.400 107.689 114.795 1.00 7.39   ? 5978 HOH A O     1 
HETATM 24511 O  O     . HOH H 5 .    ? 79.202  106.507 61.452  1.00 10.26  ? 5979 HOH A O     1 
HETATM 24512 O  O     . HOH H 5 .    ? 95.192  108.668 126.108 1.00 18.43  ? 5980 HOH A O     1 
HETATM 24513 O  O     . HOH H 5 .    ? 76.634  134.631 105.385 1.00 33.69  ? 5981 HOH A O     1 
HETATM 24514 O  O     . HOH H 5 .    ? 59.703  88.581  44.012  1.00 57.37  ? 5982 HOH A O     1 
HETATM 24515 O  O     . HOH H 5 .    ? 59.914  124.497 60.992  1.00 25.92  ? 5983 HOH A O     1 
HETATM 24516 O  O     . HOH H 5 .    ? 59.551  113.045 59.547  1.00 27.56  ? 5984 HOH A O     1 
HETATM 24517 O  O     . HOH H 5 .    ? 34.143  103.467 86.003  1.00 27.76  ? 5985 HOH A O     1 
HETATM 24518 O  O     . HOH H 5 .    ? 105.492 77.197  53.793  1.00 20.39  ? 5986 HOH A O     1 
HETATM 24519 O  O     . HOH H 5 .    ? 123.092 86.229  128.580 1.00 23.16  ? 5987 HOH A O     1 
HETATM 24520 O  O     . HOH H 5 .    ? 63.656  112.982 81.490  1.00 26.22  ? 5988 HOH A O     1 
HETATM 24521 O  O     . HOH H 5 .    ? 59.075  96.388  145.956 1.00 35.17  ? 5989 HOH A O     1 
HETATM 24522 O  O     . HOH H 5 .    ? 82.043  80.221  101.052 1.00 33.65  ? 5990 HOH A O     1 
HETATM 24523 O  O     . HOH H 5 .    ? 135.972 78.372  85.353  1.00 27.69  ? 5991 HOH A O     1 
HETATM 24524 O  O     . HOH H 5 .    ? 143.506 87.644  89.367  1.00 24.38  ? 5992 HOH A O     1 
HETATM 24525 O  O     . HOH H 5 .    ? 79.511  85.755  136.880 1.00 5.39   ? 5993 HOH A O     1 
HETATM 24526 O  O     . HOH H 5 .    ? 99.468  98.129  147.894 1.00 22.17  ? 5994 HOH A O     1 
HETATM 24527 O  O     . HOH H 5 .    ? 121.432 108.394 146.050 1.00 25.99  ? 5995 HOH A O     1 
HETATM 24528 O  O     . HOH H 5 .    ? 95.002  95.680  152.171 1.00 23.30  ? 5996 HOH A O     1 
HETATM 24529 O  O     . HOH H 5 .    ? 122.734 61.197  108.853 1.00 26.21  ? 5997 HOH A O     1 
HETATM 24530 O  O     . HOH H 5 .    ? 37.543  81.772  123.170 1.00 22.75  ? 5998 HOH A O     1 
HETATM 24531 O  O     . HOH H 5 .    ? 123.252 94.682  98.239  1.00 18.00  ? 5999 HOH A O     1 
HETATM 24532 O  O     . HOH H 5 .    ? 60.376  91.403  129.169 1.00 21.63  ? 6000 HOH A O     1 
HETATM 24533 O  O     . HOH H 5 .    ? 40.917  84.673  126.481 1.00 18.74  ? 6001 HOH A O     1 
HETATM 24534 O  O     . HOH H 5 .    ? 56.929  89.856  95.052  1.00 15.47  ? 6002 HOH A O     1 
HETATM 24535 O  O     . HOH H 5 .    ? 141.743 95.238  78.327  1.00 15.23  ? 6003 HOH A O     1 
HETATM 24536 O  O     . HOH H 5 .    ? 110.624 81.047  129.797 1.00 15.65  ? 6004 HOH A O     1 
HETATM 24537 O  O     . HOH H 5 .    ? 46.647  87.239  95.554  1.00 11.38  ? 6005 HOH A O     1 
HETATM 24538 O  O     . HOH H 5 .    ? 104.000 101.119 73.322  1.00 23.13  ? 6006 HOH A O     1 
HETATM 24539 O  O     . HOH H 5 .    ? 50.753  101.151 114.858 1.00 15.28  ? 6007 HOH A O     1 
HETATM 24540 O  O     . HOH H 5 .    ? 62.666  108.245 64.529  1.00 17.72  ? 6008 HOH A O     1 
HETATM 24541 O  O     . HOH H 5 .    ? 115.471 97.760  100.437 1.00 23.86  ? 6009 HOH A O     1 
HETATM 24542 O  O     . HOH H 5 .    ? 48.558  82.707  143.960 1.00 16.61  ? 6010 HOH A O     1 
HETATM 24543 O  O     . HOH H 5 .    ? 123.114 95.304  46.750  1.00 29.63  ? 6011 HOH A O     1 
HETATM 24544 O  O     . HOH H 5 .    ? 114.275 89.278  103.237 1.00 14.56  ? 6012 HOH A O     1 
HETATM 24545 O  O     . HOH H 5 .    ? 142.733 114.483 95.214  1.00 20.10  ? 6013 HOH A O     1 
HETATM 24546 O  O     . HOH H 5 .    ? 54.945  81.090  105.506 1.00 13.42  ? 6014 HOH A O     1 
HETATM 24547 O  O     . HOH H 5 .    ? 120.412 72.062  81.120  1.00 20.41  ? 6015 HOH A O     1 
HETATM 24548 O  O     . HOH H 5 .    ? 113.848 65.572  95.613  1.00 16.17  ? 6016 HOH A O     1 
HETATM 24549 O  O     . HOH H 5 .    ? 50.674  82.029  99.273  1.00 21.79  ? 6017 HOH A O     1 
HETATM 24550 O  O     . HOH H 5 .    ? 78.587  85.526  67.164  1.00 17.92  ? 6018 HOH A O     1 
HETATM 24551 O  O     . HOH H 5 .    ? 113.156 108.157 108.096 1.00 14.69  ? 6019 HOH A O     1 
HETATM 24552 O  O     . HOH H 5 .    ? 114.958 72.229  127.521 1.00 25.59  ? 6020 HOH A O     1 
HETATM 24553 O  O     . HOH H 5 .    ? 129.320 94.156  63.433  1.00 16.34  ? 6021 HOH A O     1 
HETATM 24554 O  O     . HOH H 5 .    ? 66.407  91.059  100.928 1.00 11.93  ? 6022 HOH A O     1 
HETATM 24555 O  O     . HOH H 5 .    ? 89.233  93.047  49.261  1.00 21.99  ? 6023 HOH A O     1 
HETATM 24556 O  O     . HOH H 5 .    ? 51.297  104.438 131.340 1.00 21.96  ? 6024 HOH A O     1 
HETATM 24557 O  O     . HOH H 5 .    ? 79.643  87.851  125.030 1.00 12.19  ? 6025 HOH A O     1 
HETATM 24558 O  O     . HOH H 5 .    ? 100.234 79.934  53.962  1.00 11.94  ? 6026 HOH A O     1 
HETATM 24559 O  O     . HOH H 5 .    ? 115.276 78.560  78.268  1.00 15.06  ? 6027 HOH A O     1 
HETATM 24560 O  O     . HOH H 5 .    ? 61.489  112.649 56.690  1.00 32.24  ? 6028 HOH A O     1 
HETATM 24561 O  O     . HOH H 5 .    ? 134.620 111.291 120.892 1.00 28.28  ? 6029 HOH A O     1 
HETATM 24562 O  O     . HOH H 5 .    ? 146.181 112.328 95.839  1.00 17.97  ? 6030 HOH A O     1 
HETATM 24563 O  O     . HOH H 5 .    ? 128.355 102.556 130.236 1.00 8.78   ? 6031 HOH A O     1 
HETATM 24564 O  O     . HOH H 5 .    ? 103.708 96.450  73.707  1.00 27.79  ? 6032 HOH A O     1 
HETATM 24565 O  O     . HOH H 5 .    ? 130.130 70.707  89.873  1.00 18.77  ? 6033 HOH A O     1 
HETATM 24566 O  O     . HOH H 5 .    ? 123.812 105.664 113.944 1.00 5.71   ? 6034 HOH A O     1 
HETATM 24567 O  O     . HOH H 5 .    ? 62.884  110.025 56.159  1.00 32.81  ? 6035 HOH A O     1 
HETATM 24568 O  O     . HOH H 5 .    ? 86.029  74.755  77.864  1.00 40.14  ? 6036 HOH A O     1 
HETATM 24569 O  O     . HOH H 5 .    ? 59.248  120.224 76.840  1.00 28.09  ? 6037 HOH A O     1 
HETATM 24570 O  O     . HOH H 5 .    ? 120.940 96.928  92.352  1.00 16.34  ? 6038 HOH A O     1 
HETATM 24571 O  O     . HOH H 5 .    ? 132.781 73.216  79.127  1.00 18.79  ? 6039 HOH A O     1 
HETATM 24572 O  O     . HOH H 5 .    ? 135.429 79.552  82.560  1.00 17.38  ? 6040 HOH A O     1 
HETATM 24573 O  O     . HOH H 5 .    ? 132.557 115.670 126.991 1.00 38.45  ? 6041 HOH A O     1 
HETATM 24574 O  O     . HOH H 5 .    ? 99.269  94.069  48.065  1.00 23.85  ? 6042 HOH A O     1 
HETATM 24575 O  O     . HOH H 5 .    ? 74.682  89.491  91.741  1.00 20.76  ? 6043 HOH A O     1 
HETATM 24576 O  O     . HOH H 5 .    ? 126.738 91.417  108.184 1.00 10.92  ? 6044 HOH A O     1 
HETATM 24577 O  O     . HOH H 5 .    ? 68.640  118.097 94.965  1.00 28.56  ? 6045 HOH A O     1 
HETATM 24578 O  O     . HOH H 5 .    ? 110.631 71.219  63.281  1.00 25.39  ? 6046 HOH A O     1 
HETATM 24579 O  O     . HOH H 5 .    ? 106.810 69.171  88.714  1.00 34.40  ? 6047 HOH A O     1 
HETATM 24580 O  O     . HOH H 5 .    ? 94.327  66.908  58.065  1.00 20.71  ? 6048 HOH A O     1 
HETATM 24581 O  O     . HOH H 5 .    ? 69.199  82.706  122.725 1.00 11.34  ? 6049 HOH A O     1 
HETATM 24582 O  O     . HOH H 5 .    ? 95.977  110.664 128.132 1.00 16.58  ? 6050 HOH A O     1 
HETATM 24583 O  O     . HOH H 5 .    ? 61.238  115.695 73.615  1.00 23.00  ? 6051 HOH A O     1 
HETATM 24584 O  O     . HOH H 5 .    ? 116.474 114.080 139.631 1.00 24.57  ? 6052 HOH A O     1 
HETATM 24585 O  O     . HOH H 5 .    ? 90.904  75.611  113.292 1.00 8.51   ? 6053 HOH A O     1 
HETATM 24586 O  O     . HOH H 5 .    ? 50.752  96.416  76.610  1.00 23.28  ? 6054 HOH A O     1 
HETATM 24587 O  O     . HOH H 5 .    ? 58.082  93.496  141.827 1.00 20.14  ? 6055 HOH A O     1 
HETATM 24588 O  O     . HOH H 5 .    ? 84.204  103.855 77.609  1.00 28.48  ? 6056 HOH A O     1 
HETATM 24589 O  O     . HOH H 5 .    ? 127.763 114.542 95.106  1.00 25.09  ? 6057 HOH A O     1 
HETATM 24590 O  O     . HOH H 5 .    ? 93.635  84.032  106.479 1.00 20.30  ? 6058 HOH A O     1 
HETATM 24591 O  O     . HOH H 5 .    ? 120.424 65.203  72.094  1.00 42.97  ? 6059 HOH A O     1 
HETATM 24592 O  O     . HOH H 5 .    ? 92.685  92.563  66.757  1.00 24.91  ? 6060 HOH A O     1 
HETATM 24593 O  O     . HOH H 5 .    ? 137.362 113.688 83.482  1.00 32.77  ? 6061 HOH A O     1 
HETATM 24594 O  O     . HOH H 5 .    ? 105.032 102.060 99.813  1.00 24.94  ? 6062 HOH A O     1 
HETATM 24595 O  O     . HOH H 5 .    ? 37.520  96.584  91.599  1.00 33.05  ? 6063 HOH A O     1 
HETATM 24596 O  O     . HOH H 5 .    ? 38.232  102.236 102.934 1.00 18.96  ? 6064 HOH A O     1 
HETATM 24597 O  O     . HOH H 5 .    ? 68.683  83.725  45.456  1.00 33.68  ? 6065 HOH A O     1 
HETATM 24598 O  O     . HOH H 5 .    ? 53.937  85.053  96.312  1.00 15.54  ? 6066 HOH A O     1 
HETATM 24599 O  O     . HOH H 5 .    ? 110.176 69.541  116.555 1.00 21.59  ? 6067 HOH A O     1 
HETATM 24600 O  O     . HOH H 5 .    ? 128.190 71.129  84.036  1.00 20.63  ? 6068 HOH A O     1 
HETATM 24601 O  O     . HOH H 5 .    ? 54.840  128.278 110.176 1.00 36.99  ? 6069 HOH A O     1 
HETATM 24602 O  O     . HOH H 5 .    ? 117.154 96.087  102.950 1.00 18.49  ? 6070 HOH A O     1 
HETATM 24603 O  O     . HOH H 5 .    ? 107.689 68.485  90.783  1.00 25.34  ? 6071 HOH A O     1 
HETATM 24604 O  O     . HOH H 5 .    ? 89.790  67.270  127.166 1.00 23.98  ? 6072 HOH A O     1 
HETATM 24605 O  O     . HOH H 5 .    ? 67.324  55.557  136.794 1.00 43.73  ? 6073 HOH A O     1 
HETATM 24606 O  O     . HOH H 5 .    ? 56.495  131.108 111.906 1.00 43.51  ? 6074 HOH A O     1 
HETATM 24607 O  O     . HOH H 5 .    ? 133.279 95.823  120.430 1.00 19.36  ? 6075 HOH A O     1 
HETATM 24608 O  O     . HOH H 5 .    ? 107.322 96.941  73.390  1.00 19.17  ? 6076 HOH A O     1 
HETATM 24609 O  O     . HOH H 5 .    ? 51.393  82.020  106.156 1.00 14.05  ? 6077 HOH A O     1 
HETATM 24610 O  O     . HOH H 5 .    ? 64.714  113.352 73.147  1.00 14.01  ? 6078 HOH A O     1 
HETATM 24611 O  O     . HOH H 5 .    ? 91.946  67.392  63.251  1.00 25.03  ? 6079 HOH A O     1 
HETATM 24612 O  O     . HOH H 5 .    ? 53.867  79.468  109.349 1.00 13.78  ? 6080 HOH A O     1 
HETATM 24613 O  O     . HOH H 5 .    ? 124.431 101.865 120.582 1.00 9.35   ? 6081 HOH A O     1 
HETATM 24614 O  O     . HOH H 5 .    ? 51.027  112.437 102.970 1.00 15.55  ? 6082 HOH A O     1 
HETATM 24615 O  O     . HOH H 5 .    ? 89.384  80.678  144.677 1.00 27.30  ? 6083 HOH A O     1 
HETATM 24616 O  O     . HOH H 5 .    ? 48.581  66.383  134.363 1.00 24.89  ? 6084 HOH A O     1 
HETATM 24617 O  O     . HOH H 5 .    ? 86.129  94.621  63.253  1.00 21.97  ? 6085 HOH A O     1 
HETATM 24618 O  O     . HOH H 5 .    ? 117.409 72.635  82.442  1.00 21.13  ? 6086 HOH A O     1 
HETATM 24619 O  O     . HOH H 5 .    ? 77.585  99.092  130.232 1.00 21.18  ? 6087 HOH A O     1 
HETATM 24620 O  O     . HOH H 5 .    ? 99.946  91.539  150.120 1.00 22.80  ? 6088 HOH A O     1 
HETATM 24621 O  O     . HOH H 5 .    ? 79.169  68.686  119.693 1.00 17.33  ? 6089 HOH A O     1 
HETATM 24622 O  O     . HOH H 5 .    ? 79.444  100.971 126.880 1.00 11.66  ? 6090 HOH A O     1 
HETATM 24623 O  O     . HOH H 5 .    ? 135.494 77.827  79.584  1.00 22.49  ? 6091 HOH A O     1 
HETATM 24624 O  O     . HOH H 5 .    ? 116.071 101.768 79.572  1.00 16.78  ? 6092 HOH A O     1 
HETATM 24625 O  O     . HOH H 5 .    ? 56.907  98.031  84.542  1.00 13.66  ? 6093 HOH A O     1 
HETATM 24626 O  O     . HOH H 5 .    ? 124.057 73.664  117.126 1.00 40.19  ? 6094 HOH A O     1 
HETATM 24627 O  O     . HOH H 5 .    ? 84.444  95.206  154.162 1.00 24.35  ? 6095 HOH A O     1 
HETATM 24628 O  O     . HOH H 5 .    ? 113.970 69.033  86.383  1.00 28.35  ? 6096 HOH A O     1 
HETATM 24629 O  O     . HOH H 5 .    ? 83.535  95.687  148.076 1.00 24.92  ? 6097 HOH A O     1 
HETATM 24630 O  O     . HOH H 5 .    ? 52.924  62.256  122.004 1.00 15.19  ? 6098 HOH A O     1 
HETATM 24631 O  O     . HOH H 5 .    ? 100.222 55.253  123.382 1.00 24.28  ? 6099 HOH A O     1 
HETATM 24632 O  O     . HOH H 5 .    ? 131.251 98.178  133.798 1.00 20.15  ? 6100 HOH A O     1 
HETATM 24633 O  O     . HOH H 5 .    ? 72.929  116.064 102.470 1.00 18.14  ? 6101 HOH A O     1 
HETATM 24634 O  O     . HOH H 5 .    ? 105.157 93.645  138.112 1.00 12.16  ? 6102 HOH A O     1 
HETATM 24635 O  O     . HOH H 5 .    ? 121.702 105.380 97.147  1.00 18.02  ? 6103 HOH A O     1 
HETATM 24636 O  O     . HOH H 5 .    ? 35.022  81.998  121.612 1.00 29.28  ? 6104 HOH A O     1 
HETATM 24637 O  O     . HOH H 5 .    ? 48.649  96.704  88.002  1.00 13.73  ? 6105 HOH A O     1 
HETATM 24638 O  O     . HOH H 5 .    ? 106.667 92.842  120.905 1.00 13.71  ? 6106 HOH A O     1 
HETATM 24639 O  O     . HOH H 5 .    ? 68.374  69.939  80.521  1.00 30.52  ? 6107 HOH A O     1 
HETATM 24640 O  O     . HOH H 5 .    ? 127.932 96.547  127.360 1.00 14.94  ? 6108 HOH A O     1 
HETATM 24641 O  O     . HOH H 5 .    ? 60.192  94.289  85.528  1.00 22.21  ? 6109 HOH A O     1 
HETATM 24642 O  O     . HOH H 5 .    ? 59.004  97.026  143.409 1.00 29.92  ? 6110 HOH A O     1 
HETATM 24643 O  O     . HOH H 5 .    ? 59.534  116.770 76.477  1.00 28.95  ? 6111 HOH A O     1 
HETATM 24644 O  O     . HOH H 5 .    ? 64.181  91.934  99.993  1.00 9.84   ? 6112 HOH A O     1 
HETATM 24645 O  O     . HOH H 5 .    ? 76.771  113.178 100.343 1.00 31.30  ? 6113 HOH A O     1 
HETATM 24646 O  O     . HOH H 5 .    ? 139.074 81.952  67.407  1.00 25.68  ? 6114 HOH A O     1 
HETATM 24647 O  O     . HOH H 5 .    ? 89.724  84.413  74.817  1.00 28.18  ? 6115 HOH A O     1 
HETATM 24648 O  O     . HOH H 5 .    ? 66.872  103.694 55.481  1.00 17.48  ? 6116 HOH A O     1 
HETATM 24649 O  O     . HOH H 5 .    ? 45.437  110.711 77.122  1.00 34.84  ? 6117 HOH A O     1 
HETATM 24650 O  O     . HOH H 5 .    ? 137.075 100.638 135.529 1.00 21.59  ? 6118 HOH A O     1 
HETATM 24651 O  O     . HOH H 5 .    ? 82.424  70.169  117.191 1.00 15.50  ? 6119 HOH A O     1 
HETATM 24652 O  O     . HOH H 5 .    ? 96.092  89.704  46.585  1.00 20.58  ? 6120 HOH A O     1 
HETATM 24653 O  O     . HOH H 5 .    ? 77.463  67.916  111.466 1.00 14.26  ? 6121 HOH A O     1 
HETATM 24654 O  O     . HOH H 5 .    ? 66.514  87.835  47.806  1.00 36.49  ? 6122 HOH A O     1 
HETATM 24655 O  O     . HOH H 5 .    ? 70.764  65.936  105.726 1.00 15.11  ? 6123 HOH A O     1 
HETATM 24656 O  O     . HOH H 5 .    ? 115.733 70.813  84.998  1.00 23.13  ? 6124 HOH A O     1 
HETATM 24657 O  O     . HOH H 5 .    ? 103.672 98.251  48.832  1.00 24.00  ? 6125 HOH A O     1 
HETATM 24658 O  O     . HOH H 5 .    ? 85.696  100.828 63.590  1.00 18.00  ? 6126 HOH A O     1 
HETATM 24659 O  O     . HOH H 5 .    ? 92.222  93.939  48.421  1.00 26.47  ? 6127 HOH A O     1 
HETATM 24660 O  O     . HOH H 5 .    ? 67.400  53.064  131.736 1.00 36.64  ? 6128 HOH A O     1 
HETATM 24661 O  O     . HOH H 5 .    ? 46.083  105.921 120.941 1.00 13.10  ? 6129 HOH A O     1 
HETATM 24662 O  O     . HOH H 5 .    ? 141.620 84.042  71.877  1.00 13.43  ? 6130 HOH A O     1 
HETATM 24663 O  O     . HOH H 5 .    ? 138.179 76.396  77.250  1.00 12.15  ? 6131 HOH A O     1 
HETATM 24664 O  O     . HOH H 5 .    ? 80.173  69.224  111.086 1.00 20.44  ? 6132 HOH A O     1 
HETATM 24665 O  O     . HOH H 5 .    ? 81.524  123.924 127.775 1.00 52.15  ? 6133 HOH A O     1 
HETATM 24666 O  O     . HOH H 5 .    ? 152.363 108.753 93.583  1.00 24.59  ? 6134 HOH A O     1 
HETATM 24667 O  O     . HOH H 5 .    ? 51.440  113.280 89.440  1.00 14.46  ? 6135 HOH A O     1 
HETATM 24668 O  O     . HOH H 5 .    ? 41.091  91.433  131.062 1.00 19.11  ? 6136 HOH A O     1 
HETATM 24669 O  O     . HOH H 5 .    ? 122.787 102.913 71.279  1.00 19.46  ? 6137 HOH A O     1 
HETATM 24670 O  O     . HOH H 5 .    ? 59.634  82.793  104.931 1.00 6.61   ? 6138 HOH A O     1 
HETATM 24671 O  O     . HOH H 5 .    ? 63.648  121.374 81.279  1.00 20.54  ? 6139 HOH A O     1 
HETATM 24672 O  O     . HOH H 5 .    ? 130.080 72.822  106.946 1.00 12.69  ? 6140 HOH A O     1 
HETATM 24673 O  O     . HOH H 5 .    ? 114.739 93.435  139.247 1.00 14.32  ? 6141 HOH A O     1 
HETATM 24674 O  O     . HOH H 5 .    ? 105.560 67.013  123.547 1.00 30.36  ? 6142 HOH A O     1 
HETATM 24675 O  O     . HOH H 5 .    ? 113.072 91.351  42.666  1.00 43.26  ? 6143 HOH A O     1 
HETATM 24676 O  O     . HOH H 5 .    ? 62.716  89.440  121.087 1.00 5.76   ? 6144 HOH A O     1 
HETATM 24677 O  O     . HOH H 5 .    ? 72.435  93.512  133.236 1.00 21.96  ? 6145 HOH A O     1 
HETATM 24678 O  O     . HOH H 5 .    ? 39.633  96.572  140.193 1.00 22.09  ? 6146 HOH A O     1 
HETATM 24679 O  O     . HOH H 5 .    ? 128.641 100.294 128.420 1.00 18.28  ? 6147 HOH A O     1 
HETATM 24680 O  O     . HOH H 5 .    ? 87.083  90.424  78.873  1.00 22.04  ? 6148 HOH A O     1 
HETATM 24681 O  O     . HOH H 5 .    ? 91.625  76.114  135.436 1.00 21.12  ? 6149 HOH A O     1 
HETATM 24682 O  O     . HOH H 5 .    ? 100.137 70.304  81.503  1.00 37.61  ? 6150 HOH A O     1 
HETATM 24683 O  O     . HOH H 5 .    ? 89.861  99.172  56.063  1.00 23.44  ? 6151 HOH A O     1 
HETATM 24684 O  O     . HOH H 5 .    ? 150.549 98.621  102.949 1.00 19.75  ? 6152 HOH A O     1 
HETATM 24685 O  O     . HOH H 5 .    ? 46.580  95.438  118.054 1.00 10.89  ? 6153 HOH A O     1 
HETATM 24686 O  O     . HOH H 5 .    ? 84.309  68.551  137.652 1.00 20.65  ? 6154 HOH A O     1 
HETATM 24687 O  O     . HOH H 5 .    ? 129.300 91.202  87.344  1.00 7.56   ? 6155 HOH A O     1 
HETATM 24688 O  O     . HOH H 5 .    ? 99.895  73.349  114.842 1.00 17.57  ? 6156 HOH A O     1 
HETATM 24689 O  O     . HOH H 5 .    ? 119.573 91.257  150.449 1.00 26.34  ? 6157 HOH A O     1 
HETATM 24690 O  O     . HOH H 5 .    ? 49.880  93.935  76.393  1.00 17.24  ? 6158 HOH A O     1 
HETATM 24691 O  O     . HOH H 5 .    ? 106.999 101.030 72.265  1.00 20.28  ? 6159 HOH A O     1 
HETATM 24692 O  O     . HOH H 5 .    ? 59.874  124.384 86.274  1.00 23.15  ? 6160 HOH A O     1 
HETATM 24693 O  O     . HOH H 5 .    ? 61.194  64.867  109.796 1.00 30.67  ? 6161 HOH A O     1 
HETATM 24694 O  O     . HOH H 5 .    ? 64.696  92.257  93.309  1.00 18.18  ? 6162 HOH A O     1 
HETATM 24695 O  O     . HOH H 5 .    ? 52.570  77.729  135.451 1.00 9.43   ? 6163 HOH A O     1 
HETATM 24696 O  O     . HOH H 5 .    ? 48.201  115.365 89.958  1.00 35.53  ? 6164 HOH A O     1 
HETATM 24697 O  O     . HOH H 5 .    ? 54.912  121.137 87.972  1.00 22.44  ? 6165 HOH A O     1 
HETATM 24698 O  O     . HOH H 5 .    ? 144.352 89.015  77.614  1.00 20.96  ? 6166 HOH A O     1 
HETATM 24699 O  O     . HOH H 5 .    ? 58.871  78.162  83.640  1.00 40.13  ? 6167 HOH A O     1 
HETATM 24700 O  O     . HOH H 5 .    ? 30.557  89.640  118.418 1.00 21.42  ? 6168 HOH A O     1 
HETATM 24701 O  O     . HOH H 5 .    ? 86.016  89.240  50.618  1.00 23.74  ? 6169 HOH A O     1 
HETATM 24702 O  O     . HOH H 5 .    ? 109.836 103.559 145.195 1.00 24.39  ? 6170 HOH A O     1 
HETATM 24703 O  O     . HOH H 5 .    ? 40.990  69.127  125.179 1.00 30.46  ? 6171 HOH A O     1 
HETATM 24704 O  O     . HOH H 5 .    ? 118.966 95.533  93.322  1.00 16.11  ? 6172 HOH A O     1 
HETATM 24705 O  O     . HOH H 5 .    ? 81.761  90.149  137.577 1.00 13.15  ? 6173 HOH A O     1 
HETATM 24706 O  O     . HOH H 5 .    ? 81.399  46.550  123.918 1.00 27.30  ? 6174 HOH A O     1 
HETATM 24707 O  O     . HOH H 5 .    ? 106.912 65.952  100.589 1.00 24.24  ? 6175 HOH A O     1 
HETATM 24708 O  O     . HOH H 5 .    ? 81.954  88.119  101.817 1.00 21.68  ? 6176 HOH A O     1 
HETATM 24709 O  O     . HOH H 5 .    ? 59.188  95.436  140.585 1.00 28.33  ? 6177 HOH A O     1 
HETATM 24710 O  O     . HOH H 5 .    ? 130.216 106.998 78.676  1.00 18.73  ? 6178 HOH A O     1 
HETATM 24711 O  O     . HOH H 5 .    ? 59.149  73.983  116.597 1.00 13.57  ? 6179 HOH A O     1 
HETATM 24712 O  O     . HOH H 5 .    ? 100.554 76.521  115.703 1.00 10.76  ? 6180 HOH A O     1 
HETATM 24713 O  O     . HOH H 5 .    ? 72.958  110.656 75.461  1.00 20.33  ? 6181 HOH A O     1 
HETATM 24714 O  O     . HOH H 5 .    ? 114.948 117.141 137.719 1.00 39.99  ? 6182 HOH A O     1 
HETATM 24715 O  O     . HOH H 5 .    ? 114.656 70.859  124.462 1.00 22.89  ? 6183 HOH A O     1 
HETATM 24716 O  O     . HOH H 5 .    ? 84.754  70.131  117.486 1.00 11.76  ? 6184 HOH A O     1 
HETATM 24717 O  O     . HOH H 5 .    ? 77.278  89.856  132.947 1.00 10.24  ? 6185 HOH A O     1 
HETATM 24718 O  O     . HOH H 5 .    ? 57.504  106.583 77.371  1.00 9.12   ? 6186 HOH A O     1 
HETATM 24719 O  O     . HOH H 5 .    ? 92.732  69.221  136.049 1.00 28.36  ? 6187 HOH A O     1 
HETATM 24720 O  O     . HOH H 5 .    ? 65.318  104.714 71.389  1.00 15.14  ? 6188 HOH A O     1 
HETATM 24721 O  O     . HOH H 5 .    ? 62.893  72.184  137.312 1.00 24.22  ? 6189 HOH A O     1 
HETATM 24722 O  O     . HOH H 5 .    ? 110.730 110.983 53.991  1.00 21.49  ? 6190 HOH A O     1 
HETATM 24723 O  O     . HOH H 5 .    ? 133.311 91.460  94.936  1.00 18.52  ? 6191 HOH A O     1 
HETATM 24724 O  O     . HOH H 5 .    ? 83.384  88.635  89.018  1.00 27.67  ? 6192 HOH A O     1 
HETATM 24725 O  O     . HOH H 5 .    ? 115.125 78.496  109.547 1.00 25.81  ? 6193 HOH A O     1 
HETATM 24726 O  O     . HOH H 5 .    ? 107.284 90.364  128.730 1.00 15.23  ? 6194 HOH A O     1 
HETATM 24727 O  O     . HOH H 5 .    ? 71.511  95.811  133.538 1.00 25.12  ? 6195 HOH A O     1 
HETATM 24728 O  O     . HOH H 5 .    ? 115.410 80.990  44.234  1.00 28.89  ? 6196 HOH A O     1 
HETATM 24729 O  O     . HOH H 5 .    ? 90.859  82.652  107.603 1.00 10.00  ? 6197 HOH A O     1 
HETATM 24730 O  O     . HOH H 5 .    ? 89.106  75.944  133.636 1.00 16.57  ? 6198 HOH A O     1 
HETATM 24731 O  O     . HOH H 5 .    ? 133.528 100.308 76.582  1.00 33.59  ? 6199 HOH A O     1 
HETATM 24732 O  O     . HOH H 5 .    ? 128.615 93.104  107.116 1.00 13.01  ? 6200 HOH A O     1 
HETATM 24733 O  O     . HOH H 5 .    ? 85.311  95.614  80.386  1.00 18.77  ? 6201 HOH A O     1 
HETATM 24734 O  O     . HOH H 5 .    ? 123.221 108.489 102.156 1.00 24.41  ? 6202 HOH A O     1 
HETATM 24735 O  O     . HOH H 5 .    ? 106.452 51.718  131.679 1.00 44.24  ? 6203 HOH A O     1 
HETATM 24736 O  O     . HOH H 5 .    ? 108.687 74.590  80.020  1.00 23.94  ? 6204 HOH A O     1 
HETATM 24737 O  O     . HOH H 5 .    ? 129.116 91.605  47.850  1.00 50.04  ? 6205 HOH A O     1 
HETATM 24738 O  O     . HOH H 5 .    ? 132.181 112.751 141.149 1.00 26.72  ? 6206 HOH A O     1 
HETATM 24739 O  O     . HOH H 5 .    ? 134.918 90.767  92.135  1.00 20.33  ? 6207 HOH A O     1 
HETATM 24740 O  O     . HOH H 5 .    ? 92.211  69.664  122.258 1.00 24.38  ? 6208 HOH A O     1 
HETATM 24741 O  O     . HOH H 5 .    ? 55.958  127.699 90.023  1.00 33.96  ? 6209 HOH A O     1 
HETATM 24742 O  O     . HOH H 5 .    ? 102.145 60.736  71.531  1.00 29.40  ? 6210 HOH A O     1 
HETATM 24743 O  O     . HOH H 5 .    ? 72.188  97.186  138.208 1.00 17.57  ? 6211 HOH A O     1 
HETATM 24744 O  O     . HOH H 5 .    ? 43.936  100.698 116.294 1.00 12.61  ? 6212 HOH A O     1 
HETATM 24745 O  O     . HOH H 5 .    ? 39.100  96.096  104.766 1.00 8.86   ? 6213 HOH A O     1 
HETATM 24746 O  O     . HOH H 5 .    ? 98.577  110.520 102.643 1.00 41.34  ? 6214 HOH A O     1 
HETATM 24747 O  O     . HOH H 5 .    ? 140.087 87.197  90.429  1.00 18.82  ? 6215 HOH A O     1 
HETATM 24748 O  O     . HOH H 5 .    ? 73.642  92.154  125.501 1.00 17.89  ? 6216 HOH A O     1 
HETATM 24749 O  O     . HOH H 5 .    ? 80.239  80.288  71.552  1.00 25.04  ? 6217 HOH A O     1 
HETATM 24750 O  O     . HOH H 5 .    ? 35.838  87.348  93.615  1.00 43.28  ? 6218 HOH A O     1 
HETATM 24751 O  O     . HOH H 5 .    ? 73.908  50.290  124.764 1.00 35.65  ? 6219 HOH A O     1 
HETATM 24752 O  O     . HOH H 5 .    ? 113.538 95.730  99.349  1.00 28.92  ? 6220 HOH A O     1 
HETATM 24753 O  O     . HOH H 5 .    ? 87.776  88.358  76.998  1.00 33.55  ? 6221 HOH A O     1 
HETATM 24754 O  O     . HOH H 5 .    ? 107.337 85.435  45.008  1.00 22.18  ? 6222 HOH A O     1 
HETATM 24755 O  O     . HOH H 5 .    ? 108.291 95.718  127.757 1.00 10.75  ? 6223 HOH A O     1 
HETATM 24756 O  O     . HOH H 5 .    ? 118.972 62.742  115.173 1.00 29.33  ? 6224 HOH A O     1 
HETATM 24757 O  O     . HOH H 5 .    ? 116.005 75.303  109.087 1.00 35.77  ? 6225 HOH A O     1 
HETATM 24758 O  O     . HOH H 5 .    ? 41.198  89.623  105.827 1.00 27.86  ? 6226 HOH A O     1 
HETATM 24759 O  O     . HOH H 5 .    ? 109.509 91.368  75.393  1.00 23.69  ? 6227 HOH A O     1 
HETATM 24760 O  O     . HOH H 5 .    ? 52.513  85.782  93.600  1.00 46.89  ? 6228 HOH A O     1 
HETATM 24761 O  O     . HOH H 5 .    ? 107.074 65.371  125.048 1.00 27.72  ? 6229 HOH A O     1 
HETATM 24762 O  O     . HOH H 5 .    ? 71.635  95.695  130.982 1.00 19.91  ? 6230 HOH A O     1 
HETATM 24763 O  O     . HOH H 5 .    ? 66.751  52.675  125.799 1.00 32.32  ? 6231 HOH A O     1 
HETATM 24764 O  O     . HOH H 5 .    ? 116.333 106.406 46.465  1.00 25.21  ? 6232 HOH A O     1 
HETATM 24765 O  O     . HOH H 5 .    ? 33.326  98.717  102.022 1.00 28.36  ? 6233 HOH A O     1 
HETATM 24766 O  O     . HOH H 5 .    ? 83.557  86.451  56.900  1.00 41.92  ? 6234 HOH A O     1 
HETATM 24767 O  O     . HOH H 5 .    ? 56.700  118.402 75.929  1.00 34.37  ? 6235 HOH A O     1 
HETATM 24768 O  O     . HOH H 5 .    ? 79.092  74.092  81.200  1.00 21.93  ? 6236 HOH A O     1 
HETATM 24769 O  O     . HOH H 5 .    ? 115.993 110.265 114.114 1.00 11.70  ? 6237 HOH A O     1 
HETATM 24770 O  O     . HOH H 5 .    ? 72.312  55.081  134.472 1.00 48.34  ? 6238 HOH A O     1 
HETATM 24771 O  O     . HOH H 5 .    ? 67.991  109.978 53.981  1.00 24.43  ? 6239 HOH A O     1 
HETATM 24772 O  O     . HOH H 5 .    ? 95.583  95.493  52.983  1.00 25.89  ? 6240 HOH A O     1 
HETATM 24773 O  O     . HOH H 5 .    ? 71.873  125.769 96.770  1.00 30.56  ? 6241 HOH A O     1 
HETATM 24774 O  O     . HOH H 5 .    ? 90.474  113.931 127.598 1.00 26.93  ? 6242 HOH A O     1 
HETATM 24775 O  O     . HOH H 5 .    ? 54.071  91.478  125.914 1.00 5.33   ? 6243 HOH A O     1 
HETATM 24776 O  O     . HOH H 5 .    ? 65.698  111.497 142.995 1.00 28.63  ? 6244 HOH A O     1 
HETATM 24777 O  O     . HOH H 5 .    ? 148.799 88.608  106.764 1.00 41.77  ? 6245 HOH A O     1 
HETATM 24778 O  O     . HOH H 5 .    ? 129.320 85.404  55.210  1.00 38.02  ? 6246 HOH A O     1 
HETATM 24779 O  O     . HOH H 5 .    ? 86.396  71.516  123.558 1.00 3.74   ? 6247 HOH A O     1 
HETATM 24780 O  O     . HOH H 5 .    ? 39.312  105.408 101.724 1.00 22.32  ? 6248 HOH A O     1 
HETATM 24781 O  O     . HOH H 5 .    ? 122.848 109.139 112.573 1.00 12.10  ? 6249 HOH A O     1 
HETATM 24782 O  O     . HOH H 5 .    ? 78.864  71.557  135.865 1.00 18.31  ? 6250 HOH A O     1 
HETATM 24783 O  O     . HOH H 5 .    ? 132.265 77.806  88.538  1.00 25.34  ? 6251 HOH A O     1 
HETATM 24784 O  O     . HOH H 5 .    ? 80.646  57.288  133.668 1.00 18.33  ? 6252 HOH A O     1 
HETATM 24785 O  O     . HOH H 5 .    ? 99.142  92.279  118.556 1.00 7.73   ? 6253 HOH A O     1 
HETATM 24786 O  O     . HOH H 5 .    ? 99.512  77.998  113.012 1.00 22.37  ? 6254 HOH A O     1 
HETATM 24787 O  O     . HOH H 5 .    ? 80.213  63.304  126.814 1.00 31.72  ? 6255 HOH A O     1 
HETATM 24788 O  O     . HOH H 5 .    ? 128.770 103.455 48.733  1.00 31.67  ? 6256 HOH A O     1 
HETATM 24789 O  O     . HOH H 5 .    ? 65.672  94.821  96.112  1.00 18.13  ? 6257 HOH A O     1 
HETATM 24790 O  O     . HOH H 5 .    ? 60.813  114.842 61.239  1.00 19.02  ? 6258 HOH A O     1 
HETATM 24791 O  O     . HOH H 5 .    ? 57.673  105.631 107.874 1.00 16.06  ? 6259 HOH A O     1 
HETATM 24792 O  O     . HOH H 5 .    ? 73.866  78.837  73.630  1.00 15.52  ? 6260 HOH A O     1 
HETATM 24793 O  O     . HOH H 5 .    ? 55.569  67.750  117.199 1.00 15.16  ? 6261 HOH A O     1 
HETATM 24794 O  O     . HOH H 5 .    ? 70.201  127.702 91.543  1.00 32.84  ? 6262 HOH A O     1 
HETATM 24795 O  O     . HOH H 5 .    ? 121.661 86.882  50.750  1.00 31.51  ? 6263 HOH A O     1 
HETATM 24796 O  O     . HOH H 5 .    ? 129.056 108.615 101.923 1.00 25.46  ? 6264 HOH A O     1 
HETATM 24797 O  O     . HOH H 5 .    ? 72.131  95.176  123.693 1.00 23.85  ? 6265 HOH A O     1 
HETATM 24798 O  O     . HOH H 5 .    ? 82.079  58.374  132.167 1.00 14.52  ? 6266 HOH A O     1 
HETATM 24799 O  O     . HOH H 5 .    ? 46.314  112.017 74.276  1.00 33.15  ? 6267 HOH A O     1 
HETATM 24800 O  O     . HOH H 5 .    ? 128.109 95.397  130.099 1.00 17.33  ? 6268 HOH A O     1 
HETATM 24801 O  O     . HOH H 5 .    ? 104.489 75.441  129.766 1.00 21.06  ? 6269 HOH A O     1 
HETATM 24802 O  O     . HOH H 5 .    ? 113.070 102.681 69.441  1.00 15.86  ? 6270 HOH A O     1 
HETATM 24803 O  O     . HOH H 5 .    ? 67.694  106.101 80.216  1.00 20.55  ? 6271 HOH A O     1 
HETATM 24804 O  O     . HOH H 5 .    ? 51.168  98.371  111.293 1.00 4.04   ? 6272 HOH A O     1 
HETATM 24805 O  O     . HOH H 5 .    ? 107.382 98.384  97.654  1.00 32.30  ? 6273 HOH A O     1 
HETATM 24806 O  O     . HOH H 5 .    ? 48.164  116.849 92.627  1.00 43.90  ? 6274 HOH A O     1 
HETATM 24807 O  O     . HOH H 5 .    ? 60.567  104.820 59.764  1.00 19.09  ? 6275 HOH A O     1 
HETATM 24808 O  O     . HOH H 5 .    ? 121.645 106.891 100.675 1.00 25.65  ? 6276 HOH A O     1 
HETATM 24809 O  O     . HOH H 5 .    ? 56.748  105.352 74.693  1.00 8.47   ? 6277 HOH A O     1 
HETATM 24810 O  O     . HOH H 5 .    ? 52.696  94.388  123.589 1.00 11.50  ? 6278 HOH A O     1 
HETATM 24811 O  O     . HOH H 5 .    ? 110.338 99.957  146.007 1.00 12.02  ? 6279 HOH A O     1 
HETATM 24812 O  O     . HOH H 5 .    ? 42.731  86.223  96.053  1.00 18.31  ? 6280 HOH A O     1 
HETATM 24813 O  O     . HOH H 5 .    ? 81.303  104.701 136.599 1.00 15.31  ? 6281 HOH A O     1 
HETATM 24814 O  O     . HOH H 5 .    ? 118.284 83.376  66.362  1.00 10.30  ? 6282 HOH A O     1 
HETATM 24815 O  O     . HOH H 5 .    ? 128.159 91.101  95.084  1.00 24.63  ? 6283 HOH A O     1 
HETATM 24816 O  O     . HOH H 5 .    ? 134.646 114.277 90.909  1.00 19.93  ? 6284 HOH A O     1 
HETATM 24817 O  O     . HOH H 5 .    ? 133.180 99.068  132.281 1.00 22.47  ? 6285 HOH A O     1 
HETATM 24818 O  O     . HOH H 5 .    ? 72.628  76.783  93.155  1.00 16.65  ? 6286 HOH A O     1 
HETATM 24819 O  O     . HOH H 5 .    ? 99.572  103.210 117.946 1.00 26.81  ? 6287 HOH A O     1 
HETATM 24820 O  O     . HOH H 5 .    ? 55.926  103.155 68.917  1.00 32.89  ? 6288 HOH A O     1 
HETATM 24821 O  O     . HOH H 5 .    ? 105.036 89.699  64.528  1.00 10.92  ? 6289 HOH A O     1 
HETATM 24822 O  O     . HOH H 5 .    ? 72.547  127.237 130.280 1.00 51.59  ? 6290 HOH A O     1 
HETATM 24823 O  O     . HOH H 5 .    ? 96.344  100.256 52.729  1.00 25.02  ? 6291 HOH A O     1 
HETATM 24824 O  O     . HOH H 5 .    ? 58.164  92.784  129.161 1.00 10.71  ? 6292 HOH A O     1 
HETATM 24825 O  O     . HOH H 5 .    ? 74.489  78.816  129.191 1.00 10.57  ? 6293 HOH A O     1 
HETATM 24826 O  O     . HOH H 5 .    ? 54.102  102.760 111.752 1.00 15.11  ? 6294 HOH A O     1 
HETATM 24827 O  O     . HOH H 5 .    ? 58.108  98.151  147.740 1.00 41.27  ? 6295 HOH A O     1 
HETATM 24828 O  O     . HOH H 5 .    ? 91.203  79.670  67.293  1.00 15.80  ? 6296 HOH A O     1 
HETATM 24829 O  O     . HOH H 5 .    ? 50.958  94.195  101.843 1.00 11.49  ? 6297 HOH A O     1 
HETATM 24830 O  O     . HOH H 5 .    ? 52.102  111.249 105.480 1.00 19.02  ? 6298 HOH A O     1 
HETATM 24831 O  O     . HOH H 5 .    ? 115.372 98.176  70.236  1.00 12.83  ? 6299 HOH A O     1 
HETATM 24832 O  O     . HOH H 5 .    ? 72.046  120.500 139.777 1.00 34.52  ? 6300 HOH A O     1 
HETATM 24833 O  O     . HOH H 5 .    ? 61.844  116.545 62.429  1.00 27.76  ? 6301 HOH A O     1 
HETATM 24834 O  O     . HOH H 5 .    ? 98.361  71.906  127.919 1.00 23.15  ? 6302 HOH A O     1 
HETATM 24835 O  O     . HOH H 5 .    ? 118.879 71.113  74.734  1.00 37.45  ? 6303 HOH A O     1 
HETATM 24836 O  O     . HOH H 5 .    ? 105.074 70.393  56.841  1.00 17.85  ? 6304 HOH A O     1 
HETATM 24837 O  O     . HOH H 5 .    ? 41.994  69.882  128.711 1.00 19.36  ? 6305 HOH A O     1 
HETATM 24838 O  O     . HOH H 5 .    ? 59.052  96.824  99.426  1.00 12.63  ? 6306 HOH A O     1 
HETATM 24839 O  O     . HOH H 5 .    ? 75.126  119.702 62.913  1.00 37.03  ? 6307 HOH A O     1 
HETATM 24840 O  O     . HOH H 5 .    ? 91.936  61.369  126.975 1.00 18.95  ? 6308 HOH A O     1 
HETATM 24841 O  O     . HOH H 5 .    ? 53.113  122.163 90.601  1.00 23.63  ? 6309 HOH A O     1 
HETATM 24842 O  O     . HOH H 5 .    ? 35.254  97.418  132.549 1.00 26.34  ? 6310 HOH A O     1 
HETATM 24843 O  O     . HOH H 5 .    ? 51.843  76.641  138.706 1.00 10.72  ? 6311 HOH A O     1 
HETATM 24844 O  O     . HOH H 5 .    ? 64.753  108.491 119.087 1.00 17.03  ? 6312 HOH A O     1 
HETATM 24845 O  O     . HOH H 5 .    ? 122.287 85.357  73.591  1.00 20.43  ? 6313 HOH A O     1 
HETATM 24846 O  O     . HOH H 5 .    ? 107.891 87.504  61.597  1.00 19.23  ? 6314 HOH A O     1 
HETATM 24847 O  O     . HOH H 5 .    ? 116.941 108.344 113.094 1.00 10.07  ? 6315 HOH A O     1 
HETATM 24848 O  O     . HOH H 5 .    ? 103.068 54.209  131.977 1.00 34.56  ? 6316 HOH A O     1 
HETATM 24849 O  O     . HOH H 5 .    ? 110.901 99.438  97.709  1.00 31.03  ? 6317 HOH A O     1 
HETATM 24850 O  O     . HOH H 5 .    ? 108.741 80.627  51.819  1.00 18.56  ? 6318 HOH A O     1 
HETATM 24851 O  O     . HOH H 5 .    ? 93.229  80.704  106.195 1.00 26.50  ? 6319 HOH A O     1 
HETATM 24852 O  O     . HOH H 5 .    ? 112.313 83.076  126.772 1.00 12.16  ? 6320 HOH A O     1 
HETATM 24853 O  O     . HOH H 5 .    ? 99.624  70.704  131.819 1.00 27.98  ? 6321 HOH A O     1 
HETATM 24854 O  O     . HOH H 5 .    ? 44.145  107.927 121.064 1.00 12.72  ? 6322 HOH A O     1 
HETATM 24855 O  O     . HOH H 5 .    ? 127.778 86.975  95.252  1.00 16.86  ? 6323 HOH A O     1 
HETATM 24856 O  O     . HOH H 5 .    ? 79.300  75.402  98.589  1.00 13.00  ? 6324 HOH A O     1 
HETATM 24857 O  O     . HOH H 5 .    ? 63.122  135.220 97.956  1.00 34.47  ? 6325 HOH A O     1 
HETATM 24858 O  O     . HOH H 5 .    ? 149.056 99.875  101.814 1.00 23.78  ? 6326 HOH A O     1 
HETATM 24859 O  O     . HOH H 5 .    ? 45.374  113.586 97.850  1.00 24.70  ? 6327 HOH A O     1 
HETATM 24860 O  O     . HOH H 5 .    ? 67.948  64.820  135.962 1.00 22.58  ? 6328 HOH A O     1 
HETATM 24861 O  O     . HOH H 5 .    ? 29.517  94.437  122.976 1.00 22.99  ? 6329 HOH A O     1 
HETATM 24862 O  O     . HOH H 5 .    ? 62.540  66.639  116.142 1.00 9.65   ? 6330 HOH A O     1 
HETATM 24863 O  O     . HOH H 5 .    ? 61.488  68.665  114.999 1.00 20.37  ? 6331 HOH A O     1 
HETATM 24864 O  O     . HOH H 5 .    ? 103.715 84.296  39.064  1.00 25.31  ? 6332 HOH A O     1 
HETATM 24865 O  O     . HOH H 5 .    ? 102.055 77.622  54.010  1.00 24.59  ? 6333 HOH A O     1 
HETATM 24866 O  O     . HOH H 5 .    ? 99.299  100.322 111.358 1.00 19.05  ? 6334 HOH A O     1 
HETATM 24867 O  O     . HOH H 5 .    ? 115.701 108.559 60.272  1.00 31.09  ? 6335 HOH A O     1 
HETATM 24868 O  O     . HOH H 5 .    ? 65.950  103.341 57.553  1.00 19.69  ? 6336 HOH A O     1 
HETATM 24869 O  O     . HOH H 5 .    ? 65.820  97.873  74.064  1.00 23.39  ? 6337 HOH A O     1 
HETATM 24870 O  O     . HOH H 5 .    ? 68.167  112.798 79.952  1.00 27.41  ? 6338 HOH A O     1 
HETATM 24871 O  O     . HOH H 5 .    ? 141.958 106.783 77.576  1.00 41.87  ? 6339 HOH A O     1 
HETATM 24872 O  O     . HOH H 5 .    ? 126.864 113.554 92.225  1.00 15.64  ? 6340 HOH A O     1 
HETATM 24873 O  O     . HOH H 5 .    ? 112.623 84.667  73.751  1.00 21.45  ? 6341 HOH A O     1 
HETATM 24874 O  O     . HOH H 5 .    ? 116.629 100.359 73.206  1.00 21.57  ? 6342 HOH A O     1 
HETATM 24875 O  O     . HOH H 5 .    ? 32.909  102.949 129.230 1.00 26.95  ? 6343 HOH A O     1 
HETATM 24876 O  O     . HOH H 5 .    ? 128.868 92.994  102.891 1.00 10.65  ? 6344 HOH A O     1 
HETATM 24877 O  O     . HOH H 5 .    ? 136.358 105.914 111.980 1.00 22.94  ? 6345 HOH A O     1 
HETATM 24878 O  O     . HOH H 5 .    ? 37.005  84.032  118.782 1.00 11.41  ? 6346 HOH A O     1 
HETATM 24879 O  O     . HOH H 5 .    ? 154.092 107.906 95.579  1.00 32.99  ? 6347 HOH A O     1 
HETATM 24880 O  O     . HOH H 5 .    ? 60.000  74.667  83.656  1.00 27.94  ? 6348 HOH A O     1 
HETATM 24881 O  O     . HOH H 5 .    ? 101.546 93.553  117.500 1.00 6.83   ? 6349 HOH A O     1 
HETATM 24882 O  O     . HOH H 5 .    ? 81.578  43.881  117.890 1.00 38.37  ? 6350 HOH A O     1 
HETATM 24883 O  O     . HOH H 5 .    ? 63.344  103.187 87.688  1.00 21.10  ? 6351 HOH A O     1 
HETATM 24884 O  O     . HOH H 5 .    ? 81.642  75.408  80.981  1.00 20.43  ? 6352 HOH A O     1 
HETATM 24885 O  O     . HOH H 5 .    ? 46.572  86.674  92.726  1.00 28.99  ? 6353 HOH A O     1 
HETATM 24886 O  O     . HOH H 5 .    ? 121.664 110.375 144.238 1.00 23.35  ? 6354 HOH A O     1 
HETATM 24887 O  O     . HOH H 5 .    ? 52.978  119.086 88.574  1.00 23.15  ? 6355 HOH A O     1 
HETATM 24888 O  O     . HOH H 5 .    ? 66.329  95.550  98.908  1.00 11.28  ? 6356 HOH A O     1 
HETATM 24889 O  O     . HOH H 5 .    ? 59.731  106.080 106.735 1.00 15.08  ? 6357 HOH A O     1 
HETATM 24890 O  O     . HOH H 5 .    ? 105.999 104.745 62.957  1.00 23.52  ? 6358 HOH A O     1 
HETATM 24891 O  O     . HOH H 5 .    ? 73.038  101.377 118.291 1.00 11.57  ? 6359 HOH A O     1 
HETATM 24892 O  O     . HOH H 5 .    ? 76.769  125.716 69.416  1.00 36.50  ? 6360 HOH A O     1 
HETATM 24893 O  O     . HOH H 5 .    ? 143.964 110.850 99.624  1.00 12.71  ? 6361 HOH A O     1 
HETATM 24894 O  O     . HOH H 5 .    ? 61.139  103.860 84.858  1.00 12.31  ? 6362 HOH A O     1 
HETATM 24895 O  O     . HOH H 5 .    ? 151.221 94.784  108.521 1.00 30.00  ? 6363 HOH A O     1 
HETATM 24896 O  O     . HOH H 5 .    ? 133.955 88.608  90.412  1.00 20.00  ? 6364 HOH A O     1 
HETATM 24897 O  O     . HOH H 5 .    ? 57.863  104.391 113.869 1.00 13.85  ? 6365 HOH A O     1 
HETATM 24898 O  O     . HOH H 5 .    ? 133.446 80.438  93.944  1.00 19.57  ? 6366 HOH A O     1 
HETATM 24899 O  O     . HOH H 5 .    ? 69.874  95.522  127.742 1.00 17.00  ? 6367 HOH A O     1 
HETATM 24900 O  O     . HOH H 5 .    ? 55.362  75.570  80.590  1.00 41.99  ? 6368 HOH A O     1 
HETATM 24901 O  O     . HOH H 5 .    ? 77.055  69.437  113.305 1.00 14.66  ? 6369 HOH A O     1 
HETATM 24902 O  O     . HOH H 5 .    ? 128.934 97.758  78.291  1.00 23.08  ? 6370 HOH A O     1 
HETATM 24903 O  O     . HOH H 5 .    ? 104.046 55.920  130.497 1.00 40.29  ? 6371 HOH A O     1 
HETATM 24904 O  O     . HOH H 5 .    ? 110.588 107.916 57.945  1.00 13.93  ? 6372 HOH A O     1 
HETATM 24905 O  O     . HOH H 5 .    ? 56.844  120.629 77.045  1.00 29.93  ? 6373 HOH A O     1 
HETATM 24906 O  O     . HOH H 5 .    ? 38.659  108.957 121.482 1.00 24.14  ? 6374 HOH A O     1 
HETATM 24907 O  O     . HOH H 5 .    ? 109.724 90.786  126.772 1.00 20.74  ? 6375 HOH A O     1 
HETATM 24908 O  O     . HOH H 5 .    ? 74.834  90.347  134.000 1.00 25.58  ? 6376 HOH A O     1 
HETATM 24909 O  O     . HOH H 5 .    ? 37.571  85.820  99.180  1.00 30.69  ? 6377 HOH A O     1 
HETATM 24910 O  O     . HOH H 5 .    ? 104.738 77.863  97.635  1.00 31.19  ? 6378 HOH A O     1 
HETATM 24911 O  O     . HOH H 5 .    ? 105.710 82.840  129.769 1.00 15.38  ? 6379 HOH A O     1 
HETATM 24912 O  O     . HOH H 5 .    ? 120.066 104.487 100.497 1.00 21.10  ? 6380 HOH A O     1 
HETATM 24913 O  O     . HOH H 5 .    ? 68.295  107.942 78.800  1.00 29.60  ? 6381 HOH A O     1 
HETATM 24914 O  O     . HOH H 5 .    ? 33.842  107.022 119.955 1.00 36.06  ? 6382 HOH A O     1 
HETATM 24915 O  O     . HOH H 5 .    ? 77.208  96.988  138.844 1.00 26.73  ? 6383 HOH A O     1 
HETATM 24916 O  O     . HOH H 5 .    ? 130.091 66.532  98.767  1.00 24.52  ? 6384 HOH A O     1 
HETATM 24917 O  O     . HOH H 5 .    ? 127.300 95.583  77.996  1.00 22.45  ? 6385 HOH A O     1 
HETATM 24918 O  O     . HOH H 5 .    ? 41.275  82.879  136.359 1.00 28.52  ? 6386 HOH A O     1 
HETATM 24919 O  O     . HOH H 5 .    ? 58.565  91.300  112.736 1.00 2.03   ? 6387 HOH A O     1 
HETATM 24920 O  O     . HOH H 5 .    ? 96.143  84.148  132.467 1.00 7.54   ? 6388 HOH A O     1 
HETATM 24921 O  O     . HOH H 5 .    ? 98.382  99.126  114.755 1.00 15.19  ? 6389 HOH A O     1 
HETATM 24922 O  O     . HOH H 5 .    ? 86.054  88.667  61.705  1.00 26.23  ? 6390 HOH A O     1 
HETATM 24923 O  O     . HOH H 5 .    ? 103.834 105.687 64.299  1.00 29.49  ? 6391 HOH A O     1 
HETATM 24924 O  O     . HOH H 5 .    ? 107.852 69.462  86.279  1.00 32.10  ? 6392 HOH A O     1 
HETATM 24925 O  O     . HOH H 5 .    ? 101.806 68.454  117.928 1.00 22.00  ? 6393 HOH A O     1 
HETATM 24926 O  O     . HOH H 5 .    ? 47.418  104.752 104.506 1.00 16.74  ? 6394 HOH A O     1 
HETATM 24927 O  O     . HOH H 5 .    ? 48.698  95.893  84.030  1.00 21.81  ? 6395 HOH A O     1 
HETATM 24928 O  O     . HOH H 5 .    ? 59.066  87.736  122.771 1.00 15.29  ? 6396 HOH A O     1 
HETATM 24929 O  O     . HOH H 5 .    ? 41.896  77.270  112.526 1.00 28.52  ? 6397 HOH A O     1 
HETATM 24930 O  O     . HOH H 5 .    ? 61.560  117.728 58.588  1.00 44.35  ? 6398 HOH A O     1 
HETATM 24931 O  O     . HOH H 5 .    ? 116.635 107.448 148.355 1.00 20.56  ? 6399 HOH A O     1 
HETATM 24932 O  O     . HOH H 5 .    ? 87.551  68.595  138.120 1.00 26.52  ? 6400 HOH A O     1 
HETATM 24933 O  O     . HOH H 5 .    ? 49.209  117.903 90.026  1.00 39.63  ? 6401 HOH A O     1 
HETATM 24934 O  O     . HOH H 5 .    ? 60.966  81.916  103.139 1.00 6.91   ? 6402 HOH A O     1 
HETATM 24935 O  O     . HOH H 5 .    ? 60.697  111.760 79.401  1.00 20.89  ? 6403 HOH A O     1 
HETATM 24936 O  O     . HOH H 5 .    ? 143.364 87.614  79.524  1.00 13.86  ? 6404 HOH A O     1 
HETATM 24937 O  O     . HOH H 5 .    ? 43.746  66.028  116.359 1.00 25.05  ? 6405 HOH A O     1 
HETATM 24938 O  O     . HOH H 5 .    ? 149.330 98.853  83.258  1.00 16.15  ? 6406 HOH A O     1 
HETATM 24939 O  O     . HOH H 5 .    ? 57.450  105.664 69.888  1.00 36.84  ? 6407 HOH A O     1 
HETATM 24940 O  O     . HOH H 5 .    ? 62.737  108.145 72.698  1.00 26.31  ? 6408 HOH A O     1 
HETATM 24941 O  O     . HOH H 5 .    ? 48.725  112.273 102.039 1.00 20.48  ? 6409 HOH A O     1 
HETATM 24942 O  O     . HOH H 5 .    ? 141.658 99.052  75.852  1.00 22.89  ? 6410 HOH A O     1 
HETATM 24943 O  O     . HOH H 5 .    ? 59.139  109.744 77.458  1.00 26.87  ? 6411 HOH A O     1 
HETATM 24944 O  O     . HOH H 5 .    ? 75.015  133.536 103.168 1.00 27.19  ? 6412 HOH A O     1 
HETATM 24945 O  O     . HOH H 5 .    ? 34.521  97.556  105.707 1.00 26.62  ? 6413 HOH A O     1 
HETATM 24946 O  O     . HOH H 5 .    ? 74.608  111.493 80.121  1.00 27.65  ? 6414 HOH A O     1 
HETATM 24947 O  O     . HOH H 5 .    ? 73.992  92.676  128.697 1.00 22.02  ? 6415 HOH A O     1 
HETATM 24948 O  O     . HOH H 5 .    ? 65.019  87.884  44.027  1.00 28.09  ? 6416 HOH A O     1 
HETATM 24949 O  O     . HOH H 5 .    ? 83.200  65.328  138.712 1.00 38.45  ? 6417 HOH A O     1 
HETATM 24950 O  O     . HOH H 5 .    ? 66.188  51.318  122.779 1.00 23.64  ? 6418 HOH A O     1 
HETATM 24951 O  O     . HOH H 5 .    ? 62.780  93.386  86.534  1.00 22.61  ? 6419 HOH A O     1 
HETATM 24952 O  O     . HOH H 5 .    ? 70.873  135.699 100.888 1.00 33.33  ? 6420 HOH A O     1 
HETATM 24953 O  O     . HOH H 5 .    ? 126.373 99.381  80.206  1.00 22.47  ? 6421 HOH A O     1 
HETATM 24954 O  O     . HOH H 5 .    ? 90.295  61.780  125.172 1.00 22.99  ? 6422 HOH A O     1 
HETATM 24955 O  O     . HOH H 5 .    ? 106.140 111.654 135.929 1.00 30.14  ? 6423 HOH A O     1 
HETATM 24956 O  O     . HOH H 5 .    ? 128.765 72.532  82.203  1.00 13.46  ? 6424 HOH A O     1 
HETATM 24957 O  O     . HOH H 5 .    ? 77.286  67.481  106.923 1.00 25.29  ? 6425 HOH A O     1 
HETATM 24958 O  O     . HOH H 5 .    ? 127.256 85.770  114.826 1.00 13.77  ? 6426 HOH A O     1 
HETATM 24959 O  O     . HOH H 5 .    ? 77.823  65.235  76.875  1.00 28.88  ? 6427 HOH A O     1 
HETATM 24960 O  O     . HOH H 5 .    ? 72.075  104.757 117.268 1.00 26.59  ? 6428 HOH A O     1 
HETATM 24961 O  O     . HOH H 5 .    ? 46.483  101.347 117.089 1.00 8.09   ? 6429 HOH A O     1 
HETATM 24962 O  O     . HOH H 5 .    ? 98.861  66.669  133.394 1.00 32.75  ? 6430 HOH A O     1 
HETATM 24963 O  O     . HOH H 5 .    ? 121.157 60.804  114.347 1.00 28.09  ? 6431 HOH A O     1 
HETATM 24964 O  O     . HOH H 5 .    ? 133.552 80.205  65.311  1.00 28.01  ? 6432 HOH A O     1 
HETATM 24965 O  O     . HOH H 5 .    ? 104.800 99.482  144.352 1.00 9.14   ? 6433 HOH A O     1 
HETATM 24966 O  O     . HOH H 5 .    ? 122.173 106.729 147.606 1.00 26.33  ? 6434 HOH A O     1 
HETATM 24967 O  O     . HOH H 5 .    ? 142.051 85.863  89.918  1.00 17.89  ? 6435 HOH A O     1 
HETATM 24968 O  O     . HOH H 5 .    ? 103.071 102.890 104.903 1.00 16.38  ? 6436 HOH A O     1 
HETATM 24969 O  O     . HOH H 5 .    ? 68.224  129.590 79.049  1.00 41.01  ? 6437 HOH A O     1 
HETATM 24970 O  O     . HOH H 5 .    ? 119.382 109.188 147.080 1.00 20.53  ? 6438 HOH A O     1 
HETATM 24971 O  O     . HOH H 5 .    ? 98.128  90.503  129.257 1.00 9.84   ? 6439 HOH A O     1 
HETATM 24972 O  O     . HOH H 5 .    ? 39.137  80.959  114.969 1.00 17.94  ? 6440 HOH A O     1 
HETATM 24973 O  O     . HOH H 5 .    ? 72.220  70.720  95.518  1.00 33.31  ? 6441 HOH A O     1 
HETATM 24974 O  O     . HOH H 5 .    ? 120.789 59.488  108.510 1.00 22.51  ? 6442 HOH A O     1 
HETATM 24975 O  O     . HOH H 5 .    ? 87.708  83.366  72.070  1.00 27.56  ? 6443 HOH A O     1 
HETATM 24976 O  O     . HOH H 5 .    ? 65.588  85.912  49.077  1.00 42.49  ? 6444 HOH A O     1 
HETATM 24977 O  O     . HOH H 5 .    ? 45.507  100.914 108.901 1.00 27.92  ? 6445 HOH A O     1 
HETATM 24978 O  O     . HOH H 5 .    ? 114.033 92.094  136.482 1.00 18.77  ? 6446 HOH A O     1 
HETATM 24979 O  O     . HOH H 5 .    ? 81.830  85.464  68.283  1.00 19.87  ? 6447 HOH A O     1 
HETATM 24980 O  O     . HOH H 5 .    ? 79.843  97.260  142.942 1.00 44.71  ? 6448 HOH A O     1 
HETATM 24981 O  O     . HOH H 5 .    ? 67.071  117.899 92.939  1.00 25.99  ? 6449 HOH A O     1 
HETATM 24982 O  O     . HOH H 5 .    ? 54.764  103.663 72.184  1.00 27.10  ? 6450 HOH A O     1 
HETATM 24983 O  O     . HOH H 5 .    ? 65.959  110.082 82.455  1.00 31.63  ? 6451 HOH A O     1 
HETATM 24984 O  O     . HOH H 5 .    ? 113.845 81.680  107.374 1.00 19.52  ? 6452 HOH A O     1 
HETATM 24985 O  O     . HOH H 5 .    ? 37.184  99.123  105.746 1.00 14.19  ? 6453 HOH A O     1 
HETATM 24986 O  O     . HOH H 5 .    ? 103.880 104.973 62.072  1.00 30.73  ? 6454 HOH A O     1 
HETATM 24987 O  O     . HOH H 5 .    ? 75.365  95.324  125.151 1.00 24.90  ? 6455 HOH A O     1 
HETATM 24988 O  O     . HOH H 5 .    ? 77.040  72.091  107.318 1.00 12.56  ? 6456 HOH A O     1 
HETATM 24989 O  O     . HOH H 5 .    ? 106.525 91.798  81.606  1.00 17.94  ? 6457 HOH A O     1 
HETATM 24990 O  O     . HOH H 5 .    ? 141.365 105.247 75.413  1.00 43.90  ? 6458 HOH A O     1 
HETATM 24991 O  O     . HOH H 5 .    ? 107.568 95.976  147.859 1.00 25.00  ? 6459 HOH A O     1 
HETATM 24992 O  O     . HOH H 5 .    ? 116.904 69.041  115.877 1.00 22.14  ? 6460 HOH A O     1 
HETATM 24993 O  O     . HOH H 5 .    ? 110.159 79.640  55.685  1.00 14.52  ? 6461 HOH A O     1 
HETATM 24994 O  O     . HOH H 5 .    ? 88.747  101.504 151.673 1.00 36.80  ? 6462 HOH A O     1 
HETATM 24995 O  O     . HOH H 5 .    ? 108.190 116.238 132.654 1.00 26.76  ? 6463 HOH A O     1 
HETATM 24996 O  O     . HOH H 5 .    ? 105.443 105.104 108.187 1.00 18.52  ? 6464 HOH A O     1 
HETATM 24997 O  O     . HOH H 5 .    ? 117.461 72.758  129.008 1.00 27.32  ? 6465 HOH A O     1 
HETATM 24998 O  O     . HOH H 5 .    ? 40.681  87.183  101.058 1.00 27.27  ? 6466 HOH A O     1 
HETATM 24999 O  O     . HOH H 5 .    ? 100.146 77.114  130.046 1.00 17.02  ? 6467 HOH A O     1 
HETATM 25000 O  O     . HOH H 5 .    ? 77.177  105.612 50.695  1.00 32.18  ? 6468 HOH A O     1 
HETATM 25001 O  O     . HOH H 5 .    ? 88.960  58.523  124.752 1.00 18.40  ? 6469 HOH A O     1 
HETATM 25002 O  O     . HOH H 5 .    ? 49.651  96.905  113.755 1.00 15.22  ? 6470 HOH A O     1 
HETATM 25003 O  O     . HOH H 5 .    ? 100.624 97.105  48.449  1.00 19.06  ? 6471 HOH A O     1 
HETATM 25004 O  O     . HOH H 5 .    ? 80.828  46.351  119.097 1.00 23.33  ? 6472 HOH A O     1 
HETATM 25005 O  O     . HOH H 5 .    ? 45.013  107.356 118.961 1.00 11.26  ? 6473 HOH A O     1 
HETATM 25006 O  O     . HOH H 5 .    ? 137.562 108.774 111.752 1.00 24.58  ? 6474 HOH A O     1 
HETATM 25007 O  O     . HOH H 5 .    ? 129.006 113.687 96.850  1.00 33.93  ? 6475 HOH A O     1 
HETATM 25008 O  O     . HOH H 5 .    ? 50.721  87.582  139.307 1.00 25.93  ? 6476 HOH A O     1 
HETATM 25009 O  O     . HOH H 5 .    ? 148.810 105.412 103.328 1.00 23.08  ? 6477 HOH A O     1 
HETATM 25010 O  O     . HOH H 5 .    ? 128.610 93.590  91.148  1.00 10.82  ? 6478 HOH A O     1 
HETATM 25011 O  O     . HOH H 5 .    ? 50.683  117.042 77.058  1.00 48.29  ? 6479 HOH A O     1 
HETATM 25012 O  O     . HOH H 5 .    ? 83.267  103.949 62.066  1.00 13.75  ? 6480 HOH A O     1 
HETATM 25013 O  O     . HOH H 5 .    ? 100.041 111.029 135.219 1.00 20.96  ? 6481 HOH A O     1 
HETATM 25014 O  O     . HOH H 5 .    ? 63.762  115.652 75.167  1.00 20.11  ? 6482 HOH A O     1 
HETATM 25015 O  O     . HOH H 5 .    ? 131.872 89.851  96.928  1.00 29.02  ? 6483 HOH A O     1 
HETATM 25016 O  O     . HOH H 5 .    ? 88.404  108.915 134.377 1.00 22.07  ? 6484 HOH A O     1 
HETATM 25017 O  O     . HOH H 5 .    ? 61.550  123.575 81.390  1.00 19.47  ? 6485 HOH A O     1 
HETATM 25018 O  O     . HOH H 5 .    ? 60.220  114.776 64.636  1.00 28.93  ? 6486 HOH A O     1 
HETATM 25019 O  O     . HOH H 5 .    ? 117.129 110.174 110.333 1.00 19.62  ? 6487 HOH A O     1 
HETATM 25020 O  O     . HOH H 5 .    ? 66.205  105.412 87.360  1.00 18.05  ? 6488 HOH A O     1 
HETATM 25021 O  O     . HOH H 5 .    ? 96.830  80.076  108.198 1.00 20.55  ? 6489 HOH A O     1 
HETATM 25022 O  O     . HOH H 5 .    ? 94.386  77.270  118.210 1.00 11.87  ? 6490 HOH A O     1 
HETATM 25023 O  O     . HOH H 5 .    ? 64.643  93.395  63.992  1.00 15.23  ? 6491 HOH A O     1 
HETATM 25024 O  O     . HOH H 5 .    ? 111.041 94.047  148.593 1.00 25.88  ? 6492 HOH A O     1 
HETATM 25025 O  O     . HOH H 5 .    ? 54.559  119.336 77.792  1.00 44.70  ? 6493 HOH A O     1 
HETATM 25026 O  O     . HOH H 5 .    ? 128.912 72.645  109.756 1.00 22.59  ? 6494 HOH A O     1 
HETATM 25027 O  O     . HOH H 5 .    ? 60.827  92.567  143.378 1.00 34.20  ? 6495 HOH A O     1 
HETATM 25028 O  O     . HOH H 5 .    ? 56.686  84.657  123.879 1.00 3.67   ? 6496 HOH A O     1 
HETATM 25029 O  O     . HOH H 5 .    ? 65.906  110.387 74.491  1.00 24.32  ? 6497 HOH A O     1 
HETATM 25030 O  O     . HOH H 5 .    ? 77.335  75.758  130.061 1.00 12.60  ? 6498 HOH A O     1 
HETATM 25031 O  O     . HOH H 5 .    ? 71.254  94.016  140.761 1.00 20.43  ? 6499 HOH A O     1 
HETATM 25032 O  O     . HOH H 5 .    ? 75.360  55.746  133.761 1.00 39.36  ? 6500 HOH A O     1 
HETATM 25033 O  O     . HOH H 5 .    ? 56.051  106.912 72.331  1.00 34.44  ? 6501 HOH A O     1 
HETATM 25034 O  O     . HOH H 5 .    ? 106.505 79.963  105.246 1.00 29.25  ? 6502 HOH A O     1 
HETATM 25035 O  O     . HOH H 5 .    ? 60.282  97.528  84.976  1.00 25.34  ? 6503 HOH A O     1 
HETATM 25036 O  O     . HOH H 5 .    ? 126.211 118.684 121.410 1.00 27.70  ? 6504 HOH A O     1 
HETATM 25037 O  O     . HOH H 5 .    ? 131.456 90.509  92.692  1.00 30.73  ? 6505 HOH A O     1 
HETATM 25038 O  O     . HOH H 5 .    ? 108.127 78.631  106.223 1.00 20.56  ? 6506 HOH A O     1 
HETATM 25039 O  O     . HOH H 5 .    ? 117.236 93.257  57.730  1.00 7.50   ? 6507 HOH A O     1 
HETATM 25040 O  O     . HOH H 5 .    ? 130.584 97.440  130.776 1.00 18.15  ? 6508 HOH A O     1 
HETATM 25041 O  O     . HOH H 5 .    ? 59.488  65.714  112.241 1.00 29.78  ? 6509 HOH A O     1 
HETATM 25042 O  O     . HOH H 5 .    ? 52.329  92.209  88.265  1.00 9.08   ? 6510 HOH A O     1 
HETATM 25043 O  O     . HOH H 5 .    ? 120.686 78.949  130.037 1.00 29.21  ? 6511 HOH A O     1 
HETATM 25044 O  O     . HOH H 5 .    ? 140.000 93.384  87.842  1.00 11.14  ? 6512 HOH A O     1 
HETATM 25045 O  O     . HOH H 5 .    ? 109.317 104.762 95.753  1.00 33.26  ? 6513 HOH A O     1 
HETATM 25046 O  O     . HOH H 5 .    ? 66.049  83.229  120.883 1.00 22.58  ? 6514 HOH A O     1 
HETATM 25047 O  O     . HOH H 5 .    ? 158.866 97.821  95.096  1.00 33.57  ? 6515 HOH A O     1 
HETATM 25048 O  O     . HOH H 5 .    ? 81.118  66.523  128.638 1.00 25.21  ? 6516 HOH A O     1 
HETATM 25049 O  O     . HOH H 5 .    ? 85.279  109.376 136.623 1.00 25.78  ? 6517 HOH A O     1 
HETATM 25050 O  O     . HOH H 5 .    ? 37.477  74.849  126.874 1.00 23.10  ? 6518 HOH A O     1 
HETATM 25051 O  O     . HOH H 5 .    ? 145.841 96.722  80.666  1.00 20.20  ? 6519 HOH A O     1 
HETATM 25052 O  O     . HOH H 5 .    ? 135.548 95.041  136.342 1.00 26.31  ? 6520 HOH A O     1 
HETATM 25053 O  O     . HOH H 5 .    ? 82.118  83.752  138.351 1.00 9.50   ? 6521 HOH A O     1 
HETATM 25054 O  O     . HOH H 5 .    ? 112.302 93.184  134.066 1.00 23.10  ? 6522 HOH A O     1 
HETATM 25055 O  O     . HOH H 5 .    ? 89.280  91.808  63.725  1.00 27.69  ? 6523 HOH A O     1 
HETATM 25056 O  O     . HOH H 5 .    ? 92.649  83.357  146.174 1.00 18.19  ? 6524 HOH A O     1 
HETATM 25057 O  O     . HOH H 5 .    ? 76.233  119.814 80.316  1.00 19.18  ? 6525 HOH A O     1 
HETATM 25058 O  O     . HOH H 5 .    ? 86.721  75.699  141.160 1.00 23.67  ? 6526 HOH A O     1 
HETATM 25059 O  O     . HOH H 5 .    ? 125.418 96.859  78.336  1.00 21.90  ? 6527 HOH A O     1 
HETATM 25060 O  O     . HOH H 5 .    ? 86.011  68.824  127.019 1.00 15.84  ? 6528 HOH A O     1 
HETATM 25061 O  O     . HOH H 5 .    ? 48.927  102.525 138.864 1.00 34.93  ? 6529 HOH A O     1 
HETATM 25062 O  O     . HOH H 5 .    ? 126.860 87.140  98.401  1.00 20.61  ? 6530 HOH A O     1 
HETATM 25063 O  O     . HOH H 5 .    ? 111.647 85.101  53.889  1.00 14.49  ? 6531 HOH A O     1 
HETATM 25064 O  O     . HOH H 5 .    ? 39.510  73.140  128.708 1.00 23.67  ? 6532 HOH A O     1 
HETATM 25065 O  O     . HOH H 5 .    ? 140.256 77.411  75.611  1.00 19.94  ? 6533 HOH A O     1 
HETATM 25066 O  O     . HOH H 5 .    ? 146.600 114.681 94.268  1.00 29.63  ? 6534 HOH A O     1 
HETATM 25067 O  O     . HOH H 5 .    ? 37.352  103.531 101.281 1.00 27.03  ? 6535 HOH A O     1 
HETATM 25068 O  O     . HOH H 5 .    ? 32.738  99.329  132.087 1.00 34.05  ? 6536 HOH A O     1 
HETATM 25069 O  O     . HOH H 5 .    ? 66.414  111.101 106.649 1.00 39.30  ? 6537 HOH A O     1 
HETATM 25070 O  O     . HOH H 5 .    ? 111.420 95.704  136.299 1.00 14.09  ? 6538 HOH A O     1 
HETATM 25071 O  O     . HOH H 5 .    ? 91.523  50.047  117.653 1.00 36.47  ? 6539 HOH A O     1 
HETATM 25072 O  O     . HOH H 5 .    ? 75.229  123.079 52.797  1.00 39.62  ? 6540 HOH A O     1 
HETATM 25073 O  O     . HOH H 5 .    ? 77.303  80.793  136.916 1.00 10.52  ? 6541 HOH A O     1 
HETATM 25074 O  O     . HOH H 5 .    ? 80.374  105.979 52.165  1.00 41.23  ? 6542 HOH A O     1 
HETATM 25075 O  O     . HOH H 5 .    ? 31.210  107.444 98.171  1.00 36.58  ? 6543 HOH A O     1 
HETATM 25076 O  O     . HOH H 5 .    ? 92.443  69.005  119.371 1.00 31.11  ? 6544 HOH A O     1 
HETATM 25077 O  O     . HOH H 5 .    ? 120.044 64.224  94.675  1.00 10.30  ? 6545 HOH A O     1 
HETATM 25078 O  O     . HOH H 5 .    ? 106.109 109.909 108.043 1.00 26.89  ? 6546 HOH A O     1 
HETATM 25079 O  O     . HOH H 5 .    ? 52.407  80.180  107.652 1.00 14.21  ? 6547 HOH A O     1 
HETATM 25080 O  O     . HOH H 5 .    ? 68.724  110.397 74.375  1.00 21.65  ? 6548 HOH A O     1 
HETATM 25081 O  O     . HOH H 5 .    ? 129.327 75.240  107.938 1.00 18.93  ? 6549 HOH A O     1 
HETATM 25082 O  O     . HOH H 5 .    ? 83.404  63.596  131.990 1.00 16.76  ? 6550 HOH A O     1 
HETATM 25083 O  O     . HOH H 5 .    ? 66.358  77.050  127.227 1.00 16.47  ? 6551 HOH A O     1 
HETATM 25084 O  O     . HOH H 5 .    ? 131.882 74.284  106.282 1.00 17.04  ? 6552 HOH A O     1 
HETATM 25085 O  O     . HOH H 5 .    ? 100.614 90.150  135.289 1.00 18.37  ? 6553 HOH A O     1 
HETATM 25086 O  O     . HOH H 5 .    ? 98.652  75.473  128.953 1.00 12.18  ? 6554 HOH A O     1 
HETATM 25087 O  O     . HOH H 5 .    ? 138.528 105.698 140.656 1.00 35.29  ? 6555 HOH A O     1 
HETATM 25088 O  O     . HOH H 5 .    ? 99.132  87.664  107.043 1.00 12.96  ? 6556 HOH A O     1 
HETATM 25089 O  O     . HOH H 5 .    ? 41.761  81.885  138.680 1.00 17.30  ? 6557 HOH A O     1 
HETATM 25090 O  O     . HOH H 5 .    ? 85.711  70.616  139.753 1.00 30.99  ? 6558 HOH A O     1 
HETATM 25091 O  O     . HOH H 5 .    ? 43.935  91.146  130.662 1.00 12.67  ? 6559 HOH A O     1 
HETATM 25092 O  O     . HOH H 5 .    ? 109.328 108.920 144.137 1.00 25.86  ? 6560 HOH A O     1 
HETATM 25093 O  O     . HOH H 5 .    ? 111.327 77.792  57.807  1.00 15.94  ? 6561 HOH A O     1 
HETATM 25094 O  O     . HOH H 5 .    ? 98.371  82.501  127.568 1.00 3.70   ? 6562 HOH A O     1 
HETATM 25095 O  O     . HOH H 5 .    ? 55.483  81.969  140.023 1.00 22.19  ? 6563 HOH A O     1 
HETATM 25096 O  O     . HOH H 5 .    ? 71.621  105.225 51.721  1.00 26.76  ? 6564 HOH A O     1 
HETATM 25097 O  O     . HOH H 5 .    ? 108.610 75.932  60.843  1.00 20.12  ? 6565 HOH A O     1 
HETATM 25098 O  O     . HOH H 5 .    ? 64.106  53.751  131.841 1.00 34.52  ? 6566 HOH A O     1 
HETATM 25099 O  O     . HOH H 5 .    ? 48.686  110.021 104.034 1.00 26.18  ? 6567 HOH A O     1 
HETATM 25100 O  O     . HOH H 5 .    ? 47.025  75.900  140.484 1.00 24.05  ? 6568 HOH A O     1 
HETATM 25101 O  O     . HOH H 5 .    ? 131.424 97.230  125.991 1.00 27.80  ? 6569 HOH A O     1 
HETATM 25102 O  O     . HOH H 5 .    ? 115.465 63.648  94.503  1.00 31.09  ? 6570 HOH A O     1 
HETATM 25103 O  O     . HOH H 5 .    ? 100.201 98.592  103.646 1.00 23.00  ? 6571 HOH A O     1 
HETATM 25104 O  O     . HOH H 5 .    ? 75.337  120.268 74.238  1.00 24.09  ? 6572 HOH A O     1 
HETATM 25105 O  O     . HOH H 5 .    ? 63.006  122.309 91.602  1.00 16.82  ? 6573 HOH A O     1 
HETATM 25106 O  O     . HOH H 5 .    ? 110.223 81.257  53.485  1.00 14.46  ? 6574 HOH A O     1 
HETATM 25107 O  O     . HOH H 5 .    ? 71.902  103.680 48.767  1.00 30.30  ? 6575 HOH A O     1 
HETATM 25108 O  O     . HOH H 5 .    ? 148.753 91.917  109.884 1.00 39.25  ? 6576 HOH A O     1 
HETATM 25109 O  O     . HOH H 5 .    ? 110.479 102.712 94.383  1.00 29.69  ? 6577 HOH A O     1 
HETATM 25110 O  O     . HOH H 5 .    ? 59.272  58.648  116.215 1.00 11.87  ? 6578 HOH A O     1 
HETATM 25111 O  O     . HOH H 5 .    ? 91.957  111.116 126.249 1.00 18.35  ? 6579 HOH A O     1 
HETATM 25112 O  O     . HOH H 5 .    ? 113.304 100.146 81.494  1.00 15.62  ? 6580 HOH A O     1 
HETATM 25113 O  O     . HOH H 5 .    ? 71.893  71.510  132.517 1.00 21.13  ? 6581 HOH A O     1 
HETATM 25114 O  O     . HOH H 5 .    ? 74.609  74.566  126.517 1.00 21.73  ? 6582 HOH A O     1 
HETATM 25115 O  O     . HOH H 5 .    ? 116.559 98.795  150.158 1.00 21.15  ? 6583 HOH A O     1 
HETATM 25116 O  O     . HOH H 5 .    ? 130.940 114.338 117.332 1.00 31.04  ? 6584 HOH A O     1 
HETATM 25117 O  O     . HOH H 5 .    ? 153.853 105.479 88.068  1.00 30.32  ? 6585 HOH A O     1 
HETATM 25118 O  O     . HOH H 5 .    ? 139.714 106.241 128.452 1.00 26.08  ? 6586 HOH A O     1 
HETATM 25119 O  O     . HOH H 5 .    ? 116.006 108.202 107.764 1.00 17.89  ? 6587 HOH A O     1 
HETATM 25120 O  O     . HOH H 5 .    ? 79.389  99.030  147.724 1.00 43.99  ? 6588 HOH A O     1 
HETATM 25121 O  O     . HOH H 5 .    ? 144.239 84.026  92.478  1.00 28.36  ? 6589 HOH A O     1 
HETATM 25122 O  O     . HOH H 5 .    ? 93.924  97.219  141.915 1.00 15.52  ? 6590 HOH A O     1 
HETATM 25123 O  O     . HOH H 5 .    ? 69.884  55.000  119.986 1.00 34.10  ? 6591 HOH A O     1 
HETATM 25124 O  O     . HOH H 5 .    ? 64.255  100.686 76.931  1.00 22.49  ? 6592 HOH A O     1 
HETATM 25125 O  O     . HOH H 5 .    ? 97.649  96.162  151.785 1.00 26.96  ? 6593 HOH A O     1 
HETATM 25126 O  O     . HOH H 5 .    ? 88.188  88.577  55.859  1.00 31.14  ? 6594 HOH A O     1 
HETATM 25127 O  O     . HOH H 5 .    ? 131.850 65.346  96.137  1.00 29.58  ? 6595 HOH A O     1 
HETATM 25128 O  O     . HOH H 5 .    ? 48.022  73.526  135.158 1.00 26.99  ? 6596 HOH A O     1 
HETATM 25129 O  O     . HOH H 5 .    ? 122.908 56.988  106.595 1.00 24.13  ? 6597 HOH A O     1 
HETATM 25130 O  O     . HOH H 5 .    ? 144.133 94.766  77.684  1.00 19.96  ? 6598 HOH A O     1 
HETATM 25131 O  O     . HOH H 5 .    ? 122.386 57.887  100.428 1.00 26.99  ? 6599 HOH A O     1 
HETATM 25132 O  O     . HOH H 5 .    ? 68.154  65.694  103.945 1.00 20.63  ? 6600 HOH A O     1 
HETATM 25133 O  O     . HOH H 5 .    ? 61.119  74.956  71.658  1.00 28.19  ? 6601 HOH A O     1 
HETATM 25134 O  O     . HOH H 5 .    ? 84.245  72.097  75.354  1.00 33.80  ? 6602 HOH A O     1 
HETATM 25135 O  O     . HOH H 5 .    ? 106.150 105.489 111.079 1.00 19.35  ? 6603 HOH A O     1 
HETATM 25136 O  O     . HOH H 5 .    ? 122.757 83.597  127.476 1.00 18.11  ? 6604 HOH A O     1 
HETATM 25137 O  O     . HOH H 5 .    ? 108.456 94.730  134.197 1.00 25.97  ? 6605 HOH A O     1 
HETATM 25138 O  O     . HOH H 5 .    ? 145.970 92.515  86.110  1.00 8.81   ? 6606 HOH A O     1 
HETATM 25139 O  O     . HOH H 5 .    ? 155.601 99.807  87.268  1.00 29.18  ? 6607 HOH A O     1 
HETATM 25140 O  O     . HOH H 5 .    ? 65.728  53.481  128.545 1.00 29.50  ? 6608 HOH A O     1 
HETATM 25141 O  O     . HOH H 5 .    ? 90.316  68.824  137.005 1.00 29.02  ? 6609 HOH A O     1 
HETATM 25142 O  O     . HOH H 5 .    ? 90.648  108.219 134.372 1.00 20.70  ? 6610 HOH A O     1 
HETATM 25143 O  O     . HOH H 5 .    ? 67.508  103.119 47.698  1.00 21.32  ? 6611 HOH A O     1 
HETATM 25144 O  O     . HOH H 5 .    ? 110.103 97.472  135.002 1.00 14.38  ? 6612 HOH A O     1 
HETATM 25145 O  O     . HOH H 5 .    ? 79.550  126.403 70.735  1.00 55.23  ? 6613 HOH A O     1 
HETATM 25146 O  O     . HOH H 5 .    ? 133.761 99.681  73.632  1.00 43.79  ? 6614 HOH A O     1 
HETATM 25147 O  O     . HOH H 5 .    ? 154.852 101.124 84.571  1.00 29.86  ? 6615 HOH A O     1 
HETATM 25148 O  O     . HOH H 5 .    ? 135.408 72.584  67.673  1.00 29.41  ? 6616 HOH A O     1 
HETATM 25149 O  O     . HOH H 5 .    ? 149.646 110.028 93.616  1.00 28.29  ? 6617 HOH A O     1 
HETATM 25150 O  O     . HOH H 5 .    ? 103.594 92.390  66.983  1.00 17.32  ? 6618 HOH A O     1 
HETATM 25151 O  O     . HOH H 5 .    ? 118.132 64.809  90.272  1.00 10.11  ? 6619 HOH A O     1 
HETATM 25152 O  O     . HOH H 5 .    ? 106.592 68.224  118.318 1.00 9.11   ? 6620 HOH A O     1 
HETATM 25153 O  O     . HOH H 5 .    ? 43.816  111.762 75.778  1.00 29.81  ? 6621 HOH A O     1 
HETATM 25154 O  O     . HOH H 5 .    ? 110.806 96.716  77.901  1.00 21.89  ? 6622 HOH A O     1 
HETATM 25155 O  O     . HOH H 5 .    ? 46.462  112.975 78.312  1.00 28.83  ? 6623 HOH A O     1 
HETATM 25156 O  O     . HOH H 5 .    ? 131.914 90.668  100.040 1.00 17.16  ? 6624 HOH A O     1 
HETATM 25157 O  O     . HOH H 5 .    ? 145.339 108.686 108.992 1.00 50.55  ? 6625 HOH A O     1 
HETATM 25158 O  O     . HOH H 5 .    ? 136.408 103.687 73.682  1.00 44.98  ? 6626 HOH A O     1 
HETATM 25159 O  O     . HOH H 5 .    ? 53.791  71.491  138.381 1.00 33.01  ? 6627 HOH A O     1 
HETATM 25160 O  O     . HOH H 5 .    ? 105.478 108.309 61.803  1.00 31.92  ? 6628 HOH A O     1 
HETATM 25161 O  O     . HOH H 5 .    ? 67.506  93.374  100.211 1.00 26.61  ? 6629 HOH A O     1 
HETATM 25162 O  O     . HOH H 5 .    ? 110.353 97.650  147.773 1.00 17.07  ? 6630 HOH A O     1 
HETATM 25163 O  O     . HOH H 5 .    ? 100.850 52.754  122.383 1.00 26.65  ? 6631 HOH A O     1 
HETATM 25164 O  O     . HOH H 5 .    ? 102.762 57.867  69.617  1.00 42.92  ? 6632 HOH A O     1 
HETATM 25165 O  O     . HOH H 5 .    ? 131.169 114.422 96.321  1.00 28.85  ? 6633 HOH A O     1 
HETATM 25166 O  O     . HOH H 5 .    ? 139.748 110.940 107.328 1.00 6.07   ? 6634 HOH A O     1 
HETATM 25167 O  O     . HOH H 5 .    ? 70.082  71.286  87.755  1.00 29.34  ? 6635 HOH A O     1 
HETATM 25168 O  O     . HOH H 5 .    ? 106.322 102.383 96.891  1.00 44.86  ? 6636 HOH A O     1 
HETATM 25169 O  O     . HOH H 5 .    ? 40.972  110.975 76.109  1.00 29.88  ? 6637 HOH A O     1 
HETATM 25170 O  O     . HOH H 5 .    ? 55.515  87.034  95.694  1.00 22.69  ? 6638 HOH A O     1 
HETATM 25171 O  O     . HOH H 5 .    ? 132.710 96.351  133.830 1.00 25.04  ? 6639 HOH A O     1 
HETATM 25172 O  O     . HOH H 5 .    ? 62.192  111.028 121.837 1.00 22.94  ? 6640 HOH A O     1 
HETATM 25173 O  O     . HOH H 5 .    ? 112.249 78.991  131.271 1.00 22.83  ? 6641 HOH A O     1 
HETATM 25174 O  O     . HOH H 5 .    ? 48.756  114.616 78.123  1.00 30.00  ? 6642 HOH A O     1 
HETATM 25175 O  O     . HOH H 5 .    ? 71.446  67.893  104.709 1.00 14.21  ? 6643 HOH A O     1 
HETATM 25176 O  O     . HOH H 5 .    ? 96.512  106.135 120.942 1.00 14.55  ? 6644 HOH A O     1 
HETATM 25177 O  O     . HOH H 5 .    ? 83.204  71.354  140.113 1.00 20.11  ? 6645 HOH A O     1 
HETATM 25178 O  O     . HOH H 5 .    ? 36.344  99.017  103.421 1.00 27.13  ? 6646 HOH A O     1 
HETATM 25179 O  O     . HOH H 5 .    ? 66.863  121.050 91.941  1.00 19.40  ? 6647 HOH A O     1 
HETATM 25180 O  O     . HOH H 5 .    ? 113.354 109.902 60.522  1.00 28.29  ? 6648 HOH A O     1 
HETATM 25181 O  O     . HOH H 5 .    ? 83.813  49.060  130.930 1.00 25.80  ? 6649 HOH A O     1 
HETATM 25182 O  O     . HOH H 5 .    ? 114.976 84.137  92.949  1.00 24.12  ? 6650 HOH A O     1 
HETATM 25183 O  O     . HOH H 5 .    ? 59.221  106.379 111.209 1.00 6.95   ? 6651 HOH A O     1 
HETATM 25184 O  O     . HOH H 5 .    ? 74.154  99.709  84.370  1.00 22.16  ? 6652 HOH A O     1 
HETATM 25185 O  O     . HOH H 5 .    ? 70.196  94.748  100.054 1.00 17.57  ? 6653 HOH A O     1 
HETATM 25186 O  O     . HOH H 5 .    ? 51.572  104.147 114.351 1.00 18.23  ? 6654 HOH A O     1 
HETATM 25187 O  O     . HOH H 5 .    ? 57.177  63.396  141.024 1.00 60.57  ? 6655 HOH A O     1 
HETATM 25188 O  O     . HOH H 5 .    ? 59.727  116.962 63.501  1.00 36.21  ? 6656 HOH A O     1 
HETATM 25189 O  O     . HOH H 5 .    ? 68.022  83.189  103.253 1.00 16.32  ? 6657 HOH A O     1 
# 
