data_9BN3
# 
_entry.id   9BN3 
# 
_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   9BN3         pdb_00009bn3 10.2210/pdb9bn3/pdb 
WWPDB D_1000283551 ?            ?                   
EMDB  EMD-44720    ?            ?                   
# 
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                        9BN3 
_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        'the alpha registry-locked dynein motor domain mutant in 5mM ATP condition, class1' 
_pdbx_database_related.db_id          EMD-44720 
_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' 533069.188 1 ? ? ? ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"           427.201    3 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"          507.181    1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytoplasmic dynein heavy chain 1,Dynein heavy chain,cytosolic' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDDGEDEAQRRRKG
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
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDDGEDEAQRRRKG
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 
# 
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 ASP n 
1 2390 GLY n 
1 2391 GLU n 
1 2392 ASP n 
1 2393 GLU n 
1 2394 ALA n 
1 2395 GLN n 
1 2396 ARG n 
1 2397 ARG n 
1 2398 ARG n 
1 2399 LYS n 
1 2400 GLY n 
1 2401 LYS n 
1 2402 GLU n 
1 2403 ASP n 
1 2404 GLU n 
1 2405 GLY n 
1 2406 GLU n 
1 2407 GLU n 
1 2408 ALA n 
1 2409 ALA n 
1 2410 SER n 
1 2411 PRO n 
1 2412 MET n 
1 2413 LEU n 
1 2414 GLN n 
1 2415 ILE n 
1 2416 GLN n 
1 2417 ARG n 
1 2418 ASP n 
1 2419 ALA n 
1 2420 ALA n 
1 2421 THR n 
1 2422 ILE n 
1 2423 MET n 
1 2424 GLN n 
1 2425 PRO n 
1 2426 TYR n 
1 2427 PHE n 
1 2428 THR n 
1 2429 SER n 
1 2430 ASN n 
1 2431 GLY n 
1 2432 LEU n 
1 2433 VAL n 
1 2434 THR n 
1 2435 LYS n 
1 2436 ALA n 
1 2437 LEU n 
1 2438 GLU n 
1 2439 HIS n 
1 2440 ALA n 
1 2441 PHE n 
1 2442 GLN n 
1 2443 LEU n 
1 2444 GLU n 
1 2445 HIS n 
1 2446 ILE n 
1 2447 MET n 
1 2448 ASP n 
1 2449 LEU n 
1 2450 THR n 
1 2451 ARG n 
1 2452 LEU n 
1 2453 ARG n 
1 2454 CYS n 
1 2455 LEU n 
1 2456 GLY n 
1 2457 SER n 
1 2458 LEU n 
1 2459 PHE n 
1 2460 SER n 
1 2461 MET n 
1 2462 LEU n 
1 2463 HIS n 
1 2464 GLN n 
1 2465 ALA n 
1 2466 CYS n 
1 2467 ARG n 
1 2468 ASN n 
1 2469 VAL n 
1 2470 ALA n 
1 2471 GLN n 
1 2472 TYR n 
1 2473 ASN n 
1 2474 ALA n 
1 2475 ASN n 
1 2476 HIS n 
1 2477 PRO n 
1 2478 ASP n 
1 2479 PHE n 
1 2480 PRO n 
1 2481 MET n 
1 2482 GLN n 
1 2483 ILE n 
1 2484 GLU n 
1 2485 GLN n 
1 2486 LEU n 
1 2487 GLU n 
1 2488 ARG n 
1 2489 TYR n 
1 2490 ILE n 
1 2491 GLN n 
1 2492 ARG n 
1 2493 TYR n 
1 2494 LEU n 
1 2495 VAL n 
1 2496 TYR n 
1 2497 ALA n 
1 2498 ILE n 
1 2499 LEU n 
1 2500 TRP n 
1 2501 SER n 
1 2502 LEU n 
1 2503 SER n 
1 2504 GLY n 
1 2505 ASP n 
1 2506 SER n 
1 2507 ARG n 
1 2508 LEU n 
1 2509 LYS n 
1 2510 MET n 
1 2511 ARG n 
1 2512 ALA n 
1 2513 GLU n 
1 2514 LEU n 
1 2515 GLY n 
1 2516 GLU n 
1 2517 TYR n 
1 2518 ILE n 
1 2519 ARG n 
1 2520 ARG n 
1 2521 ILE n 
1 2522 THR n 
1 2523 THR n 
1 2524 VAL n 
1 2525 PRO n 
1 2526 LEU n 
1 2527 PRO n 
1 2528 THR n 
1 2529 ALA n 
1 2530 PRO n 
1 2531 ASN n 
1 2532 ILE n 
1 2533 PRO n 
1 2534 ILE n 
1 2535 ILE n 
1 2536 ASP n 
1 2537 TYR n 
1 2538 GLU n 
1 2539 VAL n 
1 2540 SER n 
1 2541 ILE n 
1 2542 SER n 
1 2543 GLY n 
1 2544 GLU n 
1 2545 TRP n 
1 2546 SER n 
1 2547 PRO n 
1 2548 TRP n 
1 2549 GLN n 
1 2550 ALA n 
1 2551 LYS n 
1 2552 VAL n 
1 2553 PRO n 
1 2554 GLN n 
1 2555 ILE n 
1 2556 GLU n 
1 2557 VAL n 
1 2558 GLU n 
1 2559 THR n 
1 2560 HIS n 
1 2561 LYS n 
1 2562 VAL n 
1 2563 ALA n 
1 2564 ALA n 
1 2565 PRO n 
1 2566 ASP n 
1 2567 VAL n 
1 2568 VAL n 
1 2569 VAL n 
1 2570 PRO n 
1 2571 THR n 
1 2572 LEU n 
1 2573 ASP n 
1 2574 THR n 
1 2575 VAL n 
1 2576 ARG n 
1 2577 HIS n 
1 2578 GLU n 
1 2579 ALA n 
1 2580 LEU n 
1 2581 LEU n 
1 2582 TYR n 
1 2583 THR n 
1 2584 TRP n 
1 2585 LEU n 
1 2586 ALA n 
1 2587 GLU n 
1 2588 HIS n 
1 2589 LYS n 
1 2590 PRO n 
1 2591 LEU n 
1 2592 VAL n 
1 2593 LEU n 
1 2594 CYS n 
1 2595 GLY n 
1 2596 PRO n 
1 2597 PRO n 
1 2598 GLY n 
1 2599 SER n 
1 2600 GLY n 
1 2601 LYS n 
1 2602 THR n 
1 2603 MET n 
1 2604 THR n 
1 2605 LEU n 
1 2606 PHE n 
1 2607 SER n 
1 2608 ALA n 
1 2609 LEU n 
1 2610 ARG n 
1 2611 ALA n 
1 2612 LEU n 
1 2613 PRO n 
1 2614 ASP n 
1 2615 MET n 
1 2616 GLU n 
1 2617 VAL n 
1 2618 VAL n 
1 2619 GLY n 
1 2620 LEU n 
1 2621 ASN n 
1 2622 PHE n 
1 2623 SER n 
1 2624 SER n 
1 2625 ALA n 
1 2626 THR n 
1 2627 THR n 
1 2628 PRO n 
1 2629 GLU n 
1 2630 LEU n 
1 2631 LEU n 
1 2632 LEU n 
1 2633 LYS n 
1 2634 THR n 
1 2635 PHE n 
1 2636 ASP n 
1 2637 HIS n 
1 2638 TYR n 
1 2639 CYS n 
1 2640 GLU n 
1 2641 TYR n 
1 2642 ARG n 
1 2643 ARG n 
1 2644 THR n 
1 2645 PRO n 
1 2646 ASN n 
1 2647 GLY n 
1 2648 VAL n 
1 2649 VAL n 
1 2650 LEU n 
1 2651 ALA n 
1 2652 PRO n 
1 2653 VAL n 
1 2654 GLN n 
1 2655 LEU n 
1 2656 GLY n 
1 2657 LYS n 
1 2658 TRP n 
1 2659 LEU n 
1 2660 VAL n 
1 2661 LEU n 
1 2662 PHE n 
1 2663 CYS n 
1 2664 ASP n 
1 2665 GLU n 
1 2666 ILE n 
1 2667 ASN n 
1 2668 LEU n 
1 2669 PRO n 
1 2670 ASP n 
1 2671 MET n 
1 2672 ASP n 
1 2673 LYS n 
1 2674 TYR n 
1 2675 GLY n 
1 2676 THR n 
1 2677 GLN n 
1 2678 ARG n 
1 2679 VAL n 
1 2680 ILE n 
1 2681 SER n 
1 2682 PHE n 
1 2683 ILE n 
1 2684 ARG n 
1 2685 GLN n 
1 2686 MET n 
1 2687 VAL n 
1 2688 GLU n 
1 2689 HIS n 
1 2690 GLY n 
1 2691 GLY n 
1 2692 PHE n 
1 2693 TYR n 
1 2694 ARG n 
1 2695 THR n 
1 2696 SER n 
1 2697 ASP n 
1 2698 GLN n 
1 2699 THR n 
1 2700 TRP n 
1 2701 VAL n 
1 2702 LYS n 
1 2703 LEU n 
1 2704 GLU n 
1 2705 ARG n 
1 2706 ILE n 
1 2707 GLN n 
1 2708 PHE n 
1 2709 VAL n 
1 2710 GLY n 
1 2711 ALA n 
1 2712 CYS n 
1 2713 ASN n 
1 2714 PRO n 
1 2715 PRO n 
1 2716 THR n 
1 2717 ASP n 
1 2718 PRO n 
1 2719 GLY n 
1 2720 ARG n 
1 2721 LYS n 
1 2722 PRO n 
1 2723 LEU n 
1 2724 SER n 
1 2725 HIS n 
1 2726 ARG n 
1 2727 PHE n 
1 2728 LEU n 
1 2729 ARG n 
1 2730 HIS n 
1 2731 VAL n 
1 2732 PRO n 
1 2733 VAL n 
1 2734 VAL n 
1 2735 TYR n 
1 2736 VAL n 
1 2737 ASP n 
1 2738 TYR n 
1 2739 PRO n 
1 2740 GLY n 
1 2741 PRO n 
1 2742 ALA n 
1 2743 SER n 
1 2744 LEU n 
1 2745 THR n 
1 2746 GLN n 
1 2747 ILE n 
1 2748 TYR n 
1 2749 GLY n 
1 2750 THR n 
1 2751 PHE n 
1 2752 ASN n 
1 2753 ARG n 
1 2754 ALA n 
1 2755 MET n 
1 2756 LEU n 
1 2757 ARG n 
1 2758 LEU n 
1 2759 ILE n 
1 2760 PRO n 
1 2761 SER n 
1 2762 LEU n 
1 2763 ARG n 
1 2764 THR n 
1 2765 TYR n 
1 2766 ALA n 
1 2767 GLU n 
1 2768 PRO n 
1 2769 LEU n 
1 2770 THR n 
1 2771 ALA n 
1 2772 ALA n 
1 2773 MET n 
1 2774 VAL n 
1 2775 GLU n 
1 2776 PHE n 
1 2777 TYR n 
1 2778 THR n 
1 2779 MET n 
1 2780 SER n 
1 2781 GLN n 
1 2782 GLU n 
1 2783 ARG n 
1 2784 PHE n 
1 2785 THR n 
1 2786 GLN n 
1 2787 ASP n 
1 2788 THR n 
1 2789 GLN n 
1 2790 PRO n 
1 2791 HIS n 
1 2792 TYR n 
1 2793 ILE n 
1 2794 TYR n 
1 2795 SER n 
1 2796 PRO n 
1 2797 ARG n 
1 2798 GLU n 
1 2799 MET n 
1 2800 THR n 
1 2801 ARG n 
1 2802 TRP n 
1 2803 VAL n 
1 2804 ARG n 
1 2805 GLY n 
1 2806 ILE n 
1 2807 PHE n 
1 2808 GLU n 
1 2809 ALA n 
1 2810 LEU n 
1 2811 ARG n 
1 2812 PRO n 
1 2813 LEU n 
1 2814 GLU n 
1 2815 THR n 
1 2816 LEU n 
1 2817 PRO n 
1 2818 VAL n 
1 2819 GLU n 
1 2820 GLY n 
1 2821 LEU n 
1 2822 ILE n 
1 2823 ARG n 
1 2824 ILE n 
1 2825 TRP n 
1 2826 ALA n 
1 2827 HIS n 
1 2828 GLU n 
1 2829 ALA n 
1 2830 LEU n 
1 2831 ARG n 
1 2832 LEU n 
1 2833 PHE n 
1 2834 GLN n 
1 2835 ASP n 
1 2836 ARG n 
1 2837 LEU n 
1 2838 VAL n 
1 2839 GLU n 
1 2840 ASP n 
1 2841 GLU n 
1 2842 GLU n 
1 2843 ARG n 
1 2844 ARG n 
1 2845 TRP n 
1 2846 THR n 
1 2847 ASP n 
1 2848 GLU n 
1 2849 ASN n 
1 2850 ILE n 
1 2851 ASP n 
1 2852 THR n 
1 2853 VAL n 
1 2854 ALA n 
1 2855 LEU n 
1 2856 LYS n 
1 2857 HIS n 
1 2858 PHE n 
1 2859 PRO n 
1 2860 ASN n 
1 2861 ILE n 
1 2862 ASP n 
1 2863 ARG n 
1 2864 GLU n 
1 2865 LYS n 
1 2866 ALA n 
1 2867 MET n 
1 2868 SER n 
1 2869 ARG n 
1 2870 PRO n 
1 2871 ILE n 
1 2872 LEU n 
1 2873 TYR n 
1 2874 SER n 
1 2875 ASN n 
1 2876 TRP n 
1 2877 LEU n 
1 2878 SER n 
1 2879 LYS n 
1 2880 ASP n 
1 2881 TYR n 
1 2882 ILE n 
1 2883 PRO n 
1 2884 VAL n 
1 2885 ASP n 
1 2886 GLN n 
1 2887 GLU n 
1 2888 GLU n 
1 2889 LEU n 
1 2890 ARG n 
1 2891 ASP n 
1 2892 TYR n 
1 2893 VAL n 
1 2894 LYS n 
1 2895 ALA n 
1 2896 ARG n 
1 2897 LEU n 
1 2898 LYS n 
1 2899 VAL n 
1 2900 PHE n 
1 2901 TYR n 
1 2902 GLU n 
1 2903 GLU n 
1 2904 GLU n 
1 2905 LEU n 
1 2906 ASP n 
1 2907 VAL n 
1 2908 PRO n 
1 2909 LEU n 
1 2910 VAL n 
1 2911 LEU n 
1 2912 PHE n 
1 2913 ASN n 
1 2914 GLU n 
1 2915 VAL n 
1 2916 LEU n 
1 2917 ASP n 
1 2918 HIS n 
1 2919 VAL n 
1 2920 LEU n 
1 2921 ARG n 
1 2922 ILE n 
1 2923 ASP n 
1 2924 ARG n 
1 2925 ILE n 
1 2926 PHE n 
1 2927 ARG n 
1 2928 GLN n 
1 2929 PRO n 
1 2930 GLN n 
1 2931 GLY n 
1 2932 HIS n 
1 2933 LEU n 
1 2934 LEU n 
1 2935 LEU n 
1 2936 ILE n 
1 2937 GLY n 
1 2938 VAL n 
1 2939 SER n 
1 2940 GLY n 
1 2941 ALA n 
1 2942 GLY n 
1 2943 LYS n 
1 2944 THR n 
1 2945 THR n 
1 2946 LEU n 
1 2947 SER n 
1 2948 ARG n 
1 2949 PHE n 
1 2950 VAL n 
1 2951 ALA n 
1 2952 TRP n 
1 2953 MET n 
1 2954 ASN n 
1 2955 GLY n 
1 2956 LEU n 
1 2957 SER n 
1 2958 VAL n 
1 2959 TYR n 
1 2960 GLN n 
1 2961 ILE n 
1 2962 LYS n 
1 2963 VAL n 
1 2964 HIS n 
1 2965 ARG n 
1 2966 LYS n 
1 2967 TYR n 
1 2968 THR n 
1 2969 GLY n 
1 2970 GLU n 
1 2971 ASP n 
1 2972 PHE n 
1 2973 ASP n 
1 2974 GLU n 
1 2975 ASP n 
1 2976 LEU n 
1 2977 ARG n 
1 2978 THR n 
1 2979 VAL n 
1 2980 LEU n 
1 2981 ARG n 
1 2982 ARG n 
1 2983 SER n 
1 2984 GLY n 
1 2985 CYS n 
1 2986 LYS n 
1 2987 ASN n 
1 2988 GLU n 
1 2989 LYS n 
1 2990 ILE n 
1 2991 ALA n 
1 2992 PHE n 
1 2993 ILE n 
1 2994 MET n 
1 2995 ASP n 
1 2996 GLU n 
1 2997 SER n 
1 2998 ASN n 
1 2999 VAL n 
1 3000 LEU n 
1 3001 ASP n 
1 3002 SER n 
1 3003 GLY n 
1 3004 PHE n 
1 3005 LEU n 
1 3006 GLU n 
1 3007 ARG n 
1 3008 MET n 
1 3009 ASN n 
1 3010 THR n 
1 3011 LEU n 
1 3012 LEU n 
1 3013 ALA n 
1 3014 ASN n 
1 3015 GLY n 
1 3016 GLU n 
1 3017 VAL n 
1 3018 PRO n 
1 3019 GLY n 
1 3020 LEU n 
1 3021 PHE n 
1 3022 GLU n 
1 3023 GLY n 
1 3024 ASP n 
1 3025 GLU n 
1 3026 TYR n 
1 3027 ALA n 
1 3028 THR n 
1 3029 LEU n 
1 3030 MET n 
1 3031 THR n 
1 3032 GLN n 
1 3033 CYS n 
1 3034 LYS n 
1 3035 GLU n 
1 3036 GLY n 
1 3037 ALA n 
1 3038 GLN n 
1 3039 LYS n 
1 3040 GLU n 
1 3041 GLY n 
1 3042 LEU n 
1 3043 MET n 
1 3044 LEU n 
1 3045 ASP n 
1 3046 SER n 
1 3047 HIS n 
1 3048 GLU n 
1 3049 GLU n 
1 3050 LEU n 
1 3051 TYR n 
1 3052 LYS n 
1 3053 TRP n 
1 3054 PHE n 
1 3055 THR n 
1 3056 SER n 
1 3057 GLN n 
1 3058 VAL n 
1 3059 ILE n 
1 3060 ARG n 
1 3061 ASN n 
1 3062 LEU n 
1 3063 HIS n 
1 3064 VAL n 
1 3065 VAL n 
1 3066 PHE n 
1 3067 THR n 
1 3068 MET n 
1 3069 ASN n 
1 3070 PRO n 
1 3071 SER n 
1 3072 SER n 
1 3073 GLU n 
1 3074 GLY n 
1 3075 LEU n 
1 3076 LYS n 
1 3077 ASP n 
1 3078 ARG n 
1 3079 ALA n 
1 3080 ALA n 
1 3081 THR n 
1 3082 SER n 
1 3083 PRO n 
1 3084 ALA n 
1 3085 LEU n 
1 3086 PHE n 
1 3087 ASN n 
1 3088 ARG n 
1 3089 CYS n 
1 3090 VAL n 
1 3091 LEU n 
1 3092 ASN n 
1 3093 TRP n 
1 3094 PHE n 
1 3095 GLY n 
1 3096 ASP n 
1 3097 TRP n 
1 3098 SER n 
1 3099 THR n 
1 3100 GLU n 
1 3101 ALA n 
1 3102 LEU n 
1 3103 TYR n 
1 3104 GLN n 
1 3105 VAL n 
1 3106 GLY n 
1 3107 LYS n 
1 3108 GLU n 
1 3109 PHE n 
1 3110 THR n 
1 3111 SER n 
1 3112 LYS n 
1 3113 MET n 
1 3114 ASP n 
1 3115 LEU n 
1 3116 GLU n 
1 3117 LYS n 
1 3118 PRO n 
1 3119 ASN n 
1 3120 TYR n 
1 3121 ILE n 
1 3122 VAL n 
1 3123 PRO n 
1 3124 ASP n 
1 3125 TYR n 
1 3126 MET n 
1 3127 PRO n 
1 3128 VAL n 
1 3129 VAL n 
1 3130 TYR n 
1 3131 ASP n 
1 3132 LYS n 
1 3133 LEU n 
1 3134 PRO n 
1 3135 GLN n 
1 3136 PRO n 
1 3137 PRO n 
1 3138 SER n 
1 3139 HIS n 
1 3140 ARG n 
1 3141 GLU n 
1 3142 ALA n 
1 3143 ILE n 
1 3144 VAL n 
1 3145 ASN n 
1 3146 SER n 
1 3147 CYS n 
1 3148 VAL n 
1 3149 PHE n 
1 3150 VAL n 
1 3151 HIS n 
1 3152 GLN n 
1 3153 THR n 
1 3154 LEU n 
1 3155 HIS n 
1 3156 GLN n 
1 3157 ALA n 
1 3158 ASN n 
1 3159 ALA n 
1 3160 ARG n 
1 3161 LEU n 
1 3162 ALA n 
1 3163 LYS n 
1 3164 ARG n 
1 3165 GLY n 
1 3166 GLY n 
1 3167 ARG n 
1 3168 THR n 
1 3169 MET n 
1 3170 ALA n 
1 3171 ILE n 
1 3172 THR n 
1 3173 PRO n 
1 3174 ARG n 
1 3175 HIS n 
1 3176 TYR n 
1 3177 LEU n 
1 3178 ASP n 
1 3179 PHE n 
1 3180 ILE n 
1 3181 ASN n 
1 3182 HIS n 
1 3183 TYR n 
1 3184 ALA n 
1 3185 ASN n 
1 3186 LEU n 
1 3187 PHE n 
1 3188 HIS n 
1 3189 GLU n 
1 3190 LYS n 
1 3191 ARG n 
1 3192 SER n 
1 3193 GLU n 
1 3194 LEU n 
1 3195 GLU n 
1 3196 GLU n 
1 3197 GLN n 
1 3198 GLN n 
1 3199 MET n 
1 3200 HIS n 
1 3201 LEU n 
1 3202 ASN n 
1 3203 VAL n 
1 3204 GLY n 
1 3205 LEU n 
1 3206 ARG n 
1 3207 LYS n 
1 3208 ILE n 
1 3209 LYS n 
1 3210 GLU n 
1 3211 THR n 
1 3212 VAL n 
1 3213 ASP n 
1 3214 GLN n 
1 3215 VAL n 
1 3216 GLU n 
1 3217 GLU n 
1 3218 LEU n 
1 3219 ARG n 
1 3220 ARG n 
1 3221 ASP n 
1 3222 LEU n 
1 3223 ARG n 
1 3224 ILE n 
1 3225 LYS n 
1 3226 SER n 
1 3227 GLN n 
1 3228 GLU n 
1 3229 LEU n 
1 3230 GLU n 
1 3231 VAL n 
1 3232 LYS n 
1 3233 ASN n 
1 3234 ALA n 
1 3235 ALA n 
1 3236 ALA n 
1 3237 ASN n 
1 3238 ASP n 
1 3239 LYS n 
1 3240 LEU n 
1 3241 LYS n 
1 3242 LYS n 
1 3243 MET n 
1 3244 VAL n 
1 3245 LYS n 
1 3246 ASP n 
1 3247 GLN n 
1 3248 GLN n 
1 3249 GLU n 
1 3250 ALA n 
1 3251 GLU n 
1 3252 LYS n 
1 3253 LYS n 
1 3254 LYS n 
1 3255 VAL n 
1 3256 MET n 
1 3257 SER n 
1 3258 GLN n 
1 3259 GLU n 
1 3260 ILE n 
1 3261 GLN n 
1 3262 GLU n 
1 3263 GLN n 
1 3264 LEU n 
1 3265 HIS n 
1 3266 LYS n 
1 3267 GLN n 
1 3268 GLN n 
1 3269 GLU n 
1 3270 VAL n 
1 3271 ILE n 
1 3272 ALA n 
1 3273 ASP n 
1 3274 LYS n 
1 3275 GLN n 
1 3276 MET n 
1 3277 SER n 
1 3278 VAL n 
1 3279 LYS n 
1 3280 GLU n 
1 3281 ASP n 
1 3282 LEU n 
1 3283 ASP n 
1 3284 LYS n 
1 3285 VAL n 
1 3286 GLU n 
1 3287 PRO n 
1 3288 ALA n 
1 3289 VAL n 
1 3290 ILE n 
1 3291 GLU n 
1 3292 ALA n 
1 3293 GLN n 
1 3294 ASN n 
1 3295 ALA n 
1 3296 VAL n 
1 3297 LYS n 
1 3298 SER n 
1 3299 ILE n 
1 3300 LYS n 
1 3301 LYS n 
1 3302 GLN n 
1 3303 HIS n 
1 3304 LEU n 
1 3305 VAL n 
1 3306 GLU n 
1 3307 VAL n 
1 3308 ARG n 
1 3309 SER n 
1 3310 MET n 
1 3311 ALA n 
1 3312 ASN n 
1 3313 PRO n 
1 3314 PRO n 
1 3315 ALA n 
1 3316 ALA n 
1 3317 VAL n 
1 3318 LYS n 
1 3319 LEU n 
1 3320 ALA n 
1 3321 LEU n 
1 3322 GLU n 
1 3323 SER n 
1 3324 ILE n 
1 3325 CYS n 
1 3326 LEU n 
1 3327 LEU n 
1 3328 LEU n 
1 3329 GLY n 
1 3330 GLU n 
1 3331 SER n 
1 3332 THR n 
1 3333 THR n 
1 3334 ASP n 
1 3335 TRP n 
1 3336 LYS n 
1 3337 GLN n 
1 3338 ILE n 
1 3339 ARG n 
1 3340 SER n 
1 3341 ILE n 
1 3342 ILE n 
1 3343 MET n 
1 3344 ARG n 
1 3345 GLU n 
1 3346 ASN n 
1 3347 PHE n 
1 3348 ILE n 
1 3349 PRO n 
1 3350 THR n 
1 3351 ILE n 
1 3352 VAL n 
1 3353 ASN n 
1 3354 PHE n 
1 3355 SER n 
1 3356 ALA n 
1 3357 GLU n 
1 3358 GLU n 
1 3359 ILE n 
1 3360 SER n 
1 3361 ASP n 
1 3362 ALA n 
1 3363 ILE n 
1 3364 ARG n 
1 3365 GLU n 
1 3366 LYS n 
1 3367 MET n 
1 3368 LYS n 
1 3369 LYS n 
1 3370 ASN n 
1 3371 TYR n 
1 3372 MET n 
1 3373 SER n 
1 3374 ASN n 
1 3375 PRO n 
1 3376 SER n 
1 3377 TYR n 
1 3378 ASN n 
1 3379 TYR n 
1 3380 GLU n 
1 3381 ILE n 
1 3382 VAL n 
1 3383 ASN n 
1 3384 ARG n 
1 3385 ALA n 
1 3386 SER n 
1 3387 LEU n 
1 3388 ALA n 
1 3389 CYS n 
1 3390 GLY n 
1 3391 PRO n 
1 3392 MET n 
1 3393 VAL n 
1 3394 LYS n 
1 3395 TRP n 
1 3396 ALA n 
1 3397 ILE n 
1 3398 ALA n 
1 3399 GLN n 
1 3400 LEU n 
1 3401 ASN n 
1 3402 TYR n 
1 3403 ALA n 
1 3404 ASP n 
1 3405 MET n 
1 3406 LEU n 
1 3407 LYS n 
1 3408 ARG n 
1 3409 VAL n 
1 3410 GLU n 
1 3411 PRO n 
1 3412 LEU n 
1 3413 ARG n 
1 3414 ASN n 
1 3415 GLU n 
1 3416 LEU n 
1 3417 GLN n 
1 3418 LYS n 
1 3419 LEU n 
1 3420 GLU n 
1 3421 ASP n 
1 3422 ASP n 
1 3423 ALA n 
1 3424 LYS n 
1 3425 ASP n 
1 3426 ASN n 
1 3427 GLN n 
1 3428 GLN n 
1 3429 LYS n 
1 3430 ALA n 
1 3431 ASN n 
1 3432 GLU n 
1 3433 VAL n 
1 3434 GLU n 
1 3435 GLN n 
1 3436 MET n 
1 3437 ILE n 
1 3438 ARG n 
1 3439 ASP n 
1 3440 LEU n 
1 3441 GLU n 
1 3442 ALA n 
1 3443 SER n 
1 3444 ILE n 
1 3445 ALA n 
1 3446 ARG n 
1 3447 TYR n 
1 3448 LYS n 
1 3449 GLU n 
1 3450 GLU n 
1 3451 TYR n 
1 3452 ALA n 
1 3453 VAL n 
1 3454 LEU n 
1 3455 ILE n 
1 3456 SER n 
1 3457 GLU n 
1 3458 ALA n 
1 3459 GLN n 
1 3460 ALA n 
1 3461 ILE n 
1 3462 LYS n 
1 3463 ALA n 
1 3464 ASP n 
1 3465 LEU n 
1 3466 ALA n 
1 3467 ALA n 
1 3468 VAL n 
1 3469 GLU n 
1 3470 ALA n 
1 3471 LYS n 
1 3472 VAL n 
1 3473 ASN n 
1 3474 ARG n 
1 3475 SER n 
1 3476 THR n 
1 3477 ALA n 
1 3478 LEU n 
1 3479 LEU n 
1 3480 LYS n 
1 3481 SER n 
1 3482 LEU n 
1 3483 SER n 
1 3484 ALA n 
1 3485 GLU n 
1 3486 ARG n 
1 3487 GLU n 
1 3488 ARG n 
1 3489 TRP n 
1 3490 GLU n 
1 3491 LYS n 
1 3492 THR n 
1 3493 SER n 
1 3494 GLU n 
1 3495 THR n 
1 3496 PHE n 
1 3497 LYS n 
1 3498 ASN n 
1 3499 GLN n 
1 3500 MET n 
1 3501 SER n 
1 3502 THR n 
1 3503 ILE n 
1 3504 ALA n 
1 3505 GLY n 
1 3506 ASP n 
1 3507 CYS n 
1 3508 LEU n 
1 3509 LEU n 
1 3510 SER n 
1 3511 ALA n 
1 3512 ALA n 
1 3513 PHE n 
1 3514 ILE n 
1 3515 ALA n 
1 3516 TYR n 
1 3517 ALA n 
1 3518 GLY n 
1 3519 TYR n 
1 3520 PHE n 
1 3521 ASP n 
1 3522 GLN n 
1 3523 GLN n 
1 3524 MET n 
1 3525 ARG n 
1 3526 GLN n 
1 3527 ASN n 
1 3528 LEU n 
1 3529 PHE n 
1 3530 THR n 
1 3531 THR n 
1 3532 TRP n 
1 3533 SER n 
1 3534 HIS n 
1 3535 HIS n 
1 3536 LEU n 
1 3537 GLN n 
1 3538 GLN n 
1 3539 ALA n 
1 3540 ASN n 
1 3541 ILE n 
1 3542 GLN n 
1 3543 PHE n 
1 3544 ARG n 
1 3545 THR n 
1 3546 ASP n 
1 3547 ILE n 
1 3548 ALA n 
1 3549 ARG n 
1 3550 THR n 
1 3551 GLU n 
1 3552 TYR n 
1 3553 LEU n 
1 3554 SER n 
1 3555 ASN n 
1 3556 ALA n 
1 3557 ASP n 
1 3558 GLU n 
1 3559 ARG n 
1 3560 LEU n 
1 3561 ARG n 
1 3562 TRP n 
1 3563 GLN n 
1 3564 ALA n 
1 3565 SER n 
1 3566 SER n 
1 3567 LEU n 
1 3568 PRO n 
1 3569 ALA n 
1 3570 ASP n 
1 3571 ASP n 
1 3572 LEU n 
1 3573 CYS n 
1 3574 THR n 
1 3575 GLU n 
1 3576 ASN n 
1 3577 ALA n 
1 3578 ILE n 
1 3579 MET n 
1 3580 LEU n 
1 3581 LYS n 
1 3582 ARG n 
1 3583 PHE n 
1 3584 ASN n 
1 3585 ARG n 
1 3586 TYR n 
1 3587 PRO n 
1 3588 LEU n 
1 3589 ILE n 
1 3590 ILE n 
1 3591 ASP n 
1 3592 PRO n 
1 3593 SER n 
1 3594 GLY n 
1 3595 GLN n 
1 3596 ALA n 
1 3597 THR n 
1 3598 GLU n 
1 3599 PHE n 
1 3600 ILE n 
1 3601 MET n 
1 3602 ASN n 
1 3603 GLU n 
1 3604 TYR n 
1 3605 LYS n 
1 3606 ASP n 
1 3607 ARG n 
1 3608 LYS n 
1 3609 ILE n 
1 3610 THR n 
1 3611 ARG n 
1 3612 THR n 
1 3613 SER n 
1 3614 PHE n 
1 3615 LEU n 
1 3616 ASP n 
1 3617 ASP n 
1 3618 ALA n 
1 3619 PHE n 
1 3620 ARG n 
1 3621 LYS n 
1 3622 ASN n 
1 3623 LEU n 
1 3624 GLU n 
1 3625 SER n 
1 3626 ALA n 
1 3627 LEU n 
1 3628 ARG n 
1 3629 PHE n 
1 3630 GLY n 
1 3631 ASN n 
1 3632 PRO n 
1 3633 LEU n 
1 3634 LEU n 
1 3635 VAL n 
1 3636 GLN n 
1 3637 ASP n 
1 3638 VAL n 
1 3639 GLU n 
1 3640 SER n 
1 3641 TYR n 
1 3642 ASP n 
1 3643 PRO n 
1 3644 VAL n 
1 3645 LEU n 
1 3646 ASN n 
1 3647 PRO n 
1 3648 VAL n 
1 3649 LEU n 
1 3650 ASN n 
1 3651 ARG n 
1 3652 GLU n 
1 3653 VAL n 
1 3654 ARG n 
1 3655 ARG n 
1 3656 THR n 
1 3657 GLY n 
1 3658 GLY n 
1 3659 ARG n 
1 3660 VAL n 
1 3661 LEU n 
1 3662 ILE n 
1 3663 THR n 
1 3664 LEU n 
1 3665 GLY n 
1 3666 ASP n 
1 3667 GLN n 
1 3668 ASP n 
1 3669 ILE n 
1 3670 ASP n 
1 3671 LEU n 
1 3672 SER n 
1 3673 PRO n 
1 3674 SER n 
1 3675 PHE n 
1 3676 VAL n 
1 3677 ILE n 
1 3678 PHE n 
1 3679 LEU n 
1 3680 SER n 
1 3681 THR n 
1 3682 ARG n 
1 3683 ASP n 
1 3684 PRO n 
1 3685 THR n 
1 3686 VAL n 
1 3687 GLU n 
1 3688 PHE n 
1 3689 PRO n 
1 3690 PRO n 
1 3691 ASP n 
1 3692 LEU n 
1 3693 CYS n 
1 3694 SER n 
1 3695 ARG n 
1 3696 VAL n 
1 3697 THR n 
1 3698 PHE n 
1 3699 VAL n 
1 3700 ASN n 
1 3701 PHE n 
1 3702 THR n 
1 3703 VAL n 
1 3704 THR n 
1 3705 ARG n 
1 3706 SER n 
1 3707 SER n 
1 3708 LEU n 
1 3709 GLN n 
1 3710 SER n 
1 3711 GLN n 
1 3712 CYS n 
1 3713 LEU n 
1 3714 ASN n 
1 3715 GLU n 
1 3716 VAL n 
1 3717 LEU n 
1 3718 LYS n 
1 3719 ALA n 
1 3720 GLU n 
1 3721 ARG n 
1 3722 PRO n 
1 3723 ASP n 
1 3724 VAL n 
1 3725 ASP n 
1 3726 GLU n 
1 3727 LYS n 
1 3728 ARG n 
1 3729 SER n 
1 3730 ASP n 
1 3731 LEU n 
1 3732 LEU n 
1 3733 LYS n 
1 3734 LEU n 
1 3735 GLN n 
1 3736 GLY n 
1 3737 GLU n 
1 3738 PHE n 
1 3739 GLN n 
1 3740 LEU n 
1 3741 ARG n 
1 3742 LEU n 
1 3743 ARG n 
1 3744 GLN n 
1 3745 LEU n 
1 3746 GLU n 
1 3747 LYS n 
1 3748 SER n 
1 3749 LEU n 
1 3750 LEU n 
1 3751 GLN n 
1 3752 ALA n 
1 3753 LEU n 
1 3754 ASN n 
1 3755 GLU n 
1 3756 VAL n 
1 3757 LYS n 
1 3758 GLY n 
1 3759 ARG n 
1 3760 ILE n 
1 3761 LEU n 
1 3762 ASP n 
1 3763 ASP n 
1 3764 ASP n 
1 3765 THR n 
1 3766 ILE n 
1 3767 ILE n 
1 3768 THR n 
1 3769 THR n 
1 3770 LEU n 
1 3771 GLU n 
1 3772 ASN n 
1 3773 LEU n 
1 3774 LYS n 
1 3775 ARG n 
1 3776 GLU n 
1 3777 ALA n 
1 3778 ALA n 
1 3779 GLU n 
1 3780 VAL n 
1 3781 THR n 
1 3782 ARG n 
1 3783 LYS n 
1 3784 VAL n 
1 3785 GLU n 
1 3786 GLU n 
1 3787 THR n 
1 3788 ASP n 
1 3789 ILE n 
1 3790 VAL n 
1 3791 MET n 
1 3792 GLN n 
1 3793 GLU n 
1 3794 VAL n 
1 3795 GLU n 
1 3796 THR n 
1 3797 VAL n 
1 3798 SER n 
1 3799 GLN n 
1 3800 GLN n 
1 3801 TYR n 
1 3802 LEU n 
1 3803 PRO n 
1 3804 LEU n 
1 3805 SER n 
1 3806 THR n 
1 3807 ALA n 
1 3808 CYS n 
1 3809 SER n 
1 3810 SER n 
1 3811 ILE n 
1 3812 TYR n 
1 3813 PHE n 
1 3814 THR n 
1 3815 MET n 
1 3816 GLU n 
1 3817 SER n 
1 3818 LEU n 
1 3819 LYS n 
1 3820 GLN n 
1 3821 ILE n 
1 3822 HIS n 
1 3823 PHE n 
1 3824 LEU n 
1 3825 TYR n 
1 3826 GLN n 
1 3827 TYR n 
1 3828 SER n 
1 3829 LEU n 
1 3830 GLN n 
1 3831 PHE n 
1 3832 PHE n 
1 3833 LEU n 
1 3834 ASP n 
1 3835 ILE n 
1 3836 TYR n 
1 3837 HIS n 
1 3838 ASN n 
1 3839 VAL n 
1 3840 LEU n 
1 3841 TYR n 
1 3842 GLU n 
1 3843 ASN n 
1 3844 PRO n 
1 3845 ASN n 
1 3846 LEU n 
1 3847 LYS n 
1 3848 GLY n 
1 3849 VAL n 
1 3850 THR n 
1 3851 ASP n 
1 3852 HIS n 
1 3853 THR n 
1 3854 GLN n 
1 3855 ARG n 
1 3856 LEU n 
1 3857 SER n 
1 3858 ILE n 
1 3859 ILE n 
1 3860 THR n 
1 3861 LYS n 
1 3862 ASP n 
1 3863 LEU n 
1 3864 PHE n 
1 3865 GLN n 
1 3866 VAL n 
1 3867 ALA n 
1 3868 PHE n 
1 3869 ASN n 
1 3870 ARG n 
1 3871 VAL n 
1 3872 ALA n 
1 3873 ARG n 
1 3874 GLY n 
1 3875 MET n 
1 3876 LEU n 
1 3877 HIS n 
1 3878 GLN n 
1 3879 ASP n 
1 3880 HIS n 
1 3881 ILE n 
1 3882 THR n 
1 3883 PHE n 
1 3884 ALA n 
1 3885 MET n 
1 3886 LEU n 
1 3887 LEU n 
1 3888 ALA n 
1 3889 ARG n 
1 3890 ILE n 
1 3891 LYS n 
1 3892 LEU n 
1 3893 LYS n 
1 3894 GLY n 
1 3895 THR n 
1 3896 VAL n 
1 3897 GLY n 
1 3898 GLU n 
1 3899 PRO n 
1 3900 THR n 
1 3901 TYR n 
1 3902 ASP n 
1 3903 ALA n 
1 3904 GLU n 
1 3905 PHE n 
1 3906 GLN n 
1 3907 HIS n 
1 3908 PHE n 
1 3909 LEU n 
1 3910 ARG n 
1 3911 GLY n 
1 3912 ASN n 
1 3913 GLU n 
1 3914 ILE n 
1 3915 VAL n 
1 3916 LEU n 
1 3917 SER n 
1 3918 ALA n 
1 3919 GLY n 
1 3920 SER n 
1 3921 THR n 
1 3922 PRO n 
1 3923 ARG n 
1 3924 ILE n 
1 3925 GLN n 
1 3926 GLY n 
1 3927 LEU n 
1 3928 THR n 
1 3929 VAL n 
1 3930 GLU n 
1 3931 GLN n 
1 3932 ALA n 
1 3933 GLU n 
1 3934 ALA n 
1 3935 VAL n 
1 3936 VAL n 
1 3937 ARG n 
1 3938 LEU n 
1 3939 SER n 
1 3940 CYS n 
1 3941 LEU n 
1 3942 PRO n 
1 3943 ALA n 
1 3944 PHE n 
1 3945 LYS n 
1 3946 ASP n 
1 3947 LEU n 
1 3948 ILE n 
1 3949 ALA n 
1 3950 LYS n 
1 3951 VAL n 
1 3952 GLN n 
1 3953 ALA n 
1 3954 ASP n 
1 3955 GLU n 
1 3956 GLN n 
1 3957 PHE n 
1 3958 GLY n 
1 3959 ILE n 
1 3960 TRP n 
1 3961 LEU n 
1 3962 ASP n 
1 3963 SER n 
1 3964 SER n 
1 3965 SER n 
1 3966 PRO n 
1 3967 GLU n 
1 3968 GLN n 
1 3969 THR n 
1 3970 VAL n 
1 3971 PRO n 
1 3972 TYR n 
1 3973 LEU n 
1 3974 TRP n 
1 3975 SER n 
1 3976 GLU n 
1 3977 GLU n 
1 3978 THR n 
1 3979 PRO n 
1 3980 ALA n 
1 3981 THR n 
1 3982 PRO n 
1 3983 ILE n 
1 3984 GLY n 
1 3985 GLN n 
1 3986 ALA n 
1 3987 ILE n 
1 3988 HIS n 
1 3989 ARG n 
1 3990 LEU n 
1 3991 LEU n 
1 3992 LEU n 
1 3993 ILE n 
1 3994 GLN n 
1 3995 ALA n 
1 3996 PHE n 
1 3997 ARG n 
1 3998 PRO n 
1 3999 ASP n 
1 4000 ARG n 
1 4001 LEU n 
1 4002 LEU n 
1 4003 ALA n 
1 4004 MET n 
1 4005 ALA n 
1 4006 HIS n 
1 4007 MET n 
1 4008 PHE n 
1 4009 VAL n 
1 4010 SER n 
1 4011 THR n 
1 4012 ASN n 
1 4013 LEU n 
1 4014 GLY n 
1 4015 GLU n 
1 4016 SER n 
1 4017 PHE n 
1 4018 MET n 
1 4019 SER n 
1 4020 ILE n 
1 4021 MET n 
1 4022 GLU n 
1 4023 GLN n 
1 4024 PRO n 
1 4025 LEU n 
1 4026 ASP n 
1 4027 LEU n 
1 4028 THR n 
1 4029 HIS n 
1 4030 ILE n 
1 4031 VAL n 
1 4032 GLY n 
1 4033 THR n 
1 4034 GLU n 
1 4035 VAL n 
1 4036 LYS n 
1 4037 PRO n 
1 4038 ASN n 
1 4039 THR n 
1 4040 PRO n 
1 4041 VAL n 
1 4042 LEU n 
1 4043 MET n 
1 4044 CYS n 
1 4045 SER n 
1 4046 VAL n 
1 4047 PRO n 
1 4048 GLY n 
1 4049 TYR n 
1 4050 ASP n 
1 4051 ALA n 
1 4052 SER n 
1 4053 GLY n 
1 4054 HIS n 
1 4055 VAL n 
1 4056 GLU n 
1 4057 ASP n 
1 4058 LEU n 
1 4059 ALA n 
1 4060 ALA n 
1 4061 GLU n 
1 4062 GLN n 
1 4063 ASN n 
1 4064 THR n 
1 4065 GLN n 
1 4066 ILE n 
1 4067 THR n 
1 4068 SER n 
1 4069 ILE n 
1 4070 ALA n 
1 4071 ILE n 
1 4072 GLY n 
1 4073 SER n 
1 4074 ALA n 
1 4075 GLU n 
1 4076 GLY n 
1 4077 PHE n 
1 4078 ASN n 
1 4079 GLN n 
1 4080 ALA n 
1 4081 ASP n 
1 4082 LYS n 
1 4083 ALA n 
1 4084 ILE n 
1 4085 ASN n 
1 4086 THR n 
1 4087 ALA n 
1 4088 VAL n 
1 4089 LYS n 
1 4090 SER n 
1 4091 GLY n 
1 4092 ARG n 
1 4093 TRP n 
1 4094 VAL n 
1 4095 MET n 
1 4096 LEU n 
1 4097 LYS n 
1 4098 ASN n 
1 4099 VAL n 
1 4100 HIS n 
1 4101 LEU n 
1 4102 ALA n 
1 4103 PRO n 
1 4104 GLY n 
1 4105 TRP n 
1 4106 LEU n 
1 4107 MET n 
1 4108 GLN n 
1 4109 LEU n 
1 4110 GLU n 
1 4111 LYS n 
1 4112 LYS n 
1 4113 LEU n 
1 4114 HIS n 
1 4115 SER n 
1 4116 LEU n 
1 4117 GLN n 
1 4118 PRO n 
1 4119 HIS n 
1 4120 ALA n 
1 4121 CYS n 
1 4122 PHE n 
1 4123 ARG n 
1 4124 LEU n 
1 4125 PHE n 
1 4126 LEU n 
1 4127 THR n 
1 4128 MET n 
1 4129 GLU n 
1 4130 ILE n 
1 4131 ASN n 
1 4132 PRO n 
1 4133 LYS n 
1 4134 VAL n 
1 4135 PRO n 
1 4136 VAL n 
1 4137 ASN n 
1 4138 LEU n 
1 4139 LEU n 
1 4140 ARG n 
1 4141 ALA n 
1 4142 GLY n 
1 4143 ARG n 
1 4144 ILE n 
1 4145 PHE n 
1 4146 VAL n 
1 4147 PHE n 
1 4148 GLU n 
1 4149 PRO n 
1 4150 PRO n 
1 4151 PRO n 
1 4152 GLY n 
1 4153 VAL n 
1 4154 LYS n 
1 4155 ALA n 
1 4156 ASN n 
1 4157 MET n 
1 4158 LEU n 
1 4159 ARG n 
1 4160 THR n 
1 4161 PHE n 
1 4162 SER n 
1 4163 SER n 
1 4164 ILE n 
1 4165 PRO n 
1 4166 VAL n 
1 4167 SER n 
1 4168 ARG n 
1 4169 ILE n 
1 4170 CYS n 
1 4171 LYS n 
1 4172 SER n 
1 4173 PRO n 
1 4174 ASN n 
1 4175 GLU n 
1 4176 ARG n 
1 4177 ALA n 
1 4178 ARG n 
1 4179 LEU n 
1 4180 TYR n 
1 4181 PHE n 
1 4182 LEU n 
1 4183 LEU n 
1 4184 ALA n 
1 4185 TRP n 
1 4186 PHE n 
1 4187 HIS n 
1 4188 ALA n 
1 4189 ILE n 
1 4190 ILE n 
1 4191 GLN n 
1 4192 GLU n 
1 4193 ARG n 
1 4194 LEU n 
1 4195 ARG n 
1 4196 TYR n 
1 4197 ALA n 
1 4198 PRO n 
1 4199 LEU n 
1 4200 GLY n 
1 4201 TRP n 
1 4202 SER n 
1 4203 LYS n 
1 4204 LYS n 
1 4205 TYR n 
1 4206 GLU n 
1 4207 PHE n 
1 4208 GLY n 
1 4209 GLU n 
1 4210 SER n 
1 4211 ASP n 
1 4212 LEU n 
1 4213 ARG n 
1 4214 SER n 
1 4215 ALA n 
1 4216 CYS n 
1 4217 ASP n 
1 4218 THR n 
1 4219 VAL n 
1 4220 ASP n 
1 4221 THR n 
1 4222 TRP n 
1 4223 LEU n 
1 4224 ASP n 
1 4225 ASP n 
1 4226 THR n 
1 4227 ALA n 
1 4228 LYS n 
1 4229 GLY n 
1 4230 ARG n 
1 4231 GLN n 
1 4232 ASN n 
1 4233 ILE n 
1 4234 SER n 
1 4235 PRO n 
1 4236 ASP n 
1 4237 LYS n 
1 4238 ILE n 
1 4239 PRO n 
1 4240 TRP n 
1 4241 SER n 
1 4242 ALA n 
1 4243 LEU n 
1 4244 LYS n 
1 4245 THR n 
1 4246 LEU n 
1 4247 MET n 
1 4248 ALA n 
1 4249 GLN n 
1 4250 SER n 
1 4251 ILE n 
1 4252 TYR n 
1 4253 GLY n 
1 4254 GLY n 
1 4255 ARG n 
1 4256 VAL n 
1 4257 ASP n 
1 4258 ASN n 
1 4259 GLU n 
1 4260 PHE n 
1 4261 ASP n 
1 4262 GLN n 
1 4263 ARG n 
1 4264 LEU n 
1 4265 LEU n 
1 4266 ASN n 
1 4267 THR n 
1 4268 PHE n 
1 4269 LEU n 
1 4270 GLU n 
1 4271 ARG n 
1 4272 LEU n 
1 4273 PHE n 
1 4274 THR n 
1 4275 THR n 
1 4276 ARG n 
1 4277 SER n 
1 4278 PHE n 
1 4279 ASP n 
1 4280 SER n 
1 4281 GLU n 
1 4282 PHE n 
1 4283 LYS n 
1 4284 LEU n 
1 4285 ALA n 
1 4286 CYS n 
1 4287 LYS n 
1 4288 VAL n 
1 4289 ASP n 
1 4290 GLY n 
1 4291 HIS n 
1 4292 LYS n 
1 4293 ASP n 
1 4294 ILE n 
1 4295 GLN n 
1 4296 MET n 
1 4297 PRO n 
1 4298 ASP n 
1 4299 GLY n 
1 4300 ILE n 
1 4301 ARG n 
1 4302 ARG n 
1 4303 GLU n 
1 4304 GLU n 
1 4305 PHE n 
1 4306 VAL n 
1 4307 GLN n 
1 4308 TRP n 
1 4309 VAL n 
1 4310 GLU n 
1 4311 LEU n 
1 4312 LEU n 
1 4313 PRO n 
1 4314 ASP n 
1 4315 THR n 
1 4316 GLN n 
1 4317 THR n 
1 4318 PRO n 
1 4319 SER n 
1 4320 TRP n 
1 4321 LEU n 
1 4322 GLY n 
1 4323 LEU n 
1 4324 PRO n 
1 4325 ASN n 
1 4326 ASN n 
1 4327 ALA n 
1 4328 GLU n 
1 4329 ARG n 
1 4330 VAL n 
1 4331 LEU n 
1 4332 LEU n 
1 4333 THR n 
1 4334 THR n 
1 4335 GLN n 
1 4336 GLY n 
1 4337 VAL n 
1 4338 ASP n 
1 4339 MET n 
1 4340 ILE n 
1 4341 SER n 
1 4342 LYS n 
1 4343 MET n 
1 4344 LEU n 
1 4345 LYS n 
1 4346 MET n 
1 4347 GLN n 
1 4348 MET n 
1 4349 LEU n 
1 4350 GLU n 
1 4351 ASP n 
1 4352 GLU n 
1 4353 ASP n 
1 4354 ASP n 
1 4355 LEU n 
1 4356 ALA n 
1 4357 TYR n 
1 4358 ALA n 
1 4359 GLU n 
1 4360 THR n 
1 4361 GLU n 
1 4362 LYS n 
1 4363 LYS n 
1 4364 THR n 
1 4365 ARG n 
1 4366 THR n 
1 4367 ASP n 
1 4368 SER n 
1 4369 THR n 
1 4370 SER n 
1 4371 ASP n 
1 4372 GLY n 
1 4373 ARG n 
1 4374 PRO n 
1 4375 ALA n 
1 4376 TRP n 
1 4377 MET n 
1 4378 ARG n 
1 4379 THR n 
1 4380 LEU n 
1 4381 HIS n 
1 4382 THR n 
1 4383 THR n 
1 4384 ALA n 
1 4385 SER n 
1 4386 ASN n 
1 4387 TRP n 
1 4388 LEU n 
1 4389 HIS n 
1 4390 LEU n 
1 4391 ILE n 
1 4392 PRO n 
1 4393 GLN n 
1 4394 THR n 
1 4395 LEU n 
1 4396 SER n 
1 4397 HIS n 
1 4398 LEU n 
1 4399 LYS n 
1 4400 ARG n 
1 4401 THR n 
1 4402 VAL n 
1 4403 GLU n 
1 4404 ASN n 
1 4405 ILE n 
1 4406 LYS n 
1 4407 ASP n 
1 4408 PRO n 
1 4409 LEU n 
1 4410 PHE n 
1 4411 ARG n 
1 4412 PHE n 
1 4413 PHE n 
1 4414 GLU n 
1 4415 ARG n 
1 4416 GLU n 
1 4417 VAL n 
1 4418 LYS n 
1 4419 MET n 
1 4420 GLY n 
1 4421 ALA n 
1 4422 LYS n 
1 4423 LEU n 
1 4424 LEU n 
1 4425 GLN n 
1 4426 ASP n 
1 4427 VAL n 
1 4428 ARG n 
1 4429 GLN n 
1 4430 ASP n 
1 4431 LEU n 
1 4432 ALA n 
1 4433 ASP n 
1 4434 VAL n 
1 4435 VAL n 
1 4436 GLN n 
1 4437 VAL n 
1 4438 CYS n 
1 4439 GLU n 
1 4440 GLY n 
1 4441 LYS n 
1 4442 LYS n 
1 4443 LYS n 
1 4444 GLN n 
1 4445 THR n 
1 4446 ASN n 
1 4447 TYR n 
1 4448 LEU n 
1 4449 ARG n 
1 4450 THR n 
1 4451 LEU n 
1 4452 ILE n 
1 4453 ASN n 
1 4454 GLU n 
1 4455 LEU n 
1 4456 VAL n 
1 4457 LYS n 
1 4458 GLY n 
1 4459 ILE n 
1 4460 LEU n 
1 4461 PRO n 
1 4462 ARG n 
1 4463 SER n 
1 4464 TRP n 
1 4465 SER n 
1 4466 HIS n 
1 4467 TYR n 
1 4468 THR n 
1 4469 VAL n 
1 4470 PRO n 
1 4471 ALA n 
1 4472 GLY n 
1 4473 MET n 
1 4474 THR n 
1 4475 VAL n 
1 4476 ILE n 
1 4477 GLN n 
1 4478 TRP n 
1 4479 VAL n 
1 4480 SER n 
1 4481 ASP n 
1 4482 PHE n 
1 4483 SER n 
1 4484 GLU n 
1 4485 ARG n 
1 4486 ILE n 
1 4487 LYS n 
1 4488 GLN n 
1 4489 LEU n 
1 4490 GLN n 
1 4491 ASN n 
1 4492 ILE n 
1 4493 SER n 
1 4494 LEU n 
1 4495 ALA n 
1 4496 ALA n 
1 4497 ALA n 
1 4498 SER n 
1 4499 GLY n 
1 4500 GLY n 
1 4501 ALA n 
1 4502 LYS n 
1 4503 GLU n 
1 4504 LEU n 
1 4505 LYS n 
1 4506 ASN n 
1 4507 ILE n 
1 4508 HIS n 
1 4509 VAL n 
1 4510 CYS n 
1 4511 LEU n 
1 4512 GLY n 
1 4513 GLY n 
1 4514 LEU n 
1 4515 PHE n 
1 4516 VAL n 
1 4517 PRO n 
1 4518 GLU n 
1 4519 ALA n 
1 4520 TYR n 
1 4521 ILE n 
1 4522 THR n 
1 4523 ALA n 
1 4524 THR n 
1 4525 ARG n 
1 4526 GLN n 
1 4527 TYR n 
1 4528 VAL n 
1 4529 ALA n 
1 4530 GLN n 
1 4531 ALA n 
1 4532 ASN n 
1 4533 SER n 
1 4534 TRP n 
1 4535 SER n 
1 4536 LEU n 
1 4537 GLU n 
1 4538 GLU n 
1 4539 LEU n 
1 4540 CYS n 
1 4541 LEU n 
1 4542 GLU n 
1 4543 VAL n 
1 4544 ASN n 
1 4545 VAL n 
1 4546 THR n 
1 4547 THR n 
1 4548 SER n 
1 4549 GLN n 
1 4550 GLY n 
1 4551 ALA n 
1 4552 THR n 
1 4553 LEU n 
1 4554 ASP n 
1 4555 ALA n 
1 4556 CYS n 
1 4557 SER n 
1 4558 PHE n 
1 4559 GLY n 
1 4560 VAL n 
1 4561 THR n 
1 4562 GLY n 
1 4563 LEU n 
1 4564 LYS n 
1 4565 LEU n 
1 4566 GLN n 
1 4567 GLY n 
1 4568 ALA n 
1 4569 THR n 
1 4570 CYS n 
1 4571 ASN n 
1 4572 ASN n 
1 4573 ASN n 
1 4574 LYS n 
1 4575 LEU n 
1 4576 SER n 
1 4577 LEU n 
1 4578 SER n 
1 4579 ASN n 
1 4580 ALA n 
1 4581 ILE n 
1 4582 SER n 
1 4583 THR n 
1 4584 ALA n 
1 4585 LEU n 
1 4586 PRO n 
1 4587 LEU n 
1 4588 THR n 
1 4589 GLN n 
1 4590 LEU n 
1 4591 ARG n 
1 4592 TRP n 
1 4593 VAL n 
1 4594 LYS n 
1 4595 GLN n 
1 4596 THR n 
1 4597 ASN n 
1 4598 THR n 
1 4599 GLU n 
1 4600 LYS n 
1 4601 LYS n 
1 4602 ALA n 
1 4603 SER n 
1 4604 VAL n 
1 4605 VAL n 
1 4606 THR n 
1 4607 LEU n 
1 4608 PRO n 
1 4609 VAL n 
1 4610 TYR n 
1 4611 LEU n 
1 4612 ASN n 
1 4613 PHE n 
1 4614 THR n 
1 4615 ARG n 
1 4616 ALA n 
1 4617 ASP n 
1 4618 LEU n 
1 4619 ILE n 
1 4620 PHE n 
1 4621 THR n 
1 4622 VAL n 
1 4623 ASP n 
1 4624 PHE n 
1 4625 GLU n 
1 4626 ILE n 
1 4627 ALA n 
1 4628 THR n 
1 4629 LYS n 
1 4630 GLU n 
1 4631 ASP n 
1 4632 PRO n 
1 4633 ARG n 
1 4634 SER n 
1 4635 PHE n 
1 4636 TYR n 
1 4637 GLU n 
1 4638 ARG n 
1 4639 GLY n 
1 4640 VAL n 
1 4641 ALA n 
1 4642 VAL n 
1 4643 LEU n 
1 4644 CYS n 
1 4645 THR n 
1 4646 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   4646 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               'fall armyworm' 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O10 P2' 427.201 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    GLU 3    3    ?    ?   ?   A . n 
A 1 4    PRO 4    4    ?    ?   ?   A . n 
A 1 5    GLY 5    5    ?    ?   ?   A . n 
A 1 6    GLY 6    6    ?    ?   ?   A . n 
A 1 7    GLY 7    7    ?    ?   ?   A . n 
A 1 8    GLY 8    8    ?    ?   ?   A . n 
A 1 9    GLY 9    9    ?    ?   ?   A . n 
A 1 10   GLU 10   10   ?    ?   ?   A . n 
A 1 11   ASP 11   11   ?    ?   ?   A . n 
A 1 12   GLY 12   12   ?    ?   ?   A . n 
A 1 13   SER 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   GLY 15   15   ?    ?   ?   A . n 
A 1 16   LEU 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   SER 19   19   ?    ?   ?   A . n 
A 1 20   ALA 20   20   ?    ?   ?   A . n 
A 1 21   VAL 21   21   ?    ?   ?   A . n 
A 1 22   GLN 22   22   ?    ?   ?   A . n 
A 1 23   ASN 23   23   ?    ?   ?   A . n 
A 1 24   VAL 24   24   ?    ?   ?   A . n 
A 1 25   ALA 25   25   ?    ?   ?   A . n 
A 1 26   ASP 26   26   ?    ?   ?   A . n 
A 1 27   VAL 27   27   ?    ?   ?   A . n 
A 1 28   SER 28   28   ?    ?   ?   A . n 
A 1 29   VAL 29   29   ?    ?   ?   A . n 
A 1 30   LEU 30   30   ?    ?   ?   A . n 
A 1 31   GLN 31   31   ?    ?   ?   A . n 
A 1 32   LYS 32   32   ?    ?   ?   A . n 
A 1 33   HIS 33   33   ?    ?   ?   A . n 
A 1 34   LEU 34   34   ?    ?   ?   A . n 
A 1 35   ARG 35   35   ?    ?   ?   A . n 
A 1 36   LYS 36   36   ?    ?   ?   A . n 
A 1 37   LEU 37   37   ?    ?   ?   A . n 
A 1 38   VAL 38   38   ?    ?   ?   A . n 
A 1 39   PRO 39   39   ?    ?   ?   A . n 
A 1 40   LEU 40   40   ?    ?   ?   A . n 
A 1 41   LEU 41   41   ?    ?   ?   A . n 
A 1 42   LEU 42   42   ?    ?   ?   A . n 
A 1 43   GLU 43   43   ?    ?   ?   A . n 
A 1 44   ASP 44   44   ?    ?   ?   A . n 
A 1 45   GLY 45   45   ?    ?   ?   A . n 
A 1 46   GLY 46   46   ?    ?   ?   A . n 
A 1 47   GLU 47   47   ?    ?   ?   A . n 
A 1 48   ALA 48   48   ?    ?   ?   A . n 
A 1 49   PRO 49   49   ?    ?   ?   A . n 
A 1 50   ALA 50   50   ?    ?   ?   A . n 
A 1 51   ALA 51   51   ?    ?   ?   A . n 
A 1 52   LEU 52   52   ?    ?   ?   A . n 
A 1 53   GLU 53   53   ?    ?   ?   A . n 
A 1 54   ALA 54   54   ?    ?   ?   A . n 
A 1 55   ALA 55   55   ?    ?   ?   A . n 
A 1 56   LEU 56   56   ?    ?   ?   A . n 
A 1 57   GLU 57   57   ?    ?   ?   A . n 
A 1 58   GLU 58   58   ?    ?   ?   A . n 
A 1 59   LYS 59   59   ?    ?   ?   A . n 
A 1 60   SER 60   60   ?    ?   ?   A . n 
A 1 61   ALA 61   61   ?    ?   ?   A . n 
A 1 62   LEU 62   62   ?    ?   ?   A . n 
A 1 63   GLU 63   63   ?    ?   ?   A . n 
A 1 64   GLN 64   64   ?    ?   ?   A . n 
A 1 65   MET 65   65   ?    ?   ?   A . n 
A 1 66   ARG 66   66   ?    ?   ?   A . n 
A 1 67   LYS 67   67   ?    ?   ?   A . n 
A 1 68   PHE 68   68   ?    ?   ?   A . n 
A 1 69   LEU 69   69   ?    ?   ?   A . n 
A 1 70   SER 70   70   ?    ?   ?   A . n 
A 1 71   ASP 71   71   ?    ?   ?   A . n 
A 1 72   PRO 72   72   ?    ?   ?   A . n 
A 1 73   GLN 73   73   ?    ?   ?   A . n 
A 1 74   VAL 74   74   ?    ?   ?   A . n 
A 1 75   HIS 75   75   ?    ?   ?   A . n 
A 1 76   THR 76   76   ?    ?   ?   A . n 
A 1 77   VAL 77   77   ?    ?   ?   A . n 
A 1 78   LEU 78   78   ?    ?   ?   A . n 
A 1 79   VAL 79   79   ?    ?   ?   A . n 
A 1 80   GLU 80   80   ?    ?   ?   A . n 
A 1 81   ARG 81   81   ?    ?   ?   A . n 
A 1 82   SER 82   82   ?    ?   ?   A . n 
A 1 83   THR 83   83   ?    ?   ?   A . n 
A 1 84   LEU 84   84   ?    ?   ?   A . n 
A 1 85   LYS 85   85   ?    ?   ?   A . n 
A 1 86   GLU 86   86   ?    ?   ?   A . n 
A 1 87   ASP 87   87   ?    ?   ?   A . n 
A 1 88   VAL 88   88   ?    ?   ?   A . n 
A 1 89   GLY 89   89   ?    ?   ?   A . n 
A 1 90   ASP 90   90   ?    ?   ?   A . n 
A 1 91   GLU 91   91   ?    ?   ?   A . n 
A 1 92   GLY 92   92   ?    ?   ?   A . n 
A 1 93   GLU 93   93   ?    ?   ?   A . n 
A 1 94   GLU 94   94   ?    ?   ?   A . n 
A 1 95   GLU 95   95   ?    ?   ?   A . n 
A 1 96   LYS 96   96   ?    ?   ?   A . n 
A 1 97   GLU 97   97   ?    ?   ?   A . n 
A 1 98   PHE 98   98   ?    ?   ?   A . n 
A 1 99   ILE 99   99   ?    ?   ?   A . n 
A 1 100  SER 100  100  ?    ?   ?   A . n 
A 1 101  TYR 101  101  ?    ?   ?   A . n 
A 1 102  ASN 102  102  ?    ?   ?   A . n 
A 1 103  ILE 103  103  ?    ?   ?   A . n 
A 1 104  ASN 104  104  ?    ?   ?   A . n 
A 1 105  ILE 105  105  ?    ?   ?   A . n 
A 1 106  ASP 106  106  ?    ?   ?   A . n 
A 1 107  ILE 107  107  ?    ?   ?   A . n 
A 1 108  HIS 108  108  ?    ?   ?   A . n 
A 1 109  TYR 109  109  ?    ?   ?   A . n 
A 1 110  GLY 110  110  ?    ?   ?   A . n 
A 1 111  VAL 111  111  ?    ?   ?   A . n 
A 1 112  LYS 112  112  ?    ?   ?   A . n 
A 1 113  SER 113  113  ?    ?   ?   A . n 
A 1 114  ASN 114  114  ?    ?   ?   A . n 
A 1 115  SER 115  115  ?    ?   ?   A . n 
A 1 116  LEU 116  116  ?    ?   ?   A . n 
A 1 117  ALA 117  117  ?    ?   ?   A . n 
A 1 118  PHE 118  118  ?    ?   ?   A . n 
A 1 119  ILE 119  119  ?    ?   ?   A . n 
A 1 120  LYS 120  120  ?    ?   ?   A . n 
A 1 121  ARG 121  121  ?    ?   ?   A . n 
A 1 122  THR 122  122  ?    ?   ?   A . n 
A 1 123  PRO 123  123  ?    ?   ?   A . n 
A 1 124  VAL 124  124  ?    ?   ?   A . n 
A 1 125  ILE 125  125  ?    ?   ?   A . n 
A 1 126  ASP 126  126  ?    ?   ?   A . n 
A 1 127  ALA 127  127  ?    ?   ?   A . n 
A 1 128  ASP 128  128  ?    ?   ?   A . n 
A 1 129  LYS 129  129  ?    ?   ?   A . n 
A 1 130  PRO 130  130  ?    ?   ?   A . n 
A 1 131  VAL 131  131  ?    ?   ?   A . n 
A 1 132  SER 132  132  ?    ?   ?   A . n 
A 1 133  SER 133  133  ?    ?   ?   A . n 
A 1 134  GLN 134  134  ?    ?   ?   A . n 
A 1 135  LEU 135  135  ?    ?   ?   A . n 
A 1 136  ARG 136  136  ?    ?   ?   A . n 
A 1 137  VAL 137  137  ?    ?   ?   A . n 
A 1 138  LEU 138  138  ?    ?   ?   A . n 
A 1 139  THR 139  139  ?    ?   ?   A . n 
A 1 140  LEU 140  140  ?    ?   ?   A . n 
A 1 141  SER 141  141  ?    ?   ?   A . n 
A 1 142  GLU 142  142  ?    ?   ?   A . n 
A 1 143  ASP 143  143  ?    ?   ?   A . n 
A 1 144  SER 144  144  ?    ?   ?   A . n 
A 1 145  PRO 145  145  ?    ?   ?   A . n 
A 1 146  TYR 146  146  ?    ?   ?   A . n 
A 1 147  GLU 147  147  ?    ?   ?   A . n 
A 1 148  THR 148  148  ?    ?   ?   A . n 
A 1 149  LEU 149  149  ?    ?   ?   A . n 
A 1 150  HIS 150  150  ?    ?   ?   A . n 
A 1 151  SER 151  151  ?    ?   ?   A . n 
A 1 152  PHE 152  152  ?    ?   ?   A . n 
A 1 153  ILE 153  153  ?    ?   ?   A . n 
A 1 154  SER 154  154  ?    ?   ?   A . n 
A 1 155  ASN 155  155  ?    ?   ?   A . n 
A 1 156  ALA 156  156  ?    ?   ?   A . n 
A 1 157  VAL 157  157  ?    ?   ?   A . n 
A 1 158  ALA 158  158  ?    ?   ?   A . n 
A 1 159  PRO 159  159  ?    ?   ?   A . n 
A 1 160  PHE 160  160  ?    ?   ?   A . n 
A 1 161  PHE 161  161  ?    ?   ?   A . n 
A 1 162  LYS 162  162  ?    ?   ?   A . n 
A 1 163  SER 163  163  ?    ?   ?   A . n 
A 1 164  TYR 164  164  ?    ?   ?   A . n 
A 1 165  ILE 165  165  ?    ?   ?   A . n 
A 1 166  ARG 166  166  ?    ?   ?   A . n 
A 1 167  GLU 167  167  ?    ?   ?   A . n 
A 1 168  SER 168  168  ?    ?   ?   A . n 
A 1 169  GLY 169  169  ?    ?   ?   A . n 
A 1 170  LYS 170  170  ?    ?   ?   A . n 
A 1 171  ALA 171  171  ?    ?   ?   A . n 
A 1 172  ASP 172  172  ?    ?   ?   A . n 
A 1 173  ARG 173  173  ?    ?   ?   A . n 
A 1 174  ASP 174  174  ?    ?   ?   A . n 
A 1 175  GLY 175  175  ?    ?   ?   A . n 
A 1 176  ASP 176  176  ?    ?   ?   A . n 
A 1 177  LYS 177  177  ?    ?   ?   A . n 
A 1 178  MET 178  178  ?    ?   ?   A . n 
A 1 179  ALA 179  179  ?    ?   ?   A . n 
A 1 180  PRO 180  180  ?    ?   ?   A . n 
A 1 181  SER 181  181  ?    ?   ?   A . n 
A 1 182  VAL 182  182  ?    ?   ?   A . n 
A 1 183  GLU 183  183  ?    ?   ?   A . n 
A 1 184  LYS 184  184  ?    ?   ?   A . n 
A 1 185  LYS 185  185  ?    ?   ?   A . n 
A 1 186  ILE 186  186  ?    ?   ?   A . n 
A 1 187  ALA 187  187  ?    ?   ?   A . n 
A 1 188  GLU 188  188  ?    ?   ?   A . n 
A 1 189  LEU 189  189  ?    ?   ?   A . n 
A 1 190  GLU 190  190  ?    ?   ?   A . n 
A 1 191  MET 191  191  ?    ?   ?   A . n 
A 1 192  GLY 192  192  ?    ?   ?   A . n 
A 1 193  LEU 193  193  ?    ?   ?   A . n 
A 1 194  LEU 194  194  ?    ?   ?   A . n 
A 1 195  HIS 195  195  ?    ?   ?   A . n 
A 1 196  LEU 196  196  ?    ?   ?   A . n 
A 1 197  GLN 197  197  ?    ?   ?   A . n 
A 1 198  GLN 198  198  ?    ?   ?   A . n 
A 1 199  ASN 199  199  ?    ?   ?   A . n 
A 1 200  ILE 200  200  ?    ?   ?   A . n 
A 1 201  GLU 201  201  ?    ?   ?   A . n 
A 1 202  ILE 202  202  ?    ?   ?   A . n 
A 1 203  PRO 203  203  ?    ?   ?   A . n 
A 1 204  GLU 204  204  ?    ?   ?   A . n 
A 1 205  ILE 205  205  ?    ?   ?   A . n 
A 1 206  SER 206  206  ?    ?   ?   A . n 
A 1 207  LEU 207  207  ?    ?   ?   A . n 
A 1 208  PRO 208  208  ?    ?   ?   A . n 
A 1 209  ILE 209  209  ?    ?   ?   A . n 
A 1 210  HIS 210  210  ?    ?   ?   A . n 
A 1 211  PRO 211  211  ?    ?   ?   A . n 
A 1 212  MET 212  212  ?    ?   ?   A . n 
A 1 213  ILE 213  213  ?    ?   ?   A . n 
A 1 214  THR 214  214  ?    ?   ?   A . n 
A 1 215  ASN 215  215  ?    ?   ?   A . n 
A 1 216  VAL 216  216  ?    ?   ?   A . n 
A 1 217  ALA 217  217  ?    ?   ?   A . n 
A 1 218  LYS 218  218  ?    ?   ?   A . n 
A 1 219  GLN 219  219  ?    ?   ?   A . n 
A 1 220  CYS 220  220  ?    ?   ?   A . n 
A 1 221  TYR 221  221  ?    ?   ?   A . n 
A 1 222  GLU 222  222  ?    ?   ?   A . n 
A 1 223  ARG 223  223  ?    ?   ?   A . n 
A 1 224  GLY 224  224  ?    ?   ?   A . n 
A 1 225  GLU 225  225  ?    ?   ?   A . n 
A 1 226  LYS 226  226  ?    ?   ?   A . n 
A 1 227  PRO 227  227  ?    ?   ?   A . n 
A 1 228  LYS 228  228  ?    ?   ?   A . n 
A 1 229  VAL 229  229  ?    ?   ?   A . n 
A 1 230  THR 230  230  ?    ?   ?   A . n 
A 1 231  ASP 231  231  ?    ?   ?   A . n 
A 1 232  PHE 232  232  ?    ?   ?   A . n 
A 1 233  GLY 233  233  ?    ?   ?   A . n 
A 1 234  ASP 234  234  ?    ?   ?   A . n 
A 1 235  LYS 235  235  ?    ?   ?   A . n 
A 1 236  VAL 236  236  ?    ?   ?   A . n 
A 1 237  GLU 237  237  ?    ?   ?   A . n 
A 1 238  ASP 238  238  ?    ?   ?   A . n 
A 1 239  PRO 239  239  ?    ?   ?   A . n 
A 1 240  THR 240  240  ?    ?   ?   A . n 
A 1 241  PHE 241  241  ?    ?   ?   A . n 
A 1 242  LEU 242  242  ?    ?   ?   A . n 
A 1 243  ASN 243  243  ?    ?   ?   A . n 
A 1 244  GLN 244  244  ?    ?   ?   A . n 
A 1 245  LEU 245  245  ?    ?   ?   A . n 
A 1 246  GLN 246  246  ?    ?   ?   A . n 
A 1 247  SER 247  247  ?    ?   ?   A . n 
A 1 248  GLY 248  248  ?    ?   ?   A . n 
A 1 249  VAL 249  249  ?    ?   ?   A . n 
A 1 250  ASN 250  250  ?    ?   ?   A . n 
A 1 251  ARG 251  251  ?    ?   ?   A . n 
A 1 252  TRP 252  252  ?    ?   ?   A . n 
A 1 253  ILE 253  253  ?    ?   ?   A . n 
A 1 254  ARG 254  254  ?    ?   ?   A . n 
A 1 255  GLU 255  255  ?    ?   ?   A . n 
A 1 256  ILE 256  256  ?    ?   ?   A . n 
A 1 257  GLN 257  257  ?    ?   ?   A . n 
A 1 258  LYS 258  258  ?    ?   ?   A . n 
A 1 259  VAL 259  259  ?    ?   ?   A . n 
A 1 260  THR 260  260  ?    ?   ?   A . n 
A 1 261  LYS 261  261  ?    ?   ?   A . n 
A 1 262  LEU 262  262  ?    ?   ?   A . n 
A 1 263  ASP 263  263  ?    ?   ?   A . n 
A 1 264  ARG 264  264  ?    ?   ?   A . n 
A 1 265  ASP 265  265  ?    ?   ?   A . n 
A 1 266  PRO 266  266  ?    ?   ?   A . n 
A 1 267  ALA 267  267  ?    ?   ?   A . n 
A 1 268  SER 268  268  ?    ?   ?   A . n 
A 1 269  GLY 269  269  ?    ?   ?   A . n 
A 1 270  THR 270  270  ?    ?   ?   A . n 
A 1 271  ALA 271  271  ?    ?   ?   A . n 
A 1 272  LEU 272  272  ?    ?   ?   A . n 
A 1 273  GLN 273  273  ?    ?   ?   A . n 
A 1 274  GLU 274  274  ?    ?   ?   A . n 
A 1 275  ILE 275  275  ?    ?   ?   A . n 
A 1 276  SER 276  276  ?    ?   ?   A . n 
A 1 277  PHE 277  277  ?    ?   ?   A . n 
A 1 278  TRP 278  278  ?    ?   ?   A . n 
A 1 279  LEU 279  279  ?    ?   ?   A . n 
A 1 280  ASN 280  280  ?    ?   ?   A . n 
A 1 281  LEU 281  281  ?    ?   ?   A . n 
A 1 282  GLU 282  282  ?    ?   ?   A . n 
A 1 283  ARG 283  283  ?    ?   ?   A . n 
A 1 284  ALA 284  284  ?    ?   ?   A . n 
A 1 285  LEU 285  285  ?    ?   ?   A . n 
A 1 286  TYR 286  286  ?    ?   ?   A . n 
A 1 287  ARG 287  287  ?    ?   ?   A . n 
A 1 288  ILE 288  288  ?    ?   ?   A . n 
A 1 289  GLN 289  289  ?    ?   ?   A . n 
A 1 290  GLU 290  290  ?    ?   ?   A . n 
A 1 291  LYS 291  291  ?    ?   ?   A . n 
A 1 292  ARG 292  292  ?    ?   ?   A . n 
A 1 293  GLU 293  293  ?    ?   ?   A . n 
A 1 294  SER 294  294  ?    ?   ?   A . n 
A 1 295  PRO 295  295  ?    ?   ?   A . n 
A 1 296  GLU 296  296  ?    ?   ?   A . n 
A 1 297  VAL 297  297  ?    ?   ?   A . n 
A 1 298  LEU 298  298  ?    ?   ?   A . n 
A 1 299  LEU 299  299  ?    ?   ?   A . n 
A 1 300  THR 300  300  ?    ?   ?   A . n 
A 1 301  LEU 301  301  ?    ?   ?   A . n 
A 1 302  ASP 302  302  ?    ?   ?   A . n 
A 1 303  ILE 303  303  ?    ?   ?   A . n 
A 1 304  LEU 304  304  ?    ?   ?   A . n 
A 1 305  LYS 305  305  ?    ?   ?   A . n 
A 1 306  HIS 306  306  ?    ?   ?   A . n 
A 1 307  GLY 307  307  ?    ?   ?   A . n 
A 1 308  LYS 308  308  ?    ?   ?   A . n 
A 1 309  ARG 309  309  ?    ?   ?   A . n 
A 1 310  PHE 310  310  ?    ?   ?   A . n 
A 1 311  HIS 311  311  ?    ?   ?   A . n 
A 1 312  ALA 312  312  ?    ?   ?   A . n 
A 1 313  THR 313  313  ?    ?   ?   A . n 
A 1 314  VAL 314  314  ?    ?   ?   A . n 
A 1 315  SER 315  315  ?    ?   ?   A . n 
A 1 316  PHE 316  316  ?    ?   ?   A . n 
A 1 317  ASP 317  317  ?    ?   ?   A . n 
A 1 318  THR 318  318  ?    ?   ?   A . n 
A 1 319  ASP 319  319  ?    ?   ?   A . n 
A 1 320  THR 320  320  ?    ?   ?   A . n 
A 1 321  GLY 321  321  ?    ?   ?   A . n 
A 1 322  LEU 322  322  ?    ?   ?   A . n 
A 1 323  LYS 323  323  ?    ?   ?   A . n 
A 1 324  GLN 324  324  ?    ?   ?   A . n 
A 1 325  ALA 325  325  ?    ?   ?   A . n 
A 1 326  LEU 326  326  ?    ?   ?   A . n 
A 1 327  GLU 327  327  ?    ?   ?   A . n 
A 1 328  THR 328  328  ?    ?   ?   A . n 
A 1 329  VAL 329  329  ?    ?   ?   A . n 
A 1 330  ASN 330  330  ?    ?   ?   A . n 
A 1 331  ASP 331  331  ?    ?   ?   A . n 
A 1 332  TYR 332  332  ?    ?   ?   A . n 
A 1 333  ASN 333  333  ?    ?   ?   A . n 
A 1 334  PRO 334  334  ?    ?   ?   A . n 
A 1 335  LEU 335  335  ?    ?   ?   A . n 
A 1 336  MET 336  336  ?    ?   ?   A . n 
A 1 337  LYS 337  337  ?    ?   ?   A . n 
A 1 338  ASP 338  338  ?    ?   ?   A . n 
A 1 339  PHE 339  339  ?    ?   ?   A . n 
A 1 340  PRO 340  340  ?    ?   ?   A . n 
A 1 341  LEU 341  341  ?    ?   ?   A . n 
A 1 342  ASN 342  342  ?    ?   ?   A . n 
A 1 343  ASP 343  343  ?    ?   ?   A . n 
A 1 344  LEU 344  344  ?    ?   ?   A . n 
A 1 345  LEU 345  345  ?    ?   ?   A . n 
A 1 346  SER 346  346  ?    ?   ?   A . n 
A 1 347  ALA 347  347  ?    ?   ?   A . n 
A 1 348  THR 348  348  ?    ?   ?   A . n 
A 1 349  GLU 349  349  ?    ?   ?   A . n 
A 1 350  LEU 350  350  ?    ?   ?   A . n 
A 1 351  ASP 351  351  ?    ?   ?   A . n 
A 1 352  LYS 352  352  ?    ?   ?   A . n 
A 1 353  ILE 353  353  ?    ?   ?   A . n 
A 1 354  ARG 354  354  ?    ?   ?   A . n 
A 1 355  GLN 355  355  ?    ?   ?   A . n 
A 1 356  ALA 356  356  ?    ?   ?   A . n 
A 1 357  LEU 357  357  ?    ?   ?   A . n 
A 1 358  VAL 358  358  ?    ?   ?   A . n 
A 1 359  ALA 359  359  ?    ?   ?   A . n 
A 1 360  ILE 360  360  ?    ?   ?   A . n 
A 1 361  PHE 361  361  ?    ?   ?   A . n 
A 1 362  THR 362  362  ?    ?   ?   A . n 
A 1 363  HIS 363  363  ?    ?   ?   A . n 
A 1 364  LEU 364  364  ?    ?   ?   A . n 
A 1 365  ARG 365  365  ?    ?   ?   A . n 
A 1 366  LYS 366  366  ?    ?   ?   A . n 
A 1 367  ILE 367  367  ?    ?   ?   A . n 
A 1 368  ARG 368  368  ?    ?   ?   A . n 
A 1 369  ASN 369  369  ?    ?   ?   A . n 
A 1 370  THR 370  370  ?    ?   ?   A . n 
A 1 371  LYS 371  371  ?    ?   ?   A . n 
A 1 372  TYR 372  372  ?    ?   ?   A . n 
A 1 373  PRO 373  373  ?    ?   ?   A . n 
A 1 374  ILE 374  374  ?    ?   ?   A . n 
A 1 375  GLN 375  375  ?    ?   ?   A . n 
A 1 376  ARG 376  376  ?    ?   ?   A . n 
A 1 377  ALA 377  377  ?    ?   ?   A . n 
A 1 378  LEU 378  378  ?    ?   ?   A . n 
A 1 379  ARG 379  379  ?    ?   ?   A . n 
A 1 380  LEU 380  380  ?    ?   ?   A . n 
A 1 381  VAL 381  381  ?    ?   ?   A . n 
A 1 382  GLU 382  382  ?    ?   ?   A . n 
A 1 383  ALA 383  383  ?    ?   ?   A . n 
A 1 384  ILE 384  384  ?    ?   ?   A . n 
A 1 385  SER 385  385  ?    ?   ?   A . n 
A 1 386  ARG 386  386  ?    ?   ?   A . n 
A 1 387  ASP 387  387  ?    ?   ?   A . n 
A 1 388  LEU 388  388  ?    ?   ?   A . n 
A 1 389  SER 389  389  ?    ?   ?   A . n 
A 1 390  SER 390  390  ?    ?   ?   A . n 
A 1 391  GLN 391  391  ?    ?   ?   A . n 
A 1 392  LEU 392  392  ?    ?   ?   A . n 
A 1 393  LEU 393  393  ?    ?   ?   A . n 
A 1 394  LYS 394  394  ?    ?   ?   A . n 
A 1 395  VAL 395  395  ?    ?   ?   A . n 
A 1 396  LEU 396  396  ?    ?   ?   A . n 
A 1 397  GLY 397  397  ?    ?   ?   A . n 
A 1 398  THR 398  398  ?    ?   ?   A . n 
A 1 399  ARG 399  399  ?    ?   ?   A . n 
A 1 400  LYS 400  400  ?    ?   ?   A . n 
A 1 401  LEU 401  401  ?    ?   ?   A . n 
A 1 402  MET 402  402  ?    ?   ?   A . n 
A 1 403  HIS 403  403  ?    ?   ?   A . n 
A 1 404  VAL 404  404  ?    ?   ?   A . n 
A 1 405  ALA 405  405  ?    ?   ?   A . n 
A 1 406  TYR 406  406  ?    ?   ?   A . n 
A 1 407  GLU 407  407  ?    ?   ?   A . n 
A 1 408  GLU 408  408  ?    ?   ?   A . n 
A 1 409  PHE 409  409  ?    ?   ?   A . n 
A 1 410  GLU 410  410  ?    ?   ?   A . n 
A 1 411  LYS 411  411  ?    ?   ?   A . n 
A 1 412  VAL 412  412  ?    ?   ?   A . n 
A 1 413  MET 413  413  ?    ?   ?   A . n 
A 1 414  VAL 414  414  ?    ?   ?   A . n 
A 1 415  ALA 415  415  ?    ?   ?   A . n 
A 1 416  CYS 416  416  ?    ?   ?   A . n 
A 1 417  PHE 417  417  ?    ?   ?   A . n 
A 1 418  GLU 418  418  ?    ?   ?   A . n 
A 1 419  VAL 419  419  ?    ?   ?   A . n 
A 1 420  PHE 420  420  ?    ?   ?   A . n 
A 1 421  GLN 421  421  ?    ?   ?   A . n 
A 1 422  THR 422  422  ?    ?   ?   A . n 
A 1 423  TRP 423  423  ?    ?   ?   A . n 
A 1 424  ASP 424  424  ?    ?   ?   A . n 
A 1 425  ASP 425  425  ?    ?   ?   A . n 
A 1 426  GLU 426  426  ?    ?   ?   A . n 
A 1 427  TYR 427  427  ?    ?   ?   A . n 
A 1 428  GLU 428  428  ?    ?   ?   A . n 
A 1 429  LYS 429  429  ?    ?   ?   A . n 
A 1 430  LEU 430  430  ?    ?   ?   A . n 
A 1 431  GLN 431  431  ?    ?   ?   A . n 
A 1 432  VAL 432  432  ?    ?   ?   A . n 
A 1 433  LEU 433  433  ?    ?   ?   A . n 
A 1 434  LEU 434  434  ?    ?   ?   A . n 
A 1 435  ARG 435  435  ?    ?   ?   A . n 
A 1 436  ASP 436  436  ?    ?   ?   A . n 
A 1 437  ILE 437  437  ?    ?   ?   A . n 
A 1 438  VAL 438  438  ?    ?   ?   A . n 
A 1 439  LYS 439  439  ?    ?   ?   A . n 
A 1 440  ARG 440  440  ?    ?   ?   A . n 
A 1 441  LYS 441  441  ?    ?   ?   A . n 
A 1 442  ARG 442  442  ?    ?   ?   A . n 
A 1 443  GLU 443  443  ?    ?   ?   A . n 
A 1 444  GLU 444  444  ?    ?   ?   A . n 
A 1 445  ASN 445  445  ?    ?   ?   A . n 
A 1 446  LEU 446  446  ?    ?   ?   A . n 
A 1 447  LYS 447  447  ?    ?   ?   A . n 
A 1 448  MET 448  448  ?    ?   ?   A . n 
A 1 449  VAL 449  449  ?    ?   ?   A . n 
A 1 450  TRP 450  450  ?    ?   ?   A . n 
A 1 451  ARG 451  451  ?    ?   ?   A . n 
A 1 452  ILE 452  452  ?    ?   ?   A . n 
A 1 453  ASN 453  453  ?    ?   ?   A . n 
A 1 454  PRO 454  454  ?    ?   ?   A . n 
A 1 455  ALA 455  455  ?    ?   ?   A . n 
A 1 456  HIS 456  456  ?    ?   ?   A . n 
A 1 457  ARG 457  457  ?    ?   ?   A . n 
A 1 458  LYS 458  458  ?    ?   ?   A . n 
A 1 459  LEU 459  459  ?    ?   ?   A . n 
A 1 460  GLN 460  460  ?    ?   ?   A . n 
A 1 461  ALA 461  461  ?    ?   ?   A . n 
A 1 462  ARG 462  462  ?    ?   ?   A . n 
A 1 463  LEU 463  463  ?    ?   ?   A . n 
A 1 464  ASP 464  464  ?    ?   ?   A . n 
A 1 465  GLN 465  465  ?    ?   ?   A . n 
A 1 466  MET 466  466  ?    ?   ?   A . n 
A 1 467  ARG 467  467  ?    ?   ?   A . n 
A 1 468  LYS 468  468  ?    ?   ?   A . n 
A 1 469  PHE 469  469  ?    ?   ?   A . n 
A 1 470  ARG 470  470  ?    ?   ?   A . n 
A 1 471  ARG 471  471  ?    ?   ?   A . n 
A 1 472  GLN 472  472  ?    ?   ?   A . n 
A 1 473  HIS 473  473  ?    ?   ?   A . n 
A 1 474  GLU 474  474  ?    ?   ?   A . n 
A 1 475  GLN 475  475  ?    ?   ?   A . n 
A 1 476  LEU 476  476  ?    ?   ?   A . n 
A 1 477  ARG 477  477  ?    ?   ?   A . n 
A 1 478  ALA 478  478  ?    ?   ?   A . n 
A 1 479  VAL 479  479  ?    ?   ?   A . n 
A 1 480  ILE 480  480  ?    ?   ?   A . n 
A 1 481  VAL 481  481  ?    ?   ?   A . n 
A 1 482  ARG 482  482  ?    ?   ?   A . n 
A 1 483  VAL 483  483  ?    ?   ?   A . n 
A 1 484  LEU 484  484  ?    ?   ?   A . n 
A 1 485  ARG 485  485  ?    ?   ?   A . n 
A 1 486  PRO 486  486  ?    ?   ?   A . n 
A 1 487  GLN 487  487  ?    ?   ?   A . n 
A 1 488  VAL 488  488  ?    ?   ?   A . n 
A 1 489  THR 489  489  ?    ?   ?   A . n 
A 1 490  ALA 490  490  ?    ?   ?   A . n 
A 1 491  VAL 491  491  ?    ?   ?   A . n 
A 1 492  ALA 492  492  ?    ?   ?   A . n 
A 1 493  GLN 493  493  ?    ?   ?   A . n 
A 1 494  GLN 494  494  ?    ?   ?   A . n 
A 1 495  ASN 495  495  ?    ?   ?   A . n 
A 1 496  GLN 496  496  ?    ?   ?   A . n 
A 1 497  GLY 497  497  ?    ?   ?   A . n 
A 1 498  GLU 498  498  ?    ?   ?   A . n 
A 1 499  VAL 499  499  ?    ?   ?   A . n 
A 1 500  PRO 500  500  ?    ?   ?   A . n 
A 1 501  GLU 501  501  ?    ?   ?   A . n 
A 1 502  PRO 502  502  ?    ?   ?   A . n 
A 1 503  GLN 503  503  ?    ?   ?   A . n 
A 1 504  ASP 504  504  ?    ?   ?   A . n 
A 1 505  MET 505  505  ?    ?   ?   A . n 
A 1 506  LYS 506  506  ?    ?   ?   A . n 
A 1 507  VAL 507  507  ?    ?   ?   A . n 
A 1 508  ALA 508  508  ?    ?   ?   A . n 
A 1 509  GLU 509  509  ?    ?   ?   A . n 
A 1 510  VAL 510  510  ?    ?   ?   A . n 
A 1 511  LEU 511  511  ?    ?   ?   A . n 
A 1 512  PHE 512  512  ?    ?   ?   A . n 
A 1 513  ASP 513  513  ?    ?   ?   A . n 
A 1 514  ALA 514  514  ?    ?   ?   A . n 
A 1 515  ALA 515  515  ?    ?   ?   A . n 
A 1 516  ASP 516  516  ?    ?   ?   A . n 
A 1 517  ALA 517  517  ?    ?   ?   A . n 
A 1 518  ASN 518  518  ?    ?   ?   A . n 
A 1 519  ALA 519  519  ?    ?   ?   A . n 
A 1 520  ILE 520  520  ?    ?   ?   A . n 
A 1 521  GLU 521  521  ?    ?   ?   A . n 
A 1 522  GLU 522  522  ?    ?   ?   A . n 
A 1 523  VAL 523  523  ?    ?   ?   A . n 
A 1 524  ASN 524  524  ?    ?   ?   A . n 
A 1 525  LEU 525  525  ?    ?   ?   A . n 
A 1 526  ALA 526  526  ?    ?   ?   A . n 
A 1 527  TYR 527  527  ?    ?   ?   A . n 
A 1 528  GLU 528  528  ?    ?   ?   A . n 
A 1 529  ASN 529  529  ?    ?   ?   A . n 
A 1 530  VAL 530  530  ?    ?   ?   A . n 
A 1 531  LYS 531  531  ?    ?   ?   A . n 
A 1 532  GLU 532  532  ?    ?   ?   A . n 
A 1 533  VAL 533  533  ?    ?   ?   A . n 
A 1 534  ASP 534  534  ?    ?   ?   A . n 
A 1 535  GLY 535  535  ?    ?   ?   A . n 
A 1 536  LEU 536  536  ?    ?   ?   A . n 
A 1 537  ASP 537  537  ?    ?   ?   A . n 
A 1 538  VAL 538  538  ?    ?   ?   A . n 
A 1 539  SER 539  539  ?    ?   ?   A . n 
A 1 540  LYS 540  540  ?    ?   ?   A . n 
A 1 541  GLU 541  541  ?    ?   ?   A . n 
A 1 542  GLY 542  542  ?    ?   ?   A . n 
A 1 543  THR 543  543  ?    ?   ?   A . n 
A 1 544  GLU 544  544  ?    ?   ?   A . n 
A 1 545  ALA 545  545  ?    ?   ?   A . n 
A 1 546  TRP 546  546  ?    ?   ?   A . n 
A 1 547  GLU 547  547  ?    ?   ?   A . n 
A 1 548  ALA 548  548  ?    ?   ?   A . n 
A 1 549  ALA 549  549  ?    ?   ?   A . n 
A 1 550  MET 550  550  ?    ?   ?   A . n 
A 1 551  LYS 551  551  ?    ?   ?   A . n 
A 1 552  ARG 552  552  ?    ?   ?   A . n 
A 1 553  TYR 553  553  ?    ?   ?   A . n 
A 1 554  ASP 554  554  ?    ?   ?   A . n 
A 1 555  GLU 555  555  ?    ?   ?   A . n 
A 1 556  ARG 556  556  ?    ?   ?   A . n 
A 1 557  ILE 557  557  ?    ?   ?   A . n 
A 1 558  ASP 558  558  ?    ?   ?   A . n 
A 1 559  ARG 559  559  ?    ?   ?   A . n 
A 1 560  VAL 560  560  ?    ?   ?   A . n 
A 1 561  GLU 561  561  ?    ?   ?   A . n 
A 1 562  THR 562  562  ?    ?   ?   A . n 
A 1 563  ARG 563  563  ?    ?   ?   A . n 
A 1 564  ILE 564  564  ?    ?   ?   A . n 
A 1 565  THR 565  565  ?    ?   ?   A . n 
A 1 566  ALA 566  566  ?    ?   ?   A . n 
A 1 567  ARG 567  567  ?    ?   ?   A . n 
A 1 568  LEU 568  568  ?    ?   ?   A . n 
A 1 569  ARG 569  569  ?    ?   ?   A . n 
A 1 570  ASP 570  570  ?    ?   ?   A . n 
A 1 571  GLN 571  571  ?    ?   ?   A . n 
A 1 572  LEU 572  572  ?    ?   ?   A . n 
A 1 573  GLY 573  573  ?    ?   ?   A . n 
A 1 574  THR 574  574  ?    ?   ?   A . n 
A 1 575  ALA 575  575  ?    ?   ?   A . n 
A 1 576  LYS 576  576  ?    ?   ?   A . n 
A 1 577  ASN 577  577  ?    ?   ?   A . n 
A 1 578  ALA 578  578  ?    ?   ?   A . n 
A 1 579  ASN 579  579  ?    ?   ?   A . n 
A 1 580  GLU 580  580  ?    ?   ?   A . n 
A 1 581  MET 581  581  ?    ?   ?   A . n 
A 1 582  PHE 582  582  ?    ?   ?   A . n 
A 1 583  ARG 583  583  ?    ?   ?   A . n 
A 1 584  ILE 584  584  ?    ?   ?   A . n 
A 1 585  PHE 585  585  ?    ?   ?   A . n 
A 1 586  SER 586  586  ?    ?   ?   A . n 
A 1 587  ARG 587  587  ?    ?   ?   A . n 
A 1 588  PHE 588  588  ?    ?   ?   A . n 
A 1 589  ASN 589  589  ?    ?   ?   A . n 
A 1 590  ALA 590  590  ?    ?   ?   A . n 
A 1 591  LEU 591  591  ?    ?   ?   A . n 
A 1 592  PHE 592  592  ?    ?   ?   A . n 
A 1 593  VAL 593  593  ?    ?   ?   A . n 
A 1 594  ARG 594  594  ?    ?   ?   A . n 
A 1 595  PRO 595  595  ?    ?   ?   A . n 
A 1 596  HIS 596  596  ?    ?   ?   A . n 
A 1 597  ILE 597  597  ?    ?   ?   A . n 
A 1 598  ARG 598  598  ?    ?   ?   A . n 
A 1 599  GLY 599  599  ?    ?   ?   A . n 
A 1 600  ALA 600  600  ?    ?   ?   A . n 
A 1 601  ILE 601  601  ?    ?   ?   A . n 
A 1 602  ARG 602  602  ?    ?   ?   A . n 
A 1 603  GLU 603  603  ?    ?   ?   A . n 
A 1 604  TYR 604  604  ?    ?   ?   A . n 
A 1 605  GLN 605  605  ?    ?   ?   A . n 
A 1 606  THR 606  606  ?    ?   ?   A . n 
A 1 607  GLN 607  607  ?    ?   ?   A . n 
A 1 608  LEU 608  608  ?    ?   ?   A . n 
A 1 609  ILE 609  609  ?    ?   ?   A . n 
A 1 610  GLN 610  610  ?    ?   ?   A . n 
A 1 611  ARG 611  611  ?    ?   ?   A . n 
A 1 612  VAL 612  612  ?    ?   ?   A . n 
A 1 613  LYS 613  613  ?    ?   ?   A . n 
A 1 614  ASP 614  614  ?    ?   ?   A . n 
A 1 615  ASP 615  615  ?    ?   ?   A . n 
A 1 616  ILE 616  616  ?    ?   ?   A . n 
A 1 617  GLU 617  617  ?    ?   ?   A . n 
A 1 618  SER 618  618  ?    ?   ?   A . n 
A 1 619  LEU 619  619  ?    ?   ?   A . n 
A 1 620  HIS 620  620  ?    ?   ?   A . n 
A 1 621  ASP 621  621  ?    ?   ?   A . n 
A 1 622  LYS 622  622  ?    ?   ?   A . n 
A 1 623  PHE 623  623  ?    ?   ?   A . n 
A 1 624  LYS 624  624  ?    ?   ?   A . n 
A 1 625  VAL 625  625  ?    ?   ?   A . n 
A 1 626  GLN 626  626  ?    ?   ?   A . n 
A 1 627  TYR 627  627  ?    ?   ?   A . n 
A 1 628  PRO 628  628  ?    ?   ?   A . n 
A 1 629  GLN 629  629  ?    ?   ?   A . n 
A 1 630  SER 630  630  ?    ?   ?   A . n 
A 1 631  GLN 631  631  ?    ?   ?   A . n 
A 1 632  ALA 632  632  ?    ?   ?   A . n 
A 1 633  CYS 633  633  ?    ?   ?   A . n 
A 1 634  LYS 634  634  ?    ?   ?   A . n 
A 1 635  MET 635  635  ?    ?   ?   A . n 
A 1 636  SER 636  636  ?    ?   ?   A . n 
A 1 637  HIS 637  637  ?    ?   ?   A . n 
A 1 638  VAL 638  638  ?    ?   ?   A . n 
A 1 639  ARG 639  639  ?    ?   ?   A . n 
A 1 640  ASP 640  640  ?    ?   ?   A . n 
A 1 641  LEU 641  641  ?    ?   ?   A . n 
A 1 642  PRO 642  642  ?    ?   ?   A . n 
A 1 643  PRO 643  643  ?    ?   ?   A . n 
A 1 644  VAL 644  644  ?    ?   ?   A . n 
A 1 645  SER 645  645  ?    ?   ?   A . n 
A 1 646  GLY 646  646  ?    ?   ?   A . n 
A 1 647  SER 647  647  ?    ?   ?   A . n 
A 1 648  ILE 648  648  ?    ?   ?   A . n 
A 1 649  ILE 649  649  ?    ?   ?   A . n 
A 1 650  TRP 650  650  ?    ?   ?   A . n 
A 1 651  ALA 651  651  ?    ?   ?   A . n 
A 1 652  LYS 652  652  ?    ?   ?   A . n 
A 1 653  GLN 653  653  ?    ?   ?   A . n 
A 1 654  ILE 654  654  ?    ?   ?   A . n 
A 1 655  ASP 655  655  ?    ?   ?   A . n 
A 1 656  ARG 656  656  ?    ?   ?   A . n 
A 1 657  GLN 657  657  ?    ?   ?   A . n 
A 1 658  LEU 658  658  ?    ?   ?   A . n 
A 1 659  THR 659  659  ?    ?   ?   A . n 
A 1 660  ALA 660  660  ?    ?   ?   A . n 
A 1 661  TYR 661  661  ?    ?   ?   A . n 
A 1 662  MET 662  662  ?    ?   ?   A . n 
A 1 663  LYS 663  663  ?    ?   ?   A . n 
A 1 664  ARG 664  664  ?    ?   ?   A . n 
A 1 665  VAL 665  665  ?    ?   ?   A . n 
A 1 666  GLU 666  666  ?    ?   ?   A . n 
A 1 667  ASP 667  667  ?    ?   ?   A . n 
A 1 668  VAL 668  668  ?    ?   ?   A . n 
A 1 669  LEU 669  669  ?    ?   ?   A . n 
A 1 670  GLY 670  670  ?    ?   ?   A . n 
A 1 671  LYS 671  671  ?    ?   ?   A . n 
A 1 672  GLY 672  672  ?    ?   ?   A . n 
A 1 673  TRP 673  673  ?    ?   ?   A . n 
A 1 674  GLU 674  674  ?    ?   ?   A . n 
A 1 675  ASN 675  675  ?    ?   ?   A . n 
A 1 676  HIS 676  676  ?    ?   ?   A . n 
A 1 677  VAL 677  677  ?    ?   ?   A . n 
A 1 678  GLU 678  678  ?    ?   ?   A . n 
A 1 679  GLY 679  679  ?    ?   ?   A . n 
A 1 680  GLN 680  680  ?    ?   ?   A . n 
A 1 681  LYS 681  681  ?    ?   ?   A . n 
A 1 682  LEU 682  682  ?    ?   ?   A . n 
A 1 683  LYS 683  683  ?    ?   ?   A . n 
A 1 684  GLN 684  684  ?    ?   ?   A . n 
A 1 685  ASP 685  685  ?    ?   ?   A . n 
A 1 686  GLY 686  686  ?    ?   ?   A . n 
A 1 687  ASP 687  687  ?    ?   ?   A . n 
A 1 688  SER 688  688  ?    ?   ?   A . n 
A 1 689  PHE 689  689  ?    ?   ?   A . n 
A 1 690  ARG 690  690  ?    ?   ?   A . n 
A 1 691  MET 691  691  ?    ?   ?   A . n 
A 1 692  LYS 692  692  ?    ?   ?   A . n 
A 1 693  LEU 693  693  ?    ?   ?   A . n 
A 1 694  ASN 694  694  ?    ?   ?   A . n 
A 1 695  THR 695  695  ?    ?   ?   A . n 
A 1 696  GLN 696  696  ?    ?   ?   A . n 
A 1 697  GLU 697  697  ?    ?   ?   A . n 
A 1 698  ILE 698  698  ?    ?   ?   A . n 
A 1 699  PHE 699  699  ?    ?   ?   A . n 
A 1 700  ASP 700  700  ?    ?   ?   A . n 
A 1 701  ASP 701  701  ?    ?   ?   A . n 
A 1 702  TRP 702  702  ?    ?   ?   A . n 
A 1 703  ALA 703  703  ?    ?   ?   A . n 
A 1 704  ARG 704  704  ?    ?   ?   A . n 
A 1 705  LYS 705  705  ?    ?   ?   A . n 
A 1 706  VAL 706  706  ?    ?   ?   A . n 
A 1 707  GLN 707  707  ?    ?   ?   A . n 
A 1 708  GLN 708  708  ?    ?   ?   A . n 
A 1 709  ARG 709  709  ?    ?   ?   A . n 
A 1 710  ASN 710  710  ?    ?   ?   A . n 
A 1 711  LEU 711  711  ?    ?   ?   A . n 
A 1 712  GLY 712  712  ?    ?   ?   A . n 
A 1 713  VAL 713  713  ?    ?   ?   A . n 
A 1 714  SER 714  714  ?    ?   ?   A . n 
A 1 715  GLY 715  715  ?    ?   ?   A . n 
A 1 716  ARG 716  716  ?    ?   ?   A . n 
A 1 717  ILE 717  717  ?    ?   ?   A . n 
A 1 718  PHE 718  718  ?    ?   ?   A . n 
A 1 719  THR 719  719  ?    ?   ?   A . n 
A 1 720  ILE 720  720  ?    ?   ?   A . n 
A 1 721  GLU 721  721  ?    ?   ?   A . n 
A 1 722  SER 722  722  ?    ?   ?   A . n 
A 1 723  THR 723  723  ?    ?   ?   A . n 
A 1 724  ARG 724  724  ?    ?   ?   A . n 
A 1 725  VAL 725  725  ?    ?   ?   A . n 
A 1 726  ARG 726  726  ?    ?   ?   A . n 
A 1 727  GLY 727  727  ?    ?   ?   A . n 
A 1 728  ARG 728  728  ?    ?   ?   A . n 
A 1 729  THR 729  729  ?    ?   ?   A . n 
A 1 730  GLY 730  730  ?    ?   ?   A . n 
A 1 731  ASN 731  731  ?    ?   ?   A . n 
A 1 732  VAL 732  732  ?    ?   ?   A . n 
A 1 733  LEU 733  733  ?    ?   ?   A . n 
A 1 734  LYS 734  734  ?    ?   ?   A . n 
A 1 735  LEU 735  735  ?    ?   ?   A . n 
A 1 736  LYS 736  736  ?    ?   ?   A . n 
A 1 737  VAL 737  737  ?    ?   ?   A . n 
A 1 738  ASN 738  738  ?    ?   ?   A . n 
A 1 739  PHE 739  739  ?    ?   ?   A . n 
A 1 740  LEU 740  740  ?    ?   ?   A . n 
A 1 741  PRO 741  741  ?    ?   ?   A . n 
A 1 742  GLU 742  742  ?    ?   ?   A . n 
A 1 743  ILE 743  743  ?    ?   ?   A . n 
A 1 744  ILE 744  744  ?    ?   ?   A . n 
A 1 745  THR 745  745  ?    ?   ?   A . n 
A 1 746  LEU 746  746  ?    ?   ?   A . n 
A 1 747  SER 747  747  ?    ?   ?   A . n 
A 1 748  LYS 748  748  ?    ?   ?   A . n 
A 1 749  GLU 749  749  ?    ?   ?   A . n 
A 1 750  VAL 750  750  ?    ?   ?   A . n 
A 1 751  ARG 751  751  ?    ?   ?   A . n 
A 1 752  ASN 752  752  ?    ?   ?   A . n 
A 1 753  LEU 753  753  ?    ?   ?   A . n 
A 1 754  LYS 754  754  ?    ?   ?   A . n 
A 1 755  TRP 755  755  ?    ?   ?   A . n 
A 1 756  LEU 756  756  ?    ?   ?   A . n 
A 1 757  GLY 757  757  ?    ?   ?   A . n 
A 1 758  PHE 758  758  ?    ?   ?   A . n 
A 1 759  ARG 759  759  ?    ?   ?   A . n 
A 1 760  VAL 760  760  ?    ?   ?   A . n 
A 1 761  PRO 761  761  ?    ?   ?   A . n 
A 1 762  LEU 762  762  ?    ?   ?   A . n 
A 1 763  ALA 763  763  ?    ?   ?   A . n 
A 1 764  ILE 764  764  ?    ?   ?   A . n 
A 1 765  VAL 765  765  ?    ?   ?   A . n 
A 1 766  ASN 766  766  ?    ?   ?   A . n 
A 1 767  LYS 767  767  ?    ?   ?   A . n 
A 1 768  ALA 768  768  ?    ?   ?   A . n 
A 1 769  HIS 769  769  ?    ?   ?   A . n 
A 1 770  GLN 770  770  ?    ?   ?   A . n 
A 1 771  ALA 771  771  ?    ?   ?   A . n 
A 1 772  ASN 772  772  ?    ?   ?   A . n 
A 1 773  GLN 773  773  ?    ?   ?   A . n 
A 1 774  LEU 774  774  ?    ?   ?   A . n 
A 1 775  TYR 775  775  ?    ?   ?   A . n 
A 1 776  PRO 776  776  ?    ?   ?   A . n 
A 1 777  PHE 777  777  ?    ?   ?   A . n 
A 1 778  ALA 778  778  ?    ?   ?   A . n 
A 1 779  ILE 779  779  ?    ?   ?   A . n 
A 1 780  SER 780  780  ?    ?   ?   A . n 
A 1 781  LEU 781  781  ?    ?   ?   A . n 
A 1 782  ILE 782  782  ?    ?   ?   A . n 
A 1 783  GLU 783  783  ?    ?   ?   A . n 
A 1 784  SER 784  784  ?    ?   ?   A . n 
A 1 785  VAL 785  785  ?    ?   ?   A . n 
A 1 786  ARG 786  786  ?    ?   ?   A . n 
A 1 787  THR 787  787  ?    ?   ?   A . n 
A 1 788  TYR 788  788  ?    ?   ?   A . n 
A 1 789  GLU 789  789  ?    ?   ?   A . n 
A 1 790  ARG 790  790  ?    ?   ?   A . n 
A 1 791  THR 791  791  ?    ?   ?   A . n 
A 1 792  CYS 792  792  ?    ?   ?   A . n 
A 1 793  GLU 793  793  ?    ?   ?   A . n 
A 1 794  LYS 794  794  ?    ?   ?   A . n 
A 1 795  VAL 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLU 797  797  ?    ?   ?   A . n 
A 1 798  ARG 798  798  ?    ?   ?   A . n 
A 1 799  ASN 799  799  ?    ?   ?   A . n 
A 1 800  THR 800  800  ?    ?   ?   A . n 
A 1 801  ILE 801  801  ?    ?   ?   A . n 
A 1 802  SER 802  802  ?    ?   ?   A . n 
A 1 803  LEU 803  803  ?    ?   ?   A . n 
A 1 804  LEU 804  804  ?    ?   ?   A . n 
A 1 805  VAL 805  805  ?    ?   ?   A . n 
A 1 806  ALA 806  806  ?    ?   ?   A . n 
A 1 807  GLY 807  807  ?    ?   ?   A . n 
A 1 808  LEU 808  808  ?    ?   ?   A . n 
A 1 809  LYS 809  809  ?    ?   ?   A . n 
A 1 810  LYS 810  810  ?    ?   ?   A . n 
A 1 811  GLU 811  811  ?    ?   ?   A . n 
A 1 812  VAL 812  812  ?    ?   ?   A . n 
A 1 813  GLN 813  813  ?    ?   ?   A . n 
A 1 814  ALA 814  814  ?    ?   ?   A . n 
A 1 815  LEU 815  815  ?    ?   ?   A . n 
A 1 816  ILE 816  816  ?    ?   ?   A . n 
A 1 817  ALA 817  817  ?    ?   ?   A . n 
A 1 818  GLU 818  818  ?    ?   ?   A . n 
A 1 819  GLY 819  819  ?    ?   ?   A . n 
A 1 820  ILE 820  820  ?    ?   ?   A . n 
A 1 821  ALA 821  821  ?    ?   ?   A . n 
A 1 822  LEU 822  822  ?    ?   ?   A . n 
A 1 823  VAL 823  823  ?    ?   ?   A . n 
A 1 824  TRP 824  824  ?    ?   ?   A . n 
A 1 825  GLU 825  825  ?    ?   ?   A . n 
A 1 826  SER 826  826  ?    ?   ?   A . n 
A 1 827  TYR 827  827  ?    ?   ?   A . n 
A 1 828  LYS 828  828  ?    ?   ?   A . n 
A 1 829  LEU 829  829  ?    ?   ?   A . n 
A 1 830  ASP 830  830  ?    ?   ?   A . n 
A 1 831  PRO 831  831  ?    ?   ?   A . n 
A 1 832  TYR 832  832  ?    ?   ?   A . n 
A 1 833  VAL 833  833  ?    ?   ?   A . n 
A 1 834  GLN 834  834  ?    ?   ?   A . n 
A 1 835  ARG 835  835  ?    ?   ?   A . n 
A 1 836  LEU 836  836  ?    ?   ?   A . n 
A 1 837  ALA 837  837  ?    ?   ?   A . n 
A 1 838  GLU 838  838  ?    ?   ?   A . n 
A 1 839  THR 839  839  ?    ?   ?   A . n 
A 1 840  VAL 840  840  ?    ?   ?   A . n 
A 1 841  PHE 841  841  ?    ?   ?   A . n 
A 1 842  ASN 842  842  ?    ?   ?   A . n 
A 1 843  PHE 843  843  ?    ?   ?   A . n 
A 1 844  GLN 844  844  ?    ?   ?   A . n 
A 1 845  GLU 845  845  ?    ?   ?   A . n 
A 1 846  LYS 846  846  ?    ?   ?   A . n 
A 1 847  VAL 847  847  ?    ?   ?   A . n 
A 1 848  ASP 848  848  ?    ?   ?   A . n 
A 1 849  ASP 849  849  ?    ?   ?   A . n 
A 1 850  LEU 850  850  ?    ?   ?   A . n 
A 1 851  LEU 851  851  ?    ?   ?   A . n 
A 1 852  ILE 852  852  ?    ?   ?   A . n 
A 1 853  ILE 853  853  ?    ?   ?   A . n 
A 1 854  GLU 854  854  ?    ?   ?   A . n 
A 1 855  GLU 855  855  ?    ?   ?   A . n 
A 1 856  LYS 856  856  ?    ?   ?   A . n 
A 1 857  ILE 857  857  ?    ?   ?   A . n 
A 1 858  ASP 858  858  ?    ?   ?   A . n 
A 1 859  LEU 859  859  ?    ?   ?   A . n 
A 1 860  GLU 860  860  ?    ?   ?   A . n 
A 1 861  VAL 861  861  ?    ?   ?   A . n 
A 1 862  ARG 862  862  ?    ?   ?   A . n 
A 1 863  SER 863  863  ?    ?   ?   A . n 
A 1 864  LEU 864  864  ?    ?   ?   A . n 
A 1 865  GLU 865  865  ?    ?   ?   A . n 
A 1 866  THR 866  866  ?    ?   ?   A . n 
A 1 867  CYS 867  867  ?    ?   ?   A . n 
A 1 868  MET 868  868  ?    ?   ?   A . n 
A 1 869  TYR 869  869  ?    ?   ?   A . n 
A 1 870  ASP 870  870  ?    ?   ?   A . n 
A 1 871  HIS 871  871  ?    ?   ?   A . n 
A 1 872  LYS 872  872  ?    ?   ?   A . n 
A 1 873  THR 873  873  ?    ?   ?   A . n 
A 1 874  PHE 874  874  ?    ?   ?   A . n 
A 1 875  SER 875  875  ?    ?   ?   A . n 
A 1 876  GLU 876  876  ?    ?   ?   A . n 
A 1 877  ILE 877  877  ?    ?   ?   A . n 
A 1 878  LEU 878  878  ?    ?   ?   A . n 
A 1 879  ASN 879  879  ?    ?   ?   A . n 
A 1 880  ARG 880  880  ?    ?   ?   A . n 
A 1 881  VAL 881  881  ?    ?   ?   A . n 
A 1 882  GLN 882  882  ?    ?   ?   A . n 
A 1 883  LYS 883  883  ?    ?   ?   A . n 
A 1 884  ALA 884  884  ?    ?   ?   A . n 
A 1 885  VAL 885  885  ?    ?   ?   A . n 
A 1 886  ASP 886  886  ?    ?   ?   A . n 
A 1 887  ASP 887  887  ?    ?   ?   A . n 
A 1 888  LEU 888  888  ?    ?   ?   A . n 
A 1 889  ASN 889  889  ?    ?   ?   A . n 
A 1 890  LEU 890  890  ?    ?   ?   A . n 
A 1 891  HIS 891  891  ?    ?   ?   A . n 
A 1 892  SER 892  892  ?    ?   ?   A . n 
A 1 893  TYR 893  893  ?    ?   ?   A . n 
A 1 894  SER 894  894  ?    ?   ?   A . n 
A 1 895  ASN 895  895  ?    ?   ?   A . n 
A 1 896  LEU 896  896  ?    ?   ?   A . n 
A 1 897  PRO 897  897  ?    ?   ?   A . n 
A 1 898  ILE 898  898  ?    ?   ?   A . n 
A 1 899  TRP 899  899  ?    ?   ?   A . n 
A 1 900  VAL 900  900  ?    ?   ?   A . n 
A 1 901  ASN 901  901  ?    ?   ?   A . n 
A 1 902  LYS 902  902  ?    ?   ?   A . n 
A 1 903  LEU 903  903  ?    ?   ?   A . n 
A 1 904  ASP 904  904  ?    ?   ?   A . n 
A 1 905  MET 905  905  ?    ?   ?   A . n 
A 1 906  GLU 906  906  ?    ?   ?   A . n 
A 1 907  ILE 907  907  ?    ?   ?   A . n 
A 1 908  GLU 908  908  ?    ?   ?   A . n 
A 1 909  ARG 909  909  ?    ?   ?   A . n 
A 1 910  ILE 910  910  ?    ?   ?   A . n 
A 1 911  LEU 911  911  ?    ?   ?   A . n 
A 1 912  GLY 912  912  ?    ?   ?   A . n 
A 1 913  VAL 913  913  ?    ?   ?   A . n 
A 1 914  ARG 914  914  ?    ?   ?   A . n 
A 1 915  LEU 915  915  ?    ?   ?   A . n 
A 1 916  GLN 916  916  ?    ?   ?   A . n 
A 1 917  ALA 917  917  ?    ?   ?   A . n 
A 1 918  GLY 918  918  ?    ?   ?   A . n 
A 1 919  LEU 919  919  ?    ?   ?   A . n 
A 1 920  ARG 920  920  ?    ?   ?   A . n 
A 1 921  ALA 921  921  ?    ?   ?   A . n 
A 1 922  TRP 922  922  ?    ?   ?   A . n 
A 1 923  THR 923  923  ?    ?   ?   A . n 
A 1 924  GLN 924  924  ?    ?   ?   A . n 
A 1 925  VAL 925  925  ?    ?   ?   A . n 
A 1 926  LEU 926  926  ?    ?   ?   A . n 
A 1 927  LEU 927  927  ?    ?   ?   A . n 
A 1 928  GLY 928  928  ?    ?   ?   A . n 
A 1 929  GLN 929  929  ?    ?   ?   A . n 
A 1 930  ALA 930  930  ?    ?   ?   A . n 
A 1 931  GLU 931  931  ?    ?   ?   A . n 
A 1 932  ASP 932  932  ?    ?   ?   A . n 
A 1 933  LYS 933  933  ?    ?   ?   A . n 
A 1 934  ALA 934  934  ?    ?   ?   A . n 
A 1 935  GLU 935  935  ?    ?   ?   A . n 
A 1 936  VAL 936  936  ?    ?   ?   A . n 
A 1 937  ASP 937  937  ?    ?   ?   A . n 
A 1 938  MET 938  938  ?    ?   ?   A . n 
A 1 939  ASP 939  939  ?    ?   ?   A . n 
A 1 940  THR 940  940  ?    ?   ?   A . n 
A 1 941  ASP 941  941  ?    ?   ?   A . n 
A 1 942  ALA 942  942  ?    ?   ?   A . n 
A 1 943  PRO 943  943  ?    ?   ?   A . n 
A 1 944  GLN 944  944  ?    ?   ?   A . n 
A 1 945  VAL 945  945  ?    ?   ?   A . n 
A 1 946  SER 946  946  ?    ?   ?   A . n 
A 1 947  HIS 947  947  ?    ?   ?   A . n 
A 1 948  LYS 948  948  ?    ?   ?   A . n 
A 1 949  PRO 949  949  ?    ?   ?   A . n 
A 1 950  GLY 950  950  ?    ?   ?   A . n 
A 1 951  GLY 951  951  ?    ?   ?   A . n 
A 1 952  GLU 952  952  ?    ?   ?   A . n 
A 1 953  PRO 953  953  ?    ?   ?   A . n 
A 1 954  LYS 954  954  ?    ?   ?   A . n 
A 1 955  ILE 955  955  ?    ?   ?   A . n 
A 1 956  LYS 956  956  ?    ?   ?   A . n 
A 1 957  ASN 957  957  ?    ?   ?   A . n 
A 1 958  VAL 958  958  ?    ?   ?   A . n 
A 1 959  VAL 959  959  ?    ?   ?   A . n 
A 1 960  HIS 960  960  ?    ?   ?   A . n 
A 1 961  GLU 961  961  ?    ?   ?   A . n 
A 1 962  LEU 962  962  ?    ?   ?   A . n 
A 1 963  ARG 963  963  ?    ?   ?   A . n 
A 1 964  ILE 964  964  ?    ?   ?   A . n 
A 1 965  THR 965  965  ?    ?   ?   A . n 
A 1 966  ASN 966  966  ?    ?   ?   A . n 
A 1 967  GLN 967  967  ?    ?   ?   A . n 
A 1 968  VAL 968  968  ?    ?   ?   A . n 
A 1 969  ILE 969  969  ?    ?   ?   A . n 
A 1 970  TYR 970  970  ?    ?   ?   A . n 
A 1 971  LEU 971  971  ?    ?   ?   A . n 
A 1 972  ASN 972  972  ?    ?   ?   A . n 
A 1 973  PRO 973  973  ?    ?   ?   A . n 
A 1 974  PRO 974  974  ?    ?   ?   A . n 
A 1 975  ILE 975  975  ?    ?   ?   A . n 
A 1 976  GLU 976  976  ?    ?   ?   A . n 
A 1 977  GLU 977  977  ?    ?   ?   A . n 
A 1 978  CYS 978  978  ?    ?   ?   A . n 
A 1 979  ARG 979  979  ?    ?   ?   A . n 
A 1 980  TYR 980  980  ?    ?   ?   A . n 
A 1 981  LYS 981  981  ?    ?   ?   A . n 
A 1 982  LEU 982  982  ?    ?   ?   A . n 
A 1 983  TYR 983  983  ?    ?   ?   A . n 
A 1 984  GLN 984  984  ?    ?   ?   A . n 
A 1 985  GLU 985  985  ?    ?   ?   A . n 
A 1 986  MET 986  986  ?    ?   ?   A . n 
A 1 987  PHE 987  987  ?    ?   ?   A . n 
A 1 988  ALA 988  988  ?    ?   ?   A . n 
A 1 989  TRP 989  989  ?    ?   ?   A . n 
A 1 990  LYS 990  990  ?    ?   ?   A . n 
A 1 991  MET 991  991  ?    ?   ?   A . n 
A 1 992  VAL 992  992  ?    ?   ?   A . n 
A 1 993  VAL 993  993  ?    ?   ?   A . n 
A 1 994  LEU 994  994  ?    ?   ?   A . n 
A 1 995  SER 995  995  ?    ?   ?   A . n 
A 1 996  LEU 996  996  ?    ?   ?   A . n 
A 1 997  PRO 997  997  ?    ?   ?   A . n 
A 1 998  ARG 998  998  ?    ?   ?   A . n 
A 1 999  ILE 999  999  ?    ?   ?   A . n 
A 1 1000 GLN 1000 1000 ?    ?   ?   A . n 
A 1 1001 SER 1001 1001 ?    ?   ?   A . n 
A 1 1002 GLN 1002 1002 ?    ?   ?   A . n 
A 1 1003 ARG 1003 1003 ?    ?   ?   A . n 
A 1 1004 TYR 1004 1004 ?    ?   ?   A . n 
A 1 1005 GLN 1005 1005 ?    ?   ?   A . n 
A 1 1006 VAL 1006 1006 ?    ?   ?   A . n 
A 1 1007 GLY 1007 1007 ?    ?   ?   A . n 
A 1 1008 VAL 1008 1008 ?    ?   ?   A . n 
A 1 1009 HIS 1009 1009 ?    ?   ?   A . n 
A 1 1010 TYR 1010 1010 ?    ?   ?   A . n 
A 1 1011 GLU 1011 1011 ?    ?   ?   A . n 
A 1 1012 LEU 1012 1012 ?    ?   ?   A . n 
A 1 1013 THR 1013 1013 ?    ?   ?   A . n 
A 1 1014 GLU 1014 1014 ?    ?   ?   A . n 
A 1 1015 GLU 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLU 1016 1016 ?    ?   ?   A . n 
A 1 1017 LYS 1017 1017 ?    ?   ?   A . n 
A 1 1018 PHE 1018 1018 ?    ?   ?   A . n 
A 1 1019 TYR 1019 1019 ?    ?   ?   A . n 
A 1 1020 ARG 1020 1020 ?    ?   ?   A . n 
A 1 1021 ASN 1021 1021 ?    ?   ?   A . n 
A 1 1022 ALA 1022 1022 ?    ?   ?   A . n 
A 1 1023 LEU 1023 1023 ?    ?   ?   A . n 
A 1 1024 THR 1024 1024 ?    ?   ?   A . n 
A 1 1025 ARG 1025 1025 ?    ?   ?   A . n 
A 1 1026 MET 1026 1026 ?    ?   ?   A . n 
A 1 1027 PRO 1027 1027 ?    ?   ?   A . n 
A 1 1028 ASP 1028 1028 ?    ?   ?   A . n 
A 1 1029 GLY 1029 1029 ?    ?   ?   A . n 
A 1 1030 PRO 1030 1030 ?    ?   ?   A . n 
A 1 1031 VAL 1031 1031 ?    ?   ?   A . n 
A 1 1032 ALA 1032 1032 ?    ?   ?   A . n 
A 1 1033 LEU 1033 1033 ?    ?   ?   A . n 
A 1 1034 GLU 1034 1034 ?    ?   ?   A . n 
A 1 1035 GLU 1035 1035 ?    ?   ?   A . n 
A 1 1036 SER 1036 1036 ?    ?   ?   A . n 
A 1 1037 TYR 1037 1037 ?    ?   ?   A . n 
A 1 1038 SER 1038 1038 ?    ?   ?   A . n 
A 1 1039 ALA 1039 1039 ?    ?   ?   A . n 
A 1 1040 VAL 1040 1040 ?    ?   ?   A . n 
A 1 1041 MET 1041 1041 ?    ?   ?   A . n 
A 1 1042 GLY 1042 1042 ?    ?   ?   A . n 
A 1 1043 ILE 1043 1043 ?    ?   ?   A . n 
A 1 1044 VAL 1044 1044 ?    ?   ?   A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   A . n 
A 1 1046 GLU 1046 1046 ?    ?   ?   A . n 
A 1 1047 VAL 1047 1047 ?    ?   ?   A . n 
A 1 1048 GLU 1048 1048 ?    ?   ?   A . n 
A 1 1049 GLN 1049 1049 ?    ?   ?   A . n 
A 1 1050 TYR 1050 1050 ?    ?   ?   A . n 
A 1 1051 VAL 1051 1051 ?    ?   ?   A . n 
A 1 1052 LYS 1052 1052 ?    ?   ?   A . n 
A 1 1053 VAL 1053 1053 ?    ?   ?   A . n 
A 1 1054 TRP 1054 1054 ?    ?   ?   A . n 
A 1 1055 LEU 1055 1055 ?    ?   ?   A . n 
A 1 1056 GLN 1056 1056 ?    ?   ?   A . n 
A 1 1057 TYR 1057 1057 ?    ?   ?   A . n 
A 1 1058 GLN 1058 1058 ?    ?   ?   A . n 
A 1 1059 CYS 1059 1059 ?    ?   ?   A . n 
A 1 1060 LEU 1060 1060 ?    ?   ?   A . n 
A 1 1061 TRP 1061 1061 ?    ?   ?   A . n 
A 1 1062 ASP 1062 1062 ?    ?   ?   A . n 
A 1 1063 MET 1063 1063 ?    ?   ?   A . n 
A 1 1064 GLN 1064 1064 ?    ?   ?   A . n 
A 1 1065 ALA 1065 1065 ?    ?   ?   A . n 
A 1 1066 GLU 1066 1066 ?    ?   ?   A . n 
A 1 1067 ASN 1067 1067 ?    ?   ?   A . n 
A 1 1068 ILE 1068 1068 ?    ?   ?   A . n 
A 1 1069 TYR 1069 1069 ?    ?   ?   A . n 
A 1 1070 ASN 1070 1070 ?    ?   ?   A . n 
A 1 1071 ARG 1071 1071 ?    ?   ?   A . n 
A 1 1072 LEU 1072 1072 ?    ?   ?   A . n 
A 1 1073 GLY 1073 1073 ?    ?   ?   A . n 
A 1 1074 GLU 1074 1074 ?    ?   ?   A . n 
A 1 1075 ASP 1075 1075 ?    ?   ?   A . n 
A 1 1076 LEU 1076 1076 ?    ?   ?   A . n 
A 1 1077 ASN 1077 1077 ?    ?   ?   A . n 
A 1 1078 LYS 1078 1078 ?    ?   ?   A . n 
A 1 1079 TRP 1079 1079 ?    ?   ?   A . n 
A 1 1080 GLN 1080 1080 ?    ?   ?   A . n 
A 1 1081 ALA 1081 1081 ?    ?   ?   A . n 
A 1 1082 LEU 1082 1082 ?    ?   ?   A . n 
A 1 1083 LEU 1083 1083 ?    ?   ?   A . n 
A 1 1084 VAL 1084 1084 ?    ?   ?   A . n 
A 1 1085 GLN 1085 1085 ?    ?   ?   A . n 
A 1 1086 ILE 1086 1086 ?    ?   ?   A . n 
A 1 1087 ARG 1087 1087 ?    ?   ?   A . n 
A 1 1088 LYS 1088 1088 ?    ?   ?   A . n 
A 1 1089 ALA 1089 1089 ?    ?   ?   A . n 
A 1 1090 ARG 1090 1090 ?    ?   ?   A . n 
A 1 1091 GLY 1091 1091 ?    ?   ?   A . n 
A 1 1092 THR 1092 1092 ?    ?   ?   A . n 
A 1 1093 PHE 1093 1093 ?    ?   ?   A . n 
A 1 1094 ASP 1094 1094 ?    ?   ?   A . n 
A 1 1095 ASN 1095 1095 ?    ?   ?   A . n 
A 1 1096 ALA 1096 1096 ?    ?   ?   A . n 
A 1 1097 GLU 1097 1097 ?    ?   ?   A . n 
A 1 1098 THR 1098 1098 ?    ?   ?   A . n 
A 1 1099 LYS 1099 1099 ?    ?   ?   A . n 
A 1 1100 LYS 1100 1100 ?    ?   ?   A . n 
A 1 1101 GLU 1101 1101 ?    ?   ?   A . n 
A 1 1102 PHE 1102 1102 ?    ?   ?   A . n 
A 1 1103 GLY 1103 1103 ?    ?   ?   A . n 
A 1 1104 PRO 1104 1104 ?    ?   ?   A . n 
A 1 1105 VAL 1105 1105 ?    ?   ?   A . n 
A 1 1106 VAL 1106 1106 ?    ?   ?   A . n 
A 1 1107 ILE 1107 1107 ?    ?   ?   A . n 
A 1 1108 ASP 1108 1108 ?    ?   ?   A . n 
A 1 1109 TYR 1109 1109 ?    ?   ?   A . n 
A 1 1110 GLY 1110 1110 ?    ?   ?   A . n 
A 1 1111 LYS 1111 1111 ?    ?   ?   A . n 
A 1 1112 VAL 1112 1112 ?    ?   ?   A . n 
A 1 1113 GLN 1113 1113 ?    ?   ?   A . n 
A 1 1114 SER 1114 1114 ?    ?   ?   A . n 
A 1 1115 LYS 1115 1115 ?    ?   ?   A . n 
A 1 1116 VAL 1116 1116 ?    ?   ?   A . n 
A 1 1117 ASN 1117 1117 ?    ?   ?   A . n 
A 1 1118 LEU 1118 1118 ?    ?   ?   A . n 
A 1 1119 LYS 1119 1119 ?    ?   ?   A . n 
A 1 1120 TYR 1120 1120 ?    ?   ?   A . n 
A 1 1121 ASP 1121 1121 ?    ?   ?   A . n 
A 1 1122 SER 1122 1122 ?    ?   ?   A . n 
A 1 1123 TRP 1123 1123 ?    ?   ?   A . n 
A 1 1124 HIS 1124 1124 ?    ?   ?   A . n 
A 1 1125 LYS 1125 1125 ?    ?   ?   A . n 
A 1 1126 GLU 1126 1126 ?    ?   ?   A . n 
A 1 1127 VAL 1127 1127 ?    ?   ?   A . n 
A 1 1128 LEU 1128 1128 ?    ?   ?   A . n 
A 1 1129 SER 1129 1129 ?    ?   ?   A . n 
A 1 1130 LYS 1130 1130 ?    ?   ?   A . n 
A 1 1131 PHE 1131 1131 ?    ?   ?   A . n 
A 1 1132 GLY 1132 1132 ?    ?   ?   A . n 
A 1 1133 GLN 1133 1133 ?    ?   ?   A . n 
A 1 1134 MET 1134 1134 ?    ?   ?   A . n 
A 1 1135 LEU 1135 1135 ?    ?   ?   A . n 
A 1 1136 GLY 1136 1136 ?    ?   ?   A . n 
A 1 1137 SER 1137 1137 ?    ?   ?   A . n 
A 1 1138 ASN 1138 1138 ?    ?   ?   A . n 
A 1 1139 MET 1139 1139 ?    ?   ?   A . n 
A 1 1140 THR 1140 1140 ?    ?   ?   A . n 
A 1 1141 GLU 1141 1141 ?    ?   ?   A . n 
A 1 1142 PHE 1142 1142 ?    ?   ?   A . n 
A 1 1143 HIS 1143 1143 ?    ?   ?   A . n 
A 1 1144 SER 1144 1144 ?    ?   ?   A . n 
A 1 1145 GLN 1145 1145 ?    ?   ?   A . n 
A 1 1146 ILE 1146 1146 ?    ?   ?   A . n 
A 1 1147 SER 1147 1147 ?    ?   ?   A . n 
A 1 1148 LYS 1148 1148 ?    ?   ?   A . n 
A 1 1149 SER 1149 1149 ?    ?   ?   A . n 
A 1 1150 ARG 1150 1150 ?    ?   ?   A . n 
A 1 1151 GLN 1151 1151 ?    ?   ?   A . n 
A 1 1152 GLU 1152 1152 ?    ?   ?   A . n 
A 1 1153 LEU 1153 1153 ?    ?   ?   A . n 
A 1 1154 GLU 1154 1154 ?    ?   ?   A . n 
A 1 1155 GLN 1155 1155 ?    ?   ?   A . n 
A 1 1156 HIS 1156 1156 ?    ?   ?   A . n 
A 1 1157 SER 1157 1157 ?    ?   ?   A . n 
A 1 1158 VAL 1158 1158 ?    ?   ?   A . n 
A 1 1159 ASP 1159 1159 ?    ?   ?   A . n 
A 1 1160 THR 1160 1160 ?    ?   ?   A . n 
A 1 1161 ALA 1161 1161 ?    ?   ?   A . n 
A 1 1162 SER 1162 1162 ?    ?   ?   A . n 
A 1 1163 THR 1163 1163 ?    ?   ?   A . n 
A 1 1164 SER 1164 1164 ?    ?   ?   A . n 
A 1 1165 ASP 1165 1165 ?    ?   ?   A . n 
A 1 1166 ALA 1166 1166 ?    ?   ?   A . n 
A 1 1167 VAL 1167 1167 ?    ?   ?   A . n 
A 1 1168 THR 1168 1168 ?    ?   ?   A . n 
A 1 1169 PHE 1169 1169 ?    ?   ?   A . n 
A 1 1170 ILE 1170 1170 ?    ?   ?   A . n 
A 1 1171 THR 1171 1171 ?    ?   ?   A . n 
A 1 1172 TYR 1172 1172 ?    ?   ?   A . n 
A 1 1173 VAL 1173 1173 ?    ?   ?   A . n 
A 1 1174 GLN 1174 1174 ?    ?   ?   A . n 
A 1 1175 SER 1175 1175 ?    ?   ?   A . n 
A 1 1176 LEU 1176 1176 ?    ?   ?   A . n 
A 1 1177 LYS 1177 1177 ?    ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?    ?   ?   A . n 
A 1 1179 LYS 1179 1179 ?    ?   ?   A . n 
A 1 1180 ILE 1180 1180 ?    ?   ?   A . n 
A 1 1181 LYS 1181 1181 ?    ?   ?   A . n 
A 1 1182 GLN 1182 1182 ?    ?   ?   A . n 
A 1 1183 PHE 1183 1183 ?    ?   ?   A . n 
A 1 1184 GLU 1184 1184 ?    ?   ?   A . n 
A 1 1185 LYS 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLN 1186 1186 ?    ?   ?   A . n 
A 1 1187 VAL 1187 1187 ?    ?   ?   A . n 
A 1 1188 GLU 1188 1188 ?    ?   ?   A . n 
A 1 1189 LEU 1189 1189 ?    ?   ?   A . n 
A 1 1190 TYR 1190 1190 ?    ?   ?   A . n 
A 1 1191 ARG 1191 1191 ?    ?   ?   A . n 
A 1 1192 ASN 1192 1192 ?    ?   ?   A . n 
A 1 1193 GLY 1193 1193 ?    ?   ?   A . n 
A 1 1194 GLN 1194 1194 ?    ?   ?   A . n 
A 1 1195 ARG 1195 1195 ?    ?   ?   A . n 
A 1 1196 LEU 1196 1196 ?    ?   ?   A . n 
A 1 1197 LEU 1197 1197 ?    ?   ?   A . n 
A 1 1198 GLU 1198 1198 ?    ?   ?   A . n 
A 1 1199 LYS 1199 1199 ?    ?   ?   A . n 
A 1 1200 GLN 1200 1200 ?    ?   ?   A . n 
A 1 1201 ARG 1201 1201 ?    ?   ?   A . n 
A 1 1202 PHE 1202 1202 ?    ?   ?   A . n 
A 1 1203 GLN 1203 1203 ?    ?   ?   A . n 
A 1 1204 PHE 1204 1204 ?    ?   ?   A . n 
A 1 1205 PRO 1205 1205 ?    ?   ?   A . n 
A 1 1206 PRO 1206 1206 ?    ?   ?   A . n 
A 1 1207 SER 1207 1207 ?    ?   ?   A . n 
A 1 1208 TRP 1208 1208 ?    ?   ?   A . n 
A 1 1209 LEU 1209 1209 ?    ?   ?   A . n 
A 1 1210 TYR 1210 1210 ?    ?   ?   A . n 
A 1 1211 ILE 1211 1211 ?    ?   ?   A . n 
A 1 1212 ASP 1212 1212 ?    ?   ?   A . n 
A 1 1213 ASN 1213 1213 ?    ?   ?   A . n 
A 1 1214 ILE 1214 1214 ?    ?   ?   A . n 
A 1 1215 GLU 1215 1215 ?    ?   ?   A . n 
A 1 1216 GLY 1216 1216 ?    ?   ?   A . n 
A 1 1217 GLU 1217 1217 ?    ?   ?   A . n 
A 1 1218 TRP 1218 1218 ?    ?   ?   A . n 
A 1 1219 GLY 1219 1219 ?    ?   ?   A . n 
A 1 1220 ALA 1220 1220 ?    ?   ?   A . n 
A 1 1221 PHE 1221 1221 ?    ?   ?   A . n 
A 1 1222 ASN 1222 1222 ?    ?   ?   A . n 
A 1 1223 ASP 1223 1223 ?    ?   ?   A . n 
A 1 1224 ILE 1224 1224 ?    ?   ?   A . n 
A 1 1225 MET 1225 1225 ?    ?   ?   A . n 
A 1 1226 ARG 1226 1226 ?    ?   ?   A . n 
A 1 1227 ARG 1227 1227 ?    ?   ?   A . n 
A 1 1228 LYS 1228 1228 ?    ?   ?   A . n 
A 1 1229 ASP 1229 1229 ?    ?   ?   A . n 
A 1 1230 SER 1230 1230 ?    ?   ?   A . n 
A 1 1231 ALA 1231 1231 ?    ?   ?   A . n 
A 1 1232 ILE 1232 1232 ?    ?   ?   A . n 
A 1 1233 GLN 1233 1233 ?    ?   ?   A . n 
A 1 1234 GLN 1234 1234 ?    ?   ?   A . n 
A 1 1235 GLN 1235 1235 ?    ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?    ?   ?   A . n 
A 1 1237 ALA 1237 1237 ?    ?   ?   A . n 
A 1 1238 ASN 1238 1238 ?    ?   ?   A . n 
A 1 1239 LEU 1239 1239 ?    ?   ?   A . n 
A 1 1240 GLN 1240 1240 ?    ?   ?   A . n 
A 1 1241 MET 1241 1241 ?    ?   ?   A . n 
A 1 1242 LYS 1242 1242 ?    ?   ?   A . n 
A 1 1243 ILE 1243 1243 ?    ?   ?   A . n 
A 1 1244 VAL 1244 1244 ?    ?   ?   A . n 
A 1 1245 GLN 1245 1245 ?    ?   ?   A . n 
A 1 1246 GLU 1246 1246 ?    ?   ?   A . n 
A 1 1247 ASP 1247 1247 ?    ?   ?   A . n 
A 1 1248 ARG 1248 1248 ?    ?   ?   A . n 
A 1 1249 ALA 1249 1249 ?    ?   ?   A . n 
A 1 1250 VAL 1250 1250 ?    ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?    ?   ?   A . n 
A 1 1252 SER 1252 1252 ?    ?   ?   A . n 
A 1 1253 ARG 1253 1253 ?    ?   ?   A . n 
A 1 1254 THR 1254 1254 ?    ?   ?   A . n 
A 1 1255 THR 1255 1255 ?    ?   ?   A . n 
A 1 1256 ASP 1256 1256 ?    ?   ?   A . n 
A 1 1257 LEU 1257 1257 ?    ?   ?   A . n 
A 1 1258 LEU 1258 1258 ?    ?   ?   A . n 
A 1 1259 THR 1259 1259 ?    ?   ?   A . n 
A 1 1260 ASP 1260 1260 ?    ?   ?   A . n 
A 1 1261 TRP 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLU 1262 1262 ?    ?   ?   A . n 
A 1 1263 LYS 1263 1263 ?    ?   ?   A . n 
A 1 1264 THR 1264 1264 ?    ?   ?   A . n 
A 1 1265 LYS 1265 1265 ?    ?   ?   A . n 
A 1 1266 PRO 1266 1266 ?    ?   ?   A . n 
A 1 1267 VAL 1267 1267 ?    ?   ?   A . n 
A 1 1268 THR 1268 1268 ?    ?   ?   A . n 
A 1 1269 GLY 1269 1269 ?    ?   ?   A . n 
A 1 1270 ASN 1270 1270 ?    ?   ?   A . n 
A 1 1271 LEU 1271 1271 ?    ?   ?   A . n 
A 1 1272 ARG 1272 1272 ?    ?   ?   A . n 
A 1 1273 PRO 1273 1273 ?    ?   ?   A . n 
A 1 1274 GLU 1274 1274 ?    ?   ?   A . n 
A 1 1275 GLU 1275 1275 ?    ?   ?   A . n 
A 1 1276 ALA 1276 1276 ?    ?   ?   A . n 
A 1 1277 LEU 1277 1277 ?    ?   ?   A . n 
A 1 1278 GLN 1278 1278 ?    ?   ?   A . n 
A 1 1279 ALA 1279 1279 ?    ?   ?   A . n 
A 1 1280 LEU 1280 1280 ?    ?   ?   A . n 
A 1 1281 THR 1281 1281 ?    ?   ?   A . n 
A 1 1282 ILE 1282 1282 ?    ?   ?   A . n 
A 1 1283 TYR 1283 1283 ?    ?   ?   A . n 
A 1 1284 GLU 1284 1284 ?    ?   ?   A . n 
A 1 1285 GLY 1285 1285 ?    ?   ?   A . n 
A 1 1286 LYS 1286 1286 ?    ?   ?   A . n 
A 1 1287 PHE 1287 1287 ?    ?   ?   A . n 
A 1 1288 GLY 1288 1288 ?    ?   ?   A . n 
A 1 1289 ARG 1289 1289 ?    ?   ?   A . n 
A 1 1290 LEU 1290 1290 ?    ?   ?   A . n 
A 1 1291 LYS 1291 1291 ?    ?   ?   A . n 
A 1 1292 ASP 1292 1292 ?    ?   ?   A . n 
A 1 1293 ASP 1293 1293 ?    ?   ?   A . n 
A 1 1294 ARG 1294 1294 ?    ?   ?   A . n 
A 1 1295 GLU 1295 1295 ?    ?   ?   A . n 
A 1 1296 LYS 1296 1296 ?    ?   ?   A . n 
A 1 1297 CYS 1297 1297 ?    ?   ?   A . n 
A 1 1298 ALA 1298 1298 ?    ?   ?   A . n 
A 1 1299 LYS 1299 1299 ?    ?   ?   A . n 
A 1 1300 ALA 1300 1300 ?    ?   ?   A . n 
A 1 1301 LYS 1301 1301 ?    ?   ?   A . n 
A 1 1302 GLU 1302 1302 ?    ?   ?   A . n 
A 1 1303 ALA 1303 1303 ?    ?   ?   A . n 
A 1 1304 LEU 1304 1304 ?    ?   ?   A . n 
A 1 1305 GLU 1305 1305 ?    ?   ?   A . n 
A 1 1306 LEU 1306 1306 ?    ?   ?   A . n 
A 1 1307 THR 1307 1307 ?    ?   ?   A . n 
A 1 1308 ASP 1308 1308 ?    ?   ?   A . n 
A 1 1309 THR 1309 1309 ?    ?   ?   A . n 
A 1 1310 GLY 1310 1310 ?    ?   ?   A . n 
A 1 1311 LEU 1311 1311 ?    ?   ?   A . n 
A 1 1312 LEU 1312 1312 ?    ?   ?   A . n 
A 1 1313 SER 1313 1313 ?    ?   ?   A . n 
A 1 1314 GLY 1314 1314 ?    ?   ?   A . n 
A 1 1315 SER 1315 1315 ?    ?   ?   A . n 
A 1 1316 GLU 1316 1316 ?    ?   ?   A . n 
A 1 1317 GLU 1317 1317 ?    ?   ?   A . n 
A 1 1318 ARG 1318 1318 ?    ?   ?   A . n 
A 1 1319 VAL 1319 1319 ?    ?   ?   A . n 
A 1 1320 GLN 1320 1320 ?    ?   ?   A . n 
A 1 1321 VAL 1321 1321 ?    ?   ?   A . n 
A 1 1322 ALA 1322 1322 ?    ?   ?   A . n 
A 1 1323 LEU 1323 1323 ?    ?   ?   A . n 
A 1 1324 GLU 1324 1324 ?    ?   ?   A . n 
A 1 1325 GLU 1325 1325 ?    ?   ?   A . n 
A 1 1326 LEU 1326 1326 ?    ?   ?   A . n 
A 1 1327 GLN 1327 1327 ?    ?   ?   A . n 
A 1 1328 ASP 1328 1328 ?    ?   ?   A . n 
A 1 1329 LEU 1329 1329 ?    ?   ?   A . n 
A 1 1330 LYS 1330 1330 ?    ?   ?   A . n 
A 1 1331 GLY 1331 1331 ?    ?   ?   A . n 
A 1 1332 VAL 1332 1332 ?    ?   ?   A . n 
A 1 1333 TRP 1333 1333 ?    ?   ?   A . n 
A 1 1334 SER 1334 1334 ?    ?   ?   A . n 
A 1 1335 GLU 1335 1335 ?    ?   ?   A . n 
A 1 1336 LEU 1336 1336 ?    ?   ?   A . n 
A 1 1337 SER 1337 1337 ?    ?   ?   A . n 
A 1 1338 LYS 1338 1338 ?    ?   ?   A . n 
A 1 1339 VAL 1339 1339 ?    ?   ?   A . n 
A 1 1340 TRP 1340 1340 ?    ?   ?   A . n 
A 1 1341 GLU 1341 1341 ?    ?   ?   A . n 
A 1 1342 GLN 1342 1342 ?    ?   ?   A . n 
A 1 1343 ILE 1343 1343 ?    ?   ?   A . n 
A 1 1344 ASP 1344 1344 ?    ?   ?   A . n 
A 1 1345 GLN 1345 1345 ?    ?   ?   A . n 
A 1 1346 MET 1346 1346 ?    ?   ?   A . n 
A 1 1347 LYS 1347 1347 ?    ?   ?   A . n 
A 1 1348 GLU 1348 1348 ?    ?   ?   A . n 
A 1 1349 GLN 1349 1349 ?    ?   ?   A . n 
A 1 1350 PRO 1350 1350 ?    ?   ?   A . n 
A 1 1351 TRP 1351 1351 ?    ?   ?   A . n 
A 1 1352 VAL 1352 1352 ?    ?   ?   A . n 
A 1 1353 SER 1353 1353 ?    ?   ?   A . n 
A 1 1354 VAL 1354 1354 ?    ?   ?   A . n 
A 1 1355 GLN 1355 1355 ?    ?   ?   A . n 
A 1 1356 PRO 1356 1356 ?    ?   ?   A . n 
A 1 1357 ARG 1357 1357 ?    ?   ?   A . n 
A 1 1358 LYS 1358 1358 ?    ?   ?   A . n 
A 1 1359 LEU 1359 1359 ?    ?   ?   A . n 
A 1 1360 ARG 1360 1360 ?    ?   ?   A . n 
A 1 1361 GLN 1361 1361 ?    ?   ?   A . n 
A 1 1362 ASN 1362 1362 ?    ?   ?   A . n 
A 1 1363 LEU 1363 1363 ?    ?   ?   A . n 
A 1 1364 ASP 1364 1364 ?    ?   ?   A . n 
A 1 1365 ALA 1365 1365 ?    ?   ?   A . n 
A 1 1366 LEU 1366 1366 ?    ?   ?   A . n 
A 1 1367 LEU 1367 1367 ?    ?   ?   A . n 
A 1 1368 ASN 1368 1368 ?    ?   ?   A . n 
A 1 1369 GLN 1369 1369 ?    ?   ?   A . n 
A 1 1370 LEU 1370 1370 ?    ?   ?   A . n 
A 1 1371 LYS 1371 1371 ?    ?   ?   A . n 
A 1 1372 SER 1372 1372 ?    ?   ?   A . n 
A 1 1373 PHE 1373 1373 ?    ?   ?   A . n 
A 1 1374 PRO 1374 1374 ?    ?   ?   A . n 
A 1 1375 ALA 1375 1375 ?    ?   ?   A . n 
A 1 1376 ARG 1376 1376 ?    ?   ?   A . n 
A 1 1377 LEU 1377 1377 ?    ?   ?   A . n 
A 1 1378 ARG 1378 1378 ?    ?   ?   A . n 
A 1 1379 GLN 1379 1379 ?    ?   ?   A . n 
A 1 1380 TYR 1380 1380 ?    ?   ?   A . n 
A 1 1381 ALA 1381 1381 ?    ?   ?   A . n 
A 1 1382 SER 1382 1382 ?    ?   ?   A . n 
A 1 1383 TYR 1383 1383 ?    ?   ?   A . n 
A 1 1384 GLU 1384 1384 ?    ?   ?   A . n 
A 1 1385 PHE 1385 1385 ?    ?   ?   A . n 
A 1 1386 VAL 1386 1386 ?    ?   ?   A . n 
A 1 1387 GLN 1387 1387 ?    ?   ?   A . n 
A 1 1388 ARG 1388 1388 ?    ?   ?   A . n 
A 1 1389 LEU 1389 1389 ?    ?   ?   A . n 
A 1 1390 LEU 1390 1390 ?    ?   ?   A . n 
A 1 1391 LYS 1391 1391 ?    ?   ?   A . n 
A 1 1392 GLY 1392 1392 ?    ?   ?   A . n 
A 1 1393 TYR 1393 1393 ?    ?   ?   A . n 
A 1 1394 MET 1394 1394 ?    ?   ?   A . n 
A 1 1395 LYS 1395 1395 ?    ?   ?   A . n 
A 1 1396 ILE 1396 1396 ?    ?   ?   A . n 
A 1 1397 ASN 1397 1397 ?    ?   ?   A . n 
A 1 1398 MET 1398 1398 ?    ?   ?   A . n 
A 1 1399 LEU 1399 1399 ?    ?   ?   A . n 
A 1 1400 VAL 1400 1400 ?    ?   ?   A . n 
A 1 1401 ILE 1401 1401 ?    ?   ?   A . n 
A 1 1402 GLU 1402 1402 ?    ?   ?   A . n 
A 1 1403 LEU 1403 1403 ?    ?   ?   A . n 
A 1 1404 LYS 1404 1404 ?    ?   ?   A . n 
A 1 1405 SER 1405 1405 ?    ?   ?   A . n 
A 1 1406 GLU 1406 1406 ?    ?   ?   A . n 
A 1 1407 ALA 1407 1407 ?    ?   ?   A . n 
A 1 1408 LEU 1408 1408 ?    ?   ?   A . n 
A 1 1409 LYS 1409 1409 ?    ?   ?   A . n 
A 1 1410 ASP 1410 1410 ?    ?   ?   A . n 
A 1 1411 ARG 1411 1411 ?    ?   ?   A . n 
A 1 1412 HIS 1412 1412 ?    ?   ?   A . n 
A 1 1413 TRP 1413 1413 ?    ?   ?   A . n 
A 1 1414 LYS 1414 1414 ?    ?   ?   A . n 
A 1 1415 GLN 1415 1415 ?    ?   ?   A . n 
A 1 1416 LEU 1416 1416 ?    ?   ?   A . n 
A 1 1417 MET 1417 1417 ?    ?   ?   A . n 
A 1 1418 LYS 1418 1418 ?    ?   ?   A . n 
A 1 1419 ARG 1419 1419 ?    ?   ?   A . n 
A 1 1420 LEU 1420 1420 ?    ?   ?   A . n 
A 1 1421 HIS 1421 1421 ?    ?   ?   A . n 
A 1 1422 VAL 1422 1422 ?    ?   ?   A . n 
A 1 1423 ASN 1423 1423 ?    ?   ?   A . n 
A 1 1424 TRP 1424 1424 ?    ?   ?   A . n 
A 1 1425 VAL 1425 1425 ?    ?   ?   A . n 
A 1 1426 VAL 1426 1426 ?    ?   ?   A . n 
A 1 1427 SER 1427 1427 ?    ?   ?   A . n 
A 1 1428 GLU 1428 1428 ?    ?   ?   A . n 
A 1 1429 LEU 1429 1429 ?    ?   ?   A . n 
A 1 1430 THR 1430 1430 ?    ?   ?   A . n 
A 1 1431 LEU 1431 1431 ?    ?   ?   A . n 
A 1 1432 GLY 1432 1432 ?    ?   ?   A . n 
A 1 1433 GLN 1433 1433 ?    ?   ?   A . n 
A 1 1434 ILE 1434 1434 ?    ?   ?   A . n 
A 1 1435 TRP 1435 1435 ?    ?   ?   A . n 
A 1 1436 ASP 1436 1436 ?    ?   ?   A . n 
A 1 1437 VAL 1437 1437 ?    ?   ?   A . n 
A 1 1438 ASP 1438 1438 ?    ?   ?   A . n 
A 1 1439 LEU 1439 1439 ?    ?   ?   A . n 
A 1 1440 GLN 1440 1440 ?    ?   ?   A . n 
A 1 1441 LYS 1441 1441 ?    ?   ?   A . n 
A 1 1442 ASN 1442 1442 ?    ?   ?   A . n 
A 1 1443 GLU 1443 1443 ?    ?   ?   A . n 
A 1 1444 ALA 1444 1444 ?    ?   ?   A . n 
A 1 1445 ILE 1445 1445 ?    ?   ?   A . n 
A 1 1446 VAL 1446 1446 ?    ?   ?   A . n 
A 1 1447 LYS 1447 1447 ?    ?   ?   A . n 
A 1 1448 ASP 1448 1448 ?    ?   ?   A . n 
A 1 1449 VAL 1449 1449 ?    ?   ?   A . n 
A 1 1450 LEU 1450 1450 ?    ?   ?   A . n 
A 1 1451 LEU 1451 1451 ?    ?   ?   A . n 
A 1 1452 VAL 1452 1452 ?    ?   ?   A . n 
A 1 1453 ALA 1453 1453 ?    ?   ?   A . n 
A 1 1454 GLN 1454 1454 ?    ?   ?   A . n 
A 1 1455 GLY 1455 1455 ?    ?   ?   A . n 
A 1 1456 GLU 1456 1456 ?    ?   ?   A . n 
A 1 1457 MET 1457 1457 ?    ?   ?   A . n 
A 1 1458 ALA 1458 1458 ?    ?   ?   A . n 
A 1 1459 LEU 1459 1459 ?    ?   ?   A . n 
A 1 1460 GLU 1460 1460 ?    ?   ?   A . n 
A 1 1461 GLU 1461 1461 ?    ?   ?   A . n 
A 1 1462 PHE 1462 1462 ?    ?   ?   A . n 
A 1 1463 LEU 1463 1463 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 ?    ?   ?   A . n 
A 1 2021 GLY 2021 2021 ?    ?   ?   A . n 
A 1 2022 TYR 2022 2022 ?    ?   ?   A . n 
A 1 2023 ALA 2023 2023 ?    ?   ?   A . n 
A 1 2024 GLY 2024 2024 ?    ?   ?   A . n 
A 1 2025 ARG 2025 2025 ?    ?   ?   A . n 
A 1 2026 SER 2026 2026 ?    ?   ?   A . n 
A 1 2027 ASN 2027 2027 ?    ?   ?   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 ?    ?   ?   A . n 
A 1 2116 GLU 2116 2116 ?    ?   ?   A . n 
A 1 2117 GLU 2117 2117 ?    ?   ?   A . n 
A 1 2118 ARG 2118 2118 ?    ?   ?   A . n 
A 1 2119 GLY 2119 2119 ?    ?   ?   A . n 
A 1 2120 GLU 2120 2120 ?    ?   ?   A . n 
A 1 2121 ALA 2121 2121 ?    ?   ?   A . n 
A 1 2122 VAL 2122 2122 ?    ?   ?   A . n 
A 1 2123 ASP 2123 2123 ?    ?   ?   A . n 
A 1 2124 GLU 2124 2124 ?    ?   ?   A . n 
A 1 2125 GLY 2125 2125 ?    ?   ?   A . n 
A 1 2126 GLU 2126 2126 ?    ?   ?   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 ALA A . n 
A 1 2389 ASP 2389 2389 2389 ASP ASP 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 ALA A . n 
A 1 2413 LEU 2413 2413 2413 LEU LEU A . n 
A 1 2414 GLN 2414 2414 2414 GLN GLN A . n 
A 1 2415 ILE 2415 2415 2415 ILE ILE A . n 
A 1 2416 GLN 2416 2416 2416 GLN GLN A . n 
A 1 2417 ARG 2417 2417 2417 ARG ARG A . n 
A 1 2418 ASP 2418 2418 2418 ASP ASP A . n 
A 1 2419 ALA 2419 2419 2419 ALA ALA A . n 
A 1 2420 ALA 2420 2420 2420 ALA ALA A . n 
A 1 2421 THR 2421 2421 2421 THR THR A . n 
A 1 2422 ILE 2422 2422 2422 ILE ILE A . n 
A 1 2423 MET 2423 2423 2423 MET MET A . n 
A 1 2424 GLN 2424 2424 2424 GLN GLN A . n 
A 1 2425 PRO 2425 2425 2425 PRO PRO A . n 
A 1 2426 TYR 2426 2426 2426 TYR TYR A . n 
A 1 2427 PHE 2427 2427 2427 PHE PHE A . n 
A 1 2428 THR 2428 2428 2428 THR THR A . n 
A 1 2429 SER 2429 2429 2429 SER SER A . n 
A 1 2430 ASN 2430 2430 2430 ASN ASN A . n 
A 1 2431 GLY 2431 2431 2431 GLY GLY A . n 
A 1 2432 LEU 2432 2432 2432 LEU LEU A . n 
A 1 2433 VAL 2433 2433 2433 VAL VAL A . n 
A 1 2434 THR 2434 2434 2434 THR THR A . n 
A 1 2435 LYS 2435 2435 2435 LYS LYS A . n 
A 1 2436 ALA 2436 2436 2436 ALA ALA A . n 
A 1 2437 LEU 2437 2437 2437 LEU LEU A . n 
A 1 2438 GLU 2438 2438 2438 GLU GLU A . n 
A 1 2439 HIS 2439 2439 2439 HIS HIS A . n 
A 1 2440 ALA 2440 2440 2440 ALA ALA A . n 
A 1 2441 PHE 2441 2441 2441 PHE PHE A . n 
A 1 2442 GLN 2442 2442 2442 GLN GLN A . n 
A 1 2443 LEU 2443 2443 2443 LEU LEU A . n 
A 1 2444 GLU 2444 2444 2444 GLU GLU A . n 
A 1 2445 HIS 2445 2445 2445 HIS HIS A . n 
A 1 2446 ILE 2446 2446 2446 ILE ILE A . n 
A 1 2447 MET 2447 2447 2447 MET MET A . n 
A 1 2448 ASP 2448 2448 2448 ASP ASP A . n 
A 1 2449 LEU 2449 2449 2449 LEU LEU A . n 
A 1 2450 THR 2450 2450 2450 THR THR A . n 
A 1 2451 ARG 2451 2451 2451 ARG ARG A . n 
A 1 2452 LEU 2452 2452 2452 LEU LEU A . n 
A 1 2453 ARG 2453 2453 2453 ARG ARG A . n 
A 1 2454 CYS 2454 2454 2454 CYS CYS A . n 
A 1 2455 LEU 2455 2455 2455 LEU LEU A . n 
A 1 2456 GLY 2456 2456 2456 GLY GLY A . n 
A 1 2457 SER 2457 2457 2457 SER SER A . n 
A 1 2458 LEU 2458 2458 2458 LEU LEU A . n 
A 1 2459 PHE 2459 2459 2459 PHE PHE A . n 
A 1 2460 SER 2460 2460 2460 SER SER A . n 
A 1 2461 MET 2461 2461 2461 MET MET A . n 
A 1 2462 LEU 2462 2462 2462 LEU LEU A . n 
A 1 2463 HIS 2463 2463 2463 HIS HIS A . n 
A 1 2464 GLN 2464 2464 2464 GLN GLN A . n 
A 1 2465 ALA 2465 2465 2465 ALA ALA A . n 
A 1 2466 CYS 2466 2466 2466 CYS CYS A . n 
A 1 2467 ARG 2467 2467 2467 ARG ARG A . n 
A 1 2468 ASN 2468 2468 2468 ASN ASN A . n 
A 1 2469 VAL 2469 2469 2469 VAL VAL A . n 
A 1 2470 ALA 2470 2470 2470 ALA ALA A . n 
A 1 2471 GLN 2471 2471 2471 GLN GLN A . n 
A 1 2472 TYR 2472 2472 2472 TYR TYR A . n 
A 1 2473 ASN 2473 2473 2473 ASN ASN A . n 
A 1 2474 ALA 2474 2474 2474 ALA ALA A . n 
A 1 2475 ASN 2475 2475 2475 ASN ASN A . n 
A 1 2476 HIS 2476 2476 2476 HIS HIS A . n 
A 1 2477 PRO 2477 2477 2477 PRO PRO A . n 
A 1 2478 ASP 2478 2478 2478 ASP ASP A . n 
A 1 2479 PHE 2479 2479 2479 PHE PHE A . n 
A 1 2480 PRO 2480 2480 2480 PRO PRO A . n 
A 1 2481 MET 2481 2481 2481 MET MET A . n 
A 1 2482 GLN 2482 2482 2482 GLN GLN A . n 
A 1 2483 ILE 2483 2483 2483 ILE ILE A . n 
A 1 2484 GLU 2484 2484 2484 GLU GLU A . n 
A 1 2485 GLN 2485 2485 2485 GLN GLN A . n 
A 1 2486 LEU 2486 2486 2486 LEU LEU A . n 
A 1 2487 GLU 2487 2487 2487 GLU GLU A . n 
A 1 2488 ARG 2488 2488 2488 ARG ARG A . n 
A 1 2489 TYR 2489 2489 2489 TYR TYR A . n 
A 1 2490 ILE 2490 2490 2490 ILE ILE A . n 
A 1 2491 GLN 2491 2491 2491 GLN GLN A . n 
A 1 2492 ARG 2492 2492 2492 ARG ARG A . n 
A 1 2493 TYR 2493 2493 2493 TYR TYR A . n 
A 1 2494 LEU 2494 2494 2494 LEU LEU A . n 
A 1 2495 VAL 2495 2495 2495 VAL VAL A . n 
A 1 2496 TYR 2496 2496 2496 TYR TYR A . n 
A 1 2497 ALA 2497 2497 2497 ALA ALA A . n 
A 1 2498 ILE 2498 2498 2498 ILE ILE A . n 
A 1 2499 LEU 2499 2499 2499 LEU LEU A . n 
A 1 2500 TRP 2500 2500 2500 TRP TRP A . n 
A 1 2501 SER 2501 2501 2501 SER SER A . n 
A 1 2502 LEU 2502 2502 2502 LEU LEU A . n 
A 1 2503 SER 2503 2503 2503 SER SER A . n 
A 1 2504 GLY 2504 2504 2504 GLY GLY A . n 
A 1 2505 ASP 2505 2505 2505 ASP ASP A . n 
A 1 2506 SER 2506 2506 2506 SER SER A . n 
A 1 2507 ARG 2507 2507 2507 ARG ARG A . n 
A 1 2508 LEU 2508 2508 2508 LEU LEU A . n 
A 1 2509 LYS 2509 2509 2509 LYS LYS A . n 
A 1 2510 MET 2510 2510 2510 MET MET A . n 
A 1 2511 ARG 2511 2511 2511 ARG ARG A . n 
A 1 2512 ALA 2512 2512 2512 ALA ALA A . n 
A 1 2513 GLU 2513 2513 2513 GLU GLU A . n 
A 1 2514 LEU 2514 2514 2514 LEU LEU A . n 
A 1 2515 GLY 2515 2515 2515 GLY GLY A . n 
A 1 2516 GLU 2516 2516 2516 GLU GLU A . n 
A 1 2517 TYR 2517 2517 2517 TYR TYR A . n 
A 1 2518 ILE 2518 2518 2518 ILE ILE A . n 
A 1 2519 ARG 2519 2519 2519 ARG ARG A . n 
A 1 2520 ARG 2520 2520 2520 ARG ARG A . n 
A 1 2521 ILE 2521 2521 2521 ILE ILE A . n 
A 1 2522 THR 2522 2522 2522 THR THR A . n 
A 1 2523 THR 2523 2523 2523 THR THR A . n 
A 1 2524 VAL 2524 2524 2524 VAL VAL A . n 
A 1 2525 PRO 2525 2525 2525 PRO PRO A . n 
A 1 2526 LEU 2526 2526 2526 LEU LEU A . n 
A 1 2527 PRO 2527 2527 2527 PRO PRO A . n 
A 1 2528 THR 2528 2528 2528 THR THR A . n 
A 1 2529 ALA 2529 2529 2529 ALA ALA A . n 
A 1 2530 PRO 2530 2530 2530 PRO PRO A . n 
A 1 2531 ASN 2531 2531 2531 ASN ASN A . n 
A 1 2532 ILE 2532 2532 2532 ILE ILE A . n 
A 1 2533 PRO 2533 2533 2533 PRO PRO A . n 
A 1 2534 ILE 2534 2534 2534 ILE ILE A . n 
A 1 2535 ILE 2535 2535 2535 ILE ILE A . n 
A 1 2536 ASP 2536 2536 2536 ASP ASP A . n 
A 1 2537 TYR 2537 2537 2537 TYR TYR A . n 
A 1 2538 GLU 2538 2538 2538 GLU GLU A . n 
A 1 2539 VAL 2539 2539 2539 VAL VAL A . n 
A 1 2540 SER 2540 2540 2540 SER SER A . n 
A 1 2541 ILE 2541 2541 2541 ILE ILE A . n 
A 1 2542 SER 2542 2542 2542 SER SER A . n 
A 1 2543 GLY 2543 2543 2543 GLY GLY A . n 
A 1 2544 GLU 2544 2544 2544 GLU GLU A . n 
A 1 2545 TRP 2545 2545 2545 TRP TRP A . n 
A 1 2546 SER 2546 2546 2546 SER SER A . n 
A 1 2547 PRO 2547 2547 2547 PRO PRO A . n 
A 1 2548 TRP 2548 2548 2548 TRP TRP A . n 
A 1 2549 GLN 2549 2549 2549 GLN GLN A . n 
A 1 2550 ALA 2550 2550 2550 ALA ALA A . n 
A 1 2551 LYS 2551 2551 2551 LYS LYS A . n 
A 1 2552 VAL 2552 2552 2552 VAL VAL A . n 
A 1 2553 PRO 2553 2553 2553 PRO PRO A . n 
A 1 2554 GLN 2554 2554 2554 GLN GLN A . n 
A 1 2555 ILE 2555 2555 2555 ILE ILE A . n 
A 1 2556 GLU 2556 2556 2556 GLU GLU A . n 
A 1 2557 VAL 2557 2557 2557 VAL VAL A . n 
A 1 2558 GLU 2558 2558 2558 GLU GLU A . n 
A 1 2559 THR 2559 2559 2559 THR THR A . n 
A 1 2560 HIS 2560 2560 2560 HIS HIS A . n 
A 1 2561 LYS 2561 2561 2561 LYS LYS A . n 
A 1 2562 VAL 2562 2562 2562 VAL VAL A . n 
A 1 2563 ALA 2563 2563 2563 ALA ALA A . n 
A 1 2564 ALA 2564 2564 2564 ALA ALA A . n 
A 1 2565 PRO 2565 2565 2565 PRO PRO A . n 
A 1 2566 ASP 2566 2566 2566 ASP ASP A . n 
A 1 2567 VAL 2567 2567 2567 VAL VAL A . n 
A 1 2568 VAL 2568 2568 2568 VAL VAL A . n 
A 1 2569 VAL 2569 2569 2569 VAL VAL A . n 
A 1 2570 PRO 2570 2570 2570 PRO PRO A . n 
A 1 2571 THR 2571 2571 2571 THR THR A . n 
A 1 2572 LEU 2572 2572 2572 LEU LEU A . n 
A 1 2573 ASP 2573 2573 2573 ASP ASP A . n 
A 1 2574 THR 2574 2574 2574 THR THR A . n 
A 1 2575 VAL 2575 2575 2575 VAL VAL A . n 
A 1 2576 ARG 2576 2576 2576 ARG ARG A . n 
A 1 2577 HIS 2577 2577 2577 HIS HIS A . n 
A 1 2578 GLU 2578 2578 2578 GLU GLU A . n 
A 1 2579 ALA 2579 2579 2579 ALA ALA A . n 
A 1 2580 LEU 2580 2580 2580 LEU LEU A . n 
A 1 2581 LEU 2581 2581 2581 LEU LEU A . n 
A 1 2582 TYR 2582 2582 2582 TYR TYR A . n 
A 1 2583 THR 2583 2583 2583 THR THR A . n 
A 1 2584 TRP 2584 2584 2584 TRP TRP A . n 
A 1 2585 LEU 2585 2585 2585 LEU LEU A . n 
A 1 2586 ALA 2586 2586 2586 ALA ALA A . n 
A 1 2587 GLU 2587 2587 2587 GLU GLU A . n 
A 1 2588 HIS 2588 2588 2588 HIS HIS A . n 
A 1 2589 LYS 2589 2589 2589 LYS LYS A . n 
A 1 2590 PRO 2590 2590 2590 PRO PRO A . n 
A 1 2591 LEU 2591 2591 2591 LEU LEU A . n 
A 1 2592 VAL 2592 2592 2592 VAL VAL A . n 
A 1 2593 LEU 2593 2593 2593 LEU LEU A . n 
A 1 2594 CYS 2594 2594 2594 CYS CYS A . n 
A 1 2595 GLY 2595 2595 2595 GLY GLY A . n 
A 1 2596 PRO 2596 2596 2596 PRO PRO A . n 
A 1 2597 PRO 2597 2597 2597 PRO PRO A . n 
A 1 2598 GLY 2598 2598 2598 GLY GLY A . n 
A 1 2599 SER 2599 2599 2599 SER SER A . n 
A 1 2600 GLY 2600 2600 2600 GLY GLY A . n 
A 1 2601 LYS 2601 2601 2601 LYS LYS A . n 
A 1 2602 THR 2602 2602 2602 THR THR A . n 
A 1 2603 MET 2603 2603 2603 MET MET A . n 
A 1 2604 THR 2604 2604 2604 THR THR A . n 
A 1 2605 LEU 2605 2605 2605 LEU LEU A . n 
A 1 2606 PHE 2606 2606 2606 PHE PHE A . n 
A 1 2607 SER 2607 2607 2607 SER SER A . n 
A 1 2608 ALA 2608 2608 2608 ALA ALA A . n 
A 1 2609 LEU 2609 2609 2609 LEU LEU A . n 
A 1 2610 ARG 2610 2610 2610 ARG ARG A . n 
A 1 2611 ALA 2611 2611 2611 ALA ALA A . n 
A 1 2612 LEU 2612 2612 2612 LEU LEU A . n 
A 1 2613 PRO 2613 2613 2613 PRO PRO A . n 
A 1 2614 ASP 2614 2614 2614 ASP ASP A . n 
A 1 2615 MET 2615 2615 2615 MET MET A . n 
A 1 2616 GLU 2616 2616 2616 GLU GLU A . n 
A 1 2617 VAL 2617 2617 2617 VAL VAL A . n 
A 1 2618 VAL 2618 2618 2618 VAL VAL A . n 
A 1 2619 GLY 2619 2619 2619 GLY GLY A . n 
A 1 2620 LEU 2620 2620 2620 LEU LEU A . n 
A 1 2621 ASN 2621 2621 2621 ASN ASN A . n 
A 1 2622 PHE 2622 2622 2622 PHE PHE A . n 
A 1 2623 SER 2623 2623 2623 SER SER A . n 
A 1 2624 SER 2624 2624 2624 SER SER A . n 
A 1 2625 ALA 2625 2625 2625 ALA ALA A . n 
A 1 2626 THR 2626 2626 2626 THR THR A . n 
A 1 2627 THR 2627 2627 2627 THR THR A . n 
A 1 2628 PRO 2628 2628 2628 PRO PRO A . n 
A 1 2629 GLU 2629 2629 2629 GLU GLU A . n 
A 1 2630 LEU 2630 2630 2630 LEU LEU A . n 
A 1 2631 LEU 2631 2631 2631 LEU LEU A . n 
A 1 2632 LEU 2632 2632 2632 LEU LEU A . n 
A 1 2633 LYS 2633 2633 2633 LYS LYS A . n 
A 1 2634 THR 2634 2634 2634 THR THR A . n 
A 1 2635 PHE 2635 2635 2635 PHE PHE A . n 
A 1 2636 ASP 2636 2636 2636 ASP ASP A . n 
A 1 2637 HIS 2637 2637 2637 HIS HIS A . n 
A 1 2638 TYR 2638 2638 2638 TYR TYR A . n 
A 1 2639 CYS 2639 2639 2639 CYS CYS A . n 
A 1 2640 GLU 2640 2640 2640 GLU GLU A . n 
A 1 2641 TYR 2641 2641 2641 TYR TYR A . n 
A 1 2642 ARG 2642 2642 2642 ARG ARG A . n 
A 1 2643 ARG 2643 2643 2643 ARG ARG A . n 
A 1 2644 THR 2644 2644 2644 THR THR A . n 
A 1 2645 PRO 2645 2645 2645 PRO PRO A . n 
A 1 2646 ASN 2646 2646 2646 ASN ASN A . n 
A 1 2647 GLY 2647 2647 2647 GLY GLY A . n 
A 1 2648 VAL 2648 2648 2648 VAL VAL A . n 
A 1 2649 VAL 2649 2649 2649 VAL VAL A . n 
A 1 2650 LEU 2650 2650 2650 LEU LEU A . n 
A 1 2651 ALA 2651 2651 2651 ALA ALA A . n 
A 1 2652 PRO 2652 2652 2652 PRO PRO A . n 
A 1 2653 VAL 2653 2653 2653 VAL VAL A . n 
A 1 2654 GLN 2654 2654 2654 GLN GLN A . n 
A 1 2655 LEU 2655 2655 2655 LEU LEU A . n 
A 1 2656 GLY 2656 2656 2656 GLY GLY A . n 
A 1 2657 LYS 2657 2657 2657 LYS LYS A . n 
A 1 2658 TRP 2658 2658 2658 TRP TRP A . n 
A 1 2659 LEU 2659 2659 2659 LEU LEU A . n 
A 1 2660 VAL 2660 2660 2660 VAL VAL A . n 
A 1 2661 LEU 2661 2661 2661 LEU LEU A . n 
A 1 2662 PHE 2662 2662 2662 PHE PHE A . n 
A 1 2663 CYS 2663 2663 2663 CYS CYS A . n 
A 1 2664 ASP 2664 2664 2664 ASP ASP A . n 
A 1 2665 GLU 2665 2665 2665 GLU GLU A . n 
A 1 2666 ILE 2666 2666 2666 ILE ILE A . n 
A 1 2667 ASN 2667 2667 2667 ASN ASN A . n 
A 1 2668 LEU 2668 2668 2668 LEU LEU A . n 
A 1 2669 PRO 2669 2669 2669 PRO PRO A . n 
A 1 2670 ASP 2670 2670 2670 ASP ASP A . n 
A 1 2671 MET 2671 2671 2671 MET MET A . n 
A 1 2672 ASP 2672 2672 2672 ASP ASP A . n 
A 1 2673 LYS 2673 2673 2673 LYS LYS A . n 
A 1 2674 TYR 2674 2674 2674 TYR TYR A . n 
A 1 2675 GLY 2675 2675 2675 GLY GLY A . n 
A 1 2676 THR 2676 2676 2676 THR THR A . n 
A 1 2677 GLN 2677 2677 2677 GLN GLN A . n 
A 1 2678 ARG 2678 2678 2678 ARG ARG A . n 
A 1 2679 VAL 2679 2679 2679 VAL VAL A . n 
A 1 2680 ILE 2680 2680 2680 ILE ILE A . n 
A 1 2681 SER 2681 2681 2681 SER SER A . n 
A 1 2682 PHE 2682 2682 2682 PHE PHE A . n 
A 1 2683 ILE 2683 2683 2683 ILE ILE A . n 
A 1 2684 ARG 2684 2684 2684 ARG ARG A . n 
A 1 2685 GLN 2685 2685 2685 GLN GLN A . n 
A 1 2686 MET 2686 2686 2686 MET MET A . n 
A 1 2687 VAL 2687 2687 2687 VAL VAL A . n 
A 1 2688 GLU 2688 2688 2688 GLU GLU A . n 
A 1 2689 HIS 2689 2689 2689 HIS HIS A . n 
A 1 2690 GLY 2690 2690 2690 GLY GLY A . n 
A 1 2691 GLY 2691 2691 2691 GLY GLY A . n 
A 1 2692 PHE 2692 2692 2692 PHE PHE A . n 
A 1 2693 TYR 2693 2693 2693 TYR TYR A . n 
A 1 2694 ARG 2694 2694 2694 ARG ARG A . n 
A 1 2695 THR 2695 2695 2695 THR THR A . n 
A 1 2696 SER 2696 2696 2696 SER SER A . n 
A 1 2697 ASP 2697 2697 2697 ASP ASP A . n 
A 1 2698 GLN 2698 2698 2698 GLN GLN A . n 
A 1 2699 THR 2699 2699 2699 THR THR A . n 
A 1 2700 TRP 2700 2700 2700 TRP TRP A . n 
A 1 2701 VAL 2701 2701 2701 VAL VAL A . n 
A 1 2702 LYS 2702 2702 2702 LYS LYS A . n 
A 1 2703 LEU 2703 2703 2703 LEU LEU A . n 
A 1 2704 GLU 2704 2704 2704 GLU GLU A . n 
A 1 2705 ARG 2705 2705 2705 ARG ARG A . n 
A 1 2706 ILE 2706 2706 2706 ILE ILE A . n 
A 1 2707 GLN 2707 2707 2707 GLN GLN A . n 
A 1 2708 PHE 2708 2708 2708 PHE PHE A . n 
A 1 2709 VAL 2709 2709 2709 VAL VAL A . n 
A 1 2710 GLY 2710 2710 2710 GLY GLY A . n 
A 1 2711 ALA 2711 2711 2711 ALA ALA A . n 
A 1 2712 CYS 2712 2712 2712 CYS CYS A . n 
A 1 2713 ASN 2713 2713 2713 ASN ASN A . n 
A 1 2714 PRO 2714 2714 2714 PRO PRO A . n 
A 1 2715 PRO 2715 2715 2715 PRO PRO A . n 
A 1 2716 THR 2716 2716 2716 THR THR A . n 
A 1 2717 ASP 2717 2717 2717 ASP ASP A . n 
A 1 2718 PRO 2718 2718 2718 PRO PRO A . n 
A 1 2719 GLY 2719 2719 2719 GLY GLY A . n 
A 1 2720 ARG 2720 2720 2720 ARG ARG A . n 
A 1 2721 LYS 2721 2721 2721 LYS LYS A . n 
A 1 2722 PRO 2722 2722 2722 PRO PRO A . n 
A 1 2723 LEU 2723 2723 2723 LEU LEU A . n 
A 1 2724 SER 2724 2724 2724 SER SER A . n 
A 1 2725 HIS 2725 2725 2725 HIS HIS A . n 
A 1 2726 ARG 2726 2726 2726 ARG ARG A . n 
A 1 2727 PHE 2727 2727 2727 PHE PHE A . n 
A 1 2728 LEU 2728 2728 2728 LEU LEU A . n 
A 1 2729 ARG 2729 2729 2729 ARG ARG A . n 
A 1 2730 HIS 2730 2730 2730 HIS HIS A . n 
A 1 2731 VAL 2731 2731 2731 VAL VAL A . n 
A 1 2732 PRO 2732 2732 2732 PRO PRO A . n 
A 1 2733 VAL 2733 2733 2733 VAL VAL A . n 
A 1 2734 VAL 2734 2734 2734 VAL VAL A . n 
A 1 2735 TYR 2735 2735 2735 TYR TYR A . n 
A 1 2736 VAL 2736 2736 2736 VAL VAL A . n 
A 1 2737 ASP 2737 2737 2737 ASP ASP A . n 
A 1 2738 TYR 2738 2738 2738 TYR TYR A . n 
A 1 2739 PRO 2739 2739 2739 PRO PRO A . n 
A 1 2740 GLY 2740 2740 2740 GLY GLY A . n 
A 1 2741 PRO 2741 2741 2741 PRO PRO A . n 
A 1 2742 ALA 2742 2742 2742 ALA ALA A . n 
A 1 2743 SER 2743 2743 2743 SER SER A . n 
A 1 2744 LEU 2744 2744 2744 LEU LEU A . n 
A 1 2745 THR 2745 2745 2745 THR THR A . n 
A 1 2746 GLN 2746 2746 2746 GLN GLN A . n 
A 1 2747 ILE 2747 2747 2747 ILE ILE A . n 
A 1 2748 TYR 2748 2748 2748 TYR TYR A . n 
A 1 2749 GLY 2749 2749 2749 GLY GLY A . n 
A 1 2750 THR 2750 2750 2750 THR THR A . n 
A 1 2751 PHE 2751 2751 2751 PHE PHE A . n 
A 1 2752 ASN 2752 2752 2752 ASN ASN A . n 
A 1 2753 ARG 2753 2753 2753 ARG ARG A . n 
A 1 2754 ALA 2754 2754 2754 ALA ALA A . n 
A 1 2755 MET 2755 2755 2755 MET MET A . n 
A 1 2756 LEU 2756 2756 2756 LEU LEU A . n 
A 1 2757 ARG 2757 2757 2757 ARG ARG A . n 
A 1 2758 LEU 2758 2758 2758 LEU LEU A . n 
A 1 2759 ILE 2759 2759 2759 ILE ILE A . n 
A 1 2760 PRO 2760 2760 2760 PRO PRO A . n 
A 1 2761 SER 2761 2761 2761 SER SER A . n 
A 1 2762 LEU 2762 2762 2762 LEU LEU A . n 
A 1 2763 ARG 2763 2763 2763 ARG ARG A . n 
A 1 2764 THR 2764 2764 2764 THR THR A . n 
A 1 2765 TYR 2765 2765 2765 TYR TYR A . n 
A 1 2766 ALA 2766 2766 2766 ALA ALA A . n 
A 1 2767 GLU 2767 2767 2767 GLU GLU A . n 
A 1 2768 PRO 2768 2768 2768 PRO PRO A . n 
A 1 2769 LEU 2769 2769 2769 LEU LEU A . n 
A 1 2770 THR 2770 2770 2770 THR THR A . n 
A 1 2771 ALA 2771 2771 2771 ALA ALA A . n 
A 1 2772 ALA 2772 2772 2772 ALA ALA A . n 
A 1 2773 MET 2773 2773 2773 MET MET A . n 
A 1 2774 VAL 2774 2774 2774 VAL VAL A . n 
A 1 2775 GLU 2775 2775 2775 GLU GLU A . n 
A 1 2776 PHE 2776 2776 2776 PHE PHE A . n 
A 1 2777 TYR 2777 2777 2777 TYR TYR A . n 
A 1 2778 THR 2778 2778 2778 THR THR A . n 
A 1 2779 MET 2779 2779 2779 MET MET A . n 
A 1 2780 SER 2780 2780 2780 SER SER A . n 
A 1 2781 GLN 2781 2781 2781 GLN GLN A . n 
A 1 2782 GLU 2782 2782 2782 GLU GLU A . n 
A 1 2783 ARG 2783 2783 2783 ARG ARG A . n 
A 1 2784 PHE 2784 2784 2784 PHE PHE A . n 
A 1 2785 THR 2785 2785 2785 THR THR A . n 
A 1 2786 GLN 2786 2786 2786 GLN GLN A . n 
A 1 2787 ASP 2787 2787 2787 ASP ASP A . n 
A 1 2788 THR 2788 2788 2788 THR THR A . n 
A 1 2789 GLN 2789 2789 2789 GLN GLN A . n 
A 1 2790 PRO 2790 2790 2790 PRO PRO A . n 
A 1 2791 HIS 2791 2791 2791 HIS HIS A . n 
A 1 2792 TYR 2792 2792 2792 TYR TYR A . n 
A 1 2793 ILE 2793 2793 2793 ILE ILE A . n 
A 1 2794 TYR 2794 2794 2794 TYR TYR A . n 
A 1 2795 SER 2795 2795 2795 SER SER A . n 
A 1 2796 PRO 2796 2796 2796 PRO PRO A . n 
A 1 2797 ARG 2797 2797 2797 ARG ARG A . n 
A 1 2798 GLU 2798 2798 2798 GLU GLU A . n 
A 1 2799 MET 2799 2799 2799 MET MET A . n 
A 1 2800 THR 2800 2800 2800 THR THR A . n 
A 1 2801 ARG 2801 2801 2801 ARG ARG A . n 
A 1 2802 TRP 2802 2802 2802 TRP TRP A . n 
A 1 2803 VAL 2803 2803 2803 VAL VAL A . n 
A 1 2804 ARG 2804 2804 2804 ARG ARG A . n 
A 1 2805 GLY 2805 2805 2805 GLY GLY A . n 
A 1 2806 ILE 2806 2806 2806 ILE ILE A . n 
A 1 2807 PHE 2807 2807 2807 PHE PHE A . n 
A 1 2808 GLU 2808 2808 2808 GLU GLU A . n 
A 1 2809 ALA 2809 2809 2809 ALA ALA A . n 
A 1 2810 LEU 2810 2810 2810 LEU LEU A . n 
A 1 2811 ARG 2811 2811 2811 ARG ARG A . n 
A 1 2812 PRO 2812 2812 2812 PRO PRO A . n 
A 1 2813 LEU 2813 2813 2813 LEU LEU A . n 
A 1 2814 GLU 2814 2814 2814 GLU GLU A . n 
A 1 2815 THR 2815 2815 2815 THR THR A . n 
A 1 2816 LEU 2816 2816 2816 LEU LEU A . n 
A 1 2817 PRO 2817 2817 2817 PRO PRO A . n 
A 1 2818 VAL 2818 2818 2818 VAL VAL A . n 
A 1 2819 GLU 2819 2819 2819 GLU GLU A . n 
A 1 2820 GLY 2820 2820 2820 GLY GLY A . n 
A 1 2821 LEU 2821 2821 2821 LEU LEU A . n 
A 1 2822 ILE 2822 2822 2822 ILE ILE A . n 
A 1 2823 ARG 2823 2823 2823 ARG ARG A . n 
A 1 2824 ILE 2824 2824 2824 ILE ILE A . n 
A 1 2825 TRP 2825 2825 2825 TRP TRP A . n 
A 1 2826 ALA 2826 2826 2826 ALA ALA A . n 
A 1 2827 HIS 2827 2827 2827 HIS HIS A . n 
A 1 2828 GLU 2828 2828 2828 GLU GLU A . n 
A 1 2829 ALA 2829 2829 2829 ALA ALA A . n 
A 1 2830 LEU 2830 2830 2830 LEU LEU A . n 
A 1 2831 ARG 2831 2831 2831 ARG ARG A . n 
A 1 2832 LEU 2832 2832 2832 LEU LEU A . n 
A 1 2833 PHE 2833 2833 2833 PHE PHE A . n 
A 1 2834 GLN 2834 2834 2834 GLN GLN A . n 
A 1 2835 ASP 2835 2835 2835 ASP ASP A . n 
A 1 2836 ARG 2836 2836 2836 ARG ARG A . n 
A 1 2837 LEU 2837 2837 2837 LEU LEU A . n 
A 1 2838 VAL 2838 2838 2838 VAL VAL A . n 
A 1 2839 GLU 2839 2839 2839 GLU GLU A . n 
A 1 2840 ASP 2840 2840 2840 ASP ASP A . n 
A 1 2841 GLU 2841 2841 2841 GLU GLU A . n 
A 1 2842 GLU 2842 2842 2842 GLU GLU A . n 
A 1 2843 ARG 2843 2843 2843 ARG ARG A . n 
A 1 2844 ARG 2844 2844 2844 ARG ARG A . n 
A 1 2845 TRP 2845 2845 2845 TRP TRP A . n 
A 1 2846 THR 2846 2846 2846 THR THR A . n 
A 1 2847 ASP 2847 2847 2847 ASP ASP A . n 
A 1 2848 GLU 2848 2848 2848 GLU GLU A . n 
A 1 2849 ASN 2849 2849 2849 ASN ASN A . n 
A 1 2850 ILE 2850 2850 2850 ILE ILE A . n 
A 1 2851 ASP 2851 2851 2851 ASP ASP A . n 
A 1 2852 THR 2852 2852 2852 THR THR A . n 
A 1 2853 VAL 2853 2853 2853 VAL VAL A . n 
A 1 2854 ALA 2854 2854 2854 ALA ALA A . n 
A 1 2855 LEU 2855 2855 2855 LEU LEU A . n 
A 1 2856 LYS 2856 2856 2856 LYS LYS A . n 
A 1 2857 HIS 2857 2857 2857 HIS HIS A . n 
A 1 2858 PHE 2858 2858 2858 PHE PHE A . n 
A 1 2859 PRO 2859 2859 2859 PRO PRO A . n 
A 1 2860 ASN 2860 2860 2860 ASN ASN A . n 
A 1 2861 ILE 2861 2861 2861 ILE ILE A . n 
A 1 2862 ASP 2862 2862 2862 ASP ASP A . n 
A 1 2863 ARG 2863 2863 2863 ARG ARG A . n 
A 1 2864 GLU 2864 2864 2864 GLU GLU A . n 
A 1 2865 LYS 2865 2865 2865 LYS LYS A . n 
A 1 2866 ALA 2866 2866 2866 ALA ALA A . n 
A 1 2867 MET 2867 2867 2867 MET MET A . n 
A 1 2868 SER 2868 2868 2868 SER SER A . n 
A 1 2869 ARG 2869 2869 2869 ARG ARG A . n 
A 1 2870 PRO 2870 2870 2870 PRO PRO A . n 
A 1 2871 ILE 2871 2871 2871 ILE ILE A . n 
A 1 2872 LEU 2872 2872 2872 LEU LEU A . n 
A 1 2873 TYR 2873 2873 2873 TYR TYR A . n 
A 1 2874 SER 2874 2874 2874 SER SER A . n 
A 1 2875 ASN 2875 2875 2875 ASN ASN A . n 
A 1 2876 TRP 2876 2876 2876 TRP TRP A . n 
A 1 2877 LEU 2877 2877 2877 LEU LEU A . n 
A 1 2878 SER 2878 2878 2878 SER SER A . n 
A 1 2879 LYS 2879 2879 2879 LYS LYS A . n 
A 1 2880 ASP 2880 2880 2880 ASP ASP A . n 
A 1 2881 TYR 2881 2881 2881 TYR TYR A . n 
A 1 2882 ILE 2882 2882 2882 ILE ILE A . n 
A 1 2883 PRO 2883 2883 2883 PRO PRO A . n 
A 1 2884 VAL 2884 2884 2884 VAL VAL A . n 
A 1 2885 ASP 2885 2885 2885 ASP ASP A . n 
A 1 2886 GLN 2886 2886 2886 GLN GLN A . n 
A 1 2887 GLU 2887 2887 2887 GLU GLU A . n 
A 1 2888 GLU 2888 2888 2888 GLU GLU A . n 
A 1 2889 LEU 2889 2889 2889 LEU LEU A . n 
A 1 2890 ARG 2890 2890 2890 ARG ARG A . n 
A 1 2891 ASP 2891 2891 2891 ASP ASP A . n 
A 1 2892 TYR 2892 2892 2892 TYR TYR A . n 
A 1 2893 VAL 2893 2893 2893 VAL VAL A . n 
A 1 2894 LYS 2894 2894 2894 LYS LYS A . n 
A 1 2895 ALA 2895 2895 2895 ALA ALA A . n 
A 1 2896 ARG 2896 2896 2896 ARG ARG A . n 
A 1 2897 LEU 2897 2897 2897 LEU LEU A . n 
A 1 2898 LYS 2898 2898 2898 LYS LYS A . n 
A 1 2899 VAL 2899 2899 2899 VAL VAL A . n 
A 1 2900 PHE 2900 2900 2900 PHE PHE A . n 
A 1 2901 TYR 2901 2901 2901 TYR TYR A . n 
A 1 2902 GLU 2902 2902 2902 GLU GLU A . n 
A 1 2903 GLU 2903 2903 2903 GLU GLU A . n 
A 1 2904 GLU 2904 2904 2904 GLU GLU A . n 
A 1 2905 LEU 2905 2905 2905 LEU LEU A . n 
A 1 2906 ASP 2906 2906 2906 ASP ASP A . n 
A 1 2907 VAL 2907 2907 2907 VAL VAL A . n 
A 1 2908 PRO 2908 2908 2908 PRO PRO A . n 
A 1 2909 LEU 2909 2909 2909 LEU LEU A . n 
A 1 2910 VAL 2910 2910 2910 VAL VAL A . n 
A 1 2911 LEU 2911 2911 2911 LEU LEU A . n 
A 1 2912 PHE 2912 2912 2912 PHE PHE A . n 
A 1 2913 ASN 2913 2913 2913 ASN ASN A . n 
A 1 2914 GLU 2914 2914 2914 GLU GLU A . n 
A 1 2915 VAL 2915 2915 2915 VAL VAL A . n 
A 1 2916 LEU 2916 2916 2916 LEU LEU A . n 
A 1 2917 ASP 2917 2917 2917 ASP ASP A . n 
A 1 2918 HIS 2918 2918 2918 HIS HIS A . n 
A 1 2919 VAL 2919 2919 2919 VAL VAL A . n 
A 1 2920 LEU 2920 2920 2920 LEU LEU A . n 
A 1 2921 ARG 2921 2921 2921 ARG ARG A . n 
A 1 2922 ILE 2922 2922 2922 ILE ILE A . n 
A 1 2923 ASP 2923 2923 2923 ASP ASP A . n 
A 1 2924 ARG 2924 2924 2924 ARG ARG A . n 
A 1 2925 ILE 2925 2925 2925 ILE ILE A . n 
A 1 2926 PHE 2926 2926 2926 PHE PHE A . n 
A 1 2927 ARG 2927 2927 2927 ARG ARG A . n 
A 1 2928 GLN 2928 2928 2928 GLN GLN A . n 
A 1 2929 PRO 2929 2929 2929 PRO PRO A . n 
A 1 2930 GLN 2930 2930 2930 GLN GLN A . n 
A 1 2931 GLY 2931 2931 2931 GLY GLY A . n 
A 1 2932 HIS 2932 2932 2932 HIS HIS A . n 
A 1 2933 LEU 2933 2933 2933 LEU LEU A . n 
A 1 2934 LEU 2934 2934 2934 LEU LEU A . n 
A 1 2935 LEU 2935 2935 2935 LEU LEU A . n 
A 1 2936 ILE 2936 2936 2936 ILE ILE A . n 
A 1 2937 GLY 2937 2937 2937 GLY GLY A . n 
A 1 2938 VAL 2938 2938 2938 VAL VAL A . n 
A 1 2939 SER 2939 2939 2939 SER SER A . n 
A 1 2940 GLY 2940 2940 2940 GLY GLY A . n 
A 1 2941 ALA 2941 2941 2941 ALA ALA A . n 
A 1 2942 GLY 2942 2942 2942 GLY GLY A . n 
A 1 2943 LYS 2943 2943 2943 LYS LYS A . n 
A 1 2944 THR 2944 2944 2944 THR THR A . n 
A 1 2945 THR 2945 2945 2945 THR THR A . n 
A 1 2946 LEU 2946 2946 2946 LEU LEU A . n 
A 1 2947 SER 2947 2947 2947 SER SER A . n 
A 1 2948 ARG 2948 2948 2948 ARG ARG A . n 
A 1 2949 PHE 2949 2949 2949 PHE PHE A . n 
A 1 2950 VAL 2950 2950 2950 VAL VAL A . n 
A 1 2951 ALA 2951 2951 2951 ALA ALA A . n 
A 1 2952 TRP 2952 2952 2952 TRP TRP A . n 
A 1 2953 MET 2953 2953 2953 MET MET A . n 
A 1 2954 ASN 2954 2954 2954 ASN ASN A . n 
A 1 2955 GLY 2955 2955 2955 GLY GLY A . n 
A 1 2956 LEU 2956 2956 2956 LEU LEU A . n 
A 1 2957 SER 2957 2957 2957 SER SER A . n 
A 1 2958 VAL 2958 2958 2958 VAL VAL A . n 
A 1 2959 TYR 2959 2959 2959 TYR TYR A . n 
A 1 2960 GLN 2960 2960 2960 GLN GLN A . n 
A 1 2961 ILE 2961 2961 2961 ILE ILE A . n 
A 1 2962 LYS 2962 2962 2962 LYS LYS A . n 
A 1 2963 VAL 2963 2963 2963 VAL VAL A . n 
A 1 2964 HIS 2964 2964 2964 HIS HIS A . n 
A 1 2965 ARG 2965 2965 2965 ARG ARG A . n 
A 1 2966 LYS 2966 2966 2966 LYS LYS A . n 
A 1 2967 TYR 2967 2967 2967 TYR TYR A . n 
A 1 2968 THR 2968 2968 2968 THR THR A . n 
A 1 2969 GLY 2969 2969 2969 GLY GLY A . n 
A 1 2970 GLU 2970 2970 2970 GLU GLU A . n 
A 1 2971 ASP 2971 2971 2971 ASP ASP A . n 
A 1 2972 PHE 2972 2972 2972 PHE PHE A . n 
A 1 2973 ASP 2973 2973 2973 ASP ASP A . n 
A 1 2974 GLU 2974 2974 2974 GLU GLU A . n 
A 1 2975 ASP 2975 2975 2975 ASP ASP A . n 
A 1 2976 LEU 2976 2976 2976 LEU LEU A . n 
A 1 2977 ARG 2977 2977 2977 ARG ARG A . n 
A 1 2978 THR 2978 2978 2978 THR THR A . n 
A 1 2979 VAL 2979 2979 2979 VAL VAL A . n 
A 1 2980 LEU 2980 2980 2980 LEU LEU A . n 
A 1 2981 ARG 2981 2981 2981 ARG ARG A . n 
A 1 2982 ARG 2982 2982 2982 ARG ARG A . n 
A 1 2983 SER 2983 2983 2983 SER SER A . n 
A 1 2984 GLY 2984 2984 2984 GLY GLY A . n 
A 1 2985 CYS 2985 2985 2985 CYS CYS A . n 
A 1 2986 LYS 2986 2986 2986 LYS LYS A . n 
A 1 2987 ASN 2987 2987 2987 ASN ASN A . n 
A 1 2988 GLU 2988 2988 2988 GLU GLU A . n 
A 1 2989 LYS 2989 2989 2989 LYS LYS A . n 
A 1 2990 ILE 2990 2990 2990 ILE ILE A . n 
A 1 2991 ALA 2991 2991 2991 ALA ALA A . n 
A 1 2992 PHE 2992 2992 2992 PHE PHE A . n 
A 1 2993 ILE 2993 2993 2993 ILE ILE A . n 
A 1 2994 MET 2994 2994 2994 MET MET A . n 
A 1 2995 ASP 2995 2995 2995 ASP ASP A . n 
A 1 2996 GLU 2996 2996 2996 GLU GLU A . n 
A 1 2997 SER 2997 2997 2997 SER SER A . n 
A 1 2998 ASN 2998 2998 2998 ASN ASN A . n 
A 1 2999 VAL 2999 2999 2999 VAL VAL A . n 
A 1 3000 LEU 3000 3000 3000 LEU LEU A . n 
A 1 3001 ASP 3001 3001 3001 ASP ASP A . n 
A 1 3002 SER 3002 3002 3002 SER SER A . n 
A 1 3003 GLY 3003 3003 3003 GLY GLY A . n 
A 1 3004 PHE 3004 3004 3004 PHE PHE A . n 
A 1 3005 LEU 3005 3005 3005 LEU LEU A . n 
A 1 3006 GLU 3006 3006 3006 GLU GLU A . n 
A 1 3007 ARG 3007 3007 3007 ARG ARG A . n 
A 1 3008 MET 3008 3008 3008 MET MET A . n 
A 1 3009 ASN 3009 3009 3009 ASN ASN A . n 
A 1 3010 THR 3010 3010 3010 THR THR A . n 
A 1 3011 LEU 3011 3011 3011 LEU LEU A . n 
A 1 3012 LEU 3012 3012 3012 LEU LEU A . n 
A 1 3013 ALA 3013 3013 3013 ALA ALA A . n 
A 1 3014 ASN 3014 3014 3014 ASN ASN A . n 
A 1 3015 GLY 3015 3015 3015 GLY GLY A . n 
A 1 3016 GLU 3016 3016 3016 GLU GLU A . n 
A 1 3017 VAL 3017 3017 3017 VAL VAL A . n 
A 1 3018 PRO 3018 3018 3018 PRO PRO A . n 
A 1 3019 GLY 3019 3019 3019 GLY GLY A . n 
A 1 3020 LEU 3020 3020 3020 LEU LEU A . n 
A 1 3021 PHE 3021 3021 3021 PHE PHE A . n 
A 1 3022 GLU 3022 3022 3022 GLU GLU A . n 
A 1 3023 GLY 3023 3023 3023 GLY GLY A . n 
A 1 3024 ASP 3024 3024 3024 ASP ASP A . n 
A 1 3025 GLU 3025 3025 3025 GLU GLU A . n 
A 1 3026 TYR 3026 3026 3026 TYR TYR A . n 
A 1 3027 ALA 3027 3027 3027 ALA ALA A . n 
A 1 3028 THR 3028 3028 3028 THR THR A . n 
A 1 3029 LEU 3029 3029 3029 LEU LEU A . n 
A 1 3030 MET 3030 3030 3030 MET MET A . n 
A 1 3031 THR 3031 3031 3031 THR THR A . n 
A 1 3032 GLN 3032 3032 3032 GLN GLN A . n 
A 1 3033 CYS 3033 3033 3033 CYS CYS A . n 
A 1 3034 LYS 3034 3034 3034 LYS LYS A . n 
A 1 3035 GLU 3035 3035 3035 GLU GLU A . n 
A 1 3036 GLY 3036 3036 3036 GLY GLY A . n 
A 1 3037 ALA 3037 3037 3037 ALA ALA A . n 
A 1 3038 GLN 3038 3038 3038 GLN GLN A . n 
A 1 3039 LYS 3039 3039 3039 LYS LYS A . n 
A 1 3040 GLU 3040 3040 3040 GLU GLU A . n 
A 1 3041 GLY 3041 3041 3041 GLY GLY A . n 
A 1 3042 LEU 3042 3042 3042 LEU LEU A . n 
A 1 3043 MET 3043 3043 3043 MET MET A . n 
A 1 3044 LEU 3044 3044 3044 LEU LEU A . n 
A 1 3045 ASP 3045 3045 3045 ASP ASP A . n 
A 1 3046 SER 3046 3046 3046 SER SER A . n 
A 1 3047 HIS 3047 3047 3047 HIS HIS A . n 
A 1 3048 GLU 3048 3048 3048 GLU GLU A . n 
A 1 3049 GLU 3049 3049 3049 GLU GLU A . n 
A 1 3050 LEU 3050 3050 3050 LEU LEU A . n 
A 1 3051 TYR 3051 3051 3051 TYR TYR A . n 
A 1 3052 LYS 3052 3052 3052 LYS LYS A . n 
A 1 3053 TRP 3053 3053 3053 TRP TRP A . n 
A 1 3054 PHE 3054 3054 3054 PHE PHE A . n 
A 1 3055 THR 3055 3055 3055 THR THR A . n 
A 1 3056 SER 3056 3056 3056 SER SER A . n 
A 1 3057 GLN 3057 3057 3057 GLN GLN A . n 
A 1 3058 VAL 3058 3058 3058 VAL VAL A . n 
A 1 3059 ILE 3059 3059 3059 ILE ILE A . n 
A 1 3060 ARG 3060 3060 3060 ARG ARG A . n 
A 1 3061 ASN 3061 3061 3061 ASN ASN A . n 
A 1 3062 LEU 3062 3062 3062 LEU LEU A . n 
A 1 3063 HIS 3063 3063 3063 HIS HIS A . n 
A 1 3064 VAL 3064 3064 3064 VAL VAL A . n 
A 1 3065 VAL 3065 3065 3065 VAL VAL A . n 
A 1 3066 PHE 3066 3066 3066 PHE PHE A . n 
A 1 3067 THR 3067 3067 3067 THR THR A . n 
A 1 3068 MET 3068 3068 3068 MET MET A . n 
A 1 3069 ASN 3069 3069 3069 ASN ASN A . n 
A 1 3070 PRO 3070 3070 3070 PRO PRO A . n 
A 1 3071 SER 3071 3071 3071 SER SER A . n 
A 1 3072 SER 3072 3072 3072 SER SER A . n 
A 1 3073 GLU 3073 3073 3073 GLU GLU A . n 
A 1 3074 GLY 3074 3074 3074 GLY GLY A . n 
A 1 3075 LEU 3075 3075 3075 LEU LEU A . n 
A 1 3076 LYS 3076 3076 3076 LYS LYS A . n 
A 1 3077 ASP 3077 3077 3077 ASP ASP A . n 
A 1 3078 ARG 3078 3078 3078 ARG ARG A . n 
A 1 3079 ALA 3079 3079 3079 ALA ALA A . n 
A 1 3080 ALA 3080 3080 3080 ALA ALA A . n 
A 1 3081 THR 3081 3081 3081 THR THR A . n 
A 1 3082 SER 3082 3082 3082 SER SER A . n 
A 1 3083 PRO 3083 3083 3083 PRO PRO A . n 
A 1 3084 ALA 3084 3084 3084 ALA ALA A . n 
A 1 3085 LEU 3085 3085 3085 LEU LEU A . n 
A 1 3086 PHE 3086 3086 3086 PHE PHE A . n 
A 1 3087 ASN 3087 3087 3087 ASN ASN A . n 
A 1 3088 ARG 3088 3088 3088 ARG ARG A . n 
A 1 3089 CYS 3089 3089 3089 CYS CYS A . n 
A 1 3090 VAL 3090 3090 3090 VAL VAL A . n 
A 1 3091 LEU 3091 3091 3091 LEU LEU A . n 
A 1 3092 ASN 3092 3092 3092 ASN ASN A . n 
A 1 3093 TRP 3093 3093 3093 TRP TRP A . n 
A 1 3094 PHE 3094 3094 3094 PHE PHE A . n 
A 1 3095 GLY 3095 3095 3095 GLY GLY A . n 
A 1 3096 ASP 3096 3096 3096 ASP ASP A . n 
A 1 3097 TRP 3097 3097 3097 TRP TRP A . n 
A 1 3098 SER 3098 3098 3098 SER SER A . n 
A 1 3099 THR 3099 3099 3099 THR THR A . n 
A 1 3100 GLU 3100 3100 3100 GLU GLU A . n 
A 1 3101 ALA 3101 3101 3101 ALA ALA A . n 
A 1 3102 LEU 3102 3102 3102 LEU LEU A . n 
A 1 3103 TYR 3103 3103 3103 TYR TYR A . n 
A 1 3104 GLN 3104 3104 3104 GLN GLN A . n 
A 1 3105 VAL 3105 3105 3105 VAL VAL A . n 
A 1 3106 GLY 3106 3106 3106 GLY GLY A . n 
A 1 3107 LYS 3107 3107 3107 LYS LYS A . n 
A 1 3108 GLU 3108 3108 3108 GLU GLU A . n 
A 1 3109 PHE 3109 3109 3109 PHE PHE A . n 
A 1 3110 THR 3110 3110 3110 THR THR A . n 
A 1 3111 SER 3111 3111 3111 SER SER A . n 
A 1 3112 LYS 3112 3112 3112 LYS LYS A . n 
A 1 3113 MET 3113 3113 3113 MET MET A . n 
A 1 3114 ASP 3114 3114 3114 ASP ASP A . n 
A 1 3115 LEU 3115 3115 3115 LEU LEU A . n 
A 1 3116 GLU 3116 3116 3116 GLU GLU A . n 
A 1 3117 LYS 3117 3117 3117 LYS LYS A . n 
A 1 3118 PRO 3118 3118 3118 PRO PRO A . n 
A 1 3119 ASN 3119 3119 3119 ASN ASN A . n 
A 1 3120 TYR 3120 3120 3120 TYR TYR A . n 
A 1 3121 ILE 3121 3121 3121 ILE ILE A . n 
A 1 3122 VAL 3122 3122 3122 VAL VAL A . n 
A 1 3123 PRO 3123 3123 3123 PRO PRO A . n 
A 1 3124 ASP 3124 3124 3124 ASP ASP A . n 
A 1 3125 TYR 3125 3125 3125 TYR TYR A . n 
A 1 3126 MET 3126 3126 3126 MET MET A . n 
A 1 3127 PRO 3127 3127 3127 PRO PRO A . n 
A 1 3128 VAL 3128 3128 3128 VAL VAL A . n 
A 1 3129 VAL 3129 3129 3129 VAL VAL A . n 
A 1 3130 TYR 3130 3130 3130 TYR TYR A . n 
A 1 3131 ASP 3131 3131 3131 ASP ASP A . n 
A 1 3132 LYS 3132 3132 3132 LYS LYS A . n 
A 1 3133 LEU 3133 3133 3133 LEU LEU A . n 
A 1 3134 PRO 3134 3134 3134 PRO PRO A . n 
A 1 3135 GLN 3135 3135 3135 GLN GLN A . n 
A 1 3136 PRO 3136 3136 3136 PRO PRO A . n 
A 1 3137 PRO 3137 3137 3137 PRO PRO A . n 
A 1 3138 SER 3138 3138 3138 SER SER A . n 
A 1 3139 HIS 3139 3139 3139 HIS HIS A . n 
A 1 3140 ARG 3140 3140 3140 ARG ARG A . n 
A 1 3141 GLU 3141 3141 3141 GLU GLU A . n 
A 1 3142 ALA 3142 3142 3142 ALA ALA A . n 
A 1 3143 ILE 3143 3143 3143 ILE ILE A . n 
A 1 3144 VAL 3144 3144 3144 VAL VAL A . n 
A 1 3145 ASN 3145 3145 3145 ASN ASN A . n 
A 1 3146 SER 3146 3146 3146 SER SER A . n 
A 1 3147 CYS 3147 3147 3147 CYS CYS A . n 
A 1 3148 VAL 3148 3148 3148 VAL VAL A . n 
A 1 3149 PHE 3149 3149 3149 PHE PHE A . n 
A 1 3150 VAL 3150 3150 3150 VAL VAL A . n 
A 1 3151 HIS 3151 3151 3151 HIS HIS A . n 
A 1 3152 GLN 3152 3152 3152 GLN GLN A . n 
A 1 3153 THR 3153 3153 3153 THR THR A . n 
A 1 3154 LEU 3154 3154 3154 LEU LEU A . n 
A 1 3155 HIS 3155 3155 3155 HIS HIS A . n 
A 1 3156 GLN 3156 3156 3156 GLN GLN A . n 
A 1 3157 ALA 3157 3157 3157 ALA ALA A . n 
A 1 3158 ASN 3158 3158 3158 ASN ASN A . n 
A 1 3159 ALA 3159 3159 3159 ALA ALA A . n 
A 1 3160 ARG 3160 3160 3160 ARG ARG A . n 
A 1 3161 LEU 3161 3161 3161 LEU LEU A . n 
A 1 3162 ALA 3162 3162 3162 ALA ALA A . n 
A 1 3163 LYS 3163 3163 3163 LYS LYS A . n 
A 1 3164 ARG 3164 3164 3164 ARG ARG A . n 
A 1 3165 GLY 3165 3165 3165 GLY GLY A . n 
A 1 3166 GLY 3166 3166 3166 GLY GLY A . n 
A 1 3167 ARG 3167 3167 3167 ARG ARG A . n 
A 1 3168 THR 3168 3168 3168 THR THR A . n 
A 1 3169 MET 3169 3169 3169 MET MET A . n 
A 1 3170 ALA 3170 3170 3170 ALA ALA A . n 
A 1 3171 ILE 3171 3171 3171 ILE ILE A . n 
A 1 3172 THR 3172 3172 3172 THR THR A . n 
A 1 3173 PRO 3173 3173 3173 PRO PRO A . n 
A 1 3174 ARG 3174 3174 3174 ARG ARG A . n 
A 1 3175 HIS 3175 3175 3175 HIS HIS A . n 
A 1 3176 TYR 3176 3176 3176 TYR TYR A . n 
A 1 3177 LEU 3177 3177 3177 LEU LEU A . n 
A 1 3178 ASP 3178 3178 3178 ASP ASP A . n 
A 1 3179 PHE 3179 3179 3179 PHE PHE A . n 
A 1 3180 ILE 3180 3180 3180 ILE ILE A . n 
A 1 3181 ASN 3181 3181 3181 ASN ASN A . n 
A 1 3182 HIS 3182 3182 3182 HIS HIS A . n 
A 1 3183 TYR 3183 3183 3183 TYR TYR A . n 
A 1 3184 ALA 3184 3184 3184 ALA ALA A . n 
A 1 3185 ASN 3185 3185 3185 ASN ASN A . n 
A 1 3186 LEU 3186 3186 3186 LEU LEU A . n 
A 1 3187 PHE 3187 3187 3187 PHE PHE A . n 
A 1 3188 HIS 3188 3188 3188 HIS HIS A . n 
A 1 3189 GLU 3189 3189 3189 GLU GLU A . n 
A 1 3190 LYS 3190 3190 3190 LYS LYS A . n 
A 1 3191 ARG 3191 3191 3191 ARG ARG A . n 
A 1 3192 SER 3192 3192 3192 SER SER A . n 
A 1 3193 GLU 3193 3193 3193 GLU GLU A . n 
A 1 3194 LEU 3194 3194 3194 LEU LEU A . n 
A 1 3195 GLU 3195 3195 3195 GLU GLU A . n 
A 1 3196 GLU 3196 3196 3196 GLU GLU A . n 
A 1 3197 GLN 3197 3197 3197 GLN GLN A . n 
A 1 3198 GLN 3198 3198 3198 GLN GLN A . n 
A 1 3199 MET 3199 3199 3199 MET MET A . n 
A 1 3200 HIS 3200 3200 3200 HIS HIS A . n 
A 1 3201 LEU 3201 3201 3201 LEU LEU A . n 
A 1 3202 ASN 3202 3202 3202 ASN ASN A . n 
A 1 3203 VAL 3203 3203 3203 VAL VAL A . n 
A 1 3204 GLY 3204 3204 3204 GLY GLY A . n 
A 1 3205 LEU 3205 3205 3205 LEU LEU A . n 
A 1 3206 ARG 3206 3206 3206 ARG ARG A . n 
A 1 3207 LYS 3207 3207 3207 LYS LYS A . n 
A 1 3208 ILE 3208 3208 3208 ILE ILE A . n 
A 1 3209 LYS 3209 3209 3209 LYS LYS A . n 
A 1 3210 GLU 3210 3210 3210 GLU GLU A . n 
A 1 3211 THR 3211 3211 3211 THR THR A . n 
A 1 3212 VAL 3212 3212 3212 VAL VAL A . n 
A 1 3213 ASP 3213 3213 3213 ASP ASP A . n 
A 1 3214 GLN 3214 3214 3214 GLN GLN A . n 
A 1 3215 VAL 3215 3215 3215 VAL VAL A . n 
A 1 3216 GLU 3216 3216 3216 GLU GLU A . n 
A 1 3217 GLU 3217 3217 3217 GLU GLU A . n 
A 1 3218 LEU 3218 3218 3218 LEU LEU A . n 
A 1 3219 ARG 3219 3219 3219 ARG ARG A . n 
A 1 3220 ARG 3220 3220 3220 ARG ARG A . n 
A 1 3221 ASP 3221 3221 ?    ?   ?   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 3471 LYS LYS A . n 
A 1 3472 VAL 3472 3472 3472 VAL VAL A . n 
A 1 3473 ASN 3473 3473 3473 ASN ASN A . n 
A 1 3474 ARG 3474 3474 3474 ARG ARG A . n 
A 1 3475 SER 3475 3475 3475 SER SER A . n 
A 1 3476 THR 3476 3476 3476 THR THR A . n 
A 1 3477 ALA 3477 3477 3477 ALA ALA A . n 
A 1 3478 LEU 3478 3478 3478 LEU LEU A . n 
A 1 3479 LEU 3479 3479 3479 LEU LEU A . n 
A 1 3480 LYS 3480 3480 3480 LYS LYS A . n 
A 1 3481 SER 3481 3481 3481 SER SER A . n 
A 1 3482 LEU 3482 3482 3482 LEU LEU A . n 
A 1 3483 SER 3483 3483 3483 SER SER A . n 
A 1 3484 ALA 3484 3484 3484 ALA ALA A . n 
A 1 3485 GLU 3485 3485 3485 GLU GLU A . n 
A 1 3486 ARG 3486 3486 3486 ARG ARG A . n 
A 1 3487 GLU 3487 3487 3487 GLU GLU A . n 
A 1 3488 ARG 3488 3488 3488 ARG ARG A . n 
A 1 3489 TRP 3489 3489 3489 TRP TRP A . n 
A 1 3490 GLU 3490 3490 3490 GLU GLU A . n 
A 1 3491 LYS 3491 3491 3491 LYS LYS A . n 
A 1 3492 THR 3492 3492 3492 THR THR A . n 
A 1 3493 SER 3493 3493 3493 SER SER A . n 
A 1 3494 GLU 3494 3494 3494 GLU GLU A . n 
A 1 3495 THR 3495 3495 3495 THR THR A . n 
A 1 3496 PHE 3496 3496 3496 PHE PHE A . n 
A 1 3497 LYS 3497 3497 3497 LYS LYS A . n 
A 1 3498 ASN 3498 3498 3498 ASN ASN A . n 
A 1 3499 GLN 3499 3499 3499 GLN GLN A . n 
A 1 3500 MET 3500 3500 3500 MET MET A . n 
A 1 3501 SER 3501 3501 3501 SER SER A . n 
A 1 3502 THR 3502 3502 3502 THR THR A . n 
A 1 3503 ILE 3503 3503 3503 ILE ILE A . n 
A 1 3504 ALA 3504 3504 3504 ALA ALA A . n 
A 1 3505 GLY 3505 3505 3505 GLY GLY A . n 
A 1 3506 ASP 3506 3506 3506 ASP ASP A . n 
A 1 3507 CYS 3507 3507 3507 CYS CYS A . n 
A 1 3508 LEU 3508 3508 3508 LEU LEU A . n 
A 1 3509 LEU 3509 3509 3509 LEU LEU A . n 
A 1 3510 SER 3510 3510 3510 SER SER A . n 
A 1 3511 ALA 3511 3511 3511 ALA ALA A . n 
A 1 3512 ALA 3512 3512 3512 ALA ALA A . n 
A 1 3513 PHE 3513 3513 3513 PHE PHE A . n 
A 1 3514 ILE 3514 3514 3514 ILE ILE A . n 
A 1 3515 ALA 3515 3515 3515 ALA ALA A . n 
A 1 3516 TYR 3516 3516 3516 TYR TYR A . n 
A 1 3517 ALA 3517 3517 3517 ALA ALA A . n 
A 1 3518 GLY 3518 3518 3518 GLY GLY A . n 
A 1 3519 TYR 3519 3519 3519 TYR TYR A . n 
A 1 3520 PHE 3520 3520 3520 PHE PHE A . n 
A 1 3521 ASP 3521 3521 3521 ASP ASP A . n 
A 1 3522 GLN 3522 3522 3522 GLN GLN A . n 
A 1 3523 GLN 3523 3523 3523 GLN GLN A . n 
A 1 3524 MET 3524 3524 3524 MET MET A . n 
A 1 3525 ARG 3525 3525 3525 ARG ARG A . n 
A 1 3526 GLN 3526 3526 3526 GLN GLN A . n 
A 1 3527 ASN 3527 3527 3527 ASN ASN A . n 
A 1 3528 LEU 3528 3528 3528 LEU LEU A . n 
A 1 3529 PHE 3529 3529 3529 PHE PHE A . n 
A 1 3530 THR 3530 3530 3530 THR THR A . n 
A 1 3531 THR 3531 3531 3531 THR THR A . n 
A 1 3532 TRP 3532 3532 3532 TRP TRP A . n 
A 1 3533 SER 3533 3533 3533 SER SER A . n 
A 1 3534 HIS 3534 3534 3534 HIS HIS A . n 
A 1 3535 HIS 3535 3535 3535 HIS HIS A . n 
A 1 3536 LEU 3536 3536 3536 LEU LEU A . n 
A 1 3537 GLN 3537 3537 3537 GLN GLN A . n 
A 1 3538 GLN 3538 3538 3538 GLN GLN A . n 
A 1 3539 ALA 3539 3539 3539 ALA ALA A . n 
A 1 3540 ASN 3540 3540 3540 ASN ASN A . n 
A 1 3541 ILE 3541 3541 3541 ILE ILE A . n 
A 1 3542 GLN 3542 3542 3542 GLN GLN A . n 
A 1 3543 PHE 3543 3543 3543 PHE PHE A . n 
A 1 3544 ARG 3544 3544 3544 ARG ARG A . n 
A 1 3545 THR 3545 3545 3545 THR THR A . n 
A 1 3546 ASP 3546 3546 3546 ASP ASP A . n 
A 1 3547 ILE 3547 3547 3547 ILE ILE A . n 
A 1 3548 ALA 3548 3548 3548 ALA ALA A . n 
A 1 3549 ARG 3549 3549 3549 ARG ARG A . n 
A 1 3550 THR 3550 3550 3550 THR THR A . n 
A 1 3551 GLU 3551 3551 3551 GLU GLU A . n 
A 1 3552 TYR 3552 3552 3552 TYR TYR A . n 
A 1 3553 LEU 3553 3553 3553 LEU LEU A . n 
A 1 3554 SER 3554 3554 3554 SER SER A . n 
A 1 3555 ASN 3555 3555 3555 ASN ASN A . n 
A 1 3556 ALA 3556 3556 3556 ALA ALA A . n 
A 1 3557 ASP 3557 3557 3557 ASP ASP A . n 
A 1 3558 GLU 3558 3558 3558 GLU GLU A . n 
A 1 3559 ARG 3559 3559 3559 ARG ARG A . n 
A 1 3560 LEU 3560 3560 3560 LEU LEU A . n 
A 1 3561 ARG 3561 3561 3561 ARG ARG A . n 
A 1 3562 TRP 3562 3562 3562 TRP TRP A . n 
A 1 3563 GLN 3563 3563 3563 GLN GLN A . n 
A 1 3564 ALA 3564 3564 3564 ALA ALA A . n 
A 1 3565 SER 3565 3565 3565 SER SER A . n 
A 1 3566 SER 3566 3566 3566 SER SER A . n 
A 1 3567 LEU 3567 3567 3567 LEU LEU A . n 
A 1 3568 PRO 3568 3568 3568 PRO PRO A . n 
A 1 3569 ALA 3569 3569 3569 ALA ALA A . n 
A 1 3570 ASP 3570 3570 3570 ASP ASP A . n 
A 1 3571 ASP 3571 3571 3571 ASP ASP A . n 
A 1 3572 LEU 3572 3572 3572 LEU LEU A . n 
A 1 3573 CYS 3573 3573 3573 CYS CYS A . n 
A 1 3574 THR 3574 3574 3574 THR THR A . n 
A 1 3575 GLU 3575 3575 3575 GLU GLU A . n 
A 1 3576 ASN 3576 3576 3576 ASN ASN A . n 
A 1 3577 ALA 3577 3577 3577 ALA ALA A . n 
A 1 3578 ILE 3578 3578 3578 ILE ILE A . n 
A 1 3579 MET 3579 3579 3579 MET MET A . n 
A 1 3580 LEU 3580 3580 3580 LEU LEU A . n 
A 1 3581 LYS 3581 3581 3581 LYS LYS A . n 
A 1 3582 ARG 3582 3582 3582 ARG ARG A . n 
A 1 3583 PHE 3583 3583 3583 PHE PHE A . n 
A 1 3584 ASN 3584 3584 3584 ASN ASN A . n 
A 1 3585 ARG 3585 3585 3585 ARG ARG A . n 
A 1 3586 TYR 3586 3586 3586 TYR TYR A . n 
A 1 3587 PRO 3587 3587 3587 PRO PRO A . n 
A 1 3588 LEU 3588 3588 3588 LEU LEU A . n 
A 1 3589 ILE 3589 3589 3589 ILE ILE A . n 
A 1 3590 ILE 3590 3590 3590 ILE ILE A . n 
A 1 3591 ASP 3591 3591 3591 ASP ASP A . n 
A 1 3592 PRO 3592 3592 3592 PRO PRO A . n 
A 1 3593 SER 3593 3593 3593 SER SER A . n 
A 1 3594 GLY 3594 3594 3594 GLY GLY A . n 
A 1 3595 GLN 3595 3595 3595 GLN GLN A . n 
A 1 3596 ALA 3596 3596 3596 ALA ALA A . n 
A 1 3597 THR 3597 3597 3597 THR THR A . n 
A 1 3598 GLU 3598 3598 3598 GLU GLU A . n 
A 1 3599 PHE 3599 3599 3599 PHE PHE A . n 
A 1 3600 ILE 3600 3600 3600 ILE ILE A . n 
A 1 3601 MET 3601 3601 3601 MET MET A . n 
A 1 3602 ASN 3602 3602 3602 ASN ASN A . n 
A 1 3603 GLU 3603 3603 3603 GLU GLU A . n 
A 1 3604 TYR 3604 3604 3604 TYR TYR A . n 
A 1 3605 LYS 3605 3605 3605 LYS LYS A . n 
A 1 3606 ASP 3606 3606 3606 ASP ASP A . n 
A 1 3607 ARG 3607 3607 3607 ARG ARG A . n 
A 1 3608 LYS 3608 3608 3608 LYS LYS A . n 
A 1 3609 ILE 3609 3609 3609 ILE ILE A . n 
A 1 3610 THR 3610 3610 3610 THR THR A . n 
A 1 3611 ARG 3611 3611 3611 ARG ARG A . n 
A 1 3612 THR 3612 3612 3612 THR THR A . n 
A 1 3613 SER 3613 3613 3613 SER SER A . n 
A 1 3614 PHE 3614 3614 3614 PHE PHE A . n 
A 1 3615 LEU 3615 3615 3615 LEU LEU A . n 
A 1 3616 ASP 3616 3616 3616 ASP ASP A . n 
A 1 3617 ASP 3617 3617 3617 ASP ASP A . n 
A 1 3618 ALA 3618 3618 3618 ALA ALA A . n 
A 1 3619 PHE 3619 3619 3619 PHE PHE A . n 
A 1 3620 ARG 3620 3620 3620 ARG ARG A . n 
A 1 3621 LYS 3621 3621 3621 LYS LYS A . n 
A 1 3622 ASN 3622 3622 3622 ASN ASN A . n 
A 1 3623 LEU 3623 3623 3623 LEU LEU A . n 
A 1 3624 GLU 3624 3624 3624 GLU GLU A . n 
A 1 3625 SER 3625 3625 3625 SER SER A . n 
A 1 3626 ALA 3626 3626 3626 ALA ALA A . n 
A 1 3627 LEU 3627 3627 3627 LEU LEU A . n 
A 1 3628 ARG 3628 3628 3628 ARG ARG A . n 
A 1 3629 PHE 3629 3629 3629 PHE PHE A . n 
A 1 3630 GLY 3630 3630 3630 GLY GLY A . n 
A 1 3631 ASN 3631 3631 3631 ASN ASN A . n 
A 1 3632 PRO 3632 3632 3632 PRO PRO A . n 
A 1 3633 LEU 3633 3633 3633 LEU LEU A . n 
A 1 3634 LEU 3634 3634 3634 LEU LEU A . n 
A 1 3635 VAL 3635 3635 3635 VAL VAL A . n 
A 1 3636 GLN 3636 3636 3636 GLN GLN A . n 
A 1 3637 ASP 3637 3637 3637 ASP ASP A . n 
A 1 3638 VAL 3638 3638 3638 VAL VAL A . n 
A 1 3639 GLU 3639 3639 3639 GLU GLU A . n 
A 1 3640 SER 3640 3640 3640 SER SER A . n 
A 1 3641 TYR 3641 3641 3641 TYR TYR A . n 
A 1 3642 ASP 3642 3642 3642 ASP ASP A . n 
A 1 3643 PRO 3643 3643 3643 PRO PRO A . n 
A 1 3644 VAL 3644 3644 3644 VAL VAL A . n 
A 1 3645 LEU 3645 3645 3645 LEU LEU A . n 
A 1 3646 ASN 3646 3646 3646 ASN ASN A . n 
A 1 3647 PRO 3647 3647 3647 PRO PRO A . n 
A 1 3648 VAL 3648 3648 3648 VAL VAL A . n 
A 1 3649 LEU 3649 3649 3649 LEU LEU A . n 
A 1 3650 ASN 3650 3650 3650 ASN ASN A . n 
A 1 3651 ARG 3651 3651 3651 ARG ARG A . n 
A 1 3652 GLU 3652 3652 3652 GLU GLU A . n 
A 1 3653 VAL 3653 3653 3653 VAL VAL A . n 
A 1 3654 ARG 3654 3654 3654 ARG ARG A . n 
A 1 3655 ARG 3655 3655 3655 ARG ARG A . n 
A 1 3656 THR 3656 3656 3656 THR THR A . n 
A 1 3657 GLY 3657 3657 3657 GLY GLY A . n 
A 1 3658 GLY 3658 3658 3658 GLY GLY A . n 
A 1 3659 ARG 3659 3659 3659 ARG ARG A . n 
A 1 3660 VAL 3660 3660 3660 VAL VAL A . n 
A 1 3661 LEU 3661 3661 3661 LEU LEU A . n 
A 1 3662 ILE 3662 3662 3662 ILE ILE A . n 
A 1 3663 THR 3663 3663 3663 THR THR A . n 
A 1 3664 LEU 3664 3664 3664 LEU LEU A . n 
A 1 3665 GLY 3665 3665 3665 GLY GLY A . n 
A 1 3666 ASP 3666 3666 3666 ASP ASP A . n 
A 1 3667 GLN 3667 3667 3667 GLN GLN A . n 
A 1 3668 ASP 3668 3668 3668 ASP ASP A . n 
A 1 3669 ILE 3669 3669 3669 ILE ILE A . n 
A 1 3670 ASP 3670 3670 3670 ASP ASP A . n 
A 1 3671 LEU 3671 3671 3671 LEU LEU A . n 
A 1 3672 SER 3672 3672 3672 SER SER A . n 
A 1 3673 PRO 3673 3673 3673 PRO PRO A . n 
A 1 3674 SER 3674 3674 3674 SER SER A . n 
A 1 3675 PHE 3675 3675 3675 PHE PHE A . n 
A 1 3676 VAL 3676 3676 3676 VAL VAL A . n 
A 1 3677 ILE 3677 3677 3677 ILE ILE A . n 
A 1 3678 PHE 3678 3678 3678 PHE PHE A . n 
A 1 3679 LEU 3679 3679 3679 LEU LEU A . n 
A 1 3680 SER 3680 3680 3680 SER SER A . n 
A 1 3681 THR 3681 3681 3681 THR THR A . n 
A 1 3682 ARG 3682 3682 3682 ARG ARG A . n 
A 1 3683 ASP 3683 3683 3683 ASP ASP A . n 
A 1 3684 PRO 3684 3684 3684 PRO PRO A . n 
A 1 3685 THR 3685 3685 3685 THR THR A . n 
A 1 3686 VAL 3686 3686 3686 VAL VAL A . n 
A 1 3687 GLU 3687 3687 3687 GLU GLU A . n 
A 1 3688 PHE 3688 3688 3688 PHE PHE A . n 
A 1 3689 PRO 3689 3689 3689 PRO PRO A . n 
A 1 3690 PRO 3690 3690 3690 PRO PRO A . n 
A 1 3691 ASP 3691 3691 3691 ASP ASP A . n 
A 1 3692 LEU 3692 3692 3692 LEU LEU A . n 
A 1 3693 CYS 3693 3693 3693 CYS CYS A . n 
A 1 3694 SER 3694 3694 3694 SER SER A . n 
A 1 3695 ARG 3695 3695 3695 ARG ARG A . n 
A 1 3696 VAL 3696 3696 3696 VAL VAL A . n 
A 1 3697 THR 3697 3697 3697 THR THR A . n 
A 1 3698 PHE 3698 3698 3698 PHE PHE A . n 
A 1 3699 VAL 3699 3699 3699 VAL VAL A . n 
A 1 3700 ASN 3700 3700 3700 ASN ASN A . n 
A 1 3701 PHE 3701 3701 3701 PHE PHE A . n 
A 1 3702 THR 3702 3702 3702 THR THR A . n 
A 1 3703 VAL 3703 3703 3703 VAL VAL A . n 
A 1 3704 THR 3704 3704 3704 THR THR A . n 
A 1 3705 ARG 3705 3705 3705 ARG ARG A . n 
A 1 3706 SER 3706 3706 3706 SER SER A . n 
A 1 3707 SER 3707 3707 3707 SER SER A . n 
A 1 3708 LEU 3708 3708 3708 LEU LEU A . n 
A 1 3709 GLN 3709 3709 3709 GLN GLN A . n 
A 1 3710 SER 3710 3710 3710 SER SER A . n 
A 1 3711 GLN 3711 3711 3711 GLN GLN A . n 
A 1 3712 CYS 3712 3712 3712 CYS CYS A . n 
A 1 3713 LEU 3713 3713 3713 LEU LEU A . n 
A 1 3714 ASN 3714 3714 3714 ASN ASN A . n 
A 1 3715 GLU 3715 3715 3715 GLU GLU A . n 
A 1 3716 VAL 3716 3716 3716 VAL VAL A . n 
A 1 3717 LEU 3717 3717 3717 LEU LEU A . n 
A 1 3718 LYS 3718 3718 3718 LYS LYS A . n 
A 1 3719 ALA 3719 3719 3719 ALA ALA A . n 
A 1 3720 GLU 3720 3720 3720 GLU GLU A . n 
A 1 3721 ARG 3721 3721 3721 ARG ARG A . n 
A 1 3722 PRO 3722 3722 3722 PRO PRO A . n 
A 1 3723 ASP 3723 3723 3723 ASP ASP A . n 
A 1 3724 VAL 3724 3724 3724 VAL VAL A . n 
A 1 3725 ASP 3725 3725 3725 ASP ASP A . n 
A 1 3726 GLU 3726 3726 3726 GLU GLU A . n 
A 1 3727 LYS 3727 3727 3727 LYS LYS A . n 
A 1 3728 ARG 3728 3728 3728 ARG ARG A . n 
A 1 3729 SER 3729 3729 3729 SER SER A . n 
A 1 3730 ASP 3730 3730 3730 ASP ASP A . n 
A 1 3731 LEU 3731 3731 3731 LEU LEU A . n 
A 1 3732 LEU 3732 3732 3732 LEU LEU A . n 
A 1 3733 LYS 3733 3733 3733 LYS LYS A . n 
A 1 3734 LEU 3734 3734 3734 LEU LEU A . n 
A 1 3735 GLN 3735 3735 3735 GLN GLN A . n 
A 1 3736 GLY 3736 3736 3736 GLY GLY A . n 
A 1 3737 GLU 3737 3737 3737 GLU GLU A . n 
A 1 3738 PHE 3738 3738 3738 PHE PHE A . n 
A 1 3739 GLN 3739 3739 3739 GLN GLN A . n 
A 1 3740 LEU 3740 3740 3740 LEU LEU A . n 
A 1 3741 ARG 3741 3741 3741 ARG ARG A . n 
A 1 3742 LEU 3742 3742 3742 LEU LEU A . n 
A 1 3743 ARG 3743 3743 3743 ARG ARG A . n 
A 1 3744 GLN 3744 3744 3744 GLN GLN A . n 
A 1 3745 LEU 3745 3745 3745 LEU LEU A . n 
A 1 3746 GLU 3746 3746 3746 GLU GLU A . n 
A 1 3747 LYS 3747 3747 3747 LYS LYS A . n 
A 1 3748 SER 3748 3748 3748 SER SER A . n 
A 1 3749 LEU 3749 3749 3749 LEU LEU A . n 
A 1 3750 LEU 3750 3750 3750 LEU LEU A . n 
A 1 3751 GLN 3751 3751 3751 GLN GLN A . n 
A 1 3752 ALA 3752 3752 3752 ALA ALA A . n 
A 1 3753 LEU 3753 3753 3753 LEU LEU A . n 
A 1 3754 ASN 3754 3754 3754 ASN ASN A . n 
A 1 3755 GLU 3755 3755 3755 GLU GLU A . n 
A 1 3756 VAL 3756 3756 3756 VAL VAL A . n 
A 1 3757 LYS 3757 3757 3757 LYS LYS A . n 
A 1 3758 GLY 3758 3758 3758 GLY GLY A . n 
A 1 3759 ARG 3759 3759 3759 ARG ARG A . n 
A 1 3760 ILE 3760 3760 3760 ILE ILE A . n 
A 1 3761 LEU 3761 3761 3761 LEU LEU A . n 
A 1 3762 ASP 3762 3762 3762 ASP ASP A . n 
A 1 3763 ASP 3763 3763 3763 ASP ASP A . n 
A 1 3764 ASP 3764 3764 3764 ASP ASP A . n 
A 1 3765 THR 3765 3765 3765 THR THR A . n 
A 1 3766 ILE 3766 3766 3766 ILE ILE A . n 
A 1 3767 ILE 3767 3767 3767 ILE ILE A . n 
A 1 3768 THR 3768 3768 3768 THR THR A . n 
A 1 3769 THR 3769 3769 3769 THR THR A . n 
A 1 3770 LEU 3770 3770 3770 LEU LEU A . n 
A 1 3771 GLU 3771 3771 3771 GLU GLU A . n 
A 1 3772 ASN 3772 3772 3772 ASN ASN A . n 
A 1 3773 LEU 3773 3773 3773 LEU LEU A . n 
A 1 3774 LYS 3774 3774 3774 LYS LYS A . n 
A 1 3775 ARG 3775 3775 3775 ARG ARG A . n 
A 1 3776 GLU 3776 3776 3776 GLU GLU A . n 
A 1 3777 ALA 3777 3777 3777 ALA ALA A . n 
A 1 3778 ALA 3778 3778 3778 ALA ALA A . n 
A 1 3779 GLU 3779 3779 3779 GLU GLU A . n 
A 1 3780 VAL 3780 3780 3780 VAL VAL A . n 
A 1 3781 THR 3781 3781 3781 THR THR A . n 
A 1 3782 ARG 3782 3782 3782 ARG ARG A . n 
A 1 3783 LYS 3783 3783 3783 LYS LYS A . n 
A 1 3784 VAL 3784 3784 3784 VAL VAL A . n 
A 1 3785 GLU 3785 3785 3785 GLU GLU A . n 
A 1 3786 GLU 3786 3786 3786 GLU GLU A . n 
A 1 3787 THR 3787 3787 3787 THR THR A . n 
A 1 3788 ASP 3788 3788 3788 ASP ASP A . n 
A 1 3789 ILE 3789 3789 3789 ILE ILE A . n 
A 1 3790 VAL 3790 3790 3790 VAL VAL A . n 
A 1 3791 MET 3791 3791 3791 MET MET A . n 
A 1 3792 GLN 3792 3792 3792 GLN GLN A . n 
A 1 3793 GLU 3793 3793 3793 GLU GLU A . n 
A 1 3794 VAL 3794 3794 3794 VAL VAL A . n 
A 1 3795 GLU 3795 3795 3795 GLU GLU A . n 
A 1 3796 THR 3796 3796 3796 THR THR A . n 
A 1 3797 VAL 3797 3797 3797 VAL VAL A . n 
A 1 3798 SER 3798 3798 3798 SER SER A . n 
A 1 3799 GLN 3799 3799 3799 GLN GLN A . n 
A 1 3800 GLN 3800 3800 3800 GLN GLN A . n 
A 1 3801 TYR 3801 3801 3801 TYR TYR A . n 
A 1 3802 LEU 3802 3802 3802 LEU LEU A . n 
A 1 3803 PRO 3803 3803 3803 PRO PRO A . n 
A 1 3804 LEU 3804 3804 3804 LEU LEU A . n 
A 1 3805 SER 3805 3805 3805 SER SER A . n 
A 1 3806 THR 3806 3806 3806 THR THR A . n 
A 1 3807 ALA 3807 3807 3807 ALA ALA A . n 
A 1 3808 CYS 3808 3808 3808 CYS CYS A . n 
A 1 3809 SER 3809 3809 3809 SER SER A . n 
A 1 3810 SER 3810 3810 3810 SER SER A . n 
A 1 3811 ILE 3811 3811 3811 ILE ILE A . n 
A 1 3812 TYR 3812 3812 3812 TYR TYR A . n 
A 1 3813 PHE 3813 3813 3813 PHE PHE A . n 
A 1 3814 THR 3814 3814 3814 THR THR A . n 
A 1 3815 MET 3815 3815 3815 MET MET A . n 
A 1 3816 GLU 3816 3816 3816 GLU GLU A . n 
A 1 3817 SER 3817 3817 3817 SER SER A . n 
A 1 3818 LEU 3818 3818 3818 LEU LEU A . n 
A 1 3819 LYS 3819 3819 3819 LYS LYS A . n 
A 1 3820 GLN 3820 3820 3820 GLN GLN A . n 
A 1 3821 ILE 3821 3821 3821 ILE ILE A . n 
A 1 3822 HIS 3822 3822 3822 HIS HIS A . n 
A 1 3823 PHE 3823 3823 3823 PHE PHE A . n 
A 1 3824 LEU 3824 3824 3824 LEU LEU A . n 
A 1 3825 TYR 3825 3825 3825 TYR TYR A . n 
A 1 3826 GLN 3826 3826 3826 GLN GLN A . n 
A 1 3827 TYR 3827 3827 3827 TYR TYR A . n 
A 1 3828 SER 3828 3828 3828 SER SER A . n 
A 1 3829 LEU 3829 3829 3829 LEU LEU A . n 
A 1 3830 GLN 3830 3830 3830 GLN GLN A . n 
A 1 3831 PHE 3831 3831 3831 PHE PHE A . n 
A 1 3832 PHE 3832 3832 3832 PHE PHE A . n 
A 1 3833 LEU 3833 3833 3833 LEU LEU A . n 
A 1 3834 ASP 3834 3834 3834 ASP ASP A . n 
A 1 3835 ILE 3835 3835 3835 ILE ILE A . n 
A 1 3836 TYR 3836 3836 3836 TYR TYR A . n 
A 1 3837 HIS 3837 3837 3837 HIS HIS A . n 
A 1 3838 ASN 3838 3838 3838 ASN ASN A . n 
A 1 3839 VAL 3839 3839 3839 VAL VAL A . n 
A 1 3840 LEU 3840 3840 3840 LEU LEU A . n 
A 1 3841 TYR 3841 3841 3841 TYR TYR A . n 
A 1 3842 GLU 3842 3842 3842 GLU GLU A . n 
A 1 3843 ASN 3843 3843 3843 ASN ASN A . n 
A 1 3844 PRO 3844 3844 3844 PRO PRO A . n 
A 1 3845 ASN 3845 3845 3845 ASN ASN A . n 
A 1 3846 LEU 3846 3846 3846 LEU LEU A . n 
A 1 3847 LYS 3847 3847 3847 LYS LYS A . n 
A 1 3848 GLY 3848 3848 3848 GLY GLY A . n 
A 1 3849 VAL 3849 3849 3849 VAL VAL A . n 
A 1 3850 THR 3850 3850 3850 THR THR A . n 
A 1 3851 ASP 3851 3851 3851 ASP ASP A . n 
A 1 3852 HIS 3852 3852 3852 HIS HIS A . n 
A 1 3853 THR 3853 3853 3853 THR THR A . n 
A 1 3854 GLN 3854 3854 3854 GLN GLN A . n 
A 1 3855 ARG 3855 3855 3855 ARG ARG A . n 
A 1 3856 LEU 3856 3856 3856 LEU LEU A . n 
A 1 3857 SER 3857 3857 3857 SER SER A . n 
A 1 3858 ILE 3858 3858 3858 ILE ILE A . n 
A 1 3859 ILE 3859 3859 3859 ILE ILE A . n 
A 1 3860 THR 3860 3860 3860 THR THR A . n 
A 1 3861 LYS 3861 3861 3861 LYS LYS A . n 
A 1 3862 ASP 3862 3862 3862 ASP ASP A . n 
A 1 3863 LEU 3863 3863 3863 LEU LEU A . n 
A 1 3864 PHE 3864 3864 3864 PHE PHE A . n 
A 1 3865 GLN 3865 3865 3865 GLN GLN A . n 
A 1 3866 VAL 3866 3866 3866 VAL VAL A . n 
A 1 3867 ALA 3867 3867 3867 ALA ALA A . n 
A 1 3868 PHE 3868 3868 3868 PHE PHE A . n 
A 1 3869 ASN 3869 3869 3869 ASN ASN A . n 
A 1 3870 ARG 3870 3870 3870 ARG ARG A . n 
A 1 3871 VAL 3871 3871 3871 VAL VAL A . n 
A 1 3872 ALA 3872 3872 3872 ALA ALA A . n 
A 1 3873 ARG 3873 3873 3873 ARG ARG A . n 
A 1 3874 GLY 3874 3874 3874 GLY GLY A . n 
A 1 3875 MET 3875 3875 3875 MET MET A . n 
A 1 3876 LEU 3876 3876 3876 LEU LEU A . n 
A 1 3877 HIS 3877 3877 3877 HIS HIS A . n 
A 1 3878 GLN 3878 3878 3878 GLN GLN A . n 
A 1 3879 ASP 3879 3879 3879 ASP ASP A . n 
A 1 3880 HIS 3880 3880 3880 HIS HIS A . n 
A 1 3881 ILE 3881 3881 3881 ILE ILE A . n 
A 1 3882 THR 3882 3882 3882 THR THR A . n 
A 1 3883 PHE 3883 3883 3883 PHE PHE A . n 
A 1 3884 ALA 3884 3884 3884 ALA ALA A . n 
A 1 3885 MET 3885 3885 3885 MET MET A . n 
A 1 3886 LEU 3886 3886 3886 LEU LEU A . n 
A 1 3887 LEU 3887 3887 3887 LEU LEU A . n 
A 1 3888 ALA 3888 3888 3888 ALA ALA A . n 
A 1 3889 ARG 3889 3889 3889 ARG ARG A . n 
A 1 3890 ILE 3890 3890 3890 ILE ILE A . n 
A 1 3891 LYS 3891 3891 3891 LYS LYS A . n 
A 1 3892 LEU 3892 3892 3892 LEU LEU A . n 
A 1 3893 LYS 3893 3893 3893 LYS LYS A . n 
A 1 3894 GLY 3894 3894 3894 GLY GLY A . n 
A 1 3895 THR 3895 3895 3895 THR THR A . n 
A 1 3896 VAL 3896 3896 3896 VAL VAL A . n 
A 1 3897 GLY 3897 3897 3897 GLY GLY A . n 
A 1 3898 GLU 3898 3898 3898 GLU GLU A . n 
A 1 3899 PRO 3899 3899 3899 PRO PRO A . n 
A 1 3900 THR 3900 3900 3900 THR THR A . n 
A 1 3901 TYR 3901 3901 3901 TYR TYR A . n 
A 1 3902 ASP 3902 3902 3902 ASP ASP A . n 
A 1 3903 ALA 3903 3903 3903 ALA ALA A . n 
A 1 3904 GLU 3904 3904 3904 GLU GLU A . n 
A 1 3905 PHE 3905 3905 3905 PHE PHE A . n 
A 1 3906 GLN 3906 3906 3906 GLN GLN A . n 
A 1 3907 HIS 3907 3907 3907 HIS HIS A . n 
A 1 3908 PHE 3908 3908 3908 PHE PHE A . n 
A 1 3909 LEU 3909 3909 3909 LEU LEU A . n 
A 1 3910 ARG 3910 3910 3910 ARG ARG A . n 
A 1 3911 GLY 3911 3911 3911 GLY GLY A . n 
A 1 3912 ASN 3912 3912 3912 ASN ASN A . n 
A 1 3913 GLU 3913 3913 3913 GLU GLU A . n 
A 1 3914 ILE 3914 3914 3914 ILE ILE A . n 
A 1 3915 VAL 3915 3915 3915 VAL VAL A . n 
A 1 3916 LEU 3916 3916 3916 LEU LEU A . n 
A 1 3917 SER 3917 3917 3917 SER SER A . n 
A 1 3918 ALA 3918 3918 3918 ALA ALA A . n 
A 1 3919 GLY 3919 3919 3919 GLY GLY A . n 
A 1 3920 SER 3920 3920 3920 SER SER A . n 
A 1 3921 THR 3921 3921 3921 THR THR A . n 
A 1 3922 PRO 3922 3922 3922 PRO PRO A . n 
A 1 3923 ARG 3923 3923 3923 ARG ARG A . n 
A 1 3924 ILE 3924 3924 3924 ILE ILE A . n 
A 1 3925 GLN 3925 3925 3925 GLN GLN A . n 
A 1 3926 GLY 3926 3926 3926 GLY GLY A . n 
A 1 3927 LEU 3927 3927 3927 LEU LEU A . n 
A 1 3928 THR 3928 3928 3928 THR THR A . n 
A 1 3929 VAL 3929 3929 3929 VAL VAL A . n 
A 1 3930 GLU 3930 3930 3930 GLU GLU A . n 
A 1 3931 GLN 3931 3931 3931 GLN GLN A . n 
A 1 3932 ALA 3932 3932 3932 ALA ALA A . n 
A 1 3933 GLU 3933 3933 3933 GLU GLU A . n 
A 1 3934 ALA 3934 3934 3934 ALA ALA A . n 
A 1 3935 VAL 3935 3935 3935 VAL VAL A . n 
A 1 3936 VAL 3936 3936 3936 VAL VAL A . n 
A 1 3937 ARG 3937 3937 3937 ARG ARG A . n 
A 1 3938 LEU 3938 3938 3938 LEU LEU A . n 
A 1 3939 SER 3939 3939 3939 SER SER A . n 
A 1 3940 CYS 3940 3940 3940 CYS CYS A . n 
A 1 3941 LEU 3941 3941 3941 LEU LEU A . n 
A 1 3942 PRO 3942 3942 3942 PRO PRO A . n 
A 1 3943 ALA 3943 3943 3943 ALA ALA A . n 
A 1 3944 PHE 3944 3944 3944 PHE PHE A . n 
A 1 3945 LYS 3945 3945 3945 LYS LYS A . n 
A 1 3946 ASP 3946 3946 3946 ASP ASP A . n 
A 1 3947 LEU 3947 3947 3947 LEU LEU A . n 
A 1 3948 ILE 3948 3948 3948 ILE ILE A . n 
A 1 3949 ALA 3949 3949 3949 ALA ALA A . n 
A 1 3950 LYS 3950 3950 3950 LYS LYS A . n 
A 1 3951 VAL 3951 3951 3951 VAL VAL A . n 
A 1 3952 GLN 3952 3952 3952 GLN GLN A . n 
A 1 3953 ALA 3953 3953 3953 ALA ALA A . n 
A 1 3954 ASP 3954 3954 3954 ASP ASP A . n 
A 1 3955 GLU 3955 3955 3955 GLU GLU A . n 
A 1 3956 GLN 3956 3956 3956 GLN GLN A . n 
A 1 3957 PHE 3957 3957 3957 PHE PHE A . n 
A 1 3958 GLY 3958 3958 3958 GLY GLY A . n 
A 1 3959 ILE 3959 3959 3959 ILE ILE A . n 
A 1 3960 TRP 3960 3960 3960 TRP TRP A . n 
A 1 3961 LEU 3961 3961 3961 LEU LEU A . n 
A 1 3962 ASP 3962 3962 3962 ASP ASP A . n 
A 1 3963 SER 3963 3963 3963 SER SER A . n 
A 1 3964 SER 3964 3964 3964 SER SER A . n 
A 1 3965 SER 3965 3965 3965 SER SER A . n 
A 1 3966 PRO 3966 3966 3966 PRO PRO A . n 
A 1 3967 GLU 3967 3967 3967 GLU GLU A . n 
A 1 3968 GLN 3968 3968 3968 GLN GLN A . n 
A 1 3969 THR 3969 3969 3969 THR THR A . n 
A 1 3970 VAL 3970 3970 3970 VAL VAL A . n 
A 1 3971 PRO 3971 3971 3971 PRO PRO A . n 
A 1 3972 TYR 3972 3972 3972 TYR TYR A . n 
A 1 3973 LEU 3973 3973 3973 LEU LEU A . n 
A 1 3974 TRP 3974 3974 3974 TRP TRP A . n 
A 1 3975 SER 3975 3975 3975 SER SER A . n 
A 1 3976 GLU 3976 3976 3976 GLU GLU A . n 
A 1 3977 GLU 3977 3977 3977 GLU GLU A . n 
A 1 3978 THR 3978 3978 3978 THR THR A . n 
A 1 3979 PRO 3979 3979 3979 PRO PRO A . n 
A 1 3980 ALA 3980 3980 3980 ALA ALA A . n 
A 1 3981 THR 3981 3981 3981 THR THR A . n 
A 1 3982 PRO 3982 3982 3982 PRO PRO A . n 
A 1 3983 ILE 3983 3983 3983 ILE ILE A . n 
A 1 3984 GLY 3984 3984 3984 GLY GLY A . n 
A 1 3985 GLN 3985 3985 3985 GLN GLN A . n 
A 1 3986 ALA 3986 3986 3986 ALA ALA A . n 
A 1 3987 ILE 3987 3987 3987 ILE ILE A . n 
A 1 3988 HIS 3988 3988 3988 HIS HIS A . n 
A 1 3989 ARG 3989 3989 3989 ARG ARG A . n 
A 1 3990 LEU 3990 3990 3990 LEU LEU A . n 
A 1 3991 LEU 3991 3991 3991 LEU LEU A . n 
A 1 3992 LEU 3992 3992 3992 LEU LEU A . n 
A 1 3993 ILE 3993 3993 3993 ILE ILE A . n 
A 1 3994 GLN 3994 3994 3994 GLN GLN A . n 
A 1 3995 ALA 3995 3995 3995 ALA ALA A . n 
A 1 3996 PHE 3996 3996 3996 PHE PHE A . n 
A 1 3997 ARG 3997 3997 3997 ARG ARG A . n 
A 1 3998 PRO 3998 3998 3998 PRO PRO A . n 
A 1 3999 ASP 3999 3999 3999 ASP ASP A . n 
A 1 4000 ARG 4000 4000 4000 ARG ARG A . n 
A 1 4001 LEU 4001 4001 4001 LEU LEU A . n 
A 1 4002 LEU 4002 4002 4002 LEU LEU A . n 
A 1 4003 ALA 4003 4003 4003 ALA ALA A . n 
A 1 4004 MET 4004 4004 4004 MET MET A . n 
A 1 4005 ALA 4005 4005 4005 ALA ALA A . n 
A 1 4006 HIS 4006 4006 4006 HIS HIS A . n 
A 1 4007 MET 4007 4007 4007 MET MET A . n 
A 1 4008 PHE 4008 4008 4008 PHE PHE A . n 
A 1 4009 VAL 4009 4009 4009 VAL VAL A . n 
A 1 4010 SER 4010 4010 4010 SER SER A . n 
A 1 4011 THR 4011 4011 4011 THR THR A . n 
A 1 4012 ASN 4012 4012 4012 ASN ASN A . n 
A 1 4013 LEU 4013 4013 4013 LEU LEU A . n 
A 1 4014 GLY 4014 4014 4014 GLY GLY A . n 
A 1 4015 GLU 4015 4015 4015 GLU GLU A . n 
A 1 4016 SER 4016 4016 4016 SER SER A . n 
A 1 4017 PHE 4017 4017 4017 PHE PHE A . n 
A 1 4018 MET 4018 4018 4018 MET MET A . n 
A 1 4019 SER 4019 4019 4019 SER SER A . n 
A 1 4020 ILE 4020 4020 4020 ILE ILE A . n 
A 1 4021 MET 4021 4021 4021 MET MET A . n 
A 1 4022 GLU 4022 4022 4022 GLU GLU A . n 
A 1 4023 GLN 4023 4023 4023 GLN GLN A . n 
A 1 4024 PRO 4024 4024 4024 PRO PRO A . n 
A 1 4025 LEU 4025 4025 4025 LEU LEU A . n 
A 1 4026 ASP 4026 4026 4026 ASP ASP A . n 
A 1 4027 LEU 4027 4027 4027 LEU LEU A . n 
A 1 4028 THR 4028 4028 4028 THR THR A . n 
A 1 4029 HIS 4029 4029 4029 HIS HIS A . n 
A 1 4030 ILE 4030 4030 4030 ILE ILE A . n 
A 1 4031 VAL 4031 4031 4031 VAL VAL A . n 
A 1 4032 GLY 4032 4032 4032 GLY GLY A . n 
A 1 4033 THR 4033 4033 4033 THR THR A . n 
A 1 4034 GLU 4034 4034 4034 GLU GLU A . n 
A 1 4035 VAL 4035 4035 4035 VAL VAL A . n 
A 1 4036 LYS 4036 4036 4036 LYS LYS A . n 
A 1 4037 PRO 4037 4037 4037 PRO PRO A . n 
A 1 4038 ASN 4038 4038 4038 ASN ASN A . n 
A 1 4039 THR 4039 4039 4039 THR THR A . n 
A 1 4040 PRO 4040 4040 4040 PRO PRO A . n 
A 1 4041 VAL 4041 4041 4041 VAL VAL A . n 
A 1 4042 LEU 4042 4042 4042 LEU LEU A . n 
A 1 4043 MET 4043 4043 4043 MET MET A . n 
A 1 4044 CYS 4044 4044 4044 CYS CYS A . n 
A 1 4045 SER 4045 4045 4045 SER SER A . n 
A 1 4046 VAL 4046 4046 4046 VAL VAL A . n 
A 1 4047 PRO 4047 4047 4047 PRO PRO A . n 
A 1 4048 GLY 4048 4048 4048 GLY GLY A . n 
A 1 4049 TYR 4049 4049 4049 TYR TYR A . n 
A 1 4050 ASP 4050 4050 4050 ASP ASP A . n 
A 1 4051 ALA 4051 4051 4051 ALA ALA A . n 
A 1 4052 SER 4052 4052 4052 SER SER A . n 
A 1 4053 GLY 4053 4053 4053 GLY GLY A . n 
A 1 4054 HIS 4054 4054 4054 HIS HIS A . n 
A 1 4055 VAL 4055 4055 4055 VAL VAL A . n 
A 1 4056 GLU 4056 4056 4056 GLU GLU A . n 
A 1 4057 ASP 4057 4057 4057 ASP ASP A . n 
A 1 4058 LEU 4058 4058 4058 LEU LEU A . n 
A 1 4059 ALA 4059 4059 4059 ALA ALA A . n 
A 1 4060 ALA 4060 4060 4060 ALA ALA A . n 
A 1 4061 GLU 4061 4061 4061 GLU GLU A . n 
A 1 4062 GLN 4062 4062 4062 GLN GLN A . n 
A 1 4063 ASN 4063 4063 4063 ASN ASN A . n 
A 1 4064 THR 4064 4064 4064 THR THR A . n 
A 1 4065 GLN 4065 4065 4065 GLN GLN A . n 
A 1 4066 ILE 4066 4066 4066 ILE ILE A . n 
A 1 4067 THR 4067 4067 4067 THR THR A . n 
A 1 4068 SER 4068 4068 4068 SER SER A . n 
A 1 4069 ILE 4069 4069 4069 ILE ILE A . n 
A 1 4070 ALA 4070 4070 4070 ALA ALA A . n 
A 1 4071 ILE 4071 4071 4071 ILE ILE A . n 
A 1 4072 GLY 4072 4072 4072 GLY GLY A . n 
A 1 4073 SER 4073 4073 4073 SER SER A . n 
A 1 4074 ALA 4074 4074 4074 ALA ALA A . n 
A 1 4075 GLU 4075 4075 4075 GLU GLU A . n 
A 1 4076 GLY 4076 4076 4076 GLY GLY A . n 
A 1 4077 PHE 4077 4077 4077 PHE PHE A . n 
A 1 4078 ASN 4078 4078 4078 ASN ASN A . n 
A 1 4079 GLN 4079 4079 4079 GLN GLN A . n 
A 1 4080 ALA 4080 4080 4080 ALA ALA A . n 
A 1 4081 ASP 4081 4081 4081 ASP ASP A . n 
A 1 4082 LYS 4082 4082 4082 LYS LYS A . n 
A 1 4083 ALA 4083 4083 4083 ALA ALA A . n 
A 1 4084 ILE 4084 4084 4084 ILE ILE A . n 
A 1 4085 ASN 4085 4085 4085 ASN ASN A . n 
A 1 4086 THR 4086 4086 4086 THR THR A . n 
A 1 4087 ALA 4087 4087 4087 ALA ALA A . n 
A 1 4088 VAL 4088 4088 4088 VAL VAL A . n 
A 1 4089 LYS 4089 4089 4089 LYS LYS A . n 
A 1 4090 SER 4090 4090 4090 SER SER A . n 
A 1 4091 GLY 4091 4091 4091 GLY GLY A . n 
A 1 4092 ARG 4092 4092 4092 ARG ARG A . n 
A 1 4093 TRP 4093 4093 4093 TRP TRP A . n 
A 1 4094 VAL 4094 4094 4094 VAL VAL A . n 
A 1 4095 MET 4095 4095 4095 MET MET A . n 
A 1 4096 LEU 4096 4096 4096 LEU LEU A . n 
A 1 4097 LYS 4097 4097 4097 LYS LYS A . n 
A 1 4098 ASN 4098 4098 4098 ASN ASN A . n 
A 1 4099 VAL 4099 4099 4099 VAL VAL A . n 
A 1 4100 HIS 4100 4100 4100 HIS HIS A . n 
A 1 4101 LEU 4101 4101 4101 LEU LEU A . n 
A 1 4102 ALA 4102 4102 4102 ALA ALA A . n 
A 1 4103 PRO 4103 4103 4103 PRO PRO A . n 
A 1 4104 GLY 4104 4104 4104 GLY GLY A . n 
A 1 4105 TRP 4105 4105 4105 TRP TRP A . n 
A 1 4106 LEU 4106 4106 4106 LEU LEU A . n 
A 1 4107 MET 4107 4107 4107 MET MET A . n 
A 1 4108 GLN 4108 4108 4108 GLN GLN A . n 
A 1 4109 LEU 4109 4109 4109 LEU LEU A . n 
A 1 4110 GLU 4110 4110 4110 GLU GLU A . n 
A 1 4111 LYS 4111 4111 4111 LYS LYS A . n 
A 1 4112 LYS 4112 4112 4112 LYS LYS A . n 
A 1 4113 LEU 4113 4113 4113 LEU LEU A . n 
A 1 4114 HIS 4114 4114 4114 HIS HIS A . n 
A 1 4115 SER 4115 4115 4115 SER SER A . n 
A 1 4116 LEU 4116 4116 4116 LEU LEU A . n 
A 1 4117 GLN 4117 4117 4117 GLN GLN A . n 
A 1 4118 PRO 4118 4118 4118 PRO PRO A . n 
A 1 4119 HIS 4119 4119 4119 HIS HIS A . n 
A 1 4120 ALA 4120 4120 4120 ALA ALA A . n 
A 1 4121 CYS 4121 4121 4121 CYS CYS A . n 
A 1 4122 PHE 4122 4122 4122 PHE PHE A . n 
A 1 4123 ARG 4123 4123 4123 ARG ARG A . n 
A 1 4124 LEU 4124 4124 4124 LEU LEU A . n 
A 1 4125 PHE 4125 4125 4125 PHE PHE A . n 
A 1 4126 LEU 4126 4126 4126 LEU LEU A . n 
A 1 4127 THR 4127 4127 4127 THR THR A . n 
A 1 4128 MET 4128 4128 4128 MET MET A . n 
A 1 4129 GLU 4129 4129 4129 GLU GLU A . n 
A 1 4130 ILE 4130 4130 4130 ILE ILE A . n 
A 1 4131 ASN 4131 4131 4131 ASN ASN A . n 
A 1 4132 PRO 4132 4132 4132 PRO PRO A . n 
A 1 4133 LYS 4133 4133 4133 LYS LYS A . n 
A 1 4134 VAL 4134 4134 4134 VAL VAL A . n 
A 1 4135 PRO 4135 4135 4135 PRO PRO A . n 
A 1 4136 VAL 4136 4136 4136 VAL VAL A . n 
A 1 4137 ASN 4137 4137 4137 ASN ASN A . n 
A 1 4138 LEU 4138 4138 4138 LEU LEU A . n 
A 1 4139 LEU 4139 4139 4139 LEU LEU A . n 
A 1 4140 ARG 4140 4140 4140 ARG ARG A . n 
A 1 4141 ALA 4141 4141 4141 ALA ALA A . n 
A 1 4142 GLY 4142 4142 4142 GLY GLY A . n 
A 1 4143 ARG 4143 4143 4143 ARG ARG A . n 
A 1 4144 ILE 4144 4144 4144 ILE ILE A . n 
A 1 4145 PHE 4145 4145 4145 PHE PHE A . n 
A 1 4146 VAL 4146 4146 4146 VAL VAL A . n 
A 1 4147 PHE 4147 4147 4147 PHE PHE A . n 
A 1 4148 GLU 4148 4148 4148 GLU GLU A . n 
A 1 4149 PRO 4149 4149 4149 PRO PRO A . n 
A 1 4150 PRO 4150 4150 4150 PRO PRO A . n 
A 1 4151 PRO 4151 4151 4151 PRO PRO A . n 
A 1 4152 GLY 4152 4152 4152 GLY GLY A . n 
A 1 4153 VAL 4153 4153 4153 VAL VAL A . n 
A 1 4154 LYS 4154 4154 4154 LYS LYS A . n 
A 1 4155 ALA 4155 4155 4155 ALA ALA A . n 
A 1 4156 ASN 4156 4156 4156 ASN ASN A . n 
A 1 4157 MET 4157 4157 4157 MET MET A . n 
A 1 4158 LEU 4158 4158 4158 LEU LEU A . n 
A 1 4159 ARG 4159 4159 4159 ARG ARG A . n 
A 1 4160 THR 4160 4160 4160 THR THR A . n 
A 1 4161 PHE 4161 4161 4161 PHE PHE A . n 
A 1 4162 SER 4162 4162 4162 SER SER A . n 
A 1 4163 SER 4163 4163 4163 SER SER A . n 
A 1 4164 ILE 4164 4164 4164 ILE ILE A . n 
A 1 4165 PRO 4165 4165 4165 PRO PRO A . n 
A 1 4166 VAL 4166 4166 4166 VAL VAL A . n 
A 1 4167 SER 4167 4167 4167 SER SER A . n 
A 1 4168 ARG 4168 4168 4168 ARG ARG A . n 
A 1 4169 ILE 4169 4169 4169 ILE ILE A . n 
A 1 4170 CYS 4170 4170 4170 CYS CYS A . n 
A 1 4171 LYS 4171 4171 4171 LYS LYS A . n 
A 1 4172 SER 4172 4172 4172 SER SER A . n 
A 1 4173 PRO 4173 4173 4173 PRO PRO A . n 
A 1 4174 ASN 4174 4174 4174 ASN ASN A . n 
A 1 4175 GLU 4175 4175 4175 GLU GLU A . n 
A 1 4176 ARG 4176 4176 4176 ARG ARG A . n 
A 1 4177 ALA 4177 4177 4177 ALA ALA A . n 
A 1 4178 ARG 4178 4178 4178 ARG ARG A . n 
A 1 4179 LEU 4179 4179 4179 LEU LEU A . n 
A 1 4180 TYR 4180 4180 4180 TYR TYR A . n 
A 1 4181 PHE 4181 4181 4181 PHE PHE A . n 
A 1 4182 LEU 4182 4182 4182 LEU LEU A . n 
A 1 4183 LEU 4183 4183 4183 LEU LEU A . n 
A 1 4184 ALA 4184 4184 4184 ALA ALA A . n 
A 1 4185 TRP 4185 4185 4185 TRP TRP A . n 
A 1 4186 PHE 4186 4186 4186 PHE PHE A . n 
A 1 4187 HIS 4187 4187 4187 HIS HIS A . n 
A 1 4188 ALA 4188 4188 4188 ALA ALA A . n 
A 1 4189 ILE 4189 4189 4189 ILE ILE A . n 
A 1 4190 ILE 4190 4190 4190 ILE ILE A . n 
A 1 4191 GLN 4191 4191 4191 GLN GLN A . n 
A 1 4192 GLU 4192 4192 4192 GLU GLU A . n 
A 1 4193 ARG 4193 4193 4193 ARG ARG A . n 
A 1 4194 LEU 4194 4194 4194 LEU LEU A . n 
A 1 4195 ARG 4195 4195 4195 ARG ARG A . n 
A 1 4196 TYR 4196 4196 4196 TYR TYR A . n 
A 1 4197 ALA 4197 4197 4197 ALA ALA A . n 
A 1 4198 PRO 4198 4198 4198 PRO PRO A . n 
A 1 4199 LEU 4199 4199 4199 LEU LEU A . n 
A 1 4200 GLY 4200 4200 4200 GLY GLY A . n 
A 1 4201 TRP 4201 4201 4201 TRP TRP A . n 
A 1 4202 SER 4202 4202 4202 SER SER A . n 
A 1 4203 LYS 4203 4203 4203 LYS LYS A . n 
A 1 4204 LYS 4204 4204 4204 LYS LYS A . n 
A 1 4205 TYR 4205 4205 4205 TYR TYR A . n 
A 1 4206 GLU 4206 4206 4206 GLU GLU A . n 
A 1 4207 PHE 4207 4207 4207 PHE PHE A . n 
A 1 4208 GLY 4208 4208 4208 GLY GLY A . n 
A 1 4209 GLU 4209 4209 4209 GLU GLU A . n 
A 1 4210 SER 4210 4210 4210 SER SER A . n 
A 1 4211 ASP 4211 4211 4211 ASP ASP A . n 
A 1 4212 LEU 4212 4212 4212 LEU LEU A . n 
A 1 4213 ARG 4213 4213 4213 ARG ARG A . n 
A 1 4214 SER 4214 4214 4214 SER SER A . n 
A 1 4215 ALA 4215 4215 4215 ALA ALA A . n 
A 1 4216 CYS 4216 4216 4216 CYS CYS A . n 
A 1 4217 ASP 4217 4217 4217 ASP ASP A . n 
A 1 4218 THR 4218 4218 4218 THR THR A . n 
A 1 4219 VAL 4219 4219 4219 VAL VAL A . n 
A 1 4220 ASP 4220 4220 4220 ASP ASP A . n 
A 1 4221 THR 4221 4221 4221 THR THR A . n 
A 1 4222 TRP 4222 4222 4222 TRP TRP A . n 
A 1 4223 LEU 4223 4223 4223 LEU LEU A . n 
A 1 4224 ASP 4224 4224 4224 ASP ASP A . n 
A 1 4225 ASP 4225 4225 4225 ASP ASP A . n 
A 1 4226 THR 4226 4226 4226 THR THR A . n 
A 1 4227 ALA 4227 4227 4227 ALA ALA A . n 
A 1 4228 LYS 4228 4228 4228 LYS LYS A . n 
A 1 4229 GLY 4229 4229 4229 GLY GLY A . n 
A 1 4230 ARG 4230 4230 4230 ARG ARG A . n 
A 1 4231 GLN 4231 4231 4231 GLN GLN A . n 
A 1 4232 ASN 4232 4232 4232 ASN ASN A . n 
A 1 4233 ILE 4233 4233 4233 ILE ILE A . n 
A 1 4234 SER 4234 4234 4234 SER SER A . n 
A 1 4235 PRO 4235 4235 4235 PRO PRO A . n 
A 1 4236 ASP 4236 4236 4236 ASP ASP A . n 
A 1 4237 LYS 4237 4237 4237 LYS LYS A . n 
A 1 4238 ILE 4238 4238 4238 ILE ILE A . n 
A 1 4239 PRO 4239 4239 4239 PRO PRO A . n 
A 1 4240 TRP 4240 4240 4240 TRP TRP A . n 
A 1 4241 SER 4241 4241 4241 SER SER A . n 
A 1 4242 ALA 4242 4242 4242 ALA ALA A . n 
A 1 4243 LEU 4243 4243 4243 LEU LEU A . n 
A 1 4244 LYS 4244 4244 4244 LYS LYS A . n 
A 1 4245 THR 4245 4245 4245 THR THR A . n 
A 1 4246 LEU 4246 4246 4246 LEU LEU A . n 
A 1 4247 MET 4247 4247 4247 MET MET A . n 
A 1 4248 ALA 4248 4248 4248 ALA ALA A . n 
A 1 4249 GLN 4249 4249 4249 GLN GLN A . n 
A 1 4250 SER 4250 4250 4250 SER SER A . n 
A 1 4251 ILE 4251 4251 4251 ILE ILE A . n 
A 1 4252 TYR 4252 4252 4252 TYR TYR A . n 
A 1 4253 GLY 4253 4253 4253 GLY GLY A . n 
A 1 4254 GLY 4254 4254 4254 GLY GLY A . n 
A 1 4255 ARG 4255 4255 4255 ARG ARG A . n 
A 1 4256 VAL 4256 4256 4256 VAL VAL A . n 
A 1 4257 ASP 4257 4257 4257 ASP ASP A . n 
A 1 4258 ASN 4258 4258 4258 ASN ASN A . n 
A 1 4259 GLU 4259 4259 4259 GLU GLU A . n 
A 1 4260 PHE 4260 4260 4260 PHE PHE A . n 
A 1 4261 ASP 4261 4261 4261 ASP ASP A . n 
A 1 4262 GLN 4262 4262 4262 GLN GLN A . n 
A 1 4263 ARG 4263 4263 4263 ARG ARG A . n 
A 1 4264 LEU 4264 4264 4264 LEU LEU A . n 
A 1 4265 LEU 4265 4265 4265 LEU LEU A . n 
A 1 4266 ASN 4266 4266 4266 ASN ASN A . n 
A 1 4267 THR 4267 4267 4267 THR THR A . n 
A 1 4268 PHE 4268 4268 4268 PHE PHE A . n 
A 1 4269 LEU 4269 4269 4269 LEU LEU A . n 
A 1 4270 GLU 4270 4270 4270 GLU GLU A . n 
A 1 4271 ARG 4271 4271 4271 ARG ARG A . n 
A 1 4272 LEU 4272 4272 4272 LEU LEU A . n 
A 1 4273 PHE 4273 4273 4273 PHE PHE A . n 
A 1 4274 THR 4274 4274 4274 THR THR A . n 
A 1 4275 THR 4275 4275 4275 THR THR A . n 
A 1 4276 ARG 4276 4276 4276 ARG ARG A . n 
A 1 4277 SER 4277 4277 4277 SER SER A . n 
A 1 4278 PHE 4278 4278 4278 PHE PHE A . n 
A 1 4279 ASP 4279 4279 4279 ASP ASP A . n 
A 1 4280 SER 4280 4280 4280 SER SER A . n 
A 1 4281 GLU 4281 4281 4281 GLU GLU A . n 
A 1 4282 PHE 4282 4282 4282 PHE PHE A . n 
A 1 4283 LYS 4283 4283 4283 LYS LYS A . n 
A 1 4284 LEU 4284 4284 4284 LEU LEU A . n 
A 1 4285 ALA 4285 4285 4285 ALA ALA A . n 
A 1 4286 CYS 4286 4286 4286 CYS CYS A . n 
A 1 4287 LYS 4287 4287 4287 LYS LYS A . n 
A 1 4288 VAL 4288 4288 4288 VAL VAL A . n 
A 1 4289 ASP 4289 4289 4289 ASP ALA 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 ?    ?   ?   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' ? 
# 
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 . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ASP 2388 ? CG  ? A ASP 2388 CG  
2 1 Y 1 A ASP 2388 ? OD1 ? A ASP 2388 OD1 
3 1 Y 1 A ASP 2388 ? OD2 ? A ASP 2388 OD2 
4 1 Y 1 A MET 2412 ? CG  ? A MET 2412 CG  
5 1 Y 1 A MET 2412 ? SD  ? A MET 2412 SD  
6 1 Y 1 A MET 2412 ? CE  ? A MET 2412 CE  
7 1 Y 1 A ASP 4289 ? CG  ? A ASP 4289 CG  
8 1 Y 1 A ASP 4289 ? OD1 ? A ASP 4289 OD1 
9 1 Y 1 A ASP 4289 ? OD2 ? A ASP 4289 OD2 
# 
_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                     9BN3 
_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                         9BN3 
_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                   9BN3 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9BN3 
_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' ? 0.003 ? 23659 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.642 ? 32097 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 5.747 ? 3158  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.041 ? 3612  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005 ? 4108  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9BN3 
_struct.title                        'The alpha registry-locked dynein motor domain mutant in 5mM ATP condition, class1' 
_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        9BN3 
_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 ? 
# 
_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              9BN3 
_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 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9BN3 
_struct_ref_seq_dif.mon_id                       ASP 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      2389 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q14204 
_struct_ref_seq_dif.db_mon_id                    GLU 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          2389 
_struct_ref_seq_dif.details                      conflict 
_struct_ref_seq_dif.pdbx_auth_seq_num            2389 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1   AA1 GLN A 1465 ? TRP A 1470 ? GLN A 1465 TRP A 1470 1 ? 6  
HELX_P HELX_P2   AA2 TRP A 1490 ? SER A 1510 ? TRP A 1490 SER A 1510 1 ? 21 
HELX_P HELX_P3   AA3 ALA A 1520 ? SER A 1554 ? ALA A 1520 SER A 1554 1 ? 35 
HELX_P HELX_P4   AA4 LEU A 1561 ? SER A 1585 ? LEU A 1561 SER A 1585 1 ? 25 
HELX_P HELX_P5   AA5 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P6   AA6 GLY A 1596 ? SER A 1625 ? GLY A 1596 SER A 1625 1 ? 30 
HELX_P HELX_P7   AA7 PHE A 1626 ? VAL A 1632 ? PHE A 1626 VAL A 1632 5 ? 7  
HELX_P HELX_P8   AA8 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P9   AA9 ASN A 1646 ? LYS A 1652 ? ASN A 1646 LYS A 1652 5 ? 7  
HELX_P HELX_P10  AB1 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P11  AB2 LYS A 1697 ? ALA A 1730 ? LYS A 1697 ALA A 1730 1 ? 34 
HELX_P HELX_P12  AB3 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P13  AB4 GLN A 1746 ? GLY A 1773 ? GLN A 1746 GLY A 1773 1 ? 28 
HELX_P HELX_P14  AB5 ALA A 1776 ? LEU A 1797 ? ALA A 1776 LEU A 1797 1 ? 22 
HELX_P HELX_P15  AB6 PRO A 1801 ? SER A 1828 ? PRO A 1801 SER A 1828 1 ? 28 
HELX_P HELX_P16  AB7 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P17  AB8 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P18  AB9 GLY A 1911 ? LEU A 1923 ? GLY A 1911 LEU A 1923 1 ? 13 
HELX_P HELX_P19  AC1 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P20  AC2 GLU A 1959 ? LEU A 1963 ? GLU A 1959 LEU A 1963 5 ? 5  
HELX_P HELX_P21  AC3 GLU A 1964 ? GLU A 1984 ? GLU A 1964 GLU A 1984 1 ? 21 
HELX_P HELX_P22  AC4 HIS A 1985 ? ASN A 1987 ? HIS A 1985 ASN A 1987 5 ? 3  
HELX_P HELX_P23  AC5 ASP A 2045 ? GLN A 2057 ? ASP A 2045 GLN A 2057 1 ? 13 
HELX_P HELX_P24  AC6 THR A 2061 ? ASP A 2077 ? THR A 2061 ASP A 2077 1 ? 17 
HELX_P HELX_P25  AC7 GLY A 2089 ? ARG A 2113 ? GLY A 2089 ARG A 2113 1 ? 25 
HELX_P HELX_P26  AC8 PRO A 2132 ? VAL A 2146 ? PRO A 2132 VAL A 2146 1 ? 15 
HELX_P HELX_P27  AC9 GLU A 2152 ? PHE A 2165 ? GLU A 2152 PHE A 2165 1 ? 14 
HELX_P HELX_P28  AD1 MET A 2175 ? CYS A 2186 ? MET A 2175 CYS A 2186 1 ? 12 
HELX_P HELX_P29  AD2 GLY A 2200 ? ASN A 2217 ? GLY A 2200 ASN A 2217 1 ? 18 
HELX_P HELX_P30  AD3 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P31  AD4 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P32  AD5 GLY A 2278 ? ASP A 2289 ? GLY A 2278 ASP A 2289 1 ? 12 
HELX_P HELX_P33  AD6 ASP A 2308 ? GLU A 2313 ? ASP A 2308 GLU A 2313 1 ? 6  
HELX_P HELX_P34  AD7 LEU A 2315 ? ASP A 2320 ? LEU A 2315 ASP A 2320 1 ? 6  
HELX_P HELX_P35  AD8 THR A 2352 ? ARG A 2358 ? THR A 2352 ARG A 2358 1 ? 7  
HELX_P HELX_P36  AD9 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P37  AE1 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P38  AE2 ASN A 2430 ? GLN A 2442 ? ASN A 2430 GLN A 2442 1 ? 13 
HELX_P HELX_P39  AE3 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P40  AE4 GLN A 2482 ? SER A 2503 ? GLN A 2482 SER A 2503 1 ? 22 
HELX_P HELX_P41  AE5 ARG A 2507 ? ARG A 2520 ? ARG A 2507 ARG A 2520 1 ? 14 
HELX_P HELX_P42  AE6 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P43  AE7 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P44  AE8 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P45  AE9 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P46  AF1 GLY A 2600 ? ARG A 2610 ? GLY A 2600 ARG A 2610 1 ? 11 
HELX_P HELX_P47  AF2 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P48  AF3 GLN A 2677 ? HIS A 2689 ? GLN A 2677 HIS A 2689 1 ? 13 
HELX_P HELX_P49  AF4 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P50  AF5 GLY A 2740 ? LEU A 2756 ? GLY A 2740 LEU A 2756 1 ? 17 
HELX_P HELX_P51  AF6 ARG A 2757 ? THR A 2764 ? ARG A 2757 THR A 2764 5 ? 8  
HELX_P HELX_P52  AF7 TYR A 2765 ? ARG A 2783 ? TYR A 2765 ARG A 2783 1 ? 19 
HELX_P HELX_P53  AF8 SER A 2795 ? ALA A 2809 ? SER A 2795 ALA A 2809 1 ? 15 
HELX_P HELX_P54  AF9 PRO A 2817 ? GLN A 2834 ? PRO A 2817 GLN A 2834 1 ? 18 
HELX_P HELX_P55  AG1 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P56  AG2 ASP A 2862 ? ALA A 2866 ? ASP A 2862 ALA A 2866 5 ? 5  
HELX_P HELX_P57  AG3 ASP A 2885 ? GLU A 2904 ? ASP A 2885 GLU A 2904 1 ? 20 
HELX_P HELX_P58  AG4 PHE A 2912 ? GLN A 2928 ? PHE A 2912 GLN A 2928 1 ? 17 
HELX_P HELX_P59  AG5 GLY A 2942 ? ASN A 2954 ? GLY A 2942 ASN A 2954 1 ? 13 
HELX_P HELX_P60  AG6 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P61  AG7 LYS A 2986 ? GLU A 2988 ? LYS A 2986 GLU A 2988 5 ? 3  
HELX_P HELX_P62  AG8 ASP A 3001 ? ASN A 3014 ? ASP A 3001 ASN A 3014 1 ? 14 
HELX_P HELX_P63  AG9 GLY A 3023 ? GLU A 3040 ? GLY A 3023 GLU A 3040 1 ? 18 
HELX_P HELX_P64  AH1 SER A 3046 ? ASN A 3061 ? SER A 3046 ASN A 3061 1 ? 16 
HELX_P HELX_P65  AH2 SER A 3071 ? SER A 3082 ? SER A 3071 SER A 3082 1 ? 12 
HELX_P HELX_P66  AH3 PRO A 3083 ? PHE A 3086 ? PRO A 3083 PHE A 3086 5 ? 4  
HELX_P HELX_P67  AH4 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P68  AH5 HIS A 3139 ? ARG A 3164 ? HIS A 3139 ARG A 3164 1 ? 26 
HELX_P HELX_P69  AH6 THR A 3172 ? ARG A 3220 ? THR A 3172 ARG A 3220 1 ? 49 
HELX_P HELX_P70  AH7 VAL A 3472 ? ALA A 3517 ? VAL A 3472 ALA A 3517 1 ? 46 
HELX_P HELX_P71  AH8 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P72  AH9 ALA A 3548 ? LEU A 3553 ? ALA A 3548 LEU A 3553 1 ? 6  
HELX_P HELX_P73  AI1 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P74  AI2 ASP A 3570 ? ARG A 3582 ? ASP A 3570 ARG A 3582 1 ? 13 
HELX_P HELX_P75  AI3 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P76  AI4 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P77  AI5 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P78  AI6 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P79  AI7 LEU A 3645 ? ARG A 3651 ? LEU A 3645 ARG A 3651 1 ? 7  
HELX_P HELX_P80  AI8 PRO A 3689 ? SER A 3694 ? PRO A 3689 SER A 3694 1 ? 6  
HELX_P HELX_P81  AI9 THR A 3704 ? GLU A 3720 ? THR A 3704 GLU A 3720 1 ? 17 
HELX_P HELX_P82  AJ1 ARG A 3721 ? LEU A 3734 ? ARG A 3721 LEU A 3734 1 ? 14 
HELX_P HELX_P83  AJ2 GLY A 3736 ? LYS A 3757 ? GLY A 3736 LYS A 3757 1 ? 22 
HELX_P HELX_P84  AJ3 ASP A 3763 ? GLU A 3786 ? ASP A 3763 GLU A 3786 1 ? 24 
HELX_P HELX_P85  AJ4 GLU A 3793 ? TYR A 3801 ? GLU A 3793 TYR A 3801 1 ? 9  
HELX_P HELX_P86  AJ5 TYR A 3801 ? LEU A 3818 ? TYR A 3801 LEU A 3818 1 ? 18 
HELX_P HELX_P87  AJ6 SER A 3828 ? GLU A 3842 ? SER A 3828 GLU A 3842 1 ? 15 
HELX_P HELX_P88  AJ7 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P89  AJ8 ASP A 3879 ? THR A 3895 ? ASP A 3879 THR A 3895 1 ? 17 
HELX_P HELX_P90  AJ9 TYR A 3901 ? GLY A 3911 ? TYR A 3901 GLY A 3911 1 ? 11 
HELX_P HELX_P91  AK1 ASN A 3912 ? ILE A 3914 ? ASN A 3912 ILE A 3914 5 ? 3  
HELX_P HELX_P92  AK2 THR A 3928 ? LEU A 3941 ? THR A 3928 LEU A 3941 1 ? 14 
HELX_P HELX_P93  AK3 PRO A 3942 ? LYS A 3945 ? PRO A 3942 LYS A 3945 5 ? 4  
HELX_P HELX_P94  AK4 LEU A 3947 ? ALA A 3953 ? LEU A 3947 ALA A 3953 1 ? 7  
HELX_P HELX_P95  AK5 GLU A 3955 ? ASP A 3962 ? GLU A 3955 ASP A 3962 1 ? 8  
HELX_P HELX_P96  AK6 THR A 3981 ? PHE A 3996 ? THR A 3981 PHE A 3996 1 ? 16 
HELX_P HELX_P97  AK7 ARG A 3997 ? ASP A 3999 ? ARG A 3997 ASP A 3999 5 ? 3  
HELX_P HELX_P98  AK8 ARG A 4000 ? GLY A 4014 ? ARG A 4000 GLY A 4014 1 ? 15 
HELX_P HELX_P99  AK9 MET A 4018 ? GLN A 4023 ? MET A 4018 GLN A 4023 1 ? 6  
HELX_P HELX_P100 AL1 ASP A 4026 ? VAL A 4035 ? ASP A 4026 VAL A 4035 1 ? 10 
HELX_P HELX_P101 AL2 ALA A 4051 ? ASN A 4063 ? ALA A 4051 ASN A 4063 1 ? 13 
HELX_P HELX_P102 AL3 SER A 4073 ? LYS A 4089 ? SER A 4073 LYS A 4089 1 ? 17 
HELX_P HELX_P103 AL4 ASN A 4098 ? LEU A 4101 ? ASN A 4098 LEU A 4101 5 ? 4  
HELX_P HELX_P104 AL5 ALA A 4102 ? LEU A 4113 ? ALA A 4102 LEU A 4113 1 ? 12 
HELX_P HELX_P105 AL6 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P106 AL7 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P107 AL8 PRO A 4165 ? LYS A 4171 ? PRO A 4165 LYS A 4171 1 ? 7  
HELX_P HELX_P108 AL9 ASN A 4174 ? ARG A 4193 ? ASN A 4174 ARG A 4193 1 ? 20 
HELX_P HELX_P109 AM1 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P110 AM2 SER A 4234 ? ILE A 4238 ? SER A 4234 ILE A 4238 5 ? 5  
HELX_P HELX_P111 AM3 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P112 AM4 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P113 AM5 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P114 AM6 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P115 AM7 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P116 AM8 ASN A 4326 ? MET A 4346 ? ASN A 4326 MET A 4346 1 ? 21 
HELX_P HELX_P117 AM9 TRP A 4376 ? ILE A 4391 ? TRP A 4376 ILE A 4391 1 ? 16 
HELX_P HELX_P118 AN1 ASP A 4407 ? GLY A 4440 ? ASP A 4407 GLY A 4440 1 ? 34 
HELX_P HELX_P119 AN2 THR A 4445 ? LYS A 4457 ? THR A 4445 LYS A 4457 1 ? 13 
HELX_P HELX_P120 AN3 PRO A 4461 ? SER A 4465 ? PRO A 4461 SER A 4465 5 ? 5  
HELX_P HELX_P121 AN4 THR A 4474 ? GLY A 4499 ? THR A 4474 GLY A 4499 1 ? 26 
HELX_P HELX_P122 AN5 GLY A 4512 ? LEU A 4514 ? GLY A 4512 LEU A 4514 5 ? 3  
HELX_P HELX_P123 AN6 VAL A 4516 ? ASN A 4532 ? VAL A 4516 ASN A 4532 1 ? 17 
HELX_P HELX_P124 AN7 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_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 ? 2 ? 
AA8 ? 3 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 5 ? 
AB4 ? 4 ? 
AB5 ? 5 ? 
AB6 ? 5 ? 
AB7 ? 2 ? 
AB8 ? 5 ? 
AB9 ? 2 ? 
AC1 ? 4 ? 
AC2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB3 4 5 ? parallel      
AB4 1 2 ? anti-parallel 
AB4 2 3 ? parallel      
AB4 3 4 ? 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 
AB8 1 2 ? parallel      
AB8 2 3 ? parallel      
AB8 3 4 ? parallel      
AB8 4 5 ? parallel      
AB9 1 2 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? parallel      
AC2 3 4 ? anti-parallel 
AC2 4 5 ? parallel      
AC2 5 6 ? anti-parallel 
AC2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 1477 ? VAL A 1478 ? LEU A 1477 VAL A 1478 
AA1 2 LEU A 1486 ? ILE A 1487 ? LEU A 1486 ILE A 1487 
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 VAL A 1684 ? SER A 1691 ? VAL A 1684 SER A 1691 
AA3 1 ARG A 1843 ? PHE A 1846 ? ARG A 1843 PHE A 1846 
AA3 2 LEU A 1857 ? GLN A 1860 ? LEU A 1857 GLN A 1860 
AA3 3 PHE A 1866 ? ASN A 1867 ? PHE A 1866 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 PHE A 2015 ? ILE A 2016 ? PHE A 2015 ILE A 2016 
AA6 1 THR A 1998 ? GLU A 2000 ? THR A 1998 GLU A 2000 
AA6 2 GLN A 2005 ? LYS A 2007 ? GLN A 2005 LYS A 2007 
AA7 1 MET A 2221 ? VAL A 2223 ? MET A 2221 VAL A 2223 
AA7 2 MET A 2361 ? TRP A 2363 ? MET A 2361 TRP A 2363 
AA8 1 GLU A 2248 ? ALA A 2251 ? GLU A 2248 ALA A 2251 
AA8 2 LYS A 2297 ? VAL A 2302 ? LYS A 2297 VAL A 2302 
AA8 3 ARG A 2340 ? MET A 2342 ? ARG A 2340 MET A 2342 
AA9 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA9 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AB1 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AB1 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AB2 1 TYR A 2537 ? GLU A 2538 ? TYR A 2537 GLU A 2538 
AB2 2 SER A 2546 ? PRO A 2547 ? SER A 2546 PRO A 2547 
AB3 1 MET A 2615 ? ASN A 2621 ? MET A 2615 ASN A 2621 
AB3 2 TRP A 2658 ? ASP A 2664 ? TRP A 2658 ASP A 2664 
AB3 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB3 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB3 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB4 1 CYS A 2639 ? ARG A 2642 ? CYS A 2639 ARG A 2642 
AB4 2 VAL A 2648 ? PRO A 2652 ? VAL A 2648 PRO A 2652 
AB4 3 TRP A 2700 ? LEU A 2703 ? TRP A 2700 LEU A 2703 
AB4 4 GLY A 2691 ? TYR A 2693 ? GLY A 2691 TYR A 2693 
AB5 1 SER A 2957 ? GLN A 2960 ? SER A 2957 GLN A 2960 
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 ? PHE A 3094 ? CYS A 3089 PHE A 3094 
AB6 1 THR A 3610 ? SER A 3613 ? THR A 3610 SER A 3613 
AB6 2 LEU A 3633 ? GLN A 3636 ? LEU A 3633 GLN A 3636 
AB6 3 ILE A 3677 ? THR A 3681 ? ILE A 3677 THR A 3681 
AB6 4 PRO A 3587 ? ILE A 3590 ? PRO A 3587 ILE A 3590 
AB6 5 THR A 3697 ? ASN A 3700 ? THR A 3697 ASN A 3700 
AB7 1 LEU A 3661 ? ILE A 3662 ? LEU A 3661 ILE A 3662 
AB7 2 ILE A 3669 ? ASP A 3670 ? ILE A 3669 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 PHE A 4125 ? GLU A 4129 ? PHE A 4125 GLU A 4129 
AB8 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB8 5 ARG A 4143 ? ILE A 4144 ? ARG A 4143 ILE A 4144 
AB9 1 LYS A 4283 ? VAL A 4288 ? LYS A 4283 VAL A 4288 
AB9 2 LYS A 4292 ? GLN A 4295 ? LYS A 4292 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 THR A 4588 ? LYS A 4594 ? THR A 4588 LYS A 4594 
AC1 4 LEU A 4539 ? VAL A 4545 ? LEU A 4539 VAL A 4545 
AC2 1 ALA A 4568 ? CYS A 4570 ? ALA A 4568 CYS A 4570 
AC2 2 LYS A 4574 ? LEU A 4577 ? LYS A 4574 LEU A 4577 
AC2 3 LEU A 4618 ? ILE A 4626 ? LEU A 4618 ILE A 4626 
AC2 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AC2 5 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AC2 6 LYS A 4564 ? GLN A 4566 ? LYS A 4564 GLN A 4566 
AC2 7 THR A 4583 ? ALA A 4584 ? THR A 4583 ALA A 4584 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 1478 ? N VAL A 1478 O LEU A 1486 ? O LEU A 1486 
AA2 1 2 N ILE A 1665 ? N ILE A 1665 O LEU A 1674 ? O LEU A 1674 
AA2 2 3 N LEU A 1674 ? N LEU A 1674 O PHE A 1686 ? O PHE A 1686 
AA3 1 2 N TYR A 1845 ? N TYR A 1845 O SER A 1858 ? O SER A 1858 
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 PHE A 1930 ? N PHE A 1930 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 2223 ? N VAL A 2223 O VAL A 2362 ? O VAL A 2362 
AA8 1 2 N GLU A 2248 ? N GLU A 2248 O ARG A 2298 ? O ARG A 2298 
AA8 2 3 N GLN A 2299 ? N GLN A 2299 O ARG A 2340 ? O ARG A 2340 
AA9 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AB1 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AB2 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB3 1 2 N VAL A 2618 ? N VAL A 2618 O VAL A 2660 ? O VAL A 2660 
AB3 2 3 N CYS A 2663 ? N CYS A 2663 O VAL A 2709 ? O VAL A 2709 
AB3 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2591 ? N LEU A 2591 
AB3 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB4 1 2 N GLU A 2640 ? N GLU A 2640 O ALA A 2651 ? O ALA A 2651 
AB4 2 3 N LEU A 2650 ? N LEU A 2650 O LYS A 2702 ? O LYS A 2702 
AB4 3 4 O VAL A 2701 ? O VAL A 2701 N PHE A 2692 ? N PHE A 2692 
AB5 1 2 N TYR A 2959 ? N TYR A 2959 O ILE A 2993 ? O ILE A 2993 
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 2935 ? N LEU A 2935 
AB5 4 5 N ILE A 2936 ? N ILE A 2936 O PHE A 3094 ? O PHE A 3094 
AB6 1 2 N THR A 3610 ? N THR A 3610 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 ILE A 3590 ? N ILE A 3590 O VAL A 3699 ? O VAL A 3699 
AB7 1 2 N ILE A 3662 ? N ILE A 3662 O ILE A 3669 ? O ILE A 3669 
AB8 1 2 N ILE A 4069 ? N ILE A 4069 O LYS A 4097 ? O LYS A 4097 
AB8 2 3 N LEU A 4096 ? N LEU A 4096 O THR A 4127 ? O THR A 4127 
AB8 3 4 O LEU A 4126 ? O LEU A 4126 N MET A 4043 ? N MET A 4043 
AB8 4 5 N LEU A 4042 ? N LEU A 4042 O ARG A 4143 ? O ARG A 4143 
AB9 1 2 N LEU A 4284 ? N LEU A 4284 O ILE A 4294 ? O ILE A 4294 
AC1 1 2 N VAL A 4509 ? N VAL A 4509 O THR A 4561 ? O THR A 4561 
AC1 2 3 N PHE A 4558 ? N PHE A 4558 O LEU A 4590 ? O LEU A 4590 
AC1 3 4 O ARG A 4591 ? O ARG A 4591 N GLU A 4542 ? N GLU A 4542 
AC2 1 2 N THR A 4569 ? N THR A 4569 O SER A 4576 ? O SER A 4576 
AC2 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AC2 3 4 O VAL A 4622 ? O VAL A 4622 N LEU A 4607 ? N LEU A 4607 
AC2 4 5 N PRO A 4608 ? N PRO A 4608 O VAL A 4642 ? O VAL A 4642 
AC2 5 6 O LEU A 4643 ? O LEU A 4643 N LYS A 4564 ? N LYS A 4564 
AC2 6 7 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
# 
_pdbx_entry_details.entry_id                   9BN3 
_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 O  A MET 3113 ? ? NH2 A ARG 3140 ? ? 2.18 
2 1 OH A TYR 2265 ? ? O   A TRP 2311 ? ? 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_1             3587 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            PRO 
_pdbx_validate_rmsd_bond.auth_seq_id_2             3587 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.300 
_pdbx_validate_rmsd_bond.bond_target_value         1.502 
_pdbx_validate_rmsd_bond.bond_deviation            -0.202 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.033 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A PRO 3587 ? ? CB A PRO 3587 ? ? CG A PRO 3587 ? ? 88.05 104.80 -16.75 1.90 N 
2 1 N  A PRO 3587 ? ? CD A PRO 3587 ? ? CG A PRO 3587 ? ? 86.73 103.20 -16.47 1.50 N 
# 
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 LYS A 1514 ? ? -86.65  46.71   
2  1 LEU A 1561 ? ? 62.48   65.94   
3  1 PHE A 1626 ? ? 53.68   76.15   
4  1 ASN A 1643 ? ? -92.17  56.57   
5  1 ALA A 1775 ? ? 56.93   -154.52 
6  1 MET A 1861 ? ? -95.78  -64.87  
7  1 ALA A 1862 ? ? -122.65 -57.73  
8  1 GLN A 1876 ? ? 58.20   -165.75 
9  1 ALA A 1898 ? ? -69.02  4.71    
10 1 LEU A 2002 ? ? -98.79  36.70   
11 1 ARG A 2113 ? ? -86.78  49.70   
12 1 PHE A 2165 ? ? -112.29 78.86   
13 1 GLN A 2187 ? ? 66.40   -5.76   
14 1 LEU A 2220 ? ? -46.86  150.84  
15 1 LYS A 2257 ? ? 67.34   -2.22   
16 1 ARG A 2292 ? ? 39.48   57.69   
17 1 PHE A 2427 ? ? -91.43  58.77   
18 1 ASN A 2430 ? ? 57.38   -144.31 
19 1 SER A 2540 ? ? 63.40   -138.42 
20 1 ARG A 2863 ? ? -69.95  5.25    
21 1 MET A 2867 ? ? 41.94   -134.21 
22 1 PRO A 2870 ? ? -66.28  79.60   
23 1 TYR A 2881 ? ? -92.60  53.89   
24 1 ASP A 3045 ? ? -125.66 -168.70 
25 1 PRO A 3070 ? ? -65.94  3.72    
26 1 TYR A 3130 ? ? 71.28   -7.70   
27 1 HIS A 3139 ? ? 73.45   -12.72  
28 1 ARG A 3164 ? ? -97.18  33.45   
29 1 THR A 3545 ? ? -76.31  -169.73 
30 1 ASP A 3546 ? ? 34.91   47.04   
31 1 SER A 3565 ? ? -91.32  48.46   
32 1 ARG A 3721 ? ? 57.50   71.25   
33 1 MET A 3791 ? ? 67.33   -1.02   
34 1 LEU A 3818 ? ? -58.75  -9.61   
35 1 LEU A 3840 ? ? -90.81  -60.04  
36 1 GLU A 3842 ? ? -140.73 34.26   
37 1 HIS A 3877 ? ? -81.34  45.59   
38 1 LEU A 3916 ? ? -171.04 149.06  
39 1 PRO A 3966 ? ? -84.85  41.05   
40 1 ARG A 3997 ? ? 59.99   70.21   
41 1 LEU A 4013 ? ? -140.36 15.22   
42 1 GLU A 4015 ? ? -87.58  45.74   
43 1 SER A 4016 ? ? -143.60 14.17   
44 1 MET A 4043 ? ? -96.80  54.60   
45 1 SER A 4172 ? ? 64.72   -172.87 
46 1 TYR A 4196 ? ? -94.54  52.85   
47 1 PRO A 4239 ? ? -69.80  71.02   
48 1 LYS A 4287 ? ? 56.83   15.91   
49 1 MET A 4346 ? ? -92.71  30.49   
50 1 LEU A 4398 ? ? -93.77  31.27   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BN3 
_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                    9BN3 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.8 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               433112 
_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                 'the alpha registry-locked dynein motor domain mutant in 5mM ATP condition, class1' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BN3 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             3000 
_em_imaging.calibrated_defocus_min          1200 
_em_imaging.calibrated_defocus_max          3000 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        105000 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            30 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              9BN3 
_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                9BN3 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A MET 1    ? A MET 1    
2    1 Y 1 A SER 2    ? A SER 2    
3    1 Y 1 A GLU 3    ? A GLU 3    
4    1 Y 1 A PRO 4    ? A PRO 4    
5    1 Y 1 A GLY 5    ? A GLY 5    
6    1 Y 1 A GLY 6    ? A GLY 6    
7    1 Y 1 A GLY 7    ? A GLY 7    
8    1 Y 1 A GLY 8    ? A GLY 8    
9    1 Y 1 A GLY 9    ? A GLY 9    
10   1 Y 1 A GLU 10   ? A GLU 10   
11   1 Y 1 A ASP 11   ? A ASP 11   
12   1 Y 1 A GLY 12   ? A GLY 12   
13   1 Y 1 A SER 13   ? A SER 13   
14   1 Y 1 A ALA 14   ? A ALA 14   
15   1 Y 1 A GLY 15   ? A GLY 15   
16   1 Y 1 A LEU 16   ? A LEU 16   
17   1 Y 1 A GLU 17   ? A GLU 17   
18   1 Y 1 A VAL 18   ? A VAL 18   
19   1 Y 1 A SER 19   ? A SER 19   
20   1 Y 1 A ALA 20   ? A ALA 20   
21   1 Y 1 A VAL 21   ? A VAL 21   
22   1 Y 1 A GLN 22   ? A GLN 22   
23   1 Y 1 A ASN 23   ? A ASN 23   
24   1 Y 1 A VAL 24   ? A VAL 24   
25   1 Y 1 A ALA 25   ? A ALA 25   
26   1 Y 1 A ASP 26   ? A ASP 26   
27   1 Y 1 A VAL 27   ? A VAL 27   
28   1 Y 1 A SER 28   ? A SER 28   
29   1 Y 1 A VAL 29   ? A VAL 29   
30   1 Y 1 A LEU 30   ? A LEU 30   
31   1 Y 1 A GLN 31   ? A GLN 31   
32   1 Y 1 A LYS 32   ? A LYS 32   
33   1 Y 1 A HIS 33   ? A HIS 33   
34   1 Y 1 A LEU 34   ? A LEU 34   
35   1 Y 1 A ARG 35   ? A ARG 35   
36   1 Y 1 A LYS 36   ? A LYS 36   
37   1 Y 1 A LEU 37   ? A LEU 37   
38   1 Y 1 A VAL 38   ? A VAL 38   
39   1 Y 1 A PRO 39   ? A PRO 39   
40   1 Y 1 A LEU 40   ? A LEU 40   
41   1 Y 1 A LEU 41   ? A LEU 41   
42   1 Y 1 A LEU 42   ? A LEU 42   
43   1 Y 1 A GLU 43   ? A GLU 43   
44   1 Y 1 A ASP 44   ? A ASP 44   
45   1 Y 1 A GLY 45   ? A GLY 45   
46   1 Y 1 A GLY 46   ? A GLY 46   
47   1 Y 1 A GLU 47   ? A GLU 47   
48   1 Y 1 A ALA 48   ? A ALA 48   
49   1 Y 1 A PRO 49   ? A PRO 49   
50   1 Y 1 A ALA 50   ? A ALA 50   
51   1 Y 1 A ALA 51   ? A ALA 51   
52   1 Y 1 A LEU 52   ? A LEU 52   
53   1 Y 1 A GLU 53   ? A GLU 53   
54   1 Y 1 A ALA 54   ? A ALA 54   
55   1 Y 1 A ALA 55   ? A ALA 55   
56   1 Y 1 A LEU 56   ? A LEU 56   
57   1 Y 1 A GLU 57   ? A GLU 57   
58   1 Y 1 A GLU 58   ? A GLU 58   
59   1 Y 1 A LYS 59   ? A LYS 59   
60   1 Y 1 A SER 60   ? A SER 60   
61   1 Y 1 A ALA 61   ? A ALA 61   
62   1 Y 1 A LEU 62   ? A LEU 62   
63   1 Y 1 A GLU 63   ? A GLU 63   
64   1 Y 1 A GLN 64   ? A GLN 64   
65   1 Y 1 A MET 65   ? A MET 65   
66   1 Y 1 A ARG 66   ? A ARG 66   
67   1 Y 1 A LYS 67   ? A LYS 67   
68   1 Y 1 A PHE 68   ? A PHE 68   
69   1 Y 1 A LEU 69   ? A LEU 69   
70   1 Y 1 A SER 70   ? A SER 70   
71   1 Y 1 A ASP 71   ? A ASP 71   
72   1 Y 1 A PRO 72   ? A PRO 72   
73   1 Y 1 A GLN 73   ? A GLN 73   
74   1 Y 1 A VAL 74   ? A VAL 74   
75   1 Y 1 A HIS 75   ? A HIS 75   
76   1 Y 1 A THR 76   ? A THR 76   
77   1 Y 1 A VAL 77   ? A VAL 77   
78   1 Y 1 A LEU 78   ? A LEU 78   
79   1 Y 1 A VAL 79   ? A VAL 79   
80   1 Y 1 A GLU 80   ? A GLU 80   
81   1 Y 1 A ARG 81   ? A ARG 81   
82   1 Y 1 A SER 82   ? A SER 82   
83   1 Y 1 A THR 83   ? A THR 83   
84   1 Y 1 A LEU 84   ? A LEU 84   
85   1 Y 1 A LYS 85   ? A LYS 85   
86   1 Y 1 A GLU 86   ? A GLU 86   
87   1 Y 1 A ASP 87   ? A ASP 87   
88   1 Y 1 A VAL 88   ? A VAL 88   
89   1 Y 1 A GLY 89   ? A GLY 89   
90   1 Y 1 A ASP 90   ? A ASP 90   
91   1 Y 1 A GLU 91   ? A GLU 91   
92   1 Y 1 A GLY 92   ? A GLY 92   
93   1 Y 1 A GLU 93   ? A GLU 93   
94   1 Y 1 A GLU 94   ? A GLU 94   
95   1 Y 1 A GLU 95   ? A GLU 95   
96   1 Y 1 A LYS 96   ? A LYS 96   
97   1 Y 1 A GLU 97   ? A GLU 97   
98   1 Y 1 A PHE 98   ? A PHE 98   
99   1 Y 1 A ILE 99   ? A ILE 99   
100  1 Y 1 A SER 100  ? A SER 100  
101  1 Y 1 A TYR 101  ? A TYR 101  
102  1 Y 1 A ASN 102  ? A ASN 102  
103  1 Y 1 A ILE 103  ? A ILE 103  
104  1 Y 1 A ASN 104  ? A ASN 104  
105  1 Y 1 A ILE 105  ? A ILE 105  
106  1 Y 1 A ASP 106  ? A ASP 106  
107  1 Y 1 A ILE 107  ? A ILE 107  
108  1 Y 1 A HIS 108  ? A HIS 108  
109  1 Y 1 A TYR 109  ? A TYR 109  
110  1 Y 1 A GLY 110  ? A GLY 110  
111  1 Y 1 A VAL 111  ? A VAL 111  
112  1 Y 1 A LYS 112  ? A LYS 112  
113  1 Y 1 A SER 113  ? A SER 113  
114  1 Y 1 A ASN 114  ? A ASN 114  
115  1 Y 1 A SER 115  ? A SER 115  
116  1 Y 1 A LEU 116  ? A LEU 116  
117  1 Y 1 A ALA 117  ? A ALA 117  
118  1 Y 1 A PHE 118  ? A PHE 118  
119  1 Y 1 A ILE 119  ? A ILE 119  
120  1 Y 1 A LYS 120  ? A LYS 120  
121  1 Y 1 A ARG 121  ? A ARG 121  
122  1 Y 1 A THR 122  ? A THR 122  
123  1 Y 1 A PRO 123  ? A PRO 123  
124  1 Y 1 A VAL 124  ? A VAL 124  
125  1 Y 1 A ILE 125  ? A ILE 125  
126  1 Y 1 A ASP 126  ? A ASP 126  
127  1 Y 1 A ALA 127  ? A ALA 127  
128  1 Y 1 A ASP 128  ? A ASP 128  
129  1 Y 1 A LYS 129  ? A LYS 129  
130  1 Y 1 A PRO 130  ? A PRO 130  
131  1 Y 1 A VAL 131  ? A VAL 131  
132  1 Y 1 A SER 132  ? A SER 132  
133  1 Y 1 A SER 133  ? A SER 133  
134  1 Y 1 A GLN 134  ? A GLN 134  
135  1 Y 1 A LEU 135  ? A LEU 135  
136  1 Y 1 A ARG 136  ? A ARG 136  
137  1 Y 1 A VAL 137  ? A VAL 137  
138  1 Y 1 A LEU 138  ? A LEU 138  
139  1 Y 1 A THR 139  ? A THR 139  
140  1 Y 1 A LEU 140  ? A LEU 140  
141  1 Y 1 A SER 141  ? A SER 141  
142  1 Y 1 A GLU 142  ? A GLU 142  
143  1 Y 1 A ASP 143  ? A ASP 143  
144  1 Y 1 A SER 144  ? A SER 144  
145  1 Y 1 A PRO 145  ? A PRO 145  
146  1 Y 1 A TYR 146  ? A TYR 146  
147  1 Y 1 A GLU 147  ? A GLU 147  
148  1 Y 1 A THR 148  ? A THR 148  
149  1 Y 1 A LEU 149  ? A LEU 149  
150  1 Y 1 A HIS 150  ? A HIS 150  
151  1 Y 1 A SER 151  ? A SER 151  
152  1 Y 1 A PHE 152  ? A PHE 152  
153  1 Y 1 A ILE 153  ? A ILE 153  
154  1 Y 1 A SER 154  ? A SER 154  
155  1 Y 1 A ASN 155  ? A ASN 155  
156  1 Y 1 A ALA 156  ? A ALA 156  
157  1 Y 1 A VAL 157  ? A VAL 157  
158  1 Y 1 A ALA 158  ? A ALA 158  
159  1 Y 1 A PRO 159  ? A PRO 159  
160  1 Y 1 A PHE 160  ? A PHE 160  
161  1 Y 1 A PHE 161  ? A PHE 161  
162  1 Y 1 A LYS 162  ? A LYS 162  
163  1 Y 1 A SER 163  ? A SER 163  
164  1 Y 1 A TYR 164  ? A TYR 164  
165  1 Y 1 A ILE 165  ? A ILE 165  
166  1 Y 1 A ARG 166  ? A ARG 166  
167  1 Y 1 A GLU 167  ? A GLU 167  
168  1 Y 1 A SER 168  ? A SER 168  
169  1 Y 1 A GLY 169  ? A GLY 169  
170  1 Y 1 A LYS 170  ? A LYS 170  
171  1 Y 1 A ALA 171  ? A ALA 171  
172  1 Y 1 A ASP 172  ? A ASP 172  
173  1 Y 1 A ARG 173  ? A ARG 173  
174  1 Y 1 A ASP 174  ? A ASP 174  
175  1 Y 1 A GLY 175  ? A GLY 175  
176  1 Y 1 A ASP 176  ? A ASP 176  
177  1 Y 1 A LYS 177  ? A LYS 177  
178  1 Y 1 A MET 178  ? A MET 178  
179  1 Y 1 A ALA 179  ? A ALA 179  
180  1 Y 1 A PRO 180  ? A PRO 180  
181  1 Y 1 A SER 181  ? A SER 181  
182  1 Y 1 A VAL 182  ? A VAL 182  
183  1 Y 1 A GLU 183  ? A GLU 183  
184  1 Y 1 A LYS 184  ? A LYS 184  
185  1 Y 1 A LYS 185  ? A LYS 185  
186  1 Y 1 A ILE 186  ? A ILE 186  
187  1 Y 1 A ALA 187  ? A ALA 187  
188  1 Y 1 A GLU 188  ? A GLU 188  
189  1 Y 1 A LEU 189  ? A LEU 189  
190  1 Y 1 A GLU 190  ? A GLU 190  
191  1 Y 1 A MET 191  ? A MET 191  
192  1 Y 1 A GLY 192  ? A GLY 192  
193  1 Y 1 A LEU 193  ? A LEU 193  
194  1 Y 1 A LEU 194  ? A LEU 194  
195  1 Y 1 A HIS 195  ? A HIS 195  
196  1 Y 1 A LEU 196  ? A LEU 196  
197  1 Y 1 A GLN 197  ? A GLN 197  
198  1 Y 1 A GLN 198  ? A GLN 198  
199  1 Y 1 A ASN 199  ? A ASN 199  
200  1 Y 1 A ILE 200  ? A ILE 200  
201  1 Y 1 A GLU 201  ? A GLU 201  
202  1 Y 1 A ILE 202  ? A ILE 202  
203  1 Y 1 A PRO 203  ? A PRO 203  
204  1 Y 1 A GLU 204  ? A GLU 204  
205  1 Y 1 A ILE 205  ? A ILE 205  
206  1 Y 1 A SER 206  ? A SER 206  
207  1 Y 1 A LEU 207  ? A LEU 207  
208  1 Y 1 A PRO 208  ? A PRO 208  
209  1 Y 1 A ILE 209  ? A ILE 209  
210  1 Y 1 A HIS 210  ? A HIS 210  
211  1 Y 1 A PRO 211  ? A PRO 211  
212  1 Y 1 A MET 212  ? A MET 212  
213  1 Y 1 A ILE 213  ? A ILE 213  
214  1 Y 1 A THR 214  ? A THR 214  
215  1 Y 1 A ASN 215  ? A ASN 215  
216  1 Y 1 A VAL 216  ? A VAL 216  
217  1 Y 1 A ALA 217  ? A ALA 217  
218  1 Y 1 A LYS 218  ? A LYS 218  
219  1 Y 1 A GLN 219  ? A GLN 219  
220  1 Y 1 A CYS 220  ? A CYS 220  
221  1 Y 1 A TYR 221  ? A TYR 221  
222  1 Y 1 A GLU 222  ? A GLU 222  
223  1 Y 1 A ARG 223  ? A ARG 223  
224  1 Y 1 A GLY 224  ? A GLY 224  
225  1 Y 1 A GLU 225  ? A GLU 225  
226  1 Y 1 A LYS 226  ? A LYS 226  
227  1 Y 1 A PRO 227  ? A PRO 227  
228  1 Y 1 A LYS 228  ? A LYS 228  
229  1 Y 1 A VAL 229  ? A VAL 229  
230  1 Y 1 A THR 230  ? A THR 230  
231  1 Y 1 A ASP 231  ? A ASP 231  
232  1 Y 1 A PHE 232  ? A PHE 232  
233  1 Y 1 A GLY 233  ? A GLY 233  
234  1 Y 1 A ASP 234  ? A ASP 234  
235  1 Y 1 A LYS 235  ? A LYS 235  
236  1 Y 1 A VAL 236  ? A VAL 236  
237  1 Y 1 A GLU 237  ? A GLU 237  
238  1 Y 1 A ASP 238  ? A ASP 238  
239  1 Y 1 A PRO 239  ? A PRO 239  
240  1 Y 1 A THR 240  ? A THR 240  
241  1 Y 1 A PHE 241  ? A PHE 241  
242  1 Y 1 A LEU 242  ? A LEU 242  
243  1 Y 1 A ASN 243  ? A ASN 243  
244  1 Y 1 A GLN 244  ? A GLN 244  
245  1 Y 1 A LEU 245  ? A LEU 245  
246  1 Y 1 A GLN 246  ? A GLN 246  
247  1 Y 1 A SER 247  ? A SER 247  
248  1 Y 1 A GLY 248  ? A GLY 248  
249  1 Y 1 A VAL 249  ? A VAL 249  
250  1 Y 1 A ASN 250  ? A ASN 250  
251  1 Y 1 A ARG 251  ? A ARG 251  
252  1 Y 1 A TRP 252  ? A TRP 252  
253  1 Y 1 A ILE 253  ? A ILE 253  
254  1 Y 1 A ARG 254  ? A ARG 254  
255  1 Y 1 A GLU 255  ? A GLU 255  
256  1 Y 1 A ILE 256  ? A ILE 256  
257  1 Y 1 A GLN 257  ? A GLN 257  
258  1 Y 1 A LYS 258  ? A LYS 258  
259  1 Y 1 A VAL 259  ? A VAL 259  
260  1 Y 1 A THR 260  ? A THR 260  
261  1 Y 1 A LYS 261  ? A LYS 261  
262  1 Y 1 A LEU 262  ? A LEU 262  
263  1 Y 1 A ASP 263  ? A ASP 263  
264  1 Y 1 A ARG 264  ? A ARG 264  
265  1 Y 1 A ASP 265  ? A ASP 265  
266  1 Y 1 A PRO 266  ? A PRO 266  
267  1 Y 1 A ALA 267  ? A ALA 267  
268  1 Y 1 A SER 268  ? A SER 268  
269  1 Y 1 A GLY 269  ? A GLY 269  
270  1 Y 1 A THR 270  ? A THR 270  
271  1 Y 1 A ALA 271  ? A ALA 271  
272  1 Y 1 A LEU 272  ? A LEU 272  
273  1 Y 1 A GLN 273  ? A GLN 273  
274  1 Y 1 A GLU 274  ? A GLU 274  
275  1 Y 1 A ILE 275  ? A ILE 275  
276  1 Y 1 A SER 276  ? A SER 276  
277  1 Y 1 A PHE 277  ? A PHE 277  
278  1 Y 1 A TRP 278  ? A TRP 278  
279  1 Y 1 A LEU 279  ? A LEU 279  
280  1 Y 1 A ASN 280  ? A ASN 280  
281  1 Y 1 A LEU 281  ? A LEU 281  
282  1 Y 1 A GLU 282  ? A GLU 282  
283  1 Y 1 A ARG 283  ? A ARG 283  
284  1 Y 1 A ALA 284  ? A ALA 284  
285  1 Y 1 A LEU 285  ? A LEU 285  
286  1 Y 1 A TYR 286  ? A TYR 286  
287  1 Y 1 A ARG 287  ? A ARG 287  
288  1 Y 1 A ILE 288  ? A ILE 288  
289  1 Y 1 A GLN 289  ? A GLN 289  
290  1 Y 1 A GLU 290  ? A GLU 290  
291  1 Y 1 A LYS 291  ? A LYS 291  
292  1 Y 1 A ARG 292  ? A ARG 292  
293  1 Y 1 A GLU 293  ? A GLU 293  
294  1 Y 1 A SER 294  ? A SER 294  
295  1 Y 1 A PRO 295  ? A PRO 295  
296  1 Y 1 A GLU 296  ? A GLU 296  
297  1 Y 1 A VAL 297  ? A VAL 297  
298  1 Y 1 A LEU 298  ? A LEU 298  
299  1 Y 1 A LEU 299  ? A LEU 299  
300  1 Y 1 A THR 300  ? A THR 300  
301  1 Y 1 A LEU 301  ? A LEU 301  
302  1 Y 1 A ASP 302  ? A ASP 302  
303  1 Y 1 A ILE 303  ? A ILE 303  
304  1 Y 1 A LEU 304  ? A LEU 304  
305  1 Y 1 A LYS 305  ? A LYS 305  
306  1 Y 1 A HIS 306  ? A HIS 306  
307  1 Y 1 A GLY 307  ? A GLY 307  
308  1 Y 1 A LYS 308  ? A LYS 308  
309  1 Y 1 A ARG 309  ? A ARG 309  
310  1 Y 1 A PHE 310  ? A PHE 310  
311  1 Y 1 A HIS 311  ? A HIS 311  
312  1 Y 1 A ALA 312  ? A ALA 312  
313  1 Y 1 A THR 313  ? A THR 313  
314  1 Y 1 A VAL 314  ? A VAL 314  
315  1 Y 1 A SER 315  ? A SER 315  
316  1 Y 1 A PHE 316  ? A PHE 316  
317  1 Y 1 A ASP 317  ? A ASP 317  
318  1 Y 1 A THR 318  ? A THR 318  
319  1 Y 1 A ASP 319  ? A ASP 319  
320  1 Y 1 A THR 320  ? A THR 320  
321  1 Y 1 A GLY 321  ? A GLY 321  
322  1 Y 1 A LEU 322  ? A LEU 322  
323  1 Y 1 A LYS 323  ? A LYS 323  
324  1 Y 1 A GLN 324  ? A GLN 324  
325  1 Y 1 A ALA 325  ? A ALA 325  
326  1 Y 1 A LEU 326  ? A LEU 326  
327  1 Y 1 A GLU 327  ? A GLU 327  
328  1 Y 1 A THR 328  ? A THR 328  
329  1 Y 1 A VAL 329  ? A VAL 329  
330  1 Y 1 A ASN 330  ? A ASN 330  
331  1 Y 1 A ASP 331  ? A ASP 331  
332  1 Y 1 A TYR 332  ? A TYR 332  
333  1 Y 1 A ASN 333  ? A ASN 333  
334  1 Y 1 A PRO 334  ? A PRO 334  
335  1 Y 1 A LEU 335  ? A LEU 335  
336  1 Y 1 A MET 336  ? A MET 336  
337  1 Y 1 A LYS 337  ? A LYS 337  
338  1 Y 1 A ASP 338  ? A ASP 338  
339  1 Y 1 A PHE 339  ? A PHE 339  
340  1 Y 1 A PRO 340  ? A PRO 340  
341  1 Y 1 A LEU 341  ? A LEU 341  
342  1 Y 1 A ASN 342  ? A ASN 342  
343  1 Y 1 A ASP 343  ? A ASP 343  
344  1 Y 1 A LEU 344  ? A LEU 344  
345  1 Y 1 A LEU 345  ? A LEU 345  
346  1 Y 1 A SER 346  ? A SER 346  
347  1 Y 1 A ALA 347  ? A ALA 347  
348  1 Y 1 A THR 348  ? A THR 348  
349  1 Y 1 A GLU 349  ? A GLU 349  
350  1 Y 1 A LEU 350  ? A LEU 350  
351  1 Y 1 A ASP 351  ? A ASP 351  
352  1 Y 1 A LYS 352  ? A LYS 352  
353  1 Y 1 A ILE 353  ? A ILE 353  
354  1 Y 1 A ARG 354  ? A ARG 354  
355  1 Y 1 A GLN 355  ? A GLN 355  
356  1 Y 1 A ALA 356  ? A ALA 356  
357  1 Y 1 A LEU 357  ? A LEU 357  
358  1 Y 1 A VAL 358  ? A VAL 358  
359  1 Y 1 A ALA 359  ? A ALA 359  
360  1 Y 1 A ILE 360  ? A ILE 360  
361  1 Y 1 A PHE 361  ? A PHE 361  
362  1 Y 1 A THR 362  ? A THR 362  
363  1 Y 1 A HIS 363  ? A HIS 363  
364  1 Y 1 A LEU 364  ? A LEU 364  
365  1 Y 1 A ARG 365  ? A ARG 365  
366  1 Y 1 A LYS 366  ? A LYS 366  
367  1 Y 1 A ILE 367  ? A ILE 367  
368  1 Y 1 A ARG 368  ? A ARG 368  
369  1 Y 1 A ASN 369  ? A ASN 369  
370  1 Y 1 A THR 370  ? A THR 370  
371  1 Y 1 A LYS 371  ? A LYS 371  
372  1 Y 1 A TYR 372  ? A TYR 372  
373  1 Y 1 A PRO 373  ? A PRO 373  
374  1 Y 1 A ILE 374  ? A ILE 374  
375  1 Y 1 A GLN 375  ? A GLN 375  
376  1 Y 1 A ARG 376  ? A ARG 376  
377  1 Y 1 A ALA 377  ? A ALA 377  
378  1 Y 1 A LEU 378  ? A LEU 378  
379  1 Y 1 A ARG 379  ? A ARG 379  
380  1 Y 1 A LEU 380  ? A LEU 380  
381  1 Y 1 A VAL 381  ? A VAL 381  
382  1 Y 1 A GLU 382  ? A GLU 382  
383  1 Y 1 A ALA 383  ? A ALA 383  
384  1 Y 1 A ILE 384  ? A ILE 384  
385  1 Y 1 A SER 385  ? A SER 385  
386  1 Y 1 A ARG 386  ? A ARG 386  
387  1 Y 1 A ASP 387  ? A ASP 387  
388  1 Y 1 A LEU 388  ? A LEU 388  
389  1 Y 1 A SER 389  ? A SER 389  
390  1 Y 1 A SER 390  ? A SER 390  
391  1 Y 1 A GLN 391  ? A GLN 391  
392  1 Y 1 A LEU 392  ? A LEU 392  
393  1 Y 1 A LEU 393  ? A LEU 393  
394  1 Y 1 A LYS 394  ? A LYS 394  
395  1 Y 1 A VAL 395  ? A VAL 395  
396  1 Y 1 A LEU 396  ? A LEU 396  
397  1 Y 1 A GLY 397  ? A GLY 397  
398  1 Y 1 A THR 398  ? A THR 398  
399  1 Y 1 A ARG 399  ? A ARG 399  
400  1 Y 1 A LYS 400  ? A LYS 400  
401  1 Y 1 A LEU 401  ? A LEU 401  
402  1 Y 1 A MET 402  ? A MET 402  
403  1 Y 1 A HIS 403  ? A HIS 403  
404  1 Y 1 A VAL 404  ? A VAL 404  
405  1 Y 1 A ALA 405  ? A ALA 405  
406  1 Y 1 A TYR 406  ? A TYR 406  
407  1 Y 1 A GLU 407  ? A GLU 407  
408  1 Y 1 A GLU 408  ? A GLU 408  
409  1 Y 1 A PHE 409  ? A PHE 409  
410  1 Y 1 A GLU 410  ? A GLU 410  
411  1 Y 1 A LYS 411  ? A LYS 411  
412  1 Y 1 A VAL 412  ? A VAL 412  
413  1 Y 1 A MET 413  ? A MET 413  
414  1 Y 1 A VAL 414  ? A VAL 414  
415  1 Y 1 A ALA 415  ? A ALA 415  
416  1 Y 1 A CYS 416  ? A CYS 416  
417  1 Y 1 A PHE 417  ? A PHE 417  
418  1 Y 1 A GLU 418  ? A GLU 418  
419  1 Y 1 A VAL 419  ? A VAL 419  
420  1 Y 1 A PHE 420  ? A PHE 420  
421  1 Y 1 A GLN 421  ? A GLN 421  
422  1 Y 1 A THR 422  ? A THR 422  
423  1 Y 1 A TRP 423  ? A TRP 423  
424  1 Y 1 A ASP 424  ? A ASP 424  
425  1 Y 1 A ASP 425  ? A ASP 425  
426  1 Y 1 A GLU 426  ? A GLU 426  
427  1 Y 1 A TYR 427  ? A TYR 427  
428  1 Y 1 A GLU 428  ? A GLU 428  
429  1 Y 1 A LYS 429  ? A LYS 429  
430  1 Y 1 A LEU 430  ? A LEU 430  
431  1 Y 1 A GLN 431  ? A GLN 431  
432  1 Y 1 A VAL 432  ? A VAL 432  
433  1 Y 1 A LEU 433  ? A LEU 433  
434  1 Y 1 A LEU 434  ? A LEU 434  
435  1 Y 1 A ARG 435  ? A ARG 435  
436  1 Y 1 A ASP 436  ? A ASP 436  
437  1 Y 1 A ILE 437  ? A ILE 437  
438  1 Y 1 A VAL 438  ? A VAL 438  
439  1 Y 1 A LYS 439  ? A LYS 439  
440  1 Y 1 A ARG 440  ? A ARG 440  
441  1 Y 1 A LYS 441  ? A LYS 441  
442  1 Y 1 A ARG 442  ? A ARG 442  
443  1 Y 1 A GLU 443  ? A GLU 443  
444  1 Y 1 A GLU 444  ? A GLU 444  
445  1 Y 1 A ASN 445  ? A ASN 445  
446  1 Y 1 A LEU 446  ? A LEU 446  
447  1 Y 1 A LYS 447  ? A LYS 447  
448  1 Y 1 A MET 448  ? A MET 448  
449  1 Y 1 A VAL 449  ? A VAL 449  
450  1 Y 1 A TRP 450  ? A TRP 450  
451  1 Y 1 A ARG 451  ? A ARG 451  
452  1 Y 1 A ILE 452  ? A ILE 452  
453  1 Y 1 A ASN 453  ? A ASN 453  
454  1 Y 1 A PRO 454  ? A PRO 454  
455  1 Y 1 A ALA 455  ? A ALA 455  
456  1 Y 1 A HIS 456  ? A HIS 456  
457  1 Y 1 A ARG 457  ? A ARG 457  
458  1 Y 1 A LYS 458  ? A LYS 458  
459  1 Y 1 A LEU 459  ? A LEU 459  
460  1 Y 1 A GLN 460  ? A GLN 460  
461  1 Y 1 A ALA 461  ? A ALA 461  
462  1 Y 1 A ARG 462  ? A ARG 462  
463  1 Y 1 A LEU 463  ? A LEU 463  
464  1 Y 1 A ASP 464  ? A ASP 464  
465  1 Y 1 A GLN 465  ? A GLN 465  
466  1 Y 1 A MET 466  ? A MET 466  
467  1 Y 1 A ARG 467  ? A ARG 467  
468  1 Y 1 A LYS 468  ? A LYS 468  
469  1 Y 1 A PHE 469  ? A PHE 469  
470  1 Y 1 A ARG 470  ? A ARG 470  
471  1 Y 1 A ARG 471  ? A ARG 471  
472  1 Y 1 A GLN 472  ? A GLN 472  
473  1 Y 1 A HIS 473  ? A HIS 473  
474  1 Y 1 A GLU 474  ? A GLU 474  
475  1 Y 1 A GLN 475  ? A GLN 475  
476  1 Y 1 A LEU 476  ? A LEU 476  
477  1 Y 1 A ARG 477  ? A ARG 477  
478  1 Y 1 A ALA 478  ? A ALA 478  
479  1 Y 1 A VAL 479  ? A VAL 479  
480  1 Y 1 A ILE 480  ? A ILE 480  
481  1 Y 1 A VAL 481  ? A VAL 481  
482  1 Y 1 A ARG 482  ? A ARG 482  
483  1 Y 1 A VAL 483  ? A VAL 483  
484  1 Y 1 A LEU 484  ? A LEU 484  
485  1 Y 1 A ARG 485  ? A ARG 485  
486  1 Y 1 A PRO 486  ? A PRO 486  
487  1 Y 1 A GLN 487  ? A GLN 487  
488  1 Y 1 A VAL 488  ? A VAL 488  
489  1 Y 1 A THR 489  ? A THR 489  
490  1 Y 1 A ALA 490  ? A ALA 490  
491  1 Y 1 A VAL 491  ? A VAL 491  
492  1 Y 1 A ALA 492  ? A ALA 492  
493  1 Y 1 A GLN 493  ? A GLN 493  
494  1 Y 1 A GLN 494  ? A GLN 494  
495  1 Y 1 A ASN 495  ? A ASN 495  
496  1 Y 1 A GLN 496  ? A GLN 496  
497  1 Y 1 A GLY 497  ? A GLY 497  
498  1 Y 1 A GLU 498  ? A GLU 498  
499  1 Y 1 A VAL 499  ? A VAL 499  
500  1 Y 1 A PRO 500  ? A PRO 500  
501  1 Y 1 A GLU 501  ? A GLU 501  
502  1 Y 1 A PRO 502  ? A PRO 502  
503  1 Y 1 A GLN 503  ? A GLN 503  
504  1 Y 1 A ASP 504  ? A ASP 504  
505  1 Y 1 A MET 505  ? A MET 505  
506  1 Y 1 A LYS 506  ? A LYS 506  
507  1 Y 1 A VAL 507  ? A VAL 507  
508  1 Y 1 A ALA 508  ? A ALA 508  
509  1 Y 1 A GLU 509  ? A GLU 509  
510  1 Y 1 A VAL 510  ? A VAL 510  
511  1 Y 1 A LEU 511  ? A LEU 511  
512  1 Y 1 A PHE 512  ? A PHE 512  
513  1 Y 1 A ASP 513  ? A ASP 513  
514  1 Y 1 A ALA 514  ? A ALA 514  
515  1 Y 1 A ALA 515  ? A ALA 515  
516  1 Y 1 A ASP 516  ? A ASP 516  
517  1 Y 1 A ALA 517  ? A ALA 517  
518  1 Y 1 A ASN 518  ? A ASN 518  
519  1 Y 1 A ALA 519  ? A ALA 519  
520  1 Y 1 A ILE 520  ? A ILE 520  
521  1 Y 1 A GLU 521  ? A GLU 521  
522  1 Y 1 A GLU 522  ? A GLU 522  
523  1 Y 1 A VAL 523  ? A VAL 523  
524  1 Y 1 A ASN 524  ? A ASN 524  
525  1 Y 1 A LEU 525  ? A LEU 525  
526  1 Y 1 A ALA 526  ? A ALA 526  
527  1 Y 1 A TYR 527  ? A TYR 527  
528  1 Y 1 A GLU 528  ? A GLU 528  
529  1 Y 1 A ASN 529  ? A ASN 529  
530  1 Y 1 A VAL 530  ? A VAL 530  
531  1 Y 1 A LYS 531  ? A LYS 531  
532  1 Y 1 A GLU 532  ? A GLU 532  
533  1 Y 1 A VAL 533  ? A VAL 533  
534  1 Y 1 A ASP 534  ? A ASP 534  
535  1 Y 1 A GLY 535  ? A GLY 535  
536  1 Y 1 A LEU 536  ? A LEU 536  
537  1 Y 1 A ASP 537  ? A ASP 537  
538  1 Y 1 A VAL 538  ? A VAL 538  
539  1 Y 1 A SER 539  ? A SER 539  
540  1 Y 1 A LYS 540  ? A LYS 540  
541  1 Y 1 A GLU 541  ? A GLU 541  
542  1 Y 1 A GLY 542  ? A GLY 542  
543  1 Y 1 A THR 543  ? A THR 543  
544  1 Y 1 A GLU 544  ? A GLU 544  
545  1 Y 1 A ALA 545  ? A ALA 545  
546  1 Y 1 A TRP 546  ? A TRP 546  
547  1 Y 1 A GLU 547  ? A GLU 547  
548  1 Y 1 A ALA 548  ? A ALA 548  
549  1 Y 1 A ALA 549  ? A ALA 549  
550  1 Y 1 A MET 550  ? A MET 550  
551  1 Y 1 A LYS 551  ? A LYS 551  
552  1 Y 1 A ARG 552  ? A ARG 552  
553  1 Y 1 A TYR 553  ? A TYR 553  
554  1 Y 1 A ASP 554  ? A ASP 554  
555  1 Y 1 A GLU 555  ? A GLU 555  
556  1 Y 1 A ARG 556  ? A ARG 556  
557  1 Y 1 A ILE 557  ? A ILE 557  
558  1 Y 1 A ASP 558  ? A ASP 558  
559  1 Y 1 A ARG 559  ? A ARG 559  
560  1 Y 1 A VAL 560  ? A VAL 560  
561  1 Y 1 A GLU 561  ? A GLU 561  
562  1 Y 1 A THR 562  ? A THR 562  
563  1 Y 1 A ARG 563  ? A ARG 563  
564  1 Y 1 A ILE 564  ? A ILE 564  
565  1 Y 1 A THR 565  ? A THR 565  
566  1 Y 1 A ALA 566  ? A ALA 566  
567  1 Y 1 A ARG 567  ? A ARG 567  
568  1 Y 1 A LEU 568  ? A LEU 568  
569  1 Y 1 A ARG 569  ? A ARG 569  
570  1 Y 1 A ASP 570  ? A ASP 570  
571  1 Y 1 A GLN 571  ? A GLN 571  
572  1 Y 1 A LEU 572  ? A LEU 572  
573  1 Y 1 A GLY 573  ? A GLY 573  
574  1 Y 1 A THR 574  ? A THR 574  
575  1 Y 1 A ALA 575  ? A ALA 575  
576  1 Y 1 A LYS 576  ? A LYS 576  
577  1 Y 1 A ASN 577  ? A ASN 577  
578  1 Y 1 A ALA 578  ? A ALA 578  
579  1 Y 1 A ASN 579  ? A ASN 579  
580  1 Y 1 A GLU 580  ? A GLU 580  
581  1 Y 1 A MET 581  ? A MET 581  
582  1 Y 1 A PHE 582  ? A PHE 582  
583  1 Y 1 A ARG 583  ? A ARG 583  
584  1 Y 1 A ILE 584  ? A ILE 584  
585  1 Y 1 A PHE 585  ? A PHE 585  
586  1 Y 1 A SER 586  ? A SER 586  
587  1 Y 1 A ARG 587  ? A ARG 587  
588  1 Y 1 A PHE 588  ? A PHE 588  
589  1 Y 1 A ASN 589  ? A ASN 589  
590  1 Y 1 A ALA 590  ? A ALA 590  
591  1 Y 1 A LEU 591  ? A LEU 591  
592  1 Y 1 A PHE 592  ? A PHE 592  
593  1 Y 1 A VAL 593  ? A VAL 593  
594  1 Y 1 A ARG 594  ? A ARG 594  
595  1 Y 1 A PRO 595  ? A PRO 595  
596  1 Y 1 A HIS 596  ? A HIS 596  
597  1 Y 1 A ILE 597  ? A ILE 597  
598  1 Y 1 A ARG 598  ? A ARG 598  
599  1 Y 1 A GLY 599  ? A GLY 599  
600  1 Y 1 A ALA 600  ? A ALA 600  
601  1 Y 1 A ILE 601  ? A ILE 601  
602  1 Y 1 A ARG 602  ? A ARG 602  
603  1 Y 1 A GLU 603  ? A GLU 603  
604  1 Y 1 A TYR 604  ? A TYR 604  
605  1 Y 1 A GLN 605  ? A GLN 605  
606  1 Y 1 A THR 606  ? A THR 606  
607  1 Y 1 A GLN 607  ? A GLN 607  
608  1 Y 1 A LEU 608  ? A LEU 608  
609  1 Y 1 A ILE 609  ? A ILE 609  
610  1 Y 1 A GLN 610  ? A GLN 610  
611  1 Y 1 A ARG 611  ? A ARG 611  
612  1 Y 1 A VAL 612  ? A VAL 612  
613  1 Y 1 A LYS 613  ? A LYS 613  
614  1 Y 1 A ASP 614  ? A ASP 614  
615  1 Y 1 A ASP 615  ? A ASP 615  
616  1 Y 1 A ILE 616  ? A ILE 616  
617  1 Y 1 A GLU 617  ? A GLU 617  
618  1 Y 1 A SER 618  ? A SER 618  
619  1 Y 1 A LEU 619  ? A LEU 619  
620  1 Y 1 A HIS 620  ? A HIS 620  
621  1 Y 1 A ASP 621  ? A ASP 621  
622  1 Y 1 A LYS 622  ? A LYS 622  
623  1 Y 1 A PHE 623  ? A PHE 623  
624  1 Y 1 A LYS 624  ? A LYS 624  
625  1 Y 1 A VAL 625  ? A VAL 625  
626  1 Y 1 A GLN 626  ? A GLN 626  
627  1 Y 1 A TYR 627  ? A TYR 627  
628  1 Y 1 A PRO 628  ? A PRO 628  
629  1 Y 1 A GLN 629  ? A GLN 629  
630  1 Y 1 A SER 630  ? A SER 630  
631  1 Y 1 A GLN 631  ? A GLN 631  
632  1 Y 1 A ALA 632  ? A ALA 632  
633  1 Y 1 A CYS 633  ? A CYS 633  
634  1 Y 1 A LYS 634  ? A LYS 634  
635  1 Y 1 A MET 635  ? A MET 635  
636  1 Y 1 A SER 636  ? A SER 636  
637  1 Y 1 A HIS 637  ? A HIS 637  
638  1 Y 1 A VAL 638  ? A VAL 638  
639  1 Y 1 A ARG 639  ? A ARG 639  
640  1 Y 1 A ASP 640  ? A ASP 640  
641  1 Y 1 A LEU 641  ? A LEU 641  
642  1 Y 1 A PRO 642  ? A PRO 642  
643  1 Y 1 A PRO 643  ? A PRO 643  
644  1 Y 1 A VAL 644  ? A VAL 644  
645  1 Y 1 A SER 645  ? A SER 645  
646  1 Y 1 A GLY 646  ? A GLY 646  
647  1 Y 1 A SER 647  ? A SER 647  
648  1 Y 1 A ILE 648  ? A ILE 648  
649  1 Y 1 A ILE 649  ? A ILE 649  
650  1 Y 1 A TRP 650  ? A TRP 650  
651  1 Y 1 A ALA 651  ? A ALA 651  
652  1 Y 1 A LYS 652  ? A LYS 652  
653  1 Y 1 A GLN 653  ? A GLN 653  
654  1 Y 1 A ILE 654  ? A ILE 654  
655  1 Y 1 A ASP 655  ? A ASP 655  
656  1 Y 1 A ARG 656  ? A ARG 656  
657  1 Y 1 A GLN 657  ? A GLN 657  
658  1 Y 1 A LEU 658  ? A LEU 658  
659  1 Y 1 A THR 659  ? A THR 659  
660  1 Y 1 A ALA 660  ? A ALA 660  
661  1 Y 1 A TYR 661  ? A TYR 661  
662  1 Y 1 A MET 662  ? A MET 662  
663  1 Y 1 A LYS 663  ? A LYS 663  
664  1 Y 1 A ARG 664  ? A ARG 664  
665  1 Y 1 A VAL 665  ? A VAL 665  
666  1 Y 1 A GLU 666  ? A GLU 666  
667  1 Y 1 A ASP 667  ? A ASP 667  
668  1 Y 1 A VAL 668  ? A VAL 668  
669  1 Y 1 A LEU 669  ? A LEU 669  
670  1 Y 1 A GLY 670  ? A GLY 670  
671  1 Y 1 A LYS 671  ? A LYS 671  
672  1 Y 1 A GLY 672  ? A GLY 672  
673  1 Y 1 A TRP 673  ? A TRP 673  
674  1 Y 1 A GLU 674  ? A GLU 674  
675  1 Y 1 A ASN 675  ? A ASN 675  
676  1 Y 1 A HIS 676  ? A HIS 676  
677  1 Y 1 A VAL 677  ? A VAL 677  
678  1 Y 1 A GLU 678  ? A GLU 678  
679  1 Y 1 A GLY 679  ? A GLY 679  
680  1 Y 1 A GLN 680  ? A GLN 680  
681  1 Y 1 A LYS 681  ? A LYS 681  
682  1 Y 1 A LEU 682  ? A LEU 682  
683  1 Y 1 A LYS 683  ? A LYS 683  
684  1 Y 1 A GLN 684  ? A GLN 684  
685  1 Y 1 A ASP 685  ? A ASP 685  
686  1 Y 1 A GLY 686  ? A GLY 686  
687  1 Y 1 A ASP 687  ? A ASP 687  
688  1 Y 1 A SER 688  ? A SER 688  
689  1 Y 1 A PHE 689  ? A PHE 689  
690  1 Y 1 A ARG 690  ? A ARG 690  
691  1 Y 1 A MET 691  ? A MET 691  
692  1 Y 1 A LYS 692  ? A LYS 692  
693  1 Y 1 A LEU 693  ? A LEU 693  
694  1 Y 1 A ASN 694  ? A ASN 694  
695  1 Y 1 A THR 695  ? A THR 695  
696  1 Y 1 A GLN 696  ? A GLN 696  
697  1 Y 1 A GLU 697  ? A GLU 697  
698  1 Y 1 A ILE 698  ? A ILE 698  
699  1 Y 1 A PHE 699  ? A PHE 699  
700  1 Y 1 A ASP 700  ? A ASP 700  
701  1 Y 1 A ASP 701  ? A ASP 701  
702  1 Y 1 A TRP 702  ? A TRP 702  
703  1 Y 1 A ALA 703  ? A ALA 703  
704  1 Y 1 A ARG 704  ? A ARG 704  
705  1 Y 1 A LYS 705  ? A LYS 705  
706  1 Y 1 A VAL 706  ? A VAL 706  
707  1 Y 1 A GLN 707  ? A GLN 707  
708  1 Y 1 A GLN 708  ? A GLN 708  
709  1 Y 1 A ARG 709  ? A ARG 709  
710  1 Y 1 A ASN 710  ? A ASN 710  
711  1 Y 1 A LEU 711  ? A LEU 711  
712  1 Y 1 A GLY 712  ? A GLY 712  
713  1 Y 1 A VAL 713  ? A VAL 713  
714  1 Y 1 A SER 714  ? A SER 714  
715  1 Y 1 A GLY 715  ? A GLY 715  
716  1 Y 1 A ARG 716  ? A ARG 716  
717  1 Y 1 A ILE 717  ? A ILE 717  
718  1 Y 1 A PHE 718  ? A PHE 718  
719  1 Y 1 A THR 719  ? A THR 719  
720  1 Y 1 A ILE 720  ? A ILE 720  
721  1 Y 1 A GLU 721  ? A GLU 721  
722  1 Y 1 A SER 722  ? A SER 722  
723  1 Y 1 A THR 723  ? A THR 723  
724  1 Y 1 A ARG 724  ? A ARG 724  
725  1 Y 1 A VAL 725  ? A VAL 725  
726  1 Y 1 A ARG 726  ? A ARG 726  
727  1 Y 1 A GLY 727  ? A GLY 727  
728  1 Y 1 A ARG 728  ? A ARG 728  
729  1 Y 1 A THR 729  ? A THR 729  
730  1 Y 1 A GLY 730  ? A GLY 730  
731  1 Y 1 A ASN 731  ? A ASN 731  
732  1 Y 1 A VAL 732  ? A VAL 732  
733  1 Y 1 A LEU 733  ? A LEU 733  
734  1 Y 1 A LYS 734  ? A LYS 734  
735  1 Y 1 A LEU 735  ? A LEU 735  
736  1 Y 1 A LYS 736  ? A LYS 736  
737  1 Y 1 A VAL 737  ? A VAL 737  
738  1 Y 1 A ASN 738  ? A ASN 738  
739  1 Y 1 A PHE 739  ? A PHE 739  
740  1 Y 1 A LEU 740  ? A LEU 740  
741  1 Y 1 A PRO 741  ? A PRO 741  
742  1 Y 1 A GLU 742  ? A GLU 742  
743  1 Y 1 A ILE 743  ? A ILE 743  
744  1 Y 1 A ILE 744  ? A ILE 744  
745  1 Y 1 A THR 745  ? A THR 745  
746  1 Y 1 A LEU 746  ? A LEU 746  
747  1 Y 1 A SER 747  ? A SER 747  
748  1 Y 1 A LYS 748  ? A LYS 748  
749  1 Y 1 A GLU 749  ? A GLU 749  
750  1 Y 1 A VAL 750  ? A VAL 750  
751  1 Y 1 A ARG 751  ? A ARG 751  
752  1 Y 1 A ASN 752  ? A ASN 752  
753  1 Y 1 A LEU 753  ? A LEU 753  
754  1 Y 1 A LYS 754  ? A LYS 754  
755  1 Y 1 A TRP 755  ? A TRP 755  
756  1 Y 1 A LEU 756  ? A LEU 756  
757  1 Y 1 A GLY 757  ? A GLY 757  
758  1 Y 1 A PHE 758  ? A PHE 758  
759  1 Y 1 A ARG 759  ? A ARG 759  
760  1 Y 1 A VAL 760  ? A VAL 760  
761  1 Y 1 A PRO 761  ? A PRO 761  
762  1 Y 1 A LEU 762  ? A LEU 762  
763  1 Y 1 A ALA 763  ? A ALA 763  
764  1 Y 1 A ILE 764  ? A ILE 764  
765  1 Y 1 A VAL 765  ? A VAL 765  
766  1 Y 1 A ASN 766  ? A ASN 766  
767  1 Y 1 A LYS 767  ? A LYS 767  
768  1 Y 1 A ALA 768  ? A ALA 768  
769  1 Y 1 A HIS 769  ? A HIS 769  
770  1 Y 1 A GLN 770  ? A GLN 770  
771  1 Y 1 A ALA 771  ? A ALA 771  
772  1 Y 1 A ASN 772  ? A ASN 772  
773  1 Y 1 A GLN 773  ? A GLN 773  
774  1 Y 1 A LEU 774  ? A LEU 774  
775  1 Y 1 A TYR 775  ? A TYR 775  
776  1 Y 1 A PRO 776  ? A PRO 776  
777  1 Y 1 A PHE 777  ? A PHE 777  
778  1 Y 1 A ALA 778  ? A ALA 778  
779  1 Y 1 A ILE 779  ? A ILE 779  
780  1 Y 1 A SER 780  ? A SER 780  
781  1 Y 1 A LEU 781  ? A LEU 781  
782  1 Y 1 A ILE 782  ? A ILE 782  
783  1 Y 1 A GLU 783  ? A GLU 783  
784  1 Y 1 A SER 784  ? A SER 784  
785  1 Y 1 A VAL 785  ? A VAL 785  
786  1 Y 1 A ARG 786  ? A ARG 786  
787  1 Y 1 A THR 787  ? A THR 787  
788  1 Y 1 A TYR 788  ? A TYR 788  
789  1 Y 1 A GLU 789  ? A GLU 789  
790  1 Y 1 A ARG 790  ? A ARG 790  
791  1 Y 1 A THR 791  ? A THR 791  
792  1 Y 1 A CYS 792  ? A CYS 792  
793  1 Y 1 A GLU 793  ? A GLU 793  
794  1 Y 1 A LYS 794  ? A LYS 794  
795  1 Y 1 A VAL 795  ? A VAL 795  
796  1 Y 1 A GLU 796  ? A GLU 796  
797  1 Y 1 A GLU 797  ? A GLU 797  
798  1 Y 1 A ARG 798  ? A ARG 798  
799  1 Y 1 A ASN 799  ? A ASN 799  
800  1 Y 1 A THR 800  ? A THR 800  
801  1 Y 1 A ILE 801  ? A ILE 801  
802  1 Y 1 A SER 802  ? A SER 802  
803  1 Y 1 A LEU 803  ? A LEU 803  
804  1 Y 1 A LEU 804  ? A LEU 804  
805  1 Y 1 A VAL 805  ? A VAL 805  
806  1 Y 1 A ALA 806  ? A ALA 806  
807  1 Y 1 A GLY 807  ? A GLY 807  
808  1 Y 1 A LEU 808  ? A LEU 808  
809  1 Y 1 A LYS 809  ? A LYS 809  
810  1 Y 1 A LYS 810  ? A LYS 810  
811  1 Y 1 A GLU 811  ? A GLU 811  
812  1 Y 1 A VAL 812  ? A VAL 812  
813  1 Y 1 A GLN 813  ? A GLN 813  
814  1 Y 1 A ALA 814  ? A ALA 814  
815  1 Y 1 A LEU 815  ? A LEU 815  
816  1 Y 1 A ILE 816  ? A ILE 816  
817  1 Y 1 A ALA 817  ? A ALA 817  
818  1 Y 1 A GLU 818  ? A GLU 818  
819  1 Y 1 A GLY 819  ? A GLY 819  
820  1 Y 1 A ILE 820  ? A ILE 820  
821  1 Y 1 A ALA 821  ? A ALA 821  
822  1 Y 1 A LEU 822  ? A LEU 822  
823  1 Y 1 A VAL 823  ? A VAL 823  
824  1 Y 1 A TRP 824  ? A TRP 824  
825  1 Y 1 A GLU 825  ? A GLU 825  
826  1 Y 1 A SER 826  ? A SER 826  
827  1 Y 1 A TYR 827  ? A TYR 827  
828  1 Y 1 A LYS 828  ? A LYS 828  
829  1 Y 1 A LEU 829  ? A LEU 829  
830  1 Y 1 A ASP 830  ? A ASP 830  
831  1 Y 1 A PRO 831  ? A PRO 831  
832  1 Y 1 A TYR 832  ? A TYR 832  
833  1 Y 1 A VAL 833  ? A VAL 833  
834  1 Y 1 A GLN 834  ? A GLN 834  
835  1 Y 1 A ARG 835  ? A ARG 835  
836  1 Y 1 A LEU 836  ? A LEU 836  
837  1 Y 1 A ALA 837  ? A ALA 837  
838  1 Y 1 A GLU 838  ? A GLU 838  
839  1 Y 1 A THR 839  ? A THR 839  
840  1 Y 1 A VAL 840  ? A VAL 840  
841  1 Y 1 A PHE 841  ? A PHE 841  
842  1 Y 1 A ASN 842  ? A ASN 842  
843  1 Y 1 A PHE 843  ? A PHE 843  
844  1 Y 1 A GLN 844  ? A GLN 844  
845  1 Y 1 A GLU 845  ? A GLU 845  
846  1 Y 1 A LYS 846  ? A LYS 846  
847  1 Y 1 A VAL 847  ? A VAL 847  
848  1 Y 1 A ASP 848  ? A ASP 848  
849  1 Y 1 A ASP 849  ? A ASP 849  
850  1 Y 1 A LEU 850  ? A LEU 850  
851  1 Y 1 A LEU 851  ? A LEU 851  
852  1 Y 1 A ILE 852  ? A ILE 852  
853  1 Y 1 A ILE 853  ? A ILE 853  
854  1 Y 1 A GLU 854  ? A GLU 854  
855  1 Y 1 A GLU 855  ? A GLU 855  
856  1 Y 1 A LYS 856  ? A LYS 856  
857  1 Y 1 A ILE 857  ? A ILE 857  
858  1 Y 1 A ASP 858  ? A ASP 858  
859  1 Y 1 A LEU 859  ? A LEU 859  
860  1 Y 1 A GLU 860  ? A GLU 860  
861  1 Y 1 A VAL 861  ? A VAL 861  
862  1 Y 1 A ARG 862  ? A ARG 862  
863  1 Y 1 A SER 863  ? A SER 863  
864  1 Y 1 A LEU 864  ? A LEU 864  
865  1 Y 1 A GLU 865  ? A GLU 865  
866  1 Y 1 A THR 866  ? A THR 866  
867  1 Y 1 A CYS 867  ? A CYS 867  
868  1 Y 1 A MET 868  ? A MET 868  
869  1 Y 1 A TYR 869  ? A TYR 869  
870  1 Y 1 A ASP 870  ? A ASP 870  
871  1 Y 1 A HIS 871  ? A HIS 871  
872  1 Y 1 A LYS 872  ? A LYS 872  
873  1 Y 1 A THR 873  ? A THR 873  
874  1 Y 1 A PHE 874  ? A PHE 874  
875  1 Y 1 A SER 875  ? A SER 875  
876  1 Y 1 A GLU 876  ? A GLU 876  
877  1 Y 1 A ILE 877  ? A ILE 877  
878  1 Y 1 A LEU 878  ? A LEU 878  
879  1 Y 1 A ASN 879  ? A ASN 879  
880  1 Y 1 A ARG 880  ? A ARG 880  
881  1 Y 1 A VAL 881  ? A VAL 881  
882  1 Y 1 A GLN 882  ? A GLN 882  
883  1 Y 1 A LYS 883  ? A LYS 883  
884  1 Y 1 A ALA 884  ? A ALA 884  
885  1 Y 1 A VAL 885  ? A VAL 885  
886  1 Y 1 A ASP 886  ? A ASP 886  
887  1 Y 1 A ASP 887  ? A ASP 887  
888  1 Y 1 A LEU 888  ? A LEU 888  
889  1 Y 1 A ASN 889  ? A ASN 889  
890  1 Y 1 A LEU 890  ? A LEU 890  
891  1 Y 1 A HIS 891  ? A HIS 891  
892  1 Y 1 A SER 892  ? A SER 892  
893  1 Y 1 A TYR 893  ? A TYR 893  
894  1 Y 1 A SER 894  ? A SER 894  
895  1 Y 1 A ASN 895  ? A ASN 895  
896  1 Y 1 A LEU 896  ? A LEU 896  
897  1 Y 1 A PRO 897  ? A PRO 897  
898  1 Y 1 A ILE 898  ? A ILE 898  
899  1 Y 1 A TRP 899  ? A TRP 899  
900  1 Y 1 A VAL 900  ? A VAL 900  
901  1 Y 1 A ASN 901  ? A ASN 901  
902  1 Y 1 A LYS 902  ? A LYS 902  
903  1 Y 1 A LEU 903  ? A LEU 903  
904  1 Y 1 A ASP 904  ? A ASP 904  
905  1 Y 1 A MET 905  ? A MET 905  
906  1 Y 1 A GLU 906  ? A GLU 906  
907  1 Y 1 A ILE 907  ? A ILE 907  
908  1 Y 1 A GLU 908  ? A GLU 908  
909  1 Y 1 A ARG 909  ? A ARG 909  
910  1 Y 1 A ILE 910  ? A ILE 910  
911  1 Y 1 A LEU 911  ? A LEU 911  
912  1 Y 1 A GLY 912  ? A GLY 912  
913  1 Y 1 A VAL 913  ? A VAL 913  
914  1 Y 1 A ARG 914  ? A ARG 914  
915  1 Y 1 A LEU 915  ? A LEU 915  
916  1 Y 1 A GLN 916  ? A GLN 916  
917  1 Y 1 A ALA 917  ? A ALA 917  
918  1 Y 1 A GLY 918  ? A GLY 918  
919  1 Y 1 A LEU 919  ? A LEU 919  
920  1 Y 1 A ARG 920  ? A ARG 920  
921  1 Y 1 A ALA 921  ? A ALA 921  
922  1 Y 1 A TRP 922  ? A TRP 922  
923  1 Y 1 A THR 923  ? A THR 923  
924  1 Y 1 A GLN 924  ? A GLN 924  
925  1 Y 1 A VAL 925  ? A VAL 925  
926  1 Y 1 A LEU 926  ? A LEU 926  
927  1 Y 1 A LEU 927  ? A LEU 927  
928  1 Y 1 A GLY 928  ? A GLY 928  
929  1 Y 1 A GLN 929  ? A GLN 929  
930  1 Y 1 A ALA 930  ? A ALA 930  
931  1 Y 1 A GLU 931  ? A GLU 931  
932  1 Y 1 A ASP 932  ? A ASP 932  
933  1 Y 1 A LYS 933  ? A LYS 933  
934  1 Y 1 A ALA 934  ? A ALA 934  
935  1 Y 1 A GLU 935  ? A GLU 935  
936  1 Y 1 A VAL 936  ? A VAL 936  
937  1 Y 1 A ASP 937  ? A ASP 937  
938  1 Y 1 A MET 938  ? A MET 938  
939  1 Y 1 A ASP 939  ? A ASP 939  
940  1 Y 1 A THR 940  ? A THR 940  
941  1 Y 1 A ASP 941  ? A ASP 941  
942  1 Y 1 A ALA 942  ? A ALA 942  
943  1 Y 1 A PRO 943  ? A PRO 943  
944  1 Y 1 A GLN 944  ? A GLN 944  
945  1 Y 1 A VAL 945  ? A VAL 945  
946  1 Y 1 A SER 946  ? A SER 946  
947  1 Y 1 A HIS 947  ? A HIS 947  
948  1 Y 1 A LYS 948  ? A LYS 948  
949  1 Y 1 A PRO 949  ? A PRO 949  
950  1 Y 1 A GLY 950  ? A GLY 950  
951  1 Y 1 A GLY 951  ? A GLY 951  
952  1 Y 1 A GLU 952  ? A GLU 952  
953  1 Y 1 A PRO 953  ? A PRO 953  
954  1 Y 1 A LYS 954  ? A LYS 954  
955  1 Y 1 A ILE 955  ? A ILE 955  
956  1 Y 1 A LYS 956  ? A LYS 956  
957  1 Y 1 A ASN 957  ? A ASN 957  
958  1 Y 1 A VAL 958  ? A VAL 958  
959  1 Y 1 A VAL 959  ? A VAL 959  
960  1 Y 1 A HIS 960  ? A HIS 960  
961  1 Y 1 A GLU 961  ? A GLU 961  
962  1 Y 1 A LEU 962  ? A LEU 962  
963  1 Y 1 A ARG 963  ? A ARG 963  
964  1 Y 1 A ILE 964  ? A ILE 964  
965  1 Y 1 A THR 965  ? A THR 965  
966  1 Y 1 A ASN 966  ? A ASN 966  
967  1 Y 1 A GLN 967  ? A GLN 967  
968  1 Y 1 A VAL 968  ? A VAL 968  
969  1 Y 1 A ILE 969  ? A ILE 969  
970  1 Y 1 A TYR 970  ? A TYR 970  
971  1 Y 1 A LEU 971  ? A LEU 971  
972  1 Y 1 A ASN 972  ? A ASN 972  
973  1 Y 1 A PRO 973  ? A PRO 973  
974  1 Y 1 A PRO 974  ? A PRO 974  
975  1 Y 1 A ILE 975  ? A ILE 975  
976  1 Y 1 A GLU 976  ? A GLU 976  
977  1 Y 1 A GLU 977  ? A GLU 977  
978  1 Y 1 A CYS 978  ? A CYS 978  
979  1 Y 1 A ARG 979  ? A ARG 979  
980  1 Y 1 A TYR 980  ? A TYR 980  
981  1 Y 1 A LYS 981  ? A LYS 981  
982  1 Y 1 A LEU 982  ? A LEU 982  
983  1 Y 1 A TYR 983  ? A TYR 983  
984  1 Y 1 A GLN 984  ? A GLN 984  
985  1 Y 1 A GLU 985  ? A GLU 985  
986  1 Y 1 A MET 986  ? A MET 986  
987  1 Y 1 A PHE 987  ? A PHE 987  
988  1 Y 1 A ALA 988  ? A ALA 988  
989  1 Y 1 A TRP 989  ? A TRP 989  
990  1 Y 1 A LYS 990  ? A LYS 990  
991  1 Y 1 A MET 991  ? A MET 991  
992  1 Y 1 A VAL 992  ? A VAL 992  
993  1 Y 1 A VAL 993  ? A VAL 993  
994  1 Y 1 A LEU 994  ? A LEU 994  
995  1 Y 1 A SER 995  ? A SER 995  
996  1 Y 1 A LEU 996  ? A LEU 996  
997  1 Y 1 A PRO 997  ? A PRO 997  
998  1 Y 1 A ARG 998  ? A ARG 998  
999  1 Y 1 A ILE 999  ? A ILE 999  
1000 1 Y 1 A GLN 1000 ? A GLN 1000 
1001 1 Y 1 A SER 1001 ? A SER 1001 
1002 1 Y 1 A GLN 1002 ? A GLN 1002 
1003 1 Y 1 A ARG 1003 ? A ARG 1003 
1004 1 Y 1 A TYR 1004 ? A TYR 1004 
1005 1 Y 1 A GLN 1005 ? A GLN 1005 
1006 1 Y 1 A VAL 1006 ? A VAL 1006 
1007 1 Y 1 A GLY 1007 ? A GLY 1007 
1008 1 Y 1 A VAL 1008 ? A VAL 1008 
1009 1 Y 1 A HIS 1009 ? A HIS 1009 
1010 1 Y 1 A TYR 1010 ? A TYR 1010 
1011 1 Y 1 A GLU 1011 ? A GLU 1011 
1012 1 Y 1 A LEU 1012 ? A LEU 1012 
1013 1 Y 1 A THR 1013 ? A THR 1013 
1014 1 Y 1 A GLU 1014 ? A GLU 1014 
1015 1 Y 1 A GLU 1015 ? A GLU 1015 
1016 1 Y 1 A GLU 1016 ? A GLU 1016 
1017 1 Y 1 A LYS 1017 ? A LYS 1017 
1018 1 Y 1 A PHE 1018 ? A PHE 1018 
1019 1 Y 1 A TYR 1019 ? A TYR 1019 
1020 1 Y 1 A ARG 1020 ? A ARG 1020 
1021 1 Y 1 A ASN 1021 ? A ASN 1021 
1022 1 Y 1 A ALA 1022 ? A ALA 1022 
1023 1 Y 1 A LEU 1023 ? A LEU 1023 
1024 1 Y 1 A THR 1024 ? A THR 1024 
1025 1 Y 1 A ARG 1025 ? A ARG 1025 
1026 1 Y 1 A MET 1026 ? A MET 1026 
1027 1 Y 1 A PRO 1027 ? A PRO 1027 
1028 1 Y 1 A ASP 1028 ? A ASP 1028 
1029 1 Y 1 A GLY 1029 ? A GLY 1029 
1030 1 Y 1 A PRO 1030 ? A PRO 1030 
1031 1 Y 1 A VAL 1031 ? A VAL 1031 
1032 1 Y 1 A ALA 1032 ? A ALA 1032 
1033 1 Y 1 A LEU 1033 ? A LEU 1033 
1034 1 Y 1 A GLU 1034 ? A GLU 1034 
1035 1 Y 1 A GLU 1035 ? A GLU 1035 
1036 1 Y 1 A SER 1036 ? A SER 1036 
1037 1 Y 1 A TYR 1037 ? A TYR 1037 
1038 1 Y 1 A SER 1038 ? A SER 1038 
1039 1 Y 1 A ALA 1039 ? A ALA 1039 
1040 1 Y 1 A VAL 1040 ? A VAL 1040 
1041 1 Y 1 A MET 1041 ? A MET 1041 
1042 1 Y 1 A GLY 1042 ? A GLY 1042 
1043 1 Y 1 A ILE 1043 ? A ILE 1043 
1044 1 Y 1 A VAL 1044 ? A VAL 1044 
1045 1 Y 1 A SER 1045 ? A SER 1045 
1046 1 Y 1 A GLU 1046 ? A GLU 1046 
1047 1 Y 1 A VAL 1047 ? A VAL 1047 
1048 1 Y 1 A GLU 1048 ? A GLU 1048 
1049 1 Y 1 A GLN 1049 ? A GLN 1049 
1050 1 Y 1 A TYR 1050 ? A TYR 1050 
1051 1 Y 1 A VAL 1051 ? A VAL 1051 
1052 1 Y 1 A LYS 1052 ? A LYS 1052 
1053 1 Y 1 A VAL 1053 ? A VAL 1053 
1054 1 Y 1 A TRP 1054 ? A TRP 1054 
1055 1 Y 1 A LEU 1055 ? A LEU 1055 
1056 1 Y 1 A GLN 1056 ? A GLN 1056 
1057 1 Y 1 A TYR 1057 ? A TYR 1057 
1058 1 Y 1 A GLN 1058 ? A GLN 1058 
1059 1 Y 1 A CYS 1059 ? A CYS 1059 
1060 1 Y 1 A LEU 1060 ? A LEU 1060 
1061 1 Y 1 A TRP 1061 ? A TRP 1061 
1062 1 Y 1 A ASP 1062 ? A ASP 1062 
1063 1 Y 1 A MET 1063 ? A MET 1063 
1064 1 Y 1 A GLN 1064 ? A GLN 1064 
1065 1 Y 1 A ALA 1065 ? A ALA 1065 
1066 1 Y 1 A GLU 1066 ? A GLU 1066 
1067 1 Y 1 A ASN 1067 ? A ASN 1067 
1068 1 Y 1 A ILE 1068 ? A ILE 1068 
1069 1 Y 1 A TYR 1069 ? A TYR 1069 
1070 1 Y 1 A ASN 1070 ? A ASN 1070 
1071 1 Y 1 A ARG 1071 ? A ARG 1071 
1072 1 Y 1 A LEU 1072 ? A LEU 1072 
1073 1 Y 1 A GLY 1073 ? A GLY 1073 
1074 1 Y 1 A GLU 1074 ? A GLU 1074 
1075 1 Y 1 A ASP 1075 ? A ASP 1075 
1076 1 Y 1 A LEU 1076 ? A LEU 1076 
1077 1 Y 1 A ASN 1077 ? A ASN 1077 
1078 1 Y 1 A LYS 1078 ? A LYS 1078 
1079 1 Y 1 A TRP 1079 ? A TRP 1079 
1080 1 Y 1 A GLN 1080 ? A GLN 1080 
1081 1 Y 1 A ALA 1081 ? A ALA 1081 
1082 1 Y 1 A LEU 1082 ? A LEU 1082 
1083 1 Y 1 A LEU 1083 ? A LEU 1083 
1084 1 Y 1 A VAL 1084 ? A VAL 1084 
1085 1 Y 1 A GLN 1085 ? A GLN 1085 
1086 1 Y 1 A ILE 1086 ? A ILE 1086 
1087 1 Y 1 A ARG 1087 ? A ARG 1087 
1088 1 Y 1 A LYS 1088 ? A LYS 1088 
1089 1 Y 1 A ALA 1089 ? A ALA 1089 
1090 1 Y 1 A ARG 1090 ? A ARG 1090 
1091 1 Y 1 A GLY 1091 ? A GLY 1091 
1092 1 Y 1 A THR 1092 ? A THR 1092 
1093 1 Y 1 A PHE 1093 ? A PHE 1093 
1094 1 Y 1 A ASP 1094 ? A ASP 1094 
1095 1 Y 1 A ASN 1095 ? A ASN 1095 
1096 1 Y 1 A ALA 1096 ? A ALA 1096 
1097 1 Y 1 A GLU 1097 ? A GLU 1097 
1098 1 Y 1 A THR 1098 ? A THR 1098 
1099 1 Y 1 A LYS 1099 ? A LYS 1099 
1100 1 Y 1 A LYS 1100 ? A LYS 1100 
1101 1 Y 1 A GLU 1101 ? A GLU 1101 
1102 1 Y 1 A PHE 1102 ? A PHE 1102 
1103 1 Y 1 A GLY 1103 ? A GLY 1103 
1104 1 Y 1 A PRO 1104 ? A PRO 1104 
1105 1 Y 1 A VAL 1105 ? A VAL 1105 
1106 1 Y 1 A VAL 1106 ? A VAL 1106 
1107 1 Y 1 A ILE 1107 ? A ILE 1107 
1108 1 Y 1 A ASP 1108 ? A ASP 1108 
1109 1 Y 1 A TYR 1109 ? A TYR 1109 
1110 1 Y 1 A GLY 1110 ? A GLY 1110 
1111 1 Y 1 A LYS 1111 ? A LYS 1111 
1112 1 Y 1 A VAL 1112 ? A VAL 1112 
1113 1 Y 1 A GLN 1113 ? A GLN 1113 
1114 1 Y 1 A SER 1114 ? A SER 1114 
1115 1 Y 1 A LYS 1115 ? A LYS 1115 
1116 1 Y 1 A VAL 1116 ? A VAL 1116 
1117 1 Y 1 A ASN 1117 ? A ASN 1117 
1118 1 Y 1 A LEU 1118 ? A LEU 1118 
1119 1 Y 1 A LYS 1119 ? A LYS 1119 
1120 1 Y 1 A TYR 1120 ? A TYR 1120 
1121 1 Y 1 A ASP 1121 ? A ASP 1121 
1122 1 Y 1 A SER 1122 ? A SER 1122 
1123 1 Y 1 A TRP 1123 ? A TRP 1123 
1124 1 Y 1 A HIS 1124 ? A HIS 1124 
1125 1 Y 1 A LYS 1125 ? A LYS 1125 
1126 1 Y 1 A GLU 1126 ? A GLU 1126 
1127 1 Y 1 A VAL 1127 ? A VAL 1127 
1128 1 Y 1 A LEU 1128 ? A LEU 1128 
1129 1 Y 1 A SER 1129 ? A SER 1129 
1130 1 Y 1 A LYS 1130 ? A LYS 1130 
1131 1 Y 1 A PHE 1131 ? A PHE 1131 
1132 1 Y 1 A GLY 1132 ? A GLY 1132 
1133 1 Y 1 A GLN 1133 ? A GLN 1133 
1134 1 Y 1 A MET 1134 ? A MET 1134 
1135 1 Y 1 A LEU 1135 ? A LEU 1135 
1136 1 Y 1 A GLY 1136 ? A GLY 1136 
1137 1 Y 1 A SER 1137 ? A SER 1137 
1138 1 Y 1 A ASN 1138 ? A ASN 1138 
1139 1 Y 1 A MET 1139 ? A MET 1139 
1140 1 Y 1 A THR 1140 ? A THR 1140 
1141 1 Y 1 A GLU 1141 ? A GLU 1141 
1142 1 Y 1 A PHE 1142 ? A PHE 1142 
1143 1 Y 1 A HIS 1143 ? A HIS 1143 
1144 1 Y 1 A SER 1144 ? A SER 1144 
1145 1 Y 1 A GLN 1145 ? A GLN 1145 
1146 1 Y 1 A ILE 1146 ? A ILE 1146 
1147 1 Y 1 A SER 1147 ? A SER 1147 
1148 1 Y 1 A LYS 1148 ? A LYS 1148 
1149 1 Y 1 A SER 1149 ? A SER 1149 
1150 1 Y 1 A ARG 1150 ? A ARG 1150 
1151 1 Y 1 A GLN 1151 ? A GLN 1151 
1152 1 Y 1 A GLU 1152 ? A GLU 1152 
1153 1 Y 1 A LEU 1153 ? A LEU 1153 
1154 1 Y 1 A GLU 1154 ? A GLU 1154 
1155 1 Y 1 A GLN 1155 ? A GLN 1155 
1156 1 Y 1 A HIS 1156 ? A HIS 1156 
1157 1 Y 1 A SER 1157 ? A SER 1157 
1158 1 Y 1 A VAL 1158 ? A VAL 1158 
1159 1 Y 1 A ASP 1159 ? A ASP 1159 
1160 1 Y 1 A THR 1160 ? A THR 1160 
1161 1 Y 1 A ALA 1161 ? A ALA 1161 
1162 1 Y 1 A SER 1162 ? A SER 1162 
1163 1 Y 1 A THR 1163 ? A THR 1163 
1164 1 Y 1 A SER 1164 ? A SER 1164 
1165 1 Y 1 A ASP 1165 ? A ASP 1165 
1166 1 Y 1 A ALA 1166 ? A ALA 1166 
1167 1 Y 1 A VAL 1167 ? A VAL 1167 
1168 1 Y 1 A THR 1168 ? A THR 1168 
1169 1 Y 1 A PHE 1169 ? A PHE 1169 
1170 1 Y 1 A ILE 1170 ? A ILE 1170 
1171 1 Y 1 A THR 1171 ? A THR 1171 
1172 1 Y 1 A TYR 1172 ? A TYR 1172 
1173 1 Y 1 A VAL 1173 ? A VAL 1173 
1174 1 Y 1 A GLN 1174 ? A GLN 1174 
1175 1 Y 1 A SER 1175 ? A SER 1175 
1176 1 Y 1 A LEU 1176 ? A LEU 1176 
1177 1 Y 1 A LYS 1177 ? A LYS 1177 
1178 1 Y 1 A ARG 1178 ? A ARG 1178 
1179 1 Y 1 A LYS 1179 ? A LYS 1179 
1180 1 Y 1 A ILE 1180 ? A ILE 1180 
1181 1 Y 1 A LYS 1181 ? A LYS 1181 
1182 1 Y 1 A GLN 1182 ? A GLN 1182 
1183 1 Y 1 A PHE 1183 ? A PHE 1183 
1184 1 Y 1 A GLU 1184 ? A GLU 1184 
1185 1 Y 1 A LYS 1185 ? A LYS 1185 
1186 1 Y 1 A GLN 1186 ? A GLN 1186 
1187 1 Y 1 A VAL 1187 ? A VAL 1187 
1188 1 Y 1 A GLU 1188 ? A GLU 1188 
1189 1 Y 1 A LEU 1189 ? A LEU 1189 
1190 1 Y 1 A TYR 1190 ? A TYR 1190 
1191 1 Y 1 A ARG 1191 ? A ARG 1191 
1192 1 Y 1 A ASN 1192 ? A ASN 1192 
1193 1 Y 1 A GLY 1193 ? A GLY 1193 
1194 1 Y 1 A GLN 1194 ? A GLN 1194 
1195 1 Y 1 A ARG 1195 ? A ARG 1195 
1196 1 Y 1 A LEU 1196 ? A LEU 1196 
1197 1 Y 1 A LEU 1197 ? A LEU 1197 
1198 1 Y 1 A GLU 1198 ? A GLU 1198 
1199 1 Y 1 A LYS 1199 ? A LYS 1199 
1200 1 Y 1 A GLN 1200 ? A GLN 1200 
1201 1 Y 1 A ARG 1201 ? A ARG 1201 
1202 1 Y 1 A PHE 1202 ? A PHE 1202 
1203 1 Y 1 A GLN 1203 ? A GLN 1203 
1204 1 Y 1 A PHE 1204 ? A PHE 1204 
1205 1 Y 1 A PRO 1205 ? A PRO 1205 
1206 1 Y 1 A PRO 1206 ? A PRO 1206 
1207 1 Y 1 A SER 1207 ? A SER 1207 
1208 1 Y 1 A TRP 1208 ? A TRP 1208 
1209 1 Y 1 A LEU 1209 ? A LEU 1209 
1210 1 Y 1 A TYR 1210 ? A TYR 1210 
1211 1 Y 1 A ILE 1211 ? A ILE 1211 
1212 1 Y 1 A ASP 1212 ? A ASP 1212 
1213 1 Y 1 A ASN 1213 ? A ASN 1213 
1214 1 Y 1 A ILE 1214 ? A ILE 1214 
1215 1 Y 1 A GLU 1215 ? A GLU 1215 
1216 1 Y 1 A GLY 1216 ? A GLY 1216 
1217 1 Y 1 A GLU 1217 ? A GLU 1217 
1218 1 Y 1 A TRP 1218 ? A TRP 1218 
1219 1 Y 1 A GLY 1219 ? A GLY 1219 
1220 1 Y 1 A ALA 1220 ? A ALA 1220 
1221 1 Y 1 A PHE 1221 ? A PHE 1221 
1222 1 Y 1 A ASN 1222 ? A ASN 1222 
1223 1 Y 1 A ASP 1223 ? A ASP 1223 
1224 1 Y 1 A ILE 1224 ? A ILE 1224 
1225 1 Y 1 A MET 1225 ? A MET 1225 
1226 1 Y 1 A ARG 1226 ? A ARG 1226 
1227 1 Y 1 A ARG 1227 ? A ARG 1227 
1228 1 Y 1 A LYS 1228 ? A LYS 1228 
1229 1 Y 1 A ASP 1229 ? A ASP 1229 
1230 1 Y 1 A SER 1230 ? A SER 1230 
1231 1 Y 1 A ALA 1231 ? A ALA 1231 
1232 1 Y 1 A ILE 1232 ? A ILE 1232 
1233 1 Y 1 A GLN 1233 ? A GLN 1233 
1234 1 Y 1 A GLN 1234 ? A GLN 1234 
1235 1 Y 1 A GLN 1235 ? A GLN 1235 
1236 1 Y 1 A VAL 1236 ? A VAL 1236 
1237 1 Y 1 A ALA 1237 ? A ALA 1237 
1238 1 Y 1 A ASN 1238 ? A ASN 1238 
1239 1 Y 1 A LEU 1239 ? A LEU 1239 
1240 1 Y 1 A GLN 1240 ? A GLN 1240 
1241 1 Y 1 A MET 1241 ? A MET 1241 
1242 1 Y 1 A LYS 1242 ? A LYS 1242 
1243 1 Y 1 A ILE 1243 ? A ILE 1243 
1244 1 Y 1 A VAL 1244 ? A VAL 1244 
1245 1 Y 1 A GLN 1245 ? A GLN 1245 
1246 1 Y 1 A GLU 1246 ? A GLU 1246 
1247 1 Y 1 A ASP 1247 ? A ASP 1247 
1248 1 Y 1 A ARG 1248 ? A ARG 1248 
1249 1 Y 1 A ALA 1249 ? A ALA 1249 
1250 1 Y 1 A VAL 1250 ? A VAL 1250 
1251 1 Y 1 A GLU 1251 ? A GLU 1251 
1252 1 Y 1 A SER 1252 ? A SER 1252 
1253 1 Y 1 A ARG 1253 ? A ARG 1253 
1254 1 Y 1 A THR 1254 ? A THR 1254 
1255 1 Y 1 A THR 1255 ? A THR 1255 
1256 1 Y 1 A ASP 1256 ? A ASP 1256 
1257 1 Y 1 A LEU 1257 ? A LEU 1257 
1258 1 Y 1 A LEU 1258 ? A LEU 1258 
1259 1 Y 1 A THR 1259 ? A THR 1259 
1260 1 Y 1 A ASP 1260 ? A ASP 1260 
1261 1 Y 1 A TRP 1261 ? A TRP 1261 
1262 1 Y 1 A GLU 1262 ? A GLU 1262 
1263 1 Y 1 A LYS 1263 ? A LYS 1263 
1264 1 Y 1 A THR 1264 ? A THR 1264 
1265 1 Y 1 A LYS 1265 ? A LYS 1265 
1266 1 Y 1 A PRO 1266 ? A PRO 1266 
1267 1 Y 1 A VAL 1267 ? A VAL 1267 
1268 1 Y 1 A THR 1268 ? A THR 1268 
1269 1 Y 1 A GLY 1269 ? A GLY 1269 
1270 1 Y 1 A ASN 1270 ? A ASN 1270 
1271 1 Y 1 A LEU 1271 ? A LEU 1271 
1272 1 Y 1 A ARG 1272 ? A ARG 1272 
1273 1 Y 1 A PRO 1273 ? A PRO 1273 
1274 1 Y 1 A GLU 1274 ? A GLU 1274 
1275 1 Y 1 A GLU 1275 ? A GLU 1275 
1276 1 Y 1 A ALA 1276 ? A ALA 1276 
1277 1 Y 1 A LEU 1277 ? A LEU 1277 
1278 1 Y 1 A GLN 1278 ? A GLN 1278 
1279 1 Y 1 A ALA 1279 ? A ALA 1279 
1280 1 Y 1 A LEU 1280 ? A LEU 1280 
1281 1 Y 1 A THR 1281 ? A THR 1281 
1282 1 Y 1 A ILE 1282 ? A ILE 1282 
1283 1 Y 1 A TYR 1283 ? A TYR 1283 
1284 1 Y 1 A GLU 1284 ? A GLU 1284 
1285 1 Y 1 A GLY 1285 ? A GLY 1285 
1286 1 Y 1 A LYS 1286 ? A LYS 1286 
1287 1 Y 1 A PHE 1287 ? A PHE 1287 
1288 1 Y 1 A GLY 1288 ? A GLY 1288 
1289 1 Y 1 A ARG 1289 ? A ARG 1289 
1290 1 Y 1 A LEU 1290 ? A LEU 1290 
1291 1 Y 1 A LYS 1291 ? A LYS 1291 
1292 1 Y 1 A ASP 1292 ? A ASP 1292 
1293 1 Y 1 A ASP 1293 ? A ASP 1293 
1294 1 Y 1 A ARG 1294 ? A ARG 1294 
1295 1 Y 1 A GLU 1295 ? A GLU 1295 
1296 1 Y 1 A LYS 1296 ? A LYS 1296 
1297 1 Y 1 A CYS 1297 ? A CYS 1297 
1298 1 Y 1 A ALA 1298 ? A ALA 1298 
1299 1 Y 1 A LYS 1299 ? A LYS 1299 
1300 1 Y 1 A ALA 1300 ? A ALA 1300 
1301 1 Y 1 A LYS 1301 ? A LYS 1301 
1302 1 Y 1 A GLU 1302 ? A GLU 1302 
1303 1 Y 1 A ALA 1303 ? A ALA 1303 
1304 1 Y 1 A LEU 1304 ? A LEU 1304 
1305 1 Y 1 A GLU 1305 ? A GLU 1305 
1306 1 Y 1 A LEU 1306 ? A LEU 1306 
1307 1 Y 1 A THR 1307 ? A THR 1307 
1308 1 Y 1 A ASP 1308 ? A ASP 1308 
1309 1 Y 1 A THR 1309 ? A THR 1309 
1310 1 Y 1 A GLY 1310 ? A GLY 1310 
1311 1 Y 1 A LEU 1311 ? A LEU 1311 
1312 1 Y 1 A LEU 1312 ? A LEU 1312 
1313 1 Y 1 A SER 1313 ? A SER 1313 
1314 1 Y 1 A GLY 1314 ? A GLY 1314 
1315 1 Y 1 A SER 1315 ? A SER 1315 
1316 1 Y 1 A GLU 1316 ? A GLU 1316 
1317 1 Y 1 A GLU 1317 ? A GLU 1317 
1318 1 Y 1 A ARG 1318 ? A ARG 1318 
1319 1 Y 1 A VAL 1319 ? A VAL 1319 
1320 1 Y 1 A GLN 1320 ? A GLN 1320 
1321 1 Y 1 A VAL 1321 ? A VAL 1321 
1322 1 Y 1 A ALA 1322 ? A ALA 1322 
1323 1 Y 1 A LEU 1323 ? A LEU 1323 
1324 1 Y 1 A GLU 1324 ? A GLU 1324 
1325 1 Y 1 A GLU 1325 ? A GLU 1325 
1326 1 Y 1 A LEU 1326 ? A LEU 1326 
1327 1 Y 1 A GLN 1327 ? A GLN 1327 
1328 1 Y 1 A ASP 1328 ? A ASP 1328 
1329 1 Y 1 A LEU 1329 ? A LEU 1329 
1330 1 Y 1 A LYS 1330 ? A LYS 1330 
1331 1 Y 1 A GLY 1331 ? A GLY 1331 
1332 1 Y 1 A VAL 1332 ? A VAL 1332 
1333 1 Y 1 A TRP 1333 ? A TRP 1333 
1334 1 Y 1 A SER 1334 ? A SER 1334 
1335 1 Y 1 A GLU 1335 ? A GLU 1335 
1336 1 Y 1 A LEU 1336 ? A LEU 1336 
1337 1 Y 1 A SER 1337 ? A SER 1337 
1338 1 Y 1 A LYS 1338 ? A LYS 1338 
1339 1 Y 1 A VAL 1339 ? A VAL 1339 
1340 1 Y 1 A TRP 1340 ? A TRP 1340 
1341 1 Y 1 A GLU 1341 ? A GLU 1341 
1342 1 Y 1 A GLN 1342 ? A GLN 1342 
1343 1 Y 1 A ILE 1343 ? A ILE 1343 
1344 1 Y 1 A ASP 1344 ? A ASP 1344 
1345 1 Y 1 A GLN 1345 ? A GLN 1345 
1346 1 Y 1 A MET 1346 ? A MET 1346 
1347 1 Y 1 A LYS 1347 ? A LYS 1347 
1348 1 Y 1 A GLU 1348 ? A GLU 1348 
1349 1 Y 1 A GLN 1349 ? A GLN 1349 
1350 1 Y 1 A PRO 1350 ? A PRO 1350 
1351 1 Y 1 A TRP 1351 ? A TRP 1351 
1352 1 Y 1 A VAL 1352 ? A VAL 1352 
1353 1 Y 1 A SER 1353 ? A SER 1353 
1354 1 Y 1 A VAL 1354 ? A VAL 1354 
1355 1 Y 1 A GLN 1355 ? A GLN 1355 
1356 1 Y 1 A PRO 1356 ? A PRO 1356 
1357 1 Y 1 A ARG 1357 ? A ARG 1357 
1358 1 Y 1 A LYS 1358 ? A LYS 1358 
1359 1 Y 1 A LEU 1359 ? A LEU 1359 
1360 1 Y 1 A ARG 1360 ? A ARG 1360 
1361 1 Y 1 A GLN 1361 ? A GLN 1361 
1362 1 Y 1 A ASN 1362 ? A ASN 1362 
1363 1 Y 1 A LEU 1363 ? A LEU 1363 
1364 1 Y 1 A ASP 1364 ? A ASP 1364 
1365 1 Y 1 A ALA 1365 ? A ALA 1365 
1366 1 Y 1 A LEU 1366 ? A LEU 1366 
1367 1 Y 1 A LEU 1367 ? A LEU 1367 
1368 1 Y 1 A ASN 1368 ? A ASN 1368 
1369 1 Y 1 A GLN 1369 ? A GLN 1369 
1370 1 Y 1 A LEU 1370 ? A LEU 1370 
1371 1 Y 1 A LYS 1371 ? A LYS 1371 
1372 1 Y 1 A SER 1372 ? A SER 1372 
1373 1 Y 1 A PHE 1373 ? A PHE 1373 
1374 1 Y 1 A PRO 1374 ? A PRO 1374 
1375 1 Y 1 A ALA 1375 ? A ALA 1375 
1376 1 Y 1 A ARG 1376 ? A ARG 1376 
1377 1 Y 1 A LEU 1377 ? A LEU 1377 
1378 1 Y 1 A ARG 1378 ? A ARG 1378 
1379 1 Y 1 A GLN 1379 ? A GLN 1379 
1380 1 Y 1 A TYR 1380 ? A TYR 1380 
1381 1 Y 1 A ALA 1381 ? A ALA 1381 
1382 1 Y 1 A SER 1382 ? A SER 1382 
1383 1 Y 1 A TYR 1383 ? A TYR 1383 
1384 1 Y 1 A GLU 1384 ? A GLU 1384 
1385 1 Y 1 A PHE 1385 ? A PHE 1385 
1386 1 Y 1 A VAL 1386 ? A VAL 1386 
1387 1 Y 1 A GLN 1387 ? A GLN 1387 
1388 1 Y 1 A ARG 1388 ? A ARG 1388 
1389 1 Y 1 A LEU 1389 ? A LEU 1389 
1390 1 Y 1 A LEU 1390 ? A LEU 1390 
1391 1 Y 1 A LYS 1391 ? A LYS 1391 
1392 1 Y 1 A GLY 1392 ? A GLY 1392 
1393 1 Y 1 A TYR 1393 ? A TYR 1393 
1394 1 Y 1 A MET 1394 ? A MET 1394 
1395 1 Y 1 A LYS 1395 ? A LYS 1395 
1396 1 Y 1 A ILE 1396 ? A ILE 1396 
1397 1 Y 1 A ASN 1397 ? A ASN 1397 
1398 1 Y 1 A MET 1398 ? A MET 1398 
1399 1 Y 1 A LEU 1399 ? A LEU 1399 
1400 1 Y 1 A VAL 1400 ? A VAL 1400 
1401 1 Y 1 A ILE 1401 ? A ILE 1401 
1402 1 Y 1 A GLU 1402 ? A GLU 1402 
1403 1 Y 1 A LEU 1403 ? A LEU 1403 
1404 1 Y 1 A LYS 1404 ? A LYS 1404 
1405 1 Y 1 A SER 1405 ? A SER 1405 
1406 1 Y 1 A GLU 1406 ? A GLU 1406 
1407 1 Y 1 A ALA 1407 ? A ALA 1407 
1408 1 Y 1 A LEU 1408 ? A LEU 1408 
1409 1 Y 1 A LYS 1409 ? A LYS 1409 
1410 1 Y 1 A ASP 1410 ? A ASP 1410 
1411 1 Y 1 A ARG 1411 ? A ARG 1411 
1412 1 Y 1 A HIS 1412 ? A HIS 1412 
1413 1 Y 1 A TRP 1413 ? A TRP 1413 
1414 1 Y 1 A LYS 1414 ? A LYS 1414 
1415 1 Y 1 A GLN 1415 ? A GLN 1415 
1416 1 Y 1 A LEU 1416 ? A LEU 1416 
1417 1 Y 1 A MET 1417 ? A MET 1417 
1418 1 Y 1 A LYS 1418 ? A LYS 1418 
1419 1 Y 1 A ARG 1419 ? A ARG 1419 
1420 1 Y 1 A LEU 1420 ? A LEU 1420 
1421 1 Y 1 A HIS 1421 ? A HIS 1421 
1422 1 Y 1 A VAL 1422 ? A VAL 1422 
1423 1 Y 1 A ASN 1423 ? A ASN 1423 
1424 1 Y 1 A TRP 1424 ? A TRP 1424 
1425 1 Y 1 A VAL 1425 ? A VAL 1425 
1426 1 Y 1 A VAL 1426 ? A VAL 1426 
1427 1 Y 1 A SER 1427 ? A SER 1427 
1428 1 Y 1 A GLU 1428 ? A GLU 1428 
1429 1 Y 1 A LEU 1429 ? A LEU 1429 
1430 1 Y 1 A THR 1430 ? A THR 1430 
1431 1 Y 1 A LEU 1431 ? A LEU 1431 
1432 1 Y 1 A GLY 1432 ? A GLY 1432 
1433 1 Y 1 A GLN 1433 ? A GLN 1433 
1434 1 Y 1 A ILE 1434 ? A ILE 1434 
1435 1 Y 1 A TRP 1435 ? A TRP 1435 
1436 1 Y 1 A ASP 1436 ? A ASP 1436 
1437 1 Y 1 A VAL 1437 ? A VAL 1437 
1438 1 Y 1 A ASP 1438 ? A ASP 1438 
1439 1 Y 1 A LEU 1439 ? A LEU 1439 
1440 1 Y 1 A GLN 1440 ? A GLN 1440 
1441 1 Y 1 A LYS 1441 ? A LYS 1441 
1442 1 Y 1 A ASN 1442 ? A ASN 1442 
1443 1 Y 1 A GLU 1443 ? A GLU 1443 
1444 1 Y 1 A ALA 1444 ? A ALA 1444 
1445 1 Y 1 A ILE 1445 ? A ILE 1445 
1446 1 Y 1 A VAL 1446 ? A VAL 1446 
1447 1 Y 1 A LYS 1447 ? A LYS 1447 
1448 1 Y 1 A ASP 1448 ? A ASP 1448 
1449 1 Y 1 A VAL 1449 ? A VAL 1449 
1450 1 Y 1 A LEU 1450 ? A LEU 1450 
1451 1 Y 1 A LEU 1451 ? A LEU 1451 
1452 1 Y 1 A VAL 1452 ? A VAL 1452 
1453 1 Y 1 A ALA 1453 ? A ALA 1453 
1454 1 Y 1 A GLN 1454 ? A GLN 1454 
1455 1 Y 1 A GLY 1455 ? A GLY 1455 
1456 1 Y 1 A GLU 1456 ? A GLU 1456 
1457 1 Y 1 A MET 1457 ? A MET 1457 
1458 1 Y 1 A ALA 1458 ? A ALA 1458 
1459 1 Y 1 A LEU 1459 ? A LEU 1459 
1460 1 Y 1 A GLU 1460 ? A GLU 1460 
1461 1 Y 1 A GLU 1461 ? A GLU 1461 
1462 1 Y 1 A PHE 1462 ? A PHE 1462 
1463 1 Y 1 A PRO 2020 ? A PRO 2020 
1464 1 Y 1 A GLY 2021 ? A GLY 2021 
1465 1 Y 1 A TYR 2022 ? A TYR 2022 
1466 1 Y 1 A ALA 2023 ? A ALA 2023 
1467 1 Y 1 A GLY 2024 ? A GLY 2024 
1468 1 Y 1 A ARG 2025 ? A ARG 2025 
1469 1 Y 1 A SER 2026 ? A SER 2026 
1470 1 Y 1 A ASN 2027 ? A ASN 2027 
1471 1 Y 1 A LYS 2115 ? A LYS 2115 
1472 1 Y 1 A GLU 2116 ? A GLU 2116 
1473 1 Y 1 A GLU 2117 ? A GLU 2117 
1474 1 Y 1 A ARG 2118 ? A ARG 2118 
1475 1 Y 1 A GLY 2119 ? A GLY 2119 
1476 1 Y 1 A GLU 2120 ? A GLU 2120 
1477 1 Y 1 A ALA 2121 ? A ALA 2121 
1478 1 Y 1 A VAL 2122 ? A VAL 2122 
1479 1 Y 1 A ASP 2123 ? A ASP 2123 
1480 1 Y 1 A GLU 2124 ? A GLU 2124 
1481 1 Y 1 A GLY 2125 ? A GLY 2125 
1482 1 Y 1 A GLU 2126 ? A GLU 2126 
1483 1 Y 1 A GLY 2390 ? A GLY 2390 
1484 1 Y 1 A GLU 2391 ? A GLU 2391 
1485 1 Y 1 A ASP 2392 ? A ASP 2392 
1486 1 Y 1 A GLU 2393 ? A GLU 2393 
1487 1 Y 1 A ALA 2394 ? A ALA 2394 
1488 1 Y 1 A GLN 2395 ? A GLN 2395 
1489 1 Y 1 A ARG 2396 ? A ARG 2396 
1490 1 Y 1 A ARG 2397 ? A ARG 2397 
1491 1 Y 1 A ARG 2398 ? A ARG 2398 
1492 1 Y 1 A LYS 2399 ? A LYS 2399 
1493 1 Y 1 A GLY 2400 ? A GLY 2400 
1494 1 Y 1 A LYS 2401 ? A LYS 2401 
1495 1 Y 1 A GLU 2402 ? A GLU 2402 
1496 1 Y 1 A ASP 2403 ? A ASP 2403 
1497 1 Y 1 A GLU 2404 ? A GLU 2404 
1498 1 Y 1 A GLY 2405 ? A GLY 2405 
1499 1 Y 1 A GLU 2406 ? A GLU 2406 
1500 1 Y 1 A GLU 2407 ? A GLU 2407 
1501 1 Y 1 A ALA 2408 ? A ALA 2408 
1502 1 Y 1 A ALA 2409 ? A ALA 2409 
1503 1 Y 1 A ASP 3221 ? A ASP 3221 
1504 1 Y 1 A LEU 3222 ? A LEU 3222 
1505 1 Y 1 A ARG 3223 ? A ARG 3223 
1506 1 Y 1 A ILE 3224 ? A ILE 3224 
1507 1 Y 1 A LYS 3225 ? A LYS 3225 
1508 1 Y 1 A SER 3226 ? A SER 3226 
1509 1 Y 1 A GLN 3227 ? A GLN 3227 
1510 1 Y 1 A GLU 3228 ? A GLU 3228 
1511 1 Y 1 A LEU 3229 ? A LEU 3229 
1512 1 Y 1 A GLU 3230 ? A GLU 3230 
1513 1 Y 1 A VAL 3231 ? A VAL 3231 
1514 1 Y 1 A LYS 3232 ? A LYS 3232 
1515 1 Y 1 A ASN 3233 ? A ASN 3233 
1516 1 Y 1 A ALA 3234 ? A ALA 3234 
1517 1 Y 1 A ALA 3235 ? A ALA 3235 
1518 1 Y 1 A ALA 3236 ? A ALA 3236 
1519 1 Y 1 A ASN 3237 ? A ASN 3237 
1520 1 Y 1 A ASP 3238 ? A ASP 3238 
1521 1 Y 1 A LYS 3239 ? A LYS 3239 
1522 1 Y 1 A LEU 3240 ? A LEU 3240 
1523 1 Y 1 A LYS 3241 ? A LYS 3241 
1524 1 Y 1 A LYS 3242 ? A LYS 3242 
1525 1 Y 1 A MET 3243 ? A MET 3243 
1526 1 Y 1 A VAL 3244 ? A VAL 3244 
1527 1 Y 1 A LYS 3245 ? A LYS 3245 
1528 1 Y 1 A ASP 3246 ? A ASP 3246 
1529 1 Y 1 A GLN 3247 ? A GLN 3247 
1530 1 Y 1 A GLN 3248 ? A GLN 3248 
1531 1 Y 1 A GLU 3249 ? A GLU 3249 
1532 1 Y 1 A ALA 3250 ? A ALA 3250 
1533 1 Y 1 A GLU 3251 ? A GLU 3251 
1534 1 Y 1 A LYS 3252 ? A LYS 3252 
1535 1 Y 1 A LYS 3253 ? A LYS 3253 
1536 1 Y 1 A LYS 3254 ? A LYS 3254 
1537 1 Y 1 A VAL 3255 ? A VAL 3255 
1538 1 Y 1 A MET 3256 ? A MET 3256 
1539 1 Y 1 A SER 3257 ? A SER 3257 
1540 1 Y 1 A GLN 3258 ? A GLN 3258 
1541 1 Y 1 A GLU 3259 ? A GLU 3259 
1542 1 Y 1 A ILE 3260 ? A ILE 3260 
1543 1 Y 1 A GLN 3261 ? A GLN 3261 
1544 1 Y 1 A GLU 3262 ? A GLU 3262 
1545 1 Y 1 A GLN 3263 ? A GLN 3263 
1546 1 Y 1 A LEU 3264 ? A LEU 3264 
1547 1 Y 1 A HIS 3265 ? A HIS 3265 
1548 1 Y 1 A LYS 3266 ? A LYS 3266 
1549 1 Y 1 A GLN 3267 ? A GLN 3267 
1550 1 Y 1 A GLN 3268 ? A GLN 3268 
1551 1 Y 1 A GLU 3269 ? A GLU 3269 
1552 1 Y 1 A VAL 3270 ? A VAL 3270 
1553 1 Y 1 A ILE 3271 ? A ILE 3271 
1554 1 Y 1 A ALA 3272 ? A ALA 3272 
1555 1 Y 1 A ASP 3273 ? A ASP 3273 
1556 1 Y 1 A LYS 3274 ? A LYS 3274 
1557 1 Y 1 A GLN 3275 ? A GLN 3275 
1558 1 Y 1 A MET 3276 ? A MET 3276 
1559 1 Y 1 A SER 3277 ? A SER 3277 
1560 1 Y 1 A VAL 3278 ? A VAL 3278 
1561 1 Y 1 A LYS 3279 ? A LYS 3279 
1562 1 Y 1 A GLU 3280 ? A GLU 3280 
1563 1 Y 1 A ASP 3281 ? A ASP 3281 
1564 1 Y 1 A LEU 3282 ? A LEU 3282 
1565 1 Y 1 A ASP 3283 ? A ASP 3283 
1566 1 Y 1 A LYS 3284 ? A LYS 3284 
1567 1 Y 1 A VAL 3285 ? A VAL 3285 
1568 1 Y 1 A GLU 3286 ? A GLU 3286 
1569 1 Y 1 A PRO 3287 ? A PRO 3287 
1570 1 Y 1 A ALA 3288 ? A ALA 3288 
1571 1 Y 1 A VAL 3289 ? A VAL 3289 
1572 1 Y 1 A ILE 3290 ? A ILE 3290 
1573 1 Y 1 A GLU 3291 ? A GLU 3291 
1574 1 Y 1 A ALA 3292 ? A ALA 3292 
1575 1 Y 1 A GLN 3293 ? A GLN 3293 
1576 1 Y 1 A ASN 3294 ? A ASN 3294 
1577 1 Y 1 A ALA 3295 ? A ALA 3295 
1578 1 Y 1 A VAL 3296 ? A VAL 3296 
1579 1 Y 1 A LYS 3297 ? A LYS 3297 
1580 1 Y 1 A SER 3298 ? A SER 3298 
1581 1 Y 1 A ILE 3299 ? A ILE 3299 
1582 1 Y 1 A LYS 3300 ? A LYS 3300 
1583 1 Y 1 A LYS 3301 ? A LYS 3301 
1584 1 Y 1 A GLN 3302 ? A GLN 3302 
1585 1 Y 1 A HIS 3303 ? A HIS 3303 
1586 1 Y 1 A LEU 3304 ? A LEU 3304 
1587 1 Y 1 A VAL 3305 ? A VAL 3305 
1588 1 Y 1 A GLU 3306 ? A GLU 3306 
1589 1 Y 1 A VAL 3307 ? A VAL 3307 
1590 1 Y 1 A ARG 3308 ? A ARG 3308 
1591 1 Y 1 A SER 3309 ? A SER 3309 
1592 1 Y 1 A MET 3310 ? A MET 3310 
1593 1 Y 1 A ALA 3311 ? A ALA 3311 
1594 1 Y 1 A ASN 3312 ? A ASN 3312 
1595 1 Y 1 A PRO 3313 ? A PRO 3313 
1596 1 Y 1 A PRO 3314 ? A PRO 3314 
1597 1 Y 1 A ALA 3315 ? A ALA 3315 
1598 1 Y 1 A ALA 3316 ? A ALA 3316 
1599 1 Y 1 A VAL 3317 ? A VAL 3317 
1600 1 Y 1 A LYS 3318 ? A LYS 3318 
1601 1 Y 1 A LEU 3319 ? A LEU 3319 
1602 1 Y 1 A ALA 3320 ? A ALA 3320 
1603 1 Y 1 A LEU 3321 ? A LEU 3321 
1604 1 Y 1 A GLU 3322 ? A GLU 3322 
1605 1 Y 1 A SER 3323 ? A SER 3323 
1606 1 Y 1 A ILE 3324 ? A ILE 3324 
1607 1 Y 1 A CYS 3325 ? A CYS 3325 
1608 1 Y 1 A LEU 3326 ? A LEU 3326 
1609 1 Y 1 A LEU 3327 ? A LEU 3327 
1610 1 Y 1 A LEU 3328 ? A LEU 3328 
1611 1 Y 1 A GLY 3329 ? A GLY 3329 
1612 1 Y 1 A GLU 3330 ? A GLU 3330 
1613 1 Y 1 A SER 3331 ? A SER 3331 
1614 1 Y 1 A THR 3332 ? A THR 3332 
1615 1 Y 1 A THR 3333 ? A THR 3333 
1616 1 Y 1 A ASP 3334 ? A ASP 3334 
1617 1 Y 1 A TRP 3335 ? A TRP 3335 
1618 1 Y 1 A LYS 3336 ? A LYS 3336 
1619 1 Y 1 A GLN 3337 ? A GLN 3337 
1620 1 Y 1 A ILE 3338 ? A ILE 3338 
1621 1 Y 1 A ARG 3339 ? A ARG 3339 
1622 1 Y 1 A SER 3340 ? A SER 3340 
1623 1 Y 1 A ILE 3341 ? A ILE 3341 
1624 1 Y 1 A ILE 3342 ? A ILE 3342 
1625 1 Y 1 A MET 3343 ? A MET 3343 
1626 1 Y 1 A ARG 3344 ? A ARG 3344 
1627 1 Y 1 A GLU 3345 ? A GLU 3345 
1628 1 Y 1 A ASN 3346 ? A ASN 3346 
1629 1 Y 1 A PHE 3347 ? A PHE 3347 
1630 1 Y 1 A ILE 3348 ? A ILE 3348 
1631 1 Y 1 A PRO 3349 ? A PRO 3349 
1632 1 Y 1 A THR 3350 ? A THR 3350 
1633 1 Y 1 A ILE 3351 ? A ILE 3351 
1634 1 Y 1 A VAL 3352 ? A VAL 3352 
1635 1 Y 1 A ASN 3353 ? A ASN 3353 
1636 1 Y 1 A PHE 3354 ? A PHE 3354 
1637 1 Y 1 A SER 3355 ? A SER 3355 
1638 1 Y 1 A ALA 3356 ? A ALA 3356 
1639 1 Y 1 A GLU 3357 ? A GLU 3357 
1640 1 Y 1 A GLU 3358 ? A GLU 3358 
1641 1 Y 1 A ILE 3359 ? A ILE 3359 
1642 1 Y 1 A SER 3360 ? A SER 3360 
1643 1 Y 1 A ASP 3361 ? A ASP 3361 
1644 1 Y 1 A ALA 3362 ? A ALA 3362 
1645 1 Y 1 A ILE 3363 ? A ILE 3363 
1646 1 Y 1 A ARG 3364 ? A ARG 3364 
1647 1 Y 1 A GLU 3365 ? A GLU 3365 
1648 1 Y 1 A LYS 3366 ? A LYS 3366 
1649 1 Y 1 A MET 3367 ? A MET 3367 
1650 1 Y 1 A LYS 3368 ? A LYS 3368 
1651 1 Y 1 A LYS 3369 ? A LYS 3369 
1652 1 Y 1 A ASN 3370 ? A ASN 3370 
1653 1 Y 1 A TYR 3371 ? A TYR 3371 
1654 1 Y 1 A MET 3372 ? A MET 3372 
1655 1 Y 1 A SER 3373 ? A SER 3373 
1656 1 Y 1 A ASN 3374 ? A ASN 3374 
1657 1 Y 1 A PRO 3375 ? A PRO 3375 
1658 1 Y 1 A SER 3376 ? A SER 3376 
1659 1 Y 1 A TYR 3377 ? A TYR 3377 
1660 1 Y 1 A ASN 3378 ? A ASN 3378 
1661 1 Y 1 A TYR 3379 ? A TYR 3379 
1662 1 Y 1 A GLU 3380 ? A GLU 3380 
1663 1 Y 1 A ILE 3381 ? A ILE 3381 
1664 1 Y 1 A VAL 3382 ? A VAL 3382 
1665 1 Y 1 A ASN 3383 ? A ASN 3383 
1666 1 Y 1 A ARG 3384 ? A ARG 3384 
1667 1 Y 1 A ALA 3385 ? A ALA 3385 
1668 1 Y 1 A SER 3386 ? A SER 3386 
1669 1 Y 1 A LEU 3387 ? A LEU 3387 
1670 1 Y 1 A ALA 3388 ? A ALA 3388 
1671 1 Y 1 A CYS 3389 ? A CYS 3389 
1672 1 Y 1 A GLY 3390 ? A GLY 3390 
1673 1 Y 1 A PRO 3391 ? A PRO 3391 
1674 1 Y 1 A MET 3392 ? A MET 3392 
1675 1 Y 1 A VAL 3393 ? A VAL 3393 
1676 1 Y 1 A LYS 3394 ? A LYS 3394 
1677 1 Y 1 A TRP 3395 ? A TRP 3395 
1678 1 Y 1 A ALA 3396 ? A ALA 3396 
1679 1 Y 1 A ILE 3397 ? A ILE 3397 
1680 1 Y 1 A ALA 3398 ? A ALA 3398 
1681 1 Y 1 A GLN 3399 ? A GLN 3399 
1682 1 Y 1 A LEU 3400 ? A LEU 3400 
1683 1 Y 1 A ASN 3401 ? A ASN 3401 
1684 1 Y 1 A TYR 3402 ? A TYR 3402 
1685 1 Y 1 A ALA 3403 ? A ALA 3403 
1686 1 Y 1 A ASP 3404 ? A ASP 3404 
1687 1 Y 1 A MET 3405 ? A MET 3405 
1688 1 Y 1 A LEU 3406 ? A LEU 3406 
1689 1 Y 1 A LYS 3407 ? A LYS 3407 
1690 1 Y 1 A ARG 3408 ? A ARG 3408 
1691 1 Y 1 A VAL 3409 ? A VAL 3409 
1692 1 Y 1 A GLU 3410 ? A GLU 3410 
1693 1 Y 1 A PRO 3411 ? A PRO 3411 
1694 1 Y 1 A LEU 3412 ? A LEU 3412 
1695 1 Y 1 A ARG 3413 ? A ARG 3413 
1696 1 Y 1 A ASN 3414 ? A ASN 3414 
1697 1 Y 1 A GLU 3415 ? A GLU 3415 
1698 1 Y 1 A LEU 3416 ? A LEU 3416 
1699 1 Y 1 A GLN 3417 ? A GLN 3417 
1700 1 Y 1 A LYS 3418 ? A LYS 3418 
1701 1 Y 1 A LEU 3419 ? A LEU 3419 
1702 1 Y 1 A GLU 3420 ? A GLU 3420 
1703 1 Y 1 A ASP 3421 ? A ASP 3421 
1704 1 Y 1 A ASP 3422 ? A ASP 3422 
1705 1 Y 1 A ALA 3423 ? A ALA 3423 
1706 1 Y 1 A LYS 3424 ? A LYS 3424 
1707 1 Y 1 A ASP 3425 ? A ASP 3425 
1708 1 Y 1 A ASN 3426 ? A ASN 3426 
1709 1 Y 1 A GLN 3427 ? A GLN 3427 
1710 1 Y 1 A GLN 3428 ? A GLN 3428 
1711 1 Y 1 A LYS 3429 ? A LYS 3429 
1712 1 Y 1 A ALA 3430 ? A ALA 3430 
1713 1 Y 1 A ASN 3431 ? A ASN 3431 
1714 1 Y 1 A GLU 3432 ? A GLU 3432 
1715 1 Y 1 A VAL 3433 ? A VAL 3433 
1716 1 Y 1 A GLU 3434 ? A GLU 3434 
1717 1 Y 1 A GLN 3435 ? A GLN 3435 
1718 1 Y 1 A MET 3436 ? A MET 3436 
1719 1 Y 1 A ILE 3437 ? A ILE 3437 
1720 1 Y 1 A ARG 3438 ? A ARG 3438 
1721 1 Y 1 A ASP 3439 ? A ASP 3439 
1722 1 Y 1 A LEU 3440 ? A LEU 3440 
1723 1 Y 1 A GLU 3441 ? A GLU 3441 
1724 1 Y 1 A ALA 3442 ? A ALA 3442 
1725 1 Y 1 A SER 3443 ? A SER 3443 
1726 1 Y 1 A ILE 3444 ? A ILE 3444 
1727 1 Y 1 A ALA 3445 ? A ALA 3445 
1728 1 Y 1 A ARG 3446 ? A ARG 3446 
1729 1 Y 1 A TYR 3447 ? A TYR 3447 
1730 1 Y 1 A LYS 3448 ? A LYS 3448 
1731 1 Y 1 A GLU 3449 ? A GLU 3449 
1732 1 Y 1 A GLU 3450 ? A GLU 3450 
1733 1 Y 1 A TYR 3451 ? A TYR 3451 
1734 1 Y 1 A ALA 3452 ? A ALA 3452 
1735 1 Y 1 A VAL 3453 ? A VAL 3453 
1736 1 Y 1 A LEU 3454 ? A LEU 3454 
1737 1 Y 1 A ILE 3455 ? A ILE 3455 
1738 1 Y 1 A SER 3456 ? A SER 3456 
1739 1 Y 1 A GLU 3457 ? A GLU 3457 
1740 1 Y 1 A ALA 3458 ? A ALA 3458 
1741 1 Y 1 A GLN 3459 ? A GLN 3459 
1742 1 Y 1 A ALA 3460 ? A ALA 3460 
1743 1 Y 1 A ILE 3461 ? A ILE 3461 
1744 1 Y 1 A LYS 3462 ? A LYS 3462 
1745 1 Y 1 A ALA 3463 ? A ALA 3463 
1746 1 Y 1 A ASP 3464 ? A ASP 3464 
1747 1 Y 1 A LEU 3465 ? A LEU 3465 
1748 1 Y 1 A ALA 3466 ? A ALA 3466 
1749 1 Y 1 A ALA 3467 ? A ALA 3467 
1750 1 Y 1 A VAL 3468 ? A VAL 3468 
1751 1 Y 1 A GLU 3469 ? A GLU 3469 
1752 1 Y 1 A ALA 3470 ? A ALA 3470 
1753 1 Y 1 A MET 4348 ? A MET 4348 
1754 1 Y 1 A LEU 4349 ? A LEU 4349 
1755 1 Y 1 A GLU 4350 ? A GLU 4350 
1756 1 Y 1 A ASP 4351 ? A ASP 4351 
1757 1 Y 1 A GLU 4352 ? A GLU 4352 
1758 1 Y 1 A ASP 4353 ? A ASP 4353 
1759 1 Y 1 A ASP 4354 ? A ASP 4354 
1760 1 Y 1 A LEU 4355 ? A LEU 4355 
1761 1 Y 1 A ALA 4356 ? A ALA 4356 
1762 1 Y 1 A TYR 4357 ? A TYR 4357 
1763 1 Y 1 A ALA 4358 ? A ALA 4358 
1764 1 Y 1 A GLU 4359 ? A GLU 4359 
1765 1 Y 1 A THR 4360 ? A THR 4360 
1766 1 Y 1 A GLU 4361 ? A GLU 4361 
1767 1 Y 1 A LYS 4362 ? A LYS 4362 
1768 1 Y 1 A LYS 4363 ? A LYS 4363 
1769 1 Y 1 A THR 4364 ? A THR 4364 
1770 1 Y 1 A ARG 4365 ? A ARG 4365 
1771 1 Y 1 A THR 4366 ? A THR 4366 
1772 1 Y 1 A ASP 4367 ? A ASP 4367 
1773 1 Y 1 A SER 4368 ? A SER 4368 
1774 1 Y 1 A THR 4369 ? A THR 4369 
1775 1 Y 1 A SER 4370 ? A SER 4370 
1776 1 Y 1 A ASP 4371 ? A ASP 4371 
1777 1 Y 1 A GLY 4372 ? A GLY 4372 
1778 1 Y 1 A ARG 4373 ? A ARG 4373 
1779 1 Y 1 A PRO 4374 ? A PRO 4374 
1780 1 Y 1 A GLU 4646 ? A GLU 4646 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ADP PB     P N N 1   
ADP O1B    O N N 2   
ADP O2B    O N N 3   
ADP O3B    O N N 4   
ADP PA     P N S 5   
ADP O1A    O N N 6   
ADP O2A    O N N 7   
ADP O3A    O N N 8   
ADP "O5'"  O N N 9   
ADP "C5'"  C N N 10  
ADP "C4'"  C N R 11  
ADP "O4'"  O N N 12  
ADP "C3'"  C N S 13  
ADP "O3'"  O N N 14  
ADP "C2'"  C N R 15  
ADP "O2'"  O N N 16  
ADP "C1'"  C N R 17  
ADP N9     N Y N 18  
ADP C8     C Y N 19  
ADP N7     N Y N 20  
ADP C5     C Y N 21  
ADP C6     C Y N 22  
ADP N6     N N N 23  
ADP N1     N Y N 24  
ADP C2     C Y N 25  
ADP N3     N Y N 26  
ADP C4     C Y N 27  
ADP HOB2   H N N 28  
ADP HOB3   H N N 29  
ADP HOA2   H N N 30  
ADP "H5'1" H N N 31  
ADP "H5'2" H N N 32  
ADP "H4'"  H N N 33  
ADP "H3'"  H N N 34  
ADP "HO3'" H N N 35  
ADP "H2'"  H N N 36  
ADP "HO2'" H N N 37  
ADP "H1'"  H N N 38  
ADP H8     H N N 39  
ADP HN61   H N N 40  
ADP HN62   H N N 41  
ADP H2     H N N 42  
ALA N      N N N 43  
ALA CA     C N S 44  
ALA C      C N N 45  
ALA O      O N N 46  
ALA CB     C N N 47  
ALA OXT    O N N 48  
ALA H      H N N 49  
ALA H2     H N N 50  
ALA HA     H N N 51  
ALA HB1    H N N 52  
ALA HB2    H N N 53  
ALA HB3    H N N 54  
ALA HXT    H N N 55  
ARG N      N N N 56  
ARG CA     C N S 57  
ARG C      C N N 58  
ARG O      O N N 59  
ARG CB     C N N 60  
ARG CG     C N N 61  
ARG CD     C N N 62  
ARG NE     N N N 63  
ARG CZ     C N N 64  
ARG NH1    N N N 65  
ARG NH2    N N N 66  
ARG OXT    O N N 67  
ARG H      H N N 68  
ARG H2     H N N 69  
ARG HA     H N N 70  
ARG HB2    H N N 71  
ARG HB3    H N N 72  
ARG HG2    H N N 73  
ARG HG3    H N N 74  
ARG HD2    H N N 75  
ARG HD3    H N N 76  
ARG HE     H N N 77  
ARG HH11   H N N 78  
ARG HH12   H N N 79  
ARG HH21   H N N 80  
ARG HH22   H N N 81  
ARG HXT    H N N 82  
ASN N      N N N 83  
ASN CA     C N S 84  
ASN C      C N N 85  
ASN O      O N N 86  
ASN CB     C N N 87  
ASN CG     C N N 88  
ASN OD1    O N N 89  
ASN ND2    N N N 90  
ASN OXT    O N N 91  
ASN H      H N N 92  
ASN H2     H N N 93  
ASN HA     H N N 94  
ASN HB2    H N N 95  
ASN HB3    H N N 96  
ASN HD21   H N N 97  
ASN HD22   H N N 98  
ASN HXT    H N N 99  
ASP N      N N N 100 
ASP CA     C N S 101 
ASP C      C N N 102 
ASP O      O N N 103 
ASP CB     C N N 104 
ASP CG     C N N 105 
ASP OD1    O N N 106 
ASP OD2    O N N 107 
ASP OXT    O N N 108 
ASP H      H N N 109 
ASP H2     H N N 110 
ASP HA     H N N 111 
ASP HB2    H N N 112 
ASP HB3    H N N 113 
ASP HD2    H N N 114 
ASP HXT    H N N 115 
ATP PG     P N N 116 
ATP O1G    O N N 117 
ATP O2G    O N N 118 
ATP O3G    O N N 119 
ATP PB     P N R 120 
ATP O1B    O N N 121 
ATP O2B    O N N 122 
ATP O3B    O N N 123 
ATP PA     P N R 124 
ATP O1A    O N N 125 
ATP O2A    O N N 126 
ATP O3A    O N N 127 
ATP "O5'"  O N N 128 
ATP "C5'"  C N N 129 
ATP "C4'"  C N R 130 
ATP "O4'"  O N N 131 
ATP "C3'"  C N S 132 
ATP "O3'"  O N N 133 
ATP "C2'"  C N R 134 
ATP "O2'"  O N N 135 
ATP "C1'"  C N R 136 
ATP N9     N Y N 137 
ATP C8     C Y N 138 
ATP N7     N Y N 139 
ATP C5     C Y N 140 
ATP C6     C Y N 141 
ATP N6     N N N 142 
ATP N1     N Y N 143 
ATP C2     C Y N 144 
ATP N3     N Y N 145 
ATP C4     C Y N 146 
ATP HOG2   H N N 147 
ATP HOG3   H N N 148 
ATP HOB2   H N N 149 
ATP HOA2   H N N 150 
ATP "H5'1" H N N 151 
ATP "H5'2" H N N 152 
ATP "H4'"  H N N 153 
ATP "H3'"  H N N 154 
ATP "HO3'" H N N 155 
ATP "H2'"  H N N 156 
ATP "HO2'" H N N 157 
ATP "H1'"  H N N 158 
ATP H8     H N N 159 
ATP HN61   H N N 160 
ATP HN62   H N N 161 
ATP H2     H N N 162 
CYS N      N N N 163 
CYS CA     C N R 164 
CYS C      C N N 165 
CYS O      O N N 166 
CYS CB     C N N 167 
CYS SG     S N N 168 
CYS OXT    O N N 169 
CYS H      H N N 170 
CYS H2     H N N 171 
CYS HA     H N N 172 
CYS HB2    H N N 173 
CYS HB3    H N N 174 
CYS HG     H N N 175 
CYS HXT    H N N 176 
GLN N      N N N 177 
GLN CA     C N S 178 
GLN C      C N N 179 
GLN O      O N N 180 
GLN CB     C N N 181 
GLN CG     C N N 182 
GLN CD     C N N 183 
GLN OE1    O N N 184 
GLN NE2    N N N 185 
GLN OXT    O N N 186 
GLN H      H N N 187 
GLN H2     H N N 188 
GLN HA     H N N 189 
GLN HB2    H N N 190 
GLN HB3    H N N 191 
GLN HG2    H N N 192 
GLN HG3    H N N 193 
GLN HE21   H N N 194 
GLN HE22   H N N 195 
GLN HXT    H N N 196 
GLU N      N N N 197 
GLU CA     C N S 198 
GLU C      C N N 199 
GLU O      O N N 200 
GLU CB     C N N 201 
GLU CG     C N N 202 
GLU CD     C N N 203 
GLU OE1    O N N 204 
GLU OE2    O N N 205 
GLU OXT    O N N 206 
GLU H      H N N 207 
GLU H2     H N N 208 
GLU HA     H N N 209 
GLU HB2    H N N 210 
GLU HB3    H N N 211 
GLU HG2    H N N 212 
GLU HG3    H N N 213 
GLU HE2    H N N 214 
GLU HXT    H N N 215 
GLY N      N N N 216 
GLY CA     C N N 217 
GLY C      C N N 218 
GLY O      O N N 219 
GLY OXT    O N N 220 
GLY H      H N N 221 
GLY H2     H N N 222 
GLY HA2    H N N 223 
GLY HA3    H N N 224 
GLY HXT    H N N 225 
HIS N      N N N 226 
HIS CA     C N S 227 
HIS C      C N N 228 
HIS O      O N N 229 
HIS CB     C N N 230 
HIS CG     C Y N 231 
HIS ND1    N Y N 232 
HIS CD2    C Y N 233 
HIS CE1    C Y N 234 
HIS NE2    N Y N 235 
HIS OXT    O N N 236 
HIS H      H N N 237 
HIS H2     H N N 238 
HIS HA     H N N 239 
HIS HB2    H N N 240 
HIS HB3    H N N 241 
HIS HD1    H N N 242 
HIS HD2    H N N 243 
HIS HE1    H N N 244 
HIS HE2    H N N 245 
HIS HXT    H N N 246 
ILE N      N N N 247 
ILE CA     C N S 248 
ILE C      C N N 249 
ILE O      O N N 250 
ILE CB     C N S 251 
ILE CG1    C N N 252 
ILE CG2    C N N 253 
ILE CD1    C N N 254 
ILE OXT    O N N 255 
ILE H      H N N 256 
ILE H2     H N N 257 
ILE HA     H N N 258 
ILE HB     H N N 259 
ILE HG12   H N N 260 
ILE HG13   H N N 261 
ILE HG21   H N N 262 
ILE HG22   H N N 263 
ILE HG23   H N N 264 
ILE HD11   H N N 265 
ILE HD12   H N N 266 
ILE HD13   H N N 267 
ILE HXT    H N N 268 
LEU N      N N N 269 
LEU CA     C N S 270 
LEU C      C N N 271 
LEU O      O N N 272 
LEU CB     C N N 273 
LEU CG     C N N 274 
LEU CD1    C N N 275 
LEU CD2    C N N 276 
LEU OXT    O N N 277 
LEU H      H N N 278 
LEU H2     H N N 279 
LEU HA     H N N 280 
LEU HB2    H N N 281 
LEU HB3    H N N 282 
LEU HG     H N N 283 
LEU HD11   H N N 284 
LEU HD12   H N N 285 
LEU HD13   H N N 286 
LEU HD21   H N N 287 
LEU HD22   H N N 288 
LEU HD23   H N N 289 
LEU HXT    H N N 290 
LYS N      N N N 291 
LYS CA     C N S 292 
LYS C      C N N 293 
LYS O      O N N 294 
LYS CB     C N N 295 
LYS CG     C N N 296 
LYS CD     C N N 297 
LYS CE     C N N 298 
LYS NZ     N N N 299 
LYS OXT    O N N 300 
LYS H      H N N 301 
LYS H2     H N N 302 
LYS HA     H N N 303 
LYS HB2    H N N 304 
LYS HB3    H N N 305 
LYS HG2    H N N 306 
LYS HG3    H N N 307 
LYS HD2    H N N 308 
LYS HD3    H N N 309 
LYS HE2    H N N 310 
LYS HE3    H N N 311 
LYS HZ1    H N N 312 
LYS HZ2    H N N 313 
LYS HZ3    H N N 314 
LYS HXT    H N N 315 
MET N      N N N 316 
MET CA     C N S 317 
MET C      C N N 318 
MET O      O N N 319 
MET CB     C N N 320 
MET CG     C N N 321 
MET SD     S N N 322 
MET CE     C N N 323 
MET OXT    O N N 324 
MET H      H N N 325 
MET H2     H N N 326 
MET HA     H N N 327 
MET HB2    H N N 328 
MET HB3    H N N 329 
MET HG2    H N N 330 
MET HG3    H N N 331 
MET HE1    H N N 332 
MET HE2    H N N 333 
MET HE3    H N N 334 
MET HXT    H N N 335 
PHE N      N N N 336 
PHE CA     C N S 337 
PHE C      C N N 338 
PHE O      O N N 339 
PHE CB     C N N 340 
PHE CG     C Y N 341 
PHE CD1    C Y N 342 
PHE CD2    C Y N 343 
PHE CE1    C Y N 344 
PHE CE2    C Y N 345 
PHE CZ     C Y N 346 
PHE OXT    O N N 347 
PHE H      H N N 348 
PHE H2     H N N 349 
PHE HA     H N N 350 
PHE HB2    H N N 351 
PHE HB3    H N N 352 
PHE HD1    H N N 353 
PHE HD2    H N N 354 
PHE HE1    H N N 355 
PHE HE2    H N N 356 
PHE HZ     H N N 357 
PHE HXT    H N N 358 
PRO N      N N N 359 
PRO CA     C N S 360 
PRO C      C N N 361 
PRO O      O N N 362 
PRO CB     C N N 363 
PRO CG     C N N 364 
PRO CD     C N N 365 
PRO OXT    O N N 366 
PRO H      H N N 367 
PRO HA     H N N 368 
PRO HB2    H N N 369 
PRO HB3    H N N 370 
PRO HG2    H N N 371 
PRO HG3    H N N 372 
PRO HD2    H N N 373 
PRO HD3    H N N 374 
PRO HXT    H N N 375 
SER N      N N N 376 
SER CA     C N S 377 
SER C      C N N 378 
SER O      O N N 379 
SER CB     C N N 380 
SER OG     O N N 381 
SER OXT    O N N 382 
SER H      H N N 383 
SER H2     H N N 384 
SER HA     H N N 385 
SER HB2    H N N 386 
SER HB3    H N N 387 
SER HG     H N N 388 
SER HXT    H N N 389 
THR N      N N N 390 
THR CA     C N S 391 
THR C      C N N 392 
THR O      O N N 393 
THR CB     C N R 394 
THR OG1    O N N 395 
THR CG2    C N N 396 
THR OXT    O N N 397 
THR H      H N N 398 
THR H2     H N N 399 
THR HA     H N N 400 
THR HB     H N N 401 
THR HG1    H N N 402 
THR HG21   H N N 403 
THR HG22   H N N 404 
THR HG23   H N N 405 
THR HXT    H N N 406 
TRP N      N N N 407 
TRP CA     C N S 408 
TRP C      C N N 409 
TRP O      O N N 410 
TRP CB     C N N 411 
TRP CG     C Y N 412 
TRP CD1    C Y N 413 
TRP CD2    C Y N 414 
TRP NE1    N Y N 415 
TRP CE2    C Y N 416 
TRP CE3    C Y N 417 
TRP CZ2    C Y N 418 
TRP CZ3    C Y N 419 
TRP CH2    C Y N 420 
TRP OXT    O N N 421 
TRP H      H N N 422 
TRP H2     H N N 423 
TRP HA     H N N 424 
TRP HB2    H N N 425 
TRP HB3    H N N 426 
TRP HD1    H N N 427 
TRP HE1    H N N 428 
TRP HE3    H N N 429 
TRP HZ2    H N N 430 
TRP HZ3    H N N 431 
TRP HH2    H N N 432 
TRP HXT    H N N 433 
TYR N      N N N 434 
TYR CA     C N S 435 
TYR C      C N N 436 
TYR O      O N N 437 
TYR CB     C N N 438 
TYR CG     C Y N 439 
TYR CD1    C Y N 440 
TYR CD2    C Y N 441 
TYR CE1    C Y N 442 
TYR CE2    C Y N 443 
TYR CZ     C Y N 444 
TYR OH     O N N 445 
TYR OXT    O N N 446 
TYR H      H N N 447 
TYR H2     H N N 448 
TYR HA     H N N 449 
TYR HB2    H N N 450 
TYR HB3    H N N 451 
TYR HD1    H N N 452 
TYR HD2    H N N 453 
TYR HE1    H N N 454 
TYR HE2    H N N 455 
TYR HH     H N N 456 
TYR HXT    H N N 457 
VAL N      N N N 458 
VAL CA     C N S 459 
VAL C      C N N 460 
VAL O      O N N 461 
VAL CB     C N N 462 
VAL CG1    C N N 463 
VAL CG2    C N N 464 
VAL OXT    O N N 465 
VAL H      H N N 466 
VAL H2     H N N 467 
VAL HA     H N N 468 
VAL HB     H N N 469 
VAL HG11   H N N 470 
VAL HG12   H N N 471 
VAL HG13   H N N 472 
VAL HG21   H N N 473 
VAL HG22   H N N 474 
VAL HG23   H N N 475 
VAL HXT    H N N 476 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
ATP PG    O1G    doub N N 114 
ATP PG    O2G    sing N N 115 
ATP PG    O3G    sing N N 116 
ATP PG    O3B    sing N N 117 
ATP O2G   HOG2   sing N N 118 
ATP O3G   HOG3   sing N N 119 
ATP PB    O1B    doub N N 120 
ATP PB    O2B    sing N N 121 
ATP PB    O3B    sing N N 122 
ATP PB    O3A    sing N N 123 
ATP O2B   HOB2   sing N N 124 
ATP PA    O1A    doub N N 125 
ATP PA    O2A    sing N N 126 
ATP PA    O3A    sing N N 127 
ATP PA    "O5'"  sing N N 128 
ATP O2A   HOA2   sing N N 129 
ATP "O5'" "C5'"  sing N N 130 
ATP "C5'" "C4'"  sing N N 131 
ATP "C5'" "H5'1" sing N N 132 
ATP "C5'" "H5'2" sing N N 133 
ATP "C4'" "O4'"  sing N N 134 
ATP "C4'" "C3'"  sing N N 135 
ATP "C4'" "H4'"  sing N N 136 
ATP "O4'" "C1'"  sing N N 137 
ATP "C3'" "O3'"  sing N N 138 
ATP "C3'" "C2'"  sing N N 139 
ATP "C3'" "H3'"  sing N N 140 
ATP "O3'" "HO3'" sing N N 141 
ATP "C2'" "O2'"  sing N N 142 
ATP "C2'" "C1'"  sing N N 143 
ATP "C2'" "H2'"  sing N N 144 
ATP "O2'" "HO2'" sing N N 145 
ATP "C1'" N9     sing N N 146 
ATP "C1'" "H1'"  sing N N 147 
ATP N9    C8     sing Y N 148 
ATP N9    C4     sing Y N 149 
ATP C8    N7     doub Y N 150 
ATP C8    H8     sing N N 151 
ATP N7    C5     sing Y N 152 
ATP C5    C6     sing Y N 153 
ATP C5    C4     doub Y N 154 
ATP C6    N6     sing N N 155 
ATP C6    N1     doub Y N 156 
ATP N6    HN61   sing N N 157 
ATP N6    HN62   sing N N 158 
ATP N1    C2     sing Y N 159 
ATP C2    N3     doub Y N 160 
ATP C2    H2     sing N N 161 
ATP N3    C4     sing Y N 162 
CYS N     CA     sing N N 163 
CYS N     H      sing N N 164 
CYS N     H2     sing N N 165 
CYS CA    C      sing N N 166 
CYS CA    CB     sing N N 167 
CYS CA    HA     sing N N 168 
CYS C     O      doub N N 169 
CYS C     OXT    sing N N 170 
CYS CB    SG     sing N N 171 
CYS CB    HB2    sing N N 172 
CYS CB    HB3    sing N N 173 
CYS SG    HG     sing N N 174 
CYS OXT   HXT    sing N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-02 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BN3 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'The alpha registry-locked dynein motor domain mutant in 5mM ATP condition, class1' 
# 
_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 ? ? EPU       ? 
# 
_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                    9BN3 
_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 
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     . LEU A 1 1463 ? 243.954 193.802 181.879 1.00 43.51 ? 1463 LEU A N     1 
ATOM   2     C CA    . LEU A 1 1463 ? 245.309 193.828 182.418 1.00 45.07 ? 1463 LEU A CA    1 
ATOM   3     C C     . LEU A 1 1463 ? 246.163 194.854 181.677 1.00 45.06 ? 1463 LEU A C     1 
ATOM   4     O O     . LEU A 1 1463 ? 247.171 195.331 182.199 1.00 42.04 ? 1463 LEU A O     1 
ATOM   5     C CB    . LEU A 1 1463 ? 245.944 192.438 182.333 1.00 43.52 ? 1463 LEU A CB    1 
ATOM   6     C CG    . LEU A 1 1463 ? 247.296 192.234 183.021 1.00 44.26 ? 1463 LEU A CG    1 
ATOM   7     C CD1   . LEU A 1 1463 ? 247.284 192.822 184.422 1.00 42.46 ? 1463 LEU A CD1   1 
ATOM   8     C CD2   . LEU A 1 1463 ? 247.641 190.757 183.068 1.00 42.93 ? 1463 LEU A CD2   1 
ATOM   9     N N     . LYS A 1 1464 ? 245.749 195.188 180.452 1.00 43.56 ? 1464 LYS A N     1 
ATOM   10    C CA    . LYS A 1 1464 ? 246.458 196.208 179.685 1.00 43.00 ? 1464 LYS A CA    1 
ATOM   11    C C     . LYS A 1 1464 ? 246.383 197.566 180.373 1.00 44.25 ? 1464 LYS A C     1 
ATOM   12    O O     . LYS A 1 1464 ? 247.387 198.283 180.460 1.00 42.87 ? 1464 LYS A O     1 
ATOM   13    C CB    . LYS A 1 1464 ? 245.888 196.293 178.269 1.00 41.62 ? 1464 LYS A CB    1 
ATOM   14    C CG    . LYS A 1 1464 ? 246.511 195.321 177.276 1.00 41.50 ? 1464 LYS A CG    1 
ATOM   15    C CD    . LYS A 1 1464 ? 246.031 193.896 177.501 1.00 42.13 ? 1464 LYS A CD    1 
ATOM   16    C CE    . LYS A 1 1464 ? 244.514 193.807 177.450 1.00 43.11 ? 1464 LYS A CE    1 
ATOM   17    N NZ    . LYS A 1 1464 ? 244.031 192.423 177.714 1.00 43.76 ? 1464 LYS A NZ    1 
ATOM   18    N N     . GLN A 1 1465 ? 245.201 197.938 180.866 1.00 42.04 ? 1465 GLN A N     1 
ATOM   19    C CA    . GLN A 1 1465 ? 245.054 199.197 181.587 1.00 41.54 ? 1465 GLN A CA    1 
ATOM   20    C C     . GLN A 1 1465 ? 245.635 199.121 182.993 1.00 43.18 ? 1465 GLN A C     1 
ATOM   21    O O     . GLN A 1 1465 ? 246.016 200.152 183.559 1.00 42.63 ? 1465 GLN A O     1 
ATOM   22    C CB    . GLN A 1 1465 ? 243.579 199.603 181.650 1.00 41.16 ? 1465 GLN A CB    1 
ATOM   23    C CG    . GLN A 1 1465 ? 242.702 198.675 182.482 1.00 40.77 ? 1465 GLN A CG    1 
ATOM   24    C CD    . GLN A 1 1465 ? 242.322 197.407 181.743 1.00 42.30 ? 1465 GLN A CD    1 
ATOM   25    O OE1   . GLN A 1 1465 ? 242.313 197.371 180.512 1.00 41.64 ? 1465 GLN A OE1   1 
ATOM   26    N NE2   . GLN A 1 1465 ? 242.006 196.357 182.492 1.00 41.22 ? 1465 GLN A NE2   1 
ATOM   27    N N     . ILE A 1 1466 ? 245.702 197.919 183.570 1.00 41.67 ? 1466 ILE A N     1 
ATOM   28    C CA    . ILE A 1 1466 ? 246.238 197.767 184.918 1.00 41.93 ? 1466 ILE A CA    1 
ATOM   29    C C     . ILE A 1 1466 ? 247.736 198.038 184.931 1.00 41.95 ? 1466 ILE A C     1 
ATOM   30    O O     . ILE A 1 1466 ? 248.263 198.648 185.870 1.00 39.46 ? 1466 ILE A O     1 
ATOM   31    C CB    . ILE A 1 1466 ? 245.905 196.366 185.463 1.00 41.10 ? 1466 ILE A CB    1 
ATOM   32    C CG1   . ILE A 1 1466 ? 244.404 196.098 185.343 1.00 40.16 ? 1466 ILE A CG1   1 
ATOM   33    C CG2   . ILE A 1 1466 ? 246.359 196.231 186.907 1.00 41.75 ? 1466 ILE A CG2   1 
ATOM   34    C CD1   . ILE A 1 1466 ? 243.987 194.727 185.817 1.00 41.48 ? 1466 ILE A CD1   1 
ATOM   35    N N     . ARG A 1 1467 ? 248.446 197.595 183.891 1.00 44.05 ? 1467 ARG A N     1 
ATOM   36    C CA    . ARG A 1 1467 ? 249.888 197.796 183.829 1.00 44.62 ? 1467 ARG A CA    1 
ATOM   37    C C     . ARG A 1 1467 ? 250.267 199.257 183.619 1.00 46.18 ? 1467 ARG A C     1 
ATOM   38    O O     . ARG A 1 1467 ? 251.431 199.616 183.828 1.00 46.68 ? 1467 ARG A O     1 
ATOM   39    C CB    . ARG A 1 1467 ? 250.490 196.937 182.715 1.00 43.36 ? 1467 ARG A CB    1 
ATOM   40    C CG    . ARG A 1 1467 ? 250.409 197.563 181.333 1.00 43.06 ? 1467 ARG A CG    1 
ATOM   41    C CD    . ARG A 1 1467 ? 250.637 196.530 180.240 1.00 44.62 ? 1467 ARG A CD    1 
ATOM   42    N NE    . ARG A 1 1467 ? 249.871 195.311 180.468 1.00 44.68 ? 1467 ARG A NE    1 
ATOM   43    C CZ    . ARG A 1 1467 ? 249.944 194.227 179.707 1.00 45.55 ? 1467 ARG A CZ    1 
ATOM   44    N NH1   . ARG A 1 1467 ? 250.735 194.178 178.647 1.00 45.08 ? 1467 ARG A NH1   1 
ATOM   45    N NH2   . ARG A 1 1467 ? 249.203 193.166 180.015 1.00 43.28 ? 1467 ARG A NH2   1 
ATOM   46    N N     . GLU A 1 1468 ? 249.319 200.106 183.215 1.00 42.58 ? 1468 GLU A N     1 
ATOM   47    C CA    . GLU A 1 1468 ? 249.604 201.511 182.962 1.00 40.14 ? 1468 GLU A CA    1 
ATOM   48    C C     . GLU A 1 1468 ? 248.957 202.466 183.954 1.00 41.56 ? 1468 GLU A C     1 
ATOM   49    O O     . GLU A 1 1468 ? 249.394 203.617 184.045 1.00 39.35 ? 1468 GLU A O     1 
ATOM   50    C CB    . GLU A 1 1468 ? 249.166 201.898 181.540 1.00 40.82 ? 1468 GLU A CB    1 
ATOM   51    C CG    . GLU A 1 1468 ? 247.696 201.649 181.235 1.00 40.74 ? 1468 GLU A CG    1 
ATOM   52    C CD    . GLU A 1 1468 ? 246.808 202.821 181.607 1.00 42.72 ? 1468 GLU A CD    1 
ATOM   53    O OE1   . GLU A 1 1468 ? 247.331 203.947 181.743 1.00 41.24 ? 1468 GLU A OE1   1 
ATOM   54    O OE2   . GLU A 1 1468 ? 245.585 202.616 181.763 1.00 42.91 ? 1468 GLU A OE2   1 
ATOM   55    N N     . VAL A 1 1469 ? 247.931 202.030 184.690 1.00 41.07 ? 1469 VAL A N     1 
ATOM   56    C CA    . VAL A 1 1469 ? 247.295 202.920 185.658 1.00 41.02 ? 1469 VAL A CA    1 
ATOM   57    C C     . VAL A 1 1469 ? 248.252 203.247 186.799 1.00 42.39 ? 1469 VAL A C     1 
ATOM   58    O O     . VAL A 1 1469 ? 248.255 204.369 187.321 1.00 42.59 ? 1469 VAL A O     1 
ATOM   59    C CB    . VAL A 1 1469 ? 245.975 202.307 186.165 1.00 40.41 ? 1469 VAL A CB    1 
ATOM   60    C CG1   . VAL A 1 1469 ? 246.224 201.006 186.917 1.00 39.13 ? 1469 VAL A CG1   1 
ATOM   61    C CG2   . VAL A 1 1469 ? 245.225 203.303 187.041 1.00 40.33 ? 1469 VAL A CG2   1 
ATOM   62    N N     . TRP A 1 1470 ? 249.084 202.284 187.201 1.00 44.22 ? 1470 TRP A N     1 
ATOM   63    C CA    . TRP A 1 1470 ? 250.044 202.516 188.272 1.00 42.32 ? 1470 TRP A CA    1 
ATOM   64    C C     . TRP A 1 1470 ? 251.232 203.359 187.830 1.00 43.18 ? 1470 TRP A C     1 
ATOM   65    O O     . TRP A 1 1470 ? 251.850 204.020 188.672 1.00 41.84 ? 1470 TRP A O     1 
ATOM   66    C CB    . TRP A 1 1470 ? 250.537 201.181 188.835 1.00 41.34 ? 1470 TRP A CB    1 
ATOM   67    C CG    . TRP A 1 1470 ? 249.513 200.466 189.665 1.00 41.85 ? 1470 TRP A CG    1 
ATOM   68    C CD1   . TRP A 1 1470 ? 249.063 199.190 189.489 1.00 41.94 ? 1470 TRP A CD1   1 
ATOM   69    C CD2   . TRP A 1 1470 ? 248.821 200.981 190.810 1.00 43.82 ? 1470 TRP A CD2   1 
ATOM   70    N NE1   . TRP A 1 1470 ? 248.129 198.881 190.447 1.00 43.87 ? 1470 TRP A NE1   1 
ATOM   71    C CE2   . TRP A 1 1470 ? 247.963 199.963 191.271 1.00 42.92 ? 1470 TRP A CE2   1 
ATOM   72    C CE3   . TRP A 1 1470 ? 248.843 202.204 191.489 1.00 44.20 ? 1470 TRP A CE3   1 
ATOM   73    C CZ2   . TRP A 1 1470 ? 247.135 200.131 192.378 1.00 40.98 ? 1470 TRP A CZ2   1 
ATOM   74    C CZ3   . TRP A 1 1470 ? 248.019 202.368 192.585 1.00 42.91 ? 1470 TRP A CZ3   1 
ATOM   75    C CH2   . TRP A 1 1470 ? 247.178 201.337 193.020 1.00 41.90 ? 1470 TRP A CH2   1 
ATOM   76    N N     . ASN A 1 1471 ? 251.565 203.349 186.537 1.00 43.65 ? 1471 ASN A N     1 
ATOM   77    C CA    . ASN A 1 1471 ? 252.677 204.161 186.053 1.00 41.57 ? 1471 ASN A CA    1 
ATOM   78    C C     . ASN A 1 1471 ? 252.398 205.647 186.240 1.00 40.00 ? 1471 ASN A C     1 
ATOM   79    O O     . ASN A 1 1471 ? 253.298 206.415 186.600 1.00 39.21 ? 1471 ASN A O     1 
ATOM   80    C CB    . ASN A 1 1471 ? 252.956 203.845 184.584 1.00 41.37 ? 1471 ASN A CB    1 
ATOM   81    C CG    . ASN A 1 1471 ? 253.126 202.360 184.328 1.00 42.80 ? 1471 ASN A CG    1 
ATOM   82    O OD1   . ASN A 1 1471 ? 253.304 201.575 185.259 1.00 42.21 ? 1471 ASN A OD1   1 
ATOM   83    N ND2   . ASN A 1 1471 ? 253.072 201.968 183.061 1.00 41.28 ? 1471 ASN A ND2   1 
ATOM   84    N N     . THR A 1 1472 ? 251.160 206.070 185.998 1.00 41.46 ? 1472 THR A N     1 
ATOM   85    C CA    . THR A 1 1472 ? 250.748 207.464 186.149 1.00 44.50 ? 1472 THR A CA    1 
ATOM   86    C C     . THR A 1 1472 ? 249.687 207.526 187.243 1.00 44.59 ? 1472 THR A C     1 
ATOM   87    O O     . THR A 1 1472 ? 248.494 207.359 186.969 1.00 43.19 ? 1472 THR A O     1 
ATOM   88    C CB    . THR A 1 1472 ? 250.219 208.027 184.832 1.00 45.45 ? 1472 THR A CB    1 
ATOM   89    O OG1   . THR A 1 1472 ? 249.173 207.182 184.336 1.00 44.90 ? 1472 THR A OG1   1 
ATOM   90    C CG2   . THR A 1 1472 ? 251.334 208.104 183.799 1.00 44.03 ? 1472 THR A CG2   1 
ATOM   91    N N     . TYR A 1 1473 ? 250.120 207.768 188.479 1.00 47.05 ? 1473 TYR A N     1 
ATOM   92    C CA    . TYR A 1 1473 ? 249.190 207.855 189.604 1.00 47.05 ? 1473 TYR A CA    1 
ATOM   93    C C     . TYR A 1 1473 ? 249.795 208.773 190.658 1.00 47.23 ? 1473 TYR A C     1 
ATOM   94    O O     . TYR A 1 1473 ? 250.746 208.387 191.344 1.00 45.00 ? 1473 TYR A O     1 
ATOM   95    C CB    . TYR A 1 1473 ? 248.899 206.474 190.176 1.00 46.06 ? 1473 TYR A CB    1 
ATOM   96    C CG    . TYR A 1 1473 ? 247.602 206.402 190.948 1.00 46.14 ? 1473 TYR A CG    1 
ATOM   97    C CD1   . TYR A 1 1473 ? 246.381 206.554 190.306 1.00 45.14 ? 1473 TYR A CD1   1 
ATOM   98    C CD2   . TYR A 1 1473 ? 247.600 206.181 192.318 1.00 45.92 ? 1473 TYR A CD2   1 
ATOM   99    C CE1   . TYR A 1 1473 ? 245.193 206.492 191.008 1.00 45.87 ? 1473 TYR A CE1   1 
ATOM   100   C CE2   . TYR A 1 1473 ? 246.417 206.115 193.029 1.00 47.20 ? 1473 TYR A CE2   1 
ATOM   101   C CZ    . TYR A 1 1473 ? 245.216 206.270 192.369 1.00 47.97 ? 1473 TYR A CZ    1 
ATOM   102   O OH    . TYR A 1 1473 ? 244.036 206.206 193.073 1.00 47.55 ? 1473 TYR A OH    1 
ATOM   103   N N     . GLU A 1 1474 ? 249.240 209.973 190.786 1.00 46.38 ? 1474 GLU A N     1 
ATOM   104   C CA    . GLU A 1 1474 ? 249.697 210.947 191.763 1.00 45.85 ? 1474 GLU A CA    1 
ATOM   105   C C     . GLU A 1 1474 ? 249.007 210.728 193.105 1.00 46.48 ? 1474 GLU A C     1 
ATOM   106   O O     . GLU A 1 1474 ? 247.888 210.213 193.183 1.00 46.88 ? 1474 GLU A O     1 
ATOM   107   C CB    . GLU A 1 1474 ? 249.432 212.369 191.266 1.00 47.01 ? 1474 GLU A CB    1 
ATOM   108   C CG    . GLU A 1 1474 ? 250.515 212.929 190.360 1.00 48.87 ? 1474 GLU A CG    1 
ATOM   109   C CD    . GLU A 1 1474 ? 251.891 212.860 190.987 1.00 49.78 ? 1474 GLU A CD    1 
ATOM   110   O OE1   . GLU A 1 1474 ? 252.113 213.546 192.006 1.00 47.30 ? 1474 GLU A OE1   1 
ATOM   111   O OE2   . GLU A 1 1474 ? 252.751 212.121 190.462 1.00 49.24 ? 1474 GLU A OE2   1 
ATOM   112   N N     . LEU A 1 1475 ? 249.696 211.128 194.173 1.00 45.99 ? 1475 LEU A N     1 
ATOM   113   C CA    . LEU A 1 1475 ? 249.129 211.049 195.513 1.00 46.01 ? 1475 LEU A CA    1 
ATOM   114   C C     . LEU A 1 1475 ? 248.168 212.190 195.816 1.00 46.02 ? 1475 LEU A C     1 
ATOM   115   O O     . LEU A 1 1475 ? 247.416 212.096 196.792 1.00 46.66 ? 1475 LEU A O     1 
ATOM   116   C CB    . LEU A 1 1475 ? 250.243 211.025 196.565 1.00 43.40 ? 1475 LEU A CB    1 
ATOM   117   C CG    . LEU A 1 1475 ? 250.893 209.678 196.895 1.00 45.18 ? 1475 LEU A CG    1 
ATOM   118   C CD1   . LEU A 1 1475 ? 249.860 208.709 197.458 1.00 43.38 ? 1475 LEU A CD1   1 
ATOM   119   C CD2   . LEU A 1 1475 ? 251.608 209.074 195.695 1.00 43.25 ? 1475 LEU A CD2   1 
ATOM   120   N N     . ASP A 1 1476 ? 248.178 213.254 195.010 1.00 45.32 ? 1476 ASP A N     1 
ATOM   121   C CA    . ASP A 1 1476 ? 247.268 214.390 195.161 1.00 45.82 ? 1476 ASP A CA    1 
ATOM   122   C C     . ASP A 1 1476 ? 247.398 215.013 196.554 1.00 45.72 ? 1476 ASP A C     1 
ATOM   123   O O     . ASP A 1 1476 ? 246.470 215.008 197.365 1.00 45.81 ? 1476 ASP A O     1 
ATOM   124   C CB    . ASP A 1 1476 ? 245.824 213.972 194.860 1.00 43.70 ? 1476 ASP A CB    1 
ATOM   125   C CG    . ASP A 1 1476 ? 244.881 215.153 194.772 1.00 45.75 ? 1476 ASP A CG    1 
ATOM   126   O OD1   . ASP A 1 1476 ? 245.323 216.239 194.342 1.00 41.50 ? 1476 ASP A OD1   1 
ATOM   127   O OD2   . ASP A 1 1476 ? 243.693 214.992 195.119 1.00 47.72 ? 1476 ASP A OD2   1 
ATOM   128   N N     . LEU A 1 1477 ? 248.588 215.546 196.817 1.00 42.11 ? 1477 LEU A N     1 
ATOM   129   C CA    . LEU A 1 1477 ? 248.892 216.114 198.123 1.00 41.84 ? 1477 LEU A CA    1 
ATOM   130   C C     . LEU A 1 1477 ? 248.124 217.410 198.351 1.00 42.46 ? 1477 LEU A C     1 
ATOM   131   O O     . LEU A 1 1477 ? 247.798 218.134 197.406 1.00 42.50 ? 1477 LEU A O     1 
ATOM   132   C CB    . LEU A 1 1477 ? 250.392 216.368 198.247 1.00 43.54 ? 1477 LEU A CB    1 
ATOM   133   C CG    . LEU A 1 1477 ? 251.289 215.189 197.873 1.00 45.73 ? 1477 LEU A CG    1 
ATOM   134   C CD1   . LEU A 1 1477 ? 252.748 215.577 198.004 1.00 43.16 ? 1477 LEU A CD1   1 
ATOM   135   C CD2   . LEU A 1 1477 ? 250.973 213.981 198.741 1.00 42.04 ? 1477 LEU A CD2   1 
ATOM   136   N N     . VAL A 1 1478 ? 247.835 217.700 199.619 1.00 41.07 ? 1478 VAL A N     1 
ATOM   137   C CA    . VAL A 1 1478 ? 247.118 218.906 200.010 1.00 41.38 ? 1478 VAL A CA    1 
ATOM   138   C C     . VAL A 1 1478 ? 247.847 219.560 201.173 1.00 39.39 ? 1478 VAL A C     1 
ATOM   139   O O     . VAL A 1 1478 ? 248.572 218.902 201.926 1.00 39.96 ? 1478 VAL A O     1 
ATOM   140   C CB    . VAL A 1 1478 ? 245.653 218.612 200.396 1.00 37.59 ? 1478 VAL A CB    1 
ATOM   141   C CG1   . VAL A 1 1478 ? 244.846 218.280 199.164 1.00 38.07 ? 1478 VAL A CG1   1 
ATOM   142   C CG2   . VAL A 1 1478 ? 245.583 217.483 201.411 1.00 36.02 ? 1478 VAL A CG2   1 
ATOM   143   N N     . ASN A 1 1479 ? 247.646 220.866 201.320 1.00 39.21 ? 1479 ASN A N     1 
ATOM   144   C CA    . ASN A 1 1479 ? 248.242 221.595 202.426 1.00 42.00 ? 1479 ASN A CA    1 
ATOM   145   C C     . ASN A 1 1479 ? 247.410 221.417 203.693 1.00 44.31 ? 1479 ASN A C     1 
ATOM   146   O O     . ASN A 1 1479 ? 246.243 221.017 203.655 1.00 43.79 ? 1479 ASN A O     1 
ATOM   147   C CB    . ASN A 1 1479 ? 248.374 223.080 202.085 1.00 42.85 ? 1479 ASN A CB    1 
ATOM   148   C CG    . ASN A 1 1479 ? 249.428 223.778 202.922 1.00 44.15 ? 1479 ASN A CG    1 
ATOM   149   O OD1   . ASN A 1 1479 ? 250.175 223.136 203.660 1.00 43.85 ? 1479 ASN A OD1   1 
ATOM   150   N ND2   . ASN A 1 1479 ? 249.494 225.100 202.810 1.00 44.56 ? 1479 ASN A ND2   1 
ATOM   151   N N     . TYR A 1 1480 ? 248.032 221.723 204.828 1.00 47.76 ? 1480 TYR A N     1 
ATOM   152   C CA    . TYR A 1 1480 ? 247.406 221.599 206.134 1.00 47.28 ? 1480 TYR A CA    1 
ATOM   153   C C     . TYR A 1 1480 ? 247.479 222.935 206.862 1.00 47.15 ? 1480 TYR A C     1 
ATOM   154   O O     . TYR A 1 1480 ? 248.244 223.828 206.489 1.00 45.21 ? 1480 TYR A O     1 
ATOM   155   C CB    . TYR A 1 1480 ? 248.083 220.501 206.968 1.00 45.66 ? 1480 TYR A CB    1 
ATOM   156   C CG    . TYR A 1 1480 ? 247.324 220.097 208.212 1.00 48.38 ? 1480 TYR A CG    1 
ATOM   157   C CD1   . TYR A 1 1480 ? 245.963 219.833 208.164 1.00 46.85 ? 1480 TYR A CD1   1 
ATOM   158   C CD2   . TYR A 1 1480 ? 247.972 219.977 209.435 1.00 48.73 ? 1480 TYR A CD2   1 
ATOM   159   C CE1   . TYR A 1 1480 ? 245.269 219.461 209.297 1.00 46.77 ? 1480 TYR A CE1   1 
ATOM   160   C CE2   . TYR A 1 1480 ? 247.284 219.607 210.574 1.00 47.18 ? 1480 TYR A CE2   1 
ATOM   161   C CZ    . TYR A 1 1480 ? 245.932 219.350 210.498 1.00 47.05 ? 1480 TYR A CZ    1 
ATOM   162   O OH    . TYR A 1 1480 ? 245.240 218.980 211.628 1.00 46.52 ? 1480 TYR A OH    1 
ATOM   163   N N     . GLN A 1 1481 ? 246.661 223.064 207.910 1.00 49.59 ? 1481 GLN A N     1 
ATOM   164   C CA    . GLN A 1 1481 ? 246.678 224.280 208.718 1.00 51.35 ? 1481 GLN A CA    1 
ATOM   165   C C     . GLN A 1 1481 ? 248.041 224.506 209.358 1.00 52.10 ? 1481 GLN A C     1 
ATOM   166   O O     . GLN A 1 1481 ? 248.394 225.646 209.682 1.00 52.46 ? 1481 GLN A O     1 
ATOM   167   C CB    . GLN A 1 1481 ? 245.589 224.213 209.788 1.00 49.70 ? 1481 GLN A CB    1 
ATOM   168   C CG    . GLN A 1 1481 ? 244.273 223.641 209.289 1.00 50.23 ? 1481 GLN A CG    1 
ATOM   169   C CD    . GLN A 1 1481 ? 243.377 223.170 210.415 1.00 50.71 ? 1481 GLN A CD    1 
ATOM   170   O OE1   . GLN A 1 1481 ? 242.685 223.967 211.049 1.00 50.37 ? 1481 GLN A OE1   1 
ATOM   171   N NE2   . GLN A 1 1481 ? 243.386 221.867 210.672 1.00 47.61 ? 1481 GLN A NE2   1 
ATOM   172   N N     . ASN A 1 1482 ? 248.815 223.441 209.549 1.00 48.16 ? 1482 ASN A N     1 
ATOM   173   C CA    . ASN A 1 1482 ? 250.180 223.532 210.043 1.00 47.95 ? 1482 ASN A CA    1 
ATOM   174   C C     . ASN A 1 1482 ? 251.201 223.634 208.916 1.00 48.52 ? 1482 ASN A C     1 
ATOM   175   O O     . ASN A 1 1482 ? 252.395 223.430 209.159 1.00 47.06 ? 1482 ASN A O     1 
ATOM   176   C CB    . ASN A 1 1482 ? 250.500 222.326 210.930 1.00 47.06 ? 1482 ASN A CB    1 
ATOM   177   C CG    . ASN A 1 1482 ? 249.894 222.446 212.315 1.00 48.67 ? 1482 ASN A CG    1 
ATOM   178   O OD1   . ASN A 1 1482 ? 250.508 222.997 213.228 1.00 48.45 ? 1482 ASN A OD1   1 
ATOM   179   N ND2   . ASN A 1 1482 ? 248.681 221.930 212.477 1.00 48.37 ? 1482 ASN A ND2   1 
ATOM   180   N N     . LYS A 1 1483 ? 250.753 223.938 207.696 1.00 45.89 ? 1483 LYS A N     1 
ATOM   181   C CA    . LYS A 1 1483 ? 251.620 224.057 206.523 1.00 45.03 ? 1483 LYS A CA    1 
ATOM   182   C C     . LYS A 1 1483 ? 252.395 222.759 206.280 1.00 45.55 ? 1483 LYS A C     1 
ATOM   183   O O     . LYS A 1 1483 ? 253.625 222.736 206.198 1.00 45.26 ? 1483 LYS A O     1 
ATOM   184   C CB    . LYS A 1 1483 ? 252.565 225.256 206.657 1.00 44.74 ? 1483 LYS A CB    1 
ATOM   185   C CG    . LYS A 1 1483 ? 252.137 226.477 205.857 1.00 43.40 ? 1483 LYS A CG    1 
ATOM   186   C CD    . LYS A 1 1483 ? 250.704 226.875 206.167 1.00 44.06 ? 1483 LYS A CD    1 
ATOM   187   C CE    . LYS A 1 1483 ? 250.221 227.970 205.229 1.00 44.44 ? 1483 LYS A CE    1 
ATOM   188   N NZ    . LYS A 1 1483 ? 248.825 228.392 205.533 1.00 43.85 ? 1483 LYS A NZ    1 
ATOM   189   N N     . CYS A 1 1484 ? 251.640 221.668 206.166 1.00 44.59 ? 1484 CYS A N     1 
ATOM   190   C CA    . CYS A 1 1484 ? 252.209 220.350 205.932 1.00 43.78 ? 1484 CYS A CA    1 
ATOM   191   C C     . CYS A 1 1484 ? 251.377 219.626 204.882 1.00 43.95 ? 1484 CYS A C     1 
ATOM   192   O O     . CYS A 1 1484 ? 250.192 219.911 204.693 1.00 44.35 ? 1484 CYS A O     1 
ATOM   193   C CB    . CYS A 1 1484 ? 252.277 219.530 207.226 1.00 42.79 ? 1484 CYS A CB    1 
ATOM   194   S SG    . CYS A 1 1484 ? 253.216 220.329 208.550 1.00 49.58 ? 1484 CYS A SG    1 
ATOM   195   N N     . ARG A 1 1485 ? 252.015 218.686 204.194 1.00 43.49 ? 1485 ARG A N     1 
ATOM   196   C CA    . ARG A 1 1485 ? 251.369 217.949 203.119 1.00 41.72 ? 1485 ARG A CA    1 
ATOM   197   C C     . ARG A 1 1485 ? 250.599 216.753 203.666 1.00 39.33 ? 1485 ARG A C     1 
ATOM   198   O O     . ARG A 1 1485 ? 251.041 216.078 204.599 1.00 40.49 ? 1485 ARG A O     1 
ATOM   199   C CB    . ARG A 1 1485 ? 252.400 217.480 202.092 1.00 41.68 ? 1485 ARG A CB    1 
ATOM   200   C CG    . ARG A 1 1485 ? 253.475 218.509 201.782 1.00 41.81 ? 1485 ARG A CG    1 
ATOM   201   C CD    . ARG A 1 1485 ? 252.893 219.738 201.097 1.00 42.48 ? 1485 ARG A CD    1 
ATOM   202   N NE    . ARG A 1 1485 ? 252.189 219.399 199.866 1.00 44.50 ? 1485 ARG A NE    1 
ATOM   203   C CZ    . ARG A 1 1485 ? 251.207 220.120 199.342 1.00 43.29 ? 1485 ARG A CZ    1 
ATOM   204   N NH1   . ARG A 1 1485 ? 250.786 221.235 199.915 1.00 42.38 ? 1485 ARG A NH1   1 
ATOM   205   N NH2   . ARG A 1 1485 ? 250.635 219.712 198.213 1.00 39.51 ? 1485 ARG A NH2   1 
ATOM   206   N N     . LEU A 1 1486 ? 249.435 216.499 203.070 1.00 34.70 ? 1486 LEU A N     1 
ATOM   207   C CA    . LEU A 1 1486 ? 248.605 215.359 203.435 1.00 34.13 ? 1486 LEU A CA    1 
ATOM   208   C C     . LEU A 1 1486 ? 247.970 214.787 202.177 1.00 37.92 ? 1486 LEU A C     1 
ATOM   209   O O     . LEU A 1 1486 ? 248.022 215.389 201.102 1.00 37.46 ? 1486 LEU A O     1 
ATOM   210   C CB    . LEU A 1 1486 ? 247.522 215.739 204.453 1.00 35.23 ? 1486 LEU A CB    1 
ATOM   211   C CG    . LEU A 1 1486 ? 247.965 216.170 205.852 1.00 39.33 ? 1486 LEU A CG    1 
ATOM   212   C CD1   . LEU A 1 1486 ? 246.771 216.638 206.664 1.00 38.07 ? 1486 LEU A CD1   1 
ATOM   213   C CD2   . LEU A 1 1486 ? 248.675 215.029 206.561 1.00 39.15 ? 1486 LEU A CD2   1 
ATOM   214   N N     . ILE A 1 1487 ? 247.371 213.609 202.324 1.00 39.00 ? 1487 ILE A N     1 
ATOM   215   C CA    . ILE A 1 1487 ? 246.721 212.916 201.217 1.00 40.08 ? 1487 ILE A CA    1 
ATOM   216   C C     . ILE A 1 1487 ? 245.213 213.067 201.358 1.00 39.85 ? 1487 ILE A C     1 
ATOM   217   O O     . ILE A 1 1487 ? 244.638 212.704 202.391 1.00 38.85 ? 1487 ILE A O     1 
ATOM   218   C CB    . ILE A 1 1487 ? 247.125 211.433 201.188 1.00 38.03 ? 1487 ILE A CB    1 
ATOM   219   C CG1   . ILE A 1 1487 ? 248.629 211.293 200.944 1.00 38.88 ? 1487 ILE A CG1   1 
ATOM   220   C CG2   . ILE A 1 1487 ? 246.332 210.685 200.127 1.00 37.77 ? 1487 ILE A CG2   1 
ATOM   221   C CD1   . ILE A 1 1487 ? 249.153 209.890 201.157 1.00 37.94 ? 1487 ILE A CD1   1 
ATOM   222   N N     . ARG A 1 1488 ? 244.566 213.601 200.320 1.00 40.63 ? 1488 ARG A N     1 
ATOM   223   C CA    . ARG A 1 1488 ? 243.119 213.790 200.332 1.00 40.12 ? 1488 ARG A CA    1 
ATOM   224   C C     . ARG A 1 1488 ? 242.375 212.672 199.611 1.00 41.05 ? 1488 ARG A C     1 
ATOM   225   O O     . ARG A 1 1488 ? 241.211 212.403 199.922 1.00 41.74 ? 1488 ARG A O     1 
ATOM   226   C CB    . ARG A 1 1488 ? 242.741 215.141 199.705 1.00 38.89 ? 1488 ARG A CB    1 
ATOM   227   C CG    . ARG A 1 1488 ? 242.391 215.065 198.222 1.00 38.10 ? 1488 ARG A CG    1 
ATOM   228   C CD    . ARG A 1 1488 ? 242.263 216.433 197.567 1.00 39.46 ? 1488 ARG A CD    1 
ATOM   229   N NE    . ARG A 1 1488 ? 241.233 217.253 198.193 1.00 40.45 ? 1488 ARG A NE    1 
ATOM   230   C CZ    . ARG A 1 1488 ? 241.251 218.578 198.235 1.00 39.88 ? 1488 ARG A CZ    1 
ATOM   231   N NH1   . ARG A 1 1488 ? 242.211 219.276 197.651 1.00 37.98 ? 1488 ARG A NH1   1 
ATOM   232   N NH2   . ARG A 1 1488 ? 240.274 219.221 198.868 1.00 40.69 ? 1488 ARG A NH2   1 
ATOM   233   N N     . GLY A 1 1489 ? 243.021 212.012 198.652 1.00 41.42 ? 1489 GLY A N     1 
ATOM   234   C CA    . GLY A 1 1489 ? 242.335 211.038 197.825 1.00 43.13 ? 1489 GLY A CA    1 
ATOM   235   C C     . GLY A 1 1489 ? 242.275 209.684 198.502 1.00 43.80 ? 1489 GLY A C     1 
ATOM   236   O O     . GLY A 1 1489 ? 243.321 209.065 198.760 1.00 47.12 ? 1489 GLY A O     1 
ATOM   237   N N     . TRP A 1 1490 ? 241.076 209.212 198.799 1.00 41.59 ? 1490 TRP A N     1 
ATOM   238   C CA    . TRP A 1 1490 ? 240.914 207.904 199.420 1.00 43.10 ? 1490 TRP A CA    1 
ATOM   239   C C     . TRP A 1 1490 ? 239.912 207.020 198.694 1.00 44.70 ? 1490 TRP A C     1 
ATOM   240   O O     . TRP A 1 1490 ? 240.113 205.806 198.624 1.00 43.99 ? 1490 TRP A O     1 
ATOM   241   C CB    . TRP A 1 1490 ? 240.498 208.076 200.889 1.00 42.66 ? 1490 TRP A CB    1 
ATOM   242   C CG    . TRP A 1 1490 ? 241.556 208.728 201.727 1.00 44.47 ? 1490 TRP A CG    1 
ATOM   243   C CD1   . TRP A 1 1490 ? 241.492 209.958 202.314 1.00 43.39 ? 1490 TRP A CD1   1 
ATOM   244   C CD2   . TRP A 1 1490 ? 242.842 208.192 202.061 1.00 45.60 ? 1490 TRP A CD2   1 
ATOM   245   N NE1   . TRP A 1 1490 ? 242.655 210.218 202.998 1.00 42.66 ? 1490 TRP A NE1   1 
ATOM   246   C CE2   . TRP A 1 1490 ? 243.500 209.149 202.858 1.00 44.37 ? 1490 TRP A CE2   1 
ATOM   247   C CE3   . TRP A 1 1490 ? 243.500 206.994 201.766 1.00 43.44 ? 1490 TRP A CE3   1 
ATOM   248   C CZ2   . TRP A 1 1490 ? 244.782 208.946 203.363 1.00 43.77 ? 1490 TRP A CZ2   1 
ATOM   249   C CZ3   . TRP A 1 1490 ? 244.772 206.794 202.269 1.00 44.02 ? 1490 TRP A CZ3   1 
ATOM   250   C CH2   . TRP A 1 1490 ? 245.400 207.765 203.058 1.00 44.83 ? 1490 TRP A CH2   1 
ATOM   251   N N     . ASP A 1 1491 ? 238.835 207.597 198.154 1.00 45.20 ? 1491 ASP A N     1 
ATOM   252   C CA    . ASP A 1 1491 ? 237.831 206.792 197.465 1.00 44.79 ? 1491 ASP A CA    1 
ATOM   253   C C     . ASP A 1 1491 ? 238.384 206.194 196.176 1.00 45.08 ? 1491 ASP A C     1 
ATOM   254   O O     . ASP A 1 1491 ? 238.238 204.991 195.927 1.00 43.05 ? 1491 ASP A O     1 
ATOM   255   C CB    . ASP A 1 1491 ? 236.590 207.638 197.180 1.00 44.83 ? 1491 ASP A CB    1 
ATOM   256   C CG    . ASP A 1 1491 ? 236.924 208.953 196.502 1.00 46.39 ? 1491 ASP A CG    1 
ATOM   257   O OD1   . ASP A 1 1491 ? 238.125 209.249 196.333 1.00 46.41 ? 1491 ASP A OD1   1 
ATOM   258   O OD2   . ASP A 1 1491 ? 235.985 209.692 196.137 1.00 46.46 ? 1491 ASP A OD2   1 
ATOM   259   N N     . ASP A 1 1492 ? 239.019 207.021 195.342 1.00 44.97 ? 1492 ASP A N     1 
ATOM   260   C CA    . ASP A 1 1492 ? 239.623 206.510 194.116 1.00 44.23 ? 1492 ASP A CA    1 
ATOM   261   C C     . ASP A 1 1492 ? 240.811 205.611 194.427 1.00 44.60 ? 1492 ASP A C     1 
ATOM   262   O O     . ASP A 1 1492 ? 241.172 204.744 193.624 1.00 44.04 ? 1492 ASP A O     1 
ATOM   263   C CB    . ASP A 1 1492 ? 240.052 207.670 193.217 1.00 40.99 ? 1492 ASP A CB    1 
ATOM   264   C CG    . ASP A 1 1492 ? 240.854 208.720 193.963 1.00 44.27 ? 1492 ASP A CG    1 
ATOM   265   O OD1   . ASP A 1 1492 ? 240.910 208.652 195.209 1.00 44.83 ? 1492 ASP A OD1   1 
ATOM   266   O OD2   . ASP A 1 1492 ? 241.430 209.610 193.303 1.00 43.17 ? 1492 ASP A OD2   1 
ATOM   267   N N     . LEU A 1 1493 ? 241.433 205.809 195.589 1.00 41.30 ? 1493 LEU A N     1 
ATOM   268   C CA    . LEU A 1 1493 ? 242.596 205.029 195.981 1.00 42.92 ? 1493 LEU A CA    1 
ATOM   269   C C     . LEU A 1 1493 ? 242.220 203.685 196.596 1.00 43.13 ? 1493 LEU A C     1 
ATOM   270   O O     . LEU A 1 1493 ? 243.091 202.822 196.739 1.00 42.57 ? 1493 LEU A O     1 
ATOM   271   C CB    . LEU A 1 1493 ? 243.445 205.871 196.939 1.00 40.97 ? 1493 LEU A CB    1 
ATOM   272   C CG    . LEU A 1 1493 ? 244.828 205.439 197.421 1.00 42.00 ? 1493 LEU A CG    1 
ATOM   273   C CD1   . LEU A 1 1493 ? 245.635 206.673 197.760 1.00 42.68 ? 1493 LEU A CD1   1 
ATOM   274   C CD2   . LEU A 1 1493 ? 244.703 204.569 198.646 1.00 41.35 ? 1493 LEU A CD2   1 
ATOM   275   N N     . PHE A 1 1494 ? 240.951 203.476 196.939 1.00 42.69 ? 1494 PHE A N     1 
ATOM   276   C CA    . PHE A 1 1494 ? 240.482 202.191 197.446 1.00 44.43 ? 1494 PHE A CA    1 
ATOM   277   C C     . PHE A 1 1494 ? 239.628 201.443 196.437 1.00 47.52 ? 1494 PHE A C     1 
ATOM   278   O O     . PHE A 1 1494 ? 239.871 200.256 196.185 1.00 45.43 ? 1494 PHE A O     1 
ATOM   279   C CB    . PHE A 1 1494 ? 239.689 202.385 198.751 1.00 42.38 ? 1494 PHE A CB    1 
ATOM   280   C CG    . PHE A 1 1494 ? 240.512 202.904 199.895 1.00 45.57 ? 1494 PHE A CG    1 
ATOM   281   C CD1   . PHE A 1 1494 ? 241.859 202.602 199.992 1.00 45.94 ? 1494 PHE A CD1   1 
ATOM   282   C CD2   . PHE A 1 1494 ? 239.933 203.687 200.881 1.00 44.74 ? 1494 PHE A CD2   1 
ATOM   283   C CE1   . PHE A 1 1494 ? 242.615 203.075 201.048 1.00 44.51 ? 1494 PHE A CE1   1 
ATOM   284   C CE2   . PHE A 1 1494 ? 240.685 204.164 201.937 1.00 43.04 ? 1494 PHE A CE2   1 
ATOM   285   C CZ    . PHE A 1 1494 ? 242.027 203.858 202.021 1.00 43.62 ? 1494 PHE A CZ    1 
ATOM   286   N N     . ASN A 1 1495 ? 238.620 202.104 195.858 1.00 47.28 ? 1495 ASN A N     1 
ATOM   287   C CA    . ASN A 1 1495 ? 237.708 201.421 194.945 1.00 44.48 ? 1495 ASN A CA    1 
ATOM   288   C C     . ASN A 1 1495 ? 238.426 200.935 193.693 1.00 46.76 ? 1495 ASN A C     1 
ATOM   289   O O     . ASN A 1 1495 ? 238.190 199.811 193.234 1.00 46.94 ? 1495 ASN A O     1 
ATOM   290   C CB    . ASN A 1 1495 ? 236.552 202.349 194.572 1.00 44.91 ? 1495 ASN A CB    1 
ATOM   291   C CG    . ASN A 1 1495 ? 235.852 202.924 195.786 1.00 46.96 ? 1495 ASN A CG    1 
ATOM   292   O OD1   . ASN A 1 1495 ? 236.056 202.464 196.910 1.00 47.22 ? 1495 ASN A OD1   1 
ATOM   293   N ND2   . ASN A 1 1495 ? 235.022 203.937 195.567 1.00 44.88 ? 1495 ASN A ND2   1 
ATOM   294   N N     . LYS A 1 1496 ? 239.301 201.766 193.123 1.00 43.93 ? 1496 LYS A N     1 
ATOM   295   C CA    . LYS A 1 1496 ? 240.016 201.373 191.913 1.00 45.12 ? 1496 LYS A CA    1 
ATOM   296   C C     . LYS A 1 1496 ? 240.948 200.195 192.175 1.00 43.55 ? 1496 LYS A C     1 
ATOM   297   O O     . LYS A 1 1496 ? 241.028 199.267 191.361 1.00 40.08 ? 1496 LYS A O     1 
ATOM   298   C CB    . LYS A 1 1496 ? 240.785 202.572 191.356 1.00 44.28 ? 1496 LYS A CB    1 
ATOM   299   C CG    . LYS A 1 1496 ? 241.542 202.315 190.063 1.00 42.78 ? 1496 LYS A CG    1 
ATOM   300   C CD    . LYS A 1 1496 ? 243.017 202.079 190.335 1.00 43.86 ? 1496 LYS A CD    1 
ATOM   301   C CE    . LYS A 1 1496 ? 243.679 203.334 190.873 1.00 42.84 ? 1496 LYS A CE    1 
ATOM   302   N NZ    . LYS A 1 1496 ? 245.119 203.120 191.181 1.00 44.44 ? 1496 LYS A NZ    1 
ATOM   303   N N     . VAL A 1 1497 ? 241.653 200.209 193.308 1.00 42.02 ? 1497 VAL A N     1 
ATOM   304   C CA    . VAL A 1 1497 ? 242.548 199.103 193.635 1.00 42.88 ? 1497 VAL A CA    1 
ATOM   305   C C     . VAL A 1 1497 ? 241.757 197.828 193.893 1.00 44.08 ? 1497 VAL A C     1 
ATOM   306   O O     . VAL A 1 1497 ? 242.172 196.734 193.491 1.00 43.59 ? 1497 VAL A O     1 
ATOM   307   C CB    . VAL A 1 1497 ? 243.441 199.472 194.831 1.00 44.48 ? 1497 VAL A CB    1 
ATOM   308   C CG1   . VAL A 1 1497 ? 244.510 198.413 195.038 1.00 43.64 ? 1497 VAL A CG1   1 
ATOM   309   C CG2   . VAL A 1 1497 ? 244.085 200.821 194.595 1.00 42.68 ? 1497 VAL A CG2   1 
ATOM   310   N N     . LYS A 1 1498 ? 240.612 197.939 194.572 1.00 44.09 ? 1498 LYS A N     1 
ATOM   311   C CA    . LYS A 1 1498 ? 239.778 196.763 194.790 1.00 45.22 ? 1498 LYS A CA    1 
ATOM   312   C C     . LYS A 1 1498 ? 239.267 196.202 193.469 1.00 43.03 ? 1498 LYS A C     1 
ATOM   313   O O     . LYS A 1 1498 ? 239.251 194.982 193.268 1.00 40.76 ? 1498 LYS A O     1 
ATOM   314   C CB    . LYS A 1 1498 ? 238.614 197.108 195.719 1.00 46.08 ? 1498 LYS A CB    1 
ATOM   315   C CG    . LYS A 1 1498 ? 237.760 195.914 196.112 1.00 44.77 ? 1498 LYS A CG    1 
ATOM   316   C CD    . LYS A 1 1498 ? 236.912 196.216 197.337 1.00 43.35 ? 1498 LYS A CD    1 
ATOM   317   C CE    . LYS A 1 1498 ? 236.139 197.515 197.174 1.00 43.65 ? 1498 LYS A CE    1 
ATOM   318   N NZ    . LYS A 1 1498 ? 235.315 197.519 195.932 1.00 44.48 ? 1498 LYS A NZ    1 
ATOM   319   N N     . GLU A 1 1499 ? 238.854 197.079 192.552 1.00 41.55 ? 1499 GLU A N     1 
ATOM   320   C CA    . GLU A 1 1499 ? 238.401 196.622 191.243 1.00 42.53 ? 1499 GLU A CA    1 
ATOM   321   C C     . GLU A 1 1499 ? 239.525 195.931 190.482 1.00 42.02 ? 1499 GLU A C     1 
ATOM   322   O O     . GLU A 1 1499 ? 239.311 194.880 189.866 1.00 40.25 ? 1499 GLU A O     1 
ATOM   323   C CB    . GLU A 1 1499 ? 237.850 197.801 190.440 1.00 42.04 ? 1499 GLU A CB    1 
ATOM   324   C CG    . GLU A 1 1499 ? 237.007 197.403 189.236 1.00 43.51 ? 1499 GLU A CG    1 
ATOM   325   C CD    . GLU A 1 1499 ? 237.837 197.174 187.988 1.00 42.36 ? 1499 GLU A CD    1 
ATOM   326   O OE1   . GLU A 1 1499 ? 238.937 197.756 187.889 1.00 44.75 ? 1499 GLU A OE1   1 
ATOM   327   O OE2   . GLU A 1 1499 ? 237.387 196.413 187.106 1.00 39.33 ? 1499 GLU A OE2   1 
ATOM   328   N N     . HIS A 1 1500 ? 240.733 196.500 190.519 1.00 40.50 ? 1500 HIS A N     1 
ATOM   329   C CA    . HIS A 1 1500 ? 241.857 195.886 189.819 1.00 41.65 ? 1500 HIS A CA    1 
ATOM   330   C C     . HIS A 1 1500 ? 242.216 194.530 190.415 1.00 41.29 ? 1500 HIS A C     1 
ATOM   331   O O     . HIS A 1 1500 ? 242.506 193.581 189.675 1.00 41.00 ? 1500 HIS A O     1 
ATOM   332   C CB    . HIS A 1 1500 ? 243.071 196.814 189.838 1.00 41.52 ? 1500 HIS A CB    1 
ATOM   333   C CG    . HIS A 1 1500 ? 243.005 197.915 188.827 1.00 40.22 ? 1500 HIS A CG    1 
ATOM   334   N ND1   . HIS A 1 1500 ? 242.294 197.804 187.652 1.00 40.89 ? 1500 HIS A ND1   1 
ATOM   335   C CD2   . HIS A 1 1500 ? 243.581 199.140 188.804 1.00 39.83 ? 1500 HIS A CD2   1 
ATOM   336   C CE1   . HIS A 1 1500 ? 242.422 198.919 186.955 1.00 39.63 ? 1500 HIS A CE1   1 
ATOM   337   N NE2   . HIS A 1 1500 ? 243.198 199.746 187.632 1.00 39.13 ? 1500 HIS A NE2   1 
ATOM   338   N N     . ILE A 1 1501 ? 242.214 194.415 191.745 1.00 37.76 ? 1501 ILE A N     1 
ATOM   339   C CA    . ILE A 1 1501 ? 242.574 193.140 192.358 1.00 39.01 ? 1501 ILE A CA    1 
ATOM   340   C C     . ILE A 1 1501 ? 241.496 192.094 192.087 1.00 39.06 ? 1501 ILE A C     1 
ATOM   341   O O     . ILE A 1 1501 ? 241.803 190.920 191.845 1.00 40.21 ? 1501 ILE A O     1 
ATOM   342   C CB    . ILE A 1 1501 ? 242.868 193.312 193.862 1.00 41.68 ? 1501 ILE A CB    1 
ATOM   343   C CG1   . ILE A 1 1501 ? 243.669 192.116 194.382 1.00 39.85 ? 1501 ILE A CG1   1 
ATOM   344   C CG2   . ILE A 1 1501 ? 241.598 193.494 194.678 1.00 40.18 ? 1501 ILE A CG2   1 
ATOM   345   C CD1   . ILE A 1 1501 ? 244.235 192.320 195.766 1.00 38.09 ? 1501 ILE A CD1   1 
ATOM   346   N N     . ASN A 1 1502 ? 240.223 192.500 192.089 1.00 42.18 ? 1502 ASN A N     1 
ATOM   347   C CA    . ASN A 1 1502 ? 239.161 191.569 191.722 1.00 39.68 ? 1502 ASN A CA    1 
ATOM   348   C C     . ASN A 1 1502 ? 239.308 191.119 190.275 1.00 39.77 ? 1502 ASN A C     1 
ATOM   349   O O     . ASN A 1 1502 ? 239.123 189.937 189.962 1.00 40.46 ? 1502 ASN A O     1 
ATOM   350   C CB    . ASN A 1 1502 ? 237.793 192.210 191.951 1.00 40.39 ? 1502 ASN A CB    1 
ATOM   351   C CG    . ASN A 1 1502 ? 237.502 192.452 193.418 1.00 45.99 ? 1502 ASN A CG    1 
ATOM   352   O OD1   . ASN A 1 1502 ? 238.213 191.960 194.294 1.00 45.59 ? 1502 ASN A OD1   1 
ATOM   353   N ND2   . ASN A 1 1502 ? 236.450 193.215 193.694 1.00 43.25 ? 1502 ASN A ND2   1 
ATOM   354   N N     . SER A 1 1503 ? 239.651 192.048 189.379 1.00 39.53 ? 1503 SER A N     1 
ATOM   355   C CA    . SER A 1 1503 ? 239.823 191.696 187.974 1.00 40.86 ? 1503 SER A CA    1 
ATOM   356   C C     . SER A 1 1503 ? 240.978 190.722 187.782 1.00 39.92 ? 1503 SER A C     1 
ATOM   357   O O     . SER A 1 1503 ? 240.848 189.739 187.043 1.00 37.30 ? 1503 SER A O     1 
ATOM   358   C CB    . SER A 1 1503 ? 240.041 192.959 187.141 1.00 39.75 ? 1503 SER A CB    1 
ATOM   359   O OG    . SER A 1 1503 ? 240.043 192.661 185.756 1.00 39.00 ? 1503 SER A OG    1 
ATOM   360   N N     . VAL A 1 1504 ? 242.115 190.971 188.436 1.00 38.78 ? 1504 VAL A N     1 
ATOM   361   C CA    . VAL A 1 1504 ? 243.258 190.079 188.261 1.00 39.31 ? 1504 VAL A CA    1 
ATOM   362   C C     . VAL A 1 1504 ? 242.977 188.716 188.886 1.00 37.05 ? 1504 VAL A C     1 
ATOM   363   O O     . VAL A 1 1504 ? 243.385 187.680 188.346 1.00 36.17 ? 1504 VAL A O     1 
ATOM   364   C CB    . VAL A 1 1504 ? 244.554 190.712 188.809 1.00 39.27 ? 1504 VAL A CB    1 
ATOM   365   C CG1   . VAL A 1 1504 ? 244.831 192.040 188.121 1.00 37.68 ? 1504 VAL A CG1   1 
ATOM   366   C CG2   . VAL A 1 1504 ? 244.504 190.884 190.315 1.00 35.15 ? 1504 VAL A CG2   1 
ATOM   367   N N     . SER A 1 1505 ? 242.268 188.686 190.020 1.00 34.13 ? 1505 SER A N     1 
ATOM   368   C CA    . SER A 1 1505 ? 241.898 187.405 190.614 1.00 34.48 ? 1505 SER A CA    1 
ATOM   369   C C     . SER A 1 1505 ? 240.963 186.627 189.698 1.00 37.17 ? 1505 SER A C     1 
ATOM   370   O O     . SER A 1 1505 ? 241.109 185.409 189.538 1.00 36.74 ? 1505 SER A O     1 
ATOM   371   C CB    . SER A 1 1505 ? 241.254 187.625 191.982 1.00 33.11 ? 1505 SER A CB    1 
ATOM   372   O OG    . SER A 1 1505 ? 240.056 188.374 191.868 1.00 35.97 ? 1505 SER A OG    1 
ATOM   373   N N     . ALA A 1 1506 ? 239.997 187.315 189.083 1.00 35.14 ? 1506 ALA A N     1 
ATOM   374   C CA    . ALA A 1 1506 ? 239.096 186.650 188.149 1.00 34.56 ? 1506 ALA A CA    1 
ATOM   375   C C     . ALA A 1 1506 ? 239.849 186.116 186.937 1.00 38.00 ? 1506 ALA A C     1 
ATOM   376   O O     . ALA A 1 1506 ? 239.610 184.985 186.500 1.00 37.04 ? 1506 ALA A O     1 
ATOM   377   C CB    . ALA A 1 1506 ? 237.988 187.609 187.715 1.00 33.23 ? 1506 ALA A CB    1 
ATOM   378   N N     . MET A 1 1507 ? 240.767 186.914 186.383 1.00 39.61 ? 1507 MET A N     1 
ATOM   379   C CA    . MET A 1 1507 ? 241.532 186.463 185.223 1.00 40.39 ? 1507 MET A CA    1 
ATOM   380   C C     . MET A 1 1507 ? 242.425 185.275 185.557 1.00 39.74 ? 1507 MET A C     1 
ATOM   381   O O     . MET A 1 1507 ? 242.528 184.339 184.756 1.00 39.90 ? 1507 MET A O     1 
ATOM   382   C CB    . MET A 1 1507 ? 242.366 187.609 184.649 1.00 39.41 ? 1507 MET A CB    1 
ATOM   383   C CG    . MET A 1 1507 ? 241.552 188.812 184.202 1.00 40.04 ? 1507 MET A CG    1 
ATOM   384   S SD    . MET A 1 1507 ? 242.557 190.073 183.396 1.00 46.28 ? 1507 MET A SD    1 
ATOM   385   C CE    . MET A 1 1507 ? 243.995 190.093 184.464 1.00 38.53 ? 1507 MET A CE    1 
ATOM   386   N N     . LYS A 1 1508 ? 243.081 185.290 186.720 1.00 37.20 ? 1508 LYS A N     1 
ATOM   387   C CA    . LYS A 1 1508 ? 243.889 184.141 187.114 1.00 39.91 ? 1508 LYS A CA    1 
ATOM   388   C C     . LYS A 1 1508 ? 243.022 182.908 187.335 1.00 41.14 ? 1508 LYS A C     1 
ATOM   389   O O     . LYS A 1 1508 ? 243.401 181.797 186.946 1.00 40.93 ? 1508 LYS A O     1 
ATOM   390   C CB    . LYS A 1 1508 ? 244.697 184.463 188.370 1.00 39.18 ? 1508 LYS A CB    1 
ATOM   391   C CG    . LYS A 1 1508 ? 245.821 183.474 188.638 1.00 37.92 ? 1508 LYS A CG    1 
ATOM   392   C CD    . LYS A 1 1508 ? 246.676 183.266 187.397 1.00 38.46 ? 1508 LYS A CD    1 
ATOM   393   C CE    . LYS A 1 1508 ? 247.635 182.100 187.574 1.00 37.64 ? 1508 LYS A CE    1 
ATOM   394   N NZ    . LYS A 1 1508 ? 248.598 181.991 186.442 1.00 38.20 ? 1508 LYS A NZ    1 
ATOM   395   N N     . LEU A 1 1509 ? 241.856 183.083 187.961 1.00 38.97 ? 1509 LEU A N     1 
ATOM   396   C CA    . LEU A 1 1509 ? 240.941 181.962 188.139 1.00 39.38 ? 1509 LEU A CA    1 
ATOM   397   C C     . LEU A 1 1509 ? 240.347 181.519 186.807 1.00 38.88 ? 1509 LEU A C     1 
ATOM   398   O O     . LEU A 1 1509 ? 240.100 180.325 186.599 1.00 37.85 ? 1509 LEU A O     1 
ATOM   399   C CB    . LEU A 1 1509 ? 239.836 182.343 189.127 1.00 37.98 ? 1509 LEU A CB    1 
ATOM   400   C CG    . LEU A 1 1509 ? 238.929 181.235 189.675 1.00 40.03 ? 1509 LEU A CG    1 
ATOM   401   C CD1   . LEU A 1 1509 ? 238.516 181.552 191.104 1.00 38.33 ? 1509 LEU A CD1   1 
ATOM   402   C CD2   . LEU A 1 1509 ? 237.695 181.047 188.801 1.00 34.91 ? 1509 LEU A CD2   1 
ATOM   403   N N     . SER A 1 1510 ? 240.110 182.461 185.899 1.00 39.32 ? 1510 SER A N     1 
ATOM   404   C CA    . SER A 1 1510 ? 239.441 182.131 184.651 1.00 42.66 ? 1510 SER A CA    1 
ATOM   405   C C     . SER A 1 1510 ? 240.349 181.291 183.756 1.00 44.60 ? 1510 SER A C     1 
ATOM   406   O O     . SER A 1 1510 ? 241.571 181.469 183.763 1.00 44.29 ? 1510 SER A O     1 
ATOM   407   C CB    . SER A 1 1510 ? 239.023 183.393 183.906 1.00 44.46 ? 1510 SER A CB    1 
ATOM   408   O OG    . SER A 1 1510 ? 240.154 184.124 183.467 1.00 45.18 ? 1510 SER A OG    1 
ATOM   409   N N     . PRO A 1 1511 ? 239.780 180.369 182.981 1.00 50.12 ? 1511 PRO A N     1 
ATOM   410   C CA    . PRO A 1 1511 ? 240.597 179.576 182.049 1.00 49.84 ? 1511 PRO A CA    1 
ATOM   411   C C     . PRO A 1 1511 ? 241.231 180.398 180.942 1.00 48.67 ? 1511 PRO A C     1 
ATOM   412   O O     . PRO A 1 1511 ? 242.277 179.999 180.417 1.00 46.62 ? 1511 PRO A O     1 
ATOM   413   C CB    . PRO A 1 1511 ? 239.592 178.566 181.483 1.00 47.53 ? 1511 PRO A CB    1 
ATOM   414   C CG    . PRO A 1 1511 ? 238.495 178.521 182.505 1.00 45.36 ? 1511 PRO A CG    1 
ATOM   415   C CD    . PRO A 1 1511 ? 238.388 179.900 183.037 1.00 47.13 ? 1511 PRO A CD    1 
ATOM   416   N N     . TYR A 1 1512 ? 240.626 181.522 180.558 1.00 51.38 ? 1512 TYR A N     1 
ATOM   417   C CA    . TYR A 1 1512 ? 241.152 182.358 179.479 1.00 53.85 ? 1512 TYR A CA    1 
ATOM   418   C C     . TYR A 1 1512 ? 242.270 183.225 180.049 1.00 55.11 ? 1512 TYR A C     1 
ATOM   419   O O     . TYR A 1 1512 ? 242.091 184.396 180.394 1.00 52.96 ? 1512 TYR A O     1 
ATOM   420   C CB    . TYR A 1 1512 ? 240.044 183.196 178.854 1.00 53.23 ? 1512 TYR A CB    1 
ATOM   421   C CG    . TYR A 1 1512 ? 240.516 184.117 177.750 1.00 52.28 ? 1512 TYR A CG    1 
ATOM   422   C CD1   . TYR A 1 1512 ? 240.867 183.616 176.504 1.00 52.44 ? 1512 TYR A CD1   1 
ATOM   423   C CD2   . TYR A 1 1512 ? 240.602 185.489 177.951 1.00 51.73 ? 1512 TYR A CD2   1 
ATOM   424   C CE1   . TYR A 1 1512 ? 241.298 184.453 175.492 1.00 52.94 ? 1512 TYR A CE1   1 
ATOM   425   C CE2   . TYR A 1 1512 ? 241.032 186.334 176.946 1.00 53.98 ? 1512 TYR A CE2   1 
ATOM   426   C CZ    . TYR A 1 1512 ? 241.378 185.811 175.719 1.00 54.43 ? 1512 TYR A CZ    1 
ATOM   427   O OH    . TYR A 1 1512 ? 241.804 186.649 174.715 1.00 53.00 ? 1512 TYR A OH    1 
ATOM   428   N N     . TYR A 1 1513 ? 243.454 182.620 180.163 1.00 53.83 ? 1513 TYR A N     1 
ATOM   429   C CA    . TYR A 1 1513 ? 244.619 183.345 180.651 1.00 53.65 ? 1513 TYR A CA    1 
ATOM   430   C C     . TYR A 1 1513 ? 245.890 183.001 179.883 1.00 53.38 ? 1513 TYR A C     1 
ATOM   431   O O     . TYR A 1 1513 ? 246.984 183.342 180.350 1.00 52.30 ? 1513 TYR A O     1 
ATOM   432   C CB    . TYR A 1 1513 ? 244.836 183.082 182.150 1.00 49.48 ? 1513 TYR A CB    1 
ATOM   433   C CG    . TYR A 1 1513 ? 245.268 181.669 182.482 1.00 50.67 ? 1513 TYR A CG    1 
ATOM   434   C CD1   . TYR A 1 1513 ? 244.338 180.646 182.596 1.00 52.16 ? 1513 TYR A CD1   1 
ATOM   435   C CD2   . TYR A 1 1513 ? 246.606 181.363 182.697 1.00 48.97 ? 1513 TYR A CD2   1 
ATOM   436   C CE1   . TYR A 1 1513 ? 244.727 179.356 182.902 1.00 52.39 ? 1513 TYR A CE1   1 
ATOM   437   C CE2   . TYR A 1 1513 ? 247.005 180.077 183.004 1.00 49.89 ? 1513 TYR A CE2   1 
ATOM   438   C CZ    . TYR A 1 1513 ? 246.062 179.078 183.106 1.00 52.15 ? 1513 TYR A CZ    1 
ATOM   439   O OH    . TYR A 1 1513 ? 246.456 177.796 183.412 1.00 49.43 ? 1513 TYR A OH    1 
ATOM   440   N N     . LYS A 1 1514 ? 245.793 182.353 178.725 1.00 48.53 ? 1514 LYS A N     1 
ATOM   441   C CA    . LYS A 1 1514 ? 246.996 181.967 177.989 1.00 49.22 ? 1514 LYS A CA    1 
ATOM   442   C C     . LYS A 1 1514 ? 247.477 183.091 177.077 1.00 49.31 ? 1514 LYS A C     1 
ATOM   443   O O     . LYS A 1 1514 ? 247.793 182.887 175.906 1.00 48.81 ? 1514 LYS A O     1 
ATOM   444   C CB    . LYS A 1 1514 ? 246.728 180.696 177.192 1.00 48.10 ? 1514 LYS A CB    1 
ATOM   445   C CG    . LYS A 1 1514 ? 246.045 179.588 177.982 1.00 48.31 ? 1514 LYS A CG    1 
ATOM   446   C CD    . LYS A 1 1514 ? 246.988 178.953 178.990 1.00 48.23 ? 1514 LYS A CD    1 
ATOM   447   C CE    . LYS A 1 1514 ? 246.338 177.757 179.670 1.00 48.87 ? 1514 LYS A CE    1 
ATOM   448   N NZ    . LYS A 1 1514 ? 247.170 177.225 180.784 1.00 48.18 ? 1514 LYS A NZ    1 
ATOM   449   N N     . VAL A 1 1515 ? 247.531 184.302 177.628 1.00 47.61 ? 1515 VAL A N     1 
ATOM   450   C CA    . VAL A 1 1515 ? 248.237 185.423 177.019 1.00 47.55 ? 1515 VAL A CA    1 
ATOM   451   C C     . VAL A 1 1515 ? 248.984 186.144 178.133 1.00 48.89 ? 1515 VAL A C     1 
ATOM   452   O O     . VAL A 1 1515 ? 249.887 186.950 177.880 1.00 49.55 ? 1515 VAL A O     1 
ATOM   453   C CB    . VAL A 1 1515 ? 247.272 186.359 176.267 1.00 47.79 ? 1515 VAL A CB    1 
ATOM   454   C CG1   . VAL A 1 1515 ? 246.446 187.179 177.242 1.00 46.11 ? 1515 VAL A CG1   1 
ATOM   455   C CG2   . VAL A 1 1515 ? 248.038 187.261 175.305 1.00 46.01 ? 1515 VAL A CG2   1 
ATOM   456   N N     . PHE A 1 1516 ? 248.614 185.839 179.375 1.00 48.08 ? 1516 PHE A N     1 
ATOM   457   C CA    . PHE A 1 1516 ? 249.149 186.457 180.585 1.00 49.08 ? 1516 PHE A CA    1 
ATOM   458   C C     . PHE A 1 1516 ? 249.596 185.383 181.568 1.00 51.03 ? 1516 PHE A C     1 
ATOM   459   O O     . PHE A 1 1516 ? 249.215 185.383 182.741 1.00 49.77 ? 1516 PHE A O     1 
ATOM   460   C CB    . PHE A 1 1516 ? 248.124 187.379 181.241 1.00 47.78 ? 1516 PHE A CB    1 
ATOM   461   C CG    . PHE A 1 1516 ? 247.652 188.499 180.357 1.00 49.71 ? 1516 PHE A CG    1 
ATOM   462   C CD1   . PHE A 1 1516 ? 248.547 189.206 179.571 1.00 49.44 ? 1516 PHE A CD1   1 
ATOM   463   C CD2   . PHE A 1 1516 ? 246.313 188.854 180.323 1.00 50.37 ? 1516 PHE A CD2   1 
ATOM   464   C CE1   . PHE A 1 1516 ? 248.114 190.239 178.761 1.00 50.09 ? 1516 PHE A CE1   1 
ATOM   465   C CE2   . PHE A 1 1516 ? 245.875 189.887 179.514 1.00 50.26 ? 1516 PHE A CE2   1 
ATOM   466   C CZ    . PHE A 1 1516 ? 246.777 190.580 178.733 1.00 48.83 ? 1516 PHE A CZ    1 
ATOM   467   N N     . GLU A 1 1517 ? 250.398 184.431 181.079 1.00 51.35 ? 1517 GLU A N     1 
ATOM   468   C CA    . GLU A 1 1517 ? 250.818 183.299 181.903 1.00 50.09 ? 1517 GLU A CA    1 
ATOM   469   C C     . GLU A 1 1517 ? 251.462 183.754 183.207 1.00 50.86 ? 1517 GLU A C     1 
ATOM   470   O O     . GLU A 1 1517 ? 251.266 183.129 184.256 1.00 48.89 ? 1517 GLU A O     1 
ATOM   471   C CB    . GLU A 1 1517 ? 251.777 182.406 181.115 1.00 46.89 ? 1517 GLU A CB    1 
ATOM   472   C CG    . GLU A 1 1517 ? 251.169 181.792 179.865 1.00 48.63 ? 1517 GLU A CG    1 
ATOM   473   C CD    . GLU A 1 1517 ? 250.111 180.751 180.181 1.00 51.82 ? 1517 GLU A CD    1 
ATOM   474   O OE1   . GLU A 1 1517 ? 248.955 181.135 180.457 1.00 51.10 ? 1517 GLU A OE1   1 
ATOM   475   O OE2   . GLU A 1 1517 ? 250.437 179.545 180.154 1.00 51.16 ? 1517 GLU A OE2   1 
ATOM   476   N N     . GLU A 1 1518 ? 252.234 184.840 183.165 1.00 49.38 ? 1518 GLU A N     1 
ATOM   477   C CA    . GLU A 1 1518 ? 252.756 185.433 184.398 1.00 48.98 ? 1518 GLU A CA    1 
ATOM   478   C C     . GLU A 1 1518 ? 252.831 186.946 184.184 1.00 49.37 ? 1518 GLU A C     1 
ATOM   479   O O     . GLU A 1 1518 ? 253.836 187.470 183.699 1.00 49.23 ? 1518 GLU A O     1 
ATOM   480   C CB    . GLU A 1 1518 ? 254.111 184.848 184.769 1.00 47.32 ? 1518 GLU A CB    1 
ATOM   481   C CG    . GLU A 1 1518 ? 254.703 185.422 186.045 1.00 48.69 ? 1518 GLU A CG    1 
ATOM   482   C CD    . GLU A 1 1518 ? 253.672 185.570 187.146 1.00 49.37 ? 1518 GLU A CD    1 
ATOM   483   O OE1   . GLU A 1 1518 ? 253.122 184.540 187.589 1.00 47.99 ? 1518 GLU A OE1   1 
ATOM   484   O OE2   . GLU A 1 1518 ? 253.409 186.717 187.566 1.00 47.14 ? 1518 GLU A OE2   1 
ATOM   485   N N     . ASP A 1 1519 ? 251.748 187.635 184.547 1.00 48.18 ? 1519 ASP A N     1 
ATOM   486   C CA    . ASP A 1 1519 ? 251.726 189.091 184.540 1.00 47.73 ? 1519 ASP A CA    1 
ATOM   487   C C     . ASP A 1 1519 ? 251.000 189.701 185.730 1.00 47.83 ? 1519 ASP A C     1 
ATOM   488   O O     . ASP A 1 1519 ? 251.169 190.899 185.973 1.00 51.01 ? 1519 ASP A O     1 
ATOM   489   C CB    . ASP A 1 1519 ? 251.086 189.612 183.245 1.00 48.12 ? 1519 ASP A CB    1 
ATOM   490   C CG    . ASP A 1 1519 ? 251.457 191.053 182.949 1.00 48.48 ? 1519 ASP A CG    1 
ATOM   491   O OD1   . ASP A 1 1519 ? 252.524 191.503 183.419 1.00 47.59 ? 1519 ASP A OD1   1 
ATOM   492   O OD2   . ASP A 1 1519 ? 250.683 191.737 182.247 1.00 47.81 ? 1519 ASP A OD2   1 
ATOM   493   N N     . ALA A 1 1520 ? 250.211 188.932 186.480 1.00 42.48 ? 1520 ALA A N     1 
ATOM   494   C CA    . ALA A 1 1520 ? 249.430 189.460 187.591 1.00 45.77 ? 1520 ALA A CA    1 
ATOM   495   C C     . ALA A 1 1520 ? 249.903 188.985 188.955 1.00 46.77 ? 1520 ALA A C     1 
ATOM   496   O O     . ALA A 1 1520 ? 249.680 189.685 189.945 1.00 44.40 ? 1520 ALA A O     1 
ATOM   497   C CB    . ALA A 1 1520 ? 247.951 189.089 187.426 1.00 42.56 ? 1520 ALA A CB    1 
ATOM   498   N N     . LEU A 1 1521 ? 250.540 187.814 189.034 1.00 45.24 ? 1521 LEU A N     1 
ATOM   499   C CA    . LEU A 1 1521 ? 251.055 187.341 190.316 1.00 43.94 ? 1521 LEU A CA    1 
ATOM   500   C C     . LEU A 1 1521 ? 252.133 188.274 190.849 1.00 44.33 ? 1521 LEU A C     1 
ATOM   501   O O     . LEU A 1 1521 ? 252.213 188.517 192.059 1.00 42.04 ? 1521 LEU A O     1 
ATOM   502   C CB    . LEU A 1 1521 ? 251.594 185.915 190.184 1.00 42.54 ? 1521 LEU A CB    1 
ATOM   503   C CG    . LEU A 1 1521 ? 250.611 184.736 190.187 1.00 43.60 ? 1521 LEU A CG    1 
ATOM   504   C CD1   . LEU A 1 1521 ? 249.934 184.608 191.546 1.00 40.92 ? 1521 LEU A CD1   1 
ATOM   505   C CD2   . LEU A 1 1521 ? 249.577 184.823 189.072 1.00 42.57 ? 1521 LEU A CD2   1 
ATOM   506   N N     . SER A 1 1522 ? 252.973 188.807 189.960 1.00 45.64 ? 1522 SER A N     1 
ATOM   507   C CA    . SER A 1 1522 ? 253.945 189.816 190.357 1.00 46.92 ? 1522 SER A CA    1 
ATOM   508   C C     . SER A 1 1522 ? 253.295 191.144 190.719 1.00 48.24 ? 1522 SER A C     1 
ATOM   509   O O     . SER A 1 1522 ? 253.970 192.007 191.289 1.00 47.08 ? 1522 SER A O     1 
ATOM   510   C CB    . SER A 1 1522 ? 254.968 190.028 189.239 1.00 45.46 ? 1522 SER A CB    1 
ATOM   511   O OG    . SER A 1 1522 ? 254.329 190.158 187.981 1.00 46.53 ? 1522 SER A OG    1 
ATOM   512   N N     . TRP A 1 1523 ? 252.012 191.329 190.404 1.00 47.80 ? 1523 TRP A N     1 
ATOM   513   C CA    . TRP A 1 1523 ? 251.304 192.557 190.732 1.00 48.88 ? 1523 TRP A CA    1 
ATOM   514   C C     . TRP A 1 1523 ? 250.168 192.360 191.726 1.00 47.87 ? 1523 TRP A C     1 
ATOM   515   O O     . TRP A 1 1523 ? 249.693 193.346 192.298 1.00 43.97 ? 1523 TRP A O     1 
ATOM   516   C CB    . TRP A 1 1523 ? 250.758 193.213 189.455 1.00 47.66 ? 1523 TRP A CB    1 
ATOM   517   C CG    . TRP A 1 1523 ? 251.797 193.995 188.711 1.00 47.83 ? 1523 TRP A CG    1 
ATOM   518   C CD1   . TRP A 1 1523 ? 253.097 193.637 188.504 1.00 48.07 ? 1523 TRP A CD1   1 
ATOM   519   C CD2   . TRP A 1 1523 ? 251.629 195.274 188.090 1.00 49.52 ? 1523 TRP A CD2   1 
ATOM   520   N NE1   . TRP A 1 1523 ? 253.747 194.610 187.786 1.00 52.33 ? 1523 TRP A NE1   1 
ATOM   521   C CE2   . TRP A 1 1523 ? 252.868 195.626 187.519 1.00 50.20 ? 1523 TRP A CE2   1 
ATOM   522   C CE3   . TRP A 1 1523 ? 250.552 196.154 187.957 1.00 48.18 ? 1523 TRP A CE3   1 
ATOM   523   C CZ2   . TRP A 1 1523 ? 253.059 196.820 186.827 1.00 46.97 ? 1523 TRP A CZ2   1 
ATOM   524   C CZ3   . TRP A 1 1523 ? 250.744 197.338 187.269 1.00 48.81 ? 1523 TRP A CZ3   1 
ATOM   525   C CH2   . TRP A 1 1523 ? 251.988 197.660 186.713 1.00 46.76 ? 1523 TRP A CH2   1 
ATOM   526   N N     . GLU A 1 1524 ? 249.721 191.122 191.954 1.00 47.73 ? 1524 GLU A N     1 
ATOM   527   C CA    . GLU A 1 1524 ? 248.741 190.882 193.010 1.00 48.39 ? 1524 GLU A CA    1 
ATOM   528   C C     . GLU A 1 1524 ? 249.320 191.224 194.378 1.00 47.60 ? 1524 GLU A C     1 
ATOM   529   O O     . GLU A 1 1524 ? 248.647 191.845 195.212 1.00 47.05 ? 1524 GLU A O     1 
ATOM   530   C CB    . GLU A 1 1524 ? 248.272 189.429 192.973 1.00 46.29 ? 1524 GLU A CB    1 
ATOM   531   C CG    . GLU A 1 1524 ? 247.135 189.122 193.932 1.00 46.52 ? 1524 GLU A CG    1 
ATOM   532   C CD    . GLU A 1 1524 ? 246.641 187.695 193.810 1.00 49.07 ? 1524 GLU A CD    1 
ATOM   533   O OE1   . GLU A 1 1524 ? 247.378 186.773 194.217 1.00 48.36 ? 1524 GLU A OE1   1 
ATOM   534   O OE2   . GLU A 1 1524 ? 245.517 187.494 193.304 1.00 48.22 ? 1524 GLU A OE2   1 
ATOM   535   N N     . ASP A 1 1525 ? 250.573 190.831 194.624 1.00 48.21 ? 1525 ASP A N     1 
ATOM   536   C CA    . ASP A 1 1525 ? 251.235 191.220 195.863 1.00 47.00 ? 1525 ASP A CA    1 
ATOM   537   C C     . ASP A 1 1525 ? 251.436 192.726 195.934 1.00 46.84 ? 1525 ASP A C     1 
ATOM   538   O O     . ASP A 1 1525 ? 251.358 193.311 197.019 1.00 46.08 ? 1525 ASP A O     1 
ATOM   539   C CB    . ASP A 1 1525 ? 252.572 190.490 196.001 1.00 46.39 ? 1525 ASP A CB    1 
ATOM   540   C CG    . ASP A 1 1525 ? 253.583 190.919 194.957 1.00 48.37 ? 1525 ASP A CG    1 
ATOM   541   O OD1   . ASP A 1 1525 ? 253.346 190.660 193.759 1.00 46.61 ? 1525 ASP A OD1   1 
ATOM   542   O OD2   . ASP A 1 1525 ? 254.614 191.517 195.333 1.00 48.09 ? 1525 ASP A OD2   1 
ATOM   543   N N     . LYS A 1 1526 ? 251.690 193.372 194.793 1.00 43.71 ? 1526 LYS A N     1 
ATOM   544   C CA    . LYS A 1 1526 ? 251.789 194.828 194.775 1.00 46.92 ? 1526 LYS A CA    1 
ATOM   545   C C     . LYS A 1 1526 ? 250.473 195.472 195.191 1.00 47.08 ? 1526 LYS A C     1 
ATOM   546   O O     . LYS A 1 1526 ? 250.459 196.424 195.978 1.00 43.09 ? 1526 LYS A O     1 
ATOM   547   C CB    . LYS A 1 1526 ? 252.199 195.307 193.382 1.00 45.96 ? 1526 LYS A CB    1 
ATOM   548   C CG    . LYS A 1 1526 ? 253.650 195.037 193.022 1.00 45.77 ? 1526 LYS A CG    1 
ATOM   549   C CD    . LYS A 1 1526 ? 253.911 195.355 191.558 1.00 44.25 ? 1526 LYS A CD    1 
ATOM   550   C CE    . LYS A 1 1526 ? 255.387 195.597 191.293 1.00 45.70 ? 1526 LYS A CE    1 
ATOM   551   N NZ    . LYS A 1 1526 ? 255.636 195.978 189.876 1.00 44.12 ? 1526 LYS A NZ    1 
ATOM   552   N N     . LEU A 1 1527 ? 249.356 194.962 194.667 1.00 45.20 ? 1527 LEU A N     1 
ATOM   553   C CA    . LEU A 1 1527 ? 248.047 195.492 195.039 1.00 43.65 ? 1527 LEU A CA    1 
ATOM   554   C C     . LEU A 1 1527 ? 247.757 195.259 196.517 1.00 43.31 ? 1527 LEU A C     1 
ATOM   555   O O     . LEU A 1 1527 ? 247.204 196.133 197.195 1.00 41.58 ? 1527 LEU A O     1 
ATOM   556   C CB    . LEU A 1 1527 ? 246.958 194.863 194.172 1.00 41.90 ? 1527 LEU A CB    1 
ATOM   557   C CG    . LEU A 1 1527 ? 247.013 195.179 192.676 1.00 42.26 ? 1527 LEU A CG    1 
ATOM   558   C CD1   . LEU A 1 1527 ? 246.330 194.086 191.871 1.00 43.08 ? 1527 LEU A CD1   1 
ATOM   559   C CD2   . LEU A 1 1527 ? 246.385 196.532 192.388 1.00 41.96 ? 1527 LEU A CD2   1 
ATOM   560   N N     . ASN A 1 1528 ? 248.119 194.081 197.031 1.00 42.55 ? 1528 ASN A N     1 
ATOM   561   C CA    . ASN A 1 1528 ? 247.939 193.812 198.456 1.00 42.46 ? 1528 ASN A CA    1 
ATOM   562   C C     . ASN A 1 1528 ? 248.766 194.769 199.306 1.00 42.96 ? 1528 ASN A C     1 
ATOM   563   O O     . ASN A 1 1528 ? 248.293 195.267 200.336 1.00 43.76 ? 1528 ASN A O     1 
ATOM   564   C CB    . ASN A 1 1528 ? 248.308 192.362 198.769 1.00 42.95 ? 1528 ASN A CB    1 
ATOM   565   C CG    . ASN A 1 1528 ? 247.349 191.368 198.145 1.00 44.37 ? 1528 ASN A CG    1 
ATOM   566   O OD1   . ASN A 1 1528 ? 246.132 191.504 198.263 1.00 45.33 ? 1528 ASN A OD1   1 
ATOM   567   N ND2   . ASN A 1 1528 ? 247.896 190.360 197.475 1.00 44.32 ? 1528 ASN A ND2   1 
ATOM   568   N N     . ARG A 1 1529 ? 250.011 195.028 198.895 1.00 41.72 ? 1529 ARG A N     1 
ATOM   569   C CA    . ARG A 1 1529 ? 250.854 195.973 199.619 1.00 43.36 ? 1529 ARG A CA    1 
ATOM   570   C C     . ARG A 1 1529 ? 250.257 197.373 199.590 1.00 44.63 ? 1529 ARG A C     1 
ATOM   571   O O     . ARG A 1 1529 ? 250.254 198.074 200.608 1.00 46.20 ? 1529 ARG A O     1 
ATOM   572   C CB    . ARG A 1 1529 ? 252.263 195.979 199.028 1.00 44.72 ? 1529 ARG A CB    1 
ATOM   573   C CG    . ARG A 1 1529 ? 253.096 194.759 199.384 1.00 44.59 ? 1529 ARG A CG    1 
ATOM   574   C CD    . ARG A 1 1529 ? 254.495 194.862 198.802 1.00 44.70 ? 1529 ARG A CD    1 
ATOM   575   N NE    . ARG A 1 1529 ? 255.203 196.036 199.295 1.00 46.41 ? 1529 ARG A NE    1 
ATOM   576   C CZ    . ARG A 1 1529 ? 256.388 196.437 198.855 1.00 45.79 ? 1529 ARG A CZ    1 
ATOM   577   N NH1   . ARG A 1 1529 ? 257.029 195.782 197.901 1.00 43.32 ? 1529 ARG A NH1   1 
ATOM   578   N NH2   . ARG A 1 1529 ? 256.944 197.523 199.385 1.00 43.91 ? 1529 ARG A NH2   1 
ATOM   579   N N     . ILE A 1 1530 ? 249.750 197.797 198.429 1.00 41.16 ? 1530 ILE A N     1 
ATOM   580   C CA    . ILE A 1 1530 ? 249.085 199.095 198.330 1.00 41.49 ? 1530 ILE A CA    1 
ATOM   581   C C     . ILE A 1 1530 ? 247.921 199.167 199.309 1.00 40.47 ? 1530 ILE A C     1 
ATOM   582   O O     . ILE A 1 1530 ? 247.787 200.129 200.077 1.00 39.83 ? 1530 ILE A O     1 
ATOM   583   C CB    . ILE A 1 1530 ? 248.610 199.349 196.887 1.00 42.44 ? 1530 ILE A CB    1 
ATOM   584   C CG1   . ILE A 1 1530 ? 249.796 199.456 195.927 1.00 41.87 ? 1530 ILE A CG1   1 
ATOM   585   C CG2   . ILE A 1 1530 ? 247.752 200.604 196.820 1.00 42.44 ? 1530 ILE A CG2   1 
ATOM   586   C CD1   . ILE A 1 1530 ? 250.625 200.690 196.123 1.00 40.97 ? 1530 ILE A CD1   1 
ATOM   587   N N     . MET A 1 1531 ? 247.068 198.140 199.299 1.00 39.82 ? 1531 MET A N     1 
ATOM   588   C CA    . MET A 1 1531 ? 245.881 198.146 200.146 1.00 40.90 ? 1531 MET A CA    1 
ATOM   589   C C     . MET A 1 1531 ? 246.256 198.215 201.620 1.00 39.02 ? 1531 MET A C     1 
ATOM   590   O O     . MET A 1 1531 ? 245.708 199.028 202.372 1.00 41.23 ? 1531 MET A O     1 
ATOM   591   C CB    . MET A 1 1531 ? 245.028 196.910 199.863 1.00 38.21 ? 1531 MET A CB    1 
ATOM   592   C CG    . MET A 1 1531 ? 243.575 197.050 200.285 1.00 37.98 ? 1531 MET A CG    1 
ATOM   593   S SD    . MET A 1 1531 ? 242.690 198.307 199.345 1.00 46.58 ? 1531 MET A SD    1 
ATOM   594   C CE    . MET A 1 1531 ? 241.042 197.605 199.310 1.00 41.01 ? 1531 MET A CE    1 
ATOM   595   N N     . ALA A 1 1532 ? 247.202 197.377 202.050 1.00 33.57 ? 1532 ALA A N     1 
ATOM   596   C CA    . ALA A 1 1532 ? 247.590 197.366 203.458 1.00 36.01 ? 1532 ALA A CA    1 
ATOM   597   C C     . ALA A 1 1532 ? 248.226 198.690 203.863 1.00 38.89 ? 1532 ALA A C     1 
ATOM   598   O O     . ALA A 1 1532 ? 247.824 199.312 204.859 1.00 40.48 ? 1532 ALA A O     1 
ATOM   599   C CB    . ALA A 1 1532 ? 248.543 196.202 203.731 1.00 35.50 ? 1532 ALA A CB    1 
ATOM   600   N N     . LEU A 1 1533 ? 249.213 199.150 203.088 1.00 35.47 ? 1533 LEU A N     1 
ATOM   601   C CA    . LEU A 1 1533 ? 249.878 200.405 203.409 1.00 35.32 ? 1533 LEU A CA    1 
ATOM   602   C C     . LEU A 1 1533 ? 248.877 201.541 203.523 1.00 38.32 ? 1533 LEU A C     1 
ATOM   603   O O     . LEU A 1 1533 ? 248.921 202.317 204.480 1.00 38.59 ? 1533 LEU A O     1 
ATOM   604   C CB    . LEU A 1 1533 ? 250.933 200.732 202.353 1.00 34.26 ? 1533 LEU A CB    1 
ATOM   605   C CG    . LEU A 1 1533 ? 251.932 201.825 202.740 1.00 38.21 ? 1533 LEU A CG    1 
ATOM   606   C CD1   . LEU A 1 1533 ? 252.885 201.338 203.818 1.00 36.42 ? 1533 LEU A CD1   1 
ATOM   607   C CD2   . LEU A 1 1533 ? 252.696 202.315 201.523 1.00 37.82 ? 1533 LEU A CD2   1 
ATOM   608   N N     . PHE A 1 1534 ? 247.931 201.633 202.590 1.00 39.60 ? 1534 PHE A N     1 
ATOM   609   C CA    . PHE A 1 1534 ? 247.104 202.830 202.568 1.00 40.10 ? 1534 PHE A CA    1 
ATOM   610   C C     . PHE A 1 1534 ? 245.903 202.737 203.504 1.00 40.57 ? 1534 PHE A C     1 
ATOM   611   O O     . PHE A 1 1534 ? 245.454 203.769 204.018 1.00 40.99 ? 1534 PHE A O     1 
ATOM   612   C CB    . PHE A 1 1534 ? 246.666 203.129 201.139 1.00 37.67 ? 1534 PHE A CB    1 
ATOM   613   C CG    . PHE A 1 1534 ? 247.696 203.887 200.349 1.00 39.86 ? 1534 PHE A CG    1 
ATOM   614   C CD1   . PHE A 1 1534 ? 248.751 203.220 199.750 1.00 39.96 ? 1534 PHE A CD1   1 
ATOM   615   C CD2   . PHE A 1 1534 ? 247.643 205.267 200.253 1.00 40.38 ? 1534 PHE A CD2   1 
ATOM   616   C CE1   . PHE A 1 1534 ? 249.710 203.910 199.034 1.00 39.80 ? 1534 PHE A CE1   1 
ATOM   617   C CE2   . PHE A 1 1534 ? 248.600 205.963 199.539 1.00 41.66 ? 1534 PHE A CE2   1 
ATOM   618   C CZ    . PHE A 1 1534 ? 249.635 205.283 198.930 1.00 39.90 ? 1534 PHE A CZ    1 
ATOM   619   N N     . ASP A 1 1535 ? 245.385 201.536 203.780 1.00 35.47 ? 1535 ASP A N     1 
ATOM   620   C CA    . ASP A 1 1535 ? 244.333 201.450 204.782 1.00 36.32 ? 1535 ASP A CA    1 
ATOM   621   C C     . ASP A 1 1535 ? 244.880 201.499 206.203 1.00 37.87 ? 1535 ASP A C     1 
ATOM   622   O O     . ASP A 1 1535 ? 244.097 201.676 207.142 1.00 39.42 ? 1535 ASP A O     1 
ATOM   623   C CB    . ASP A 1 1535 ? 243.462 200.199 204.563 1.00 35.35 ? 1535 ASP A CB    1 
ATOM   624   C CG    . ASP A 1 1535 ? 244.135 198.898 204.988 1.00 37.68 ? 1535 ASP A CG    1 
ATOM   625   O OD1   . ASP A 1 1535 ? 245.317 198.895 205.375 1.00 37.75 ? 1535 ASP A OD1   1 
ATOM   626   O OD2   . ASP A 1 1535 ? 243.455 197.852 204.928 1.00 38.95 ? 1535 ASP A OD2   1 
ATOM   627   N N     . VAL A 1 1536 ? 246.193 201.345 206.385 1.00 36.15 ? 1536 VAL A N     1 
ATOM   628   C CA    . VAL A 1 1536 ? 246.804 201.788 207.635 1.00 37.64 ? 1536 VAL A CA    1 
ATOM   629   C C     . VAL A 1 1536 ? 247.110 203.287 207.602 1.00 37.19 ? 1536 VAL A C     1 
ATOM   630   O O     . VAL A 1 1536 ? 246.985 203.968 208.626 1.00 37.83 ? 1536 VAL A O     1 
ATOM   631   C CB    . VAL A 1 1536 ? 248.069 200.967 207.941 1.00 35.46 ? 1536 VAL A CB    1 
ATOM   632   C CG1   . VAL A 1 1536 ? 248.675 201.392 209.267 1.00 32.51 ? 1536 VAL A CG1   1 
ATOM   633   C CG2   . VAL A 1 1536 ? 247.738 199.486 207.978 1.00 34.79 ? 1536 VAL A CG2   1 
ATOM   634   N N     . TRP A 1 1537 ? 247.486 203.814 206.433 1.00 37.45 ? 1537 TRP A N     1 
ATOM   635   C CA    . TRP A 1 1537 ? 247.860 205.219 206.311 1.00 38.47 ? 1537 TRP A CA    1 
ATOM   636   C C     . TRP A 1 1537 ? 246.681 206.139 206.598 1.00 40.42 ? 1537 TRP A C     1 
ATOM   637   O O     . TRP A 1 1537 ? 246.854 207.208 207.192 1.00 38.65 ? 1537 TRP A O     1 
ATOM   638   C CB    . TRP A 1 1537 ? 248.401 205.484 204.907 1.00 38.78 ? 1537 TRP A CB    1 
ATOM   639   C CG    . TRP A 1 1537 ? 249.167 206.759 204.770 1.00 42.22 ? 1537 TRP A CG    1 
ATOM   640   C CD1   . TRP A 1 1537 ? 248.662 208.025 204.780 1.00 41.60 ? 1537 TRP A CD1   1 
ATOM   641   C CD2   . TRP A 1 1537 ? 250.574 206.889 204.542 1.00 41.54 ? 1537 TRP A CD2   1 
ATOM   642   N NE1   . TRP A 1 1537 ? 249.672 208.938 204.605 1.00 40.60 ? 1537 TRP A NE1   1 
ATOM   643   C CE2   . TRP A 1 1537 ? 250.856 208.266 204.452 1.00 42.29 ? 1537 TRP A CE2   1 
ATOM   644   C CE3   . TRP A 1 1537 ? 251.624 205.976 204.415 1.00 39.05 ? 1537 TRP A CE3   1 
ATOM   645   C CZ2   . TRP A 1 1537 ? 252.144 208.751 204.243 1.00 39.74 ? 1537 TRP A CZ2   1 
ATOM   646   C CZ3   . TRP A 1 1537 ? 252.902 206.460 204.209 1.00 42.01 ? 1537 TRP A CZ3   1 
ATOM   647   C CH2   . TRP A 1 1537 ? 253.151 207.835 204.124 1.00 41.81 ? 1537 TRP A CH2   1 
ATOM   648   N N     . ILE A 1 1538 ? 245.483 205.762 206.147 1.00 41.12 ? 1538 ILE A N     1 
ATOM   649   C CA    . ILE A 1 1538 ? 244.312 206.608 206.374 1.00 43.89 ? 1538 ILE A CA    1 
ATOM   650   C C     . ILE A 1 1538 ? 244.017 206.730 207.867 1.00 44.01 ? 1538 ILE A C     1 
ATOM   651   O O     . ILE A 1 1538 ? 243.759 207.829 208.378 1.00 40.39 ? 1538 ILE A O     1 
ATOM   652   C CB    . ILE A 1 1538 ? 243.100 206.080 205.579 1.00 41.69 ? 1538 ILE A CB    1 
ATOM   653   C CG1   . ILE A 1 1538 ? 241.920 207.049 205.695 1.00 42.41 ? 1538 ILE A CG1   1 
ATOM   654   C CG2   . ILE A 1 1538 ? 242.720 204.660 205.994 1.00 40.06 ? 1538 ILE A CG2   1 
ATOM   655   C CD1   . ILE A 1 1538 ? 240.809 206.773 204.710 1.00 41.85 ? 1538 ILE A CD1   1 
ATOM   656   N N     . ASP A 1 1539 ? 244.071 205.610 208.594 1.00 40.15 ? 1539 ASP A N     1 
ATOM   657   C CA    . ASP A 1 1539 ? 243.886 205.658 210.039 1.00 39.18 ? 1539 ASP A CA    1 
ATOM   658   C C     . ASP A 1 1539 ? 244.986 206.474 210.700 1.00 41.91 ? 1539 ASP A C     1 
ATOM   659   O O     . ASP A 1 1539 ? 244.720 207.271 211.610 1.00 43.33 ? 1539 ASP A O     1 
ATOM   660   C CB    . ASP A 1 1539 ? 243.851 204.240 210.608 1.00 39.30 ? 1539 ASP A CB    1 
ATOM   661   C CG    . ASP A 1 1539 ? 243.913 204.216 212.121 1.00 41.15 ? 1539 ASP A CG    1 
ATOM   662   O OD1   . ASP A 1 1539 ? 243.220 205.036 212.760 1.00 41.60 ? 1539 ASP A OD1   1 
ATOM   663   O OD2   . ASP A 1 1539 ? 244.658 203.379 212.672 1.00 42.25 ? 1539 ASP A OD2   1 
ATOM   664   N N     . VAL A 1 1540 ? 246.229 206.297 210.242 1.00 39.38 ? 1540 VAL A N     1 
ATOM   665   C CA    . VAL A 1 1540 ? 247.346 207.052 210.802 1.00 38.04 ? 1540 VAL A CA    1 
ATOM   666   C C     . VAL A 1 1540 ? 247.116 208.547 210.644 1.00 37.83 ? 1540 VAL A C     1 
ATOM   667   O O     . VAL A 1 1540 ? 247.263 209.315 211.601 1.00 39.22 ? 1540 VAL A O     1 
ATOM   668   C CB    . VAL A 1 1540 ? 248.667 206.617 210.141 1.00 37.05 ? 1540 VAL A CB    1 
ATOM   669   C CG1   . VAL A 1 1540 ? 249.726 207.682 210.340 1.00 35.41 ? 1540 VAL A CG1   1 
ATOM   670   C CG2   . VAL A 1 1540 ? 249.133 205.295 210.712 1.00 33.86 ? 1540 VAL A CG2   1 
ATOM   671   N N     . GLN A 1 1541 ? 246.740 208.984 209.441 1.00 37.06 ? 1541 GLN A N     1 
ATOM   672   C CA    . GLN A 1 1541 ? 246.609 210.414 209.188 1.00 40.47 ? 1541 GLN A CA    1 
ATOM   673   C C     . GLN A 1 1541 ? 245.405 210.997 209.920 1.00 41.39 ? 1541 GLN A C     1 
ATOM   674   O O     . GLN A 1 1541 ? 245.472 212.115 210.443 1.00 42.00 ? 1541 GLN A O     1 
ATOM   675   C CB    . GLN A 1 1541 ? 246.538 210.686 207.680 1.00 41.83 ? 1541 GLN A CB    1 
ATOM   676   C CG    . GLN A 1 1541 ? 245.339 210.104 206.947 1.00 43.32 ? 1541 GLN A CG    1 
ATOM   677   C CD    . GLN A 1 1541 ? 244.114 210.999 207.006 1.00 43.46 ? 1541 GLN A CD    1 
ATOM   678   O OE1   . GLN A 1 1541 ? 244.228 212.222 207.083 1.00 39.28 ? 1541 GLN A OE1   1 
ATOM   679   N NE2   . GLN A 1 1541 ? 242.935 210.390 206.974 1.00 44.00 ? 1541 GLN A NE2   1 
ATOM   680   N N     . ARG A 1 1542 ? 244.298 210.248 209.990 1.00 39.86 ? 1542 ARG A N     1 
ATOM   681   C CA    . ARG A 1 1542 ? 243.140 210.742 210.730 1.00 42.98 ? 1542 ARG A CA    1 
ATOM   682   C C     . ARG A 1 1542 ? 243.457 210.898 212.212 1.00 39.67 ? 1542 ARG A C     1 
ATOM   683   O O     . ARG A 1 1542 ? 243.159 211.941 212.815 1.00 39.34 ? 1542 ARG A O     1 
ATOM   684   C CB    . ARG A 1 1542 ? 241.948 209.808 210.531 1.00 41.84 ? 1542 ARG A CB    1 
ATOM   685   C CG    . ARG A 1 1542 ? 240.608 210.523 210.511 1.00 42.24 ? 1542 ARG A CG    1 
ATOM   686   C CD    . ARG A 1 1542 ? 239.466 209.575 210.830 1.00 43.42 ? 1542 ARG A CD    1 
ATOM   687   N NE    . ARG A 1 1542 ? 239.524 208.358 210.030 1.00 43.41 ? 1542 ARG A NE    1 
ATOM   688   C CZ    . ARG A 1 1542 ? 239.423 207.132 210.523 1.00 43.12 ? 1542 ARG A CZ    1 
ATOM   689   N NH1   . ARG A 1 1542 ? 239.263 206.920 211.819 1.00 39.17 ? 1542 ARG A NH1   1 
ATOM   690   N NH2   . ARG A 1 1542 ? 239.482 206.093 209.695 1.00 43.28 ? 1542 ARG A NH2   1 
ATOM   691   N N     . ARG A 1 1543 ? 244.076 209.880 212.814 1.00 32.94 ? 1543 ARG A N     1 
ATOM   692   C CA    . ARG A 1 1543 ? 244.449 209.981 214.219 1.00 33.80 ? 1543 ARG A CA    1 
ATOM   693   C C     . ARG A 1 1543 ? 245.441 211.114 214.440 1.00 35.32 ? 1543 ARG A C     1 
ATOM   694   O O     . ARG A 1 1543 ? 245.334 211.863 215.420 1.00 37.71 ? 1543 ARG A O     1 
ATOM   695   C CB    . ARG A 1 1543 ? 245.031 208.652 214.698 1.00 33.72 ? 1543 ARG A CB    1 
ATOM   696   C CG    . ARG A 1 1543 ? 244.001 207.640 215.160 1.00 33.66 ? 1543 ARG A CG    1 
ATOM   697   C CD    . ARG A 1 1543 ? 244.662 206.314 215.495 1.00 35.28 ? 1543 ARG A CD    1 
ATOM   698   N NE    . ARG A 1 1543 ? 243.729 205.368 216.093 1.00 36.61 ? 1543 ARG A NE    1 
ATOM   699   C CZ    . ARG A 1 1543 ? 244.012 204.097 216.344 1.00 35.81 ? 1543 ARG A CZ    1 
ATOM   700   N NH1   . ARG A 1 1543 ? 245.197 203.584 216.060 1.00 36.26 ? 1543 ARG A NH1   1 
ATOM   701   N NH2   . ARG A 1 1543 ? 243.081 203.322 216.894 1.00 34.91 ? 1543 ARG A NH2   1 
ATOM   702   N N     . TRP A 1 1544 ? 246.411 211.265 213.532 1.00 34.50 ? 1544 TRP A N     1 
ATOM   703   C CA    . TRP A 1 1544 ? 247.418 212.303 213.702 1.00 33.43 ? 1544 TRP A CA    1 
ATOM   704   C C     . TRP A 1 1544 ? 246.801 213.690 213.635 1.00 36.78 ? 1544 TRP A C     1 
ATOM   705   O O     . TRP A 1 1544 ? 247.146 214.559 214.439 1.00 35.66 ? 1544 TRP A O     1 
ATOM   706   C CB    . TRP A 1 1544 ? 248.519 212.163 212.652 1.00 32.32 ? 1544 TRP A CB    1 
ATOM   707   C CG    . TRP A 1 1544 ? 249.626 213.157 212.849 1.00 34.85 ? 1544 TRP A CG    1 
ATOM   708   C CD1   . TRP A 1 1544 ? 250.775 212.972 213.560 1.00 35.35 ? 1544 TRP A CD1   1 
ATOM   709   C CD2   . TRP A 1 1544 ? 249.680 214.498 212.344 1.00 36.08 ? 1544 TRP A CD2   1 
ATOM   710   N NE1   . TRP A 1 1544 ? 251.544 214.109 213.523 1.00 36.95 ? 1544 TRP A NE1   1 
ATOM   711   C CE2   . TRP A 1 1544 ? 250.893 215.061 212.784 1.00 35.83 ? 1544 TRP A CE2   1 
ATOM   712   C CE3   . TRP A 1 1544 ? 248.821 215.275 211.560 1.00 33.92 ? 1544 TRP A CE3   1 
ATOM   713   C CZ2   . TRP A 1 1544 ? 251.269 216.364 212.467 1.00 31.68 ? 1544 TRP A CZ2   1 
ATOM   714   C CZ3   . TRP A 1 1544 ? 249.196 216.567 211.248 1.00 33.57 ? 1544 TRP A CZ3   1 
ATOM   715   C CH2   . TRP A 1 1544 ? 250.409 217.099 211.700 1.00 32.69 ? 1544 TRP A CH2   1 
ATOM   716   N N     . VAL A 1 1545 ? 245.891 213.928 212.686 1.00 34.84 ? 1545 VAL A N     1 
ATOM   717   C CA    . VAL A 1 1545 ? 245.296 215.258 212.588 1.00 35.05 ? 1545 VAL A CA    1 
ATOM   718   C C     . VAL A 1 1545 ? 244.399 215.530 213.790 1.00 37.88 ? 1545 VAL A C     1 
ATOM   719   O O     . VAL A 1 1545 ? 244.384 216.648 214.326 1.00 37.58 ? 1545 VAL A O     1 
ATOM   720   C CB    . VAL A 1 1545 ? 244.546 215.443 211.252 1.00 34.29 ? 1545 VAL A CB    1 
ATOM   721   C CG1   . VAL A 1 1545 ? 245.511 215.328 210.079 1.00 38.43 ? 1545 VAL A CG1   1 
ATOM   722   C CG2   . VAL A 1 1545 ? 243.401 214.461 211.106 1.00 34.57 ? 1545 VAL A CG2   1 
ATOM   723   N N     . TYR A 1 1546 ? 243.660 214.516 214.256 1.00 34.67 ? 1546 TYR A N     1 
ATOM   724   C CA    . TYR A 1 1546 ? 242.807 214.723 215.422 1.00 32.02 ? 1546 TYR A CA    1 
ATOM   725   C C     . TYR A 1 1546 ? 243.646 215.089 216.644 1.00 31.36 ? 1546 TYR A C     1 
ATOM   726   O O     . TYR A 1 1546 ? 243.363 216.072 217.342 1.00 31.51 ? 1546 TYR A O     1 
ATOM   727   C CB    . TYR A 1 1546 ? 241.971 213.470 215.691 1.00 28.76 ? 1546 TYR A CB    1 
ATOM   728   C CG    . TYR A 1 1546 ? 241.342 213.421 217.066 1.00 32.01 ? 1546 TYR A CG    1 
ATOM   729   C CD1   . TYR A 1 1546 ? 241.476 212.305 217.879 1.00 33.38 ? 1546 TYR A CD1   1 
ATOM   730   C CD2   . TYR A 1 1546 ? 240.572 214.480 217.532 1.00 31.07 ? 1546 TYR A CD2   1 
ATOM   731   C CE1   . TYR A 1 1546 ? 240.890 212.260 219.133 1.00 32.23 ? 1546 TYR A CE1   1 
ATOM   732   C CE2   . TYR A 1 1546 ? 239.981 214.441 218.777 1.00 29.71 ? 1546 TYR A CE2   1 
ATOM   733   C CZ    . TYR A 1 1546 ? 240.143 213.331 219.575 1.00 32.12 ? 1546 TYR A CZ    1 
ATOM   734   O OH    . TYR A 1 1546 ? 239.553 213.294 220.817 1.00 31.28 ? 1546 TYR A OH    1 
ATOM   735   N N     . LEU A 1 1547 ? 244.711 214.323 216.897 1.00 29.07 ? 1547 LEU A N     1 
ATOM   736   C CA    . LEU A 1 1547 ? 245.549 214.599 218.059 1.00 31.28 ? 1547 LEU A CA    1 
ATOM   737   C C     . LEU A 1 1547 ? 246.353 215.882 217.896 1.00 33.15 ? 1547 LEU A C     1 
ATOM   738   O O     . LEU A 1 1547 ? 246.653 216.546 218.892 1.00 32.04 ? 1547 LEU A O     1 
ATOM   739   C CB    . LEU A 1 1547 ? 246.478 213.421 218.335 1.00 33.03 ? 1547 LEU A CB    1 
ATOM   740   C CG    . LEU A 1 1547 ? 245.922 212.316 219.233 1.00 31.63 ? 1547 LEU A CG    1 
ATOM   741   C CD1   . LEU A 1 1547 ? 244.921 211.437 218.509 1.00 31.39 ? 1547 LEU A CD1   1 
ATOM   742   C CD2   . LEU A 1 1547 ? 247.064 211.489 219.770 1.00 31.85 ? 1547 LEU A CD2   1 
ATOM   743   N N     . GLU A 1 1548 ? 246.717 216.249 216.667 1.00 34.93 ? 1548 GLU A N     1 
ATOM   744   C CA    . GLU A 1 1548 ? 247.386 217.525 216.443 1.00 36.20 ? 1548 GLU A CA    1 
ATOM   745   C C     . GLU A 1 1548 ? 246.468 218.680 216.810 1.00 36.28 ? 1548 GLU A C     1 
ATOM   746   O O     . GLU A 1 1548 ? 246.879 219.629 217.490 1.00 34.43 ? 1548 GLU A O     1 
ATOM   747   C CB    . GLU A 1 1548 ? 247.833 217.624 214.984 1.00 30.76 ? 1548 GLU A CB    1 
ATOM   748   C CG    . GLU A 1 1548 ? 248.349 218.989 214.565 1.00 34.75 ? 1548 GLU A CG    1 
ATOM   749   C CD    . GLU A 1 1548 ? 249.761 219.254 215.050 1.00 38.29 ? 1548 GLU A CD    1 
ATOM   750   O OE1   . GLU A 1 1548 ? 250.466 218.284 215.395 1.00 40.22 ? 1548 GLU A OE1   1 
ATOM   751   O OE2   . GLU A 1 1548 ? 250.173 220.432 215.068 1.00 34.25 ? 1548 GLU A OE2   1 
ATOM   752   N N     . GLY A 1 1549 ? 245.206 218.603 216.381 1.00 33.05 ? 1549 GLY A N     1 
ATOM   753   C CA    . GLY A 1 1549 ? 244.238 219.602 216.797 1.00 33.69 ? 1549 GLY A CA    1 
ATOM   754   C C     . GLY A 1 1549 ? 244.076 219.654 218.303 1.00 34.56 ? 1549 GLY A C     1 
ATOM   755   O O     . GLY A 1 1549 ? 244.040 220.736 218.895 1.00 35.03 ? 1549 GLY A O     1 
ATOM   756   N N     . ILE A 1 1550 ? 244.004 218.486 218.946 1.00 32.28 ? 1550 ILE A N     1 
ATOM   757   C CA    . ILE A 1 1550 ? 243.849 218.453 220.400 1.00 31.97 ? 1550 ILE A CA    1 
ATOM   758   C C     . ILE A 1 1550 ? 245.045 219.098 221.092 1.00 34.79 ? 1550 ILE A C     1 
ATOM   759   O O     . ILE A 1 1550 ? 244.884 219.929 221.994 1.00 34.58 ? 1550 ILE A O     1 
ATOM   760   C CB    . ILE A 1 1550 ? 243.635 217.008 220.888 1.00 28.69 ? 1550 ILE A CB    1 
ATOM   761   C CG1   . ILE A 1 1550 ? 242.326 216.447 220.337 1.00 30.72 ? 1550 ILE A CG1   1 
ATOM   762   C CG2   . ILE A 1 1550 ? 243.651 216.950 222.405 1.00 26.60 ? 1550 ILE A CG2   1 
ATOM   763   C CD1   . ILE A 1 1550 ? 241.147 217.371 220.520 1.00 34.02 ? 1550 ILE A CD1   1 
ATOM   764   N N     . PHE A 1 1551 ? 246.259 218.735 220.681 1.00 34.67 ? 1551 PHE A N     1 
ATOM   765   C CA    . PHE A 1 1551 ? 247.461 219.174 221.375 1.00 32.41 ? 1551 PHE A CA    1 
ATOM   766   C C     . PHE A 1 1551 ? 247.847 220.612 221.061 1.00 32.25 ? 1551 PHE A C     1 
ATOM   767   O O     . PHE A 1 1551 ? 248.575 221.222 221.852 1.00 33.23 ? 1551 PHE A O     1 
ATOM   768   C CB    . PHE A 1 1551 ? 248.641 218.253 221.041 1.00 30.54 ? 1551 PHE A CB    1 
ATOM   769   C CG    . PHE A 1 1551 ? 248.617 216.932 221.766 1.00 32.93 ? 1551 PHE A CG    1 
ATOM   770   C CD1   . PHE A 1 1551 ? 247.436 216.229 221.934 1.00 32.67 ? 1551 PHE A CD1   1 
ATOM   771   C CD2   . PHE A 1 1551 ? 249.783 216.399 222.287 1.00 33.12 ? 1551 PHE A CD2   1 
ATOM   772   C CE1   . PHE A 1 1551 ? 247.422 215.018 222.596 1.00 31.85 ? 1551 PHE A CE1   1 
ATOM   773   C CE2   . PHE A 1 1551 ? 249.772 215.190 222.954 1.00 31.62 ? 1551 PHE A CE2   1 
ATOM   774   C CZ    . PHE A 1 1551 ? 248.591 214.499 223.108 1.00 31.77 ? 1551 PHE A CZ    1 
ATOM   775   N N     . THR A 1 1552 ? 247.393 221.171 219.941 1.00 29.70 ? 1552 THR A N     1 
ATOM   776   C CA    . THR A 1 1552 ? 247.739 222.543 219.587 1.00 32.59 ? 1552 THR A CA    1 
ATOM   777   C C     . THR A 1 1552 ? 246.642 223.551 219.888 1.00 34.50 ? 1552 THR A C     1 
ATOM   778   O O     . THR A 1 1552 ? 246.945 224.672 220.302 1.00 32.39 ? 1552 THR A O     1 
ATOM   779   C CB    . THR A 1 1552 ? 248.108 222.630 218.103 1.00 33.13 ? 1552 THR A CB    1 
ATOM   780   O OG1   . THR A 1 1552 ? 246.996 222.204 217.306 1.00 32.29 ? 1552 THR A OG1   1 
ATOM   781   C CG2   . THR A 1 1552 ? 249.314 221.755 217.807 1.00 33.55 ? 1552 THR A CG2   1 
ATOM   782   N N     . GLY A 1 1553 ? 245.374 223.193 219.689 1.00 34.10 ? 1553 GLY A N     1 
ATOM   783   C CA    . GLY A 1 1553 ? 244.286 224.114 219.953 1.00 32.08 ? 1553 GLY A CA    1 
ATOM   784   C C     . GLY A 1 1553 ? 244.159 224.491 221.415 1.00 34.29 ? 1553 GLY A C     1 
ATOM   785   O O     . GLY A 1 1553 ? 243.975 225.666 221.747 1.00 32.62 ? 1553 GLY A O     1 
ATOM   786   N N     . SER A 1 1554 ? 244.250 223.501 222.296 1.00 33.41 ? 1554 SER A N     1 
ATOM   787   C CA    . SER A 1 1554 ? 244.141 223.746 223.725 1.00 34.94 ? 1554 SER A CA    1 
ATOM   788   C C     . SER A 1 1554 ? 245.517 223.975 224.341 1.00 34.86 ? 1554 SER A C     1 
ATOM   789   O O     . SER A 1 1554 ? 246.511 223.362 223.943 1.00 37.85 ? 1554 SER A O     1 
ATOM   790   C CB    . SER A 1 1554 ? 243.447 222.573 224.415 1.00 35.41 ? 1554 SER A CB    1 
ATOM   791   O OG    . SER A 1 1554 ? 243.247 222.842 225.790 1.00 36.91 ? 1554 SER A OG    1 
ATOM   792   N N     . ALA A 1 1555 ? 245.564 224.869 225.325 1.00 31.44 ? 1555 ALA A N     1 
ATOM   793   C CA    . ALA A 1 1555 ? 246.807 225.215 225.991 1.00 32.59 ? 1555 ALA A CA    1 
ATOM   794   C C     . ALA A 1 1555 ? 247.035 224.303 227.196 1.00 36.13 ? 1555 ALA A C     1 
ATOM   795   O O     . ALA A 1 1555 ? 246.213 223.444 227.523 1.00 35.57 ? 1555 ALA A O     1 
ATOM   796   C CB    . ALA A 1 1555 ? 246.797 226.686 226.405 1.00 31.52 ? 1555 ALA A CB    1 
ATOM   797   N N     . ASP A 1 1556 ? 248.187 224.480 227.849 1.00 40.13 ? 1556 ASP A N     1 
ATOM   798   C CA    . ASP A 1 1556 ? 248.564 223.735 229.048 1.00 39.77 ? 1556 ASP A CA    1 
ATOM   799   C C     . ASP A 1 1556 ? 248.667 222.236 228.784 1.00 41.41 ? 1556 ASP A C     1 
ATOM   800   O O     . ASP A 1 1556 ? 248.793 221.442 229.722 1.00 37.53 ? 1556 ASP A O     1 
ATOM   801   C CB    . ASP A 1 1556 ? 247.578 224.007 230.186 1.00 36.44 ? 1556 ASP A CB    1 
ATOM   802   C CG    . ASP A 1 1556 ? 247.620 225.446 230.659 1.00 40.46 ? 1556 ASP A CG    1 
ATOM   803   O OD1   . ASP A 1 1556 ? 248.391 226.240 230.080 1.00 40.73 ? 1556 ASP A OD1   1 
ATOM   804   O OD2   . ASP A 1 1556 ? 246.885 225.784 231.609 1.00 40.36 ? 1556 ASP A OD2   1 
ATOM   805   N N     . ILE A 1 1557 ? 248.614 221.840 227.510 1.00 40.62 ? 1557 ILE A N     1 
ATOM   806   C CA    . ILE A 1 1557 ? 248.819 220.446 227.135 1.00 38.33 ? 1557 ILE A CA    1 
ATOM   807   C C     . ILE A 1 1557 ? 250.270 220.023 227.304 1.00 40.71 ? 1557 ILE A C     1 
ATOM   808   O O     . ILE A 1 1557 ? 250.555 218.829 227.434 1.00 39.71 ? 1557 ILE A O     1 
ATOM   809   C CB    . ILE A 1 1557 ? 248.320 220.239 225.688 1.00 41.18 ? 1557 ILE A CB    1 
ATOM   810   C CG1   . ILE A 1 1557 ? 246.822 220.539 225.599 1.00 38.09 ? 1557 ILE A CG1   1 
ATOM   811   C CG2   . ILE A 1 1557 ? 248.567 218.819 225.205 1.00 42.13 ? 1557 ILE A CG2   1 
ATOM   812   C CD1   . ILE A 1 1557 ? 246.000 219.916 226.710 1.00 39.10 ? 1557 ILE A CD1   1 
ATOM   813   N N     . LYS A 1 1558 ? 251.201 220.977 227.314 1.00 46.99 ? 1558 LYS A N     1 
ATOM   814   C CA    . LYS A 1 1558 ? 252.594 220.653 227.599 1.00 48.86 ? 1558 LYS A CA    1 
ATOM   815   C C     . LYS A 1 1558 ? 252.798 220.338 229.077 1.00 46.73 ? 1558 LYS A C     1 
ATOM   816   O O     . LYS A 1 1558 ? 253.475 219.364 229.424 1.00 45.12 ? 1558 LYS A O     1 
ATOM   817   C CB    . LYS A 1 1558 ? 253.500 221.804 227.157 1.00 47.78 ? 1558 LYS A CB    1 
ATOM   818   C CG    . LYS A 1 1558 ? 253.484 222.061 225.657 1.00 47.15 ? 1558 LYS A CG    1 
ATOM   819   C CD    . LYS A 1 1558 ? 252.472 223.134 225.282 1.00 47.98 ? 1558 LYS A CD    1 
ATOM   820   C CE    . LYS A 1 1558 ? 252.165 223.106 223.793 1.00 48.18 ? 1558 LYS A CE    1 
ATOM   821   N NZ    . LYS A 1 1558 ? 251.094 224.073 223.428 1.00 47.72 ? 1558 LYS A NZ    1 
ATOM   822   N N     . HIS A 1 1559 ? 252.217 221.153 229.963 1.00 45.52 ? 1559 HIS A N     1 
ATOM   823   C CA    . HIS A 1 1559 ? 252.370 220.918 231.396 1.00 47.30 ? 1559 HIS A CA    1 
ATOM   824   C C     . HIS A 1 1559 ? 251.562 219.709 231.851 1.00 46.53 ? 1559 HIS A C     1 
ATOM   825   O O     . HIS A 1 1559 ? 252.064 218.865 232.602 1.00 43.74 ? 1559 HIS A O     1 
ATOM   826   C CB    . HIS A 1 1559 ? 251.958 222.164 232.178 1.00 46.17 ? 1559 HIS A CB    1 
ATOM   827   C CG    . HIS A 1 1559 ? 252.412 223.447 231.555 1.00 47.88 ? 1559 HIS A CG    1 
ATOM   828   N ND1   . HIS A 1 1559 ? 251.676 224.110 230.596 1.00 48.86 ? 1559 HIS A ND1   1 
ATOM   829   C CD2   . HIS A 1 1559 ? 253.526 224.190 231.753 1.00 46.69 ? 1559 HIS A CD2   1 
ATOM   830   C CE1   . HIS A 1 1559 ? 252.317 225.205 230.231 1.00 47.94 ? 1559 HIS A CE1   1 
ATOM   831   N NE2   . HIS A 1 1559 ? 253.443 225.277 230.918 1.00 48.42 ? 1559 HIS A NE2   1 
ATOM   832   N N     . LEU A 1 1560 ? 250.312 219.608 231.408 1.00 42.04 ? 1560 LEU A N     1 
ATOM   833   C CA    . LEU A 1 1560 ? 249.464 218.466 231.720 1.00 39.51 ? 1560 LEU A CA    1 
ATOM   834   C C     . LEU A 1 1560 ? 249.746 217.353 230.720 1.00 39.69 ? 1560 LEU A C     1 
ATOM   835   O O     . LEU A 1 1560 ? 249.666 217.573 229.509 1.00 40.61 ? 1560 LEU A O     1 
ATOM   836   C CB    . LEU A 1 1560 ? 247.986 218.858 231.674 1.00 36.65 ? 1560 LEU A CB    1 
ATOM   837   C CG    . LEU A 1 1560 ? 247.334 219.419 232.940 1.00 37.18 ? 1560 LEU A CG    1 
ATOM   838   C CD1   . LEU A 1 1560 ? 247.992 220.717 233.385 1.00 38.90 ? 1560 LEU A CD1   1 
ATOM   839   C CD2   . LEU A 1 1560 ? 245.851 219.633 232.705 1.00 35.85 ? 1560 LEU A CD2   1 
ATOM   840   N N     . LEU A 1 1561 ? 250.065 216.162 231.230 1.00 36.64 ? 1561 LEU A N     1 
ATOM   841   C CA    . LEU A 1 1561 ? 250.489 215.023 230.420 1.00 37.36 ? 1561 LEU A CA    1 
ATOM   842   C C     . LEU A 1 1561 ? 251.788 215.361 229.697 1.00 38.37 ? 1561 LEU A C     1 
ATOM   843   O O     . LEU A 1 1561 ? 251.803 215.451 228.463 1.00 37.87 ? 1561 LEU A O     1 
ATOM   844   C CB    . LEU A 1 1561 ? 249.418 214.629 229.397 1.00 37.54 ? 1561 LEU A CB    1 
ATOM   845   C CG    . LEU A 1 1561 ? 248.182 213.854 229.849 1.00 35.66 ? 1561 LEU A CG    1 
ATOM   846   C CD1   . LEU A 1 1561 ? 247.276 214.764 230.647 1.00 35.63 ? 1561 LEU A CD1   1 
ATOM   847   C CD2   . LEU A 1 1561 ? 247.440 213.289 228.650 1.00 33.15 ? 1561 LEU A CD2   1 
ATOM   848   N N     . PRO A 1 1562 ? 252.896 215.557 230.420 1.00 40.49 ? 1562 PRO A N     1 
ATOM   849   C CA    . PRO A 1 1562 ? 254.139 215.937 229.730 1.00 40.64 ? 1562 PRO A CA    1 
ATOM   850   C C     . PRO A 1 1562 ? 254.733 214.808 228.910 1.00 41.25 ? 1562 PRO A C     1 
ATOM   851   O O     . PRO A 1 1562 ? 255.225 215.047 227.799 1.00 39.89 ? 1562 PRO A O     1 
ATOM   852   C CB    . PRO A 1 1562 ? 255.068 216.359 230.882 1.00 39.86 ? 1562 PRO A CB    1 
ATOM   853   C CG    . PRO A 1 1562 ? 254.216 216.345 232.133 1.00 38.32 ? 1562 PRO A CG    1 
ATOM   854   C CD    . PRO A 1 1562 ? 253.104 215.393 231.865 1.00 37.93 ? 1562 PRO A CD    1 
ATOM   855   N N     . VAL A 1 1563 ? 254.702 213.578 229.429 1.00 38.63 ? 1563 VAL A N     1 
ATOM   856   C CA    . VAL A 1 1563 ? 255.244 212.447 228.683 1.00 38.34 ? 1563 VAL A CA    1 
ATOM   857   C C     . VAL A 1 1563 ? 254.431 212.206 227.416 1.00 39.14 ? 1563 VAL A C     1 
ATOM   858   O O     . VAL A 1 1563 ? 254.990 211.943 226.345 1.00 40.01 ? 1563 VAL A O     1 
ATOM   859   C CB    . VAL A 1 1563 ? 255.316 211.193 229.578 1.00 37.65 ? 1563 VAL A CB    1 
ATOM   860   C CG1   . VAL A 1 1563 ? 253.938 210.794 230.089 1.00 37.86 ? 1563 VAL A CG1   1 
ATOM   861   C CG2   . VAL A 1 1563 ? 255.964 210.041 228.825 1.00 38.17 ? 1563 VAL A CG2   1 
ATOM   862   N N     . GLU A 1 1564 ? 253.103 212.313 227.510 1.00 39.19 ? 1564 GLU A N     1 
ATOM   863   C CA    . GLU A 1 1564 ? 252.270 212.166 226.323 1.00 39.00 ? 1564 GLU A CA    1 
ATOM   864   C C     . GLU A 1 1564 ? 252.581 213.250 225.301 1.00 37.58 ? 1564 GLU A C     1 
ATOM   865   O O     . GLU A 1 1564 ? 252.668 212.974 224.100 1.00 40.20 ? 1564 GLU A O     1 
ATOM   866   C CB    . GLU A 1 1564 ? 250.792 212.203 226.707 1.00 39.16 ? 1564 GLU A CB    1 
ATOM   867   C CG    . GLU A 1 1564 ? 250.453 211.399 227.949 1.00 40.35 ? 1564 GLU A CG    1 
ATOM   868   C CD    . GLU A 1 1564 ? 250.349 209.915 227.669 1.00 38.85 ? 1564 GLU A CD    1 
ATOM   869   O OE1   . GLU A 1 1564 ? 250.107 209.546 226.501 1.00 38.83 ? 1564 GLU A OE1   1 
ATOM   870   O OE2   . GLU A 1 1564 ? 250.507 209.117 228.617 1.00 36.42 ? 1564 GLU A OE2   1 
ATOM   871   N N     . THR A 1 1565 ? 252.766 214.489 225.763 1.00 35.02 ? 1565 THR A N     1 
ATOM   872   C CA    . THR A 1 1565 ? 253.058 215.583 224.844 1.00 40.34 ? 1565 THR A CA    1 
ATOM   873   C C     . THR A 1 1565 ? 254.396 215.382 224.142 1.00 40.13 ? 1565 THR A C     1 
ATOM   874   O O     . THR A 1 1565 ? 254.503 215.592 222.929 1.00 35.86 ? 1565 THR A O     1 
ATOM   875   C CB    . THR A 1 1565 ? 253.036 216.918 225.589 1.00 43.42 ? 1565 THR A CB    1 
ATOM   876   O OG1   . THR A 1 1565 ? 251.892 216.965 226.450 1.00 44.25 ? 1565 THR A OG1   1 
ATOM   877   C CG2   . THR A 1 1565 ? 252.961 218.074 224.602 1.00 39.79 ? 1565 THR A CG2   1 
ATOM   878   N N     . GLN A 1 1566 ? 255.430 214.966 224.882 1.00 39.62 ? 1566 GLN A N     1 
ATOM   879   C CA    . GLN A 1 1566 ? 256.736 214.779 224.252 1.00 41.31 ? 1566 GLN A CA    1 
ATOM   880   C C     . GLN A 1 1566 ? 256.734 213.579 223.307 1.00 42.58 ? 1566 GLN A C     1 
ATOM   881   O O     . GLN A 1 1566 ? 257.356 213.624 222.235 1.00 41.96 ? 1566 GLN A O     1 
ATOM   882   C CB    . GLN A 1 1566 ? 257.833 214.642 225.312 1.00 39.58 ? 1566 GLN A CB    1 
ATOM   883   C CG    . GLN A 1 1566 ? 257.757 213.396 226.173 1.00 41.57 ? 1566 GLN A CG    1 
ATOM   884   C CD    . GLN A 1 1566 ? 258.879 213.322 227.190 1.00 43.88 ? 1566 GLN A CD    1 
ATOM   885   O OE1   . GLN A 1 1566 ? 259.753 214.188 227.231 1.00 42.82 ? 1566 GLN A OE1   1 
ATOM   886   N NE2   . GLN A 1 1566 ? 258.861 212.283 228.016 1.00 42.40 ? 1566 GLN A NE2   1 
ATOM   887   N N     . ARG A 1 1567 ? 256.032 212.501 223.675 1.00 37.68 ? 1567 ARG A N     1 
ATOM   888   C CA    . ARG A 1 1567 ? 255.924 211.365 222.767 1.00 39.69 ? 1567 ARG A CA    1 
ATOM   889   C C     . ARG A 1 1567 ? 255.176 211.748 221.499 1.00 38.05 ? 1567 ARG A C     1 
ATOM   890   O O     . ARG A 1 1567 ? 255.565 211.345 220.398 1.00 36.23 ? 1567 ARG A O     1 
ATOM   891   C CB    . ARG A 1 1567 ? 255.243 210.184 223.459 1.00 38.76 ? 1567 ARG A CB    1 
ATOM   892   C CG    . ARG A 1 1567 ? 256.046 209.590 224.604 1.00 40.53 ? 1567 ARG A CG    1 
ATOM   893   C CD    . ARG A 1 1567 ? 255.414 208.307 225.115 1.00 41.32 ? 1567 ARG A CD    1 
ATOM   894   N NE    . ARG A 1 1567 ? 253.994 208.468 225.401 1.00 43.26 ? 1567 ARG A NE    1 
ATOM   895   C CZ    . ARG A 1 1567 ? 253.185 207.476 225.748 1.00 42.35 ? 1567 ARG A CZ    1 
ATOM   896   N NH1   . ARG A 1 1567 ? 253.628 206.237 225.879 1.00 39.44 ? 1567 ARG A NH1   1 
ATOM   897   N NH2   . ARG A 1 1567 ? 251.899 207.735 225.969 1.00 41.99 ? 1567 ARG A NH2   1 
ATOM   898   N N     . PHE A 1 1568 ? 254.107 212.538 221.628 1.00 36.76 ? 1568 PHE A N     1 
ATOM   899   C CA    . PHE A 1 1568 ? 253.395 212.988 220.439 1.00 35.89 ? 1568 PHE A CA    1 
ATOM   900   C C     . PHE A 1 1568 ? 254.244 213.937 219.608 1.00 39.33 ? 1568 PHE A C     1 
ATOM   901   O O     . PHE A 1 1568 ? 254.116 213.958 218.384 1.00 40.64 ? 1568 PHE A O     1 
ATOM   902   C CB    . PHE A 1 1568 ? 252.080 213.665 220.817 1.00 37.97 ? 1568 PHE A CB    1 
ATOM   903   C CG    . PHE A 1 1568 ? 251.307 214.175 219.635 1.00 36.85 ? 1568 PHE A CG    1 
ATOM   904   C CD1   . PHE A 1 1568 ? 250.592 213.302 218.835 1.00 34.62 ? 1568 PHE A CD1   1 
ATOM   905   C CD2   . PHE A 1 1568 ? 251.303 215.523 219.317 1.00 36.40 ? 1568 PHE A CD2   1 
ATOM   906   C CE1   . PHE A 1 1568 ? 249.882 213.763 217.744 1.00 36.08 ? 1568 PHE A CE1   1 
ATOM   907   C CE2   . PHE A 1 1568 ? 250.594 215.989 218.227 1.00 34.70 ? 1568 PHE A CE2   1 
ATOM   908   C CZ    . PHE A 1 1568 ? 249.882 215.107 217.440 1.00 34.84 ? 1568 PHE A CZ    1 
ATOM   909   N N     . GLN A 1 1569 ? 255.101 214.736 220.246 1.00 39.57 ? 1569 GLN A N     1 
ATOM   910   C CA    . GLN A 1 1569 ? 256.001 215.599 219.487 1.00 39.85 ? 1569 GLN A CA    1 
ATOM   911   C C     . GLN A 1 1569 ? 256.990 214.776 218.669 1.00 38.04 ? 1569 GLN A C     1 
ATOM   912   O O     . GLN A 1 1569 ? 257.222 215.063 217.488 1.00 33.43 ? 1569 GLN A O     1 
ATOM   913   C CB    . GLN A 1 1569 ? 256.733 216.552 220.434 1.00 39.70 ? 1569 GLN A CB    1 
ATOM   914   C CG    . GLN A 1 1569 ? 257.893 217.306 219.805 1.00 38.99 ? 1569 GLN A CG    1 
ATOM   915   C CD    . GLN A 1 1569 ? 259.235 216.676 220.117 1.00 41.81 ? 1569 GLN A CD    1 
ATOM   916   O OE1   . GLN A 1 1569 ? 259.352 215.861 221.032 1.00 42.56 ? 1569 GLN A OE1   1 
ATOM   917   N NE2   . GLN A 1 1569 ? 260.257 217.053 219.357 1.00 38.75 ? 1569 GLN A NE2   1 
ATOM   918   N N     . SER A 1 1570 ? 257.573 213.739 219.277 1.00 38.06 ? 1570 SER A N     1 
ATOM   919   C CA    . SER A 1 1570 ? 258.466 212.856 218.528 1.00 39.20 ? 1570 SER A CA    1 
ATOM   920   C C     . SER A 1 1570 ? 257.721 212.143 217.403 1.00 36.07 ? 1570 SER A C     1 
ATOM   921   O O     . SER A 1 1570 ? 258.233 212.017 216.280 1.00 37.39 ? 1570 SER A O     1 
ATOM   922   C CB    . SER A 1 1570 ? 259.112 211.841 219.471 1.00 38.61 ? 1570 SER A CB    1 
ATOM   923   O OG    . SER A 1 1570 ? 260.021 211.004 218.778 1.00 39.99 ? 1570 SER A OG    1 
ATOM   924   N N     . ILE A 1 1571 ? 256.505 211.675 217.689 1.00 35.09 ? 1571 ILE A N     1 
ATOM   925   C CA    . ILE A 1 1571 ? 255.682 211.014 216.682 1.00 36.29 ? 1571 ILE A CA    1 
ATOM   926   C C     . ILE A 1 1571 ? 255.375 211.955 215.526 1.00 35.07 ? 1571 ILE A C     1 
ATOM   927   O O     . ILE A 1 1571 ? 255.429 211.562 214.356 1.00 35.10 ? 1571 ILE A O     1 
ATOM   928   C CB    . ILE A 1 1571 ? 254.394 210.476 217.332 1.00 38.54 ? 1571 ILE A CB    1 
ATOM   929   C CG1   . ILE A 1 1571 ? 254.699 209.254 218.205 1.00 39.04 ? 1571 ILE A CG1   1 
ATOM   930   C CG2   . ILE A 1 1571 ? 253.338 210.206 216.293 1.00 33.13 ? 1571 ILE A CG2   1 
ATOM   931   C CD1   . ILE A 1 1571 ? 253.609 208.931 219.201 1.00 38.01 ? 1571 ILE A CD1   1 
ATOM   932   N N     . SER A 1 1572 ? 255.031 213.206 215.833 1.00 34.36 ? 1572 SER A N     1 
ATOM   933   C CA    . SER A 1 1572 ? 254.737 214.179 214.790 1.00 35.00 ? 1572 SER A CA    1 
ATOM   934   C C     . SER A 1 1572 ? 255.982 214.505 213.980 1.00 38.08 ? 1572 SER A C     1 
ATOM   935   O O     . SER A 1 1572 ? 255.895 214.730 212.770 1.00 36.36 ? 1572 SER A O     1 
ATOM   936   C CB    . SER A 1 1572 ? 254.144 215.445 215.407 1.00 36.09 ? 1572 SER A CB    1 
ATOM   937   O OG    . SER A 1 1572 ? 253.776 216.378 214.406 1.00 36.19 ? 1572 SER A OG    1 
ATOM   938   N N     . THR A 1 1573 ? 257.150 214.535 214.626 1.00 37.79 ? 1573 THR A N     1 
ATOM   939   C CA    . THR A 1 1573 ? 258.393 214.729 213.886 1.00 35.87 ? 1573 THR A CA    1 
ATOM   940   C C     . THR A 1 1573 ? 258.612 213.600 212.885 1.00 35.64 ? 1573 THR A C     1 
ATOM   941   O O     . THR A 1 1573 ? 258.927 213.842 211.713 1.00 36.21 ? 1573 THR A O     1 
ATOM   942   C CB    . THR A 1 1573 ? 259.572 214.827 214.855 1.00 36.46 ? 1573 THR A CB    1 
ATOM   943   O OG1   . THR A 1 1573 ? 259.386 215.950 215.725 1.00 37.03 ? 1573 THR A OG1   1 
ATOM   944   C CG2   . THR A 1 1573 ? 260.875 214.997 214.093 1.00 35.78 ? 1573 THR A CG2   1 
ATOM   945   N N     . GLU A 1 1574 ? 258.430 212.353 213.330 1.00 33.78 ? 1574 GLU A N     1 
ATOM   946   C CA    . GLU A 1 1574 ? 258.583 211.219 212.419 1.00 33.06 ? 1574 GLU A CA    1 
ATOM   947   C C     . GLU A 1 1574 ? 257.552 211.263 211.294 1.00 34.80 ? 1574 GLU A C     1 
ATOM   948   O O     . GLU A 1 1574 ? 257.879 211.005 210.128 1.00 37.15 ? 1574 GLU A O     1 
ATOM   949   C CB    . GLU A 1 1574 ? 258.479 209.901 213.189 1.00 34.63 ? 1574 GLU A CB    1 
ATOM   950   C CG    . GLU A 1 1574 ? 259.426 209.777 214.377 1.00 36.30 ? 1574 GLU A CG    1 
ATOM   951   C CD    . GLU A 1 1574 ? 260.829 210.277 214.077 1.00 38.58 ? 1574 GLU A CD    1 
ATOM   952   O OE1   . GLU A 1 1574 ? 261.392 209.894 213.030 1.00 37.45 ? 1574 GLU A OE1   1 
ATOM   953   O OE2   . GLU A 1 1574 ? 261.368 211.054 214.892 1.00 37.25 ? 1574 GLU A OE2   1 
ATOM   954   N N     . PHE A 1 1575 ? 256.301 211.589 211.627 1.00 35.16 ? 1575 PHE A N     1 
ATOM   955   C CA    . PHE A 1 1575 ? 255.244 211.644 210.623 1.00 36.02 ? 1575 PHE A CA    1 
ATOM   956   C C     . PHE A 1 1575 ? 255.505 212.741 209.600 1.00 34.24 ? 1575 PHE A C     1 
ATOM   957   O O     . PHE A 1 1575 ? 255.271 212.548 208.403 1.00 31.74 ? 1575 PHE A O     1 
ATOM   958   C CB    . PHE A 1 1575 ? 253.890 211.853 211.303 1.00 36.52 ? 1575 PHE A CB    1 
ATOM   959   C CG    . PHE A 1 1575 ? 252.729 211.904 210.350 1.00 36.65 ? 1575 PHE A CG    1 
ATOM   960   C CD1   . PHE A 1 1575 ? 252.174 210.740 209.850 1.00 33.28 ? 1575 PHE A CD1   1 
ATOM   961   C CD2   . PHE A 1 1575 ? 252.186 213.119 209.964 1.00 35.47 ? 1575 PHE A CD2   1 
ATOM   962   C CE1   . PHE A 1 1575 ? 251.103 210.784 208.976 1.00 33.57 ? 1575 PHE A CE1   1 
ATOM   963   C CE2   . PHE A 1 1575 ? 251.116 213.171 209.091 1.00 33.89 ? 1575 PHE A CE2   1 
ATOM   964   C CZ    . PHE A 1 1575 ? 250.574 212.001 208.597 1.00 33.89 ? 1575 PHE A CZ    1 
ATOM   965   N N     . LEU A 1 1576 ? 255.988 213.901 210.048 1.00 31.66 ? 1576 LEU A N     1 
ATOM   966   C CA    . LEU A 1 1576 ? 256.289 214.984 209.122 1.00 33.29 ? 1576 LEU A CA    1 
ATOM   967   C C     . LEU A 1 1576 ? 257.500 214.660 208.260 1.00 36.47 ? 1576 LEU A C     1 
ATOM   968   O O     . LEU A 1 1576 ? 257.540 215.044 207.086 1.00 35.38 ? 1576 LEU A O     1 
ATOM   969   C CB    . LEU A 1 1576 ? 256.506 216.287 209.889 1.00 31.47 ? 1576 LEU A CB    1 
ATOM   970   C CG    . LEU A 1 1576 ? 255.229 216.926 210.440 1.00 32.86 ? 1576 LEU A CG    1 
ATOM   971   C CD1   . LEU A 1 1576 ? 255.520 218.290 211.046 1.00 33.43 ? 1576 LEU A CD1   1 
ATOM   972   C CD2   . LEU A 1 1576 ? 254.165 217.021 209.360 1.00 31.24 ? 1576 LEU A CD2   1 
ATOM   973   N N     . ALA A 1 1577 ? 258.492 213.956 208.813 1.00 34.22 ? 1577 ALA A N     1 
ATOM   974   C CA    . ALA A 1 1577 ? 259.602 213.491 207.988 1.00 33.13 ? 1577 ALA A CA    1 
ATOM   975   C C     . ALA A 1 1577 ? 259.114 212.531 206.909 1.00 33.32 ? 1577 ALA A C     1 
ATOM   976   O O     . ALA A 1 1577 ? 259.527 212.626 205.746 1.00 35.63 ? 1577 ALA A O     1 
ATOM   977   C CB    . ALA A 1 1577 ? 260.664 212.827 208.862 1.00 32.09 ? 1577 ALA A CB    1 
ATOM   978   N N     . LEU A 1 1578 ? 258.222 211.608 207.276 1.00 32.87 ? 1578 LEU A N     1 
ATOM   979   C CA    . LEU A 1 1578 ? 257.656 210.690 206.293 1.00 35.49 ? 1578 LEU A CA    1 
ATOM   980   C C     . LEU A 1 1578 ? 256.848 211.437 205.238 1.00 35.58 ? 1578 LEU A C     1 
ATOM   981   O O     . LEU A 1 1578 ? 256.886 211.090 204.050 1.00 35.64 ? 1578 LEU A O     1 
ATOM   982   C CB    . LEU A 1 1578 ? 256.788 209.646 206.995 1.00 34.92 ? 1578 LEU A CB    1 
ATOM   983   C CG    . LEU A 1 1578 ? 256.155 208.565 206.118 1.00 34.72 ? 1578 LEU A CG    1 
ATOM   984   C CD1   . LEU A 1 1578 ? 257.226 207.737 205.429 1.00 35.07 ? 1578 LEU A CD1   1 
ATOM   985   C CD2   . LEU A 1 1578 ? 255.241 207.680 206.950 1.00 35.15 ? 1578 LEU A CD2   1 
ATOM   986   N N     . MET A 1 1579 ? 256.101 212.461 205.655 1.00 35.69 ? 1579 MET A N     1 
ATOM   987   C CA    . MET A 1 1579 ? 255.307 213.233 204.706 1.00 36.80 ? 1579 MET A CA    1 
ATOM   988   C C     . MET A 1 1579 ? 256.199 214.019 203.754 1.00 40.50 ? 1579 MET A C     1 
ATOM   989   O O     . MET A 1 1579 ? 255.893 214.139 202.564 1.00 41.68 ? 1579 MET A O     1 
ATOM   990   C CB    . MET A 1 1579 ? 254.354 214.166 205.452 1.00 38.14 ? 1579 MET A CB    1 
ATOM   991   C CG    . MET A 1 1579 ? 253.127 213.463 206.006 1.00 39.10 ? 1579 MET A CG    1 
ATOM   992   S SD    . MET A 1 1579 ? 252.565 212.113 204.951 1.00 45.01 ? 1579 MET A SD    1 
ATOM   993   C CE    . MET A 1 1579 ? 251.367 212.946 203.916 1.00 37.07 ? 1579 MET A CE    1 
ATOM   994   N N     . LYS A 1 1580 ? 257.309 214.561 204.256 1.00 41.95 ? 1580 LYS A N     1 
ATOM   995   C CA    . LYS A 1 1580 ? 258.267 215.223 203.376 1.00 41.80 ? 1580 LYS A CA    1 
ATOM   996   C C     . LYS A 1 1580 ? 258.883 214.234 202.394 1.00 40.98 ? 1580 LYS A C     1 
ATOM   997   O O     . LYS A 1 1580 ? 259.075 214.556 201.214 1.00 40.11 ? 1580 LYS A O     1 
ATOM   998   C CB    . LYS A 1 1580 ? 259.353 215.911 204.202 1.00 40.63 ? 1580 LYS A CB    1 
ATOM   999   C CG    . LYS A 1 1580 ? 260.097 217.009 203.457 1.00 41.60 ? 1580 LYS A CG    1 
ATOM   1000  C CD    . LYS A 1 1580 ? 259.167 218.151 203.085 1.00 41.72 ? 1580 LYS A CD    1 
ATOM   1001  C CE    . LYS A 1 1580 ? 258.578 218.813 204.319 1.00 41.14 ? 1580 LYS A CE    1 
ATOM   1002  N NZ    . LYS A 1 1580 ? 257.565 219.845 203.962 1.00 41.08 ? 1580 LYS A NZ    1 
ATOM   1003  N N     . LYS A 1 1581 ? 259.200 213.025 202.864 1.00 39.89 ? 1581 LYS A N     1 
ATOM   1004  C CA    . LYS A 1 1581 ? 259.761 212.012 201.974 1.00 40.23 ? 1581 LYS A CA    1 
ATOM   1005  C C     . LYS A 1 1581 ? 258.779 211.633 200.871 1.00 40.91 ? 1581 LYS A C     1 
ATOM   1006  O O     . LYS A 1 1581 ? 259.168 211.500 199.705 1.00 43.27 ? 1581 LYS A O     1 
ATOM   1007  C CB    . LYS A 1 1581 ? 260.174 210.776 202.773 1.00 39.61 ? 1581 LYS A CB    1 
ATOM   1008  C CG    . LYS A 1 1581 ? 261.400 210.983 203.646 1.00 41.24 ? 1581 LYS A CG    1 
ATOM   1009  C CD    . LYS A 1 1581 ? 262.661 211.074 202.801 1.00 41.67 ? 1581 LYS A CD    1 
ATOM   1010  C CE    . LYS A 1 1581 ? 263.907 211.151 203.669 1.00 40.54 ? 1581 LYS A CE    1 
ATOM   1011  N NZ    . LYS A 1 1581 ? 264.024 209.976 204.576 1.00 40.47 ? 1581 LYS A NZ    1 
ATOM   1012  N N     . VAL A 1 1582 ? 257.502 211.452 201.217 1.00 37.36 ? 1582 VAL A N     1 
ATOM   1013  C CA    . VAL A 1 1582 ? 256.514 211.107 200.197 1.00 40.04 ? 1582 VAL A CA    1 
ATOM   1014  C C     . VAL A 1 1582 ? 256.184 212.300 199.304 1.00 37.32 ? 1582 VAL A C     1 
ATOM   1015  O O     . VAL A 1 1582 ? 255.786 212.108 198.148 1.00 37.55 ? 1582 VAL A O     1 
ATOM   1016  C CB    . VAL A 1 1582 ? 255.236 210.526 200.834 1.00 40.16 ? 1582 VAL A CB    1 
ATOM   1017  C CG1   . VAL A 1 1582 ? 254.493 211.574 201.633 1.00 38.80 ? 1582 VAL A CG1   1 
ATOM   1018  C CG2   . VAL A 1 1582 ? 254.322 209.918 199.776 1.00 36.64 ? 1582 VAL A CG2   1 
ATOM   1019  N N     . SER A 1 1583 ? 256.355 213.529 199.798 1.00 35.08 ? 1583 SER A N     1 
ATOM   1020  C CA    . SER A 1 1583 ? 256.103 214.706 198.976 1.00 39.20 ? 1583 SER A CA    1 
ATOM   1021  C C     . SER A 1 1583 ? 257.224 214.966 197.980 1.00 43.43 ? 1583 SER A C     1 
ATOM   1022  O O     . SER A 1 1583 ? 256.959 215.443 196.871 1.00 41.44 ? 1583 SER A O     1 
ATOM   1023  C CB    . SER A 1 1583 ? 255.900 215.934 199.865 1.00 39.95 ? 1583 SER A CB    1 
ATOM   1024  O OG    . SER A 1 1583 ? 257.139 216.534 200.197 1.00 40.71 ? 1583 SER A OG    1 
ATOM   1025  N N     . LYS A 1 1584 ? 258.474 214.674 198.354 1.00 44.59 ? 1584 LYS A N     1 
ATOM   1026  C CA    . LYS A 1 1584 ? 259.580 214.877 197.423 1.00 43.42 ? 1584 LYS A CA    1 
ATOM   1027  C C     . LYS A 1 1584 ? 259.446 213.988 196.194 1.00 43.68 ? 1584 LYS A C     1 
ATOM   1028  O O     . LYS A 1 1584 ? 259.899 214.362 195.106 1.00 44.82 ? 1584 LYS A O     1 
ATOM   1029  C CB    . LYS A 1 1584 ? 260.916 214.621 198.122 1.00 43.17 ? 1584 LYS A CB    1 
ATOM   1030  C CG    . LYS A 1 1584 ? 261.359 215.747 199.044 1.00 43.96 ? 1584 LYS A CG    1 
ATOM   1031  C CD    . LYS A 1 1584 ? 262.678 215.417 199.725 1.00 42.85 ? 1584 LYS A CD    1 
ATOM   1032  C CE    . LYS A 1 1584 ? 262.562 214.177 200.593 1.00 43.24 ? 1584 LYS A CE    1 
ATOM   1033  N NZ    . LYS A 1 1584 ? 263.840 213.873 201.292 1.00 45.96 ? 1584 LYS A NZ    1 
ATOM   1034  N N     . SER A 1 1585 ? 258.831 212.817 196.344 1.00 40.04 ? 1585 SER A N     1 
ATOM   1035  C CA    . SER A 1 1585 ? 258.558 211.904 195.235 1.00 42.88 ? 1585 SER A CA    1 
ATOM   1036  C C     . SER A 1 1585 ? 257.085 211.525 195.292 1.00 41.84 ? 1585 SER A C     1 
ATOM   1037  O O     . SER A 1 1585 ? 256.724 210.457 195.806 1.00 40.90 ? 1585 SER A O     1 
ATOM   1038  C CB    . SER A 1 1585 ? 259.455 210.666 195.297 1.00 44.13 ? 1585 SER A CB    1 
ATOM   1039  O OG    . SER A 1 1585 ? 260.825 211.028 195.319 1.00 45.14 ? 1585 SER A OG    1 
ATOM   1040  N N     . PRO A 1 1586 ? 256.201 212.378 194.770 1.00 42.61 ? 1586 PRO A N     1 
ATOM   1041  C CA    . PRO A 1 1586 ? 254.761 212.108 194.882 1.00 42.13 ? 1586 PRO A CA    1 
ATOM   1042  C C     . PRO A 1 1586 ? 254.274 211.034 193.922 1.00 40.91 ? 1586 PRO A C     1 
ATOM   1043  O O     . PRO A 1 1586 ? 253.297 211.237 193.195 1.00 40.82 ? 1586 PRO A O     1 
ATOM   1044  C CB    . PRO A 1 1586 ? 254.128 213.468 194.564 1.00 40.39 ? 1586 PRO A CB    1 
ATOM   1045  C CG    . PRO A 1 1586 ? 255.111 214.133 193.665 1.00 41.61 ? 1586 PRO A CG    1 
ATOM   1046  C CD    . PRO A 1 1586 ? 256.481 213.635 194.054 1.00 41.58 ? 1586 PRO A CD    1 
ATOM   1047  N N     . LEU A 1 1587 ? 254.944 209.886 193.917 1.00 40.83 ? 1587 LEU A N     1 
ATOM   1048  C CA    . LEU A 1 1587 ? 254.559 208.742 193.102 1.00 42.95 ? 1587 LEU A CA    1 
ATOM   1049  C C     . LEU A 1 1587 ? 254.395 207.528 194.004 1.00 43.44 ? 1587 LEU A C     1 
ATOM   1050  O O     . LEU A 1 1587 ? 255.267 207.240 194.829 1.00 42.85 ? 1587 LEU A O     1 
ATOM   1051  C CB    . LEU A 1 1587 ? 255.598 208.467 192.015 1.00 41.81 ? 1587 LEU A CB    1 
ATOM   1052  C CG    . LEU A 1 1587 ? 255.128 207.693 190.784 1.00 42.97 ? 1587 LEU A CG    1 
ATOM   1053  C CD1   . LEU A 1 1587 ? 253.796 208.225 190.288 1.00 43.59 ? 1587 LEU A CD1   1 
ATOM   1054  C CD2   . LEU A 1 1587 ? 256.177 207.747 189.689 1.00 42.45 ? 1587 LEU A CD2   1 
ATOM   1055  N N     . VAL A 1 1588 ? 253.276 206.820 193.845 1.00 44.76 ? 1588 VAL A N     1 
ATOM   1056  C CA    . VAL A 1 1588 ? 252.965 205.712 194.743 1.00 44.77 ? 1588 VAL A CA    1 
ATOM   1057  C C     . VAL A 1 1588 ? 253.913 204.533 194.520 1.00 45.63 ? 1588 VAL A C     1 
ATOM   1058  O O     . VAL A 1 1588 ? 254.332 203.873 195.480 1.00 43.74 ? 1588 VAL A O     1 
ATOM   1059  C CB    . VAL A 1 1588 ? 251.476 205.332 194.613 1.00 44.51 ? 1588 VAL A CB    1 
ATOM   1060  C CG1   . VAL A 1 1588 ? 251.142 204.877 193.211 1.00 44.09 ? 1588 VAL A CG1   1 
ATOM   1061  C CG2   . VAL A 1 1588 ? 251.117 204.257 195.624 1.00 42.78 ? 1588 VAL A CG2   1 
ATOM   1062  N N     . MET A 1 1589 ? 254.285 204.256 193.266 1.00 48.19 ? 1589 MET A N     1 
ATOM   1063  C CA    . MET A 1 1589 ? 255.391 203.330 193.021 1.00 48.72 ? 1589 MET A CA    1 
ATOM   1064  C C     . MET A 1 1589 ? 256.695 203.835 193.626 1.00 51.51 ? 1589 MET A C     1 
ATOM   1065  O O     . MET A 1 1589 ? 257.444 203.056 194.227 1.00 51.63 ? 1589 MET A O     1 
ATOM   1066  C CB    . MET A 1 1589 ? 255.562 203.072 191.521 1.00 46.16 ? 1589 MET A CB    1 
ATOM   1067  C CG    . MET A 1 1589 ? 254.324 202.679 190.696 1.00 47.87 ? 1589 MET A CG    1 
ATOM   1068  S SD    . MET A 1 1589 ? 253.372 201.217 191.228 1.00 52.14 ? 1589 MET A SD    1 
ATOM   1069  C CE    . MET A 1 1589 ? 252.384 201.748 192.619 1.00 47.24 ? 1589 MET A CE    1 
ATOM   1070  N N     . ASP A 1 1590 ? 256.987 205.129 193.486 1.00 45.17 ? 1590 ASP A N     1 
ATOM   1071  C CA    . ASP A 1 1590 ? 258.244 205.661 194.001 1.00 44.05 ? 1590 ASP A CA    1 
ATOM   1072  C C     . ASP A 1 1590 ? 258.322 205.640 195.522 1.00 44.79 ? 1590 ASP A C     1 
ATOM   1073  O O     . ASP A 1 1590 ? 259.428 205.742 196.065 1.00 46.69 ? 1590 ASP A O     1 
ATOM   1074  C CB    . ASP A 1 1590 ? 258.464 207.088 193.495 1.00 45.25 ? 1590 ASP A CB    1 
ATOM   1075  C CG    . ASP A 1 1590 ? 258.808 207.138 192.018 1.00 45.90 ? 1590 ASP A CG    1 
ATOM   1076  O OD1   . ASP A 1 1590 ? 258.719 206.088 191.348 1.00 43.41 ? 1590 ASP A OD1   1 
ATOM   1077  O OD2   . ASP A 1 1590 ? 259.164 208.229 191.526 1.00 46.51 ? 1590 ASP A OD2   1 
ATOM   1078  N N     . VAL A 1 1591 ? 257.194 205.507 196.220 1.00 39.96 ? 1591 VAL A N     1 
ATOM   1079  C CA    . VAL A 1 1591 ? 257.202 205.446 197.671 1.00 42.27 ? 1591 VAL A CA    1 
ATOM   1080  C C     . VAL A 1 1591 ? 256.979 204.031 198.198 1.00 43.56 ? 1591 VAL A C     1 
ATOM   1081  O O     . VAL A 1 1591 ? 257.315 203.758 199.356 1.00 43.63 ? 1591 VAL A O     1 
ATOM   1082  C CB    . VAL A 1 1591 ? 256.169 206.421 198.275 1.00 42.50 ? 1591 VAL A CB    1 
ATOM   1083  C CG1   . VAL A 1 1591 ? 256.464 207.843 197.821 1.00 42.04 ? 1591 VAL A CG1   1 
ATOM   1084  C CG2   . VAL A 1 1591 ? 254.756 206.005 197.909 1.00 40.05 ? 1591 VAL A CG2   1 
ATOM   1085  N N     . LEU A 1 1592 ? 256.419 203.125 197.392 1.00 42.77 ? 1592 LEU A N     1 
ATOM   1086  C CA    . LEU A 1 1592 ? 256.387 201.722 197.795 1.00 45.13 ? 1592 LEU A CA    1 
ATOM   1087  C C     . LEU A 1 1592 ? 257.767 201.084 197.712 1.00 45.51 ? 1592 LEU A C     1 
ATOM   1088  O O     . LEU A 1 1592 ? 258.059 200.142 198.457 1.00 42.23 ? 1592 LEU A O     1 
ATOM   1089  C CB    . LEU A 1 1592 ? 255.389 200.942 196.939 1.00 44.54 ? 1592 LEU A CB    1 
ATOM   1090  C CG    . LEU A 1 1592 ? 253.995 200.739 197.534 1.00 43.58 ? 1592 LEU A CG    1 
ATOM   1091  C CD1   . LEU A 1 1592 ? 254.058 199.801 198.728 1.00 41.40 ? 1592 LEU A CD1   1 
ATOM   1092  C CD2   . LEU A 1 1592 ? 253.386 202.069 197.938 1.00 43.27 ? 1592 LEU A CD2   1 
ATOM   1093  N N     . ASN A 1 1593 ? 258.623 201.576 196.813 1.00 46.81 ? 1593 ASN A N     1 
ATOM   1094  C CA    . ASN A 1 1593 ? 259.983 201.063 196.711 1.00 46.84 ? 1593 ASN A CA    1 
ATOM   1095  C C     . ASN A 1 1593 ? 260.826 201.416 197.930 1.00 46.79 ? 1593 ASN A C     1 
ATOM   1096  O O     . ASN A 1 1593 ? 261.843 200.758 198.177 1.00 44.78 ? 1593 ASN A O     1 
ATOM   1097  C CB    . ASN A 1 1593 ? 260.649 201.597 195.441 1.00 45.93 ? 1593 ASN A CB    1 
ATOM   1098  C CG    . ASN A 1 1593 ? 261.940 200.873 195.109 1.00 46.88 ? 1593 ASN A CG    1 
ATOM   1099  O OD1   . ASN A 1 1593 ? 262.171 199.752 195.560 1.00 47.26 ? 1593 ASN A OD1   1 
ATOM   1100  N ND2   . ASN A 1 1593 ? 262.791 201.517 194.319 1.00 45.03 ? 1593 ASN A ND2   1 
ATOM   1101  N N     . ILE A 1 1594 ? 260.430 202.433 198.695 1.00 43.57 ? 1594 ILE A N     1 
ATOM   1102  C CA    . ILE A 1 1594 ? 261.192 202.832 199.871 1.00 42.49 ? 1594 ILE A CA    1 
ATOM   1103  C C     . ILE A 1 1594 ? 261.036 201.776 200.956 1.00 43.20 ? 1594 ILE A C     1 
ATOM   1104  O O     . ILE A 1 1594 ? 259.917 201.373 201.298 1.00 42.92 ? 1594 ILE A O     1 
ATOM   1105  C CB    . ILE A 1 1594 ? 260.739 204.213 200.366 1.00 42.13 ? 1594 ILE A CB    1 
ATOM   1106  C CG1   . ILE A 1 1594 ? 260.783 205.229 199.223 1.00 42.98 ? 1594 ILE A CG1   1 
ATOM   1107  C CG2   . ILE A 1 1594 ? 261.610 204.675 201.524 1.00 40.36 ? 1594 ILE A CG2   1 
ATOM   1108  C CD1   . ILE A 1 1594 ? 260.429 206.639 199.645 1.00 43.27 ? 1594 ILE A CD1   1 
ATOM   1109  N N     . GLN A 1 1595 ? 262.160 201.322 201.502 1.00 43.82 ? 1595 GLN A N     1 
ATOM   1110  C CA    . GLN A 1 1595 ? 262.146 200.274 202.509 1.00 42.30 ? 1595 GLN A CA    1 
ATOM   1111  C C     . GLN A 1 1595 ? 261.780 200.836 203.879 1.00 40.60 ? 1595 GLN A C     1 
ATOM   1112  O O     . GLN A 1 1595 ? 262.056 201.997 204.196 1.00 40.10 ? 1595 GLN A O     1 
ATOM   1113  C CB    . GLN A 1 1595 ? 263.505 199.573 202.577 1.00 42.56 ? 1595 GLN A CB    1 
ATOM   1114  C CG    . GLN A 1 1595 ? 264.622 200.401 203.200 1.00 42.41 ? 1595 GLN A CG    1 
ATOM   1115  C CD    . GLN A 1 1595 ? 265.156 201.470 202.266 1.00 43.82 ? 1595 GLN A CD    1 
ATOM   1116  O OE1   . GLN A 1 1595 ? 265.001 201.381 201.048 1.00 43.80 ? 1595 GLN A OE1   1 
ATOM   1117  N NE2   . GLN A 1 1595 ? 265.789 202.490 202.835 1.00 41.52 ? 1595 GLN A NE2   1 
ATOM   1118  N N     . GLY A 1 1596 ? 261.142 199.994 204.690 1.00 36.55 ? 1596 GLY A N     1 
ATOM   1119  C CA    . GLY A 1 1596 ? 260.789 200.344 206.049 1.00 37.81 ? 1596 GLY A CA    1 
ATOM   1120  C C     . GLY A 1 1596 ? 259.518 201.149 206.209 1.00 39.84 ? 1596 GLY A C     1 
ATOM   1121  O O     . GLY A 1 1596 ? 259.176 201.509 207.342 1.00 39.05 ? 1596 GLY A O     1 
ATOM   1122  N N     . VAL A 1 1597 ? 258.807 201.444 205.119 1.00 37.75 ? 1597 VAL A N     1 
ATOM   1123  C CA    . VAL A 1 1597 ? 257.617 202.284 205.215 1.00 36.07 ? 1597 VAL A CA    1 
ATOM   1124  C C     . VAL A 1 1597 ? 256.491 201.551 205.937 1.00 35.61 ? 1597 VAL A C     1 
ATOM   1125  O O     . VAL A 1 1597 ? 255.802 202.129 206.784 1.00 34.26 ? 1597 VAL A O     1 
ATOM   1126  C CB    . VAL A 1 1597 ? 257.186 202.755 203.814 1.00 36.22 ? 1597 VAL A CB    1 
ATOM   1127  C CG1   . VAL A 1 1597 ? 255.885 203.538 203.891 1.00 35.97 ? 1597 VAL A CG1   1 
ATOM   1128  C CG2   . VAL A 1 1597 ? 258.284 203.597 203.181 1.00 36.56 ? 1597 VAL A CG2   1 
ATOM   1129  N N     . GLN A 1 1598 ? 256.287 200.270 205.618 1.00 36.63 ? 1598 GLN A N     1 
ATOM   1130  C CA    . GLN A 1 1598 ? 255.189 199.514 206.217 1.00 36.66 ? 1598 GLN A CA    1 
ATOM   1131  C C     . GLN A 1 1598 ? 255.385 199.338 207.719 1.00 36.69 ? 1598 GLN A C     1 
ATOM   1132  O O     . GLN A 1 1598 ? 254.457 199.549 208.511 1.00 36.36 ? 1598 GLN A O     1 
ATOM   1133  C CB    . GLN A 1 1598 ? 255.064 198.153 205.532 1.00 35.92 ? 1598 GLN A CB    1 
ATOM   1134  C CG    . GLN A 1 1598 ? 253.870 197.328 205.983 1.00 34.82 ? 1598 GLN A CG    1 
ATOM   1135  C CD    . GLN A 1 1598 ? 252.548 198.009 205.699 1.00 35.97 ? 1598 GLN A CD    1 
ATOM   1136  O OE1   . GLN A 1 1598 ? 252.210 198.277 204.547 1.00 34.50 ? 1598 GLN A OE1   1 
ATOM   1137  N NE2   . GLN A 1 1598 ? 251.788 198.290 206.751 1.00 33.86 ? 1598 GLN A NE2   1 
ATOM   1138  N N     . ARG A 1 1599 ? 256.588 198.924 208.127 1.00 38.59 ? 1599 ARG A N     1 
ATOM   1139  C CA    . ARG A 1 1599 ? 256.857 198.712 209.545 1.00 38.34 ? 1599 ARG A CA    1 
ATOM   1140  C C     . ARG A 1 1599 ? 256.795 200.022 210.321 1.00 36.61 ? 1599 ARG A C     1 
ATOM   1141  O O     . ARG A 1 1599 ? 256.243 200.075 211.427 1.00 35.29 ? 1599 ARG A O     1 
ATOM   1142  C CB    . ARG A 1 1599 ? 258.217 198.038 209.721 1.00 37.50 ? 1599 ARG A CB    1 
ATOM   1143  C CG    . ARG A 1 1599 ? 258.540 197.662 211.154 1.00 36.70 ? 1599 ARG A CG    1 
ATOM   1144  C CD    . ARG A 1 1599 ? 259.993 197.958 211.480 1.00 37.81 ? 1599 ARG A CD    1 
ATOM   1145  N NE    . ARG A 1 1599 ? 260.428 199.234 210.924 1.00 41.88 ? 1599 ARG A NE    1 
ATOM   1146  C CZ    . ARG A 1 1599 ? 260.124 200.418 211.438 1.00 40.81 ? 1599 ARG A CZ    1 
ATOM   1147  N NH1   . ARG A 1 1599 ? 259.363 200.530 212.515 1.00 35.42 ? 1599 ARG A NH1   1 
ATOM   1148  N NH2   . ARG A 1 1599 ? 260.592 201.518 210.855 1.00 37.80 ? 1599 ARG A NH2   1 
ATOM   1149  N N     . SER A 1 1600 ? 257.353 201.094 209.754 1.00 35.10 ? 1600 SER A N     1 
ATOM   1150  C CA    . SER A 1 1600 ? 257.251 202.396 210.402 1.00 37.42 ? 1600 SER A CA    1 
ATOM   1151  C C     . SER A 1 1600 ? 255.801 202.837 210.527 1.00 38.26 ? 1600 SER A C     1 
ATOM   1152  O O     . SER A 1 1600 ? 255.415 203.412 211.548 1.00 36.55 ? 1600 SER A O     1 
ATOM   1153  C CB    . SER A 1 1600 ? 258.056 203.440 209.628 1.00 33.90 ? 1600 SER A CB    1 
ATOM   1154  O OG    . SER A 1 1600 ? 257.613 203.530 208.286 1.00 36.60 ? 1600 SER A OG    1 
ATOM   1155  N N     . LEU A 1 1601 ? 254.982 202.563 209.510 1.00 37.32 ? 1601 LEU A N     1 
ATOM   1156  C CA    . LEU A 1 1601 ? 253.582 202.968 209.557 1.00 35.72 ? 1601 LEU A CA    1 
ATOM   1157  C C     . LEU A 1 1601 ? 252.806 202.183 210.606 1.00 36.77 ? 1601 LEU A C     1 
ATOM   1158  O O     . LEU A 1 1601 ? 251.963 202.752 211.308 1.00 38.33 ? 1601 LEU A O     1 
ATOM   1159  C CB    . LEU A 1 1601 ? 252.940 202.807 208.182 1.00 34.96 ? 1601 LEU A CB    1 
ATOM   1160  C CG    . LEU A 1 1601 ? 251.684 203.652 207.975 1.00 36.19 ? 1601 LEU A CG    1 
ATOM   1161  C CD1   . LEU A 1 1601 ? 252.052 205.115 207.816 1.00 34.64 ? 1601 LEU A CD1   1 
ATOM   1162  C CD2   . LEU A 1 1601 ? 250.907 203.162 206.772 1.00 37.01 ? 1601 LEU A CD2   1 
ATOM   1163  N N     . GLU A 1 1602 ? 253.052 200.875 210.720 1.00 35.59 ? 1602 GLU A N     1 
ATOM   1164  C CA    . GLU A 1 1602 ? 252.356 200.111 211.755 1.00 36.67 ? 1602 GLU A CA    1 
ATOM   1165  C C     . GLU A 1 1602 ? 252.811 200.539 213.147 1.00 36.57 ? 1602 GLU A C     1 
ATOM   1166  O O     . GLU A 1 1602 ? 251.991 200.640 214.070 1.00 37.25 ? 1602 GLU A O     1 
ATOM   1167  C CB    . GLU A 1 1602 ? 252.541 198.604 211.553 1.00 36.64 ? 1602 GLU A CB    1 
ATOM   1168  C CG    . GLU A 1 1602 ? 253.966 198.091 211.619 1.00 37.10 ? 1602 GLU A CG    1 
ATOM   1169  C CD    . GLU A 1 1602 ? 254.340 197.564 212.993 1.00 38.54 ? 1602 GLU A CD    1 
ATOM   1170  O OE1   . GLU A 1 1602 ? 253.440 197.429 213.848 1.00 34.67 ? 1602 GLU A OE1   1 
ATOM   1171  O OE2   . GLU A 1 1602 ? 255.536 197.283 213.217 1.00 39.15 ? 1602 GLU A OE2   1 
ATOM   1172  N N     . ARG A 1 1603 ? 254.109 200.817 213.315 1.00 34.77 ? 1603 ARG A N     1 
ATOM   1173  C CA    . ARG A 1 1603 ? 254.587 201.369 214.580 1.00 35.47 ? 1603 ARG A CA    1 
ATOM   1174  C C     . ARG A 1 1603 ? 253.889 202.684 214.896 1.00 36.69 ? 1603 ARG A C     1 
ATOM   1175  O O     . ARG A 1 1603 ? 253.462 202.923 216.032 1.00 36.27 ? 1603 ARG A O     1 
ATOM   1176  C CB    . ARG A 1 1603 ? 256.100 201.583 214.524 1.00 37.49 ? 1603 ARG A CB    1 
ATOM   1177  C CG    . ARG A 1 1603 ? 256.657 202.285 215.755 1.00 36.89 ? 1603 ARG A CG    1 
ATOM   1178  C CD    . ARG A 1 1603 ? 258.169 202.421 215.700 1.00 38.24 ? 1603 ARG A CD    1 
ATOM   1179  N NE    . ARG A 1 1603 ? 258.582 203.347 214.652 1.00 38.20 ? 1603 ARG A NE    1 
ATOM   1180  C CZ    . ARG A 1 1603 ? 259.754 203.307 214.033 1.00 37.62 ? 1603 ARG A CZ    1 
ATOM   1181  N NH1   . ARG A 1 1603 ? 260.675 202.413 214.353 1.00 36.53 ? 1603 ARG A NH1   1 
ATOM   1182  N NH2   . ARG A 1 1603 ? 260.011 204.191 213.072 1.00 39.88 ? 1603 ARG A NH2   1 
ATOM   1183  N N     . LEU A 1 1604 ? 253.773 203.553 213.892 1.00 34.01 ? 1604 LEU A N     1 
ATOM   1184  C CA    . LEU A 1 1604 ? 253.160 204.860 214.081 1.00 34.18 ? 1604 LEU A CA    1 
ATOM   1185  C C     . LEU A 1 1604 ? 251.691 204.728 214.460 1.00 33.81 ? 1604 LEU A C     1 
ATOM   1186  O O     . LEU A 1 1604 ? 251.210 205.414 215.370 1.00 28.76 ? 1604 LEU A O     1 
ATOM   1187  C CB    . LEU A 1 1604 ? 253.333 205.675 212.799 1.00 30.66 ? 1604 LEU A CB    1 
ATOM   1188  C CG    . LEU A 1 1604 ? 252.855 207.116 212.704 1.00 33.74 ? 1604 LEU A CG    1 
ATOM   1189  C CD1   . LEU A 1 1604 ? 253.617 207.940 213.700 1.00 35.63 ? 1604 LEU A CD1   1 
ATOM   1190  C CD2   . LEU A 1 1604 ? 253.110 207.631 211.305 1.00 32.78 ? 1604 LEU A CD2   1 
ATOM   1191  N N     . ALA A 1 1605 ? 250.967 203.834 213.782 1.00 33.62 ? 1605 ALA A N     1 
ATOM   1192  C CA    . ALA A 1 1605 ? 249.560 203.610 214.102 1.00 33.90 ? 1605 ALA A CA    1 
ATOM   1193  C C     . ALA A 1 1605 ? 249.393 203.061 215.511 1.00 35.61 ? 1605 ALA A C     1 
ATOM   1194  O O     . ALA A 1 1605 ? 248.477 203.462 216.236 1.00 36.01 ? 1605 ALA A O     1 
ATOM   1195  C CB    . ALA A 1 1605 ? 248.932 202.657 213.085 1.00 31.62 ? 1605 ALA A CB    1 
ATOM   1196  N N     . ASP A 1 1606 ? 250.259 202.130 215.915 1.00 36.05 ? 1606 ASP A N     1 
ATOM   1197  C CA    . ASP A 1 1606 ? 250.126 201.544 217.244 1.00 34.03 ? 1606 ASP A CA    1 
ATOM   1198  C C     . ASP A 1 1606 ? 250.450 202.572 218.325 1.00 33.34 ? 1606 ASP A C     1 
ATOM   1199  O O     . ASP A 1 1606 ? 249.779 202.627 219.366 1.00 31.92 ? 1606 ASP A O     1 
ATOM   1200  C CB    . ASP A 1 1606 ? 251.025 200.312 217.349 1.00 33.59 ? 1606 ASP A CB    1 
ATOM   1201  C CG    . ASP A 1 1606 ? 250.712 199.460 218.560 1.00 36.29 ? 1606 ASP A CG    1 
ATOM   1202  O OD1   . ASP A 1 1606 ? 249.982 198.459 218.403 1.00 34.95 ? 1606 ASP A OD1   1 
ATOM   1203  O OD2   . ASP A 1 1606 ? 251.206 199.769 219.659 1.00 35.88 ? 1606 ASP A OD2   1 
ATOM   1204  N N     . LEU A 1 1607 ? 251.460 203.415 218.082 1.00 33.49 ? 1607 LEU A N     1 
ATOM   1205  C CA    . LEU A 1 1607 ? 251.758 204.508 219.003 1.00 37.10 ? 1607 LEU A CA    1 
ATOM   1206  C C     . LEU A 1 1607 ? 250.587 205.475 219.104 1.00 35.53 ? 1607 LEU A C     1 
ATOM   1207  O O     . LEU A 1 1607 ? 250.245 205.937 220.200 1.00 32.86 ? 1607 LEU A O     1 
ATOM   1208  C CB    . LEU A 1 1607 ? 253.012 205.253 218.547 1.00 37.19 ? 1607 LEU A CB    1 
ATOM   1209  C CG    . LEU A 1 1607 ? 254.378 204.580 218.690 1.00 36.31 ? 1607 LEU A CG    1 
ATOM   1210  C CD1   . LEU A 1 1607 ? 255.476 205.528 218.234 1.00 35.70 ? 1607 LEU A CD1   1 
ATOM   1211  C CD2   . LEU A 1 1607 ? 254.625 204.125 220.116 1.00 32.62 ? 1607 LEU A CD2   1 
ATOM   1212  N N     . LEU A 1 1608 ? 249.972 205.808 217.965 1.00 31.54 ? 1608 LEU A N     1 
ATOM   1213  C CA    . LEU A 1 1608 ? 248.816 206.698 217.975 1.00 31.48 ? 1608 LEU A CA    1 
ATOM   1214  C C     . LEU A 1 1608 ? 247.663 206.087 218.755 1.00 33.51 ? 1608 LEU A C     1 
ATOM   1215  O O     . LEU A 1 1608 ? 246.984 206.782 219.519 1.00 34.74 ? 1608 LEU A O     1 
ATOM   1216  C CB    . LEU A 1 1608 ? 248.385 207.022 216.544 1.00 29.42 ? 1608 LEU A CB    1 
ATOM   1217  C CG    . LEU A 1 1608 ? 248.870 208.361 215.990 1.00 32.39 ? 1608 LEU A CG    1 
ATOM   1218  C CD1   . LEU A 1 1608 ? 250.357 208.463 216.156 1.00 32.00 ? 1608 LEU A CD1   1 
ATOM   1219  C CD2   . LEU A 1 1608 ? 248.514 208.500 214.527 1.00 32.11 ? 1608 LEU A CD2   1 
ATOM   1220  N N     . GLY A 1 1609 ? 247.430 204.788 218.580 1.00 32.98 ? 1609 GLY A N     1 
ATOM   1221  C CA    . GLY A 1 1609 ? 246.397 204.126 219.356 1.00 30.10 ? 1609 GLY A CA    1 
ATOM   1222  C C     . GLY A 1 1609 ? 246.661 204.203 220.847 1.00 31.09 ? 1609 GLY A C     1 
ATOM   1223  O O     . GLY A 1 1609 ? 245.764 204.521 221.631 1.00 32.25 ? 1609 GLY A O     1 
ATOM   1224  N N     . LYS A 1 1610 ? 247.903 203.928 221.257 1.00 32.07 ? 1610 LYS A N     1 
ATOM   1225  C CA    . LYS A 1 1610 ? 248.220 203.956 222.685 1.00 33.15 ? 1610 LYS A CA    1 
ATOM   1226  C C     . LYS A 1 1610 ? 248.082 205.359 223.263 1.00 34.18 ? 1610 LYS A C     1 
ATOM   1227  O O     . LYS A 1 1610 ? 247.558 205.536 224.369 1.00 33.66 ? 1610 LYS A O     1 
ATOM   1228  C CB    . LYS A 1 1610 ? 249.623 203.411 222.947 1.00 34.63 ? 1610 LYS A CB    1 
ATOM   1229  C CG    . LYS A 1 1610 ? 249.676 201.904 223.096 1.00 32.90 ? 1610 LYS A CG    1 
ATOM   1230  C CD    . LYS A 1 1610 ? 250.790 201.312 222.272 1.00 35.40 ? 1610 LYS A CD    1 
ATOM   1231  C CE    . LYS A 1 1610 ? 252.133 201.851 222.729 1.00 37.59 ? 1610 LYS A CE    1 
ATOM   1232  N NZ    . LYS A 1 1610 ? 253.210 201.534 221.757 1.00 36.39 ? 1610 LYS A NZ    1 
ATOM   1233  N N     . ILE A 1 1611 ? 248.555 206.373 222.539 1.00 31.99 ? 1611 ILE A N     1 
ATOM   1234  C CA    . ILE A 1 1611 ? 248.492 207.729 223.076 1.00 31.74 ? 1611 ILE A CA    1 
ATOM   1235  C C     . ILE A 1 1611 ? 247.054 208.243 223.091 1.00 31.18 ? 1611 ILE A C     1 
ATOM   1236  O O     . ILE A 1 1611 ? 246.653 208.962 224.014 1.00 29.48 ? 1611 ILE A O     1 
ATOM   1237  C CB    . ILE A 1 1611 ? 249.447 208.663 222.308 1.00 32.87 ? 1611 ILE A CB    1 
ATOM   1238  C CG1   . ILE A 1 1611 ? 249.559 210.009 223.025 1.00 33.70 ? 1611 ILE A CG1   1 
ATOM   1239  C CG2   . ILE A 1 1611 ? 249.029 208.820 220.866 1.00 32.51 ? 1611 ILE A CG2   1 
ATOM   1240  C CD1   . ILE A 1 1611 ? 250.698 210.857 222.539 1.00 35.30 ? 1611 ILE A CD1   1 
ATOM   1241  N N     . GLN A 1 1612 ? 246.247 207.871 222.093 1.00 32.89 ? 1612 GLN A N     1 
ATOM   1242  C CA    . GLN A 1 1612 ? 244.834 208.233 222.119 1.00 33.11 ? 1612 GLN A CA    1 
ATOM   1243  C C     . GLN A 1 1612 ? 244.111 207.544 223.271 1.00 35.59 ? 1612 GLN A C     1 
ATOM   1244  O O     . GLN A 1 1612 ? 243.274 208.159 223.945 1.00 35.41 ? 1612 GLN A O     1 
ATOM   1245  C CB    . GLN A 1 1612 ? 244.180 207.884 220.781 1.00 31.11 ? 1612 GLN A CB    1 
ATOM   1246  C CG    . GLN A 1 1612 ? 242.658 207.833 220.816 1.00 30.18 ? 1612 GLN A CG    1 
ATOM   1247  C CD    . GLN A 1 1612 ? 242.030 208.122 219.464 1.00 35.77 ? 1612 GLN A CD    1 
ATOM   1248  O OE1   . GLN A 1 1612 ? 241.736 209.270 219.138 1.00 30.62 ? 1612 GLN A OE1   1 
ATOM   1249  N NE2   . GLN A 1 1612 ? 241.824 207.078 218.669 1.00 36.13 ? 1612 GLN A NE2   1 
ATOM   1250  N N     . LYS A 1 1613 ? 244.429 206.271 223.517 1.00 32.73 ? 1613 LYS A N     1 
ATOM   1251  C CA    . LYS A 1 1613 ? 243.845 205.571 224.656 1.00 29.70 ? 1613 LYS A CA    1 
ATOM   1252  C C     . LYS A 1 1613 ? 244.249 206.231 225.967 1.00 28.31 ? 1613 LYS A C     1 
ATOM   1253  O O     . LYS A 1 1613 ? 243.429 206.367 226.880 1.00 29.56 ? 1613 LYS A O     1 
ATOM   1254  C CB    . LYS A 1 1613 ? 244.265 204.102 224.637 1.00 31.86 ? 1613 LYS A CB    1 
ATOM   1255  C CG    . LYS A 1 1613 ? 243.463 203.207 225.568 1.00 35.53 ? 1613 LYS A CG    1 
ATOM   1256  C CD    . LYS A 1 1613 ? 242.005 203.135 225.146 1.00 32.16 ? 1613 LYS A CD    1 
ATOM   1257  C CE    . LYS A 1 1613 ? 241.237 202.129 225.986 1.00 28.91 ? 1613 LYS A CE    1 
ATOM   1258  N NZ    . LYS A 1 1613 ? 241.236 202.500 227.427 1.00 29.96 ? 1613 LYS A NZ    1 
ATOM   1259  N N     . ALA A 1 1614 ? 245.512 206.649 226.078 1.00 25.13 ? 1614 ALA A N     1 
ATOM   1260  C CA    . ALA A 1 1614 ? 245.963 207.330 227.288 1.00 30.19 ? 1614 ALA A CA    1 
ATOM   1261  C C     . ALA A 1 1614 ? 245.247 208.662 227.472 1.00 29.26 ? 1614 ALA A C     1 
ATOM   1262  O O     . ALA A 1 1614 ? 244.901 209.037 228.598 1.00 27.57 ? 1614 ALA A O     1 
ATOM   1263  C CB    . ALA A 1 1614 ? 247.477 207.532 227.246 1.00 32.68 ? 1614 ALA A CB    1 
ATOM   1264  N N     . LEU A 1 1615 ? 245.027 209.397 226.380 1.00 26.80 ? 1615 LEU A N     1 
ATOM   1265  C CA    . LEU A 1 1615 ? 244.276 210.645 226.474 1.00 25.59 ? 1615 LEU A CA    1 
ATOM   1266  C C     . LEU A 1 1615 ? 242.849 210.388 226.940 1.00 25.30 ? 1615 LEU A C     1 
ATOM   1267  O O     . LEU A 1 1615 ? 242.318 211.126 227.780 1.00 29.52 ? 1615 LEU A O     1 
ATOM   1268  C CB    . LEU A 1 1615 ? 244.291 211.370 225.125 1.00 26.53 ? 1615 LEU A CB    1 
ATOM   1269  C CG    . LEU A 1 1615 ? 243.719 212.787 225.018 1.00 25.89 ? 1615 LEU A CG    1 
ATOM   1270  C CD1   . LEU A 1 1615 ? 244.420 213.531 223.900 1.00 24.95 ? 1615 LEU A CD1   1 
ATOM   1271  C CD2   . LEU A 1 1615 ? 242.219 212.777 224.758 1.00 26.74 ? 1615 LEU A CD2   1 
ATOM   1272  N N     . GLY A 1 1616 ? 242.213 209.341 226.410 1.00 24.18 ? 1616 GLY A N     1 
ATOM   1273  C CA    . GLY A 1 1616 ? 240.877 208.994 226.868 1.00 26.70 ? 1616 GLY A CA    1 
ATOM   1274  C C     . GLY A 1 1616 ? 240.842 208.613 228.337 1.00 25.61 ? 1616 GLY A C     1 
ATOM   1275  O O     . GLY A 1 1616 ? 239.930 209.003 229.070 1.00 23.42 ? 1616 GLY A O     1 
ATOM   1276  N N     . GLU A 1 1617 ? 241.841 207.849 228.788 1.00 25.50 ? 1617 GLU A N     1 
ATOM   1277  C CA    . GLU A 1 1617 ? 241.907 207.469 230.197 1.00 26.46 ? 1617 GLU A CA    1 
ATOM   1278  C C     . GLU A 1 1617 ? 242.121 208.683 231.093 1.00 26.45 ? 1617 GLU A C     1 
ATOM   1279  O O     . GLU A 1 1617 ? 241.545 208.765 232.183 1.00 25.07 ? 1617 GLU A O     1 
ATOM   1280  C CB    . GLU A 1 1617 ? 243.014 206.437 230.422 1.00 26.63 ? 1617 GLU A CB    1 
ATOM   1281  C CG    . GLU A 1 1617 ? 242.881 205.121 229.643 1.00 28.54 ? 1617 GLU A CG    1 
ATOM   1282  C CD    . GLU A 1 1617 ? 241.679 204.263 230.039 1.00 32.14 ? 1617 GLU A CD    1 
ATOM   1283  O OE1   . GLU A 1 1617 ? 241.785 203.026 229.911 1.00 31.41 ? 1617 GLU A OE1   1 
ATOM   1284  O OE2   . GLU A 1 1617 ? 240.638 204.798 230.474 1.00 31.64 ? 1617 GLU A OE2   1 
ATOM   1285  N N     . TYR A 1 1618 ? 242.961 209.629 230.664 1.00 24.63 ? 1618 TYR A N     1 
ATOM   1286  C CA    . TYR A 1 1618 ? 243.151 210.838 231.459 1.00 26.60 ? 1618 TYR A CA    1 
ATOM   1287  C C     . TYR A 1 1618 ? 241.875 211.660 231.514 1.00 25.64 ? 1618 TYR A C     1 
ATOM   1288  O O     . TYR A 1 1618 ? 241.528 212.216 232.563 1.00 21.89 ? 1618 TYR A O     1 
ATOM   1289  C CB    . TYR A 1 1618 ? 244.298 211.682 230.908 1.00 25.60 ? 1618 TYR A CB    1 
ATOM   1290  C CG    . TYR A 1 1618 ? 244.396 213.032 231.584 1.00 25.13 ? 1618 TYR A CG    1 
ATOM   1291  C CD1   . TYR A 1 1618 ? 245.059 213.172 232.795 1.00 24.91 ? 1618 TYR A CD1   1 
ATOM   1292  C CD2   . TYR A 1 1618 ? 243.820 214.163 231.018 1.00 23.61 ? 1618 TYR A CD2   1 
ATOM   1293  C CE1   . TYR A 1 1618 ? 245.149 214.398 233.422 1.00 24.45 ? 1618 TYR A CE1   1 
ATOM   1294  C CE2   . TYR A 1 1618 ? 243.905 215.393 231.639 1.00 23.18 ? 1618 TYR A CE2   1 
ATOM   1295  C CZ    . TYR A 1 1618 ? 244.572 215.504 232.839 1.00 24.38 ? 1618 TYR A CZ    1 
ATOM   1296  O OH    . TYR A 1 1618 ? 244.662 216.725 233.463 1.00 23.81 ? 1618 TYR A OH    1 
ATOM   1297  N N     . LEU A 1 1619 ? 241.170 211.760 230.387 1.00 24.06 ? 1619 LEU A N     1 
ATOM   1298  C CA    . LEU A 1 1619 ? 239.888 212.450 230.385 1.00 23.47 ? 1619 LEU A CA    1 
ATOM   1299  C C     . LEU A 1 1619 ? 238.919 211.783 231.352 1.00 26.81 ? 1619 LEU A C     1 
ATOM   1300  O O     . LEU A 1 1619 ? 238.205 212.463 232.097 1.00 27.02 ? 1619 LEU A O     1 
ATOM   1301  C CB    . LEU A 1 1619 ? 239.327 212.482 228.962 1.00 18.62 ? 1619 LEU A CB    1 
ATOM   1302  C CG    . LEU A 1 1619 ? 238.079 213.305 228.643 1.00 22.28 ? 1619 LEU A CG    1 
ATOM   1303  C CD1   . LEU A 1 1619 ? 238.112 213.745 227.191 1.00 21.60 ? 1619 LEU A CD1   1 
ATOM   1304  C CD2   . LEU A 1 1619 ? 236.809 212.513 228.919 1.00 23.87 ? 1619 LEU A CD2   1 
ATOM   1305  N N     . GLU A 1 1620 ? 238.905 210.449 231.379 1.00 25.20 ? 1620 GLU A N     1 
ATOM   1306  C CA    . GLU A 1 1620 ? 238.017 209.737 232.293 1.00 18.81 ? 1620 GLU A CA    1 
ATOM   1307  C C     . GLU A 1 1620 ? 238.405 209.955 233.751 1.00 19.47 ? 1620 GLU A C     1 
ATOM   1308  O O     . GLU A 1 1620 ? 237.531 210.108 234.609 1.00 23.53 ? 1620 GLU A O     1 
ATOM   1309  C CB    . GLU A 1 1620 ? 237.996 208.247 231.960 1.00 20.51 ? 1620 GLU A CB    1 
ATOM   1310  C CG    . GLU A 1 1620 ? 236.948 207.879 230.929 1.00 26.25 ? 1620 GLU A CG    1 
ATOM   1311  C CD    . GLU A 1 1620 ? 235.555 208.313 231.349 1.00 26.94 ? 1620 GLU A CD    1 
ATOM   1312  O OE1   . GLU A 1 1620 ? 235.170 208.043 232.507 1.00 23.22 ? 1620 GLU A OE1   1 
ATOM   1313  O OE2   . GLU A 1 1620 ? 234.844 208.923 230.524 1.00 24.05 ? 1620 GLU A OE2   1 
ATOM   1314  N N     . ARG A 1 1621 ? 239.704 209.956 234.063 1.00 19.58 ? 1621 ARG A N     1 
ATOM   1315  C CA    . ARG A 1 1621 ? 240.088 210.118 235.464 1.00 21.56 ? 1621 ARG A CA    1 
ATOM   1316  C C     . ARG A 1 1621 ? 239.879 211.554 235.930 1.00 23.85 ? 1621 ARG A C     1 
ATOM   1317  O O     . ARG A 1 1621 ? 239.605 211.795 237.111 1.00 25.26 ? 1621 ARG A O     1 
ATOM   1318  C CB    . ARG A 1 1621 ? 241.534 209.676 235.714 1.00 24.83 ? 1621 ARG A CB    1 
ATOM   1319  C CG    . ARG A 1 1621 ? 242.631 210.485 235.041 1.00 26.94 ? 1621 ARG A CG    1 
ATOM   1320  C CD    . ARG A 1 1621 ? 243.999 209.953 235.471 1.00 24.94 ? 1621 ARG A CD    1 
ATOM   1321  N NE    . ARG A 1 1621 ? 244.257 208.583 235.042 1.00 27.43 ? 1621 ARG A NE    1 
ATOM   1322  C CZ    . ARG A 1 1621 ? 244.816 208.246 233.888 1.00 27.21 ? 1621 ARG A CZ    1 
ATOM   1323  N NH1   . ARG A 1 1621 ? 245.281 209.158 233.052 1.00 24.43 ? 1621 ARG A NH1   1 
ATOM   1324  N NH2   . ARG A 1 1621 ? 244.941 206.958 233.579 1.00 23.18 ? 1621 ARG A NH2   1 
ATOM   1325  N N     . GLU A 1 1622 ? 240.002 212.523 235.020 1.00 23.40 ? 1622 GLU A N     1 
ATOM   1326  C CA    . GLU A 1 1622 ? 239.705 213.903 235.389 1.00 21.44 ? 1622 GLU A CA    1 
ATOM   1327  C C     . GLU A 1 1622 ? 238.204 214.145 235.480 1.00 15.18 ? 1622 GLU A C     1 
ATOM   1328  O O     . GLU A 1 1622 ? 237.762 215.015 236.237 1.00 11.54 ? 1622 GLU A O     1 
ATOM   1329  C CB    . GLU A 1 1622 ? 240.340 214.867 234.390 1.00 20.17 ? 1622 GLU A CB    1 
ATOM   1330  C CG    . GLU A 1 1622 ? 240.439 216.297 234.893 1.00 19.40 ? 1622 GLU A CG    1 
ATOM   1331  C CD    . GLU A 1 1622 ? 241.535 216.475 235.922 1.00 22.16 ? 1622 GLU A CD    1 
ATOM   1332  O OE1   . GLU A 1 1622 ? 242.707 216.193 235.598 1.00 22.27 ? 1622 GLU A OE1   1 
ATOM   1333  O OE2   . GLU A 1 1622 ? 241.225 216.899 237.055 1.00 24.45 ? 1622 GLU A OE2   1 
ATOM   1334  N N     . ARG A 1 1623 ? 237.413 213.398 234.710 1.00 16.04 ? 1623 ARG A N     1 
ATOM   1335  C CA    . ARG A 1 1623 ? 235.963 213.510 234.775 1.00 15.65 ? 1623 ARG A CA    1 
ATOM   1336  C C     . ARG A 1 1623 ? 235.394 212.789 235.991 1.00 13.13 ? 1623 ARG A C     1 
ATOM   1337  O O     . ARG A 1 1623 ? 234.330 213.169 236.493 1.00 11.81 ? 1623 ARG A O     1 
ATOM   1338  C CB    . ARG A 1 1623 ? 235.366 212.961 233.480 1.00 12.48 ? 1623 ARG A CB    1 
ATOM   1339  C CG    . ARG A 1 1623 ? 233.861 212.930 233.400 1.00 13.11 ? 1623 ARG A CG    1 
ATOM   1340  C CD    . ARG A 1 1623 ? 233.446 212.575 231.986 1.00 15.96 ? 1623 ARG A CD    1 
ATOM   1341  N NE    . ARG A 1 1623 ? 233.560 213.715 231.086 1.00 12.24 ? 1623 ARG A NE    1 
ATOM   1342  C CZ    . ARG A 1 1623 ? 233.311 213.669 229.785 1.00 12.28 ? 1623 ARG A CZ    1 
ATOM   1343  N NH1   . ARG A 1 1623 ? 232.951 212.545 229.190 1.00 13.54 ? 1623 ARG A NH1   1 
ATOM   1344  N NH2   . ARG A 1 1623 ? 233.432 214.777 229.061 1.00 15.08 ? 1623 ARG A NH2   1 
ATOM   1345  N N     . SER A 1 1624 ? 236.086 211.755 236.474 1.00 13.63 ? 1624 SER A N     1 
ATOM   1346  C CA    . SER A 1 1624 ? 235.646 211.050 237.673 1.00 10.13 ? 1624 SER A CA    1 
ATOM   1347  C C     . SER A 1 1624 ? 235.657 211.976 238.881 1.00 10.87 ? 1624 SER A C     1 
ATOM   1348  O O     . SER A 1 1624 ? 234.719 211.979 239.687 1.00 16.33 ? 1624 SER A O     1 
ATOM   1349  C CB    . SER A 1 1624 ? 236.539 209.832 237.915 1.00 13.83 ? 1624 SER A CB    1 
ATOM   1350  O OG    . SER A 1 1624 ? 236.009 209.001 238.931 1.00 18.54 ? 1624 SER A OG    1 
ATOM   1351  N N     . SER A 1 1625 ? 236.716 212.765 239.026 1.00 12.53 ? 1625 SER A N     1 
ATOM   1352  C CA    . SER A 1 1625 ? 236.723 213.827 240.019 1.00 14.99 ? 1625 SER A CA    1 
ATOM   1353  C C     . SER A 1 1625 ? 235.910 215.008 239.506 1.00 15.03 ? 1625 SER A C     1 
ATOM   1354  O O     . SER A 1 1625 ? 235.963 215.345 238.321 1.00 20.12 ? 1625 SER A O     1 
ATOM   1355  C CB    . SER A 1 1625 ? 238.154 214.259 240.326 1.00 12.57 ? 1625 SER A CB    1 
ATOM   1356  O OG    . SER A 1 1625 ? 238.893 213.203 240.915 1.00 15.02 ? 1625 SER A OG    1 
ATOM   1357  N N     . PHE A 1 1626 ? 235.168 215.646 240.412 1.00 12.22 ? 1626 PHE A N     1 
ATOM   1358  C CA    . PHE A 1 1626 ? 234.206 216.686 240.060 1.00 11.24 ? 1626 PHE A CA    1 
ATOM   1359  C C     . PHE A 1 1626 ? 233.268 216.106 239.002 1.00 8.59  ? 1626 PHE A C     1 
ATOM   1360  O O     . PHE A 1 1626 ? 233.429 216.364 237.803 1.00 2.47  ? 1626 PHE A O     1 
ATOM   1361  C CB    . PHE A 1 1626 ? 234.927 217.964 239.606 1.00 4.30  ? 1626 PHE A CB    1 
ATOM   1362  C CG    . PHE A 1 1626 ? 234.009 219.066 239.145 1.00 6.12  ? 1626 PHE A CG    1 
ATOM   1363  C CD1   . PHE A 1 1626 ? 233.652 219.200 237.817 1.00 6.92  ? 1626 PHE A CD1   1 
ATOM   1364  C CD2   . PHE A 1 1626 ? 233.482 219.959 240.062 1.00 9.05  ? 1626 PHE A CD2   1 
ATOM   1365  C CE1   . PHE A 1 1626 ? 232.811 220.210 237.412 1.00 5.74  ? 1626 PHE A CE1   1 
ATOM   1366  C CE2   . PHE A 1 1626 ? 232.634 220.969 239.661 1.00 2.31  ? 1626 PHE A CE2   1 
ATOM   1367  C CZ    . PHE A 1 1626 ? 232.298 221.093 238.335 1.00 2.64  ? 1626 PHE A CZ    1 
ATOM   1368  N N     . PRO A 1 1627 ? 232.323 215.253 239.411 1.00 3.32  ? 1627 PRO A N     1 
ATOM   1369  C CA    . PRO A 1 1627 ? 231.524 214.487 238.442 1.00 3.00  ? 1627 PRO A CA    1 
ATOM   1370  C C     . PRO A 1 1627 ? 230.607 215.314 237.552 1.00 13.58 ? 1627 PRO A C     1 
ATOM   1371  O O     . PRO A 1 1627 ? 229.923 214.750 236.692 1.00 14.57 ? 1627 PRO A O     1 
ATOM   1372  C CB    . PRO A 1 1627 ? 230.702 213.550 239.337 1.00 1.69  ? 1627 PRO A CB    1 
ATOM   1373  C CG    . PRO A 1 1627 ? 231.420 213.518 240.641 1.00 5.22  ? 1627 PRO A CG    1 
ATOM   1374  C CD    . PRO A 1 1627 ? 232.027 214.868 240.799 1.00 4.06  ? 1627 PRO A CD    1 
ATOM   1375  N N     . ARG A 1 1628 ? 230.557 216.635 237.743 1.00 11.53 ? 1628 ARG A N     1 
ATOM   1376  C CA    . ARG A 1 1628 ? 229.771 217.468 236.840 1.00 1.12  ? 1628 ARG A CA    1 
ATOM   1377  C C     . ARG A 1 1628 ? 230.336 217.467 235.427 1.00 4.77  ? 1628 ARG A C     1 
ATOM   1378  O O     . ARG A 1 1628 ? 229.624 217.832 234.488 1.00 16.22 ? 1628 ARG A O     1 
ATOM   1379  C CB    . ARG A 1 1628 ? 229.690 218.902 237.362 1.00 4.81  ? 1628 ARG A CB    1 
ATOM   1380  C CG    . ARG A 1 1628 ? 229.192 219.039 238.787 1.00 9.00  ? 1628 ARG A CG    1 
ATOM   1381  C CD    . ARG A 1 1628 ? 227.705 219.326 238.814 1.00 5.41  ? 1628 ARG A CD    1 
ATOM   1382  N NE    . ARG A 1 1628 ? 227.258 219.780 240.124 1.00 0.00  ? 1628 ARG A NE    1 
ATOM   1383  C CZ    . ARG A 1 1628 ? 226.137 220.453 240.338 1.00 0.40  ? 1628 ARG A CZ    1 
ATOM   1384  N NH1   . ARG A 1 1628 ? 225.329 220.783 239.345 1.00 2.37  ? 1628 ARG A NH1   1 
ATOM   1385  N NH2   . ARG A 1 1628 ? 225.818 220.804 241.580 1.00 3.76  ? 1628 ARG A NH2   1 
ATOM   1386  N N     . PHE A 1 1629 ? 231.596 217.059 235.256 1.00 5.92  ? 1629 PHE A N     1 
ATOM   1387  C CA    . PHE A 1 1629 ? 232.207 216.966 233.935 1.00 5.75  ? 1629 PHE A CA    1 
ATOM   1388  C C     . PHE A 1 1629 ? 231.565 215.902 233.057 1.00 5.28  ? 1629 PHE A C     1 
ATOM   1389  O O     . PHE A 1 1629 ? 231.829 215.882 231.851 1.00 7.83  ? 1629 PHE A O     1 
ATOM   1390  C CB    . PHE A 1 1629 ? 233.703 216.681 234.066 1.00 9.63  ? 1629 PHE A CB    1 
ATOM   1391  C CG    . PHE A 1 1629 ? 234.527 217.896 234.376 1.00 11.79 ? 1629 PHE A CG    1 
ATOM   1392  C CD1   . PHE A 1 1629 ? 234.117 219.150 233.964 1.00 7.82  ? 1629 PHE A CD1   1 
ATOM   1393  C CD2   . PHE A 1 1629 ? 235.714 217.782 235.078 1.00 9.12  ? 1629 PHE A CD2   1 
ATOM   1394  C CE1   . PHE A 1 1629 ? 234.874 220.267 234.247 1.00 6.81  ? 1629 PHE A CE1   1 
ATOM   1395  C CE2   . PHE A 1 1629 ? 236.475 218.896 235.363 1.00 3.88  ? 1629 PHE A CE2   1 
ATOM   1396  C CZ    . PHE A 1 1629 ? 236.055 220.139 234.947 1.00 5.89  ? 1629 PHE A CZ    1 
ATOM   1397  N N     . TYR A 1 1630 ? 230.745 215.016 233.624 1.00 8.04  ? 1630 TYR A N     1 
ATOM   1398  C CA    . TYR A 1 1630 ? 230.048 214.023 232.819 1.00 8.66  ? 1630 TYR A CA    1 
ATOM   1399  C C     . TYR A 1 1630 ? 228.949 214.627 231.958 1.00 7.83  ? 1630 TYR A C     1 
ATOM   1400  O O     . TYR A 1 1630 ? 228.409 213.930 231.094 1.00 8.73  ? 1630 TYR A O     1 
ATOM   1401  C CB    . TYR A 1 1630 ? 229.448 212.941 233.714 1.00 3.49  ? 1630 TYR A CB    1 
ATOM   1402  C CG    . TYR A 1 1630 ? 230.440 211.903 234.177 1.00 6.71  ? 1630 TYR A CG    1 
ATOM   1403  C CD1   . TYR A 1 1630 ? 230.771 210.825 233.372 1.00 1.97  ? 1630 TYR A CD1   1 
ATOM   1404  C CD2   . TYR A 1 1630 ? 231.028 211.988 235.431 1.00 11.36 ? 1630 TYR A CD2   1 
ATOM   1405  C CE1   . TYR A 1 1630 ? 231.674 209.873 233.793 1.00 6.48  ? 1630 TYR A CE1   1 
ATOM   1406  C CE2   . TYR A 1 1630 ? 231.929 211.038 235.862 1.00 7.36  ? 1630 TYR A CE2   1 
ATOM   1407  C CZ    . TYR A 1 1630 ? 232.247 209.983 235.040 1.00 10.29 ? 1630 TYR A CZ    1 
ATOM   1408  O OH    . TYR A 1 1630 ? 233.146 209.034 235.466 1.00 16.19 ? 1630 TYR A OH    1 
ATOM   1409  N N     . PHE A 1 1631 ? 228.598 215.890 232.175 1.00 7.47  ? 1631 PHE A N     1 
ATOM   1410  C CA    . PHE A 1 1631 ? 227.568 216.553 231.392 1.00 2.10  ? 1631 PHE A CA    1 
ATOM   1411  C C     . PHE A 1 1631 ? 228.123 217.281 230.178 1.00 8.44  ? 1631 PHE A C     1 
ATOM   1412  O O     . PHE A 1 1631 ? 227.345 217.862 229.416 1.00 17.15 ? 1631 PHE A O     1 
ATOM   1413  C CB    . PHE A 1 1631 ? 226.790 217.533 232.273 1.00 3.31  ? 1631 PHE A CB    1 
ATOM   1414  C CG    . PHE A 1 1631 ? 226.162 216.895 233.477 1.00 5.92  ? 1631 PHE A CG    1 
ATOM   1415  C CD1   . PHE A 1 1631 ? 225.236 215.879 233.331 1.00 8.86  ? 1631 PHE A CD1   1 
ATOM   1416  C CD2   . PHE A 1 1631 ? 226.495 217.309 234.752 1.00 6.18  ? 1631 PHE A CD2   1 
ATOM   1417  C CE1   . PHE A 1 1631 ? 224.655 215.289 234.433 1.00 1.27  ? 1631 PHE A CE1   1 
ATOM   1418  C CE2   . PHE A 1 1631 ? 225.918 216.721 235.857 1.00 4.76  ? 1631 PHE A CE2   1 
ATOM   1419  C CZ    . PHE A 1 1631 ? 224.996 215.712 235.697 1.00 4.28  ? 1631 PHE A CZ    1 
ATOM   1420  N N     . VAL A 1 1632 ? 229.439 217.259 229.975 1.00 8.34  ? 1632 VAL A N     1 
ATOM   1421  C CA    . VAL A 1 1632 ? 230.069 217.916 228.839 1.00 5.58  ? 1632 VAL A CA    1 
ATOM   1422  C C     . VAL A 1 1632 ? 230.762 216.865 227.981 1.00 7.15  ? 1632 VAL A C     1 
ATOM   1423  O O     . VAL A 1 1632 ? 231.076 215.761 228.432 1.00 11.19 ? 1632 VAL A O     1 
ATOM   1424  C CB    . VAL A 1 1632 ? 231.067 219.010 229.277 1.00 9.26  ? 1632 VAL A CB    1 
ATOM   1425  C CG1   . VAL A 1 1632 ? 230.423 219.940 230.291 1.00 9.12  ? 1632 VAL A CG1   1 
ATOM   1426  C CG2   . VAL A 1 1632 ? 232.325 218.389 229.850 1.00 13.49 ? 1632 VAL A CG2   1 
ATOM   1427  N N     . GLY A 1 1633 ? 230.991 217.225 226.719 1.00 14.41 ? 1633 GLY A N     1 
ATOM   1428  C CA    . GLY A 1 1633 ? 231.653 216.344 225.783 1.00 18.02 ? 1633 GLY A CA    1 
ATOM   1429  C C     . GLY A 1 1633 ? 233.159 216.340 225.948 1.00 21.87 ? 1633 GLY A C     1 
ATOM   1430  O O     . GLY A 1 1633 ? 233.736 217.059 226.763 1.00 24.61 ? 1633 GLY A O     1 
ATOM   1431  N N     . ASP A 1 1634 ? 233.809 215.491 225.146 1.00 25.23 ? 1634 ASP A N     1 
ATOM   1432  C CA    . ASP A 1 1634 ? 235.262 215.371 225.220 1.00 26.82 ? 1634 ASP A CA    1 
ATOM   1433  C C     . ASP A 1 1634 ? 235.950 216.663 224.800 1.00 27.89 ? 1634 ASP A C     1 
ATOM   1434  O O     . ASP A 1 1634 ? 236.908 217.102 225.447 1.00 27.14 ? 1634 ASP A O     1 
ATOM   1435  C CB    . ASP A 1 1634 ? 235.738 214.207 224.353 1.00 25.71 ? 1634 ASP A CB    1 
ATOM   1436  C CG    . ASP A 1 1634 ? 235.347 212.861 224.920 1.00 27.72 ? 1634 ASP A CG    1 
ATOM   1437  O OD1   . ASP A 1 1634 ? 235.119 212.776 226.144 1.00 24.91 ? 1634 ASP A OD1   1 
ATOM   1438  O OD2   . ASP A 1 1634 ? 235.272 211.886 224.144 1.00 30.64 ? 1634 ASP A OD2   1 
ATOM   1439  N N     . GLU A 1 1635 ? 235.482 217.285 223.716 1.00 28.34 ? 1635 GLU A N     1 
ATOM   1440  C CA    . GLU A 1 1635 ? 236.087 218.534 223.265 1.00 28.52 ? 1635 GLU A CA    1 
ATOM   1441  C C     . GLU A 1 1635 ? 235.866 219.653 224.277 1.00 32.18 ? 1635 GLU A C     1 
ATOM   1442  O O     . GLU A 1 1635 ? 236.788 220.425 224.568 1.00 30.91 ? 1635 GLU A O     1 
ATOM   1443  C CB    . GLU A 1 1635 ? 235.543 218.928 221.887 1.00 29.91 ? 1635 GLU A CB    1 
ATOM   1444  C CG    . GLU A 1 1635 ? 234.032 219.193 221.784 1.00 31.11 ? 1635 GLU A CG    1 
ATOM   1445  C CD    . GLU A 1 1635 ? 233.158 217.970 222.031 1.00 35.34 ? 1635 GLU A CD    1 
ATOM   1446  O OE1   . GLU A 1 1635 ? 233.699 216.870 222.276 1.00 35.46 ? 1635 GLU A OE1   1 
ATOM   1447  O OE2   . GLU A 1 1635 ? 231.918 218.112 221.981 1.00 37.21 ? 1635 GLU A OE2   1 
ATOM   1448  N N     . ASP A 1 1636 ? 234.655 219.747 224.833 1.00 27.05 ? 1636 ASP A N     1 
ATOM   1449  C CA    . ASP A 1 1636 ? 234.372 220.780 225.822 1.00 21.95 ? 1636 ASP A CA    1 
ATOM   1450  C C     . ASP A 1 1636 ? 235.195 220.575 227.086 1.00 21.74 ? 1636 ASP A C     1 
ATOM   1451  O O     . ASP A 1 1636 ? 235.709 221.539 227.664 1.00 26.12 ? 1636 ASP A O     1 
ATOM   1452  C CB    . ASP A 1 1636 ? 232.880 220.798 226.147 1.00 20.83 ? 1636 ASP A CB    1 
ATOM   1453  C CG    . ASP A 1 1636 ? 232.031 221.167 224.949 1.00 28.81 ? 1636 ASP A CG    1 
ATOM   1454  O OD1   . ASP A 1 1636 ? 232.541 221.866 224.049 1.00 25.99 ? 1636 ASP A OD1   1 
ATOM   1455  O OD2   . ASP A 1 1636 ? 230.851 220.761 224.907 1.00 28.81 ? 1636 ASP A OD2   1 
ATOM   1456  N N     . LEU A 1 1637 ? 235.340 219.325 227.531 1.00 19.18 ? 1637 LEU A N     1 
ATOM   1457  C CA    . LEU A 1 1637 ? 236.135 219.065 228.726 1.00 22.03 ? 1637 LEU A CA    1 
ATOM   1458  C C     . LEU A 1 1637 ? 237.617 219.317 228.467 1.00 24.98 ? 1637 LEU A C     1 
ATOM   1459  O O     . LEU A 1 1637 ? 238.339 219.782 229.357 1.00 25.87 ? 1637 LEU A O     1 
ATOM   1460  C CB    . LEU A 1 1637 ? 235.896 217.638 229.220 1.00 16.22 ? 1637 LEU A CB    1 
ATOM   1461  C CG    . LEU A 1 1637 ? 236.795 217.157 230.358 1.00 16.83 ? 1637 LEU A CG    1 
ATOM   1462  C CD1   . LEU A 1 1637 ? 236.600 218.027 231.576 1.00 18.80 ? 1637 LEU A CD1   1 
ATOM   1463  C CD2   . LEU A 1 1637 ? 236.476 215.722 230.700 1.00 18.18 ? 1637 LEU A CD2   1 
ATOM   1464  N N     . LEU A 1 1638 ? 238.089 219.020 227.255 1.00 21.59 ? 1638 LEU A N     1 
ATOM   1465  C CA    . LEU A 1 1638 ? 239.464 219.356 226.900 1.00 23.52 ? 1638 LEU A CA    1 
ATOM   1466  C C     . LEU A 1 1638 ? 239.680 220.864 226.923 1.00 26.64 ? 1638 LEU A C     1 
ATOM   1467  O O     . LEU A 1 1638 ? 240.710 221.344 227.411 1.00 26.28 ? 1638 LEU A O     1 
ATOM   1468  C CB    . LEU A 1 1638 ? 239.810 218.781 225.528 1.00 22.51 ? 1638 LEU A CB    1 
ATOM   1469  C CG    . LEU A 1 1638 ? 240.269 217.323 225.515 1.00 24.01 ? 1638 LEU A CG    1 
ATOM   1470  C CD1   . LEU A 1 1638 ? 240.323 216.791 224.095 1.00 25.75 ? 1638 LEU A CD1   1 
ATOM   1471  C CD2   . LEU A 1 1638 ? 241.622 217.185 226.190 1.00 23.92 ? 1638 LEU A CD2   1 
ATOM   1472  N N     . GLU A 1 1639 ? 238.714 221.627 226.407 1.00 25.83 ? 1639 GLU A N     1 
ATOM   1473  C CA    . GLU A 1 1639 ? 238.792 223.081 226.506 1.00 24.39 ? 1639 GLU A CA    1 
ATOM   1474  C C     . GLU A 1 1639 ? 238.823 223.528 227.961 1.00 24.68 ? 1639 GLU A C     1 
ATOM   1475  O O     . GLU A 1 1639 ? 239.603 224.412 228.333 1.00 29.94 ? 1639 GLU A O     1 
ATOM   1476  C CB    . GLU A 1 1639 ? 237.607 223.726 225.788 1.00 21.64 ? 1639 GLU A CB    1 
ATOM   1477  C CG    . GLU A 1 1639 ? 237.543 223.459 224.301 1.00 26.22 ? 1639 GLU A CG    1 
ATOM   1478  C CD    . GLU A 1 1639 ? 236.279 224.013 223.676 1.00 29.25 ? 1639 GLU A CD    1 
ATOM   1479  O OE1   . GLU A 1 1639 ? 235.695 224.953 224.254 1.00 22.41 ? 1639 GLU A OE1   1 
ATOM   1480  O OE2   . GLU A 1 1639 ? 235.871 223.508 222.609 1.00 30.71 ? 1639 GLU A OE2   1 
ATOM   1481  N N     . ILE A 1 1640 ? 237.980 222.922 228.797 1.00 20.05 ? 1640 ILE A N     1 
ATOM   1482  C CA    . ILE A 1 1640 ? 237.894 223.316 230.200 1.00 23.27 ? 1640 ILE A CA    1 
ATOM   1483  C C     . ILE A 1 1640 ? 239.224 223.073 230.906 1.00 27.11 ? 1640 ILE A C     1 
ATOM   1484  O O     . ILE A 1 1640 ? 239.744 223.947 231.609 1.00 27.98 ? 1640 ILE A O     1 
ATOM   1485  C CB    . ILE A 1 1640 ? 236.742 222.564 230.889 1.00 22.26 ? 1640 ILE A CB    1 
ATOM   1486  C CG1   . ILE A 1 1640 ? 235.393 223.138 230.454 1.00 18.02 ? 1640 ILE A CG1   1 
ATOM   1487  C CG2   . ILE A 1 1640 ? 236.882 222.623 232.396 1.00 21.51 ? 1640 ILE A CG2   1 
ATOM   1488  C CD1   . ILE A 1 1640 ? 234.208 222.359 230.973 1.00 18.34 ? 1640 ILE A CD1   1 
ATOM   1489  N N     . ILE A 1 1641 ? 239.805 221.888 230.710 1.00 24.32 ? 1641 ILE A N     1 
ATOM   1490  C CA    . ILE A 1 1641 ? 241.016 221.530 231.441 1.00 24.36 ? 1641 ILE A CA    1 
ATOM   1491  C C     . ILE A 1 1641 ? 242.279 222.078 230.790 1.00 31.05 ? 1641 ILE A C     1 
ATOM   1492  O O     . ILE A 1 1641 ? 243.354 222.017 231.400 1.00 32.77 ? 1641 ILE A O     1 
ATOM   1493  C CB    . ILE A 1 1641 ? 241.136 220.005 231.593 1.00 24.71 ? 1641 ILE A CB    1 
ATOM   1494  C CG1   . ILE A 1 1641 ? 241.411 219.351 230.237 1.00 24.00 ? 1641 ILE A CG1   1 
ATOM   1495  C CG2   . ILE A 1 1641 ? 239.879 219.437 232.228 1.00 23.32 ? 1641 ILE A CG2   1 
ATOM   1496  C CD1   . ILE A 1 1641 ? 241.630 217.858 230.313 1.00 25.33 ? 1641 ILE A CD1   1 
ATOM   1497  N N     . GLY A 1 1642 ? 242.188 222.607 229.573 1.00 32.31 ? 1642 GLY A N     1 
ATOM   1498  C CA    . GLY A 1 1642 ? 243.355 223.167 228.923 1.00 29.47 ? 1642 GLY A CA    1 
ATOM   1499  C C     . GLY A 1 1642 ? 243.531 224.650 229.167 1.00 30.70 ? 1642 GLY A C     1 
ATOM   1500  O O     . GLY A 1 1642 ? 244.659 225.144 229.258 1.00 33.15 ? 1642 GLY A O     1 
ATOM   1501  N N     . ASN A 1 1643 ? 242.418 225.376 229.274 1.00 31.20 ? 1643 ASN A N     1 
ATOM   1502  C CA    . ASN A 1 1643 ? 242.449 226.823 229.472 1.00 31.57 ? 1643 ASN A CA    1 
ATOM   1503  C C     . ASN A 1 1643 ? 242.416 227.166 230.963 1.00 33.38 ? 1643 ASN A C     1 
ATOM   1504  O O     . ASN A 1 1643 ? 241.552 227.891 231.455 1.00 35.85 ? 1643 ASN A O     1 
ATOM   1505  C CB    . ASN A 1 1643 ? 241.295 227.476 228.722 1.00 28.75 ? 1643 ASN A CB    1 
ATOM   1506  C CG    . ASN A 1 1643 ? 241.156 226.957 227.304 1.00 29.17 ? 1643 ASN A CG    1 
ATOM   1507  O OD1   . ASN A 1 1643 ? 240.053 226.684 226.835 1.00 27.83 ? 1643 ASN A OD1   1 
ATOM   1508  N ND2   . ASN A 1 1643 ? 242.281 226.818 226.613 1.00 31.07 ? 1643 ASN A ND2   1 
ATOM   1509  N N     . SER A 1 1644 ? 243.393 226.617 231.689 1.00 35.51 ? 1644 SER A N     1 
ATOM   1510  C CA    . SER A 1 1644 ? 243.507 226.912 233.113 1.00 36.81 ? 1644 SER A CA    1 
ATOM   1511  C C     . SER A 1 1644 ? 243.879 228.370 233.349 1.00 34.37 ? 1644 SER A C     1 
ATOM   1512  O O     . SER A 1 1644 ? 243.330 229.019 234.247 1.00 37.26 ? 1644 SER A O     1 
ATOM   1513  C CB    . SER A 1 1644 ? 244.533 225.984 233.763 1.00 35.57 ? 1644 SER A CB    1 
ATOM   1514  O OG    . SER A 1 1644 ? 244.663 226.258 235.148 1.00 35.15 ? 1644 SER A OG    1 
ATOM   1515  N N     . LYS A 1 1645 ? 244.815 228.902 232.561 1.00 35.86 ? 1645 LYS A N     1 
ATOM   1516  C CA    . LYS A 1 1645 ? 245.197 230.301 232.722 1.00 37.72 ? 1645 LYS A CA    1 
ATOM   1517  C C     . LYS A 1 1645 ? 244.105 231.233 232.215 1.00 36.75 ? 1645 LYS A C     1 
ATOM   1518  O O     . LYS A 1 1645 ? 243.760 232.216 232.882 1.00 36.54 ? 1645 LYS A O     1 
ATOM   1519  C CB    . LYS A 1 1645 ? 246.517 230.574 232.000 1.00 38.46 ? 1645 LYS A CB    1 
ATOM   1520  C CG    . LYS A 1 1645 ? 247.630 229.600 232.353 1.00 38.64 ? 1645 LYS A CG    1 
ATOM   1521  C CD    . LYS A 1 1645 ? 247.766 229.441 233.860 1.00 36.33 ? 1645 LYS A CD    1 
ATOM   1522  C CE    . LYS A 1 1645 ? 248.703 228.299 234.214 1.00 36.92 ? 1645 LYS A CE    1 
ATOM   1523  N NZ    . LYS A 1 1645 ? 248.762 228.069 235.683 1.00 37.70 ? 1645 LYS A NZ    1 
ATOM   1524  N N     . ASN A 1 1646 ? 243.543 230.940 231.041 1.00 34.11 ? 1646 ASN A N     1 
ATOM   1525  C CA    . ASN A 1 1646 ? 242.480 231.762 230.466 1.00 33.79 ? 1646 ASN A CA    1 
ATOM   1526  C C     . ASN A 1 1646 ? 241.130 231.265 230.986 1.00 32.93 ? 1646 ASN A C     1 
ATOM   1527  O O     . ASN A 1 1646 ? 240.360 230.589 230.300 1.00 30.08 ? 1646 ASN A O     1 
ATOM   1528  C CB    . ASN A 1 1646 ? 242.547 231.741 228.946 1.00 31.49 ? 1646 ASN A CB    1 
ATOM   1529  C CG    . ASN A 1 1646 ? 241.765 232.874 228.314 1.00 33.84 ? 1646 ASN A CG    1 
ATOM   1530  O OD1   . ASN A 1 1646 ? 241.725 233.985 228.842 1.00 31.49 ? 1646 ASN A OD1   1 
ATOM   1531  N ND2   . ASN A 1 1646 ? 241.148 232.603 227.171 1.00 33.65 ? 1646 ASN A ND2   1 
ATOM   1532  N N     . VAL A 1 1647 ? 240.856 231.621 232.243 1.00 32.33 ? 1647 VAL A N     1 
ATOM   1533  C CA    . VAL A 1 1647 ? 239.630 231.205 232.916 1.00 26.52 ? 1647 VAL A CA    1 
ATOM   1534  C C     . VAL A 1 1647 ? 238.377 231.732 232.234 1.00 26.85 ? 1647 VAL A C     1 
ATOM   1535  O O     . VAL A 1 1647 ? 237.327 231.084 232.303 1.00 28.15 ? 1647 VAL A O     1 
ATOM   1536  C CB    . VAL A 1 1647 ? 239.684 231.660 234.391 1.00 26.98 ? 1647 VAL A CB    1 
ATOM   1537  C CG1   . VAL A 1 1647 ? 238.387 231.343 235.118 1.00 29.34 ? 1647 VAL A CG1   1 
ATOM   1538  C CG2   . VAL A 1 1647 ? 240.865 231.017 235.101 1.00 27.56 ? 1647 VAL A CG2   1 
ATOM   1539  N N     . ALA A 1 1648 ? 238.470 232.866 231.539 1.00 26.44 ? 1648 ALA A N     1 
ATOM   1540  C CA    . ALA A 1 1648 ? 237.305 233.530 230.967 1.00 25.93 ? 1648 ALA A CA    1 
ATOM   1541  C C     . ALA A 1 1648 ? 236.563 232.685 229.938 1.00 24.51 ? 1648 ALA A C     1 
ATOM   1542  O O     . ALA A 1 1648 ? 235.401 232.983 229.646 1.00 23.37 ? 1648 ALA A O     1 
ATOM   1543  C CB    . ALA A 1 1648 ? 237.721 234.857 230.329 1.00 25.55 ? 1648 ALA A CB    1 
ATOM   1544  N N     . LYS A 1 1649 ? 237.194 231.654 229.381 1.00 22.48 ? 1649 LYS A N     1 
ATOM   1545  C CA    . LYS A 1 1649 ? 236.520 230.766 228.443 1.00 24.12 ? 1649 LYS A CA    1 
ATOM   1546  C C     . LYS A 1 1649 ? 235.696 229.686 229.131 1.00 27.58 ? 1649 LYS A C     1 
ATOM   1547  O O     . LYS A 1 1649 ? 234.928 228.993 228.456 1.00 25.20 ? 1649 LYS A O     1 
ATOM   1548  C CB    . LYS A 1 1649 ? 237.540 230.109 227.509 1.00 23.44 ? 1649 LYS A CB    1 
ATOM   1549  C CG    . LYS A 1 1649 ? 238.345 231.099 226.689 1.00 23.34 ? 1649 LYS A CG    1 
ATOM   1550  C CD    . LYS A 1 1649 ? 238.547 230.619 225.262 1.00 22.87 ? 1649 LYS A CD    1 
ATOM   1551  C CE    . LYS A 1 1649 ? 238.952 229.158 225.217 1.00 21.68 ? 1649 LYS A CE    1 
ATOM   1552  N NZ    . LYS A 1 1649 ? 239.082 228.658 223.822 1.00 23.08 ? 1649 LYS A NZ    1 
ATOM   1553  N N     . LEU A 1 1650 ? 235.837 229.525 230.448 1.00 27.25 ? 1650 LEU A N     1 
ATOM   1554  C CA    . LEU A 1 1650 ? 235.068 228.509 231.158 1.00 20.98 ? 1650 LEU A CA    1 
ATOM   1555  C C     . LEU A 1 1650 ? 233.615 228.922 231.340 1.00 17.14 ? 1650 LEU A C     1 
ATOM   1556  O O     . LEU A 1 1650 ? 232.742 228.059 231.473 1.00 17.39 ? 1650 LEU A O     1 
ATOM   1557  C CB    . LEU A 1 1650 ? 235.702 228.222 232.518 1.00 21.08 ? 1650 LEU A CB    1 
ATOM   1558  C CG    . LEU A 1 1650 ? 236.763 227.125 232.599 1.00 20.50 ? 1650 LEU A CG    1 
ATOM   1559  C CD1   . LEU A 1 1650 ? 238.004 227.495 231.806 1.00 19.99 ? 1650 LEU A CD1   1 
ATOM   1560  C CD2   . LEU A 1 1650 ? 237.111 226.858 234.053 1.00 24.51 ? 1650 LEU A CD2   1 
ATOM   1561  N N     . GLN A 1 1651 ? 233.335 230.227 231.341 1.00 11.86 ? 1651 GLN A N     1 
ATOM   1562  C CA    . GLN A 1 1651 ? 231.995 230.718 231.637 1.00 18.12 ? 1651 GLN A CA    1 
ATOM   1563  C C     . GLN A 1 1651 ? 230.959 230.302 230.603 1.00 19.84 ? 1651 GLN A C     1 
ATOM   1564  O O     . GLN A 1 1651 ? 229.760 230.419 230.878 1.00 26.28 ? 1651 GLN A O     1 
ATOM   1565  C CB    . GLN A 1 1651 ? 232.010 232.243 231.770 1.00 17.99 ? 1651 GLN A CB    1 
ATOM   1566  C CG    . GLN A 1 1651 ? 232.560 232.757 233.097 1.00 18.95 ? 1651 GLN A CG    1 
ATOM   1567  C CD    . GLN A 1 1651 ? 234.069 232.643 233.208 1.00 24.71 ? 1651 GLN A CD    1 
ATOM   1568  O OE1   . GLN A 1 1651 ? 234.721 232.013 232.377 1.00 24.61 ? 1651 GLN A OE1   1 
ATOM   1569  N NE2   . GLN A 1 1651 ? 234.632 233.253 234.244 1.00 19.63 ? 1651 GLN A NE2   1 
ATOM   1570  N N     . LYS A 1 1652 ? 231.377 229.826 229.434 1.00 13.61 ? 1652 LYS A N     1 
ATOM   1571  C CA    . LYS A 1 1652 ? 230.443 229.319 228.439 1.00 14.30 ? 1652 LYS A CA    1 
ATOM   1572  C C     . LYS A 1 1652 ? 230.052 227.869 228.686 1.00 20.38 ? 1652 LYS A C     1 
ATOM   1573  O O     . LYS A 1 1652 ? 229.148 227.363 228.014 1.00 20.67 ? 1652 LYS A O     1 
ATOM   1574  C CB    . LYS A 1 1652 ? 231.035 229.460 227.033 1.00 18.40 ? 1652 LYS A CB    1 
ATOM   1575  C CG    . LYS A 1 1652 ? 232.207 228.537 226.753 1.00 17.95 ? 1652 LYS A CG    1 
ATOM   1576  C CD    . LYS A 1 1652 ? 232.847 228.853 225.411 1.00 16.78 ? 1652 LYS A CD    1 
ATOM   1577  C CE    . LYS A 1 1652 ? 233.985 227.894 225.105 1.00 21.41 ? 1652 LYS A CE    1 
ATOM   1578  N NZ    . LYS A 1 1652 ? 234.695 228.249 223.847 1.00 21.86 ? 1652 LYS A NZ    1 
ATOM   1579  N N     . HIS A 1 1653 ? 230.705 227.192 229.634 1.00 21.83 ? 1653 HIS A N     1 
ATOM   1580  C CA    . HIS A 1 1653 ? 230.421 225.797 229.935 1.00 12.81 ? 1653 HIS A CA    1 
ATOM   1581  C C     . HIS A 1 1653 ? 229.698 225.589 231.256 1.00 12.21 ? 1653 HIS A C     1 
ATOM   1582  O O     . HIS A 1 1653 ? 229.159 224.502 231.478 1.00 14.23 ? 1653 HIS A O     1 
ATOM   1583  C CB    . HIS A 1 1653 ? 231.720 224.979 229.953 1.00 11.43 ? 1653 HIS A CB    1 
ATOM   1584  C CG    . HIS A 1 1653 ? 232.370 224.848 228.612 1.00 11.72 ? 1653 HIS A CG    1 
ATOM   1585  N ND1   . HIS A 1 1653 ? 231.700 224.379 227.504 1.00 15.66 ? 1653 HIS A ND1   1 
ATOM   1586  C CD2   . HIS A 1 1653 ? 233.628 225.131 228.201 1.00 18.07 ? 1653 HIS A CD2   1 
ATOM   1587  C CE1   . HIS A 1 1653 ? 232.518 224.375 226.467 1.00 19.73 ? 1653 HIS A CE1   1 
ATOM   1588  N NE2   . HIS A 1 1653 ? 233.694 224.827 226.863 1.00 22.22 ? 1653 HIS A NE2   1 
ATOM   1589  N N     . PHE A 1 1654 ? 229.678 226.593 232.135 1.00 15.93 ? 1654 PHE A N     1 
ATOM   1590  C CA    . PHE A 1 1654 ? 228.985 226.453 233.410 1.00 11.51 ? 1654 PHE A CA    1 
ATOM   1591  C C     . PHE A 1 1654 ? 227.479 226.337 233.234 1.00 8.24  ? 1654 PHE A C     1 
ATOM   1592  O O     . PHE A 1 1654 ? 226.793 225.863 234.145 1.00 9.48  ? 1654 PHE A O     1 
ATOM   1593  C CB    . PHE A 1 1654 ? 229.313 227.638 234.317 1.00 7.36  ? 1654 PHE A CB    1 
ATOM   1594  C CG    . PHE A 1 1654 ? 230.681 227.571 234.926 1.00 6.68  ? 1654 PHE A CG    1 
ATOM   1595  C CD1   . PHE A 1 1654 ? 230.965 226.655 235.921 1.00 10.33 ? 1654 PHE A CD1   1 
ATOM   1596  C CD2   . PHE A 1 1654 ? 231.683 228.425 234.504 1.00 13.57 ? 1654 PHE A CD2   1 
ATOM   1597  C CE1   . PHE A 1 1654 ? 232.225 226.591 236.481 1.00 13.45 ? 1654 PHE A CE1   1 
ATOM   1598  C CE2   . PHE A 1 1654 ? 232.944 228.365 235.060 1.00 14.22 ? 1654 PHE A CE2   1 
ATOM   1599  C CZ    . PHE A 1 1654 ? 233.215 227.447 236.050 1.00 14.78 ? 1654 PHE A CZ    1 
ATOM   1600  N N     . LYS A 1 1655 ? 226.951 226.758 232.083 1.00 12.96 ? 1655 LYS A N     1 
ATOM   1601  C CA    . LYS A 1 1655 ? 225.512 226.701 231.853 1.00 10.11 ? 1655 LYS A CA    1 
ATOM   1602  C C     . LYS A 1 1655 ? 225.005 225.265 231.830 1.00 9.08  ? 1655 LYS A C     1 
ATOM   1603  O O     . LYS A 1 1655 ? 223.917 224.984 232.345 1.00 13.30 ? 1655 LYS A O     1 
ATOM   1604  C CB    . LYS A 1 1655 ? 225.176 227.437 230.550 1.00 9.58  ? 1655 LYS A CB    1 
ATOM   1605  C CG    . LYS A 1 1655 ? 223.722 227.367 230.079 1.00 9.49  ? 1655 LYS A CG    1 
ATOM   1606  C CD    . LYS A 1 1655 ? 223.444 226.157 229.196 1.00 9.18  ? 1655 LYS A CD    1 
ATOM   1607  C CE    . LYS A 1 1655 ? 221.959 225.852 229.127 1.00 6.66  ? 1655 LYS A CE    1 
ATOM   1608  N NZ    . LYS A 1 1655 ? 221.704 224.512 228.532 1.00 10.05 ? 1655 LYS A NZ    1 
ATOM   1609  N N     . LYS A 1 1656 ? 225.768 224.345 231.241 1.00 9.24  ? 1656 LYS A N     1 
ATOM   1610  C CA    . LYS A 1 1656 ? 225.357 222.951 231.158 1.00 8.94  ? 1656 LYS A CA    1 
ATOM   1611  C C     . LYS A 1 1656 ? 225.796 222.118 232.354 1.00 8.36  ? 1656 LYS A C     1 
ATOM   1612  O O     . LYS A 1 1656 ? 225.216 221.054 232.592 1.00 8.93  ? 1656 LYS A O     1 
ATOM   1613  C CB    . LYS A 1 1656 ? 225.906 222.313 229.876 1.00 6.86  ? 1656 LYS A CB    1 
ATOM   1614  C CG    . LYS A 1 1656 ? 227.424 222.279 229.801 1.00 8.62  ? 1656 LYS A CG    1 
ATOM   1615  C CD    . LYS A 1 1656 ? 227.906 222.065 228.376 1.00 7.01  ? 1656 LYS A CD    1 
ATOM   1616  C CE    . LYS A 1 1656 ? 227.520 220.686 227.871 1.00 11.83 ? 1656 LYS A CE    1 
ATOM   1617  N NZ    . LYS A 1 1656 ? 228.039 220.416 226.503 1.00 12.97 ? 1656 LYS A NZ    1 
ATOM   1618  N N     . MET A 1 1657 ? 226.796 222.573 233.105 1.00 7.02  ? 1657 MET A N     1 
ATOM   1619  C CA    . MET A 1 1657 ? 227.292 221.851 234.268 1.00 9.31  ? 1657 MET A CA    1 
ATOM   1620  C C     . MET A 1 1657 ? 226.471 222.106 235.525 1.00 13.36 ? 1657 MET A C     1 
ATOM   1621  O O     . MET A 1 1657 ? 226.587 221.340 236.487 1.00 11.42 ? 1657 MET A O     1 
ATOM   1622  C CB    . MET A 1 1657 ? 228.751 222.233 234.529 1.00 9.35  ? 1657 MET A CB    1 
ATOM   1623  C CG    . MET A 1 1657 ? 229.744 221.497 233.656 1.00 4.73  ? 1657 MET A CG    1 
ATOM   1624  S SD    . MET A 1 1657 ? 231.287 221.146 234.508 1.00 24.25 ? 1657 MET A SD    1 
ATOM   1625  C CE    . MET A 1 1657 ? 231.886 222.804 234.817 1.00 10.12 ? 1657 MET A CE    1 
ATOM   1626  N N     . PHE A 1 1658 ? 225.645 223.150 235.536 1.00 9.93  ? 1658 PHE A N     1 
ATOM   1627  C CA    . PHE A 1 1658 ? 224.848 223.524 236.694 1.00 4.80  ? 1658 PHE A CA    1 
ATOM   1628  C C     . PHE A 1 1658 ? 223.451 223.906 236.223 1.00 9.35  ? 1658 PHE A C     1 
ATOM   1629  O O     . PHE A 1 1658 ? 223.185 224.008 235.022 1.00 5.31  ? 1658 PHE A O     1 
ATOM   1630  C CB    . PHE A 1 1658 ? 225.497 224.681 237.464 1.00 3.26  ? 1658 PHE A CB    1 
ATOM   1631  C CG    . PHE A 1 1658 ? 226.820 224.340 238.087 1.00 2.53  ? 1658 PHE A CG    1 
ATOM   1632  C CD1   . PHE A 1 1658 ? 226.881 223.780 239.350 1.00 8.09  ? 1658 PHE A CD1   1 
ATOM   1633  C CD2   . PHE A 1 1658 ? 228.002 224.584 237.413 1.00 4.01  ? 1658 PHE A CD2   1 
ATOM   1634  C CE1   . PHE A 1 1658 ? 228.094 223.472 239.930 1.00 2.80  ? 1658 PHE A CE1   1 
ATOM   1635  C CE2   . PHE A 1 1658 ? 229.219 224.275 237.987 1.00 4.08  ? 1658 PHE A CE2   1 
ATOM   1636  C CZ    . PHE A 1 1658 ? 229.265 223.718 239.246 1.00 2.13  ? 1658 PHE A CZ    1 
ATOM   1637  N N     . ALA A 1 1659 ? 222.552 224.123 237.179 1.00 8.31  ? 1659 ALA A N     1 
ATOM   1638  C CA    . ALA A 1 1659 ? 221.193 224.586 236.906 1.00 6.13  ? 1659 ALA A CA    1 
ATOM   1639  C C     . ALA A 1 1659 ? 221.066 226.006 237.442 1.00 8.26  ? 1659 ALA A C     1 
ATOM   1640  O O     . ALA A 1 1659 ? 220.675 226.214 238.587 1.00 14.76 ? 1659 ALA A O     1 
ATOM   1641  C CB    . ALA A 1 1659 ? 220.150 223.677 237.543 1.00 1.73  ? 1659 ALA A CB    1 
ATOM   1642  N N     . GLY A 1 1660 ? 221.385 226.986 236.607 1.00 7.52  ? 1660 GLY A N     1 
ATOM   1643  C CA    . GLY A 1 1660 ? 221.256 228.366 237.027 1.00 6.21  ? 1660 GLY A CA    1 
ATOM   1644  C C     . GLY A 1 1660 ? 222.575 229.103 237.080 1.00 7.34  ? 1660 GLY A C     1 
ATOM   1645  O O     . GLY A 1 1660 ? 222.642 230.285 236.732 1.00 16.13 ? 1660 GLY A O     1 
ATOM   1646  N N     . VAL A 1 1661 ? 223.633 228.421 237.512 1.00 2.94  ? 1661 VAL A N     1 
ATOM   1647  C CA    . VAL A 1 1661 ? 224.959 229.026 237.502 1.00 5.38  ? 1661 VAL A CA    1 
ATOM   1648  C C     . VAL A 1 1661 ? 225.417 229.173 236.058 1.00 10.10 ? 1661 VAL A C     1 
ATOM   1649  O O     . VAL A 1 1661 ? 225.403 228.207 235.286 1.00 9.36  ? 1661 VAL A O     1 
ATOM   1650  C CB    . VAL A 1 1661 ? 225.953 228.193 238.320 1.00 1.84  ? 1661 VAL A CB    1 
ATOM   1651  C CG1   . VAL A 1 1661 ? 227.269 228.936 238.463 1.00 2.48  ? 1661 VAL A CG1   1 
ATOM   1652  C CG2   . VAL A 1 1661 ? 225.372 227.873 239.684 1.00 6.80  ? 1661 VAL A CG2   1 
ATOM   1653  N N     . SER A 1 1662 ? 225.809 230.390 235.683 1.00 9.45  ? 1662 SER A N     1 
ATOM   1654  C CA    . SER A 1 1662 ? 226.316 230.670 234.349 1.00 11.32 ? 1662 SER A CA    1 
ATOM   1655  C C     . SER A 1 1662 ? 227.662 231.371 234.342 1.00 13.19 ? 1662 SER A C     1 
ATOM   1656  O O     . SER A 1 1662 ? 228.340 231.351 233.310 1.00 18.08 ? 1662 SER A O     1 
ATOM   1657  C CB    . SER A 1 1662 ? 225.314 231.527 233.561 1.00 7.38  ? 1662 SER A CB    1 
ATOM   1658  O OG    . SER A 1 1662 ? 224.012 230.973 233.624 1.00 11.23 ? 1662 SER A OG    1 
ATOM   1659  N N     . SER A 1 1663 ? 228.069 231.980 235.452 1.00 6.92  ? 1663 SER A N     1 
ATOM   1660  C CA    . SER A 1 1663 ? 229.330 232.698 235.522 1.00 3.87  ? 1663 SER A CA    1 
ATOM   1661  C C     . SER A 1 1663 ? 229.895 232.555 236.925 1.00 7.51  ? 1663 SER A C     1 
ATOM   1662  O O     . SER A 1 1663 ? 229.178 232.227 237.873 1.00 17.97 ? 1663 SER A O     1 
ATOM   1663  C CB    . SER A 1 1663 ? 229.153 234.179 235.167 1.00 7.48  ? 1663 SER A CB    1 
ATOM   1664  O OG    . SER A 1 1663 ? 228.459 234.331 233.942 1.00 8.61  ? 1663 SER A OG    1 
ATOM   1665  N N     . ILE A 1 1664 ? 231.195 232.801 237.049 1.00 6.68  ? 1664 ILE A N     1 
ATOM   1666  C CA    . ILE A 1 1664 ? 231.876 232.814 238.337 1.00 8.27  ? 1664 ILE A CA    1 
ATOM   1667  C C     . ILE A 1 1664 ? 232.461 234.204 238.541 1.00 13.94 ? 1664 ILE A C     1 
ATOM   1668  O O     . ILE A 1 1664 ? 233.145 234.737 237.658 1.00 19.22 ? 1664 ILE A O     1 
ATOM   1669  C CB    . ILE A 1 1664 ? 232.960 231.728 238.424 1.00 7.88  ? 1664 ILE A CB    1 
ATOM   1670  C CG1   . ILE A 1 1664 ? 233.790 231.681 237.140 1.00 15.24 ? 1664 ILE A CG1   1 
ATOM   1671  C CG2   . ILE A 1 1664 ? 232.331 230.374 238.700 1.00 9.87  ? 1664 ILE A CG2   1 
ATOM   1672  C CD1   . ILE A 1 1664 ? 234.892 230.646 237.166 1.00 12.45 ? 1664 ILE A CD1   1 
ATOM   1673  N N     . ILE A 1 1665 ? 232.177 234.799 239.698 1.00 13.00 ? 1665 ILE A N     1 
ATOM   1674  C CA    . ILE A 1 1665 ? 232.669 236.134 240.029 1.00 13.09 ? 1665 ILE A CA    1 
ATOM   1675  C C     . ILE A 1 1665 ? 234.112 235.974 240.499 1.00 14.08 ? 1665 ILE A C     1 
ATOM   1676  O O     . ILE A 1 1665 ? 234.369 235.484 241.598 1.00 12.24 ? 1665 ILE A O     1 
ATOM   1677  C CB    . ILE A 1 1665 ? 231.800 236.821 241.085 1.00 14.63 ? 1665 ILE A CB    1 
ATOM   1678  C CG1   . ILE A 1 1665 ? 230.325 236.802 240.673 1.00 9.66  ? 1665 ILE A CG1   1 
ATOM   1679  C CG2   . ILE A 1 1665 ? 232.267 238.249 241.311 1.00 13.79 ? 1665 ILE A CG2   1 
ATOM   1680  C CD1   . ILE A 1 1665 ? 230.076 237.194 239.229 1.00 10.20 ? 1665 ILE A CD1   1 
ATOM   1681  N N     . LEU A 1 1666 ? 235.058 236.386 239.660 1.00 13.29 ? 1666 LEU A N     1 
ATOM   1682  C CA    . LEU A 1 1666 ? 236.472 236.242 239.955 1.00 18.01 ? 1666 LEU A CA    1 
ATOM   1683  C C     . LEU A 1 1666 ? 237.020 237.515 240.596 1.00 20.21 ? 1666 LEU A C     1 
ATOM   1684  O O     . LEU A 1 1666 ? 236.339 238.537 240.704 1.00 19.70 ? 1666 LEU A O     1 
ATOM   1685  C CB    . LEU A 1 1666 ? 237.242 235.894 238.683 1.00 18.98 ? 1666 LEU A CB    1 
ATOM   1686  C CG    . LEU A 1 1666 ? 236.955 234.525 238.068 1.00 17.19 ? 1666 LEU A CG    1 
ATOM   1687  C CD1   . LEU A 1 1666 ? 237.340 234.510 236.604 1.00 15.96 ? 1666 LEU A CD1   1 
ATOM   1688  C CD2   . LEU A 1 1666 ? 237.706 233.446 238.825 1.00 19.78 ? 1666 LEU A CD2   1 
ATOM   1689  N N     . ASN A 1 1667 ? 238.280 237.453 241.018 1.00 23.07 ? 1667 ASN A N     1 
ATOM   1690  C CA    . ASN A 1 1667 ? 238.948 238.586 241.635 1.00 20.64 ? 1667 ASN A CA    1 
ATOM   1691  C C     . ASN A 1 1667 ? 239.273 239.640 240.580 1.00 25.13 ? 1667 ASN A C     1 
ATOM   1692  O O     . ASN A 1 1667 ? 238.886 239.535 239.413 1.00 25.14 ? 1667 ASN A O     1 
ATOM   1693  C CB    . ASN A 1 1667 ? 240.211 238.121 242.357 1.00 23.32 ? 1667 ASN A CB    1 
ATOM   1694  C CG    . ASN A 1 1667 ? 240.522 238.952 243.583 1.00 29.18 ? 1667 ASN A CG    1 
ATOM   1695  O OD1   . ASN A 1 1667 ? 239.664 239.673 244.094 1.00 31.45 ? 1667 ASN A OD1   1 
ATOM   1696  N ND2   . ASN A 1 1667 ? 241.754 238.852 244.068 1.00 25.41 ? 1667 ASN A ND2   1 
ATOM   1697  N N     . GLU A 1 1668 ? 239.987 240.687 241.002 1.00 33.11 ? 1668 GLU A N     1 
ATOM   1698  C CA    . GLU A 1 1668 ? 240.435 241.700 240.053 1.00 31.38 ? 1668 GLU A CA    1 
ATOM   1699  C C     . GLU A 1 1668 ? 241.398 241.104 239.034 1.00 31.18 ? 1668 GLU A C     1 
ATOM   1700  O O     . GLU A 1 1668 ? 241.347 241.443 237.846 1.00 27.41 ? 1668 GLU A O     1 
ATOM   1701  C CB    . GLU A 1 1668 ? 241.089 242.864 240.797 1.00 29.10 ? 1668 GLU A CB    1 
ATOM   1702  C CG    . GLU A 1 1668 ? 241.430 244.048 239.910 1.00 30.79 ? 1668 GLU A CG    1 
ATOM   1703  C CD    . GLU A 1 1668 ? 240.275 244.449 239.013 1.00 33.13 ? 1668 GLU A CD    1 
ATOM   1704  O OE1   . GLU A 1 1668 ? 239.259 244.949 239.539 1.00 31.92 ? 1668 GLU A OE1   1 
ATOM   1705  O OE2   . GLU A 1 1668 ? 240.383 244.264 237.783 1.00 34.32 ? 1668 GLU A OE2   1 
ATOM   1706  N N     . ASP A 1 1669 ? 242.281 240.213 239.480 1.00 32.31 ? 1669 ASP A N     1 
ATOM   1707  C CA    . ASP A 1 1669 ? 243.216 239.522 238.604 1.00 29.07 ? 1669 ASP A CA    1 
ATOM   1708  C C     . ASP A 1 1669 ? 242.750 238.119 238.234 1.00 28.90 ? 1669 ASP A C     1 
ATOM   1709  O O     . ASP A 1 1669 ? 243.541 237.344 237.686 1.00 31.20 ? 1669 ASP A O     1 
ATOM   1710  C CB    . ASP A 1 1669 ? 244.599 239.454 239.256 1.00 29.46 ? 1669 ASP A CB    1 
ATOM   1711  C CG    . ASP A 1 1669 ? 244.585 238.714 240.576 1.00 31.56 ? 1669 ASP A CG    1 
ATOM   1712  O OD1   . ASP A 1 1669 ? 243.515 238.661 241.218 1.00 33.01 ? 1669 ASP A OD1   1 
ATOM   1713  O OD2   . ASP A 1 1669 ? 245.643 238.183 240.972 1.00 33.53 ? 1669 ASP A OD2   1 
ATOM   1714  N N     . ASN A 1 1670 ? 241.492 237.780 238.527 1.00 26.15 ? 1670 ASN A N     1 
ATOM   1715  C CA    . ASN A 1 1670 ? 240.913 236.475 238.201 1.00 24.44 ? 1670 ASN A CA    1 
ATOM   1716  C C     . ASN A 1 1670 ? 241.713 235.335 238.832 1.00 27.05 ? 1670 ASN A C     1 
ATOM   1717  O O     . ASN A 1 1670 ? 242.055 234.347 238.179 1.00 25.83 ? 1670 ASN A O     1 
ATOM   1718  C CB    . ASN A 1 1670 ? 240.794 236.288 236.687 1.00 23.15 ? 1670 ASN A CB    1 
ATOM   1719  C CG    . ASN A 1 1670 ? 239.693 237.133 236.081 1.00 24.76 ? 1670 ASN A CG    1 
ATOM   1720  O OD1   . ASN A 1 1670 ? 239.232 238.099 236.686 1.00 26.86 ? 1670 ASN A OD1   1 
ATOM   1721  N ND2   . ASN A 1 1670 ? 239.268 236.774 234.876 1.00 21.94 ? 1670 ASN A ND2   1 
ATOM   1722  N N     . SER A 1 1671 ? 242.011 235.480 240.122 1.00 30.82 ? 1671 SER A N     1 
ATOM   1723  C CA    . SER A 1 1671 ? 242.705 234.444 240.878 1.00 26.47 ? 1671 SER A CA    1 
ATOM   1724  C C     . SER A 1 1671 ? 241.918 233.915 242.065 1.00 26.93 ? 1671 SER A C     1 
ATOM   1725  O O     . SER A 1 1671 ? 242.258 232.838 242.569 1.00 28.50 ? 1671 SER A O     1 
ATOM   1726  C CB    . SER A 1 1671 ? 244.062 234.959 241.379 1.00 27.46 ? 1671 SER A CB    1 
ATOM   1727  O OG    . SER A 1 1671 ? 244.901 233.886 241.769 1.00 26.94 ? 1671 SER A OG    1 
ATOM   1728  N N     . VAL A 1 1672 ? 240.894 234.623 242.532 1.00 25.85 ? 1672 VAL A N     1 
ATOM   1729  C CA    . VAL A 1 1672 ? 240.058 234.188 243.644 1.00 22.29 ? 1672 VAL A CA    1 
ATOM   1730  C C     . VAL A 1 1672 ? 238.608 234.230 243.188 1.00 24.66 ? 1672 VAL A C     1 
ATOM   1731  O O     . VAL A 1 1672 ? 238.152 235.247 242.653 1.00 22.05 ? 1672 VAL A O     1 
ATOM   1732  C CB    . VAL A 1 1672 ? 240.260 235.069 244.892 1.00 22.37 ? 1672 VAL A CB    1 
ATOM   1733  C CG1   . VAL A 1 1672 ? 239.413 234.562 246.044 1.00 19.37 ? 1672 VAL A CG1   1 
ATOM   1734  C CG2   . VAL A 1 1672 ? 241.729 235.113 245.282 1.00 26.49 ? 1672 VAL A CG2   1 
ATOM   1735  N N     . VAL A 1 1673 ? 237.886 233.132 243.397 1.00 25.86 ? 1673 VAL A N     1 
ATOM   1736  C CA    . VAL A 1 1673 ? 236.482 233.044 243.007 1.00 17.32 ? 1673 VAL A CA    1 
ATOM   1737  C C     . VAL A 1 1673 ? 235.640 233.623 244.140 1.00 16.61 ? 1673 VAL A C     1 
ATOM   1738  O O     . VAL A 1 1673 ? 235.530 233.027 245.213 1.00 17.50 ? 1673 VAL A O     1 
ATOM   1739  C CB    . VAL A 1 1673 ? 236.075 231.600 242.695 1.00 13.02 ? 1673 VAL A CB    1 
ATOM   1740  C CG1   . VAL A 1 1673 ? 234.590 231.522 242.393 1.00 17.34 ? 1673 VAL A CG1   1 
ATOM   1741  C CG2   . VAL A 1 1673 ? 236.888 231.061 241.534 1.00 15.37 ? 1673 VAL A CG2   1 
ATOM   1742  N N     . LEU A 1 1674 ? 235.043 234.789 243.901 1.00 16.23 ? 1674 LEU A N     1 
ATOM   1743  C CA    . LEU A 1 1674 ? 234.273 235.473 244.931 1.00 14.38 ? 1674 LEU A CA    1 
ATOM   1744  C C     . LEU A 1 1674 ? 232.821 235.025 244.984 1.00 9.49  ? 1674 LEU A C     1 
ATOM   1745  O O     . LEU A 1 1674 ? 232.128 235.320 245.964 1.00 11.17 ? 1674 LEU A O     1 
ATOM   1746  C CB    . LEU A 1 1674 ? 234.324 236.989 244.714 1.00 16.66 ? 1674 LEU A CB    1 
ATOM   1747  C CG    . LEU A 1 1674 ? 235.644 237.610 244.256 1.00 10.83 ? 1674 LEU A CG    1 
ATOM   1748  C CD1   . LEU A 1 1674 ? 235.504 239.116 244.161 1.00 12.53 ? 1674 LEU A CD1   1 
ATOM   1749  C CD2   . LEU A 1 1674 ? 236.770 237.245 245.210 1.00 12.88 ? 1674 LEU A CD2   1 
ATOM   1750  N N     . GLY A 1 1675 ? 232.343 234.329 243.962 1.00 8.09  ? 1675 GLY A N     1 
ATOM   1751  C CA    . GLY A 1 1675 ? 230.957 233.908 243.952 1.00 8.60  ? 1675 GLY A CA    1 
ATOM   1752  C C     . GLY A 1 1675 ? 230.558 233.381 242.593 1.00 6.57  ? 1675 GLY A C     1 
ATOM   1753  O O     . GLY A 1 1675 ? 231.402 233.029 241.768 1.00 15.11 ? 1675 GLY A O     1 
ATOM   1754  N N     . ILE A 1 1676 ? 229.246 233.326 242.376 1.00 1.64  ? 1676 ILE A N     1 
ATOM   1755  C CA    . ILE A 1 1676 ? 228.684 232.843 241.121 1.00 2.69  ? 1676 ILE A CA    1 
ATOM   1756  C C     . ILE A 1 1676 ? 227.601 233.803 240.653 1.00 4.38  ? 1676 ILE A C     1 
ATOM   1757  O O     . ILE A 1 1676 ? 227.196 234.708 241.391 1.00 12.82 ? 1676 ILE A O     1 
ATOM   1758  C CB    . ILE A 1 1676 ? 228.126 231.417 241.272 1.00 7.48  ? 1676 ILE A CB    1 
ATOM   1759  C CG1   . ILE A 1 1676 ? 227.220 231.333 242.500 1.00 8.08  ? 1676 ILE A CG1   1 
ATOM   1760  C CG2   . ILE A 1 1676 ? 229.256 230.407 241.362 1.00 12.08 ? 1676 ILE A CG2   1 
ATOM   1761  C CD1   . ILE A 1 1676 ? 226.404 230.072 242.570 1.00 4.81  ? 1676 ILE A CD1   1 
ATOM   1762  N N     . SER A 1 1677 ? 227.120 233.611 239.429 1.00 0.00  ? 1677 SER A N     1 
ATOM   1763  C CA    . SER A 1 1677 ? 226.088 234.465 238.861 1.00 1.70  ? 1677 SER A CA    1 
ATOM   1764  C C     . SER A 1 1677 ? 225.092 233.583 238.120 1.00 3.73  ? 1677 SER A C     1 
ATOM   1765  O O     . SER A 1 1677 ? 225.151 232.353 238.195 1.00 8.86  ? 1677 SER A O     1 
ATOM   1766  C CB    . SER A 1 1677 ? 226.705 235.534 237.951 1.00 7.56  ? 1677 SER A CB    1 
ATOM   1767  O OG    . SER A 1 1677 ? 225.729 236.472 237.536 1.00 11.66 ? 1677 SER A OG    1 
ATOM   1768  N N     . SER A 1 1678 ? 224.175 234.215 237.394 1.00 6.59  ? 1678 SER A N     1 
ATOM   1769  C CA    . SER A 1 1678 ? 223.132 233.494 236.684 1.00 5.14  ? 1678 SER A CA    1 
ATOM   1770  C C     . SER A 1 1678 ? 222.878 234.183 235.350 1.00 8.05  ? 1678 SER A C     1 
ATOM   1771  O O     . SER A 1 1678 ? 223.561 235.144 234.983 1.00 13.88 ? 1678 SER A O     1 
ATOM   1772  C CB    . SER A 1 1678 ? 221.854 233.411 237.523 1.00 9.40  ? 1678 SER A CB    1 
ATOM   1773  O OG    . SER A 1 1678 ? 220.984 232.409 237.031 1.00 12.75 ? 1678 SER A OG    1 
ATOM   1774  N N     . ARG A 1 1679 ? 221.884 233.674 234.619 1.00 5.02  ? 1679 ARG A N     1 
ATOM   1775  C CA    . ARG A 1 1679 ? 221.519 234.271 233.338 1.00 9.52  ? 1679 ARG A CA    1 
ATOM   1776  C C     . ARG A 1 1679 ? 220.997 235.691 233.518 1.00 10.52 ? 1679 ARG A C     1 
ATOM   1777  O O     . ARG A 1 1679 ? 221.366 236.601 232.767 1.00 11.52 ? 1679 ARG A O     1 
ATOM   1778  C CB    . ARG A 1 1679 ? 220.475 233.403 232.637 1.00 8.42  ? 1679 ARG A CB    1 
ATOM   1779  C CG    . ARG A 1 1679 ? 220.098 233.899 231.252 1.00 11.47 ? 1679 ARG A CG    1 
ATOM   1780  C CD    . ARG A 1 1679 ? 218.649 233.553 230.927 1.00 13.27 ? 1679 ARG A CD    1 
ATOM   1781  N NE    . ARG A 1 1679 ? 217.712 234.602 231.325 1.00 16.98 ? 1679 ARG A NE    1 
ATOM   1782  C CZ    . ARG A 1 1679 ? 217.715 235.849 230.870 1.00 13.91 ? 1679 ARG A CZ    1 
ATOM   1783  N NH1   . ARG A 1 1679 ? 218.561 236.245 229.933 1.00 12.14 ? 1679 ARG A NH1   1 
ATOM   1784  N NH2   . ARG A 1 1679 ? 216.837 236.719 231.360 1.00 11.65 ? 1679 ARG A NH2   1 
ATOM   1785  N N     . GLU A 1 1680 ? 220.127 235.897 234.508 1.00 6.46  ? 1680 GLU A N     1 
ATOM   1786  C CA    . GLU A 1 1680 ? 219.557 237.222 234.731 1.00 7.09  ? 1680 GLU A CA    1 
ATOM   1787  C C     . GLU A 1 1680 ? 220.618 238.203 235.209 1.00 10.98 ? 1680 GLU A C     1 
ATOM   1788  O O     . GLU A 1 1680 ? 220.588 239.385 234.849 1.00 16.14 ? 1680 GLU A O     1 
ATOM   1789  C CB    . GLU A 1 1680 ? 218.406 237.159 235.740 1.00 10.63 ? 1680 GLU A CB    1 
ATOM   1790  C CG    . GLU A 1 1680 ? 217.331 236.095 235.490 1.00 12.38 ? 1680 GLU A CG    1 
ATOM   1791  C CD    . GLU A 1 1680 ? 217.831 234.674 235.656 1.00 11.08 ? 1680 GLU A CD    1 
ATOM   1792  O OE1   . GLU A 1 1680 ? 217.297 233.769 234.982 1.00 11.18 ? 1680 GLU A OE1   1 
ATOM   1793  O OE2   . GLU A 1 1680 ? 218.764 234.465 236.459 1.00 11.24 ? 1680 GLU A OE2   1 
ATOM   1794  N N     . GLY A 1 1681 ? 221.555 237.734 236.025 1.00 10.87 ? 1681 GLY A N     1 
ATOM   1795  C CA    . GLY A 1 1681 ? 222.582 238.598 236.565 1.00 8.93  ? 1681 GLY A CA    1 
ATOM   1796  C C     . GLY A 1 1681 ? 222.594 238.590 238.077 1.00 10.81 ? 1681 GLY A C     1 
ATOM   1797  O O     . GLY A 1 1681 ? 223.277 239.403 238.703 1.00 15.21 ? 1681 GLY A O     1 
ATOM   1798  N N     . GLU A 1 1682 ? 221.827 237.682 238.673 1.00 4.86  ? 1682 GLU A N     1 
ATOM   1799  C CA    . GLU A 1 1682 ? 221.784 237.582 240.124 1.00 6.92  ? 1682 GLU A CA    1 
ATOM   1800  C C     . GLU A 1 1682 ? 223.082 236.983 240.646 1.00 4.70  ? 1682 GLU A C     1 
ATOM   1801  O O     . GLU A 1 1682 ? 223.507 235.912 240.205 1.00 11.06 ? 1682 GLU A O     1 
ATOM   1802  C CB    . GLU A 1 1682 ? 220.590 236.731 240.554 1.00 7.37  ? 1682 GLU A CB    1 
ATOM   1803  C CG    . GLU A 1 1682 ? 220.173 236.928 241.998 1.00 6.43  ? 1682 GLU A CG    1 
ATOM   1804  C CD    . GLU A 1 1682 ? 219.010 236.043 242.389 1.00 6.68  ? 1682 GLU A CD    1 
ATOM   1805  O OE1   . GLU A 1 1682 ? 219.013 234.856 242.007 1.00 2.03  ? 1682 GLU A OE1   1 
ATOM   1806  O OE2   . GLU A 1 1682 ? 218.089 236.537 243.071 1.00 9.62  ? 1682 GLU A OE2   1 
ATOM   1807  N N     . GLU A 1 1683 ? 223.711 237.673 241.591 1.00 0.57  ? 1683 GLU A N     1 
ATOM   1808  C CA    . GLU A 1 1683 ? 224.997 237.266 242.135 1.00 4.44  ? 1683 GLU A CA    1 
ATOM   1809  C C     . GLU A 1 1683 ? 224.800 236.521 243.446 1.00 4.73  ? 1683 GLU A C     1 
ATOM   1810  O O     . GLU A 1 1683 ? 223.822 236.752 244.162 1.00 12.72 ? 1683 GLU A O     1 
ATOM   1811  C CB    . GLU A 1 1683 ? 225.915 238.470 242.373 1.00 8.64  ? 1683 GLU A CB    1 
ATOM   1812  C CG    . GLU A 1 1683 ? 226.385 239.192 241.122 1.00 10.64 ? 1683 GLU A CG    1 
ATOM   1813  C CD    . GLU A 1 1683 ? 225.372 240.192 240.610 1.00 11.31 ? 1683 GLU A CD    1 
ATOM   1814  O OE1   . GLU A 1 1683 ? 224.325 240.369 241.268 1.00 13.53 ? 1683 GLU A OE1   1 
ATOM   1815  O OE2   . GLU A 1 1683 ? 225.623 240.805 239.552 1.00 8.48  ? 1683 GLU A OE2   1 
ATOM   1816  N N     . VAL A 1 1684 ? 225.729 235.619 243.746 1.00 0.85  ? 1684 VAL A N     1 
ATOM   1817  C CA    . VAL A 1 1684 ? 225.790 234.931 245.031 1.00 2.89  ? 1684 VAL A CA    1 
ATOM   1818  C C     . VAL A 1 1684 ? 227.228 235.047 245.517 1.00 0.33  ? 1684 VAL A C     1 
ATOM   1819  O O     . VAL A 1 1684 ? 228.069 234.202 245.193 1.00 8.68  ? 1684 VAL A O     1 
ATOM   1820  C CB    . VAL A 1 1684 ? 225.352 233.465 244.931 1.00 3.90  ? 1684 VAL A CB    1 
ATOM   1821  C CG1   . VAL A 1 1684 ? 225.384 232.805 246.300 1.00 4.54  ? 1684 VAL A CG1   1 
ATOM   1822  C CG2   . VAL A 1 1684 ? 223.963 233.360 244.322 1.00 0.43  ? 1684 VAL A CG2   1 
ATOM   1823  N N     . MET A 1 1685 ? 227.522 236.091 246.290 1.00 0.00  ? 1685 MET A N     1 
ATOM   1824  C CA    . MET A 1 1685 ? 228.854 236.235 246.864 1.00 3.11  ? 1685 MET A CA    1 
ATOM   1825  C C     . MET A 1 1685 ? 229.138 235.114 247.851 1.00 3.20  ? 1685 MET A C     1 
ATOM   1826  O O     . MET A 1 1685 ? 228.322 234.819 248.728 1.00 6.49  ? 1685 MET A O     1 
ATOM   1827  C CB    . MET A 1 1685 ? 228.998 237.592 247.554 1.00 11.10 ? 1685 MET A CB    1 
ATOM   1828  C CG    . MET A 1 1685 ? 229.261 238.762 246.621 1.00 9.78  ? 1685 MET A CG    1 
ATOM   1829  S SD    . MET A 1 1685 ? 230.289 238.320 245.207 1.00 18.67 ? 1685 MET A SD    1 
ATOM   1830  C CE    . MET A 1 1685 ? 229.093 238.347 243.882 1.00 8.96  ? 1685 MET A CE    1 
ATOM   1831  N N     . PHE A 1 1686 ? 230.304 234.497 247.705 1.00 6.39  ? 1686 PHE A N     1 
ATOM   1832  C CA    . PHE A 1 1686 ? 230.696 233.418 248.596 1.00 5.58  ? 1686 PHE A CA    1 
ATOM   1833  C C     . PHE A 1 1686 ? 230.993 233.977 249.980 1.00 6.14  ? 1686 PHE A C     1 
ATOM   1834  O O     . PHE A 1 1686 ? 231.591 235.047 250.117 1.00 10.43 ? 1686 PHE A O     1 
ATOM   1835  C CB    . PHE A 1 1686 ? 231.933 232.704 248.054 1.00 10.11 ? 1686 PHE A CB    1 
ATOM   1836  C CG    . PHE A 1 1686 ? 231.638 231.727 246.958 1.00 7.74  ? 1686 PHE A CG    1 
ATOM   1837  C CD1   . PHE A 1 1686 ? 230.413 231.092 246.884 1.00 6.41  ? 1686 PHE A CD1   1 
ATOM   1838  C CD2   . PHE A 1 1686 ? 232.594 231.438 246.002 1.00 9.67  ? 1686 PHE A CD2   1 
ATOM   1839  C CE1   . PHE A 1 1686 ? 230.145 230.200 245.869 1.00 5.91  ? 1686 PHE A CE1   1 
ATOM   1840  C CE2   . PHE A 1 1686 ? 232.331 230.541 244.990 1.00 6.74  ? 1686 PHE A CE2   1 
ATOM   1841  C CZ    . PHE A 1 1686 ? 231.107 229.922 244.923 1.00 5.79  ? 1686 PHE A CZ    1 
ATOM   1842  N N     . LYS A 1 1687 ? 230.563 233.253 251.014 1.00 6.29  ? 1687 LYS A N     1 
ATOM   1843  C CA    . LYS A 1 1687 ? 230.917 233.656 252.370 1.00 12.01 ? 1687 LYS A CA    1 
ATOM   1844  C C     . LYS A 1 1687 ? 232.421 233.559 252.589 1.00 13.54 ? 1687 LYS A C     1 
ATOM   1845  O O     . LYS A 1 1687 ? 233.021 234.435 253.223 1.00 8.54  ? 1687 LYS A O     1 
ATOM   1846  C CB    . LYS A 1 1687 ? 230.161 232.805 253.388 1.00 10.81 ? 1687 LYS A CB    1 
ATOM   1847  C CG    . LYS A 1 1687 ? 228.672 232.710 253.115 1.00 7.60  ? 1687 LYS A CG    1 
ATOM   1848  C CD    . LYS A 1 1687 ? 228.031 234.087 253.097 1.00 8.71  ? 1687 LYS A CD    1 
ATOM   1849  C CE    . LYS A 1 1687 ? 227.920 234.666 254.492 1.00 9.17  ? 1687 LYS A CE    1 
ATOM   1850  N NZ    . LYS A 1 1687 ? 227.061 233.828 255.368 1.00 5.88  ? 1687 LYS A NZ    1 
ATOM   1851  N N     . THR A 1 1688 ? 233.043 232.506 252.073 1.00 12.36 ? 1688 THR A N     1 
ATOM   1852  C CA    . THR A 1 1688 ? 234.497 232.358 252.096 1.00 14.38 ? 1688 THR A CA    1 
ATOM   1853  C C     . THR A 1 1688 ? 234.991 232.133 250.675 1.00 13.71 ? 1688 THR A C     1 
ATOM   1854  O O     . THR A 1 1688 ? 234.863 231.011 250.150 1.00 8.33  ? 1688 THR A O     1 
ATOM   1855  C CB    . THR A 1 1688 ? 234.918 231.199 252.999 1.00 13.50 ? 1688 THR A CB    1 
ATOM   1856  O OG1   . THR A 1 1688 ? 234.463 231.443 254.335 1.00 18.40 ? 1688 THR A OG1   1 
ATOM   1857  C CG2   . THR A 1 1688 ? 236.433 231.056 253.009 1.00 15.48 ? 1688 THR A CG2   1 
ATOM   1858  N N     . PRO A 1 1689 ? 235.539 233.146 250.008 1.00 17.59 ? 1689 PRO A N     1 
ATOM   1859  C CA    . PRO A 1 1689 ? 236.020 232.952 248.637 1.00 16.80 ? 1689 PRO A CA    1 
ATOM   1860  C C     . PRO A 1 1689 ? 237.158 231.946 248.573 1.00 19.99 ? 1689 PRO A C     1 
ATOM   1861  O O     . PRO A 1 1689 ? 237.944 231.795 249.511 1.00 22.20 ? 1689 PRO A O     1 
ATOM   1862  C CB    . PRO A 1 1689 ? 236.493 234.350 248.227 1.00 16.74 ? 1689 PRO A CB    1 
ATOM   1863  C CG    . PRO A 1 1689 ? 235.723 235.277 249.099 1.00 19.32 ? 1689 PRO A CG    1 
ATOM   1864  C CD    . PRO A 1 1689 ? 235.576 234.562 250.409 1.00 17.11 ? 1689 PRO A CD    1 
ATOM   1865  N N     . VAL A 1 1690 ? 237.240 231.255 247.439 1.00 18.97 ? 1690 VAL A N     1 
ATOM   1866  C CA    . VAL A 1 1690 ? 238.253 230.234 247.199 1.00 21.25 ? 1690 VAL A CA    1 
ATOM   1867  C C     . VAL A 1 1690 ? 239.287 230.791 246.231 1.00 24.70 ? 1690 VAL A C     1 
ATOM   1868  O O     . VAL A 1 1690 ? 238.937 231.459 245.250 1.00 22.12 ? 1690 VAL A O     1 
ATOM   1869  C CB    . VAL A 1 1690 ? 237.630 228.928 246.673 1.00 22.04 ? 1690 VAL A CB    1 
ATOM   1870  C CG1   . VAL A 1 1690 ? 236.993 229.127 245.307 1.00 17.72 ? 1690 VAL A CG1   1 
ATOM   1871  C CG2   . VAL A 1 1690 ? 238.682 227.838 246.610 1.00 22.67 ? 1690 VAL A CG2   1 
ATOM   1872  N N     . SER A 1 1691 ? 240.559 230.539 246.522 1.00 27.56 ? 1691 SER A N     1 
ATOM   1873  C CA    . SER A 1 1691 ? 241.665 231.054 245.728 1.00 26.74 ? 1691 SER A CA    1 
ATOM   1874  C C     . SER A 1 1691 ? 242.180 229.954 244.810 1.00 26.20 ? 1691 SER A C     1 
ATOM   1875  O O     . SER A 1 1691 ? 242.584 228.885 245.280 1.00 29.63 ? 1691 SER A O     1 
ATOM   1876  C CB    . SER A 1 1691 ? 242.789 231.570 246.627 1.00 25.19 ? 1691 SER A CB    1 
ATOM   1877  O OG    . SER A 1 1691 ? 243.110 230.624 247.631 1.00 29.60 ? 1691 SER A OG    1 
ATOM   1878  N N     . ILE A 1 1692 ? 242.163 230.219 243.502 1.00 24.17 ? 1692 ILE A N     1 
ATOM   1879  C CA    . ILE A 1 1692 ? 242.729 229.273 242.547 1.00 20.59 ? 1692 ILE A CA    1 
ATOM   1880  C C     . ILE A 1 1692 ? 244.245 229.218 242.684 1.00 27.96 ? 1692 ILE A C     1 
ATOM   1881  O O     . ILE A 1 1692 ? 244.878 228.239 242.270 1.00 30.44 ? 1692 ILE A O     1 
ATOM   1882  C CB    . ILE A 1 1692 ? 242.296 229.646 241.117 1.00 21.02 ? 1692 ILE A CB    1 
ATOM   1883  C CG1   . ILE A 1 1692 ? 240.800 229.968 241.085 1.00 24.88 ? 1692 ILE A CG1   1 
ATOM   1884  C CG2   . ILE A 1 1692 ? 242.614 228.526 240.145 1.00 20.39 ? 1692 ILE A CG2   1 
ATOM   1885  C CD1   . ILE A 1 1692 ? 240.296 230.416 239.730 1.00 21.37 ? 1692 ILE A CD1   1 
ATOM   1886  N N     . THR A 1 1693 ? 244.853 230.255 243.265 1.00 27.78 ? 1693 THR A N     1 
ATOM   1887  C CA    . THR A 1 1693 ? 246.301 230.262 243.448 1.00 26.17 ? 1693 THR A CA    1 
ATOM   1888  C C     . THR A 1 1693 ? 246.758 229.132 244.363 1.00 26.63 ? 1693 THR A C     1 
ATOM   1889  O O     . THR A 1 1693 ? 247.751 228.459 244.064 1.00 27.32 ? 1693 THR A O     1 
ATOM   1890  C CB    . THR A 1 1693 ? 246.752 231.612 244.007 1.00 27.62 ? 1693 THR A CB    1 
ATOM   1891  O OG1   . THR A 1 1693 ? 246.485 232.642 243.047 1.00 27.55 ? 1693 THR A OG1   1 
ATOM   1892  C CG2   . THR A 1 1693 ? 248.241 231.596 244.320 1.00 26.88 ? 1693 THR A CG2   1 
ATOM   1893  N N     . GLU A 1 1694 ? 246.049 228.903 245.467 1.00 28.88 ? 1694 GLU A N     1 
ATOM   1894  C CA    . GLU A 1 1694 ? 246.394 227.838 246.398 1.00 29.55 ? 1694 GLU A CA    1 
ATOM   1895  C C     . GLU A 1 1694 ? 245.906 226.468 245.948 1.00 29.76 ? 1694 GLU A C     1 
ATOM   1896  O O     . GLU A 1 1694 ? 246.367 225.456 246.486 1.00 29.42 ? 1694 GLU A O     1 
ATOM   1897  C CB    . GLU A 1 1694 ? 245.829 228.150 247.788 1.00 28.35 ? 1694 GLU A CB    1 
ATOM   1898  C CG    . GLU A 1 1694 ? 246.324 229.462 248.377 1.00 31.05 ? 1694 GLU A CG    1 
ATOM   1899  C CD    . GLU A 1 1694 ? 247.818 229.462 248.642 1.00 33.95 ? 1694 GLU A CD    1 
ATOM   1900  O OE1   . GLU A 1 1694 ? 248.436 230.545 248.563 1.00 33.84 ? 1694 GLU A OE1   1 
ATOM   1901  O OE2   . GLU A 1 1694 ? 248.374 228.382 248.933 1.00 31.57 ? 1694 GLU A OE2   1 
ATOM   1902  N N     . HIS A 1 1695 ? 244.992 226.410 244.980 1.00 26.02 ? 1695 HIS A N     1 
ATOM   1903  C CA    . HIS A 1 1695 ? 244.504 225.155 244.406 1.00 27.21 ? 1695 HIS A CA    1 
ATOM   1904  C C     . HIS A 1 1695 ? 244.620 225.263 242.893 1.00 28.62 ? 1695 HIS A C     1 
ATOM   1905  O O     . HIS A 1 1695 ? 243.621 225.492 242.196 1.00 31.89 ? 1695 HIS A O     1 
ATOM   1906  C CB    . HIS A 1 1695 ? 243.066 224.866 244.835 1.00 24.74 ? 1695 HIS A CB    1 
ATOM   1907  C CG    . HIS A 1 1695 ? 242.814 225.087 246.294 1.00 27.19 ? 1695 HIS A CG    1 
ATOM   1908  N ND1   . HIS A 1 1695 ? 243.166 224.167 247.258 1.00 27.51 ? 1695 HIS A ND1   1 
ATOM   1909  C CD2   . HIS A 1 1695 ? 242.243 226.122 246.953 1.00 26.57 ? 1695 HIS A CD2   1 
ATOM   1910  C CE1   . HIS A 1 1695 ? 242.823 224.627 248.448 1.00 27.70 ? 1695 HIS A CE1   1 
ATOM   1911  N NE2   . HIS A 1 1695 ? 242.261 225.812 248.291 1.00 30.16 ? 1695 HIS A NE2   1 
ATOM   1912  N N     . PRO A 1 1696 ? 245.831 225.118 242.349 1.00 27.41 ? 1696 PRO A N     1 
ATOM   1913  C CA    . PRO A 1 1696 ? 246.014 225.325 240.903 1.00 22.66 ? 1696 PRO A CA    1 
ATOM   1914  C C     . PRO A 1 1696 ? 245.208 224.376 240.034 1.00 23.95 ? 1696 PRO A C     1 
ATOM   1915  O O     . PRO A 1 1696 ? 244.757 224.780 238.955 1.00 26.31 ? 1696 PRO A O     1 
ATOM   1916  C CB    . PRO A 1 1696 ? 247.524 225.120 240.712 1.00 26.21 ? 1696 PRO A CB    1 
ATOM   1917  C CG    . PRO A 1 1696 ? 247.944 224.283 241.874 1.00 28.40 ? 1696 PRO A CG    1 
ATOM   1918  C CD    . PRO A 1 1696 ? 247.084 224.728 243.016 1.00 26.55 ? 1696 PRO A CD    1 
ATOM   1919  N N     . LYS A 1 1697 ? 245.013 223.132 240.462 1.00 23.10 ? 1697 LYS A N     1 
ATOM   1920  C CA    . LYS A 1 1697 ? 244.312 222.162 239.632 1.00 20.18 ? 1697 LYS A CA    1 
ATOM   1921  C C     . LYS A 1 1697 ? 242.842 222.545 239.504 1.00 14.15 ? 1697 LYS A C     1 
ATOM   1922  O O     . LYS A 1 1697 ? 242.207 222.966 240.474 1.00 16.75 ? 1697 LYS A O     1 
ATOM   1923  C CB    . LYS A 1 1697 ? 244.451 220.759 240.221 1.00 21.55 ? 1697 LYS A CB    1 
ATOM   1924  C CG    . LYS A 1 1697 ? 243.880 219.654 239.350 1.00 22.01 ? 1697 LYS A CG    1 
ATOM   1925  C CD    . LYS A 1 1697 ? 244.247 219.853 237.888 1.00 20.68 ? 1697 LYS A CD    1 
ATOM   1926  C CE    . LYS A 1 1697 ? 244.329 218.529 237.151 1.00 20.82 ? 1697 LYS A CE    1 
ATOM   1927  N NZ    . LYS A 1 1697 ? 243.813 218.647 235.760 1.00 21.85 ? 1697 LYS A NZ    1 
ATOM   1928  N N     . ILE A 1 1698 ? 242.302 222.400 238.292 1.00 15.83 ? 1698 ILE A N     1 
ATOM   1929  C CA    . ILE A 1 1698 ? 240.981 222.947 238.001 1.00 15.52 ? 1698 ILE A CA    1 
ATOM   1930  C C     . ILE A 1 1698 ? 239.890 222.165 238.724 1.00 18.05 ? 1698 ILE A C     1 
ATOM   1931  O O     . ILE A 1 1698 ? 238.921 222.749 239.224 1.00 20.33 ? 1698 ILE A O     1 
ATOM   1932  C CB    . ILE A 1 1698 ? 240.741 222.996 236.482 1.00 14.08 ? 1698 ILE A CB    1 
ATOM   1933  C CG1   . ILE A 1 1698 ? 239.319 223.472 236.189 1.00 12.94 ? 1698 ILE A CG1   1 
ATOM   1934  C CG2   . ILE A 1 1698 ? 241.002 221.639 235.846 1.00 17.07 ? 1698 ILE A CG2   1 
ATOM   1935  C CD1   . ILE A 1 1698 ? 239.122 223.937 234.784 1.00 13.95 ? 1698 ILE A CD1   1 
ATOM   1936  N N     . ASN A 1 1699 ? 240.021 220.839 238.792 1.00 17.53 ? 1699 ASN A N     1 
ATOM   1937  C CA    . ASN A 1 1699 ? 239.001 220.037 239.459 1.00 14.66 ? 1699 ASN A CA    1 
ATOM   1938  C C     . ASN A 1 1699 ? 238.913 220.379 240.942 1.00 16.16 ? 1699 ASN A C     1 
ATOM   1939  O O     . ASN A 1 1699 ? 237.817 220.414 241.514 1.00 16.89 ? 1699 ASN A O     1 
ATOM   1940  C CB    . ASN A 1 1699 ? 239.279 218.547 239.243 1.00 11.75 ? 1699 ASN A CB    1 
ATOM   1941  C CG    . ASN A 1 1699 ? 240.294 217.983 240.222 1.00 18.27 ? 1699 ASN A CG    1 
ATOM   1942  O OD1   . ASN A 1 1699 ? 241.225 218.670 240.636 1.00 20.70 ? 1699 ASN A OD1   1 
ATOM   1943  N ND2   . ASN A 1 1699 ? 240.120 216.724 240.593 1.00 18.17 ? 1699 ASN A ND2   1 
ATOM   1944  N N     . GLU A 1 1700 ? 240.056 220.659 241.575 1.00 13.61 ? 1700 GLU A N     1 
ATOM   1945  C CA    . GLU A 1 1700 ? 240.059 220.981 242.998 1.00 14.97 ? 1700 GLU A CA    1 
ATOM   1946  C C     . GLU A 1 1700 ? 239.262 222.248 243.279 1.00 16.10 ? 1700 GLU A C     1 
ATOM   1947  O O     . GLU A 1 1700 ? 238.352 222.251 244.118 1.00 18.66 ? 1700 GLU A O     1 
ATOM   1948  C CB    . GLU A 1 1700 ? 241.495 221.134 243.499 1.00 17.54 ? 1700 GLU A CB    1 
ATOM   1949  C CG    . GLU A 1 1700 ? 242.360 219.902 243.313 1.00 15.95 ? 1700 GLU A CG    1 
ATOM   1950  C CD    . GLU A 1 1700 ? 243.592 219.919 244.195 1.00 19.11 ? 1700 GLU A CD    1 
ATOM   1951  O OE1   . GLU A 1 1700 ? 244.457 219.034 244.028 1.00 21.65 ? 1700 GLU A OE1   1 
ATOM   1952  O OE2   . GLU A 1 1700 ? 243.697 220.818 245.056 1.00 19.66 ? 1700 GLU A OE2   1 
ATOM   1953  N N     . TRP A 1 1701 ? 239.576 223.336 242.573 1.00 13.73 ? 1701 TRP A N     1 
ATOM   1954  C CA    . TRP A 1 1701 ? 238.871 224.577 242.857 1.00 11.91 ? 1701 TRP A CA    1 
ATOM   1955  C C     . TRP A 1 1701 ? 237.453 224.564 242.309 1.00 8.54  ? 1701 TRP A C     1 
ATOM   1956  O O     . TRP A 1 1701 ? 236.607 225.282 242.834 1.00 15.26 ? 1701 TRP A O     1 
ATOM   1957  C CB    . TRP A 1 1701 ? 239.650 225.791 242.334 1.00 12.21 ? 1701 TRP A CB    1 
ATOM   1958  C CG    . TRP A 1 1701 ? 239.674 225.991 240.848 1.00 14.42 ? 1701 TRP A CG    1 
ATOM   1959  C CD1   . TRP A 1 1701 ? 240.688 225.667 239.999 1.00 16.99 ? 1701 TRP A CD1   1 
ATOM   1960  C CD2   . TRP A 1 1701 ? 238.665 226.619 240.044 1.00 13.58 ? 1701 TRP A CD2   1 
ATOM   1961  N NE1   . TRP A 1 1701 ? 240.364 226.025 238.714 1.00 17.46 ? 1701 TRP A NE1   1 
ATOM   1962  C CE2   . TRP A 1 1701 ? 239.127 226.612 238.715 1.00 16.56 ? 1701 TRP A CE2   1 
ATOM   1963  C CE3   . TRP A 1 1701 ? 237.412 227.171 240.318 1.00 12.26 ? 1701 TRP A CE3   1 
ATOM   1964  C CZ2   . TRP A 1 1701 ? 238.380 227.134 237.664 1.00 10.91 ? 1701 TRP A CZ2   1 
ATOM   1965  C CZ3   . TRP A 1 1701 ? 236.674 227.688 239.273 1.00 12.88 ? 1701 TRP A CZ3   1 
ATOM   1966  C CH2   . TRP A 1 1701 ? 237.160 227.667 237.963 1.00 10.10 ? 1701 TRP A CH2   1 
ATOM   1967  N N     . LEU A 1 1702 ? 237.155 223.740 241.303 1.00 4.61  ? 1702 LEU A N     1 
ATOM   1968  C CA    . LEU A 1 1702 ? 235.764 223.598 240.880 1.00 10.17 ? 1702 LEU A CA    1 
ATOM   1969  C C     . LEU A 1 1702 ? 234.931 222.888 241.943 1.00 12.98 ? 1702 LEU A C     1 
ATOM   1970  O O     . LEU A 1 1702 ? 233.798 223.298 242.236 1.00 13.69 ? 1702 LEU A O     1 
ATOM   1971  C CB    . LEU A 1 1702 ? 235.693 222.855 239.548 1.00 8.21  ? 1702 LEU A CB    1 
ATOM   1972  C CG    . LEU A 1 1702 ? 235.697 223.750 238.312 1.00 7.64  ? 1702 LEU A CG    1 
ATOM   1973  C CD1   . LEU A 1 1702 ? 235.522 222.926 237.054 1.00 8.75  ? 1702 LEU A CD1   1 
ATOM   1974  C CD2   . LEU A 1 1702 ? 234.606 224.799 238.418 1.00 9.73  ? 1702 LEU A CD2   1 
ATOM   1975  N N     . THR A 1 1703 ? 235.479 221.826 242.539 1.00 6.58  ? 1703 THR A N     1 
ATOM   1976  C CA    . THR A 1 1703 ? 234.807 221.178 243.657 1.00 3.13  ? 1703 THR A CA    1 
ATOM   1977  C C     . THR A 1 1703 ? 234.647 222.141 244.826 1.00 10.05 ? 1703 THR A C     1 
ATOM   1978  O O     . THR A 1 1703 ? 233.601 222.162 245.486 1.00 10.30 ? 1703 THR A O     1 
ATOM   1979  C CB    . THR A 1 1703 ? 235.588 219.936 244.088 1.00 7.49  ? 1703 THR A CB    1 
ATOM   1980  O OG1   . THR A 1 1703 ? 235.800 219.088 242.953 1.00 15.21 ? 1703 THR A OG1   1 
ATOM   1981  C CG2   . THR A 1 1703 ? 234.823 219.165 245.149 1.00 11.32 ? 1703 THR A CG2   1 
ATOM   1982  N N     . LEU A 1 1704 ? 235.677 222.946 245.094 1.00 11.17 ? 1704 LEU A N     1 
ATOM   1983  C CA    . LEU A 1 1704 ? 235.586 223.927 246.171 1.00 4.73  ? 1704 LEU A CA    1 
ATOM   1984  C C     . LEU A 1 1704 ? 234.535 224.989 245.870 1.00 5.28  ? 1704 LEU A C     1 
ATOM   1985  O O     . LEU A 1 1704 ? 233.836 225.447 246.778 1.00 9.11  ? 1704 LEU A O     1 
ATOM   1986  C CB    . LEU A 1 1704 ? 236.952 224.566 246.416 1.00 6.08  ? 1704 LEU A CB    1 
ATOM   1987  C CG    . LEU A 1 1704 ? 237.967 223.637 247.083 1.00 10.99 ? 1704 LEU A CG    1 
ATOM   1988  C CD1   . LEU A 1 1704 ? 239.218 224.392 247.493 1.00 15.47 ? 1704 LEU A CD1   1 
ATOM   1989  C CD2   . LEU A 1 1704 ? 237.341 222.948 248.283 1.00 10.19 ? 1704 LEU A CD2   1 
ATOM   1990  N N     . VAL A 1 1705 ? 234.411 225.397 244.606 1.00 6.43  ? 1705 VAL A N     1 
ATOM   1991  C CA    . VAL A 1 1705 ? 233.372 226.350 244.227 1.00 5.73  ? 1705 VAL A CA    1 
ATOM   1992  C C     . VAL A 1 1705 ? 231.991 225.755 244.454 1.00 6.51  ? 1705 VAL A C     1 
ATOM   1993  O O     . VAL A 1 1705 ? 231.095 226.423 244.978 1.00 10.75 ? 1705 VAL A O     1 
ATOM   1994  C CB    . VAL A 1 1705 ? 233.559 226.808 242.768 1.00 4.99  ? 1705 VAL A CB    1 
ATOM   1995  C CG1   . VAL A 1 1705 ? 232.329 227.547 242.287 1.00 4.05  ? 1705 VAL A CG1   1 
ATOM   1996  C CG2   . VAL A 1 1705 ? 234.759 227.722 242.662 1.00 10.85 ? 1705 VAL A CG2   1 
ATOM   1997  N N     . GLU A 1 1706 ? 231.791 224.494 244.067 1.00 7.98  ? 1706 GLU A N     1 
ATOM   1998  C CA    . GLU A 1 1706 ? 230.496 223.857 244.301 1.00 3.85  ? 1706 GLU A CA    1 
ATOM   1999  C C     . GLU A 1 1706 ? 230.188 223.765 245.795 1.00 7.41  ? 1706 GLU A C     1 
ATOM   2000  O O     . GLU A 1 1706 ? 229.071 224.070 246.238 1.00 7.16  ? 1706 GLU A O     1 
ATOM   2001  C CB    . GLU A 1 1706 ? 230.473 222.469 243.668 1.00 1.03  ? 1706 GLU A CB    1 
ATOM   2002  C CG    . GLU A 1 1706 ? 229.178 221.723 243.895 1.00 3.84  ? 1706 GLU A CG    1 
ATOM   2003  C CD    . GLU A 1 1706 ? 229.045 220.505 243.009 1.00 12.31 ? 1706 GLU A CD    1 
ATOM   2004  O OE1   . GLU A 1 1706 ? 230.078 220.022 242.500 1.00 11.07 ? 1706 GLU A OE1   1 
ATOM   2005  O OE2   . GLU A 1 1706 ? 227.906 220.030 242.822 1.00 16.91 ? 1706 GLU A OE2   1 
ATOM   2006  N N     . LYS A 1 1707 ? 231.180 223.353 246.589 1.00 7.99  ? 1707 LYS A N     1 
ATOM   2007  C CA    . LYS A 1 1707 ? 230.985 223.229 248.030 1.00 0.68  ? 1707 LYS A CA    1 
ATOM   2008  C C     . LYS A 1 1707 ? 230.682 224.577 248.667 1.00 2.87  ? 1707 LYS A C     1 
ATOM   2009  O O     . LYS A 1 1707 ? 229.793 224.685 249.520 1.00 6.17  ? 1707 LYS A O     1 
ATOM   2010  C CB    . LYS A 1 1707 ? 232.225 222.604 248.666 1.00 4.21  ? 1707 LYS A CB    1 
ATOM   2011  C CG    . LYS A 1 1707 ? 232.044 222.170 250.109 1.00 12.12 ? 1707 LYS A CG    1 
ATOM   2012  C CD    . LYS A 1 1707 ? 233.359 222.247 250.867 1.00 3.36  ? 1707 LYS A CD    1 
ATOM   2013  C CE    . LYS A 1 1707 ? 233.135 222.273 252.369 1.00 5.05  ? 1707 LYS A CE    1 
ATOM   2014  N NZ    . LYS A 1 1707 ? 232.512 223.548 252.816 1.00 8.88  ? 1707 LYS A NZ    1 
ATOM   2015  N N     . GLU A 1 1708 ? 231.413 225.619 248.268 1.00 5.14  ? 1708 GLU A N     1 
ATOM   2016  C CA    . GLU A 1 1708 ? 231.191 226.938 248.840 1.00 3.46  ? 1708 GLU A CA    1 
ATOM   2017  C C     . GLU A 1 1708 ? 229.876 227.530 248.364 1.00 4.03  ? 1708 GLU A C     1 
ATOM   2018  O O     . GLU A 1 1708 ? 229.256 228.309 249.087 1.00 4.30  ? 1708 GLU A O     1 
ATOM   2019  C CB    . GLU A 1 1708 ? 232.356 227.865 248.494 1.00 3.77  ? 1708 GLU A CB    1 
ATOM   2020  C CG    . GLU A 1 1708 ? 232.397 229.178 249.272 1.00 10.48 ? 1708 GLU A CG    1 
ATOM   2021  C CD    . GLU A 1 1708 ? 232.172 229.005 250.767 1.00 16.54 ? 1708 GLU A CD    1 
ATOM   2022  O OE1   . GLU A 1 1708 ? 231.007 228.898 251.203 1.00 12.45 ? 1708 GLU A OE1   1 
ATOM   2023  O OE2   . GLU A 1 1708 ? 233.172 228.965 251.512 1.00 18.57 ? 1708 GLU A OE2   1 
ATOM   2024  N N     . MET A 1 1709 ? 229.425 227.163 247.165 1.00 1.87  ? 1709 MET A N     1 
ATOM   2025  C CA    . MET A 1 1709 ? 228.092 227.560 246.728 1.00 0.00  ? 1709 MET A CA    1 
ATOM   2026  C C     . MET A 1 1709 ? 227.021 226.934 247.607 1.00 5.34  ? 1709 MET A C     1 
ATOM   2027  O O     . MET A 1 1709 ? 226.087 227.617 248.044 1.00 11.05 ? 1709 MET A O     1 
ATOM   2028  C CB    . MET A 1 1709 ? 227.895 227.175 245.263 1.00 0.00  ? 1709 MET A CB    1 
ATOM   2029  C CG    . MET A 1 1709 ? 226.451 227.108 244.814 1.00 0.00  ? 1709 MET A CG    1 
ATOM   2030  S SD    . MET A 1 1709 ? 226.291 226.247 243.240 1.00 4.01  ? 1709 MET A SD    1 
ATOM   2031  C CE    . MET A 1 1709 ? 225.846 224.608 243.792 1.00 2.44  ? 1709 MET A CE    1 
ATOM   2032  N N     . ARG A 1 1710 ? 227.156 225.640 247.904 1.00 5.98  ? 1710 ARG A N     1 
ATOM   2033  C CA    . ARG A 1 1710 ? 226.205 224.992 248.802 1.00 0.00  ? 1710 ARG A CA    1 
ATOM   2034  C C     . ARG A 1 1710 ? 226.220 225.651 250.177 1.00 2.47  ? 1710 ARG A C     1 
ATOM   2035  O O     . ARG A 1 1710 ? 225.166 225.959 250.750 1.00 8.49  ? 1710 ARG A O     1 
ATOM   2036  C CB    . ARG A 1 1710 ? 226.530 223.505 248.928 1.00 4.33  ? 1710 ARG A CB    1 
ATOM   2037  C CG    . ARG A 1 1710 ? 226.289 222.688 247.676 1.00 3.09  ? 1710 ARG A CG    1 
ATOM   2038  C CD    . ARG A 1 1710 ? 226.343 221.208 247.996 1.00 3.44  ? 1710 ARG A CD    1 
ATOM   2039  N NE    . ARG A 1 1710 ? 225.948 220.386 246.860 1.00 6.39  ? 1710 ARG A NE    1 
ATOM   2040  C CZ    . ARG A 1 1710 ? 226.802 219.768 246.058 1.00 5.34  ? 1710 ARG A CZ    1 
ATOM   2041  N NH1   . ARG A 1 1710 ? 228.106 219.822 246.267 1.00 6.38  ? 1710 ARG A NH1   1 
ATOM   2042  N NH2   . ARG A 1 1710 ? 226.335 219.069 245.027 1.00 5.48  ? 1710 ARG A NH2   1 
ATOM   2043  N N     . VAL A 1 1711 ? 227.418 225.883 250.715 1.00 2.71  ? 1711 VAL A N     1 
ATOM   2044  C CA    . VAL A 1 1711 ? 227.546 226.464 252.048 1.00 2.02  ? 1711 VAL A CA    1 
ATOM   2045  C C     . VAL A 1 1711 ? 226.968 227.873 252.078 1.00 3.04  ? 1711 VAL A C     1 
ATOM   2046  O O     . VAL A 1 1711 ? 226.249 228.243 253.013 1.00 7.02  ? 1711 VAL A O     1 
ATOM   2047  C CB    . VAL A 1 1711 ? 229.018 226.438 252.496 1.00 2.22  ? 1711 VAL A CB    1 
ATOM   2048  C CG1   . VAL A 1 1711 ? 229.262 227.449 253.601 1.00 5.52  ? 1711 VAL A CG1   1 
ATOM   2049  C CG2   . VAL A 1 1711 ? 229.401 225.044 252.952 1.00 1.27  ? 1711 VAL A CG2   1 
ATOM   2050  N N     . THR A 1 1712 ? 227.275 228.681 251.061 1.00 3.34  ? 1712 THR A N     1 
ATOM   2051  C CA    . THR A 1 1712 ? 226.764 230.043 251.003 1.00 4.89  ? 1712 THR A CA    1 
ATOM   2052  C C     . THR A 1 1712 ? 225.248 230.053 250.917 1.00 3.69  ? 1712 THR A C     1 
ATOM   2053  O O     . THR A 1 1712 ? 224.589 230.853 251.588 1.00 4.99  ? 1712 THR A O     1 
ATOM   2054  C CB    . THR A 1 1712 ? 227.373 230.777 249.809 1.00 4.24  ? 1712 THR A CB    1 
ATOM   2055  O OG1   . THR A 1 1712 ? 228.787 230.905 249.997 1.00 12.77 ? 1712 THR A OG1   1 
ATOM   2056  C CG2   . THR A 1 1712 ? 226.762 232.158 249.664 1.00 2.07  ? 1712 THR A CG2   1 
ATOM   2057  N N     . LEU A 1 1713 ? 224.675 229.165 250.101 1.00 0.47  ? 1713 LEU A N     1 
ATOM   2058  C CA    . LEU A 1 1713 ? 223.223 229.074 250.026 1.00 2.85  ? 1713 LEU A CA    1 
ATOM   2059  C C     . LEU A 1 1713 ? 222.629 228.711 251.381 1.00 3.86  ? 1713 LEU A C     1 
ATOM   2060  O O     . LEU A 1 1713 ? 221.607 229.273 251.788 1.00 0.68  ? 1713 LEU A O     1 
ATOM   2061  C CB    . LEU A 1 1713 ? 222.815 228.053 248.963 1.00 4.20  ? 1713 LEU A CB    1 
ATOM   2062  C CG    . LEU A 1 1713 ? 222.513 228.552 247.544 1.00 3.86  ? 1713 LEU A CG    1 
ATOM   2063  C CD1   . LEU A 1 1713 ? 221.257 229.398 247.516 1.00 3.90  ? 1713 LEU A CD1   1 
ATOM   2064  C CD2   . LEU A 1 1713 ? 223.679 229.330 246.966 1.00 7.76  ? 1713 LEU A CD2   1 
ATOM   2065  N N     . ALA A 1 1714 ? 223.273 227.793 252.108 1.00 4.44  ? 1714 ALA A N     1 
ATOM   2066  C CA    . ALA A 1 1714 ? 222.766 227.403 253.422 1.00 1.24  ? 1714 ALA A CA    1 
ATOM   2067  C C     . ALA A 1 1714 ? 222.816 228.562 254.415 1.00 6.03  ? 1714 ALA A C     1 
ATOM   2068  O O     . ALA A 1 1714 ? 221.844 228.817 255.138 1.00 11.31 ? 1714 ALA A O     1 
ATOM   2069  C CB    . ALA A 1 1714 ? 223.554 226.208 253.951 1.00 0.00  ? 1714 ALA A CB    1 
ATOM   2070  N N     . LYS A 1 1715 ? 223.949 229.271 254.479 1.00 2.56  ? 1715 LYS A N     1 
ATOM   2071  C CA    . LYS A 1 1715 ? 224.055 230.391 255.416 1.00 1.35  ? 1715 LYS A CA    1 
ATOM   2072  C C     . LYS A 1 1715 ? 223.088 231.512 255.062 1.00 3.49  ? 1715 LYS A C     1 
ATOM   2073  O O     . LYS A 1 1715 ? 222.475 232.115 255.952 1.00 7.33  ? 1715 LYS A O     1 
ATOM   2074  C CB    . LYS A 1 1715 ? 225.483 230.938 255.482 1.00 3.21  ? 1715 LYS A CB    1 
ATOM   2075  C CG    . LYS A 1 1715 ? 226.594 229.918 255.417 1.00 6.16  ? 1715 LYS A CG    1 
ATOM   2076  C CD    . LYS A 1 1715 ? 226.629 229.058 256.665 1.00 4.70  ? 1715 LYS A CD    1 
ATOM   2077  C CE    . LYS A 1 1715 ? 227.996 228.424 256.851 1.00 4.70  ? 1715 LYS A CE    1 
ATOM   2078  N NZ    . LYS A 1 1715 ? 229.087 229.435 256.817 1.00 6.46  ? 1715 LYS A NZ    1 
ATOM   2079  N N     . LEU A 1 1716 ? 222.948 231.823 253.772 1.00 2.52  ? 1716 LEU A N     1 
ATOM   2080  C CA    . LEU A 1 1716 ? 222.004 232.861 253.385 1.00 0.00  ? 1716 LEU A CA    1 
ATOM   2081  C C     . LEU A 1 1716 ? 220.570 232.443 253.667 1.00 1.36  ? 1716 LEU A C     1 
ATOM   2082  O O     . LEU A 1 1716 ? 219.751 233.285 254.040 1.00 9.79  ? 1716 LEU A O     1 
ATOM   2083  C CB    . LEU A 1 1716 ? 222.179 233.227 251.915 1.00 0.00  ? 1716 LEU A CB    1 
ATOM   2084  C CG    . LEU A 1 1716 ? 223.530 233.790 251.480 1.00 2.73  ? 1716 LEU A CG    1 
ATOM   2085  C CD1   . LEU A 1 1716 ? 223.458 234.283 250.048 1.00 0.00  ? 1716 LEU A CD1   1 
ATOM   2086  C CD2   . LEU A 1 1716 ? 223.967 234.907 252.411 1.00 9.05  ? 1716 LEU A CD2   1 
ATOM   2087  N N     . LEU A 1 1717 ? 220.246 231.156 253.515 1.00 0.00  ? 1717 LEU A N     1 
ATOM   2088  C CA    . LEU A 1 1717 ? 218.926 230.681 253.915 1.00 0.00  ? 1717 LEU A CA    1 
ATOM   2089  C C     . LEU A 1 1717 ? 218.711 230.846 255.412 1.00 1.07  ? 1717 LEU A C     1 
ATOM   2090  O O     . LEU A 1 1717 ? 217.624 231.239 255.850 1.00 2.35  ? 1717 LEU A O     1 
ATOM   2091  C CB    . LEU A 1 1717 ? 218.744 229.221 253.510 1.00 0.11  ? 1717 LEU A CB    1 
ATOM   2092  C CG    . LEU A 1 1717 ? 217.375 228.627 253.835 1.00 0.00  ? 1717 LEU A CG    1 
ATOM   2093  C CD1   . LEU A 1 1717 ? 216.286 229.358 253.080 1.00 1.49  ? 1717 LEU A CD1   1 
ATOM   2094  C CD2   . LEU A 1 1717 ? 217.348 227.149 253.512 1.00 3.94  ? 1717 LEU A CD2   1 
ATOM   2095  N N     . ALA A 1 1718 ? 219.734 230.542 256.214 1.00 3.38  ? 1718 ALA A N     1 
ATOM   2096  C CA    . ALA A 1 1718 ? 219.618 230.711 257.660 1.00 0.00  ? 1718 ALA A CA    1 
ATOM   2097  C C     . ALA A 1 1718 ? 219.359 232.169 258.023 1.00 5.10  ? 1718 ALA A C     1 
ATOM   2098  O O     . ALA A 1 1718 ? 218.443 232.480 258.797 1.00 9.51  ? 1718 ALA A O     1 
ATOM   2099  C CB    . ALA A 1 1718 ? 220.882 230.199 258.347 1.00 0.00  ? 1718 ALA A CB    1 
ATOM   2100  N N     . GLU A 1 1719 ? 220.149 233.083 257.458 1.00 8.15  ? 1719 GLU A N     1 
ATOM   2101  C CA    . GLU A 1 1719 ? 219.952 234.500 257.750 1.00 3.41  ? 1719 GLU A CA    1 
ATOM   2102  C C     . GLU A 1 1719 ? 218.599 234.990 257.247 1.00 5.71  ? 1719 GLU A C     1 
ATOM   2103  O O     . GLU A 1 1719 ? 217.933 235.788 257.916 1.00 6.25  ? 1719 GLU A O     1 
ATOM   2104  C CB    . GLU A 1 1719 ? 221.082 235.337 257.151 1.00 2.76  ? 1719 GLU A CB    1 
ATOM   2105  C CG    . GLU A 1 1719 ? 222.480 234.844 257.465 1.00 3.66  ? 1719 GLU A CG    1 
ATOM   2106  C CD    . GLU A 1 1719 ? 223.498 235.303 256.438 1.00 9.12  ? 1719 GLU A CD    1 
ATOM   2107  O OE1   . GLU A 1 1719 ? 224.582 234.690 256.351 1.00 11.02 ? 1719 GLU A OE1   1 
ATOM   2108  O OE2   . GLU A 1 1719 ? 223.212 236.283 255.719 1.00 12.69 ? 1719 GLU A OE2   1 
ATOM   2109  N N     . SER A 1 1720 ? 218.171 234.523 256.072 1.00 2.07  ? 1720 SER A N     1 
ATOM   2110  C CA    . SER A 1 1720 ? 216.897 234.963 255.517 1.00 0.00  ? 1720 SER A CA    1 
ATOM   2111  C C     . SER A 1 1720 ? 215.724 234.476 256.354 1.00 7.70  ? 1720 SER A C     1 
ATOM   2112  O O     . SER A 1 1720 ? 214.761 235.219 256.567 1.00 22.40 ? 1720 SER A O     1 
ATOM   2113  C CB    . SER A 1 1720 ? 216.759 234.485 254.075 1.00 0.00  ? 1720 SER A CB    1 
ATOM   2114  O OG    . SER A 1 1720 ? 215.484 234.814 253.554 1.00 0.00  ? 1720 SER A OG    1 
ATOM   2115  N N     . VAL A 1 1721 ? 215.773 233.229 256.828 1.00 3.44  ? 1721 VAL A N     1 
ATOM   2116  C CA    . VAL A 1 1721 ? 214.684 232.742 257.666 1.00 2.23  ? 1721 VAL A CA    1 
ATOM   2117  C C     . VAL A 1 1721 ? 214.690 233.465 259.008 1.00 4.38  ? 1721 VAL A C     1 
ATOM   2118  O O     . VAL A 1 1721 ? 213.629 233.793 259.553 1.00 7.64  ? 1721 VAL A O     1 
ATOM   2119  C CB    . VAL A 1 1721 ? 214.741 231.208 257.819 1.00 3.65  ? 1721 VAL A CB    1 
ATOM   2120  C CG1   . VAL A 1 1721 ? 215.900 230.766 258.689 1.00 6.01  ? 1721 VAL A CG1   1 
ATOM   2121  C CG2   . VAL A 1 1721 ? 213.422 230.684 258.372 1.00 5.77  ? 1721 VAL A CG2   1 
ATOM   2122  N N     . THR A 1 1722 ? 215.880 233.772 259.538 1.00 8.50  ? 1722 THR A N     1 
ATOM   2123  C CA    . THR A 1 1722 ? 215.950 234.566 260.760 1.00 12.05 ? 1722 THR A CA    1 
ATOM   2124  C C     . THR A 1 1722 ? 215.313 235.935 260.559 1.00 9.96  ? 1722 THR A C     1 
ATOM   2125  O O     . THR A 1 1722 ? 214.574 236.417 261.425 1.00 13.63 ? 1722 THR A O     1 
ATOM   2126  C CB    . THR A 1 1722 ? 217.403 234.711 261.212 1.00 5.46  ? 1722 THR A CB    1 
ATOM   2127  O OG1   . THR A 1 1722 ? 217.924 233.426 261.569 1.00 10.06 ? 1722 THR A OG1   1 
ATOM   2128  C CG2   . THR A 1 1722 ? 217.498 235.634 262.413 1.00 3.92  ? 1722 THR A CG2   1 
ATOM   2129  N N     . GLU A 1 1723 ? 215.578 236.570 259.416 1.00 11.23 ? 1723 GLU A N     1 
ATOM   2130  C CA    . GLU A 1 1723 ? 214.999 237.882 259.143 1.00 11.06 ? 1723 GLU A CA    1 
ATOM   2131  C C     . GLU A 1 1723 ? 213.488 237.803 258.954 1.00 9.74  ? 1723 GLU A C     1 
ATOM   2132  O O     . GLU A 1 1723 ? 212.753 238.671 259.438 1.00 16.38 ? 1723 GLU A O     1 
ATOM   2133  C CB    . GLU A 1 1723 ? 215.654 238.501 257.910 1.00 7.62  ? 1723 GLU A CB    1 
ATOM   2134  C CG    . GLU A 1 1723 ? 217.092 238.931 258.123 1.00 10.46 ? 1723 GLU A CG    1 
ATOM   2135  C CD    . GLU A 1 1723 ? 217.631 239.740 256.964 1.00 9.28  ? 1723 GLU A CD    1 
ATOM   2136  O OE1   . GLU A 1 1723 ? 216.829 240.131 256.091 1.00 10.80 ? 1723 GLU A OE1   1 
ATOM   2137  O OE2   . GLU A 1 1723 ? 218.855 239.981 256.923 1.00 10.99 ? 1723 GLU A OE2   1 
ATOM   2138  N N     . VAL A 1 1724 ? 213.004 236.780 258.247 1.00 7.87  ? 1724 VAL A N     1 
ATOM   2139  C CA    . VAL A 1 1724 ? 211.576 236.701 257.957 1.00 12.14 ? 1724 VAL A CA    1 
ATOM   2140  C C     . VAL A 1 1724 ? 210.784 236.211 259.167 1.00 16.73 ? 1724 VAL A C     1 
ATOM   2141  O O     . VAL A 1 1724 ? 209.550 236.319 259.178 1.00 14.94 ? 1724 VAL A O     1 
ATOM   2142  C CB    . VAL A 1 1724 ? 211.322 235.808 256.728 1.00 10.02 ? 1724 VAL A CB    1 
ATOM   2143  C CG1   . VAL A 1 1724 ? 211.673 234.370 257.024 1.00 7.12  ? 1724 VAL A CG1   1 
ATOM   2144  C CG2   . VAL A 1 1724 ? 209.888 235.939 256.215 1.00 14.43 ? 1724 VAL A CG2   1 
ATOM   2145  N N     . GLU A 1 1725 ? 211.457 235.685 260.195 1.00 19.12 ? 1725 GLU A N     1 
ATOM   2146  C CA    . GLU A 1 1725 ? 210.751 235.360 261.433 1.00 18.71 ? 1725 GLU A CA    1 
ATOM   2147  C C     . GLU A 1 1725 ? 210.078 236.593 262.027 1.00 22.88 ? 1725 GLU A C     1 
ATOM   2148  O O     . GLU A 1 1725 ? 208.928 236.524 262.480 1.00 23.70 ? 1725 GLU A O     1 
ATOM   2149  C CB    . GLU A 1 1725 ? 211.713 234.741 262.447 1.00 17.42 ? 1725 GLU A CB    1 
ATOM   2150  C CG    . GLU A 1 1725 ? 212.078 233.298 262.160 1.00 16.33 ? 1725 GLU A CG    1 
ATOM   2151  C CD    . GLU A 1 1725 ? 210.887 232.367 262.233 1.00 21.10 ? 1725 GLU A CD    1 
ATOM   2152  O OE1   . GLU A 1 1725 ? 209.935 232.670 262.982 1.00 23.49 ? 1725 GLU A OE1   1 
ATOM   2153  O OE2   . GLU A 1 1725 ? 210.898 231.335 261.531 1.00 16.36 ? 1725 GLU A OE2   1 
ATOM   2154  N N     . ILE A 1 1726 ? 210.779 237.731 262.031 1.00 18.39 ? 1726 ILE A N     1 
ATOM   2155  C CA    . ILE A 1 1726 ? 210.209 238.958 262.582 1.00 20.71 ? 1726 ILE A CA    1 
ATOM   2156  C C     . ILE A 1 1726 ? 208.974 239.379 261.796 1.00 24.29 ? 1726 ILE A C     1 
ATOM   2157  O O     . ILE A 1 1726 ? 207.950 239.755 262.379 1.00 29.61 ? 1726 ILE A O     1 
ATOM   2158  C CB    . ILE A 1 1726 ? 211.265 240.080 262.621 1.00 24.83 ? 1726 ILE A CB    1 
ATOM   2159  C CG1   . ILE A 1 1726 ? 212.426 239.719 263.555 1.00 25.36 ? 1726 ILE A CG1   1 
ATOM   2160  C CG2   . ILE A 1 1726 ? 210.634 241.398 263.038 1.00 26.90 ? 1726 ILE A CG2   1 
ATOM   2161  C CD1   . ILE A 1 1726 ? 213.556 238.971 262.901 1.00 24.60 ? 1726 ILE A CD1   1 
ATOM   2162  N N     . PHE A 1 1727 ? 209.047 239.325 260.465 1.00 21.75 ? 1727 PHE A N     1 
ATOM   2163  C CA    . PHE A 1 1727 ? 207.887 239.687 259.656 1.00 22.24 ? 1727 PHE A CA    1 
ATOM   2164  C C     . PHE A 1 1727 ? 206.722 238.739 259.902 1.00 24.30 ? 1727 PHE A C     1 
ATOM   2165  O O     . PHE A 1 1727 ? 205.568 239.175 259.989 1.00 30.35 ? 1727 PHE A O     1 
ATOM   2166  C CB    . PHE A 1 1727 ? 208.249 239.707 258.169 1.00 21.14 ? 1727 PHE A CB    1 
ATOM   2167  C CG    . PHE A 1 1727 ? 209.511 240.460 257.854 1.00 24.76 ? 1727 PHE A CG    1 
ATOM   2168  C CD1   . PHE A 1 1727 ? 209.850 241.604 258.557 1.00 23.93 ? 1727 PHE A CD1   1 
ATOM   2169  C CD2   . PHE A 1 1727 ? 210.347 240.034 256.836 1.00 15.56 ? 1727 PHE A CD2   1 
ATOM   2170  C CE1   . PHE A 1 1727 ? 211.006 242.298 258.262 1.00 25.08 ? 1727 PHE A CE1   1 
ATOM   2171  C CE2   . PHE A 1 1727 ? 211.502 240.725 256.535 1.00 18.75 ? 1727 PHE A CE2   1 
ATOM   2172  C CZ    . PHE A 1 1727 ? 211.833 241.859 257.249 1.00 24.79 ? 1727 PHE A CZ    1 
ATOM   2173  N N     . GLY A 1 1728 ? 207.000 237.439 260.014 1.00 25.94 ? 1728 GLY A N     1 
ATOM   2174  C CA    . GLY A 1 1728 ? 205.926 236.478 260.206 1.00 27.36 ? 1728 GLY A CA    1 
ATOM   2175  C C     . GLY A 1 1728 ? 205.247 236.599 261.557 1.00 28.52 ? 1728 GLY A C     1 
ATOM   2176  O O     . GLY A 1 1728 ? 204.027 236.443 261.663 1.00 23.61 ? 1728 GLY A O     1 
ATOM   2177  N N     . LYS A 1 1729 ? 206.023 236.872 262.610 1.00 27.53 ? 1729 LYS A N     1 
ATOM   2178  C CA    . LYS A 1 1729 ? 205.452 236.890 263.954 1.00 29.62 ? 1729 LYS A CA    1 
ATOM   2179  C C     . LYS A 1 1729 ? 204.581 238.121 264.182 1.00 31.52 ? 1729 LYS A C     1 
ATOM   2180  O O     . LYS A 1 1729 ? 203.614 238.068 264.951 1.00 34.00 ? 1729 LYS A O     1 
ATOM   2181  C CB    . LYS A 1 1729 ? 206.569 236.798 265.000 1.00 29.28 ? 1729 LYS A CB    1 
ATOM   2182  C CG    . LYS A 1 1729 ? 207.549 237.971 265.037 1.00 30.31 ? 1729 LYS A CG    1 
ATOM   2183  C CD    . LYS A 1 1729 ? 207.116 239.070 265.999 1.00 29.48 ? 1729 LYS A CD    1 
ATOM   2184  C CE    . LYS A 1 1729 ? 208.164 240.167 266.091 1.00 27.25 ? 1729 LYS A CE    1 
ATOM   2185  N NZ    . LYS A 1 1729 ? 207.744 241.259 267.012 1.00 32.53 ? 1729 LYS A NZ    1 
ATOM   2186  N N     . ALA A 1 1730 ? 204.899 239.233 263.524 1.00 27.44 ? 1730 ALA A N     1 
ATOM   2187  C CA    . ALA A 1 1730 ? 204.229 240.500 263.783 1.00 32.46 ? 1730 ALA A CA    1 
ATOM   2188  C C     . ALA A 1 1730 ? 203.120 240.738 262.766 1.00 31.77 ? 1730 ALA A C     1 
ATOM   2189  O O     . ALA A 1 1730 ? 203.318 240.543 261.563 1.00 27.68 ? 1730 ALA A O     1 
ATOM   2190  C CB    . ALA A 1 1730 ? 205.231 241.654 263.752 1.00 30.65 ? 1730 ALA A CB    1 
ATOM   2191  N N     . THR A 1 1731 ? 201.951 241.158 263.259 1.00 36.31 ? 1731 THR A N     1 
ATOM   2192  C CA    . THR A 1 1731 ? 200.843 241.484 262.367 1.00 36.27 ? 1731 THR A CA    1 
ATOM   2193  C C     . THR A 1 1731 ? 201.155 242.711 261.519 1.00 32.50 ? 1731 THR A C     1 
ATOM   2194  O O     . THR A 1 1731 ? 200.922 242.710 260.305 1.00 29.70 ? 1731 THR A O     1 
ATOM   2195  C CB    . THR A 1 1731 ? 199.565 241.708 263.176 1.00 32.68 ? 1731 THR A CB    1 
ATOM   2196  O OG1   . THR A 1 1731 ? 199.724 242.857 264.018 1.00 30.41 ? 1731 THR A OG1   1 
ATOM   2197  C CG2   . THR A 1 1731 ? 199.258 240.493 264.037 1.00 33.13 ? 1731 THR A CG2   1 
ATOM   2198  N N     . SER A 1 1732 ? 201.686 243.763 262.137 1.00 28.48 ? 1732 SER A N     1 
ATOM   2199  C CA    . SER A 1 1732 ? 202.041 244.976 261.412 1.00 33.62 ? 1732 SER A CA    1 
ATOM   2200  C C     . SER A 1 1732 ? 203.343 244.742 260.658 1.00 33.95 ? 1732 SER A C     1 
ATOM   2201  O O     . SER A 1 1732 ? 204.361 244.387 261.261 1.00 35.52 ? 1732 SER A O     1 
ATOM   2202  C CB    . SER A 1 1732 ? 202.173 246.154 262.375 1.00 34.97 ? 1732 SER A CB    1 
ATOM   2203  O OG    . SER A 1 1732 ? 202.751 247.277 261.733 1.00 36.26 ? 1732 SER A OG    1 
ATOM   2204  N N     . ILE A 1 1733 ? 203.311 244.938 259.342 1.00 25.80 ? 1733 ILE A N     1 
ATOM   2205  C CA    . ILE A 1 1733 ? 204.465 244.702 258.483 1.00 23.98 ? 1733 ILE A CA    1 
ATOM   2206  C C     . ILE A 1 1733 ? 204.769 245.988 257.724 1.00 25.19 ? 1733 ILE A C     1 
ATOM   2207  O O     . ILE A 1 1733 ? 203.857 246.640 257.199 1.00 23.60 ? 1733 ILE A O     1 
ATOM   2208  C CB    . ILE A 1 1733 ? 204.240 243.515 257.525 1.00 26.68 ? 1733 ILE A CB    1 
ATOM   2209  C CG1   . ILE A 1 1733 ? 205.570 243.010 256.957 1.00 25.71 ? 1733 ILE A CG1   1 
ATOM   2210  C CG2   . ILE A 1 1733 ? 203.243 243.846 256.425 1.00 22.48 ? 1733 ILE A CG2   1 
ATOM   2211  C CD1   . ILE A 1 1733 ? 205.430 241.760 256.117 1.00 18.92 ? 1733 ILE A CD1   1 
ATOM   2212  N N     . ASP A 1 1734 ? 206.031 246.381 257.722 1.00 27.08 ? 1734 ASP A N     1 
ATOM   2213  C CA    . ASP A 1 1734 ? 206.472 247.581 257.022 1.00 22.98 ? 1734 ASP A CA    1 
ATOM   2214  C C     . ASP A 1 1734 ? 206.902 247.214 255.606 1.00 20.84 ? 1734 ASP A C     1 
ATOM   2215  O O     . ASP A 1 1734 ? 207.831 246.416 255.438 1.00 20.34 ? 1734 ASP A O     1 
ATOM   2216  C CB    . ASP A 1 1734 ? 207.628 248.238 257.767 1.00 21.88 ? 1734 ASP A CB    1 
ATOM   2217  C CG    . ASP A 1 1734 ? 207.986 249.609 257.219 1.00 25.91 ? 1734 ASP A CG    1 
ATOM   2218  O OD1   . ASP A 1 1734 ? 207.358 250.054 256.237 1.00 21.67 ? 1734 ASP A OD1   1 
ATOM   2219  O OD2   . ASP A 1 1734 ? 208.901 250.246 257.780 1.00 26.85 ? 1734 ASP A OD2   1 
ATOM   2220  N N     . PRO A 1 1735 ? 206.251 247.757 254.574 1.00 22.19 ? 1735 PRO A N     1 
ATOM   2221  C CA    . PRO A 1 1735 ? 206.646 247.411 253.199 1.00 20.58 ? 1735 PRO A CA    1 
ATOM   2222  C C     . PRO A 1 1735 ? 208.092 247.740 252.875 1.00 16.65 ? 1735 PRO A C     1 
ATOM   2223  O O     . PRO A 1 1735 ? 208.710 247.030 252.072 1.00 12.13 ? 1735 PRO A O     1 
ATOM   2224  C CB    . PRO A 1 1735 ? 205.674 248.234 252.342 1.00 19.36 ? 1735 PRO A CB    1 
ATOM   2225  C CG    . PRO A 1 1735 ? 204.494 248.450 253.222 1.00 19.40 ? 1735 PRO A CG    1 
ATOM   2226  C CD    . PRO A 1 1735 ? 205.048 248.604 254.607 1.00 20.86 ? 1735 PRO A CD    1 
ATOM   2227  N N     . ASN A 1 1736 ? 208.656 248.787 253.480 1.00 20.94 ? 1736 ASN A N     1 
ATOM   2228  C CA    . ASN A 1 1736 ? 210.030 249.170 253.172 1.00 19.35 ? 1736 ASN A CA    1 
ATOM   2229  C C     . ASN A 1 1736 ? 211.010 248.064 253.548 1.00 18.54 ? 1736 ASN A C     1 
ATOM   2230  O O     . ASN A 1 1736 ? 211.809 247.617 252.716 1.00 21.61 ? 1736 ASN A O     1 
ATOM   2231  C CB    . ASN A 1 1736 ? 210.383 250.469 253.898 1.00 15.69 ? 1736 ASN A CB    1 
ATOM   2232  C CG    . ASN A 1 1736 ? 211.131 251.445 253.015 1.00 20.70 ? 1736 ASN A CG    1 
ATOM   2233  O OD1   . ASN A 1 1736 ? 210.990 251.428 251.793 1.00 24.08 ? 1736 ASN A OD1   1 
ATOM   2234  N ND2   . ASN A 1 1736 ? 211.933 252.304 253.632 1.00 21.50 ? 1736 ASN A ND2   1 
ATOM   2235  N N     . THR A 1 1737 ? 210.947 247.590 254.794 1.00 15.49 ? 1737 THR A N     1 
ATOM   2236  C CA    . THR A 1 1737 ? 211.891 246.565 255.229 1.00 13.56 ? 1737 THR A CA    1 
ATOM   2237  C C     . THR A 1 1737 ? 211.594 245.226 254.568 1.00 13.55 ? 1737 THR A C     1 
ATOM   2238  O O     . THR A 1 1737 ? 212.502 244.415 254.361 1.00 14.13 ? 1737 THR A O     1 
ATOM   2239  C CB    . THR A 1 1737 ? 211.874 246.431 256.753 1.00 20.59 ? 1737 THR A CB    1 
ATOM   2240  O OG1   . THR A 1 1737 ? 212.772 245.388 257.151 1.00 22.06 ? 1737 THR A OG1   1 
ATOM   2241  C CG2   . THR A 1 1737 ? 210.478 246.105 257.252 1.00 15.06 ? 1737 THR A CG2   1 
ATOM   2242  N N     . TYR A 1 1738 ? 210.333 244.984 254.209 1.00 17.05 ? 1738 TYR A N     1 
ATOM   2243  C CA    . TYR A 1 1738 ? 209.987 243.735 253.540 1.00 12.66 ? 1738 TYR A CA    1 
ATOM   2244  C C     . TYR A 1 1738 ? 210.571 243.693 252.131 1.00 6.12  ? 1738 TYR A C     1 
ATOM   2245  O O     . TYR A 1 1738 ? 211.156 242.681 251.720 1.00 3.44  ? 1738 TYR A O     1 
ATOM   2246  C CB    . TYR A 1 1738 ? 208.467 243.574 253.520 1.00 9.85  ? 1738 TYR A CB    1 
ATOM   2247  C CG    . TYR A 1 1738 ? 207.972 242.274 252.936 1.00 10.10 ? 1738 TYR A CG    1 
ATOM   2248  C CD1   . TYR A 1 1738 ? 208.055 241.095 253.662 1.00 12.78 ? 1738 TYR A CD1   1 
ATOM   2249  C CD2   . TYR A 1 1738 ? 207.401 242.226 251.675 1.00 12.62 ? 1738 TYR A CD2   1 
ATOM   2250  C CE1   . TYR A 1 1738 ? 207.597 239.903 253.144 1.00 8.73  ? 1738 TYR A CE1   1 
ATOM   2251  C CE2   . TYR A 1 1738 ? 206.938 241.037 251.148 1.00 8.93  ? 1738 TYR A CE2   1 
ATOM   2252  C CZ    . TYR A 1 1738 ? 207.040 239.879 251.887 1.00 9.05  ? 1738 TYR A CZ    1 
ATOM   2253  O OH    . TYR A 1 1738 ? 206.581 238.692 251.367 1.00 9.92  ? 1738 TYR A OH    1 
ATOM   2254  N N     . ILE A 1 1739 ? 210.452 244.796 251.388 1.00 9.75  ? 1739 ILE A N     1 
ATOM   2255  C CA    . ILE A 1 1739 ? 211.094 244.885 250.079 1.00 8.54  ? 1739 ILE A CA    1 
ATOM   2256  C C     . ILE A 1 1739 ? 212.610 244.852 250.222 1.00 10.06 ? 1739 ILE A C     1 
ATOM   2257  O O     . ILE A 1 1739 ? 213.312 244.299 249.368 1.00 10.37 ? 1739 ILE A O     1 
ATOM   2258  C CB    . ILE A 1 1739 ? 210.617 246.143 249.330 1.00 10.09 ? 1739 ILE A CB    1 
ATOM   2259  C CG1   . ILE A 1 1739 ? 209.102 246.102 249.130 1.00 11.82 ? 1739 ILE A CG1   1 
ATOM   2260  C CG2   . ILE A 1 1739 ? 211.322 246.275 247.992 1.00 6.72  ? 1739 ILE A CG2   1 
ATOM   2261  C CD1   . ILE A 1 1739 ? 208.628 244.927 248.311 1.00 8.26  ? 1739 ILE A CD1   1 
ATOM   2262  N N     . THR A 1 1740 ? 213.144 245.443 251.294 1.00 8.20  ? 1740 THR A N     1 
ATOM   2263  C CA    . THR A 1 1740 ? 214.583 245.367 251.530 1.00 8.06  ? 1740 THR A CA    1 
ATOM   2264  C C     . THR A 1 1740 ? 215.034 243.923 251.718 1.00 5.82  ? 1740 THR A C     1 
ATOM   2265  O O     . THR A 1 1740 ? 216.061 243.505 251.167 1.00 7.88  ? 1740 THR A O     1 
ATOM   2266  C CB    . THR A 1 1740 ? 214.958 246.209 252.750 1.00 10.60 ? 1740 THR A CB    1 
ATOM   2267  O OG1   . THR A 1 1740 ? 214.709 247.592 252.471 1.00 14.91 ? 1740 THR A OG1   1 
ATOM   2268  C CG2   . THR A 1 1740 ? 216.428 246.028 253.094 1.00 12.32 ? 1740 THR A CG2   1 
ATOM   2269  N N     . TRP A 1 1741 ? 214.271 243.145 252.488 1.00 8.81  ? 1741 TRP A N     1 
ATOM   2270  C CA    . TRP A 1 1741 ? 214.583 241.732 252.673 1.00 2.35  ? 1741 TRP A CA    1 
ATOM   2271  C C     . TRP A 1 1741 ? 214.496 240.974 251.355 1.00 5.60  ? 1741 TRP A C     1 
ATOM   2272  O O     . TRP A 1 1741 ? 215.342 240.121 251.064 1.00 7.51  ? 1741 TRP A O     1 
ATOM   2273  C CB    . TRP A 1 1741 ? 213.633 241.115 253.697 1.00 3.75  ? 1741 TRP A CB    1 
ATOM   2274  C CG    . TRP A 1 1741 ? 213.632 239.621 253.675 1.00 3.79  ? 1741 TRP A CG    1 
ATOM   2275  C CD1   . TRP A 1 1741 ? 214.586 238.795 254.188 1.00 9.02  ? 1741 TRP A CD1   1 
ATOM   2276  C CD2   . TRP A 1 1741 ? 212.649 238.773 253.074 1.00 6.53  ? 1741 TRP A CD2   1 
ATOM   2277  N NE1   . TRP A 1 1741 ? 214.247 237.483 253.964 1.00 3.78  ? 1741 TRP A NE1   1 
ATOM   2278  C CE2   . TRP A 1 1741 ? 213.063 237.443 253.278 1.00 6.15  ? 1741 TRP A CE2   1 
ATOM   2279  C CE3   . TRP A 1 1741 ? 211.455 239.008 252.387 1.00 5.36  ? 1741 TRP A CE3   1 
ATOM   2280  C CZ2   . TRP A 1 1741 ? 212.325 236.355 252.824 1.00 4.91  ? 1741 TRP A CZ2   1 
ATOM   2281  C CZ3   . TRP A 1 1741 ? 210.725 237.927 251.937 1.00 3.27  ? 1741 TRP A CZ3   1 
ATOM   2282  C CH2   . TRP A 1 1741 ? 211.161 236.617 252.157 1.00 5.53  ? 1741 TRP A CH2   1 
ATOM   2283  N N     . ILE A 1 1742 ? 213.470 241.266 250.550 1.00 8.20  ? 1742 ILE A N     1 
ATOM   2284  C CA    . ILE A 1 1742 ? 213.344 240.621 249.243 1.00 3.74  ? 1742 ILE A CA    1 
ATOM   2285  C C     . ILE A 1 1742 ? 214.560 240.924 248.381 1.00 4.61  ? 1742 ILE A C     1 
ATOM   2286  O O     . ILE A 1 1742 ? 215.124 240.030 247.738 1.00 9.66  ? 1742 ILE A O     1 
ATOM   2287  C CB    . ILE A 1 1742 ? 212.045 241.063 248.543 1.00 0.99  ? 1742 ILE A CB    1 
ATOM   2288  C CG1   . ILE A 1 1742 ? 210.817 240.543 249.284 1.00 11.46 ? 1742 ILE A CG1   1 
ATOM   2289  C CG2   . ILE A 1 1742 ? 212.027 240.589 247.103 1.00 0.00  ? 1742 ILE A CG2   1 
ATOM   2290  C CD1   . ILE A 1 1742 ? 209.522 241.091 248.741 1.00 9.17  ? 1742 ILE A CD1   1 
ATOM   2291  N N     . ASP A 1 1743 ? 214.982 242.188 248.354 1.00 6.55  ? 1743 ASP A N     1 
ATOM   2292  C CA    . ASP A 1 1743 ? 216.117 242.585 247.528 1.00 2.36  ? 1743 ASP A CA    1 
ATOM   2293  C C     . ASP A 1 1743 ? 217.408 241.937 248.006 1.00 1.63  ? 1743 ASP A C     1 
ATOM   2294  O O     . ASP A 1 1743 ? 218.248 241.541 247.190 1.00 5.71  ? 1743 ASP A O     1 
ATOM   2295  C CB    . ASP A 1 1743 ? 216.253 244.106 247.532 1.00 2.42  ? 1743 ASP A CB    1 
ATOM   2296  C CG    . ASP A 1 1743 ? 215.607 244.750 246.327 1.00 7.09  ? 1743 ASP A CG    1 
ATOM   2297  O OD1   . ASP A 1 1743 ? 214.927 244.034 245.565 1.00 1.42  ? 1743 ASP A OD1   1 
ATOM   2298  O OD2   . ASP A 1 1743 ? 215.778 245.973 246.143 1.00 11.08 ? 1743 ASP A OD2   1 
ATOM   2299  N N     . LYS A 1 1744 ? 217.588 241.829 249.323 1.00 1.68  ? 1744 LYS A N     1 
ATOM   2300  C CA    . LYS A 1 1744 ? 218.854 241.340 249.860 1.00 3.25  ? 1744 LYS A CA    1 
ATOM   2301  C C     . LYS A 1 1744 ? 219.104 239.885 249.484 1.00 2.59  ? 1744 LYS A C     1 
ATOM   2302  O O     . LYS A 1 1744 ? 220.245 239.499 249.205 1.00 3.26  ? 1744 LYS A O     1 
ATOM   2303  C CB    . LYS A 1 1744 ? 218.877 241.512 251.378 1.00 6.27  ? 1744 LYS A CB    1 
ATOM   2304  C CG    . LYS A 1 1744 ? 220.160 241.037 252.033 1.00 0.26  ? 1744 LYS A CG    1 
ATOM   2305  C CD    . LYS A 1 1744 ? 220.091 241.167 253.541 1.00 1.45  ? 1744 LYS A CD    1 
ATOM   2306  C CE    . LYS A 1 1744 ? 221.331 240.589 254.196 1.00 5.23  ? 1744 LYS A CE    1 
ATOM   2307  N NZ    . LYS A 1 1744 ? 221.210 240.557 255.678 1.00 14.07 ? 1744 LYS A NZ    1 
ATOM   2308  N N     . TYR A 1 1745 ? 218.059 239.067 249.461 1.00 5.14  ? 1745 TYR A N     1 
ATOM   2309  C CA    . TYR A 1 1745 ? 218.198 237.624 249.353 1.00 3.34  ? 1745 TYR A CA    1 
ATOM   2310  C C     . TYR A 1 1745 ? 217.693 237.128 248.004 1.00 8.49  ? 1745 TYR A C     1 
ATOM   2311  O O     . TYR A 1 1745 ? 216.789 237.716 247.404 1.00 9.17  ? 1745 TYR A O     1 
ATOM   2312  C CB    . TYR A 1 1745 ? 217.446 236.936 250.492 1.00 0.00  ? 1745 TYR A CB    1 
ATOM   2313  C CG    . TYR A 1 1745 ? 218.123 237.138 251.826 1.00 4.25  ? 1745 TYR A CG    1 
ATOM   2314  C CD1   . TYR A 1 1745 ? 219.443 236.761 252.019 1.00 3.56  ? 1745 TYR A CD1   1 
ATOM   2315  C CD2   . TYR A 1 1745 ? 217.458 237.753 252.875 1.00 5.52  ? 1745 TYR A CD2   1 
ATOM   2316  C CE1   . TYR A 1 1745 ? 220.071 236.959 253.230 1.00 1.07  ? 1745 TYR A CE1   1 
ATOM   2317  C CE2   . TYR A 1 1745 ? 218.077 237.957 254.087 1.00 4.79  ? 1745 TYR A CE2   1 
ATOM   2318  C CZ    . TYR A 1 1745 ? 219.383 237.557 254.260 1.00 1.50  ? 1745 TYR A CZ    1 
ATOM   2319  O OH    . TYR A 1 1745 ? 220.003 237.762 255.468 1.00 5.64  ? 1745 TYR A OH    1 
ATOM   2320  N N     . GLN A 1 1746 ? 218.290 236.035 247.539 1.00 9.38  ? 1746 GLN A N     1 
ATOM   2321  C CA    . GLN A 1 1746 ? 217.988 235.490 246.225 1.00 3.99  ? 1746 GLN A CA    1 
ATOM   2322  C C     . GLN A 1 1746 ? 216.565 234.941 246.174 1.00 5.24  ? 1746 GLN A C     1 
ATOM   2323  O O     . GLN A 1 1746 ? 215.964 234.599 247.195 1.00 9.49  ? 1746 GLN A O     1 
ATOM   2324  C CB    . GLN A 1 1746 ? 218.989 234.395 245.859 1.00 1.30  ? 1746 GLN A CB    1 
ATOM   2325  C CG    . GLN A 1 1746 ? 220.408 234.894 245.642 1.00 0.00  ? 1746 GLN A CG    1 
ATOM   2326  C CD    . GLN A 1 1746 ? 221.154 235.141 246.937 1.00 0.00  ? 1746 GLN A CD    1 
ATOM   2327  O OE1   . GLN A 1 1746 ? 220.636 234.892 248.024 1.00 3.01  ? 1746 GLN A OE1   1 
ATOM   2328  N NE2   . GLN A 1 1746 ? 222.378 235.638 246.826 1.00 0.00  ? 1746 GLN A NE2   1 
ATOM   2329  N N     . ALA A 1 1747 ? 216.030 234.856 244.952 1.00 3.11  ? 1747 ALA A N     1 
ATOM   2330  C CA    . ALA A 1 1747 ? 214.645 234.429 244.773 1.00 3.84  ? 1747 ALA A CA    1 
ATOM   2331  C C     . ALA A 1 1747 ? 214.420 233.024 245.314 1.00 4.16  ? 1747 ALA A C     1 
ATOM   2332  O O     . ALA A 1 1747 ? 213.422 232.766 245.998 1.00 5.50  ? 1747 ALA A O     1 
ATOM   2333  C CB    . ALA A 1 1747 ? 214.262 234.501 243.295 1.00 3.71  ? 1747 ALA A CB    1 
ATOM   2334  N N     . GLN A 1 1748 ? 215.341 232.105 245.017 1.00 3.62  ? 1748 GLN A N     1 
ATOM   2335  C CA    . GLN A 1 1748 ? 215.270 230.761 245.580 1.00 1.07  ? 1748 GLN A CA    1 
ATOM   2336  C C     . GLN A 1 1748 ? 215.161 230.809 247.097 1.00 3.16  ? 1748 GLN A C     1 
ATOM   2337  O O     . GLN A 1 1748 ? 214.255 230.205 247.685 1.00 9.29  ? 1748 GLN A O     1 
ATOM   2338  C CB    . GLN A 1 1748 ? 216.505 229.968 245.157 1.00 3.25  ? 1748 GLN A CB    1 
ATOM   2339  C CG    . GLN A 1 1748 ? 216.616 228.583 245.752 1.00 4.73  ? 1748 GLN A CG    1 
ATOM   2340  C CD    . GLN A 1 1748 ? 217.861 227.860 245.284 1.00 2.75  ? 1748 GLN A CD    1 
ATOM   2341  O OE1   . GLN A 1 1748 ? 218.623 228.381 244.474 1.00 2.38  ? 1748 GLN A OE1   1 
ATOM   2342  N NE2   . GLN A 1 1748 ? 218.077 226.656 245.799 1.00 3.73  ? 1748 GLN A NE2   1 
ATOM   2343  N N     . LEU A 1 1749 ? 216.054 231.557 247.743 1.00 2.56  ? 1749 LEU A N     1 
ATOM   2344  C CA    . LEU A 1 1749 ? 216.067 231.636 249.197 1.00 3.29  ? 1749 LEU A CA    1 
ATOM   2345  C C     . LEU A 1 1749 ? 214.899 232.441 249.746 1.00 2.31  ? 1749 LEU A C     1 
ATOM   2346  O O     . LEU A 1 1749 ? 214.428 232.149 250.844 1.00 0.00  ? 1749 LEU A O     1 
ATOM   2347  C CB    . LEU A 1 1749 ? 217.390 232.228 249.669 1.00 0.30  ? 1749 LEU A CB    1 
ATOM   2348  C CG    . LEU A 1 1749 ? 218.579 231.379 249.234 1.00 0.00  ? 1749 LEU A CG    1 
ATOM   2349  C CD1   . LEU A 1 1749 ? 219.867 232.006 249.688 1.00 3.67  ? 1749 LEU A CD1   1 
ATOM   2350  C CD2   . LEU A 1 1749 ? 218.443 229.972 249.789 1.00 0.00  ? 1749 LEU A CD2   1 
ATOM   2351  N N     . VAL A 1 1750 ? 214.416 233.443 249.012 1.00 0.00  ? 1750 VAL A N     1 
ATOM   2352  C CA    . VAL A 1 1750 ? 213.236 234.182 249.454 1.00 2.42  ? 1750 VAL A CA    1 
ATOM   2353  C C     . VAL A 1 1750 ? 212.021 233.262 249.509 1.00 5.43  ? 1750 VAL A C     1 
ATOM   2354  O O     . VAL A 1 1750 ? 211.283 233.229 250.505 1.00 12.47 ? 1750 VAL A O     1 
ATOM   2355  C CB    . VAL A 1 1750 ? 212.995 235.391 248.534 1.00 2.11  ? 1750 VAL A CB    1 
ATOM   2356  C CG1   . VAL A 1 1750 ? 211.595 235.931 248.718 1.00 8.64  ? 1750 VAL A CG1   1 
ATOM   2357  C CG2   . VAL A 1 1750 ? 214.016 236.476 248.819 1.00 0.00  ? 1750 VAL A CG2   1 
ATOM   2358  N N     . VAL A 1 1751 ? 211.809 232.488 248.443 1.00 0.23  ? 1751 VAL A N     1 
ATOM   2359  C CA    . VAL A 1 1751 ? 210.707 231.529 248.413 1.00 0.00  ? 1751 VAL A CA    1 
ATOM   2360  C C     . VAL A 1 1751 ? 210.877 230.475 249.499 1.00 0.00  ? 1751 VAL A C     1 
ATOM   2361  O O     . VAL A 1 1751 ? 209.917 230.122 250.198 1.00 2.26  ? 1751 VAL A O     1 
ATOM   2362  C CB    . VAL A 1 1751 ? 210.598 230.897 247.015 1.00 1.85  ? 1751 VAL A CB    1 
ATOM   2363  C CG1   . VAL A 1 1751 ? 209.435 229.965 246.956 1.00 2.88  ? 1751 VAL A CG1   1 
ATOM   2364  C CG2   . VAL A 1 1751 ? 210.410 231.979 245.978 1.00 2.53  ? 1751 VAL A CG2   1 
ATOM   2365  N N     . LEU A 1 1752 ? 212.099 229.960 249.663 1.00 0.90  ? 1752 LEU A N     1 
ATOM   2366  C CA    . LEU A 1 1752 ? 212.343 228.960 250.695 1.00 2.43  ? 1752 LEU A CA    1 
ATOM   2367  C C     . LEU A 1 1752 ? 212.067 229.513 252.085 1.00 6.20  ? 1752 LEU A C     1 
ATOM   2368  O O     . LEU A 1 1752 ? 211.494 228.820 252.932 1.00 10.33 ? 1752 LEU A O     1 
ATOM   2369  C CB    . LEU A 1 1752 ? 213.780 228.460 250.612 1.00 0.39  ? 1752 LEU A CB    1 
ATOM   2370  C CG    . LEU A 1 1752 ? 214.048 227.192 249.816 1.00 0.00  ? 1752 LEU A CG    1 
ATOM   2371  C CD1   . LEU A 1 1752 ? 215.539 227.009 249.716 1.00 0.13  ? 1752 LEU A CD1   1 
ATOM   2372  C CD2   . LEU A 1 1752 ? 213.392 225.996 250.478 1.00 0.00  ? 1752 LEU A CD2   1 
ATOM   2373  N N     . SER A 1 1753 ? 212.494 230.748 252.348 1.00 2.24  ? 1753 SER A N     1 
ATOM   2374  C CA    . SER A 1 1753 ? 212.281 231.352 253.655 1.00 0.00  ? 1753 SER A CA    1 
ATOM   2375  C C     . SER A 1 1753 ? 210.800 231.532 253.935 1.00 0.00  ? 1753 SER A C     1 
ATOM   2376  O O     . SER A 1 1753 ? 210.330 231.239 255.041 1.00 0.05  ? 1753 SER A O     1 
ATOM   2377  C CB    . SER A 1 1753 ? 213.003 232.694 253.725 1.00 1.69  ? 1753 SER A CB    1 
ATOM   2378  O OG    . SER A 1 1753 ? 214.390 232.528 253.509 1.00 8.17  ? 1753 SER A OG    1 
ATOM   2379  N N     . ALA A 1 1754 ? 210.047 232.011 252.941 1.00 0.00  ? 1754 ALA A N     1 
ATOM   2380  C CA    . ALA A 1 1754 ? 208.607 232.145 253.126 1.00 0.81  ? 1754 ALA A CA    1 
ATOM   2381  C C     . ALA A 1 1754 ? 207.961 230.797 253.411 1.00 3.98  ? 1754 ALA A C     1 
ATOM   2382  O O     . ALA A 1 1754 ? 207.114 230.687 254.308 1.00 5.06  ? 1754 ALA A O     1 
ATOM   2383  C CB    . ALA A 1 1754 ? 207.975 232.789 251.895 1.00 0.00  ? 1754 ALA A CB    1 
ATOM   2384  N N     . GLN A 1 1755 ? 208.366 229.760 252.677 1.00 7.35  ? 1755 GLN A N     1 
ATOM   2385  C CA    . GLN A 1 1755 ? 207.790 228.435 252.867 1.00 0.00  ? 1755 GLN A CA    1 
ATOM   2386  C C     . GLN A 1 1755 ? 208.117 227.868 254.243 1.00 0.00  ? 1755 GLN A C     1 
ATOM   2387  O O     . GLN A 1 1755 ? 207.239 227.307 254.908 1.00 7.28  ? 1755 GLN A O     1 
ATOM   2388  C CB    . GLN A 1 1755 ? 208.285 227.506 251.761 1.00 0.62  ? 1755 GLN A CB    1 
ATOM   2389  C CG    . GLN A 1 1755 ? 207.385 227.519 250.541 1.00 2.65  ? 1755 GLN A CG    1 
ATOM   2390  C CD    . GLN A 1 1755 ? 207.838 226.570 249.459 1.00 2.87  ? 1755 GLN A CD    1 
ATOM   2391  O OE1   . GLN A 1 1755 ? 207.092 225.686 249.042 1.00 7.13  ? 1755 GLN A OE1   1 
ATOM   2392  N NE2   . GLN A 1 1755 ? 209.067 226.750 248.990 1.00 5.80  ? 1755 GLN A NE2   1 
ATOM   2393  N N     . ILE A 1 1756 ? 209.365 228.017 254.691 1.00 0.00  ? 1756 ILE A N     1 
ATOM   2394  C CA    . ILE A 1 1756 ? 209.754 227.513 256.004 1.00 0.00  ? 1756 ILE A CA    1 
ATOM   2395  C C     . ILE A 1 1756 ? 209.012 228.257 257.105 1.00 0.94  ? 1756 ILE A C     1 
ATOM   2396  O O     . ILE A 1 1756 ? 208.525 227.645 258.066 1.00 1.36  ? 1756 ILE A O     1 
ATOM   2397  C CB    . ILE A 1 1756 ? 211.278 227.612 256.187 1.00 0.00  ? 1756 ILE A CB    1 
ATOM   2398  C CG1   . ILE A 1 1756 ? 211.997 226.696 255.200 1.00 0.00  ? 1756 ILE A CG1   1 
ATOM   2399  C CG2   . ILE A 1 1756 ? 211.665 227.255 257.607 1.00 4.29  ? 1756 ILE A CG2   1 
ATOM   2400  C CD1   . ILE A 1 1756 ? 213.491 226.888 255.173 1.00 0.00  ? 1756 ILE A CD1   1 
ATOM   2401  N N     . ALA A 1 1757 ? 208.922 229.585 256.995 1.00 1.14  ? 1757 ALA A N     1 
ATOM   2402  C CA    . ALA A 1 1757 ? 208.217 230.358 258.008 1.00 0.00  ? 1757 ALA A CA    1 
ATOM   2403  C C     . ALA A 1 1757 ? 206.752 229.957 258.083 1.00 0.00  ? 1757 ALA A C     1 
ATOM   2404  O O     . ALA A 1 1757 ? 206.206 229.781 259.178 1.00 0.69  ? 1757 ALA A O     1 
ATOM   2405  C CB    . ALA A 1 1757 ? 208.354 231.851 257.718 1.00 1.19  ? 1757 ALA A CB    1 
ATOM   2406  N N     . TRP A 1 1758 ? 206.102 229.793 256.928 1.00 1.61  ? 1758 TRP A N     1 
ATOM   2407  C CA    . TRP A 1 1758 ? 204.705 229.372 256.924 1.00 0.74  ? 1758 TRP A CA    1 
ATOM   2408  C C     . TRP A 1 1758 ? 204.534 227.984 257.526 1.00 0.00  ? 1758 TRP A C     1 
ATOM   2409  O O     . TRP A 1 1758 ? 203.596 227.745 258.295 1.00 3.50  ? 1758 TRP A O     1 
ATOM   2410  C CB    . TRP A 1 1758 ? 204.158 229.394 255.504 1.00 0.00  ? 1758 TRP A CB    1 
ATOM   2411  C CG    . TRP A 1 1758 ? 202.788 228.830 255.399 1.00 0.00  ? 1758 TRP A CG    1 
ATOM   2412  C CD1   . TRP A 1 1758 ? 201.630 229.405 255.822 1.00 4.68  ? 1758 TRP A CD1   1 
ATOM   2413  C CD2   . TRP A 1 1758 ? 202.431 227.557 254.857 1.00 2.38  ? 1758 TRP A CD2   1 
ATOM   2414  N NE1   . TRP A 1 1758 ? 200.568 228.576 255.560 1.00 8.82  ? 1758 TRP A NE1   1 
ATOM   2415  C CE2   . TRP A 1 1758 ? 201.035 227.432 254.970 1.00 3.74  ? 1758 TRP A CE2   1 
ATOM   2416  C CE3   . TRP A 1 1758 ? 203.157 226.512 254.280 1.00 4.60  ? 1758 TRP A CE3   1 
ATOM   2417  C CZ2   . TRP A 1 1758 ? 200.351 226.306 254.527 1.00 1.20  ? 1758 TRP A CZ2   1 
ATOM   2418  C CZ3   . TRP A 1 1758 ? 202.477 225.397 253.842 1.00 2.21  ? 1758 TRP A CZ3   1 
ATOM   2419  C CH2   . TRP A 1 1758 ? 201.089 225.302 253.968 1.00 3.60  ? 1758 TRP A CH2   1 
ATOM   2420  N N     . SER A 1 1759 ? 205.419 227.050 257.173 1.00 0.00  ? 1759 SER A N     1 
ATOM   2421  C CA    . SER A 1 1759 ? 205.317 225.699 257.710 1.00 0.00  ? 1759 SER A CA    1 
ATOM   2422  C C     . SER A 1 1759 ? 205.457 225.697 259.226 1.00 5.90  ? 1759 SER A C     1 
ATOM   2423  O O     . SER A 1 1759 ? 204.650 225.076 259.931 1.00 11.36 ? 1759 SER A O     1 
ATOM   2424  C CB    . SER A 1 1759 ? 206.377 224.805 257.069 1.00 0.00  ? 1759 SER A CB    1 
ATOM   2425  O OG    . SER A 1 1759 ? 206.403 223.528 257.678 1.00 10.65 ? 1759 SER A OG    1 
ATOM   2426  N N     . GLU A 1 1760 ? 206.463 226.403 259.750 1.00 1.90  ? 1760 GLU A N     1 
ATOM   2427  C CA    . GLU A 1 1760 ? 206.636 226.458 261.197 1.00 2.66  ? 1760 GLU A CA    1 
ATOM   2428  C C     . GLU A 1 1760 ? 205.452 227.136 261.874 1.00 7.65  ? 1760 GLU A C     1 
ATOM   2429  O O     . GLU A 1 1760 ? 204.997 226.679 262.928 1.00 12.42 ? 1760 GLU A O     1 
ATOM   2430  C CB    . GLU A 1 1760 ? 207.938 227.169 261.560 1.00 5.00  ? 1760 GLU A CB    1 
ATOM   2431  C CG    . GLU A 1 1760 ? 209.187 226.520 260.998 1.00 9.18  ? 1760 GLU A CG    1 
ATOM   2432  C CD    . GLU A 1 1760 ? 210.390 227.437 261.057 1.00 13.73 ? 1760 GLU A CD    1 
ATOM   2433  O OE1   . GLU A 1 1760 ? 210.197 228.670 261.072 1.00 10.43 ? 1760 GLU A OE1   1 
ATOM   2434  O OE2   . GLU A 1 1760 ? 211.529 226.926 261.091 1.00 12.84 ? 1760 GLU A OE2   1 
ATOM   2435  N N     . ASN A 1 1761 ? 204.940 228.225 261.294 1.00 4.38  ? 1761 ASN A N     1 
ATOM   2436  C CA    . ASN A 1 1761 ? 203.807 228.912 261.905 1.00 0.85  ? 1761 ASN A CA    1 
ATOM   2437  C C     . ASN A 1 1761 ? 202.581 228.013 261.957 1.00 5.39  ? 1761 ASN A C     1 
ATOM   2438  O O     . ASN A 1 1761 ? 201.885 227.954 262.980 1.00 8.63  ? 1761 ASN A O     1 
ATOM   2439  C CB    . ASN A 1 1761 ? 203.497 230.197 261.142 1.00 0.00  ? 1761 ASN A CB    1 
ATOM   2440  C CG    . ASN A 1 1761 ? 204.587 231.236 261.284 1.00 1.45  ? 1761 ASN A CG    1 
ATOM   2441  O OD1   . ASN A 1 1761 ? 205.417 231.160 262.188 1.00 5.63  ? 1761 ASN A OD1   1 
ATOM   2442  N ND2   . ASN A 1 1761 ? 204.589 232.216 260.390 1.00 3.31  ? 1761 ASN A ND2   1 
ATOM   2443  N N     . VAL A 1 1762 ? 202.307 227.292 260.868 1.00 3.82  ? 1762 VAL A N     1 
ATOM   2444  C CA    . VAL A 1 1762 ? 201.151 226.404 260.847 1.00 3.30  ? 1762 VAL A CA    1 
ATOM   2445  C C     . VAL A 1 1762 ? 201.336 225.271 261.848 1.00 4.92  ? 1762 VAL A C     1 
ATOM   2446  O O     . VAL A 1 1762 ? 200.382 224.857 262.514 1.00 13.04 ? 1762 VAL A O     1 
ATOM   2447  C CB    . VAL A 1 1762 ? 200.902 225.874 259.423 1.00 0.00  ? 1762 VAL A CB    1 
ATOM   2448  C CG1   . VAL A 1 1762 ? 200.026 224.636 259.458 1.00 1.16  ? 1762 VAL A CG1   1 
ATOM   2449  C CG2   . VAL A 1 1762 ? 200.265 226.946 258.565 1.00 5.42  ? 1762 VAL A CG2   1 
ATOM   2450  N N     . GLU A 1 1763 ? 202.563 224.763 261.990 1.00 0.01  ? 1763 GLU A N     1 
ATOM   2451  C CA    . GLU A 1 1763 ? 202.782 223.677 262.939 1.00 2.18  ? 1763 GLU A CA    1 
ATOM   2452  C C     . GLU A 1 1763 ? 202.626 224.141 264.383 1.00 14.34 ? 1763 GLU A C     1 
ATOM   2453  O O     . GLU A 1 1763 ? 202.059 223.415 265.207 1.00 20.04 ? 1763 GLU A O     1 
ATOM   2454  C CB    . GLU A 1 1763 ? 204.149 223.042 262.714 1.00 2.64  ? 1763 GLU A CB    1 
ATOM   2455  C CG    . GLU A 1 1763 ? 204.213 222.277 261.418 1.00 5.75  ? 1763 GLU A CG    1 
ATOM   2456  C CD    . GLU A 1 1763 ? 205.550 221.630 261.185 1.00 9.93  ? 1763 GLU A CD    1 
ATOM   2457  O OE1   . GLU A 1 1763 ? 206.481 221.874 261.980 1.00 16.18 ? 1763 GLU A OE1   1 
ATOM   2458  O OE2   . GLU A 1 1763 ? 205.665 220.877 260.198 1.00 7.12  ? 1763 GLU A OE2   1 
ATOM   2459  N N     . THR A 1 1764 ? 203.120 225.336 264.720 1.00 8.08  ? 1764 THR A N     1 
ATOM   2460  C CA    . THR A 1 1764 ? 202.884 225.848 266.070 1.00 9.54  ? 1764 THR A CA    1 
ATOM   2461  C C     . THR A 1 1764 ? 201.399 226.083 266.320 1.00 10.46 ? 1764 THR A C     1 
ATOM   2462  O O     . THR A 1 1764 ? 200.888 225.770 267.403 1.00 10.70 ? 1764 THR A O     1 
ATOM   2463  C CB    . THR A 1 1764 ? 203.675 227.134 266.328 1.00 10.90 ? 1764 THR A CB    1 
ATOM   2464  O OG1   . THR A 1 1764 ? 203.040 228.241 265.674 1.00 11.91 ? 1764 THR A OG1   1 
ATOM   2465  C CG2   . THR A 1 1764 ? 205.123 227.000 265.890 1.00 3.98  ? 1764 THR A CG2   1 
ATOM   2466  N N     . ALA A 1 1765 ? 200.687 226.629 265.329 1.00 7.77  ? 1765 ALA A N     1 
ATOM   2467  C CA    . ALA A 1 1765 ? 199.251 226.827 265.489 1.00 9.86  ? 1765 ALA A CA    1 
ATOM   2468  C C     . ALA A 1 1765 ? 198.533 225.500 265.699 1.00 14.96 ? 1765 ALA A C     1 
ATOM   2469  O O     . ALA A 1 1765 ? 197.626 225.399 266.532 1.00 20.30 ? 1765 ALA A O     1 
ATOM   2470  C CB    . ALA A 1 1765 ? 198.682 227.561 264.277 1.00 8.61  ? 1765 ALA A CB    1 
ATOM   2471  N N     . LEU A 1 1766 ? 198.939 224.466 264.963 1.00 13.63 ? 1766 LEU A N     1 
ATOM   2472  C CA    . LEU A 1 1766 ? 198.290 223.166 265.083 1.00 8.84  ? 1766 LEU A CA    1 
ATOM   2473  C C     . LEU A 1 1766 ? 198.616 222.507 266.418 1.00 13.85 ? 1766 LEU A C     1 
ATOM   2474  O O     . LEU A 1 1766 ? 197.762 221.841 267.011 1.00 23.52 ? 1766 LEU A O     1 
ATOM   2475  C CB    . LEU A 1 1766 ? 198.711 222.272 263.918 1.00 10.45 ? 1766 LEU A CB    1 
ATOM   2476  C CG    . LEU A 1 1766 ? 197.852 222.369 262.655 1.00 8.95  ? 1766 LEU A CG    1 
ATOM   2477  C CD1   . LEU A 1 1766 ? 198.326 221.379 261.606 1.00 8.80  ? 1766 LEU A CD1   1 
ATOM   2478  C CD2   . LEU A 1 1766 ? 196.380 222.170 262.967 1.00 13.30 ? 1766 LEU A CD2   1 
ATOM   2479  N N     . SER A 1 1767 ? 199.846 222.678 266.908 1.00 11.02 ? 1767 SER A N     1 
ATOM   2480  C CA    . SER A 1 1767 ? 200.193 222.146 268.222 1.00 16.79 ? 1767 SER A CA    1 
ATOM   2481  C C     . SER A 1 1767 ? 199.395 222.836 269.321 1.00 16.05 ? 1767 SER A C     1 
ATOM   2482  O O     . SER A 1 1767 ? 198.929 222.186 270.264 1.00 17.15 ? 1767 SER A O     1 
ATOM   2483  C CB    . SER A 1 1767 ? 201.692 222.293 268.475 1.00 17.20 ? 1767 SER A CB    1 
ATOM   2484  O OG    . SER A 1 1767 ? 202.008 223.606 268.903 1.00 22.43 ? 1767 SER A OG    1 
ATOM   2485  N N     . SER A 1 1768 ? 199.232 224.158 269.220 1.00 15.84 ? 1768 SER A N     1 
ATOM   2486  C CA    . SER A 1 1768 ? 198.400 224.869 270.186 1.00 17.92 ? 1768 SER A CA    1 
ATOM   2487  C C     . SER A 1 1768 ? 196.945 224.425 270.090 1.00 21.24 ? 1768 SER A C     1 
ATOM   2488  O O     . SER A 1 1768 ? 196.249 224.332 271.108 1.00 25.20 ? 1768 SER A O     1 
ATOM   2489  C CB    . SER A 1 1768 ? 198.522 226.376 269.975 1.00 18.84 ? 1768 SER A CB    1 
ATOM   2490  O OG    . SER A 1 1768 ? 197.984 226.756 268.724 1.00 16.37 ? 1768 SER A OG    1 
ATOM   2491  N N     . MET A 1 1769 ? 196.465 224.155 268.873 1.00 18.86 ? 1769 MET A N     1 
ATOM   2492  C CA    . MET A 1 1769 ? 195.122 223.607 268.706 1.00 19.76 ? 1769 MET A CA    1 
ATOM   2493  C C     . MET A 1 1769 ? 194.986 222.260 269.401 1.00 22.90 ? 1769 MET A C     1 
ATOM   2494  O O     . MET A 1 1769 ? 193.981 221.993 270.068 1.00 22.76 ? 1769 MET A O     1 
ATOM   2495  C CB    . MET A 1 1769 ? 194.795 223.458 267.221 1.00 18.51 ? 1769 MET A CB    1 
ATOM   2496  C CG    . MET A 1 1769 ? 194.383 224.731 266.511 1.00 19.18 ? 1769 MET A CG    1 
ATOM   2497  S SD    . MET A 1 1769 ? 193.135 224.359 265.265 1.00 31.89 ? 1769 MET A SD    1 
ATOM   2498  C CE    . MET A 1 1769 ? 192.557 225.994 264.842 1.00 23.78 ? 1769 MET A CE    1 
ATOM   2499  N N     . GLY A 1 1770 ? 195.983 221.391 269.239 1.00 21.48 ? 1770 GLY A N     1 
ATOM   2500  C CA    . GLY A 1 1770 ? 195.930 220.089 269.883 1.00 20.70 ? 1770 GLY A CA    1 
ATOM   2501  C C     . GLY A 1 1770 ? 195.971 220.185 271.396 1.00 27.90 ? 1770 GLY A C     1 
ATOM   2502  O O     . GLY A 1 1770 ? 195.254 219.463 272.093 1.00 29.75 ? 1770 GLY A O     1 
ATOM   2503  N N     . GLY A 1 1771 ? 196.808 221.075 271.922 1.00 33.59 ? 1771 GLY A N     1 
ATOM   2504  C CA    . GLY A 1 1771 ? 196.909 221.257 273.356 1.00 30.95 ? 1771 GLY A CA    1 
ATOM   2505  C C     . GLY A 1 1771 ? 195.701 221.926 273.981 1.00 30.29 ? 1771 GLY A C     1 
ATOM   2506  O O     . GLY A 1 1771 ? 194.960 221.297 274.743 1.00 27.61 ? 1771 GLY A O     1 
ATOM   2507  N N     . GLY A 1 1772 ? 195.492 223.206 273.668 1.00 31.11 ? 1772 GLY A N     1 
ATOM   2508  C CA    . GLY A 1 1772 ? 194.390 223.935 274.277 1.00 35.31 ? 1772 GLY A CA    1 
ATOM   2509  C C     . GLY A 1 1772 ? 193.032 223.485 273.772 1.00 38.00 ? 1772 GLY A C     1 
ATOM   2510  O O     . GLY A 1 1772 ? 192.098 223.290 274.555 1.00 34.53 ? 1772 GLY A O     1 
ATOM   2511  N N     . GLY A 1 1773 ? 192.902 223.315 272.458 1.00 39.78 ? 1773 GLY A N     1 
ATOM   2512  C CA    . GLY A 1 1773 ? 191.622 222.953 271.882 1.00 37.55 ? 1773 GLY A CA    1 
ATOM   2513  C C     . GLY A 1 1773 ? 190.603 224.068 271.851 1.00 38.19 ? 1773 GLY A C     1 
ATOM   2514  O O     . GLY A 1 1773 ? 189.409 223.798 271.700 1.00 35.54 ? 1773 GLY A O     1 
ATOM   2515  N N     . ASP A 1 1774 ? 191.041 225.317 271.985 1.00 37.55 ? 1774 ASP A N     1 
ATOM   2516  C CA    . ASP A 1 1774 ? 190.153 226.469 272.029 1.00 38.61 ? 1774 ASP A CA    1 
ATOM   2517  C C     . ASP A 1 1774 ? 190.600 227.511 271.013 1.00 39.70 ? 1774 ASP A C     1 
ATOM   2518  O O     . ASP A 1 1774 ? 191.789 227.606 270.689 1.00 37.55 ? 1774 ASP A O     1 
ATOM   2519  C CB    . ASP A 1 1774 ? 190.119 227.088 273.432 1.00 36.45 ? 1774 ASP A CB    1 
ATOM   2520  C CG    . ASP A 1 1774 ? 189.607 226.124 274.483 1.00 37.19 ? 1774 ASP A CG    1 
ATOM   2521  O OD1   . ASP A 1 1774 ? 188.813 225.226 274.133 1.00 36.79 ? 1774 ASP A OD1   1 
ATOM   2522  O OD2   . ASP A 1 1774 ? 189.998 226.265 275.661 1.00 39.58 ? 1774 ASP A OD2   1 
ATOM   2523  N N     . ALA A 1 1775 ? 189.640 228.282 270.519 1.00 32.08 ? 1775 ALA A N     1 
ATOM   2524  C CA    . ALA A 1 1775 ? 189.863 229.369 269.561 1.00 28.46 ? 1775 ALA A CA    1 
ATOM   2525  C C     . ALA A 1 1775 ? 190.561 228.805 268.320 1.00 30.88 ? 1775 ALA A C     1 
ATOM   2526  O O     . ALA A 1 1775 ? 190.440 227.615 268.010 1.00 27.34 ? 1775 ALA A O     1 
ATOM   2527  C CB    . ALA A 1 1775 ? 190.602 230.505 270.246 1.00 29.61 ? 1775 ALA A CB    1 
ATOM   2528  N N     . ALA A 1 1776 ? 191.297 229.649 267.597 1.00 29.19 ? 1776 ALA A N     1 
ATOM   2529  C CA    . ALA A 1 1776 ? 191.945 229.207 266.370 1.00 24.55 ? 1776 ALA A CA    1 
ATOM   2530  C C     . ALA A 1 1776 ? 193.128 230.096 266.005 1.00 19.87 ? 1776 ALA A C     1 
ATOM   2531  O O     . ALA A 1 1776 ? 192.954 231.107 265.313 1.00 13.69 ? 1776 ALA A O     1 
ATOM   2532  C CB    . ALA A 1 1776 ? 190.938 229.181 265.220 1.00 21.27 ? 1776 ALA A CB    1 
ATOM   2533  N N     . PRO A 1 1777 ? 194.337 229.769 266.466 1.00 19.50 ? 1777 PRO A N     1 
ATOM   2534  C CA    . PRO A 1 1777 ? 195.530 230.453 265.939 1.00 17.16 ? 1777 PRO A CA    1 
ATOM   2535  C C     . PRO A 1 1777 ? 195.728 230.255 264.445 1.00 17.64 ? 1777 PRO A C     1 
ATOM   2536  O O     . PRO A 1 1777 ? 196.421 231.065 263.815 1.00 16.78 ? 1777 PRO A O     1 
ATOM   2537  C CB    . PRO A 1 1777 ? 196.686 229.831 266.736 1.00 15.63 ? 1777 PRO A CB    1 
ATOM   2538  C CG    . PRO A 1 1777 ? 196.064 229.009 267.818 1.00 19.85 ? 1777 PRO A CG    1 
ATOM   2539  C CD    . PRO A 1 1777 ? 194.583 229.143 267.773 1.00 21.21 ? 1777 PRO A CD    1 
ATOM   2540  N N     . LEU A 1 1778 ? 195.164 229.192 263.862 1.00 15.46 ? 1778 LEU A N     1 
ATOM   2541  C CA    . LEU A 1 1778 ? 195.210 229.033 262.412 1.00 10.34 ? 1778 LEU A CA    1 
ATOM   2542  C C     . LEU A 1 1778 ? 194.536 230.198 261.704 1.00 9.38  ? 1778 LEU A C     1 
ATOM   2543  O O     . LEU A 1 1778 ? 194.951 230.581 260.604 1.00 15.52 ? 1778 LEU A O     1 
ATOM   2544  C CB    . LEU A 1 1778 ? 194.554 227.716 262.002 1.00 13.13 ? 1778 LEU A CB    1 
ATOM   2545  C CG    . LEU A 1 1778 ? 195.453 226.482 261.936 1.00 10.86 ? 1778 LEU A CG    1 
ATOM   2546  C CD1   . LEU A 1 1778 ? 194.735 225.353 261.221 1.00 10.32 ? 1778 LEU A CD1   1 
ATOM   2547  C CD2   . LEU A 1 1778 ? 196.756 226.812 261.234 1.00 9.50  ? 1778 LEU A CD2   1 
ATOM   2548  N N     . HIS A 1 1779 ? 193.498 230.773 262.313 1.00 10.02 ? 1779 HIS A N     1 
ATOM   2549  C CA    . HIS A 1 1779 ? 192.902 231.981 261.760 1.00 10.00 ? 1779 HIS A CA    1 
ATOM   2550  C C     . HIS A 1 1779 ? 193.906 233.125 261.754 1.00 12.80 ? 1779 HIS A C     1 
ATOM   2551  O O     . HIS A 1 1779 ? 193.957 233.912 260.803 1.00 11.43 ? 1779 HIS A O     1 
ATOM   2552  C CB    . HIS A 1 1779 ? 191.653 232.359 262.553 1.00 12.44 ? 1779 HIS A CB    1 
ATOM   2553  C CG    . HIS A 1 1779 ? 190.392 231.762 262.013 1.00 14.10 ? 1779 HIS A CG    1 
ATOM   2554  N ND1   . HIS A 1 1779 ? 189.845 230.601 262.514 1.00 9.78  ? 1779 HIS A ND1   1 
ATOM   2555  C CD2   . HIS A 1 1779 ? 189.571 232.164 261.014 1.00 16.52 ? 1779 HIS A CD2   1 
ATOM   2556  C CE1   . HIS A 1 1779 ? 188.741 230.313 261.848 1.00 11.22 ? 1779 HIS A CE1   1 
ATOM   2557  N NE2   . HIS A 1 1779 ? 188.552 231.246 260.933 1.00 16.97 ? 1779 HIS A NE2   1 
ATOM   2558  N N     . SER A 1 1780 ? 194.720 233.228 262.807 1.00 11.22 ? 1780 SER A N     1 
ATOM   2559  C CA    . SER A 1 1780 ? 195.764 234.247 262.840 1.00 3.46  ? 1780 SER A CA    1 
ATOM   2560  C C     . SER A 1 1780 ? 196.815 233.999 261.765 1.00 8.52  ? 1780 SER A C     1 
ATOM   2561  O O     . SER A 1 1780 ? 197.312 234.946 261.144 1.00 14.76 ? 1780 SER A O     1 
ATOM   2562  C CB    . SER A 1 1780 ? 196.410 234.290 264.224 1.00 9.35  ? 1780 SER A CB    1 
ATOM   2563  O OG    . SER A 1 1780 ? 197.461 233.348 264.325 1.00 8.72  ? 1780 SER A OG    1 
ATOM   2564  N N     . VAL A 1 1781 ? 197.177 232.734 261.539 1.00 12.95 ? 1781 VAL A N     1 
ATOM   2565  C CA    . VAL A 1 1781 ? 198.143 232.414 260.488 1.00 5.58  ? 1781 VAL A CA    1 
ATOM   2566  C C     . VAL A 1 1781 ? 197.588 232.794 259.120 1.00 0.74  ? 1781 VAL A C     1 
ATOM   2567  O O     . VAL A 1 1781 ? 198.289 233.384 258.286 1.00 9.02  ? 1781 VAL A O     1 
ATOM   2568  C CB    . VAL A 1 1781 ? 198.528 230.924 260.549 1.00 6.31  ? 1781 VAL A CB    1 
ATOM   2569  C CG1   . VAL A 1 1781 ? 199.367 230.540 259.345 1.00 1.88  ? 1781 VAL A CG1   1 
ATOM   2570  C CG2   . VAL A 1 1781 ? 199.278 230.625 261.835 1.00 9.18  ? 1781 VAL A CG2   1 
ATOM   2571  N N     . LEU A 1 1782 ? 196.319 232.468 258.872 1.00 0.00  ? 1782 LEU A N     1 
ATOM   2572  C CA    . LEU A 1 1782 ? 195.688 232.850 257.614 1.00 1.52  ? 1782 LEU A CA    1 
ATOM   2573  C C     . LEU A 1 1782 ? 195.633 234.364 257.464 1.00 4.55  ? 1782 LEU A C     1 
ATOM   2574  O O     . LEU A 1 1782 ? 195.866 234.893 256.372 1.00 9.03  ? 1782 LEU A O     1 
ATOM   2575  C CB    . LEU A 1 1782 ? 194.284 232.253 257.525 1.00 8.35  ? 1782 LEU A CB    1 
ATOM   2576  C CG    . LEU A 1 1782 ? 193.476 232.621 256.280 1.00 7.36  ? 1782 LEU A CG    1 
ATOM   2577  C CD1   . LEU A 1 1782 ? 194.192 232.170 255.022 1.00 6.13  ? 1782 LEU A CD1   1 
ATOM   2578  C CD2   . LEU A 1 1782 ? 192.079 232.029 256.346 1.00 9.51  ? 1782 LEU A CD2   1 
ATOM   2579  N N     . SER A 1 1783 ? 195.319 235.078 258.547 1.00 4.37  ? 1783 SER A N     1 
ATOM   2580  C CA    . SER A 1 1783 ? 195.271 236.535 258.488 1.00 4.06  ? 1783 SER A CA    1 
ATOM   2581  C C     . SER A 1 1783 ? 196.642 237.121 258.177 1.00 5.76  ? 1783 SER A C     1 
ATOM   2582  O O     . SER A 1 1783 ? 196.755 238.071 257.396 1.00 12.32 ? 1783 SER A O     1 
ATOM   2583  C CB    . SER A 1 1783 ? 194.734 237.094 259.805 1.00 9.32  ? 1783 SER A CB    1 
ATOM   2584  O OG    . SER A 1 1783 ? 193.436 236.597 260.076 1.00 11.35 ? 1783 SER A OG    1 
ATOM   2585  N N     . ASN A 1 1784 ? 197.695 236.572 258.784 1.00 3.90  ? 1784 ASN A N     1 
ATOM   2586  C CA    . ASN A 1 1784 ? 199.045 237.048 258.498 1.00 6.89  ? 1784 ASN A CA    1 
ATOM   2587  C C     . ASN A 1 1784 ? 199.420 236.797 257.043 1.00 1.74  ? 1784 ASN A C     1 
ATOM   2588  O O     . ASN A 1 1784 ? 200.023 237.658 256.388 1.00 2.17  ? 1784 ASN A O     1 
ATOM   2589  C CB    . ASN A 1 1784 ? 200.047 236.373 259.433 1.00 6.57  ? 1784 ASN A CB    1 
ATOM   2590  C CG    . ASN A 1 1784 ? 201.481 236.730 259.106 1.00 9.88  ? 1784 ASN A CG    1 
ATOM   2591  O OD1   . ASN A 1 1784 ? 201.771 237.839 258.660 1.00 9.40  ? 1784 ASN A OD1   1 
ATOM   2592  N ND2   . ASN A 1 1784 ? 202.387 235.788 259.324 1.00 9.69  ? 1784 ASN A ND2   1 
ATOM   2593  N N     . VAL A 1 1785 ? 199.077 235.618 256.521 1.00 5.70  ? 1785 VAL A N     1 
ATOM   2594  C CA    . VAL A 1 1785 ? 199.371 235.321 255.122 1.00 4.54  ? 1785 VAL A CA    1 
ATOM   2595  C C     . VAL A 1 1785 ? 198.593 236.259 254.208 1.00 4.76  ? 1785 VAL A C     1 
ATOM   2596  O O     . VAL A 1 1785 ? 199.104 236.711 253.179 1.00 9.68  ? 1785 VAL A O     1 
ATOM   2597  C CB    . VAL A 1 1785 ? 199.078 233.840 254.816 1.00 1.07  ? 1785 VAL A CB    1 
ATOM   2598  C CG1   . VAL A 1 1785 ? 198.875 233.625 253.327 1.00 0.00  ? 1785 VAL A CG1   1 
ATOM   2599  C CG2   . VAL A 1 1785 ? 200.210 232.960 255.329 1.00 2.93  ? 1785 VAL A CG2   1 
ATOM   2600  N N     . GLU A 1 1786 ? 197.352 236.582 254.578 1.00 8.77  ? 1786 GLU A N     1 
ATOM   2601  C CA    . GLU A 1 1786 ? 196.556 237.518 253.790 1.00 2.23  ? 1786 GLU A CA    1 
ATOM   2602  C C     . GLU A 1 1786 ? 197.151 238.922 253.818 1.00 1.51  ? 1786 GLU A C     1 
ATOM   2603  O O     . GLU A 1 1786 ? 197.128 239.629 252.806 1.00 2.46  ? 1786 GLU A O     1 
ATOM   2604  C CB    . GLU A 1 1786 ? 195.117 237.532 254.300 1.00 3.92  ? 1786 GLU A CB    1 
ATOM   2605  C CG    . GLU A 1 1786 ? 194.278 236.369 253.804 1.00 6.12  ? 1786 GLU A CG    1 
ATOM   2606  C CD    . GLU A 1 1786 ? 192.944 236.276 254.509 1.00 11.15 ? 1786 GLU A CD    1 
ATOM   2607  O OE1   . GLU A 1 1786 ? 192.782 236.927 255.562 1.00 8.43  ? 1786 GLU A OE1   1 
ATOM   2608  O OE2   . GLU A 1 1786 ? 192.057 235.552 254.012 1.00 9.58  ? 1786 GLU A OE2   1 
ATOM   2609  N N     . VAL A 1 1787 ? 197.673 239.349 254.970 1.00 6.71  ? 1787 VAL A N     1 
ATOM   2610  C CA    . VAL A 1 1787 ? 198.341 240.648 255.052 1.00 5.53  ? 1787 VAL A CA    1 
ATOM   2611  C C     . VAL A 1 1787 ? 199.579 240.673 254.164 1.00 5.10  ? 1787 VAL A C     1 
ATOM   2612  O O     . VAL A 1 1787 ? 199.825 241.647 253.438 1.00 4.99  ? 1787 VAL A O     1 
ATOM   2613  C CB    . VAL A 1 1787 ? 198.689 240.984 256.514 1.00 2.69  ? 1787 VAL A CB    1 
ATOM   2614  C CG1   . VAL A 1 1787 ? 199.479 242.275 256.582 1.00 6.97  ? 1787 VAL A CG1   1 
ATOM   2615  C CG2   . VAL A 1 1787 ? 197.426 241.116 257.340 1.00 2.88  ? 1787 VAL A CG2   1 
ATOM   2616  N N     . THR A 1 1788 ? 200.381 239.607 254.210 1.00 3.29  ? 1788 THR A N     1 
ATOM   2617  C CA    . THR A 1 1788 ? 201.560 239.538 253.352 1.00 0.00  ? 1788 THR A CA    1 
ATOM   2618  C C     . THR A 1 1788 ? 201.163 239.548 251.881 1.00 0.00  ? 1788 THR A C     1 
ATOM   2619  O O     . THR A 1 1788 ? 201.817 240.194 251.055 1.00 6.66  ? 1788 THR A O     1 
ATOM   2620  C CB    . THR A 1 1788 ? 202.379 238.291 253.683 1.00 1.89  ? 1788 THR A CB    1 
ATOM   2621  O OG1   . THR A 1 1788 ? 202.900 238.399 255.012 1.00 10.73 ? 1788 THR A OG1   1 
ATOM   2622  C CG2   . THR A 1 1788 ? 203.536 238.144 252.717 1.00 4.94  ? 1788 THR A CG2   1 
ATOM   2623  N N     . LEU A 1 1789 ? 200.081 238.846 251.540 1.00 7.30  ? 1789 LEU A N     1 
ATOM   2624  C CA    . LEU A 1 1789 ? 199.576 238.843 250.171 1.00 2.10  ? 1789 LEU A CA    1 
ATOM   2625  C C     . LEU A 1 1789 ? 199.120 240.230 249.740 1.00 1.49  ? 1789 LEU A C     1 
ATOM   2626  O O     . LEU A 1 1789 ? 199.354 240.638 248.599 1.00 5.19  ? 1789 LEU A O     1 
ATOM   2627  C CB    . LEU A 1 1789 ? 198.435 237.835 250.049 1.00 3.93  ? 1789 LEU A CB    1 
ATOM   2628  C CG    . LEU A 1 1789 ? 198.225 237.146 248.703 1.00 4.68  ? 1789 LEU A CG    1 
ATOM   2629  C CD1   . LEU A 1 1789 ? 199.509 236.530 248.208 1.00 2.96  ? 1789 LEU A CD1   1 
ATOM   2630  C CD2   . LEU A 1 1789 ? 197.148 236.084 248.839 1.00 0.18  ? 1789 LEU A CD2   1 
ATOM   2631  N N     . ASN A 1 1790 ? 198.452 240.962 250.633 1.00 2.55  ? 1790 ASN A N     1 
ATOM   2632  C CA    . ASN A 1 1790 ? 198.027 242.321 250.310 1.00 2.27  ? 1790 ASN A CA    1 
ATOM   2633  C C     . ASN A 1 1790 ? 199.226 243.231 250.079 1.00 4.11  ? 1790 ASN A C     1 
ATOM   2634  O O     . ASN A 1 1790 ? 199.221 244.057 249.158 1.00 5.80  ? 1790 ASN A O     1 
ATOM   2635  C CB    . ASN A 1 1790 ? 197.142 242.870 251.428 1.00 4.57  ? 1790 ASN A CB    1 
ATOM   2636  C CG    . ASN A 1 1790 ? 196.402 244.127 251.020 1.00 10.12 ? 1790 ASN A CG    1 
ATOM   2637  O OD1   . ASN A 1 1790 ? 196.133 244.347 249.840 1.00 9.74  ? 1790 ASN A OD1   1 
ATOM   2638  N ND2   . ASN A 1 1790 ? 196.067 244.959 251.999 1.00 9.39  ? 1790 ASN A ND2   1 
ATOM   2639  N N     . VAL A 1 1791 ? 200.262 243.095 250.908 1.00 5.97  ? 1791 VAL A N     1 
ATOM   2640  C CA    . VAL A 1 1791 ? 201.475 243.889 250.719 1.00 3.67  ? 1791 VAL A CA    1 
ATOM   2641  C C     . VAL A 1 1791 ? 202.136 243.551 249.388 1.00 0.00  ? 1791 VAL A C     1 
ATOM   2642  O O     . VAL A 1 1791 ? 202.603 244.440 248.666 1.00 6.67  ? 1791 VAL A O     1 
ATOM   2643  C CB    . VAL A 1 1791 ? 202.438 243.683 251.902 1.00 0.97  ? 1791 VAL A CB    1 
ATOM   2644  C CG1   . VAL A 1 1791 ? 203.748 244.408 251.657 1.00 1.82  ? 1791 VAL A CG1   1 
ATOM   2645  C CG2   . VAL A 1 1791 ? 201.798 244.174 253.184 1.00 2.76  ? 1791 VAL A CG2   1 
ATOM   2646  N N     . LEU A 1 1792 ? 202.196 242.262 249.048 1.00 1.55  ? 1792 LEU A N     1 
ATOM   2647  C CA    . LEU A 1 1792 ? 202.800 241.851 247.783 1.00 0.11  ? 1792 LEU A CA    1 
ATOM   2648  C C     . LEU A 1 1792 ? 202.002 242.374 246.594 1.00 0.57  ? 1792 LEU A C     1 
ATOM   2649  O O     . LEU A 1 1792 ? 202.575 242.845 245.606 1.00 6.73  ? 1792 LEU A O     1 
ATOM   2650  C CB    . LEU A 1 1792 ? 202.907 240.327 247.729 1.00 0.72  ? 1792 LEU A CB    1 
ATOM   2651  C CG    . LEU A 1 1792 ? 203.917 239.653 248.657 1.00 2.31  ? 1792 LEU A CG    1 
ATOM   2652  C CD1   . LEU A 1 1792 ? 203.626 238.167 248.753 1.00 5.17  ? 1792 LEU A CD1   1 
ATOM   2653  C CD2   . LEU A 1 1792 ? 205.335 239.885 248.190 1.00 2.53  ? 1792 LEU A CD2   1 
ATOM   2654  N N     . ALA A 1 1793 ? 200.672 242.295 246.672 1.00 3.94  ? 1793 ALA A N     1 
ATOM   2655  C CA    . ALA A 1 1793 ? 199.831 242.728 245.562 1.00 2.00  ? 1793 ALA A CA    1 
ATOM   2656  C C     . ALA A 1 1793 ? 199.834 244.241 245.405 1.00 7.20  ? 1793 ALA A C     1 
ATOM   2657  O O     . ALA A 1 1793 ? 199.670 244.745 244.289 1.00 11.93 ? 1793 ALA A O     1 
ATOM   2658  C CB    . ALA A 1 1793 ? 198.403 242.220 245.754 1.00 4.83  ? 1793 ALA A CB    1 
ATOM   2659  N N     . ASP A 1 1794 ? 199.995 244.982 246.500 1.00 5.13  ? 1794 ASP A N     1 
ATOM   2660  C CA    . ASP A 1 1794 ? 200.161 246.424 246.395 1.00 1.40  ? 1794 ASP A CA    1 
ATOM   2661  C C     . ASP A 1 1794 ? 201.540 246.820 245.889 1.00 2.31  ? 1794 ASP A C     1 
ATOM   2662  O O     . ASP A 1 1794 ? 201.695 247.927 245.365 1.00 10.75 ? 1794 ASP A O     1 
ATOM   2663  C CB    . ASP A 1 1794 ? 199.904 247.086 247.751 1.00 7.19  ? 1794 ASP A CB    1 
ATOM   2664  C CG    . ASP A 1 1794 ? 198.452 247.008 248.171 1.00 11.14 ? 1794 ASP A CG    1 
ATOM   2665  O OD1   . ASP A 1 1794 ? 197.577 246.972 247.281 1.00 13.82 ? 1794 ASP A OD1   1 
ATOM   2666  O OD2   . ASP A 1 1794 ? 198.185 246.986 249.390 1.00 8.59  ? 1794 ASP A OD2   1 
ATOM   2667  N N     . SER A 1 1795 ? 202.536 245.948 246.026 1.00 5.12  ? 1795 SER A N     1 
ATOM   2668  C CA    . SER A 1 1795 ? 203.901 246.239 245.616 1.00 3.90  ? 1795 SER A CA    1 
ATOM   2669  C C     . SER A 1 1795 ? 204.199 245.809 244.188 1.00 4.62  ? 1795 SER A C     1 
ATOM   2670  O O     . SER A 1 1795 ? 205.284 246.109 243.680 1.00 9.36  ? 1795 SER A O     1 
ATOM   2671  C CB    . SER A 1 1795 ? 204.890 245.565 246.570 1.00 3.83  ? 1795 SER A CB    1 
ATOM   2672  O OG    . SER A 1 1795 ? 206.226 245.809 246.170 1.00 11.11 ? 1795 SER A OG    1 
ATOM   2673  N N     . VAL A 1 1796 ? 203.273 245.119 243.528 1.00 8.34  ? 1796 VAL A N     1 
ATOM   2674  C CA    . VAL A 1 1796 ? 203.462 244.698 242.143 1.00 7.14  ? 1796 VAL A CA    1 
ATOM   2675  C C     . VAL A 1 1796 ? 202.854 245.682 241.157 1.00 7.65  ? 1796 VAL A C     1 
ATOM   2676  O O     . VAL A 1 1796 ? 203.257 245.690 239.981 1.00 11.47 ? 1796 VAL A O     1 
ATOM   2677  C CB    . VAL A 1 1796 ? 202.902 243.278 241.904 1.00 2.79  ? 1796 VAL A CB    1 
ATOM   2678  C CG1   . VAL A 1 1796 ? 201.393 243.255 242.062 1.00 3.51  ? 1796 VAL A CG1   1 
ATOM   2679  C CG2   . VAL A 1 1796 ? 203.332 242.724 240.551 1.00 4.11  ? 1796 VAL A CG2   1 
ATOM   2680  N N     . LEU A 1 1797 ? 201.924 246.532 241.596 1.00 6.80  ? 1797 LEU A N     1 
ATOM   2681  C CA    . LEU A 1 1797 ? 201.374 247.560 240.724 1.00 5.71  ? 1797 LEU A CA    1 
ATOM   2682  C C     . LEU A 1 1797 ? 202.398 248.627 240.364 1.00 7.26  ? 1797 LEU A C     1 
ATOM   2683  O O     . LEU A 1 1797 ? 202.387 249.121 239.233 1.00 5.13  ? 1797 LEU A O     1 
ATOM   2684  C CB    . LEU A 1 1797 ? 200.163 248.215 241.386 1.00 9.32  ? 1797 LEU A CB    1 
ATOM   2685  C CG    . LEU A 1 1797 ? 198.968 247.307 241.665 1.00 8.07  ? 1797 LEU A CG    1 
ATOM   2686  C CD1   . LEU A 1 1797 ? 198.073 247.915 242.730 1.00 6.82  ? 1797 LEU A CD1   1 
ATOM   2687  C CD2   . LEU A 1 1797 ? 198.194 247.056 240.388 1.00 8.02  ? 1797 LEU A CD2   1 
ATOM   2688  N N     . MET A 1 1798 ? 203.283 248.987 241.287 1.00 8.40  ? 1798 MET A N     1 
ATOM   2689  C CA    . MET A 1 1798 ? 204.219 250.077 241.075 1.00 12.77 ? 1798 MET A CA    1 
ATOM   2690  C C     . MET A 1 1798 ? 205.440 249.580 240.303 1.00 12.63 ? 1798 MET A C     1 
ATOM   2691  O O     . MET A 1 1798 ? 205.524 248.416 239.904 1.00 12.14 ? 1798 MET A O     1 
ATOM   2692  C CB    . MET A 1 1798 ? 204.593 250.708 242.417 1.00 10.54 ? 1798 MET A CB    1 
ATOM   2693  C CG    . MET A 1 1798 ? 205.053 249.722 243.468 1.00 7.08  ? 1798 MET A CG    1 
ATOM   2694  S SD    . MET A 1 1798 ? 205.055 250.439 245.121 1.00 14.69 ? 1798 MET A SD    1 
ATOM   2695  C CE    . MET A 1 1798 ? 203.342 250.940 245.265 1.00 10.77 ? 1798 MET A CE    1 
ATOM   2696  N N     . GLU A 1 1799 ? 206.398 250.476 240.079 1.00 13.37 ? 1799 GLU A N     1 
ATOM   2697  C CA    . GLU A 1 1799 ? 207.561 250.189 239.250 1.00 11.66 ? 1799 GLU A CA    1 
ATOM   2698  C C     . GLU A 1 1799 ? 208.572 249.377 240.050 1.00 11.99 ? 1799 GLU A C     1 
ATOM   2699  O O     . GLU A 1 1799 ? 209.011 249.807 241.121 1.00 16.61 ? 1799 GLU A O     1 
ATOM   2700  C CB    . GLU A 1 1799 ? 208.199 251.484 238.753 1.00 16.00 ? 1799 GLU A CB    1 
ATOM   2701  C CG    . GLU A 1 1799 ? 207.628 251.996 237.447 1.00 21.05 ? 1799 GLU A CG    1 
ATOM   2702  C CD    . GLU A 1 1799 ? 206.393 252.846 237.659 1.00 22.50 ? 1799 GLU A CD    1 
ATOM   2703  O OE1   . GLU A 1 1799 ? 205.721 253.176 236.664 1.00 17.65 ? 1799 GLU A OE1   1 
ATOM   2704  O OE2   . GLU A 1 1799 ? 206.096 253.185 238.824 1.00 18.85 ? 1799 GLU A OE2   1 
ATOM   2705  N N     . GLN A 1 1800 ? 208.943 248.214 239.527 1.00 11.66 ? 1800 GLN A N     1 
ATOM   2706  C CA    . GLN A 1 1800 ? 209.920 247.350 240.167 1.00 10.41 ? 1800 GLN A CA    1 
ATOM   2707  C C     . GLN A 1 1800 ? 210.966 246.906 239.159 1.00 8.70  ? 1800 GLN A C     1 
ATOM   2708  O O     . GLN A 1 1800 ? 210.683 246.816 237.960 1.00 2.64  ? 1800 GLN A O     1 
ATOM   2709  C CB    . GLN A 1 1800 ? 209.256 246.110 240.786 1.00 2.08  ? 1800 GLN A CB    1 
ATOM   2710  C CG    . GLN A 1 1800 ? 207.989 246.396 241.566 1.00 2.98  ? 1800 GLN A CG    1 
ATOM   2711  C CD    . GLN A 1 1800 ? 208.277 246.856 242.977 1.00 8.76  ? 1800 GLN A CD    1 
ATOM   2712  O OE1   . GLN A 1 1800 ? 209.421 246.829 243.428 1.00 12.66 ? 1800 GLN A OE1   1 
ATOM   2713  N NE2   . GLN A 1 1800 ? 207.241 247.288 243.682 1.00 8.75  ? 1800 GLN A NE2   1 
ATOM   2714  N N     . PRO A 1 1801 ? 212.188 246.636 239.615 1.00 8.56  ? 1801 PRO A N     1 
ATOM   2715  C CA    . PRO A 1 1801 ? 213.169 246.016 238.735 1.00 3.95  ? 1801 PRO A CA    1 
ATOM   2716  C C     . PRO A 1 1801 ? 212.708 244.633 238.323 1.00 6.58  ? 1801 PRO A C     1 
ATOM   2717  O O     . PRO A 1 1801 ? 211.951 243.968 239.056 1.00 8.70  ? 1801 PRO A O     1 
ATOM   2718  C CB    . PRO A 1 1801 ? 214.433 245.956 239.603 1.00 9.33  ? 1801 PRO A CB    1 
ATOM   2719  C CG    . PRO A 1 1801 ? 214.238 247.010 240.632 1.00 6.31  ? 1801 PRO A CG    1 
ATOM   2720  C CD    . PRO A 1 1801 ? 212.771 247.030 240.908 1.00 6.84  ? 1801 PRO A CD    1 
ATOM   2721  N N     . PRO A 1 1802 ? 213.122 244.163 237.143 1.00 6.62  ? 1802 PRO A N     1 
ATOM   2722  C CA    . PRO A 1 1802 ? 212.638 242.851 236.673 1.00 5.19  ? 1802 PRO A CA    1 
ATOM   2723  C C     . PRO A 1 1802 ? 212.972 241.698 237.606 1.00 4.03  ? 1802 PRO A C     1 
ATOM   2724  O O     . PRO A 1 1802 ? 212.141 240.799 237.789 1.00 2.85  ? 1802 PRO A O     1 
ATOM   2725  C CB    . PRO A 1 1802 ? 213.322 242.701 235.306 1.00 8.11  ? 1802 PRO A CB    1 
ATOM   2726  C CG    . PRO A 1 1802 ? 214.502 243.615 235.362 1.00 4.64  ? 1802 PRO A CG    1 
ATOM   2727  C CD    . PRO A 1 1802 ? 214.075 244.774 236.203 1.00 0.91  ? 1802 PRO A CD    1 
ATOM   2728  N N     . LEU A 1 1803 ? 214.163 241.700 238.211 1.00 3.67  ? 1803 LEU A N     1 
ATOM   2729  C CA    . LEU A 1 1803 ? 214.514 240.645 239.158 1.00 0.53  ? 1803 LEU A CA    1 
ATOM   2730  C C     . LEU A 1 1803 ? 213.626 240.700 240.393 1.00 0.50  ? 1803 LEU A C     1 
ATOM   2731  O O     . LEU A 1 1803 ? 213.100 239.674 240.846 1.00 6.52  ? 1803 LEU A O     1 
ATOM   2732  C CB    . LEU A 1 1803 ? 215.984 240.763 239.554 1.00 9.60  ? 1803 LEU A CB    1 
ATOM   2733  C CG    . LEU A 1 1803 ? 216.629 239.499 240.121 1.00 9.99  ? 1803 LEU A CG    1 
ATOM   2734  C CD1   . LEU A 1 1803 ? 216.489 238.348 239.144 1.00 5.00  ? 1803 LEU A CD1   1 
ATOM   2735  C CD2   . LEU A 1 1803 ? 218.089 239.749 240.456 1.00 9.55  ? 1803 LEU A CD2   1 
ATOM   2736  N N     . ARG A 1 1804 ? 213.450 241.894 240.957 1.00 3.40  ? 1804 ARG A N     1 
ATOM   2737  C CA    . ARG A 1 1804 ? 212.551 242.028 242.094 1.00 1.80  ? 1804 ARG A CA    1 
ATOM   2738  C C     . ARG A 1 1804 ? 211.107 241.774 241.689 1.00 0.70  ? 1804 ARG A C     1 
ATOM   2739  O O     . ARG A 1 1804 ? 210.323 241.277 242.498 1.00 0.00  ? 1804 ARG A O     1 
ATOM   2740  C CB    . ARG A 1 1804 ? 212.707 243.404 242.739 1.00 2.10  ? 1804 ARG A CB    1 
ATOM   2741  C CG    . ARG A 1 1804 ? 212.146 243.472 244.148 1.00 3.10  ? 1804 ARG A CG    1 
ATOM   2742  C CD    . ARG A 1 1804 ? 211.755 244.883 244.536 1.00 7.34  ? 1804 ARG A CD    1 
ATOM   2743  N NE    . ARG A 1 1804 ? 212.921 245.752 244.638 1.00 9.37  ? 1804 ARG A NE    1 
ATOM   2744  C CZ    . ARG A 1 1804 ? 212.865 247.063 244.828 1.00 7.29  ? 1804 ARG A CZ    1 
ATOM   2745  N NH1   . ARG A 1 1804 ? 211.709 247.698 244.927 1.00 11.51 ? 1804 ARG A NH1   1 
ATOM   2746  N NH2   . ARG A 1 1804 ? 213.997 247.753 244.923 1.00 7.17  ? 1804 ARG A NH2   1 
ATOM   2747  N N     . ARG A 1 1805 ? 210.743 242.085 240.445 1.00 1.72  ? 1805 ARG A N     1 
ATOM   2748  C CA    . ARG A 1 1805 ? 209.412 241.732 239.960 1.00 1.18  ? 1805 ARG A CA    1 
ATOM   2749  C C     . ARG A 1 1805 ? 209.204 240.222 239.977 1.00 1.53  ? 1805 ARG A C     1 
ATOM   2750  O O     . ARG A 1 1805 ? 208.153 239.735 240.412 1.00 2.73  ? 1805 ARG A O     1 
ATOM   2751  C CB    . ARG A 1 1805 ? 209.213 242.288 238.551 1.00 11.77 ? 1805 ARG A CB    1 
ATOM   2752  C CG    . ARG A 1 1805 ? 208.027 241.717 237.795 1.00 6.20  ? 1805 ARG A CG    1 
ATOM   2753  C CD    . ARG A 1 1805 ? 206.704 242.000 238.486 1.00 2.29  ? 1805 ARG A CD    1 
ATOM   2754  N NE    . ARG A 1 1805 ? 206.579 243.384 238.928 1.00 4.07  ? 1805 ARG A NE    1 
ATOM   2755  C CZ    . ARG A 1 1805 ? 206.475 244.427 238.116 1.00 0.28  ? 1805 ARG A CZ    1 
ATOM   2756  N NH1   . ARG A 1 1805 ? 206.555 244.291 236.804 1.00 2.13  ? 1805 ARG A NH1   1 
ATOM   2757  N NH2   . ARG A 1 1805 ? 206.295 245.638 238.634 1.00 1.56  ? 1805 ARG A NH2   1 
ATOM   2758  N N     . ARG A 1 1806 ? 210.199 239.462 239.513 1.00 4.32  ? 1806 ARG A N     1 
ATOM   2759  C CA    . ARG A 1 1806 ? 210.083 238.007 239.537 1.00 2.06  ? 1806 ARG A CA    1 
ATOM   2760  C C     . ARG A 1 1806 ? 210.051 237.472 240.964 1.00 2.03  ? 1806 ARG A C     1 
ATOM   2761  O O     . ARG A 1 1806 ? 209.293 236.542 241.263 1.00 9.73  ? 1806 ARG A O     1 
ATOM   2762  C CB    . ARG A 1 1806 ? 211.224 237.370 238.748 1.00 1.51  ? 1806 ARG A CB    1 
ATOM   2763  C CG    . ARG A 1 1806 ? 210.981 237.348 237.253 1.00 3.89  ? 1806 ARG A CG    1 
ATOM   2764  C CD    . ARG A 1 1806 ? 212.281 237.288 236.474 1.00 7.31  ? 1806 ARG A CD    1 
ATOM   2765  N NE    . ARG A 1 1806 ? 212.850 235.946 236.464 1.00 8.57  ? 1806 ARG A NE    1 
ATOM   2766  C CZ    . ARG A 1 1806 ? 212.339 234.913 235.807 1.00 10.22 ? 1806 ARG A CZ    1 
ATOM   2767  N NH1   . ARG A 1 1806 ? 211.244 235.033 235.074 1.00 8.29  ? 1806 ARG A NH1   1 
ATOM   2768  N NH2   . ARG A 1 1806 ? 212.943 233.732 235.884 1.00 9.17  ? 1806 ARG A NH2   1 
ATOM   2769  N N     . LYS A 1 1807 ? 210.876 238.033 241.854 1.00 1.67  ? 1807 LYS A N     1 
ATOM   2770  C CA    . LYS A 1 1807 ? 210.833 237.628 243.257 1.00 0.14  ? 1807 LYS A CA    1 
ATOM   2771  C C     . LYS A 1 1807 ? 209.451 237.873 243.850 1.00 1.44  ? 1807 LYS A C     1 
ATOM   2772  O O     . LYS A 1 1807 ? 208.881 237.004 244.524 1.00 1.19  ? 1807 LYS A O     1 
ATOM   2773  C CB    . LYS A 1 1807 ? 211.892 238.382 244.060 1.00 2.81  ? 1807 LYS A CB    1 
ATOM   2774  C CG    . LYS A 1 1807 ? 213.325 237.983 243.777 1.00 0.65  ? 1807 LYS A CG    1 
ATOM   2775  C CD    . LYS A 1 1807 ? 214.262 238.657 244.760 1.00 0.00  ? 1807 LYS A CD    1 
ATOM   2776  C CE    . LYS A 1 1807 ? 215.709 238.508 244.345 1.00 3.90  ? 1807 LYS A CE    1 
ATOM   2777  N NZ    . LYS A 1 1807 ? 216.598 239.367 245.172 1.00 4.02  ? 1807 LYS A NZ    1 
ATOM   2778  N N     . LEU A 1 1808 ? 208.896 239.061 243.599 1.00 3.68  ? 1808 LEU A N     1 
ATOM   2779  C CA    . LEU A 1 1808 ? 207.535 239.364 244.017 1.00 0.82  ? 1808 LEU A CA    1 
ATOM   2780  C C     . LEU A 1 1808 ? 206.562 238.314 243.508 1.00 1.85  ? 1808 LEU A C     1 
ATOM   2781  O O     . LEU A 1 1808 ? 205.818 237.725 244.294 1.00 11.37 ? 1808 LEU A O     1 
ATOM   2782  C CB    . LEU A 1 1808 ? 207.134 240.758 243.526 1.00 0.39  ? 1808 LEU A CB    1 
ATOM   2783  C CG    . LEU A 1 1808 ? 207.331 242.000 244.405 1.00 0.00  ? 1808 LEU A CG    1 
ATOM   2784  C CD1   . LEU A 1 1808 ? 206.339 241.989 245.542 1.00 2.49  ? 1808 LEU A CD1   1 
ATOM   2785  C CD2   . LEU A 1 1808 ? 208.734 242.092 244.963 1.00 0.47  ? 1808 LEU A CD2   1 
ATOM   2786  N N     . GLU A 1 1809 ? 206.588 238.032 242.203 1.00 0.00  ? 1809 GLU A N     1 
ATOM   2787  C CA    . GLU A 1 1809 ? 205.607 237.118 241.618 1.00 3.13  ? 1809 GLU A CA    1 
ATOM   2788  C C     . GLU A 1 1809 ? 205.727 235.714 242.204 1.00 5.37  ? 1809 GLU A C     1 
ATOM   2789  O O     . GLU A 1 1809 ? 204.713 235.055 242.474 1.00 5.60  ? 1809 GLU A O     1 
ATOM   2790  C CB    . GLU A 1 1809 ? 205.766 237.087 240.100 1.00 4.85  ? 1809 GLU A CB    1 
ATOM   2791  C CG    . GLU A 1 1809 ? 205.084 238.244 239.393 1.00 8.22  ? 1809 GLU A CG    1 
ATOM   2792  C CD    . GLU A 1 1809 ? 205.383 238.283 237.909 1.00 9.85  ? 1809 GLU A CD    1 
ATOM   2793  O OE1   . GLU A 1 1809 ? 206.577 238.271 237.541 1.00 13.75 ? 1809 GLU A OE1   1 
ATOM   2794  O OE2   . GLU A 1 1809 ? 204.425 238.331 237.109 1.00 6.94  ? 1809 GLU A OE2   1 
ATOM   2795  N N     . HIS A 1 1810 ? 206.959 235.238 242.411 1.00 3.25  ? 1810 HIS A N     1 
ATOM   2796  C CA    . HIS A 1 1810 ? 207.150 233.970 243.107 1.00 0.00  ? 1810 HIS A CA    1 
ATOM   2797  C C     . HIS A 1 1810 ? 206.514 234.017 244.490 1.00 1.28  ? 1810 HIS A C     1 
ATOM   2798  O O     . HIS A 1 1810 ? 205.902 233.038 244.944 1.00 8.61  ? 1810 HIS A O     1 
ATOM   2799  C CB    . HIS A 1 1810 ? 208.639 233.648 243.237 1.00 0.00  ? 1810 HIS A CB    1 
ATOM   2800  C CG    . HIS A 1 1810 ? 209.334 233.408 241.934 1.00 0.00  ? 1810 HIS A CG    1 
ATOM   2801  N ND1   . HIS A 1 1810 ? 208.805 232.619 240.938 1.00 3.04  ? 1810 HIS A ND1   1 
ATOM   2802  C CD2   . HIS A 1 1810 ? 210.547 233.813 241.486 1.00 4.22  ? 1810 HIS A CD2   1 
ATOM   2803  C CE1   . HIS A 1 1810 ? 209.645 232.576 239.919 1.00 0.00  ? 1810 HIS A CE1   1 
ATOM   2804  N NE2   . HIS A 1 1810 ? 210.711 233.290 240.227 1.00 0.00  ? 1810 HIS A NE2   1 
ATOM   2805  N N     . LEU A 1 1811 ? 206.663 235.150 245.180 1.00 1.31  ? 1811 LEU A N     1 
ATOM   2806  C CA    . LEU A 1 1811 ? 206.104 235.274 246.520 1.00 0.05  ? 1811 LEU A CA    1 
ATOM   2807  C C     . LEU A 1 1811 ? 204.580 235.259 246.495 1.00 0.00  ? 1811 LEU A C     1 
ATOM   2808  O O     . LEU A 1 1811 ? 203.954 234.648 247.364 1.00 2.64  ? 1811 LEU A O     1 
ATOM   2809  C CB    . LEU A 1 1811 ? 206.627 236.540 247.193 1.00 5.72  ? 1811 LEU A CB    1 
ATOM   2810  C CG    . LEU A 1 1811 ? 207.912 236.325 247.993 1.00 2.72  ? 1811 LEU A CG    1 
ATOM   2811  C CD1   . LEU A 1 1811 ? 208.393 237.628 248.601 1.00 8.27  ? 1811 LEU A CD1   1 
ATOM   2812  C CD2   . LEU A 1 1811 ? 207.708 235.269 249.062 1.00 0.00  ? 1811 LEU A CD2   1 
ATOM   2813  N N     . ILE A 1 1812 ? 203.960 235.938 245.524 1.00 2.90  ? 1812 ILE A N     1 
ATOM   2814  C CA    . ILE A 1 1812 ? 202.505 235.835 245.397 1.00 0.00  ? 1812 ILE A CA    1 
ATOM   2815  C C     . ILE A 1 1812 ? 202.089 234.394 245.138 1.00 2.83  ? 1812 ILE A C     1 
ATOM   2816  O O     . ILE A 1 1812 ? 201.104 233.914 245.705 1.00 10.20 ? 1812 ILE A O     1 
ATOM   2817  C CB    . ILE A 1 1812 ? 201.917 236.789 244.332 1.00 0.00  ? 1812 ILE A CB    1 
ATOM   2818  C CG1   . ILE A 1 1812 ? 202.052 238.272 244.707 1.00 0.44  ? 1812 ILE A CG1   1 
ATOM   2819  C CG2   . ILE A 1 1812 ? 200.458 236.458 244.056 1.00 0.73  ? 1812 ILE A CG2   1 
ATOM   2820  C CD1   . ILE A 1 1812 ? 203.263 238.968 244.257 1.00 3.95  ? 1812 ILE A CD1   1 
ATOM   2821  N N     . THR A 1 1813 ? 202.832 233.673 244.296 1.00 3.79  ? 1813 THR A N     1 
ATOM   2822  C CA    . THR A 1 1813 ? 202.460 232.287 244.018 1.00 0.00  ? 1813 THR A CA    1 
ATOM   2823  C C     . THR A 1 1813 ? 202.482 231.441 245.293 1.00 3.29  ? 1813 THR A C     1 
ATOM   2824  O O     . THR A 1 1813 ? 201.495 230.765 245.623 1.00 6.62  ? 1813 THR A O     1 
ATOM   2825  C CB    . THR A 1 1813 ? 203.385 231.694 242.956 1.00 0.00  ? 1813 THR A CB    1 
ATOM   2826  O OG1   . THR A 1 1813 ? 203.280 232.460 241.752 1.00 0.00  ? 1813 THR A OG1   1 
ATOM   2827  C CG2   . THR A 1 1813 ? 202.981 230.264 242.653 1.00 1.14  ? 1813 THR A CG2   1 
ATOM   2828  N N     . GLU A 1 1814 ? 203.597 231.481 246.035 1.00 0.00  ? 1814 GLU A N     1 
ATOM   2829  C CA    . GLU A 1 1814 ? 203.661 230.730 247.292 1.00 0.00  ? 1814 GLU A CA    1 
ATOM   2830  C C     . GLU A 1 1814 ? 202.626 231.185 248.306 1.00 4.56  ? 1814 GLU A C     1 
ATOM   2831  O O     . GLU A 1 1814 ? 201.992 230.347 248.949 1.00 12.23 ? 1814 GLU A O     1 
ATOM   2832  C CB    . GLU A 1 1814 ? 205.048 230.798 247.922 1.00 1.26  ? 1814 GLU A CB    1 
ATOM   2833  C CG    . GLU A 1 1814 ? 206.098 230.056 247.180 1.00 6.37  ? 1814 GLU A CG    1 
ATOM   2834  C CD    . GLU A 1 1814 ? 205.853 228.554 247.234 1.00 8.07  ? 1814 GLU A CD    1 
ATOM   2835  O OE1   . GLU A 1 1814 ? 205.302 228.087 248.250 1.00 6.18  ? 1814 GLU A OE1   1 
ATOM   2836  O OE2   . GLU A 1 1814 ? 206.222 227.830 246.290 1.00 10.75 ? 1814 GLU A OE2   1 
ATOM   2837  N N     . LEU A 1 1815 ? 202.462 232.491 248.505 1.00 3.37  ? 1815 LEU A N     1 
ATOM   2838  C CA    . LEU A 1 1815 ? 201.530 232.933 249.533 1.00 0.65  ? 1815 LEU A CA    1 
ATOM   2839  C C     . LEU A 1 1815 ? 200.092 232.613 249.159 1.00 0.67  ? 1815 LEU A C     1 
ATOM   2840  O O     . LEU A 1 1815 ? 199.283 232.332 250.043 1.00 7.36  ? 1815 LEU A O     1 
ATOM   2841  C CB    . LEU A 1 1815 ? 201.712 234.424 249.820 1.00 2.62  ? 1815 LEU A CB    1 
ATOM   2842  C CG    . LEU A 1 1815 ? 202.786 234.862 250.823 1.00 1.60  ? 1815 LEU A CG    1 
ATOM   2843  C CD1   . LEU A 1 1815 ? 202.432 234.345 252.201 1.00 5.24  ? 1815 LEU A CD1   1 
ATOM   2844  C CD2   . LEU A 1 1815 ? 204.176 234.394 250.439 1.00 5.86  ? 1815 LEU A CD2   1 
ATOM   2845  N N     . VAL A 1 1816 ? 199.758 232.604 247.868 1.00 0.00  ? 1816 VAL A N     1 
ATOM   2846  C CA    . VAL A 1 1816 ? 198.431 232.158 247.461 1.00 0.29  ? 1816 VAL A CA    1 
ATOM   2847  C C     . VAL A 1 1816 ? 198.256 230.673 247.751 1.00 4.43  ? 1816 VAL A C     1 
ATOM   2848  O O     . VAL A 1 1816 ? 197.220 230.250 248.280 1.00 5.05  ? 1816 VAL A O     1 
ATOM   2849  C CB    . VAL A 1 1816 ? 198.185 232.485 245.976 1.00 0.00  ? 1816 VAL A CB    1 
ATOM   2850  C CG1   . VAL A 1 1816 ? 197.006 231.692 245.445 1.00 0.73  ? 1816 VAL A CG1   1 
ATOM   2851  C CG2   . VAL A 1 1816 ? 197.934 233.969 245.802 1.00 1.26  ? 1816 VAL A CG2   1 
ATOM   2852  N N     . HIS A 1 1817 ? 199.265 229.860 247.422 1.00 7.01  ? 1817 HIS A N     1 
ATOM   2853  C CA    . HIS A 1 1817 ? 199.182 228.432 247.722 1.00 0.00  ? 1817 HIS A CA    1 
ATOM   2854  C C     . HIS A 1 1817 ? 198.997 228.200 249.217 1.00 4.67  ? 1817 HIS A C     1 
ATOM   2855  O O     . HIS A 1 1817 ? 198.149 227.402 249.638 1.00 10.57 ? 1817 HIS A O     1 
ATOM   2856  C CB    . HIS A 1 1817 ? 200.435 227.718 247.221 1.00 0.00  ? 1817 HIS A CB    1 
ATOM   2857  C CG    . HIS A 1 1817 ? 200.443 226.249 247.502 1.00 2.53  ? 1817 HIS A CG    1 
ATOM   2858  N ND1   . HIS A 1 1817 ? 199.299 225.481 247.478 1.00 4.29  ? 1817 HIS A ND1   1 
ATOM   2859  C CD2   . HIS A 1 1817 ? 201.453 225.409 247.827 1.00 3.77  ? 1817 HIS A CD2   1 
ATOM   2860  C CE1   . HIS A 1 1817 ? 199.606 224.229 247.766 1.00 4.29  ? 1817 HIS A CE1   1 
ATOM   2861  N NE2   . HIS A 1 1817 ? 200.906 224.159 247.985 1.00 5.30  ? 1817 HIS A NE2   1 
ATOM   2862  N N     . GLN A 1 1818 ? 199.781 228.905 250.033 1.00 4.84  ? 1818 GLN A N     1 
ATOM   2863  C CA    . GLN A 1 1818 ? 199.669 228.795 251.483 1.00 0.87  ? 1818 GLN A CA    1 
ATOM   2864  C C     . GLN A 1 1818 ? 198.309 229.270 251.970 1.00 2.97  ? 1818 GLN A C     1 
ATOM   2865  O O     . GLN A 1 1818 ? 197.755 228.711 252.920 1.00 0.58  ? 1818 GLN A O     1 
ATOM   2866  C CB    . GLN A 1 1818 ? 200.784 229.597 252.149 1.00 0.00  ? 1818 GLN A CB    1 
ATOM   2867  C CG    . GLN A 1 1818 ? 202.178 229.167 251.753 1.00 1.08  ? 1818 GLN A CG    1 
ATOM   2868  C CD    . GLN A 1 1818 ? 203.244 230.072 252.322 1.00 8.95  ? 1818 GLN A CD    1 
ATOM   2869  O OE1   . GLN A 1 1818 ? 202.946 231.005 253.065 1.00 10.17 ? 1818 GLN A OE1   1 
ATOM   2870  N NE2   . GLN A 1 1818 ? 204.497 229.798 251.984 1.00 8.63  ? 1818 GLN A NE2   1 
ATOM   2871  N N     . ARG A 1 1819 ? 197.762 230.309 251.338 1.00 2.50  ? 1819 ARG A N     1 
ATOM   2872  C CA    . ARG A 1 1819 ? 196.448 230.801 251.724 1.00 2.56  ? 1819 ARG A CA    1 
ATOM   2873  C C     . ARG A 1 1819 ? 195.373 229.753 251.481 1.00 8.08  ? 1819 ARG A C     1 
ATOM   2874  O O     . ARG A 1 1819 ? 194.539 229.502 252.358 1.00 12.18 ? 1819 ARG A O     1 
ATOM   2875  C CB    . ARG A 1 1819 ? 196.136 232.089 250.965 1.00 0.69  ? 1819 ARG A CB    1 
ATOM   2876  C CG    . ARG A 1 1819 ? 194.679 232.485 250.987 1.00 3.19  ? 1819 ARG A CG    1 
ATOM   2877  C CD    . ARG A 1 1819 ? 194.490 233.874 250.408 1.00 4.66  ? 1819 ARG A CD    1 
ATOM   2878  N NE    . ARG A 1 1819 ? 194.484 233.886 248.949 1.00 7.56  ? 1819 ARG A NE    1 
ATOM   2879  C CZ    . ARG A 1 1819 ? 193.607 233.250 248.184 1.00 7.90  ? 1819 ARG A CZ    1 
ATOM   2880  N NH1   . ARG A 1 1819 ? 192.610 232.551 248.702 1.00 8.68  ? 1819 ARG A NH1   1 
ATOM   2881  N NH2   . ARG A 1 1819 ? 193.724 233.328 246.862 1.00 4.99  ? 1819 ARG A NH2   1 
ATOM   2882  N N     . ASP A 1 1820 ? 195.381 229.115 250.307 1.00 4.19  ? 1820 ASP A N     1 
ATOM   2883  C CA    . ASP A 1 1820 ? 194.394 228.060 250.070 1.00 1.74  ? 1820 ASP A CA    1 
ATOM   2884  C C     . ASP A 1 1820 ? 194.610 226.867 250.994 1.00 3.59  ? 1820 ASP A C     1 
ATOM   2885  O O     . ASP A 1 1820 ? 193.640 226.276 251.481 1.00 3.02  ? 1820 ASP A O     1 
ATOM   2886  C CB    . ASP A 1 1820 ? 194.371 227.601 248.609 1.00 3.84  ? 1820 ASP A CB    1 
ATOM   2887  C CG    . ASP A 1 1820 ? 194.293 228.747 247.624 1.00 14.90 ? 1820 ASP A CG    1 
ATOM   2888  O OD1   . ASP A 1 1820 ? 195.330 229.142 247.065 1.00 16.25 ? 1820 ASP A OD1   1 
ATOM   2889  O OD2   . ASP A 1 1820 ? 193.174 229.262 247.413 1.00 15.83 ? 1820 ASP A OD2   1 
ATOM   2890  N N     . VAL A 1 1821 ? 195.866 226.495 251.253 1.00 2.08  ? 1821 VAL A N     1 
ATOM   2891  C CA    . VAL A 1 1821 ? 196.119 225.356 252.136 1.00 0.00  ? 1821 VAL A CA    1 
ATOM   2892  C C     . VAL A 1 1821 ? 195.611 225.646 253.544 1.00 4.14  ? 1821 VAL A C     1 
ATOM   2893  O O     . VAL A 1 1821 ? 194.929 224.818 254.161 1.00 14.52 ? 1821 VAL A O     1 
ATOM   2894  C CB    . VAL A 1 1821 ? 197.615 224.997 252.142 1.00 0.00  ? 1821 VAL A CB    1 
ATOM   2895  C CG1   . VAL A 1 1821 ? 197.912 224.020 253.264 1.00 6.62  ? 1821 VAL A CG1   1 
ATOM   2896  C CG2   . VAL A 1 1821 ? 198.015 224.403 250.812 1.00 0.00  ? 1821 VAL A CG2   1 
ATOM   2897  N N     . THR A 1 1822 ? 195.929 226.830 254.071 1.00 11.55 ? 1822 THR A N     1 
ATOM   2898  C CA    . THR A 1 1822 ? 195.486 227.193 255.412 1.00 4.78  ? 1822 THR A CA    1 
ATOM   2899  C C     . THR A 1 1822 ? 193.971 227.324 255.476 1.00 5.36  ? 1822 THR A C     1 
ATOM   2900  O O     . THR A 1 1822 ? 193.353 226.942 256.474 1.00 6.32  ? 1822 THR A O     1 
ATOM   2901  C CB    . THR A 1 1822 ? 196.160 228.491 255.853 1.00 5.07  ? 1822 THR A CB    1 
ATOM   2902  O OG1   . THR A 1 1822 ? 197.581 228.314 255.858 1.00 9.71  ? 1822 THR A OG1   1 
ATOM   2903  C CG2   . THR A 1 1822 ? 195.711 228.877 257.249 1.00 5.35  ? 1822 THR A CG2   1 
ATOM   2904  N N     . ARG A 1 1823 ? 193.352 227.864 254.423 1.00 9.85  ? 1823 ARG A N     1 
ATOM   2905  C CA    . ARG A 1 1823 ? 191.900 227.987 254.399 1.00 6.75  ? 1823 ARG A CA    1 
ATOM   2906  C C     . ARG A 1 1823 ? 191.233 226.616 254.388 1.00 12.69 ? 1823 ARG A C     1 
ATOM   2907  O O     . ARG A 1 1823 ? 190.214 226.408 255.058 1.00 16.47 ? 1823 ARG A O     1 
ATOM   2908  C CB    . ARG A 1 1823 ? 191.479 228.813 253.186 1.00 2.68  ? 1823 ARG A CB    1 
ATOM   2909  C CG    . ARG A 1 1823 ? 189.995 229.098 253.088 1.00 10.63 ? 1823 ARG A CG    1 
ATOM   2910  C CD    . ARG A 1 1823 ? 189.710 229.989 251.891 1.00 10.32 ? 1823 ARG A CD    1 
ATOM   2911  N NE    . ARG A 1 1823 ? 190.275 231.322 252.065 1.00 10.81 ? 1823 ARG A NE    1 
ATOM   2912  C CZ    . ARG A 1 1823 ? 190.332 232.243 251.114 1.00 11.34 ? 1823 ARG A CZ    1 
ATOM   2913  N NH1   . ARG A 1 1823 ? 189.862 232.012 249.899 1.00 9.52  ? 1823 ARG A NH1   1 
ATOM   2914  N NH2   . ARG A 1 1823 ? 190.875 233.426 251.388 1.00 9.82  ? 1823 ARG A NH2   1 
ATOM   2915  N N     . SER A 1 1824 ? 191.794 225.668 253.633 1.00 14.08 ? 1824 SER A N     1 
ATOM   2916  C CA    . SER A 1 1824 ? 191.270 224.306 253.643 1.00 9.63  ? 1824 SER A CA    1 
ATOM   2917  C C     . SER A 1 1824 ? 191.444 223.660 255.011 1.00 6.76  ? 1824 SER A C     1 
ATOM   2918  O O     . SER A 1 1824 ? 190.554 222.946 255.486 1.00 16.60 ? 1824 SER A O     1 
ATOM   2919  C CB    . SER A 1 1824 ? 191.958 223.468 252.568 1.00 10.98 ? 1824 SER A CB    1 
ATOM   2920  O OG    . SER A 1 1824 ? 193.289 223.163 252.942 1.00 11.25 ? 1824 SER A OG    1 
ATOM   2921  N N     . LEU A 1 1825 ? 192.591 223.891 255.655 1.00 3.15  ? 1825 LEU A N     1 
ATOM   2922  C CA    . LEU A 1 1825 ? 192.802 223.358 256.997 1.00 10.88 ? 1825 LEU A CA    1 
ATOM   2923  C C     . LEU A 1 1825 ? 191.792 223.933 257.982 1.00 15.33 ? 1825 LEU A C     1 
ATOM   2924  O O     . LEU A 1 1825 ? 191.255 223.210 258.829 1.00 20.25 ? 1825 LEU A O     1 
ATOM   2925  C CB    . LEU A 1 1825 ? 194.226 223.655 257.465 1.00 8.13  ? 1825 LEU A CB    1 
ATOM   2926  C CG    . LEU A 1 1825 ? 195.363 222.865 256.819 1.00 5.83  ? 1825 LEU A CG    1 
ATOM   2927  C CD1   . LEU A 1 1825 ? 196.701 223.403 257.285 1.00 8.68  ? 1825 LEU A CD1   1 
ATOM   2928  C CD2   . LEU A 1 1825 ? 195.239 221.390 257.137 1.00 9.02  ? 1825 LEU A CD2   1 
ATOM   2929  N N     . ILE A 1 1826 ? 191.528 225.236 257.886 1.00 13.19 ? 1826 ILE A N     1 
ATOM   2930  C CA    . ILE A 1 1826 ? 190.569 225.882 258.776 1.00 11.10 ? 1826 ILE A CA    1 
ATOM   2931  C C     . ILE A 1 1826 ? 189.168 225.334 258.542 1.00 12.43 ? 1826 ILE A C     1 
ATOM   2932  O O     . ILE A 1 1826 ? 188.439 225.028 259.493 1.00 18.75 ? 1826 ILE A O     1 
ATOM   2933  C CB    . ILE A 1 1826 ? 190.624 227.408 258.584 1.00 10.31 ? 1826 ILE A CB    1 
ATOM   2934  C CG1   . ILE A 1 1826 ? 191.900 227.976 259.204 1.00 8.56  ? 1826 ILE A CG1   1 
ATOM   2935  C CG2   . ILE A 1 1826 ? 189.398 228.069 259.181 1.00 11.53 ? 1826 ILE A CG2   1 
ATOM   2936  C CD1   . ILE A 1 1826 ? 192.042 229.465 259.040 1.00 10.14 ? 1826 ILE A CD1   1 
ATOM   2937  N N     . LYS A 1 1827 ? 188.768 225.198 257.275 1.00 8.65  ? 1827 LYS A N     1 
ATOM   2938  C CA    . LYS A 1 1827 ? 187.433 224.692 256.976 1.00 15.37 ? 1827 LYS A CA    1 
ATOM   2939  C C     . LYS A 1 1827 ? 187.287 223.227 257.364 1.00 15.57 ? 1827 LYS A C     1 
ATOM   2940  O O     . LYS A 1 1827 ? 186.179 222.772 257.672 1.00 16.31 ? 1827 LYS A O     1 
ATOM   2941  C CB    . LYS A 1 1827 ? 187.120 224.889 255.492 1.00 13.29 ? 1827 LYS A CB    1 
ATOM   2942  C CG    . LYS A 1 1827 ? 185.708 224.499 255.092 1.00 12.16 ? 1827 LYS A CG    1 
ATOM   2943  C CD    . LYS A 1 1827 ? 185.489 224.670 253.601 1.00 14.10 ? 1827 LYS A CD    1 
ATOM   2944  C CE    . LYS A 1 1827 ? 185.572 223.339 252.877 1.00 16.61 ? 1827 LYS A CE    1 
ATOM   2945  N NZ    . LYS A 1 1827 ? 184.588 223.256 251.763 1.00 16.59 ? 1827 LYS A NZ    1 
ATOM   2946  N N     . SER A 1 1828 ? 188.387 222.477 257.369 1.00 10.81 ? 1828 SER A N     1 
ATOM   2947  C CA    . SER A 1 1828 ? 188.355 221.063 257.719 1.00 12.78 ? 1828 SER A CA    1 
ATOM   2948  C C     . SER A 1 1828 ? 188.407 220.818 259.220 1.00 14.82 ? 1828 SER A C     1 
ATOM   2949  O O     . SER A 1 1828 ? 188.341 219.657 259.639 1.00 18.69 ? 1828 SER A O     1 
ATOM   2950  C CB    . SER A 1 1828 ? 189.512 220.326 257.041 1.00 12.44 ? 1828 SER A CB    1 
ATOM   2951  O OG    . SER A 1 1828 ? 189.387 220.373 255.631 1.00 18.09 ? 1828 SER A OG    1 
ATOM   2952  N N     . LYS A 1 1829 ? 188.522 221.871 260.029 1.00 14.84 ? 1829 LYS A N     1 
ATOM   2953  C CA    . LYS A 1 1829 ? 188.588 221.760 261.486 1.00 19.82 ? 1829 LYS A CA    1 
ATOM   2954  C C     . LYS A 1 1829 ? 189.726 220.830 261.915 1.00 16.36 ? 1829 LYS A C     1 
ATOM   2955  O O     . LYS A 1 1829 ? 189.561 219.937 262.747 1.00 15.49 ? 1829 LYS A O     1 
ATOM   2956  C CB    . LYS A 1 1829 ? 187.246 221.295 262.064 1.00 17.90 ? 1829 LYS A CB    1 
ATOM   2957  C CG    . LYS A 1 1829 ? 186.031 222.043 261.534 1.00 16.14 ? 1829 LYS A CG    1 
ATOM   2958  C CD    . LYS A 1 1829 ? 186.116 223.529 261.834 1.00 18.06 ? 1829 LYS A CD    1 
ATOM   2959  C CE    . LYS A 1 1829 ? 184.997 224.296 261.146 1.00 19.30 ? 1829 LYS A CE    1 
ATOM   2960  N NZ    . LYS A 1 1829 ? 185.040 224.148 259.666 1.00 17.04 ? 1829 LYS A NZ    1 
ATOM   2961  N N     . ILE A 1 1830 ? 190.895 221.060 261.327 1.00 10.15 ? 1830 ILE A N     1 
ATOM   2962  C CA    . ILE A 1 1830 ? 192.104 220.313 261.652 1.00 13.75 ? 1830 ILE A CA    1 
ATOM   2963  C C     . ILE A 1 1830 ? 192.685 220.872 262.940 1.00 19.19 ? 1830 ILE A C     1 
ATOM   2964  O O     . ILE A 1 1830 ? 192.904 222.084 263.057 1.00 21.86 ? 1830 ILE A O     1 
ATOM   2965  C CB    . ILE A 1 1830 ? 193.132 220.383 260.509 1.00 14.55 ? 1830 ILE A CB    1 
ATOM   2966  C CG1   . ILE A 1 1830 ? 192.526 219.876 259.198 1.00 15.45 ? 1830 ILE A CG1   1 
ATOM   2967  C CG2   . ILE A 1 1830 ? 194.383 219.601 260.866 1.00 11.31 ? 1830 ILE A CG2   1 
ATOM   2968  C CD1   . ILE A 1 1830 ? 191.751 218.584 259.341 1.00 19.04 ? 1830 ILE A CD1   1 
ATOM   2969  N N     . ASP A 1 1831 ? 192.933 219.993 263.909 1.00 13.04 ? 1831 ASP A N     1 
ATOM   2970  C CA    . ASP A 1 1831 ? 193.492 220.412 265.187 1.00 11.66 ? 1831 ASP A CA    1 
ATOM   2971  C C     . ASP A 1 1831 ? 194.789 219.671 265.481 1.00 12.57 ? 1831 ASP A C     1 
ATOM   2972  O O     . ASP A 1 1831 ? 195.723 220.244 266.047 1.00 16.75 ? 1831 ASP A O     1 
ATOM   2973  C CB    . ASP A 1 1831 ? 192.480 220.192 266.314 1.00 17.63 ? 1831 ASP A CB    1 
ATOM   2974  C CG    . ASP A 1 1831 ? 192.122 218.731 266.500 1.00 20.14 ? 1831 ASP A CG    1 
ATOM   2975  O OD1   . ASP A 1 1831 ? 191.257 218.230 265.753 1.00 22.14 ? 1831 ASP A OD1   1 
ATOM   2976  O OD2   . ASP A 1 1831 ? 192.703 218.084 267.396 1.00 20.01 ? 1831 ASP A OD2   1 
ATOM   2977  N N     . ASN A 1 1832 ? 194.856 218.398 265.105 1.00 14.99 ? 1832 ASN A N     1 
ATOM   2978  C CA    . ASN A 1 1832 ? 196.058 217.608 265.320 1.00 13.03 ? 1832 ASN A CA    1 
ATOM   2979  C C     . ASN A 1 1832 ? 197.055 217.832 264.192 1.00 10.63 ? 1832 ASN A C     1 
ATOM   2980  O O     . ASN A 1 1832 ? 196.685 217.885 263.016 1.00 11.27 ? 1832 ASN A O     1 
ATOM   2981  C CB    . ASN A 1 1832 ? 195.706 216.124 265.435 1.00 10.57 ? 1832 ASN A CB    1 
ATOM   2982  C CG    . ASN A 1 1832 ? 194.881 215.628 264.265 1.00 13.00 ? 1832 ASN A CG    1 
ATOM   2983  O OD1   . ASN A 1 1832 ? 194.209 216.409 263.591 1.00 15.52 ? 1832 ASN A OD1   1 
ATOM   2984  N ND2   . ASN A 1 1832 ? 194.923 214.324 264.021 1.00 10.56 ? 1832 ASN A ND2   1 
ATOM   2985  N N     . ALA A 1 1833 ? 198.328 217.968 264.560 1.00 11.32 ? 1833 ALA A N     1 
ATOM   2986  C CA    . ALA A 1 1833 ? 199.377 218.227 263.584 1.00 8.13  ? 1833 ALA A CA    1 
ATOM   2987  C C     . ALA A 1 1833 ? 199.861 216.968 262.882 1.00 5.46  ? 1833 ALA A C     1 
ATOM   2988  O O     . ALA A 1 1833 ? 200.651 217.071 261.939 1.00 6.84  ? 1833 ALA A O     1 
ATOM   2989  C CB    . ALA A 1 1833 ? 200.563 218.923 264.255 1.00 11.42 ? 1833 ALA A CB    1 
ATOM   2990  N N     . LYS A 1 1834 ? 199.420 215.790 263.320 1.00 4.32  ? 1834 LYS A N     1 
ATOM   2991  C CA    . LYS A 1 1834 ? 199.767 214.535 262.669 1.00 0.31  ? 1834 LYS A CA    1 
ATOM   2992  C C     . LYS A 1 1834 ? 198.690 214.071 261.700 1.00 1.34  ? 1834 LYS A C     1 
ATOM   2993  O O     . LYS A 1 1834 ? 198.826 212.997 261.106 1.00 4.37  ? 1834 LYS A O     1 
ATOM   2994  C CB    . LYS A 1 1834 ? 200.033 213.451 263.715 1.00 1.20  ? 1834 LYS A CB    1 
ATOM   2995  C CG    . LYS A 1 1834 ? 201.255 213.712 264.578 1.00 4.40  ? 1834 LYS A CG    1 
ATOM   2996  C CD    . LYS A 1 1834 ? 202.504 213.864 263.731 1.00 7.37  ? 1834 LYS A CD    1 
ATOM   2997  C CE    . LYS A 1 1834 ? 203.307 212.576 263.694 1.00 14.75 ? 1834 LYS A CE    1 
ATOM   2998  N NZ    . LYS A 1 1834 ? 204.109 212.463 262.445 1.00 12.86 ? 1834 LYS A NZ    1 
ATOM   2999  N N     . SER A 1 1835 ? 197.625 214.849 261.530 1.00 1.07  ? 1835 SER A N     1 
ATOM   3000  C CA    . SER A 1 1835 ? 196.559 214.473 260.616 1.00 0.14  ? 1835 SER A CA    1 
ATOM   3001  C C     . SER A 1 1835 ? 197.062 214.499 259.182 1.00 4.16  ? 1835 SER A C     1 
ATOM   3002  O O     . SER A 1 1835 ? 197.910 215.318 258.821 1.00 10.21 ? 1835 SER A O     1 
ATOM   3003  C CB    . SER A 1 1835 ? 195.370 215.417 260.764 1.00 3.72  ? 1835 SER A CB    1 
ATOM   3004  O OG    . SER A 1 1835 ? 195.704 216.715 260.313 1.00 9.23  ? 1835 SER A OG    1 
ATOM   3005  N N     . PHE A 1 1836 ? 196.524 213.599 258.358 1.00 9.78  ? 1836 PHE A N     1 
ATOM   3006  C CA    . PHE A 1 1836 ? 196.987 213.502 256.979 1.00 3.05  ? 1836 PHE A CA    1 
ATOM   3007  C C     . PHE A 1 1836 ? 196.646 214.759 256.191 1.00 6.56  ? 1836 PHE A C     1 
ATOM   3008  O O     . PHE A 1 1836 ? 197.417 215.181 255.325 1.00 12.77 ? 1836 PHE A O     1 
ATOM   3009  C CB    . PHE A 1 1836 ? 196.392 212.270 256.302 1.00 1.85  ? 1836 PHE A CB    1 
ATOM   3010  C CG    . PHE A 1 1836 ? 197.031 211.944 254.987 1.00 0.00  ? 1836 PHE A CG    1 
ATOM   3011  C CD1   . PHE A 1 1836 ? 198.346 211.522 254.933 1.00 0.39  ? 1836 PHE A CD1   1 
ATOM   3012  C CD2   . PHE A 1 1836 ? 196.326 212.070 253.807 1.00 0.00  ? 1836 PHE A CD2   1 
ATOM   3013  C CE1   . PHE A 1 1836 ? 198.943 211.222 253.730 1.00 0.00  ? 1836 PHE A CE1   1 
ATOM   3014  C CE2   . PHE A 1 1836 ? 196.922 211.777 252.602 1.00 0.00  ? 1836 PHE A CE2   1 
ATOM   3015  C CZ    . PHE A 1 1836 ? 198.230 211.350 252.563 1.00 0.74  ? 1836 PHE A CZ    1 
ATOM   3016  N N     . GLU A 1 1837 ? 195.497 215.377 256.481 1.00 3.47  ? 1837 GLU A N     1 
ATOM   3017  C CA    . GLU A 1 1837 ? 195.102 216.583 255.760 1.00 0.54  ? 1837 GLU A CA    1 
ATOM   3018  C C     . GLU A 1 1837 ? 196.144 217.687 255.864 1.00 1.66  ? 1837 GLU A C     1 
ATOM   3019  O O     . GLU A 1 1837 ? 196.240 218.521 254.957 1.00 0.00  ? 1837 GLU A O     1 
ATOM   3020  C CB    . GLU A 1 1837 ? 193.749 217.079 256.269 1.00 2.43  ? 1837 GLU A CB    1 
ATOM   3021  C CG    . GLU A 1 1837 ? 192.590 216.172 255.895 1.00 8.33  ? 1837 GLU A CG    1 
ATOM   3022  C CD    . GLU A 1 1837 ? 192.240 215.185 256.987 1.00 15.15 ? 1837 GLU A CD    1 
ATOM   3023  O OE1   . GLU A 1 1837 ? 193.098 214.929 257.857 1.00 13.03 ? 1837 GLU A OE1   1 
ATOM   3024  O OE2   . GLU A 1 1837 ? 191.107 214.660 256.972 1.00 18.59 ? 1837 GLU A OE2   1 
ATOM   3025  N N     . TRP A 1 1838 ? 196.926 217.711 256.940 1.00 1.91  ? 1838 TRP A N     1 
ATOM   3026  C CA    . TRP A 1 1838 ? 198.106 218.559 257.020 1.00 0.00  ? 1838 TRP A CA    1 
ATOM   3027  C C     . TRP A 1 1838 ? 199.377 217.802 256.672 1.00 2.19  ? 1838 TRP A C     1 
ATOM   3028  O O     . TRP A 1 1838 ? 200.279 218.367 256.048 1.00 11.26 ? 1838 TRP A O     1 
ATOM   3029  C CB    . TRP A 1 1838 ? 198.243 219.158 258.422 1.00 0.00  ? 1838 TRP A CB    1 
ATOM   3030  C CG    . TRP A 1 1838 ? 199.632 219.634 258.741 1.00 2.86  ? 1838 TRP A CG    1 
ATOM   3031  C CD1   . TRP A 1 1838 ? 200.479 219.125 259.680 1.00 6.17  ? 1838 TRP A CD1   1 
ATOM   3032  C CD2   . TRP A 1 1838 ? 200.325 220.728 258.128 1.00 0.77  ? 1838 TRP A CD2   1 
ATOM   3033  N NE1   . TRP A 1 1838 ? 201.659 219.827 259.684 1.00 1.96  ? 1838 TRP A NE1   1 
ATOM   3034  C CE2   . TRP A 1 1838 ? 201.589 220.818 258.742 1.00 0.00  ? 1838 TRP A CE2   1 
ATOM   3035  C CE3   . TRP A 1 1838 ? 200.000 221.637 257.118 1.00 6.44  ? 1838 TRP A CE3   1 
ATOM   3036  C CZ2   . TRP A 1 1838 ? 202.525 221.779 258.380 1.00 0.00  ? 1838 TRP A CZ2   1 
ATOM   3037  C CZ3   . TRP A 1 1838 ? 200.933 222.588 256.758 1.00 2.81  ? 1838 TRP A CZ3   1 
ATOM   3038  C CH2   . TRP A 1 1838 ? 202.180 222.652 257.387 1.00 0.45  ? 1838 TRP A CH2   1 
ATOM   3039  N N     . LEU A 1 1839 ? 199.463 216.528 257.055 1.00 1.39  ? 1839 LEU A N     1 
ATOM   3040  C CA    . LEU A 1 1839 ? 200.647 215.731 256.773 1.00 0.01  ? 1839 LEU A CA    1 
ATOM   3041  C C     . LEU A 1 1839 ? 200.804 215.417 255.292 1.00 1.05  ? 1839 LEU A C     1 
ATOM   3042  O O     . LEU A 1 1839 ? 201.892 215.005 254.882 1.00 1.78  ? 1839 LEU A O     1 
ATOM   3043  C CB    . LEU A 1 1839 ? 200.604 214.429 257.573 1.00 0.00  ? 1839 LEU A CB    1 
ATOM   3044  C CG    . LEU A 1 1839 ? 201.935 213.843 258.039 1.00 0.79  ? 1839 LEU A CG    1 
ATOM   3045  C CD1   . LEU A 1 1839 ? 202.728 214.882 258.812 1.00 0.57  ? 1839 LEU A CD1   1 
ATOM   3046  C CD2   . LEU A 1 1839 ? 201.702 212.610 258.888 1.00 3.44  ? 1839 LEU A CD2   1 
ATOM   3047  N N     . SER A 1 1840 ? 199.755 215.594 254.488 1.00 0.00  ? 1840 SER A N     1 
ATOM   3048  C CA    . SER A 1 1840 ? 199.839 215.369 253.051 1.00 0.00  ? 1840 SER A CA    1 
ATOM   3049  C C     . SER A 1 1840 ? 200.383 216.566 252.288 1.00 4.40  ? 1840 SER A C     1 
ATOM   3050  O O     . SER A 1 1840 ? 200.558 216.470 251.070 1.00 8.32  ? 1840 SER A O     1 
ATOM   3051  C CB    . SER A 1 1840 ? 198.466 215.006 252.486 1.00 0.00  ? 1840 SER A CB    1 
ATOM   3052  O OG    . SER A 1 1840 ? 198.427 215.206 251.087 1.00 3.09  ? 1840 SER A OG    1 
ATOM   3053  N N     . GLN A 1 1841 ? 200.629 217.685 252.956 1.00 5.82  ? 1841 GLN A N     1 
ATOM   3054  C CA    . GLN A 1 1841 ? 201.182 218.864 252.311 1.00 0.60  ? 1841 GLN A CA    1 
ATOM   3055  C C     . GLN A 1 1841 ? 202.701 218.841 252.382 1.00 3.08  ? 1841 GLN A C     1 
ATOM   3056  O O     . GLN A 1 1841 ? 203.288 218.299 253.321 1.00 11.86 ? 1841 GLN A O     1 
ATOM   3057  C CB    . GLN A 1 1841 ? 200.655 220.140 252.969 1.00 3.19  ? 1841 GLN A CB    1 
ATOM   3058  C CG    . GLN A 1 1841 ? 199.193 220.083 253.362 1.00 4.44  ? 1841 GLN A CG    1 
ATOM   3059  C CD    . GLN A 1 1841 ? 198.267 220.143 252.169 1.00 8.19  ? 1841 GLN A CD    1 
ATOM   3060  O OE1   . GLN A 1 1841 ? 198.679 220.500 251.066 1.00 7.83  ? 1841 GLN A OE1   1 
ATOM   3061  N NE2   . GLN A 1 1841 ? 197.005 219.796 252.382 1.00 10.49 ? 1841 GLN A NE2   1 
ATOM   3062  N N     . MET A 1 1842 ? 203.336 219.433 251.374 1.00 0.00  ? 1842 MET A N     1 
ATOM   3063  C CA    . MET A 1 1842 ? 204.783 219.608 251.395 1.00 0.00  ? 1842 MET A CA    1 
ATOM   3064  C C     . MET A 1 1842 ? 205.150 220.551 252.531 1.00 3.35  ? 1842 MET A C     1 
ATOM   3065  O O     . MET A 1 1842 ? 204.755 221.720 252.532 1.00 9.67  ? 1842 MET A O     1 
ATOM   3066  C CB    . MET A 1 1842 ? 205.276 220.144 250.056 1.00 4.84  ? 1842 MET A CB    1 
ATOM   3067  C CG    . MET A 1 1842 ? 206.773 219.992 249.854 1.00 8.43  ? 1842 MET A CG    1 
ATOM   3068  S SD    . MET A 1 1842 ? 207.259 220.000 248.123 1.00 3.06  ? 1842 MET A SD    1 
ATOM   3069  C CE    . MET A 1 1842 ? 207.380 218.246 247.799 1.00 13.63 ? 1842 MET A CE    1 
ATOM   3070  N N     . ARG A 1 1843 ? 205.905 220.045 253.501 1.00 0.52  ? 1843 ARG A N     1 
ATOM   3071  C CA    . ARG A 1 1843 ? 206.248 220.787 254.703 1.00 0.00  ? 1843 ARG A CA    1 
ATOM   3072  C C     . ARG A 1 1843 ? 207.758 220.919 254.807 1.00 0.00  ? 1843 ARG A C     1 
ATOM   3073  O O     . ARG A 1 1843 ? 208.499 220.033 254.372 1.00 4.29  ? 1843 ARG A O     1 
ATOM   3074  C CB    . ARG A 1 1843 ? 205.696 220.093 255.945 1.00 0.00  ? 1843 ARG A CB    1 
ATOM   3075  C CG    . ARG A 1 1843 ? 204.189 219.986 255.954 1.00 0.00  ? 1843 ARG A CG    1 
ATOM   3076  C CD    . ARG A 1 1843 ? 203.742 218.809 256.787 1.00 0.00  ? 1843 ARG A CD    1 
ATOM   3077  N NE    . ARG A 1 1843 ? 203.770 217.565 256.031 1.00 0.00  ? 1843 ARG A NE    1 
ATOM   3078  C CZ    . ARG A 1 1843 ? 204.534 216.527 256.334 1.00 0.00  ? 1843 ARG A CZ    1 
ATOM   3079  N NH1   . ARG A 1 1843 ? 205.358 216.554 257.367 1.00 0.00  ? 1843 ARG A NH1   1 
ATOM   3080  N NH2   . ARG A 1 1843 ? 204.469 215.432 255.582 1.00 7.29  ? 1843 ARG A NH2   1 
ATOM   3081  N N     . PHE A 1 1844 ? 208.210 222.023 255.392 1.00 2.12  ? 1844 PHE A N     1 
ATOM   3082  C CA    . PHE A 1 1844 ? 209.619 222.379 255.414 1.00 0.00  ? 1844 PHE A CA    1 
ATOM   3083  C C     . PHE A 1 1844 ? 210.105 222.515 256.850 1.00 1.83  ? 1844 PHE A C     1 
ATOM   3084  O O     . PHE A 1 1844 ? 209.485 223.205 257.663 1.00 16.05 ? 1844 PHE A O     1 
ATOM   3085  C CB    . PHE A 1 1844 ? 209.857 223.681 254.650 1.00 0.00  ? 1844 PHE A CB    1 
ATOM   3086  C CG    . PHE A 1 1844 ? 209.548 223.585 253.184 1.00 0.00  ? 1844 PHE A CG    1 
ATOM   3087  C CD1   . PHE A 1 1844 ? 208.238 223.539 252.737 1.00 0.29  ? 1844 PHE A CD1   1 
ATOM   3088  C CD2   . PHE A 1 1844 ? 210.565 223.538 252.252 1.00 2.16  ? 1844 PHE A CD2   1 
ATOM   3089  C CE1   . PHE A 1 1844 ? 207.952 223.446 251.395 1.00 1.15  ? 1844 PHE A CE1   1 
ATOM   3090  C CE2   . PHE A 1 1844 ? 210.283 223.445 250.908 1.00 1.42  ? 1844 PHE A CE2   1 
ATOM   3091  C CZ    . PHE A 1 1844 ? 208.975 223.401 250.481 1.00 3.67  ? 1844 PHE A CZ    1 
ATOM   3092  N N     . TYR A 1 1845 ? 211.220 221.854 257.151 1.00 0.00  ? 1845 TYR A N     1 
ATOM   3093  C CA    . TYR A 1 1845 ? 211.796 221.835 258.489 1.00 0.39  ? 1845 TYR A CA    1 
ATOM   3094  C C     . TYR A 1 1845 ? 213.246 222.274 258.386 1.00 3.55  ? 1845 TYR A C     1 
ATOM   3095  O O     . TYR A 1 1845 ? 214.054 221.596 257.744 1.00 11.77 ? 1845 TYR A O     1 
ATOM   3096  C CB    . TYR A 1 1845 ? 211.708 220.440 259.108 1.00 3.56  ? 1845 TYR A CB    1 
ATOM   3097  C CG    . TYR A 1 1845 ? 210.305 219.897 259.194 1.00 4.25  ? 1845 TYR A CG    1 
ATOM   3098  C CD1   . TYR A 1 1845 ? 209.714 219.273 258.105 1.00 4.86  ? 1845 TYR A CD1   1 
ATOM   3099  C CD2   . TYR A 1 1845 ? 209.574 220.000 260.365 1.00 4.79  ? 1845 TYR A CD2   1 
ATOM   3100  C CE1   . TYR A 1 1845 ? 208.435 218.777 258.178 1.00 6.29  ? 1845 TYR A CE1   1 
ATOM   3101  C CE2   . TYR A 1 1845 ? 208.297 219.501 260.448 1.00 7.28  ? 1845 TYR A CE2   1 
ATOM   3102  C CZ    . TYR A 1 1845 ? 207.730 218.891 259.352 1.00 3.08  ? 1845 TYR A CZ    1 
ATOM   3103  O OH    . TYR A 1 1845 ? 206.451 218.395 259.433 1.00 1.62  ? 1845 TYR A OH    1 
ATOM   3104  N N     . PHE A 1 1846 ? 213.578 223.391 259.022 1.00 1.36  ? 1846 PHE A N     1 
ATOM   3105  C CA    . PHE A 1 1846 ? 214.908 223.973 258.925 1.00 3.42  ? 1846 PHE A CA    1 
ATOM   3106  C C     . PHE A 1 1846 ? 215.548 224.019 260.305 1.00 14.59 ? 1846 PHE A C     1 
ATOM   3107  O O     . PHE A 1 1846 ? 214.970 224.574 261.245 1.00 17.63 ? 1846 PHE A O     1 
ATOM   3108  C CB    . PHE A 1 1846 ? 214.833 225.369 258.305 1.00 2.04  ? 1846 PHE A CB    1 
ATOM   3109  C CG    . PHE A 1 1846 ? 216.168 226.003 258.078 1.00 4.01  ? 1846 PHE A CG    1 
ATOM   3110  C CD1   . PHE A 1 1846 ? 217.022 225.509 257.109 1.00 7.04  ? 1846 PHE A CD1   1 
ATOM   3111  C CD2   . PHE A 1 1846 ? 216.557 227.111 258.803 1.00 2.73  ? 1846 PHE A CD2   1 
ATOM   3112  C CE1   . PHE A 1 1846 ? 218.251 226.091 256.887 1.00 11.31 ? 1846 PHE A CE1   1 
ATOM   3113  C CE2   . PHE A 1 1846 ? 217.781 227.700 258.578 1.00 6.47  ? 1846 PHE A CE2   1 
ATOM   3114  C CZ    . PHE A 1 1846 ? 218.629 227.187 257.623 1.00 12.82 ? 1846 PHE A CZ    1 
ATOM   3115  N N     . ASP A 1 1847 ? 216.738 223.431 260.421 1.00 14.69 ? 1847 ASP A N     1 
ATOM   3116  C CA    . ASP A 1 1847 ? 217.473 223.380 261.684 1.00 10.49 ? 1847 ASP A CA    1 
ATOM   3117  C C     . ASP A 1 1847 ? 218.907 223.831 261.431 1.00 19.95 ? 1847 ASP A C     1 
ATOM   3118  O O     . ASP A 1 1847 ? 219.730 223.052 260.924 1.00 21.50 ? 1847 ASP A O     1 
ATOM   3119  C CB    . ASP A 1 1847 ? 217.439 221.979 262.289 1.00 16.18 ? 1847 ASP A CB    1 
ATOM   3120  C CG    . ASP A 1 1847 ? 217.677 221.984 263.788 1.00 26.46 ? 1847 ASP A CG    1 
ATOM   3121  O OD1   . ASP A 1 1847 ? 218.634 221.320 264.241 1.00 27.26 ? 1847 ASP A OD1   1 
ATOM   3122  O OD2   . ASP A 1 1847 ? 216.908 222.648 264.513 1.00 27.02 ? 1847 ASP A OD2   1 
ATOM   3123  N N     . PRO A 1 1848 ? 219.242 225.080 261.763 1.00 24.54 ? 1848 PRO A N     1 
ATOM   3124  C CA    . PRO A 1 1848 ? 220.604 225.581 261.544 1.00 23.69 ? 1848 PRO A CA    1 
ATOM   3125  C C     . PRO A 1 1848 ? 221.672 224.882 262.369 1.00 29.48 ? 1848 PRO A C     1 
ATOM   3126  O O     . PRO A 1 1848 ? 222.855 224.970 262.019 1.00 27.99 ? 1848 PRO A O     1 
ATOM   3127  C CB    . PRO A 1 1848 ? 220.468 227.055 261.970 1.00 26.17 ? 1848 PRO A CB    1 
ATOM   3128  C CG    . PRO A 1 1848 ? 219.023 227.337 261.667 1.00 23.60 ? 1848 PRO A CG    1 
ATOM   3129  C CD    . PRO A 1 1848 ? 218.411 226.149 262.332 1.00 23.20 ? 1848 PRO A CD    1 
ATOM   3130  N N     . LYS A 1 1849 ? 221.288 224.199 263.449 1.00 30.01 ? 1849 LYS A N     1 
ATOM   3131  C CA    . LYS A 1 1849 ? 222.267 223.678 264.396 1.00 28.55 ? 1849 LYS A CA    1 
ATOM   3132  C C     . LYS A 1 1849 ? 223.112 222.560 263.798 1.00 28.65 ? 1849 LYS A C     1 
ATOM   3133  O O     . LYS A 1 1849 ? 224.214 222.292 264.290 1.00 29.48 ? 1849 LYS A O     1 
ATOM   3134  C CB    . LYS A 1 1849 ? 221.552 223.189 265.655 1.00 27.20 ? 1849 LYS A CB    1 
ATOM   3135  C CG    . LYS A 1 1849 ? 220.918 224.305 266.471 1.00 28.80 ? 1849 LYS A CG    1 
ATOM   3136  C CD    . LYS A 1 1849 ? 220.247 223.768 267.723 1.00 31.73 ? 1849 LYS A CD    1 
ATOM   3137  C CE    . LYS A 1 1849 ? 219.596 224.886 268.522 1.00 32.05 ? 1849 LYS A CE    1 
ATOM   3138  N NZ    . LYS A 1 1849 ? 218.921 224.377 269.748 1.00 31.52 ? 1849 LYS A NZ    1 
ATOM   3139  N N     . GLN A 1 1850 ? 222.625 221.901 262.749 1.00 24.36 ? 1850 GLN A N     1 
ATOM   3140  C CA    . GLN A 1 1850 ? 223.368 220.793 262.164 1.00 27.91 ? 1850 GLN A CA    1 
ATOM   3141  C C     . GLN A 1 1850 ? 224.613 221.300 261.447 1.00 28.63 ? 1850 GLN A C     1 
ATOM   3142  O O     . GLN A 1 1850 ? 224.556 222.267 260.683 1.00 26.76 ? 1850 GLN A O     1 
ATOM   3143  C CB    . GLN A 1 1850 ? 222.478 220.009 261.201 1.00 23.76 ? 1850 GLN A CB    1 
ATOM   3144  C CG    . GLN A 1 1850 ? 221.665 218.922 261.877 1.00 25.35 ? 1850 GLN A CG    1 
ATOM   3145  C CD    . GLN A 1 1850 ? 222.329 217.564 261.787 1.00 28.69 ? 1850 GLN A CD    1 
ATOM   3146  O OE1   . GLN A 1 1850 ? 222.892 217.204 260.754 1.00 27.78 ? 1850 GLN A OE1   1 
ATOM   3147  N NE2   . GLN A 1 1850 ? 222.274 216.804 262.876 1.00 30.01 ? 1850 GLN A NE2   1 
ATOM   3148  N N     . THR A 1 1851 ? 225.744 220.637 261.696 1.00 28.79 ? 1851 THR A N     1 
ATOM   3149  C CA    . THR A 1 1851 ? 227.005 221.086 261.116 1.00 28.81 ? 1851 THR A CA    1 
ATOM   3150  C C     . THR A 1 1851 ? 227.099 220.730 259.636 1.00 22.51 ? 1851 THR A C     1 
ATOM   3151  O O     . THR A 1 1851 ? 227.798 221.408 258.874 1.00 23.59 ? 1851 THR A O     1 
ATOM   3152  C CB    . THR A 1 1851 ? 228.184 220.496 261.893 1.00 30.78 ? 1851 THR A CB    1 
ATOM   3153  O OG1   . THR A 1 1851 ? 229.408 221.074 261.421 1.00 29.65 ? 1851 THR A OG1   1 
ATOM   3154  C CG2   . THR A 1 1851 ? 228.243 218.983 261.733 1.00 28.84 ? 1851 THR A CG2   1 
ATOM   3155  N N     . ASP A 1 1852 ? 226.411 219.674 259.210 1.00 19.79 ? 1852 ASP A N     1 
ATOM   3156  C CA    . ASP A 1 1852 ? 226.419 219.306 257.802 1.00 19.85 ? 1852 ASP A CA    1 
ATOM   3157  C C     . ASP A 1 1852 ? 225.525 220.251 257.012 1.00 23.10 ? 1852 ASP A C     1 
ATOM   3158  O O     . ASP A 1 1852 ? 224.397 220.544 257.414 1.00 27.47 ? 1852 ASP A O     1 
ATOM   3159  C CB    . ASP A 1 1852 ? 225.951 217.863 257.621 1.00 19.21 ? 1852 ASP A CB    1 
ATOM   3160  C CG    . ASP A 1 1852 ? 226.149 217.356 256.202 1.00 23.33 ? 1852 ASP A CG    1 
ATOM   3161  O OD1   . ASP A 1 1852 ? 226.627 218.128 255.345 1.00 19.04 ? 1852 ASP A OD1   1 
ATOM   3162  O OD2   . ASP A 1 1852 ? 225.826 216.178 255.943 1.00 27.19 ? 1852 ASP A OD2   1 
ATOM   3163  N N     . VAL A 1 1853 ? 226.038 220.724 255.876 1.00 23.12 ? 1853 VAL A N     1 
ATOM   3164  C CA    . VAL A 1 1853 ? 225.318 221.716 255.082 1.00 18.58 ? 1853 VAL A CA    1 
ATOM   3165  C C     . VAL A 1 1853 ? 224.067 221.110 254.453 1.00 9.67  ? 1853 VAL A C     1 
ATOM   3166  O O     . VAL A 1 1853 ? 223.023 221.767 254.359 1.00 4.04  ? 1853 VAL A O     1 
ATOM   3167  C CB    . VAL A 1 1853 ? 226.260 222.324 254.023 1.00 15.98 ? 1853 VAL A CB    1 
ATOM   3168  C CG1   . VAL A 1 1853 ? 226.828 221.243 253.115 1.00 18.30 ? 1853 VAL A CG1   1 
ATOM   3169  C CG2   . VAL A 1 1853 ? 225.536 223.366 253.202 1.00 10.58 ? 1853 VAL A CG2   1 
ATOM   3170  N N     . LEU A 1 1854 ? 224.142 219.848 254.032 1.00 11.09 ? 1854 LEU A N     1 
ATOM   3171  C CA    . LEU A 1 1854 ? 223.100 219.284 253.181 1.00 16.73 ? 1854 LEU A CA    1 
ATOM   3172  C C     . LEU A 1 1854 ? 221.822 218.991 253.960 1.00 18.40 ? 1854 LEU A C     1 
ATOM   3173  O O     . LEU A 1 1854 ? 220.723 219.038 253.394 1.00 14.02 ? 1854 LEU A O     1 
ATOM   3174  C CB    . LEU A 1 1854 ? 223.619 218.016 252.502 1.00 15.51 ? 1854 LEU A CB    1 
ATOM   3175  C CG    . LEU A 1 1854 ? 224.788 218.220 251.534 1.00 15.88 ? 1854 LEU A CG    1 
ATOM   3176  C CD1   . LEU A 1 1854 ? 225.379 216.887 251.108 1.00 14.37 ? 1854 LEU A CD1   1 
ATOM   3177  C CD2   . LEU A 1 1854 ? 224.349 219.025 250.322 1.00 12.90 ? 1854 LEU A CD2   1 
ATOM   3178  N N     . GLN A 1 1855 ? 221.937 218.686 255.253 1.00 15.29 ? 1855 GLN A N     1 
ATOM   3179  C CA    . GLN A 1 1855 ? 220.805 218.202 256.033 1.00 9.66  ? 1855 GLN A CA    1 
ATOM   3180  C C     . GLN A 1 1855 ? 220.232 219.252 256.979 1.00 9.60  ? 1855 GLN A C     1 
ATOM   3181  O O     . GLN A 1 1855 ? 219.480 218.904 257.894 1.00 13.45 ? 1855 GLN A O     1 
ATOM   3182  C CB    . GLN A 1 1855 ? 221.202 216.952 256.817 1.00 10.11 ? 1855 GLN A CB    1 
ATOM   3183  C CG    . GLN A 1 1855 ? 222.146 216.028 256.074 1.00 14.67 ? 1855 GLN A CG    1 
ATOM   3184  C CD    . GLN A 1 1855 ? 222.816 215.028 256.992 1.00 18.81 ? 1855 GLN A CD    1 
ATOM   3185  O OE1   . GLN A 1 1855 ? 222.155 214.357 257.784 1.00 20.97 ? 1855 GLN A OE1   1 
ATOM   3186  N NE2   . GLN A 1 1855 ? 224.135 214.922 256.890 1.00 18.04 ? 1855 GLN A NE2   1 
ATOM   3187  N N     . GLN A 1 1856 ? 220.564 220.529 256.785 1.00 7.44  ? 1856 GLN A N     1 
ATOM   3188  C CA    . GLN A 1 1856 ? 219.981 221.564 257.635 1.00 8.77  ? 1856 GLN A CA    1 
ATOM   3189  C C     . GLN A 1 1856 ? 218.505 221.771 257.321 1.00 6.35  ? 1856 GLN A C     1 
ATOM   3190  O O     . GLN A 1 1856 ? 217.708 222.067 258.218 1.00 11.63 ? 1856 GLN A O     1 
ATOM   3191  C CB    . GLN A 1 1856 ? 220.753 222.874 257.487 1.00 12.61 ? 1856 GLN A CB    1 
ATOM   3192  C CG    . GLN A 1 1856 ? 222.252 222.720 257.633 1.00 12.21 ? 1856 GLN A CG    1 
ATOM   3193  C CD    . GLN A 1 1856 ? 222.991 224.039 257.568 1.00 14.85 ? 1856 GLN A CD    1 
ATOM   3194  O OE1   . GLN A 1 1856 ? 222.392 225.088 257.342 1.00 21.45 ? 1856 GLN A OE1   1 
ATOM   3195  N NE2   . GLN A 1 1856 ? 224.301 223.992 257.773 1.00 14.45 ? 1856 GLN A NE2   1 
ATOM   3196  N N     . LEU A 1 1857 ? 218.123 221.624 256.058 1.00 1.54  ? 1857 LEU A N     1 
ATOM   3197  C CA    . LEU A 1 1857 ? 216.743 221.801 255.627 1.00 1.80  ? 1857 LEU A CA    1 
ATOM   3198  C C     . LEU A 1 1857 ? 216.166 220.460 255.196 1.00 5.54  ? 1857 LEU A C     1 
ATOM   3199  O O     . LEU A 1 1857 ? 216.750 219.770 254.356 1.00 14.11 ? 1857 LEU A O     1 
ATOM   3200  C CB    . LEU A 1 1857 ? 216.659 222.809 254.481 1.00 0.00  ? 1857 LEU A CB    1 
ATOM   3201  C CG    . LEU A 1 1857 ? 215.308 222.983 253.790 1.00 0.00  ? 1857 LEU A CG    1 
ATOM   3202  C CD1   . LEU A 1 1857 ? 214.221 223.341 254.784 1.00 0.84  ? 1857 LEU A CD1   1 
ATOM   3203  C CD2   . LEU A 1 1857 ? 215.418 224.041 252.720 1.00 2.25  ? 1857 LEU A CD2   1 
ATOM   3204  N N     . SER A 1 1858 ? 215.022 220.100 255.770 1.00 2.73  ? 1858 SER A N     1 
ATOM   3205  C CA    . SER A 1 1858 ? 214.340 218.852 255.464 1.00 0.00  ? 1858 SER A CA    1 
ATOM   3206  C C     . SER A 1 1858 ? 212.947 219.146 254.929 1.00 2.96  ? 1858 SER A C     1 
ATOM   3207  O O     . SER A 1 1858 ? 212.210 219.953 255.502 1.00 14.10 ? 1858 SER A O     1 
ATOM   3208  C CB    . SER A 1 1858 ? 214.244 217.958 256.699 1.00 3.22  ? 1858 SER A CB    1 
ATOM   3209  O OG    . SER A 1 1858 ? 213.241 216.972 256.533 1.00 14.40 ? 1858 SER A OG    1 
ATOM   3210  N N     . ILE A 1 1859 ? 212.590 218.485 253.832 1.00 1.26  ? 1859 ILE A N     1 
ATOM   3211  C CA    . ILE A 1 1859 ? 211.307 218.676 253.167 1.00 0.00  ? 1859 ILE A CA    1 
ATOM   3212  C C     . ILE A 1 1859 ? 210.558 217.353 253.200 1.00 3.13  ? 1859 ILE A C     1 
ATOM   3213  O O     . ILE A 1 1859 ? 211.098 216.319 252.794 1.00 13.87 ? 1859 ILE A O     1 
ATOM   3214  C CB    . ILE A 1 1859 ? 211.489 219.165 251.720 1.00 0.00  ? 1859 ILE A CB    1 
ATOM   3215  C CG1   . ILE A 1 1859 ? 212.213 220.510 251.706 1.00 0.00  ? 1859 ILE A CG1   1 
ATOM   3216  C CG2   . ILE A 1 1859 ? 210.148 219.278 251.027 1.00 0.00  ? 1859 ILE A CG2   1 
ATOM   3217  C CD1   . ILE A 1 1859 ? 212.739 220.906 250.351 1.00 0.17  ? 1859 ILE A CD1   1 
ATOM   3218  N N     . GLN A 1 1860 ? 209.319 217.386 253.685 1.00 3.56  ? 1860 GLN A N     1 
ATOM   3219  C CA    . GLN A 1 1860 ? 208.519 216.182 253.871 1.00 0.00  ? 1860 GLN A CA    1 
ATOM   3220  C C     . GLN A 1 1860 ? 207.166 216.390 253.212 1.00 0.00  ? 1860 GLN A C     1 
ATOM   3221  O O     . GLN A 1 1860 ? 206.493 217.388 253.486 1.00 5.84  ? 1860 GLN A O     1 
ATOM   3222  C CB    . GLN A 1 1860 ? 208.359 215.867 255.359 1.00 1.38  ? 1860 GLN A CB    1 
ATOM   3223  C CG    . GLN A 1 1860 ? 209.687 215.647 256.064 1.00 5.44  ? 1860 GLN A CG    1 
ATOM   3224  C CD    . GLN A 1 1860 ? 209.543 215.460 257.557 1.00 7.71  ? 1860 GLN A CD    1 
ATOM   3225  O OE1   . GLN A 1 1860 ? 208.448 215.568 258.106 1.00 15.11 ? 1860 GLN A OE1   1 
ATOM   3226  N NE2   . GLN A 1 1860 ? 210.656 215.194 258.226 1.00 6.28  ? 1860 GLN A NE2   1 
ATOM   3227  N N     . MET A 1 1861 ? 206.770 215.462 252.337 1.00 0.00  ? 1861 MET A N     1 
ATOM   3228  C CA    . MET A 1 1861 ? 205.525 215.653 251.592 1.00 0.00  ? 1861 MET A CA    1 
ATOM   3229  C C     . MET A 1 1861 ? 204.350 214.942 252.260 1.00 6.81  ? 1861 MET A C     1 
ATOM   3230  O O     . MET A 1 1861 ? 203.401 215.587 252.713 1.00 16.53 ? 1861 MET A O     1 
ATOM   3231  C CB    . MET A 1 1861 ? 205.708 215.178 250.149 1.00 1.77  ? 1861 MET A CB    1 
ATOM   3232  C CG    . MET A 1 1861 ? 204.435 215.136 249.328 1.00 0.00  ? 1861 MET A CG    1 
ATOM   3233  S SD    . MET A 1 1861 ? 204.063 216.732 248.588 1.00 0.00  ? 1861 MET A SD    1 
ATOM   3234  C CE    . MET A 1 1861 ? 202.284 216.647 248.449 1.00 1.92  ? 1861 MET A CE    1 
ATOM   3235  N N     . ALA A 1 1862 ? 204.386 213.609 252.322 1.00 1.69  ? 1862 ALA A N     1 
ATOM   3236  C CA    . ALA A 1 1862 ? 203.433 212.852 253.130 1.00 0.00  ? 1862 ALA A CA    1 
ATOM   3237  C C     . ALA A 1 1862 ? 204.137 211.973 254.153 1.00 0.39  ? 1862 ALA A C     1 
ATOM   3238  O O     . ALA A 1 1862 ? 203.899 212.111 255.356 1.00 4.56  ? 1862 ALA A O     1 
ATOM   3239  C CB    . ALA A 1 1862 ? 202.526 212.005 252.228 1.00 0.41  ? 1862 ALA A CB    1 
ATOM   3240  N N     . ASN A 1 1863 ? 205.009 211.080 253.701 1.00 2.47  ? 1863 ASN A N     1 
ATOM   3241  C CA    . ASN A 1 1863 ? 205.941 210.368 254.560 1.00 5.81  ? 1863 ASN A CA    1 
ATOM   3242  C C     . ASN A 1 1863 ? 207.358 210.416 254.030 1.00 5.63  ? 1863 ASN A C     1 
ATOM   3243  O O     . ASN A 1 1863 ? 208.272 209.937 254.712 1.00 7.48  ? 1863 ASN A O     1 
ATOM   3244  C CB    . ASN A 1 1863 ? 205.516 208.903 254.742 1.00 0.00  ? 1863 ASN A CB    1 
ATOM   3245  C CG    . ASN A 1 1863 ? 205.279 208.190 253.427 1.00 0.00  ? 1863 ASN A CG    1 
ATOM   3246  O OD1   . ASN A 1 1863 ? 206.172 208.092 252.589 1.00 1.02  ? 1863 ASN A OD1   1 
ATOM   3247  N ND2   . ASN A 1 1863 ? 204.066 207.685 253.241 1.00 4.77  ? 1863 ASN A ND2   1 
ATOM   3248  N N     . ALA A 1 1864 ? 207.565 210.964 252.837 1.00 1.35  ? 1864 ALA A N     1 
ATOM   3249  C CA    . ALA A 1 1864 ? 208.899 211.209 252.320 1.00 1.90  ? 1864 ALA A CA    1 
ATOM   3250  C C     . ALA A 1 1864 ? 209.621 212.231 253.180 1.00 4.94  ? 1864 ALA A C     1 
ATOM   3251  O O     . ALA A 1 1864 ? 208.999 213.124 253.757 1.00 13.73 ? 1864 ALA A O     1 
ATOM   3252  C CB    . ALA A 1 1864 ? 208.809 211.703 250.880 1.00 0.00  ? 1864 ALA A CB    1 
ATOM   3253  N N     . LYS A 1 1865 ? 210.936 212.087 253.283 1.00 2.26  ? 1865 LYS A N     1 
ATOM   3254  C CA    . LYS A 1 1865 ? 211.780 213.051 253.979 1.00 3.64  ? 1865 LYS A CA    1 
ATOM   3255  C C     . LYS A 1 1865 ? 213.009 213.299 253.113 1.00 12.19 ? 1865 LYS A C     1 
ATOM   3256  O O     . LYS A 1 1865 ? 214.030 212.623 253.253 1.00 22.63 ? 1865 LYS A O     1 
ATOM   3257  C CB    . LYS A 1 1865 ? 212.151 212.552 255.378 1.00 12.00 ? 1865 LYS A CB    1 
ATOM   3258  C CG    . LYS A 1 1865 ? 210.946 212.309 256.275 1.00 12.27 ? 1865 LYS A CG    1 
ATOM   3259  C CD    . LYS A 1 1865 ? 211.273 211.415 257.453 1.00 14.70 ? 1865 LYS A CD    1 
ATOM   3260  C CE    . LYS A 1 1865 ? 210.007 211.044 258.209 1.00 19.06 ? 1865 LYS A CE    1 
ATOM   3261  N NZ    . LYS A 1 1865 ? 209.105 210.182 257.396 1.00 18.30 ? 1865 LYS A NZ    1 
ATOM   3262  N N     . PHE A 1 1866 ? 212.903 214.269 252.209 1.00 2.20  ? 1866 PHE A N     1 
ATOM   3263  C CA    . PHE A 1 1866 ? 214.041 214.670 251.404 1.00 0.00  ? 1866 PHE A CA    1 
ATOM   3264  C C     . PHE A 1 1866 ? 214.833 215.763 252.105 1.00 0.93  ? 1866 PHE A C     1 
ATOM   3265  O O     . PHE A 1 1866 ? 214.287 216.604 252.822 1.00 12.00 ? 1866 PHE A O     1 
ATOM   3266  C CB    . PHE A 1 1866 ? 213.600 215.179 250.032 1.00 0.00  ? 1866 PHE A CB    1 
ATOM   3267  C CG    . PHE A 1 1866 ? 212.612 214.294 249.341 1.00 3.10  ? 1866 PHE A CG    1 
ATOM   3268  C CD1   . PHE A 1 1866 ? 213.031 213.175 248.646 1.00 1.76  ? 1866 PHE A CD1   1 
ATOM   3269  C CD2   . PHE A 1 1866 ? 211.265 214.591 249.371 1.00 2.49  ? 1866 PHE A CD2   1 
ATOM   3270  C CE1   . PHE A 1 1866 ? 212.124 212.364 248.005 1.00 0.00  ? 1866 PHE A CE1   1 
ATOM   3271  C CE2   . PHE A 1 1866 ? 210.358 213.787 248.729 1.00 2.91  ? 1866 PHE A CE2   1 
ATOM   3272  C CZ    . PHE A 1 1866 ? 210.786 212.670 248.048 1.00 4.86  ? 1866 PHE A CZ    1 
ATOM   3273  N N     . ASN A 1 1867 ? 216.141 215.743 251.887 1.00 1.33  ? 1867 ASN A N     1 
ATOM   3274  C CA    . ASN A 1 1867 ? 216.994 216.864 252.226 1.00 2.26  ? 1867 ASN A CA    1 
ATOM   3275  C C     . ASN A 1 1867 ? 216.992 217.842 251.057 1.00 3.20  ? 1867 ASN A C     1 
ATOM   3276  O O     . ASN A 1 1867 ? 216.549 217.526 249.952 1.00 7.15  ? 1867 ASN A O     1 
ATOM   3277  C CB    . ASN A 1 1867 ? 218.408 216.390 252.558 1.00 2.67  ? 1867 ASN A CB    1 
ATOM   3278  C CG    . ASN A 1 1867 ? 218.470 215.605 253.850 1.00 9.65  ? 1867 ASN A CG    1 
ATOM   3279  O OD1   . ASN A 1 1867 ? 217.516 215.587 254.626 1.00 11.90 ? 1867 ASN A OD1   1 
ATOM   3280  N ND2   . ASN A 1 1867 ? 219.598 214.947 254.088 1.00 11.96 ? 1867 ASN A ND2   1 
ATOM   3281  N N     . TYR A 1 1868 ? 217.492 219.044 251.299 1.00 2.77  ? 1868 TYR A N     1 
ATOM   3282  C CA    . TYR A 1 1868 ? 217.540 220.081 250.277 1.00 0.00  ? 1868 TYR A CA    1 
ATOM   3283  C C     . TYR A 1 1868 ? 218.936 220.092 249.675 1.00 0.00  ? 1868 TYR A C     1 
ATOM   3284  O O     . TYR A 1 1868 ? 219.919 220.343 250.378 1.00 13.33 ? 1868 TYR A O     1 
ATOM   3285  C CB    . TYR A 1 1868 ? 217.183 221.447 250.855 1.00 2.71  ? 1868 TYR A CB    1 
ATOM   3286  C CG    . TYR A 1 1868 ? 216.910 222.493 249.800 1.00 0.00  ? 1868 TYR A CG    1 
ATOM   3287  C CD1   . TYR A 1 1868 ? 215.716 222.501 249.097 1.00 1.25  ? 1868 TYR A CD1   1 
ATOM   3288  C CD2   . TYR A 1 1868 ? 217.852 223.464 249.500 1.00 0.00  ? 1868 TYR A CD2   1 
ATOM   3289  C CE1   . TYR A 1 1868 ? 215.466 223.450 248.131 1.00 1.78  ? 1868 TYR A CE1   1 
ATOM   3290  C CE2   . TYR A 1 1868 ? 217.611 224.417 248.534 1.00 0.00  ? 1868 TYR A CE2   1 
ATOM   3291  C CZ    . TYR A 1 1868 ? 216.416 224.403 247.851 1.00 0.00  ? 1868 TYR A CZ    1 
ATOM   3292  O OH    . TYR A 1 1868 ? 216.164 225.352 246.888 1.00 0.00  ? 1868 TYR A OH    1 
ATOM   3293  N N     . GLY A 1 1869 ? 219.023 219.805 248.382 1.00 0.00  ? 1869 GLY A N     1 
ATOM   3294  C CA    . GLY A 1 1869 ? 220.269 219.993 247.675 1.00 0.00  ? 1869 GLY A CA    1 
ATOM   3295  C C     . GLY A 1 1869 ? 220.526 221.473 247.512 1.00 1.54  ? 1869 GLY A C     1 
ATOM   3296  O O     . GLY A 1 1869 ? 219.846 222.146 246.735 1.00 0.70  ? 1869 GLY A O     1 
ATOM   3297  N N     . PHE A 1 1870 ? 221.497 222.002 248.249 1.00 6.20  ? 1870 PHE A N     1 
ATOM   3298  C CA    . PHE A 1 1870 ? 221.729 223.444 248.277 1.00 3.81  ? 1870 PHE A CA    1 
ATOM   3299  C C     . PHE A 1 1870 ? 222.505 223.845 247.028 1.00 5.31  ? 1870 PHE A C     1 
ATOM   3300  O O     . PHE A 1 1870 ? 223.635 224.334 247.077 1.00 3.22  ? 1870 PHE A O     1 
ATOM   3301  C CB    . PHE A 1 1870 ? 222.449 223.840 249.557 1.00 0.00  ? 1870 PHE A CB    1 
ATOM   3302  C CG    . PHE A 1 1870 ? 221.521 224.079 250.708 1.00 0.03  ? 1870 PHE A CG    1 
ATOM   3303  C CD1   . PHE A 1 1870 ? 220.643 225.147 250.689 1.00 0.47  ? 1870 PHE A CD1   1 
ATOM   3304  C CD2   . PHE A 1 1870 ? 221.501 223.220 251.789 1.00 2.50  ? 1870 PHE A CD2   1 
ATOM   3305  C CE1   . PHE A 1 1870 ? 219.781 225.368 251.737 1.00 0.00  ? 1870 PHE A CE1   1 
ATOM   3306  C CE2   . PHE A 1 1870 ? 220.636 223.435 252.840 1.00 8.17  ? 1870 PHE A CE2   1 
ATOM   3307  C CZ    . PHE A 1 1870 ? 219.777 224.511 252.814 1.00 5.57  ? 1870 PHE A CZ    1 
ATOM   3308  N N     . GLU A 1 1871 ? 221.868 223.638 245.880 1.00 0.83  ? 1871 GLU A N     1 
ATOM   3309  C CA    . GLU A 1 1871 ? 222.426 224.011 244.590 1.00 2.98  ? 1871 GLU A CA    1 
ATOM   3310  C C     . GLU A 1 1871 ? 221.663 225.223 244.081 1.00 9.49  ? 1871 GLU A C     1 
ATOM   3311  O O     . GLU A 1 1871 ? 220.427 225.217 244.062 1.00 4.69  ? 1871 GLU A O     1 
ATOM   3312  C CB    . GLU A 1 1871 ? 222.335 222.857 243.593 1.00 1.39  ? 1871 GLU A CB    1 
ATOM   3313  C CG    . GLU A 1 1871 ? 222.947 223.172 242.246 1.00 3.23  ? 1871 GLU A CG    1 
ATOM   3314  C CD    . GLU A 1 1871 ? 222.180 222.557 241.112 1.00 4.03  ? 1871 GLU A CD    1 
ATOM   3315  O OE1   . GLU A 1 1871 ? 221.070 222.051 241.367 1.00 11.26 ? 1871 GLU A OE1   1 
ATOM   3316  O OE2   . GLU A 1 1871 ? 222.684 222.579 239.971 1.00 7.16  ? 1871 GLU A OE2   1 
ATOM   3317  N N     . TYR A 1 1872 ? 222.396 226.259 243.680 1.00 11.99 ? 1872 TYR A N     1 
ATOM   3318  C CA    . TYR A 1 1872 ? 221.772 227.503 243.252 1.00 3.69  ? 1872 TYR A CA    1 
ATOM   3319  C C     . TYR A 1 1872 ? 221.016 227.269 241.953 1.00 0.00  ? 1872 TYR A C     1 
ATOM   3320  O O     . TYR A 1 1872 ? 221.611 226.875 240.948 1.00 6.68  ? 1872 TYR A O     1 
ATOM   3321  C CB    . TYR A 1 1872 ? 222.830 228.587 243.069 1.00 4.01  ? 1872 TYR A CB    1 
ATOM   3322  C CG    . TYR A 1 1872 ? 222.275 229.908 242.592 1.00 2.78  ? 1872 TYR A CG    1 
ATOM   3323  C CD1   . TYR A 1 1872 ? 221.058 230.377 243.063 1.00 7.11  ? 1872 TYR A CD1   1 
ATOM   3324  C CD2   . TYR A 1 1872 ? 222.967 230.687 241.675 1.00 3.60  ? 1872 TYR A CD2   1 
ATOM   3325  C CE1   . TYR A 1 1872 ? 220.544 231.581 242.640 1.00 7.93  ? 1872 TYR A CE1   1 
ATOM   3326  C CE2   . TYR A 1 1872 ? 222.460 231.895 241.242 1.00 4.56  ? 1872 TYR A CE2   1 
ATOM   3327  C CZ    . TYR A 1 1872 ? 221.248 232.337 241.729 1.00 9.87  ? 1872 TYR A CZ    1 
ATOM   3328  O OH    . TYR A 1 1872 ? 220.730 233.539 241.306 1.00 12.18 ? 1872 TYR A OH    1 
ATOM   3329  N N     . LEU A 1 1873 ? 219.708 227.513 241.972 1.00 0.00  ? 1873 LEU A N     1 
ATOM   3330  C CA    . LEU A 1 1873 ? 218.861 227.288 240.810 1.00 3.14  ? 1873 LEU A CA    1 
ATOM   3331  C C     . LEU A 1 1873 ? 218.780 228.488 239.880 1.00 1.39  ? 1873 LEU A C     1 
ATOM   3332  O O     . LEU A 1 1873 ? 218.232 228.363 238.782 1.00 6.18  ? 1873 LEU A O     1 
ATOM   3333  C CB    . LEU A 1 1873 ? 217.444 226.908 241.250 1.00 6.52  ? 1873 LEU A CB    1 
ATOM   3334  C CG    . LEU A 1 1873 ? 217.310 225.686 242.153 1.00 2.04  ? 1873 LEU A CG    1 
ATOM   3335  C CD1   . LEU A 1 1873 ? 215.876 225.538 242.600 1.00 0.36  ? 1873 LEU A CD1   1 
ATOM   3336  C CD2   . LEU A 1 1873 ? 217.778 224.442 241.427 1.00 0.00  ? 1873 LEU A CD2   1 
ATOM   3337  N N     . GLY A 1 1874 ? 219.307 229.625 240.276 1.00 1.05  ? 1874 GLY A N     1 
ATOM   3338  C CA    . GLY A 1 1874 ? 219.106 230.856 239.521 1.00 3.96  ? 1874 GLY A CA    1 
ATOM   3339  C C     . GLY A 1 1874 ? 217.817 231.543 239.949 1.00 8.84  ? 1874 GLY A C     1 
ATOM   3340  O O     . GLY A 1 1874 ? 217.601 231.761 241.138 1.00 12.59 ? 1874 GLY A O     1 
ATOM   3341  N N     . VAL A 1 1875 ? 216.968 231.872 238.978 1.00 6.82  ? 1875 VAL A N     1 
ATOM   3342  C CA    . VAL A 1 1875 ? 215.653 232.443 239.234 1.00 6.64  ? 1875 VAL A CA    1 
ATOM   3343  C C     . VAL A 1 1875 ? 214.544 231.522 238.741 1.00 11.31 ? 1875 VAL A C     1 
ATOM   3344  O O     . VAL A 1 1875 ? 213.519 231.351 239.409 1.00 17.37 ? 1875 VAL A O     1 
ATOM   3345  C CB    . VAL A 1 1875 ? 215.516 233.846 238.605 1.00 2.78  ? 1875 VAL A CB    1 
ATOM   3346  C CG1   . VAL A 1 1875 ? 214.207 234.484 239.029 1.00 7.35  ? 1875 VAL A CG1   1 
ATOM   3347  C CG2   . VAL A 1 1875 ? 216.688 234.717 239.013 1.00 9.95  ? 1875 VAL A CG2   1 
ATOM   3348  N N     . GLN A 1 1876 ? 214.732 230.925 237.564 1.00 12.40 ? 1876 GLN A N     1 
ATOM   3349  C CA    . GLN A 1 1876 ? 213.821 229.930 237.010 1.00 14.92 ? 1876 GLN A CA    1 
ATOM   3350  C C     . GLN A 1 1876 ? 212.408 230.470 236.851 1.00 12.10 ? 1876 GLN A C     1 
ATOM   3351  O O     . GLN A 1 1876 ? 212.180 231.682 236.922 1.00 13.26 ? 1876 GLN A O     1 
ATOM   3352  C CB    . GLN A 1 1876 ? 213.800 228.672 237.882 1.00 9.96  ? 1876 GLN A CB    1 
ATOM   3353  C CG    . GLN A 1 1876 ? 215.164 228.051 238.087 1.00 3.53  ? 1876 GLN A CG    1 
ATOM   3354  C CD    . GLN A 1 1876 ? 215.443 226.935 237.108 1.00 6.77  ? 1876 GLN A CD    1 
ATOM   3355  O OE1   . GLN A 1 1876 ? 214.608 226.612 236.265 1.00 8.19  ? 1876 GLN A OE1   1 
ATOM   3356  N NE2   . GLN A 1 1876 ? 216.627 226.347 237.205 1.00 11.02 ? 1876 GLN A NE2   1 
ATOM   3357  N N     . ASP A 1 1877 ? 211.455 229.569 236.636 1.00 7.74  ? 1877 ASP A N     1 
ATOM   3358  C CA    . ASP A 1 1877 ? 210.050 229.916 236.506 1.00 7.52  ? 1877 ASP A CA    1 
ATOM   3359  C C     . ASP A 1 1877 ? 209.239 229.012 237.416 1.00 11.42 ? 1877 ASP A C     1 
ATOM   3360  O O     . ASP A 1 1877 ? 209.510 227.813 237.521 1.00 14.04 ? 1877 ASP A O     1 
ATOM   3361  C CB    . ASP A 1 1877 ? 209.566 229.787 235.060 1.00 10.97 ? 1877 ASP A CB    1 
ATOM   3362  C CG    . ASP A 1 1877 ? 210.376 230.630 234.099 1.00 19.17 ? 1877 ASP A CG    1 
ATOM   3363  O OD1   . ASP A 1 1877 ? 211.409 230.139 233.599 1.00 18.84 ? 1877 ASP A OD1   1 
ATOM   3364  O OD2   . ASP A 1 1877 ? 209.979 231.787 233.845 1.00 16.27 ? 1877 ASP A OD2   1 
ATOM   3365  N N     . LYS A 1 1878 ? 208.243 229.595 238.067 1.00 12.29 ? 1878 LYS A N     1 
ATOM   3366  C CA    . LYS A 1 1878 ? 207.509 228.942 239.138 1.00 0.49  ? 1878 LYS A CA    1 
ATOM   3367  C C     . LYS A 1 1878 ? 206.131 228.515 238.660 1.00 6.52  ? 1878 LYS A C     1 
ATOM   3368  O O     . LYS A 1 1878 ? 205.423 229.293 238.014 1.00 13.43 ? 1878 LYS A O     1 
ATOM   3369  C CB    . LYS A 1 1878 ? 207.378 229.877 240.331 1.00 0.00  ? 1878 LYS A CB    1 
ATOM   3370  C CG    . LYS A 1 1878 ? 206.764 229.236 241.521 1.00 3.05  ? 1878 LYS A CG    1 
ATOM   3371  C CD    . LYS A 1 1878 ? 206.743 230.200 242.659 1.00 6.42  ? 1878 LYS A CD    1 
ATOM   3372  C CE    . LYS A 1 1878 ? 206.233 229.506 243.866 1.00 1.54  ? 1878 LYS A CE    1 
ATOM   3373  N NZ    . LYS A 1 1878 ? 207.110 228.365 244.247 1.00 1.02  ? 1878 LYS A NZ    1 
ATOM   3374  N N     . LEU A 1 1879 ? 205.752 227.287 238.997 1.00 5.28  ? 1879 LEU A N     1 
ATOM   3375  C CA    . LEU A 1 1879 ? 204.457 226.753 238.609 1.00 1.76  ? 1879 LEU A CA    1 
ATOM   3376  C C     . LEU A 1 1879 ? 203.411 227.049 239.673 1.00 0.00  ? 1879 LEU A C     1 
ATOM   3377  O O     . LEU A 1 1879 ? 203.709 227.073 240.870 1.00 4.22  ? 1879 LEU A O     1 
ATOM   3378  C CB    . LEU A 1 1879 ? 204.557 225.246 238.383 1.00 0.00  ? 1879 LEU A CB    1 
ATOM   3379  C CG    . LEU A 1 1879 ? 204.719 224.800 236.934 1.00 0.33  ? 1879 LEU A CG    1 
ATOM   3380  C CD1   . LEU A 1 1879 ? 206.082 225.207 236.413 1.00 6.53  ? 1879 LEU A CD1   1 
ATOM   3381  C CD2   . LEU A 1 1879 ? 204.540 223.302 236.840 1.00 1.36  ? 1879 LEU A CD2   1 
ATOM   3382  N N     . VAL A 1 1880 ? 202.177 227.283 239.228 1.00 0.37  ? 1880 VAL A N     1 
ATOM   3383  C CA    . VAL A 1 1880 ? 201.067 227.415 240.161 1.00 0.00  ? 1880 VAL A CA    1 
ATOM   3384  C C     . VAL A 1 1880 ? 200.720 226.041 240.709 1.00 1.38  ? 1880 VAL A C     1 
ATOM   3385  O O     . VAL A 1 1880 ? 200.526 225.083 239.952 1.00 1.09  ? 1880 VAL A O     1 
ATOM   3386  C CB    . VAL A 1 1880 ? 199.862 228.066 239.467 1.00 0.05  ? 1880 VAL A CB    1 
ATOM   3387  C CG1   . VAL A 1 1880 ? 198.649 228.048 240.378 1.00 0.00  ? 1880 VAL A CG1   1 
ATOM   3388  C CG2   . VAL A 1 1880 ? 200.199 229.482 239.041 1.00 0.00  ? 1880 VAL A CG2   1 
ATOM   3389  N N     . GLN A 1 1881 ? 200.640 225.935 242.033 1.00 0.00  ? 1881 GLN A N     1 
ATOM   3390  C CA    . GLN A 1 1881 ? 200.350 224.655 242.676 1.00 0.00  ? 1881 GLN A CA    1 
ATOM   3391  C C     . GLN A 1 1881 ? 198.856 224.385 242.579 1.00 0.21  ? 1881 GLN A C     1 
ATOM   3392  O O     . GLN A 1 1881 ? 198.097 224.585 243.527 1.00 4.18  ? 1881 GLN A O     1 
ATOM   3393  C CB    . GLN A 1 1881 ? 200.826 224.653 244.121 1.00 3.94  ? 1881 GLN A CB    1 
ATOM   3394  C CG    . GLN A 1 1881 ? 202.328 224.706 244.258 1.00 3.82  ? 1881 GLN A CG    1 
ATOM   3395  C CD    . GLN A 1 1881 ? 202.958 223.333 244.180 1.00 0.81  ? 1881 GLN A CD    1 
ATOM   3396  O OE1   . GLN A 1 1881 ? 202.540 222.405 244.871 1.00 0.00  ? 1881 GLN A OE1   1 
ATOM   3397  N NE2   . GLN A 1 1881 ? 203.968 223.194 243.331 1.00 7.25  ? 1881 GLN A NE2   1 
ATOM   3398  N N     . THR A 1 1882 ? 198.434 223.931 241.408 1.00 0.00  ? 1882 THR A N     1 
ATOM   3399  C CA    . THR A 1 1882 ? 197.069 223.486 241.190 1.00 0.90  ? 1882 THR A CA    1 
ATOM   3400  C C     . THR A 1 1882 ? 196.870 222.125 241.842 1.00 5.90  ? 1882 THR A C     1 
ATOM   3401  O O     . THR A 1 1882 ? 197.837 221.446 242.188 1.00 13.11 ? 1882 THR A O     1 
ATOM   3402  C CB    . THR A 1 1882 ? 196.781 223.436 239.692 1.00 2.05  ? 1882 THR A CB    1 
ATOM   3403  O OG1   . THR A 1 1882 ? 197.634 222.469 239.069 1.00 0.63  ? 1882 THR A OG1   1 
ATOM   3404  C CG2   . THR A 1 1882 ? 197.029 224.789 239.072 1.00 3.47  ? 1882 THR A CG2   1 
ATOM   3405  N N     . PRO A 1 1883 ? 195.619 221.706 242.053 1.00 4.81  ? 1883 PRO A N     1 
ATOM   3406  C CA    . PRO A 1 1883 ? 195.395 220.363 242.614 1.00 7.18  ? 1883 PRO A CA    1 
ATOM   3407  C C     . PRO A 1 1883 ? 196.033 219.258 241.791 1.00 0.26  ? 1883 PRO A C     1 
ATOM   3408  O O     . PRO A 1 1883 ? 196.493 218.259 242.356 1.00 3.69  ? 1883 PRO A O     1 
ATOM   3409  C CB    . PRO A 1 1883 ? 193.863 220.246 242.645 1.00 8.31  ? 1883 PRO A CB    1 
ATOM   3410  C CG    . PRO A 1 1883 ? 193.355 221.373 241.807 1.00 14.01 ? 1883 PRO A CG    1 
ATOM   3411  C CD    . PRO A 1 1883 ? 194.361 222.458 241.942 1.00 10.71 ? 1883 PRO A CD    1 
ATOM   3412  N N     . LEU A 1 1884 ? 196.083 219.411 240.467 1.00 6.67  ? 1884 LEU A N     1 
ATOM   3413  C CA    . LEU A 1 1884 ? 196.804 218.447 239.644 1.00 4.47  ? 1884 LEU A CA    1 
ATOM   3414  C C     . LEU A 1 1884 ? 198.294 218.466 239.959 1.00 0.00  ? 1884 LEU A C     1 
ATOM   3415  O O     . LEU A 1 1884 ? 198.934 217.412 240.031 1.00 4.58  ? 1884 LEU A O     1 
ATOM   3416  C CB    . LEU A 1 1884 ? 196.564 218.732 238.163 1.00 1.51  ? 1884 LEU A CB    1 
ATOM   3417  C CG    . LEU A 1 1884 ? 197.030 217.635 237.205 1.00 0.76  ? 1884 LEU A CG    1 
ATOM   3418  C CD1   . LEU A 1 1884 ? 196.191 216.383 237.383 1.00 4.34  ? 1884 LEU A CD1   1 
ATOM   3419  C CD2   . LEU A 1 1884 ? 196.976 218.115 235.769 1.00 5.00  ? 1884 LEU A CD2   1 
ATOM   3420  N N     . THR A 1 1885 ? 198.863 219.656 240.157 1.00 0.00  ? 1885 THR A N     1 
ATOM   3421  C CA    . THR A 1 1885 ? 200.274 219.745 240.521 1.00 1.31  ? 1885 THR A CA    1 
ATOM   3422  C C     . THR A 1 1885 ? 200.521 219.167 241.908 1.00 7.27  ? 1885 THR A C     1 
ATOM   3423  O O     . THR A 1 1885 ? 201.561 218.546 242.154 1.00 7.23  ? 1885 THR A O     1 
ATOM   3424  C CB    . THR A 1 1885 ? 200.746 221.196 240.451 1.00 0.92  ? 1885 THR A CB    1 
ATOM   3425  O OG1   . THR A 1 1885 ? 200.400 221.746 239.175 1.00 8.27  ? 1885 THR A OG1   1 
ATOM   3426  C CG2   . THR A 1 1885 ? 202.254 221.273 240.626 1.00 0.00  ? 1885 THR A CG2   1 
ATOM   3427  N N     . ASP A 1 1886 ? 199.578 219.360 242.831 1.00 6.59  ? 1886 ASP A N     1 
ATOM   3428  C CA    . ASP A 1 1886 ? 199.714 218.773 244.160 1.00 0.00  ? 1886 ASP A CA    1 
ATOM   3429  C C     . ASP A 1 1886 ? 199.668 217.251 244.094 1.00 6.30  ? 1886 ASP A C     1 
ATOM   3430  O O     . ASP A 1 1886 ? 200.446 216.563 244.766 1.00 9.64  ? 1886 ASP A O     1 
ATOM   3431  C CB    . ASP A 1 1886 ? 198.619 219.307 245.082 1.00 0.00  ? 1886 ASP A CB    1 
ATOM   3432  C CG    . ASP A 1 1886 ? 198.890 220.721 245.545 1.00 6.50  ? 1886 ASP A CG    1 
ATOM   3433  O OD1   . ASP A 1 1886 ? 199.949 220.952 246.165 1.00 12.55 ? 1886 ASP A OD1   1 
ATOM   3434  O OD2   . ASP A 1 1886 ? 198.042 221.602 245.294 1.00 9.18  ? 1886 ASP A OD2   1 
ATOM   3435  N N     . ARG A 1 1887 ? 198.751 216.706 243.289 1.00 7.49  ? 1887 ARG A N     1 
ATOM   3436  C CA    . ARG A 1 1887 ? 198.697 215.259 243.109 1.00 1.08  ? 1887 ARG A CA    1 
ATOM   3437  C C     . ARG A 1 1887 ? 199.976 214.739 242.471 1.00 0.00  ? 1887 ARG A C     1 
ATOM   3438  O O     . ARG A 1 1887 ? 200.478 213.674 242.848 1.00 1.86  ? 1887 ARG A O     1 
ATOM   3439  C CB    . ARG A 1 1887 ? 197.479 214.869 242.271 1.00 0.00  ? 1887 ARG A CB    1 
ATOM   3440  C CG    . ARG A 1 1887 ? 197.431 213.384 241.961 1.00 6.32  ? 1887 ARG A CG    1 
ATOM   3441  C CD    . ARG A 1 1887 ? 196.520 213.047 240.799 1.00 8.28  ? 1887 ARG A CD    1 
ATOM   3442  N NE    . ARG A 1 1887 ? 195.185 212.665 241.238 1.00 11.25 ? 1887 ARG A NE    1 
ATOM   3443  C CZ    . ARG A 1 1887 ? 194.389 211.840 240.573 1.00 6.59  ? 1887 ARG A CZ    1 
ATOM   3444  N NH1   . ARG A 1 1887 ? 194.773 211.272 239.442 1.00 6.26  ? 1887 ARG A NH1   1 
ATOM   3445  N NH2   . ARG A 1 1887 ? 193.181 211.571 241.057 1.00 5.65  ? 1887 ARG A NH2   1 
ATOM   3446  N N     . CYS A 1 1888 ? 200.516 215.474 241.496 1.00 0.00  ? 1888 CYS A N     1 
ATOM   3447  C CA    . CYS A 1 1888 ? 201.781 215.081 240.889 1.00 0.00  ? 1888 CYS A CA    1 
ATOM   3448  C C     . CYS A 1 1888 ? 202.905 215.082 241.913 1.00 1.67  ? 1888 CYS A C     1 
ATOM   3449  O O     . CYS A 1 1888 ? 203.715 214.153 241.954 1.00 4.85  ? 1888 CYS A O     1 
ATOM   3450  C CB    . CYS A 1 1888 ? 202.120 216.008 239.724 1.00 6.21  ? 1888 CYS A CB    1 
ATOM   3451  S SG    . CYS A 1 1888 ? 203.655 215.592 238.862 1.00 5.07  ? 1888 CYS A SG    1 
ATOM   3452  N N     . TYR A 1 1889 ? 202.964 216.114 242.755 1.00 0.00  ? 1889 TYR A N     1 
ATOM   3453  C CA    . TYR A 1 1889 ? 203.978 216.164 243.801 1.00 1.13  ? 1889 TYR A CA    1 
ATOM   3454  C C     . TYR A 1 1889 ? 203.857 214.966 244.730 1.00 1.35  ? 1889 TYR A C     1 
ATOM   3455  O O     . TYR A 1 1889 ? 204.849 214.292 245.028 1.00 0.49  ? 1889 TYR A O     1 
ATOM   3456  C CB    . TYR A 1 1889 ? 203.845 217.468 244.589 1.00 3.20  ? 1889 TYR A CB    1 
ATOM   3457  C CG    . TYR A 1 1889 ? 204.666 218.615 244.049 1.00 4.37  ? 1889 TYR A CG    1 
ATOM   3458  C CD1   . TYR A 1 1889 ? 204.972 218.704 242.699 1.00 6.64  ? 1889 TYR A CD1   1 
ATOM   3459  C CD2   . TYR A 1 1889 ? 205.127 219.613 244.891 1.00 3.74  ? 1889 TYR A CD2   1 
ATOM   3460  C CE1   . TYR A 1 1889 ? 205.719 219.752 242.207 1.00 0.03  ? 1889 TYR A CE1   1 
ATOM   3461  C CE2   . TYR A 1 1889 ? 205.875 220.663 244.407 1.00 9.22  ? 1889 TYR A CE2   1 
ATOM   3462  C CZ    . TYR A 1 1889 ? 206.168 220.728 243.066 1.00 4.33  ? 1889 TYR A CZ    1 
ATOM   3463  O OH    . TYR A 1 1889 ? 206.912 221.778 242.585 1.00 7.81  ? 1889 TYR A OH    1 
ATOM   3464  N N     . LEU A 1 1890 ? 202.634 214.675 245.181 1.00 3.41  ? 1890 LEU A N     1 
ATOM   3465  C CA    . LEU A 1 1890 ? 202.415 213.560 246.096 1.00 0.00  ? 1890 LEU A CA    1 
ATOM   3466  C C     . LEU A 1 1890 ? 202.837 212.240 245.465 1.00 0.00  ? 1890 LEU A C     1 
ATOM   3467  O O     . LEU A 1 1890 ? 203.583 211.458 246.066 1.00 4.82  ? 1890 LEU A O     1 
ATOM   3468  C CB    . LEU A 1 1890 ? 200.944 213.515 246.509 1.00 0.03  ? 1890 LEU A CB    1 
ATOM   3469  C CG    . LEU A 1 1890 ? 200.521 212.451 247.519 1.00 0.29  ? 1890 LEU A CG    1 
ATOM   3470  C CD1   . LEU A 1 1890 ? 201.397 212.511 248.755 1.00 0.00  ? 1890 LEU A CD1   1 
ATOM   3471  C CD2   . LEU A 1 1890 ? 199.057 212.617 247.884 1.00 0.00  ? 1890 LEU A CD2   1 
ATOM   3472  N N     . THR A 1 1891 ? 202.380 211.984 244.238 1.00 1.00  ? 1891 THR A N     1 
ATOM   3473  C CA    . THR A 1 1891 ? 202.680 210.720 243.577 1.00 0.00  ? 1891 THR A CA    1 
ATOM   3474  C C     . THR A 1 1891 ? 204.169 210.569 243.300 1.00 0.16  ? 1891 THR A C     1 
ATOM   3475  O O     . THR A 1 1891 ? 204.736 209.492 243.517 1.00 6.68  ? 1891 THR A O     1 
ATOM   3476  C CB    . THR A 1 1891 ? 201.882 210.609 242.283 1.00 0.00  ? 1891 THR A CB    1 
ATOM   3477  O OG1   . THR A 1 1891 ? 200.509 210.916 242.549 1.00 0.10  ? 1891 THR A OG1   1 
ATOM   3478  C CG2   . THR A 1 1891 ? 201.984 209.207 241.716 1.00 0.00  ? 1891 THR A CG2   1 
ATOM   3479  N N     . MET A 1 1892 ? 204.825 211.630 242.824 1.00 0.00  ? 1892 MET A N     1 
ATOM   3480  C CA    . MET A 1 1892 ? 206.244 211.525 242.510 1.00 0.00  ? 1892 MET A CA    1 
ATOM   3481  C C     . MET A 1 1892 ? 207.080 211.367 243.772 1.00 3.60  ? 1892 MET A C     1 
ATOM   3482  O O     . MET A 1 1892 ? 208.063 210.622 243.778 1.00 12.38 ? 1892 MET A O     1 
ATOM   3483  C CB    . MET A 1 1892 ? 206.703 212.738 241.704 1.00 2.47  ? 1892 MET A CB    1 
ATOM   3484  C CG    . MET A 1 1892 ? 205.982 212.932 240.380 1.00 8.97  ? 1892 MET A CG    1 
ATOM   3485  S SD    . MET A 1 1892 ? 206.042 211.493 239.301 1.00 16.87 ? 1892 MET A SD    1 
ATOM   3486  C CE    . MET A 1 1892 ? 204.357 210.903 239.401 1.00 1.81  ? 1892 MET A CE    1 
ATOM   3487  N N     . THR A 1 1893 ? 206.705 212.049 244.857 1.00 6.35  ? 1893 THR A N     1 
ATOM   3488  C CA    . THR A 1 1893 ? 207.425 211.867 246.113 1.00 0.05  ? 1893 THR A CA    1 
ATOM   3489  C C     . THR A 1 1893 ? 207.238 210.454 246.653 1.00 2.59  ? 1893 THR A C     1 
ATOM   3490  O O     . THR A 1 1893 ? 208.183 209.853 247.182 1.00 7.51  ? 1893 THR A O     1 
ATOM   3491  C CB    . THR A 1 1893 ? 206.964 212.905 247.133 1.00 1.24  ? 1893 THR A CB    1 
ATOM   3492  O OG1   . THR A 1 1893 ? 205.535 212.992 247.113 1.00 0.44  ? 1893 THR A OG1   1 
ATOM   3493  C CG2   . THR A 1 1893 ? 207.544 214.267 246.794 1.00 0.00  ? 1893 THR A CG2   1 
ATOM   3494  N N     . GLN A 1 1894 ? 206.026 209.908 246.528 1.00 0.69  ? 1894 GLN A N     1 
ATOM   3495  C CA    . GLN A 1 1894 ? 205.792 208.531 246.949 1.00 0.00  ? 1894 GLN A CA    1 
ATOM   3496  C C     . GLN A 1 1894 ? 206.615 207.558 246.116 1.00 3.24  ? 1894 GLN A C     1 
ATOM   3497  O O     . GLN A 1 1894 ? 207.158 206.581 246.643 1.00 6.08  ? 1894 GLN A O     1 
ATOM   3498  C CB    . GLN A 1 1894 ? 204.305 208.204 246.849 1.00 0.00  ? 1894 GLN A CB    1 
ATOM   3499  C CG    . GLN A 1 1894 ? 203.480 208.792 247.972 1.00 0.00  ? 1894 GLN A CG    1 
ATOM   3500  C CD    . GLN A 1 1894 ? 203.815 208.186 249.313 1.00 1.52  ? 1894 GLN A CD    1 
ATOM   3501  O OE1   . GLN A 1 1894 ? 203.886 208.885 250.322 1.00 9.99  ? 1894 GLN A OE1   1 
ATOM   3502  N NE2   . GLN A 1 1894 ? 204.016 206.876 249.335 1.00 5.70  ? 1894 GLN A NE2   1 
ATOM   3503  N N     . ALA A 1 1895 ? 206.716 207.810 244.811 1.00 5.46  ? 1895 ALA A N     1 
ATOM   3504  C CA    . ALA A 1 1895 ? 207.572 206.994 243.959 1.00 0.00  ? 1895 ALA A CA    1 
ATOM   3505  C C     . ALA A 1 1895 ? 209.032 207.115 244.369 1.00 0.00  ? 1895 ALA A C     1 
ATOM   3506  O O     . ALA A 1 1895 ? 209.788 206.140 244.298 1.00 10.08 ? 1895 ALA A O     1 
ATOM   3507  C CB    . ALA A 1 1895 ? 207.391 207.396 242.497 1.00 0.00  ? 1895 ALA A CB    1 
ATOM   3508  N N     . LEU A 1 1896 ? 209.452 208.311 244.785 1.00 0.00  ? 1896 LEU A N     1 
ATOM   3509  C CA    . LEU A 1 1896 ? 210.834 208.510 245.206 1.00 6.23  ? 1896 LEU A CA    1 
ATOM   3510  C C     . LEU A 1 1896 ? 211.152 207.767 246.498 1.00 2.71  ? 1896 LEU A C     1 
ATOM   3511  O O     . LEU A 1 1896 ? 212.258 207.234 246.642 1.00 0.64  ? 1896 LEU A O     1 
ATOM   3512  C CB    . LEU A 1 1896 ? 211.127 210.001 245.361 1.00 9.88  ? 1896 LEU A CB    1 
ATOM   3513  C CG    . LEU A 1 1896 ? 211.142 210.816 244.068 1.00 4.48  ? 1896 LEU A CG    1 
ATOM   3514  C CD1   . LEU A 1 1896 ? 211.106 212.302 244.366 1.00 13.88 ? 1896 LEU A CD1   1 
ATOM   3515  C CD2   . LEU A 1 1896 ? 212.360 210.467 243.242 1.00 0.72  ? 1896 LEU A CD2   1 
ATOM   3516  N N     . GLU A 1 1897 ? 210.217 207.730 247.452 1.00 5.56  ? 1897 GLU A N     1 
ATOM   3517  C CA    . GLU A 1 1897 ? 210.465 206.966 248.673 1.00 4.90  ? 1897 GLU A CA    1 
ATOM   3518  C C     . GLU A 1 1897 ? 210.501 205.470 248.406 1.00 9.14  ? 1897 GLU A C     1 
ATOM   3519  O O     . GLU A 1 1897 ? 211.330 204.752 248.978 1.00 9.62  ? 1897 GLU A O     1 
ATOM   3520  C CB    . GLU A 1 1897 ? 209.419 207.282 249.735 1.00 0.11  ? 1897 GLU A CB    1 
ATOM   3521  C CG    . GLU A 1 1897 ? 209.825 208.417 250.615 1.00 7.89  ? 1897 GLU A CG    1 
ATOM   3522  C CD    . GLU A 1 1897 ? 210.717 207.975 251.760 1.00 8.55  ? 1897 GLU A CD    1 
ATOM   3523  O OE1   . GLU A 1 1897 ? 210.452 206.903 252.341 1.00 7.17  ? 1897 GLU A OE1   1 
ATOM   3524  O OE2   . GLU A 1 1897 ? 211.685 208.697 252.076 1.00 7.47  ? 1897 GLU A OE2   1 
ATOM   3525  N N     . ALA A 1 1898 ? 209.614 204.979 247.549 1.00 4.38  ? 1898 ALA A N     1 
ATOM   3526  C CA    . ALA A 1 1898 ? 209.605 203.570 247.187 1.00 1.28  ? 1898 ALA A CA    1 
ATOM   3527  C C     . ALA A 1 1898 ? 210.813 203.172 246.354 1.00 7.25  ? 1898 ALA A C     1 
ATOM   3528  O O     . ALA A 1 1898 ? 210.884 202.021 245.910 1.00 10.44 ? 1898 ALA A O     1 
ATOM   3529  C CB    . ALA A 1 1898 ? 208.320 203.231 246.431 1.00 1.30  ? 1898 ALA A CB    1 
ATOM   3530  N N     . ARG A 1 1899 ? 211.757 204.092 246.140 1.00 4.73  ? 1899 ARG A N     1 
ATOM   3531  C CA    . ARG A 1 1899 ? 212.892 203.884 245.245 1.00 0.00  ? 1899 ARG A CA    1 
ATOM   3532  C C     . ARG A 1 1899 ? 212.428 203.512 243.844 1.00 1.21  ? 1899 ARG A C     1 
ATOM   3533  O O     . ARG A 1 1899 ? 213.126 202.814 243.106 1.00 8.91  ? 1899 ARG A O     1 
ATOM   3534  C CB    . ARG A 1 1899 ? 213.856 202.834 245.800 1.00 4.21  ? 1899 ARG A CB    1 
ATOM   3535  C CG    . ARG A 1 1899 ? 214.625 203.297 247.020 1.00 4.57  ? 1899 ARG A CG    1 
ATOM   3536  C CD    . ARG A 1 1899 ? 215.430 204.543 246.702 1.00 7.43  ? 1899 ARG A CD    1 
ATOM   3537  N NE    . ARG A 1 1899 ? 216.111 205.075 247.875 1.00 9.69  ? 1899 ARG A NE    1 
ATOM   3538  C CZ    . ARG A 1 1899 ? 216.746 206.237 247.907 1.00 6.75  ? 1899 ARG A CZ    1 
ATOM   3539  N NH1   . ARG A 1 1899 ? 216.814 207.016 246.841 1.00 7.25  ? 1899 ARG A NH1   1 
ATOM   3540  N NH2   . ARG A 1 1899 ? 217.332 206.626 249.036 1.00 6.35  ? 1899 ARG A NH2   1 
ATOM   3541  N N     . LEU A 1 1900 ? 211.243 203.979 243.478 1.00 0.61  ? 1900 LEU A N     1 
ATOM   3542  C CA    . LEU A 1 1900 ? 210.693 203.811 242.150 1.00 0.11  ? 1900 LEU A CA    1 
ATOM   3543  C C     . LEU A 1 1900 ? 210.904 205.097 241.364 1.00 0.00  ? 1900 LEU A C     1 
ATOM   3544  O O     . LEU A 1 1900 ? 211.428 206.089 241.876 1.00 0.00  ? 1900 LEU A O     1 
ATOM   3545  C CB    . LEU A 1 1900 ? 209.213 203.435 242.239 1.00 0.58  ? 1900 LEU A CB    1 
ATOM   3546  C CG    . LEU A 1 1900 ? 208.899 202.058 242.821 1.00 0.08  ? 1900 LEU A CG    1 
ATOM   3547  C CD1   . LEU A 1 1900 ? 207.407 201.829 242.875 1.00 0.75  ? 1900 LEU A CD1   1 
ATOM   3548  C CD2   . LEU A 1 1900 ? 209.573 200.981 241.997 1.00 3.64  ? 1900 LEU A CD2   1 
ATOM   3549  N N     . GLY A 1 1901 ? 210.495 205.086 240.095 1.00 0.31  ? 1901 GLY A N     1 
ATOM   3550  C CA    . GLY A 1 1901 ? 210.527 206.264 239.265 1.00 0.00  ? 1901 GLY A CA    1 
ATOM   3551  C C     . GLY A 1 1901 ? 209.117 206.784 239.039 1.00 0.00  ? 1901 GLY A C     1 
ATOM   3552  O O     . GLY A 1 1901 ? 208.124 206.086 239.269 1.00 2.77  ? 1901 GLY A O     1 
ATOM   3553  N N     . GLY A 1 1902 ? 209.042 208.033 238.595 1.00 0.00  ? 1902 GLY A N     1 
ATOM   3554  C CA    . GLY A 1 1902 ? 207.784 208.667 238.258 1.00 0.00  ? 1902 GLY A CA    1 
ATOM   3555  C C     . GLY A 1 1902 ? 207.614 208.712 236.749 1.00 0.00  ? 1902 GLY A C     1 
ATOM   3556  O O     . GLY A 1 1902 ? 208.554 209.025 236.021 1.00 6.37  ? 1902 GLY A O     1 
ATOM   3557  N N     . SER A 1 1903 ? 206.409 208.384 236.298 1.00 0.00  ? 1903 SER A N     1 
ATOM   3558  C CA    . SER A 1 1903 ? 206.084 208.358 234.874 1.00 0.00  ? 1903 SER A CA    1 
ATOM   3559  C C     . SER A 1 1903 ? 204.784 209.108 234.627 1.00 4.42  ? 1903 SER A C     1 
ATOM   3560  O O     . SER A 1 1903 ? 203.729 208.498 234.424 1.00 11.27 ? 1903 SER A O     1 
ATOM   3561  C CB    . SER A 1 1903 ? 205.990 206.923 234.359 1.00 0.00  ? 1903 SER A CB    1 
ATOM   3562  O OG    . SER A 1 1903 ? 205.617 206.903 232.994 1.00 2.90  ? 1903 SER A OG    1 
ATOM   3563  N N     . PRO A 1 1904 ? 204.821 210.440 234.643 1.00 0.00  ? 1904 PRO A N     1 
ATOM   3564  C CA    . PRO A 1 1904 ? 203.633 211.206 234.249 1.00 1.42  ? 1904 PRO A CA    1 
ATOM   3565  C C     . PRO A 1 1904 ? 203.292 210.937 232.792 1.00 1.72  ? 1904 PRO A C     1 
ATOM   3566  O O     . PRO A 1 1904 ? 204.180 210.829 231.945 1.00 10.24 ? 1904 PRO A O     1 
ATOM   3567  C CB    . PRO A 1 1904 ? 204.060 212.663 234.469 1.00 4.80  ? 1904 PRO A CB    1 
ATOM   3568  C CG    . PRO A 1 1904 ? 205.271 212.583 235.345 1.00 6.40  ? 1904 PRO A CG    1 
ATOM   3569  C CD    . PRO A 1 1904 ? 205.956 211.325 234.939 1.00 0.59  ? 1904 PRO A CD    1 
ATOM   3570  N N     . PHE A 1 1905 ? 202.003 210.833 232.499 1.00 0.00  ? 1905 PHE A N     1 
ATOM   3571  C CA    . PHE A 1 1905 ? 201.551 210.640 231.133 1.00 0.39  ? 1905 PHE A CA    1 
ATOM   3572  C C     . PHE A 1 1905 ? 200.309 211.480 230.875 1.00 1.78  ? 1905 PHE A C     1 
ATOM   3573  O O     . PHE A 1 1905 ? 199.584 211.861 231.797 1.00 9.65  ? 1905 PHE A O     1 
ATOM   3574  C CB    . PHE A 1 1905 ? 201.280 209.156 230.827 1.00 8.88  ? 1905 PHE A CB    1 
ATOM   3575  C CG    . PHE A 1 1905 ? 200.171 208.548 231.642 1.00 5.21  ? 1905 PHE A CG    1 
ATOM   3576  C CD1   . PHE A 1 1905 ? 198.863 208.577 231.191 1.00 5.23  ? 1905 PHE A CD1   1 
ATOM   3577  C CD2   . PHE A 1 1905 ? 200.441 207.932 232.848 1.00 11.19 ? 1905 PHE A CD2   1 
ATOM   3578  C CE1   . PHE A 1 1905 ? 197.848 208.016 231.934 1.00 4.99  ? 1905 PHE A CE1   1 
ATOM   3579  C CE2   . PHE A 1 1905 ? 199.428 207.370 233.595 1.00 4.73  ? 1905 PHE A CE2   1 
ATOM   3580  C CZ    . PHE A 1 1905 ? 198.132 207.410 233.135 1.00 3.06  ? 1905 PHE A CZ    1 
ATOM   3581  N N     . GLY A 1 1906 ? 200.082 211.779 229.602 1.00 0.00  ? 1906 GLY A N     1 
ATOM   3582  C CA    . GLY A 1 1906 ? 198.958 212.582 229.194 1.00 0.00  ? 1906 GLY A CA    1 
ATOM   3583  C C     . GLY A 1 1906 ? 199.271 213.364 227.938 1.00 0.63  ? 1906 GLY A C     1 
ATOM   3584  O O     . GLY A 1 1906 ? 200.369 213.274 227.384 1.00 5.45  ? 1906 GLY A O     1 
ATOM   3585  N N     . PRO A 1 1907 ? 198.306 214.149 227.464 1.00 0.00  ? 1907 PRO A N     1 
ATOM   3586  C CA    . PRO A 1 1907 ? 198.531 214.945 226.253 1.00 0.00  ? 1907 PRO A CA    1 
ATOM   3587  C C     . PRO A 1 1907 ? 199.640 215.966 226.458 1.00 1.93  ? 1907 PRO A C     1 
ATOM   3588  O O     . PRO A 1 1907 ? 199.882 216.434 227.572 1.00 16.00 ? 1907 PRO A O     1 
ATOM   3589  C CB    . PRO A 1 1907 ? 197.178 215.623 226.023 1.00 2.91  ? 1907 PRO A CB    1 
ATOM   3590  C CG    . PRO A 1 1907 ? 196.196 214.732 226.706 1.00 2.88  ? 1907 PRO A CG    1 
ATOM   3591  C CD    . PRO A 1 1907 ? 196.911 214.234 227.923 1.00 0.75  ? 1907 PRO A CD    1 
ATOM   3592  N N     . ALA A 1 1908 ? 200.324 216.301 225.368 1.00 1.00  ? 1908 ALA A N     1 
ATOM   3593  C CA    . ALA A 1 1908 ? 201.387 217.293 225.434 1.00 1.89  ? 1908 ALA A CA    1 
ATOM   3594  C C     . ALA A 1 1908 ? 200.820 218.658 225.801 1.00 5.08  ? 1908 ALA A C     1 
ATOM   3595  O O     . ALA A 1 1908 ? 199.715 219.022 225.390 1.00 9.96  ? 1908 ALA A O     1 
ATOM   3596  C CB    . ALA A 1 1908 ? 202.126 217.370 224.099 1.00 2.34  ? 1908 ALA A CB    1 
ATOM   3597  N N     . GLY A 1 1909 ? 201.585 219.415 226.585 1.00 3.13  ? 1909 GLY A N     1 
ATOM   3598  C CA    . GLY A 1 1909 ? 201.195 220.737 227.025 1.00 7.70  ? 1909 GLY A CA    1 
ATOM   3599  C C     . GLY A 1 1909 ? 200.489 220.766 228.362 1.00 9.66  ? 1909 GLY A C     1 
ATOM   3600  O O     . GLY A 1 1909 ? 200.091 221.848 228.812 1.00 13.54 ? 1909 GLY A O     1 
ATOM   3601  N N     . THR A 1 1910 ? 200.312 219.612 229.005 1.00 7.00  ? 1910 THR A N     1 
ATOM   3602  C CA    . THR A 1 1910 ? 199.632 219.580 230.296 1.00 4.56  ? 1910 THR A CA    1 
ATOM   3603  C C     . THR A 1 1910 ? 200.534 220.108 231.407 1.00 5.68  ? 1910 THR A C     1 
ATOM   3604  O O     . THR A 1 1910 ? 200.083 220.842 232.293 1.00 12.95 ? 1910 THR A O     1 
ATOM   3605  C CB    . THR A 1 1910 ? 199.163 218.160 230.607 1.00 0.97  ? 1910 THR A CB    1 
ATOM   3606  O OG1   . THR A 1 1910 ? 198.211 217.744 229.621 1.00 0.14  ? 1910 THR A OG1   1 
ATOM   3607  C CG2   . THR A 1 1910 ? 198.511 218.111 231.976 1.00 10.63 ? 1910 THR A CG2   1 
ATOM   3608  N N     . GLY A 1 1911 ? 201.815 219.758 231.370 1.00 0.00  ? 1911 GLY A N     1 
ATOM   3609  C CA    . GLY A 1 1911 ? 202.740 220.229 232.380 1.00 0.00  ? 1911 GLY A CA    1 
ATOM   3610  C C     . GLY A 1 1911 ? 203.485 219.128 233.102 1.00 0.00  ? 1911 GLY A C     1 
ATOM   3611  O O     . GLY A 1 1911 ? 203.957 219.327 234.223 1.00 1.76  ? 1911 GLY A O     1 
ATOM   3612  N N     . LYS A 1 1912 ? 203.608 217.963 232.465 1.00 2.02  ? 1912 LYS A N     1 
ATOM   3613  C CA    . LYS A 1 1912 ? 204.299 216.840 233.090 1.00 0.00  ? 1912 LYS A CA    1 
ATOM   3614  C C     . LYS A 1 1912 ? 205.774 217.150 233.309 1.00 0.00  ? 1912 LYS A C     1 
ATOM   3615  O O     . LYS A 1 1912 ? 206.296 217.001 234.422 1.00 2.16  ? 1912 LYS A O     1 
ATOM   3616  C CB    . LYS A 1 1912 ? 204.128 215.591 232.228 1.00 1.49  ? 1912 LYS A CB    1 
ATOM   3617  C CG    . LYS A 1 1912 ? 202.699 215.364 231.768 1.00 3.29  ? 1912 LYS A CG    1 
ATOM   3618  C CD    . LYS A 1 1912 ? 202.601 214.223 230.778 1.00 3.96  ? 1912 LYS A CD    1 
ATOM   3619  C CE    . LYS A 1 1912 ? 203.365 214.520 229.507 1.00 1.91  ? 1912 LYS A CE    1 
ATOM   3620  N NZ    . LYS A 1 1912 ? 202.540 215.326 228.567 1.00 3.15  ? 1912 LYS A NZ    1 
ATOM   3621  N N     . THR A 1 1913 ? 206.464 217.590 232.256 1.00 0.00  ? 1913 THR A N     1 
ATOM   3622  C CA    . THR A 1 1913 ? 207.881 217.912 232.380 1.00 0.00  ? 1913 THR A CA    1 
ATOM   3623  C C     . THR A 1 1913 ? 208.096 219.097 233.312 1.00 1.61  ? 1913 THR A C     1 
ATOM   3624  O O     . THR A 1 1913 ? 209.009 219.085 234.144 1.00 3.22  ? 1913 THR A O     1 
ATOM   3625  C CB    . THR A 1 1913 ? 208.477 218.194 231.002 1.00 1.01  ? 1913 THR A CB    1 
ATOM   3626  O OG1   . THR A 1 1913 ? 208.568 216.970 230.265 1.00 6.34  ? 1913 THR A OG1   1 
ATOM   3627  C CG2   . THR A 1 1913 ? 209.863 218.800 231.129 1.00 2.28  ? 1913 THR A CG2   1 
ATOM   3628  N N     . GLU A 1 1914 ? 207.255 220.125 233.196 1.00 6.13  ? 1914 GLU A N     1 
ATOM   3629  C CA    . GLU A 1 1914 ? 207.394 221.286 234.067 1.00 0.00  ? 1914 GLU A CA    1 
ATOM   3630  C C     . GLU A 1 1914 ? 207.077 220.943 235.515 1.00 6.33  ? 1914 GLU A C     1 
ATOM   3631  O O     . GLU A 1 1914 ? 207.716 221.470 236.426 1.00 13.93 ? 1914 GLU A O     1 
ATOM   3632  C CB    . GLU A 1 1914 ? 206.511 222.431 233.577 1.00 0.00  ? 1914 GLU A CB    1 
ATOM   3633  C CG    . GLU A 1 1914 ? 207.096 223.201 232.403 1.00 6.96  ? 1914 GLU A CG    1 
ATOM   3634  C CD    . GLU A 1 1914 ? 208.571 223.527 232.568 1.00 10.28 ? 1914 GLU A CD    1 
ATOM   3635  O OE1   . GLU A 1 1914 ? 209.316 223.418 231.572 1.00 5.58  ? 1914 GLU A OE1   1 
ATOM   3636  O OE2   . GLU A 1 1914 ? 208.982 223.922 233.680 1.00 11.95 ? 1914 GLU A OE2   1 
ATOM   3637  N N     . SER A 1 1915 ? 206.093 220.070 235.755 1.00 0.46  ? 1915 SER A N     1 
ATOM   3638  C CA    . SER A 1 1915 ? 205.811 219.655 237.127 1.00 0.00  ? 1915 SER A CA    1 
ATOM   3639  C C     . SER A 1 1915 ? 206.964 218.848 237.708 1.00 2.70  ? 1915 SER A C     1 
ATOM   3640  O O     . SER A 1 1915 ? 207.321 219.017 238.880 1.00 3.92  ? 1915 SER A O     1 
ATOM   3641  C CB    . SER A 1 1915 ? 204.515 218.852 237.187 1.00 0.00  ? 1915 SER A CB    1 
ATOM   3642  O OG    . SER A 1 1915 ? 203.402 219.667 236.878 1.00 4.99  ? 1915 SER A OG    1 
ATOM   3643  N N     . VAL A 1 1916 ? 207.557 217.959 236.907 1.00 6.14  ? 1916 VAL A N     1 
ATOM   3644  C CA    . VAL A 1 1916 ? 208.707 217.195 237.384 1.00 1.00  ? 1916 VAL A CA    1 
ATOM   3645  C C     . VAL A 1 1916 ? 209.868 218.127 237.702 1.00 7.46  ? 1916 VAL A C     1 
ATOM   3646  O O     . VAL A 1 1916 ? 210.531 217.990 238.739 1.00 13.64 ? 1916 VAL A O     1 
ATOM   3647  C CB    . VAL A 1 1916 ? 209.102 216.124 236.350 1.00 0.05  ? 1916 VAL A CB    1 
ATOM   3648  C CG1   . VAL A 1 1916 ? 210.483 215.569 236.654 1.00 3.78  ? 1916 VAL A CG1   1 
ATOM   3649  C CG2   . VAL A 1 1916 ? 208.069 215.012 236.324 1.00 0.00  ? 1916 VAL A CG2   1 
ATOM   3650  N N     . LYS A 1 1917 ? 210.123 219.099 236.823 1.00 10.28 ? 1917 LYS A N     1 
ATOM   3651  C CA    . LYS A 1 1917 ? 211.194 220.060 237.060 1.00 5.23  ? 1917 LYS A CA    1 
ATOM   3652  C C     . LYS A 1 1917 ? 210.910 220.920 238.284 1.00 6.15  ? 1917 LYS A C     1 
ATOM   3653  O O     . LYS A 1 1917 ? 211.822 221.226 239.056 1.00 10.05 ? 1917 LYS A O     1 
ATOM   3654  C CB    . LYS A 1 1917 ? 211.392 220.935 235.824 1.00 11.45 ? 1917 LYS A CB    1 
ATOM   3655  C CG    . LYS A 1 1917 ? 212.841 221.155 235.442 1.00 10.96 ? 1917 LYS A CG    1 
ATOM   3656  C CD    . LYS A 1 1917 ? 212.950 222.079 234.243 1.00 10.62 ? 1917 LYS A CD    1 
ATOM   3657  C CE    . LYS A 1 1917 ? 214.389 222.485 233.993 1.00 13.56 ? 1917 LYS A CE    1 
ATOM   3658  N NZ    . LYS A 1 1917 ? 215.248 221.318 233.666 1.00 14.19 ? 1917 LYS A NZ    1 
ATOM   3659  N N     . ALA A 1 1918 ? 209.653 221.323 238.474 1.00 8.90  ? 1918 ALA A N     1 
ATOM   3660  C CA    . ALA A 1 1918 ? 209.291 222.124 239.635 1.00 5.67  ? 1918 ALA A CA    1 
ATOM   3661  C C     . ALA A 1 1918 ? 209.486 221.343 240.924 1.00 8.34  ? 1918 ALA A C     1 
ATOM   3662  O O     . ALA A 1 1918 ? 209.970 221.889 241.921 1.00 18.50 ? 1918 ALA A O     1 
ATOM   3663  C CB    . ALA A 1 1918 ? 207.846 222.603 239.510 1.00 3.83  ? 1918 ALA A CB    1 
ATOM   3664  N N     . LEU A 1 1919 ? 209.110 220.063 240.929 1.00 12.19 ? 1919 LEU A N     1 
ATOM   3665  C CA    . LEU A 1 1919 ? 209.337 219.241 242.112 1.00 11.78 ? 1919 LEU A CA    1 
ATOM   3666  C C     . LEU A 1 1919 ? 210.824 219.062 242.380 1.00 1.85  ? 1919 LEU A C     1 
ATOM   3667  O O     . LEU A 1 1919 ? 211.265 219.113 243.533 1.00 5.95  ? 1919 LEU A O     1 
ATOM   3668  C CB    . LEU A 1 1919 ? 208.656 217.883 241.956 1.00 12.10 ? 1919 LEU A CB    1 
ATOM   3669  C CG    . LEU A 1 1919 ? 208.894 216.926 243.124 1.00 9.63  ? 1919 LEU A CG    1 
ATOM   3670  C CD1   . LEU A 1 1919 ? 207.980 217.267 244.283 1.00 11.13 ? 1919 LEU A CD1   1 
ATOM   3671  C CD2   . LEU A 1 1919 ? 208.695 215.492 242.690 1.00 10.16 ? 1919 LEU A CD2   1 
ATOM   3672  N N     . GLY A 1 1920 ? 211.614 218.848 241.328 1.00 1.68  ? 1920 GLY A N     1 
ATOM   3673  C CA    . GLY A 1 1920 ? 213.047 218.701 241.516 1.00 2.53  ? 1920 GLY A CA    1 
ATOM   3674  C C     . GLY A 1 1920 ? 213.706 219.972 242.013 1.00 4.87  ? 1920 GLY A C     1 
ATOM   3675  O O     . GLY A 1 1920 ? 214.662 219.926 242.789 1.00 12.55 ? 1920 GLY A O     1 
ATOM   3676  N N     . HIS A 1 1921 ? 213.208 221.123 241.563 1.00 6.63  ? 1921 HIS A N     1 
ATOM   3677  C CA    . HIS A 1 1921 ? 213.759 222.398 242.004 1.00 0.00  ? 1921 HIS A CA    1 
ATOM   3678  C C     . HIS A 1 1921 ? 213.309 222.737 243.417 1.00 7.57  ? 1921 HIS A C     1 
ATOM   3679  O O     . HIS A 1 1921 ? 214.040 223.407 244.154 1.00 18.83 ? 1921 HIS A O     1 
ATOM   3680  C CB    . HIS A 1 1921 ? 213.352 223.499 241.027 1.00 5.08  ? 1921 HIS A CB    1 
ATOM   3681  C CG    . HIS A 1 1921 ? 214.077 223.437 239.718 1.00 6.28  ? 1921 HIS A CG    1 
ATOM   3682  N ND1   . HIS A 1 1921 ? 215.332 222.882 239.590 1.00 3.21  ? 1921 HIS A ND1   1 
ATOM   3683  C CD2   . HIS A 1 1921 ? 213.718 223.844 238.479 1.00 1.73  ? 1921 HIS A CD2   1 
ATOM   3684  C CE1   . HIS A 1 1921 ? 215.717 222.955 238.329 1.00 0.00  ? 1921 HIS A CE1   1 
ATOM   3685  N NE2   . HIS A 1 1921 ? 214.755 223.534 237.634 1.00 0.00  ? 1921 HIS A NE2   1 
ATOM   3686  N N     . GLN A 1 1922 ? 212.114 222.288 243.808 1.00 3.76  ? 1922 GLN A N     1 
ATOM   3687  C CA    . GLN A 1 1922 ? 211.655 222.484 245.178 1.00 0.00  ? 1922 GLN A CA    1 
ATOM   3688  C C     . GLN A 1 1922 ? 212.563 221.773 246.170 1.00 5.07  ? 1922 GLN A C     1 
ATOM   3689  O O     . GLN A 1 1922 ? 212.789 222.266 247.281 1.00 6.41  ? 1922 GLN A O     1 
ATOM   3690  C CB    . GLN A 1 1922 ? 210.218 221.991 245.321 1.00 0.00  ? 1922 GLN A CB    1 
ATOM   3691  C CG    . GLN A 1 1922 ? 209.628 222.206 246.696 1.00 0.00  ? 1922 GLN A CG    1 
ATOM   3692  C CD    . GLN A 1 1922 ? 209.065 223.595 246.878 1.00 7.36  ? 1922 GLN A CD    1 
ATOM   3693  O OE1   . GLN A 1 1922 ? 209.701 224.459 247.479 1.00 7.42  ? 1922 GLN A OE1   1 
ATOM   3694  N NE2   . GLN A 1 1922 ? 207.867 223.820 246.354 1.00 8.81  ? 1922 GLN A NE2   1 
ATOM   3695  N N     . LEU A 1 1923 ? 213.085 220.610 245.790 1.00 5.03  ? 1923 LEU A N     1 
ATOM   3696  C CA    . LEU A 1 1923 ? 214.036 219.893 246.625 1.00 0.00  ? 1923 LEU A CA    1 
ATOM   3697  C C     . LEU A 1 1923 ? 215.474 220.321 246.376 1.00 0.00  ? 1923 LEU A C     1 
ATOM   3698  O O     . LEU A 1 1923 ? 216.385 219.751 246.983 1.00 9.01  ? 1923 LEU A O     1 
ATOM   3699  C CB    . LEU A 1 1923 ? 213.892 218.385 246.406 1.00 0.30  ? 1923 LEU A CB    1 
ATOM   3700  C CG    . LEU A 1 1923 ? 212.453 217.867 246.324 1.00 0.00  ? 1923 LEU A CG    1 
ATOM   3701  C CD1   . LEU A 1 1923 ? 212.423 216.406 245.927 1.00 2.59  ? 1923 LEU A CD1   1 
ATOM   3702  C CD2   . LEU A 1 1923 ? 211.730 218.074 247.640 1.00 0.00  ? 1923 LEU A CD2   1 
ATOM   3703  N N     . GLY A 1 1924 ? 215.699 221.301 245.504 1.00 0.00  ? 1924 GLY A N     1 
ATOM   3704  C CA    . GLY A 1 1924 ? 217.028 221.818 245.260 1.00 0.00  ? 1924 GLY A CA    1 
ATOM   3705  C C     . GLY A 1 1924 ? 217.896 220.967 244.366 1.00 0.00  ? 1924 GLY A C     1 
ATOM   3706  O O     . GLY A 1 1924 ? 219.100 221.223 244.272 1.00 1.35  ? 1924 GLY A O     1 
ATOM   3707  N N     . ARG A 1 1925 ? 217.328 219.968 243.702 1.00 5.62  ? 1925 ARG A N     1 
ATOM   3708  C CA    . ARG A 1 1925 ? 218.117 219.054 242.892 1.00 2.76  ? 1925 ARG A CA    1 
ATOM   3709  C C     . ARG A 1 1925 ? 218.381 219.636 241.510 1.00 0.00  ? 1925 ARG A C     1 
ATOM   3710  O O     . ARG A 1 1925 ? 217.602 220.442 240.995 1.00 0.78  ? 1925 ARG A O     1 
ATOM   3711  C CB    . ARG A 1 1925 ? 217.405 217.708 242.771 1.00 0.44  ? 1925 ARG A CB    1 
ATOM   3712  C CG    . ARG A 1 1925 ? 217.295 216.964 244.085 1.00 0.85  ? 1925 ARG A CG    1 
ATOM   3713  C CD    . ARG A 1 1925 ? 218.658 216.489 244.553 1.00 0.00  ? 1925 ARG A CD    1 
ATOM   3714  N NE    . ARG A 1 1925 ? 218.741 216.410 246.005 1.00 2.05  ? 1925 ARG A NE    1 
ATOM   3715  C CZ    . ARG A 1 1925 ? 219.876 216.411 246.690 1.00 7.57  ? 1925 ARG A CZ    1 
ATOM   3716  N NH1   . ARG A 1 1925 ? 221.049 216.485 246.083 1.00 8.59  ? 1925 ARG A NH1   1 
ATOM   3717  N NH2   . ARG A 1 1925 ? 219.833 216.336 248.018 1.00 4.92  ? 1925 ARG A NH2   1 
ATOM   3718  N N     . PHE A 1 1926 ? 219.495 219.218 240.914 1.00 0.00  ? 1926 PHE A N     1 
ATOM   3719  C CA    . PHE A 1 1926 ? 219.891 219.631 239.570 1.00 0.00  ? 1926 PHE A CA    1 
ATOM   3720  C C     . PHE A 1 1926 ? 219.158 218.736 238.578 1.00 1.83  ? 1926 PHE A C     1 
ATOM   3721  O O     . PHE A 1 1926 ? 219.537 217.592 238.335 1.00 5.67  ? 1926 PHE A O     1 
ATOM   3722  C CB    . PHE A 1 1926 ? 221.408 219.564 239.434 1.00 0.15  ? 1926 PHE A CB    1 
ATOM   3723  C CG    . PHE A 1 1926 ? 221.919 219.681 238.027 1.00 0.79  ? 1926 PHE A CG    1 
ATOM   3724  C CD1   . PHE A 1 1926 ? 221.468 220.677 237.190 1.00 0.00  ? 1926 PHE A CD1   1 
ATOM   3725  C CD2   . PHE A 1 1926 ? 222.932 218.853 237.579 1.00 6.41  ? 1926 PHE A CD2   1 
ATOM   3726  C CE1   . PHE A 1 1926 ? 221.957 220.802 235.908 1.00 0.72  ? 1926 PHE A CE1   1 
ATOM   3727  C CE2   . PHE A 1 1926 ? 223.436 218.981 236.301 1.00 3.75  ? 1926 PHE A CE2   1 
ATOM   3728  C CZ    . PHE A 1 1926 ? 222.946 219.957 235.465 1.00 0.90  ? 1926 PHE A CZ    1 
ATOM   3729  N N     . VAL A 1 1927 ? 218.079 219.265 238.010 1.00 1.76  ? 1927 VAL A N     1 
ATOM   3730  C CA    . VAL A 1 1927 ? 217.197 218.481 237.153 1.00 1.35  ? 1927 VAL A CA    1 
ATOM   3731  C C     . VAL A 1 1927 ? 217.577 218.706 235.697 1.00 1.68  ? 1927 VAL A C     1 
ATOM   3732  O O     . VAL A 1 1927 ? 217.745 219.848 235.256 1.00 7.47  ? 1927 VAL A O     1 
ATOM   3733  C CB    . VAL A 1 1927 ? 215.728 218.854 237.401 1.00 0.00  ? 1927 VAL A CB    1 
ATOM   3734  C CG1   . VAL A 1 1927 ? 214.815 218.104 236.444 1.00 3.78  ? 1927 VAL A CG1   1 
ATOM   3735  C CG2   . VAL A 1 1927 ? 215.351 218.576 238.837 1.00 1.64  ? 1927 VAL A CG2   1 
ATOM   3736  N N     . LEU A 1 1928 ? 217.706 217.616 234.947 1.00 0.00  ? 1928 LEU A N     1 
ATOM   3737  C CA    . LEU A 1 1928 ? 218.000 217.667 233.523 1.00 1.43  ? 1928 LEU A CA    1 
ATOM   3738  C C     . LEU A 1 1928 ? 216.793 217.175 232.740 1.00 2.67  ? 1928 LEU A C     1 
ATOM   3739  O O     . LEU A 1 1928 ? 216.201 216.146 233.077 1.00 12.05 ? 1928 LEU A O     1 
ATOM   3740  C CB    . LEU A 1 1928 ? 219.212 216.807 233.162 1.00 0.00  ? 1928 LEU A CB    1 
ATOM   3741  C CG    . LEU A 1 1928 ? 220.608 217.333 233.485 1.00 0.68  ? 1928 LEU A CG    1 
ATOM   3742  C CD1   . LEU A 1 1928 ? 220.847 217.251 234.976 1.00 1.29  ? 1928 LEU A CD1   1 
ATOM   3743  C CD2   . LEU A 1 1928 ? 221.668 216.566 232.716 1.00 6.52  ? 1928 LEU A CD2   1 
ATOM   3744  N N     . VAL A 1 1929 ? 216.434 217.909 231.693 1.00 0.00  ? 1929 VAL A N     1 
ATOM   3745  C CA    . VAL A 1 1929 ? 215.351 217.527 230.799 1.00 0.00  ? 1929 VAL A CA    1 
ATOM   3746  C C     . VAL A 1 1929 ? 215.960 217.104 229.472 1.00 5.07  ? 1929 VAL A C     1 
ATOM   3747  O O     . VAL A 1 1929 ? 216.721 217.863 228.861 1.00 11.29 ? 1929 VAL A O     1 
ATOM   3748  C CB    . VAL A 1 1929 ? 214.340 218.669 230.601 1.00 0.00  ? 1929 VAL A CB    1 
ATOM   3749  C CG1   . VAL A 1 1929 ? 213.295 218.272 229.576 1.00 4.73  ? 1929 VAL A CG1   1 
ATOM   3750  C CG2   . VAL A 1 1929 ? 213.677 219.010 231.920 1.00 2.29  ? 1929 VAL A CG2   1 
ATOM   3751  N N     . PHE A 1 1930 ? 215.634 215.891 229.036 1.00 4.50  ? 1930 PHE A N     1 
ATOM   3752  C CA    . PHE A 1 1930 ? 216.112 215.348 227.775 1.00 0.89  ? 1930 PHE A CA    1 
ATOM   3753  C C     . PHE A 1 1930 ? 214.960 215.335 226.785 1.00 8.33  ? 1930 PHE A C     1 
ATOM   3754  O O     . PHE A 1 1930 ? 213.933 214.695 227.032 1.00 16.88 ? 1930 PHE A O     1 
ATOM   3755  C CB    . PHE A 1 1930 ? 216.668 213.936 227.961 1.00 1.71  ? 1930 PHE A CB    1 
ATOM   3756  C CG    . PHE A 1 1930 ? 217.584 213.798 229.140 1.00 0.00  ? 1930 PHE A CG    1 
ATOM   3757  C CD1   . PHE A 1 1930 ? 217.285 212.917 230.162 1.00 0.80  ? 1930 PHE A CD1   1 
ATOM   3758  C CD2   . PHE A 1 1930 ? 218.741 214.547 229.227 1.00 5.43  ? 1930 PHE A CD2   1 
ATOM   3759  C CE1   . PHE A 1 1930 ? 218.122 212.786 231.249 1.00 4.87  ? 1930 PHE A CE1   1 
ATOM   3760  C CE2   . PHE A 1 1930 ? 219.582 214.420 230.313 1.00 6.15  ? 1930 PHE A CE2   1 
ATOM   3761  C CZ    . PHE A 1 1930 ? 219.269 213.538 231.325 1.00 6.06  ? 1930 PHE A CZ    1 
ATOM   3762  N N     . ASN A 1 1931 ? 215.128 216.036 225.670 1.00 11.29 ? 1931 ASN A N     1 
ATOM   3763  C CA    . ASN A 1 1931 ? 214.093 216.085 224.648 1.00 9.79  ? 1931 ASN A CA    1 
ATOM   3764  C C     . ASN A 1 1931 ? 214.180 214.823 223.800 1.00 15.67 ? 1931 ASN A C     1 
ATOM   3765  O O     . ASN A 1 1931 ? 215.163 214.618 223.079 1.00 19.00 ? 1931 ASN A O     1 
ATOM   3766  C CB    . ASN A 1 1931 ? 214.247 217.338 223.792 1.00 11.95 ? 1931 ASN A CB    1 
ATOM   3767  C CG    . ASN A 1 1931 ? 212.950 217.753 223.132 1.00 14.27 ? 1931 ASN A CG    1 
ATOM   3768  O OD1   . ASN A 1 1931 ? 211.865 217.464 223.635 1.00 13.15 ? 1931 ASN A OD1   1 
ATOM   3769  N ND2   . ASN A 1 1931 ? 213.053 218.434 221.997 1.00 20.75 ? 1931 ASN A ND2   1 
ATOM   3770  N N     . CYS A 1 1932 ? 213.158 213.975 223.892 1.00 13.90 ? 1932 CYS A N     1 
ATOM   3771  C CA    . CYS A 1 1932 ? 213.170 212.660 223.267 1.00 13.50 ? 1932 CYS A CA    1 
ATOM   3772  C C     . CYS A 1 1932 ? 212.490 212.641 221.904 1.00 19.85 ? 1932 CYS A C     1 
ATOM   3773  O O     . CYS A 1 1932 ? 212.364 211.569 221.305 1.00 19.47 ? 1932 CYS A O     1 
ATOM   3774  C CB    . CYS A 1 1932 ? 212.509 211.636 224.191 1.00 10.72 ? 1932 CYS A CB    1 
ATOM   3775  S SG    . CYS A 1 1932 ? 213.415 211.316 225.719 1.00 20.38 ? 1932 CYS A SG    1 
ATOM   3776  N N     . ASP A 1 1933 ? 212.049 213.792 221.400 1.00 23.95 ? 1933 ASP A N     1 
ATOM   3777  C CA    . ASP A 1 1933 ? 211.412 213.838 220.090 1.00 22.73 ? 1933 ASP A CA    1 
ATOM   3778  C C     . ASP A 1 1933 ? 212.440 213.871 218.964 1.00 25.99 ? 1933 ASP A C     1 
ATOM   3779  O O     . ASP A 1 1933 ? 212.325 213.120 217.990 1.00 26.79 ? 1933 ASP A O     1 
ATOM   3780  C CB    . ASP A 1 1933 ? 210.477 215.050 219.998 1.00 21.06 ? 1933 ASP A CB    1 
ATOM   3781  C CG    . ASP A 1 1933 ? 211.189 216.363 220.272 1.00 23.41 ? 1933 ASP A CG    1 
ATOM   3782  O OD1   . ASP A 1 1933 ? 212.398 216.335 220.581 1.00 21.53 ? 1933 ASP A OD1   1 
ATOM   3783  O OD2   . ASP A 1 1933 ? 210.538 217.424 220.175 1.00 22.65 ? 1933 ASP A OD2   1 
ATOM   3784  N N     . GLU A 1 1934 ? 213.448 214.727 219.090 1.00 26.33 ? 1934 GLU A N     1 
ATOM   3785  C CA    . GLU A 1 1934 ? 214.488 214.874 218.082 1.00 28.41 ? 1934 GLU A CA    1 
ATOM   3786  C C     . GLU A 1 1934 ? 215.665 215.584 218.741 1.00 29.15 ? 1934 GLU A C     1 
ATOM   3787  O O     . GLU A 1 1934 ? 215.558 216.085 219.864 1.00 25.12 ? 1934 GLU A O     1 
ATOM   3788  C CB    . GLU A 1 1934 ? 213.958 215.626 216.854 1.00 28.96 ? 1934 GLU A CB    1 
ATOM   3789  C CG    . GLU A 1 1934 ? 214.860 215.609 215.619 1.00 27.49 ? 1934 GLU A CG    1 
ATOM   3790  C CD    . GLU A 1 1934 ? 215.423 214.232 215.307 1.00 33.02 ? 1934 GLU A CD    1 
ATOM   3791  O OE1   . GLU A 1 1934 ? 216.415 213.822 215.948 1.00 34.18 ? 1934 GLU A OE1   1 
ATOM   3792  O OE2   . GLU A 1 1934 ? 214.869 213.556 214.416 1.00 30.22 ? 1934 GLU A OE2   1 
ATOM   3793  N N     . THR A 1 1935 ? 216.797 215.617 218.033 1.00 26.72 ? 1935 THR A N     1 
ATOM   3794  C CA    . THR A 1 1935 ? 218.045 216.177 218.556 1.00 28.66 ? 1935 THR A CA    1 
ATOM   3795  C C     . THR A 1 1935 ? 218.449 215.483 219.855 1.00 24.52 ? 1935 THR A C     1 
ATOM   3796  O O     . THR A 1 1935 ? 218.980 216.104 220.777 1.00 24.59 ? 1935 THR A O     1 
ATOM   3797  C CB    . THR A 1 1935 ? 217.944 217.692 218.756 1.00 29.31 ? 1935 THR A CB    1 
ATOM   3798  O OG1   . THR A 1 1935 ? 217.171 217.972 219.930 1.00 24.04 ? 1935 THR A OG1   1 
ATOM   3799  C CG2   . THR A 1 1935 ? 217.288 218.351 217.551 1.00 26.41 ? 1935 THR A CG2   1 
ATOM   3800  N N     . PHE A 1 1936 ? 218.189 214.181 219.925 1.00 21.60 ? 1936 PHE A N     1 
ATOM   3801  C CA    . PHE A 1 1936 ? 218.524 213.366 221.083 1.00 22.22 ? 1936 PHE A CA    1 
ATOM   3802  C C     . PHE A 1 1936 ? 219.899 212.752 220.863 1.00 22.56 ? 1936 PHE A C     1 
ATOM   3803  O O     . PHE A 1 1936 ? 220.077 211.927 219.960 1.00 20.91 ? 1936 PHE A O     1 
ATOM   3804  C CB    . PHE A 1 1936 ? 217.470 212.280 221.304 1.00 24.91 ? 1936 PHE A CB    1 
ATOM   3805  C CG    . PHE A 1 1936 ? 217.654 211.502 222.575 1.00 26.78 ? 1936 PHE A CG    1 
ATOM   3806  C CD1   . PHE A 1 1936 ? 217.113 211.956 223.765 1.00 24.54 ? 1936 PHE A CD1   1 
ATOM   3807  C CD2   . PHE A 1 1936 ? 218.359 210.311 222.578 1.00 25.19 ? 1936 PHE A CD2   1 
ATOM   3808  C CE1   . PHE A 1 1936 ? 217.281 211.243 224.933 1.00 20.54 ? 1936 PHE A CE1   1 
ATOM   3809  C CE2   . PHE A 1 1936 ? 218.528 209.593 223.743 1.00 18.35 ? 1936 PHE A CE2   1 
ATOM   3810  C CZ    . PHE A 1 1936 ? 217.989 210.059 224.921 1.00 17.44 ? 1936 PHE A CZ    1 
ATOM   3811  N N     . ASP A 1 1937 ? 220.865 213.152 221.686 1.00 23.06 ? 1937 ASP A N     1 
ATOM   3812  C CA    . ASP A 1 1937 ? 222.247 212.695 221.555 1.00 27.25 ? 1937 ASP A CA    1 
ATOM   3813  C C     . ASP A 1 1937 ? 222.387 211.401 222.348 1.00 26.94 ? 1937 ASP A C     1 
ATOM   3814  O O     . ASP A 1 1937 ? 222.549 211.410 223.568 1.00 28.81 ? 1937 ASP A O     1 
ATOM   3815  C CB    . ASP A 1 1937 ? 223.221 213.765 222.033 1.00 27.37 ? 1937 ASP A CB    1 
ATOM   3816  C CG    . ASP A 1 1937 ? 224.525 213.754 221.259 1.00 30.52 ? 1937 ASP A CG    1 
ATOM   3817  O OD1   . ASP A 1 1937 ? 224.558 213.169 220.155 1.00 27.08 ? 1937 ASP A OD1   1 
ATOM   3818  O OD2   . ASP A 1 1937 ? 225.517 214.333 221.751 1.00 27.46 ? 1937 ASP A OD2   1 
ATOM   3819  N N     . PHE A 1 1938 ? 222.314 210.273 221.636 1.00 22.10 ? 1938 PHE A N     1 
ATOM   3820  C CA    . PHE A 1 1938 ? 222.474 208.976 222.283 1.00 22.41 ? 1938 PHE A CA    1 
ATOM   3821  C C     . PHE A 1 1938 ? 223.869 208.777 222.855 1.00 26.54 ? 1938 PHE A C     1 
ATOM   3822  O O     . PHE A 1 1938 ? 224.011 208.233 223.956 1.00 27.40 ? 1938 PHE A O     1 
ATOM   3823  C CB    . PHE A 1 1938 ? 222.149 207.848 221.308 1.00 22.95 ? 1938 PHE A CB    1 
ATOM   3824  C CG    . PHE A 1 1938 ? 221.758 206.574 221.985 1.00 25.13 ? 1938 PHE A CG    1 
ATOM   3825  C CD1   . PHE A 1 1938 ? 222.732 205.733 222.501 1.00 25.73 ? 1938 PHE A CD1   1 
ATOM   3826  C CD2   . PHE A 1 1938 ? 220.433 206.229 222.142 1.00 26.22 ? 1938 PHE A CD2   1 
ATOM   3827  C CE1   . PHE A 1 1938 ? 222.391 204.565 223.137 1.00 24.29 ? 1938 PHE A CE1   1 
ATOM   3828  C CE2   . PHE A 1 1938 ? 220.089 205.059 222.780 1.00 25.81 ? 1938 PHE A CE2   1 
ATOM   3829  C CZ    . PHE A 1 1938 ? 221.070 204.231 223.278 1.00 22.39 ? 1938 PHE A CZ    1 
ATOM   3830  N N     . GLN A 1 1939 ? 224.910 209.179 222.121 1.00 23.13 ? 1939 GLN A N     1 
ATOM   3831  C CA    . GLN A 1 1939 ? 226.267 208.959 222.609 1.00 23.68 ? 1939 GLN A CA    1 
ATOM   3832  C C     . GLN A 1 1939 ? 226.514 209.692 223.920 1.00 21.74 ? 1939 GLN A C     1 
ATOM   3833  O O     . GLN A 1 1939 ? 227.347 209.260 224.724 1.00 21.54 ? 1939 GLN A O     1 
ATOM   3834  C CB    . GLN A 1 1939 ? 227.285 209.390 221.552 1.00 24.88 ? 1939 GLN A CB    1 
ATOM   3835  C CG    . GLN A 1 1939 ? 227.252 210.870 221.209 1.00 27.43 ? 1939 GLN A CG    1 
ATOM   3836  C CD    . GLN A 1 1939 ? 228.245 211.676 222.024 1.00 26.60 ? 1939 GLN A CD    1 
ATOM   3837  O OE1   . GLN A 1 1939 ? 229.201 211.129 222.575 1.00 26.00 ? 1939 GLN A OE1   1 
ATOM   3838  N NE2   . GLN A 1 1939 ? 228.023 212.982 222.105 1.00 23.33 ? 1939 GLN A NE2   1 
ATOM   3839  N N     . ALA A 1 1940 ? 225.793 210.788 224.156 1.00 16.17 ? 1940 ALA A N     1 
ATOM   3840  C CA    . ALA A 1 1940 ? 225.958 211.550 225.386 1.00 20.12 ? 1940 ALA A CA    1 
ATOM   3841  C C     . ALA A 1 1940 ? 225.311 210.867 226.584 1.00 17.32 ? 1940 ALA A C     1 
ATOM   3842  O O     . ALA A 1 1940 ? 225.781 211.043 227.713 1.00 15.17 ? 1940 ALA A O     1 
ATOM   3843  C CB    . ALA A 1 1940 ? 225.377 212.953 225.210 1.00 20.52 ? 1940 ALA A CB    1 
ATOM   3844  N N     . MET A 1 1941 ? 224.252 210.083 226.359 1.00 8.39  ? 1941 MET A N     1 
ATOM   3845  C CA    . MET A 1 1941 ? 223.477 209.534 227.468 1.00 8.29  ? 1941 MET A CA    1 
ATOM   3846  C C     . MET A 1 1941 ? 224.305 208.610 228.349 1.00 11.51 ? 1941 MET A C     1 
ATOM   3847  O O     . MET A 1 1941 ? 224.059 208.528 229.558 1.00 12.11 ? 1941 MET A O     1 
ATOM   3848  C CB    . MET A 1 1941 ? 222.250 208.797 226.938 1.00 7.80  ? 1941 MET A CB    1 
ATOM   3849  C CG    . MET A 1 1941 ? 221.250 209.700 226.256 1.00 13.39 ? 1941 MET A CG    1 
ATOM   3850  S SD    . MET A 1 1941 ? 220.614 210.949 227.389 1.00 21.25 ? 1941 MET A SD    1 
ATOM   3851  C CE    . MET A 1 1941 ? 219.643 209.935 228.494 1.00 9.64  ? 1941 MET A CE    1 
ATOM   3852  N N     . GLY A 1 1942 ? 225.290 207.920 227.774 1.00 14.32 ? 1942 GLY A N     1 
ATOM   3853  C CA    . GLY A 1 1942 ? 226.117 207.033 228.574 1.00 7.84  ? 1942 GLY A CA    1 
ATOM   3854  C C     . GLY A 1 1942 ? 226.823 207.752 229.707 1.00 8.23  ? 1942 GLY A C     1 
ATOM   3855  O O     . GLY A 1 1942 ? 226.799 207.295 230.851 1.00 8.41  ? 1942 GLY A O     1 
ATOM   3856  N N     . ARG A 1 1943 ? 227.446 208.892 229.411 1.00 7.69  ? 1943 ARG A N     1 
ATOM   3857  C CA    . ARG A 1 1943 ? 228.084 209.680 230.457 1.00 7.30  ? 1943 ARG A CA    1 
ATOM   3858  C C     . ARG A 1 1943 ? 227.092 210.543 231.222 1.00 8.59  ? 1943 ARG A C     1 
ATOM   3859  O O     . ARG A 1 1943 ? 227.351 210.891 232.378 1.00 15.94 ? 1943 ARG A O     1 
ATOM   3860  C CB    . ARG A 1 1943 ? 229.181 210.572 229.871 1.00 6.78  ? 1943 ARG A CB    1 
ATOM   3861  C CG    . ARG A 1 1943 ? 228.846 211.180 228.528 1.00 8.01  ? 1943 ARG A CG    1 
ATOM   3862  C CD    . ARG A 1 1943 ? 229.773 212.339 228.214 1.00 9.77  ? 1943 ARG A CD    1 
ATOM   3863  N NE    . ARG A 1 1943 ? 229.334 213.085 227.041 1.00 11.56 ? 1943 ARG A NE    1 
ATOM   3864  C CZ    . ARG A 1 1943 ? 228.379 214.004 227.054 1.00 11.36 ? 1943 ARG A CZ    1 
ATOM   3865  N NH1   . ARG A 1 1943 ? 227.722 214.302 228.163 1.00 14.27 ? 1943 ARG A NH1   1 
ATOM   3866  N NH2   . ARG A 1 1943 ? 228.075 214.640 225.927 1.00 9.14  ? 1943 ARG A NH2   1 
ATOM   3867  N N     . ILE A 1 1944 ? 225.962 210.895 230.607 1.00 7.77  ? 1944 ILE A N     1 
ATOM   3868  C CA    . ILE A 1 1944 ? 224.961 211.697 231.305 1.00 6.42  ? 1944 ILE A CA    1 
ATOM   3869  C C     . ILE A 1 1944 ? 224.375 210.916 232.474 1.00 1.76  ? 1944 ILE A C     1 
ATOM   3870  O O     . ILE A 1 1944 ? 224.176 211.460 233.567 1.00 10.58 ? 1944 ILE A O     1 
ATOM   3871  C CB    . ILE A 1 1944 ? 223.873 212.160 230.319 1.00 8.41  ? 1944 ILE A CB    1 
ATOM   3872  C CG1   . ILE A 1 1944 ? 224.392 213.320 229.469 1.00 8.65  ? 1944 ILE A CG1   1 
ATOM   3873  C CG2   . ILE A 1 1944 ? 222.617 212.570 231.063 1.00 5.61  ? 1944 ILE A CG2   1 
ATOM   3874  C CD1   . ILE A 1 1944 ? 223.331 213.973 228.615 1.00 12.95 ? 1944 ILE A CD1   1 
ATOM   3875  N N     . PHE A 1 1945 ? 224.090 209.629 232.265 1.00 0.00  ? 1945 PHE A N     1 
ATOM   3876  C CA    . PHE A 1 1945 ? 223.589 208.798 233.354 1.00 3.25  ? 1945 PHE A CA    1 
ATOM   3877  C C     . PHE A 1 1945 ? 224.619 208.672 234.471 1.00 7.97  ? 1945 PHE A C     1 
ATOM   3878  O O     . PHE A 1 1945 ? 224.265 208.702 235.657 1.00 14.08 ? 1945 PHE A O     1 
ATOM   3879  C CB    . PHE A 1 1945 ? 223.197 207.421 232.823 1.00 6.26  ? 1945 PHE A CB    1 
ATOM   3880  C CG    . PHE A 1 1945 ? 221.804 207.360 232.269 1.00 6.10  ? 1945 PHE A CG    1 
ATOM   3881  C CD1   . PHE A 1 1945 ? 220.718 207.723 233.046 1.00 7.20  ? 1945 PHE A CD1   1 
ATOM   3882  C CD2   . PHE A 1 1945 ? 221.581 206.937 230.972 1.00 9.21  ? 1945 PHE A CD2   1 
ATOM   3883  C CE1   . PHE A 1 1945 ? 219.434 207.666 232.537 1.00 5.58  ? 1945 PHE A CE1   1 
ATOM   3884  C CE2   . PHE A 1 1945 ? 220.300 206.878 230.458 1.00 7.28  ? 1945 PHE A CE2   1 
ATOM   3885  C CZ    . PHE A 1 1945 ? 219.226 207.244 231.242 1.00 6.41  ? 1945 PHE A CZ    1 
ATOM   3886  N N     . VAL A 1 1946 ? 225.899 208.539 234.116 1.00 5.66  ? 1946 VAL A N     1 
ATOM   3887  C CA    . VAL A 1 1946 ? 226.943 208.460 235.134 1.00 6.59  ? 1946 VAL A CA    1 
ATOM   3888  C C     . VAL A 1 1946 ? 227.024 209.767 235.911 1.00 3.78  ? 1946 VAL A C     1 
ATOM   3889  O O     . VAL A 1 1946 ? 227.262 209.773 237.124 1.00 4.64  ? 1946 VAL A O     1 
ATOM   3890  C CB    . VAL A 1 1946 ? 228.295 208.099 234.492 1.00 5.01  ? 1946 VAL A CB    1 
ATOM   3891  C CG1   . VAL A 1 1946 ? 229.364 207.963 235.558 1.00 2.99  ? 1946 VAL A CG1   1 
ATOM   3892  C CG2   . VAL A 1 1946 ? 228.175 206.817 233.697 1.00 7.06  ? 1946 VAL A CG2   1 
ATOM   3893  N N     . GLY A 1 1947 ? 226.841 210.893 235.224 1.00 0.17  ? 1947 GLY A N     1 
ATOM   3894  C CA    . GLY A 1 1947 ? 226.813 212.169 235.917 1.00 0.72  ? 1947 GLY A CA    1 
ATOM   3895  C C     . GLY A 1 1947 ? 225.643 212.284 236.873 1.00 5.49  ? 1947 GLY A C     1 
ATOM   3896  O O     . GLY A 1 1947 ? 225.790 212.774 237.993 1.00 12.37 ? 1947 GLY A O     1 
ATOM   3897  N N     . LEU A 1 1948 ? 224.464 211.832 236.443 1.00 4.08  ? 1948 LEU A N     1 
ATOM   3898  C CA    . LEU A 1 1948 ? 223.308 211.827 237.335 1.00 0.00  ? 1948 LEU A CA    1 
ATOM   3899  C C     . LEU A 1 1948 ? 223.562 210.951 238.553 1.00 0.00  ? 1948 LEU A C     1 
ATOM   3900  O O     . LEU A 1 1948 ? 223.123 211.272 239.662 1.00 6.69  ? 1948 LEU A O     1 
ATOM   3901  C CB    . LEU A 1 1948 ? 222.059 211.352 236.594 1.00 0.00  ? 1948 LEU A CB    1 
ATOM   3902  C CG    . LEU A 1 1948 ? 221.628 212.109 235.338 1.00 0.00  ? 1948 LEU A CG    1 
ATOM   3903  C CD1   . LEU A 1 1948 ? 220.250 211.661 234.894 1.00 0.00  ? 1948 LEU A CD1   1 
ATOM   3904  C CD2   . LEU A 1 1948 ? 221.658 213.603 235.572 1.00 0.46  ? 1948 LEU A CD2   1 
ATOM   3905  N N     . CYS A 1 1949 ? 224.266 209.835 238.363 1.00 0.00  ? 1949 CYS A N     1 
ATOM   3906  C CA    . CYS A 1 1949 ? 224.547 208.938 239.480 1.00 3.58  ? 1949 CYS A CA    1 
ATOM   3907  C C     . CYS A 1 1949 ? 225.554 209.544 240.452 1.00 6.34  ? 1949 CYS A C     1 
ATOM   3908  O O     . CYS A 1 1949 ? 225.346 209.520 241.670 1.00 7.66  ? 1949 CYS A O     1 
ATOM   3909  C CB    . CYS A 1 1949 ? 225.050 207.596 238.955 1.00 6.55  ? 1949 CYS A CB    1 
ATOM   3910  S SG    . CYS A 1 1949 ? 223.816 206.681 238.026 1.00 12.45 ? 1949 CYS A SG    1 
ATOM   3911  N N     . GLN A 1 1950 ? 226.653 210.087 239.938 1.00 3.69  ? 1950 GLN A N     1 
ATOM   3912  C CA    . GLN A 1 1950 ? 227.738 210.559 240.789 1.00 2.23  ? 1950 GLN A CA    1 
ATOM   3913  C C     . GLN A 1 1950 ? 227.571 212.003 241.241 1.00 6.36  ? 1950 GLN A C     1 
ATOM   3914  O O     . GLN A 1 1950 ? 228.404 212.492 242.011 1.00 8.51  ? 1950 GLN A O     1 
ATOM   3915  C CB    . GLN A 1 1950 ? 229.083 210.394 240.076 1.00 3.92  ? 1950 GLN A CB    1 
ATOM   3916  C CG    . GLN A 1 1950 ? 229.283 209.033 239.439 1.00 10.56 ? 1950 GLN A CG    1 
ATOM   3917  C CD    . GLN A 1 1950 ? 230.727 208.578 239.488 1.00 16.21 ? 1950 GLN A CD    1 
ATOM   3918  O OE1   . GLN A 1 1950 ? 231.649 209.394 239.463 1.00 16.33 ? 1950 GLN A OE1   1 
ATOM   3919  N NE2   . GLN A 1 1950 ? 230.932 207.268 239.558 1.00 12.55 ? 1950 GLN A NE2   1 
ATOM   3920  N N     . VAL A 1 1951 ? 226.528 212.694 240.793 1.00 6.04  ? 1951 VAL A N     1 
ATOM   3921  C CA    . VAL A 1 1951 ? 226.226 214.040 241.251 1.00 1.90  ? 1951 VAL A CA    1 
ATOM   3922  C C     . VAL A 1 1951 ? 225.042 214.054 242.210 1.00 5.94  ? 1951 VAL A C     1 
ATOM   3923  O O     . VAL A 1 1951 ? 225.055 214.780 243.206 1.00 8.67  ? 1951 VAL A O     1 
ATOM   3924  C CB    . VAL A 1 1951 ? 225.979 214.984 240.053 1.00 0.00  ? 1951 VAL A CB    1 
ATOM   3925  C CG1   . VAL A 1 1951 ? 225.365 216.293 240.515 1.00 5.71  ? 1951 VAL A CG1   1 
ATOM   3926  C CG2   . VAL A 1 1951 ? 227.277 215.252 239.318 1.00 3.35  ? 1951 VAL A CG2   1 
ATOM   3927  N N     . GLY A 1 1952 ? 224.028 213.239 241.945 1.00 3.72  ? 1952 GLY A N     1 
ATOM   3928  C CA    . GLY A 1 1952 ? 222.802 213.299 242.713 1.00 1.11  ? 1952 GLY A CA    1 
ATOM   3929  C C     . GLY A 1 1952 ? 221.794 214.176 242.007 1.00 2.33  ? 1952 GLY A C     1 
ATOM   3930  O O     . GLY A 1 1952 ? 220.995 214.871 242.639 1.00 11.85 ? 1952 GLY A O     1 
ATOM   3931  N N     . ALA A 1 1953 ? 221.836 214.143 240.681 1.00 0.00  ? 1953 ALA A N     1 
ATOM   3932  C CA    . ALA A 1 1953 ? 221.017 214.989 239.834 1.00 0.00  ? 1953 ALA A CA    1 
ATOM   3933  C C     . ALA A 1 1953 ? 219.824 214.198 239.320 1.00 0.00  ? 1953 ALA A C     1 
ATOM   3934  O O     . ALA A 1 1953 ? 219.854 212.967 239.264 1.00 1.25  ? 1953 ALA A O     1 
ATOM   3935  C CB    . ALA A 1 1953 ? 221.834 215.536 238.658 1.00 3.83  ? 1953 ALA A CB    1 
ATOM   3936  N N     . TRP A 1 1954 ? 218.769 214.915 238.951 1.00 0.00  ? 1954 TRP A N     1 
ATOM   3937  C CA    . TRP A 1 1954 ? 217.575 214.271 238.434 1.00 0.00  ? 1954 TRP A CA    1 
ATOM   3938  C C     . TRP A 1 1954 ? 217.653 214.157 236.915 1.00 0.00  ? 1954 TRP A C     1 
ATOM   3939  O O     . TRP A 1 1954 ? 218.588 214.638 236.272 1.00 8.50  ? 1954 TRP A O     1 
ATOM   3940  C CB    . TRP A 1 1954 ? 216.327 215.040 238.860 1.00 0.30  ? 1954 TRP A CB    1 
ATOM   3941  C CG    . TRP A 1 1954 ? 215.892 214.756 240.259 1.00 0.00  ? 1954 TRP A CG    1 
ATOM   3942  C CD1   . TRP A 1 1954 ? 216.661 214.275 241.274 1.00 0.00  ? 1954 TRP A CD1   1 
ATOM   3943  C CD2   . TRP A 1 1954 ? 214.578 214.929 240.797 1.00 0.00  ? 1954 TRP A CD2   1 
ATOM   3944  N NE1   . TRP A 1 1954 ? 215.911 214.144 242.414 1.00 0.00  ? 1954 TRP A NE1   1 
ATOM   3945  C CE2   . TRP A 1 1954 ? 214.626 214.536 242.147 1.00 0.00  ? 1954 TRP A CE2   1 
ATOM   3946  C CE3   . TRP A 1 1954 ? 213.366 215.379 240.269 1.00 0.00  ? 1954 TRP A CE3   1 
ATOM   3947  C CZ2   . TRP A 1 1954 ? 213.512 214.581 242.974 1.00 0.00  ? 1954 TRP A CZ2   1 
ATOM   3948  C CZ3   . TRP A 1 1954 ? 212.261 215.417 241.091 1.00 1.40  ? 1954 TRP A CZ3   1 
ATOM   3949  C CH2   . TRP A 1 1954 ? 212.342 215.026 242.429 1.00 1.26  ? 1954 TRP A CH2   1 
ATOM   3950  N N     . GLY A 1 1955 ? 216.648 213.510 236.334 1.00 3.34  ? 1955 GLY A N     1 
ATOM   3951  C CA    . GLY A 1 1955 ? 216.563 213.380 234.895 1.00 2.57  ? 1955 GLY A CA    1 
ATOM   3952  C C     . GLY A 1 1955 ? 215.136 213.194 234.431 1.00 0.00  ? 1955 GLY A C     1 
ATOM   3953  O O     . GLY A 1 1955 ? 214.425 212.319 234.930 1.00 4.79  ? 1955 GLY A O     1 
ATOM   3954  N N     . CYS A 1 1956 ? 214.706 214.013 233.476 1.00 0.00  ? 1956 CYS A N     1 
ATOM   3955  C CA    . CYS A 1 1956 ? 213.346 213.968 232.959 1.00 0.00  ? 1956 CYS A CA    1 
ATOM   3956  C C     . CYS A 1 1956 ? 213.397 213.761 231.455 1.00 0.00  ? 1956 CYS A C     1 
ATOM   3957  O O     . CYS A 1 1956 ? 214.140 214.454 230.755 1.00 3.04  ? 1956 CYS A O     1 
ATOM   3958  C CB    . CYS A 1 1956 ? 212.583 215.251 233.299 1.00 0.00  ? 1956 CYS A CB    1 
ATOM   3959  S SG    . CYS A 1 1956 ? 210.851 215.244 232.806 1.00 10.67 ? 1956 CYS A SG    1 
ATOM   3960  N N     . PHE A 1 1957 ? 212.611 212.811 230.964 1.00 4.38  ? 1957 PHE A N     1 
ATOM   3961  C CA    . PHE A 1 1957 ? 212.565 212.467 229.546 1.00 1.50  ? 1957 PHE A CA    1 
ATOM   3962  C C     . PHE A 1 1957 ? 211.256 213.002 228.981 1.00 0.00  ? 1957 PHE A C     1 
ATOM   3963  O O     . PHE A 1 1957 ? 210.203 212.380 229.138 1.00 5.08  ? 1957 PHE A O     1 
ATOM   3964  C CB    . PHE A 1 1957 ? 212.678 210.959 229.347 1.00 0.00  ? 1957 PHE A CB    1 
ATOM   3965  C CG    . PHE A 1 1957 ? 214.047 210.406 229.631 1.00 0.25  ? 1957 PHE A CG    1 
ATOM   3966  C CD1   . PHE A 1 1957 ? 214.481 210.231 230.932 1.00 0.84  ? 1957 PHE A CD1   1 
ATOM   3967  C CD2   . PHE A 1 1957 ? 214.892 210.048 228.596 1.00 4.21  ? 1957 PHE A CD2   1 
ATOM   3968  C CE1   . PHE A 1 1957 ? 215.733 209.717 231.196 1.00 0.00  ? 1957 PHE A CE1   1 
ATOM   3969  C CE2   . PHE A 1 1957 ? 216.144 209.534 228.855 1.00 7.17  ? 1957 PHE A CE2   1 
ATOM   3970  C CZ    . PHE A 1 1957 ? 216.565 209.369 230.156 1.00 2.32  ? 1957 PHE A CZ    1 
ATOM   3971  N N     . ASP A 1 1958 ? 211.322 214.156 228.324 1.00 0.00  ? 1958 ASP A N     1 
ATOM   3972  C CA    . ASP A 1 1958 ? 210.126 214.738 227.730 1.00 0.00  ? 1958 ASP A CA    1 
ATOM   3973  C C     . ASP A 1 1958 ? 209.677 213.913 226.532 1.00 3.30  ? 1958 ASP A C     1 
ATOM   3974  O O     . ASP A 1 1958 ? 210.410 213.777 225.549 1.00 11.99 ? 1958 ASP A O     1 
ATOM   3975  C CB    . ASP A 1 1958 ? 210.394 216.183 227.313 1.00 5.38  ? 1958 ASP A CB    1 
ATOM   3976  C CG    . ASP A 1 1958 ? 209.135 216.903 226.871 1.00 8.18  ? 1958 ASP A CG    1 
ATOM   3977  O OD1   . ASP A 1 1958 ? 208.048 216.583 227.394 1.00 6.47  ? 1958 ASP A OD1   1 
ATOM   3978  O OD2   . ASP A 1 1958 ? 209.233 217.793 226.001 1.00 11.32 ? 1958 ASP A OD2   1 
ATOM   3979  N N     . GLU A 1 1959 ? 208.463 213.369 226.617 1.00 4.55  ? 1959 GLU A N     1 
ATOM   3980  C CA    . GLU A 1 1959 ? 207.894 212.520 225.572 1.00 6.16  ? 1959 GLU A CA    1 
ATOM   3981  C C     . GLU A 1 1959 ? 208.823 211.347 225.261 1.00 8.09  ? 1959 GLU A C     1 
ATOM   3982  O O     . GLU A 1 1959 ? 209.364 211.212 224.163 1.00 20.07 ? 1959 GLU A O     1 
ATOM   3983  C CB    . GLU A 1 1959 ? 207.583 213.332 224.312 1.00 4.18  ? 1959 GLU A CB    1 
ATOM   3984  C CG    . GLU A 1 1959 ? 206.843 214.633 224.561 1.00 3.79  ? 1959 GLU A CG    1 
ATOM   3985  C CD    . GLU A 1 1959 ? 205.491 214.415 225.209 1.00 12.73 ? 1959 GLU A CD    1 
ATOM   3986  O OE1   . GLU A 1 1959 ? 204.721 213.579 224.695 1.00 12.66 ? 1959 GLU A OE1   1 
ATOM   3987  O OE2   . GLU A 1 1959 ? 205.196 215.078 226.225 1.00 12.92 ? 1959 GLU A OE2   1 
ATOM   3988  N N     . PHE A 1 1960 ? 209.003 210.493 226.270 1.00 0.96  ? 1960 PHE A N     1 
ATOM   3989  C CA    . PHE A 1 1960 ? 209.936 209.377 226.152 1.00 0.00  ? 1960 PHE A CA    1 
ATOM   3990  C C     . PHE A 1 1960 ? 209.511 208.405 225.059 1.00 1.91  ? 1960 PHE A C     1 
ATOM   3991  O O     . PHE A 1 1960 ? 210.355 207.733 224.455 1.00 9.82  ? 1960 PHE A O     1 
ATOM   3992  C CB    . PHE A 1 1960 ? 210.039 208.659 227.495 1.00 6.03  ? 1960 PHE A CB    1 
ATOM   3993  C CG    . PHE A 1 1960 ? 211.043 207.544 227.522 1.00 2.88  ? 1960 PHE A CG    1 
ATOM   3994  C CD1   . PHE A 1 1960 ? 212.392 207.814 227.626 1.00 9.52  ? 1960 PHE A CD1   1 
ATOM   3995  C CD2   . PHE A 1 1960 ? 210.635 206.224 227.460 1.00 4.91  ? 1960 PHE A CD2   1 
ATOM   3996  C CE1   . PHE A 1 1960 ? 213.314 206.793 227.664 1.00 5.36  ? 1960 PHE A CE1   1 
ATOM   3997  C CE2   . PHE A 1 1960 ? 211.555 205.199 227.496 1.00 6.57  ? 1960 PHE A CE2   1 
ATOM   3998  C CZ    . PHE A 1 1960 ? 212.895 205.485 227.597 1.00 1.09  ? 1960 PHE A CZ    1 
ATOM   3999  N N     . ASN A 1 1961 ? 208.208 208.312 224.792 1.00 1.86  ? 1961 ASN A N     1 
ATOM   4000  C CA    . ASN A 1 1961 ? 207.725 207.371 223.789 1.00 3.75  ? 1961 ASN A CA    1 
ATOM   4001  C C     . ASN A 1 1961 ? 208.038 207.820 222.367 1.00 7.37  ? 1961 ASN A C     1 
ATOM   4002  O O     . ASN A 1 1961 ? 207.950 207.007 221.442 1.00 14.95 ? 1961 ASN A O     1 
ATOM   4003  C CB    . ASN A 1 1961 ? 206.221 207.152 223.960 1.00 4.83  ? 1961 ASN A CB    1 
ATOM   4004  C CG    . ASN A 1 1961 ? 205.423 208.435 223.839 1.00 7.97  ? 1961 ASN A CG    1 
ATOM   4005  O OD1   . ASN A 1 1961 ? 205.979 209.513 223.637 1.00 9.36  ? 1961 ASN A OD1   1 
ATOM   4006  N ND2   . ASN A 1 1961 ? 204.107 208.322 223.963 1.00 8.14  ? 1961 ASN A ND2   1 
ATOM   4007  N N     . ARG A 1 1962 ? 208.403 209.089 222.170 1.00 3.12  ? 1962 ARG A N     1 
ATOM   4008  C CA    . ARG A 1 1962 ? 208.758 209.567 220.839 1.00 3.57  ? 1962 ARG A CA    1 
ATOM   4009  C C     . ARG A 1 1962 ? 210.037 208.930 220.315 1.00 13.54 ? 1962 ARG A C     1 
ATOM   4010  O O     . ARG A 1 1962 ? 210.277 208.960 219.103 1.00 20.11 ? 1962 ARG A O     1 
ATOM   4011  C CB    . ARG A 1 1962 ? 208.905 211.087 220.845 1.00 5.34  ? 1962 ARG A CB    1 
ATOM   4012  C CG    . ARG A 1 1962 ? 207.614 211.835 221.110 1.00 9.14  ? 1962 ARG A CG    1 
ATOM   4013  C CD    . ARG A 1 1962 ? 207.374 212.907 220.059 1.00 11.44 ? 1962 ARG A CD    1 
ATOM   4014  N NE    . ARG A 1 1962 ? 206.041 213.486 220.167 1.00 16.67 ? 1962 ARG A NE    1 
ATOM   4015  C CZ    . ARG A 1 1962 ? 204.970 213.016 219.543 1.00 13.38 ? 1962 ARG A CZ    1 
ATOM   4016  N NH1   . ARG A 1 1962 ? 205.039 211.956 218.756 1.00 8.05  ? 1962 ARG A NH1   1 
ATOM   4017  N NH2   . ARG A 1 1962 ? 203.800 213.625 219.715 1.00 9.06  ? 1962 ARG A NH2   1 
ATOM   4018  N N     . LEU A 1 1963 ? 210.862 208.373 221.195 1.00 11.22 ? 1963 LEU A N     1 
ATOM   4019  C CA    . LEU A 1 1963 ? 212.059 207.662 220.773 1.00 11.92 ? 1963 LEU A CA    1 
ATOM   4020  C C     . LEU A 1 1963 ? 211.686 206.460 219.914 1.00 14.20 ? 1963 LEU A C     1 
ATOM   4021  O O     . LEU A 1 1963 ? 210.742 205.727 220.223 1.00 11.23 ? 1963 LEU A O     1 
ATOM   4022  C CB    . LEU A 1 1963 ? 212.850 207.196 221.994 1.00 7.69  ? 1963 LEU A CB    1 
ATOM   4023  C CG    . LEU A 1 1963 ? 213.712 208.209 222.744 1.00 6.50  ? 1963 LEU A CG    1 
ATOM   4024  C CD1   . LEU A 1 1963 ? 214.062 207.674 224.120 1.00 6.91  ? 1963 LEU A CD1   1 
ATOM   4025  C CD2   . LEU A 1 1963 ? 214.965 208.527 221.971 1.00 15.61 ? 1963 LEU A CD2   1 
ATOM   4026  N N     . GLU A 1 1964 ? 212.427 206.256 218.828 1.00 15.00 ? 1964 GLU A N     1 
ATOM   4027  C CA    . GLU A 1 1964 ? 212.202 205.063 218.029 1.00 20.45 ? 1964 GLU A CA    1 
ATOM   4028  C C     . GLU A 1 1964 ? 212.787 203.841 218.732 1.00 19.16 ? 1964 GLU A C     1 
ATOM   4029  O O     . GLU A 1 1964 ? 213.633 203.950 219.623 1.00 21.67 ? 1964 GLU A O     1 
ATOM   4030  C CB    . GLU A 1 1964 ? 212.793 205.214 216.625 1.00 26.25 ? 1964 GLU A CB    1 
ATOM   4031  C CG    . GLU A 1 1964 ? 214.309 205.247 216.540 1.00 22.06 ? 1964 GLU A CG    1 
ATOM   4032  C CD    . GLU A 1 1964 ? 214.882 206.630 216.768 1.00 23.45 ? 1964 GLU A CD    1 
ATOM   4033  O OE1   . GLU A 1 1964 ? 214.158 207.507 217.285 1.00 19.43 ? 1964 GLU A OE1   1 
ATOM   4034  O OE2   . GLU A 1 1964 ? 216.056 206.847 216.401 1.00 25.48 ? 1964 GLU A OE2   1 
ATOM   4035  N N     . GLU A 1 1965 ? 212.335 202.662 218.294 1.00 22.89 ? 1965 GLU A N     1 
ATOM   4036  C CA    . GLU A 1 1965 ? 212.529 201.442 219.075 1.00 24.73 ? 1965 GLU A CA    1 
ATOM   4037  C C     . GLU A 1 1965 ? 214.004 201.135 219.307 1.00 27.92 ? 1965 GLU A C     1 
ATOM   4038  O O     . GLU A 1 1965 ? 214.377 200.651 220.382 1.00 28.13 ? 1965 GLU A O     1 
ATOM   4039  C CB    . GLU A 1 1965 ? 211.844 200.266 218.381 1.00 24.03 ? 1965 GLU A CB    1 
ATOM   4040  C CG    . GLU A 1 1965 ? 210.479 199.928 218.951 1.00 26.21 ? 1965 GLU A CG    1 
ATOM   4041  C CD    . GLU A 1 1965 ? 210.518 199.700 220.450 1.00 29.20 ? 1965 GLU A CD    1 
ATOM   4042  O OE1   . GLU A 1 1965 ? 211.377 198.920 220.912 1.00 31.90 ? 1965 GLU A OE1   1 
ATOM   4043  O OE2   . GLU A 1 1965 ? 209.691 200.303 221.166 1.00 28.35 ? 1965 GLU A OE2   1 
ATOM   4044  N N     . ARG A 1 1966 ? 214.858 201.416 218.321 1.00 29.65 ? 1966 ARG A N     1 
ATOM   4045  C CA    . ARG A 1 1966 ? 216.270 201.064 218.445 1.00 30.01 ? 1966 ARG A CA    1 
ATOM   4046  C C     . ARG A 1 1966 ? 216.913 201.760 219.637 1.00 29.67 ? 1966 ARG A C     1 
ATOM   4047  O O     . ARG A 1 1966 ? 217.543 201.115 220.483 1.00 28.52 ? 1966 ARG A O     1 
ATOM   4048  C CB    . ARG A 1 1966 ? 217.016 201.420 217.160 1.00 29.86 ? 1966 ARG A CB    1 
ATOM   4049  C CG    . ARG A 1 1966 ? 218.468 200.978 217.163 1.00 29.67 ? 1966 ARG A CG    1 
ATOM   4050  C CD    . ARG A 1 1966 ? 219.141 201.283 215.840 1.00 31.66 ? 1966 ARG A CD    1 
ATOM   4051  N NE    . ARG A 1 1966 ? 219.214 202.717 215.590 1.00 33.83 ? 1966 ARG A NE    1 
ATOM   4052  C CZ    . ARG A 1 1966 ? 218.557 203.341 214.622 1.00 34.34 ? 1966 ARG A CZ    1 
ATOM   4053  N NH1   . ARG A 1 1966 ? 217.758 202.686 213.796 1.00 30.18 ? 1966 ARG A NH1   1 
ATOM   4054  N NH2   . ARG A 1 1966 ? 218.704 204.655 214.481 1.00 35.25 ? 1966 ARG A NH2   1 
ATOM   4055  N N     . MET A 1 1967 ? 216.766 203.083 219.719 1.00 21.42 ? 1967 MET A N     1 
ATOM   4056  C CA    . MET A 1 1967 ? 217.365 203.821 220.825 1.00 16.65 ? 1967 MET A CA    1 
ATOM   4057  C C     . MET A 1 1967 ? 216.495 203.750 222.074 1.00 20.10 ? 1967 MET A C     1 
ATOM   4058  O O     . MET A 1 1967 ? 217.007 203.831 223.198 1.00 24.32 ? 1967 MET A O     1 
ATOM   4059  C CB    . MET A 1 1967 ? 217.617 205.269 220.407 1.00 15.83 ? 1967 MET A CB    1 
ATOM   4060  C CG    . MET A 1 1967 ? 216.427 205.978 219.803 1.00 21.78 ? 1967 MET A CG    1 
ATOM   4061  S SD    . MET A 1 1967 ? 216.877 207.619 219.208 1.00 25.89 ? 1967 MET A SD    1 
ATOM   4062  C CE    . MET A 1 1967 ? 218.512 207.311 218.550 1.00 22.43 ? 1967 MET A CE    1 
ATOM   4063  N N     . LEU A 1 1968 ? 215.180 203.592 221.897 1.00 15.41 ? 1968 LEU A N     1 
ATOM   4064  C CA    . LEU A 1 1968 ? 214.294 203.445 223.047 1.00 14.59 ? 1968 LEU A CA    1 
ATOM   4065  C C     . LEU A 1 1968 ? 214.660 202.218 223.865 1.00 19.88 ? 1968 LEU A C     1 
ATOM   4066  O O     . LEU A 1 1968 ? 214.673 202.272 225.097 1.00 20.89 ? 1968 LEU A O     1 
ATOM   4067  C CB    . LEU A 1 1968 ? 212.837 203.358 222.594 1.00 17.77 ? 1968 LEU A CB    1 
ATOM   4068  C CG    . LEU A 1 1968 ? 211.764 203.504 223.677 1.00 12.73 ? 1968 LEU A CG    1 
ATOM   4069  C CD1   . LEU A 1 1968 ? 210.600 204.332 223.171 1.00 15.65 ? 1968 LEU A CD1   1 
ATOM   4070  C CD2   . LEU A 1 1968 ? 211.276 202.142 224.142 1.00 14.84 ? 1968 LEU A CD2   1 
ATOM   4071  N N     . SER A 1 1969 ? 214.962 201.102 223.199 1.00 18.82 ? 1969 SER A N     1 
ATOM   4072  C CA    . SER A 1 1969 ? 215.287 199.876 223.920 1.00 19.16 ? 1969 SER A CA    1 
ATOM   4073  C C     . SER A 1 1969 ? 216.552 200.036 224.755 1.00 18.04 ? 1969 SER A C     1 
ATOM   4074  O O     . SER A 1 1969 ? 216.601 199.597 225.908 1.00 19.48 ? 1969 SER A O     1 
ATOM   4075  C CB    . SER A 1 1969 ? 215.432 198.716 222.936 1.00 20.99 ? 1969 SER A CB    1 
ATOM   4076  O OG    . SER A 1 1969 ? 214.197 198.436 222.302 1.00 22.46 ? 1969 SER A OG    1 
ATOM   4077  N N     . ALA A 1 1970 ? 217.582 200.675 224.199 1.00 12.93 ? 1970 ALA A N     1 
ATOM   4078  C CA    . ALA A 1 1970 ? 218.837 200.810 224.933 1.00 12.40 ? 1970 ALA A CA    1 
ATOM   4079  C C     . ALA A 1 1970 ? 218.721 201.834 226.057 1.00 18.84 ? 1970 ALA A C     1 
ATOM   4080  O O     . ALA A 1 1970 ? 219.271 201.629 227.150 1.00 25.24 ? 1970 ALA A O     1 
ATOM   4081  C CB    . ALA A 1 1970 ? 219.966 201.174 223.975 1.00 14.25 ? 1970 ALA A CB    1 
ATOM   4082  N N     . VAL A 1 1971 ? 218.008 202.940 225.821 1.00 17.81 ? 1971 VAL A N     1 
ATOM   4083  C CA    . VAL A 1 1971 ? 217.762 203.889 226.904 1.00 13.29 ? 1971 VAL A CA    1 
ATOM   4084  C C     . VAL A 1 1971 ? 216.949 203.227 228.008 1.00 11.10 ? 1971 VAL A C     1 
ATOM   4085  O O     . VAL A 1 1971 ? 217.197 203.450 229.198 1.00 13.55 ? 1971 VAL A O     1 
ATOM   4086  C CB    . VAL A 1 1971 ? 217.072 205.158 226.372 1.00 11.19 ? 1971 VAL A CB    1 
ATOM   4087  C CG1   . VAL A 1 1971 ? 216.722 206.085 227.519 1.00 12.26 ? 1971 VAL A CG1   1 
ATOM   4088  C CG2   . VAL A 1 1971 ? 217.978 205.879 225.401 1.00 11.95 ? 1971 VAL A CG2   1 
ATOM   4089  N N     . SER A 1 1972 ? 215.975 202.395 227.634 1.00 5.33  ? 1972 SER A N     1 
ATOM   4090  C CA    . SER A 1 1972 ? 215.189 201.670 228.622 1.00 2.81  ? 1972 SER A CA    1 
ATOM   4091  C C     . SER A 1 1972 ? 216.054 200.693 229.402 1.00 7.02  ? 1972 SER A C     1 
ATOM   4092  O O     . SER A 1 1972 ? 215.865 200.520 230.606 1.00 20.80 ? 1972 SER A O     1 
ATOM   4093  C CB    . SER A 1 1972 ? 214.039 200.937 227.937 1.00 9.23  ? 1972 SER A CB    1 
ATOM   4094  O OG    . SER A 1 1972 ? 213.140 201.852 227.339 1.00 16.38 ? 1972 SER A OG    1 
ATOM   4095  N N     . GLN A 1 1973 ? 217.000 200.037 228.730 1.00 4.03  ? 1973 GLN A N     1 
ATOM   4096  C CA    . GLN A 1 1973 ? 217.908 199.133 229.428 1.00 8.68  ? 1973 GLN A CA    1 
ATOM   4097  C C     . GLN A 1 1973 ? 218.752 199.882 230.452 1.00 6.46  ? 1973 GLN A C     1 
ATOM   4098  O O     . GLN A 1 1973 ? 218.908 199.427 231.593 1.00 7.70  ? 1973 GLN A O     1 
ATOM   4099  C CB    . GLN A 1 1973 ? 218.799 198.408 228.420 1.00 13.60 ? 1973 GLN A CB    1 
ATOM   4100  C CG    . GLN A 1 1973 ? 219.500 197.176 228.972 1.00 13.83 ? 1973 GLN A CG    1 
ATOM   4101  C CD    . GLN A 1 1973 ? 220.816 197.508 229.647 1.00 17.40 ? 1973 GLN A CD    1 
ATOM   4102  O OE1   . GLN A 1 1973 ? 221.481 198.480 229.290 1.00 17.77 ? 1973 GLN A OE1   1 
ATOM   4103  N NE2   . GLN A 1 1973 ? 221.199 196.700 230.628 1.00 10.64 ? 1973 GLN A NE2   1 
ATOM   4104  N N     . GLN A 1 1974 ? 219.304 201.034 230.066 1.00 3.65  ? 1974 GLN A N     1 
ATOM   4105  C CA    . GLN A 1 1974 ? 220.105 201.809 231.011 1.00 4.45  ? 1974 GLN A CA    1 
ATOM   4106  C C     . GLN A 1 1974 ? 219.255 202.323 232.169 1.00 7.38  ? 1974 GLN A C     1 
ATOM   4107  O O     . GLN A 1 1974 ? 219.681 202.283 233.331 1.00 11.79 ? 1974 GLN A O     1 
ATOM   4108  C CB    . GLN A 1 1974 ? 220.796 202.968 230.295 1.00 7.51  ? 1974 GLN A CB    1 
ATOM   4109  C CG    . GLN A 1 1974 ? 221.675 202.541 229.136 1.00 7.68  ? 1974 GLN A CG    1 
ATOM   4110  C CD    . GLN A 1 1974 ? 222.572 203.657 228.644 1.00 13.49 ? 1974 GLN A CD    1 
ATOM   4111  O OE1   . GLN A 1 1974 ? 222.887 204.585 229.385 1.00 13.70 ? 1974 GLN A OE1   1 
ATOM   4112  N NE2   . GLN A 1 1974 ? 222.986 203.573 227.387 1.00 14.49 ? 1974 GLN A NE2   1 
ATOM   4113  N N     . VAL A 1 1975 ? 218.045 202.800 231.872 1.00 12.88 ? 1975 VAL A N     1 
ATOM   4114  C CA    . VAL A 1 1975 ? 217.152 203.288 232.917 1.00 2.70  ? 1975 VAL A CA    1 
ATOM   4115  C C     . VAL A 1 1975 ? 216.767 202.157 233.862 1.00 0.56  ? 1975 VAL A C     1 
ATOM   4116  O O     . VAL A 1 1975 ? 216.674 202.354 235.077 1.00 5.33  ? 1975 VAL A O     1 
ATOM   4117  C CB    . VAL A 1 1975 ? 215.915 203.952 232.284 1.00 0.00  ? 1975 VAL A CB    1 
ATOM   4118  C CG1   . VAL A 1 1975 ? 214.803 204.096 233.299 1.00 4.12  ? 1975 VAL A CG1   1 
ATOM   4119  C CG2   . VAL A 1 1975 ? 216.281 205.302 231.701 1.00 3.11  ? 1975 VAL A CG2   1 
ATOM   4120  N N     . GLN A 1 1976 ? 216.535 200.958 233.322 1.00 1.76  ? 1976 GLN A N     1 
ATOM   4121  C CA    . GLN A 1 1976 ? 216.224 199.805 234.158 1.00 3.75  ? 1976 GLN A CA    1 
ATOM   4122  C C     . GLN A 1 1976 ? 217.398 199.439 235.050 1.00 9.65  ? 1976 GLN A C     1 
ATOM   4123  O O     . GLN A 1 1976 ? 217.211 199.107 236.225 1.00 18.71 ? 1976 GLN A O     1 
ATOM   4124  C CB    . GLN A 1 1976 ? 215.834 198.614 233.286 1.00 3.60  ? 1976 GLN A CB    1 
ATOM   4125  C CG    . GLN A 1 1976 ? 215.318 197.426 234.074 1.00 8.53  ? 1976 GLN A CG    1 
ATOM   4126  C CD    . GLN A 1 1976 ? 215.411 196.132 233.300 1.00 11.11 ? 1976 GLN A CD    1 
ATOM   4127  O OE1   . GLN A 1 1976 ? 215.475 196.133 232.072 1.00 9.76  ? 1976 GLN A OE1   1 
ATOM   4128  N NE2   . GLN A 1 1976 ? 215.423 195.016 234.016 1.00 15.51 ? 1976 GLN A NE2   1 
ATOM   4129  N N     . CYS A 1 1977 ? 218.615 199.479 234.509 1.00 5.89  ? 1977 CYS A N     1 
ATOM   4130  C CA    . CYS A 1 1977 ? 219.785 199.222 235.339 1.00 2.75  ? 1977 CYS A CA    1 
ATOM   4131  C C     . CYS A 1 1977 ? 219.868 200.227 236.478 1.00 2.24  ? 1977 CYS A C     1 
ATOM   4132  O O     . CYS A 1 1977 ? 220.113 199.854 237.633 1.00 3.19  ? 1977 CYS A O     1 
ATOM   4133  C CB    . CYS A 1 1977 ? 221.053 199.264 234.487 1.00 10.85 ? 1977 CYS A CB    1 
ATOM   4134  S SG    . CYS A 1 1977 ? 222.555 198.787 235.365 1.00 39.44 ? 1977 CYS A SG    1 
ATOM   4135  N N     . ILE A 1 1978 ? 219.627 201.505 236.175 1.00 10.90 ? 1978 ILE A N     1 
ATOM   4136  C CA    . ILE A 1 1978 ? 219.698 202.544 237.201 1.00 6.62  ? 1978 ILE A CA    1 
ATOM   4137  C C     . ILE A 1 1978 ? 218.621 202.322 238.257 1.00 4.95  ? 1978 ILE A C     1 
ATOM   4138  O O     . ILE A 1 1978 ? 218.872 202.438 239.462 1.00 9.10  ? 1978 ILE A O     1 
ATOM   4139  C CB    . ILE A 1 1978 ? 219.572 203.939 236.566 1.00 4.73  ? 1978 ILE A CB    1 
ATOM   4140  C CG1   . ILE A 1 1978 ? 220.732 204.193 235.610 1.00 4.60  ? 1978 ILE A CG1   1 
ATOM   4141  C CG2   . ILE A 1 1978 ? 219.568 205.000 237.647 1.00 2.71  ? 1978 ILE A CG2   1 
ATOM   4142  C CD1   . ILE A 1 1978 ? 222.043 204.309 236.293 1.00 7.98  ? 1978 ILE A CD1   1 
ATOM   4143  N N     . GLN A 1 1979 ? 217.402 202.009 237.818 1.00 1.16  ? 1979 GLN A N     1 
ATOM   4144  C CA    . GLN A 1 1979 ? 216.295 201.830 238.750 1.00 0.00  ? 1979 GLN A CA    1 
ATOM   4145  C C     . GLN A 1 1979 ? 216.498 200.612 239.637 1.00 2.21  ? 1979 GLN A C     1 
ATOM   4146  O O     . GLN A 1 1979 ? 216.178 200.652 240.828 1.00 12.45 ? 1979 GLN A O     1 
ATOM   4147  C CB    . GLN A 1 1979 ? 214.976 201.722 237.990 1.00 3.68  ? 1979 GLN A CB    1 
ATOM   4148  C CG    . GLN A 1 1979 ? 214.296 203.053 237.749 1.00 3.53  ? 1979 GLN A CG    1 
ATOM   4149  C CD    . GLN A 1 1979 ? 213.933 203.756 239.039 1.00 2.45  ? 1979 GLN A CD    1 
ATOM   4150  O OE1   . GLN A 1 1979 ? 212.891 203.485 239.630 1.00 1.95  ? 1979 GLN A OE1   1 
ATOM   4151  N NE2   . GLN A 1 1979 ? 214.787 204.670 239.479 1.00 9.39  ? 1979 GLN A NE2   1 
ATOM   4152  N N     . GLU A 1 1980 ? 217.015 199.516 239.082 1.00 5.99  ? 1980 GLU A N     1 
ATOM   4153  C CA    . GLU A 1 1980 ? 217.270 198.342 239.909 1.00 3.03  ? 1980 GLU A CA    1 
ATOM   4154  C C     . GLU A 1 1980 ? 218.439 198.571 240.858 1.00 6.36  ? 1980 GLU A C     1 
ATOM   4155  O O     . GLU A 1 1980 ? 218.446 198.027 241.967 1.00 6.26  ? 1980 GLU A O     1 
ATOM   4156  C CB    . GLU A 1 1980 ? 217.514 197.115 239.033 1.00 6.31  ? 1980 GLU A CB    1 
ATOM   4157  C CG    . GLU A 1 1980 ? 216.352 196.779 238.112 1.00 8.37  ? 1980 GLU A CG    1 
ATOM   4158  C CD    . GLU A 1 1980 ? 215.402 195.758 238.707 1.00 12.21 ? 1980 GLU A CD    1 
ATOM   4159  O OE1   . GLU A 1 1980 ? 215.129 195.833 239.924 1.00 9.44  ? 1980 GLU A OE1   1 
ATOM   4160  O OE2   . GLU A 1 1980 ? 214.923 194.883 237.956 1.00 10.68 ? 1980 GLU A OE2   1 
ATOM   4161  N N     . ALA A 1 1981 ? 219.429 199.370 240.453 1.00 8.05  ? 1981 ALA A N     1 
ATOM   4162  C CA    . ALA A 1 1981 ? 220.492 199.739 241.379 1.00 9.22  ? 1981 ALA A CA    1 
ATOM   4163  C C     . ALA A 1 1981 ? 219.985 200.643 242.493 1.00 7.95  ? 1981 ALA A C     1 
ATOM   4164  O O     . ALA A 1 1981 ? 220.473 200.562 243.624 1.00 17.69 ? 1981 ALA A O     1 
ATOM   4165  C CB    . ALA A 1 1981 ? 221.629 200.430 240.628 1.00 7.87  ? 1981 ALA A CB    1 
ATOM   4166  N N     . LEU A 1 1982 ? 219.016 201.505 242.188 1.00 9.97  ? 1982 LEU A N     1 
ATOM   4167  C CA    . LEU A 1 1982 ? 218.504 202.460 243.163 1.00 8.46  ? 1982 LEU A CA    1 
ATOM   4168  C C     . LEU A 1 1982 ? 217.468 201.835 244.088 1.00 4.08  ? 1982 LEU A C     1 
ATOM   4169  O O     . LEU A 1 1982 ? 217.302 202.292 245.223 1.00 7.59  ? 1982 LEU A O     1 
ATOM   4170  C CB    . LEU A 1 1982 ? 217.908 203.661 242.429 1.00 10.32 ? 1982 LEU A CB    1 
ATOM   4171  C CG    . LEU A 1 1982 ? 217.706 204.972 243.181 1.00 10.58 ? 1982 LEU A CG    1 
ATOM   4172  C CD1   . LEU A 1 1982 ? 219.043 205.536 243.625 1.00 6.99  ? 1982 LEU A CD1   1 
ATOM   4173  C CD2   . LEU A 1 1982 ? 216.978 205.961 242.290 1.00 5.50  ? 1982 LEU A CD2   1 
ATOM   4174  N N     . ARG A 1 1983 ? 216.764 200.803 243.621 1.00 8.23  ? 1983 ARG A N     1 
ATOM   4175  C CA    . ARG A 1 1983 ? 215.776 200.118 244.443 1.00 5.37  ? 1983 ARG A CA    1 
ATOM   4176  C C     . ARG A 1 1983 ? 216.405 199.422 245.640 1.00 16.21 ? 1983 ARG A C     1 
ATOM   4177  O O     . ARG A 1 1983 ? 215.735 199.244 246.663 1.00 18.24 ? 1983 ARG A O     1 
ATOM   4178  C CB    . ARG A 1 1983 ? 215.010 199.100 243.596 1.00 0.92  ? 1983 ARG A CB    1 
ATOM   4179  C CG    . ARG A 1 1983 ? 213.765 198.542 244.256 1.00 7.84  ? 1983 ARG A CG    1 
ATOM   4180  C CD    . ARG A 1 1983 ? 212.690 199.598 244.380 1.00 9.30  ? 1983 ARG A CD    1 
ATOM   4181  N NE    . ARG A 1 1983 ? 211.541 199.122 245.141 1.00 16.44 ? 1983 ARG A NE    1 
ATOM   4182  C CZ    . ARG A 1 1983 ? 210.516 198.464 244.620 1.00 13.99 ? 1983 ARG A CZ    1 
ATOM   4183  N NH1   . ARG A 1 1983 ? 210.483 198.140 243.338 1.00 7.40  ? 1983 ARG A NH1   1 
ATOM   4184  N NH2   . ARG A 1 1983 ? 209.502 198.114 245.406 1.00 16.47 ? 1983 ARG A NH2   1 
ATOM   4185  N N     . GLU A 1 1984 ? 217.677 199.032 245.538 1.00 24.51 ? 1984 GLU A N     1 
ATOM   4186  C CA    . GLU A 1 1984 ? 218.339 198.337 246.634 1.00 21.61 ? 1984 GLU A CA    1 
ATOM   4187  C C     . GLU A 1 1984 ? 218.763 199.279 247.753 1.00 21.92 ? 1984 GLU A C     1 
ATOM   4188  O O     . GLU A 1 1984 ? 219.221 198.807 248.798 1.00 28.59 ? 1984 GLU A O     1 
ATOM   4189  C CB    . GLU A 1 1984 ? 219.544 197.560 246.106 1.00 17.93 ? 1984 GLU A CB    1 
ATOM   4190  C CG    . GLU A 1 1984 ? 219.223 196.708 244.888 1.00 21.08 ? 1984 GLU A CG    1 
ATOM   4191  C CD    . GLU A 1 1984 ? 220.459 196.221 244.164 1.00 25.43 ? 1984 GLU A CD    1 
ATOM   4192  O OE1   . GLU A 1 1984 ? 221.533 196.826 244.346 1.00 22.45 ? 1984 GLU A OE1   1 
ATOM   4193  O OE2   . GLU A 1 1984 ? 220.355 195.231 243.409 1.00 26.05 ? 1984 GLU A OE2   1 
ATOM   4194  N N     . HIS A 1 1985 ? 218.628 200.594 247.562 1.00 13.46 ? 1985 HIS A N     1 
ATOM   4195  C CA    . HIS A 1 1985 ? 218.897 201.527 248.649 1.00 12.11 ? 1985 HIS A CA    1 
ATOM   4196  C C     . HIS A 1 1985 ? 217.880 201.408 249.775 1.00 22.03 ? 1985 HIS A C     1 
ATOM   4197  O O     . HIS A 1 1985 ? 218.155 201.859 250.891 1.00 29.88 ? 1985 HIS A O     1 
ATOM   4198  C CB    . HIS A 1 1985 ? 218.921 202.965 248.131 1.00 14.98 ? 1985 HIS A CB    1 
ATOM   4199  C CG    . HIS A 1 1985 ? 220.177 203.325 247.401 1.00 18.95 ? 1985 HIS A CG    1 
ATOM   4200  N ND1   . HIS A 1 1985 ? 220.459 202.866 246.133 1.00 18.78 ? 1985 HIS A ND1   1 
ATOM   4201  C CD2   . HIS A 1 1985 ? 221.232 204.089 247.767 1.00 15.97 ? 1985 HIS A CD2   1 
ATOM   4202  C CE1   . HIS A 1 1985 ? 221.630 203.339 245.746 1.00 11.91 ? 1985 HIS A CE1   1 
ATOM   4203  N NE2   . HIS A 1 1985 ? 222.121 204.083 246.720 1.00 15.46 ? 1985 HIS A NE2   1 
ATOM   4204  N N     . SER A 1 1986 ? 216.718 200.817 249.510 1.00 25.99 ? 1986 SER A N     1 
ATOM   4205  C CA    . SER A 1 1986 ? 215.667 200.636 250.502 1.00 31.38 ? 1986 SER A CA    1 
ATOM   4206  C C     . SER A 1 1986 ? 215.475 199.160 250.827 1.00 32.71 ? 1986 SER A C     1 
ATOM   4207  O O     . SER A 1 1986 ? 214.356 198.694 251.051 1.00 35.86 ? 1986 SER A O     1 
ATOM   4208  C CB    . SER A 1 1986 ? 214.357 201.255 250.025 1.00 32.17 ? 1986 SER A CB    1 
ATOM   4209  O OG    . SER A 1 1986 ? 213.692 200.399 249.112 1.00 36.63 ? 1986 SER A OG    1 
ATOM   4210  N N     . ASN A 1 1987 ? 216.571 198.408 250.849 1.00 39.71 ? 1987 ASN A N     1 
ATOM   4211  C CA    . ASN A 1 1987 ? 216.494 196.997 251.193 1.00 44.08 ? 1987 ASN A CA    1 
ATOM   4212  C C     . ASN A 1 1987 ? 216.099 196.834 252.659 1.00 45.85 ? 1987 ASN A C     1 
ATOM   4213  O O     . ASN A 1 1987 ? 216.635 197.528 253.529 1.00 43.98 ? 1987 ASN A O     1 
ATOM   4214  C CB    . ASN A 1 1987 ? 217.833 196.307 250.935 1.00 42.34 ? 1987 ASN A CB    1 
ATOM   4215  C CG    . ASN A 1 1987 ? 218.007 195.898 249.486 1.00 45.06 ? 1987 ASN A CG    1 
ATOM   4216  O OD1   . ASN A 1 1987 ? 217.119 196.105 248.659 1.00 47.35 ? 1987 ASN A OD1   1 
ATOM   4217  N ND2   . ASN A 1 1987 ? 219.158 195.316 249.169 1.00 43.98 ? 1987 ASN A ND2   1 
ATOM   4218  N N     . PRO A 1 1988 ? 215.156 195.938 252.963 1.00 48.04 ? 1988 PRO A N     1 
ATOM   4219  C CA    . PRO A 1 1988 ? 214.780 195.726 254.370 1.00 48.40 ? 1988 PRO A CA    1 
ATOM   4220  C C     . PRO A 1 1988 ? 215.928 195.236 255.233 1.00 48.59 ? 1988 PRO A C     1 
ATOM   4221  O O     . PRO A 1 1988 ? 215.998 195.593 256.416 1.00 48.67 ? 1988 PRO A O     1 
ATOM   4222  C CB    . PRO A 1 1988 ? 213.655 194.686 254.279 1.00 47.36 ? 1988 PRO A CB    1 
ATOM   4223  C CG    . PRO A 1 1988 ? 213.890 193.984 252.984 1.00 48.10 ? 1988 PRO A CG    1 
ATOM   4224  C CD    . PRO A 1 1988 ? 214.465 195.010 252.052 1.00 44.98 ? 1988 PRO A CD    1 
ATOM   4225  N N     . ASN A 1 1989 ? 216.834 194.432 254.678 1.00 54.10 ? 1989 ASN A N     1 
ATOM   4226  C CA    . ASN A 1 1989 ? 217.960 193.899 255.427 1.00 54.47 ? 1989 ASN A CA    1 
ATOM   4227  C C     . ASN A 1 1989 ? 219.281 194.581 255.105 1.00 54.12 ? 1989 ASN A C     1 
ATOM   4228  O O     . ASN A 1 1989 ? 220.264 194.355 255.819 1.00 53.95 ? 1989 ASN A O     1 
ATOM   4229  C CB    . ASN A 1 1989 ? 218.098 192.389 255.177 1.00 51.46 ? 1989 ASN A CB    1 
ATOM   4230  C CG    . ASN A 1 1989 ? 218.596 192.073 253.781 1.00 54.02 ? 1989 ASN A CG    1 
ATOM   4231  O OD1   . ASN A 1 1989 ? 217.910 192.332 252.791 1.00 54.88 ? 1989 ASN A OD1   1 
ATOM   4232  N ND2   . ASN A 1 1989 ? 219.797 191.513 253.694 1.00 53.13 ? 1989 ASN A ND2   1 
ATOM   4233  N N     . TYR A 1 1990 ? 219.335 195.402 254.059 1.00 54.45 ? 1990 TYR A N     1 
ATOM   4234  C CA    . TYR A 1 1990 ? 220.540 196.131 253.686 1.00 56.14 ? 1990 TYR A CA    1 
ATOM   4235  C C     . TYR A 1 1990 ? 220.234 197.616 253.546 1.00 56.27 ? 1990 TYR A C     1 
ATOM   4236  O O     . TYR A 1 1990 ? 220.710 198.288 252.626 1.00 54.20 ? 1990 TYR A O     1 
ATOM   4237  C CB    . TYR A 1 1990 ? 221.141 195.571 252.398 1.00 56.10 ? 1990 TYR A CB    1 
ATOM   4238  C CG    . TYR A 1 1990 ? 222.560 196.023 252.126 1.00 58.08 ? 1990 TYR A CG    1 
ATOM   4239  C CD1   . TYR A 1 1990 ? 223.371 196.487 253.154 1.00 56.10 ? 1990 TYR A CD1   1 
ATOM   4240  C CD2   . TYR A 1 1990 ? 223.087 195.988 250.842 1.00 57.59 ? 1990 TYR A CD2   1 
ATOM   4241  C CE1   . TYR A 1 1990 ? 224.666 196.900 252.912 1.00 55.19 ? 1990 TYR A CE1   1 
ATOM   4242  C CE2   . TYR A 1 1990 ? 224.382 196.400 250.589 1.00 57.91 ? 1990 TYR A CE2   1 
ATOM   4243  C CZ    . TYR A 1 1990 ? 225.167 196.855 251.628 1.00 58.09 ? 1990 TYR A CZ    1 
ATOM   4244  O OH    . TYR A 1 1990 ? 226.457 197.267 251.382 1.00 57.50 ? 1990 TYR A OH    1 
ATOM   4245  N N     . ASP A 1 1991 ? 219.413 198.146 254.457 1.00 53.59 ? 1991 ASP A N     1 
ATOM   4246  C CA    . ASP A 1 1991 ? 219.084 199.567 254.418 1.00 54.33 ? 1991 ASP A CA    1 
ATOM   4247  C C     . ASP A 1 1991 ? 220.317 200.425 254.673 1.00 54.30 ? 1991 ASP A C     1 
ATOM   4248  O O     . ASP A 1 1991 ? 220.530 201.437 253.994 1.00 52.75 ? 1991 ASP A O     1 
ATOM   4249  C CB    . ASP A 1 1991 ? 217.985 199.879 255.434 1.00 51.64 ? 1991 ASP A CB    1 
ATOM   4250  C CG    . ASP A 1 1991 ? 218.313 199.367 256.824 1.00 51.79 ? 1991 ASP A CG    1 
ATOM   4251  O OD1   . ASP A 1 1991 ? 218.658 198.174 256.952 1.00 52.79 ? 1991 ASP A OD1   1 
ATOM   4252  O OD2   . ASP A 1 1991 ? 218.221 200.156 257.787 1.00 50.43 ? 1991 ASP A OD2   1 
ATOM   4253  N N     . LYS A 1 1992 ? 221.143 200.036 255.641 1.00 53.45 ? 1992 LYS A N     1 
ATOM   4254  C CA    . LYS A 1 1992 ? 222.391 200.740 255.915 1.00 53.20 ? 1992 LYS A CA    1 
ATOM   4255  C C     . LYS A 1 1992 ? 223.466 200.184 254.990 1.00 54.11 ? 1992 LYS A C     1 
ATOM   4256  O O     . LYS A 1 1992 ? 224.002 199.098 255.230 1.00 52.88 ? 1992 LYS A O     1 
ATOM   4257  C CB    . LYS A 1 1992 ? 222.784 200.587 257.382 1.00 51.50 ? 1992 LYS A CB    1 
ATOM   4258  C CG    . LYS A 1 1992 ? 223.920 201.500 257.821 1.00 53.35 ? 1992 LYS A CG    1 
ATOM   4259  C CD    . LYS A 1 1992 ? 225.264 200.789 257.773 1.00 53.05 ? 1992 LYS A CD    1 
ATOM   4260  C CE    . LYS A 1 1992 ? 226.384 201.685 258.271 1.00 53.70 ? 1992 LYS A CE    1 
ATOM   4261  N NZ    . LYS A 1 1992 ? 227.706 201.004 258.194 1.00 52.59 ? 1992 LYS A NZ    1 
ATOM   4262  N N     . THR A 1 1993 ? 223.783 200.927 253.934 1.00 54.01 ? 1993 THR A N     1 
ATOM   4263  C CA    . THR A 1 1993 ? 224.725 200.481 252.911 1.00 54.15 ? 1993 THR A CA    1 
ATOM   4264  C C     . THR A 1 1993 ? 226.104 201.036 253.251 1.00 54.76 ? 1993 THR A C     1 
ATOM   4265  O O     . THR A 1 1993 ? 226.429 202.175 252.907 1.00 53.14 ? 1993 THR A O     1 
ATOM   4266  C CB    . THR A 1 1993 ? 224.273 200.925 251.524 1.00 52.84 ? 1993 THR A CB    1 
ATOM   4267  O OG1   . THR A 1 1993 ? 223.871 202.301 251.566 1.00 52.71 ? 1993 THR A OG1   1 
ATOM   4268  C CG2   . THR A 1 1993 ? 223.101 200.079 251.050 1.00 50.51 ? 1993 THR A CG2   1 
ATOM   4269  N N     . SER A 1 1994 ? 226.914 200.226 253.939 1.00 47.74 ? 1994 SER A N     1 
ATOM   4270  C CA    . SER A 1 1994 ? 228.299 200.610 254.187 1.00 43.99 ? 1994 SER A CA    1 
ATOM   4271  C C     . SER A 1 1994 ? 229.069 200.742 252.880 1.00 41.53 ? 1994 SER A C     1 
ATOM   4272  O O     . SER A 1 1994 ? 229.827 201.700 252.689 1.00 40.63 ? 1994 SER A O     1 
ATOM   4273  C CB    . SER A 1 1994 ? 228.970 199.589 255.107 1.00 42.76 ? 1994 SER A CB    1 
ATOM   4274  O OG    . SER A 1 1994 ? 230.258 200.027 255.504 1.00 43.52 ? 1994 SER A OG    1 
ATOM   4275  N N     . ALA A 1 1995 ? 228.884 199.789 251.967 1.00 37.56 ? 1995 ALA A N     1 
ATOM   4276  C CA    . ALA A 1 1995 ? 229.441 199.881 250.628 1.00 40.09 ? 1995 ALA A CA    1 
ATOM   4277  C C     . ALA A 1 1995 ? 228.396 200.477 249.701 1.00 39.97 ? 1995 ALA A C     1 
ATOM   4278  O O     . ALA A 1 1995 ? 227.281 199.937 249.618 1.00 37.49 ? 1995 ALA A O     1 
ATOM   4279  C CB    . ALA A 1 1995 ? 229.873 198.509 250.126 1.00 37.76 ? 1995 ALA A CB    1 
ATOM   4280  N N     . PRO A 1 1996 ? 228.689 201.576 249.008 1.00 36.90 ? 1996 PRO A N     1 
ATOM   4281  C CA    . PRO A 1 1996 ? 227.674 202.197 248.150 1.00 36.07 ? 1996 PRO A CA    1 
ATOM   4282  C C     . PRO A 1 1996 ? 227.248 201.270 247.021 1.00 32.77 ? 1996 PRO A C     1 
ATOM   4283  O O     . PRO A 1 1996 ? 228.038 200.478 246.503 1.00 30.42 ? 1996 PRO A O     1 
ATOM   4284  C CB    . PRO A 1 1996 ? 228.380 203.448 247.615 1.00 34.33 ? 1996 PRO A CB    1 
ATOM   4285  C CG    . PRO A 1 1996 ? 229.832 203.102 247.674 1.00 31.55 ? 1996 PRO A CG    1 
ATOM   4286  C CD    . PRO A 1 1996 ? 229.991 202.257 248.905 1.00 32.40 ? 1996 PRO A CD    1 
ATOM   4287  N N     . ILE A 1 1997 ? 225.975 201.379 246.646 1.00 22.89 ? 1997 ILE A N     1 
ATOM   4288  C CA    . ILE A 1 1997 ? 225.424 200.529 245.598 1.00 24.39 ? 1997 ILE A CA    1 
ATOM   4289  C C     . ILE A 1 1997 ? 225.831 201.065 244.234 1.00 23.36 ? 1997 ILE A C     1 
ATOM   4290  O O     . ILE A 1 1997 ? 225.738 202.269 243.966 1.00 23.44 ? 1997 ILE A O     1 
ATOM   4291  C CB    . ILE A 1 1997 ? 223.899 200.432 245.732 1.00 21.02 ? 1997 ILE A CB    1 
ATOM   4292  C CG1   . ILE A 1 1997 ? 223.516 200.258 247.201 1.00 26.06 ? 1997 ILE A CG1   1 
ATOM   4293  C CG2   . ILE A 1 1997 ? 223.367 199.292 244.891 1.00 21.29 ? 1997 ILE A CG2   1 
ATOM   4294  C CD1   . ILE A 1 1997 ? 222.040 200.280 247.452 1.00 21.68 ? 1997 ILE A CD1   1 
ATOM   4295  N N     . THR A 1 1998 ? 226.285 200.167 243.363 1.00 18.16 ? 1998 THR A N     1 
ATOM   4296  C CA    . THR A 1 1998 ? 226.790 200.524 242.049 1.00 18.48 ? 1998 THR A CA    1 
ATOM   4297  C C     . THR A 1 1998 ? 225.995 199.811 240.964 1.00 20.96 ? 1998 THR A C     1 
ATOM   4298  O O     . THR A 1 1998 ? 225.373 198.774 241.207 1.00 26.49 ? 1998 THR A O     1 
ATOM   4299  C CB    . THR A 1 1998 ? 228.273 200.165 241.908 1.00 21.99 ? 1998 THR A CB    1 
ATOM   4300  O OG1   . THR A 1 1998 ? 228.437 198.750 242.060 1.00 21.22 ? 1998 THR A OG1   1 
ATOM   4301  C CG2   . THR A 1 1998 ? 229.097 200.876 242.967 1.00 21.46 ? 1998 THR A CG2   1 
ATOM   4302  N N     . CYS A 1 1999 ? 226.013 200.387 239.768 1.00 20.65 ? 1999 CYS A N     1 
ATOM   4303  C CA    . CYS A 1 1999 ? 225.455 199.772 238.571 1.00 22.01 ? 1999 CYS A CA    1 
ATOM   4304  C C     . CYS A 1 1999 ? 226.544 199.704 237.502 1.00 23.44 ? 1999 CYS A C     1 
ATOM   4305  O O     . CYS A 1 1999 ? 227.705 200.042 237.747 1.00 24.91 ? 1999 CYS A O     1 
ATOM   4306  C CB    . CYS A 1 1999 ? 224.230 200.546 238.081 1.00 18.96 ? 1999 CYS A CB    1 
ATOM   4307  S SG    . CYS A 1 1999 ? 224.553 202.281 237.719 1.00 33.70 ? 1999 CYS A SG    1 
ATOM   4308  N N     . GLU A 1 2000 ? 226.164 199.266 236.304 1.00 24.38 ? 2000 GLU A N     1 
ATOM   4309  C CA    . GLU A 1 2000 ? 227.100 199.164 235.189 1.00 25.96 ? 2000 GLU A CA    1 
ATOM   4310  C C     . GLU A 1 2000 ? 226.522 199.914 234.000 1.00 24.65 ? 2000 GLU A C     1 
ATOM   4311  O O     . GLU A 1 2000 ? 225.536 199.470 233.404 1.00 24.36 ? 2000 GLU A O     1 
ATOM   4312  C CB    . GLU A 1 2000 ? 227.379 197.700 234.831 1.00 25.22 ? 2000 GLU A CB    1 
ATOM   4313  C CG    . GLU A 1 2000 ? 228.369 197.508 233.692 1.00 26.48 ? 2000 GLU A CG    1 
ATOM   4314  C CD    . GLU A 1 2000 ? 227.690 197.335 232.347 1.00 27.14 ? 2000 GLU A CD    1 
ATOM   4315  O OE1   . GLU A 1 2000 ? 226.778 196.487 232.244 1.00 23.13 ? 2000 GLU A OE1   1 
ATOM   4316  O OE2   . GLU A 1 2000 ? 228.064 198.048 231.393 1.00 29.14 ? 2000 GLU A OE2   1 
ATOM   4317  N N     . LEU A 1 2001 ? 227.135 201.045 233.659 1.00 21.38 ? 2001 LEU A N     1 
ATOM   4318  C CA    . LEU A 1 2001 ? 226.696 201.881 232.549 1.00 24.63 ? 2001 LEU A CA    1 
ATOM   4319  C C     . LEU A 1 2001 ? 227.732 201.976 231.443 1.00 26.17 ? 2001 LEU A C     1 
ATOM   4320  O O     . LEU A 1 2001 ? 227.416 201.717 230.276 1.00 25.84 ? 2001 LEU A O     1 
ATOM   4321  C CB    . LEU A 1 2001 ? 226.357 203.289 233.059 1.00 25.22 ? 2001 LEU A CB    1 
ATOM   4322  C CG    . LEU A 1 2001 ? 225.181 203.423 234.021 1.00 22.00 ? 2001 LEU A CG    1 
ATOM   4323  C CD1   . LEU A 1 2001 ? 225.113 204.843 234.541 1.00 15.24 ? 2001 LEU A CD1   1 
ATOM   4324  C CD2   . LEU A 1 2001 ? 223.885 203.040 233.328 1.00 21.87 ? 2001 LEU A CD2   1 
ATOM   4325  N N     . LEU A 1 2002 ? 228.969 202.341 231.780 1.00 33.80 ? 2002 LEU A N     1 
ATOM   4326  C CA    . LEU A 1 2002 ? 230.047 202.501 230.811 1.00 34.68 ? 2002 LEU A CA    1 
ATOM   4327  C C     . LEU A 1 2002 ? 230.957 201.282 230.754 1.00 36.91 ? 2002 LEU A C     1 
ATOM   4328  O O     . LEU A 1 2002 ? 232.178 201.432 230.602 1.00 38.53 ? 2002 LEU A O     1 
ATOM   4329  C CB    . LEU A 1 2002 ? 230.857 203.757 231.136 1.00 35.06 ? 2002 LEU A CB    1 
ATOM   4330  C CG    . LEU A 1 2002 ? 231.505 204.506 229.970 1.00 40.07 ? 2002 LEU A CG    1 
ATOM   4331  C CD1   . LEU A 1 2002 ? 230.452 205.250 229.163 1.00 36.25 ? 2002 LEU A CD1   1 
ATOM   4332  C CD2   . LEU A 1 2002 ? 232.579 205.458 230.475 1.00 36.72 ? 2002 LEU A CD2   1 
ATOM   4333  N N     . ASN A 1 2003 ? 230.392 200.081 230.895 1.00 34.76 ? 2003 ASN A N     1 
ATOM   4334  C CA    . ASN A 1 2003 ? 231.155 198.837 230.997 1.00 37.49 ? 2003 ASN A CA    1 
ATOM   4335  C C     . ASN A 1 2003 ? 232.061 198.839 232.225 1.00 36.85 ? 2003 ASN A C     1 
ATOM   4336  O O     . ASN A 1 2003 ? 233.093 198.162 232.253 1.00 38.91 ? 2003 ASN A O     1 
ATOM   4337  C CB    . ASN A 1 2003 ? 231.966 198.565 229.725 1.00 36.49 ? 2003 ASN A CB    1 
ATOM   4338  C CG    . ASN A 1 2003 ? 231.250 197.637 228.766 1.00 38.52 ? 2003 ASN A CG    1 
ATOM   4339  O OD1   . ASN A 1 2003 ? 230.520 196.737 229.182 1.00 39.39 ? 2003 ASN A OD1   1 
ATOM   4340  N ND2   . ASN A 1 2003 ? 231.457 197.849 227.472 1.00 37.85 ? 2003 ASN A ND2   1 
ATOM   4341  N N     . LYS A 1 2004 ? 231.678 199.602 233.246 1.00 29.76 ? 2004 LYS A N     1 
ATOM   4342  C CA    . LYS A 1 2004 ? 232.406 199.646 234.504 1.00 33.03 ? 2004 LYS A CA    1 
ATOM   4343  C C     . LYS A 1 2004 ? 231.446 200.071 235.604 1.00 34.64 ? 2004 LYS A C     1 
ATOM   4344  O O     . LYS A 1 2004 ? 230.424 200.713 235.348 1.00 33.68 ? 2004 LYS A O     1 
ATOM   4345  C CB    . LYS A 1 2004 ? 233.608 200.595 234.428 1.00 29.51 ? 2004 LYS A CB    1 
ATOM   4346  C CG    . LYS A 1 2004 ? 233.257 202.024 234.051 1.00 31.52 ? 2004 LYS A CG    1 
ATOM   4347  C CD    . LYS A 1 2004 ? 234.425 202.713 233.361 1.00 33.44 ? 2004 LYS A CD    1 
ATOM   4348  C CE    . LYS A 1 2004 ? 235.681 202.687 234.219 1.00 32.42 ? 2004 LYS A CE    1 
ATOM   4349  N NZ    . LYS A 1 2004 ? 235.480 203.365 235.528 1.00 30.64 ? 2004 LYS A NZ    1 
ATOM   4350  N N     . GLN A 1 2005 ? 231.784 199.703 236.836 1.00 26.64 ? 2005 GLN A N     1 
ATOM   4351  C CA    . GLN A 1 2005 ? 230.915 199.975 237.972 1.00 22.17 ? 2005 GLN A CA    1 
ATOM   4352  C C     . GLN A 1 2005 ? 231.007 201.440 238.376 1.00 24.53 ? 2005 GLN A C     1 
ATOM   4353  O O     . GLN A 1 2005 ? 232.104 201.979 238.550 1.00 25.83 ? 2005 GLN A O     1 
ATOM   4354  C CB    . GLN A 1 2005 ? 231.282 199.076 239.151 1.00 21.07 ? 2005 GLN A CB    1 
ATOM   4355  C CG    . GLN A 1 2005 ? 231.075 197.594 238.886 1.00 26.31 ? 2005 GLN A CG    1 
ATOM   4356  C CD    . GLN A 1 2005 ? 229.620 197.244 238.640 1.00 26.40 ? 2005 GLN A CD    1 
ATOM   4357  O OE1   . GLN A 1 2005 ? 228.748 197.562 239.447 1.00 24.26 ? 2005 GLN A OE1   1 
ATOM   4358  N NE2   . GLN A 1 2005 ? 229.352 196.588 237.518 1.00 23.07 ? 2005 GLN A NE2   1 
ATOM   4359  N N     . VAL A 1 2006 ? 229.850 202.081 238.528 1.00 21.42 ? 2006 VAL A N     1 
ATOM   4360  C CA    . VAL A 1 2006 ? 229.762 203.474 238.948 1.00 17.89 ? 2006 VAL A CA    1 
ATOM   4361  C C     . VAL A 1 2006 ? 228.827 203.563 240.146 1.00 20.20 ? 2006 VAL A C     1 
ATOM   4362  O O     . VAL A 1 2006 ? 227.773 202.918 240.175 1.00 19.16 ? 2006 VAL A O     1 
ATOM   4363  C CB    . VAL A 1 2006 ? 229.285 204.394 237.802 1.00 20.47 ? 2006 VAL A CB    1 
ATOM   4364  C CG1   . VAL A 1 2006 ? 230.277 204.361 236.650 1.00 22.38 ? 2006 VAL A CG1   1 
ATOM   4365  C CG2   . VAL A 1 2006 ? 227.902 203.991 237.317 1.00 19.11 ? 2006 VAL A CG2   1 
ATOM   4366  N N     . LYS A 1 2007 ? 229.226 204.346 241.144 1.00 19.86 ? 2007 LYS A N     1 
ATOM   4367  C CA    . LYS A 1 2007 ? 228.419 204.503 242.346 1.00 16.76 ? 2007 LYS A CA    1 
ATOM   4368  C C     . LYS A 1 2007 ? 227.140 205.272 242.036 1.00 15.06 ? 2007 LYS A C     1 
ATOM   4369  O O     . LYS A 1 2007 ? 227.135 206.200 241.224 1.00 13.30 ? 2007 LYS A O     1 
ATOM   4370  C CB    . LYS A 1 2007 ? 229.220 205.225 243.427 1.00 17.44 ? 2007 LYS A CB    1 
ATOM   4371  C CG    . LYS A 1 2007 ? 230.433 204.452 243.916 1.00 19.59 ? 2007 LYS A CG    1 
ATOM   4372  C CD    . LYS A 1 2007 ? 231.180 205.218 244.995 1.00 20.20 ? 2007 LYS A CD    1 
ATOM   4373  C CE    . LYS A 1 2007 ? 232.402 204.449 245.472 1.00 21.55 ? 2007 LYS A CE    1 
ATOM   4374  N NZ    . LYS A 1 2007 ? 233.150 205.194 246.520 1.00 20.42 ? 2007 LYS A NZ    1 
ATOM   4375  N N     . VAL A 1 2008 ? 226.052 204.882 242.692 1.00 12.66 ? 2008 VAL A N     1 
ATOM   4376  C CA    . VAL A 1 2008 ? 224.744 205.494 242.490 1.00 14.38 ? 2008 VAL A CA    1 
ATOM   4377  C C     . VAL A 1 2008 ? 224.356 206.199 243.781 1.00 8.56  ? 2008 VAL A C     1 
ATOM   4378  O O     . VAL A 1 2008 ? 224.137 205.551 244.812 1.00 9.02  ? 2008 VAL A O     1 
ATOM   4379  C CB    . VAL A 1 2008 ? 223.685 204.460 242.088 1.00 14.82 ? 2008 VAL A CB    1 
ATOM   4380  C CG1   . VAL A 1 2008 ? 222.411 205.155 241.643 1.00 11.54 ? 2008 VAL A CG1   1 
ATOM   4381  C CG2   . VAL A 1 2008 ? 224.216 203.566 240.989 1.00 16.50 ? 2008 VAL A CG2   1 
ATOM   4382  N N     . SER A 1 2009 ? 224.268 207.522 243.728 1.00 1.85  ? 2009 SER A N     1 
ATOM   4383  C CA    . SER A 1 2009 ? 223.848 208.280 244.896 1.00 8.41  ? 2009 SER A CA    1 
ATOM   4384  C C     . SER A 1 2009 ? 222.344 208.126 245.107 1.00 8.01  ? 2009 SER A C     1 
ATOM   4385  O O     . SER A 1 2009 ? 221.581 208.103 244.139 1.00 9.17  ? 2009 SER A O     1 
ATOM   4386  C CB    . SER A 1 2009 ? 224.197 209.756 244.734 1.00 8.12  ? 2009 SER A CB    1 
ATOM   4387  O OG    . SER A 1 2009 ? 223.445 210.335 243.685 1.00 10.28 ? 2009 SER A OG    1 
ATOM   4388  N N     . PRO A 1 2010 ? 221.893 208.015 246.360 1.00 2.59  ? 2010 PRO A N     1 
ATOM   4389  C CA    . PRO A 1 2010 ? 220.448 207.905 246.612 1.00 1.11  ? 2010 PRO A CA    1 
ATOM   4390  C C     . PRO A 1 2010 ? 219.665 209.148 246.234 1.00 6.23  ? 2010 PRO A C     1 
ATOM   4391  O O     . PRO A 1 2010 ? 218.443 209.062 246.065 1.00 9.92  ? 2010 PRO A O     1 
ATOM   4392  C CB    . PRO A 1 2010 ? 220.377 207.641 248.121 1.00 4.12  ? 2010 PRO A CB    1 
ATOM   4393  C CG    . PRO A 1 2010 ? 221.637 208.230 248.660 1.00 4.87  ? 2010 PRO A CG    1 
ATOM   4394  C CD    . PRO A 1 2010 ? 222.677 208.008 247.605 1.00 5.50  ? 2010 PRO A CD    1 
ATOM   4395  N N     . ASP A 1 2011 ? 220.326 210.298 246.095 1.00 4.42  ? 2011 ASP A N     1 
ATOM   4396  C CA    . ASP A 1 2011 ? 219.626 211.548 245.825 1.00 2.88  ? 2011 ASP A CA    1 
ATOM   4397  C C     . ASP A 1 2011 ? 219.112 211.641 244.394 1.00 1.89  ? 2011 ASP A C     1 
ATOM   4398  O O     . ASP A 1 2011 ? 218.212 212.443 244.126 1.00 0.26  ? 2011 ASP A O     1 
ATOM   4399  C CB    . ASP A 1 2011 ? 220.552 212.727 246.115 1.00 5.77  ? 2011 ASP A CB    1 
ATOM   4400  C CG    . ASP A 1 2011 ? 220.922 212.828 247.578 1.00 9.85  ? 2011 ASP A CG    1 
ATOM   4401  O OD1   . ASP A 1 2011 ? 220.108 212.409 248.426 1.00 7.81  ? 2011 ASP A OD1   1 
ATOM   4402  O OD2   . ASP A 1 2011 ? 222.031 213.319 247.879 1.00 10.58 ? 2011 ASP A OD2   1 
ATOM   4403  N N     . MET A 1 2012 ? 219.659 210.851 243.474 1.00 2.91  ? 2012 MET A N     1 
ATOM   4404  C CA    . MET A 1 2012 ? 219.309 210.989 242.071 1.00 1.69  ? 2012 MET A CA    1 
ATOM   4405  C C     . MET A 1 2012 ? 217.945 210.362 241.791 1.00 0.43  ? 2012 MET A C     1 
ATOM   4406  O O     . MET A 1 2012 ? 217.407 209.585 242.584 1.00 0.41  ? 2012 MET A O     1 
ATOM   4407  C CB    . MET A 1 2012 ? 220.374 210.345 241.187 1.00 0.00  ? 2012 MET A CB    1 
ATOM   4408  C CG    . MET A 1 2012 ? 220.377 208.834 241.226 1.00 0.67  ? 2012 MET A CG    1 
ATOM   4409  S SD    . MET A 1 2012 ? 220.811 208.135 239.627 1.00 13.98 ? 2012 MET A SD    1 
ATOM   4410  C CE    . MET A 1 2012 ? 219.326 208.498 238.698 1.00 3.42  ? 2012 MET A CE    1 
ATOM   4411  N N     . ALA A 1 2013 ? 217.386 210.711 240.636 1.00 0.00  ? 2013 ALA A N     1 
ATOM   4412  C CA    . ALA A 1 2013 ? 216.097 210.179 240.220 1.00 0.00  ? 2013 ALA A CA    1 
ATOM   4413  C C     . ALA A 1 2013 ? 216.008 210.226 238.704 1.00 2.05  ? 2013 ALA A C     1 
ATOM   4414  O O     . ALA A 1 2013 ? 216.776 210.925 238.040 1.00 5.55  ? 2013 ALA A O     1 
ATOM   4415  C CB    . ALA A 1 2013 ? 214.937 210.954 240.847 1.00 0.00  ? 2013 ALA A CB    1 
ATOM   4416  N N     . ILE A 1 2014 ? 215.064 209.458 238.167 1.00 4.67  ? 2014 ILE A N     1 
ATOM   4417  C CA    . ILE A 1 2014 ? 214.785 209.425 236.736 1.00 2.67  ? 2014 ILE A CA    1 
ATOM   4418  C C     . ILE A 1 2014 ? 213.278 209.483 236.548 1.00 0.34  ? 2014 ILE A C     1 
ATOM   4419  O O     . ILE A 1 2014 ? 212.538 208.749 237.211 1.00 1.23  ? 2014 ILE A O     1 
ATOM   4420  C CB    . ILE A 1 2014 ? 215.365 208.166 236.062 1.00 1.73  ? 2014 ILE A CB    1 
ATOM   4421  C CG1   . ILE A 1 2014 ? 216.885 208.251 235.984 1.00 1.97  ? 2014 ILE A CG1   1 
ATOM   4422  C CG2   . ILE A 1 2014 ? 214.798 207.990 234.666 1.00 0.76  ? 2014 ILE A CG2   1 
ATOM   4423  C CD1   . ILE A 1 2014 ? 217.518 206.991 235.474 1.00 3.29  ? 2014 ILE A CD1   1 
ATOM   4424  N N     . PHE A 1 2015 ? 212.822 210.351 235.650 1.00 0.06  ? 2015 PHE A N     1 
ATOM   4425  C CA    . PHE A 1 2015 ? 211.405 210.510 235.363 1.00 0.00  ? 2015 PHE A CA    1 
ATOM   4426  C C     . PHE A 1 2015 ? 211.160 210.298 233.878 1.00 0.00  ? 2015 PHE A C     1 
ATOM   4427  O O     . PHE A 1 2015 ? 211.897 210.820 233.036 1.00 4.36  ? 2015 PHE A O     1 
ATOM   4428  C CB    . PHE A 1 2015 ? 210.911 211.889 235.801 1.00 1.44  ? 2015 PHE A CB    1 
ATOM   4429  C CG    . PHE A 1 2015 ? 210.790 212.036 237.289 1.00 3.31  ? 2015 PHE A CG    1 
ATOM   4430  C CD1   . PHE A 1 2015 ? 211.915 212.243 238.068 1.00 0.00  ? 2015 PHE A CD1   1 
ATOM   4431  C CD2   . PHE A 1 2015 ? 209.558 211.956 237.910 1.00 0.87  ? 2015 PHE A CD2   1 
ATOM   4432  C CE1   . PHE A 1 2015 ? 211.812 212.369 239.434 1.00 0.87  ? 2015 PHE A CE1   1 
ATOM   4433  C CE2   . PHE A 1 2015 ? 209.450 212.083 239.277 1.00 0.00  ? 2015 PHE A CE2   1 
ATOM   4434  C CZ    . PHE A 1 2015 ? 210.576 212.291 240.039 1.00 3.64  ? 2015 PHE A CZ    1 
ATOM   4435  N N     . ILE A 1 2016 ? 210.122 209.529 233.564 1.00 0.00  ? 2016 ILE A N     1 
ATOM   4436  C CA    . ILE A 1 2016 ? 209.820 209.112 232.194 1.00 0.53  ? 2016 ILE A CA    1 
ATOM   4437  C C     . ILE A 1 2016 ? 208.435 209.660 231.862 1.00 0.03  ? 2016 ILE A C     1 
ATOM   4438  O O     . ILE A 1 2016 ? 207.415 209.024 232.141 1.00 11.15 ? 2016 ILE A O     1 
ATOM   4439  C CB    . ILE A 1 2016 ? 209.867 207.590 232.019 1.00 4.87  ? 2016 ILE A CB    1 
ATOM   4440  C CG1   . ILE A 1 2016 ? 211.253 207.038 232.358 1.00 2.74  ? 2016 ILE A CG1   1 
ATOM   4441  C CG2   . ILE A 1 2016 ? 209.460 207.194 230.618 1.00 6.58  ? 2016 ILE A CG2   1 
ATOM   4442  C CD1   . ILE A 1 2016 ? 212.348 207.559 231.476 1.00 3.93  ? 2016 ILE A CD1   1 
ATOM   4443  N N     . THR A 1 2017 ? 208.388 210.842 231.260 1.00 0.00  ? 2017 THR A N     1 
ATOM   4444  C CA    . THR A 1 2017 ? 207.119 211.396 230.819 1.00 0.84  ? 2017 THR A CA    1 
ATOM   4445  C C     . THR A 1 2017 ? 206.751 210.836 229.451 1.00 2.15  ? 2017 THR A C     1 
ATOM   4446  O O     . THR A 1 2017 ? 207.606 210.652 228.581 1.00 8.39  ? 2017 THR A O     1 
ATOM   4447  C CB    . THR A 1 2017 ? 207.183 212.921 230.766 1.00 3.00  ? 2017 THR A CB    1 
ATOM   4448  O OG1   . THR A 1 2017 ? 208.005 213.327 229.666 1.00 16.53 ? 2017 THR A OG1   1 
ATOM   4449  C CG2   . THR A 1 2017 ? 207.780 213.466 232.049 1.00 0.00  ? 2017 THR A CG2   1 
ATOM   4450  N N     . MET A 1 2018 ? 205.462 210.564 229.262 1.00 0.00  ? 2018 MET A N     1 
ATOM   4451  C CA    . MET A 1 2018 ? 204.992 209.907 228.050 1.00 2.07  ? 2018 MET A CA    1 
ATOM   4452  C C     . MET A 1 2018 ? 203.815 210.687 227.482 1.00 2.61  ? 2018 MET A C     1 
ATOM   4453  O O     . MET A 1 2018 ? 203.488 211.785 227.940 1.00 7.90  ? 2018 MET A O     1 
ATOM   4454  C CB    . MET A 1 2018 ? 204.612 208.449 228.328 1.00 2.49  ? 2018 MET A CB    1 
ATOM   4455  C CG    . MET A 1 2018 ? 205.773 207.565 228.698 1.00 3.64  ? 2018 MET A CG    1 
ATOM   4456  S SD    . MET A 1 2018 ? 205.173 205.920 229.071 1.00 23.83 ? 2018 MET A SD    1 
ATOM   4457  C CE    . MET A 1 2018 ? 204.699 205.389 227.430 1.00 9.14  ? 2018 MET A CE    1 
ATOM   4458  N N     . ASN A 1 2019 ? 203.176 210.108 226.472 1.00 2.12  ? 2019 ASN A N     1 
ATOM   4459  C CA    . ASN A 1 2019 ? 202.048 210.737 225.801 1.00 1.25  ? 2019 ASN A CA    1 
ATOM   4460  C C     . ASN A 1 2019 ? 200.881 209.760 225.697 1.00 2.03  ? 2019 ASN A C     1 
ATOM   4461  O O     . ASN A 1 2019 ? 199.714 210.146 225.731 0.00 4.98  ? 2019 ASN A O     1 
ATOM   4462  C CB    . ASN A 1 2019 ? 202.462 211.223 224.411 1.00 0.00  ? 2019 ASN A CB    1 
ATOM   4463  C CG    . ASN A 1 2019 ? 201.690 212.447 223.967 1.00 0.00  ? 2019 ASN A CG    1 
ATOM   4464  O OD1   . ASN A 1 2019 ? 201.170 213.197 224.786 1.00 0.15  ? 2019 ASN A OD1   1 
ATOM   4465  N ND2   . ASN A 1 2019 ? 201.620 212.659 222.660 1.00 10.51 ? 2019 ASN A ND2   1 
ATOM   4466  N N     . LEU A 1 2028 ? 204.514 202.175 228.101 1.00 0.00  ? 2028 LEU A N     1 
ATOM   4467  C CA    . LEU A 1 2028 ? 205.916 202.179 228.505 1.00 6.82  ? 2028 LEU A CA    1 
ATOM   4468  C C     . LEU A 1 2028 ? 206.519 200.788 228.350 1.00 14.23 ? 2028 LEU A C     1 
ATOM   4469  O O     . LEU A 1 2028 ? 205.803 199.790 228.427 1.00 19.71 ? 2028 LEU A O     1 
ATOM   4470  C CB    . LEU A 1 2028 ? 206.064 202.678 229.947 1.00 5.77  ? 2028 LEU A CB    1 
ATOM   4471  C CG    . LEU A 1 2028 ? 205.640 201.810 231.130 1.00 7.19  ? 2028 LEU A CG    1 
ATOM   4472  C CD1   . LEU A 1 2028 ? 206.251 202.367 232.405 1.00 8.15  ? 2028 LEU A CD1   1 
ATOM   4473  C CD2   . LEU A 1 2028 ? 204.125 201.741 231.254 1.00 5.90  ? 2028 LEU A CD2   1 
ATOM   4474  N N     . PRO A 1 2029 ? 207.830 200.721 228.115 1.00 13.75 ? 2029 PRO A N     1 
ATOM   4475  C CA    . PRO A 1 2029 ? 208.467 199.420 227.886 1.00 13.59 ? 2029 PRO A CA    1 
ATOM   4476  C C     . PRO A 1 2029 ? 208.321 198.499 229.086 1.00 10.33 ? 2029 PRO A C     1 
ATOM   4477  O O     . PRO A 1 2029 ? 208.288 198.936 230.238 1.00 7.78  ? 2029 PRO A O     1 
ATOM   4478  C CB    . PRO A 1 2029 ? 209.935 199.781 227.629 1.00 11.44 ? 2029 PRO A CB    1 
ATOM   4479  C CG    . PRO A 1 2029 ? 210.103 201.144 228.202 1.00 10.74 ? 2029 PRO A CG    1 
ATOM   4480  C CD    . PRO A 1 2029 ? 208.794 201.828 228.000 1.00 9.74  ? 2029 PRO A CD    1 
ATOM   4481  N N     . ASP A 1 2030 ? 208.229 197.201 228.794 1.00 12.39 ? 2030 ASP A N     1 
ATOM   4482  C CA    . ASP A 1 2030 ? 208.056 196.185 229.823 1.00 10.91 ? 2030 ASP A CA    1 
ATOM   4483  C C     . ASP A 1 2030 ? 209.237 196.100 230.780 1.00 8.55  ? 2030 ASP A C     1 
ATOM   4484  O O     . ASP A 1 2030 ? 209.093 195.518 231.860 1.00 17.72 ? 2030 ASP A O     1 
ATOM   4485  C CB    . ASP A 1 2030 ? 207.810 194.826 229.165 1.00 15.64 ? 2030 ASP A CB    1 
ATOM   4486  C CG    . ASP A 1 2030 ? 208.894 194.454 228.170 1.00 21.44 ? 2030 ASP A CG    1 
ATOM   4487  O OD1   . ASP A 1 2030 ? 209.800 195.280 227.934 1.00 19.88 ? 2030 ASP A OD1   1 
ATOM   4488  O OD2   . ASP A 1 2030 ? 208.835 193.336 227.615 1.00 23.17 ? 2030 ASP A OD2   1 
ATOM   4489  N N     . ASN A 1 2031 ? 210.394 196.655 230.413 1.00 5.19  ? 2031 ASN A N     1 
ATOM   4490  C CA    . ASN A 1 2031 ? 211.509 196.719 231.351 1.00 7.19  ? 2031 ASN A CA    1 
ATOM   4491  C C     . ASN A 1 2031 ? 211.161 197.576 232.560 1.00 11.70 ? 2031 ASN A C     1 
ATOM   4492  O O     . ASN A 1 2031 ? 211.495 197.225 233.698 1.00 14.10 ? 2031 ASN A O     1 
ATOM   4493  C CB    . ASN A 1 2031 ? 212.752 197.277 230.658 1.00 7.98  ? 2031 ASN A CB    1 
ATOM   4494  C CG    . ASN A 1 2031 ? 213.281 196.361 229.583 1.00 16.34 ? 2031 ASN A CG    1 
ATOM   4495  O OD1   . ASN A 1 2031 ? 213.136 196.636 228.392 1.00 15.74 ? 2031 ASN A OD1   1 
ATOM   4496  N ND2   . ASN A 1 2031 ? 213.904 195.264 229.994 1.00 22.41 ? 2031 ASN A ND2   1 
ATOM   4497  N N     . LEU A 1 2032 ? 210.489 198.701 232.332 1.00 9.38  ? 2032 LEU A N     1 
ATOM   4498  C CA    . LEU A 1 2032 ? 210.291 199.719 233.351 1.00 4.78  ? 2032 LEU A CA    1 
ATOM   4499  C C     . LEU A 1 2032 ? 208.883 199.738 233.926 1.00 3.42  ? 2032 LEU A C     1 
ATOM   4500  O O     . LEU A 1 2032 ? 208.568 200.631 234.717 1.00 10.58 ? 2032 LEU A O     1 
ATOM   4501  C CB    . LEU A 1 2032 ? 210.624 201.096 232.775 1.00 7.11  ? 2032 LEU A CB    1 
ATOM   4502  C CG    . LEU A 1 2032 ? 211.882 201.136 231.909 1.00 3.09  ? 2032 LEU A CG    1 
ATOM   4503  C CD1   . LEU A 1 2032 ? 211.921 202.402 231.074 1.00 4.79  ? 2032 LEU A CD1   1 
ATOM   4504  C CD2   . LEU A 1 2032 ? 213.120 201.006 232.764 1.00 4.61  ? 2032 LEU A CD2   1 
ATOM   4505  N N     . LYS A 1 2033 ? 208.027 198.788 233.548 1.00 2.29  ? 2033 LYS A N     1 
ATOM   4506  C CA    . LYS A 1 2033 ? 206.665 198.779 234.071 1.00 2.06  ? 2033 LYS A CA    1 
ATOM   4507  C C     . LYS A 1 2033 ? 206.639 198.531 235.572 1.00 7.66  ? 2033 LYS A C     1 
ATOM   4508  O O     . LYS A 1 2033 ? 205.827 199.129 236.286 1.00 14.97 ? 2033 LYS A O     1 
ATOM   4509  C CB    . LYS A 1 2033 ? 205.829 197.727 233.344 1.00 2.22  ? 2033 LYS A CB    1 
ATOM   4510  C CG    . LYS A 1 2033 ? 205.183 198.229 232.066 1.00 4.46  ? 2033 LYS A CG    1 
ATOM   4511  C CD    . LYS A 1 2033 ? 204.210 197.209 231.508 1.00 8.61  ? 2033 LYS A CD    1 
ATOM   4512  C CE    . LYS A 1 2033 ? 203.683 197.633 230.148 1.00 8.94  ? 2033 LYS A CE    1 
ATOM   4513  N NZ    . LYS A 1 2033 ? 202.790 198.818 230.248 1.00 9.59  ? 2033 LYS A NZ    1 
ATOM   4514  N N     . LYS A 1 2034 ? 207.515 197.660 236.069 1.00 9.04  ? 2034 LYS A N     1 
ATOM   4515  C CA    . LYS A 1 2034 ? 207.553 197.317 237.483 1.00 3.57  ? 2034 LYS A CA    1 
ATOM   4516  C C     . LYS A 1 2034 ? 208.356 198.303 238.322 1.00 3.33  ? 2034 LYS A C     1 
ATOM   4517  O O     . LYS A 1 2034 ? 208.286 198.240 239.553 1.00 8.21  ? 2034 LYS A O     1 
ATOM   4518  C CB    . LYS A 1 2034 ? 208.144 195.917 237.668 1.00 6.46  ? 2034 LYS A CB    1 
ATOM   4519  C CG    . LYS A 1 2034 ? 209.598 195.813 237.233 1.00 7.85  ? 2034 LYS A CG    1 
ATOM   4520  C CD    . LYS A 1 2034 ? 210.135 194.400 237.376 1.00 9.04  ? 2034 LYS A CD    1 
ATOM   4521  C CE    . LYS A 1 2034 ? 211.598 194.326 236.962 1.00 9.72  ? 2034 LYS A CE    1 
ATOM   4522  N NZ    . LYS A 1 2034 ? 211.783 194.570 235.505 1.00 8.63  ? 2034 LYS A NZ    1 
ATOM   4523  N N     . LEU A 1 2035 ? 209.114 199.204 237.695 1.00 6.81  ? 2035 LEU A N     1 
ATOM   4524  C CA    . LEU A 1 2035 ? 210.001 200.108 238.417 1.00 2.67  ? 2035 LEU A CA    1 
ATOM   4525  C C     . LEU A 1 2035 ? 209.603 201.572 238.298 1.00 2.58  ? 2035 LEU A C     1 
ATOM   4526  O O     . LEU A 1 2035 ? 210.399 202.444 238.664 1.00 10.51 ? 2035 LEU A O     1 
ATOM   4527  C CB    . LEU A 1 2035 ? 211.445 199.939 237.936 1.00 1.03  ? 2035 LEU A CB    1 
ATOM   4528  C CG    . LEU A 1 2035 ? 211.989 198.523 237.769 1.00 7.08  ? 2035 LEU A CG    1 
ATOM   4529  C CD1   . LEU A 1 2035 ? 213.184 198.531 236.837 1.00 3.93  ? 2035 LEU A CD1   1 
ATOM   4530  C CD2   . LEU A 1 2035 ? 212.367 197.948 239.119 1.00 8.55  ? 2035 LEU A CD2   1 
ATOM   4531  N N     . PHE A 1 2036 ? 208.406 201.876 237.802 1.00 1.34  ? 2036 PHE A N     1 
ATOM   4532  C CA    . PHE A 1 2036 ? 208.008 203.262 237.601 1.00 0.00  ? 2036 PHE A CA    1 
ATOM   4533  C C     . PHE A 1 2036 ? 206.552 203.448 237.990 1.00 0.00  ? 2036 PHE A C     1 
ATOM   4534  O O     . PHE A 1 2036 ? 205.686 202.696 237.536 1.00 6.68  ? 2036 PHE A O     1 
ATOM   4535  C CB    . PHE A 1 2036 ? 208.222 203.691 236.146 1.00 0.00  ? 2036 PHE A CB    1 
ATOM   4536  C CG    . PHE A 1 2036 ? 209.597 204.221 235.871 1.00 0.00  ? 2036 PHE A CG    1 
ATOM   4537  C CD1   . PHE A 1 2036 ? 210.636 203.363 235.572 1.00 2.13  ? 2036 PHE A CD1   1 
ATOM   4538  C CD2   . PHE A 1 2036 ? 209.852 205.577 235.925 1.00 0.29  ? 2036 PHE A CD2   1 
ATOM   4539  C CE1   . PHE A 1 2036 ? 211.903 203.849 235.327 1.00 2.87  ? 2036 PHE A CE1   1 
ATOM   4540  C CE2   . PHE A 1 2036 ? 211.118 206.068 235.684 1.00 0.57  ? 2036 PHE A CE2   1 
ATOM   4541  C CZ    . PHE A 1 2036 ? 212.143 205.203 235.383 1.00 0.00  ? 2036 PHE A CZ    1 
ATOM   4542  N N     . ARG A 1 2037 ? 206.290 204.447 238.827 1.00 0.00  ? 2037 ARG A N     1 
ATOM   4543  C CA    . ARG A 1 2037 ? 204.924 204.843 239.126 1.00 0.00  ? 2037 ARG A CA    1 
ATOM   4544  C C     . ARG A 1 2037 ? 204.428 205.830 238.079 1.00 1.12  ? 2037 ARG A C     1 
ATOM   4545  O O     . ARG A 1 2037 ? 205.157 206.725 237.646 1.00 12.68 ? 2037 ARG A O     1 
ATOM   4546  C CB    . ARG A 1 2037 ? 204.828 205.475 240.514 1.00 0.00  ? 2037 ARG A CB    1 
ATOM   4547  C CG    . ARG A 1 2037 ? 205.185 204.552 241.663 1.00 4.87  ? 2037 ARG A CG    1 
ATOM   4548  C CD    . ARG A 1 2037 ? 204.397 203.255 241.623 1.00 12.73 ? 2037 ARG A CD    1 
ATOM   4549  N NE    . ARG A 1 2037 ? 202.956 203.459 241.549 1.00 8.32  ? 2037 ARG A NE    1 
ATOM   4550  C CZ    . ARG A 1 2037 ? 202.099 202.539 241.129 1.00 7.57  ? 2037 ARG A CZ    1 
ATOM   4551  N NH1   . ARG A 1 2037 ? 202.503 201.334 240.763 1.00 6.66  ? 2037 ARG A NH1   1 
ATOM   4552  N NH2   . ARG A 1 2037 ? 200.805 202.836 241.070 1.00 10.96 ? 2037 ARG A NH2   1 
ATOM   4553  N N     . SER A 1 2038 ? 203.174 205.666 237.677 1.00 0.00  ? 2038 SER A N     1 
ATOM   4554  C CA    . SER A 1 2038 ? 202.583 206.482 236.630 1.00 0.00  ? 2038 SER A CA    1 
ATOM   4555  C C     . SER A 1 2038 ? 201.545 207.425 237.219 1.00 5.10  ? 2038 SER A C     1 
ATOM   4556  O O     . SER A 1 2038 ? 200.829 207.077 238.163 1.00 18.61 ? 2038 SER A O     1 
ATOM   4557  C CB    . SER A 1 2038 ? 201.934 205.614 235.548 1.00 0.00  ? 2038 SER A CB    1 
ATOM   4558  O OG    . SER A 1 2038 ? 202.906 204.856 234.852 1.00 6.59  ? 2038 SER A OG    1 
ATOM   4559  N N     . LEU A 1 2039 ? 201.473 208.627 236.657 1.00 0.55  ? 2039 LEU A N     1 
ATOM   4560  C CA    . LEU A 1 2039 ? 200.454 209.596 237.024 1.00 0.00  ? 2039 LEU A CA    1 
ATOM   4561  C C     . LEU A 1 2039 ? 199.794 210.143 235.770 1.00 2.99  ? 2039 LEU A C     1 
ATOM   4562  O O     . LEU A 1 2039 ? 200.475 210.496 234.804 1.00 15.21 ? 2039 LEU A O     1 
ATOM   4563  C CB    . LEU A 1 2039 ? 201.028 210.748 237.839 1.00 1.03  ? 2039 LEU A CB    1 
ATOM   4564  C CG    . LEU A 1 2039 ? 199.924 211.703 238.289 1.00 2.82  ? 2039 LEU A CG    1 
ATOM   4565  C CD1   . LEU A 1 2039 ? 199.365 211.279 239.627 1.00 3.90  ? 2039 LEU A CD1   1 
ATOM   4566  C CD2   . LEU A 1 2039 ? 200.423 213.122 238.331 1.00 1.81  ? 2039 LEU A CD2   1 
ATOM   4567  N N     . ALA A 1 2040 ? 198.468 210.224 235.794 1.00 1.36  ? 2040 ALA A N     1 
ATOM   4568  C CA    . ALA A 1 2040 ? 197.692 210.728 234.665 1.00 0.80  ? 2040 ALA A CA    1 
ATOM   4569  C C     . ALA A 1 2040 ? 197.616 212.246 234.778 1.00 2.40  ? 2040 ALA A C     1 
ATOM   4570  O O     . ALA A 1 2040 ? 196.847 212.794 235.568 1.00 6.68  ? 2040 ALA A O     1 
ATOM   4571  C CB    . ALA A 1 2040 ? 196.307 210.098 234.631 1.00 5.92  ? 2040 ALA A CB    1 
ATOM   4572  N N     . MET A 1 2041 ? 198.434 212.928 233.978 1.00 0.00  ? 2041 MET A N     1 
ATOM   4573  C CA    . MET A 1 2041 ? 198.370 214.383 233.850 1.00 1.48  ? 2041 MET A CA    1 
ATOM   4574  C C     . MET A 1 2041 ? 197.580 214.698 232.584 1.00 4.97  ? 2041 MET A C     1 
ATOM   4575  O O     . MET A 1 2041 ? 198.127 215.017 231.528 1.00 11.10 ? 2041 MET A O     1 
ATOM   4576  C CB    . MET A 1 2041 ? 199.770 214.982 233.810 1.00 0.32  ? 2041 MET A CB    1 
ATOM   4577  C CG    . MET A 1 2041 ? 200.613 214.673 235.032 1.00 1.23  ? 2041 MET A CG    1 
ATOM   4578  S SD    . MET A 1 2041 ? 201.705 216.028 235.493 1.00 5.21  ? 2041 MET A SD    1 
ATOM   4579  C CE    . MET A 1 2041 ? 200.520 217.257 236.025 1.00 0.90  ? 2041 MET A CE    1 
ATOM   4580  N N     . THR A 1 2042 ? 196.257 214.593 232.699 1.00 0.80  ? 2042 THR A N     1 
ATOM   4581  C CA    . THR A 1 2042 ? 195.404 214.698 231.519 1.00 1.46  ? 2042 THR A CA    1 
ATOM   4582  C C     . THR A 1 2042 ? 195.070 216.150 231.195 1.00 1.98  ? 2042 THR A C     1 
ATOM   4583  O O     . THR A 1 2042 ? 195.335 216.625 230.087 1.00 6.67  ? 2042 THR A O     1 
ATOM   4584  C CB    . THR A 1 2042 ? 194.127 213.882 231.724 1.00 5.45  ? 2042 THR A CB    1 
ATOM   4585  O OG1   . THR A 1 2042 ? 194.469 212.508 231.938 1.00 8.43  ? 2042 THR A OG1   1 
ATOM   4586  C CG2   . THR A 1 2042 ? 193.231 213.985 230.503 1.00 4.22  ? 2042 THR A CG2   1 
ATOM   4587  N N     . LYS A 1 2043 ? 194.481 216.868 232.149 1.00 2.56  ? 2043 LYS A N     1 
ATOM   4588  C CA    . LYS A 1 2043 ? 194.084 218.250 231.935 1.00 5.91  ? 2043 LYS A CA    1 
ATOM   4589  C C     . LYS A 1 2043 ? 194.479 219.093 233.142 1.00 4.42  ? 2043 LYS A C     1 
ATOM   4590  O O     . LYS A 1 2043 ? 194.095 218.767 234.279 1.00 4.11  ? 2043 LYS A O     1 
ATOM   4591  C CB    . LYS A 1 2043 ? 192.573 218.347 231.671 1.00 5.47  ? 2043 LYS A CB    1 
ATOM   4592  C CG    . LYS A 1 2043 ? 191.702 217.695 232.734 1.00 3.44  ? 2043 LYS A CG    1 
ATOM   4593  C CD    . LYS A 1 2043 ? 190.264 217.558 232.269 1.00 10.07 ? 2043 LYS A CD    1 
ATOM   4594  C CE    . LYS A 1 2043 ? 190.031 216.218 231.590 1.00 9.96  ? 2043 LYS A CE    1 
ATOM   4595  N NZ    . LYS A 1 2043 ? 190.244 215.078 232.525 1.00 6.71  ? 2043 LYS A NZ    1 
ATOM   4596  N N     . PRO A 1 2044 ? 195.244 220.161 232.951 1.00 4.78  ? 2044 PRO A N     1 
ATOM   4597  C CA    . PRO A 1 2044 ? 195.580 221.040 234.073 1.00 4.55  ? 2044 PRO A CA    1 
ATOM   4598  C C     . PRO A 1 2044 ? 194.441 221.995 234.393 1.00 4.12  ? 2044 PRO A C     1 
ATOM   4599  O O     . PRO A 1 2044 ? 193.520 222.204 233.602 1.00 10.39 ? 2044 PRO A O     1 
ATOM   4600  C CB    . PRO A 1 2044 ? 196.812 221.796 233.568 1.00 4.12  ? 2044 PRO A CB    1 
ATOM   4601  C CG    . PRO A 1 2044 ? 196.625 221.850 232.095 1.00 2.65  ? 2044 PRO A CG    1 
ATOM   4602  C CD    . PRO A 1 2044 ? 195.892 220.591 231.699 1.00 3.12  ? 2044 PRO A CD    1 
ATOM   4603  N N     . ASP A 1 2045 ? 194.515 222.574 235.588 1.00 4.20  ? 2045 ASP A N     1 
ATOM   4604  C CA    . ASP A 1 2045 ? 193.540 223.576 236.015 1.00 5.07  ? 2045 ASP A CA    1 
ATOM   4605  C C     . ASP A 1 2045 ? 193.961 224.911 235.420 1.00 4.61  ? 2045 ASP A C     1 
ATOM   4606  O O     . ASP A 1 2045 ? 194.725 225.672 236.013 1.00 1.55  ? 2045 ASP A O     1 
ATOM   4607  C CB    . ASP A 1 2045 ? 193.447 223.638 237.534 1.00 7.20  ? 2045 ASP A CB    1 
ATOM   4608  C CG    . ASP A 1 2045 ? 192.064 224.037 238.016 1.00 10.75 ? 2045 ASP A CG    1 
ATOM   4609  O OD1   . ASP A 1 2045 ? 191.233 224.444 237.176 1.00 16.15 ? 2045 ASP A OD1   1 
ATOM   4610  O OD2   . ASP A 1 2045 ? 191.804 223.943 239.234 1.00 10.89 ? 2045 ASP A OD2   1 
ATOM   4611  N N     . ARG A 1 2046 ? 193.457 225.192 234.216 1.00 11.60 ? 2046 ARG A N     1 
ATOM   4612  C CA    . ARG A 1 2046 ? 193.817 226.429 233.535 1.00 6.17  ? 2046 ARG A CA    1 
ATOM   4613  C C     . ARG A 1 2046 ? 193.211 227.648 234.211 1.00 6.85  ? 2046 ARG A C     1 
ATOM   4614  O O     . ARG A 1 2046 ? 193.834 228.714 234.226 1.00 5.76  ? 2046 ARG A O     1 
ATOM   4615  C CB    . ARG A 1 2046 ? 193.390 226.371 232.070 1.00 15.85 ? 2046 ARG A CB    1 
ATOM   4616  C CG    . ARG A 1 2046 ? 194.297 225.532 231.195 1.00 15.71 ? 2046 ARG A CG    1 
ATOM   4617  C CD    . ARG A 1 2046 ? 193.513 224.743 230.168 1.00 14.70 ? 2046 ARG A CD    1 
ATOM   4618  N NE    . ARG A 1 2046 ? 194.353 223.766 229.488 1.00 17.55 ? 2046 ARG A NE    1 
ATOM   4619  C CZ    . ARG A 1 2046 ? 194.893 223.951 228.291 1.00 15.59 ? 2046 ARG A CZ    1 
ATOM   4620  N NH1   . ARG A 1 2046 ? 194.699 225.069 227.611 1.00 10.99 ? 2046 ARG A NH1   1 
ATOM   4621  N NH2   . ARG A 1 2046 ? 195.652 222.994 227.766 1.00 14.78 ? 2046 ARG A NH2   1 
ATOM   4622  N N     . GLN A 1 2047 ? 192.003 227.521 234.763 1.00 9.07  ? 2047 GLN A N     1 
ATOM   4623  C CA    . GLN A 1 2047 ? 191.387 228.655 235.443 1.00 2.29  ? 2047 GLN A CA    1 
ATOM   4624  C C     . GLN A 1 2047 ? 192.204 229.066 236.660 1.00 10.28 ? 2047 GLN A C     1 
ATOM   4625  O O     . GLN A 1 2047 ? 192.427 230.257 236.896 1.00 13.47 ? 2047 GLN A O     1 
ATOM   4626  C CB    . GLN A 1 2047 ? 189.950 228.318 235.843 1.00 8.73  ? 2047 GLN A CB    1 
ATOM   4627  C CG    . GLN A 1 2047 ? 189.220 229.455 236.552 1.00 16.16 ? 2047 GLN A CG    1 
ATOM   4628  C CD    . GLN A 1 2047 ? 189.412 229.442 238.059 1.00 18.73 ? 2047 GLN A CD    1 
ATOM   4629  O OE1   . GLN A 1 2047 ? 189.763 228.419 238.643 1.00 24.88 ? 2047 GLN A OE1   1 
ATOM   4630  N NE2   . GLN A 1 2047 ? 189.186 230.586 238.693 1.00 7.12  ? 2047 GLN A NE2   1 
ATOM   4631  N N     . LEU A 1 2048 ? 192.665 228.088 237.444 1.00 10.12 ? 2048 LEU A N     1 
ATOM   4632  C CA    . LEU A 1 2048 ? 193.451 228.401 238.633 1.00 0.55  ? 2048 LEU A CA    1 
ATOM   4633  C C     . LEU A 1 2048 ? 194.796 229.013 238.264 1.00 2.01  ? 2048 LEU A C     1 
ATOM   4634  O O     . LEU A 1 2048 ? 195.242 229.978 238.895 1.00 10.03 ? 2048 LEU A O     1 
ATOM   4635  C CB    . LEU A 1 2048 ? 193.649 227.147 239.482 1.00 2.87  ? 2048 LEU A CB    1 
ATOM   4636  C CG    . LEU A 1 2048 ? 194.284 227.396 240.851 1.00 3.48  ? 2048 LEU A CG    1 
ATOM   4637  C CD1   . LEU A 1 2048 ? 193.496 228.442 241.626 1.00 7.40  ? 2048 LEU A CD1   1 
ATOM   4638  C CD2   . LEU A 1 2048 ? 194.399 226.108 241.642 1.00 1.69  ? 2048 LEU A CD2   1 
ATOM   4639  N N     . ILE A 1 2049 ? 195.463 228.456 237.250 1.00 0.00  ? 2049 ILE A N     1 
ATOM   4640  C CA    . ILE A 1 2049 ? 196.741 229.007 236.808 1.00 0.00  ? 2049 ILE A CA    1 
ATOM   4641  C C     . ILE A 1 2049 ? 196.557 230.438 236.332 1.00 0.00  ? 2049 ILE A C     1 
ATOM   4642  O O     . ILE A 1 2049 ? 197.326 231.337 236.691 1.00 4.51  ? 2049 ILE A O     1 
ATOM   4643  C CB    . ILE A 1 2049 ? 197.352 228.129 235.701 1.00 0.82  ? 2049 ILE A CB    1 
ATOM   4644  C CG1   . ILE A 1 2049 ? 197.761 226.768 236.255 1.00 2.61  ? 2049 ILE A CG1   1 
ATOM   4645  C CG2   . ILE A 1 2049 ? 198.547 228.822 235.066 1.00 0.57  ? 2049 ILE A CG2   1 
ATOM   4646  C CD1   . ILE A 1 2049 ? 197.978 225.727 235.193 1.00 5.92  ? 2049 ILE A CD1   1 
ATOM   4647  N N     . ALA A 1 2050 ? 195.521 230.670 235.524 1.00 0.00  ? 2050 ALA A N     1 
ATOM   4648  C CA    . ALA A 1 2050 ? 195.259 232.007 235.011 1.00 0.00  ? 2050 ALA A CA    1 
ATOM   4649  C C     . ALA A 1 2050 ? 194.954 232.978 236.142 1.00 0.59  ? 2050 ALA A C     1 
ATOM   4650  O O     . ALA A 1 2050 ? 195.448 234.109 236.149 1.00 9.30  ? 2050 ALA A O     1 
ATOM   4651  C CB    . ALA A 1 2050 ? 194.108 231.963 234.005 1.00 0.00  ? 2050 ALA A CB    1 
ATOM   4652  N N     . GLN A 1 2051 ? 194.148 232.550 237.117 1.00 0.66  ? 2051 GLN A N     1 
ATOM   4653  C CA    . GLN A 1 2051 ? 193.797 233.427 238.227 1.00 0.00  ? 2051 GLN A CA    1 
ATOM   4654  C C     . GLN A 1 2051 ? 195.016 233.780 239.068 1.00 0.00  ? 2051 GLN A C     1 
ATOM   4655  O O     . GLN A 1 2051 ? 195.217 234.948 239.418 1.00 0.96  ? 2051 GLN A O     1 
ATOM   4656  C CB    . GLN A 1 2051 ? 192.725 232.769 239.092 1.00 0.37  ? 2051 GLN A CB    1 
ATOM   4657  C CG    . GLN A 1 2051 ? 192.259 233.626 240.247 1.00 0.00  ? 2051 GLN A CG    1 
ATOM   4658  C CD    . GLN A 1 2051 ? 191.348 232.875 241.190 1.00 1.55  ? 2051 GLN A CD    1 
ATOM   4659  O OE1   . GLN A 1 2051 ? 190.927 231.756 240.902 1.00 6.06  ? 2051 GLN A OE1   1 
ATOM   4660  N NE2   . GLN A 1 2051 ? 191.037 233.487 242.326 1.00 3.12  ? 2051 GLN A NE2   1 
ATOM   4661  N N     . VAL A 1 2052 ? 195.843 232.788 239.400 1.00 1.35  ? 2052 VAL A N     1 
ATOM   4662  C CA    . VAL A 1 2052 ? 197.018 233.059 240.220 1.00 0.00  ? 2052 VAL A CA    1 
ATOM   4663  C C     . VAL A 1 2052 ? 198.004 233.944 239.468 1.00 2.01  ? 2052 VAL A C     1 
ATOM   4664  O O     . VAL A 1 2052 ? 198.587 234.871 240.041 1.00 4.22  ? 2052 VAL A O     1 
ATOM   4665  C CB    . VAL A 1 2052 ? 197.667 231.742 240.682 1.00 0.00  ? 2052 VAL A CB    1 
ATOM   4666  C CG1   . VAL A 1 2052 ? 198.969 232.021 241.409 1.00 0.00  ? 2052 VAL A CG1   1 
ATOM   4667  C CG2   . VAL A 1 2052 ? 196.717 230.982 241.586 1.00 0.00  ? 2052 VAL A CG2   1 
ATOM   4668  N N     . MET A 1 2053 ? 198.196 233.688 238.172 1.00 1.34  ? 2053 MET A N     1 
ATOM   4669  C CA    . MET A 1 2053 ? 199.123 234.499 237.390 1.00 1.83  ? 2053 MET A CA    1 
ATOM   4670  C C     . MET A 1 2053 ? 198.620 235.931 237.241 1.00 2.03  ? 2053 MET A C     1 
ATOM   4671  O O     . MET A 1 2053 ? 199.403 236.883 237.338 1.00 5.14  ? 2053 MET A O     1 
ATOM   4672  C CB    . MET A 1 2053 ? 199.337 233.854 236.024 1.00 0.00  ? 2053 MET A CB    1 
ATOM   4673  C CG    . MET A 1 2053 ? 200.520 232.913 235.977 1.00 0.00  ? 2053 MET A CG    1 
ATOM   4674  S SD    . MET A 1 2053 ? 200.931 232.424 234.301 1.00 5.07  ? 2053 MET A SD    1 
ATOM   4675  C CE    . MET A 1 2053 ? 202.014 233.763 233.836 1.00 5.39  ? 2053 MET A CE    1 
ATOM   4676  N N     . LEU A 1 2054 ? 197.317 236.105 237.014 1.00 0.00  ? 2054 LEU A N     1 
ATOM   4677  C CA    . LEU A 1 2054 ? 196.757 237.445 236.904 1.00 0.00  ? 2054 LEU A CA    1 
ATOM   4678  C C     . LEU A 1 2054 ? 196.853 238.188 238.231 1.00 2.06  ? 2054 LEU A C     1 
ATOM   4679  O O     . LEU A 1 2054 ? 197.150 239.387 238.260 1.00 6.83  ? 2054 LEU A O     1 
ATOM   4680  C CB    . LEU A 1 2054 ? 195.306 237.364 236.434 1.00 0.00  ? 2054 LEU A CB    1 
ATOM   4681  C CG    . LEU A 1 2054 ? 195.088 237.195 234.929 1.00 0.00  ? 2054 LEU A CG    1 
ATOM   4682  C CD1   . LEU A 1 2054 ? 193.712 236.615 234.654 1.00 0.00  ? 2054 LEU A CD1   1 
ATOM   4683  C CD2   . LEU A 1 2054 ? 195.288 238.500 234.186 1.00 0.36  ? 2054 LEU A CD2   1 
ATOM   4684  N N     . TYR A 1 2055 ? 196.599 237.492 239.342 1.00 0.19  ? 2055 TYR A N     1 
ATOM   4685  C CA    . TYR A 1 2055 ? 196.723 238.115 240.653 1.00 1.01  ? 2055 TYR A CA    1 
ATOM   4686  C C     . TYR A 1 2055 ? 198.167 238.496 240.947 1.00 0.00  ? 2055 TYR A C     1 
ATOM   4687  O O     . TYR A 1 2055 ? 198.419 239.527 241.579 1.00 0.00  ? 2055 TYR A O     1 
ATOM   4688  C CB    . TYR A 1 2055 ? 196.173 237.171 241.727 1.00 0.59  ? 2055 TYR A CB    1 
ATOM   4689  C CG    . TYR A 1 2055 ? 196.098 237.759 243.120 1.00 1.01  ? 2055 TYR A CG    1 
ATOM   4690  C CD1   . TYR A 1 2055 ? 194.930 238.352 243.578 1.00 2.94  ? 2055 TYR A CD1   1 
ATOM   4691  C CD2   . TYR A 1 2055 ? 197.182 237.700 243.984 1.00 0.85  ? 2055 TYR A CD2   1 
ATOM   4692  C CE1   . TYR A 1 2055 ? 194.851 238.885 244.849 1.00 2.17  ? 2055 TYR A CE1   1 
ATOM   4693  C CE2   . TYR A 1 2055 ? 197.112 238.230 245.256 1.00 1.01  ? 2055 TYR A CE2   1 
ATOM   4694  C CZ    . TYR A 1 2055 ? 195.944 238.821 245.684 1.00 1.03  ? 2055 TYR A CZ    1 
ATOM   4695  O OH    . TYR A 1 2055 ? 195.869 239.350 246.952 1.00 2.60  ? 2055 TYR A OH    1 
ATOM   4696  N N     . SER A 1 2056 ? 199.125 237.684 240.496 1.00 0.00  ? 2056 SER A N     1 
ATOM   4697  C CA    . SER A 1 2056 ? 200.532 238.032 240.630 1.00 0.69  ? 2056 SER A CA    1 
ATOM   4698  C C     . SER A 1 2056 ? 200.954 239.131 239.667 1.00 3.42  ? 2056 SER A C     1 
ATOM   4699  O O     . SER A 1 2056 ? 202.012 239.737 239.865 1.00 3.11  ? 2056 SER A O     1 
ATOM   4700  C CB    . SER A 1 2056 ? 201.405 236.796 240.412 1.00 0.00  ? 2056 SER A CB    1 
ATOM   4701  O OG    . SER A 1 2056 ? 201.340 236.359 239.067 1.00 0.00  ? 2056 SER A OG    1 
ATOM   4702  N N     . GLN A 1 2057 ? 200.166 239.391 238.628 1.00 5.28  ? 2057 GLN A N     1 
ATOM   4703  C CA    . GLN A 1 2057 ? 200.401 240.521 237.740 1.00 0.00  ? 2057 GLN A CA    1 
ATOM   4704  C C     . GLN A 1 2057 ? 199.760 241.808 238.243 1.00 0.00  ? 2057 GLN A C     1 
ATOM   4705  O O     . GLN A 1 2057 ? 199.909 242.849 237.597 1.00 0.48  ? 2057 GLN A O     1 
ATOM   4706  C CB    . GLN A 1 2057 ? 199.885 240.209 236.332 1.00 3.87  ? 2057 GLN A CB    1 
ATOM   4707  C CG    . GLN A 1 2057 ? 200.722 239.197 235.567 1.00 3.85  ? 2057 GLN A CG    1 
ATOM   4708  C CD    . GLN A 1 2057 ? 202.094 239.727 235.200 1.00 2.85  ? 2057 GLN A CD    1 
ATOM   4709  O OE1   . GLN A 1 2057 ? 202.297 240.934 235.082 1.00 0.00  ? 2057 GLN A OE1   1 
ATOM   4710  N NE2   . GLN A 1 2057 ? 203.047 238.822 235.022 1.00 4.31  ? 2057 GLN A NE2   1 
ATOM   4711  N N     . GLY A 1 2058 ? 199.059 241.765 239.371 1.00 6.76  ? 2058 GLY A N     1 
ATOM   4712  C CA    . GLY A 1 2058 ? 198.419 242.941 239.916 1.00 3.70  ? 2058 GLY A CA    1 
ATOM   4713  C C     . GLY A 1 2058 ? 197.002 243.182 239.454 1.00 1.99  ? 2058 GLY A C     1 
ATOM   4714  O O     . GLY A 1 2058 ? 196.499 244.299 239.618 1.00 6.99  ? 2058 GLY A O     1 
ATOM   4715  N N     . PHE A 1 2059 ? 196.341 242.180 238.883 1.00 1.32  ? 2059 PHE A N     1 
ATOM   4716  C CA    . PHE A 1 2059 ? 194.996 242.359 238.356 1.00 1.31  ? 2059 PHE A CA    1 
ATOM   4717  C C     . PHE A 1 2059 ? 193.976 242.152 239.467 1.00 6.08  ? 2059 PHE A C     1 
ATOM   4718  O O     . PHE A 1 2059 ? 193.864 241.051 240.015 1.00 9.67  ? 2059 PHE A O     1 
ATOM   4719  C CB    . PHE A 1 2059 ? 194.729 241.378 237.216 1.00 0.00  ? 2059 PHE A CB    1 
ATOM   4720  C CG    . PHE A 1 2059 ? 195.323 241.792 235.903 1.00 0.71  ? 2059 PHE A CG    1 
ATOM   4721  C CD1   . PHE A 1 2059 ? 196.692 241.898 235.750 1.00 0.00  ? 2059 PHE A CD1   1 
ATOM   4722  C CD2   . PHE A 1 2059 ? 194.510 242.093 234.827 1.00 0.66  ? 2059 PHE A CD2   1 
ATOM   4723  C CE1   . PHE A 1 2059 ? 197.237 242.279 234.547 1.00 0.09  ? 2059 PHE A CE1   1 
ATOM   4724  C CE2   . PHE A 1 2059 ? 195.049 242.482 233.623 1.00 0.00  ? 2059 PHE A CE2   1 
ATOM   4725  C CZ    . PHE A 1 2059 ? 196.414 242.574 233.483 1.00 4.12  ? 2059 PHE A CZ    1 
ATOM   4726  N N     . ARG A 1 2060 ? 193.234 243.203 239.806 1.00 7.88  ? 2060 ARG A N     1 
ATOM   4727  C CA    . ARG A 1 2060 ? 192.074 243.019 240.661 1.00 3.41  ? 2060 ARG A CA    1 
ATOM   4728  C C     . ARG A 1 2060 ? 190.974 242.321 239.872 1.00 4.72  ? 2060 ARG A C     1 
ATOM   4729  O O     . ARG A 1 2060 ? 190.877 242.457 238.650 1.00 5.78  ? 2060 ARG A O     1 
ATOM   4730  C CB    . ARG A 1 2060 ? 191.572 244.357 241.204 1.00 2.98  ? 2060 ARG A CB    1 
ATOM   4731  C CG    . ARG A 1 2060 ? 191.702 245.526 240.245 1.00 9.48  ? 2060 ARG A CG    1 
ATOM   4732  C CD    . ARG A 1 2060 ? 190.796 246.673 240.667 1.00 10.59 ? 2060 ARG A CD    1 
ATOM   4733  N NE    . ARG A 1 2060 ? 189.381 246.362 240.501 1.00 13.76 ? 2060 ARG A NE    1 
ATOM   4734  C CZ    . ARG A 1 2060 ? 188.726 246.418 239.349 1.00 11.11 ? 2060 ARG A CZ    1 
ATOM   4735  N NH1   . ARG A 1 2060 ? 189.329 246.777 238.228 1.00 5.11  ? 2060 ARG A NH1   1 
ATOM   4736  N NH2   . ARG A 1 2060 ? 187.432 246.113 239.324 1.00 11.02 ? 2060 ARG A NH2   1 
ATOM   4737  N N     . THR A 1 2061 ? 190.136 241.569 240.586 1.00 5.62  ? 2061 THR A N     1 
ATOM   4738  C CA    . THR A 1 2061 ? 189.127 240.703 239.975 1.00 7.90  ? 2061 THR A CA    1 
ATOM   4739  C C     . THR A 1 2061 ? 189.778 239.744 238.976 1.00 3.54  ? 2061 THR A C     1 
ATOM   4740  O O     . THR A 1 2061 ? 189.371 239.627 237.820 1.00 5.21  ? 2061 THR A O     1 
ATOM   4741  C CB    . THR A 1 2061 ? 188.011 241.517 239.305 1.00 7.66  ? 2061 THR A CB    1 
ATOM   4742  O OG1   . THR A 1 2061 ? 188.560 242.322 238.255 1.00 0.00  ? 2061 THR A OG1   1 
ATOM   4743  C CG2   . THR A 1 2061 ? 187.327 242.420 240.321 1.00 12.88 ? 2061 THR A CG2   1 
ATOM   4744  N N     . ALA A 1 2062 ? 190.817 239.056 239.453 1.00 0.94  ? 2062 ALA A N     1 
ATOM   4745  C CA    . ALA A 1 2062 ? 191.536 238.114 238.603 1.00 0.00  ? 2062 ALA A CA    1 
ATOM   4746  C C     . ALA A 1 2062 ? 190.742 236.832 238.394 1.00 0.00  ? 2062 ALA A C     1 
ATOM   4747  O O     . ALA A 1 2062 ? 190.916 236.150 237.379 1.00 7.88  ? 2062 ALA A O     1 
ATOM   4748  C CB    . ALA A 1 2062 ? 192.904 237.804 239.206 1.00 0.69  ? 2062 ALA A CB    1 
ATOM   4749  N N     . GLU A 1 2063 ? 189.881 236.473 239.349 1.00 0.62  ? 2063 GLU A N     1 
ATOM   4750  C CA    . GLU A 1 2063 ? 189.070 235.268 239.197 1.00 0.00  ? 2063 GLU A CA    1 
ATOM   4751  C C     . GLU A 1 2063 ? 188.111 235.389 238.020 1.00 0.89  ? 2063 GLU A C     1 
ATOM   4752  O O     . GLU A 1 2063 ? 187.983 234.456 237.218 1.00 4.27  ? 2063 GLU A O     1 
ATOM   4753  C CB    . GLU A 1 2063 ? 188.297 234.988 240.483 1.00 0.81  ? 2063 GLU A CB    1 
ATOM   4754  C CG    . GLU A 1 2063 ? 187.838 233.549 240.625 1.00 7.16  ? 2063 GLU A CG    1 
ATOM   4755  C CD    . GLU A 1 2063 ? 186.771 233.380 241.687 1.00 10.09 ? 2063 GLU A CD    1 
ATOM   4756  O OE1   . GLU A 1 2063 ? 186.881 234.023 242.752 1.00 11.70 ? 2063 GLU A OE1   1 
ATOM   4757  O OE2   . GLU A 1 2063 ? 185.820 232.604 241.456 1.00 4.53  ? 2063 GLU A OE2   1 
ATOM   4758  N N     . VAL A 1 2064 ? 187.427 236.528 237.905 1.00 0.19  ? 2064 VAL A N     1 
ATOM   4759  C CA    . VAL A 1 2064 ? 186.507 236.743 236.792 1.00 0.00  ? 2064 VAL A CA    1 
ATOM   4760  C C     . VAL A 1 2064 ? 187.264 236.745 235.472 1.00 1.10  ? 2064 VAL A C     1 
ATOM   4761  O O     . VAL A 1 2064 ? 186.828 236.136 234.486 1.00 0.99  ? 2064 VAL A O     1 
ATOM   4762  C CB    . VAL A 1 2064 ? 185.726 238.052 237.000 1.00 0.63  ? 2064 VAL A CB    1 
ATOM   4763  C CG1   . VAL A 1 2064 ? 184.683 238.227 235.913 1.00 0.97  ? 2064 VAL A CG1   1 
ATOM   4764  C CG2   . VAL A 1 2064 ? 185.085 238.071 238.375 1.00 2.78  ? 2064 VAL A CG2   1 
ATOM   4765  N N     . LEU A 1 2065 ? 188.415 237.415 235.436 1.00 0.00  ? 2065 LEU A N     1 
ATOM   4766  C CA    . LEU A 1 2065 ? 189.207 237.463 234.215 1.00 0.00  ? 2065 LEU A CA    1 
ATOM   4767  C C     . LEU A 1 2065 ? 189.671 236.074 233.803 1.00 0.00  ? 2065 LEU A C     1 
ATOM   4768  O O     . LEU A 1 2065 ? 189.661 235.743 232.615 1.00 2.90  ? 2065 LEU A O     1 
ATOM   4769  C CB    . LEU A 1 2065 ? 190.404 238.388 234.404 1.00 0.00  ? 2065 LEU A CB    1 
ATOM   4770  C CG    . LEU A 1 2065 ? 190.119 239.885 234.330 1.00 0.18  ? 2065 LEU A CG    1 
ATOM   4771  C CD1   . LEU A 1 2065 ? 191.408 240.648 234.513 1.00 1.98  ? 2065 LEU A CD1   1 
ATOM   4772  C CD2   . LEU A 1 2065 ? 189.450 240.254 233.020 1.00 1.47  ? 2065 LEU A CD2   1 
ATOM   4773  N N     . ALA A 1 2066 ? 190.088 235.251 234.766 1.00 0.67  ? 2066 ALA A N     1 
ATOM   4774  C CA    . ALA A 1 2066 ? 190.540 233.901 234.449 1.00 0.00  ? 2066 ALA A CA    1 
ATOM   4775  C C     . ALA A 1 2066 ? 189.389 233.032 233.956 1.00 0.00  ? 2066 ALA A C     1 
ATOM   4776  O O     . ALA A 1 2066 ? 189.510 232.337 232.938 1.00 2.56  ? 2066 ALA A O     1 
ATOM   4777  C CB    . ALA A 1 2066 ? 191.200 233.274 235.675 1.00 0.00  ? 2066 ALA A CB    1 
ATOM   4778  N N     . ASN A 1 2067 ? 188.260 233.057 234.668 1.00 1.77  ? 2067 ASN A N     1 
ATOM   4779  C CA    . ASN A 1 2067 ? 187.118 232.246 234.269 1.00 3.11  ? 2067 ASN A CA    1 
ATOM   4780  C C     . ASN A 1 2067 ? 186.427 232.779 233.023 1.00 3.19  ? 2067 ASN A C     1 
ATOM   4781  O O     . ASN A 1 2067 ? 185.495 232.134 232.532 1.00 5.54  ? 2067 ASN A O     1 
ATOM   4782  C CB    . ASN A 1 2067 ? 186.144 232.086 235.453 1.00 0.59  ? 2067 ASN A CB    1 
ATOM   4783  C CG    . ASN A 1 2067 ? 185.294 233.329 235.738 1.00 3.16  ? 2067 ASN A CG    1 
ATOM   4784  O OD1   . ASN A 1 2067 ? 184.912 234.084 234.846 1.00 4.52  ? 2067 ASN A OD1   1 
ATOM   4785  N ND2   . ASN A 1 2067 ? 184.988 233.529 237.014 1.00 2.87  ? 2067 ASN A ND2   1 
ATOM   4786  N N     . LYS A 1 2068 ? 186.829 233.948 232.529 1.00 1.12  ? 2068 LYS A N     1 
ATOM   4787  C CA    . LYS A 1 2068 ? 186.461 234.378 231.186 1.00 0.17  ? 2068 LYS A CA    1 
ATOM   4788  C C     . LYS A 1 2068 ? 187.488 233.980 230.133 1.00 2.43  ? 2068 LYS A C     1 
ATOM   4789  O O     . LYS A 1 2068 ? 187.112 233.496 229.063 1.00 8.68  ? 2068 LYS A O     1 
ATOM   4790  C CB    . LYS A 1 2068 ? 186.261 235.895 231.146 1.00 0.00  ? 2068 LYS A CB    1 
ATOM   4791  C CG    . LYS A 1 2068 ? 184.952 236.364 231.743 1.00 0.00  ? 2068 LYS A CG    1 
ATOM   4792  C CD    . LYS A 1 2068 ? 184.892 237.876 231.824 1.00 0.00  ? 2068 LYS A CD    1 
ATOM   4793  C CE    . LYS A 1 2068 ? 183.458 238.371 231.807 1.00 2.36  ? 2068 LYS A CE    1 
ATOM   4794  N NZ    . LYS A 1 2068 ? 182.790 238.098 230.512 1.00 4.45  ? 2068 LYS A NZ    1 
ATOM   4795  N N     . ILE A 1 2069 ? 188.780 234.159 230.411 1.00 1.68  ? 2069 ILE A N     1 
ATOM   4796  C CA    . ILE A 1 2069 ? 189.795 233.970 229.381 1.00 0.00  ? 2069 ILE A CA    1 
ATOM   4797  C C     . ILE A 1 2069 ? 189.999 232.491 229.075 1.00 0.00  ? 2069 ILE A C     1 
ATOM   4798  O O     . ILE A 1 2069 ? 190.270 232.122 227.926 1.00 0.75  ? 2069 ILE A O     1 
ATOM   4799  C CB    . ILE A 1 2069 ? 191.112 234.665 229.781 1.00 2.88  ? 2069 ILE A CB    1 
ATOM   4800  C CG1   . ILE A 1 2069 ? 192.056 234.738 228.581 1.00 1.90  ? 2069 ILE A CG1   1 
ATOM   4801  C CG2   . ILE A 1 2069 ? 191.791 233.956 230.943 1.00 6.22  ? 2069 ILE A CG2   1 
ATOM   4802  C CD1   . ILE A 1 2069 ? 191.549 235.617 227.466 1.00 0.27  ? 2069 ILE A CD1   1 
ATOM   4803  N N     . VAL A 1 2070 ? 189.896 231.618 230.082 1.00 0.00  ? 2070 VAL A N     1 
ATOM   4804  C CA    . VAL A 1 2070 ? 190.061 230.185 229.826 1.00 0.18  ? 2070 VAL A CA    1 
ATOM   4805  C C     . VAL A 1 2070 ? 188.962 229.637 228.921 1.00 2.06  ? 2070 VAL A C     1 
ATOM   4806  O O     . VAL A 1 2070 ? 189.287 228.933 227.948 1.00 3.92  ? 2070 VAL A O     1 
ATOM   4807  C CB    . VAL A 1 2070 ? 190.189 229.419 231.155 1.00 0.14  ? 2070 VAL A CB    1 
ATOM   4808  C CG1   . VAL A 1 2070 ? 190.213 227.924 230.901 1.00 0.00  ? 2070 VAL A CG1   1 
ATOM   4809  C CG2   . VAL A 1 2070 ? 191.446 229.849 231.885 1.00 5.19  ? 2070 VAL A CG2   1 
ATOM   4810  N N     . PRO A 1 2071 ? 187.672 229.908 229.158 1.00 2.45  ? 2071 PRO A N     1 
ATOM   4811  C CA    . PRO A 1 2071 ? 186.662 229.496 228.172 1.00 2.84  ? 2071 PRO A CA    1 
ATOM   4812  C C     . PRO A 1 2071 ? 186.869 230.108 226.800 1.00 0.00  ? 2071 PRO A C     1 
ATOM   4813  O O     . PRO A 1 2071 ? 186.543 229.465 225.798 1.00 0.00  ? 2071 PRO A O     1 
ATOM   4814  C CB    . PRO A 1 2071 ? 185.346 229.965 228.807 1.00 1.95  ? 2071 PRO A CB    1 
ATOM   4815  C CG    . PRO A 1 2071 ? 185.623 229.953 230.251 1.00 0.61  ? 2071 PRO A CG    1 
ATOM   4816  C CD    . PRO A 1 2071 ? 187.034 230.436 230.376 1.00 2.36  ? 2071 PRO A CD    1 
ATOM   4817  N N     . PHE A 1 2072 ? 187.391 231.333 226.717 1.00 0.00  ? 2072 PHE A N     1 
ATOM   4818  C CA    . PHE A 1 2072 ? 187.649 231.936 225.412 1.00 0.00  ? 2072 PHE A CA    1 
ATOM   4819  C C     . PHE A 1 2072 ? 188.719 231.167 224.647 1.00 0.00  ? 2072 PHE A C     1 
ATOM   4820  O O     . PHE A 1 2072 ? 188.577 230.906 223.446 1.00 3.21  ? 2072 PHE A O     1 
ATOM   4821  C CB    . PHE A 1 2072 ? 188.052 233.399 225.580 1.00 2.45  ? 2072 PHE A CB    1 
ATOM   4822  C CG    . PHE A 1 2072 ? 188.497 234.045 224.305 1.00 0.76  ? 2072 PHE A CG    1 
ATOM   4823  C CD1   . PHE A 1 2072 ? 187.573 234.455 223.364 1.00 0.00  ? 2072 PHE A CD1   1 
ATOM   4824  C CD2   . PHE A 1 2072 ? 189.844 234.250 224.051 1.00 0.00  ? 2072 PHE A CD2   1 
ATOM   4825  C CE1   . PHE A 1 2072 ? 187.982 235.043 222.190 1.00 1.33  ? 2072 PHE A CE1   1 
ATOM   4826  C CE2   . PHE A 1 2072 ? 190.257 234.842 222.881 1.00 0.00  ? 2072 PHE A CE2   1 
ATOM   4827  C CZ    . PHE A 1 2072 ? 189.326 235.240 221.949 1.00 2.07  ? 2072 PHE A CZ    1 
ATOM   4828  N N     . PHE A 1 2073 ? 189.807 230.804 225.327 1.00 4.12  ? 2073 PHE A N     1 
ATOM   4829  C CA    . PHE A 1 2073 ? 190.833 229.989 224.693 1.00 0.00  ? 2073 PHE A CA    1 
ATOM   4830  C C     . PHE A 1 2073 ? 190.318 228.597 224.363 1.00 0.00  ? 2073 PHE A C     1 
ATOM   4831  O O     . PHE A 1 2073 ? 190.817 227.973 223.422 1.00 2.15  ? 2073 PHE A O     1 
ATOM   4832  C CB    . PHE A 1 2073 ? 192.062 229.899 225.597 1.00 0.00  ? 2073 PHE A CB    1 
ATOM   4833  C CG    . PHE A 1 2073 ? 193.110 230.927 225.292 1.00 0.89  ? 2073 PHE A CG    1 
ATOM   4834  C CD1   . PHE A 1 2073 ? 192.937 232.243 225.681 1.00 1.59  ? 2073 PHE A CD1   1 
ATOM   4835  C CD2   . PHE A 1 2073 ? 194.268 230.582 224.620 1.00 0.00  ? 2073 PHE A CD2   1 
ATOM   4836  C CE1   . PHE A 1 2073 ? 193.897 233.194 225.403 1.00 0.98  ? 2073 PHE A CE1   1 
ATOM   4837  C CE2   . PHE A 1 2073 ? 195.229 231.530 224.341 1.00 0.00  ? 2073 PHE A CE2   1 
ATOM   4838  C CZ    . PHE A 1 2073 ? 195.042 232.837 224.732 1.00 0.00  ? 2073 PHE A CZ    1 
ATOM   4839  N N     . LYS A 1 2074 ? 189.339 228.098 225.121 1.00 2.14  ? 2074 LYS A N     1 
ATOM   4840  C CA    . LYS A 1 2074 ? 188.682 226.846 224.758 1.00 0.97  ? 2074 LYS A CA    1 
ATOM   4841  C C     . LYS A 1 2074 ? 187.882 226.995 223.468 1.00 0.39  ? 2074 LYS A C     1 
ATOM   4842  O O     . LYS A 1 2074 ? 187.946 226.130 222.588 1.00 1.88  ? 2074 LYS A O     1 
ATOM   4843  C CB    . LYS A 1 2074 ? 187.779 226.388 225.903 1.00 1.95  ? 2074 LYS A CB    1 
ATOM   4844  C CG    . LYS A 1 2074 ? 186.926 225.168 225.603 1.00 3.95  ? 2074 LYS A CG    1 
ATOM   4845  C CD    . LYS A 1 2074 ? 187.757 223.899 225.562 1.00 7.93  ? 2074 LYS A CD    1 
ATOM   4846  C CE    . LYS A 1 2074 ? 186.881 222.669 225.727 1.00 6.38  ? 2074 LYS A CE    1 
ATOM   4847  N NZ    . LYS A 1 2074 ? 186.864 222.188 227.136 1.00 5.50  ? 2074 LYS A NZ    1 
ATOM   4848  N N     . LEU A 1 2075 ? 187.120 228.086 223.341 1.00 3.56  ? 2075 LEU A N     1 
ATOM   4849  C CA    . LEU A 1 2075 ? 186.331 228.314 222.133 1.00 0.00  ? 2075 LEU A CA    1 
ATOM   4850  C C     . LEU A 1 2075 ? 187.213 228.507 220.910 1.00 0.00  ? 2075 LEU A C     1 
ATOM   4851  O O     . LEU A 1 2075 ? 186.864 228.044 219.820 1.00 13.98 ? 2075 LEU A O     1 
ATOM   4852  C CB    . LEU A 1 2075 ? 185.420 229.532 222.291 1.00 0.00  ? 2075 LEU A CB    1 
ATOM   4853  C CG    . LEU A 1 2075 ? 184.522 229.682 223.515 1.00 1.25  ? 2075 LEU A CG    1 
ATOM   4854  C CD1   . LEU A 1 2075 ? 183.646 230.917 223.378 1.00 0.14  ? 2075 LEU A CD1   1 
ATOM   4855  C CD2   . LEU A 1 2075 ? 183.683 228.442 223.726 1.00 6.98  ? 2075 LEU A CD2   1 
ATOM   4856  N N     . CYS A 1 2076 ? 188.345 229.197 221.064 1.00 0.04  ? 2076 CYS A N     1 
ATOM   4857  C CA    . CYS A 1 2076 ? 189.221 229.437 219.922 1.00 0.00  ? 2076 CYS A CA    1 
ATOM   4858  C C     . CYS A 1 2076 ? 189.758 228.146 219.316 1.00 0.95  ? 2076 CYS A C     1 
ATOM   4859  O O     . CYS A 1 2076 ? 190.200 228.156 218.163 1.00 2.98  ? 2076 CYS A O     1 
ATOM   4860  C CB    . CYS A 1 2076 ? 190.384 230.343 220.325 1.00 0.00  ? 2076 CYS A CB    1 
ATOM   4861  S SG    . CYS A 1 2076 ? 189.924 232.057 220.624 1.00 20.61 ? 2076 CYS A SG    1 
ATOM   4862  N N     . ASP A 1 2077 ? 189.742 227.043 220.061 1.00 0.23  ? 2077 ASP A N     1 
ATOM   4863  C CA    . ASP A 1 2077 ? 190.087 225.738 219.512 1.00 1.14  ? 2077 ASP A CA    1 
ATOM   4864  C C     . ASP A 1 2077 ? 188.914 225.047 218.832 1.00 1.30  ? 2077 ASP A C     1 
ATOM   4865  O O     . ASP A 1 2077 ? 189.116 224.014 218.184 1.00 3.77  ? 2077 ASP A O     1 
ATOM   4866  C CB    . ASP A 1 2077 ? 190.637 224.824 220.611 1.00 2.86  ? 2077 ASP A CB    1 
ATOM   4867  C CG    . ASP A 1 2077 ? 192.116 225.023 220.848 1.00 4.59  ? 2077 ASP A CG    1 
ATOM   4868  O OD1   . ASP A 1 2077 ? 192.813 225.460 219.911 1.00 3.91  ? 2077 ASP A OD1   1 
ATOM   4869  O OD2   . ASP A 1 2077 ? 192.585 224.735 221.969 1.00 8.20  ? 2077 ASP A OD2   1 
ATOM   4870  N N     . GLU A 1 2078 ? 187.701 225.581 218.958 1.00 1.26  ? 2078 GLU A N     1 
ATOM   4871  C CA    . GLU A 1 2078 ? 186.518 224.980 218.359 1.00 0.00  ? 2078 GLU A CA    1 
ATOM   4872  C C     . GLU A 1 2078 ? 185.959 225.827 217.223 1.00 2.88  ? 2078 GLU A C     1 
ATOM   4873  O O     . GLU A 1 2078 ? 185.790 225.330 216.106 1.00 10.24 ? 2078 GLU A O     1 
ATOM   4874  C CB    . GLU A 1 2078 ? 185.439 224.756 219.428 1.00 2.14  ? 2078 GLU A CB    1 
ATOM   4875  C CG    . GLU A 1 2078 ? 185.757 223.664 220.429 1.00 8.15  ? 2078 GLU A CG    1 
ATOM   4876  C CD    . GLU A 1 2078 ? 184.577 223.345 221.325 1.00 10.70 ? 2078 GLU A CD    1 
ATOM   4877  O OE1   . GLU A 1 2078 ? 183.576 224.092 221.276 1.00 14.06 ? 2078 GLU A OE1   1 
ATOM   4878  O OE2   . GLU A 1 2078 ? 184.649 222.351 222.077 1.00 6.39  ? 2078 GLU A OE2   1 
ATOM   4879  N N     . GLN A 1 2079 ? 185.666 227.100 217.480 1.00 1.22  ? 2079 GLN A N     1 
ATOM   4880  C CA    . GLN A 1 2079 ? 185.037 227.951 216.479 1.00 0.00  ? 2079 GLN A CA    1 
ATOM   4881  C C     . GLN A 1 2079 ? 185.988 228.377 215.370 1.00 0.03  ? 2079 GLN A C     1 
ATOM   4882  O O     . GLN A 1 2079 ? 185.523 228.698 214.272 1.00 9.64  ? 2079 GLN A O     1 
ATOM   4883  C CB    . GLN A 1 2079 ? 184.446 229.198 217.141 1.00 0.00  ? 2079 GLN A CB    1 
ATOM   4884  C CG    . GLN A 1 2079 ? 183.026 229.037 217.664 1.00 0.00  ? 2079 GLN A CG    1 
ATOM   4885  C CD    . GLN A 1 2079 ? 182.869 227.868 218.612 1.00 4.29  ? 2079 GLN A CD    1 
ATOM   4886  O OE1   . GLN A 1 2079 ? 183.802 227.498 219.320 1.00 10.46 ? 2079 GLN A OE1   1 
ATOM   4887  N NE2   . GLN A 1 2079 ? 181.680 227.279 218.631 1.00 15.74 ? 2079 GLN A NE2   1 
ATOM   4888  N N     . LEU A 1 2080 ? 187.293 228.380 215.618 1.00 0.00  ? 2080 LEU A N     1 
ATOM   4889  C CA    . LEU A 1 2080 ? 188.275 228.864 214.659 1.00 2.11  ? 2080 LEU A CA    1 
ATOM   4890  C C     . LEU A 1 2080 ? 188.787 227.713 213.806 1.00 1.73  ? 2080 LEU A C     1 
ATOM   4891  O O     . LEU A 1 2080 ? 188.988 226.600 214.302 1.00 4.19  ? 2080 LEU A O     1 
ATOM   4892  C CB    . LEU A 1 2080 ? 189.444 229.549 215.370 1.00 4.38  ? 2080 LEU A CB    1 
ATOM   4893  C CG    . LEU A 1 2080 ? 189.428 231.076 215.428 1.00 0.00  ? 2080 LEU A CG    1 
ATOM   4894  C CD1   . LEU A 1 2080 ? 188.176 231.582 216.123 1.00 0.00  ? 2080 LEU A CD1   1 
ATOM   4895  C CD2   . LEU A 1 2080 ? 190.672 231.577 216.134 1.00 0.00  ? 2080 LEU A CD2   1 
ATOM   4896  N N     . SER A 1 2081 ? 188.992 227.988 212.519 1.00 0.17  ? 2081 SER A N     1 
ATOM   4897  C CA    . SER A 1 2081 ? 189.480 226.968 211.602 1.00 6.47  ? 2081 SER A CA    1 
ATOM   4898  C C     . SER A 1 2081 ? 190.870 226.504 212.012 1.00 2.07  ? 2081 SER A C     1 
ATOM   4899  O O     . SER A 1 2081 ? 191.735 227.311 212.360 1.00 4.40  ? 2081 SER A O     1 
ATOM   4900  C CB    . SER A 1 2081 ? 189.508 227.510 210.175 1.00 12.19 ? 2081 SER A CB    1 
ATOM   4901  O OG    . SER A 1 2081 ? 190.461 228.550 210.049 1.00 14.11 ? 2081 SER A OG    1 
ATOM   4902  N N     . SER A 1 2082 ? 191.082 225.192 211.965 1.00 2.77  ? 2082 SER A N     1 
ATOM   4903  C CA    . SER A 1 2082 ? 192.338 224.621 212.428 1.00 0.97  ? 2082 SER A CA    1 
ATOM   4904  C C     . SER A 1 2082 ? 193.483 225.029 211.511 1.00 5.89  ? 2082 SER A C     1 
ATOM   4905  O O     . SER A 1 2082 ? 193.439 224.798 210.299 1.00 9.57  ? 2082 SER A O     1 
ATOM   4906  C CB    . SER A 1 2082 ? 192.232 223.099 212.496 1.00 4.69  ? 2082 SER A CB    1 
ATOM   4907  O OG    . SER A 1 2082 ? 193.457 222.522 212.912 1.00 8.11  ? 2082 SER A OG    1 
ATOM   4908  N N     . GLN A 1 2083 ? 194.513 225.633 212.097 1.00 10.19 ? 2083 GLN A N     1 
ATOM   4909  C CA    . GLN A 1 2083 ? 195.722 226.009 211.383 1.00 3.16  ? 2083 GLN A CA    1 
ATOM   4910  C C     . GLN A 1 2083 ? 196.918 225.387 212.089 1.00 8.39  ? 2083 GLN A C     1 
ATOM   4911  O O     . GLN A 1 2083 ? 196.911 225.186 213.305 1.00 4.67  ? 2083 GLN A O     1 
ATOM   4912  C CB    . GLN A 1 2083 ? 195.893 227.531 211.312 1.00 1.28  ? 2083 GLN A CB    1 
ATOM   4913  C CG    . GLN A 1 2083 ? 194.773 228.278 210.602 1.00 7.21  ? 2083 GLN A CG    1 
ATOM   4914  C CD    . GLN A 1 2083 ? 194.500 227.767 209.204 1.00 9.45  ? 2083 GLN A CD    1 
ATOM   4915  O OE1   . GLN A 1 2083 ? 193.392 227.330 208.895 1.00 8.56  ? 2083 GLN A OE1   1 
ATOM   4916  N NE2   . GLN A 1 2083 ? 195.511 227.825 208.345 1.00 12.39 ? 2083 GLN A NE2   1 
ATOM   4917  N N     . SER A 1 2084 ? 197.954 225.085 211.308 1.00 13.32 ? 2084 SER A N     1 
ATOM   4918  C CA    . SER A 1 2084 ? 199.143 224.449 211.859 1.00 6.73  ? 2084 SER A CA    1 
ATOM   4919  C C     . SER A 1 2084 ? 199.956 225.379 212.749 1.00 9.71  ? 2084 SER A C     1 
ATOM   4920  O O     . SER A 1 2084 ? 200.867 224.906 213.437 1.00 12.36 ? 2084 SER A O     1 
ATOM   4921  C CB    . SER A 1 2084 ? 200.023 223.919 210.726 1.00 6.33  ? 2084 SER A CB    1 
ATOM   4922  O OG    . SER A 1 2084 ? 200.167 224.883 209.698 1.00 3.45  ? 2084 SER A OG    1 
ATOM   4923  N N     . HIS A 1 2085 ? 199.657 226.677 212.754 1.00 7.09  ? 2085 HIS A N     1 
ATOM   4924  C CA    . HIS A 1 2085 ? 200.404 227.642 213.545 1.00 5.81  ? 2085 HIS A CA    1 
ATOM   4925  C C     . HIS A 1 2085 ? 199.614 228.194 214.722 1.00 9.29  ? 2085 HIS A C     1 
ATOM   4926  O O     . HIS A 1 2085 ? 200.163 228.981 215.501 1.00 13.01 ? 2085 HIS A O     1 
ATOM   4927  C CB    . HIS A 1 2085 ? 200.876 228.802 212.658 1.00 3.28  ? 2085 HIS A CB    1 
ATOM   4928  C CG    . HIS A 1 2085 ? 199.760 229.565 212.017 1.00 2.18  ? 2085 HIS A CG    1 
ATOM   4929  N ND1   . HIS A 1 2085 ? 199.161 229.164 210.843 1.00 5.09  ? 2085 HIS A ND1   1 
ATOM   4930  C CD2   . HIS A 1 2085 ? 199.141 230.713 212.381 1.00 0.39  ? 2085 HIS A CD2   1 
ATOM   4931  C CE1   . HIS A 1 2085 ? 198.215 230.027 210.517 1.00 3.15  ? 2085 HIS A CE1   1 
ATOM   4932  N NE2   . HIS A 1 2085 ? 198.184 230.977 211.433 1.00 2.81  ? 2085 HIS A NE2   1 
ATOM   4933  N N     . TYR A 1 2086 ? 198.348 227.812 214.874 1.00 7.07  ? 2086 TYR A N     1 
ATOM   4934  C CA    . TYR A 1 2086 ? 197.551 228.282 215.998 1.00 0.00  ? 2086 TYR A CA    1 
ATOM   4935  C C     . TYR A 1 2086 ? 198.025 227.623 217.286 1.00 0.11  ? 2086 TYR A C     1 
ATOM   4936  O O     . TYR A 1 2086 ? 198.226 226.406 217.336 1.00 7.96  ? 2086 TYR A O     1 
ATOM   4937  C CB    . TYR A 1 2086 ? 196.074 227.973 215.769 1.00 0.00  ? 2086 TYR A CB    1 
ATOM   4938  C CG    . TYR A 1 2086 ? 195.378 228.911 214.812 1.00 0.00  ? 2086 TYR A CG    1 
ATOM   4939  C CD1   . TYR A 1 2086 ? 196.061 229.956 214.208 1.00 0.00  ? 2086 TYR A CD1   1 
ATOM   4940  C CD2   . TYR A 1 2086 ? 194.034 228.748 214.515 1.00 0.00  ? 2086 TYR A CD2   1 
ATOM   4941  C CE1   . TYR A 1 2086 ? 195.423 230.808 213.332 1.00 0.00  ? 2086 TYR A CE1   1 
ATOM   4942  C CE2   . TYR A 1 2086 ? 193.390 229.595 213.646 1.00 0.00  ? 2086 TYR A CE2   1 
ATOM   4943  C CZ    . TYR A 1 2086 ? 194.087 230.622 213.057 1.00 0.00  ? 2086 TYR A CZ    1 
ATOM   4944  O OH    . TYR A 1 2086 ? 193.440 231.465 212.187 1.00 10.06 ? 2086 TYR A OH    1 
ATOM   4945  N N     . ASP A 1 2087 ? 198.201 228.427 218.331 1.00 1.07  ? 2087 ASP A N     1 
ATOM   4946  C CA    . ASP A 1 2087 ? 198.598 227.934 219.648 1.00 1.82  ? 2087 ASP A CA    1 
ATOM   4947  C C     . ASP A 1 2087 ? 197.648 228.525 220.683 1.00 6.17  ? 2087 ASP A C     1 
ATOM   4948  O O     . ASP A 1 2087 ? 197.794 229.685 221.079 1.00 0.00  ? 2087 ASP A O     1 
ATOM   4949  C CB    . ASP A 1 2087 ? 200.046 228.288 219.961 1.00 0.30  ? 2087 ASP A CB    1 
ATOM   4950  C CG    . ASP A 1 2087 ? 200.729 227.241 220.816 1.00 7.93  ? 2087 ASP A CG    1 
ATOM   4951  O OD1   . ASP A 1 2087 ? 200.086 226.221 221.136 1.00 0.00  ? 2087 ASP A OD1   1 
ATOM   4952  O OD2   . ASP A 1 2087 ? 201.909 227.440 221.173 1.00 14.91 ? 2087 ASP A OD2   1 
ATOM   4953  N N     . PHE A 1 2088 ? 196.672 227.727 221.113 1.00 2.81  ? 2088 PHE A N     1 
ATOM   4954  C CA    . PHE A 1 2088 ? 195.745 228.106 222.169 1.00 0.00  ? 2088 PHE A CA    1 
ATOM   4955  C C     . PHE A 1 2088 ? 195.946 227.254 223.417 1.00 0.00  ? 2088 PHE A C     1 
ATOM   4956  O O     . PHE A 1 2088 ? 194.992 226.964 224.142 1.00 1.60  ? 2088 PHE A O     1 
ATOM   4957  C CB    . PHE A 1 2088 ? 194.304 228.007 221.675 1.00 0.00  ? 2088 PHE A CB    1 
ATOM   4958  C CG    . PHE A 1 2088 ? 194.000 228.907 220.513 1.00 0.00  ? 2088 PHE A CG    1 
ATOM   4959  C CD1   . PHE A 1 2088 ? 194.075 230.281 220.647 1.00 1.71  ? 2088 PHE A CD1   1 
ATOM   4960  C CD2   . PHE A 1 2088 ? 193.646 228.378 219.285 1.00 1.95  ? 2088 PHE A CD2   1 
ATOM   4961  C CE1   . PHE A 1 2088 ? 193.798 231.109 219.578 1.00 2.34  ? 2088 PHE A CE1   1 
ATOM   4962  C CE2   . PHE A 1 2088 ? 193.369 229.200 218.214 1.00 0.91  ? 2088 PHE A CE2   1 
ATOM   4963  C CZ    . PHE A 1 2088 ? 193.445 230.567 218.360 1.00 0.33  ? 2088 PHE A CZ    1 
ATOM   4964  N N     . GLY A 1 2089 ? 197.186 226.845 223.672 1.00 0.00  ? 2089 GLY A N     1 
ATOM   4965  C CA    . GLY A 1 2089 ? 197.507 225.999 224.798 1.00 0.00  ? 2089 GLY A CA    1 
ATOM   4966  C C     . GLY A 1 2089 ? 197.773 226.794 226.061 1.00 2.05  ? 2089 GLY A C     1 
ATOM   4967  O O     . GLY A 1 2089 ? 197.442 227.975 226.177 1.00 6.11  ? 2089 GLY A O     1 
ATOM   4968  N N     . LEU A 1 2090 ? 198.380 226.112 227.032 1.00 3.35  ? 2090 LEU A N     1 
ATOM   4969  C CA    . LEU A 1 2090 ? 198.648 226.743 228.319 1.00 1.24  ? 2090 LEU A CA    1 
ATOM   4970  C C     . LEU A 1 2090 ? 199.802 227.731 228.227 1.00 5.50  ? 2090 LEU A C     1 
ATOM   4971  O O     . LEU A 1 2090 ? 199.762 228.797 228.851 1.00 11.68 ? 2090 LEU A O     1 
ATOM   4972  C CB    . LEU A 1 2090 ? 198.936 225.676 229.372 1.00 3.78  ? 2090 LEU A CB    1 
ATOM   4973  C CG    . LEU A 1 2090 ? 198.938 226.141 230.825 1.00 10.73 ? 2090 LEU A CG    1 
ATOM   4974  C CD1   . LEU A 1 2090 ? 197.680 226.934 231.132 1.00 5.99  ? 2090 LEU A CD1   1 
ATOM   4975  C CD2   . LEU A 1 2090 ? 199.058 224.946 231.746 1.00 7.34  ? 2090 LEU A CD2   1 
ATOM   4976  N N     . ARG A 1 2091 ? 200.844 227.393 227.465 1.00 6.11  ? 2091 ARG A N     1 
ATOM   4977  C CA    . ARG A 1 2091 ? 201.986 228.291 227.322 1.00 6.72  ? 2091 ARG A CA    1 
ATOM   4978  C C     . ARG A 1 2091 ? 201.575 229.596 226.652 1.00 7.17  ? 2091 ARG A C     1 
ATOM   4979  O O     . ARG A 1 2091 ? 201.994 230.685 227.065 1.00 11.69 ? 2091 ARG A O     1 
ATOM   4980  C CB    . ARG A 1 2091 ? 203.090 227.597 226.527 1.00 11.06 ? 2091 ARG A CB    1 
ATOM   4981  C CG    . ARG A 1 2091 ? 204.384 228.377 226.441 1.00 14.32 ? 2091 ARG A CG    1 
ATOM   4982  C CD    . ARG A 1 2091 ? 205.441 227.596 225.687 1.00 12.63 ? 2091 ARG A CD    1 
ATOM   4983  N NE    . ARG A 1 2091 ? 205.793 226.357 226.372 1.00 19.94 ? 2091 ARG A NE    1 
ATOM   4984  C CZ    . ARG A 1 2091 ? 206.797 226.232 227.228 1.00 16.83 ? 2091 ARG A CZ    1 
ATOM   4985  N NH1   . ARG A 1 2091 ? 207.573 227.257 227.539 1.00 17.58 ? 2091 ARG A NH1   1 
ATOM   4986  N NH2   . ARG A 1 2091 ? 207.026 225.048 227.790 1.00 9.54  ? 2091 ARG A NH2   1 
ATOM   4987  N N     . ALA A 1 2092 ? 200.745 229.503 225.611 1.00 0.84  ? 2092 ALA A N     1 
ATOM   4988  C CA    . ALA A 1 2092 ? 200.249 230.700 224.943 1.00 0.00  ? 2092 ALA A CA    1 
ATOM   4989  C C     . ALA A 1 2092 ? 199.374 231.529 225.873 1.00 4.19  ? 2092 ALA A C     1 
ATOM   4990  O O     . ALA A 1 2092 ? 199.430 232.765 225.853 1.00 13.04 ? 2092 ALA A O     1 
ATOM   4991  C CB    . ALA A 1 2092 ? 199.479 230.313 223.684 1.00 4.36  ? 2092 ALA A CB    1 
ATOM   4992  N N     . LEU A 1 2093 ? 198.550 230.869 226.688 1.00 0.00  ? 2093 LEU A N     1 
ATOM   4993  C CA    . LEU A 1 2093 ? 197.736 231.589 227.660 1.00 0.00  ? 2093 LEU A CA    1 
ATOM   4994  C C     . LEU A 1 2093 ? 198.605 232.330 228.669 1.00 4.05  ? 2093 LEU A C     1 
ATOM   4995  O O     . LEU A 1 2093 ? 198.338 233.491 228.993 1.00 14.11 ? 2093 LEU A O     1 
ATOM   4996  C CB    . LEU A 1 2093 ? 196.790 230.619 228.367 1.00 0.00  ? 2093 LEU A CB    1 
ATOM   4997  C CG    . LEU A 1 2093 ? 195.798 231.208 229.369 1.00 1.85  ? 2093 LEU A CG    1 
ATOM   4998  C CD1   . LEU A 1 2093 ? 194.777 232.080 228.676 1.00 5.56  ? 2093 LEU A CD1   1 
ATOM   4999  C CD2   . LEU A 1 2093 ? 195.105 230.095 230.131 1.00 0.00  ? 2093 LEU A CD2   1 
ATOM   5000  N N     . LYS A 1 2094 ? 199.658 231.679 229.164 1.00 1.96  ? 2094 LYS A N     1 
ATOM   5001  C CA    . LYS A 1 2094 ? 200.570 232.333 230.097 1.00 0.00  ? 2094 LYS A CA    1 
ATOM   5002  C C     . LYS A 1 2094 ? 201.256 233.530 229.449 1.00 4.27  ? 2094 LYS A C     1 
ATOM   5003  O O     . LYS A 1 2094 ? 201.439 234.577 230.083 1.00 12.72 ? 2094 LYS A O     1 
ATOM   5004  C CB    . LYS A 1 2094 ? 201.608 231.329 230.598 1.00 4.08  ? 2094 LYS A CB    1 
ATOM   5005  C CG    . LYS A 1 2094 ? 201.035 230.158 231.370 1.00 1.84  ? 2094 LYS A CG    1 
ATOM   5006  C CD    . LYS A 1 2094 ? 202.140 229.244 231.859 1.00 0.00  ? 2094 LYS A CD    1 
ATOM   5007  C CE    . LYS A 1 2094 ? 203.038 229.946 232.855 1.00 1.58  ? 2094 LYS A CE    1 
ATOM   5008  N NZ    . LYS A 1 2094 ? 204.049 229.025 233.437 1.00 5.24  ? 2094 LYS A NZ    1 
ATOM   5009  N N     . SER A 1 2095 ? 201.668 233.382 228.188 1.00 4.32  ? 2095 SER A N     1 
ATOM   5010  C CA    . SER A 1 2095 ? 202.298 234.496 227.485 1.00 6.83  ? 2095 SER A CA    1 
ATOM   5011  C C     . SER A 1 2095 ? 201.331 235.664 227.328 1.00 7.71  ? 2095 SER A C     1 
ATOM   5012  O O     . SER A 1 2095 ? 201.706 236.827 227.527 1.00 12.96 ? 2095 SER A O     1 
ATOM   5013  C CB    . SER A 1 2095 ? 202.811 234.030 226.124 1.00 12.07 ? 2095 SER A CB    1 
ATOM   5014  O OG    . SER A 1 2095 ? 203.451 235.086 225.432 1.00 15.73 ? 2095 SER A OG    1 
ATOM   5015  N N     . VAL A 1 2096 ? 200.077 235.371 226.980 1.00 7.01  ? 2096 VAL A N     1 
ATOM   5016  C CA    . VAL A 1 2096 ? 199.070 236.421 226.880 1.00 1.77  ? 2096 VAL A CA    1 
ATOM   5017  C C     . VAL A 1 2096 ? 198.876 237.103 228.228 1.00 1.49  ? 2096 VAL A C     1 
ATOM   5018  O O     . VAL A 1 2096 ? 198.719 238.325 228.301 1.00 7.80  ? 2096 VAL A O     1 
ATOM   5019  C CB    . VAL A 1 2096 ? 197.751 235.842 226.336 1.00 1.31  ? 2096 VAL A CB    1 
ATOM   5020  C CG1   . VAL A 1 2096 ? 196.590 236.777 226.628 1.00 1.46  ? 2096 VAL A CG1   1 
ATOM   5021  C CG2   . VAL A 1 2096 ? 197.864 235.581 224.846 1.00 0.56  ? 2096 VAL A CG2   1 
ATOM   5022  N N     . LEU A 1 2097 ? 198.893 236.330 229.315 1.00 0.00  ? 2097 LEU A N     1 
ATOM   5023  C CA    . LEU A 1 2097 ? 198.686 236.909 230.640 1.00 0.00  ? 2097 LEU A CA    1 
ATOM   5024  C C     . LEU A 1 2097 ? 199.841 237.818 231.049 1.00 0.00  ? 2097 LEU A C     1 
ATOM   5025  O O     . LEU A 1 2097 ? 199.617 238.898 231.611 1.00 5.26  ? 2097 LEU A O     1 
ATOM   5026  C CB    . LEU A 1 2097 ? 198.482 235.799 231.668 1.00 0.33  ? 2097 LEU A CB    1 
ATOM   5027  C CG    . LEU A 1 2097 ? 197.215 234.958 231.504 1.00 0.00  ? 2097 LEU A CG    1 
ATOM   5028  C CD1   . LEU A 1 2097 ? 197.083 233.983 232.649 1.00 0.00  ? 2097 LEU A CD1   1 
ATOM   5029  C CD2   . LEU A 1 2097 ? 195.986 235.838 231.405 1.00 0.00  ? 2097 LEU A CD2   1 
ATOM   5030  N N     . VAL A 1 2098 ? 201.084 237.403 230.792 1.00 0.00  ? 2098 VAL A N     1 
ATOM   5031  C CA    . VAL A 1 2098 ? 202.204 238.274 231.143 1.00 0.00  ? 2098 VAL A CA    1 
ATOM   5032  C C     . VAL A 1 2098 ? 202.204 239.524 230.270 1.00 0.03  ? 2098 VAL A C     1 
ATOM   5033  O O     . VAL A 1 2098 ? 202.543 240.620 230.740 1.00 7.11  ? 2098 VAL A O     1 
ATOM   5034  C CB    . VAL A 1 2098 ? 203.554 237.530 231.073 1.00 4.27  ? 2098 VAL A CB    1 
ATOM   5035  C CG1   . VAL A 1 2098 ? 203.558 236.349 232.018 1.00 5.11  ? 2098 VAL A CG1   1 
ATOM   5036  C CG2   . VAL A 1 2098 ? 203.881 237.090 229.662 1.00 6.77  ? 2098 VAL A CG2   1 
ATOM   5037  N N     . SER A 1 2099 ? 201.810 239.399 228.999 1.00 2.49  ? 2099 SER A N     1 
ATOM   5038  C CA    . SER A 1 2099 ? 201.692 240.585 228.158 1.00 0.00  ? 2099 SER A CA    1 
ATOM   5039  C C     . SER A 1 2099 ? 200.588 241.509 228.660 1.00 0.00  ? 2099 SER A C     1 
ATOM   5040  O O     . SER A 1 2099 ? 200.721 242.734 228.597 1.00 4.47  ? 2099 SER A O     1 
ATOM   5041  C CB    . SER A 1 2099 ? 201.448 240.179 226.706 1.00 0.09  ? 2099 SER A CB    1 
ATOM   5042  O OG    . SER A 1 2099 ? 202.558 239.470 226.185 1.00 3.25  ? 2099 SER A OG    1 
ATOM   5043  N N     . ALA A 1 2100 ? 199.491 240.940 229.163 1.00 0.82  ? 2100 ALA A N     1 
ATOM   5044  C CA    . ALA A 1 2100 ? 198.427 241.756 229.739 1.00 0.00  ? 2100 ALA A CA    1 
ATOM   5045  C C     . ALA A 1 2100 ? 198.909 242.489 230.981 1.00 0.00  ? 2100 ALA A C     1 
ATOM   5046  O O     . ALA A 1 2100 ? 198.542 243.647 231.212 1.00 1.22  ? 2100 ALA A O     1 
ATOM   5047  C CB    . ALA A 1 2100 ? 197.216 240.885 230.070 1.00 0.00  ? 2100 ALA A CB    1 
ATOM   5048  N N     . GLY A 1 2101 ? 199.722 241.825 231.801 1.00 0.00  ? 2101 GLY A N     1 
ATOM   5049  C CA    . GLY A 1 2101 ? 200.319 242.504 232.940 1.00 0.00  ? 2101 GLY A CA    1 
ATOM   5050  C C     . GLY A 1 2101 ? 201.217 243.654 232.526 1.00 0.73  ? 2101 GLY A C     1 
ATOM   5051  O O     . GLY A 1 2101 ? 201.174 244.738 233.118 1.00 0.93  ? 2101 GLY A O     1 
ATOM   5052  N N     . ASN A 1 2102 ? 202.041 243.435 231.497 1.00 0.00  ? 2102 ASN A N     1 
ATOM   5053  C CA    . ASN A 1 2102 ? 202.886 244.513 230.989 1.00 0.00  ? 2102 ASN A CA    1 
ATOM   5054  C C     . ASN A 1 2102 ? 202.047 245.670 230.460 1.00 0.00  ? 2102 ASN A C     1 
ATOM   5055  O O     . ASN A 1 2102 ? 202.376 246.840 230.689 1.00 7.40  ? 2102 ASN A O     1 
ATOM   5056  C CB    . ASN A 1 2102 ? 203.816 243.987 229.896 1.00 0.00  ? 2102 ASN A CB    1 
ATOM   5057  C CG    . ASN A 1 2102 ? 204.757 242.915 230.398 1.00 1.40  ? 2102 ASN A CG    1 
ATOM   5058  O OD1   . ASN A 1 2102 ? 205.080 242.861 231.584 1.00 4.15  ? 2102 ASN A OD1   1 
ATOM   5059  N ND2   . ASN A 1 2102 ? 205.207 242.056 229.494 1.00 2.33  ? 2102 ASN A ND2   1 
ATOM   5060  N N     . VAL A 1 2103 ? 200.960 245.362 229.749 1.00 0.00  ? 2103 VAL A N     1 
ATOM   5061  C CA    . VAL A 1 2103 ? 200.083 246.406 229.226 1.00 0.00  ? 2103 VAL A CA    1 
ATOM   5062  C C     . VAL A 1 2103 ? 199.459 247.201 230.366 1.00 3.39  ? 2103 VAL A C     1 
ATOM   5063  O O     . VAL A 1 2103 ? 199.375 248.433 230.308 1.00 10.01 ? 2103 VAL A O     1 
ATOM   5064  C CB    . VAL A 1 2103 ? 199.007 245.791 228.309 1.00 0.00  ? 2103 VAL A CB    1 
ATOM   5065  C CG1   . VAL A 1 2103 ? 197.940 246.817 227.977 1.00 0.00  ? 2103 VAL A CG1   1 
ATOM   5066  C CG2   . VAL A 1 2103 ? 199.636 245.256 227.037 1.00 0.00  ? 2103 VAL A CG2   1 
ATOM   5067  N N     . LYS A 1 2104 ? 199.004 246.512 231.415 1.00 5.76  ? 2104 LYS A N     1 
ATOM   5068  C CA    . LYS A 1 2104 ? 198.398 247.206 232.548 1.00 0.00  ? 2104 LYS A CA    1 
ATOM   5069  C C     . LYS A 1 2104 ? 199.403 248.115 233.240 1.00 1.95  ? 2104 LYS A C     1 
ATOM   5070  O O     . LYS A 1 2104 ? 199.078 249.253 233.605 1.00 14.76 ? 2104 LYS A O     1 
ATOM   5071  C CB    . LYS A 1 2104 ? 197.823 246.193 233.537 1.00 0.00  ? 2104 LYS A CB    1 
ATOM   5072  C CG    . LYS A 1 2104 ? 197.241 246.813 234.794 1.00 0.00  ? 2104 LYS A CG    1 
ATOM   5073  C CD    . LYS A 1 2104 ? 196.956 245.757 235.844 1.00 3.11  ? 2104 LYS A CD    1 
ATOM   5074  C CE    . LYS A 1 2104 ? 196.270 246.354 237.061 1.00 7.10  ? 2104 LYS A CE    1 
ATOM   5075  N NZ    . LYS A 1 2104 ? 195.029 247.087 236.699 1.00 7.47  ? 2104 LYS A NZ    1 
ATOM   5076  N N     . ARG A 1 2105 ? 200.630 247.628 233.436 1.00 0.24  ? 2105 ARG A N     1 
ATOM   5077  C CA    . ARG A 1 2105 ? 201.653 248.461 234.061 1.00 1.85  ? 2105 ARG A CA    1 
ATOM   5078  C C     . ARG A 1 2105 ? 201.988 249.669 233.196 1.00 5.52  ? 2105 ARG A C     1 
ATOM   5079  O O     . ARG A 1 2105 ? 202.169 250.780 233.710 1.00 8.72  ? 2105 ARG A O     1 
ATOM   5080  C CB    . ARG A 1 2105 ? 202.901 247.633 234.354 1.00 3.45  ? 2105 ARG A CB    1 
ATOM   5081  C CG    . ARG A 1 2105 ? 202.781 246.797 235.611 1.00 0.59  ? 2105 ARG A CG    1 
ATOM   5082  C CD    . ARG A 1 2105 ? 204.075 246.087 235.922 1.00 0.13  ? 2105 ARG A CD    1 
ATOM   5083  N NE    . ARG A 1 2105 ? 204.395 245.050 234.949 1.00 1.01  ? 2105 ARG A NE    1 
ATOM   5084  C CZ    . ARG A 1 2105 ? 203.944 243.805 235.009 1.00 4.04  ? 2105 ARG A CZ    1 
ATOM   5085  N NH1   . ARG A 1 2105 ? 203.119 243.415 235.967 1.00 4.30  ? 2105 ARG A NH1   1 
ATOM   5086  N NH2   . ARG A 1 2105 ? 204.333 242.929 234.088 1.00 4.15  ? 2105 ARG A NH2   1 
ATOM   5087  N N     . GLU A 1 2106 ? 202.067 249.475 231.877 1.00 6.71  ? 2106 GLU A N     1 
ATOM   5088  C CA    . GLU A 1 2106 ? 202.296 250.599 230.976 1.00 5.51  ? 2106 GLU A CA    1 
ATOM   5089  C C     . GLU A 1 2106 ? 201.168 251.619 231.073 1.00 8.99  ? 2106 GLU A C     1 
ATOM   5090  O O     . GLU A 1 2106 ? 201.417 252.829 231.107 1.00 13.84 ? 2106 GLU A O     1 
ATOM   5091  C CB    . GLU A 1 2106 ? 202.440 250.095 229.540 1.00 5.26  ? 2106 GLU A CB    1 
ATOM   5092  C CG    . GLU A 1 2106 ? 202.722 251.183 228.514 1.00 11.54 ? 2106 GLU A CG    1 
ATOM   5093  C CD    . GLU A 1 2106 ? 204.064 251.861 228.715 1.00 10.12 ? 2106 GLU A CD    1 
ATOM   5094  O OE1   . GLU A 1 2106 ? 204.976 251.228 229.288 1.00 9.01  ? 2106 GLU A OE1   1 
ATOM   5095  O OE2   . GLU A 1 2106 ? 204.205 253.033 228.306 1.00 11.67 ? 2106 GLU A OE2   1 
ATOM   5096  N N     . ARG A 1 2107 ? 199.923 251.146 231.135 1.00 4.69  ? 2107 ARG A N     1 
ATOM   5097  C CA    . ARG A 1 2107 ? 198.786 252.054 231.235 1.00 1.51  ? 2107 ARG A CA    1 
ATOM   5098  C C     . ARG A 1 2107 ? 198.843 252.870 232.520 1.00 7.17  ? 2107 ARG A C     1 
ATOM   5099  O O     . ARG A 1 2107 ? 198.645 254.092 232.498 1.00 16.08 ? 2107 ARG A O     1 
ATOM   5100  C CB    . ARG A 1 2107 ? 197.480 251.265 231.165 1.00 0.08  ? 2107 ARG A CB    1 
ATOM   5101  C CG    . ARG A 1 2107 ? 196.874 251.174 229.778 1.00 5.63  ? 2107 ARG A CG    1 
ATOM   5102  C CD    . ARG A 1 2107 ? 196.072 249.893 229.635 1.00 9.12  ? 2107 ARG A CD    1 
ATOM   5103  N NE    . ARG A 1 2107 ? 195.403 249.786 228.344 1.00 5.28  ? 2107 ARG A NE    1 
ATOM   5104  C CZ    . ARG A 1 2107 ? 194.151 250.155 228.115 1.00 5.26  ? 2107 ARG A CZ    1 
ATOM   5105  N NH1   . ARG A 1 2107 ? 193.405 250.693 229.065 1.00 4.37  ? 2107 ARG A NH1   1 
ATOM   5106  N NH2   . ARG A 1 2107 ? 193.635 249.978 226.903 1.00 9.23  ? 2107 ARG A NH2   1 
ATOM   5107  N N     . ILE A 1 2108 ? 199.117 252.215 233.651 1.00 6.63  ? 2108 ILE A N     1 
ATOM   5108  C CA    . ILE A 1 2108 ? 199.108 252.946 234.916 1.00 5.02  ? 2108 ILE A CA    1 
ATOM   5109  C C     . ILE A 1 2108 ? 200.283 253.914 234.991 1.00 13.01 ? 2108 ILE A C     1 
ATOM   5110  O O     . ILE A 1 2108 ? 200.150 255.019 235.529 1.00 18.68 ? 2108 ILE A O     1 
ATOM   5111  C CB    . ILE A 1 2108 ? 199.077 251.991 236.126 1.00 5.46  ? 2108 ILE A CB    1 
ATOM   5112  C CG1   . ILE A 1 2108 ? 200.166 250.932 236.034 1.00 10.47 ? 2108 ILE A CG1   1 
ATOM   5113  C CG2   . ILE A 1 2108 ? 197.719 251.327 236.253 1.00 6.61  ? 2108 ILE A CG2   1 
ATOM   5114  C CD1   . ILE A 1 2108 ? 200.151 249.963 237.190 1.00 9.09  ? 2108 ILE A CD1   1 
ATOM   5115  N N     . GLN A 1 2109 ? 201.450 253.534 234.455 1.00 12.90 ? 2109 GLN A N     1 
ATOM   5116  C CA    . GLN A 1 2109 ? 202.573 254.466 234.511 1.00 11.65 ? 2109 GLN A CA    1 
ATOM   5117  C C     . GLN A 1 2109 ? 202.402 255.612 233.524 1.00 13.79 ? 2109 GLN A C     1 
ATOM   5118  O O     . GLN A 1 2109 ? 202.964 256.693 233.734 1.00 17.75 ? 2109 GLN A O     1 
ATOM   5119  C CB    . GLN A 1 2109 ? 203.902 253.758 234.261 1.00 8.20  ? 2109 GLN A CB    1 
ATOM   5120  C CG    . GLN A 1 2109 ? 204.090 253.167 232.885 1.00 16.28 ? 2109 GLN A CG    1 
ATOM   5121  C CD    . GLN A 1 2109 ? 205.417 252.442 232.765 1.00 20.75 ? 2109 GLN A CD    1 
ATOM   5122  O OE1   . GLN A 1 2109 ? 206.214 252.431 233.704 1.00 20.12 ? 2109 GLN A OE1   1 
ATOM   5123  N NE2   . GLN A 1 2109 ? 205.665 251.839 231.609 1.00 14.71 ? 2109 GLN A NE2   1 
ATOM   5124  N N     . LYS A 1 2110 ? 201.646 255.403 232.443 1.00 12.84 ? 2110 LYS A N     1 
ATOM   5125  C CA    . LYS A 1 2110 ? 201.333 256.511 231.548 1.00 16.30 ? 2110 LYS A CA    1 
ATOM   5126  C C     . LYS A 1 2110 ? 200.332 257.465 232.185 1.00 18.88 ? 2110 LYS A C     1 
ATOM   5127  O O     . LYS A 1 2110 ? 200.453 258.687 232.042 1.00 25.03 ? 2110 LYS A O     1 
ATOM   5128  C CB    . LYS A 1 2110 ? 200.794 255.978 230.222 1.00 16.62 ? 2110 LYS A CB    1 
ATOM   5129  C CG    . LYS A 1 2110 ? 200.559 257.049 229.175 1.00 18.78 ? 2110 LYS A CG    1 
ATOM   5130  C CD    . LYS A 1 2110 ? 199.620 256.558 228.084 1.00 19.89 ? 2110 LYS A CD    1 
ATOM   5131  C CE    . LYS A 1 2110 ? 198.231 256.276 228.632 1.00 18.40 ? 2110 LYS A CE    1 
ATOM   5132  N NZ    . LYS A 1 2110 ? 197.684 257.442 229.378 1.00 21.20 ? 2110 LYS A NZ    1 
ATOM   5133  N N     . ILE A 1 2111 ? 199.333 256.927 232.885 1.00 14.22 ? 2111 ILE A N     1 
ATOM   5134  C CA    . ILE A 1 2111 ? 198.365 257.783 233.565 1.00 16.65 ? 2111 ILE A CA    1 
ATOM   5135  C C     . ILE A 1 2111 ? 199.024 258.536 234.713 1.00 18.50 ? 2111 ILE A C     1 
ATOM   5136  O O     . ILE A 1 2111 ? 198.667 259.684 235.004 1.00 20.92 ? 2111 ILE A O     1 
ATOM   5137  C CB    . ILE A 1 2111 ? 197.158 256.955 234.037 1.00 21.52 ? 2111 ILE A CB    1 
ATOM   5138  C CG1   . ILE A 1 2111 ? 196.430 256.366 232.832 1.00 22.50 ? 2111 ILE A CG1   1 
ATOM   5139  C CG2   . ILE A 1 2111 ? 196.205 257.802 234.864 1.00 22.58 ? 2111 ILE A CG2   1 
ATOM   5140  C CD1   . ILE A 1 2111 ? 195.405 255.348 233.199 1.00 18.19 ? 2111 ILE A CD1   1 
ATOM   5141  N N     . LYS A 1 2112 ? 199.993 257.909 235.384 1.00 19.07 ? 2112 LYS A N     1 
ATOM   5142  C CA    . LYS A 1 2112 ? 200.686 258.578 236.481 1.00 20.21 ? 2112 LYS A CA    1 
ATOM   5143  C C     . LYS A 1 2112 ? 201.378 259.846 235.999 1.00 27.83 ? 2112 LYS A C     1 
ATOM   5144  O O     . LYS A 1 2112 ? 201.327 260.888 236.663 1.00 31.60 ? 2112 LYS A O     1 
ATOM   5145  C CB    . LYS A 1 2112 ? 201.697 257.627 237.123 1.00 21.23 ? 2112 LYS A CB    1 
ATOM   5146  C CG    . LYS A 1 2112 ? 202.857 258.340 237.800 1.00 25.23 ? 2112 LYS A CG    1 
ATOM   5147  C CD    . LYS A 1 2112 ? 204.021 257.405 238.081 1.00 25.56 ? 2112 LYS A CD    1 
ATOM   5148  C CE    . LYS A 1 2112 ? 203.735 256.506 239.268 1.00 27.98 ? 2112 LYS A CE    1 
ATOM   5149  N NZ    . LYS A 1 2112 ? 204.898 255.635 239.585 1.00 29.55 ? 2112 LYS A NZ    1 
ATOM   5150  N N     . ARG A 1 2113 ? 202.019 259.780 234.831 1.00 25.98 ? 2113 ARG A N     1 
ATOM   5151  C CA    . ARG A 1 2113 ? 202.748 260.920 234.273 1.00 26.25 ? 2113 ARG A CA    1 
ATOM   5152  C C     . ARG A 1 2113 ? 201.779 261.790 233.463 1.00 28.55 ? 2113 ARG A C     1 
ATOM   5153  O O     . ARG A 1 2113 ? 202.042 262.233 232.343 1.00 26.93 ? 2113 ARG A O     1 
ATOM   5154  C CB    . ARG A 1 2113 ? 203.966 260.412 233.497 1.00 25.85 ? 2113 ARG A CB    1 
ATOM   5155  C CG    . ARG A 1 2113 ? 203.817 260.103 232.009 1.00 25.56 ? 2113 ARG A CG    1 
ATOM   5156  C CD    . ARG A 1 2113 ? 205.168 259.834 231.371 1.00 25.73 ? 2113 ARG A CD    1 
ATOM   5157  N NE    . ARG A 1 2113 ? 205.732 258.565 231.817 1.00 24.58 ? 2113 ARG A NE    1 
ATOM   5158  C CZ    . ARG A 1 2113 ? 205.865 257.492 231.049 1.00 27.33 ? 2113 ARG A CZ    1 
ATOM   5159  N NH1   . ARG A 1 2113 ? 205.479 257.495 229.784 1.00 25.42 ? 2113 ARG A NH1   1 
ATOM   5160  N NH2   . ARG A 1 2113 ? 206.396 256.388 231.565 1.00 28.20 ? 2113 ARG A NH2   1 
ATOM   5161  N N     . GLU A 1 2114 ? 200.655 262.106 234.097 1.00 30.41 ? 2114 GLU A N     1 
ATOM   5162  C CA    . GLU A 1 2114 ? 199.659 262.987 233.502 1.00 29.20 ? 2114 GLU A CA    1 
ATOM   5163  C C     . GLU A 1 2114 ? 199.140 263.982 234.533 1.00 26.25 ? 2114 GLU A C     1 
ATOM   5164  O O     . GLU A 1 2114 ? 198.601 265.032 234.187 0.00 29.36 ? 2114 GLU A O     1 
ATOM   5165  C CB    . GLU A 1 2114 ? 198.500 262.177 232.921 1.00 30.16 ? 2114 GLU A CB    1 
ATOM   5166  C CG    . GLU A 1 2114 ? 198.649 261.851 231.445 1.00 30.46 ? 2114 GLU A CG    1 
ATOM   5167  C CD    . GLU A 1 2114 ? 197.349 261.390 230.819 1.00 32.67 ? 2114 GLU A CD    1 
ATOM   5168  O OE1   . GLU A 1 2114 ? 196.938 260.240 231.080 1.00 31.68 ? 2114 GLU A OE1   1 
ATOM   5169  O OE2   . GLU A 1 2114 ? 196.737 262.177 230.066 1.00 32.52 ? 2114 GLU A OE2   1 
ATOM   5170  N N     . ILE A 1 2127 ? 197.258 252.522 243.728 1.00 22.60 ? 2127 ILE A N     1 
ATOM   5171  C CA    . ILE A 1 2127 ? 197.174 253.947 243.436 1.00 22.99 ? 2127 ILE A CA    1 
ATOM   5172  C C     . ILE A 1 2127 ? 196.530 254.171 242.073 1.00 23.90 ? 2127 ILE A C     1 
ATOM   5173  O O     . ILE A 1 2127 ? 196.968 253.605 241.071 1.00 26.06 ? 2127 ILE A O     1 
ATOM   5174  C CB    . ILE A 1 2127 ? 198.568 254.616 243.516 1.00 24.36 ? 2127 ILE A CB    1 
ATOM   5175  C CG1   . ILE A 1 2127 ? 198.488 256.086 243.093 1.00 23.75 ? 2127 ILE A CG1   1 
ATOM   5176  C CG2   . ILE A 1 2127 ? 199.596 253.850 242.689 1.00 20.94 ? 2127 ILE A CG2   1 
ATOM   5177  C CD1   . ILE A 1 2127 ? 197.626 256.939 243.999 1.00 21.53 ? 2127 ILE A CD1   1 
ATOM   5178  N N     . ALA A 1 2128 ? 195.481 254.996 242.052 1.00 24.53 ? 2128 ALA A N     1 
ATOM   5179  C CA    . ALA A 1 2128 ? 194.755 255.327 240.826 1.00 24.48 ? 2128 ALA A CA    1 
ATOM   5180  C C     . ALA A 1 2128 ? 194.308 254.063 240.096 1.00 22.74 ? 2128 ALA A C     1 
ATOM   5181  O O     . ALA A 1 2128 ? 194.507 253.903 238.890 1.00 15.26 ? 2128 ALA A O     1 
ATOM   5182  C CB    . ALA A 1 2128 ? 195.598 256.219 239.913 1.00 21.45 ? 2128 ALA A CB    1 
ATOM   5183  N N     . GLU A 1 2129 ? 193.702 253.146 240.852 1.00 24.74 ? 2129 GLU A N     1 
ATOM   5184  C CA    . GLU A 1 2129 ? 193.334 251.831 240.332 1.00 19.17 ? 2129 GLU A CA    1 
ATOM   5185  C C     . GLU A 1 2129 ? 191.851 251.834 239.970 1.00 18.97 ? 2129 GLU A C     1 
ATOM   5186  O O     . GLU A 1 2129 ? 190.988 251.399 240.732 1.00 15.66 ? 2129 GLU A O     1 
ATOM   5187  C CB    . GLU A 1 2129 ? 193.669 250.741 241.346 1.00 21.52 ? 2129 GLU A CB    1 
ATOM   5188  C CG    . GLU A 1 2129 ? 193.367 249.317 240.885 1.00 22.45 ? 2129 GLU A CG    1 
ATOM   5189  C CD    . GLU A 1 2129 ? 193.659 249.068 239.410 1.00 22.27 ? 2129 GLU A CD    1 
ATOM   5190  O OE1   . GLU A 1 2129 ? 192.943 248.243 238.806 1.00 20.52 ? 2129 GLU A OE1   1 
ATOM   5191  O OE2   . GLU A 1 2129 ? 194.636 249.629 238.866 1.00 20.75 ? 2129 GLU A OE2   1 
ATOM   5192  N N     . ASN A 1 2130 ? 191.561 252.336 238.768 1.00 22.22 ? 2130 ASN A N     1 
ATOM   5193  C CA    . ASN A 1 2130 ? 190.199 252.332 238.252 1.00 21.50 ? 2130 ASN A CA    1 
ATOM   5194  C C     . ASN A 1 2130 ? 190.138 251.918 236.787 1.00 19.74 ? 2130 ASN A C     1 
ATOM   5195  O O     . ASN A 1 2130 ? 189.110 252.147 236.137 1.00 16.57 ? 2130 ASN A O     1 
ATOM   5196  C CB    . ASN A 1 2130 ? 189.548 253.711 238.427 1.00 23.04 ? 2130 ASN A CB    1 
ATOM   5197  C CG    . ASN A 1 2130 ? 189.257 254.040 239.880 1.00 24.93 ? 2130 ASN A CG    1 
ATOM   5198  O OD1   . ASN A 1 2130 ? 188.798 253.190 240.642 1.00 22.71 ? 2130 ASN A OD1   1 
ATOM   5199  N ND2   . ASN A 1 2130 ? 189.526 255.280 240.270 1.00 23.22 ? 2130 ASN A ND2   1 
ATOM   5200  N N     . LEU A 1 2131 ? 191.197 251.318 236.249 1.00 15.62 ? 2131 LEU A N     1 
ATOM   5201  C CA    . LEU A 1 2131 ? 191.201 250.927 234.851 1.00 15.38 ? 2131 LEU A CA    1 
ATOM   5202  C C     . LEU A 1 2131 ? 190.298 249.720 234.612 1.00 16.24 ? 2131 LEU A C     1 
ATOM   5203  O O     . LEU A 1 2131 ? 190.117 248.880 235.497 1.00 13.90 ? 2131 LEU A O     1 
ATOM   5204  C CB    . LEU A 1 2131 ? 192.615 250.602 234.385 1.00 12.34 ? 2131 LEU A CB    1 
ATOM   5205  C CG    . LEU A 1 2131 ? 193.569 251.787 234.365 1.00 13.89 ? 2131 LEU A CG    1 
ATOM   5206  C CD1   . LEU A 1 2131 ? 194.967 251.328 234.021 1.00 11.17 ? 2131 LEU A CD1   1 
ATOM   5207  C CD2   . LEU A 1 2131 ? 193.063 252.788 233.351 1.00 17.61 ? 2131 LEU A CD2   1 
ATOM   5208  N N     . PRO A 1 2132 ? 189.717 249.614 233.417 1.00 13.40 ? 2132 PRO A N     1 
ATOM   5209  C CA    . PRO A 1 2132 ? 188.964 248.404 233.068 1.00 12.13 ? 2132 PRO A CA    1 
ATOM   5210  C C     . PRO A 1 2132 ? 189.895 247.242 232.766 1.00 10.59 ? 2132 PRO A C     1 
ATOM   5211  O O     . PRO A 1 2132 ? 190.666 247.289 231.803 1.00 10.37 ? 2132 PRO A O     1 
ATOM   5212  C CB    . PRO A 1 2132 ? 188.167 248.833 231.831 1.00 8.75  ? 2132 PRO A CB    1 
ATOM   5213  C CG    . PRO A 1 2132 ? 188.964 249.939 231.236 1.00 7.12  ? 2132 PRO A CG    1 
ATOM   5214  C CD    . PRO A 1 2132 ? 189.619 250.654 232.378 1.00 11.60 ? 2132 PRO A CD    1 
ATOM   5215  N N     . GLU A 1 2133 ? 189.839 246.197 233.594 1.00 6.15  ? 2133 GLU A N     1 
ATOM   5216  C CA    . GLU A 1 2133 ? 190.763 245.079 233.437 1.00 0.00  ? 2133 GLU A CA    1 
ATOM   5217  C C     . GLU A 1 2133 ? 190.453 244.268 232.186 1.00 1.59  ? 2133 GLU A C     1 
ATOM   5218  O O     . GLU A 1 2133 ? 191.368 243.759 231.530 1.00 4.19  ? 2133 GLU A O     1 
ATOM   5219  C CB    . GLU A 1 2133 ? 190.720 244.184 234.673 1.00 4.69  ? 2133 GLU A CB    1 
ATOM   5220  C CG    . GLU A 1 2133 ? 191.001 244.900 235.980 1.00 8.78  ? 2133 GLU A CG    1 
ATOM   5221  C CD    . GLU A 1 2133 ? 192.433 245.373 236.093 1.00 11.72 ? 2133 GLU A CD    1 
ATOM   5222  O OE1   . GLU A 1 2133 ? 193.312 244.781 235.438 1.00 9.30  ? 2133 GLU A OE1   1 
ATOM   5223  O OE2   . GLU A 1 2133 ? 192.683 246.336 236.844 1.00 17.55 ? 2133 GLU A OE2   1 
ATOM   5224  N N     . GLN A 1 2134 ? 189.169 244.123 231.847 1.00 5.03  ? 2134 GLN A N     1 
ATOM   5225  C CA    . GLN A 1 2134 ? 188.795 243.292 230.707 1.00 1.73  ? 2134 GLN A CA    1 
ATOM   5226  C C     . GLN A 1 2134 ? 189.356 243.849 229.406 1.00 3.58  ? 2134 GLN A C     1 
ATOM   5227  O O     . GLN A 1 2134 ? 189.905 243.101 228.592 1.00 4.67  ? 2134 GLN A O     1 
ATOM   5228  C CB    . GLN A 1 2134 ? 187.276 243.161 230.628 1.00 3.83  ? 2134 GLN A CB    1 
ATOM   5229  C CG    . GLN A 1 2134 ? 186.681 242.323 231.743 1.00 0.67  ? 2134 GLN A CG    1 
ATOM   5230  C CD    . GLN A 1 2134 ? 185.192 242.108 231.587 1.00 1.74  ? 2134 GLN A CD    1 
ATOM   5231  O OE1   . GLN A 1 2134 ? 184.566 242.644 230.675 1.00 5.72  ? 2134 GLN A OE1   1 
ATOM   5232  N NE2   . GLN A 1 2134 ? 184.611 241.336 232.495 1.00 4.71  ? 2134 GLN A NE2   1 
ATOM   5233  N N     . GLU A 1 2135 ? 189.245 245.164 229.199 1.00 7.66  ? 2135 GLU A N     1 
ATOM   5234  C CA    . GLU A 1 2135 ? 189.815 245.781 228.005 1.00 4.16  ? 2135 GLU A CA    1 
ATOM   5235  C C     . GLU A 1 2135 ? 191.328 245.626 227.931 1.00 0.00  ? 2135 GLU A C     1 
ATOM   5236  O O     . GLU A 1 2135 ? 191.869 245.511 226.828 1.00 1.27  ? 2135 GLU A O     1 
ATOM   5237  C CB    . GLU A 1 2135 ? 189.441 247.262 227.943 1.00 5.04  ? 2135 GLU A CB    1 
ATOM   5238  C CG    . GLU A 1 2135 ? 188.040 247.539 227.415 1.00 8.25  ? 2135 GLU A CG    1 
ATOM   5239  C CD    . GLU A 1 2135 ? 187.009 247.684 228.514 1.00 18.23 ? 2135 GLU A CD    1 
ATOM   5240  O OE1   . GLU A 1 2135 ? 187.166 247.032 229.566 1.00 10.88 ? 2135 GLU A OE1   1 
ATOM   5241  O OE2   . GLU A 1 2135 ? 186.047 248.458 228.328 1.00 15.96 ? 2135 GLU A OE2   1 
ATOM   5242  N N     . ILE A 1 2136 ? 192.020 245.621 229.070 1.00 0.00  ? 2136 ILE A N     1 
ATOM   5243  C CA    . ILE A 1 2136 ? 193.455 245.364 229.052 1.00 0.84  ? 2136 ILE A CA    1 
ATOM   5244  C C     . ILE A 1 2136 ? 193.745 243.918 228.669 1.00 1.02  ? 2136 ILE A C     1 
ATOM   5245  O O     . ILE A 1 2136 ? 194.702 243.648 227.936 1.00 3.16  ? 2136 ILE A O     1 
ATOM   5246  C CB    . ILE A 1 2136 ? 194.080 245.721 230.410 1.00 2.34  ? 2136 ILE A CB    1 
ATOM   5247  C CG1   . ILE A 1 2136 ? 193.699 247.146 230.814 1.00 2.40  ? 2136 ILE A CG1   1 
ATOM   5248  C CG2   . ILE A 1 2136 ? 195.588 245.551 230.372 1.00 0.00  ? 2136 ILE A CG2   1 
ATOM   5249  C CD1   . ILE A 1 2136 ? 194.343 247.604 232.098 1.00 5.13  ? 2136 ILE A CD1   1 
ATOM   5250  N N     . LEU A 1 2137 ? 192.942 242.970 229.156 1.00 2.70  ? 2137 LEU A N     1 
ATOM   5251  C CA    . LEU A 1 2137 ? 193.119 241.577 228.760 1.00 0.66  ? 2137 LEU A CA    1 
ATOM   5252  C C     . LEU A 1 2137 ? 192.841 241.372 227.278 1.00 2.52  ? 2137 LEU A C     1 
ATOM   5253  O O     . LEU A 1 2137 ? 193.574 240.634 226.611 1.00 6.71  ? 2137 LEU A O     1 
ATOM   5254  C CB    . LEU A 1 2137 ? 192.214 240.673 229.596 1.00 3.39  ? 2137 LEU A CB    1 
ATOM   5255  C CG    . LEU A 1 2137 ? 192.577 239.188 229.636 1.00 3.43  ? 2137 LEU A CG    1 
ATOM   5256  C CD1   . LEU A 1 2137 ? 194.049 238.992 229.959 1.00 1.03  ? 2137 LEU A CD1   1 
ATOM   5257  C CD2   . LEU A 1 2137 ? 191.704 238.452 230.636 1.00 2.39  ? 2137 LEU A CD2   1 
ATOM   5258  N N     . ILE A 1 2138 ? 191.795 242.008 226.747 1.00 4.05  ? 2138 ILE A N     1 
ATOM   5259  C CA    . ILE A 1 2138 ? 191.449 241.858 225.338 1.00 0.00  ? 2138 ILE A CA    1 
ATOM   5260  C C     . ILE A 1 2138 ? 192.518 242.423 224.412 1.00 1.63  ? 2138 ILE A C     1 
ATOM   5261  O O     . ILE A 1 2138 ? 192.808 241.813 223.373 1.00 8.08  ? 2138 ILE A O     1 
ATOM   5262  C CB    . ILE A 1 2138 ? 190.098 242.528 225.033 1.00 0.84  ? 2138 ILE A CB    1 
ATOM   5263  C CG1   . ILE A 1 2138 ? 189.013 241.921 225.913 1.00 5.88  ? 2138 ILE A CG1   1 
ATOM   5264  C CG2   . ILE A 1 2138 ? 189.734 242.375 223.570 1.00 2.99  ? 2138 ILE A CG2   1 
ATOM   5265  C CD1   . ILE A 1 2138 ? 188.852 240.458 225.717 1.00 5.84  ? 2138 ILE A CD1   1 
ATOM   5266  N N     . GLN A 1 2139 ? 193.111 243.565 224.756 1.00 0.82  ? 2139 GLN A N     1 
ATOM   5267  C CA    . GLN A 1 2139 ? 194.191 244.119 223.951 1.00 0.00  ? 2139 GLN A CA    1 
ATOM   5268  C C     . GLN A 1 2139 ? 195.366 243.158 223.865 1.00 0.09  ? 2139 GLN A C     1 
ATOM   5269  O O     . GLN A 1 2139 ? 195.960 242.993 222.795 1.00 2.51  ? 2139 GLN A O     1 
ATOM   5270  C CB    . GLN A 1 2139 ? 194.642 245.457 224.534 1.00 0.53  ? 2139 GLN A CB    1 
ATOM   5271  C CG    . GLN A 1 2139 ? 195.922 245.992 223.925 1.00 0.70  ? 2139 GLN A CG    1 
ATOM   5272  C CD    . GLN A 1 2139 ? 196.441 247.211 224.648 1.00 3.17  ? 2139 GLN A CD    1 
ATOM   5273  O OE1   . GLN A 1 2139 ? 195.711 247.860 225.396 1.00 3.95  ? 2139 GLN A OE1   1 
ATOM   5274  N NE2   . GLN A 1 2139 ? 197.709 247.532 224.432 1.00 3.47  ? 2139 GLN A NE2   1 
ATOM   5275  N N     . SER A 1 2140 ? 195.713 242.518 224.982 1.00 0.98  ? 2140 SER A N     1 
ATOM   5276  C CA    . SER A 1 2140 ? 196.810 241.557 224.978 1.00 1.63  ? 2140 SER A CA    1 
ATOM   5277  C C     . SER A 1 2140 ? 196.486 240.346 224.113 1.00 1.91  ? 2140 SER A C     1 
ATOM   5278  O O     . SER A 1 2140 ? 197.363 239.824 223.415 1.00 6.67  ? 2140 SER A O     1 
ATOM   5279  C CB    . SER A 1 2140 ? 197.125 241.126 226.406 1.00 0.87  ? 2140 SER A CB    1 
ATOM   5280  O OG    . SER A 1 2140 ? 198.377 240.475 226.468 1.00 6.72  ? 2140 SER A OG    1 
ATOM   5281  N N     . VAL A 1 2141 ? 195.240 239.874 224.161 1.00 2.20  ? 2141 VAL A N     1 
ATOM   5282  C CA    . VAL A 1 2141 ? 194.833 238.757 223.312 1.00 0.00  ? 2141 VAL A CA    1 
ATOM   5283  C C     . VAL A 1 2141 ? 194.918 239.149 221.844 1.00 0.00  ? 2141 VAL A C     1 
ATOM   5284  O O     . VAL A 1 2141 ? 195.465 238.413 221.015 1.00 3.95  ? 2141 VAL A O     1 
ATOM   5285  C CB    . VAL A 1 2141 ? 193.415 238.289 223.686 1.00 0.00  ? 2141 VAL A CB    1 
ATOM   5286  C CG1   . VAL A 1 2141 ? 192.875 237.338 222.635 1.00 0.00  ? 2141 VAL A CG1   1 
ATOM   5287  C CG2   . VAL A 1 2141 ? 193.420 237.629 225.046 1.00 0.33  ? 2141 VAL A CG2   1 
ATOM   5288  N N     . CYS A 1 2142 ? 194.388 240.324 221.504 1.00 0.15  ? 2142 CYS A N     1 
ATOM   5289  C CA    . CYS A 1 2142 ? 194.318 240.757 220.116 1.00 0.00  ? 2142 CYS A CA    1 
ATOM   5290  C C     . CYS A 1 2142 ? 195.663 241.196 219.555 1.00 0.00  ? 2142 CYS A C     1 
ATOM   5291  O O     . CYS A 1 2142 ? 195.862 241.112 218.339 1.00 2.66  ? 2142 CYS A O     1 
ATOM   5292  C CB    . CYS A 1 2142 ? 193.307 241.893 219.983 1.00 1.63  ? 2142 CYS A CB    1 
ATOM   5293  S SG    . CYS A 1 2142 ? 191.591 241.375 220.137 1.00 0.37  ? 2142 CYS A SG    1 
ATOM   5294  N N     . GLU A 1 2143 ? 196.589 241.649 220.391 1.00 0.00  ? 2143 GLU A N     1 
ATOM   5295  C CA    . GLU A 1 2143 ? 197.910 242.032 219.917 1.00 0.00  ? 2143 GLU A CA    1 
ATOM   5296  C C     . GLU A 1 2143 ? 198.811 240.830 219.674 1.00 2.32  ? 2143 GLU A C     1 
ATOM   5297  O O     . GLU A 1 2143 ? 199.925 240.999 219.166 1.00 9.86  ? 2143 GLU A O     1 
ATOM   5298  C CB    . GLU A 1 2143 ? 198.570 242.998 220.908 1.00 0.00  ? 2143 GLU A CB    1 
ATOM   5299  C CG    . GLU A 1 2143 ? 199.417 242.336 221.980 1.00 2.25  ? 2143 GLU A CG    1 
ATOM   5300  C CD    . GLU A 1 2143 ? 199.933 243.326 223.007 1.00 9.17  ? 2143 GLU A CD    1 
ATOM   5301  O OE1   . GLU A 1 2143 ? 199.971 244.536 222.701 1.00 11.20 ? 2143 GLU A OE1   1 
ATOM   5302  O OE2   . GLU A 1 2143 ? 200.301 242.895 224.119 1.00 7.58  ? 2143 GLU A OE2   1 
ATOM   5303  N N     . THR A 1 2144 ? 198.351 239.631 220.001 1.00 0.27  ? 2144 THR A N     1 
ATOM   5304  C CA    . THR A 1 2144 ? 199.103 238.399 219.793 1.00 0.51  ? 2144 THR A CA    1 
ATOM   5305  C C     . THR A 1 2144 ? 198.401 237.428 218.856 1.00 0.20  ? 2144 THR A C     1 
ATOM   5306  O O     . THR A 1 2144 ? 199.064 236.785 218.040 1.00 5.62  ? 2144 THR A O     1 
ATOM   5307  C CB    . THR A 1 2144 ? 199.373 237.715 221.147 1.00 1.07  ? 2144 THR A CB    1 
ATOM   5308  O OG1   . THR A 1 2144 ? 200.038 238.632 222.024 1.00 1.04  ? 2144 THR A OG1   1 
ATOM   5309  C CG2   . THR A 1 2144 ? 200.243 236.480 220.968 1.00 4.36  ? 2144 THR A CG2   1 
ATOM   5310  N N     . MET A 1 2145 ? 197.076 237.315 218.940 1.00 0.00  ? 2145 MET A N     1 
ATOM   5311  C CA    . MET A 1 2145 ? 196.356 236.323 218.151 1.00 0.00  ? 2145 MET A CA    1 
ATOM   5312  C C     . MET A 1 2145 ? 195.934 236.842 216.781 1.00 0.00  ? 2145 MET A C     1 
ATOM   5313  O O     . MET A 1 2145 ? 195.927 236.075 215.814 1.00 0.53  ? 2145 MET A O     1 
ATOM   5314  C CB    . MET A 1 2145 ? 195.133 235.828 218.925 1.00 0.00  ? 2145 MET A CB    1 
ATOM   5315  C CG    . MET A 1 2145 ? 195.499 235.078 220.191 1.00 0.75  ? 2145 MET A CG    1 
ATOM   5316  S SD    . MET A 1 2145 ? 196.414 233.564 219.851 1.00 19.09 ? 2145 MET A SD    1 
ATOM   5317  C CE    . MET A 1 2145 ? 196.884 233.074 221.507 1.00 7.40  ? 2145 MET A CE    1 
ATOM   5318  N N     . VAL A 1 2146 ? 195.574 238.123 216.676 1.00 0.00  ? 2146 VAL A N     1 
ATOM   5319  C CA    . VAL A 1 2146 ? 195.140 238.669 215.387 1.00 1.08  ? 2146 VAL A CA    1 
ATOM   5320  C C     . VAL A 1 2146 ? 196.212 238.549 214.307 1.00 5.25  ? 2146 VAL A C     1 
ATOM   5321  O O     . VAL A 1 2146 ? 195.870 238.182 213.171 1.00 8.67  ? 2146 VAL A O     1 
ATOM   5322  C CB    . VAL A 1 2146 ? 194.638 240.113 215.566 1.00 0.00  ? 2146 VAL A CB    1 
ATOM   5323  C CG1   . VAL A 1 2146 ? 194.344 240.745 214.217 1.00 1.82  ? 2146 VAL A CG1   1 
ATOM   5324  C CG2   . VAL A 1 2146 ? 193.395 240.132 216.433 1.00 0.00  ? 2146 VAL A CG2   1 
ATOM   5325  N N     . PRO A 1 2147 ? 197.493 238.848 214.565 1.00 2.23  ? 2147 PRO A N     1 
ATOM   5326  C CA    . PRO A 1 2147 ? 198.489 238.700 213.490 1.00 2.09  ? 2147 PRO A CA    1 
ATOM   5327  C C     . PRO A 1 2147 ? 198.562 237.302 212.902 1.00 2.17  ? 2147 PRO A C     1 
ATOM   5328  O O     . PRO A 1 2147 ? 198.804 237.163 211.698 1.00 3.70  ? 2147 PRO A O     1 
ATOM   5329  C CB    . PRO A 1 2147 ? 199.803 239.091 214.179 1.00 0.24  ? 2147 PRO A CB    1 
ATOM   5330  C CG    . PRO A 1 2147 ? 199.390 240.013 215.249 1.00 0.90  ? 2147 PRO A CG    1 
ATOM   5331  C CD    . PRO A 1 2147 ? 198.089 239.480 215.756 1.00 0.00  ? 2147 PRO A CD    1 
ATOM   5332  N N     . LYS A 1 2148 ? 198.360 236.260 213.706 1.00 1.79  ? 2148 LYS A N     1 
ATOM   5333  C CA    . LYS A 1 2148 ? 198.388 234.893 213.206 1.00 0.74  ? 2148 LYS A CA    1 
ATOM   5334  C C     . LYS A 1 2148 ? 197.074 234.458 212.574 1.00 0.00  ? 2148 LYS A C     1 
ATOM   5335  O O     . LYS A 1 2148 ? 197.033 233.404 211.932 1.00 2.24  ? 2148 LYS A O     1 
ATOM   5336  C CB    . LYS A 1 2148 ? 198.746 233.921 214.334 1.00 0.00  ? 2148 LYS A CB    1 
ATOM   5337  C CG    . LYS A 1 2148 ? 199.918 234.359 215.186 1.00 0.00  ? 2148 LYS A CG    1 
ATOM   5338  C CD    . LYS A 1 2148 ? 200.050 233.496 216.426 1.00 0.00  ? 2148 LYS A CD    1 
ATOM   5339  C CE    . LYS A 1 2148 ? 201.304 233.849 217.200 1.00 3.69  ? 2148 LYS A CE    1 
ATOM   5340  N NZ    . LYS A 1 2148 ? 201.667 235.282 217.029 1.00 7.38  ? 2148 LYS A NZ    1 
ATOM   5341  N N     . LEU A 1 2149 ? 196.010 235.234 212.734 1.00 0.00  ? 2149 LEU A N     1 
ATOM   5342  C CA    . LEU A 1 2149 ? 194.699 234.830 212.253 1.00 0.00  ? 2149 LEU A CA    1 
ATOM   5343  C C     . LEU A 1 2149 ? 194.608 234.958 210.740 1.00 2.00  ? 2149 LEU A C     1 
ATOM   5344  O O     . LEU A 1 2149 ? 195.135 235.903 210.148 1.00 11.59 ? 2149 LEU A O     1 
ATOM   5345  C CB    . LEU A 1 2149 ? 193.609 235.678 212.902 1.00 0.72  ? 2149 LEU A CB    1 
ATOM   5346  C CG    . LEU A 1 2149 ? 193.213 235.317 214.329 1.00 0.00  ? 2149 LEU A CG    1 
ATOM   5347  C CD1   . LEU A 1 2149 ? 191.959 236.065 214.699 1.00 0.00  ? 2149 LEU A CD1   1 
ATOM   5348  C CD2   . LEU A 1 2149 ? 193.017 233.824 214.481 1.00 0.37  ? 2149 LEU A CD2   1 
ATOM   5349  N N     . VAL A 1 2150 ? 193.927 234.000 210.118 1.00 0.34  ? 2150 VAL A N     1 
ATOM   5350  C CA    . VAL A 1 2150 ? 193.597 234.090 208.701 1.00 0.93  ? 2150 VAL A CA    1 
ATOM   5351  C C     . VAL A 1 2150 ? 192.398 235.019 208.568 1.00 2.74  ? 2150 VAL A C     1 
ATOM   5352  O O     . VAL A 1 2150 ? 191.731 235.326 209.562 1.00 2.81  ? 2150 VAL A O     1 
ATOM   5353  C CB    . VAL A 1 2150 ? 193.318 232.703 208.096 1.00 0.21  ? 2150 VAL A CB    1 
ATOM   5354  C CG1   . VAL A 1 2150 ? 194.429 231.734 208.464 1.00 0.56  ? 2150 VAL A CG1   1 
ATOM   5355  C CG2   . VAL A 1 2150 ? 191.977 232.181 208.566 1.00 2.04  ? 2150 VAL A CG2   1 
ATOM   5356  N N     . ALA A 1 2151 ? 192.119 235.477 207.345 1.00 4.32  ? 2151 ALA A N     1 
ATOM   5357  C CA    . ALA A 1 2151 ? 191.087 236.492 207.153 1.00 3.76  ? 2151 ALA A CA    1 
ATOM   5358  C C     . ALA A 1 2151 ? 189.709 235.992 207.560 1.00 3.46  ? 2151 ALA A C     1 
ATOM   5359  O O     . ALA A 1 2151 ? 188.859 236.788 207.973 1.00 4.30  ? 2151 ALA A O     1 
ATOM   5360  C CB    . ALA A 1 2151 ? 191.070 236.957 205.698 1.00 5.46  ? 2151 ALA A CB    1 
ATOM   5361  N N     . GLU A 1 2152 ? 189.466 234.686 207.447 1.00 0.00  ? 2152 GLU A N     1 
ATOM   5362  C CA    . GLU A 1 2152 ? 188.173 234.138 207.843 1.00 1.84  ? 2152 GLU A CA    1 
ATOM   5363  C C     . GLU A 1 2152 ? 188.006 234.146 209.358 1.00 7.54  ? 2152 GLU A C     1 
ATOM   5364  O O     . GLU A 1 2152 ? 186.901 234.370 209.865 1.00 6.64  ? 2152 GLU A O     1 
ATOM   5365  C CB    . GLU A 1 2152 ? 188.015 232.720 207.294 1.00 0.00  ? 2152 GLU A CB    1 
ATOM   5366  C CG    . GLU A 1 2152 ? 188.329 232.573 205.810 1.00 5.96  ? 2152 GLU A CG    1 
ATOM   5367  C CD    . GLU A 1 2152 ? 189.807 232.362 205.533 1.00 9.70  ? 2152 GLU A CD    1 
ATOM   5368  O OE1   . GLU A 1 2152 ? 190.166 231.306 204.970 1.00 7.72  ? 2152 GLU A OE1   1 
ATOM   5369  O OE2   . GLU A 1 2152 ? 190.609 233.261 205.860 1.00 6.34  ? 2152 GLU A OE2   1 
ATOM   5370  N N     . ASP A 1 2153 ? 189.092 233.902 210.096 1.00 5.57  ? 2153 ASP A N     1 
ATOM   5371  C CA    . ASP A 1 2153 ? 189.022 233.811 211.549 1.00 0.00  ? 2153 ASP A CA    1 
ATOM   5372  C C     . ASP A 1 2153 ? 188.980 235.166 212.238 1.00 1.15  ? 2153 ASP A C     1 
ATOM   5373  O O     . ASP A 1 2153 ? 188.631 235.225 213.421 1.00 1.37  ? 2153 ASP A O     1 
ATOM   5374  C CB    . ASP A 1 2153 ? 190.214 233.018 212.084 1.00 1.28  ? 2153 ASP A CB    1 
ATOM   5375  C CG    . ASP A 1 2153 ? 190.284 231.620 211.517 1.00 0.35  ? 2153 ASP A CG    1 
ATOM   5376  O OD1   . ASP A 1 2153 ? 189.323 231.202 210.842 1.00 4.88  ? 2153 ASP A OD1   1 
ATOM   5377  O OD2   . ASP A 1 2153 ? 191.304 230.940 211.745 1.00 0.00  ? 2153 ASP A OD2   1 
ATOM   5378  N N     . ILE A 1 2154 ? 189.339 236.248 211.545 1.00 6.01  ? 2154 ILE A N     1 
ATOM   5379  C CA    . ILE A 1 2154 ? 189.382 237.559 212.196 1.00 4.98  ? 2154 ILE A CA    1 
ATOM   5380  C C     . ILE A 1 2154 ? 188.010 238.001 212.693 1.00 3.19  ? 2154 ILE A C     1 
ATOM   5381  O O     . ILE A 1 2154 ? 187.900 238.378 213.871 1.00 5.94  ? 2154 ILE A O     1 
ATOM   5382  C CB    . ILE A 1 2154 ? 190.047 238.591 211.268 1.00 1.12  ? 2154 ILE A CB    1 
ATOM   5383  C CG1   . ILE A 1 2154 ? 191.540 238.294 211.129 1.00 0.00  ? 2154 ILE A CG1   1 
ATOM   5384  C CG2   . ILE A 1 2154 ? 189.839 239.995 211.806 1.00 1.19  ? 2154 ILE A CG2   1 
ATOM   5385  C CD1   . ILE A 1 2154 ? 192.250 239.179 210.134 1.00 3.64  ? 2154 ILE A CD1   1 
ATOM   5386  N N     . PRO A 1 2155 ? 186.942 237.985 211.886 1.00 2.52  ? 2155 PRO A N     1 
ATOM   5387  C CA    . PRO A 1 2155 ? 185.615 238.282 212.451 1.00 2.61  ? 2155 PRO A CA    1 
ATOM   5388  C C     . PRO A 1 2155 ? 185.161 237.270 213.489 1.00 6.69  ? 2155 PRO A C     1 
ATOM   5389  O O     . PRO A 1 2155 ? 184.458 237.647 214.436 1.00 9.72  ? 2155 PRO A O     1 
ATOM   5390  C CB    . PRO A 1 2155 ? 184.700 238.278 211.219 1.00 4.65  ? 2155 PRO A CB    1 
ATOM   5391  C CG    . PRO A 1 2155 ? 185.401 237.417 210.242 1.00 6.46  ? 2155 PRO A CG    1 
ATOM   5392  C CD    . PRO A 1 2155 ? 186.854 237.711 210.440 1.00 2.88  ? 2155 PRO A CD    1 
ATOM   5393  N N     . LEU A 1 2156 ? 185.541 235.998 213.342 1.00 4.50  ? 2156 LEU A N     1 
ATOM   5394  C CA    . LEU A 1 2156 ? 185.168 234.982 214.319 1.00 0.37  ? 2156 LEU A CA    1 
ATOM   5395  C C     . LEU A 1 2156 ? 185.783 235.261 215.682 1.00 1.67  ? 2156 LEU A C     1 
ATOM   5396  O O     . LEU A 1 2156 ? 185.130 235.058 216.712 1.00 8.43  ? 2156 LEU A O     1 
ATOM   5397  C CB    . LEU A 1 2156 ? 185.588 233.596 213.829 1.00 0.55  ? 2156 LEU A CB    1 
ATOM   5398  C CG    . LEU A 1 2156 ? 184.577 232.814 212.994 1.00 2.45  ? 2156 LEU A CG    1 
ATOM   5399  C CD1   . LEU A 1 2156 ? 185.159 231.474 212.591 1.00 0.06  ? 2156 LEU A CD1   1 
ATOM   5400  C CD2   . LEU A 1 2156 ? 183.284 232.627 213.765 1.00 7.14  ? 2156 LEU A CD2   1 
ATOM   5401  N N     . LEU A 1 2157 ? 187.038 235.714 215.709 1.00 1.06  ? 2157 LEU A N     1 
ATOM   5402  C CA    . LEU A 1 2157 ? 187.682 236.010 216.983 1.00 1.09  ? 2157 LEU A CA    1 
ATOM   5403  C C     . LEU A 1 2157 ? 186.940 237.104 217.732 1.00 3.42  ? 2157 LEU A C     1 
ATOM   5404  O O     . LEU A 1 2157 ? 186.724 236.998 218.943 1.00 8.02  ? 2157 LEU A O     1 
ATOM   5405  C CB    . LEU A 1 2157 ? 189.134 236.419 216.763 1.00 0.00  ? 2157 LEU A CB    1 
ATOM   5406  C CG    . LEU A 1 2157 ? 189.920 236.660 218.052 1.00 0.00  ? 2157 LEU A CG    1 
ATOM   5407  C CD1   . LEU A 1 2157 ? 190.461 235.350 218.592 1.00 3.48  ? 2157 LEU A CD1   1 
ATOM   5408  C CD2   . LEU A 1 2157 ? 191.037 237.664 217.838 1.00 4.30  ? 2157 LEU A CD2   1 
ATOM   5409  N N     . PHE A 1 2158 ? 186.532 238.162 217.032 1.00 0.80  ? 2158 PHE A N     1 
ATOM   5410  C CA    . PHE A 1 2158 ? 185.831 239.245 217.708 1.00 0.00  ? 2158 PHE A CA    1 
ATOM   5411  C C     . PHE A 1 2158 ? 184.396 238.869 218.044 1.00 1.05  ? 2158 PHE A C     1 
ATOM   5412  O O     . PHE A 1 2158 ? 183.846 239.371 219.029 1.00 6.32  ? 2158 PHE A O     1 
ATOM   5413  C CB    . PHE A 1 2158 ? 185.900 240.517 216.867 1.00 0.07  ? 2158 PHE A CB    1 
ATOM   5414  C CG    . PHE A 1 2158 ? 187.289 241.067 216.738 1.00 0.06  ? 2158 PHE A CG    1 
ATOM   5415  C CD1   . PHE A 1 2158 ? 187.865 241.768 217.783 1.00 0.17  ? 2158 PHE A CD1   1 
ATOM   5416  C CD2   . PHE A 1 2158 ? 188.029 240.864 215.590 1.00 2.58  ? 2158 PHE A CD2   1 
ATOM   5417  C CE1   . PHE A 1 2158 ? 189.145 242.268 217.679 1.00 0.00  ? 2158 PHE A CE1   1 
ATOM   5418  C CE2   . PHE A 1 2158 ? 189.312 241.361 215.481 1.00 5.34  ? 2158 PHE A CE2   1 
ATOM   5419  C CZ    . PHE A 1 2158 ? 189.870 242.064 216.527 1.00 0.25  ? 2158 PHE A CZ    1 
ATOM   5420  N N     . SER A 1 2159 ? 183.780 237.973 217.269 1.00 0.00  ? 2159 SER A N     1 
ATOM   5421  C CA    . SER A 1 2159 ? 182.486 237.434 217.678 1.00 1.73  ? 2159 SER A CA    1 
ATOM   5422  C C     . SER A 1 2159 ? 182.607 236.659 218.985 1.00 0.88  ? 2159 SER A C     1 
ATOM   5423  O O     . SER A 1 2159 ? 181.792 236.831 219.902 1.00 1.54  ? 2159 SER A O     1 
ATOM   5424  C CB    . SER A 1 2159 ? 181.916 236.544 216.575 1.00 3.13  ? 2159 SER A CB    1 
ATOM   5425  O OG    . SER A 1 2159 ? 180.849 235.754 217.064 1.00 8.63  ? 2159 SER A OG    1 
ATOM   5426  N N     . LEU A 1 2160 ? 183.637 235.819 219.100 1.00 0.00  ? 2160 LEU A N     1 
ATOM   5427  C CA    . LEU A 1 2160 ? 183.868 235.089 220.343 1.00 0.00  ? 2160 LEU A CA    1 
ATOM   5428  C C     . LEU A 1 2160 ? 184.216 236.038 221.484 1.00 0.91  ? 2160 LEU A C     1 
ATOM   5429  O O     . LEU A 1 2160 ? 183.843 235.796 222.638 1.00 10.01 ? 2160 LEU A O     1 
ATOM   5430  C CB    . LEU A 1 2160 ? 184.978 234.059 220.147 1.00 0.00  ? 2160 LEU A CB    1 
ATOM   5431  C CG    . LEU A 1 2160 ? 184.727 232.986 219.088 1.00 0.79  ? 2160 LEU A CG    1 
ATOM   5432  C CD1   . LEU A 1 2160 ? 185.857 231.975 219.074 1.00 0.00  ? 2160 LEU A CD1   1 
ATOM   5433  C CD2   . LEU A 1 2160 ? 183.391 232.304 219.321 1.00 4.44  ? 2160 LEU A CD2   1 
ATOM   5434  N N     . LEU A 1 2161 ? 184.945 237.113 221.181 1.00 0.63  ? 2161 LEU A N     1 
ATOM   5435  C CA    . LEU A 1 2161 ? 185.280 238.101 222.200 1.00 0.00  ? 2161 LEU A CA    1 
ATOM   5436  C C     . LEU A 1 2161 ? 184.030 238.794 222.722 1.00 1.41  ? 2161 LEU A C     1 
ATOM   5437  O O     . LEU A 1 2161 ? 183.874 238.980 223.933 1.00 3.70  ? 2161 LEU A O     1 
ATOM   5438  C CB    . LEU A 1 2161 ? 186.258 239.124 221.627 1.00 0.00  ? 2161 LEU A CB    1 
ATOM   5439  C CG    . LEU A 1 2161 ? 187.717 238.685 221.534 1.00 0.00  ? 2161 LEU A CG    1 
ATOM   5440  C CD1   . LEU A 1 2161 ? 188.528 239.710 220.772 1.00 0.67  ? 2161 LEU A CD1   1 
ATOM   5441  C CD2   . LEU A 1 2161 ? 188.300 238.456 222.907 1.00 0.00  ? 2161 LEU A CD2   1 
ATOM   5442  N N     . SER A 1 2162 ? 183.129 239.190 221.822 1.00 2.75  ? 2162 SER A N     1 
ATOM   5443  C CA    . SER A 1 2162 ? 181.858 239.769 222.234 1.00 3.33  ? 2162 SER A CA    1 
ATOM   5444  C C     . SER A 1 2162 ? 180.960 238.761 222.933 1.00 2.93  ? 2162 SER A C     1 
ATOM   5445  O O     . SER A 1 2162 ? 180.059 239.167 223.673 1.00 6.77  ? 2162 SER A O     1 
ATOM   5446  C CB    . SER A 1 2162 ? 181.133 240.361 221.024 1.00 3.63  ? 2162 SER A CB    1 
ATOM   5447  O OG    . SER A 1 2162 ? 180.325 239.388 220.386 1.00 8.65  ? 2162 SER A OG    1 
ATOM   5448  N N     . ASP A 1 2163 ? 181.172 237.466 222.706 1.00 2.24  ? 2163 ASP A N     1 
ATOM   5449  C CA    . ASP A 1 2163 ? 180.461 236.428 223.444 1.00 2.17  ? 2163 ASP A CA    1 
ATOM   5450  C C     . ASP A 1 2163 ? 180.957 236.282 224.878 1.00 1.88  ? 2163 ASP A C     1 
ATOM   5451  O O     . ASP A 1 2163 ? 180.162 236.345 225.818 1.00 10.66 ? 2163 ASP A O     1 
ATOM   5452  C CB    . ASP A 1 2163 ? 180.581 235.083 222.719 1.00 1.59  ? 2163 ASP A CB    1 
ATOM   5453  C CG    . ASP A 1 2163 ? 179.458 234.854 221.734 1.00 10.50 ? 2163 ASP A CG    1 
ATOM   5454  O OD1   . ASP A 1 2163 ? 178.459 235.595 221.803 1.00 12.62 ? 2163 ASP A OD1   1 
ATOM   5455  O OD2   . ASP A 1 2163 ? 179.568 233.933 220.898 1.00 12.28 ? 2163 ASP A OD2   1 
ATOM   5456  N N     . VAL A 1 2164 ? 182.262 236.081 225.064 1.00 3.45  ? 2164 VAL A N     1 
ATOM   5457  C CA    . VAL A 1 2164 ? 182.792 235.857 226.406 1.00 0.90  ? 2164 VAL A CA    1 
ATOM   5458  C C     . VAL A 1 2164 ? 182.945 237.176 227.157 1.00 6.15  ? 2164 VAL A C     1 
ATOM   5459  O O     . VAL A 1 2164 ? 182.645 237.261 228.353 1.00 8.92  ? 2164 VAL A O     1 
ATOM   5460  C CB    . VAL A 1 2164 ? 184.120 235.085 226.332 1.00 0.00  ? 2164 VAL A CB    1 
ATOM   5461  C CG1   . VAL A 1 2164 ? 184.805 235.086 227.679 1.00 0.00  ? 2164 VAL A CG1   1 
ATOM   5462  C CG2   . VAL A 1 2164 ? 183.873 233.663 225.863 1.00 5.35  ? 2164 VAL A CG2   1 
ATOM   5463  N N     . PHE A 1 2165 ? 183.418 238.220 226.474 1.00 7.41  ? 2165 PHE A N     1 
ATOM   5464  C CA    . PHE A 1 2165 ? 183.576 239.556 227.046 1.00 2.62  ? 2165 PHE A CA    1 
ATOM   5465  C C     . PHE A 1 2165 ? 182.584 240.505 226.380 1.00 5.30  ? 2165 PHE A C     1 
ATOM   5466  O O     . PHE A 1 2165 ? 182.954 241.284 225.492 1.00 9.71  ? 2165 PHE A O     1 
ATOM   5467  C CB    . PHE A 1 2165 ? 185.000 240.083 226.876 1.00 0.00  ? 2165 PHE A CB    1 
ATOM   5468  C CG    . PHE A 1 2165 ? 186.074 239.109 227.266 1.00 0.81  ? 2165 PHE A CG    1 
ATOM   5469  C CD1   . PHE A 1 2165 ? 186.703 239.216 228.495 1.00 4.60  ? 2165 PHE A CD1   1 
ATOM   5470  C CD2   . PHE A 1 2165 ? 186.473 238.101 226.404 1.00 3.35  ? 2165 PHE A CD2   1 
ATOM   5471  C CE1   . PHE A 1 2165 ? 187.700 238.334 228.861 1.00 0.51  ? 2165 PHE A CE1   1 
ATOM   5472  C CE2   . PHE A 1 2165 ? 187.470 237.217 226.766 1.00 5.73  ? 2165 PHE A CE2   1 
ATOM   5473  C CZ    . PHE A 1 2165 ? 188.082 237.334 227.997 1.00 3.20  ? 2165 PHE A CZ    1 
ATOM   5474  N N     . PRO A 1 2166 ? 181.317 240.470 226.786 1.00 2.48  ? 2166 PRO A N     1 
ATOM   5475  C CA    . PRO A 1 2166 ? 180.319 241.318 226.130 1.00 7.47  ? 2166 PRO A CA    1 
ATOM   5476  C C     . PRO A 1 2166 ? 180.473 242.777 226.526 1.00 10.74 ? 2166 PRO A C     1 
ATOM   5477  O O     . PRO A 1 2166 ? 180.761 243.102 227.680 1.00 10.67 ? 2166 PRO A O     1 
ATOM   5478  C CB    . PRO A 1 2166 ? 178.990 240.742 226.625 1.00 6.63  ? 2166 PRO A CB    1 
ATOM   5479  C CG    . PRO A 1 2166 ? 179.316 240.194 227.965 1.00 9.55  ? 2166 PRO A CG    1 
ATOM   5480  C CD    . PRO A 1 2166 ? 180.737 239.702 227.901 1.00 5.29  ? 2166 PRO A CD    1 
ATOM   5481  N N     . GLY A 1 2167 ? 180.277 243.661 225.549 1.00 14.76 ? 2167 GLY A N     1 
ATOM   5482  C CA    . GLY A 1 2167 ? 180.267 245.086 225.772 1.00 19.70 ? 2167 GLY A CA    1 
ATOM   5483  C C     . GLY A 1 2167 ? 181.602 245.779 225.585 1.00 22.64 ? 2167 GLY A C     1 
ATOM   5484  O O     . GLY A 1 2167 ? 181.629 246.946 225.180 1.00 22.05 ? 2167 GLY A O     1 
ATOM   5485  N N     . VAL A 1 2168 ? 182.705 245.098 225.863 1.00 17.07 ? 2168 VAL A N     1 
ATOM   5486  C CA    . VAL A 1 2168 ? 184.018 245.717 225.773 1.00 17.35 ? 2168 VAL A CA    1 
ATOM   5487  C C     . VAL A 1 2168 ? 184.518 245.618 224.338 1.00 18.93 ? 2168 VAL A C     1 
ATOM   5488  O O     . VAL A 1 2168 ? 184.181 244.692 223.595 1.00 15.73 ? 2168 VAL A O     1 
ATOM   5489  C CB    . VAL A 1 2168 ? 185.019 245.082 226.760 1.00 11.55 ? 2168 VAL A CB    1 
ATOM   5490  C CG1   . VAL A 1 2168 ? 184.546 245.278 228.192 1.00 12.88 ? 2168 VAL A CG1   1 
ATOM   5491  C CG2   . VAL A 1 2168 ? 185.214 243.615 226.455 1.00 14.51 ? 2168 VAL A CG2   1 
ATOM   5492  N N     . GLN A 1 2169 ? 185.337 246.590 223.942 1.00 19.80 ? 2169 GLN A N     1 
ATOM   5493  C CA    . GLN A 1 2169 ? 185.837 246.674 222.578 1.00 18.30 ? 2169 GLN A CA    1 
ATOM   5494  C C     . GLN A 1 2169 ? 187.352 246.809 222.599 1.00 16.43 ? 2169 GLN A C     1 
ATOM   5495  O O     . GLN A 1 2169 ? 187.947 247.245 223.587 1.00 17.52 ? 2169 GLN A O     1 
ATOM   5496  C CB    . GLN A 1 2169 ? 185.214 247.850 221.815 1.00 19.10 ? 2169 GLN A CB    1 
ATOM   5497  C CG    . GLN A 1 2169 ? 183.796 247.595 221.336 1.00 23.21 ? 2169 GLN A CG    1 
ATOM   5498  C CD    . GLN A 1 2169 ? 182.759 248.305 222.182 1.00 25.06 ? 2169 GLN A CD    1 
ATOM   5499  O OE1   . GLN A 1 2169 ? 183.024 249.365 222.747 1.00 20.42 ? 2169 GLN A OE1   1 
ATOM   5500  N NE2   . GLN A 1 2169 ? 181.570 247.720 222.276 1.00 21.58 ? 2169 GLN A NE2   1 
ATOM   5501  N N     . TYR A 1 2170 ? 187.969 246.428 221.485 1.00 16.46 ? 2170 TYR A N     1 
ATOM   5502  C CA    . TYR A 1 2170 ? 189.416 246.447 221.338 1.00 14.10 ? 2170 TYR A CA    1 
ATOM   5503  C C     . TYR A 1 2170 ? 189.818 247.689 220.555 1.00 16.56 ? 2170 TYR A C     1 
ATOM   5504  O O     . TYR A 1 2170 ? 189.365 247.889 219.423 1.00 15.20 ? 2170 TYR A O     1 
ATOM   5505  C CB    . TYR A 1 2170 ? 189.901 245.186 220.619 1.00 11.95 ? 2170 TYR A CB    1 
ATOM   5506  C CG    . TYR A 1 2170 ? 191.328 245.243 220.118 1.00 11.07 ? 2170 TYR A CG    1 
ATOM   5507  C CD1   . TYR A 1 2170 ? 192.361 245.652 220.949 1.00 10.52 ? 2170 TYR A CD1   1 
ATOM   5508  C CD2   . TYR A 1 2170 ? 191.640 244.896 218.811 1.00 7.97  ? 2170 TYR A CD2   1 
ATOM   5509  C CE1   . TYR A 1 2170 ? 193.665 245.700 220.496 1.00 12.79 ? 2170 TYR A CE1   1 
ATOM   5510  C CE2   . TYR A 1 2170 ? 192.939 244.946 218.349 1.00 6.72  ? 2170 TYR A CE2   1 
ATOM   5511  C CZ    . TYR A 1 2170 ? 193.948 245.347 219.196 1.00 10.49 ? 2170 TYR A CZ    1 
ATOM   5512  O OH    . TYR A 1 2170 ? 195.246 245.399 218.743 1.00 5.18  ? 2170 TYR A OH    1 
ATOM   5513  N N     . HIS A 1 2171 ? 190.663 248.518 221.159 1.00 22.20 ? 2171 HIS A N     1 
ATOM   5514  C CA    . HIS A 1 2171 ? 191.161 249.738 220.538 1.00 17.85 ? 2171 HIS A CA    1 
ATOM   5515  C C     . HIS A 1 2171 ? 192.636 249.552 220.208 1.00 17.48 ? 2171 HIS A C     1 
ATOM   5516  O O     . HIS A 1 2171 ? 193.417 249.126 221.064 1.00 21.45 ? 2171 HIS A O     1 
ATOM   5517  C CB    . HIS A 1 2171 ? 190.959 250.944 221.460 1.00 17.16 ? 2171 HIS A CB    1 
ATOM   5518  C CG    . HIS A 1 2171 ? 189.583 251.035 222.049 1.00 22.43 ? 2171 HIS A CG    1 
ATOM   5519  N ND1   . HIS A 1 2171 ? 188.453 251.217 221.282 1.00 22.23 ? 2171 HIS A ND1   1 
ATOM   5520  C CD2   . HIS A 1 2171 ? 189.158 250.966 223.333 1.00 20.62 ? 2171 HIS A CD2   1 
ATOM   5521  C CE1   . HIS A 1 2171 ? 187.391 251.260 222.067 1.00 23.14 ? 2171 HIS A CE1   1 
ATOM   5522  N NE2   . HIS A 1 2171 ? 187.792 251.109 223.317 1.00 22.91 ? 2171 HIS A NE2   1 
ATOM   5523  N N     . ARG A 1 2172 ? 193.008 249.863 218.971 1.00 12.82 ? 2172 ARG A N     1 
ATOM   5524  C CA    . ARG A 1 2172 ? 194.342 249.579 218.462 1.00 11.02 ? 2172 ARG A CA    1 
ATOM   5525  C C     . ARG A 1 2172 ? 195.243 250.805 218.567 1.00 17.60 ? 2172 ARG A C     1 
ATOM   5526  O O     . ARG A 1 2172 ? 194.793 251.946 218.437 1.00 16.01 ? 2172 ARG A O     1 
ATOM   5527  C CB    . ARG A 1 2172 ? 194.259 249.105 217.008 1.00 12.37 ? 2172 ARG A CB    1 
ATOM   5528  C CG    . ARG A 1 2172 ? 195.432 248.256 216.543 1.00 16.30 ? 2172 ARG A CG    1 
ATOM   5529  C CD    . ARG A 1 2172 ? 195.873 248.611 215.127 1.00 16.11 ? 2172 ARG A CD    1 
ATOM   5530  N NE    . ARG A 1 2172 ? 196.633 247.529 214.511 1.00 21.45 ? 2172 ARG A NE    1 
ATOM   5531  C CZ    . ARG A 1 2172 ? 197.949 247.402 214.607 1.00 15.78 ? 2172 ARG A CZ    1 
ATOM   5532  N NH1   . ARG A 1 2172 ? 198.675 248.269 215.289 1.00 15.09 ? 2172 ARG A NH1   1 
ATOM   5533  N NH2   . ARG A 1 2172 ? 198.548 246.377 214.010 1.00 12.33 ? 2172 ARG A NH2   1 
ATOM   5534  N N     . GLY A 1 2173 ? 196.526 250.555 218.817 1.00 24.70 ? 2173 GLY A N     1 
ATOM   5535  C CA    . GLY A 1 2173 ? 197.499 251.637 218.848 1.00 23.40 ? 2173 GLY A CA    1 
ATOM   5536  C C     . GLY A 1 2173 ? 197.621 252.289 217.482 1.00 25.27 ? 2173 GLY A C     1 
ATOM   5537  O O     . GLY A 1 2173 ? 197.773 251.605 216.463 1.00 24.53 ? 2173 GLY A O     1 
ATOM   5538  N N     . GLU A 1 2174 ? 197.554 253.622 217.454 1.00 25.11 ? 2174 GLU A N     1 
ATOM   5539  C CA    . GLU A 1 2174 ? 197.502 254.329 216.178 1.00 27.70 ? 2174 GLU A CA    1 
ATOM   5540  C C     . GLU A 1 2174 ? 198.840 254.278 215.447 1.00 28.34 ? 2174 GLU A C     1 
ATOM   5541  O O     . GLU A 1 2174 ? 198.875 254.064 214.229 1.00 25.77 ? 2174 GLU A O     1 
ATOM   5542  C CB    . GLU A 1 2174 ? 197.044 255.776 216.396 1.00 25.06 ? 2174 GLU A CB    1 
ATOM   5543  C CG    . GLU A 1 2174 ? 198.054 256.712 217.057 1.00 25.85 ? 2174 GLU A CG    1 
ATOM   5544  C CD    . GLU A 1 2174 ? 198.298 256.389 218.519 1.00 30.80 ? 2174 GLU A CD    1 
ATOM   5545  O OE1   . GLU A 1 2174 ? 197.436 255.728 219.136 1.00 30.51 ? 2174 GLU A OE1   1 
ATOM   5546  O OE2   . GLU A 1 2174 ? 199.349 256.803 219.053 1.00 32.28 ? 2174 GLU A OE2   1 
ATOM   5547  N N     . MET A 1 2175 ? 199.947 254.449 216.171 1.00 25.06 ? 2175 MET A N     1 
ATOM   5548  C CA    . MET A 1 2175 ? 201.279 254.580 215.577 1.00 22.73 ? 2175 MET A CA    1 
ATOM   5549  C C     . MET A 1 2175 ? 201.273 255.566 214.410 1.00 16.60 ? 2175 MET A C     1 
ATOM   5550  O O     . MET A 1 2175 ? 201.683 255.250 213.292 1.00 13.82 ? 2175 MET A O     1 
ATOM   5551  C CB    . MET A 1 2175 ? 201.838 253.224 215.147 1.00 16.39 ? 2175 MET A CB    1 
ATOM   5552  C CG    . MET A 1 2175 ? 202.131 252.288 216.301 1.00 21.79 ? 2175 MET A CG    1 
ATOM   5553  S SD    . MET A 1 2175 ? 202.851 250.730 215.764 1.00 30.77 ? 2175 MET A SD    1 
ATOM   5554  C CE    . MET A 1 2175 ? 201.425 249.919 215.058 1.00 18.50 ? 2175 MET A CE    1 
ATOM   5555  N N     . THR A 1 2176 ? 200.784 256.777 214.682 1.00 20.64 ? 2176 THR A N     1 
ATOM   5556  C CA    . THR A 1 2176 ? 200.764 257.824 213.669 1.00 19.17 ? 2176 THR A CA    1 
ATOM   5557  C C     . THR A 1 2176 ? 202.166 258.150 213.166 1.00 16.79 ? 2176 THR A C     1 
ATOM   5558  O O     . THR A 1 2176 ? 202.327 258.500 211.991 1.00 20.58 ? 2176 THR A O     1 
ATOM   5559  C CB    . THR A 1 2176 ? 200.084 259.077 214.237 1.00 18.89 ? 2176 THR A CB    1 
ATOM   5560  O OG1   . THR A 1 2176 ? 198.668 258.871 214.288 1.00 23.21 ? 2176 THR A OG1   1 
ATOM   5561  C CG2   . THR A 1 2176 ? 200.361 260.298 213.376 1.00 20.32 ? 2176 THR A CG2   1 
ATOM   5562  N N     . ALA A 1 2177 ? 203.184 258.002 214.017 1.00 12.13 ? 2177 ALA A N     1 
ATOM   5563  C CA    . ALA A 1 2177 ? 204.549 258.324 213.611 1.00 14.72 ? 2177 ALA A CA    1 
ATOM   5564  C C     . ALA A 1 2177 ? 205.009 257.456 212.446 1.00 17.30 ? 2177 ALA A C     1 
ATOM   5565  O O     . ALA A 1 2177 ? 205.576 257.967 211.474 1.00 14.64 ? 2177 ALA A O     1 
ATOM   5566  C CB    . ALA A 1 2177 ? 205.498 258.172 214.799 1.00 15.03 ? 2177 ALA A CB    1 
ATOM   5567  N N     . LEU A 1 2178 ? 204.774 256.146 212.519 1.00 20.95 ? 2178 LEU A N     1 
ATOM   5568  C CA    . LEU A 1 2178 ? 205.162 255.253 211.434 1.00 14.15 ? 2178 LEU A CA    1 
ATOM   5569  C C     . LEU A 1 2178 ? 204.181 255.272 210.274 1.00 11.31 ? 2178 LEU A C     1 
ATOM   5570  O O     . LEU A 1 2178 ? 204.593 255.091 209.123 1.00 16.96 ? 2178 LEU A O     1 
ATOM   5571  C CB    . LEU A 1 2178 ? 205.309 253.817 211.944 1.00 10.37 ? 2178 LEU A CB    1 
ATOM   5572  C CG    . LEU A 1 2178 ? 206.042 252.855 211.004 1.00 13.13 ? 2178 LEU A CG    1 
ATOM   5573  C CD1   . LEU A 1 2178 ? 207.475 253.300 210.768 1.00 9.96  ? 2178 LEU A CD1   1 
ATOM   5574  C CD2   . LEU A 1 2178 ? 206.003 251.439 211.545 1.00 13.55 ? 2178 LEU A CD2   1 
ATOM   5575  N N     . ARG A 1 2179 ? 202.894 255.483 210.545 1.00 14.43 ? 2179 ARG A N     1 
ATOM   5576  C CA    . ARG A 1 2179 ? 201.904 255.520 209.478 1.00 6.20  ? 2179 ARG A CA    1 
ATOM   5577  C C     . ARG A 1 2179 ? 202.081 256.713 208.553 1.00 10.51 ? 2179 ARG A C     1 
ATOM   5578  O O     . ARG A 1 2179 ? 201.536 256.698 207.445 1.00 17.16 ? 2179 ARG A O     1 
ATOM   5579  C CB    . ARG A 1 2179 ? 200.495 255.522 210.070 1.00 8.12  ? 2179 ARG A CB    1 
ATOM   5580  C CG    . ARG A 1 2179 ? 199.874 254.140 210.142 1.00 8.40  ? 2179 ARG A CG    1 
ATOM   5581  C CD    . ARG A 1 2179 ? 198.570 254.141 210.913 1.00 13.78 ? 2179 ARG A CD    1 
ATOM   5582  N NE    . ARG A 1 2179 ? 197.775 252.959 210.606 1.00 14.13 ? 2179 ARG A NE    1 
ATOM   5583  C CZ    . ARG A 1 2179 ? 196.563 252.986 210.071 1.00 15.77 ? 2179 ARG A CZ    1 
ATOM   5584  N NH1   . ARG A 1 2179 ? 195.962 254.127 209.778 1.00 14.61 ? 2179 ARG A NH1   1 
ATOM   5585  N NH2   . ARG A 1 2179 ? 195.937 251.839 209.822 1.00 14.25 ? 2179 ARG A NH2   1 
ATOM   5586  N N     . GLU A 1 2180 ? 202.820 257.739 208.974 1.00 11.30 ? 2180 GLU A N     1 
ATOM   5587  C CA    . GLU A 1 2180 ? 203.169 258.845 208.095 1.00 17.17 ? 2180 GLU A CA    1 
ATOM   5588  C C     . GLU A 1 2180 ? 204.384 258.554 207.229 1.00 13.87 ? 2180 GLU A C     1 
ATOM   5589  O O     . GLU A 1 2180 ? 204.392 258.938 206.055 1.00 14.72 ? 2180 GLU A O     1 
ATOM   5590  C CB    . GLU A 1 2180 ? 203.428 260.118 208.911 1.00 18.05 ? 2180 GLU A CB    1 
ATOM   5591  C CG    . GLU A 1 2180 ? 202.185 260.956 209.156 1.00 18.26 ? 2180 GLU A CG    1 
ATOM   5592  C CD    . GLU A 1 2180 ? 201.333 261.109 207.912 1.00 20.52 ? 2180 GLU A CD    1 
ATOM   5593  O OE1   . GLU A 1 2180 ? 200.231 260.522 207.869 1.00 22.78 ? 2180 GLU A OE1   1 
ATOM   5594  O OE2   . GLU A 1 2180 ? 201.765 261.813 206.976 1.00 13.40 ? 2180 GLU A OE2   1 
ATOM   5595  N N     . GLU A 1 2181 ? 205.403 257.887 207.773 1.00 12.57 ? 2181 GLU A N     1 
ATOM   5596  C CA    . GLU A 1 2181 ? 206.542 257.471 206.967 1.00 8.52  ? 2181 GLU A CA    1 
ATOM   5597  C C     . GLU A 1 2181 ? 206.191 256.343 206.010 1.00 11.99 ? 2181 GLU A C     1 
ATOM   5598  O O     . GLU A 1 2181 ? 206.882 256.166 205.001 1.00 20.93 ? 2181 GLU A O     1 
ATOM   5599  C CB    . GLU A 1 2181 ? 207.703 257.045 207.869 1.00 12.37 ? 2181 GLU A CB    1 
ATOM   5600  C CG    . GLU A 1 2181 ? 208.487 258.207 208.466 1.00 22.59 ? 2181 GLU A CG    1 
ATOM   5601  C CD    . GLU A 1 2181 ? 209.529 258.781 207.518 1.00 22.54 ? 2181 GLU A CD    1 
ATOM   5602  O OE1   . GLU A 1 2181 ? 209.435 258.546 206.295 1.00 17.91 ? 2181 GLU A OE1   1 
ATOM   5603  O OE2   . GLU A 1 2181 ? 210.447 259.475 208.001 1.00 18.60 ? 2181 GLU A OE2   1 
ATOM   5604  N N     . LEU A 1 2182 ? 205.144 255.570 206.307 1.00 15.36 ? 2182 LEU A N     1 
ATOM   5605  C CA    . LEU A 1 2182 ? 204.648 254.597 205.339 1.00 9.87  ? 2182 LEU A CA    1 
ATOM   5606  C C     . LEU A 1 2182 ? 204.098 255.293 204.101 1.00 12.12 ? 2182 LEU A C     1 
ATOM   5607  O O     . LEU A 1 2182 ? 204.323 254.839 202.974 1.00 18.91 ? 2182 LEU A O     1 
ATOM   5608  C CB    . LEU A 1 2182 ? 203.576 253.713 205.976 1.00 10.79 ? 2182 LEU A CB    1 
ATOM   5609  C CG    . LEU A 1 2182 ? 204.040 252.669 206.992 1.00 9.67  ? 2182 LEU A CG    1 
ATOM   5610  C CD1   . LEU A 1 2182 ? 202.863 251.839 207.474 1.00 7.52  ? 2182 LEU A CD1   1 
ATOM   5611  C CD2   . LEU A 1 2182 ? 205.120 251.784 206.402 1.00 12.86 ? 2182 LEU A CD2   1 
ATOM   5612  N N     . LYS A 1 2183 ? 203.373 256.399 204.291 1.00 12.11 ? 2183 LYS A N     1 
ATOM   5613  C CA    . LYS A 1 2183 ? 202.859 257.167 203.163 1.00 10.55 ? 2183 LYS A CA    1 
ATOM   5614  C C     . LYS A 1 2183 ? 203.969 257.750 202.301 1.00 9.37  ? 2183 LYS A C     1 
ATOM   5615  O O     . LYS A 1 2183 ? 203.723 258.074 201.136 1.00 14.03 ? 2183 LYS A O     1 
ATOM   5616  C CB    . LYS A 1 2183 ? 201.960 258.300 203.654 1.00 12.64 ? 2183 LYS A CB    1 
ATOM   5617  C CG    . LYS A 1 2183 ? 200.657 257.844 204.256 1.00 12.91 ? 2183 LYS A CG    1 
ATOM   5618  C CD    . LYS A 1 2183 ? 199.860 259.019 204.786 1.00 15.30 ? 2183 LYS A CD    1 
ATOM   5619  C CE    . LYS A 1 2183 ? 199.322 259.876 203.652 1.00 16.11 ? 2183 LYS A CE    1 
ATOM   5620  N NZ    . LYS A 1 2183 ? 198.285 259.164 202.857 1.00 13.65 ? 2183 LYS A NZ    1 
ATOM   5621  N N     . LYS A 1 2184 ? 205.171 257.912 202.848 1.00 9.61  ? 2184 LYS A N     1 
ATOM   5622  C CA    . LYS A 1 2184 ? 206.303 258.405 202.078 1.00 11.27 ? 2184 LYS A CA    1 
ATOM   5623  C C     . LYS A 1 2184 ? 207.127 257.292 201.450 1.00 12.84 ? 2184 LYS A C     1 
ATOM   5624  O O     . LYS A 1 2184 ? 207.637 257.471 200.341 1.00 19.45 ? 2184 LYS A O     1 
ATOM   5625  C CB    . LYS A 1 2184 ? 207.208 259.275 202.957 1.00 11.65 ? 2184 LYS A CB    1 
ATOM   5626  C CG    . LYS A 1 2184 ? 206.652 260.668 203.215 1.00 11.93 ? 2184 LYS A CG    1 
ATOM   5627  C CD    . LYS A 1 2184 ? 206.496 260.948 204.700 1.00 14.71 ? 2184 LYS A CD    1 
ATOM   5628  C CE    . LYS A 1 2184 ? 205.913 262.330 204.941 1.00 15.70 ? 2184 LYS A CE    1 
ATOM   5629  N NZ    . LYS A 1 2184 ? 205.595 262.562 206.376 1.00 16.79 ? 2184 LYS A NZ    1 
ATOM   5630  N N     . VAL A 1 2185 ? 207.279 256.154 202.130 1.00 6.06  ? 2185 VAL A N     1 
ATOM   5631  C CA    . VAL A 1 2185 ? 207.901 254.999 201.492 1.00 6.18  ? 2185 VAL A CA    1 
ATOM   5632  C C     . VAL A 1 2185 ? 207.007 254.465 200.383 1.00 10.12 ? 2185 VAL A C     1 
ATOM   5633  O O     . VAL A 1 2185 ? 207.479 254.138 199.288 1.00 20.51 ? 2185 VAL A O     1 
ATOM   5634  C CB    . VAL A 1 2185 ? 208.230 253.918 202.533 1.00 6.53  ? 2185 VAL A CB    1 
ATOM   5635  C CG1   . VAL A 1 2185 ? 208.674 252.649 201.841 1.00 10.83 ? 2185 VAL A CG1   1 
ATOM   5636  C CG2   . VAL A 1 2185 ? 209.315 254.417 203.461 1.00 11.37 ? 2185 VAL A CG2   1 
ATOM   5637  N N     . CYS A 1 2186 ? 205.709 254.359 200.647 1.00 13.29 ? 2186 CYS A N     1 
ATOM   5638  C CA    . CYS A 1 2186 ? 204.750 254.201 199.570 1.00 7.44  ? 2186 CYS A CA    1 
ATOM   5639  C C     . CYS A 1 2186 ? 204.533 255.550 198.892 1.00 12.22 ? 2186 CYS A C     1 
ATOM   5640  O O     . CYS A 1 2186 ? 205.079 256.574 199.306 1.00 20.81 ? 2186 CYS A O     1 
ATOM   5641  C CB    . CYS A 1 2186 ? 203.435 253.629 200.095 1.00 9.29  ? 2186 CYS A CB    1 
ATOM   5642  S SG    . CYS A 1 2186 ? 203.627 252.187 201.166 1.00 7.61  ? 2186 CYS A SG    1 
ATOM   5643  N N     . GLN A 1 2187 ? 203.758 255.539 197.809 1.00 10.29 ? 2187 GLN A N     1 
ATOM   5644  C CA    . GLN A 1 2187 ? 203.512 256.685 196.935 1.00 17.90 ? 2187 GLN A CA    1 
ATOM   5645  C C     . GLN A 1 2187 ? 204.773 257.113 196.195 1.00 20.03 ? 2187 GLN A C     1 
ATOM   5646  O O     . GLN A 1 2187 ? 204.704 258.006 195.343 1.00 22.81 ? 2187 GLN A O     1 
ATOM   5647  C CB    . GLN A 1 2187 ? 202.932 257.899 197.677 1.00 14.75 ? 2187 GLN A CB    1 
ATOM   5648  C CG    . GLN A 1 2187 ? 201.744 257.593 198.580 1.00 16.05 ? 2187 GLN A CG    1 
ATOM   5649  C CD    . GLN A 1 2187 ? 200.810 256.553 197.997 1.00 24.14 ? 2187 GLN A CD    1 
ATOM   5650  O OE1   . GLN A 1 2187 ? 200.856 255.382 198.372 1.00 22.45 ? 2187 GLN A OE1   1 
ATOM   5651  N NE2   . GLN A 1 2187 ? 199.958 256.975 197.070 1.00 22.72 ? 2187 GLN A NE2   1 
ATOM   5652  N N     . GLU A 1 2188 ? 205.923 256.512 196.498 1.00 11.25 ? 2188 GLU A N     1 
ATOM   5653  C CA    . GLU A 1 2188 ? 207.120 256.618 195.683 1.00 8.10  ? 2188 GLU A CA    1 
ATOM   5654  C C     . GLU A 1 2188 ? 207.604 255.268 195.191 1.00 11.98 ? 2188 GLU A C     1 
ATOM   5655  O O     . GLU A 1 2188 ? 208.355 255.219 194.211 1.00 15.56 ? 2188 GLU A O     1 
ATOM   5656  C CB    . GLU A 1 2188 ? 208.256 257.298 196.463 1.00 11.56 ? 2188 GLU A CB    1 
ATOM   5657  C CG    . GLU A 1 2188 ? 208.824 256.451 197.582 1.00 10.75 ? 2188 GLU A CG    1 
ATOM   5658  C CD    . GLU A 1 2188 ? 209.932 257.148 198.335 1.00 14.10 ? 2188 GLU A CD    1 
ATOM   5659  O OE1   . GLU A 1 2188 ? 210.263 258.298 197.980 1.00 17.71 ? 2188 GLU A OE1   1 
ATOM   5660  O OE2   . GLU A 1 2188 ? 210.472 256.548 199.287 1.00 12.31 ? 2188 GLU A OE2   1 
ATOM   5661  N N     . MET A 1 2189 ? 207.208 254.180 195.848 1.00 10.86 ? 2189 MET A N     1 
ATOM   5662  C CA    . MET A 1 2189 ? 207.350 252.833 195.321 1.00 7.38  ? 2189 MET A CA    1 
ATOM   5663  C C     . MET A 1 2189 ? 206.094 252.376 194.594 1.00 9.29  ? 2189 MET A C     1 
ATOM   5664  O O     . MET A 1 2189 ? 205.952 251.182 194.312 1.00 12.22 ? 2189 MET A O     1 
ATOM   5665  C CB    . MET A 1 2189 ? 207.699 251.856 196.445 1.00 0.00  ? 2189 MET A CB    1 
ATOM   5666  C CG    . MET A 1 2189 ? 209.088 252.068 197.021 1.00 7.66  ? 2189 MET A CG    1 
ATOM   5667  S SD    . MET A 1 2189 ? 209.462 250.998 198.421 1.00 20.54 ? 2189 MET A SD    1 
ATOM   5668  C CE    . MET A 1 2189 ? 208.432 249.585 198.051 1.00 15.98 ? 2189 MET A CE    1 
ATOM   5669  N N     . TYR A 1 2190 ? 205.179 253.305 194.304 1.00 8.97  ? 2190 TYR A N     1 
ATOM   5670  C CA    . TYR A 1 2190 ? 204.004 253.047 193.474 1.00 2.04  ? 2190 TYR A CA    1 
ATOM   5671  C C     . TYR A 1 2190 ? 203.093 251.990 194.093 1.00 6.90  ? 2190 TYR A C     1 
ATOM   5672  O O     . TYR A 1 2190 ? 202.511 251.159 193.393 1.00 13.06 ? 2190 TYR A O     1 
ATOM   5673  C CB    . TYR A 1 2190 ? 204.416 252.654 192.053 1.00 3.45  ? 2190 TYR A CB    1 
ATOM   5674  C CG    . TYR A 1 2190 ? 205.601 253.437 191.526 1.00 5.63  ? 2190 TYR A CG    1 
ATOM   5675  C CD1   . TYR A 1 2190 ? 205.544 254.817 191.403 1.00 9.20  ? 2190 TYR A CD1   1 
ATOM   5676  C CD2   . TYR A 1 2190 ? 206.780 252.798 191.176 1.00 5.09  ? 2190 TYR A CD2   1 
ATOM   5677  C CE1   . TYR A 1 2190 ? 206.621 255.538 190.931 1.00 6.81  ? 2190 TYR A CE1   1 
ATOM   5678  C CE2   . TYR A 1 2190 ? 207.863 253.511 190.703 1.00 7.12  ? 2190 TYR A CE2   1 
ATOM   5679  C CZ    . TYR A 1 2190 ? 207.778 254.880 190.582 1.00 7.93  ? 2190 TYR A CZ    1 
ATOM   5680  O OH    . TYR A 1 2190 ? 208.856 255.596 190.113 1.00 12.82 ? 2190 TYR A OH    1 
ATOM   5681  N N     . LEU A 1 2191 ? 202.955 252.028 195.413 1.00 7.99  ? 2191 LEU A N     1 
ATOM   5682  C CA    . LEU A 1 2191 ? 202.064 251.137 196.142 1.00 0.00  ? 2191 LEU A CA    1 
ATOM   5683  C C     . LEU A 1 2191 ? 200.879 251.925 196.690 1.00 0.00  ? 2191 LEU A C     1 
ATOM   5684  O O     . LEU A 1 2191 ? 200.874 253.157 196.711 1.00 2.45  ? 2191 LEU A O     1 
ATOM   5685  C CB    . LEU A 1 2191 ? 202.814 250.422 197.265 1.00 0.95  ? 2191 LEU A CB    1 
ATOM   5686  C CG    . LEU A 1 2191 ? 204.015 249.583 196.834 1.00 1.69  ? 2191 LEU A CG    1 
ATOM   5687  C CD1   . LEU A 1 2191 ? 204.756 249.075 198.048 1.00 3.02  ? 2191 LEU A CD1   1 
ATOM   5688  C CD2   . LEU A 1 2191 ? 203.578 248.431 195.948 1.00 2.35  ? 2191 LEU A CD2   1 
ATOM   5689  N N     . THR A 1 2192 ? 199.868 251.193 197.146 1.00 2.86  ? 2192 THR A N     1 
ATOM   5690  C CA    . THR A 1 2192 ? 198.626 251.774 197.640 1.00 8.27  ? 2192 THR A CA    1 
ATOM   5691  C C     . THR A 1 2192 ? 198.629 251.773 199.161 1.00 12.72 ? 2192 THR A C     1 
ATOM   5692  O O     . THR A 1 2192 ? 198.934 250.753 199.786 1.00 13.41 ? 2192 THR A O     1 
ATOM   5693  C CB    . THR A 1 2192 ? 197.413 251.001 197.118 1.00 2.09  ? 2192 THR A CB    1 
ATOM   5694  O OG1   . THR A 1 2192 ? 197.507 250.872 195.695 1.00 7.32  ? 2192 THR A OG1   1 
ATOM   5695  C CG2   . THR A 1 2192 ? 196.129 251.727 197.472 1.00 0.86  ? 2192 THR A CG2   1 
ATOM   5696  N N     . TYR A 1 2193 ? 198.283 252.914 199.749 1.00 14.27 ? 2193 TYR A N     1 
ATOM   5697  C CA    . TYR A 1 2193 ? 198.257 253.089 201.192 1.00 2.92  ? 2193 TYR A CA    1 
ATOM   5698  C C     . TYR A 1 2193 ? 196.817 253.190 201.669 1.00 6.13  ? 2193 TYR A C     1 
ATOM   5699  O O     . TYR A 1 2193 ? 195.951 253.707 200.957 1.00 16.15 ? 2193 TYR A O     1 
ATOM   5700  C CB    . TYR A 1 2193 ? 199.019 254.344 201.613 1.00 8.84  ? 2193 TYR A CB    1 
ATOM   5701  C CG    . TYR A 1 2193 ? 199.060 254.543 203.106 1.00 12.99 ? 2193 TYR A CG    1 
ATOM   5702  C CD1   . TYR A 1 2193 ? 199.916 253.798 203.902 1.00 12.92 ? 2193 TYR A CD1   1 
ATOM   5703  C CD2   . TYR A 1 2193 ? 198.210 255.446 203.725 1.00 11.46 ? 2193 TYR A CD2   1 
ATOM   5704  C CE1   . TYR A 1 2193 ? 199.947 253.971 205.268 1.00 7.95  ? 2193 TYR A CE1   1 
ATOM   5705  C CE2   . TYR A 1 2193 ? 198.231 255.621 205.089 1.00 7.54  ? 2193 TYR A CE2   1 
ATOM   5706  C CZ    . TYR A 1 2193 ? 199.101 254.882 205.854 1.00 6.93  ? 2193 TYR A CZ    1 
ATOM   5707  O OH    . TYR A 1 2193 ? 199.121 255.059 207.213 1.00 15.36 ? 2193 TYR A OH    1 
ATOM   5708  N N     . GLY A 1 2194 ? 196.566 252.693 202.881 1.00 3.92  ? 2194 GLY A N     1 
ATOM   5709  C CA    . GLY A 1 2194 ? 195.259 252.782 203.495 1.00 9.25  ? 2194 GLY A CA    1 
ATOM   5710  C C     . GLY A 1 2194 ? 195.370 253.163 204.960 1.00 11.03 ? 2194 GLY A C     1 
ATOM   5711  O O     . GLY A 1 2194 ? 196.455 253.157 205.543 1.00 16.35 ? 2194 GLY A O     1 
ATOM   5712  N N     . ASP A 1 2195 ? 194.217 253.496 205.540 1.00 11.59 ? 2195 ASP A N     1 
ATOM   5713  C CA    . ASP A 1 2195 ? 194.181 253.899 206.939 1.00 10.18 ? 2195 ASP A CA    1 
ATOM   5714  C C     . ASP A 1 2195 ? 193.011 253.290 207.700 1.00 16.53 ? 2195 ASP A C     1 
ATOM   5715  O O     . ASP A 1 2195 ? 192.651 253.808 208.765 1.00 22.72 ? 2195 ASP A O     1 
ATOM   5716  C CB    . ASP A 1 2195 ? 194.133 255.427 207.060 1.00 13.70 ? 2195 ASP A CB    1 
ATOM   5717  C CG    . ASP A 1 2195 ? 195.495 256.031 207.329 1.00 17.08 ? 2195 ASP A CG    1 
ATOM   5718  O OD1   . ASP A 1 2195 ? 196.437 255.265 207.617 1.00 14.69 ? 2195 ASP A OD1   1 
ATOM   5719  O OD2   . ASP A 1 2195 ? 195.625 257.271 207.252 1.00 19.66 ? 2195 ASP A OD2   1 
ATOM   5720  N N     . GLY A 1 2196 ? 192.409 252.219 207.198 1.00 16.51 ? 2196 GLY A N     1 
ATOM   5721  C CA    . GLY A 1 2196 ? 191.260 251.632 207.853 1.00 20.99 ? 2196 GLY A CA    1 
ATOM   5722  C C     . GLY A 1 2196 ? 190.436 250.794 206.902 1.00 23.50 ? 2196 GLY A C     1 
ATOM   5723  O O     . GLY A 1 2196 ? 190.965 249.908 206.225 1.00 22.81 ? 2196 GLY A O     1 
ATOM   5724  N N     . GLU A 1 2197 ? 189.132 251.061 206.848 1.00 26.14 ? 2197 GLU A N     1 
ATOM   5725  C CA    . GLU A 1 2197 ? 188.264 250.378 205.901 1.00 22.67 ? 2197 GLU A CA    1 
ATOM   5726  C C     . GLU A 1 2197 ? 188.547 250.766 204.455 1.00 25.49 ? 2197 GLU A C     1 
ATOM   5727  O O     . GLU A 1 2197 ? 188.044 250.099 203.546 1.00 29.20 ? 2197 GLU A O     1 
ATOM   5728  C CB    . GLU A 1 2197 ? 186.800 250.664 206.236 1.00 24.81 ? 2197 GLU A CB    1 
ATOM   5729  C CG    . GLU A 1 2197 ? 186.355 250.125 207.588 1.00 27.28 ? 2197 GLU A CG    1 
ATOM   5730  C CD    . GLU A 1 2197 ? 186.881 248.729 207.866 1.00 28.13 ? 2197 GLU A CD    1 
ATOM   5731  O OE1   . GLU A 1 2197 ? 186.269 247.755 207.380 1.00 28.17 ? 2197 GLU A OE1   1 
ATOM   5732  O OE2   . GLU A 1 2197 ? 187.901 248.605 208.576 1.00 28.21 ? 2197 GLU A OE2   1 
ATOM   5733  N N     . GLU A 1 2198 ? 189.325 251.820 204.220 1.00 16.15 ? 2198 GLU A N     1 
ATOM   5734  C CA    . GLU A 1 2198 ? 189.632 252.235 202.862 1.00 14.81 ? 2198 GLU A CA    1 
ATOM   5735  C C     . GLU A 1 2198 ? 190.603 251.253 202.208 1.00 14.81 ? 2198 GLU A C     1 
ATOM   5736  O O     . GLU A 1 2198 ? 191.173 250.370 202.854 1.00 16.84 ? 2198 GLU A O     1 
ATOM   5737  C CB    . GLU A 1 2198 ? 190.209 253.650 202.848 1.00 15.31 ? 2198 GLU A CB    1 
ATOM   5738  C CG    . GLU A 1 2198 ? 191.201 253.937 203.958 1.00 20.03 ? 2198 GLU A CG    1 
ATOM   5739  C CD    . GLU A 1 2198 ? 191.656 255.382 203.966 1.00 20.00 ? 2198 GLU A CD    1 
ATOM   5740  O OE1   . GLU A 1 2198 ? 190.787 256.278 203.982 1.00 20.88 ? 2198 GLU A OE1   1 
ATOM   5741  O OE2   . GLU A 1 2198 ? 192.881 255.624 203.955 1.00 19.46 ? 2198 GLU A OE2   1 
ATOM   5742  N N     . VAL A 1 2199 ? 190.784 251.422 200.896 1.00 17.26 ? 2199 VAL A N     1 
ATOM   5743  C CA    . VAL A 1 2199 ? 191.628 250.514 200.131 1.00 8.31  ? 2199 VAL A CA    1 
ATOM   5744  C C     . VAL A 1 2199 ? 193.066 250.594 200.622 1.00 5.83  ? 2199 VAL A C     1 
ATOM   5745  O O     . VAL A 1 2199 ? 193.636 251.682 200.773 1.00 6.02  ? 2199 VAL A O     1 
ATOM   5746  C CB    . VAL A 1 2199 ? 191.534 250.837 198.631 1.00 5.24  ? 2199 VAL A CB    1 
ATOM   5747  C CG1   . VAL A 1 2199 ? 192.172 249.733 197.809 1.00 4.97  ? 2199 VAL A CG1   1 
ATOM   5748  C CG2   . VAL A 1 2199 ? 190.082 251.032 198.229 1.00 8.76  ? 2199 VAL A CG2   1 
ATOM   5749  N N     . GLY A 1 2200 ? 193.662 249.428 200.869 1.00 2.40  ? 2200 GLY A N     1 
ATOM   5750  C CA    . GLY A 1 2200 ? 194.999 249.340 201.408 1.00 0.28  ? 2200 GLY A CA    1 
ATOM   5751  C C     . GLY A 1 2200 ? 195.078 249.271 202.917 1.00 7.17  ? 2200 GLY A C     1 
ATOM   5752  O O     . GLY A 1 2200 ? 196.184 249.151 203.456 1.00 5.05  ? 2200 GLY A O     1 
ATOM   5753  N N     . GLY A 1 2201 ? 193.943 249.340 203.614 1.00 10.83 ? 2201 GLY A N     1 
ATOM   5754  C CA    . GLY A 1 2201 ? 193.975 249.328 205.068 1.00 4.89  ? 2201 GLY A CA    1 
ATOM   5755  C C     . GLY A 1 2201 ? 194.473 248.016 205.641 1.00 5.00  ? 2201 GLY A C     1 
ATOM   5756  O O     . GLY A 1 2201 ? 195.284 248.002 206.568 1.00 10.82 ? 2201 GLY A O     1 
ATOM   5757  N N     . MET A 1 2202 ? 193.996 246.894 205.099 1.00 2.64  ? 2202 MET A N     1 
ATOM   5758  C CA    . MET A 1 2202 ? 194.414 245.594 205.612 1.00 0.71  ? 2202 MET A CA    1 
ATOM   5759  C C     . MET A 1 2202 ? 195.913 245.391 205.435 1.00 0.31  ? 2202 MET A C     1 
ATOM   5760  O O     . MET A 1 2202 ? 196.587 244.864 206.329 1.00 5.77  ? 2202 MET A O     1 
ATOM   5761  C CB    . MET A 1 2202 ? 193.635 244.483 204.913 1.00 0.00  ? 2202 MET A CB    1 
ATOM   5762  C CG    . MET A 1 2202 ? 192.135 244.563 205.114 1.00 0.14  ? 2202 MET A CG    1 
ATOM   5763  S SD    . MET A 1 2202 ? 191.221 243.525 203.960 1.00 18.63 ? 2202 MET A SD    1 
ATOM   5764  C CE    . MET A 1 2202 ? 190.209 242.576 205.091 1.00 7.29  ? 2202 MET A CE    1 
ATOM   5765  N N     . TRP A 1 2203 ? 196.453 245.813 204.292 1.00 0.00  ? 2203 TRP A N     1 
ATOM   5766  C CA    . TRP A 1 2203 ? 197.877 245.639 204.034 1.00 1.28  ? 2203 TRP A CA    1 
ATOM   5767  C C     . TRP A 1 2203 ? 198.719 246.452 205.013 1.00 8.39  ? 2203 TRP A C     1 
ATOM   5768  O O     . TRP A 1 2203 ? 199.727 245.962 205.536 1.00 15.32 ? 2203 TRP A O     1 
ATOM   5769  C CB    . TRP A 1 2203 ? 198.190 246.021 202.587 1.00 1.91  ? 2203 TRP A CB    1 
ATOM   5770  C CG    . TRP A 1 2203 ? 199.621 245.833 202.210 1.00 0.00  ? 2203 TRP A CG    1 
ATOM   5771  C CD1   . TRP A 1 2203 ? 200.261 244.651 201.992 1.00 0.00  ? 2203 TRP A CD1   1 
ATOM   5772  C CD2   . TRP A 1 2203 ? 200.595 246.861 202.004 1.00 0.00  ? 2203 TRP A CD2   1 
ATOM   5773  N NE1   . TRP A 1 2203 ? 201.574 244.878 201.667 1.00 0.00  ? 2203 TRP A NE1   1 
ATOM   5774  C CE2   . TRP A 1 2203 ? 201.805 246.228 201.667 1.00 0.00  ? 2203 TRP A CE2   1 
ATOM   5775  C CE3   . TRP A 1 2203 ? 200.562 248.256 202.075 1.00 0.82  ? 2203 TRP A CE3   1 
ATOM   5776  C CZ2   . TRP A 1 2203 ? 202.969 246.938 201.403 1.00 0.00  ? 2203 TRP A CZ2   1 
ATOM   5777  C CZ3   . TRP A 1 2203 ? 201.716 248.958 201.811 1.00 1.50  ? 2203 TRP A CZ3   1 
ATOM   5778  C CH2   . TRP A 1 2203 ? 202.904 248.300 201.479 1.00 2.71  ? 2203 TRP A CH2   1 
ATOM   5779  N N     . VAL A 1 2204 ? 198.321 247.697 205.285 1.00 4.18  ? 2204 VAL A N     1 
ATOM   5780  C CA    . VAL A 1 2204 ? 199.105 248.522 206.202 1.00 4.48  ? 2204 VAL A CA    1 
ATOM   5781  C C     . VAL A 1 2204 ? 198.954 248.026 207.636 1.00 4.92  ? 2204 VAL A C     1 
ATOM   5782  O O     . VAL A 1 2204 ? 199.895 248.106 208.432 1.00 4.12  ? 2204 VAL A O     1 
ATOM   5783  C CB    . VAL A 1 2204 ? 198.736 250.012 206.063 1.00 3.23  ? 2204 VAL A CB    1 
ATOM   5784  C CG1   . VAL A 1 2204 ? 198.946 250.474 204.633 1.00 9.67  ? 2204 VAL A CG1   1 
ATOM   5785  C CG2   . VAL A 1 2204 ? 197.317 250.276 206.509 1.00 4.67  ? 2204 VAL A CG2   1 
ATOM   5786  N N     . GLU A 1 2205 ? 197.778 247.498 207.992 1.00 2.52  ? 2205 GLU A N     1 
ATOM   5787  C CA    . GLU A 1 2205 ? 197.638 246.870 209.303 1.00 0.00  ? 2205 GLU A CA    1 
ATOM   5788  C C     . GLU A 1 2205 ? 198.563 245.669 209.429 1.00 2.05  ? 2205 GLU A C     1 
ATOM   5789  O O     . GLU A 1 2205 ? 199.168 245.445 210.482 1.00 11.87 ? 2205 GLU A O     1 
ATOM   5790  C CB    . GLU A 1 2205 ? 196.188 246.460 209.562 1.00 1.17  ? 2205 GLU A CB    1 
ATOM   5791  C CG    . GLU A 1 2205 ? 195.188 247.603 209.550 1.00 7.77  ? 2205 GLU A CG    1 
ATOM   5792  C CD    . GLU A 1 2205 ? 195.260 248.461 210.797 1.00 13.62 ? 2205 GLU A CD    1 
ATOM   5793  O OE1   . GLU A 1 2205 ? 195.608 247.927 211.870 1.00 12.32 ? 2205 GLU A OE1   1 
ATOM   5794  O OE2   . GLU A 1 2205 ? 194.964 249.671 210.704 1.00 12.29 ? 2205 GLU A OE2   1 
ATOM   5795  N N     . LYS A 1 2206 ? 198.685 244.881 208.360 1.00 4.72  ? 2206 LYS A N     1 
ATOM   5796  C CA    . LYS A 1 2206 ? 199.611 243.753 208.387 1.00 3.86  ? 2206 LYS A CA    1 
ATOM   5797  C C     . LYS A 1 2206 ? 201.053 244.228 208.508 1.00 3.53  ? 2206 LYS A C     1 
ATOM   5798  O O     . LYS A 1 2206 ? 201.863 243.595 209.192 1.00 11.74 ? 2206 LYS A O     1 
ATOM   5799  C CB    . LYS A 1 2206 ? 199.426 242.890 207.141 1.00 0.00  ? 2206 LYS A CB    1 
ATOM   5800  C CG    . LYS A 1 2206 ? 198.148 242.079 207.164 1.00 0.00  ? 2206 LYS A CG    1 
ATOM   5801  C CD    . LYS A 1 2206 ? 198.191 241.012 208.238 1.00 0.00  ? 2206 LYS A CD    1 
ATOM   5802  C CE    . LYS A 1 2206 ? 196.824 240.386 208.437 1.00 9.07  ? 2206 LYS A CE    1 
ATOM   5803  N NZ    . LYS A 1 2206 ? 196.842 239.356 209.510 1.00 6.29  ? 2206 LYS A NZ    1 
ATOM   5804  N N     . VAL A 1 2207 ? 201.391 245.340 207.854 1.00 0.00  ? 2207 VAL A N     1 
ATOM   5805  C CA    . VAL A 1 2207 ? 202.734 245.905 207.995 1.00 0.87  ? 2207 VAL A CA    1 
ATOM   5806  C C     . VAL A 1 2207 ? 202.986 246.338 209.435 1.00 5.56  ? 2207 VAL A C     1 
ATOM   5807  O O     . VAL A 1 2207 ? 204.072 246.122 209.986 1.00 7.74  ? 2207 VAL A O     1 
ATOM   5808  C CB    . VAL A 1 2207 ? 202.936 247.073 207.012 1.00 7.06  ? 2207 VAL A CB    1 
ATOM   5809  C CG1   . VAL A 1 2207 ? 204.291 247.723 207.235 1.00 1.97  ? 2207 VAL A CG1   1 
ATOM   5810  C CG2   . VAL A 1 2207 ? 202.813 246.591 205.581 1.00 9.85  ? 2207 VAL A CG2   1 
ATOM   5811  N N     . LEU A 1 2208 ? 201.992 246.970 210.063 1.00 6.83  ? 2208 LEU A N     1 
ATOM   5812  C CA    . LEU A 1 2208 ? 202.140 247.397 211.451 1.00 0.69  ? 2208 LEU A CA    1 
ATOM   5813  C C     . LEU A 1 2208 ? 202.292 246.202 212.387 1.00 2.28  ? 2208 LEU A C     1 
ATOM   5814  O O     . LEU A 1 2208 ? 203.102 246.234 213.322 1.00 13.06 ? 2208 LEU A O     1 
ATOM   5815  C CB    . LEU A 1 2208 ? 200.947 248.257 211.863 1.00 2.38  ? 2208 LEU A CB    1 
ATOM   5816  C CG    . LEU A 1 2208 ? 200.750 249.551 211.071 1.00 0.53  ? 2208 LEU A CG    1 
ATOM   5817  C CD1   . LEU A 1 2208 ? 199.462 250.234 211.480 1.00 2.77  ? 2208 LEU A CD1   1 
ATOM   5818  C CD2   . LEU A 1 2208 ? 201.935 250.485 211.236 1.00 3.93  ? 2208 LEU A CD2   1 
ATOM   5819  N N     . GLN A 1 2209 ? 201.515 245.140 212.158 1.00 1.41  ? 2209 GLN A N     1 
ATOM   5820  C CA    . GLN A 1 2209 ? 201.675 243.926 212.954 1.00 0.00  ? 2209 GLN A CA    1 
ATOM   5821  C C     . GLN A 1 2209 ? 203.054 243.316 212.750 1.00 0.00  ? 2209 GLN A C     1 
ATOM   5822  O O     . GLN A 1 2209 ? 203.666 242.807 213.697 1.00 1.42  ? 2209 GLN A O     1 
ATOM   5823  C CB    . GLN A 1 2209 ? 200.586 242.912 212.605 1.00 1.17  ? 2209 GLN A CB    1 
ATOM   5824  C CG    . GLN A 1 2209 ? 199.173 243.415 212.814 1.00 0.31  ? 2209 GLN A CG    1 
ATOM   5825  C CD    . GLN A 1 2209 ? 198.139 242.559 212.120 1.00 0.00  ? 2209 GLN A CD    1 
ATOM   5826  O OE1   . GLN A 1 2209 ? 198.400 241.411 211.779 1.00 3.46  ? 2209 GLN A OE1   1 
ATOM   5827  N NE2   . GLN A 1 2209 ? 196.949 243.110 211.923 1.00 5.33  ? 2209 GLN A NE2   1 
ATOM   5828  N N     . LEU A 1 2210 ? 203.555 243.357 211.517 1.00 0.00  ? 2210 LEU A N     1 
ATOM   5829  C CA    . LEU A 1 2210 ? 204.897 242.869 211.237 1.00 1.05  ? 2210 LEU A CA    1 
ATOM   5830  C C     . LEU A 1 2210 ? 205.935 243.681 212.001 1.00 7.16  ? 2210 LEU A C     1 
ATOM   5831  O O     . LEU A 1 2210 ? 206.896 243.125 212.548 1.00 19.19 ? 2210 LEU A O     1 
ATOM   5832  C CB    . LEU A 1 2210 ? 205.143 242.929 209.730 1.00 0.04  ? 2210 LEU A CB    1 
ATOM   5833  C CG    . LEU A 1 2210 ? 206.271 242.141 209.073 1.00 2.02  ? 2210 LEU A CG    1 
ATOM   5834  C CD1   . LEU A 1 2210 ? 205.848 241.783 207.668 1.00 12.44 ? 2210 LEU A CD1   1 
ATOM   5835  C CD2   . LEU A 1 2210 ? 207.559 242.920 209.043 1.00 4.49  ? 2210 LEU A CD2   1 
ATOM   5836  N N     . TYR A 1 2211 ? 205.743 245.001 212.064 1.00 3.10  ? 2211 TYR A N     1 
ATOM   5837  C CA    . TYR A 1 2211 ? 206.633 245.851 212.849 1.00 5.51  ? 2211 TYR A CA    1 
ATOM   5838  C C     . TYR A 1 2211 ? 206.590 245.478 214.325 1.00 6.09  ? 2211 TYR A C     1 
ATOM   5839  O O     . TYR A 1 2211 ? 207.631 245.410 214.989 1.00 9.50  ? 2211 TYR A O     1 
ATOM   5840  C CB    . TYR A 1 2211 ? 206.258 247.321 212.668 1.00 3.18  ? 2211 TYR A CB    1 
ATOM   5841  C CG    . TYR A 1 2211 ? 207.107 248.268 213.486 1.00 4.55  ? 2211 TYR A CG    1 
ATOM   5842  C CD1   . TYR A 1 2211 ? 208.491 248.166 213.485 1.00 5.02  ? 2211 TYR A CD1   1 
ATOM   5843  C CD2   . TYR A 1 2211 ? 206.525 249.255 214.270 1.00 9.76  ? 2211 TYR A CD2   1 
ATOM   5844  C CE1   . TYR A 1 2211 ? 209.272 249.025 214.231 1.00 9.65  ? 2211 TYR A CE1   1 
ATOM   5845  C CE2   . TYR A 1 2211 ? 207.299 250.120 215.021 1.00 12.14 ? 2211 TYR A CE2   1 
ATOM   5846  C CZ    . TYR A 1 2211 ? 208.672 249.999 214.998 1.00 12.20 ? 2211 TYR A CZ    1 
ATOM   5847  O OH    . TYR A 1 2211 ? 209.449 250.856 215.743 1.00 13.75 ? 2211 TYR A OH    1 
ATOM   5848  N N     . GLN A 1 2212 ? 205.390 245.239 214.856 1.00 4.86  ? 2212 GLN A N     1 
ATOM   5849  C CA    . GLN A 1 2212 ? 205.271 244.860 216.260 1.00 3.45  ? 2212 GLN A CA    1 
ATOM   5850  C C     . GLN A 1 2212 ? 205.985 243.544 216.544 1.00 8.51  ? 2212 GLN A C     1 
ATOM   5851  O O     . GLN A 1 2212 ? 206.683 243.415 217.557 1.00 16.95 ? 2212 GLN A O     1 
ATOM   5852  C CB    . GLN A 1 2212 ? 203.800 244.775 216.661 1.00 5.10  ? 2212 GLN A CB    1 
ATOM   5853  C CG    . GLN A 1 2212 ? 203.060 246.088 216.533 1.00 10.19 ? 2212 GLN A CG    1 
ATOM   5854  C CD    . GLN A 1 2212 ? 203.826 247.241 217.150 1.00 11.94 ? 2212 GLN A CD    1 
ATOM   5855  O OE1   . GLN A 1 2212 ? 204.352 248.099 216.444 1.00 13.15 ? 2212 GLN A OE1   1 
ATOM   5856  N NE2   . GLN A 1 2212 ? 203.890 247.268 218.476 1.00 12.74 ? 2212 GLN A NE2   1 
ATOM   5857  N N     . ILE A 1 2213 ? 205.830 242.556 215.661 1.00 3.88  ? 2213 ILE A N     1 
ATOM   5858  C CA    . ILE A 1 2213 ? 206.493 241.275 215.893 1.00 5.86  ? 2213 ILE A CA    1 
ATOM   5859  C C     . ILE A 1 2213 ? 208.006 241.425 215.786 1.00 7.76  ? 2213 ILE A C     1 
ATOM   5860  O O     . ILE A 1 2213 ? 208.756 240.785 216.532 1.00 12.81 ? 2213 ILE A O     1 
ATOM   5861  C CB    . ILE A 1 2213 ? 205.960 240.191 214.941 1.00 4.03  ? 2213 ILE A CB    1 
ATOM   5862  C CG1   . ILE A 1 2213 ? 204.436 240.128 214.996 1.00 5.69  ? 2213 ILE A CG1   1 
ATOM   5863  C CG2   . ILE A 1 2213 ? 206.523 238.839 215.333 1.00 10.37 ? 2213 ILE A CG2   1 
ATOM   5864  C CD1   . ILE A 1 2213 ? 203.894 239.613 216.309 1.00 9.55  ? 2213 ILE A CD1   1 
ATOM   5865  N N     . THR A 1 2214 ? 208.484 242.266 214.865 1.00 2.55  ? 2214 THR A N     1 
ATOM   5866  C CA    . THR A 1 2214 ? 209.920 242.530 214.806 1.00 7.80  ? 2214 THR A CA    1 
ATOM   5867  C C     . THR A 1 2214 ? 210.408 243.186 216.090 1.00 15.64 ? 2214 THR A C     1 
ATOM   5868  O O     . THR A 1 2214 ? 211.522 242.914 216.553 1.00 19.83 ? 2214 THR A O     1 
ATOM   5869  C CB    . THR A 1 2214 ? 210.259 243.408 213.602 1.00 9.38  ? 2214 THR A CB    1 
ATOM   5870  O OG1   . THR A 1 2214 ? 209.480 244.609 213.649 1.00 11.02 ? 2214 THR A OG1   1 
ATOM   5871  C CG2   . THR A 1 2214 ? 209.990 242.670 212.302 1.00 13.13 ? 2214 THR A CG2   1 
ATOM   5872  N N     . GLN A 1 2215 ? 209.591 244.068 216.672 1.00 13.87 ? 2215 GLN A N     1 
ATOM   5873  C CA    . GLN A 1 2215 ? 209.943 244.664 217.957 1.00 9.62  ? 2215 GLN A CA    1 
ATOM   5874  C C     . GLN A 1 2215 ? 210.025 243.606 219.050 1.00 9.17  ? 2215 GLN A C     1 
ATOM   5875  O O     . GLN A 1 2215 ? 210.947 243.621 219.873 1.00 8.28  ? 2215 GLN A O     1 
ATOM   5876  C CB    . GLN A 1 2215 ? 208.928 245.742 218.335 1.00 5.14  ? 2215 GLN A CB    1 
ATOM   5877  C CG    . GLN A 1 2215 ? 209.010 247.005 217.495 1.00 11.98 ? 2215 GLN A CG    1 
ATOM   5878  C CD    . GLN A 1 2215 ? 210.197 247.876 217.858 1.00 17.60 ? 2215 GLN A CD    1 
ATOM   5879  O OE1   . GLN A 1 2215 ? 210.077 248.808 218.652 1.00 14.54 ? 2215 GLN A OE1   1 
ATOM   5880  N NE2   . GLN A 1 2215 ? 211.350 247.581 217.268 1.00 20.06 ? 2215 GLN A NE2   1 
ATOM   5881  N N     . ILE A 1 2216 ? 209.072 242.674 219.071 1.00 9.66  ? 2216 ILE A N     1 
ATOM   5882  C CA    . ILE A 1 2216 ? 209.027 241.673 220.134 1.00 8.03  ? 2216 ILE A CA    1 
ATOM   5883  C C     . ILE A 1 2216 ? 209.993 240.530 219.850 1.00 12.07 ? 2216 ILE A C     1 
ATOM   5884  O O     . ILE A 1 2216 ? 210.925 240.274 220.622 1.00 17.81 ? 2216 ILE A O     1 
ATOM   5885  C CB    . ILE A 1 2216 ? 207.590 241.156 220.326 1.00 8.81  ? 2216 ILE A CB    1 
ATOM   5886  C CG1   . ILE A 1 2216 ? 206.634 242.323 220.573 1.00 13.16 ? 2216 ILE A CG1   1 
ATOM   5887  C CG2   . ILE A 1 2216 ? 207.532 240.161 221.468 1.00 13.22 ? 2216 ILE A CG2   1 
ATOM   5888  C CD1   . ILE A 1 2216 ? 206.983 243.147 221.793 1.00 14.04 ? 2216 ILE A CD1   1 
ATOM   5889  N N     . ASN A 1 2217 ? 209.786 239.824 218.744 1.00 11.22 ? 2217 ASN A N     1 
ATOM   5890  C CA    . ASN A 1 2217 ? 210.560 238.636 218.425 1.00 6.50  ? 2217 ASN A CA    1 
ATOM   5891  C C     . ASN A 1 2217 ? 211.778 238.994 217.581 1.00 7.10  ? 2217 ASN A C     1 
ATOM   5892  O O     . ASN A 1 2217 ? 212.048 240.159 217.282 1.00 8.17  ? 2217 ASN A O     1 
ATOM   5893  C CB    . ASN A 1 2217 ? 209.690 237.607 217.701 1.00 5.79  ? 2217 ASN A CB    1 
ATOM   5894  C CG    . ASN A 1 2217 ? 208.756 236.871 218.635 1.00 14.15 ? 2217 ASN A CG    1 
ATOM   5895  O OD1   . ASN A 1 2217 ? 207.549 237.109 218.640 1.00 20.08 ? 2217 ASN A OD1   1 
ATOM   5896  N ND2   . ASN A 1 2217 ? 209.310 235.964 219.428 1.00 16.38 ? 2217 ASN A ND2   1 
ATOM   5897  N N     . HIS A 1 2218 ? 212.527 237.962 217.196 1.00 9.74  ? 2218 HIS A N     1 
ATOM   5898  C CA    . HIS A 1 2218 ? 213.655 238.128 216.293 1.00 9.63  ? 2218 HIS A CA    1 
ATOM   5899  C C     . HIS A 1 2218 ? 213.669 237.106 215.165 1.00 9.29  ? 2218 HIS A C     1 
ATOM   5900  O O     . HIS A 1 2218 ? 214.526 237.203 214.283 1.00 15.44 ? 2218 HIS A O     1 
ATOM   5901  C CB    . HIS A 1 2218 ? 214.979 238.053 217.070 1.00 13.64 ? 2218 HIS A CB    1 
ATOM   5902  C CG    . HIS A 1 2218 ? 215.232 236.722 217.708 1.00 13.35 ? 2218 HIS A CG    1 
ATOM   5903  N ND1   . HIS A 1 2218 ? 214.803 236.413 218.980 1.00 14.08 ? 2218 HIS A ND1   1 
ATOM   5904  C CD2   . HIS A 1 2218 ? 215.883 235.626 217.253 1.00 12.18 ? 2218 HIS A CD2   1 
ATOM   5905  C CE1   . HIS A 1 2218 ? 215.169 235.178 219.277 1.00 15.42 ? 2218 HIS A CE1   1 
ATOM   5906  N NE2   . HIS A 1 2218 ? 215.827 234.679 218.246 1.00 15.26 ? 2218 HIS A NE2   1 
ATOM   5907  N N     . GLY A 1 2219 ? 212.756 236.138 215.161 1.00 4.59  ? 2219 GLY A N     1 
ATOM   5908  C CA    . GLY A 1 2219 ? 212.704 235.144 214.108 1.00 2.13  ? 2219 GLY A CA    1 
ATOM   5909  C C     . GLY A 1 2219 ? 211.403 235.152 213.331 1.00 6.30  ? 2219 GLY A C     1 
ATOM   5910  O O     . GLY A 1 2219 ? 210.910 234.091 212.940 1.00 12.84 ? 2219 GLY A O     1 
ATOM   5911  N N     . LEU A 1 2220 ? 210.863 236.347 213.079 1.00 3.52  ? 2220 LEU A N     1 
ATOM   5912  C CA    . LEU A 1 2220 ? 209.563 236.513 212.433 1.00 2.90  ? 2220 LEU A CA    1 
ATOM   5913  C C     . LEU A 1 2220 ? 209.418 235.633 211.197 1.00 2.33  ? 2220 LEU A C     1 
ATOM   5914  O O     . LEU A 1 2220 ? 210.392 235.312 210.514 1.00 9.00  ? 2220 LEU A O     1 
ATOM   5915  C CB    . LEU A 1 2220 ? 209.360 237.981 212.056 1.00 1.32  ? 2220 LEU A CB    1 
ATOM   5916  C CG    . LEU A 1 2220 ? 208.178 238.353 211.163 1.00 11.05 ? 2220 LEU A CG    1 
ATOM   5917  C CD1   . LEU A 1 2220 ? 206.860 238.250 211.905 1.00 16.31 ? 2220 LEU A CD1   1 
ATOM   5918  C CD2   . LEU A 1 2220 ? 208.395 239.755 210.647 1.00 9.40  ? 2220 LEU A CD2   1 
ATOM   5919  N N     . MET A 1 2221 ? 208.172 235.247 210.909 1.00 0.80  ? 2221 MET A N     1 
ATOM   5920  C CA    . MET A 1 2221 ? 207.851 234.321 209.819 1.00 2.42  ? 2221 MET A CA    1 
ATOM   5921  C C     . MET A 1 2221 ? 206.590 234.822 209.113 1.00 3.18  ? 2221 MET A C     1 
ATOM   5922  O O     . MET A 1 2221 ? 205.473 234.538 209.546 1.00 3.17  ? 2221 MET A O     1 
ATOM   5923  C CB    . MET A 1 2221 ? 207.672 232.911 210.365 1.00 0.00  ? 2221 MET A CB    1 
ATOM   5924  C CG    . MET A 1 2221 ? 207.451 231.840 209.316 1.00 6.91  ? 2221 MET A CG    1 
ATOM   5925  S SD    . MET A 1 2221 ? 207.257 230.211 210.058 1.00 17.53 ? 2221 MET A SD    1 
ATOM   5926  C CE    . MET A 1 2221 ? 208.934 229.888 210.590 1.00 9.05  ? 2221 MET A CE    1 
ATOM   5927  N N     . MET A 1 2222 ? 206.775 235.556 208.016 1.00 7.83  ? 2222 MET A N     1 
ATOM   5928  C CA    . MET A 1 2222 ? 205.639 236.043 207.241 1.00 2.18  ? 2222 MET A CA    1 
ATOM   5929  C C     . MET A 1 2222 ? 205.082 234.931 206.360 1.00 0.98  ? 2222 MET A C     1 
ATOM   5930  O O     . MET A 1 2222 ? 205.766 234.437 205.460 1.00 8.11  ? 2222 MET A O     1 
ATOM   5931  C CB    . MET A 1 2222 ? 206.051 237.235 206.378 1.00 0.94  ? 2222 MET A CB    1 
ATOM   5932  C CG    . MET A 1 2222 ? 206.818 238.313 207.118 1.00 10.60 ? 2222 MET A CG    1 
ATOM   5933  S SD    . MET A 1 2222 ? 207.865 239.290 206.025 1.00 9.17  ? 2222 MET A SD    1 
ATOM   5934  C CE    . MET A 1 2222 ? 209.298 238.230 205.899 1.00 6.68  ? 2222 MET A CE    1 
ATOM   5935  N N     . VAL A 1 2223 ? 203.832 234.546 206.610 1.00 0.00  ? 2223 VAL A N     1 
ATOM   5936  C CA    . VAL A 1 2223 ? 203.219 233.407 205.941 1.00 0.00  ? 2223 VAL A CA    1 
ATOM   5937  C C     . VAL A 1 2223 ? 201.907 233.843 205.308 1.00 0.00  ? 2223 VAL A C     1 
ATOM   5938  O O     . VAL A 1 2223 ? 201.144 234.622 205.887 1.00 6.26  ? 2223 VAL A O     1 
ATOM   5939  C CB    . VAL A 1 2223 ? 202.979 232.229 206.909 1.00 0.15  ? 2223 VAL A CB    1 
ATOM   5940  C CG1   . VAL A 1 2223 ? 202.595 230.984 206.139 1.00 7.33  ? 2223 VAL A CG1   1 
ATOM   5941  C CG2   . VAL A 1 2223 ? 204.204 231.976 207.761 1.00 5.51  ? 2223 VAL A CG2   1 
ATOM   5942  N N     . GLY A 1 2224 ? 201.648 233.335 204.108 1.00 0.43  ? 2224 GLY A N     1 
ATOM   5943  C CA    . GLY A 1 2224 ? 200.408 233.594 203.422 1.00 0.00  ? 2224 GLY A CA    1 
ATOM   5944  C C     . GLY A 1 2224 ? 200.410 233.043 202.012 1.00 0.00  ? 2224 GLY A C     1 
ATOM   5945  O O     . GLY A 1 2224 ? 201.458 232.691 201.464 1.00 5.67  ? 2224 GLY A O     1 
ATOM   5946  N N     . PRO A 1 2225 ? 199.232 232.958 201.397 1.00 0.00  ? 2225 PRO A N     1 
ATOM   5947  C CA    . PRO A 1 2225 ? 199.157 232.467 200.018 1.00 0.00  ? 2225 PRO A CA    1 
ATOM   5948  C C     . PRO A 1 2225 ? 199.955 233.346 199.074 1.00 2.86  ? 2225 PRO A C     1 
ATOM   5949  O O     . PRO A 1 2225 ? 200.043 234.563 199.247 1.00 10.45 ? 2225 PRO A O     1 
ATOM   5950  C CB    . PRO A 1 2225 ? 197.657 232.530 199.700 1.00 0.00  ? 2225 PRO A CB    1 
ATOM   5951  C CG    . PRO A 1 2225 ? 196.989 232.558 201.035 1.00 3.76  ? 2225 PRO A CG    1 
ATOM   5952  C CD    . PRO A 1 2225 ? 197.909 233.343 201.906 1.00 8.53  ? 2225 PRO A CD    1 
ATOM   5953  N N     . SER A 1 2226 ? 200.556 232.708 198.073 1.00 2.32  ? 2226 SER A N     1 
ATOM   5954  C CA    . SER A 1 2226 ? 201.373 233.442 197.119 1.00 0.00  ? 2226 SER A CA    1 
ATOM   5955  C C     . SER A 1 2226 ? 200.521 234.459 196.374 1.00 2.44  ? 2226 SER A C     1 
ATOM   5956  O O     . SER A 1 2226 ? 199.425 234.151 195.901 1.00 10.19 ? 2226 SER A O     1 
ATOM   5957  C CB    . SER A 1 2226 ? 202.038 232.486 196.132 1.00 7.04  ? 2226 SER A CB    1 
ATOM   5958  O OG    . SER A 1 2226 ? 202.720 233.205 195.120 1.00 8.09  ? 2226 SER A OG    1 
ATOM   5959  N N     . GLY A 1 2227 ? 201.034 235.679 196.273 1.00 5.96  ? 2227 GLY A N     1 
ATOM   5960  C CA    . GLY A 1 2227 ? 200.295 236.789 195.715 1.00 4.20  ? 2227 GLY A CA    1 
ATOM   5961  C C     . GLY A 1 2227 ? 199.879 237.830 196.725 1.00 5.84  ? 2227 GLY A C     1 
ATOM   5962  O O     . GLY A 1 2227 ? 199.426 238.908 196.324 1.00 7.57  ? 2227 GLY A O     1 
ATOM   5963  N N     . SER A 1 2228 ? 199.999 237.544 198.018 1.00 8.20  ? 2228 SER A N     1 
ATOM   5964  C CA    . SER A 1 2228 ? 199.799 238.557 199.039 1.00 2.66  ? 2228 SER A CA    1 
ATOM   5965  C C     . SER A 1 2228 ? 201.056 239.412 199.171 1.00 1.33  ? 2228 SER A C     1 
ATOM   5966  O O     . SER A 1 2228 ? 202.163 238.999 198.817 1.00 7.75  ? 2228 SER A O     1 
ATOM   5967  C CB    . SER A 1 2228 ? 199.445 237.912 200.376 1.00 1.46  ? 2228 SER A CB    1 
ATOM   5968  O OG    . SER A 1 2228 ? 198.196 237.252 200.304 1.00 2.59  ? 2228 SER A OG    1 
ATOM   5969  N N     . GLY A 1 2229 ? 200.877 240.621 199.691 1.00 0.00  ? 2229 GLY A N     1 
ATOM   5970  C CA    . GLY A 1 2229 ? 201.974 241.561 199.762 1.00 0.00  ? 2229 GLY A CA    1 
ATOM   5971  C C     . GLY A 1 2229 ? 202.919 241.331 200.922 1.00 0.00  ? 2229 GLY A C     1 
ATOM   5972  O O     . GLY A 1 2229 ? 203.092 242.219 201.756 1.00 2.66  ? 2229 GLY A O     1 
ATOM   5973  N N     . LYS A 1 2230 ? 203.539 240.151 200.988 1.00 0.00  ? 2230 LYS A N     1 
ATOM   5974  C CA    . LYS A 1 2230 ? 204.498 239.871 202.054 1.00 0.00  ? 2230 LYS A CA    1 
ATOM   5975  C C     . LYS A 1 2230 ? 205.816 240.597 201.818 1.00 4.06  ? 2230 LYS A C     1 
ATOM   5976  O O     . LYS A 1 2230 ? 206.274 241.376 202.666 1.00 17.15 ? 2230 LYS A O     1 
ATOM   5977  C CB    . LYS A 1 2230 ? 204.744 238.367 202.163 1.00 0.00  ? 2230 LYS A CB    1 
ATOM   5978  C CG    . LYS A 1 2230 ? 203.568 237.564 202.670 1.00 0.00  ? 2230 LYS A CG    1 
ATOM   5979  C CD    . LYS A 1 2230 ? 203.890 236.080 202.710 1.00 3.98  ? 2230 LYS A CD    1 
ATOM   5980  C CE    . LYS A 1 2230 ? 204.061 235.499 201.321 1.00 3.57  ? 2230 LYS A CE    1 
ATOM   5981  N NZ    . LYS A 1 2230 ? 202.818 235.627 200.512 1.00 1.27  ? 2230 LYS A NZ    1 
ATOM   5982  N N     . SER A 1 2231 ? 206.452 240.331 200.675 1.00 0.73  ? 2231 SER A N     1 
ATOM   5983  C CA    . SER A 1 2231 ? 207.746 240.937 200.383 1.00 0.00  ? 2231 SER A CA    1 
ATOM   5984  C C     . SER A 1 2231 ? 207.632 242.450 200.325 1.00 0.00  ? 2231 SER A C     1 
ATOM   5985  O O     . SER A 1 2231 ? 208.499 243.172 200.830 1.00 0.08  ? 2231 SER A O     1 
ATOM   5986  C CB    . SER A 1 2231 ? 208.301 240.388 199.072 1.00 3.32  ? 2231 SER A CB    1 
ATOM   5987  O OG    . SER A 1 2231 ? 209.577 240.930 198.787 1.00 13.21 ? 2231 SER A OG    1 
ATOM   5988  N N     . MET A 1 2232 ? 206.558 242.946 199.713 1.00 0.00  ? 2232 MET A N     1 
ATOM   5989  C CA    . MET A 1 2232 ? 206.326 244.382 199.696 1.00 4.39  ? 2232 MET A CA    1 
ATOM   5990  C C     . MET A 1 2232 ? 206.164 244.920 201.109 1.00 6.64  ? 2232 MET A C     1 
ATOM   5991  O O     . MET A 1 2232 ? 206.688 245.990 201.434 1.00 13.32 ? 2232 MET A O     1 
ATOM   5992  C CB    . MET A 1 2232 ? 205.097 244.706 198.852 1.00 0.00  ? 2232 MET A CB    1 
ATOM   5993  C CG    . MET A 1 2232 ? 205.353 244.931 197.358 1.00 4.82  ? 2232 MET A CG    1 
ATOM   5994  S SD    . MET A 1 2232 ? 206.581 246.177 196.902 1.00 14.01 ? 2232 MET A SD    1 
ATOM   5995  C CE    . MET A 1 2232 ? 208.107 245.234 196.892 1.00 2.56  ? 2232 MET A CE    1 
ATOM   5996  N N     . ALA A 1 2233 ? 205.454 244.184 201.967 1.00 5.60  ? 2233 ALA A N     1 
ATOM   5997  C CA    . ALA A 1 2233 ? 205.264 244.628 203.343 1.00 3.19  ? 2233 ALA A CA    1 
ATOM   5998  C C     . ALA A 1 2233 ? 206.595 244.789 204.060 1.00 1.67  ? 2233 ALA A C     1 
ATOM   5999  O O     . ALA A 1 2233 ? 206.862 245.834 204.663 1.00 5.57  ? 2233 ALA A O     1 
ATOM   6000  C CB    . ALA A 1 2233 ? 204.373 243.647 204.102 1.00 0.00  ? 2233 ALA A CB    1 
ATOM   6001  N N     . TRP A 1 2234 ? 207.454 243.768 204.004 1.00 4.30  ? 2234 TRP A N     1 
ATOM   6002  C CA    . TRP A 1 2234 ? 208.688 243.886 204.775 1.00 5.69  ? 2234 TRP A CA    1 
ATOM   6003  C C     . TRP A 1 2234 ? 209.671 244.856 204.130 1.00 12.34 ? 2234 TRP A C     1 
ATOM   6004  O O     . TRP A 1 2234 ? 210.434 245.516 204.844 1.00 21.12 ? 2234 TRP A O     1 
ATOM   6005  C CB    . TRP A 1 2234 ? 209.328 242.515 205.030 1.00 0.00  ? 2234 TRP A CB    1 
ATOM   6006  C CG    . TRP A 1 2234 ? 209.983 241.804 203.883 1.00 0.56  ? 2234 TRP A CG    1 
ATOM   6007  C CD1   . TRP A 1 2234 ? 209.502 240.714 203.225 1.00 4.10  ? 2234 TRP A CD1   1 
ATOM   6008  C CD2   . TRP A 1 2234 ? 211.263 242.090 203.299 1.00 2.45  ? 2234 TRP A CD2   1 
ATOM   6009  N NE1   . TRP A 1 2234 ? 210.384 240.316 202.254 1.00 0.00  ? 2234 TRP A NE1   1 
ATOM   6010  C CE2   . TRP A 1 2234 ? 211.473 241.145 202.277 1.00 6.11  ? 2234 TRP A CE2   1 
ATOM   6011  C CE3   . TRP A 1 2234 ? 212.242 243.060 203.530 1.00 6.54  ? 2234 TRP A CE3   1 
ATOM   6012  C CZ2   . TRP A 1 2234 ? 212.619 241.142 201.488 1.00 7.96  ? 2234 TRP A CZ2   1 
ATOM   6013  C CZ3   . TRP A 1 2234 ? 213.378 243.056 202.745 1.00 7.34  ? 2234 TRP A CZ3   1 
ATOM   6014  C CH2   . TRP A 1 2234 ? 213.558 242.104 201.737 1.00 5.30  ? 2234 TRP A CH2   1 
ATOM   6015  N N     . ARG A 1 2235 ? 209.648 245.000 202.802 1.00 5.78  ? 2235 ARG A N     1 
ATOM   6016  C CA    . ARG A 1 2235 ? 210.490 246.009 202.166 1.00 5.53  ? 2235 ARG A CA    1 
ATOM   6017  C C     . ARG A 1 2235 ? 210.061 247.416 202.568 1.00 8.41  ? 2235 ARG A C     1 
ATOM   6018  O O     . ARG A 1 2235 ? 210.899 248.267 202.903 1.00 16.24 ? 2235 ARG A O     1 
ATOM   6019  C CB    . ARG A 1 2235 ? 210.440 245.847 200.648 1.00 4.25  ? 2235 ARG A CB    1 
ATOM   6020  C CG    . ARG A 1 2235 ? 211.257 244.689 200.112 1.00 5.87  ? 2235 ARG A CG    1 
ATOM   6021  C CD    . ARG A 1 2235 ? 211.287 244.725 198.599 1.00 5.19  ? 2235 ARG A CD    1 
ATOM   6022  N NE    . ARG A 1 2235 ? 211.811 243.494 198.022 1.00 2.37  ? 2235 ARG A NE    1 
ATOM   6023  C CZ    . ARG A 1 2235 ? 213.100 243.238 197.855 1.00 6.85  ? 2235 ARG A CZ    1 
ATOM   6024  N NH1   . ARG A 1 2235 ? 214.030 244.100 198.228 1.00 7.50  ? 2235 ARG A NH1   1 
ATOM   6025  N NH2   . ARG A 1 2235 ? 213.464 242.090 197.291 1.00 10.15 ? 2235 ARG A NH2   1 
ATOM   6026  N N     . VAL A 1 2236 ? 208.752 247.679 202.543 1.00 2.90  ? 2236 VAL A N     1 
ATOM   6027  C CA    . VAL A 1 2236 ? 208.245 248.987 202.938 1.00 2.71  ? 2236 VAL A CA    1 
ATOM   6028  C C     . VAL A 1 2236 ? 208.530 249.245 204.408 1.00 7.29  ? 2236 VAL A C     1 
ATOM   6029  O O     . VAL A 1 2236 ? 208.857 250.370 204.798 1.00 13.65 ? 2236 VAL A O     1 
ATOM   6030  C CB    . VAL A 1 2236 ? 206.744 249.097 202.618 1.00 2.52  ? 2236 VAL A CB    1 
ATOM   6031  C CG1   . VAL A 1 2236 ? 206.164 250.367 203.202 1.00 0.97  ? 2236 VAL A CG1   1 
ATOM   6032  C CG2   . VAL A 1 2236 ? 206.533 249.087 201.126 1.00 3.55  ? 2236 VAL A CG2   1 
ATOM   6033  N N     . LEU A 1 2237 ? 208.422 248.214 205.249 1.00 11.62 ? 2237 LEU A N     1 
ATOM   6034  C CA    . LEU A 1 2237 ? 208.750 248.395 206.657 1.00 13.52 ? 2237 LEU A CA    1 
ATOM   6035  C C     . LEU A 1 2237 ? 210.224 248.721 206.844 1.00 10.55 ? 2237 LEU A C     1 
ATOM   6036  O O     . LEU A 1 2237 ? 210.574 249.580 207.658 1.00 17.03 ? 2237 LEU A O     1 
ATOM   6037  C CB    . LEU A 1 2237 ? 208.385 247.154 207.464 1.00 9.34  ? 2237 LEU A CB    1 
ATOM   6038  C CG    . LEU A 1 2237 ? 208.472 247.467 208.958 1.00 6.30  ? 2237 LEU A CG    1 
ATOM   6039  C CD1   . LEU A 1 2237 ? 207.351 248.417 209.356 1.00 9.95  ? 2237 LEU A CD1   1 
ATOM   6040  C CD2   . LEU A 1 2237 ? 208.462 246.215 209.799 1.00 7.93  ? 2237 LEU A CD2   1 
ATOM   6041  N N     . LEU A 1 2238 ? 211.105 248.036 206.114 1.00 6.24  ? 2238 LEU A N     1 
ATOM   6042  C CA    . LEU A 1 2238 ? 212.531 248.319 206.229 1.00 11.26 ? 2238 LEU A CA    1 
ATOM   6043  C C     . LEU A 1 2238 ? 212.837 249.756 205.828 1.00 10.96 ? 2238 LEU A C     1 
ATOM   6044  O O     . LEU A 1 2238 ? 213.569 250.467 206.527 1.00 15.21 ? 2238 LEU A O     1 
ATOM   6045  C CB    . LEU A 1 2238 ? 213.329 247.337 205.372 1.00 10.70 ? 2238 LEU A CB    1 
ATOM   6046  C CG    . LEU A 1 2238 ? 214.832 247.267 205.643 1.00 13.06 ? 2238 LEU A CG    1 
ATOM   6047  C CD1   . LEU A 1 2238 ? 215.106 247.177 207.135 1.00 10.95 ? 2238 LEU A CD1   1 
ATOM   6048  C CD2   . LEU A 1 2238 ? 215.450 246.089 204.911 1.00 16.06 ? 2238 LEU A CD2   1 
ATOM   6049  N N     . LYS A 1 2239 ? 212.265 250.209 204.710 1.00 6.50  ? 2239 LYS A N     1 
ATOM   6050  C CA    . LYS A 1 2239 ? 212.513 251.583 204.279 1.00 6.27  ? 2239 LYS A CA    1 
ATOM   6051  C C     . LYS A 1 2239 ? 211.918 252.594 205.254 1.00 11.19 ? 2239 LYS A C     1 
ATOM   6052  O O     . LYS A 1 2239 ? 212.541 253.621 205.548 1.00 20.31 ? 2239 LYS A O     1 
ATOM   6053  C CB    . LYS A 1 2239 ? 211.973 251.806 202.868 1.00 9.27  ? 2239 LYS A CB    1 
ATOM   6054  C CG    . LYS A 1 2239 ? 212.451 250.784 201.853 1.00 15.42 ? 2239 LYS A CG    1 
ATOM   6055  C CD    . LYS A 1 2239 ? 213.972 250.747 201.790 1.00 13.59 ? 2239 LYS A CD    1 
ATOM   6056  C CE    . LYS A 1 2239 ? 214.461 249.761 200.742 1.00 11.17 ? 2239 LYS A CE    1 
ATOM   6057  N NZ    . LYS A 1 2239 ? 213.889 248.402 200.948 1.00 10.07 ? 2239 LYS A NZ    1 
ATOM   6058  N N     . ALA A 1 2240 ? 210.716 252.322 205.771 1.00 7.15  ? 2240 ALA A N     1 
ATOM   6059  C CA    . ALA A 1 2240 ? 210.090 253.238 206.718 1.00 9.20  ? 2240 ALA A CA    1 
ATOM   6060  C C     . ALA A 1 2240 ? 210.886 253.326 208.011 1.00 13.35 ? 2240 ALA A C     1 
ATOM   6061  O O     . ALA A 1 2240 ? 211.031 254.410 208.583 1.00 19.10 ? 2240 ALA A O     1 
ATOM   6062  C CB    . ALA A 1 2240 ? 208.654 252.801 207.000 1.00 14.61 ? 2240 ALA A CB    1 
ATOM   6063  N N     . LEU A 1 2241 ? 211.396 252.193 208.496 1.00 12.50 ? 2241 LEU A N     1 
ATOM   6064  C CA    . LEU A 1 2241 ? 212.233 252.205 209.689 1.00 10.41 ? 2241 LEU A CA    1 
ATOM   6065  C C     . LEU A 1 2241 ? 213.534 252.953 209.442 1.00 13.69 ? 2241 LEU A C     1 
ATOM   6066  O O     . LEU A 1 2241 ? 213.994 253.710 210.305 1.00 19.74 ? 2241 LEU A O     1 
ATOM   6067  C CB    . LEU A 1 2241 ? 212.508 250.775 210.149 1.00 11.62 ? 2241 LEU A CB    1 
ATOM   6068  C CG    . LEU A 1 2241 ? 211.597 250.250 211.258 1.00 14.54 ? 2241 LEU A CG    1 
ATOM   6069  C CD1   . LEU A 1 2241 ? 210.159 250.184 210.799 1.00 13.13 ? 2241 LEU A CD1   1 
ATOM   6070  C CD2   . LEU A 1 2241 ? 212.064 248.881 211.701 1.00 14.72 ? 2241 LEU A CD2   1 
ATOM   6071  N N     . GLU A 1 2242 ? 214.141 252.762 208.268 1.00 15.92 ? 2242 GLU A N     1 
ATOM   6072  C CA    . GLU A 1 2242 ? 215.368 253.486 207.957 1.00 15.03 ? 2242 GLU A CA    1 
ATOM   6073  C C     . GLU A 1 2242 ? 215.122 254.989 207.912 1.00 10.90 ? 2242 GLU A C     1 
ATOM   6074  O O     . GLU A 1 2242 ? 215.962 255.777 208.361 1.00 14.78 ? 2242 GLU A O     1 
ATOM   6075  C CB    . GLU A 1 2242 ? 215.952 252.990 206.635 1.00 17.36 ? 2242 GLU A CB    1 
ATOM   6076  C CG    . GLU A 1 2242 ? 217.178 253.759 206.168 1.00 18.28 ? 2242 GLU A CG    1 
ATOM   6077  C CD    . GLU A 1 2242 ? 217.309 253.792 204.659 1.00 21.74 ? 2242 GLU A CD    1 
ATOM   6078  O OE1   . GLU A 1 2242 ? 216.419 253.249 203.971 1.00 23.26 ? 2242 GLU A OE1   1 
ATOM   6079  O OE2   . GLU A 1 2242 ? 218.303 254.359 204.160 1.00 19.39 ? 2242 GLU A OE2   1 
ATOM   6080  N N     . ARG A 1 2243 ? 213.975 255.405 207.374 1.00 12.98 ? 2243 ARG A N     1 
ATOM   6081  C CA    . ARG A 1 2243 ? 213.660 256.830 207.329 1.00 16.49 ? 2243 ARG A CA    1 
ATOM   6082  C C     . ARG A 1 2243 ? 213.346 257.384 208.715 1.00 18.35 ? 2243 ARG A C     1 
ATOM   6083  O O     . ARG A 1 2243 ? 213.852 258.447 209.091 1.00 20.21 ? 2243 ARG A O     1 
ATOM   6084  C CB    . ARG A 1 2243 ? 212.488 257.077 206.381 1.00 16.70 ? 2243 ARG A CB    1 
ATOM   6085  C CG    . ARG A 1 2243 ? 212.872 257.062 204.917 1.00 17.16 ? 2243 ARG A CG    1 
ATOM   6086  C CD    . ARG A 1 2243 ? 211.676 257.346 204.030 1.00 16.38 ? 2243 ARG A CD    1 
ATOM   6087  N NE    . ARG A 1 2243 ? 212.057 257.388 202.625 1.00 20.23 ? 2243 ARG A NE    1 
ATOM   6088  C CZ    . ARG A 1 2243 ? 211.487 258.168 201.718 1.00 19.25 ? 2243 ARG A CZ    1 
ATOM   6089  N NH1   . ARG A 1 2243 ? 210.489 258.978 202.032 1.00 16.99 ? 2243 ARG A NH1   1 
ATOM   6090  N NH2   . ARG A 1 2243 ? 211.932 258.139 200.466 1.00 17.12 ? 2243 ARG A NH2   1 
ATOM   6091  N N     . LEU A 1 2244 ? 212.509 256.685 209.483 1.00 18.32 ? 2244 LEU A N     1 
ATOM   6092  C CA    . LEU A 1 2244 ? 212.045 257.213 210.763 1.00 19.00 ? 2244 LEU A CA    1 
ATOM   6093  C C     . LEU A 1 2244 ? 213.158 257.218 211.803 1.00 21.85 ? 2244 LEU A C     1 
ATOM   6094  O O     . LEU A 1 2244 ? 213.383 258.228 212.480 1.00 17.72 ? 2244 LEU A O     1 
ATOM   6095  C CB    . LEU A 1 2244 ? 210.852 256.394 211.255 1.00 15.95 ? 2244 LEU A CB    1 
ATOM   6096  C CG    . LEU A 1 2244 ? 210.185 256.837 212.557 1.00 21.18 ? 2244 LEU A CG    1 
ATOM   6097  C CD1   . LEU A 1 2244 ? 209.596 258.230 212.408 1.00 21.50 ? 2244 LEU A CD1   1 
ATOM   6098  C CD2   . LEU A 1 2244 ? 209.116 255.840 212.974 1.00 19.81 ? 2244 LEU A CD2   1 
ATOM   6099  N N     . GLU A 1 2245 ? 213.866 256.100 211.946 1.00 26.03 ? 2245 GLU A N     1 
ATOM   6100  C CA    . GLU A 1 2245 ? 214.885 255.953 212.975 1.00 22.87 ? 2245 GLU A CA    1 
ATOM   6101  C C     . GLU A 1 2245 ? 216.272 256.374 212.510 1.00 21.81 ? 2245 GLU A C     1 
ATOM   6102  O O     . GLU A 1 2245 ? 217.191 256.435 213.333 1.00 22.01 ? 2245 GLU A O     1 
ATOM   6103  C CB    . GLU A 1 2245 ? 214.929 254.502 213.463 1.00 17.38 ? 2245 GLU A CB    1 
ATOM   6104  C CG    . GLU A 1 2245 ? 213.581 253.959 213.906 1.00 19.62 ? 2245 GLU A CG    1 
ATOM   6105  C CD    . GLU A 1 2245 ? 213.656 252.519 214.369 1.00 26.67 ? 2245 GLU A CD    1 
ATOM   6106  O OE1   . GLU A 1 2245 ? 214.577 251.798 213.931 1.00 28.51 ? 2245 GLU A OE1   1 
ATOM   6107  O OE2   . GLU A 1 2245 ? 212.793 252.105 215.170 1.00 23.84 ? 2245 GLU A OE2   1 
ATOM   6108  N N     . GLY A 1 2246 ? 216.448 256.665 211.224 1.00 19.14 ? 2246 GLY A N     1 
ATOM   6109  C CA    . GLY A 1 2246 ? 217.757 257.040 210.728 1.00 23.09 ? 2246 GLY A CA    1 
ATOM   6110  C C     . GLY A 1 2246 ? 218.779 255.928 210.760 1.00 26.75 ? 2246 GLY A C     1 
ATOM   6111  O O     . GLY A 1 2246 ? 219.979 256.196 210.668 1.00 27.32 ? 2246 GLY A O     1 
ATOM   6112  N N     . VAL A 1 2247 ? 218.336 254.681 210.886 1.00 23.19 ? 2247 VAL A N     1 
ATOM   6113  C CA    . VAL A 1 2247 ? 219.218 253.522 210.942 1.00 24.63 ? 2247 VAL A CA    1 
ATOM   6114  C C     . VAL A 1 2247 ? 219.102 252.763 209.626 1.00 24.63 ? 2247 VAL A C     1 
ATOM   6115  O O     . VAL A 1 2247 ? 217.997 252.419 209.191 1.00 24.71 ? 2247 VAL A O     1 
ATOM   6116  C CB    . VAL A 1 2247 ? 218.896 252.628 212.155 1.00 26.69 ? 2247 VAL A CB    1 
ATOM   6117  C CG1   . VAL A 1 2247 ? 217.456 252.129 212.116 1.00 22.72 ? 2247 VAL A CG1   1 
ATOM   6118  C CG2   . VAL A 1 2247 ? 219.857 251.457 212.219 1.00 27.02 ? 2247 VAL A CG2   1 
ATOM   6119  N N     . GLU A 1 2248 ? 220.240 252.527 208.981 1.00 28.70 ? 2248 GLU A N     1 
ATOM   6120  C CA    . GLU A 1 2248 ? 220.237 251.901 207.669 1.00 28.09 ? 2248 GLU A CA    1 
ATOM   6121  C C     . GLU A 1 2248 ? 219.773 250.450 207.765 1.00 28.95 ? 2248 GLU A C     1 
ATOM   6122  O O     . GLU A 1 2248 ? 220.054 249.739 208.732 1.00 28.06 ? 2248 GLU A O     1 
ATOM   6123  C CB    . GLU A 1 2248 ? 221.629 251.979 207.041 1.00 28.42 ? 2248 GLU A CB    1 
ATOM   6124  C CG    . GLU A 1 2248 ? 221.716 251.423 205.631 1.00 30.09 ? 2248 GLU A CG    1 
ATOM   6125  C CD    . GLU A 1 2248 ? 223.099 251.570 205.034 1.00 30.63 ? 2248 GLU A CD    1 
ATOM   6126  O OE1   . GLU A 1 2248 ? 223.995 252.087 205.733 1.00 28.33 ? 2248 GLU A OE1   1 
ATOM   6127  O OE2   . GLU A 1 2248 ? 223.290 251.169 203.867 1.00 31.20 ? 2248 GLU A OE2   1 
ATOM   6128  N N     . GLY A 1 2249 ? 219.040 250.016 206.742 1.00 24.92 ? 2249 GLY A N     1 
ATOM   6129  C CA    . GLY A 1 2249 ? 218.544 248.656 206.694 1.00 27.24 ? 2249 GLY A CA    1 
ATOM   6130  C C     . GLY A 1 2249 ? 219.016 247.895 205.473 1.00 27.90 ? 2249 GLY A C     1 
ATOM   6131  O O     . GLY A 1 2249 ? 218.745 248.299 204.339 1.00 28.16 ? 2249 GLY A O     1 
ATOM   6132  N N     . VAL A 1 2250 ? 219.723 246.789 205.693 1.00 23.28 ? 2250 VAL A N     1 
ATOM   6133  C CA    . VAL A 1 2250 ? 220.264 245.961 204.623 1.00 24.32 ? 2250 VAL A CA    1 
ATOM   6134  C C     . VAL A 1 2250 ? 219.620 244.586 204.715 1.00 22.88 ? 2250 VAL A C     1 
ATOM   6135  O O     . VAL A 1 2250 ? 219.606 243.972 205.788 1.00 23.66 ? 2250 VAL A O     1 
ATOM   6136  C CB    . VAL A 1 2250 ? 221.798 245.860 204.706 1.00 23.89 ? 2250 VAL A CB    1 
ATOM   6137  C CG1   . VAL A 1 2250 ? 222.298 244.635 203.957 1.00 23.49 ? 2250 VAL A CG1   1 
ATOM   6138  C CG2   . VAL A 1 2250 ? 222.441 247.125 204.160 1.00 23.92 ? 2250 VAL A CG2   1 
ATOM   6139  N N     . ALA A 1 2251 ? 219.087 244.106 203.595 1.00 20.80 ? 2251 ALA A N     1 
ATOM   6140  C CA    . ALA A 1 2251 ? 218.354 242.850 203.539 1.00 19.53 ? 2251 ALA A CA    1 
ATOM   6141  C C     . ALA A 1 2251 ? 219.179 241.797 202.812 1.00 18.12 ? 2251 ALA A C     1 
ATOM   6142  O O     . ALA A 1 2251 ? 219.713 242.059 201.730 1.00 20.67 ? 2251 ALA A O     1 
ATOM   6143  C CB    . ALA A 1 2251 ? 217.006 243.037 202.840 1.00 16.92 ? 2251 ALA A CB    1 
ATOM   6144  N N     . HIS A 1 2252 ? 219.280 240.615 203.410 1.00 15.63 ? 2252 HIS A N     1 
ATOM   6145  C CA    . HIS A 1 2252 ? 219.981 239.476 202.823 1.00 13.82 ? 2252 HIS A CA    1 
ATOM   6146  C C     . HIS A 1 2252 ? 218.941 238.399 202.534 1.00 13.29 ? 2252 HIS A C     1 
ATOM   6147  O O     . HIS A 1 2252 ? 218.599 237.602 203.411 1.00 20.17 ? 2252 HIS A O     1 
ATOM   6148  C CB    . HIS A 1 2252 ? 221.074 238.964 203.756 1.00 14.74 ? 2252 HIS A CB    1 
ATOM   6149  C CG    . HIS A 1 2252 ? 221.989 240.035 204.259 1.00 15.45 ? 2252 HIS A CG    1 
ATOM   6150  N ND1   . HIS A 1 2252 ? 223.157 240.379 203.613 1.00 17.44 ? 2252 HIS A ND1   1 
ATOM   6151  C CD2   . HIS A 1 2252 ? 221.906 240.842 205.342 1.00 17.64 ? 2252 HIS A CD2   1 
ATOM   6152  C CE1   . HIS A 1 2252 ? 223.755 241.351 204.278 1.00 20.78 ? 2252 HIS A CE1   1 
ATOM   6153  N NE2   . HIS A 1 2252 ? 223.017 241.650 205.332 1.00 21.81 ? 2252 HIS A NE2   1 
ATOM   6154  N N     . ILE A 1 2253 ? 218.444 238.376 201.300 1.00 12.36 ? 2253 ILE A N     1 
ATOM   6155  C CA    . ILE A 1 2253 ? 217.380 237.452 200.906 1.00 10.07 ? 2253 ILE A CA    1 
ATOM   6156  C C     . ILE A 1 2253 ? 218.058 236.145 200.510 1.00 8.93  ? 2253 ILE A C     1 
ATOM   6157  O O     . ILE A 1 2253 ? 218.416 235.924 199.354 1.00 20.93 ? 2253 ILE A O     1 
ATOM   6158  C CB    . ILE A 1 2253 ? 216.514 238.022 199.789 1.00 7.10  ? 2253 ILE A CB    1 
ATOM   6159  C CG1   . ILE A 1 2253 ? 215.986 239.399 200.191 1.00 11.72 ? 2253 ILE A CG1   1 
ATOM   6160  C CG2   . ILE A 1 2253 ? 215.367 237.080 199.473 1.00 6.57  ? 2253 ILE A CG2   1 
ATOM   6161  C CD1   . ILE A 1 2253 ? 215.329 240.145 199.070 1.00 8.74  ? 2253 ILE A CD1   1 
ATOM   6162  N N     . ILE A 1 2254 ? 218.237 235.267 201.491 1.00 7.47  ? 2254 ILE A N     1 
ATOM   6163  C CA    . ILE A 1 2254 ? 218.825 233.954 201.253 1.00 12.04 ? 2254 ILE A CA    1 
ATOM   6164  C C     . ILE A 1 2254 ? 217.703 232.982 200.913 1.00 11.56 ? 2254 ILE A C     1 
ATOM   6165  O O     . ILE A 1 2254 ? 216.763 232.808 201.694 1.00 20.35 ? 2254 ILE A O     1 
ATOM   6166  C CB    . ILE A 1 2254 ? 219.620 233.476 202.476 1.00 16.07 ? 2254 ILE A CB    1 
ATOM   6167  C CG1   . ILE A 1 2254 ? 220.854 234.353 202.685 1.00 15.09 ? 2254 ILE A CG1   1 
ATOM   6168  C CG2   . ILE A 1 2254 ? 220.013 232.017 202.318 1.00 11.44 ? 2254 ILE A CG2   1 
ATOM   6169  C CD1   . ILE A 1 2254 ? 221.583 234.078 203.974 1.00 16.47 ? 2254 ILE A CD1   1 
ATOM   6170  N N     . ASP A 1 2255 ? 217.798 232.347 199.747 1.00 12.64 ? 2255 ASP A N     1 
ATOM   6171  C CA    . ASP A 1 2255 ? 216.759 231.433 199.303 1.00 15.67 ? 2255 ASP A CA    1 
ATOM   6172  C C     . ASP A 1 2255 ? 217.166 230.006 199.628 1.00 18.27 ? 2255 ASP A C     1 
ATOM   6173  O O     . ASP A 1 2255 ? 218.122 229.494 199.026 1.00 20.13 ? 2255 ASP A O     1 
ATOM   6174  C CB    . ASP A 1 2255 ? 216.509 231.583 197.805 1.00 18.72 ? 2255 ASP A CB    1 
ATOM   6175  C CG    . ASP A 1 2255 ? 215.348 230.735 197.318 1.00 18.30 ? 2255 ASP A CG    1 
ATOM   6176  O OD1   . ASP A 1 2255 ? 214.186 231.157 197.489 1.00 21.27 ? 2255 ASP A OD1   1 
ATOM   6177  O OD2   . ASP A 1 2255 ? 215.594 229.642 196.770 1.00 15.02 ? 2255 ASP A OD2   1 
ATOM   6178  N N     . PRO A 1 2256 ? 216.493 229.332 200.549 1.00 21.02 ? 2256 PRO A N     1 
ATOM   6179  C CA    . PRO A 1 2256 ? 216.766 227.917 200.802 1.00 16.02 ? 2256 PRO A CA    1 
ATOM   6180  C C     . PRO A 1 2256 ? 216.171 227.061 199.689 1.00 17.97 ? 2256 PRO A C     1 
ATOM   6181  O O     . PRO A 1 2256 ? 215.482 227.553 198.797 1.00 23.15 ? 2256 PRO A O     1 
ATOM   6182  C CB    . PRO A 1 2256 ? 216.072 227.671 202.140 1.00 20.71 ? 2256 PRO A CB    1 
ATOM   6183  C CG    . PRO A 1 2256 ? 214.918 228.609 202.114 1.00 17.11 ? 2256 PRO A CG    1 
ATOM   6184  C CD    . PRO A 1 2256 ? 215.411 229.844 201.408 1.00 17.15 ? 2256 PRO A CD    1 
ATOM   6185  N N     . LYS A 1 2257 ? 216.480 225.764 199.745 1.00 15.96 ? 2257 LYS A N     1 
ATOM   6186  C CA    . LYS A 1 2257 ? 215.981 224.769 198.799 1.00 17.05 ? 2257 LYS A CA    1 
ATOM   6187  C C     . LYS A 1 2257 ? 216.548 224.990 197.400 1.00 17.86 ? 2257 LYS A C     1 
ATOM   6188  O O     . LYS A 1 2257 ? 216.273 224.209 196.484 1.00 21.20 ? 2257 LYS A O     1 
ATOM   6189  C CB    . LYS A 1 2257 ? 214.449 224.773 198.763 1.00 14.13 ? 2257 LYS A CB    1 
ATOM   6190  C CG    . LYS A 1 2257 ? 213.795 224.595 200.123 1.00 13.16 ? 2257 LYS A CG    1 
ATOM   6191  C CD    . LYS A 1 2257 ? 214.136 223.251 200.732 1.00 19.32 ? 2257 LYS A CD    1 
ATOM   6192  C CE    . LYS A 1 2257 ? 213.267 222.151 200.156 1.00 20.72 ? 2257 LYS A CE    1 
ATOM   6193  N NZ    . LYS A 1 2257 ? 211.863 222.263 200.631 1.00 17.43 ? 2257 LYS A NZ    1 
ATOM   6194  N N     . ALA A 1 2258 ? 217.348 226.041 197.227 1.00 18.06 ? 2258 ALA A N     1 
ATOM   6195  C CA    . ALA A 1 2258 ? 218.052 226.299 195.979 1.00 18.40 ? 2258 ALA A CA    1 
ATOM   6196  C C     . ALA A 1 2258 ? 219.506 225.868 196.016 1.00 22.84 ? 2258 ALA A C     1 
ATOM   6197  O O     . ALA A 1 2258 ? 220.069 225.545 194.968 1.00 20.29 ? 2258 ALA A O     1 
ATOM   6198  C CB    . ALA A 1 2258 ? 217.987 227.789 195.624 1.00 16.09 ? 2258 ALA A CB    1 
ATOM   6199  N N     . ILE A 1 2259 ? 220.122 225.860 197.193 1.00 25.69 ? 2259 ILE A N     1 
ATOM   6200  C CA    . ILE A 1 2259 ? 221.469 225.347 197.376 1.00 22.24 ? 2259 ILE A CA    1 
ATOM   6201  C C     . ILE A 1 2259 ? 221.407 224.202 198.375 1.00 22.37 ? 2259 ILE A C     1 
ATOM   6202  O O     . ILE A 1 2259 ? 220.459 224.069 199.154 1.00 19.88 ? 2259 ILE A O     1 
ATOM   6203  C CB    . ILE A 1 2259 ? 222.452 226.434 197.854 1.00 18.79 ? 2259 ILE A CB    1 
ATOM   6204  C CG1   . ILE A 1 2259 ? 221.860 227.206 199.033 1.00 16.86 ? 2259 ILE A CG1   1 
ATOM   6205  C CG2   . ILE A 1 2259 ? 222.794 227.380 196.717 1.00 24.45 ? 2259 ILE A CG2   1 
ATOM   6206  C CD1   . ILE A 1 2259 ? 222.721 228.355 199.501 1.00 21.95 ? 2259 ILE A CD1   1 
ATOM   6207  N N     . SER A 1 2260 ? 222.433 223.358 198.340 1.00 29.20 ? 2260 SER A N     1 
ATOM   6208  C CA    . SER A 1 2260 ? 222.522 222.267 199.297 1.00 25.97 ? 2260 SER A CA    1 
ATOM   6209  C C     . SER A 1 2260 ? 222.770 222.815 200.698 1.00 29.78 ? 2260 SER A C     1 
ATOM   6210  O O     . SER A 1 2260 ? 223.341 223.894 200.876 1.00 28.70 ? 2260 SER A O     1 
ATOM   6211  C CB    . SER A 1 2260 ? 223.637 221.297 198.908 1.00 25.58 ? 2260 SER A CB    1 
ATOM   6212  O OG    . SER A 1 2260 ? 224.910 221.841 199.204 1.00 29.62 ? 2260 SER A OG    1 
ATOM   6213  N N     . LYS A 1 2261 ? 222.324 222.055 201.700 1.00 32.12 ? 2261 LYS A N     1 
ATOM   6214  C CA    . LYS A 1 2261 ? 222.456 222.503 203.084 1.00 32.04 ? 2261 LYS A CA    1 
ATOM   6215  C C     . LYS A 1 2261 ? 223.922 222.653 203.467 1.00 32.81 ? 2261 LYS A C     1 
ATOM   6216  O O     . LYS A 1 2261 ? 224.278 223.512 204.286 1.00 30.74 ? 2261 LYS A O     1 
ATOM   6217  C CB    . LYS A 1 2261 ? 221.745 221.532 204.033 1.00 30.58 ? 2261 LYS A CB    1 
ATOM   6218  C CG    . LYS A 1 2261 ? 220.204 221.622 204.085 1.00 30.88 ? 2261 LYS A CG    1 
ATOM   6219  C CD    . LYS A 1 2261 ? 219.546 221.770 202.715 1.00 34.03 ? 2261 LYS A CD    1 
ATOM   6220  C CE    . LYS A 1 2261 ? 218.075 222.124 202.817 1.00 33.25 ? 2261 LYS A CE    1 
ATOM   6221  N NZ    . LYS A 1 2261 ? 217.490 222.435 201.485 1.00 28.28 ? 2261 LYS A NZ    1 
ATOM   6222  N N     . ASP A 1 2262 ? 224.789 221.830 202.873 1.00 35.61 ? 2262 ASP A N     1 
ATOM   6223  C CA    . ASP A 1 2262 ? 226.225 221.982 203.076 1.00 36.44 ? 2262 ASP A CA    1 
ATOM   6224  C C     . ASP A 1 2262 ? 226.700 223.341 202.580 1.00 36.71 ? 2262 ASP A C     1 
ATOM   6225  O O     . ASP A 1 2262 ? 227.507 224.009 203.236 1.00 36.95 ? 2262 ASP A O     1 
ATOM   6226  C CB    . ASP A 1 2262 ? 226.974 220.855 202.366 1.00 32.25 ? 2262 ASP A CB    1 
ATOM   6227  C CG    . ASP A 1 2262 ? 226.744 219.504 203.012 1.00 36.09 ? 2262 ASP A CG    1 
ATOM   6228  O OD1   . ASP A 1 2262 ? 226.507 219.461 204.238 1.00 40.07 ? 2262 ASP A OD1   1 
ATOM   6229  O OD2   . ASP A 1 2262 ? 226.797 218.484 202.294 1.00 36.38 ? 2262 ASP A OD2   1 
ATOM   6230  N N     . HIS A 1 2263 ? 226.208 223.770 201.417 1.00 29.64 ? 2263 HIS A N     1 
ATOM   6231  C CA    . HIS A 1 2263 ? 226.549 225.096 200.921 1.00 27.50 ? 2263 HIS A CA    1 
ATOM   6232  C C     . HIS A 1 2263 ? 225.829 226.195 201.689 1.00 28.92 ? 2263 HIS A C     1 
ATOM   6233  O O     . HIS A 1 2263 ? 226.259 227.352 201.642 1.00 33.65 ? 2263 HIS A O     1 
ATOM   6234  C CB    . HIS A 1 2263 ? 226.234 225.200 199.429 1.00 31.49 ? 2263 HIS A CB    1 
ATOM   6235  C CG    . HIS A 1 2263 ? 227.235 224.512 198.555 1.00 35.33 ? 2263 HIS A CG    1 
ATOM   6236  N ND1   . HIS A 1 2263 ? 228.491 225.025 198.315 1.00 31.19 ? 2263 HIS A ND1   1 
ATOM   6237  C CD2   . HIS A 1 2263 ? 227.166 223.349 197.865 1.00 32.30 ? 2263 HIS A CD2   1 
ATOM   6238  C CE1   . HIS A 1 2263 ? 229.153 224.208 197.515 1.00 31.26 ? 2263 HIS A CE1   1 
ATOM   6239  N NE2   . HIS A 1 2263 ? 228.371 223.184 197.227 1.00 32.75 ? 2263 HIS A NE2   1 
ATOM   6240  N N     . LEU A 1 2264 ? 224.746 225.861 202.393 1.00 24.97 ? 2264 LEU A N     1 
ATOM   6241  C CA    . LEU A 1 2264 ? 224.071 226.847 203.228 1.00 29.96 ? 2264 LEU A CA    1 
ATOM   6242  C C     . LEU A 1 2264 ? 224.841 227.113 204.516 1.00 33.67 ? 2264 LEU A C     1 
ATOM   6243  O O     . LEU A 1 2264 ? 224.884 228.253 204.991 1.00 32.85 ? 2264 LEU A O     1 
ATOM   6244  C CB    . LEU A 1 2264 ? 222.648 226.381 203.542 1.00 30.14 ? 2264 LEU A CB    1 
ATOM   6245  C CG    . LEU A 1 2264 ? 221.712 227.394 204.205 1.00 29.22 ? 2264 LEU A CG    1 
ATOM   6246  C CD1   . LEU A 1 2264 ? 221.766 228.731 203.487 1.00 26.87 ? 2264 LEU A CD1   1 
ATOM   6247  C CD2   . LEU A 1 2264 ? 220.288 226.860 204.236 1.00 25.43 ? 2264 LEU A CD2   1 
ATOM   6248  N N     . TYR A 1 2265 ? 225.455 226.083 205.094 1.00 33.48 ? 2265 TYR A N     1 
ATOM   6249  C CA    . TYR A 1 2265 ? 226.153 226.214 206.368 1.00 30.28 ? 2265 TYR A CA    1 
ATOM   6250  C C     . TYR A 1 2265 ? 227.652 225.978 206.272 1.00 30.33 ? 2265 TYR A C     1 
ATOM   6251  O O     . TYR A 1 2265 ? 228.439 226.784 206.779 1.00 29.74 ? 2265 TYR A O     1 
ATOM   6252  C CB    . TYR A 1 2265 ? 225.539 225.254 207.396 1.00 30.37 ? 2265 TYR A CB    1 
ATOM   6253  C CG    . TYR A 1 2265 ? 224.082 225.532 207.693 1.00 32.61 ? 2265 TYR A CG    1 
ATOM   6254  C CD1   . TYR A 1 2265 ? 223.680 226.770 208.175 1.00 31.77 ? 2265 TYR A CD1   1 
ATOM   6255  C CD2   . TYR A 1 2265 ? 223.110 224.565 207.479 1.00 31.14 ? 2265 TYR A CD2   1 
ATOM   6256  C CE1   . TYR A 1 2265 ? 222.354 227.033 208.449 1.00 29.67 ? 2265 TYR A CE1   1 
ATOM   6257  C CE2   . TYR A 1 2265 ? 221.778 224.822 207.747 1.00 28.84 ? 2265 TYR A CE2   1 
ATOM   6258  C CZ    . TYR A 1 2265 ? 221.408 226.057 208.232 1.00 29.18 ? 2265 TYR A CZ    1 
ATOM   6259  O OH    . TYR A 1 2265 ? 220.086 226.321 208.502 1.00 30.15 ? 2265 TYR A OH    1 
ATOM   6260  N N     . GLY A 1 2266 ? 228.072 224.899 205.632 1.00 32.12 ? 2266 GLY A N     1 
ATOM   6261  C CA    . GLY A 1 2266 ? 229.464 224.504 205.586 1.00 34.50 ? 2266 GLY A CA    1 
ATOM   6262  C C     . GLY A 1 2266 ? 229.645 223.076 206.059 1.00 38.08 ? 2266 GLY A C     1 
ATOM   6263  O O     . GLY A 1 2266 ? 228.719 222.426 206.542 1.00 40.33 ? 2266 GLY A O     1 
ATOM   6264  N N     . THR A 1 2267 ? 230.875 222.595 205.913 1.00 41.62 ? 2267 THR A N     1 
ATOM   6265  C CA    . THR A 1 2267 ? 231.189 221.207 206.221 1.00 42.77 ? 2267 THR A CA    1 
ATOM   6266  C C     . THR A 1 2267 ? 232.691 221.125 206.472 1.00 42.30 ? 2267 THR A C     1 
ATOM   6267  O O     . THR A 1 2267 ? 233.446 222.035 206.122 1.00 43.80 ? 2267 THR A O     1 
ATOM   6268  C CB    . THR A 1 2267 ? 230.736 220.280 205.075 1.00 40.85 ? 2267 THR A CB    1 
ATOM   6269  O OG1   . THR A 1 2267 ? 229.352 220.517 204.784 1.00 38.52 ? 2267 THR A OG1   1 
ATOM   6270  C CG2   . THR A 1 2267 ? 230.880 218.810 205.449 1.00 41.46 ? 2267 THR A CG2   1 
ATOM   6271  N N     . LEU A 1 2268 ? 233.117 220.023 207.086 1.00 38.96 ? 2268 LEU A N     1 
ATOM   6272  C CA    . LEU A 1 2268 ? 234.518 219.751 207.382 1.00 38.71 ? 2268 LEU A CA    1 
ATOM   6273  C C     . LEU A 1 2268 ? 234.991 218.590 206.519 1.00 39.71 ? 2268 LEU A C     1 
ATOM   6274  O O     . LEU A 1 2268 ? 234.351 217.535 206.491 1.00 39.83 ? 2268 LEU A O     1 
ATOM   6275  C CB    . LEU A 1 2268 ? 234.702 219.418 208.870 1.00 38.30 ? 2268 LEU A CB    1 
ATOM   6276  C CG    . LEU A 1 2268 ? 234.265 220.479 209.881 1.00 41.33 ? 2268 LEU A CG    1 
ATOM   6277  C CD1   . LEU A 1 2268 ? 234.759 220.188 211.282 1.00 40.41 ? 2268 LEU A CD1   1 
ATOM   6278  C CD2   . LEU A 1 2268 ? 234.840 221.792 209.423 1.00 39.87 ? 2268 LEU A CD2   1 
ATOM   6279  N N     . ASP A 1 2269 ? 236.101 218.783 205.818 1.00 38.11 ? 2269 ASP A N     1 
ATOM   6280  C CA    . ASP A 1 2269 ? 236.673 217.686 205.047 1.00 37.54 ? 2269 ASP A CA    1 
ATOM   6281  C C     . ASP A 1 2269 ? 237.328 216.687 205.995 1.00 39.91 ? 2269 ASP A C     1 
ATOM   6282  O O     . ASP A 1 2269 ? 238.201 217.068 206.784 1.00 39.19 ? 2269 ASP A O     1 
ATOM   6283  C CB    . ASP A 1 2269 ? 237.677 218.204 204.018 1.00 36.69 ? 2269 ASP A CB    1 
ATOM   6284  C CG    . ASP A 1 2269 ? 238.609 219.256 204.581 1.00 40.51 ? 2269 ASP A CG    1 
ATOM   6285  O OD1   . ASP A 1 2269 ? 238.384 219.705 205.723 1.00 41.21 ? 2269 ASP A OD1   1 
ATOM   6286  O OD2   . ASP A 1 2269 ? 239.568 219.636 203.878 1.00 39.20 ? 2269 ASP A OD2   1 
ATOM   6287  N N     . PRO A 1 2270 ? 236.946 215.407 205.944 1.00 42.57 ? 2270 PRO A N     1 
ATOM   6288  C CA    . PRO A 1 2270 ? 237.414 214.448 206.957 1.00 40.20 ? 2270 PRO A CA    1 
ATOM   6289  C C     . PRO A 1 2270 ? 238.903 214.159 206.903 1.00 40.55 ? 2270 PRO A C     1 
ATOM   6290  O O     . PRO A 1 2270 ? 239.399 213.410 207.752 1.00 42.21 ? 2270 PRO A O     1 
ATOM   6291  C CB    . PRO A 1 2270 ? 236.600 213.185 206.641 1.00 39.83 ? 2270 PRO A CB    1 
ATOM   6292  C CG    . PRO A 1 2270 ? 236.276 213.302 205.192 1.00 38.88 ? 2270 PRO A CG    1 
ATOM   6293  C CD    . PRO A 1 2270 ? 236.098 214.771 204.921 1.00 38.56 ? 2270 PRO A CD    1 
ATOM   6294  N N     . ASN A 1 2271 ? 239.634 214.714 205.939 1.00 41.67 ? 2271 ASN A N     1 
ATOM   6295  C CA    . ASN A 1 2271 ? 241.070 214.498 205.841 1.00 40.97 ? 2271 ASN A CA    1 
ATOM   6296  C C     . ASN A 1 2271 ? 241.879 215.673 206.374 1.00 41.56 ? 2271 ASN A C     1 
ATOM   6297  O O     . ASN A 1 2271 ? 242.729 215.493 207.251 1.00 42.80 ? 2271 ASN A O     1 
ATOM   6298  C CB    . ASN A 1 2271 ? 241.452 214.214 204.384 1.00 38.48 ? 2271 ASN A CB    1 
ATOM   6299  C CG    . ASN A 1 2271 ? 240.623 213.102 203.777 1.00 38.80 ? 2271 ASN A CG    1 
ATOM   6300  O OD1   . ASN A 1 2271 ? 240.425 212.056 204.395 1.00 38.85 ? 2271 ASN A OD1   1 
ATOM   6301  N ND2   . ASN A 1 2271 ? 240.125 213.325 202.567 1.00 39.33 ? 2271 ASN A ND2   1 
ATOM   6302  N N     . THR A 1 2272 ? 241.621 216.879 205.869 1.00 38.36 ? 2272 THR A N     1 
ATOM   6303  C CA    . THR A 1 2272 ? 242.373 218.063 206.261 1.00 37.62 ? 2272 THR A CA    1 
ATOM   6304  C C     . THR A 1 2272 ? 241.731 218.803 207.425 1.00 40.84 ? 2272 THR A C     1 
ATOM   6305  O O     . THR A 1 2272 ? 242.426 219.544 208.130 1.00 45.98 ? 2272 THR A O     1 
ATOM   6306  C CB    . THR A 1 2272 ? 242.520 219.007 205.057 1.00 41.75 ? 2272 THR A CB    1 
ATOM   6307  O OG1   . THR A 1 2272 ? 243.207 218.319 204.006 1.00 44.19 ? 2272 THR A OG1   1 
ATOM   6308  C CG2   . THR A 1 2272 ? 243.328 220.251 205.413 1.00 39.16 ? 2272 THR A CG2   1 
ATOM   6309  N N     . ARG A 1 2273 ? 240.438 218.589 207.662 1.00 39.94 ? 2273 ARG A N     1 
ATOM   6310  C CA    . ARG A 1 2273 ? 239.718 219.192 208.778 1.00 39.88 ? 2273 ARG A CA    1 
ATOM   6311  C C     . ARG A 1 2273 ? 239.704 220.720 208.672 1.00 37.77 ? 2273 ARG A C     1 
ATOM   6312  O O     . ARG A 1 2273 ? 239.622 221.424 209.682 1.00 36.84 ? 2273 ARG A O     1 
ATOM   6313  C CB    . ARG A 1 2273 ? 240.316 218.726 210.120 1.00 38.79 ? 2273 ARG A CB    1 
ATOM   6314  C CG    . ARG A 1 2273 ? 239.487 218.984 211.372 1.00 38.91 ? 2273 ARG A CG    1 
ATOM   6315  C CD    . ARG A 1 2273 ? 237.993 218.714 211.207 1.00 36.12 ? 2273 ARG A CD    1 
ATOM   6316  N NE    . ARG A 1 2273 ? 237.652 217.513 210.449 1.00 37.31 ? 2273 ARG A NE    1 
ATOM   6317  C CZ    . ARG A 1 2273 ? 237.285 216.368 211.011 1.00 41.57 ? 2273 ARG A CZ    1 
ATOM   6318  N NH1   . ARG A 1 2273 ? 237.231 216.230 212.326 1.00 38.82 ? 2273 ARG A NH1   1 
ATOM   6319  N NH2   . ARG A 1 2273 ? 236.965 215.335 210.237 1.00 39.50 ? 2273 ARG A NH2   1 
ATOM   6320  N N     . GLU A 1 2274 ? 239.799 221.251 207.452 1.00 39.25 ? 2274 GLU A N     1 
ATOM   6321  C CA    . GLU A 1 2274 ? 239.693 222.687 207.230 1.00 42.71 ? 2274 GLU A CA    1 
ATOM   6322  C C     . GLU A 1 2274 ? 238.221 223.073 207.128 1.00 41.33 ? 2274 GLU A C     1 
ATOM   6323  O O     . GLU A 1 2274 ? 237.424 222.351 206.520 1.00 37.73 ? 2274 GLU A O     1 
ATOM   6324  C CB    . GLU A 1 2274 ? 240.450 223.091 205.960 1.00 42.38 ? 2274 GLU A CB    1 
ATOM   6325  C CG    . GLU A 1 2274 ? 240.473 224.593 205.626 1.00 39.89 ? 2274 GLU A CG    1 
ATOM   6326  C CD    . GLU A 1 2274 ? 241.274 225.453 206.608 1.00 41.56 ? 2274 GLU A CD    1 
ATOM   6327  O OE1   . GLU A 1 2274 ? 241.367 225.117 207.808 1.00 40.31 ? 2274 GLU A OE1   1 
ATOM   6328  O OE2   . GLU A 1 2274 ? 241.821 226.486 206.167 1.00 42.89 ? 2274 GLU A OE2   1 
ATOM   6329  N N     . TRP A 1 2275 ? 237.858 224.200 207.736 1.00 42.55 ? 2275 TRP A N     1 
ATOM   6330  C CA    . TRP A 1 2275 ? 236.470 224.639 207.812 1.00 43.26 ? 2275 TRP A CA    1 
ATOM   6331  C C     . TRP A 1 2275 ? 236.205 225.679 206.733 1.00 41.62 ? 2275 TRP A C     1 
ATOM   6332  O O     . TRP A 1 2275 ? 236.927 226.676 206.635 1.00 40.86 ? 2275 TRP A O     1 
ATOM   6333  C CB    . TRP A 1 2275 ? 236.153 225.217 209.192 1.00 42.20 ? 2275 TRP A CB    1 
ATOM   6334  C CG    . TRP A 1 2275 ? 234.915 226.080 209.232 1.00 42.74 ? 2275 TRP A CG    1 
ATOM   6335  C CD1   . TRP A 1 2275 ? 234.864 227.430 209.429 1.00 42.39 ? 2275 TRP A CD1   1 
ATOM   6336  C CD2   . TRP A 1 2275 ? 233.554 225.646 209.097 1.00 42.90 ? 2275 TRP A CD2   1 
ATOM   6337  N NE1   . TRP A 1 2275 ? 233.561 227.863 209.414 1.00 40.13 ? 2275 TRP A NE1   1 
ATOM   6338  C CE2   . TRP A 1 2275 ? 232.738 226.787 209.213 1.00 40.86 ? 2275 TRP A CE2   1 
ATOM   6339  C CE3   . TRP A 1 2275 ? 232.947 224.406 208.884 1.00 41.16 ? 2275 TRP A CE3   1 
ATOM   6340  C CZ2   . TRP A 1 2275 ? 231.349 226.723 209.125 1.00 40.59 ? 2275 TRP A CZ2   1 
ATOM   6341  C CZ3   . TRP A 1 2275 ? 231.571 224.343 208.798 1.00 39.54 ? 2275 TRP A CZ3   1 
ATOM   6342  C CH2   . TRP A 1 2275 ? 230.787 225.494 208.917 1.00 41.47 ? 2275 TRP A CH2   1 
ATOM   6343  N N     . THR A 1 2276 ? 235.173 225.441 205.929 1.00 41.65 ? 2276 THR A N     1 
ATOM   6344  C CA    . THR A 1 2276 ? 234.697 226.403 204.948 1.00 44.88 ? 2276 THR A CA    1 
ATOM   6345  C C     . THR A 1 2276 ? 233.250 226.759 205.260 1.00 44.25 ? 2276 THR A C     1 
ATOM   6346  O O     . THR A 1 2276 ? 232.420 225.878 205.506 1.00 40.94 ? 2276 THR A O     1 
ATOM   6347  C CB    . THR A 1 2276 ? 234.831 225.858 203.517 1.00 44.42 ? 2276 THR A CB    1 
ATOM   6348  O OG1   . THR A 1 2276 ? 234.255 226.788 202.591 1.00 44.16 ? 2276 THR A OG1   1 
ATOM   6349  C CG2   . THR A 1 2276 ? 234.157 224.496 203.378 1.00 40.93 ? 2276 THR A CG2   1 
ATOM   6350  N N     . ASP A 1 2277 ? 232.958 228.055 205.266 1.00 40.16 ? 2277 ASP A N     1 
ATOM   6351  C CA    . ASP A 1 2277 ? 231.666 228.553 205.710 1.00 36.61 ? 2277 ASP A CA    1 
ATOM   6352  C C     . ASP A 1 2277 ? 230.671 228.605 204.558 1.00 39.75 ? 2277 ASP A C     1 
ATOM   6353  O O     . ASP A 1 2277 ? 231.037 228.816 203.399 1.00 40.48 ? 2277 ASP A O     1 
ATOM   6354  C CB    . ASP A 1 2277 ? 231.812 229.941 206.335 1.00 37.67 ? 2277 ASP A CB    1 
ATOM   6355  C CG    . ASP A 1 2277 ? 232.742 230.839 205.545 1.00 40.76 ? 2277 ASP A CG    1 
ATOM   6356  O OD1   . ASP A 1 2277 ? 233.186 230.425 204.453 1.00 38.79 ? 2277 ASP A OD1   1 
ATOM   6357  O OD2   . ASP A 1 2277 ? 233.031 231.959 206.017 1.00 39.53 ? 2277 ASP A OD2   1 
ATOM   6358  N N     . GLY A 1 2278 ? 229.401 228.412 204.894 1.00 36.61 ? 2278 GLY A N     1 
ATOM   6359  C CA    . GLY A 1 2278 ? 228.325 228.452 203.929 1.00 33.47 ? 2278 GLY A CA    1 
ATOM   6360  C C     . GLY A 1 2278 ? 227.836 229.861 203.673 1.00 31.26 ? 2278 GLY A C     1 
ATOM   6361  O O     . GLY A 1 2278 ? 228.445 230.847 204.092 1.00 31.89 ? 2278 GLY A O     1 
ATOM   6362  N N     . LEU A 1 2279 ? 226.706 229.949 202.972 1.00 23.52 ? 2279 LEU A N     1 
ATOM   6363  C CA    . LEU A 1 2279 ? 226.141 231.249 202.626 1.00 27.54 ? 2279 LEU A CA    1 
ATOM   6364  C C     . LEU A 1 2279 ? 225.644 231.977 203.868 1.00 28.30 ? 2279 LEU A C     1 
ATOM   6365  O O     . LEU A 1 2279 ? 226.103 233.081 204.186 1.00 30.35 ? 2279 LEU A O     1 
ATOM   6366  C CB    . LEU A 1 2279 ? 225.002 231.064 201.622 1.00 28.37 ? 2279 LEU A CB    1 
ATOM   6367  C CG    . LEU A 1 2279 ? 224.152 232.289 201.283 1.00 24.94 ? 2279 LEU A CG    1 
ATOM   6368  C CD1   . LEU A 1 2279 ? 225.013 233.460 200.827 1.00 25.56 ? 2279 LEU A CD1   1 
ATOM   6369  C CD2   . LEU A 1 2279 ? 223.110 231.928 200.242 1.00 24.75 ? 2279 LEU A CD2   1 
ATOM   6370  N N     . PHE A 1 2280 ? 224.691 231.370 204.579 1.00 23.47 ? 2280 PHE A N     1 
ATOM   6371  C CA    . PHE A 1 2280 ? 224.161 231.985 205.790 1.00 23.05 ? 2280 PHE A CA    1 
ATOM   6372  C C     . PHE A 1 2280 ? 225.246 232.137 206.846 1.00 26.54 ? 2280 PHE A C     1 
ATOM   6373  O O     . PHE A 1 2280 ? 225.286 233.140 207.567 1.00 26.62 ? 2280 PHE A O     1 
ATOM   6374  C CB    . PHE A 1 2280 ? 223.003 231.152 206.335 1.00 26.36 ? 2280 PHE A CB    1 
ATOM   6375  C CG    . PHE A 1 2280 ? 222.338 231.757 207.534 1.00 25.61 ? 2280 PHE A CG    1 
ATOM   6376  C CD1   . PHE A 1 2280 ? 221.947 230.965 208.597 1.00 22.17 ? 2280 PHE A CD1   1 
ATOM   6377  C CD2   . PHE A 1 2280 ? 222.073 233.114 207.585 1.00 23.68 ? 2280 PHE A CD2   1 
ATOM   6378  C CE1   . PHE A 1 2280 ? 221.332 231.519 209.697 1.00 20.33 ? 2280 PHE A CE1   1 
ATOM   6379  C CE2   . PHE A 1 2280 ? 221.451 233.669 208.684 1.00 22.39 ? 2280 PHE A CE2   1 
ATOM   6380  C CZ    . PHE A 1 2280 ? 221.080 232.870 209.740 1.00 19.92 ? 2280 PHE A CZ    1 
ATOM   6381  N N     . THR A 1 2281 ? 226.128 231.142 206.962 1.00 29.32 ? 2281 THR A N     1 
ATOM   6382  C CA    . THR A 1 2281 ? 227.226 231.240 207.916 1.00 29.97 ? 2281 THR A CA    1 
ATOM   6383  C C     . THR A 1 2281 ? 228.146 232.410 207.583 1.00 27.45 ? 2281 THR A C     1 
ATOM   6384  O O     . THR A 1 2281 ? 228.558 233.152 208.480 1.00 25.90 ? 2281 THR A O     1 
ATOM   6385  C CB    . THR A 1 2281 ? 228.008 229.927 207.960 1.00 29.68 ? 2281 THR A CB    1 
ATOM   6386  O OG1   . THR A 1 2281 ? 227.121 228.854 208.300 1.00 29.07 ? 2281 THR A OG1   1 
ATOM   6387  C CG2   . THR A 1 2281 ? 229.113 230.001 209.004 1.00 28.46 ? 2281 THR A CG2   1 
ATOM   6388  N N     . HIS A 1 2282 ? 228.487 232.590 206.303 1.00 26.60 ? 2282 HIS A N     1 
ATOM   6389  C CA    . HIS A 1 2282 ? 229.335 233.720 205.925 1.00 28.07 ? 2282 HIS A CA    1 
ATOM   6390  C C     . HIS A 1 2282 ? 228.626 235.049 206.155 1.00 27.21 ? 2282 HIS A C     1 
ATOM   6391  O O     . HIS A 1 2282 ? 229.263 236.041 206.532 1.00 26.29 ? 2282 HIS A O     1 
ATOM   6392  C CB    . HIS A 1 2282 ? 229.781 233.600 204.468 1.00 29.25 ? 2282 HIS A CB    1 
ATOM   6393  C CG    . HIS A 1 2282 ? 230.860 234.566 204.088 1.00 31.64 ? 2282 HIS A CG    1 
ATOM   6394  N ND1   . HIS A 1 2282 ? 230.645 235.625 203.233 1.00 29.90 ? 2282 HIS A ND1   1 
ATOM   6395  C CD2   . HIS A 1 2282 ? 232.163 234.634 204.451 1.00 33.47 ? 2282 HIS A CD2   1 
ATOM   6396  C CE1   . HIS A 1 2282 ? 231.770 236.303 203.084 1.00 31.00 ? 2282 HIS A CE1   1 
ATOM   6397  N NE2   . HIS A 1 2282 ? 232.706 235.722 203.812 1.00 33.76 ? 2282 HIS A NE2   1 
ATOM   6398  N N     . VAL A 1 2283 ? 227.314 235.099 205.913 1.00 25.87 ? 2283 VAL A N     1 
ATOM   6399  C CA    . VAL A 1 2283 ? 226.557 236.315 206.202 1.00 27.45 ? 2283 VAL A CA    1 
ATOM   6400  C C     . VAL A 1 2283 ? 226.621 236.632 207.692 1.00 28.49 ? 2283 VAL A C     1 
ATOM   6401  O O     . VAL A 1 2283 ? 226.827 237.784 208.097 1.00 25.29 ? 2283 VAL A O     1 
ATOM   6402  C CB    . VAL A 1 2283 ? 225.105 236.176 205.712 1.00 26.57 ? 2283 VAL A CB    1 
ATOM   6403  C CG1   . VAL A 1 2283 ? 224.230 237.259 206.321 1.00 26.93 ? 2283 VAL A CG1   1 
ATOM   6404  C CG2   . VAL A 1 2283 ? 225.051 236.240 204.196 1.00 23.23 ? 2283 VAL A CG2   1 
ATOM   6405  N N     . LEU A 1 2284 ? 226.456 235.606 208.530 1.00 27.12 ? 2284 LEU A N     1 
ATOM   6406  C CA    . LEU A 1 2284 ? 226.536 235.803 209.973 1.00 27.66 ? 2284 LEU A CA    1 
ATOM   6407  C C     . LEU A 1 2284 ? 227.932 236.252 210.393 1.00 29.73 ? 2284 LEU A C     1 
ATOM   6408  O O     . LEU A 1 2284 ? 228.074 237.105 211.276 1.00 29.06 ? 2284 LEU A O     1 
ATOM   6409  C CB    . LEU A 1 2284 ? 226.129 234.519 210.695 1.00 29.33 ? 2284 LEU A CB    1 
ATOM   6410  C CG    . LEU A 1 2284 ? 225.445 234.669 212.055 1.00 29.96 ? 2284 LEU A CG    1 
ATOM   6411  C CD1   . LEU A 1 2284 ? 224.302 235.667 211.977 1.00 25.40 ? 2284 LEU A CD1   1 
ATOM   6412  C CD2   . LEU A 1 2284 ? 224.934 233.320 212.526 1.00 26.80 ? 2284 LEU A CD2   1 
ATOM   6413  N N     . ARG A 1 2285 ? 228.976 235.685 209.778 1.00 28.75 ? 2285 ARG A N     1 
ATOM   6414  C CA    . ARG A 1 2285 ? 230.334 236.175 210.017 1.00 26.48 ? 2285 ARG A CA    1 
ATOM   6415  C C     . ARG A 1 2285 ? 230.467 237.653 209.678 1.00 25.97 ? 2285 ARG A C     1 
ATOM   6416  O O     . ARG A 1 2285 ? 230.984 238.436 210.484 1.00 27.83 ? 2285 ARG A O     1 
ATOM   6417  C CB    . ARG A 1 2285 ? 231.362 235.372 209.215 1.00 26.08 ? 2285 ARG A CB    1 
ATOM   6418  C CG    . ARG A 1 2285 ? 231.400 233.872 209.434 1.00 26.34 ? 2285 ARG A CG    1 
ATOM   6419  C CD    . ARG A 1 2285 ? 231.200 233.510 210.899 1.00 26.37 ? 2285 ARG A CD    1 
ATOM   6420  N NE    . ARG A 1 2285 ? 231.257 232.071 211.140 1.00 29.88 ? 2285 ARG A NE    1 
ATOM   6421  C CZ    . ARG A 1 2285 ? 232.310 231.302 210.888 1.00 30.96 ? 2285 ARG A CZ    1 
ATOM   6422  N NH1   . ARG A 1 2285 ? 233.438 231.801 210.411 1.00 29.06 ? 2285 ARG A NH1   1 
ATOM   6423  N NH2   . ARG A 1 2285 ? 232.235 230.000 211.138 1.00 31.65 ? 2285 ARG A NH2   1 
ATOM   6424  N N     . LYS A 1 2286 ? 230.018 238.055 208.487 1.00 24.83 ? 2286 LYS A N     1 
ATOM   6425  C CA    . LYS A 1 2286 ? 230.221 239.438 208.068 1.00 28.28 ? 2286 LYS A CA    1 
ATOM   6426  C C     . LYS A 1 2286 ? 229.399 240.399 208.919 1.00 26.85 ? 2286 LYS A C     1 
ATOM   6427  O O     . LYS A 1 2286 ? 229.774 241.566 209.084 1.00 24.26 ? 2286 LYS A O     1 
ATOM   6428  C CB    . LYS A 1 2286 ? 229.898 239.603 206.580 1.00 30.86 ? 2286 LYS A CB    1 
ATOM   6429  C CG    . LYS A 1 2286 ? 228.438 239.853 206.246 1.00 30.45 ? 2286 LYS A CG    1 
ATOM   6430  C CD    . LYS A 1 2286 ? 228.085 239.251 204.898 1.00 27.15 ? 2286 LYS A CD    1 
ATOM   6431  C CE    . LYS A 1 2286 ? 228.557 240.134 203.756 1.00 26.55 ? 2286 LYS A CE    1 
ATOM   6432  N NZ    . LYS A 1 2286 ? 228.156 239.589 202.430 1.00 27.75 ? 2286 LYS A NZ    1 
ATOM   6433  N N     . ILE A 1 2287 ? 228.275 239.934 209.468 1.00 24.75 ? 2287 ILE A N     1 
ATOM   6434  C CA    . ILE A 1 2287 ? 227.513 240.784 210.379 1.00 26.40 ? 2287 ILE A CA    1 
ATOM   6435  C C     . ILE A 1 2287 ? 228.202 240.878 211.737 1.00 30.03 ? 2287 ILE A C     1 
ATOM   6436  O O     . ILE A 1 2287 ? 228.293 241.960 212.329 1.00 30.30 ? 2287 ILE A O     1 
ATOM   6437  C CB    . ILE A 1 2287 ? 226.066 240.282 210.514 1.00 28.57 ? 2287 ILE A CB    1 
ATOM   6438  C CG1   . ILE A 1 2287 ? 225.344 240.362 209.168 1.00 28.05 ? 2287 ILE A CG1   1 
ATOM   6439  C CG2   . ILE A 1 2287 ? 225.325 241.106 211.544 1.00 26.63 ? 2287 ILE A CG2   1 
ATOM   6440  C CD1   . ILE A 1 2287 ? 224.012 239.652 209.153 1.00 27.24 ? 2287 ILE A CD1   1 
ATOM   6441  N N     . ILE A 1 2288 ? 228.703 239.755 212.249 1.00 29.52 ? 2288 ILE A N     1 
ATOM   6442  C CA    . ILE A 1 2288 ? 229.260 239.731 213.600 1.00 30.08 ? 2288 ILE A CA    1 
ATOM   6443  C C     . ILE A 1 2288 ? 230.682 240.275 213.611 1.00 30.28 ? 2288 ILE A C     1 
ATOM   6444  O O     . ILE A 1 2288 ? 230.976 241.276 214.274 1.00 30.34 ? 2288 ILE A O     1 
ATOM   6445  C CB    . ILE A 1 2288 ? 229.209 238.305 214.177 1.00 28.62 ? 2288 ILE A CB    1 
ATOM   6446  C CG1   . ILE A 1 2288 ? 227.763 237.828 214.305 1.00 30.24 ? 2288 ILE A CG1   1 
ATOM   6447  C CG2   . ILE A 1 2288 ? 229.910 238.252 215.523 1.00 25.98 ? 2288 ILE A CG2   1 
ATOM   6448  C CD1   . ILE A 1 2288 ? 227.638 236.334 214.474 1.00 28.97 ? 2288 ILE A CD1   1 
ATOM   6449  N N     . ASP A 1 2289 ? 231.584 239.617 212.879 1.00 29.02 ? 2289 ASP A N     1 
ATOM   6450  C CA    . ASP A 1 2289 ? 233.006 239.938 212.965 1.00 29.87 ? 2289 ASP A CA    1 
ATOM   6451  C C     . ASP A 1 2289 ? 233.281 241.364 212.504 1.00 28.31 ? 2289 ASP A C     1 
ATOM   6452  O O     . ASP A 1 2289 ? 233.756 242.203 213.278 1.00 33.56 ? 2289 ASP A O     1 
ATOM   6453  C CB    . ASP A 1 2289 ? 233.813 238.933 212.143 1.00 29.46 ? 2289 ASP A CB    1 
ATOM   6454  C CG    . ASP A 1 2289 ? 233.920 237.581 212.819 1.00 31.70 ? 2289 ASP A CG    1 
ATOM   6455  O OD1   . ASP A 1 2289 ? 233.724 237.513 214.051 1.00 32.81 ? 2289 ASP A OD1   1 
ATOM   6456  O OD2   . ASP A 1 2289 ? 234.195 236.584 212.119 1.00 28.44 ? 2289 ASP A OD2   1 
ATOM   6457  N N     . SER A 1 2290 ? 232.993 241.655 211.240 1.00 27.62 ? 2290 SER A N     1 
ATOM   6458  C CA    . SER A 1 2290 ? 233.171 242.999 210.713 1.00 34.16 ? 2290 SER A CA    1 
ATOM   6459  C C     . SER A 1 2290 ? 232.029 243.888 211.187 1.00 32.51 ? 2290 SER A C     1 
ATOM   6460  O O     . SER A 1 2290 ? 230.862 243.486 211.145 1.00 29.90 ? 2290 SER A O     1 
ATOM   6461  C CB    . SER A 1 2290 ? 233.230 242.968 209.187 1.00 36.23 ? 2290 SER A CB    1 
ATOM   6462  O OG    . SER A 1 2290 ? 233.422 244.265 208.658 1.00 29.92 ? 2290 SER A OG    1 
ATOM   6463  N N     . VAL A 1 2291 ? 232.363 245.093 211.645 1.00 37.19 ? 2291 VAL A N     1 
ATOM   6464  C CA    . VAL A 1 2291 ? 231.352 245.990 212.194 1.00 38.23 ? 2291 VAL A CA    1 
ATOM   6465  C C     . VAL A 1 2291 ? 230.603 246.683 211.064 1.00 37.74 ? 2291 VAL A C     1 
ATOM   6466  O O     . VAL A 1 2291 ? 229.415 246.416 210.846 1.00 35.75 ? 2291 VAL A O     1 
ATOM   6467  C CB    . VAL A 1 2291 ? 231.986 247.021 213.146 1.00 37.89 ? 2291 VAL A CB    1 
ATOM   6468  C CG1   . VAL A 1 2291 ? 230.922 247.950 213.708 1.00 35.81 ? 2291 VAL A CG1   1 
ATOM   6469  C CG2   . VAL A 1 2291 ? 232.734 246.316 214.268 1.00 37.62 ? 2291 VAL A CG2   1 
ATOM   6470  N N     . ARG A 1 2292 ? 231.305 247.529 210.312 1.00 40.25 ? 2292 ARG A N     1 
ATOM   6471  C CA    . ARG A 1 2292 ? 230.728 248.335 209.233 1.00 40.11 ? 2292 ARG A CA    1 
ATOM   6472  C C     . ARG A 1 2292 ? 229.349 248.872 209.616 1.00 39.87 ? 2292 ARG A C     1 
ATOM   6473  O O     . ARG A 1 2292 ? 228.343 248.634 208.949 1.00 39.52 ? 2292 ARG A O     1 
ATOM   6474  C CB    . ARG A 1 2292 ? 230.667 247.542 207.928 1.00 39.86 ? 2292 ARG A CB    1 
ATOM   6475  C CG    . ARG A 1 2292 ? 231.962 246.834 207.577 1.00 39.66 ? 2292 ARG A CG    1 
ATOM   6476  C CD    . ARG A 1 2292 ? 233.142 247.794 207.651 1.00 41.02 ? 2292 ARG A CD    1 
ATOM   6477  N NE    . ARG A 1 2292 ? 234.417 247.101 207.786 1.00 43.55 ? 2292 ARG A NE    1 
ATOM   6478  C CZ    . ARG A 1 2292 ? 234.973 246.779 208.945 1.00 42.10 ? 2292 ARG A CZ    1 
ATOM   6479  N NH1   . ARG A 1 2292 ? 234.393 247.078 210.096 1.00 39.19 ? 2292 ARG A NH1   1 
ATOM   6480  N NH2   . ARG A 1 2292 ? 236.140 246.140 208.951 1.00 41.75 ? 2292 ARG A NH2   1 
ATOM   6481  N N     . GLY A 1 2293 ? 229.324 249.612 210.722 1.00 38.84 ? 2293 GLY A N     1 
ATOM   6482  C CA    . GLY A 1 2293 ? 228.073 250.108 211.257 1.00 36.58 ? 2293 GLY A CA    1 
ATOM   6483  C C     . GLY A 1 2293 ? 227.158 248.994 211.721 1.00 38.20 ? 2293 GLY A C     1 
ATOM   6484  O O     . GLY A 1 2293 ? 225.965 248.990 211.407 1.00 37.08 ? 2293 GLY A O     1 
ATOM   6485  N N     . GLU A 1 2294 ? 227.717 248.041 212.471 1.00 39.76 ? 2294 GLU A N     1 
ATOM   6486  C CA    . GLU A 1 2294 ? 226.967 246.859 212.886 1.00 38.41 ? 2294 GLU A CA    1 
ATOM   6487  C C     . GLU A 1 2294 ? 225.699 247.239 213.642 1.00 37.40 ? 2294 GLU A C     1 
ATOM   6488  O O     . GLU A 1 2294 ? 224.585 246.942 213.199 1.00 36.84 ? 2294 GLU A O     1 
ATOM   6489  C CB    . GLU A 1 2294 ? 227.859 245.957 213.743 1.00 36.20 ? 2294 GLU A CB    1 
ATOM   6490  C CG    . GLU A 1 2294 ? 227.152 244.750 214.329 1.00 37.05 ? 2294 GLU A CG    1 
ATOM   6491  C CD    . GLU A 1 2294 ? 228.078 243.884 215.160 1.00 38.23 ? 2294 GLU A CD    1 
ATOM   6492  O OE1   . GLU A 1 2294 ? 229.308 243.974 214.966 1.00 38.89 ? 2294 GLU A OE1   1 
ATOM   6493  O OE2   . GLU A 1 2294 ? 227.578 243.116 216.007 1.00 38.03 ? 2294 GLU A OE2   1 
ATOM   6494  N N     . LEU A 1 2295 ? 225.851 247.910 214.785 1.00 36.47 ? 2295 LEU A N     1 
ATOM   6495  C CA    . LEU A 1 2295 ? 224.691 248.245 215.604 1.00 39.78 ? 2295 LEU A CA    1 
ATOM   6496  C C     . LEU A 1 2295 ? 223.782 249.273 214.941 1.00 38.13 ? 2295 LEU A C     1 
ATOM   6497  O O     . LEU A 1 2295 ? 222.615 249.388 215.329 1.00 39.63 ? 2295 LEU A O     1 
ATOM   6498  C CB    . LEU A 1 2295 ? 225.137 248.756 216.975 1.00 39.81 ? 2295 LEU A CB    1 
ATOM   6499  C CG    . LEU A 1 2295 ? 225.302 247.706 218.079 1.00 38.98 ? 2295 LEU A CG    1 
ATOM   6500  C CD1   . LEU A 1 2295 ? 223.975 247.003 218.346 1.00 38.24 ? 2295 LEU A CD1   1 
ATOM   6501  C CD2   . LEU A 1 2295 ? 226.397 246.699 217.750 1.00 37.71 ? 2295 LEU A CD2   1 
ATOM   6502  N N     . GLN A 1 2296 ? 224.283 250.018 213.955 1.00 30.14 ? 2296 GLN A N     1 
ATOM   6503  C CA    . GLN A 1 2296 ? 223.482 251.003 213.240 1.00 32.61 ? 2296 GLN A CA    1 
ATOM   6504  C C     . GLN A 1 2296 ? 223.108 250.538 211.837 1.00 33.05 ? 2296 GLN A C     1 
ATOM   6505  O O     . GLN A 1 2296 ? 222.881 251.368 210.951 1.00 33.93 ? 2296 GLN A O     1 
ATOM   6506  C CB    . GLN A 1 2296 ? 224.205 252.350 213.188 1.00 34.60 ? 2296 GLN A CB    1 
ATOM   6507  C CG    . GLN A 1 2296 ? 225.626 252.294 212.659 1.00 35.68 ? 2296 GLN A CG    1 
ATOM   6508  C CD    . GLN A 1 2296 ? 226.639 251.982 213.745 1.00 35.81 ? 2296 GLN A CD    1 
ATOM   6509  O OE1   . GLN A 1 2296 ? 226.687 250.867 214.265 1.00 31.84 ? 2296 GLN A OE1   1 
ATOM   6510  N NE2   . GLN A 1 2296 ? 227.455 252.970 214.094 1.00 34.12 ? 2296 GLN A NE2   1 
ATOM   6511  N N     . LYS A 1 2297 ? 223.043 249.226 211.616 1.00 31.65 ? 2297 LYS A N     1 
ATOM   6512  C CA    . LYS A 1 2297 ? 222.493 248.656 210.393 1.00 30.88 ? 2297 LYS A CA    1 
ATOM   6513  C C     . LYS A 1 2297 ? 221.509 247.555 210.755 1.00 30.33 ? 2297 LYS A C     1 
ATOM   6514  O O     . LYS A 1 2297 ? 221.819 246.687 211.577 1.00 29.19 ? 2297 LYS A O     1 
ATOM   6515  C CB    . LYS A 1 2297 ? 223.589 248.106 209.474 1.00 29.01 ? 2297 LYS A CB    1 
ATOM   6516  C CG    . LYS A 1 2297 ? 224.308 249.167 208.660 1.00 30.66 ? 2297 LYS A CG    1 
ATOM   6517  C CD    . LYS A 1 2297 ? 225.230 248.538 207.630 1.00 31.32 ? 2297 LYS A CD    1 
ATOM   6518  C CE    . LYS A 1 2297 ? 225.871 249.595 206.749 1.00 31.72 ? 2297 LYS A CE    1 
ATOM   6519  N NZ    . LYS A 1 2297 ? 225.871 250.935 207.400 1.00 31.33 ? 2297 LYS A NZ    1 
ATOM   6520  N N     . ARG A 1 2298 ? 220.328 247.593 210.142 1.00 27.56 ? 2298 ARG A N     1 
ATOM   6521  C CA    . ARG A 1 2298 ? 219.301 246.575 210.353 1.00 24.58 ? 2298 ARG A CA    1 
ATOM   6522  C C     . ARG A 1 2298 ? 219.523 245.462 209.338 1.00 25.26 ? 2298 ARG A C     1 
ATOM   6523  O O     . ARG A 1 2298 ? 219.145 245.585 208.171 1.00 26.78 ? 2298 ARG A O     1 
ATOM   6524  C CB    . ARG A 1 2298 ? 217.906 247.174 210.222 1.00 20.22 ? 2298 ARG A CB    1 
ATOM   6525  C CG    . ARG A 1 2298 ? 217.496 248.053 211.385 1.00 26.00 ? 2298 ARG A CG    1 
ATOM   6526  C CD    . ARG A 1 2298 ? 216.059 248.519 211.244 1.00 25.34 ? 2298 ARG A CD    1 
ATOM   6527  N NE    . ARG A 1 2298 ? 215.487 248.902 212.528 1.00 24.72 ? 2298 ARG A NE    1 
ATOM   6528  C CZ    . ARG A 1 2298 ? 214.909 248.059 213.372 1.00 26.78 ? 2298 ARG A CZ    1 
ATOM   6529  N NH1   . ARG A 1 2298 ? 214.808 246.768 213.099 1.00 24.79 ? 2298 ARG A NH1   1 
ATOM   6530  N NH2   . ARG A 1 2298 ? 214.417 248.521 214.518 1.00 25.46 ? 2298 ARG A NH2   1 
ATOM   6531  N N     . GLN A 1 2299 ? 220.138 244.370 209.780 1.00 19.98 ? 2299 GLN A N     1 
ATOM   6532  C CA    . GLN A 1 2299 ? 220.382 243.215 208.924 1.00 22.35 ? 2299 GLN A CA    1 
ATOM   6533  C C     . GLN A 1 2299 ? 219.188 242.272 209.016 1.00 24.67 ? 2299 GLN A C     1 
ATOM   6534  O O     . GLN A 1 2299 ? 219.065 241.507 209.977 1.00 23.88 ? 2299 GLN A O     1 
ATOM   6535  C CB    . GLN A 1 2299 ? 221.675 242.510 209.323 1.00 24.94 ? 2299 GLN A CB    1 
ATOM   6536  C CG    . GLN A 1 2299 ? 222.848 243.445 209.542 1.00 25.00 ? 2299 GLN A CG    1 
ATOM   6537  C CD    . GLN A 1 2299 ? 223.394 244.001 208.243 1.00 24.11 ? 2299 GLN A CD    1 
ATOM   6538  O OE1   . GLN A 1 2299 ? 224.169 243.342 207.551 1.00 22.96 ? 2299 GLN A OE1   1 
ATOM   6539  N NE2   . GLN A 1 2299 ? 222.992 245.220 207.905 1.00 24.18 ? 2299 GLN A NE2   1 
ATOM   6540  N N     . TRP A 1 2300 ? 218.313 242.326 208.016 1.00 16.74 ? 2300 TRP A N     1 
ATOM   6541  C CA    . TRP A 1 2300 ? 217.147 241.451 207.930 1.00 11.44 ? 2300 TRP A CA    1 
ATOM   6542  C C     . TRP A 1 2300 ? 217.495 240.317 206.975 1.00 14.35 ? 2300 TRP A C     1 
ATOM   6543  O O     . TRP A 1 2300 ? 217.476 240.493 205.755 1.00 24.56 ? 2300 TRP A O     1 
ATOM   6544  C CB    . TRP A 1 2300 ? 215.916 242.215 207.455 1.00 14.57 ? 2300 TRP A CB    1 
ATOM   6545  C CG    . TRP A 1 2300 ? 215.243 242.995 208.532 1.00 17.13 ? 2300 TRP A CG    1 
ATOM   6546  C CD1   . TRP A 1 2300 ? 215.649 243.123 209.826 1.00 15.72 ? 2300 TRP A CD1   1 
ATOM   6547  C CD2   . TRP A 1 2300 ? 214.032 243.751 208.414 1.00 17.63 ? 2300 TRP A CD2   1 
ATOM   6548  N NE1   . TRP A 1 2300 ? 214.771 243.918 210.521 1.00 17.29 ? 2300 TRP A NE1   1 
ATOM   6549  C CE2   . TRP A 1 2300 ? 213.769 244.315 209.676 1.00 15.94 ? 2300 TRP A CE2   1 
ATOM   6550  C CE3   . TRP A 1 2300 ? 213.148 244.008 207.363 1.00 10.81 ? 2300 TRP A CE3   1 
ATOM   6551  C CZ2   . TRP A 1 2300 ? 212.660 245.120 209.915 1.00 14.58 ? 2300 TRP A CZ2   1 
ATOM   6552  C CZ3   . TRP A 1 2300 ? 212.048 244.805 207.603 1.00 10.28 ? 2300 TRP A CZ3   1 
ATOM   6553  C CH2   . TRP A 1 2300 ? 211.812 245.352 208.868 1.00 14.91 ? 2300 TRP A CH2   1 
ATOM   6554  N N     . ILE A 1 2301 ? 217.811 239.153 207.534 1.00 10.07 ? 2301 ILE A N     1 
ATOM   6555  C CA    . ILE A 1 2301 ? 218.170 237.992 206.731 1.00 11.70 ? 2301 ILE A CA    1 
ATOM   6556  C C     . ILE A 1 2301 ? 216.900 237.240 206.366 1.00 13.15 ? 2301 ILE A C     1 
ATOM   6557  O O     . ILE A 1 2301 ? 216.517 236.280 207.043 1.00 21.08 ? 2301 ILE A O     1 
ATOM   6558  C CB    . ILE A 1 2301 ? 219.165 237.088 207.480 1.00 12.54 ? 2301 ILE A CB    1 
ATOM   6559  C CG1   . ILE A 1 2301 ? 220.283 237.936 208.087 1.00 15.49 ? 2301 ILE A CG1   1 
ATOM   6560  C CG2   . ILE A 1 2301 ? 219.734 236.034 206.549 1.00 17.48 ? 2301 ILE A CG2   1 
ATOM   6561  C CD1   . ILE A 1 2301 ? 221.362 237.132 208.758 1.00 14.66 ? 2301 ILE A CD1   1 
ATOM   6562  N N     . VAL A 1 2302 ? 216.243 237.669 205.293 1.00 9.80  ? 2302 VAL A N     1 
ATOM   6563  C CA    . VAL A 1 2302 ? 214.963 237.094 204.897 1.00 9.37  ? 2302 VAL A CA    1 
ATOM   6564  C C     . VAL A 1 2302 ? 215.211 235.744 204.237 1.00 6.97  ? 2302 VAL A C     1 
ATOM   6565  O O     . VAL A 1 2302 ? 215.979 235.643 203.275 1.00 15.45 ? 2302 VAL A O     1 
ATOM   6566  C CB    . VAL A 1 2302 ? 214.198 238.036 203.958 1.00 3.08  ? 2302 VAL A CB    1 
ATOM   6567  C CG1   . VAL A 1 2302 ? 212.817 237.477 203.662 1.00 1.63  ? 2302 VAL A CG1   1 
ATOM   6568  C CG2   . VAL A 1 2302 ? 214.100 239.423 204.569 1.00 6.88  ? 2302 VAL A CG2   1 
ATOM   6569  N N     . PHE A 1 2303 ? 214.568 234.707 204.758 1.00 4.58  ? 2303 PHE A N     1 
ATOM   6570  C CA    . PHE A 1 2303 ? 214.676 233.361 204.200 1.00 3.21  ? 2303 PHE A CA    1 
ATOM   6571  C C     . PHE A 1 2303 ? 213.488 233.073 203.285 1.00 7.26  ? 2303 PHE A C     1 
ATOM   6572  O O     . PHE A 1 2303 ? 212.666 232.194 203.540 1.00 12.52 ? 2303 PHE A O     1 
ATOM   6573  C CB    . PHE A 1 2303 ? 214.772 232.332 205.321 1.00 11.55 ? 2303 PHE A CB    1 
ATOM   6574  C CG    . PHE A 1 2303 ? 216.178 231.936 205.662 1.00 13.37 ? 2303 PHE A CG    1 
ATOM   6575  C CD1   . PHE A 1 2303 ? 216.815 232.482 206.762 1.00 14.04 ? 2303 PHE A CD1   1 
ATOM   6576  C CD2   . PHE A 1 2303 ? 216.865 231.026 204.880 1.00 12.87 ? 2303 PHE A CD2   1 
ATOM   6577  C CE1   . PHE A 1 2303 ? 218.108 232.122 207.079 1.00 16.56 ? 2303 PHE A CE1   1 
ATOM   6578  C CE2   . PHE A 1 2303 ? 218.158 230.661 205.192 1.00 16.12 ? 2303 PHE A CE2   1 
ATOM   6579  C CZ    . PHE A 1 2303 ? 218.781 231.210 206.292 1.00 20.14 ? 2303 PHE A CZ    1 
ATOM   6580  N N     . ASP A 1 2304 ? 213.404 233.846 202.205 1.00 12.07 ? 2304 ASP A N     1 
ATOM   6581  C CA    . ASP A 1 2304 ? 212.302 233.685 201.267 1.00 10.35 ? 2304 ASP A CA    1 
ATOM   6582  C C     . ASP A 1 2304 ? 212.434 232.363 200.524 1.00 9.82  ? 2304 ASP A C     1 
ATOM   6583  O O     . ASP A 1 2304 ? 213.510 232.009 200.036 1.00 14.50 ? 2304 ASP A O     1 
ATOM   6584  C CB    . ASP A 1 2304 ? 212.269 234.852 200.280 1.00 4.24  ? 2304 ASP A CB    1 
ATOM   6585  C CG    . ASP A 1 2304 ? 211.125 234.747 199.291 1.00 9.67  ? 2304 ASP A CG    1 
ATOM   6586  O OD1   . ASP A 1 2304 ? 210.108 234.103 199.618 1.00 12.71 ? 2304 ASP A OD1   1 
ATOM   6587  O OD2   . ASP A 1 2304 ? 211.241 235.314 198.185 1.00 17.36 ? 2304 ASP A OD2   1 
ATOM   6588  N N     . GLY A 1 2305 ? 211.338 231.637 200.443 1.00 6.13  ? 2305 GLY A N     1 
ATOM   6589  C CA    . GLY A 1 2305 ? 211.329 230.333 199.824 1.00 13.78 ? 2305 GLY A CA    1 
ATOM   6590  C C     . GLY A 1 2305 ? 210.277 229.450 200.483 1.00 10.55 ? 2305 GLY A C     1 
ATOM   6591  O O     . GLY A 1 2305 ? 209.144 229.882 200.701 1.00 9.32  ? 2305 GLY A O     1 
ATOM   6592  N N     . ASP A 1 2306 ? 210.674 228.218 200.785 1.00 11.23 ? 2306 ASP A N     1 
ATOM   6593  C CA    . ASP A 1 2306 ? 209.809 227.250 201.441 1.00 16.24 ? 2306 ASP A CA    1 
ATOM   6594  C C     . ASP A 1 2306 ? 210.478 226.741 202.710 1.00 21.85 ? 2306 ASP A C     1 
ATOM   6595  O O     . ASP A 1 2306 ? 211.653 226.360 202.696 1.00 18.08 ? 2306 ASP A O     1 
ATOM   6596  C CB    . ASP A 1 2306 ? 209.486 226.074 200.515 1.00 18.46 ? 2306 ASP A CB    1 
ATOM   6597  C CG    . ASP A 1 2306 ? 208.171 225.405 200.864 1.00 21.85 ? 2306 ASP A CG    1 
ATOM   6598  O OD1   . ASP A 1 2306 ? 207.740 224.508 200.109 1.00 19.36 ? 2306 ASP A OD1   1 
ATOM   6599  O OD2   . ASP A 1 2306 ? 207.568 225.777 201.893 1.00 16.97 ? 2306 ASP A OD2   1 
ATOM   6600  N N     . VAL A 1 2307 ? 209.722 226.734 203.803 1.00 21.31 ? 2307 VAL A N     1 
ATOM   6601  C CA    . VAL A 1 2307 ? 210.235 226.276 205.088 1.00 18.38 ? 2307 VAL A CA    1 
ATOM   6602  C C     . VAL A 1 2307 ? 210.316 224.756 205.080 1.00 17.53 ? 2307 VAL A C     1 
ATOM   6603  O O     . VAL A 1 2307 ? 209.464 224.069 204.504 1.00 19.36 ? 2307 VAL A O     1 
ATOM   6604  C CB    . VAL A 1 2307 ? 209.357 226.801 206.239 1.00 16.58 ? 2307 VAL A CB    1 
ATOM   6605  C CG1   . VAL A 1 2307 ? 207.963 226.197 206.176 1.00 17.85 ? 2307 VAL A CG1   1 
ATOM   6606  C CG2   . VAL A 1 2307 ? 210.012 226.520 207.582 1.00 19.13 ? 2307 VAL A CG2   1 
ATOM   6607  N N     . ASP A 1 2308 ? 211.365 224.224 205.711 1.00 22.09 ? 2308 ASP A N     1 
ATOM   6608  C CA    . ASP A 1 2308 ? 211.661 222.802 205.651 1.00 19.68 ? 2308 ASP A CA    1 
ATOM   6609  C C     . ASP A 1 2308 ? 212.455 222.418 206.885 1.00 25.94 ? 2308 ASP A C     1 
ATOM   6610  O O     . ASP A 1 2308 ? 213.321 223.195 207.308 1.00 25.37 ? 2308 ASP A O     1 
ATOM   6611  C CB    . ASP A 1 2308 ? 212.447 222.470 204.379 1.00 21.53 ? 2308 ASP A CB    1 
ATOM   6612  C CG    . ASP A 1 2308 ? 212.820 221.019 204.288 1.00 23.42 ? 2308 ASP A CG    1 
ATOM   6613  O OD1   . ASP A 1 2308 ? 211.902 220.185 204.273 1.00 26.13 ? 2308 ASP A OD1   1 
ATOM   6614  O OD2   . ASP A 1 2308 ? 214.028 220.713 204.219 1.00 22.98 ? 2308 ASP A OD2   1 
ATOM   6615  N N     . PRO A 1 2309 ? 212.188 221.259 207.496 1.00 25.34 ? 2309 PRO A N     1 
ATOM   6616  C CA    . PRO A 1 2309 ? 212.940 220.888 208.706 1.00 17.66 ? 2309 PRO A CA    1 
ATOM   6617  C C     . PRO A 1 2309 ? 214.441 220.805 208.495 1.00 20.58 ? 2309 PRO A C     1 
ATOM   6618  O O     . PRO A 1 2309 ? 215.210 221.171 209.394 1.00 22.98 ? 2309 PRO A O     1 
ATOM   6619  C CB    . PRO A 1 2309 ? 212.350 219.520 209.070 1.00 17.16 ? 2309 PRO A CB    1 
ATOM   6620  C CG    . PRO A 1 2309 ? 210.980 219.539 208.507 1.00 18.44 ? 2309 PRO A CG    1 
ATOM   6621  C CD    . PRO A 1 2309 ? 211.062 220.344 207.244 1.00 24.07 ? 2309 PRO A CD    1 
ATOM   6622  N N     . GLU A 1 2310 ? 214.877 220.347 207.318 1.00 23.07 ? 2310 GLU A N     1 
ATOM   6623  C CA    . GLU A 1 2310 ? 216.265 219.931 207.142 1.00 25.25 ? 2310 GLU A CA    1 
ATOM   6624  C C     . GLU A 1 2310 ? 217.232 221.099 207.301 1.00 30.17 ? 2310 GLU A C     1 
ATOM   6625  O O     . GLU A 1 2310 ? 218.288 220.960 207.928 1.00 35.92 ? 2310 GLU A O     1 
ATOM   6626  C CB    . GLU A 1 2310 ? 216.440 219.257 205.781 1.00 26.92 ? 2310 GLU A CB    1 
ATOM   6627  C CG    . GLU A 1 2310 ? 217.880 218.906 205.443 1.00 28.46 ? 2310 GLU A CG    1 
ATOM   6628  C CD    . GLU A 1 2310 ? 218.104 218.716 203.956 1.00 31.92 ? 2310 GLU A CD    1 
ATOM   6629  O OE1   . GLU A 1 2310 ? 217.199 219.054 203.166 1.00 29.98 ? 2310 GLU A OE1   1 
ATOM   6630  O OE2   . GLU A 1 2310 ? 219.186 218.223 203.577 1.00 32.26 ? 2310 GLU A OE2   1 
ATOM   6631  N N     . TRP A 1 2311 ? 216.897 222.259 206.741 1.00 22.87 ? 2311 TRP A N     1 
ATOM   6632  C CA    . TRP A 1 2311 ? 217.786 223.407 206.860 1.00 21.40 ? 2311 TRP A CA    1 
ATOM   6633  C C     . TRP A 1 2311 ? 217.468 224.280 208.066 1.00 24.09 ? 2311 TRP A C     1 
ATOM   6634  O O     . TRP A 1 2311 ? 218.178 225.261 208.303 1.00 25.94 ? 2311 TRP A O     1 
ATOM   6635  C CB    . TRP A 1 2311 ? 217.753 224.265 205.589 1.00 24.13 ? 2311 TRP A CB    1 
ATOM   6636  C CG    . TRP A 1 2311 ? 216.406 224.779 205.214 1.00 22.95 ? 2311 TRP A CG    1 
ATOM   6637  C CD1   . TRP A 1 2311 ? 215.450 224.130 204.495 1.00 21.38 ? 2311 TRP A CD1   1 
ATOM   6638  C CD2   . TRP A 1 2311 ? 215.868 226.069 205.525 1.00 20.48 ? 2311 TRP A CD2   1 
ATOM   6639  N NE1   . TRP A 1 2311 ? 214.346 224.932 204.344 1.00 19.85 ? 2311 TRP A NE1   1 
ATOM   6640  C CE2   . TRP A 1 2311 ? 214.577 226.127 204.971 1.00 17.16 ? 2311 TRP A CE2   1 
ATOM   6641  C CE3   . TRP A 1 2311 ? 216.352 227.177 206.226 1.00 19.66 ? 2311 TRP A CE3   1 
ATOM   6642  C CZ2   . TRP A 1 2311 ? 213.763 227.247 205.093 1.00 19.75 ? 2311 TRP A CZ2   1 
ATOM   6643  C CZ3   . TRP A 1 2311 ? 215.543 228.287 206.345 1.00 20.57 ? 2311 TRP A CZ3   1 
ATOM   6644  C CH2   . TRP A 1 2311 ? 214.264 228.315 205.780 1.00 22.82 ? 2311 TRP A CH2   1 
ATOM   6645  N N     . VAL A 1 2312 ? 216.422 223.955 208.830 1.00 25.61 ? 2312 VAL A N     1 
ATOM   6646  C CA    . VAL A 1 2312 ? 216.139 224.667 210.069 1.00 27.22 ? 2312 VAL A CA    1 
ATOM   6647  C C     . VAL A 1 2312 ? 216.545 223.872 211.300 1.00 29.79 ? 2312 VAL A C     1 
ATOM   6648  O O     . VAL A 1 2312 ? 216.369 224.360 212.425 1.00 30.24 ? 2312 VAL A O     1 
ATOM   6649  C CB    . VAL A 1 2312 ? 214.655 225.076 210.169 1.00 21.97 ? 2312 VAL A CB    1 
ATOM   6650  C CG1   . VAL A 1 2312 ? 214.214 225.807 208.912 1.00 20.96 ? 2312 VAL A CG1   1 
ATOM   6651  C CG2   . VAL A 1 2312 ? 213.781 223.869 210.438 1.00 22.48 ? 2312 VAL A CG2   1 
ATOM   6652  N N     . GLU A 1 2313 ? 217.083 222.659 211.128 1.00 23.62 ? 2313 GLU A N     1 
ATOM   6653  C CA    . GLU A 1 2313 ? 217.688 221.975 212.268 1.00 24.05 ? 2313 GLU A CA    1 
ATOM   6654  C C     . GLU A 1 2313 ? 218.772 222.834 212.907 1.00 25.03 ? 2313 GLU A C     1 
ATOM   6655  O O     . GLU A 1 2313 ? 218.821 222.977 214.134 1.00 26.14 ? 2313 GLU A O     1 
ATOM   6656  C CB    . GLU A 1 2313 ? 218.275 220.626 211.849 1.00 23.19 ? 2313 GLU A CB    1 
ATOM   6657  C CG    . GLU A 1 2313 ? 217.424 219.819 210.895 1.00 24.01 ? 2313 GLU A CG    1 
ATOM   6658  C CD    . GLU A 1 2313 ? 217.807 218.353 210.864 1.00 27.87 ? 2313 GLU A CD    1 
ATOM   6659  O OE1   . GLU A 1 2313 ? 217.824 217.768 209.760 1.00 28.99 ? 2313 GLU A OE1   1 
ATOM   6660  O OE2   . GLU A 1 2313 ? 218.091 217.786 211.940 1.00 28.34 ? 2313 GLU A OE2   1 
ATOM   6661  N N     . ASN A 1 2314 ? 219.651 223.417 212.088 1.00 24.45 ? 2314 ASN A N     1 
ATOM   6662  C CA    . ASN A 1 2314 ? 220.694 224.283 212.625 1.00 25.12 ? 2314 ASN A CA    1 
ATOM   6663  C C     . ASN A 1 2314 ? 220.133 225.619 213.092 1.00 25.35 ? 2314 ASN A C     1 
ATOM   6664  O O     . ASN A 1 2314 ? 220.729 226.271 213.956 1.00 27.96 ? 2314 ASN A O     1 
ATOM   6665  C CB    . ASN A 1 2314 ? 221.785 224.503 211.577 1.00 28.08 ? 2314 ASN A CB    1 
ATOM   6666  C CG    . ASN A 1 2314 ? 222.503 223.222 211.205 1.00 32.17 ? 2314 ASN A CG    1 
ATOM   6667  O OD1   . ASN A 1 2314 ? 223.190 222.620 212.029 1.00 34.52 ? 2314 ASN A OD1   1 
ATOM   6668  N ND2   . ASN A 1 2314 ? 222.347 222.796 209.957 1.00 27.72 ? 2314 ASN A ND2   1 
ATOM   6669  N N     . LEU A 1 2315 ? 218.998 226.044 212.535 1.00 23.49 ? 2315 LEU A N     1 
ATOM   6670  C CA    . LEU A 1 2315 ? 218.424 227.332 212.904 1.00 23.39 ? 2315 LEU A CA    1 
ATOM   6671  C C     . LEU A 1 2315 ? 217.637 227.278 214.205 1.00 21.53 ? 2315 LEU A C     1 
ATOM   6672  O O     . LEU A 1 2315 ? 217.470 228.318 214.851 1.00 26.29 ? 2315 LEU A O     1 
ATOM   6673  C CB    . LEU A 1 2315 ? 217.530 227.849 211.778 1.00 23.20 ? 2315 LEU A CB    1 
ATOM   6674  C CG    . LEU A 1 2315 ? 218.266 228.699 210.747 1.00 23.22 ? 2315 LEU A CG    1 
ATOM   6675  C CD1   . LEU A 1 2315 ? 217.283 229.434 209.862 1.00 27.63 ? 2315 LEU A CD1   1 
ATOM   6676  C CD2   . LEU A 1 2315 ? 219.166 229.676 211.470 1.00 19.67 ? 2315 LEU A CD2   1 
ATOM   6677  N N     . ASN A 1 2316 ? 217.158 226.097 214.603 1.00 16.24 ? 2316 ASN A N     1 
ATOM   6678  C CA    . ASN A 1 2316 ? 216.398 225.986 215.844 1.00 15.87 ? 2316 ASN A CA    1 
ATOM   6679  C C     . ASN A 1 2316 ? 217.200 226.476 217.043 1.00 23.33 ? 2316 ASN A C     1 
ATOM   6680  O O     . ASN A 1 2316 ? 216.618 226.918 218.039 1.00 27.14 ? 2316 ASN A O     1 
ATOM   6681  C CB    . ASN A 1 2316 ? 215.952 224.540 216.056 1.00 20.15 ? 2316 ASN A CB    1 
ATOM   6682  C CG    . ASN A 1 2316 ? 214.691 224.204 215.289 1.00 25.51 ? 2316 ASN A CG    1 
ATOM   6683  O OD1   . ASN A 1 2316 ? 214.113 225.059 214.619 1.00 24.59 ? 2316 ASN A OD1   1 
ATOM   6684  N ND2   . ASN A 1 2316 ? 214.256 222.954 215.383 1.00 23.56 ? 2316 ASN A ND2   1 
ATOM   6685  N N     . SER A 1 2317 ? 218.529 226.407 216.970 1.00 23.62 ? 2317 SER A N     1 
ATOM   6686  C CA    . SER A 1 2317 ? 219.377 226.978 218.007 1.00 18.46 ? 2317 SER A CA    1 
ATOM   6687  C C     . SER A 1 2317 ? 219.494 228.492 217.907 1.00 18.97 ? 2317 SER A C     1 
ATOM   6688  O O     . SER A 1 2317 ? 220.032 229.116 218.828 1.00 24.96 ? 2317 SER A O     1 
ATOM   6689  C CB    . SER A 1 2317 ? 220.773 226.353 217.948 1.00 24.84 ? 2317 SER A CB    1 
ATOM   6690  O OG    . SER A 1 2317 ? 220.698 224.946 217.807 1.00 29.32 ? 2317 SER A OG    1 
ATOM   6691  N N     . VAL A 1 2318 ? 219.008 229.093 216.823 1.00 21.97 ? 2318 VAL A N     1 
ATOM   6692  C CA    . VAL A 1 2318 ? 219.117 230.526 216.602 1.00 22.66 ? 2318 VAL A CA    1 
ATOM   6693  C C     . VAL A 1 2318 ? 217.780 231.231 216.800 1.00 19.04 ? 2318 VAL A C     1 
ATOM   6694  O O     . VAL A 1 2318 ? 217.742 232.398 217.196 1.00 18.26 ? 2318 VAL A O     1 
ATOM   6695  C CB    . VAL A 1 2318 ? 219.689 230.813 215.195 1.00 19.32 ? 2318 VAL A CB    1 
ATOM   6696  C CG1   . VAL A 1 2318 ? 220.019 232.286 215.038 1.00 18.82 ? 2318 VAL A CG1   1 
ATOM   6697  C CG2   . VAL A 1 2318 ? 220.917 229.958 214.935 1.00 20.26 ? 2318 VAL A CG2   1 
ATOM   6698  N N     . LEU A 1 2319 ? 216.672 230.537 216.535 1.00 17.21 ? 2319 LEU A N     1 
ATOM   6699  C CA    . LEU A 1 2319 ? 215.360 231.165 216.659 1.00 21.42 ? 2319 LEU A CA    1 
ATOM   6700  C C     . LEU A 1 2319 ? 214.962 231.353 218.119 1.00 22.57 ? 2319 LEU A C     1 
ATOM   6701  O O     . LEU A 1 2319 ? 214.180 232.255 218.442 1.00 20.33 ? 2319 LEU A O     1 
ATOM   6702  C CB    . LEU A 1 2319 ? 214.307 230.344 215.915 1.00 20.80 ? 2319 LEU A CB    1 
ATOM   6703  C CG    . LEU A 1 2319 ? 214.094 230.625 214.424 1.00 20.30 ? 2319 LEU A CG    1 
ATOM   6704  C CD1   . LEU A 1 2319 ? 215.231 230.096 213.574 1.00 14.63 ? 2319 LEU A CD1   1 
ATOM   6705  C CD2   . LEU A 1 2319 ? 212.775 230.025 213.971 1.00 20.30 ? 2319 LEU A CD2   1 
ATOM   6706  N N     . ASP A 1 2320 ? 215.484 230.518 219.014 1.00 24.56 ? 2320 ASP A N     1 
ATOM   6707  C CA    . ASP A 1 2320 ? 215.131 230.601 220.422 1.00 24.10 ? 2320 ASP A CA    1 
ATOM   6708  C C     . ASP A 1 2320 ? 215.904 231.729 221.103 1.00 24.67 ? 2320 ASP A C     1 
ATOM   6709  O O     . ASP A 1 2320 ? 216.606 232.517 220.465 1.00 24.66 ? 2320 ASP A O     1 
ATOM   6710  C CB    . ASP A 1 2320 ? 215.384 229.263 221.113 1.00 24.88 ? 2320 ASP A CB    1 
ATOM   6711  C CG    . ASP A 1 2320 ? 216.779 228.732 220.864 1.00 25.26 ? 2320 ASP A CG    1 
ATOM   6712  O OD1   . ASP A 1 2320 ? 217.568 229.423 220.187 1.00 27.34 ? 2320 ASP A OD1   1 
ATOM   6713  O OD2   . ASP A 1 2320 ? 217.088 227.622 221.343 1.00 23.03 ? 2320 ASP A OD2   1 
ATOM   6714  N N     . ASP A 1 2321 ? 215.770 231.805 222.428 1.00 29.82 ? 2321 ASP A N     1 
ATOM   6715  C CA    . ASP A 1 2321 ? 216.449 232.835 223.205 1.00 32.44 ? 2321 ASP A CA    1 
ATOM   6716  C C     . ASP A 1 2321 ? 217.961 232.664 223.221 1.00 33.45 ? 2321 ASP A C     1 
ATOM   6717  O O     . ASP A 1 2321 ? 218.666 233.604 223.604 1.00 33.59 ? 2321 ASP A O     1 
ATOM   6718  C CB    . ASP A 1 2321 ? 215.916 232.843 224.637 1.00 31.73 ? 2321 ASP A CB    1 
ATOM   6719  C CG    . ASP A 1 2321 ? 214.402 232.810 224.693 1.00 32.35 ? 2321 ASP A CG    1 
ATOM   6720  O OD1   . ASP A 1 2321 ? 213.837 231.711 224.879 1.00 32.11 ? 2321 ASP A OD1   1 
ATOM   6721  O OD2   . ASP A 1 2321 ? 213.776 233.881 224.549 1.00 32.57 ? 2321 ASP A OD2   1 
ATOM   6722  N N     . ASN A 1 2322 ? 218.472 231.496 222.825 1.00 30.76 ? 2322 ASN A N     1 
ATOM   6723  C CA    . ASN A 1 2322 ? 219.917 231.302 222.773 1.00 30.05 ? 2322 ASN A CA    1 
ATOM   6724  C C     . ASN A 1 2322 ? 220.562 232.249 221.770 1.00 29.97 ? 2322 ASN A C     1 
ATOM   6725  O O     . ASN A 1 2322 ? 221.610 232.842 222.052 1.00 31.07 ? 2322 ASN A O     1 
ATOM   6726  C CB    . ASN A 1 2322 ? 220.235 229.850 222.421 1.00 26.94 ? 2322 ASN A CB    1 
ATOM   6727  C CG    . ASN A 1 2322 ? 219.932 228.896 223.558 1.00 28.72 ? 2322 ASN A CG    1 
ATOM   6728  O OD1   . ASN A 1 2322 ? 220.208 229.191 224.721 1.00 30.05 ? 2322 ASN A OD1   1 
ATOM   6729  N ND2   . ASN A 1 2322 ? 219.359 227.745 223.228 1.00 28.14 ? 2322 ASN A ND2   1 
ATOM   6730  N N     . LYS A 1 2323 ? 219.947 232.403 220.596 1.00 21.35 ? 2323 LYS A N     1 
ATOM   6731  C CA    . LYS A 1 2323 ? 220.428 233.305 219.549 1.00 28.18 ? 2323 LYS A CA    1 
ATOM   6732  C C     . LYS A 1 2323 ? 221.864 232.992 219.138 1.00 31.88 ? 2323 LYS A C     1 
ATOM   6733  O O     . LYS A 1 2323 ? 222.651 233.898 218.854 1.00 28.14 ? 2323 LYS A O     1 
ATOM   6734  C CB    . LYS A 1 2323 ? 220.304 234.769 219.980 1.00 22.48 ? 2323 LYS A CB    1 
ATOM   6735  C CG    . LYS A 1 2323 ? 218.879 235.219 220.246 1.00 23.34 ? 2323 LYS A CG    1 
ATOM   6736  C CD    . LYS A 1 2323 ? 218.843 236.358 221.248 1.00 27.30 ? 2323 LYS A CD    1 
ATOM   6737  C CE    . LYS A 1 2323 ? 219.659 237.546 220.768 1.00 28.62 ? 2323 LYS A CE    1 
ATOM   6738  N NZ    . LYS A 1 2323 ? 218.973 238.281 219.673 1.00 24.72 ? 2323 LYS A NZ    1 
ATOM   6739  N N     . LEU A 1 2324 ? 222.219 231.710 219.100 1.00 25.32 ? 2324 LEU A N     1 
ATOM   6740  C CA    . LEU A 1 2324 ? 223.562 231.284 218.741 1.00 24.85 ? 2324 LEU A CA    1 
ATOM   6741  C C     . LEU A 1 2324 ? 223.486 230.121 217.764 1.00 27.08 ? 2324 LEU A C     1 
ATOM   6742  O O     . LEU A 1 2324 ? 222.598 229.270 217.865 1.00 25.68 ? 2324 LEU A O     1 
ATOM   6743  C CB    . LEU A 1 2324 ? 224.376 230.893 219.988 1.00 25.19 ? 2324 LEU A CB    1 
ATOM   6744  C CG    . LEU A 1 2324 ? 223.858 229.782 220.908 1.00 29.80 ? 2324 LEU A CG    1 
ATOM   6745  C CD1   . LEU A 1 2324 ? 224.367 228.407 220.486 1.00 28.59 ? 2324 LEU A CD1   1 
ATOM   6746  C CD2   . LEU A 1 2324 ? 224.222 230.073 222.358 1.00 29.09 ? 2324 LEU A CD2   1 
ATOM   6747  N N     . LEU A 1 2325 ? 224.422 230.090 216.821 1.00 30.77 ? 2325 LEU A N     1 
ATOM   6748  C CA    . LEU A 1 2325 ? 224.487 229.052 215.802 1.00 32.90 ? 2325 LEU A CA    1 
ATOM   6749  C C     . LEU A 1 2325 ? 225.642 228.113 216.119 1.00 31.61 ? 2325 LEU A C     1 
ATOM   6750  O O     . LEU A 1 2325 ? 226.788 228.556 216.250 1.00 28.47 ? 2325 LEU A O     1 
ATOM   6751  C CB    . LEU A 1 2325 ? 224.665 229.666 214.412 1.00 30.89 ? 2325 LEU A CB    1 
ATOM   6752  C CG    . LEU A 1 2325 ? 224.742 228.719 213.213 1.00 28.61 ? 2325 LEU A CG    1 
ATOM   6753  C CD1   . LEU A 1 2325 ? 223.501 227.847 213.127 1.00 27.55 ? 2325 LEU A CD1   1 
ATOM   6754  C CD2   . LEU A 1 2325 ? 224.933 229.509 211.931 1.00 27.68 ? 2325 LEU A CD2   1 
ATOM   6755  N N     . THR A 1 2326 ? 225.341 226.822 216.237 1.00 27.50 ? 2326 THR A N     1 
ATOM   6756  C CA    . THR A 1 2326 ? 226.352 225.810 216.536 1.00 30.12 ? 2326 THR A CA    1 
ATOM   6757  C C     . THR A 1 2326 ? 226.804 225.185 215.217 1.00 31.50 ? 2326 THR A C     1 
ATOM   6758  O O     . THR A 1 2326 ? 225.997 224.658 214.446 1.00 31.15 ? 2326 THR A O     1 
ATOM   6759  C CB    . THR A 1 2326 ? 225.820 224.778 217.533 1.00 32.36 ? 2326 THR A CB    1 
ATOM   6760  O OG1   . THR A 1 2326 ? 226.871 223.876 217.905 1.00 32.85 ? 2326 THR A OG1   1 
ATOM   6761  C CG2   . THR A 1 2326 ? 224.622 223.999 216.988 1.00 30.40 ? 2326 THR A CG2   1 
ATOM   6762  N N     . LEU A 1 2327 ? 228.100 225.291 214.940 1.00 35.18 ? 2327 LEU A N     1 
ATOM   6763  C CA    . LEU A 1 2327 ? 228.651 224.780 213.700 1.00 32.38 ? 2327 LEU A CA    1 
ATOM   6764  C C     . LEU A 1 2327 ? 229.170 223.357 213.893 1.00 36.51 ? 2327 LEU A C     1 
ATOM   6765  O O     . LEU A 1 2327 ? 229.413 222.920 215.020 1.00 36.95 ? 2327 LEU A O     1 
ATOM   6766  C CB    . LEU A 1 2327 ? 229.775 225.688 213.212 1.00 31.70 ? 2327 LEU A CB    1 
ATOM   6767  C CG    . LEU A 1 2327 ? 229.568 227.194 213.354 1.00 33.84 ? 2327 LEU A CG    1 
ATOM   6768  C CD1   . LEU A 1 2327 ? 230.837 227.916 212.973 1.00 33.37 ? 2327 LEU A CD1   1 
ATOM   6769  C CD2   . LEU A 1 2327 ? 228.410 227.663 212.492 1.00 33.73 ? 2327 LEU A CD2   1 
ATOM   6770  N N     . PRO A 1 2328 ? 229.342 222.608 212.800 1.00 38.64 ? 2328 PRO A N     1 
ATOM   6771  C CA    . PRO A 1 2328 ? 229.939 221.269 212.925 1.00 37.17 ? 2328 PRO A CA    1 
ATOM   6772  C C     . PRO A 1 2328 ? 231.347 221.281 213.496 1.00 37.95 ? 2328 PRO A C     1 
ATOM   6773  O O     . PRO A 1 2328 ? 231.749 220.300 214.135 1.00 38.60 ? 2328 PRO A O     1 
ATOM   6774  C CB    . PRO A 1 2328 ? 229.914 220.742 211.483 1.00 37.65 ? 2328 PRO A CB    1 
ATOM   6775  C CG    . PRO A 1 2328 ? 228.809 221.503 210.826 1.00 37.02 ? 2328 PRO A CG    1 
ATOM   6776  C CD    . PRO A 1 2328 ? 228.860 222.871 211.432 1.00 39.19 ? 2328 PRO A CD    1 
ATOM   6777  N N     . ASN A 1 2329 ? 232.112 222.356 213.292 1.00 36.72 ? 2329 ASN A N     1 
ATOM   6778  C CA    . ASN A 1 2329 ? 233.474 222.403 213.814 1.00 39.28 ? 2329 ASN A CA    1 
ATOM   6779  C C     . ASN A 1 2329 ? 233.534 222.788 215.286 1.00 42.20 ? 2329 ASN A C     1 
ATOM   6780  O O     . ASN A 1 2329 ? 234.623 222.760 215.869 1.00 43.45 ? 2329 ASN A O     1 
ATOM   6781  C CB    . ASN A 1 2329 ? 234.330 223.368 212.985 1.00 40.98 ? 2329 ASN A CB    1 
ATOM   6782  C CG    . ASN A 1 2329 ? 233.881 224.810 213.107 1.00 43.29 ? 2329 ASN A CG    1 
ATOM   6783  O OD1   . ASN A 1 2329 ? 232.811 225.101 213.639 1.00 44.15 ? 2329 ASN A OD1   1 
ATOM   6784  N ND2   . ASN A 1 2329 ? 234.701 225.726 212.605 1.00 39.81 ? 2329 ASN A ND2   1 
ATOM   6785  N N     . GLY A 1 2330 ? 232.405 223.150 215.896 1.00 40.20 ? 2330 GLY A N     1 
ATOM   6786  C CA    . GLY A 1 2330 ? 232.335 223.428 217.311 1.00 39.94 ? 2330 GLY A CA    1 
ATOM   6787  C C     . GLY A 1 2330 ? 232.283 224.897 217.675 1.00 40.95 ? 2330 GLY A C     1 
ATOM   6788  O O     . GLY A 1 2330 ? 232.000 225.221 218.834 1.00 42.37 ? 2330 GLY A O     1 
ATOM   6789  N N     . GLU A 1 2331 ? 232.557 225.792 216.729 1.00 36.67 ? 2331 GLU A N     1 
ATOM   6790  C CA    . GLU A 1 2331 ? 232.511 227.218 217.021 1.00 37.21 ? 2331 GLU A CA    1 
ATOM   6791  C C     . GLU A 1 2331 ? 231.067 227.682 217.171 1.00 36.04 ? 2331 GLU A C     1 
ATOM   6792  O O     . GLU A 1 2331 ? 230.148 227.107 216.583 1.00 37.76 ? 2331 GLU A O     1 
ATOM   6793  C CB    . GLU A 1 2331 ? 233.216 228.008 215.917 1.00 37.53 ? 2331 GLU A CB    1 
ATOM   6794  C CG    . GLU A 1 2331 ? 233.316 229.504 216.179 1.00 37.40 ? 2331 GLU A CG    1 
ATOM   6795  C CD    . GLU A 1 2331 ? 233.814 230.281 214.979 1.00 36.84 ? 2331 GLU A CD    1 
ATOM   6796  O OE1   . GLU A 1 2331 ? 234.129 229.650 213.949 1.00 35.09 ? 2331 GLU A OE1   1 
ATOM   6797  O OE2   . GLU A 1 2331 ? 233.891 231.524 215.067 1.00 36.12 ? 2331 GLU A OE2   1 
ATOM   6798  N N     . ARG A 1 2332 ? 230.869 228.725 217.974 1.00 34.39 ? 2332 ARG A N     1 
ATOM   6799  C CA    . ARG A 1 2332 ? 229.556 229.305 218.212 1.00 37.77 ? 2332 ARG A CA    1 
ATOM   6800  C C     . ARG A 1 2332 ? 229.563 230.778 217.828 1.00 38.69 ? 2332 ARG A C     1 
ATOM   6801  O O     . ARG A 1 2332 ? 230.458 231.530 218.227 1.00 35.51 ? 2332 ARG A O     1 
ATOM   6802  C CB    . ARG A 1 2332 ? 229.147 229.157 219.681 1.00 36.63 ? 2332 ARG A CB    1 
ATOM   6803  C CG    . ARG A 1 2332 ? 228.927 227.723 220.133 1.00 36.69 ? 2332 ARG A CG    1 
ATOM   6804  C CD    . ARG A 1 2332 ? 229.244 227.560 221.613 1.00 38.91 ? 2332 ARG A CD    1 
ATOM   6805  N NE    . ARG A 1 2332 ? 228.073 227.785 222.452 1.00 38.08 ? 2332 ARG A NE    1 
ATOM   6806  C CZ    . ARG A 1 2332 ? 227.984 228.731 223.377 1.00 37.92 ? 2332 ARG A CZ    1 
ATOM   6807  N NH1   . ARG A 1 2332 ? 228.983 229.566 223.611 1.00 36.48 ? 2332 ARG A NH1   1 
ATOM   6808  N NH2   . ARG A 1 2332 ? 226.863 228.843 224.085 1.00 38.92 ? 2332 ARG A NH2   1 
ATOM   6809  N N     . LEU A 1 2333 ? 228.561 231.186 217.051 1.00 36.19 ? 2333 LEU A N     1 
ATOM   6810  C CA    . LEU A 1 2333 ? 228.386 232.575 216.643 1.00 31.63 ? 2333 LEU A CA    1 
ATOM   6811  C C     . LEU A 1 2333 ? 227.067 233.078 217.211 1.00 32.00 ? 2333 LEU A C     1 
ATOM   6812  O O     . LEU A 1 2333 ? 226.022 232.454 217.001 1.00 30.47 ? 2333 LEU A O     1 
ATOM   6813  C CB    . LEU A 1 2333 ? 228.405 232.720 215.119 1.00 31.22 ? 2333 LEU A CB    1 
ATOM   6814  C CG    . LEU A 1 2333 ? 229.752 232.810 214.390 1.00 34.85 ? 2333 LEU A CG    1 
ATOM   6815  C CD1   . LEU A 1 2333 ? 230.510 234.068 214.795 1.00 33.11 ? 2333 LEU A CD1   1 
ATOM   6816  C CD2   . LEU A 1 2333 ? 230.605 231.570 214.607 1.00 34.27 ? 2333 LEU A CD2   1 
ATOM   6817  N N     . SER A 1 2334 ? 227.117 234.201 217.923 1.00 32.72 ? 2334 SER A N     1 
ATOM   6818  C CA    . SER A 1 2334 ? 225.941 234.758 218.579 1.00 28.47 ? 2334 SER A CA    1 
ATOM   6819  C C     . SER A 1 2334 ? 225.310 235.827 217.697 1.00 27.77 ? 2334 SER A C     1 
ATOM   6820  O O     . SER A 1 2334 ? 226.003 236.718 217.197 1.00 29.41 ? 2334 SER A O     1 
ATOM   6821  C CB    . SER A 1 2334 ? 226.310 235.345 219.941 1.00 27.58 ? 2334 SER A CB    1 
ATOM   6822  O OG    . SER A 1 2334 ? 227.127 236.494 219.795 1.00 26.70 ? 2334 SER A OG    1 
ATOM   6823  N N     . LEU A 1 2335 ? 224.001 235.738 217.519 1.00 24.38 ? 2335 LEU A N     1 
ATOM   6824  C CA    . LEU A 1 2335 ? 223.285 236.664 216.650 1.00 24.12 ? 2335 LEU A CA    1 
ATOM   6825  C C     . LEU A 1 2335 ? 223.216 238.049 217.282 1.00 22.79 ? 2335 LEU A C     1 
ATOM   6826  O O     . LEU A 1 2335 ? 222.683 238.189 218.390 1.00 25.95 ? 2335 LEU A O     1 
ATOM   6827  C CB    . LEU A 1 2335 ? 221.885 236.116 216.373 1.00 26.02 ? 2335 LEU A CB    1 
ATOM   6828  C CG    . LEU A 1 2335 ? 220.943 236.849 215.418 1.00 25.61 ? 2335 LEU A CG    1 
ATOM   6829  C CD1   . LEU A 1 2335 ? 220.145 235.850 214.615 1.00 22.75 ? 2335 LEU A CD1   1 
ATOM   6830  C CD2   . LEU A 1 2335 ? 219.994 237.732 216.199 1.00 27.51 ? 2335 LEU A CD2   1 
ATOM   6831  N N     . PRO A 1 2336 ? 223.740 239.089 216.628 1.00 22.97 ? 2336 PRO A N     1 
ATOM   6832  C CA    . PRO A 1 2336 ? 223.651 240.431 217.201 1.00 26.89 ? 2336 PRO A CA    1 
ATOM   6833  C C     . PRO A 1 2336 ? 222.210 240.900 217.262 1.00 26.48 ? 2336 PRO A C     1 
ATOM   6834  O O     . PRO A 1 2336 ? 221.373 240.487 216.442 1.00 29.54 ? 2336 PRO A O     1 
ATOM   6835  C CB    . PRO A 1 2336 ? 224.483 241.288 216.228 1.00 25.45 ? 2336 PRO A CB    1 
ATOM   6836  C CG    . PRO A 1 2336 ? 225.336 240.314 215.485 1.00 25.88 ? 2336 PRO A CG    1 
ATOM   6837  C CD    . PRO A 1 2336 ? 224.520 239.069 215.382 1.00 22.99 ? 2336 PRO A CD    1 
ATOM   6838  N N     . PRO A 1 2337 ? 221.874 241.781 218.209 1.00 25.85 ? 2337 PRO A N     1 
ATOM   6839  C CA    . PRO A 1 2337 ? 220.458 242.139 218.409 1.00 26.96 ? 2337 PRO A CA    1 
ATOM   6840  C C     . PRO A 1 2337 ? 219.809 242.812 217.211 1.00 26.82 ? 2337 PRO A C     1 
ATOM   6841  O O     . PRO A 1 2337 ? 218.575 242.812 217.112 1.00 32.43 ? 2337 PRO A O     1 
ATOM   6842  C CB    . PRO A 1 2337 ? 220.507 243.077 219.623 1.00 26.94 ? 2337 PRO A CB    1 
ATOM   6843  C CG    . PRO A 1 2337 ? 221.893 243.629 219.619 1.00 27.09 ? 2337 PRO A CG    1 
ATOM   6844  C CD    . PRO A 1 2337 ? 222.768 242.526 219.110 1.00 28.01 ? 2337 PRO A CD    1 
ATOM   6845  N N     . ASN A 1 2338 ? 220.592 243.394 216.302 1.00 23.68 ? 2338 ASN A N     1 
ATOM   6846  C CA    . ASN A 1 2338 ? 220.000 244.049 215.139 1.00 25.26 ? 2338 ASN A CA    1 
ATOM   6847  C C     . ASN A 1 2338 ? 219.542 243.045 214.086 1.00 23.59 ? 2338 ASN A C     1 
ATOM   6848  O O     . ASN A 1 2338 ? 218.715 243.382 213.231 1.00 25.60 ? 2338 ASN A O     1 
ATOM   6849  C CB    . ASN A 1 2338 ? 220.992 245.046 214.538 1.00 25.09 ? 2338 ASN A CB    1 
ATOM   6850  C CG    . ASN A 1 2338 ? 222.285 244.392 214.088 1.00 28.11 ? 2338 ASN A CG    1 
ATOM   6851  O OD1   . ASN A 1 2338 ? 222.433 243.173 214.140 1.00 29.84 ? 2338 ASN A OD1   1 
ATOM   6852  N ND2   . ASN A 1 2338 ? 223.228 245.207 213.638 1.00 26.50 ? 2338 ASN A ND2   1 
ATOM   6853  N N     . VAL A 1 2339 ? 220.064 241.819 214.126 1.00 21.45 ? 2339 VAL A N     1 
ATOM   6854  C CA    . VAL A 1 2339 ? 219.728 240.822 213.116 1.00 24.39 ? 2339 VAL A CA    1 
ATOM   6855  C C     . VAL A 1 2339 ? 218.329 240.280 213.368 1.00 24.01 ? 2339 VAL A C     1 
ATOM   6856  O O     . VAL A 1 2339 ? 217.963 239.959 214.507 1.00 19.43 ? 2339 VAL A O     1 
ATOM   6857  C CB    . VAL A 1 2339 ? 220.768 239.693 213.110 1.00 26.11 ? 2339 VAL A CB    1 
ATOM   6858  C CG1   . VAL A 1 2339 ? 220.434 238.666 212.040 1.00 24.24 ? 2339 VAL A CG1   1 
ATOM   6859  C CG2   . VAL A 1 2339 ? 222.151 240.256 212.879 1.00 23.70 ? 2339 VAL A CG2   1 
ATOM   6860  N N     . ARG A 1 2340 ? 217.537 240.177 212.302 1.00 19.55 ? 2340 ARG A N     1 
ATOM   6861  C CA    . ARG A 1 2340 ? 216.210 239.576 212.355 1.00 15.41 ? 2340 ARG A CA    1 
ATOM   6862  C C     . ARG A 1 2340 ? 216.146 238.476 211.308 1.00 11.52 ? 2340 ARG A C     1 
ATOM   6863  O O     . ARG A 1 2340 ? 216.382 238.733 210.123 1.00 20.71 ? 2340 ARG A O     1 
ATOM   6864  C CB    . ARG A 1 2340 ? 215.119 240.619 212.103 1.00 17.71 ? 2340 ARG A CB    1 
ATOM   6865  C CG    . ARG A 1 2340 ? 215.035 241.691 213.172 1.00 21.50 ? 2340 ARG A CG    1 
ATOM   6866  C CD    . ARG A 1 2340 ? 214.305 241.199 214.414 1.00 19.43 ? 2340 ARG A CD    1 
ATOM   6867  N NE    . ARG A 1 2340 ? 214.195 242.202 215.471 1.00 16.56 ? 2340 ARG A NE    1 
ATOM   6868  C CZ    . ARG A 1 2340 ? 215.198 242.913 215.974 1.00 19.07 ? 2340 ARG A CZ    1 
ATOM   6869  N NH1   . ARG A 1 2340 ? 216.454 242.698 215.617 1.00 19.07 ? 2340 ARG A NH1   1 
ATOM   6870  N NH2   . ARG A 1 2340 ? 214.936 243.849 216.880 1.00 23.54 ? 2340 ARG A NH2   1 
ATOM   6871  N N     . ILE A 1 2341 ? 215.827 237.260 211.737 1.00 4.56  ? 2341 ILE A N     1 
ATOM   6872  C CA    . ILE A 1 2341 ? 215.769 236.100 210.854 1.00 8.05  ? 2341 ILE A CA    1 
ATOM   6873  C C     . ILE A 1 2341 ? 214.328 235.979 210.377 1.00 11.20 ? 2341 ILE A C     1 
ATOM   6874  O O     . ILE A 1 2341 ? 213.459 235.491 211.101 1.00 19.24 ? 2341 ILE A O     1 
ATOM   6875  C CB    . ILE A 1 2341 ? 216.244 234.826 211.554 1.00 9.99  ? 2341 ILE A CB    1 
ATOM   6876  C CG1   . ILE A 1 2341 ? 217.657 235.020 212.101 1.00 10.06 ? 2341 ILE A CG1   1 
ATOM   6877  C CG2   . ILE A 1 2341 ? 216.199 233.650 210.596 1.00 10.84 ? 2341 ILE A CG2   1 
ATOM   6878  C CD1   . ILE A 1 2341 ? 218.709 235.166 211.028 1.00 16.47 ? 2341 ILE A CD1   1 
ATOM   6879  N N     . MET A 1 2342 ? 214.073 236.407 209.148 1.00 6.66  ? 2342 MET A N     1 
ATOM   6880  C CA    . MET A 1 2342 ? 212.723 236.513 208.621 1.00 3.35  ? 2342 MET A CA    1 
ATOM   6881  C C     . MET A 1 2342 ? 212.459 235.378 207.642 1.00 3.27  ? 2342 MET A C     1 
ATOM   6882  O O     . MET A 1 2342 ? 213.275 235.106 206.757 1.00 14.22 ? 2342 MET A O     1 
ATOM   6883  C CB    . MET A 1 2342 ? 212.527 237.874 207.951 1.00 3.77  ? 2342 MET A CB    1 
ATOM   6884  C CG    . MET A 1 2342 ? 212.192 238.990 208.932 1.00 6.62  ? 2342 MET A CG    1 
ATOM   6885  S SD    . MET A 1 2342 ? 212.331 240.633 208.209 1.00 26.84 ? 2342 MET A SD    1 
ATOM   6886  C CE    . MET A 1 2342 ? 210.617 241.081 208.004 1.00 13.53 ? 2342 MET A CE    1 
ATOM   6887  N N     . PHE A 1 2343 ? 211.329 234.702 207.823 1.00 0.50  ? 2343 PHE A N     1 
ATOM   6888  C CA    . PHE A 1 2343 ? 210.936 233.568 206.991 1.00 2.18  ? 2343 PHE A CA    1 
ATOM   6889  C C     . PHE A 1 2343 ? 209.741 233.992 206.147 1.00 6.04  ? 2343 PHE A C     1 
ATOM   6890  O O     . PHE A 1 2343 ? 208.597 233.939 206.604 1.00 6.62  ? 2343 PHE A O     1 
ATOM   6891  C CB    . PHE A 1 2343 ? 210.592 232.349 207.839 1.00 4.02  ? 2343 PHE A CB    1 
ATOM   6892  C CG    . PHE A 1 2343 ? 211.769 231.733 208.528 1.00 8.68  ? 2343 PHE A CG    1 
ATOM   6893  C CD1   . PHE A 1 2343 ? 212.214 232.222 209.743 1.00 10.22 ? 2343 PHE A CD1   1 
ATOM   6894  C CD2   . PHE A 1 2343 ? 212.435 230.665 207.957 1.00 12.02 ? 2343 PHE A CD2   1 
ATOM   6895  C CE1   . PHE A 1 2343 ? 213.294 231.650 210.376 1.00 7.77  ? 2343 PHE A CE1   1 
ATOM   6896  C CE2   . PHE A 1 2343 ? 213.517 230.094 208.584 1.00 10.55 ? 2343 PHE A CE2   1 
ATOM   6897  C CZ    . PHE A 1 2343 ? 213.948 230.587 209.794 1.00 8.24  ? 2343 PHE A CZ    1 
ATOM   6898  N N     . GLU A 1 2344 ? 210.009 234.411 204.916 1.00 10.11 ? 2344 GLU A N     1 
ATOM   6899  C CA    . GLU A 1 2344 ? 208.951 234.744 203.965 1.00 5.57  ? 2344 GLU A CA    1 
ATOM   6900  C C     . GLU A 1 2344 ? 208.577 233.479 203.203 1.00 1.95  ? 2344 GLU A C     1 
ATOM   6901  O O     . GLU A 1 2344 ? 209.237 233.104 202.233 1.00 5.16  ? 2344 GLU A O     1 
ATOM   6902  C CB    . GLU A 1 2344 ? 209.418 235.853 203.030 1.00 4.85  ? 2344 GLU A CB    1 
ATOM   6903  C CG    . GLU A 1 2344 ? 208.385 236.321 202.026 1.00 6.00  ? 2344 GLU A CG    1 
ATOM   6904  C CD    . GLU A 1 2344 ? 209.000 237.172 200.934 1.00 16.57 ? 2344 GLU A CD    1 
ATOM   6905  O OE1   . GLU A 1 2344 ? 209.978 237.892 201.220 1.00 19.95 ? 2344 GLU A OE1   1 
ATOM   6906  O OE2   . GLU A 1 2344 ? 208.524 237.107 199.784 1.00 15.60 ? 2344 GLU A OE2   1 
ATOM   6907  N N     . VAL A 1 2345 ? 207.517 232.809 203.649 1.00 1.20  ? 2345 VAL A N     1 
ATOM   6908  C CA    . VAL A 1 2345 ? 207.139 231.499 203.139 1.00 1.27  ? 2345 VAL A CA    1 
ATOM   6909  C C     . VAL A 1 2345 ? 205.662 231.543 202.749 1.00 3.53  ? 2345 VAL A C     1 
ATOM   6910  O O     . VAL A 1 2345 ? 204.906 232.407 203.188 1.00 10.08 ? 2345 VAL A O     1 
ATOM   6911  C CB    . VAL A 1 2345 ? 207.417 230.379 204.166 1.00 2.28  ? 2345 VAL A CB    1 
ATOM   6912  C CG1   . VAL A 1 2345 ? 206.517 230.526 205.378 1.00 2.79  ? 2345 VAL A CG1   1 
ATOM   6913  C CG2   . VAL A 1 2345 ? 207.298 228.992 203.545 1.00 8.36  ? 2345 VAL A CG2   1 
ATOM   6914  N N     . GLN A 1 2346 ? 205.264 230.598 201.899 1.00 3.22  ? 2346 GLN A N     1 
ATOM   6915  C CA    . GLN A 1 2346 ? 203.901 230.506 201.392 1.00 0.67  ? 2346 GLN A CA    1 
ATOM   6916  C C     . GLN A 1 2346 ? 202.972 229.715 202.305 1.00 5.43  ? 2346 GLN A C     1 
ATOM   6917  O O     . GLN A 1 2346 ? 201.794 230.061 202.429 1.00 7.87  ? 2346 GLN A O     1 
ATOM   6918  C CB    . GLN A 1 2346 ? 203.907 229.873 199.997 1.00 1.22  ? 2346 GLN A CB    1 
ATOM   6919  C CG    . GLN A 1 2346 ? 202.545 229.796 199.334 1.00 4.15  ? 2346 GLN A CG    1 
ATOM   6920  C CD    . GLN A 1 2346 ? 202.588 229.077 198.002 1.00 10.34 ? 2346 GLN A CD    1 
ATOM   6921  O OE1   . GLN A 1 2346 ? 203.578 228.430 197.664 1.00 13.74 ? 2346 GLN A OE1   1 
ATOM   6922  N NE2   . GLN A 1 2346 ? 201.511 229.191 197.235 1.00 10.78 ? 2346 GLN A NE2   1 
ATOM   6923  N N     . ASP A 1 2347 ? 203.466 228.659 202.946 1.00 9.66  ? 2347 ASP A N     1 
ATOM   6924  C CA    . ASP A 1 2347 ? 202.633 227.852 203.826 1.00 9.68  ? 2347 ASP A CA    1 
ATOM   6925  C C     . ASP A 1 2347 ? 203.518 227.116 204.818 1.00 12.03 ? 2347 ASP A C     1 
ATOM   6926  O O     . ASP A 1 2347 ? 204.736 227.023 204.643 1.00 18.46 ? 2347 ASP A O     1 
ATOM   6927  C CB    . ASP A 1 2347 ? 201.774 226.859 203.037 1.00 14.76 ? 2347 ASP A CB    1 
ATOM   6928  C CG    . ASP A 1 2347 ? 200.432 226.601 203.693 1.00 17.57 ? 2347 ASP A CG    1 
ATOM   6929  O OD1   . ASP A 1 2347 ? 200.314 226.830 204.915 1.00 10.77 ? 2347 ASP A OD1   1 
ATOM   6930  O OD2   . ASP A 1 2347 ? 199.498 226.165 202.988 1.00 17.46 ? 2347 ASP A OD2   1 
ATOM   6931  N N     . LEU A 1 2348 ? 202.884 226.595 205.868 1.00 6.67  ? 2348 LEU A N     1 
ATOM   6932  C CA    . LEU A 1 2348 ? 203.566 225.843 206.914 1.00 9.66  ? 2348 LEU A CA    1 
ATOM   6933  C C     . LEU A 1 2348 ? 203.177 224.367 206.904 1.00 16.45 ? 2348 LEU A C     1 
ATOM   6934  O O     . LEU A 1 2348 ? 203.042 223.748 207.962 1.00 20.04 ? 2348 LEU A O     1 
ATOM   6935  C CB    . LEU A 1 2348 ? 203.281 226.457 208.284 1.00 13.24 ? 2348 LEU A CB    1 
ATOM   6936  C CG    . LEU A 1 2348 ? 203.691 227.917 208.469 1.00 13.95 ? 2348 LEU A CG    1 
ATOM   6937  C CD1   . LEU A 1 2348 ? 203.413 228.373 209.887 1.00 7.75  ? 2348 LEU A CD1   1 
ATOM   6938  C CD2   . LEU A 1 2348 ? 205.157 228.089 208.127 1.00 11.45 ? 2348 LEU A CD2   1 
ATOM   6939  N N     . LYS A 1 2349 ? 202.991 223.792 205.714 1.00 17.16 ? 2349 LYS A N     1 
ATOM   6940  C CA    . LYS A 1 2349 ? 202.606 222.388 205.625 1.00 16.73 ? 2349 LYS A CA    1 
ATOM   6941  C C     . LYS A 1 2349 ? 203.736 221.462 206.054 1.00 17.73 ? 2349 LYS A C     1 
ATOM   6942  O O     . LYS A 1 2349 ? 203.479 220.377 206.588 1.00 13.99 ? 2349 LYS A O     1 
ATOM   6943  C CB    . LYS A 1 2349 ? 202.166 222.051 204.201 1.00 15.29 ? 2349 LYS A CB    1 
ATOM   6944  C CG    . LYS A 1 2349 ? 200.784 222.558 203.842 1.00 17.25 ? 2349 LYS A CG    1 
ATOM   6945  C CD    . LYS A 1 2349 ? 200.292 221.931 202.548 1.00 15.83 ? 2349 LYS A CD    1 
ATOM   6946  C CE    . LYS A 1 2349 ? 200.197 220.419 202.672 1.00 20.39 ? 2349 LYS A CE    1 
ATOM   6947  N NZ    . LYS A 1 2349 ? 199.392 220.008 203.855 1.00 19.16 ? 2349 LYS A NZ    1 
ATOM   6948  N N     . TYR A 1 2350 ? 204.982 221.865 205.833 1.00 18.58 ? 2350 TYR A N     1 
ATOM   6949  C CA    . TYR A 1 2350 ? 206.145 221.024 206.090 1.00 21.60 ? 2350 TYR A CA    1 
ATOM   6950  C C     . TYR A 1 2350 ? 207.102 221.724 207.042 1.00 23.48 ? 2350 TYR A C     1 
ATOM   6951  O O     . TYR A 1 2350 ? 208.319 221.731 206.854 1.00 24.39 ? 2350 TYR A O     1 
ATOM   6952  C CB    . TYR A 1 2350 ? 206.835 220.660 204.780 1.00 20.57 ? 2350 TYR A CB    1 
ATOM   6953  C CG    . TYR A 1 2350 ? 205.915 219.985 203.790 1.00 20.01 ? 2350 TYR A CG    1 
ATOM   6954  C CD1   . TYR A 1 2350 ? 205.285 218.789 204.101 1.00 19.28 ? 2350 TYR A CD1   1 
ATOM   6955  C CD2   . TYR A 1 2350 ? 205.657 220.558 202.553 1.00 22.11 ? 2350 TYR A CD2   1 
ATOM   6956  C CE1   . TYR A 1 2350 ? 204.437 218.174 203.202 1.00 21.18 ? 2350 TYR A CE1   1 
ATOM   6957  C CE2   . TYR A 1 2350 ? 204.810 219.951 201.648 1.00 22.52 ? 2350 TYR A CE2   1 
ATOM   6958  C CZ    . TYR A 1 2350 ? 204.203 218.760 201.977 1.00 22.22 ? 2350 TYR A CZ    1 
ATOM   6959  O OH    . TYR A 1 2350 ? 203.358 218.152 201.079 1.00 18.79 ? 2350 TYR A OH    1 
ATOM   6960  N N     . ALA A 1 2351 ? 206.549 222.335 208.085 1.00 17.27 ? 2351 ALA A N     1 
ATOM   6961  C CA    . ALA A 1 2351 ? 207.330 223.011 209.111 1.00 15.13 ? 2351 ALA A CA    1 
ATOM   6962  C C     . ALA A 1 2351 ? 207.143 222.284 210.433 1.00 20.51 ? 2351 ALA A C     1 
ATOM   6963  O O     . ALA A 1 2351 ? 206.009 222.002 210.834 1.00 19.52 ? 2351 ALA A O     1 
ATOM   6964  C CB    . ALA A 1 2351 ? 206.915 224.477 209.247 1.00 12.79 ? 2351 ALA A CB    1 
ATOM   6965  N N     . THR A 1 2352 ? 208.252 221.980 211.101 1.00 21.90 ? 2352 THR A N     1 
ATOM   6966  C CA    . THR A 1 2352 ? 208.188 221.308 212.389 1.00 17.46 ? 2352 THR A CA    1 
ATOM   6967  C C     . THR A 1 2352 ? 207.524 222.205 213.425 1.00 18.17 ? 2352 THR A C     1 
ATOM   6968  O O     . THR A 1 2352 ? 207.578 223.435 213.341 1.00 15.98 ? 2352 THR A O     1 
ATOM   6969  C CB    . THR A 1 2352 ? 209.587 220.917 212.864 1.00 19.22 ? 2352 THR A CB    1 
ATOM   6970  O OG1   . THR A 1 2352 ? 210.455 222.055 212.794 1.00 18.21 ? 2352 THR A OG1   1 
ATOM   6971  C CG2   . THR A 1 2352 ? 210.150 219.803 212.003 1.00 16.39 ? 2352 THR A CG2   1 
ATOM   6972  N N     . LEU A 1 2353 ? 206.883 221.572 214.411 1.00 18.19 ? 2353 LEU A N     1 
ATOM   6973  C CA    . LEU A 1 2353 ? 206.239 222.332 215.476 1.00 17.65 ? 2353 LEU A CA    1 
ATOM   6974  C C     . LEU A 1 2353 ? 207.246 223.181 216.239 1.00 17.95 ? 2353 LEU A C     1 
ATOM   6975  O O     . LEU A 1 2353 ? 206.909 224.272 216.711 1.00 18.07 ? 2353 LEU A O     1 
ATOM   6976  C CB    . LEU A 1 2353 ? 205.502 221.390 216.427 1.00 18.94 ? 2353 LEU A CB    1 
ATOM   6977  C CG    . LEU A 1 2353 ? 204.720 222.055 217.561 1.00 19.33 ? 2353 LEU A CG    1 
ATOM   6978  C CD1   . LEU A 1 2353 ? 203.611 222.932 217.003 1.00 19.24 ? 2353 LEU A CD1   1 
ATOM   6979  C CD2   . LEU A 1 2353 ? 204.156 221.012 218.511 1.00 17.98 ? 2353 LEU A CD2   1 
ATOM   6980  N N     . ALA A 1 2354 ? 208.488 222.707 216.355 1.00 20.02 ? 2354 ALA A N     1 
ATOM   6981  C CA    . ALA A 1 2354 ? 209.515 223.468 217.056 1.00 19.71 ? 2354 ALA A CA    1 
ATOM   6982  C C     . ALA A 1 2354 ? 209.797 224.792 216.356 1.00 16.13 ? 2354 ALA A C     1 
ATOM   6983  O O     . ALA A 1 2354 ? 209.865 225.846 216.999 1.00 22.13 ? 2354 ALA A O     1 
ATOM   6984  C CB    . ALA A 1 2354 ? 210.789 222.633 217.169 1.00 20.85 ? 2354 ALA A CB    1 
ATOM   6985  N N     . THR A 1 2355 ? 209.955 224.758 215.031 1.00 16.31 ? 2355 THR A N     1 
ATOM   6986  C CA    . THR A 1 2355 ? 210.299 225.972 214.297 1.00 18.80 ? 2355 THR A CA    1 
ATOM   6987  C C     . THR A 1 2355 ? 209.144 226.966 214.290 1.00 18.45 ? 2355 THR A C     1 
ATOM   6988  O O     . THR A 1 2355 ? 209.355 228.173 214.456 1.00 22.15 ? 2355 THR A O     1 
ATOM   6989  C CB    . THR A 1 2355 ? 210.712 225.622 212.867 1.00 19.90 ? 2355 THR A CB    1 
ATOM   6990  O OG1   . THR A 1 2355 ? 211.729 224.614 212.896 1.00 22.78 ? 2355 THR A OG1   1 
ATOM   6991  C CG2   . THR A 1 2355 ? 211.250 226.852 212.152 1.00 12.66 ? 2355 THR A CG2   1 
ATOM   6992  N N     . VAL A 1 2356 ? 207.916 226.481 214.096 1.00 18.03 ? 2356 VAL A N     1 
ATOM   6993  C CA    . VAL A 1 2356 ? 206.769 227.382 214.061 1.00 16.60 ? 2356 VAL A CA    1 
ATOM   6994  C C     . VAL A 1 2356 ? 206.502 227.965 215.445 1.00 15.14 ? 2356 VAL A C     1 
ATOM   6995  O O     . VAL A 1 2356 ? 206.142 229.141 215.577 1.00 17.69 ? 2356 VAL A O     1 
ATOM   6996  C CB    . VAL A 1 2356 ? 205.535 226.660 213.485 1.00 18.12 ? 2356 VAL A CB    1 
ATOM   6997  C CG1   . VAL A 1 2356 ? 205.202 225.427 214.283 1.00 20.13 ? 2356 VAL A CG1   1 
ATOM   6998  C CG2   . VAL A 1 2356 ? 204.339 227.581 213.451 1.00 16.90 ? 2356 VAL A CG2   1 
ATOM   6999  N N     . SER A 1 2357 ? 206.687 227.165 216.498 1.00 13.87 ? 2357 SER A N     1 
ATOM   7000  C CA    . SER A 1 2357 ? 206.442 227.640 217.854 1.00 14.64 ? 2357 SER A CA    1 
ATOM   7001  C C     . SER A 1 2357 ? 207.590 228.471 218.408 1.00 15.69 ? 2357 SER A C     1 
ATOM   7002  O O     . SER A 1 2357 ? 207.402 229.167 219.411 1.00 15.83 ? 2357 SER A O     1 
ATOM   7003  C CB    . SER A 1 2357 ? 206.176 226.456 218.784 1.00 16.80 ? 2357 SER A CB    1 
ATOM   7004  O OG    . SER A 1 2357 ? 207.309 225.610 218.864 1.00 19.97 ? 2357 SER A OG    1 
ATOM   7005  N N     . ARG A 1 2358 ? 208.763 228.423 217.784 1.00 14.95 ? 2358 ARG A N     1 
ATOM   7006  C CA    . ARG A 1 2358 ? 209.929 229.149 218.267 1.00 16.97 ? 2358 ARG A CA    1 
ATOM   7007  C C     . ARG A 1 2358 ? 209.979 230.593 217.783 1.00 11.50 ? 2358 ARG A C     1 
ATOM   7008  O O     . ARG A 1 2358 ? 210.932 231.308 218.108 1.00 7.80  ? 2358 ARG A O     1 
ATOM   7009  C CB    . ARG A 1 2358 ? 211.210 228.413 217.854 1.00 17.61 ? 2358 ARG A CB    1 
ATOM   7010  C CG    . ARG A 1 2358 ? 212.417 228.724 218.725 1.00 19.94 ? 2358 ARG A CG    1 
ATOM   7011  C CD    . ARG A 1 2358 ? 213.598 227.823 218.423 1.00 17.82 ? 2358 ARG A CD    1 
ATOM   7012  N NE    . ARG A 1 2358 ? 213.219 226.434 218.203 1.00 16.83 ? 2358 ARG A NE    1 
ATOM   7013  C CZ    . ARG A 1 2358 ? 213.500 225.449 219.044 1.00 19.23 ? 2358 ARG A CZ    1 
ATOM   7014  N NH1   . ARG A 1 2358 ? 214.164 225.669 220.167 1.00 19.80 ? 2358 ARG A NH1   1 
ATOM   7015  N NH2   . ARG A 1 2358 ? 213.113 224.212 218.750 1.00 19.13 ? 2358 ARG A NH2   1 
ATOM   7016  N N     . CYS A 1 2359 ? 208.983 231.049 217.029 1.00 14.77 ? 2359 CYS A N     1 
ATOM   7017  C CA    . CYS A 1 2359 ? 209.024 232.411 216.520 1.00 17.72 ? 2359 CYS A CA    1 
ATOM   7018  C C     . CYS A 1 2359 ? 207.613 232.891 216.218 1.00 11.32 ? 2359 CYS A C     1 
ATOM   7019  O O     . CYS A 1 2359 ? 206.758 232.116 215.782 1.00 5.76  ? 2359 CYS A O     1 
ATOM   7020  C CB    . CYS A 1 2359 ? 209.895 232.504 215.267 1.00 16.43 ? 2359 CYS A CB    1 
ATOM   7021  S SG    . CYS A 1 2359 ? 209.416 231.386 213.933 1.00 10.90 ? 2359 CYS A SG    1 
ATOM   7022  N N     . GLY A 1 2360 ? 207.388 234.180 216.450 1.00 11.44 ? 2360 GLY A N     1 
ATOM   7023  C CA    . GLY A 1 2360 ? 206.111 234.783 216.139 1.00 12.51 ? 2360 GLY A CA    1 
ATOM   7024  C C     . GLY A 1 2360 ? 205.938 234.997 214.650 1.00 2.99  ? 2360 GLY A C     1 
ATOM   7025  O O     . GLY A 1 2360 ? 206.873 234.896 213.858 1.00 5.15  ? 2360 GLY A O     1 
ATOM   7026  N N     . MET A 1 2361 ? 204.705 235.307 214.260 1.00 1.64  ? 2361 MET A N     1 
ATOM   7027  C CA    . MET A 1 2361 ? 204.405 235.440 212.845 1.00 2.01  ? 2361 MET A CA    1 
ATOM   7028  C C     . MET A 1 2361 ? 203.218 236.362 212.635 1.00 5.65  ? 2361 MET A C     1 
ATOM   7029  O O     . MET A 1 2361 ? 202.438 236.633 213.550 1.00 14.66 ? 2361 MET A O     1 
ATOM   7030  C CB    . MET A 1 2361 ? 204.098 234.090 212.201 1.00 2.90  ? 2361 MET A CB    1 
ATOM   7031  C CG    . MET A 1 2361 ? 202.852 233.428 212.728 1.00 0.93  ? 2361 MET A CG    1 
ATOM   7032  S SD    . MET A 1 2361 ? 202.661 231.816 211.969 1.00 13.63 ? 2361 MET A SD    1 
ATOM   7033  C CE    . MET A 1 2361 ? 203.959 230.944 212.826 1.00 6.39  ? 2361 MET A CE    1 
ATOM   7034  N N     . VAL A 1 2362 ? 203.096 236.830 211.397 1.00 0.00  ? 2362 VAL A N     1 
ATOM   7035  C CA    . VAL A 1 2362 ? 201.922 237.541 210.914 1.00 0.00  ? 2362 VAL A CA    1 
ATOM   7036  C C     . VAL A 1 2362 ? 201.440 236.840 209.651 1.00 0.00  ? 2362 VAL A C     1 
ATOM   7037  O O     . VAL A 1 2362 ? 202.235 236.529 208.758 1.00 9.59  ? 2362 VAL A O     1 
ATOM   7038  C CB    . VAL A 1 2362 ? 202.223 239.035 210.661 1.00 1.39  ? 2362 VAL A CB    1 
ATOM   7039  C CG1   . VAL A 1 2362 ? 203.382 239.201 209.698 1.00 4.84  ? 2362 VAL A CG1   1 
ATOM   7040  C CG2   . VAL A 1 2362 ? 200.993 239.738 210.127 1.00 5.06  ? 2362 VAL A CG2   1 
ATOM   7041  N N     . TRP A 1 2363 ? 200.143 236.556 209.593 1.00 0.00  ? 2363 TRP A N     1 
ATOM   7042  C CA    . TRP A 1 2363 ? 199.559 235.835 208.469 1.00 0.00  ? 2363 TRP A CA    1 
ATOM   7043  C C     . TRP A 1 2363 ? 199.083 236.826 207.415 1.00 1.50  ? 2363 TRP A C     1 
ATOM   7044  O O     . TRP A 1 2363 ? 198.240 237.683 207.698 1.00 5.93  ? 2363 TRP A O     1 
ATOM   7045  C CB    . TRP A 1 2363 ? 198.400 234.956 208.931 1.00 0.39  ? 2363 TRP A CB    1 
ATOM   7046  C CG    . TRP A 1 2363 ? 197.806 234.136 207.835 1.00 0.00  ? 2363 TRP A CG    1 
ATOM   7047  C CD1   . TRP A 1 2363 ? 196.763 234.480 207.032 1.00 1.24  ? 2363 TRP A CD1   1 
ATOM   7048  C CD2   . TRP A 1 2363 ? 198.216 232.828 207.422 1.00 4.49  ? 2363 TRP A CD2   1 
ATOM   7049  N NE1   . TRP A 1 2363 ? 196.497 233.472 206.140 1.00 2.19  ? 2363 TRP A NE1   1 
ATOM   7050  C CE2   . TRP A 1 2363 ? 197.376 232.445 206.360 1.00 3.91  ? 2363 TRP A CE2   1 
ATOM   7051  C CE3   . TRP A 1 2363 ? 199.211 231.944 207.847 1.00 1.53  ? 2363 TRP A CE3   1 
ATOM   7052  C CZ2   . TRP A 1 2363 ? 197.501 231.218 205.717 1.00 4.09  ? 2363 TRP A CZ2   1 
ATOM   7053  C CZ3   . TRP A 1 2363 ? 199.331 230.727 207.210 1.00 0.79  ? 2363 TRP A CZ3   1 
ATOM   7054  C CH2   . TRP A 1 2363 ? 198.483 230.375 206.155 1.00 4.38  ? 2363 TRP A CH2   1 
ATOM   7055  N N     . PHE A 1 2364 ? 199.615 236.701 206.201 1.00 3.13  ? 2364 PHE A N     1 
ATOM   7056  C CA    . PHE A 1 2364 ? 199.226 237.554 205.081 1.00 0.00  ? 2364 PHE A CA    1 
ATOM   7057  C C     . PHE A 1 2364 ? 198.192 236.807 204.247 1.00 0.00  ? 2364 PHE A C     1 
ATOM   7058  O O     . PHE A 1 2364 ? 198.516 236.063 203.325 1.00 2.68  ? 2364 PHE A O     1 
ATOM   7059  C CB    . PHE A 1 2364 ? 200.441 237.934 204.246 1.00 0.00  ? 2364 PHE A CB    1 
ATOM   7060  C CG    . PHE A 1 2364 ? 201.263 239.036 204.831 1.00 0.00  ? 2364 PHE A CG    1 
ATOM   7061  C CD1   . PHE A 1 2364 ? 202.284 238.755 205.720 1.00 0.00  ? 2364 PHE A CD1   1 
ATOM   7062  C CD2   . PHE A 1 2364 ? 201.035 240.349 204.472 1.00 0.06  ? 2364 PHE A CD2   1 
ATOM   7063  C CE1   . PHE A 1 2364 ? 203.049 239.764 206.251 1.00 0.00  ? 2364 PHE A CE1   1 
ATOM   7064  C CE2   . PHE A 1 2364 ? 201.799 241.362 205.001 1.00 0.00  ? 2364 PHE A CE2   1 
ATOM   7065  C CZ    . PHE A 1 2364 ? 202.808 241.069 205.892 1.00 2.00  ? 2364 PHE A CZ    1 
ATOM   7066  N N     . SER A 1 2365 ? 196.924 237.020 204.576 1.00 0.75  ? 2365 SER A N     1 
ATOM   7067  C CA    . SER A 1 2365 ? 195.865 236.390 203.809 1.00 0.87  ? 2365 SER A CA    1 
ATOM   7068  C C     . SER A 1 2365 ? 195.805 236.987 202.406 1.00 0.90  ? 2365 SER A C     1 
ATOM   7069  O O     . SER A 1 2365 ? 196.371 238.044 202.128 1.00 4.66  ? 2365 SER A O     1 
ATOM   7070  C CB    . SER A 1 2365 ? 194.519 236.555 204.512 1.00 4.71  ? 2365 SER A CB    1 
ATOM   7071  O OG    . SER A 1 2365 ? 193.481 235.957 203.759 1.00 10.15 ? 2365 SER A OG    1 
ATOM   7072  N N     . GLU A 1 2366 ? 195.117 236.282 201.508 1.00 3.28  ? 2366 GLU A N     1 
ATOM   7073  C CA    . GLU A 1 2366 ? 194.972 236.776 200.144 1.00 0.00  ? 2366 GLU A CA    1 
ATOM   7074  C C     . GLU A 1 2366 ? 194.068 238.000 200.069 1.00 0.00  ? 2366 GLU A C     1 
ATOM   7075  O O     . GLU A 1 2366 ? 194.049 238.680 199.039 1.00 0.72  ? 2366 GLU A O     1 
ATOM   7076  C CB    . GLU A 1 2366 ? 194.431 235.667 199.239 1.00 3.80  ? 2366 GLU A CB    1 
ATOM   7077  C CG    . GLU A 1 2366 ? 194.713 235.869 197.757 1.00 6.86  ? 2366 GLU A CG    1 
ATOM   7078  C CD    . GLU A 1 2366 ? 196.153 235.565 197.387 1.00 8.88  ? 2366 GLU A CD    1 
ATOM   7079  O OE1   . GLU A 1 2366 ? 196.949 236.517 197.248 1.00 7.57  ? 2366 GLU A OE1   1 
ATOM   7080  O OE2   . GLU A 1 2366 ? 196.486 234.373 197.226 1.00 7.50  ? 2366 GLU A OE2   1 
ATOM   7081  N N     . ASP A 1 2367 ? 193.326 238.297 201.136 1.00 0.65  ? 2367 ASP A N     1 
ATOM   7082  C CA    . ASP A 1 2367 ? 192.395 239.416 201.127 1.00 0.09  ? 2367 ASP A CA    1 
ATOM   7083  C C     . ASP A 1 2367 ? 193.058 240.751 201.441 1.00 2.40  ? 2367 ASP A C     1 
ATOM   7084  O O     . ASP A 1 2367 ? 192.453 241.797 201.181 1.00 2.45  ? 2367 ASP A O     1 
ATOM   7085  C CB    . ASP A 1 2367 ? 191.268 239.166 202.130 1.00 3.67  ? 2367 ASP A CB    1 
ATOM   7086  C CG    . ASP A 1 2367 ? 190.240 238.181 201.616 1.00 6.25  ? 2367 ASP A CG    1 
ATOM   7087  O OD1   . ASP A 1 2367 ? 189.463 238.548 200.709 1.00 12.62 ? 2367 ASP A OD1   1 
ATOM   7088  O OD2   . ASP A 1 2367 ? 190.208 237.038 202.118 1.00 3.14  ? 2367 ASP A OD2   1 
ATOM   7089  N N     . VAL A 1 2368 ? 194.271 240.749 201.997 1.00 3.27  ? 2368 VAL A N     1 
ATOM   7090  C CA    . VAL A 1 2368 ? 194.915 242.010 202.352 1.00 2.23  ? 2368 VAL A CA    1 
ATOM   7091  C C     . VAL A 1 2368 ? 195.292 242.783 201.094 1.00 1.74  ? 2368 VAL A C     1 
ATOM   7092  O O     . VAL A 1 2368 ? 195.242 244.018 201.066 1.00 2.98  ? 2368 VAL A O     1 
ATOM   7093  C CB    . VAL A 1 2368 ? 196.135 241.771 203.263 1.00 1.84  ? 2368 VAL A CB    1 
ATOM   7094  C CG1   . VAL A 1 2368 ? 195.709 241.093 204.555 1.00 2.57  ? 2368 VAL A CG1   1 
ATOM   7095  C CG2   . VAL A 1 2368 ? 197.222 240.980 202.556 1.00 0.00  ? 2368 VAL A CG2   1 
ATOM   7096  N N     . LEU A 1 2369 ? 195.676 242.070 200.039 1.00 0.00  ? 2369 LEU A N     1 
ATOM   7097  C CA    . LEU A 1 2369 ? 196.054 242.682 198.771 1.00 0.00  ? 2369 LEU A CA    1 
ATOM   7098  C C     . LEU A 1 2369 ? 194.896 242.514 197.794 1.00 0.00  ? 2369 LEU A C     1 
ATOM   7099  O O     . LEU A 1 2369 ? 194.692 241.428 197.244 1.00 2.97  ? 2369 LEU A O     1 
ATOM   7100  C CB    . LEU A 1 2369 ? 197.331 242.042 198.236 1.00 0.05  ? 2369 LEU A CB    1 
ATOM   7101  C CG    . LEU A 1 2369 ? 197.986 242.671 197.009 1.00 0.62  ? 2369 LEU A CG    1 
ATOM   7102  C CD1   . LEU A 1 2369 ? 198.136 244.164 197.194 1.00 2.17  ? 2369 LEU A CD1   1 
ATOM   7103  C CD2   . LEU A 1 2369 ? 199.333 242.032 196.755 1.00 1.88  ? 2369 LEU A CD2   1 
ATOM   7104  N N     . SER A 1 2370 ? 194.138 243.583 197.581 1.00 0.00  ? 2370 SER A N     1 
ATOM   7105  C CA    . SER A 1 2370 ? 192.984 243.535 196.700 1.00 0.00  ? 2370 SER A CA    1 
ATOM   7106  C C     . SER A 1 2370 ? 193.389 243.843 195.259 1.00 5.59  ? 2370 SER A C     1 
ATOM   7107  O O     . SER A 1 2370 ? 194.486 244.331 194.981 1.00 3.67  ? 2370 SER A O     1 
ATOM   7108  C CB    . SER A 1 2370 ? 191.906 244.506 197.180 1.00 0.00  ? 2370 SER A CB    1 
ATOM   7109  O OG    . SER A 1 2370 ? 192.257 245.847 196.899 1.00 3.52  ? 2370 SER A OG    1 
ATOM   7110  N N     . THR A 1 2371 ? 192.478 243.535 194.331 1.00 4.11  ? 2371 THR A N     1 
ATOM   7111  C CA    . THR A 1 2371 ? 192.749 243.764 192.915 1.00 5.45  ? 2371 THR A CA    1 
ATOM   7112  C C     . THR A 1 2371 ? 192.906 245.248 192.613 1.00 3.15  ? 2371 THR A C     1 
ATOM   7113  O O     . THR A 1 2371 ? 193.702 245.629 191.746 1.00 5.73  ? 2371 THR A O     1 
ATOM   7114  C CB    . THR A 1 2371 ? 191.631 243.168 192.060 1.00 7.69  ? 2371 THR A CB    1 
ATOM   7115  O OG1   . THR A 1 2371 ? 190.361 243.590 192.571 1.00 16.35 ? 2371 THR A OG1   1 
ATOM   7116  C CG2   . THR A 1 2371 ? 191.696 241.654 192.081 1.00 1.70  ? 2371 THR A CG2   1 
ATOM   7117  N N     . ASP A 1 2372 ? 192.146 246.096 193.309 1.00 1.80  ? 2372 ASP A N     1 
ATOM   7118  C CA    . ASP A 1 2372 ? 192.257 247.536 193.108 1.00 1.67  ? 2372 ASP A CA    1 
ATOM   7119  C C     . ASP A 1 2372 ? 193.662 248.028 193.416 1.00 1.32  ? 2372 ASP A C     1 
ATOM   7120  O O     . ASP A 1 2372 ? 194.194 248.893 192.716 1.00 3.02  ? 2372 ASP A O     1 
ATOM   7121  C CB    . ASP A 1 2372 ? 191.236 248.265 193.979 1.00 6.52  ? 2372 ASP A CB    1 
ATOM   7122  C CG    . ASP A 1 2372 ? 189.813 248.029 193.527 1.00 16.33 ? 2372 ASP A CG    1 
ATOM   7123  O OD1   . ASP A 1 2372 ? 189.602 247.806 192.316 1.00 12.20 ? 2372 ASP A OD1   1 
ATOM   7124  O OD2   . ASP A 1 2372 ? 188.905 248.066 194.382 1.00 15.84 ? 2372 ASP A OD2   1 
ATOM   7125  N N     . MET A 1 2373 ? 194.277 247.484 194.467 1.00 5.39  ? 2373 MET A N     1 
ATOM   7126  C CA    . MET A 1 2373 ? 195.640 247.865 194.818 1.00 5.95  ? 2373 MET A CA    1 
ATOM   7127  C C     . MET A 1 2373 ? 196.616 247.497 193.707 1.00 4.82  ? 2373 MET A C     1 
ATOM   7128  O O     . MET A 1 2373 ? 197.524 248.271 193.380 1.00 2.60  ? 2373 MET A O     1 
ATOM   7129  C CB    . MET A 1 2373 ? 196.026 247.195 196.137 1.00 4.87  ? 2373 MET A CB    1 
ATOM   7130  C CG    . MET A 1 2373 ? 195.098 247.564 197.286 1.00 1.75  ? 2373 MET A CG    1 
ATOM   7131  S SD    . MET A 1 2373 ? 195.413 246.701 198.836 1.00 7.21  ? 2373 MET A SD    1 
ATOM   7132  C CE    . MET A 1 2373 ? 197.112 247.139 199.157 1.00 2.52  ? 2373 MET A CE    1 
ATOM   7133  N N     . ILE A 1 2374 ? 196.431 246.323 193.100 1.00 6.13  ? 2374 ILE A N     1 
ATOM   7134  C CA    . ILE A 1 2374 ? 197.325 245.881 192.033 1.00 1.14  ? 2374 ILE A CA    1 
ATOM   7135  C C     . ILE A 1 2374 ? 197.132 246.739 190.787 1.00 0.60  ? 2374 ILE A C     1 
ATOM   7136  O O     . ILE A 1 2374 ? 198.100 247.109 190.111 1.00 8.56  ? 2374 ILE A O     1 
ATOM   7137  C CB    . ILE A 1 2374 ? 197.104 244.388 191.736 1.00 1.69  ? 2374 ILE A CB    1 
ATOM   7138  C CG1   . ILE A 1 2374 ? 197.866 243.529 192.743 1.00 4.22  ? 2374 ILE A CG1   1 
ATOM   7139  C CG2   . ILE A 1 2374 ? 197.581 244.049 190.342 1.00 5.96  ? 2374 ILE A CG2   1 
ATOM   7140  C CD1   . ILE A 1 2374 ? 197.265 242.160 192.945 1.00 1.24  ? 2374 ILE A CD1   1 
ATOM   7141  N N     . PHE A 1 2375 ? 195.879 247.066 190.460 1.00 1.14  ? 2375 PHE A N     1 
ATOM   7142  C CA    . PHE A 1 2375 ? 195.630 247.960 189.332 1.00 0.00  ? 2375 PHE A CA    1 
ATOM   7143  C C     . PHE A 1 2375 ? 196.241 249.334 189.572 1.00 3.84  ? 2375 PHE A C     1 
ATOM   7144  O O     . PHE A 1 2375 ? 196.806 249.940 188.653 1.00 11.11 ? 2375 PHE A O     1 
ATOM   7145  C CB    . PHE A 1 2375 ? 194.131 248.090 189.061 1.00 0.00  ? 2375 PHE A CB    1 
ATOM   7146  C CG    . PHE A 1 2375 ? 193.459 246.799 188.703 1.00 0.00  ? 2375 PHE A CG    1 
ATOM   7147  C CD1   . PHE A 1 2375 ? 194.131 245.831 187.978 1.00 1.91  ? 2375 PHE A CD1   1 
ATOM   7148  C CD2   . PHE A 1 2375 ? 192.142 246.569 189.056 1.00 3.11  ? 2375 PHE A CD2   1 
ATOM   7149  C CE1   . PHE A 1 2375 ? 193.511 244.649 187.638 1.00 5.88  ? 2375 PHE A CE1   1 
ATOM   7150  C CE2   . PHE A 1 2375 ? 191.515 245.390 188.714 1.00 2.13  ? 2375 PHE A CE2   1 
ATOM   7151  C CZ    . PHE A 1 2375 ? 192.201 244.429 188.004 1.00 7.55  ? 2375 PHE A CZ    1 
ATOM   7152  N N     . ASN A 1 2376 ? 196.126 249.847 190.799 1.00 1.85  ? 2376 ASN A N     1 
ATOM   7153  C CA    . ASN A 1 2376 ? 196.746 251.126 191.124 1.00 0.96  ? 2376 ASN A CA    1 
ATOM   7154  C C     . ASN A 1 2376 ? 198.256 251.057 190.970 1.00 2.40  ? 2376 ASN A C     1 
ATOM   7155  O O     . ASN A 1 2376 ? 198.873 251.993 190.454 1.00 9.74  ? 2376 ASN A O     1 
ATOM   7156  C CB    . ASN A 1 2376 ? 196.369 251.558 192.541 1.00 2.37  ? 2376 ASN A CB    1 
ATOM   7157  C CG    . ASN A 1 2376 ? 194.892 251.861 192.684 1.00 3.55  ? 2376 ASN A CG    1 
ATOM   7158  O OD1   . ASN A 1 2376 ? 194.185 252.039 191.694 1.00 13.00 ? 2376 ASN A OD1   1 
ATOM   7159  N ND2   . ASN A 1 2376 ? 194.419 251.929 193.922 1.00 0.00  ? 2376 ASN A ND2   1 
ATOM   7160  N N     . ASN A 1 2377 ? 198.871 249.957 191.409 1.00 2.27  ? 2377 ASN A N     1 
ATOM   7161  C CA    . ASN A 1 2377 ? 200.311 249.794 191.225 1.00 0.90  ? 2377 ASN A CA    1 
ATOM   7162  C C     . ASN A 1 2377 ? 200.674 249.790 189.746 1.00 8.49  ? 2377 ASN A C     1 
ATOM   7163  O O     . ASN A 1 2377 ? 201.638 250.442 189.328 1.00 10.08 ? 2377 ASN A O     1 
ATOM   7164  C CB    . ASN A 1 2377 ? 200.782 248.504 191.895 1.00 0.00  ? 2377 ASN A CB    1 
ATOM   7165  C CG    . ASN A 1 2377 ? 202.294 248.371 191.921 1.00 0.00  ? 2377 ASN A CG    1 
ATOM   7166  O OD1   . ASN A 1 2377 ? 202.839 247.405 192.447 1.00 5.77  ? 2377 ASN A OD1   1 
ATOM   7167  N ND2   . ASN A 1 2377 ? 202.980 249.355 191.357 1.00 4.86  ? 2377 ASN A ND2   1 
ATOM   7168  N N     . PHE A 1 2378 ? 199.906 249.056 188.938 1.00 4.77  ? 2378 PHE A N     1 
ATOM   7169  C CA    . PHE A 1 2378 ? 200.189 248.980 187.509 1.00 0.00  ? 2378 PHE A CA    1 
ATOM   7170  C C     . PHE A 1 2378 ? 200.101 250.352 186.858 1.00 8.52  ? 2378 PHE A C     1 
ATOM   7171  O O     . PHE A 1 2378 ? 200.987 250.748 186.094 1.00 18.14 ? 2378 PHE A O     1 
ATOM   7172  C CB    . PHE A 1 2378 ? 199.222 248.013 186.829 1.00 3.08  ? 2378 PHE A CB    1 
ATOM   7173  C CG    . PHE A 1 2378 ? 199.224 248.116 185.331 1.00 4.37  ? 2378 PHE A CG    1 
ATOM   7174  C CD1   . PHE A 1 2378 ? 200.359 247.805 184.604 1.00 0.00  ? 2378 PHE A CD1   1 
ATOM   7175  C CD2   . PHE A 1 2378 ? 198.097 248.544 184.652 1.00 1.25  ? 2378 PHE A CD2   1 
ATOM   7176  C CE1   . PHE A 1 2378 ? 200.365 247.905 183.229 1.00 0.00  ? 2378 PHE A CE1   1 
ATOM   7177  C CE2   . PHE A 1 2378 ? 198.100 248.646 183.278 1.00 1.00  ? 2378 PHE A CE2   1 
ATOM   7178  C CZ    . PHE A 1 2378 ? 199.236 248.327 182.567 1.00 0.00  ? 2378 PHE A CZ    1 
ATOM   7179  N N     . LEU A 1 2379 ? 199.036 251.098 187.157 1.00 3.51  ? 2379 LEU A N     1 
ATOM   7180  C CA    . LEU A 1 2379 ? 198.856 252.400 186.527 1.00 2.95  ? 2379 LEU A CA    1 
ATOM   7181  C C     . LEU A 1 2379 ? 199.844 253.434 187.054 1.00 7.45  ? 2379 LEU A C     1 
ATOM   7182  O O     . LEU A 1 2379 ? 200.261 254.322 186.305 1.00 9.84  ? 2379 LEU A O     1 
ATOM   7183  C CB    . LEU A 1 2379 ? 197.417 252.875 186.712 1.00 5.12  ? 2379 LEU A CB    1 
ATOM   7184  C CG    . LEU A 1 2379 ? 196.385 251.910 186.129 1.00 3.86  ? 2379 LEU A CG    1 
ATOM   7185  C CD1   . LEU A 1 2379 ? 195.005 252.160 186.703 1.00 2.09  ? 2379 LEU A CD1   1 
ATOM   7186  C CD2   . LEU A 1 2379 ? 196.361 252.022 184.617 1.00 1.55  ? 2379 LEU A CD2   1 
ATOM   7187  N N     . ALA A 1 2380 ? 200.233 253.340 188.327 1.00 5.17  ? 2380 ALA A N     1 
ATOM   7188  C CA    . ALA A 1 2380 ? 201.218 254.271 188.863 1.00 2.63  ? 2380 ALA A CA    1 
ATOM   7189  C C     . ALA A 1 2380 ? 202.597 254.013 188.273 1.00 5.37  ? 2380 ALA A C     1 
ATOM   7190  O O     . ALA A 1 2380 ? 203.327 254.957 187.952 1.00 15.43 ? 2380 ALA A O     1 
ATOM   7191  C CB    . ALA A 1 2380 ? 201.256 254.173 190.387 1.00 3.16  ? 2380 ALA A CB    1 
ATOM   7192  N N     . ARG A 1 2381 ? 202.976 252.741 188.128 1.00 0.96  ? 2381 ARG A N     1 
ATOM   7193  C CA    . ARG A 1 2381 ? 204.242 252.425 187.478 1.00 4.67  ? 2381 ARG A CA    1 
ATOM   7194  C C     . ARG A 1 2381 ? 204.205 252.797 186.002 1.00 15.06 ? 2381 ARG A C     1 
ATOM   7195  O O     . ARG A 1 2381 ? 205.217 253.228 185.437 1.00 15.25 ? 2381 ARG A O     1 
ATOM   7196  C CB    . ARG A 1 2381 ? 204.560 250.941 187.648 1.00 0.26  ? 2381 ARG A CB    1 
ATOM   7197  C CG    . ARG A 1 2381 ? 205.032 250.557 189.034 1.00 1.84  ? 2381 ARG A CG    1 
ATOM   7198  C CD    . ARG A 1 2381 ? 205.367 249.081 189.103 1.00 4.87  ? 2381 ARG A CD    1 
ATOM   7199  N NE    . ARG A 1 2381 ? 206.489 248.735 188.241 1.00 3.39  ? 2381 ARG A NE    1 
ATOM   7200  C CZ    . ARG A 1 2381 ? 207.754 248.716 188.636 1.00 7.23  ? 2381 ARG A CZ    1 
ATOM   7201  N NH1   . ARG A 1 2381 ? 208.095 249.015 189.879 1.00 7.63  ? 2381 ARG A NH1   1 
ATOM   7202  N NH2   . ARG A 1 2381 ? 208.702 248.387 187.764 1.00 11.88 ? 2381 ARG A NH2   1 
ATOM   7203  N N     . LEU A 1 2382 ? 203.045 252.629 185.365 1.00 11.28 ? 2382 LEU A N     1 
ATOM   7204  C CA    . LEU A 1 2382 ? 202.912 252.932 183.945 1.00 7.10  ? 2382 LEU A CA    1 
ATOM   7205  C C     . LEU A 1 2382 ? 203.116 254.416 183.673 1.00 13.01 ? 2382 LEU A C     1 
ATOM   7206  O O     . LEU A 1 2382 ? 203.786 254.792 182.705 1.00 10.16 ? 2382 LEU A O     1 
ATOM   7207  C CB    . LEU A 1 2382 ? 201.538 252.475 183.452 1.00 1.74  ? 2382 LEU A CB    1 
ATOM   7208  C CG    . LEU A 1 2382 ? 201.217 252.547 181.959 1.00 5.22  ? 2382 LEU A CG    1 
ATOM   7209  C CD1   . LEU A 1 2382 ? 202.168 251.680 181.155 1.00 2.01  ? 2382 LEU A CD1   1 
ATOM   7210  C CD2   . LEU A 1 2382 ? 199.779 252.131 181.717 1.00 2.55  ? 2382 LEU A CD2   1 
ATOM   7211  N N     . ARG A 1 2383 ? 202.552 255.277 184.523 1.00 9.43  ? 2383 ARG A N     1 
ATOM   7212  C CA    . ARG A 1 2383 ? 202.647 256.713 184.299 1.00 9.51  ? 2383 ARG A CA    1 
ATOM   7213  C C     . ARG A 1 2383 ? 204.005 257.281 184.689 1.00 13.37 ? 2383 ARG A C     1 
ATOM   7214  O O     . ARG A 1 2383 ? 204.335 258.395 184.273 1.00 14.40 ? 2383 ARG A O     1 
ATOM   7215  C CB    . ARG A 1 2383 ? 201.552 257.443 185.076 1.00 6.67  ? 2383 ARG A CB    1 
ATOM   7216  C CG    . ARG A 1 2383 ? 200.136 257.112 184.643 1.00 6.95  ? 2383 ARG A CG    1 
ATOM   7217  C CD    . ARG A 1 2383 ? 199.138 257.627 185.668 1.00 11.31 ? 2383 ARG A CD    1 
ATOM   7218  N NE    . ARG A 1 2383 ? 197.821 257.019 185.530 1.00 11.05 ? 2383 ARG A NE    1 
ATOM   7219  C CZ    . ARG A 1 2383 ? 196.807 257.565 184.875 1.00 13.50 ? 2383 ARG A CZ    1 
ATOM   7220  N NH1   . ARG A 1 2383 ? 196.930 258.726 184.254 1.00 10.65 ? 2383 ARG A NH1   1 
ATOM   7221  N NH2   . ARG A 1 2383 ? 195.639 256.930 184.842 1.00 10.74 ? 2383 ARG A NH2   1 
ATOM   7222  N N     . SER A 1 2384 ? 204.797 256.554 185.469 1.00 11.29 ? 2384 SER A N     1 
ATOM   7223  C CA    . SER A 1 2384 ? 206.054 257.084 185.982 1.00 11.99 ? 2384 SER A CA    1 
ATOM   7224  C C     . SER A 1 2384 ? 207.286 256.398 185.417 1.00 13.55 ? 2384 SER A C     1 
ATOM   7225  O O     . SER A 1 2384 ? 208.189 257.079 184.925 1.00 24.19 ? 2384 SER A O     1 
ATOM   7226  C CB    . SER A 1 2384 ? 206.082 256.984 187.511 1.00 9.73  ? 2384 SER A CB    1 
ATOM   7227  O OG    . SER A 1 2384 ? 205.857 255.652 187.933 1.00 15.76 ? 2384 SER A OG    1 
ATOM   7228  N N     . ILE A 1 2385 ? 207.359 255.073 185.479 1.00 7.38  ? 2385 ILE A N     1 
ATOM   7229  C CA    . ILE A 1 2385 ? 208.549 254.354 185.029 1.00 16.52 ? 2385 ILE A CA    1 
ATOM   7230  C C     . ILE A 1 2385 ? 208.545 254.279 183.507 1.00 19.78 ? 2385 ILE A C     1 
ATOM   7231  O O     . ILE A 1 2385 ? 207.568 253.801 182.913 1.00 19.19 ? 2385 ILE A O     1 
ATOM   7232  C CB    . ILE A 1 2385 ? 208.624 252.951 185.650 1.00 18.42 ? 2385 ILE A CB    1 
ATOM   7233  C CG1   . ILE A 1 2385 ? 208.913 253.046 187.149 1.00 16.31 ? 2385 ILE A CG1   1 
ATOM   7234  C CG2   . ILE A 1 2385 ? 209.689 252.118 184.954 1.00 13.08 ? 2385 ILE A CG2   1 
ATOM   7235  C CD1   . ILE A 1 2385 ? 210.363 253.326 187.475 1.00 14.32 ? 2385 ILE A CD1   1 
ATOM   7236  N N     . PRO A 1 2386 ? 209.601 254.743 182.837 1.00 22.18 ? 2386 PRO A N     1 
ATOM   7237  C CA    . PRO A 1 2386 ? 209.647 254.643 181.372 1.00 18.16 ? 2386 PRO A CA    1 
ATOM   7238  C C     . PRO A 1 2386 ? 209.890 253.208 180.931 1.00 15.22 ? 2386 PRO A C     1 
ATOM   7239  O O     . PRO A 1 2386 ? 210.735 252.507 181.490 1.00 20.89 ? 2386 PRO A O     1 
ATOM   7240  C CB    . PRO A 1 2386 ? 210.816 255.559 180.985 1.00 16.46 ? 2386 PRO A CB    1 
ATOM   7241  C CG    . PRO A 1 2386 ? 211.204 256.289 182.247 1.00 14.08 ? 2386 PRO A CG    1 
ATOM   7242  C CD    . PRO A 1 2386 ? 210.793 255.412 183.377 1.00 16.74 ? 2386 PRO A CD    1 
ATOM   7243  N N     . LEU A 1 2387 ? 209.132 252.772 179.922 1.00 11.70 ? 2387 LEU A N     1 
ATOM   7244  C CA    . LEU A 1 2387 ? 209.351 251.442 179.364 1.00 19.34 ? 2387 LEU A CA    1 
ATOM   7245  C C     . LEU A 1 2387 ? 210.716 251.351 178.695 1.00 19.16 ? 2387 LEU A C     1 
ATOM   7246  O O     . LEU A 1 2387 ? 211.396 250.322 178.788 1.00 17.48 ? 2387 LEU A O     1 
ATOM   7247  C CB    . LEU A 1 2387 ? 208.236 251.096 178.380 1.00 16.14 ? 2387 LEU A CB    1 
ATOM   7248  C CG    . LEU A 1 2387 ? 206.910 250.689 179.028 1.00 12.43 ? 2387 LEU A CG    1 
ATOM   7249  C CD1   . LEU A 1 2387 ? 205.800 250.608 177.996 1.00 11.93 ? 2387 LEU A CD1   1 
ATOM   7250  C CD2   . LEU A 1 2387 ? 207.056 249.374 179.774 1.00 10.38 ? 2387 LEU A CD2   1 
ATOM   7251  N N     . ASP A 1 2388 ? 211.132 252.417 178.017 1.00 22.92 ? 2388 ASP A N     1 
ATOM   7252  C CA    . ASP A 1 2388 ? 212.471 252.501 177.440 1.00 22.94 ? 2388 ASP A CA    1 
ATOM   7253  C C     . ASP A 1 2388 ? 213.406 253.074 178.496 1.00 23.58 ? 2388 ASP A C     1 
ATOM   7254  O O     . ASP A 1 2388 ? 213.315 254.250 178.854 1.00 23.06 ? 2388 ASP A O     1 
ATOM   7255  C CB    . ASP A 1 2388 ? 212.462 253.358 176.180 1.00 20.47 ? 2388 ASP A CB    1 
ATOM   7256  N N     . ASP A 1 2389 ? 214.308 252.241 179.005 1.00 30.27 ? 2389 ASP A N     1 
ATOM   7257  C CA    . ASP A 1 2389 ? 215.250 252.667 180.033 1.00 29.72 ? 2389 ASP A CA    1 
ATOM   7258  C C     . ASP A 1 2389 ? 216.344 253.552 179.448 1.00 31.66 ? 2389 ASP A C     1 
ATOM   7259  O O     . ASP A 1 2389 ? 216.964 254.345 180.157 0.00 30.14 ? 2389 ASP A O     1 
ATOM   7260  C CB    . ASP A 1 2389 ? 215.873 251.454 180.725 1.00 31.68 ? 2389 ASP A CB    1 
ATOM   7261  C CG    . ASP A 1 2389 ? 214.834 250.519 181.309 1.00 34.11 ? 2389 ASP A CG    1 
ATOM   7262  O OD1   . ASP A 1 2389 ? 213.639 250.883 181.309 1.00 34.02 ? 2389 ASP A OD1   1 
ATOM   7263  O OD2   . ASP A 1 2389 ? 215.211 249.421 181.768 1.00 34.32 ? 2389 ASP A OD2   1 
ATOM   7264  N N     . SER A 1 2410 ? 211.355 260.289 177.014 1.00 27.84 ? 2410 SER A N     1 
ATOM   7265  C CA    . SER A 1 2410 ? 210.373 261.311 177.363 1.00 29.98 ? 2410 SER A CA    1 
ATOM   7266  C C     . SER A 1 2410 ? 209.037 261.146 176.615 1.00 28.65 ? 2410 SER A C     1 
ATOM   7267  O O     . SER A 1 2410 ? 207.982 261.203 177.247 1.00 30.64 ? 2410 SER A O     1 
ATOM   7268  C CB    . SER A 1 2410 ? 210.952 262.712 177.123 1.00 31.85 ? 2410 SER A CB    1 
ATOM   7269  O OG    . SER A 1 2410 ? 209.989 263.716 177.387 1.00 29.58 ? 2410 SER A OG    1 
ATOM   7270  N N     . PRO A 1 2411 ? 209.055 260.961 175.286 1.00 25.30 ? 2411 PRO A N     1 
ATOM   7271  C CA    . PRO A 1 2411 ? 207.787 260.656 174.600 1.00 25.60 ? 2411 PRO A CA    1 
ATOM   7272  C C     . PRO A 1 2411 ? 207.183 259.331 175.029 1.00 31.04 ? 2411 PRO A C     1 
ATOM   7273  O O     . PRO A 1 2411 ? 205.954 259.175 174.994 1.00 28.31 ? 2411 PRO A O     1 
ATOM   7274  C CB    . PRO A 1 2411 ? 208.173 260.649 173.113 1.00 25.63 ? 2411 PRO A CB    1 
ATOM   7275  C CG    . PRO A 1 2411 ? 209.499 261.313 173.039 1.00 27.33 ? 2411 PRO A CG    1 
ATOM   7276  C CD    . PRO A 1 2411 ? 210.175 261.018 174.328 1.00 26.48 ? 2411 PRO A CD    1 
ATOM   7277  N N     . MET A 1 2412 ? 208.018 258.367 175.426 1.00 30.09 ? 2412 MET A N     1 
ATOM   7278  C CA    . MET A 1 2412 ? 207.501 257.099 175.928 1.00 22.39 ? 2412 MET A CA    1 
ATOM   7279  C C     . MET A 1 2412 ? 206.657 257.311 177.176 1.00 22.42 ? 2412 MET A C     1 
ATOM   7280  O O     . MET A 1 2412 ? 205.581 256.720 177.315 1.00 24.24 ? 2412 MET A O     1 
ATOM   7281  C CB    . MET A 1 2412 ? 208.652 256.135 176.211 1.00 20.21 ? 2412 MET A CB    1 
ATOM   7282  N N     . LEU A 1 2413 ? 207.119 258.168 178.089 1.00 19.37 ? 2413 LEU A N     1 
ATOM   7283  C CA    . LEU A 1 2413 ? 206.307 258.502 179.254 1.00 19.09 ? 2413 LEU A CA    1 
ATOM   7284  C C     . LEU A 1 2413 ? 204.993 259.151 178.848 1.00 19.61 ? 2413 LEU A C     1 
ATOM   7285  O O     . LEU A 1 2413 ? 203.945 258.844 179.421 1.00 21.28 ? 2413 LEU A O     1 
ATOM   7286  C CB    . LEU A 1 2413 ? 207.081 259.418 180.200 1.00 22.18 ? 2413 LEU A CB    1 
ATOM   7287  C CG    . LEU A 1 2413 ? 208.301 258.794 180.865 1.00 26.65 ? 2413 LEU A CG    1 
ATOM   7288  C CD1   . LEU A 1 2413 ? 209.072 259.829 181.668 1.00 26.95 ? 2413 LEU A CD1   1 
ATOM   7289  C CD2   . LEU A 1 2413 ? 207.826 257.669 181.759 1.00 17.04 ? 2413 LEU A CD2   1 
ATOM   7290  N N     . GLN A 1 2414 ? 205.028 260.062 177.876 1.00 21.23 ? 2414 GLN A N     1 
ATOM   7291  C CA    . GLN A 1 2414 ? 203.808 260.761 177.482 1.00 21.75 ? 2414 GLN A CA    1 
ATOM   7292  C C     . GLN A 1 2414 ? 202.783 259.790 176.909 1.00 19.37 ? 2414 GLN A C     1 
ATOM   7293  O O     . GLN A 1 2414 ? 201.593 259.846 177.251 1.00 20.16 ? 2414 GLN A O     1 
ATOM   7294  C CB    . GLN A 1 2414 ? 204.141 261.864 176.477 1.00 23.90 ? 2414 GLN A CB    1 
ATOM   7295  C CG    . GLN A 1 2414 ? 203.255 263.093 176.594 1.00 21.10 ? 2414 GLN A CG    1 
ATOM   7296  C CD    . GLN A 1 2414 ? 201.882 262.883 175.991 1.00 21.08 ? 2414 GLN A CD    1 
ATOM   7297  O OE1   . GLN A 1 2414 ? 201.754 262.437 174.852 1.00 21.99 ? 2414 GLN A OE1   1 
ATOM   7298  N NE2   . GLN A 1 2414 ? 200.844 263.201 176.756 1.00 19.14 ? 2414 GLN A NE2   1 
ATOM   7299  N N     . ILE A 1 2415 ? 203.230 258.874 176.046 1.00 18.35 ? 2415 ILE A N     1 
ATOM   7300  C CA    . ILE A 1 2415 ? 202.292 257.908 175.485 1.00 20.90 ? 2415 ILE A CA    1 
ATOM   7301  C C     . ILE A 1 2415 ? 201.831 256.922 176.552 1.00 17.75 ? 2415 ILE A C     1 
ATOM   7302  O O     . ILE A 1 2415 ? 200.692 256.445 176.509 1.00 15.94 ? 2415 ILE A O     1 
ATOM   7303  C CB    . ILE A 1 2415 ? 202.896 257.192 174.260 1.00 20.23 ? 2415 ILE A CB    1 
ATOM   7304  C CG1   . ILE A 1 2415 ? 204.141 256.396 174.640 1.00 19.29 ? 2415 ILE A CG1   1 
ATOM   7305  C CG2   . ILE A 1 2415 ? 203.224 258.195 173.166 1.00 19.69 ? 2415 ILE A CG2   1 
ATOM   7306  C CD1   . ILE A 1 2415 ? 204.641 255.494 173.539 1.00 19.35 ? 2415 ILE A CD1   1 
ATOM   7307  N N     . GLN A 1 2416 ? 202.684 256.615 177.536 1.00 18.44 ? 2416 GLN A N     1 
ATOM   7308  C CA    . GLN A 1 2416 ? 202.258 255.757 178.639 1.00 14.99 ? 2416 GLN A CA    1 
ATOM   7309  C C     . GLN A 1 2416 ? 201.164 256.417 179.471 1.00 17.44 ? 2416 GLN A C     1 
ATOM   7310  O O     . GLN A 1 2416 ? 200.192 255.762 179.861 1.00 16.56 ? 2416 GLN A O     1 
ATOM   7311  C CB    . GLN A 1 2416 ? 203.454 255.406 179.522 1.00 10.15 ? 2416 GLN A CB    1 
ATOM   7312  C CG    . GLN A 1 2416 ? 204.339 254.310 178.970 1.00 10.03 ? 2416 GLN A CG    1 
ATOM   7313  C CD    . GLN A 1 2416 ? 205.589 254.112 179.798 1.00 11.54 ? 2416 GLN A CD    1 
ATOM   7314  O OE1   . GLN A 1 2416 ? 206.686 253.967 179.263 1.00 13.84 ? 2416 GLN A OE1   1 
ATOM   7315  N NE2   . GLN A 1 2416 ? 205.429 254.107 181.115 1.00 15.36 ? 2416 GLN A NE2   1 
ATOM   7316  N N     . ARG A 1 2417 ? 201.316 257.710 179.772 1.00 14.23 ? 2417 ARG A N     1 
ATOM   7317  C CA    . ARG A 1 2417 ? 200.282 258.418 180.521 1.00 11.44 ? 2417 ARG A CA    1 
ATOM   7318  C C     . ARG A 1 2417 ? 198.992 258.512 179.719 1.00 11.16 ? 2417 ARG A C     1 
ATOM   7319  O O     . ARG A 1 2417 ? 197.896 258.381 180.276 1.00 15.84 ? 2417 ARG A O     1 
ATOM   7320  C CB    . ARG A 1 2417 ? 200.760 259.813 180.929 1.00 12.44 ? 2417 ARG A CB    1 
ATOM   7321  C CG    . ARG A 1 2417 ? 202.147 259.865 181.537 1.00 10.63 ? 2417 ARG A CG    1 
ATOM   7322  C CD    . ARG A 1 2417 ? 202.439 261.228 182.140 1.00 15.34 ? 2417 ARG A CD    1 
ATOM   7323  N NE    . ARG A 1 2417 ? 203.784 261.300 182.697 1.00 18.06 ? 2417 ARG A NE    1 
ATOM   7324  C CZ    . ARG A 1 2417 ? 204.059 261.360 183.992 1.00 18.19 ? 2417 ARG A CZ    1 
ATOM   7325  N NH1   . ARG A 1 2417 ? 203.100 261.357 184.903 1.00 16.30 ? 2417 ARG A NH1   1 
ATOM   7326  N NH2   . ARG A 1 2417 ? 205.329 261.419 184.383 1.00 19.96 ? 2417 ARG A NH2   1 
ATOM   7327  N N     . ASP A 1 2418 ? 199.099 258.744 178.408 1.00 12.08 ? 2418 ASP A N     1 
ATOM   7328  C CA    . ASP A 1 2418 ? 197.901 258.743 177.574 1.00 15.77 ? 2418 ASP A CA    1 
ATOM   7329  C C     . ASP A 1 2418 ? 197.214 257.383 177.597 1.00 15.14 ? 2418 ASP A C     1 
ATOM   7330  O O     . ASP A 1 2418 ? 195.985 257.299 177.718 1.00 14.93 ? 2418 ASP A O     1 
ATOM   7331  C CB    . ASP A 1 2418 ? 198.257 259.138 176.142 1.00 15.59 ? 2418 ASP A CB    1 
ATOM   7332  C CG    . ASP A 1 2418 ? 198.672 260.588 176.024 1.00 19.96 ? 2418 ASP A CG    1 
ATOM   7333  O OD1   . ASP A 1 2418 ? 198.194 261.413 176.830 1.00 22.01 ? 2418 ASP A OD1   1 
ATOM   7334  O OD2   . ASP A 1 2418 ? 199.475 260.902 175.123 1.00 17.50 ? 2418 ASP A OD2   1 
ATOM   7335  N N     . ALA A 1 2419 ? 197.995 256.305 177.487 1.00 14.19 ? 2419 ALA A N     1 
ATOM   7336  C CA    . ALA A 1 2419 ? 197.435 254.960 177.544 1.00 11.81 ? 2419 ALA A CA    1 
ATOM   7337  C C     . ALA A 1 2419 ? 196.749 254.704 178.876 1.00 12.59 ? 2419 ALA A C     1 
ATOM   7338  O O     . ALA A 1 2419 ? 195.644 254.153 178.917 1.00 12.96 ? 2419 ALA A O     1 
ATOM   7339  C CB    . ALA A 1 2419 ? 198.534 253.927 177.305 1.00 7.76  ? 2419 ALA A CB    1 
ATOM   7340  N N     . ALA A 1 2420 ? 197.394 255.093 179.977 1.00 14.01 ? 2420 ALA A N     1 
ATOM   7341  C CA    . ALA A 1 2420 ? 196.802 254.899 181.295 1.00 7.48  ? 2420 ALA A CA    1 
ATOM   7342  C C     . ALA A 1 2420 ? 195.502 255.678 181.436 1.00 6.56  ? 2420 ALA A C     1 
ATOM   7343  O O     . ALA A 1 2420 ? 194.521 255.165 181.986 1.00 11.13 ? 2420 ALA A O     1 
ATOM   7344  C CB    . ALA A 1 2420 ? 197.794 255.311 182.379 1.00 9.27  ? 2420 ALA A CB    1 
ATOM   7345  N N     . THR A 1 2421 ? 195.473 256.917 180.939 1.00 11.34 ? 2421 THR A N     1 
ATOM   7346  C CA    . THR A 1 2421 ? 194.248 257.707 180.997 1.00 12.29 ? 2421 THR A CA    1 
ATOM   7347  C C     . THR A 1 2421 ? 193.135 257.055 180.186 1.00 11.06 ? 2421 THR A C     1 
ATOM   7348  O O     . THR A 1 2421 ? 191.978 257.023 180.621 1.00 7.88  ? 2421 THR A O     1 
ATOM   7349  C CB    . THR A 1 2421 ? 194.510 259.126 180.495 1.00 16.45 ? 2421 THR A CB    1 
ATOM   7350  O OG1   . THR A 1 2421 ? 195.711 259.632 181.091 1.00 18.12 ? 2421 THR A OG1   1 
ATOM   7351  C CG2   . THR A 1 2421 ? 193.349 260.038 180.856 1.00 14.02 ? 2421 THR A CG2   1 
ATOM   7352  N N     . ILE A 1 2422 ? 193.465 256.533 179.004 1.00 11.72 ? 2422 ILE A N     1 
ATOM   7353  C CA    . ILE A 1 2422 ? 192.461 255.869 178.175 1.00 11.63 ? 2422 ILE A CA    1 
ATOM   7354  C C     . ILE A 1 2422 ? 191.938 254.616 178.868 1.00 13.37 ? 2422 ILE A C     1 
ATOM   7355  O O     . ILE A 1 2422 ? 190.737 254.327 178.846 1.00 13.59 ? 2422 ILE A O     1 
ATOM   7356  C CB    . ILE A 1 2422 ? 193.040 255.543 176.785 1.00 10.01 ? 2422 ILE A CB    1 
ATOM   7357  C CG1   . ILE A 1 2422 ? 193.350 256.828 176.017 1.00 13.90 ? 2422 ILE A CG1   1 
ATOM   7358  C CG2   . ILE A 1 2422 ? 192.081 254.669 175.992 1.00 12.15 ? 2422 ILE A CG2   1 
ATOM   7359  C CD1   . ILE A 1 2422 ? 194.464 256.678 175.009 1.00 12.42 ? 2422 ILE A CD1   1 
ATOM   7360  N N     . MET A 1 2423 ? 192.832 253.859 179.491 1.00 14.76 ? 2423 MET A N     1 
ATOM   7361  C CA    . MET A 1 2423 ? 192.518 252.556 180.059 1.00 9.51  ? 2423 MET A CA    1 
ATOM   7362  C C     . MET A 1 2423 ? 192.219 252.605 181.553 1.00 6.20  ? 2423 MET A C     1 
ATOM   7363  O O     . MET A 1 2423 ? 191.995 251.554 182.161 1.00 3.77  ? 2423 MET A O     1 
ATOM   7364  C CB    . MET A 1 2423 ? 193.682 251.608 179.769 1.00 8.43  ? 2423 MET A CB    1 
ATOM   7365  C CG    . MET A 1 2423 ? 194.854 251.736 180.715 1.00 11.81 ? 2423 MET A CG    1 
ATOM   7366  S SD    . MET A 1 2423 ? 196.282 250.925 179.990 1.00 7.73  ? 2423 MET A SD    1 
ATOM   7367  C CE    . MET A 1 2423 ? 195.637 249.274 179.903 1.00 6.95  ? 2423 MET A CE    1 
ATOM   7368  N N     . GLN A 1 2424 ? 192.196 253.797 182.148 1.00 11.31 ? 2424 GLN A N     1 
ATOM   7369  C CA    . GLN A 1 2424 ? 191.835 253.926 183.558 1.00 11.72 ? 2424 GLN A CA    1 
ATOM   7370  C C     . GLN A 1 2424 ? 190.415 253.471 183.887 1.00 8.86  ? 2424 GLN A C     1 
ATOM   7371  O O     . GLN A 1 2424 ? 190.251 252.759 184.893 1.00 7.57  ? 2424 GLN A O     1 
ATOM   7372  C CB    . GLN A 1 2424 ? 192.054 255.377 184.008 1.00 10.88 ? 2424 GLN A CB    1 
ATOM   7373  C CG    . GLN A 1 2424 ? 191.707 255.658 185.463 1.00 4.76  ? 2424 GLN A CG    1 
ATOM   7374  C CD    . GLN A 1 2424 ? 192.882 255.455 186.396 1.00 7.42  ? 2424 GLN A CD    1 
ATOM   7375  O OE1   . GLN A 1 2424 ? 193.870 256.186 186.337 1.00 9.77  ? 2424 GLN A OE1   1 
ATOM   7376  N NE2   . GLN A 1 2424 ? 192.770 254.472 187.280 1.00 11.31 ? 2424 GLN A NE2   1 
ATOM   7377  N N     . PRO A 1 2425 ? 189.365 253.837 183.138 1.00 5.90  ? 2425 PRO A N     1 
ATOM   7378  C CA    . PRO A 1 2425 ? 188.008 253.458 183.573 1.00 10.42 ? 2425 PRO A CA    1 
ATOM   7379  C C     . PRO A 1 2425 ? 187.768 251.961 183.632 1.00 7.19  ? 2425 PRO A C     1 
ATOM   7380  O O     . PRO A 1 2425 ? 186.841 251.521 184.322 1.00 7.63  ? 2425 PRO A O     1 
ATOM   7381  C CB    . PRO A 1 2425 ? 187.104 254.133 182.532 1.00 12.98 ? 2425 PRO A CB    1 
ATOM   7382  C CG    . PRO A 1 2425 ? 187.955 254.297 181.339 1.00 12.21 ? 2425 PRO A CG    1 
ATOM   7383  C CD    . PRO A 1 2425 ? 189.332 254.572 181.860 1.00 5.85  ? 2425 PRO A CD    1 
ATOM   7384  N N     . TYR A 1 2426 ? 188.562 251.161 182.922 1.00 11.32 ? 2426 TYR A N     1 
ATOM   7385  C CA    . TYR A 1 2426 ? 188.435 249.712 183.028 1.00 11.71 ? 2426 TYR A CA    1 
ATOM   7386  C C     . TYR A 1 2426 ? 189.187 249.155 184.230 1.00 12.87 ? 2426 TYR A C     1 
ATOM   7387  O O     . TYR A 1 2426 ? 188.764 248.145 184.804 1.00 12.43 ? 2426 TYR A O     1 
ATOM   7388  C CB    . TYR A 1 2426 ? 188.923 249.049 181.740 1.00 9.22  ? 2426 TYR A CB    1 
ATOM   7389  C CG    . TYR A 1 2426 ? 188.399 249.705 180.480 1.00 11.12 ? 2426 TYR A CG    1 
ATOM   7390  C CD1   . TYR A 1 2426 ? 187.123 249.425 180.009 1.00 11.27 ? 2426 TYR A CD1   1 
ATOM   7391  C CD2   . TYR A 1 2426 ? 189.175 250.612 179.769 1.00 8.51  ? 2426 TYR A CD2   1 
ATOM   7392  C CE1   . TYR A 1 2426 ? 186.638 250.020 178.863 1.00 7.78  ? 2426 TYR A CE1   1 
ATOM   7393  C CE2   . TYR A 1 2426 ? 188.696 251.212 178.621 1.00 9.53  ? 2426 TYR A CE2   1 
ATOM   7394  C CZ    . TYR A 1 2426 ? 187.428 250.913 178.175 1.00 11.49 ? 2426 TYR A CZ    1 
ATOM   7395  O OH    . TYR A 1 2426 ? 186.945 251.509 177.033 1.00 13.90 ? 2426 TYR A OH    1 
ATOM   7396  N N     . PHE A 1 2427 ? 190.289 249.791 184.625 1.00 12.11 ? 2427 PHE A N     1 
ATOM   7397  C CA    . PHE A 1 2427 ? 191.075 249.359 185.781 1.00 5.52  ? 2427 PHE A CA    1 
ATOM   7398  C C     . PHE A 1 2427 ? 190.600 250.065 187.053 1.00 8.86  ? 2427 PHE A C     1 
ATOM   7399  O O     . PHE A 1 2427 ? 191.350 250.760 187.737 1.00 13.78 ? 2427 PHE A O     1 
ATOM   7400  C CB    . PHE A 1 2427 ? 192.557 249.617 185.537 1.00 6.62  ? 2427 PHE A CB    1 
ATOM   7401  C CG    . PHE A 1 2427 ? 193.245 248.539 184.753 1.00 6.88  ? 2427 PHE A CG    1 
ATOM   7402  C CD1   . PHE A 1 2427 ? 193.088 247.209 185.097 1.00 12.07 ? 2427 PHE A CD1   1 
ATOM   7403  C CD2   . PHE A 1 2427 ? 194.065 248.857 183.685 1.00 6.00  ? 2427 PHE A CD2   1 
ATOM   7404  C CE1   . PHE A 1 2427 ? 193.730 246.217 184.387 1.00 11.73 ? 2427 PHE A CE1   1 
ATOM   7405  C CE2   . PHE A 1 2427 ? 194.708 247.869 182.970 1.00 0.86  ? 2427 PHE A CE2   1 
ATOM   7406  C CZ    . PHE A 1 2427 ? 194.539 246.548 183.320 1.00 3.75  ? 2427 PHE A CZ    1 
ATOM   7407  N N     . THR A 1 2428 ? 189.322 249.872 187.366 1.00 8.71  ? 2428 THR A N     1 
ATOM   7408  C CA    . THR A 1 2428 ? 188.712 250.433 188.564 1.00 13.64 ? 2428 THR A CA    1 
ATOM   7409  C C     . THR A 1 2428 ? 188.030 249.315 189.340 1.00 16.28 ? 2428 THR A C     1 
ATOM   7410  O O     . THR A 1 2428 ? 188.093 248.142 188.963 1.00 19.05 ? 2428 THR A O     1 
ATOM   7411  C CB    . THR A 1 2428 ? 187.709 251.541 188.219 1.00 13.25 ? 2428 THR A CB    1 
ATOM   7412  O OG1   . THR A 1 2428 ? 186.695 251.020 187.351 1.00 11.76 ? 2428 THR A OG1   1 
ATOM   7413  C CG2   . THR A 1 2428 ? 188.411 252.707 187.541 1.00 12.04 ? 2428 THR A CG2   1 
ATOM   7414  N N     . SER A 1 2429 ? 187.383 249.682 190.445 1.00 22.41 ? 2429 SER A N     1 
ATOM   7415  C CA    . SER A 1 2429 ? 186.565 248.721 191.170 1.00 19.91 ? 2429 SER A CA    1 
ATOM   7416  C C     . SER A 1 2429 ? 185.444 248.226 190.267 1.00 18.42 ? 2429 SER A C     1 
ATOM   7417  O O     . SER A 1 2429 ? 184.791 249.014 189.576 1.00 21.52 ? 2429 SER A O     1 
ATOM   7418  C CB    . SER A 1 2429 ? 185.990 249.353 192.438 1.00 19.59 ? 2429 SER A CB    1 
ATOM   7419  O OG    . SER A 1 2429 ? 185.263 250.533 192.139 1.00 25.79 ? 2429 SER A OG    1 
ATOM   7420  N N     . ASN A 1 2430 ? 185.230 246.915 190.273 1.00 15.96 ? 2430 ASN A N     1 
ATOM   7421  C CA    . ASN A 1 2430 ? 184.335 246.260 189.311 1.00 21.09 ? 2430 ASN A CA    1 
ATOM   7422  C C     . ASN A 1 2430 ? 184.852 246.599 187.909 1.00 23.98 ? 2430 ASN A C     1 
ATOM   7423  O O     . ASN A 1 2430 ? 186.065 246.705 187.690 1.00 22.62 ? 2430 ASN A O     1 
ATOM   7424  C CB    . ASN A 1 2430 ? 182.890 246.651 189.574 1.00 23.04 ? 2430 ASN A CB    1 
ATOM   7425  C CG    . ASN A 1 2430 ? 182.403 246.196 190.934 1.00 25.06 ? 2430 ASN A CG    1 
ATOM   7426  O OD1   . ASN A 1 2430 ? 183.065 245.410 191.612 1.00 25.69 ? 2430 ASN A OD1   1 
ATOM   7427  N ND2   . ASN A 1 2430 ? 181.240 246.691 191.343 1.00 24.51 ? 2430 ASN A ND2   1 
ATOM   7428  N N     . GLY A 1 2431 ? 183.957 246.783 186.951 1.00 22.71 ? 2431 GLY A N     1 
ATOM   7429  C CA    . GLY A 1 2431 ? 184.382 247.133 185.616 1.00 18.05 ? 2431 GLY A CA    1 
ATOM   7430  C C     . GLY A 1 2431 ? 184.869 245.937 184.820 1.00 17.14 ? 2431 GLY A C     1 
ATOM   7431  O O     . GLY A 1 2431 ? 184.757 244.775 185.227 1.00 16.39 ? 2431 GLY A O     1 
ATOM   7432  N N     . LEU A 1 2432 ? 185.442 246.250 183.655 1.00 16.67 ? 2432 LEU A N     1 
ATOM   7433  C CA    . LEU A 1 2432 ? 185.753 245.222 182.668 1.00 16.87 ? 2432 LEU A CA    1 
ATOM   7434  C C     . LEU A 1 2432 ? 186.744 244.200 183.208 1.00 12.65 ? 2432 LEU A C     1 
ATOM   7435  O O     . LEU A 1 2432 ? 186.487 242.993 183.168 1.00 11.02 ? 2432 LEU A O     1 
ATOM   7436  C CB    . LEU A 1 2432 ? 186.302 245.870 181.397 1.00 18.03 ? 2432 LEU A CB    1 
ATOM   7437  C CG    . LEU A 1 2432 ? 186.617 244.911 180.248 1.00 15.70 ? 2432 LEU A CG    1 
ATOM   7438  C CD1   . LEU A 1 2432 ? 185.353 244.216 179.767 1.00 15.62 ? 2432 LEU A CD1   1 
ATOM   7439  C CD2   . LEU A 1 2432 ? 187.316 245.636 179.108 1.00 12.77 ? 2432 LEU A CD2   1 
ATOM   7440  N N     . VAL A 1 2433 ? 187.883 244.664 183.723 1.00 15.66 ? 2433 VAL A N     1 
ATOM   7441  C CA    . VAL A 1 2433 ? 188.949 243.742 184.105 1.00 10.91 ? 2433 VAL A CA    1 
ATOM   7442  C C     . VAL A 1 2433 ? 188.538 242.914 185.314 1.00 12.86 ? 2433 VAL A C     1 
ATOM   7443  O O     . VAL A 1 2433 ? 188.784 241.705 185.366 1.00 17.87 ? 2433 VAL A O     1 
ATOM   7444  C CB    . VAL A 1 2433 ? 190.258 244.505 184.361 1.00 5.71  ? 2433 VAL A CB    1 
ATOM   7445  C CG1   . VAL A 1 2433 ? 191.415 243.530 184.456 1.00 2.43  ? 2433 VAL A CG1   1 
ATOM   7446  C CG2   . VAL A 1 2433 ? 190.501 245.506 183.251 1.00 6.81  ? 2433 VAL A CG2   1 
ATOM   7447  N N     . THR A 1 2434 ? 187.912 243.548 186.307 1.00 11.94 ? 2434 THR A N     1 
ATOM   7448  C CA    . THR A 1 2434 ? 187.486 242.810 187.493 1.00 12.84 ? 2434 THR A CA    1 
ATOM   7449  C C     . THR A 1 2434 ? 186.423 241.772 187.152 1.00 16.32 ? 2434 THR A C     1 
ATOM   7450  O O     . THR A 1 2434 ? 186.505 240.622 187.603 1.00 15.92 ? 2434 THR A O     1 
ATOM   7451  C CB    . THR A 1 2434 ? 186.968 243.775 188.557 1.00 16.07 ? 2434 THR A CB    1 
ATOM   7452  O OG1   . THR A 1 2434 ? 188.012 244.685 188.926 1.00 18.51 ? 2434 THR A OG1   1 
ATOM   7453  C CG2   . THR A 1 2434 ? 186.503 243.016 189.787 1.00 17.27 ? 2434 THR A CG2   1 
ATOM   7454  N N     . LYS A 1 2435 ? 185.421 242.154 186.355 1.00 16.71 ? 2435 LYS A N     1 
ATOM   7455  C CA    . LYS A 1 2435 ? 184.387 241.200 185.970 1.00 11.39 ? 2435 LYS A CA    1 
ATOM   7456  C C     . LYS A 1 2435 ? 184.969 240.062 185.142 1.00 11.64 ? 2435 LYS A C     1 
ATOM   7457  O O     . LYS A 1 2435 ? 184.612 238.894 185.341 1.00 17.72 ? 2435 LYS A O     1 
ATOM   7458  C CB    . LYS A 1 2435 ? 183.275 241.915 185.203 1.00 15.85 ? 2435 LYS A CB    1 
ATOM   7459  C CG    . LYS A 1 2435 ? 182.450 242.866 186.054 1.00 17.71 ? 2435 LYS A CG    1 
ATOM   7460  C CD    . LYS A 1 2435 ? 181.296 243.458 185.267 1.00 19.00 ? 2435 LYS A CD    1 
ATOM   7461  C CE    . LYS A 1 2435 ? 180.059 243.618 186.134 1.00 21.35 ? 2435 LYS A CE    1 
ATOM   7462  N NZ    . LYS A 1 2435 ? 178.987 244.378 185.433 1.00 20.68 ? 2435 LYS A NZ    1 
ATOM   7463  N N     . ALA A 1 2436 ? 185.879 240.381 184.218 1.00 12.35 ? 2436 ALA A N     1 
ATOM   7464  C CA    . ALA A 1 2436 ? 186.497 239.352 183.392 1.00 10.98 ? 2436 ALA A CA    1 
ATOM   7465  C C     . ALA A 1 2436 ? 187.331 238.395 184.231 1.00 13.65 ? 2436 ALA A C     1 
ATOM   7466  O O     . ALA A 1 2436 ? 187.311 237.183 184.000 1.00 18.19 ? 2436 ALA A O     1 
ATOM   7467  C CB    . ALA A 1 2436 ? 187.353 239.998 182.305 1.00 10.23 ? 2436 ALA A CB    1 
ATOM   7468  N N     . LEU A 1 2437 ? 188.077 238.920 185.204 1.00 13.22 ? 2437 LEU A N     1 
ATOM   7469  C CA    . LEU A 1 2437 ? 188.893 238.061 186.055 1.00 8.66  ? 2437 LEU A CA    1 
ATOM   7470  C C     . LEU A 1 2437 ? 188.019 237.171 186.930 1.00 13.14 ? 2437 LEU A C     1 
ATOM   7471  O O     . LEU A 1 2437 ? 188.303 235.977 187.099 1.00 17.84 ? 2437 LEU A O     1 
ATOM   7472  C CB    . LEU A 1 2437 ? 189.833 238.920 186.900 1.00 8.20  ? 2437 LEU A CB    1 
ATOM   7473  C CG    . LEU A 1 2437 ? 190.841 238.224 187.811 1.00 12.45 ? 2437 LEU A CG    1 
ATOM   7474  C CD1   . LEU A 1 2437 ? 191.808 237.392 186.991 1.00 17.25 ? 2437 LEU A CD1   1 
ATOM   7475  C CD2   . LEU A 1 2437 ? 191.596 239.254 188.630 1.00 11.00 ? 2437 LEU A CD2   1 
ATOM   7476  N N     . GLU A 1 2438 ? 186.937 237.729 187.478 1.00 17.73 ? 2438 GLU A N     1 
ATOM   7477  C CA    . GLU A 1 2438 ? 186.012 236.924 188.267 1.00 17.09 ? 2438 GLU A CA    1 
ATOM   7478  C C     . GLU A 1 2438 ? 185.393 235.817 187.425 1.00 17.10 ? 2438 GLU A C     1 
ATOM   7479  O O     . GLU A 1 2438 ? 185.239 234.683 187.893 1.00 20.09 ? 2438 GLU A O     1 
ATOM   7480  C CB    . GLU A 1 2438 ? 184.925 237.814 188.870 1.00 16.13 ? 2438 GLU A CB    1 
ATOM   7481  C CG    . GLU A 1 2438 ? 185.171 238.205 190.318 1.00 19.30 ? 2438 GLU A CG    1 
ATOM   7482  C CD    . GLU A 1 2438 ? 184.285 239.349 190.772 1.00 22.70 ? 2438 GLU A CD    1 
ATOM   7483  O OE1   . GLU A 1 2438 ? 184.626 240.005 191.779 1.00 22.36 ? 2438 GLU A OE1   1 
ATOM   7484  O OE2   . GLU A 1 2438 ? 183.249 239.595 190.121 1.00 23.84 ? 2438 GLU A OE2   1 
ATOM   7485  N N     . HIS A 1 2439 ? 185.030 236.126 186.178 1.00 13.22 ? 2439 HIS A N     1 
ATOM   7486  C CA    . HIS A 1 2439 ? 184.448 235.110 185.306 1.00 16.89 ? 2439 HIS A CA    1 
ATOM   7487  C C     . HIS A 1 2439 ? 185.480 234.068 184.893 1.00 19.87 ? 2439 HIS A C     1 
ATOM   7488  O O     . HIS A 1 2439 ? 185.148 232.888 184.735 1.00 22.17 ? 2439 HIS A O     1 
ATOM   7489  C CB    . HIS A 1 2439 ? 183.830 235.768 184.075 1.00 18.73 ? 2439 HIS A CB    1 
ATOM   7490  C CG    . HIS A 1 2439 ? 182.959 234.849 183.278 1.00 20.45 ? 2439 HIS A CG    1 
ATOM   7491  N ND1   . HIS A 1 2439 ? 181.623 234.661 183.558 1.00 23.60 ? 2439 HIS A ND1   1 
ATOM   7492  C CD2   . HIS A 1 2439 ? 183.231 234.076 182.200 1.00 20.52 ? 2439 HIS A CD2   1 
ATOM   7493  C CE1   . HIS A 1 2439 ? 181.111 233.805 182.692 1.00 22.58 ? 2439 HIS A CE1   1 
ATOM   7494  N NE2   . HIS A 1 2439 ? 182.066 233.436 181.857 1.00 26.04 ? 2439 HIS A NE2   1 
ATOM   7495  N N     . ALA A 1 2440 ? 186.731 234.482 184.694 1.00 19.44 ? 2440 ALA A N     1 
ATOM   7496  C CA    . ALA A 1 2440 ? 187.766 233.535 184.300 1.00 16.46 ? 2440 ALA A CA    1 
ATOM   7497  C C     . ALA A 1 2440 ? 188.144 232.610 185.445 1.00 11.40 ? 2440 ALA A C     1 
ATOM   7498  O O     . ALA A 1 2440 ? 188.589 231.482 185.207 1.00 14.78 ? 2440 ALA A O     1 
ATOM   7499  C CB    . ALA A 1 2440 ? 188.999 234.282 183.793 1.00 14.34 ? 2440 ALA A CB    1 
ATOM   7500  N N     . PHE A 1 2441 ? 187.985 233.065 186.689 1.00 12.56 ? 2441 PHE A N     1 
ATOM   7501  C CA    . PHE A 1 2441 ? 188.316 232.205 187.820 1.00 17.66 ? 2441 PHE A CA    1 
ATOM   7502  C C     . PHE A 1 2441 ? 187.395 230.995 187.913 1.00 22.26 ? 2441 PHE A C     1 
ATOM   7503  O O     . PHE A 1 2441 ? 187.787 229.965 188.473 1.00 20.50 ? 2441 PHE A O     1 
ATOM   7504  C CB    . PHE A 1 2441 ? 188.286 233.001 189.123 1.00 15.41 ? 2441 PHE A CB    1 
ATOM   7505  C CG    . PHE A 1 2441 ? 189.631 233.507 189.545 1.00 15.20 ? 2441 PHE A CG    1 
ATOM   7506  C CD1   . PHE A 1 2441 ? 190.580 232.634 190.046 1.00 14.73 ? 2441 PHE A CD1   1 
ATOM   7507  C CD2   . PHE A 1 2441 ? 189.954 234.846 189.435 1.00 16.77 ? 2441 PHE A CD2   1 
ATOM   7508  C CE1   . PHE A 1 2441 ? 191.822 233.088 190.433 1.00 16.83 ? 2441 PHE A CE1   1 
ATOM   7509  C CE2   . PHE A 1 2441 ? 191.196 235.306 189.821 1.00 20.46 ? 2441 PHE A CE2   1 
ATOM   7510  C CZ    . PHE A 1 2441 ? 192.130 234.426 190.320 1.00 21.00 ? 2441 PHE A CZ    1 
ATOM   7511  N N     . GLN A 1 2442 ? 186.179 231.086 187.376 1.00 25.22 ? 2442 GLN A N     1 
ATOM   7512  C CA    . GLN A 1 2442 ? 185.258 229.958 187.409 1.00 23.46 ? 2442 GLN A CA    1 
ATOM   7513  C C     . GLN A 1 2442 ? 185.334 229.094 186.157 1.00 22.05 ? 2442 GLN A C     1 
ATOM   7514  O O     . GLN A 1 2442 ? 184.565 228.135 186.038 1.00 24.15 ? 2442 GLN A O     1 
ATOM   7515  C CB    . GLN A 1 2442 ? 183.818 230.441 187.616 1.00 26.17 ? 2442 GLN A CB    1 
ATOM   7516  C CG    . GLN A 1 2442 ? 183.228 231.205 186.449 1.00 28.18 ? 2442 GLN A CG    1 
ATOM   7517  C CD    . GLN A 1 2442 ? 181.832 231.720 186.739 1.00 29.74 ? 2442 GLN A CD    1 
ATOM   7518  O OE1   . GLN A 1 2442 ? 181.271 231.458 187.802 1.00 26.23 ? 2442 GLN A OE1   1 
ATOM   7519  N NE2   . GLN A 1 2442 ? 181.262 232.454 185.791 1.00 24.46 ? 2442 GLN A NE2   1 
ATOM   7520  N N     . LEU A 1 2443 ? 186.231 229.405 185.226 1.00 22.38 ? 2443 LEU A N     1 
ATOM   7521  C CA    . LEU A 1 2443 ? 186.465 228.561 184.066 1.00 19.01 ? 2443 LEU A CA    1 
ATOM   7522  C C     . LEU A 1 2443 ? 187.423 227.435 184.452 1.00 18.97 ? 2443 LEU A C     1 
ATOM   7523  O O     . LEU A 1 2443 ? 187.735 227.231 185.628 1.00 21.41 ? 2443 LEU A O     1 
ATOM   7524  C CB    . LEU A 1 2443 ? 187.002 229.388 182.900 1.00 15.04 ? 2443 LEU A CB    1 
ATOM   7525  C CG    . LEU A 1 2443 ? 186.145 230.553 182.401 1.00 22.95 ? 2443 LEU A CG    1 
ATOM   7526  C CD1   . LEU A 1 2443 ? 186.663 231.059 181.066 1.00 19.95 ? 2443 LEU A CD1   1 
ATOM   7527  C CD2   . LEU A 1 2443 ? 184.688 230.143 182.286 1.00 23.12 ? 2443 LEU A CD2   1 
ATOM   7528  N N     . GLU A 1 2444 ? 187.901 226.688 183.462 1.00 20.19 ? 2444 GLU A N     1 
ATOM   7529  C CA    . GLU A 1 2444 ? 188.843 225.601 183.682 1.00 19.33 ? 2444 GLU A CA    1 
ATOM   7530  C C     . GLU A 1 2444 ? 190.112 225.869 182.889 1.00 20.53 ? 2444 GLU A C     1 
ATOM   7531  O O     . GLU A 1 2444 ? 190.050 226.150 181.688 1.00 18.56 ? 2444 GLU A O     1 
ATOM   7532  C CB    . GLU A 1 2444 ? 188.238 224.254 183.281 1.00 22.18 ? 2444 GLU A CB    1 
ATOM   7533  C CG    . GLU A 1 2444 ? 189.219 223.097 183.334 1.00 24.06 ? 2444 GLU A CG    1 
ATOM   7534  C CD    . GLU A 1 2444 ? 188.528 221.750 183.328 1.00 26.38 ? 2444 GLU A CD    1 
ATOM   7535  O OE1   . GLU A 1 2444 ? 189.234 220.719 183.322 1.00 25.88 ? 2444 GLU A OE1   1 
ATOM   7536  O OE2   . GLU A 1 2444 ? 187.279 221.722 183.332 1.00 24.65 ? 2444 GLU A OE2   1 
ATOM   7537  N N     . HIS A 1 2445 ? 191.256 225.781 183.562 1.00 16.40 ? 2445 HIS A N     1 
ATOM   7538  C CA    . HIS A 1 2445 ? 192.552 226.015 182.947 1.00 12.78 ? 2445 HIS A CA    1 
ATOM   7539  C C     . HIS A 1 2445 ? 193.431 224.790 183.146 1.00 13.23 ? 2445 HIS A C     1 
ATOM   7540  O O     . HIS A 1 2445 ? 193.204 223.976 184.044 1.00 17.58 ? 2445 HIS A O     1 
ATOM   7541  C CB    . HIS A 1 2445 ? 193.238 227.263 183.527 1.00 9.77  ? 2445 HIS A CB    1 
ATOM   7542  C CG    . HIS A 1 2445 ? 192.346 228.463 183.602 1.00 12.67 ? 2445 HIS A CG    1 
ATOM   7543  N ND1   . HIS A 1 2445 ? 192.394 229.484 182.678 1.00 12.54 ? 2445 HIS A ND1   1 
ATOM   7544  C CD2   . HIS A 1 2445 ? 191.377 228.801 184.485 1.00 13.75 ? 2445 HIS A CD2   1 
ATOM   7545  C CE1   . HIS A 1 2445 ? 191.496 230.400 182.990 1.00 13.09 ? 2445 HIS A CE1   1 
ATOM   7546  N NE2   . HIS A 1 2445 ? 190.864 230.009 184.081 1.00 10.67 ? 2445 HIS A NE2   1 
ATOM   7547  N N     . ILE A 1 2446 ? 194.440 224.664 182.283 1.00 11.06 ? 2446 ILE A N     1 
ATOM   7548  C CA    . ILE A 1 2446 ? 195.341 223.518 182.361 1.00 9.28  ? 2446 ILE A CA    1 
ATOM   7549  C C     . ILE A 1 2446 ? 196.160 223.566 183.644 1.00 14.21 ? 2446 ILE A C     1 
ATOM   7550  O O     . ILE A 1 2446 ? 196.456 222.529 184.249 1.00 13.86 ? 2446 ILE A O     1 
ATOM   7551  C CB    . ILE A 1 2446 ? 196.240 223.456 181.114 1.00 9.24  ? 2446 ILE A CB    1 
ATOM   7552  C CG1   . ILE A 1 2446 ? 195.408 223.686 179.853 1.00 17.63 ? 2446 ILE A CG1   1 
ATOM   7553  C CG2   . ILE A 1 2446 ? 196.937 222.117 181.038 1.00 14.10 ? 2446 ILE A CG2   1 
ATOM   7554  C CD1   . ILE A 1 2446 ? 194.302 222.669 179.662 1.00 9.95  ? 2446 ILE A CD1   1 
ATOM   7555  N N     . MET A 1 2447 ? 196.541 224.762 184.075 1.00 18.65 ? 2447 MET A N     1 
ATOM   7556  C CA    . MET A 1 2447 ? 197.256 224.952 185.325 1.00 9.11  ? 2447 MET A CA    1 
ATOM   7557  C C     . MET A 1 2447 ? 196.365 225.666 186.330 1.00 9.41  ? 2447 MET A C     1 
ATOM   7558  O O     . MET A 1 2447 ? 195.375 226.308 185.970 1.00 9.87  ? 2447 MET A O     1 
ATOM   7559  C CB    . MET A 1 2447 ? 198.544 225.748 185.106 1.00 4.19  ? 2447 MET A CB    1 
ATOM   7560  C CG    . MET A 1 2447 ? 199.657 224.944 184.476 1.00 8.59  ? 2447 MET A CG    1 
ATOM   7561  S SD    . MET A 1 2447 ? 201.208 225.848 184.461 1.00 22.50 ? 2447 MET A SD    1 
ATOM   7562  C CE    . MET A 1 2447 ? 202.162 224.854 183.330 1.00 7.00  ? 2447 MET A CE    1 
ATOM   7563  N N     . ASP A 1 2448 ? 196.724 225.534 187.605 1.00 16.71 ? 2448 ASP A N     1 
ATOM   7564  C CA    . ASP A 1 2448 ? 195.971 226.197 188.660 1.00 15.47 ? 2448 ASP A CA    1 
ATOM   7565  C C     . ASP A 1 2448 ? 196.008 227.704 188.456 1.00 14.03 ? 2448 ASP A C     1 
ATOM   7566  O O     . ASP A 1 2448 ? 197.075 228.289 188.248 1.00 15.58 ? 2448 ASP A O     1 
ATOM   7567  C CB    . ASP A 1 2448 ? 196.538 225.829 190.030 1.00 13.63 ? 2448 ASP A CB    1 
ATOM   7568  C CG    . ASP A 1 2448 ? 195.767 224.707 190.694 1.00 18.78 ? 2448 ASP A CG    1 
ATOM   7569  O OD1   . ASP A 1 2448 ? 194.668 224.370 190.206 1.00 16.89 ? 2448 ASP A OD1   1 
ATOM   7570  O OD2   . ASP A 1 2448 ? 196.259 224.162 191.704 1.00 23.57 ? 2448 ASP A OD2   1 
ATOM   7571  N N     . LEU A 1 2449 ? 194.839 228.331 188.516 1.00 15.15 ? 2449 LEU A N     1 
ATOM   7572  C CA    . LEU A 1 2449 ? 194.728 229.742 188.184 1.00 10.75 ? 2449 LEU A CA    1 
ATOM   7573  C C     . LEU A 1 2449 ? 195.201 230.599 189.351 1.00 10.02 ? 2449 LEU A C     1 
ATOM   7574  O O     . LEU A 1 2449 ? 194.689 230.483 190.468 1.00 9.49  ? 2449 LEU A O     1 
ATOM   7575  C CB    . LEU A 1 2449 ? 193.287 230.095 187.826 1.00 13.58 ? 2449 LEU A CB    1 
ATOM   7576  C CG    . LEU A 1 2449 ? 193.124 231.518 187.299 1.00 11.93 ? 2449 LEU A CG    1 
ATOM   7577  C CD1   . LEU A 1 2449 ? 194.190 231.782 186.265 1.00 5.76  ? 2449 LEU A CD1   1 
ATOM   7578  C CD2   . LEU A 1 2449 ? 191.746 231.739 186.716 1.00 14.90 ? 2449 LEU A CD2   1 
ATOM   7579  N N     . THR A 1 2450 ? 196.176 231.461 189.084 1.00 10.65 ? 2450 THR A N     1 
ATOM   7580  C CA    . THR A 1 2450 ? 196.674 232.423 190.055 1.00 6.78  ? 2450 THR A CA    1 
ATOM   7581  C C     . THR A 1 2450 ? 196.397 233.826 189.540 1.00 1.11  ? 2450 THR A C     1 
ATOM   7582  O O     . THR A 1 2450 ? 196.702 234.143 188.386 1.00 5.17  ? 2450 THR A O     1 
ATOM   7583  C CB    . THR A 1 2450 ? 198.174 232.238 190.310 1.00 7.24  ? 2450 THR A CB    1 
ATOM   7584  O OG1   . THR A 1 2450 ? 198.433 230.876 190.670 1.00 6.71  ? 2450 THR A OG1   1 
ATOM   7585  C CG2   . THR A 1 2450 ? 198.640 233.142 191.437 1.00 3.56  ? 2450 THR A CG2   1 
ATOM   7586  N N     . ARG A 1 2451 ? 195.817 234.661 190.404 1.00 0.27  ? 2451 ARG A N     1 
ATOM   7587  C CA    . ARG A 1 2451 ? 195.417 236.006 189.998 1.00 1.80  ? 2451 ARG A CA    1 
ATOM   7588  C C     . ARG A 1 2451 ? 196.619 236.819 189.535 1.00 1.30  ? 2451 ARG A C     1 
ATOM   7589  O O     . ARG A 1 2451 ? 196.546 237.552 188.541 1.00 5.89  ? 2451 ARG A O     1 
ATOM   7590  C CB    . ARG A 1 2451 ? 194.704 236.699 191.160 1.00 0.72  ? 2451 ARG A CB    1 
ATOM   7591  C CG    . ARG A 1 2451 ? 194.371 238.157 190.928 1.00 1.34  ? 2451 ARG A CG    1 
ATOM   7592  C CD    . ARG A 1 2451 ? 193.916 238.820 192.217 1.00 3.18  ? 2451 ARG A CD    1 
ATOM   7593  N NE    . ARG A 1 2451 ? 194.957 238.814 193.238 1.00 9.92  ? 2451 ARG A NE    1 
ATOM   7594  C CZ    . ARG A 1 2451 ? 194.851 239.405 194.420 1.00 0.91  ? 2451 ARG A CZ    1 
ATOM   7595  N NH1   . ARG A 1 2451 ? 193.751 240.045 194.777 1.00 0.00  ? 2451 ARG A NH1   1 
ATOM   7596  N NH2   . ARG A 1 2451 ? 195.875 239.352 195.266 1.00 0.00  ? 2451 ARG A NH2   1 
ATOM   7597  N N     . LEU A 1 2452 ? 197.742 236.692 190.241 1.00 5.76  ? 2452 LEU A N     1 
ATOM   7598  C CA    . LEU A 1 2452 ? 198.937 237.441 189.869 1.00 0.70  ? 2452 LEU A CA    1 
ATOM   7599  C C     . LEU A 1 2452 ? 199.475 237.001 188.515 1.00 0.36  ? 2452 LEU A C     1 
ATOM   7600  O O     . LEU A 1 2452 ? 200.022 237.817 187.773 1.00 5.13  ? 2452 LEU A O     1 
ATOM   7601  C CB    . LEU A 1 2452 ? 200.013 237.306 190.947 1.00 5.15  ? 2452 LEU A CB    1 
ATOM   7602  C CG    . LEU A 1 2452 ? 199.930 238.238 192.160 1.00 6.23  ? 2452 LEU A CG    1 
ATOM   7603  C CD1   . LEU A 1 2452 ? 200.109 239.676 191.714 1.00 0.00  ? 2452 LEU A CD1   1 
ATOM   7604  C CD2   . LEU A 1 2452 ? 198.622 238.082 192.915 1.00 11.32 ? 2452 LEU A CD2   1 
ATOM   7605  N N     . ARG A 1 2453 ? 199.321 235.723 188.166 1.00 1.32  ? 2453 ARG A N     1 
ATOM   7606  C CA    . ARG A 1 2453 ? 199.816 235.253 186.874 1.00 0.00  ? 2453 ARG A CA    1 
ATOM   7607  C C     . ARG A 1 2453 ? 199.077 235.935 185.728 1.00 3.09  ? 2453 ARG A C     1 
ATOM   7608  O O     . ARG A 1 2453 ? 199.696 236.511 184.822 1.00 10.83 ? 2453 ARG A O     1 
ATOM   7609  C CB    . ARG A 1 2453 ? 199.673 233.733 186.784 1.00 0.01  ? 2453 ARG A CB    1 
ATOM   7610  C CG    . ARG A 1 2453 ? 200.416 233.085 185.625 1.00 2.91  ? 2453 ARG A CG    1 
ATOM   7611  C CD    . ARG A 1 2453 ? 199.479 232.579 184.545 1.00 9.94  ? 2453 ARG A CD    1 
ATOM   7612  N NE    . ARG A 1 2453 ? 198.407 231.747 185.077 1.00 14.76 ? 2453 ARG A NE    1 
ATOM   7613  C CZ    . ARG A 1 2453 ? 198.500 230.441 185.285 1.00 8.22  ? 2453 ARG A CZ    1 
ATOM   7614  N NH1   . ARG A 1 2453 ? 199.631 229.789 185.083 1.00 7.04  ? 2453 ARG A NH1   1 
ATOM   7615  N NH2   . ARG A 1 2453 ? 197.434 229.775 185.718 1.00 7.67  ? 2453 ARG A NH2   1 
ATOM   7616  N N     . CYS A 1 2454 ? 197.742 235.894 185.765 1.00 1.65  ? 2454 CYS A N     1 
ATOM   7617  C CA    . CYS A 1 2454 ? 196.942 236.544 184.733 1.00 0.00  ? 2454 CYS A CA    1 
ATOM   7618  C C     . CYS A 1 2454 ? 197.160 238.048 184.725 1.00 2.56  ? 2454 CYS A C     1 
ATOM   7619  O O     . CYS A 1 2454 ? 197.278 238.654 183.655 1.00 11.22 ? 2454 CYS A O     1 
ATOM   7620  C CB    . CYS A 1 2454 ? 195.463 236.228 184.936 1.00 0.00  ? 2454 CYS A CB    1 
ATOM   7621  S SG    . CYS A 1 2454 ? 195.004 234.554 184.481 1.00 26.71 ? 2454 CYS A SG    1 
ATOM   7622  N N     . LEU A 1 2455 ? 197.207 238.671 185.904 1.00 3.94  ? 2455 LEU A N     1 
ATOM   7623  C CA    . LEU A 1 2455 ? 197.393 240.116 185.953 1.00 0.00  ? 2455 LEU A CA    1 
ATOM   7624  C C     . LEU A 1 2455 ? 198.758 240.520 185.410 1.00 0.00  ? 2455 LEU A C     1 
ATOM   7625  O O     . LEU A 1 2455 ? 198.869 241.506 184.679 1.00 8.92  ? 2455 LEU A O     1 
ATOM   7626  C CB    . LEU A 1 2455 ? 197.193 240.625 187.378 1.00 0.35  ? 2455 LEU A CB    1 
ATOM   7627  C CG    . LEU A 1 2455 ? 195.736 240.608 187.842 1.00 0.00  ? 2455 LEU A CG    1 
ATOM   7628  C CD1   . LEU A 1 2455 ? 195.560 241.380 189.133 1.00 0.03  ? 2455 LEU A CD1   1 
ATOM   7629  C CD2   . LEU A 1 2455 ? 194.825 241.161 186.759 1.00 0.00  ? 2455 LEU A CD2   1 
ATOM   7630  N N     . GLY A 1 2456 ? 199.806 239.765 185.738 1.00 0.00  ? 2456 GLY A N     1 
ATOM   7631  C CA    . GLY A 1 2456 ? 201.124 240.086 185.222 1.00 2.70  ? 2456 GLY A CA    1 
ATOM   7632  C C     . GLY A 1 2456 ? 201.225 239.896 183.723 1.00 0.50  ? 2456 GLY A C     1 
ATOM   7633  O O     . GLY A 1 2456 ? 201.849 240.701 183.029 1.00 7.37  ? 2456 GLY A O     1 
ATOM   7634  N N     . SER A 1 2457 ? 200.620 238.826 183.202 1.00 0.00  ? 2457 SER A N     1 
ATOM   7635  C CA    . SER A 1 2457 ? 200.599 238.642 181.755 1.00 0.00  ? 2457 SER A CA    1 
ATOM   7636  C C     . SER A 1 2457 ? 199.842 239.773 181.069 1.00 0.73  ? 2457 SER A C     1 
ATOM   7637  O O     . SER A 1 2457 ? 200.288 240.296 180.039 1.00 6.55  ? 2457 SER A O     1 
ATOM   7638  C CB    . SER A 1 2457 ? 199.987 237.286 181.414 1.00 4.19  ? 2457 SER A CB    1 
ATOM   7639  O OG    . SER A 1 2457 ? 198.623 237.239 181.779 1.00 4.15  ? 2457 SER A OG    1 
ATOM   7640  N N     . LEU A 1 2458 ? 198.705 240.178 181.641 1.00 1.47  ? 2458 LEU A N     1 
ATOM   7641  C CA    . LEU A 1 2458 ? 197.949 241.303 181.102 1.00 0.00  ? 2458 LEU A CA    1 
ATOM   7642  C C     . LEU A 1 2458 ? 198.778 242.579 181.112 1.00 0.00  ? 2458 LEU A C     1 
ATOM   7643  O O     . LEU A 1 2458 ? 198.788 243.332 180.134 1.00 7.23  ? 2458 LEU A O     1 
ATOM   7644  C CB    . LEU A 1 2458 ? 196.664 241.495 181.905 1.00 0.00  ? 2458 LEU A CB    1 
ATOM   7645  C CG    . LEU A 1 2458 ? 195.833 242.734 181.576 1.00 0.00  ? 2458 LEU A CG    1 
ATOM   7646  C CD1   . LEU A 1 2458 ? 195.264 242.645 180.177 1.00 5.18  ? 2458 LEU A CD1   1 
ATOM   7647  C CD2   . LEU A 1 2458 ? 194.721 242.917 182.593 1.00 1.13  ? 2458 LEU A CD2   1 
ATOM   7648  N N     . PHE A 1 2459 ? 199.478 242.841 182.216 1.00 0.67  ? 2459 PHE A N     1 
ATOM   7649  C CA    . PHE A 1 2459 ? 200.272 244.060 182.318 1.00 0.00  ? 2459 PHE A CA    1 
ATOM   7650  C C     . PHE A 1 2459 ? 201.428 244.053 181.328 1.00 0.40  ? 2459 PHE A C     1 
ATOM   7651  O O     . PHE A 1 2459 ? 201.748 245.088 180.740 1.00 7.26  ? 2459 PHE A O     1 
ATOM   7652  C CB    . PHE A 1 2459 ? 200.784 244.243 183.747 1.00 0.00  ? 2459 PHE A CB    1 
ATOM   7653  C CG    . PHE A 1 2459 ? 199.693 244.345 184.777 1.00 0.28  ? 2459 PHE A CG    1 
ATOM   7654  C CD1   . PHE A 1 2459 ? 198.440 244.828 184.439 1.00 0.00  ? 2459 PHE A CD1   1 
ATOM   7655  C CD2   . PHE A 1 2459 ? 199.926 243.973 186.089 1.00 3.68  ? 2459 PHE A CD2   1 
ATOM   7656  C CE1   . PHE A 1 2459 ? 197.441 244.923 185.387 1.00 0.00  ? 2459 PHE A CE1   1 
ATOM   7657  C CE2   . PHE A 1 2459 ? 198.929 244.064 187.036 1.00 0.00  ? 2459 PHE A CE2   1 
ATOM   7658  C CZ    . PHE A 1 2459 ? 197.688 244.542 186.685 1.00 0.00  ? 2459 PHE A CZ    1 
ATOM   7659  N N     . SER A 1 2460 ? 202.068 242.899 181.130 1.00 3.19  ? 2460 SER A N     1 
ATOM   7660  C CA    . SER A 1 2460 ? 203.140 242.815 180.144 1.00 0.00  ? 2460 SER A CA    1 
ATOM   7661  C C     . SER A 1 2460 ? 202.612 243.042 178.731 1.00 1.46  ? 2460 SER A C     1 
ATOM   7662  O O     . SER A 1 2460 ? 203.243 243.745 177.927 1.00 11.47 ? 2460 SER A O     1 
ATOM   7663  C CB    . SER A 1 2460 ? 203.843 241.463 180.252 1.00 2.01  ? 2460 SER A CB    1 
ATOM   7664  O OG    . SER A 1 2460 ? 204.852 241.333 179.269 1.00 14.22 ? 2460 SER A OG    1 
ATOM   7665  N N     . MET A 1 2461 ? 201.448 242.469 178.412 1.00 0.87  ? 2461 MET A N     1 
ATOM   7666  C CA    . MET A 1 2461 ? 200.860 242.701 177.096 1.00 0.00  ? 2461 MET A CA    1 
ATOM   7667  C C     . MET A 1 2461 ? 200.497 244.167 176.892 1.00 1.72  ? 2461 MET A C     1 
ATOM   7668  O O     . MET A 1 2461 ? 200.742 244.722 175.816 1.00 6.69  ? 2461 MET A O     1 
ATOM   7669  C CB    . MET A 1 2461 ? 199.629 241.819 176.904 1.00 0.72  ? 2461 MET A CB    1 
ATOM   7670  C CG    . MET A 1 2461 ? 199.950 240.381 176.551 1.00 4.55  ? 2461 MET A CG    1 
ATOM   7671  S SD    . MET A 1 2461 ? 198.481 239.349 176.463 1.00 7.41  ? 2461 MET A SD    1 
ATOM   7672  C CE    . MET A 1 2461 ? 198.186 239.357 174.700 1.00 7.91  ? 2461 MET A CE    1 
ATOM   7673  N N     . LEU A 1 2462 ? 199.917 244.806 177.909 1.00 1.65  ? 2462 LEU A N     1 
ATOM   7674  C CA    . LEU A 1 2462 ? 199.586 246.225 177.818 1.00 0.00  ? 2462 LEU A CA    1 
ATOM   7675  C C     . LEU A 1 2462 ? 200.837 247.086 177.717 1.00 1.35  ? 2462 LEU A C     1 
ATOM   7676  O O     . LEU A 1 2462 ? 200.818 248.127 177.054 1.00 4.58  ? 2462 LEU A O     1 
ATOM   7677  C CB    . LEU A 1 2462 ? 198.749 246.630 179.028 1.00 1.28  ? 2462 LEU A CB    1 
ATOM   7678  C CG    . LEU A 1 2462 ? 197.441 245.854 179.161 1.00 0.03  ? 2462 LEU A CG    1 
ATOM   7679  C CD1   . LEU A 1 2462 ? 196.767 246.150 180.480 1.00 3.17  ? 2462 LEU A CD1   1 
ATOM   7680  C CD2   . LEU A 1 2462 ? 196.515 246.182 178.003 1.00 3.07  ? 2462 LEU A CD2   1 
ATOM   7681  N N     . HIS A 1 2463 ? 201.924 246.676 178.371 1.00 3.43  ? 2463 HIS A N     1 
ATOM   7682  C CA    . HIS A 1 2463 ? 203.196 247.366 178.208 1.00 2.95  ? 2463 HIS A CA    1 
ATOM   7683  C C     . HIS A 1 2463 ? 203.682 247.275 176.773 1.00 3.55  ? 2463 HIS A C     1 
ATOM   7684  O O     . HIS A 1 2463 ? 204.214 248.250 176.232 1.00 9.85  ? 2463 HIS A O     1 
ATOM   7685  C CB    . HIS A 1 2463 ? 204.236 246.776 179.158 1.00 2.13  ? 2463 HIS A CB    1 
ATOM   7686  C CG    . HIS A 1 2463 ? 204.128 247.285 180.560 1.00 3.67  ? 2463 HIS A CG    1 
ATOM   7687  N ND1   . HIS A 1 2463 ? 204.925 246.819 181.583 1.00 1.78  ? 2463 HIS A ND1   1 
ATOM   7688  C CD2   . HIS A 1 2463 ? 203.304 248.205 181.114 1.00 3.47  ? 2463 HIS A CD2   1 
ATOM   7689  C CE1   . HIS A 1 2463 ? 204.604 247.438 182.704 1.00 5.16  ? 2463 HIS A CE1   1 
ATOM   7690  N NE2   . HIS A 1 2463 ? 203.623 248.284 182.447 1.00 5.18  ? 2463 HIS A NE2   1 
ATOM   7691  N N     . GLN A 1 2464 ? 203.518 246.109 176.146 1.00 3.35  ? 2464 GLN A N     1 
ATOM   7692  C CA    . GLN A 1 2464 ? 203.796 245.997 174.717 1.00 2.10  ? 2464 GLN A CA    1 
ATOM   7693  C C     . GLN A 1 2464 ? 202.886 246.889 173.883 1.00 7.10  ? 2464 GLN A C     1 
ATOM   7694  O O     . GLN A 1 2464 ? 203.334 247.453 172.879 1.00 17.82 ? 2464 GLN A O     1 
ATOM   7695  C CB    . GLN A 1 2464 ? 203.660 244.549 174.254 1.00 1.76  ? 2464 GLN A CB    1 
ATOM   7696  C CG    . GLN A 1 2464 ? 204.382 244.258 172.949 1.00 5.87  ? 2464 GLN A CG    1 
ATOM   7697  C CD    . GLN A 1 2464 ? 205.889 244.267 173.097 1.00 11.09 ? 2464 GLN A CD    1 
ATOM   7698  O OE1   . GLN A 1 2464 ? 206.418 244.153 174.202 1.00 16.48 ? 2464 GLN A OE1   1 
ATOM   7699  N NE2   . GLN A 1 2464 ? 206.590 244.411 171.979 1.00 5.90  ? 2464 GLN A NE2   1 
ATOM   7700  N N     . ALA A 1 2465 ? 201.616 247.023 174.271 1.00 5.85  ? 2465 ALA A N     1 
ATOM   7701  C CA    . ALA A 1 2465 ? 200.701 247.885 173.529 1.00 2.65  ? 2465 ALA A CA    1 
ATOM   7702  C C     . ALA A 1 2465 ? 201.161 249.337 173.539 1.00 4.00  ? 2465 ALA A C     1 
ATOM   7703  O O     . ALA A 1 2465 ? 200.805 250.105 172.638 1.00 3.31  ? 2465 ALA A O     1 
ATOM   7704  C CB    . ALA A 1 2465 ? 199.290 247.776 174.101 1.00 3.92  ? 2465 ALA A CB    1 
ATOM   7705  N N     . CYS A 1 2466 ? 201.933 249.736 174.548 1.00 5.89  ? 2466 CYS A N     1 
ATOM   7706  C CA    . CYS A 1 2466 ? 202.513 251.071 174.592 1.00 3.02  ? 2466 CYS A CA    1 
ATOM   7707  C C     . CYS A 1 2466 ? 203.856 251.162 173.883 1.00 8.09  ? 2466 CYS A C     1 
ATOM   7708  O O     . CYS A 1 2466 ? 204.349 252.274 173.670 1.00 13.47 ? 2466 CYS A O     1 
ATOM   7709  C CB    . CYS A 1 2466 ? 202.670 251.541 176.043 1.00 2.80  ? 2466 CYS A CB    1 
ATOM   7710  S SG    . CYS A 1 2466 ? 201.247 251.213 177.103 1.00 14.15 ? 2466 CYS A SG    1 
ATOM   7711  N N     . ARG A 1 2467 ? 204.462 250.034 173.519 1.00 2.77  ? 2467 ARG A N     1 
ATOM   7712  C CA    . ARG A 1 2467 ? 205.637 250.045 172.658 1.00 0.56  ? 2467 ARG A CA    1 
ATOM   7713  C C     . ARG A 1 2467 ? 205.284 249.961 171.184 1.00 4.57  ? 2467 ARG A C     1 
ATOM   7714  O O     . ARG A 1 2467 ? 206.044 250.460 170.346 1.00 13.66 ? 2467 ARG A O     1 
ATOM   7715  C CB    . ARG A 1 2467 ? 206.585 248.897 173.019 1.00 4.70  ? 2467 ARG A CB    1 
ATOM   7716  C CG    . ARG A 1 2467 ? 206.843 248.752 174.504 1.00 5.25  ? 2467 ARG A CG    1 
ATOM   7717  C CD    . ARG A 1 2467 ? 207.613 247.483 174.811 1.00 5.89  ? 2467 ARG A CD    1 
ATOM   7718  N NE    . ARG A 1 2467 ? 208.252 247.548 176.119 1.00 13.86 ? 2467 ARG A NE    1 
ATOM   7719  C CZ    . ARG A 1 2467 ? 208.668 246.492 176.804 1.00 14.29 ? 2467 ARG A CZ    1 
ATOM   7720  N NH1   . ARG A 1 2467 ? 208.538 245.265 176.329 1.00 8.79  ? 2467 ARG A NH1   1 
ATOM   7721  N NH2   . ARG A 1 2467 ? 209.229 246.673 177.996 1.00 13.90 ? 2467 ARG A NH2   1 
ATOM   7722  N N     . ASN A 1 2468 ? 204.148 249.345 170.849 1.00 3.86  ? 2468 ASN A N     1 
ATOM   7723  C CA    . ASN A 1 2468 ? 203.662 249.401 169.478 1.00 7.33  ? 2468 ASN A CA    1 
ATOM   7724  C C     . ASN A 1 2468 ? 203.431 250.838 169.042 1.00 13.60 ? 2468 ASN A C     1 
ATOM   7725  O O     . ASN A 1 2468 ? 203.752 251.203 167.907 1.00 20.96 ? 2468 ASN A O     1 
ATOM   7726  C CB    . ASN A 1 2468 ? 202.371 248.595 169.339 1.00 9.16  ? 2468 ASN A CB    1 
ATOM   7727  C CG    . ASN A 1 2468 ? 202.578 247.117 169.586 1.00 11.11 ? 2468 ASN A CG    1 
ATOM   7728  O OD1   . ASN A 1 2468 ? 203.708 246.650 169.712 1.00 12.57 ? 2468 ASN A OD1   1 
ATOM   7729  N ND2   . ASN A 1 2468 ? 201.483 246.370 169.650 1.00 5.32  ? 2468 ASN A ND2   1 
ATOM   7730  N N     . VAL A 1 2469 ? 202.889 251.667 169.934 1.00 11.77 ? 2469 VAL A N     1 
ATOM   7731  C CA    . VAL A 1 2469 ? 202.712 253.084 169.638 1.00 6.43  ? 2469 VAL A CA    1 
ATOM   7732  C C     . VAL A 1 2469 ? 204.059 253.768 169.447 1.00 6.34  ? 2469 VAL A C     1 
ATOM   7733  O O     . VAL A 1 2469 ? 204.208 254.640 168.585 1.00 15.15 ? 2469 VAL A O     1 
ATOM   7734  C CB    . VAL A 1 2469 ? 201.885 253.749 170.750 1.00 7.77  ? 2469 VAL A CB    1 
ATOM   7735  C CG1   . VAL A 1 2469 ? 201.675 255.224 170.458 1.00 11.97 ? 2469 VAL A CG1   1 
ATOM   7736  C CG2   . VAL A 1 2469 ? 200.559 253.029 170.902 1.00 10.04 ? 2469 VAL A CG2   1 
ATOM   7737  N N     . ALA A 1 2470 ? 205.057 253.394 170.250 1.00 6.59  ? 2470 ALA A N     1 
ATOM   7738  C CA    . ALA A 1 2470 ? 206.383 253.986 170.104 1.00 13.42 ? 2470 ALA A CA    1 
ATOM   7739  C C     . ALA A 1 2470 ? 206.985 253.659 168.742 1.00 16.73 ? 2470 ALA A C     1 
ATOM   7740  O O     . ALA A 1 2470 ? 207.524 254.540 168.061 1.00 18.03 ? 2470 ALA A O     1 
ATOM   7741  C CB    . ALA A 1 2470 ? 207.298 253.508 171.230 1.00 16.76 ? 2470 ALA A CB    1 
ATOM   7742  N N     . GLN A 1 2471 ? 206.893 252.395 168.321 1.00 12.16 ? 2471 GLN A N     1 
ATOM   7743  C CA    . GLN A 1 2471 ? 207.406 252.028 167.003 1.00 15.58 ? 2471 GLN A CA    1 
ATOM   7744  C C     . GLN A 1 2471 ? 206.595 252.673 165.886 1.00 17.65 ? 2471 GLN A C     1 
ATOM   7745  O O     . GLN A 1 2471 ? 207.153 253.049 164.849 1.00 23.05 ? 2471 GLN A O     1 
ATOM   7746  C CB    . GLN A 1 2471 ? 207.440 250.507 166.840 1.00 12.47 ? 2471 GLN A CB    1 
ATOM   7747  C CG    . GLN A 1 2471 ? 208.690 249.840 167.414 1.00 15.69 ? 2471 GLN A CG    1 
ATOM   7748  C CD    . GLN A 1 2471 ? 208.784 249.922 168.923 1.00 21.50 ? 2471 GLN A CD    1 
ATOM   7749  O OE1   . GLN A 1 2471 ? 209.720 250.506 169.469 1.00 22.93 ? 2471 GLN A OE1   1 
ATOM   7750  N NE2   . GLN A 1 2471 ? 207.827 249.311 169.607 1.00 22.20 ? 2471 GLN A NE2   1 
ATOM   7751  N N     . TYR A 1 2472 ? 205.280 252.808 166.072 1.00 12.35 ? 2472 TYR A N     1 
ATOM   7752  C CA    . TYR A 1 2472 ? 204.457 253.480 165.073 1.00 14.00 ? 2472 TYR A CA    1 
ATOM   7753  C C     . TYR A 1 2472 ? 204.866 254.939 164.914 1.00 20.71 ? 2472 TYR A C     1 
ATOM   7754  O O     . TYR A 1 2472 ? 204.950 255.450 163.792 1.00 27.18 ? 2472 TYR A O     1 
ATOM   7755  C CB    . TYR A 1 2472 ? 202.984 253.371 165.461 1.00 15.06 ? 2472 TYR A CB    1 
ATOM   7756  C CG    . TYR A 1 2472 ? 202.025 254.004 164.482 1.00 18.14 ? 2472 TYR A CG    1 
ATOM   7757  C CD1   . TYR A 1 2472 ? 201.590 253.312 163.361 1.00 21.81 ? 2472 TYR A CD1   1 
ATOM   7758  C CD2   . TYR A 1 2472 ? 201.550 255.291 164.681 1.00 18.05 ? 2472 TYR A CD2   1 
ATOM   7759  C CE1   . TYR A 1 2472 ? 200.709 253.886 162.465 1.00 19.02 ? 2472 TYR A CE1   1 
ATOM   7760  C CE2   . TYR A 1 2472 ? 200.670 255.873 163.790 1.00 21.80 ? 2472 TYR A CE2   1 
ATOM   7761  C CZ    . TYR A 1 2472 ? 200.251 255.167 162.686 1.00 17.38 ? 2472 TYR A CZ    1 
ATOM   7762  O OH    . TYR A 1 2472 ? 199.374 255.746 161.799 1.00 19.15 ? 2472 TYR A OH    1 
ATOM   7763  N N     . ASN A 1 2473 ? 205.118 255.626 166.030 1.00 16.62 ? 2473 ASN A N     1 
ATOM   7764  C CA    . ASN A 1 2473 ? 205.564 257.014 165.964 1.00 17.06 ? 2473 ASN A CA    1 
ATOM   7765  C C     . ASN A 1 2473 ? 206.953 257.120 165.348 1.00 19.61 ? 2473 ASN A C     1 
ATOM   7766  O O     . ASN A 1 2473 ? 207.230 258.054 164.587 1.00 25.80 ? 2473 ASN A O     1 
ATOM   7767  C CB    . ASN A 1 2473 ? 205.546 257.642 167.357 1.00 17.94 ? 2473 ASN A CB    1 
ATOM   7768  C CG    . ASN A 1 2473 ? 204.143 257.804 167.906 1.00 18.43 ? 2473 ASN A CG    1 
ATOM   7769  O OD1   . ASN A 1 2473 ? 203.165 257.805 167.158 1.00 18.87 ? 2473 ASN A OD1   1 
ATOM   7770  N ND2   . ASN A 1 2473 ? 204.038 257.948 169.221 1.00 14.57 ? 2473 ASN A ND2   1 
ATOM   7771  N N     . ALA A 1 2474 ? 207.844 256.181 165.676 1.00 21.47 ? 2474 ALA A N     1 
ATOM   7772  C CA    . ALA A 1 2474 ? 209.185 256.207 165.101 1.00 22.99 ? 2474 ALA A CA    1 
ATOM   7773  C C     . ALA A 1 2474 ? 209.145 255.989 163.594 1.00 20.90 ? 2474 ALA A C     1 
ATOM   7774  O O     . ALA A 1 2474 ? 209.898 256.627 162.849 1.00 25.60 ? 2474 ALA A O     1 
ATOM   7775  C CB    . ALA A 1 2474 ? 210.066 255.156 165.773 1.00 19.11 ? 2474 ALA A CB    1 
ATOM   7776  N N     . ASN A 1 2475 ? 208.278 255.089 163.128 1.00 18.33 ? 2475 ASN A N     1 
ATOM   7777  C CA    . ASN A 1 2475 ? 208.173 254.833 161.695 1.00 23.94 ? 2475 ASN A CA    1 
ATOM   7778  C C     . ASN A 1 2475 ? 207.545 256.012 160.964 1.00 27.50 ? 2475 ASN A C     1 
ATOM   7779  O O     . ASN A 1 2475 ? 207.769 256.196 159.762 1.00 32.47 ? 2475 ASN A O     1 
ATOM   7780  C CB    . ASN A 1 2475 ? 207.367 253.559 161.450 1.00 22.83 ? 2475 ASN A CB    1 
ATOM   7781  C CG    . ASN A 1 2475 ? 208.129 252.307 161.833 1.00 26.26 ? 2475 ASN A CG    1 
ATOM   7782  O OD1   . ASN A 1 2475 ? 209.133 252.370 162.542 1.00 25.19 ? 2475 ASN A OD1   1 
ATOM   7783  N ND2   . ASN A 1 2475 ? 207.653 251.160 161.367 1.00 25.01 ? 2475 ASN A ND2   1 
ATOM   7784  N N     . HIS A 1 2476 ? 206.759 256.825 161.671 1.00 22.96 ? 2476 HIS A N     1 
ATOM   7785  C CA    . HIS A 1 2476 ? 206.037 257.953 161.083 1.00 26.21 ? 2476 HIS A CA    1 
ATOM   7786  C C     . HIS A 1 2476 ? 206.403 259.217 161.848 1.00 27.86 ? 2476 HIS A C     1 
ATOM   7787  O O     . HIS A 1 2476 ? 205.646 259.661 162.726 1.00 26.58 ? 2476 HIS A O     1 
ATOM   7788  C CB    . HIS A 1 2476 ? 204.529 257.713 161.117 1.00 25.84 ? 2476 HIS A CB    1 
ATOM   7789  C CG    . HIS A 1 2476 ? 204.083 256.555 160.280 1.00 27.50 ? 2476 HIS A CG    1 
ATOM   7790  N ND1   . HIS A 1 2476 ? 204.018 255.268 160.767 1.00 22.64 ? 2476 HIS A ND1   1 
ATOM   7791  C CD2   . HIS A 1 2476 ? 203.677 256.490 158.990 1.00 30.01 ? 2476 HIS A CD2   1 
ATOM   7792  C CE1   . HIS A 1 2476 ? 203.593 254.459 159.813 1.00 27.25 ? 2476 HIS A CE1   1 
ATOM   7793  N NE2   . HIS A 1 2476 ? 203.378 255.176 158.725 1.00 32.98 ? 2476 HIS A NE2   1 
ATOM   7794  N N     . PRO A 1 2477 ? 207.559 259.824 161.560 1.00 30.75 ? 2477 PRO A N     1 
ATOM   7795  C CA    . PRO A 1 2477 ? 207.918 261.069 162.266 1.00 30.18 ? 2477 PRO A CA    1 
ATOM   7796  C C     . PRO A 1 2477 ? 206.879 262.164 162.099 1.00 30.62 ? 2477 PRO A C     1 
ATOM   7797  O O     . PRO A 1 2477 ? 206.603 262.909 163.048 1.00 30.84 ? 2477 PRO A O     1 
ATOM   7798  C CB    . PRO A 1 2477 ? 209.270 261.448 161.640 1.00 32.06 ? 2477 PRO A CB    1 
ATOM   7799  C CG    . PRO A 1 2477 ? 209.342 260.677 160.357 1.00 31.29 ? 2477 PRO A CG    1 
ATOM   7800  C CD    . PRO A 1 2477 ? 208.594 259.409 160.601 1.00 28.34 ? 2477 PRO A CD    1 
ATOM   7801  N N     . ASP A 1 2478 ? 206.292 262.281 160.913 1.00 34.23 ? 2478 ASP A N     1 
ATOM   7802  C CA    . ASP A 1 2478 ? 205.169 263.181 160.723 1.00 34.60 ? 2478 ASP A CA    1 
ATOM   7803  C C     . ASP A 1 2478 ? 203.856 262.418 160.865 1.00 33.53 ? 2478 ASP A C     1 
ATOM   7804  O O     . ASP A 1 2478 ? 203.797 261.195 160.704 1.00 31.37 ? 2478 ASP A O     1 
ATOM   7805  C CB    . ASP A 1 2478 ? 205.241 263.865 159.357 1.00 33.79 ? 2478 ASP A CB    1 
ATOM   7806  C CG    . ASP A 1 2478 ? 205.381 262.877 158.217 1.00 36.53 ? 2478 ASP A CG    1 
ATOM   7807  O OD1   . ASP A 1 2478 ? 205.665 261.690 158.485 1.00 35.21 ? 2478 ASP A OD1   1 
ATOM   7808  O OD2   . ASP A 1 2478 ? 205.205 263.290 157.051 1.00 36.11 ? 2478 ASP A OD2   1 
ATOM   7809  N N     . PHE A 1 2479 ? 202.798 263.162 161.167 1.00 33.60 ? 2479 PHE A N     1 
ATOM   7810  C CA    . PHE A 1 2479 ? 201.474 262.603 161.413 1.00 34.67 ? 2479 PHE A CA    1 
ATOM   7811  C C     . PHE A 1 2479 ? 201.508 261.506 162.482 1.00 37.17 ? 2479 PHE A C     1 
ATOM   7812  O O     . PHE A 1 2479 ? 201.157 260.354 162.206 1.00 35.34 ? 2479 PHE A O     1 
ATOM   7813  C CB    . PHE A 1 2479 ? 200.863 262.074 160.123 1.00 34.44 ? 2479 PHE A CB    1 
ATOM   7814  C CG    . PHE A 1 2479 ? 200.524 263.142 159.125 1.00 34.86 ? 2479 PHE A CG    1 
ATOM   7815  C CD1   . PHE A 1 2479 ? 200.467 264.473 159.502 1.00 34.50 ? 2479 PHE A CD1   1 
ATOM   7816  C CD2   . PHE A 1 2479 ? 200.269 262.814 157.804 1.00 36.34 ? 2479 PHE A CD2   1 
ATOM   7817  C CE1   . PHE A 1 2479 ? 200.157 265.456 158.581 1.00 37.34 ? 2479 PHE A CE1   1 
ATOM   7818  C CE2   . PHE A 1 2479 ? 199.959 263.790 156.879 1.00 36.42 ? 2479 PHE A CE2   1 
ATOM   7819  C CZ    . PHE A 1 2479 ? 199.903 265.113 157.268 1.00 39.83 ? 2479 PHE A CZ    1 
ATOM   7820  N N     . PRO A 1 2480 ? 201.930 261.825 163.704 1.00 35.69 ? 2480 PRO A N     1 
ATOM   7821  C CA    . PRO A 1 2480 ? 201.897 260.822 164.770 1.00 30.83 ? 2480 PRO A CA    1 
ATOM   7822  C C     . PRO A 1 2480 ? 200.463 260.501 165.157 1.00 31.58 ? 2480 PRO A C     1 
ATOM   7823  O O     . PRO A 1 2480 ? 199.554 261.321 165.012 1.00 32.03 ? 2480 PRO A O     1 
ATOM   7824  C CB    . PRO A 1 2480 ? 202.646 261.500 165.919 1.00 28.76 ? 2480 PRO A CB    1 
ATOM   7825  C CG    . PRO A 1 2480 ? 202.372 262.946 165.716 1.00 33.40 ? 2480 PRO A CG    1 
ATOM   7826  C CD    . PRO A 1 2480 ? 202.286 263.159 164.223 1.00 33.05 ? 2480 PRO A CD    1 
ATOM   7827  N N     . MET A 1 2481 ? 200.262 259.279 165.648 1.00 26.53 ? 2481 MET A N     1 
ATOM   7828  C CA    . MET A 1 2481 ? 198.927 258.861 166.065 1.00 26.16 ? 2481 MET A CA    1 
ATOM   7829  C C     . MET A 1 2481 ? 198.492 259.700 167.262 1.00 27.83 ? 2481 MET A C     1 
ATOM   7830  O O     . MET A 1 2481 ? 199.193 259.777 168.277 1.00 28.59 ? 2481 MET A O     1 
ATOM   7831  C CB    . MET A 1 2481 ? 198.891 257.361 166.360 1.00 26.17 ? 2481 MET A CB    1 
ATOM   7832  C CG    . MET A 1 2481 ? 199.378 256.909 167.727 1.00 24.80 ? 2481 MET A CG    1 
ATOM   7833  S SD    . MET A 1 2481 ? 199.300 255.117 167.900 1.00 35.91 ? 2481 MET A SD    1 
ATOM   7834  C CE    . MET A 1 2481 ? 197.600 254.819 167.429 1.00 24.85 ? 2481 MET A CE    1 
ATOM   7835  N N     . GLN A 1 2482 ? 197.362 260.381 167.117 1.00 28.22 ? 2482 GLN A N     1 
ATOM   7836  C CA    . GLN A 1 2482 ? 196.883 261.302 168.136 1.00 28.57 ? 2482 GLN A CA    1 
ATOM   7837  C C     . GLN A 1 2482 ? 196.059 260.540 169.172 1.00 27.11 ? 2482 GLN A C     1 
ATOM   7838  O O     . GLN A 1 2482 ? 196.012 259.308 169.185 1.00 31.66 ? 2482 GLN A O     1 
ATOM   7839  C CB    . GLN A 1 2482 ? 196.097 262.438 167.486 1.00 27.92 ? 2482 GLN A CB    1 
ATOM   7840  C CG    . GLN A 1 2482 ? 196.753 263.011 166.236 1.00 29.23 ? 2482 GLN A CG    1 
ATOM   7841  C CD    . GLN A 1 2482 ? 198.072 263.707 166.524 1.00 31.38 ? 2482 GLN A CD    1 
ATOM   7842  O OE1   . GLN A 1 2482 ? 198.367 264.061 167.666 1.00 31.36 ? 2482 GLN A OE1   1 
ATOM   7843  N NE2   . GLN A 1 2482 ? 198.873 263.907 165.484 1.00 28.84 ? 2482 GLN A NE2   1 
ATOM   7844  N N     . ILE A 1 2483 ? 195.393 261.283 170.058 1.00 26.62 ? 2483 ILE A N     1 
ATOM   7845  C CA    . ILE A 1 2483 ? 194.603 260.661 171.116 1.00 23.95 ? 2483 ILE A CA    1 
ATOM   7846  C C     . ILE A 1 2483 ? 193.417 259.906 170.527 1.00 24.30 ? 2483 ILE A C     1 
ATOM   7847  O O     . ILE A 1 2483 ? 192.980 258.888 171.075 1.00 27.90 ? 2483 ILE A O     1 
ATOM   7848  C CB    . ILE A 1 2483 ? 194.155 261.725 172.135 1.00 25.64 ? 2483 ILE A CB    1 
ATOM   7849  C CG1   . ILE A 1 2483 ? 195.372 262.421 172.744 1.00 27.27 ? 2483 ILE A CG1   1 
ATOM   7850  C CG2   . ILE A 1 2483 ? 193.321 261.098 173.238 1.00 25.00 ? 2483 ILE A CG2   1 
ATOM   7851  C CD1   . ILE A 1 2483 ? 196.297 261.490 173.495 1.00 25.37 ? 2483 ILE A CD1   1 
ATOM   7852  N N     . GLU A 1 2484 ? 192.877 260.388 169.406 1.00 24.85 ? 2484 GLU A N     1 
ATOM   7853  C CA    . GLU A 1 2484 ? 191.710 259.745 168.809 1.00 27.64 ? 2484 GLU A CA    1 
ATOM   7854  C C     . GLU A 1 2484 ? 192.025 258.324 168.355 1.00 28.52 ? 2484 GLU A C     1 
ATOM   7855  O O     . GLU A 1 2484 ? 191.296 257.380 168.682 1.00 27.22 ? 2484 GLU A O     1 
ATOM   7856  C CB    . GLU A 1 2484 ? 191.193 260.582 167.638 1.00 30.23 ? 2484 GLU A CB    1 
ATOM   7857  C CG    . GLU A 1 2484 ? 190.050 259.933 166.878 1.00 30.94 ? 2484 GLU A CG    1 
ATOM   7858  C CD    . GLU A 1 2484 ? 188.832 259.694 167.746 1.00 32.51 ? 2484 GLU A CD    1 
ATOM   7859  O OE1   . GLU A 1 2484 ? 188.621 260.462 168.708 1.00 31.73 ? 2484 GLU A OE1   1 
ATOM   7860  O OE2   . GLU A 1 2484 ? 188.088 258.731 167.467 1.00 29.44 ? 2484 GLU A OE2   1 
ATOM   7861  N N     . GLN A 1 2485 ? 193.103 258.154 167.586 1.00 27.69 ? 2485 GLN A N     1 
ATOM   7862  C CA    . GLN A 1 2485 ? 193.509 256.816 167.165 1.00 23.69 ? 2485 GLN A CA    1 
ATOM   7863  C C     . GLN A 1 2485 ? 193.970 255.974 168.346 1.00 21.75 ? 2485 GLN A C     1 
ATOM   7864  O O     . GLN A 1 2485 ? 193.676 254.773 168.406 1.00 21.87 ? 2485 GLN A O     1 
ATOM   7865  C CB    . GLN A 1 2485 ? 194.618 256.912 166.116 1.00 24.40 ? 2485 GLN A CB    1 
ATOM   7866  C CG    . GLN A 1 2485 ? 194.801 255.672 165.246 1.00 24.38 ? 2485 GLN A CG    1 
ATOM   7867  C CD    . GLN A 1 2485 ? 193.598 255.363 164.375 1.00 24.27 ? 2485 GLN A CD    1 
ATOM   7868  O OE1   . GLN A 1 2485 ? 192.549 254.947 164.865 1.00 23.37 ? 2485 GLN A OE1   1 
ATOM   7869  N NE2   . GLN A 1 2485 ? 193.747 255.566 163.072 1.00 22.08 ? 2485 GLN A NE2   1 
ATOM   7870  N N     . LEU A 1 2486 ? 194.688 256.591 169.287 1.00 19.60 ? 2486 LEU A N     1 
ATOM   7871  C CA    . LEU A 1 2486 ? 195.223 255.864 170.432 1.00 14.02 ? 2486 LEU A CA    1 
ATOM   7872  C C     . LEU A 1 2486 ? 194.108 255.275 171.283 1.00 13.09 ? 2486 LEU A C     1 
ATOM   7873  O O     . LEU A 1 2486 ? 194.215 254.142 171.766 1.00 22.26 ? 2486 LEU A O     1 
ATOM   7874  C CB    . LEU A 1 2486 ? 196.095 256.799 171.267 1.00 14.15 ? 2486 LEU A CB    1 
ATOM   7875  C CG    . LEU A 1 2486 ? 196.978 256.162 172.333 1.00 14.36 ? 2486 LEU A CG    1 
ATOM   7876  C CD1   . LEU A 1 2486 ? 197.823 255.090 171.693 1.00 18.75 ? 2486 LEU A CD1   1 
ATOM   7877  C CD2   . LEU A 1 2486 ? 197.853 257.205 173.000 1.00 17.76 ? 2486 LEU A CD2   1 
ATOM   7878  N N     . GLU A 1 2487 ? 193.032 256.035 171.483 1.00 14.05 ? 2487 GLU A N     1 
ATOM   7879  C CA    . GLU A 1 2487 ? 191.919 255.564 172.300 1.00 16.69 ? 2487 GLU A CA    1 
ATOM   7880  C C     . GLU A 1 2487 ? 191.299 254.306 171.709 1.00 17.25 ? 2487 GLU A C     1 
ATOM   7881  O O     . GLU A 1 2487 ? 191.110 253.301 172.408 1.00 16.80 ? 2487 GLU A O     1 
ATOM   7882  C CB    . GLU A 1 2487 ? 190.878 256.676 172.427 1.00 16.35 ? 2487 GLU A CB    1 
ATOM   7883  C CG    . GLU A 1 2487 ? 189.803 256.430 173.463 1.00 12.85 ? 2487 GLU A CG    1 
ATOM   7884  C CD    . GLU A 1 2487 ? 189.353 257.708 174.143 1.00 21.70 ? 2487 GLU A CD    1 
ATOM   7885  O OE1   . GLU A 1 2487 ? 189.119 257.681 175.370 1.00 23.44 ? 2487 GLU A OE1   1 
ATOM   7886  O OE2   . GLU A 1 2487 ? 189.234 258.740 173.450 1.00 22.80 ? 2487 GLU A OE2   1 
ATOM   7887  N N     . ARG A 1 2488 ? 190.981 254.341 170.412 1.00 16.87 ? 2488 ARG A N     1 
ATOM   7888  C CA    . ARG A 1 2488 ? 190.344 253.195 169.774 1.00 14.23 ? 2488 ARG A CA    1 
ATOM   7889  C C     . ARG A 1 2488 ? 191.303 252.022 169.635 1.00 15.97 ? 2488 ARG A C     1 
ATOM   7890  O O     . ARG A 1 2488 ? 190.863 250.868 169.603 1.00 17.71 ? 2488 ARG A O     1 
ATOM   7891  C CB    . ARG A 1 2488 ? 189.786 253.588 168.407 1.00 15.95 ? 2488 ARG A CB    1 
ATOM   7892  C CG    . ARG A 1 2488 ? 188.385 254.176 168.467 1.00 19.28 ? 2488 ARG A CG    1 
ATOM   7893  C CD    . ARG A 1 2488 ? 187.799 254.545 167.098 1.00 20.97 ? 2488 ARG A CD    1 
ATOM   7894  N NE    . ARG A 1 2488 ? 188.753 255.142 166.169 1.00 24.17 ? 2488 ARG A NE    1 
ATOM   7895  C CZ    . ARG A 1 2488 ? 189.478 254.463 165.291 1.00 18.40 ? 2488 ARG A CZ    1 
ATOM   7896  N NH1   . ARG A 1 2488 ? 189.380 253.149 165.181 1.00 14.39 ? 2488 ARG A NH1   1 
ATOM   7897  N NH2   . ARG A 1 2488 ? 190.318 255.121 164.497 1.00 18.47 ? 2488 ARG A NH2   1 
ATOM   7898  N N     . TYR A 1 2489 ? 192.608 252.288 169.541 1.00 15.85 ? 2489 TYR A N     1 
ATOM   7899  C CA    . TYR A 1 2489 ? 193.573 251.195 169.552 1.00 12.05 ? 2489 TYR A CA    1 
ATOM   7900  C C     . TYR A 1 2489 ? 193.605 250.501 170.907 1.00 12.00 ? 2489 TYR A C     1 
ATOM   7901  O O     . TYR A 1 2489 ? 193.510 249.270 170.988 1.00 15.53 ? 2489 TYR A O     1 
ATOM   7902  C CB    . TYR A 1 2489 ? 194.963 251.711 169.180 1.00 7.35  ? 2489 TYR A CB    1 
ATOM   7903  C CG    . TYR A 1 2489 ? 196.045 250.667 169.316 1.00 9.20  ? 2489 TYR A CG    1 
ATOM   7904  C CD1   . TYR A 1 2489 ? 196.298 249.766 168.296 1.00 11.39 ? 2489 TYR A CD1   1 
ATOM   7905  C CD2   . TYR A 1 2489 ? 196.827 250.592 170.461 1.00 13.68 ? 2489 TYR A CD2   1 
ATOM   7906  C CE1   . TYR A 1 2489 ? 197.282 248.813 168.417 1.00 10.51 ? 2489 TYR A CE1   1 
ATOM   7907  C CE2   . TYR A 1 2489 ? 197.817 249.640 170.587 1.00 13.27 ? 2489 TYR A CE2   1 
ATOM   7908  C CZ    . TYR A 1 2489 ? 198.041 248.753 169.559 1.00 9.80  ? 2489 TYR A CZ    1 
ATOM   7909  O OH    . TYR A 1 2489 ? 199.026 247.801 169.670 1.00 11.66 ? 2489 TYR A OH    1 
ATOM   7910  N N     . ILE A 1 2490 ? 193.731 251.275 171.984 1.00 8.80  ? 2490 ILE A N     1 
ATOM   7911  C CA    . ILE A 1 2490 ? 193.962 250.668 173.289 1.00 6.70  ? 2490 ILE A CA    1 
ATOM   7912  C C     . ILE A 1 2490 ? 192.689 250.071 173.874 1.00 10.13 ? 2490 ILE A C     1 
ATOM   7913  O O     . ILE A 1 2490 ? 192.758 249.084 174.612 1.00 16.09 ? 2490 ILE A O     1 
ATOM   7914  C CB    . ILE A 1 2490 ? 194.614 251.679 174.244 1.00 7.85  ? 2490 ILE A CB    1 
ATOM   7915  C CG1   . ILE A 1 2490 ? 195.891 252.228 173.613 1.00 8.82  ? 2490 ILE A CG1   1 
ATOM   7916  C CG2   . ILE A 1 2490 ? 194.931 251.039 175.583 1.00 9.71  ? 2490 ILE A CG2   1 
ATOM   7917  C CD1   . ILE A 1 2490 ? 196.568 253.261 174.446 1.00 15.41 ? 2490 ILE A CD1   1 
ATOM   7918  N N     . GLN A 1 2491 ? 191.511 250.605 173.542 1.00 10.76 ? 2491 GLN A N     1 
ATOM   7919  C CA    . GLN A 1 2491 ? 190.289 249.953 174.005 1.00 7.12  ? 2491 GLN A CA    1 
ATOM   7920  C C     . GLN A 1 2491 ? 190.197 248.526 173.480 1.00 14.50 ? 2491 GLN A C     1 
ATOM   7921  O O     . GLN A 1 2491 ? 189.816 247.609 174.216 1.00 13.56 ? 2491 GLN A O     1 
ATOM   7922  C CB    . GLN A 1 2491 ? 189.056 250.751 173.585 1.00 11.08 ? 2491 GLN A CB    1 
ATOM   7923  C CG    . GLN A 1 2491 ? 188.891 252.081 174.287 1.00 14.47 ? 2491 GLN A CG    1 
ATOM   7924  C CD    . GLN A 1 2491 ? 187.702 252.856 173.764 1.00 17.50 ? 2491 GLN A CD    1 
ATOM   7925  O OE1   . GLN A 1 2491 ? 186.817 252.294 173.119 1.00 15.22 ? 2491 GLN A OE1   1 
ATOM   7926  N NE2   . GLN A 1 2491 ? 187.666 254.150 174.049 1.00 17.22 ? 2491 GLN A NE2   1 
ATOM   7927  N N     . ARG A 1 2492 ? 190.549 248.319 172.211 1.00 17.19 ? 2492 ARG A N     1 
ATOM   7928  C CA    . ARG A 1 2492 ? 190.497 246.983 171.627 1.00 11.91 ? 2492 ARG A CA    1 
ATOM   7929  C C     . ARG A 1 2492 ? 191.670 246.119 172.076 1.00 9.76  ? 2492 ARG A C     1 
ATOM   7930  O O     . ARG A 1 2492 ? 191.506 244.910 172.289 1.00 8.94  ? 2492 ARG A O     1 
ATOM   7931  C CB    . ARG A 1 2492 ? 190.444 247.088 170.104 1.00 8.78  ? 2492 ARG A CB    1 
ATOM   7932  C CG    . ARG A 1 2492 ? 189.130 247.655 169.593 1.00 9.12  ? 2492 ARG A CG    1 
ATOM   7933  C CD    . ARG A 1 2492 ? 189.152 247.903 168.095 1.00 14.16 ? 2492 ARG A CD    1 
ATOM   7934  N NE    . ARG A 1 2492 ? 187.984 248.651 167.640 1.00 14.88 ? 2492 ARG A NE    1 
ATOM   7935  C CZ    . ARG A 1 2492 ? 187.698 249.901 167.984 1.00 14.85 ? 2492 ARG A CZ    1 
ATOM   7936  N NH1   . ARG A 1 2492 ? 188.493 250.602 168.775 1.00 15.42 ? 2492 ARG A NH1   1 
ATOM   7937  N NH2   . ARG A 1 2492 ? 186.589 250.463 167.514 1.00 15.62 ? 2492 ARG A NH2   1 
ATOM   7938  N N     . TYR A 1 2493 ? 192.857 246.712 172.229 1.00 9.72  ? 2493 TYR A N     1 
ATOM   7939  C CA    . TYR A 1 2493 ? 193.992 245.934 172.711 1.00 7.84  ? 2493 TYR A CA    1 
ATOM   7940  C C     . TYR A 1 2493 ? 193.777 245.460 174.140 1.00 4.49  ? 2493 TYR A C     1 
ATOM   7941  O O     . TYR A 1 2493 ? 194.249 244.383 174.508 1.00 9.89  ? 2493 TYR A O     1 
ATOM   7942  C CB    . TYR A 1 2493 ? 195.286 246.741 172.602 1.00 4.56  ? 2493 TYR A CB    1 
ATOM   7943  C CG    . TYR A 1 2493 ? 196.531 245.879 172.528 1.00 4.59  ? 2493 TYR A CG    1 
ATOM   7944  C CD1   . TYR A 1 2493 ? 196.970 245.156 173.630 1.00 3.08  ? 2493 TYR A CD1   1 
ATOM   7945  C CD2   . TYR A 1 2493 ? 197.254 245.771 171.350 1.00 10.26 ? 2493 TYR A CD2   1 
ATOM   7946  C CE1   . TYR A 1 2493 ? 198.096 244.365 173.567 1.00 0.28  ? 2493 TYR A CE1   1 
ATOM   7947  C CE2   . TYR A 1 2493 ? 198.385 244.980 171.277 1.00 10.97 ? 2493 TYR A CE2   1 
ATOM   7948  C CZ    . TYR A 1 2493 ? 198.799 244.279 172.389 1.00 7.07  ? 2493 TYR A CZ    1 
ATOM   7949  O OH    . TYR A 1 2493 ? 199.923 243.491 172.322 1.00 14.45 ? 2493 TYR A OH    1 
ATOM   7950  N N     . LEU A 1 2494 ? 193.073 246.240 174.961 1.00 6.22  ? 2494 LEU A N     1 
ATOM   7951  C CA    . LEU A 1 2494 ? 192.775 245.788 176.313 1.00 6.03  ? 2494 LEU A CA    1 
ATOM   7952  C C     . LEU A 1 2494 ? 191.936 244.519 176.294 1.00 10.07 ? 2494 LEU A C     1 
ATOM   7953  O O     . LEU A 1 2494 ? 192.222 243.571 177.031 1.00 15.17 ? 2494 LEU A O     1 
ATOM   7954  C CB    . LEU A 1 2494 ? 192.063 246.892 177.092 1.00 7.89  ? 2494 LEU A CB    1 
ATOM   7955  C CG    . LEU A 1 2494 ? 191.766 246.576 178.557 1.00 8.62  ? 2494 LEU A CG    1 
ATOM   7956  C CD1   . LEU A 1 2494 ? 193.035 246.170 179.286 1.00 6.44  ? 2494 LEU A CD1   1 
ATOM   7957  C CD2   . LEU A 1 2494 ? 191.135 247.774 179.221 1.00 7.62  ? 2494 LEU A CD2   1 
ATOM   7958  N N     . VAL A 1 2495 ? 190.907 244.475 175.445 1.00 9.76  ? 2495 VAL A N     1 
ATOM   7959  C CA    . VAL A 1 2495 ? 190.083 243.275 175.330 1.00 8.08  ? 2495 VAL A CA    1 
ATOM   7960  C C     . VAL A 1 2495 ? 190.902 242.113 174.786 1.00 6.54  ? 2495 VAL A C     1 
ATOM   7961  O O     . VAL A 1 2495 ? 190.777 240.975 175.254 1.00 7.40  ? 2495 VAL A O     1 
ATOM   7962  C CB    . VAL A 1 2495 ? 188.851 243.556 174.453 1.00 6.66  ? 2495 VAL A CB    1 
ATOM   7963  C CG1   . VAL A 1 2495 ? 187.899 242.376 174.488 1.00 6.11  ? 2495 VAL A CG1   1 
ATOM   7964  C CG2   . VAL A 1 2495 ? 188.153 244.821 174.913 1.00 10.45 ? 2495 VAL A CG2   1 
ATOM   7965  N N     . TYR A 1 2496 ? 191.747 242.378 173.789 1.00 4.14  ? 2496 TYR A N     1 
ATOM   7966  C CA    . TYR A 1 2496 ? 192.579 241.325 173.211 1.00 3.14  ? 2496 TYR A CA    1 
ATOM   7967  C C     . TYR A 1 2496 ? 193.507 240.722 174.264 1.00 6.12  ? 2496 TYR A C     1 
ATOM   7968  O O     . TYR A 1 2496 ? 193.619 239.495 174.391 1.00 11.06 ? 2496 TYR A O     1 
ATOM   7969  C CB    . TYR A 1 2496 ? 193.369 241.911 172.039 1.00 4.93  ? 2496 TYR A CB    1 
ATOM   7970  C CG    . TYR A 1 2496 ? 194.602 241.153 171.608 1.00 3.16  ? 2496 TYR A CG    1 
ATOM   7971  C CD1   . TYR A 1 2496 ? 194.534 239.817 171.246 1.00 8.37  ? 2496 TYR A CD1   1 
ATOM   7972  C CD2   . TYR A 1 2496 ? 195.836 241.783 171.553 1.00 6.44  ? 2496 TYR A CD2   1 
ATOM   7973  C CE1   . TYR A 1 2496 ? 195.661 239.132 170.840 1.00 12.07 ? 2496 TYR A CE1   1 
ATOM   7974  C CE2   . TYR A 1 2496 ? 196.968 241.104 171.154 1.00 9.54  ? 2496 TYR A CE2   1 
ATOM   7975  C CZ    . TYR A 1 2496 ? 196.875 239.778 170.800 1.00 9.56  ? 2496 TYR A CZ    1 
ATOM   7976  O OH    . TYR A 1 2496 ? 198.000 239.097 170.402 1.00 6.62  ? 2496 TYR A OH    1 
ATOM   7977  N N     . ALA A 1 2497 ? 194.158 241.581 175.052 1.00 5.12  ? 2497 ALA A N     1 
ATOM   7978  C CA    . ALA A 1 2497 ? 195.081 241.115 176.079 1.00 0.65  ? 2497 ALA A CA    1 
ATOM   7979  C C     . ALA A 1 2497 ? 194.345 240.422 177.217 1.00 3.80  ? 2497 ALA A C     1 
ATOM   7980  O O     . ALA A 1 2497 ? 194.847 239.440 177.771 1.00 12.54 ? 2497 ALA A O     1 
ATOM   7981  C CB    . ALA A 1 2497 ? 195.913 242.283 176.604 1.00 0.00  ? 2497 ALA A CB    1 
ATOM   7982  N N     . ILE A 1 2498 ? 193.157 240.910 177.581 1.00 4.33  ? 2498 ILE A N     1 
ATOM   7983  C CA    . ILE A 1 2498 ? 192.353 240.224 178.589 1.00 3.38  ? 2498 ILE A CA    1 
ATOM   7984  C C     . ILE A 1 2498 ? 192.007 238.821 178.118 1.00 3.10  ? 2498 ILE A C     1 
ATOM   7985  O O     . ILE A 1 2498 ? 192.133 237.847 178.868 1.00 6.00  ? 2498 ILE A O     1 
ATOM   7986  C CB    . ILE A 1 2498 ? 191.083 241.035 178.907 1.00 4.56  ? 2498 ILE A CB    1 
ATOM   7987  C CG1   . ILE A 1 2498 ? 191.400 242.213 179.825 1.00 6.82  ? 2498 ILE A CG1   1 
ATOM   7988  C CG2   . ILE A 1 2498 ? 190.025 240.152 179.544 1.00 5.88  ? 2498 ILE A CG2   1 
ATOM   7989  C CD1   . ILE A 1 2498 ? 190.253 243.193 179.947 1.00 11.45 ? 2498 ILE A CD1   1 
ATOM   7990  N N     . LEU A 1 2499 ? 191.578 238.696 176.861 1.00 6.10  ? 2499 LEU A N     1 
ATOM   7991  C CA    . LEU A 1 2499 ? 191.202 237.391 176.330 1.00 5.44  ? 2499 LEU A CA    1 
ATOM   7992  C C     . LEU A 1 2499 ? 192.390 236.441 176.302 1.00 4.40  ? 2499 LEU A C     1 
ATOM   7993  O O     . LEU A 1 2499 ? 192.255 235.260 176.642 1.00 7.20  ? 2499 LEU A O     1 
ATOM   7994  C CB    . LEU A 1 2499 ? 190.611 237.551 174.931 1.00 5.57  ? 2499 LEU A CB    1 
ATOM   7995  C CG    . LEU A 1 2499 ? 189.106 237.801 174.858 1.00 5.85  ? 2499 LEU A CG    1 
ATOM   7996  C CD1   . LEU A 1 2499 ? 188.701 238.112 173.436 1.00 11.25 ? 2499 LEU A CD1   1 
ATOM   7997  C CD2   . LEU A 1 2499 ? 188.341 236.600 175.375 1.00 10.74 ? 2499 LEU A CD2   1 
ATOM   7998  N N     . TRP A 1 2500 ? 193.560 236.929 175.899 1.00 5.09  ? 2500 TRP A N     1 
ATOM   7999  C CA    . TRP A 1 2500 ? 194.710 236.043 175.772 1.00 6.15  ? 2500 TRP A CA    1 
ATOM   8000  C C     . TRP A 1 2500 ? 195.474 235.843 177.075 1.00 5.15  ? 2500 TRP A C     1 
ATOM   8001  O O     . TRP A 1 2500 ? 196.344 234.970 177.135 1.00 8.45  ? 2500 TRP A O     1 
ATOM   8002  C CB    . TRP A 1 2500 ? 195.667 236.552 174.695 1.00 2.24  ? 2500 TRP A CB    1 
ATOM   8003  C CG    . TRP A 1 2500 ? 195.491 235.833 173.403 1.00 8.74  ? 2500 TRP A CG    1 
ATOM   8004  C CD1   . TRP A 1 2500 ? 194.964 236.334 172.253 1.00 6.92  ? 2500 TRP A CD1   1 
ATOM   8005  C CD2   . TRP A 1 2500 ? 195.772 234.452 173.147 1.00 10.53 ? 2500 TRP A CD2   1 
ATOM   8006  N NE1   . TRP A 1 2500 ? 194.942 235.365 171.281 1.00 8.61  ? 2500 TRP A NE1   1 
ATOM   8007  C CE2   . TRP A 1 2500 ? 195.426 234.198 171.808 1.00 6.93  ? 2500 TRP A CE2   1 
ATOM   8008  C CE3   . TRP A 1 2500 ? 196.292 233.407 173.917 1.00 8.60  ? 2500 TRP A CE3   1 
ATOM   8009  C CZ2   . TRP A 1 2500 ? 195.587 232.950 171.223 1.00 8.47  ? 2500 TRP A CZ2   1 
ATOM   8010  C CZ3   . TRP A 1 2500 ? 196.459 232.172 173.332 1.00 9.83  ? 2500 TRP A CZ3   1 
ATOM   8011  C CH2   . TRP A 1 2500 ? 196.105 231.952 171.999 1.00 10.58 ? 2500 TRP A CH2   1 
ATOM   8012  N N     . SER A 1 2501 ? 195.179 236.617 178.114 1.00 2.83  ? 2501 SER A N     1 
ATOM   8013  C CA    . SER A 1 2501 ? 195.835 236.462 179.404 1.00 0.00  ? 2501 SER A CA    1 
ATOM   8014  C C     . SER A 1 2501 ? 194.986 235.722 180.421 1.00 3.21  ? 2501 SER A C     1 
ATOM   8015  O O     . SER A 1 2501 ? 195.518 234.926 181.197 1.00 5.04  ? 2501 SER A O     1 
ATOM   8016  C CB    . SER A 1 2501 ? 196.213 237.835 179.964 1.00 0.00  ? 2501 SER A CB    1 
ATOM   8017  O OG    . SER A 1 2501 ? 195.076 238.504 180.475 1.00 3.20  ? 2501 SER A OG    1 
ATOM   8018  N N     . LEU A 1 2502 ? 193.678 235.962 180.438 1.00 1.34  ? 2502 LEU A N     1 
ATOM   8019  C CA    . LEU A 1 2502 ? 192.775 235.269 181.343 1.00 1.20  ? 2502 LEU A CA    1 
ATOM   8020  C C     . LEU A 1 2502 ? 192.297 233.931 180.797 1.00 8.46  ? 2502 LEU A C     1 
ATOM   8021  O O     . LEU A 1 2502 ? 191.728 233.139 181.555 1.00 6.64  ? 2502 LEU A O     1 
ATOM   8022  C CB    . LEU A 1 2502 ? 191.564 236.154 181.652 1.00 6.89  ? 2502 LEU A CB    1 
ATOM   8023  C CG    . LEU A 1 2502 ? 191.624 237.095 182.857 1.00 3.76  ? 2502 LEU A CG    1 
ATOM   8024  C CD1   . LEU A 1 2502 ? 192.917 237.885 182.893 1.00 4.80  ? 2502 LEU A CD1   1 
ATOM   8025  C CD2   . LEU A 1 2502 ? 190.446 238.036 182.807 1.00 10.54 ? 2502 LEU A CD2   1 
ATOM   8026  N N     . SER A 1 2503 ? 192.506 233.662 179.503 1.00 13.25 ? 2503 SER A N     1 
ATOM   8027  C CA    . SER A 1 2503 ? 192.093 232.394 178.914 1.00 5.31  ? 2503 SER A CA    1 
ATOM   8028  C C     . SER A 1 2503 ? 193.134 231.830 177.955 1.00 2.66  ? 2503 SER A C     1 
ATOM   8029  O O     . SER A 1 2503 ? 192.798 230.976 177.128 1.00 15.80 ? 2503 SER A O     1 
ATOM   8030  C CB    . SER A 1 2503 ? 190.757 232.532 178.181 1.00 10.65 ? 2503 SER A CB    1 
ATOM   8031  O OG    . SER A 1 2503 ? 189.671 232.433 179.084 1.00 22.16 ? 2503 SER A OG    1 
ATOM   8032  N N     . GLY A 1 2504 ? 194.382 232.273 178.044 1.00 7.33  ? 2504 GLY A N     1 
ATOM   8033  C CA    . GLY A 1 2504 ? 195.419 231.718 177.205 1.00 11.35 ? 2504 GLY A CA    1 
ATOM   8034  C C     . GLY A 1 2504 ? 195.948 230.381 177.654 1.00 11.60 ? 2504 GLY A C     1 
ATOM   8035  O O     . GLY A 1 2504 ? 196.813 229.806 176.989 1.00 13.89 ? 2504 GLY A O     1 
ATOM   8036  N N     . ASP A 1 2505 ? 195.451 229.868 178.780 1.00 9.35  ? 2505 ASP A N     1 
ATOM   8037  C CA    . ASP A 1 2505 ? 195.859 228.576 179.314 1.00 8.06  ? 2505 ASP A CA    1 
ATOM   8038  C C     . ASP A 1 2505 ? 194.668 227.636 179.437 1.00 12.84 ? 2505 ASP A C     1 
ATOM   8039  O O     . ASP A 1 2505 ? 194.642 226.770 180.313 1.00 14.67 ? 2505 ASP A O     1 
ATOM   8040  C CB    . ASP A 1 2505 ? 196.548 228.738 180.668 1.00 9.01  ? 2505 ASP A CB    1 
ATOM   8041  C CG    . ASP A 1 2505 ? 195.839 229.732 181.570 1.00 18.27 ? 2505 ASP A CG    1 
ATOM   8042  O OD1   . ASP A 1 2505 ? 196.466 230.204 182.542 1.00 16.78 ? 2505 ASP A OD1   1 
ATOM   8043  O OD2   . ASP A 1 2505 ? 194.657 230.042 181.310 1.00 13.30 ? 2505 ASP A OD2   1 
ATOM   8044  N N     . SER A 1 2506 ? 193.673 227.799 178.572 1.00 8.96  ? 2506 SER A N     1 
ATOM   8045  C CA    . SER A 1 2506 ? 192.452 227.013 178.626 1.00 10.64 ? 2506 SER A CA    1 
ATOM   8046  C C     . SER A 1 2506 ? 192.088 226.546 177.220 1.00 18.17 ? 2506 SER A C     1 
ATOM   8047  O O     . SER A 1 2506 ? 192.707 226.942 176.228 1.00 16.41 ? 2506 SER A O     1 
ATOM   8048  C CB    . SER A 1 2506 ? 191.310 227.819 179.256 1.00 12.99 ? 2506 SER A CB    1 
ATOM   8049  O OG    . SER A 1 2506 ? 191.132 229.056 178.593 1.00 14.75 ? 2506 SER A OG    1 
ATOM   8050  N N     . ARG A 1 2507 ? 191.069 225.693 177.145 1.00 21.02 ? 2507 ARG A N     1 
ATOM   8051  C CA    . ARG A 1 2507 ? 190.623 225.138 175.878 1.00 12.71 ? 2507 ARG A CA    1 
ATOM   8052  C C     . ARG A 1 2507 ? 190.039 226.234 174.989 1.00 15.57 ? 2507 ARG A C     1 
ATOM   8053  O O     . ARG A 1 2507 ? 189.833 227.375 175.409 1.00 21.03 ? 2507 ARG A O     1 
ATOM   8054  C CB    . ARG A 1 2507 ? 189.579 224.047 176.114 1.00 15.22 ? 2507 ARG A CB    1 
ATOM   8055  C CG    . ARG A 1 2507 ? 190.098 222.809 176.823 1.00 17.89 ? 2507 ARG A CG    1 
ATOM   8056  C CD    . ARG A 1 2507 ? 190.852 221.892 175.872 1.00 18.37 ? 2507 ARG A CD    1 
ATOM   8057  N NE    . ARG A 1 2507 ? 192.034 221.300 176.488 1.00 18.91 ? 2507 ARG A NE    1 
ATOM   8058  C CZ    . ARG A 1 2507 ? 192.006 220.370 177.434 1.00 19.95 ? 2507 ARG A CZ    1 
ATOM   8059  N NH1   . ARG A 1 2507 ? 190.865 219.885 177.896 1.00 19.99 ? 2507 ARG A NH1   1 
ATOM   8060  N NH2   . ARG A 1 2507 ? 193.153 219.911 177.925 1.00 19.88 ? 2507 ARG A NH2   1 
ATOM   8061  N N     . LEU A 1 2508 ? 189.769 225.870 173.733 1.00 15.25 ? 2508 LEU A N     1 
ATOM   8062  C CA    . LEU A 1 2508 ? 189.127 226.811 172.821 1.00 19.38 ? 2508 LEU A CA    1 
ATOM   8063  C C     . LEU A 1 2508 ? 187.692 227.104 173.239 1.00 21.48 ? 2508 LEU A C     1 
ATOM   8064  O O     . LEU A 1 2508 ? 187.203 228.222 173.037 1.00 20.84 ? 2508 LEU A O     1 
ATOM   8065  C CB    . LEU A 1 2508 ? 189.163 226.274 171.391 1.00 15.98 ? 2508 LEU A CB    1 
ATOM   8066  C CG    . LEU A 1 2508 ? 189.081 227.335 170.292 1.00 19.81 ? 2508 LEU A CG    1 
ATOM   8067  C CD1   . LEU A 1 2508 ? 190.232 228.324 170.414 1.00 16.50 ? 2508 LEU A CD1   1 
ATOM   8068  C CD2   . LEU A 1 2508 ? 189.062 226.691 168.915 1.00 21.96 ? 2508 LEU A CD2   1 
ATOM   8069  N N     . LYS A 1 2509 ? 187.001 226.117 173.814 1.00 20.02 ? 2509 LYS A N     1 
ATOM   8070  C CA    . LYS A 1 2509 ? 185.647 226.356 174.301 1.00 21.17 ? 2509 LYS A CA    1 
ATOM   8071  C C     . LYS A 1 2509 ? 185.646 227.365 175.441 1.00 22.52 ? 2509 LYS A C     1 
ATOM   8072  O O     . LYS A 1 2509 ? 184.767 228.232 175.514 1.00 20.32 ? 2509 LYS A O     1 
ATOM   8073  C CB    . LYS A 1 2509 ? 185.003 225.044 174.747 1.00 20.88 ? 2509 LYS A CB    1 
ATOM   8074  C CG    . LYS A 1 2509 ? 183.548 225.190 175.166 1.00 21.95 ? 2509 LYS A CG    1 
ATOM   8075  C CD    . LYS A 1 2509 ? 183.113 224.065 176.089 1.00 20.83 ? 2509 LYS A CD    1 
ATOM   8076  C CE    . LYS A 1 2509 ? 183.546 224.330 177.519 1.00 20.23 ? 2509 LYS A CE    1 
ATOM   8077  N NZ    . LYS A 1 2509 ? 183.319 225.749 177.913 1.00 23.73 ? 2509 LYS A NZ    1 
ATOM   8078  N N     . MET A 1 2510 ? 186.623 227.267 176.345 1.00 25.39 ? 2510 MET A N     1 
ATOM   8079  C CA    . MET A 1 2510 ? 186.732 228.240 177.427 1.00 20.34 ? 2510 MET A CA    1 
ATOM   8080  C C     . MET A 1 2510 ? 187.047 229.631 176.889 1.00 23.09 ? 2510 MET A C     1 
ATOM   8081  O O     . MET A 1 2510 ? 186.520 230.631 177.390 1.00 29.62 ? 2510 MET A O     1 
ATOM   8082  C CB    . MET A 1 2510 ? 187.794 227.792 178.428 1.00 17.68 ? 2510 MET A CB    1 
ATOM   8083  C CG    . MET A 1 2510 ? 187.399 226.561 179.224 1.00 22.12 ? 2510 MET A CG    1 
ATOM   8084  S SD    . MET A 1 2510 ? 185.700 226.662 179.822 1.00 32.18 ? 2510 MET A SD    1 
ATOM   8085  C CE    . MET A 1 2510 ? 185.623 225.223 180.883 1.00 18.67 ? 2510 MET A CE    1 
ATOM   8086  N N     . ARG A 1 2511 ? 187.905 229.713 175.869 1.00 16.57 ? 2511 ARG A N     1 
ATOM   8087  C CA    . ARG A 1 2511 ? 188.193 231.000 175.246 1.00 14.82 ? 2511 ARG A CA    1 
ATOM   8088  C C     . ARG A 1 2511 ? 186.936 231.601 174.628 1.00 21.38 ? 2511 ARG A C     1 
ATOM   8089  O O     . ARG A 1 2511 ? 186.677 232.803 174.768 1.00 21.79 ? 2511 ARG A O     1 
ATOM   8090  C CB    . ARG A 1 2511 ? 189.281 230.831 174.187 1.00 14.39 ? 2511 ARG A CB    1 
ATOM   8091  C CG    . ARG A 1 2511 ? 190.631 230.429 174.745 1.00 13.84 ? 2511 ARG A CG    1 
ATOM   8092  C CD    . ARG A 1 2511 ? 191.716 230.517 173.687 1.00 17.19 ? 2511 ARG A CD    1 
ATOM   8093  N NE    . ARG A 1 2511 ? 193.025 230.162 174.222 1.00 16.72 ? 2511 ARG A NE    1 
ATOM   8094  C CZ    . ARG A 1 2511 ? 193.933 229.450 173.570 1.00 14.05 ? 2511 ARG A CZ    1 
ATOM   8095  N NH1   . ARG A 1 2511 ? 193.719 229.019 172.339 1.00 17.73 ? 2511 ARG A NH1   1 
ATOM   8096  N NH2   . ARG A 1 2511 ? 195.087 229.167 174.166 1.00 12.94 ? 2511 ARG A NH2   1 
ATOM   8097  N N     . ALA A 1 2512 ? 186.140 230.775 173.944 1.00 23.69 ? 2512 ALA A N     1 
ATOM   8098  C CA    . ALA A 1 2512 ? 184.895 231.258 173.356 1.00 24.75 ? 2512 ALA A CA    1 
ATOM   8099  C C     . ALA A 1 2512 ? 183.912 231.701 174.431 1.00 27.37 ? 2512 ALA A C     1 
ATOM   8100  O O     . ALA A 1 2512 ? 183.202 232.698 174.260 1.00 29.11 ? 2512 ALA A O     1 
ATOM   8101  C CB    . ALA A 1 2512 ? 184.276 230.176 172.474 1.00 22.73 ? 2512 ALA A CB    1 
ATOM   8102  N N     . GLU A 1 2513 ? 183.846 230.964 175.542 1.00 20.53 ? 2513 GLU A N     1 
ATOM   8103  C CA    . GLU A 1 2513 ? 182.967 231.354 176.640 1.00 21.22 ? 2513 GLU A CA    1 
ATOM   8104  C C     . GLU A 1 2513 ? 183.384 232.693 177.233 1.00 23.71 ? 2513 GLU A C     1 
ATOM   8105  O O     . GLU A 1 2513 ? 182.535 233.549 177.514 1.00 25.53 ? 2513 GLU A O     1 
ATOM   8106  C CB    . GLU A 1 2513 ? 182.965 230.272 177.718 1.00 24.03 ? 2513 GLU A CB    1 
ATOM   8107  C CG    . GLU A 1 2513 ? 182.060 230.579 178.897 1.00 23.29 ? 2513 GLU A CG    1 
ATOM   8108  C CD    . GLU A 1 2513 ? 181.619 229.330 179.628 1.00 27.99 ? 2513 GLU A CD    1 
ATOM   8109  O OE1   . GLU A 1 2513 ? 180.875 229.454 180.624 1.00 26.75 ? 2513 GLU A OE1   1 
ATOM   8110  O OE2   . GLU A 1 2513 ? 182.016 228.223 179.208 1.00 26.91 ? 2513 GLU A OE2   1 
ATOM   8111  N N     . LEU A 1 2514 ? 184.690 232.893 177.435 1.00 19.92 ? 2514 LEU A N     1 
ATOM   8112  C CA    . LEU A 1 2514 ? 185.158 234.170 177.961 1.00 18.03 ? 2514 LEU A CA    1 
ATOM   8113  C C     . LEU A 1 2514 ? 184.867 235.300 176.984 1.00 18.90 ? 2514 LEU A C     1 
ATOM   8114  O O     . LEU A 1 2514 ? 184.473 236.397 177.394 1.00 24.43 ? 2514 LEU A O     1 
ATOM   8115  C CB    . LEU A 1 2514 ? 186.652 234.111 178.279 1.00 19.69 ? 2514 LEU A CB    1 
ATOM   8116  C CG    . LEU A 1 2514 ? 187.223 235.452 178.754 1.00 21.02 ? 2514 LEU A CG    1 
ATOM   8117  C CD1   . LEU A 1 2514 ? 186.623 235.840 180.096 1.00 21.15 ? 2514 LEU A CD1   1 
ATOM   8118  C CD2   . LEU A 1 2514 ? 188.739 235.440 178.831 1.00 13.52 ? 2514 LEU A CD2   1 
ATOM   8119  N N     . GLY A 1 2515 ? 185.048 235.051 175.686 1.00 17.66 ? 2515 GLY A N     1 
ATOM   8120  C CA    . GLY A 1 2515 ? 184.717 236.068 174.700 1.00 23.94 ? 2515 GLY A CA    1 
ATOM   8121  C C     . GLY A 1 2515 ? 183.241 236.417 174.691 1.00 24.97 ? 2515 GLY A C     1 
ATOM   8122  O O     . GLY A 1 2515 ? 182.870 237.589 174.581 1.00 24.67 ? 2515 GLY A O     1 
ATOM   8123  N N     . GLU A 1 2516 ? 182.378 235.405 174.806 1.00 24.92 ? 2516 GLU A N     1 
ATOM   8124  C CA    . GLU A 1 2516 ? 180.940 235.653 174.839 1.00 26.26 ? 2516 GLU A CA    1 
ATOM   8125  C C     . GLU A 1 2516 ? 180.544 236.436 176.083 1.00 27.40 ? 2516 GLU A C     1 
ATOM   8126  O O     . GLU A 1 2516 ? 179.697 237.334 176.016 1.00 31.42 ? 2516 GLU A O     1 
ATOM   8127  C CB    . GLU A 1 2516 ? 180.176 234.332 174.768 1.00 26.84 ? 2516 GLU A CB    1 
ATOM   8128  C CG    . GLU A 1 2516 ? 180.202 233.673 173.396 1.00 31.30 ? 2516 GLU A CG    1 
ATOM   8129  C CD    . GLU A 1 2516 ? 180.274 234.681 172.263 1.00 35.24 ? 2516 GLU A CD    1 
ATOM   8130  O OE1   . GLU A 1 2516 ? 179.265 235.374 172.015 1.00 31.00 ? 2516 GLU A OE1   1 
ATOM   8131  O OE2   . GLU A 1 2516 ? 181.341 234.781 171.621 1.00 36.87 ? 2516 GLU A OE2   1 
ATOM   8132  N N     . TYR A 1 2517 ? 181.140 236.106 177.232 1.00 24.98 ? 2517 TYR A N     1 
ATOM   8133  C CA    . TYR A 1 2517 ? 180.875 236.879 178.442 1.00 23.44 ? 2517 TYR A CA    1 
ATOM   8134  C C     . TYR A 1 2517 ? 181.365 238.314 178.299 1.00 25.80 ? 2517 TYR A C     1 
ATOM   8135  O O     . TYR A 1 2517 ? 180.698 239.252 178.748 1.00 29.22 ? 2517 TYR A O     1 
ATOM   8136  C CB    . TYR A 1 2517 ? 181.523 236.216 179.655 1.00 24.91 ? 2517 TYR A CB    1 
ATOM   8137  C CG    . TYR A 1 2517 ? 181.138 236.871 180.961 1.00 26.94 ? 2517 TYR A CG    1 
ATOM   8138  C CD1   . TYR A 1 2517 ? 179.891 236.653 181.529 1.00 27.98 ? 2517 TYR A CD1   1 
ATOM   8139  C CD2   . TYR A 1 2517 ? 182.020 237.715 181.622 1.00 25.91 ? 2517 TYR A CD2   1 
ATOM   8140  C CE1   . TYR A 1 2517 ? 179.535 237.253 182.721 1.00 28.52 ? 2517 TYR A CE1   1 
ATOM   8141  C CE2   . TYR A 1 2517 ? 181.673 238.319 182.813 1.00 27.15 ? 2517 TYR A CE2   1 
ATOM   8142  C CZ    . TYR A 1 2517 ? 180.430 238.086 183.358 1.00 27.68 ? 2517 TYR A CZ    1 
ATOM   8143  O OH    . TYR A 1 2517 ? 180.082 238.687 184.546 1.00 27.51 ? 2517 TYR A OH    1 
ATOM   8144  N N     . ILE A 1 2518 ? 182.534 238.502 177.684 1.00 24.53 ? 2518 ILE A N     1 
ATOM   8145  C CA    . ILE A 1 2518 ? 183.067 239.845 177.486 1.00 24.42 ? 2518 ILE A CA    1 
ATOM   8146  C C     . ILE A 1 2518 ? 182.139 240.655 176.592 1.00 27.64 ? 2518 ILE A C     1 
ATOM   8147  O O     . ILE A 1 2518 ? 181.887 241.839 176.845 1.00 26.73 ? 2518 ILE A O     1 
ATOM   8148  C CB    . ILE A 1 2518 ? 184.493 239.770 176.908 1.00 21.49 ? 2518 ILE A CB    1 
ATOM   8149  C CG1   . ILE A 1 2518 ? 185.502 239.472 178.018 1.00 22.96 ? 2518 ILE A CG1   1 
ATOM   8150  C CG2   . ILE A 1 2518 ? 184.857 241.062 176.193 1.00 22.77 ? 2518 ILE A CG2   1 
ATOM   8151  C CD1   . ILE A 1 2518 ? 185.808 240.657 178.902 1.00 27.27 ? 2518 ILE A CD1   1 
ATOM   8152  N N     . ARG A 1 2519 ? 181.599 240.024 175.545 1.00 28.45 ? 2519 ARG A N     1 
ATOM   8153  C CA    . ARG A 1 2519 ? 180.752 240.738 174.594 1.00 26.52 ? 2519 ARG A CA    1 
ATOM   8154  C C     . ARG A 1 2519 ? 179.536 241.365 175.264 1.00 31.43 ? 2519 ARG A C     1 
ATOM   8155  O O     . ARG A 1 2519 ? 179.095 242.446 174.857 1.00 34.12 ? 2519 ARG A O     1 
ATOM   8156  C CB    . ARG A 1 2519 ? 180.311 239.795 173.474 1.00 26.00 ? 2519 ARG A CB    1 
ATOM   8157  C CG    . ARG A 1 2519 ? 179.497 240.471 172.378 1.00 29.80 ? 2519 ARG A CG    1 
ATOM   8158  C CD    . ARG A 1 2519 ? 179.062 239.484 171.302 1.00 31.81 ? 2519 ARG A CD    1 
ATOM   8159  N NE    . ARG A 1 2519 ? 180.188 238.828 170.647 1.00 32.71 ? 2519 ARG A NE    1 
ATOM   8160  C CZ    . ARG A 1 2519 ? 181.041 239.431 169.829 1.00 32.99 ? 2519 ARG A CZ    1 
ATOM   8161  N NH1   . ARG A 1 2519 ? 180.919 240.712 169.522 1.00 29.69 ? 2519 ARG A NH1   1 
ATOM   8162  N NH2   . ARG A 1 2519 ? 182.037 238.728 169.298 1.00 30.87 ? 2519 ARG A NH2   1 
ATOM   8163  N N     . ARG A 1 2520 ? 178.987 240.720 176.288 1.00 26.55 ? 2520 ARG A N     1 
ATOM   8164  C CA    . ARG A 1 2520 ? 177.776 241.208 176.930 1.00 28.42 ? 2520 ARG A CA    1 
ATOM   8165  C C     . ARG A 1 2520 ? 178.047 242.139 178.106 1.00 29.33 ? 2520 ARG A C     1 
ATOM   8166  O O     . ARG A 1 2520 ? 177.092 242.628 178.717 1.00 31.21 ? 2520 ARG A O     1 
ATOM   8167  C CB    . ARG A 1 2520 ? 176.912 240.029 177.392 1.00 28.21 ? 2520 ARG A CB    1 
ATOM   8168  C CG    . ARG A 1 2520 ? 177.440 239.306 178.615 1.00 30.03 ? 2520 ARG A CG    1 
ATOM   8169  C CD    . ARG A 1 2520 ? 176.542 238.141 178.992 1.00 30.52 ? 2520 ARG A CD    1 
ATOM   8170  N NE    . ARG A 1 2520 ? 175.139 238.532 179.056 1.00 32.01 ? 2520 ARG A NE    1 
ATOM   8171  C CZ    . ARG A 1 2520 ? 174.584 239.172 180.076 1.00 31.62 ? 2520 ARG A CZ    1 
ATOM   8172  N NH1   . ARG A 1 2520 ? 175.286 239.510 181.145 1.00 29.18 ? 2520 ARG A NH1   1 
ATOM   8173  N NH2   . ARG A 1 2520 ? 173.291 239.479 180.023 1.00 30.85 ? 2520 ARG A NH2   1 
ATOM   8174  N N     . ILE A 1 2521 ? 179.313 242.401 178.439 1.00 26.72 ? 2521 ILE A N     1 
ATOM   8175  C CA    . ILE A 1 2521 ? 179.652 243.264 179.564 1.00 25.52 ? 2521 ILE A CA    1 
ATOM   8176  C C     . ILE A 1 2521 ? 180.572 244.411 179.179 1.00 26.04 ? 2521 ILE A C     1 
ATOM   8177  O O     . ILE A 1 2521 ? 180.882 245.248 180.029 1.00 28.24 ? 2521 ILE A O     1 
ATOM   8178  C CB    . ILE A 1 2521 ? 180.276 242.461 180.726 1.00 26.11 ? 2521 ILE A CB    1 
ATOM   8179  C CG1   . ILE A 1 2521 ? 181.722 242.085 180.398 1.00 26.16 ? 2521 ILE A CG1   1 
ATOM   8180  C CG2   . ILE A 1 2521 ? 179.445 241.226 181.043 1.00 25.36 ? 2521 ILE A CG2   1 
ATOM   8181  C CD1   . ILE A 1 2521 ? 182.490 241.535 181.574 1.00 22.48 ? 2521 ILE A CD1   1 
ATOM   8182  N N     . THR A 1 2522 ? 181.024 244.488 177.932 1.00 25.34 ? 2522 THR A N     1 
ATOM   8183  C CA    . THR A 1 2522 ? 181.964 245.519 177.522 1.00 23.29 ? 2522 THR A CA    1 
ATOM   8184  C C     . THR A 1 2522 ? 181.255 246.614 176.736 1.00 25.01 ? 2522 THR A C     1 
ATOM   8185  O O     . THR A 1 2522 ? 180.140 246.439 176.239 1.00 24.57 ? 2522 THR A O     1 
ATOM   8186  C CB    . THR A 1 2522 ? 183.097 244.937 176.671 1.00 23.51 ? 2522 THR A CB    1 
ATOM   8187  O OG1   . THR A 1 2522 ? 184.085 245.949 176.439 1.00 26.04 ? 2522 THR A OG1   1 
ATOM   8188  C CG2   . THR A 1 2522 ? 182.563 244.470 175.330 1.00 22.10 ? 2522 THR A CG2   1 
ATOM   8189  N N     . THR A 1 2523 ? 181.928 247.763 176.640 1.00 24.75 ? 2523 THR A N     1 
ATOM   8190  C CA    . THR A 1 2523 ? 181.496 248.864 175.787 1.00 22.65 ? 2523 THR A CA    1 
ATOM   8191  C C     . THR A 1 2523 ? 182.510 249.142 174.685 1.00 24.42 ? 2523 THR A C     1 
ATOM   8192  O O     . THR A 1 2523 ? 182.376 250.128 173.953 1.00 24.58 ? 2523 THR A O     1 
ATOM   8193  C CB    . THR A 1 2523 ? 181.250 250.128 176.614 1.00 23.83 ? 2523 THR A CB    1 
ATOM   8194  O OG1   . THR A 1 2523 ? 182.419 250.433 177.385 1.00 26.95 ? 2523 THR A OG1   1 
ATOM   8195  C CG2   . THR A 1 2523 ? 180.067 249.930 177.550 1.00 23.54 ? 2523 THR A CG2   1 
ATOM   8196  N N     . VAL A 1 2524 ? 183.521 248.295 174.560 1.00 23.61 ? 2524 VAL A N     1 
ATOM   8197  C CA    . VAL A 1 2524 ? 184.540 248.413 173.521 1.00 23.42 ? 2524 VAL A CA    1 
ATOM   8198  C C     . VAL A 1 2524 ? 183.979 247.807 172.239 1.00 22.55 ? 2524 VAL A C     1 
ATOM   8199  O O     . VAL A 1 2524 ? 183.439 246.693 172.285 1.00 23.37 ? 2524 VAL A O     1 
ATOM   8200  C CB    . VAL A 1 2524 ? 185.847 247.708 173.930 1.00 22.27 ? 2524 VAL A CB    1 
ATOM   8201  C CG1   . VAL A 1 2524 ? 186.826 247.678 172.768 1.00 20.48 ? 2524 VAL A CG1   1 
ATOM   8202  C CG2   . VAL A 1 2524 ? 186.464 248.394 175.137 1.00 17.20 ? 2524 VAL A CG2   1 
ATOM   8203  N N     . PRO A 1 2525 ? 184.058 248.500 171.103 1.00 20.19 ? 2525 PRO A N     1 
ATOM   8204  C CA    . PRO A 1 2525 ? 183.563 247.920 169.845 1.00 17.82 ? 2525 PRO A CA    1 
ATOM   8205  C C     . PRO A 1 2525 ? 184.281 246.619 169.519 1.00 20.68 ? 2525 PRO A C     1 
ATOM   8206  O O     . PRO A 1 2525 ? 185.512 246.549 169.513 1.00 21.24 ? 2525 PRO A O     1 
ATOM   8207  C CB    . PRO A 1 2525 ? 183.864 249.013 168.813 1.00 20.40 ? 2525 PRO A CB    1 
ATOM   8208  C CG    . PRO A 1 2525 ? 183.935 250.274 169.610 1.00 21.60 ? 2525 PRO A CG    1 
ATOM   8209  C CD    . PRO A 1 2525 ? 184.534 249.882 170.926 1.00 21.92 ? 2525 PRO A CD    1 
ATOM   8210  N N     . LEU A 1 2526 ? 183.498 245.588 169.246 1.00 26.74 ? 2526 LEU A N     1 
ATOM   8211  C CA    . LEU A 1 2526 ? 183.971 244.238 169.005 1.00 24.85 ? 2526 LEU A CA    1 
ATOM   8212  C C     . LEU A 1 2526 ? 183.785 243.846 167.544 1.00 27.77 ? 2526 LEU A C     1 
ATOM   8213  O O     . LEU A 1 2526 ? 183.158 244.574 166.767 1.00 26.28 ? 2526 LEU A O     1 
ATOM   8214  C CB    . LEU A 1 2526 ? 183.226 243.259 169.918 1.00 23.10 ? 2526 LEU A CB    1 
ATOM   8215  C CG    . LEU A 1 2526 ? 183.570 243.390 171.401 1.00 25.83 ? 2526 LEU A CG    1 
ATOM   8216  C CD1   . LEU A 1 2526 ? 182.746 242.419 172.213 1.00 25.21 ? 2526 LEU A CD1   1 
ATOM   8217  C CD2   . LEU A 1 2526 ? 185.056 243.164 171.635 1.00 22.85 ? 2526 LEU A CD2   1 
ATOM   8218  N N     . PRO A 1 2527 ? 184.348 242.710 167.126 1.00 30.98 ? 2527 PRO A N     1 
ATOM   8219  C CA    . PRO A 1 2527 ? 184.128 242.241 165.753 1.00 28.43 ? 2527 PRO A CA    1 
ATOM   8220  C C     . PRO A 1 2527 ? 182.646 242.162 165.416 1.00 31.22 ? 2527 PRO A C     1 
ATOM   8221  O O     . PRO A 1 2527 ? 181.830 241.691 166.211 1.00 32.69 ? 2527 PRO A O     1 
ATOM   8222  C CB    . PRO A 1 2527 ? 184.775 240.852 165.743 1.00 25.91 ? 2527 PRO A CB    1 
ATOM   8223  C CG    . PRO A 1 2527 ? 185.697 240.816 166.924 1.00 25.90 ? 2527 PRO A CG    1 
ATOM   8224  C CD    . PRO A 1 2527 ? 185.509 242.049 167.748 1.00 25.99 ? 2527 PRO A CD    1 
ATOM   8225  N N     . THR A 1 2528 ? 182.304 242.641 164.218 1.00 32.51 ? 2528 THR A N     1 
ATOM   8226  C CA    . THR A 1 2528 ? 180.907 242.674 163.799 1.00 30.30 ? 2528 THR A CA    1 
ATOM   8227  C C     . THR A 1 2528 ? 180.343 241.269 163.630 1.00 32.67 ? 2528 THR A C     1 
ATOM   8228  O O     . THR A 1 2528 ? 179.200 241.003 164.020 1.00 31.79 ? 2528 THR A O     1 
ATOM   8229  C CB    . THR A 1 2528 ? 180.770 243.469 162.500 1.00 32.28 ? 2528 THR A CB    1 
ATOM   8230  O OG1   . THR A 1 2528 ? 181.253 244.803 162.703 1.00 33.32 ? 2528 THR A OG1   1 
ATOM   8231  C CG2   . THR A 1 2528 ? 179.316 243.528 162.057 1.00 34.37 ? 2528 THR A CG2   1 
ATOM   8232  N N     . ALA A 1 2529 ? 181.124 240.362 163.061 1.00 33.54 ? 2529 ALA A N     1 
ATOM   8233  C CA    . ALA A 1 2529 ? 180.643 239.011 162.799 1.00 33.59 ? 2529 ALA A CA    1 
ATOM   8234  C C     . ALA A 1 2529 ? 180.438 238.264 164.110 1.00 39.52 ? 2529 ALA A C     1 
ATOM   8235  O O     . ALA A 1 2529 ? 181.397 238.104 164.877 1.00 41.91 ? 2529 ALA A O     1 
ATOM   8236  C CB    . ALA A 1 2529 ? 181.630 238.261 161.910 1.00 31.85 ? 2529 ALA A CB    1 
ATOM   8237  N N     . PRO A 1 2530 ? 179.224 237.790 164.408 1.00 46.75 ? 2530 PRO A N     1 
ATOM   8238  C CA    . PRO A 1 2530 ? 179.009 237.077 165.675 1.00 44.75 ? 2530 PRO A CA    1 
ATOM   8239  C C     . PRO A 1 2530 ? 179.423 235.618 165.638 1.00 42.38 ? 2530 PRO A C     1 
ATOM   8240  O O     . PRO A 1 2530 ? 179.619 235.024 166.708 1.00 42.31 ? 2530 PRO A O     1 
ATOM   8241  C CB    . PRO A 1 2530 ? 177.497 237.212 165.893 1.00 42.88 ? 2530 PRO A CB    1 
ATOM   8242  C CG    . PRO A 1 2530 ? 176.943 237.254 164.504 1.00 41.65 ? 2530 PRO A CG    1 
ATOM   8243  C CD    . PRO A 1 2530 ? 177.973 237.961 163.649 1.00 42.18 ? 2530 PRO A CD    1 
ATOM   8244  N N     . ASN A 1 2531 ? 179.565 235.023 164.454 1.00 36.92 ? 2531 ASN A N     1 
ATOM   8245  C CA    . ASN A 1 2531 ? 179.877 233.605 164.342 1.00 41.00 ? 2531 ASN A CA    1 
ATOM   8246  C C     . ASN A 1 2531 ? 181.358 233.296 164.520 1.00 40.23 ? 2531 ASN A C     1 
ATOM   8247  O O     . ASN A 1 2531 ? 181.723 232.117 164.575 1.00 39.55 ? 2531 ASN A O     1 
ATOM   8248  C CB    . ASN A 1 2531 ? 179.402 233.073 162.987 1.00 41.15 ? 2531 ASN A CB    1 
ATOM   8249  C CG    . ASN A 1 2531 ? 179.704 234.029 161.848 1.00 44.14 ? 2531 ASN A CG    1 
ATOM   8250  O OD1   . ASN A 1 2531 ? 180.745 234.686 161.832 1.00 43.93 ? 2531 ASN A OD1   1 
ATOM   8251  N ND2   . ASN A 1 2531 ? 178.789 234.113 160.889 1.00 42.91 ? 2531 ASN A ND2   1 
ATOM   8252  N N     . ILE A 1 2532 ? 182.209 234.306 164.612 1.00 32.13 ? 2532 ILE A N     1 
ATOM   8253  C CA    . ILE A 1 2532 ? 183.652 234.125 164.758 1.00 32.97 ? 2532 ILE A CA    1 
ATOM   8254  C C     . ILE A 1 2532 ? 184.061 234.660 166.124 1.00 33.78 ? 2532 ILE A C     1 
ATOM   8255  O O     . ILE A 1 2532 ? 183.716 235.799 166.458 1.00 30.90 ? 2532 ILE A O     1 
ATOM   8256  C CB    . ILE A 1 2532 ? 184.436 234.836 163.639 1.00 35.34 ? 2532 ILE A CB    1 
ATOM   8257  C CG1   . ILE A 1 2532 ? 184.010 234.300 162.273 1.00 34.32 ? 2532 ILE A CG1   1 
ATOM   8258  C CG2   . ILE A 1 2532 ? 185.929 234.638 163.830 1.00 33.71 ? 2532 ILE A CG2   1 
ATOM   8259  C CD1   . ILE A 1 2532 ? 184.271 232.822 162.092 1.00 33.77 ? 2532 ILE A CD1   1 
ATOM   8260  N N     . PRO A 1 2533 ? 184.778 233.882 166.936 1.00 31.47 ? 2533 PRO A N     1 
ATOM   8261  C CA    . PRO A 1 2533 ? 185.177 234.366 168.262 1.00 26.55 ? 2533 PRO A CA    1 
ATOM   8262  C C     . PRO A 1 2533 ? 186.127 235.550 168.173 1.00 26.10 ? 2533 PRO A C     1 
ATOM   8263  O O     . PRO A 1 2533 ? 186.869 235.709 167.202 1.00 28.41 ? 2533 PRO A O     1 
ATOM   8264  C CB    . PRO A 1 2533 ? 185.866 233.149 168.890 1.00 23.71 ? 2533 PRO A CB    1 
ATOM   8265  C CG    . PRO A 1 2533 ? 185.319 231.977 168.150 1.00 21.97 ? 2533 PRO A CG    1 
ATOM   8266  C CD    . PRO A 1 2533 ? 185.093 232.457 166.748 1.00 24.11 ? 2533 PRO A CD    1 
ATOM   8267  N N     . ILE A 1 2534 ? 186.092 236.389 169.212 1.00 21.52 ? 2534 ILE A N     1 
ATOM   8268  C CA    . ILE A 1 2534 ? 186.994 237.536 169.283 1.00 19.86 ? 2534 ILE A CA    1 
ATOM   8269  C C     . ILE A 1 2534 ? 188.442 237.076 169.356 1.00 15.98 ? 2534 ILE A C     1 
ATOM   8270  O O     . ILE A 1 2534 ? 189.359 237.809 168.968 1.00 17.08 ? 2534 ILE A O     1 
ATOM   8271  C CB    . ILE A 1 2534 ? 186.628 238.427 170.486 1.00 21.11 ? 2534 ILE A CB    1 
ATOM   8272  C CG1   . ILE A 1 2534 ? 185.124 238.690 170.525 1.00 24.36 ? 2534 ILE A CG1   1 
ATOM   8273  C CG2   . ILE A 1 2534 ? 187.378 239.748 170.424 1.00 18.81 ? 2534 ILE A CG2   1 
ATOM   8274  C CD1   . ILE A 1 2534 ? 184.648 239.268 171.838 1.00 19.75 ? 2534 ILE A CD1   1 
ATOM   8275  N N     . ILE A 1 2535 ? 188.671 235.853 169.842 1.00 13.85 ? 2535 ILE A N     1 
ATOM   8276  C CA    . ILE A 1 2535 ? 190.028 235.338 170.000 1.00 14.50 ? 2535 ILE A CA    1 
ATOM   8277  C C     . ILE A 1 2535 ? 190.710 235.174 168.647 1.00 20.87 ? 2535 ILE A C     1 
ATOM   8278  O O     . ILE A 1 2535 ? 191.936 235.023 168.573 1.00 18.03 ? 2535 ILE A O     1 
ATOM   8279  C CB    . ILE A 1 2535 ? 189.987 234.010 170.784 1.00 13.18 ? 2535 ILE A CB    1 
ATOM   8280  C CG1   . ILE A 1 2535 ? 191.380 233.613 171.272 1.00 12.11 ? 2535 ILE A CG1   1 
ATOM   8281  C CG2   . ILE A 1 2535 ? 189.384 232.905 169.933 1.00 15.64 ? 2535 ILE A CG2   1 
ATOM   8282  C CD1   . ILE A 1 2535 ? 191.946 234.554 172.306 1.00 13.38 ? 2535 ILE A CD1   1 
ATOM   8283  N N     . ASP A 1 2536 ? 189.940 235.213 167.558 1.00 22.33 ? 2536 ASP A N     1 
ATOM   8284  C CA    . ASP A 1 2536 ? 190.463 235.034 166.210 1.00 14.06 ? 2536 ASP A CA    1 
ATOM   8285  C C     . ASP A 1 2536 ? 190.863 236.343 165.539 1.00 14.78 ? 2536 ASP A C     1 
ATOM   8286  O O     . ASP A 1 2536 ? 191.272 236.318 164.373 1.00 21.31 ? 2536 ASP A O     1 
ATOM   8287  C CB    . ASP A 1 2536 ? 189.434 234.308 165.340 1.00 15.25 ? 2536 ASP A CB    1 
ATOM   8288  C CG    . ASP A 1 2536 ? 189.238 232.864 165.752 1.00 21.00 ? 2536 ASP A CG    1 
ATOM   8289  O OD1   . ASP A 1 2536 ? 190.195 232.256 166.272 1.00 21.04 ? 2536 ASP A OD1   1 
ATOM   8290  O OD2   . ASP A 1 2536 ? 188.124 232.337 165.556 1.00 25.99 ? 2536 ASP A OD2   1 
ATOM   8291  N N     . TYR A 1 2537 ? 190.768 237.477 166.229 1.00 14.05 ? 2537 TYR A N     1 
ATOM   8292  C CA    . TYR A 1 2537 ? 191.041 238.770 165.623 1.00 17.01 ? 2537 TYR A CA    1 
ATOM   8293  C C     . TYR A 1 2537 ? 192.280 239.404 166.237 1.00 13.28 ? 2537 TYR A C     1 
ATOM   8294  O O     . TYR A 1 2537 ? 192.769 238.989 167.289 1.00 16.40 ? 2537 TYR A O     1 
ATOM   8295  C CB    . TYR A 1 2537 ? 189.851 239.729 165.763 1.00 17.79 ? 2537 TYR A CB    1 
ATOM   8296  C CG    . TYR A 1 2537 ? 188.606 239.271 165.043 1.00 18.12 ? 2537 TYR A CG    1 
ATOM   8297  C CD1   . TYR A 1 2537 ? 188.260 239.808 163.811 1.00 11.87 ? 2537 TYR A CD1   1 
ATOM   8298  C CD2   . TYR A 1 2537 ? 187.777 238.306 165.592 1.00 19.73 ? 2537 TYR A CD2   1 
ATOM   8299  C CE1   . TYR A 1 2537 ? 187.126 239.396 163.148 1.00 17.71 ? 2537 TYR A CE1   1 
ATOM   8300  C CE2   . TYR A 1 2537 ? 186.640 237.888 164.936 1.00 18.74 ? 2537 TYR A CE2   1 
ATOM   8301  C CZ    . TYR A 1 2537 ? 186.320 238.435 163.714 1.00 20.69 ? 2537 TYR A CZ    1 
ATOM   8302  O OH    . TYR A 1 2537 ? 185.186 238.020 163.057 1.00 26.05 ? 2537 TYR A OH    1 
ATOM   8303  N N     . GLU A 1 2538 ? 192.778 240.424 165.546 1.00 6.84  ? 2538 GLU A N     1 
ATOM   8304  C CA    . GLU A 1 2538 ? 193.937 241.194 165.962 1.00 5.10  ? 2538 GLU A CA    1 
ATOM   8305  C C     . GLU A 1 2538 ? 193.571 242.672 165.950 1.00 18.18 ? 2538 GLU A C     1 
ATOM   8306  O O     . GLU A 1 2538 ? 192.685 243.099 165.206 1.00 21.67 ? 2538 GLU A O     1 
ATOM   8307  C CB    . GLU A 1 2538 ? 195.134 240.929 165.038 1.00 5.07  ? 2538 GLU A CB    1 
ATOM   8308  C CG    . GLU A 1 2538 ? 196.453 241.483 165.531 1.00 8.98  ? 2538 GLU A CG    1 
ATOM   8309  C CD    . GLU A 1 2538 ? 197.414 241.761 164.396 1.00 14.37 ? 2538 GLU A CD    1 
ATOM   8310  O OE1   . GLU A 1 2538 ? 198.640 241.674 164.616 1.00 25.52 ? 2538 GLU A OE1   1 
ATOM   8311  O OE2   . GLU A 1 2538 ? 196.942 242.060 163.280 1.00 12.64 ? 2538 GLU A OE2   1 
ATOM   8312  N N     . VAL A 1 2539 ? 194.258 243.453 166.784 1.00 13.69 ? 2539 VAL A N     1 
ATOM   8313  C CA    . VAL A 1 2539 ? 193.958 244.877 166.877 1.00 8.98  ? 2539 VAL A CA    1 
ATOM   8314  C C     . VAL A 1 2539 ? 194.740 245.693 165.849 1.00 13.89 ? 2539 VAL A C     1 
ATOM   8315  O O     . VAL A 1 2539 ? 194.344 246.823 165.534 1.00 22.09 ? 2539 VAL A O     1 
ATOM   8316  C CB    . VAL A 1 2539 ? 194.221 245.355 168.317 1.00 9.98  ? 2539 VAL A CB    1 
ATOM   8317  C CG1   . VAL A 1 2539 ? 193.977 246.851 168.469 1.00 9.76  ? 2539 VAL A CG1   1 
ATOM   8318  C CG2   . VAL A 1 2539 ? 193.353 244.575 169.288 1.00 13.05 ? 2539 VAL A CG2   1 
ATOM   8319  N N     . SER A 1 2540 ? 195.810 245.137 165.288 1.00 12.10 ? 2540 SER A N     1 
ATOM   8320  C CA    . SER A 1 2540 ? 196.652 245.835 164.306 1.00 16.36 ? 2540 SER A CA    1 
ATOM   8321  C C     . SER A 1 2540 ? 197.281 247.043 165.006 1.00 15.83 ? 2540 SER A C     1 
ATOM   8322  O O     . SER A 1 2540 ? 197.741 246.935 166.149 1.00 19.86 ? 2540 SER A O     1 
ATOM   8323  C CB    . SER A 1 2540 ? 195.849 246.167 163.057 1.00 14.94 ? 2540 SER A CB    1 
ATOM   8324  O OG    . SER A 1 2540 ? 195.036 247.308 163.266 1.00 14.06 ? 2540 SER A OG    1 
ATOM   8325  N N     . ILE A 1 2541 ? 197.338 248.189 164.329 1.00 7.20  ? 2541 ILE A N     1 
ATOM   8326  C CA    . ILE A 1 2541 ? 197.862 249.409 164.934 1.00 5.83  ? 2541 ILE A CA    1 
ATOM   8327  C C     . ILE A 1 2541 ? 196.899 250.557 164.653 1.00 11.48 ? 2541 ILE A C     1 
ATOM   8328  O O     . ILE A 1 2541 ? 197.013 251.640 165.237 1.00 15.99 ? 2541 ILE A O     1 
ATOM   8329  C CB    . ILE A 1 2541 ? 199.279 249.722 164.419 1.00 9.62  ? 2541 ILE A CB    1 
ATOM   8330  C CG1   . ILE A 1 2541 ? 199.943 250.801 165.278 1.00 12.13 ? 2541 ILE A CG1   1 
ATOM   8331  C CG2   . ILE A 1 2541 ? 199.233 250.151 162.964 1.00 13.42 ? 2541 ILE A CG2   1 
ATOM   8332  C CD1   . ILE A 1 2541 ? 200.213 250.370 166.700 1.00 10.25 ? 2541 ILE A CD1   1 
ATOM   8333  N N     . SER A 1 2542 ? 195.934 250.323 163.768 1.00 15.82 ? 2542 SER A N     1 
ATOM   8334  C CA    . SER A 1 2542 ? 194.954 251.334 163.397 1.00 13.40 ? 2542 SER A CA    1 
ATOM   8335  C C     . SER A 1 2542 ? 193.692 251.262 164.244 1.00 14.42 ? 2542 SER A C     1 
ATOM   8336  O O     . SER A 1 2542 ? 192.712 251.948 163.937 1.00 17.13 ? 2542 SER A O     1 
ATOM   8337  C CB    . SER A 1 2542 ? 194.599 251.208 161.913 1.00 11.61 ? 2542 SER A CB    1 
ATOM   8338  O OG    . SER A 1 2542 ? 193.928 249.990 161.645 1.00 13.32 ? 2542 SER A OG    1 
ATOM   8339  N N     . GLY A 1 2543 ? 193.694 250.458 165.300 1.00 13.81 ? 2543 GLY A N     1 
ATOM   8340  C CA    . GLY A 1 2543 ? 192.515 250.305 166.135 1.00 13.74 ? 2543 GLY A CA    1 
ATOM   8341  C C     . GLY A 1 2543 ? 191.361 249.606 165.451 1.00 12.59 ? 2543 GLY A C     1 
ATOM   8342  O O     . GLY A 1 2543 ? 190.204 250.005 165.633 1.00 13.50 ? 2543 GLY A O     1 
ATOM   8343  N N     . GLU A 1 2544 ? 191.647 248.568 164.670 1.00 14.05 ? 2544 GLU A N     1 
ATOM   8344  C CA    . GLU A 1 2544 ? 190.633 247.810 163.955 1.00 16.30 ? 2544 GLU A CA    1 
ATOM   8345  C C     . GLU A 1 2544 ? 190.849 246.325 164.199 1.00 17.16 ? 2544 GLU A C     1 
ATOM   8346  O O     . GLU A 1 2544 ? 191.990 245.869 164.317 1.00 13.58 ? 2544 GLU A O     1 
ATOM   8347  C CB    . GLU A 1 2544 ? 190.681 248.101 162.448 1.00 16.48 ? 2544 GLU A CB    1 
ATOM   8348  C CG    . GLU A 1 2544 ? 189.834 249.280 161.979 1.00 16.34 ? 2544 GLU A CG    1 
ATOM   8349  C CD    . GLU A 1 2544 ? 188.435 249.315 162.576 1.00 20.74 ? 2544 GLU A CD    1 
ATOM   8350  O OE1   . GLU A 1 2544 ? 187.900 250.429 162.747 1.00 19.77 ? 2544 GLU A OE1   1 
ATOM   8351  O OE2   . GLU A 1 2544 ? 187.847 248.240 162.825 1.00 22.87 ? 2544 GLU A OE2   1 
ATOM   8352  N N     . TRP A 1 2545 ? 189.754 245.572 164.269 1.00 16.04 ? 2545 TRP A N     1 
ATOM   8353  C CA    . TRP A 1 2545 ? 189.836 244.118 164.395 1.00 15.42 ? 2545 TRP A CA    1 
ATOM   8354  C C     . TRP A 1 2545 ? 190.183 243.520 163.038 1.00 18.13 ? 2545 TRP A C     1 
ATOM   8355  O O     . TRP A 1 2545 ? 189.327 243.341 162.170 1.00 23.09 ? 2545 TRP A O     1 
ATOM   8356  C CB    . TRP A 1 2545 ? 188.539 243.534 164.937 1.00 17.42 ? 2545 TRP A CB    1 
ATOM   8357  C CG    . TRP A 1 2545 ? 188.079 244.129 166.222 1.00 18.40 ? 2545 TRP A CG    1 
ATOM   8358  C CD1   . TRP A 1 2545 ? 187.181 245.140 166.387 1.00 19.76 ? 2545 TRP A CD1   1 
ATOM   8359  C CD2   . TRP A 1 2545 ? 188.495 243.741 167.535 1.00 20.85 ? 2545 TRP A CD2   1 
ATOM   8360  N NE1   . TRP A 1 2545 ? 187.008 245.404 167.725 1.00 18.03 ? 2545 TRP A NE1   1 
ATOM   8361  C CE2   . TRP A 1 2545 ? 187.806 244.558 168.450 1.00 20.36 ? 2545 TRP A CE2   1 
ATOM   8362  C CE3   . TRP A 1 2545 ? 189.383 242.779 168.026 1.00 19.75 ? 2545 TRP A CE3   1 
ATOM   8363  C CZ2   . TRP A 1 2545 ? 187.977 244.443 169.827 1.00 21.45 ? 2545 TRP A CZ2   1 
ATOM   8364  C CZ3   . TRP A 1 2545 ? 189.553 242.668 169.392 1.00 13.37 ? 2545 TRP A CZ3   1 
ATOM   8365  C CH2   . TRP A 1 2545 ? 188.855 243.495 170.276 1.00 17.51 ? 2545 TRP A CH2   1 
ATOM   8366  N N     . SER A 1 2546 ? 191.464 243.205 162.855 1.00 10.32 ? 2546 SER A N     1 
ATOM   8367  C CA    . SER A 1 2546 ? 191.922 242.508 161.666 1.00 14.23 ? 2546 SER A CA    1 
ATOM   8368  C C     . SER A 1 2546 ? 192.012 241.024 161.970 1.00 16.40 ? 2546 SER A C     1 
ATOM   8369  O O     . SER A 1 2546 ? 192.764 240.637 162.877 1.00 18.31 ? 2546 SER A O     1 
ATOM   8370  C CB    . SER A 1 2546 ? 193.278 243.040 161.218 1.00 13.86 ? 2546 SER A CB    1 
ATOM   8371  O OG    . SER A 1 2546 ? 194.331 242.424 161.935 1.00 17.66 ? 2546 SER A OG    1 
ATOM   8372  N N     . PRO A 1 2547 ? 191.274 240.166 161.268 1.00 18.44 ? 2547 PRO A N     1 
ATOM   8373  C CA    . PRO A 1 2547 ? 191.312 238.734 161.584 1.00 10.86 ? 2547 PRO A CA    1 
ATOM   8374  C C     . PRO A 1 2547 ? 192.693 238.145 161.337 1.00 8.50  ? 2547 PRO A C     1 
ATOM   8375  O O     . PRO A 1 2547 ? 193.438 238.593 160.464 1.00 13.03 ? 2547 PRO A O     1 
ATOM   8376  C CB    . PRO A 1 2547 ? 190.269 238.132 160.636 1.00 11.62 ? 2547 PRO A CB    1 
ATOM   8377  C CG    . PRO A 1 2547 ? 190.167 239.111 159.518 1.00 16.28 ? 2547 PRO A CG    1 
ATOM   8378  C CD    . PRO A 1 2547 ? 190.392 240.460 160.127 1.00 15.49 ? 2547 PRO A CD    1 
ATOM   8379  N N     . TRP A 1 2548 ? 193.032 237.129 162.134 1.00 5.12  ? 2548 TRP A N     1 
ATOM   8380  C CA    . TRP A 1 2548 ? 194.330 236.481 161.984 1.00 9.08  ? 2548 TRP A CA    1 
ATOM   8381  C C     . TRP A 1 2548 ? 194.441 235.739 160.659 1.00 17.28 ? 2548 TRP A C     1 
ATOM   8382  O O     . TRP A 1 2548 ? 195.547 235.589 160.127 1.00 17.63 ? 2548 TRP A O     1 
ATOM   8383  C CB    . TRP A 1 2548 ? 194.583 235.520 163.144 1.00 11.46 ? 2548 TRP A CB    1 
ATOM   8384  C CG    . TRP A 1 2548 ? 194.969 236.189 164.424 1.00 13.85 ? 2548 TRP A CG    1 
ATOM   8385  C CD1   . TRP A 1 2548 ? 194.219 236.282 165.558 1.00 11.49 ? 2548 TRP A CD1   1 
ATOM   8386  C CD2   . TRP A 1 2548 ? 196.201 236.865 164.702 1.00 6.36  ? 2548 TRP A CD2   1 
ATOM   8387  N NE1   . TRP A 1 2548 ? 194.908 236.968 166.527 1.00 6.80  ? 2548 TRP A NE1   1 
ATOM   8388  C CE2   . TRP A 1 2548 ? 196.128 237.337 166.025 1.00 4.05  ? 2548 TRP A CE2   1 
ATOM   8389  C CE3   . TRP A 1 2548 ? 197.359 237.114 163.960 1.00 10.49 ? 2548 TRP A CE3   1 
ATOM   8390  C CZ2   . TRP A 1 2548 ? 197.166 238.045 166.621 1.00 11.16 ? 2548 TRP A CZ2   1 
ATOM   8391  C CZ3   . TRP A 1 2548 ? 198.388 237.815 164.554 1.00 8.78  ? 2548 TRP A CZ3   1 
ATOM   8392  C CH2   . TRP A 1 2548 ? 198.285 238.274 165.870 1.00 7.41  ? 2548 TRP A CH2   1 
ATOM   8393  N N     . GLN A 1 2549 ? 193.316 235.267 160.115 1.00 17.05 ? 2549 GLN A N     1 
ATOM   8394  C CA    . GLN A 1 2549 ? 193.343 234.549 158.846 1.00 13.77 ? 2549 GLN A CA    1 
ATOM   8395  C C     . GLN A 1 2549 ? 193.836 235.421 157.701 1.00 12.67 ? 2549 GLN A C     1 
ATOM   8396  O O     . GLN A 1 2549 ? 194.300 234.889 156.688 1.00 16.91 ? 2549 GLN A O     1 
ATOM   8397  C CB    . GLN A 1 2549 ? 191.954 234.004 158.517 1.00 10.38 ? 2549 GLN A CB    1 
ATOM   8398  C CG    . GLN A 1 2549 ? 191.511 232.863 159.411 1.00 11.54 ? 2549 GLN A CG    1 
ATOM   8399  C CD    . GLN A 1 2549 ? 190.418 232.027 158.781 1.00 16.09 ? 2549 GLN A CD    1 
ATOM   8400  O OE1   . GLN A 1 2549 ? 189.685 232.496 157.911 1.00 17.98 ? 2549 GLN A OE1   1 
ATOM   8401  N NE2   . GLN A 1 2549 ? 190.302 230.779 159.219 1.00 12.46 ? 2549 GLN A NE2   1 
ATOM   8402  N N     . ALA A 1 2550 ? 193.738 236.741 157.831 1.00 11.63 ? 2550 ALA A N     1 
ATOM   8403  C CA    . ALA A 1 2550 ? 194.281 237.636 156.820 1.00 15.92 ? 2550 ALA A CA    1 
ATOM   8404  C C     . ALA A 1 2550 ? 195.799 237.730 156.873 1.00 13.10 ? 2550 ALA A C     1 
ATOM   8405  O O     . ALA A 1 2550 ? 196.398 238.317 155.966 1.00 16.26 ? 2550 ALA A O     1 
ATOM   8406  C CB    . ALA A 1 2550 ? 193.675 239.032 156.973 1.00 18.48 ? 2550 ALA A CB    1 
ATOM   8407  N N     . LYS A 1 2551 ? 196.431 237.169 157.904 1.00 9.96  ? 2551 LYS A N     1 
ATOM   8408  C CA    . LYS A 1 2551 ? 197.870 237.275 158.094 1.00 15.87 ? 2551 LYS A CA    1 
ATOM   8409  C C     . LYS A 1 2551 ? 198.577 235.928 157.979 1.00 19.13 ? 2551 LYS A C     1 
ATOM   8410  O O     . LYS A 1 2551 ? 199.750 235.815 158.348 1.00 19.06 ? 2551 LYS A O     1 
ATOM   8411  C CB    . LYS A 1 2551 ? 198.173 237.922 159.446 1.00 12.37 ? 2551 LYS A CB    1 
ATOM   8412  C CG    . LYS A 1 2551 ? 199.439 238.763 159.465 1.00 16.85 ? 2551 LYS A CG    1 
ATOM   8413  C CD    . LYS A 1 2551 ? 199.394 239.798 160.574 1.00 17.44 ? 2551 LYS A CD    1 
ATOM   8414  C CE    . LYS A 1 2551 ? 198.333 240.850 160.297 1.00 18.13 ? 2551 LYS A CE    1 
ATOM   8415  N NZ    . LYS A 1 2551 ? 198.360 241.945 161.303 1.00 21.65 ? 2551 LYS A NZ    1 
ATOM   8416  N N     . VAL A 1 2552 ? 197.897 234.906 157.470 1.00 16.26 ? 2552 VAL A N     1 
ATOM   8417  C CA    . VAL A 1 2552 ? 198.507 233.598 157.264 1.00 13.38 ? 2552 VAL A CA    1 
ATOM   8418  C C     . VAL A 1 2552 ? 198.841 233.464 155.777 1.00 19.54 ? 2552 VAL A C     1 
ATOM   8419  O O     . VAL A 1 2552 ? 197.934 233.401 154.932 1.00 23.09 ? 2552 VAL A O     1 
ATOM   8420  C CB    . VAL A 1 2552 ? 197.610 232.456 157.768 1.00 11.93 ? 2552 VAL A CB    1 
ATOM   8421  C CG1   . VAL A 1 2552 ? 197.405 232.585 159.263 1.00 13.26 ? 2552 VAL A CG1   1 
ATOM   8422  C CG2   . VAL A 1 2552 ? 196.250 232.454 157.092 1.00 15.18 ? 2552 VAL A CG2   1 
ATOM   8423  N N     . PRO A 1 2553 ? 200.115 233.463 155.404 1.00 20.53 ? 2553 PRO A N     1 
ATOM   8424  C CA    . PRO A 1 2553 ? 200.475 233.330 153.992 1.00 19.55 ? 2553 PRO A CA    1 
ATOM   8425  C C     . PRO A 1 2553 ? 200.349 231.894 153.508 1.00 22.45 ? 2553 PRO A C     1 
ATOM   8426  O O     . PRO A 1 2553 ? 200.309 230.941 154.288 1.00 21.66 ? 2553 PRO A O     1 
ATOM   8427  C CB    . PRO A 1 2553 ? 201.939 233.793 153.949 1.00 20.71 ? 2553 PRO A CB    1 
ATOM   8428  C CG    . PRO A 1 2553 ? 202.201 234.430 155.291 1.00 23.70 ? 2553 PRO A CG    1 
ATOM   8429  C CD    . PRO A 1 2553 ? 201.292 233.732 156.242 1.00 22.46 ? 2553 PRO A CD    1 
ATOM   8430  N N     . GLN A 1 2554 ? 200.285 231.758 152.187 1.00 29.60 ? 2554 GLN A N     1 
ATOM   8431  C CA    . GLN A 1 2554 ? 200.310 230.458 151.526 1.00 28.04 ? 2554 GLN A CA    1 
ATOM   8432  C C     . GLN A 1 2554 ? 201.706 230.254 150.951 1.00 27.80 ? 2554 GLN A C     1 
ATOM   8433  O O     . GLN A 1 2554 ? 202.046 230.826 149.910 1.00 29.19 ? 2554 GLN A O     1 
ATOM   8434  C CB    . GLN A 1 2554 ? 199.246 230.374 150.436 1.00 26.07 ? 2554 GLN A CB    1 
ATOM   8435  C CG    . GLN A 1 2554 ? 198.785 228.961 150.137 1.00 27.71 ? 2554 GLN A CG    1 
ATOM   8436  C CD    . GLN A 1 2554 ? 197.624 228.534 151.006 1.00 27.74 ? 2554 GLN A CD    1 
ATOM   8437  O OE1   . GLN A 1 2554 ? 197.228 229.248 151.927 1.00 24.59 ? 2554 GLN A OE1   1 
ATOM   8438  N NE2   . GLN A 1 2554 ? 197.065 227.365 150.713 1.00 26.75 ? 2554 GLN A NE2   1 
ATOM   8439  N N     . ILE A 1 2555 ? 202.509 229.444 151.627 1.00 24.74 ? 2555 ILE A N     1 
ATOM   8440  C CA    . ILE A 1 2555 ? 203.888 229.223 151.237 1.00 26.00 ? 2555 ILE A CA    1 
ATOM   8441  C C     . ILE A 1 2555 ? 203.992 227.906 150.481 1.00 28.80 ? 2555 ILE A C     1 
ATOM   8442  O O     . ILE A 1 2555 ? 203.159 227.005 150.616 1.00 29.41 ? 2555 ILE A O     1 
ATOM   8443  C CB    . ILE A 1 2555 ? 204.839 229.239 152.457 1.00 25.55 ? 2555 ILE A CB    1 
ATOM   8444  C CG1   . ILE A 1 2555 ? 204.552 228.049 153.375 1.00 20.20 ? 2555 ILE A CG1   1 
ATOM   8445  C CG2   . ILE A 1 2555 ? 204.719 230.552 153.211 1.00 28.13 ? 2555 ILE A CG2   1 
ATOM   8446  C CD1   . ILE A 1 2555 ? 205.734 227.632 154.216 1.00 21.26 ? 2555 ILE A CD1   1 
ATOM   8447  N N     . GLU A 1 2556 ? 205.033 227.800 149.659 1.00 25.47 ? 2556 GLU A N     1 
ATOM   8448  C CA    . GLU A 1 2556 ? 205.348 226.578 148.928 1.00 22.98 ? 2556 GLU A CA    1 
ATOM   8449  C C     . GLU A 1 2556 ? 206.781 226.195 149.263 1.00 24.84 ? 2556 GLU A C     1 
ATOM   8450  O O     . GLU A 1 2556 ? 207.726 226.778 148.721 1.00 25.28 ? 2556 GLU A O     1 
ATOM   8451  C CB    . GLU A 1 2556 ? 205.167 226.765 147.421 1.00 23.91 ? 2556 GLU A CB    1 
ATOM   8452  C CG    . GLU A 1 2556 ? 203.812 227.321 147.014 1.00 24.83 ? 2556 GLU A CG    1 
ATOM   8453  C CD    . GLU A 1 2556 ? 202.682 226.327 147.208 1.00 25.31 ? 2556 GLU A CD    1 
ATOM   8454  O OE1   . GLU A 1 2556 ? 202.963 225.134 147.447 1.00 27.31 ? 2556 GLU A OE1   1 
ATOM   8455  O OE2   . GLU A 1 2556 ? 201.507 226.740 147.120 1.00 26.08 ? 2556 GLU A OE2   1 
ATOM   8456  N N     . VAL A 1 2557 ? 206.940 225.223 150.156 1.00 22.48 ? 2557 VAL A N     1 
ATOM   8457  C CA    . VAL A 1 2557 ? 208.268 224.796 150.572 1.00 23.26 ? 2557 VAL A CA    1 
ATOM   8458  C C     . VAL A 1 2557 ? 208.897 223.930 149.484 1.00 23.48 ? 2557 VAL A C     1 
ATOM   8459  O O     . VAL A 1 2557 ? 208.224 223.163 148.792 1.00 23.38 ? 2557 VAL A O     1 
ATOM   8460  C CB    . VAL A 1 2557 ? 208.203 224.057 151.922 1.00 20.35 ? 2557 VAL A CB    1 
ATOM   8461  C CG1   . VAL A 1 2557 ? 207.418 222.761 151.793 1.00 18.79 ? 2557 VAL A CG1   1 
ATOM   8462  C CG2   . VAL A 1 2557 ? 209.598 223.804 152.466 1.00 23.34 ? 2557 VAL A CG2   1 
ATOM   8463  N N     . GLU A 1 2558 ? 210.209 224.080 149.313 1.00 24.56 ? 2558 GLU A N     1 
ATOM   8464  C CA    . GLU A 1 2558 ? 210.895 223.313 148.287 1.00 25.59 ? 2558 GLU A CA    1 
ATOM   8465  C C     . GLU A 1 2558 ? 210.963 221.843 148.693 1.00 28.37 ? 2558 GLU A C     1 
ATOM   8466  O O     . GLU A 1 2558 ? 210.815 221.486 149.864 1.00 26.42 ? 2558 GLU A O     1 
ATOM   8467  C CB    . GLU A 1 2558 ? 212.291 223.886 148.018 1.00 26.96 ? 2558 GLU A CB    1 
ATOM   8468  C CG    . GLU A 1 2558 ? 213.264 223.851 149.184 1.00 32.27 ? 2558 GLU A CG    1 
ATOM   8469  C CD    . GLU A 1 2558 ? 214.025 222.542 149.264 1.00 32.55 ? 2558 GLU A CD    1 
ATOM   8470  O OE1   . GLU A 1 2558 ? 214.084 221.825 148.243 1.00 27.12 ? 2558 GLU A OE1   1 
ATOM   8471  O OE2   . GLU A 1 2558 ? 214.576 222.235 150.340 1.00 29.89 ? 2558 GLU A OE2   1 
ATOM   8472  N N     . THR A 1 2559 ? 211.188 220.986 147.695 1.00 27.36 ? 2559 THR A N     1 
ATOM   8473  C CA    . THR A 1 2559 ? 210.971 219.553 147.879 1.00 21.69 ? 2559 THR A CA    1 
ATOM   8474  C C     . THR A 1 2559 ? 211.914 218.960 148.920 1.00 23.78 ? 2559 THR A C     1 
ATOM   8475  O O     . THR A 1 2559 ? 211.519 218.078 149.691 1.00 27.73 ? 2559 THR A O     1 
ATOM   8476  C CB    . THR A 1 2559 ? 211.123 218.827 146.545 1.00 24.19 ? 2559 THR A CB    1 
ATOM   8477  O OG1   . THR A 1 2559 ? 210.327 219.482 145.551 1.00 27.11 ? 2559 THR A OG1   1 
ATOM   8478  C CG2   . THR A 1 2559 ? 210.655 217.399 146.683 1.00 26.32 ? 2559 THR A CG2   1 
ATOM   8479  N N     . HIS A 1 2560 ? 213.165 219.420 148.960 1.00 28.28 ? 2560 HIS A N     1 
ATOM   8480  C CA    . HIS A 1 2560 ? 214.116 218.856 149.912 1.00 28.56 ? 2560 HIS A CA    1 
ATOM   8481  C C     . HIS A 1 2560 ? 213.808 219.251 151.351 1.00 28.80 ? 2560 HIS A C     1 
ATOM   8482  O O     . HIS A 1 2560 ? 214.465 218.749 152.269 1.00 30.89 ? 2560 HIS A O     1 
ATOM   8483  C CB    . HIS A 1 2560 ? 215.544 219.270 149.555 1.00 32.45 ? 2560 HIS A CB    1 
ATOM   8484  C CG    . HIS A 1 2560 ? 215.966 218.864 148.176 1.00 35.96 ? 2560 HIS A CG    1 
ATOM   8485  N ND1   . HIS A 1 2560 ? 216.951 217.928 147.947 1.00 35.97 ? 2560 HIS A ND1   1 
ATOM   8486  C CD2   . HIS A 1 2560 ? 215.541 219.269 146.956 1.00 32.67 ? 2560 HIS A CD2   1 
ATOM   8487  C CE1   . HIS A 1 2560 ? 217.112 217.771 146.645 1.00 35.21 ? 2560 HIS A CE1   1 
ATOM   8488  N NE2   . HIS A 1 2560 ? 216.269 218.574 146.021 1.00 32.76 ? 2560 HIS A NE2   1 
ATOM   8489  N N     . LYS A 1 2561 ? 212.838 220.137 151.570 1.00 27.25 ? 2561 LYS A N     1 
ATOM   8490  C CA    . LYS A 1 2561 ? 212.471 220.600 152.904 1.00 29.62 ? 2561 LYS A CA    1 
ATOM   8491  C C     . LYS A 1 2561 ? 211.032 220.230 153.259 1.00 25.57 ? 2561 LYS A C     1 
ATOM   8492  O O     . LYS A 1 2561 ? 210.342 220.970 153.962 1.00 28.73 ? 2561 LYS A O     1 
ATOM   8493  C CB    . LYS A 1 2561 ? 212.674 222.109 153.022 1.00 25.11 ? 2561 LYS A CB    1 
ATOM   8494  C CG    . LYS A 1 2561 ? 214.085 222.532 153.398 1.00 24.85 ? 2561 LYS A CG    1 
ATOM   8495  C CD    . LYS A 1 2561 ? 214.444 222.120 154.813 1.00 28.16 ? 2561 LYS A CD    1 
ATOM   8496  C CE    . LYS A 1 2561 ? 215.416 223.107 155.436 1.00 28.02 ? 2561 LYS A CE    1 
ATOM   8497  N NZ    . LYS A 1 2561 ? 215.474 222.971 156.917 1.00 30.13 ? 2561 LYS A NZ    1 
ATOM   8498  N N     . VAL A 1 2562 ? 210.559 219.082 152.782 1.00 18.21 ? 2562 VAL A N     1 
ATOM   8499  C CA    . VAL A 1 2562 ? 209.208 218.616 153.082 1.00 18.79 ? 2562 VAL A CA    1 
ATOM   8500  C C     . VAL A 1 2562 ? 209.218 217.930 154.440 1.00 21.82 ? 2562 VAL A C     1 
ATOM   8501  O O     . VAL A 1 2562 ? 209.927 216.937 154.636 1.00 22.09 ? 2562 VAL A O     1 
ATOM   8502  C CB    . VAL A 1 2562 ? 208.684 217.668 151.995 1.00 20.57 ? 2562 VAL A CB    1 
ATOM   8503  C CG1   . VAL A 1 2562 ? 207.325 217.120 152.393 1.00 17.80 ? 2562 VAL A CG1   1 
ATOM   8504  C CG2   . VAL A 1 2562 ? 208.585 218.389 150.672 1.00 23.78 ? 2562 VAL A CG2   1 
ATOM   8505  N N     . ALA A 1 2563 ? 208.430 218.463 155.377 1.00 20.35 ? 2563 ALA A N     1 
ATOM   8506  C CA    . ALA A 1 2563 ? 208.321 217.933 156.738 1.00 15.85 ? 2563 ALA A CA    1 
ATOM   8507  C C     . ALA A 1 2563 ? 209.682 217.826 157.418 1.00 17.84 ? 2563 ALA A C     1 
ATOM   8508  O O     . ALA A 1 2563 ? 209.860 217.047 158.357 1.00 17.44 ? 2563 ALA A O     1 
ATOM   8509  C CB    . ALA A 1 2563 ? 207.603 216.581 156.755 1.00 14.47 ? 2563 ALA A CB    1 
ATOM   8510  N N     . ALA A 1 2564 ? 210.651 218.607 156.948 1.00 24.91 ? 2564 ALA A N     1 
ATOM   8511  C CA    . ALA A 1 2564 ? 211.971 218.618 157.543 1.00 25.57 ? 2564 ALA A CA    1 
ATOM   8512  C C     . ALA A 1 2564 ? 211.931 219.338 158.888 1.00 26.87 ? 2564 ALA A C     1 
ATOM   8513  O O     . ALA A 1 2564 ? 211.031 220.142 159.144 1.00 29.02 ? 2564 ALA A O     1 
ATOM   8514  C CB    . ALA A 1 2564 ? 212.968 219.294 156.604 1.00 21.69 ? 2564 ALA A CB    1 
ATOM   8515  N N     . PRO A 1 2565 ? 212.886 219.053 159.772 1.00 26.53 ? 2565 PRO A N     1 
ATOM   8516  C CA    . PRO A 1 2565 ? 212.920 219.752 161.061 1.00 26.05 ? 2565 PRO A CA    1 
ATOM   8517  C C     . PRO A 1 2565 ? 213.077 221.255 160.876 1.00 25.02 ? 2565 PRO A C     1 
ATOM   8518  O O     . PRO A 1 2565 ? 213.731 221.720 159.940 1.00 24.94 ? 2565 PRO A O     1 
ATOM   8519  C CB    . PRO A 1 2565 ? 214.137 219.140 161.768 1.00 23.47 ? 2565 PRO A CB    1 
ATOM   8520  C CG    . PRO A 1 2565 ? 214.930 218.474 160.686 1.00 27.40 ? 2565 PRO A CG    1 
ATOM   8521  C CD    . PRO A 1 2565 ? 213.922 218.011 159.689 1.00 23.30 ? 2565 PRO A CD    1 
ATOM   8522  N N     . ASP A 1 2566 ? 212.451 222.010 161.780 1.00 20.56 ? 2566 ASP A N     1 
ATOM   8523  C CA    . ASP A 1 2566 ? 212.505 223.473 161.783 1.00 24.20 ? 2566 ASP A CA    1 
ATOM   8524  C C     . ASP A 1 2566 ? 211.923 224.063 160.498 1.00 25.42 ? 2566 ASP A C     1 
ATOM   8525  O O     . ASP A 1 2566 ? 212.422 225.060 159.975 1.00 22.29 ? 2566 ASP A O     1 
ATOM   8526  C CB    . ASP A 1 2566 ? 213.932 223.978 162.012 1.00 23.21 ? 2566 ASP A CB    1 
ATOM   8527  C CG    . ASP A 1 2566 ? 214.622 223.270 163.161 1.00 25.28 ? 2566 ASP A CG    1 
ATOM   8528  O OD1   . ASP A 1 2566 ? 214.255 223.528 164.327 1.00 25.14 ? 2566 ASP A OD1   1 
ATOM   8529  O OD2   . ASP A 1 2566 ? 215.530 222.454 162.898 1.00 26.78 ? 2566 ASP A OD2   1 
ATOM   8530  N N     . VAL A 1 2567 ? 210.860 223.445 159.987 1.00 21.49 ? 2567 VAL A N     1 
ATOM   8531  C CA    . VAL A 1 2567 ? 210.114 223.955 158.840 1.00 20.40 ? 2567 VAL A CA    1 
ATOM   8532  C C     . VAL A 1 2567 ? 208.672 224.119 159.302 1.00 18.34 ? 2567 VAL A C     1 
ATOM   8533  O O     . VAL A 1 2567 ? 208.016 223.139 159.670 1.00 17.85 ? 2567 VAL A O     1 
ATOM   8534  C CB    . VAL A 1 2567 ? 210.203 223.034 157.619 1.00 20.31 ? 2567 VAL A CB    1 
ATOM   8535  C CG1   . VAL A 1 2567 ? 209.322 223.560 156.497 1.00 17.45 ? 2567 VAL A CG1   1 
ATOM   8536  C CG2   . VAL A 1 2567 ? 211.645 222.912 157.151 1.00 20.45 ? 2567 VAL A CG2   1 
ATOM   8537  N N     . VAL A 1 2568 ? 208.175 225.353 159.286 1.00 14.57 ? 2568 VAL A N     1 
ATOM   8538  C CA    . VAL A 1 2568 ? 206.847 225.683 159.789 1.00 8.92  ? 2568 VAL A CA    1 
ATOM   8539  C C     . VAL A 1 2568 ? 206.017 226.242 158.645 1.00 14.07 ? 2568 VAL A C     1 
ATOM   8540  O O     . VAL A 1 2568 ? 206.458 227.157 157.938 1.00 18.72 ? 2568 VAL A O     1 
ATOM   8541  C CB    . VAL A 1 2568 ? 206.919 226.695 160.945 1.00 10.07 ? 2568 VAL A CB    1 
ATOM   8542  C CG1   . VAL A 1 2568 ? 205.563 226.819 161.622 1.00 10.54 ? 2568 VAL A CG1   1 
ATOM   8543  C CG2   . VAL A 1 2568 ? 207.992 226.295 161.938 1.00 14.20 ? 2568 VAL A CG2   1 
ATOM   8544  N N     . VAL A 1 2569 ? 204.824 225.696 158.461 1.00 11.71 ? 2569 VAL A N     1 
ATOM   8545  C CA    . VAL A 1 2569 ? 203.859 226.298 157.540 1.00 10.95 ? 2569 VAL A CA    1 
ATOM   8546  C C     . VAL A 1 2569 ? 202.908 227.186 158.339 1.00 13.09 ? 2569 VAL A C     1 
ATOM   8547  O O     . VAL A 1 2569 ? 202.338 226.728 159.343 1.00 11.60 ? 2569 VAL A O     1 
ATOM   8548  C CB    . VAL A 1 2569 ? 203.106 225.224 156.755 1.00 4.32  ? 2569 VAL A CB    1 
ATOM   8549  C CG1   . VAL A 1 2569 ? 204.079 224.432 155.899 1.00 11.29 ? 2569 VAL A CG1   1 
ATOM   8550  C CG2   . VAL A 1 2569 ? 202.367 224.281 157.680 1.00 6.75  ? 2569 VAL A CG2   1 
ATOM   8551  N N     . PRO A 1 2570 ? 202.761 228.457 157.975 1.00 12.00 ? 2570 PRO A N     1 
ATOM   8552  C CA    . PRO A 1 2570 ? 201.898 229.355 158.749 1.00 7.88  ? 2570 PRO A CA    1 
ATOM   8553  C C     . PRO A 1 2570 ? 200.460 228.862 158.800 1.00 9.70  ? 2570 PRO A C     1 
ATOM   8554  O O     . PRO A 1 2570 ? 199.922 228.353 157.815 1.00 14.06 ? 2570 PRO A O     1 
ATOM   8555  C CB    . PRO A 1 2570 ? 202.013 230.679 157.993 1.00 9.51  ? 2570 PRO A CB    1 
ATOM   8556  C CG    . PRO A 1 2570 ? 203.370 230.627 157.378 1.00 14.17 ? 2570 PRO A CG    1 
ATOM   8557  C CD    . PRO A 1 2570 ? 203.573 229.188 156.986 1.00 11.84 ? 2570 PRO A CD    1 
ATOM   8558  N N     . THR A 1 2571 ? 199.835 229.023 159.962 1.00 3.83  ? 2571 THR A N     1 
ATOM   8559  C CA    . THR A 1 2571 ? 198.442 228.646 160.161 1.00 4.75  ? 2571 THR A CA    1 
ATOM   8560  C C     . THR A 1 2571 ? 197.837 229.590 161.194 1.00 5.64  ? 2571 THR A C     1 
ATOM   8561  O O     . THR A 1 2571 ? 198.470 230.564 161.613 1.00 11.29 ? 2571 THR A O     1 
ATOM   8562  C CB    . THR A 1 2571 ? 198.326 227.174 160.579 1.00 7.15  ? 2571 THR A CB    1 
ATOM   8563  O OG1   . THR A 1 2571 ? 196.948 226.836 160.771 1.00 15.15 ? 2571 THR A OG1   1 
ATOM   8564  C CG2   . THR A 1 2571 ? 199.079 226.926 161.866 1.00 8.33  ? 2571 THR A CG2   1 
ATOM   8565  N N     . LEU A 1 2572 ? 196.599 229.304 161.604 1.00 7.11  ? 2572 LEU A N     1 
ATOM   8566  C CA    . LEU A 1 2572 ? 195.912 230.181 162.547 1.00 4.42  ? 2572 LEU A CA    1 
ATOM   8567  C C     . LEU A 1 2572 ? 196.614 230.235 163.896 1.00 5.50  ? 2572 LEU A C     1 
ATOM   8568  O O     . LEU A 1 2572 ? 196.777 231.321 164.463 1.00 8.90  ? 2572 LEU A O     1 
ATOM   8569  C CB    . LEU A 1 2572 ? 194.466 229.726 162.736 1.00 5.43  ? 2572 LEU A CB    1 
ATOM   8570  C CG    . LEU A 1 2572 ? 193.527 230.758 163.363 1.00 4.80  ? 2572 LEU A CG    1 
ATOM   8571  C CD1   . LEU A 1 2572 ? 193.624 232.086 162.636 1.00 10.35 ? 2572 LEU A CD1   1 
ATOM   8572  C CD2   . LEU A 1 2572 ? 192.096 230.252 163.374 1.00 11.85 ? 2572 LEU A CD2   1 
ATOM   8573  N N     . ASP A 1 2573 ? 197.031 229.088 164.425 1.00 9.87  ? 2573 ASP A N     1 
ATOM   8574  C CA    . ASP A 1 2573 ? 197.645 229.035 165.745 1.00 0.56  ? 2573 ASP A CA    1 
ATOM   8575  C C     . ASP A 1 2573 ? 199.067 229.574 165.749 1.00 2.45  ? 2573 ASP A C     1 
ATOM   8576  O O     . ASP A 1 2573 ? 199.461 230.268 166.691 1.00 14.36 ? 2573 ASP A O     1 
ATOM   8577  C CB    . ASP A 1 2573 ? 197.638 227.599 166.266 1.00 5.13  ? 2573 ASP A CB    1 
ATOM   8578  C CG    . ASP A 1 2573 ? 196.266 226.967 166.205 1.00 15.25 ? 2573 ASP A CG    1 
ATOM   8579  O OD1   . ASP A 1 2573 ? 195.267 227.716 166.206 1.00 15.73 ? 2573 ASP A OD1   1 
ATOM   8580  O OD2   . ASP A 1 2573 ? 196.186 225.722 166.153 1.00 19.35 ? 2573 ASP A OD2   1 
ATOM   8581  N N     . THR A 1 2574 ? 199.848 229.267 164.719 1.00 2.69  ? 2574 THR A N     1 
ATOM   8582  C CA    . THR A 1 2574 ? 201.239 229.692 164.663 1.00 6.92  ? 2574 THR A CA    1 
ATOM   8583  C C     . THR A 1 2574 ? 201.395 231.186 164.406 1.00 9.89  ? 2574 THR A C     1 
ATOM   8584  O O     . THR A 1 2574 ? 202.471 231.730 164.662 1.00 15.90 ? 2574 THR A O     1 
ATOM   8585  C CB    . THR A 1 2574 ? 201.985 228.891 163.589 1.00 6.12  ? 2574 THR A CB    1 
ATOM   8586  O OG1   . THR A 1 2574 ? 201.593 227.516 163.669 1.00 10.33 ? 2574 THR A OG1   1 
ATOM   8587  C CG2   . THR A 1 2574 ? 203.492 228.975 163.791 1.00 7.17  ? 2574 THR A CG2   1 
ATOM   8588  N N     . VAL A 1 2575 ? 200.356 231.870 163.930 1.00 6.27  ? 2575 VAL A N     1 
ATOM   8589  C CA    . VAL A 1 2575 ? 200.447 233.309 163.715 1.00 6.29  ? 2575 VAL A CA    1 
ATOM   8590  C C     . VAL A 1 2575 ? 200.045 234.107 164.953 1.00 11.04 ? 2575 VAL A C     1 
ATOM   8591  O O     . VAL A 1 2575 ? 200.521 235.239 165.125 1.00 19.76 ? 2575 VAL A O     1 
ATOM   8592  C CB    . VAL A 1 2575 ? 199.604 233.741 162.493 1.00 4.65  ? 2575 VAL A CB    1 
ATOM   8593  C CG1   . VAL A 1 2575 ? 198.119 233.732 162.818 1.00 4.81  ? 2575 VAL A CG1   1 
ATOM   8594  C CG2   . VAL A 1 2575 ? 200.047 235.108 161.989 1.00 10.67 ? 2575 VAL A CG2   1 
ATOM   8595  N N     . ARG A 1 2576 ? 199.210 233.548 165.827 1.00 1.86  ? 2576 ARG A N     1 
ATOM   8596  C CA    . ARG A 1 2576 ? 198.801 234.192 167.069 1.00 0.00  ? 2576 ARG A CA    1 
ATOM   8597  C C     . ARG A 1 2576 ? 199.691 233.827 168.251 1.00 11.92 ? 2576 ARG A C     1 
ATOM   8598  O O     . ARG A 1 2576 ? 200.053 234.704 169.049 1.00 22.45 ? 2576 ARG A O     1 
ATOM   8599  C CB    . ARG A 1 2576 ? 197.342 233.838 167.381 1.00 0.00  ? 2576 ARG A CB    1 
ATOM   8600  C CG    . ARG A 1 2576 ? 197.087 232.350 167.531 1.00 8.80  ? 2576 ARG A CG    1 
ATOM   8601  C CD    . ARG A 1 2576 ? 195.685 232.036 168.008 1.00 5.69  ? 2576 ARG A CD    1 
ATOM   8602  N NE    . ARG A 1 2576 ? 194.666 232.320 167.009 1.00 13.63 ? 2576 ARG A NE    1 
ATOM   8603  C CZ    . ARG A 1 2576 ? 193.371 232.096 167.182 1.00 13.39 ? 2576 ARG A CZ    1 
ATOM   8604  N NH1   . ARG A 1 2576 ? 192.907 231.561 168.299 1.00 8.07  ? 2576 ARG A NH1   1 
ATOM   8605  N NH2   . ARG A 1 2576 ? 192.523 232.409 166.209 1.00 19.76 ? 2576 ARG A NH2   1 
ATOM   8606  N N     . HIS A 1 2577 ? 200.065 232.552 168.383 1.00 4.23  ? 2577 HIS A N     1 
ATOM   8607  C CA    . HIS A 1 2577 ? 200.993 232.174 169.439 1.00 0.00  ? 2577 HIS A CA    1 
ATOM   8608  C C     . HIS A 1 2577 ? 202.345 232.840 169.236 1.00 4.21  ? 2577 HIS A C     1 
ATOM   8609  O O     . HIS A 1 2577 ? 202.985 233.253 170.206 1.00 15.38 ? 2577 HIS A O     1 
ATOM   8610  C CB    . HIS A 1 2577 ? 201.140 230.656 169.501 1.00 3.06  ? 2577 HIS A CB    1 
ATOM   8611  C CG    . HIS A 1 2577 ? 199.882 229.943 169.889 1.00 4.36  ? 2577 HIS A CG    1 
ATOM   8612  N ND1   . HIS A 1 2577 ? 199.254 229.038 169.062 1.00 9.46  ? 2577 HIS A ND1   1 
ATOM   8613  C CD2   . HIS A 1 2577 ? 199.134 230.007 171.014 1.00 6.05  ? 2577 HIS A CD2   1 
ATOM   8614  C CE1   . HIS A 1 2577 ? 198.175 228.571 169.664 1.00 6.40  ? 2577 HIS A CE1   1 
ATOM   8615  N NE2   . HIS A 1 2577 ? 198.079 229.143 170.850 1.00 1.76  ? 2577 HIS A NE2   1 
ATOM   8616  N N     . GLU A 1 2578 ? 202.791 232.964 167.985 1.00 2.28  ? 2578 GLU A N     1 
ATOM   8617  C CA    . GLU A 1 2578 ? 204.021 233.700 167.713 1.00 5.56  ? 2578 GLU A CA    1 
ATOM   8618  C C     . GLU A 1 2578 ? 203.887 235.160 168.124 1.00 7.27  ? 2578 GLU A C     1 
ATOM   8619  O O     . GLU A 1 2578 ? 204.848 235.765 168.614 1.00 10.79 ? 2578 GLU A O     1 
ATOM   8620  C CB    . GLU A 1 2578 ? 204.384 233.600 166.234 1.00 5.95  ? 2578 GLU A CB    1 
ATOM   8621  C CG    . GLU A 1 2578 ? 205.249 232.408 165.874 1.00 10.36 ? 2578 GLU A CG    1 
ATOM   8622  C CD    . GLU A 1 2578 ? 206.061 232.649 164.619 1.00 14.46 ? 2578 GLU A CD    1 
ATOM   8623  O OE1   . GLU A 1 2578 ? 206.511 231.662 164.002 1.00 11.63 ? 2578 GLU A OE1   1 
ATOM   8624  O OE2   . GLU A 1 2578 ? 206.248 233.826 164.247 1.00 18.18 ? 2578 GLU A OE2   1 
ATOM   8625  N N     . ALA A 1 2579 ? 202.706 235.746 167.921 1.00 5.92  ? 2579 ALA A N     1 
ATOM   8626  C CA    . ALA A 1 2579 ? 202.486 237.124 168.348 1.00 6.03  ? 2579 ALA A CA    1 
ATOM   8627  C C     . ALA A 1 2579 ? 202.628 237.259 169.857 1.00 8.33  ? 2579 ALA A C     1 
ATOM   8628  O O     . ALA A 1 2579 ? 203.302 238.175 170.346 1.00 12.42 ? 2579 ALA A O     1 
ATOM   8629  C CB    . ALA A 1 2579 ? 201.109 237.602 167.892 1.00 3.13  ? 2579 ALA A CB    1 
ATOM   8630  N N     . LEU A 1 2580 ? 202.015 236.346 170.614 1.00 4.53  ? 2580 LEU A N     1 
ATOM   8631  C CA    . LEU A 1 2580 ? 202.171 236.405 172.067 1.00 5.69  ? 2580 LEU A CA    1 
ATOM   8632  C C     . LEU A 1 2580 ? 203.610 236.143 172.500 1.00 6.42  ? 2580 LEU A C     1 
ATOM   8633  O O     . LEU A 1 2580 ? 204.087 236.743 173.469 1.00 12.22 ? 2580 LEU A O     1 
ATOM   8634  C CB    . LEU A 1 2580 ? 201.229 235.439 172.779 1.00 2.45  ? 2580 LEU A CB    1 
ATOM   8635  C CG    . LEU A 1 2580 ? 199.776 235.874 172.960 1.00 2.52  ? 2580 LEU A CG    1 
ATOM   8636  C CD1   . LEU A 1 2580 ? 198.954 235.855 171.680 1.00 6.60  ? 2580 LEU A CD1   1 
ATOM   8637  C CD2   . LEU A 1 2580 ? 199.147 235.040 174.052 1.00 1.85  ? 2580 LEU A CD2   1 
ATOM   8638  N N     . LEU A 1 2581 ? 204.310 235.232 171.822 1.00 3.08  ? 2581 LEU A N     1 
ATOM   8639  C CA    . LEU A 1 2581 ? 205.704 234.984 172.176 1.00 3.78  ? 2581 LEU A CA    1 
ATOM   8640  C C     . LEU A 1 2581 ? 206.560 236.220 171.936 1.00 7.18  ? 2581 LEU A C     1 
ATOM   8641  O O     . LEU A 1 2581 ? 207.421 236.555 172.756 1.00 13.75 ? 2581 LEU A O     1 
ATOM   8642  C CB    . LEU A 1 2581 ? 206.253 233.786 171.402 1.00 8.11  ? 2581 LEU A CB    1 
ATOM   8643  C CG    . LEU A 1 2581 ? 205.561 232.434 171.598 1.00 8.01  ? 2581 LEU A CG    1 
ATOM   8644  C CD1   . LEU A 1 2581 ? 206.505 231.305 171.245 1.00 10.94 ? 2581 LEU A CD1   1 
ATOM   8645  C CD2   . LEU A 1 2581 ? 205.042 232.272 173.018 1.00 4.74  ? 2581 LEU A CD2   1 
ATOM   8646  N N     . TYR A 1 2582 ? 206.332 236.917 170.821 1.00 8.05  ? 2582 TYR A N     1 
ATOM   8647  C CA    . TYR A 1 2582 ? 207.017 238.186 170.590 1.00 8.18  ? 2582 TYR A CA    1 
ATOM   8648  C C     . TYR A 1 2582 ? 206.688 239.189 171.688 1.00 9.59  ? 2582 TYR A C     1 
ATOM   8649  O O     . TYR A 1 2582 ? 207.583 239.861 172.217 1.00 8.63  ? 2582 TYR A O     1 
ATOM   8650  C CB    . TYR A 1 2582 ? 206.626 238.746 169.223 1.00 6.94  ? 2582 TYR A CB    1 
ATOM   8651  C CG    . TYR A 1 2582 ? 207.602 238.433 168.115 1.00 10.24 ? 2582 TYR A CG    1 
ATOM   8652  C CD1   . TYR A 1 2582 ? 208.659 239.287 167.836 1.00 11.52 ? 2582 TYR A CD1   1 
ATOM   8653  C CD2   . TYR A 1 2582 ? 207.469 237.282 167.350 1.00 10.81 ? 2582 TYR A CD2   1 
ATOM   8654  C CE1   . TYR A 1 2582 ? 209.551 239.010 166.819 1.00 13.12 ? 2582 TYR A CE1   1 
ATOM   8655  C CE2   . TYR A 1 2582 ? 208.360 236.992 166.335 1.00 12.68 ? 2582 TYR A CE2   1 
ATOM   8656  C CZ    . TYR A 1 2582 ? 209.401 237.859 166.075 1.00 15.30 ? 2582 TYR A CZ    1 
ATOM   8657  O OH    . TYR A 1 2582 ? 210.291 237.576 165.064 1.00 13.60 ? 2582 TYR A OH    1 
ATOM   8658  N N     . THR A 1 2583 ? 205.407 239.283 172.055 1.00 7.96  ? 2583 THR A N     1 
ATOM   8659  C CA    . THR A 1 2583 ? 204.986 240.226 173.086 1.00 5.77  ? 2583 THR A CA    1 
ATOM   8660  C C     . THR A 1 2583 ? 205.681 239.952 174.413 1.00 7.74  ? 2583 THR A C     1 
ATOM   8661  O O     . THR A 1 2583 ? 206.170 240.877 175.071 1.00 13.95 ? 2583 THR A O     1 
ATOM   8662  C CB    . THR A 1 2583 ? 203.468 240.159 173.260 1.00 3.20  ? 2583 THR A CB    1 
ATOM   8663  O OG1   . THR A 1 2583 ? 202.825 240.501 172.026 1.00 13.62 ? 2583 THR A OG1   1 
ATOM   8664  C CG2   . THR A 1 2583 ? 203.001 241.091 174.357 1.00 1.85  ? 2583 THR A CG2   1 
ATOM   8665  N N     . TRP A 1 2584 ? 205.744 238.687 174.817 1.00 10.05 ? 2584 TRP A N     1 
ATOM   8666  C CA    . TRP A 1 2584 ? 206.254 238.344 176.136 1.00 2.68  ? 2584 TRP A CA    1 
ATOM   8667  C C     . TRP A 1 2584 ? 207.766 238.174 176.167 1.00 5.18  ? 2584 TRP A C     1 
ATOM   8668  O O     . TRP A 1 2584 ? 208.342 238.140 177.259 1.00 14.53 ? 2584 TRP A O     1 
ATOM   8669  C CB    . TRP A 1 2584 ? 205.576 237.072 176.638 1.00 3.64  ? 2584 TRP A CB    1 
ATOM   8670  C CG    . TRP A 1 2584 ? 204.252 237.341 177.265 1.00 5.82  ? 2584 TRP A CG    1 
ATOM   8671  C CD1   . TRP A 1 2584 ? 203.905 238.429 178.007 1.00 10.56 ? 2584 TRP A CD1   1 
ATOM   8672  C CD2   . TRP A 1 2584 ? 203.088 236.513 177.199 1.00 4.36  ? 2584 TRP A CD2   1 
ATOM   8673  N NE1   . TRP A 1 2584 ? 202.597 238.331 178.410 1.00 5.05  ? 2584 TRP A NE1   1 
ATOM   8674  C CE2   . TRP A 1 2584 ? 202.074 237.162 177.927 1.00 3.49  ? 2584 TRP A CE2   1 
ATOM   8675  C CE3   . TRP A 1 2584 ? 202.806 235.285 176.598 1.00 7.80  ? 2584 TRP A CE3   1 
ATOM   8676  C CZ2   . TRP A 1 2584 ? 200.800 236.624 178.070 1.00 6.04  ? 2584 TRP A CZ2   1 
ATOM   8677  C CZ3   . TRP A 1 2584 ? 201.542 234.754 176.742 1.00 11.53 ? 2584 TRP A CZ3   1 
ATOM   8678  C CH2   . TRP A 1 2584 ? 200.554 235.421 177.472 1.00 8.74  ? 2584 TRP A CH2   1 
ATOM   8679  N N     . LEU A 1 2585 ? 208.421 238.062 175.012 1.00 7.50  ? 2585 LEU A N     1 
ATOM   8680  C CA    . LEU A 1 2585 ? 209.875 238.081 174.966 1.00 8.81  ? 2585 LEU A CA    1 
ATOM   8681  C C     . LEU A 1 2585 ? 210.444 239.480 174.790 1.00 15.02 ? 2585 LEU A C     1 
ATOM   8682  O O     . LEU A 1 2585 ? 211.587 239.720 175.195 1.00 17.96 ? 2585 LEU A O     1 
ATOM   8683  C CB    . LEU A 1 2585 ? 210.388 237.187 173.835 1.00 14.67 ? 2585 LEU A CB    1 
ATOM   8684  C CG    . LEU A 1 2585 ? 210.744 235.740 174.175 1.00 13.11 ? 2585 LEU A CG    1 
ATOM   8685  C CD1   . LEU A 1 2585 ? 209.509 234.906 174.449 1.00 12.93 ? 2585 LEU A CD1   1 
ATOM   8686  C CD2   . LEU A 1 2585 ? 211.550 235.144 173.045 1.00 13.81 ? 2585 LEU A CD2   1 
ATOM   8687  N N     . ALA A 1 2586 ? 209.686 240.403 174.191 1.00 14.66 ? 2586 ALA A N     1 
ATOM   8688  C CA    . ALA A 1 2586 ? 210.141 241.787 174.140 1.00 13.47 ? 2586 ALA A CA    1 
ATOM   8689  C C     . ALA A 1 2586 ? 210.259 242.382 175.536 1.00 13.41 ? 2586 ALA A C     1 
ATOM   8690  O O     . ALA A 1 2586 ? 211.032 243.324 175.747 1.00 18.88 ? 2586 ALA A O     1 
ATOM   8691  C CB    . ALA A 1 2586 ? 209.196 242.623 173.279 1.00 12.23 ? 2586 ALA A CB    1 
ATOM   8692  N N     . GLU A 1 2587 ? 209.505 241.851 176.494 1.00 7.26  ? 2587 GLU A N     1 
ATOM   8693  C CA    . GLU A 1 2587 ? 209.604 242.239 177.893 1.00 11.39 ? 2587 GLU A CA    1 
ATOM   8694  C C     . GLU A 1 2587 ? 210.673 241.446 178.637 1.00 13.97 ? 2587 GLU A C     1 
ATOM   8695  O O     . GLU A 1 2587 ? 210.971 241.764 179.793 1.00 14.71 ? 2587 GLU A O     1 
ATOM   8696  C CB    . GLU A 1 2587 ? 208.239 242.059 178.574 1.00 11.86 ? 2587 GLU A CB    1 
ATOM   8697  C CG    . GLU A 1 2587 ? 208.107 242.686 179.956 1.00 11.92 ? 2587 GLU A CG    1 
ATOM   8698  C CD    . GLU A 1 2587 ? 207.481 244.064 179.916 1.00 13.33 ? 2587 GLU A CD    1 
ATOM   8699  O OE1   . GLU A 1 2587 ? 207.142 244.595 180.994 1.00 9.33  ? 2587 GLU A OE1   1 
ATOM   8700  O OE2   . GLU A 1 2587 ? 207.325 244.616 178.807 1.00 14.36 ? 2587 GLU A OE2   1 
ATOM   8701  N N     . HIS A 1 2588 ? 211.266 240.440 177.989 1.00 16.01 ? 2588 HIS A N     1 
ATOM   8702  C CA    . HIS A 1 2588 ? 212.203 239.514 178.630 1.00 14.12 ? 2588 HIS A CA    1 
ATOM   8703  C C     . HIS A 1 2588 ? 211.555 238.817 179.823 1.00 12.14 ? 2588 HIS A C     1 
ATOM   8704  O O     . HIS A 1 2588 ? 212.216 238.476 180.805 1.00 21.12 ? 2588 HIS A O     1 
ATOM   8705  C CB    . HIS A 1 2588 ? 213.499 240.218 179.043 1.00 17.62 ? 2588 HIS A CB    1 
ATOM   8706  C CG    . HIS A 1 2588 ? 214.143 240.997 177.939 1.00 19.45 ? 2588 HIS A CG    1 
ATOM   8707  N ND1   . HIS A 1 2588 ? 214.915 240.405 176.963 1.00 18.99 ? 2588 HIS A ND1   1 
ATOM   8708  C CD2   . HIS A 1 2588 ? 214.136 242.322 177.660 1.00 17.31 ? 2588 HIS A CD2   1 
ATOM   8709  C CE1   . HIS A 1 2588 ? 215.352 241.330 176.128 1.00 21.08 ? 2588 HIS A CE1   1 
ATOM   8710  N NE2   . HIS A 1 2588 ? 214.893 242.502 176.529 1.00 22.82 ? 2588 HIS A NE2   1 
ATOM   8711  N N     . LYS A 1 2589 ? 210.249 238.600 179.732 1.00 9.75  ? 2589 LYS A N     1 
ATOM   8712  C CA    . LYS A 1 2589 ? 209.460 237.929 180.759 1.00 10.65 ? 2589 LYS A CA    1 
ATOM   8713  C C     . LYS A 1 2589 ? 209.506 236.422 180.553 1.00 9.15  ? 2589 LYS A C     1 
ATOM   8714  O O     . LYS A 1 2589 ? 209.218 235.947 179.448 1.00 14.65 ? 2589 LYS A O     1 
ATOM   8715  C CB    . LYS A 1 2589 ? 208.016 238.406 180.728 1.00 9.96  ? 2589 LYS A CB    1 
ATOM   8716  C CG    . LYS A 1 2589 ? 207.090 237.625 181.643 1.00 12.36 ? 2589 LYS A CG    1 
ATOM   8717  C CD    . LYS A 1 2589 ? 205.760 238.333 181.828 1.00 14.75 ? 2589 LYS A CD    1 
ATOM   8718  C CE    . LYS A 1 2589 ? 205.891 239.504 182.782 1.00 11.72 ? 2589 LYS A CE    1 
ATOM   8719  N NZ    . LYS A 1 2589 ? 206.184 239.047 184.168 1.00 12.22 ? 2589 LYS A NZ    1 
ATOM   8720  N N     . PRO A 1 2590 ? 209.873 235.648 181.572 1.00 11.91 ? 2590 PRO A N     1 
ATOM   8721  C CA    . PRO A 1 2590 ? 209.837 234.188 181.435 1.00 17.97 ? 2590 PRO A CA    1 
ATOM   8722  C C     . PRO A 1 2590 ? 208.425 233.698 181.159 1.00 12.36 ? 2590 PRO A C     1 
ATOM   8723  O O     . PRO A 1 2590 ? 207.447 234.257 181.657 1.00 17.35 ? 2590 PRO A O     1 
ATOM   8724  C CB    . PRO A 1 2590 ? 210.351 233.694 182.791 1.00 9.79  ? 2590 PRO A CB    1 
ATOM   8725  C CG    . PRO A 1 2590 ? 211.137 234.840 183.331 1.00 11.70 ? 2590 PRO A CG    1 
ATOM   8726  C CD    . PRO A 1 2590 ? 210.407 236.062 182.878 1.00 10.00 ? 2590 PRO A CD    1 
ATOM   8727  N N     . LEU A 1 2591 ? 208.324 232.647 180.349 1.00 3.49  ? 2591 LEU A N     1 
ATOM   8728  C CA    . LEU A 1 2591 ? 207.031 232.065 180.022 1.00 4.85  ? 2591 LEU A CA    1 
ATOM   8729  C C     . LEU A 1 2591 ? 207.188 230.559 179.888 1.00 9.77  ? 2591 LEU A C     1 
ATOM   8730  O O     . LEU A 1 2591 ? 208.289 230.046 179.674 1.00 13.57 ? 2591 LEU A O     1 
ATOM   8731  C CB    . LEU A 1 2591 ? 206.438 232.680 178.743 1.00 6.96  ? 2591 LEU A CB    1 
ATOM   8732  C CG    . LEU A 1 2591 ? 207.185 232.599 177.405 1.00 10.74 ? 2591 LEU A CG    1 
ATOM   8733  C CD1   . LEU A 1 2591 ? 206.994 231.261 176.706 1.00 11.73 ? 2591 LEU A CD1   1 
ATOM   8734  C CD2   . LEU A 1 2591 ? 206.752 233.728 176.494 1.00 5.84  ? 2591 LEU A CD2   1 
ATOM   8735  N N     . VAL A 1 2592 ? 206.068 229.854 180.023 1.00 9.26  ? 2592 VAL A N     1 
ATOM   8736  C CA    . VAL A 1 2592 ? 206.026 228.403 179.906 1.00 3.74  ? 2592 VAL A CA    1 
ATOM   8737  C C     . VAL A 1 2592 ? 204.939 228.031 178.909 1.00 9.57  ? 2592 VAL A C     1 
ATOM   8738  O O     . VAL A 1 2592 ? 203.790 228.462 179.048 1.00 4.33  ? 2592 VAL A O     1 
ATOM   8739  C CB    . VAL A 1 2592 ? 205.771 227.724 181.264 1.00 1.29  ? 2592 VAL A CB    1 
ATOM   8740  C CG1   . VAL A 1 2592 ? 205.611 226.228 181.083 1.00 6.69  ? 2592 VAL A CG1   1 
ATOM   8741  C CG2   . VAL A 1 2592 ? 206.913 228.018 182.222 1.00 6.47  ? 2592 VAL A CG2   1 
ATOM   8742  N N     . LEU A 1 2593 ? 205.301 227.235 177.909 1.00 14.44 ? 2593 LEU A N     1 
ATOM   8743  C CA    . LEU A 1 2593 ? 204.368 226.775 176.889 1.00 3.64  ? 2593 LEU A CA    1 
ATOM   8744  C C     . LEU A 1 2593 ? 203.811 225.422 177.314 1.00 6.94  ? 2593 LEU A C     1 
ATOM   8745  O O     . LEU A 1 2593 ? 204.559 224.448 177.428 1.00 13.41 ? 2593 LEU A O     1 
ATOM   8746  C CB    . LEU A 1 2593 ? 205.062 226.674 175.531 1.00 0.00  ? 2593 LEU A CB    1 
ATOM   8747  C CG    . LEU A 1 2593 ? 205.272 227.992 174.785 1.00 4.25  ? 2593 LEU A CG    1 
ATOM   8748  C CD1   . LEU A 1 2593 ? 206.472 227.898 173.861 1.00 4.10  ? 2593 LEU A CD1   1 
ATOM   8749  C CD2   . LEU A 1 2593 ? 204.027 228.379 174.012 1.00 9.43  ? 2593 LEU A CD2   1 
ATOM   8750  N N     . CYS A 1 2594 ? 202.505 225.359 177.544 1.00 2.73  ? 2594 CYS A N     1 
ATOM   8751  C CA    . CYS A 1 2594 ? 201.858 224.153 178.040 1.00 1.40  ? 2594 CYS A CA    1 
ATOM   8752  C C     . CYS A 1 2594 ? 200.971 223.564 176.954 1.00 4.61  ? 2594 CYS A C     1 
ATOM   8753  O O     . CYS A 1 2594 ? 200.251 224.297 176.272 1.00 12.38 ? 2594 CYS A O     1 
ATOM   8754  C CB    . CYS A 1 2594 ? 201.034 224.452 179.293 1.00 5.25  ? 2594 CYS A CB    1 
ATOM   8755  S SG    . CYS A 1 2594 ? 200.177 223.021 179.968 1.00 18.87 ? 2594 CYS A SG    1 
ATOM   8756  N N     . GLY A 1 2595 ? 201.033 222.246 176.788 1.00 5.20  ? 2595 GLY A N     1 
ATOM   8757  C CA    . GLY A 1 2595 ? 200.205 221.571 175.819 1.00 8.70  ? 2595 GLY A CA    1 
ATOM   8758  C C     . GLY A 1 2595 ? 200.453 220.079 175.758 1.00 10.11 ? 2595 GLY A C     1 
ATOM   8759  O O     . GLY A 1 2595 ? 201.422 219.560 176.319 1.00 4.34  ? 2595 GLY A O     1 
ATOM   8760  N N     . PRO A 1 2596 ? 199.572 219.359 175.065 1.00 14.39 ? 2596 PRO A N     1 
ATOM   8761  C CA    . PRO A 1 2596 ? 199.762 217.921 174.921 1.00 6.66  ? 2596 PRO A CA    1 
ATOM   8762  C C     . PRO A 1 2596 ? 201.021 217.630 174.129 1.00 9.66  ? 2596 PRO A C     1 
ATOM   8763  O O     . PRO A 1 2596 ? 201.504 218.485 173.364 1.00 15.31 ? 2596 PRO A O     1 
ATOM   8764  C CB    . PRO A 1 2596 ? 198.505 217.475 174.163 1.00 8.50  ? 2596 PRO A CB    1 
ATOM   8765  C CG    . PRO A 1 2596 ? 197.498 218.531 174.439 1.00 8.75  ? 2596 PRO A CG    1 
ATOM   8766  C CD    . PRO A 1 2596 ? 198.281 219.803 174.517 1.00 8.56  ? 2596 PRO A CD    1 
ATOM   8767  N N     . PRO A 1 2597 ? 201.602 216.443 174.299 1.00 5.34  ? 2597 PRO A N     1 
ATOM   8768  C CA    . PRO A 1 2597 ? 202.854 216.128 173.596 1.00 7.68  ? 2597 PRO A CA    1 
ATOM   8769  C C     . PRO A 1 2597 ? 202.682 216.210 172.086 1.00 7.93  ? 2597 PRO A C     1 
ATOM   8770  O O     . PRO A 1 2597 ? 201.665 215.784 171.535 1.00 8.76  ? 2597 PRO A O     1 
ATOM   8771  C CB    . PRO A 1 2597 ? 203.163 214.697 174.049 1.00 5.23  ? 2597 PRO A CB    1 
ATOM   8772  C CG    . PRO A 1 2597 ? 202.442 214.539 175.338 1.00 8.83  ? 2597 PRO A CG    1 
ATOM   8773  C CD    . PRO A 1 2597 ? 201.204 215.375 175.230 1.00 7.02  ? 2597 PRO A CD    1 
ATOM   8774  N N     . GLY A 1 2598 ? 203.691 216.766 171.418 1.00 1.62  ? 2598 GLY A N     1 
ATOM   8775  C CA    . GLY A 1 2598 ? 203.695 216.871 169.977 1.00 1.57  ? 2598 GLY A CA    1 
ATOM   8776  C C     . GLY A 1 2598 ? 202.772 217.923 169.402 1.00 7.09  ? 2598 GLY A C     1 
ATOM   8777  O O     . GLY A 1 2598 ? 202.598 217.965 168.178 1.00 8.55  ? 2598 GLY A O     1 
ATOM   8778  N N     . SER A 1 2599 ? 202.178 218.776 170.240 1.00 9.89  ? 2599 SER A N     1 
ATOM   8779  C CA    . SER A 1 2599 ? 201.206 219.746 169.747 1.00 4.11  ? 2599 SER A CA    1 
ATOM   8780  C C     . SER A 1 2599 ? 201.881 220.878 168.982 1.00 3.24  ? 2599 SER A C     1 
ATOM   8781  O O     . SER A 1 2599 ? 201.244 221.543 168.157 1.00 14.92 ? 2599 SER A O     1 
ATOM   8782  C CB    . SER A 1 2599 ? 200.383 220.300 170.909 1.00 5.62  ? 2599 SER A CB    1 
ATOM   8783  O OG    . SER A 1 2599 ? 201.221 220.877 171.894 1.00 10.25 ? 2599 SER A OG    1 
ATOM   8784  N N     . GLY A 1 2600 ? 203.161 221.119 169.244 1.00 0.00  ? 2600 GLY A N     1 
ATOM   8785  C CA    . GLY A 1 2600 ? 203.892 222.137 168.515 1.00 2.79  ? 2600 GLY A CA    1 
ATOM   8786  C C     . GLY A 1 2600 ? 204.445 223.242 169.390 1.00 5.84  ? 2600 GLY A C     1 
ATOM   8787  O O     . GLY A 1 2600 ? 204.673 224.357 168.915 1.00 7.76  ? 2600 GLY A O     1 
ATOM   8788  N N     . LYS A 1 2601 ? 204.671 222.941 170.669 1.00 11.37 ? 2601 LYS A N     1 
ATOM   8789  C CA    . LYS A 1 2601 ? 205.182 223.950 171.592 1.00 2.23  ? 2601 LYS A CA    1 
ATOM   8790  C C     . LYS A 1 2601 ? 206.611 224.339 171.241 1.00 0.00  ? 2601 LYS A C     1 
ATOM   8791  O O     . LYS A 1 2601 ? 206.948 225.527 171.186 1.00 7.58  ? 2601 LYS A O     1 
ATOM   8792  C CB    . LYS A 1 2601 ? 205.116 223.425 173.025 1.00 2.05  ? 2601 LYS A CB    1 
ATOM   8793  C CG    . LYS A 1 2601 ? 203.719 223.126 173.521 1.00 0.73  ? 2601 LYS A CG    1 
ATOM   8794  C CD    . LYS A 1 2601 ? 203.768 222.491 174.897 1.00 3.15  ? 2601 LYS A CD    1 
ATOM   8795  C CE    . LYS A 1 2601 ? 204.316 221.079 174.834 1.00 5.02  ? 2601 LYS A CE    1 
ATOM   8796  N NZ    . LYS A 1 2601 ? 203.395 220.155 174.125 1.00 0.33  ? 2601 LYS A NZ    1 
ATOM   8797  N N     . THR A 1 2602 ? 207.469 223.344 171.008 1.00 0.83  ? 2602 THR A N     1 
ATOM   8798  C CA    . THR A 1 2602 ? 208.868 223.623 170.701 1.00 3.44  ? 2602 THR A CA    1 
ATOM   8799  C C     . THR A 1 2602 ? 209.011 224.306 169.347 1.00 9.72  ? 2602 THR A C     1 
ATOM   8800  O O     . THR A 1 2602 ? 209.814 225.233 169.192 1.00 17.81 ? 2602 THR A O     1 
ATOM   8801  C CB    . THR A 1 2602 ? 209.676 222.326 170.734 1.00 8.47  ? 2602 THR A CB    1 
ATOM   8802  O OG1   . THR A 1 2602 ? 209.497 221.688 172.003 1.00 16.02 ? 2602 THR A OG1   1 
ATOM   8803  C CG2   . THR A 1 2602 ? 211.147 222.610 170.531 1.00 8.10  ? 2602 THR A CG2   1 
ATOM   8804  N N     . MET A 1 2603 ? 208.241 223.858 168.355 1.00 9.93  ? 2603 MET A N     1 
ATOM   8805  C CA    . MET A 1 2603 ? 208.333 224.440 167.021 1.00 9.92  ? 2603 MET A CA    1 
ATOM   8806  C C     . MET A 1 2603 ? 207.813 225.872 167.010 1.00 6.74  ? 2603 MET A C     1 
ATOM   8807  O O     . MET A 1 2603 ? 208.356 226.737 166.314 1.00 9.61  ? 2603 MET A O     1 
ATOM   8808  C CB    . MET A 1 2603 ? 207.571 223.567 166.023 1.00 10.26 ? 2603 MET A CB    1 
ATOM   8809  C CG    . MET A 1 2603 ? 207.214 224.262 164.730 1.00 13.04 ? 2603 MET A CG    1 
ATOM   8810  S SD    . MET A 1 2603 ? 205.627 223.732 164.077 1.00 20.82 ? 2603 MET A SD    1 
ATOM   8811  C CE    . MET A 1 2603 ? 204.498 224.642 165.124 1.00 9.44  ? 2603 MET A CE    1 
ATOM   8812  N N     . THR A 1 2604 ? 206.758 226.144 167.783 1.00 6.36  ? 2604 THR A N     1 
ATOM   8813  C CA    . THR A 1 2604 ? 206.230 227.502 167.863 1.00 6.28  ? 2604 THR A CA    1 
ATOM   8814  C C     . THR A 1 2604 ? 207.241 228.452 168.490 1.00 10.04 ? 2604 THR A C     1 
ATOM   8815  O O     . THR A 1 2604 ? 207.292 229.634 168.131 1.00 12.17 ? 2604 THR A O     1 
ATOM   8816  C CB    . THR A 1 2604 ? 204.930 227.515 168.667 1.00 6.67  ? 2604 THR A CB    1 
ATOM   8817  O OG1   . THR A 1 2604 ? 204.037 226.523 168.149 1.00 18.46 ? 2604 THR A OG1   1 
ATOM   8818  C CG2   . THR A 1 2604 ? 204.257 228.873 168.580 1.00 9.63  ? 2604 THR A CG2   1 
ATOM   8819  N N     . LEU A 1 2605 ? 208.057 227.952 169.416 1.00 8.66  ? 2605 LEU A N     1 
ATOM   8820  C CA    . LEU A 1 2605 ? 209.047 228.792 170.078 1.00 6.54  ? 2605 LEU A CA    1 
ATOM   8821  C C     . LEU A 1 2605 ? 210.232 229.089 169.168 1.00 15.71 ? 2605 LEU A C     1 
ATOM   8822  O O     . LEU A 1 2605 ? 210.593 230.253 168.970 1.00 22.61 ? 2605 LEU A O     1 
ATOM   8823  C CB    . LEU A 1 2605 ? 209.521 228.121 171.362 1.00 3.50  ? 2605 LEU A CB    1 
ATOM   8824  C CG    . LEU A 1 2605 ? 210.323 229.028 172.288 1.00 12.07 ? 2605 LEU A CG    1 
ATOM   8825  C CD1   . LEU A 1 2605 ? 209.422 230.049 172.955 1.00 14.28 ? 2605 LEU A CD1   1 
ATOM   8826  C CD2   . LEU A 1 2605 ? 211.056 228.192 173.309 1.00 15.26 ? 2605 LEU A CD2   1 
ATOM   8827  N N     . PHE A 1 2606 ? 210.854 228.049 168.609 1.00 11.65 ? 2606 PHE A N     1 
ATOM   8828  C CA    . PHE A 1 2606 ? 212.010 228.254 167.746 1.00 7.97  ? 2606 PHE A CA    1 
ATOM   8829  C C     . PHE A 1 2606 ? 211.663 228.963 166.447 1.00 10.73 ? 2606 PHE A C     1 
ATOM   8830  O O     . PHE A 1 2606 ? 212.573 229.455 165.772 1.00 22.93 ? 2606 PHE A O     1 
ATOM   8831  C CB    . PHE A 1 2606 ? 212.688 226.919 167.445 1.00 14.66 ? 2606 PHE A CB    1 
ATOM   8832  C CG    . PHE A 1 2606 ? 213.515 226.397 168.579 1.00 13.54 ? 2606 PHE A CG    1 
ATOM   8833  C CD1   . PHE A 1 2606 ? 213.120 225.280 169.290 1.00 14.34 ? 2606 PHE A CD1   1 
ATOM   8834  C CD2   . PHE A 1 2606 ? 214.693 227.029 168.935 1.00 14.20 ? 2606 PHE A CD2   1 
ATOM   8835  C CE1   . PHE A 1 2606 ? 213.885 224.804 170.334 1.00 14.48 ? 2606 PHE A CE1   1 
ATOM   8836  C CE2   . PHE A 1 2606 ? 215.462 226.556 169.976 1.00 18.59 ? 2606 PHE A CE2   1 
ATOM   8837  C CZ    . PHE A 1 2606 ? 215.057 225.442 170.677 1.00 16.25 ? 2606 PHE A CZ    1 
ATOM   8838  N N     . SER A 1 2607 ? 210.383 229.035 166.081 1.00 12.27 ? 2607 SER A N     1 
ATOM   8839  C CA    . SER A 1 2607 ? 209.995 229.843 164.933 1.00 16.23 ? 2607 SER A CA    1 
ATOM   8840  C C     . SER A 1 2607 ? 209.962 231.325 165.275 1.00 15.24 ? 2607 SER A C     1 
ATOM   8841  O O     . SER A 1 2607 ? 209.784 232.154 164.377 1.00 16.91 ? 2607 SER A O     1 
ATOM   8842  C CB    . SER A 1 2607 ? 208.637 229.389 164.400 1.00 14.79 ? 2607 SER A CB    1 
ATOM   8843  O OG    . SER A 1 2607 ? 207.597 229.714 165.303 1.00 13.16 ? 2607 SER A OG    1 
ATOM   8844  N N     . ALA A 1 2608 ? 210.125 231.671 166.550 1.00 16.61 ? 2608 ALA A N     1 
ATOM   8845  C CA    . ALA A 1 2608 ? 210.236 233.052 166.992 1.00 18.19 ? 2608 ALA A CA    1 
ATOM   8846  C C     . ALA A 1 2608 ? 211.587 233.389 167.603 1.00 21.25 ? 2608 ALA A C     1 
ATOM   8847  O O     . ALA A 1 2608 ? 212.041 234.525 167.459 1.00 28.17 ? 2608 ALA A O     1 
ATOM   8848  C CB    . ALA A 1 2608 ? 209.136 233.378 168.014 1.00 15.25 ? 2608 ALA A CB    1 
ATOM   8849  N N     . LEU A 1 2609 ? 212.240 232.438 168.274 1.00 19.16 ? 2609 LEU A N     1 
ATOM   8850  C CA    . LEU A 1 2609 ? 213.531 232.715 168.898 1.00 21.58 ? 2609 LEU A CA    1 
ATOM   8851  C C     . LEU A 1 2609 ? 214.598 233.023 167.856 1.00 30.49 ? 2609 LEU A C     1 
ATOM   8852  O O     . LEU A 1 2609 ? 215.161 234.124 167.831 1.00 31.69 ? 2609 LEU A O     1 
ATOM   8853  C CB    . LEU A 1 2609 ? 213.967 231.527 169.753 1.00 24.04 ? 2609 LEU A CB    1 
ATOM   8854  C CG    . LEU A 1 2609 ? 213.179 231.161 171.004 1.00 21.65 ? 2609 LEU A CG    1 
ATOM   8855  C CD1   . LEU A 1 2609 ? 213.728 229.874 171.582 1.00 22.52 ? 2609 LEU A CD1   1 
ATOM   8856  C CD2   . LEU A 1 2609 ? 213.284 232.272 172.015 1.00 23.69 ? 2609 LEU A CD2   1 
ATOM   8857  N N     . ARG A 1 2610 ? 214.893 232.056 166.986 1.00 32.96 ? 2610 ARG A N     1 
ATOM   8858  C CA    . ARG A 1 2610 ? 215.967 232.223 166.016 1.00 35.69 ? 2610 ARG A CA    1 
ATOM   8859  C C     . ARG A 1 2610 ? 215.635 233.251 164.944 1.00 35.01 ? 2610 ARG A C     1 
ATOM   8860  O O     . ARG A 1 2610 ? 216.531 233.655 164.194 1.00 36.22 ? 2610 ARG A O     1 
ATOM   8861  C CB    . ARG A 1 2610 ? 216.309 230.875 165.379 1.00 34.21 ? 2610 ARG A CB    1 
ATOM   8862  C CG    . ARG A 1 2610 ? 216.862 229.863 166.376 1.00 33.40 ? 2610 ARG A CG    1 
ATOM   8863  C CD    . ARG A 1 2610 ? 217.320 228.584 165.695 1.00 37.04 ? 2610 ARG A CD    1 
ATOM   8864  N NE    . ARG A 1 2610 ? 217.673 227.551 166.663 1.00 40.07 ? 2610 ARG A NE    1 
ATOM   8865  C CZ    . ARG A 1 2610 ? 218.859 227.445 167.249 1.00 38.90 ? 2610 ARG A CZ    1 
ATOM   8866  N NH1   . ARG A 1 2610 ? 219.839 228.294 166.986 1.00 38.41 ? 2610 ARG A NH1   1 
ATOM   8867  N NH2   . ARG A 1 2610 ? 219.067 226.461 168.119 1.00 36.02 ? 2610 ARG A NH2   1 
ATOM   8868  N N     . ALA A 1 2611 ? 214.374 233.679 164.851 1.00 27.14 ? 2611 ALA A N     1 
ATOM   8869  C CA    . ALA A 1 2611 ? 214.050 234.828 164.015 1.00 29.64 ? 2611 ALA A CA    1 
ATOM   8870  C C     . ALA A 1 2611 ? 214.703 236.094 164.556 1.00 33.33 ? 2611 ALA A C     1 
ATOM   8871  O O     . ALA A 1 2611 ? 215.177 236.935 163.783 1.00 31.52 ? 2611 ALA A O     1 
ATOM   8872  C CB    . ALA A 1 2611 ? 212.534 235.000 163.921 1.00 25.68 ? 2611 ALA A CB    1 
ATOM   8873  N N     . LEU A 1 2612 ? 214.742 236.240 165.875 1.00 31.71 ? 2612 LEU A N     1 
ATOM   8874  C CA    . LEU A 1 2612 ? 215.358 237.412 166.484 1.00 28.94 ? 2612 LEU A CA    1 
ATOM   8875  C C     . LEU A 1 2612 ? 216.869 237.362 166.290 1.00 30.18 ? 2612 LEU A C     1 
ATOM   8876  O O     . LEU A 1 2612 ? 217.497 236.349 166.621 1.00 28.39 ? 2612 LEU A O     1 
ATOM   8877  C CB    . LEU A 1 2612 ? 215.025 237.480 167.969 1.00 23.80 ? 2612 LEU A CB    1 
ATOM   8878  C CG    . LEU A 1 2612 ? 213.834 238.340 168.383 1.00 25.76 ? 2612 LEU A CG    1 
ATOM   8879  C CD1   . LEU A 1 2612 ? 212.575 237.806 167.745 1.00 26.58 ? 2612 LEU A CD1   1 
ATOM   8880  C CD2   . LEU A 1 2612 ? 213.696 238.371 169.893 1.00 31.66 ? 2612 LEU A CD2   1 
ATOM   8881  N N     . PRO A 1 2613 ? 217.483 238.418 165.751 1.00 34.46 ? 2613 PRO A N     1 
ATOM   8882  C CA    . PRO A 1 2613 ? 218.932 238.364 165.484 1.00 33.75 ? 2613 PRO A CA    1 
ATOM   8883  C C     . PRO A 1 2613 ? 219.783 238.142 166.724 1.00 35.66 ? 2613 PRO A C     1 
ATOM   8884  O O     . PRO A 1 2613 ? 220.774 237.403 166.665 1.00 33.77 ? 2613 PRO A O     1 
ATOM   8885  C CB    . PRO A 1 2613 ? 219.216 239.731 164.844 1.00 33.25 ? 2613 PRO A CB    1 
ATOM   8886  C CG    . PRO A 1 2613 ? 217.889 240.204 164.333 1.00 34.15 ? 2613 PRO A CG    1 
ATOM   8887  C CD    . PRO A 1 2613 ? 216.884 239.688 165.311 1.00 33.61 ? 2613 PRO A CD    1 
ATOM   8888  N N     . ASP A 1 2614 ? 219.425 238.757 167.848 1.00 32.76 ? 2614 ASP A N     1 
ATOM   8889  C CA    . ASP A 1 2614 ? 220.261 238.745 169.041 1.00 32.12 ? 2614 ASP A CA    1 
ATOM   8890  C C     . ASP A 1 2614 ? 219.786 237.771 170.111 1.00 31.92 ? 2614 ASP A C     1 
ATOM   8891  O O     . ASP A 1 2614 ? 220.411 237.688 171.172 1.00 34.45 ? 2614 ASP A O     1 
ATOM   8892  C CB    . ASP A 1 2614 ? 220.345 240.159 169.630 1.00 32.50 ? 2614 ASP A CB    1 
ATOM   8893  C CG    . ASP A 1 2614 ? 218.991 240.697 170.069 1.00 35.25 ? 2614 ASP A CG    1 
ATOM   8894  O OD1   . ASP A 1 2614 ? 217.970 240.005 169.873 1.00 34.62 ? 2614 ASP A OD1   1 
ATOM   8895  O OD2   . ASP A 1 2614 ? 218.948 241.821 170.611 1.00 36.74 ? 2614 ASP A OD2   1 
ATOM   8896  N N     . MET A 1 2615 ? 218.710 237.031 169.863 1.00 27.33 ? 2615 MET A N     1 
ATOM   8897  C CA    . MET A 1 2615 ? 218.109 236.184 170.889 1.00 22.94 ? 2615 MET A CA    1 
ATOM   8898  C C     . MET A 1 2615 ? 218.636 234.756 170.741 1.00 22.98 ? 2615 MET A C     1 
ATOM   8899  O O     . MET A 1 2615 ? 217.934 233.831 170.331 1.00 23.98 ? 2615 MET A O     1 
ATOM   8900  C CB    . MET A 1 2615 ? 216.589 236.241 170.792 1.00 27.77 ? 2615 MET A CB    1 
ATOM   8901  C CG    . MET A 1 2615 ? 215.860 235.506 171.889 1.00 29.26 ? 2615 MET A CG    1 
ATOM   8902  S SD    . MET A 1 2615 ? 216.224 236.286 173.467 1.00 37.84 ? 2615 MET A SD    1 
ATOM   8903  C CE    . MET A 1 2615 ? 215.279 237.797 173.311 1.00 24.56 ? 2615 MET A CE    1 
ATOM   8904  N N     . GLU A 1 2616 ? 219.915 234.596 171.072 1.00 25.99 ? 2616 GLU A N     1 
ATOM   8905  C CA    . GLU A 1 2616 ? 220.553 233.291 170.966 1.00 27.38 ? 2616 GLU A CA    1 
ATOM   8906  C C     . GLU A 1 2616 ? 219.952 232.324 171.979 1.00 22.41 ? 2616 GLU A C     1 
ATOM   8907  O O     . GLU A 1 2616 ? 219.654 232.696 173.117 1.00 28.82 ? 2616 GLU A O     1 
ATOM   8908  C CB    . GLU A 1 2616 ? 222.063 233.419 171.173 1.00 29.68 ? 2616 GLU A CB    1 
ATOM   8909  C CG    . GLU A 1 2616 ? 222.777 232.104 171.452 1.00 29.01 ? 2616 GLU A CG    1 
ATOM   8910  C CD    . GLU A 1 2616 ? 224.227 232.297 171.844 1.00 31.30 ? 2616 GLU A CD    1 
ATOM   8911  O OE1   . GLU A 1 2616 ? 224.811 233.337 171.476 1.00 31.94 ? 2616 GLU A OE1   1 
ATOM   8912  O OE2   . GLU A 1 2616 ? 224.786 231.404 172.514 1.00 31.18 ? 2616 GLU A OE2   1 
ATOM   8913  N N     . VAL A 1 2617 ? 219.773 231.075 171.559 1.00 18.66 ? 2617 VAL A N     1 
ATOM   8914  C CA    . VAL A 1 2617 ? 219.071 230.063 172.339 1.00 20.58 ? 2617 VAL A CA    1 
ATOM   8915  C C     . VAL A 1 2617 ? 220.075 229.032 172.831 1.00 22.43 ? 2617 VAL A C     1 
ATOM   8916  O O     . VAL A 1 2617 ? 220.969 228.620 172.082 1.00 29.41 ? 2617 VAL A O     1 
ATOM   8917  C CB    . VAL A 1 2617 ? 217.965 229.388 171.513 1.00 23.04 ? 2617 VAL A CB    1 
ATOM   8918  C CG1   . VAL A 1 2617 ? 217.055 228.569 172.413 1.00 14.85 ? 2617 VAL A CG1   1 
ATOM   8919  C CG2   . VAL A 1 2617 ? 217.185 230.430 170.740 1.00 25.37 ? 2617 VAL A CG2   1 
ATOM   8920  N N     . VAL A 1 2618 ? 219.927 228.620 174.086 1.00 18.71 ? 2618 VAL A N     1 
ATOM   8921  C CA    . VAL A 1 2618 ? 220.736 227.562 174.675 1.00 22.29 ? 2618 VAL A CA    1 
ATOM   8922  C C     . VAL A 1 2618 ? 219.820 226.388 174.985 1.00 18.03 ? 2618 VAL A C     1 
ATOM   8923  O O     . VAL A 1 2618 ? 218.923 226.499 175.829 1.00 16.09 ? 2618 VAL A O     1 
ATOM   8924  C CB    . VAL A 1 2618 ? 221.459 228.043 175.943 1.00 24.30 ? 2618 VAL A CB    1 
ATOM   8925  C CG1   . VAL A 1 2618 ? 222.141 226.875 176.644 1.00 19.24 ? 2618 VAL A CG1   1 
ATOM   8926  C CG2   . VAL A 1 2618 ? 222.444 229.141 175.602 1.00 24.22 ? 2618 VAL A CG2   1 
ATOM   8927  N N     . GLY A 1 2619 ? 220.041 225.267 174.301 1.00 20.69 ? 2619 GLY A N     1 
ATOM   8928  C CA    . GLY A 1 2619 ? 219.247 224.074 174.522 1.00 21.57 ? 2619 GLY A CA    1 
ATOM   8929  C C     . GLY A 1 2619 ? 219.552 223.466 175.875 1.00 26.77 ? 2619 GLY A C     1 
ATOM   8930  O O     . GLY A 1 2619 ? 220.717 223.279 176.235 1.00 27.64 ? 2619 GLY A O     1 
ATOM   8931  N N     . LEU A 1 2620 ? 218.498 223.160 176.625 1.00 26.33 ? 2620 LEU A N     1 
ATOM   8932  C CA    . LEU A 1 2620 ? 218.638 222.606 177.962 1.00 21.85 ? 2620 LEU A CA    1 
ATOM   8933  C C     . LEU A 1 2620 ? 217.426 221.735 178.256 1.00 21.33 ? 2620 LEU A C     1 
ATOM   8934  O O     . LEU A 1 2620 ? 216.287 222.148 178.030 1.00 20.76 ? 2620 LEU A O     1 
ATOM   8935  C CB    . LEU A 1 2620 ? 218.782 223.727 179.001 1.00 20.34 ? 2620 LEU A CB    1 
ATOM   8936  C CG    . LEU A 1 2620 ? 218.525 223.446 180.480 1.00 23.48 ? 2620 LEU A CG    1 
ATOM   8937  C CD1   . LEU A 1 2620 ? 219.352 222.269 180.947 1.00 21.17 ? 2620 LEU A CD1   1 
ATOM   8938  C CD2   . LEU A 1 2620 ? 218.845 224.680 181.303 1.00 26.56 ? 2620 LEU A CD2   1 
ATOM   8939  N N     . ASN A 1 2621 ? 217.675 220.526 178.751 1.00 22.74 ? 2621 ASN A N     1 
ATOM   8940  C CA    . ASN A 1 2621 ? 216.626 219.541 178.981 1.00 22.75 ? 2621 ASN A CA    1 
ATOM   8941  C C     . ASN A 1 2621 ? 216.504 219.273 180.473 1.00 25.60 ? 2621 ASN A C     1 
ATOM   8942  O O     . ASN A 1 2621 ? 217.505 219.000 181.144 1.00 27.33 ? 2621 ASN A O     1 
ATOM   8943  C CB    . ASN A 1 2621 ? 216.916 218.246 178.219 1.00 25.41 ? 2621 ASN A CB    1 
ATOM   8944  C CG    . ASN A 1 2621 ? 215.654 217.570 177.724 1.00 26.36 ? 2621 ASN A CG    1 
ATOM   8945  O OD1   . ASN A 1 2621 ? 214.651 217.507 178.434 1.00 26.91 ? 2621 ASN A OD1   1 
ATOM   8946  N ND2   . ASN A 1 2621 ? 215.695 217.066 176.497 1.00 21.16 ? 2621 ASN A ND2   1 
ATOM   8947  N N     . PHE A 1 2622 ? 215.280 219.350 180.984 1.00 23.59 ? 2622 PHE A N     1 
ATOM   8948  C CA    . PHE A 1 2622 ? 214.972 219.111 182.389 1.00 24.39 ? 2622 PHE A CA    1 
ATOM   8949  C C     . PHE A 1 2622 ? 214.344 217.735 182.552 1.00 23.03 ? 2622 PHE A C     1 
ATOM   8950  O O     . PHE A 1 2622 ? 213.336 217.427 181.908 1.00 21.56 ? 2622 PHE A O     1 
ATOM   8951  C CB    . PHE A 1 2622 ? 214.046 220.203 182.929 1.00 16.58 ? 2622 PHE A CB    1 
ATOM   8952  C CG    . PHE A 1 2622 ? 214.716 221.535 183.089 1.00 17.20 ? 2622 PHE A CG    1 
ATOM   8953  C CD1   . PHE A 1 2622 ? 215.437 221.817 184.229 1.00 18.10 ? 2622 PHE A CD1   1 
ATOM   8954  C CD2   . PHE A 1 2622 ? 214.692 222.473 182.078 1.00 23.46 ? 2622 PHE A CD2   1 
ATOM   8955  C CE1   . PHE A 1 2622 ? 216.072 223.026 184.387 1.00 20.18 ? 2622 PHE A CE1   1 
ATOM   8956  C CE2   . PHE A 1 2622 ? 215.340 223.685 182.230 1.00 22.67 ? 2622 PHE A CE2   1 
ATOM   8957  C CZ    . PHE A 1 2622 ? 216.025 223.961 183.386 1.00 17.88 ? 2622 PHE A CZ    1 
ATOM   8958  N N     . SER A 1 2623 ? 214.943 216.917 183.411 1.00 23.87 ? 2623 SER A N     1 
ATOM   8959  C CA    . SER A 1 2623 ? 214.436 215.608 183.782 1.00 21.44 ? 2623 SER A CA    1 
ATOM   8960  C C     . SER A 1 2623 ? 214.197 215.573 185.289 1.00 19.04 ? 2623 SER A C     1 
ATOM   8961  O O     . SER A 1 2623 ? 214.342 216.583 185.986 1.00 22.63 ? 2623 SER A O     1 
ATOM   8962  C CB    . SER A 1 2623 ? 215.408 214.517 183.328 1.00 22.28 ? 2623 SER A CB    1 
ATOM   8963  O OG    . SER A 1 2623 ? 216.714 214.760 183.820 1.00 25.22 ? 2623 SER A OG    1 
ATOM   8964  N N     . SER A 1 2624 ? 213.824 214.395 185.796 1.00 18.09 ? 2624 SER A N     1 
ATOM   8965  C CA    . SER A 1 2624 ? 213.547 214.263 187.223 1.00 20.63 ? 2624 SER A CA    1 
ATOM   8966  C C     . SER A 1 2624 ? 214.789 214.539 188.060 1.00 20.08 ? 2624 SER A C     1 
ATOM   8967  O O     . SER A 1 2624 ? 214.719 215.239 189.075 1.00 20.29 ? 2624 SER A O     1 
ATOM   8968  C CB    . SER A 1 2624 ? 212.997 212.869 187.523 1.00 21.17 ? 2624 SER A CB    1 
ATOM   8969  O OG    . SER A 1 2624 ? 211.637 212.766 187.142 1.00 21.92 ? 2624 SER A OG    1 
ATOM   8970  N N     . ALA A 1 2625 ? 215.937 214.013 187.644 1.00 22.21 ? 2625 ALA A N     1 
ATOM   8971  C CA    . ALA A 1 2625 ? 217.175 214.171 188.393 1.00 21.21 ? 2625 ALA A CA    1 
ATOM   8972  C C     . ALA A 1 2625 ? 217.851 215.515 188.157 1.00 21.11 ? 2625 ALA A C     1 
ATOM   8973  O O     . ALA A 1 2625 ? 218.998 215.694 188.577 1.00 19.67 ? 2625 ALA A O     1 
ATOM   8974  C CB    . ALA A 1 2625 ? 218.149 213.041 188.050 1.00 19.68 ? 2625 ALA A CB    1 
ATOM   8975  N N     . THR A 1 2626 ? 217.179 216.453 187.497 1.00 21.37 ? 2626 THR A N     1 
ATOM   8976  C CA    . THR A 1 2626 ? 217.775 217.757 187.241 1.00 24.48 ? 2626 THR A CA    1 
ATOM   8977  C C     . THR A 1 2626 ? 217.892 218.554 188.535 1.00 24.89 ? 2626 THR A C     1 
ATOM   8978  O O     . THR A 1 2626 ? 216.958 218.608 189.339 1.00 25.89 ? 2626 THR A O     1 
ATOM   8979  C CB    . THR A 1 2626 ? 216.942 218.535 186.224 1.00 22.15 ? 2626 THR A CB    1 
ATOM   8980  O OG1   . THR A 1 2626 ? 217.000 217.878 184.952 1.00 18.12 ? 2626 THR A OG1   1 
ATOM   8981  C CG2   . THR A 1 2626 ? 217.487 219.940 186.073 1.00 19.66 ? 2626 THR A CG2   1 
ATOM   8982  N N     . THR A 1 2627 ? 219.046 219.175 188.730 1.00 23.95 ? 2627 THR A N     1 
ATOM   8983  C CA    . THR A 1 2627 ? 219.343 219.985 189.899 1.00 23.63 ? 2627 THR A CA    1 
ATOM   8984  C C     . THR A 1 2627 ? 219.941 221.310 189.457 1.00 25.83 ? 2627 THR A C     1 
ATOM   8985  O O     . THR A 1 2627 ? 220.450 221.429 188.337 1.00 29.83 ? 2627 THR A O     1 
ATOM   8986  C CB    . THR A 1 2627 ? 220.312 219.260 190.844 1.00 28.77 ? 2627 THR A CB    1 
ATOM   8987  O OG1   . THR A 1 2627 ? 221.447 218.796 190.105 1.00 31.90 ? 2627 THR A OG1   1 
ATOM   8988  C CG2   . THR A 1 2627 ? 219.627 218.076 191.507 1.00 25.62 ? 2627 THR A CG2   1 
ATOM   8989  N N     . PRO A 1 2628 ? 219.872 222.342 190.313 1.00 22.75 ? 2628 PRO A N     1 
ATOM   8990  C CA    . PRO A 1 2628 ? 220.456 223.649 189.970 1.00 22.21 ? 2628 PRO A CA    1 
ATOM   8991  C C     . PRO A 1 2628 ? 221.890 223.609 189.457 1.00 25.57 ? 2628 PRO A C     1 
ATOM   8992  O O     . PRO A 1 2628 ? 222.336 224.558 188.803 1.00 22.11 ? 2628 PRO A O     1 
ATOM   8993  C CB    . PRO A 1 2628 ? 220.378 224.422 191.294 1.00 26.09 ? 2628 PRO A CB    1 
ATOM   8994  C CG    . PRO A 1 2628 ? 219.389 223.677 192.159 1.00 26.25 ? 2628 PRO A CG    1 
ATOM   8995  C CD    . PRO A 1 2628 ? 218.938 222.441 191.445 1.00 22.84 ? 2628 PRO A CD    1 
ATOM   8996  N N     . GLU A 1 2629 ? 222.630 222.535 189.751 1.00 33.75 ? 2629 GLU A N     1 
ATOM   8997  C CA    . GLU A 1 2629 ? 223.989 222.427 189.232 1.00 34.45 ? 2629 GLU A CA    1 
ATOM   8998  C C     . GLU A 1 2629 ? 223.998 222.364 187.711 1.00 32.74 ? 2629 GLU A C     1 
ATOM   8999  O O     . GLU A 1 2629 ? 224.985 222.756 187.080 1.00 30.03 ? 2629 GLU A O     1 
ATOM   9000  C CB    . GLU A 1 2629 ? 224.696 221.203 189.819 1.00 30.88 ? 2629 GLU A CB    1 
ATOM   9001  C CG    . GLU A 1 2629 ? 224.261 219.876 189.221 1.00 32.63 ? 2629 GLU A CG    1 
ATOM   9002  C CD    . GLU A 1 2629 ? 225.078 218.707 189.735 1.00 38.12 ? 2629 GLU A CD    1 
ATOM   9003  O OE1   . GLU A 1 2629 ? 225.703 218.842 190.808 1.00 37.46 ? 2629 GLU A OE1   1 
ATOM   9004  O OE2   . GLU A 1 2629 ? 225.095 217.653 189.065 1.00 35.95 ? 2629 GLU A OE2   1 
ATOM   9005  N N     . LEU A 1 2630 ? 222.912 221.881 187.104 1.00 31.98 ? 2630 LEU A N     1 
ATOM   9006  C CA    . LEU A 1 2630 ? 222.817 221.887 185.649 1.00 30.64 ? 2630 LEU A CA    1 
ATOM   9007  C C     . LEU A 1 2630 ? 222.780 223.312 185.112 1.00 31.30 ? 2630 LEU A C     1 
ATOM   9008  O O     . LEU A 1 2630 ? 223.509 223.652 184.169 1.00 36.52 ? 2630 LEU A O     1 
ATOM   9009  C CB    . LEU A 1 2630 ? 221.583 221.100 185.212 1.00 29.48 ? 2630 LEU A CB    1 
ATOM   9010  C CG    . LEU A 1 2630 ? 221.286 220.970 183.720 1.00 30.94 ? 2630 LEU A CG    1 
ATOM   9011  C CD1   . LEU A 1 2630 ? 222.526 220.541 182.956 1.00 31.75 ? 2630 LEU A CD1   1 
ATOM   9012  C CD2   . LEU A 1 2630 ? 220.163 219.966 183.518 1.00 31.10 ? 2630 LEU A CD2   1 
ATOM   9013  N N     . LEU A 1 2631 ? 221.952 224.168 185.717 1.00 28.97 ? 2631 LEU A N     1 
ATOM   9014  C CA    . LEU A 1 2631 ? 221.944 225.579 185.350 1.00 31.36 ? 2631 LEU A CA    1 
ATOM   9015  C C     . LEU A 1 2631 ? 223.295 226.222 185.628 1.00 29.40 ? 2631 LEU A C     1 
ATOM   9016  O O     . LEU A 1 2631 ? 223.749 227.084 184.867 1.00 25.02 ? 2631 LEU A O     1 
ATOM   9017  C CB    . LEU A 1 2631 ? 220.839 226.320 186.107 1.00 33.48 ? 2631 LEU A CB    1 
ATOM   9018  C CG    . LEU A 1 2631 ? 219.409 226.311 185.557 1.00 27.92 ? 2631 LEU A CG    1 
ATOM   9019  C CD1   . LEU A 1 2631 ? 219.351 227.009 184.210 1.00 24.48 ? 2631 LEU A CD1   1 
ATOM   9020  C CD2   . LEU A 1 2631 ? 218.840 224.905 185.464 1.00 25.85 ? 2631 LEU A CD2   1 
ATOM   9021  N N     . LEU A 1 2632 ? 223.952 225.818 186.718 1.00 31.28 ? 2632 LEU A N     1 
ATOM   9022  C CA    . LEU A 1 2632 ? 225.258 226.384 187.044 1.00 35.22 ? 2632 LEU A CA    1 
ATOM   9023  C C     . LEU A 1 2632 ? 226.300 226.036 185.987 1.00 34.38 ? 2632 LEU A C     1 
ATOM   9024  O O     . LEU A 1 2632 ? 227.078 226.900 185.565 1.00 33.49 ? 2632 LEU A O     1 
ATOM   9025  C CB    . LEU A 1 2632 ? 225.707 225.906 188.423 1.00 34.39 ? 2632 LEU A CB    1 
ATOM   9026  C CG    . LEU A 1 2632 ? 225.012 226.587 189.602 1.00 31.61 ? 2632 LEU A CG    1 
ATOM   9027  C CD1   . LEU A 1 2632 ? 225.484 225.998 190.920 1.00 34.06 ? 2632 LEU A CD1   1 
ATOM   9028  C CD2   . LEU A 1 2632 ? 225.255 228.085 189.561 1.00 29.00 ? 2632 LEU A CD2   1 
ATOM   9029  N N     . LYS A 1 2633 ? 226.335 224.776 185.545 1.00 33.59 ? 2633 LYS A N     1 
ATOM   9030  C CA    . LYS A 1 2633 ? 227.292 224.396 184.510 1.00 32.48 ? 2633 LYS A CA    1 
ATOM   9031  C C     . LYS A 1 2633 ? 226.949 225.050 183.178 1.00 30.58 ? 2633 LYS A C     1 
ATOM   9032  O O     . LYS A 1 2633 ? 227.846 225.421 182.414 1.00 33.77 ? 2633 LYS A O     1 
ATOM   9033  C CB    . LYS A 1 2633 ? 227.370 222.876 184.357 1.00 30.80 ? 2633 LYS A CB    1 
ATOM   9034  C CG    . LYS A 1 2633 ? 227.936 222.150 185.576 1.00 33.06 ? 2633 LYS A CG    1 
ATOM   9035  C CD    . LYS A 1 2633 ? 228.073 220.631 185.384 1.00 30.58 ? 2633 LYS A CD    1 
ATOM   9036  C CE    . LYS A 1 2633 ? 226.936 219.953 184.617 1.00 32.17 ? 2633 LYS A CE    1 
ATOM   9037  N NZ    . LYS A 1 2633 ? 225.573 220.479 184.882 1.00 30.65 ? 2633 LYS A NZ    1 
ATOM   9038  N N     . THR A 1 2634 ? 225.655 225.204 182.882 1.00 26.98 ? 2634 THR A N     1 
ATOM   9039  C CA    . THR A 1 2634 ? 225.269 225.930 181.676 1.00 29.52 ? 2634 THR A CA    1 
ATOM   9040  C C     . THR A 1 2634 ? 225.763 227.371 181.724 1.00 29.76 ? 2634 THR A C     1 
ATOM   9041  O O     . THR A 1 2634 ? 226.289 227.891 180.731 1.00 32.40 ? 2634 THR A O     1 
ATOM   9042  C CB    . THR A 1 2634 ? 223.751 225.892 181.500 1.00 31.44 ? 2634 THR A CB    1 
ATOM   9043  O OG1   . THR A 1 2634 ? 223.291 224.537 181.582 1.00 25.84 ? 2634 THR A OG1   1 
ATOM   9044  C CG2   . THR A 1 2634 ? 223.355 226.476 180.153 1.00 29.56 ? 2634 THR A CG2   1 
ATOM   9045  N N     . PHE A 1 2635 ? 225.611 228.028 182.877 1.00 30.71 ? 2635 PHE A N     1 
ATOM   9046  C CA    . PHE A 1 2635 ? 226.106 229.392 183.030 1.00 34.84 ? 2635 PHE A CA    1 
ATOM   9047  C C     . PHE A 1 2635 ? 227.619 229.450 182.875 1.00 36.34 ? 2635 PHE A C     1 
ATOM   9048  O O     . PHE A 1 2635 ? 228.146 230.332 182.190 1.00 34.12 ? 2635 PHE A O     1 
ATOM   9049  C CB    . PHE A 1 2635 ? 225.688 229.954 184.389 1.00 35.75 ? 2635 PHE A CB    1 
ATOM   9050  C CG    . PHE A 1 2635 ? 224.207 230.164 184.534 1.00 36.15 ? 2635 PHE A CG    1 
ATOM   9051  C CD1   . PHE A 1 2635 ? 223.412 230.393 183.426 1.00 34.36 ? 2635 PHE A CD1   1 
ATOM   9052  C CD2   . PHE A 1 2635 ? 223.610 230.130 185.783 1.00 32.16 ? 2635 PHE A CD2   1 
ATOM   9053  C CE1   . PHE A 1 2635 ? 222.052 230.587 183.562 1.00 31.90 ? 2635 PHE A CE1   1 
ATOM   9054  C CE2   . PHE A 1 2635 ? 222.250 230.320 185.923 1.00 30.29 ? 2635 PHE A CE2   1 
ATOM   9055  C CZ    . PHE A 1 2635 ? 221.470 230.549 184.811 1.00 31.10 ? 2635 PHE A CZ    1 
ATOM   9056  N N     . ASP A 1 2636 ? 228.337 228.515 183.500 1.00 40.21 ? 2636 ASP A N     1 
ATOM   9057  C CA    . ASP A 1 2636 ? 229.791 228.515 183.375 1.00 42.14 ? 2636 ASP A CA    1 
ATOM   9058  C C     . ASP A 1 2636 ? 230.234 228.289 181.935 1.00 44.26 ? 2636 ASP A C     1 
ATOM   9059  O O     . ASP A 1 2636 ? 231.233 228.872 181.499 1.00 43.59 ? 2636 ASP A O     1 
ATOM   9060  C CB    . ASP A 1 2636 ? 230.410 227.461 184.292 1.00 40.33 ? 2636 ASP A CB    1 
ATOM   9061  C CG    . ASP A 1 2636 ? 229.993 227.629 185.738 1.00 45.26 ? 2636 ASP A CG    1 
ATOM   9062  O OD1   . ASP A 1 2636 ? 229.836 228.788 186.179 1.00 42.81 ? 2636 ASP A OD1   1 
ATOM   9063  O OD2   . ASP A 1 2636 ? 229.830 226.606 186.437 1.00 45.03 ? 2636 ASP A OD2   1 
ATOM   9064  N N     . HIS A 1 2637 ? 229.517 227.451 181.186 1.00 41.49 ? 2637 HIS A N     1 
ATOM   9065  C CA    . HIS A 1 2637 ? 229.939 227.163 179.822 1.00 39.29 ? 2637 HIS A CA    1 
ATOM   9066  C C     . HIS A 1 2637 ? 229.594 228.299 178.863 1.00 40.72 ? 2637 HIS A C     1 
ATOM   9067  O O     . HIS A 1 2637 ? 230.385 228.609 177.965 1.00 43.65 ? 2637 HIS A O     1 
ATOM   9068  C CB    . HIS A 1 2637 ? 229.325 225.850 179.341 1.00 37.99 ? 2637 HIS A CB    1 
ATOM   9069  C CG    . HIS A 1 2637 ? 229.839 225.403 178.008 1.00 42.27 ? 2637 HIS A CG    1 
ATOM   9070  N ND1   . HIS A 1 2637 ? 229.287 225.820 176.817 1.00 42.98 ? 2637 HIS A ND1   1 
ATOM   9071  C CD2   . HIS A 1 2637 ? 230.865 224.584 177.680 1.00 43.45 ? 2637 HIS A CD2   1 
ATOM   9072  C CE1   . HIS A 1 2637 ? 229.945 225.271 175.812 1.00 40.60 ? 2637 HIS A CE1   1 
ATOM   9073  N NE2   . HIS A 1 2637 ? 230.909 224.517 176.308 1.00 42.95 ? 2637 HIS A NE2   1 
ATOM   9074  N N     . TYR A 1 2638 ? 228.426 228.934 179.021 1.00 35.92 ? 2638 TYR A N     1 
ATOM   9075  C CA    . TYR A 1 2638 ? 228.013 229.975 178.087 1.00 35.68 ? 2638 TYR A CA    1 
ATOM   9076  C C     . TYR A 1 2638 ? 228.147 231.399 178.614 1.00 38.07 ? 2638 TYR A C     1 
ATOM   9077  O O     . TYR A 1 2638 ? 227.990 232.338 177.826 1.00 37.96 ? 2638 TYR A O     1 
ATOM   9078  C CB    . TYR A 1 2638 ? 226.556 229.773 177.635 1.00 33.42 ? 2638 TYR A CB    1 
ATOM   9079  C CG    . TYR A 1 2638 ? 226.292 228.544 176.792 1.00 37.31 ? 2638 TYR A CG    1 
ATOM   9080  C CD1   . TYR A 1 2638 ? 225.795 228.668 175.502 1.00 39.02 ? 2638 TYR A CD1   1 
ATOM   9081  C CD2   . TYR A 1 2638 ? 226.485 227.266 177.296 1.00 38.45 ? 2638 TYR A CD2   1 
ATOM   9082  C CE1   . TYR A 1 2638 ? 225.535 227.559 174.723 1.00 37.37 ? 2638 TYR A CE1   1 
ATOM   9083  C CE2   . TYR A 1 2638 ? 226.221 226.148 176.524 1.00 39.82 ? 2638 TYR A CE2   1 
ATOM   9084  C CZ    . TYR A 1 2638 ? 225.748 226.302 175.239 1.00 36.70 ? 2638 TYR A CZ    1 
ATOM   9085  O OH    . TYR A 1 2638 ? 225.486 225.195 174.465 1.00 36.04 ? 2638 TYR A OH    1 
ATOM   9086  N N     . CYS A 1 2639 ? 228.433 231.599 179.898 1.00 39.29 ? 2639 CYS A N     1 
ATOM   9087  C CA    . CYS A 1 2639 ? 228.421 232.937 180.477 1.00 38.81 ? 2639 CYS A CA    1 
ATOM   9088  C C     . CYS A 1 2639 ? 229.693 233.187 181.275 1.00 38.58 ? 2639 CYS A C     1 
ATOM   9089  O O     . CYS A 1 2639 ? 230.341 232.259 181.765 1.00 35.66 ? 2639 CYS A O     1 
ATOM   9090  C CB    . CYS A 1 2639 ? 227.195 233.152 181.378 1.00 39.41 ? 2639 CYS A CB    1 
ATOM   9091  S SG    . CYS A 1 2639 ? 225.636 232.563 180.684 1.00 45.74 ? 2639 CYS A SG    1 
ATOM   9092  N N     . GLU A 1 2640 ? 230.035 234.468 181.409 1.00 40.29 ? 2640 GLU A N     1 
ATOM   9093  C CA    . GLU A 1 2640 ? 231.228 234.903 182.119 1.00 41.68 ? 2640 GLU A CA    1 
ATOM   9094  C C     . GLU A 1 2640 ? 230.850 235.819 183.276 1.00 42.22 ? 2640 GLU A C     1 
ATOM   9095  O O     . GLU A 1 2640 ? 229.896 236.598 183.188 1.00 39.57 ? 2640 GLU A O     1 
ATOM   9096  C CB    . GLU A 1 2640 ? 232.200 235.635 181.183 1.00 38.49 ? 2640 GLU A CB    1 
ATOM   9097  C CG    . GLU A 1 2640 ? 232.809 234.755 180.106 1.00 39.47 ? 2640 GLU A CG    1 
ATOM   9098  C CD    . GLU A 1 2640 ? 233.748 233.708 180.671 1.00 40.03 ? 2640 GLU A CD    1 
ATOM   9099  O OE1   . GLU A 1 2640 ? 234.401 233.984 181.699 1.00 40.54 ? 2640 GLU A OE1   1 
ATOM   9100  O OE2   . GLU A 1 2640 ? 233.829 232.606 180.089 1.00 38.90 ? 2640 GLU A OE2   1 
ATOM   9101  N N     . TYR A 1 2641 ? 231.612 235.719 184.362 1.00 40.63 ? 2641 TYR A N     1 
ATOM   9102  C CA    . TYR A 1 2641 ? 231.396 236.538 185.551 1.00 39.59 ? 2641 TYR A CA    1 
ATOM   9103  C C     . TYR A 1 2641 ? 232.237 237.804 185.434 1.00 39.14 ? 2641 TYR A C     1 
ATOM   9104  O O     . TYR A 1 2641 ? 233.471 237.738 185.410 1.00 40.23 ? 2641 TYR A O     1 
ATOM   9105  C CB    . TYR A 1 2641 ? 231.752 235.761 186.816 1.00 39.60 ? 2641 TYR A CB    1 
ATOM   9106  C CG    . TYR A 1 2641 ? 230.842 234.588 187.105 1.00 42.70 ? 2641 TYR A CG    1 
ATOM   9107  C CD1   . TYR A 1 2641 ? 229.815 234.695 188.033 1.00 39.81 ? 2641 TYR A CD1   1 
ATOM   9108  C CD2   . TYR A 1 2641 ? 231.013 233.373 186.457 1.00 40.49 ? 2641 TYR A CD2   1 
ATOM   9109  C CE1   . TYR A 1 2641 ? 228.982 233.626 188.303 1.00 36.23 ? 2641 TYR A CE1   1 
ATOM   9110  C CE2   . TYR A 1 2641 ? 230.185 232.299 186.721 1.00 39.39 ? 2641 TYR A CE2   1 
ATOM   9111  C CZ    . TYR A 1 2641 ? 229.172 232.432 187.645 1.00 36.27 ? 2641 TYR A CZ    1 
ATOM   9112  O OH    . TYR A 1 2641 ? 228.345 231.365 187.911 1.00 36.52 ? 2641 TYR A OH    1 
ATOM   9113  N N     . ARG A 1 2642 ? 231.573 238.954 185.356 1.00 38.10 ? 2642 ARG A N     1 
ATOM   9114  C CA    . ARG A 1 2642 ? 232.287 240.222 185.298 1.00 41.32 ? 2642 ARG A CA    1 
ATOM   9115  C C     . ARG A 1 2642 ? 232.967 240.510 186.630 1.00 41.88 ? 2642 ARG A C     1 
ATOM   9116  O O     . ARG A 1 2642 ? 232.411 240.245 187.700 1.00 38.79 ? 2642 ARG A O     1 
ATOM   9117  C CB    . ARG A 1 2642 ? 231.334 241.360 184.938 1.00 38.66 ? 2642 ARG A CB    1 
ATOM   9118  C CG    . ARG A 1 2642 ? 230.665 241.207 183.585 1.00 37.82 ? 2642 ARG A CG    1 
ATOM   9119  C CD    . ARG A 1 2642 ? 229.909 242.468 183.205 1.00 38.01 ? 2642 ARG A CD    1 
ATOM   9120  N NE    . ARG A 1 2642 ? 229.141 242.292 181.979 1.00 42.36 ? 2642 ARG A NE    1 
ATOM   9121  C CZ    . ARG A 1 2642 ? 228.372 243.226 181.437 1.00 42.18 ? 2642 ARG A CZ    1 
ATOM   9122  N NH1   . ARG A 1 2642 ? 228.248 244.423 181.986 1.00 40.84 ? 2642 ARG A NH1   1 
ATOM   9123  N NH2   . ARG A 1 2642 ? 227.712 242.952 180.315 1.00 38.60 ? 2642 ARG A NH2   1 
ATOM   9124  N N     . ARG A 1 2643 ? 234.178 241.063 186.560 1.00 47.09 ? 2643 ARG A N     1 
ATOM   9125  C CA    . ARG A 1 2643 ? 234.976 241.332 187.756 1.00 44.37 ? 2643 ARG A CA    1 
ATOM   9126  C C     . ARG A 1 2643 ? 234.464 242.595 188.451 1.00 41.67 ? 2643 ARG A C     1 
ATOM   9127  O O     . ARG A 1 2643 ? 235.103 243.650 188.471 1.00 44.06 ? 2643 ARG A O     1 
ATOM   9128  C CB    . ARG A 1 2643 ? 236.452 241.438 187.401 1.00 43.19 ? 2643 ARG A CB    1 
ATOM   9129  C CG    . ARG A 1 2643 ? 237.072 240.113 186.987 1.00 42.60 ? 2643 ARG A CG    1 
ATOM   9130  C CD    . ARG A 1 2643 ? 237.157 239.162 188.173 1.00 44.91 ? 2643 ARG A CD    1 
ATOM   9131  N NE    . ARG A 1 2643 ? 235.991 238.289 188.259 1.00 44.54 ? 2643 ARG A NE    1 
ATOM   9132  C CZ    . ARG A 1 2643 ? 235.692 237.539 189.311 1.00 44.47 ? 2643 ARG A CZ    1 
ATOM   9133  N NH1   . ARG A 1 2643 ? 236.450 237.536 190.395 1.00 42.77 ? 2643 ARG A NH1   1 
ATOM   9134  N NH2   . ARG A 1 2643 ? 234.603 236.777 189.276 1.00 43.20 ? 2643 ARG A NH2   1 
ATOM   9135  N N     . THR A 1 2644 ? 233.273 242.458 189.034 1.00 31.23 ? 2644 THR A N     1 
ATOM   9136  C CA    . THR A 1 2644 ? 232.632 243.436 189.908 1.00 34.47 ? 2644 THR A CA    1 
ATOM   9137  C C     . THR A 1 2644 ? 232.588 244.842 189.319 1.00 32.64 ? 2644 THR A C     1 
ATOM   9138  O O     . THR A 1 2644 ? 233.246 245.747 189.848 1.00 31.12 ? 2644 THR A O     1 
ATOM   9139  C CB    . THR A 1 2644 ? 233.345 243.482 191.262 1.00 35.16 ? 2644 THR A CB    1 
ATOM   9140  O OG1   . THR A 1 2644 ? 234.674 243.990 191.091 1.00 33.36 ? 2644 THR A OG1   1 
ATOM   9141  C CG2   . THR A 1 2644 ? 233.419 242.091 191.871 1.00 32.06 ? 2644 THR A CG2   1 
ATOM   9142  N N     . PRO A 1 2645 ? 231.842 245.074 188.231 1.00 29.89 ? 2645 PRO A N     1 
ATOM   9143  C CA    . PRO A 1 2645 ? 231.566 246.460 187.827 1.00 28.89 ? 2645 PRO A CA    1 
ATOM   9144  C C     . PRO A 1 2645 ? 230.834 247.194 188.937 1.00 30.40 ? 2645 PRO A C     1 
ATOM   9145  O O     . PRO A 1 2645 ? 231.288 248.233 189.428 1.00 29.39 ? 2645 PRO A O     1 
ATOM   9146  C CB    . PRO A 1 2645 ? 230.695 246.301 186.574 1.00 27.21 ? 2645 PRO A CB    1 
ATOM   9147  C CG    . PRO A 1 2645 ? 230.971 244.915 186.087 1.00 32.85 ? 2645 PRO A CG    1 
ATOM   9148  C CD    . PRO A 1 2645 ? 231.220 244.102 187.318 1.00 29.00 ? 2645 PRO A CD    1 
ATOM   9149  N N     . ASN A 1 2646 ? 229.685 246.646 189.332 1.00 30.61 ? 2646 ASN A N     1 
ATOM   9150  C CA    . ASN A 1 2646 ? 228.988 247.021 190.565 1.00 25.82 ? 2646 ASN A CA    1 
ATOM   9151  C C     . ASN A 1 2646 ? 228.440 245.713 191.131 1.00 25.38 ? 2646 ASN A C     1 
ATOM   9152  O O     . ASN A 1 2646 ? 227.283 245.356 190.893 1.00 26.70 ? 2646 ASN A O     1 
ATOM   9153  C CB    . ASN A 1 2646 ? 227.890 248.043 190.305 1.00 23.97 ? 2646 ASN A CB    1 
ATOM   9154  C CG    . ASN A 1 2646 ? 227.233 248.530 191.580 1.00 25.36 ? 2646 ASN A CG    1 
ATOM   9155  O OD1   . ASN A 1 2646 ? 227.767 248.354 192.675 1.00 27.57 ? 2646 ASN A OD1   1 
ATOM   9156  N ND2   . ASN A 1 2646 ? 226.067 249.151 191.444 1.00 25.02 ? 2646 ASN A ND2   1 
ATOM   9157  N N     . GLY A 1 2647 ? 229.275 245.008 191.882 1.00 22.92 ? 2647 GLY A N     1 
ATOM   9158  C CA    . GLY A 1 2647 ? 228.969 243.655 192.292 1.00 22.30 ? 2647 GLY A CA    1 
ATOM   9159  C C     . GLY A 1 2647 ? 229.208 242.654 191.174 1.00 21.96 ? 2647 GLY A C     1 
ATOM   9160  O O     . GLY A 1 2647 ? 229.319 242.996 189.998 1.00 24.95 ? 2647 GLY A O     1 
ATOM   9161  N N     . VAL A 1 2648 ? 229.286 241.381 191.560 1.00 21.03 ? 2648 VAL A N     1 
ATOM   9162  C CA    . VAL A 1 2648 ? 229.512 240.321 190.585 1.00 22.31 ? 2648 VAL A CA    1 
ATOM   9163  C C     . VAL A 1 2648 ? 228.270 240.164 189.720 1.00 26.14 ? 2648 VAL A C     1 
ATOM   9164  O O     . VAL A 1 2648 ? 227.150 240.031 190.229 1.00 29.89 ? 2648 VAL A O     1 
ATOM   9165  C CB    . VAL A 1 2648 ? 229.875 239.006 191.288 1.00 23.84 ? 2648 VAL A CB    1 
ATOM   9166  C CG1   . VAL A 1 2648 ? 230.009 237.883 190.275 1.00 22.66 ? 2648 VAL A CG1   1 
ATOM   9167  C CG2   . VAL A 1 2648 ? 231.162 239.166 192.081 1.00 25.00 ? 2648 VAL A CG2   1 
ATOM   9168  N N     . VAL A 1 2649 ? 228.461 240.183 188.403 1.00 24.07 ? 2649 VAL A N     1 
ATOM   9169  C CA    . VAL A 1 2649 ? 227.366 240.129 187.444 1.00 24.01 ? 2649 VAL A CA    1 
ATOM   9170  C C     . VAL A 1 2649 ? 227.628 238.987 186.473 1.00 26.92 ? 2649 VAL A C     1 
ATOM   9171  O O     . VAL A 1 2649 ? 228.718 238.894 185.897 1.00 32.94 ? 2649 VAL A O     1 
ATOM   9172  C CB    . VAL A 1 2649 ? 227.208 241.462 186.686 1.00 23.86 ? 2649 VAL A CB    1 
ATOM   9173  C CG1   . VAL A 1 2649 ? 226.371 241.271 185.434 1.00 21.47 ? 2649 VAL A CG1   1 
ATOM   9174  C CG2   . VAL A 1 2649 ? 226.592 242.515 187.591 1.00 23.78 ? 2649 VAL A CG2   1 
ATOM   9175  N N     . LEU A 1 2650 ? 226.633 238.121 186.293 1.00 23.93 ? 2650 LEU A N     1 
ATOM   9176  C CA    . LEU A 1 2650 ? 226.725 237.014 185.350 1.00 22.80 ? 2650 LEU A CA    1 
ATOM   9177  C C     . LEU A 1 2650 ? 226.188 237.474 184.000 1.00 28.36 ? 2650 LEU A C     1 
ATOM   9178  O O     . LEU A 1 2650 ? 225.012 237.841 183.886 1.00 25.12 ? 2650 LEU A O     1 
ATOM   9179  C CB    . LEU A 1 2650 ? 225.949 235.800 185.862 1.00 24.25 ? 2650 LEU A CB    1 
ATOM   9180  C CG    . LEU A 1 2650 ? 225.967 234.515 185.029 1.00 26.23 ? 2650 LEU A CG    1 
ATOM   9181  C CD1   . LEU A 1 2650 ? 225.954 233.303 185.940 1.00 25.95 ? 2650 LEU A CD1   1 
ATOM   9182  C CD2   . LEU A 1 2650 ? 224.787 234.458 184.074 1.00 26.58 ? 2650 LEU A CD2   1 
ATOM   9183  N N     . ALA A 1 2651 ? 227.044 237.451 182.984 1.00 38.35 ? 2651 ALA A N     1 
ATOM   9184  C CA    . ALA A 1 2651 ? 226.683 237.898 181.650 1.00 34.01 ? 2651 ALA A CA    1 
ATOM   9185  C C     . ALA A 1 2651 ? 227.138 236.884 180.613 1.00 29.91 ? 2651 ALA A C     1 
ATOM   9186  O O     . ALA A 1 2651 ? 228.125 236.172 180.825 1.00 27.21 ? 2651 ALA A O     1 
ATOM   9187  C CB    . ALA A 1 2651 ? 227.309 239.265 181.337 1.00 30.90 ? 2651 ALA A CB    1 
ATOM   9188  N N     . PRO A 1 2652 ? 226.436 236.796 179.484 1.00 34.88 ? 2652 PRO A N     1 
ATOM   9189  C CA    . PRO A 1 2652 ? 226.877 235.907 178.403 1.00 37.94 ? 2652 PRO A CA    1 
ATOM   9190  C C     . PRO A 1 2652 ? 228.229 236.328 177.845 1.00 39.53 ? 2652 PRO A C     1 
ATOM   9191  O O     . PRO A 1 2652 ? 228.634 237.490 177.927 1.00 37.69 ? 2652 PRO A O     1 
ATOM   9192  C CB    . PRO A 1 2652 ? 225.772 236.051 177.350 1.00 33.39 ? 2652 PRO A CB    1 
ATOM   9193  C CG    . PRO A 1 2652 ? 224.576 236.505 178.117 1.00 32.44 ? 2652 PRO A CG    1 
ATOM   9194  C CD    . PRO A 1 2652 ? 225.102 237.363 179.227 1.00 35.21 ? 2652 PRO A CD    1 
ATOM   9195  N N     . VAL A 1 2653 ? 228.935 235.347 177.275 1.00 39.59 ? 2653 VAL A N     1 
ATOM   9196  C CA    . VAL A 1 2653 ? 230.288 235.586 176.775 1.00 39.86 ? 2653 VAL A CA    1 
ATOM   9197  C C     . VAL A 1 2653 ? 230.273 236.651 175.686 1.00 41.58 ? 2653 VAL A C     1 
ATOM   9198  O O     . VAL A 1 2653 ? 231.088 237.582 175.690 1.00 39.17 ? 2653 VAL A O     1 
ATOM   9199  C CB    . VAL A 1 2653 ? 230.914 234.274 176.270 1.00 37.81 ? 2653 VAL A CB    1 
ATOM   9200  C CG1   . VAL A 1 2653 ? 232.280 234.539 175.655 1.00 38.27 ? 2653 VAL A CG1   1 
ATOM   9201  C CG2   . VAL A 1 2653 ? 231.020 233.262 177.397 1.00 36.62 ? 2653 VAL A CG2   1 
ATOM   9202  N N     . GLN A 1 2654 ? 229.345 236.536 174.741 1.00 41.77 ? 2654 GLN A N     1 
ATOM   9203  C CA    . GLN A 1 2654 ? 229.206 237.525 173.684 1.00 41.75 ? 2654 GLN A CA    1 
ATOM   9204  C C     . GLN A 1 2654 ? 228.348 238.693 174.153 1.00 41.56 ? 2654 GLN A C     1 
ATOM   9205  O O     . GLN A 1 2654 ? 227.392 238.524 174.914 1.00 44.53 ? 2654 GLN A O     1 
ATOM   9206  C CB    . GLN A 1 2654 ? 228.599 236.903 172.423 1.00 41.69 ? 2654 GLN A CB    1 
ATOM   9207  C CG    . GLN A 1 2654 ? 229.537 235.981 171.644 1.00 44.37 ? 2654 GLN A CG    1 
ATOM   9208  C CD    . GLN A 1 2654 ? 229.846 234.684 172.368 1.00 44.74 ? 2654 GLN A CD    1 
ATOM   9209  O OE1   . GLN A 1 2654 ? 231.002 234.391 172.673 1.00 43.22 ? 2654 GLN A OE1   1 
ATOM   9210  N NE2   . GLN A 1 2654 ? 228.812 233.899 172.643 1.00 43.20 ? 2654 GLN A NE2   1 
ATOM   9211  N N     . LEU A 1 2655 ? 228.703 239.886 173.685 1.00 40.79 ? 2655 LEU A N     1 
ATOM   9212  C CA    . LEU A 1 2655 ? 228.020 241.111 174.072 1.00 39.26 ? 2655 LEU A CA    1 
ATOM   9213  C C     . LEU A 1 2655 ? 226.895 241.420 173.094 1.00 39.87 ? 2655 LEU A C     1 
ATOM   9214  O O     . LEU A 1 2655 ? 227.011 241.166 171.892 1.00 39.25 ? 2655 LEU A O     1 
ATOM   9215  C CB    . LEU A 1 2655 ? 229.008 242.279 174.128 1.00 37.36 ? 2655 LEU A CB    1 
ATOM   9216  C CG    . LEU A 1 2655 ? 228.566 243.585 174.796 1.00 39.06 ? 2655 LEU A CG    1 
ATOM   9217  C CD1   . LEU A 1 2655 ? 229.744 244.237 175.500 1.00 40.31 ? 2655 LEU A CD1   1 
ATOM   9218  C CD2   . LEU A 1 2655 ? 227.961 244.548 173.782 1.00 38.16 ? 2655 LEU A CD2   1 
ATOM   9219  N N     . GLY A 1 2656 ? 225.803 241.968 173.621 1.00 37.34 ? 2656 GLY A N     1 
ATOM   9220  C CA    . GLY A 1 2656 ? 224.678 242.373 172.808 1.00 37.20 ? 2656 GLY A CA    1 
ATOM   9221  C C     . GLY A 1 2656 ? 223.698 241.274 172.466 1.00 37.04 ? 2656 GLY A C     1 
ATOM   9222  O O     . GLY A 1 2656 ? 222.685 241.554 171.813 1.00 36.12 ? 2656 GLY A O     1 
ATOM   9223  N N     . LYS A 1 2657 ? 223.958 240.039 172.885 1.00 33.96 ? 2657 LYS A N     1 
ATOM   9224  C CA    . LYS A 1 2657 ? 223.100 238.906 172.575 1.00 31.77 ? 2657 LYS A CA    1 
ATOM   9225  C C     . LYS A 1 2657 ? 222.481 238.367 173.857 1.00 31.99 ? 2657 LYS A C     1 
ATOM   9226  O O     . LYS A 1 2657 ? 223.155 238.257 174.886 1.00 35.28 ? 2657 LYS A O     1 
ATOM   9227  C CB    . LYS A 1 2657 ? 223.884 237.801 171.859 1.00 30.90 ? 2657 LYS A CB    1 
ATOM   9228  C CG    . LYS A 1 2657 ? 224.329 238.178 170.453 1.00 33.86 ? 2657 LYS A CG    1 
ATOM   9229  C CD    . LYS A 1 2657 ? 225.163 237.082 169.813 1.00 33.81 ? 2657 LYS A CD    1 
ATOM   9230  C CE    . LYS A 1 2657 ? 224.312 235.872 169.471 1.00 32.10 ? 2657 LYS A CE    1 
ATOM   9231  N NZ    . LYS A 1 2657 ? 223.342 236.172 168.382 1.00 31.84 ? 2657 LYS A NZ    1 
ATOM   9232  N N     . TRP A 1 2658 ? 221.196 238.035 173.787 1.00 28.60 ? 2658 TRP A N     1 
ATOM   9233  C CA    . TRP A 1 2658 ? 220.442 237.537 174.930 1.00 24.08 ? 2658 TRP A CA    1 
ATOM   9234  C C     . TRP A 1 2658 ? 220.376 236.017 174.858 1.00 23.70 ? 2658 TRP A C     1 
ATOM   9235  O O     . TRP A 1 2658 ? 220.111 235.454 173.791 1.00 30.73 ? 2658 TRP A O     1 
ATOM   9236  C CB    . TRP A 1 2658 ? 219.034 238.130 174.948 1.00 23.53 ? 2658 TRP A CB    1 
ATOM   9237  C CG    . TRP A 1 2658 ? 218.966 239.513 175.504 1.00 24.20 ? 2658 TRP A CG    1 
ATOM   9238  C CD1   . TRP A 1 2658 ? 219.311 240.669 174.869 1.00 28.66 ? 2658 TRP A CD1   1 
ATOM   9239  C CD2   . TRP A 1 2658 ? 218.503 239.893 176.805 1.00 24.44 ? 2658 TRP A CD2   1 
ATOM   9240  N NE1   . TRP A 1 2658 ? 219.103 241.745 175.697 1.00 29.38 ? 2658 TRP A NE1   1 
ATOM   9241  C CE2   . TRP A 1 2658 ? 218.607 241.295 176.891 1.00 27.50 ? 2658 TRP A CE2   1 
ATOM   9242  C CE3   . TRP A 1 2658 ? 218.015 239.184 177.905 1.00 25.42 ? 2658 TRP A CE3   1 
ATOM   9243  C CZ2   . TRP A 1 2658 ? 218.240 242.000 178.034 1.00 29.34 ? 2658 TRP A CZ2   1 
ATOM   9244  C CZ3   . TRP A 1 2658 ? 217.653 239.885 179.038 1.00 26.51 ? 2658 TRP A CZ3   1 
ATOM   9245  C CH2   . TRP A 1 2658 ? 217.767 241.279 179.095 1.00 26.81 ? 2658 TRP A CH2   1 
ATOM   9246  N N     . LEU A 1 2659 ? 220.622 235.359 175.986 1.00 22.50 ? 2659 LEU A N     1 
ATOM   9247  C CA    . LEU A 1 2659 ? 220.510 233.910 176.068 1.00 23.60 ? 2659 LEU A CA    1 
ATOM   9248  C C     . LEU A 1 2659 ? 219.156 233.519 176.640 1.00 23.02 ? 2659 LEU A C     1 
ATOM   9249  O O     . LEU A 1 2659 ? 218.753 234.004 177.701 1.00 26.89 ? 2659 LEU A O     1 
ATOM   9250  C CB    . LEU A 1 2659 ? 221.621 233.322 176.938 1.00 24.20 ? 2659 LEU A CB    1 
ATOM   9251  C CG    . LEU A 1 2659 ? 223.064 233.433 176.447 1.00 29.24 ? 2659 LEU A CG    1 
ATOM   9252  C CD1   . LEU A 1 2659 ? 224.010 232.911 177.510 1.00 28.85 ? 2659 LEU A CD1   1 
ATOM   9253  C CD2   . LEU A 1 2659 ? 223.253 232.677 175.145 1.00 26.77 ? 2659 LEU A CD2   1 
ATOM   9254  N N     . VAL A 1 2660 ? 218.455 232.638 175.933 1.00 18.57 ? 2660 VAL A N     1 
ATOM   9255  C CA    . VAL A 1 2660 ? 217.236 232.016 176.435 1.00 16.47 ? 2660 VAL A CA    1 
ATOM   9256  C C     . VAL A 1 2660 ? 217.537 230.547 176.685 1.00 16.59 ? 2660 VAL A C     1 
ATOM   9257  O O     . VAL A 1 2660 ? 218.069 229.855 175.808 1.00 24.78 ? 2660 VAL A O     1 
ATOM   9258  C CB    . VAL A 1 2660 ? 216.045 232.187 175.476 1.00 13.10 ? 2660 VAL A CB    1 
ATOM   9259  C CG1   . VAL A 1 2660 ? 215.603 233.620 175.450 1.00 13.74 ? 2660 VAL A CG1   1 
ATOM   9260  C CG2   . VAL A 1 2660 ? 216.409 231.753 174.076 1.00 19.52 ? 2660 VAL A CG2   1 
ATOM   9261  N N     . LEU A 1 2661 ? 217.226 230.081 177.888 1.00 13.52 ? 2661 LEU A N     1 
ATOM   9262  C CA    . LEU A 1 2661 ? 217.439 228.688 178.266 1.00 14.40 ? 2661 LEU A CA    1 
ATOM   9263  C C     . LEU A 1 2661 ? 216.088 227.992 178.168 1.00 12.48 ? 2661 LEU A C     1 
ATOM   9264  O O     . LEU A 1 2661 ? 215.296 227.996 179.111 1.00 20.51 ? 2661 LEU A O     1 
ATOM   9265  C CB    . LEU A 1 2661 ? 218.037 228.582 179.664 1.00 13.22 ? 2661 LEU A CB    1 
ATOM   9266  C CG    . LEU A 1 2661 ? 219.062 229.648 180.052 1.00 11.79 ? 2661 LEU A CG    1 
ATOM   9267  C CD1   . LEU A 1 2661 ? 219.549 229.404 181.461 1.00 13.91 ? 2661 LEU A CD1   1 
ATOM   9268  C CD2   . LEU A 1 2661 ? 220.231 229.655 179.082 1.00 17.54 ? 2661 LEU A CD2   1 
ATOM   9269  N N     . PHE A 1 2662 ? 215.822 227.401 177.008 1.00 9.91  ? 2662 PHE A N     1 
ATOM   9270  C CA    . PHE A 1 2662 ? 214.566 226.697 176.801 1.00 12.67 ? 2662 PHE A CA    1 
ATOM   9271  C C     . PHE A 1 2662 ? 214.471 225.521 177.760 1.00 15.65 ? 2662 PHE A C     1 
ATOM   9272  O O     . PHE A 1 2662 ? 215.358 224.664 177.795 1.00 16.68 ? 2662 PHE A O     1 
ATOM   9273  C CB    . PHE A 1 2662 ? 214.462 226.225 175.352 1.00 13.86 ? 2662 PHE A CB    1 
ATOM   9274  C CG    . PHE A 1 2662 ? 213.157 225.564 175.022 1.00 14.95 ? 2662 PHE A CG    1 
ATOM   9275  C CD1   . PHE A 1 2662 ? 213.091 224.579 174.054 1.00 16.76 ? 2662 PHE A CD1   1 
ATOM   9276  C CD2   . PHE A 1 2662 ? 211.997 225.921 175.684 1.00 11.38 ? 2662 PHE A CD2   1 
ATOM   9277  C CE1   . PHE A 1 2662 ? 211.892 223.970 173.748 1.00 13.70 ? 2662 PHE A CE1   1 
ATOM   9278  C CE2   . PHE A 1 2662 ? 210.799 225.314 175.383 1.00 10.59 ? 2662 PHE A CE2   1 
ATOM   9279  C CZ    . PHE A 1 2662 ? 210.746 224.337 174.416 1.00 11.64 ? 2662 PHE A CZ    1 
ATOM   9280  N N     . CYS A 1 2663 ? 213.397 225.488 178.545 1.00 17.01 ? 2663 CYS A N     1 
ATOM   9281  C CA    . CYS A 1 2663 ? 213.219 224.480 179.586 1.00 9.75  ? 2663 CYS A CA    1 
ATOM   9282  C C     . CYS A 1 2663 ? 212.323 223.369 179.057 1.00 11.77 ? 2663 CYS A C     1 
ATOM   9283  O O     . CYS A 1 2663 ? 211.096 223.478 179.084 1.00 13.18 ? 2663 CYS A O     1 
ATOM   9284  C CB    . CYS A 1 2663 ? 212.636 225.109 180.846 1.00 9.02  ? 2663 CYS A CB    1 
ATOM   9285  S SG    . CYS A 1 2663 ? 213.568 226.520 181.487 1.00 18.67 ? 2663 CYS A SG    1 
ATOM   9286  N N     . ASP A 1 2664 ? 212.938 222.291 178.582 1.00 15.37 ? 2664 ASP A N     1 
ATOM   9287  C CA    . ASP A 1 2664 ? 212.179 221.133 178.134 1.00 14.99 ? 2664 ASP A CA    1 
ATOM   9288  C C     . ASP A 1 2664 ? 211.590 220.414 179.340 1.00 17.12 ? 2664 ASP A C     1 
ATOM   9289  O O     . ASP A 1 2664 ? 212.331 219.926 180.200 1.00 24.34 ? 2664 ASP A O     1 
ATOM   9290  C CB    . ASP A 1 2664 ? 213.072 220.191 177.330 1.00 18.22 ? 2664 ASP A CB    1 
ATOM   9291  C CG    . ASP A 1 2664 ? 213.539 220.802 176.026 1.00 21.10 ? 2664 ASP A CG    1 
ATOM   9292  O OD1   . ASP A 1 2664 ? 212.792 221.620 175.454 1.00 21.30 ? 2664 ASP A OD1   1 
ATOM   9293  O OD2   . ASP A 1 2664 ? 214.653 220.466 175.571 1.00 20.61 ? 2664 ASP A OD2   1 
ATOM   9294  N N     . GLU A 1 2665 ? 210.258 220.351 179.404 1.00 10.77 ? 2665 GLU A N     1 
ATOM   9295  C CA    . GLU A 1 2665 ? 209.535 219.696 180.494 1.00 8.61  ? 2665 GLU A CA    1 
ATOM   9296  C C     . GLU A 1 2665 ? 209.911 220.319 181.843 1.00 14.56 ? 2665 GLU A C     1 
ATOM   9297  O O     . GLU A 1 2665 ? 210.507 219.688 182.717 1.00 19.97 ? 2665 GLU A O     1 
ATOM   9298  C CB    . GLU A 1 2665 ? 209.789 218.184 180.483 1.00 13.79 ? 2665 GLU A CB    1 
ATOM   9299  C CG    . GLU A 1 2665 ? 209.322 217.486 179.219 1.00 17.89 ? 2665 GLU A CG    1 
ATOM   9300  C CD    . GLU A 1 2665 ? 207.829 217.614 179.002 1.00 21.39 ? 2665 GLU A CD    1 
ATOM   9301  O OE1   . GLU A 1 2665 ? 207.077 217.558 179.998 1.00 20.94 ? 2665 GLU A OE1   1 
ATOM   9302  O OE2   . GLU A 1 2665 ? 207.408 217.773 177.837 1.00 15.54 ? 2665 GLU A OE2   1 
ATOM   9303  N N     . ILE A 1 2666 ? 209.552 221.598 181.977 1.00 18.85 ? 2666 ILE A N     1 
ATOM   9304  C CA    . ILE A 1 2666 ? 209.894 222.353 183.178 1.00 11.62 ? 2666 ILE A CA    1 
ATOM   9305  C C     . ILE A 1 2666 ? 209.223 221.789 184.426 1.00 11.88 ? 2666 ILE A C     1 
ATOM   9306  O O     . ILE A 1 2666 ? 209.759 221.940 185.530 1.00 18.22 ? 2666 ILE A O     1 
ATOM   9307  C CB    . ILE A 1 2666 ? 209.552 223.844 182.985 1.00 4.08  ? 2666 ILE A CB    1 
ATOM   9308  C CG1   . ILE A 1 2666 ? 210.515 224.722 183.787 1.00 10.72 ? 2666 ILE A CG1   1 
ATOM   9309  C CG2   . ILE A 1 2666 ? 208.101 224.137 183.346 1.00 0.47  ? 2666 ILE A CG2   1 
ATOM   9310  C CD1   . ILE A 1 2666 ? 210.423 226.191 183.452 1.00 11.70 ? 2666 ILE A CD1   1 
ATOM   9311  N N     . ASN A 1 2667 ? 208.071 221.138 184.288 1.00 5.94  ? 2667 ASN A N     1 
ATOM   9312  C CA    . ASN A 1 2667 ? 207.381 220.538 185.421 1.00 7.04  ? 2667 ASN A CA    1 
ATOM   9313  C C     . ASN A 1 2667 ? 207.752 219.076 185.627 1.00 14.75 ? 2667 ASN A C     1 
ATOM   9314  O O     . ASN A 1 2667 ? 207.228 218.438 186.546 1.00 18.06 ? 2667 ASN A O     1 
ATOM   9315  C CB    . ASN A 1 2667 ? 205.867 220.679 185.244 1.00 8.43  ? 2667 ASN A CB    1 
ATOM   9316  C CG    . ASN A 1 2667 ? 205.342 219.886 184.070 1.00 11.16 ? 2667 ASN A CG    1 
ATOM   9317  O OD1   . ASN A 1 2667 ? 206.099 219.481 183.191 1.00 13.72 ? 2667 ASN A OD1   1 
ATOM   9318  N ND2   . ASN A 1 2667 ? 204.033 219.675 184.039 1.00 15.88 ? 2667 ASN A ND2   1 
ATOM   9319  N N     . LEU A 1 2668 ? 208.629 218.535 184.786 1.00 20.28 ? 2668 LEU A N     1 
ATOM   9320  C CA    . LEU A 1 2668 ? 209.096 217.164 184.966 1.00 15.31 ? 2668 LEU A CA    1 
ATOM   9321  C C     . LEU A 1 2668 ? 209.874 216.927 186.258 1.00 13.45 ? 2668 LEU A C     1 
ATOM   9322  O O     . LEU A 1 2668 ? 209.645 215.878 186.886 1.00 11.02 ? 2668 LEU A O     1 
ATOM   9323  C CB    . LEU A 1 2668 ? 209.933 216.751 183.749 1.00 14.52 ? 2668 LEU A CB    1 
ATOM   9324  C CG    . LEU A 1 2668 ? 210.326 215.282 183.639 1.00 17.17 ? 2668 LEU A CG    1 
ATOM   9325  C CD1   . LEU A 1 2668 ? 209.089 214.412 183.604 1.00 17.82 ? 2668 LEU A CD1   1 
ATOM   9326  C CD2   . LEU A 1 2668 ? 211.157 215.069 182.393 1.00 19.51 ? 2668 LEU A CD2   1 
ATOM   9327  N N     . PRO A 1 2669 ? 210.815 217.814 186.701 1.00 11.77 ? 2669 PRO A N     1 
ATOM   9328  C CA    . PRO A 1 2669 ? 211.641 217.501 187.880 1.00 13.75 ? 2669 PRO A CA    1 
ATOM   9329  C C     . PRO A 1 2669 ? 210.882 216.931 189.069 1.00 19.23 ? 2669 PRO A C     1 
ATOM   9330  O O     . PRO A 1 2669 ? 209.741 217.315 189.341 1.00 17.71 ? 2669 PRO A O     1 
ATOM   9331  C CB    . PRO A 1 2669 ? 212.262 218.856 188.225 1.00 11.87 ? 2669 PRO A CB    1 
ATOM   9332  C CG    . PRO A 1 2669 ? 212.441 219.499 186.912 1.00 14.59 ? 2669 PRO A CG    1 
ATOM   9333  C CD    . PRO A 1 2669 ? 211.280 219.056 186.052 1.00 14.48 ? 2669 PRO A CD    1 
ATOM   9334  N N     . ASP A 1 2670 ? 211.527 216.010 189.783 1.00 23.21 ? 2670 ASP A N     1 
ATOM   9335  C CA    . ASP A 1 2670 ? 210.847 215.220 190.800 1.00 18.69 ? 2670 ASP A CA    1 
ATOM   9336  C C     . ASP A 1 2670 ? 210.406 216.081 191.976 1.00 20.72 ? 2670 ASP A C     1 
ATOM   9337  O O     . ASP A 1 2670 ? 211.136 216.961 192.438 1.00 23.89 ? 2670 ASP A O     1 
ATOM   9338  C CB    . ASP A 1 2670 ? 211.758 214.096 191.295 1.00 18.69 ? 2670 ASP A CB    1 
ATOM   9339  C CG    . ASP A 1 2670 ? 213.175 214.567 191.567 1.00 22.55 ? 2670 ASP A CG    1 
ATOM   9340  O OD1   . ASP A 1 2670 ? 213.423 215.790 191.522 1.00 19.21 ? 2670 ASP A OD1   1 
ATOM   9341  O OD2   . ASP A 1 2670 ? 214.045 213.712 191.833 1.00 27.28 ? 2670 ASP A OD2   1 
ATOM   9342  N N     . MET A 1 2671 ? 209.195 215.818 192.457 1.00 18.63 ? 2671 MET A N     1 
ATOM   9343  C CA    . MET A 1 2671 ? 208.719 216.454 193.675 1.00 18.84 ? 2671 MET A CA    1 
ATOM   9344  C C     . MET A 1 2671 ? 209.485 215.902 194.869 1.00 22.07 ? 2671 MET A C     1 
ATOM   9345  O O     . MET A 1 2671 ? 209.607 214.684 195.031 1.00 24.56 ? 2671 MET A O     1 
ATOM   9346  C CB    . MET A 1 2671 ? 207.221 216.209 193.849 1.00 17.91 ? 2671 MET A CB    1 
ATOM   9347  C CG    . MET A 1 2671 ? 206.523 217.203 194.758 1.00 17.64 ? 2671 MET A CG    1 
ATOM   9348  S SD    . MET A 1 2671 ? 206.519 218.870 194.082 1.00 25.44 ? 2671 MET A SD    1 
ATOM   9349  C CE    . MET A 1 2671 ? 204.798 219.031 193.616 1.00 21.03 ? 2671 MET A CE    1 
ATOM   9350  N N     . ASP A 1 2672 ? 210.006 216.795 195.704 1.00 21.82 ? 2672 ASP A N     1 
ATOM   9351  C CA    . ASP A 1 2672 ? 210.689 216.358 196.908 1.00 21.74 ? 2672 ASP A CA    1 
ATOM   9352  C C     . ASP A 1 2672 ? 209.685 215.826 197.924 1.00 23.95 ? 2672 ASP A C     1 
ATOM   9353  O O     . ASP A 1 2672 ? 208.470 215.989 197.785 1.00 24.28 ? 2672 ASP A O     1 
ATOM   9354  C CB    . ASP A 1 2672 ? 211.496 217.501 197.523 1.00 15.52 ? 2672 ASP A CB    1 
ATOM   9355  C CG    . ASP A 1 2672 ? 212.812 217.731 196.812 1.00 21.73 ? 2672 ASP A CG    1 
ATOM   9356  O OD1   . ASP A 1 2672 ? 212.998 217.176 195.710 1.00 24.98 ? 2672 ASP A OD1   1 
ATOM   9357  O OD2   . ASP A 1 2672 ? 213.661 218.468 197.357 1.00 21.56 ? 2672 ASP A OD2   1 
ATOM   9358  N N     . LYS A 1 2673 ? 210.212 215.173 198.960 1.00 28.16 ? 2673 LYS A N     1 
ATOM   9359  C CA    . LYS A 1 2673 ? 209.368 214.711 200.053 1.00 27.30 ? 2673 LYS A CA    1 
ATOM   9360  C C     . LYS A 1 2673 ? 208.740 215.863 200.823 1.00 28.42 ? 2673 LYS A C     1 
ATOM   9361  O O     . LYS A 1 2673 ? 207.803 215.635 201.595 1.00 29.31 ? 2673 LYS A O     1 
ATOM   9362  C CB    . LYS A 1 2673 ? 210.177 213.831 201.006 1.00 25.38 ? 2673 LYS A CB    1 
ATOM   9363  C CG    . LYS A 1 2673 ? 211.529 214.413 201.376 1.00 26.87 ? 2673 LYS A CG    1 
ATOM   9364  C CD    . LYS A 1 2673 ? 212.577 213.329 201.553 1.00 31.93 ? 2673 LYS A CD    1 
ATOM   9365  C CE    . LYS A 1 2673 ? 213.955 213.933 201.772 1.00 29.03 ? 2673 LYS A CE    1 
ATOM   9366  N NZ    . LYS A 1 2673 ? 214.422 214.695 200.581 1.00 30.79 ? 2673 LYS A NZ    1 
ATOM   9367  N N     . TYR A 1 2674 ? 209.231 217.085 200.627 1.00 23.95 ? 2674 TYR A N     1 
ATOM   9368  C CA    . TYR A 1 2674 ? 208.718 218.273 201.294 1.00 20.19 ? 2674 TYR A CA    1 
ATOM   9369  C C     . TYR A 1 2674 ? 208.117 219.261 200.298 1.00 21.77 ? 2674 TYR A C     1 
ATOM   9370  O O     . TYR A 1 2674 ? 208.068 220.464 200.558 1.00 20.90 ? 2674 TYR A O     1 
ATOM   9371  C CB    . TYR A 1 2674 ? 209.821 218.930 202.120 1.00 21.32 ? 2674 TYR A CB    1 
ATOM   9372  C CG    . TYR A 1 2674 ? 210.509 217.978 203.075 1.00 24.20 ? 2674 TYR A CG    1 
ATOM   9373  C CD1   . TYR A 1 2674 ? 209.831 217.450 204.165 1.00 23.78 ? 2674 TYR A CD1   1 
ATOM   9374  C CD2   . TYR A 1 2674 ? 211.834 217.606 202.884 1.00 25.57 ? 2674 TYR A CD2   1 
ATOM   9375  C CE1   . TYR A 1 2674 ? 210.454 216.584 205.043 1.00 24.61 ? 2674 TYR A CE1   1 
ATOM   9376  C CE2   . TYR A 1 2674 ? 212.465 216.743 203.760 1.00 25.90 ? 2674 TYR A CE2   1 
ATOM   9377  C CZ    . TYR A 1 2674 ? 211.770 216.233 204.835 1.00 27.20 ? 2674 TYR A CZ    1 
ATOM   9378  O OH    . TYR A 1 2674 ? 212.394 215.369 205.705 1.00 29.66 ? 2674 TYR A OH    1 
ATOM   9379  N N     . GLY A 1 2675 ? 207.668 218.760 199.148 1.00 25.71 ? 2675 GLY A N     1 
ATOM   9380  C CA    . GLY A 1 2675 ? 206.912 219.549 198.193 1.00 22.60 ? 2675 GLY A CA    1 
ATOM   9381  C C     . GLY A 1 2675 ? 207.628 220.744 197.599 1.00 19.46 ? 2675 GLY A C     1 
ATOM   9382  O O     . GLY A 1 2675 ? 207.061 221.838 197.543 1.00 24.78 ? 2675 GLY A O     1 
ATOM   9383  N N     . THR A 1 2676 ? 208.866 220.560 197.148 1.00 17.57 ? 2676 THR A N     1 
ATOM   9384  C CA    . THR A 1 2676 ? 209.624 221.667 196.568 1.00 12.90 ? 2676 THR A CA    1 
ATOM   9385  C C     . THR A 1 2676 ? 210.596 221.124 195.536 1.00 20.82 ? 2676 THR A C     1 
ATOM   9386  O O     . THR A 1 2676 ? 211.520 220.385 195.887 1.00 29.53 ? 2676 THR A O     1 
ATOM   9387  C CB    . THR A 1 2676 ? 210.374 222.442 197.649 1.00 12.61 ? 2676 THR A CB    1 
ATOM   9388  O OG1   . THR A 1 2676 ? 209.437 223.040 198.552 1.00 23.01 ? 2676 THR A OG1   1 
ATOM   9389  C CG2   . THR A 1 2676 ? 211.238 223.525 197.027 1.00 16.19 ? 2676 THR A CG2   1 
ATOM   9390  N N     . GLN A 1 2677 ? 210.396 221.491 194.273 1.00 17.04 ? 2677 GLN A N     1 
ATOM   9391  C CA    . GLN A 1 2677 ? 211.371 221.196 193.232 1.00 12.86 ? 2677 GLN A CA    1 
ATOM   9392  C C     . GLN A 1 2677 ? 212.501 222.213 193.317 1.00 16.54 ? 2677 GLN A C     1 
ATOM   9393  O O     . GLN A 1 2677 ? 212.274 223.417 193.161 1.00 18.70 ? 2677 GLN A O     1 
ATOM   9394  C CB    . GLN A 1 2677 ? 210.715 221.220 191.854 1.00 15.97 ? 2677 GLN A CB    1 
ATOM   9395  C CG    . GLN A 1 2677 ? 209.268 220.758 191.846 1.00 17.22 ? 2677 GLN A CG    1 
ATOM   9396  C CD    . GLN A 1 2677 ? 208.683 220.710 190.449 1.00 17.03 ? 2677 GLN A CD    1 
ATOM   9397  O OE1   . GLN A 1 2677 ? 209.408 220.766 189.459 1.00 16.74 ? 2677 GLN A OE1   1 
ATOM   9398  N NE2   . GLN A 1 2677 ? 207.364 220.601 190.364 1.00 18.56 ? 2677 GLN A NE2   1 
ATOM   9399  N N     . ARG A 1 2678 ? 213.717 221.726 193.567 1.00 18.81 ? 2678 ARG A N     1 
ATOM   9400  C CA    . ARG A 1 2678 ? 214.836 222.622 193.839 1.00 16.92 ? 2678 ARG A CA    1 
ATOM   9401  C C     . ARG A 1 2678 ? 215.153 223.512 192.645 1.00 18.48 ? 2678 ARG A C     1 
ATOM   9402  O O     . ARG A 1 2678 ? 215.439 224.702 192.812 1.00 17.68 ? 2678 ARG A O     1 
ATOM   9403  C CB    . ARG A 1 2678 ? 216.063 221.807 194.246 1.00 17.32 ? 2678 ARG A CB    1 
ATOM   9404  C CG    . ARG A 1 2678 ? 215.821 220.893 195.435 1.00 16.95 ? 2678 ARG A CG    1 
ATOM   9405  C CD    . ARG A 1 2678 ? 217.116 220.276 195.931 1.00 21.28 ? 2678 ARG A CD    1 
ATOM   9406  N NE    . ARG A 1 2678 ? 218.079 221.290 196.340 1.00 22.51 ? 2678 ARG A NE    1 
ATOM   9407  C CZ    . ARG A 1 2678 ? 219.239 221.502 195.734 1.00 24.73 ? 2678 ARG A CZ    1 
ATOM   9408  N NH1   . ARG A 1 2678 ? 219.621 220.773 194.700 1.00 21.49 ? 2678 ARG A NH1   1 
ATOM   9409  N NH2   . ARG A 1 2678 ? 220.035 222.469 196.178 1.00 22.18 ? 2678 ARG A NH2   1 
ATOM   9410  N N     . VAL A 1 2679 ? 215.118 222.957 191.433 1.00 18.41 ? 2679 VAL A N     1 
ATOM   9411  C CA    . VAL A 1 2679 ? 215.479 223.740 190.254 1.00 18.21 ? 2679 VAL A CA    1 
ATOM   9412  C C     . VAL A 1 2679 ? 214.428 224.811 189.971 1.00 20.79 ? 2679 VAL A C     1 
ATOM   9413  O O     . VAL A 1 2679 ? 214.758 225.922 189.538 1.00 22.83 ? 2679 VAL A O     1 
ATOM   9414  C CB    . VAL A 1 2679 ? 215.708 222.815 189.043 1.00 14.68 ? 2679 VAL A CB    1 
ATOM   9415  C CG1   . VAL A 1 2679 ? 214.441 222.049 188.685 1.00 14.67 ? 2679 VAL A CG1   1 
ATOM   9416  C CG2   . VAL A 1 2679 ? 216.226 223.609 187.857 1.00 11.83 ? 2679 VAL A CG2   1 
ATOM   9417  N N     . ILE A 1 2680 ? 213.152 224.498 190.209 1.00 18.67 ? 2680 ILE A N     1 
ATOM   9418  C CA    . ILE A 1 2680 ? 212.096 225.482 189.992 1.00 14.09 ? 2680 ILE A CA    1 
ATOM   9419  C C     . ILE A 1 2680 ? 212.261 226.660 190.943 1.00 12.67 ? 2680 ILE A C     1 
ATOM   9420  O O     . ILE A 1 2680 ? 212.153 227.823 190.539 1.00 12.34 ? 2680 ILE A O     1 
ATOM   9421  C CB    . ILE A 1 2680 ? 210.714 224.821 190.138 1.00 18.10 ? 2680 ILE A CB    1 
ATOM   9422  C CG1   . ILE A 1 2680 ? 210.440 223.905 188.944 1.00 13.58 ? 2680 ILE A CG1   1 
ATOM   9423  C CG2   . ILE A 1 2680 ? 209.626 225.872 190.268 1.00 13.41 ? 2680 ILE A CG2   1 
ATOM   9424  C CD1   . ILE A 1 2680 ? 210.090 224.643 187.678 1.00 11.46 ? 2680 ILE A CD1   1 
ATOM   9425  N N     . SER A 1 2681 ? 212.538 226.381 192.219 1.00 15.33 ? 2681 SER A N     1 
ATOM   9426  C CA    . SER A 1 2681 ? 212.800 227.455 193.170 1.00 9.98  ? 2681 SER A CA    1 
ATOM   9427  C C     . SER A 1 2681 ? 214.072 228.216 192.818 1.00 12.90 ? 2681 SER A C     1 
ATOM   9428  O O     . SER A 1 2681 ? 214.130 229.439 192.991 1.00 15.52 ? 2681 SER A O     1 
ATOM   9429  C CB    . SER A 1 2681 ? 212.890 226.888 194.585 1.00 13.47 ? 2681 SER A CB    1 
ATOM   9430  O OG    . SER A 1 2681 ? 211.604 226.551 195.078 1.00 16.12 ? 2681 SER A OG    1 
ATOM   9431  N N     . PHE A 1 2682 ? 215.091 227.516 192.319 1.00 15.19 ? 2682 PHE A N     1 
ATOM   9432  C CA    . PHE A 1 2682 ? 216.331 228.177 191.927 1.00 16.56 ? 2682 PHE A CA    1 
ATOM   9433  C C     . PHE A 1 2682 ? 216.093 229.171 190.798 1.00 16.77 ? 2682 PHE A C     1 
ATOM   9434  O O     . PHE A 1 2682 ? 216.594 230.300 190.841 1.00 13.05 ? 2682 PHE A O     1 
ATOM   9435  C CB    . PHE A 1 2682 ? 217.365 227.133 191.510 1.00 10.26 ? 2682 PHE A CB    1 
ATOM   9436  C CG    . PHE A 1 2682 ? 218.668 227.716 191.047 1.00 13.61 ? 2682 PHE A CG    1 
ATOM   9437  C CD1   . PHE A 1 2682 ? 219.350 228.632 191.829 1.00 20.26 ? 2682 PHE A CD1   1 
ATOM   9438  C CD2   . PHE A 1 2682 ? 219.217 227.342 189.833 1.00 14.20 ? 2682 PHE A CD2   1 
ATOM   9439  C CE1   . PHE A 1 2682 ? 220.553 229.165 191.409 1.00 18.31 ? 2682 PHE A CE1   1 
ATOM   9440  C CE2   . PHE A 1 2682 ? 220.420 227.871 189.409 1.00 18.49 ? 2682 PHE A CE2   1 
ATOM   9441  C CZ    . PHE A 1 2682 ? 221.090 228.782 190.199 1.00 18.29 ? 2682 PHE A CZ    1 
ATOM   9442  N N     . ILE A 1 2683 ? 215.328 228.772 189.780 1.00 15.18 ? 2683 ILE A N     1 
ATOM   9443  C CA    . ILE A 1 2683 ? 215.071 229.684 188.671 1.00 12.19 ? 2683 ILE A CA    1 
ATOM   9444  C C     . ILE A 1 2683 ? 214.089 230.774 189.082 1.00 16.08 ? 2683 ILE A C     1 
ATOM   9445  O O     . ILE A 1 2683 ? 214.146 231.891 188.558 1.00 14.58 ? 2683 ILE A O     1 
ATOM   9446  C CB    . ILE A 1 2683 ? 214.590 228.921 187.420 1.00 8.90  ? 2683 ILE A CB    1 
ATOM   9447  C CG1   . ILE A 1 2683 ? 213.271 228.199 187.681 1.00 15.82 ? 2683 ILE A CG1   1 
ATOM   9448  C CG2   . ILE A 1 2683 ? 215.650 227.936 186.956 1.00 13.37 ? 2683 ILE A CG2   1 
ATOM   9449  C CD1   . ILE A 1 2683 ? 212.640 227.630 186.433 1.00 17.68 ? 2683 ILE A CD1   1 
ATOM   9450  N N     . ARG A 1 2684 ? 213.182 230.485 190.021 1.00 18.09 ? 2684 ARG A N     1 
ATOM   9451  C CA    . ARG A 1 2684 ? 212.312 231.533 190.548 1.00 11.04 ? 2684 ARG A CA    1 
ATOM   9452  C C     . ARG A 1 2684 ? 213.116 232.600 191.279 1.00 10.37 ? 2684 ARG A C     1 
ATOM   9453  O O     . ARG A 1 2684 ? 212.805 233.794 191.190 1.00 11.71 ? 2684 ARG A O     1 
ATOM   9454  C CB    . ARG A 1 2684 ? 211.261 230.929 191.477 1.00 4.85  ? 2684 ARG A CB    1 
ATOM   9455  C CG    . ARG A 1 2684 ? 210.385 231.965 192.156 1.00 7.47  ? 2684 ARG A CG    1 
ATOM   9456  C CD    . ARG A 1 2684 ? 209.630 231.378 193.330 1.00 11.85 ? 2684 ARG A CD    1 
ATOM   9457  N NE    . ARG A 1 2684 ? 208.987 232.414 194.128 1.00 10.85 ? 2684 ARG A NE    1 
ATOM   9458  C CZ    . ARG A 1 2684 ? 209.516 232.960 195.214 1.00 11.59 ? 2684 ARG A CZ    1 
ATOM   9459  N NH1   . ARG A 1 2684 ? 210.699 232.585 195.670 1.00 11.89 ? 2684 ARG A NH1   1 
ATOM   9460  N NH2   . ARG A 1 2684 ? 208.840 233.906 195.859 1.00 11.20 ? 2684 ARG A NH2   1 
ATOM   9461  N N     . GLN A 1 2685 ? 214.148 232.184 192.016 1.00 11.82 ? 2685 GLN A N     1 
ATOM   9462  C CA    . GLN A 1 2685 ? 214.995 233.136 192.728 1.00 15.87 ? 2685 GLN A CA    1 
ATOM   9463  C C     . GLN A 1 2685 ? 215.566 234.191 191.792 1.00 14.47 ? 2685 GLN A C     1 
ATOM   9464  O O     . GLN A 1 2685 ? 215.681 235.364 192.162 1.00 12.48 ? 2685 GLN A O     1 
ATOM   9465  C CB    . GLN A 1 2685 ? 216.128 232.396 193.438 1.00 16.16 ? 2685 GLN A CB    1 
ATOM   9466  C CG    . GLN A 1 2685 ? 216.975 233.279 194.332 1.00 11.64 ? 2685 GLN A CG    1 
ATOM   9467  C CD    . GLN A 1 2685 ? 218.151 232.539 194.922 1.00 14.23 ? 2685 GLN A CD    1 
ATOM   9468  O OE1   . GLN A 1 2685 ? 218.398 231.381 194.591 1.00 15.93 ? 2685 GLN A OE1   1 
ATOM   9469  N NE2   . GLN A 1 2685 ? 218.888 233.204 195.803 1.00 17.73 ? 2685 GLN A NE2   1 
ATOM   9470  N N     . MET A 1 2686 ? 215.926 233.795 190.573 1.00 16.49 ? 2686 MET A N     1 
ATOM   9471  C CA    . MET A 1 2686 ? 216.544 234.716 189.630 1.00 18.98 ? 2686 MET A CA    1 
ATOM   9472  C C     . MET A 1 2686 ? 215.552 235.344 188.660 1.00 14.65 ? 2686 MET A C     1 
ATOM   9473  O O     . MET A 1 2686 ? 215.884 236.349 188.023 1.00 12.45 ? 2686 MET A O     1 
ATOM   9474  C CB    . MET A 1 2686 ? 217.656 233.997 188.864 1.00 11.55 ? 2686 MET A CB    1 
ATOM   9475  C CG    . MET A 1 2686 ? 217.180 232.866 187.988 1.00 13.03 ? 2686 MET A CG    1 
ATOM   9476  S SD    . MET A 1 2686 ? 218.572 232.025 187.227 1.00 25.32 ? 2686 MET A SD    1 
ATOM   9477  C CE    . MET A 1 2686 ? 219.218 231.147 188.635 1.00 14.87 ? 2686 MET A CE    1 
ATOM   9478  N N     . VAL A 1 2687 ? 214.355 234.778 188.521 1.00 12.01 ? 2687 VAL A N     1 
ATOM   9479  C CA    . VAL A 1 2687 ? 213.289 235.499 187.834 1.00 11.01 ? 2687 VAL A CA    1 
ATOM   9480  C C     . VAL A 1 2687 ? 212.798 236.662 188.685 1.00 14.35 ? 2687 VAL A C     1 
ATOM   9481  O O     . VAL A 1 2687 ? 212.555 237.761 188.174 1.00 18.24 ? 2687 VAL A O     1 
ATOM   9482  C CB    . VAL A 1 2687 ? 212.138 234.547 187.460 1.00 10.11 ? 2687 VAL A CB    1 
ATOM   9483  C CG1   . VAL A 1 2687 ? 210.976 235.329 186.885 1.00 8.82  ? 2687 VAL A CG1   1 
ATOM   9484  C CG2   . VAL A 1 2687 ? 212.608 233.527 186.443 1.00 7.95  ? 2687 VAL A CG2   1 
ATOM   9485  N N     . GLU A 1 2688 ? 212.657 236.449 189.994 1.00 11.37 ? 2688 GLU A N     1 
ATOM   9486  C CA    . GLU A 1 2688 ? 212.096 237.455 190.891 1.00 9.24  ? 2688 GLU A CA    1 
ATOM   9487  C C     . GLU A 1 2688 ? 213.159 238.402 191.438 1.00 15.14 ? 2688 GLU A C     1 
ATOM   9488  O O     . GLU A 1 2688 ? 213.025 239.623 191.318 1.00 12.32 ? 2688 GLU A O     1 
ATOM   9489  C CB    . GLU A 1 2688 ? 211.346 236.769 192.039 1.00 5.68  ? 2688 GLU A CB    1 
ATOM   9490  C CG    . GLU A 1 2688 ? 210.612 237.729 192.953 1.00 8.55  ? 2688 GLU A CG    1 
ATOM   9491  C CD    . GLU A 1 2688 ? 209.837 237.017 194.039 1.00 15.83 ? 2688 GLU A CD    1 
ATOM   9492  O OE1   . GLU A 1 2688 ? 210.257 235.914 194.443 1.00 17.60 ? 2688 GLU A OE1   1 
ATOM   9493  O OE2   . GLU A 1 2688 ? 208.806 237.560 194.488 1.00 14.90 ? 2688 GLU A OE2   1 
ATOM   9494  N N     . HIS A 1 2689 ? 214.214 237.864 192.047 1.00 14.45 ? 2689 HIS A N     1 
ATOM   9495  C CA    . HIS A 1 2689 ? 215.260 238.700 192.623 1.00 12.00 ? 2689 HIS A CA    1 
ATOM   9496  C C     . HIS A 1 2689 ? 216.380 239.018 191.643 1.00 16.67 ? 2689 HIS A C     1 
ATOM   9497  O O     . HIS A 1 2689 ? 217.302 239.758 192.003 1.00 17.61 ? 2689 HIS A O     1 
ATOM   9498  C CB    . HIS A 1 2689 ? 215.834 238.039 193.878 1.00 12.48 ? 2689 HIS A CB    1 
ATOM   9499  C CG    . HIS A 1 2689 ? 214.789 237.551 194.832 1.00 10.31 ? 2689 HIS A CG    1 
ATOM   9500  N ND1   . HIS A 1 2689 ? 214.413 236.229 194.913 1.00 12.95 ? 2689 HIS A ND1   1 
ATOM   9501  C CD2   . HIS A 1 2689 ? 214.030 238.214 195.736 1.00 8.98  ? 2689 HIS A CD2   1 
ATOM   9502  C CE1   . HIS A 1 2689 ? 213.473 236.096 195.831 1.00 7.72  ? 2689 HIS A CE1   1 
ATOM   9503  N NE2   . HIS A 1 2689 ? 213.221 237.286 196.345 1.00 7.65  ? 2689 HIS A NE2   1 
ATOM   9504  N N     . GLY A 1 2690 ? 216.326 238.488 190.423 1.00 15.70 ? 2690 GLY A N     1 
ATOM   9505  C CA    . GLY A 1 2690 ? 217.288 238.860 189.406 1.00 13.39 ? 2690 GLY A CA    1 
ATOM   9506  C C     . GLY A 1 2690 ? 218.676 238.292 189.580 1.00 14.81 ? 2690 GLY A C     1 
ATOM   9507  O O     . GLY A 1 2690 ? 219.634 238.868 189.062 1.00 23.76 ? 2690 GLY A O     1 
ATOM   9508  N N     . GLY A 1 2691 ? 218.818 237.184 190.292 1.00 3.42  ? 2691 GLY A N     1 
ATOM   9509  C CA    . GLY A 1 2691 ? 220.129 236.597 190.469 1.00 10.34 ? 2691 GLY A CA    1 
ATOM   9510  C C     . GLY A 1 2691 ? 220.095 235.455 191.456 1.00 17.26 ? 2691 GLY A C     1 
ATOM   9511  O O     . GLY A 1 2691 ? 219.028 234.951 191.809 1.00 23.94 ? 2691 GLY A O     1 
ATOM   9512  N N     . PHE A 1 2692 ? 221.281 235.052 191.898 1.00 19.81 ? 2692 PHE A N     1 
ATOM   9513  C CA    . PHE A 1 2692 ? 221.428 233.970 192.865 1.00 18.42 ? 2692 PHE A CA    1 
ATOM   9514  C C     . PHE A 1 2692 ? 222.739 234.176 193.617 1.00 20.42 ? 2692 PHE A C     1 
ATOM   9515  O O     . PHE A 1 2692 ? 223.410 235.201 193.460 1.00 19.23 ? 2692 PHE A O     1 
ATOM   9516  C CB    . PHE A 1 2692 ? 221.356 232.603 192.174 1.00 17.74 ? 2692 PHE A CB    1 
ATOM   9517  C CG    . PHE A 1 2692 ? 222.466 232.356 191.192 1.00 21.55 ? 2692 PHE A CG    1 
ATOM   9518  C CD1   . PHE A 1 2692 ? 222.412 232.887 189.914 1.00 22.36 ? 2692 PHE A CD1   1 
ATOM   9519  C CD2   . PHE A 1 2692 ? 223.560 231.585 191.544 1.00 24.14 ? 2692 PHE A CD2   1 
ATOM   9520  C CE1   . PHE A 1 2692 ? 223.430 232.658 189.011 1.00 24.51 ? 2692 PHE A CE1   1 
ATOM   9521  C CE2   . PHE A 1 2692 ? 224.581 231.355 190.644 1.00 20.15 ? 2692 PHE A CE2   1 
ATOM   9522  C CZ    . PHE A 1 2692 ? 224.515 231.889 189.376 1.00 21.98 ? 2692 PHE A CZ    1 
ATOM   9523  N N     . TYR A 1 2693 ? 223.101 233.199 194.444 1.00 27.11 ? 2693 TYR A N     1 
ATOM   9524  C CA    . TYR A 1 2693 ? 224.290 233.264 195.282 1.00 24.46 ? 2693 TYR A CA    1 
ATOM   9525  C C     . TYR A 1 2693 ? 225.294 232.213 194.832 1.00 26.05 ? 2693 TYR A C     1 
ATOM   9526  O O     . TYR A 1 2693 ? 224.960 231.026 194.753 1.00 26.20 ? 2693 TYR A O     1 
ATOM   9527  C CB    . TYR A 1 2693 ? 223.929 233.047 196.754 1.00 25.23 ? 2693 TYR A CB    1 
ATOM   9528  C CG    . TYR A 1 2693 ? 223.473 234.295 197.475 1.00 26.75 ? 2693 TYR A CG    1 
ATOM   9529  C CD1   . TYR A 1 2693 ? 224.322 235.382 197.628 1.00 28.15 ? 2693 TYR A CD1   1 
ATOM   9530  C CD2   . TYR A 1 2693 ? 222.190 234.389 197.998 1.00 25.52 ? 2693 TYR A CD2   1 
ATOM   9531  C CE1   . TYR A 1 2693 ? 223.909 236.523 198.286 1.00 27.34 ? 2693 TYR A CE1   1 
ATOM   9532  C CE2   . TYR A 1 2693 ? 221.768 235.525 198.656 1.00 28.09 ? 2693 TYR A CE2   1 
ATOM   9533  C CZ    . TYR A 1 2693 ? 222.630 236.589 198.798 1.00 27.43 ? 2693 TYR A CZ    1 
ATOM   9534  O OH    . TYR A 1 2693 ? 222.212 237.724 199.453 1.00 26.02 ? 2693 TYR A OH    1 
ATOM   9535  N N     . ARG A 1 2694 ? 226.517 232.648 194.541 1.00 32.19 ? 2694 ARG A N     1 
ATOM   9536  C CA    . ARG A 1 2694 ? 227.578 231.709 194.209 1.00 33.53 ? 2694 ARG A CA    1 
ATOM   9537  C C     . ARG A 1 2694 ? 227.943 230.873 195.428 1.00 38.08 ? 2694 ARG A C     1 
ATOM   9538  O O     . ARG A 1 2694 ? 227.920 231.356 196.563 1.00 40.40 ? 2694 ARG A O     1 
ATOM   9539  C CB    . ARG A 1 2694 ? 228.813 232.450 193.699 1.00 35.20 ? 2694 ARG A CB    1 
ATOM   9540  C CG    . ARG A 1 2694 ? 228.520 233.632 192.797 1.00 34.68 ? 2694 ARG A CG    1 
ATOM   9541  C CD    . ARG A 1 2694 ? 229.813 234.262 192.304 1.00 36.00 ? 2694 ARG A CD    1 
ATOM   9542  N NE    . ARG A 1 2694 ? 230.774 233.261 191.855 1.00 37.75 ? 2694 ARG A NE    1 
ATOM   9543  C CZ    . ARG A 1 2694 ? 231.976 233.543 191.372 1.00 37.83 ? 2694 ARG A CZ    1 
ATOM   9544  N NH1   . ARG A 1 2694 ? 232.402 234.791 191.263 1.00 37.14 ? 2694 ARG A NH1   1 
ATOM   9545  N NH2   . ARG A 1 2694 ? 232.772 232.548 190.992 1.00 36.32 ? 2694 ARG A NH2   1 
ATOM   9546  N N     . THR A 1 2695 ? 228.282 229.610 195.188 1.00 37.22 ? 2695 THR A N     1 
ATOM   9547  C CA    . THR A 1 2695 ? 228.666 228.698 196.256 1.00 37.57 ? 2695 THR A CA    1 
ATOM   9548  C C     . THR A 1 2695 ? 230.167 228.678 196.512 1.00 37.88 ? 2695 THR A C     1 
ATOM   9549  O O     . THR A 1 2695 ? 230.616 227.959 197.410 1.00 37.04 ? 2695 THR A O     1 
ATOM   9550  C CB    . THR A 1 2695 ? 228.184 227.280 195.937 1.00 36.55 ? 2695 THR A CB    1 
ATOM   9551  O OG1   . THR A 1 2695 ? 228.672 226.885 194.649 1.00 39.61 ? 2695 THR A OG1   1 
ATOM   9552  C CG2   . THR A 1 2695 ? 226.664 227.223 195.939 1.00 34.85 ? 2695 THR A CG2   1 
ATOM   9553  N N     . SER A 1 2696 ? 230.950 229.443 195.753 1.00 42.55 ? 2696 SER A N     1 
ATOM   9554  C CA    . SER A 1 2696 ? 232.397 229.461 195.925 1.00 41.85 ? 2696 SER A CA    1 
ATOM   9555  C C     . SER A 1 2696 ? 232.866 230.556 196.872 1.00 41.97 ? 2696 SER A C     1 
ATOM   9556  O O     . SER A 1 2696 ? 233.755 230.312 197.696 1.00 43.87 ? 2696 SER A O     1 
ATOM   9557  C CB    . SER A 1 2696 ? 233.087 229.631 194.570 1.00 41.28 ? 2696 SER A CB    1 
ATOM   9558  O OG    . SER A 1 2696 ? 234.496 229.613 194.710 1.00 41.16 ? 2696 SER A OG    1 
ATOM   9559  N N     . ASP A 1 2697 ? 232.290 231.755 196.776 1.00 38.53 ? 2697 ASP A N     1 
ATOM   9560  C CA    . ASP A 1 2697 ? 232.676 232.852 197.654 1.00 44.26 ? 2697 ASP A CA    1 
ATOM   9561  C C     . ASP A 1 2697 ? 231.484 233.476 198.370 1.00 44.86 ? 2697 ASP A C     1 
ATOM   9562  O O     . ASP A 1 2697 ? 231.658 234.497 199.049 1.00 43.29 ? 2697 ASP A O     1 
ATOM   9563  C CB    . ASP A 1 2697 ? 233.434 233.930 196.870 1.00 44.17 ? 2697 ASP A CB    1 
ATOM   9564  C CG    . ASP A 1 2697 ? 232.762 234.275 195.558 1.00 44.34 ? 2697 ASP A CG    1 
ATOM   9565  O OD1   . ASP A 1 2697 ? 231.639 233.783 195.320 1.00 42.84 ? 2697 ASP A OD1   1 
ATOM   9566  O OD2   . ASP A 1 2697 ? 233.354 235.040 194.768 1.00 45.50 ? 2697 ASP A OD2   1 
ATOM   9567  N N     . GLN A 1 2698 ? 230.290 232.894 198.243 1.00 38.80 ? 2698 GLN A N     1 
ATOM   9568  C CA    . GLN A 1 2698 ? 229.093 233.354 198.950 1.00 38.21 ? 2698 GLN A CA    1 
ATOM   9569  C C     . GLN A 1 2698 ? 228.811 234.830 198.682 1.00 38.94 ? 2698 GLN A C     1 
ATOM   9570  O O     . GLN A 1 2698 ? 228.519 235.605 199.594 1.00 39.59 ? 2698 GLN A O     1 
ATOM   9571  C CB    . GLN A 1 2698 ? 229.203 233.091 200.454 1.00 39.51 ? 2698 GLN A CB    1 
ATOM   9572  C CG    . GLN A 1 2698 ? 229.612 231.674 200.825 1.00 39.28 ? 2698 GLN A CG    1 
ATOM   9573  C CD    . GLN A 1 2698 ? 231.116 231.513 200.951 1.00 40.63 ? 2698 GLN A CD    1 
ATOM   9574  O OE1   . GLN A 1 2698 ? 231.745 232.110 201.825 1.00 36.67 ? 2698 GLN A OE1   1 
ATOM   9575  N NE2   . GLN A 1 2698 ? 231.699 230.700 200.079 1.00 39.72 ? 2698 GLN A NE2   1 
ATOM   9576  N N     . THR A 1 2699 ? 228.902 235.226 197.416 1.00 36.24 ? 2699 THR A N     1 
ATOM   9577  C CA    . THR A 1 2699 ? 228.610 236.591 197.003 1.00 34.88 ? 2699 THR A CA    1 
ATOM   9578  C C     . THR A 1 2699 ? 227.425 236.599 196.048 1.00 33.48 ? 2699 THR A C     1 
ATOM   9579  O O     . THR A 1 2699 ? 227.170 235.615 195.346 1.00 31.30 ? 2699 THR A O     1 
ATOM   9580  C CB    . THR A 1 2699 ? 229.826 237.249 196.341 1.00 35.59 ? 2699 THR A CB    1 
ATOM   9581  O OG1   . THR A 1 2699 ? 229.553 238.636 196.107 1.00 35.88 ? 2699 THR A OG1   1 
ATOM   9582  C CG2   . THR A 1 2699 ? 230.149 236.580 195.021 1.00 35.94 ? 2699 THR A CG2   1 
ATOM   9583  N N     . TRP A 1 2700 ? 226.692 237.709 196.039 1.00 23.82 ? 2700 TRP A N     1 
ATOM   9584  C CA    . TRP A 1 2700 ? 225.519 237.834 195.184 1.00 23.92 ? 2700 TRP A CA    1 
ATOM   9585  C C     . TRP A 1 2700 ? 225.948 238.085 193.745 1.00 24.42 ? 2700 TRP A C     1 
ATOM   9586  O O     . TRP A 1 2700 ? 226.661 239.053 193.461 1.00 23.93 ? 2700 TRP A O     1 
ATOM   9587  C CB    . TRP A 1 2700 ? 224.621 238.962 195.684 1.00 24.91 ? 2700 TRP A CB    1 
ATOM   9588  C CG    . TRP A 1 2700 ? 223.383 239.168 194.862 1.00 26.76 ? 2700 TRP A CG    1 
ATOM   9589  C CD1   . TRP A 1 2700 ? 223.147 240.179 193.979 1.00 24.39 ? 2700 TRP A CD1   1 
ATOM   9590  C CD2   . TRP A 1 2700 ? 222.213 238.341 194.847 1.00 26.61 ? 2700 TRP A CD2   1 
ATOM   9591  N NE1   . TRP A 1 2700 ? 221.902 240.035 193.416 1.00 22.69 ? 2700 TRP A NE1   1 
ATOM   9592  C CE2   . TRP A 1 2700 ? 221.309 238.914 193.932 1.00 22.66 ? 2700 TRP A CE2   1 
ATOM   9593  C CE3   . TRP A 1 2700 ? 221.842 237.173 195.519 1.00 24.12 ? 2700 TRP A CE3   1 
ATOM   9594  C CZ2   . TRP A 1 2700 ? 220.060 238.358 193.672 1.00 22.79 ? 2700 TRP A CZ2   1 
ATOM   9595  C CZ3   . TRP A 1 2700 ? 220.602 236.624 195.259 1.00 21.15 ? 2700 TRP A CZ3   1 
ATOM   9596  C CH2   . TRP A 1 2700 ? 219.726 237.216 194.345 1.00 22.03 ? 2700 TRP A CH2   1 
ATOM   9597  N N     . VAL A 1 2701 ? 225.512 237.215 192.840 1.00 22.17 ? 2701 VAL A N     1 
ATOM   9598  C CA    . VAL A 1 2701 ? 225.769 237.352 191.412 1.00 19.96 ? 2701 VAL A CA    1 
ATOM   9599  C C     . VAL A 1 2701 ? 224.456 237.709 190.730 1.00 22.97 ? 2701 VAL A C     1 
ATOM   9600  O O     . VAL A 1 2701 ? 223.404 237.145 191.055 1.00 28.59 ? 2701 VAL A O     1 
ATOM   9601  C CB    . VAL A 1 2701 ? 226.398 236.076 190.817 1.00 20.31 ? 2701 VAL A CB    1 
ATOM   9602  C CG1   . VAL A 1 2701 ? 225.442 234.902 190.894 1.00 18.33 ? 2701 VAL A CG1   1 
ATOM   9603  C CG2   . VAL A 1 2701 ? 226.825 236.317 189.382 1.00 24.21 ? 2701 VAL A CG2   1 
ATOM   9604  N N     . LYS A 1 2702 ? 224.510 238.673 189.817 1.00 16.88 ? 2702 LYS A N     1 
ATOM   9605  C CA    . LYS A 1 2702 ? 223.325 239.226 189.179 1.00 13.08 ? 2702 LYS A CA    1 
ATOM   9606  C C     . LYS A 1 2702 ? 223.297 238.834 187.710 1.00 18.99 ? 2702 LYS A C     1 
ATOM   9607  O O     . LYS A 1 2702 ? 224.305 238.968 187.008 1.00 26.53 ? 2702 LYS A O     1 
ATOM   9608  C CB    . LYS A 1 2702 ? 223.298 240.749 189.322 1.00 13.46 ? 2702 LYS A CB    1 
ATOM   9609  C CG    . LYS A 1 2702 ? 222.234 241.430 188.488 1.00 17.42 ? 2702 LYS A CG    1 
ATOM   9610  C CD    . LYS A 1 2702 ? 222.017 242.862 188.937 1.00 17.71 ? 2702 LYS A CD    1 
ATOM   9611  C CE    . LYS A 1 2702 ? 221.355 243.677 187.842 1.00 19.63 ? 2702 LYS A CE    1 
ATOM   9612  N NZ    . LYS A 1 2702 ? 220.298 242.894 187.145 1.00 22.46 ? 2702 LYS A NZ    1 
ATOM   9613  N N     . LEU A 1 2703 ? 222.147 238.347 187.251 1.00 16.32 ? 2703 LEU A N     1 
ATOM   9614  C CA    . LEU A 1 2703 ? 221.977 238.032 185.840 1.00 19.73 ? 2703 LEU A CA    1 
ATOM   9615  C C     . LEU A 1 2703 ? 221.875 239.310 185.019 1.00 25.24 ? 2703 LEU A C     1 
ATOM   9616  O O     . LEU A 1 2703 ? 221.133 240.233 185.366 1.00 15.87 ? 2703 LEU A O     1 
ATOM   9617  C CB    . LEU A 1 2703 ? 220.729 237.180 185.630 1.00 14.13 ? 2703 LEU A CB    1 
ATOM   9618  C CG    . LEU A 1 2703 ? 220.631 235.848 186.372 1.00 16.50 ? 2703 LEU A CG    1 
ATOM   9619  C CD1   . LEU A 1 2703 ? 219.613 234.969 185.680 1.00 18.01 ? 2703 LEU A CD1   1 
ATOM   9620  C CD2   . LEU A 1 2703 ? 221.979 235.153 186.442 1.00 17.37 ? 2703 LEU A CD2   1 
ATOM   9621  N N     . GLU A 1 2704 ? 222.627 239.362 183.920 1.00 26.73 ? 2704 GLU A N     1 
ATOM   9622  C CA    . GLU A 1 2704 ? 222.656 240.539 183.058 1.00 24.97 ? 2704 GLU A CA    1 
ATOM   9623  C C     . GLU A 1 2704 ? 221.702 240.410 181.874 1.00 30.01 ? 2704 GLU A C     1 
ATOM   9624  O O     . GLU A 1 2704 ? 220.791 241.228 181.714 1.00 27.87 ? 2704 GLU A O     1 
ATOM   9625  C CB    . GLU A 1 2704 ? 224.087 240.794 182.568 1.00 25.01 ? 2704 GLU A CB    1 
ATOM   9626  C CG    . GLU A 1 2704 ? 224.229 242.031 181.699 1.00 29.67 ? 2704 GLU A CG    1 
ATOM   9627  C CD    . GLU A 1 2704 ? 223.940 243.313 182.456 1.00 27.76 ? 2704 GLU A CD    1 
ATOM   9628  O OE1   . GLU A 1 2704 ? 224.110 243.330 183.693 1.00 25.92 ? 2704 GLU A OE1   1 
ATOM   9629  O OE2   . GLU A 1 2704 ? 223.541 244.306 181.812 1.00 29.05 ? 2704 GLU A OE2   1 
ATOM   9630  N N     . ARG A 1 2705 ? 221.899 239.397 181.035 1.00 25.51 ? 2705 ARG A N     1 
ATOM   9631  C CA    . ARG A 1 2705 ? 221.096 239.205 179.830 1.00 19.57 ? 2705 ARG A CA    1 
ATOM   9632  C C     . ARG A 1 2705 ? 220.679 237.743 179.699 1.00 21.08 ? 2705 ARG A C     1 
ATOM   9633  O O     . ARG A 1 2705 ? 220.827 237.122 178.647 1.00 27.13 ? 2705 ARG A O     1 
ATOM   9634  C CB    . ARG A 1 2705 ? 221.846 239.668 178.582 1.00 26.24 ? 2705 ARG A CB    1 
ATOM   9635  C CG    . ARG A 1 2705 ? 222.374 241.091 178.652 1.00 28.05 ? 2705 ARG A CG    1 
ATOM   9636  C CD    . ARG A 1 2705 ? 223.126 241.465 177.387 1.00 27.06 ? 2705 ARG A CD    1 
ATOM   9637  N NE    . ARG A 1 2705 ? 224.044 240.415 176.962 1.00 29.79 ? 2705 ARG A NE    1 
ATOM   9638  C CZ    . ARG A 1 2705 ? 225.328 240.366 177.292 1.00 29.77 ? 2705 ARG A CZ    1 
ATOM   9639  N NH1   . ARG A 1 2705 ? 225.880 241.291 178.058 1.00 29.89 ? 2705 ARG A NH1   1 
ATOM   9640  N NH2   . ARG A 1 2705 ? 226.076 239.365 176.838 1.00 28.85 ? 2705 ARG A NH2   1 
ATOM   9641  N N     . ILE A 1 2706 ? 220.154 237.173 180.780 1.00 19.78 ? 2706 ILE A N     1 
ATOM   9642  C CA    . ILE A 1 2706 ? 219.709 235.784 180.807 1.00 19.34 ? 2706 ILE A CA    1 
ATOM   9643  C C     . ILE A 1 2706 ? 218.188 235.762 180.840 1.00 17.73 ? 2706 ILE A C     1 
ATOM   9644  O O     . ILE A 1 2706 ? 217.567 236.458 181.652 1.00 26.72 ? 2706 ILE A O     1 
ATOM   9645  C CB    . ILE A 1 2706 ? 220.297 235.023 182.007 1.00 23.31 ? 2706 ILE A CB    1 
ATOM   9646  C CG1   . ILE A 1 2706 ? 221.809 235.239 182.088 1.00 23.78 ? 2706 ILE A CG1   1 
ATOM   9647  C CG2   . ILE A 1 2706 ? 219.971 233.542 181.907 1.00 22.04 ? 2706 ILE A CG2   1 
ATOM   9648  C CD1   . ILE A 1 2706 ? 222.570 234.653 180.925 1.00 25.11 ? 2706 ILE A CD1   1 
ATOM   9649  N N     . GLN A 1 2707 ? 217.594 234.963 179.959 1.00 8.79  ? 2707 GLN A N     1 
ATOM   9650  C CA    . GLN A 1 2707 ? 216.151 234.826 179.844 1.00 9.50  ? 2707 GLN A CA    1 
ATOM   9651  C C     . GLN A 1 2707 ? 215.776 233.353 179.931 1.00 10.30 ? 2707 GLN A C     1 
ATOM   9652  O O     . GLN A 1 2707 ? 216.541 232.479 179.514 1.00 17.93 ? 2707 GLN A O     1 
ATOM   9653  C CB    . GLN A 1 2707 ? 215.649 235.420 178.523 1.00 17.97 ? 2707 GLN A CB    1 
ATOM   9654  C CG    . GLN A 1 2707 ? 214.146 235.365 178.320 1.00 18.26 ? 2707 GLN A CG    1 
ATOM   9655  C CD    . GLN A 1 2707 ? 213.628 236.526 177.502 1.00 17.21 ? 2707 GLN A CD    1 
ATOM   9656  O OE1   . GLN A 1 2707 ? 214.371 237.448 177.170 1.00 13.36 ? 2707 GLN A OE1   1 
ATOM   9657  N NE2   . GLN A 1 2707 ? 212.346 236.484 177.162 1.00 17.84 ? 2707 GLN A NE2   1 
ATOM   9658  N N     . PHE A 1 2708 ? 214.598 233.078 180.481 1.00 8.16  ? 2708 PHE A N     1 
ATOM   9659  C CA    . PHE A 1 2708 ? 214.117 231.717 180.661 1.00 7.98  ? 2708 PHE A CA    1 
ATOM   9660  C C     . PHE A 1 2708 ? 212.826 231.497 179.890 1.00 13.76 ? 2708 PHE A C     1 
ATOM   9661  O O     . PHE A 1 2708 ? 211.928 232.343 179.904 1.00 20.10 ? 2708 PHE A O     1 
ATOM   9662  C CB    . PHE A 1 2708 ? 213.893 231.395 182.138 1.00 9.63  ? 2708 PHE A CB    1 
ATOM   9663  C CG    . PHE A 1 2708 ? 215.160 231.212 182.911 1.00 17.59 ? 2708 PHE A CG    1 
ATOM   9664  C CD1   . PHE A 1 2708 ? 215.874 232.303 183.373 1.00 13.69 ? 2708 PHE A CD1   1 
ATOM   9665  C CD2   . PHE A 1 2708 ? 215.644 229.941 183.166 1.00 13.59 ? 2708 PHE A CD2   1 
ATOM   9666  C CE1   . PHE A 1 2708 ? 217.042 232.127 184.077 1.00 8.57  ? 2708 PHE A CE1   1 
ATOM   9667  C CE2   . PHE A 1 2708 ? 216.809 229.761 183.870 1.00 13.37 ? 2708 PHE A CE2   1 
ATOM   9668  C CZ    . PHE A 1 2708 ? 217.511 230.853 184.323 1.00 15.74 ? 2708 PHE A CZ    1 
ATOM   9669  N N     . VAL A 1 2709 ? 212.751 230.361 179.203 1.00 11.47 ? 2709 VAL A N     1 
ATOM   9670  C CA    . VAL A 1 2709 ? 211.543 229.918 178.525 1.00 11.13 ? 2709 VAL A CA    1 
ATOM   9671  C C     . VAL A 1 2709 ? 211.316 228.455 178.872 1.00 9.56  ? 2709 VAL A C     1 
ATOM   9672  O O     . VAL A 1 2709 ? 212.251 227.649 178.878 1.00 10.48 ? 2709 VAL A O     1 
ATOM   9673  C CB    . VAL A 1 2709 ? 211.619 230.100 176.995 1.00 9.47  ? 2709 VAL A CB    1 
ATOM   9674  C CG1   . VAL A 1 2709 ? 210.262 229.859 176.387 1.00 9.50  ? 2709 VAL A CG1   1 
ATOM   9675  C CG2   . VAL A 1 2709 ? 212.124 231.487 176.635 1.00 10.15 ? 2709 VAL A CG2   1 
ATOM   9676  N N     . GLY A 1 2710 ? 210.062 228.110 179.162 1.00 7.75  ? 2710 GLY A N     1 
ATOM   9677  C CA    . GLY A 1 2710 ? 209.724 226.763 179.554 1.00 4.61  ? 2710 GLY A CA    1 
ATOM   9678  C C     . GLY A 1 2710 ? 208.675 226.161 178.639 1.00 7.05  ? 2710 GLY A C     1 
ATOM   9679  O O     . GLY A 1 2710 ? 207.989 226.857 177.893 1.00 16.66 ? 2710 GLY A O     1 
ATOM   9680  N N     . ALA A 1 2711 ? 208.576 224.837 178.706 1.00 2.41  ? 2711 ALA A N     1 
ATOM   9681  C CA    . ALA A 1 2711 ? 207.549 224.092 177.993 1.00 6.59  ? 2711 ALA A CA    1 
ATOM   9682  C C     . ALA A 1 2711 ? 207.246 222.832 178.784 1.00 6.86  ? 2711 ALA A C     1 
ATOM   9683  O O     . ALA A 1 2711 ? 208.134 222.282 179.436 1.00 14.08 ? 2711 ALA A O     1 
ATOM   9684  C CB    . ALA A 1 2711 ? 207.981 223.733 176.570 1.00 4.63  ? 2711 ALA A CB    1 
ATOM   9685  N N     . CYS A 1 2712 ? 205.997 222.379 178.727 1.00 3.43  ? 2712 CYS A N     1 
ATOM   9686  C CA    . CYS A 1 2712 ? 205.593 221.245 179.543 1.00 6.79  ? 2712 CYS A CA    1 
ATOM   9687  C C     . CYS A 1 2712 ? 204.290 220.651 179.033 1.00 6.39  ? 2712 CYS A C     1 
ATOM   9688  O O     . CYS A 1 2712 ? 203.493 221.335 178.389 1.00 8.67  ? 2712 CYS A O     1 
ATOM   9689  C CB    . CYS A 1 2712 ? 205.427 221.661 181.006 1.00 14.08 ? 2712 CYS A CB    1 
ATOM   9690  S SG    . CYS A 1 2712 ? 204.105 222.849 181.275 1.00 15.84 ? 2712 CYS A SG    1 
ATOM   9691  N N     . ASN A 1 2713 ? 204.089 219.374 179.331 1.00 8.31  ? 2713 ASN A N     1 
ATOM   9692  C CA    . ASN A 1 2713 ? 202.810 218.714 179.148 1.00 7.67  ? 2713 ASN A CA    1 
ATOM   9693  C C     . ASN A 1 2713 ? 201.878 219.073 180.302 1.00 11.46 ? 2713 ASN A C     1 
ATOM   9694  O O     . ASN A 1 2713 ? 202.330 219.544 181.348 1.00 9.81  ? 2713 ASN A O     1 
ATOM   9695  C CB    . ASN A 1 2713 ? 203.016 217.205 179.063 1.00 9.77  ? 2713 ASN A CB    1 
ATOM   9696  C CG    . ASN A 1 2713 ? 203.867 216.801 177.876 1.00 12.47 ? 2713 ASN A CG    1 
ATOM   9697  O OD1   . ASN A 1 2713 ? 204.572 215.794 177.918 1.00 18.32 ? 2713 ASN A OD1   1 
ATOM   9698  N ND2   . ASN A 1 2713 ? 203.808 217.590 176.811 1.00 8.98  ? 2713 ASN A ND2   1 
ATOM   9699  N N     . PRO A 1 2714 ? 200.570 218.881 180.137 1.00 11.08 ? 2714 PRO A N     1 
ATOM   9700  C CA    . PRO A 1 2714 ? 199.628 219.239 181.204 1.00 9.30  ? 2714 PRO A CA    1 
ATOM   9701  C C     . PRO A 1 2714 ? 199.947 218.501 182.491 1.00 13.85 ? 2714 PRO A C     1 
ATOM   9702  O O     . PRO A 1 2714 ? 200.394 217.344 182.459 1.00 20.43 ? 2714 PRO A O     1 
ATOM   9703  C CB    . PRO A 1 2714 ? 198.269 218.808 180.636 1.00 13.57 ? 2714 PRO A CB    1 
ATOM   9704  C CG    . PRO A 1 2714 ? 198.446 218.870 179.170 1.00 17.61 ? 2714 PRO A CG    1 
ATOM   9705  C CD    . PRO A 1 2714 ? 199.867 218.469 178.908 1.00 17.38 ? 2714 PRO A CD    1 
ATOM   9706  N N     . PRO A 1 2715 ? 199.745 219.142 183.644 1.00 18.39 ? 2715 PRO A N     1 
ATOM   9707  C CA    . PRO A 1 2715 ? 200.109 218.498 184.917 1.00 18.29 ? 2715 PRO A CA    1 
ATOM   9708  C C     . PRO A 1 2715 ? 199.319 217.236 185.216 1.00 23.38 ? 2715 PRO A C     1 
ATOM   9709  O O     . PRO A 1 2715 ? 199.779 216.415 186.019 1.00 22.76 ? 2715 PRO A O     1 
ATOM   9710  C CB    . PRO A 1 2715 ? 199.831 219.594 185.954 1.00 13.91 ? 2715 PRO A CB    1 
ATOM   9711  C CG    . PRO A 1 2715 ? 198.802 220.461 185.314 1.00 16.32 ? 2715 PRO A CG    1 
ATOM   9712  C CD    . PRO A 1 2715 ? 199.124 220.461 183.849 1.00 20.82 ? 2715 PRO A CD    1 
ATOM   9713  N N     . THR A 1 2716 ? 198.146 217.054 184.604 1.00 26.71 ? 2716 THR A N     1 
ATOM   9714  C CA    . THR A 1 2716 ? 197.371 215.840 184.825 1.00 25.62 ? 2716 THR A CA    1 
ATOM   9715  C C     . THR A 1 2716 ? 198.058 214.604 184.259 1.00 23.45 ? 2716 THR A C     1 
ATOM   9716  O O     . THR A 1 2716 ? 197.754 213.489 184.694 1.00 26.42 ? 2716 THR A O     1 
ATOM   9717  C CB    . THR A 1 2716 ? 195.980 215.980 184.208 1.00 27.18 ? 2716 THR A CB    1 
ATOM   9718  O OG1   . THR A 1 2716 ? 196.089 215.981 182.779 1.00 27.74 ? 2716 THR A OG1   1 
ATOM   9719  C CG2   . THR A 1 2716 ? 195.330 217.275 184.659 1.00 25.43 ? 2716 THR A CG2   1 
ATOM   9720  N N     . ASP A 1 2717 ? 198.967 214.776 183.304 1.00 20.21 ? 2717 ASP A N     1 
ATOM   9721  C CA    . ASP A 1 2717 ? 199.692 213.646 182.752 1.00 20.75 ? 2717 ASP A CA    1 
ATOM   9722  C C     . ASP A 1 2717 ? 200.636 213.062 183.803 1.00 25.24 ? 2717 ASP A C     1 
ATOM   9723  O O     . ASP A 1 2717 ? 201.187 213.794 184.628 1.00 23.37 ? 2717 ASP A O     1 
ATOM   9724  C CB    . ASP A 1 2717 ? 200.482 214.073 181.519 1.00 21.50 ? 2717 ASP A CB    1 
ATOM   9725  C CG    . ASP A 1 2717 ? 199.590 214.389 180.337 1.00 23.65 ? 2717 ASP A CG    1 
ATOM   9726  O OD1   . ASP A 1 2717 ? 198.353 214.295 180.481 1.00 22.08 ? 2717 ASP A OD1   1 
ATOM   9727  O OD2   . ASP A 1 2717 ? 200.126 214.736 179.264 1.00 23.55 ? 2717 ASP A OD2   1 
ATOM   9728  N N     . PRO A 1 2718 ? 200.826 211.742 183.801 1.00 29.10 ? 2718 PRO A N     1 
ATOM   9729  C CA    . PRO A 1 2718 ? 201.703 211.122 184.803 1.00 26.20 ? 2718 PRO A CA    1 
ATOM   9730  C C     . PRO A 1 2718 ? 203.133 211.631 184.693 1.00 23.34 ? 2718 PRO A C     1 
ATOM   9731  O O     . PRO A 1 2718 ? 203.664 211.824 183.597 1.00 22.47 ? 2718 PRO A O     1 
ATOM   9732  C CB    . PRO A 1 2718 ? 201.611 209.627 184.479 1.00 28.95 ? 2718 PRO A CB    1 
ATOM   9733  C CG    . PRO A 1 2718 ? 200.338 209.479 183.705 1.00 26.71 ? 2718 PRO A CG    1 
ATOM   9734  C CD    . PRO A 1 2718 ? 200.203 210.743 182.918 1.00 22.32 ? 2718 PRO A CD    1 
ATOM   9735  N N     . GLY A 1 2719 ? 203.760 211.834 185.849 1.00 16.74 ? 2719 GLY A N     1 
ATOM   9736  C CA    . GLY A 1 2719 ? 205.108 212.353 185.910 1.00 18.65 ? 2719 GLY A CA    1 
ATOM   9737  C C     . GLY A 1 2719 ? 205.222 213.858 185.818 1.00 21.82 ? 2719 GLY A C     1 
ATOM   9738  O O     . GLY A 1 2719 ? 206.339 214.383 185.907 1.00 21.56 ? 2719 GLY A O     1 
ATOM   9739  N N     . ARG A 1 2720 ? 204.110 214.569 185.646 1.00 24.93 ? 2720 ARG A N     1 
ATOM   9740  C CA    . ARG A 1 2720 ? 204.108 216.025 185.526 1.00 19.87 ? 2720 ARG A CA    1 
ATOM   9741  C C     . ARG A 1 2720 ? 203.669 216.600 186.869 1.00 19.05 ? 2720 ARG A C     1 
ATOM   9742  O O     . ARG A 1 2720 ? 202.492 216.532 187.230 1.00 18.10 ? 2720 ARG A O     1 
ATOM   9743  C CB    . ARG A 1 2720 ? 203.188 216.488 184.399 1.00 13.08 ? 2720 ARG A CB    1 
ATOM   9744  C CG    . ARG A 1 2720 ? 203.726 216.308 182.979 1.00 15.64 ? 2720 ARG A CG    1 
ATOM   9745  C CD    . ARG A 1 2720 ? 203.743 214.849 182.551 1.00 17.83 ? 2720 ARG A CD    1 
ATOM   9746  N NE    . ARG A 1 2720 ? 204.238 214.667 181.191 1.00 20.09 ? 2720 ARG A NE    1 
ATOM   9747  C CZ    . ARG A 1 2720 ? 205.508 214.452 180.876 1.00 21.77 ? 2720 ARG A CZ    1 
ATOM   9748  N NH1   . ARG A 1 2720 ? 206.446 214.378 181.802 1.00 22.98 ? 2720 ARG A NH1   1 
ATOM   9749  N NH2   . ARG A 1 2720 ? 205.842 214.305 179.597 1.00 16.75 ? 2720 ARG A NH2   1 
ATOM   9750  N N     . LYS A 1 2721 ? 204.615 217.160 187.605 1.00 16.94 ? 2721 LYS A N     1 
ATOM   9751  C CA    . LYS A 1 2721 ? 204.313 217.746 188.906 1.00 12.86 ? 2721 LYS A CA    1 
ATOM   9752  C C     . LYS A 1 2721 ? 203.814 219.175 188.726 1.00 17.60 ? 2721 LYS A C     1 
ATOM   9753  O O     . LYS A 1 2721 ? 204.463 219.965 188.033 1.00 17.74 ? 2721 LYS A O     1 
ATOM   9754  C CB    . LYS A 1 2721 ? 205.547 217.735 189.807 1.00 11.96 ? 2721 LYS A CB    1 
ATOM   9755  C CG    . LYS A 1 2721 ? 206.029 216.347 190.208 1.00 15.29 ? 2721 LYS A CG    1 
ATOM   9756  C CD    . LYS A 1 2721 ? 206.964 215.757 189.163 1.00 18.05 ? 2721 LYS A CD    1 
ATOM   9757  C CE    . LYS A 1 2721 ? 207.416 214.361 189.540 1.00 19.84 ? 2721 LYS A CE    1 
ATOM   9758  N NZ    . LYS A 1 2721 ? 208.207 213.735 188.446 1.00 16.14 ? 2721 LYS A NZ    1 
ATOM   9759  N N     . PRO A 1 2722 ? 202.674 219.539 189.313 1.00 18.60 ? 2722 PRO A N     1 
ATOM   9760  C CA    . PRO A 1 2722 ? 202.190 220.919 189.184 1.00 12.67 ? 2722 PRO A CA    1 
ATOM   9761  C C     . PRO A 1 2722 ? 203.191 221.913 189.753 1.00 11.87 ? 2722 PRO A C     1 
ATOM   9762  O O     . PRO A 1 2722 ? 203.836 221.662 190.772 1.00 11.22 ? 2722 PRO A O     1 
ATOM   9763  C CB    . PRO A 1 2722 ? 200.880 220.915 189.981 1.00 6.08  ? 2722 PRO A CB    1 
ATOM   9764  C CG    . PRO A 1 2722 ? 200.959 219.718 190.863 1.00 10.20 ? 2722 PRO A CG    1 
ATOM   9765  C CD    . PRO A 1 2722 ? 201.769 218.706 190.119 1.00 14.99 ? 2722 PRO A CD    1 
ATOM   9766  N N     . LEU A 1 2723 ? 203.317 223.051 189.077 1.00 9.64  ? 2723 LEU A N     1 
ATOM   9767  C CA    . LEU A 1 2723 ? 204.292 224.057 189.462 1.00 10.82 ? 2723 LEU A CA    1 
ATOM   9768  C C     . LEU A 1 2723 ? 203.768 224.906 190.614 1.00 11.45 ? 2723 LEU A C     1 
ATOM   9769  O O     . LEU A 1 2723 ? 202.562 225.132 190.751 1.00 11.15 ? 2723 LEU A O     1 
ATOM   9770  C CB    . LEU A 1 2723 ? 204.641 224.947 188.270 1.00 8.66  ? 2723 LEU A CB    1 
ATOM   9771  C CG    . LEU A 1 2723 ? 205.302 224.232 187.090 1.00 5.65  ? 2723 LEU A CG    1 
ATOM   9772  C CD1   . LEU A 1 2723 ? 205.471 225.170 185.908 1.00 6.45  ? 2723 LEU A CD1   1 
ATOM   9773  C CD2   . LEU A 1 2723 ? 206.635 223.642 187.502 1.00 10.54 ? 2723 LEU A CD2   1 
ATOM   9774  N N     . SER A 1 2724 ? 204.692 225.373 191.450 1.00 9.76  ? 2724 SER A N     1 
ATOM   9775  C CA    . SER A 1 2724 ? 204.321 226.176 192.604 1.00 7.05  ? 2724 SER A CA    1 
ATOM   9776  C C     . SER A 1 2724 ? 203.811 227.545 192.168 1.00 10.51 ? 2724 SER A C     1 
ATOM   9777  O O     . SER A 1 2724 ? 204.291 228.131 191.195 1.00 9.25  ? 2724 SER A O     1 
ATOM   9778  C CB    . SER A 1 2724 ? 205.511 226.336 193.550 1.00 4.10  ? 2724 SER A CB    1 
ATOM   9779  O OG    . SER A 1 2724 ? 206.514 227.154 192.977 1.00 5.25  ? 2724 SER A OG    1 
ATOM   9780  N N     . HIS A 1 2725 ? 202.825 228.054 192.911 1.00 7.55  ? 2725 HIS A N     1 
ATOM   9781  C CA    . HIS A 1 2725 ? 202.212 229.331 192.565 1.00 0.00  ? 2725 HIS A CA    1 
ATOM   9782  C C     . HIS A 1 2725 ? 203.203 230.481 192.674 1.00 0.00  ? 2725 HIS A C     1 
ATOM   9783  O O     . HIS A 1 2725 ? 203.099 231.460 191.926 1.00 6.83  ? 2725 HIS A O     1 
ATOM   9784  C CB    . HIS A 1 2725 ? 201.005 229.590 193.464 1.00 7.13  ? 2725 HIS A CB    1 
ATOM   9785  C CG    . HIS A 1 2725 ? 199.892 228.608 193.279 1.00 10.19 ? 2725 HIS A CG    1 
ATOM   9786  N ND1   . HIS A 1 2725 ? 198.758 228.897 192.551 1.00 13.80 ? 2725 HIS A ND1   1 
ATOM   9787  C CD2   . HIS A 1 2725 ? 199.738 227.341 193.728 1.00 5.73  ? 2725 HIS A CD2   1 
ATOM   9788  C CE1   . HIS A 1 2725 ? 197.954 227.850 192.560 1.00 13.68 ? 2725 HIS A CE1   1 
ATOM   9789  N NE2   . HIS A 1 2725 ? 198.525 226.892 193.267 1.00 9.23  ? 2725 HIS A NE2   1 
ATOM   9790  N N     . ARG A 1 2726 ? 204.164 230.381 193.594 1.00 0.00  ? 2726 ARG A N     1 
ATOM   9791  C CA    . ARG A 1 2726 ? 205.167 231.431 193.742 1.00 2.02  ? 2726 ARG A CA    1 
ATOM   9792  C C     . ARG A 1 2726 ? 205.963 231.615 192.457 1.00 4.17  ? 2726 ARG A C     1 
ATOM   9793  O O     . ARG A 1 2726 ? 206.202 232.746 192.021 1.00 7.98  ? 2726 ARG A O     1 
ATOM   9794  C CB    . ARG A 1 2726 ? 206.101 231.095 194.903 1.00 5.30  ? 2726 ARG A CB    1 
ATOM   9795  C CG    . ARG A 1 2726 ? 205.397 230.784 196.210 1.00 5.59  ? 2726 ARG A CG    1 
ATOM   9796  C CD    . ARG A 1 2726 ? 206.292 231.106 197.391 1.00 2.69  ? 2726 ARG A CD    1 
ATOM   9797  N NE    . ARG A 1 2726 ? 206.420 232.537 197.626 1.00 0.00  ? 2726 ARG A NE    1 
ATOM   9798  C CZ    . ARG A 1 2726 ? 207.076 233.067 198.648 1.00 0.44  ? 2726 ARG A CZ    1 
ATOM   9799  N NH1   . ARG A 1 2726 ? 207.708 232.311 199.528 1.00 7.02  ? 2726 ARG A NH1   1 
ATOM   9800  N NH2   . ARG A 1 2726 ? 207.102 234.388 198.788 1.00 1.68  ? 2726 ARG A NH2   1 
ATOM   9801  N N     . PHE A 1 2727 ? 206.390 230.511 191.842 1.00 4.89  ? 2727 PHE A N     1 
ATOM   9802  C CA    . PHE A 1 2727 ? 207.011 230.577 190.526 1.00 6.49  ? 2727 PHE A CA    1 
ATOM   9803  C C     . PHE A 1 2727 ? 205.988 230.814 189.426 1.00 6.08  ? 2727 PHE A C     1 
ATOM   9804  O O     . PHE A 1 2727 ? 206.303 231.459 188.421 1.00 13.06 ? 2727 PHE A O     1 
ATOM   9805  C CB    . PHE A 1 2727 ? 207.788 229.289 190.246 1.00 8.70  ? 2727 PHE A CB    1 
ATOM   9806  C CG    . PHE A 1 2727 ? 208.353 229.212 188.857 1.00 6.27  ? 2727 PHE A CG    1 
ATOM   9807  C CD1   . PHE A 1 2727 ? 209.362 230.067 188.454 1.00 9.36  ? 2727 PHE A CD1   1 
ATOM   9808  C CD2   . PHE A 1 2727 ? 207.873 228.279 187.955 1.00 3.79  ? 2727 PHE A CD2   1 
ATOM   9809  C CE1   . PHE A 1 2727 ? 209.876 229.995 187.177 1.00 3.51  ? 2727 PHE A CE1   1 
ATOM   9810  C CE2   . PHE A 1 2727 ? 208.386 228.202 186.680 1.00 4.18  ? 2727 PHE A CE2   1 
ATOM   9811  C CZ    . PHE A 1 2727 ? 209.388 229.061 186.290 1.00 7.14  ? 2727 PHE A CZ    1 
ATOM   9812  N N     . LEU A 1 2728 ? 204.765 230.318 189.607 1.00 5.69  ? 2728 LEU A N     1 
ATOM   9813  C CA    . LEU A 1 2728 ? 203.781 230.354 188.533 1.00 4.69  ? 2728 LEU A CA    1 
ATOM   9814  C C     . LEU A 1 2728 ? 203.323 231.777 188.239 1.00 0.45  ? 2728 LEU A C     1 
ATOM   9815  O O     . LEU A 1 2728 ? 203.006 232.106 187.091 1.00 9.68  ? 2728 LEU A O     1 
ATOM   9816  C CB    . LEU A 1 2728 ? 202.594 229.466 188.895 1.00 9.45  ? 2728 LEU A CB    1 
ATOM   9817  C CG    . LEU A 1 2728 ? 201.547 229.228 187.814 1.00 3.34  ? 2728 LEU A CG    1 
ATOM   9818  C CD1   . LEU A 1 2728 ? 202.132 228.318 186.761 1.00 3.35  ? 2728 LEU A CD1   1 
ATOM   9819  C CD2   . LEU A 1 2728 ? 200.305 228.610 188.420 1.00 4.44  ? 2728 LEU A CD2   1 
ATOM   9820  N N     . ARG A 1 2729 ? 203.277 232.638 189.259 1.00 0.67  ? 2729 ARG A N     1 
ATOM   9821  C CA    . ARG A 1 2729 ? 202.804 234.001 189.036 1.00 0.23  ? 2729 ARG A CA    1 
ATOM   9822  C C     . ARG A 1 2729 ? 203.752 234.792 188.144 1.00 4.38  ? 2729 ARG A C     1 
ATOM   9823  O O     . ARG A 1 2729 ? 203.322 235.724 187.455 1.00 10.92 ? 2729 ARG A O     1 
ATOM   9824  C CB    . ARG A 1 2729 ? 202.611 234.728 190.367 1.00 1.07  ? 2729 ARG A CB    1 
ATOM   9825  C CG    . ARG A 1 2729 ? 203.866 234.842 191.212 1.00 7.08  ? 2729 ARG A CG    1 
ATOM   9826  C CD    . ARG A 1 2729 ? 203.571 235.528 192.534 1.00 8.35  ? 2729 ARG A CD    1 
ATOM   9827  N NE    . ARG A 1 2729 ? 203.418 236.969 192.377 1.00 8.55  ? 2729 ARG A NE    1 
ATOM   9828  C CZ    . ARG A 1 2729 ? 204.330 237.863 192.736 1.00 7.78  ? 2729 ARG A CZ    1 
ATOM   9829  N NH1   . ARG A 1 2729 ? 205.465 237.501 193.309 1.00 11.23 ? 2729 ARG A NH1   1 
ATOM   9830  N NH2   . ARG A 1 2729 ? 204.095 239.152 192.516 1.00 8.42  ? 2729 ARG A NH2   1 
ATOM   9831  N N     . HIS A 1 2730 ? 205.039 234.445 188.142 1.00 2.87  ? 2730 HIS A N     1 
ATOM   9832  C CA    . HIS A 1 2730 ? 206.014 235.167 187.337 1.00 2.99  ? 2730 HIS A CA    1 
ATOM   9833  C C     . HIS A 1 2730 ? 206.063 234.699 185.891 1.00 6.28  ? 2730 HIS A C     1 
ATOM   9834  O O     . HIS A 1 2730 ? 206.677 235.374 185.059 1.00 6.78  ? 2730 HIS A O     1 
ATOM   9835  C CB    . HIS A 1 2730 ? 207.406 235.037 187.955 1.00 6.27  ? 2730 HIS A CB    1 
ATOM   9836  C CG    . HIS A 1 2730 ? 207.526 235.660 189.309 1.00 11.29 ? 2730 HIS A CG    1 
ATOM   9837  N ND1   . HIS A 1 2730 ? 207.190 236.973 189.554 1.00 11.39 ? 2730 HIS A ND1   1 
ATOM   9838  C CD2   . HIS A 1 2730 ? 207.941 235.150 190.492 1.00 10.32 ? 2730 HIS A CD2   1 
ATOM   9839  C CE1   . HIS A 1 2730 ? 207.397 237.248 190.828 1.00 8.75  ? 2730 HIS A CE1   1 
ATOM   9840  N NE2   . HIS A 1 2730 ? 207.850 236.158 191.421 1.00 12.04 ? 2730 HIS A NE2   1 
ATOM   9841  N N     . VAL A 1 2731 ? 205.444 233.569 185.570 1.00 7.45  ? 2731 VAL A N     1 
ATOM   9842  C CA    . VAL A 1 2731 ? 205.495 232.996 184.233 1.00 2.11  ? 2731 VAL A CA    1 
ATOM   9843  C C     . VAL A 1 2731 ? 204.075 232.878 183.691 1.00 1.53  ? 2731 VAL A C     1 
ATOM   9844  O O     . VAL A 1 2731 ? 203.275 232.097 184.212 1.00 10.33 ? 2731 VAL A O     1 
ATOM   9845  C CB    . VAL A 1 2731 ? 206.203 231.629 184.215 1.00 1.77  ? 2731 VAL A CB    1 
ATOM   9846  C CG1   . VAL A 1 2731 ? 207.700 231.819 184.344 1.00 8.99  ? 2731 VAL A CG1   1 
ATOM   9847  C CG2   . VAL A 1 2731 ? 205.706 230.736 185.335 1.00 2.28  ? 2731 VAL A CG2   1 
ATOM   9848  N N     . PRO A 1 2732 ? 203.701 233.648 182.674 1.00 2.17  ? 2732 PRO A N     1 
ATOM   9849  C CA    . PRO A 1 2732 ? 202.460 233.358 181.954 1.00 5.28  ? 2732 PRO A CA    1 
ATOM   9850  C C     . PRO A 1 2732 ? 202.592 232.073 181.153 1.00 7.12  ? 2732 PRO A C     1 
ATOM   9851  O O     . PRO A 1 2732 ? 203.681 231.677 180.732 1.00 7.99  ? 2732 PRO A O     1 
ATOM   9852  C CB    . PRO A 1 2732 ? 202.292 234.574 181.041 1.00 7.60  ? 2732 PRO A CB    1 
ATOM   9853  C CG    . PRO A 1 2732 ? 203.683 235.049 180.813 1.00 8.06  ? 2732 PRO A CG    1 
ATOM   9854  C CD    . PRO A 1 2732 ? 204.408 234.807 182.106 1.00 7.79  ? 2732 PRO A CD    1 
ATOM   9855  N N     . VAL A 1 2733 ? 201.458 231.413 180.946 1.00 4.76  ? 2733 VAL A N     1 
ATOM   9856  C CA    . VAL A 1 2733 ? 201.446 230.126 180.267 1.00 5.44  ? 2733 VAL A CA    1 
ATOM   9857  C C     . VAL A 1 2733 ? 200.506 230.188 179.072 1.00 9.19  ? 2733 VAL A C     1 
ATOM   9858  O O     . VAL A 1 2733 ? 199.398 230.728 179.147 1.00 9.39  ? 2733 VAL A O     1 
ATOM   9859  C CB    . VAL A 1 2733 ? 201.053 228.974 181.216 1.00 3.99  ? 2733 VAL A CB    1 
ATOM   9860  C CG1   . VAL A 1 2733 ? 202.164 228.714 182.217 1.00 6.20  ? 2733 VAL A CG1   1 
ATOM   9861  C CG2   . VAL A 1 2733 ? 199.769 229.296 181.932 1.00 8.11  ? 2733 VAL A CG2   1 
ATOM   9862  N N     . VAL A 1 2734 ? 200.967 229.626 177.957 1.00 8.65  ? 2734 VAL A N     1 
ATOM   9863  C CA    . VAL A 1 2734 ? 200.208 229.566 176.715 1.00 4.57  ? 2734 VAL A CA    1 
ATOM   9864  C C     . VAL A 1 2734 ? 199.840 228.114 176.460 1.00 7.61  ? 2734 VAL A C     1 
ATOM   9865  O O     . VAL A 1 2734 ? 200.713 227.239 176.461 1.00 12.30 ? 2734 VAL A O     1 
ATOM   9866  C CB    . VAL A 1 2734 ? 201.008 230.136 175.530 1.00 1.28  ? 2734 VAL A CB    1 
ATOM   9867  C CG1   . VAL A 1 2734 ? 200.108 230.314 174.321 1.00 3.53  ? 2734 VAL A CG1   1 
ATOM   9868  C CG2   . VAL A 1 2734 ? 201.667 231.440 175.916 1.00 6.03  ? 2734 VAL A CG2   1 
ATOM   9869  N N     . TYR A 1 2735 ? 198.554 227.858 176.242 1.00 5.34  ? 2735 TYR A N     1 
ATOM   9870  C CA    . TYR A 1 2735 ? 198.071 226.506 175.977 1.00 0.00  ? 2735 TYR A CA    1 
ATOM   9871  C C     . TYR A 1 2735 ? 198.179 226.236 174.482 1.00 2.07  ? 2735 TYR A C     1 
ATOM   9872  O O     . TYR A 1 2735 ? 197.442 226.813 173.679 1.00 11.35 ? 2735 TYR A O     1 
ATOM   9873  C CB    . TYR A 1 2735 ? 196.640 226.331 176.467 1.00 4.70  ? 2735 TYR A CB    1 
ATOM   9874  C CG    . TYR A 1 2735 ? 196.172 224.899 176.425 1.00 6.53  ? 2735 TYR A CG    1 
ATOM   9875  C CD1   . TYR A 1 2735 ? 197.057 223.855 176.648 1.00 10.21 ? 2735 TYR A CD1   1 
ATOM   9876  C CD2   . TYR A 1 2735 ? 194.850 224.587 176.150 1.00 8.70  ? 2735 TYR A CD2   1 
ATOM   9877  C CE1   . TYR A 1 2735 ? 196.638 222.543 176.607 1.00 9.72  ? 2735 TYR A CE1   1 
ATOM   9878  C CE2   . TYR A 1 2735 ? 194.423 223.280 176.105 1.00 11.42 ? 2735 TYR A CE2   1 
ATOM   9879  C CZ    . TYR A 1 2735 ? 195.321 222.261 176.335 1.00 14.84 ? 2735 TYR A CZ    1 
ATOM   9880  O OH    . TYR A 1 2735 ? 194.901 220.952 176.294 1.00 21.56 ? 2735 TYR A OH    1 
ATOM   9881  N N     . VAL A 1 2736 ? 199.101 225.352 174.105 1.00 1.62  ? 2736 VAL A N     1 
ATOM   9882  C CA    . VAL A 1 2736 ? 199.270 224.949 172.708 1.00 2.73  ? 2736 VAL A CA    1 
ATOM   9883  C C     . VAL A 1 2736 ? 198.586 223.592 172.568 1.00 3.75  ? 2736 VAL A C     1 
ATOM   9884  O O     . VAL A 1 2736 ? 199.087 222.566 173.022 1.00 8.22  ? 2736 VAL A O     1 
ATOM   9885  C CB    . VAL A 1 2736 ? 200.738 224.907 172.296 1.00 0.00  ? 2736 VAL A CB    1 
ATOM   9886  C CG1   . VAL A 1 2736 ? 200.861 224.744 170.792 1.00 1.92  ? 2736 VAL A CG1   1 
ATOM   9887  C CG2   . VAL A 1 2736 ? 201.449 226.166 172.753 1.00 3.71  ? 2736 VAL A CG2   1 
ATOM   9888  N N     . ASP A 1 2737 ? 197.423 223.591 171.925 1.00 2.26  ? 2737 ASP A N     1 
ATOM   9889  C CA    . ASP A 1 2737 ? 196.645 222.376 171.757 1.00 6.56  ? 2737 ASP A CA    1 
ATOM   9890  C C     . ASP A 1 2737 ? 196.956 221.723 170.410 1.00 12.72 ? 2737 ASP A C     1 
ATOM   9891  O O     . ASP A 1 2737 ? 197.681 222.266 169.573 1.00 12.68 ? 2737 ASP A O     1 
ATOM   9892  C CB    . ASP A 1 2737 ? 195.154 222.688 171.876 1.00 7.47  ? 2737 ASP A CB    1 
ATOM   9893  C CG    . ASP A 1 2737 ? 194.332 221.478 172.270 1.00 11.62 ? 2737 ASP A CG    1 
ATOM   9894  O OD1   . ASP A 1 2737 ? 194.925 220.411 172.527 1.00 10.67 ? 2737 ASP A OD1   1 
ATOM   9895  O OD2   . ASP A 1 2737 ? 193.091 221.598 172.328 1.00 15.31 ? 2737 ASP A OD2   1 
ATOM   9896  N N     . TYR A 1 2738 ? 196.404 220.530 170.214 1.00 11.50 ? 2738 TYR A N     1 
ATOM   9897  C CA    . TYR A 1 2738 ? 196.508 219.859 168.926 1.00 2.86  ? 2738 TYR A CA    1 
ATOM   9898  C C     . TYR A 1 2738 ? 195.813 220.674 167.841 1.00 10.10 ? 2738 TYR A C     1 
ATOM   9899  O O     . TYR A 1 2738 ? 194.698 221.168 168.060 1.00 13.15 ? 2738 TYR A O     1 
ATOM   9900  C CB    . TYR A 1 2738 ? 195.902 218.459 168.998 1.00 8.19  ? 2738 TYR A CB    1 
ATOM   9901  C CG    . TYR A 1 2738 ? 196.727 217.463 169.772 1.00 6.25  ? 2738 TYR A CG    1 
ATOM   9902  C CD1   . TYR A 1 2738 ? 198.060 217.713 170.055 1.00 6.60  ? 2738 TYR A CD1   1 
ATOM   9903  C CD2   . TYR A 1 2738 ? 196.171 216.280 170.231 1.00 9.51  ? 2738 TYR A CD2   1 
ATOM   9904  C CE1   . TYR A 1 2738 ? 198.821 216.804 170.753 1.00 8.45  ? 2738 TYR A CE1   1 
ATOM   9905  C CE2   . TYR A 1 2738 ? 196.923 215.367 170.939 1.00 10.61 ? 2738 TYR A CE2   1 
ATOM   9906  C CZ    . TYR A 1 2738 ? 198.248 215.635 171.197 1.00 10.82 ? 2738 TYR A CZ    1 
ATOM   9907  O OH    . TYR A 1 2738 ? 199.005 214.730 171.903 1.00 9.99  ? 2738 TYR A OH    1 
ATOM   9908  N N     . PRO A 1 2739 ? 196.434 220.846 166.678 1.00 12.86 ? 2739 PRO A N     1 
ATOM   9909  C CA    . PRO A 1 2739 ? 195.760 221.527 165.569 1.00 8.99  ? 2739 PRO A CA    1 
ATOM   9910  C C     . PRO A 1 2739 ? 194.484 220.804 165.163 1.00 10.55 ? 2739 PRO A C     1 
ATOM   9911  O O     . PRO A 1 2739 ? 194.405 219.574 165.199 1.00 8.63  ? 2739 PRO A O     1 
ATOM   9912  C CB    . PRO A 1 2739 ? 196.809 221.491 164.455 1.00 8.44  ? 2739 PRO A CB    1 
ATOM   9913  C CG    . PRO A 1 2739 ? 198.108 221.439 165.174 1.00 11.10 ? 2739 PRO A CG    1 
ATOM   9914  C CD    . PRO A 1 2739 ? 197.860 220.608 166.399 1.00 12.34 ? 2739 PRO A CD    1 
ATOM   9915  N N     . GLY A 1 2740 ? 193.477 221.580 164.774 1.00 17.44 ? 2740 GLY A N     1 
ATOM   9916  C CA    . GLY A 1 2740 ? 192.208 221.034 164.360 1.00 17.88 ? 2740 GLY A CA    1 
ATOM   9917  C C     . GLY A 1 2740 ? 192.265 220.437 162.969 1.00 14.26 ? 2740 GLY A C     1 
ATOM   9918  O O     . GLY A 1 2740 ? 193.269 220.552 162.260 1.00 12.19 ? 2740 GLY A O     1 
ATOM   9919  N N     . PRO A 1 2741 ? 191.181 219.771 162.558 1.00 12.98 ? 2741 PRO A N     1 
ATOM   9920  C CA    . PRO A 1 2741 ? 191.180 219.138 161.226 1.00 13.48 ? 2741 PRO A CA    1 
ATOM   9921  C C     . PRO A 1 2741 ? 191.446 220.109 160.087 1.00 17.86 ? 2741 PRO A C     1 
ATOM   9922  O O     . PRO A 1 2741 ? 192.187 219.774 159.155 1.00 20.57 ? 2741 PRO A O     1 
ATOM   9923  C CB    . PRO A 1 2741 ? 189.777 218.523 161.141 1.00 15.07 ? 2741 PRO A CB    1 
ATOM   9924  C CG    . PRO A 1 2741 ? 189.361 218.324 162.557 1.00 15.12 ? 2741 PRO A CG    1 
ATOM   9925  C CD    . PRO A 1 2741 ? 189.971 219.451 163.332 1.00 16.56 ? 2741 PRO A CD    1 
ATOM   9926  N N     . ALA A 1 2742 ? 190.869 221.312 160.137 1.00 19.15 ? 2742 ALA A N     1 
ATOM   9927  C CA    . ALA A 1 2742 ? 191.146 222.299 159.098 1.00 18.52 ? 2742 ALA A CA    1 
ATOM   9928  C C     . ALA A 1 2742 ? 192.592 222.770 159.163 1.00 20.63 ? 2742 ALA A C     1 
ATOM   9929  O O     . ALA A 1 2742 ? 193.265 222.896 158.131 1.00 17.85 ? 2742 ALA A O     1 
ATOM   9930  C CB    . ALA A 1 2742 ? 190.190 223.482 159.227 1.00 17.87 ? 2742 ALA A CB    1 
ATOM   9931  N N     . SER A 1 2743 ? 193.086 223.036 160.373 1.00 20.41 ? 2743 SER A N     1 
ATOM   9932  C CA    . SER A 1 2743 ? 194.478 223.436 160.527 1.00 13.58 ? 2743 SER A CA    1 
ATOM   9933  C C     . SER A 1 2743 ? 195.420 222.322 160.094 1.00 14.39 ? 2743 SER A C     1 
ATOM   9934  O O     . SER A 1 2743 ? 196.416 222.580 159.414 1.00 19.46 ? 2743 SER A O     1 
ATOM   9935  C CB    . SER A 1 2743 ? 194.745 223.846 161.972 1.00 13.41 ? 2743 SER A CB    1 
ATOM   9936  O OG    . SER A 1 2743 ? 194.467 222.777 162.852 1.00 14.61 ? 2743 SER A OG    1 
ATOM   9937  N N     . LEU A 1 2744 ? 195.117 221.074 160.465 1.00 15.37 ? 2744 LEU A N     1 
ATOM   9938  C CA    . LEU A 1 2744 ? 195.945 219.951 160.031 1.00 13.46 ? 2744 LEU A CA    1 
ATOM   9939  C C     . LEU A 1 2744 ? 195.947 219.819 158.514 1.00 14.97 ? 2744 LEU A C     1 
ATOM   9940  O O     . LEU A 1 2744 ? 196.992 219.547 157.904 1.00 15.01 ? 2744 LEU A O     1 
ATOM   9941  C CB    . LEU A 1 2744 ? 195.451 218.654 160.669 1.00 11.56 ? 2744 LEU A CB    1 
ATOM   9942  C CG    . LEU A 1 2744 ? 195.809 218.390 162.129 1.00 15.37 ? 2744 LEU A CG    1 
ATOM   9943  C CD1   . LEU A 1 2744 ? 194.851 217.374 162.723 1.00 11.80 ? 2744 LEU A CD1   1 
ATOM   9944  C CD2   . LEU A 1 2744 ? 197.244 217.908 162.239 1.00 9.60  ? 2744 LEU A CD2   1 
ATOM   9945  N N     . THR A 1 2745 ? 194.778 219.987 157.892 1.00 12.13 ? 2745 THR A N     1 
ATOM   9946  C CA    . THR A 1 2745 ? 194.689 219.916 156.440 1.00 11.26 ? 2745 THR A CA    1 
ATOM   9947  C C     . THR A 1 2745 ? 195.543 220.994 155.792 1.00 11.75 ? 2745 THR A C     1 
ATOM   9948  O O     . THR A 1 2745 ? 196.310 220.719 154.865 1.00 17.11 ? 2745 THR A O     1 
ATOM   9949  C CB    . THR A 1 2745 ? 193.232 220.043 155.997 1.00 10.68 ? 2745 THR A CB    1 
ATOM   9950  O OG1   . THR A 1 2745 ? 192.463 218.976 156.565 1.00 12.23 ? 2745 THR A OG1   1 
ATOM   9951  C CG2   . THR A 1 2745 ? 193.130 219.982 154.483 1.00 16.33 ? 2745 THR A CG2   1 
ATOM   9952  N N     . GLN A 1 2746 ? 195.443 222.230 156.284 1.00 12.40 ? 2746 GLN A N     1 
ATOM   9953  C CA    . GLN A 1 2746 ? 196.260 223.302 155.729 1.00 15.32 ? 2746 GLN A CA    1 
ATOM   9954  C C     . GLN A 1 2746 ? 197.745 223.078 155.982 1.00 10.69 ? 2746 GLN A C     1 
ATOM   9955  O O     . GLN A 1 2746 ? 198.572 223.474 155.153 1.00 8.89  ? 2746 GLN A O     1 
ATOM   9956  C CB    . GLN A 1 2746 ? 195.826 224.651 156.304 1.00 16.32 ? 2746 GLN A CB    1 
ATOM   9957  C CG    . GLN A 1 2746 ? 196.388 225.849 155.556 1.00 11.50 ? 2746 GLN A CG    1 
ATOM   9958  C CD    . GLN A 1 2746 ? 196.677 227.025 156.465 1.00 13.94 ? 2746 GLN A CD    1 
ATOM   9959  O OE1   . GLN A 1 2746 ? 195.906 227.322 157.377 1.00 15.22 ? 2746 GLN A OE1   1 
ATOM   9960  N NE2   . GLN A 1 2746 ? 197.790 227.704 156.217 1.00 13.06 ? 2746 GLN A NE2   1 
ATOM   9961  N N     . ILE A 1 2747 ? 198.098 222.450 157.099 1.00 8.68  ? 2747 ILE A N     1 
ATOM   9962  C CA    . ILE A 1 2747 ? 199.494 222.185 157.433 1.00 7.74  ? 2747 ILE A CA    1 
ATOM   9963  C C     . ILE A 1 2747 ? 200.102 221.156 156.499 1.00 16.19 ? 2747 ILE A C     1 
ATOM   9964  O O     . ILE A 1 2747 ? 201.197 221.352 155.966 1.00 27.34 ? 2747 ILE A O     1 
ATOM   9965  C CB    . ILE A 1 2747 ? 199.607 221.725 158.901 1.00 6.88  ? 2747 ILE A CB    1 
ATOM   9966  C CG1   . ILE A 1 2747 ? 199.337 222.881 159.857 1.00 12.69 ? 2747 ILE A CG1   1 
ATOM   9967  C CG2   . ILE A 1 2747 ? 200.987 221.146 159.171 1.00 5.97  ? 2747 ILE A CG2   1 
ATOM   9968  C CD1   . ILE A 1 2747 ? 199.233 222.437 161.285 1.00 14.60 ? 2747 ILE A CD1   1 
ATOM   9969  N N     . TYR A 1 2748 ? 199.407 220.042 156.284 1.00 10.40 ? 2748 TYR A N     1 
ATOM   9970  C CA    . TYR A 1 2748 ? 200.039 218.936 155.578 1.00 10.31 ? 2748 TYR A CA    1 
ATOM   9971  C C     . TYR A 1 2748 ? 199.661 218.859 154.106 1.00 15.17 ? 2748 TYR A C     1 
ATOM   9972  O O     . TYR A 1 2748 ? 200.312 218.125 153.357 1.00 20.04 ? 2748 TYR A O     1 
ATOM   9973  C CB    . TYR A 1 2748 ? 199.731 217.616 156.290 1.00 6.65  ? 2748 TYR A CB    1 
ATOM   9974  C CG    . TYR A 1 2748 ? 200.429 217.540 157.628 1.00 14.20 ? 2748 TYR A CG    1 
ATOM   9975  C CD1   . TYR A 1 2748 ? 201.790 217.288 157.705 1.00 9.60  ? 2748 TYR A CD1   1 
ATOM   9976  C CD2   . TYR A 1 2748 ? 199.736 217.755 158.810 1.00 15.52 ? 2748 TYR A CD2   1 
ATOM   9977  C CE1   . TYR A 1 2748 ? 202.439 217.240 158.921 1.00 4.26  ? 2748 TYR A CE1   1 
ATOM   9978  C CE2   . TYR A 1 2748 ? 200.377 217.708 160.031 1.00 5.10  ? 2748 TYR A CE2   1 
ATOM   9979  C CZ    . TYR A 1 2748 ? 201.728 217.451 160.079 1.00 0.89  ? 2748 TYR A CZ    1 
ATOM   9980  O OH    . TYR A 1 2748 ? 202.371 217.399 161.292 1.00 10.66 ? 2748 TYR A OH    1 
ATOM   9981  N N     . GLY A 1 2749 ? 198.666 219.624 153.651 1.00 8.92  ? 2749 GLY A N     1 
ATOM   9982  C CA    . GLY A 1 2749 ? 198.437 219.730 152.222 1.00 5.67  ? 2749 GLY A CA    1 
ATOM   9983  C C     . GLY A 1 2749 ? 199.599 220.384 151.507 1.00 15.71 ? 2749 GLY A C     1 
ATOM   9984  O O     . GLY A 1 2749 ? 199.973 219.975 150.407 1.00 22.89 ? 2749 GLY A O     1 
ATOM   9985  N N     . THR A 1 2750 ? 200.190 221.408 152.126 1.00 10.87 ? 2750 THR A N     1 
ATOM   9986  C CA    . THR A 1 2750 ? 201.381 222.030 151.557 1.00 12.96 ? 2750 THR A CA    1 
ATOM   9987  C C     . THR A 1 2750 ? 202.523 221.028 151.461 1.00 14.57 ? 2750 THR A C     1 
ATOM   9988  O O     . THR A 1 2750 ? 203.225 220.965 150.444 1.00 19.06 ? 2750 THR A O     1 
ATOM   9989  C CB    . THR A 1 2750 ? 201.794 223.235 152.404 1.00 13.95 ? 2750 THR A CB    1 
ATOM   9990  O OG1   . THR A 1 2750 ? 200.826 224.281 152.256 1.00 21.32 ? 2750 THR A OG1   1 
ATOM   9991  C CG2   . THR A 1 2750 ? 203.157 223.753 151.978 1.00 17.44 ? 2750 THR A CG2   1 
ATOM   9992  N N     . PHE A 1 2751 ? 202.710 220.226 152.509 1.00 10.95 ? 2751 PHE A N     1 
ATOM   9993  C CA    . PHE A 1 2751 ? 203.755 219.209 152.501 1.00 13.47 ? 2751 PHE A CA    1 
ATOM   9994  C C     . PHE A 1 2751 ? 203.506 218.166 151.418 1.00 18.70 ? 2751 PHE A C     1 
ATOM   9995  O O     . PHE A 1 2751 ? 204.436 217.763 150.710 1.00 21.06 ? 2751 PHE A O     1 
ATOM   9996  C CB    . PHE A 1 2751 ? 203.839 218.556 153.878 1.00 14.01 ? 2751 PHE A CB    1 
ATOM   9997  C CG    . PHE A 1 2751 ? 204.626 219.352 154.876 1.00 11.86 ? 2751 PHE A CG    1 
ATOM   9998  C CD1   . PHE A 1 2751 ? 205.469 220.366 154.460 1.00 16.04 ? 2751 PHE A CD1   1 
ATOM   9999  C CD2   . PHE A 1 2751 ? 204.502 219.106 156.231 1.00 7.13  ? 2751 PHE A CD2   1 
ATOM   10000 C CE1   . PHE A 1 2751 ? 206.192 221.104 155.376 1.00 13.02 ? 2751 PHE A CE1   1 
ATOM   10001 C CE2   . PHE A 1 2751 ? 205.220 219.844 157.150 1.00 12.95 ? 2751 PHE A CE2   1 
ATOM   10002 C CZ    . PHE A 1 2751 ? 206.066 220.843 156.722 1.00 9.00  ? 2751 PHE A CZ    1 
ATOM   10003 N N     . ASN A 1 2752 ? 202.256 217.719 151.269 1.00 12.71 ? 2752 ASN A N     1 
ATOM   10004 C CA    . ASN A 1 2752 ? 201.939 216.748 150.227 1.00 11.96 ? 2752 ASN A CA    1 
ATOM   10005 C C     . ASN A 1 2752 ? 202.177 217.326 148.836 1.00 18.41 ? 2752 ASN A C     1 
ATOM   10006 O O     . ASN A 1 2752 ? 202.732 216.648 147.963 1.00 23.58 ? 2752 ASN A O     1 
ATOM   10007 C CB    . ASN A 1 2752 ? 200.493 216.269 150.362 1.00 11.93 ? 2752 ASN A CB    1 
ATOM   10008 C CG    . ASN A 1 2752 ? 200.269 215.419 151.597 1.00 15.05 ? 2752 ASN A CG    1 
ATOM   10009 O OD1   . ASN A 1 2752 ? 199.437 215.738 152.441 1.00 11.60 ? 2752 ASN A OD1   1 
ATOM   10010 N ND2   . ASN A 1 2752 ? 201.022 214.335 151.714 1.00 22.08 ? 2752 ASN A ND2   1 
ATOM   10011 N N     . ARG A 1 2753 ? 201.754 218.573 148.605 1.00 11.11 ? 2753 ARG A N     1 
ATOM   10012 C CA    . ARG A 1 2753 ? 201.963 219.189 147.299 1.00 13.50 ? 2753 ARG A CA    1 
ATOM   10013 C C     . ARG A 1 2753 ? 203.446 219.348 146.995 1.00 18.27 ? 2753 ARG A C     1 
ATOM   10014 O O     . ARG A 1 2753 ? 203.881 219.117 145.861 1.00 21.90 ? 2753 ARG A O     1 
ATOM   10015 C CB    . ARG A 1 2753 ? 201.254 220.541 147.220 1.00 19.51 ? 2753 ARG A CB    1 
ATOM   10016 C CG    . ARG A 1 2753 ? 199.744 220.477 147.376 1.00 17.45 ? 2753 ARG A CG    1 
ATOM   10017 C CD    . ARG A 1 2753 ? 199.091 221.792 146.974 1.00 17.26 ? 2753 ARG A CD    1 
ATOM   10018 N NE    . ARG A 1 2753 ? 199.737 222.944 147.592 1.00 14.11 ? 2753 ARG A NE    1 
ATOM   10019 C CZ    . ARG A 1 2753 ? 199.384 223.466 148.758 1.00 16.49 ? 2753 ARG A CZ    1 
ATOM   10020 N NH1   . ARG A 1 2753 ? 198.377 222.974 149.460 1.00 11.86 ? 2753 ARG A NH1   1 
ATOM   10021 N NH2   . ARG A 1 2753 ? 200.054 224.513 149.230 1.00 19.90 ? 2753 ARG A NH2   1 
ATOM   10022 N N     . ALA A 1 2754 ? 204.238 219.747 147.991 1.00 9.92  ? 2754 ALA A N     1 
ATOM   10023 C CA    . ALA A 1 2754 ? 205.674 219.874 147.775 1.00 15.92 ? 2754 ALA A CA    1 
ATOM   10024 C C     . ALA A 1 2754 ? 206.327 218.521 147.527 1.00 22.12 ? 2754 ALA A C     1 
ATOM   10025 O O     . ALA A 1 2754 ? 207.264 218.422 146.727 1.00 24.04 ? 2754 ALA A O     1 
ATOM   10026 C CB    . ALA A 1 2754 ? 206.325 220.567 148.969 1.00 17.28 ? 2754 ALA A CB    1 
ATOM   10027 N N     . MET A 1 2755 ? 205.848 217.475 148.200 1.00 18.14 ? 2755 MET A N     1 
ATOM   10028 C CA    . MET A 1 2755 ? 206.425 216.147 148.032 1.00 14.24 ? 2755 MET A CA    1 
ATOM   10029 C C     . MET A 1 2755 ? 206.102 215.564 146.662 1.00 18.31 ? 2755 MET A C     1 
ATOM   10030 O O     . MET A 1 2755 ? 206.969 214.963 146.016 1.00 22.42 ? 2755 MET A O     1 
ATOM   10031 C CB    . MET A 1 2755 ? 205.915 215.228 149.136 1.00 15.90 ? 2755 MET A CB    1 
ATOM   10032 C CG    . MET A 1 2755 ? 205.844 213.771 148.753 1.00 18.53 ? 2755 MET A CG    1 
ATOM   10033 S SD    . MET A 1 2755 ? 205.339 212.768 150.152 1.00 20.21 ? 2755 MET A SD    1 
ATOM   10034 C CE    . MET A 1 2755 ? 203.582 213.094 150.157 1.00 11.10 ? 2755 MET A CE    1 
ATOM   10035 N N     . LEU A 1 2756 ? 204.867 215.742 146.194 1.00 17.54 ? 2756 LEU A N     1 
ATOM   10036 C CA    . LEU A 1 2756 ? 204.430 215.123 144.949 1.00 17.19 ? 2756 LEU A CA    1 
ATOM   10037 C C     . LEU A 1 2756 ? 204.999 215.794 143.705 1.00 21.24 ? 2756 LEU A C     1 
ATOM   10038 O O     . LEU A 1 2756 ? 204.533 215.503 142.600 1.00 27.87 ? 2756 LEU A O     1 
ATOM   10039 C CB    . LEU A 1 2756 ? 202.901 215.114 144.871 1.00 16.29 ? 2756 LEU A CB    1 
ATOM   10040 C CG    . LEU A 1 2756 ? 202.188 214.255 145.915 1.00 16.87 ? 2756 LEU A CG    1 
ATOM   10041 C CD1   . LEU A 1 2756 ? 200.704 214.191 145.631 1.00 16.78 ? 2756 LEU A CD1   1 
ATOM   10042 C CD2   . LEU A 1 2756 ? 202.784 212.860 145.958 1.00 21.03 ? 2756 LEU A CD2   1 
ATOM   10043 N N     . ARG A 1 2757 ? 205.986 216.680 143.850 1.00 21.31 ? 2757 ARG A N     1 
ATOM   10044 C CA    . ARG A 1 2757 ? 206.588 217.309 142.683 1.00 23.31 ? 2757 ARG A CA    1 
ATOM   10045 C C     . ARG A 1 2757 ? 207.509 216.363 141.920 1.00 28.85 ? 2757 ARG A C     1 
ATOM   10046 O O     . ARG A 1 2757 ? 207.861 216.657 140.773 1.00 28.38 ? 2757 ARG A O     1 
ATOM   10047 C CB    . ARG A 1 2757 ? 207.347 218.569 143.100 1.00 20.12 ? 2757 ARG A CB    1 
ATOM   10048 C CG    . ARG A 1 2757 ? 206.453 219.790 143.250 1.00 22.04 ? 2757 ARG A CG    1 
ATOM   10049 C CD    . ARG A 1 2757 ? 207.238 221.083 143.106 1.00 23.80 ? 2757 ARG A CD    1 
ATOM   10050 N NE    . ARG A 1 2757 ? 208.062 221.354 144.277 1.00 23.79 ? 2757 ARG A NE    1 
ATOM   10051 C CZ    . ARG A 1 2757 ? 207.635 221.992 145.359 1.00 23.76 ? 2757 ARG A CZ    1 
ATOM   10052 N NH1   . ARG A 1 2757 ? 206.394 222.439 145.452 1.00 22.74 ? 2757 ARG A NH1   1 
ATOM   10053 N NH2   . ARG A 1 2757 ? 208.474 222.185 146.372 1.00 22.05 ? 2757 ARG A NH2   1 
ATOM   10054 N N     . LEU A 1 2758 ? 207.908 215.239 142.523 1.00 23.75 ? 2758 LEU A N     1 
ATOM   10055 C CA    . LEU A 1 2758 ? 208.673 214.242 141.782 1.00 22.84 ? 2758 LEU A CA    1 
ATOM   10056 C C     . LEU A 1 2758 ? 207.802 213.451 140.819 1.00 24.75 ? 2758 LEU A C     1 
ATOM   10057 O O     . LEU A 1 2758 ? 208.330 212.830 139.891 1.00 28.27 ? 2758 LEU A O     1 
ATOM   10058 C CB    . LEU A 1 2758 ? 209.380 213.271 142.730 1.00 25.53 ? 2758 LEU A CB    1 
ATOM   10059 C CG    . LEU A 1 2758 ? 210.680 213.728 143.397 1.00 27.88 ? 2758 LEU A CG    1 
ATOM   10060 C CD1   . LEU A 1 2758 ? 210.396 214.680 144.533 1.00 20.73 ? 2758 LEU A CD1   1 
ATOM   10061 C CD2   . LEU A 1 2758 ? 211.491 212.541 143.877 1.00 25.99 ? 2758 LEU A CD2   1 
ATOM   10062 N N     . ILE A 1 2759 ? 206.490 213.455 141.019 1.00 24.83 ? 2759 ILE A N     1 
ATOM   10063 C CA    . ILE A 1 2759 ? 205.564 212.721 140.162 1.00 24.94 ? 2759 ILE A CA    1 
ATOM   10064 C C     . ILE A 1 2759 ? 204.475 213.663 139.649 1.00 25.02 ? 2759 ILE A C     1 
ATOM   10065 O O     . ILE A 1 2759 ? 203.363 213.703 140.193 1.00 21.29 ? 2759 ILE A O     1 
ATOM   10066 C CB    . ILE A 1 2759 ? 205.025 211.476 140.893 1.00 20.24 ? 2759 ILE A CB    1 
ATOM   10067 C CG1   . ILE A 1 2759 ? 204.246 211.836 142.165 1.00 21.73 ? 2759 ILE A CG1   1 
ATOM   10068 C CG2   . ILE A 1 2759 ? 206.151 210.498 141.205 1.00 23.62 ? 2759 ILE A CG2   1 
ATOM   10069 C CD1   . ILE A 1 2759 ? 203.518 210.672 142.778 1.00 23.41 ? 2759 ILE A CD1   1 
ATOM   10070 N N     . PRO A 1 2760 ? 204.766 214.453 138.609 1.00 26.01 ? 2760 PRO A N     1 
ATOM   10071 C CA    . PRO A 1 2760 ? 203.727 215.313 138.016 1.00 24.91 ? 2760 PRO A CA    1 
ATOM   10072 C C     . PRO A 1 2760 ? 202.439 214.588 137.673 1.00 24.11 ? 2760 PRO A C     1 
ATOM   10073 O O     . PRO A 1 2760 ? 201.395 215.238 137.545 1.00 29.80 ? 2760 PRO A O     1 
ATOM   10074 C CB    . PRO A 1 2760 ? 204.406 215.849 136.747 1.00 25.98 ? 2760 PRO A CB    1 
ATOM   10075 C CG    . PRO A 1 2760 ? 205.887 215.661 136.958 1.00 25.50 ? 2760 PRO A CG    1 
ATOM   10076 C CD    . PRO A 1 2760 ? 206.116 214.907 138.233 1.00 24.86 ? 2760 PRO A CD    1 
ATOM   10077 N N     . SER A 1 2761 ? 202.474 213.263 137.518 1.00 19.98 ? 2761 SER A N     1 
ATOM   10078 C CA    . SER A 1 2761 ? 201.290 212.509 137.128 1.00 22.94 ? 2761 SER A CA    1 
ATOM   10079 C C     . SER A 1 2761 ? 200.256 212.397 138.240 1.00 23.98 ? 2761 SER A C     1 
ATOM   10080 O O     . SER A 1 2761 ? 199.141 211.940 137.973 1.00 25.18 ? 2761 SER A O     1 
ATOM   10081 C CB    . SER A 1 2761 ? 201.700 211.110 136.665 1.00 24.50 ? 2761 SER A CB    1 
ATOM   10082 O OG    . SER A 1 2761 ? 202.294 210.376 137.721 1.00 27.47 ? 2761 SER A OG    1 
ATOM   10083 N N     . LEU A 1 2762 ? 200.588 212.797 139.469 1.00 22.22 ? 2762 LEU A N     1 
ATOM   10084 C CA    . LEU A 1 2762 ? 199.693 212.604 140.604 1.00 24.71 ? 2762 LEU A CA    1 
ATOM   10085 C C     . LEU A 1 2762 ? 199.511 213.884 141.413 1.00 28.92 ? 2762 LEU A C     1 
ATOM   10086 O O     . LEU A 1 2762 ? 199.252 213.828 142.618 1.00 26.84 ? 2762 LEU A O     1 
ATOM   10087 C CB    . LEU A 1 2762 ? 200.195 211.472 141.502 1.00 23.94 ? 2762 LEU A CB    1 
ATOM   10088 C CG    . LEU A 1 2762 ? 199.898 210.060 140.992 1.00 28.68 ? 2762 LEU A CG    1 
ATOM   10089 C CD1   . LEU A 1 2762 ? 200.571 209.002 141.847 1.00 23.94 ? 2762 LEU A CD1   1 
ATOM   10090 C CD2   . LEU A 1 2762 ? 198.401 209.826 140.942 1.00 27.20 ? 2762 LEU A CD2   1 
ATOM   10091 N N     . ARG A 1 2763 ? 199.633 215.048 140.767 1.00 27.59 ? 2763 ARG A N     1 
ATOM   10092 C CA    . ARG A 1 2763 ? 199.342 216.304 141.454 1.00 26.00 ? 2763 ARG A CA    1 
ATOM   10093 C C     . ARG A 1 2763 ? 197.885 216.385 141.880 1.00 26.94 ? 2763 ARG A C     1 
ATOM   10094 O O     . ARG A 1 2763 ? 197.584 216.883 142.970 1.00 26.31 ? 2763 ARG A O     1 
ATOM   10095 C CB    . ARG A 1 2763 ? 199.687 217.500 140.565 1.00 29.42 ? 2763 ARG A CB    1 
ATOM   10096 C CG    . ARG A 1 2763 ? 201.022 217.423 139.852 1.00 28.30 ? 2763 ARG A CG    1 
ATOM   10097 C CD    . ARG A 1 2763 ? 202.141 217.081 140.817 1.00 26.52 ? 2763 ARG A CD    1 
ATOM   10098 N NE    . ARG A 1 2763 ? 202.198 218.035 141.918 1.00 29.28 ? 2763 ARG A NE    1 
ATOM   10099 C CZ    . ARG A 1 2763 ? 203.012 219.080 141.962 1.00 31.13 ? 2763 ARG A CZ    1 
ATOM   10100 N NH1   . ARG A 1 2763 ? 203.838 219.356 140.966 1.00 29.66 ? 2763 ARG A NH1   1 
ATOM   10101 N NH2   . ARG A 1 2763 ? 202.993 219.873 143.030 1.00 27.67 ? 2763 ARG A NH2   1 
ATOM   10102 N N     . THR A 1 2764 ? 196.972 215.900 141.039 1.00 27.60 ? 2764 THR A N     1 
ATOM   10103 C CA    . THR A 1 2764 ? 195.551 215.989 141.344 1.00 31.18 ? 2764 THR A CA    1 
ATOM   10104 C C     . THR A 1 2764 ? 195.158 215.134 142.539 1.00 26.50 ? 2764 THR A C     1 
ATOM   10105 O O     . THR A 1 2764 ? 194.037 215.270 143.039 1.00 24.96 ? 2764 THR A O     1 
ATOM   10106 C CB    . THR A 1 2764 ? 194.721 215.579 140.127 1.00 30.94 ? 2764 THR A CB    1 
ATOM   10107 O OG1   . THR A 1 2764 ? 194.740 214.152 139.993 1.00 24.96 ? 2764 THR A OG1   1 
ATOM   10108 C CG2   . THR A 1 2764 ? 195.282 216.210 138.862 1.00 28.55 ? 2764 THR A CG2   1 
ATOM   10109 N N     . TYR A 1 2765 ? 196.045 214.256 143.005 1.00 21.24 ? 2765 TYR A N     1 
ATOM   10110 C CA    . TYR A 1 2765 ? 195.744 213.379 144.125 1.00 21.20 ? 2765 TYR A CA    1 
ATOM   10111 C C     . TYR A 1 2765 ? 196.359 213.858 145.435 1.00 25.76 ? 2765 TYR A C     1 
ATOM   10112 O O     . TYR A 1 2765 ? 196.324 213.123 146.426 1.00 23.23 ? 2765 TYR A O     1 
ATOM   10113 C CB    . TYR A 1 2765 ? 196.205 211.953 143.819 1.00 19.35 ? 2765 TYR A CB    1 
ATOM   10114 C CG    . TYR A 1 2765 ? 195.164 211.149 143.076 1.00 25.10 ? 2765 TYR A CG    1 
ATOM   10115 C CD1   . TYR A 1 2765 ? 194.113 210.548 143.751 1.00 22.42 ? 2765 TYR A CD1   1 
ATOM   10116 C CD2   . TYR A 1 2765 ? 195.234 210.991 141.700 1.00 25.29 ? 2765 TYR A CD2   1 
ATOM   10117 C CE1   . TYR A 1 2765 ? 193.156 209.818 143.076 1.00 23.14 ? 2765 TYR A CE1   1 
ATOM   10118 C CE2   . TYR A 1 2765 ? 194.286 210.259 141.016 1.00 21.11 ? 2765 TYR A CE2   1 
ATOM   10119 C CZ    . TYR A 1 2765 ? 193.249 209.675 141.708 1.00 22.24 ? 2765 TYR A CZ    1 
ATOM   10120 O OH    . TYR A 1 2765 ? 192.300 208.945 141.031 1.00 22.59 ? 2765 TYR A OH    1 
ATOM   10121 N N     . ALA A 1 2766 ? 196.913 215.072 145.466 1.00 25.11 ? 2766 ALA A N     1 
ATOM   10122 C CA    . ALA A 1 2766 ? 197.468 215.599 146.709 1.00 18.02 ? 2766 ALA A CA    1 
ATOM   10123 C C     . ALA A 1 2766 ? 196.365 215.957 147.698 1.00 16.91 ? 2766 ALA A C     1 
ATOM   10124 O O     . ALA A 1 2766 ? 196.493 215.710 148.902 1.00 16.78 ? 2766 ALA A O     1 
ATOM   10125 C CB    . ALA A 1 2766 ? 198.345 216.816 146.418 1.00 17.92 ? 2766 ALA A CB    1 
ATOM   10126 N N     . GLU A 1 2767 ? 195.279 216.554 147.207 1.00 21.39 ? 2767 GLU A N     1 
ATOM   10127 C CA    . GLU A 1 2767 ? 194.158 216.906 148.079 1.00 17.24 ? 2767 GLU A CA    1 
ATOM   10128 C C     . GLU A 1 2767 ? 193.515 215.690 148.737 1.00 14.40 ? 2767 GLU A C     1 
ATOM   10129 O O     . GLU A 1 2767 ? 193.362 215.695 149.973 1.00 16.34 ? 2767 GLU A O     1 
ATOM   10130 C CB    . GLU A 1 2767 ? 193.135 217.723 147.278 1.00 20.37 ? 2767 GLU A CB    1 
ATOM   10131 C CG    . GLU A 1 2767 ? 191.925 218.201 148.064 1.00 17.70 ? 2767 GLU A CG    1 
ATOM   10132 C CD    . GLU A 1 2767 ? 192.279 219.194 149.151 1.00 24.27 ? 2767 GLU A CD    1 
ATOM   10133 O OE1   . GLU A 1 2767 ? 193.312 219.884 149.017 1.00 26.76 ? 2767 GLU A OE1   1 
ATOM   10134 O OE2   . GLU A 1 2767 ? 191.520 219.287 150.139 1.00 25.78 ? 2767 GLU A OE2   1 
ATOM   10135 N N     . PRO A 1 2768 ? 193.124 214.633 148.013 1.00 14.74 ? 2768 PRO A N     1 
ATOM   10136 C CA    . PRO A 1 2768 ? 192.527 213.479 148.703 1.00 14.10 ? 2768 PRO A CA    1 
ATOM   10137 C C     . PRO A 1 2768 ? 193.517 212.727 149.570 1.00 17.70 ? 2768 PRO A C     1 
ATOM   10138 O O     . PRO A 1 2768 ? 193.113 212.114 150.563 1.00 19.43 ? 2768 PRO A O     1 
ATOM   10139 C CB    . PRO A 1 2768 ? 192.006 212.612 147.550 1.00 13.17 ? 2768 PRO A CB    1 
ATOM   10140 C CG    . PRO A 1 2768 ? 192.871 212.961 146.411 1.00 17.26 ? 2768 PRO A CG    1 
ATOM   10141 C CD    . PRO A 1 2768 ? 193.164 214.421 146.554 1.00 19.74 ? 2768 PRO A CD    1 
ATOM   10142 N N     . LEU A 1 2769 ? 194.807 212.766 149.232 1.00 19.93 ? 2769 LEU A N     1 
ATOM   10143 C CA    . LEU A 1 2769 ? 195.815 212.131 150.075 1.00 12.66 ? 2769 LEU A CA    1 
ATOM   10144 C C     . LEU A 1 2769 ? 195.849 212.772 151.455 1.00 10.02 ? 2769 LEU A C     1 
ATOM   10145 O O     . LEU A 1 2769 ? 195.791 212.081 152.479 1.00 9.87  ? 2769 LEU A O     1 
ATOM   10146 C CB    . LEU A 1 2769 ? 197.186 212.226 149.407 1.00 12.71 ? 2769 LEU A CB    1 
ATOM   10147 C CG    . LEU A 1 2769 ? 198.345 211.546 150.129 1.00 12.51 ? 2769 LEU A CG    1 
ATOM   10148 C CD1   . LEU A 1 2769 ? 198.093 210.054 150.202 1.00 12.13 ? 2769 LEU A CD1   1 
ATOM   10149 C CD2   . LEU A 1 2769 ? 199.665 211.842 149.440 1.00 13.06 ? 2769 LEU A CD2   1 
ATOM   10150 N N     . THR A 1 2770 ? 195.939 214.104 151.497 1.00 15.33 ? 2770 THR A N     1 
ATOM   10151 C CA    . THR A 1 2770 ? 195.913 214.816 152.769 1.00 9.15  ? 2770 THR A CA    1 
ATOM   10152 C C     . THR A 1 2770 ? 194.580 214.625 153.479 1.00 8.80  ? 2770 THR A C     1 
ATOM   10153 O O     . THR A 1 2770 ? 194.541 214.465 154.704 1.00 11.54 ? 2770 THR A O     1 
ATOM   10154 C CB    . THR A 1 2770 ? 196.192 216.301 152.547 1.00 12.01 ? 2770 THR A CB    1 
ATOM   10155 O OG1   . THR A 1 2770 ? 197.406 216.453 151.803 1.00 17.77 ? 2770 THR A OG1   1 
ATOM   10156 C CG2   . THR A 1 2770 ? 196.337 217.020 153.875 1.00 8.30  ? 2770 THR A CG2   1 
ATOM   10157 N N     . ALA A 1 2771 ? 193.474 214.648 152.729 1.00 11.04 ? 2771 ALA A N     1 
ATOM   10158 C CA    . ALA A 1 2771 ? 192.175 214.430 153.354 1.00 9.85  ? 2771 ALA A CA    1 
ATOM   10159 C C     . ALA A 1 2771 ? 192.114 213.079 154.053 1.00 7.10  ? 2771 ALA A C     1 
ATOM   10160 O O     . ALA A 1 2771 ? 191.676 212.999 155.205 1.00 6.14  ? 2771 ALA A O     1 
ATOM   10161 C CB    . ALA A 1 2771 ? 191.063 214.541 152.312 1.00 13.70 ? 2771 ALA A CB    1 
ATOM   10162 N N     . ALA A 1 2772 ? 192.567 212.017 153.384 1.00 13.45 ? 2772 ALA A N     1 
ATOM   10163 C CA    . ALA A 1 2772 ? 192.583 210.687 153.983 1.00 11.58 ? 2772 ALA A CA    1 
ATOM   10164 C C     . ALA A 1 2772 ? 193.532 210.613 155.171 1.00 11.83 ? 2772 ALA A C     1 
ATOM   10165 O O     . ALA A 1 2772 ? 193.191 210.016 156.198 1.00 10.05 ? 2772 ALA A O     1 
ATOM   10166 C CB    . ALA A 1 2772 ? 192.964 209.643 152.934 1.00 10.11 ? 2772 ALA A CB    1 
ATOM   10167 N N     . MET A 1 2773 ? 194.724 211.205 155.050 1.00 12.74 ? 2773 MET A N     1 
ATOM   10168 C CA    . MET A 1 2773 ? 195.668 211.205 156.163 1.00 2.07  ? 2773 MET A CA    1 
ATOM   10169 C C     . MET A 1 2773 ? 195.046 211.827 157.404 1.00 7.16  ? 2773 MET A C     1 
ATOM   10170 O O     . MET A 1 2773 ? 195.034 211.218 158.481 1.00 20.00 ? 2773 MET A O     1 
ATOM   10171 C CB    . MET A 1 2773 ? 196.940 211.960 155.777 1.00 0.04  ? 2773 MET A CB    1 
ATOM   10172 C CG    . MET A 1 2773 ? 198.000 211.105 155.124 1.00 4.58  ? 2773 MET A CG    1 
ATOM   10173 S SD    . MET A 1 2773 ? 199.418 212.056 154.566 1.00 7.79  ? 2773 MET A SD    1 
ATOM   10174 C CE    . MET A 1 2773 ? 200.259 212.307 156.120 1.00 11.99 ? 2773 MET A CE    1 
ATOM   10175 N N     . VAL A 1 2774 ? 194.500 213.036 157.264 1.00 9.83  ? 2774 VAL A N     1 
ATOM   10176 C CA    . VAL A 1 2774 ? 193.932 213.729 158.415 1.00 5.78  ? 2774 VAL A CA    1 
ATOM   10177 C C     . VAL A 1 2774 ? 192.709 212.994 158.944 1.00 5.90  ? 2774 VAL A C     1 
ATOM   10178 O O     . VAL A 1 2774 ? 192.521 212.887 160.159 1.00 8.77  ? 2774 VAL A O     1 
ATOM   10179 C CB    . VAL A 1 2774 ? 193.611 215.192 158.066 1.00 8.53  ? 2774 VAL A CB    1 
ATOM   10180 C CG1   . VAL A 1 2774 ? 193.238 215.954 159.320 1.00 15.42 ? 2774 VAL A CG1   1 
ATOM   10181 C CG2   . VAL A 1 2774 ? 194.817 215.848 157.428 1.00 9.70  ? 2774 VAL A CG2   1 
ATOM   10182 N N     . GLU A 1 2775 ? 191.852 212.482 158.057 1.00 10.80 ? 2775 GLU A N     1 
ATOM   10183 C CA    . GLU A 1 2775 ? 190.634 211.834 158.528 1.00 7.61  ? 2775 GLU A CA    1 
ATOM   10184 C C     . GLU A 1 2775 ? 190.950 210.552 159.287 1.00 11.43 ? 2775 GLU A C     1 
ATOM   10185 O O     . GLU A 1 2775 ? 190.383 210.302 160.358 1.00 18.17 ? 2775 GLU A O     1 
ATOM   10186 C CB    . GLU A 1 2775 ? 189.695 211.567 157.353 1.00 10.88 ? 2775 GLU A CB    1 
ATOM   10187 C CG    . GLU A 1 2775 ? 188.240 211.393 157.760 1.00 13.77 ? 2775 GLU A CG    1 
ATOM   10188 C CD    . GLU A 1 2775 ? 187.850 209.947 157.952 1.00 18.37 ? 2775 GLU A CD    1 
ATOM   10189 O OE1   . GLU A 1 2775 ? 188.125 209.142 157.042 1.00 18.27 ? 2775 GLU A OE1   1 
ATOM   10190 O OE2   . GLU A 1 2775 ? 187.271 209.615 159.006 1.00 14.86 ? 2775 GLU A OE2   1 
ATOM   10191 N N     . PHE A 1 2776 ? 191.875 209.739 158.768 1.00 10.66 ? 2776 PHE A N     1 
ATOM   10192 C CA    . PHE A 1 2776 ? 192.296 208.542 159.489 1.00 10.64 ? 2776 PHE A CA    1 
ATOM   10193 C C     . PHE A 1 2776 ? 192.973 208.892 160.808 1.00 13.71 ? 2776 PHE A C     1 
ATOM   10194 O O     . PHE A 1 2776 ? 192.731 208.233 161.827 1.00 19.79 ? 2776 PHE A O     1 
ATOM   10195 C CB    . PHE A 1 2776 ? 193.229 207.702 158.619 1.00 13.82 ? 2776 PHE A CB    1 
ATOM   10196 C CG    . PHE A 1 2776 ? 193.695 206.439 159.282 1.00 14.50 ? 2776 PHE A CG    1 
ATOM   10197 C CD1   . PHE A 1 2776 ? 192.806 205.413 159.553 1.00 16.23 ? 2776 PHE A CD1   1 
ATOM   10198 C CD2   . PHE A 1 2776 ? 195.022 206.281 159.645 1.00 7.30  ? 2776 PHE A CD2   1 
ATOM   10199 C CE1   . PHE A 1 2776 ? 193.232 204.254 160.169 1.00 16.10 ? 2776 PHE A CE1   1 
ATOM   10200 C CE2   . PHE A 1 2776 ? 195.453 205.125 160.261 1.00 7.84  ? 2776 PHE A CE2   1 
ATOM   10201 C CZ    . PHE A 1 2776 ? 194.558 204.110 160.522 1.00 14.58 ? 2776 PHE A CZ    1 
ATOM   10202 N N     . TYR A 1 2777 ? 193.833 209.916 160.811 1.00 8.64  ? 2777 TYR A N     1 
ATOM   10203 C CA    . TYR A 1 2777 ? 194.519 210.295 162.040 1.00 4.89  ? 2777 TYR A CA    1 
ATOM   10204 C C     . TYR A 1 2777 ? 193.535 210.759 163.105 1.00 13.09 ? 2777 TYR A C     1 
ATOM   10205 O O     . TYR A 1 2777 ? 193.643 210.367 164.271 1.00 15.63 ? 2777 TYR A O     1 
ATOM   10206 C CB    . TYR A 1 2777 ? 195.550 211.381 161.742 1.00 5.42  ? 2777 TYR A CB    1 
ATOM   10207 C CG    . TYR A 1 2777 ? 196.026 212.142 162.957 1.00 15.83 ? 2777 TYR A CG    1 
ATOM   10208 C CD1   . TYR A 1 2777 ? 196.902 211.564 163.865 1.00 17.00 ? 2777 TYR A CD1   1 
ATOM   10209 C CD2   . TYR A 1 2777 ? 195.610 213.445 163.190 1.00 11.27 ? 2777 TYR A CD2   1 
ATOM   10210 C CE1   . TYR A 1 2777 ? 197.341 212.257 164.975 1.00 9.26  ? 2777 TYR A CE1   1 
ATOM   10211 C CE2   . TYR A 1 2777 ? 196.044 214.146 164.296 1.00 12.89 ? 2777 TYR A CE2   1 
ATOM   10212 C CZ    . TYR A 1 2777 ? 196.910 213.547 165.184 1.00 13.97 ? 2777 TYR A CZ    1 
ATOM   10213 O OH    . TYR A 1 2777 ? 197.343 214.244 166.288 1.00 17.38 ? 2777 TYR A OH    1 
ATOM   10214 N N     . THR A 1 2778 ? 192.552 211.577 162.724 1.00 19.16 ? 2778 THR A N     1 
ATOM   10215 C CA    . THR A 1 2778 ? 191.545 212.009 163.688 1.00 17.31 ? 2778 THR A CA    1 
ATOM   10216 C C     . THR A 1 2778 ? 190.689 210.839 164.159 1.00 18.73 ? 2778 THR A C     1 
ATOM   10217 O O     . THR A 1 2778 ? 190.347 210.752 165.344 1.00 18.52 ? 2778 THR A O     1 
ATOM   10218 C CB    . THR A 1 2778 ? 190.665 213.109 163.091 1.00 15.05 ? 2778 THR A CB    1 
ATOM   10219 O OG1   . THR A 1 2778 ? 189.977 212.609 161.938 1.00 14.98 ? 2778 THR A OG1   1 
ATOM   10220 C CG2   . THR A 1 2778 ? 191.500 214.323 162.713 1.00 16.55 ? 2778 THR A CG2   1 
ATOM   10221 N N     . MET A 1 2779 ? 190.332 209.929 163.248 1.00 19.52 ? 2779 MET A N     1 
ATOM   10222 C CA    . MET A 1 2779 ? 189.520 208.781 163.638 1.00 19.66 ? 2779 MET A CA    1 
ATOM   10223 C C     . MET A 1 2779 ? 190.254 207.903 164.642 1.00 21.61 ? 2779 MET A C     1 
ATOM   10224 O O     . MET A 1 2779 ? 189.651 207.399 165.596 1.00 27.57 ? 2779 MET A O     1 
ATOM   10225 C CB    . MET A 1 2779 ? 189.129 207.973 162.402 1.00 18.72 ? 2779 MET A CB    1 
ATOM   10226 C CG    . MET A 1 2779 ? 187.909 207.092 162.598 1.00 22.06 ? 2779 MET A CG    1 
ATOM   10227 S SD    . MET A 1 2779 ? 187.416 206.269 161.075 1.00 38.07 ? 2779 MET A SD    1 
ATOM   10228 C CE    . MET A 1 2779 ? 189.019 205.903 160.369 1.00 26.51 ? 2779 MET A CE    1 
ATOM   10229 N N     . SER A 1 2780 ? 191.558 207.704 164.441 1.00 17.63 ? 2780 SER A N     1 
ATOM   10230 C CA    . SER A 1 2780 ? 192.343 206.935 165.401 1.00 16.05 ? 2780 SER A CA    1 
ATOM   10231 C C     . SER A 1 2780 ? 192.672 207.753 166.644 1.00 19.41 ? 2780 SER A C     1 
ATOM   10232 O O     . SER A 1 2780 ? 193.108 207.192 167.654 1.00 20.65 ? 2780 SER A O     1 
ATOM   10233 C CB    . SER A 1 2780 ? 193.624 206.429 164.745 1.00 17.64 ? 2780 SER A CB    1 
ATOM   10234 O OG    . SER A 1 2780 ? 194.344 205.580 165.620 1.00 17.44 ? 2780 SER A OG    1 
ATOM   10235 N N     . GLN A 1 2781 ? 192.511 209.076 166.576 1.00 28.17 ? 2781 GLN A N     1 
ATOM   10236 C CA    . GLN A 1 2781 ? 192.668 209.909 167.764 1.00 19.69 ? 2781 GLN A CA    1 
ATOM   10237 C C     . GLN A 1 2781 ? 191.443 209.827 168.668 1.00 18.72 ? 2781 GLN A C     1 
ATOM   10238 O O     . GLN A 1 2781 ? 191.572 209.838 169.897 1.00 17.64 ? 2781 GLN A O     1 
ATOM   10239 C CB    . GLN A 1 2781 ? 192.933 211.356 167.347 1.00 23.04 ? 2781 GLN A CB    1 
ATOM   10240 C CG    . GLN A 1 2781 ? 193.256 212.306 168.489 1.00 22.89 ? 2781 GLN A CG    1 
ATOM   10241 C CD    . GLN A 1 2781 ? 194.722 212.294 168.871 1.00 22.96 ? 2781 GLN A CD    1 
ATOM   10242 O OE1   . GLN A 1 2781 ? 195.108 211.707 169.881 1.00 23.21 ? 2781 GLN A OE1   1 
ATOM   10243 N NE2   . GLN A 1 2781 ? 195.547 212.952 168.067 1.00 18.77 ? 2781 GLN A NE2   1 
ATOM   10244 N N     . GLU A 1 2782 ? 190.247 209.751 168.076 1.00 27.91 ? 2782 GLU A N     1 
ATOM   10245 C CA    . GLU A 1 2782 ? 189.022 209.783 168.871 1.00 33.56 ? 2782 GLU A CA    1 
ATOM   10246 C C     . GLU A 1 2782 ? 188.931 208.589 169.811 1.00 32.29 ? 2782 GLU A C     1 
ATOM   10247 O O     . GLU A 1 2782 ? 188.604 208.743 170.994 1.00 34.81 ? 2782 GLU A O     1 
ATOM   10248 C CB    . GLU A 1 2782 ? 187.798 209.835 167.956 1.00 29.87 ? 2782 GLU A CB    1 
ATOM   10249 C CG    . GLU A 1 2782 ? 187.760 211.040 167.036 1.00 30.40 ? 2782 GLU A CG    1 
ATOM   10250 C CD    . GLU A 1 2782 ? 186.978 210.778 165.765 1.00 34.90 ? 2782 GLU A CD    1 
ATOM   10251 O OE1   . GLU A 1 2782 ? 186.250 209.765 165.711 1.00 34.02 ? 2782 GLU A OE1   1 
ATOM   10252 O OE2   . GLU A 1 2782 ? 187.096 211.583 164.818 1.00 34.19 ? 2782 GLU A OE2   1 
ATOM   10253 N N     . ARG A 1 2783 ? 189.215 207.394 169.310 1.00 26.33 ? 2783 ARG A N     1 
ATOM   10254 C CA    . ARG A 1 2783 ? 189.229 206.190 170.123 1.00 31.53 ? 2783 ARG A CA    1 
ATOM   10255 C C     . ARG A 1 2783 ? 190.650 205.647 170.207 1.00 30.97 ? 2783 ARG A C     1 
ATOM   10256 O O     . ARG A 1 2783 ? 191.562 206.130 169.535 1.00 33.02 ? 2783 ARG A O     1 
ATOM   10257 C CB    . ARG A 1 2783 ? 188.259 205.143 169.562 1.00 32.05 ? 2783 ARG A CB    1 
ATOM   10258 C CG    . ARG A 1 2783 ? 188.870 204.128 168.616 1.00 29.01 ? 2783 ARG A CG    1 
ATOM   10259 C CD    . ARG A 1 2783 ? 187.804 203.160 168.129 1.00 32.29 ? 2783 ARG A CD    1 
ATOM   10260 N NE    . ARG A 1 2783 ? 187.506 202.130 169.116 1.00 35.03 ? 2783 ARG A NE    1 
ATOM   10261 C CZ    . ARG A 1 2783 ? 186.768 201.056 168.877 1.00 32.24 ? 2783 ARG A CZ    1 
ATOM   10262 N NH1   . ARG A 1 2783 ? 186.215 200.846 167.694 1.00 30.40 ? 2783 ARG A NH1   1 
ATOM   10263 N NH2   . ARG A 1 2783 ? 186.576 200.170 169.850 1.00 31.01 ? 2783 ARG A NH2   1 
ATOM   10264 N N     . PHE A 1 2784 ? 190.830 204.640 171.063 1.00 27.62 ? 2784 PHE A N     1 
ATOM   10265 C CA    . PHE A 1 2784 ? 192.144 204.068 171.357 1.00 27.12 ? 2784 PHE A CA    1 
ATOM   10266 C C     . PHE A 1 2784 ? 193.058 205.135 171.964 1.00 24.71 ? 2784 PHE A C     1 
ATOM   10267 O O     . PHE A 1 2784 ? 194.201 205.335 171.548 1.00 21.20 ? 2784 PHE A O     1 
ATOM   10268 C CB    . PHE A 1 2784 ? 192.778 203.441 170.108 1.00 25.47 ? 2784 PHE A CB    1 
ATOM   10269 C CG    . PHE A 1 2784 ? 192.050 202.229 169.591 1.00 29.11 ? 2784 PHE A CG    1 
ATOM   10270 C CD1   . PHE A 1 2784 ? 190.906 201.758 170.219 1.00 28.74 ? 2784 PHE A CD1   1 
ATOM   10271 C CD2   . PHE A 1 2784 ? 192.502 201.572 168.462 1.00 27.28 ? 2784 PHE A CD2   1 
ATOM   10272 C CE1   . PHE A 1 2784 ? 190.237 200.652 169.737 1.00 27.65 ? 2784 PHE A CE1   1 
ATOM   10273 C CE2   . PHE A 1 2784 ? 191.837 200.467 167.978 1.00 29.12 ? 2784 PHE A CE2   1 
ATOM   10274 C CZ    . PHE A 1 2784 ? 190.700 200.009 168.613 1.00 30.02 ? 2784 PHE A CZ    1 
ATOM   10275 N N     . THR A 1 2785 ? 192.519 205.826 172.962 1.00 25.07 ? 2785 THR A N     1 
ATOM   10276 C CA    . THR A 1 2785 ? 193.211 206.920 173.623 1.00 26.51 ? 2785 THR A CA    1 
ATOM   10277 C C     . THR A 1 2785 ? 194.113 206.375 174.730 1.00 23.39 ? 2785 THR A C     1 
ATOM   10278 O O     . THR A 1 2785 ? 194.359 205.171 174.832 1.00 20.21 ? 2785 THR A O     1 
ATOM   10279 C CB    . THR A 1 2785 ? 192.201 207.930 174.162 1.00 27.97 ? 2785 THR A CB    1 
ATOM   10280 O OG1   . THR A 1 2785 ? 191.310 207.277 175.074 1.00 25.69 ? 2785 THR A OG1   1 
ATOM   10281 C CG2   . THR A 1 2785 ? 191.396 208.533 173.023 1.00 26.16 ? 2785 THR A CG2   1 
ATOM   10282 N N     . GLN A 1 2786 ? 194.622 207.273 175.575 1.00 22.04 ? 2786 GLN A N     1 
ATOM   10283 C CA    . GLN A 1 2786 ? 195.535 206.893 176.645 1.00 22.69 ? 2786 GLN A CA    1 
ATOM   10284 C C     . GLN A 1 2786 ? 194.838 206.153 177.781 1.00 28.07 ? 2786 GLN A C     1 
ATOM   10285 O O     . GLN A 1 2786 ? 195.521 205.590 178.643 1.00 26.13 ? 2786 GLN A O     1 
ATOM   10286 C CB    . GLN A 1 2786 ? 196.242 208.143 177.177 1.00 21.98 ? 2786 GLN A CB    1 
ATOM   10287 C CG    . GLN A 1 2786 ? 197.452 207.871 178.055 1.00 23.13 ? 2786 GLN A CG    1 
ATOM   10288 C CD    . GLN A 1 2786 ? 198.559 208.884 177.849 1.00 23.03 ? 2786 GLN A CD    1 
ATOM   10289 O OE1   . GLN A 1 2786 ? 198.433 209.803 177.040 1.00 24.55 ? 2786 GLN A OE1   1 
ATOM   10290 N NE2   . GLN A 1 2786 ? 199.653 208.723 178.584 1.00 23.38 ? 2786 GLN A NE2   1 
ATOM   10291 N N     . ASP A 1 2787 ? 193.503 206.132 177.802 1.00 29.47 ? 2787 ASP A N     1 
ATOM   10292 C CA    . ASP A 1 2787 ? 192.795 205.427 178.866 1.00 25.71 ? 2787 ASP A CA    1 
ATOM   10293 C C     . ASP A 1 2787 ? 193.063 203.927 178.815 1.00 25.45 ? 2787 ASP A C     1 
ATOM   10294 O O     . ASP A 1 2787 ? 193.235 203.285 179.858 1.00 27.50 ? 2787 ASP A O     1 
ATOM   10295 C CB    . ASP A 1 2787 ? 191.295 205.711 178.777 1.00 27.63 ? 2787 ASP A CB    1 
ATOM   10296 C CG    . ASP A 1 2787 ? 190.713 205.367 177.420 1.00 32.48 ? 2787 ASP A CG    1 
ATOM   10297 O OD1   . ASP A 1 2787 ? 191.451 205.451 176.416 1.00 27.36 ? 2787 ASP A OD1   1 
ATOM   10298 O OD2   . ASP A 1 2787 ? 189.517 205.013 177.357 1.00 37.33 ? 2787 ASP A OD2   1 
ATOM   10299 N N     . THR A 1 2788 ? 193.101 203.350 177.612 1.00 23.19 ? 2788 THR A N     1 
ATOM   10300 C CA    . THR A 1 2788 ? 193.301 201.909 177.492 1.00 25.34 ? 2788 THR A CA    1 
ATOM   10301 C C     . THR A 1 2788 ? 194.756 201.528 177.744 1.00 21.13 ? 2788 THR A C     1 
ATOM   10302 O O     . THR A 1 2788 ? 195.041 200.629 178.544 1.00 15.45 ? 2788 THR A O     1 
ATOM   10303 C CB    . THR A 1 2788 ? 192.849 201.429 176.112 1.00 24.89 ? 2788 THR A CB    1 
ATOM   10304 O OG1   . THR A 1 2788 ? 193.599 202.107 175.099 1.00 26.16 ? 2788 THR A OG1   1 
ATOM   10305 C CG2   . THR A 1 2788 ? 191.369 201.713 175.912 1.00 24.27 ? 2788 THR A CG2   1 
ATOM   10306 N N     . GLN A 1 2789 ? 195.688 202.197 177.075 1.00 19.73 ? 2789 GLN A N     1 
ATOM   10307 C CA    . GLN A 1 2789 ? 197.109 201.929 177.229 1.00 19.08 ? 2789 GLN A CA    1 
ATOM   10308 C C     . GLN A 1 2789 ? 197.848 203.244 177.417 1.00 18.93 ? 2789 GLN A C     1 
ATOM   10309 O O     . GLN A 1 2789 ? 197.440 204.271 176.864 1.00 18.97 ? 2789 GLN A O     1 
ATOM   10310 C CB    . GLN A 1 2789 ? 197.683 201.184 176.013 1.00 19.45 ? 2789 GLN A CB    1 
ATOM   10311 C CG    . GLN A 1 2789 ? 197.163 199.766 175.842 1.00 23.73 ? 2789 GLN A CG    1 
ATOM   10312 C CD    . GLN A 1 2789 ? 197.533 198.862 176.999 1.00 22.72 ? 2789 GLN A CD    1 
ATOM   10313 O OE1   . GLN A 1 2789 ? 198.674 198.858 177.460 1.00 19.77 ? 2789 GLN A OE1   1 
ATOM   10314 N NE2   . GLN A 1 2789 ? 196.566 198.087 177.475 1.00 22.53 ? 2789 GLN A NE2   1 
ATOM   10315 N N     . PRO A 1 2790 ? 198.943 203.242 178.177 1.00 19.01 ? 2790 PRO A N     1 
ATOM   10316 C CA    . PRO A 1 2790 ? 199.662 204.487 178.462 1.00 18.88 ? 2790 PRO A CA    1 
ATOM   10317 C C     . PRO A 1 2790 ? 200.546 204.989 177.330 1.00 20.48 ? 2790 PRO A C     1 
ATOM   10318 O O     . PRO A 1 2790 ? 201.158 206.050 177.479 1.00 20.57 ? 2790 PRO A O     1 
ATOM   10319 C CB    . PRO A 1 2790 ? 200.514 204.105 179.681 1.00 18.92 ? 2790 PRO A CB    1 
ATOM   10320 C CG    . PRO A 1 2790 ? 200.789 202.663 179.490 1.00 20.16 ? 2790 PRO A CG    1 
ATOM   10321 C CD    . PRO A 1 2790 ? 199.552 202.085 178.857 1.00 19.82 ? 2790 PRO A CD    1 
ATOM   10322 N N     . HIS A 1 2791 ? 200.637 204.270 176.212 1.00 16.27 ? 2791 HIS A N     1 
ATOM   10323 C CA    . HIS A 1 2791 ? 201.496 204.673 175.107 1.00 12.08 ? 2791 HIS A CA    1 
ATOM   10324 C C     . HIS A 1 2791 ? 200.702 205.088 173.876 1.00 16.36 ? 2791 HIS A C     1 
ATOM   10325 O O     . HIS A 1 2791 ? 201.300 205.348 172.825 1.00 20.83 ? 2791 HIS A O     1 
ATOM   10326 C CB    . HIS A 1 2791 ? 202.463 203.543 174.745 1.00 11.93 ? 2791 HIS A CB    1 
ATOM   10327 C CG    . HIS A 1 2791 ? 201.791 202.228 174.503 1.00 13.57 ? 2791 HIS A CG    1 
ATOM   10328 N ND1   . HIS A 1 2791 ? 201.757 201.223 175.445 1.00 18.57 ? 2791 HIS A ND1   1 
ATOM   10329 C CD2   . HIS A 1 2791 ? 201.140 201.748 173.418 1.00 12.76 ? 2791 HIS A CD2   1 
ATOM   10330 C CE1   . HIS A 1 2791 ? 201.104 200.185 174.955 1.00 18.37 ? 2791 HIS A CE1   1 
ATOM   10331 N NE2   . HIS A 1 2791 ? 200.720 200.477 173.726 1.00 14.98 ? 2791 HIS A NE2   1 
ATOM   10332 N N     . TYR A 1 2792 ? 199.376 205.158 173.974 1.00 17.52 ? 2792 TYR A N     1 
ATOM   10333 C CA    . TYR A 1 2792 ? 198.537 205.558 172.845 1.00 13.12 ? 2792 TYR A CA    1 
ATOM   10334 C C     . TYR A 1 2792 ? 198.508 207.083 172.746 1.00 16.26 ? 2792 TYR A C     1 
ATOM   10335 O O     . TYR A 1 2792 ? 197.520 207.751 173.052 1.00 20.42 ? 2792 TYR A O     1 
ATOM   10336 C CB    . TYR A 1 2792 ? 197.137 204.975 172.989 1.00 15.68 ? 2792 TYR A CB    1 
ATOM   10337 C CG    . TYR A 1 2792 ? 197.065 203.478 172.799 1.00 16.46 ? 2792 TYR A CG    1 
ATOM   10338 C CD1   . TYR A 1 2792 ? 198.123 202.774 172.240 1.00 13.35 ? 2792 TYR A CD1   1 
ATOM   10339 C CD2   . TYR A 1 2792 ? 195.933 202.769 173.171 1.00 18.30 ? 2792 TYR A CD2   1 
ATOM   10340 C CE1   . TYR A 1 2792 ? 198.056 201.406 172.063 1.00 12.69 ? 2792 TYR A CE1   1 
ATOM   10341 C CE2   . TYR A 1 2792 ? 195.857 201.403 172.998 1.00 17.97 ? 2792 TYR A CE2   1 
ATOM   10342 C CZ    . TYR A 1 2792 ? 196.920 200.726 172.445 1.00 13.62 ? 2792 TYR A CZ    1 
ATOM   10343 O OH    . TYR A 1 2792 ? 196.843 199.365 172.274 1.00 14.28 ? 2792 TYR A OH    1 
ATOM   10344 N N     . ILE A 1 2793 ? 199.633 207.628 172.299 1.00 12.60 ? 2793 ILE A N     1 
ATOM   10345 C CA    . ILE A 1 2793 ? 199.805 209.065 172.127 1.00 15.31 ? 2793 ILE A CA    1 
ATOM   10346 C C     . ILE A 1 2793 ? 199.786 209.346 170.631 1.00 15.29 ? 2793 ILE A C     1 
ATOM   10347 O O     . ILE A 1 2793 ? 200.649 208.869 169.887 1.00 17.84 ? 2793 ILE A O     1 
ATOM   10348 C CB    . ILE A 1 2793 ? 201.104 209.560 172.776 1.00 15.23 ? 2793 ILE A CB    1 
ATOM   10349 C CG1   . ILE A 1 2793 ? 200.924 209.693 174.287 1.00 11.93 ? 2793 ILE A CG1   1 
ATOM   10350 C CG2   . ILE A 1 2793 ? 201.526 210.897 172.184 1.00 14.88 ? 2793 ILE A CG2   1 
ATOM   10351 C CD1   . ILE A 1 2793 ? 202.221 209.689 175.054 1.00 13.81 ? 2793 ILE A CD1   1 
ATOM   10352 N N     . TYR A 1 2794 ? 198.798 210.116 170.186 1.00 10.98 ? 2794 TYR A N     1 
ATOM   10353 C CA    . TYR A 1 2794 ? 198.632 210.464 168.780 1.00 11.47 ? 2794 TYR A CA    1 
ATOM   10354 C C     . TYR A 1 2794 ? 198.780 211.974 168.651 1.00 16.18 ? 2794 TYR A C     1 
ATOM   10355 O O     . TYR A 1 2794 ? 197.937 212.730 169.147 1.00 16.63 ? 2794 TYR A O     1 
ATOM   10356 C CB    . TYR A 1 2794 ? 197.277 209.996 168.260 1.00 16.78 ? 2794 TYR A CB    1 
ATOM   10357 C CG    . TYR A 1 2794 ? 197.084 208.499 168.300 1.00 17.19 ? 2794 TYR A CG    1 
ATOM   10358 C CD1   . TYR A 1 2794 ? 197.905 207.651 167.570 1.00 13.47 ? 2794 TYR A CD1   1 
ATOM   10359 C CD2   . TYR A 1 2794 ? 196.077 207.933 169.069 1.00 16.08 ? 2794 TYR A CD2   1 
ATOM   10360 C CE1   . TYR A 1 2794 ? 197.727 206.283 167.606 1.00 12.81 ? 2794 TYR A CE1   1 
ATOM   10361 C CE2   . TYR A 1 2794 ? 195.893 206.567 169.111 1.00 18.94 ? 2794 TYR A CE2   1 
ATOM   10362 C CZ    . TYR A 1 2794 ? 196.720 205.747 168.378 1.00 17.93 ? 2794 TYR A CZ    1 
ATOM   10363 O OH    . TYR A 1 2794 ? 196.538 204.385 168.417 1.00 14.07 ? 2794 TYR A OH    1 
ATOM   10364 N N     . SER A 1 2795 ? 199.838 212.407 167.983 1.00 13.96 ? 2795 SER A N     1 
ATOM   10365 C CA    . SER A 1 2795 ? 200.199 213.809 167.842 1.00 8.42  ? 2795 SER A CA    1 
ATOM   10366 C C     . SER A 1 2795 ? 200.523 214.104 166.390 1.00 7.93  ? 2795 SER A C     1 
ATOM   10367 O O     . SER A 1 2795 ? 200.746 213.187 165.593 1.00 16.04 ? 2795 SER A O     1 
ATOM   10368 C CB    . SER A 1 2795 ? 201.405 214.147 168.733 1.00 9.83  ? 2795 SER A CB    1 
ATOM   10369 O OG    . SER A 1 2795 ? 202.514 213.324 168.422 1.00 6.01  ? 2795 SER A OG    1 
ATOM   10370 N N     . PRO A 1 2796 ? 200.539 215.382 166.001 1.00 7.89  ? 2796 PRO A N     1 
ATOM   10371 C CA    . PRO A 1 2796 ? 201.002 215.726 164.646 1.00 5.42  ? 2796 PRO A CA    1 
ATOM   10372 C C     . PRO A 1 2796 ? 202.407 215.238 164.329 1.00 4.68  ? 2796 PRO A C     1 
ATOM   10373 O O     . PRO A 1 2796 ? 202.817 215.302 163.164 1.00 8.45  ? 2796 PRO A O     1 
ATOM   10374 C CB    . PRO A 1 2796 ? 200.921 217.257 164.633 1.00 7.97  ? 2796 PRO A CB    1 
ATOM   10375 C CG    . PRO A 1 2796 ? 199.825 217.563 165.589 1.00 6.69  ? 2796 PRO A CG    1 
ATOM   10376 C CD    . PRO A 1 2796 ? 199.942 216.543 166.685 1.00 8.32  ? 2796 PRO A CD    1 
ATOM   10377 N N     . ARG A 1 2797 ? 203.161 214.760 165.321 1.00 5.40  ? 2797 ARG A N     1 
ATOM   10378 C CA    . ARG A 1 2797 ? 204.430 214.100 165.032 1.00 7.76  ? 2797 ARG A CA    1 
ATOM   10379 C C     . ARG A 1 2797 ? 204.212 212.830 164.220 1.00 6.76  ? 2797 ARG A C     1 
ATOM   10380 O O     . ARG A 1 2797 ? 205.035 212.482 163.365 1.00 8.84  ? 2797 ARG A O     1 
ATOM   10381 C CB    . ARG A 1 2797 ? 205.169 213.790 166.333 1.00 6.11  ? 2797 ARG A CB    1 
ATOM   10382 C CG    . ARG A 1 2797 ? 205.653 215.021 167.072 1.00 8.47  ? 2797 ARG A CG    1 
ATOM   10383 C CD    . ARG A 1 2797 ? 206.330 214.659 168.379 1.00 7.36  ? 2797 ARG A CD    1 
ATOM   10384 N NE    . ARG A 1 2797 ? 205.418 213.959 169.275 1.00 16.94 ? 2797 ARG A NE    1 
ATOM   10385 C CZ    . ARG A 1 2797 ? 205.707 213.617 170.522 1.00 16.50 ? 2797 ARG A CZ    1 
ATOM   10386 N NH1   . ARG A 1 2797 ? 206.874 213.916 171.068 1.00 14.43 ? 2797 ARG A NH1   1 
ATOM   10387 N NH2   . ARG A 1 2797 ? 204.800 212.962 171.242 1.00 11.60 ? 2797 ARG A NH2   1 
ATOM   10388 N N     . GLU A 1 2798 ? 203.109 212.123 164.473 1.00 6.43  ? 2798 GLU A N     1 
ATOM   10389 C CA    . GLU A 1 2798 ? 202.771 210.966 163.650 1.00 2.33  ? 2798 GLU A CA    1 
ATOM   10390 C C     . GLU A 1 2798 ? 202.504 211.385 162.210 1.00 11.99 ? 2798 GLU A C     1 
ATOM   10391 O O     . GLU A 1 2798 ? 202.922 210.705 161.269 1.00 17.56 ? 2798 GLU A O     1 
ATOM   10392 C CB    . GLU A 1 2798 ? 201.563 210.232 164.236 1.00 3.40  ? 2798 GLU A CB    1 
ATOM   10393 C CG    . GLU A 1 2798 ? 201.542 210.154 165.759 1.00 8.66  ? 2798 GLU A CG    1 
ATOM   10394 C CD    . GLU A 1 2798 ? 202.681 209.336 166.346 1.00 16.03 ? 2798 GLU A CD    1 
ATOM   10395 O OE1   . GLU A 1 2798 ? 203.398 208.647 165.589 1.00 19.59 ? 2798 GLU A OE1   1 
ATOM   10396 O OE2   . GLU A 1 2798 ? 202.865 209.392 167.579 1.00 12.04 ? 2798 GLU A OE2   1 
ATOM   10397 N N     . MET A 1 2799 ? 201.811 212.511 162.020 1.00 8.90  ? 2799 MET A N     1 
ATOM   10398 C CA    . MET A 1 2799 ? 201.597 213.037 160.674 1.00 4.45  ? 2799 MET A CA    1 
ATOM   10399 C C     . MET A 1 2799 ? 202.915 213.401 160.004 1.00 3.28  ? 2799 MET A C     1 
ATOM   10400 O O     . MET A 1 2799 ? 203.109 213.132 158.811 1.00 10.57 ? 2799 MET A O     1 
ATOM   10401 C CB    . MET A 1 2799 ? 200.677 214.253 160.731 1.00 5.13  ? 2799 MET A CB    1 
ATOM   10402 C CG    . MET A 1 2799 ? 199.375 214.017 161.458 1.00 4.73  ? 2799 MET A CG    1 
ATOM   10403 S SD    . MET A 1 2799 ? 198.223 213.098 160.429 1.00 17.21 ? 2799 MET A SD    1 
ATOM   10404 C CE    . MET A 1 2799 ? 198.002 214.242 159.073 1.00 8.99  ? 2799 MET A CE    1 
ATOM   10405 N N     . THR A 1 2800 ? 203.826 214.027 160.750 1.00 0.00  ? 2800 THR A N     1 
ATOM   10406 C CA    . THR A 1 2800 ? 205.124 214.389 160.191 1.00 1.57  ? 2800 THR A CA    1 
ATOM   10407 C C     . THR A 1 2800 ? 205.905 213.150 159.773 1.00 8.61  ? 2800 THR A C     1 
ATOM   10408 O O     . THR A 1 2800 ? 206.514 213.118 158.698 1.00 13.56 ? 2800 THR A O     1 
ATOM   10409 C CB    . THR A 1 2800 ? 205.919 215.211 161.204 1.00 7.29  ? 2800 THR A CB    1 
ATOM   10410 O OG1   . THR A 1 2800 ? 205.188 216.397 161.535 1.00 18.40 ? 2800 THR A OG1   1 
ATOM   10411 C CG2   . THR A 1 2800 ? 207.274 215.596 160.635 1.00 9.17  ? 2800 THR A CG2   1 
ATOM   10412 N N     . ARG A 1 2801 ? 205.898 212.115 160.617 1.00 7.54  ? 2801 ARG A N     1 
ATOM   10413 C CA    . ARG A 1 2801 ? 206.582 210.873 160.270 1.00 5.04  ? 2801 ARG A CA    1 
ATOM   10414 C C     . ARG A 1 2801 ? 205.919 210.197 159.079 1.00 6.09  ? 2801 ARG A C     1 
ATOM   10415 O O     . ARG A 1 2801 ? 206.596 209.590 158.244 1.00 9.54  ? 2801 ARG A O     1 
ATOM   10416 C CB    . ARG A 1 2801 ? 206.614 209.934 161.474 1.00 6.55  ? 2801 ARG A CB    1 
ATOM   10417 C CG    . ARG A 1 2801 ? 207.786 210.168 162.408 1.00 7.50  ? 2801 ARG A CG    1 
ATOM   10418 C CD    . ARG A 1 2801 ? 207.638 209.360 163.686 1.00 12.69 ? 2801 ARG A CD    1 
ATOM   10419 N NE    . ARG A 1 2801 ? 208.043 210.120 164.863 1.00 16.19 ? 2801 ARG A NE    1 
ATOM   10420 C CZ    . ARG A 1 2801 ? 207.318 210.234 165.967 1.00 14.81 ? 2801 ARG A CZ    1 
ATOM   10421 N NH1   . ARG A 1 2801 ? 206.137 209.650 166.082 1.00 3.89  ? 2801 ARG A NH1   1 
ATOM   10422 N NH2   . ARG A 1 2801 ? 207.789 210.954 166.981 1.00 15.98 ? 2801 ARG A NH2   1 
ATOM   10423 N N     . TRP A 1 2802 ? 204.593 210.294 158.984 1.00 4.06  ? 2802 TRP A N     1 
ATOM   10424 C CA    . TRP A 1 2802 ? 203.872 209.749 157.839 1.00 4.10  ? 2802 TRP A CA    1 
ATOM   10425 C C     . TRP A 1 2802 ? 204.327 210.417 156.548 1.00 4.49  ? 2802 TRP A C     1 
ATOM   10426 O O     . TRP A 1 2802 ? 204.638 209.744 155.555 1.00 13.70 ? 2802 TRP A O     1 
ATOM   10427 C CB    . TRP A 1 2802 ? 202.375 209.962 158.057 1.00 2.27  ? 2802 TRP A CB    1 
ATOM   10428 C CG    . TRP A 1 2802 ? 201.472 209.092 157.263 1.00 0.00  ? 2802 TRP A CG    1 
ATOM   10429 C CD1   . TRP A 1 2802 ? 201.751 208.468 156.089 1.00 0.00  ? 2802 TRP A CD1   1 
ATOM   10430 C CD2   . TRP A 1 2802 ? 200.112 208.781 157.572 1.00 0.00  ? 2802 TRP A CD2   1 
ATOM   10431 N NE1   . TRP A 1 2802 ? 200.655 207.764 155.657 1.00 6.85  ? 2802 TRP A NE1   1 
ATOM   10432 C CE2   . TRP A 1 2802 ? 199.633 207.945 156.551 1.00 0.00  ? 2802 TRP A CE2   1 
ATOM   10433 C CE3   . TRP A 1 2802 ? 199.253 209.125 158.619 1.00 4.99  ? 2802 TRP A CE3   1 
ATOM   10434 C CZ2   . TRP A 1 2802 ? 198.336 207.448 156.544 1.00 2.41  ? 2802 TRP A CZ2   1 
ATOM   10435 C CZ3   . TRP A 1 2802 ? 197.966 208.628 158.611 1.00 3.02  ? 2802 TRP A CZ3   1 
ATOM   10436 C CH2   . TRP A 1 2802 ? 197.520 207.798 157.582 1.00 2.28  ? 2802 TRP A CH2   1 
ATOM   10437 N N     . VAL A 1 2803 ? 204.386 211.751 156.557 1.00 4.79  ? 2803 VAL A N     1 
ATOM   10438 C CA    . VAL A 1 2803 ? 204.822 212.496 155.379 1.00 6.00  ? 2803 VAL A CA    1 
ATOM   10439 C C     . VAL A 1 2803 ? 206.268 212.163 155.041 1.00 7.46  ? 2803 VAL A C     1 
ATOM   10440 O O     . VAL A 1 2803 ? 206.617 211.977 153.870 1.00 10.89 ? 2803 VAL A O     1 
ATOM   10441 C CB    . VAL A 1 2803 ? 204.629 214.008 155.596 1.00 8.57  ? 2803 VAL A CB    1 
ATOM   10442 C CG1   . VAL A 1 2803 ? 205.162 214.789 154.408 1.00 5.19  ? 2803 VAL A CG1   1 
ATOM   10443 C CG2   . VAL A 1 2803 ? 203.167 214.326 155.813 1.00 10.94 ? 2803 VAL A CG2   1 
ATOM   10444 N N     . ARG A 1 2804 ? 207.135 212.095 156.055 1.00 5.10  ? 2804 ARG A N     1 
ATOM   10445 C CA    . ARG A 1 2804 ? 208.539 211.783 155.808 1.00 3.72  ? 2804 ARG A CA    1 
ATOM   10446 C C     . ARG A 1 2804 ? 208.704 210.389 155.220 1.00 11.20 ? 2804 ARG A C     1 
ATOM   10447 O O     . ARG A 1 2804 ? 209.508 210.187 154.305 1.00 16.78 ? 2804 ARG A O     1 
ATOM   10448 C CB    . ARG A 1 2804 ? 209.348 211.920 157.096 1.00 3.38  ? 2804 ARG A CB    1 
ATOM   10449 C CG    . ARG A 1 2804 ? 209.637 213.353 157.492 1.00 13.04 ? 2804 ARG A CG    1 
ATOM   10450 C CD    . ARG A 1 2804 ? 210.188 214.141 156.314 1.00 17.92 ? 2804 ARG A CD    1 
ATOM   10451 N NE    . ARG A 1 2804 ? 211.423 213.567 155.792 1.00 21.75 ? 2804 ARG A NE    1 
ATOM   10452 C CZ    . ARG A 1 2804 ? 212.304 214.231 155.057 1.00 15.88 ? 2804 ARG A CZ    1 
ATOM   10453 N NH1   . ARG A 1 2804 ? 212.116 215.499 154.729 1.00 10.65 ? 2804 ARG A NH1   1 
ATOM   10454 N NH2   . ARG A 1 2804 ? 213.400 213.606 154.636 1.00 15.76 ? 2804 ARG A NH2   1 
ATOM   10455 N N     . GLY A 1 2805 ? 207.952 209.412 155.731 1.00 5.92  ? 2805 GLY A N     1 
ATOM   10456 C CA    . GLY A 1 2805 ? 208.034 208.070 155.185 1.00 4.26  ? 2805 GLY A CA    1 
ATOM   10457 C C     . GLY A 1 2805 ? 207.553 207.993 153.750 1.00 10.76 ? 2805 GLY A C     1 
ATOM   10458 O O     . GLY A 1 2805 ? 208.202 207.372 152.901 1.00 19.54 ? 2805 GLY A O     1 
ATOM   10459 N N     . ILE A 1 2806 ? 206.420 208.633 153.452 1.00 11.10 ? 2806 ILE A N     1 
ATOM   10460 C CA    . ILE A 1 2806 ? 205.920 208.623 152.079 1.00 5.61  ? 2806 ILE A CA    1 
ATOM   10461 C C     . ILE A 1 2806 ? 206.908 209.318 151.150 1.00 5.44  ? 2806 ILE A C     1 
ATOM   10462 O O     . ILE A 1 2806 ? 207.178 208.843 150.041 1.00 11.24 ? 2806 ILE A O     1 
ATOM   10463 C CB    . ILE A 1 2806 ? 204.521 209.263 152.008 1.00 5.89  ? 2806 ILE A CB    1 
ATOM   10464 C CG1   . ILE A 1 2806 ? 203.484 208.342 152.644 1.00 8.18  ? 2806 ILE A CG1   1 
ATOM   10465 C CG2   . ILE A 1 2806 ? 204.123 209.504 150.570 1.00 8.51  ? 2806 ILE A CG2   1 
ATOM   10466 C CD1   . ILE A 1 2806 ? 202.085 208.906 152.624 1.00 8.93  ? 2806 ILE A CD1   1 
ATOM   10467 N N     . PHE A 1 2807 ? 207.479 210.442 151.592 1.00 6.05  ? 2807 PHE A N     1 
ATOM   10468 C CA    . PHE A 1 2807 ? 208.438 211.172 150.768 1.00 8.45  ? 2807 PHE A CA    1 
ATOM   10469 C C     . PHE A 1 2807 ? 209.703 210.356 150.531 1.00 10.04 ? 2807 PHE A C     1 
ATOM   10470 O O     . PHE A 1 2807 ? 210.255 210.362 149.425 1.00 15.78 ? 2807 PHE A O     1 
ATOM   10471 C CB    . PHE A 1 2807 ? 208.748 212.524 151.427 1.00 8.52  ? 2807 PHE A CB    1 
ATOM   10472 C CG    . PHE A 1 2807 ? 209.987 213.210 150.906 1.00 12.50 ? 2807 PHE A CG    1 
ATOM   10473 C CD1   . PHE A 1 2807 ? 211.251 212.853 151.353 1.00 14.11 ? 2807 PHE A CD1   1 
ATOM   10474 C CD2   . PHE A 1 2807 ? 209.880 214.223 149.970 1.00 12.87 ? 2807 PHE A CD2   1 
ATOM   10475 C CE1   . PHE A 1 2807 ? 212.377 213.488 150.872 1.00 15.95 ? 2807 PHE A CE1   1 
ATOM   10476 C CE2   . PHE A 1 2807 ? 211.004 214.860 149.487 1.00 13.75 ? 2807 PHE A CE2   1 
ATOM   10477 C CZ    . PHE A 1 2807 ? 212.254 214.492 149.939 1.00 14.83 ? 2807 PHE A CZ    1 
ATOM   10478 N N     . GLU A 1 2808 ? 210.188 209.658 151.559 1.00 7.81  ? 2808 GLU A N     1 
ATOM   10479 C CA    . GLU A 1 2808 ? 211.362 208.811 151.383 1.00 9.89  ? 2808 GLU A CA    1 
ATOM   10480 C C     . GLU A 1 2808 ? 211.050 207.625 150.483 1.00 11.75 ? 2808 GLU A C     1 
ATOM   10481 O O     . GLU A 1 2808 ? 211.947 207.073 149.836 1.00 16.60 ? 2808 GLU A O     1 
ATOM   10482 C CB    . GLU A 1 2808 ? 211.875 208.333 152.739 1.00 9.89  ? 2808 GLU A CB    1 
ATOM   10483 C CG    . GLU A 1 2808 ? 213.042 209.135 153.280 1.00 16.35 ? 2808 GLU A CG    1 
ATOM   10484 C CD    . GLU A 1 2808 ? 213.452 208.693 154.669 1.00 16.55 ? 2808 GLU A CD    1 
ATOM   10485 O OE1   . GLU A 1 2808 ? 213.638 207.475 154.874 1.00 10.72 ? 2808 GLU A OE1   1 
ATOM   10486 O OE2   . GLU A 1 2808 ? 213.585 209.561 155.556 1.00 13.47 ? 2808 GLU A OE2   1 
ATOM   10487 N N     . ALA A 1 2809 ? 209.782 207.213 150.434 1.00 12.40 ? 2809 ALA A N     1 
ATOM   10488 C CA    . ALA A 1 2809 ? 209.397 206.115 149.557 1.00 7.12  ? 2809 ALA A CA    1 
ATOM   10489 C C     . ALA A 1 2809 ? 209.127 206.573 148.131 1.00 12.71 ? 2809 ALA A C     1 
ATOM   10490 O O     . ALA A 1 2809 ? 208.800 205.738 147.280 1.00 21.36 ? 2809 ALA A O     1 
ATOM   10491 C CB    . ALA A 1 2809 ? 208.172 205.398 150.120 1.00 5.50  ? 2809 ALA A CB    1 
ATOM   10492 N N     . LEU A 1 2810 ? 209.236 207.873 147.847 1.00 12.23 ? 2810 LEU A N     1 
ATOM   10493 C CA    . LEU A 1 2810 ? 209.084 208.401 146.496 1.00 11.01 ? 2810 LEU A CA    1 
ATOM   10494 C C     . LEU A 1 2810 ? 210.342 209.094 145.987 1.00 14.28 ? 2810 LEU A C     1 
ATOM   10495 O O     . LEU A 1 2810 ? 210.292 209.764 144.951 1.00 21.39 ? 2810 LEU A O     1 
ATOM   10496 C CB    . LEU A 1 2810 ? 207.898 209.364 146.418 1.00 11.11 ? 2810 LEU A CB    1 
ATOM   10497 C CG    . LEU A 1 2810 ? 206.539 208.964 146.980 1.00 12.79 ? 2810 LEU A CG    1 
ATOM   10498 C CD1   . LEU A 1 2810 ? 205.485 209.940 146.505 1.00 12.74 ? 2810 LEU A CD1   1 
ATOM   10499 C CD2   . LEU A 1 2810 ? 206.185 207.565 146.543 1.00 13.13 ? 2810 LEU A CD2   1 
ATOM   10500 N N     . ARG A 1 2811 ? 211.478 208.953 146.686 1.00 15.36 ? 2811 ARG A N     1 
ATOM   10501 C CA    . ARG A 1 2811 ? 212.670 209.692 146.266 1.00 20.51 ? 2811 ARG A CA    1 
ATOM   10502 C C     . ARG A 1 2811 ? 213.259 209.126 144.979 1.00 23.51 ? 2811 ARG A C     1 
ATOM   10503 O O     . ARG A 1 2811 ? 213.318 209.857 143.977 1.00 24.37 ? 2811 ARG A O     1 
ATOM   10504 C CB    . ARG A 1 2811 ? 213.689 209.749 147.409 1.00 21.16 ? 2811 ARG A CB    1 
ATOM   10505 C CG    . ARG A 1 2811 ? 213.656 211.020 148.226 1.00 19.72 ? 2811 ARG A CG    1 
ATOM   10506 C CD    . ARG A 1 2811 ? 214.970 211.207 148.964 1.00 20.32 ? 2811 ARG A CD    1 
ATOM   10507 N NE    . ARG A 1 2811 ? 215.185 212.586 149.381 1.00 26.75 ? 2811 ARG A NE    1 
ATOM   10508 C CZ    . ARG A 1 2811 ? 215.796 213.505 148.645 1.00 28.06 ? 2811 ARG A CZ    1 
ATOM   10509 N NH1   . ARG A 1 2811 ? 216.274 213.221 147.447 1.00 22.80 ? 2811 ARG A NH1   1 
ATOM   10510 N NH2   . ARG A 1 2811 ? 215.932 214.737 149.128 1.00 24.79 ? 2811 ARG A NH2   1 
ATOM   10511 N N     . PRO A 1 2812 ? 213.702 207.868 144.919 1.00 23.36 ? 2812 PRO A N     1 
ATOM   10512 C CA    . PRO A 1 2812 ? 214.233 207.315 143.660 1.00 26.21 ? 2812 PRO A CA    1 
ATOM   10513 C C     . PRO A 1 2812 ? 213.172 206.826 142.684 1.00 24.98 ? 2812 PRO A C     1 
ATOM   10514 O O     . PRO A 1 2812 ? 213.536 206.434 141.573 1.00 28.93 ? 2812 PRO A O     1 
ATOM   10515 C CB    . PRO A 1 2812 ? 215.075 206.122 144.165 1.00 27.60 ? 2812 PRO A CB    1 
ATOM   10516 C CG    . PRO A 1 2812 ? 215.398 206.500 145.590 1.00 23.03 ? 2812 PRO A CG    1 
ATOM   10517 C CD    . PRO A 1 2812 ? 213.968 206.869 145.945 1.00 20.55 ? 2812 PRO A CD    1 
ATOM   10518 N N     . LEU A 1 2813 ? 211.899 206.849 143.062 1.00 20.77 ? 2813 LEU A N     1 
ATOM   10519 C CA    . LEU A 1 2813 ? 210.848 206.144 142.347 1.00 23.06 ? 2813 LEU A CA    1 
ATOM   10520 C C     . LEU A 1 2813 ? 210.014 207.128 141.540 1.00 26.14 ? 2813 LEU A C     1 
ATOM   10521 O O     . LEU A 1 2813 ? 209.574 208.155 142.066 1.00 27.64 ? 2813 LEU A O     1 
ATOM   10522 C CB    . LEU A 1 2813 ? 209.986 205.364 143.343 1.00 20.31 ? 2813 LEU A CB    1 
ATOM   10523 C CG    . LEU A 1 2813 ? 208.907 204.386 142.886 1.00 24.94 ? 2813 LEU A CG    1 
ATOM   10524 C CD1   . LEU A 1 2813 ? 208.697 203.331 143.953 1.00 24.98 ? 2813 LEU A CD1   1 
ATOM   10525 C CD2   . LEU A 1 2813 ? 207.603 205.099 142.620 1.00 23.76 ? 2813 LEU A CD2   1 
ATOM   10526 N N     . GLU A 1 2814 ? 209.795 206.806 140.270 1.00 25.47 ? 2814 GLU A N     1 
ATOM   10527 C CA    . GLU A 1 2814 ? 209.029 207.629 139.347 1.00 24.95 ? 2814 GLU A CA    1 
ATOM   10528 C C     . GLU A 1 2814 ? 207.806 206.861 138.850 1.00 27.87 ? 2814 GLU A C     1 
ATOM   10529 O O     . GLU A 1 2814 ? 207.540 205.730 139.268 1.00 26.20 ? 2814 GLU A O     1 
ATOM   10530 C CB    . GLU A 1 2814 ? 209.902 208.071 138.169 1.00 26.55 ? 2814 GLU A CB    1 
ATOM   10531 C CG    . GLU A 1 2814 ? 211.249 208.647 138.565 1.00 25.15 ? 2814 GLU A CG    1 
ATOM   10532 C CD    . GLU A 1 2814 ? 211.797 209.598 137.520 1.00 27.12 ? 2814 GLU A CD    1 
ATOM   10533 O OE1   . GLU A 1 2814 ? 212.009 209.169 136.367 1.00 26.78 ? 2814 GLU A OE1   1 
ATOM   10534 O OE2   . GLU A 1 2814 ? 212.020 210.779 137.852 1.00 26.07 ? 2814 GLU A OE2   1 
ATOM   10535 N N     . THR A 1 2815 ? 207.051 207.516 137.959 1.00 27.79 ? 2815 THR A N     1 
ATOM   10536 C CA    . THR A 1 2815 ? 205.910 206.963 137.226 1.00 31.01 ? 2815 THR A CA    1 
ATOM   10537 C C     . THR A 1 2815 ? 205.008 206.090 138.094 1.00 30.33 ? 2815 THR A C     1 
ATOM   10538 O O     . THR A 1 2815 ? 204.410 205.124 137.608 1.00 29.99 ? 2815 THR A O     1 
ATOM   10539 C CB    . THR A 1 2815 ? 206.376 206.192 135.975 1.00 31.71 ? 2815 THR A CB    1 
ATOM   10540 O OG1   . THR A 1 2815 ? 205.235 205.816 135.192 1.00 32.95 ? 2815 THR A OG1   1 
ATOM   10541 C CG2   . THR A 1 2815 ? 207.183 204.938 136.312 1.00 23.77 ? 2815 THR A CG2   1 
ATOM   10542 N N     . LEU A 1 2816 ? 204.880 206.440 139.365 1.00 20.30 ? 2816 LEU A N     1 
ATOM   10543 C CA    . LEU A 1 2816 ? 204.083 205.638 140.282 1.00 16.50 ? 2816 LEU A CA    1 
ATOM   10544 C C     . LEU A 1 2816 ? 202.601 205.818 139.978 1.00 21.80 ? 2816 LEU A C     1 
ATOM   10545 O O     . LEU A 1 2816 ? 202.133 206.956 139.857 1.00 29.85 ? 2816 LEU A O     1 
ATOM   10546 C CB    . LEU A 1 2816 ? 204.371 206.043 141.722 1.00 19.57 ? 2816 LEU A CB    1 
ATOM   10547 C CG    . LEU A 1 2816 ? 203.669 205.254 142.826 1.00 18.20 ? 2816 LEU A CG    1 
ATOM   10548 C CD1   . LEU A 1 2816 ? 204.105 203.800 142.788 1.00 18.21 ? 2816 LEU A CD1   1 
ATOM   10549 C CD2   . LEU A 1 2816 ? 203.966 205.864 144.178 1.00 16.54 ? 2816 LEU A CD2   1 
ATOM   10550 N N     . PRO A 1 2817 ? 201.835 204.739 139.839 1.00 16.01 ? 2817 PRO A N     1 
ATOM   10551 C CA    . PRO A 1 2817 ? 200.379 204.886 139.712 1.00 20.41 ? 2817 PRO A CA    1 
ATOM   10552 C C     . PRO A 1 2817 ? 199.744 205.300 141.028 1.00 18.76 ? 2817 PRO A C     1 
ATOM   10553 O O     . PRO A 1 2817 ? 200.410 205.298 142.068 1.00 17.20 ? 2817 PRO A O     1 
ATOM   10554 C CB    . PRO A 1 2817 ? 199.923 203.490 139.276 1.00 21.59 ? 2817 PRO A CB    1 
ATOM   10555 C CG    . PRO A 1 2817 ? 200.973 202.576 139.805 1.00 18.77 ? 2817 PRO A CG    1 
ATOM   10556 C CD    . PRO A 1 2817 ? 202.265 203.337 139.713 1.00 17.15 ? 2817 PRO A CD    1 
ATOM   10557 N N     . VAL A 1 2818 ? 198.459 205.663 140.999 1.00 22.60 ? 2818 VAL A N     1 
ATOM   10558 C CA    . VAL A 1 2818 ? 197.770 206.014 142.237 1.00 21.92 ? 2818 VAL A CA    1 
ATOM   10559 C C     . VAL A 1 2818 ? 197.722 204.819 143.177 1.00 23.58 ? 2818 VAL A C     1 
ATOM   10560 O O     . VAL A 1 2818 ? 197.789 204.980 144.402 1.00 23.21 ? 2818 VAL A O     1 
ATOM   10561 C CB    . VAL A 1 2818 ? 196.359 206.565 141.937 1.00 21.20 ? 2818 VAL A CB    1 
ATOM   10562 C CG1   . VAL A 1 2818 ? 195.480 205.501 141.300 1.00 17.72 ? 2818 VAL A CG1   1 
ATOM   10563 C CG2   . VAL A 1 2818 ? 195.718 207.097 143.208 1.00 17.66 ? 2818 VAL A CG2   1 
ATOM   10564 N N     . GLU A 1 2819 ? 197.626 203.606 142.624 1.00 24.36 ? 2819 GLU A N     1 
ATOM   10565 C CA    . GLU A 1 2819 ? 197.581 202.407 143.452 1.00 21.91 ? 2819 GLU A CA    1 
ATOM   10566 C C     . GLU A 1 2819 ? 198.855 202.256 144.274 1.00 19.68 ? 2819 GLU A C     1 
ATOM   10567 O O     . GLU A 1 2819 ? 198.798 201.932 145.464 1.00 19.86 ? 2819 GLU A O     1 
ATOM   10568 C CB    . GLU A 1 2819 ? 197.361 201.175 142.575 1.00 26.23 ? 2819 GLU A CB    1 
ATOM   10569 C CG    . GLU A 1 2819 ? 196.499 201.429 141.348 1.00 25.51 ? 2819 GLU A CG    1 
ATOM   10570 C CD    . GLU A 1 2819 ? 195.037 201.622 141.690 1.00 31.25 ? 2819 GLU A CD    1 
ATOM   10571 O OE1   . GLU A 1 2819 ? 194.623 201.199 142.789 1.00 33.49 ? 2819 GLU A OE1   1 
ATOM   10572 O OE2   . GLU A 1 2819 ? 194.300 202.195 140.860 1.00 31.05 ? 2819 GLU A OE2   1 
ATOM   10573 N N     . GLY A 1 2820 ? 200.013 202.500 143.661 1.00 15.61 ? 2820 GLY A N     1 
ATOM   10574 C CA    . GLY A 1 2820 ? 201.259 202.412 144.404 1.00 11.98 ? 2820 GLY A CA    1 
ATOM   10575 C C     . GLY A 1 2820 ? 201.378 203.476 145.477 1.00 16.98 ? 2820 GLY A C     1 
ATOM   10576 O O     . GLY A 1 2820 ? 201.872 203.212 146.577 1.00 17.23 ? 2820 GLY A O     1 
ATOM   10577 N N     . LEU A 1 2821 ? 200.926 204.695 145.174 1.00 18.04 ? 2821 LEU A N     1 
ATOM   10578 C CA    . LEU A 1 2821 ? 200.958 205.765 146.166 1.00 10.03 ? 2821 LEU A CA    1 
ATOM   10579 C C     . LEU A 1 2821 ? 200.089 205.426 147.368 1.00 6.93  ? 2821 LEU A C     1 
ATOM   10580 O O     . LEU A 1 2821 ? 200.498 205.621 148.518 1.00 17.68 ? 2821 LEU A O     1 
ATOM   10581 C CB    . LEU A 1 2821 ? 200.509 207.084 145.537 1.00 16.38 ? 2821 LEU A CB    1 
ATOM   10582 C CG    . LEU A 1 2821 ? 200.677 208.326 146.415 1.00 13.34 ? 2821 LEU A CG    1 
ATOM   10583 C CD1   . LEU A 1 2821 ? 202.102 208.437 146.921 1.00 14.07 ? 2821 LEU A CD1   1 
ATOM   10584 C CD2   . LEU A 1 2821 ? 200.280 209.578 145.653 1.00 19.12 ? 2821 LEU A CD2   1 
ATOM   10585 N N     . ILE A 1 2822 ? 198.883 204.910 147.127 1.00 4.86  ? 2822 ILE A N     1 
ATOM   10586 C CA    . ILE A 1 2822 ? 198.019 204.620 148.265 1.00 7.50  ? 2822 ILE A CA    1 
ATOM   10587 C C     . ILE A 1 2822 ? 198.495 203.354 148.971 1.00 11.91 ? 2822 ILE A C     1 
ATOM   10588 O O     . ILE A 1 2822 ? 198.265 203.182 150.172 1.00 17.53 ? 2822 ILE A O     1 
ATOM   10589 C CB    . ILE A 1 2822 ? 196.545 204.540 147.822 1.00 14.56 ? 2822 ILE A CB    1 
ATOM   10590 C CG1   . ILE A 1 2822 ? 195.647 204.092 148.969 1.00 14.43 ? 2822 ILE A CG1   1 
ATOM   10591 C CG2   . ILE A 1 2822 ? 196.376 203.555 146.696 1.00 18.96 ? 2822 ILE A CG2   1 
ATOM   10592 C CD1   . ILE A 1 2822 ? 194.184 204.194 148.639 1.00 15.23 ? 2822 ILE A CD1   1 
ATOM   10593 N N     . ARG A 1 2823 ? 199.206 202.472 148.263 1.00 14.63 ? 2823 ARG A N     1 
ATOM   10594 C CA    . ARG A 1 2823 ? 199.868 201.348 148.921 1.00 9.96  ? 2823 ARG A CA    1 
ATOM   10595 C C     . ARG A 1 2823 ? 200.926 201.839 149.902 1.00 9.85  ? 2823 ARG A C     1 
ATOM   10596 O O     . ARG A 1 2823 ? 201.014 201.353 151.036 1.00 10.48 ? 2823 ARG A O     1 
ATOM   10597 C CB    . ARG A 1 2823 ? 200.493 200.429 147.868 1.00 16.15 ? 2823 ARG A CB    1 
ATOM   10598 C CG    . ARG A 1 2823 ? 201.247 199.223 148.416 1.00 14.85 ? 2823 ARG A CG    1 
ATOM   10599 C CD    . ARG A 1 2823 ? 200.332 198.049 148.711 1.00 17.58 ? 2823 ARG A CD    1 
ATOM   10600 N NE    . ARG A 1 2823 ? 201.066 196.906 149.239 1.00 16.15 ? 2823 ARG A NE    1 
ATOM   10601 C CZ    . ARG A 1 2823 ? 201.736 196.038 148.494 1.00 16.98 ? 2823 ARG A CZ    1 
ATOM   10602 N NH1   . ARG A 1 2823 ? 201.788 196.152 147.178 1.00 18.64 ? 2823 ARG A NH1   1 
ATOM   10603 N NH2   . ARG A 1 2823 ? 202.372 195.031 149.086 1.00 18.51 ? 2823 ARG A NH2   1 
ATOM   10604 N N     . ILE A 1 2824 ? 201.742 202.807 149.478 1.00 12.41 ? 2824 ILE A N     1 
ATOM   10605 C CA    . ILE A 1 2824 ? 202.747 203.385 150.371 1.00 11.00 ? 2824 ILE A CA    1 
ATOM   10606 C C     . ILE A 1 2824 ? 202.075 204.082 151.545 1.00 6.11  ? 2824 ILE A C     1 
ATOM   10607 O O     . ILE A 1 2824 ? 202.522 203.979 152.694 1.00 12.43 ? 2824 ILE A O     1 
ATOM   10608 C CB    . ILE A 1 2824 ? 203.661 204.352 149.597 1.00 6.81  ? 2824 ILE A CB    1 
ATOM   10609 C CG1   . ILE A 1 2824 ? 204.361 203.624 148.452 1.00 8.38  ? 2824 ILE A CG1   1 
ATOM   10610 C CG2   . ILE A 1 2824 ? 204.674 204.976 150.533 1.00 6.85  ? 2824 ILE A CG2   1 
ATOM   10611 C CD1   . ILE A 1 2824 ? 205.551 204.349 147.895 1.00 11.89 ? 2824 ILE A CD1   1 
ATOM   10612 N N     . TRP A 1 2825 ? 201.004 204.824 151.263 1.00 3.87  ? 2825 TRP A N     1 
ATOM   10613 C CA    . TRP A 1 2825 ? 200.217 205.464 152.311 1.00 1.67  ? 2825 TRP A CA    1 
ATOM   10614 C C     . TRP A 1 2825 ? 199.733 204.453 153.345 1.00 6.78  ? 2825 TRP A C     1 
ATOM   10615 O O     . TRP A 1 2825 ? 199.872 204.669 154.554 1.00 10.04 ? 2825 TRP A O     1 
ATOM   10616 C CB    . TRP A 1 2825 ? 199.050 206.207 151.660 1.00 3.56  ? 2825 TRP A CB    1 
ATOM   10617 C CG    . TRP A 1 2825 ? 198.095 206.857 152.594 1.00 5.24  ? 2825 TRP A CG    1 
ATOM   10618 C CD1   . TRP A 1 2825 ? 198.104 208.152 153.006 1.00 8.78  ? 2825 TRP A CD1   1 
ATOM   10619 C CD2   . TRP A 1 2825 ? 196.927 206.261 153.168 1.00 5.62  ? 2825 TRP A CD2   1 
ATOM   10620 N NE1   . TRP A 1 2825 ? 197.039 208.391 153.836 1.00 7.63  ? 2825 TRP A NE1   1 
ATOM   10621 C CE2   . TRP A 1 2825 ? 196.298 207.245 153.950 1.00 5.05  ? 2825 TRP A CE2   1 
ATOM   10622 C CE3   . TRP A 1 2825 ? 196.363 204.985 153.111 1.00 7.67  ? 2825 TRP A CE3   1 
ATOM   10623 C CZ2   . TRP A 1 2825 ? 195.137 206.995 154.673 1.00 5.80  ? 2825 TRP A CZ2   1 
ATOM   10624 C CZ3   . TRP A 1 2825 ? 195.209 204.739 153.827 1.00 12.13 ? 2825 TRP A CZ3   1 
ATOM   10625 C CH2   . TRP A 1 2825 ? 194.609 205.738 154.598 1.00 10.77 ? 2825 TRP A CH2   1 
ATOM   10626 N N     . ALA A 1 2826 ? 199.176 203.332 152.885 1.00 8.11  ? 2826 ALA A N     1 
ATOM   10627 C CA    . ALA A 1 2826 ? 198.670 202.318 153.803 1.00 3.30  ? 2826 ALA A CA    1 
ATOM   10628 C C     . ALA A 1 2826 ? 199.799 201.661 154.585 1.00 7.24  ? 2826 ALA A C     1 
ATOM   10629 O O     . ALA A 1 2826 ? 199.642 201.359 155.774 1.00 14.52 ? 2826 ALA A O     1 
ATOM   10630 C CB    . ALA A 1 2826 ? 197.864 201.271 153.036 1.00 6.83  ? 2826 ALA A CB    1 
ATOM   10631 N N     . HIS A 1 2827 ? 200.939 201.420 153.936 1.00 7.11  ? 2827 HIS A N     1 
ATOM   10632 C CA    . HIS A 1 2827 ? 202.076 200.827 154.631 1.00 7.21  ? 2827 HIS A CA    1 
ATOM   10633 C C     . HIS A 1 2827 ? 202.564 201.739 155.749 1.00 5.74  ? 2827 HIS A C     1 
ATOM   10634 O O     . HIS A 1 2827 ? 202.815 201.289 156.873 1.00 7.37  ? 2827 HIS A O     1 
ATOM   10635 C CB    . HIS A 1 2827 ? 203.205 200.548 153.640 1.00 5.72  ? 2827 HIS A CB    1 
ATOM   10636 C CG    . HIS A 1 2827 ? 204.501 200.177 154.288 1.00 7.53  ? 2827 HIS A CG    1 
ATOM   10637 N ND1   . HIS A 1 2827 ? 204.584 199.262 155.314 1.00 7.26  ? 2827 HIS A ND1   1 
ATOM   10638 C CD2   . HIS A 1 2827 ? 205.763 200.613 154.070 1.00 10.51 ? 2827 HIS A CD2   1 
ATOM   10639 C CE1   . HIS A 1 2827 ? 205.844 199.138 155.689 1.00 6.26  ? 2827 HIS A CE1   1 
ATOM   10640 N NE2   . HIS A 1 2827 ? 206.580 199.949 154.951 1.00 9.25  ? 2827 HIS A NE2   1 
ATOM   10641 N N     . GLU A 1 2828 ? 202.692 203.035 155.457 1.00 4.39  ? 2828 GLU A N     1 
ATOM   10642 C CA    . GLU A 1 2828 ? 203.110 203.988 156.479 1.00 1.53  ? 2828 GLU A CA    1 
ATOM   10643 C C     . GLU A 1 2828 ? 202.080 204.081 157.598 1.00 0.04  ? 2828 GLU A C     1 
ATOM   10644 O O     . GLU A 1 2828 ? 202.443 204.180 158.775 1.00 9.28  ? 2828 GLU A O     1 
ATOM   10645 C CB    . GLU A 1 2828 ? 203.345 205.361 155.853 1.00 5.25  ? 2828 GLU A CB    1 
ATOM   10646 C CG    . GLU A 1 2828 ? 204.597 205.467 154.999 1.00 7.13  ? 2828 GLU A CG    1 
ATOM   10647 C CD    . GLU A 1 2828 ? 205.748 204.635 155.526 1.00 9.08  ? 2828 GLU A CD    1 
ATOM   10648 O OE1   . GLU A 1 2828 ? 206.212 204.903 156.653 1.00 9.67  ? 2828 GLU A OE1   1 
ATOM   10649 O OE2   . GLU A 1 2828 ? 206.199 203.721 154.806 1.00 5.04  ? 2828 GLU A OE2   1 
ATOM   10650 N N     . ALA A 1 2829 ? 200.792 204.064 157.250 1.00 0.65  ? 2829 ALA A N     1 
ATOM   10651 C CA    . ALA A 1 2829 ? 199.753 204.135 158.270 1.00 0.00  ? 2829 ALA A CA    1 
ATOM   10652 C C     . ALA A 1 2829 ? 199.794 202.924 159.188 1.00 6.97  ? 2829 ALA A C     1 
ATOM   10653 O O     . ALA A 1 2829 ? 199.624 203.054 160.403 1.00 14.22 ? 2829 ALA A O     1 
ATOM   10654 C CB    . ALA A 1 2829 ? 198.381 204.258 157.616 1.00 3.12  ? 2829 ALA A CB    1 
ATOM   10655 N N     . LEU A 1 2830 ? 199.998 201.734 158.624 1.00 7.58  ? 2830 LEU A N     1 
ATOM   10656 C CA    . LEU A 1 2830 ? 200.137 200.544 159.455 1.00 5.65  ? 2830 LEU A CA    1 
ATOM   10657 C C     . LEU A 1 2830 ? 201.389 200.606 160.318 1.00 4.07  ? 2830 LEU A C     1 
ATOM   10658 O O     . LEU A 1 2830 ? 201.357 200.195 161.483 1.00 4.72  ? 2830 LEU A O     1 
ATOM   10659 C CB    . LEU A 1 2830 ? 200.153 199.289 158.585 1.00 5.31  ? 2830 LEU A CB    1 
ATOM   10660 C CG    . LEU A 1 2830 ? 198.855 198.974 157.845 1.00 4.26  ? 2830 LEU A CG    1 
ATOM   10661 C CD1   . LEU A 1 2830 ? 198.938 197.614 157.184 1.00 13.56 ? 2830 LEU A CD1   1 
ATOM   10662 C CD2   . LEU A 1 2830 ? 197.678 199.033 158.802 1.00 8.91  ? 2830 LEU A CD2   1 
ATOM   10663 N N     . ARG A 1 2831 ? 202.494 201.119 159.774 1.00 6.26  ? 2831 ARG A N     1 
ATOM   10664 C CA    . ARG A 1 2831 ? 203.732 201.157 160.542 1.00 4.83  ? 2831 ARG A CA    1 
ATOM   10665 C C     . ARG A 1 2831 ? 203.665 202.172 161.674 1.00 0.00  ? 2831 ARG A C     1 
ATOM   10666 O O     . ARG A 1 2831 ? 204.306 201.981 162.713 1.00 5.14  ? 2831 ARG A O     1 
ATOM   10667 C CB    . ARG A 1 2831 ? 204.915 201.471 159.627 1.00 2.82  ? 2831 ARG A CB    1 
ATOM   10668 C CG    . ARG A 1 2831 ? 205.518 200.272 158.882 1.00 2.87  ? 2831 ARG A CG    1 
ATOM   10669 C CD    . ARG A 1 2831 ? 206.034 199.140 159.776 1.00 5.87  ? 2831 ARG A CD    1 
ATOM   10670 N NE    . ARG A 1 2831 ? 204.979 198.362 160.420 1.00 9.90  ? 2831 ARG A NE    1 
ATOM   10671 C CZ    . ARG A 1 2831 ? 204.048 197.665 159.781 1.00 7.26  ? 2831 ARG A CZ    1 
ATOM   10672 N NH1   . ARG A 1 2831 ? 204.033 197.571 158.461 1.00 7.61  ? 2831 ARG A NH1   1 
ATOM   10673 N NH2   . ARG A 1 2831 ? 203.110 197.038 160.485 1.00 5.15  ? 2831 ARG A NH2   1 
ATOM   10674 N N     . LEU A 1 2832 ? 202.913 203.256 161.495 1.00 1.82  ? 2832 LEU A N     1 
ATOM   10675 C CA    . LEU A 1 2832 ? 202.843 204.313 162.494 1.00 8.01  ? 2832 LEU A CA    1 
ATOM   10676 C C     . LEU A 1 2832 ? 201.563 204.294 163.319 1.00 3.98  ? 2832 LEU A C     1 
ATOM   10677 O O     . LEU A 1 2832 ? 201.405 205.143 164.200 1.00 5.17  ? 2832 LEU A O     1 
ATOM   10678 C CB    . LEU A 1 2832 ? 202.980 205.683 161.820 1.00 4.59  ? 2832 LEU A CB    1 
ATOM   10679 C CG    . LEU A 1 2832 ? 204.366 206.030 161.278 1.00 4.32  ? 2832 LEU A CG    1 
ATOM   10680 C CD1   . LEU A 1 2832 ? 204.295 207.280 160.434 1.00 6.13  ? 2832 LEU A CD1   1 
ATOM   10681 C CD2   . LEU A 1 2832 ? 205.352 206.211 162.416 1.00 5.44  ? 2832 LEU A CD2   1 
ATOM   10682 N N     . PHE A 1 2833 ? 200.655 203.357 163.065 1.00 5.78  ? 2833 PHE A N     1 
ATOM   10683 C CA    . PHE A 1 2833 ? 199.363 203.349 163.735 1.00 4.88  ? 2833 PHE A CA    1 
ATOM   10684 C C     . PHE A 1 2833 ? 198.956 201.995 164.288 1.00 11.38 ? 2833 PHE A C     1 
ATOM   10685 O O     . PHE A 1 2833 ? 198.133 201.955 165.209 1.00 17.87 ? 2833 PHE A O     1 
ATOM   10686 C CB    . PHE A 1 2833 ? 198.264 203.828 162.772 1.00 7.91  ? 2833 PHE A CB    1 
ATOM   10687 C CG    . PHE A 1 2833 ? 197.984 205.300 162.853 1.00 10.17 ? 2833 PHE A CG    1 
ATOM   10688 C CD1   . PHE A 1 2833 ? 197.094 205.804 163.784 1.00 8.54  ? 2833 PHE A CD1   1 
ATOM   10689 C CD2   . PHE A 1 2833 ? 198.615 206.182 161.993 1.00 4.84  ? 2833 PHE A CD2   1 
ATOM   10690 C CE1   . PHE A 1 2833 ? 196.844 207.158 163.856 1.00 6.27  ? 2833 PHE A CE1   1 
ATOM   10691 C CE2   . PHE A 1 2833 ? 198.367 207.534 162.062 1.00 7.29  ? 2833 PHE A CE2   1 
ATOM   10692 C CZ    . PHE A 1 2833 ? 197.479 208.022 162.993 1.00 8.84  ? 2833 PHE A CZ    1 
ATOM   10693 N N     . GLN A 1 2834 ? 199.494 200.891 163.769 1.00 11.46 ? 2834 GLN A N     1 
ATOM   10694 C CA    . GLN A 1 2834 ? 199.055 199.556 164.151 1.00 5.79  ? 2834 GLN A CA    1 
ATOM   10695 C C     . GLN A 1 2834 ? 200.093 198.763 164.925 1.00 7.13  ? 2834 GLN A C     1 
ATOM   10696 O O     . GLN A 1 2834 ? 199.722 198.013 165.830 1.00 17.05 ? 2834 GLN A O     1 
ATOM   10697 C CB    . GLN A 1 2834 ? 198.651 198.755 162.907 1.00 7.61  ? 2834 GLN A CB    1 
ATOM   10698 C CG    . GLN A 1 2834 ? 197.891 197.477 163.213 1.00 8.14  ? 2834 GLN A CG    1 
ATOM   10699 C CD    . GLN A 1 2834 ? 198.194 196.370 162.226 1.00 15.44 ? 2834 GLN A CD    1 
ATOM   10700 O OE1   . GLN A 1 2834 ? 199.354 196.070 161.947 1.00 17.18 ? 2834 GLN A OE1   1 
ATOM   10701 N NE2   . GLN A 1 2834 ? 197.148 195.757 161.690 1.00 19.01 ? 2834 GLN A NE2   1 
ATOM   10702 N N     . ASP A 1 2835 ? 201.378 198.909 164.602 1.00 6.97  ? 2835 ASP A N     1 
ATOM   10703 C CA    . ASP A 1 2835 ? 202.408 198.140 165.294 1.00 9.46  ? 2835 ASP A CA    1 
ATOM   10704 C C     . ASP A 1 2835 ? 202.541 198.524 166.763 1.00 4.70  ? 2835 ASP A C     1 
ATOM   10705 O O     . ASP A 1 2835 ? 203.177 197.792 167.527 1.00 8.75  ? 2835 ASP A O     1 
ATOM   10706 C CB    . ASP A 1 2835 ? 203.736 198.256 164.525 1.00 7.57  ? 2835 ASP A CB    1 
ATOM   10707 C CG    . ASP A 1 2835 ? 204.519 199.537 164.818 1.00 9.85  ? 2835 ASP A CG    1 
ATOM   10708 O OD1   . ASP A 1 2835 ? 204.167 200.330 165.715 1.00 11.46 ? 2835 ASP A OD1   1 
ATOM   10709 O OD2   . ASP A 1 2835 ? 205.522 199.758 164.109 1.00 8.62  ? 2835 ASP A OD2   1 
ATOM   10710 N N     . ARG A 1 2836 ? 201.968 199.655 167.163 1.00 7.75  ? 2836 ARG A N     1 
ATOM   10711 C CA    . ARG A 1 2836 ? 201.915 200.078 168.555 1.00 9.71  ? 2836 ARG A CA    1 
ATOM   10712 C C     . ARG A 1 2836 ? 200.773 199.434 169.334 1.00 9.76  ? 2836 ARG A C     1 
ATOM   10713 O O     . ARG A 1 2836 ? 200.903 199.244 170.548 1.00 10.38 ? 2836 ARG A O     1 
ATOM   10714 C CB    . ARG A 1 2836 ? 201.807 201.608 168.613 1.00 8.15  ? 2836 ARG A CB    1 
ATOM   10715 C CG    . ARG A 1 2836 ? 201.132 202.177 169.846 1.00 8.80  ? 2836 ARG A CG    1 
ATOM   10716 C CD    . ARG A 1 2836 ? 200.631 203.583 169.581 1.00 10.52 ? 2836 ARG A CD    1 
ATOM   10717 N NE    . ARG A 1 2836 ? 201.737 204.522 169.438 1.00 13.81 ? 2836 ARG A NE    1 
ATOM   10718 C CZ    . ARG A 1 2836 ? 201.777 205.507 168.553 1.00 12.61 ? 2836 ARG A CZ    1 
ATOM   10719 N NH1   . ARG A 1 2836 ? 200.784 205.714 167.705 1.00 15.16 ? 2836 ARG A NH1   1 
ATOM   10720 N NH2   . ARG A 1 2836 ? 202.841 206.302 168.515 1.00 9.11  ? 2836 ARG A NH2   1 
ATOM   10721 N N     . LEU A 1 2837 ? 199.681 199.068 168.667 1.00 6.93  ? 2837 LEU A N     1 
ATOM   10722 C CA    . LEU A 1 2837 ? 198.513 198.543 169.359 1.00 9.80  ? 2837 LEU A CA    1 
ATOM   10723 C C     . LEU A 1 2837 ? 198.816 197.209 170.031 1.00 15.20 ? 2837 LEU A C     1 
ATOM   10724 O O     . LEU A 1 2837 ? 199.684 196.447 169.598 1.00 15.71 ? 2837 LEU A O     1 
ATOM   10725 C CB    . LEU A 1 2837 ? 197.343 198.379 168.391 1.00 10.59 ? 2837 LEU A CB    1 
ATOM   10726 C CG    . LEU A 1 2837 ? 197.000 199.597 167.537 1.00 4.40  ? 2837 LEU A CG    1 
ATOM   10727 C CD1   . LEU A 1 2837 ? 196.178 199.182 166.335 1.00 11.45 ? 2837 LEU A CD1   1 
ATOM   10728 C CD2   . LEU A 1 2837 ? 196.260 200.624 168.366 1.00 15.31 ? 2837 LEU A CD2   1 
ATOM   10729 N N     . VAL A 1 2838 ? 198.081 196.933 171.104 1.00 16.77 ? 2838 VAL A N     1 
ATOM   10730 C CA    . VAL A 1 2838 ? 198.303 195.754 171.927 1.00 13.83 ? 2838 VAL A CA    1 
ATOM   10731 C C     . VAL A 1 2838 ? 197.429 194.583 171.494 1.00 16.50 ? 2838 VAL A C     1 
ATOM   10732 O O     . VAL A 1 2838 ? 197.939 193.498 171.216 1.00 22.20 ? 2838 VAL A O     1 
ATOM   10733 C CB    . VAL A 1 2838 ? 198.072 196.099 173.414 1.00 16.23 ? 2838 VAL A CB    1 
ATOM   10734 C CG1   . VAL A 1 2838 ? 197.982 194.837 174.248 1.00 16.91 ? 2838 VAL A CG1   1 
ATOM   10735 C CG2   . VAL A 1 2838 ? 199.187 196.995 173.927 1.00 13.34 ? 2838 VAL A CG2   1 
ATOM   10736 N N     . GLU A 1 2839 ? 196.117 194.782 171.426 1.00 15.09 ? 2839 GLU A N     1 
ATOM   10737 C CA    . GLU A 1 2839 ? 195.181 193.693 171.193 1.00 21.88 ? 2839 GLU A CA    1 
ATOM   10738 C C     . GLU A 1 2839 ? 194.973 193.453 169.703 1.00 22.36 ? 2839 GLU A C     1 
ATOM   10739 O O     . GLU A 1 2839 ? 195.094 194.365 168.882 1.00 24.53 ? 2839 GLU A O     1 
ATOM   10740 C CB    . GLU A 1 2839 ? 193.837 193.980 171.864 1.00 21.41 ? 2839 GLU A CB    1 
ATOM   10741 C CG    . GLU A 1 2839 ? 193.949 194.423 173.312 1.00 21.40 ? 2839 GLU A CG    1 
ATOM   10742 C CD    . GLU A 1 2839 ? 192.609 194.799 173.910 1.00 25.28 ? 2839 GLU A CD    1 
ATOM   10743 O OE1   . GLU A 1 2839 ? 192.540 194.990 175.143 1.00 27.07 ? 2839 GLU A OE1   1 
ATOM   10744 O OE2   . GLU A 1 2839 ? 191.625 194.902 173.149 1.00 23.32 ? 2839 GLU A OE2   1 
ATOM   10745 N N     . ASP A 1 2840 ? 194.660 192.198 169.366 1.00 24.05 ? 2840 ASP A N     1 
ATOM   10746 C CA    . ASP A 1 2840 ? 194.372 191.838 167.982 1.00 26.41 ? 2840 ASP A CA    1 
ATOM   10747 C C     . ASP A 1 2840 ? 193.135 192.575 167.481 1.00 27.07 ? 2840 ASP A C     1 
ATOM   10748 O O     . ASP A 1 2840 ? 193.080 192.977 166.313 1.00 24.72 ? 2840 ASP A O     1 
ATOM   10749 C CB    . ASP A 1 2840 ? 194.198 190.315 167.888 1.00 28.65 ? 2840 ASP A CB    1 
ATOM   10750 C CG    . ASP A 1 2840 ? 193.648 189.839 166.541 1.00 30.13 ? 2840 ASP A CG    1 
ATOM   10751 O OD1   . ASP A 1 2840 ? 193.682 190.586 165.542 1.00 27.15 ? 2840 ASP A OD1   1 
ATOM   10752 O OD2   . ASP A 1 2840 ? 193.171 188.686 166.488 1.00 31.38 ? 2840 ASP A OD2   1 
ATOM   10753 N N     . GLU A 1 2841 ? 192.145 192.777 168.355 1.00 27.37 ? 2841 GLU A N     1 
ATOM   10754 C CA    . GLU A 1 2841 ? 190.956 193.531 167.970 1.00 27.45 ? 2841 GLU A CA    1 
ATOM   10755 C C     . GLU A 1 2841 ? 191.320 194.939 167.520 1.00 30.73 ? 2841 GLU A C     1 
ATOM   10756 O O     . GLU A 1 2841 ? 190.781 195.439 166.526 1.00 34.03 ? 2841 GLU A O     1 
ATOM   10757 C CB    . GLU A 1 2841 ? 189.964 193.576 169.133 1.00 25.02 ? 2841 GLU A CB    1 
ATOM   10758 C CG    . GLU A 1 2841 ? 189.031 194.776 169.106 1.00 28.66 ? 2841 GLU A CG    1 
ATOM   10759 C CD    . GLU A 1 2841 ? 187.982 194.676 168.015 1.00 34.80 ? 2841 GLU A CD    1 
ATOM   10760 O OE1   . GLU A 1 2841 ? 187.592 193.543 167.663 1.00 31.01 ? 2841 GLU A OE1   1 
ATOM   10761 O OE2   . GLU A 1 2841 ? 187.551 195.731 167.503 1.00 32.03 ? 2841 GLU A OE2   1 
ATOM   10762 N N     . GLU A 1 2842 ? 192.240 195.589 168.235 1.00 25.14 ? 2842 GLU A N     1 
ATOM   10763 C CA    . GLU A 1 2842 ? 192.696 196.914 167.829 1.00 18.83 ? 2842 GLU A CA    1 
ATOM   10764 C C     . GLU A 1 2842 ? 193.352 196.872 166.455 1.00 22.51 ? 2842 GLU A C     1 
ATOM   10765 O O     . GLU A 1 2842 ? 193.114 197.749 165.615 1.00 26.69 ? 2842 GLU A O     1 
ATOM   10766 C CB    . GLU A 1 2842 ? 193.668 197.468 168.870 1.00 18.75 ? 2842 GLU A CB    1 
ATOM   10767 C CG    . GLU A 1 2842 ? 192.998 198.026 170.113 1.00 23.67 ? 2842 GLU A CG    1 
ATOM   10768 C CD    . GLU A 1 2842 ? 193.903 198.018 171.325 1.00 27.66 ? 2842 GLU A CD    1 
ATOM   10769 O OE1   . GLU A 1 2842 ? 193.379 198.094 172.456 1.00 25.69 ? 2842 GLU A OE1   1 
ATOM   10770 O OE2   . GLU A 1 2842 ? 195.136 197.938 171.148 1.00 27.79 ? 2842 GLU A OE2   1 
ATOM   10771 N N     . ARG A 1 2843 ? 194.177 195.852 166.206 1.00 19.74 ? 2843 ARG A N     1 
ATOM   10772 C CA    . ARG A 1 2843 ? 194.878 195.749 164.930 1.00 16.50 ? 2843 ARG A CA    1 
ATOM   10773 C C     . ARG A 1 2843 ? 193.899 195.561 163.779 1.00 23.39 ? 2843 ARG A C     1 
ATOM   10774 O O     . ARG A 1 2843 ? 194.037 196.186 162.720 1.00 26.48 ? 2843 ARG A O     1 
ATOM   10775 C CB    . ARG A 1 2843 ? 195.867 194.588 164.972 1.00 20.19 ? 2843 ARG A CB    1 
ATOM   10776 C CG    . ARG A 1 2843 ? 197.122 194.845 165.776 1.00 14.74 ? 2843 ARG A CG    1 
ATOM   10777 C CD    . ARG A 1 2843 ? 197.778 193.525 166.116 1.00 17.49 ? 2843 ARG A CD    1 
ATOM   10778 N NE    . ARG A 1 2843 ? 198.289 193.483 167.478 1.00 22.21 ? 2843 ARG A NE    1 
ATOM   10779 C CZ    . ARG A 1 2843 ? 199.217 192.635 167.899 1.00 25.18 ? 2843 ARG A CZ    1 
ATOM   10780 N NH1   . ARG A 1 2843 ? 199.783 191.767 167.077 1.00 22.91 ? 2843 ARG A NH1   1 
ATOM   10781 N NH2   . ARG A 1 2843 ? 199.582 192.654 169.176 1.00 20.33 ? 2843 ARG A NH2   1 
ATOM   10782 N N     . ARG A 1 2844 ? 192.903 194.689 163.961 1.00 25.41 ? 2844 ARG A N     1 
ATOM   10783 C CA    . ARG A 1 2844 ? 191.946 194.465 162.884 1.00 27.66 ? 2844 ARG A CA    1 
ATOM   10784 C C     . ARG A 1 2844 ? 191.011 195.655 162.710 1.00 27.79 ? 2844 ARG A C     1 
ATOM   10785 O O     . ARG A 1 2844 ? 190.570 195.929 161.590 1.00 31.38 ? 2844 ARG A O     1 
ATOM   10786 C CB    . ARG A 1 2844 ? 191.154 193.176 163.113 1.00 28.88 ? 2844 ARG A CB    1 
ATOM   10787 C CG    . ARG A 1 2844 ? 190.285 193.135 164.354 1.00 27.23 ? 2844 ARG A CG    1 
ATOM   10788 C CD    . ARG A 1 2844 ? 189.440 191.869 164.347 1.00 27.08 ? 2844 ARG A CD    1 
ATOM   10789 N NE    . ARG A 1 2844 ? 188.650 191.706 165.560 1.00 30.95 ? 2844 ARG A NE    1 
ATOM   10790 C CZ    . ARG A 1 2844 ? 189.025 190.980 166.604 1.00 32.02 ? 2844 ARG A CZ    1 
ATOM   10791 N NH1   . ARG A 1 2844 ? 190.175 190.327 166.615 1.00 26.95 ? 2844 ARG A NH1   1 
ATOM   10792 N NH2   . ARG A 1 2844 ? 188.223 190.902 167.663 1.00 32.84 ? 2844 ARG A NH2   1 
ATOM   10793 N N     . TRP A 1 2845 ? 190.711 196.381 163.790 1.00 22.70 ? 2845 TRP A N     1 
ATOM   10794 C CA    . TRP A 1 2845 ? 189.990 197.642 163.654 1.00 23.07 ? 2845 TRP A CA    1 
ATOM   10795 C C     . TRP A 1 2845 ? 190.779 198.620 162.796 1.00 20.57 ? 2845 TRP A C     1 
ATOM   10796 O O     . TRP A 1 2845 ? 190.226 199.257 161.890 1.00 26.86 ? 2845 TRP A O     1 
ATOM   10797 C CB    . TRP A 1 2845 ? 189.727 198.234 165.039 1.00 23.65 ? 2845 TRP A CB    1 
ATOM   10798 C CG    . TRP A 1 2845 ? 189.093 199.595 165.045 1.00 25.13 ? 2845 TRP A CG    1 
ATOM   10799 C CD1   . TRP A 1 2845 ? 187.762 199.877 165.113 1.00 27.00 ? 2845 TRP A CD1   1 
ATOM   10800 C CD2   . TRP A 1 2845 ? 189.767 200.859 164.972 1.00 28.00 ? 2845 TRP A CD2   1 
ATOM   10801 N NE1   . TRP A 1 2845 ? 187.565 201.237 165.100 1.00 29.54 ? 2845 TRP A NE1   1 
ATOM   10802 C CE2   . TRP A 1 2845 ? 188.781 201.861 165.017 1.00 29.32 ? 2845 TRP A CE2   1 
ATOM   10803 C CE3   . TRP A 1 2845 ? 191.110 201.239 164.878 1.00 28.48 ? 2845 TRP A CE3   1 
ATOM   10804 C CZ2   . TRP A 1 2845 ? 189.092 203.217 164.956 1.00 27.51 ? 2845 TRP A CZ2   1 
ATOM   10805 C CZ3   . TRP A 1 2845 ? 191.417 202.585 164.829 1.00 25.09 ? 2845 TRP A CZ3   1 
ATOM   10806 C CH2   . TRP A 1 2845 ? 190.414 203.557 164.868 1.00 26.75 ? 2845 TRP A CH2   1 
ATOM   10807 N N     . THR A 1 2846 ? 192.084 198.733 163.058 1.00 18.38 ? 2846 THR A N     1 
ATOM   10808 C CA    . THR A 1 2846 ? 192.928 199.619 162.266 1.00 20.33 ? 2846 THR A CA    1 
ATOM   10809 C C     . THR A 1 2846 ? 192.960 199.190 160.805 1.00 19.57 ? 2846 THR A C     1 
ATOM   10810 O O     . THR A 1 2846 ? 192.866 200.030 159.907 1.00 25.07 ? 2846 THR A O     1 
ATOM   10811 C CB    . THR A 1 2846 ? 194.343 199.661 162.847 1.00 21.90 ? 2846 THR A CB    1 
ATOM   10812 O OG1   . THR A 1 2846 ? 194.349 200.466 164.031 1.00 20.34 ? 2846 THR A OG1   1 
ATOM   10813 C CG2   . THR A 1 2846 ? 195.324 200.247 161.844 1.00 19.03 ? 2846 THR A CG2   1 
ATOM   10814 N N     . ASP A 1 2847 ? 193.078 197.886 160.548 1.00 16.20 ? 2847 ASP A N     1 
ATOM   10815 C CA    . ASP A 1 2847 ? 193.114 197.399 159.170 1.00 22.57 ? 2847 ASP A CA    1 
ATOM   10816 C C     . ASP A 1 2847 ? 191.797 197.675 158.448 1.00 25.48 ? 2847 ASP A C     1 
ATOM   10817 O O     . ASP A 1 2847 ? 191.781 198.177 157.315 1.00 22.85 ? 2847 ASP A O     1 
ATOM   10818 C CB    . ASP A 1 2847 ? 193.434 195.905 159.153 1.00 26.59 ? 2847 ASP A CB    1 
ATOM   10819 C CG    . ASP A 1 2847 ? 194.919 195.629 159.093 1.00 23.12 ? 2847 ASP A CG    1 
ATOM   10820 O OD1   . ASP A 1 2847 ? 195.665 196.502 158.605 1.00 20.56 ? 2847 ASP A OD1   1 
ATOM   10821 O OD2   . ASP A 1 2847 ? 195.342 194.538 159.528 1.00 24.42 ? 2847 ASP A OD2   1 
ATOM   10822 N N     . GLU A 1 2848 ? 190.675 197.360 159.096 1.00 26.17 ? 2848 GLU A N     1 
ATOM   10823 C CA    . GLU A 1 2848 ? 189.378 197.589 158.474 1.00 22.74 ? 2848 GLU A CA    1 
ATOM   10824 C C     . GLU A 1 2848 ? 189.170 199.065 158.169 1.00 25.18 ? 2848 GLU A C     1 
ATOM   10825 O O     . GLU A 1 2848 ? 188.708 199.424 157.079 1.00 27.41 ? 2848 GLU A O     1 
ATOM   10826 C CB    . GLU A 1 2848 ? 188.264 197.067 159.379 1.00 22.84 ? 2848 GLU A CB    1 
ATOM   10827 C CG    . GLU A 1 2848 ? 186.872 197.224 158.797 1.00 28.26 ? 2848 GLU A CG    1 
ATOM   10828 C CD    . GLU A 1 2848 ? 185.800 196.657 159.701 1.00 32.33 ? 2848 GLU A CD    1 
ATOM   10829 O OE1   . GLU A 1 2848 ? 185.762 195.421 159.875 1.00 31.28 ? 2848 GLU A OE1   1 
ATOM   10830 O OE2   . GLU A 1 2848 ? 184.996 197.448 160.237 1.00 31.09 ? 2848 GLU A OE2   1 
ATOM   10831 N N     . ASN A 1 2849 ? 189.531 199.942 159.106 1.00 21.78 ? 2849 ASN A N     1 
ATOM   10832 C CA    . ASN A 1 2849 ? 189.245 201.355 158.896 1.00 21.05 ? 2849 ASN A CA    1 
ATOM   10833 C C     . ASN A 1 2849 ? 190.252 202.016 157.963 1.00 20.57 ? 2849 ASN A C     1 
ATOM   10834 O O     . ASN A 1 2849 ? 189.902 202.969 157.264 1.00 28.10 ? 2849 ASN A O     1 
ATOM   10835 C CB    . ASN A 1 2849 ? 189.150 202.077 160.233 1.00 19.96 ? 2849 ASN A CB    1 
ATOM   10836 C CG    . ASN A 1 2849 ? 187.899 201.696 160.988 1.00 22.40 ? 2849 ASN A CG    1 
ATOM   10837 O OD1   . ASN A 1 2849 ? 186.822 201.583 160.404 1.00 24.63 ? 2849 ASN A OD1   1 
ATOM   10838 N ND2   . ASN A 1 2849 ? 188.033 201.474 162.277 1.00 22.59 ? 2849 ASN A ND2   1 
ATOM   10839 N N     . ILE A 1 2850 ? 191.491 201.522 157.901 1.00 14.22 ? 2850 ILE A N     1 
ATOM   10840 C CA    . ILE A 1 2850 ? 192.402 202.031 156.880 1.00 13.67 ? 2850 ILE A CA    1 
ATOM   10841 C C     . ILE A 1 2850 ? 191.894 201.645 155.497 1.00 20.95 ? 2850 ILE A C     1 
ATOM   10842 O O     . ILE A 1 2850 ? 191.911 202.460 154.563 1.00 23.32 ? 2850 ILE A O     1 
ATOM   10843 C CB    . ILE A 1 2850 ? 193.848 201.554 157.127 1.00 14.63 ? 2850 ILE A CB    1 
ATOM   10844 C CG1   . ILE A 1 2850 ? 194.801 202.203 156.135 1.00 18.98 ? 2850 ILE A CG1   1 
ATOM   10845 C CG2   . ILE A 1 2850 ? 194.004 200.072 156.968 1.00 20.76 ? 2850 ILE A CG2   1 
ATOM   10846 C CD1   . ILE A 1 2850 ? 196.230 201.826 156.380 1.00 17.39 ? 2850 ILE A CD1   1 
ATOM   10847 N N     . ASP A 1 2851 ? 191.384 200.417 155.352 1.00 23.16 ? 2851 ASP A N     1 
ATOM   10848 C CA    . ASP A 1 2851 ? 190.777 200.033 154.083 1.00 22.63 ? 2851 ASP A CA    1 
ATOM   10849 C C     . ASP A 1 2851 ? 189.573 200.911 153.759 1.00 22.17 ? 2851 ASP A C     1 
ATOM   10850 O O     . ASP A 1 2851 ? 189.405 201.348 152.612 1.00 18.29 ? 2851 ASP A O     1 
ATOM   10851 C CB    . ASP A 1 2851 ? 190.372 198.562 154.117 1.00 24.25 ? 2851 ASP A CB    1 
ATOM   10852 C CG    . ASP A 1 2851 ? 191.544 197.634 153.897 1.00 26.42 ? 2851 ASP A CG    1 
ATOM   10853 O OD1   . ASP A 1 2851 ? 192.307 197.856 152.934 1.00 25.67 ? 2851 ASP A OD1   1 
ATOM   10854 O OD2   . ASP A 1 2851 ? 191.703 196.677 154.684 1.00 26.38 ? 2851 ASP A OD2   1 
ATOM   10855 N N     . THR A 1 2852 ? 188.726 201.188 154.755 1.00 19.79 ? 2852 THR A N     1 
ATOM   10856 C CA    . THR A 1 2852 ? 187.505 201.933 154.464 1.00 22.59 ? 2852 THR A CA    1 
ATOM   10857 C C     . THR A 1 2852 ? 187.807 203.395 154.142 1.00 22.83 ? 2852 THR A C     1 
ATOM   10858 O O     . THR A 1 2852 ? 187.155 203.982 153.273 1.00 29.13 ? 2852 THR A O     1 
ATOM   10859 C CB    . THR A 1 2852 ? 186.494 201.807 155.611 1.00 21.13 ? 2852 THR A CB    1 
ATOM   10860 O OG1   . THR A 1 2852 ? 185.189 202.147 155.126 1.00 24.59 ? 2852 THR A OG1   1 
ATOM   10861 C CG2   . THR A 1 2852 ? 186.819 202.737 156.759 1.00 19.22 ? 2852 THR A CG2   1 
ATOM   10862 N N     . VAL A 1 2853 ? 188.808 203.998 154.793 1.00 19.09 ? 2853 VAL A N     1 
ATOM   10863 C CA    . VAL A 1 2853 ? 189.145 205.377 154.453 1.00 17.55 ? 2853 VAL A CA    1 
ATOM   10864 C C     . VAL A 1 2853 ? 189.799 205.426 153.080 1.00 21.06 ? 2853 VAL A C     1 
ATOM   10865 O O     . VAL A 1 2853 ? 189.576 206.365 152.305 1.00 27.66 ? 2853 VAL A O     1 
ATOM   10866 C CB    . VAL A 1 2853 ? 190.040 206.027 155.527 1.00 18.26 ? 2853 VAL A CB    1 
ATOM   10867 C CG1   . VAL A 1 2853 ? 189.244 206.302 156.789 1.00 19.62 ? 2853 VAL A CG1   1 
ATOM   10868 C CG2   . VAL A 1 2853 ? 191.293 205.227 155.798 1.00 20.86 ? 2853 VAL A CG2   1 
ATOM   10869 N N     . ALA A 1 2854 ? 190.612 204.416 152.753 1.00 22.28 ? 2854 ALA A N     1 
ATOM   10870 C CA    . ALA A 1 2854 ? 191.209 204.355 151.425 1.00 21.16 ? 2854 ALA A CA    1 
ATOM   10871 C C     . ALA A 1 2854 ? 190.140 204.257 150.344 1.00 27.09 ? 2854 ALA A C     1 
ATOM   10872 O O     . ALA A 1 2854 ? 190.235 204.922 149.307 1.00 26.61 ? 2854 ALA A O     1 
ATOM   10873 C CB    . ALA A 1 2854 ? 192.172 203.172 151.344 1.00 22.97 ? 2854 ALA A CB    1 
ATOM   10874 N N     . LEU A 1 2855 ? 189.111 203.436 150.567 1.00 27.02 ? 2855 LEU A N     1 
ATOM   10875 C CA    . LEU A 1 2855 ? 188.071 203.306 149.550 1.00 26.63 ? 2855 LEU A CA    1 
ATOM   10876 C C     . LEU A 1 2855 ? 187.140 204.514 149.531 1.00 27.23 ? 2855 LEU A C     1 
ATOM   10877 O O     . LEU A 1 2855 ? 186.556 204.822 148.486 1.00 31.25 ? 2855 LEU A O     1 
ATOM   10878 C CB    . LEU A 1 2855 ? 187.280 202.009 149.750 1.00 25.48 ? 2855 LEU A CB    1 
ATOM   10879 C CG    . LEU A 1 2855 ? 186.482 201.733 151.027 1.00 26.14 ? 2855 LEU A CG    1 
ATOM   10880 C CD1   . LEU A 1 2855 ? 185.093 202.359 150.990 1.00 24.96 ? 2855 LEU A CD1   1 
ATOM   10881 C CD2   . LEU A 1 2855 ? 186.385 200.234 151.267 1.00 25.52 ? 2855 LEU A CD2   1 
ATOM   10882 N N     . LYS A 1 2856 ? 186.980 205.205 150.663 1.00 20.81 ? 2856 LYS A N     1 
ATOM   10883 C CA    . LYS A 1 2856 ? 186.113 206.379 150.689 1.00 20.97 ? 2856 LYS A CA    1 
ATOM   10884 C C     . LYS A 1 2856 ? 186.772 207.569 150.003 1.00 22.14 ? 2856 LYS A C     1 
ATOM   10885 O O     . LYS A 1 2856 ? 186.110 208.331 149.290 1.00 23.19 ? 2856 LYS A O     1 
ATOM   10886 C CB    . LYS A 1 2856 ? 185.738 206.727 152.130 1.00 21.18 ? 2856 LYS A CB    1 
ATOM   10887 C CG    . LYS A 1 2856 ? 184.625 207.756 152.239 1.00 26.22 ? 2856 LYS A CG    1 
ATOM   10888 C CD    . LYS A 1 2856 ? 184.068 207.836 153.652 1.00 25.82 ? 2856 LYS A CD    1 
ATOM   10889 C CE    . LYS A 1 2856 ? 185.103 208.373 154.625 1.00 23.00 ? 2856 LYS A CE    1 
ATOM   10890 N NZ    . LYS A 1 2856 ? 185.379 209.819 154.400 1.00 21.72 ? 2856 LYS A NZ    1 
ATOM   10891 N N     . HIS A 1 2857 ? 188.076 207.754 150.214 1.00 21.35 ? 2857 HIS A N     1 
ATOM   10892 C CA    . HIS A 1 2857 ? 188.766 208.878 149.593 1.00 20.23 ? 2857 HIS A CA    1 
ATOM   10893 C C     . HIS A 1 2857 ? 189.373 208.525 148.243 1.00 22.66 ? 2857 HIS A C     1 
ATOM   10894 O O     . HIS A 1 2857 ? 189.858 209.422 147.545 1.00 24.68 ? 2857 HIS A O     1 
ATOM   10895 C CB    . HIS A 1 2857 ? 189.848 209.414 150.531 1.00 16.47 ? 2857 HIS A CB    1 
ATOM   10896 C CG    . HIS A 1 2857 ? 189.313 210.294 151.616 1.00 17.02 ? 2857 HIS A CG    1 
ATOM   10897 N ND1   . HIS A 1 2857 ? 188.808 209.796 152.797 1.00 19.54 ? 2857 HIS A ND1   1 
ATOM   10898 C CD2   . HIS A 1 2857 ? 189.189 211.640 151.693 1.00 18.46 ? 2857 HIS A CD2   1 
ATOM   10899 C CE1   . HIS A 1 2857 ? 188.403 210.797 153.558 1.00 21.69 ? 2857 HIS A CE1   1 
ATOM   10900 N NE2   . HIS A 1 2857 ? 188.623 211.927 152.911 1.00 23.71 ? 2857 HIS A NE2   1 
ATOM   10901 N N     . PHE A 1 2858 ? 189.369 207.249 147.865 1.00 22.04 ? 2858 PHE A N     1 
ATOM   10902 C CA    . PHE A 1 2858 ? 189.815 206.802 146.546 1.00 26.07 ? 2858 PHE A CA    1 
ATOM   10903 C C     . PHE A 1 2858 ? 188.838 205.750 146.037 1.00 28.21 ? 2858 PHE A C     1 
ATOM   10904 O O     . PHE A 1 2858 ? 189.150 204.552 146.023 1.00 32.68 ? 2858 PHE A O     1 
ATOM   10905 C CB    . PHE A 1 2858 ? 191.242 206.255 146.599 1.00 23.66 ? 2858 PHE A CB    1 
ATOM   10906 C CG    . PHE A 1 2858 ? 192.254 207.239 147.114 1.00 21.34 ? 2858 PHE A CG    1 
ATOM   10907 C CD1   . PHE A 1 2858 ? 192.494 207.361 148.472 1.00 23.68 ? 2858 PHE A CD1   1 
ATOM   10908 C CD2   . PHE A 1 2858 ? 192.979 208.027 146.239 1.00 19.17 ? 2858 PHE A CD2   1 
ATOM   10909 C CE1   . PHE A 1 2858 ? 193.427 208.262 148.945 1.00 21.29 ? 2858 PHE A CE1   1 
ATOM   10910 C CE2   . PHE A 1 2858 ? 193.914 208.926 146.708 1.00 21.16 ? 2858 PHE A CE2   1 
ATOM   10911 C CZ    . PHE A 1 2858 ? 194.137 209.045 148.061 1.00 21.43 ? 2858 PHE A CZ    1 
ATOM   10912 N N     . PRO A 1 2859 ? 187.641 206.160 145.613 1.00 29.23 ? 2859 PRO A N     1 
ATOM   10913 C CA    . PRO A 1 2859 ? 186.621 205.198 145.184 1.00 30.64 ? 2859 PRO A CA    1 
ATOM   10914 C C     . PRO A 1 2859 ? 186.849 204.584 143.811 1.00 30.71 ? 2859 PRO A C     1 
ATOM   10915 O O     . PRO A 1 2859 ? 186.082 203.700 143.420 1.00 31.46 ? 2859 PRO A O     1 
ATOM   10916 C CB    . PRO A 1 2859 ? 185.360 206.085 145.181 1.00 31.33 ? 2859 PRO A CB    1 
ATOM   10917 C CG    . PRO A 1 2859 ? 185.701 207.074 146.269 1.00 29.92 ? 2859 PRO A CG    1 
ATOM   10918 C CD    . PRO A 1 2859 ? 187.013 207.483 145.695 1.00 29.65 ? 2859 PRO A CD    1 
ATOM   10919 N N     . ASN A 1 2860 ? 187.870 205.010 143.074 1.00 28.99 ? 2860 ASN A N     1 
ATOM   10920 C CA    . ASN A 1 2860 ? 188.089 204.586 141.693 1.00 31.32 ? 2860 ASN A CA    1 
ATOM   10921 C C     . ASN A 1 2860 ? 189.482 203.994 141.531 1.00 32.54 ? 2860 ASN A C     1 
ATOM   10922 O O     . ASN A 1 2860 ? 190.232 204.339 140.616 1.00 33.39 ? 2860 ASN A O     1 
ATOM   10923 C CB    . ASN A 1 2860 ? 187.882 205.751 140.729 1.00 29.08 ? 2860 ASN A CB    1 
ATOM   10924 C CG    . ASN A 1 2860 ? 186.512 206.386 140.867 1.00 32.62 ? 2860 ASN A CG    1 
ATOM   10925 O OD1   . ASN A 1 2860 ? 185.502 205.693 140.984 1.00 33.45 ? 2860 ASN A OD1   1 
ATOM   10926 N ND2   . ASN A 1 2860 ? 186.472 207.713 140.855 1.00 35.73 ? 2860 ASN A ND2   1 
ATOM   10927 N N     . ILE A 1 2861 ? 189.846 203.081 142.429 1.00 29.41 ? 2861 ILE A N     1 
ATOM   10928 C CA    . ILE A 1 2861 ? 191.164 202.464 142.420 1.00 28.51 ? 2861 ILE A CA    1 
ATOM   10929 C C     . ILE A 1 2861 ? 191.017 200.952 142.322 1.00 32.77 ? 2861 ILE A C     1 
ATOM   10930 O O     . ILE A 1 2861 ? 189.959 200.380 142.598 1.00 34.45 ? 2861 ILE A O     1 
ATOM   10931 C CB    . ILE A 1 2861 ? 191.994 202.845 143.663 1.00 27.27 ? 2861 ILE A CB    1 
ATOM   10932 C CG1   . ILE A 1 2861 ? 191.296 202.359 144.934 1.00 27.92 ? 2861 ILE A CG1   1 
ATOM   10933 C CG2   . ILE A 1 2861 ? 192.246 204.343 143.700 1.00 29.81 ? 2861 ILE A CG2   1 
ATOM   10934 C CD1   . ILE A 1 2861 ? 192.142 202.479 146.176 1.00 27.03 ? 2861 ILE A CD1   1 
ATOM   10935 N N     . ASP A 1 2862 ? 192.108 200.308 141.921 1.00 33.21 ? 2862 ASP A N     1 
ATOM   10936 C CA    . ASP A 1 2862 ? 192.159 198.865 141.753 1.00 30.44 ? 2862 ASP A CA    1 
ATOM   10937 C C     . ASP A 1 2862 ? 192.570 198.200 143.068 1.00 31.54 ? 2862 ASP A C     1 
ATOM   10938 O O     . ASP A 1 2862 ? 193.093 198.843 143.982 1.00 30.08 ? 2862 ASP A O     1 
ATOM   10939 C CB    . ASP A 1 2862 ? 193.130 198.514 140.618 1.00 32.72 ? 2862 ASP A CB    1 
ATOM   10940 C CG    . ASP A 1 2862 ? 193.409 197.026 140.506 1.00 35.96 ? 2862 ASP A CG    1 
ATOM   10941 O OD1   . ASP A 1 2862 ? 192.503 196.222 140.811 1.00 33.65 ? 2862 ASP A OD1   1 
ATOM   10942 O OD2   . ASP A 1 2862 ? 194.535 196.661 140.110 1.00 34.77 ? 2862 ASP A OD2   1 
ATOM   10943 N N     . ARG A 1 2863 ? 192.324 196.891 143.157 1.00 39.71 ? 2863 ARG A N     1 
ATOM   10944 C CA    . ARG A 1 2863 ? 192.690 196.112 144.336 1.00 38.98 ? 2863 ARG A CA    1 
ATOM   10945 C C     . ARG A 1 2863 ? 194.204 195.956 144.450 1.00 37.88 ? 2863 ARG A C     1 
ATOM   10946 O O     . ARG A 1 2863 ? 194.704 195.253 145.335 1.00 32.27 ? 2863 ARG A O     1 
ATOM   10947 C CB    . ARG A 1 2863 ? 191.995 194.745 144.302 1.00 37.53 ? 2863 ARG A CB    1 
ATOM   10948 C CG    . ARG A 1 2863 ? 191.911 194.034 145.652 1.00 36.74 ? 2863 ARG A CG    1 
ATOM   10949 C CD    . ARG A 1 2863 ? 191.343 194.927 146.753 1.00 37.63 ? 2863 ARG A CD    1 
ATOM   10950 N NE    . ARG A 1 2863 ? 190.241 195.769 146.299 1.00 40.51 ? 2863 ARG A NE    1 
ATOM   10951 C CZ    . ARG A 1 2863 ? 189.754 196.795 146.984 1.00 36.95 ? 2863 ARG A CZ    1 
ATOM   10952 N NH1   . ARG A 1 2863 ? 190.256 197.144 148.157 1.00 36.51 ? 2863 ARG A NH1   1 
ATOM   10953 N NH2   . ARG A 1 2863 ? 188.737 197.488 146.480 1.00 35.99 ? 2863 ARG A NH2   1 
ATOM   10954 N N     . GLU A 1 2864 ? 194.944 196.620 143.558 1.00 40.66 ? 2864 GLU A N     1 
ATOM   10955 C CA    . GLU A 1 2864 ? 196.382 196.776 143.730 1.00 36.68 ? 2864 GLU A CA    1 
ATOM   10956 C C     . GLU A 1 2864 ? 196.707 197.587 144.978 1.00 37.78 ? 2864 GLU A C     1 
ATOM   10957 O O     . GLU A 1 2864 ? 197.857 197.584 145.432 1.00 33.57 ? 2864 GLU A O     1 
ATOM   10958 C CB    . GLU A 1 2864 ? 196.972 197.448 142.484 1.00 33.31 ? 2864 GLU A CB    1 
ATOM   10959 C CG    . GLU A 1 2864 ? 198.493 197.427 142.363 1.00 34.99 ? 2864 GLU A CG    1 
ATOM   10960 C CD    . GLU A 1 2864 ? 199.087 196.040 142.510 1.00 40.27 ? 2864 GLU A CD    1 
ATOM   10961 O OE1   . GLU A 1 2864 ? 199.238 195.564 143.655 1.00 39.11 ? 2864 GLU A OE1   1 
ATOM   10962 O OE2   . GLU A 1 2864 ? 199.405 195.422 141.472 1.00 39.55 ? 2864 GLU A OE2   1 
ATOM   10963 N N     . LYS A 1 2865 ? 195.711 198.282 145.536 1.00 34.75 ? 2865 LYS A N     1 
ATOM   10964 C CA    . LYS A 1 2865 ? 195.921 199.105 146.723 1.00 29.61 ? 2865 LYS A CA    1 
ATOM   10965 C C     . LYS A 1 2865 ? 196.412 198.280 147.904 1.00 27.37 ? 2865 LYS A C     1 
ATOM   10966 O O     . LYS A 1 2865 ? 197.330 198.694 148.619 1.00 26.70 ? 2865 LYS A O     1 
ATOM   10967 C CB    . LYS A 1 2865 ? 194.619 199.822 147.088 1.00 31.19 ? 2865 LYS A CB    1 
ATOM   10968 C CG    . LYS A 1 2865 ? 194.704 200.721 148.316 1.00 29.47 ? 2865 LYS A CG    1 
ATOM   10969 C CD    . LYS A 1 2865 ? 194.273 200.018 149.604 1.00 29.84 ? 2865 LYS A CD    1 
ATOM   10970 C CE    . LYS A 1 2865 ? 192.779 199.753 149.632 1.00 29.71 ? 2865 LYS A CE    1 
ATOM   10971 N NZ    . LYS A 1 2865 ? 192.372 199.077 150.894 1.00 23.39 ? 2865 LYS A NZ    1 
ATOM   10972 N N     . ALA A 1 2866 ? 195.798 197.125 148.142 1.00 30.31 ? 2866 ALA A N     1 
ATOM   10973 C CA    . ALA A 1 2866 ? 196.100 196.327 149.323 1.00 31.43 ? 2866 ALA A CA    1 
ATOM   10974 C C     . ALA A 1 2866 ? 196.582 194.929 148.980 1.00 34.56 ? 2866 ALA A C     1 
ATOM   10975 O O     . ALA A 1 2866 ? 197.485 194.414 149.651 1.00 27.28 ? 2866 ALA A O     1 
ATOM   10976 C CB    . ALA A 1 2866 ? 194.865 196.248 150.234 1.00 27.90 ? 2866 ALA A CB    1 
ATOM   10977 N N     . MET A 1 2867 ? 196.010 194.309 147.943 1.00 35.80 ? 2867 MET A N     1 
ATOM   10978 C CA    . MET A 1 2867 ? 196.236 192.903 147.565 1.00 32.44 ? 2867 MET A CA    1 
ATOM   10979 C C     . MET A 1 2867 ? 196.251 192.076 148.852 1.00 34.67 ? 2867 MET A C     1 
ATOM   10980 O O     . MET A 1 2867 ? 195.362 192.263 149.694 1.00 34.66 ? 2867 MET A O     1 
ATOM   10981 C CB    . MET A 1 2867 ? 197.462 192.791 146.645 1.00 33.27 ? 2867 MET A CB    1 
ATOM   10982 C CG    . MET A 1 2867 ? 198.836 193.238 147.162 1.00 35.33 ? 2867 MET A CG    1 
ATOM   10983 S SD    . MET A 1 2867 ? 199.575 192.309 148.514 1.00 47.25 ? 2867 MET A SD    1 
ATOM   10984 C CE    . MET A 1 2867 ? 200.182 190.870 147.637 1.00 33.14 ? 2867 MET A CE    1 
ATOM   10985 N N     . SER A 1 2868 ? 197.197 191.165 149.047 1.00 37.90 ? 2868 SER A N     1 
ATOM   10986 C CA    . SER A 1 2868 ? 197.232 190.420 150.298 1.00 37.57 ? 2868 SER A CA    1 
ATOM   10987 C C     . SER A 1 2868 ? 197.545 191.370 151.450 1.00 34.10 ? 2868 SER A C     1 
ATOM   10988 O O     . SER A 1 2868 ? 198.391 192.260 151.325 1.00 27.43 ? 2868 SER A O     1 
ATOM   10989 C CB    . SER A 1 2868 ? 198.269 189.299 150.218 1.00 33.28 ? 2868 SER A CB    1 
ATOM   10990 O OG    . SER A 1 2868 ? 198.177 188.428 151.330 1.00 35.50 ? 2868 SER A OG    1 
ATOM   10991 N N     . ARG A 1 2869 ? 196.848 191.188 152.570 1.00 32.71 ? 2869 ARG A N     1 
ATOM   10992 C CA    . ARG A 1 2869 ? 196.998 192.044 153.744 1.00 32.83 ? 2869 ARG A CA    1 
ATOM   10993 C C     . ARG A 1 2869 ? 198.442 192.209 154.219 1.00 33.86 ? 2869 ARG A C     1 
ATOM   10994 O O     . ARG A 1 2869 ? 198.765 193.243 154.819 1.00 30.56 ? 2869 ARG A O     1 
ATOM   10995 C CB    . ARG A 1 2869 ? 196.128 191.522 154.891 1.00 29.95 ? 2869 ARG A CB    1 
ATOM   10996 C CG    . ARG A 1 2869 ? 194.640 191.818 154.731 1.00 29.94 ? 2869 ARG A CG    1 
ATOM   10997 C CD    . ARG A 1 2869 ? 194.400 193.259 154.290 1.00 29.53 ? 2869 ARG A CD    1 
ATOM   10998 N NE    . ARG A 1 2869 ? 195.180 194.217 155.066 1.00 30.63 ? 2869 ARG A NE    1 
ATOM   10999 C CZ    . ARG A 1 2869 ? 195.012 195.531 155.023 1.00 31.82 ? 2869 ARG A CZ    1 
ATOM   11000 N NH1   . ARG A 1 2869 ? 194.112 196.085 154.230 1.00 32.13 ? 2869 ARG A NH1   1 
ATOM   11001 N NH2   . ARG A 1 2869 ? 195.773 196.309 155.787 1.00 27.04 ? 2869 ARG A NH2   1 
ATOM   11002 N N     . PRO A 1 2870 ? 199.346 191.237 153.990 1.00 28.33 ? 2870 PRO A N     1 
ATOM   11003 C CA    . PRO A 1 2870 ? 200.763 191.501 154.269 1.00 27.33 ? 2870 PRO A CA    1 
ATOM   11004 C C     . PRO A 1 2870 ? 201.369 192.556 153.356 1.00 24.80 ? 2870 PRO A C     1 
ATOM   11005 O O     . PRO A 1 2870 ? 202.053 192.232 152.380 1.00 26.95 ? 2870 PRO A O     1 
ATOM   11006 C CB    . PRO A 1 2870 ? 201.420 190.133 154.059 1.00 25.37 ? 2870 PRO A CB    1 
ATOM   11007 C CG    . PRO A 1 2870 ? 200.368 189.175 154.405 1.00 28.56 ? 2870 PRO A CG    1 
ATOM   11008 C CD    . PRO A 1 2870 ? 199.089 189.785 153.919 1.00 26.44 ? 2870 PRO A CD    1 
ATOM   11009 N N     . ILE A 1 2871 ? 201.108 193.823 153.666 1.00 19.81 ? 2871 ILE A N     1 
ATOM   11010 C CA    . ILE A 1 2871 ? 201.757 194.945 152.993 1.00 20.75 ? 2871 ILE A CA    1 
ATOM   11011 C C     . ILE A 1 2871 ? 203.175 195.068 153.546 1.00 14.97 ? 2871 ILE A C     1 
ATOM   11012 O O     . ILE A 1 2871 ? 203.368 195.456 154.700 1.00 11.46 ? 2871 ILE A O     1 
ATOM   11013 C CB    . ILE A 1 2871 ? 200.971 196.246 153.193 1.00 19.18 ? 2871 ILE A CB    1 
ATOM   11014 C CG1   . ILE A 1 2871 ? 199.564 196.127 152.603 1.00 21.37 ? 2871 ILE A CG1   1 
ATOM   11015 C CG2   . ILE A 1 2871 ? 201.704 197.416 152.560 1.00 11.06 ? 2871 ILE A CG2   1 
ATOM   11016 C CD1   . ILE A 1 2871 ? 198.627 197.257 153.013 1.00 11.83 ? 2871 ILE A CD1   1 
ATOM   11017 N N     . LEU A 1 2872 ? 204.169 194.742 152.724 1.00 9.88  ? 2872 LEU A N     1 
ATOM   11018 C CA    . LEU A 1 2872 ? 205.571 194.776 153.117 1.00 10.08 ? 2872 LEU A CA    1 
ATOM   11019 C C     . LEU A 1 2872 ? 206.371 195.637 152.150 1.00 9.92  ? 2872 LEU A C     1 
ATOM   11020 O O     . LEU A 1 2872 ? 206.156 195.589 150.935 1.00 10.88 ? 2872 LEU A O     1 
ATOM   11021 C CB    . LEU A 1 2872 ? 206.173 193.356 153.189 1.00 13.41 ? 2872 LEU A CB    1 
ATOM   11022 C CG    . LEU A 1 2872 ? 205.864 192.478 154.409 1.00 14.07 ? 2872 LEU A CG    1 
ATOM   11023 C CD1   . LEU A 1 2872 ? 204.443 192.010 154.411 1.00 15.82 ? 2872 LEU A CD1   1 
ATOM   11024 C CD2   . LEU A 1 2872 ? 206.784 191.265 154.442 1.00 15.81 ? 2872 LEU A CD2   1 
ATOM   11025 N N     . TYR A 1 2873 ? 207.275 196.443 152.703 1.00 8.30  ? 2873 TYR A N     1 
ATOM   11026 C CA    . TYR A 1 2873 ? 208.239 197.225 151.938 1.00 7.71  ? 2873 TYR A CA    1 
ATOM   11027 C C     . TYR A 1 2873 ? 209.638 196.925 152.450 1.00 8.52  ? 2873 TYR A C     1 
ATOM   11028 O O     . TYR A 1 2873 ? 209.869 196.920 153.663 1.00 4.17  ? 2873 TYR A O     1 
ATOM   11029 C CB    . TYR A 1 2873 ? 207.957 198.728 152.037 1.00 9.95  ? 2873 TYR A CB    1 
ATOM   11030 C CG    . TYR A 1 2873 ? 206.895 199.226 151.089 1.00 6.12  ? 2873 TYR A CG    1 
ATOM   11031 C CD1   . TYR A 1 2873 ? 205.560 198.901 151.271 1.00 8.04  ? 2873 TYR A CD1   1 
ATOM   11032 C CD2   . TYR A 1 2873 ? 207.232 200.018 150.005 1.00 7.80  ? 2873 TYR A CD2   1 
ATOM   11033 C CE1   . TYR A 1 2873 ? 204.591 199.353 150.401 1.00 6.01  ? 2873 TYR A CE1   1 
ATOM   11034 C CE2   . TYR A 1 2873 ? 206.271 200.474 149.132 1.00 10.35 ? 2873 TYR A CE2   1 
ATOM   11035 C CZ    . TYR A 1 2873 ? 204.953 200.137 149.332 1.00 12.43 ? 2873 TYR A CZ    1 
ATOM   11036 O OH    . TYR A 1 2873 ? 203.995 200.588 148.459 1.00 17.64 ? 2873 TYR A OH    1 
ATOM   11037 N N     . SER A 1 2874 ? 210.566 196.673 151.527 1.00 11.65 ? 2874 SER A N     1 
ATOM   11038 C CA    . SER A 1 2874 ? 211.946 196.368 151.874 1.00 11.79 ? 2874 SER A CA    1 
ATOM   11039 C C     . SER A 1 2874 ? 212.869 196.864 150.773 1.00 12.42 ? 2874 SER A C     1 
ATOM   11040 O O     . SER A 1 2874 ? 212.491 196.894 149.600 1.00 17.67 ? 2874 SER A O     1 
ATOM   11041 C CB    . SER A 1 2874 ? 212.156 194.864 152.086 1.00 15.28 ? 2874 SER A CB    1 
ATOM   11042 O OG    . SER A 1 2874 ? 213.513 194.580 152.381 1.00 21.05 ? 2874 SER A OG    1 
ATOM   11043 N N     . ASN A 1 2875 ? 214.082 197.253 151.161 1.00 12.97 ? 2875 ASN A N     1 
ATOM   11044 C CA    . ASN A 1 2875 ? 215.112 197.677 150.225 1.00 16.12 ? 2875 ASN A CA    1 
ATOM   11045 C C     . ASN A 1 2875 ? 216.230 196.649 150.090 1.00 19.82 ? 2875 ASN A C     1 
ATOM   11046 O O     . ASN A 1 2875 ? 217.349 197.002 149.706 1.00 21.46 ? 2875 ASN A O     1 
ATOM   11047 C CB    . ASN A 1 2875 ? 215.680 199.031 150.650 1.00 17.67 ? 2875 ASN A CB    1 
ATOM   11048 C CG    . ASN A 1 2875 ? 216.299 198.990 152.028 1.00 21.51 ? 2875 ASN A CG    1 
ATOM   11049 O OD1   . ASN A 1 2875 ? 215.596 198.895 153.033 1.00 27.86 ? 2875 ASN A OD1   1 
ATOM   11050 N ND2   . ASN A 1 2875 ? 217.622 199.063 152.085 1.00 18.84 ? 2875 ASN A ND2   1 
ATOM   11051 N N     . TRP A 1 2876 ? 215.947 195.384 150.407 1.00 23.37 ? 2876 TRP A N     1 
ATOM   11052 C CA    . TRP A 1 2876 ? 216.957 194.337 150.306 1.00 15.06 ? 2876 TRP A CA    1 
ATOM   11053 C C     . TRP A 1 2876 ? 216.994 193.720 148.913 1.00 15.31 ? 2876 TRP A C     1 
ATOM   11054 O O     . TRP A 1 2876 ? 218.075 193.502 148.357 1.00 14.34 ? 2876 TRP A O     1 
ATOM   11055 C CB    . TRP A 1 2876 ? 216.688 193.254 151.350 1.00 12.07 ? 2876 TRP A CB    1 
ATOM   11056 C CG    . TRP A 1 2876 ? 216.906 193.698 152.759 1.00 14.48 ? 2876 TRP A CG    1 
ATOM   11057 C CD1   . TRP A 1 2876 ? 217.854 194.569 153.210 1.00 19.31 ? 2876 TRP A CD1   1 
ATOM   11058 C CD2   . TRP A 1 2876 ? 216.151 193.299 153.906 1.00 16.93 ? 2876 TRP A CD2   1 
ATOM   11059 N NE1   . TRP A 1 2876 ? 217.740 194.730 154.569 1.00 21.97 ? 2876 TRP A NE1   1 
ATOM   11060 C CE2   . TRP A 1 2876 ? 216.700 193.961 155.020 1.00 16.79 ? 2876 TRP A CE2   1 
ATOM   11061 C CE3   . TRP A 1 2876 ? 215.065 192.442 154.101 1.00 18.26 ? 2876 TRP A CE3   1 
ATOM   11062 C CZ2   . TRP A 1 2876 ? 216.199 193.794 156.306 1.00 14.24 ? 2876 TRP A CZ2   1 
ATOM   11063 C CZ3   . TRP A 1 2876 ? 214.570 192.278 155.379 1.00 14.82 ? 2876 TRP A CZ3   1 
ATOM   11064 C CH2   . TRP A 1 2876 ? 215.135 192.950 156.464 1.00 13.00 ? 2876 TRP A CH2   1 
ATOM   11065 N N     . LEU A 1 2877 ? 215.824 193.431 148.340 1.00 20.26 ? 2877 LEU A N     1 
ATOM   11066 C CA    . LEU A 1 2877 ? 215.774 192.764 147.043 1.00 23.43 ? 2877 LEU A CA    1 
ATOM   11067 C C     . LEU A 1 2877 ? 216.177 193.696 145.907 1.00 24.94 ? 2877 LEU A C     1 
ATOM   11068 O O     . LEU A 1 2877 ? 216.751 193.242 144.911 1.00 25.14 ? 2877 LEU A O     1 
ATOM   11069 C CB    . LEU A 1 2877 ? 214.374 192.201 146.796 1.00 22.44 ? 2877 LEU A CB    1 
ATOM   11070 C CG    . LEU A 1 2877 ? 213.986 190.918 147.536 1.00 20.34 ? 2877 LEU A CG    1 
ATOM   11071 C CD1   . LEU A 1 2877 ? 213.584 191.203 148.973 1.00 17.46 ? 2877 LEU A CD1   1 
ATOM   11072 C CD2   . LEU A 1 2877 ? 212.865 190.202 146.802 1.00 23.07 ? 2877 LEU A CD2   1 
ATOM   11073 N N     . SER A 1 2878 ? 215.890 194.990 146.034 1.00 28.66 ? 2878 SER A N     1 
ATOM   11074 C CA    . SER A 1 2878 ? 216.207 195.961 144.998 1.00 27.24 ? 2878 SER A CA    1 
ATOM   11075 C C     . SER A 1 2878 ? 216.914 197.152 145.628 1.00 24.90 ? 2878 SER A C     1 
ATOM   11076 O O     . SER A 1 2878 ? 216.942 197.310 146.851 1.00 26.84 ? 2878 SER A O     1 
ATOM   11077 C CB    . SER A 1 2878 ? 214.947 196.416 144.250 1.00 26.35 ? 2878 SER A CB    1 
ATOM   11078 O OG    . SER A 1 2878 ? 215.264 197.364 143.244 1.00 28.08 ? 2878 SER A OG    1 
ATOM   11079 N N     . LYS A 1 2879 ? 217.506 197.988 144.772 1.00 25.99 ? 2879 LYS A N     1 
ATOM   11080 C CA    . LYS A 1 2879 ? 218.180 199.189 145.255 1.00 27.85 ? 2879 LYS A CA    1 
ATOM   11081 C C     . LYS A 1 2879 ? 217.190 200.145 145.911 1.00 27.31 ? 2879 LYS A C     1 
ATOM   11082 O O     . LYS A 1 2879 ? 217.459 200.688 146.988 1.00 28.24 ? 2879 LYS A O     1 
ATOM   11083 C CB    . LYS A 1 2879 ? 218.915 199.869 144.096 1.00 29.20 ? 2879 LYS A CB    1 
ATOM   11084 C CG    . LYS A 1 2879 ? 219.148 201.373 144.238 1.00 31.71 ? 2879 LYS A CG    1 
ATOM   11085 C CD    . LYS A 1 2879 ? 220.033 201.725 145.429 1.00 29.95 ? 2879 LYS A CD    1 
ATOM   11086 C CE    . LYS A 1 2879 ? 220.019 203.221 145.696 1.00 30.11 ? 2879 LYS A CE    1 
ATOM   11087 N NZ    . LYS A 1 2879 ? 220.052 203.526 147.153 1.00 31.99 ? 2879 LYS A NZ    1 
ATOM   11088 N N     . ASP A 1 2880 ? 216.031 200.345 145.289 1.00 21.84 ? 2880 ASP A N     1 
ATOM   11089 C CA    . ASP A 1 2880 ? 215.037 201.263 145.820 1.00 20.30 ? 2880 ASP A CA    1 
ATOM   11090 C C     . ASP A 1 2880 ? 214.203 200.578 146.901 1.00 23.16 ? 2880 ASP A C     1 
ATOM   11091 O O     . ASP A 1 2880 ? 214.395 199.405 147.231 1.00 27.75 ? 2880 ASP A O     1 
ATOM   11092 C CB    . ASP A 1 2880 ? 214.155 201.797 144.694 1.00 20.46 ? 2880 ASP A CB    1 
ATOM   11093 C CG    . ASP A 1 2880 ? 213.748 200.718 143.714 1.00 26.17 ? 2880 ASP A CG    1 
ATOM   11094 O OD1   . ASP A 1 2880 ? 212.992 201.023 142.769 1.00 26.50 ? 2880 ASP A OD1   1 
ATOM   11095 O OD2   . ASP A 1 2880 ? 214.189 199.563 143.887 1.00 25.97 ? 2880 ASP A OD2   1 
ATOM   11096 N N     . TYR A 1 2881 ? 213.257 201.330 147.459 1.00 19.33 ? 2881 TYR A N     1 
ATOM   11097 C CA    . TYR A 1 2881 ? 212.405 200.852 148.547 1.00 13.57 ? 2881 TYR A CA    1 
ATOM   11098 C C     . TYR A 1 2881 ? 211.115 200.251 147.983 1.00 15.71 ? 2881 TYR A C     1 
ATOM   11099 O O     . TYR A 1 2881 ? 209.999 200.621 148.344 1.00 16.56 ? 2881 TYR A O     1 
ATOM   11100 C CB    . TYR A 1 2881 ? 212.126 201.996 149.515 1.00 13.25 ? 2881 TYR A CB    1 
ATOM   11101 C CG    . TYR A 1 2881 ? 211.549 201.591 150.849 1.00 13.12 ? 2881 TYR A CG    1 
ATOM   11102 C CD1   . TYR A 1 2881 ? 212.303 200.872 151.764 1.00 14.96 ? 2881 TYR A CD1   1 
ATOM   11103 C CD2   . TYR A 1 2881 ? 210.260 201.956 151.207 1.00 10.81 ? 2881 TYR A CD2   1 
ATOM   11104 C CE1   . TYR A 1 2881 ? 211.781 200.510 152.988 1.00 13.71 ? 2881 TYR A CE1   1 
ATOM   11105 C CE2   . TYR A 1 2881 ? 209.732 201.603 152.429 1.00 7.55  ? 2881 TYR A CE2   1 
ATOM   11106 C CZ    . TYR A 1 2881 ? 210.495 200.877 153.315 1.00 10.11 ? 2881 TYR A CZ    1 
ATOM   11107 O OH    . TYR A 1 2881 ? 209.969 200.522 154.534 1.00 12.82 ? 2881 TYR A OH    1 
ATOM   11108 N N     . ILE A 1 2882 ? 211.298 199.304 147.070 1.00 11.12 ? 2882 ILE A N     1 
ATOM   11109 C CA    . ILE A 1 2882 ? 210.171 198.661 146.382 1.00 9.62  ? 2882 ILE A CA    1 
ATOM   11110 C C     . ILE A 1 2882 ? 209.410 197.785 147.370 1.00 10.64 ? 2882 ILE A C     1 
ATOM   11111 O O     . ILE A 1 2882 ? 210.023 197.238 148.305 1.00 15.98 ? 2882 ILE A O     1 
ATOM   11112 C CB    . ILE A 1 2882 ? 210.684 197.842 145.189 1.00 13.15 ? 2882 ILE A CB    1 
ATOM   11113 C CG1   . ILE A 1 2882 ? 209.534 197.365 144.299 1.00 15.06 ? 2882 ILE A CG1   1 
ATOM   11114 C CG2   . ILE A 1 2882 ? 211.533 196.666 145.655 1.00 14.64 ? 2882 ILE A CG2   1 
ATOM   11115 C CD1   . ILE A 1 2882 ? 209.974 196.835 142.954 1.00 15.76 ? 2882 ILE A CD1   1 
ATOM   11116 N N     . PRO A 1 2883 ? 208.091 197.647 147.244 1.00 8.47  ? 2883 PRO A N     1 
ATOM   11117 C CA    . PRO A 1 2883 ? 207.387 196.624 148.024 1.00 6.40  ? 2883 PRO A CA    1 
ATOM   11118 C C     . PRO A 1 2883 ? 207.796 195.227 147.585 1.00 13.29 ? 2883 PRO A C     1 
ATOM   11119 O O     . PRO A 1 2883 ? 208.088 194.978 146.413 1.00 20.08 ? 2883 PRO A O     1 
ATOM   11120 C CB    . PRO A 1 2883 ? 205.909 196.894 147.721 1.00 8.36  ? 2883 PRO A CB    1 
ATOM   11121 C CG    . PRO A 1 2883 ? 205.913 197.660 146.447 1.00 13.78 ? 2883 PRO A CG    1 
ATOM   11122 C CD    . PRO A 1 2883 ? 207.157 198.488 146.479 1.00 14.06 ? 2883 PRO A CD    1 
ATOM   11123 N N     . VAL A 1 2884 ? 207.802 194.304 148.546 1.00 17.43 ? 2884 VAL A N     1 
ATOM   11124 C CA    . VAL A 1 2884 ? 208.281 192.949 148.316 1.00 19.31 ? 2884 VAL A CA    1 
ATOM   11125 C C     . VAL A 1 2884 ? 207.203 191.957 148.728 1.00 20.53 ? 2884 VAL A C     1 
ATOM   11126 O O     . VAL A 1 2884 ? 206.301 192.267 149.510 1.00 17.92 ? 2884 VAL A O     1 
ATOM   11127 C CB    . VAL A 1 2884 ? 209.595 192.656 149.074 1.00 17.60 ? 2884 VAL A CB    1 
ATOM   11128 C CG1   . VAL A 1 2884 ? 210.695 193.601 148.613 1.00 14.38 ? 2884 VAL A CG1   1 
ATOM   11129 C CG2   . VAL A 1 2884 ? 209.380 192.764 150.573 1.00 12.29 ? 2884 VAL A CG2   1 
ATOM   11130 N N     . ASP A 1 2885 ? 207.308 190.751 148.181 1.00 20.90 ? 2885 ASP A N     1 
ATOM   11131 C CA    . ASP A 1 2885 ? 206.356 189.686 148.449 1.00 15.10 ? 2885 ASP A CA    1 
ATOM   11132 C C     . ASP A 1 2885 ? 206.800 188.892 149.676 1.00 20.17 ? 2885 ASP A C     1 
ATOM   11133 O O     . ASP A 1 2885 ? 207.969 188.909 150.070 1.00 25.00 ? 2885 ASP A O     1 
ATOM   11134 C CB    . ASP A 1 2885 ? 206.224 188.774 147.224 1.00 15.68 ? 2885 ASP A CB    1 
ATOM   11135 C CG    . ASP A 1 2885 ? 205.108 187.745 147.360 1.00 25.34 ? 2885 ASP A CG    1 
ATOM   11136 O OD1   . ASP A 1 2885 ? 204.703 187.180 146.322 1.00 26.19 ? 2885 ASP A OD1   1 
ATOM   11137 O OD2   . ASP A 1 2885 ? 204.619 187.505 148.484 1.00 23.78 ? 2885 ASP A OD2   1 
ATOM   11138 N N     . GLN A 1 2886 ? 205.836 188.198 150.284 1.00 17.55 ? 2886 GLN A N     1 
ATOM   11139 C CA    . GLN A 1 2886 ? 206.111 187.427 151.493 1.00 16.10 ? 2886 GLN A CA    1 
ATOM   11140 C C     . GLN A 1 2886 ? 207.124 186.318 151.232 1.00 18.62 ? 2886 GLN A C     1 
ATOM   11141 O O     . GLN A 1 2886 ? 208.107 186.173 151.968 1.00 17.78 ? 2886 GLN A O     1 
ATOM   11142 C CB    . GLN A 1 2886 ? 204.807 186.840 152.034 1.00 18.57 ? 2886 GLN A CB    1 
ATOM   11143 C CG    . GLN A 1 2886 ? 204.912 186.218 153.412 1.00 10.41 ? 2886 GLN A CG    1 
ATOM   11144 C CD    . GLN A 1 2886 ? 204.914 187.247 154.516 1.00 13.50 ? 2886 GLN A CD    1 
ATOM   11145 O OE1   . GLN A 1 2886 ? 205.911 187.933 154.738 1.00 17.24 ? 2886 GLN A OE1   1 
ATOM   11146 N NE2   . GLN A 1 2886 ? 203.791 187.370 155.211 1.00 17.53 ? 2886 GLN A NE2   1 
ATOM   11147 N N     . GLU A 1 2887 ? 206.899 185.525 150.183 1.00 16.91 ? 2887 GLU A N     1 
ATOM   11148 C CA    . GLU A 1 2887 ? 207.731 184.348 149.953 1.00 13.48 ? 2887 GLU A CA    1 
ATOM   11149 C C     . GLU A 1 2887 ? 209.153 184.731 149.569 1.00 15.21 ? 2887 GLU A C     1 
ATOM   11150 O O     . GLU A 1 2887 ? 210.115 184.128 150.059 1.00 20.27 ? 2887 GLU A O     1 
ATOM   11151 C CB    . GLU A 1 2887 ? 207.101 183.465 148.877 1.00 19.55 ? 2887 GLU A CB    1 
ATOM   11152 C CG    . GLU A 1 2887 ? 205.589 183.309 148.993 1.00 18.79 ? 2887 GLU A CG    1 
ATOM   11153 C CD    . GLU A 1 2887 ? 205.157 182.473 150.188 1.00 19.50 ? 2887 GLU A CD    1 
ATOM   11154 O OE1   . GLU A 1 2887 ? 206.027 182.007 150.955 1.00 21.66 ? 2887 GLU A OE1   1 
ATOM   11155 O OE2   . GLU A 1 2887 ? 203.935 182.283 150.363 1.00 21.67 ? 2887 GLU A OE2   1 
ATOM   11156 N N     . GLU A 1 2888 ? 209.310 185.719 148.685 1.00 12.71 ? 2888 GLU A N     1 
ATOM   11157 C CA    . GLU A 1 2888 ? 210.649 186.133 148.282 1.00 14.84 ? 2888 GLU A CA    1 
ATOM   11158 C C     . GLU A 1 2888 ? 211.430 186.692 149.464 1.00 15.51 ? 2888 GLU A C     1 
ATOM   11159 O O     . GLU A 1 2888 ? 212.618 186.386 149.635 1.00 18.59 ? 2888 GLU A O     1 
ATOM   11160 C CB    . GLU A 1 2888 ? 210.570 187.162 147.155 1.00 14.34 ? 2888 GLU A CB    1 
ATOM   11161 C CG    . GLU A 1 2888 ? 209.693 186.746 145.988 1.00 15.35 ? 2888 GLU A CG    1 
ATOM   11162 C CD    . GLU A 1 2888 ? 209.356 187.908 145.074 1.00 22.15 ? 2888 GLU A CD    1 
ATOM   11163 O OE1   . GLU A 1 2888 ? 209.619 189.066 145.462 1.00 21.37 ? 2888 GLU A OE1   1 
ATOM   11164 O OE2   . GLU A 1 2888 ? 208.832 187.663 143.967 1.00 20.99 ? 2888 GLU A OE2   1 
ATOM   11165 N N     . LEU A 1 2889 ? 210.778 187.507 150.296 1.00 11.87 ? 2889 LEU A N     1 
ATOM   11166 C CA    . LEU A 1 2889 ? 211.454 188.032 151.476 1.00 14.74 ? 2889 LEU A CA    1 
ATOM   11167 C C     . LEU A 1 2889 ? 211.823 186.912 152.437 1.00 17.88 ? 2889 LEU A C     1 
ATOM   11168 O O     . LEU A 1 2889 ? 212.911 186.921 153.020 1.00 12.35 ? 2889 LEU A O     1 
ATOM   11169 C CB    . LEU A 1 2889 ? 210.584 189.068 152.185 1.00 16.04 ? 2889 LEU A CB    1 
ATOM   11170 C CG    . LEU A 1 2889 ? 211.173 189.449 153.545 1.00 12.66 ? 2889 LEU A CG    1 
ATOM   11171 C CD1   . LEU A 1 2889 ? 212.410 190.304 153.339 1.00 10.94 ? 2889 LEU A CD1   1 
ATOM   11172 C CD2   . LEU A 1 2889 ? 210.172 190.149 154.440 1.00 11.81 ? 2889 LEU A CD2   1 
ATOM   11173 N N     . ARG A 1 2890 ? 210.927 185.941 152.622 1.00 20.61 ? 2890 ARG A N     1 
ATOM   11174 C CA    . ARG A 1 2890 ? 211.224 184.823 153.512 1.00 13.53 ? 2890 ARG A CA    1 
ATOM   11175 C C     . ARG A 1 2890 ? 212.434 184.041 153.018 1.00 13.39 ? 2890 ARG A C     1 
ATOM   11176 O O     . ARG A 1 2890 ? 213.315 183.674 153.805 1.00 13.82 ? 2890 ARG A O     1 
ATOM   11177 C CB    . ARG A 1 2890 ? 210.004 183.911 153.627 1.00 11.34 ? 2890 ARG A CB    1 
ATOM   11178 C CG    . ARG A 1 2890 ? 210.078 182.919 154.770 1.00 9.59  ? 2890 ARG A CG    1 
ATOM   11179 C CD    . ARG A 1 2890 ? 208.755 182.198 154.958 1.00 7.48  ? 2890 ARG A CD    1 
ATOM   11180 N NE    . ARG A 1 2890 ? 207.965 182.769 156.042 1.00 12.26 ? 2890 ARG A NE    1 
ATOM   11181 C CZ    . ARG A 1 2890 ? 206.749 183.274 155.893 1.00 12.10 ? 2890 ARG A CZ    1 
ATOM   11182 N NH1   . ARG A 1 2890 ? 206.148 183.293 154.715 1.00 12.90 ? 2890 ARG A NH1   1 
ATOM   11183 N NH2   . ARG A 1 2890 ? 206.119 183.772 156.953 1.00 6.51  ? 2890 ARG A NH2   1 
ATOM   11184 N N     . ASP A 1 2891 ? 212.495 183.780 151.710 1.00 10.35 ? 2891 ASP A N     1 
ATOM   11185 C CA    . ASP A 1 2891 ? 213.641 183.068 151.151 1.00 10.27 ? 2891 ASP A CA    1 
ATOM   11186 C C     . ASP A 1 2891 ? 214.927 183.865 151.329 1.00 13.82 ? 2891 ASP A C     1 
ATOM   11187 O O     . ASP A 1 2891 ? 215.972 183.304 151.681 1.00 14.82 ? 2891 ASP A O     1 
ATOM   11188 C CB    . ASP A 1 2891 ? 213.402 182.755 149.674 1.00 16.60 ? 2891 ASP A CB    1 
ATOM   11189 C CG    . ASP A 1 2891 ? 212.088 182.038 149.435 1.00 18.90 ? 2891 ASP A CG    1 
ATOM   11190 O OD1   . ASP A 1 2891 ? 211.530 181.476 150.400 1.00 16.92 ? 2891 ASP A OD1   1 
ATOM   11191 O OD2   . ASP A 1 2891 ? 211.612 182.035 148.280 1.00 13.78 ? 2891 ASP A OD2   1 
ATOM   11192 N N     . TYR A 1 2892 ? 214.868 185.179 151.098 1.00 13.56 ? 2892 TYR A N     1 
ATOM   11193 C CA    . TYR A 1 2892 ? 216.046 186.016 151.307 1.00 16.22 ? 2892 TYR A CA    1 
ATOM   11194 C C     . TYR A 1 2892 ? 216.492 185.995 152.763 1.00 17.77 ? 2892 TYR A C     1 
ATOM   11195 O O     . TYR A 1 2892 ? 217.694 185.959 153.052 1.00 15.63 ? 2892 TYR A O     1 
ATOM   11196 C CB    . TYR A 1 2892 ? 215.761 187.448 150.857 1.00 17.88 ? 2892 TYR A CB    1 
ATOM   11197 C CG    . TYR A 1 2892 ? 216.938 188.382 151.030 1.00 14.84 ? 2892 TYR A CG    1 
ATOM   11198 C CD1   . TYR A 1 2892 ? 217.966 188.416 150.101 1.00 15.78 ? 2892 TYR A CD1   1 
ATOM   11199 C CD2   . TYR A 1 2892 ? 217.015 189.233 152.124 1.00 10.93 ? 2892 TYR A CD2   1 
ATOM   11200 C CE1   . TYR A 1 2892 ? 219.041 189.267 150.258 1.00 15.38 ? 2892 TYR A CE1   1 
ATOM   11201 C CE2   . TYR A 1 2892 ? 218.084 190.087 152.289 1.00 15.04 ? 2892 TYR A CE2   1 
ATOM   11202 C CZ    . TYR A 1 2892 ? 219.094 190.101 151.354 1.00 15.87 ? 2892 TYR A CZ    1 
ATOM   11203 O OH    . TYR A 1 2892 ? 220.162 190.952 151.516 1.00 15.23 ? 2892 TYR A OH    1 
ATOM   11204 N N     . VAL A 1 2893 ? 215.540 186.035 153.695 1.00 16.13 ? 2893 VAL A N     1 
ATOM   11205 C CA    . VAL A 1 2893 ? 215.893 186.068 155.108 1.00 12.71 ? 2893 VAL A CA    1 
ATOM   11206 C C     . VAL A 1 2893 ? 216.486 184.732 155.540 1.00 14.67 ? 2893 VAL A C     1 
ATOM   11207 O O     . VAL A 1 2893 ? 217.415 184.693 156.348 1.00 15.82 ? 2893 VAL A O     1 
ATOM   11208 C CB    . VAL A 1 2893 ? 214.676 186.472 155.961 1.00 12.43 ? 2893 VAL A CB    1 
ATOM   11209 C CG1   . VAL A 1 2893 ? 214.991 186.335 157.439 1.00 12.08 ? 2893 VAL A CG1   1 
ATOM   11210 C CG2   . VAL A 1 2893 ? 214.270 187.901 155.654 1.00 16.34 ? 2893 VAL A CG2   1 
ATOM   11211 N N     . LYS A 1 2894 ? 215.977 183.618 155.001 1.00 16.24 ? 2894 LYS A N     1 
ATOM   11212 C CA    . LYS A 1 2894 ? 216.624 182.329 155.249 1.00 14.57 ? 2894 LYS A CA    1 
ATOM   11213 C C     . LYS A 1 2894 ? 218.044 182.308 154.696 1.00 15.18 ? 2894 LYS A C     1 
ATOM   11214 O O     . LYS A 1 2894 ? 218.971 181.808 155.349 1.00 15.14 ? 2894 LYS A O     1 
ATOM   11215 C CB    . LYS A 1 2894 ? 215.816 181.183 154.637 1.00 13.68 ? 2894 LYS A CB    1 
ATOM   11216 C CG    . LYS A 1 2894 ? 214.378 181.077 155.093 1.00 15.95 ? 2894 LYS A CG    1 
ATOM   11217 C CD    . LYS A 1 2894 ? 213.695 179.873 154.461 1.00 16.36 ? 2894 LYS A CD    1 
ATOM   11218 C CE    . LYS A 1 2894 ? 212.193 179.898 154.687 1.00 16.11 ? 2894 LYS A CE    1 
ATOM   11219 N NZ    . LYS A 1 2894 ? 211.845 179.712 156.121 1.00 15.38 ? 2894 LYS A NZ    1 
ATOM   11220 N N     . ALA A 1 2895 ? 218.231 182.840 153.486 1.00 17.21 ? 2895 ALA A N     1 
ATOM   11221 C CA    . ALA A 1 2895 ? 219.561 182.860 152.887 1.00 17.61 ? 2895 ALA A CA    1 
ATOM   11222 C C     . ALA A 1 2895 ? 220.536 183.662 153.738 1.00 18.05 ? 2895 ALA A C     1 
ATOM   11223 O O     . ALA A 1 2895 ? 221.685 183.251 153.936 1.00 19.93 ? 2895 ALA A O     1 
ATOM   11224 C CB    . ALA A 1 2895 ? 219.490 183.426 151.470 1.00 16.82 ? 2895 ALA A CB    1 
ATOM   11225 N N     . ARG A 1 2896 ? 220.095 184.812 154.251 1.00 19.23 ? 2896 ARG A N     1 
ATOM   11226 C CA    . ARG A 1 2896 ? 220.968 185.612 155.104 1.00 20.41 ? 2896 ARG A CA    1 
ATOM   11227 C C     . ARG A 1 2896 ? 221.147 184.976 156.478 1.00 21.91 ? 2896 ARG A C     1 
ATOM   11228 O O     . ARG A 1 2896 ? 222.210 185.118 157.093 1.00 22.58 ? 2896 ARG A O     1 
ATOM   11229 C CB    . ARG A 1 2896 ? 220.420 187.032 155.240 1.00 14.25 ? 2896 ARG A CB    1 
ATOM   11230 C CG    . ARG A 1 2896 ? 220.198 187.729 153.913 1.00 16.01 ? 2896 ARG A CG    1 
ATOM   11231 C CD    . ARG A 1 2896 ? 221.499 188.238 153.327 1.00 17.53 ? 2896 ARG A CD    1 
ATOM   11232 N NE    . ARG A 1 2896 ? 222.176 189.176 154.213 1.00 20.70 ? 2896 ARG A NE    1 
ATOM   11233 C CZ    . ARG A 1 2896 ? 223.398 188.996 154.695 1.00 19.24 ? 2896 ARG A CZ    1 
ATOM   11234 N NH1   . ARG A 1 2896 ? 224.105 187.918 154.402 1.00 20.10 ? 2896 ARG A NH1   1 
ATOM   11235 N NH2   . ARG A 1 2896 ? 223.923 189.922 155.492 1.00 19.21 ? 2896 ARG A NH2   1 
ATOM   11236 N N     . LEU A 1 2897 ? 220.128 184.266 156.968 1.00 19.67 ? 2897 LEU A N     1 
ATOM   11237 C CA    . LEU A 1 2897 ? 220.235 183.586 158.251 1.00 20.10 ? 2897 LEU A CA    1 
ATOM   11238 C C     . LEU A 1 2897 ? 221.222 182.434 158.192 1.00 23.58 ? 2897 LEU A C     1 
ATOM   11239 O O     . LEU A 1 2897 ? 221.797 182.070 159.218 1.00 19.95 ? 2897 LEU A O     1 
ATOM   11240 C CB    . LEU A 1 2897 ? 218.867 183.074 158.697 1.00 20.57 ? 2897 LEU A CB    1 
ATOM   11241 C CG    . LEU A 1 2897 ? 218.046 183.972 159.620 1.00 15.65 ? 2897 LEU A CG    1 
ATOM   11242 C CD1   . LEU A 1 2897 ? 216.699 183.336 159.895 1.00 18.03 ? 2897 LEU A CD1   1 
ATOM   11243 C CD2   . LEU A 1 2897 ? 218.791 184.227 160.914 1.00 14.84 ? 2897 LEU A CD2   1 
ATOM   11244 N N     . LYS A 1 2898 ? 221.417 181.835 157.017 1.00 22.72 ? 2898 LYS A N     1 
ATOM   11245 C CA    . LYS A 1 2898 ? 222.469 180.830 156.886 1.00 21.43 ? 2898 LYS A CA    1 
ATOM   11246 C C     . LYS A 1 2898 ? 223.827 181.414 157.268 1.00 23.31 ? 2898 LYS A C     1 
ATOM   11247 O O     . LYS A 1 2898 ? 224.542 180.863 158.117 1.00 24.95 ? 2898 LYS A O     1 
ATOM   11248 C CB    . LYS A 1 2898 ? 222.505 180.277 155.461 1.00 20.17 ? 2898 LYS A CB    1 
ATOM   11249 C CG    . LYS A 1 2898 ? 221.551 179.121 155.202 1.00 19.64 ? 2898 LYS A CG    1 
ATOM   11250 C CD    . LYS A 1 2898 ? 220.950 179.202 153.807 1.00 21.82 ? 2898 LYS A CD    1 
ATOM   11251 C CE    . LYS A 1 2898 ? 219.664 178.402 153.706 1.00 22.49 ? 2898 LYS A CE    1 
ATOM   11252 N NZ    . LYS A 1 2898 ? 218.864 178.787 152.510 1.00 20.33 ? 2898 LYS A NZ    1 
ATOM   11253 N N     . VAL A 1 2899 ? 224.187 182.549 156.666 1.00 22.04 ? 2899 VAL A N     1 
ATOM   11254 C CA    . VAL A 1 2899 ? 225.464 183.186 156.975 1.00 23.12 ? 2899 VAL A CA    1 
ATOM   11255 C C     . VAL A 1 2899 ? 225.467 183.707 158.407 1.00 25.54 ? 2899 VAL A C     1 
ATOM   11256 O O     . VAL A 1 2899 ? 226.497 183.678 159.091 1.00 26.67 ? 2899 VAL A O     1 
ATOM   11257 C CB    . VAL A 1 2899 ? 225.762 184.302 155.955 1.00 22.71 ? 2899 VAL A CB    1 
ATOM   11258 C CG1   . VAL A 1 2899 ? 226.883 185.204 156.445 1.00 19.52 ? 2899 VAL A CG1   1 
ATOM   11259 C CG2   . VAL A 1 2899 ? 226.112 183.702 154.602 1.00 24.62 ? 2899 VAL A CG2   1 
ATOM   11260 N N     . PHE A 1 2900 ? 224.316 184.189 158.885 1.00 24.13 ? 2900 PHE A N     1 
ATOM   11261 C CA    . PHE A 1 2900 ? 224.225 184.657 160.266 1.00 22.92 ? 2900 PHE A CA    1 
ATOM   11262 C C     . PHE A 1 2900 ? 224.512 183.530 161.252 1.00 26.36 ? 2900 PHE A C     1 
ATOM   11263 O O     . PHE A 1 2900 ? 225.244 183.724 162.228 1.00 27.23 ? 2900 PHE A O     1 
ATOM   11264 C CB    . PHE A 1 2900 ? 222.843 185.264 160.512 1.00 25.48 ? 2900 PHE A CB    1 
ATOM   11265 C CG    . PHE A 1 2900 ? 222.642 185.786 161.905 1.00 22.94 ? 2900 PHE A CG    1 
ATOM   11266 C CD1   . PHE A 1 2900 ? 223.378 186.861 162.370 1.00 25.13 ? 2900 PHE A CD1   1 
ATOM   11267 C CD2   . PHE A 1 2900 ? 221.690 185.224 162.738 1.00 22.17 ? 2900 PHE A CD2   1 
ATOM   11268 C CE1   . PHE A 1 2900 ? 223.186 187.348 163.648 1.00 25.70 ? 2900 PHE A CE1   1 
ATOM   11269 C CE2   . PHE A 1 2900 ? 221.492 185.709 164.015 1.00 23.35 ? 2900 PHE A CE2   1 
ATOM   11270 C CZ    . PHE A 1 2900 ? 222.241 186.773 164.470 1.00 22.12 ? 2900 PHE A CZ    1 
ATOM   11271 N N     . TYR A 1 2901 ? 223.951 182.343 161.006 1.00 27.87 ? 2901 TYR A N     1 
ATOM   11272 C CA    . TYR A 1 2901 ? 224.260 181.176 161.824 1.00 28.57 ? 2901 TYR A CA    1 
ATOM   11273 C C     . TYR A 1 2901 ? 225.733 180.819 161.723 1.00 29.08 ? 2901 TYR A C     1 
ATOM   11274 O O     . TYR A 1 2901 ? 226.375 180.509 162.734 1.00 24.71 ? 2901 TYR A O     1 
ATOM   11275 C CB    . TYR A 1 2901 ? 223.408 179.982 161.391 1.00 27.64 ? 2901 TYR A CB    1 
ATOM   11276 C CG    . TYR A 1 2901 ? 221.923 180.122 161.632 1.00 28.11 ? 2901 TYR A CG    1 
ATOM   11277 C CD1   . TYR A 1 2901 ? 221.426 181.044 162.541 1.00 27.08 ? 2901 TYR A CD1   1 
ATOM   11278 C CD2   . TYR A 1 2901 ? 221.017 179.319 160.952 1.00 26.61 ? 2901 TYR A CD2   1 
ATOM   11279 C CE1   . TYR A 1 2901 ? 220.068 181.166 162.761 1.00 25.72 ? 2901 TYR A CE1   1 
ATOM   11280 C CE2   . TYR A 1 2901 ? 219.658 179.433 161.165 1.00 25.78 ? 2901 TYR A CE2   1 
ATOM   11281 C CZ    . TYR A 1 2901 ? 219.189 180.358 162.070 1.00 27.44 ? 2901 TYR A CZ    1 
ATOM   11282 O OH    . TYR A 1 2901 ? 217.836 180.474 162.285 1.00 31.90 ? 2901 TYR A OH    1 
ATOM   11283 N N     . GLU A 1 2902 ? 226.283 180.849 160.506 1.00 31.66 ? 2902 GLU A N     1 
ATOM   11284 C CA    . GLU A 1 2902 ? 227.705 180.567 160.331 1.00 30.76 ? 2902 GLU A CA    1 
ATOM   11285 C C     . GLU A 1 2902 ? 228.554 181.498 161.186 1.00 32.54 ? 2902 GLU A C     1 
ATOM   11286 O O     . GLU A 1 2902 ? 229.556 181.076 161.775 1.00 32.36 ? 2902 GLU A O     1 
ATOM   11287 C CB    . GLU A 1 2902 ? 228.080 180.684 158.851 1.00 29.44 ? 2902 GLU A CB    1 
ATOM   11288 C CG    . GLU A 1 2902 ? 229.540 180.380 158.521 1.00 30.18 ? 2902 GLU A CG    1 
ATOM   11289 C CD    . GLU A 1 2902 ? 230.456 181.577 158.700 1.00 34.07 ? 2902 GLU A CD    1 
ATOM   11290 O OE1   . GLU A 1 2902 ? 231.392 181.494 159.522 1.00 34.98 ? 2902 GLU A OE1   1 
ATOM   11291 O OE2   . GLU A 1 2902 ? 230.244 182.599 158.014 1.00 33.93 ? 2902 GLU A OE2   1 
ATOM   11292 N N     . GLU A 1 2903 ? 228.165 182.772 161.266 1.00 33.36 ? 2903 GLU A N     1 
ATOM   11293 C CA    . GLU A 1 2903 ? 228.880 183.719 162.114 1.00 34.08 ? 2903 GLU A CA    1 
ATOM   11294 C C     . GLU A 1 2903 ? 228.706 183.387 163.592 1.00 39.47 ? 2903 GLU A C     1 
ATOM   11295 O O     . GLU A 1 2903 ? 229.689 183.279 164.334 1.00 41.57 ? 2903 GLU A O     1 
ATOM   11296 C CB    . GLU A 1 2903 ? 228.398 185.140 161.827 1.00 34.31 ? 2903 GLU A CB    1 
ATOM   11297 C CG    . GLU A 1 2903 ? 228.985 186.186 162.755 1.00 37.42 ? 2903 GLU A CG    1 
ATOM   11298 C CD    . GLU A 1 2903 ? 228.230 187.496 162.700 1.00 39.13 ? 2903 GLU A CD    1 
ATOM   11299 O OE1   . GLU A 1 2903 ? 227.194 187.554 162.005 1.00 38.29 ? 2903 GLU A OE1   1 
ATOM   11300 O OE2   . GLU A 1 2903 ? 228.668 188.466 163.353 1.00 37.12 ? 2903 GLU A OE2   1 
ATOM   11301 N N     . GLU A 1 2904 ? 227.463 183.209 164.035 1.00 43.56 ? 2904 GLU A N     1 
ATOM   11302 C CA    . GLU A 1 2904 ? 227.165 183.039 165.453 1.00 43.78 ? 2904 GLU A CA    1 
ATOM   11303 C C     . GLU A 1 2904 ? 225.715 182.597 165.601 1.00 43.84 ? 2904 GLU A C     1 
ATOM   11304 O O     . GLU A 1 2904 ? 224.919 182.688 164.664 1.00 41.53 ? 2904 GLU A O     1 
ATOM   11305 C CB    . GLU A 1 2904 ? 227.416 184.333 166.231 1.00 39.22 ? 2904 GLU A CB    1 
ATOM   11306 C CG    . GLU A 1 2904 ? 226.654 185.528 165.685 1.00 35.98 ? 2904 GLU A CG    1 
ATOM   11307 C CD    . GLU A 1 2904 ? 227.198 186.848 166.189 1.00 44.28 ? 2904 GLU A CD    1 
ATOM   11308 O OE1   . GLU A 1 2904 ? 228.305 186.854 166.767 1.00 44.09 ? 2904 GLU A OE1   1 
ATOM   11309 O OE2   . GLU A 1 2904 ? 226.520 187.880 166.005 1.00 45.39 ? 2904 GLU A OE2   1 
ATOM   11310 N N     . LEU A 1 2905 ? 225.384 182.123 166.800 1.00 41.97 ? 2905 LEU A N     1 
ATOM   11311 C CA    . LEU A 1 2905 ? 224.023 181.720 167.152 1.00 39.24 ? 2905 LEU A CA    1 
ATOM   11312 C C     . LEU A 1 2905 ? 223.499 180.638 166.208 1.00 38.60 ? 2905 LEU A C     1 
ATOM   11313 O O     . LEU A 1 2905 ? 222.582 180.853 165.414 1.00 40.26 ? 2905 LEU A O     1 
ATOM   11314 C CB    . LEU A 1 2905 ? 223.079 182.924 167.180 1.00 38.66 ? 2905 LEU A CB    1 
ATOM   11315 C CG    . LEU A 1 2905 ? 223.327 183.980 168.256 1.00 38.01 ? 2905 LEU A CG    1 
ATOM   11316 C CD1   . LEU A 1 2905 ? 222.391 185.154 168.055 1.00 39.65 ? 2905 LEU A CD1   1 
ATOM   11317 C CD2   . LEU A 1 2905 ? 223.146 183.383 169.639 1.00 37.60 ? 2905 LEU A CD2   1 
ATOM   11318 N N     . ASP A 1 2906 ? 224.107 179.454 166.306 1.00 34.85 ? 2906 ASP A N     1 
ATOM   11319 C CA    . ASP A 1 2906 ? 223.643 178.301 165.540 1.00 36.94 ? 2906 ASP A CA    1 
ATOM   11320 C C     . ASP A 1 2906 ? 222.231 177.862 165.911 1.00 37.74 ? 2906 ASP A C     1 
ATOM   11321 O O     . ASP A 1 2906 ? 221.721 176.919 165.294 1.00 37.80 ? 2906 ASP A O     1 
ATOM   11322 C CB    . ASP A 1 2906 ? 224.604 177.124 165.724 1.00 39.24 ? 2906 ASP A CB    1 
ATOM   11323 C CG    . ASP A 1 2906 ? 225.943 177.352 165.054 1.00 40.42 ? 2906 ASP A CG    1 
ATOM   11324 O OD1   . ASP A 1 2906 ? 225.985 178.077 164.040 1.00 37.28 ? 2906 ASP A OD1   1 
ATOM   11325 O OD2   . ASP A 1 2906 ? 226.954 176.803 165.540 1.00 40.76 ? 2906 ASP A OD2   1 
ATOM   11326 N N     . VAL A 1 2907 ? 221.597 178.503 166.889 1.00 28.99 ? 2907 VAL A N     1 
ATOM   11327 C CA    . VAL A 1 2907 ? 220.234 178.124 167.275 1.00 26.43 ? 2907 VAL A CA    1 
ATOM   11328 C C     . VAL A 1 2907 ? 219.284 178.399 166.114 1.00 26.79 ? 2907 VAL A C     1 
ATOM   11329 O O     . VAL A 1 2907 ? 219.395 179.451 165.454 1.00 30.05 ? 2907 VAL A O     1 
ATOM   11330 C CB    . VAL A 1 2907 ? 219.801 178.881 168.544 1.00 25.36 ? 2907 VAL A CB    1 
ATOM   11331 C CG1   . VAL A 1 2907 ? 220.706 178.515 169.706 1.00 29.81 ? 2907 VAL A CG1   1 
ATOM   11332 C CG2   . VAL A 1 2907 ? 219.840 180.385 168.317 1.00 22.21 ? 2907 VAL A CG2   1 
ATOM   11333 N N     . PRO A 1 2908 ? 218.367 177.489 165.793 1.00 20.31 ? 2908 PRO A N     1 
ATOM   11334 C CA    . PRO A 1 2908 ? 217.448 177.738 164.678 1.00 17.98 ? 2908 PRO A CA    1 
ATOM   11335 C C     . PRO A 1 2908 ? 216.406 178.783 165.038 1.00 17.42 ? 2908 PRO A C     1 
ATOM   11336 O O     . PRO A 1 2908 ? 215.912 178.833 166.167 1.00 20.79 ? 2908 PRO A O     1 
ATOM   11337 C CB    . PRO A 1 2908 ? 216.806 176.368 164.437 1.00 19.53 ? 2908 PRO A CB    1 
ATOM   11338 C CG    . PRO A 1 2908 ? 216.881 175.693 165.762 1.00 20.69 ? 2908 PRO A CG    1 
ATOM   11339 C CD    . PRO A 1 2908 ? 218.164 176.160 166.394 1.00 20.15 ? 2908 PRO A CD    1 
ATOM   11340 N N     . LEU A 1 2909 ? 216.073 179.621 164.058 1.00 11.05 ? 2909 LEU A N     1 
ATOM   11341 C CA    . LEU A 1 2909 ? 214.996 180.604 164.173 1.00 4.69  ? 2909 LEU A CA    1 
ATOM   11342 C C     . LEU A 1 2909 ? 214.017 180.344 163.035 1.00 5.16  ? 2909 LEU A C     1 
ATOM   11343 O O     . LEU A 1 2909 ? 214.352 180.546 161.865 1.00 8.32  ? 2909 LEU A O     1 
ATOM   11344 C CB    . LEU A 1 2909 ? 215.527 182.034 164.120 1.00 8.44  ? 2909 LEU A CB    1 
ATOM   11345 C CG    . LEU A 1 2909 ? 216.699 182.459 165.003 1.00 15.41 ? 2909 LEU A CG    1 
ATOM   11346 C CD1   . LEU A 1 2909 ? 216.825 183.969 164.984 1.00 15.88 ? 2909 LEU A CD1   1 
ATOM   11347 C CD2   . LEU A 1 2909 ? 216.517 181.973 166.428 1.00 13.06 ? 2909 LEU A CD2   1 
ATOM   11348 N N     . VAL A 1 2910 ? 212.810 179.892 163.371 1.00 7.28  ? 2910 VAL A N     1 
ATOM   11349 C CA    . VAL A 1 2910 ? 211.794 179.680 162.350 1.00 7.52  ? 2910 VAL A CA    1 
ATOM   11350 C C     . VAL A 1 2910 ? 211.215 181.025 161.937 1.00 8.29  ? 2910 VAL A C     1 
ATOM   11351 O O     . VAL A 1 2910 ? 210.966 181.901 162.776 1.00 8.07  ? 2910 VAL A O     1 
ATOM   11352 C CB    . VAL A 1 2910 ? 210.702 178.726 162.855 1.00 4.77  ? 2910 VAL A CB    1 
ATOM   11353 C CG1   . VAL A 1 2910 ? 211.300 177.378 163.175 1.00 8.09  ? 2910 VAL A CG1   1 
ATOM   11354 C CG2   . VAL A 1 2910 ? 210.015 179.295 164.064 1.00 5.57  ? 2910 VAL A CG2   1 
ATOM   11355 N N     . LEU A 1 2911 ? 211.017 181.206 160.638 1.00 8.65  ? 2911 LEU A N     1 
ATOM   11356 C CA    . LEU A 1 2911 ? 210.534 182.471 160.103 1.00 5.38  ? 2911 LEU A CA    1 
ATOM   11357 C C     . LEU A 1 2911 ? 209.047 182.354 159.807 1.00 7.10  ? 2911 LEU A C     1 
ATOM   11358 O O     . LEU A 1 2911 ? 208.654 181.894 158.731 1.00 15.67 ? 2911 LEU A O     1 
ATOM   11359 C CB    . LEU A 1 2911 ? 211.315 182.854 158.851 1.00 4.57  ? 2911 LEU A CB    1 
ATOM   11360 C CG    . LEU A 1 2911 ? 212.822 182.944 159.065 1.00 4.99  ? 2911 LEU A CG    1 
ATOM   11361 C CD1   . LEU A 1 2911 ? 213.513 183.196 157.754 1.00 8.58  ? 2911 LEU A CD1   1 
ATOM   11362 C CD2   . LEU A 1 2911 ? 213.139 184.043 160.056 1.00 4.01  ? 2911 LEU A CD2   1 
ATOM   11363 N N     . PHE A 1 2912 ? 208.223 182.776 160.754 1.00 1.53  ? 2912 PHE A N     1 
ATOM   11364 C CA    . PHE A 1 2912 ? 206.802 182.954 160.520 1.00 7.33  ? 2912 PHE A CA    1 
ATOM   11365 C C     . PHE A 1 2912 ? 206.536 184.423 160.207 1.00 14.05 ? 2912 PHE A C     1 
ATOM   11366 O O     . PHE A 1 2912 ? 207.446 185.256 160.208 1.00 14.20 ? 2912 PHE A O     1 
ATOM   11367 C CB    . PHE A 1 2912 ? 205.972 182.451 161.707 1.00 5.18  ? 2912 PHE A CB    1 
ATOM   11368 C CG    . PHE A 1 2912 ? 206.521 182.825 163.056 1.00 7.33  ? 2912 PHE A CG    1 
ATOM   11369 C CD1   . PHE A 1 2912 ? 205.999 183.894 163.760 1.00 9.44  ? 2912 PHE A CD1   1 
ATOM   11370 C CD2   . PHE A 1 2912 ? 207.521 182.069 163.646 1.00 10.69 ? 2912 PHE A CD2   1 
ATOM   11371 C CE1   . PHE A 1 2912 ? 206.493 184.228 165.005 1.00 7.35  ? 2912 PHE A CE1   1 
ATOM   11372 C CE2   . PHE A 1 2912 ? 208.017 182.397 164.892 1.00 2.81  ? 2912 PHE A CE2   1 
ATOM   11373 C CZ    . PHE A 1 2912 ? 207.499 183.474 165.573 1.00 5.26  ? 2912 PHE A CZ    1 
ATOM   11374 N N     . ASN A 1 2913 ? 205.269 184.731 159.922 1.00 13.43 ? 2913 ASN A N     1 
ATOM   11375 C CA    . ASN A 1 2913 ? 204.927 186.041 159.378 1.00 9.25  ? 2913 ASN A CA    1 
ATOM   11376 C C     . ASN A 1 2913 ? 205.327 187.164 160.328 1.00 7.48  ? 2913 ASN A C     1 
ATOM   11377 O O     . ASN A 1 2913 ? 205.873 188.189 159.896 1.00 12.15 ? 2913 ASN A O     1 
ATOM   11378 C CB    . ASN A 1 2913 ? 203.430 186.098 159.078 1.00 6.67  ? 2913 ASN A CB    1 
ATOM   11379 C CG    . ASN A 1 2913 ? 202.989 185.008 158.126 1.00 7.12  ? 2913 ASN A CG    1 
ATOM   11380 O OD1   . ASN A 1 2913 ? 203.815 184.326 157.522 1.00 12.81 ? 2913 ASN A OD1   1 
ATOM   11381 N ND2   . ASN A 1 2913 ? 201.682 184.833 157.992 1.00 9.31  ? 2913 ASN A ND2   1 
ATOM   11382 N N     . GLU A 1 2914 ? 205.075 186.983 161.625 1.00 3.83  ? 2914 GLU A N     1 
ATOM   11383 C CA    . GLU A 1 2914 ? 205.366 188.035 162.592 1.00 7.84  ? 2914 GLU A CA    1 
ATOM   11384 C C     . GLU A 1 2914 ? 206.861 188.310 162.672 1.00 7.77  ? 2914 GLU A C     1 
ATOM   11385 O O     . GLU A 1 2914 ? 207.280 189.452 162.884 1.00 16.97 ? 2914 GLU A O     1 
ATOM   11386 C CB    . GLU A 1 2914 ? 204.806 187.654 163.961 1.00 11.34 ? 2914 GLU A CB    1 
ATOM   11387 C CG    . GLU A 1 2914 ? 203.311 187.886 164.095 1.00 7.41  ? 2914 GLU A CG    1 
ATOM   11388 C CD    . GLU A 1 2914 ? 202.490 186.718 163.585 1.00 9.55  ? 2914 GLU A CD    1 
ATOM   11389 O OE1   . GLU A 1 2914 ? 201.263 186.706 163.820 1.00 14.40 ? 2914 GLU A OE1   1 
ATOM   11390 O OE2   . GLU A 1 2914 ? 203.068 185.812 162.950 1.00 4.51  ? 2914 GLU A OE2   1 
ATOM   11391 N N     . VAL A 1 2915 ? 207.685 187.275 162.498 1.00 5.42  ? 2915 VAL A N     1 
ATOM   11392 C CA    . VAL A 1 2915 ? 209.132 187.472 162.528 1.00 6.25  ? 2915 VAL A CA    1 
ATOM   11393 C C     . VAL A 1 2915 ? 209.572 188.354 161.368 1.00 7.59  ? 2915 VAL A C     1 
ATOM   11394 O O     . VAL A 1 2915 ? 210.368 189.284 161.540 1.00 11.25 ? 2915 VAL A O     1 
ATOM   11395 C CB    . VAL A 1 2915 ? 209.863 186.120 162.517 1.00 2.70  ? 2915 VAL A CB    1 
ATOM   11396 C CG1   . VAL A 1 2915 ? 211.336 186.322 162.223 1.00 3.20  ? 2915 VAL A CG1   1 
ATOM   11397 C CG2   . VAL A 1 2915 ? 209.695 185.432 163.846 1.00 2.46  ? 2915 VAL A CG2   1 
ATOM   11398 N N     . LEU A 1 2916 ? 209.058 188.078 160.167 1.00 4.47  ? 2916 LEU A N     1 
ATOM   11399 C CA    . LEU A 1 2916 ? 209.398 188.907 159.015 1.00 6.76  ? 2916 LEU A CA    1 
ATOM   11400 C C     . LEU A 1 2916 ? 208.914 190.338 159.206 1.00 7.89  ? 2916 LEU A C     1 
ATOM   11401 O O     . LEU A 1 2916 ? 209.634 191.295 158.890 1.00 11.65 ? 2916 LEU A O     1 
ATOM   11402 C CB    . LEU A 1 2916 ? 208.805 188.305 157.740 1.00 9.68  ? 2916 LEU A CB    1 
ATOM   11403 C CG    . LEU A 1 2916 ? 209.250 186.894 157.353 1.00 8.14  ? 2916 LEU A CG    1 
ATOM   11404 C CD1   . LEU A 1 2916 ? 208.701 186.530 155.988 1.00 6.81  ? 2916 LEU A CD1   1 
ATOM   11405 C CD2   . LEU A 1 2916 ? 210.765 186.783 157.368 1.00 9.96  ? 2916 LEU A CD2   1 
ATOM   11406 N N     . ASP A 1 2917 ? 207.697 190.503 159.731 1.00 5.59  ? 2917 ASP A N     1 
ATOM   11407 C CA    . ASP A 1 2917 ? 207.173 191.843 159.975 1.00 2.05  ? 2917 ASP A CA    1 
ATOM   11408 C C     . ASP A 1 2917 ? 208.052 192.611 160.955 1.00 7.47  ? 2917 ASP A C     1 
ATOM   11409 O O     . ASP A 1 2917 ? 208.403 193.773 160.708 1.00 14.02 ? 2917 ASP A O     1 
ATOM   11410 C CB    . ASP A 1 2917 ? 205.742 191.752 160.500 1.00 1.23  ? 2917 ASP A CB    1 
ATOM   11411 C CG    . ASP A 1 2917 ? 204.800 191.110 159.507 1.00 14.79 ? 2917 ASP A CG    1 
ATOM   11412 O OD1   . ASP A 1 2917 ? 205.062 191.212 158.290 1.00 15.94 ? 2917 ASP A OD1   1 
ATOM   11413 O OD2   . ASP A 1 2917 ? 203.800 190.500 159.941 1.00 18.03 ? 2917 ASP A OD2   1 
ATOM   11414 N N     . HIS A 1 2918 ? 208.427 191.973 162.066 1.00 4.89  ? 2918 HIS A N     1 
ATOM   11415 C CA    . HIS A 1 2918 ? 209.259 192.635 163.063 1.00 0.00  ? 2918 HIS A CA    1 
ATOM   11416 C C     . HIS A 1 2918 ? 210.637 192.959 162.509 1.00 0.30  ? 2918 HIS A C     1 
ATOM   11417 O O     . HIS A 1 2918 ? 211.192 194.025 162.794 1.00 7.69  ? 2918 HIS A O     1 
ATOM   11418 C CB    . HIS A 1 2918 ? 209.373 191.762 164.310 1.00 0.00  ? 2918 HIS A CB    1 
ATOM   11419 C CG    . HIS A 1 2918 ? 208.096 191.641 165.078 1.00 0.00  ? 2918 HIS A CG    1 
ATOM   11420 N ND1   . HIS A 1 2918 ? 207.213 192.689 165.222 1.00 3.25  ? 2918 HIS A ND1   1 
ATOM   11421 C CD2   . HIS A 1 2918 ? 207.550 190.596 165.742 1.00 4.76  ? 2918 HIS A CD2   1 
ATOM   11422 C CE1   . HIS A 1 2918 ? 206.180 192.295 165.944 1.00 8.52  ? 2918 HIS A CE1   1 
ATOM   11423 N NE2   . HIS A 1 2918 ? 206.358 191.028 166.270 1.00 7.20  ? 2918 HIS A NE2   1 
ATOM   11424 N N     . VAL A 1 2919 ? 211.212 192.048 161.721 1.00 2.72  ? 2919 VAL A N     1 
ATOM   11425 C CA    . VAL A 1 2919 ? 212.518 192.307 161.124 1.00 6.04  ? 2919 VAL A CA    1 
ATOM   11426 C C     . VAL A 1 2919 ? 212.450 193.517 160.205 1.00 10.67 ? 2919 VAL A C     1 
ATOM   11427 O O     . VAL A 1 2919 ? 213.336 194.380 160.226 1.00 10.46 ? 2919 VAL A O     1 
ATOM   11428 C CB    . VAL A 1 2919 ? 213.028 191.056 160.385 1.00 5.15  ? 2919 VAL A CB    1 
ATOM   11429 C CG1   . VAL A 1 2919 ? 214.196 191.409 159.491 1.00 6.61  ? 2919 VAL A CG1   1 
ATOM   11430 C CG2   . VAL A 1 2919 ? 213.444 189.995 161.382 1.00 8.06  ? 2919 VAL A CG2   1 
ATOM   11431 N N     . LEU A 1 2920 ? 211.393 193.611 159.394 1.00 12.35 ? 2920 LEU A N     1 
ATOM   11432 C CA    . LEU A 1 2920 ? 211.257 194.769 158.517 1.00 6.59  ? 2920 LEU A CA    1 
ATOM   11433 C C     . LEU A 1 2920 ? 211.085 196.056 159.312 1.00 8.66  ? 2920 LEU A C     1 
ATOM   11434 O O     . LEU A 1 2920 ? 211.657 197.093 158.952 1.00 15.19 ? 2920 LEU A O     1 
ATOM   11435 C CB    . LEU A 1 2920 ? 210.086 194.577 157.558 1.00 1.43  ? 2920 LEU A CB    1 
ATOM   11436 C CG    . LEU A 1 2920 ? 210.386 193.693 156.354 1.00 4.04  ? 2920 LEU A CG    1 
ATOM   11437 C CD1   . LEU A 1 2920 ? 209.169 193.609 155.473 1.00 8.00  ? 2920 LEU A CD1   1 
ATOM   11438 C CD2   . LEU A 1 2920 ? 211.574 194.232 155.586 1.00 6.42  ? 2920 LEU A CD2   1 
ATOM   11439 N N     . ARG A 1 2921 ? 210.294 196.018 160.387 1.00 7.66  ? 2921 ARG A N     1 
ATOM   11440 C CA    . ARG A 1 2921 ? 210.107 197.221 161.194 1.00 6.13  ? 2921 ARG A CA    1 
ATOM   11441 C C     . ARG A 1 2921 ? 211.421 197.678 161.816 1.00 5.28  ? 2921 ARG A C     1 
ATOM   11442 O O     . ARG A 1 2921 ? 211.762 198.869 161.778 1.00 11.42 ? 2921 ARG A O     1 
ATOM   11443 C CB    . ARG A 1 2921 ? 209.065 196.971 162.282 1.00 1.01  ? 2921 ARG A CB    1 
ATOM   11444 C CG    . ARG A 1 2921 ? 207.691 196.616 161.760 1.00 0.00  ? 2921 ARG A CG    1 
ATOM   11445 C CD    . ARG A 1 2921 ? 206.847 195.991 162.851 1.00 0.16  ? 2921 ARG A CD    1 
ATOM   11446 N NE    . ARG A 1 2921 ? 205.567 195.512 162.346 1.00 7.79  ? 2921 ARG A NE    1 
ATOM   11447 C CZ    . ARG A 1 2921 ? 204.664 194.879 163.080 1.00 5.84  ? 2921 ARG A CZ    1 
ATOM   11448 N NH1   . ARG A 1 2921 ? 204.850 194.667 164.371 1.00 4.53  ? 2921 ARG A NH1   1 
ATOM   11449 N NH2   . ARG A 1 2921 ? 203.543 194.455 162.505 1.00 9.23  ? 2921 ARG A NH2   1 
ATOM   11450 N N     . ILE A 1 2922 ? 212.183 196.742 162.384 1.00 2.17  ? 2922 ILE A N     1 
ATOM   11451 C CA    . ILE A 1 2922 ? 213.443 197.117 163.012 1.00 6.53  ? 2922 ILE A CA    1 
ATOM   11452 C C     . ILE A 1 2922 ? 214.434 197.608 161.964 1.00 9.59  ? 2922 ILE A C     1 
ATOM   11453 O O     . ILE A 1 2922 ? 215.223 198.524 162.220 1.00 11.47 ? 2922 ILE A O     1 
ATOM   11454 C CB    . ILE A 1 2922 ? 214.012 195.949 163.835 1.00 8.23  ? 2922 ILE A CB    1 
ATOM   11455 C CG1   . ILE A 1 2922 ? 212.979 195.448 164.841 1.00 7.26  ? 2922 ILE A CG1   1 
ATOM   11456 C CG2   . ILE A 1 2922 ? 215.218 196.407 164.607 1.00 7.69  ? 2922 ILE A CG2   1 
ATOM   11457 C CD1   . ILE A 1 2922 ? 213.409 194.206 165.580 1.00 1.20  ? 2922 ILE A CD1   1 
ATOM   11458 N N     . ASP A 1 2923 ? 214.406 197.020 160.765 1.00 9.97  ? 2923 ASP A N     1 
ATOM   11459 C CA    . ASP A 1 2923 ? 215.283 197.495 159.700 1.00 8.15  ? 2923 ASP A CA    1 
ATOM   11460 C C     . ASP A 1 2923 ? 214.943 198.921 159.291 1.00 13.15 ? 2923 ASP A C     1 
ATOM   11461 O O     . ASP A 1 2923 ? 215.839 199.760 159.142 1.00 14.21 ? 2923 ASP A O     1 
ATOM   11462 C CB    . ASP A 1 2923 ? 215.199 196.567 158.491 1.00 8.56  ? 2923 ASP A CB    1 
ATOM   11463 C CG    . ASP A 1 2923 ? 216.127 196.991 157.373 1.00 19.43 ? 2923 ASP A CG    1 
ATOM   11464 O OD1   . ASP A 1 2923 ? 217.248 197.446 157.675 1.00 18.78 ? 2923 ASP A OD1   1 
ATOM   11465 O OD2   . ASP A 1 2923 ? 215.732 196.882 156.194 1.00 23.16 ? 2923 ASP A OD2   1 
ATOM   11466 N N     . ARG A 1 2924 ? 213.654 199.219 159.104 1.00 16.22 ? 2924 ARG A N     1 
ATOM   11467 C CA    . ARG A 1 2924 ? 213.281 200.568 158.691 1.00 8.24  ? 2924 ARG A CA    1 
ATOM   11468 C C     . ARG A 1 2924 ? 213.591 201.577 159.789 1.00 6.71  ? 2924 ARG A C     1 
ATOM   11469 O O     . ARG A 1 2924 ? 213.866 202.748 159.504 1.00 12.20 ? 2924 ARG A O     1 
ATOM   11470 C CB    . ARG A 1 2924 ? 211.805 200.632 158.293 1.00 6.87  ? 2924 ARG A CB    1 
ATOM   11471 C CG    . ARG A 1 2924 ? 210.830 200.586 159.445 1.00 8.84  ? 2924 ARG A CG    1 
ATOM   11472 C CD    . ARG A 1 2924 ? 209.416 200.880 158.987 1.00 11.43 ? 2924 ARG A CD    1 
ATOM   11473 N NE    . ARG A 1 2924 ? 209.187 202.309 158.814 1.00 7.68  ? 2924 ARG A NE    1 
ATOM   11474 C CZ    . ARG A 1 2924 ? 208.331 202.830 157.947 1.00 10.85 ? 2924 ARG A CZ    1 
ATOM   11475 N NH1   . ARG A 1 2924 ? 207.611 202.067 157.142 1.00 12.18 ? 2924 ARG A NH1   1 
ATOM   11476 N NH2   . ARG A 1 2924 ? 208.193 204.151 157.886 1.00 9.89  ? 2924 ARG A NH2   1 
ATOM   11477 N N     . ILE A 1 2925 ? 213.557 201.144 161.051 1.00 11.90 ? 2925 ILE A N     1 
ATOM   11478 C CA    . ILE A 1 2925 ? 213.996 202.031 162.125 1.00 14.46 ? 2925 ILE A CA    1 
ATOM   11479 C C     . ILE A 1 2925 ? 215.504 202.246 162.058 1.00 13.90 ? 2925 ILE A C     1 
ATOM   11480 O O     . ILE A 1 2925 ? 215.996 203.364 162.246 1.00 16.05 ? 2925 ILE A O     1 
ATOM   11481 C CB    . ILE A 1 2925 ? 213.562 201.480 163.493 1.00 15.74 ? 2925 ILE A CB    1 
ATOM   11482 C CG1   . ILE A 1 2925 ? 212.090 201.794 163.736 1.00 12.14 ? 2925 ILE A CG1   1 
ATOM   11483 C CG2   . ILE A 1 2925 ? 214.412 202.079 164.597 1.00 8.67  ? 2925 ILE A CG2   1 
ATOM   11484 C CD1   . ILE A 1 2925 ? 211.845 203.232 164.089 1.00 14.45 ? 2925 ILE A CD1   1 
ATOM   11485 N N     . PHE A 1 2926 ? 216.260 201.181 161.788 1.00 14.75 ? 2926 PHE A N     1 
ATOM   11486 C CA    . PHE A 1 2926 ? 217.712 201.298 161.708 1.00 10.17 ? 2926 PHE A CA    1 
ATOM   11487 C C     . PHE A 1 2926 ? 218.145 202.142 160.518 1.00 18.19 ? 2926 PHE A C     1 
ATOM   11488 O O     . PHE A 1 2926 ? 219.261 202.675 160.512 1.00 17.59 ? 2926 PHE A O     1 
ATOM   11489 C CB    . PHE A 1 2926 ? 218.339 199.909 161.620 1.00 13.67 ? 2926 PHE A CB    1 
ATOM   11490 C CG    . PHE A 1 2926 ? 218.586 199.270 162.953 1.00 14.25 ? 2926 PHE A CG    1 
ATOM   11491 C CD1   . PHE A 1 2926 ? 217.776 199.557 164.035 1.00 15.49 ? 2926 PHE A CD1   1 
ATOM   11492 C CD2   . PHE A 1 2926 ? 219.618 198.366 163.119 1.00 17.79 ? 2926 PHE A CD2   1 
ATOM   11493 C CE1   . PHE A 1 2926 ? 218.001 198.968 165.259 1.00 16.93 ? 2926 PHE A CE1   1 
ATOM   11494 C CE2   . PHE A 1 2926 ? 219.846 197.774 164.342 1.00 16.88 ? 2926 PHE A CE2   1 
ATOM   11495 C CZ    . PHE A 1 2926 ? 219.036 198.074 165.412 1.00 16.99 ? 2926 PHE A CZ    1 
ATOM   11496 N N     . ARG A 1 2927 ? 217.288 202.260 159.501 1.00 20.72 ? 2927 ARG A N     1 
ATOM   11497 C CA    . ARG A 1 2927 ? 217.647 203.031 158.315 1.00 18.07 ? 2927 ARG A CA    1 
ATOM   11498 C C     . ARG A 1 2927 ? 217.836 204.507 158.647 1.00 22.75 ? 2927 ARG A C     1 
ATOM   11499 O O     . ARG A 1 2927 ? 218.793 205.136 158.183 1.00 24.90 ? 2927 ARG A O     1 
ATOM   11500 C CB    . ARG A 1 2927 ? 216.578 202.860 157.236 1.00 18.88 ? 2927 ARG A CB    1 
ATOM   11501 C CG    . ARG A 1 2927 ? 216.564 201.497 156.552 1.00 21.85 ? 2927 ARG A CG    1 
ATOM   11502 C CD    . ARG A 1 2927 ? 217.818 201.241 155.732 1.00 25.18 ? 2927 ARG A CD    1 
ATOM   11503 N NE    . ARG A 1 2927 ? 218.882 200.633 156.521 1.00 28.34 ? 2927 ARG A NE    1 
ATOM   11504 C CZ    . ARG A 1 2927 ? 220.158 200.601 156.162 1.00 29.68 ? 2927 ARG A CZ    1 
ATOM   11505 N NH1   . ARG A 1 2927 ? 220.568 201.132 155.021 1.00 25.83 ? 2927 ARG A NH1   1 
ATOM   11506 N NH2   . ARG A 1 2927 ? 221.044 200.022 156.966 1.00 24.34 ? 2927 ARG A NH2   1 
ATOM   11507 N N     . GLN A 1 2928 ? 216.937 205.077 159.447 1.00 20.71 ? 2928 GLN A N     1 
ATOM   11508 C CA    . GLN A 1 2928 ? 217.030 206.491 159.768 1.00 21.00 ? 2928 GLN A CA    1 
ATOM   11509 C C     . GLN A 1 2928 ? 218.148 206.737 160.782 1.00 23.80 ? 2928 GLN A C     1 
ATOM   11510 O O     . GLN A 1 2928 ? 218.424 205.887 161.632 1.00 20.97 ? 2928 GLN A O     1 
ATOM   11511 C CB    . GLN A 1 2928 ? 215.703 207.009 160.315 1.00 19.01 ? 2928 GLN A CB    1 
ATOM   11512 C CG    . GLN A 1 2928 ? 215.202 206.285 161.546 1.00 19.14 ? 2928 GLN A CG    1 
ATOM   11513 C CD    . GLN A 1 2928 ? 213.707 206.436 161.743 1.00 24.82 ? 2928 GLN A CD    1 
ATOM   11514 O OE1   . GLN A 1 2928 ? 212.958 206.616 160.783 1.00 22.53 ? 2928 GLN A OE1   1 
ATOM   11515 N NE2   . GLN A 1 2928 ? 213.265 206.368 162.993 1.00 24.93 ? 2928 GLN A NE2   1 
ATOM   11516 N N     . PRO A 1 2929 ? 218.820 207.891 160.698 1.00 32.07 ? 2929 PRO A N     1 
ATOM   11517 C CA    . PRO A 1 2929 ? 219.926 208.161 161.635 1.00 28.32 ? 2929 PRO A CA    1 
ATOM   11518 C C     . PRO A 1 2929 ? 219.514 208.170 163.098 1.00 24.74 ? 2929 PRO A C     1 
ATOM   11519 O O     . PRO A 1 2929 ? 220.277 207.698 163.950 1.00 26.86 ? 2929 PRO A O     1 
ATOM   11520 C CB    . PRO A 1 2929 ? 220.436 209.537 161.179 1.00 23.60 ? 2929 PRO A CB    1 
ATOM   11521 C CG    . PRO A 1 2929 ? 219.999 209.652 159.756 1.00 21.39 ? 2929 PRO A CG    1 
ATOM   11522 C CD    . PRO A 1 2929 ? 218.674 208.960 159.696 1.00 26.50 ? 2929 PRO A CD    1 
ATOM   11523 N N     . GLN A 1 2930 ? 218.323 208.681 163.419 1.00 21.60 ? 2930 GLN A N     1 
ATOM   11524 C CA    . GLN A 1 2930 ? 217.867 208.780 164.801 1.00 24.43 ? 2930 GLN A CA    1 
ATOM   11525 C C     . GLN A 1 2930 ? 217.033 207.580 165.230 1.00 24.12 ? 2930 GLN A C     1 
ATOM   11526 O O     . GLN A 1 2930 ? 216.176 207.707 166.116 1.00 21.06 ? 2930 GLN A O     1 
ATOM   11527 C CB    . GLN A 1 2930 ? 217.078 210.076 165.014 1.00 25.74 ? 2930 GLN A CB    1 
ATOM   11528 C CG    . GLN A 1 2930 ? 215.761 210.222 164.228 1.00 20.79 ? 2930 GLN A CG    1 
ATOM   11529 C CD    . GLN A 1 2930 ? 215.928 210.365 162.721 1.00 28.35 ? 2930 GLN A CD    1 
ATOM   11530 O OE1   . GLN A 1 2930 ? 216.876 209.854 162.128 1.00 28.17 ? 2930 GLN A OE1   1 
ATOM   11531 N NE2   . GLN A 1 2930 ? 214.995 211.072 162.096 1.00 29.48 ? 2930 GLN A NE2   1 
ATOM   11532 N N     . GLY A 1 2931 ? 217.266 206.415 164.631 1.00 23.77 ? 2931 GLY A N     1 
ATOM   11533 C CA    . GLY A 1 2931 ? 216.438 205.257 164.900 1.00 22.70 ? 2931 GLY A CA    1 
ATOM   11534 C C     . GLY A 1 2931 ? 216.644 204.736 166.308 1.00 17.24 ? 2931 GLY A C     1 
ATOM   11535 O O     . GLY A 1 2931 ? 217.721 204.208 166.631 1.00 10.69 ? 2931 GLY A O     1 
ATOM   11536 N N     . HIS A 1 2932 ? 215.628 204.869 167.155 1.00 15.82 ? 2932 HIS A N     1 
ATOM   11537 C CA    . HIS A 1 2932 ? 215.635 204.308 168.496 1.00 10.93 ? 2932 HIS A CA    1 
ATOM   11538 C C     . HIS A 1 2932 ? 214.385 203.461 168.667 1.00 16.08 ? 2932 HIS A C     1 
ATOM   11539 O O     . HIS A 1 2932 ? 213.318 203.807 168.151 1.00 20.22 ? 2932 HIS A O     1 
ATOM   11540 C CB    . HIS A 1 2932 ? 215.689 205.405 169.561 1.00 15.89 ? 2932 HIS A CB    1 
ATOM   11541 C CG    . HIS A 1 2932 ? 216.975 206.172 169.573 1.00 17.19 ? 2932 HIS A CG    1 
ATOM   11542 N ND1   . HIS A 1 2932 ? 218.205 205.560 169.661 1.00 13.92 ? 2932 HIS A ND1   1 
ATOM   11543 C CD2   . HIS A 1 2932 ? 217.221 207.502 169.509 1.00 18.92 ? 2932 HIS A CD2   1 
ATOM   11544 C CE1   . HIS A 1 2932 ? 219.154 206.479 169.649 1.00 13.78 ? 2932 HIS A CE1   1 
ATOM   11545 N NE2   . HIS A 1 2932 ? 218.583 207.665 169.559 1.00 15.45 ? 2932 HIS A NE2   1 
ATOM   11546 N N     . LEU A 1 2933 ? 214.517 202.352 169.389 1.00 14.00 ? 2933 LEU A N     1 
ATOM   11547 C CA    . LEU A 1 2933 ? 213.465 201.353 169.479 1.00 4.84  ? 2933 LEU A CA    1 
ATOM   11548 C C     . LEU A 1 2933 ? 213.010 201.155 170.915 1.00 7.68  ? 2933 LEU A C     1 
ATOM   11549 O O     . LEU A 1 2933 ? 213.791 201.290 171.860 1.00 18.09 ? 2933 LEU A O     1 
ATOM   11550 C CB    . LEU A 1 2933 ? 213.930 200.011 168.923 1.00 7.13  ? 2933 LEU A CB    1 
ATOM   11551 C CG    . LEU A 1 2933 ? 214.038 199.909 167.410 1.00 11.61 ? 2933 LEU A CG    1 
ATOM   11552 C CD1   . LEU A 1 2933 ? 215.047 198.854 167.059 1.00 8.79  ? 2933 LEU A CD1   1 
ATOM   11553 C CD2   . LEU A 1 2933 ? 212.684 199.580 166.807 1.00 11.82 ? 2933 LEU A CD2   1 
ATOM   11554 N N     . LEU A 1 2934 ? 211.729 200.824 171.061 1.00 4.76  ? 2934 LEU A N     1 
ATOM   11555 C CA    . LEU A 1 2934 ? 211.147 200.384 172.326 1.00 8.18  ? 2934 LEU A CA    1 
ATOM   11556 C C     . LEU A 1 2934 ? 210.393 199.095 172.010 1.00 10.47 ? 2934 LEU A C     1 
ATOM   11557 O O     . LEU A 1 2934 ? 209.197 199.118 171.714 1.00 14.24 ? 2934 LEU A O     1 
ATOM   11558 C CB    . LEU A 1 2934 ? 210.244 201.457 172.927 1.00 3.51  ? 2934 LEU A CB    1 
ATOM   11559 C CG    . LEU A 1 2934 ? 209.499 201.112 174.216 1.00 4.69  ? 2934 LEU A CG    1 
ATOM   11560 C CD1   . LEU A 1 2934 ? 210.463 200.648 175.291 1.00 14.60 ? 2934 LEU A CD1   1 
ATOM   11561 C CD2   . LEU A 1 2934 ? 208.695 202.304 174.696 1.00 11.81 ? 2934 LEU A CD2   1 
ATOM   11562 N N     . LEU A 1 2935 ? 211.097 197.968 172.062 1.00 8.02  ? 2935 LEU A N     1 
ATOM   11563 C CA    . LEU A 1 2935 ? 210.513 196.679 171.700 1.00 0.29  ? 2935 LEU A CA    1 
ATOM   11564 C C     . LEU A 1 2935 ? 209.840 196.100 172.936 1.00 0.00  ? 2935 LEU A C     1 
ATOM   11565 O O     . LEU A 1 2935 ? 210.507 195.623 173.853 1.00 10.74 ? 2935 LEU A O     1 
ATOM   11566 C CB    . LEU A 1 2935 ? 211.581 195.734 171.161 1.00 2.92  ? 2935 LEU A CB    1 
ATOM   11567 C CG    . LEU A 1 2935 ? 212.305 196.159 169.883 1.00 4.27  ? 2935 LEU A CG    1 
ATOM   11568 C CD1   . LEU A 1 2935 ? 213.548 195.313 169.679 1.00 4.40  ? 2935 LEU A CD1   1 
ATOM   11569 C CD2   . LEU A 1 2935 ? 211.402 196.108 168.667 1.00 8.97  ? 2935 LEU A CD2   1 
ATOM   11570 N N     . ILE A 1 2936 ? 208.515 196.135 172.967 1.00 0.00  ? 2936 ILE A N     1 
ATOM   11571 C CA    . ILE A 1 2936 ? 207.751 195.707 174.131 1.00 5.23  ? 2936 ILE A CA    1 
ATOM   11572 C C     . ILE A 1 2936 ? 207.056 194.398 173.784 1.00 12.14 ? 2936 ILE A C     1 
ATOM   11573 O O     . ILE A 1 2936 ? 206.218 194.348 172.879 1.00 16.52 ? 2936 ILE A O     1 
ATOM   11574 C CB    . ILE A 1 2936 ? 206.747 196.779 174.568 1.00 2.63  ? 2936 ILE A CB    1 
ATOM   11575 C CG1   . ILE A 1 2936 ? 207.488 198.002 175.104 1.00 6.82  ? 2936 ILE A CG1   1 
ATOM   11576 C CG2   . ILE A 1 2936 ? 205.810 196.229 175.621 1.00 6.07  ? 2936 ILE A CG2   1 
ATOM   11577 C CD1   . ILE A 1 2936 ? 206.590 199.164 175.409 1.00 14.97 ? 2936 ILE A CD1   1 
ATOM   11578 N N     . GLY A 1 2937 ? 207.402 193.338 174.506 1.00 6.71  ? 2937 GLY A N     1 
ATOM   11579 C CA    . GLY A 1 2937 ? 206.794 192.040 174.286 1.00 3.89  ? 2937 GLY A CA    1 
ATOM   11580 C C     . GLY A 1 2937 ? 207.291 191.043 175.304 1.00 8.24  ? 2937 GLY A C     1 
ATOM   11581 O O     . GLY A 1 2937 ? 208.294 191.272 175.988 1.00 9.52  ? 2937 GLY A O     1 
ATOM   11582 N N     . VAL A 1 2938 ? 206.572 189.921 175.395 1.00 11.29 ? 2938 VAL A N     1 
ATOM   11583 C CA    . VAL A 1 2938 ? 206.884 188.914 176.401 1.00 3.06  ? 2938 VAL A CA    1 
ATOM   11584 C C     . VAL A 1 2938 ? 208.310 188.409 176.217 1.00 4.55  ? 2938 VAL A C     1 
ATOM   11585 O O     . VAL A 1 2938 ? 208.875 188.449 175.117 1.00 12.04 ? 2938 VAL A O     1 
ATOM   11586 C CB    . VAL A 1 2938 ? 205.883 187.748 176.339 1.00 2.20  ? 2938 VAL A CB    1 
ATOM   11587 C CG1   . VAL A 1 2938 ? 204.475 188.236 176.628 1.00 6.11  ? 2938 VAL A CG1   1 
ATOM   11588 C CG2   . VAL A 1 2938 ? 205.946 187.068 174.983 1.00 5.00  ? 2938 VAL A CG2   1 
ATOM   11589 N N     . SER A 1 2939 ? 208.903 187.941 177.312 1.00 0.62  ? 2939 SER A N     1 
ATOM   11590 C CA    . SER A 1 2939 ? 210.247 187.386 177.253 1.00 3.00  ? 2939 SER A CA    1 
ATOM   11591 C C     . SER A 1 2939 ? 210.265 186.139 176.380 1.00 1.77  ? 2939 SER A C     1 
ATOM   11592 O O     . SER A 1 2939 ? 209.317 185.352 176.361 1.00 8.68  ? 2939 SER A O     1 
ATOM   11593 C CB    . SER A 1 2939 ? 210.746 187.054 178.658 1.00 6.19  ? 2939 SER A CB    1 
ATOM   11594 O OG    . SER A 1 2939 ? 210.824 188.221 179.456 1.00 8.82  ? 2939 SER A OG    1 
ATOM   11595 N N     . GLY A 1 2940 ? 211.350 185.971 175.631 1.00 0.00  ? 2940 GLY A N     1 
ATOM   11596 C CA    . GLY A 1 2940 ? 211.477 184.854 174.726 1.00 3.61  ? 2940 GLY A CA    1 
ATOM   11597 C C     . GLY A 1 2940 ? 210.743 185.013 173.413 1.00 5.04  ? 2940 GLY A C     1 
ATOM   11598 O O     . GLY A 1 2940 ? 210.784 184.094 172.585 1.00 8.15  ? 2940 GLY A O     1 
ATOM   11599 N N     . ALA A 1 2941 ? 210.069 186.146 173.195 1.00 2.33  ? 2941 ALA A N     1 
ATOM   11600 C CA    . ALA A 1 2941 ? 209.392 186.372 171.924 1.00 2.51  ? 2941 ALA A CA    1 
ATOM   11601 C C     . ALA A 1 2941 ? 210.382 186.624 170.797 1.00 3.20  ? 2941 ALA A C     1 
ATOM   11602 O O     . ALA A 1 2941 ? 209.998 186.617 169.623 1.00 6.00  ? 2941 ALA A O     1 
ATOM   11603 C CB    . ALA A 1 2941 ? 208.418 187.541 172.047 1.00 1.76  ? 2941 ALA A CB    1 
ATOM   11604 N N     . GLY A 1 2942 ? 211.647 186.849 171.128 1.00 2.78  ? 2942 GLY A N     1 
ATOM   11605 C CA    . GLY A 1 2942 ? 212.675 187.045 170.134 1.00 2.41  ? 2942 GLY A CA    1 
ATOM   11606 C C     . GLY A 1 2942 ? 213.085 188.476 169.879 1.00 5.98  ? 2942 GLY A C     1 
ATOM   11607 O O     . GLY A 1 2942 ? 213.733 188.735 168.861 1.00 12.68 ? 2942 GLY A O     1 
ATOM   11608 N N     . LYS A 1 2943 ? 212.738 189.409 170.767 1.00 0.71  ? 2943 LYS A N     1 
ATOM   11609 C CA    . LYS A 1 2943 ? 213.072 190.812 170.540 1.00 1.31  ? 2943 LYS A CA    1 
ATOM   11610 C C     . LYS A 1 2943 ? 214.578 191.015 170.442 1.00 0.97  ? 2943 LYS A C     1 
ATOM   11611 O O     . LYS A 1 2943 ? 215.068 191.691 169.531 1.00 7.52  ? 2943 LYS A O     1 
ATOM   11612 C CB    . LYS A 1 2943 ? 212.479 191.677 171.653 1.00 4.86  ? 2943 LYS A CB    1 
ATOM   11613 C CG    . LYS A 1 2943 ? 211.059 191.304 172.036 1.00 4.39  ? 2943 LYS A CG    1 
ATOM   11614 C CD    . LYS A 1 2943 ? 210.477 192.291 173.030 1.00 0.77  ? 2943 LYS A CD    1 
ATOM   11615 C CE    . LYS A 1 2943 ? 211.172 192.210 174.371 1.00 2.35  ? 2943 LYS A CE    1 
ATOM   11616 N NZ    . LYS A 1 2943 ? 210.814 190.966 175.097 1.00 3.99  ? 2943 LYS A NZ    1 
ATOM   11617 N N     . THR A 1 2944 ? 215.333 190.414 171.363 1.00 0.00  ? 2944 THR A N     1 
ATOM   11618 C CA    . THR A 1 2944 ? 216.783 190.579 171.350 1.00 0.83  ? 2944 THR A CA    1 
ATOM   11619 C C     . THR A 1 2944 ? 217.412 189.867 170.157 1.00 10.99 ? 2944 THR A C     1 
ATOM   11620 O O     . THR A 1 2944 ? 218.297 190.415 169.489 1.00 16.37 ? 2944 THR A O     1 
ATOM   11621 C CB    . THR A 1 2944 ? 217.378 190.068 172.662 1.00 3.01  ? 2944 THR A CB    1 
ATOM   11622 O OG1   . THR A 1 2944 ? 216.765 190.750 173.762 1.00 5.62  ? 2944 THR A OG1   1 
ATOM   11623 C CG2   . THR A 1 2944 ? 218.879 190.304 172.697 1.00 2.56  ? 2944 THR A CG2   1 
ATOM   11624 N N     . THR A 1 2945 ? 216.972 188.637 169.877 1.00 9.74  ? 2945 THR A N     1 
ATOM   11625 C CA    . THR A 1 2945 ? 217.534 187.897 168.750 1.00 1.61  ? 2945 THR A CA    1 
ATOM   11626 C C     . THR A 1 2945 ? 217.237 188.596 167.432 1.00 4.49  ? 2945 THR A C     1 
ATOM   11627 O O     . THR A 1 2945 ? 218.120 188.731 166.579 1.00 13.48 ? 2945 THR A O     1 
ATOM   11628 C CB    . THR A 1 2945 ? 217.004 186.462 168.727 1.00 4.21  ? 2945 THR A CB    1 
ATOM   11629 O OG1   . THR A 1 2945 ? 215.578 186.473 168.594 1.00 8.81  ? 2945 THR A OG1   1 
ATOM   11630 C CG2   . THR A 1 2945 ? 217.407 185.717 169.989 1.00 6.32  ? 2945 THR A CG2   1 
ATOM   11631 N N     . LEU A 1 2946 ? 215.996 189.054 167.247 1.00 2.21  ? 2946 LEU A N     1 
ATOM   11632 C CA    . LEU A 1 2946 ? 215.660 189.774 166.023 1.00 5.27  ? 2946 LEU A CA    1 
ATOM   11633 C C     . LEU A 1 2946 ? 216.431 191.082 165.928 1.00 5.56  ? 2946 LEU A C     1 
ATOM   11634 O O     . LEU A 1 2946 ? 216.889 191.463 164.844 1.00 10.55 ? 2946 LEU A O     1 
ATOM   11635 C CB    . LEU A 1 2946 ? 214.157 190.031 165.949 1.00 2.02  ? 2946 LEU A CB    1 
ATOM   11636 C CG    . LEU A 1 2946 ? 213.289 188.797 165.712 1.00 1.44  ? 2946 LEU A CG    1 
ATOM   11637 C CD1   . LEU A 1 2946 ? 211.831 189.188 165.568 1.00 3.41  ? 2946 LEU A CD1   1 
ATOM   11638 C CD2   . LEU A 1 2946 ? 213.771 188.030 164.494 1.00 10.98 ? 2946 LEU A CD2   1 
ATOM   11639 N N     . SER A 1 2947 ? 216.593 191.778 167.056 1.00 6.95  ? 2947 SER A N     1 
ATOM   11640 C CA    . SER A 1 2947 ? 217.346 193.026 167.055 1.00 5.93  ? 2947 SER A CA    1 
ATOM   11641 C C     . SER A 1 2947 ? 218.782 192.801 166.601 1.00 4.93  ? 2947 SER A C     1 
ATOM   11642 O O     . SER A 1 2947 ? 219.276 193.500 165.711 1.00 8.38  ? 2947 SER A O     1 
ATOM   11643 C CB    . SER A 1 2947 ? 217.310 193.655 168.446 1.00 2.75  ? 2947 SER A CB    1 
ATOM   11644 O OG    . SER A 1 2947 ? 217.925 194.930 168.438 1.00 11.98 ? 2947 SER A OG    1 
ATOM   11645 N N     . ARG A 1 2948 ? 219.464 191.811 167.184 1.00 3.31  ? 2948 ARG A N     1 
ATOM   11646 C CA    . ARG A 1 2948 ? 220.842 191.542 166.777 1.00 6.47  ? 2948 ARG A CA    1 
ATOM   11647 C C     . ARG A 1 2948 ? 220.916 191.034 165.342 1.00 14.58 ? 2948 ARG A C     1 
ATOM   11648 O O     . ARG A 1 2948 ? 221.847 191.378 164.604 1.00 17.98 ? 2948 ARG A O     1 
ATOM   11649 C CB    . ARG A 1 2948 ? 221.508 190.546 167.725 1.00 7.14  ? 2948 ARG A CB    1 
ATOM   11650 C CG    . ARG A 1 2948 ? 221.305 190.825 169.199 1.00 14.48 ? 2948 ARG A CG    1 
ATOM   11651 C CD    . ARG A 1 2948 ? 222.204 189.972 170.105 1.00 14.30 ? 2948 ARG A CD    1 
ATOM   11652 N NE    . ARG A 1 2948 ? 223.617 190.000 169.738 1.00 15.74 ? 2948 ARG A NE    1 
ATOM   11653 C CZ    . ARG A 1 2948 ? 224.201 189.164 168.890 1.00 17.99 ? 2948 ARG A CZ    1 
ATOM   11654 N NH1   . ARG A 1 2948 ? 223.530 188.180 168.316 1.00 16.61 ? 2948 ARG A NH1   1 
ATOM   11655 N NH2   . ARG A 1 2948 ? 225.493 189.316 168.615 1.00 18.11 ? 2948 ARG A NH2   1 
ATOM   11656 N N     . PHE A 1 2949 ? 219.951 190.210 164.928 1.00 13.95 ? 2949 PHE A N     1 
ATOM   11657 C CA    . PHE A 1 2949 ? 219.971 189.667 163.575 1.00 8.12  ? 2949 PHE A CA    1 
ATOM   11658 C C     . PHE A 1 2949 ? 219.862 190.778 162.542 1.00 10.07 ? 2949 PHE A C     1 
ATOM   11659 O O     . PHE A 1 2949 ? 220.634 190.824 161.578 1.00 19.91 ? 2949 PHE A O     1 
ATOM   11660 C CB    . PHE A 1 2949 ? 218.834 188.657 163.411 1.00 9.31  ? 2949 PHE A CB    1 
ATOM   11661 C CG    . PHE A 1 2949 ? 218.410 188.435 161.987 1.00 11.97 ? 2949 PHE A CG    1 
ATOM   11662 C CD1   . PHE A 1 2949 ? 219.296 187.922 161.055 1.00 16.60 ? 2949 PHE A CD1   1 
ATOM   11663 C CD2   . PHE A 1 2949 ? 217.120 188.729 161.584 1.00 11.56 ? 2949 PHE A CD2   1 
ATOM   11664 C CE1   . PHE A 1 2949 ? 218.904 187.715 159.748 1.00 18.77 ? 2949 PHE A CE1   1 
ATOM   11665 C CE2   . PHE A 1 2949 ? 216.723 188.523 160.279 1.00 11.74 ? 2949 PHE A CE2   1 
ATOM   11666 C CZ    . PHE A 1 2949 ? 217.616 188.014 159.360 1.00 10.72 ? 2949 PHE A CZ    1 
ATOM   11667 N N     . VAL A 1 2950 ? 218.917 191.699 162.737 1.00 11.83 ? 2950 VAL A N     1 
ATOM   11668 C CA    . VAL A 1 2950 ? 218.737 192.769 161.765 1.00 14.84 ? 2950 VAL A CA    1 
ATOM   11669 C C     . VAL A 1 2950 ? 219.827 193.824 161.912 1.00 14.14 ? 2950 VAL A C     1 
ATOM   11670 O O     . VAL A 1 2950 ? 220.130 194.548 160.956 1.00 16.02 ? 2950 VAL A O     1 
ATOM   11671 C CB    . VAL A 1 2950 ? 217.330 193.372 161.903 1.00 8.61  ? 2950 VAL A CB    1 
ATOM   11672 C CG1   . VAL A 1 2950 ? 217.220 194.099 163.205 1.00 9.84  ? 2950 VAL A CG1   1 
ATOM   11673 C CG2   . VAL A 1 2950 ? 217.018 194.292 160.737 1.00 16.43 ? 2950 VAL A CG2   1 
ATOM   11674 N N     . ALA A 1 2951 ? 220.435 193.937 163.097 1.00 12.55 ? 2951 ALA A N     1 
ATOM   11675 C CA    . ALA A 1 2951 ? 221.578 194.829 163.249 1.00 12.34 ? 2951 ALA A CA    1 
ATOM   11676 C C     . ALA A 1 2951 ? 222.772 194.326 162.454 1.00 19.19 ? 2951 ALA A C     1 
ATOM   11677 O O     . ALA A 1 2951 ? 223.458 195.109 161.788 1.00 23.75 ? 2951 ALA A O     1 
ATOM   11678 C CB    . ALA A 1 2951 ? 221.937 194.972 164.726 1.00 7.54  ? 2951 ALA A CB    1 
ATOM   11679 N N     . TRP A 1 2952 ? 223.038 193.020 162.516 1.00 15.66 ? 2952 TRP A N     1 
ATOM   11680 C CA    . TRP A 1 2952 ? 224.074 192.438 161.672 1.00 16.38 ? 2952 TRP A CA    1 
ATOM   11681 C C     . TRP A 1 2952 ? 223.711 192.550 160.198 1.00 19.54 ? 2952 TRP A C     1 
ATOM   11682 O O     . TRP A 1 2952 ? 224.572 192.836 159.358 1.00 22.76 ? 2952 TRP A O     1 
ATOM   11683 C CB    . TRP A 1 2952 ? 224.306 190.978 162.050 1.00 16.30 ? 2952 TRP A CB    1 
ATOM   11684 C CG    . TRP A 1 2952 ? 225.262 190.300 161.132 1.00 20.88 ? 2952 TRP A CG    1 
ATOM   11685 C CD1   . TRP A 1 2952 ? 226.622 190.379 161.158 1.00 21.68 ? 2952 TRP A CD1   1 
ATOM   11686 C CD2   . TRP A 1 2952 ? 224.929 189.465 160.018 1.00 21.83 ? 2952 TRP A CD2   1 
ATOM   11687 N NE1   . TRP A 1 2952 ? 227.158 189.628 160.140 1.00 22.94 ? 2952 TRP A NE1   1 
ATOM   11688 C CE2   . TRP A 1 2952 ? 226.138 189.059 159.424 1.00 22.86 ? 2952 TRP A CE2   1 
ATOM   11689 C CE3   . TRP A 1 2952 ? 223.724 189.018 159.470 1.00 18.90 ? 2952 TRP A CE3   1 
ATOM   11690 C CZ2   . TRP A 1 2952 ? 226.177 188.225 158.312 1.00 22.44 ? 2952 TRP A CZ2   1 
ATOM   11691 C CZ3   . TRP A 1 2952 ? 223.765 188.191 158.367 1.00 22.07 ? 2952 TRP A CZ3   1 
ATOM   11692 C CH2   . TRP A 1 2952 ? 224.982 187.804 157.799 1.00 21.51 ? 2952 TRP A CH2   1 
ATOM   11693 N N     . MET A 1 2953 ? 222.438 192.323 159.864 1.00 18.19 ? 2953 MET A N     1 
ATOM   11694 C CA    . MET A 1 2953 ? 222.017 192.369 158.469 1.00 14.47 ? 2953 MET A CA    1 
ATOM   11695 C C     . MET A 1 2953 ? 222.153 193.769 157.883 1.00 15.98 ? 2953 MET A C     1 
ATOM   11696 O O     . MET A 1 2953 ? 222.195 193.924 156.657 1.00 20.95 ? 2953 MET A O     1 
ATOM   11697 C CB    . MET A 1 2953 ? 220.582 191.860 158.348 1.00 11.39 ? 2953 MET A CB    1 
ATOM   11698 C CG    . MET A 1 2953 ? 220.199 191.380 156.963 1.00 20.47 ? 2953 MET A CG    1 
ATOM   11699 S SD    . MET A 1 2953 ? 218.682 190.410 156.993 1.00 26.37 ? 2953 MET A SD    1 
ATOM   11700 C CE    . MET A 1 2953 ? 217.727 191.335 158.189 1.00 19.45 ? 2953 MET A CE    1 
ATOM   11701 N N     . ASN A 1 2954 ? 222.219 194.793 158.732 1.00 16.75 ? 2954 ASN A N     1 
ATOM   11702 C CA    . ASN A 1 2954 ? 222.513 196.153 158.305 1.00 21.26 ? 2954 ASN A CA    1 
ATOM   11703 C C     . ASN A 1 2954 ? 223.924 196.588 158.678 1.00 19.42 ? 2954 ASN A C     1 
ATOM   11704 O O     . ASN A 1 2954 ? 224.261 197.765 158.523 1.00 18.80 ? 2954 ASN A O     1 
ATOM   11705 C CB    . ASN A 1 2954 ? 221.492 197.126 158.896 1.00 20.97 ? 2954 ASN A CB    1 
ATOM   11706 C CG    . ASN A 1 2954 ? 220.067 196.713 158.612 1.00 22.26 ? 2954 ASN A CG    1 
ATOM   11707 O OD1   . ASN A 1 2954 ? 219.769 196.164 157.552 1.00 25.45 ? 2954 ASN A OD1   1 
ATOM   11708 N ND2   . ASN A 1 2954 ? 219.175 196.974 159.558 1.00 16.52 ? 2954 ASN A ND2   1 
ATOM   11709 N N     . GLY A 1 2955 ? 224.753 195.667 159.157 1.00 20.01 ? 2955 GLY A N     1 
ATOM   11710 C CA    . GLY A 1 2955 ? 226.127 195.986 159.504 1.00 20.07 ? 2955 GLY A CA    1 
ATOM   11711 C C     . GLY A 1 2955 ? 226.300 196.901 160.697 1.00 20.24 ? 2955 GLY A C     1 
ATOM   11712 O O     . GLY A 1 2955 ? 227.183 197.768 160.683 1.00 21.45 ? 2955 GLY A O     1 
ATOM   11713 N N     . LEU A 1 2956 ? 225.485 196.729 161.734 1.00 19.36 ? 2956 LEU A N     1 
ATOM   11714 C CA    . LEU A 1 2956 ? 225.632 197.459 162.985 1.00 15.44 ? 2956 LEU A CA    1 
ATOM   11715 C C     . LEU A 1 2956 ? 226.196 196.522 164.042 1.00 19.03 ? 2956 LEU A C     1 
ATOM   11716 O O     . LEU A 1 2956 ? 225.754 195.374 164.159 1.00 23.78 ? 2956 LEU A O     1 
ATOM   11717 C CB    . LEU A 1 2956 ? 224.301 198.040 163.467 1.00 13.41 ? 2956 LEU A CB    1 
ATOM   11718 C CG    . LEU A 1 2956 ? 223.754 199.305 162.804 1.00 18.74 ? 2956 LEU A CG    1 
ATOM   11719 C CD1   . LEU A 1 2956 ? 223.254 199.024 161.398 1.00 18.76 ? 2956 LEU A CD1   1 
ATOM   11720 C CD2   . LEU A 1 2956 ? 222.666 199.929 163.657 1.00 16.82 ? 2956 LEU A CD2   1 
ATOM   11721 N N     . SER A 1 2957 ? 227.171 197.008 164.805 1.00 19.63 ? 2957 SER A N     1 
ATOM   11722 C CA    . SER A 1 2957 ? 227.772 196.215 165.871 1.00 21.53 ? 2957 SER A CA    1 
ATOM   11723 C C     . SER A 1 2957 ? 226.904 196.327 167.117 1.00 20.68 ? 2957 SER A C     1 
ATOM   11724 O O     . SER A 1 2957 ? 226.793 197.403 167.712 1.00 19.58 ? 2957 SER A O     1 
ATOM   11725 C CB    . SER A 1 2957 ? 229.197 196.683 166.151 1.00 20.83 ? 2957 SER A CB    1 
ATOM   11726 O OG    . SER A 1 2957 ? 229.986 196.653 164.975 1.00 24.91 ? 2957 SER A OG    1 
ATOM   11727 N N     . VAL A 1 2958 ? 226.285 195.215 167.515 1.00 19.55 ? 2958 VAL A N     1 
ATOM   11728 C CA    . VAL A 1 2958 ? 225.453 195.210 168.709 1.00 16.63 ? 2958 VAL A CA    1 
ATOM   11729 C C     . VAL A 1 2958 ? 226.334 195.324 169.945 1.00 17.90 ? 2958 VAL A C     1 
ATOM   11730 O O     . VAL A 1 2958 ? 227.340 194.616 170.083 1.00 21.53 ? 2958 VAL A O     1 
ATOM   11731 C CB    . VAL A 1 2958 ? 224.590 193.939 168.761 1.00 14.20 ? 2958 VAL A CB    1 
ATOM   11732 C CG1   . VAL A 1 2958 ? 223.514 194.073 169.826 1.00 14.18 ? 2958 VAL A CG1   1 
ATOM   11733 C CG2   . VAL A 1 2958 ? 223.974 193.662 167.404 1.00 15.07 ? 2958 VAL A CG2   1 
ATOM   11734 N N     . TYR A 1 2959 ? 225.959 196.222 170.851 1.00 19.15 ? 2959 TYR A N     1 
ATOM   11735 C CA    . TYR A 1 2959 ? 226.666 196.411 172.107 1.00 21.35 ? 2959 TYR A CA    1 
ATOM   11736 C C     . TYR A 1 2959 ? 225.669 196.264 173.244 1.00 23.68 ? 2959 TYR A C     1 
ATOM   11737 O O     . TYR A 1 2959 ? 224.574 196.833 173.200 1.00 24.49 ? 2959 TYR A O     1 
ATOM   11738 C CB    . TYR A 1 2959 ? 227.366 197.784 172.149 1.00 22.15 ? 2959 TYR A CB    1 
ATOM   11739 C CG    . TYR A 1 2959 ? 228.087 198.116 173.443 1.00 22.63 ? 2959 TYR A CG    1 
ATOM   11740 C CD1   . TYR A 1 2959 ? 229.472 198.132 173.495 1.00 22.06 ? 2959 TYR A CD1   1 
ATOM   11741 C CD2   . TYR A 1 2959 ? 227.390 198.464 174.592 1.00 21.94 ? 2959 TYR A CD2   1 
ATOM   11742 C CE1   . TYR A 1 2959 ? 230.142 198.441 174.660 1.00 23.65 ? 2959 TYR A CE1   1 
ATOM   11743 C CE2   . TYR A 1 2959 ? 228.051 198.776 175.760 1.00 20.98 ? 2959 TYR A CE2   1 
ATOM   11744 C CZ    . TYR A 1 2959 ? 229.426 198.765 175.789 1.00 24.24 ? 2959 TYR A CZ    1 
ATOM   11745 O OH    . TYR A 1 2959 ? 230.090 199.079 176.952 1.00 24.73 ? 2959 TYR A OH    1 
ATOM   11746 N N     . GLN A 1 2960 ? 226.055 195.502 174.264 1.00 25.23 ? 2960 GLN A N     1 
ATOM   11747 C CA    . GLN A 1 2960 ? 225.177 195.199 175.382 1.00 22.30 ? 2960 GLN A CA    1 
ATOM   11748 C C     . GLN A 1 2960 ? 225.867 195.589 176.679 1.00 24.87 ? 2960 GLN A C     1 
ATOM   11749 O O     . GLN A 1 2960 ? 227.097 195.612 176.763 1.00 27.70 ? 2960 GLN A O     1 
ATOM   11750 C CB    . GLN A 1 2960 ? 224.805 193.711 175.422 1.00 22.19 ? 2960 GLN A CB    1 
ATOM   11751 C CG    . GLN A 1 2960 ? 223.768 193.304 174.398 1.00 21.92 ? 2960 GLN A CG    1 
ATOM   11752 C CD    . GLN A 1 2960 ? 222.702 192.395 174.971 1.00 21.22 ? 2960 GLN A CD    1 
ATOM   11753 O OE1   . GLN A 1 2960 ? 222.250 192.585 176.100 1.00 22.47 ? 2960 GLN A OE1   1 
ATOM   11754 N NE2   . GLN A 1 2960 ? 222.289 191.404 174.192 1.00 21.31 ? 2960 GLN A NE2   1 
ATOM   11755 N N     . ILE A 1 2961 ? 225.062 195.895 177.691 1.00 23.30 ? 2961 ILE A N     1 
ATOM   11756 C CA    . ILE A 1 2961 ? 225.561 196.225 179.020 1.00 24.42 ? 2961 ILE A CA    1 
ATOM   11757 C C     . ILE A 1 2961 ? 225.497 194.973 179.881 1.00 28.11 ? 2961 ILE A C     1 
ATOM   11758 O O     . ILE A 1 2961 ? 224.430 194.365 180.029 1.00 30.38 ? 2961 ILE A O     1 
ATOM   11759 C CB    . ILE A 1 2961 ? 224.753 197.366 179.657 1.00 24.59 ? 2961 ILE A CB    1 
ATOM   11760 C CG1   . ILE A 1 2961 ? 224.922 198.659 178.863 1.00 29.95 ? 2961 ILE A CG1   1 
ATOM   11761 C CG2   . ILE A 1 2961 ? 225.192 197.574 181.092 1.00 27.17 ? 2961 ILE A CG2   1 
ATOM   11762 C CD1   . ILE A 1 2961 ? 226.347 199.120 178.751 1.00 27.35 ? 2961 ILE A CD1   1 
ATOM   11763 N N     . LYS A 1 2962 ? 226.637 194.588 180.448 1.00 29.38 ? 2962 LYS A N     1 
ATOM   11764 C CA    . LYS A 1 2962 ? 226.719 193.427 181.327 1.00 28.33 ? 2962 LYS A CA    1 
ATOM   11765 C C     . LYS A 1 2962 ? 226.435 193.891 182.751 1.00 28.95 ? 2962 LYS A C     1 
ATOM   11766 O O     . LYS A 1 2962 ? 227.317 194.432 183.425 1.00 32.90 ? 2962 LYS A O     1 
ATOM   11767 C CB    . LYS A 1 2962 ? 228.090 192.769 181.208 1.00 31.54 ? 2962 LYS A CB    1 
ATOM   11768 C CG    . LYS A 1 2962 ? 228.491 192.484 179.768 1.00 33.11 ? 2962 LYS A CG    1 
ATOM   11769 C CD    . LYS A 1 2962 ? 229.983 192.250 179.633 1.00 30.95 ? 2962 LYS A CD    1 
ATOM   11770 C CE    . LYS A 1 2962 ? 230.372 192.001 178.185 1.00 29.63 ? 2962 LYS A CE    1 
ATOM   11771 N NZ    . LYS A 1 2962 ? 229.888 190.681 177.698 1.00 29.42 ? 2962 LYS A NZ    1 
ATOM   11772 N N     . VAL A 1 2963 ? 225.206 193.672 183.207 1.00 27.80 ? 2963 VAL A N     1 
ATOM   11773 C CA    . VAL A 1 2963 ? 224.708 194.240 184.454 1.00 27.52 ? 2963 VAL A CA    1 
ATOM   11774 C C     . VAL A 1 2963 ? 224.761 193.191 185.555 1.00 30.87 ? 2963 VAL A C     1 
ATOM   11775 O O     . VAL A 1 2963 ? 224.407 192.024 185.344 1.00 29.24 ? 2963 VAL A O     1 
ATOM   11776 C CB    . VAL A 1 2963 ? 223.280 194.796 184.273 1.00 26.03 ? 2963 VAL A CB    1 
ATOM   11777 C CG1   . VAL A 1 2963 ? 222.302 193.687 183.909 1.00 29.30 ? 2963 VAL A CG1   1 
ATOM   11778 C CG2   . VAL A 1 2963 ? 222.826 195.512 185.528 1.00 26.33 ? 2963 VAL A CG2   1 
ATOM   11779 N N     . HIS A 1 2964 ? 225.239 193.603 186.728 1.00 36.89 ? 2964 HIS A N     1 
ATOM   11780 C CA    . HIS A 1 2964 ? 225.223 192.774 187.924 1.00 33.72 ? 2964 HIS A CA    1 
ATOM   11781 C C     . HIS A 1 2964 ? 224.800 193.644 189.101 1.00 34.05 ? 2964 HIS A C     1 
ATOM   11782 O O     . HIS A 1 2964 ? 224.419 194.807 188.934 1.00 33.78 ? 2964 HIS A O     1 
ATOM   11783 C CB    . HIS A 1 2964 ? 226.584 192.113 188.170 1.00 33.60 ? 2964 HIS A CB    1 
ATOM   11784 C CG    . HIS A 1 2964 ? 227.745 193.048 188.038 1.00 36.33 ? 2964 HIS A CG    1 
ATOM   11785 N ND1   . HIS A 1 2964 ? 228.198 193.823 189.084 1.00 34.89 ? 2964 HIS A ND1   1 
ATOM   11786 C CD2   . HIS A 1 2964 ? 228.550 193.328 186.986 1.00 35.85 ? 2964 HIS A CD2   1 
ATOM   11787 C CE1   . HIS A 1 2964 ? 229.230 194.542 188.681 1.00 34.69 ? 2964 HIS A CE1   1 
ATOM   11788 N NE2   . HIS A 1 2964 ? 229.464 194.261 187.412 1.00 35.42 ? 2964 HIS A NE2   1 
ATOM   11789 N N     . ARG A 1 2965 ? 224.856 193.071 190.304 1.00 34.56 ? 2965 ARG A N     1 
ATOM   11790 C CA    . ARG A 1 2965 ? 224.436 193.813 191.488 1.00 36.37 ? 2965 ARG A CA    1 
ATOM   11791 C C     . ARG A 1 2965 ? 225.395 194.949 191.823 1.00 38.28 ? 2965 ARG A C     1 
ATOM   11792 O O     . ARG A 1 2965 ? 224.950 196.060 192.134 1.00 35.86 ? 2965 ARG A O     1 
ATOM   11793 C CB    . ARG A 1 2965 ? 224.294 192.868 192.678 1.00 36.96 ? 2965 ARG A CB    1 
ATOM   11794 C CG    . ARG A 1 2965 ? 223.541 193.473 193.847 1.00 37.93 ? 2965 ARG A CG    1 
ATOM   11795 C CD    . ARG A 1 2965 ? 223.451 192.494 195.005 1.00 39.04 ? 2965 ARG A CD    1 
ATOM   11796 N NE    . ARG A 1 2965 ? 222.410 191.493 194.795 1.00 39.37 ? 2965 ARG A NE    1 
ATOM   11797 C CZ    . ARG A 1 2965 ? 221.120 191.756 194.626 1.00 36.63 ? 2965 ARG A CZ    1 
ATOM   11798 N NH1   . ARG A 1 2965 ? 220.641 192.985 194.728 1.00 35.98 ? 2965 ARG A NH1   1 
ATOM   11799 N NH2   . ARG A 1 2965 ? 220.286 190.756 194.363 1.00 33.56 ? 2965 ARG A NH2   1 
ATOM   11800 N N     . LYS A 1 2966 ? 226.700 194.699 191.767 1.00 39.44 ? 2966 LYS A N     1 
ATOM   11801 C CA    . LYS A 1 2966 ? 227.701 195.716 192.061 1.00 40.50 ? 2966 LYS A CA    1 
ATOM   11802 C C     . LYS A 1 2966 ? 227.924 196.676 190.902 1.00 39.17 ? 2966 LYS A C     1 
ATOM   11803 O O     . LYS A 1 2966 ? 228.850 197.491 190.958 1.00 36.95 ? 2966 LYS A O     1 
ATOM   11804 C CB    . LYS A 1 2966 ? 229.028 195.059 192.448 1.00 39.39 ? 2966 LYS A CB    1 
ATOM   11805 C CG    . LYS A 1 2966 ? 228.907 194.001 193.527 1.00 37.51 ? 2966 LYS A CG    1 
ATOM   11806 C CD    . LYS A 1 2966 ? 228.605 194.641 194.871 1.00 38.82 ? 2966 LYS A CD    1 
ATOM   11807 C CE    . LYS A 1 2966 ? 229.748 195.535 195.323 1.00 38.29 ? 2966 LYS A CE    1 
ATOM   11808 N NZ    . LYS A 1 2966 ? 229.472 196.172 196.640 1.00 38.27 ? 2966 LYS A NZ    1 
ATOM   11809 N N     . TYR A 1 2967 ? 227.103 196.599 189.859 1.00 39.27 ? 2967 TYR A N     1 
ATOM   11810 C CA    . TYR A 1 2967 ? 227.258 197.452 188.687 1.00 36.71 ? 2967 TYR A CA    1 
ATOM   11811 C C     . TYR A 1 2967 ? 226.703 198.829 189.034 1.00 37.78 ? 2967 TYR A C     1 
ATOM   11812 O O     . TYR A 1 2967 ? 225.484 199.027 189.066 1.00 38.16 ? 2967 TYR A O     1 
ATOM   11813 C CB    . TYR A 1 2967 ? 226.541 196.827 187.494 1.00 31.24 ? 2967 TYR A CB    1 
ATOM   11814 C CG    . TYR A 1 2967 ? 226.442 197.699 186.266 1.00 34.23 ? 2967 TYR A CG    1 
ATOM   11815 C CD1   . TYR A 1 2967 ? 227.483 197.747 185.350 1.00 35.12 ? 2967 TYR A CD1   1 
ATOM   11816 C CD2   . TYR A 1 2967 ? 225.305 198.452 186.007 1.00 35.37 ? 2967 TYR A CD2   1 
ATOM   11817 C CE1   . TYR A 1 2967 ? 227.403 198.527 184.221 1.00 34.63 ? 2967 TYR A CE1   1 
ATOM   11818 C CE2   . TYR A 1 2967 ? 225.218 199.239 184.878 1.00 32.33 ? 2967 TYR A CE2   1 
ATOM   11819 C CZ    . TYR A 1 2967 ? 226.271 199.271 183.989 1.00 33.57 ? 2967 TYR A CZ    1 
ATOM   11820 O OH    . TYR A 1 2967 ? 226.197 200.047 182.859 1.00 36.90 ? 2967 TYR A OH    1 
ATOM   11821 N N     . THR A 1 2968 ? 227.594 199.775 189.307 1.00 35.40 ? 2968 THR A N     1 
ATOM   11822 C CA    . THR A 1 2968 ? 227.228 201.069 189.861 1.00 34.10 ? 2968 THR A CA    1 
ATOM   11823 C C     . THR A 1 2968 ? 227.052 202.114 188.763 1.00 34.87 ? 2968 THR A C     1 
ATOM   11824 O O     . THR A 1 2968 ? 227.182 201.837 187.569 1.00 37.50 ? 2968 THR A O     1 
ATOM   11825 C CB    . THR A 1 2968 ? 228.281 201.533 190.871 1.00 35.40 ? 2968 THR A CB    1 
ATOM   11826 O OG1   . THR A 1 2968 ? 229.548 201.660 190.216 1.00 39.20 ? 2968 THR A OG1   1 
ATOM   11827 C CG2   . THR A 1 2968 ? 228.404 200.536 192.012 1.00 35.06 ? 2968 THR A CG2   1 
ATOM   11828 N N     . GLY A 1 2969 ? 226.750 203.340 189.198 1.00 29.82 ? 2969 GLY A N     1 
ATOM   11829 C CA    . GLY A 1 2969 ? 226.487 204.418 188.260 1.00 30.18 ? 2969 GLY A CA    1 
ATOM   11830 C C     . GLY A 1 2969 ? 227.691 204.821 187.434 1.00 33.29 ? 2969 GLY A C     1 
ATOM   11831 O O     . GLY A 1 2969 ? 227.557 205.110 186.241 1.00 34.16 ? 2969 GLY A O     1 
ATOM   11832 N N     . GLU A 1 2970 ? 228.877 204.860 188.046 1.00 35.10 ? 2970 GLU A N     1 
ATOM   11833 C CA    . GLU A 1 2970 ? 230.065 205.242 187.288 1.00 36.06 ? 2970 GLU A CA    1 
ATOM   11834 C C     . GLU A 1 2970 ? 230.445 204.162 186.283 1.00 36.18 ? 2970 GLU A C     1 
ATOM   11835 O O     . GLU A 1 2970 ? 231.044 204.459 185.244 1.00 36.39 ? 2970 GLU A O     1 
ATOM   11836 C CB    . GLU A 1 2970 ? 231.229 205.551 188.232 1.00 34.86 ? 2970 GLU A CB    1 
ATOM   11837 C CG    . GLU A 1 2970 ? 231.984 204.340 188.747 1.00 35.18 ? 2970 GLU A CG    1 
ATOM   11838 C CD    . GLU A 1 2970 ? 231.483 203.877 190.097 1.00 37.71 ? 2970 GLU A CD    1 
ATOM   11839 O OE1   . GLU A 1 2970 ? 231.883 202.779 190.536 1.00 39.86 ? 2970 GLU A OE1   1 
ATOM   11840 O OE2   . GLU A 1 2970 ? 230.688 204.611 190.721 1.00 36.59 ? 2970 GLU A OE2   1 
ATOM   11841 N N     . ASP A 1 2971 ? 230.091 202.905 186.562 1.00 31.72 ? 2971 ASP A N     1 
ATOM   11842 C CA    . ASP A 1 2971 ? 230.260 201.857 185.560 1.00 33.95 ? 2971 ASP A CA    1 
ATOM   11843 C C     . ASP A 1 2971 ? 229.389 202.126 184.339 1.00 39.03 ? 2971 ASP A C     1 
ATOM   11844 O O     . ASP A 1 2971 ? 229.840 201.975 183.197 1.00 39.52 ? 2971 ASP A O     1 
ATOM   11845 C CB    . ASP A 1 2971 ? 229.933 200.494 186.166 1.00 32.69 ? 2971 ASP A CB    1 
ATOM   11846 C CG    . ASP A 1 2971 ? 230.763 199.378 185.568 1.00 39.93 ? 2971 ASP A CG    1 
ATOM   11847 O OD1   . ASP A 1 2971 ? 231.546 199.652 184.635 1.00 40.65 ? 2971 ASP A OD1   1 
ATOM   11848 O OD2   . ASP A 1 2971 ? 230.631 198.225 186.029 1.00 40.72 ? 2971 ASP A OD2   1 
ATOM   11849 N N     . PHE A 1 2972 ? 228.138 202.536 184.565 1.00 36.87 ? 2972 PHE A N     1 
ATOM   11850 C CA    . PHE A 1 2972 ? 227.266 202.913 183.458 1.00 32.31 ? 2972 PHE A CA    1 
ATOM   11851 C C     . PHE A 1 2972 ? 227.811 204.124 182.717 1.00 32.81 ? 2972 PHE A C     1 
ATOM   11852 O O     . PHE A 1 2972 ? 227.722 204.200 181.487 1.00 36.19 ? 2972 PHE A O     1 
ATOM   11853 C CB    . PHE A 1 2972 ? 225.854 203.186 183.975 1.00 29.07 ? 2972 PHE A CB    1 
ATOM   11854 C CG    . PHE A 1 2972 ? 224.830 203.366 182.890 1.00 30.38 ? 2972 PHE A CG    1 
ATOM   11855 C CD1   . PHE A 1 2972 ? 224.538 204.626 182.396 1.00 36.09 ? 2972 PHE A CD1   1 
ATOM   11856 C CD2   . PHE A 1 2972 ? 224.159 202.277 182.363 1.00 33.41 ? 2972 PHE A CD2   1 
ATOM   11857 C CE1   . PHE A 1 2972 ? 223.596 204.794 181.400 1.00 32.68 ? 2972 PHE A CE1   1 
ATOM   11858 C CE2   . PHE A 1 2972 ? 223.218 202.440 181.366 1.00 32.72 ? 2972 PHE A CE2   1 
ATOM   11859 C CZ    . PHE A 1 2972 ? 222.936 203.700 180.885 1.00 30.39 ? 2972 PHE A CZ    1 
ATOM   11860 N N     . ASP A 1 2973 ? 228.370 205.088 183.450 1.00 31.44 ? 2973 ASP A N     1 
ATOM   11861 C CA    . ASP A 1 2973 ? 228.957 206.258 182.806 1.00 33.27 ? 2973 ASP A CA    1 
ATOM   11862 C C     . ASP A 1 2973 ? 230.141 205.868 181.929 1.00 36.00 ? 2973 ASP A C     1 
ATOM   11863 O O     . ASP A 1 2973 ? 230.292 206.379 180.814 1.00 37.29 ? 2973 ASP A O     1 
ATOM   11864 C CB    . ASP A 1 2973 ? 229.379 207.278 183.862 1.00 33.93 ? 2973 ASP A CB    1 
ATOM   11865 C CG    . ASP A 1 2973 ? 228.204 207.809 184.659 1.00 35.64 ? 2973 ASP A CG    1 
ATOM   11866 O OD1   . ASP A 1 2973 ? 227.051 207.626 184.214 1.00 32.95 ? 2973 ASP A OD1   1 
ATOM   11867 O OD2   . ASP A 1 2973 ? 228.433 208.409 185.730 1.00 36.92 ? 2973 ASP A OD2   1 
ATOM   11868 N N     . GLU A 1 2974 ? 230.992 204.962 182.415 1.00 33.02 ? 2974 GLU A N     1 
ATOM   11869 C CA    . GLU A 1 2974 ? 232.128 204.505 181.620 1.00 33.65 ? 2974 GLU A CA    1 
ATOM   11870 C C     . GLU A 1 2974 ? 231.668 203.730 180.392 1.00 32.52 ? 2974 GLU A C     1 
ATOM   11871 O O     . GLU A 1 2974 ? 232.249 203.868 179.309 1.00 31.77 ? 2974 GLU A O     1 
ATOM   11872 C CB    . GLU A 1 2974 ? 233.059 203.649 182.479 1.00 32.25 ? 2974 GLU A CB    1 
ATOM   11873 C CG    . GLU A 1 2974 ? 234.292 203.141 181.748 1.00 36.30 ? 2974 GLU A CG    1 
ATOM   11874 C CD    . GLU A 1 2974 ? 235.107 204.260 181.125 1.00 38.08 ? 2974 GLU A CD    1 
ATOM   11875 O OE1   . GLU A 1 2974 ? 235.878 204.914 181.859 1.00 38.35 ? 2974 GLU A OE1   1 
ATOM   11876 O OE2   . GLU A 1 2974 ? 234.980 204.482 179.903 1.00 34.62 ? 2974 GLU A OE2   1 
ATOM   11877 N N     . ASP A 1 2975 ? 230.631 202.903 180.542 1.00 32.21 ? 2975 ASP A N     1 
ATOM   11878 C CA    . ASP A 1 2975 ? 230.095 202.179 179.394 1.00 33.24 ? 2975 ASP A CA    1 
ATOM   11879 C C     . ASP A 1 2975 ? 229.510 203.137 178.363 1.00 33.54 ? 2975 ASP A C     1 
ATOM   11880 O O     . ASP A 1 2975 ? 229.683 202.942 177.154 1.00 34.24 ? 2975 ASP A O     1 
ATOM   11881 C CB    . ASP A 1 2975 ? 229.045 201.172 179.857 1.00 33.31 ? 2975 ASP A CB    1 
ATOM   11882 C CG    . ASP A 1 2975 ? 229.651 199.839 180.248 1.00 37.98 ? 2975 ASP A CG    1 
ATOM   11883 O OD1   . ASP A 1 2975 ? 228.936 199.014 180.856 1.00 39.98 ? 2975 ASP A OD1   1 
ATOM   11884 O OD2   . ASP A 1 2975 ? 230.843 199.616 179.950 1.00 35.10 ? 2975 ASP A OD2   1 
ATOM   11885 N N     . LEU A 1 2976 ? 228.811 204.177 178.825 1.00 29.70 ? 2976 LEU A N     1 
ATOM   11886 C CA    . LEU A 1 2976 ? 228.310 205.201 177.916 1.00 27.77 ? 2976 LEU A CA    1 
ATOM   11887 C C     . LEU A 1 2976 ? 229.455 205.910 177.209 1.00 32.04 ? 2976 LEU A C     1 
ATOM   11888 O O     . LEU A 1 2976 ? 229.379 206.187 176.007 1.00 32.66 ? 2976 LEU A O     1 
ATOM   11889 C CB    . LEU A 1 2976 ? 227.454 206.211 178.678 1.00 28.61 ? 2976 LEU A CB    1 
ATOM   11890 C CG    . LEU A 1 2976 ? 225.958 205.926 178.777 1.00 28.35 ? 2976 LEU A CG    1 
ATOM   11891 C CD1   . LEU A 1 2976 ? 225.238 207.120 179.375 1.00 30.71 ? 2976 LEU A CD1   1 
ATOM   11892 C CD2   . LEU A 1 2976 ? 225.392 205.578 177.414 1.00 31.32 ? 2976 LEU A CD2   1 
ATOM   11893 N N     . ARG A 1 2977 ? 230.525 206.215 177.943 1.00 33.38 ? 2977 ARG A N     1 
ATOM   11894 C CA    . ARG A 1 2977 ? 231.690 206.839 177.329 1.00 34.79 ? 2977 ARG A CA    1 
ATOM   11895 C C     . ARG A 1 2977 ? 232.270 205.951 176.237 1.00 33.97 ? 2977 ARG A C     1 
ATOM   11896 O O     . ARG A 1 2977 ? 232.581 206.427 175.140 1.00 34.79 ? 2977 ARG A O     1 
ATOM   11897 C CB    . ARG A 1 2977 ? 232.741 207.136 178.399 1.00 33.98 ? 2977 ARG A CB    1 
ATOM   11898 C CG    . ARG A 1 2977 ? 232.401 208.321 179.286 1.00 32.99 ? 2977 ARG A CG    1 
ATOM   11899 C CD    . ARG A 1 2977 ? 233.629 208.851 180.004 1.00 33.61 ? 2977 ARG A CD    1 
ATOM   11900 N NE    . ARG A 1 2977 ? 234.141 207.891 180.973 1.00 31.68 ? 2977 ARG A NE    1 
ATOM   11901 C CZ    . ARG A 1 2977 ? 233.669 207.747 182.204 1.00 35.66 ? 2977 ARG A CZ    1 
ATOM   11902 N NH1   . ARG A 1 2977 ? 232.672 208.492 182.654 1.00 31.72 ? 2977 ARG A NH1   1 
ATOM   11903 N NH2   . ARG A 1 2977 ? 234.210 206.833 183.004 1.00 35.18 ? 2977 ARG A NH2   1 
ATOM   11904 N N     . THR A 1 2978 ? 232.398 204.652 176.513 1.00 30.07 ? 2978 THR A N     1 
ATOM   11905 C CA    . THR A 1 2978 ? 232.949 203.730 175.524 1.00 28.63 ? 2978 THR A CA    1 
ATOM   11906 C C     . THR A 1 2978 ? 232.055 203.630 174.293 1.00 30.72 ? 2978 THR A C     1 
ATOM   11907 O O     . THR A 1 2978 ? 232.545 203.648 173.154 1.00 34.03 ? 2978 THR A O     1 
ATOM   11908 C CB    . THR A 1 2978 ? 233.150 202.350 176.153 1.00 26.53 ? 2978 THR A CB    1 
ATOM   11909 O OG1   . THR A 1 2978 ? 234.061 202.453 177.254 1.00 30.62 ? 2978 THR A OG1   1 
ATOM   11910 C CG2   . THR A 1 2978 ? 233.710 201.373 175.132 1.00 26.40 ? 2978 THR A CG2   1 
ATOM   11911 N N     . VAL A 1 2979 ? 230.739 203.530 174.495 1.00 27.56 ? 2979 VAL A N     1 
ATOM   11912 C CA    . VAL A 1 2979 ? 229.845 203.374 173.352 1.00 26.71 ? 2979 VAL A CA    1 
ATOM   11913 C C     . VAL A 1 2979 ? 229.816 204.650 172.518 1.00 27.43 ? 2979 VAL A C     1 
ATOM   11914 O O     . VAL A 1 2979 ? 229.761 204.595 171.285 1.00 27.78 ? 2979 VAL A O     1 
ATOM   11915 C CB    . VAL A 1 2979 ? 228.436 202.935 173.803 1.00 25.10 ? 2979 VAL A CB    1 
ATOM   11916 C CG1   . VAL A 1 2979 ? 227.708 204.038 174.544 1.00 23.93 ? 2979 VAL A CG1   1 
ATOM   11917 C CG2   . VAL A 1 2979 ? 227.620 202.476 172.608 1.00 26.03 ? 2979 VAL A CG2   1 
ATOM   11918 N N     . LEU A 1 2980 ? 229.883 205.819 173.163 1.00 26.35 ? 2980 LEU A N     1 
ATOM   11919 C CA    . LEU A 1 2980 ? 229.915 207.062 172.400 1.00 26.36 ? 2980 LEU A CA    1 
ATOM   11920 C C     . LEU A 1 2980 ? 231.244 207.250 171.679 1.00 27.96 ? 2980 LEU A C     1 
ATOM   11921 O O     . LEU A 1 2980 ? 231.269 207.805 170.575 1.00 30.96 ? 2980 LEU A O     1 
ATOM   11922 C CB    . LEU A 1 2980 ? 229.619 208.255 173.307 1.00 28.18 ? 2980 LEU A CB    1 
ATOM   11923 C CG    . LEU A 1 2980 ? 228.241 208.244 173.968 1.00 25.09 ? 2980 LEU A CG    1 
ATOM   11924 C CD1   . LEU A 1 2980 ? 228.034 209.488 174.808 1.00 27.27 ? 2980 LEU A CD1   1 
ATOM   11925 C CD2   . LEU A 1 2980 ? 227.151 208.116 172.919 1.00 29.41 ? 2980 LEU A CD2   1 
ATOM   11926 N N     . ARG A 1 2981 ? 232.352 206.797 172.274 1.00 29.26 ? 2981 ARG A N     1 
ATOM   11927 C CA    . ARG A 1 2981 ? 233.622 206.824 171.556 1.00 30.68 ? 2981 ARG A CA    1 
ATOM   11928 C C     . ARG A 1 2981 ? 233.573 205.939 170.320 1.00 31.56 ? 2981 ARG A C     1 
ATOM   11929 O O     . ARG A 1 2981 ? 234.049 206.331 169.249 1.00 30.70 ? 2981 ARG A O     1 
ATOM   11930 C CB    . ARG A 1 2981 ? 234.768 206.392 172.472 1.00 30.42 ? 2981 ARG A CB    1 
ATOM   11931 C CG    . ARG A 1 2981 ? 235.064 207.349 173.609 1.00 34.07 ? 2981 ARG A CG    1 
ATOM   11932 C CD    . ARG A 1 2981 ? 235.851 206.656 174.709 1.00 32.92 ? 2981 ARG A CD    1 
ATOM   11933 N NE    . ARG A 1 2981 ? 236.711 207.584 175.432 1.00 36.82 ? 2981 ARG A NE    1 
ATOM   11934 C CZ    . ARG A 1 2981 ? 237.885 208.016 174.990 1.00 35.47 ? 2981 ARG A CZ    1 
ATOM   11935 N NH1   . ARG A 1 2981 ? 238.371 207.623 173.824 1.00 32.61 ? 2981 ARG A NH1   1 
ATOM   11936 N NH2   . ARG A 1 2981 ? 238.587 208.863 175.736 1.00 34.08 ? 2981 ARG A NH2   1 
ATOM   11937 N N     . ARG A 1 2982 ? 232.999 204.740 170.443 1.00 27.90 ? 2982 ARG A N     1 
ATOM   11938 C CA    . ARG A 1 2982 ? 232.901 203.871 169.274 1.00 28.15 ? 2982 ARG A CA    1 
ATOM   11939 C C     . ARG A 1 2982 ? 231.956 204.450 168.227 1.00 29.06 ? 2982 ARG A C     1 
ATOM   11940 O O     . ARG A 1 2982 ? 232.212 204.335 167.023 1.00 32.09 ? 2982 ARG A O     1 
ATOM   11941 C CB    . ARG A 1 2982 ? 232.456 202.466 169.677 1.00 30.02 ? 2982 ARG A CB    1 
ATOM   11942 C CG    . ARG A 1 2982 ? 233.458 201.715 170.532 1.00 29.06 ? 2982 ARG A CG    1 
ATOM   11943 C CD    . ARG A 1 2982 ? 232.877 200.400 171.013 1.00 27.08 ? 2982 ARG A CD    1 
ATOM   11944 N NE    . ARG A 1 2982 ? 232.523 199.541 169.888 1.00 27.56 ? 2982 ARG A NE    1 
ATOM   11945 C CZ    . ARG A 1 2982 ? 231.887 198.383 169.997 1.00 30.27 ? 2982 ARG A CZ    1 
ATOM   11946 N NH1   . ARG A 1 2982 ? 231.535 197.897 171.175 1.00 30.65 ? 2982 ARG A NH1   1 
ATOM   11947 N NH2   . ARG A 1 2982 ? 231.601 197.694 168.897 1.00 29.41 ? 2982 ARG A NH2   1 
ATOM   11948 N N     . SER A 1 2983 ? 230.859 205.074 168.661 1.00 27.63 ? 2983 SER A N     1 
ATOM   11949 C CA    . SER A 1 2983 ? 229.882 205.599 167.713 1.00 27.90 ? 2983 SER A CA    1 
ATOM   11950 C C     . SER A 1 2983 ? 230.424 206.812 166.966 1.00 28.27 ? 2983 SER A C     1 
ATOM   11951 O O     . SER A 1 2983 ? 230.293 206.907 165.741 1.00 31.18 ? 2983 SER A O     1 
ATOM   11952 C CB    . SER A 1 2983 ? 228.588 205.950 168.444 1.00 28.82 ? 2983 SER A CB    1 
ATOM   11953 O OG    . SER A 1 2983 ? 228.636 207.272 168.944 1.00 26.25 ? 2983 SER A OG    1 
ATOM   11954 N N     . GLY A 1 2984 ? 231.033 207.752 167.686 1.00 30.04 ? 2984 GLY A N     1 
ATOM   11955 C CA    . GLY A 1 2984 ? 231.550 208.957 167.067 1.00 31.55 ? 2984 GLY A CA    1 
ATOM   11956 C C     . GLY A 1 2984 ? 232.893 208.764 166.397 1.00 32.05 ? 2984 GLY A C     1 
ATOM   11957 O O     . GLY A 1 2984 ? 233.029 208.971 165.188 1.00 27.74 ? 2984 GLY A O     1 
ATOM   11958 N N     . CYS A 1 2985 ? 233.897 208.371 167.177 1.00 34.06 ? 2985 CYS A N     1 
ATOM   11959 C CA    . CYS A 1 2985 ? 235.217 208.095 166.633 1.00 32.69 ? 2985 CYS A CA    1 
ATOM   11960 C C     . CYS A 1 2985 ? 235.206 206.781 165.861 1.00 31.29 ? 2985 CYS A C     1 
ATOM   11961 O O     . CYS A 1 2985 ? 234.419 205.877 166.157 1.00 30.15 ? 2985 CYS A O     1 
ATOM   11962 C CB    . CYS A 1 2985 ? 236.256 208.041 167.752 1.00 32.95 ? 2985 CYS A CB    1 
ATOM   11963 S SG    . CYS A 1 2985 ? 236.041 209.300 169.031 1.00 34.13 ? 2985 CYS A SG    1 
ATOM   11964 N N     . LYS A 1 2986 ? 236.072 206.697 164.849 1.00 35.71 ? 2986 LYS A N     1 
ATOM   11965 C CA    . LYS A 1 2986 ? 236.221 205.522 163.993 1.00 33.21 ? 2986 LYS A CA    1 
ATOM   11966 C C     . LYS A 1 2986 ? 234.981 205.261 163.143 1.00 30.16 ? 2986 LYS A C     1 
ATOM   11967 O O     . LYS A 1 2986 ? 234.958 204.305 162.361 1.00 32.51 ? 2986 LYS A O     1 
ATOM   11968 C CB    . LYS A 1 2986 ? 236.568 204.278 164.821 1.00 29.45 ? 2986 LYS A CB    1 
ATOM   11969 C CG    . LYS A 1 2986 ? 237.811 204.429 165.684 1.00 29.28 ? 2986 LYS A CG    1 
ATOM   11970 C CD    . LYS A 1 2986 ? 237.850 203.395 166.800 1.00 33.17 ? 2986 LYS A CD    1 
ATOM   11971 C CE    . LYS A 1 2986 ? 236.600 203.449 167.657 1.00 33.62 ? 2986 LYS A CE    1 
ATOM   11972 N NZ    . LYS A 1 2986 ? 236.417 204.789 168.275 1.00 28.05 ? 2986 LYS A NZ    1 
ATOM   11973 N N     . ASN A 1 2987 ? 233.959 206.107 163.278 1.00 26.18 ? 2987 ASN A N     1 
ATOM   11974 C CA    . ASN A 1 2987 ? 232.751 206.053 162.454 1.00 27.02 ? 2987 ASN A CA    1 
ATOM   11975 C C     . ASN A 1 2987 ? 232.156 204.645 162.428 1.00 30.73 ? 2987 ASN A C     1 
ATOM   11976 O O     . ASN A 1 2987 ? 231.972 204.032 161.375 1.00 31.20 ? 2987 ASN A O     1 
ATOM   11977 C CB    . ASN A 1 2987 ? 233.040 206.551 161.036 1.00 29.00 ? 2987 ASN A CB    1 
ATOM   11978 C CG    . ASN A 1 2987 ? 231.782 206.930 160.285 1.00 28.83 ? 2987 ASN A CG    1 
ATOM   11979 O OD1   . ASN A 1 2987 ? 230.977 207.730 160.761 1.00 27.62 ? 2987 ASN A OD1   1 
ATOM   11980 N ND2   . ASN A 1 2987 ? 231.602 206.353 159.103 1.00 29.20 ? 2987 ASN A ND2   1 
ATOM   11981 N N     . GLU A 1 2988 ? 231.855 204.137 163.617 1.00 30.11 ? 2988 GLU A N     1 
ATOM   11982 C CA    . GLU A 1 2988 ? 231.328 202.791 163.785 1.00 27.12 ? 2988 GLU A CA    1 
ATOM   11983 C C     . GLU A 1 2988 ? 229.865 202.868 164.194 1.00 23.18 ? 2988 GLU A C     1 
ATOM   11984 O O     . GLU A 1 2988 ? 229.526 203.528 165.181 1.00 23.61 ? 2988 GLU A O     1 
ATOM   11985 C CB    . GLU A 1 2988 ? 232.138 202.015 164.826 1.00 25.97 ? 2988 GLU A CB    1 
ATOM   11986 C CG    . GLU A 1 2988 ? 232.006 200.508 164.725 1.00 26.12 ? 2988 GLU A CG    1 
ATOM   11987 C CD    . GLU A 1 2988 ? 232.186 199.820 166.062 1.00 30.80 ? 2988 GLU A CD    1 
ATOM   11988 O OE1   . GLU A 1 2988 ? 232.993 200.310 166.880 1.00 29.07 ? 2988 GLU A OE1   1 
ATOM   11989 O OE2   . GLU A 1 2988 ? 231.527 198.787 166.293 1.00 27.97 ? 2988 GLU A OE2   1 
ATOM   11990 N N     . LYS A 1 2989 ? 229.006 202.199 163.431 1.00 17.45 ? 2989 LYS A N     1 
ATOM   11991 C CA    . LYS A 1 2989 ? 227.572 202.179 163.708 1.00 22.00 ? 2989 LYS A CA    1 
ATOM   11992 C C     . LYS A 1 2989 ? 227.321 201.179 164.828 1.00 25.16 ? 2989 LYS A C     1 
ATOM   11993 O O     . LYS A 1 2989 ? 227.721 200.016 164.742 1.00 24.96 ? 2989 LYS A O     1 
ATOM   11994 C CB    . LYS A 1 2989 ? 226.791 201.828 162.447 1.00 20.19 ? 2989 LYS A CB    1 
ATOM   11995 C CG    . LYS A 1 2989 ? 226.488 203.030 161.568 1.00 20.13 ? 2989 LYS A CG    1 
ATOM   11996 C CD    . LYS A 1 2989 ? 225.069 202.991 161.028 1.00 18.45 ? 2989 LYS A CD    1 
ATOM   11997 C CE    . LYS A 1 2989 ? 224.897 201.873 160.016 1.00 22.72 ? 2989 LYS A CE    1 
ATOM   11998 N NZ    . LYS A 1 2989 ? 223.625 202.003 159.253 1.00 27.59 ? 2989 LYS A NZ    1 
ATOM   11999 N N     . ILE A 1 2990 ? 226.663 201.633 165.891 1.00 22.04 ? 2990 ILE A N     1 
ATOM   12000 C CA    . ILE A 1 2990 ? 226.445 200.830 167.088 1.00 17.48 ? 2990 ILE A CA    1 
ATOM   12001 C C     . ILE A 1 2990 ? 224.951 200.608 167.269 1.00 14.70 ? 2990 ILE A C     1 
ATOM   12002 O O     . ILE A 1 2990 ? 224.174 201.568 167.323 1.00 16.16 ? 2990 ILE A O     1 
ATOM   12003 C CB    . ILE A 1 2990 ? 227.050 201.502 168.329 1.00 20.89 ? 2990 ILE A CB    1 
ATOM   12004 C CG1   . ILE A 1 2990 ? 228.568 201.616 168.192 1.00 20.18 ? 2990 ILE A CG1   1 
ATOM   12005 C CG2   . ILE A 1 2990 ? 226.679 200.726 169.581 1.00 19.16 ? 2990 ILE A CG2   1 
ATOM   12006 C CD1   . ILE A 1 2990 ? 229.258 200.290 168.014 1.00 21.02 ? 2990 ILE A CD1   1 
ATOM   12007 N N     . ALA A 1 2991 ? 224.551 199.344 167.362 1.00 20.11 ? 2991 ALA A N     1 
ATOM   12008 C CA    . ALA A 1 2991 ? 223.194 198.978 167.768 1.00 17.90 ? 2991 ALA A CA    1 
ATOM   12009 C C     . ALA A 1 2991 ? 223.173 198.620 169.252 1.00 13.94 ? 2991 ALA A C     1 
ATOM   12010 O O     . ALA A 1 2991 ? 223.081 197.461 169.650 1.00 20.66 ? 2991 ALA A O     1 
ATOM   12011 C CB    . ALA A 1 2991 ? 222.672 197.832 166.908 1.00 16.98 ? 2991 ALA A CB    1 
ATOM   12012 N N     . PHE A 1 2992 ? 223.276 199.657 170.075 1.00 14.57 ? 2992 PHE A N     1 
ATOM   12013 C CA    . PHE A 1 2992 ? 223.383 199.477 171.515 1.00 16.58 ? 2992 PHE A CA    1 
ATOM   12014 C C     . PHE A 1 2992 ? 222.009 199.176 172.106 1.00 17.10 ? 2992 PHE A C     1 
ATOM   12015 O O     . PHE A 1 2992 ? 221.076 199.973 171.974 1.00 16.50 ? 2992 PHE A O     1 
ATOM   12016 C CB    . PHE A 1 2992 ? 223.998 200.733 172.133 1.00 18.78 ? 2992 PHE A CB    1 
ATOM   12017 C CG    . PHE A 1 2992 ? 223.733 200.901 173.596 1.00 20.66 ? 2992 PHE A CG    1 
ATOM   12018 C CD1   . PHE A 1 2992 ? 224.435 200.157 174.526 1.00 22.65 ? 2992 PHE A CD1   1 
ATOM   12019 C CD2   . PHE A 1 2992 ? 222.817 201.834 174.046 1.00 16.94 ? 2992 PHE A CD2   1 
ATOM   12020 C CE1   . PHE A 1 2992 ? 224.209 200.320 175.873 1.00 18.73 ? 2992 PHE A CE1   1 
ATOM   12021 C CE2   . PHE A 1 2992 ? 222.588 202.000 175.395 1.00 19.91 ? 2992 PHE A CE2   1 
ATOM   12022 C CZ    . PHE A 1 2992 ? 223.289 201.245 176.308 1.00 17.76 ? 2992 PHE A CZ    1 
ATOM   12023 N N     . ILE A 1 2993 ? 221.887 198.023 172.765 1.00 18.41 ? 2993 ILE A N     1 
ATOM   12024 C CA    . ILE A 1 2993 ? 220.600 197.489 173.192 1.00 20.41 ? 2993 ILE A CA    1 
ATOM   12025 C C     . ILE A 1 2993 ? 220.586 197.291 174.703 1.00 17.89 ? 2993 ILE A C     1 
ATOM   12026 O O     . ILE A 1 2993 ? 221.584 196.907 175.317 1.00 21.09 ? 2993 ILE A O     1 
ATOM   12027 C CB    . ILE A 1 2993 ? 220.258 196.166 172.464 1.00 19.27 ? 2993 ILE A CB    1 
ATOM   12028 C CG1   . ILE A 1 2993 ? 218.823 195.730 172.758 1.00 18.41 ? 2993 ILE A CG1   1 
ATOM   12029 C CG2   . ILE A 1 2993 ? 221.247 195.078 172.808 1.00 17.67 ? 2993 ILE A CG2   1 
ATOM   12030 C CD1   . ILE A 1 2993 ? 218.333 194.631 171.853 1.00 17.81 ? 2993 ILE A CD1   1 
ATOM   12031 N N     . MET A 1 2994 ? 219.432 197.584 175.301 1.00 17.85 ? 2994 MET A N     1 
ATOM   12032 C CA    . MET A 1 2994 ? 219.229 197.406 176.731 1.00 20.51 ? 2994 MET A CA    1 
ATOM   12033 C C     . MET A 1 2994 ? 217.872 196.769 176.977 1.00 21.84 ? 2994 MET A C     1 
ATOM   12034 O O     . MET A 1 2994 ? 216.949 196.891 176.170 1.00 25.79 ? 2994 MET A O     1 
ATOM   12035 C CB    . MET A 1 2994 ? 219.314 198.730 177.497 1.00 19.75 ? 2994 MET A CB    1 
ATOM   12036 C CG    . MET A 1 2994 ? 220.625 199.462 177.354 1.00 23.28 ? 2994 MET A CG    1 
ATOM   12037 S SD    . MET A 1 2994 ? 220.821 200.744 178.605 1.00 35.76 ? 2994 MET A SD    1 
ATOM   12038 C CE    . MET A 1 2994 ? 220.086 199.939 180.024 1.00 26.73 ? 2994 MET A CE    1 
ATOM   12039 N N     . ASP A 1 2995 ? 217.763 196.091 178.115 1.00 22.77 ? 2995 ASP A N     1 
ATOM   12040 C CA    . ASP A 1 2995 ? 216.522 195.493 178.578 1.00 19.99 ? 2995 ASP A CA    1 
ATOM   12041 C C     . ASP A 1 2995 ? 216.146 196.076 179.934 1.00 24.35 ? 2995 ASP A C     1 
ATOM   12042 O O     . ASP A 1 2995 ? 216.858 196.910 180.497 1.00 32.38 ? 2995 ASP A O     1 
ATOM   12043 C CB    . ASP A 1 2995 ? 216.640 193.965 178.658 1.00 21.49 ? 2995 ASP A CB    1 
ATOM   12044 C CG    . ASP A 1 2995 ? 217.848 193.513 179.448 1.00 30.51 ? 2995 ASP A CG    1 
ATOM   12045 O OD1   . ASP A 1 2995 ? 217.685 192.697 180.379 1.00 31.81 ? 2995 ASP A OD1   1 
ATOM   12046 O OD2   . ASP A 1 2995 ? 218.967 193.963 179.126 1.00 29.48 ? 2995 ASP A OD2   1 
ATOM   12047 N N     . GLU A 1 2996 ? 214.996 195.639 180.450 1.00 23.37 ? 2996 GLU A N     1 
ATOM   12048 C CA    . GLU A 1 2996 ? 214.554 196.116 181.756 1.00 25.13 ? 2996 GLU A CA    1 
ATOM   12049 C C     . GLU A 1 2996 ? 215.434 195.582 182.878 1.00 31.13 ? 2996 GLU A C     1 
ATOM   12050 O O     . GLU A 1 2996 ? 215.709 196.302 183.845 1.00 30.95 ? 2996 GLU A O     1 
ATOM   12051 C CB    . GLU A 1 2996 ? 213.092 195.737 181.990 1.00 27.82 ? 2996 GLU A CB    1 
ATOM   12052 C CG    . GLU A 1 2996 ? 212.812 194.248 181.941 1.00 29.02 ? 2996 GLU A CG    1 
ATOM   12053 C CD    . GLU A 1 2996 ? 211.341 193.940 182.085 1.00 29.29 ? 2996 GLU A CD    1 
ATOM   12054 O OE1   . GLU A 1 2996 ? 210.549 194.900 182.188 1.00 31.62 ? 2996 GLU A OE1   1 
ATOM   12055 O OE2   . GLU A 1 2996 ? 210.977 192.745 182.097 1.00 29.13 ? 2996 GLU A OE2   1 
ATOM   12056 N N     . SER A 1 2997 ? 215.887 194.331 182.772 1.00 29.88 ? 2997 SER A N     1 
ATOM   12057 C CA    . SER A 1 2997 ? 216.803 193.787 183.767 1.00 30.02 ? 2997 SER A CA    1 
ATOM   12058 C C     . SER A 1 2997 ? 218.153 194.486 183.740 1.00 27.95 ? 2997 SER A C     1 
ATOM   12059 O O     . SER A 1 2997 ? 218.924 194.361 184.697 1.00 29.99 ? 2997 SER A O     1 
ATOM   12060 C CB    . SER A 1 2997 ? 216.991 192.284 183.548 1.00 29.52 ? 2997 SER A CB    1 
ATOM   12061 O OG    . SER A 1 2997 ? 217.733 191.701 184.606 1.00 31.07 ? 2997 SER A OG    1 
ATOM   12062 N N     . ASN A 1 2998 ? 218.452 195.215 182.668 1.00 28.45 ? 2998 ASN A N     1 
ATOM   12063 C CA    . ASN A 1 2998 ? 219.688 195.971 182.544 1.00 28.52 ? 2998 ASN A CA    1 
ATOM   12064 C C     . ASN A 1 2998 ? 219.657 197.277 183.327 1.00 26.56 ? 2998 ASN A C     1 
ATOM   12065 O O     . ASN A 1 2998 ? 220.719 197.843 183.604 1.00 29.37 ? 2998 ASN A O     1 
ATOM   12066 C CB    . ASN A 1 2998 ? 219.962 196.251 181.064 1.00 27.48 ? 2998 ASN A CB    1 
ATOM   12067 C CG    . ASN A 1 2998 ? 221.427 196.473 180.769 1.00 30.85 ? 2998 ASN A CG    1 
ATOM   12068 O OD1   . ASN A 1 2998 ? 222.079 197.310 181.386 1.00 31.09 ? 2998 ASN A OD1   1 
ATOM   12069 N ND2   . ASN A 1 2998 ? 221.955 195.712 179.817 1.00 28.14 ? 2998 ASN A ND2   1 
ATOM   12070 N N     . VAL A 1 2999 ? 218.477 197.754 183.712 1.00 23.25 ? 2999 VAL A N     1 
ATOM   12071 C CA    . VAL A 1 2999 ? 218.324 199.016 184.426 1.00 28.81 ? 2999 VAL A CA    1 
ATOM   12072 C C     . VAL A 1 2999 ? 218.108 198.705 185.898 1.00 31.24 ? 2999 VAL A C     1 
ATOM   12073 O O     . VAL A 1 2999 ? 217.155 198.000 186.256 1.00 34.88 ? 2999 VAL A O     1 
ATOM   12074 C CB    . VAL A 1 2999 ? 217.159 199.851 183.872 1.00 29.50 ? 2999 VAL A CB    1 
ATOM   12075 C CG1   . VAL A 1 2999 ? 216.936 201.081 184.735 1.00 28.62 ? 2999 VAL A CG1   1 
ATOM   12076 C CG2   . VAL A 1 2999 ? 217.425 200.247 182.433 1.00 29.22 ? 2999 VAL A CG2   1 
ATOM   12077 N N     . LEU A 1 3000 ? 218.990 199.227 186.748 1.00 30.87 ? 3000 LEU A N     1 
ATOM   12078 C CA    . LEU A 1 3000 ? 218.840 199.115 188.189 1.00 32.89 ? 3000 LEU A CA    1 
ATOM   12079 C C     . LEU A 1 3000 ? 218.760 200.462 188.890 1.00 35.69 ? 3000 LEU A C     1 
ATOM   12080 O O     . LEU A 1 3000 ? 218.378 200.505 190.065 1.00 36.64 ? 3000 LEU A O     1 
ATOM   12081 C CB    . LEU A 1 3000 ? 219.998 198.299 188.791 1.00 33.38 ? 3000 LEU A CB    1 
ATOM   12082 C CG    . LEU A 1 3000 ? 221.436 198.775 188.558 1.00 36.51 ? 3000 LEU A CG    1 
ATOM   12083 C CD1   . LEU A 1 3000 ? 221.910 199.713 189.663 1.00 34.55 ? 3000 LEU A CD1   1 
ATOM   12084 C CD2   . LEU A 1 3000 ? 222.377 197.589 188.432 1.00 33.85 ? 3000 LEU A CD2   1 
ATOM   12085 N N     . ASP A 1 3001 ? 219.100 201.555 188.210 1.00 34.02 ? 3001 ASP A N     1 
ATOM   12086 C CA    . ASP A 1 3001 ? 219.101 202.885 188.798 1.00 34.04 ? 3001 ASP A CA    1 
ATOM   12087 C C     . ASP A 1 3001 ? 218.407 203.844 187.844 1.00 34.51 ? 3001 ASP A C     1 
ATOM   12088 O O     . ASP A 1 3001 ? 218.515 203.703 186.623 1.00 31.51 ? 3001 ASP A O     1 
ATOM   12089 C CB    . ASP A 1 3001 ? 220.533 203.362 189.086 1.00 33.95 ? 3001 ASP A CB    1 
ATOM   12090 C CG    . ASP A 1 3001 ? 220.576 204.622 189.933 1.00 38.40 ? 3001 ASP A CG    1 
ATOM   12091 O OD1   . ASP A 1 3001 ? 219.503 205.189 190.230 1.00 41.92 ? 3001 ASP A OD1   1 
ATOM   12092 O OD2   . ASP A 1 3001 ? 221.691 205.051 190.299 1.00 34.89 ? 3001 ASP A OD2   1 
ATOM   12093 N N     . SER A 1 3002 ? 217.692 204.820 188.409 1.00 30.59 ? 3002 SER A N     1 
ATOM   12094 C CA    . SER A 1 3002 ? 217.001 205.804 187.580 1.00 29.13 ? 3002 SER A CA    1 
ATOM   12095 C C     . SER A 1 3002 ? 217.982 206.732 186.877 1.00 30.54 ? 3002 SER A C     1 
ATOM   12096 O O     . SER A 1 3002 ? 217.618 207.393 185.895 1.00 35.12 ? 3002 SER A O     1 
ATOM   12097 C CB    . SER A 1 3002 ? 216.020 206.610 188.430 1.00 30.41 ? 3002 SER A CB    1 
ATOM   12098 O OG    . SER A 1 3002 ? 215.330 207.564 187.641 1.00 34.32 ? 3002 SER A OG    1 
ATOM   12099 N N     . GLY A 1 3003 ? 219.222 206.804 187.363 1.00 24.83 ? 3003 GLY A N     1 
ATOM   12100 C CA    . GLY A 1 3003 ? 220.231 207.589 186.677 1.00 28.60 ? 3003 GLY A CA    1 
ATOM   12101 C C     . GLY A 1 3003 ? 220.513 207.083 185.278 1.00 32.88 ? 3003 GLY A C     1 
ATOM   12102 O O     . GLY A 1 3003 ? 220.847 207.866 184.383 1.00 30.41 ? 3003 GLY A O     1 
ATOM   12103 N N     . PHE A 1 3004 ? 220.382 205.771 185.066 1.00 31.06 ? 3004 PHE A N     1 
ATOM   12104 C CA    . PHE A 1 3004 ? 220.529 205.227 183.722 1.00 25.45 ? 3004 PHE A CA    1 
ATOM   12105 C C     . PHE A 1 3004 ? 219.507 205.848 182.781 1.00 30.18 ? 3004 PHE A C     1 
ATOM   12106 O O     . PHE A 1 3004 ? 219.861 206.338 181.702 1.00 34.91 ? 3004 PHE A O     1 
ATOM   12107 C CB    . PHE A 1 3004 ? 220.376 203.703 183.732 1.00 26.20 ? 3004 PHE A CB    1 
ATOM   12108 C CG    . PHE A 1 3004 ? 221.313 202.981 184.674 1.00 29.68 ? 3004 PHE A CG    1 
ATOM   12109 C CD1   . PHE A 1 3004 ? 222.353 203.639 185.314 1.00 29.91 ? 3004 PHE A CD1   1 
ATOM   12110 C CD2   . PHE A 1 3004 ? 221.146 201.627 184.912 1.00 31.53 ? 3004 PHE A CD2   1 
ATOM   12111 C CE1   . PHE A 1 3004 ? 223.195 202.963 186.175 1.00 31.11 ? 3004 PHE A CE1   1 
ATOM   12112 C CE2   . PHE A 1 3004 ? 221.988 200.947 185.768 1.00 30.77 ? 3004 PHE A CE2   1 
ATOM   12113 C CZ    . PHE A 1 3004 ? 223.014 201.615 186.399 1.00 30.87 ? 3004 PHE A CZ    1 
ATOM   12114 N N     . LEU A 1 3005 ? 218.236 205.860 183.189 1.00 29.16 ? 3005 LEU A N     1 
ATOM   12115 C CA    . LEU A 1 3005 ? 217.196 206.464 182.364 1.00 29.59 ? 3005 LEU A CA    1 
ATOM   12116 C C     . LEU A 1 3005 ? 217.402 207.965 182.221 1.00 31.71 ? 3005 LEU A C     1 
ATOM   12117 O O     . LEU A 1 3005 ? 217.089 208.538 181.173 1.00 28.58 ? 3005 LEU A O     1 
ATOM   12118 C CB    . LEU A 1 3005 ? 215.817 206.163 182.947 1.00 29.49 ? 3005 LEU A CB    1 
ATOM   12119 C CG    . LEU A 1 3005 ? 215.577 204.698 183.300 1.00 30.24 ? 3005 LEU A CG    1 
ATOM   12120 C CD1   . LEU A 1 3005 ? 214.382 204.549 184.231 1.00 28.22 ? 3005 LEU A CD1   1 
ATOM   12121 C CD2   . LEU A 1 3005 ? 215.392 203.895 182.024 1.00 27.45 ? 3005 LEU A CD2   1 
ATOM   12122 N N     . GLU A 1 3006 ? 217.926 208.622 183.260 1.00 28.37 ? 3006 GLU A N     1 
ATOM   12123 C CA    . GLU A 1 3006 ? 218.217 210.047 183.138 1.00 26.37 ? 3006 GLU A CA    1 
ATOM   12124 C C     . GLU A 1 3006 ? 219.273 210.313 182.073 1.00 28.08 ? 3006 GLU A C     1 
ATOM   12125 O O     . GLU A 1 3006 ? 219.158 211.285 181.318 1.00 31.91 ? 3006 GLU A O     1 
ATOM   12126 C CB    . GLU A 1 3006 ? 218.668 210.621 184.479 1.00 25.62 ? 3006 GLU A CB    1 
ATOM   12127 C CG    . GLU A 1 3006 ? 218.492 212.132 184.586 1.00 28.49 ? 3006 GLU A CG    1 
ATOM   12128 C CD    . GLU A 1 3006 ? 219.742 212.912 184.219 1.00 30.20 ? 3006 GLU A CD    1 
ATOM   12129 O OE1   . GLU A 1 3006 ? 219.696 214.160 184.266 1.00 29.67 ? 3006 GLU A OE1   1 
ATOM   12130 O OE2   . GLU A 1 3006 ? 220.771 212.285 183.889 1.00 30.57 ? 3006 GLU A OE2   1 
ATOM   12131 N N     . ARG A 1 3007 ? 220.309 209.476 182.004 1.00 25.49 ? 3007 ARG A N     1 
ATOM   12132 C CA    . ARG A 1 3007 ? 221.321 209.640 180.963 1.00 27.40 ? 3007 ARG A CA    1 
ATOM   12133 C C     . ARG A 1 3007 ? 220.754 209.326 179.583 1.00 27.86 ? 3007 ARG A C     1 
ATOM   12134 O O     . ARG A 1 3007 ? 221.019 210.048 178.613 1.00 28.35 ? 3007 ARG A O     1 
ATOM   12135 C CB    . ARG A 1 3007 ? 222.539 208.767 181.261 1.00 26.60 ? 3007 ARG A CB    1 
ATOM   12136 C CG    . ARG A 1 3007 ? 223.170 209.034 182.610 1.00 29.43 ? 3007 ARG A CG    1 
ATOM   12137 C CD    . ARG A 1 3007 ? 223.613 210.483 182.718 1.00 29.98 ? 3007 ARG A CD    1 
ATOM   12138 N NE    . ARG A 1 3007 ? 224.624 210.671 183.752 1.00 30.69 ? 3007 ARG A NE    1 
ATOM   12139 C CZ    . ARG A 1 3007 ? 225.923 210.781 183.515 1.00 31.64 ? 3007 ARG A CZ    1 
ATOM   12140 N NH1   . ARG A 1 3007 ? 226.409 210.722 182.286 1.00 29.06 ? 3007 ARG A NH1   1 
ATOM   12141 N NH2   . ARG A 1 3007 ? 226.757 210.953 184.536 1.00 31.53 ? 3007 ARG A NH2   1 
ATOM   12142 N N     . MET A 1 3008 ? 219.972 208.247 179.470 1.00 26.93 ? 3008 MET A N     1 
ATOM   12143 C CA    . MET A 1 3008 ? 219.376 207.935 178.175 1.00 26.98 ? 3008 MET A CA    1 
ATOM   12144 C C     . MET A 1 3008 ? 218.381 208.994 177.724 1.00 27.57 ? 3008 MET A C     1 
ATOM   12145 O O     . MET A 1 3008 ? 218.177 209.151 176.520 1.00 31.13 ? 3008 MET A O     1 
ATOM   12146 C CB    . MET A 1 3008 ? 218.696 206.562 178.177 1.00 28.72 ? 3008 MET A CB    1 
ATOM   12147 C CG    . MET A 1 3008 ? 219.440 205.469 178.912 1.00 28.06 ? 3008 MET A CG    1 
ATOM   12148 S SD    . MET A 1 3008 ? 221.023 205.049 178.158 1.00 35.46 ? 3008 MET A SD    1 
ATOM   12149 C CE    . MET A 1 3008 ? 220.588 205.042 176.422 1.00 25.97 ? 3008 MET A CE    1 
ATOM   12150 N N     . ASN A 1 3009 ? 217.771 209.734 178.650 1.00 26.70 ? 3009 ASN A N     1 
ATOM   12151 C CA    . ASN A 1 3009 ? 216.878 210.816 178.249 1.00 27.01 ? 3009 ASN A CA    1 
ATOM   12152 C C     . ASN A 1 3009 ? 217.606 211.819 177.363 1.00 27.27 ? 3009 ASN A C     1 
ATOM   12153 O O     . ASN A 1 3009 ? 217.123 212.182 176.283 1.00 32.18 ? 3009 ASN A O     1 
ATOM   12154 C CB    . ASN A 1 3009 ? 216.302 211.501 179.488 1.00 24.99 ? 3009 ASN A CB    1 
ATOM   12155 C CG    . ASN A 1 3009 ? 215.185 212.467 179.155 1.00 28.59 ? 3009 ASN A CG    1 
ATOM   12156 O OD1   . ASN A 1 3009 ? 214.407 212.239 178.231 1.00 30.31 ? 3009 ASN A OD1   1 
ATOM   12157 N ND2   . ASN A 1 3009 ? 215.102 213.556 179.908 1.00 28.28 ? 3009 ASN A ND2   1 
ATOM   12158 N N     . THR A 1 3010 ? 218.791 212.256 177.792 1.00 26.78 ? 3010 THR A N     1 
ATOM   12159 C CA    . THR A 1 3010 ? 219.585 213.174 176.986 1.00 28.39 ? 3010 THR A CA    1 
ATOM   12160 C C     . THR A 1 3010 ? 220.234 212.478 175.796 1.00 27.05 ? 3010 THR A C     1 
ATOM   12161 O O     . THR A 1 3010 ? 220.401 213.099 174.740 1.00 28.14 ? 3010 THR A O     1 
ATOM   12162 C CB    . THR A 1 3010 ? 220.658 213.841 177.848 1.00 29.99 ? 3010 THR A CB    1 
ATOM   12163 O OG1   . THR A 1 3010 ? 221.556 212.845 178.354 1.00 31.98 ? 3010 THR A OG1   1 
ATOM   12164 C CG2   . THR A 1 3010 ? 220.017 214.576 179.016 1.00 26.94 ? 3010 THR A CG2   1 
ATOM   12165 N N     . LEU A 1 3011 ? 220.607 211.204 175.942 1.00 25.62 ? 3011 LEU A N     1 
ATOM   12166 C CA    . LEU A 1 3011 ? 221.204 210.483 174.821 1.00 28.59 ? 3011 LEU A CA    1 
ATOM   12167 C C     . LEU A 1 3011 ? 220.213 210.286 173.681 1.00 22.57 ? 3011 LEU A C     1 
ATOM   12168 O O     . LEU A 1 3011 ? 220.621 210.167 172.520 1.00 23.50 ? 3011 LEU A O     1 
ATOM   12169 C CB    . LEU A 1 3011 ? 221.742 209.131 175.287 1.00 28.46 ? 3011 LEU A CB    1 
ATOM   12170 C CG    . LEU A 1 3011 ? 222.657 208.402 174.302 1.00 26.02 ? 3011 LEU A CG    1 
ATOM   12171 C CD1   . LEU A 1 3011 ? 223.701 209.346 173.728 1.00 28.98 ? 3011 LEU A CD1   1 
ATOM   12172 C CD2   . LEU A 1 3011 ? 223.315 207.207 174.961 1.00 25.23 ? 3011 LEU A CD2   1 
ATOM   12173 N N     . LEU A 1 3012 ? 218.919 210.239 173.987 1.00 20.71 ? 3012 LEU A N     1 
ATOM   12174 C CA    . LEU A 1 3012 ? 217.895 210.039 172.969 1.00 23.63 ? 3012 LEU A CA    1 
ATOM   12175 C C     . LEU A 1 3012 ? 217.362 211.373 172.454 1.00 24.57 ? 3012 LEU A C     1 
ATOM   12176 O O     . LEU A 1 3012 ? 217.406 211.642 171.250 1.00 21.89 ? 3012 LEU A O     1 
ATOM   12177 C CB    . LEU A 1 3012 ? 216.750 209.189 173.531 1.00 24.80 ? 3012 LEU A CB    1 
ATOM   12178 C CG    . LEU A 1 3012 ? 217.062 207.770 174.015 1.00 23.80 ? 3012 LEU A CG    1 
ATOM   12179 C CD1   . LEU A 1 3012 ? 215.905 207.232 174.843 1.00 21.97 ? 3012 LEU A CD1   1 
ATOM   12180 C CD2   . LEU A 1 3012 ? 217.384 206.841 172.867 1.00 21.19 ? 3012 LEU A CD2   1 
ATOM   12181 N N     . ALA A 1 3013 ? 216.860 212.217 173.361 1.00 30.30 ? 3013 ALA A N     1 
ATOM   12182 C CA    . ALA A 1 3013 ? 216.200 213.451 172.946 1.00 27.21 ? 3013 ALA A CA    1 
ATOM   12183 C C     . ALA A 1 3013 ? 217.160 214.375 172.206 1.00 25.94 ? 3013 ALA A C     1 
ATOM   12184 O O     . ALA A 1 3013 ? 216.827 214.914 171.145 1.00 31.20 ? 3013 ALA A O     1 
ATOM   12185 C CB    . ALA A 1 3013 ? 215.602 214.157 174.163 1.00 21.64 ? 3013 ALA A CB    1 
ATOM   12186 N N     . ASN A 1 3014 ? 218.362 214.564 172.746 1.00 26.73 ? 3014 ASN A N     1 
ATOM   12187 C CA    . ASN A 1 3014 ? 219.335 215.476 172.160 1.00 30.80 ? 3014 ASN A CA    1 
ATOM   12188 C C     . ASN A 1 3014 ? 220.540 214.780 171.552 1.00 29.81 ? 3014 ASN A C     1 
ATOM   12189 O O     . ASN A 1 3014 ? 221.230 215.379 170.726 1.00 22.79 ? 3014 ASN A O     1 
ATOM   12190 C CB    . ASN A 1 3014 ? 219.820 216.482 173.211 1.00 30.27 ? 3014 ASN A CB    1 
ATOM   12191 C CG    . ASN A 1 3014 ? 218.800 217.568 173.488 1.00 34.02 ? 3014 ASN A CG    1 
ATOM   12192 O OD1   . ASN A 1 3014 ? 217.745 217.620 172.857 1.00 32.02 ? 3014 ASN A OD1   1 
ATOM   12193 N ND2   . ASN A 1 3014 ? 219.110 218.442 174.438 1.00 33.61 ? 3014 ASN A ND2   1 
ATOM   12194 N N     . GLY A 1 3015 ? 220.811 213.537 171.941 1.00 36.19 ? 3015 GLY A N     1 
ATOM   12195 C CA    . GLY A 1 3015 ? 221.917 212.789 171.389 1.00 33.83 ? 3015 GLY A CA    1 
ATOM   12196 C C     . GLY A 1 3015 ? 223.258 213.058 172.026 1.00 33.54 ? 3015 GLY A C     1 
ATOM   12197 O O     . GLY A 1 3015 ? 224.244 212.412 171.649 1.00 34.60 ? 3015 GLY A O     1 
ATOM   12198 N N     . GLU A 1 3016 ? 223.333 213.984 172.976 1.00 34.71 ? 3016 GLU A N     1 
ATOM   12199 C CA    . GLU A 1 3016 ? 224.565 214.273 173.693 1.00 37.01 ? 3016 GLU A CA    1 
ATOM   12200 C C     . GLU A 1 3016 ? 224.283 214.219 175.185 1.00 37.20 ? 3016 GLU A C     1 
ATOM   12201 O O     . GLU A 1 3016 ? 223.182 214.566 175.626 1.00 33.82 ? 3016 GLU A O     1 
ATOM   12202 C CB    . GLU A 1 3016 ? 225.139 215.640 173.291 1.00 36.30 ? 3016 GLU A CB    1 
ATOM   12203 C CG    . GLU A 1 3016 ? 224.672 216.810 174.142 1.00 37.43 ? 3016 GLU A CG    1 
ATOM   12204 C CD    . GLU A 1 3016 ? 223.482 217.526 173.538 1.00 35.89 ? 3016 GLU A CD    1 
ATOM   12205 O OE1   . GLU A 1 3016 ? 223.113 218.606 174.045 1.00 34.75 ? 3016 GLU A OE1   1 
ATOM   12206 O OE2   . GLU A 1 3016 ? 222.921 217.011 172.548 1.00 36.26 ? 3016 GLU A OE2   1 
ATOM   12207 N N     . VAL A 1 3017 ? 225.263 213.754 175.952 1.00 37.12 ? 3017 VAL A N     1 
ATOM   12208 C CA    . VAL A 1 3017 ? 225.173 213.718 177.408 1.00 36.02 ? 3017 VAL A CA    1 
ATOM   12209 C C     . VAL A 1 3017 ? 226.145 214.764 177.949 1.00 35.72 ? 3017 VAL A C     1 
ATOM   12210 O O     . VAL A 1 3017 ? 227.367 214.549 177.883 1.00 37.98 ? 3017 VAL A O     1 
ATOM   12211 C CB    . VAL A 1 3017 ? 225.487 212.323 177.962 1.00 37.15 ? 3017 VAL A CB    1 
ATOM   12212 C CG1   . VAL A 1 3017 ? 225.482 212.346 179.481 1.00 37.54 ? 3017 VAL A CG1   1 
ATOM   12213 C CG2   . VAL A 1 3017 ? 224.491 211.304 177.432 1.00 35.61 ? 3017 VAL A CG2   1 
ATOM   12214 N N     . PRO A 1 3018 ? 225.666 215.893 178.470 1.00 34.00 ? 3018 PRO A N     1 
ATOM   12215 C CA    . PRO A 1 3018 ? 226.584 216.962 178.890 1.00 35.20 ? 3018 PRO A CA    1 
ATOM   12216 C C     . PRO A 1 3018 ? 227.460 216.574 180.071 1.00 37.09 ? 3018 PRO A C     1 
ATOM   12217 O O     . PRO A 1 3018 ? 228.682 216.748 180.025 1.00 37.65 ? 3018 PRO A O     1 
ATOM   12218 C CB    . PRO A 1 3018 ? 225.636 218.114 179.247 1.00 36.53 ? 3018 PRO A CB    1 
ATOM   12219 C CG    . PRO A 1 3018 ? 224.340 217.455 179.576 1.00 37.71 ? 3018 PRO A CG    1 
ATOM   12220 C CD    . PRO A 1 3018 ? 224.254 216.248 178.692 1.00 36.99 ? 3018 PRO A CD    1 
ATOM   12221 N N     . GLY A 1 3019 ? 226.853 216.044 181.129 1.00 32.67 ? 3019 GLY A N     1 
ATOM   12222 C CA    . GLY A 1 3019 ? 227.594 215.712 182.330 1.00 32.22 ? 3019 GLY A CA    1 
ATOM   12223 C C     . GLY A 1 3019 ? 228.244 214.345 182.296 1.00 31.38 ? 3019 GLY A C     1 
ATOM   12224 O O     . GLY A 1 3019 ? 228.153 213.588 183.267 1.00 29.61 ? 3019 GLY A O     1 
ATOM   12225 N N     . LEU A 1 3020 ? 228.902 214.013 181.187 1.00 31.05 ? 3020 LEU A N     1 
ATOM   12226 C CA    . LEU A 1 3020 ? 229.567 212.727 181.028 1.00 34.58 ? 3020 LEU A CA    1 
ATOM   12227 C C     . LEU A 1 3020 ? 231.071 212.851 180.840 1.00 36.48 ? 3020 LEU A C     1 
ATOM   12228 O O     . LEU A 1 3020 ? 231.838 212.204 181.559 1.00 40.45 ? 3020 LEU A O     1 
ATOM   12229 C CB    . LEU A 1 3020 ? 228.964 211.964 179.841 1.00 34.19 ? 3020 LEU A CB    1 
ATOM   12230 C CG    . LEU A 1 3020 ? 229.519 210.562 179.588 1.00 32.95 ? 3020 LEU A CG    1 
ATOM   12231 C CD1   . LEU A 1 3020 ? 229.237 209.650 180.768 1.00 34.68 ? 3020 LEU A CD1   1 
ATOM   12232 C CD2   . LEU A 1 3020 ? 228.936 209.981 178.315 1.00 33.53 ? 3020 LEU A CD2   1 
ATOM   12233 N N     . PHE A 1 3021 ? 231.515 213.664 179.887 1.00 35.71 ? 3021 PHE A N     1 
ATOM   12234 C CA    . PHE A 1 3021 ? 232.930 213.775 179.542 1.00 37.06 ? 3021 PHE A CA    1 
ATOM   12235 C C     . PHE A 1 3021 ? 233.483 215.036 180.199 1.00 39.35 ? 3021 PHE A C     1 
ATOM   12236 O O     . PHE A 1 3021 ? 233.239 216.151 179.728 1.00 37.59 ? 3021 PHE A O     1 
ATOM   12237 C CB    . PHE A 1 3021 ? 233.119 213.807 178.029 1.00 36.30 ? 3021 PHE A CB    1 
ATOM   12238 C CG    . PHE A 1 3021 ? 233.327 212.452 177.417 1.00 36.05 ? 3021 PHE A CG    1 
ATOM   12239 C CD1   . PHE A 1 3021 ? 232.243 211.669 177.060 1.00 37.51 ? 3021 PHE A CD1   1 
ATOM   12240 C CD2   . PHE A 1 3021 ? 234.603 211.952 177.221 1.00 37.43 ? 3021 PHE A CD2   1 
ATOM   12241 C CE1   . PHE A 1 3021 ? 232.427 210.421 176.498 1.00 39.19 ? 3021 PHE A CE1   1 
ATOM   12242 C CE2   . PHE A 1 3021 ? 234.795 210.701 176.663 1.00 38.52 ? 3021 PHE A CE2   1 
ATOM   12243 C CZ    . PHE A 1 3021 ? 233.705 209.935 176.302 1.00 40.21 ? 3021 PHE A CZ    1 
ATOM   12244 N N     . GLU A 1 3022 ? 234.235 214.855 181.284 1.00 40.39 ? 3022 GLU A N     1 
ATOM   12245 C CA    . GLU A 1 3022 ? 234.812 215.960 182.033 1.00 43.63 ? 3022 GLU A CA    1 
ATOM   12246 C C     . GLU A 1 3022 ? 236.289 215.698 182.293 1.00 42.56 ? 3022 GLU A C     1 
ATOM   12247 O O     . GLU A 1 3022 ? 236.716 214.551 182.447 1.00 38.68 ? 3022 GLU A O     1 
ATOM   12248 C CB    . GLU A 1 3022 ? 234.090 216.179 183.372 1.00 39.92 ? 3022 GLU A CB    1 
ATOM   12249 C CG    . GLU A 1 3022 ? 232.574 216.198 183.280 1.00 38.08 ? 3022 GLU A CG    1 
ATOM   12250 C CD    . GLU A 1 3022 ? 232.060 217.242 182.309 1.00 41.35 ? 3022 GLU A CD    1 
ATOM   12251 O OE1   . GLU A 1 3022 ? 232.556 218.388 182.346 1.00 39.60 ? 3022 GLU A OE1   1 
ATOM   12252 O OE2   . GLU A 1 3022 ? 231.159 216.916 181.509 1.00 42.66 ? 3022 GLU A OE2   1 
ATOM   12253 N N     . GLY A 1 3023 ? 237.061 216.780 182.345 1.00 40.00 ? 3023 GLY A N     1 
ATOM   12254 C CA    . GLY A 1 3023 ? 238.465 216.672 182.708 1.00 38.38 ? 3023 GLY A CA    1 
ATOM   12255 C C     . GLY A 1 3023 ? 239.280 215.945 181.657 1.00 40.63 ? 3023 GLY A C     1 
ATOM   12256 O O     . GLY A 1 3023 ? 239.206 216.243 180.460 1.00 37.90 ? 3023 GLY A O     1 
ATOM   12257 N N     . ASP A 1 3024 ? 240.077 214.975 182.115 1.00 39.77 ? 3024 ASP A N     1 
ATOM   12258 C CA    . ASP A 1 3024 ? 240.979 214.258 181.217 1.00 41.66 ? 3024 ASP A CA    1 
ATOM   12259 C C     . ASP A 1 3024 ? 240.208 213.487 180.154 1.00 40.03 ? 3024 ASP A C     1 
ATOM   12260 O O     . ASP A 1 3024 ? 240.657 213.381 179.005 1.00 35.20 ? 3024 ASP A O     1 
ATOM   12261 C CB    . ASP A 1 3024 ? 241.874 213.316 182.022 1.00 40.77 ? 3024 ASP A CB    1 
ATOM   12262 C CG    . ASP A 1 3024 ? 242.892 212.597 181.157 1.00 41.13 ? 3024 ASP A CG    1 
ATOM   12263 O OD1   . ASP A 1 3024 ? 243.328 213.177 180.141 1.00 39.47 ? 3024 ASP A OD1   1 
ATOM   12264 O OD2   . ASP A 1 3024 ? 243.257 211.452 181.496 1.00 40.07 ? 3024 ASP A OD2   1 
ATOM   12265 N N     . GLU A 1 3025 ? 239.051 212.934 180.521 1.00 40.39 ? 3025 GLU A N     1 
ATOM   12266 C CA    . GLU A 1 3025 ? 238.231 212.222 179.547 1.00 38.07 ? 3025 GLU A CA    1 
ATOM   12267 C C     . GLU A 1 3025 ? 237.806 213.143 178.413 1.00 37.69 ? 3025 GLU A C     1 
ATOM   12268 O O     . GLU A 1 3025 ? 237.798 212.739 177.245 1.00 37.94 ? 3025 GLU A O     1 
ATOM   12269 C CB    . GLU A 1 3025 ? 237.007 211.615 180.232 1.00 38.60 ? 3025 GLU A CB    1 
ATOM   12270 C CG    . GLU A 1 3025 ? 237.332 210.743 181.432 1.00 39.27 ? 3025 GLU A CG    1 
ATOM   12271 C CD    . GLU A 1 3025 ? 236.175 210.642 182.406 1.00 39.27 ? 3025 GLU A CD    1 
ATOM   12272 O OE1   . GLU A 1 3025 ? 235.278 211.510 182.356 1.00 39.73 ? 3025 GLU A OE1   1 
ATOM   12273 O OE2   . GLU A 1 3025 ? 236.163 209.697 183.222 1.00 36.89 ? 3025 GLU A OE2   1 
ATOM   12274 N N     . TYR A 1 3026 ? 237.456 214.388 178.739 1.00 39.32 ? 3026 TYR A N     1 
ATOM   12275 C CA    . TYR A 1 3026 ? 237.033 215.344 177.719 1.00 40.95 ? 3026 TYR A CA    1 
ATOM   12276 C C     . TYR A 1 3026 ? 238.165 215.633 176.737 1.00 42.38 ? 3026 TYR A C     1 
ATOM   12277 O O     . TYR A 1 3026 ? 237.961 215.640 175.515 1.00 40.62 ? 3026 TYR A O     1 
ATOM   12278 C CB    . TYR A 1 3026 ? 236.555 216.626 178.402 1.00 36.78 ? 3026 TYR A CB    1 
ATOM   12279 C CG    . TYR A 1 3026 ? 235.747 217.561 177.534 1.00 38.93 ? 3026 TYR A CG    1 
ATOM   12280 C CD1   . TYR A 1 3026 ? 234.596 217.125 176.895 1.00 42.04 ? 3026 TYR A CD1   1 
ATOM   12281 C CD2   . TYR A 1 3026 ? 236.117 218.890 177.381 1.00 39.30 ? 3026 TYR A CD2   1 
ATOM   12282 C CE1   . TYR A 1 3026 ? 233.846 217.980 176.112 1.00 42.66 ? 3026 TYR A CE1   1 
ATOM   12283 C CE2   . TYR A 1 3026 ? 235.373 219.753 176.600 1.00 40.13 ? 3026 TYR A CE2   1 
ATOM   12284 C CZ    . TYR A 1 3026 ? 234.238 219.293 175.970 1.00 40.91 ? 3026 TYR A CZ    1 
ATOM   12285 O OH    . TYR A 1 3026 ? 233.495 220.147 175.189 1.00 39.52 ? 3026 TYR A OH    1 
ATOM   12286 N N     . ALA A 1 3027 ? 239.375 215.857 177.256 1.00 42.25 ? 3027 ALA A N     1 
ATOM   12287 C CA    . ALA A 1 3027 ? 240.518 216.137 176.391 1.00 42.92 ? 3027 ALA A CA    1 
ATOM   12288 C C     . ALA A 1 3027 ? 240.874 214.932 175.529 1.00 41.45 ? 3027 ALA A C     1 
ATOM   12289 O O     . ALA A 1 3027 ? 241.175 215.077 174.337 1.00 37.50 ? 3027 ALA A O     1 
ATOM   12290 C CB    . ALA A 1 3027 ? 241.718 216.570 177.232 1.00 39.51 ? 3027 ALA A CB    1 
ATOM   12291 N N     . THR A 1 3028 ? 240.856 213.732 176.115 1.00 40.70 ? 3028 THR A N     1 
ATOM   12292 C CA    . THR A 1 3028 ? 241.142 212.535 175.331 1.00 41.55 ? 3028 THR A CA    1 
ATOM   12293 C C     . THR A 1 3028 ? 240.100 212.337 174.239 1.00 43.02 ? 3028 THR A C     1 
ATOM   12294 O O     . THR A 1 3028 ? 240.438 211.972 173.106 1.00 43.13 ? 3028 THR A O     1 
ATOM   12295 C CB    . THR A 1 3028 ? 241.208 211.308 176.239 1.00 41.13 ? 3028 THR A CB    1 
ATOM   12296 O OG1   . THR A 1 3028 ? 240.069 211.292 177.107 1.00 44.83 ? 3028 THR A OG1   1 
ATOM   12297 C CG2   . THR A 1 3028 ? 242.475 211.333 177.079 1.00 41.22 ? 3028 THR A CG2   1 
ATOM   12298 N N     . LEU A 1 3029 ? 238.825 212.574 174.563 1.00 44.64 ? 3029 LEU A N     1 
ATOM   12299 C CA    . LEU A 1 3029 ? 237.770 212.467 173.565 1.00 43.52 ? 3029 LEU A CA    1 
ATOM   12300 C C     . LEU A 1 3029 ? 237.984 213.461 172.436 1.00 43.39 ? 3029 LEU A C     1 
ATOM   12301 O O     . LEU A 1 3029 ? 237.793 213.126 171.262 1.00 42.16 ? 3029 LEU A O     1 
ATOM   12302 C CB    . LEU A 1 3029 ? 236.405 212.687 174.215 1.00 41.43 ? 3029 LEU A CB    1 
ATOM   12303 C CG    . LEU A 1 3029 ? 235.217 212.650 173.256 1.00 43.33 ? 3029 LEU A CG    1 
ATOM   12304 C CD1   . LEU A 1 3029 ? 235.037 211.246 172.702 1.00 41.07 ? 3029 LEU A CD1   1 
ATOM   12305 C CD2   . LEU A 1 3029 ? 233.947 213.136 173.936 1.00 41.45 ? 3029 LEU A CD2   1 
ATOM   12306 N N     . MET A 1 3030 ? 238.380 214.692 172.771 1.00 40.91 ? 3030 MET A N     1 
ATOM   12307 C CA    . MET A 1 3030 ? 238.706 215.661 171.728 1.00 43.30 ? 3030 MET A CA    1 
ATOM   12308 C C     . MET A 1 3030 ? 239.853 215.170 170.856 1.00 44.84 ? 3030 MET A C     1 
ATOM   12309 O O     . MET A 1 3030 ? 239.807 215.304 169.628 1.00 43.85 ? 3030 MET A O     1 
ATOM   12310 C CB    . MET A 1 3030 ? 239.034 217.021 172.342 1.00 41.81 ? 3030 MET A CB    1 
ATOM   12311 C CG    . MET A 1 3030 ? 237.853 217.667 173.032 1.00 42.56 ? 3030 MET A CG    1 
ATOM   12312 S SD    . MET A 1 3030 ? 236.569 218.015 171.814 1.00 57.52 ? 3030 MET A SD    1 
ATOM   12313 C CE    . MET A 1 3030 ? 235.219 218.537 172.860 1.00 42.76 ? 3030 MET A CE    1 
ATOM   12314 N N     . THR A 1 3031 ? 240.879 214.578 171.468 1.00 44.28 ? 3031 THR A N     1 
ATOM   12315 C CA    . THR A 1 3031 ? 242.001 214.058 170.691 1.00 43.30 ? 3031 THR A CA    1 
ATOM   12316 C C     . THR A 1 3031 ? 241.543 212.985 169.707 1.00 43.85 ? 3031 THR A C     1 
ATOM   12317 O O     . THR A 1 3031 ? 241.820 213.069 168.502 1.00 41.17 ? 3031 THR A O     1 
ATOM   12318 C CB    . THR A 1 3031 ? 243.075 213.503 171.627 1.00 43.62 ? 3031 THR A CB    1 
ATOM   12319 O OG1   . THR A 1 3031 ? 243.474 214.519 172.555 1.00 43.51 ? 3031 THR A OG1   1 
ATOM   12320 C CG2   . THR A 1 3031 ? 244.288 213.046 170.830 1.00 43.93 ? 3031 THR A CG2   1 
ATOM   12321 N N     . GLN A 1 3032 ? 240.823 211.971 170.201 1.00 42.82 ? 3032 GLN A N     1 
ATOM   12322 C CA    . GLN A 1 3032 ? 240.422 210.877 169.318 1.00 42.14 ? 3032 GLN A CA    1 
ATOM   12323 C C     . GLN A 1 3032 ? 239.426 211.342 168.261 1.00 42.87 ? 3032 GLN A C     1 
ATOM   12324 O O     . GLN A 1 3032 ? 239.481 210.890 167.113 1.00 40.69 ? 3032 GLN A O     1 
ATOM   12325 C CB    . GLN A 1 3032 ? 239.849 209.689 170.099 1.00 40.32 ? 3032 GLN A CB    1 
ATOM   12326 C CG    . GLN A 1 3032 ? 240.876 208.876 170.884 1.00 40.82 ? 3032 GLN A CG    1 
ATOM   12327 C CD    . GLN A 1 3032 ? 240.832 209.126 172.374 1.00 45.68 ? 3032 GLN A CD    1 
ATOM   12328 O OE1   . GLN A 1 3032 ? 239.787 209.470 172.924 1.00 45.34 ? 3032 GLN A OE1   1 
ATOM   12329 N NE2   . GLN A 1 3032 ? 241.969 208.957 173.037 1.00 45.29 ? 3032 GLN A NE2   1 
ATOM   12330 N N     . CYS A 1 3033 ? 238.512 212.249 168.616 1.00 42.03 ? 3033 CYS A N     1 
ATOM   12331 C CA    . CYS A 1 3033 ? 237.531 212.686 167.630 1.00 41.66 ? 3033 CYS A CA    1 
ATOM   12332 C C     . CYS A 1 3033 ? 238.159 213.585 166.572 1.00 41.30 ? 3033 CYS A C     1 
ATOM   12333 O O     . CYS A 1 3033 ? 237.781 213.506 165.399 1.00 41.94 ? 3033 CYS A O     1 
ATOM   12334 C CB    . CYS A 1 3033 ? 236.357 213.389 168.313 1.00 39.42 ? 3033 CYS A CB    1 
ATOM   12335 S SG    . CYS A 1 3033 ? 236.711 215.017 168.980 1.00 42.51 ? 3033 CYS A SG    1 
ATOM   12336 N N     . LYS A 1 3034 ? 239.127 214.428 166.945 1.00 40.74 ? 3034 LYS A N     1 
ATOM   12337 C CA    . LYS A 1 3034 ? 239.826 215.201 165.925 1.00 43.64 ? 3034 LYS A CA    1 
ATOM   12338 C C     . LYS A 1 3034 ? 240.665 214.299 165.029 1.00 43.45 ? 3034 LYS A C     1 
ATOM   12339 O O     . LYS A 1 3034 ? 240.736 214.530 163.815 1.00 40.88 ? 3034 LYS A O     1 
ATOM   12340 C CB    . LYS A 1 3034 ? 240.679 216.299 166.573 1.00 44.74 ? 3034 LYS A CB    1 
ATOM   12341 C CG    . LYS A 1 3034 ? 242.050 215.869 167.070 1.00 43.81 ? 3034 LYS A CG    1 
ATOM   12342 C CD    . LYS A 1 3034 ? 242.868 217.061 167.539 1.00 43.30 ? 3034 LYS A CD    1 
ATOM   12343 C CE    . LYS A 1 3034 ? 243.998 216.626 168.457 1.00 43.83 ? 3034 LYS A CE    1 
ATOM   12344 N NZ    . LYS A 1 3034 ? 244.766 215.483 167.891 1.00 42.26 ? 3034 LYS A NZ    1 
ATOM   12345 N N     . GLU A 1 3035 ? 241.280 213.251 165.590 1.00 42.59 ? 3035 GLU A N     1 
ATOM   12346 C CA    . GLU A 1 3035 ? 241.991 212.296 164.745 1.00 42.51 ? 3035 GLU A CA    1 
ATOM   12347 C C     . GLU A 1 3035 ? 241.037 211.591 163.789 1.00 41.44 ? 3035 GLU A C     1 
ATOM   12348 O O     . GLU A 1 3035 ? 241.371 211.369 162.618 1.00 40.19 ? 3035 GLU A O     1 
ATOM   12349 C CB    . GLU A 1 3035 ? 242.743 211.284 165.608 1.00 39.98 ? 3035 GLU A CB    1 
ATOM   12350 C CG    . GLU A 1 3035 ? 243.926 211.877 166.351 1.00 43.32 ? 3035 GLU A CG    1 
ATOM   12351 C CD    . GLU A 1 3035 ? 244.687 212.887 165.513 1.00 45.79 ? 3035 GLU A CD    1 
ATOM   12352 O OE1   . GLU A 1 3035 ? 245.283 212.486 164.491 1.00 41.85 ? 3035 GLU A OE1   1 
ATOM   12353 O OE2   . GLU A 1 3035 ? 244.688 214.083 165.875 1.00 44.27 ? 3035 GLU A OE2   1 
ATOM   12354 N N     . GLY A 1 3036 ? 239.847 211.227 164.270 1.00 41.36 ? 3036 GLY A N     1 
ATOM   12355 C CA    . GLY A 1 3036 ? 238.853 210.638 163.388 1.00 41.98 ? 3036 GLY A CA    1 
ATOM   12356 C C     . GLY A 1 3036 ? 238.424 211.588 162.288 1.00 39.64 ? 3036 GLY A C     1 
ATOM   12357 O O     . GLY A 1 3036 ? 238.237 211.181 161.140 1.00 37.66 ? 3036 GLY A O     1 
ATOM   12358 N N     . ALA A 1 3037 ? 238.270 212.870 162.624 1.00 37.98 ? 3037 ALA A N     1 
ATOM   12359 C CA    . ALA A 1 3037 ? 237.943 213.867 161.612 1.00 39.83 ? 3037 ALA A CA    1 
ATOM   12360 C C     . ALA A 1 3037 ? 239.037 213.953 160.556 1.00 41.31 ? 3037 ALA A C     1 
ATOM   12361 O O     . ALA A 1 3037 ? 238.748 214.074 159.360 1.00 39.22 ? 3037 ALA A O     1 
ATOM   12362 C CB    . ALA A 1 3037 ? 237.716 215.228 162.269 1.00 37.14 ? 3037 ALA A CB    1 
ATOM   12363 N N     . GLN A 1 3038 ? 240.303 213.898 160.979 1.00 44.94 ? 3038 GLN A N     1 
ATOM   12364 C CA    . GLN A 1 3038 ? 241.399 213.910 160.012 1.00 44.01 ? 3038 GLN A CA    1 
ATOM   12365 C C     . GLN A 1 3038 ? 241.386 212.666 159.129 1.00 44.34 ? 3038 GLN A C     1 
ATOM   12366 O O     . GLN A 1 3038 ? 241.581 212.762 157.912 1.00 44.09 ? 3038 GLN A O     1 
ATOM   12367 C CB    . GLN A 1 3038 ? 242.748 214.055 160.720 1.00 42.22 ? 3038 GLN A CB    1 
ATOM   12368 C CG    . GLN A 1 3038 ? 242.816 215.188 161.723 1.00 43.92 ? 3038 GLN A CG    1 
ATOM   12369 C CD    . GLN A 1 3038 ? 242.268 216.488 161.165 1.00 45.06 ? 3038 GLN A CD    1 
ATOM   12370 O OE1   . GLN A 1 3038 ? 241.339 217.073 161.720 1.00 44.44 ? 3038 GLN A OE1   1 
ATOM   12371 N NE2   . GLN A 1 3038 ? 242.847 216.949 160.062 1.00 43.06 ? 3038 GLN A NE2   1 
ATOM   12372 N N     . LYS A 1 3039 ? 241.160 211.484 159.713 1.00 42.12 ? 3039 LYS A N     1 
ATOM   12373 C CA    . LYS A 1 3039 ? 241.195 210.289 158.873 1.00 44.72 ? 3039 LYS A CA    1 
ATOM   12374 C C     . LYS A 1 3039 ? 239.891 210.045 158.123 1.00 43.63 ? 3039 LYS A C     1 
ATOM   12375 O O     . LYS A 1 3039 ? 239.842 209.131 157.294 1.00 42.14 ? 3039 LYS A O     1 
ATOM   12376 C CB    . LYS A 1 3039 ? 241.554 209.032 159.676 1.00 42.75 ? 3039 LYS A CB    1 
ATOM   12377 C CG    . LYS A 1 3039 ? 240.706 208.724 160.898 1.00 39.28 ? 3039 LYS A CG    1 
ATOM   12378 C CD    . LYS A 1 3039 ? 241.470 207.771 161.816 1.00 41.14 ? 3039 LYS A CD    1 
ATOM   12379 C CE    . LYS A 1 3039 ? 240.788 207.556 163.157 1.00 44.59 ? 3039 LYS A CE    1 
ATOM   12380 N NZ    . LYS A 1 3039 ? 241.200 208.554 164.177 1.00 45.68 ? 3039 LYS A NZ    1 
ATOM   12381 N N     . GLU A 1 3040 ? 238.843 210.823 158.388 1.00 40.20 ? 3040 GLU A N     1 
ATOM   12382 C CA    . GLU A 1 3040 ? 237.604 210.739 157.628 1.00 41.20 ? 3040 GLU A CA    1 
ATOM   12383 C C     . GLU A 1 3040 ? 237.421 211.914 156.676 1.00 41.63 ? 3040 GLU A C     1 
ATOM   12384 O O     . GLU A 1 3040 ? 236.310 212.131 156.183 1.00 41.20 ? 3040 GLU A O     1 
ATOM   12385 C CB    . GLU A 1 3040 ? 236.404 210.635 158.572 1.00 42.66 ? 3040 GLU A CB    1 
ATOM   12386 C CG    . GLU A 1 3040 ? 236.377 209.363 159.404 1.00 41.26 ? 3040 GLU A CG    1 
ATOM   12387 C CD    . GLU A 1 3040 ? 235.539 209.506 160.658 1.00 42.71 ? 3040 GLU A CD    1 
ATOM   12388 O OE1   . GLU A 1 3040 ? 234.707 210.435 160.715 1.00 43.99 ? 3040 GLU A OE1   1 
ATOM   12389 O OE2   . GLU A 1 3040 ? 235.714 208.691 161.588 1.00 42.35 ? 3040 GLU A OE2   1 
ATOM   12390 N N     . GLY A 1 3041 ? 238.480 212.669 156.406 1.00 41.61 ? 3041 GLY A N     1 
ATOM   12391 C CA    . GLY A 1 3041 ? 238.389 213.805 155.504 1.00 40.05 ? 3041 GLY A CA    1 
ATOM   12392 C C     . GLY A 1 3041 ? 237.526 214.938 156.015 1.00 39.64 ? 3041 GLY A C     1 
ATOM   12393 O O     . GLY A 1 3041 ? 236.755 215.522 155.243 1.00 40.62 ? 3041 GLY A O     1 
ATOM   12394 N N     . LEU A 1 3042 ? 237.636 215.265 157.300 1.00 39.69 ? 3042 LEU A N     1 
ATOM   12395 C CA    . LEU A 1 3042 ? 236.845 216.317 157.922 1.00 42.22 ? 3042 LEU A CA    1 
ATOM   12396 C C     . LEU A 1 3042 ? 237.781 217.351 158.530 1.00 44.58 ? 3042 LEU A C     1 
ATOM   12397 O O     . LEU A 1 3042 ? 238.717 216.997 159.255 1.00 41.27 ? 3042 LEU A O     1 
ATOM   12398 C CB    . LEU A 1 3042 ? 235.913 215.735 158.987 1.00 38.65 ? 3042 LEU A CB    1 
ATOM   12399 C CG    . LEU A 1 3042 ? 235.087 214.538 158.508 1.00 41.06 ? 3042 LEU A CG    1 
ATOM   12400 C CD1   . LEU A 1 3042 ? 234.585 213.712 159.680 1.00 40.01 ? 3042 LEU A CD1   1 
ATOM   12401 C CD2   . LEU A 1 3042 ? 233.926 215.003 157.639 1.00 40.73 ? 3042 LEU A CD2   1 
ATOM   12402 N N     . MET A 1 3043 ? 237.528 218.623 158.231 1.00 46.96 ? 3043 MET A N     1 
ATOM   12403 C CA    . MET A 1 3043 ? 238.400 219.693 158.695 1.00 44.20 ? 3043 MET A CA    1 
ATOM   12404 C C     . MET A 1 3043 ? 238.250 219.906 160.197 1.00 42.63 ? 3043 MET A C     1 
ATOM   12405 O O     . MET A 1 3043 ? 237.136 219.963 160.726 1.00 40.88 ? 3043 MET A O     1 
ATOM   12406 C CB    . MET A 1 3043 ? 238.090 220.988 157.944 1.00 43.92 ? 3043 MET A CB    1 
ATOM   12407 C CG    . MET A 1 3043 ? 238.377 222.257 158.731 1.00 45.97 ? 3043 MET A CG    1 
ATOM   12408 S SD    . MET A 1 3043 ? 240.095 222.790 158.600 1.00 52.14 ? 3043 MET A SD    1 
ATOM   12409 C CE    . MET A 1 3043 ? 240.096 223.540 156.974 1.00 42.89 ? 3043 MET A CE    1 
ATOM   12410 N N     . LEU A 1 3044 ? 239.385 220.027 160.882 1.00 42.06 ? 3044 LEU A N     1 
ATOM   12411 C CA    . LEU A 1 3044 ? 239.388 220.281 162.315 1.00 44.27 ? 3044 LEU A CA    1 
ATOM   12412 C C     . LEU A 1 3044 ? 238.947 221.714 162.589 1.00 44.64 ? 3044 LEU A C     1 
ATOM   12413 O O     . LEU A 1 3044 ? 239.386 222.649 161.912 1.00 45.09 ? 3044 LEU A O     1 
ATOM   12414 C CB    . LEU A 1 3044 ? 240.780 220.032 162.896 1.00 44.15 ? 3044 LEU A CB    1 
ATOM   12415 C CG    . LEU A 1 3044 ? 241.038 220.456 164.345 1.00 44.94 ? 3044 LEU A CG    1 
ATOM   12416 C CD1   . LEU A 1 3044 ? 240.028 219.821 165.289 1.00 43.59 ? 3044 LEU A CD1   1 
ATOM   12417 C CD2   . LEU A 1 3044 ? 242.459 220.103 164.761 1.00 45.83 ? 3044 LEU A CD2   1 
ATOM   12418 N N     . ASP A 1 3045 ? 238.080 221.883 163.585 1.00 44.61 ? 3045 ASP A N     1 
ATOM   12419 C CA    . ASP A 1 3045 ? 237.570 223.199 163.946 1.00 43.92 ? 3045 ASP A CA    1 
ATOM   12420 C C     . ASP A 1 3045 ? 237.806 223.476 165.426 1.00 41.35 ? 3045 ASP A C     1 
ATOM   12421 O O     . ASP A 1 3045 ? 238.549 222.744 166.088 1.00 41.44 ? 3045 ASP A O     1 
ATOM   12422 C CB    . ASP A 1 3045 ? 236.081 223.309 163.612 1.00 45.44 ? 3045 ASP A CB    1 
ATOM   12423 C CG    . ASP A 1 3045 ? 235.812 223.240 162.121 1.00 46.46 ? 3045 ASP A CG    1 
ATOM   12424 O OD1   . ASP A 1 3045 ? 236.739 223.524 161.334 1.00 42.13 ? 3045 ASP A OD1   1 
ATOM   12425 O OD2   . ASP A 1 3045 ? 234.673 222.902 161.735 1.00 46.05 ? 3045 ASP A OD2   1 
ATOM   12426 N N     . SER A 1 3046 ? 237.190 224.535 165.946 1.00 40.55 ? 3046 SER A N     1 
ATOM   12427 C CA    . SER A 1 3046 ? 237.326 224.872 167.353 1.00 43.91 ? 3046 SER A CA    1 
ATOM   12428 C C     . SER A 1 3046 ? 236.748 223.759 168.230 1.00 43.69 ? 3046 SER A C     1 
ATOM   12429 O O     . SER A 1 3046 ? 236.081 222.836 167.757 1.00 41.97 ? 3046 SER A O     1 
ATOM   12430 C CB    . SER A 1 3046 ? 236.631 226.199 167.654 1.00 44.12 ? 3046 SER A CB    1 
ATOM   12431 O OG    . SER A 1 3046 ? 235.224 226.073 167.544 1.00 45.26 ? 3046 SER A OG    1 
ATOM   12432 N N     . HIS A 1 3047 ? 237.016 223.864 169.534 1.00 45.95 ? 3047 HIS A N     1 
ATOM   12433 C CA    . HIS A 1 3047 ? 236.591 222.826 170.468 1.00 48.00 ? 3047 HIS A CA    1 
ATOM   12434 C C     . HIS A 1 3047 ? 235.075 222.682 170.484 1.00 46.29 ? 3047 HIS A C     1 
ATOM   12435 O O     . HIS A 1 3047 ? 234.547 221.565 170.496 1.00 47.66 ? 3047 HIS A O     1 
ATOM   12436 C CB    . HIS A 1 3047 ? 237.117 223.134 171.870 1.00 47.52 ? 3047 HIS A CB    1 
ATOM   12437 C CG    . HIS A 1 3047 ? 238.609 223.096 171.977 1.00 49.10 ? 3047 HIS A CG    1 
ATOM   12438 N ND1   . HIS A 1 3047 ? 239.324 221.918 172.001 1.00 49.64 ? 3047 HIS A ND1   1 
ATOM   12439 C CD2   . HIS A 1 3047 ? 239.522 224.092 172.065 1.00 47.46 ? 3047 HIS A CD2   1 
ATOM   12440 C CE1   . HIS A 1 3047 ? 240.613 222.189 172.100 1.00 49.32 ? 3047 HIS A CE1   1 
ATOM   12441 N NE2   . HIS A 1 3047 ? 240.760 223.501 172.141 1.00 49.94 ? 3047 HIS A NE2   1 
ATOM   12442 N N     . GLU A 1 3048 ? 234.354 223.806 170.486 1.00 41.35 ? 3048 GLU A N     1 
ATOM   12443 C CA    . GLU A 1 3048 ? 232.896 223.741 170.483 1.00 43.45 ? 3048 GLU A CA    1 
ATOM   12444 C C     . GLU A 1 3048 ? 232.365 223.165 169.176 1.00 44.13 ? 3048 GLU A C     1 
ATOM   12445 O O     . GLU A 1 3048 ? 231.456 222.327 169.186 1.00 43.65 ? 3048 GLU A O     1 
ATOM   12446 C CB    . GLU A 1 3048 ? 232.311 225.129 170.741 1.00 44.45 ? 3048 GLU A CB    1 
ATOM   12447 C CG    . GLU A 1 3048 ? 232.923 225.837 171.938 1.00 45.42 ? 3048 GLU A CG    1 
ATOM   12448 C CD    . GLU A 1 3048 ? 232.813 225.023 173.213 1.00 46.29 ? 3048 GLU A CD    1 
ATOM   12449 O OE1   . GLU A 1 3048 ? 231.752 224.403 173.435 1.00 44.63 ? 3048 GLU A OE1   1 
ATOM   12450 O OE2   . GLU A 1 3048 ? 233.788 225.002 173.992 1.00 46.78 ? 3048 GLU A OE2   1 
ATOM   12451 N N     . GLU A 1 3049 ? 232.923 223.591 168.041 1.00 38.68 ? 3049 GLU A N     1 
ATOM   12452 C CA    . GLU A 1 3049 ? 232.472 223.055 166.761 1.00 39.90 ? 3049 GLU A CA    1 
ATOM   12453 C C     . GLU A 1 3049 ? 232.860 221.589 166.608 1.00 39.39 ? 3049 GLU A C     1 
ATOM   12454 O O     . GLU A 1 3049 ? 232.101 220.797 166.037 1.00 38.58 ? 3049 GLU A O     1 
ATOM   12455 C CB    . GLU A 1 3049 ? 233.035 223.889 165.611 1.00 40.99 ? 3049 GLU A CB    1 
ATOM   12456 C CG    . GLU A 1 3049 ? 232.053 224.911 165.061 1.00 43.11 ? 3049 GLU A CG    1 
ATOM   12457 C CD    . GLU A 1 3049 ? 230.731 224.288 164.649 1.00 41.83 ? 3049 GLU A CD    1 
ATOM   12458 O OE1   . GLU A 1 3049 ? 229.672 224.799 165.071 1.00 39.14 ? 3049 GLU A OE1   1 
ATOM   12459 O OE2   . GLU A 1 3049 ? 230.750 223.286 163.904 1.00 40.17 ? 3049 GLU A OE2   1 
ATOM   12460 N N     . LEU A 1 3050 ? 234.035 221.209 167.112 1.00 37.16 ? 3050 LEU A N     1 
ATOM   12461 C CA    . LEU A 1 3050 ? 234.428 219.803 167.086 1.00 38.19 ? 3050 LEU A CA    1 
ATOM   12462 C C     . LEU A 1 3050 ? 233.500 218.958 167.952 1.00 38.22 ? 3050 LEU A C     1 
ATOM   12463 O O     . LEU A 1 3050 ? 233.126 217.841 167.573 1.00 38.21 ? 3050 LEU A O     1 
ATOM   12464 C CB    . LEU A 1 3050 ? 235.879 219.661 167.543 1.00 39.47 ? 3050 LEU A CB    1 
ATOM   12465 C CG    . LEU A 1 3050 ? 236.488 218.262 167.519 1.00 39.99 ? 3050 LEU A CG    1 
ATOM   12466 C CD1   . LEU A 1 3050 ? 236.525 217.724 166.098 1.00 41.11 ? 3050 LEU A CD1   1 
ATOM   12467 C CD2   . LEU A 1 3050 ? 237.885 218.286 168.120 1.00 37.25 ? 3050 LEU A CD2   1 
ATOM   12468 N N     . TYR A 1 3051 ? 233.113 219.478 169.119 1.00 35.84 ? 3051 TYR A N     1 
ATOM   12469 C CA    . TYR A 1 3051 ? 232.149 218.780 169.962 1.00 34.19 ? 3051 TYR A CA    1 
ATOM   12470 C C     . TYR A 1 3051 ? 230.801 218.654 169.266 1.00 37.49 ? 3051 TYR A C     1 
ATOM   12471 O O     . TYR A 1 3051 ? 230.138 217.616 169.365 1.00 38.41 ? 3051 TYR A O     1 
ATOM   12472 C CB    . TYR A 1 3051 ? 231.995 219.507 171.296 1.00 34.93 ? 3051 TYR A CB    1 
ATOM   12473 C CG    . TYR A 1 3051 ? 231.186 218.743 172.319 1.00 36.56 ? 3051 TYR A CG    1 
ATOM   12474 C CD1   . TYR A 1 3051 ? 231.481 217.420 172.618 1.00 37.80 ? 3051 TYR A CD1   1 
ATOM   12475 C CD2   . TYR A 1 3051 ? 230.126 219.344 172.983 1.00 36.71 ? 3051 TYR A CD2   1 
ATOM   12476 C CE1   . TYR A 1 3051 ? 230.744 216.717 173.553 1.00 38.22 ? 3051 TYR A CE1   1 
ATOM   12477 C CE2   . TYR A 1 3051 ? 229.382 218.650 173.918 1.00 37.91 ? 3051 TYR A CE2   1 
ATOM   12478 C CZ    . TYR A 1 3051 ? 229.696 217.337 174.199 1.00 40.33 ? 3051 TYR A CZ    1 
ATOM   12479 O OH    . TYR A 1 3051 ? 228.958 216.643 175.130 1.00 39.15 ? 3051 TYR A OH    1 
ATOM   12480 N N     . LYS A 1 3052 ? 230.370 219.709 168.570 1.00 37.84 ? 3052 LYS A N     1 
ATOM   12481 C CA    . LYS A 1 3052 ? 229.113 219.643 167.831 1.00 36.01 ? 3052 LYS A CA    1 
ATOM   12482 C C     . LYS A 1 3052 ? 229.189 218.584 166.737 1.00 32.87 ? 3052 LYS A C     1 
ATOM   12483 O O     . LYS A 1 3052 ? 228.234 217.824 166.526 1.00 33.07 ? 3052 LYS A O     1 
ATOM   12484 C CB    . LYS A 1 3052 ? 228.782 221.027 167.257 1.00 35.59 ? 3052 LYS A CB    1 
ATOM   12485 C CG    . LYS A 1 3052 ? 227.336 221.263 166.777 1.00 35.37 ? 3052 LYS A CG    1 
ATOM   12486 C CD    . LYS A 1 3052 ? 226.951 220.489 165.522 1.00 33.66 ? 3052 LYS A CD    1 
ATOM   12487 C CE    . LYS A 1 3052 ? 225.760 221.121 164.821 1.00 33.90 ? 3052 LYS A CE    1 
ATOM   12488 N NZ    . LYS A 1 3052 ? 225.335 220.330 163.634 1.00 33.58 ? 3052 LYS A NZ    1 
ATOM   12489 N N     . TRP A 1 3053 ? 230.322 218.514 166.034 1.00 31.88 ? 3053 TRP A N     1 
ATOM   12490 C CA    . TRP A 1 3053 ? 230.485 217.493 165.005 1.00 32.26 ? 3053 TRP A CA    1 
ATOM   12491 C C     . TRP A 1 3053 ? 230.453 216.097 165.613 1.00 33.96 ? 3053 TRP A C     1 
ATOM   12492 O O     . TRP A 1 3053 ? 229.867 215.176 165.036 1.00 33.57 ? 3053 TRP A O     1 
ATOM   12493 C CB    . TRP A 1 3053 ? 231.791 217.703 164.241 1.00 31.57 ? 3053 TRP A CB    1 
ATOM   12494 C CG    . TRP A 1 3053 ? 232.253 216.462 163.538 1.00 31.94 ? 3053 TRP A CG    1 
ATOM   12495 C CD1   . TRP A 1 3053 ? 231.857 216.026 162.308 1.00 34.72 ? 3053 TRP A CD1   1 
ATOM   12496 C CD2   . TRP A 1 3053 ? 233.176 215.483 164.031 1.00 31.91 ? 3053 TRP A CD2   1 
ATOM   12497 N NE1   . TRP A 1 3053 ? 232.484 214.844 161.999 1.00 33.20 ? 3053 TRP A NE1   1 
ATOM   12498 C CE2   . TRP A 1 3053 ? 233.299 214.489 163.041 1.00 35.26 ? 3053 TRP A CE2   1 
ATOM   12499 C CE3   . TRP A 1 3053 ? 233.912 215.352 165.212 1.00 30.26 ? 3053 TRP A CE3   1 
ATOM   12500 C CZ2   . TRP A 1 3053 ? 234.128 213.381 163.195 1.00 34.86 ? 3053 TRP A CZ2   1 
ATOM   12501 C CZ3   . TRP A 1 3053 ? 234.734 214.252 165.361 1.00 33.34 ? 3053 TRP A CZ3   1 
ATOM   12502 C CH2   . TRP A 1 3053 ? 234.836 213.281 164.359 1.00 35.99 ? 3053 TRP A CH2   1 
ATOM   12503 N N     . PHE A 1 3054 ? 231.091 215.920 166.772 1.00 34.64 ? 3054 PHE A N     1 
ATOM   12504 C CA    . PHE A 1 3054 ? 231.054 214.627 167.451 1.00 34.76 ? 3054 PHE A CA    1 
ATOM   12505 C C     . PHE A 1 3054 ? 229.634 214.256 167.860 1.00 30.32 ? 3054 PHE A C     1 
ATOM   12506 O O     . PHE A 1 3054 ? 229.223 213.097 167.727 1.00 28.80 ? 3054 PHE A O     1 
ATOM   12507 C CB    . PHE A 1 3054 ? 231.972 214.648 168.672 1.00 34.47 ? 3054 PHE A CB    1 
ATOM   12508 C CG    . PHE A 1 3054 ? 232.024 213.344 169.411 1.00 33.18 ? 3054 PHE A CG    1 
ATOM   12509 C CD1   . PHE A 1 3054 ? 232.746 212.275 168.909 1.00 34.73 ? 3054 PHE A CD1   1 
ATOM   12510 C CD2   . PHE A 1 3054 ? 231.350 213.187 170.611 1.00 31.36 ? 3054 PHE A CD2   1 
ATOM   12511 C CE1   . PHE A 1 3054 ? 232.796 211.074 169.591 1.00 33.54 ? 3054 PHE A CE1   1 
ATOM   12512 C CE2   . PHE A 1 3054 ? 231.396 211.988 171.296 1.00 33.31 ? 3054 PHE A CE2   1 
ATOM   12513 C CZ    . PHE A 1 3054 ? 232.119 210.931 170.784 1.00 34.65 ? 3054 PHE A CZ    1 
ATOM   12514 N N     . THR A 1 3055 ? 228.870 215.226 168.365 1.00 28.34 ? 3055 THR A N     1 
ATOM   12515 C CA    . THR A 1 3055 ? 227.483 214.955 168.728 1.00 30.93 ? 3055 THR A CA    1 
ATOM   12516 C C     . THR A 1 3055 ? 226.663 214.559 167.507 1.00 33.27 ? 3055 THR A C     1 
ATOM   12517 O O     . THR A 1 3055 ? 225.851 213.633 167.574 1.00 35.78 ? 3055 THR A O     1 
ATOM   12518 C CB    . THR A 1 3055 ? 226.859 216.168 169.418 1.00 31.83 ? 3055 THR A CB    1 
ATOM   12519 O OG1   . THR A 1 3055 ? 226.966 217.314 168.566 1.00 32.08 ? 3055 THR A OG1   1 
ATOM   12520 C CG2   . THR A 1 3055 ? 227.551 216.448 170.741 1.00 32.82 ? 3055 THR A CG2   1 
ATOM   12521 N N     . SER A 1 3056 ? 226.862 215.246 166.380 1.00 28.86 ? 3056 SER A N     1 
ATOM   12522 C CA    . SER A 1 3056 ? 226.140 214.882 165.163 1.00 28.25 ? 3056 SER A CA    1 
ATOM   12523 C C     . SER A 1 3056 ? 226.551 213.497 164.671 1.00 27.40 ? 3056 SER A C     1 
ATOM   12524 O O     . SER A 1 3056 ? 225.716 212.727 164.178 1.00 29.85 ? 3056 SER A O     1 
ATOM   12525 C CB    . SER A 1 3056 ? 226.374 215.931 164.078 1.00 30.05 ? 3056 SER A CB    1 
ATOM   12526 O OG    . SER A 1 3056 ? 225.619 215.638 162.915 1.00 25.77 ? 3056 SER A OG    1 
ATOM   12527 N N     . GLN A 1 3057 ? 227.839 213.169 164.794 1.00 25.22 ? 3057 GLN A N     1 
ATOM   12528 C CA    . GLN A 1 3057 ? 228.312 211.835 164.441 1.00 29.76 ? 3057 GLN A CA    1 
ATOM   12529 C C     . GLN A 1 3057 ? 227.639 210.781 165.308 1.00 30.41 ? 3057 GLN A C     1 
ATOM   12530 O O     . GLN A 1 3057 ? 227.297 209.694 164.830 1.00 26.58 ? 3057 GLN A O     1 
ATOM   12531 C CB    . GLN A 1 3057 ? 229.832 211.771 164.599 1.00 29.87 ? 3057 GLN A CB    1 
ATOM   12532 C CG    . GLN A 1 3057 ? 230.624 211.985 163.317 1.00 27.81 ? 3057 GLN A CG    1 
ATOM   12533 C CD    . GLN A 1 3057 ? 230.624 210.777 162.406 1.00 30.19 ? 3057 GLN A CD    1 
ATOM   12534 O OE1   . GLN A 1 3057 ? 229.867 210.718 161.439 1.00 27.71 ? 3057 GLN A OE1   1 
ATOM   12535 N NE2   . GLN A 1 3057 ? 231.465 209.800 162.717 1.00 31.58 ? 3057 GLN A NE2   1 
ATOM   12536 N N     . VAL A 1 3058 ? 227.446 211.090 166.592 1.00 31.60 ? 3058 VAL A N     1 
ATOM   12537 C CA    . VAL A 1 3058 ? 226.687 210.207 167.474 1.00 28.18 ? 3058 VAL A CA    1 
ATOM   12538 C C     . VAL A 1 3058 ? 225.242 210.101 167.000 1.00 27.06 ? 3058 VAL A C     1 
ATOM   12539 O O     . VAL A 1 3058 ? 224.644 209.018 167.017 1.00 28.22 ? 3058 VAL A O     1 
ATOM   12540 C CB    . VAL A 1 3058 ? 226.775 210.706 168.929 1.00 25.74 ? 3058 VAL A CB    1 
ATOM   12541 C CG1   . VAL A 1 3058 ? 225.625 210.161 169.759 1.00 23.69 ? 3058 VAL A CG1   1 
ATOM   12542 C CG2   . VAL A 1 3058 ? 228.114 210.326 169.542 1.00 26.82 ? 3058 VAL A CG2   1 
ATOM   12543 N N     . ILE A 1 3059 ? 224.661 211.224 166.571 1.00 26.07 ? 3059 ILE A N     1 
ATOM   12544 C CA    . ILE A 1 3059 ? 223.289 211.218 166.065 1.00 25.43 ? 3059 ILE A CA    1 
ATOM   12545 C C     . ILE A 1 3059 ? 223.147 210.241 164.908 1.00 22.92 ? 3059 ILE A C     1 
ATOM   12546 O O     . ILE A 1 3059 ? 222.206 209.440 164.865 1.00 24.04 ? 3059 ILE A O     1 
ATOM   12547 C CB    . ILE A 1 3059 ? 222.853 212.635 165.643 1.00 23.73 ? 3059 ILE A CB    1 
ATOM   12548 C CG1   . ILE A 1 3059 ? 222.908 213.605 166.820 1.00 25.42 ? 3059 ILE A CG1   1 
ATOM   12549 C CG2   . ILE A 1 3059 ? 221.454 212.604 165.045 1.00 25.90 ? 3059 ILE A CG2   1 
ATOM   12550 C CD1   . ILE A 1 3059 ? 221.992 213.231 167.943 1.00 28.15 ? 3059 ILE A CD1   1 
ATOM   12551 N N     . ARG A 1 3060 ? 224.074 210.285 163.957 1.00 22.40 ? 3060 ARG A N     1 
ATOM   12552 C CA    . ARG A 1 3060 ? 223.947 209.469 162.757 1.00 28.70 ? 3060 ARG A CA    1 
ATOM   12553 C C     . ARG A 1 3060 ? 224.580 208.087 162.887 1.00 29.87 ? 3060 ARG A C     1 
ATOM   12554 O O     . ARG A 1 3060 ? 224.443 207.277 161.964 1.00 30.06 ? 3060 ARG A O     1 
ATOM   12555 C CB    . ARG A 1 3060 ? 224.549 210.201 161.553 1.00 26.85 ? 3060 ARG A CB    1 
ATOM   12556 C CG    . ARG A 1 3060 ? 225.980 210.663 161.742 1.00 25.62 ? 3060 ARG A CG    1 
ATOM   12557 C CD    . ARG A 1 3060 ? 226.635 210.950 160.402 1.00 26.26 ? 3060 ARG A CD    1 
ATOM   12558 N NE    . ARG A 1 3060 ? 226.861 209.732 159.633 1.00 27.46 ? 3060 ARG A NE    1 
ATOM   12559 C CZ    . ARG A 1 3060 ? 226.873 209.675 158.309 1.00 31.05 ? 3060 ARG A CZ    1 
ATOM   12560 N NH1   . ARG A 1 3060 ? 226.664 210.752 157.569 1.00 28.93 ? 3060 ARG A NH1   1 
ATOM   12561 N NH2   . ARG A 1 3060 ? 227.096 208.508 157.711 1.00 30.59 ? 3060 ARG A NH2   1 
ATOM   12562 N N     . ASN A 1 3061 ? 225.251 207.786 163.998 1.00 23.14 ? 3061 ASN A N     1 
ATOM   12563 C CA    . ASN A 1 3061 ? 225.955 206.515 164.156 1.00 22.77 ? 3061 ASN A CA    1 
ATOM   12564 C C     . ASN A 1 3061 ? 225.671 205.880 165.511 1.00 24.56 ? 3061 ASN A C     1 
ATOM   12565 O O     . ASN A 1 3061 ? 226.538 205.230 166.099 1.00 26.17 ? 3061 ASN A O     1 
ATOM   12566 C CB    . ASN A 1 3061 ? 227.461 206.693 163.967 1.00 20.64 ? 3061 ASN A CB    1 
ATOM   12567 C CG    . ASN A 1 3061 ? 227.879 206.661 162.510 1.00 27.34 ? 3061 ASN A CG    1 
ATOM   12568 O OD1   . ASN A 1 3061 ? 227.201 207.208 161.644 1.00 27.37 ? 3061 ASN A OD1   1 
ATOM   12569 N ND2   . ASN A 1 3061 ? 229.005 206.015 162.235 1.00 29.18 ? 3061 ASN A ND2   1 
ATOM   12570 N N     . LEU A 1 3062 ? 224.457 206.043 166.032 1.00 21.45 ? 3062 LEU A N     1 
ATOM   12571 C CA    . LEU A 1 3062 ? 224.098 205.392 167.288 1.00 16.42 ? 3062 LEU A CA    1 
ATOM   12572 C C     . LEU A 1 3062 ? 222.609 205.097 167.300 1.00 15.68 ? 3062 LEU A C     1 
ATOM   12573 O O     . LEU A 1 3062 ? 221.795 205.997 167.072 1.00 20.86 ? 3062 LEU A O     1 
ATOM   12574 C CB    . LEU A 1 3062 ? 224.464 206.255 168.499 1.00 22.32 ? 3062 LEU A CB    1 
ATOM   12575 C CG    . LEU A 1 3062 ? 224.144 205.619 169.854 1.00 20.78 ? 3062 LEU A CG    1 
ATOM   12576 C CD1   . LEU A 1 3062 ? 225.254 204.673 170.287 1.00 16.61 ? 3062 LEU A CD1   1 
ATOM   12577 C CD2   . LEU A 1 3062 ? 223.890 206.680 170.912 1.00 20.22 ? 3062 LEU A CD2   1 
ATOM   12578 N N     . HIS A 1 3063 ? 222.261 203.843 167.575 1.00 15.64 ? 3063 HIS A N     1 
ATOM   12579 C CA    . HIS A 1 3063 ? 220.873 203.422 167.718 1.00 17.95 ? 3063 HIS A CA    1 
ATOM   12580 C C     . HIS A 1 3063 ? 220.722 202.703 169.048 1.00 13.53 ? 3063 HIS A C     1 
ATOM   12581 O O     . HIS A 1 3063 ? 221.457 201.751 169.329 1.00 16.82 ? 3063 HIS A O     1 
ATOM   12582 C CB    . HIS A 1 3063 ? 220.443 202.520 166.559 1.00 14.97 ? 3063 HIS A CB    1 
ATOM   12583 C CG    . HIS A 1 3063 ? 220.592 203.156 165.212 1.00 14.38 ? 3063 HIS A CG    1 
ATOM   12584 N ND1   . HIS A 1 3063 ? 221.819 203.399 164.635 1.00 17.74 ? 3063 HIS A ND1   1 
ATOM   12585 C CD2   . HIS A 1 3063 ? 219.667 203.612 164.335 1.00 15.25 ? 3063 HIS A CD2   1 
ATOM   12586 C CE1   . HIS A 1 3063 ? 221.644 203.968 163.456 1.00 18.70 ? 3063 HIS A CE1   1 
ATOM   12587 N NE2   . HIS A 1 3063 ? 220.348 204.109 163.251 1.00 17.22 ? 3063 HIS A NE2   1 
ATOM   12588 N N     . VAL A 1 3064 ? 219.774 203.156 169.860 1.00 10.14 ? 3064 VAL A N     1 
ATOM   12589 C CA    . VAL A 1 3064 ? 219.513 202.582 171.174 1.00 12.40 ? 3064 VAL A CA    1 
ATOM   12590 C C     . VAL A 1 3064 ? 218.203 201.811 171.114 1.00 16.12 ? 3064 VAL A C     1 
ATOM   12591 O O     . VAL A 1 3064 ? 217.189 202.328 170.630 1.00 20.53 ? 3064 VAL A O     1 
ATOM   12592 C CB    . VAL A 1 3064 ? 219.465 203.669 172.259 1.00 11.30 ? 3064 VAL A CB    1 
ATOM   12593 C CG1   . VAL A 1 3064 ? 219.198 203.045 173.614 1.00 11.89 ? 3064 VAL A CG1   1 
ATOM   12594 C CG2   . VAL A 1 3064 ? 220.769 204.445 172.282 1.00 15.84 ? 3064 VAL A CG2   1 
ATOM   12595 N N     . VAL A 1 3065 ? 218.224 200.576 171.606 1.00 13.99 ? 3065 VAL A N     1 
ATOM   12596 C CA    . VAL A 1 3065 ? 217.076 199.680 171.553 1.00 9.14  ? 3065 VAL A CA    1 
ATOM   12597 C C     . VAL A 1 3065 ? 216.677 199.333 172.979 1.00 9.80  ? 3065 VAL A C     1 
ATOM   12598 O O     . VAL A 1 3065 ? 217.523 198.925 173.782 1.00 17.48 ? 3065 VAL A O     1 
ATOM   12599 C CB    . VAL A 1 3065 ? 217.393 198.404 170.753 1.00 9.39  ? 3065 VAL A CB    1 
ATOM   12600 C CG1   . VAL A 1 3065 ? 216.212 197.454 170.783 1.00 12.87 ? 3065 VAL A CG1   1 
ATOM   12601 C CG2   . VAL A 1 3065 ? 217.792 198.749 169.331 1.00 12.40 ? 3065 VAL A CG2   1 
ATOM   12602 N N     . PHE A 1 3066 ? 215.396 199.495 173.290 1.00 9.40  ? 3066 PHE A N     1 
ATOM   12603 C CA    . PHE A 1 3066 ? 214.850 199.146 174.594 1.00 6.51  ? 3066 PHE A CA    1 
ATOM   12604 C C     . PHE A 1 3066 ? 213.900 197.969 174.447 1.00 7.15  ? 3066 PHE A C     1 
ATOM   12605 O O     . PHE A 1 3066 ? 212.978 198.009 173.627 1.00 12.19 ? 3066 PHE A O     1 
ATOM   12606 C CB    . PHE A 1 3066 ? 214.112 200.328 175.226 1.00 9.46  ? 3066 PHE A CB    1 
ATOM   12607 C CG    . PHE A 1 3066 ? 214.967 201.540 175.433 1.00 16.13 ? 3066 PHE A CG    1 
ATOM   12608 C CD1   . PHE A 1 3066 ? 215.734 201.672 176.576 1.00 14.85 ? 3066 PHE A CD1   1 
ATOM   12609 C CD2   . PHE A 1 3066 ? 214.993 202.555 174.493 1.00 14.28 ? 3066 PHE A CD2   1 
ATOM   12610 C CE1   . PHE A 1 3066 ? 216.519 202.789 176.773 1.00 13.18 ? 3066 PHE A CE1   1 
ATOM   12611 C CE2   . PHE A 1 3066 ? 215.775 203.672 174.684 1.00 13.94 ? 3066 PHE A CE2   1 
ATOM   12612 C CZ    . PHE A 1 3066 ? 216.538 203.790 175.826 1.00 15.85 ? 3066 PHE A CZ    1 
ATOM   12613 N N     . THR A 1 3067 ? 214.123 196.930 175.244 1.00 5.91  ? 3067 THR A N     1 
ATOM   12614 C CA    . THR A 1 3067 ? 213.236 195.778 175.309 1.00 7.63  ? 3067 THR A CA    1 
ATOM   12615 C C     . THR A 1 3067 ? 212.596 195.740 176.690 1.00 7.09  ? 3067 THR A C     1 
ATOM   12616 O O     . THR A 1 3067 ? 213.289 195.896 177.700 1.00 16.60 ? 3067 THR A O     1 
ATOM   12617 C CB    . THR A 1 3067 ? 213.995 194.481 175.021 1.00 9.79  ? 3067 THR A CB    1 
ATOM   12618 O OG1   . THR A 1 3067 ? 215.003 194.285 176.016 1.00 20.24 ? 3067 THR A OG1   1 
ATOM   12619 C CG2   . THR A 1 3067 ? 214.661 194.554 173.658 1.00 5.19  ? 3067 THR A CG2   1 
ATOM   12620 N N     . MET A 1 3068 ? 211.280 195.543 176.734 1.00 4.92  ? 3068 MET A N     1 
ATOM   12621 C CA    . MET A 1 3068 ? 210.531 195.765 177.962 1.00 6.25  ? 3068 MET A CA    1 
ATOM   12622 C C     . MET A 1 3068 ? 209.466 194.695 178.160 1.00 14.55 ? 3068 MET A C     1 
ATOM   12623 O O     . MET A 1 3068 ? 209.025 194.042 177.212 1.00 10.08 ? 3068 MET A O     1 
ATOM   12624 C CB    . MET A 1 3068 ? 209.876 197.152 177.960 1.00 8.31  ? 3068 MET A CB    1 
ATOM   12625 C CG    . MET A 1 3068 ? 209.674 197.746 179.339 1.00 14.81 ? 3068 MET A CG    1 
ATOM   12626 S SD    . MET A 1 3068 ? 209.651 199.546 179.323 1.00 34.75 ? 3068 MET A SD    1 
ATOM   12627 C CE    . MET A 1 3068 ? 211.339 199.901 178.845 1.00 18.34 ? 3068 MET A CE    1 
ATOM   12628 N N     . ASN A 1 3069 ? 209.077 194.521 179.420 1.00 23.49 ? 3069 ASN A N     1 
ATOM   12629 C CA    . ASN A 1 3069 ? 207.957 193.662 179.782 1.00 18.80 ? 3069 ASN A CA    1 
ATOM   12630 C C     . ASN A 1 3069 ? 206.661 194.270 179.253 1.00 18.89 ? 3069 ASN A C     1 
ATOM   12631 O O     . ASN A 1 3069 ? 206.456 195.484 179.381 1.00 21.78 ? 3069 ASN A O     1 
ATOM   12632 C CB    . ASN A 1 3069 ? 207.905 193.530 181.308 1.00 25.77 ? 3069 ASN A CB    1 
ATOM   12633 C CG    . ASN A 1 3069 ? 206.923 192.475 181.799 1.00 27.48 ? 3069 ASN A CG    1 
ATOM   12634 O OD1   . ASN A 1 3069 ? 206.243 191.815 181.022 1.00 25.90 ? 3069 ASN A OD1   1 
ATOM   12635 N ND2   . ASN A 1 3069 ? 206.846 192.324 183.116 1.00 24.47 ? 3069 ASN A ND2   1 
ATOM   12636 N N     . PRO A 1 3070 ? 205.765 193.475 178.659 1.00 18.11 ? 3070 PRO A N     1 
ATOM   12637 C CA    . PRO A 1 3070 ? 204.485 194.026 178.188 1.00 18.79 ? 3070 PRO A CA    1 
ATOM   12638 C C     . PRO A 1 3070 ? 203.566 194.522 179.296 1.00 22.19 ? 3070 PRO A C     1 
ATOM   12639 O O     . PRO A 1 3070 ? 202.434 194.932 179.020 1.00 22.84 ? 3070 PRO A O     1 
ATOM   12640 C CB    . PRO A 1 3070 ? 203.857 192.842 177.438 1.00 15.71 ? 3070 PRO A CB    1 
ATOM   12641 C CG    . PRO A 1 3070 ? 204.601 191.641 177.911 1.00 18.71 ? 3070 PRO A CG    1 
ATOM   12642 C CD    . PRO A 1 3070 ? 205.990 192.128 178.120 1.00 19.87 ? 3070 PRO A CD    1 
ATOM   12643 N N     . SER A 1 3071 ? 204.024 194.484 180.546 1.00 23.53 ? 3071 SER A N     1 
ATOM   12644 C CA    . SER A 1 3071 ? 203.245 195.017 181.657 1.00 26.44 ? 3071 SER A CA    1 
ATOM   12645 C C     . SER A 1 3071 ? 203.123 196.531 181.544 1.00 28.06 ? 3071 SER A C     1 
ATOM   12646 O O     . SER A 1 3071 ? 204.099 197.255 181.766 1.00 30.19 ? 3071 SER A O     1 
ATOM   12647 C CB    . SER A 1 3071 ? 203.882 194.631 182.992 1.00 27.09 ? 3071 SER A CB    1 
ATOM   12648 O OG    . SER A 1 3071 ? 205.222 195.086 183.064 1.00 27.24 ? 3071 SER A OG    1 
ATOM   12649 N N     . SER A 1 3072 ? 201.925 197.018 181.204 1.00 28.66 ? 3072 SER A N     1 
ATOM   12650 C CA    . SER A 1 3072 ? 201.719 198.448 180.998 1.00 32.01 ? 3072 SER A CA    1 
ATOM   12651 C C     . SER A 1 3072 ? 201.922 199.259 182.271 1.00 33.45 ? 3072 SER A C     1 
ATOM   12652 O O     . SER A 1 3072 ? 202.234 200.453 182.186 1.00 29.04 ? 3072 SER A O     1 
ATOM   12653 C CB    . SER A 1 3072 ? 200.318 198.701 180.440 1.00 32.78 ? 3072 SER A CB    1 
ATOM   12654 O OG    . SER A 1 3072 ? 200.177 198.149 179.142 1.00 27.78 ? 3072 SER A OG    1 
ATOM   12655 N N     . GLU A 1 3073 ? 201.751 198.640 183.442 1.00 34.52 ? 3073 GLU A N     1 
ATOM   12656 C CA    . GLU A 1 3073 ? 201.988 199.346 184.696 1.00 34.57 ? 3073 GLU A CA    1 
ATOM   12657 C C     . GLU A 1 3073 ? 203.435 199.806 184.797 1.00 33.85 ? 3073 GLU A C     1 
ATOM   12658 O O     . GLU A 1 3073 ? 203.713 200.918 185.264 1.00 29.77 ? 3073 GLU A O     1 
ATOM   12659 C CB    . GLU A 1 3073 ? 201.625 198.446 185.877 1.00 33.55 ? 3073 GLU A CB    1 
ATOM   12660 C CG    . GLU A 1 3073 ? 201.786 199.098 187.240 1.00 37.19 ? 3073 GLU A CG    1 
ATOM   12661 C CD    . GLU A 1 3073 ? 200.824 200.251 187.453 1.00 38.47 ? 3073 GLU A CD    1 
ATOM   12662 O OE1   . GLU A 1 3073 ? 199.747 200.254 186.821 1.00 37.63 ? 3073 GLU A OE1   1 
ATOM   12663 O OE2   . GLU A 1 3073 ? 201.141 201.151 188.258 1.00 34.92 ? 3073 GLU A OE2   1 
ATOM   12664 N N     . GLY A 1 3074 ? 204.373 198.962 184.367 1.00 32.37 ? 3074 GLY A N     1 
ATOM   12665 C CA    . GLY A 1 3074 ? 205.760 199.386 184.307 1.00 30.87 ? 3074 GLY A CA    1 
ATOM   12666 C C     . GLY A 1 3074 ? 205.978 200.513 183.316 1.00 33.28 ? 3074 GLY A C     1 
ATOM   12667 O O     . GLY A 1 3074 ? 206.735 201.447 183.583 1.00 34.00 ? 3074 GLY A O     1 
ATOM   12668 N N     . LEU A 1 3075 ? 205.316 200.442 182.160 1.00 32.11 ? 3075 LEU A N     1 
ATOM   12669 C CA    . LEU A 1 3075 ? 205.466 201.490 181.156 1.00 29.54 ? 3075 LEU A CA    1 
ATOM   12670 C C     . LEU A 1 3075 ? 204.951 202.832 181.661 1.00 32.51 ? 3075 LEU A C     1 
ATOM   12671 O O     . LEU A 1 3075 ? 205.495 203.882 181.291 1.00 32.57 ? 3075 LEU A O     1 
ATOM   12672 C CB    . LEU A 1 3075 ? 204.737 201.093 179.873 1.00 29.23 ? 3075 LEU A CB    1 
ATOM   12673 C CG    . LEU A 1 3075 ? 205.029 201.924 178.622 1.00 32.09 ? 3075 LEU A CG    1 
ATOM   12674 C CD1   . LEU A 1 3075 ? 206.524 202.142 178.444 1.00 29.08 ? 3075 LEU A CD1   1 
ATOM   12675 C CD2   . LEU A 1 3075 ? 204.429 201.261 177.399 1.00 27.96 ? 3075 LEU A CD2   1 
ATOM   12676 N N     . LYS A 1 3076 ? 203.924 202.817 182.517 1.00 31.59 ? 3076 LYS A N     1 
ATOM   12677 C CA    . LYS A 1 3076 ? 203.328 204.062 182.998 1.00 31.99 ? 3076 LYS A CA    1 
ATOM   12678 C C     . LYS A 1 3076 ? 204.365 204.953 183.672 1.00 35.42 ? 3076 LYS A C     1 
ATOM   12679 O O     . LYS A 1 3076 ? 204.443 206.154 183.387 1.00 35.73 ? 3076 LYS A O     1 
ATOM   12680 C CB    . LYS A 1 3076 ? 202.177 203.766 183.960 1.00 32.57 ? 3076 LYS A CB    1 
ATOM   12681 C CG    . LYS A 1 3076 ? 200.969 203.100 183.326 1.00 34.02 ? 3076 LYS A CG    1 
ATOM   12682 C CD    . LYS A 1 3076 ? 199.991 202.622 184.390 1.00 34.00 ? 3076 LYS A CD    1 
ATOM   12683 C CE    . LYS A 1 3076 ? 198.744 202.002 183.775 1.00 34.99 ? 3076 LYS A CE    1 
ATOM   12684 N NZ    . LYS A 1 3076 ? 199.067 200.864 182.871 1.00 34.25 ? 3076 LYS A NZ    1 
ATOM   12685 N N     . ASP A 1 3077 ? 205.174 204.389 184.569 1.00 30.45 ? 3077 ASP A N     1 
ATOM   12686 C CA    . ASP A 1 3077 ? 206.210 205.182 185.217 1.00 30.37 ? 3077 ASP A CA    1 
ATOM   12687 C C     . ASP A 1 3077 ? 207.548 205.124 184.490 1.00 32.86 ? 3077 ASP A C     1 
ATOM   12688 O O     . ASP A 1 3077 ? 208.410 205.972 184.751 1.00 29.31 ? 3077 ASP A O     1 
ATOM   12689 C CB    . ASP A 1 3077 ? 206.377 204.767 186.689 1.00 30.59 ? 3077 ASP A CB    1 
ATOM   12690 C CG    . ASP A 1 3077 ? 206.836 203.330 186.860 1.00 33.35 ? 3077 ASP A CG    1 
ATOM   12691 O OD1   . ASP A 1 3077 ? 206.994 202.619 185.854 1.00 31.36 ? 3077 ASP A OD1   1 
ATOM   12692 O OD2   . ASP A 1 3077 ? 207.039 202.909 188.018 1.00 32.94 ? 3077 ASP A OD2   1 
ATOM   12693 N N     . ARG A 1 3078 ? 207.737 204.172 183.570 1.00 30.91 ? 3078 ARG A N     1 
ATOM   12694 C CA    . ARG A 1 3078 ? 208.906 204.219 182.700 1.00 31.84 ? 3078 ARG A CA    1 
ATOM   12695 C C     . ARG A 1 3078 ? 208.873 205.472 181.838 1.00 32.99 ? 3078 ARG A C     1 
ATOM   12696 O O     . ARG A 1 3078 ? 209.906 206.113 181.613 1.00 32.02 ? 3078 ARG A O     1 
ATOM   12697 C CB    . ARG A 1 3078 ? 208.955 202.970 181.819 1.00 31.73 ? 3078 ARG A CB    1 
ATOM   12698 C CG    . ARG A 1 3078 ? 209.630 201.758 182.448 1.00 32.25 ? 3078 ARG A CG    1 
ATOM   12699 C CD    . ARG A 1 3078 ? 211.126 201.923 182.629 1.00 32.49 ? 3078 ARG A CD    1 
ATOM   12700 N NE    . ARG A 1 3078 ? 211.592 201.150 183.774 1.00 37.14 ? 3078 ARG A NE    1 
ATOM   12701 C CZ    . ARG A 1 3078 ? 212.866 200.945 184.079 1.00 35.40 ? 3078 ARG A CZ    1 
ATOM   12702 N NH1   . ARG A 1 3078 ? 213.843 201.412 183.321 1.00 30.83 ? 3078 ARG A NH1   1 
ATOM   12703 N NH2   . ARG A 1 3078 ? 213.167 200.245 185.169 1.00 34.44 ? 3078 ARG A NH2   1 
ATOM   12704 N N     . ALA A 1 3079 ? 207.686 205.831 181.342 1.00 32.72 ? 3079 ALA A N     1 
ATOM   12705 C CA    . ALA A 1 3079 ? 207.536 207.077 180.597 1.00 33.74 ? 3079 ALA A CA    1 
ATOM   12706 C C     . ALA A 1 3079 ? 207.825 208.285 181.479 1.00 32.32 ? 3079 ALA A C     1 
ATOM   12707 O O     . ALA A 1 3079 ? 208.459 209.249 181.035 1.00 30.86 ? 3079 ALA A O     1 
ATOM   12708 C CB    . ALA A 1 3079 ? 206.129 207.169 180.009 1.00 31.32 ? 3079 ALA A CB    1 
ATOM   12709 N N     . ALA A 1 3080 ? 207.359 208.255 182.730 1.00 31.88 ? 3080 ALA A N     1 
ATOM   12710 C CA    . ALA A 1 3080 ? 207.582 209.379 183.633 1.00 33.91 ? 3080 ALA A CA    1 
ATOM   12711 C C     . ALA A 1 3080 ? 209.064 209.574 183.925 1.00 33.63 ? 3080 ALA A C     1 
ATOM   12712 O O     . ALA A 1 3080 ? 209.549 210.710 183.965 1.00 30.73 ? 3080 ALA A O     1 
ATOM   12713 C CB    . ALA A 1 3080 ? 206.803 209.172 184.931 1.00 32.59 ? 3080 ALA A CB    1 
ATOM   12714 N N     . THR A 1 3081 ? 209.799 208.479 184.139 1.00 35.46 ? 3081 THR A N     1 
ATOM   12715 C CA    . THR A 1 3081 ? 211.229 208.595 184.410 1.00 36.07 ? 3081 THR A CA    1 
ATOM   12716 C C     . THR A 1 3081 ? 211.981 209.161 183.211 1.00 37.17 ? 3081 THR A C     1 
ATOM   12717 O O     . THR A 1 3081 ? 212.876 209.999 183.372 1.00 33.77 ? 3081 THR A O     1 
ATOM   12718 C CB    . THR A 1 3081 ? 211.805 207.237 184.808 1.00 37.89 ? 3081 THR A CB    1 
ATOM   12719 O OG1   . THR A 1 3081 ? 211.547 206.282 183.771 1.00 41.05 ? 3081 THR A OG1   1 
ATOM   12720 C CG2   . THR A 1 3081 ? 211.187 206.754 186.111 1.00 33.01 ? 3081 THR A CG2   1 
ATOM   12721 N N     . SER A 1 3082 ? 211.637 208.717 182.003 1.00 37.47 ? 3082 SER A N     1 
ATOM   12722 C CA    . SER A 1 3082 ? 212.315 209.158 180.785 1.00 34.56 ? 3082 SER A CA    1 
ATOM   12723 C C     . SER A 1 3082 ? 211.271 209.500 179.729 1.00 35.42 ? 3082 SER A C     1 
ATOM   12724 O O     . SER A 1 3082 ? 210.732 208.600 179.066 1.00 33.56 ? 3082 SER A O     1 
ATOM   12725 C CB    . SER A 1 3082 ? 213.281 208.094 180.272 1.00 33.79 ? 3082 SER A CB    1 
ATOM   12726 O OG    . SER A 1 3082 ? 213.913 208.512 179.075 1.00 34.81 ? 3082 SER A OG    1 
ATOM   12727 N N     . PRO A 1 3083 ? 210.952 210.785 179.550 1.00 32.17 ? 3083 PRO A N     1 
ATOM   12728 C CA    . PRO A 1 3083 ? 209.988 211.161 178.504 1.00 27.11 ? 3083 PRO A CA    1 
ATOM   12729 C C     . PRO A 1 3083 ? 210.473 210.867 177.097 1.00 26.91 ? 3083 PRO A C     1 
ATOM   12730 O O     . PRO A 1 3083 ? 209.646 210.763 176.184 1.00 31.66 ? 3083 PRO A O     1 
ATOM   12731 C CB    . PRO A 1 3083 ? 209.798 212.667 178.727 1.00 29.26 ? 3083 PRO A CB    1 
ATOM   12732 C CG    . PRO A 1 3083 ? 211.055 213.105 179.394 1.00 31.40 ? 3083 PRO A CG    1 
ATOM   12733 C CD    . PRO A 1 3083 ? 211.484 211.959 180.263 1.00 29.43 ? 3083 PRO A CD    1 
ATOM   12734 N N     . ALA A 1 3084 ? 211.785 210.729 176.890 1.00 26.17 ? 3084 ALA A N     1 
ATOM   12735 C CA    . ALA A 1 3084 ? 212.315 210.446 175.563 1.00 29.92 ? 3084 ALA A CA    1 
ATOM   12736 C C     . ALA A 1 3084 ? 211.943 209.059 175.061 1.00 33.29 ? 3084 ALA A C     1 
ATOM   12737 O O     . ALA A 1 3084 ? 212.150 208.774 173.877 1.00 33.27 ? 3084 ALA A O     1 
ATOM   12738 C CB    . ALA A 1 3084 ? 213.836 210.603 175.556 1.00 27.20 ? 3084 ALA A CB    1 
ATOM   12739 N N     . LEU A 1 3085 ? 211.412 208.191 175.925 1.00 27.70 ? 3085 LEU A N     1 
ATOM   12740 C CA    . LEU A 1 3085 ? 210.970 206.872 175.495 1.00 25.20 ? 3085 LEU A CA    1 
ATOM   12741 C C     . LEU A 1 3085 ? 209.799 206.932 174.524 1.00 27.82 ? 3085 LEU A C     1 
ATOM   12742 O O     . LEU A 1 3085 ? 209.694 206.060 173.656 1.00 31.98 ? 3085 LEU A O     1 
ATOM   12743 C CB    . LEU A 1 3085 ? 210.595 206.023 176.710 1.00 26.03 ? 3085 LEU A CB    1 
ATOM   12744 C CG    . LEU A 1 3085 ? 211.735 205.206 177.323 1.00 30.87 ? 3085 LEU A CG    1 
ATOM   12745 C CD1   . LEU A 1 3085 ? 211.217 204.288 178.420 1.00 27.69 ? 3085 LEU A CD1   1 
ATOM   12746 C CD2   . LEU A 1 3085 ? 212.461 204.411 176.255 1.00 25.42 ? 3085 LEU A CD2   1 
ATOM   12747 N N     . PHE A 1 3086 ? 208.918 207.927 174.647 1.00 28.10 ? 3086 PHE A N     1 
ATOM   12748 C CA    . PHE A 1 3086 ? 207.839 208.135 173.687 1.00 27.76 ? 3086 PHE A CA    1 
ATOM   12749 C C     . PHE A 1 3086 ? 208.136 209.288 172.735 1.00 28.68 ? 3086 PHE A C     1 
ATOM   12750 O O     . PHE A 1 3086 ? 207.253 209.708 171.981 1.00 31.16 ? 3086 PHE A O     1 
ATOM   12751 C CB    . PHE A 1 3086 ? 206.500 208.378 174.391 1.00 28.61 ? 3086 PHE A CB    1 
ATOM   12752 C CG    . PHE A 1 3086 ? 206.070 207.268 175.316 1.00 28.98 ? 3086 PHE A CG    1 
ATOM   12753 C CD1   . PHE A 1 3086 ? 204.984 207.446 176.156 1.00 30.06 ? 3086 PHE A CD1   1 
ATOM   12754 C CD2   . PHE A 1 3086 ? 206.708 206.037 175.313 1.00 27.98 ? 3086 PHE A CD2   1 
ATOM   12755 C CE1   . PHE A 1 3086 ? 204.566 206.436 176.998 1.00 32.86 ? 3086 PHE A CE1   1 
ATOM   12756 C CE2   . PHE A 1 3086 ? 206.296 205.024 176.156 1.00 31.22 ? 3086 PHE A CE2   1 
ATOM   12757 C CZ    . PHE A 1 3086 ? 205.223 205.224 176.998 1.00 32.09 ? 3086 PHE A CZ    1 
ATOM   12758 N N     . ASN A 1 3087 ? 209.361 209.808 172.750 1.00 27.69 ? 3087 ASN A N     1 
ATOM   12759 C CA    . ASN A 1 3087 ? 209.746 210.922 171.895 1.00 27.22 ? 3087 ASN A CA    1 
ATOM   12760 C C     . ASN A 1 3087 ? 210.666 210.497 170.762 1.00 26.32 ? 3087 ASN A C     1 
ATOM   12761 O O     . ASN A 1 3087 ? 210.398 210.806 169.598 1.00 27.97 ? 3087 ASN A O     1 
ATOM   12762 C CB    . ASN A 1 3087 ? 210.422 212.019 172.732 1.00 29.17 ? 3087 ASN A CB    1 
ATOM   12763 C CG    . ASN A 1 3087 ? 210.876 213.199 171.894 1.00 33.91 ? 3087 ASN A CG    1 
ATOM   12764 O OD1   . ASN A 1 3087 ? 211.966 213.734 172.092 1.00 32.17 ? 3087 ASN A OD1   1 
ATOM   12765 N ND2   . ASN A 1 3087 ? 210.034 213.615 170.954 1.00 35.45 ? 3087 ASN A ND2   1 
ATOM   12766 N N     . ARG A 1 3088 ? 211.750 209.789 171.075 1.00 25.82 ? 3088 ARG A N     1 
ATOM   12767 C CA    . ARG A 1 3088 ? 212.707 209.355 170.070 1.00 26.91 ? 3088 ARG A CA    1 
ATOM   12768 C C     . ARG A 1 3088 ? 212.655 207.862 169.786 1.00 24.78 ? 3088 ARG A C     1 
ATOM   12769 O O     . ARG A 1 3088 ? 213.297 207.410 168.832 1.00 25.75 ? 3088 ARG A O     1 
ATOM   12770 C CB    . ARG A 1 3088 ? 214.131 209.736 170.497 1.00 26.76 ? 3088 ARG A CB    1 
ATOM   12771 C CG    . ARG A 1 3088 ? 214.331 211.226 170.691 1.00 28.59 ? 3088 ARG A CG    1 
ATOM   12772 C CD    . ARG A 1 3088 ? 214.637 211.915 169.373 1.00 25.07 ? 3088 ARG A CD    1 
ATOM   12773 N NE    . ARG A 1 3088 ? 214.967 213.323 169.558 1.00 23.29 ? 3088 ARG A NE    1 
ATOM   12774 C CZ    . ARG A 1 3088 ? 214.074 214.303 169.584 1.00 25.77 ? 3088 ARG A CZ    1 
ATOM   12775 N NH1   . ARG A 1 3088 ? 212.780 214.063 169.450 1.00 25.50 ? 3088 ARG A NH1   1 
ATOM   12776 N NH2   . ARG A 1 3088 ? 214.490 215.555 169.750 1.00 25.16 ? 3088 ARG A NH2   1 
ATOM   12777 N N     . CYS A 1 3089 ? 211.915 207.090 170.576 1.00 21.04 ? 3089 CYS A N     1 
ATOM   12778 C CA    . CYS A 1 3089 ? 211.828 205.645 170.413 1.00 10.63 ? 3089 CYS A CA    1 
ATOM   12779 C C     . CYS A 1 3089 ? 210.463 205.287 169.844 1.00 9.65  ? 3089 CYS A C     1 
ATOM   12780 O O     . CYS A 1 3089 ? 209.434 205.580 170.460 1.00 13.18 ? 3089 CYS A O     1 
ATOM   12781 C CB    . CYS A 1 3089 ? 212.059 204.932 171.744 1.00 13.21 ? 3089 CYS A CB    1 
ATOM   12782 S SG    . CYS A 1 3089 ? 213.581 205.408 172.584 1.00 30.86 ? 3089 CYS A SG    1 
ATOM   12783 N N     . VAL A 1 3090 ? 210.460 204.652 168.674 1.00 10.94 ? 3090 VAL A N     1 
ATOM   12784 C CA    . VAL A 1 3090 ? 209.237 204.157 168.053 1.00 7.08  ? 3090 VAL A CA    1 
ATOM   12785 C C     . VAL A 1 3090 ? 208.975 202.777 168.645 1.00 11.17 ? 3090 VAL A C     1 
ATOM   12786 O O     . VAL A 1 3090 ? 209.671 201.811 168.332 1.00 18.20 ? 3090 VAL A O     1 
ATOM   12787 C CB    . VAL A 1 3090 ? 209.351 204.107 166.530 1.00 5.73  ? 3090 VAL A CB    1 
ATOM   12788 C CG1   . VAL A 1 3090 ? 208.049 203.625 165.921 1.00 10.36 ? 3090 VAL A CG1   1 
ATOM   12789 C CG2   . VAL A 1 3090 ? 209.720 205.475 165.985 1.00 17.22 ? 3090 VAL A CG2   1 
ATOM   12790 N N     . LEU A 1 3091 ? 207.969 202.686 169.509 1.00 7.25  ? 3091 LEU A N     1 
ATOM   12791 C CA    . LEU A 1 3091 ? 207.708 201.431 170.197 1.00 5.88  ? 3091 LEU A CA    1 
ATOM   12792 C C     . LEU A 1 3091 ? 207.096 200.414 169.243 1.00 7.58  ? 3091 LEU A C     1 
ATOM   12793 O O     . LEU A 1 3091 ? 206.198 200.736 168.460 1.00 9.87  ? 3091 LEU A O     1 
ATOM   12794 C CB    . LEU A 1 3091 ? 206.796 201.651 171.405 1.00 7.87  ? 3091 LEU A CB    1 
ATOM   12795 C CG    . LEU A 1 3091 ? 205.310 201.954 171.228 1.00 9.80  ? 3091 LEU A CG    1 
ATOM   12796 C CD1   . LEU A 1 3091 ? 204.606 201.745 172.549 1.00 7.73  ? 3091 LEU A CD1   1 
ATOM   12797 C CD2   . LEU A 1 3091 ? 205.083 203.374 170.732 1.00 9.92  ? 3091 LEU A CD2   1 
ATOM   12798 N N     . ASN A 1 3092 ? 207.602 199.185 169.301 1.00 2.97  ? 3092 ASN A N     1 
ATOM   12799 C CA    . ASN A 1 3092 ? 207.086 198.066 168.522 1.00 0.16  ? 3092 ASN A CA    1 
ATOM   12800 C C     . ASN A 1 3092 ? 206.578 197.019 169.502 1.00 4.38  ? 3092 ASN A C     1 
ATOM   12801 O O     . ASN A 1 3092 ? 207.367 196.414 170.233 1.00 16.41 ? 3092 ASN A O     1 
ATOM   12802 C CB    . ASN A 1 3092 ? 208.166 197.485 167.612 1.00 4.35  ? 3092 ASN A CB    1 
ATOM   12803 C CG    . ASN A 1 3092 ? 208.347 198.286 166.344 1.00 11.56 ? 3092 ASN A CG    1 
ATOM   12804 O OD1   . ASN A 1 3092 ? 207.415 198.445 165.561 1.00 20.36 ? 3092 ASN A OD1   1 
ATOM   12805 N ND2   . ASN A 1 3092 ? 209.553 198.797 166.134 1.00 5.92  ? 3092 ASN A ND2   1 
ATOM   12806 N N     . TRP A 1 3093 ? 205.267 196.808 169.521 1.00 2.45  ? 3093 TRP A N     1 
ATOM   12807 C CA    . TRP A 1 3093 ? 204.668 195.869 170.458 1.00 4.63  ? 3093 TRP A CA    1 
ATOM   12808 C C     . TRP A 1 3093 ? 204.778 194.451 169.908 1.00 6.74  ? 3093 TRP A C     1 
ATOM   12809 O O     . TRP A 1 3093 ? 204.254 194.157 168.828 1.00 11.58 ? 3093 TRP A O     1 
ATOM   12810 C CB    . TRP A 1 3093 ? 203.209 196.235 170.715 1.00 9.22  ? 3093 TRP A CB    1 
ATOM   12811 C CG    . TRP A 1 3093 ? 202.423 195.136 171.342 1.00 10.30 ? 3093 TRP A CG    1 
ATOM   12812 C CD1   . TRP A 1 3093 ? 201.737 194.150 170.701 1.00 10.89 ? 3093 TRP A CD1   1 
ATOM   12813 C CD2   . TRP A 1 3093 ? 202.227 194.917 172.742 1.00 10.01 ? 3093 TRP A CD2   1 
ATOM   12814 N NE1   . TRP A 1 3093 ? 201.133 193.322 171.614 1.00 14.03 ? 3093 TRP A NE1   1 
ATOM   12815 C CE2   . TRP A 1 3093 ? 201.418 193.773 172.875 1.00 9.25  ? 3093 TRP A CE2   1 
ATOM   12816 C CE3   . TRP A 1 3093 ? 202.659 195.575 173.896 1.00 13.27 ? 3093 TRP A CE3   1 
ATOM   12817 C CZ2   . TRP A 1 3093 ? 201.035 193.271 174.115 1.00 11.00 ? 3093 TRP A CZ2   1 
ATOM   12818 C CZ3   . TRP A 1 3093 ? 202.276 195.078 175.125 1.00 15.37 ? 3093 TRP A CZ3   1 
ATOM   12819 C CH2   . TRP A 1 3093 ? 201.470 193.939 175.224 1.00 15.63 ? 3093 TRP A CH2   1 
ATOM   12820 N N     . PHE A 1 3094 ? 205.452 193.574 170.650 1.00 6.92  ? 3094 PHE A N     1 
ATOM   12821 C CA    . PHE A 1 3094 ? 205.520 192.155 170.316 1.00 6.83  ? 3094 PHE A CA    1 
ATOM   12822 C C     . PHE A 1 3094 ? 204.388 191.431 171.034 1.00 12.50 ? 3094 PHE A C     1 
ATOM   12823 O O     . PHE A 1 3094 ? 204.377 191.347 172.266 1.00 12.39 ? 3094 PHE A O     1 
ATOM   12824 C CB    . PHE A 1 3094 ? 206.866 191.553 170.710 1.00 4.50  ? 3094 PHE A CB    1 
ATOM   12825 C CG    . PHE A 1 3094 ? 207.989 191.884 169.774 1.00 2.11  ? 3094 PHE A CG    1 
ATOM   12826 C CD1   . PHE A 1 3094 ? 208.235 193.186 169.386 1.00 5.65  ? 3094 PHE A CD1   1 
ATOM   12827 C CD2   . PHE A 1 3094 ? 208.814 190.881 169.293 1.00 5.13  ? 3094 PHE A CD2   1 
ATOM   12828 C CE1   . PHE A 1 3094 ? 209.273 193.478 168.527 1.00 11.04 ? 3094 PHE A CE1   1 
ATOM   12829 C CE2   . PHE A 1 3094 ? 209.856 191.169 168.437 1.00 1.35  ? 3094 PHE A CE2   1 
ATOM   12830 C CZ    . PHE A 1 3094 ? 210.087 192.470 168.054 1.00 7.95  ? 3094 PHE A CZ    1 
ATOM   12831 N N     . GLY A 1 3095 ? 203.442 190.907 170.271 1.00 8.99  ? 3095 GLY A N     1 
ATOM   12832 C CA    . GLY A 1 3095 ? 202.423 190.064 170.851 1.00 12.91 ? 3095 GLY A CA    1 
ATOM   12833 C C     . GLY A 1 3095 ? 202.960 188.681 171.161 1.00 18.10 ? 3095 GLY A C     1 
ATOM   12834 O O     . GLY A 1 3095 ? 203.987 188.240 170.645 1.00 17.20 ? 3095 GLY A O     1 
ATOM   12835 N N     . ASP A 1 3096 ? 202.246 187.984 172.039 1.00 17.25 ? 3096 ASP A N     1 
ATOM   12836 C CA    . ASP A 1 3096 ? 202.587 186.601 172.326 1.00 13.25 ? 3096 ASP A CA    1 
ATOM   12837 C C     . ASP A 1 3096 ? 202.436 185.766 171.061 1.00 14.41 ? 3096 ASP A C     1 
ATOM   12838 O O     . ASP A 1 3096 ? 201.586 186.044 170.210 1.00 17.28 ? 3096 ASP A O     1 
ATOM   12839 C CB    . ASP A 1 3096 ? 201.696 186.050 173.439 1.00 16.93 ? 3096 ASP A CB    1 
ATOM   12840 C CG    . ASP A 1 3096 ? 202.105 184.660 173.879 1.00 21.31 ? 3096 ASP A CG    1 
ATOM   12841 O OD1   . ASP A 1 3096 ? 203.320 184.374 173.897 1.00 19.96 ? 3096 ASP A OD1   1 
ATOM   12842 O OD2   . ASP A 1 3096 ? 201.211 183.852 174.205 1.00 21.80 ? 3096 ASP A OD2   1 
ATOM   12843 N N     . TRP A 1 3097 ? 203.290 184.752 170.929 1.00 9.73  ? 3097 TRP A N     1 
ATOM   12844 C CA    . TRP A 1 3097 ? 203.321 183.941 169.718 1.00 11.86 ? 3097 TRP A CA    1 
ATOM   12845 C C     . TRP A 1 3097 ? 201.938 183.389 169.415 1.00 10.90 ? 3097 TRP A C     1 
ATOM   12846 O O     . TRP A 1 3097 ? 201.351 182.671 170.229 1.00 14.92 ? 3097 TRP A O     1 
ATOM   12847 C CB    . TRP A 1 3097 ? 204.321 182.796 169.875 1.00 9.79  ? 3097 TRP A CB    1 
ATOM   12848 C CG    . TRP A 1 3097 ? 205.750 183.211 169.746 1.00 5.37  ? 3097 TRP A CG    1 
ATOM   12849 C CD1   . TRP A 1 3097 ? 206.228 184.481 169.633 1.00 6.36  ? 3097 TRP A CD1   1 
ATOM   12850 C CD2   . TRP A 1 3097 ? 206.890 182.348 169.710 1.00 6.35  ? 3097 TRP A CD2   1 
ATOM   12851 N NE1   . TRP A 1 3097 ? 207.597 184.464 169.540 1.00 0.87  ? 3097 TRP A NE1   1 
ATOM   12852 C CE2   . TRP A 1 3097 ? 208.029 183.165 169.583 1.00 6.90  ? 3097 TRP A CE2   1 
ATOM   12853 C CE3   . TRP A 1 3097 ? 207.059 180.962 169.778 1.00 8.76  ? 3097 TRP A CE3   1 
ATOM   12854 C CZ2   . TRP A 1 3097 ? 209.319 182.644 169.520 1.00 5.66  ? 3097 TRP A CZ2   1 
ATOM   12855 C CZ3   . TRP A 1 3097 ? 208.341 180.447 169.715 1.00 4.85  ? 3097 TRP A CZ3   1 
ATOM   12856 C CH2   . TRP A 1 3097 ? 209.454 181.286 169.587 1.00 0.00  ? 3097 TRP A CH2   1 
ATOM   12857 N N     . SER A 1 3098 ? 201.416 183.737 168.243 1.00 5.19  ? 3098 SER A N     1 
ATOM   12858 C CA    . SER A 1 3098 ? 200.075 183.323 167.871 1.00 8.57  ? 3098 SER A CA    1 
ATOM   12859 C C     . SER A 1 3098 ? 200.032 181.817 167.630 1.00 6.86  ? 3098 SER A C     1 
ATOM   12860 O O     . SER A 1 3098 ? 201.059 181.137 167.569 1.00 10.01 ? 3098 SER A O     1 
ATOM   12861 C CB    . SER A 1 3098 ? 199.609 184.080 166.629 1.00 12.76 ? 3098 SER A CB    1 
ATOM   12862 O OG    . SER A 1 3098 ? 200.437 183.792 165.517 1.00 15.11 ? 3098 SER A OG    1 
ATOM   12863 N N     . THR A 1 3099 ? 198.810 181.295 167.503 1.00 9.04  ? 3099 THR A N     1 
ATOM   12864 C CA    . THR A 1 3099 ? 198.640 179.871 167.241 1.00 8.56  ? 3099 THR A CA    1 
ATOM   12865 C C     . THR A 1 3099 ? 199.373 179.446 165.978 1.00 6.61  ? 3099 THR A C     1 
ATOM   12866 O O     . THR A 1 3099 ? 199.933 178.346 165.927 1.00 11.10 ? 3099 THR A O     1 
ATOM   12867 C CB    . THR A 1 3099 ? 197.153 179.531 167.133 1.00 9.50  ? 3099 THR A CB    1 
ATOM   12868 O OG1   . THR A 1 3099 ? 196.426 180.228 168.152 1.00 11.97 ? 3099 THR A OG1   1 
ATOM   12869 C CG2   . THR A 1 3099 ? 196.936 178.041 167.292 1.00 10.46 ? 3099 THR A CG2   1 
ATOM   12870 N N     . GLU A 1 3100 ? 199.386 180.301 164.955 1.00 7.55  ? 3100 GLU A N     1 
ATOM   12871 C CA    . GLU A 1 3100 ? 200.154 180.009 163.750 1.00 10.81 ? 3100 GLU A CA    1 
ATOM   12872 C C     . GLU A 1 3100 ? 201.640 179.897 164.065 1.00 5.10  ? 3100 GLU A C     1 
ATOM   12873 O O     . GLU A 1 3100 ? 202.322 178.981 163.593 1.00 8.50  ? 3100 GLU A O     1 
ATOM   12874 C CB    . GLU A 1 3100 ? 199.904 181.094 162.703 1.00 13.66 ? 3100 GLU A CB    1 
ATOM   12875 C CG    . GLU A 1 3100 ? 200.206 180.679 161.275 1.00 13.71 ? 3100 GLU A CG    1 
ATOM   12876 C CD    . GLU A 1 3100 ? 199.434 181.498 160.259 1.00 17.30 ? 3100 GLU A CD    1 
ATOM   12877 O OE1   . GLU A 1 3100 ? 199.297 182.723 160.464 1.00 18.39 ? 3100 GLU A OE1   1 
ATOM   12878 O OE2   . GLU A 1 3100 ? 198.964 180.920 159.258 1.00 19.01 ? 3100 GLU A OE2   1 
ATOM   12879 N N     . ALA A 1 3101 ? 202.159 180.826 164.873 1.00 2.73  ? 3101 ALA A N     1 
ATOM   12880 C CA    . ALA A 1 3101 ? 203.574 180.801 165.226 1.00 4.25  ? 3101 ALA A CA    1 
ATOM   12881 C C     . ALA A 1 3101 ? 203.924 179.560 166.034 1.00 17.22 ? 3101 ALA A C     1 
ATOM   12882 O O     . ALA A 1 3101 ? 204.942 178.907 165.772 1.00 18.01 ? 3101 ALA A O     1 
ATOM   12883 C CB    . ALA A 1 3101 ? 203.940 182.062 166.005 1.00 4.61  ? 3101 ALA A CB    1 
ATOM   12884 N N     . LEU A 1 3102 ? 203.095 179.219 167.023 1.00 19.59 ? 3102 LEU A N     1 
ATOM   12885 C CA    . LEU A 1 3102 ? 203.346 178.024 167.820 1.00 5.70  ? 3102 LEU A CA    1 
ATOM   12886 C C     . LEU A 1 3102 ? 203.281 176.769 166.962 1.00 5.53  ? 3102 LEU A C     1 
ATOM   12887 O O     . LEU A 1 3102 ? 204.109 175.863 167.112 1.00 9.48  ? 3102 LEU A O     1 
ATOM   12888 C CB    . LEU A 1 3102 ? 202.340 177.935 168.964 1.00 1.67  ? 3102 LEU A CB    1 
ATOM   12889 C CG    . LEU A 1 3102 ? 202.459 178.981 170.067 1.00 0.00  ? 3102 LEU A CG    1 
ATOM   12890 C CD1   . LEU A 1 3102 ? 201.299 178.843 171.035 1.00 5.59  ? 3102 LEU A CD1   1 
ATOM   12891 C CD2   . LEU A 1 3102 ? 203.790 178.847 170.783 1.00 3.98  ? 3102 LEU A CD2   1 
ATOM   12892 N N     . TYR A 1 3103 ? 202.301 176.698 166.060 1.00 0.68  ? 3103 TYR A N     1 
ATOM   12893 C CA    . TYR A 1 3103 ? 202.188 175.546 165.174 1.00 5.51  ? 3103 TYR A CA    1 
ATOM   12894 C C     . TYR A 1 3103 ? 203.413 175.422 164.283 1.00 7.60  ? 3103 TYR A C     1 
ATOM   12895 O O     . TYR A 1 3103 ? 203.925 174.319 164.074 1.00 12.28 ? 3103 TYR A O     1 
ATOM   12896 C CB    . TYR A 1 3103 ? 200.919 175.660 164.332 1.00 12.69 ? 3103 TYR A CB    1 
ATOM   12897 C CG    . TYR A 1 3103 ? 200.514 174.384 163.627 1.00 13.30 ? 3103 TYR A CG    1 
ATOM   12898 C CD1   . TYR A 1 3103 ? 199.510 173.575 164.141 1.00 11.79 ? 3103 TYR A CD1   1 
ATOM   12899 C CD2   . TYR A 1 3103 ? 201.129 173.993 162.444 1.00 12.17 ? 3103 TYR A CD2   1 
ATOM   12900 C CE1   . TYR A 1 3103 ? 199.133 172.414 163.501 1.00 11.24 ? 3103 TYR A CE1   1 
ATOM   12901 C CE2   . TYR A 1 3103 ? 200.758 172.832 161.798 1.00 11.49 ? 3103 TYR A CE2   1 
ATOM   12902 C CZ    . TYR A 1 3103 ? 199.760 172.048 162.331 1.00 14.06 ? 3103 TYR A CZ    1 
ATOM   12903 O OH    . TYR A 1 3103 ? 199.386 170.892 161.691 1.00 21.30 ? 3103 TYR A OH    1 
ATOM   12904 N N     . GLN A 1 3104 ? 203.902 176.543 163.751 1.00 5.84  ? 3104 GLN A N     1 
ATOM   12905 C CA    . GLN A 1 3104 ? 205.074 176.492 162.884 1.00 6.04  ? 3104 GLN A CA    1 
ATOM   12906 C C     . GLN A 1 3104 ? 206.319 176.078 163.659 1.00 8.49  ? 3104 GLN A C     1 
ATOM   12907 O O     . GLN A 1 3104 ? 207.124 175.276 163.169 1.00 17.69 ? 3104 GLN A O     1 
ATOM   12908 C CB    . GLN A 1 3104 ? 205.276 177.845 162.205 1.00 9.69  ? 3104 GLN A CB    1 
ATOM   12909 C CG    . GLN A 1 3104 ? 204.294 178.104 161.073 1.00 6.83  ? 3104 GLN A CG    1 
ATOM   12910 C CD    . GLN A 1 3104 ? 204.539 179.423 160.376 1.00 13.11 ? 3104 GLN A CD    1 
ATOM   12911 O OE1   . GLN A 1 3104 ? 203.648 180.267 160.287 1.00 13.99 ? 3104 GLN A OE1   1 
ATOM   12912 N NE2   . GLN A 1 3104 ? 205.753 179.608 159.873 1.00 15.33 ? 3104 GLN A NE2   1 
ATOM   12913 N N     . VAL A 1 3105 ? 206.488 176.602 164.877 1.00 8.69  ? 3105 VAL A N     1 
ATOM   12914 C CA    . VAL A 1 3105 ? 207.636 176.223 165.700 1.00 6.83  ? 3105 VAL A CA    1 
ATOM   12915 C C     . VAL A 1 3105 ? 207.587 174.735 166.023 1.00 8.41  ? 3105 VAL A C     1 
ATOM   12916 O O     . VAL A 1 3105 ? 208.591 174.022 165.910 1.00 9.58  ? 3105 VAL A O     1 
ATOM   12917 C CB    . VAL A 1 3105 ? 207.688 177.070 166.985 1.00 8.00  ? 3105 VAL A CB    1 
ATOM   12918 C CG1   . VAL A 1 3105 ? 208.820 176.599 167.882 1.00 12.73 ? 3105 VAL A CG1   1 
ATOM   12919 C CG2   . VAL A 1 3105 ? 207.858 178.535 166.661 1.00 6.79  ? 3105 VAL A CG2   1 
ATOM   12920 N N     . GLY A 1 3106 ? 206.415 174.244 166.430 1.00 2.26  ? 3106 GLY A N     1 
ATOM   12921 C CA    . GLY A 1 3106 ? 206.284 172.830 166.732 1.00 2.10  ? 3106 GLY A CA    1 
ATOM   12922 C C     . GLY A 1 3106 ? 206.518 171.949 165.521 1.00 11.37 ? 3106 GLY A C     1 
ATOM   12923 O O     . GLY A 1 3106 ? 207.199 170.926 165.609 1.00 20.51 ? 3106 GLY A O     1 
ATOM   12924 N N     . LYS A 1 3107 ? 205.966 172.339 164.370 1.00 9.80  ? 3107 LYS A N     1 
ATOM   12925 C CA    . LYS A 1 3107 ? 206.138 171.550 163.158 1.00 9.73  ? 3107 LYS A CA    1 
ATOM   12926 C C     . LYS A 1 3107 ? 207.600 171.487 162.743 1.00 6.75  ? 3107 LYS A C     1 
ATOM   12927 O O     . LYS A 1 3107 ? 208.088 170.427 162.337 1.00 13.23 ? 3107 LYS A O     1 
ATOM   12928 C CB    . LYS A 1 3107 ? 205.283 172.127 162.031 1.00 12.90 ? 3107 LYS A CB    1 
ATOM   12929 C CG    . LYS A 1 3107 ? 205.321 171.320 160.747 1.00 12.13 ? 3107 LYS A CG    1 
ATOM   12930 C CD    . LYS A 1 3107 ? 204.360 170.146 160.798 1.00 11.21 ? 3107 LYS A CD    1 
ATOM   12931 C CE    . LYS A 1 3107 ? 203.679 169.937 159.457 1.00 11.45 ? 3107 LYS A CE    1 
ATOM   12932 N NZ    . LYS A 1 3107 ? 203.069 168.584 159.347 1.00 17.25 ? 3107 LYS A NZ    1 
ATOM   12933 N N     . GLU A 1 3108 ? 208.319 172.606 162.843 1.00 9.38  ? 3108 GLU A N     1 
ATOM   12934 C CA    . GLU A 1 3108 ? 209.708 172.608 162.401 1.00 12.21 ? 3108 GLU A CA    1 
ATOM   12935 C C     . GLU A 1 3108 ? 210.603 171.872 163.392 1.00 12.11 ? 3108 GLU A C     1 
ATOM   12936 O O     . GLU A 1 3108 ? 211.499 171.120 162.992 1.00 16.83 ? 3108 GLU A O     1 
ATOM   12937 C CB    . GLU A 1 3108 ? 210.202 174.039 162.205 1.00 7.78  ? 3108 GLU A CB    1 
ATOM   12938 C CG    . GLU A 1 3108 ? 211.512 174.120 161.439 1.00 10.33 ? 3108 GLU A CG    1 
ATOM   12939 C CD    . GLU A 1 3108 ? 212.724 174.192 162.343 1.00 17.60 ? 3108 GLU A CD    1 
ATOM   12940 O OE1   . GLU A 1 3108 ? 212.568 174.547 163.528 1.00 22.99 ? 3108 GLU A OE1   1 
ATOM   12941 O OE2   . GLU A 1 3108 ? 213.838 173.892 161.864 1.00 15.84 ? 3108 GLU A OE2   1 
ATOM   12942 N N     . PHE A 1 3109 ? 210.382 172.080 164.692 1.00 8.50  ? 3109 PHE A N     1 
ATOM   12943 C CA    . PHE A 1 3109 ? 211.287 171.508 165.685 1.00 10.04 ? 3109 PHE A CA    1 
ATOM   12944 C C     . PHE A 1 3109 ? 211.035 170.019 165.890 1.00 15.30 ? 3109 PHE A C     1 
ATOM   12945 O O     . PHE A 1 3109 ? 211.971 169.260 166.168 1.00 17.86 ? 3109 PHE A O     1 
ATOM   12946 C CB    . PHE A 1 3109 ? 211.167 172.267 167.004 1.00 11.14 ? 3109 PHE A CB    1 
ATOM   12947 C CG    . PHE A 1 3109 ? 212.020 173.500 167.071 1.00 13.90 ? 3109 PHE A CG    1 
ATOM   12948 C CD1   . PHE A 1 3109 ? 211.560 174.707 166.579 1.00 11.82 ? 3109 PHE A CD1   1 
ATOM   12949 C CD2   . PHE A 1 3109 ? 213.290 173.447 167.617 1.00 12.67 ? 3109 PHE A CD2   1 
ATOM   12950 C CE1   . PHE A 1 3109 ? 212.347 175.840 166.637 1.00 11.97 ? 3109 PHE A CE1   1 
ATOM   12951 C CE2   . PHE A 1 3109 ? 214.080 174.576 167.678 1.00 12.08 ? 3109 PHE A CE2   1 
ATOM   12952 C CZ    . PHE A 1 3109 ? 213.608 175.774 167.187 1.00 11.16 ? 3109 PHE A CZ    1 
ATOM   12953 N N     . THR A 1 3110 ? 209.784 169.578 165.766 1.00 14.65 ? 3110 THR A N     1 
ATOM   12954 C CA    . THR A 1 3110 ? 209.492 168.151 165.822 1.00 7.82  ? 3110 THR A CA    1 
ATOM   12955 C C     . THR A 1 3110 ? 209.610 167.532 164.435 1.00 12.42 ? 3110 THR A C     1 
ATOM   12956 O O     . THR A 1 3110 ? 208.674 166.886 163.954 1.00 21.67 ? 3110 THR A O     1 
ATOM   12957 C CB    . THR A 1 3110 ? 208.098 167.896 166.400 1.00 7.69  ? 3110 THR A CB    1 
ATOM   12958 O OG1   . THR A 1 3110 ? 207.102 168.334 165.468 1.00 16.35 ? 3110 THR A OG1   1 
ATOM   12959 C CG2   . THR A 1 3110 ? 207.920 168.631 167.717 1.00 3.77  ? 3110 THR A CG2   1 
ATOM   12960 N N     . SER A 1 3111 ? 210.757 167.725 163.785 1.00 10.78 ? 3111 SER A N     1 
ATOM   12961 C CA    . SER A 1 3111 ? 210.996 167.186 162.453 1.00 13.43 ? 3111 SER A CA    1 
ATOM   12962 C C     . SER A 1 3111 ? 212.010 166.053 162.440 1.00 15.50 ? 3111 SER A C     1 
ATOM   12963 O O     . SER A 1 3111 ? 211.847 165.102 161.668 1.00 15.87 ? 3111 SER A O     1 
ATOM   12964 C CB    . SER A 1 3111 ? 211.471 168.294 161.509 1.00 11.18 ? 3111 SER A CB    1 
ATOM   12965 O OG    . SER A 1 3111 ? 212.813 168.650 161.784 1.00 15.17 ? 3111 SER A OG    1 
ATOM   12966 N N     . LYS A 1 3112 ? 213.057 166.133 163.265 1.00 13.69 ? 3112 LYS A N     1 
ATOM   12967 C CA    . LYS A 1 3112 ? 213.964 165.000 163.411 1.00 12.32 ? 3112 LYS A CA    1 
ATOM   12968 C C     . LYS A 1 3112 ? 213.244 163.808 164.025 1.00 11.83 ? 3112 LYS A C     1 
ATOM   12969 O O     . LYS A 1 3112 ? 213.619 162.654 163.788 1.00 13.67 ? 3112 LYS A O     1 
ATOM   12970 C CB    . LYS A 1 3112 ? 215.169 165.396 164.262 1.00 12.76 ? 3112 LYS A CB    1 
ATOM   12971 C CG    . LYS A 1 3112 ? 215.781 166.736 163.896 1.00 14.02 ? 3112 LYS A CG    1 
ATOM   12972 C CD    . LYS A 1 3112 ? 216.429 166.690 162.525 1.00 12.27 ? 3112 LYS A CD    1 
ATOM   12973 C CE    . LYS A 1 3112 ? 216.622 168.087 161.960 1.00 15.13 ? 3112 LYS A CE    1 
ATOM   12974 N NZ    . LYS A 1 3112 ? 216.891 169.087 163.031 1.00 16.60 ? 3112 LYS A NZ    1 
ATOM   12975 N N     . MET A 1 3113 ? 212.214 164.071 164.822 1.00 10.89 ? 3113 MET A N     1 
ATOM   12976 C CA    . MET A 1 3113 ? 211.394 163.026 165.407 1.00 10.28 ? 3113 MET A CA    1 
ATOM   12977 C C     . MET A 1 3113 ? 210.627 162.282 164.317 1.00 14.37 ? 3113 MET A C     1 
ATOM   12978 O O     . MET A 1 3113 ? 210.206 162.860 163.313 1.00 15.18 ? 3113 MET A O     1 
ATOM   12979 C CB    . MET A 1 3113 ? 210.421 163.631 166.417 1.00 11.00 ? 3113 MET A CB    1 
ATOM   12980 C CG    . MET A 1 3113 ? 211.087 164.133 167.686 1.00 13.67 ? 3113 MET A CG    1 
ATOM   12981 S SD    . MET A 1 3113 ? 209.921 164.888 168.835 1.00 0.00  ? 3113 MET A SD    1 
ATOM   12982 C CE    . MET A 1 3113 ? 208.559 163.734 168.736 1.00 8.37  ? 3113 MET A CE    1 
ATOM   12983 N N     . ASP A 1 3114 ? 210.454 160.978 164.518 1.00 15.61 ? 3114 ASP A N     1 
ATOM   12984 C CA    . ASP A 1 3114 ? 209.743 160.129 163.562 1.00 15.70 ? 3114 ASP A CA    1 
ATOM   12985 C C     . ASP A 1 3114 ? 208.332 159.848 164.078 1.00 16.85 ? 3114 ASP A C     1 
ATOM   12986 O O     . ASP A 1 3114 ? 208.056 158.814 164.687 1.00 20.19 ? 3114 ASP A O     1 
ATOM   12987 C CB    . ASP A 1 3114 ? 210.546 158.861 163.272 1.00 15.94 ? 3114 ASP A CB    1 
ATOM   12988 C CG    . ASP A 1 3114 ? 210.854 158.052 164.517 1.00 17.15 ? 3114 ASP A CG    1 
ATOM   12989 O OD1   . ASP A 1 3114 ? 210.517 158.502 165.629 1.00 17.83 ? 3114 ASP A OD1   1 
ATOM   12990 O OD2   . ASP A 1 3114 ? 211.439 156.957 164.381 1.00 17.04 ? 3114 ASP A OD2   1 
ATOM   12991 N N     . LEU A 1 3115 ? 207.421 160.779 163.798 1.00 17.14 ? 3115 LEU A N     1 
ATOM   12992 C CA    . LEU A 1 3115 ? 206.030 160.680 164.215 1.00 21.77 ? 3115 LEU A CA    1 
ATOM   12993 C C     . LEU A 1 3115 ? 205.121 160.146 163.117 1.00 27.27 ? 3115 LEU A C     1 
ATOM   12994 O O     . LEU A 1 3115 ? 203.896 160.233 163.246 1.00 27.35 ? 3115 LEU A O     1 
ATOM   12995 C CB    . LEU A 1 3115 ? 205.520 162.044 164.678 1.00 13.73 ? 3115 LEU A CB    1 
ATOM   12996 C CG    . LEU A 1 3115 ? 206.198 162.649 165.901 1.00 17.02 ? 3115 LEU A CG    1 
ATOM   12997 C CD1   . LEU A 1 3115 ? 205.937 164.140 165.940 1.00 16.37 ? 3115 LEU A CD1   1 
ATOM   12998 C CD2   . LEU A 1 3115 ? 205.704 161.976 167.167 1.00 18.77 ? 3115 LEU A CD2   1 
ATOM   12999 N N     . GLU A 1 3116 ? 205.687 159.608 162.042 1.00 23.39 ? 3116 GLU A N     1 
ATOM   13000 C CA    . GLU A 1 3116 ? 204.897 159.120 160.914 1.00 23.54 ? 3116 GLU A CA    1 
ATOM   13001 C C     . GLU A 1 3116 ? 204.327 157.750 161.257 1.00 28.83 ? 3116 GLU A C     1 
ATOM   13002 O O     . GLU A 1 3116 ? 205.048 156.751 161.286 1.00 31.33 ? 3116 GLU A O     1 
ATOM   13003 C CB    . GLU A 1 3116 ? 205.746 159.064 159.649 1.00 27.56 ? 3116 GLU A CB    1 
ATOM   13004 C CG    . GLU A 1 3116 ? 206.554 160.329 159.329 1.00 28.48 ? 3116 GLU A CG    1 
ATOM   13005 C CD    . GLU A 1 3116 ? 205.703 161.548 158.975 1.00 30.30 ? 3116 GLU A CD    1 
ATOM   13006 O OE1   . GLU A 1 3116 ? 206.254 162.483 158.357 1.00 29.49 ? 3116 GLU A OE1   1 
ATOM   13007 O OE2   . GLU A 1 3116 ? 204.494 161.582 159.286 1.00 31.83 ? 3116 GLU A OE2   1 
ATOM   13008 N N     . LYS A 1 3117 ? 203.024 157.704 161.519 1.00 30.78 ? 3117 LYS A N     1 
ATOM   13009 C CA    . LYS A 1 3117 ? 202.306 156.447 161.695 1.00 31.45 ? 3117 LYS A CA    1 
ATOM   13010 C C     . LYS A 1 3117 ? 201.379 156.235 160.509 1.00 33.17 ? 3117 LYS A C     1 
ATOM   13011 O O     . LYS A 1 3117 ? 200.439 157.023 160.318 1.00 32.49 ? 3117 LYS A O     1 
ATOM   13012 C CB    . LYS A 1 3117 ? 201.509 156.446 163.000 1.00 25.02 ? 3117 LYS A CB    1 
ATOM   13013 C CG    . LYS A 1 3117 ? 202.358 156.402 164.256 1.00 27.90 ? 3117 LYS A CG    1 
ATOM   13014 C CD    . LYS A 1 3117 ? 201.492 156.546 165.493 1.00 32.53 ? 3117 LYS A CD    1 
ATOM   13015 C CE    . LYS A 1 3117 ? 200.648 155.302 165.717 1.00 31.11 ? 3117 LYS A CE    1 
ATOM   13016 N NZ    . LYS A 1 3117 ? 199.872 155.367 166.986 1.00 29.02 ? 3117 LYS A NZ    1 
ATOM   13017 N N     . PRO A 1 3118 ? 201.601 155.207 159.684 1.00 31.76 ? 3118 PRO A N     1 
ATOM   13018 C CA    . PRO A 1 3118 ? 200.713 155.001 158.527 1.00 31.63 ? 3118 PRO A CA    1 
ATOM   13019 C C     . PRO A 1 3118 ? 199.262 154.767 158.907 1.00 33.69 ? 3118 PRO A C     1 
ATOM   13020 O O     . PRO A 1 3118 ? 198.359 155.193 158.176 1.00 36.53 ? 3118 PRO A O     1 
ATOM   13021 C CB    . PRO A 1 3118 ? 201.328 153.778 157.833 1.00 33.61 ? 3118 PRO A CB    1 
ATOM   13022 C CG    . PRO A 1 3118 ? 202.089 153.073 158.906 1.00 31.67 ? 3118 PRO A CG    1 
ATOM   13023 C CD    . PRO A 1 3118 ? 202.619 154.152 159.801 1.00 32.64 ? 3118 PRO A CD    1 
ATOM   13024 N N     . ASN A 1 3119 ? 199.007 154.104 160.033 1.00 27.65 ? 3119 ASN A N     1 
ATOM   13025 C CA    . ASN A 1 3119 ? 197.648 153.802 160.480 1.00 26.47 ? 3119 ASN A CA    1 
ATOM   13026 C C     . ASN A 1 3119 ? 197.217 154.857 161.495 1.00 29.65 ? 3119 ASN A C     1 
ATOM   13027 O O     . ASN A 1 3119 ? 197.700 154.883 162.629 1.00 32.95 ? 3119 ASN A O     1 
ATOM   13028 C CB    . ASN A 1 3119 ? 197.568 152.390 161.055 1.00 30.09 ? 3119 ASN A CB    1 
ATOM   13029 C CG    . ASN A 1 3119 ? 198.694 152.084 162.026 1.00 34.29 ? 3119 ASN A CG    1 
ATOM   13030 O OD1   . ASN A 1 3119 ? 199.548 152.927 162.294 1.00 34.61 ? 3119 ASN A OD1   1 
ATOM   13031 N ND2   . ASN A 1 3119 ? 198.697 150.868 162.561 1.00 32.80 ? 3119 ASN A ND2   1 
ATOM   13032 N N     . TYR A 1 3120 ? 196.301 155.729 161.079 1.00 25.58 ? 3120 TYR A N     1 
ATOM   13033 C CA    . TYR A 1 3120 ? 195.789 156.790 161.934 1.00 22.97 ? 3120 TYR A CA    1 
ATOM   13034 C C     . TYR A 1 3120 ? 194.473 157.284 161.353 1.00 25.24 ? 3120 TYR A C     1 
ATOM   13035 O O     . TYR A 1 3120 ? 194.385 157.558 160.154 1.00 29.21 ? 3120 TYR A O     1 
ATOM   13036 C CB    . TYR A 1 3120 ? 196.794 157.942 162.050 1.00 23.87 ? 3120 TYR A CB    1 
ATOM   13037 C CG    . TYR A 1 3120 ? 196.311 159.106 162.882 1.00 26.59 ? 3120 TYR A CG    1 
ATOM   13038 C CD1   . TYR A 1 3120 ? 195.723 158.901 164.122 1.00 25.89 ? 3120 TYR A CD1   1 
ATOM   13039 C CD2   . TYR A 1 3120 ? 196.442 160.411 162.427 1.00 25.71 ? 3120 TYR A CD2   1 
ATOM   13040 C CE1   . TYR A 1 3120 ? 195.281 159.963 164.886 1.00 24.92 ? 3120 TYR A CE1   1 
ATOM   13041 C CE2   . TYR A 1 3120 ? 196.002 161.479 163.184 1.00 24.06 ? 3120 TYR A CE2   1 
ATOM   13042 C CZ    . TYR A 1 3120 ? 195.422 161.248 164.412 1.00 22.48 ? 3120 TYR A CZ    1 
ATOM   13043 O OH    . TYR A 1 3120 ? 194.982 162.306 165.171 1.00 21.21 ? 3120 TYR A OH    1 
ATOM   13044 N N     . ILE A 1 3121 ? 193.454 157.395 162.204 1.00 23.96 ? 3121 ILE A N     1 
ATOM   13045 C CA    . ILE A 1 3121 ? 192.109 157.765 161.778 1.00 25.37 ? 3121 ILE A CA    1 
ATOM   13046 C C     . ILE A 1 3121 ? 191.636 158.955 162.601 1.00 28.03 ? 3121 ILE A C     1 
ATOM   13047 O O     . ILE A 1 3121 ? 191.810 158.978 163.824 1.00 29.84 ? 3121 ILE A O     1 
ATOM   13048 C CB    . ILE A 1 3121 ? 191.124 156.587 161.911 1.00 26.40 ? 3121 ILE A CB    1 
ATOM   13049 C CG1   . ILE A 1 3121 ? 191.291 155.893 163.264 1.00 25.19 ? 3121 ILE A CG1   1 
ATOM   13050 C CG2   . ILE A 1 3121 ? 191.322 155.595 160.775 1.00 25.81 ? 3121 ILE A CG2   1 
ATOM   13051 C CD1   . ILE A 1 3121 ? 190.223 154.861 163.555 1.00 23.75 ? 3121 ILE A CD1   1 
ATOM   13052 N N     . VAL A 1 3122 ? 191.043 159.939 161.931 1.00 27.73 ? 3122 VAL A N     1 
ATOM   13053 C CA    . VAL A 1 3122 ? 190.525 161.135 162.594 1.00 29.64 ? 3122 VAL A CA    1 
ATOM   13054 C C     . VAL A 1 3122 ? 189.000 161.170 162.497 1.00 31.82 ? 3122 VAL A C     1 
ATOM   13055 O O     . VAL A 1 3122 ? 188.440 161.361 161.408 1.00 31.73 ? 3122 VAL A O     1 
ATOM   13056 C CB    . VAL A 1 3122 ? 191.184 162.407 162.029 1.00 30.10 ? 3122 VAL A CB    1 
ATOM   13057 C CG1   . VAL A 1 3122 ? 192.675 162.371 162.296 1.00 28.85 ? 3122 VAL A CG1   1 
ATOM   13058 C CG2   . VAL A 1 3122 ? 190.969 162.530 160.526 1.00 30.89 ? 3122 VAL A CG2   1 
ATOM   13059 N N     . PRO A 1 3123 ? 188.287 160.943 163.602 1.00 39.38 ? 3123 PRO A N     1 
ATOM   13060 C CA    . PRO A 1 3123 ? 186.820 160.952 163.551 1.00 39.80 ? 3123 PRO A CA    1 
ATOM   13061 C C     . PRO A 1 3123 ? 186.195 162.302 163.876 1.00 38.85 ? 3123 PRO A C     1 
ATOM   13062 O O     . PRO A 1 3123 ? 185.029 162.539 163.546 1.00 41.19 ? 3123 PRO A O     1 
ATOM   13063 C CB    . PRO A 1 3123 ? 186.443 159.899 164.598 1.00 38.53 ? 3123 PRO A CB    1 
ATOM   13064 C CG    . PRO A 1 3123 ? 187.539 159.994 165.619 1.00 38.64 ? 3123 PRO A CG    1 
ATOM   13065 C CD    . PRO A 1 3123 ? 188.785 160.517 164.920 1.00 37.84 ? 3123 PRO A CD    1 
ATOM   13066 N N     . ASP A 1 3124 ? 186.949 163.192 164.519 1.00 43.78 ? 3124 ASP A N     1 
ATOM   13067 C CA    . ASP A 1 3124 ? 186.415 164.450 165.023 1.00 46.22 ? 3124 ASP A CA    1 
ATOM   13068 C C     . ASP A 1 3124 ? 187.209 165.606 164.417 1.00 49.06 ? 3124 ASP A C     1 
ATOM   13069 O O     . ASP A 1 3124 ? 188.082 165.408 163.567 1.00 49.63 ? 3124 ASP A O     1 
ATOM   13070 C CB    . ASP A 1 3124 ? 186.449 164.483 166.558 1.00 45.37 ? 3124 ASP A CB    1 
ATOM   13071 C CG    . ASP A 1 3124 ? 185.479 165.495 167.143 1.00 45.69 ? 3124 ASP A CG    1 
ATOM   13072 O OD1   . ASP A 1 3124 ? 184.543 165.904 166.425 1.00 44.11 ? 3124 ASP A OD1   1 
ATOM   13073 O OD2   . ASP A 1 3124 ? 185.653 165.883 168.318 1.00 44.70 ? 3124 ASP A OD2   1 
ATOM   13074 N N     . TYR A 1 3125 ? 186.898 166.826 164.851 1.00 47.98 ? 3125 TYR A N     1 
ATOM   13075 C CA    . TYR A 1 3125 ? 187.449 168.050 164.268 1.00 48.12 ? 3125 TYR A CA    1 
ATOM   13076 C C     . TYR A 1 3125 ? 187.850 168.976 165.412 1.00 48.83 ? 3125 TYR A C     1 
ATOM   13077 O O     . TYR A 1 3125 ? 186.994 169.628 166.013 1.00 50.71 ? 3125 TYR A O     1 
ATOM   13078 C CB    . TYR A 1 3125 ? 186.421 168.714 163.361 1.00 46.08 ? 3125 TYR A CB    1 
ATOM   13079 C CG    . TYR A 1 3125 ? 185.912 167.803 162.276 1.00 47.96 ? 3125 TYR A CG    1 
ATOM   13080 C CD1   . TYR A 1 3125 ? 186.673 167.541 161.149 1.00 49.60 ? 3125 TYR A CD1   1 
ATOM   13081 C CD2   . TYR A 1 3125 ? 184.670 167.192 162.389 1.00 50.04 ? 3125 TYR A CD2   1 
ATOM   13082 C CE1   . TYR A 1 3125 ? 186.211 166.702 160.159 1.00 52.19 ? 3125 TYR A CE1   1 
ATOM   13083 C CE2   . TYR A 1 3125 ? 184.198 166.351 161.405 1.00 51.60 ? 3125 TYR A CE2   1 
ATOM   13084 C CZ    . TYR A 1 3125 ? 184.973 166.109 160.291 1.00 52.38 ? 3125 TYR A CZ    1 
ATOM   13085 O OH    . TYR A 1 3125 ? 184.508 165.270 159.305 1.00 49.59 ? 3125 TYR A OH    1 
ATOM   13086 N N     . MET A 1 3126 ? 189.146 169.037 165.726 1.00 43.66 ? 3126 MET A N     1 
ATOM   13087 C CA    . MET A 1 3126 ? 189.631 169.832 166.853 1.00 40.37 ? 3126 MET A CA    1 
ATOM   13088 C C     . MET A 1 3126 ? 190.885 170.619 166.475 1.00 39.56 ? 3126 MET A C     1 
ATOM   13089 O O     . MET A 1 3126 ? 191.953 170.449 167.083 1.00 41.74 ? 3126 MET A O     1 
ATOM   13090 C CB    . MET A 1 3126 ? 189.857 168.909 168.046 1.00 37.92 ? 3126 MET A CB    1 
ATOM   13091 C CG    . MET A 1 3126 ? 190.939 167.877 167.843 1.00 37.81 ? 3126 MET A CG    1 
ATOM   13092 S SD    . MET A 1 3126 ? 190.975 166.820 169.274 1.00 46.61 ? 3126 MET A SD    1 
ATOM   13093 C CE    . MET A 1 3126 ? 189.478 165.909 168.929 1.00 42.89 ? 3126 MET A CE    1 
ATOM   13094 N N     . PRO A 1 3127 ? 190.786 171.531 165.515 1.00 37.62 ? 3127 PRO A N     1 
ATOM   13095 C CA    . PRO A 1 3127 ? 191.955 172.325 165.141 1.00 34.76 ? 3127 PRO A CA    1 
ATOM   13096 C C     . PRO A 1 3127 ? 192.179 173.468 166.121 1.00 34.58 ? 3127 PRO A C     1 
ATOM   13097 O O     . PRO A 1 3127 ? 191.287 173.867 166.871 1.00 35.54 ? 3127 PRO A O     1 
ATOM   13098 C CB    . PRO A 1 3127 ? 191.577 172.844 163.748 1.00 33.55 ? 3127 PRO A CB    1 
ATOM   13099 C CG    . PRO A 1 3127 ? 190.097 173.029 163.835 1.00 36.64 ? 3127 PRO A CG    1 
ATOM   13100 C CD    . PRO A 1 3127 ? 189.579 171.964 164.786 1.00 38.64 ? 3127 PRO A CD    1 
ATOM   13101 N N     . VAL A 1 3128 ? 193.417 173.959 166.139 1.00 27.88 ? 3128 VAL A N     1 
ATOM   13102 C CA    . VAL A 1 3128 ? 193.739 175.167 166.892 1.00 26.72 ? 3128 VAL A CA    1 
ATOM   13103 C C     . VAL A 1 3128 ? 194.294 176.200 165.921 1.00 26.16 ? 3128 VAL A C     1 
ATOM   13104 O O     . VAL A 1 3128 ? 194.022 177.398 166.047 1.00 26.37 ? 3128 VAL A O     1 
ATOM   13105 C CB    . VAL A 1 3128 ? 194.712 174.889 168.058 1.00 25.60 ? 3128 VAL A CB    1 
ATOM   13106 C CG1   . VAL A 1 3128 ? 194.087 173.916 169.052 1.00 21.54 ? 3128 VAL A CG1   1 
ATOM   13107 C CG2   . VAL A 1 3128 ? 196.059 174.377 167.566 1.00 23.49 ? 3128 VAL A CG2   1 
ATOM   13108 N N     . VAL A 1 3129 ? 195.087 175.739 164.950 1.00 26.16 ? 3129 VAL A N     1 
ATOM   13109 C CA    . VAL A 1 3129 ? 195.649 176.638 163.948 1.00 28.18 ? 3129 VAL A CA    1 
ATOM   13110 C C     . VAL A 1 3129 ? 194.567 177.122 162.984 1.00 33.62 ? 3129 VAL A C     1 
ATOM   13111 O O     . VAL A 1 3129 ? 194.579 178.281 162.551 1.00 34.43 ? 3129 VAL A O     1 
ATOM   13112 C CB    . VAL A 1 3129 ? 196.818 175.942 163.224 1.00 24.43 ? 3129 VAL A CB    1 
ATOM   13113 C CG1   . VAL A 1 3129 ? 196.367 174.632 162.600 1.00 29.97 ? 3129 VAL A CG1   1 
ATOM   13114 C CG2   . VAL A 1 3129 ? 197.434 176.856 162.186 1.00 20.85 ? 3129 VAL A CG2   1 
ATOM   13115 N N     . TYR A 1 3130 ? 193.638 176.236 162.609 1.00 35.45 ? 3130 TYR A N     1 
ATOM   13116 C CA    . TYR A 1 3130 ? 192.448 176.550 161.818 1.00 34.05 ? 3130 TYR A CA    1 
ATOM   13117 C C     . TYR A 1 3130 ? 192.703 176.880 160.351 1.00 34.74 ? 3130 TYR A C     1 
ATOM   13118 O O     . TYR A 1 3130 ? 191.741 177.008 159.586 1.00 40.52 ? 3130 TYR A O     1 
ATOM   13119 C CB    . TYR A 1 3130 ? 191.661 177.719 162.429 1.00 31.84 ? 3130 TYR A CB    1 
ATOM   13120 C CG    . TYR A 1 3130 ? 191.197 177.533 163.852 1.00 35.55 ? 3130 TYR A CG    1 
ATOM   13121 C CD1   . TYR A 1 3130 ? 190.506 176.392 164.231 1.00 34.82 ? 3130 TYR A CD1   1 
ATOM   13122 C CD2   . TYR A 1 3130 ? 191.419 178.512 164.809 1.00 34.48 ? 3130 TYR A CD2   1 
ATOM   13123 C CE1   . TYR A 1 3130 ? 190.062 176.223 165.526 1.00 32.54 ? 3130 TYR A CE1   1 
ATOM   13124 C CE2   . TYR A 1 3130 ? 190.983 178.349 166.111 1.00 35.90 ? 3130 TYR A CE2   1 
ATOM   13125 C CZ    . TYR A 1 3130 ? 190.306 177.201 166.464 1.00 36.31 ? 3130 TYR A CZ    1 
ATOM   13126 O OH    . TYR A 1 3130 ? 189.868 177.033 167.757 1.00 35.71 ? 3130 TYR A OH    1 
ATOM   13127 N N     . ASP A 1 3131 ? 193.950 177.016 159.924 1.00 33.40 ? 3131 ASP A N     1 
ATOM   13128 C CA    . ASP A 1 3131 ? 194.024 177.524 158.555 1.00 41.11 ? 3131 ASP A CA    1 
ATOM   13129 C C     . ASP A 1 3131 ? 194.841 176.662 157.605 1.00 42.08 ? 3131 ASP A C     1 
ATOM   13130 O O     . ASP A 1 3131 ? 194.435 176.487 156.453 1.00 42.98 ? 3131 ASP A O     1 
ATOM   13131 C CB    . ASP A 1 3131 ? 194.571 178.965 158.543 1.00 38.55 ? 3131 ASP A CB    1 
ATOM   13132 C CG    . ASP A 1 3131 ? 196.011 179.049 158.987 1.00 40.03 ? 3131 ASP A CG    1 
ATOM   13133 O OD1   . ASP A 1 3131 ? 196.260 178.952 160.205 1.00 39.93 ? 3131 ASP A OD1   1 
ATOM   13134 O OD2   . ASP A 1 3131 ? 196.894 179.207 158.119 1.00 38.52 ? 3131 ASP A OD2   1 
ATOM   13135 N N     . LYS A 1 3132 ? 195.973 176.119 158.043 1.00 38.47 ? 3132 LYS A N     1 
ATOM   13136 C CA    . LYS A 1 3132 ? 196.875 175.409 157.144 1.00 39.59 ? 3132 LYS A CA    1 
ATOM   13137 C C     . LYS A 1 3132 ? 196.825 173.912 157.424 1.00 39.58 ? 3132 LYS A C     1 
ATOM   13138 O O     . LYS A 1 3132 ? 196.923 173.482 158.579 1.00 33.50 ? 3132 LYS A O     1 
ATOM   13139 C CB    . LYS A 1 3132 ? 198.300 175.956 157.244 1.00 36.14 ? 3132 LYS A CB    1 
ATOM   13140 C CG    . LYS A 1 3132 ? 198.971 175.838 158.596 1.00 40.88 ? 3132 LYS A CG    1 
ATOM   13141 C CD    . LYS A 1 3132 ? 200.358 176.461 158.541 1.00 35.46 ? 3132 LYS A CD    1 
ATOM   13142 C CE    . LYS A 1 3132 ? 201.063 176.372 159.876 1.00 34.31 ? 3132 LYS A CE    1 
ATOM   13143 N NZ    . LYS A 1 3132 ? 200.398 177.235 160.886 1.00 31.91 ? 3132 LYS A NZ    1 
ATOM   13144 N N     . LEU A 1 3133 ? 196.654 173.136 156.357 1.00 42.59 ? 3133 LEU A N     1 
ATOM   13145 C CA    . LEU A 1 3133 ? 196.546 171.682 156.416 1.00 42.39 ? 3133 LEU A CA    1 
ATOM   13146 C C     . LEU A 1 3133 ? 195.462 171.181 157.376 1.00 41.61 ? 3133 LEU A C     1 
ATOM   13147 O O     . LEU A 1 3133 ? 195.758 170.445 158.323 1.00 38.96 ? 3133 LEU A O     1 
ATOM   13148 C CB    . LEU A 1 3133 ? 197.896 171.070 156.762 1.00 41.05 ? 3133 LEU A CB    1 
ATOM   13149 C CG    . LEU A 1 3133 ? 198.934 170.995 155.630 1.00 41.97 ? 3133 LEU A CG    1 
ATOM   13150 C CD1   . LEU A 1 3133 ? 199.495 172.366 155.266 1.00 40.80 ? 3133 LEU A CD1   1 
ATOM   13151 C CD2   . LEU A 1 3133 ? 200.069 170.054 155.988 1.00 39.08 ? 3133 LEU A CD2   1 
ATOM   13152 N N     . PRO A 1 3134 ? 194.195 171.556 157.162 1.00 48.42 ? 3134 PRO A N     1 
ATOM   13153 C CA    . PRO A 1 3134 ? 193.106 170.958 157.945 1.00 46.40 ? 3134 PRO A CA    1 
ATOM   13154 C C     . PRO A 1 3134 ? 192.720 169.557 157.497 1.00 44.72 ? 3134 PRO A C     1 
ATOM   13155 O O     . PRO A 1 3134 ? 191.907 168.914 158.170 1.00 42.99 ? 3134 PRO A O     1 
ATOM   13156 C CB    . PRO A 1 3134 ? 191.938 171.934 157.716 1.00 46.24 ? 3134 PRO A CB    1 
ATOM   13157 C CG    . PRO A 1 3134 ? 192.564 173.193 157.229 1.00 45.13 ? 3134 PRO A CG    1 
ATOM   13158 C CD    . PRO A 1 3134 ? 193.713 172.721 156.400 1.00 45.11 ? 3134 PRO A CD    1 
ATOM   13159 N N     . GLN A 1 3135 ? 193.273 169.077 156.386 1.00 39.25 ? 3135 GLN A N     1 
ATOM   13160 C CA    . GLN A 1 3135 ? 192.930 167.767 155.864 1.00 38.69 ? 3135 GLN A CA    1 
ATOM   13161 C C     . GLN A 1 3135 ? 193.416 166.681 156.822 1.00 38.63 ? 3135 GLN A C     1 
ATOM   13162 O O     . GLN A 1 3135 ? 194.257 166.943 157.685 1.00 36.67 ? 3135 GLN A O     1 
ATOM   13163 C CB    . GLN A 1 3135 ? 193.541 167.585 154.474 1.00 41.63 ? 3135 GLN A CB    1 
ATOM   13164 C CG    . GLN A 1 3135 ? 195.059 167.686 154.426 1.00 40.85 ? 3135 GLN A CG    1 
ATOM   13165 C CD    . GLN A 1 3135 ? 195.738 166.345 154.623 1.00 41.24 ? 3135 GLN A CD    1 
ATOM   13166 O OE1   . GLN A 1 3135 ? 195.182 165.301 154.282 1.00 40.94 ? 3135 GLN A OE1   1 
ATOM   13167 N NE2   . GLN A 1 3135 ? 196.943 166.366 155.179 1.00 40.37 ? 3135 GLN A NE2   1 
ATOM   13168 N N     . PRO A 1 3136 ? 192.866 165.469 156.718 1.00 39.22 ? 3136 PRO A N     1 
ATOM   13169 C CA    . PRO A 1 3136 ? 193.288 164.371 157.604 1.00 41.48 ? 3136 PRO A CA    1 
ATOM   13170 C C     . PRO A 1 3136 ? 194.800 164.281 157.701 1.00 40.52 ? 3136 PRO A C     1 
ATOM   13171 O O     . PRO A 1 3136 ? 195.487 164.000 156.707 1.00 36.21 ? 3136 PRO A O     1 
ATOM   13172 C CB    . PRO A 1 3136 ? 192.697 163.126 156.929 1.00 38.16 ? 3136 PRO A CB    1 
ATOM   13173 C CG    . PRO A 1 3136 ? 191.521 163.626 156.165 1.00 37.18 ? 3136 PRO A CG    1 
ATOM   13174 C CD    . PRO A 1 3136 ? 191.703 165.097 155.892 1.00 36.69 ? 3136 PRO A CD    1 
ATOM   13175 N N     . PRO A 1 3137 ? 195.352 164.506 158.888 1.00 35.48 ? 3137 PRO A N     1 
ATOM   13176 C CA    . PRO A 1 3137 ? 196.805 164.617 159.037 1.00 29.55 ? 3137 PRO A CA    1 
ATOM   13177 C C     . PRO A 1 3137 ? 197.501 163.265 158.951 1.00 34.76 ? 3137 PRO A C     1 
ATOM   13178 O O     . PRO A 1 3137 ? 196.879 162.210 158.819 1.00 40.74 ? 3137 PRO A O     1 
ATOM   13179 C CB    . PRO A 1 3137 ? 196.972 165.225 160.436 1.00 24.55 ? 3137 PRO A CB    1 
ATOM   13180 C CG    . PRO A 1 3137 ? 195.603 165.711 160.833 1.00 26.81 ? 3137 PRO A CG    1 
ATOM   13181 C CD    . PRO A 1 3137 ? 194.651 164.800 160.146 1.00 30.31 ? 3137 PRO A CD    1 
ATOM   13182 N N     . SER A 1 3138 ? 198.831 163.325 159.026 1.00 29.60 ? 3138 SER A N     1 
ATOM   13183 C CA    . SER A 1 3138 ? 199.681 162.146 159.119 1.00 34.41 ? 3138 SER A CA    1 
ATOM   13184 C C     . SER A 1 3138 ? 200.131 161.887 160.552 1.00 32.41 ? 3138 SER A C     1 
ATOM   13185 O O     . SER A 1 3138 ? 201.193 161.292 160.773 1.00 33.65 ? 3138 SER A O     1 
ATOM   13186 C CB    . SER A 1 3138 ? 200.891 162.290 158.197 1.00 31.57 ? 3138 SER A CB    1 
ATOM   13187 O OG    . SER A 1 3138 ? 201.655 163.435 158.533 1.00 31.37 ? 3138 SER A OG    1 
ATOM   13188 N N     . HIS A 1 3139 ? 199.350 162.369 161.523 1.00 21.79 ? 3139 HIS A N     1 
ATOM   13189 C CA    . HIS A 1 3139 ? 199.576 162.237 162.960 1.00 21.77 ? 3139 HIS A CA    1 
ATOM   13190 C C     . HIS A 1 3139 ? 200.712 163.140 163.431 1.00 21.19 ? 3139 HIS A C     1 
ATOM   13191 O O     . HIS A 1 3139 ? 200.825 163.429 164.626 1.00 27.33 ? 3139 HIS A O     1 
ATOM   13192 C CB    . HIS A 1 3139 ? 199.855 160.774 163.324 1.00 20.33 ? 3139 HIS A CB    1 
ATOM   13193 C CG    . HIS A 1 3139 ? 200.134 160.546 164.775 1.00 18.64 ? 3139 HIS A CG    1 
ATOM   13194 N ND1   . HIS A 1 3139 ? 201.356 160.106 165.235 1.00 14.37 ? 3139 HIS A ND1   1 
ATOM   13195 C CD2   . HIS A 1 3139 ? 199.349 160.686 165.869 1.00 20.71 ? 3139 HIS A CD2   1 
ATOM   13196 C CE1   . HIS A 1 3139 ? 201.314 159.991 166.550 1.00 18.72 ? 3139 HIS A CE1   1 
ATOM   13197 N NE2   . HIS A 1 3139 ? 200.107 160.336 166.959 1.00 21.20 ? 3139 HIS A NE2   1 
ATOM   13198 N N     . ARG A 1 3140 ? 201.483 163.690 162.493 1.00 16.98 ? 3140 ARG A N     1 
ATOM   13199 C CA    . ARG A 1 3140 ? 202.499 164.674 162.853 1.00 14.11 ? 3140 ARG A CA    1 
ATOM   13200 C C     . ARG A 1 3140 ? 201.873 166.048 163.020 1.00 13.64 ? 3140 ARG A C     1 
ATOM   13201 O O     . ARG A 1 3140 ? 202.175 166.770 163.982 1.00 16.64 ? 3140 ARG A O     1 
ATOM   13202 C CB    . ARG A 1 3140 ? 203.591 164.712 161.787 1.00 16.87 ? 3140 ARG A CB    1 
ATOM   13203 C CG    . ARG A 1 3140 ? 204.367 166.013 161.744 1.00 15.81 ? 3140 ARG A CG    1 
ATOM   13204 C CD    . ARG A 1 3140 ? 205.731 165.797 161.132 1.00 15.59 ? 3140 ARG A CD    1 
ATOM   13205 N NE    . ARG A 1 3140 ? 206.496 164.811 161.881 1.00 19.81 ? 3140 ARG A NE    1 
ATOM   13206 C CZ    . ARG A 1 3140 ? 207.777 164.544 161.677 1.00 16.15 ? 3140 ARG A CZ    1 
ATOM   13207 N NH1   . ARG A 1 3140 ? 208.477 165.180 160.753 1.00 20.22 ? 3140 ARG A NH1   1 
ATOM   13208 N NH2   . ARG A 1 3140 ? 208.370 163.614 162.417 1.00 15.62 ? 3140 ARG A NH2   1 
ATOM   13209 N N     . GLU A 1 3141 ? 200.991 166.413 162.090 1.00 19.47 ? 3141 GLU A N     1 
ATOM   13210 C CA    . GLU A 1 3141 ? 200.182 167.608 162.264 1.00 18.46 ? 3141 GLU A CA    1 
ATOM   13211 C C     . GLU A 1 3141 ? 199.360 167.506 163.537 1.00 17.70 ? 3141 GLU A C     1 
ATOM   13212 O O     . GLU A 1 3141 ? 199.180 168.496 164.249 1.00 18.78 ? 3141 GLU A O     1 
ATOM   13213 C CB    . GLU A 1 3141 ? 199.270 167.795 161.053 1.00 19.40 ? 3141 GLU A CB    1 
ATOM   13214 C CG    . GLU A 1 3141 ? 199.979 167.648 159.720 1.00 21.33 ? 3141 GLU A CG    1 
ATOM   13215 C CD    . GLU A 1 3141 ? 199.018 167.596 158.552 1.00 27.61 ? 3141 GLU A CD    1 
ATOM   13216 O OE1   . GLU A 1 3141 ? 197.798 167.739 158.774 1.00 30.63 ? 3141 GLU A OE1   1 
ATOM   13217 O OE2   . GLU A 1 3141 ? 199.477 167.369 157.415 1.00 29.85 ? 3141 GLU A OE2   1 
ATOM   13218 N N     . ALA A 1 3142 ? 198.862 166.305 163.845 1.00 10.79 ? 3142 ALA A N     1 
ATOM   13219 C CA    . ALA A 1 3142 ? 198.108 166.100 165.077 1.00 9.38  ? 3142 ALA A CA    1 
ATOM   13220 C C     . ALA A 1 3142 ? 198.986 166.293 166.308 1.00 12.34 ? 3142 ALA A C     1 
ATOM   13221 O O     . ALA A 1 3142 ? 198.553 166.901 167.293 1.00 14.89 ? 3142 ALA A O     1 
ATOM   13222 C CB    . ALA A 1 3142 ? 197.477 164.709 165.078 1.00 15.15 ? 3142 ALA A CB    1 
ATOM   13223 N N     . ILE A 1 3143 ? 200.222 165.789 166.273 1.00 12.18 ? 3143 ILE A N     1 
ATOM   13224 C CA    . ILE A 1 3143 ? 201.126 165.976 167.408 1.00 7.87  ? 3143 ILE A CA    1 
ATOM   13225 C C     . ILE A 1 3143 ? 201.408 167.457 167.630 1.00 5.69  ? 3143 ILE A C     1 
ATOM   13226 O O     . ILE A 1 3143 ? 201.355 167.957 168.761 1.00 10.00 ? 3143 ILE A O     1 
ATOM   13227 C CB    . ILE A 1 3143 ? 202.428 165.182 167.199 1.00 9.27  ? 3143 ILE A CB    1 
ATOM   13228 C CG1   . ILE A 1 3143 ? 202.187 163.687 167.408 1.00 8.99  ? 3143 ILE A CG1   1 
ATOM   13229 C CG2   . ILE A 1 3143 ? 203.510 165.681 168.137 1.00 10.58 ? 3143 ILE A CG2   1 
ATOM   13230 C CD1   . ILE A 1 3143 ? 201.915 163.311 168.841 1.00 10.50 ? 3143 ILE A CD1   1 
ATOM   13231 N N     . VAL A 1 3144 ? 201.712 168.184 166.553 1.00 5.48  ? 3144 VAL A N     1 
ATOM   13232 C CA    . VAL A 1 3144 ? 202.024 169.606 166.697 1.00 6.34  ? 3144 VAL A CA    1 
ATOM   13233 C C     . VAL A 1 3144 ? 200.788 170.387 167.138 1.00 6.96  ? 3144 VAL A C     1 
ATOM   13234 O O     . VAL A 1 3144 ? 200.878 171.321 167.946 1.00 13.48 ? 3144 VAL A O     1 
ATOM   13235 C CB    . VAL A 1 3144 ? 202.617 170.159 165.390 1.00 6.86  ? 3144 VAL A CB    1 
ATOM   13236 C CG1   . VAL A 1 3144 ? 202.989 171.614 165.562 1.00 5.48  ? 3144 VAL A CG1   1 
ATOM   13237 C CG2   . VAL A 1 3144 ? 203.835 169.351 164.988 1.00 4.96  ? 3144 VAL A CG2   1 
ATOM   13238 N N     . ASN A 1 3145 ? 199.618 170.017 166.615 1.00 10.43 ? 3145 ASN A N     1 
ATOM   13239 C CA    . ASN A 1 3145 ? 198.368 170.630 167.045 1.00 8.50  ? 3145 ASN A CA    1 
ATOM   13240 C C     . ASN A 1 3145 ? 198.147 170.423 168.537 1.00 5.73  ? 3145 ASN A C     1 
ATOM   13241 O O     . ASN A 1 3145 ? 197.730 171.343 169.248 1.00 5.66  ? 3145 ASN A O     1 
ATOM   13242 C CB    . ASN A 1 3145 ? 197.216 170.036 166.231 1.00 10.87 ? 3145 ASN A CB    1 
ATOM   13243 C CG    . ASN A 1 3145 ? 195.861 170.510 166.694 1.00 14.26 ? 3145 ASN A CG    1 
ATOM   13244 O OD1   . ASN A 1 3145 ? 195.433 171.612 166.363 1.00 17.81 ? 3145 ASN A OD1   1 
ATOM   13245 N ND2   . ASN A 1 3145 ? 195.169 169.673 167.457 1.00 14.29 ? 3145 ASN A ND2   1 
ATOM   13246 N N     . SER A 1 3146 ? 198.438 169.219 169.030 1.00 4.26  ? 3146 SER A N     1 
ATOM   13247 C CA    . SER A 1 3146 ? 198.304 168.943 170.455 1.00 5.66  ? 3146 SER A CA    1 
ATOM   13248 C C     . SER A 1 3146 ? 199.309 169.741 171.279 1.00 8.20  ? 3146 SER A C     1 
ATOM   13249 O O     . SER A 1 3146 ? 198.998 170.174 172.392 1.00 12.41 ? 3146 SER A O     1 
ATOM   13250 C CB    . SER A 1 3146 ? 198.463 167.448 170.703 1.00 5.33  ? 3146 SER A CB    1 
ATOM   13251 O OG    . SER A 1 3146 ? 199.831 167.115 170.796 1.00 8.33  ? 3146 SER A OG    1 
ATOM   13252 N N     . CYS A 1 3147 ? 200.523 169.934 170.760 1.00 5.95  ? 3147 CYS A N     1 
ATOM   13253 C CA    . CYS A 1 3147 ? 201.510 170.752 171.469 1.00 1.12  ? 3147 CYS A CA    1 
ATOM   13254 C C     . CYS A 1 3147 ? 201.027 172.194 171.612 1.00 3.46  ? 3147 CYS A C     1 
ATOM   13255 O O     . CYS A 1 3147 ? 201.093 172.797 172.699 1.00 13.72 ? 3147 CYS A O     1 
ATOM   13256 C CB    . CYS A 1 3147 ? 202.845 170.712 170.726 1.00 4.47  ? 3147 CYS A CB    1 
ATOM   13257 S SG    . CYS A 1 3147 ? 203.722 169.139 170.798 1.00 0.00  ? 3147 CYS A SG    1 
ATOM   13258 N N     . VAL A 1 3148 ? 200.534 172.765 170.511 1.00 3.33  ? 3148 VAL A N     1 
ATOM   13259 C CA    . VAL A 1 3148 ? 199.977 174.110 170.572 1.00 1.65  ? 3148 VAL A CA    1 
ATOM   13260 C C     . VAL A 1 3148 ? 198.789 174.153 171.518 1.00 7.35  ? 3148 VAL A C     1 
ATOM   13261 O O     . VAL A 1 3148 ? 198.601 175.137 172.243 1.00 10.07 ? 3148 VAL A O     1 
ATOM   13262 C CB    . VAL A 1 3148 ? 199.595 174.602 169.166 1.00 0.81  ? 3148 VAL A CB    1 
ATOM   13263 C CG1   . VAL A 1 3148 ? 199.228 176.067 169.213 1.00 6.63  ? 3148 VAL A CG1   1 
ATOM   13264 C CG2   . VAL A 1 3148 ? 200.747 174.395 168.218 1.00 6.93  ? 3148 VAL A CG2   1 
ATOM   13265 N N     . PHE A 1 3149 ? 197.970 173.099 171.535 1.00 4.80  ? 3149 PHE A N     1 
ATOM   13266 C CA    . PHE A 1 3149 ? 196.853 173.066 172.468 1.00 0.98  ? 3149 PHE A CA    1 
ATOM   13267 C C     . PHE A 1 3149 ? 197.343 173.028 173.906 1.00 1.69  ? 3149 PHE A C     1 
ATOM   13268 O O     . PHE A 1 3149 ? 196.695 173.577 174.796 1.00 13.09 ? 3149 PHE A O     1 
ATOM   13269 C CB    . PHE A 1 3149 ? 195.942 171.872 172.185 1.00 7.99  ? 3149 PHE A CB    1 
ATOM   13270 C CG    . PHE A 1 3149 ? 195.004 171.551 173.317 1.00 9.81  ? 3149 PHE A CG    1 
ATOM   13271 C CD1   . PHE A 1 3149 ? 193.755 172.138 173.379 1.00 10.25 ? 3149 PHE A CD1   1 
ATOM   13272 C CD2   . PHE A 1 3149 ? 195.366 170.657 174.311 1.00 6.33  ? 3149 PHE A CD2   1 
ATOM   13273 C CE1   . PHE A 1 3149 ? 192.891 171.853 174.413 1.00 8.14  ? 3149 PHE A CE1   1 
ATOM   13274 C CE2   . PHE A 1 3149 ? 194.510 170.372 175.348 1.00 6.91  ? 3149 PHE A CE2   1 
ATOM   13275 C CZ    . PHE A 1 3149 ? 193.266 170.964 175.395 1.00 7.30  ? 3149 PHE A CZ    1 
ATOM   13276 N N     . VAL A 1 3150 ? 198.465 172.355 174.162 1.00 3.19  ? 3150 VAL A N     1 
ATOM   13277 C CA    . VAL A 1 3150 ? 199.029 172.348 175.510 1.00 4.25  ? 3150 VAL A CA    1 
ATOM   13278 C C     . VAL A 1 3150 ? 199.397 173.764 175.932 1.00 5.60  ? 3150 VAL A C     1 
ATOM   13279 O O     . VAL A 1 3150 ? 199.087 174.200 177.051 1.00 12.15 ? 3150 VAL A O     1 
ATOM   13280 C CB    . VAL A 1 3150 ? 200.241 171.400 175.586 1.00 0.43  ? 3150 VAL A CB    1 
ATOM   13281 C CG1   . VAL A 1 3150 ? 200.966 171.568 176.907 1.00 0.00  ? 3150 VAL A CG1   1 
ATOM   13282 C CG2   . VAL A 1 3150 ? 199.796 169.960 175.424 1.00 4.89  ? 3150 VAL A CG2   1 
ATOM   13283 N N     . HIS A 1 3151 ? 200.048 174.509 175.037 1.00 5.39  ? 3151 HIS A N     1 
ATOM   13284 C CA    . HIS A 1 3151 ? 200.371 175.903 175.349 1.00 0.00  ? 3151 HIS A CA    1 
ATOM   13285 C C     . HIS A 1 3151 ? 199.108 176.726 175.609 1.00 3.12  ? 3151 HIS A C     1 
ATOM   13286 O O     . HIS A 1 3151 ? 199.015 177.453 176.611 1.00 2.67  ? 3151 HIS A O     1 
ATOM   13287 C CB    . HIS A 1 3151 ? 201.197 176.518 174.221 1.00 0.00  ? 3151 HIS A CB    1 
ATOM   13288 C CG    . HIS A 1 3151 ? 202.082 177.641 174.666 1.00 5.93  ? 3151 HIS A CG    1 
ATOM   13289 N ND1   . HIS A 1 3151 ? 203.442 177.497 174.836 1.00 6.55  ? 3151 HIS A ND1   1 
ATOM   13290 C CD2   . HIS A 1 3151 ? 201.801 178.930 174.967 1.00 6.65  ? 3151 HIS A CD2   1 
ATOM   13291 C CE1   . HIS A 1 3151 ? 203.959 178.647 175.229 1.00 1.93  ? 3151 HIS A CE1   1 
ATOM   13292 N NE2   . HIS A 1 3151 ? 202.985 179.534 175.313 1.00 0.11  ? 3151 HIS A NE2   1 
ATOM   13293 N N     . GLN A 1 3152 ? 198.113 176.611 174.723 1.00 9.85  ? 3152 GLN A N     1 
ATOM   13294 C CA    . GLN A 1 3152 ? 196.867 177.350 174.920 1.00 8.74  ? 3152 GLN A CA    1 
ATOM   13295 C C     . GLN A 1 3152 ? 196.186 176.964 176.225 1.00 9.02  ? 3152 GLN A C     1 
ATOM   13296 O O     . GLN A 1 3152 ? 195.660 177.831 176.929 1.00 8.15  ? 3152 GLN A O     1 
ATOM   13297 C CB    . GLN A 1 3152 ? 195.898 177.126 173.753 1.00 9.91  ? 3152 GLN A CB    1 
ATOM   13298 C CG    . GLN A 1 3152 ? 196.438 177.276 172.323 1.00 6.22  ? 3152 GLN A CG    1 
ATOM   13299 C CD    . GLN A 1 3152 ? 197.037 178.639 171.995 1.00 10.23 ? 3152 GLN A CD    1 
ATOM   13300 O OE1   . GLN A 1 3152 ? 197.407 179.415 172.874 1.00 12.28 ? 3152 GLN A OE1   1 
ATOM   13301 N NE2   . GLN A 1 3152 ? 197.118 178.938 170.705 1.00 9.53  ? 3152 GLN A NE2   1 
ATOM   13302 N N     . THR A 1 3153 ? 196.179 175.672 176.554 1.00 8.09  ? 3153 THR A N     1 
ATOM   13303 C CA    . THR A 1 3153 ? 195.525 175.197 177.765 1.00 5.77  ? 3153 THR A CA    1 
ATOM   13304 C C     . THR A 1 3153 ? 196.214 175.735 179.005 1.00 11.50 ? 3153 THR A C     1 
ATOM   13305 O O     . THR A 1 3153 ? 195.554 176.049 179.999 1.00 17.63 ? 3153 THR A O     1 
ATOM   13306 C CB    . THR A 1 3153 ? 195.509 173.671 177.787 1.00 7.13  ? 3153 THR A CB    1 
ATOM   13307 O OG1   . THR A 1 3153 ? 194.864 173.191 176.604 1.00 16.09 ? 3153 THR A OG1   1 
ATOM   13308 C CG2   . THR A 1 3153 ? 194.757 173.163 179.001 1.00 7.39  ? 3153 THR A CG2   1 
ATOM   13309 N N     . LEU A 1 3154 ? 197.542 175.847 178.974 1.00 10.43 ? 3154 LEU A N     1 
ATOM   13310 C CA    . LEU A 1 3154 ? 198.214 176.474 180.107 1.00 8.87  ? 3154 LEU A CA    1 
ATOM   13311 C C     . LEU A 1 3154 ? 197.866 177.952 180.202 1.00 7.37  ? 3154 LEU A C     1 
ATOM   13312 O O     . LEU A 1 3154 ? 197.767 178.505 181.305 1.00 10.89 ? 3154 LEU A O     1 
ATOM   13313 C CB    . LEU A 1 3154 ? 199.723 176.280 180.030 1.00 2.40  ? 3154 LEU A CB    1 
ATOM   13314 C CG    . LEU A 1 3154 ? 200.225 176.326 181.471 1.00 8.58  ? 3154 LEU A CG    1 
ATOM   13315 C CD1   . LEU A 1 3154 ? 199.655 175.161 182.225 1.00 11.67 ? 3154 LEU A CD1   1 
ATOM   13316 C CD2   . LEU A 1 3154 ? 201.713 176.294 181.552 1.00 10.05 ? 3154 LEU A CD2   1 
ATOM   13317 N N     . HIS A 1 3155 ? 197.671 178.613 179.060 1.00 11.13 ? 3155 HIS A N     1 
ATOM   13318 C CA    . HIS A 1 3155 ? 197.215 180.002 179.110 1.00 7.30  ? 3155 HIS A CA    1 
ATOM   13319 C C     . HIS A 1 3155 ? 195.830 180.111 179.747 1.00 11.84 ? 3155 HIS A C     1 
ATOM   13320 O O     . HIS A 1 3155 ? 195.591 180.988 180.590 1.00 10.97 ? 3155 HIS A O     1 
ATOM   13321 C CB    . HIS A 1 3155 ? 197.223 180.608 177.708 1.00 10.76 ? 3155 HIS A CB    1 
ATOM   13322 C CG    . HIS A 1 3155 ? 198.539 181.210 177.325 1.00 8.96  ? 3155 HIS A CG    1 
ATOM   13323 N ND1   . HIS A 1 3155 ? 199.314 181.928 178.209 1.00 6.65  ? 3155 HIS A ND1   1 
ATOM   13324 C CD2   . HIS A 1 3155 ? 199.222 181.190 176.156 1.00 9.43  ? 3155 HIS A CD2   1 
ATOM   13325 C CE1   . HIS A 1 3155 ? 200.416 182.330 177.601 1.00 9.58  ? 3155 HIS A CE1   1 
ATOM   13326 N NE2   . HIS A 1 3155 ? 200.385 181.895 176.354 1.00 10.30 ? 3155 HIS A NE2   1 
ATOM   13327 N N     . GLN A 1 3156 ? 194.905 179.224 179.366 1.00 14.86 ? 3156 GLN A N     1 
ATOM   13328 C CA    . GLN A 1 3156 ? 193.587 179.218 180.004 1.00 9.20  ? 3156 GLN A CA    1 
ATOM   13329 C C     . GLN A 1 3156 ? 193.691 178.884 181.485 1.00 8.98  ? 3156 GLN A C     1 
ATOM   13330 O O     . GLN A 1 3156 ? 192.925 179.410 182.298 1.00 16.25 ? 3156 GLN A O     1 
ATOM   13331 C CB    . GLN A 1 3156 ? 192.625 178.240 179.319 1.00 7.42  ? 3156 GLN A CB    1 
ATOM   13332 C CG    . GLN A 1 3156 ? 192.862 177.945 177.852 1.00 13.81 ? 3156 GLN A CG    1 
ATOM   13333 C CD    . GLN A 1 3156 ? 192.867 179.188 176.979 1.00 17.83 ? 3156 GLN A CD    1 
ATOM   13334 O OE1   . GLN A 1 3156 ? 192.342 180.236 177.357 1.00 15.27 ? 3156 GLN A OE1   1 
ATOM   13335 N NE2   . GLN A 1 3156 ? 193.462 179.074 175.797 1.00 13.60 ? 3156 GLN A NE2   1 
ATOM   13336 N N     . ALA A 1 3157 ? 194.611 177.990 181.851 1.00 10.86 ? 3157 ALA A N     1 
ATOM   13337 C CA    . ALA A 1 3157 ? 194.804 177.653 183.256 1.00 13.44 ? 3157 ALA A CA    1 
ATOM   13338 C C     . ALA A 1 3157 ? 195.263 178.865 184.051 1.00 12.31 ? 3157 ALA A C     1 
ATOM   13339 O O     . ALA A 1 3157 ? 194.761 179.122 185.150 1.00 18.19 ? 3157 ALA A O     1 
ATOM   13340 C CB    . ALA A 1 3157 ? 195.815 176.515 183.387 1.00 13.26 ? 3157 ALA A CB    1 
ATOM   13341 N N     . ASN A 1 3158 ? 196.212 179.626 183.504 1.00 9.93  ? 3158 ASN A N     1 
ATOM   13342 C CA    . ASN A 1 3158 ? 196.650 180.853 184.161 1.00 14.02 ? 3158 ASN A CA    1 
ATOM   13343 C C     . ASN A 1 3158 ? 195.505 181.850 184.286 1.00 19.57 ? 3158 ASN A C     1 
ATOM   13344 O O     . ASN A 1 3158 ? 195.331 182.481 185.336 1.00 18.34 ? 3158 ASN A O     1 
ATOM   13345 C CB    . ASN A 1 3158 ? 197.814 181.470 183.390 1.00 13.19 ? 3158 ASN A CB    1 
ATOM   13346 C CG    . ASN A 1 3158 ? 199.158 181.065 183.946 1.00 9.77  ? 3158 ASN A CG    1 
ATOM   13347 O OD1   . ASN A 1 3158 ? 199.250 180.197 184.811 1.00 12.00 ? 3158 ASN A OD1   1 
ATOM   13348 N ND2   . ASN A 1 3158 ? 200.213 181.689 183.445 1.00 10.92 ? 3158 ASN A ND2   1 
ATOM   13349 N N     . ALA A 1 3159 ? 194.711 182.005 183.222 1.00 23.76 ? 3159 ALA A N     1 
ATOM   13350 C CA    . ALA A 1 3159 ? 193.593 182.945 183.269 1.00 17.45 ? 3159 ALA A CA    1 
ATOM   13351 C C     . ALA A 1 3159 ? 192.567 182.542 184.322 1.00 20.28 ? 3159 ALA A C     1 
ATOM   13352 O O     . ALA A 1 3159 ? 192.088 183.386 185.089 1.00 21.68 ? 3159 ALA A O     1 
ATOM   13353 C CB    . ALA A 1 3159 ? 192.937 183.048 181.893 1.00 14.91 ? 3159 ALA A CB    1 
ATOM   13354 N N     . ARG A 1 3160 ? 192.215 181.255 184.375 1.00 19.89 ? 3160 ARG A N     1 
ATOM   13355 C CA    . ARG A 1 3160 ? 191.247 180.783 185.359 1.00 19.99 ? 3160 ARG A CA    1 
ATOM   13356 C C     . ARG A 1 3160 ? 191.790 180.909 186.775 1.00 23.78 ? 3160 ARG A C     1 
ATOM   13357 O O     . ARG A 1 3160 ? 191.046 181.252 187.702 1.00 27.69 ? 3160 ARG A O     1 
ATOM   13358 C CB    . ARG A 1 3160 ? 190.857 179.335 185.061 1.00 21.11 ? 3160 ARG A CB    1 
ATOM   13359 C CG    . ARG A 1 3160 ? 189.723 179.189 184.059 1.00 23.48 ? 3160 ARG A CG    1 
ATOM   13360 C CD    . ARG A 1 3160 ? 189.045 177.833 184.179 1.00 24.62 ? 3160 ARG A CD    1 
ATOM   13361 N NE    . ARG A 1 3160 ? 189.088 177.314 185.540 1.00 25.82 ? 3160 ARG A NE    1 
ATOM   13362 C CZ    . ARG A 1 3160 ? 188.938 176.035 185.859 1.00 27.64 ? 3160 ARG A CZ    1 
ATOM   13363 N NH1   . ARG A 1 3160 ? 188.736 175.112 184.934 1.00 27.02 ? 3160 ARG A NH1   1 
ATOM   13364 N NH2   . ARG A 1 3160 ? 188.993 175.675 187.138 1.00 23.01 ? 3160 ARG A NH2   1 
ATOM   13365 N N     . LEU A 1 3161 ? 193.080 180.624 186.966 1.00 20.96 ? 3161 LEU A N     1 
ATOM   13366 C CA    . LEU A 1 3161 ? 193.676 180.739 188.291 1.00 20.56 ? 3161 LEU A CA    1 
ATOM   13367 C C     . LEU A 1 3161 ? 193.696 182.189 188.756 1.00 23.20 ? 3161 LEU A C     1 
ATOM   13368 O O     . LEU A 1 3161 ? 193.458 182.473 189.936 1.00 26.89 ? 3161 LEU A O     1 
ATOM   13369 C CB    . LEU A 1 3161 ? 195.084 180.135 188.270 1.00 19.56 ? 3161 LEU A CB    1 
ATOM   13370 C CG    . LEU A 1 3161 ? 195.955 180.031 189.525 1.00 22.52 ? 3161 LEU A CG    1 
ATOM   13371 C CD1   . LEU A 1 3161 ? 197.008 178.961 189.311 1.00 18.87 ? 3161 LEU A CD1   1 
ATOM   13372 C CD2   . LEU A 1 3161 ? 196.634 181.346 189.855 1.00 26.73 ? 3161 LEU A CD2   1 
ATOM   13373 N N     . ALA A 1 3162 ? 193.985 183.122 187.846 1.00 25.09 ? 3162 ALA A N     1 
ATOM   13374 C CA    . ALA A 1 3162 ? 193.956 184.535 188.210 1.00 26.95 ? 3162 ALA A CA    1 
ATOM   13375 C C     . ALA A 1 3162 ? 192.535 185.003 188.498 1.00 26.15 ? 3162 ALA A C     1 
ATOM   13376 O O     . ALA A 1 3162 ? 192.307 185.782 189.431 1.00 23.59 ? 3162 ALA A O     1 
ATOM   13377 C CB    . ALA A 1 3162 ? 194.586 185.378 187.102 1.00 22.86 ? 3162 ALA A CB    1 
ATOM   13378 N N     . LYS A 1 3163 ? 191.565 184.543 187.704 1.00 25.70 ? 3163 LYS A N     1 
ATOM   13379 C CA    . LYS A 1 3163 ? 190.178 184.952 187.907 1.00 27.15 ? 3163 LYS A CA    1 
ATOM   13380 C C     . LYS A 1 3163 ? 189.637 184.441 189.238 1.00 29.17 ? 3163 LYS A C     1 
ATOM   13381 O O     . LYS A 1 3163 ? 188.947 185.170 189.960 1.00 29.25 ? 3163 LYS A O     1 
ATOM   13382 C CB    . LYS A 1 3163 ? 189.312 184.458 186.747 1.00 27.16 ? 3163 LYS A CB    1 
ATOM   13383 C CG    . LYS A 1 3163 ? 187.865 184.918 186.809 1.00 26.95 ? 3163 LYS A CG    1 
ATOM   13384 C CD    . LYS A 1 3163 ? 187.402 185.470 185.471 1.00 28.30 ? 3163 LYS A CD    1 
ATOM   13385 C CE    . LYS A 1 3163 ? 185.903 185.726 185.469 1.00 27.75 ? 3163 LYS A CE    1 
ATOM   13386 N NZ    . LYS A 1 3163 ? 185.341 185.733 184.090 1.00 24.85 ? 3163 LYS A NZ    1 
ATOM   13387 N N     . ARG A 1 3164 ? 189.941 183.189 189.582 1.00 28.37 ? 3164 ARG A N     1 
ATOM   13388 C CA    . ARG A 1 3164 ? 189.445 182.562 190.801 1.00 27.10 ? 3164 ARG A CA    1 
ATOM   13389 C C     . ARG A 1 3164 ? 190.455 182.627 191.941 1.00 29.19 ? 3164 ARG A C     1 
ATOM   13390 O O     . ARG A 1 3164 ? 190.522 181.708 192.764 1.00 30.40 ? 3164 ARG A O     1 
ATOM   13391 C CB    . ARG A 1 3164 ? 189.050 181.111 190.531 1.00 29.54 ? 3164 ARG A CB    1 
ATOM   13392 C CG    . ARG A 1 3164 ? 188.109 180.922 189.356 1.00 29.66 ? 3164 ARG A CG    1 
ATOM   13393 C CD    . ARG A 1 3164 ? 186.671 181.185 189.766 1.00 31.51 ? 3164 ARG A CD    1 
ATOM   13394 N NE    . ARG A 1 3164 ? 186.175 180.169 190.687 1.00 33.50 ? 3164 ARG A NE    1 
ATOM   13395 C CZ    . ARG A 1 3164 ? 185.582 179.043 190.314 1.00 31.04 ? 3164 ARG A CZ    1 
ATOM   13396 N NH1   . ARG A 1 3164 ? 185.395 178.750 189.038 1.00 31.24 ? 3164 ARG A NH1   1 
ATOM   13397 N NH2   . ARG A 1 3164 ? 185.167 178.190 191.246 1.00 29.44 ? 3164 ARG A NH2   1 
ATOM   13398 N N     . GLY A 1 3165 ? 191.243 183.695 192.007 1.00 26.64 ? 3165 GLY A N     1 
ATOM   13399 C CA    . GLY A 1 3165 ? 192.248 183.824 193.042 1.00 28.01 ? 3165 GLY A CA    1 
ATOM   13400 C C     . GLY A 1 3165 ? 193.352 184.785 192.660 1.00 28.08 ? 3165 GLY A C     1 
ATOM   13401 O O     . GLY A 1 3165 ? 193.082 185.917 192.248 1.00 27.12 ? 3165 GLY A O     1 
ATOM   13402 N N     . GLY A 1 3166 ? 194.591 184.352 192.789 1.00 31.36 ? 3166 GLY A N     1 
ATOM   13403 C CA    . GLY A 1 3166 ? 195.724 185.184 192.441 1.00 31.60 ? 3166 GLY A CA    1 
ATOM   13404 C C     . GLY A 1 3166 ? 197.010 184.397 192.385 1.00 30.21 ? 3166 GLY A C     1 
ATOM   13405 O O     . GLY A 1 3166 ? 197.009 183.168 192.486 1.00 24.68 ? 3166 GLY A O     1 
ATOM   13406 N N     . ARG A 1 3167 ? 198.115 185.125 192.222 1.00 33.12 ? 3167 ARG A N     1 
ATOM   13407 C CA    . ARG A 1 3167 ? 199.456 184.545 192.152 1.00 30.66 ? 3167 ARG A CA    1 
ATOM   13408 C C     . ARG A 1 3167 ? 199.564 183.566 190.983 1.00 28.19 ? 3167 ARG A C     1 
ATOM   13409 O O     . ARG A 1 3167 ? 199.812 182.371 191.153 1.00 26.06 ? 3167 ARG A O     1 
ATOM   13410 C CB    . ARG A 1 3167 ? 199.843 183.886 193.480 1.00 30.39 ? 3167 ARG A CB    1 
ATOM   13411 C CG    . ARG A 1 3167 ? 201.275 183.378 193.537 1.00 27.07 ? 3167 ARG A CG    1 
ATOM   13412 C CD    . ARG A 1 3167 ? 202.244 184.505 193.848 1.00 26.28 ? 3167 ARG A CD    1 
ATOM   13413 N NE    . ARG A 1 3167 ? 202.115 184.953 195.229 1.00 28.15 ? 3167 ARG A NE    1 
ATOM   13414 C CZ    . ARG A 1 3167 ? 201.783 186.184 195.592 1.00 34.91 ? 3167 ARG A CZ    1 
ATOM   13415 N NH1   . ARG A 1 3167 ? 201.545 187.128 194.696 1.00 32.32 ? 3167 ARG A NH1   1 
ATOM   13416 N NH2   . ARG A 1 3167 ? 201.686 186.476 196.886 1.00 32.96 ? 3167 ARG A NH2   1 
ATOM   13417 N N     . THR A 1 3168 ? 199.330 184.078 189.779 1.00 24.78 ? 3168 THR A N     1 
ATOM   13418 C CA    . THR A 1 3168 ? 199.569 183.341 188.547 1.00 22.01 ? 3168 THR A CA    1 
ATOM   13419 C C     . THR A 1 3168 ? 200.934 183.742 188.008 1.00 20.56 ? 3168 THR A C     1 
ATOM   13420 O O     . THR A 1 3168 ? 201.509 184.742 188.450 1.00 23.74 ? 3168 THR A O     1 
ATOM   13421 C CB    . THR A 1 3168 ? 198.481 183.627 187.513 1.00 24.29 ? 3168 THR A CB    1 
ATOM   13422 O OG1   . THR A 1 3168 ? 198.646 182.755 186.389 1.00 25.48 ? 3168 THR A OG1   1 
ATOM   13423 C CG2   . THR A 1 3168 ? 198.562 185.068 187.039 1.00 21.86 ? 3168 THR A CG2   1 
ATOM   13424 N N     . MET A 1 3169 ? 201.454 182.968 187.064 1.00 18.12 ? 3169 MET A N     1 
ATOM   13425 C CA    . MET A 1 3169 ? 202.775 183.237 186.522 1.00 16.05 ? 3169 MET A CA    1 
ATOM   13426 C C     . MET A 1 3169 ? 202.738 183.252 184.999 1.00 17.20 ? 3169 MET A C     1 
ATOM   13427 O O     . MET A 1 3169 ? 202.075 182.427 184.366 1.00 20.14 ? 3169 MET A O     1 
ATOM   13428 C CB    . MET A 1 3169 ? 203.782 182.200 187.017 1.00 14.44 ? 3169 MET A CB    1 
ATOM   13429 C CG    . MET A 1 3169 ? 204.242 182.470 188.436 1.00 18.02 ? 3169 MET A CG    1 
ATOM   13430 S SD    . MET A 1 3169 ? 205.767 183.415 188.528 1.00 28.50 ? 3169 MET A SD    1 
ATOM   13431 C CE    . MET A 1 3169 ? 206.115 183.336 190.281 1.00 13.44 ? 3169 MET A CE    1 
ATOM   13432 N N     . ALA A 1 3170 ? 203.465 184.201 184.417 1.00 12.88 ? 3170 ALA A N     1 
ATOM   13433 C CA    . ALA A 1 3170 ? 203.482 184.423 182.978 1.00 11.73 ? 3170 ALA A CA    1 
ATOM   13434 C C     . ALA A 1 3170 ? 204.174 183.258 182.288 1.00 11.25 ? 3170 ALA A C     1 
ATOM   13435 O O     . ALA A 1 3170 ? 205.217 182.786 182.753 1.00 9.35  ? 3170 ALA A O     1 
ATOM   13436 C CB    . ALA A 1 3170 ? 204.190 185.734 182.633 1.00 13.34 ? 3170 ALA A CB    1 
ATOM   13437 N N     . ILE A 1 3171 ? 203.593 182.798 181.185 1.00 11.79 ? 3171 ILE A N     1 
ATOM   13438 C CA    . ILE A 1 3171 ? 204.155 181.696 180.414 1.00 6.27  ? 3171 ILE A CA    1 
ATOM   13439 C C     . ILE A 1 3171 ? 204.594 182.244 179.062 1.00 4.61  ? 3171 ILE A C     1 
ATOM   13440 O O     . ILE A 1 3171 ? 203.798 182.833 178.328 1.00 9.47  ? 3171 ILE A O     1 
ATOM   13441 C CB    . ILE A 1 3171 ? 203.153 180.547 180.263 1.00 2.92  ? 3171 ILE A CB    1 
ATOM   13442 C CG1   . ILE A 1 3171 ? 202.848 179.960 181.642 1.00 3.93  ? 3171 ILE A CG1   1 
ATOM   13443 C CG2   . ILE A 1 3171 ? 203.690 179.491 179.310 1.00 6.31  ? 3171 ILE A CG2   1 
ATOM   13444 C CD1   . ILE A 1 3171 ? 203.867 178.943 182.114 1.00 6.46  ? 3171 ILE A CD1   1 
ATOM   13445 N N     . THR A 1 3172 ? 205.858 182.048 178.739 1.00 2.70  ? 3172 THR A N     1 
ATOM   13446 C CA    . THR A 1 3172 ? 206.538 182.668 177.616 1.00 1.90  ? 3172 THR A CA    1 
ATOM   13447 C C     . THR A 1 3172 ? 206.747 181.670 176.485 1.00 4.78  ? 3172 THR A C     1 
ATOM   13448 O O     . THR A 1 3172 ? 206.559 180.464 176.664 1.00 10.84 ? 3172 THR A O     1 
ATOM   13449 C CB    . THR A 1 3172 ? 207.883 183.225 178.078 1.00 3.19  ? 3172 THR A CB    1 
ATOM   13450 O OG1   . THR A 1 3172 ? 208.801 182.148 178.299 1.00 8.21  ? 3172 THR A OG1   1 
ATOM   13451 C CG2   . THR A 1 3172 ? 207.717 184.014 179.364 1.00 1.45  ? 3172 THR A CG2   1 
ATOM   13452 N N     . PRO A 1 3173 ? 207.118 182.144 175.290 1.00 0.42  ? 3173 PRO A N     1 
ATOM   13453 C CA    . PRO A 1 3173 ? 207.510 181.207 174.225 1.00 0.00  ? 3173 PRO A CA    1 
ATOM   13454 C C     . PRO A 1 3173 ? 208.711 180.355 174.582 1.00 0.43  ? 3173 PRO A C     1 
ATOM   13455 O O     . PRO A 1 3173 ? 208.883 179.275 174.002 1.00 5.78  ? 3173 PRO A O     1 
ATOM   13456 C CB    . PRO A 1 3173 ? 207.813 182.135 173.044 1.00 3.23  ? 3173 PRO A CB    1 
ATOM   13457 C CG    . PRO A 1 3173 ? 206.960 183.316 173.290 1.00 3.56  ? 3173 PRO A CG    1 
ATOM   13458 C CD    . PRO A 1 3173 ? 207.002 183.519 174.774 1.00 2.65  ? 3173 PRO A CD    1 
ATOM   13459 N N     . ARG A 1 3174 ? 209.557 180.808 175.509 1.00 0.00  ? 3174 ARG A N     1 
ATOM   13460 C CA    . ARG A 1 3174 ? 210.661 179.973 175.964 1.00 1.70  ? 3174 ARG A CA    1 
ATOM   13461 C C     . ARG A 1 3174 ? 210.156 178.730 176.682 1.00 1.99  ? 3174 ARG A C     1 
ATOM   13462 O O     . ARG A 1 3174 ? 210.803 177.680 176.629 1.00 7.96  ? 3174 ARG A O     1 
ATOM   13463 C CB    . ARG A 1 3174 ? 211.593 180.787 176.858 1.00 3.06  ? 3174 ARG A CB    1 
ATOM   13464 C CG    . ARG A 1 3174 ? 212.644 181.548 176.070 1.00 7.50  ? 3174 ARG A CG    1 
ATOM   13465 C CD    . ARG A 1 3174 ? 213.996 181.518 176.752 1.00 4.61  ? 3174 ARG A CD    1 
ATOM   13466 N NE    . ARG A 1 3174 ? 214.071 182.505 177.821 1.00 4.89  ? 3174 ARG A NE    1 
ATOM   13467 C CZ    . ARG A 1 3174 ? 214.649 183.692 177.698 1.00 8.94  ? 3174 ARG A CZ    1 
ATOM   13468 N NH1   . ARG A 1 3174 ? 215.241 184.059 176.574 1.00 8.36  ? 3174 ARG A NH1   1 
ATOM   13469 N NH2   . ARG A 1 3174 ? 214.632 184.531 178.729 1.00 9.66  ? 3174 ARG A NH2   1 
ATOM   13470 N N     . HIS A 1 3175 ? 208.991 178.819 177.328 1.00 0.96  ? 3175 HIS A N     1 
ATOM   13471 C CA    . HIS A 1 3175 ? 208.350 177.622 177.859 1.00 0.00  ? 3175 HIS A CA    1 
ATOM   13472 C C     . HIS A 1 3175 ? 207.984 176.656 176.741 1.00 1.05  ? 3175 HIS A C     1 
ATOM   13473 O O     . HIS A 1 3175 ? 208.159 175.443 176.880 1.00 9.47  ? 3175 HIS A O     1 
ATOM   13474 C CB    . HIS A 1 3175 ? 207.110 178.001 178.664 1.00 1.81  ? 3175 HIS A CB    1 
ATOM   13475 C CG    . HIS A 1 3175 ? 207.417 178.701 179.950 1.00 5.82  ? 3175 HIS A CG    1 
ATOM   13476 N ND1   . HIS A 1 3175 ? 207.976 179.959 179.997 1.00 6.12  ? 3175 HIS A ND1   1 
ATOM   13477 C CD2   . HIS A 1 3175 ? 207.240 178.319 181.236 1.00 7.31  ? 3175 HIS A CD2   1 
ATOM   13478 C CE1   . HIS A 1 3175 ? 208.134 180.321 181.257 1.00 6.30  ? 3175 HIS A CE1   1 
ATOM   13479 N NE2   . HIS A 1 3175 ? 207.694 179.345 182.029 1.00 8.00  ? 3175 HIS A NE2   1 
ATOM   13480 N N     . TYR A 1 3176 ? 207.472 177.176 175.623 1.00 4.20  ? 3176 TYR A N     1 
ATOM   13481 C CA    . TYR A 1 3176 ? 207.153 176.321 174.484 1.00 1.00  ? 3176 TYR A CA    1 
ATOM   13482 C C     . TYR A 1 3176 ? 208.405 175.660 173.922 1.00 0.00  ? 3176 TYR A C     1 
ATOM   13483 O O     . TYR A 1 3176 ? 208.396 174.471 173.583 1.00 8.64  ? 3176 TYR A O     1 
ATOM   13484 C CB    . TYR A 1 3176 ? 206.444 177.133 173.401 1.00 2.00  ? 3176 TYR A CB    1 
ATOM   13485 C CG    . TYR A 1 3176 ? 205.837 176.294 172.301 1.00 1.13  ? 3176 TYR A CG    1 
ATOM   13486 C CD1   . TYR A 1 3176 ? 204.670 175.576 172.512 1.00 1.37  ? 3176 TYR A CD1   1 
ATOM   13487 C CD2   . TYR A 1 3176 ? 206.432 176.223 171.051 1.00 0.00  ? 3176 TYR A CD2   1 
ATOM   13488 C CE1   . TYR A 1 3176 ? 204.115 174.811 171.511 1.00 0.65  ? 3176 TYR A CE1   1 
ATOM   13489 C CE2   . TYR A 1 3176 ? 205.884 175.459 170.044 1.00 0.57  ? 3176 TYR A CE2   1 
ATOM   13490 C CZ    . TYR A 1 3176 ? 204.726 174.756 170.279 1.00 1.35  ? 3176 TYR A CZ    1 
ATOM   13491 O OH    . TYR A 1 3176 ? 204.177 173.995 169.275 1.00 5.65  ? 3176 TYR A OH    1 
ATOM   13492 N N     . LEU A 1 3177 ? 209.492 176.422 173.804 1.00 0.00  ? 3177 LEU A N     1 
ATOM   13493 C CA    . LEU A 1 3177 ? 210.733 175.849 173.291 1.00 1.37  ? 3177 LEU A CA    1 
ATOM   13494 C C     . LEU A 1 3177 ? 211.272 174.776 174.227 1.00 2.85  ? 3177 LEU A C     1 
ATOM   13495 O O     . LEU A 1 3177 ? 211.744 173.724 173.776 1.00 10.52 ? 3177 LEU A O     1 
ATOM   13496 C CB    . LEU A 1 3177 ? 211.772 176.949 173.078 1.00 3.00  ? 3177 LEU A CB    1 
ATOM   13497 C CG    . LEU A 1 3177 ? 211.402 178.037 172.071 1.00 4.40  ? 3177 LEU A CG    1 
ATOM   13498 C CD1   . LEU A 1 3177 ? 212.345 179.214 172.205 1.00 3.42  ? 3177 LEU A CD1   1 
ATOM   13499 C CD2   . LEU A 1 3177 ? 211.425 177.489 170.658 1.00 5.72  ? 3177 LEU A CD2   1 
ATOM   13500 N N     . ASP A 1 3178 ? 211.206 175.022 175.537 1.00 3.40  ? 3178 ASP A N     1 
ATOM   13501 C CA    . ASP A 1 3178 ? 211.660 174.031 176.506 1.00 0.98  ? 3178 ASP A CA    1 
ATOM   13502 C C     . ASP A 1 3178 ? 210.783 172.785 176.461 1.00 2.06  ? 3178 ASP A C     1 
ATOM   13503 O O     . ASP A 1 3178 ? 211.276 171.660 176.581 1.00 11.85 ? 3178 ASP A O     1 
ATOM   13504 C CB    . ASP A 1 3178 ? 211.671 174.649 177.905 1.00 4.78  ? 3178 ASP A CB    1 
ATOM   13505 C CG    . ASP A 1 3178 ? 212.058 173.659 178.979 1.00 12.99 ? 3178 ASP A CG    1 
ATOM   13506 O OD1   . ASP A 1 3178 ? 212.992 172.863 178.746 1.00 15.04 ? 3178 ASP A OD1   1 
ATOM   13507 O OD2   . ASP A 1 3178 ? 211.436 173.685 180.061 1.00 12.91 ? 3178 ASP A OD2   1 
ATOM   13508 N N     . PHE A 1 3179 ? 209.473 172.970 176.286 1.00 0.84  ? 3179 PHE A N     1 
ATOM   13509 C CA    . PHE A 1 3179 ? 208.561 171.838 176.155 1.00 0.26  ? 3179 PHE A CA    1 
ATOM   13510 C C     . PHE A 1 3179 ? 208.876 171.012 174.918 1.00 1.03  ? 3179 PHE A C     1 
ATOM   13511 O O     . PHE A 1 3179 ? 208.870 169.778 174.970 1.00 9.28  ? 3179 PHE A O     1 
ATOM   13512 C CB    . PHE A 1 3179 ? 207.121 172.351 176.131 1.00 0.02  ? 3179 PHE A CB    1 
ATOM   13513 C CG    . PHE A 1 3179 ? 206.126 171.403 175.515 1.00 0.00  ? 3179 PHE A CG    1 
ATOM   13514 C CD1   . PHE A 1 3179 ? 206.000 170.100 175.960 1.00 1.93  ? 3179 PHE A CD1   1 
ATOM   13515 C CD2   . PHE A 1 3179 ? 205.271 171.844 174.518 1.00 0.69  ? 3179 PHE A CD2   1 
ATOM   13516 C CE1   . PHE A 1 3179 ? 205.076 169.248 175.391 1.00 3.74  ? 3179 PHE A CE1   1 
ATOM   13517 C CE2   . PHE A 1 3179 ? 204.340 170.998 173.958 1.00 1.18  ? 3179 PHE A CE2   1 
ATOM   13518 C CZ    . PHE A 1 3179 ? 204.243 169.699 174.394 1.00 1.89  ? 3179 PHE A CZ    1 
ATOM   13519 N N     . ILE A 1 3180 ? 209.163 171.671 173.797 1.00 4.65  ? 3180 ILE A N     1 
ATOM   13520 C CA    . ILE A 1 3180 ? 209.471 170.935 172.575 1.00 5.07  ? 3180 ILE A CA    1 
ATOM   13521 C C     . ILE A 1 3180 ? 210.794 170.190 172.723 1.00 1.19  ? 3180 ILE A C     1 
ATOM   13522 O O     . ILE A 1 3180 ? 210.931 169.043 172.278 1.00 3.73  ? 3180 ILE A O     1 
ATOM   13523 C CB    . ILE A 1 3180 ? 209.476 171.890 171.369 1.00 2.91  ? 3180 ILE A CB    1 
ATOM   13524 C CG1   . ILE A 1 3180 ? 208.051 172.343 171.051 1.00 0.00  ? 3180 ILE A CG1   1 
ATOM   13525 C CG2   . ILE A 1 3180 ? 210.061 171.204 170.161 1.00 6.45  ? 3180 ILE A CG2   1 
ATOM   13526 C CD1   . ILE A 1 3180 ? 207.105 171.217 170.725 1.00 0.96  ? 3180 ILE A CD1   1 
ATOM   13527 N N     . ASN A 1 3181 ? 211.786 170.823 173.356 1.00 0.00  ? 3181 ASN A N     1 
ATOM   13528 C CA    . ASN A 1 3181 ? 213.061 170.149 173.594 1.00 1.89  ? 3181 ASN A CA    1 
ATOM   13529 C C     . ASN A 1 3181 ? 212.893 168.945 174.514 1.00 4.04  ? 3181 ASN A C     1 
ATOM   13530 O O     . ASN A 1 3181 ? 213.484 167.882 174.277 1.00 5.78  ? 3181 ASN A O     1 
ATOM   13531 C CB    . ASN A 1 3181 ? 214.071 171.133 174.180 1.00 2.33  ? 3181 ASN A CB    1 
ATOM   13532 C CG    . ASN A 1 3181 ? 215.460 170.945 173.613 1.00 11.27 ? 3181 ASN A CG    1 
ATOM   13533 O OD1   . ASN A 1 3181 ? 215.628 170.734 172.413 1.00 9.72  ? 3181 ASN A OD1   1 
ATOM   13534 N ND2   . ASN A 1 3181 ? 216.466 171.023 174.474 1.00 10.69 ? 3181 ASN A ND2   1 
ATOM   13535 N N     . HIS A 1 3182 ? 212.098 169.096 175.577 1.00 6.71  ? 3182 HIS A N     1 
ATOM   13536 C CA    . HIS A 1 3182 ? 211.815 167.978 176.469 1.00 0.53  ? 3182 HIS A CA    1 
ATOM   13537 C C     . HIS A 1 3182 ? 211.124 166.849 175.725 1.00 3.86  ? 3182 HIS A C     1 
ATOM   13538 O O     . HIS A 1 3182 ? 211.464 165.675 175.908 1.00 13.36 ? 3182 HIS A O     1 
ATOM   13539 C CB    . HIS A 1 3182 ? 210.947 168.446 177.637 1.00 0.00  ? 3182 HIS A CB    1 
ATOM   13540 C CG    . HIS A 1 3182 ? 211.728 168.951 178.807 1.00 3.09  ? 3182 HIS A CG    1 
ATOM   13541 N ND1   . HIS A 1 3182 ? 211.134 169.557 179.892 1.00 6.73  ? 3182 HIS A ND1   1 
ATOM   13542 C CD2   . HIS A 1 3182 ? 213.055 168.928 179.071 1.00 7.83  ? 3182 HIS A CD2   1 
ATOM   13543 C CE1   . HIS A 1 3182 ? 212.061 169.896 180.768 1.00 5.08  ? 3182 HIS A CE1   1 
ATOM   13544 N NE2   . HIS A 1 3182 ? 213.236 169.526 180.294 1.00 4.95  ? 3182 HIS A NE2   1 
ATOM   13545 N N     . TYR A 1 3183 ? 210.149 167.187 174.882 1.00 0.35  ? 3183 TYR A N     1 
ATOM   13546 C CA    . TYR A 1 3183 ? 209.444 166.174 174.109 1.00 0.00  ? 3183 TYR A CA    1 
ATOM   13547 C C     . TYR A 1 3183 ? 210.400 165.423 173.197 1.00 2.40  ? 3183 TYR A C     1 
ATOM   13548 O O     . TYR A 1 3183 ? 210.380 164.189 173.142 1.00 10.08 ? 3183 TYR A O     1 
ATOM   13549 C CB    . TYR A 1 3183 ? 208.317 166.836 173.317 1.00 3.56  ? 3183 TYR A CB    1 
ATOM   13550 C CG    . TYR A 1 3183 ? 207.455 165.892 172.515 1.00 2.87  ? 3183 TYR A CG    1 
ATOM   13551 C CD1   . TYR A 1 3183 ? 207.195 164.606 172.960 1.00 5.60  ? 3183 TYR A CD1   1 
ATOM   13552 C CD2   . TYR A 1 3183 ? 206.853 166.311 171.339 1.00 0.00  ? 3183 TYR A CD2   1 
ATOM   13553 C CE1   . TYR A 1 3183 ? 206.399 163.750 172.231 1.00 2.95  ? 3183 TYR A CE1   1 
ATOM   13554 C CE2   . TYR A 1 3183 ? 206.050 165.465 170.611 1.00 3.88  ? 3183 TYR A CE2   1 
ATOM   13555 C CZ    . TYR A 1 3183 ? 205.824 164.186 171.061 1.00 2.42  ? 3183 TYR A CZ    1 
ATOM   13556 O OH    . TYR A 1 3183 ? 205.022 163.339 170.337 1.00 13.57 ? 3183 TYR A OH    1 
ATOM   13557 N N     . ALA A 1 3184 ? 211.278 166.151 172.505 1.00 4.12  ? 3184 ALA A N     1 
ATOM   13558 C CA    . ALA A 1 3184 ? 212.223 165.504 171.602 1.00 0.99  ? 3184 ALA A CA    1 
ATOM   13559 C C     . ALA A 1 3184 ? 213.162 164.572 172.359 1.00 3.52  ? 3184 ALA A C     1 
ATOM   13560 O O     . ALA A 1 3184 ? 213.345 163.411 171.974 1.00 7.33  ? 3184 ALA A O     1 
ATOM   13561 C CB    . ALA A 1 3184 ? 213.013 166.559 170.830 1.00 4.76  ? 3184 ALA A CB    1 
ATOM   13562 N N     . ASN A 1 3185 ? 213.760 165.061 173.451 1.00 3.28  ? 3185 ASN A N     1 
ATOM   13563 C CA    . ASN A 1 3185 ? 214.720 164.247 174.191 1.00 2.16  ? 3185 ASN A CA    1 
ATOM   13564 C C     . ASN A 1 3185 ? 214.058 163.023 174.812 1.00 5.93  ? 3185 ASN A C     1 
ATOM   13565 O O     . ASN A 1 3185 ? 214.603 161.912 174.752 1.00 13.58 ? 3185 ASN A O     1 
ATOM   13566 C CB    . ASN A 1 3185 ? 215.401 165.084 175.272 1.00 0.35  ? 3185 ASN A CB    1 
ATOM   13567 C CG    . ASN A 1 3185 ? 216.339 166.120 174.700 1.00 9.22  ? 3185 ASN A CG    1 
ATOM   13568 O OD1   . ASN A 1 3185 ? 217.080 165.850 173.755 1.00 10.78 ? 3185 ASN A OD1   1 
ATOM   13569 N ND2   . ASN A 1 3185 ? 216.323 167.314 175.277 1.00 12.35 ? 3185 ASN A ND2   1 
ATOM   13570 N N     . LEU A 1 3186 ? 212.887 163.206 175.423 1.00 3.89  ? 3186 LEU A N     1 
ATOM   13571 C CA    . LEU A 1 3186 ? 212.205 162.091 176.065 1.00 2.74  ? 3186 LEU A CA    1 
ATOM   13572 C C     . LEU A 1 3186 ? 211.751 161.064 175.039 1.00 8.07  ? 3186 LEU A C     1 
ATOM   13573 O O     . LEU A 1 3186 ? 211.862 159.854 175.274 1.00 24.57 ? 3186 LEU A O     1 
ATOM   13574 C CB    . LEU A 1 3186 ? 211.021 162.614 176.874 1.00 6.10  ? 3186 LEU A CB    1 
ATOM   13575 C CG    . LEU A 1 3186 ? 210.430 161.685 177.925 1.00 11.71 ? 3186 LEU A CG    1 
ATOM   13576 C CD1   . LEU A 1 3186 ? 211.349 161.598 179.128 1.00 9.86  ? 3186 LEU A CD1   1 
ATOM   13577 C CD2   . LEU A 1 3186 ? 209.071 162.198 178.330 1.00 10.31 ? 3186 LEU A CD2   1 
ATOM   13578 N N     . PHE A 1 3187 ? 211.249 161.527 173.892 1.00 7.03  ? 3187 PHE A N     1 
ATOM   13579 C CA    . PHE A 1 3187 ? 210.891 160.618 172.813 1.00 2.79  ? 3187 PHE A CA    1 
ATOM   13580 C C     . PHE A 1 3187 ? 212.103 159.816 172.359 1.00 5.94  ? 3187 PHE A C     1 
ATOM   13581 O O     . PHE A 1 3187 ? 212.020 158.594 172.194 1.00 10.87 ? 3187 PHE A O     1 
ATOM   13582 C CB    . PHE A 1 3187 ? 210.300 161.424 171.656 1.00 5.61  ? 3187 PHE A CB    1 
ATOM   13583 C CG    . PHE A 1 3187 ? 209.732 160.590 170.550 1.00 8.36  ? 3187 PHE A CG    1 
ATOM   13584 C CD1   . PHE A 1 3187 ? 208.411 160.179 170.586 1.00 11.85 ? 3187 PHE A CD1   1 
ATOM   13585 C CD2   . PHE A 1 3187 ? 210.510 160.237 169.463 1.00 10.21 ? 3187 PHE A CD2   1 
ATOM   13586 C CE1   . PHE A 1 3187 ? 207.881 159.421 169.564 1.00 10.89 ? 3187 PHE A CE1   1 
ATOM   13587 C CE2   . PHE A 1 3187 ? 209.987 159.478 168.442 1.00 13.90 ? 3187 PHE A CE2   1 
ATOM   13588 C CZ    . PHE A 1 3187 ? 208.669 159.070 168.491 1.00 11.86 ? 3187 PHE A CZ    1 
ATOM   13589 N N     . HIS A 1 3188 ? 213.247 160.483 172.180 1.00 10.62 ? 3188 HIS A N     1 
ATOM   13590 C CA    . HIS A 1 3188 ? 214.453 159.776 171.761 1.00 10.08 ? 3188 HIS A CA    1 
ATOM   13591 C C     . HIS A 1 3188 ? 214.847 158.708 172.770 1.00 12.64 ? 3188 HIS A C     1 
ATOM   13592 O O     . HIS A 1 3188 ? 215.140 157.566 172.399 1.00 19.34 ? 3188 HIS A O     1 
ATOM   13593 C CB    . HIS A 1 3188 ? 215.604 160.760 171.561 1.00 10.63 ? 3188 HIS A CB    1 
ATOM   13594 C CG    . HIS A 1 3188 ? 216.883 160.105 171.144 1.00 14.81 ? 3188 HIS A CG    1 
ATOM   13595 N ND1   . HIS A 1 3188 ? 216.962 159.242 170.073 1.00 15.65 ? 3188 HIS A ND1   1 
ATOM   13596 C CD2   . HIS A 1 3188 ? 218.129 160.168 171.669 1.00 14.72 ? 3188 HIS A CD2   1 
ATOM   13597 C CE1   . HIS A 1 3188 ? 218.205 158.811 169.948 1.00 16.09 ? 3188 HIS A CE1   1 
ATOM   13598 N NE2   . HIS A 1 3188 ? 218.933 159.358 170.904 1.00 18.87 ? 3188 HIS A NE2   1 
ATOM   13599 N N     . GLU A 1 3189 ? 214.861 159.064 174.056 1.00 9.99  ? 3189 GLU A N     1 
ATOM   13600 C CA    . GLU A 1 3189 ? 215.259 158.106 175.084 1.00 12.71 ? 3189 GLU A CA    1 
ATOM   13601 C C     . GLU A 1 3189 ? 214.314 156.912 175.117 1.00 10.53 ? 3189 GLU A C     1 
ATOM   13602 O O     . GLU A 1 3189 ? 214.750 155.755 175.200 1.00 15.71 ? 3189 GLU A O     1 
ATOM   13603 C CB    . GLU A 1 3189 ? 215.298 158.789 176.451 1.00 13.29 ? 3189 GLU A CB    1 
ATOM   13604 C CG    . GLU A 1 3189 ? 216.623 159.429 176.816 1.00 14.98 ? 3189 GLU A CG    1 
ATOM   13605 C CD    . GLU A 1 3189 ? 216.551 160.171 178.138 1.00 18.20 ? 3189 GLU A CD    1 
ATOM   13606 O OE1   . GLU A 1 3189 ? 216.432 159.506 179.189 1.00 11.28 ? 3189 GLU A OE1   1 
ATOM   13607 O OE2   . GLU A 1 3189 ? 216.601 161.420 178.127 1.00 13.98 ? 3189 GLU A OE2   1 
ATOM   13608 N N     . LYS A 1 3190 ? 213.007 157.173 175.049 1.00 5.96  ? 3190 LYS A N     1 
ATOM   13609 C CA    . LYS A 1 3190 ? 212.033 156.108 175.240 1.00 8.69  ? 3190 LYS A CA    1 
ATOM   13610 C C     . LYS A 1 3190 ? 211.819 155.281 173.980 1.00 16.95 ? 3190 LYS A C     1 
ATOM   13611 O O     . LYS A 1 3190 ? 211.200 154.215 174.055 1.00 20.66 ? 3190 LYS A O     1 
ATOM   13612 C CB    . LYS A 1 3190 ? 210.717 156.704 175.733 1.00 9.44  ? 3190 LYS A CB    1 
ATOM   13613 C CG    . LYS A 1 3190 ? 210.709 156.961 177.235 1.00 10.96 ? 3190 LYS A CG    1 
ATOM   13614 C CD    . LYS A 1 3190 ? 210.725 155.668 178.032 1.00 18.60 ? 3190 LYS A CD    1 
ATOM   13615 C CE    . LYS A 1 3190 ? 210.949 155.934 179.513 1.00 13.85 ? 3190 LYS A CE    1 
ATOM   13616 N NZ    . LYS A 1 3190 ? 211.983 156.983 179.737 1.00 16.26 ? 3190 LYS A NZ    1 
ATOM   13617 N N     . ARG A 1 3191 ? 212.303 155.745 172.826 1.00 19.14 ? 3191 ARG A N     1 
ATOM   13618 C CA    . ARG A 1 3191 ? 212.416 154.876 171.659 1.00 14.90 ? 3191 ARG A CA    1 
ATOM   13619 C C     . ARG A 1 3191 ? 213.706 154.065 171.683 1.00 17.28 ? 3191 ARG A C     1 
ATOM   13620 O O     . ARG A 1 3191 ? 213.697 152.875 171.344 1.00 24.22 ? 3191 ARG A O     1 
ATOM   13621 C CB    . ARG A 1 3191 ? 212.349 155.698 170.368 1.00 13.03 ? 3191 ARG A CB    1 
ATOM   13622 C CG    . ARG A 1 3191 ? 211.105 156.560 170.222 1.00 15.27 ? 3191 ARG A CG    1 
ATOM   13623 C CD    . ARG A 1 3191 ? 209.956 155.846 169.539 1.00 15.47 ? 3191 ARG A CD    1 
ATOM   13624 N NE    . ARG A 1 3191 ? 210.251 155.625 168.129 1.00 16.93 ? 3191 ARG A NE    1 
ATOM   13625 C CZ    . ARG A 1 3191 ? 209.337 155.586 167.169 1.00 18.61 ? 3191 ARG A CZ    1 
ATOM   13626 N NH1   . ARG A 1 3191 ? 208.051 155.751 167.431 1.00 20.45 ? 3191 ARG A NH1   1 
ATOM   13627 N NH2   . ARG A 1 3191 ? 209.725 155.378 165.914 1.00 18.57 ? 3191 ARG A NH2   1 
ATOM   13628 N N     . SER A 1 3192 ? 214.816 154.692 172.086 1.00 16.65 ? 3192 SER A N     1 
ATOM   13629 C CA    . SER A 1 3192 ? 216.102 154.006 172.093 1.00 24.34 ? 3192 SER A CA    1 
ATOM   13630 C C     . SER A 1 3192 ? 216.114 152.851 173.084 1.00 24.93 ? 3192 SER A C     1 
ATOM   13631 O O     . SER A 1 3192 ? 216.638 151.771 172.781 1.00 26.43 ? 3192 SER A O     1 
ATOM   13632 C CB    . SER A 1 3192 ? 217.218 155.000 172.414 1.00 21.14 ? 3192 SER A CB    1 
ATOM   13633 O OG    . SER A 1 3192 ? 218.442 154.332 172.659 1.00 23.58 ? 3192 SER A OG    1 
ATOM   13634 N N     . GLU A 1 3193 ? 215.547 153.056 174.276 1.00 20.99 ? 3193 GLU A N     1 
ATOM   13635 C CA    . GLU A 1 3193 ? 215.541 151.984 175.268 1.00 22.48 ? 3193 GLU A CA    1 
ATOM   13636 C C     . GLU A 1 3193 ? 214.708 150.795 174.796 1.00 24.74 ? 3193 GLU A C     1 
ATOM   13637 O O     . GLU A 1 3193 ? 215.111 149.636 174.966 1.00 30.36 ? 3193 GLU A O     1 
ATOM   13638 C CB    . GLU A 1 3193 ? 215.063 152.525 176.620 1.00 25.16 ? 3193 GLU A CB    1 
ATOM   13639 C CG    . GLU A 1 3193 ? 213.607 152.976 176.700 1.00 24.44 ? 3193 GLU A CG    1 
ATOM   13640 C CD    . GLU A 1 3193 ? 212.638 151.846 176.985 1.00 31.19 ? 3193 GLU A CD    1 
ATOM   13641 O OE1   . GLU A 1 3193 ? 213.079 150.791 177.488 1.00 33.92 ? 3193 GLU A OE1   1 
ATOM   13642 O OE2   . GLU A 1 3193 ? 211.433 152.016 176.706 1.00 31.47 ? 3193 GLU A OE2   1 
ATOM   13643 N N     . LEU A 1 3194 ? 213.556 151.058 174.174 1.00 19.94 ? 3194 LEU A N     1 
ATOM   13644 C CA    . LEU A 1 3194 ? 212.740 149.960 173.671 1.00 24.87 ? 3194 LEU A CA    1 
ATOM   13645 C C     . LEU A 1 3194 ? 213.443 149.233 172.532 1.00 31.55 ? 3194 LEU A C     1 
ATOM   13646 O O     . LEU A 1 3194 ? 213.396 148.001 172.456 1.00 33.88 ? 3194 LEU A O     1 
ATOM   13647 C CB    . LEU A 1 3194 ? 211.368 150.474 173.231 1.00 24.99 ? 3194 LEU A CB    1 
ATOM   13648 C CG    . LEU A 1 3194 ? 210.300 149.418 172.918 1.00 29.74 ? 3194 LEU A CG    1 
ATOM   13649 C CD1   . LEU A 1 3194 ? 208.920 149.970 173.210 1.00 28.93 ? 3194 LEU A CD1   1 
ATOM   13650 C CD2   . LEU A 1 3194 ? 210.366 148.932 171.475 1.00 28.67 ? 3194 LEU A CD2   1 
ATOM   13651 N N     . GLU A 1 3195 ? 214.103 149.972 171.638 1.00 30.62 ? 3195 GLU A N     1 
ATOM   13652 C CA    . GLU A 1 3195 ? 214.801 149.313 170.538 1.00 27.34 ? 3195 GLU A CA    1 
ATOM   13653 C C     . GLU A 1 3195 ? 215.948 148.450 171.050 1.00 30.21 ? 3195 GLU A C     1 
ATOM   13654 O O     . GLU A 1 3195 ? 216.164 147.333 170.558 1.00 33.45 ? 3195 GLU A O     1 
ATOM   13655 C CB    . GLU A 1 3195 ? 215.305 150.350 169.534 1.00 27.49 ? 3195 GLU A CB    1 
ATOM   13656 C CG    . GLU A 1 3195 ? 214.201 151.056 168.744 1.00 29.12 ? 3195 GLU A CG    1 
ATOM   13657 C CD    . GLU A 1 3195 ? 213.537 150.179 167.690 1.00 33.45 ? 3195 GLU A CD    1 
ATOM   13658 O OE1   . GLU A 1 3195 ? 213.704 148.941 167.723 1.00 33.69 ? 3195 GLU A OE1   1 
ATOM   13659 O OE2   . GLU A 1 3195 ? 212.834 150.737 166.821 1.00 31.72 ? 3195 GLU A OE2   1 
ATOM   13660 N N     . GLU A 1 3196 ? 216.693 148.941 172.045 1.00 27.33 ? 3196 GLU A N     1 
ATOM   13661 C CA    . GLU A 1 3196 ? 217.810 148.155 172.560 1.00 29.00 ? 3196 GLU A CA    1 
ATOM   13662 C C     . GLU A 1 3196 ? 217.321 146.921 173.313 1.00 32.17 ? 3196 GLU A C     1 
ATOM   13663 O O     . GLU A 1 3196 ? 217.920 145.843 173.200 1.00 35.12 ? 3196 GLU A O     1 
ATOM   13664 C CB    . GLU A 1 3196 ? 218.722 149.026 173.430 1.00 28.49 ? 3196 GLU A CB    1 
ATOM   13665 C CG    . GLU A 1 3196 ? 218.178 149.425 174.789 1.00 31.73 ? 3196 GLU A CG    1 
ATOM   13666 C CD    . GLU A 1 3196 ? 218.485 148.404 175.866 1.00 34.47 ? 3196 GLU A CD    1 
ATOM   13667 O OE1   . GLU A 1 3196 ? 219.423 147.601 175.673 1.00 34.36 ? 3196 GLU A OE1   1 
ATOM   13668 O OE2   . GLU A 1 3196 ? 217.789 148.403 176.903 1.00 32.35 ? 3196 GLU A OE2   1 
ATOM   13669 N N     . GLN A 1 3197 ? 216.220 147.034 174.064 1.00 27.96 ? 3197 GLN A N     1 
ATOM   13670 C CA    . GLN A 1 3197 ? 215.713 145.831 174.716 1.00 29.28 ? 3197 GLN A CA    1 
ATOM   13671 C C     . GLN A 1 3197 ? 215.131 144.851 173.701 1.00 32.24 ? 3197 GLN A C     1 
ATOM   13672 O O     . GLN A 1 3197 ? 215.223 143.635 173.896 1.00 37.14 ? 3197 GLN A O     1 
ATOM   13673 C CB    . GLN A 1 3197 ? 214.688 146.181 175.798 1.00 29.98 ? 3197 GLN A CB    1 
ATOM   13674 C CG    . GLN A 1 3197 ? 213.410 146.817 175.312 1.00 33.01 ? 3197 GLN A CG    1 
ATOM   13675 C CD    . GLN A 1 3197 ? 212.476 147.182 176.450 1.00 35.46 ? 3197 GLN A CD    1 
ATOM   13676 O OE1   . GLN A 1 3197 ? 212.765 146.909 177.615 1.00 36.07 ? 3197 GLN A OE1   1 
ATOM   13677 N NE2   . GLN A 1 3197 ? 211.348 147.796 176.116 1.00 34.41 ? 3197 GLN A NE2   1 
ATOM   13678 N N     . GLN A 1 3198 ? 214.567 145.351 172.597 1.00 30.03 ? 3198 GLN A N     1 
ATOM   13679 C CA    . GLN A 1 3198 ? 214.079 144.454 171.552 1.00 29.70 ? 3198 GLN A CA    1 
ATOM   13680 C C     . GLN A 1 3198 ? 215.225 143.705 170.879 1.00 33.68 ? 3198 GLN A C     1 
ATOM   13681 O O     . GLN A 1 3198 ? 215.109 142.504 170.597 1.00 36.42 ? 3198 GLN A O     1 
ATOM   13682 C CB    . GLN A 1 3198 ? 213.272 145.240 170.520 1.00 29.48 ? 3198 GLN A CB    1 
ATOM   13683 C CG    . GLN A 1 3198 ? 212.349 144.383 169.672 1.00 30.83 ? 3198 GLN A CG    1 
ATOM   13684 C CD    . GLN A 1 3198 ? 211.232 145.184 169.031 1.00 34.85 ? 3198 GLN A CD    1 
ATOM   13685 O OE1   . GLN A 1 3198 ? 211.105 146.387 169.259 1.00 35.51 ? 3198 GLN A OE1   1 
ATOM   13686 N NE2   . GLN A 1 3198 ? 210.416 144.519 168.222 1.00 33.00 ? 3198 GLN A NE2   1 
ATOM   13687 N N     . MET A 1 3199 ? 216.339 144.390 170.606 1.00 31.26 ? 3199 MET A N     1 
ATOM   13688 C CA    . MET A 1 3199 ? 217.466 143.685 170.000 1.00 33.79 ? 3199 MET A CA    1 
ATOM   13689 C C     . MET A 1 3199 ? 218.102 142.709 170.984 1.00 35.39 ? 3199 MET A C     1 
ATOM   13690 O O     . MET A 1 3199 ? 218.575 141.641 170.575 1.00 35.22 ? 3199 MET A O     1 
ATOM   13691 C CB    . MET A 1 3199 ? 218.497 144.675 169.443 1.00 35.13 ? 3199 MET A CB    1 
ATOM   13692 C CG    . MET A 1 3199 ? 219.158 145.615 170.438 1.00 34.49 ? 3199 MET A CG    1 
ATOM   13693 S SD    . MET A 1 3199 ? 220.435 144.873 171.477 1.00 39.18 ? 3199 MET A SD    1 
ATOM   13694 C CE    . MET A 1 3199 ? 221.878 145.086 170.438 1.00 34.47 ? 3199 MET A CE    1 
ATOM   13695 N N     . HIS A 1 3200 ? 218.104 143.039 172.280 1.00 32.93 ? 3200 HIS A N     1 
ATOM   13696 C CA    . HIS A 1 3200 ? 218.528 142.063 173.281 1.00 32.55 ? 3200 HIS A CA    1 
ATOM   13697 C C     . HIS A 1 3200 ? 217.620 140.836 173.274 1.00 36.36 ? 3200 HIS A C     1 
ATOM   13698 O O     . HIS A 1 3200 ? 218.095 139.699 173.390 1.00 37.06 ? 3200 HIS A O     1 
ATOM   13699 C CB    . HIS A 1 3200 ? 218.551 142.707 174.667 1.00 29.72 ? 3200 HIS A CB    1 
ATOM   13700 C CG    . HIS A 1 3200 ? 219.367 141.956 175.673 1.00 35.80 ? 3200 HIS A CG    1 
ATOM   13701 N ND1   . HIS A 1 3200 ? 219.775 142.513 176.866 1.00 36.59 ? 3200 HIS A ND1   1 
ATOM   13702 C CD2   . HIS A 1 3200 ? 219.849 140.690 175.666 1.00 38.59 ? 3200 HIS A CD2   1 
ATOM   13703 C CE1   . HIS A 1 3200 ? 220.472 141.624 177.550 1.00 35.79 ? 3200 HIS A CE1   1 
ATOM   13704 N NE2   . HIS A 1 3200 ? 220.532 140.509 176.844 1.00 38.45 ? 3200 HIS A NE2   1 
ATOM   13705 N N     . LEU A 1 3201 ? 216.308 141.049 173.141 1.00 34.21 ? 3201 LEU A N     1 
ATOM   13706 C CA    . LEU A 1 3201 ? 215.372 139.931 173.069 1.00 32.03 ? 3201 LEU A CA    1 
ATOM   13707 C C     . LEU A 1 3201 ? 215.646 139.058 171.849 1.00 35.03 ? 3201 LEU A C     1 
ATOM   13708 O O     . LEU A 1 3201 ? 215.599 137.824 171.932 1.00 37.66 ? 3201 LEU A O     1 
ATOM   13709 C CB    . LEU A 1 3201 ? 213.938 140.459 173.040 1.00 34.21 ? 3201 LEU A CB    1 
ATOM   13710 C CG    . LEU A 1 3201 ? 212.792 139.447 173.095 1.00 38.18 ? 3201 LEU A CG    1 
ATOM   13711 C CD1   . LEU A 1 3201 ? 212.428 139.123 174.535 1.00 36.94 ? 3201 LEU A CD1   1 
ATOM   13712 C CD2   . LEU A 1 3201 ? 211.581 139.969 172.341 1.00 33.34 ? 3201 LEU A CD2   1 
ATOM   13713 N N     . ASN A 1 3202 ? 215.930 139.683 170.704 1.00 34.78 ? 3202 ASN A N     1 
ATOM   13714 C CA    . ASN A 1 3202 ? 216.248 138.914 169.502 1.00 34.95 ? 3202 ASN A CA    1 
ATOM   13715 C C     . ASN A 1 3202 ? 217.543 138.123 169.676 1.00 34.40 ? 3202 ASN A C     1 
ATOM   13716 O O     . ASN A 1 3202 ? 217.644 136.971 169.232 1.00 36.54 ? 3202 ASN A O     1 
ATOM   13717 C CB    . ASN A 1 3202 ? 216.343 139.844 168.293 1.00 33.16 ? 3202 ASN A CB    1 
ATOM   13718 C CG    . ASN A 1 3202 ? 216.297 139.095 166.973 1.00 35.77 ? 3202 ASN A CG    1 
ATOM   13719 O OD1   . ASN A 1 3202 ? 216.177 137.870 166.944 1.00 35.82 ? 3202 ASN A OD1   1 
ATOM   13720 N ND2   . ASN A 1 3202 ? 216.390 139.831 165.872 1.00 36.54 ? 3202 ASN A ND2   1 
ATOM   13721 N N     . VAL A 1 3203 ? 218.545 138.728 170.319 1.00 34.19 ? 3203 VAL A N     1 
ATOM   13722 C CA    . VAL A 1 3203 ? 219.793 138.019 170.594 1.00 36.67 ? 3203 VAL A CA    1 
ATOM   13723 C C     . VAL A 1 3203 ? 219.532 136.810 171.485 1.00 37.81 ? 3203 VAL A C     1 
ATOM   13724 O O     . VAL A 1 3203 ? 220.080 135.722 171.263 1.00 38.00 ? 3203 VAL A O     1 
ATOM   13725 C CB    . VAL A 1 3203 ? 220.824 138.977 171.220 1.00 37.34 ? 3203 VAL A CB    1 
ATOM   13726 C CG1   . VAL A 1 3203 ? 221.970 138.200 171.850 1.00 35.73 ? 3203 VAL A CG1   1 
ATOM   13727 C CG2   . VAL A 1 3203 ? 221.350 139.944 170.170 1.00 36.10 ? 3203 VAL A CG2   1 
ATOM   13728 N N     . GLY A 1 3204 ? 218.691 136.981 172.506 1.00 36.00 ? 3204 GLY A N     1 
ATOM   13729 C CA    . GLY A 1 3204 ? 218.340 135.854 173.355 1.00 34.30 ? 3204 GLY A CA    1 
ATOM   13730 C C     . GLY A 1 3204 ? 217.614 134.755 172.602 1.00 36.15 ? 3204 GLY A C     1 
ATOM   13731 O O     . GLY A 1 3204 ? 217.837 133.567 172.849 1.00 38.89 ? 3204 GLY A O     1 
ATOM   13732 N N     . LEU A 1 3205 ? 216.719 135.135 171.685 1.00 33.46 ? 3205 LEU A N     1 
ATOM   13733 C CA    . LEU A 1 3205 ? 216.037 134.139 170.863 1.00 35.86 ? 3205 LEU A CA    1 
ATOM   13734 C C     . LEU A 1 3205 ? 217.031 133.350 170.018 1.00 36.78 ? 3205 LEU A C     1 
ATOM   13735 O O     . LEU A 1 3205 ? 216.928 132.120 169.901 1.00 36.39 ? 3205 LEU A O     1 
ATOM   13736 C CB    . LEU A 1 3205 ? 215.001 134.816 169.966 1.00 38.48 ? 3205 LEU A CB    1 
ATOM   13737 C CG    . LEU A 1 3205 ? 213.663 135.225 170.581 1.00 39.05 ? 3205 LEU A CG    1 
ATOM   13738 C CD1   . LEU A 1 3205 ? 212.940 136.199 169.667 1.00 37.30 ? 3205 LEU A CD1   1 
ATOM   13739 C CD2   . LEU A 1 3205 ? 212.800 134.004 170.847 1.00 35.16 ? 3205 LEU A CD2   1 
ATOM   13740 N N     . ARG A 1 3206 ? 218.000 134.044 169.419 1.00 38.10 ? 3206 ARG A N     1 
ATOM   13741 C CA    . ARG A 1 3206 ? 219.021 133.357 168.633 1.00 39.21 ? 3206 ARG A CA    1 
ATOM   13742 C C     . ARG A 1 3206 ? 219.850 132.423 169.509 1.00 39.68 ? 3206 ARG A C     1 
ATOM   13743 O O     . ARG A 1 3206 ? 220.198 131.311 169.091 1.00 39.36 ? 3206 ARG A O     1 
ATOM   13744 C CB    . ARG A 1 3206 ? 219.906 134.382 167.920 1.00 38.26 ? 3206 ARG A CB    1 
ATOM   13745 C CG    . ARG A 1 3206 ? 221.080 133.801 167.143 1.00 36.05 ? 3206 ARG A CG    1 
ATOM   13746 C CD    . ARG A 1 3206 ? 222.327 134.678 167.261 1.00 38.59 ? 3206 ARG A CD    1 
ATOM   13747 N NE    . ARG A 1 3206 ? 222.573 135.166 168.614 1.00 40.88 ? 3206 ARG A NE    1 
ATOM   13748 C CZ    . ARG A 1 3206 ? 222.881 134.396 169.651 1.00 39.73 ? 3206 ARG A CZ    1 
ATOM   13749 N NH1   . ARG A 1 3206 ? 223.066 133.093 169.515 1.00 39.67 ? 3206 ARG A NH1   1 
ATOM   13750 N NH2   . ARG A 1 3206 ? 223.032 134.953 170.849 1.00 37.58 ? 3206 ARG A NH2   1 
ATOM   13751 N N     . LYS A 1 3207 ? 220.162 132.853 170.734 1.00 34.75 ? 3207 LYS A N     1 
ATOM   13752 C CA    . LYS A 1 3207 ? 220.915 131.997 171.646 1.00 35.81 ? 3207 LYS A CA    1 
ATOM   13753 C C     . LYS A 1 3207 ? 220.119 130.750 172.021 1.00 38.06 ? 3207 LYS A C     1 
ATOM   13754 O O     . LYS A 1 3207 ? 220.680 129.653 172.121 1.00 37.14 ? 3207 LYS A O     1 
ATOM   13755 C CB    . LYS A 1 3207 ? 221.314 132.781 172.896 1.00 33.92 ? 3207 LYS A CB    1 
ATOM   13756 C CG    . LYS A 1 3207 ? 221.783 131.911 174.049 1.00 35.63 ? 3207 LYS A CG    1 
ATOM   13757 C CD    . LYS A 1 3207 ? 223.294 131.736 174.013 1.00 38.18 ? 3207 LYS A CD    1 
ATOM   13758 C CE    . LYS A 1 3207 ? 223.714 130.386 174.568 1.00 37.33 ? 3207 LYS A CE    1 
ATOM   13759 N NZ    . LYS A 1 3207 ? 223.615 129.309 173.544 1.00 36.96 ? 3207 LYS A NZ    1 
ATOM   13760 N N     . ILE A 1 3208 ? 218.810 130.897 172.231 1.00 36.51 ? 3208 ILE A N     1 
ATOM   13761 C CA    . ILE A 1 3208 ? 217.988 129.735 172.559 1.00 37.54 ? 3208 ILE A CA    1 
ATOM   13762 C C     . ILE A 1 3208 ? 217.901 128.784 171.369 1.00 38.36 ? 3208 ILE A C     1 
ATOM   13763 O O     . ILE A 1 3208 ? 217.902 127.559 171.538 1.00 36.65 ? 3208 ILE A O     1 
ATOM   13764 C CB    . ILE A 1 3208 ? 216.595 130.170 173.048 1.00 38.02 ? 3208 ILE A CB    1 
ATOM   13765 C CG1   . ILE A 1 3208 ? 216.710 130.933 174.366 1.00 36.75 ? 3208 ILE A CG1   1 
ATOM   13766 C CG2   . ILE A 1 3208 ? 215.691 128.966 173.237 1.00 35.71 ? 3208 ILE A CG2   1 
ATOM   13767 C CD1   . ILE A 1 3208 ? 215.516 131.799 174.666 1.00 37.27 ? 3208 ILE A CD1   1 
ATOM   13768 N N     . LYS A 1 3209 ? 217.833 129.323 170.148 1.00 37.41 ? 3209 LYS A N     1 
ATOM   13769 C CA    . LYS A 1 3209 ? 217.876 128.457 168.970 1.00 37.97 ? 3209 LYS A CA    1 
ATOM   13770 C C     . LYS A 1 3209 ? 219.200 127.701 168.889 1.00 40.52 ? 3209 LYS A C     1 
ATOM   13771 O O     . LYS A 1 3209 ? 219.232 126.511 168.545 1.00 39.31 ? 3209 LYS A O     1 
ATOM   13772 C CB    . LYS A 1 3209 ? 217.650 129.277 167.700 1.00 38.67 ? 3209 LYS A CB    1 
ATOM   13773 C CG    . LYS A 1 3209 ? 216.191 129.582 167.402 1.00 40.21 ? 3209 LYS A CG    1 
ATOM   13774 C CD    . LYS A 1 3209 ? 216.058 130.540 166.229 1.00 41.47 ? 3209 LYS A CD    1 
ATOM   13775 C CE    . LYS A 1 3209 ? 214.661 131.137 166.156 1.00 38.33 ? 3209 LYS A CE    1 
ATOM   13776 N NZ    . LYS A 1 3209 ? 213.605 130.087 166.164 1.00 39.41 ? 3209 LYS A NZ    1 
ATOM   13777 N N     . GLU A 1 3210 ? 220.306 128.381 169.199 1.00 40.25 ? 3210 GLU A N     1 
ATOM   13778 C CA    . GLU A 1 3210 ? 221.611 127.725 169.204 1.00 39.92 ? 3210 GLU A CA    1 
ATOM   13779 C C     . GLU A 1 3210 ? 221.662 126.622 170.261 1.00 42.03 ? 3210 GLU A C     1 
ATOM   13780 O O     . GLU A 1 3210 ? 222.242 125.550 170.035 1.00 42.24 ? 3210 GLU A O     1 
ATOM   13781 C CB    . GLU A 1 3210 ? 222.697 128.780 169.435 1.00 37.17 ? 3210 GLU A CB    1 
ATOM   13782 C CG    . GLU A 1 3210 ? 224.136 128.338 169.213 1.00 41.61 ? 3210 GLU A CG    1 
ATOM   13783 C CD    . GLU A 1 3210 ? 224.723 127.593 170.387 1.00 45.04 ? 3210 GLU A CD    1 
ATOM   13784 O OE1   . GLU A 1 3210 ? 224.776 128.165 171.496 1.00 39.88 ? 3210 GLU A OE1   1 
ATOM   13785 O OE2   . GLU A 1 3210 ? 225.162 126.444 170.190 1.00 44.88 ? 3210 GLU A OE2   1 
ATOM   13786 N N     . THR A 1 3211 ? 221.047 126.868 171.420 1.00 37.52 ? 3211 THR A N     1 
ATOM   13787 C CA    . THR A 1 3211 ? 220.955 125.842 172.455 1.00 38.36 ? 3211 THR A CA    1 
ATOM   13788 C C     . THR A 1 3211 ? 220.118 124.655 171.986 1.00 39.51 ? 3211 THR A C     1 
ATOM   13789 O O     . THR A 1 3211 ? 220.438 123.500 172.293 1.00 40.11 ? 3211 THR A O     1 
ATOM   13790 C CB    . THR A 1 3211 ? 220.368 126.441 173.735 1.00 38.51 ? 3211 THR A CB    1 
ATOM   13791 O OG1   . THR A 1 3211 ? 221.213 127.501 174.199 1.00 39.97 ? 3211 THR A OG1   1 
ATOM   13792 C CG2   . THR A 1 3211 ? 220.256 125.383 174.824 1.00 36.50 ? 3211 THR A CG2   1 
ATOM   13793 N N     . VAL A 1 3212 ? 219.035 124.921 171.251 1.00 36.95 ? 3212 VAL A N     1 
ATOM   13794 C CA    . VAL A 1 3212 ? 218.233 123.838 170.682 1.00 39.34 ? 3212 VAL A CA    1 
ATOM   13795 C C     . VAL A 1 3212 ? 219.073 123.007 169.720 1.00 40.37 ? 3212 VAL A C     1 
ATOM   13796 O O     . VAL A 1 3212 ? 218.969 121.774 169.682 1.00 38.48 ? 3212 VAL A O     1 
ATOM   13797 C CB    . VAL A 1 3212 ? 216.977 124.401 169.989 1.00 38.30 ? 3212 VAL A CB    1 
ATOM   13798 C CG1   . VAL A 1 3212 ? 216.232 123.297 169.256 1.00 36.76 ? 3212 VAL A CG1   1 
ATOM   13799 C CG2   . VAL A 1 3212 ? 216.064 125.060 171.001 1.00 38.08 ? 3212 VAL A CG2   1 
ATOM   13800 N N     . ASP A 1 3213 ? 219.907 123.671 168.918 1.00 40.82 ? 3213 ASP A N     1 
ATOM   13801 C CA    . ASP A 1 3213 ? 220.797 122.943 168.017 1.00 42.67 ? 3213 ASP A CA    1 
ATOM   13802 C C     . ASP A 1 3213 ? 221.774 122.065 168.794 1.00 44.42 ? 3213 ASP A C     1 
ATOM   13803 O O     . ASP A 1 3213 ? 222.011 120.906 168.425 1.00 44.39 ? 3213 ASP A O     1 
ATOM   13804 C CB    . ASP A 1 3213 ? 221.549 123.925 167.119 1.00 43.15 ? 3213 ASP A CB    1 
ATOM   13805 C CG    . ASP A 1 3213 ? 220.626 124.679 166.183 1.00 43.83 ? 3213 ASP A CG    1 
ATOM   13806 O OD1   . ASP A 1 3213 ? 219.492 124.207 165.958 1.00 45.04 ? 3213 ASP A OD1   1 
ATOM   13807 O OD2   . ASP A 1 3213 ? 221.031 125.746 165.674 1.00 44.94 ? 3213 ASP A OD2   1 
ATOM   13808 N N     . GLN A 1 3214 ? 222.344 122.598 169.879 1.00 41.98 ? 3214 GLN A N     1 
ATOM   13809 C CA    . GLN A 1 3214 ? 223.231 121.786 170.713 1.00 43.58 ? 3214 GLN A CA    1 
ATOM   13810 C C     . GLN A 1 3214 ? 222.499 120.586 171.299 1.00 43.67 ? 3214 GLN A C     1 
ATOM   13811 O O     . GLN A 1 3214 ? 223.053 119.483 171.366 1.00 44.48 ? 3214 GLN A O     1 
ATOM   13812 C CB    . GLN A 1 3214 ? 223.838 122.623 171.839 1.00 41.71 ? 3214 GLN A CB    1 
ATOM   13813 C CG    . GLN A 1 3214 ? 224.812 123.678 171.382 1.00 42.21 ? 3214 GLN A CG    1 
ATOM   13814 C CD    . GLN A 1 3214 ? 225.377 124.480 172.538 1.00 45.59 ? 3214 GLN A CD    1 
ATOM   13815 O OE1   . GLN A 1 3214 ? 224.991 124.286 173.691 1.00 46.04 ? 3214 GLN A OE1   1 
ATOM   13816 N NE2   . GLN A 1 3214 ? 226.300 125.386 172.234 1.00 41.85 ? 3214 GLN A NE2   1 
ATOM   13817 N N     . VAL A 1 3215 ? 221.260 120.787 171.748 1.00 41.86 ? 3215 VAL A N     1 
ATOM   13818 C CA    . VAL A 1 3215 ? 220.494 119.693 172.336 1.00 44.64 ? 3215 VAL A CA    1 
ATOM   13819 C C     . VAL A 1 3215 ? 220.198 118.623 171.292 1.00 44.88 ? 3215 VAL A C     1 
ATOM   13820 O O     . VAL A 1 3215 ? 220.284 117.421 171.573 1.00 43.24 ? 3215 VAL A O     1 
ATOM   13821 C CB    . VAL A 1 3215 ? 219.208 120.237 172.981 1.00 45.52 ? 3215 VAL A CB    1 
ATOM   13822 C CG1   . VAL A 1 3215 ? 218.198 119.117 173.190 1.00 44.42 ? 3215 VAL A CG1   1 
ATOM   13823 C CG2   . VAL A 1 3215 ? 219.540 120.928 174.294 1.00 42.78 ? 3215 VAL A CG2   1 
ATOM   13824 N N     . GLU A 1 3216 ? 219.843 119.040 170.074 1.00 48.15 ? 3216 GLU A N     1 
ATOM   13825 C CA    . GLU A 1 3216 ? 219.625 118.078 168.998 1.00 49.53 ? 3216 GLU A CA    1 
ATOM   13826 C C     . GLU A 1 3216 ? 220.895 117.293 168.701 1.00 49.22 ? 3216 GLU A C     1 
ATOM   13827 O O     . GLU A 1 3216 ? 220.842 116.081 168.455 1.00 47.34 ? 3216 GLU A O     1 
ATOM   13828 C CB    . GLU A 1 3216 ? 219.134 118.791 167.738 1.00 49.68 ? 3216 GLU A CB    1 
ATOM   13829 C CG    . GLU A 1 3216 ? 218.711 117.843 166.627 1.00 48.92 ? 3216 GLU A CG    1 
ATOM   13830 C CD    . GLU A 1 3216 ? 218.005 118.552 165.489 1.00 51.26 ? 3216 GLU A CD    1 
ATOM   13831 O OE1   . GLU A 1 3216 ? 218.644 119.397 164.828 1.00 51.07 ? 3216 GLU A OE1   1 
ATOM   13832 O OE2   . GLU A 1 3216 ? 216.812 118.264 165.255 1.00 52.16 ? 3216 GLU A OE2   1 
ATOM   13833 N N     . GLU A 1 3217 ? 222.047 117.967 168.710 1.00 46.75 ? 3217 GLU A N     1 
ATOM   13834 C CA    . GLU A 1 3217 ? 223.311 117.261 168.522 1.00 46.50 ? 3217 GLU A CA    1 
ATOM   13835 C C     . GLU A 1 3217 ? 223.556 116.258 169.643 1.00 47.71 ? 3217 GLU A C     1 
ATOM   13836 O O     . GLU A 1 3217 ? 224.024 115.140 169.396 1.00 45.98 ? 3217 GLU A O     1 
ATOM   13837 C CB    . GLU A 1 3217 ? 224.464 118.261 168.442 1.00 44.20 ? 3217 GLU A CB    1 
ATOM   13838 C CG    . GLU A 1 3217 ? 224.675 118.863 167.066 1.00 44.59 ? 3217 GLU A CG    1 
ATOM   13839 C CD    . GLU A 1 3217 ? 225.821 119.854 167.042 1.00 46.66 ? 3217 GLU A CD    1 
ATOM   13840 O OE1   . GLU A 1 3217 ? 225.658 120.967 167.585 1.00 46.32 ? 3217 GLU A OE1   1 
ATOM   13841 O OE2   . GLU A 1 3217 ? 226.886 119.519 166.482 1.00 47.80 ? 3217 GLU A OE2   1 
ATOM   13842 N N     . LEU A 1 3218 ? 223.247 116.642 170.883 1.00 45.27 ? 3218 LEU A N     1 
ATOM   13843 C CA    . LEU A 1 3218 ? 223.532 115.781 172.027 1.00 46.18 ? 3218 LEU A CA    1 
ATOM   13844 C C     . LEU A 1 3218 ? 222.616 114.562 172.059 1.00 47.81 ? 3218 LEU A C     1 
ATOM   13845 O O     . LEU A 1 3218 ? 223.043 113.471 172.457 1.00 47.19 ? 3218 LEU A O     1 
ATOM   13846 C CB    . LEU A 1 3218 ? 223.407 116.578 173.325 1.00 45.69 ? 3218 LEU A CB    1 
ATOM   13847 C CG    . LEU A 1 3218 ? 224.640 117.378 173.750 1.00 46.03 ? 3218 LEU A CG    1 
ATOM   13848 C CD1   . LEU A 1 3218 ? 224.333 118.235 174.968 1.00 44.95 ? 3218 LEU A CD1   1 
ATOM   13849 C CD2   . LEU A 1 3218 ? 225.813 116.451 174.027 1.00 44.18 ? 3218 LEU A CD2   1 
ATOM   13850 N N     . ARG A 1 3219 ? 221.353 114.726 171.657 1.00 52.12 ? 3219 ARG A N     1 
ATOM   13851 C CA    . ARG A 1 3219 ? 220.405 113.617 171.728 1.00 52.62 ? 3219 ARG A CA    1 
ATOM   13852 C C     . ARG A 1 3219 ? 220.819 112.466 170.820 1.00 51.88 ? 3219 ARG A C     1 
ATOM   13853 O O     . ARG A 1 3219 ? 220.712 111.295 171.203 1.00 51.72 ? 3219 ARG A O     1 
ATOM   13854 C CB    . ARG A 1 3219 ? 218.999 114.098 171.370 1.00 51.56 ? 3219 ARG A CB    1 
ATOM   13855 C CG    . ARG A 1 3219 ? 218.139 114.452 172.572 1.00 52.20 ? 3219 ARG A CG    1 
ATOM   13856 C CD    . ARG A 1 3219 ? 216.836 115.100 172.141 1.00 52.44 ? 3219 ARG A CD    1 
ATOM   13857 N NE    . ARG A 1 3219 ? 217.054 116.367 171.453 1.00 55.40 ? 3219 ARG A NE    1 
ATOM   13858 C CZ    . ARG A 1 3219 ? 216.137 116.989 170.725 1.00 52.36 ? 3219 ARG A CZ    1 
ATOM   13859 N NH1   . ARG A 1 3219 ? 214.929 116.479 170.553 1.00 52.15 ? 3219 ARG A NH1   1 
ATOM   13860 N NH2   . ARG A 1 3219 ? 216.441 118.151 170.154 1.00 46.65 ? 3219 ARG A NH2   1 
ATOM   13861 N N     . ARG A 1 3220 ? 221.288 112.775 169.616 1.00 48.76 ? 3220 ARG A N     1 
ATOM   13862 C CA    . ARG A 1 3220 ? 221.687 111.743 168.668 1.00 49.27 ? 3220 ARG A CA    1 
ATOM   13863 C C     . ARG A 1 3220 ? 223.169 111.415 168.810 1.00 49.11 ? 3220 ARG A C     1 
ATOM   13864 O O     . ARG A 1 3220 ? 223.641 110.385 168.330 0.00 48.32 ? 3220 ARG A O     1 
ATOM   13865 C CB    . ARG A 1 3220 ? 221.376 112.182 167.236 1.00 48.33 ? 3220 ARG A CB    1 
ATOM   13866 C CG    . ARG A 1 3220 ? 219.896 112.402 166.966 1.00 47.96 ? 3220 ARG A CG    1 
ATOM   13867 C CD    . ARG A 1 3220 ? 219.664 112.936 165.563 1.00 49.77 ? 3220 ARG A CD    1 
ATOM   13868 N NE    . ARG A 1 3220 ? 220.414 114.162 165.316 1.00 51.60 ? 3220 ARG A NE    1 
ATOM   13869 C CZ    . ARG A 1 3220 ? 220.147 115.021 164.342 1.00 51.09 ? 3220 ARG A CZ    1 
ATOM   13870 N NH1   . ARG A 1 3220 ? 219.146 114.821 163.500 1.00 47.45 ? 3220 ARG A NH1   1 
ATOM   13871 N NH2   . ARG A 1 3220 ? 220.902 116.107 164.210 1.00 51.01 ? 3220 ARG A NH2   1 
ATOM   13872 N N     . LYS A 1 3471 ? 220.421 112.586 179.130 1.00 44.44 ? 3471 LYS A N     1 
ATOM   13873 C CA    . LYS A 1 3471 ? 219.249 111.832 179.560 1.00 46.32 ? 3471 LYS A CA    1 
ATOM   13874 C C     . LYS A 1 3471 ? 218.014 112.269 178.778 1.00 47.33 ? 3471 LYS A C     1 
ATOM   13875 O O     . LYS A 1 3471 ? 217.834 113.454 178.498 1.00 46.65 ? 3471 LYS A O     1 
ATOM   13876 C CB    . LYS A 1 3471 ? 219.024 112.006 181.064 1.00 45.60 ? 3471 LYS A CB    1 
ATOM   13877 C CG    . LYS A 1 3471 ? 217.941 111.113 181.646 1.00 45.46 ? 3471 LYS A CG    1 
ATOM   13878 C CD    . LYS A 1 3471 ? 217.546 111.568 183.041 1.00 46.89 ? 3471 LYS A CD    1 
ATOM   13879 C CE    . LYS A 1 3471 ? 216.505 110.644 183.651 1.00 46.64 ? 3471 LYS A CE    1 
ATOM   13880 N NZ    . LYS A 1 3471 ? 216.034 111.136 184.975 1.00 45.66 ? 3471 LYS A NZ    1 
ATOM   13881 N N     . VAL A 1 3472 ? 217.167 111.299 178.424 1.00 43.35 ? 3472 VAL A N     1 
ATOM   13882 C CA    . VAL A 1 3472 ? 215.990 111.594 177.611 1.00 43.07 ? 3472 VAL A CA    1 
ATOM   13883 C C     . VAL A 1 3472 ? 214.999 112.455 178.386 1.00 43.25 ? 3472 VAL A C     1 
ATOM   13884 O O     . VAL A 1 3472 ? 214.362 113.353 177.821 1.00 40.20 ? 3472 VAL A O     1 
ATOM   13885 C CB    . VAL A 1 3472 ? 215.343 110.288 177.118 1.00 43.81 ? 3472 VAL A CB    1 
ATOM   13886 C CG1   . VAL A 1 3472 ? 214.241 110.586 176.112 1.00 42.43 ? 3472 VAL A CG1   1 
ATOM   13887 C CG2   . VAL A 1 3472 ? 216.395 109.372 176.511 1.00 40.94 ? 3472 VAL A CG2   1 
ATOM   13888 N N     . ASN A 1 3473 ? 214.841 112.188 179.685 1.00 44.66 ? 3473 ASN A N     1 
ATOM   13889 C CA    . ASN A 1 3473 ? 213.917 112.978 180.495 1.00 45.07 ? 3473 ASN A CA    1 
ATOM   13890 C C     . ASN A 1 3473 ? 214.349 114.438 180.558 1.00 43.50 ? 3473 ASN A C     1 
ATOM   13891 O O     . ASN A 1 3473 ? 213.518 115.346 180.427 1.00 41.41 ? 3473 ASN A O     1 
ATOM   13892 C CB    . ASN A 1 3473 ? 213.818 112.387 181.901 1.00 44.75 ? 3473 ASN A CB    1 
ATOM   13893 C CG    . ASN A 1 3473 ? 213.071 111.068 181.928 1.00 45.76 ? 3473 ASN A CG    1 
ATOM   13894 O OD1   . ASN A 1 3473 ? 212.537 110.624 180.912 1.00 45.41 ? 3473 ASN A OD1   1 
ATOM   13895 N ND2   . ASN A 1 3473 ? 213.034 110.433 183.093 1.00 42.95 ? 3473 ASN A ND2   1 
ATOM   13896 N N     . ARG A 1 3474 ? 215.648 114.682 180.751 1.00 41.64 ? 3474 ARG A N     1 
ATOM   13897 C CA    . ARG A 1 3474 ? 216.153 116.051 180.754 1.00 43.29 ? 3474 ARG A CA    1 
ATOM   13898 C C     . ARG A 1 3474 ? 215.933 116.716 179.403 1.00 40.44 ? 3474 ARG A C     1 
ATOM   13899 O O     . ARG A 1 3474 ? 215.575 117.898 179.336 1.00 38.94 ? 3474 ARG A O     1 
ATOM   13900 C CB    . ARG A 1 3474 ? 217.637 116.066 181.119 1.00 42.00 ? 3474 ARG A CB    1 
ATOM   13901 C CG    . ARG A 1 3474 ? 217.990 115.241 182.344 1.00 42.65 ? 3474 ARG A CG    1 
ATOM   13902 C CD    . ARG A 1 3474 ? 217.416 115.850 183.610 1.00 41.98 ? 3474 ARG A CD    1 
ATOM   13903 N NE    . ARG A 1 3474 ? 217.863 115.141 184.803 1.00 42.99 ? 3474 ARG A NE    1 
ATOM   13904 C CZ    . ARG A 1 3474 ? 217.482 115.438 186.037 1.00 43.94 ? 3474 ARG A CZ    1 
ATOM   13905 N NH1   . ARG A 1 3474 ? 216.642 116.431 186.282 1.00 43.46 ? 3474 ARG A NH1   1 
ATOM   13906 N NH2   . ARG A 1 3474 ? 217.954 114.719 187.052 1.00 42.58 ? 3474 ARG A NH2   1 
ATOM   13907 N N     . SER A 1 3475 ? 216.147 115.970 178.316 1.00 40.08 ? 3475 SER A N     1 
ATOM   13908 C CA    . SER A 1 3475 ? 215.940 116.524 176.983 1.00 42.40 ? 3475 SER A CA    1 
ATOM   13909 C C     . SER A 1 3475 ? 214.486 116.926 176.770 1.00 42.16 ? 3475 SER A C     1 
ATOM   13910 O O     . SER A 1 3475 ? 214.206 118.012 176.255 1.00 41.72 ? 3475 SER A O     1 
ATOM   13911 C CB    . SER A 1 3475 ? 216.379 115.516 175.921 1.00 41.76 ? 3475 SER A CB    1 
ATOM   13912 O OG    . SER A 1 3475 ? 217.773 115.271 175.996 1.00 43.55 ? 3475 SER A OG    1 
ATOM   13913 N N     . THR A 1 3476 ? 213.544 116.068 177.170 1.00 40.87 ? 3476 THR A N     1 
ATOM   13914 C CA    . THR A 1 3476 ? 212.131 116.402 177.016 1.00 41.03 ? 3476 THR A CA    1 
ATOM   13915 C C     . THR A 1 3476 ? 211.744 117.592 177.888 1.00 41.28 ? 3476 THR A C     1 
ATOM   13916 O O     . THR A 1 3476 ? 210.984 118.472 177.455 1.00 39.36 ? 3476 THR A O     1 
ATOM   13917 C CB    . THR A 1 3476 ? 211.264 115.186 177.347 1.00 40.47 ? 3476 THR A CB    1 
ATOM   13918 O OG1   . THR A 1 3476 ? 211.642 114.086 176.510 1.00 38.50 ? 3476 THR A OG1   1 
ATOM   13919 C CG2   . THR A 1 3476 ? 209.791 115.501 177.122 1.00 38.42 ? 3476 THR A CG2   1 
ATOM   13920 N N     . ALA A 1 3477 ? 212.256 117.636 179.121 1.00 36.99 ? 3477 ALA A N     1 
ATOM   13921 C CA    . ALA A 1 3477 ? 211.945 118.749 180.013 1.00 39.24 ? 3477 ALA A CA    1 
ATOM   13922 C C     . ALA A 1 3477 ? 212.449 120.068 179.440 1.00 40.13 ? 3477 ALA A C     1 
ATOM   13923 O O     . ALA A 1 3477 ? 211.720 121.067 179.413 1.00 38.26 ? 3477 ALA A O     1 
ATOM   13924 C CB    . ALA A 1 3477 ? 212.545 118.495 181.396 1.00 36.87 ? 3477 ALA A CB    1 
ATOM   13925 N N     . LEU A 1 3478 ? 213.694 120.088 178.957 1.00 38.73 ? 3478 LEU A N     1 
ATOM   13926 C CA    . LEU A 1 3478 ? 214.213 121.319 178.375 1.00 37.64 ? 3478 LEU A CA    1 
ATOM   13927 C C     . LEU A 1 3478 ? 213.506 121.656 177.069 1.00 38.16 ? 3478 LEU A C     1 
ATOM   13928 O O     . LEU A 1 3478 ? 213.349 122.835 176.746 1.00 39.32 ? 3478 LEU A O     1 
ATOM   13929 C CB    . LEU A 1 3478 ? 215.727 121.227 178.168 1.00 36.21 ? 3478 LEU A CB    1 
ATOM   13930 C CG    . LEU A 1 3478 ? 216.337 120.179 177.235 1.00 39.99 ? 3478 LEU A CG    1 
ATOM   13931 C CD1   . LEU A 1 3478 ? 216.325 120.644 175.789 1.00 35.58 ? 3478 LEU A CD1   1 
ATOM   13932 C CD2   . LEU A 1 3478 ? 217.753 119.843 177.673 1.00 40.00 ? 3478 LEU A CD2   1 
ATOM   13933 N N     . LEU A 1 3479 ? 213.060 120.648 176.315 1.00 34.84 ? 3479 LEU A N     1 
ATOM   13934 C CA    . LEU A 1 3479 ? 212.331 120.917 175.080 1.00 36.83 ? 3479 LEU A CA    1 
ATOM   13935 C C     . LEU A 1 3479 ? 211.013 121.625 175.366 1.00 38.91 ? 3479 LEU A C     1 
ATOM   13936 O O     . LEU A 1 3479 ? 210.688 122.638 174.732 1.00 35.56 ? 3479 LEU A O     1 
ATOM   13937 C CB    . LEU A 1 3479 ? 212.087 119.613 174.321 1.00 37.73 ? 3479 LEU A CB    1 
ATOM   13938 C CG    . LEU A 1 3479 ? 213.173 119.175 173.339 1.00 38.57 ? 3479 LEU A CG    1 
ATOM   13939 C CD1   . LEU A 1 3479 ? 213.005 117.707 172.986 1.00 38.61 ? 3479 LEU A CD1   1 
ATOM   13940 C CD2   . LEU A 1 3479 ? 213.142 120.037 172.088 1.00 34.21 ? 3479 LEU A CD2   1 
ATOM   13941 N N     . LYS A 1 3480 ? 210.239 121.109 176.324 1.00 38.60 ? 3480 LYS A N     1 
ATOM   13942 C CA    . LYS A 1 3480 ? 208.976 121.765 176.652 1.00 39.60 ? 3480 LYS A CA    1 
ATOM   13943 C C     . LYS A 1 3480 ? 209.215 123.134 177.285 1.00 39.40 ? 3480 LYS A C     1 
ATOM   13944 O O     . LYS A 1 3480 ? 208.480 124.092 177.003 1.00 37.60 ? 3480 LYS A O     1 
ATOM   13945 C CB    . LYS A 1 3480 ? 208.121 120.875 177.559 1.00 36.12 ? 3480 LYS A CB    1 
ATOM   13946 C CG    . LYS A 1 3480 ? 208.762 120.465 178.870 1.00 37.02 ? 3480 LYS A CG    1 
ATOM   13947 C CD    . LYS A 1 3480 ? 207.717 119.978 179.862 1.00 38.84 ? 3480 LYS A CD    1 
ATOM   13948 C CE    . LYS A 1 3480 ? 208.329 119.059 180.906 1.00 38.33 ? 3480 LYS A CE    1 
ATOM   13949 N NZ    . LYS A 1 3480 ? 208.682 117.730 180.336 1.00 34.61 ? 3480 LYS A NZ    1 
ATOM   13950 N N     . SER A 1 3481 ? 210.256 123.257 178.116 1.00 37.23 ? 3481 SER A N     1 
ATOM   13951 C CA    . SER A 1 3481 ? 210.572 124.552 178.711 1.00 38.16 ? 3481 SER A CA    1 
ATOM   13952 C C     . SER A 1 3481 ? 210.942 125.577 177.645 1.00 35.69 ? 3481 SER A C     1 
ATOM   13953 O O     . SER A 1 3481 ? 210.515 126.735 177.711 1.00 33.93 ? 3481 SER A O     1 
ATOM   13954 C CB    . SER A 1 3481 ? 211.705 124.400 179.724 1.00 36.64 ? 3481 SER A CB    1 
ATOM   13955 O OG    . SER A 1 3481 ? 212.035 125.651 180.300 1.00 37.82 ? 3481 SER A OG    1 
ATOM   13956 N N     . LEU A 1 3482 ? 211.723 125.170 176.645 1.00 33.79 ? 3482 LEU A N     1 
ATOM   13957 C CA    . LEU A 1 3482 ? 212.137 126.095 175.599 1.00 36.13 ? 3482 LEU A CA    1 
ATOM   13958 C C     . LEU A 1 3482 ? 211.005 126.404 174.628 1.00 38.32 ? 3482 LEU A C     1 
ATOM   13959 O O     . LEU A 1 3482 ? 210.969 127.499 174.061 1.00 38.15 ? 3482 LEU A O     1 
ATOM   13960 C CB    . LEU A 1 3482 ? 213.355 125.536 174.862 1.00 36.24 ? 3482 LEU A CB    1 
ATOM   13961 C CG    . LEU A 1 3482 ? 214.715 126.014 175.386 1.00 36.61 ? 3482 LEU A CG    1 
ATOM   13962 C CD1   . LEU A 1 3482 ? 214.929 125.622 176.841 1.00 32.70 ? 3482 LEU A CD1   1 
ATOM   13963 C CD2   . LEU A 1 3482 ? 215.842 125.467 174.530 1.00 35.56 ? 3482 LEU A CD2   1 
ATOM   13964 N N     . SER A 1 3483 ? 210.066 125.475 174.432 1.00 38.97 ? 3483 SER A N     1 
ATOM   13965 C CA    . SER A 1 3483 ? 208.858 125.811 173.681 1.00 39.80 ? 3483 SER A CA    1 
ATOM   13966 C C     . SER A 1 3483 ? 208.031 126.858 174.420 1.00 38.03 ? 3483 SER A C     1 
ATOM   13967 O O     . SER A 1 3483 ? 207.514 127.808 173.809 1.00 35.75 ? 3483 SER A O     1 
ATOM   13968 C CB    . SER A 1 3483 ? 208.032 124.551 173.425 1.00 37.91 ? 3483 SER A CB    1 
ATOM   13969 O OG    . SER A 1 3483 ? 208.759 123.615 172.649 1.00 36.86 ? 3483 SER A OG    1 
ATOM   13970 N N     . ALA A 1 3484 ? 207.897 126.703 175.741 1.00 36.49 ? 3484 ALA A N     1 
ATOM   13971 C CA    . ALA A 1 3484 ? 207.223 127.724 176.536 1.00 35.85 ? 3484 ALA A CA    1 
ATOM   13972 C C     . ALA A 1 3484 ? 207.957 129.057 176.449 1.00 36.96 ? 3484 ALA A C     1 
ATOM   13973 O O     . ALA A 1 3484 ? 207.329 130.121 176.399 1.00 37.63 ? 3484 ALA A O     1 
ATOM   13974 C CB    . ALA A 1 3484 ? 207.104 127.266 177.989 1.00 34.59 ? 3484 ALA A CB    1 
ATOM   13975 N N     . GLU A 1 3485 ? 209.292 129.014 176.434 1.00 38.50 ? 3485 GLU A N     1 
ATOM   13976 C CA    . GLU A 1 3485 ? 210.080 130.231 176.261 1.00 37.40 ? 3485 GLU A CA    1 
ATOM   13977 C C     . GLU A 1 3485 ? 209.816 130.875 174.905 1.00 36.28 ? 3485 GLU A C     1 
ATOM   13978 O O     . GLU A 1 3485 ? 209.716 132.101 174.803 1.00 34.00 ? 3485 GLU A O     1 
ATOM   13979 C CB    . GLU A 1 3485 ? 211.568 129.921 176.423 1.00 35.65 ? 3485 GLU A CB    1 
ATOM   13980 C CG    . GLU A 1 3485 ? 211.998 129.660 177.854 1.00 35.28 ? 3485 GLU A CG    1 
ATOM   13981 C CD    . GLU A 1 3485 ? 211.929 130.903 178.714 1.00 39.02 ? 3485 GLU A CD    1 
ATOM   13982 O OE1   . GLU A 1 3485 ? 212.165 132.008 178.182 1.00 39.56 ? 3485 GLU A OE1   1 
ATOM   13983 O OE2   . GLU A 1 3485 ? 211.641 130.777 179.922 1.00 41.74 ? 3485 GLU A OE2   1 
ATOM   13984 N N     . ARG A 1 3486 ? 209.714 130.062 173.851 1.00 37.02 ? 3486 ARG A N     1 
ATOM   13985 C CA    . ARG A 1 3486 ? 209.387 130.584 172.526 1.00 38.85 ? 3486 ARG A CA    1 
ATOM   13986 C C     . ARG A 1 3486 ? 208.049 131.309 172.540 1.00 40.26 ? 3486 ARG A C     1 
ATOM   13987 O O     . ARG A 1 3486 ? 207.923 132.421 172.009 1.00 39.14 ? 3486 ARG A O     1 
ATOM   13988 C CB    . ARG A 1 3486 ? 209.358 129.443 171.507 1.00 37.59 ? 3486 ARG A CB    1 
ATOM   13989 C CG    . ARG A 1 3486 ? 210.694 129.105 170.869 1.00 37.63 ? 3486 ARG A CG    1 
ATOM   13990 C CD    . ARG A 1 3486 ? 211.221 130.273 170.056 1.00 39.02 ? 3486 ARG A CD    1 
ATOM   13991 N NE    . ARG A 1 3486 ? 212.647 130.154 169.781 1.00 41.27 ? 3486 ARG A NE    1 
ATOM   13992 C CZ    . ARG A 1 3486 ? 213.606 130.431 170.653 1.00 42.07 ? 3486 ARG A CZ    1 
ATOM   13993 N NH1   . ARG A 1 3486 ? 213.329 130.832 171.883 1.00 38.79 ? 3486 ARG A NH1   1 
ATOM   13994 N NH2   . ARG A 1 3486 ? 214.876 130.303 170.281 1.00 39.37 ? 3486 ARG A NH2   1 
ATOM   13995 N N     . GLU A 1 3487 ? 207.034 130.686 173.142 1.00 41.36 ? 3487 GLU A N     1 
ATOM   13996 C CA    . GLU A 1 3487 ? 205.716 131.317 173.206 1.00 40.13 ? 3487 GLU A CA    1 
ATOM   13997 C C     . GLU A 1 3487 ? 205.767 132.616 174.005 1.00 39.61 ? 3487 GLU A C     1 
ATOM   13998 O O     . GLU A 1 3487 ? 205.245 133.655 173.572 1.00 38.93 ? 3487 GLU A O     1 
ATOM   13999 C CB    . GLU A 1 3487 ? 204.703 130.346 173.813 1.00 37.91 ? 3487 GLU A CB    1 
ATOM   14000 C CG    . GLU A 1 3487 ? 203.264 130.829 173.743 1.00 39.98 ? 3487 GLU A CG    1 
ATOM   14001 C CD    . GLU A 1 3487 ? 202.788 131.426 175.052 1.00 41.60 ? 3487 GLU A CD    1 
ATOM   14002 O OE1   . GLU A 1 3487 ? 203.396 131.122 176.101 1.00 38.79 ? 3487 GLU A OE1   1 
ATOM   14003 O OE2   . GLU A 1 3487 ? 201.807 132.198 175.032 1.00 40.70 ? 3487 GLU A OE2   1 
ATOM   14004 N N     . ARG A 1 3488 ? 206.418 132.581 175.171 1.00 37.17 ? 3488 ARG A N     1 
ATOM   14005 C CA    . ARG A 1 3488 ? 206.518 133.772 176.006 1.00 39.50 ? 3488 ARG A CA    1 
ATOM   14006 C C     . ARG A 1 3488 ? 207.247 134.895 175.283 1.00 40.30 ? 3488 ARG A C     1 
ATOM   14007 O O     . ARG A 1 3488 ? 206.877 136.068 175.404 1.00 34.87 ? 3488 ARG A O     1 
ATOM   14008 C CB    . ARG A 1 3488 ? 207.228 133.429 177.316 1.00 37.18 ? 3488 ARG A CB    1 
ATOM   14009 C CG    . ARG A 1 3488 ? 207.522 134.627 178.200 1.00 35.36 ? 3488 ARG A CG    1 
ATOM   14010 C CD    . ARG A 1 3488 ? 208.553 134.276 179.257 1.00 37.40 ? 3488 ARG A CD    1 
ATOM   14011 N NE    . ARG A 1 3488 ? 209.428 135.403 179.555 1.00 36.98 ? 3488 ARG A NE    1 
ATOM   14012 C CZ    . ARG A 1 3488 ? 210.666 135.286 180.013 1.00 37.21 ? 3488 ARG A CZ    1 
ATOM   14013 N NH1   . ARG A 1 3488 ? 211.208 134.102 180.245 1.00 37.27 ? 3488 ARG A NH1   1 
ATOM   14014 N NH2   . ARG A 1 3488 ? 211.382 136.384 180.236 1.00 35.14 ? 3488 ARG A NH2   1 
ATOM   14015 N N     . TRP A 1 3489 ? 208.269 134.559 174.501 1.00 40.27 ? 3489 TRP A N     1 
ATOM   14016 C CA    . TRP A 1 3489 ? 209.090 135.608 173.919 1.00 37.02 ? 3489 TRP A CA    1 
ATOM   14017 C C     . TRP A 1 3489 ? 208.477 136.159 172.638 1.00 35.08 ? 3489 TRP A C     1 
ATOM   14018 O O     . TRP A 1 3489 ? 208.667 137.339 172.329 1.00 36.85 ? 3489 TRP A O     1 
ATOM   14019 C CB    . TRP A 1 3489 ? 210.503 135.084 173.683 1.00 36.10 ? 3489 TRP A CB    1 
ATOM   14020 C CG    . TRP A 1 3489 ? 211.335 135.232 174.916 1.00 36.60 ? 3489 TRP A CG    1 
ATOM   14021 C CD1   . TRP A 1 3489 ? 210.873 135.379 176.191 1.00 36.13 ? 3489 TRP A CD1   1 
ATOM   14022 C CD2   . TRP A 1 3489 ? 212.762 135.253 175.005 1.00 38.99 ? 3489 TRP A CD2   1 
ATOM   14023 N NE1   . TRP A 1 3489 ? 211.921 135.483 177.068 1.00 37.43 ? 3489 TRP A NE1   1 
ATOM   14024 C CE2   . TRP A 1 3489 ? 213.093 135.411 176.364 1.00 37.46 ? 3489 TRP A CE2   1 
ATOM   14025 C CE3   . TRP A 1 3489 ? 213.792 135.153 174.070 1.00 38.25 ? 3489 TRP A CE3   1 
ATOM   14026 C CZ2   . TRP A 1 3489 ? 214.407 135.469 176.809 1.00 36.96 ? 3489 TRP A CZ2   1 
ATOM   14027 C CZ3   . TRP A 1 3489 ? 215.095 135.215 174.514 1.00 36.41 ? 3489 TRP A CZ3   1 
ATOM   14028 C CH2   . TRP A 1 3489 ? 215.393 135.370 175.870 1.00 38.67 ? 3489 TRP A CH2   1 
ATOM   14029 N N     . GLU A 1 3490 ? 207.709 135.352 171.900 1.00 35.50 ? 3490 GLU A N     1 
ATOM   14030 C CA    . GLU A 1 3490 ? 206.916 135.938 170.823 1.00 37.99 ? 3490 GLU A CA    1 
ATOM   14031 C C     . GLU A 1 3490 ? 205.808 136.828 171.381 1.00 38.39 ? 3490 GLU A C     1 
ATOM   14032 O O     . GLU A 1 3490 ? 205.479 137.862 170.779 1.00 37.70 ? 3490 GLU A O     1 
ATOM   14033 C CB    . GLU A 1 3490 ? 206.348 134.848 169.909 1.00 38.97 ? 3490 GLU A CB    1 
ATOM   14034 C CG    . GLU A 1 3490 ? 205.315 133.930 170.540 1.00 39.59 ? 3490 GLU A CG    1 
ATOM   14035 C CD    . GLU A 1 3490 ? 203.892 134.414 170.331 1.00 42.54 ? 3490 GLU A CD    1 
ATOM   14036 O OE1   . GLU A 1 3490 ? 203.694 135.356 169.535 1.00 42.86 ? 3490 GLU A OE1   1 
ATOM   14037 O OE2   . GLU A 1 3490 ? 202.973 133.855 170.966 1.00 41.37 ? 3490 GLU A OE2   1 
ATOM   14038 N N     . LYS A 1 3491 ? 205.242 136.465 172.539 1.00 35.79 ? 3491 LYS A N     1 
ATOM   14039 C CA    . LYS A 1 3491 ? 204.309 137.370 173.206 1.00 36.52 ? 3491 LYS A CA    1 
ATOM   14040 C C     . LYS A 1 3491 ? 205.005 138.669 173.606 1.00 35.57 ? 3491 LYS A C     1 
ATOM   14041 O O     . LYS A 1 3491 ? 204.434 139.760 173.476 1.00 32.58 ? 3491 LYS A O     1 
ATOM   14042 C CB    . LYS A 1 3491 ? 203.693 136.675 174.424 1.00 35.13 ? 3491 LYS A CB    1 
ATOM   14043 C CG    . LYS A 1 3491 ? 202.423 137.325 174.974 1.00 33.53 ? 3491 LYS A CG    1 
ATOM   14044 C CD    . LYS A 1 3491 ? 202.723 138.493 175.903 1.00 35.11 ? 3491 LYS A CD    1 
ATOM   14045 C CE    . LYS A 1 3491 ? 201.523 139.414 176.043 1.00 35.01 ? 3491 LYS A CE    1 
ATOM   14046 N NZ    . LYS A 1 3491 ? 201.763 140.473 177.061 1.00 33.44 ? 3491 LYS A NZ    1 
ATOM   14047 N N     . THR A 1 3492 ? 206.239 138.569 174.100 1.00 34.93 ? 3492 THR A N     1 
ATOM   14048 C CA    . THR A 1 3492 ? 207.007 139.767 174.424 1.00 31.84 ? 3492 THR A CA    1 
ATOM   14049 C C     . THR A 1 3492 ? 207.242 140.622 173.184 1.00 35.58 ? 3492 THR A C     1 
ATOM   14050 O O     . THR A 1 3492 ? 207.158 141.854 173.245 1.00 37.71 ? 3492 THR A O     1 
ATOM   14051 C CB    . THR A 1 3492 ? 208.338 139.379 175.067 1.00 33.31 ? 3492 THR A CB    1 
ATOM   14052 O OG1   . THR A 1 3492 ? 208.099 138.474 176.153 1.00 38.25 ? 3492 THR A OG1   1 
ATOM   14053 C CG2   . THR A 1 3492 ? 209.059 140.610 175.588 1.00 30.38 ? 3492 THR A CG2   1 
ATOM   14054 N N     . SER A 1 3493 ? 207.542 139.985 172.050 1.00 35.80 ? 3493 SER A N     1 
ATOM   14055 C CA    . SER A 1 3493 ? 207.754 140.730 170.812 1.00 36.04 ? 3493 SER A CA    1 
ATOM   14056 C C     . SER A 1 3493 ? 206.492 141.469 170.382 1.00 36.47 ? 3493 SER A C     1 
ATOM   14057 O O     . SER A 1 3493 ? 206.555 142.634 169.967 1.00 36.57 ? 3493 SER A O     1 
ATOM   14058 C CB    . SER A 1 3493 ? 208.222 139.787 169.703 1.00 33.20 ? 3493 SER A CB    1 
ATOM   14059 O OG    . SER A 1 3493 ? 209.484 139.222 170.009 1.00 34.25 ? 3493 SER A OG    1 
ATOM   14060 N N     . GLU A 1 3494 ? 205.332 140.813 170.469 1.00 36.22 ? 3494 GLU A N     1 
ATOM   14061 C CA    . GLU A 1 3494 ? 204.106 141.502 170.072 1.00 37.71 ? 3494 GLU A CA    1 
ATOM   14062 C C     . GLU A 1 3494 ? 203.748 142.619 171.051 1.00 35.51 ? 3494 GLU A C     1 
ATOM   14063 O O     . GLU A 1 3494 ? 203.230 143.663 170.633 1.00 36.45 ? 3494 GLU A O     1 
ATOM   14064 C CB    . GLU A 1 3494 ? 202.954 140.507 169.907 1.00 36.56 ? 3494 GLU A CB    1 
ATOM   14065 C CG    . GLU A 1 3494 ? 202.497 139.808 171.167 1.00 35.81 ? 3494 GLU A CG    1 
ATOM   14066 C CD    . GLU A 1 3494 ? 201.404 138.792 170.903 1.00 38.19 ? 3494 GLU A CD    1 
ATOM   14067 O OE1   . GLU A 1 3494 ? 200.986 138.657 169.734 1.00 38.77 ? 3494 GLU A OE1   1 
ATOM   14068 O OE2   . GLU A 1 3494 ? 200.965 138.125 171.864 1.00 40.75 ? 3494 GLU A OE2   1 
ATOM   14069 N N     . THR A 1 3495 ? 204.046 142.445 172.342 1.00 32.48 ? 3495 THR A N     1 
ATOM   14070 C CA    . THR A 1 3495 ? 203.868 143.544 173.290 1.00 33.81 ? 3495 THR A CA    1 
ATOM   14071 C C     . THR A 1 3495 ? 204.784 144.717 172.951 1.00 36.21 ? 3495 THR A C     1 
ATOM   14072 O O     . THR A 1 3495 ? 204.382 145.888 173.048 1.00 37.76 ? 3495 THR A O     1 
ATOM   14073 C CB    . THR A 1 3495 ? 204.130 143.056 174.716 1.00 36.07 ? 3495 THR A CB    1 
ATOM   14074 O OG1   . THR A 1 3495 ? 203.176 142.044 175.061 1.00 39.01 ? 3495 THR A OG1   1 
ATOM   14075 C CG2   . THR A 1 3495 ? 204.011 144.204 175.705 1.00 34.06 ? 3495 THR A CG2   1 
ATOM   14076 N N     . PHE A 1 3496 ? 206.025 144.418 172.559 1.00 33.90 ? 3496 PHE A N     1 
ATOM   14077 C CA    . PHE A 1 3496 ? 206.959 145.462 172.151 1.00 35.55 ? 3496 PHE A CA    1 
ATOM   14078 C C     . PHE A 1 3496 ? 206.439 146.212 170.935 1.00 36.00 ? 3496 PHE A C     1 
ATOM   14079 O O     . PHE A 1 3496 ? 206.568 147.438 170.847 1.00 33.43 ? 3496 PHE A O     1 
ATOM   14080 C CB    . PHE A 1 3496 ? 208.324 144.846 171.852 1.00 33.17 ? 3496 PHE A CB    1 
ATOM   14081 C CG    . PHE A 1 3496 ? 209.203 144.700 173.058 1.00 33.16 ? 3496 PHE A CG    1 
ATOM   14082 C CD1   . PHE A 1 3496 ? 208.662 144.704 174.332 1.00 33.89 ? 3496 PHE A CD1   1 
ATOM   14083 C CD2   . PHE A 1 3496 ? 210.570 144.534 172.915 1.00 34.24 ? 3496 PHE A CD2   1 
ATOM   14084 C CE1   . PHE A 1 3496 ? 209.470 144.563 175.442 1.00 35.32 ? 3496 PHE A CE1   1 
ATOM   14085 C CE2   . PHE A 1 3496 ? 211.381 144.389 174.020 1.00 35.38 ? 3496 PHE A CE2   1 
ATOM   14086 C CZ    . PHE A 1 3496 ? 210.832 144.405 175.286 1.00 34.11 ? 3496 PHE A CZ    1 
ATOM   14087 N N     . LYS A 1 3497 ? 205.858 145.485 169.979 1.00 36.22 ? 3497 LYS A N     1 
ATOM   14088 C CA    . LYS A 1 3497 ? 205.229 146.138 168.835 1.00 34.51 ? 3497 LYS A CA    1 
ATOM   14089 C C     . LYS A 1 3497 ? 204.061 147.016 169.266 1.00 33.83 ? 3497 LYS A C     1 
ATOM   14090 O O     . LYS A 1 3497 ? 203.855 148.097 168.702 1.00 32.09 ? 3497 LYS A O     1 
ATOM   14091 C CB    . LYS A 1 3497 ? 204.762 145.097 167.817 1.00 34.62 ? 3497 LYS A CB    1 
ATOM   14092 C CG    . LYS A 1 3497 ? 205.889 144.355 167.115 1.00 35.07 ? 3497 LYS A CG    1 
ATOM   14093 C CD    . LYS A 1 3497 ? 205.364 143.534 165.945 1.00 35.46 ? 3497 LYS A CD    1 
ATOM   14094 C CE    . LYS A 1 3497 ? 204.588 142.316 166.416 1.00 34.86 ? 3497 LYS A CE    1 
ATOM   14095 N NZ    . LYS A 1 3497 ? 205.476 141.311 167.059 1.00 35.18 ? 3497 LYS A NZ    1 
ATOM   14096 N N     . ASN A 1 3498 ? 203.281 146.566 170.252 1.00 34.08 ? 3498 ASN A N     1 
ATOM   14097 C CA    . ASN A 1 3498 ? 202.146 147.357 170.723 1.00 34.07 ? 3498 ASN A CA    1 
ATOM   14098 C C     . ASN A 1 3498 ? 202.595 148.664 171.371 1.00 35.73 ? 3498 ASN A C     1 
ATOM   14099 O O     . ASN A 1 3498 ? 201.951 149.705 171.188 1.00 36.69 ? 3498 ASN A O     1 
ATOM   14100 C CB    . ASN A 1 3498 ? 201.304 146.541 171.704 1.00 34.75 ? 3498 ASN A CB    1 
ATOM   14101 C CG    . ASN A 1 3498 ? 200.742 145.280 171.081 1.00 36.18 ? 3498 ASN A CG    1 
ATOM   14102 O OD1   . ASN A 1 3498 ? 200.616 145.178 169.861 1.00 35.31 ? 3498 ASN A OD1   1 
ATOM   14103 N ND2   . ASN A 1 3498 ? 200.403 144.308 171.920 1.00 34.94 ? 3498 ASN A ND2   1 
ATOM   14104 N N     . GLN A 1 3499 ? 203.684 148.629 172.144 1.00 33.00 ? 3499 GLN A N     1 
ATOM   14105 C CA    . GLN A 1 3499 ? 204.121 149.819 172.880 1.00 33.83 ? 3499 GLN A CA    1 
ATOM   14106 C C     . GLN A 1 3499 ? 204.534 150.969 171.960 1.00 33.58 ? 3499 GLN A C     1 
ATOM   14107 O O     . GLN A 1 3499 ? 204.518 152.140 172.385 1.00 29.45 ? 3499 GLN A O     1 
ATOM   14108 C CB    . GLN A 1 3499 ? 205.278 149.454 173.809 1.00 31.01 ? 3499 GLN A CB    1 
ATOM   14109 C CG    . GLN A 1 3499 ? 204.831 148.945 175.165 1.00 29.68 ? 3499 GLN A CG    1 
ATOM   14110 C CD    . GLN A 1 3499 ? 205.968 148.861 176.159 1.00 33.32 ? 3499 GLN A CD    1 
ATOM   14111 O OE1   . GLN A 1 3499 ? 207.137 148.785 175.780 1.00 35.90 ? 3499 GLN A OE1   1 
ATOM   14112 N NE2   . GLN A 1 3499 ? 205.633 148.880 177.442 1.00 35.04 ? 3499 GLN A NE2   1 
ATOM   14113 N N     . MET A 1 3500 ? 204.918 150.653 170.721 1.00 33.17 ? 3500 MET A N     1 
ATOM   14114 C CA    . MET A 1 3500 ? 205.287 151.680 169.755 1.00 30.74 ? 3500 MET A CA    1 
ATOM   14115 C C     . MET A 1 3500 ? 204.138 152.645 169.510 1.00 31.80 ? 3500 MET A C     1 
ATOM   14116 O O     . MET A 1 3500 ? 204.363 153.841 169.294 1.00 32.57 ? 3500 MET A O     1 
ATOM   14117 C CB    . MET A 1 3500 ? 205.698 151.022 168.437 1.00 32.97 ? 3500 MET A CB    1 
ATOM   14118 C CG    . MET A 1 3500 ? 206.996 150.235 168.493 1.00 34.27 ? 3500 MET A CG    1 
ATOM   14119 S SD    . MET A 1 3500 ? 208.320 151.091 169.357 1.00 41.54 ? 3500 MET A SD    1 
ATOM   14120 C CE    . MET A 1 3500 ? 208.514 152.526 168.311 1.00 30.50 ? 3500 MET A CE    1 
ATOM   14121 N N     . SER A 1 3501 ? 202.903 152.143 169.547 1.00 33.01 ? 3501 SER A N     1 
ATOM   14122 C CA    . SER A 1 3501 ? 201.747 152.982 169.257 1.00 36.81 ? 3501 SER A CA    1 
ATOM   14123 C C     . SER A 1 3501 ? 201.539 154.035 170.335 1.00 35.88 ? 3501 SER A C     1 
ATOM   14124 O O     . SER A 1 3501 ? 200.981 155.105 170.067 1.00 34.15 ? 3501 SER A O     1 
ATOM   14125 C CB    . SER A 1 3501 ? 200.498 152.115 169.112 1.00 34.89 ? 3501 SER A CB    1 
ATOM   14126 O OG    . SER A 1 3501 ? 200.200 151.456 170.330 1.00 33.22 ? 3501 SER A OG    1 
ATOM   14127 N N     . THR A 1 3502 ? 201.982 153.757 171.561 1.00 24.71 ? 3502 THR A N     1 
ATOM   14128 C CA    . THR A 1 3502 ? 201.705 154.648 172.678 1.00 21.05 ? 3502 THR A CA    1 
ATOM   14129 C C     . THR A 1 3502 ? 202.882 155.532 173.066 1.00 21.93 ? 3502 THR A C     1 
ATOM   14130 O O     . THR A 1 3502 ? 202.664 156.536 173.760 1.00 24.57 ? 3502 THR A O     1 
ATOM   14131 C CB    . THR A 1 3502 ? 201.255 153.844 173.906 1.00 22.44 ? 3502 THR A CB    1 
ATOM   14132 O OG1   . THR A 1 3502 ? 200.736 154.740 174.893 1.00 25.20 ? 3502 THR A OG1   1 
ATOM   14133 C CG2   . THR A 1 3502 ? 202.416 153.081 174.509 1.00 23.18 ? 3502 THR A CG2   1 
ATOM   14134 N N     . ILE A 1 3503 ? 204.109 155.188 172.650 1.00 19.52 ? 3503 ILE A N     1 
ATOM   14135 C CA    . ILE A 1 3503 ? 205.272 155.977 173.071 1.00 12.93 ? 3503 ILE A CA    1 
ATOM   14136 C C     . ILE A 1 3503 ? 205.104 157.450 172.705 1.00 10.58 ? 3503 ILE A C     1 
ATOM   14137 O O     . ILE A 1 3503 ? 205.411 158.338 173.507 1.00 16.31 ? 3503 ILE A O     1 
ATOM   14138 C CB    . ILE A 1 3503 ? 206.574 155.409 172.480 1.00 19.62 ? 3503 ILE A CB    1 
ATOM   14139 C CG1   . ILE A 1 3503 ? 206.846 153.998 172.997 1.00 22.63 ? 3503 ILE A CG1   1 
ATOM   14140 C CG2   . ILE A 1 3503 ? 207.740 156.331 172.803 1.00 11.05 ? 3503 ILE A CG2   1 
ATOM   14141 C CD1   . ILE A 1 3503 ? 207.959 153.299 172.261 1.00 20.26 ? 3503 ILE A CD1   1 
ATOM   14142 N N     . ALA A 1 3504 ? 204.621 157.734 171.492 1.00 15.08 ? 3504 ALA A N     1 
ATOM   14143 C CA    . ALA A 1 3504 ? 204.572 159.116 171.014 1.00 11.63 ? 3504 ALA A CA    1 
ATOM   14144 C C     . ALA A 1 3504 ? 203.754 160.007 171.944 1.00 6.27  ? 3504 ALA A C     1 
ATOM   14145 O O     . ALA A 1 3504 ? 204.289 160.928 172.575 1.00 4.57  ? 3504 ALA A O     1 
ATOM   14146 C CB    . ALA A 1 3504 ? 203.999 159.159 169.597 1.00 11.88 ? 3504 ALA A CB    1 
ATOM   14147 N N     . GLY A 1 3505 ? 202.451 159.740 172.047 1.00 9.86  ? 3505 GLY A N     1 
ATOM   14148 C CA    . GLY A 1 3505 ? 201.596 160.571 172.878 1.00 5.95  ? 3505 GLY A CA    1 
ATOM   14149 C C     . GLY A 1 3505 ? 201.935 160.472 174.351 1.00 4.09  ? 3505 GLY A C     1 
ATOM   14150 O O     . GLY A 1 3505 ? 201.745 161.430 175.110 1.00 5.65  ? 3505 GLY A O     1 
ATOM   14151 N N     . ASP A 1 3506 ? 202.456 159.322 174.778 1.00 12.49 ? 3506 ASP A N     1 
ATOM   14152 C CA    . ASP A 1 3506 ? 202.793 159.142 176.180 1.00 8.81  ? 3506 ASP A CA    1 
ATOM   14153 C C     . ASP A 1 3506 ? 203.954 160.050 176.587 1.00 4.54  ? 3506 ASP A C     1 
ATOM   14154 O O     . ASP A 1 3506 ? 203.880 160.762 177.601 1.00 5.99  ? 3506 ASP A O     1 
ATOM   14155 C CB    . ASP A 1 3506 ? 203.121 157.668 176.396 1.00 10.23 ? 3506 ASP A CB    1 
ATOM   14156 C CG    . ASP A 1 3506 ? 203.335 157.328 177.826 1.00 19.54 ? 3506 ASP A CG    1 
ATOM   14157 O OD1   . ASP A 1 3506 ? 202.335 157.262 178.562 1.00 28.25 ? 3506 ASP A OD1   1 
ATOM   14158 O OD2   . ASP A 1 3506 ? 204.485 157.113 178.222 1.00 20.64 ? 3506 ASP A OD2   1 
ATOM   14159 N N     . CYS A 1 3507 ? 205.032 160.055 175.794 1.00 7.06  ? 3507 CYS A N     1 
ATOM   14160 C CA    . CYS A 1 3507 ? 206.126 160.992 176.031 1.00 2.89  ? 3507 CYS A CA    1 
ATOM   14161 C C     . CYS A 1 3507 ? 205.673 162.431 175.827 1.00 2.40  ? 3507 CYS A C     1 
ATOM   14162 O O     . CYS A 1 3507 ? 206.201 163.346 176.467 1.00 6.01  ? 3507 CYS A O     1 
ATOM   14163 C CB    . CYS A 1 3507 ? 207.310 160.674 175.118 1.00 5.10  ? 3507 CYS A CB    1 
ATOM   14164 S SG    . CYS A 1 3507 ? 208.122 159.092 175.423 1.00 24.44 ? 3507 CYS A SG    1 
ATOM   14165 N N     . LEU A 1 3508 ? 204.701 162.655 174.939 1.00 4.96  ? 3508 LEU A N     1 
ATOM   14166 C CA    . LEU A 1 3508 ? 204.140 163.995 174.790 1.00 2.62  ? 3508 LEU A CA    1 
ATOM   14167 C C     . LEU A 1 3508 ? 203.563 164.500 176.105 1.00 6.04  ? 3508 LEU A C     1 
ATOM   14168 O O     . LEU A 1 3508 ? 203.900 165.598 176.564 1.00 5.59  ? 3508 LEU A O     1 
ATOM   14169 C CB    . LEU A 1 3508 ? 203.068 163.988 173.705 1.00 9.31  ? 3508 LEU A CB    1 
ATOM   14170 C CG    . LEU A 1 3508 ? 202.282 165.277 173.487 1.00 0.78  ? 3508 LEU A CG    1 
ATOM   14171 C CD1   . LEU A 1 3508 ? 203.181 166.391 173.010 1.00 7.07  ? 3508 LEU A CD1   1 
ATOM   14172 C CD2   . LEU A 1 3508 ? 201.191 165.003 172.486 1.00 7.37  ? 3508 LEU A CD2   1 
ATOM   14173 N N     . LEU A 1 3509 ? 202.692 163.701 176.725 1.00 10.87 ? 3509 LEU A N     1 
ATOM   14174 C CA    . LEU A 1 3509 ? 202.107 164.095 178.004 1.00 0.03  ? 3509 LEU A CA    1 
ATOM   14175 C C     . LEU A 1 3509 ? 203.176 164.262 179.072 1.00 0.00  ? 3509 LEU A C     1 
ATOM   14176 O O     . LEU A 1 3509 ? 203.133 165.216 179.860 1.00 3.03  ? 3509 LEU A O     1 
ATOM   14177 C CB    . LEU A 1 3509 ? 201.069 163.071 178.458 1.00 7.50  ? 3509 LEU A CB    1 
ATOM   14178 C CG    . LEU A 1 3509 ? 199.808 162.922 177.614 1.00 10.19 ? 3509 LEU A CG    1 
ATOM   14179 C CD1   . LEU A 1 3509 ? 198.869 161.921 178.254 1.00 10.83 ? 3509 LEU A CD1   1 
ATOM   14180 C CD2   . LEU A 1 3509 ? 199.134 164.266 177.480 1.00 11.95 ? 3509 LEU A CD2   1 
ATOM   14181 N N     . SER A 1 3510 ? 204.142 163.342 179.120 1.00 3.49  ? 3510 SER A N     1 
ATOM   14182 C CA    . SER A 1 3510 ? 205.170 163.421 180.153 1.00 2.10  ? 3510 SER A CA    1 
ATOM   14183 C C     . SER A 1 3510 ? 205.996 164.698 180.026 1.00 2.66  ? 3510 SER A C     1 
ATOM   14184 O O     . SER A 1 3510 ? 206.255 165.381 181.025 1.00 5.30  ? 3510 SER A O     1 
ATOM   14185 C CB    . SER A 1 3510 ? 206.066 162.190 180.085 1.00 3.63  ? 3510 SER A CB    1 
ATOM   14186 O OG    . SER A 1 3510 ? 205.333 161.015 180.376 1.00 12.67 ? 3510 SER A OG    1 
ATOM   14187 N N     . ALA A 1 3511 ? 206.406 165.048 178.806 1.00 8.19  ? 3511 ALA A N     1 
ATOM   14188 C CA    . ALA A 1 3511 ? 207.219 166.244 178.616 1.00 2.22  ? 3511 ALA A CA    1 
ATOM   14189 C C     . ALA A 1 3511 ? 206.402 167.511 178.822 1.00 2.84  ? 3511 ALA A C     1 
ATOM   14190 O O     . ALA A 1 3511 ? 206.922 168.513 179.330 1.00 2.06  ? 3511 ALA A O     1 
ATOM   14191 C CB    . ALA A 1 3511 ? 207.849 166.234 177.228 1.00 4.17  ? 3511 ALA A CB    1 
ATOM   14192 N N     . ALA A 1 3512 ? 205.124 167.494 178.432 1.00 8.08  ? 3512 ALA A N     1 
ATOM   14193 C CA    . ALA A 1 3512 ? 204.260 168.633 178.713 1.00 0.00  ? 3512 ALA A CA    1 
ATOM   14194 C C     . ALA A 1 3512 ? 204.103 168.849 180.207 1.00 0.00  ? 3512 ALA A C     1 
ATOM   14195 O O     . ALA A 1 3512 ? 204.033 169.993 180.665 1.00 4.02  ? 3512 ALA A O     1 
ATOM   14196 C CB    . ALA A 1 3512 ? 202.894 168.436 178.058 1.00 2.60  ? 3512 ALA A CB    1 
ATOM   14197 N N     . PHE A 1 3513 ? 204.037 167.768 180.982 1.00 3.22  ? 3513 PHE A N     1 
ATOM   14198 C CA    . PHE A 1 3513 ? 203.987 167.909 182.432 1.00 2.72  ? 3513 PHE A CA    1 
ATOM   14199 C C     . PHE A 1 3513 ? 205.303 168.450 182.978 1.00 4.00  ? 3513 PHE A C     1 
ATOM   14200 O O     . PHE A 1 3513 ? 205.312 169.356 183.819 1.00 6.77  ? 3513 PHE A O     1 
ATOM   14201 C CB    . PHE A 1 3513 ? 203.650 166.567 183.079 1.00 1.85  ? 3513 PHE A CB    1 
ATOM   14202 C CG    . PHE A 1 3513 ? 203.727 166.586 184.576 1.00 5.36  ? 3513 PHE A CG    1 
ATOM   14203 C CD1   . PHE A 1 3513 ? 202.730 167.186 185.324 1.00 2.59  ? 3513 PHE A CD1   1 
ATOM   14204 C CD2   . PHE A 1 3513 ? 204.803 166.017 185.234 1.00 5.51  ? 3513 PHE A CD2   1 
ATOM   14205 C CE1   . PHE A 1 3513 ? 202.800 167.211 186.699 1.00 7.21  ? 3513 PHE A CE1   1 
ATOM   14206 C CE2   . PHE A 1 3513 ? 204.878 166.039 186.611 1.00 4.77  ? 3513 PHE A CE2   1 
ATOM   14207 C CZ    . PHE A 1 3513 ? 203.875 166.636 187.344 1.00 5.61  ? 3513 PHE A CZ    1 
ATOM   14208 N N     . ILE A 1 3514 ? 206.428 167.905 182.513 1.00 4.01  ? 3514 ILE A N     1 
ATOM   14209 C CA    . ILE A 1 3514 ? 207.718 168.278 183.088 1.00 0.08  ? 3514 ILE A CA    1 
ATOM   14210 C C     . ILE A 1 3514 ? 208.051 169.734 182.792 1.00 1.03  ? 3514 ILE A C     1 
ATOM   14211 O O     . ILE A 1 3514 ? 208.439 170.489 183.691 1.00 8.68  ? 3514 ILE A O     1 
ATOM   14212 C CB    . ILE A 1 3514 ? 208.823 167.335 182.583 1.00 2.54  ? 3514 ILE A CB    1 
ATOM   14213 C CG1   . ILE A 1 3514 ? 208.584 165.928 183.121 1.00 5.99  ? 3514 ILE A CG1   1 
ATOM   14214 C CG2   . ILE A 1 3514 ? 210.190 167.844 183.000 1.00 2.67  ? 3514 ILE A CG2   1 
ATOM   14215 C CD1   . ILE A 1 3514 ? 208.554 165.872 184.628 1.00 10.96 ? 3514 ILE A CD1   1 
ATOM   14216 N N     . ALA A 1 3515 ? 207.912 170.155 181.537 1.00 0.82  ? 3515 ALA A N     1 
ATOM   14217 C CA    . ALA A 1 3515 ? 208.359 171.492 181.166 1.00 0.67  ? 3515 ALA A CA    1 
ATOM   14218 C C     . ALA A 1 3515 ? 207.390 172.579 181.604 1.00 3.93  ? 3515 ALA A C     1 
ATOM   14219 O O     . ALA A 1 3515 ? 207.823 173.690 181.927 1.00 6.53  ? 3515 ALA A O     1 
ATOM   14220 C CB    . ALA A 1 3515 ? 208.574 171.576 179.658 1.00 2.75  ? 3515 ALA A CB    1 
ATOM   14221 N N     . TYR A 1 3516 ? 206.091 172.292 181.623 1.00 4.24  ? 3516 TYR A N     1 
ATOM   14222 C CA    . TYR A 1 3516 ? 205.110 173.350 181.833 1.00 1.85  ? 3516 TYR A CA    1 
ATOM   14223 C C     . TYR A 1 3516 ? 204.686 173.421 183.296 1.00 0.23  ? 3516 TYR A C     1 
ATOM   14224 O O     . TYR A 1 3516 ? 204.845 174.458 183.946 1.00 3.28  ? 3516 TYR A O     1 
ATOM   14225 C CB    . TYR A 1 3516 ? 203.891 173.118 180.935 1.00 8.49  ? 3516 TYR A CB    1 
ATOM   14226 C CG    . TYR A 1 3516 ? 203.995 173.787 179.587 1.00 0.78  ? 3516 TYR A CG    1 
ATOM   14227 C CD1   . TYR A 1 3516 ? 203.947 175.164 179.460 1.00 0.74  ? 3516 TYR A CD1   1 
ATOM   14228 C CD2   . TYR A 1 3516 ? 204.115 173.032 178.434 1.00 0.00  ? 3516 TYR A CD2   1 
ATOM   14229 C CE1   . TYR A 1 3516 ? 204.035 175.772 178.231 1.00 0.94  ? 3516 TYR A CE1   1 
ATOM   14230 C CE2   . TYR A 1 3516 ? 204.199 173.630 177.201 1.00 6.61  ? 3516 TYR A CE2   1 
ATOM   14231 C CZ    . TYR A 1 3516 ? 204.162 174.998 177.103 1.00 5.90  ? 3516 TYR A CZ    1 
ATOM   14232 O OH    . TYR A 1 3516 ? 204.249 175.594 175.869 1.00 15.07 ? 3516 TYR A OH    1 
ATOM   14233 N N     . ALA A 1 3517 ? 204.149 172.325 183.823 1.00 7.85  ? 3517 ALA A N     1 
ATOM   14234 C CA    . ALA A 1 3517 ? 203.772 172.272 185.224 1.00 5.87  ? 3517 ALA A CA    1 
ATOM   14235 C C     . ALA A 1 3517 ? 205.014 172.193 186.103 1.00 5.15  ? 3517 ALA A C     1 
ATOM   14236 O O     . ALA A 1 3517 ? 206.126 171.931 185.636 1.00 13.68 ? 3517 ALA A O     1 
ATOM   14237 C CB    . ALA A 1 3517 ? 202.860 171.076 185.495 1.00 0.00  ? 3517 ALA A CB    1 
ATOM   14238 N N     . GLY A 1 3518 ? 204.813 172.421 187.394 1.00 0.28  ? 3518 GLY A N     1 
ATOM   14239 C CA    . GLY A 1 3518 ? 205.921 172.435 188.325 1.00 0.04  ? 3518 GLY A CA    1 
ATOM   14240 C C     . GLY A 1 3518 ? 205.783 173.538 189.346 1.00 5.30  ? 3518 GLY A C     1 
ATOM   14241 O O     . GLY A 1 3518 ? 206.265 173.416 190.475 1.00 14.77 ? 3518 GLY A O     1 
ATOM   14242 N N     . TYR A 1 3519 ? 205.133 174.627 188.950 1.00 6.45  ? 3519 TYR A N     1 
ATOM   14243 C CA    . TYR A 1 3519 ? 204.792 175.694 189.878 1.00 2.59  ? 3519 TYR A CA    1 
ATOM   14244 C C     . TYR A 1 3519 ? 203.390 175.522 190.439 1.00 2.64  ? 3519 TYR A C     1 
ATOM   14245 O O     . TYR A 1 3519 ? 203.103 176.000 191.542 1.00 10.23 ? 3519 TYR A O     1 
ATOM   14246 C CB    . TYR A 1 3519 ? 204.942 177.051 189.180 1.00 2.75  ? 3519 TYR A CB    1 
ATOM   14247 C CG    . TYR A 1 3519 ? 204.561 178.256 190.011 1.00 9.06  ? 3519 TYR A CG    1 
ATOM   14248 C CD1   . TYR A 1 3519 ? 203.237 178.661 190.135 1.00 9.39  ? 3519 TYR A CD1   1 
ATOM   14249 C CD2   . TYR A 1 3519 ? 205.529 178.972 190.698 1.00 10.19 ? 3519 TYR A CD2   1 
ATOM   14250 C CE1   . TYR A 1 3519 ? 202.896 179.755 190.900 1.00 8.39  ? 3519 TYR A CE1   1 
ATOM   14251 C CE2   . TYR A 1 3519 ? 205.196 180.063 191.466 1.00 10.05 ? 3519 TYR A CE2   1 
ATOM   14252 C CZ    . TYR A 1 3519 ? 203.880 180.451 191.563 1.00 10.79 ? 3519 TYR A CZ    1 
ATOM   14253 O OH    . TYR A 1 3519 ? 203.551 181.540 192.330 1.00 17.13 ? 3519 TYR A OH    1 
ATOM   14254 N N     . PHE A 1 3520 ? 202.522 174.829 189.712 1.00 0.42  ? 3520 PHE A N     1 
ATOM   14255 C CA    . PHE A 1 3520 ? 201.160 174.608 190.165 1.00 6.41  ? 3520 PHE A CA    1 
ATOM   14256 C C     . PHE A 1 3520 ? 201.121 173.518 191.230 1.00 4.82  ? 3520 PHE A C     1 
ATOM   14257 O O     . PHE A 1 3520 ? 202.038 172.703 191.353 1.00 10.14 ? 3520 PHE A O     1 
ATOM   14258 C CB    . PHE A 1 3520 ? 200.272 174.232 188.981 1.00 7.30  ? 3520 PHE A CB    1 
ATOM   14259 C CG    . PHE A 1 3520 ? 200.261 175.260 187.885 1.00 5.23  ? 3520 PHE A CG    1 
ATOM   14260 C CD1   . PHE A 1 3520 ? 201.235 175.254 186.900 1.00 6.46  ? 3520 PHE A CD1   1 
ATOM   14261 C CD2   . PHE A 1 3520 ? 199.281 176.235 187.840 1.00 5.60  ? 3520 PHE A CD2   1 
ATOM   14262 C CE1   . PHE A 1 3520 ? 201.231 176.199 185.896 1.00 9.39  ? 3520 PHE A CE1   1 
ATOM   14263 C CE2   . PHE A 1 3520 ? 199.270 177.182 186.836 1.00 8.05  ? 3520 PHE A CE2   1 
ATOM   14264 C CZ    . PHE A 1 3520 ? 200.246 177.163 185.863 1.00 12.26 ? 3520 PHE A CZ    1 
ATOM   14265 N N     . ASP A 1 3521 ? 200.045 173.514 192.011 1.00 4.21  ? 3521 ASP A N     1 
ATOM   14266 C CA    . ASP A 1 3521 ? 199.886 172.521 193.060 1.00 5.80  ? 3521 ASP A CA    1 
ATOM   14267 C C     . ASP A 1 3521 ? 199.423 171.191 192.465 1.00 3.67  ? 3521 ASP A C     1 
ATOM   14268 O O     . ASP A 1 3521 ? 199.241 171.049 191.254 1.00 11.86 ? 3521 ASP A O     1 
ATOM   14269 C CB    . ASP A 1 3521 ? 198.921 173.032 194.128 1.00 9.90  ? 3521 ASP A CB    1 
ATOM   14270 C CG    . ASP A 1 3521 ? 197.535 173.314 193.584 1.00 12.14 ? 3521 ASP A CG    1 
ATOM   14271 O OD1   . ASP A 1 3521 ? 197.325 173.169 192.364 1.00 18.47 ? 3521 ASP A OD1   1 
ATOM   14272 O OD2   . ASP A 1 3521 ? 196.648 173.681 194.381 1.00 9.33  ? 3521 ASP A OD2   1 
ATOM   14273 N N     . GLN A 1 3522 ? 199.232 170.202 193.341 1.00 0.90  ? 3522 GLN A N     1 
ATOM   14274 C CA    . GLN A 1 3522 ? 198.872 168.863 192.883 1.00 6.55  ? 3522 GLN A CA    1 
ATOM   14275 C C     . GLN A 1 3522 ? 197.537 168.863 192.147 1.00 8.00  ? 3522 GLN A C     1 
ATOM   14276 O O     . GLN A 1 3522 ? 197.393 168.205 191.110 1.00 14.49 ? 3522 GLN A O     1 
ATOM   14277 C CB    . GLN A 1 3522 ? 198.833 167.899 194.067 1.00 8.03  ? 3522 GLN A CB    1 
ATOM   14278 C CG    . GLN A 1 3522 ? 198.552 166.459 193.680 1.00 10.53 ? 3522 GLN A CG    1 
ATOM   14279 C CD    . GLN A 1 3522 ? 198.577 165.523 194.866 1.00 13.26 ? 3522 GLN A CD    1 
ATOM   14280 O OE1   . GLN A 1 3522 ? 198.771 165.950 196.002 1.00 20.07 ? 3522 GLN A OE1   1 
ATOM   14281 N NE2   . GLN A 1 3522 ? 198.377 164.236 194.610 1.00 12.82 ? 3522 GLN A NE2   1 
ATOM   14282 N N     . GLN A 1 3523 ? 196.550 169.593 192.668 1.00 4.34  ? 3523 GLN A N     1 
ATOM   14283 C CA    . GLN A 1 3523 ? 195.241 169.632 192.025 1.00 6.14  ? 3523 GLN A CA    1 
ATOM   14284 C C     . GLN A 1 3523 ? 195.337 170.212 190.621 1.00 3.56  ? 3523 GLN A C     1 
ATOM   14285 O O     . GLN A 1 3523 ? 194.773 169.663 189.669 1.00 5.75  ? 3523 GLN A O     1 
ATOM   14286 C CB    . GLN A 1 3523 ? 194.265 170.444 192.874 1.00 8.28  ? 3523 GLN A CB    1 
ATOM   14287 C CG    . GLN A 1 3523 ? 192.805 170.112 192.632 1.00 7.31  ? 3523 GLN A CG    1 
ATOM   14288 C CD    . GLN A 1 3523 ? 191.871 171.002 193.424 1.00 12.89 ? 3523 GLN A CD    1 
ATOM   14289 O OE1   . GLN A 1 3523 ? 192.255 172.084 193.868 1.00 13.57 ? 3523 GLN A OE1   1 
ATOM   14290 N NE2   . GLN A 1 3523 ? 190.634 170.553 193.605 1.00 13.72 ? 3523 GLN A NE2   1 
ATOM   14291 N N     . MET A 1 3524 ? 196.065 171.321 190.470 1.00 2.23  ? 3524 MET A N     1 
ATOM   14292 C CA    . MET A 1 3524 ? 196.176 171.943 189.156 1.00 4.31  ? 3524 MET A CA    1 
ATOM   14293 C C     . MET A 1 3524 ? 197.030 171.111 188.210 1.00 5.71  ? 3524 MET A C     1 
ATOM   14294 O O     . MET A 1 3524 ? 196.725 171.036 187.016 1.00 8.91  ? 3524 MET A O     1 
ATOM   14295 C CB    . MET A 1 3524 ? 196.743 173.355 189.281 1.00 5.54  ? 3524 MET A CB    1 
ATOM   14296 C CG    . MET A 1 3524 ? 196.419 174.234 188.092 1.00 9.64  ? 3524 MET A CG    1 
ATOM   14297 S SD    . MET A 1 3524 ? 194.644 174.303 187.793 1.00 21.12 ? 3524 MET A SD    1 
ATOM   14298 C CE    . MET A 1 3524 ? 194.598 174.309 186.005 1.00 6.58  ? 3524 MET A CE    1 
ATOM   14299 N N     . ARG A 1 3525 ? 198.093 170.482 188.714 1.00 7.26  ? 3525 ARG A N     1 
ATOM   14300 C CA    . ARG A 1 3525 ? 198.882 169.581 187.879 1.00 1.39  ? 3525 ARG A CA    1 
ATOM   14301 C C     . ARG A 1 3525 ? 198.021 168.442 187.350 1.00 3.43  ? 3525 ARG A C     1 
ATOM   14302 O O     . ARG A 1 3525 ? 198.085 168.093 186.165 1.00 11.03 ? 3525 ARG A O     1 
ATOM   14303 C CB    . ARG A 1 3525 ? 200.066 169.026 188.671 1.00 0.00  ? 3525 ARG A CB    1 
ATOM   14304 C CG    . ARG A 1 3525 ? 201.172 170.018 188.965 1.00 0.65  ? 3525 ARG A CG    1 
ATOM   14305 C CD    . ARG A 1 3525 ? 202.183 169.405 189.916 1.00 0.00  ? 3525 ARG A CD    1 
ATOM   14306 N NE    . ARG A 1 3525 ? 203.153 170.372 190.411 1.00 0.00  ? 3525 ARG A NE    1 
ATOM   14307 C CZ    . ARG A 1 3525 ? 204.348 170.053 190.888 1.00 0.00  ? 3525 ARG A CZ    1 
ATOM   14308 N NH1   . ARG A 1 3525 ? 204.761 168.798 190.937 1.00 3.80  ? 3525 ARG A NH1   1 
ATOM   14309 N NH2   . ARG A 1 3525 ? 205.148 171.018 191.331 1.00 2.81  ? 3525 ARG A NH2   1 
ATOM   14310 N N     . GLN A 1 3526 ? 197.196 167.855 188.220 1.00 1.56  ? 3526 GLN A N     1 
ATOM   14311 C CA    . GLN A 1 3526 ? 196.335 166.759 187.792 1.00 0.28  ? 3526 GLN A CA    1 
ATOM   14312 C C     . GLN A 1 3526 ? 195.272 167.237 186.811 1.00 7.29  ? 3526 GLN A C     1 
ATOM   14313 O O     . GLN A 1 3526 ? 194.938 166.525 185.859 1.00 10.17 ? 3526 GLN A O     1 
ATOM   14314 C CB    . GLN A 1 3526 ? 195.689 166.091 189.005 1.00 5.36  ? 3526 GLN A CB    1 
ATOM   14315 C CG    . GLN A 1 3526 ? 194.990 164.785 188.677 1.00 6.45  ? 3526 GLN A CG    1 
ATOM   14316 C CD    . GLN A 1 3526 ? 195.801 163.913 187.740 1.00 12.78 ? 3526 GLN A CD    1 
ATOM   14317 O OE1   . GLN A 1 3526 ? 196.927 163.525 188.053 1.00 14.74 ? 3526 GLN A OE1   1 
ATOM   14318 N NE2   . GLN A 1 3526 ? 195.233 163.602 186.581 1.00 9.51  ? 3526 GLN A NE2   1 
ATOM   14319 N N     . ASN A 1 3527 ? 194.715 168.431 187.033 1.00 5.08  ? 3527 ASN A N     1 
ATOM   14320 C CA    . ASN A 1 3527 ? 193.736 168.969 186.093 1.00 1.56  ? 3527 ASN A CA    1 
ATOM   14321 C C     . ASN A 1 3527 ? 194.360 169.201 184.724 1.00 2.56  ? 3527 ASN A C     1 
ATOM   14322 O O     . ASN A 1 3527 ? 193.761 168.871 183.693 1.00 12.35 ? 3527 ASN A O     1 
ATOM   14323 C CB    . ASN A 1 3527 ? 193.142 170.268 186.635 1.00 4.85  ? 3527 ASN A CB    1 
ATOM   14324 C CG    . ASN A 1 3527 ? 192.338 170.056 187.898 1.00 8.31  ? 3527 ASN A CG    1 
ATOM   14325 O OD1   . ASN A 1 3527 ? 191.788 168.979 188.125 1.00 6.57  ? 3527 ASN A OD1   1 
ATOM   14326 N ND2   . ASN A 1 3527 ? 192.261 171.088 188.730 1.00 10.65 ? 3527 ASN A ND2   1 
ATOM   14327 N N     . LEU A 1 3528 ? 195.570 169.761 184.697 1.00 5.12  ? 3528 LEU A N     1 
ATOM   14328 C CA    . LEU A 1 3528 ? 196.290 169.938 183.442 1.00 2.30  ? 3528 LEU A CA    1 
ATOM   14329 C C     . LEU A 1 3528 ? 196.508 168.606 182.745 1.00 1.66  ? 3528 LEU A C     1 
ATOM   14330 O O     . LEU A 1 3528 ? 196.256 168.473 181.541 1.00 8.45  ? 3528 LEU A O     1 
ATOM   14331 C CB    . LEU A 1 3528 ? 197.635 170.603 183.717 1.00 5.07  ? 3528 LEU A CB    1 
ATOM   14332 C CG    . LEU A 1 3528 ? 197.647 172.052 184.188 1.00 4.44  ? 3528 LEU A CG    1 
ATOM   14333 C CD1   . LEU A 1 3528 ? 199.079 172.514 184.330 1.00 4.05  ? 3528 LEU A CD1   1 
ATOM   14334 C CD2   . LEU A 1 3528 ? 196.887 172.934 183.215 1.00 4.20  ? 3528 LEU A CD2   1 
ATOM   14335 N N     . PHE A 1 3529 ? 196.979 167.606 183.491 1.00 0.00  ? 3529 PHE A N     1 
ATOM   14336 C CA    . PHE A 1 3529 ? 197.295 166.322 182.881 1.00 0.00  ? 3529 PHE A CA    1 
ATOM   14337 C C     . PHE A 1 3529 ? 196.041 165.636 182.353 1.00 2.93  ? 3529 PHE A C     1 
ATOM   14338 O O     . PHE A 1 3529 ? 196.059 165.054 181.264 1.00 6.49  ? 3529 PHE A O     1 
ATOM   14339 C CB    . PHE A 1 3529 ? 198.023 165.432 183.885 1.00 1.13  ? 3529 PHE A CB    1 
ATOM   14340 C CG    . PHE A 1 3529 ? 198.812 164.334 183.247 1.00 5.14  ? 3529 PHE A CG    1 
ATOM   14341 C CD1   . PHE A 1 3529 ? 200.091 164.572 182.779 1.00 1.82  ? 3529 PHE A CD1   1 
ATOM   14342 C CD2   . PHE A 1 3529 ? 198.275 163.070 183.103 1.00 12.21 ? 3529 PHE A CD2   1 
ATOM   14343 C CE1   . PHE A 1 3529 ? 200.820 163.569 182.186 1.00 3.79  ? 3529 PHE A CE1   1 
ATOM   14344 C CE2   . PHE A 1 3529 ? 199.000 162.066 182.509 1.00 10.85 ? 3529 PHE A CE2   1 
ATOM   14345 C CZ    . PHE A 1 3529 ? 200.275 162.313 182.053 1.00 8.32  ? 3529 PHE A CZ    1 
ATOM   14346 N N     . THR A 1 3530 ? 194.936 165.702 183.100 1.00 7.31  ? 3530 THR A N     1 
ATOM   14347 C CA    . THR A 1 3530 ? 193.711 165.062 182.634 1.00 9.39  ? 3530 THR A CA    1 
ATOM   14348 C C     . THR A 1 3530 ? 193.109 165.800 181.443 1.00 6.14  ? 3530 THR A C     1 
ATOM   14349 O O     . THR A 1 3530 ? 192.560 165.159 180.541 1.00 9.05  ? 3530 THR A O     1 
ATOM   14350 C CB    . THR A 1 3530 ? 192.695 164.931 183.776 1.00 9.50  ? 3530 THR A CB    1 
ATOM   14351 O OG1   . THR A 1 3530 ? 191.648 164.035 183.381 1.00 11.22 ? 3530 THR A OG1   1 
ATOM   14352 C CG2   . THR A 1 3530 ? 192.084 166.269 184.149 1.00 6.97  ? 3530 THR A CG2   1 
ATOM   14353 N N     . THR A 1 3531 ? 193.226 167.131 181.397 1.00 6.25  ? 3531 THR A N     1 
ATOM   14354 C CA    . THR A 1 3531 ? 192.769 167.861 180.219 1.00 6.17  ? 3531 THR A CA    1 
ATOM   14355 C C     . THR A 1 3531 ? 193.594 167.492 178.992 1.00 8.94  ? 3531 THR A C     1 
ATOM   14356 O O     . THR A 1 3531 ? 193.039 167.249 177.911 1.00 17.06 ? 3531 THR A O     1 
ATOM   14357 C CB    . THR A 1 3531 ? 192.830 169.366 180.478 1.00 5.49  ? 3531 THR A CB    1 
ATOM   14358 O OG1   . THR A 1 3531 ? 191.799 169.733 181.402 1.00 11.19 ? 3531 THR A OG1   1 
ATOM   14359 C CG2   . THR A 1 3531 ? 192.636 170.141 179.186 1.00 4.46  ? 3531 THR A CG2   1 
ATOM   14360 N N     . TRP A 1 3532 ? 194.919 167.425 179.144 1.00 6.14  ? 3532 TRP A N     1 
ATOM   14361 C CA    . TRP A 1 3532 ? 195.769 167.049 178.020 1.00 4.97  ? 3532 TRP A CA    1 
ATOM   14362 C C     . TRP A 1 3532 ? 195.473 165.627 177.562 1.00 10.05 ? 3532 TRP A C     1 
ATOM   14363 O O     . TRP A 1 3532 ? 195.436 165.348 176.358 1.00 11.30 ? 3532 TRP A O     1 
ATOM   14364 C CB    . TRP A 1 3532 ? 197.242 167.184 178.400 1.00 7.49  ? 3532 TRP A CB    1 
ATOM   14365 C CG    . TRP A 1 3532 ? 197.658 168.572 178.744 1.00 4.20  ? 3532 TRP A CG    1 
ATOM   14366 C CD1   . TRP A 1 3532 ? 197.107 169.731 178.287 1.00 2.78  ? 3532 TRP A CD1   1 
ATOM   14367 C CD2   . TRP A 1 3532 ? 198.731 168.950 179.610 1.00 0.00  ? 3532 TRP A CD2   1 
ATOM   14368 N NE1   . TRP A 1 3532 ? 197.765 170.809 178.824 1.00 3.39  ? 3532 TRP A NE1   1 
ATOM   14369 C CE2   . TRP A 1 3532 ? 198.767 170.355 179.640 1.00 6.07  ? 3532 TRP A CE2   1 
ATOM   14370 C CE3   . TRP A 1 3532 ? 199.662 168.235 180.366 1.00 0.00  ? 3532 TRP A CE3   1 
ATOM   14371 C CZ2   . TRP A 1 3532 ? 199.699 171.059 180.395 1.00 9.56  ? 3532 TRP A CZ2   1 
ATOM   14372 C CZ3   . TRP A 1 3532 ? 200.583 168.934 181.115 1.00 0.00  ? 3532 TRP A CZ3   1 
ATOM   14373 C CH2   . TRP A 1 3532 ? 200.596 170.332 181.124 1.00 0.61  ? 3532 TRP A CH2   1 
ATOM   14374 N N     . SER A 1 3533 ? 195.268 164.711 178.511 1.00 8.21  ? 3533 SER A N     1 
ATOM   14375 C CA    . SER A 1 3533 ? 194.969 163.329 178.157 1.00 10.82 ? 3533 SER A CA    1 
ATOM   14376 C C     . SER A 1 3533 ? 193.629 163.219 177.443 1.00 11.32 ? 3533 SER A C     1 
ATOM   14377 O O     . SER A 1 3533 ? 193.491 162.448 176.486 1.00 20.47 ? 3533 SER A O     1 
ATOM   14378 C CB    . SER A 1 3533 ? 194.986 162.456 179.410 1.00 14.95 ? 3533 SER A CB    1 
ATOM   14379 O OG    . SER A 1 3533 ? 193.918 162.787 180.277 1.00 18.63 ? 3533 SER A OG    1 
ATOM   14380 N N     . HIS A 1 3534 ? 192.626 163.974 177.898 1.00 6.34  ? 3534 HIS A N     1 
ATOM   14381 C CA    . HIS A 1 3534 ? 191.336 163.964 177.221 1.00 14.46 ? 3534 HIS A CA    1 
ATOM   14382 C C     . HIS A 1 3534 ? 191.463 164.502 175.803 1.00 12.49 ? 3534 HIS A C     1 
ATOM   14383 O O     . HIS A 1 3534 ? 190.867 163.956 174.867 1.00 18.77 ? 3534 HIS A O     1 
ATOM   14384 C CB    . HIS A 1 3534 ? 190.316 164.776 178.018 1.00 13.46 ? 3534 HIS A CB    1 
ATOM   14385 C CG    . HIS A 1 3534 ? 189.046 165.049 177.274 1.00 19.50 ? 3534 HIS A CG    1 
ATOM   14386 N ND1   . HIS A 1 3534 ? 188.505 166.311 177.162 1.00 19.40 ? 3534 HIS A ND1   1 
ATOM   14387 C CD2   . HIS A 1 3534 ? 188.208 164.220 176.607 1.00 22.33 ? 3534 HIS A CD2   1 
ATOM   14388 C CE1   . HIS A 1 3534 ? 187.388 166.248 176.458 1.00 19.14 ? 3534 HIS A CE1   1 
ATOM   14389 N NE2   . HIS A 1 3534 ? 187.186 164.991 176.108 1.00 23.93 ? 3534 HIS A NE2   1 
ATOM   14390 N N     . HIS A 1 3535 ? 192.245 165.567 175.622 1.00 8.76  ? 3535 HIS A N     1 
ATOM   14391 C CA    . HIS A 1 3535 ? 192.448 166.104 174.281 1.00 14.00 ? 3535 HIS A CA    1 
ATOM   14392 C C     . HIS A 1 3535 ? 193.161 165.098 173.384 1.00 15.73 ? 3535 HIS A C     1 
ATOM   14393 O O     . HIS A 1 3535 ? 192.807 164.947 172.209 1.00 18.09 ? 3535 HIS A O     1 
ATOM   14394 C CB    . HIS A 1 3535 ? 193.234 167.410 174.353 1.00 11.87 ? 3535 HIS A CB    1 
ATOM   14395 C CG    . HIS A 1 3535 ? 193.775 167.867 173.034 1.00 11.61 ? 3535 HIS A CG    1 
ATOM   14396 N ND1   . HIS A 1 3535 ? 193.018 168.574 172.125 1.00 11.58 ? 3535 HIS A ND1   1 
ATOM   14397 C CD2   . HIS A 1 3535 ? 194.998 167.721 172.472 1.00 10.54 ? 3535 HIS A CD2   1 
ATOM   14398 C CE1   . HIS A 1 3535 ? 193.751 168.845 171.061 1.00 12.51 ? 3535 HIS A CE1   1 
ATOM   14399 N NE2   . HIS A 1 3535 ? 194.956 168.337 171.245 1.00 12.97 ? 3535 HIS A NE2   1 
ATOM   14400 N N     . LEU A 1 3536 ? 194.173 164.408 173.915 1.00 14.35 ? 3536 LEU A N     1 
ATOM   14401 C CA    . LEU A 1 3536 ? 194.903 163.430 173.113 1.00 12.63 ? 3536 LEU A CA    1 
ATOM   14402 C C     . LEU A 1 3536 ? 194.026 162.241 172.740 1.00 15.87 ? 3536 LEU A C     1 
ATOM   14403 O O     . LEU A 1 3536 ? 194.070 161.770 171.598 1.00 19.64 ? 3536 LEU A O     1 
ATOM   14404 C CB    . LEU A 1 3536 ? 196.152 162.954 173.854 1.00 14.35 ? 3536 LEU A CB    1 
ATOM   14405 C CG    . LEU A 1 3536 ? 197.474 163.606 173.449 1.00 11.74 ? 3536 LEU A CG    1 
ATOM   14406 C CD1   . LEU A 1 3536 ? 197.460 165.093 173.753 1.00 13.85 ? 3536 LEU A CD1   1 
ATOM   14407 C CD2   . LEU A 1 3536 ? 198.642 162.917 174.131 1.00 8.63  ? 3536 LEU A CD2   1 
ATOM   14408 N N     . GLN A 1 3537 ? 193.227 161.733 173.683 1.00 13.23 ? 3537 GLN A N     1 
ATOM   14409 C CA    . GLN A 1 3537 ? 192.390 160.580 173.368 1.00 19.26 ? 3537 GLN A CA    1 
ATOM   14410 C C     . GLN A 1 3537 ? 191.259 160.972 172.429 1.00 22.48 ? 3537 GLN A C     1 
ATOM   14411 O O     . GLN A 1 3537 ? 190.804 160.157 171.617 1.00 21.21 ? 3537 GLN A O     1 
ATOM   14412 C CB    . GLN A 1 3537 ? 191.825 159.947 174.640 1.00 16.48 ? 3537 GLN A CB    1 
ATOM   14413 C CG    . GLN A 1 3537 ? 190.867 160.831 175.414 1.00 17.60 ? 3537 GLN A CG    1 
ATOM   14414 C CD    . GLN A 1 3537 ? 190.378 160.185 176.692 1.00 25.10 ? 3537 GLN A CD    1 
ATOM   14415 O OE1   . GLN A 1 3537 ? 190.713 159.039 176.988 1.00 24.70 ? 3537 GLN A OE1   1 
ATOM   14416 N NE2   . GLN A 1 3537 ? 189.576 160.917 177.456 1.00 22.36 ? 3537 GLN A NE2   1 
ATOM   14417 N N     . GLN A 1 3538 ? 190.791 162.218 172.523 1.00 24.71 ? 3538 GLN A N     1 
ATOM   14418 C CA    . GLN A 1 3538 ? 189.707 162.651 171.653 1.00 25.42 ? 3538 GLN A CA    1 
ATOM   14419 C C     . GLN A 1 3538 ? 190.201 162.829 170.223 1.00 25.34 ? 3538 GLN A C     1 
ATOM   14420 O O     . GLN A 1 3538 ? 189.429 162.655 169.274 1.00 32.04 ? 3538 GLN A O     1 
ATOM   14421 C CB    . GLN A 1 3538 ? 189.085 163.938 172.201 1.00 21.60 ? 3538 GLN A CB    1 
ATOM   14422 C CG    . GLN A 1 3538 ? 187.762 164.328 171.562 1.00 25.40 ? 3538 GLN A CG    1 
ATOM   14423 C CD    . GLN A 1 3538 ? 187.092 165.493 172.268 1.00 32.27 ? 3538 GLN A CD    1 
ATOM   14424 O OE1   . GLN A 1 3538 ? 187.411 165.810 173.415 1.00 30.57 ? 3538 GLN A OE1   1 
ATOM   14425 N NE2   . GLN A 1 3538 ? 186.158 166.140 171.582 1.00 31.36 ? 3538 GLN A NE2   1 
ATOM   14426 N N     . ALA A 1 3539 ? 191.485 163.151 170.050 1.00 18.87 ? 3539 ALA A N     1 
ATOM   14427 C CA    . ALA A 1 3539 ? 192.123 163.204 168.738 1.00 19.14 ? 3539 ALA A CA    1 
ATOM   14428 C C     . ALA A 1 3539 ? 192.769 161.887 168.337 1.00 22.56 ? 3539 ALA A C     1 
ATOM   14429 O O     . ALA A 1 3539 ? 193.424 161.833 167.290 1.00 21.95 ? 3539 ALA A O     1 
ATOM   14430 C CB    . ALA A 1 3539 ? 193.186 164.301 168.701 1.00 18.11 ? 3539 ALA A CB    1 
ATOM   14431 N N     . ASN A 1 3540 ? 192.622 160.844 169.149 1.00 22.46 ? 3540 ASN A N     1 
ATOM   14432 C CA    . ASN A 1 3540 ? 193.171 159.518 168.879 1.00 22.45 ? 3540 ASN A CA    1 
ATOM   14433 C C     . ASN A 1 3540 ? 194.676 159.536 168.649 1.00 21.31 ? 3540 ASN A C     1 
ATOM   14434 O O     . ASN A 1 3540 ? 195.186 158.797 167.802 1.00 23.86 ? 3540 ASN A O     1 
ATOM   14435 C CB    . ASN A 1 3540 ? 192.462 158.855 167.696 1.00 24.47 ? 3540 ASN A CB    1 
ATOM   14436 C CG    . ASN A 1 3540 ? 190.998 158.597 167.973 1.00 26.75 ? 3540 ASN A CG    1 
ATOM   14437 O OD1   . ASN A 1 3540 ? 190.124 159.178 167.338 1.00 27.03 ? 3540 ASN A OD1   1 
ATOM   14438 N ND2   . ASN A 1 3540 ? 190.724 157.722 168.933 1.00 23.80 ? 3540 ASN A ND2   1 
ATOM   14439 N N     . ILE A 1 3541 ? 195.401 160.370 169.387 1.00 17.37 ? 3541 ILE A N     1 
ATOM   14440 C CA    . ILE A 1 3541 ? 196.841 160.198 169.526 1.00 17.31 ? 3541 ILE A CA    1 
ATOM   14441 C C     . ILE A 1 3541 ? 197.065 159.123 170.580 1.00 17.41 ? 3541 ILE A C     1 
ATOM   14442 O O     . ILE A 1 3541 ? 196.880 159.366 171.777 1.00 17.21 ? 3541 ILE A O     1 
ATOM   14443 C CB    . ILE A 1 3541 ? 197.530 161.514 169.908 1.00 19.75 ? 3541 ILE A CB    1 
ATOM   14444 C CG1   . ILE A 1 3541 ? 197.128 162.627 168.939 1.00 18.35 ? 3541 ILE A CG1   1 
ATOM   14445 C CG2   . ILE A 1 3541 ? 199.036 161.335 169.932 1.00 16.60 ? 3541 ILE A CG2   1 
ATOM   14446 C CD1   . ILE A 1 3541 ? 196.992 163.981 169.590 1.00 20.18 ? 3541 ILE A CD1   1 
ATOM   14447 N N     . GLN A 1 3542 ? 197.442 157.927 170.133 1.00 20.73 ? 3542 GLN A N     1 
ATOM   14448 C CA    . GLN A 1 3542 ? 197.457 156.753 171.000 1.00 21.63 ? 3542 GLN A CA    1 
ATOM   14449 C C     . GLN A 1 3542 ? 198.433 156.966 172.149 1.00 22.58 ? 3542 GLN A C     1 
ATOM   14450 O O     . GLN A 1 3542 ? 199.650 157.006 171.946 1.00 22.69 ? 3542 GLN A O     1 
ATOM   14451 C CB    . GLN A 1 3542 ? 197.825 155.507 170.198 1.00 22.82 ? 3542 GLN A CB    1 
ATOM   14452 C CG    . GLN A 1 3542 ? 196.793 155.069 169.161 1.00 24.29 ? 3542 GLN A CG    1 
ATOM   14453 C CD    . GLN A 1 3542 ? 195.355 155.269 169.612 1.00 26.11 ? 3542 GLN A CD    1 
ATOM   14454 O OE1   . GLN A 1 3542 ? 194.546 155.853 168.891 1.00 24.73 ? 3542 GLN A OE1   1 
ATOM   14455 N NE2   . GLN A 1 3542 ? 195.020 154.748 170.788 1.00 25.03 ? 3542 GLN A NE2   1 
ATOM   14456 N N     . PHE A 1 3543 ? 197.892 157.114 173.353 1.00 20.96 ? 3543 PHE A N     1 
ATOM   14457 C CA    . PHE A 1 3543 ? 198.668 157.125 174.582 1.00 19.21 ? 3543 PHE A CA    1 
ATOM   14458 C C     . PHE A 1 3543 ? 198.032 156.144 175.554 1.00 21.79 ? 3543 PHE A C     1 
ATOM   14459 O O     . PHE A 1 3543 ? 196.803 156.047 175.637 1.00 23.88 ? 3543 PHE A O     1 
ATOM   14460 C CB    . PHE A 1 3543 ? 198.741 158.528 175.198 1.00 17.37 ? 3543 PHE A CB    1 
ATOM   14461 C CG    . PHE A 1 3543 ? 197.495 158.940 175.924 1.00 17.49 ? 3543 PHE A CG    1 
ATOM   14462 C CD1   . PHE A 1 3543 ? 196.376 159.350 175.224 1.00 17.38 ? 3543 PHE A CD1   1 
ATOM   14463 C CD2   . PHE A 1 3543 ? 197.440 158.910 177.305 1.00 16.11 ? 3543 PHE A CD2   1 
ATOM   14464 C CE1   . PHE A 1 3543 ? 195.229 159.728 175.887 1.00 16.71 ? 3543 PHE A CE1   1 
ATOM   14465 C CE2   . PHE A 1 3543 ? 196.296 159.284 177.973 1.00 15.07 ? 3543 PHE A CE2   1 
ATOM   14466 C CZ    . PHE A 1 3543 ? 195.189 159.694 177.262 1.00 16.09 ? 3543 PHE A CZ    1 
ATOM   14467 N N     . ARG A 1 3544 ? 198.868 155.404 176.274 1.00 19.98 ? 3544 ARG A N     1 
ATOM   14468 C CA    . ARG A 1 3544 ? 198.354 154.378 177.168 1.00 25.35 ? 3544 ARG A CA    1 
ATOM   14469 C C     . ARG A 1 3544 ? 197.670 155.006 178.377 1.00 26.27 ? 3544 ARG A C     1 
ATOM   14470 O O     . ARG A 1 3544 ? 198.137 156.003 178.935 1.00 24.86 ? 3544 ARG A O     1 
ATOM   14471 C CB    . ARG A 1 3544 ? 199.483 153.431 177.588 1.00 23.87 ? 3544 ARG A CB    1 
ATOM   14472 C CG    . ARG A 1 3544 ? 200.359 153.885 178.742 1.00 21.67 ? 3544 ARG A CG    1 
ATOM   14473 C CD    . ARG A 1 3544 ? 201.816 153.555 178.437 1.00 25.66 ? 3544 ARG A CD    1 
ATOM   14474 N NE    . ARG A 1 3544 ? 202.725 153.941 179.509 1.00 25.38 ? 3544 ARG A NE    1 
ATOM   14475 C CZ    . ARG A 1 3544 ? 203.078 153.148 180.511 1.00 25.07 ? 3544 ARG A CZ    1 
ATOM   14476 N NH1   . ARG A 1 3544 ? 202.622 151.910 180.606 1.00 22.09 ? 3544 ARG A NH1   1 
ATOM   14477 N NH2   . ARG A 1 3544 ? 203.914 153.606 181.438 1.00 25.15 ? 3544 ARG A NH2   1 
ATOM   14478 N N     . THR A 1 3545 ? 196.537 154.424 178.764 1.00 33.44 ? 3545 THR A N     1 
ATOM   14479 C CA    . THR A 1 3545 ? 195.764 154.929 179.886 1.00 30.79 ? 3545 THR A CA    1 
ATOM   14480 C C     . THR A 1 3545 ? 196.437 154.532 181.197 1.00 28.27 ? 3545 THR A C     1 
ATOM   14481 O O     . THR A 1 3545 ? 197.585 154.085 181.221 1.00 30.56 ? 3545 THR A O     1 
ATOM   14482 C CB    . THR A 1 3545 ? 194.330 154.408 179.825 1.00 35.64 ? 3545 THR A CB    1 
ATOM   14483 O OG1   . THR A 1 3545 ? 194.330 152.982 179.968 1.00 32.45 ? 3545 THR A OG1   1 
ATOM   14484 C CG2   . THR A 1 3545 ? 193.684 154.780 178.499 1.00 32.11 ? 3545 THR A CG2   1 
ATOM   14485 N N     . ASP A 1 3546 ? 195.712 154.752 182.300 1.00 29.02 ? 3546 ASP A N     1 
ATOM   14486 C CA    . ASP A 1 3546 ? 196.134 154.487 183.678 1.00 30.84 ? 3546 ASP A CA    1 
ATOM   14487 C C     . ASP A 1 3546 ? 197.625 154.746 183.867 1.00 30.33 ? 3546 ASP A C     1 
ATOM   14488 O O     . ASP A 1 3546 ? 198.345 153.947 184.474 1.00 32.48 ? 3546 ASP A O     1 
ATOM   14489 C CB    . ASP A 1 3546 ? 195.708 153.074 184.129 1.00 30.32 ? 3546 ASP A CB    1 
ATOM   14490 C CG    . ASP A 1 3546 ? 196.394 151.933 183.371 1.00 34.03 ? 3546 ASP A CG    1 
ATOM   14491 O OD1   . ASP A 1 3546 ? 197.452 152.112 182.744 1.00 32.38 ? 3546 ASP A OD1   1 
ATOM   14492 O OD2   . ASP A 1 3546 ? 195.840 150.815 183.407 1.00 37.65 ? 3546 ASP A OD2   1 
ATOM   14493 N N     . ILE A 1 3547 ? 198.075 155.890 183.365 1.00 21.83 ? 3547 ILE A N     1 
ATOM   14494 C CA    . ILE A 1 3547 ? 199.487 156.247 183.356 1.00 16.69 ? 3547 ILE A CA    1 
ATOM   14495 C C     . ILE A 1 3547 ? 199.945 156.556 184.773 1.00 20.82 ? 3547 ILE A C     1 
ATOM   14496 O O     . ILE A 1 3547 ? 199.156 157.001 185.615 1.00 24.77 ? 3547 ILE A O     1 
ATOM   14497 C CB    . ILE A 1 3547 ? 199.729 157.449 182.430 1.00 17.94 ? 3547 ILE A CB    1 
ATOM   14498 C CG1   . ILE A 1 3547 ? 201.226 157.691 182.230 1.00 19.99 ? 3547 ILE A CG1   1 
ATOM   14499 C CG2   . ILE A 1 3547 ? 199.045 158.684 182.977 1.00 19.88 ? 3547 ILE A CG2   1 
ATOM   14500 C CD1   . ILE A 1 3547 ? 201.536 158.649 181.119 1.00 16.58 ? 3547 ILE A CD1   1 
ATOM   14501 N N     . ALA A 1 3548 ? 201.220 156.299 185.042 1.00 20.81 ? 3548 ALA A N     1 
ATOM   14502 C CA    . ALA A 1 3548 ? 201.896 156.810 186.226 1.00 15.55 ? 3548 ALA A CA    1 
ATOM   14503 C C     . ALA A 1 3548 ? 203.066 157.663 185.755 1.00 10.16 ? 3548 ALA A C     1 
ATOM   14504 O O     . ALA A 1 3548 ? 204.031 157.143 185.187 1.00 13.89 ? 3548 ALA A O     1 
ATOM   14505 C CB    . ALA A 1 3548 ? 202.365 155.668 187.121 1.00 15.58 ? 3548 ALA A CB    1 
ATOM   14506 N N     . ARG A 1 3549 ? 202.977 158.976 185.977 1.00 10.81 ? 3549 ARG A N     1 
ATOM   14507 C CA    . ARG A 1 3549 ? 204.057 159.869 185.570 1.00 13.31 ? 3549 ARG A CA    1 
ATOM   14508 C C     . ARG A 1 3549 ? 205.348 159.521 186.298 1.00 11.61 ? 3549 ARG A C     1 
ATOM   14509 O O     . ARG A 1 3549 ? 206.433 159.500 185.701 1.00 17.60 ? 3549 ARG A O     1 
ATOM   14510 C CB    . ARG A 1 3549 ? 203.668 161.321 185.849 1.00 11.45 ? 3549 ARG A CB    1 
ATOM   14511 C CG    . ARG A 1 3549 ? 202.477 161.831 185.063 1.00 5.66  ? 3549 ARG A CG    1 
ATOM   14512 C CD    . ARG A 1 3549 ? 202.259 163.312 185.329 1.00 9.08  ? 3549 ARG A CD    1 
ATOM   14513 N NE    . ARG A 1 3549 ? 201.795 163.587 186.683 1.00 5.76  ? 3549 ARG A NE    1 
ATOM   14514 C CZ    . ARG A 1 3549 ? 200.521 163.633 187.047 1.00 8.25  ? 3549 ARG A CZ    1 
ATOM   14515 N NH1   . ARG A 1 3549 ? 199.546 163.415 186.181 1.00 9.50  ? 3549 ARG A NH1   1 
ATOM   14516 N NH2   . ARG A 1 3549 ? 200.217 163.907 188.311 1.00 11.47 ? 3549 ARG A NH2   1 
ATOM   14517 N N     . THR A 1 3550 ? 205.239 159.227 187.596 1.00 6.66  ? 3550 THR A N     1 
ATOM   14518 C CA    . THR A 1 3550 ? 206.418 159.043 188.433 1.00 4.96  ? 3550 THR A CA    1 
ATOM   14519 C C     . THR A 1 3550 ? 207.275 157.877 187.958 1.00 16.79 ? 3550 THR A C     1 
ATOM   14520 O O     . THR A 1 3550 ? 208.506 157.982 187.917 1.00 19.38 ? 3550 THR A O     1 
ATOM   14521 C CB    . THR A 1 3550 ? 205.998 158.837 189.887 1.00 13.86 ? 3550 THR A CB    1 
ATOM   14522 O OG1   . THR A 1 3550 ? 204.939 159.746 190.214 1.00 19.99 ? 3550 THR A OG1   1 
ATOM   14523 C CG2   . THR A 1 3550 ? 207.172 159.070 190.821 1.00 17.76 ? 3550 THR A CG2   1 
ATOM   14524 N N     . GLU A 1 3551 ? 206.648 156.755 187.598 1.00 18.96 ? 3551 GLU A N     1 
ATOM   14525 C CA    . GLU A 1 3551 ? 207.434 155.579 187.244 1.00 15.32 ? 3551 GLU A CA    1 
ATOM   14526 C C     . GLU A 1 3551 ? 207.702 155.493 185.747 1.00 18.80 ? 3551 GLU A C     1 
ATOM   14527 O O     . GLU A 1 3551 ? 208.525 154.677 185.318 1.00 25.20 ? 3551 GLU A O     1 
ATOM   14528 C CB    . GLU A 1 3551 ? 206.749 154.311 187.748 1.00 15.09 ? 3551 GLU A CB    1 
ATOM   14529 C CG    . GLU A 1 3551 ? 206.319 154.398 189.199 1.00 22.04 ? 3551 GLU A CG    1 
ATOM   14530 C CD    . GLU A 1 3551 ? 206.248 153.041 189.867 1.00 22.21 ? 3551 GLU A CD    1 
ATOM   14531 O OE1   . GLU A 1 3551 ? 206.158 152.027 189.148 1.00 20.19 ? 3551 GLU A OE1   1 
ATOM   14532 O OE2   . GLU A 1 3551 ? 206.303 152.987 191.113 1.00 21.71 ? 3551 GLU A OE2   1 
ATOM   14533 N N     . TYR A 1 3552 ? 207.020 156.301 184.934 1.00 12.11 ? 3552 TYR A N     1 
ATOM   14534 C CA    . TYR A 1 3552 ? 207.438 156.414 183.542 1.00 11.74 ? 3552 TYR A CA    1 
ATOM   14535 C C     . TYR A 1 3552 ? 208.648 157.327 183.411 1.00 8.28  ? 3552 TYR A C     1 
ATOM   14536 O O     . TYR A 1 3552 ? 209.501 157.112 182.544 1.00 16.47 ? 3552 TYR A O     1 
ATOM   14537 C CB    . TYR A 1 3552 ? 206.294 156.922 182.664 1.00 13.36 ? 3552 TYR A CB    1 
ATOM   14538 C CG    . TYR A 1 3552 ? 206.644 156.954 181.190 1.00 11.83 ? 3552 TYR A CG    1 
ATOM   14539 C CD1   . TYR A 1 3552 ? 206.701 155.783 180.446 1.00 12.33 ? 3552 TYR A CD1   1 
ATOM   14540 C CD2   . TYR A 1 3552 ? 206.918 158.152 180.541 1.00 9.35  ? 3552 TYR A CD2   1 
ATOM   14541 C CE1   . TYR A 1 3552 ? 207.023 155.801 179.103 1.00 12.38 ? 3552 TYR A CE1   1 
ATOM   14542 C CE2   . TYR A 1 3552 ? 207.242 158.179 179.196 1.00 8.75  ? 3552 TYR A CE2   1 
ATOM   14543 C CZ    . TYR A 1 3552 ? 207.297 157.000 178.484 1.00 12.68 ? 3552 TYR A CZ    1 
ATOM   14544 O OH    . TYR A 1 3552 ? 207.605 157.018 177.145 1.00 12.75 ? 3552 TYR A OH    1 
ATOM   14545 N N     . LEU A 1 3553 ? 208.748 158.334 184.274 1.00 4.55  ? 3553 LEU A N     1 
ATOM   14546 C CA    . LEU A 1 3553 ? 209.854 159.276 184.224 1.00 8.74  ? 3553 LEU A CA    1 
ATOM   14547 C C     . LEU A 1 3553 ? 210.948 158.963 185.234 1.00 15.15 ? 3553 LEU A C     1 
ATOM   14548 O O     . LEU A 1 3553 ? 211.835 159.797 185.443 1.00 20.37 ? 3553 LEU A O     1 
ATOM   14549 C CB    . LEU A 1 3553 ? 209.332 160.699 184.435 1.00 13.50 ? 3553 LEU A CB    1 
ATOM   14550 C CG    . LEU A 1 3553 ? 208.279 161.141 183.416 1.00 9.97  ? 3553 LEU A CG    1 
ATOM   14551 C CD1   . LEU A 1 3553 ? 207.588 162.422 183.848 1.00 4.06  ? 3553 LEU A CD1   1 
ATOM   14552 C CD2   . LEU A 1 3553 ? 208.913 161.305 182.051 1.00 10.42 ? 3553 LEU A CD2   1 
ATOM   14553 N N     . SER A 1 3554 ? 210.908 157.790 185.863 1.00 12.70 ? 3554 SER A N     1 
ATOM   14554 C CA    . SER A 1 3554 ? 211.959 157.360 186.774 1.00 14.08 ? 3554 SER A CA    1 
ATOM   14555 C C     . SER A 1 3554 ? 211.917 155.844 186.900 1.00 19.79 ? 3554 SER A C     1 
ATOM   14556 O O     . SER A 1 3554 ? 210.889 155.211 186.651 1.00 20.20 ? 3554 SER A O     1 
ATOM   14557 C CB    . SER A 1 3554 ? 211.811 158.022 188.148 1.00 18.47 ? 3554 SER A CB    1 
ATOM   14558 O OG    . SER A 1 3554 ? 210.626 157.589 188.793 1.00 25.60 ? 3554 SER A OG    1 
ATOM   14559 N N     . ASN A 1 3555 ? 213.047 155.263 187.299 1.00 22.58 ? 3555 ASN A N     1 
ATOM   14560 C CA    . ASN A 1 3555 ? 213.144 153.832 187.541 1.00 21.94 ? 3555 ASN A CA    1 
ATOM   14561 C C     . ASN A 1 3555 ? 213.273 153.564 189.040 1.00 25.68 ? 3555 ASN A C     1 
ATOM   14562 O O     . ASN A 1 3555 ? 213.206 154.473 189.869 1.00 19.60 ? 3555 ASN A O     1 
ATOM   14563 C CB    . ASN A 1 3555 ? 214.315 153.221 186.765 1.00 20.83 ? 3555 ASN A CB    1 
ATOM   14564 C CG    . ASN A 1 3555 ? 214.013 153.051 185.289 1.00 29.11 ? 3555 ASN A CG    1 
ATOM   14565 O OD1   . ASN A 1 3555 ? 212.926 152.612 184.913 1.00 29.60 ? 3555 ASN A OD1   1 
ATOM   14566 N ND2   . ASN A 1 3555 ? 214.978 153.396 184.444 1.00 28.02 ? 3555 ASN A ND2   1 
ATOM   14567 N N     . ALA A 1 3556 ? 213.466 152.287 189.387 1.00 31.31 ? 3556 ALA A N     1 
ATOM   14568 C CA    . ALA A 1 3556 ? 213.422 151.874 190.788 1.00 28.06 ? 3556 ALA A CA    1 
ATOM   14569 C C     . ALA A 1 3556 ? 214.584 152.443 191.589 1.00 26.24 ? 3556 ALA A C     1 
ATOM   14570 O O     . ALA A 1 3556 ? 214.387 152.961 192.694 1.00 25.69 ? 3556 ALA A O     1 
ATOM   14571 C CB    . ALA A 1 3556 ? 213.431 150.350 190.890 1.00 27.38 ? 3556 ALA A CB    1 
ATOM   14572 N N     . ASP A 1 3557 ? 215.804 152.341 191.060 1.00 25.91 ? 3557 ASP A N     1 
ATOM   14573 C CA    . ASP A 1 3557 ? 216.970 152.719 191.850 1.00 26.85 ? 3557 ASP A CA    1 
ATOM   14574 C C     . ASP A 1 3557 ? 217.048 154.228 192.054 1.00 26.24 ? 3557 ASP A C     1 
ATOM   14575 O O     . ASP A 1 3557 ? 217.484 154.688 193.114 1.00 28.98 ? 3557 ASP A O     1 
ATOM   14576 C CB    . ASP A 1 3557 ? 218.246 152.177 191.204 1.00 29.48 ? 3557 ASP A CB    1 
ATOM   14577 C CG    . ASP A 1 3557 ? 218.375 152.562 189.749 1.00 31.24 ? 3557 ASP A CG    1 
ATOM   14578 O OD1   . ASP A 1 3557 ? 217.402 153.108 189.191 1.00 31.47 ? 3557 ASP A OD1   1 
ATOM   14579 O OD2   . ASP A 1 3557 ? 219.451 152.315 189.164 1.00 29.52 ? 3557 ASP A OD2   1 
ATOM   14580 N N     . GLU A 1 3558 ? 216.624 155.018 191.063 1.00 25.51 ? 3558 GLU A N     1 
ATOM   14581 C CA    . GLU A 1 3558 ? 216.623 156.467 191.249 1.00 25.13 ? 3558 GLU A CA    1 
ATOM   14582 C C     . GLU A 1 3558 ? 215.651 156.880 192.347 1.00 24.43 ? 3558 GLU A C     1 
ATOM   14583 O O     . GLU A 1 3558 ? 215.997 157.680 193.224 1.00 24.78 ? 3558 GLU A O     1 
ATOM   14584 C CB    . GLU A 1 3558 ? 216.274 157.181 189.943 1.00 27.64 ? 3558 GLU A CB    1 
ATOM   14585 C CG    . GLU A 1 3558 ? 217.350 157.109 188.875 1.00 28.45 ? 3558 GLU A CG    1 
ATOM   14586 C CD    . GLU A 1 3558 ? 217.142 155.953 187.925 1.00 29.96 ? 3558 GLU A CD    1 
ATOM   14587 O OE1   . GLU A 1 3558 ? 216.093 155.290 188.036 1.00 28.13 ? 3558 GLU A OE1   1 
ATOM   14588 O OE2   . GLU A 1 3558 ? 218.024 155.704 187.077 1.00 29.62 ? 3558 GLU A OE2   1 
ATOM   14589 N N     . ARG A 1 3559 ? 214.434 156.334 192.321 1.00 25.90 ? 3559 ARG A N     1 
ATOM   14590 C CA    . ARG A 1 3559 ? 213.468 156.626 193.374 1.00 20.20 ? 3559 ARG A CA    1 
ATOM   14591 C C     . ARG A 1 3559 ? 213.977 156.159 194.729 1.00 24.88 ? 3559 ARG A C     1 
ATOM   14592 O O     . ARG A 1 3559 ? 213.804 156.851 195.738 1.00 26.71 ? 3559 ARG A O     1 
ATOM   14593 C CB    . ARG A 1 3559 ? 212.129 155.959 193.063 1.00 21.36 ? 3559 ARG A CB    1 
ATOM   14594 C CG    . ARG A 1 3559 ? 211.523 156.328 191.729 1.00 22.24 ? 3559 ARG A CG    1 
ATOM   14595 C CD    . ARG A 1 3559 ? 210.003 156.281 191.787 1.00 18.75 ? 3559 ARG A CD    1 
ATOM   14596 N NE    . ARG A 1 3559 ? 209.490 154.955 191.458 1.00 22.22 ? 3559 ARG A NE    1 
ATOM   14597 C CZ    . ARG A 1 3559 ? 209.689 154.318 190.310 1.00 24.02 ? 3559 ARG A CZ    1 
ATOM   14598 N NH1   . ARG A 1 3559 ? 210.313 154.891 189.296 1.00 22.02 ? 3559 ARG A NH1   1 
ATOM   14599 N NH2   . ARG A 1 3559 ? 209.243 153.074 190.174 1.00 25.90 ? 3559 ARG A NH2   1 
ATOM   14600 N N     . LEU A 1 3560 ? 214.593 154.976 194.775 1.00 28.31 ? 3560 LEU A N     1 
ATOM   14601 C CA    . LEU A 1 3560 ? 215.067 154.448 196.049 1.00 26.69 ? 3560 LEU A CA    1 
ATOM   14602 C C     . LEU A 1 3560 ? 216.184 155.310 196.623 1.00 28.25 ? 3560 LEU A C     1 
ATOM   14603 O O     . LEU A 1 3560 ? 216.189 155.606 197.824 1.00 28.52 ? 3560 LEU A O     1 
ATOM   14604 C CB    . LEU A 1 3560 ? 215.530 153.002 195.880 1.00 25.56 ? 3560 LEU A CB    1 
ATOM   14605 C CG    . LEU A 1 3560 ? 215.993 152.290 197.152 1.00 27.94 ? 3560 LEU A CG    1 
ATOM   14606 C CD1   . LEU A 1 3560 ? 214.850 152.178 198.150 1.00 27.42 ? 3560 LEU A CD1   1 
ATOM   14607 C CD2   . LEU A 1 3560 ? 216.560 150.920 196.828 1.00 29.21 ? 3560 LEU A CD2   1 
ATOM   14608 N N     . ARG A 1 3561 ? 217.133 155.738 195.785 1.00 27.31 ? 3561 ARG A N     1 
ATOM   14609 C CA    . ARG A 1 3561 ? 218.186 156.618 196.276 1.00 24.82 ? 3561 ARG A CA    1 
ATOM   14610 C C     . ARG A 1 3561 ? 217.617 157.975 196.669 1.00 22.23 ? 3561 ARG A C     1 
ATOM   14611 O O     . ARG A 1 3561 ? 218.113 158.615 197.605 1.00 27.90 ? 3561 ARG A O     1 
ATOM   14612 C CB    . ARG A 1 3561 ? 219.300 156.766 195.235 1.00 24.52 ? 3561 ARG A CB    1 
ATOM   14613 C CG    . ARG A 1 3561 ? 220.088 158.070 195.350 1.00 26.43 ? 3561 ARG A CG    1 
ATOM   14614 C CD    . ARG A 1 3561 ? 221.188 158.215 194.300 1.00 27.26 ? 3561 ARG A CD    1 
ATOM   14615 N NE    . ARG A 1 3561 ? 220.821 157.768 192.961 1.00 29.42 ? 3561 ARG A NE    1 
ATOM   14616 C CZ    . ARG A 1 3561 ? 219.968 158.394 192.162 1.00 31.00 ? 3561 ARG A CZ    1 
ATOM   14617 N NH1   . ARG A 1 3561 ? 219.389 159.528 192.519 1.00 26.96 ? 3561 ARG A NH1   1 
ATOM   14618 N NH2   . ARG A 1 3561 ? 219.712 157.882 190.963 1.00 31.39 ? 3561 ARG A NH2   1 
ATOM   14619 N N     . TRP A 1 3562 ? 216.562 158.422 195.982 1.00 21.45 ? 3562 TRP A N     1 
ATOM   14620 C CA    . TRP A 1 3562 ? 215.896 159.656 196.382 1.00 25.47 ? 3562 TRP A CA    1 
ATOM   14621 C C     . TRP A 1 3562 ? 215.332 159.530 197.789 1.00 24.96 ? 3562 TRP A C     1 
ATOM   14622 O O     . TRP A 1 3562 ? 215.553 160.398 198.641 1.00 25.81 ? 3562 TRP A O     1 
ATOM   14623 C CB    . TRP A 1 3562 ? 214.777 159.995 195.399 1.00 26.57 ? 3562 TRP A CB    1 
ATOM   14624 C CG    . TRP A 1 3562 ? 215.231 160.597 194.116 1.00 25.20 ? 3562 TRP A CG    1 
ATOM   14625 C CD1   . TRP A 1 3562 ? 216.419 161.220 193.873 1.00 23.26 ? 3562 TRP A CD1   1 
ATOM   14626 C CD2   . TRP A 1 3562 ? 214.483 160.669 192.900 1.00 26.04 ? 3562 TRP A CD2   1 
ATOM   14627 N NE1   . TRP A 1 3562 ? 216.465 161.655 192.571 1.00 23.91 ? 3562 TRP A NE1   1 
ATOM   14628 C CE2   . TRP A 1 3562 ? 215.285 161.331 191.954 1.00 22.34 ? 3562 TRP A CE2   1 
ATOM   14629 C CE3   . TRP A 1 3562 ? 213.212 160.229 192.517 1.00 24.39 ? 3562 TRP A CE3   1 
ATOM   14630 C CZ2   . TRP A 1 3562 ? 214.861 161.564 190.651 1.00 20.65 ? 3562 TRP A CZ2   1 
ATOM   14631 C CZ3   . TRP A 1 3562 ? 212.794 160.459 191.224 1.00 20.91 ? 3562 TRP A CZ3   1 
ATOM   14632 C CH2   . TRP A 1 3562 ? 213.614 161.121 190.307 1.00 21.18 ? 3562 TRP A CH2   1 
ATOM   14633 N N     . GLN A 1 3563 ? 214.600 158.444 198.051 1.00 24.75 ? 3563 GLN A N     1 
ATOM   14634 C CA    . GLN A 1 3563 ? 214.042 158.233 199.385 1.00 28.74 ? 3563 GLN A CA    1 
ATOM   14635 C C     . GLN A 1 3563 ? 215.146 158.103 200.424 1.00 31.92 ? 3563 GLN A C     1 
ATOM   14636 O O     . GLN A 1 3563 ? 214.991 158.556 201.565 1.00 31.68 ? 3563 GLN A O     1 
ATOM   14637 C CB    . GLN A 1 3563 ? 213.141 156.998 199.409 1.00 28.12 ? 3563 GLN A CB    1 
ATOM   14638 C CG    . GLN A 1 3563 ? 212.131 156.922 198.280 1.00 29.93 ? 3563 GLN A CG    1 
ATOM   14639 C CD    . GLN A 1 3563 ? 211.082 158.012 198.356 1.00 31.68 ? 3563 GLN A CD    1 
ATOM   14640 O OE1   . GLN A 1 3563 ? 210.730 158.475 199.441 1.00 32.39 ? 3563 GLN A OE1   1 
ATOM   14641 N NE2   . GLN A 1 3563 ? 210.578 158.429 197.201 1.00 26.19 ? 3563 GLN A NE2   1 
ATOM   14642 N N     . ALA A 1 3564 ? 216.265 157.478 200.051 1.00 32.00 ? 3564 ALA A N     1 
ATOM   14643 C CA    . ALA A 1 3564 ? 217.396 157.375 200.966 1.00 31.56 ? 3564 ALA A CA    1 
ATOM   14644 C C     . ALA A 1 3564 ? 217.956 158.749 201.310 1.00 29.25 ? 3564 ALA A C     1 
ATOM   14645 O O     . ALA A 1 3564 ? 218.325 159.007 202.462 1.00 29.83 ? 3564 ALA A O     1 
ATOM   14646 C CB    . ALA A 1 3564 ? 218.484 156.490 200.360 1.00 28.25 ? 3564 ALA A CB    1 
ATOM   14647 N N     . SER A 1 3565 ? 218.025 159.644 200.330 1.00 24.63 ? 3565 SER A N     1 
ATOM   14648 C CA    . SER A 1 3565 ? 218.601 160.973 200.532 1.00 26.24 ? 3565 SER A CA    1 
ATOM   14649 C C     . SER A 1 3565 ? 217.546 161.997 200.944 1.00 27.75 ? 3565 SER A C     1 
ATOM   14650 O O     . SER A 1 3565 ? 217.473 163.094 200.395 1.00 27.55 ? 3565 SER A O     1 
ATOM   14651 C CB    . SER A 1 3565 ? 219.328 161.418 199.268 1.00 28.24 ? 3565 SER A CB    1 
ATOM   14652 O OG    . SER A 1 3565 ? 218.462 161.394 198.147 1.00 26.46 ? 3565 SER A OG    1 
ATOM   14653 N N     . SER A 1 3566 ? 216.725 161.637 201.934 1.00 26.05 ? 3566 SER A N     1 
ATOM   14654 C CA    . SER A 1 3566 ? 215.784 162.555 202.579 1.00 25.24 ? 3566 SER A CA    1 
ATOM   14655 C C     . SER A 1 3566 ? 214.787 163.147 201.580 1.00 28.80 ? 3566 SER A C     1 
ATOM   14656 O O     . SER A 1 3566 ? 214.800 164.342 201.278 1.00 28.53 ? 3566 SER A O     1 
ATOM   14657 C CB    . SER A 1 3566 ? 216.533 163.662 203.329 1.00 27.07 ? 3566 SER A CB    1 
ATOM   14658 O OG    . SER A 1 3566 ? 217.116 164.588 202.430 1.00 26.87 ? 3566 SER A OG    1 
ATOM   14659 N N     . LEU A 1 3567 ? 213.913 162.282 201.065 1.00 31.21 ? 3567 LEU A N     1 
ATOM   14660 C CA    . LEU A 1 3567 ? 212.804 162.711 200.225 1.00 28.14 ? 3567 LEU A CA    1 
ATOM   14661 C C     . LEU A 1 3567 ? 211.506 162.195 200.832 1.00 28.89 ? 3567 LEU A C     1 
ATOM   14662 O O     . LEU A 1 3567 ? 211.400 160.994 201.136 1.00 29.17 ? 3567 LEU A O     1 
ATOM   14663 C CB    . LEU A 1 3567 ? 212.947 162.202 198.787 1.00 25.21 ? 3567 LEU A CB    1 
ATOM   14664 C CG    . LEU A 1 3567 ? 211.883 162.686 197.796 1.00 24.74 ? 3567 LEU A CG    1 
ATOM   14665 C CD1   . LEU A 1 3567 ? 211.972 164.193 197.610 1.00 25.00 ? 3567 LEU A CD1   1 
ATOM   14666 C CD2   . LEU A 1 3567 ? 211.992 161.973 196.459 1.00 24.16 ? 3567 LEU A CD2   1 
ATOM   14667 N N     . PRO A 1 3568 ? 210.506 163.050 201.029 1.00 24.52 ? 3568 PRO A N     1 
ATOM   14668 C CA    . PRO A 1 3568 ? 209.210 162.563 201.511 1.00 26.01 ? 3568 PRO A CA    1 
ATOM   14669 C C     . PRO A 1 3568 ? 208.556 161.631 200.504 1.00 22.81 ? 3568 PRO A C     1 
ATOM   14670 O O     . PRO A 1 3568 ? 208.757 161.742 199.293 1.00 24.28 ? 3568 PRO A O     1 
ATOM   14671 C CB    . PRO A 1 3568 ? 208.391 163.847 201.699 1.00 27.67 ? 3568 PRO A CB    1 
ATOM   14672 C CG    . PRO A 1 3568 ? 209.405 164.947 201.769 1.00 22.86 ? 3568 PRO A CG    1 
ATOM   14673 C CD    . PRO A 1 3568 ? 210.530 164.514 200.890 1.00 20.22 ? 3568 PRO A CD    1 
ATOM   14674 N N     . ALA A 1 3569 ? 207.761 160.697 201.028 1.00 21.89 ? 3569 ALA A N     1 
ATOM   14675 C CA    . ALA A 1 3569 ? 207.119 159.691 200.191 1.00 22.50 ? 3569 ALA A CA    1 
ATOM   14676 C C     . ALA A 1 3569 ? 205.958 160.246 199.378 1.00 24.76 ? 3569 ALA A C     1 
ATOM   14677 O O     . ALA A 1 3569 ? 205.399 159.512 198.556 1.00 25.37 ? 3569 ALA A O     1 
ATOM   14678 C CB    . ALA A 1 3569 ? 206.633 158.525 201.053 1.00 23.14 ? 3569 ALA A CB    1 
ATOM   14679 N N     . ASP A 1 3570 ? 205.579 161.505 199.592 1.00 22.08 ? 3570 ASP A N     1 
ATOM   14680 C CA    . ASP A 1 3570 ? 204.460 162.088 198.864 1.00 22.21 ? 3570 ASP A CA    1 
ATOM   14681 C C     . ASP A 1 3570 ? 204.758 162.134 197.371 1.00 20.08 ? 3570 ASP A C     1 
ATOM   14682 O O     . ASP A 1 3570 ? 205.905 162.316 196.953 1.00 20.43 ? 3570 ASP A O     1 
ATOM   14683 C CB    . ASP A 1 3570 ? 204.164 163.494 199.384 1.00 23.32 ? 3570 ASP A CB    1 
ATOM   14684 C CG    . ASP A 1 3570 ? 202.898 164.081 198.791 1.00 25.37 ? 3570 ASP A CG    1 
ATOM   14685 O OD1   . ASP A 1 3570 ? 202.070 163.307 198.266 1.00 24.16 ? 3570 ASP A OD1   1 
ATOM   14686 O OD2   . ASP A 1 3570 ? 202.731 165.318 198.845 1.00 17.75 ? 3570 ASP A OD2   1 
ATOM   14687 N N     . ASP A 1 3571 ? 203.709 161.963 196.563 1.00 14.79 ? 3571 ASP A N     1 
ATOM   14688 C CA    . ASP A 1 3571 ? 203.888 161.929 195.116 1.00 19.69 ? 3571 ASP A CA    1 
ATOM   14689 C C     . ASP A 1 3571 ? 204.345 163.275 194.570 1.00 18.86 ? 3571 ASP A C     1 
ATOM   14690 O O     . ASP A 1 3571 ? 205.056 163.324 193.559 1.00 22.28 ? 3571 ASP A O     1 
ATOM   14691 C CB    . ASP A 1 3571 ? 202.590 161.482 194.440 1.00 20.82 ? 3571 ASP A CB    1 
ATOM   14692 C CG    . ASP A 1 3571 ? 201.511 162.548 194.476 1.00 21.98 ? 3571 ASP A CG    1 
ATOM   14693 O OD1   . ASP A 1 3571 ? 200.596 162.434 195.318 1.00 21.22 ? 3571 ASP A OD1   1 
ATOM   14694 O OD2   . ASP A 1 3571 ? 201.565 163.488 193.654 1.00 24.66 ? 3571 ASP A OD2   1 
ATOM   14695 N N     . LEU A 1 3572 ? 203.947 164.374 195.214 1.00 13.41 ? 3572 LEU A N     1 
ATOM   14696 C CA    . LEU A 1 3572 ? 204.378 165.692 194.760 1.00 13.01 ? 3572 LEU A CA    1 
ATOM   14697 C C     . LEU A 1 3572 ? 205.890 165.836 194.861 1.00 13.75 ? 3572 LEU A C     1 
ATOM   14698 O O     . LEU A 1 3572 ? 206.531 166.381 193.956 1.00 19.13 ? 3572 LEU A O     1 
ATOM   14699 C CB    . LEU A 1 3572 ? 203.666 166.782 195.564 1.00 19.73 ? 3572 LEU A CB    1 
ATOM   14700 C CG    . LEU A 1 3572 ? 203.862 168.242 195.147 1.00 18.33 ? 3572 LEU A CG    1 
ATOM   14701 C CD1   . LEU A 1 3572 ? 202.571 169.013 195.330 1.00 17.90 ? 3572 LEU A CD1   1 
ATOM   14702 C CD2   . LEU A 1 3572 ? 204.970 168.892 195.953 1.00 16.90 ? 3572 LEU A CD2   1 
ATOM   14703 N N     . CYS A 1 3573 ? 206.479 165.346 195.954 1.00 13.99 ? 3573 CYS A N     1 
ATOM   14704 C CA    . CYS A 1 3573 ? 207.930 165.396 196.096 1.00 15.02 ? 3573 CYS A CA    1 
ATOM   14705 C C     . CYS A 1 3573 ? 208.619 164.527 195.051 1.00 20.22 ? 3573 CYS A C     1 
ATOM   14706 O O     . CYS A 1 3573 ? 209.682 164.889 194.537 1.00 17.76 ? 3573 CYS A O     1 
ATOM   14707 C CB    . CYS A 1 3573 ? 208.333 164.968 197.506 1.00 16.43 ? 3573 CYS A CB    1 
ATOM   14708 S SG    . CYS A 1 3573 ? 207.948 166.190 198.776 1.00 32.42 ? 3573 CYS A SG    1 
ATOM   14709 N N     . THR A 1 3574 ? 208.032 163.372 194.728 1.00 18.26 ? 3574 THR A N     1 
ATOM   14710 C CA    . THR A 1 3574 ? 208.610 162.517 193.695 1.00 14.62 ? 3574 THR A CA    1 
ATOM   14711 C C     . THR A 1 3574 ? 208.569 163.194 192.329 1.00 16.83 ? 3574 THR A C     1 
ATOM   14712 O O     . THR A 1 3574 ? 209.542 163.133 191.569 1.00 24.47 ? 3574 THR A O     1 
ATOM   14713 C CB    . THR A 1 3574 ? 207.880 161.177 193.648 1.00 15.70 ? 3574 THR A CB    1 
ATOM   14714 O OG1   . THR A 1 3574 ? 206.516 161.387 193.265 1.00 20.26 ? 3574 THR A OG1   1 
ATOM   14715 C CG2   . THR A 1 3574 ? 207.924 160.499 195.008 1.00 16.88 ? 3574 THR A CG2   1 
ATOM   14716 N N     . GLU A 1 3575 ? 207.452 163.845 191.999 1.00 12.53 ? 3575 GLU A N     1 
ATOM   14717 C CA    . GLU A 1 3575 ? 207.365 164.555 190.726 1.00 10.83 ? 3575 GLU A CA    1 
ATOM   14718 C C     . GLU A 1 3575 ? 208.327 165.736 190.689 1.00 10.48 ? 3575 GLU A C     1 
ATOM   14719 O O     . GLU A 1 3575 ? 208.913 166.041 189.642 1.00 16.83 ? 3575 GLU A O     1 
ATOM   14720 C CB    . GLU A 1 3575 ? 205.930 165.013 190.478 1.00 11.20 ? 3575 GLU A CB    1 
ATOM   14721 C CG    . GLU A 1 3575 ? 204.973 163.868 190.209 1.00 13.83 ? 3575 GLU A CG    1 
ATOM   14722 C CD    . GLU A 1 3575 ? 203.523 164.284 190.303 1.00 16.83 ? 3575 GLU A CD    1 
ATOM   14723 O OE1   . GLU A 1 3575 ? 202.644 163.421 190.097 1.00 20.21 ? 3575 GLU A OE1   1 
ATOM   14724 O OE2   . GLU A 1 3575 ? 203.260 165.472 190.582 1.00 13.20 ? 3575 GLU A OE2   1 
ATOM   14725 N N     . ASN A 1 3576 ? 208.505 166.413 191.824 1.00 8.00  ? 3576 ASN A N     1 
ATOM   14726 C CA    . ASN A 1 3576 ? 209.499 167.475 191.902 1.00 7.74  ? 3576 ASN A CA    1 
ATOM   14727 C C     . ASN A 1 3576 ? 210.905 166.932 191.679 1.00 13.25 ? 3576 ASN A C     1 
ATOM   14728 O O     . ASN A 1 3576 ? 211.712 167.546 190.973 1.00 17.94 ? 3576 ASN A O     1 
ATOM   14729 C CB    . ASN A 1 3576 ? 209.398 168.179 193.252 1.00 7.19  ? 3576 ASN A CB    1 
ATOM   14730 C CG    . ASN A 1 3576 ? 208.149 169.024 193.376 1.00 5.36  ? 3576 ASN A CG    1 
ATOM   14731 O OD1   . ASN A 1 3576 ? 207.411 169.205 192.410 1.00 11.68 ? 3576 ASN A OD1   1 
ATOM   14732 N ND2   . ASN A 1 3576 ? 207.910 169.556 194.566 1.00 8.51  ? 3576 ASN A ND2   1 
ATOM   14733 N N     . ALA A 1 3577 ? 211.217 165.777 192.268 1.00 8.36  ? 3577 ALA A N     1 
ATOM   14734 C CA    . ALA A 1 3577 ? 212.521 165.161 192.045 1.00 5.57  ? 3577 ALA A CA    1 
ATOM   14735 C C     . ALA A 1 3577 ? 212.699 164.770 190.584 1.00 7.96  ? 3577 ALA A C     1 
ATOM   14736 O O     . ALA A 1 3577 ? 213.807 164.851 190.040 1.00 9.50  ? 3577 ALA A O     1 
ATOM   14737 C CB    . ALA A 1 3577 ? 212.688 163.945 192.952 1.00 14.92 ? 3577 ALA A CB    1 
ATOM   14738 N N     . ILE A 1 3578 ? 211.619 164.328 189.939 1.00 9.80  ? 3578 ILE A N     1 
ATOM   14739 C CA    . ILE A 1 3578 ? 211.671 164.010 188.514 1.00 8.09  ? 3578 ILE A CA    1 
ATOM   14740 C C     . ILE A 1 3578 ? 211.998 165.258 187.707 1.00 8.55  ? 3578 ILE A C     1 
ATOM   14741 O O     . ILE A 1 3578 ? 212.854 165.240 186.815 1.00 14.46 ? 3578 ILE A O     1 
ATOM   14742 C CB    . ILE A 1 3578 ? 210.342 163.387 188.058 1.00 7.95  ? 3578 ILE A CB    1 
ATOM   14743 C CG1   . ILE A 1 3578 ? 210.202 161.975 188.611 1.00 10.74 ? 3578 ILE A CG1   1 
ATOM   14744 C CG2   . ILE A 1 3578 ? 210.252 163.381 186.549 1.00 10.36 ? 3578 ILE A CG2   1 
ATOM   14745 C CD1   . ILE A 1 3578 ? 208.785 161.552 188.745 1.00 9.86  ? 3578 ILE A CD1   1 
ATOM   14746 N N     . MET A 1 3579 ? 211.313 166.362 188.006 1.00 9.21  ? 3579 MET A N     1 
ATOM   14747 C CA    . MET A 1 3579 ? 211.624 167.625 187.345 1.00 9.37  ? 3579 MET A CA    1 
ATOM   14748 C C     . MET A 1 3579 ? 213.046 168.073 187.647 1.00 10.15 ? 3579 MET A C     1 
ATOM   14749 O O     . MET A 1 3579 ? 213.644 168.819 186.864 1.00 13.14 ? 3579 MET A O     1 
ATOM   14750 C CB    . MET A 1 3579 ? 210.634 168.703 187.776 1.00 6.55  ? 3579 MET A CB    1 
ATOM   14751 C CG    . MET A 1 3579 ? 209.207 168.439 187.352 1.00 7.92  ? 3579 MET A CG    1 
ATOM   14752 S SD    . MET A 1 3579 ? 208.104 169.739 187.917 1.00 2.88  ? 3579 MET A SD    1 
ATOM   14753 C CE    . MET A 1 3579 ? 206.539 168.879 187.911 1.00 4.40  ? 3579 MET A CE    1 
ATOM   14754 N N     . LEU A 1 3580 ? 213.596 167.632 188.778 1.00 9.79  ? 3580 LEU A N     1 
ATOM   14755 C CA    . LEU A 1 3580 ? 214.927 168.067 189.180 1.00 7.10  ? 3580 LEU A CA    1 
ATOM   14756 C C     . LEU A 1 3580 ? 216.026 167.241 188.524 1.00 7.68  ? 3580 LEU A C     1 
ATOM   14757 O O     . LEU A 1 3580 ? 217.130 167.752 188.307 1.00 5.96  ? 3580 LEU A O     1 
ATOM   14758 C CB    . LEU A 1 3580 ? 215.048 168.005 190.700 1.00 5.71  ? 3580 LEU A CB    1 
ATOM   14759 C CG    . LEU A 1 3580 ? 214.590 169.265 191.433 1.00 7.82  ? 3580 LEU A CG    1 
ATOM   14760 C CD1   . LEU A 1 3580 ? 214.256 168.950 192.880 1.00 10.26 ? 3580 LEU A CD1   1 
ATOM   14761 C CD2   . LEU A 1 3580 ? 215.654 170.342 191.347 1.00 10.82 ? 3580 LEU A CD2   1 
ATOM   14762 N N     . LYS A 1 3581 ? 215.766 165.967 188.220 1.00 12.39 ? 3581 LYS A N     1 
ATOM   14763 C CA    . LYS A 1 3581 ? 216.803 165.152 187.591 1.00 13.35 ? 3581 LYS A CA    1 
ATOM   14764 C C     . LYS A 1 3581 ? 216.976 165.523 186.122 1.00 12.36 ? 3581 LYS A C     1 
ATOM   14765 O O     . LYS A 1 3581 ? 218.102 165.615 185.621 1.00 15.00 ? 3581 LYS A O     1 
ATOM   14766 C CB    . LYS A 1 3581 ? 216.496 163.655 187.731 1.00 7.35  ? 3581 LYS A CB    1 
ATOM   14767 C CG    . LYS A 1 3581 ? 215.282 163.165 186.964 1.00 7.07  ? 3581 LYS A CG    1 
ATOM   14768 C CD    . LYS A 1 3581 ? 215.055 161.684 187.174 1.00 12.79 ? 3581 LYS A CD    1 
ATOM   14769 C CE    . LYS A 1 3581 ? 216.138 160.871 186.490 1.00 11.98 ? 3581 LYS A CE    1 
ATOM   14770 N NZ    . LYS A 1 3581 ? 216.078 161.004 185.010 1.00 6.37  ? 3581 LYS A NZ    1 
ATOM   14771 N N     . ARG A 1 3582 ? 215.870 165.740 185.416 1.00 8.50  ? 3582 ARG A N     1 
ATOM   14772 C CA    . ARG A 1 3582 ? 215.890 166.069 184.000 1.00 9.35  ? 3582 ARG A CA    1 
ATOM   14773 C C     . ARG A 1 3582 ? 215.265 167.439 183.792 1.00 7.11  ? 3582 ARG A C     1 
ATOM   14774 O O     . ARG A 1 3582 ? 214.085 167.644 184.094 1.00 7.66  ? 3582 ARG A O     1 
ATOM   14775 C CB    . ARG A 1 3582 ? 215.159 165.008 183.174 1.00 9.11  ? 3582 ARG A CB    1 
ATOM   14776 C CG    . ARG A 1 3582 ? 213.849 164.521 183.767 1.00 7.29  ? 3582 ARG A CG    1 
ATOM   14777 C CD    . ARG A 1 3582 ? 213.224 163.462 182.877 1.00 8.24  ? 3582 ARG A CD    1 
ATOM   14778 N NE    . ARG A 1 3582 ? 214.097 162.306 182.716 1.00 11.13 ? 3582 ARG A NE    1 
ATOM   14779 C CZ    . ARG A 1 3582 ? 213.672 161.069 182.501 1.00 12.53 ? 3582 ARG A CZ    1 
ATOM   14780 N NH1   . ARG A 1 3582 ? 212.383 160.787 182.415 1.00 11.26 ? 3582 ARG A NH1   1 
ATOM   14781 N NH2   . ARG A 1 3582 ? 214.563 160.092 182.364 1.00 14.78 ? 3582 ARG A NH2   1 
ATOM   14782 N N     . PHE A 1 3583 ? 216.061 168.370 183.279 1.00 8.88  ? 3583 PHE A N     1 
ATOM   14783 C CA    . PHE A 1 3583 ? 215.624 169.739 183.062 1.00 7.89  ? 3583 PHE A CA    1 
ATOM   14784 C C     . PHE A 1 3583 ? 216.552 170.379 182.045 1.00 13.61 ? 3583 PHE A C     1 
ATOM   14785 O O     . PHE A 1 3583 ? 217.723 170.004 181.935 1.00 14.17 ? 3583 PHE A O     1 
ATOM   14786 C CB    . PHE A 1 3583 ? 215.633 170.549 184.365 1.00 5.73  ? 3583 PHE A CB    1 
ATOM   14787 C CG    . PHE A 1 3583 ? 216.986 170.627 185.018 1.00 8.89  ? 3583 PHE A CG    1 
ATOM   14788 C CD1   . PHE A 1 3583 ? 217.425 169.620 185.859 1.00 12.02 ? 3583 PHE A CD1   1 
ATOM   14789 C CD2   . PHE A 1 3583 ? 217.826 171.700 184.775 1.00 12.69 ? 3583 PHE A CD2   1 
ATOM   14790 C CE1   . PHE A 1 3583 ? 218.668 169.688 186.454 1.00 13.10 ? 3583 PHE A CE1   1 
ATOM   14791 C CE2   . PHE A 1 3583 ? 219.069 171.771 185.366 1.00 10.99 ? 3583 PHE A CE2   1 
ATOM   14792 C CZ    . PHE A 1 3583 ? 219.490 170.765 186.207 1.00 13.40 ? 3583 PHE A CZ    1 
ATOM   14793 N N     . ASN A 1 3584 ? 216.017 171.345 181.303 1.00 9.53  ? 3584 ASN A N     1 
ATOM   14794 C CA    . ASN A 1 3584 ? 216.825 172.187 180.432 1.00 5.74  ? 3584 ASN A CA    1 
ATOM   14795 C C     . ASN A 1 3584 ? 217.079 173.558 181.035 1.00 11.21 ? 3584 ASN A C     1 
ATOM   14796 O O     . ASN A 1 3584 ? 218.216 174.037 181.019 1.00 17.26 ? 3584 ASN A O     1 
ATOM   14797 C CB    . ASN A 1 3584 ? 216.157 172.343 179.065 1.00 7.38  ? 3584 ASN A CB    1 
ATOM   14798 C CG    . ASN A 1 3584 ? 216.207 171.072 178.247 1.00 11.77 ? 3584 ASN A CG    1 
ATOM   14799 O OD1   . ASN A 1 3584 ? 215.174 170.541 177.848 1.00 7.52  ? 3584 ASN A OD1   1 
ATOM   14800 N ND2   . ASN A 1 3584 ? 217.413 170.573 177.997 1.00 15.58 ? 3584 ASN A ND2   1 
ATOM   14801 N N     . ARG A 1 3585 ? 216.044 174.195 181.574 1.00 9.07  ? 3585 ARG A N     1 
ATOM   14802 C CA    . ARG A 1 3585 ? 216.199 175.429 182.327 1.00 8.54  ? 3585 ARG A CA    1 
ATOM   14803 C C     . ARG A 1 3585 ? 216.484 175.080 183.780 1.00 8.02  ? 3585 ARG A C     1 
ATOM   14804 O O     . ARG A 1 3585 ? 215.794 174.243 184.370 1.00 7.78  ? 3585 ARG A O     1 
ATOM   14805 C CB    . ARG A 1 3585 ? 214.948 176.296 182.213 1.00 6.15  ? 3585 ARG A CB    1 
ATOM   14806 C CG    . ARG A 1 3585 ? 214.483 176.513 180.789 1.00 5.20  ? 3585 ARG A CG    1 
ATOM   14807 C CD    . ARG A 1 3585 ? 213.158 177.253 180.738 1.00 8.27  ? 3585 ARG A CD    1 
ATOM   14808 N NE    . ARG A 1 3585 ? 212.030 176.377 181.039 1.00 12.46 ? 3585 ARG A NE    1 
ATOM   14809 C CZ    . ARG A 1 3585 ? 210.843 176.802 181.449 1.00 10.75 ? 3585 ARG A CZ    1 
ATOM   14810 N NH1   . ARG A 1 3585 ? 210.588 178.089 181.610 1.00 5.80  ? 3585 ARG A NH1   1 
ATOM   14811 N NH2   . ARG A 1 3585 ? 209.888 175.913 181.705 1.00 3.25  ? 3585 ARG A NH2   1 
ATOM   14812 N N     . TYR A 1 3586 ? 217.508 175.713 184.340 1.00 13.11 ? 3586 TYR A N     1 
ATOM   14813 C CA    . TYR A 1 3586 ? 217.962 175.374 185.679 1.00 9.75  ? 3586 TYR A CA    1 
ATOM   14814 C C     . TYR A 1 3586 ? 216.837 175.607 186.683 1.00 8.57  ? 3586 TYR A C     1 
ATOM   14815 O O     . TYR A 1 3586 ? 216.233 176.687 186.691 1.00 12.35 ? 3586 TYR A O     1 
ATOM   14816 C CB    . TYR A 1 3586 ? 219.181 176.215 186.042 1.00 7.81  ? 3586 TYR A CB    1 
ATOM   14817 C CG    . TYR A 1 3586 ? 220.439 175.810 185.312 1.00 14.07 ? 3586 TYR A CG    1 
ATOM   14818 C CD1   . TYR A 1 3586 ? 220.943 174.526 185.425 1.00 13.12 ? 3586 TYR A CD1   1 
ATOM   14819 C CD2   . TYR A 1 3586 ? 221.101 176.703 184.480 1.00 13.07 ? 3586 TYR A CD2   1 
ATOM   14820 C CE1   . TYR A 1 3586 ? 222.087 174.148 184.756 1.00 13.70 ? 3586 TYR A CE1   1 
ATOM   14821 C CE2   . TYR A 1 3586 ? 222.252 176.333 183.805 1.00 13.60 ? 3586 TYR A CE2   1 
ATOM   14822 C CZ    . TYR A 1 3586 ? 222.738 175.053 183.945 1.00 15.67 ? 3586 TYR A CZ    1 
ATOM   14823 O OH    . TYR A 1 3586 ? 223.879 174.678 183.273 1.00 17.09 ? 3586 TYR A OH    1 
ATOM   14824 N N     . PRO A 1 3587 ? 216.527 174.629 187.532 1.00 10.69 ? 3587 PRO A N     1 
ATOM   14825 C CA    . PRO A 1 3587 ? 215.346 174.749 188.415 1.00 5.17  ? 3587 PRO A CA    1 
ATOM   14826 C C     . PRO A 1 3587 ? 215.432 175.879 189.429 1.00 6.28  ? 3587 PRO A C     1 
ATOM   14827 O O     . PRO A 1 3587 ? 216.514 176.316 189.833 1.00 12.48 ? 3587 PRO A O     1 
ATOM   14828 C CB    . PRO A 1 3587 ? 215.418 173.377 189.054 1.00 6.13  ? 3587 PRO A CB    1 
ATOM   14829 C CG    . PRO A 1 3587 ? 216.920 173.513 189.055 1.00 10.27 ? 3587 PRO A CG    1 
ATOM   14830 C CD    . PRO A 1 3587 ? 217.044 173.244 187.789 1.00 13.56 ? 3587 PRO A CD    1 
ATOM   14831 N N     . LEU A 1 3588 ? 214.260 176.389 189.799 1.00 9.02  ? 3588 LEU A N     1 
ATOM   14832 C CA    . LEU A 1 3588 ? 214.118 177.389 190.854 1.00 8.24  ? 3588 LEU A CA    1 
ATOM   14833 C C     . LEU A 1 3588 ? 213.148 176.782 191.865 1.00 8.98  ? 3588 LEU A C     1 
ATOM   14834 O O     . LEU A 1 3588 ? 211.975 176.557 191.557 1.00 9.03  ? 3588 LEU A O     1 
ATOM   14835 C CB    . LEU A 1 3588 ? 213.633 178.726 190.297 1.00 9.90  ? 3588 LEU A CB    1 
ATOM   14836 C CG    . LEU A 1 3588 ? 213.599 179.949 191.217 1.00 8.00  ? 3588 LEU A CG    1 
ATOM   14837 C CD1   . LEU A 1 3588 ? 213.757 181.210 190.386 1.00 11.82 ? 3588 LEU A CD1   1 
ATOM   14838 C CD2   . LEU A 1 3588 ? 212.314 180.011 192.010 1.00 10.29 ? 3588 LEU A CD2   1 
ATOM   14839 N N     . ILE A 1 3589 ? 213.652 176.504 193.061 1.00 11.85 ? 3589 ILE A N     1 
ATOM   14840 C CA    . ILE A 1 3589 ? 212.927 175.706 194.042 1.00 9.48  ? 3589 ILE A CA    1 
ATOM   14841 C C     . ILE A 1 3589 ? 212.058 176.623 194.888 1.00 10.47 ? 3589 ILE A C     1 
ATOM   14842 O O     . ILE A 1 3589 ? 212.524 177.654 195.387 1.00 20.15 ? 3589 ILE A O     1 
ATOM   14843 C CB    . ILE A 1 3589 ? 213.909 174.919 194.920 1.00 14.01 ? 3589 ILE A CB    1 
ATOM   14844 C CG1   . ILE A 1 3589 ? 214.805 174.041 194.051 1.00 11.95 ? 3589 ILE A CG1   1 
ATOM   14845 C CG2   . ILE A 1 3589 ? 213.159 174.074 195.928 1.00 8.66  ? 3589 ILE A CG2   1 
ATOM   14846 C CD1   . ILE A 1 3589 ? 216.193 173.891 194.607 1.00 13.10 ? 3589 ILE A CD1   1 
ATOM   14847 N N     . ILE A 1 3590 ? 210.793 176.253 195.051 1.00 10.83 ? 3590 ILE A N     1 
ATOM   14848 C CA    . ILE A 1 3590 ? 209.862 176.966 195.915 1.00 9.27  ? 3590 ILE A CA    1 
ATOM   14849 C C     . ILE A 1 3590 ? 209.522 176.032 197.068 1.00 11.55 ? 3590 ILE A C     1 
ATOM   14850 O O     . ILE A 1 3590 ? 208.700 175.121 196.916 1.00 15.39 ? 3590 ILE A O     1 
ATOM   14851 C CB    . ILE A 1 3590 ? 208.593 177.392 195.166 1.00 13.72 ? 3590 ILE A CB    1 
ATOM   14852 C CG1   . ILE A 1 3590 ? 208.937 178.191 193.910 1.00 9.23  ? 3590 ILE A CG1   1 
ATOM   14853 C CG2   . ILE A 1 3590 ? 207.714 178.224 196.072 1.00 9.88  ? 3590 ILE A CG2   1 
ATOM   14854 C CD1   . ILE A 1 3590 ? 209.564 179.521 194.189 1.00 12.36 ? 3590 ILE A CD1   1 
ATOM   14855 N N     . ASP A 1 3591 ? 210.147 176.249 198.219 1.00 18.15 ? 3591 ASP A N     1 
ATOM   14856 C CA    . ASP A 1 3591 ? 209.836 175.440 199.390 1.00 20.03 ? 3591 ASP A CA    1 
ATOM   14857 C C     . ASP A 1 3591 ? 209.864 176.290 200.655 1.00 20.78 ? 3591 ASP A C     1 
ATOM   14858 O O     . ASP A 1 3591 ? 210.929 176.769 201.063 1.00 20.49 ? 3591 ASP A O     1 
ATOM   14859 C CB    . ASP A 1 3591 ? 210.803 174.258 199.514 1.00 18.19 ? 3591 ASP A CB    1 
ATOM   14860 C CG    . ASP A 1 3591 ? 212.258 174.677 199.444 1.00 21.13 ? 3591 ASP A CG    1 
ATOM   14861 O OD1   . ASP A 1 3591 ? 212.531 175.838 199.084 1.00 21.36 ? 3591 ASP A OD1   1 
ATOM   14862 O OD2   . ASP A 1 3591 ? 213.132 173.849 199.768 1.00 24.92 ? 3591 ASP A OD2   1 
ATOM   14863 N N     . PRO A 1 3592 ? 208.712 176.514 201.291 1.00 19.26 ? 3592 PRO A N     1 
ATOM   14864 C CA    . PRO A 1 3592 ? 208.718 177.245 202.567 1.00 23.12 ? 3592 PRO A CA    1 
ATOM   14865 C C     . PRO A 1 3592 ? 209.562 176.574 203.634 1.00 26.76 ? 3592 PRO A C     1 
ATOM   14866 O O     . PRO A 1 3592 ? 210.205 177.267 204.432 1.00 25.77 ? 3592 PRO A O     1 
ATOM   14867 C CB    . PRO A 1 3592 ? 207.232 177.288 202.952 1.00 23.23 ? 3592 PRO A CB    1 
ATOM   14868 C CG    . PRO A 1 3592 ? 206.605 176.165 202.191 1.00 21.89 ? 3592 PRO A CG    1 
ATOM   14869 C CD    . PRO A 1 3592 ? 207.361 176.077 200.905 1.00 17.47 ? 3592 PRO A CD    1 
ATOM   14870 N N     . SER A 1 3593 ? 209.584 175.245 203.671 1.00 28.76 ? 3593 SER A N     1 
ATOM   14871 C CA    . SER A 1 3593 ? 210.468 174.508 204.559 1.00 25.61 ? 3593 SER A CA    1 
ATOM   14872 C C     . SER A 1 3593 ? 211.722 174.104 203.781 1.00 25.02 ? 3593 SER A C     1 
ATOM   14873 O O     . SER A 1 3593 ? 211.956 174.568 202.662 1.00 29.90 ? 3593 SER A O     1 
ATOM   14874 C CB    . SER A 1 3593 ? 209.728 173.319 205.165 1.00 26.22 ? 3593 SER A CB    1 
ATOM   14875 O OG    . SER A 1 3593 ? 208.630 173.748 205.950 1.00 30.66 ? 3593 SER A OG    1 
ATOM   14876 N N     . GLY A 1 3594 ? 212.550 173.238 204.362 1.00 26.98 ? 3594 GLY A N     1 
ATOM   14877 C CA    . GLY A 1 3594 ? 213.854 172.944 203.800 1.00 26.97 ? 3594 GLY A CA    1 
ATOM   14878 C C     . GLY A 1 3594 ? 214.121 171.540 203.308 1.00 27.59 ? 3594 GLY A C     1 
ATOM   14879 O O     . GLY A 1 3594 ? 215.292 171.196 203.097 1.00 29.97 ? 3594 GLY A O     1 
ATOM   14880 N N     . GLN A 1 3595 ? 213.095 170.708 203.108 1.00 29.72 ? 3595 GLN A N     1 
ATOM   14881 C CA    . GLN A 1 3595 ? 213.349 169.334 202.683 1.00 29.12 ? 3595 GLN A CA    1 
ATOM   14882 C C     . GLN A 1 3595 ? 213.968 169.286 201.292 1.00 31.69 ? 3595 GLN A C     1 
ATOM   14883 O O     . GLN A 1 3595 ? 214.803 168.422 201.010 1.00 28.87 ? 3595 GLN A O     1 
ATOM   14884 C CB    . GLN A 1 3595 ? 212.064 168.502 202.720 1.00 26.81 ? 3595 GLN A CB    1 
ATOM   14885 C CG    . GLN A 1 3595 ? 211.251 168.636 203.992 1.00 27.51 ? 3595 GLN A CG    1 
ATOM   14886 C CD    . GLN A 1 3595 ? 210.335 169.834 203.963 1.00 32.86 ? 3595 GLN A CD    1 
ATOM   14887 O OE1   . GLN A 1 3595 ? 210.764 170.943 203.657 1.00 31.21 ? 3595 GLN A OE1   1 
ATOM   14888 N NE2   . GLN A 1 3595 ? 209.065 169.620 204.284 1.00 32.36 ? 3595 GLN A NE2   1 
ATOM   14889 N N     . ALA A 1 3596 ? 213.568 170.201 200.406 1.00 25.68 ? 3596 ALA A N     1 
ATOM   14890 C CA    . ALA A 1 3596 ? 214.118 170.201 199.054 1.00 22.50 ? 3596 ALA A CA    1 
ATOM   14891 C C     . ALA A 1 3596 ? 215.588 170.603 199.047 1.00 23.92 ? 3596 ALA A C     1 
ATOM   14892 O O     . ALA A 1 3596 ? 216.396 170.013 198.318 1.00 23.67 ? 3596 ALA A O     1 
ATOM   14893 C CB    . ALA A 1 3596 ? 213.306 171.132 198.158 1.00 24.74 ? 3596 ALA A CB    1 
ATOM   14894 N N     . THR A 1 3597 ? 215.953 171.610 199.842 1.00 24.65 ? 3597 THR A N     1 
ATOM   14895 C CA    . THR A 1 3597 ? 217.338 172.066 199.869 1.00 25.18 ? 3597 THR A CA    1 
ATOM   14896 C C     . THR A 1 3597 ? 218.262 170.983 200.412 1.00 29.09 ? 3597 THR A C     1 
ATOM   14897 O O     . THR A 1 3597 ? 219.318 170.704 199.833 1.00 34.62 ? 3597 THR A O     1 
ATOM   14898 C CB    . THR A 1 3597 ? 217.452 173.344 200.700 1.00 25.69 ? 3597 THR A CB    1 
ATOM   14899 O OG1   . THR A 1 3597 ? 216.909 173.116 202.006 1.00 29.57 ? 3597 THR A OG1   1 
ATOM   14900 C CG2   . THR A 1 3597 ? 216.691 174.478 200.033 1.00 22.97 ? 3597 THR A CG2   1 
ATOM   14901 N N     . GLU A 1 3598 ? 217.873 170.347 201.521 1.00 24.86 ? 3598 GLU A N     1 
ATOM   14902 C CA    . GLU A 1 3598 ? 218.678 169.250 202.047 1.00 26.97 ? 3598 GLU A CA    1 
ATOM   14903 C C     . GLU A 1 3598 ? 218.661 168.050 201.109 1.00 27.10 ? 3598 GLU A C     1 
ATOM   14904 O O     . GLU A 1 3598 ? 219.670 167.351 200.988 1.00 27.05 ? 3598 GLU A O     1 
ATOM   14905 C CB    . GLU A 1 3598 ? 218.196 168.855 203.444 1.00 29.77 ? 3598 GLU A CB    1 
ATOM   14906 C CG    . GLU A 1 3598 ? 216.764 168.357 203.506 1.00 27.36 ? 3598 GLU A CG    1 
ATOM   14907 C CD    . GLU A 1 3598 ? 216.134 168.561 204.869 1.00 29.53 ? 3598 GLU A CD    1 
ATOM   14908 O OE1   . GLU A 1 3598 ? 216.217 169.689 205.400 1.00 25.63 ? 3598 GLU A OE1   1 
ATOM   14909 O OE2   . GLU A 1 3598 ? 215.557 167.595 205.409 1.00 30.63 ? 3598 GLU A OE2   1 
ATOM   14910 N N     . PHE A 1 3599 ? 217.537 167.811 200.428 1.00 26.84 ? 3599 PHE A N     1 
ATOM   14911 C CA    . PHE A 1 3599 ? 217.474 166.767 199.410 1.00 26.55 ? 3599 PHE A CA    1 
ATOM   14912 C C     . PHE A 1 3599 ? 218.520 166.975 198.328 1.00 25.13 ? 3599 PHE A C     1 
ATOM   14913 O O     . PHE A 1 3599 ? 219.226 166.038 197.940 1.00 30.91 ? 3599 PHE A O     1 
ATOM   14914 C CB    . PHE A 1 3599 ? 216.077 166.732 198.792 1.00 25.02 ? 3599 PHE A CB    1 
ATOM   14915 C CG    . PHE A 1 3599 ? 215.906 165.673 197.745 1.00 26.12 ? 3599 PHE A CG    1 
ATOM   14916 C CD1   . PHE A 1 3599 ? 215.765 164.342 198.088 1.00 29.39 ? 3599 PHE A CD1   1 
ATOM   14917 C CD2   . PHE A 1 3599 ? 215.882 166.020 196.405 1.00 24.23 ? 3599 PHE A CD2   1 
ATOM   14918 C CE1   . PHE A 1 3599 ? 215.614 163.378 197.110 1.00 30.40 ? 3599 PHE A CE1   1 
ATOM   14919 C CE2   . PHE A 1 3599 ? 215.726 165.063 195.428 1.00 24.88 ? 3599 PHE A CE2   1 
ATOM   14920 C CZ    . PHE A 1 3599 ? 215.590 163.741 195.781 1.00 27.57 ? 3599 PHE A CZ    1 
ATOM   14921 N N     . ILE A 1 3600 ? 218.628 168.200 197.817 1.00 24.84 ? 3600 ILE A N     1 
ATOM   14922 C CA    . ILE A 1 3600 ? 219.549 168.436 196.711 1.00 25.25 ? 3600 ILE A CA    1 
ATOM   14923 C C     . ILE A 1 3600 ? 220.985 168.539 197.210 1.00 27.25 ? 3600 ILE A C     1 
ATOM   14924 O O     . ILE A 1 3600 ? 221.929 168.243 196.468 1.00 26.72 ? 3600 ILE A O     1 
ATOM   14925 C CB    . ILE A 1 3600 ? 219.093 169.671 195.915 1.00 25.98 ? 3600 ILE A CB    1 
ATOM   14926 C CG1   . ILE A 1 3600 ? 217.724 169.380 195.304 1.00 25.82 ? 3600 ILE A CG1   1 
ATOM   14927 C CG2   . ILE A 1 3600 ? 220.082 170.021 194.819 1.00 30.65 ? 3600 ILE A CG2   1 
ATOM   14928 C CD1   . ILE A 1 3600 ? 217.050 170.566 194.716 1.00 27.68 ? 3600 ILE A CD1   1 
ATOM   14929 N N     . MET A 1 3601 ? 221.184 168.923 198.473 1.00 28.68 ? 3601 MET A N     1 
ATOM   14930 C CA    . MET A 1 3601 ? 222.518 168.813 199.055 1.00 29.74 ? 3601 MET A CA    1 
ATOM   14931 C C     . MET A 1 3601 ? 222.942 167.353 199.184 1.00 31.50 ? 3601 MET A C     1 
ATOM   14932 O O     . MET A 1 3601 ? 224.108 167.014 198.951 1.00 31.01 ? 3601 MET A O     1 
ATOM   14933 C CB    . MET A 1 3601 ? 222.568 169.514 200.412 1.00 27.00 ? 3601 MET A CB    1 
ATOM   14934 C CG    . MET A 1 3601 ? 222.378 171.018 200.337 1.00 30.85 ? 3601 MET A CG    1 
ATOM   14935 S SD    . MET A 1 3601 ? 223.659 171.819 199.354 1.00 37.39 ? 3601 MET A SD    1 
ATOM   14936 C CE    . MET A 1 3601 ? 225.086 171.598 200.411 1.00 31.94 ? 3601 MET A CE    1 
ATOM   14937 N N     . ASN A 1 3602 ? 222.007 166.475 199.559 1.00 28.31 ? 3602 ASN A N     1 
ATOM   14938 C CA    . ASN A 1 3602 ? 222.321 165.054 199.666 1.00 26.64 ? 3602 ASN A CA    1 
ATOM   14939 C C     . ASN A 1 3602 ? 222.550 164.426 198.297 1.00 31.26 ? 3602 ASN A C     1 
ATOM   14940 O O     . ASN A 1 3602 ? 223.436 163.579 198.134 1.00 32.12 ? 3602 ASN A O     1 
ATOM   14941 C CB    . ASN A 1 3602 ? 221.202 164.317 200.403 1.00 25.88 ? 3602 ASN A CB    1 
ATOM   14942 C CG    . ASN A 1 3602 ? 220.955 164.866 201.790 1.00 31.69 ? 3602 ASN A CG    1 
ATOM   14943 O OD1   . ASN A 1 3602 ? 221.860 165.409 202.424 1.00 34.55 ? 3602 ASN A OD1   1 
ATOM   14944 N ND2   . ASN A 1 3602 ? 219.727 164.727 202.273 1.00 31.35 ? 3602 ASN A ND2   1 
ATOM   14945 N N     . GLU A 1 3603 ? 221.756 164.824 197.302 1.00 31.26 ? 3603 GLU A N     1 
ATOM   14946 C CA    . GLU A 1 3603 ? 221.849 164.208 195.983 1.00 27.80 ? 3603 GLU A CA    1 
ATOM   14947 C C     . GLU A 1 3603 ? 223.171 164.532 195.301 1.00 29.40 ? 3603 GLU A C     1 
ATOM   14948 O O     . GLU A 1 3603 ? 223.531 163.888 194.308 1.00 29.63 ? 3603 GLU A O     1 
ATOM   14949 C CB    . GLU A 1 3603 ? 220.676 164.664 195.113 1.00 26.29 ? 3603 GLU A CB    1 
ATOM   14950 C CG    . GLU A 1 3603 ? 220.422 163.799 193.889 1.00 26.14 ? 3603 GLU A CG    1 
ATOM   14951 C CD    . GLU A 1 3603 ? 219.556 162.596 194.192 1.00 32.69 ? 3603 GLU A CD    1 
ATOM   14952 O OE1   . GLU A 1 3603 ? 218.996 162.529 195.306 1.00 34.04 ? 3603 GLU A OE1   1 
ATOM   14953 O OE2   . GLU A 1 3603 ? 219.437 161.714 193.316 1.00 30.91 ? 3603 GLU A OE2   1 
ATOM   14954 N N     . TYR A 1 3604 ? 223.913 165.510 195.817 1.00 29.70 ? 3604 TYR A N     1 
ATOM   14955 C CA    . TYR A 1 3604 ? 225.109 166.003 195.147 1.00 30.66 ? 3604 TYR A CA    1 
ATOM   14956 C C     . TYR A 1 3604 ? 226.306 166.102 196.089 1.00 34.52 ? 3604 TYR A C     1 
ATOM   14957 O O     . TYR A 1 3604 ? 227.173 166.956 195.896 1.00 32.56 ? 3604 TYR A O     1 
ATOM   14958 C CB    . TYR A 1 3604 ? 224.830 167.358 194.497 1.00 31.55 ? 3604 TYR A CB    1 
ATOM   14959 C CG    . TYR A 1 3604 ? 223.846 167.297 193.347 1.00 30.36 ? 3604 TYR A CG    1 
ATOM   14960 C CD1   . TYR A 1 3604 ? 224.279 167.085 192.048 1.00 29.28 ? 3604 TYR A CD1   1 
ATOM   14961 C CD2   . TYR A 1 3604 ? 222.485 167.455 193.563 1.00 28.85 ? 3604 TYR A CD2   1 
ATOM   14962 C CE1   . TYR A 1 3604 ? 223.385 167.029 190.997 1.00 26.54 ? 3604 TYR A CE1   1 
ATOM   14963 C CE2   . TYR A 1 3604 ? 221.585 167.401 192.519 1.00 27.51 ? 3604 TYR A CE2   1 
ATOM   14964 C CZ    . TYR A 1 3604 ? 222.041 167.188 191.238 1.00 26.66 ? 3604 TYR A CZ    1 
ATOM   14965 O OH    . TYR A 1 3604 ? 221.146 167.134 190.195 1.00 30.97 ? 3604 TYR A OH    1 
ATOM   14966 N N     . LYS A 1 3605 ? 226.380 165.244 197.113 1.00 37.04 ? 3605 LYS A N     1 
ATOM   14967 C CA    . LYS A 1 3605 ? 227.589 165.219 197.934 1.00 34.12 ? 3605 LYS A CA    1 
ATOM   14968 C C     . LYS A 1 3605 ? 228.802 164.810 197.111 1.00 34.55 ? 3605 LYS A C     1 
ATOM   14969 O O     . LYS A 1 3605 ? 229.872 165.419 197.222 1.00 34.19 ? 3605 LYS A O     1 
ATOM   14970 C CB    . LYS A 1 3605 ? 227.451 164.268 199.126 1.00 34.52 ? 3605 LYS A CB    1 
ATOM   14971 C CG    . LYS A 1 3605 ? 226.292 164.484 200.082 1.00 34.72 ? 3605 LYS A CG    1 
ATOM   14972 C CD    . LYS A 1 3605 ? 225.610 163.152 200.376 1.00 35.10 ? 3605 LYS A CD    1 
ATOM   14973 C CE    . LYS A 1 3605 ? 224.604 163.264 201.509 1.00 33.04 ? 3605 LYS A CE    1 
ATOM   14974 N NZ    . LYS A 1 3605 ? 223.820 162.010 201.682 1.00 34.53 ? 3605 LYS A NZ    1 
ATOM   14975 N N     . ASP A 1 3606 ? 228.651 163.778 196.278 1.00 35.26 ? 3606 ASP A N     1 
ATOM   14976 C CA    . ASP A 1 3606 ? 229.799 163.214 195.575 1.00 37.17 ? 3606 ASP A CA    1 
ATOM   14977 C C     . ASP A 1 3606 ? 230.386 164.193 194.564 1.00 35.91 ? 3606 ASP A C     1 
ATOM   14978 O O     . ASP A 1 3606 ? 231.581 164.129 194.254 1.00 36.66 ? 3606 ASP A O     1 
ATOM   14979 C CB    . ASP A 1 3606 ? 229.404 161.894 194.909 1.00 39.31 ? 3606 ASP A CB    1 
ATOM   14980 C CG    . ASP A 1 3606 ? 228.309 162.059 193.870 1.00 43.38 ? 3606 ASP A CG    1 
ATOM   14981 O OD1   . ASP A 1 3606 ? 227.807 163.188 193.690 1.00 43.58 ? 3606 ASP A OD1   1 
ATOM   14982 O OD2   . ASP A 1 3606 ? 227.945 161.050 193.231 1.00 40.78 ? 3606 ASP A OD2   1 
ATOM   14983 N N     . ARG A 1 3607 ? 229.569 165.104 194.038 1.00 33.45 ? 3607 ARG A N     1 
ATOM   14984 C CA    . ARG A 1 3607 ? 230.092 166.124 193.139 1.00 34.82 ? 3607 ARG A CA    1 
ATOM   14985 C C     . ARG A 1 3607 ? 230.440 167.422 193.857 1.00 34.49 ? 3607 ARG A C     1 
ATOM   14986 O O     . ARG A 1 3607 ? 230.743 168.415 193.188 1.00 34.26 ? 3607 ARG A O     1 
ATOM   14987 C CB    . ARG A 1 3607 ? 229.104 166.402 192.001 1.00 33.33 ? 3607 ARG A CB    1 
ATOM   14988 C CG    . ARG A 1 3607 ? 228.533 165.152 191.353 1.00 32.66 ? 3607 ARG A CG    1 
ATOM   14989 C CD    . ARG A 1 3607 ? 227.146 165.398 190.778 1.00 34.64 ? 3607 ARG A CD    1 
ATOM   14990 N NE    . ARG A 1 3607 ? 227.215 165.822 189.384 1.00 37.41 ? 3607 ARG A NE    1 
ATOM   14991 C CZ    . ARG A 1 3607 ? 226.765 166.980 188.920 1.00 35.16 ? 3607 ARG A CZ    1 
ATOM   14992 N NH1   . ARG A 1 3607 ? 226.212 167.877 189.718 1.00 31.98 ? 3607 ARG A NH1   1 
ATOM   14993 N NH2   . ARG A 1 3607 ? 226.878 167.247 187.623 1.00 30.50 ? 3607 ARG A NH2   1 
ATOM   14994 N N     . LYS A 1 3608 ? 230.406 167.432 195.191 1.00 34.34 ? 3608 LYS A N     1 
ATOM   14995 C CA    . LYS A 1 3608 ? 230.855 168.565 196.004 1.00 34.67 ? 3608 LYS A CA    1 
ATOM   14996 C C     . LYS A 1 3608 ? 230.060 169.833 195.684 1.00 32.23 ? 3608 LYS A C     1 
ATOM   14997 O O     . LYS A 1 3608 ? 230.592 170.828 195.189 1.00 33.90 ? 3608 LYS A O     1 
ATOM   14998 C CB    . LYS A 1 3608 ? 232.363 168.803 195.832 1.00 34.26 ? 3608 LYS A CB    1 
ATOM   14999 C CG    . LYS A 1 3608 ? 233.263 167.559 195.913 1.00 37.17 ? 3608 LYS A CG    1 
ATOM   15000 C CD    . LYS A 1 3608 ? 232.851 166.544 196.984 1.00 35.89 ? 3608 LYS A CD    1 
ATOM   15001 C CE    . LYS A 1 3608 ? 232.867 167.140 198.389 1.00 34.57 ? 3608 LYS A CE    1 
ATOM   15002 N NZ    . LYS A 1 3608 ? 234.250 167.255 198.928 1.00 34.67 ? 3608 LYS A NZ    1 
ATOM   15003 N N     . ILE A 1 3609 ? 228.765 169.780 195.982 1.00 29.84 ? 3609 ILE A N     1 
ATOM   15004 C CA    . ILE A 1 3609 ? 227.882 170.915 195.739 1.00 33.67 ? 3609 ILE A CA    1 
ATOM   15005 C C     . ILE A 1 3609 ? 228.196 172.010 196.753 1.00 29.76 ? 3609 ILE A C     1 
ATOM   15006 O O     . ILE A 1 3609 ? 228.248 171.759 197.961 1.00 29.44 ? 3609 ILE A O     1 
ATOM   15007 C CB    . ILE A 1 3609 ? 226.405 170.498 195.805 1.00 36.37 ? 3609 ILE A CB    1 
ATOM   15008 C CG1   . ILE A 1 3609 ? 225.498 171.728 195.719 1.00 32.74 ? 3609 ILE A CG1   1 
ATOM   15009 C CG2   . ILE A 1 3609 ? 226.115 169.706 197.072 1.00 28.32 ? 3609 ILE A CG2   1 
ATOM   15010 C CD1   . ILE A 1 3609 ? 224.054 171.400 195.404 1.00 30.83 ? 3609 ILE A CD1   1 
ATOM   15011 N N     . THR A 1 3610 ? 228.422 173.223 196.260 1.00 25.30 ? 3610 THR A N     1 
ATOM   15012 C CA    . THR A 1 3610 ? 228.730 174.359 197.115 1.00 28.66 ? 3610 THR A CA    1 
ATOM   15013 C C     . THR A 1 3610 ? 227.457 175.132 197.432 1.00 26.88 ? 3610 THR A C     1 
ATOM   15014 O O     . THR A 1 3610 ? 226.602 175.327 196.565 1.00 29.22 ? 3610 THR A O     1 
ATOM   15015 C CB    . THR A 1 3610 ? 229.750 175.278 196.441 1.00 28.98 ? 3610 THR A CB    1 
ATOM   15016 O OG1   . THR A 1 3610 ? 230.893 174.513 196.039 1.00 26.56 ? 3610 THR A OG1   1 
ATOM   15017 C CG2   . THR A 1 3610 ? 230.199 176.376 197.395 1.00 28.75 ? 3610 THR A CG2   1 
ATOM   15018 N N     . ARG A 1 3611 ? 227.334 175.565 198.683 1.00 25.59 ? 3611 ARG A N     1 
ATOM   15019 C CA    . ARG A 1 3611 ? 226.180 176.326 199.142 1.00 23.38 ? 3611 ARG A CA    1 
ATOM   15020 C C     . ARG A 1 3611 ? 226.539 177.807 199.161 1.00 24.72 ? 3611 ARG A C     1 
ATOM   15021 O O     . ARG A 1 3611 ? 227.516 178.206 199.804 1.00 26.15 ? 3611 ARG A O     1 
ATOM   15022 C CB    . ARG A 1 3611 ? 225.738 175.857 200.526 1.00 27.40 ? 3611 ARG A CB    1 
ATOM   15023 C CG    . ARG A 1 3611 ? 224.305 176.207 200.879 1.00 25.39 ? 3611 ARG A CG    1 
ATOM   15024 C CD    . ARG A 1 3611 ? 223.898 175.521 202.170 1.00 27.04 ? 3611 ARG A CD    1 
ATOM   15025 N NE    . ARG A 1 3611 ? 222.452 175.442 202.328 1.00 25.57 ? 3611 ARG A NE    1 
ATOM   15026 C CZ    . ARG A 1 3611 ? 221.734 176.278 203.065 1.00 26.14 ? 3611 ARG A CZ    1 
ATOM   15027 N NH1   . ARG A 1 3611 ? 222.297 177.282 203.717 1.00 26.01 ? 3611 ARG A NH1   1 
ATOM   15028 N NH2   . ARG A 1 3611 ? 220.419 176.101 203.153 1.00 26.79 ? 3611 ARG A NH2   1 
ATOM   15029 N N     . THR A 1 3612 ? 225.748 178.614 198.457 1.00 23.62 ? 3612 THR A N     1 
ATOM   15030 C CA    . THR A 1 3612 ? 226.013 180.040 198.319 1.00 24.24 ? 3612 THR A CA    1 
ATOM   15031 C C     . THR A 1 3612 ? 224.675 180.771 198.257 1.00 21.26 ? 3612 THR A C     1 
ATOM   15032 O O     . THR A 1 3612 ? 223.643 180.142 198.013 1.00 23.42 ? 3612 THR A O     1 
ATOM   15033 C CB    . THR A 1 3612 ? 226.870 180.296 197.069 1.00 28.85 ? 3612 THR A CB    1 
ATOM   15034 O OG1   . THR A 1 3612 ? 228.096 179.563 197.178 1.00 31.09 ? 3612 THR A OG1   1 
ATOM   15035 C CG2   . THR A 1 3612 ? 227.217 181.770 196.912 1.00 25.98 ? 3612 THR A CG2   1 
ATOM   15036 N N     . SER A 1 3613 ? 224.664 182.078 198.512 1.00 21.90 ? 3613 SER A N     1 
ATOM   15037 C CA    . SER A 1 3613 ? 223.442 182.861 198.410 1.00 22.24 ? 3613 SER A CA    1 
ATOM   15038 C C     . SER A 1 3613 ? 223.743 184.156 197.671 1.00 24.47 ? 3613 SER A C     1 
ATOM   15039 O O     . SER A 1 3613 ? 224.890 184.608 197.614 1.00 26.68 ? 3613 SER A O     1 
ATOM   15040 C CB    . SER A 1 3613 ? 222.841 183.152 199.789 1.00 22.85 ? 3613 SER A CB    1 
ATOM   15041 O OG    . SER A 1 3613 ? 221.672 183.944 199.678 1.00 25.69 ? 3613 SER A OG    1 
ATOM   15042 N N     . PHE A 1 3614 ? 222.695 184.746 197.092 1.00 24.86 ? 3614 PHE A N     1 
ATOM   15043 C CA    . PHE A 1 3614 ? 222.861 186.019 196.396 1.00 25.47 ? 3614 PHE A CA    1 
ATOM   15044 C C     . PHE A 1 3614 ? 223.270 187.126 197.359 1.00 27.90 ? 3614 PHE A C     1 
ATOM   15045 O O     . PHE A 1 3614 ? 224.029 188.030 196.991 1.00 29.34 ? 3614 PHE A O     1 
ATOM   15046 C CB    . PHE A 1 3614 ? 221.573 186.401 195.665 1.00 23.08 ? 3614 PHE A CB    1 
ATOM   15047 C CG    . PHE A 1 3614 ? 221.204 185.467 194.550 1.00 26.87 ? 3614 PHE A CG    1 
ATOM   15048 C CD1   . PHE A 1 3614 ? 222.036 185.310 193.455 1.00 28.14 ? 3614 PHE A CD1   1 
ATOM   15049 C CD2   . PHE A 1 3614 ? 220.014 184.761 194.585 1.00 28.45 ? 3614 PHE A CD2   1 
ATOM   15050 C CE1   . PHE A 1 3614 ? 221.695 184.456 192.424 1.00 28.15 ? 3614 PHE A CE1   1 
ATOM   15051 C CE2   . PHE A 1 3614 ? 219.669 183.908 193.557 1.00 25.75 ? 3614 PHE A CE2   1 
ATOM   15052 C CZ    . PHE A 1 3614 ? 220.510 183.755 192.476 1.00 25.40 ? 3614 PHE A CZ    1 
ATOM   15053 N N     . LEU A 1 3615 ? 222.772 187.075 198.596 1.00 27.60 ? 3615 LEU A N     1 
ATOM   15054 C CA    . LEU A 1 3615 ? 223.120 188.099 199.576 1.00 28.45 ? 3615 LEU A CA    1 
ATOM   15055 C C     . LEU A 1 3615 ? 224.597 188.051 199.945 1.00 29.84 ? 3615 LEU A C     1 
ATOM   15056 O O     . LEU A 1 3615 ? 225.142 189.040 200.450 1.00 29.12 ? 3615 LEU A O     1 
ATOM   15057 C CB    . LEU A 1 3615 ? 222.255 187.942 200.826 1.00 28.52 ? 3615 LEU A CB    1 
ATOM   15058 C CG    . LEU A 1 3615 ? 220.743 187.982 200.600 1.00 29.66 ? 3615 LEU A CG    1 
ATOM   15059 C CD1   . LEU A 1 3615 ? 220.015 187.239 201.708 1.00 24.17 ? 3615 LEU A CD1   1 
ATOM   15060 C CD2   . LEU A 1 3615 ? 220.254 189.417 200.502 1.00 29.91 ? 3615 LEU A CD2   1 
ATOM   15061 N N     . ASP A 1 3616 ? 225.258 186.920 199.710 1.00 32.71 ? 3616 ASP A N     1 
ATOM   15062 C CA    . ASP A 1 3616 ? 226.679 186.805 200.010 1.00 32.93 ? 3616 ASP A CA    1 
ATOM   15063 C C     . ASP A 1 3616 ? 227.493 187.695 199.078 1.00 35.65 ? 3616 ASP A C     1 
ATOM   15064 O O     . ASP A 1 3616 ? 227.278 187.706 197.863 1.00 34.90 ? 3616 ASP A O     1 
ATOM   15065 C CB    . ASP A 1 3616 ? 227.126 185.349 199.881 1.00 31.89 ? 3616 ASP A CB    1 
ATOM   15066 C CG    . ASP A 1 3616 ? 228.635 185.197 199.899 1.00 34.87 ? 3616 ASP A CG    1 
ATOM   15067 O OD1   . ASP A 1 3616 ? 229.301 185.913 200.677 1.00 34.64 ? 3616 ASP A OD1   1 
ATOM   15068 O OD2   . ASP A 1 3616 ? 229.156 184.359 199.134 1.00 34.04 ? 3616 ASP A OD2   1 
ATOM   15069 N N     . ASP A 1 3617 ? 228.435 188.444 199.657 1.00 36.78 ? 3617 ASP A N     1 
ATOM   15070 C CA    . ASP A 1 3617 ? 229.291 189.309 198.852 1.00 37.32 ? 3617 ASP A CA    1 
ATOM   15071 C C     . ASP A 1 3617 ? 230.256 188.503 197.993 1.00 36.77 ? 3617 ASP A C     1 
ATOM   15072 O O     . ASP A 1 3617 ? 230.720 188.993 196.958 1.00 34.21 ? 3617 ASP A O     1 
ATOM   15073 C CB    . ASP A 1 3617 ? 230.062 190.274 199.752 1.00 35.63 ? 3617 ASP A CB    1 
ATOM   15074 C CG    . ASP A 1 3617 ? 231.063 189.566 200.643 1.00 40.14 ? 3617 ASP A CG    1 
ATOM   15075 O OD1   . ASP A 1 3617 ? 230.750 188.456 201.124 1.00 38.83 ? 3617 ASP A OD1   1 
ATOM   15076 O OD2   . ASP A 1 3617 ? 232.160 190.119 200.863 1.00 39.24 ? 3617 ASP A OD2   1 
ATOM   15077 N N     . ALA A 1 3618 ? 230.570 187.275 198.402 1.00 35.18 ? 3618 ALA A N     1 
ATOM   15078 C CA    . ALA A 1 3618 ? 231.447 186.395 197.645 1.00 37.17 ? 3618 ALA A CA    1 
ATOM   15079 C C     . ALA A 1 3618 ? 230.685 185.518 196.659 1.00 37.99 ? 3618 ALA A C     1 
ATOM   15080 O O     . ALA A 1 3618 ? 231.177 184.445 196.291 1.00 35.82 ? 3618 ALA A O     1 
ATOM   15081 C CB    . ALA A 1 3618 ? 232.269 185.524 198.596 1.00 36.36 ? 3618 ALA A CB    1 
ATOM   15082 N N     . PHE A 1 3619 ? 229.494 185.945 196.232 1.00 34.17 ? 3619 PHE A N     1 
ATOM   15083 C CA    . PHE A 1 3619 ? 228.708 185.146 195.298 1.00 32.20 ? 3619 PHE A CA    1 
ATOM   15084 C C     . PHE A 1 3619 ? 229.440 184.957 193.976 1.00 33.96 ? 3619 PHE A C     1 
ATOM   15085 O O     . PHE A 1 3619 ? 229.494 183.846 193.439 1.00 35.27 ? 3619 PHE A O     1 
ATOM   15086 C CB    . PHE A 1 3619 ? 227.343 185.793 195.066 1.00 31.54 ? 3619 PHE A CB    1 
ATOM   15087 C CG    . PHE A 1 3619 ? 226.546 185.137 193.977 1.00 34.56 ? 3619 PHE A CG    1 
ATOM   15088 C CD1   . PHE A 1 3619 ? 225.853 183.963 194.216 1.00 31.69 ? 3619 PHE A CD1   1 
ATOM   15089 C CD2   . PHE A 1 3619 ? 226.489 185.696 192.711 1.00 33.95 ? 3619 PHE A CD2   1 
ATOM   15090 C CE1   . PHE A 1 3619 ? 225.124 183.358 193.213 1.00 29.20 ? 3619 PHE A CE1   1 
ATOM   15091 C CE2   . PHE A 1 3619 ? 225.760 185.095 191.705 1.00 33.57 ? 3619 PHE A CE2   1 
ATOM   15092 C CZ    . PHE A 1 3619 ? 225.077 183.925 191.957 1.00 30.83 ? 3619 PHE A CZ    1 
ATOM   15093 N N     . ARG A 1 3620 ? 230.001 186.037 193.428 1.00 35.25 ? 3620 ARG A N     1 
ATOM   15094 C CA    . ARG A 1 3620 ? 230.715 185.924 192.160 1.00 36.18 ? 3620 ARG A CA    1 
ATOM   15095 C C     . ARG A 1 3620 ? 231.965 185.066 192.308 1.00 34.96 ? 3620 ARG A C     1 
ATOM   15096 O O     . ARG A 1 3620 ? 232.291 184.270 191.418 1.00 31.46 ? 3620 ARG A O     1 
ATOM   15097 C CB    . ARG A 1 3620 ? 231.073 187.311 191.627 1.00 37.29 ? 3620 ARG A CB    1 
ATOM   15098 C CG    . ARG A 1 3620 ? 229.870 188.155 191.240 1.00 36.02 ? 3620 ARG A CG    1 
ATOM   15099 C CD    . ARG A 1 3620 ? 230.201 189.087 190.087 1.00 35.25 ? 3620 ARG A CD    1 
ATOM   15100 N NE    . ARG A 1 3620 ? 231.208 188.515 189.202 1.00 35.36 ? 3620 ARG A NE    1 
ATOM   15101 C CZ    . ARG A 1 3620 ? 231.687 189.116 188.121 1.00 37.46 ? 3620 ARG A CZ    1 
ATOM   15102 N NH1   . ARG A 1 3620 ? 231.272 190.318 187.758 1.00 34.20 ? 3620 ARG A NH1   1 
ATOM   15103 N NH2   . ARG A 1 3620 ? 232.604 188.494 187.386 1.00 36.50 ? 3620 ARG A NH2   1 
ATOM   15104 N N     . LYS A 1 3621 ? 232.683 185.220 193.422 1.00 38.93 ? 3621 LYS A N     1 
ATOM   15105 C CA    . LYS A 1 3621 ? 233.873 184.408 193.654 1.00 38.74 ? 3621 LYS A CA    1 
ATOM   15106 C C     . LYS A 1 3621 ? 233.509 182.938 193.817 1.00 38.43 ? 3621 LYS A C     1 
ATOM   15107 O O     . LYS A 1 3621 ? 234.200 182.056 193.293 1.00 40.16 ? 3621 LYS A O     1 
ATOM   15108 C CB    . LYS A 1 3621 ? 234.629 184.915 194.885 1.00 38.29 ? 3621 LYS A CB    1 
ATOM   15109 C CG    . LYS A 1 3621 ? 234.840 186.430 194.950 1.00 38.73 ? 3621 LYS A CG    1 
ATOM   15110 C CD    . LYS A 1 3621 ? 235.159 187.041 193.587 1.00 38.67 ? 3621 LYS A CD    1 
ATOM   15111 C CE    . LYS A 1 3621 ? 235.137 188.559 193.643 1.00 40.03 ? 3621 LYS A CE    1 
ATOM   15112 N NZ    . LYS A 1 3621 ? 233.745 189.089 193.650 1.00 38.72 ? 3621 LYS A NZ    1 
ATOM   15113 N N     . ASN A 1 3622 ? 232.424 182.654 194.542 1.00 36.40 ? 3622 ASN A N     1 
ATOM   15114 C CA    . ASN A 1 3622 ? 231.984 181.277 194.723 1.00 35.87 ? 3622 ASN A CA    1 
ATOM   15115 C C     . ASN A 1 3622 ? 231.389 180.687 193.452 1.00 35.16 ? 3622 ASN A C     1 
ATOM   15116 O O     . ASN A 1 3622 ? 231.346 179.460 193.315 1.00 34.42 ? 3622 ASN A O     1 
ATOM   15117 C CB    . ASN A 1 3622 ? 230.959 181.199 195.856 1.00 35.13 ? 3622 ASN A CB    1 
ATOM   15118 C CG    . ASN A 1 3622 ? 231.584 180.815 197.182 1.00 36.75 ? 3622 ASN A CG    1 
ATOM   15119 O OD1   . ASN A 1 3622 ? 232.729 180.365 197.235 1.00 38.58 ? 3622 ASN A OD1   1 
ATOM   15120 N ND2   . ASN A 1 3622 ? 230.833 180.993 198.263 1.00 35.59 ? 3622 ASN A ND2   1 
ATOM   15121 N N     . LEU A 1 3623 ? 230.932 181.528 192.525 1.00 33.12 ? 3623 LEU A N     1 
ATOM   15122 C CA    . LEU A 1 3623 ? 230.313 181.058 191.293 1.00 30.79 ? 3623 LEU A CA    1 
ATOM   15123 C C     . LEU A 1 3623 ? 231.332 180.823 190.186 1.00 34.51 ? 3623 LEU A C     1 
ATOM   15124 O O     . LEU A 1 3623 ? 231.229 179.831 189.459 1.00 34.78 ? 3623 LEU A O     1 
ATOM   15125 C CB    . LEU A 1 3623 ? 229.250 182.056 190.825 1.00 31.00 ? 3623 LEU A CB    1 
ATOM   15126 C CG    . LEU A 1 3623 ? 228.806 181.983 189.362 1.00 33.51 ? 3623 LEU A CG    1 
ATOM   15127 C CD1   . LEU A 1 3623 ? 227.938 180.760 189.120 1.00 31.14 ? 3623 LEU A CD1   1 
ATOM   15128 C CD2   . LEU A 1 3623 ? 228.067 183.250 188.966 1.00 32.83 ? 3623 LEU A CD2   1 
ATOM   15129 N N     . GLU A 1 3624 ? 232.317 181.713 190.041 1.00 35.81 ? 3624 GLU A N     1 
ATOM   15130 C CA    . GLU A 1 3624 ? 233.348 181.515 189.027 1.00 36.29 ? 3624 GLU A CA    1 
ATOM   15131 C C     . GLU A 1 3624 ? 234.151 180.250 189.302 1.00 35.62 ? 3624 GLU A C     1 
ATOM   15132 O O     . GLU A 1 3624 ? 234.399 179.445 188.392 1.00 35.64 ? 3624 GLU A O     1 
ATOM   15133 C CB    . GLU A 1 3624 ? 234.271 182.732 188.980 1.00 34.63 ? 3624 GLU A CB    1 
ATOM   15134 C CG    . GLU A 1 3624 ? 233.699 183.927 188.239 1.00 34.51 ? 3624 GLU A CG    1 
ATOM   15135 C CD    . GLU A 1 3624 ? 234.123 185.246 188.854 1.00 36.44 ? 3624 GLU A CD    1 
ATOM   15136 O OE1   . GLU A 1 3624 ? 233.284 186.168 188.925 1.00 34.29 ? 3624 GLU A OE1   1 
ATOM   15137 O OE2   . GLU A 1 3624 ? 235.296 185.359 189.268 1.00 38.80 ? 3624 GLU A OE2   1 
ATOM   15138 N N     . SER A 1 3625 ? 234.561 180.058 190.558 1.00 36.03 ? 3625 SER A N     1 
ATOM   15139 C CA    . SER A 1 3625 ? 235.309 178.861 190.922 1.00 37.40 ? 3625 SER A CA    1 
ATOM   15140 C C     . SER A 1 3625 ? 234.471 177.608 190.717 1.00 37.59 ? 3625 SER A C     1 
ATOM   15141 O O     . SER A 1 3625 ? 234.975 176.589 190.235 1.00 37.03 ? 3625 SER A O     1 
ATOM   15142 C CB    . SER A 1 3625 ? 235.781 178.960 192.372 1.00 34.93 ? 3625 SER A CB    1 
ATOM   15143 O OG    . SER A 1 3625 ? 236.742 177.963 192.664 1.00 35.67 ? 3625 SER A OG    1 
ATOM   15144 N N     . ALA A 1 3626 ? 233.188 177.665 191.081 1.00 34.49 ? 3626 ALA A N     1 
ATOM   15145 C CA    . ALA A 1 3626 ? 232.311 176.516 190.881 1.00 34.23 ? 3626 ALA A CA    1 
ATOM   15146 C C     . ALA A 1 3626 ? 232.155 176.190 189.403 1.00 34.11 ? 3626 ALA A C     1 
ATOM   15147 O O     . ALA A 1 3626 ? 232.190 175.018 189.010 1.00 35.81 ? 3626 ALA A O     1 
ATOM   15148 C CB    . ALA A 1 3626 ? 230.947 176.780 191.518 1.00 31.56 ? 3626 ALA A CB    1 
ATOM   15149 N N     . LEU A 1 3627 ? 231.993 177.216 188.566 1.00 32.15 ? 3627 LEU A N     1 
ATOM   15150 C CA    . LEU A 1 3627 ? 231.779 176.990 187.142 1.00 34.22 ? 3627 LEU A CA    1 
ATOM   15151 C C     . LEU A 1 3627 ? 233.031 176.427 186.481 1.00 36.14 ? 3627 LEU A C     1 
ATOM   15152 O O     . LEU A 1 3627 ? 232.939 175.565 185.600 1.00 37.56 ? 3627 LEU A O     1 
ATOM   15153 C CB    . LEU A 1 3627 ? 231.333 178.295 186.478 1.00 33.75 ? 3627 LEU A CB    1 
ATOM   15154 C CG    . LEU A 1 3627 ? 230.867 178.316 185.020 1.00 34.64 ? 3627 LEU A CG    1 
ATOM   15155 C CD1   . LEU A 1 3627 ? 229.906 179.472 184.817 1.00 33.83 ? 3627 LEU A CD1   1 
ATOM   15156 C CD2   . LEU A 1 3627 ? 232.034 178.442 184.056 1.00 34.43 ? 3627 LEU A CD2   1 
ATOM   15157 N N     . ARG A 1 3628 ? 234.213 176.903 186.886 1.00 36.75 ? 3628 ARG A N     1 
ATOM   15158 C CA    . ARG A 1 3628 ? 235.444 176.311 186.365 1.00 38.43 ? 3628 ARG A CA    1 
ATOM   15159 C C     . ARG A 1 3628 ? 235.620 174.879 186.864 1.00 39.28 ? 3628 ARG A C     1 
ATOM   15160 O O     . ARG A 1 3628 ? 235.810 173.960 186.058 1.00 39.27 ? 3628 ARG A O     1 
ATOM   15161 C CB    . ARG A 1 3628 ? 236.642 177.206 186.722 1.00 37.95 ? 3628 ARG A CB    1 
ATOM   15162 C CG    . ARG A 1 3628 ? 238.093 176.636 186.662 1.00 38.37 ? 3628 ARG A CG    1 
ATOM   15163 C CD    . ARG A 1 3628 ? 238.394 175.506 185.664 1.00 39.19 ? 3628 ARG A CD    1 
ATOM   15164 N NE    . ARG A 1 3628 ? 238.379 175.879 184.256 1.00 38.03 ? 3628 ARG A NE    1 
ATOM   15165 C CZ    . ARG A 1 3628 ? 238.225 175.009 183.267 1.00 39.14 ? 3628 ARG A CZ    1 
ATOM   15166 N NH1   . ARG A 1 3628 ? 238.067 173.716 183.503 1.00 35.95 ? 3628 ARG A NH1   1 
ATOM   15167 N NH2   . ARG A 1 3628 ? 238.233 175.442 182.010 1.00 40.50 ? 3628 ARG A NH2   1 
ATOM   15168 N N     . PHE A 1 3629 ? 235.524 174.658 188.175 1.00 33.97 ? 3629 PHE A N     1 
ATOM   15169 C CA    . PHE A 1 3629 ? 235.777 173.326 188.715 1.00 36.27 ? 3629 PHE A CA    1 
ATOM   15170 C C     . PHE A 1 3629 ? 234.734 172.319 188.246 1.00 38.65 ? 3629 PHE A C     1 
ATOM   15171 O O     . PHE A 1 3629 ? 234.970 171.107 188.304 1.00 39.07 ? 3629 PHE A O     1 
ATOM   15172 C CB    . PHE A 1 3629 ? 235.826 173.378 190.242 1.00 37.32 ? 3629 PHE A CB    1 
ATOM   15173 C CG    . PHE A 1 3629 ? 237.027 174.100 190.785 1.00 41.35 ? 3629 PHE A CG    1 
ATOM   15174 C CD1   . PHE A 1 3629 ? 238.138 174.323 189.987 1.00 38.51 ? 3629 PHE A CD1   1 
ATOM   15175 C CD2   . PHE A 1 3629 ? 237.051 174.546 192.096 1.00 37.92 ? 3629 PHE A CD2   1 
ATOM   15176 C CE1   . PHE A 1 3629 ? 239.245 174.984 190.483 1.00 39.61 ? 3629 PHE A CE1   1 
ATOM   15177 C CE2   . PHE A 1 3629 ? 238.157 175.206 192.598 1.00 37.77 ? 3629 PHE A CE2   1 
ATOM   15178 C CZ    . PHE A 1 3629 ? 239.254 175.426 191.790 1.00 38.45 ? 3629 PHE A CZ    1 
ATOM   15179 N N     . GLY A 1 3630 ? 233.588 172.794 187.777 1.00 34.59 ? 3630 GLY A N     1 
ATOM   15180 C CA    . GLY A 1 3630 ? 232.548 171.930 187.279 1.00 33.32 ? 3630 GLY A CA    1 
ATOM   15181 C C     . GLY A 1 3630 ? 231.695 171.268 188.335 1.00 31.15 ? 3630 GLY A C     1 
ATOM   15182 O O     . GLY A 1 3630 ? 231.096 170.224 188.055 1.00 28.02 ? 3630 GLY A O     1 
ATOM   15183 N N     . ASN A 1 3631 ? 231.620 171.835 189.534 1.00 27.29 ? 3631 ASN A N     1 
ATOM   15184 C CA    . ASN A 1 3631 ? 230.806 171.242 190.577 1.00 29.15 ? 3631 ASN A CA    1 
ATOM   15185 C C     . ASN A 1 3631 ? 229.470 171.967 190.710 1.00 28.95 ? 3631 ASN A C     1 
ATOM   15186 O O     . ASN A 1 3631 ? 229.358 173.137 190.327 1.00 26.09 ? 3631 ASN A O     1 
ATOM   15187 C CB    . ASN A 1 3631 ? 231.549 171.241 191.926 1.00 29.87 ? 3631 ASN A CB    1 
ATOM   15188 C CG    . ASN A 1 3631 ? 231.874 172.637 192.441 1.00 29.65 ? 3631 ASN A CG    1 
ATOM   15189 O OD1   . ASN A 1 3631 ? 231.463 173.643 191.873 1.00 28.16 ? 3631 ASN A OD1   1 
ATOM   15190 N ND2   . ASN A 1 3631 ? 232.618 172.694 193.538 1.00 31.00 ? 3631 ASN A ND2   1 
ATOM   15191 N N     . PRO A 1 3632 ? 228.433 171.290 191.200 1.00 27.07 ? 3632 PRO A N     1 
ATOM   15192 C CA    . PRO A 1 3632 ? 227.136 171.954 191.363 1.00 24.08 ? 3632 PRO A CA    1 
ATOM   15193 C C     . PRO A 1 3632 ? 227.211 173.097 192.363 1.00 22.77 ? 3632 PRO A C     1 
ATOM   15194 O O     . PRO A 1 3632 ? 227.982 173.066 193.323 1.00 27.13 ? 3632 PRO A O     1 
ATOM   15195 C CB    . PRO A 1 3632 ? 226.216 170.832 191.865 1.00 26.54 ? 3632 PRO A CB    1 
ATOM   15196 C CG    . PRO A 1 3632 ? 227.123 169.740 192.316 1.00 26.75 ? 3632 PRO A CG    1 
ATOM   15197 C CD    . PRO A 1 3632 ? 228.364 169.852 191.502 1.00 26.94 ? 3632 PRO A CD    1 
ATOM   15198 N N     . LEU A 1 3633 ? 226.398 174.121 192.114 1.00 20.00 ? 3633 LEU A N     1 
ATOM   15199 C CA    . LEU A 1 3633 ? 226.276 175.274 192.997 1.00 22.61 ? 3633 LEU A CA    1 
ATOM   15200 C C     . LEU A 1 3633 ? 224.800 175.536 193.236 1.00 21.20 ? 3633 LEU A C     1 
ATOM   15201 O O     . LEU A 1 3633 ? 224.036 175.695 192.279 1.00 30.05 ? 3633 LEU A O     1 
ATOM   15202 C CB    . LEU A 1 3633 ? 226.953 176.510 192.398 1.00 22.50 ? 3633 LEU A CB    1 
ATOM   15203 C CG    . LEU A 1 3633 ? 226.945 177.788 193.241 1.00 19.04 ? 3633 LEU A CG    1 
ATOM   15204 C CD1   . LEU A 1 3633 ? 227.702 177.598 194.539 1.00 23.97 ? 3633 LEU A CD1   1 
ATOM   15205 C CD2   . LEU A 1 3633 ? 227.524 178.950 192.455 1.00 22.20 ? 3633 LEU A CD2   1 
ATOM   15206 N N     . LEU A 1 3634 ? 224.399 175.573 194.501 1.00 14.81 ? 3634 LEU A N     1 
ATOM   15207 C CA    . LEU A 1 3634 ? 223.015 175.836 194.876 1.00 13.64 ? 3634 LEU A CA    1 
ATOM   15208 C C     . LEU A 1 3634 ? 222.962 177.212 195.529 1.00 14.86 ? 3634 LEU A C     1 
ATOM   15209 O O     . LEU A 1 3634 ? 223.670 177.470 196.507 1.00 21.87 ? 3634 LEU A O     1 
ATOM   15210 C CB    . LEU A 1 3634 ? 222.491 174.738 195.801 1.00 17.00 ? 3634 LEU A CB    1 
ATOM   15211 C CG    . LEU A 1 3634 ? 221.130 174.860 196.491 1.00 19.89 ? 3634 LEU A CG    1 
ATOM   15212 C CD1   . LEU A 1 3634 ? 220.577 173.474 196.758 1.00 22.29 ? 3634 LEU A CD1   1 
ATOM   15213 C CD2   . LEU A 1 3634 ? 221.233 175.617 197.797 1.00 16.33 ? 3634 LEU A CD2   1 
ATOM   15214 N N     . VAL A 1 3635 ? 222.129 178.094 194.985 1.00 16.99 ? 3635 VAL A N     1 
ATOM   15215 C CA    . VAL A 1 3635 ? 222.025 179.475 195.443 1.00 18.49 ? 3635 VAL A CA    1 
ATOM   15216 C C     . VAL A 1 3635 ? 220.616 179.702 195.968 1.00 18.22 ? 3635 VAL A C     1 
ATOM   15217 O O     . VAL A 1 3635 ? 219.637 179.530 195.232 1.00 25.31 ? 3635 VAL A O     1 
ATOM   15218 C CB    . VAL A 1 3635 ? 222.359 180.470 194.323 1.00 18.26 ? 3635 VAL A CB    1 
ATOM   15219 C CG1   . VAL A 1 3635 ? 222.351 181.888 194.862 1.00 15.02 ? 3635 VAL A CG1   1 
ATOM   15220 C CG2   . VAL A 1 3635 ? 223.702 180.134 193.697 1.00 19.53 ? 3635 VAL A CG2   1 
ATOM   15221 N N     . GLN A 1 3636 ? 220.512 180.098 197.231 1.00 17.45 ? 3636 GLN A N     1 
ATOM   15222 C CA    . GLN A 1 3636 ? 219.223 180.361 197.846 1.00 16.25 ? 3636 GLN A CA    1 
ATOM   15223 C C     . GLN A 1 3636 ? 218.928 181.858 197.859 1.00 19.73 ? 3636 GLN A C     1 
ATOM   15224 O O     . GLN A 1 3636 ? 219.699 182.676 197.352 1.00 20.74 ? 3636 GLN A O     1 
ATOM   15225 C CB    . GLN A 1 3636 ? 219.179 179.794 199.264 1.00 16.69 ? 3636 GLN A CB    1 
ATOM   15226 C CG    . GLN A 1 3636 ? 219.711 178.380 199.360 1.00 21.46 ? 3636 GLN A CG    1 
ATOM   15227 C CD    . GLN A 1 3636 ? 219.369 177.710 200.672 1.00 24.40 ? 3636 GLN A CD    1 
ATOM   15228 O OE1   . GLN A 1 3636 ? 219.524 176.498 200.821 1.00 26.95 ? 3636 GLN A OE1   1 
ATOM   15229 N NE2   . GLN A 1 3636 ? 218.906 178.496 201.636 1.00 22.50 ? 3636 GLN A NE2   1 
ATOM   15230 N N     . ASP A 1 3637 ? 217.785 182.207 198.451 1.00 22.63 ? 3637 ASP A N     1 
ATOM   15231 C CA    . ASP A 1 3637 ? 217.323 183.590 198.551 1.00 20.66 ? 3637 ASP A CA    1 
ATOM   15232 C C     . ASP A 1 3637 ? 217.261 184.248 197.171 1.00 20.55 ? 3637 ASP A C     1 
ATOM   15233 O O     . ASP A 1 3637 ? 217.907 185.262 196.902 1.00 24.22 ? 3637 ASP A O     1 
ATOM   15234 C CB    . ASP A 1 3637 ? 218.207 184.396 199.510 1.00 22.21 ? 3637 ASP A CB    1 
ATOM   15235 C CG    . ASP A 1 3637 ? 218.054 183.958 200.953 1.00 26.18 ? 3637 ASP A CG    1 
ATOM   15236 O OD1   . ASP A 1 3637 ? 216.961 183.475 201.316 1.00 30.41 ? 3637 ASP A OD1   1 
ATOM   15237 O OD2   . ASP A 1 3637 ? 219.028 184.094 201.723 1.00 21.39 ? 3637 ASP A OD2   1 
ATOM   15238 N N     . VAL A 1 3638 ? 216.462 183.641 196.287 1.00 19.63 ? 3638 VAL A N     1 
ATOM   15239 C CA    . VAL A 1 3638 ? 216.296 184.169 194.934 1.00 19.27 ? 3638 VAL A CA    1 
ATOM   15240 C C     . VAL A 1 3638 ? 215.419 185.406 194.892 1.00 20.95 ? 3638 VAL A C     1 
ATOM   15241 O O     . VAL A 1 3638 ? 215.179 185.943 193.803 1.00 21.83 ? 3638 VAL A O     1 
ATOM   15242 C CB    . VAL A 1 3638 ? 215.697 183.122 193.973 1.00 20.59 ? 3638 VAL A CB    1 
ATOM   15243 C CG1   . VAL A 1 3638 ? 216.712 182.037 193.674 1.00 20.90 ? 3638 VAL A CG1   1 
ATOM   15244 C CG2   . VAL A 1 3638 ? 214.424 182.535 194.546 1.00 20.63 ? 3638 VAL A CG2   1 
ATOM   15245 N N     . GLU A 1 3639 ? 214.922 185.870 196.041 1.00 21.01 ? 3639 GLU A N     1 
ATOM   15246 C CA    . GLU A 1 3639 ? 214.151 187.108 196.071 1.00 21.32 ? 3639 GLU A CA    1 
ATOM   15247 C C     . GLU A 1 3639 ? 214.987 188.268 195.553 1.00 23.07 ? 3639 GLU A C     1 
ATOM   15248 O O     . GLU A 1 3639 ? 214.506 189.107 194.783 1.00 27.06 ? 3639 GLU A O     1 
ATOM   15249 C CB    . GLU A 1 3639 ? 213.668 187.387 197.495 1.00 23.67 ? 3639 GLU A CB    1 
ATOM   15250 C CG    . GLU A 1 3639 ? 213.233 186.154 198.289 1.00 23.25 ? 3639 GLU A CG    1 
ATOM   15251 C CD    . GLU A 1 3639 ? 212.008 185.446 197.729 1.00 24.03 ? 3639 GLU A CD    1 
ATOM   15252 O OE1   . GLU A 1 3639 ? 211.494 184.544 198.420 1.00 24.77 ? 3639 GLU A OE1   1 
ATOM   15253 O OE2   . GLU A 1 3639 ? 211.539 185.790 196.625 1.00 23.63 ? 3639 GLU A OE2   1 
ATOM   15254 N N     . SER A 1 3640 ? 216.246 188.331 195.973 1.00 21.73 ? 3640 SER A N     1 
ATOM   15255 C CA    . SER A 1 3640 ? 217.206 189.282 195.419 1.00 24.75 ? 3640 SER A CA    1 
ATOM   15256 C C     . SER A 1 3640 ? 218.066 188.596 194.355 1.00 26.60 ? 3640 SER A C     1 
ATOM   15257 O O     . SER A 1 3640 ? 219.278 188.442 194.494 1.00 29.86 ? 3640 SER A O     1 
ATOM   15258 C CB    . SER A 1 3640 ? 218.058 189.876 196.533 1.00 25.31 ? 3640 SER A CB    1 
ATOM   15259 O OG    . SER A 1 3640 ? 219.094 188.987 196.911 1.00 24.11 ? 3640 SER A OG    1 
ATOM   15260 N N     . TYR A 1 3641 ? 217.402 188.167 193.282 1.00 24.11 ? 3641 TYR A N     1 
ATOM   15261 C CA    . TYR A 1 3641 ? 218.097 187.500 192.187 1.00 23.11 ? 3641 TYR A CA    1 
ATOM   15262 C C     . TYR A 1 3641 ? 219.141 188.432 191.585 1.00 26.80 ? 3641 TYR A C     1 
ATOM   15263 O O     . TYR A 1 3641 ? 218.875 189.613 191.346 1.00 28.79 ? 3641 TYR A O     1 
ATOM   15264 C CB    . TYR A 1 3641 ? 217.094 187.049 191.121 1.00 22.73 ? 3641 TYR A CB    1 
ATOM   15265 C CG    . TYR A 1 3641 ? 217.718 186.695 189.787 1.00 17.58 ? 3641 TYR A CG    1 
ATOM   15266 C CD1   . TYR A 1 3641 ? 218.596 185.626 189.672 1.00 23.64 ? 3641 TYR A CD1   1 
ATOM   15267 C CD2   . TYR A 1 3641 ? 217.422 187.424 188.643 1.00 19.93 ? 3641 TYR A CD2   1 
ATOM   15268 C CE1   . TYR A 1 3641 ? 219.169 185.298 188.459 1.00 24.10 ? 3641 TYR A CE1   1 
ATOM   15269 C CE2   . TYR A 1 3641 ? 217.990 187.102 187.423 1.00 25.23 ? 3641 TYR A CE2   1 
ATOM   15270 C CZ    . TYR A 1 3641 ? 218.863 186.037 187.338 1.00 24.63 ? 3641 TYR A CZ    1 
ATOM   15271 O OH    . TYR A 1 3641 ? 219.433 185.710 186.128 1.00 23.86 ? 3641 TYR A OH    1 
ATOM   15272 N N     . ASP A 1 3642 ? 220.337 187.900 191.348 1.00 28.28 ? 3642 ASP A N     1 
ATOM   15273 C CA    . ASP A 1 3642 ? 221.451 188.722 190.896 1.00 28.36 ? 3642 ASP A CA    1 
ATOM   15274 C C     . ASP A 1 3642 ? 221.516 188.636 189.377 1.00 26.90 ? 3642 ASP A C     1 
ATOM   15275 O O     . ASP A 1 3642 ? 221.611 187.527 188.836 1.00 29.44 ? 3642 ASP A O     1 
ATOM   15276 C CB    . ASP A 1 3642 ? 222.756 188.246 191.528 1.00 28.88 ? 3642 ASP A CB    1 
ATOM   15277 C CG    . ASP A 1 3642 ? 223.995 188.967 190.992 1.00 31.26 ? 3642 ASP A CG    1 
ATOM   15278 O OD1   . ASP A 1 3642 ? 224.871 189.300 191.818 1.00 31.88 ? 3642 ASP A OD1   1 
ATOM   15279 O OD2   . ASP A 1 3642 ? 224.104 189.241 189.782 1.00 31.47 ? 3642 ASP A OD2   1 
ATOM   15280 N N     . PRO A 1 3643 ? 221.475 189.760 188.657 1.00 23.46 ? 3643 PRO A N     1 
ATOM   15281 C CA    . PRO A 1 3643 ? 221.370 189.698 187.191 1.00 24.83 ? 3643 PRO A CA    1 
ATOM   15282 C C     . PRO A 1 3643 ? 222.605 189.157 186.481 1.00 28.50 ? 3643 PRO A C     1 
ATOM   15283 O O     . PRO A 1 3643 ? 222.573 189.053 185.249 1.00 25.96 ? 3643 PRO A O     1 
ATOM   15284 C CB    . PRO A 1 3643 ? 221.113 191.158 186.799 1.00 27.15 ? 3643 PRO A CB    1 
ATOM   15285 C CG    . PRO A 1 3643 ? 220.525 191.778 188.020 1.00 29.57 ? 3643 PRO A CG    1 
ATOM   15286 C CD    . PRO A 1 3643 ? 221.216 191.114 189.172 1.00 27.13 ? 3643 PRO A CD    1 
ATOM   15287 N N     . VAL A 1 3644 ? 223.683 188.805 187.189 1.00 31.06 ? 3644 VAL A N     1 
ATOM   15288 C CA    . VAL A 1 3644 ? 224.858 188.300 186.485 1.00 31.32 ? 3644 VAL A CA    1 
ATOM   15289 C C     . VAL A 1 3644 ? 224.625 186.869 186.017 1.00 31.29 ? 3644 VAL A C     1 
ATOM   15290 O O     . VAL A 1 3644 ? 225.372 186.362 185.174 1.00 35.09 ? 3644 VAL A O     1 
ATOM   15291 C CB    . VAL A 1 3644 ? 226.127 188.376 187.361 1.00 31.65 ? 3644 VAL A CB    1 
ATOM   15292 C CG1   . VAL A 1 3644 ? 226.057 187.393 188.524 1.00 27.38 ? 3644 VAL A CG1   1 
ATOM   15293 C CG2   . VAL A 1 3644 ? 227.393 188.186 186.529 1.00 31.24 ? 3644 VAL A CG2   1 
ATOM   15294 N N     . LEU A 1 3645 ? 223.595 186.207 186.537 1.00 29.38 ? 3645 LEU A N     1 
ATOM   15295 C CA    . LEU A 1 3645 ? 223.274 184.841 186.151 1.00 30.44 ? 3645 LEU A CA    1 
ATOM   15296 C C     . LEU A 1 3645 ? 222.520 184.756 184.832 1.00 31.20 ? 3645 LEU A C     1 
ATOM   15297 O O     . LEU A 1 3645 ? 222.272 183.643 184.355 1.00 31.52 ? 3645 LEU A O     1 
ATOM   15298 C CB    . LEU A 1 3645 ? 222.455 184.164 187.252 1.00 27.89 ? 3645 LEU A CB    1 
ATOM   15299 C CG    . LEU A 1 3645 ? 223.248 183.438 188.339 1.00 32.53 ? 3645 LEU A CG    1 
ATOM   15300 C CD1   . LEU A 1 3645 ? 222.310 182.659 189.247 1.00 27.72 ? 3645 LEU A CD1   1 
ATOM   15301 C CD2   . LEU A 1 3645 ? 224.296 182.523 187.726 1.00 31.32 ? 3645 LEU A CD2   1 
ATOM   15302 N N     . ASN A 1 3646 ? 222.142 185.891 184.242 1.00 25.59 ? 3646 ASN A N     1 
ATOM   15303 C CA    . ASN A 1 3646 ? 221.414 185.863 182.975 1.00 21.69 ? 3646 ASN A CA    1 
ATOM   15304 C C     . ASN A 1 3646 ? 222.151 185.099 181.882 1.00 27.05 ? 3646 ASN A C     1 
ATOM   15305 O O     . ASN A 1 3646 ? 221.508 184.292 181.191 1.00 33.86 ? 3646 ASN A O     1 
ATOM   15306 C CB    . ASN A 1 3646 ? 221.087 187.293 182.532 1.00 25.47 ? 3646 ASN A CB    1 
ATOM   15307 C CG    . ASN A 1 3646 ? 219.907 187.879 183.278 1.00 29.02 ? 3646 ASN A CG    1 
ATOM   15308 O OD1   . ASN A 1 3646 ? 218.880 187.224 183.449 1.00 29.90 ? 3646 ASN A OD1   1 
ATOM   15309 N ND2   . ASN A 1 3646 ? 220.044 189.123 183.717 1.00 30.13 ? 3646 ASN A ND2   1 
ATOM   15310 N N     . PRO A 1 3647 ? 223.456 185.300 181.649 1.00 28.01 ? 3647 PRO A N     1 
ATOM   15311 C CA    . PRO A 1 3647 ? 224.143 184.436 180.673 1.00 30.52 ? 3647 PRO A CA    1 
ATOM   15312 C C     . PRO A 1 3647 ? 224.120 182.968 181.054 1.00 29.56 ? 3647 PRO A C     1 
ATOM   15313 O O     . PRO A 1 3647 ? 224.044 182.101 180.175 1.00 33.32 ? 3647 PRO A O     1 
ATOM   15314 C CB    . PRO A 1 3647 ? 225.571 184.997 180.654 1.00 31.98 ? 3647 PRO A CB    1 
ATOM   15315 C CG    . PRO A 1 3647 ? 225.435 186.393 181.127 1.00 31.94 ? 3647 PRO A CG    1 
ATOM   15316 C CD    . PRO A 1 3647 ? 224.357 186.350 182.158 1.00 29.93 ? 3647 PRO A CD    1 
ATOM   15317 N N     . VAL A 1 3648 ? 224.184 182.665 182.351 1.00 26.10 ? 3648 VAL A N     1 
ATOM   15318 C CA    . VAL A 1 3648 ? 224.181 181.275 182.795 1.00 25.99 ? 3648 VAL A CA    1 
ATOM   15319 C C     . VAL A 1 3648 ? 222.813 180.646 182.565 1.00 21.22 ? 3648 VAL A C     1 
ATOM   15320 O O     . VAL A 1 3648 ? 222.705 179.513 182.083 1.00 26.74 ? 3648 VAL A O     1 
ATOM   15321 C CB    . VAL A 1 3648 ? 224.605 181.189 184.272 1.00 28.12 ? 3648 VAL A CB    1 
ATOM   15322 C CG1   . VAL A 1 3648 ? 224.506 179.759 184.776 1.00 26.92 ? 3648 VAL A CG1   1 
ATOM   15323 C CG2   . VAL A 1 3648 ? 226.014 181.733 184.451 1.00 25.07 ? 3648 VAL A CG2   1 
ATOM   15324 N N     . LEU A 1 3649 ? 221.746 181.372 182.905 1.00 16.65 ? 3649 LEU A N     1 
ATOM   15325 C CA    . LEU A 1 3649 ? 220.400 180.836 182.724 1.00 22.55 ? 3649 LEU A CA    1 
ATOM   15326 C C     . LEU A 1 3649 ? 220.025 180.752 181.249 1.00 23.97 ? 3649 LEU A C     1 
ATOM   15327 O O     . LEU A 1 3649 ? 219.293 179.843 180.841 1.00 20.16 ? 3649 LEU A O     1 
ATOM   15328 C CB    . LEU A 1 3649 ? 219.388 181.684 183.492 1.00 21.43 ? 3649 LEU A CB    1 
ATOM   15329 C CG    . LEU A 1 3649 ? 219.610 181.799 185.000 1.00 20.41 ? 3649 LEU A CG    1 
ATOM   15330 C CD1   . LEU A 1 3649 ? 218.377 182.378 185.665 1.00 16.44 ? 3649 LEU A CD1   1 
ATOM   15331 C CD2   . LEU A 1 3649 ? 219.963 180.450 185.604 1.00 21.91 ? 3649 LEU A CD2   1 
ATOM   15332 N N     . ASN A 1 3650 ? 220.502 181.695 180.437 1.00 19.54 ? 3650 ASN A N     1 
ATOM   15333 C CA    . ASN A 1 3650 ? 220.240 181.657 179.005 1.00 19.34 ? 3650 ASN A CA    1 
ATOM   15334 C C     . ASN A 1 3650 ? 221.032 180.577 178.289 1.00 23.32 ? 3650 ASN A C     1 
ATOM   15335 O O     . ASN A 1 3650 ? 220.632 180.169 177.193 1.00 24.06 ? 3650 ASN A O     1 
ATOM   15336 C CB    . ASN A 1 3650 ? 220.555 183.015 178.378 1.00 23.41 ? 3650 ASN A CB    1 
ATOM   15337 C CG    . ASN A 1 3650 ? 219.425 184.003 178.536 1.00 21.33 ? 3650 ASN A CG    1 
ATOM   15338 O OD1   . ASN A 1 3650 ? 218.333 183.645 178.970 1.00 21.33 ? 3650 ASN A OD1   1 
ATOM   15339 N ND2   . ASN A 1 3650 ? 219.683 185.257 178.194 1.00 20.89 ? 3650 ASN A ND2   1 
ATOM   15340 N N     . ARG A 1 3651 ? 222.129 180.104 178.881 1.00 22.09 ? 3651 ARG A N     1 
ATOM   15341 C CA    . ARG A 1 3651 ? 223.024 179.151 178.232 1.00 23.41 ? 3651 ARG A CA    1 
ATOM   15342 C C     . ARG A 1 3651 ? 223.514 179.696 176.892 1.00 32.17 ? 3651 ARG A C     1 
ATOM   15343 O O     . ARG A 1 3651 ? 223.625 178.973 175.900 1.00 32.06 ? 3651 ARG A O     1 
ATOM   15344 C CB    . ARG A 1 3651 ? 222.348 177.789 178.064 1.00 22.47 ? 3651 ARG A CB    1 
ATOM   15345 C CG    . ARG A 1 3651 ? 222.079 177.078 179.379 1.00 23.31 ? 3651 ARG A CG    1 
ATOM   15346 C CD    . ARG A 1 3651 ? 221.612 175.654 179.152 1.00 22.76 ? 3651 ARG A CD    1 
ATOM   15347 N NE    . ARG A 1 3651 ? 221.501 174.913 180.402 1.00 21.00 ? 3651 ARG A NE    1 
ATOM   15348 C CZ    . ARG A 1 3651 ? 221.300 173.605 180.478 1.00 24.99 ? 3651 ARG A CZ    1 
ATOM   15349 N NH1   . ARG A 1 3651 ? 221.193 172.858 179.392 1.00 26.07 ? 3651 ARG A NH1   1 
ATOM   15350 N NH2   . ARG A 1 3651 ? 221.214 173.030 181.674 1.00 22.21 ? 3651 ARG A NH2   1 
ATOM   15351 N N     . GLU A 1 3652 ? 223.820 180.994 176.872 1.00 35.95 ? 3652 GLU A N     1 
ATOM   15352 C CA    . GLU A 1 3652 ? 224.276 181.686 175.675 1.00 34.93 ? 3652 GLU A CA    1 
ATOM   15353 C C     . GLU A 1 3652 ? 225.781 181.550 175.457 1.00 36.71 ? 3652 GLU A C     1 
ATOM   15354 O O     . GLU A 1 3652 ? 226.367 182.350 174.720 1.00 40.68 ? 3652 GLU A O     1 
ATOM   15355 C CB    . GLU A 1 3652 ? 223.859 183.161 175.741 1.00 35.35 ? 3652 GLU A CB    1 
ATOM   15356 C CG    . GLU A 1 3652 ? 224.408 183.934 176.936 1.00 35.62 ? 3652 GLU A CG    1 
ATOM   15357 C CD    . GLU A 1 3652 ? 225.732 184.618 176.653 1.00 38.33 ? 3652 GLU A CD    1 
ATOM   15358 O OE1   . GLU A 1 3652 ? 226.032 184.879 175.469 1.00 36.83 ? 3652 GLU A OE1   1 
ATOM   15359 O OE2   . GLU A 1 3652 ? 226.478 184.888 177.615 1.00 38.56 ? 3652 GLU A OE2   1 
ATOM   15360 N N     . VAL A 1 3653 ? 226.408 180.542 176.070 1.00 35.38 ? 3653 VAL A N     1 
ATOM   15361 C CA    . VAL A 1 3653 ? 227.837 180.313 175.888 1.00 36.46 ? 3653 VAL A CA    1 
ATOM   15362 C C     . VAL A 1 3653 ? 228.149 180.144 174.408 1.00 37.74 ? 3653 VAL A C     1 
ATOM   15363 O O     . VAL A 1 3653 ? 227.456 179.419 173.683 1.00 37.48 ? 3653 VAL A O     1 
ATOM   15364 C CB    . VAL A 1 3653 ? 228.283 179.092 176.707 1.00 41.61 ? 3653 VAL A CB    1 
ATOM   15365 C CG1   . VAL A 1 3653 ? 227.438 177.873 176.361 1.00 37.72 ? 3653 VAL A CG1   1 
ATOM   15366 C CG2   . VAL A 1 3653 ? 229.753 178.797 176.470 1.00 40.71 ? 3653 VAL A CG2   1 
ATOM   15367 N N     . ARG A 1 3654 ? 229.191 180.834 173.947 1.00 41.40 ? 3654 ARG A N     1 
ATOM   15368 C CA    . ARG A 1 3654 ? 229.575 180.815 172.537 1.00 42.41 ? 3654 ARG A CA    1 
ATOM   15369 C C     . ARG A 1 3654 ? 230.463 179.601 172.288 1.00 43.75 ? 3654 ARG A C     1 
ATOM   15370 O O     . ARG A 1 3654 ? 231.603 179.535 172.755 1.00 46.06 ? 3654 ARG A O     1 
ATOM   15371 C CB    . ARG A 1 3654 ? 230.256 182.124 172.148 1.00 40.54 ? 3654 ARG A CB    1 
ATOM   15372 C CG    . ARG A 1 3654 ? 231.386 182.566 173.067 1.00 40.38 ? 3654 ARG A CG    1 
ATOM   15373 C CD    . ARG A 1 3654 ? 232.048 183.834 172.553 1.00 40.65 ? 3654 ARG A CD    1 
ATOM   15374 N NE    . ARG A 1 3654 ? 233.120 184.286 173.431 1.00 41.88 ? 3654 ARG A NE    1 
ATOM   15375 C CZ    . ARG A 1 3654 ? 234.388 183.914 173.319 1.00 43.04 ? 3654 ARG A CZ    1 
ATOM   15376 N NH1   . ARG A 1 3654 ? 234.783 183.079 172.372 1.00 42.93 ? 3654 ARG A NH1   1 
ATOM   15377 N NH2   . ARG A 1 3654 ? 235.282 184.392 174.180 1.00 43.20 ? 3654 ARG A NH2   1 
ATOM   15378 N N     . ARG A 1 3655 ? 229.926 178.624 171.558 1.00 42.11 ? 3655 ARG A N     1 
ATOM   15379 C CA    . ARG A 1 3655 ? 230.663 177.416 171.212 1.00 43.39 ? 3655 ARG A CA    1 
ATOM   15380 C C     . ARG A 1 3655 ? 231.498 177.589 169.948 1.00 44.36 ? 3655 ARG A C     1 
ATOM   15381 O O     . ARG A 1 3655 ? 232.309 176.711 169.631 1.00 43.41 ? 3655 ARG A O     1 
ATOM   15382 C CB    . ARG A 1 3655 ? 229.678 176.249 171.056 1.00 42.02 ? 3655 ARG A CB    1 
ATOM   15383 C CG    . ARG A 1 3655 ? 230.304 174.875 170.865 1.00 40.71 ? 3655 ARG A CG    1 
ATOM   15384 C CD    . ARG A 1 3655 ? 229.264 173.773 171.000 1.00 41.91 ? 3655 ARG A CD    1 
ATOM   15385 N NE    . ARG A 1 3655 ? 228.622 173.780 172.309 1.00 45.18 ? 3655 ARG A NE    1 
ATOM   15386 C CZ    . ARG A 1 3655 ? 229.017 173.050 173.342 1.00 44.16 ? 3655 ARG A CZ    1 
ATOM   15387 N NH1   . ARG A 1 3655 ? 230.058 172.238 173.258 1.00 42.03 ? 3655 ARG A NH1   1 
ATOM   15388 N NH2   . ARG A 1 3655 ? 228.349 173.135 174.490 1.00 41.11 ? 3655 ARG A NH2   1 
ATOM   15389 N N     . THR A 1 3656 ? 231.336 178.709 169.237 1.00 42.49 ? 3656 THR A N     1 
ATOM   15390 C CA    . THR A 1 3656 ? 232.084 178.930 168.003 1.00 42.89 ? 3656 THR A CA    1 
ATOM   15391 C C     . THR A 1 3656 ? 233.587 178.939 168.258 1.00 42.48 ? 3656 THR A C     1 
ATOM   15392 O O     . THR A 1 3656 ? 234.370 178.466 167.425 1.00 40.95 ? 3656 THR A O     1 
ATOM   15393 C CB    . THR A 1 3656 ? 231.642 180.241 167.351 1.00 43.65 ? 3656 THR A CB    1 
ATOM   15394 O OG1   . THR A 1 3656 ? 230.218 180.238 167.189 1.00 43.24 ? 3656 THR A OG1   1 
ATOM   15395 C CG2   . THR A 1 3656 ? 232.296 180.411 165.987 1.00 41.37 ? 3656 THR A CG2   1 
ATOM   15396 N N     . GLY A 1 3657 ? 234.009 179.466 169.406 1.00 41.63 ? 3657 GLY A N     1 
ATOM   15397 C CA    . GLY A 1 3657 ? 235.420 179.450 169.738 1.00 41.55 ? 3657 GLY A CA    1 
ATOM   15398 C C     . GLY A 1 3657 ? 235.924 178.040 169.977 1.00 41.71 ? 3657 GLY A C     1 
ATOM   15399 O O     . GLY A 1 3657 ? 235.149 177.099 170.159 1.00 41.71 ? 3657 GLY A O     1 
ATOM   15400 N N     . GLY A 1 3658 ? 237.249 177.897 169.966 1.00 37.18 ? 3658 GLY A N     1 
ATOM   15401 C CA    . GLY A 1 3658 ? 237.880 176.602 170.139 1.00 35.43 ? 3658 GLY A CA    1 
ATOM   15402 C C     . GLY A 1 3658 ? 237.484 175.917 171.430 1.00 36.11 ? 3658 GLY A C     1 
ATOM   15403 O O     . GLY A 1 3658 ? 237.177 174.721 171.440 1.00 35.72 ? 3658 GLY A O     1 
ATOM   15404 N N     . ARG A 1 3659 ? 237.489 176.666 172.527 1.00 40.38 ? 3659 ARG A N     1 
ATOM   15405 C CA    . ARG A 1 3659 ? 237.004 176.184 173.810 1.00 41.67 ? 3659 ARG A CA    1 
ATOM   15406 C C     . ARG A 1 3659 ? 235.694 176.880 174.159 1.00 43.51 ? 3659 ARG A C     1 
ATOM   15407 O O     . ARG A 1 3659 ? 235.455 178.026 173.769 1.00 42.89 ? 3659 ARG A O     1 
ATOM   15408 C CB    . ARG A 1 3659 ? 238.044 176.416 174.911 1.00 41.37 ? 3659 ARG A CB    1 
ATOM   15409 C CG    . ARG A 1 3659 ? 238.238 177.872 175.298 1.00 38.41 ? 3659 ARG A CG    1 
ATOM   15410 C CD    . ARG A 1 3659 ? 239.412 178.041 176.247 1.00 39.57 ? 3659 ARG A CD    1 
ATOM   15411 N NE    . ARG A 1 3659 ? 239.299 177.181 177.420 1.00 43.45 ? 3659 ARG A NE    1 
ATOM   15412 C CZ    . ARG A 1 3659 ? 240.307 176.879 178.226 1.00 44.61 ? 3659 ARG A CZ    1 
ATOM   15413 N NH1   . ARG A 1 3659 ? 241.526 177.350 178.016 1.00 43.60 ? 3659 ARG A NH1   1 
ATOM   15414 N NH2   . ARG A 1 3659 ? 240.088 176.084 179.269 1.00 43.91 ? 3659 ARG A NH2   1 
ATOM   15415 N N     . VAL A 1 3660 ? 234.837 176.170 174.892 1.00 41.98 ? 3660 VAL A N     1 
ATOM   15416 C CA    . VAL A 1 3660 ? 233.518 176.690 175.235 1.00 41.56 ? 3660 VAL A CA    1 
ATOM   15417 C C     . VAL A 1 3660 ? 233.649 177.760 176.313 1.00 37.74 ? 3660 VAL A C     1 
ATOM   15418 O O     . VAL A 1 3660 ? 233.752 177.457 177.506 1.00 34.06 ? 3660 VAL A O     1 
ATOM   15419 C CB    . VAL A 1 3660 ? 232.568 175.554 175.663 1.00 40.21 ? 3660 VAL A CB    1 
ATOM   15420 C CG1   . VAL A 1 3660 ? 232.124 174.762 174.446 1.00 38.20 ? 3660 VAL A CG1   1 
ATOM   15421 C CG2   . VAL A 1 3660 ? 233.255 174.617 176.648 1.00 36.07 ? 3660 VAL A CG2   1 
ATOM   15422 N N     . LEU A 1 3661 ? 233.633 179.022 175.896 1.00 38.94 ? 3661 LEU A N     1 
ATOM   15423 C CA    . LEU A 1 3661 ? 233.820 180.160 176.786 1.00 40.49 ? 3661 LEU A CA    1 
ATOM   15424 C C     . LEU A 1 3661 ? 232.494 180.881 176.979 1.00 39.37 ? 3661 LEU A C     1 
ATOM   15425 O O     . LEU A 1 3661 ? 231.821 181.222 176.000 1.00 38.33 ? 3661 LEU A O     1 
ATOM   15426 C CB    . LEU A 1 3661 ? 234.862 181.128 176.220 1.00 40.67 ? 3661 LEU A CB    1 
ATOM   15427 C CG    . LEU A 1 3661 ? 236.341 180.787 176.403 1.00 42.14 ? 3661 LEU A CG    1 
ATOM   15428 C CD1   . LEU A 1 3661 ? 237.195 181.599 175.442 1.00 38.69 ? 3661 LEU A CD1   1 
ATOM   15429 C CD2   . LEU A 1 3661 ? 236.779 181.029 177.837 1.00 40.74 ? 3661 LEU A CD2   1 
ATOM   15430 N N     . ILE A 1 3662 ? 232.124 181.114 178.235 1.00 36.25 ? 3662 ILE A N     1 
ATOM   15431 C CA    . ILE A 1 3662 ? 230.946 181.904 178.572 1.00 37.46 ? 3662 ILE A CA    1 
ATOM   15432 C C     . ILE A 1 3662 ? 231.403 183.305 178.953 1.00 38.87 ? 3662 ILE A C     1 
ATOM   15433 O O     . ILE A 1 3662 ? 232.454 183.481 179.585 1.00 38.43 ? 3662 ILE A O     1 
ATOM   15434 C CB    . ILE A 1 3662 ? 230.122 181.243 179.699 1.00 37.17 ? 3662 ILE A CB    1 
ATOM   15435 C CG1   . ILE A 1 3662 ? 228.680 181.752 179.680 1.00 39.85 ? 3662 ILE A CG1   1 
ATOM   15436 C CG2   . ILE A 1 3662 ? 230.741 181.479 181.068 1.00 36.43 ? 3662 ILE A CG2   1 
ATOM   15437 C CD1   . ILE A 1 3662 ? 227.780 181.056 180.676 1.00 35.17 ? 3662 ILE A CD1   1 
ATOM   15438 N N     . THR A 1 3663 ? 230.639 184.310 178.531 1.00 37.73 ? 3663 THR A N     1 
ATOM   15439 C CA    . THR A 1 3663 ? 230.992 185.705 178.796 1.00 40.30 ? 3663 THR A CA    1 
ATOM   15440 C C     . THR A 1 3663 ? 230.317 186.196 180.080 1.00 37.65 ? 3663 THR A C     1 
ATOM   15441 O O     . THR A 1 3663 ? 229.535 187.146 180.106 1.00 36.01 ? 3663 THR A O     1 
ATOM   15442 C CB    . THR A 1 3663 ? 230.651 186.577 177.589 1.00 39.83 ? 3663 THR A CB    1 
ATOM   15443 O OG1   . THR A 1 3663 ? 230.994 187.942 177.861 1.00 40.31 ? 3663 THR A OG1   1 
ATOM   15444 C CG2   . THR A 1 3663 ? 229.178 186.460 177.197 1.00 35.84 ? 3663 THR A CG2   1 
ATOM   15445 N N     . LEU A 1 3664 ? 230.663 185.522 181.174 1.00 36.78 ? 3664 LEU A N     1 
ATOM   15446 C CA    . LEU A 1 3664 ? 230.145 185.874 182.492 1.00 37.32 ? 3664 LEU A CA    1 
ATOM   15447 C C     . LEU A 1 3664 ? 230.741 187.207 182.922 1.00 37.41 ? 3664 LEU A C     1 
ATOM   15448 O O     . LEU A 1 3664 ? 231.897 187.269 183.354 1.00 39.23 ? 3664 LEU A O     1 
ATOM   15449 C CB    . LEU A 1 3664 ? 230.480 184.776 183.496 1.00 36.57 ? 3664 LEU A CB    1 
ATOM   15450 C CG    . LEU A 1 3664 ? 229.779 184.843 184.852 1.00 37.33 ? 3664 LEU A CG    1 
ATOM   15451 C CD1   . LEU A 1 3664 ? 228.308 185.165 184.666 1.00 37.82 ? 3664 LEU A CD1   1 
ATOM   15452 C CD2   . LEU A 1 3664 ? 229.956 183.540 185.613 1.00 36.56 ? 3664 LEU A CD2   1 
ATOM   15453 N N     . GLY A 1 3665 ? 229.954 188.274 182.818 1.00 37.49 ? 3665 GLY A N     1 
ATOM   15454 C CA    . GLY A 1 3665 ? 230.487 189.588 183.099 1.00 37.38 ? 3665 GLY A CA    1 
ATOM   15455 C C     . GLY A 1 3665 ? 231.401 190.066 181.979 1.00 39.42 ? 3665 GLY A C     1 
ATOM   15456 O O     . GLY A 1 3665 ? 231.343 189.601 180.837 1.00 39.08 ? 3665 GLY A O     1 
ATOM   15457 N N     . ASP A 1 3666 ? 232.265 191.021 182.333 1.00 39.53 ? 3666 ASP A N     1 
ATOM   15458 C CA    . ASP A 1 3666 ? 233.183 191.591 181.352 1.00 39.95 ? 3666 ASP A CA    1 
ATOM   15459 C C     . ASP A 1 3666 ? 234.144 190.539 180.812 1.00 42.09 ? 3666 ASP A C     1 
ATOM   15460 O O     . ASP A 1 3666 ? 234.438 190.513 179.611 1.00 41.03 ? 3666 ASP A O     1 
ATOM   15461 C CB    . ASP A 1 3666 ? 233.959 192.752 181.975 1.00 40.84 ? 3666 ASP A CB    1 
ATOM   15462 C CG    . ASP A 1 3666 ? 233.070 193.932 182.310 1.00 44.28 ? 3666 ASP A CG    1 
ATOM   15463 O OD1   . ASP A 1 3666 ? 231.857 193.725 182.524 1.00 43.24 ? 3666 ASP A OD1   1 
ATOM   15464 O OD2   . ASP A 1 3666 ? 233.587 195.068 182.364 1.00 44.63 ? 3666 ASP A OD2   1 
ATOM   15465 N N     . GLN A 1 3667 ? 234.641 189.665 181.680 1.00 41.56 ? 3667 GLN A N     1 
ATOM   15466 C CA    . GLN A 1 3667 ? 235.638 188.683 181.286 1.00 42.27 ? 3667 GLN A CA    1 
ATOM   15467 C C     . GLN A 1 3667 ? 234.976 187.369 180.878 1.00 42.19 ? 3667 GLN A C     1 
ATOM   15468 O O     . GLN A 1 3667 ? 233.819 187.100 181.212 1.00 40.61 ? 3667 GLN A O     1 
ATOM   15469 C CB    . GLN A 1 3667 ? 236.623 188.452 182.431 1.00 42.05 ? 3667 GLN A CB    1 
ATOM   15470 C CG    . GLN A 1 3667 ? 237.972 187.917 182.004 1.00 43.01 ? 3667 GLN A CG    1 
ATOM   15471 C CD    . GLN A 1 3667 ? 238.130 186.461 182.361 1.00 42.58 ? 3667 GLN A CD    1 
ATOM   15472 O OE1   . GLN A 1 3667 ? 237.551 185.992 183.340 1.00 40.41 ? 3667 GLN A OE1   1 
ATOM   15473 N NE2   . GLN A 1 3667 ? 238.908 185.733 181.568 1.00 43.51 ? 3667 GLN A NE2   1 
ATOM   15474 N N     . ASP A 1 3668 ? 235.727 186.550 180.144 1.00 40.88 ? 3668 ASP A N     1 
ATOM   15475 C CA    . ASP A 1 3668 ? 235.233 185.288 179.608 1.00 40.99 ? 3668 ASP A CA    1 
ATOM   15476 C C     . ASP A 1 3668 ? 235.774 184.122 180.427 1.00 42.98 ? 3668 ASP A C     1 
ATOM   15477 O O     . ASP A 1 3668 ? 236.961 184.093 180.768 1.00 42.95 ? 3668 ASP A O     1 
ATOM   15478 C CB    . ASP A 1 3668 ? 235.632 185.128 178.140 1.00 40.51 ? 3668 ASP A CB    1 
ATOM   15479 C CG    . ASP A 1 3668 ? 234.919 186.111 177.232 1.00 43.56 ? 3668 ASP A CG    1 
ATOM   15480 O OD1   . ASP A 1 3668 ? 233.949 186.750 177.690 1.00 42.52 ? 3668 ASP A OD1   1 
ATOM   15481 O OD2   . ASP A 1 3668 ? 235.329 186.245 176.060 1.00 45.49 ? 3668 ASP A OD2   1 
ATOM   15482 N N     . ILE A 1 3669 ? 234.901 183.165 180.736 1.00 41.86 ? 3669 ILE A N     1 
ATOM   15483 C CA    . ILE A 1 3669 ? 235.244 181.987 181.524 1.00 40.58 ? 3669 ILE A CA    1 
ATOM   15484 C C     . ILE A 1 3669 ? 234.793 180.750 180.758 1.00 38.57 ? 3669 ILE A C     1 
ATOM   15485 O O     . ILE A 1 3669 ? 233.694 180.734 180.193 1.00 40.42 ? 3669 ILE A O     1 
ATOM   15486 C CB    . ILE A 1 3669 ? 234.598 182.035 182.922 1.00 40.92 ? 3669 ILE A CB    1 
ATOM   15487 C CG1   . ILE A 1 3669 ? 235.088 183.260 183.697 1.00 39.22 ? 3669 ILE A CG1   1 
ATOM   15488 C CG2   . ILE A 1 3669 ? 234.897 180.765 183.702 1.00 41.13 ? 3669 ILE A CG2   1 
ATOM   15489 C CD1   . ILE A 1 3669 ? 234.099 184.404 183.724 1.00 38.15 ? 3669 ILE A CD1   1 
ATOM   15490 N N     . ASP A 1 3670 ? 235.643 179.726 180.727 1.00 38.37 ? 3670 ASP A N     1 
ATOM   15491 C CA    . ASP A 1 3670 ? 235.283 178.482 180.060 1.00 39.14 ? 3670 ASP A CA    1 
ATOM   15492 C C     . ASP A 1 3670 ? 234.251 177.717 180.880 1.00 39.91 ? 3670 ASP A C     1 
ATOM   15493 O O     . ASP A 1 3670 ? 234.415 177.517 182.087 1.00 38.22 ? 3670 ASP A O     1 
ATOM   15494 C CB    . ASP A 1 3670 ? 236.521 177.615 179.832 1.00 38.28 ? 3670 ASP A CB    1 
ATOM   15495 C CG    . ASP A 1 3670 ? 236.236 176.404 178.968 1.00 43.16 ? 3670 ASP A CG    1 
ATOM   15496 O OD1   . ASP A 1 3670 ? 235.819 175.362 179.517 1.00 41.07 ? 3670 ASP A OD1   1 
ATOM   15497 O OD2   . ASP A 1 3670 ? 236.435 176.491 177.738 1.00 42.25 ? 3670 ASP A OD2   1 
ATOM   15498 N N     . LEU A 1 3671 ? 233.187 177.277 180.211 1.00 39.99 ? 3671 LEU A N     1 
ATOM   15499 C CA    . LEU A 1 3671 ? 232.065 176.615 180.869 1.00 38.87 ? 3671 LEU A CA    1 
ATOM   15500 C C     . LEU A 1 3671 ? 232.342 175.119 180.959 1.00 39.67 ? 3671 LEU A C     1 
ATOM   15501 O O     . LEU A 1 3671 ? 232.413 174.429 179.936 1.00 38.02 ? 3671 LEU A O     1 
ATOM   15502 C CB    . LEU A 1 3671 ? 230.767 176.886 180.113 1.00 39.79 ? 3671 LEU A CB    1 
ATOM   15503 C CG    . LEU A 1 3671 ? 229.579 175.997 180.483 1.00 38.95 ? 3671 LEU A CG    1 
ATOM   15504 C CD1   . LEU A 1 3671 ? 228.945 176.459 181.785 1.00 35.34 ? 3671 LEU A CD1   1 
ATOM   15505 C CD2   . LEU A 1 3671 ? 228.557 175.978 179.357 1.00 38.18 ? 3671 LEU A CD2   1 
ATOM   15506 N N     . SER A 1 3672 ? 232.499 174.619 182.181 1.00 37.42 ? 3672 SER A N     1 
ATOM   15507 C CA    . SER A 1 3672 ? 232.679 173.189 182.375 1.00 35.16 ? 3672 SER A CA    1 
ATOM   15508 C C     . SER A 1 3672 ? 231.367 172.458 182.095 1.00 35.53 ? 3672 SER A C     1 
ATOM   15509 O O     . SER A 1 3672 ? 230.297 172.923 182.500 1.00 37.75 ? 3672 SER A O     1 
ATOM   15510 C CB    . SER A 1 3672 ? 233.151 172.893 183.797 1.00 35.59 ? 3672 SER A CB    1 
ATOM   15511 O OG    . SER A 1 3672 ? 233.301 171.500 184.006 1.00 34.53 ? 3672 SER A OG    1 
ATOM   15512 N N     . PRO A 1 3673 ? 231.416 171.318 181.403 1.00 34.12 ? 3673 PRO A N     1 
ATOM   15513 C CA    . PRO A 1 3673 ? 230.169 170.615 181.056 1.00 35.15 ? 3673 PRO A CA    1 
ATOM   15514 C C     . PRO A 1 3673 ? 229.389 170.111 182.257 1.00 33.14 ? 3673 PRO A C     1 
ATOM   15515 O O     . PRO A 1 3673 ? 228.181 169.873 182.132 1.00 34.91 ? 3673 PRO A O     1 
ATOM   15516 C CB    . PRO A 1 3673 ? 230.654 169.453 180.177 1.00 33.70 ? 3673 PRO A CB    1 
ATOM   15517 C CG    . PRO A 1 3673 ? 232.085 169.259 180.557 1.00 34.79 ? 3673 PRO A CG    1 
ATOM   15518 C CD    . PRO A 1 3673 ? 232.609 170.621 180.895 1.00 34.37 ? 3673 PRO A CD    1 
ATOM   15519 N N     . SER A 1 3674 ? 230.029 169.938 183.412 1.00 28.65 ? 3674 SER A N     1 
ATOM   15520 C CA    . SER A 1 3674 ? 229.375 169.383 184.588 1.00 30.94 ? 3674 SER A CA    1 
ATOM   15521 C C     . SER A 1 3674 ? 228.797 170.451 185.508 1.00 29.10 ? 3674 SER A C     1 
ATOM   15522 O O     . SER A 1 3674 ? 228.267 170.115 186.572 1.00 31.70 ? 3674 SER A O     1 
ATOM   15523 C CB    . SER A 1 3674 ? 230.352 168.498 185.365 1.00 32.35 ? 3674 SER A CB    1 
ATOM   15524 O OG    . SER A 1 3674 ? 231.413 169.262 185.908 1.00 31.97 ? 3674 SER A OG    1 
ATOM   15525 N N     . PHE A 1 3675 ? 228.886 171.724 185.130 1.00 26.60 ? 3675 PHE A N     1 
ATOM   15526 C CA    . PHE A 1 3675 ? 228.333 172.807 185.941 1.00 26.19 ? 3675 PHE A CA    1 
ATOM   15527 C C     . PHE A 1 3675 ? 226.814 172.775 185.879 1.00 27.31 ? 3675 PHE A C     1 
ATOM   15528 O O     . PHE A 1 3675 ? 226.217 172.936 184.813 1.00 28.95 ? 3675 PHE A O     1 
ATOM   15529 C CB    . PHE A 1 3675 ? 228.855 174.158 185.471 1.00 26.74 ? 3675 PHE A CB    1 
ATOM   15530 C CG    . PHE A 1 3675 ? 228.203 175.322 186.158 1.00 24.30 ? 3675 PHE A CG    1 
ATOM   15531 C CD1   . PHE A 1 3675 ? 228.393 175.543 187.510 1.00 26.40 ? 3675 PHE A CD1   1 
ATOM   15532 C CD2   . PHE A 1 3675 ? 227.386 176.188 185.452 1.00 25.36 ? 3675 PHE A CD2   1 
ATOM   15533 C CE1   . PHE A 1 3675 ? 227.788 176.611 188.143 1.00 26.21 ? 3675 PHE A CE1   1 
ATOM   15534 C CE2   . PHE A 1 3675 ? 226.778 177.257 186.079 1.00 25.35 ? 3675 PHE A CE2   1 
ATOM   15535 C CZ    . PHE A 1 3675 ? 226.979 177.469 187.427 1.00 26.27 ? 3675 PHE A CZ    1 
ATOM   15536 N N     . VAL A 1 3676 ? 226.180 172.561 187.031 1.00 23.79 ? 3676 VAL A N     1 
ATOM   15537 C CA    . VAL A 1 3676 ? 224.738 172.733 187.167 1.00 19.81 ? 3676 VAL A CA    1 
ATOM   15538 C C     . VAL A 1 3676 ? 224.467 173.704 188.311 1.00 15.87 ? 3676 VAL A C     1 
ATOM   15539 O O     . VAL A 1 3676 ? 225.016 173.564 189.410 1.00 16.99 ? 3676 VAL A O     1 
ATOM   15540 C CB    . VAL A 1 3676 ? 224.020 171.379 187.358 1.00 16.81 ? 3676 VAL A CB    1 
ATOM   15541 C CG1   . VAL A 1 3676 ? 224.440 170.402 186.271 1.00 21.05 ? 3676 VAL A CG1   1 
ATOM   15542 C CG2   . VAL A 1 3676 ? 224.320 170.774 188.719 1.00 16.49 ? 3676 VAL A CG2   1 
ATOM   15543 N N     . ILE A 1 3677 ? 223.665 174.728 188.047 1.00 17.40 ? 3677 ILE A N     1 
ATOM   15544 C CA    . ILE A 1 3677 ? 223.318 175.701 189.076 1.00 13.00 ? 3677 ILE A CA    1 
ATOM   15545 C C     . ILE A 1 3677 ? 221.911 175.413 189.582 1.00 15.15 ? 3677 ILE A C     1 
ATOM   15546 O O     . ILE A 1 3677 ? 221.035 174.961 188.836 1.00 25.76 ? 3677 ILE A O     1 
ATOM   15547 C CB    . ILE A 1 3677 ? 223.452 177.144 188.543 1.00 11.68 ? 3677 ILE A CB    1 
ATOM   15548 C CG1   . ILE A 1 3677 ? 223.313 178.165 189.672 1.00 13.95 ? 3677 ILE A CG1   1 
ATOM   15549 C CG2   . ILE A 1 3677 ? 222.414 177.436 187.497 1.00 18.05 ? 3677 ILE A CG2   1 
ATOM   15550 C CD1   . ILE A 1 3677 ? 224.557 178.348 190.484 1.00 19.20 ? 3677 ILE A CD1   1 
ATOM   15551 N N     . PHE A 1 3678 ? 221.695 175.658 190.870 1.00 8.71  ? 3678 PHE A N     1 
ATOM   15552 C CA    . PHE A 1 3678 ? 220.395 175.451 191.485 1.00 8.00  ? 3678 PHE A CA    1 
ATOM   15553 C C     . PHE A 1 3678 ? 219.969 176.729 192.188 1.00 11.77 ? 3678 PHE A C     1 
ATOM   15554 O O     . PHE A 1 3678 ? 220.763 177.373 192.876 1.00 17.37 ? 3678 PHE A O     1 
ATOM   15555 C CB    . PHE A 1 3678 ? 220.421 174.287 192.484 1.00 14.18 ? 3678 PHE A CB    1 
ATOM   15556 C CG    . PHE A 1 3678 ? 220.538 172.938 191.838 1.00 18.30 ? 3678 PHE A CG    1 
ATOM   15557 C CD1   . PHE A 1 3678 ? 219.449 172.360 191.211 1.00 17.74 ? 3678 PHE A CD1   1 
ATOM   15558 C CD2   . PHE A 1 3678 ? 221.740 172.253 191.849 1.00 19.28 ? 3678 PHE A CD2   1 
ATOM   15559 C CE1   . PHE A 1 3678 ? 219.555 171.121 190.612 1.00 16.22 ? 3678 PHE A CE1   1 
ATOM   15560 C CE2   . PHE A 1 3678 ? 221.851 171.015 191.253 1.00 18.45 ? 3678 PHE A CE2   1 
ATOM   15561 C CZ    . PHE A 1 3678 ? 220.757 170.448 190.633 1.00 14.18 ? 3678 PHE A CZ    1 
ATOM   15562 N N     . LEU A 1 3679 ? 218.706 177.091 192.003 1.00 11.55 ? 3679 LEU A N     1 
ATOM   15563 C CA    . LEU A 1 3679 ? 218.118 178.247 192.656 1.00 12.29 ? 3679 LEU A CA    1 
ATOM   15564 C C     . LEU A 1 3679 ? 217.003 177.785 193.582 1.00 11.49 ? 3679 LEU A C     1 
ATOM   15565 O O     . LEU A 1 3679 ? 216.289 176.824 193.287 1.00 13.81 ? 3679 LEU A O     1 
ATOM   15566 C CB    . LEU A 1 3679 ? 217.573 179.254 191.639 1.00 15.41 ? 3679 LEU A CB    1 
ATOM   15567 C CG    . LEU A 1 3679 ? 218.502 179.697 190.508 1.00 13.07 ? 3679 LEU A CG    1 
ATOM   15568 C CD1   . LEU A 1 3679 ? 217.867 180.830 189.722 1.00 12.91 ? 3679 LEU A CD1   1 
ATOM   15569 C CD2   . LEU A 1 3679 ? 219.853 180.116 191.056 1.00 13.78 ? 3679 LEU A CD2   1 
ATOM   15570 N N     . SER A 1 3680 ? 216.864 178.475 194.709 1.00 6.64  ? 3680 SER A N     1 
ATOM   15571 C CA    . SER A 1 3680 ? 215.873 178.101 195.704 1.00 10.47 ? 3680 SER A CA    1 
ATOM   15572 C C     . SER A 1 3680 ? 215.453 179.340 196.476 1.00 16.14 ? 3680 SER A C     1 
ATOM   15573 O O     . SER A 1 3680 ? 216.155 180.354 196.491 1.00 19.60 ? 3680 SER A O     1 
ATOM   15574 C CB    . SER A 1 3680 ? 216.414 177.032 196.661 1.00 14.90 ? 3680 SER A CB    1 
ATOM   15575 O OG    . SER A 1 3680 ? 215.398 176.562 197.530 1.00 19.93 ? 3680 SER A OG    1 
ATOM   15576 N N     . THR A 1 3681 ? 214.292 179.246 197.119 1.00 14.30 ? 3681 THR A N     1 
ATOM   15577 C CA    . THR A 1 3681 ? 213.786 180.315 197.963 1.00 14.50 ? 3681 THR A CA    1 
ATOM   15578 C C     . THR A 1 3681 ? 213.255 179.704 199.251 1.00 19.67 ? 3681 THR A C     1 
ATOM   15579 O O     . THR A 1 3681 ? 212.991 178.502 199.333 1.00 19.43 ? 3681 THR A O     1 
ATOM   15580 C CB    . THR A 1 3681 ? 212.691 181.124 197.262 1.00 12.93 ? 3681 THR A CB    1 
ATOM   15581 O OG1   . THR A 1 3681 ? 212.352 182.261 198.064 1.00 21.53 ? 3681 THR A OG1   1 
ATOM   15582 C CG2   . THR A 1 3681 ? 211.453 180.278 197.079 1.00 19.07 ? 3681 THR A CG2   1 
ATOM   15583 N N     . ARG A 1 3682 ? 213.098 180.549 200.268 1.00 22.87 ? 3682 ARG A N     1 
ATOM   15584 C CA    . ARG A 1 3682 ? 212.549 180.125 201.547 1.00 22.20 ? 3682 ARG A CA    1 
ATOM   15585 C C     . ARG A 1 3682 ? 211.099 180.559 201.711 1.00 22.92 ? 3682 ARG A C     1 
ATOM   15586 O O     . ARG A 1 3682 ? 210.463 180.195 202.706 1.00 26.45 ? 3682 ARG A O     1 
ATOM   15587 C CB    . ARG A 1 3682 ? 213.392 180.683 202.700 1.00 26.41 ? 3682 ARG A CB    1 
ATOM   15588 C CG    . ARG A 1 3682 ? 214.837 180.214 202.698 1.00 26.30 ? 3682 ARG A CG    1 
ATOM   15589 C CD    . ARG A 1 3682 ? 214.927 178.725 202.955 1.00 22.82 ? 3682 ARG A CD    1 
ATOM   15590 N NE    . ARG A 1 3682 ? 214.436 178.385 204.285 1.00 25.21 ? 3682 ARG A NE    1 
ATOM   15591 C CZ    . ARG A 1 3682 ? 214.088 177.163 204.662 1.00 26.77 ? 3682 ARG A CZ    1 
ATOM   15592 N NH1   . ARG A 1 3682 ? 214.163 176.138 203.832 1.00 27.30 ? 3682 ARG A NH1   1 
ATOM   15593 N NH2   . ARG A 1 3682 ? 213.654 176.966 205.904 1.00 24.68 ? 3682 ARG A NH2   1 
ATOM   15594 N N     . ASP A 1 3683 ? 210.560 181.313 200.757 1.00 22.73 ? 3683 ASP A N     1 
ATOM   15595 C CA    . ASP A 1 3683 ? 209.238 181.900 200.848 1.00 24.37 ? 3683 ASP A CA    1 
ATOM   15596 C C     . ASP A 1 3683 ? 208.245 181.041 200.075 1.00 26.11 ? 3683 ASP A C     1 
ATOM   15597 O O     . ASP A 1 3683 ? 208.489 180.691 198.916 1.00 28.44 ? 3683 ASP A O     1 
ATOM   15598 C CB    . ASP A 1 3683 ? 209.259 183.339 200.304 1.00 22.91 ? 3683 ASP A CB    1 
ATOM   15599 C CG    . ASP A 1 3683 ? 207.880 183.991 200.235 1.00 30.88 ? 3683 ASP A CG    1 
ATOM   15600 O OD1   . ASP A 1 3683 ? 207.788 185.179 200.607 1.00 32.65 ? 3683 ASP A OD1   1 
ATOM   15601 O OD2   . ASP A 1 3683 ? 206.901 183.369 199.780 1.00 30.76 ? 3683 ASP A OD2   1 
ATOM   15602 N N     . PRO A 1 3684 ? 207.118 180.679 200.697 1.00 28.91 ? 3684 PRO A N     1 
ATOM   15603 C CA    . PRO A 1 3684 ? 206.150 179.790 200.038 1.00 25.73 ? 3684 PRO A CA    1 
ATOM   15604 C C     . PRO A 1 3684 ? 205.589 180.333 198.732 1.00 24.86 ? 3684 PRO A C     1 
ATOM   15605 O O     . PRO A 1 3684 ? 205.349 179.563 197.798 1.00 24.55 ? 3684 PRO A O     1 
ATOM   15606 C CB    . PRO A 1 3684 ? 205.044 179.636 201.090 1.00 27.79 ? 3684 PRO A CB    1 
ATOM   15607 C CG    . PRO A 1 3684 ? 205.184 180.831 201.973 1.00 30.32 ? 3684 PRO A CG    1 
ATOM   15608 C CD    . PRO A 1 3684 ? 206.650 181.128 202.018 1.00 28.71 ? 3684 PRO A CD    1 
ATOM   15609 N N     . THR A 1 3685 ? 205.371 181.644 198.649 1.00 27.09 ? 3685 THR A N     1 
ATOM   15610 C CA    . THR A 1 3685 ? 204.759 182.220 197.460 1.00 32.24 ? 3685 THR A CA    1 
ATOM   15611 C C     . THR A 1 3685 ? 205.117 183.698 197.349 1.00 29.74 ? 3685 THR A C     1 
ATOM   15612 O O     . THR A 1 3685 ? 204.914 184.474 198.287 1.00 25.37 ? 3685 THR A O     1 
ATOM   15613 C CB    . THR A 1 3685 ? 203.235 182.013 197.470 1.00 33.70 ? 3685 THR A CB    1 
ATOM   15614 O OG1   . THR A 1 3685 ? 202.657 182.582 196.290 1.00 32.62 ? 3685 THR A OG1   1 
ATOM   15615 C CG2   . THR A 1 3685 ? 202.585 182.610 198.716 1.00 30.28 ? 3685 THR A CG2   1 
ATOM   15616 N N     . VAL A 1 3686 ? 205.657 184.074 196.190 1.00 32.05 ? 3686 VAL A N     1 
ATOM   15617 C CA    . VAL A 1 3686 ? 206.127 185.433 195.947 1.00 33.42 ? 3686 VAL A CA    1 
ATOM   15618 C C     . VAL A 1 3686 ? 206.203 185.647 194.442 1.00 33.37 ? 3686 VAL A C     1 
ATOM   15619 O O     . VAL A 1 3686 ? 206.421 184.707 193.673 1.00 35.36 ? 3686 VAL A O     1 
ATOM   15620 C CB    . VAL A 1 3686 ? 207.494 185.684 196.629 1.00 31.25 ? 3686 VAL A CB    1 
ATOM   15621 C CG1   . VAL A 1 3686 ? 208.569 184.815 196.003 1.00 29.40 ? 3686 VAL A CG1   1 
ATOM   15622 C CG2   . VAL A 1 3686 ? 207.875 187.157 196.572 1.00 30.51 ? 3686 VAL A CG2   1 
ATOM   15623 N N     . GLU A 1 3687 ? 206.006 186.894 194.021 1.00 28.37 ? 3687 GLU A N     1 
ATOM   15624 C CA    . GLU A 1 3687 ? 206.045 187.238 192.606 1.00 29.62 ? 3687 GLU A CA    1 
ATOM   15625 C C     . GLU A 1 3687 ? 207.485 187.285 192.110 1.00 30.75 ? 3687 GLU A C     1 
ATOM   15626 O O     . GLU A 1 3687 ? 208.389 187.708 192.836 1.00 28.81 ? 3687 GLU A O     1 
ATOM   15627 C CB    . GLU A 1 3687 ? 205.360 188.583 192.369 1.00 29.83 ? 3687 GLU A CB    1 
ATOM   15628 C CG    . GLU A 1 3687 ? 203.995 188.707 193.021 1.00 31.90 ? 3687 GLU A CG    1 
ATOM   15629 C CD    . GLU A 1 3687 ? 202.858 188.595 192.025 1.00 36.33 ? 3687 GLU A CD    1 
ATOM   15630 O OE1   . GLU A 1 3687 ? 201.700 188.858 192.411 1.00 36.92 ? 3687 GLU A OE1   1 
ATOM   15631 O OE2   . GLU A 1 3687 ? 203.121 188.243 190.856 1.00 35.58 ? 3687 GLU A OE2   1 
ATOM   15632 N N     . PHE A 1 3688 ? 207.694 186.849 190.866 1.00 29.16 ? 3688 PHE A N     1 
ATOM   15633 C CA    . PHE A 1 3688 ? 208.991 186.894 190.213 1.00 25.83 ? 3688 PHE A CA    1 
ATOM   15634 C C     . PHE A 1 3688 ? 208.904 187.694 188.916 1.00 27.74 ? 3688 PHE A C     1 
ATOM   15635 O O     . PHE A 1 3688 ? 207.855 187.715 188.264 1.00 29.83 ? 3688 PHE A O     1 
ATOM   15636 C CB    . PHE A 1 3688 ? 209.511 185.488 189.888 1.00 23.16 ? 3688 PHE A CB    1 
ATOM   15637 C CG    . PHE A 1 3688 ? 210.047 184.744 191.075 1.00 25.37 ? 3688 PHE A CG    1 
ATOM   15638 C CD1   . PHE A 1 3688 ? 209.196 184.045 191.913 1.00 27.33 ? 3688 PHE A CD1   1 
ATOM   15639 C CD2   . PHE A 1 3688 ? 211.403 184.741 191.350 1.00 22.86 ? 3688 PHE A CD2   1 
ATOM   15640 C CE1   . PHE A 1 3688 ? 209.689 183.354 193.002 1.00 27.01 ? 3688 PHE A CE1   1 
ATOM   15641 C CE2   . PHE A 1 3688 ? 211.901 184.056 192.440 1.00 23.72 ? 3688 PHE A CE2   1 
ATOM   15642 C CZ    . PHE A 1 3688 ? 211.042 183.361 193.267 1.00 26.76 ? 3688 PHE A CZ    1 
ATOM   15643 N N     . PRO A 1 3689 ? 209.980 188.366 188.517 1.00 24.38 ? 3689 PRO A N     1 
ATOM   15644 C CA    . PRO A 1 3689 ? 209.992 189.047 187.219 1.00 21.10 ? 3689 PRO A CA    1 
ATOM   15645 C C     . PRO A 1 3689 ? 209.915 188.044 186.083 1.00 19.23 ? 3689 PRO A C     1 
ATOM   15646 O O     . PRO A 1 3689 ? 210.559 186.985 186.135 1.00 14.87 ? 3689 PRO A O     1 
ATOM   15647 C CB    . PRO A 1 3689 ? 211.336 189.791 187.221 1.00 20.59 ? 3689 PRO A CB    1 
ATOM   15648 C CG    . PRO A 1 3689 ? 212.177 189.043 188.199 1.00 21.49 ? 3689 PRO A CG    1 
ATOM   15649 C CD    . PRO A 1 3689 ? 211.230 188.583 189.264 1.00 20.44 ? 3689 PRO A CD    1 
ATOM   15650 N N     . PRO A 1 3690 ? 209.138 188.341 185.037 1.00 20.24 ? 3690 PRO A N     1 
ATOM   15651 C CA    . PRO A 1 3690 ? 208.982 187.371 183.939 1.00 17.66 ? 3690 PRO A CA    1 
ATOM   15652 C C     . PRO A 1 3690 ? 210.283 187.022 183.242 1.00 16.51 ? 3690 PRO A C     1 
ATOM   15653 O O     . PRO A 1 3690 ? 210.416 185.906 182.721 1.00 18.38 ? 3690 PRO A O     1 
ATOM   15654 C CB    . PRO A 1 3690 ? 208.001 188.074 182.990 1.00 17.14 ? 3690 PRO A CB    1 
ATOM   15655 C CG    . PRO A 1 3690 ? 207.283 189.064 183.845 1.00 19.21 ? 3690 PRO A CG    1 
ATOM   15656 C CD    . PRO A 1 3690 ? 208.284 189.526 184.857 1.00 19.92 ? 3690 PRO A CD    1 
ATOM   15657 N N     . ASP A 1 3691 ? 211.246 187.945 183.206 1.00 20.17 ? 3691 ASP A N     1 
ATOM   15658 C CA    . ASP A 1 3691 ? 212.535 187.634 182.598 1.00 17.26 ? 3691 ASP A CA    1 
ATOM   15659 C C     . ASP A 1 3691 ? 213.244 186.509 183.341 1.00 17.74 ? 3691 ASP A C     1 
ATOM   15660 O O     . ASP A 1 3691 ? 213.853 185.638 182.711 1.00 13.21 ? 3691 ASP A O     1 
ATOM   15661 C CB    . ASP A 1 3691 ? 213.402 188.896 182.527 1.00 13.94 ? 3691 ASP A CB    1 
ATOM   15662 C CG    . ASP A 1 3691 ? 213.724 189.479 183.895 1.00 22.58 ? 3691 ASP A CG    1 
ATOM   15663 O OD1   . ASP A 1 3691 ? 213.381 190.657 184.127 1.00 22.81 ? 3691 ASP A OD1   1 
ATOM   15664 O OD2   . ASP A 1 3691 ? 214.338 188.781 184.730 1.00 22.90 ? 3691 ASP A OD2   1 
ATOM   15665 N N     . LEU A 1 3692 ? 213.186 186.512 184.675 1.00 17.73 ? 3692 LEU A N     1 
ATOM   15666 C CA    . LEU A 1 3692 ? 213.691 185.373 185.433 1.00 16.14 ? 3692 LEU A CA    1 
ATOM   15667 C C     . LEU A 1 3692 ? 212.780 184.163 185.282 1.00 14.58 ? 3692 LEU A C     1 
ATOM   15668 O O     . LEU A 1 3692 ? 213.259 183.024 185.284 1.00 17.04 ? 3692 LEU A O     1 
ATOM   15669 C CB    . LEU A 1 3692 ? 213.841 185.748 186.907 1.00 16.87 ? 3692 LEU A CB    1 
ATOM   15670 C CG    . LEU A 1 3692 ? 214.237 184.638 187.883 1.00 11.64 ? 3692 LEU A CG    1 
ATOM   15671 C CD1   . LEU A 1 3692 ? 215.531 183.970 187.453 1.00 10.22 ? 3692 LEU A CD1   1 
ATOM   15672 C CD2   . LEU A 1 3692 ? 214.357 185.190 189.290 1.00 19.44 ? 3692 LEU A CD2   1 
ATOM   15673 N N     . CYS A 1 3693 ? 211.473 184.392 185.140 1.00 15.64 ? 3693 CYS A N     1 
ATOM   15674 C CA    . CYS A 1 3693 ? 210.523 183.290 185.040 1.00 12.12 ? 3693 CYS A CA    1 
ATOM   15675 C C     . CYS A 1 3693 ? 210.776 182.436 183.807 1.00 9.90  ? 3693 CYS A C     1 
ATOM   15676 O O     . CYS A 1 3693 ? 210.675 181.207 183.872 1.00 14.30 ? 3693 CYS A O     1 
ATOM   15677 C CB    . CYS A 1 3693 ? 209.096 183.835 185.006 1.00 14.77 ? 3693 CYS A CB    1 
ATOM   15678 S SG    . CYS A 1 3693 ? 208.420 184.252 186.615 1.00 19.83 ? 3693 CYS A SG    1 
ATOM   15679 N N     . SER A 1 3694 ? 211.106 183.062 182.682 1.00 10.02 ? 3694 SER A N     1 
ATOM   15680 C CA    . SER A 1 3694 ? 211.301 182.346 181.429 1.00 4.92  ? 3694 SER A CA    1 
ATOM   15681 C C     . SER A 1 3694 ? 212.623 181.593 181.369 1.00 7.92  ? 3694 SER A C     1 
ATOM   15682 O O     . SER A 1 3694 ? 212.844 180.839 180.417 1.00 7.59  ? 3694 SER A O     1 
ATOM   15683 C CB    . SER A 1 3694 ? 211.213 183.318 180.248 1.00 8.05  ? 3694 SER A CB    1 
ATOM   15684 O OG    . SER A 1 3694 ? 212.269 184.261 180.279 1.00 14.31 ? 3694 SER A OG    1 
ATOM   15685 N N     . ARG A 1 3695 ? 213.500 181.770 182.354 1.00 11.42 ? 3695 ARG A N     1 
ATOM   15686 C CA    . ARG A 1 3695 ? 214.827 181.174 182.328 1.00 12.11 ? 3695 ARG A CA    1 
ATOM   15687 C C     . ARG A 1 3695 ? 215.002 180.029 183.314 1.00 13.43 ? 3695 ARG A C     1 
ATOM   15688 O O     . ARG A 1 3695 ? 216.086 179.440 183.368 1.00 15.36 ? 3695 ARG A O     1 
ATOM   15689 C CB    . ARG A 1 3695 ? 215.884 182.249 182.597 1.00 9.32  ? 3695 ARG A CB    1 
ATOM   15690 C CG    . ARG A 1 3695 ? 216.003 183.267 181.486 1.00 11.05 ? 3695 ARG A CG    1 
ATOM   15691 C CD    . ARG A 1 3695 ? 217.055 184.311 181.794 1.00 15.83 ? 3695 ARG A CD    1 
ATOM   15692 N NE    . ARG A 1 3695 ? 217.181 185.270 180.704 1.00 14.50 ? 3695 ARG A NE    1 
ATOM   15693 C CZ    . ARG A 1 3695 ? 216.494 186.399 180.612 1.00 16.67 ? 3695 ARG A CZ    1 
ATOM   15694 N NH1   . ARG A 1 3695 ? 215.622 186.754 181.539 1.00 17.27 ? 3695 ARG A NH1   1 
ATOM   15695 N NH2   . ARG A 1 3695 ? 216.688 187.194 179.564 1.00 15.99 ? 3695 ARG A NH2   1 
ATOM   15696 N N     . VAL A 1 3696 ? 213.974 179.694 184.092 1.00 11.22 ? 3696 VAL A N     1 
ATOM   15697 C CA    . VAL A 1 3696 ? 214.066 178.639 185.090 1.00 12.66 ? 3696 VAL A CA    1 
ATOM   15698 C C     . VAL A 1 3696 ? 212.823 177.764 185.019 1.00 12.59 ? 3696 VAL A C     1 
ATOM   15699 O O     . VAL A 1 3696 ? 211.754 178.193 184.581 1.00 13.35 ? 3696 VAL A O     1 
ATOM   15700 C CB    . VAL A 1 3696 ? 214.236 179.202 186.516 1.00 6.54  ? 3696 VAL A CB    1 
ATOM   15701 C CG1   . VAL A 1 3696 ? 215.579 179.898 186.666 1.00 6.38  ? 3696 VAL A CG1   1 
ATOM   15702 C CG2   . VAL A 1 3696 ? 213.110 180.157 186.826 1.00 5.14  ? 3696 VAL A CG2   1 
ATOM   15703 N N     . THR A 1 3697 ? 212.979 176.520 185.466 1.00 5.75  ? 3697 THR A N     1 
ATOM   15704 C CA    . THR A 1 3697 ? 211.864 175.596 185.638 1.00 2.66  ? 3697 THR A CA    1 
ATOM   15705 C C     . THR A 1 3697 ? 211.424 175.646 187.095 1.00 7.36  ? 3697 THR A C     1 
ATOM   15706 O O     . THR A 1 3697 ? 212.054 175.032 187.960 1.00 16.87 ? 3697 THR A O     1 
ATOM   15707 C CB    . THR A 1 3697 ? 212.245 174.171 185.243 1.00 5.13  ? 3697 THR A CB    1 
ATOM   15708 O OG1   . THR A 1 3697 ? 213.316 173.710 186.073 1.00 1.68  ? 3697 THR A OG1   1 
ATOM   15709 C CG2   . THR A 1 3697 ? 212.655 174.097 183.786 1.00 14.38 ? 3697 THR A CG2   1 
ATOM   15710 N N     . PHE A 1 3698 ? 210.345 176.379 187.362 1.00 9.40  ? 3698 PHE A N     1 
ATOM   15711 C CA    . PHE A 1 3698 ? 209.759 176.415 188.695 1.00 3.47  ? 3698 PHE A CA    1 
ATOM   15712 C C     . PHE A 1 3698 ? 209.404 175.023 189.187 1.00 7.84  ? 3698 PHE A C     1 
ATOM   15713 O O     . PHE A 1 3698 ? 208.560 174.341 188.599 1.00 10.21 ? 3698 PHE A O     1 
ATOM   15714 C CB    . PHE A 1 3698 ? 208.514 177.301 188.715 1.00 5.39  ? 3698 PHE A CB    1 
ATOM   15715 C CG    . PHE A 1 3698 ? 208.809 178.762 188.601 1.00 5.09  ? 3698 PHE A CG    1 
ATOM   15716 C CD1   . PHE A 1 3698 ? 210.083 179.244 188.834 1.00 4.70  ? 3698 PHE A CD1   1 
ATOM   15717 C CD2   . PHE A 1 3698 ? 207.816 179.653 188.247 1.00 8.21  ? 3698 PHE A CD2   1 
ATOM   15718 C CE1   . PHE A 1 3698 ? 210.354 180.587 188.737 1.00 6.75  ? 3698 PHE A CE1   1 
ATOM   15719 C CE2   . PHE A 1 3698 ? 208.086 180.995 188.141 1.00 11.44 ? 3698 PHE A CE2   1 
ATOM   15720 C CZ    . PHE A 1 3698 ? 209.357 181.463 188.386 1.00 13.13 ? 3698 PHE A CZ    1 
ATOM   15721 N N     . VAL A 1 3699 ? 210.054 174.595 190.261 1.00 11.15 ? 3699 VAL A N     1 
ATOM   15722 C CA    . VAL A 1 3699 ? 209.689 173.383 190.979 1.00 7.25  ? 3699 VAL A CA    1 
ATOM   15723 C C     . VAL A 1 3699 ? 209.190 173.812 192.354 1.00 5.79  ? 3699 VAL A C     1 
ATOM   15724 O O     . VAL A 1 3699 ? 209.910 174.470 193.115 1.00 14.26 ? 3699 VAL A O     1 
ATOM   15725 C CB    . VAL A 1 3699 ? 210.859 172.384 191.038 1.00 2.78  ? 3699 VAL A CB    1 
ATOM   15726 C CG1   . VAL A 1 3699 ? 212.045 172.928 191.821 1.00 11.43 ? 3699 VAL A CG1   1 
ATOM   15727 C CG2   . VAL A 1 3699 ? 210.398 171.075 191.615 1.00 8.01  ? 3699 VAL A CG2   1 
ATOM   15728 N N     . ASN A 1 3700 ? 207.935 173.494 192.648 1.00 3.69  ? 3700 ASN A N     1 
ATOM   15729 C CA    . ASN A 1 3700 ? 207.224 174.074 193.780 1.00 5.46  ? 3700 ASN A CA    1 
ATOM   15730 C C     . ASN A 1 3700 ? 206.934 172.986 194.802 1.00 6.89  ? 3700 ASN A C     1 
ATOM   15731 O O     . ASN A 1 3700 ? 206.117 172.094 194.550 1.00 7.84  ? 3700 ASN A O     1 
ATOM   15732 C CB    . ASN A 1 3700 ? 205.929 174.745 193.314 1.00 7.58  ? 3700 ASN A CB    1 
ATOM   15733 C CG    . ASN A 1 3700 ? 205.106 175.292 194.456 1.00 7.77  ? 3700 ASN A CG    1 
ATOM   15734 O OD1   . ASN A 1 3700 ? 205.305 176.425 194.890 1.00 9.55  ? 3700 ASN A OD1   1 
ATOM   15735 N ND2   . ASN A 1 3700 ? 204.163 174.494 194.940 1.00 12.56 ? 3700 ASN A ND2   1 
ATOM   15736 N N     . PHE A 1 3701 ? 207.596 173.067 195.952 1.00 6.68  ? 3701 PHE A N     1 
ATOM   15737 C CA    . PHE A 1 3701 ? 207.372 172.140 197.050 1.00 10.66 ? 3701 PHE A CA    1 
ATOM   15738 C C     . PHE A 1 3701 ? 206.330 172.648 198.034 1.00 10.96 ? 3701 PHE A C     1 
ATOM   15739 O O     . PHE A 1 3701 ? 206.089 171.994 199.052 1.00 11.88 ? 3701 PHE A O     1 
ATOM   15740 C CB    . PHE A 1 3701 ? 208.683 171.866 197.792 1.00 11.73 ? 3701 PHE A CB    1 
ATOM   15741 C CG    . PHE A 1 3701 ? 209.669 171.046 197.011 1.00 8.12  ? 3701 PHE A CG    1 
ATOM   15742 C CD1   . PHE A 1 3701 ? 210.394 171.609 195.975 1.00 9.53  ? 3701 PHE A CD1   1 
ATOM   15743 C CD2   . PHE A 1 3701 ? 209.874 169.713 197.314 1.00 7.15  ? 3701 PHE A CD2   1 
ATOM   15744 C CE1   . PHE A 1 3701 ? 211.301 170.859 195.260 1.00 7.81  ? 3701 PHE A CE1   1 
ATOM   15745 C CE2   . PHE A 1 3701 ? 210.782 168.958 196.601 1.00 10.41 ? 3701 PHE A CE2   1 
ATOM   15746 C CZ    . PHE A 1 3701 ? 211.497 169.533 195.574 1.00 7.46  ? 3701 PHE A CZ    1 
ATOM   15747 N N     . THR A 1 3702 ? 205.712 173.793 197.753 1.00 9.17  ? 3702 THR A N     1 
ATOM   15748 C CA    . THR A 1 3702 ? 204.739 174.371 198.669 1.00 6.44  ? 3702 THR A CA    1 
ATOM   15749 C C     . THR A 1 3702 ? 203.557 173.432 198.853 1.00 11.69 ? 3702 THR A C     1 
ATOM   15750 O O     . THR A 1 3702 ? 203.122 172.758 197.916 1.00 17.00 ? 3702 THR A O     1 
ATOM   15751 C CB    . THR A 1 3702 ? 204.259 175.727 198.152 1.00 8.36  ? 3702 THR A CB    1 
ATOM   15752 O OG1   . THR A 1 3702 ? 205.382 176.491 197.698 1.00 12.26 ? 3702 THR A OG1   1 
ATOM   15753 C CG2   . THR A 1 3702 ? 203.539 176.496 199.249 1.00 10.20 ? 3702 THR A CG2   1 
ATOM   15754 N N     . VAL A 1 3703 ? 203.045 173.386 200.078 1.00 15.04 ? 3703 VAL A N     1 
ATOM   15755 C CA    . VAL A 1 3703 ? 202.020 172.417 200.427 1.00 10.66 ? 3703 VAL A CA    1 
ATOM   15756 C C     . VAL A 1 3703 ? 200.642 173.069 200.325 1.00 8.07  ? 3703 VAL A C     1 
ATOM   15757 O O     . VAL A 1 3703 ? 200.470 174.266 200.565 1.00 4.24  ? 3703 VAL A O     1 
ATOM   15758 C CB    . VAL A 1 3703 ? 202.290 171.855 201.834 1.00 7.18  ? 3703 VAL A CB    1 
ATOM   15759 C CG1   . VAL A 1 3703 ? 201.353 170.734 202.147 1.00 9.52  ? 3703 VAL A CG1   1 
ATOM   15760 C CG2   . VAL A 1 3703 ? 203.735 171.395 201.950 1.00 12.72 ? 3703 VAL A CG2   1 
ATOM   15761 N N     . THR A 1 3704 ? 199.647 172.267 199.954 1.00 10.45 ? 3704 THR A N     1 
ATOM   15762 C CA    . THR A 1 3704 ? 198.334 172.780 199.577 1.00 8.66  ? 3704 THR A CA    1 
ATOM   15763 C C     . THR A 1 3704 ? 197.286 171.800 200.104 1.00 10.09 ? 3704 THR A C     1 
ATOM   15764 O O     . THR A 1 3704 ? 197.611 170.679 200.502 1.00 14.27 ? 3704 THR A O     1 
ATOM   15765 C CB    . THR A 1 3704 ? 198.267 172.977 198.054 1.00 12.23 ? 3704 THR A CB    1 
ATOM   15766 O OG1   . THR A 1 3704 ? 199.287 173.899 197.655 1.00 14.43 ? 3704 THR A OG1   1 
ATOM   15767 C CG2   . THR A 1 3704 ? 196.931 173.557 197.611 1.00 12.66 ? 3704 THR A CG2   1 
ATOM   15768 N N     . ARG A 1 3705 ? 196.023 172.239 200.129 1.00 7.43  ? 3705 ARG A N     1 
ATOM   15769 C CA    . ARG A 1 3705 ? 194.938 171.390 200.616 1.00 10.00 ? 3705 ARG A CA    1 
ATOM   15770 C C     . ARG A 1 3705 ? 194.917 170.044 199.901 1.00 11.09 ? 3705 ARG A C     1 
ATOM   15771 O O     . ARG A 1 3705 ? 194.752 168.995 200.534 1.00 10.90 ? 3705 ARG A O     1 
ATOM   15772 C CB    . ARG A 1 3705 ? 193.597 172.103 200.447 1.00 11.56 ? 3705 ARG A CB    1 
ATOM   15773 C CG    . ARG A 1 3705 ? 193.387 173.275 201.383 1.00 8.00  ? 3705 ARG A CG    1 
ATOM   15774 C CD    . ARG A 1 3705 ? 192.027 173.910 201.171 1.00 9.38  ? 3705 ARG A CD    1 
ATOM   15775 N NE    . ARG A 1 3705 ? 191.670 174.803 202.265 1.00 10.14 ? 3705 ARG A NE    1 
ATOM   15776 C CZ    . ARG A 1 3705 ? 190.831 174.487 203.242 1.00 12.49 ? 3705 ARG A CZ    1 
ATOM   15777 N NH1   . ARG A 1 3705 ? 190.225 173.312 203.280 1.00 13.06 ? 3705 ARG A NH1   1 
ATOM   15778 N NH2   . ARG A 1 3705 ? 190.594 175.373 204.205 1.00 8.68  ? 3705 ARG A NH2   1 
ATOM   15779 N N     . SER A 1 3706 ? 195.078 170.056 198.577 1.00 9.14  ? 3706 SER A N     1 
ATOM   15780 C CA    . SER A 1 3706 ? 195.148 168.803 197.831 1.00 12.19 ? 3706 SER A CA    1 
ATOM   15781 C C     . SER A 1 3706 ? 196.378 167.996 198.227 1.00 11.38 ? 3706 SER A C     1 
ATOM   15782 O O     . SER A 1 3706 ? 196.326 166.762 198.293 1.00 10.66 ? 3706 SER A O     1 
ATOM   15783 C CB    . SER A 1 3706 ? 195.148 169.087 196.332 1.00 13.52 ? 3706 SER A CB    1 
ATOM   15784 O OG    . SER A 1 3706 ? 196.196 169.976 195.988 1.00 14.77 ? 3706 SER A OG    1 
ATOM   15785 N N     . SER A 1 3707 ? 197.496 168.677 198.487 1.00 8.82  ? 3707 SER A N     1 
ATOM   15786 C CA    . SER A 1 3707 ? 198.693 167.985 198.951 1.00 10.79 ? 3707 SER A CA    1 
ATOM   15787 C C     . SER A 1 3707 ? 198.459 167.319 200.302 1.00 12.30 ? 3707 SER A C     1 
ATOM   15788 O O     . SER A 1 3707 ? 198.876 166.174 200.512 1.00 13.07 ? 3707 SER A O     1 
ATOM   15789 C CB    . SER A 1 3707 ? 199.868 168.959 199.023 1.00 15.12 ? 3707 SER A CB    1 
ATOM   15790 O OG    . SER A 1 3707 ? 201.056 168.294 199.410 1.00 21.24 ? 3707 SER A OG    1 
ATOM   15791 N N     . LEU A 1 3708 ? 197.799 168.019 201.234 1.00 9.68  ? 3708 LEU A N     1 
ATOM   15792 C CA    . LEU A 1 3708 ? 197.443 167.387 202.503 1.00 6.24  ? 3708 LEU A CA    1 
ATOM   15793 C C     . LEU A 1 3708 ? 196.526 166.196 202.290 1.00 11.98 ? 3708 LEU A C     1 
ATOM   15794 O O     . LEU A 1 3708 ? 196.685 165.164 202.946 1.00 21.63 ? 3708 LEU A O     1 
ATOM   15795 C CB    . LEU A 1 3708 ? 196.767 168.372 203.458 1.00 9.54  ? 3708 LEU A CB    1 
ATOM   15796 C CG    . LEU A 1 3708 ? 197.555 169.331 204.349 1.00 11.52 ? 3708 LEU A CG    1 
ATOM   15797 C CD1   . LEU A 1 3708 ? 198.397 168.553 205.351 1.00 10.52 ? 3708 LEU A CD1   1 
ATOM   15798 C CD2   . LEU A 1 3708 ? 198.385 170.284 203.560 1.00 15.98 ? 3708 LEU A CD2   1 
ATOM   15799 N N     . GLN A 1 3709 ? 195.538 166.330 201.404 1.00 5.74  ? 3709 GLN A N     1 
ATOM   15800 C CA    . GLN A 1 3709 ? 194.618 165.224 201.169 1.00 2.27  ? 3709 GLN A CA    1 
ATOM   15801 C C     . GLN A 1 3709 ? 195.366 164.001 200.662 1.00 11.33 ? 3709 GLN A C     1 
ATOM   15802 O O     . GLN A 1 3709 ? 195.149 162.884 201.141 1.00 15.29 ? 3709 GLN A O     1 
ATOM   15803 C CB    . GLN A 1 3709 ? 193.534 165.640 200.177 1.00 8.48  ? 3709 GLN A CB    1 
ATOM   15804 C CG    . GLN A 1 3709 ? 192.479 166.552 200.760 1.00 11.47 ? 3709 GLN A CG    1 
ATOM   15805 C CD    . GLN A 1 3709 ? 191.378 166.857 199.772 1.00 14.18 ? 3709 GLN A CD    1 
ATOM   15806 O OE1   . GLN A 1 3709 ? 191.051 166.034 198.918 1.00 16.55 ? 3709 GLN A OE1   1 
ATOM   15807 N NE2   . GLN A 1 3709 ? 190.802 168.049 199.876 1.00 13.84 ? 3709 GLN A NE2   1 
ATOM   15808 N N     . SER A 1 3710 ? 196.277 164.202 199.707 1.00 15.30 ? 3710 SER A N     1 
ATOM   15809 C CA    . SER A 1 3710 ? 197.047 163.083 199.173 1.00 11.91 ? 3710 SER A CA    1 
ATOM   15810 C C     . SER A 1 3710 ? 197.953 162.471 200.234 1.00 12.79 ? 3710 SER A C     1 
ATOM   15811 O O     . SER A 1 3710 ? 198.005 161.244 200.379 1.00 15.91 ? 3710 SER A O     1 
ATOM   15812 C CB    . SER A 1 3710 ? 197.866 163.539 197.968 1.00 8.62  ? 3710 SER A CB    1 
ATOM   15813 O OG    . SER A 1 3710 ? 199.092 164.113 198.379 1.00 17.70 ? 3710 SER A OG    1 
ATOM   15814 N N     . GLN A 1 3711 ? 198.675 163.309 200.986 1.00 8.48  ? 3711 GLN A N     1 
ATOM   15815 C CA    . GLN A 1 3711 ? 199.569 162.794 202.021 1.00 5.94  ? 3711 GLN A CA    1 
ATOM   15816 C C     . GLN A 1 3711 ? 198.801 162.007 203.071 1.00 12.79 ? 3711 GLN A C     1 
ATOM   15817 O O     . GLN A 1 3711 ? 199.215 160.912 203.466 1.00 24.04 ? 3711 GLN A O     1 
ATOM   15818 C CB    . GLN A 1 3711 ? 200.325 163.942 202.687 1.00 9.08  ? 3711 GLN A CB    1 
ATOM   15819 C CG    . GLN A 1 3711 ? 201.343 164.634 201.813 1.00 15.60 ? 3711 GLN A CG    1 
ATOM   15820 C CD    . GLN A 1 3711 ? 202.384 165.375 202.628 1.00 17.60 ? 3711 GLN A CD    1 
ATOM   15821 O OE1   . GLN A 1 3711 ? 202.623 165.050 203.791 1.00 9.92  ? 3711 GLN A OE1   1 
ATOM   15822 N NE2   . GLN A 1 3711 ? 203.008 166.378 202.023 1.00 15.51 ? 3711 GLN A NE2   1 
ATOM   15823 N N     . CYS A 1 3712 ? 197.675 162.550 203.533 1.00 9.90  ? 3712 CYS A N     1 
ATOM   15824 C CA    . CYS A 1 3712 ? 196.899 161.890 204.572 1.00 12.76 ? 3712 CYS A CA    1 
ATOM   15825 C C     . CYS A 1 3712 ? 196.259 160.610 204.054 1.00 12.85 ? 3712 CYS A C     1 
ATOM   15826 O O     . CYS A 1 3712 ? 196.192 159.613 204.780 1.00 18.65 ? 3712 CYS A O     1 
ATOM   15827 C CB    . CYS A 1 3712 ? 195.842 162.850 205.114 1.00 10.91 ? 3712 CYS A CB    1 
ATOM   15828 S SG    . CYS A 1 3712 ? 196.537 164.283 205.970 1.00 14.58 ? 3712 CYS A SG    1 
ATOM   15829 N N     . LEU A 1 3713 ? 195.781 160.614 202.807 1.00 6.18  ? 3713 LEU A N     1 
ATOM   15830 C CA    . LEU A 1 3713 ? 195.224 159.397 202.231 1.00 4.82  ? 3713 LEU A CA    1 
ATOM   15831 C C     . LEU A 1 3713 ? 196.285 158.312 202.123 1.00 10.14 ? 3713 LEU A C     1 
ATOM   15832 O O     . LEU A 1 3713 ? 196.038 157.155 202.480 1.00 18.68 ? 3713 LEU A O     1 
ATOM   15833 C CB    . LEU A 1 3713 ? 194.616 159.702 200.863 1.00 8.69  ? 3713 LEU A CB    1 
ATOM   15834 C CG    . LEU A 1 3713 ? 193.834 158.589 200.168 1.00 11.54 ? 3713 LEU A CG    1 
ATOM   15835 C CD1   . LEU A 1 3713 ? 192.842 157.969 201.124 1.00 13.76 ? 3713 LEU A CD1   1 
ATOM   15836 C CD2   . LEU A 1 3713 ? 193.119 159.136 198.948 1.00 12.86 ? 3713 LEU A CD2   1 
ATOM   15837 N N     . ASN A 1 3714 ? 197.484 158.674 201.661 1.00 14.71 ? 3714 ASN A N     1 
ATOM   15838 C CA    . ASN A 1 3714 ? 198.567 157.701 201.589 1.00 14.46 ? 3714 ASN A CA    1 
ATOM   15839 C C     . ASN A 1 3714 ? 198.922 157.174 202.972 1.00 13.42 ? 3714 ASN A C     1 
ATOM   15840 O O     . ASN A 1 3714 ? 199.139 155.971 203.148 1.00 18.29 ? 3714 ASN A O     1 
ATOM   15841 C CB    . ASN A 1 3714 ? 199.792 158.326 200.924 1.00 12.71 ? 3714 ASN A CB    1 
ATOM   15842 C CG    . ASN A 1 3714 ? 199.577 158.607 199.455 1.00 15.54 ? 3714 ASN A CG    1 
ATOM   15843 O OD1   . ASN A 1 3714 ? 198.557 158.226 198.882 1.00 15.03 ? 3714 ASN A OD1   1 
ATOM   15844 N ND2   . ASN A 1 3714 ? 200.539 159.277 198.834 1.00 16.30 ? 3714 ASN A ND2   1 
ATOM   15845 N N     . GLU A 1 3715 ? 198.981 158.061 203.967 1.00 8.16  ? 3715 GLU A N     1 
ATOM   15846 C CA    . GLU A 1 3715 ? 199.374 157.640 205.308 1.00 10.03 ? 3715 GLU A CA    1 
ATOM   15847 C C     . GLU A 1 3715 ? 198.331 156.722 205.934 1.00 15.55 ? 3715 GLU A C     1 
ATOM   15848 O O     . GLU A 1 3715 ? 198.681 155.716 206.561 1.00 20.88 ? 3715 GLU A O     1 
ATOM   15849 C CB    . GLU A 1 3715 ? 199.616 158.865 206.188 1.00 8.21  ? 3715 GLU A CB    1 
ATOM   15850 C CG    . GLU A 1 3715 ? 200.390 158.572 207.460 1.00 16.39 ? 3715 GLU A CG    1 
ATOM   15851 C CD    . GLU A 1 3715 ? 201.788 158.059 207.185 1.00 17.84 ? 3715 GLU A CD    1 
ATOM   15852 O OE1   . GLU A 1 3715 ? 202.397 158.496 206.186 1.00 19.18 ? 3715 GLU A OE1   1 
ATOM   15853 O OE2   . GLU A 1 3715 ? 202.281 157.220 207.969 1.00 17.92 ? 3715 GLU A OE2   1 
ATOM   15854 N N     . VAL A 1 3716 ? 197.045 157.046 205.776 1.00 11.32 ? 3716 VAL A N     1 
ATOM   15855 C CA    . VAL A 1 3716 ? 196.005 156.201 206.354 1.00 7.18  ? 3716 VAL A CA    1 
ATOM   15856 C C     . VAL A 1 3716 ? 195.904 154.881 205.602 1.00 13.55 ? 3716 VAL A C     1 
ATOM   15857 O O     . VAL A 1 3716 ? 195.579 153.847 206.197 1.00 20.25 ? 3716 VAL A O     1 
ATOM   15858 C CB    . VAL A 1 3716 ? 194.653 156.944 206.400 1.00 10.02 ? 3716 VAL A CB    1 
ATOM   15859 C CG1   . VAL A 1 3716 ? 194.111 157.202 205.006 1.00 13.02 ? 3716 VAL A CG1   1 
ATOM   15860 C CG2   . VAL A 1 3716 ? 193.643 156.165 207.234 1.00 13.26 ? 3716 VAL A CG2   1 
ATOM   15861 N N     . LEU A 1 3717 ? 196.185 154.878 204.295 1.00 13.83 ? 3717 LEU A N     1 
ATOM   15862 C CA    . LEU A 1 3717 ? 196.184 153.624 203.551 1.00 12.94 ? 3717 LEU A CA    1 
ATOM   15863 C C     . LEU A 1 3717 ? 197.370 152.747 203.930 1.00 13.44 ? 3717 LEU A C     1 
ATOM   15864 O O     . LEU A 1 3717 ? 197.247 151.518 203.955 1.00 23.25 ? 3717 LEU A O     1 
ATOM   15865 C CB    . LEU A 1 3717 ? 196.180 153.909 202.050 1.00 14.94 ? 3717 LEU A CB    1 
ATOM   15866 C CG    . LEU A 1 3717 ? 194.824 154.310 201.467 1.00 14.65 ? 3717 LEU A CG    1 
ATOM   15867 C CD1   . LEU A 1 3717 ? 194.991 154.968 200.109 1.00 14.90 ? 3717 LEU A CD1   1 
ATOM   15868 C CD2   . LEU A 1 3717 ? 193.916 153.103 201.365 1.00 13.33 ? 3717 LEU A CD2   1 
ATOM   15869 N N     . LYS A 1 3718 ? 198.524 153.352 204.212 1.00 11.33 ? 3718 LYS A N     1 
ATOM   15870 C CA    . LYS A 1 3718 ? 199.651 152.580 204.723 1.00 11.89 ? 3718 LYS A CA    1 
ATOM   15871 C C     . LYS A 1 3718 ? 199.358 152.035 206.115 1.00 13.15 ? 3718 LYS A C     1 
ATOM   15872 O O     . LYS A 1 3718 ? 199.696 150.887 206.423 1.00 17.70 ? 3718 LYS A O     1 
ATOM   15873 C CB    . LYS A 1 3718 ? 200.913 153.440 204.741 1.00 14.68 ? 3718 LYS A CB    1 
ATOM   15874 C CG    . LYS A 1 3718 ? 202.153 152.701 205.207 1.00 19.37 ? 3718 LYS A CG    1 
ATOM   15875 C CD    . LYS A 1 3718 ? 203.390 153.572 205.097 1.00 21.95 ? 3718 LYS A CD    1 
ATOM   15876 C CE    . LYS A 1 3718 ? 204.602 152.884 205.705 1.00 19.41 ? 3718 LYS A CE    1 
ATOM   15877 N NZ    . LYS A 1 3718 ? 204.991 151.668 204.942 1.00 15.98 ? 3718 LYS A NZ    1 
ATOM   15878 N N     . ALA A 1 3719 ? 198.728 152.843 206.968 1.00 10.56 ? 3719 ALA A N     1 
ATOM   15879 C CA    . ALA A 1 3719 ? 198.420 152.410 208.326 1.00 13.66 ? 3719 ALA A CA    1 
ATOM   15880 C C     . ALA A 1 3719 ? 197.222 151.467 208.346 1.00 14.65 ? 3719 ALA A C     1 
ATOM   15881 O O     . ALA A 1 3719 ? 197.331 150.315 208.779 1.00 15.74 ? 3719 ALA A O     1 
ATOM   15882 C CB    . ALA A 1 3719 ? 198.164 153.627 209.217 1.00 13.10 ? 3719 ALA A CB    1 
ATOM   15883 N N     . GLU A 1 3720 ? 196.071 151.940 207.878 1.00 16.53 ? 3720 GLU A N     1 
ATOM   15884 C CA    . GLU A 1 3720 ? 194.869 151.123 207.810 1.00 15.14 ? 3720 GLU A CA    1 
ATOM   15885 C C     . GLU A 1 3720 ? 194.818 150.412 206.465 1.00 17.73 ? 3720 GLU A C     1 
ATOM   15886 O O     . GLU A 1 3720 ? 194.992 151.042 205.418 1.00 22.36 ? 3720 GLU A O     1 
ATOM   15887 C CB    . GLU A 1 3720 ? 193.619 151.981 208.005 1.00 14.77 ? 3720 GLU A CB    1 
ATOM   15888 C CG    . GLU A 1 3720 ? 193.544 152.658 209.358 1.00 15.46 ? 3720 GLU A CG    1 
ATOM   15889 C CD    . GLU A 1 3720 ? 193.350 151.673 210.492 1.00 22.58 ? 3720 GLU A CD    1 
ATOM   15890 O OE1   . GLU A 1 3720 ? 192.654 150.658 210.285 1.00 26.01 ? 3720 GLU A OE1   1 
ATOM   15891 O OE2   . GLU A 1 3720 ? 193.902 151.907 211.587 1.00 20.11 ? 3720 GLU A OE2   1 
ATOM   15892 N N     . ARG A 1 3721 ? 194.574 149.103 206.502 1.00 17.32 ? 3721 ARG A N     1 
ATOM   15893 C CA    . ARG A 1 3721 ? 194.561 148.260 205.312 1.00 24.08 ? 3721 ARG A CA    1 
ATOM   15894 C C     . ARG A 1 3721 ? 195.893 148.340 204.574 1.00 22.37 ? 3721 ARG A C     1 
ATOM   15895 O O     . ARG A 1 3721 ? 195.967 148.950 203.502 1.00 21.38 ? 3721 ARG A O     1 
ATOM   15896 C CB    . ARG A 1 3721 ? 193.417 148.654 204.373 1.00 25.04 ? 3721 ARG A CB    1 
ATOM   15897 C CG    . ARG A 1 3721 ? 192.083 148.859 205.068 1.00 23.15 ? 3721 ARG A CG    1 
ATOM   15898 C CD    . ARG A 1 3721 ? 190.938 148.978 204.069 1.00 22.44 ? 3721 ARG A CD    1 
ATOM   15899 N NE    . ARG A 1 3721 ? 191.031 148.036 202.958 1.00 22.28 ? 3721 ARG A NE    1 
ATOM   15900 C CZ    . ARG A 1 3721 ? 191.008 146.714 203.072 1.00 22.96 ? 3721 ARG A CZ    1 
ATOM   15901 N NH1   . ARG A 1 3721 ? 190.858 146.120 204.244 1.00 24.86 ? 3721 ARG A NH1   1 
ATOM   15902 N NH2   . ARG A 1 3721 ? 191.128 145.968 201.978 1.00 25.51 ? 3721 ARG A NH2   1 
ATOM   15903 N N     . PRO A 1 3722 ? 196.969 147.764 205.118 1.00 22.41 ? 3722 PRO A N     1 
ATOM   15904 C CA    . PRO A 1 3722 ? 198.229 147.717 204.358 1.00 23.23 ? 3722 PRO A CA    1 
ATOM   15905 C C     . PRO A 1 3722 ? 198.131 146.906 203.077 1.00 25.04 ? 3722 PRO A C     1 
ATOM   15906 O O     . PRO A 1 3722 ? 198.987 147.064 202.199 1.00 25.38 ? 3722 PRO A O     1 
ATOM   15907 C CB    . PRO A 1 3722 ? 199.209 147.071 205.345 1.00 25.73 ? 3722 PRO A CB    1 
ATOM   15908 C CG    . PRO A 1 3722 ? 198.630 147.350 206.690 1.00 24.40 ? 3722 PRO A CG    1 
ATOM   15909 C CD    . PRO A 1 3722 ? 197.145 147.285 206.499 1.00 24.27 ? 3722 PRO A CD    1 
ATOM   15910 N N     . ASP A 1 3723 ? 197.130 146.029 202.953 1.00 27.42 ? 3723 ASP A N     1 
ATOM   15911 C CA    . ASP A 1 3723 ? 197.023 145.171 201.776 1.00 27.04 ? 3723 ASP A CA    1 
ATOM   15912 C C     . ASP A 1 3723 ? 196.732 145.977 200.515 1.00 26.38 ? 3723 ASP A C     1 
ATOM   15913 O O     . ASP A 1 3723 ? 197.328 145.730 199.458 1.00 28.45 ? 3723 ASP A O     1 
ATOM   15914 C CB    . ASP A 1 3723 ? 195.938 144.119 201.999 1.00 27.20 ? 3723 ASP A CB    1 
ATOM   15915 C CG    . ASP A 1 3723 ? 194.621 144.725 202.444 1.00 28.84 ? 3723 ASP A CG    1 
ATOM   15916 O OD1   . ASP A 1 3723 ? 194.558 145.269 203.567 1.00 25.94 ? 3723 ASP A OD1   1 
ATOM   15917 O OD2   . ASP A 1 3723 ? 193.645 144.647 201.670 1.00 30.21 ? 3723 ASP A OD2   1 
ATOM   15918 N N     . VAL A 1 3724 ? 195.808 146.935 200.596 1.00 24.17 ? 3724 VAL A N     1 
ATOM   15919 C CA    . VAL A 1 3724 ? 195.523 147.761 199.427 1.00 25.36 ? 3724 VAL A CA    1 
ATOM   15920 C C     . VAL A 1 3724 ? 196.729 148.623 199.078 1.00 30.00 ? 3724 VAL A C     1 
ATOM   15921 O O     . VAL A 1 3724 ? 197.007 148.866 197.901 1.00 32.81 ? 3724 VAL A O     1 
ATOM   15922 C CB    . VAL A 1 3724 ? 194.247 148.596 199.639 1.00 24.75 ? 3724 VAL A CB    1 
ATOM   15923 C CG1   . VAL A 1 3724 ? 193.052 147.678 199.827 1.00 24.94 ? 3724 VAL A CG1   1 
ATOM   15924 C CG2   . VAL A 1 3724 ? 194.394 149.515 200.831 1.00 27.64 ? 3724 VAL A CG2   1 
ATOM   15925 N N     . ASP A 1 3725 ? 197.473 149.087 200.085 1.00 29.66 ? 3725 ASP A N     1 
ATOM   15926 C CA    . ASP A 1 3725 ? 198.692 149.841 199.801 1.00 28.28 ? 3725 ASP A CA    1 
ATOM   15927 C C     . ASP A 1 3725 ? 199.732 148.981 199.091 1.00 31.91 ? 3725 ASP A C     1 
ATOM   15928 O O     . ASP A 1 3725 ? 200.370 149.432 198.132 1.00 31.81 ? 3725 ASP A O     1 
ATOM   15929 C CB    . ASP A 1 3725 ? 199.271 150.426 201.087 1.00 28.02 ? 3725 ASP A CB    1 
ATOM   15930 C CG    . ASP A 1 3725 ? 200.166 151.624 200.828 1.00 32.90 ? 3725 ASP A CG    1 
ATOM   15931 O OD1   . ASP A 1 3725 ? 199.634 152.725 200.580 1.00 37.62 ? 3725 ASP A OD1   1 
ATOM   15932 O OD2   . ASP A 1 3725 ? 201.405 151.463 200.874 1.00 33.19 ? 3725 ASP A OD2   1 
ATOM   15933 N N     . GLU A 1 3726 ? 199.920 147.736 199.539 1.00 32.21 ? 3726 GLU A N     1 
ATOM   15934 C CA    . GLU A 1 3726 ? 200.931 146.897 198.905 1.00 29.48 ? 3726 GLU A CA    1 
ATOM   15935 C C     . GLU A 1 3726 ? 200.511 146.506 197.493 1.00 31.89 ? 3726 GLU A C     1 
ATOM   15936 O O     . GLU A 1 3726 ? 201.351 146.422 196.590 1.00 35.20 ? 3726 GLU A O     1 
ATOM   15937 C CB    . GLU A 1 3726 ? 201.235 145.665 199.766 1.00 29.04 ? 3726 GLU A CB    1 
ATOM   15938 C CG    . GLU A 1 3726 ? 200.083 144.707 200.015 1.00 31.92 ? 3726 GLU A CG    1 
ATOM   15939 C CD    . GLU A 1 3726 ? 199.924 143.669 198.923 1.00 35.52 ? 3726 GLU A CD    1 
ATOM   15940 O OE1   . GLU A 1 3726 ? 200.899 143.441 198.177 1.00 35.10 ? 3726 GLU A OE1   1 
ATOM   15941 O OE2   . GLU A 1 3726 ? 198.826 143.083 198.810 1.00 35.33 ? 3726 GLU A OE2   1 
ATOM   15942 N N     . LYS A 1 3727 ? 199.210 146.303 197.264 1.00 30.42 ? 3727 LYS A N     1 
ATOM   15943 C CA    . LYS A 1 3727 ? 198.790 145.991 195.901 1.00 30.57 ? 3727 LYS A CA    1 
ATOM   15944 C C     . LYS A 1 3727 ? 198.800 147.227 195.007 1.00 28.83 ? 3727 LYS A C     1 
ATOM   15945 O O     . LYS A 1 3727 ? 199.015 147.105 193.800 1.00 31.37 ? 3727 LYS A O     1 
ATOM   15946 C CB    . LYS A 1 3727 ? 197.419 145.316 195.886 1.00 31.17 ? 3727 LYS A CB    1 
ATOM   15947 C CG    . LYS A 1 3727 ? 196.259 146.146 196.369 1.00 29.43 ? 3727 LYS A CG    1 
ATOM   15948 C CD    . LYS A 1 3727 ? 194.973 145.344 196.255 1.00 30.11 ? 3727 LYS A CD    1 
ATOM   15949 C CE    . LYS A 1 3727 ? 194.899 144.245 197.303 1.00 31.76 ? 3727 LYS A CE    1 
ATOM   15950 N NZ    . LYS A 1 3727 ? 193.587 143.542 197.273 1.00 31.93 ? 3727 LYS A NZ    1 
ATOM   15951 N N     . ARG A 1 3728 ? 198.598 148.421 195.569 1.00 26.54 ? 3728 ARG A N     1 
ATOM   15952 C CA    . ARG A 1 3728 ? 198.835 149.639 194.800 1.00 28.38 ? 3728 ARG A CA    1 
ATOM   15953 C C     . ARG A 1 3728 ? 200.298 149.755 194.403 1.00 30.88 ? 3728 ARG A C     1 
ATOM   15954 O O     . ARG A 1 3728 ? 200.615 150.118 193.263 1.00 30.31 ? 3728 ARG A O     1 
ATOM   15955 C CB    . ARG A 1 3728 ? 198.420 150.864 195.607 1.00 29.15 ? 3728 ARG A CB    1 
ATOM   15956 C CG    . ARG A 1 3728 ? 196.938 151.096 195.684 1.00 29.64 ? 3728 ARG A CG    1 
ATOM   15957 C CD    . ARG A 1 3728 ? 196.581 152.463 196.267 1.00 28.92 ? 3728 ARG A CD    1 
ATOM   15958 N NE    . ARG A 1 3728 ? 197.276 153.584 195.640 1.00 31.20 ? 3728 ARG A NE    1 
ATOM   15959 C CZ    . ARG A 1 3728 ? 198.447 154.071 196.033 1.00 32.96 ? 3728 ARG A CZ    1 
ATOM   15960 N NH1   . ARG A 1 3728 ? 199.075 153.594 197.095 1.00 34.55 ? 3728 ARG A NH1   1 
ATOM   15961 N NH2   . ARG A 1 3728 ? 198.995 155.071 195.349 1.00 31.37 ? 3728 ARG A NH2   1 
ATOM   15962 N N     . SER A 1 3729 ? 201.202 149.452 195.336 1.00 34.31 ? 3729 SER A N     1 
ATOM   15963 C CA    . SER A 1 3729 ? 202.621 149.429 195.003 1.00 33.11 ? 3729 SER A CA    1 
ATOM   15964 C C     . SER A 1 3729 ? 202.897 148.427 193.895 1.00 35.60 ? 3729 SER A C     1 
ATOM   15965 O O     . SER A 1 3729 ? 203.687 148.701 192.988 1.00 34.62 ? 3729 SER A O     1 
ATOM   15966 C CB    . SER A 1 3729 ? 203.461 149.096 196.236 1.00 31.35 ? 3729 SER A CB    1 
ATOM   15967 O OG    . SER A 1 3729 ? 203.347 150.096 197.233 1.00 34.27 ? 3729 SER A OG    1 
ATOM   15968 N N     . ASP A 1 3730 ? 202.264 147.256 193.960 1.00 31.08 ? 3730 ASP A N     1 
ATOM   15969 C CA    . ASP A 1 3730 ? 202.433 146.260 192.907 1.00 28.52 ? 3730 ASP A CA    1 
ATOM   15970 C C     . ASP A 1 3730 ? 201.894 146.766 191.571 1.00 32.69 ? 3730 ASP A C     1 
ATOM   15971 O O     . ASP A 1 3730 ? 202.490 146.509 190.518 1.00 36.54 ? 3730 ASP A O     1 
ATOM   15972 C CB    . ASP A 1 3730 ? 201.740 144.959 193.318 1.00 29.02 ? 3730 ASP A CB    1 
ATOM   15973 C CG    . ASP A 1 3730 ? 202.547 144.158 194.322 1.00 34.00 ? 3730 ASP A CG    1 
ATOM   15974 O OD1   . ASP A 1 3730 ? 203.391 144.755 195.026 1.00 35.64 ? 3730 ASP A OD1   1 
ATOM   15975 O OD2   . ASP A 1 3730 ? 202.326 142.934 194.422 1.00 35.72 ? 3730 ASP A OD2   1 
ATOM   15976 N N     . LEU A 1 3731 ? 200.765 147.481 191.601 1.00 29.17 ? 3731 LEU A N     1 
ATOM   15977 C CA    . LEU A 1 3731 ? 200.213 148.083 190.392 1.00 27.42 ? 3731 LEU A CA    1 
ATOM   15978 C C     . LEU A 1 3731 ? 201.215 149.032 189.766 1.00 30.33 ? 3731 LEU A C     1 
ATOM   15979 O O     . LEU A 1 3731 ? 201.388 149.064 188.542 1.00 34.71 ? 3731 LEU A O     1 
ATOM   15980 C CB    . LEU A 1 3731 ? 198.933 148.849 190.717 1.00 27.17 ? 3731 LEU A CB    1 
ATOM   15981 C CG    . LEU A 1 3731 ? 197.630 148.074 190.811 1.00 28.29 ? 3731 LEU A CG    1 
ATOM   15982 C CD1   . LEU A 1 3731 ? 196.556 149.121 190.800 1.00 26.43 ? 3731 LEU A CD1   1 
ATOM   15983 C CD2   . LEU A 1 3731 ? 197.467 147.080 189.658 1.00 31.09 ? 3731 LEU A CD2   1 
ATOM   15984 N N     . LEU A 1 3732 ? 201.851 149.858 190.597 1.00 27.76 ? 3732 LEU A N     1 
ATOM   15985 C CA    . LEU A 1 3732 ? 202.917 150.713 190.088 1.00 27.00 ? 3732 LEU A CA    1 
ATOM   15986 C C     . LEU A 1 3732 ? 204.055 149.869 189.526 1.00 29.21 ? 3732 LEU A C     1 
ATOM   15987 O O     . LEU A 1 3732 ? 204.475 150.070 188.382 1.00 29.85 ? 3732 LEU A O     1 
ATOM   15988 C CB    . LEU A 1 3732 ? 203.424 151.653 191.181 1.00 30.87 ? 3732 LEU A CB    1 
ATOM   15989 C CG    . LEU A 1 3732 ? 202.689 152.981 191.428 1.00 28.32 ? 3732 LEU A CG    1 
ATOM   15990 C CD1   . LEU A 1 3732 ? 202.763 153.893 190.223 1.00 27.71 ? 3732 LEU A CD1   1 
ATOM   15991 C CD2   . LEU A 1 3732 ? 201.249 152.786 191.830 1.00 30.78 ? 3732 LEU A CD2   1 
ATOM   15992 N N     . LYS A 1 3733 ? 204.514 148.867 190.283 1.00 27.37 ? 3733 LYS A N     1 
ATOM   15993 C CA    . LYS A 1 3733 ? 205.612 148.037 189.805 1.00 34.25 ? 3733 LYS A CA    1 
ATOM   15994 C C     . LYS A 1 3733 ? 205.290 147.335 188.492 1.00 34.66 ? 3733 LYS A C     1 
ATOM   15995 O O     . LYS A 1 3733 ? 206.217 146.943 187.777 1.00 34.51 ? 3733 LYS A O     1 
ATOM   15996 C CB    . LYS A 1 3733 ? 206.028 147.011 190.863 1.00 35.57 ? 3733 LYS A CB    1 
ATOM   15997 C CG    . LYS A 1 3733 ? 206.403 147.638 192.176 1.00 31.38 ? 3733 LYS A CG    1 
ATOM   15998 C CD    . LYS A 1 3733 ? 206.905 146.591 193.179 1.00 34.72 ? 3733 LYS A CD    1 
ATOM   15999 C CE    . LYS A 1 3733 ? 206.389 146.819 194.580 1.00 35.74 ? 3733 LYS A CE    1 
ATOM   16000 N NZ    . LYS A 1 3733 ? 205.013 146.240 194.788 1.00 34.65 ? 3733 LYS A NZ    1 
ATOM   16001 N N     . LEU A 1 3734 ? 204.005 147.213 188.143 1.00 30.21 ? 3734 LEU A N     1 
ATOM   16002 C CA    . LEU A 1 3734 ? 203.625 146.652 186.858 1.00 28.35 ? 3734 LEU A CA    1 
ATOM   16003 C C     . LEU A 1 3734 ? 204.091 147.491 185.690 1.00 30.32 ? 3734 LEU A C     1 
ATOM   16004 O O     . LEU A 1 3734 ? 204.035 147.010 184.555 1.00 30.55 ? 3734 LEU A O     1 
ATOM   16005 C CB    . LEU A 1 3734 ? 202.110 146.486 186.737 1.00 27.00 ? 3734 LEU A CB    1 
ATOM   16006 C CG    . LEU A 1 3734 ? 201.376 145.504 187.641 1.00 29.71 ? 3734 LEU A CG    1 
ATOM   16007 C CD1   . LEU A 1 3734 ? 199.887 145.487 187.256 1.00 29.31 ? 3734 LEU A CD1   1 
ATOM   16008 C CD2   . LEU A 1 3734 ? 202.046 144.131 187.513 1.00 30.37 ? 3734 LEU A CD2   1 
ATOM   16009 N N     . GLN A 1 3735 ? 204.518 148.730 185.922 1.00 31.74 ? 3735 GLN A N     1 
ATOM   16010 C CA    . GLN A 1 3735 ? 204.993 149.594 184.846 1.00 32.74 ? 3735 GLN A CA    1 
ATOM   16011 C C     . GLN A 1 3735 ? 206.517 149.547 184.811 1.00 29.89 ? 3735 GLN A C     1 
ATOM   16012 O O     . GLN A 1 3735 ? 207.216 150.339 185.444 1.00 28.56 ? 3735 GLN A O     1 
ATOM   16013 C CB    . GLN A 1 3735 ? 204.459 151.000 185.025 1.00 27.80 ? 3735 GLN A CB    1 
ATOM   16014 C CG    . GLN A 1 3735 ? 202.959 151.021 185.051 1.00 26.97 ? 3735 GLN A CG    1 
ATOM   16015 C CD    . GLN A 1 3735 ? 202.384 152.405 184.934 1.00 29.32 ? 3735 GLN A CD    1 
ATOM   16016 O OE1   . GLN A 1 3735 ? 202.997 153.307 184.368 1.00 27.91 ? 3735 GLN A OE1   1 
ATOM   16017 N NE2   . GLN A 1 3735 ? 201.193 152.585 185.482 1.00 28.77 ? 3735 GLN A NE2   1 
ATOM   16018 N N     . GLY A 1 3736 ? 207.030 148.561 184.087 1.00 32.25 ? 3736 GLY A N     1 
ATOM   16019 C CA    . GLY A 1 3736 ? 208.431 148.500 183.716 1.00 35.99 ? 3736 GLY A CA    1 
ATOM   16020 C C     . GLY A 1 3736 ? 209.447 147.886 184.666 1.00 37.70 ? 3736 GLY A C     1 
ATOM   16021 O O     . GLY A 1 3736 ? 210.302 147.117 184.230 1.00 35.80 ? 3736 GLY A O     1 
ATOM   16022 N N     . GLU A 1 3737 ? 209.390 148.224 185.951 1.00 34.90 ? 3737 GLU A N     1 
ATOM   16023 C CA    . GLU A 1 3737 ? 210.402 147.722 186.877 1.00 33.78 ? 3737 GLU A CA    1 
ATOM   16024 C C     . GLU A 1 3737 ? 210.215 146.244 187.209 1.00 34.75 ? 3737 GLU A C     1 
ATOM   16025 O O     . GLU A 1 3737 ? 211.199 145.529 187.431 1.00 35.62 ? 3737 GLU A O     1 
ATOM   16026 C CB    . GLU A 1 3737 ? 210.444 148.596 188.121 1.00 33.67 ? 3737 GLU A CB    1 
ATOM   16027 C CG    . GLU A 1 3737 ? 209.222 148.645 189.033 1.00 34.77 ? 3737 GLU A CG    1 
ATOM   16028 C CD    . GLU A 1 3737 ? 209.489 149.621 190.151 1.00 36.57 ? 3737 GLU A CD    1 
ATOM   16029 O OE1   . GLU A 1 3737 ? 210.581 150.214 190.146 1.00 35.41 ? 3737 GLU A OE1   1 
ATOM   16030 O OE2   . GLU A 1 3737 ? 208.647 149.797 191.040 1.00 35.68 ? 3737 GLU A OE2   1 
ATOM   16031 N N     . PHE A 1 3738 ? 208.972 145.756 187.262 1.00 34.41 ? 3738 PHE A N     1 
ATOM   16032 C CA    . PHE A 1 3738 ? 208.807 144.310 187.122 1.00 32.83 ? 3738 PHE A CA    1 
ATOM   16033 C C     . PHE A 1 3738 ? 209.368 143.818 185.800 1.00 35.01 ? 3738 PHE A C     1 
ATOM   16034 O O     . PHE A 1 3738 ? 210.039 142.785 185.761 1.00 36.64 ? 3738 PHE A O     1 
ATOM   16035 C CB    . PHE A 1 3738 ? 207.351 143.869 187.238 1.00 33.84 ? 3738 PHE A CB    1 
ATOM   16036 C CG    . PHE A 1 3738 ? 206.822 143.796 188.635 1.00 33.75 ? 3738 PHE A CG    1 
ATOM   16037 C CD1   . PHE A 1 3738 ? 207.664 143.710 189.732 1.00 36.99 ? 3738 PHE A CD1   1 
ATOM   16038 C CD2   . PHE A 1 3738 ? 205.457 143.810 188.846 1.00 30.92 ? 3738 PHE A CD2   1 
ATOM   16039 C CE1   . PHE A 1 3738 ? 207.148 143.626 191.012 1.00 36.01 ? 3738 PHE A CE1   1 
ATOM   16040 C CE2   . PHE A 1 3738 ? 204.935 143.738 190.123 1.00 30.81 ? 3738 PHE A CE2   1 
ATOM   16041 C CZ    . PHE A 1 3738 ? 205.784 143.642 191.209 1.00 34.14 ? 3738 PHE A CZ    1 
ATOM   16042 N N     . GLN A 1 3739 ? 209.090 144.524 184.700 1.00 32.99 ? 3739 GLN A N     1 
ATOM   16043 C CA    . GLN A 1 3739 ? 209.709 144.150 183.431 1.00 36.03 ? 3739 GLN A CA    1 
ATOM   16044 C C     . GLN A 1 3739 ? 211.222 144.321 183.500 1.00 36.53 ? 3739 GLN A C     1 
ATOM   16045 O O     . GLN A 1 3739 ? 211.971 143.599 182.833 1.00 38.93 ? 3739 GLN A O     1 
ATOM   16046 C CB    . GLN A 1 3739 ? 209.126 144.976 182.282 1.00 38.17 ? 3739 GLN A CB    1 
ATOM   16047 C CG    . GLN A 1 3739 ? 207.743 144.532 181.806 1.00 37.57 ? 3739 GLN A CG    1 
ATOM   16048 C CD    . GLN A 1 3739 ? 206.636 144.854 182.799 1.00 34.86 ? 3739 GLN A CD    1 
ATOM   16049 O OE1   . GLN A 1 3739 ? 206.407 146.017 183.132 1.00 33.36 ? 3739 GLN A OE1   1 
ATOM   16050 N NE2   . GLN A 1 3739 ? 205.942 143.824 183.272 1.00 32.92 ? 3739 GLN A NE2   1 
ATOM   16051 N N     . LEU A 1 3740 ? 211.694 145.272 184.309 1.00 33.35 ? 3740 LEU A N     1 
ATOM   16052 C CA    . LEU A 1 3740 ? 213.132 145.409 184.504 1.00 36.30 ? 3740 LEU A CA    1 
ATOM   16053 C C     . LEU A 1 3740 ? 213.715 144.171 185.176 1.00 39.43 ? 3740 LEU A C     1 
ATOM   16054 O O     . LEU A 1 3740 ? 214.759 143.659 184.753 1.00 40.18 ? 3740 LEU A O     1 
ATOM   16055 C CB    . LEU A 1 3740 ? 213.437 146.665 185.319 1.00 34.77 ? 3740 LEU A CB    1 
ATOM   16056 C CG    . LEU A 1 3740 ? 214.834 147.257 185.140 1.00 36.96 ? 3740 LEU A CG    1 
ATOM   16057 C CD1   . LEU A 1 3740 ? 214.927 147.970 183.802 1.00 36.79 ? 3740 LEU A CD1   1 
ATOM   16058 C CD2   . LEU A 1 3740 ? 215.151 148.213 186.276 1.00 34.42 ? 3740 LEU A CD2   1 
ATOM   16059 N N     . ARG A 1 3741 ? 213.048 143.662 186.215 1.00 40.67 ? 3741 ARG A N     1 
ATOM   16060 C CA    . ARG A 1 3741 ? 213.526 142.447 186.871 1.00 39.83 ? 3741 ARG A CA    1 
ATOM   16061 C C     . ARG A 1 3741 ? 213.370 141.239 185.948 1.00 38.34 ? 3741 ARG A C     1 
ATOM   16062 O O     . ARG A 1 3741 ? 214.180 140.303 185.991 1.00 36.62 ? 3741 ARG A O     1 
ATOM   16063 C CB    . ARG A 1 3741 ? 212.789 142.262 188.204 1.00 35.85 ? 3741 ARG A CB    1 
ATOM   16064 C CG    . ARG A 1 3741 ? 213.153 141.022 189.018 1.00 38.49 ? 3741 ARG A CG    1 
ATOM   16065 C CD    . ARG A 1 3741 ? 212.234 139.844 188.741 1.00 39.92 ? 3741 ARG A CD    1 
ATOM   16066 N NE    . ARG A 1 3741 ? 212.712 138.610 189.353 1.00 36.61 ? 3741 ARG A NE    1 
ATOM   16067 C CZ    . ARG A 1 3741 ? 212.542 137.406 188.826 1.00 38.10 ? 3741 ARG A CZ    1 
ATOM   16068 N NH1   . ARG A 1 3741 ? 211.896 137.239 187.685 1.00 38.73 ? 3741 ARG A NH1   1 
ATOM   16069 N NH2   . ARG A 1 3741 ? 213.023 136.343 189.466 1.00 36.39 ? 3741 ARG A NH2   1 
ATOM   16070 N N     . LEU A 1 3742 ? 212.343 141.260 185.093 1.00 38.92 ? 3742 LEU A N     1 
ATOM   16071 C CA    . LEU A 1 3742 ? 212.213 140.275 184.023 1.00 41.81 ? 3742 LEU A CA    1 
ATOM   16072 C C     . LEU A 1 3742 ? 213.450 140.258 183.137 1.00 44.27 ? 3742 LEU A C     1 
ATOM   16073 O O     . LEU A 1 3742 ? 214.000 139.191 182.840 1.00 42.06 ? 3742 LEU A O     1 
ATOM   16074 C CB    . LEU A 1 3742 ? 210.969 140.585 183.186 1.00 41.98 ? 3742 LEU A CB    1 
ATOM   16075 C CG    . LEU A 1 3742 ? 210.529 139.610 182.090 1.00 41.64 ? 3742 LEU A CG    1 
ATOM   16076 C CD1   . LEU A 1 3742 ? 210.124 138.285 182.678 1.00 41.63 ? 3742 LEU A CD1   1 
ATOM   16077 C CD2   . LEU A 1 3742 ? 209.394 140.198 181.260 1.00 40.43 ? 3742 LEU A CD2   1 
ATOM   16078 N N     . ARG A 1 3743 ? 213.902 141.436 182.704 1.00 46.14 ? 3743 ARG A N     1 
ATOM   16079 C CA    . ARG A 1 3743 ? 215.081 141.502 181.847 1.00 44.73 ? 3743 ARG A CA    1 
ATOM   16080 C C     . ARG A 1 3743 ? 216.334 141.075 182.600 1.00 44.49 ? 3743 ARG A C     1 
ATOM   16081 O O     . ARG A 1 3743 ? 217.246 140.480 182.012 1.00 45.82 ? 3743 ARG A O     1 
ATOM   16082 C CB    . ARG A 1 3743 ? 215.248 142.911 181.279 1.00 43.55 ? 3743 ARG A CB    1 
ATOM   16083 C CG    . ARG A 1 3743 ? 214.031 143.423 180.531 1.00 42.66 ? 3743 ARG A CG    1 
ATOM   16084 C CD    . ARG A 1 3743 ? 213.493 142.390 179.556 1.00 42.07 ? 3743 ARG A CD    1 
ATOM   16085 N NE    . ARG A 1 3743 ? 212.118 142.684 179.171 1.00 44.21 ? 3743 ARG A NE    1 
ATOM   16086 C CZ    . ARG A 1 3743 ? 211.277 141.795 178.660 1.00 46.92 ? 3743 ARG A CZ    1 
ATOM   16087 N NH1   . ARG A 1 3743 ? 211.639 140.540 178.451 1.00 46.65 ? 3743 ARG A NH1   1 
ATOM   16088 N NH2   . ARG A 1 3743 ? 210.040 142.176 178.353 1.00 45.85 ? 3743 ARG A NH2   1 
ATOM   16089 N N     . GLN A 1 3744 ? 216.407 141.384 183.897 1.00 39.89 ? 3744 GLN A N     1 
ATOM   16090 C CA    . GLN A 1 3744 ? 217.545 140.926 184.692 1.00 42.92 ? 3744 GLN A CA    1 
ATOM   16091 C C     . GLN A 1 3744 ? 217.603 139.403 184.747 1.00 44.21 ? 3744 GLN A C     1 
ATOM   16092 O O     . GLN A 1 3744 ? 218.673 138.804 184.578 1.00 41.38 ? 3744 GLN A O     1 
ATOM   16093 C CB    . GLN A 1 3744 ? 217.482 141.512 186.102 1.00 41.76 ? 3744 GLN A CB    1 
ATOM   16094 C CG    . GLN A 1 3744 ? 217.510 143.027 186.144 1.00 42.26 ? 3744 GLN A CG    1 
ATOM   16095 C CD    . GLN A 1 3744 ? 218.630 143.608 185.307 1.00 45.10 ? 3744 GLN A CD    1 
ATOM   16096 O OE1   . GLN A 1 3744 ? 219.808 143.361 185.566 1.00 43.56 ? 3744 GLN A OE1   1 
ATOM   16097 N NE2   . GLN A 1 3744 ? 218.268 144.384 184.292 1.00 45.71 ? 3744 GLN A NE2   1 
ATOM   16098 N N     . LEU A 1 3745 ? 216.459 138.754 184.972 1.00 43.43 ? 3745 LEU A N     1 
ATOM   16099 C CA    . LEU A 1 3745 ? 216.447 137.295 184.957 1.00 42.86 ? 3745 LEU A CA    1 
ATOM   16100 C C     . LEU A 1 3745 ? 216.742 136.758 183.561 1.00 43.72 ? 3745 LEU A C     1 
ATOM   16101 O O     . LEU A 1 3745 ? 217.364 135.700 183.415 1.00 42.66 ? 3745 LEU A O     1 
ATOM   16102 C CB    . LEU A 1 3745 ? 215.112 136.762 185.474 1.00 42.73 ? 3745 LEU A CB    1 
ATOM   16103 C CG    . LEU A 1 3745 ? 215.195 135.332 186.017 1.00 44.12 ? 3745 LEU A CG    1 
ATOM   16104 C CD1   . LEU A 1 3745 ? 216.299 135.221 187.055 1.00 43.18 ? 3745 LEU A CD1   1 
ATOM   16105 C CD2   . LEU A 1 3745 ? 213.870 134.893 186.609 1.00 41.88 ? 3745 LEU A CD2   1 
ATOM   16106 N N     . GLU A 1 3746 ? 216.313 137.480 182.523 1.00 45.51 ? 3746 GLU A N     1 
ATOM   16107 C CA    . GLU A 1 3746 ? 216.626 137.082 181.153 1.00 46.96 ? 3746 GLU A CA    1 
ATOM   16108 C C     . GLU A 1 3746 ? 218.130 137.071 180.907 1.00 45.29 ? 3746 GLU A C     1 
ATOM   16109 O O     . GLU A 1 3746 ? 218.675 136.112 180.345 1.00 46.72 ? 3746 GLU A O     1 
ATOM   16110 C CB    . GLU A 1 3746 ? 215.931 138.025 180.172 1.00 45.42 ? 3746 GLU A CB    1 
ATOM   16111 C CG    . GLU A 1 3746 ? 216.144 137.675 178.713 1.00 43.19 ? 3746 GLU A CG    1 
ATOM   16112 C CD    . GLU A 1 3746 ? 215.396 138.607 177.778 1.00 48.99 ? 3746 GLU A CD    1 
ATOM   16113 O OE1   . GLU A 1 3746 ? 214.722 139.534 178.276 1.00 48.99 ? 3746 GLU A OE1   1 
ATOM   16114 O OE2   . GLU A 1 3746 ? 215.486 138.419 176.547 1.00 47.66 ? 3746 GLU A OE2   1 
ATOM   16115 N N     . LYS A 1 3747 ? 218.822 138.133 181.322 1.00 39.86 ? 3747 LYS A N     1 
ATOM   16116 C CA    . LYS A 1 3747 ? 220.264 138.179 181.101 1.00 43.12 ? 3747 LYS A CA    1 
ATOM   16117 C C     . LYS A 1 3747 ? 220.995 137.186 181.997 1.00 44.41 ? 3747 LYS A C     1 
ATOM   16118 O O     . LYS A 1 3747 ? 222.034 136.646 181.599 1.00 45.34 ? 3747 LYS A O     1 
ATOM   16119 C CB    . LYS A 1 3747 ? 220.803 139.597 181.302 1.00 42.46 ? 3747 LYS A CB    1 
ATOM   16120 C CG    . LYS A 1 3747 ? 220.668 140.155 182.702 1.00 40.41 ? 3747 LYS A CG    1 
ATOM   16121 C CD    . LYS A 1 3747 ? 220.991 141.639 182.732 1.00 41.95 ? 3747 LYS A CD    1 
ATOM   16122 C CE    . LYS A 1 3747 ? 222.410 141.909 182.253 1.00 42.18 ? 3747 LYS A CE    1 
ATOM   16123 N NZ    . LYS A 1 3747 ? 223.400 141.005 182.901 1.00 43.11 ? 3747 LYS A NZ    1 
ATOM   16124 N N     . SER A 1 3748 ? 220.464 136.913 183.193 1.00 38.97 ? 3748 SER A N     1 
ATOM   16125 C CA    . SER A 1 3748 ? 221.035 135.850 184.017 1.00 37.22 ? 3748 SER A CA    1 
ATOM   16126 C C     . SER A 1 3748 ? 220.911 134.495 183.329 1.00 35.53 ? 3748 SER A C     1 
ATOM   16127 O O     . SER A 1 3748 ? 221.852 133.691 183.344 1.00 35.01 ? 3748 SER A O     1 
ATOM   16128 C CB    . SER A 1 3748 ? 220.358 135.823 185.386 1.00 38.24 ? 3748 SER A CB    1 
ATOM   16129 O OG    . SER A 1 3748 ? 220.625 137.012 186.109 1.00 38.74 ? 3748 SER A OG    1 
ATOM   16130 N N     . LEU A 1 3749 ? 219.754 134.226 182.718 1.00 34.56 ? 3749 LEU A N     1 
ATOM   16131 C CA    . LEU A 1 3749 ? 219.580 132.994 181.956 1.00 37.75 ? 3749 LEU A CA    1 
ATOM   16132 C C     . LEU A 1 3749 ? 220.559 132.928 180.791 1.00 41.01 ? 3749 LEU A C     1 
ATOM   16133 O O     . LEU A 1 3749 ? 221.142 131.872 180.516 1.00 40.80 ? 3749 LEU A O     1 
ATOM   16134 C CB    . LEU A 1 3749 ? 218.141 132.892 181.447 1.00 37.41 ? 3749 LEU A CB    1 
ATOM   16135 C CG    . LEU A 1 3749 ? 217.843 131.737 180.487 1.00 39.21 ? 3749 LEU A CG    1 
ATOM   16136 C CD1   . LEU A 1 3749 ? 217.915 130.402 181.213 1.00 38.09 ? 3749 LEU A CD1   1 
ATOM   16137 C CD2   . LEU A 1 3749 ? 216.499 131.913 179.798 1.00 37.65 ? 3749 LEU A CD2   1 
ATOM   16138 N N     . LEU A 1 3750 ? 220.745 134.050 180.092 1.00 40.12 ? 3750 LEU A N     1 
ATOM   16139 C CA    . LEU A 1 3750 ? 221.686 134.077 178.974 1.00 38.78 ? 3750 LEU A CA    1 
ATOM   16140 C C     . LEU A 1 3750 ? 223.107 133.785 179.438 1.00 37.97 ? 3750 LEU A C     1 
ATOM   16141 O O     . LEU A 1 3750 ? 223.848 133.053 178.770 1.00 39.42 ? 3750 LEU A O     1 
ATOM   16142 C CB    . LEU A 1 3750 ? 221.624 135.428 178.264 1.00 35.29 ? 3750 LEU A CB    1 
ATOM   16143 C CG    . LEU A 1 3750 ? 220.436 135.640 177.326 1.00 38.29 ? 3750 LEU A CG    1 
ATOM   16144 C CD1   . LEU A 1 3750 ? 220.341 137.097 176.907 1.00 38.49 ? 3750 LEU A CD1   1 
ATOM   16145 C CD2   . LEU A 1 3750 ? 220.553 134.734 176.112 1.00 37.18 ? 3750 LEU A CD2   1 
ATOM   16146 N N     . GLN A 1 3751 ? 223.510 134.355 180.577 1.00 35.22 ? 3751 GLN A N     1 
ATOM   16147 C CA    . GLN A 1 3751 ? 224.837 134.068 181.116 1.00 37.90 ? 3751 GLN A CA    1 
ATOM   16148 C C     . GLN A 1 3751 ? 224.971 132.601 181.511 1.00 38.38 ? 3751 GLN A C     1 
ATOM   16149 O O     . GLN A 1 3751 ? 226.005 131.972 181.254 1.00 35.98 ? 3751 GLN A O     1 
ATOM   16150 C CB    . GLN A 1 3751 ? 225.128 134.976 182.311 1.00 37.48 ? 3751 GLN A CB    1 
ATOM   16151 C CG    . GLN A 1 3751 ? 225.184 136.453 181.967 1.00 36.68 ? 3751 GLN A CG    1 
ATOM   16152 C CD    . GLN A 1 3751 ? 226.218 136.760 180.902 1.00 37.35 ? 3751 GLN A CD    1 
ATOM   16153 O OE1   . GLN A 1 3751 ? 225.879 137.084 179.764 1.00 36.18 ? 3751 GLN A OE1   1 
ATOM   16154 N NE2   . GLN A 1 3751 ? 227.490 136.657 181.268 1.00 36.40 ? 3751 GLN A NE2   1 
ATOM   16155 N N     . ALA A 1 3752 ? 223.936 132.036 182.135 1.00 38.39 ? 3752 ALA A N     1 
ATOM   16156 C CA    . ALA A 1 3752 ? 223.999 130.631 182.522 1.00 36.98 ? 3752 ALA A CA    1 
ATOM   16157 C C     . ALA A 1 3752 ? 224.066 129.712 181.308 1.00 35.32 ? 3752 ALA A C     1 
ATOM   16158 O O     . ALA A 1 3752 ? 224.689 128.644 181.374 1.00 35.43 ? 3752 ALA A O     1 
ATOM   16159 C CB    . ALA A 1 3752 ? 222.798 130.270 183.395 1.00 35.81 ? 3752 ALA A CB    1 
ATOM   16160 N N     . LEU A 1 3753 ? 223.442 130.113 180.197 1.00 34.07 ? 3753 LEU A N     1 
ATOM   16161 C CA    . LEU A 1 3753 ? 223.377 129.248 179.022 1.00 39.44 ? 3753 LEU A CA    1 
ATOM   16162 C C     . LEU A 1 3753 ? 224.767 128.930 178.483 1.00 41.18 ? 3753 LEU A C     1 
ATOM   16163 O O     . LEU A 1 3753 ? 225.067 127.775 178.158 1.00 38.06 ? 3753 LEU A O     1 
ATOM   16164 C CB    . LEU A 1 3753 ? 222.512 129.895 177.941 1.00 39.22 ? 3753 LEU A CB    1 
ATOM   16165 C CG    . LEU A 1 3753 ? 221.002 129.703 178.090 1.00 38.36 ? 3753 LEU A CG    1 
ATOM   16166 C CD1   . LEU A 1 3753 ? 220.247 130.699 177.226 1.00 36.84 ? 3753 LEU A CD1   1 
ATOM   16167 C CD2   . LEU A 1 3753 ? 220.606 128.276 177.746 1.00 37.39 ? 3753 LEU A CD2   1 
ATOM   16168 N N     . ASN A 1 3754 ? 225.631 129.937 178.375 1.00 41.96 ? 3754 ASN A N     1 
ATOM   16169 C CA    . ASN A 1 3754 ? 227.003 129.689 177.954 1.00 41.29 ? 3754 ASN A CA    1 
ATOM   16170 C C     . ASN A 1 3754 ? 227.949 129.460 179.126 1.00 40.98 ? 3754 ASN A C     1 
ATOM   16171 O O     . ASN A 1 3754 ? 229.121 129.143 178.901 1.00 41.30 ? 3754 ASN A O     1 
ATOM   16172 C CB    . ASN A 1 3754 ? 227.526 130.835 177.075 1.00 39.33 ? 3754 ASN A CB    1 
ATOM   16173 C CG    . ASN A 1 3754 ? 227.209 132.202 177.637 1.00 39.37 ? 3754 ASN A CG    1 
ATOM   16174 O OD1   . ASN A 1 3754 ? 226.677 132.327 178.735 1.00 36.98 ? 3754 ASN A OD1   1 
ATOM   16175 N ND2   . ASN A 1 3754 ? 227.545 133.242 176.882 1.00 39.41 ? 3754 ASN A ND2   1 
ATOM   16176 N N     . GLU A 1 3755 ? 227.476 129.608 180.368 1.00 40.59 ? 3755 GLU A N     1 
ATOM   16177 C CA    . GLU A 1 3755 ? 228.267 129.139 181.500 1.00 42.06 ? 3755 GLU A CA    1 
ATOM   16178 C C     . GLU A 1 3755 ? 228.271 127.617 181.572 1.00 40.01 ? 3755 GLU A C     1 
ATOM   16179 O O     . GLU A 1 3755 ? 229.315 127.004 181.821 1.00 41.14 ? 3755 GLU A O     1 
ATOM   16180 C CB    . GLU A 1 3755 ? 227.731 129.734 182.802 1.00 40.05 ? 3755 GLU A CB    1 
ATOM   16181 C CG    . GLU A 1 3755 ? 228.530 129.338 184.033 0.00 37.84 ? 3755 GLU A CG    1 
ATOM   16182 C CD    . GLU A 1 3755 ? 227.914 129.848 185.321 0.00 37.87 ? 3755 GLU A CD    1 
ATOM   16183 O OE1   . GLU A 1 3755 ? 226.850 129.328 185.719 0.00 37.82 ? 3755 GLU A OE1   1 
ATOM   16184 O OE2   . GLU A 1 3755 ? 228.494 130.767 185.936 0.00 37.90 ? 3755 GLU A OE2   1 
ATOM   16185 N N     . VAL A 1 3756 ? 227.111 126.988 181.352 1.00 37.47 ? 3756 VAL A N     1 
ATOM   16186 C CA    . VAL A 1 3756 ? 227.027 125.529 181.396 1.00 41.06 ? 3756 VAL A CA    1 
ATOM   16187 C C     . VAL A 1 3756 ? 227.366 124.876 180.064 1.00 38.52 ? 3756 VAL A C     1 
ATOM   16188 O O     . VAL A 1 3756 ? 227.594 123.656 180.027 1.00 35.54 ? 3756 VAL A O     1 
ATOM   16189 C CB    . VAL A 1 3756 ? 225.627 125.063 181.842 1.00 40.32 ? 3756 VAL A CB    1 
ATOM   16190 C CG1   . VAL A 1 3756 ? 225.267 125.676 183.187 1.00 37.01 ? 3756 VAL A CG1   1 
ATOM   16191 C CG2   . VAL A 1 3756 ? 224.586 125.413 180.788 1.00 36.24 ? 3756 VAL A CG2   1 
ATOM   16192 N N     . LYS A 1 3757 ? 227.413 125.645 178.974 1.00 34.88 ? 3757 LYS A N     1 
ATOM   16193 C CA    . LYS A 1 3757 ? 227.724 125.126 177.640 1.00 37.85 ? 3757 LYS A CA    1 
ATOM   16194 C C     . LYS A 1 3757 ? 226.780 123.991 177.249 1.00 38.84 ? 3757 LYS A C     1 
ATOM   16195 O O     . LYS A 1 3757 ? 227.181 123.004 176.629 1.00 36.41 ? 3757 LYS A O     1 
ATOM   16196 C CB    . LYS A 1 3757 ? 229.184 124.675 177.549 1.00 35.98 ? 3757 LYS A CB    1 
ATOM   16197 C CG    . LYS A 1 3757 ? 229.832 124.959 176.204 0.00 34.59 ? 3757 LYS A CG    1 
ATOM   16198 C CD    . LYS A 1 3757 ? 231.241 124.396 176.133 0.00 34.55 ? 3757 LYS A CD    1 
ATOM   16199 C CE    . LYS A 1 3757 ? 231.231 122.877 176.196 0.00 34.56 ? 3757 LYS A CE    1 
ATOM   16200 N NZ    . LYS A 1 3757 ? 232.590 122.321 176.440 0.00 34.55 ? 3757 LYS A NZ    1 
ATOM   16201 N N     . GLY A 1 3758 ? 225.509 124.139 177.611 1.00 39.57 ? 3758 GLY A N     1 
ATOM   16202 C CA    . GLY A 1 3758 ? 224.514 123.135 177.267 1.00 36.84 ? 3758 GLY A CA    1 
ATOM   16203 C C     . GLY A 1 3758 ? 224.739 121.788 177.918 1.00 35.69 ? 3758 GLY A C     1 
ATOM   16204 O O     . GLY A 1 3758 ? 224.640 120.753 177.247 1.00 36.18 ? 3758 GLY A O     1 
ATOM   16205 N N     . ARG A 1 3759 ? 225.048 121.776 179.214 1.00 38.16 ? 3759 ARG A N     1 
ATOM   16206 C CA    . ARG A 1 3759 ? 225.245 120.518 179.921 1.00 41.93 ? 3759 ARG A CA    1 
ATOM   16207 C C     . ARG A 1 3759 ? 223.948 119.721 179.967 1.00 40.38 ? 3759 ARG A C     1 
ATOM   16208 O O     . ARG A 1 3759 ? 222.872 120.265 180.232 1.00 40.71 ? 3759 ARG A O     1 
ATOM   16209 C CB    . ARG A 1 3759 ? 225.752 120.778 181.340 1.00 40.02 ? 3759 ARG A CB    1 
ATOM   16210 C CG    . ARG A 1 3759 ? 226.514 119.610 181.945 0.00 37.06 ? 3759 ARG A CG    1 
ATOM   16211 C CD    . ARG A 1 3759 ? 228.005 119.716 181.676 0.00 37.06 ? 3759 ARG A CD    1 
ATOM   16212 N NE    . ARG A 1 3759 ? 228.537 121.021 182.051 0.00 37.03 ? 3759 ARG A NE    1 
ATOM   16213 C CZ    . ARG A 1 3759 ? 229.565 121.611 181.456 0.00 37.01 ? 3759 ARG A CZ    1 
ATOM   16214 N NH1   . ARG A 1 3759 ? 230.198 121.041 180.443 0.00 36.98 ? 3759 ARG A NH1   1 
ATOM   16215 N NH2   . ARG A 1 3759 ? 229.968 122.802 181.888 0.00 36.99 ? 3759 ARG A NH2   1 
ATOM   16216 N N     . ILE A 1 3760 ? 224.055 118.419 179.705 1.00 39.99 ? 3760 ILE A N     1 
ATOM   16217 C CA    . ILE A 1 3760 ? 222.900 117.539 179.719 1.00 40.72 ? 3760 ILE A CA    1 
ATOM   16218 C C     . ILE A 1 3760 ? 222.929 116.553 180.884 1.00 42.56 ? 3760 ILE A C     1 
ATOM   16219 O O     . ILE A 1 3760 ? 221.861 116.141 181.355 1.00 43.22 ? 3760 ILE A O     1 
ATOM   16220 C CB    . ILE A 1 3760 ? 222.764 116.795 178.372 1.00 38.15 ? 3760 ILE A CB    1 
ATOM   16221 C CG1   . ILE A 1 3760 ? 221.382 116.147 178.246 0.00 38.52 ? 3760 ILE A CG1   1 
ATOM   16222 C CG2   . ILE A 1 3760 ? 223.871 115.761 178.202 0.00 38.49 ? 3760 ILE A CG2   1 
ATOM   16223 C CD1   . ILE A 1 3760 ? 220.248 117.143 178.163 0.00 38.45 ? 3760 ILE A CD1   1 
ATOM   16224 N N     . LEU A 1 3761 ? 224.113 116.168 181.371 1.00 40.44 ? 3761 LEU A N     1 
ATOM   16225 C CA    . LEU A 1 3761 ? 224.182 115.279 182.527 1.00 39.21 ? 3761 LEU A CA    1 
ATOM   16226 C C     . LEU A 1 3761 ? 223.621 115.952 183.774 1.00 39.21 ? 3761 LEU A C     1 
ATOM   16227 O O     . LEU A 1 3761 ? 222.874 115.330 184.539 1.00 38.95 ? 3761 LEU A O     1 
ATOM   16228 C CB    . LEU A 1 3761 ? 225.624 114.831 182.762 1.00 35.89 ? 3761 LEU A CB    1 
ATOM   16229 C CG    . LEU A 1 3761 ? 225.827 113.794 183.869 0.00 36.24 ? 3761 LEU A CG    1 
ATOM   16230 C CD1   . LEU A 1 3761 ? 224.989 112.553 183.603 0.00 36.21 ? 3761 LEU A CD1   1 
ATOM   16231 C CD2   . LEU A 1 3761 ? 227.297 113.434 184.007 0.00 36.21 ? 3761 LEU A CD2   1 
ATOM   16232 N N     . ASP A 1 3762 ? 223.968 117.217 183.993 1.00 37.45 ? 3762 ASP A N     1 
ATOM   16233 C CA    . ASP A 1 3762 ? 223.451 118.011 185.104 1.00 38.06 ? 3762 ASP A CA    1 
ATOM   16234 C C     . ASP A 1 3762 ? 222.629 119.142 184.496 1.00 41.35 ? 3762 ASP A C     1 
ATOM   16235 O O     . ASP A 1 3762 ? 223.134 120.246 184.277 1.00 43.00 ? 3762 ASP A O     1 
ATOM   16236 C CB    . ASP A 1 3762 ? 224.585 118.542 185.983 1.00 36.61 ? 3762 ASP A CB    1 
ATOM   16237 C CG    . ASP A 1 3762 ? 224.129 118.862 187.394 0.00 36.20 ? 3762 ASP A CG    1 
ATOM   16238 O OD1   . ASP A 1 3762 ? 222.929 119.154 187.581 0.00 36.11 ? 3762 ASP A OD1   1 
ATOM   16239 O OD2   . ASP A 1 3762 ? 224.971 118.824 188.315 0.00 36.20 ? 3762 ASP A OD2   1 
ATOM   16240 N N     . ASP A 1 3763 ? 221.355 118.861 184.224 1.00 40.34 ? 3763 ASP A N     1 
ATOM   16241 C CA    . ASP A 1 3763 ? 220.473 119.841 183.608 1.00 40.60 ? 3763 ASP A CA    1 
ATOM   16242 C C     . ASP A 1 3763 ? 219.724 120.693 184.623 1.00 37.57 ? 3763 ASP A C     1 
ATOM   16243 O O     . ASP A 1 3763 ? 219.177 121.736 184.248 1.00 33.70 ? 3763 ASP A O     1 
ATOM   16244 C CB    . ASP A 1 3763 ? 219.464 119.139 182.692 1.00 37.16 ? 3763 ASP A CB    1 
ATOM   16245 C CG    . ASP A 1 3763 ? 218.860 120.075 181.663 0.00 35.59 ? 3763 ASP A CG    1 
ATOM   16246 O OD1   . ASP A 1 3763 ? 219.585 120.961 181.164 0.00 35.41 ? 3763 ASP A OD1   1 
ATOM   16247 O OD2   . ASP A 1 3763 ? 217.660 119.925 181.352 0.00 35.62 ? 3763 ASP A OD2   1 
ATOM   16248 N N     . ASP A 1 3764 ? 219.700 120.283 185.895 1.00 35.63 ? 3764 ASP A N     1 
ATOM   16249 C CA    . ASP A 1 3764 ? 218.924 121.010 186.896 1.00 36.08 ? 3764 ASP A CA    1 
ATOM   16250 C C     . ASP A 1 3764 ? 219.437 122.431 187.089 1.00 35.80 ? 3764 ASP A C     1 
ATOM   16251 O O     . ASP A 1 3764 ? 218.673 123.314 187.498 1.00 34.38 ? 3764 ASP A O     1 
ATOM   16252 C CB    . ASP A 1 3764 ? 218.943 120.254 188.225 1.00 34.26 ? 3764 ASP A CB    1 
ATOM   16253 C CG    . ASP A 1 3764 ? 217.722 120.541 189.078 0.00 33.39 ? 3764 ASP A CG    1 
ATOM   16254 O OD1   . ASP A 1 3764 ? 216.891 121.379 188.669 0.00 33.56 ? 3764 ASP A OD1   1 
ATOM   16255 O OD2   . ASP A 1 3764 ? 217.593 119.928 190.159 0.00 33.33 ? 3764 ASP A OD2   1 
ATOM   16256 N N     . THR A 1 3765 ? 220.715 122.675 186.785 1.00 37.89 ? 3765 THR A N     1 
ATOM   16257 C CA    . THR A 1 3765 ? 221.280 124.011 186.951 1.00 38.31 ? 3765 THR A CA    1 
ATOM   16258 C C     . THR A 1 3765 ? 220.547 125.031 186.087 1.00 37.42 ? 3765 THR A C     1 
ATOM   16259 O O     . THR A 1 3765 ? 220.334 126.173 186.509 1.00 33.59 ? 3765 THR A O     1 
ATOM   16260 C CB    . THR A 1 3765 ? 222.771 123.997 186.614 1.00 37.90 ? 3765 THR A CB    1 
ATOM   16261 O OG1   . THR A 1 3765 ? 223.403 122.896 187.279 1.00 38.32 ? 3765 THR A OG1   1 
ATOM   16262 C CG2   . THR A 1 3765 ? 223.430 125.294 187.060 1.00 34.15 ? 3765 THR A CG2   1 
ATOM   16263 N N     . ILE A 1 3766 ? 220.156 124.639 184.875 1.00 39.05 ? 3766 ILE A N     1 
ATOM   16264 C CA    . ILE A 1 3766 ? 219.352 125.503 184.020 1.00 39.21 ? 3766 ILE A CA    1 
ATOM   16265 C C     . ILE A 1 3766 ? 217.854 125.262 184.195 1.00 38.18 ? 3766 ILE A C     1 
ATOM   16266 O O     . ILE A 1 3766 ? 217.059 126.182 183.944 1.00 37.81 ? 3766 ILE A O     1 
ATOM   16267 C CB    . ILE A 1 3766 ? 219.753 125.341 182.537 1.00 37.61 ? 3766 ILE A CB    1 
ATOM   16268 C CG1   . ILE A 1 3766 ? 219.404 126.603 181.744 1.00 37.30 ? 3766 ILE A CG1   1 
ATOM   16269 C CG2   . ILE A 1 3766 ? 219.089 124.119 181.918 1.00 33.38 ? 3766 ILE A CG2   1 
ATOM   16270 C CD1   . ILE A 1 3766 ? 220.349 127.757 181.991 1.00 38.12 ? 3766 ILE A CD1   1 
ATOM   16271 N N     . ILE A 1 3767 ? 217.448 124.067 184.632 1.00 38.47 ? 3767 ILE A N     1 
ATOM   16272 C CA    . ILE A 1 3767 ? 216.029 123.789 184.824 1.00 38.65 ? 3767 ILE A CA    1 
ATOM   16273 C C     . ILE A 1 3767 ? 215.466 124.639 185.955 1.00 38.63 ? 3767 ILE A C     1 
ATOM   16274 O O     . ILE A 1 3767 ? 214.323 125.104 185.886 1.00 38.44 ? 3767 ILE A O     1 
ATOM   16275 C CB    . ILE A 1 3767 ? 215.804 122.284 185.069 1.00 36.90 ? 3767 ILE A CB    1 
ATOM   16276 C CG1   . ILE A 1 3767 ? 216.111 121.488 183.799 1.00 36.67 ? 3767 ILE A CG1   1 
ATOM   16277 C CG2   . ILE A 1 3767 ? 214.376 122.014 185.525 1.00 34.01 ? 3767 ILE A CG2   1 
ATOM   16278 C CD1   . ILE A 1 3767 ? 215.223 121.844 182.624 1.00 34.07 ? 3767 ILE A CD1   1 
ATOM   16279 N N     . THR A 1 3768 ? 216.256 124.864 187.009 1.00 37.12 ? 3768 THR A N     1 
ATOM   16280 C CA    . THR A 1 3768 ? 215.796 125.719 188.099 1.00 38.59 ? 3768 THR A CA    1 
ATOM   16281 C C     . THR A 1 3768 ? 215.541 127.141 187.613 1.00 39.30 ? 3768 THR A C     1 
ATOM   16282 O O     . THR A 1 3768 ? 214.511 127.744 187.941 1.00 39.34 ? 3768 THR A O     1 
ATOM   16283 C CB    . THR A 1 3768 ? 216.817 125.715 189.237 1.00 37.81 ? 3768 THR A CB    1 
ATOM   16284 O OG1   . THR A 1 3768 ? 217.002 124.375 189.711 1.00 34.10 ? 3768 THR A OG1   1 
ATOM   16285 C CG2   . THR A 1 3768 ? 216.339 126.590 190.386 1.00 35.99 ? 3768 THR A CG2   1 
ATOM   16286 N N     . THR A 1 3769 ? 216.463 127.688 186.815 1.00 40.71 ? 3769 THR A N     1 
ATOM   16287 C CA    . THR A 1 3769 ? 216.279 129.036 186.284 1.00 41.32 ? 3769 THR A CA    1 
ATOM   16288 C C     . THR A 1 3769 ? 215.077 129.104 185.351 1.00 38.45 ? 3769 THR A C     1 
ATOM   16289 O O     . THR A 1 3769 ? 214.303 130.068 185.393 1.00 36.77 ? 3769 THR A O     1 
ATOM   16290 C CB    . THR A 1 3769 ? 217.544 129.492 185.557 1.00 40.98 ? 3769 THR A CB    1 
ATOM   16291 O OG1   . THR A 1 3769 ? 218.692 129.211 186.368 1.00 41.41 ? 3769 THR A OG1   1 
ATOM   16292 C CG2   . THR A 1 3769 ? 217.485 130.984 185.271 1.00 38.29 ? 3769 THR A CG2   1 
ATOM   16293 N N     . LEU A 1 3770 ? 214.905 128.091 184.498 1.00 38.32 ? 3770 LEU A N     1 
ATOM   16294 C CA    . LEU A 1 3770 ? 213.762 128.078 183.589 1.00 41.38 ? 3770 LEU A CA    1 
ATOM   16295 C C     . LEU A 1 3770 ? 212.446 128.000 184.357 1.00 42.46 ? 3770 LEU A C     1 
ATOM   16296 O O     . LEU A 1 3770 ? 211.471 128.675 184.005 1.00 41.77 ? 3770 LEU A O     1 
ATOM   16297 C CB    . LEU A 1 3770 ? 213.891 126.914 182.608 1.00 39.38 ? 3770 LEU A CB    1 
ATOM   16298 C CG    . LEU A 1 3770 ? 215.064 127.012 181.628 1.00 41.65 ? 3770 LEU A CG    1 
ATOM   16299 C CD1   . LEU A 1 3770 ? 215.197 125.747 180.793 1.00 41.23 ? 3770 LEU A CD1   1 
ATOM   16300 C CD2   . LEU A 1 3770 ? 214.916 128.233 180.734 1.00 40.78 ? 3770 LEU A CD2   1 
ATOM   16301 N N     . GLU A 1 3771 ? 212.401 127.182 185.411 1.00 40.03 ? 3771 GLU A N     1 
ATOM   16302 C CA    . GLU A 1 3771 ? 211.197 127.079 186.229 1.00 40.18 ? 3771 GLU A CA    1 
ATOM   16303 C C     . GLU A 1 3771 ? 210.903 128.391 186.947 1.00 40.97 ? 3771 GLU A C     1 
ATOM   16304 O O     . GLU A 1 3771 ? 209.741 128.808 187.037 1.00 39.15 ? 3771 GLU A O     1 
ATOM   16305 C CB    . GLU A 1 3771 ? 211.350 125.933 187.230 1.00 39.82 ? 3771 GLU A CB    1 
ATOM   16306 C CG    . GLU A 1 3771 ? 210.059 125.494 187.899 1.00 40.02 ? 3771 GLU A CG    1 
ATOM   16307 C CD    . GLU A 1 3771 ? 209.782 126.245 189.184 1.00 42.95 ? 3771 GLU A CD    1 
ATOM   16308 O OE1   . GLU A 1 3771 ? 210.735 126.806 189.764 1.00 42.38 ? 3771 GLU A OE1   1 
ATOM   16309 O OE2   . GLU A 1 3771 ? 208.612 126.267 189.620 1.00 43.49 ? 3771 GLU A OE2   1 
ATOM   16310 N N     . ASN A 1 3772 ? 211.940 129.053 187.466 1.00 39.48 ? 3772 ASN A N     1 
ATOM   16311 C CA    . ASN A 1 3772 ? 211.737 130.350 188.104 1.00 39.58 ? 3772 ASN A CA    1 
ATOM   16312 C C     . ASN A 1 3772 ? 211.212 131.375 187.107 1.00 41.03 ? 3772 ASN A C     1 
ATOM   16313 O O     . ASN A 1 3772 ? 210.326 132.175 187.435 1.00 38.94 ? 3772 ASN A O     1 
ATOM   16314 C CB    . ASN A 1 3772 ? 213.038 130.837 188.740 1.00 38.13 ? 3772 ASN A CB    1 
ATOM   16315 C CG    . ASN A 1 3772 ? 213.506 129.941 189.869 1.00 40.83 ? 3772 ASN A CG    1 
ATOM   16316 O OD1   . ASN A 1 3772 ? 214.697 129.659 190.002 1.00 41.48 ? 3772 ASN A OD1   1 
ATOM   16317 N ND2   . ASN A 1 3772 ? 212.566 129.484 190.688 1.00 39.83 ? 3772 ASN A ND2   1 
ATOM   16318 N N     . LEU A 1 3773 ? 211.751 131.368 185.884 1.00 41.04 ? 3773 LEU A N     1 
ATOM   16319 C CA    . LEU A 1 3773 ? 211.260 132.275 184.852 1.00 39.89 ? 3773 LEU A CA    1 
ATOM   16320 C C     . LEU A 1 3773 ? 209.800 131.997 184.523 1.00 38.81 ? 3773 LEU A C     1 
ATOM   16321 O O     . LEU A 1 3773 ? 209.002 132.929 184.377 1.00 37.47 ? 3773 LEU A O     1 
ATOM   16322 C CB    . LEU A 1 3773 ? 212.123 132.159 183.596 1.00 40.11 ? 3773 LEU A CB    1 
ATOM   16323 C CG    . LEU A 1 3773 ? 213.364 133.051 183.554 1.00 40.05 ? 3773 LEU A CG    1 
ATOM   16324 C CD1   . LEU A 1 3773 ? 214.437 132.431 182.682 1.00 41.74 ? 3773 LEU A CD1   1 
ATOM   16325 C CD2   . LEU A 1 3773 ? 213.007 134.442 183.056 1.00 36.39 ? 3773 LEU A CD2   1 
ATOM   16326 N N     . LYS A 1 3774 ? 209.432 130.720 184.405 1.00 38.54 ? 3774 LYS A N     1 
ATOM   16327 C CA    . LYS A 1 3774 ? 208.038 130.374 184.142 1.00 38.99 ? 3774 LYS A CA    1 
ATOM   16328 C C     . LYS A 1 3774 ? 207.132 130.865 185.266 1.00 39.13 ? 3774 LYS A C     1 
ATOM   16329 O O     . LYS A 1 3774 ? 206.065 131.440 185.012 1.00 38.45 ? 3774 LYS A O     1 
ATOM   16330 C CB    . LYS A 1 3774 ? 207.904 128.861 183.962 1.00 38.18 ? 3774 LYS A CB    1 
ATOM   16331 C CG    . LYS A 1 3774 ? 206.491 128.356 183.684 1.00 36.85 ? 3774 LYS A CG    1 
ATOM   16332 C CD    . LYS A 1 3774 ? 205.750 129.226 182.678 1.00 37.23 ? 3774 LYS A CD    1 
ATOM   16333 C CE    . LYS A 1 3774 ? 206.141 128.874 181.252 1.00 37.77 ? 3774 LYS A CE    1 
ATOM   16334 N NZ    . LYS A 1 3774 ? 205.630 129.873 180.275 1.00 38.91 ? 3774 LYS A NZ    1 
ATOM   16335 N N     . ARG A 1 3775 ? 207.549 130.661 186.519 1.00 39.29 ? 3775 ARG A N     1 
ATOM   16336 C CA    . ARG A 1 3775 ? 206.722 131.069 187.650 1.00 40.28 ? 3775 ARG A CA    1 
ATOM   16337 C C     . ARG A 1 3775 ? 206.558 132.583 187.710 1.00 40.44 ? 3775 ARG A C     1 
ATOM   16338 O O     . ARG A 1 3775 ? 205.451 133.083 187.941 1.00 35.69 ? 3775 ARG A O     1 
ATOM   16339 C CB    . ARG A 1 3775 ? 207.317 130.541 188.956 1.00 36.31 ? 3775 ARG A CB    1 
ATOM   16340 C CG    . ARG A 1 3775 ? 207.100 129.048 189.217 0.00 36.54 ? 3775 ARG A CG    1 
ATOM   16341 C CD    . ARG A 1 3775 ? 205.636 128.676 189.499 0.00 36.41 ? 3775 ARG A CD    1 
ATOM   16342 N NE    . ARG A 1 3775 ? 204.764 128.746 188.331 0.00 36.35 ? 3775 ARG A NE    1 
ATOM   16343 C CZ    . ARG A 1 3775 ? 204.859 127.961 187.265 0.00 36.38 ? 3775 ARG A CZ    1 
ATOM   16344 N NH1   . ARG A 1 3775 ? 205.761 126.996 187.193 0.00 36.44 ? 3775 ARG A NH1   1 
ATOM   16345 N NH2   . ARG A 1 3775 ? 204.020 128.143 186.249 0.00 36.33 ? 3775 ARG A NH2   1 
ATOM   16346 N N     . GLU A 1 3776 ? 207.642 133.335 187.500 1.00 39.60 ? 3776 GLU A N     1 
ATOM   16347 C CA    . GLU A 1 3776 ? 207.533 134.791 187.550 1.00 37.13 ? 3776 GLU A CA    1 
ATOM   16348 C C     . GLU A 1 3776 ? 206.741 135.334 186.364 1.00 37.09 ? 3776 GLU A C     1 
ATOM   16349 O O     . GLU A 1 3776 ? 206.017 136.328 186.500 1.00 34.19 ? 3776 GLU A O     1 
ATOM   16350 C CB    . GLU A 1 3776 ? 208.921 135.427 187.630 1.00 33.74 ? 3776 GLU A CB    1 
ATOM   16351 C CG    . GLU A 1 3776 ? 209.839 135.103 186.471 1.00 37.60 ? 3776 GLU A CG    1 
ATOM   16352 C CD    . GLU A 1 3776 ? 209.639 136.010 185.281 1.00 40.02 ? 3776 GLU A CD    1 
ATOM   16353 O OE1   . GLU A 1 3776 ? 209.078 137.112 185.456 1.00 38.96 ? 3776 GLU A OE1   1 
ATOM   16354 O OE2   . GLU A 1 3776 ? 210.031 135.606 184.167 1.00 39.95 ? 3776 GLU A OE2   1 
ATOM   16355 N N     . ALA A 1 3777 ? 206.856 134.699 185.194 1.00 35.68 ? 3777 ALA A N     1 
ATOM   16356 C CA    . ALA A 1 3777 ? 206.028 135.098 184.061 1.00 35.16 ? 3777 ALA A CA    1 
ATOM   16357 C C     . ALA A 1 3777 ? 204.555 134.864 184.358 1.00 34.95 ? 3777 ALA A C     1 
ATOM   16358 O O     . ALA A 1 3777 ? 203.707 135.707 184.042 1.00 32.80 ? 3777 ALA A O     1 
ATOM   16359 C CB    . ALA A 1 3777 ? 206.451 134.341 182.803 1.00 35.10 ? 3777 ALA A CB    1 
ATOM   16360 N N     . ALA A 1 3778 ? 204.232 133.722 184.972 1.00 36.91 ? 3778 ALA A N     1 
ATOM   16361 C CA    . ALA A 1 3778 ? 202.851 133.464 185.367 1.00 37.38 ? 3778 ALA A CA    1 
ATOM   16362 C C     . ALA A 1 3778 ? 202.373 134.487 186.388 1.00 38.76 ? 3778 ALA A C     1 
ATOM   16363 O O     . ALA A 1 3778 ? 201.226 134.940 186.333 1.00 37.85 ? 3778 ALA A O     1 
ATOM   16364 C CB    . ALA A 1 3778 ? 202.720 132.045 185.921 1.00 34.99 ? 3778 ALA A CB    1 
ATOM   16365 N N     . GLU A 1 3779 ? 203.242 134.861 187.330 1.00 36.76 ? 3779 GLU A N     1 
ATOM   16366 C CA    . GLU A 1 3779 ? 202.878 135.864 188.328 1.00 35.83 ? 3779 GLU A CA    1 
ATOM   16367 C C     . GLU A 1 3779 ? 202.581 137.212 187.681 1.00 38.75 ? 3779 GLU A C     1 
ATOM   16368 O O     . GLU A 1 3779 ? 201.591 137.872 188.023 1.00 38.73 ? 3779 GLU A O     1 
ATOM   16369 C CB    . GLU A 1 3779 ? 203.999 135.999 189.357 1.00 36.55 ? 3779 GLU A CB    1 
ATOM   16370 C CG    . GLU A 1 3779 ? 204.063 137.350 190.045 1.00 35.83 ? 3779 GLU A CG    1 
ATOM   16371 C CD    . GLU A 1 3779 ? 205.342 137.536 190.832 1.00 38.37 ? 3779 GLU A CD    1 
ATOM   16372 O OE1   . GLU A 1 3779 ? 206.093 136.550 190.986 1.00 39.40 ? 3779 GLU A OE1   1 
ATOM   16373 O OE2   . GLU A 1 3779 ? 205.598 138.666 191.297 1.00 41.26 ? 3779 GLU A OE2   1 
ATOM   16374 N N     . VAL A 1 3780 ? 203.428 137.636 186.741 1.00 40.91 ? 3780 VAL A N     1 
ATOM   16375 C CA    . VAL A 1 3780 ? 203.208 138.911 186.065 1.00 38.24 ? 3780 VAL A CA    1 
ATOM   16376 C C     . VAL A 1 3780 ? 201.938 138.857 185.225 1.00 35.08 ? 3780 VAL A C     1 
ATOM   16377 O O     . VAL A 1 3780 ? 201.178 139.830 185.162 1.00 37.30 ? 3780 VAL A O     1 
ATOM   16378 C CB    . VAL A 1 3780 ? 204.440 139.289 185.221 1.00 38.40 ? 3780 VAL A CB    1 
ATOM   16379 C CG1   . VAL A 1 3780 ? 204.144 140.499 184.350 1.00 34.63 ? 3780 VAL A CG1   1 
ATOM   16380 C CG2   . VAL A 1 3780 ? 205.628 139.571 186.126 1.00 36.84 ? 3780 VAL A CG2   1 
ATOM   16381 N N     . THR A 1 3781 ? 201.681 137.719 184.573 1.00 35.56 ? 3781 THR A N     1 
ATOM   16382 C CA    . THR A 1 3781 ? 200.447 137.568 183.809 1.00 37.48 ? 3781 THR A CA    1 
ATOM   16383 C C     . THR A 1 3781 ? 199.224 137.653 184.716 1.00 36.44 ? 3781 THR A C     1 
ATOM   16384 O O     . THR A 1 3781 ? 198.222 138.284 184.360 1.00 34.14 ? 3781 THR A O     1 
ATOM   16385 C CB    . THR A 1 3781 ? 200.461 136.243 183.047 1.00 38.16 ? 3781 THR A CB    1 
ATOM   16386 O OG1   . THR A 1 3781 ? 201.583 136.215 182.156 1.00 38.11 ? 3781 THR A OG1   1 
ATOM   16387 C CG2   . THR A 1 3781 ? 199.182 136.073 182.242 1.00 34.56 ? 3781 THR A CG2   1 
ATOM   16388 N N     . ARG A 1 3782 ? 199.290 137.026 185.893 1.00 36.63 ? 3782 ARG A N     1 
ATOM   16389 C CA    . ARG A 1 3782 ? 198.185 137.113 186.844 1.00 37.85 ? 3782 ARG A CA    1 
ATOM   16390 C C     . ARG A 1 3782 ? 197.972 138.546 187.309 1.00 37.39 ? 3782 ARG A C     1 
ATOM   16391 O O     . ARG A 1 3782 ? 196.831 139.000 187.449 1.00 35.12 ? 3782 ARG A O     1 
ATOM   16392 C CB    . ARG A 1 3782 ? 198.443 136.201 188.044 1.00 34.98 ? 3782 ARG A CB    1 
ATOM   16393 C CG    . ARG A 1 3782 ? 198.399 134.719 187.731 1.00 36.54 ? 3782 ARG A CG    1 
ATOM   16394 C CD    . ARG A 1 3782 ? 198.583 133.889 188.991 1.00 37.55 ? 3782 ARG A CD    1 
ATOM   16395 N NE    . ARG A 1 3782 ? 199.932 133.995 189.534 1.00 38.82 ? 3782 ARG A NE    1 
ATOM   16396 C CZ    . ARG A 1 3782 ? 200.232 134.573 190.690 1.00 39.94 ? 3782 ARG A CZ    1 
ATOM   16397 N NH1   . ARG A 1 3782 ? 199.299 135.125 191.449 1.00 39.49 ? 3782 ARG A NH1   1 
ATOM   16398 N NH2   . ARG A 1 3782 ? 201.499 134.595 191.095 1.00 38.81 ? 3782 ARG A NH2   1 
ATOM   16399 N N     . LYS A 1 3783 ? 199.062 139.270 187.571 1.00 36.41 ? 3783 LYS A N     1 
ATOM   16400 C CA    . LYS A 1 3783 ? 198.934 140.661 187.992 1.00 33.23 ? 3783 LYS A CA    1 
ATOM   16401 C C     . LYS A 1 3783 ? 198.309 141.517 186.897 1.00 33.00 ? 3783 LYS A C     1 
ATOM   16402 O O     . LYS A 1 3783 ? 197.454 142.365 187.175 1.00 34.58 ? 3783 LYS A O     1 
ATOM   16403 C CB    . LYS A 1 3783 ? 200.297 141.216 188.396 1.00 30.65 ? 3783 LYS A CB    1 
ATOM   16404 C CG    . LYS A 1 3783 ? 200.762 140.783 189.771 1.00 33.03 ? 3783 LYS A CG    1 
ATOM   16405 C CD    . LYS A 1 3783 ? 202.076 141.449 190.131 1.00 34.65 ? 3783 LYS A CD    1 
ATOM   16406 C CE    . LYS A 1 3783 ? 202.382 141.309 191.609 1.00 32.46 ? 3783 LYS A CE    1 
ATOM   16407 N NZ    . LYS A 1 3783 ? 202.656 139.895 191.979 1.00 34.16 ? 3783 LYS A NZ    1 
ATOM   16408 N N     . VAL A 1 3784 ? 198.724 141.312 185.644 1.00 34.03 ? 3784 VAL A N     1 
ATOM   16409 C CA    . VAL A 1 3784 ? 198.168 142.095 184.544 1.00 32.47 ? 3784 VAL A CA    1 
ATOM   16410 C C     . VAL A 1 3784 ? 196.697 141.759 184.330 1.00 33.48 ? 3784 VAL A C     1 
ATOM   16411 O O     . VAL A 1 3784 ? 195.874 142.648 184.082 1.00 29.98 ? 3784 VAL A O     1 
ATOM   16412 C CB    . VAL A 1 3784 ? 198.992 141.888 183.260 1.00 31.61 ? 3784 VAL A CB    1 
ATOM   16413 C CG1   . VAL A 1 3784 ? 198.346 142.617 182.094 1.00 30.72 ? 3784 VAL A CG1   1 
ATOM   16414 C CG2   . VAL A 1 3784 ? 200.411 142.392 183.457 1.00 28.82 ? 3784 VAL A CG2   1 
ATOM   16415 N N     . GLU A 1 3785 ? 196.337 140.477 184.419 1.00 36.40 ? 3785 GLU A N     1 
ATOM   16416 C CA    . GLU A 1 3785 ? 194.944 140.094 184.225 1.00 35.91 ? 3785 GLU A CA    1 
ATOM   16417 C C     . GLU A 1 3785 ? 194.056 140.496 185.394 1.00 36.27 ? 3785 GLU A C     1 
ATOM   16418 O O     . GLU A 1 3785 ? 192.832 140.521 185.234 1.00 39.78 ? 3785 GLU A O     1 
ATOM   16419 C CB    . GLU A 1 3785 ? 194.834 138.586 183.980 1.00 34.39 ? 3785 GLU A CB    1 
ATOM   16420 C CG    . GLU A 1 3785 ? 195.010 137.729 185.219 1.00 36.60 ? 3785 GLU A CG    1 
ATOM   16421 C CD    . GLU A 1 3785 ? 195.017 136.246 184.905 1.00 38.34 ? 3785 GLU A CD    1 
ATOM   16422 O OE1   . GLU A 1 3785 ? 194.938 135.890 183.711 1.00 37.93 ? 3785 GLU A OE1   1 
ATOM   16423 O OE2   . GLU A 1 3785 ? 195.101 135.436 185.853 1.00 36.84 ? 3785 GLU A OE2   1 
ATOM   16424 N N     . GLU A 1 3786 ? 194.632 140.804 186.555 1.00 32.34 ? 3786 GLU A N     1 
ATOM   16425 C CA    . GLU A 1 3786 ? 193.877 141.315 187.691 1.00 32.55 ? 3786 GLU A CA    1 
ATOM   16426 C C     . GLU A 1 3786 ? 193.828 142.836 187.732 1.00 33.34 ? 3786 GLU A C     1 
ATOM   16427 O O     . GLU A 1 3786 ? 193.236 143.397 188.659 1.00 34.06 ? 3786 GLU A O     1 
ATOM   16428 C CB    . GLU A 1 3786 ? 194.461 140.784 189.005 1.00 34.14 ? 3786 GLU A CB    1 
ATOM   16429 C CG    . GLU A 1 3786 ? 194.180 139.314 189.269 1.00 34.21 ? 3786 GLU A CG    1 
ATOM   16430 C CD    . GLU A 1 3786 ? 194.984 138.769 190.434 1.00 35.19 ? 3786 GLU A CD    1 
ATOM   16431 O OE1   . GLU A 1 3786 ? 195.798 139.526 191.003 1.00 36.15 ? 3786 GLU A OE1   1 
ATOM   16432 O OE2   . GLU A 1 3786 ? 194.800 137.584 190.782 1.00 35.87 ? 3786 GLU A OE2   1 
ATOM   16433 N N     . THR A 1 3787 ? 194.433 143.514 186.754 1.00 32.82 ? 3787 THR A N     1 
ATOM   16434 C CA    . THR A 1 3787 ? 194.385 144.970 186.681 1.00 30.54 ? 3787 THR A CA    1 
ATOM   16435 C C     . THR A 1 3787 ? 192.959 145.493 186.536 1.00 30.97 ? 3787 THR A C     1 
ATOM   16436 O O     . THR A 1 3787 ? 192.705 146.658 186.856 1.00 28.90 ? 3787 THR A O     1 
ATOM   16437 C CB    . THR A 1 3787 ? 195.262 145.451 185.517 1.00 31.53 ? 3787 THR A CB    1 
ATOM   16438 O OG1   . THR A 1 3787 ? 196.607 145.007 185.727 1.00 30.90 ? 3787 THR A OG1   1 
ATOM   16439 C CG2   . THR A 1 3787 ? 195.276 146.971 185.414 1.00 31.35 ? 3787 THR A CG2   1 
ATOM   16440 N N     . ASP A 1 3788 ? 192.025 144.662 186.075 1.00 37.42 ? 3788 ASP A N     1 
ATOM   16441 C CA    . ASP A 1 3788 ? 190.617 145.037 186.055 1.00 37.00 ? 3788 ASP A CA    1 
ATOM   16442 C C     . ASP A 1 3788 ? 189.967 144.895 187.428 1.00 35.07 ? 3788 ASP A C     1 
ATOM   16443 O O     . ASP A 1 3788 ? 189.223 145.785 187.854 1.00 31.56 ? 3788 ASP A O     1 
ATOM   16444 C CB    . ASP A 1 3788 ? 189.863 144.193 185.022 1.00 34.21 ? 3788 ASP A CB    1 
ATOM   16445 C CG    . ASP A 1 3788 ? 190.086 142.704 185.208 1.00 34.36 ? 3788 ASP A CG    1 
ATOM   16446 O OD1   . ASP A 1 3788 ? 190.887 142.327 186.089 1.00 33.30 ? 3788 ASP A OD1   1 
ATOM   16447 O OD2   . ASP A 1 3788 ? 189.460 141.911 184.474 1.00 36.76 ? 3788 ASP A OD2   1 
ATOM   16448 N N     . ILE A 1 3789 ? 190.233 143.787 188.127 1.00 32.09 ? 3789 ILE A N     1 
ATOM   16449 C CA    . ILE A 1 3789 ? 189.712 143.616 189.480 1.00 31.51 ? 3789 ILE A CA    1 
ATOM   16450 C C     . ILE A 1 3789 ? 190.329 144.641 190.422 1.00 32.97 ? 3789 ILE A C     1 
ATOM   16451 O O     . ILE A 1 3789 ? 189.633 145.254 191.239 1.00 35.82 ? 3789 ILE A O     1 
ATOM   16452 C CB    . ILE A 1 3789 ? 189.958 142.178 189.972 1.00 33.34 ? 3789 ILE A CB    1 
ATOM   16453 C CG1   . ILE A 1 3789 ? 189.355 141.166 188.997 1.00 34.18 ? 3789 ILE A CG1   1 
ATOM   16454 C CG2   . ILE A 1 3789 ? 189.392 141.989 191.371 1.00 30.34 ? 3789 ILE A CG2   1 
ATOM   16455 C CD1   . ILE A 1 3789 ? 189.481 139.727 189.454 1.00 31.48 ? 3789 ILE A CD1   1 
ATOM   16456 N N     . VAL A 1 3790 ? 191.636 144.837 190.330 1.00 34.10 ? 3790 VAL A N     1 
ATOM   16457 C CA    . VAL A 1 3790 ? 192.312 145.870 191.100 1.00 31.48 ? 3790 VAL A CA    1 
ATOM   16458 C C     . VAL A 1 3790 ? 192.058 147.205 190.408 1.00 33.47 ? 3790 VAL A C     1 
ATOM   16459 O O     . VAL A 1 3790 ? 191.737 147.246 189.216 1.00 33.81 ? 3790 VAL A O     1 
ATOM   16460 C CB    . VAL A 1 3790 ? 193.813 145.531 191.224 1.00 28.57 ? 3790 VAL A CB    1 
ATOM   16461 C CG1   . VAL A 1 3790 ? 194.557 146.571 192.027 1.00 27.74 ? 3790 VAL A CG1   1 
ATOM   16462 C CG2   . VAL A 1 3790 ? 193.993 144.149 191.833 1.00 27.08 ? 3790 VAL A CG2   1 
ATOM   16463 N N     . MET A 1 3791 ? 192.155 148.305 191.157 1.00 33.39 ? 3791 MET A N     1 
ATOM   16464 C CA    . MET A 1 3791 ? 191.669 149.637 190.790 1.00 30.75 ? 3791 MET A CA    1 
ATOM   16465 C C     . MET A 1 3791 ? 190.151 149.693 190.717 1.00 29.69 ? 3791 MET A C     1 
ATOM   16466 O O     . MET A 1 3791 ? 189.599 150.757 190.423 1.00 30.05 ? 3791 MET A O     1 
ATOM   16467 C CB    . MET A 1 3791 ? 192.232 150.154 189.456 1.00 31.10 ? 3791 MET A CB    1 
ATOM   16468 C CG    . MET A 1 3791 ? 193.714 150.430 189.459 1.00 33.31 ? 3791 MET A CG    1 
ATOM   16469 S SD    . MET A 1 3791 ? 194.351 150.955 187.856 1.00 42.38 ? 3791 MET A SD    1 
ATOM   16470 C CE    . MET A 1 3791 ? 193.640 152.593 187.724 1.00 33.73 ? 3791 MET A CE    1 
ATOM   16471 N N     . GLN A 1 3792 ? 189.459 148.584 190.959 1.00 37.18 ? 3792 GLN A N     1 
ATOM   16472 C CA    . GLN A 1 3792 ? 188.015 148.565 191.134 1.00 38.57 ? 3792 GLN A CA    1 
ATOM   16473 C C     . GLN A 1 3792 ? 187.624 148.492 192.600 1.00 36.22 ? 3792 GLN A C     1 
ATOM   16474 O O     . GLN A 1 3792 ? 186.644 149.121 193.012 1.00 36.64 ? 3792 GLN A O     1 
ATOM   16475 C CB    . GLN A 1 3792 ? 187.403 147.383 190.374 1.00 37.76 ? 3792 GLN A CB    1 
ATOM   16476 C CG    . GLN A 1 3792 ? 185.896 147.460 190.197 1.00 37.03 ? 3792 GLN A CG    1 
ATOM   16477 C CD    . GLN A 1 3792 ? 185.144 146.835 191.355 1.00 37.39 ? 3792 GLN A CD    1 
ATOM   16478 O OE1   . GLN A 1 3792 ? 185.639 145.915 192.007 1.00 35.80 ? 3792 GLN A OE1   1 
ATOM   16479 N NE2   . GLN A 1 3792 ? 183.941 147.331 191.618 1.00 38.34 ? 3792 GLN A NE2   1 
ATOM   16480 N N     . GLU A 1 3793 ? 188.373 147.728 193.393 1.00 29.20 ? 3793 GLU A N     1 
ATOM   16481 C CA    . GLU A 1 3793 ? 188.251 147.773 194.842 1.00 33.87 ? 3793 GLU A CA    1 
ATOM   16482 C C     . GLU A 1 3793 ? 189.254 148.728 195.469 1.00 31.16 ? 3793 GLU A C     1 
ATOM   16483 O O     . GLU A 1 3793 ? 189.014 149.232 196.572 1.00 27.91 ? 3793 GLU A O     1 
ATOM   16484 C CB    . GLU A 1 3793 ? 188.419 146.370 195.432 1.00 32.88 ? 3793 GLU A CB    1 
ATOM   16485 C CG    . GLU A 1 3793 ? 189.634 145.615 194.922 1.00 34.28 ? 3793 GLU A CG    1 
ATOM   16486 C CD    . GLU A 1 3793 ? 190.867 145.849 195.770 1.00 32.54 ? 3793 GLU A CD    1 
ATOM   16487 O OE1   . GLU A 1 3793 ? 190.719 146.305 196.922 1.00 34.07 ? 3793 GLU A OE1   1 
ATOM   16488 O OE2   . GLU A 1 3793 ? 191.982 145.571 195.285 1.00 31.55 ? 3793 GLU A OE2   1 
ATOM   16489 N N     . VAL A 1 3794 ? 190.372 148.991 194.788 1.00 29.82 ? 3794 VAL A N     1 
ATOM   16490 C CA    . VAL A 1 3794 ? 191.315 149.999 195.265 1.00 28.14 ? 3794 VAL A CA    1 
ATOM   16491 C C     . VAL A 1 3794 ? 190.674 151.380 195.254 1.00 29.99 ? 3794 VAL A C     1 
ATOM   16492 O O     . VAL A 1 3794 ? 190.847 152.166 196.192 1.00 33.53 ? 3794 VAL A O     1 
ATOM   16493 C CB    . VAL A 1 3794 ? 192.606 149.967 194.430 1.00 27.91 ? 3794 VAL A CB    1 
ATOM   16494 C CG1   . VAL A 1 3794 ? 193.520 151.097 194.841 1.00 26.64 ? 3794 VAL A CG1   1 
ATOM   16495 C CG2   . VAL A 1 3794 ? 193.309 148.642 194.623 1.00 29.71 ? 3794 VAL A CG2   1 
ATOM   16496 N N     . GLU A 1 3795 ? 189.932 151.704 194.193 1.00 27.69 ? 3795 GLU A N     1 
ATOM   16497 C CA    . GLU A 1 3795 ? 189.229 152.982 194.161 1.00 24.97 ? 3795 GLU A CA    1 
ATOM   16498 C C     . GLU A 1 3795 ? 188.168 153.046 195.252 1.00 24.61 ? 3795 GLU A C     1 
ATOM   16499 O O     . GLU A 1 3795 ? 187.964 154.097 195.867 1.00 28.84 ? 3795 GLU A O     1 
ATOM   16500 C CB    . GLU A 1 3795 ? 188.615 153.221 192.779 1.00 29.71 ? 3795 GLU A CB    1 
ATOM   16501 C CG    . GLU A 1 3795 ? 187.567 152.206 192.334 1.00 31.57 ? 3795 GLU A CG    1 
ATOM   16502 C CD    . GLU A 1 3795 ? 186.164 152.572 192.780 1.00 33.53 ? 3795 GLU A CD    1 
ATOM   16503 O OE1   . GLU A 1 3795 ? 185.933 153.758 193.096 1.00 32.52 ? 3795 GLU A OE1   1 
ATOM   16504 O OE2   . GLU A 1 3795 ? 185.294 151.676 192.811 1.00 31.19 ? 3795 GLU A OE2   1 
ATOM   16505 N N     . THR A 1 3796 ? 187.493 151.924 195.519 1.00 23.06 ? 3796 THR A N     1 
ATOM   16506 C CA    . THR A 1 3796 ? 186.508 151.891 196.594 1.00 24.99 ? 3796 THR A CA    1 
ATOM   16507 C C     . THR A 1 3796 ? 187.159 152.153 197.947 1.00 20.79 ? 3796 THR A C     1 
ATOM   16508 O O     . THR A 1 3796 ? 186.647 152.941 198.751 1.00 22.83 ? 3796 THR A O     1 
ATOM   16509 C CB    . THR A 1 3796 ? 185.784 150.544 196.599 1.00 24.72 ? 3796 THR A CB    1 
ATOM   16510 O OG1   . THR A 1 3796 ? 185.027 150.400 195.390 1.00 24.18 ? 3796 THR A OG1   1 
ATOM   16511 C CG2   . THR A 1 3796 ? 184.844 150.445 197.788 1.00 23.17 ? 3796 THR A CG2   1 
ATOM   16512 N N     . VAL A 1 3797 ? 188.300 151.511 198.209 1.00 21.93 ? 3797 VAL A N     1 
ATOM   16513 C CA    . VAL A 1 3797 ? 188.994 151.710 199.479 1.00 21.48 ? 3797 VAL A CA    1 
ATOM   16514 C C     . VAL A 1 3797 ? 189.499 153.142 199.596 1.00 17.07 ? 3797 VAL A C     1 
ATOM   16515 O O     . VAL A 1 3797 ? 189.397 153.767 200.659 1.00 20.76 ? 3797 VAL A O     1 
ATOM   16516 C CB    . VAL A 1 3797 ? 190.135 150.687 199.631 1.00 20.79 ? 3797 VAL A CB    1 
ATOM   16517 C CG1   . VAL A 1 3797 ? 190.959 150.988 200.868 1.00 20.08 ? 3797 VAL A CG1   1 
ATOM   16518 C CG2   . VAL A 1 3797 ? 189.571 149.280 199.709 1.00 23.29 ? 3797 VAL A CG2   1 
ATOM   16519 N N     . SER A 1 3798 ? 190.053 153.687 198.510 1.00 15.97 ? 3798 SER A N     1 
ATOM   16520 C CA    . SER A 1 3798 ? 190.557 155.056 198.540 1.00 15.64 ? 3798 SER A CA    1 
ATOM   16521 C C     . SER A 1 3798 ? 189.432 156.052 198.791 1.00 16.03 ? 3798 SER A C     1 
ATOM   16522 O O     . SER A 1 3798 ? 189.596 157.011 199.553 1.00 23.95 ? 3798 SER A O     1 
ATOM   16523 C CB    . SER A 1 3798 ? 191.283 155.376 197.234 1.00 19.80 ? 3798 SER A CB    1 
ATOM   16524 O OG    . SER A 1 3798 ? 192.581 154.809 197.221 1.00 21.78 ? 3798 SER A OG    1 
ATOM   16525 N N     . GLN A 1 3799 ? 188.277 155.846 198.153 1.00 17.74 ? 3799 GLN A N     1 
ATOM   16526 C CA    . GLN A 1 3799 ? 187.130 156.709 198.407 1.00 18.11 ? 3799 GLN A CA    1 
ATOM   16527 C C     . GLN A 1 3799 ? 186.562 156.509 199.803 1.00 21.55 ? 3799 GLN A C     1 
ATOM   16528 O O     . GLN A 1 3799 ? 185.922 157.422 200.335 1.00 24.22 ? 3799 GLN A O     1 
ATOM   16529 C CB    . GLN A 1 3799 ? 186.039 156.465 197.363 1.00 18.49 ? 3799 GLN A CB    1 
ATOM   16530 C CG    . GLN A 1 3799 ? 186.417 156.895 195.956 1.00 19.97 ? 3799 GLN A CG    1 
ATOM   16531 C CD    . GLN A 1 3799 ? 186.593 158.394 195.834 1.00 24.73 ? 3799 GLN A CD    1 
ATOM   16532 O OE1   . GLN A 1 3799 ? 185.625 159.153 195.899 1.00 24.08 ? 3799 GLN A OE1   1 
ATOM   16533 N NE2   . GLN A 1 3799 ? 187.834 158.831 195.657 1.00 24.83 ? 3799 GLN A NE2   1 
ATOM   16534 N N     . GLN A 1 3800 ? 186.771 155.335 200.402 1.00 19.83 ? 3800 GLN A N     1 
ATOM   16535 C CA    . GLN A 1 3800 ? 186.326 155.115 201.773 1.00 15.06 ? 3800 GLN A CA    1 
ATOM   16536 C C     . GLN A 1 3800 ? 187.119 155.974 202.751 1.00 16.48 ? 3800 GLN A C     1 
ATOM   16537 O O     . GLN A 1 3800 ? 186.576 156.450 203.754 1.00 23.52 ? 3800 GLN A O     1 
ATOM   16538 C CB    . GLN A 1 3800 ? 186.446 153.632 202.126 1.00 14.27 ? 3800 GLN A CB    1 
ATOM   16539 C CG    . GLN A 1 3800 ? 186.163 153.301 203.581 1.00 17.39 ? 3800 GLN A CG    1 
ATOM   16540 C CD    . GLN A 1 3800 ? 187.001 152.144 204.089 1.00 21.19 ? 3800 GLN A CD    1 
ATOM   16541 O OE1   . GLN A 1 3800 ? 188.032 151.808 203.509 1.00 22.90 ? 3800 GLN A OE1   1 
ATOM   16542 N NE2   . GLN A 1 3800 ? 186.558 151.524 205.177 1.00 20.97 ? 3800 GLN A NE2   1 
ATOM   16543 N N     . TYR A 1 3801 ? 188.402 156.194 202.467 1.00 17.75 ? 3801 TYR A N     1 
ATOM   16544 C CA    . TYR A 1 3801 ? 189.290 156.944 203.342 1.00 12.56 ? 3801 TYR A CA    1 
ATOM   16545 C C     . TYR A 1 3801 ? 189.431 158.405 202.926 1.00 11.03 ? 3801 TYR A C     1 
ATOM   16546 O O     . TYR A 1 3801 ? 190.302 159.108 203.448 1.00 16.33 ? 3801 TYR A O     1 
ATOM   16547 C CB    . TYR A 1 3801 ? 190.666 156.276 203.381 1.00 12.93 ? 3801 TYR A CB    1 
ATOM   16548 C CG    . TYR A 1 3801 ? 190.706 154.999 204.186 1.00 11.59 ? 3801 TYR A CG    1 
ATOM   16549 C CD1   . TYR A 1 3801 ? 190.128 154.932 205.441 1.00 13.55 ? 3801 TYR A CD1   1 
ATOM   16550 C CD2   . TYR A 1 3801 ? 191.319 153.859 203.688 1.00 17.03 ? 3801 TYR A CD2   1 
ATOM   16551 C CE1   . TYR A 1 3801 ? 190.158 153.770 206.181 1.00 18.15 ? 3801 TYR A CE1   1 
ATOM   16552 C CE2   . TYR A 1 3801 ? 191.355 152.690 204.422 1.00 20.60 ? 3801 TYR A CE2   1 
ATOM   16553 C CZ    . TYR A 1 3801 ? 190.772 152.652 205.669 1.00 21.24 ? 3801 TYR A CZ    1 
ATOM   16554 O OH    . TYR A 1 3801 ? 190.799 151.495 206.411 1.00 23.84 ? 3801 TYR A OH    1 
ATOM   16555 N N     . LEU A 1 3802 ? 188.599 158.871 201.998 1.00 12.37 ? 3802 LEU A N     1 
ATOM   16556 C CA    . LEU A 1 3802 ? 188.658 160.234 201.478 1.00 12.29 ? 3802 LEU A CA    1 
ATOM   16557 C C     . LEU A 1 3802 ? 188.063 161.264 202.439 1.00 18.14 ? 3802 LEU A C     1 
ATOM   16558 O O     . LEU A 1 3802 ? 188.622 162.363 202.565 1.00 17.80 ? 3802 LEU A O     1 
ATOM   16559 C CB    . LEU A 1 3802 ? 187.951 160.313 200.122 1.00 10.07 ? 3802 LEU A CB    1 
ATOM   16560 C CG    . LEU A 1 3802 ? 188.155 161.599 199.322 1.00 13.84 ? 3802 LEU A CG    1 
ATOM   16561 C CD1   . LEU A 1 3802 ? 189.618 161.769 198.948 1.00 17.59 ? 3802 LEU A CD1   1 
ATOM   16562 C CD2   . LEU A 1 3802 ? 187.273 161.607 198.084 1.00 14.81 ? 3802 LEU A CD2   1 
ATOM   16563 N N     . PRO A 1 3803 ? 186.928 160.987 203.103 1.00 17.06 ? 3803 PRO A N     1 
ATOM   16564 C CA    . PRO A 1 3803 ? 186.441 161.954 204.102 1.00 11.73 ? 3803 PRO A CA    1 
ATOM   16565 C C     . PRO A 1 3803 ? 187.456 162.257 205.189 1.00 8.25  ? 3803 PRO A C     1 
ATOM   16566 O O     . PRO A 1 3803 ? 187.577 163.412 205.612 1.00 8.50  ? 3803 PRO A O     1 
ATOM   16567 C CB    . PRO A 1 3803 ? 185.190 161.270 204.664 1.00 8.74  ? 3803 PRO A CB    1 
ATOM   16568 C CG    . PRO A 1 3803 ? 184.698 160.446 203.549 1.00 10.65 ? 3803 PRO A CG    1 
ATOM   16569 C CD    . PRO A 1 3803 ? 185.924 159.935 202.851 1.00 12.77 ? 3803 PRO A CD    1 
ATOM   16570 N N     . LEU A 1 3804 ? 188.205 161.249 205.642 1.00 4.30  ? 3804 LEU A N     1 
ATOM   16571 C CA    . LEU A 1 3804 ? 189.242 161.490 206.639 1.00 6.11  ? 3804 LEU A CA    1 
ATOM   16572 C C     . LEU A 1 3804 ? 190.308 162.438 206.107 1.00 12.84 ? 3804 LEU A C     1 
ATOM   16573 O O     . LEU A 1 3804 ? 190.751 163.346 206.818 1.00 21.59 ? 3804 LEU A O     1 
ATOM   16574 C CB    . LEU A 1 3804 ? 189.871 160.165 207.068 1.00 9.17  ? 3804 LEU A CB    1 
ATOM   16575 C CG    . LEU A 1 3804 ? 190.973 160.229 208.127 1.00 3.14  ? 3804 LEU A CG    1 
ATOM   16576 C CD1   . LEU A 1 3804 ? 190.520 161.034 209.329 1.00 9.03  ? 3804 LEU A CD1   1 
ATOM   16577 C CD2   . LEU A 1 3804 ? 191.398 158.834 208.543 1.00 4.29  ? 3804 LEU A CD2   1 
ATOM   16578 N N     . SER A 1 3805 ? 190.727 162.250 204.855 1.00 6.43  ? 3805 SER A N     1 
ATOM   16579 C CA    . SER A 1 3805 ? 191.780 163.090 204.293 1.00 3.31  ? 3805 SER A CA    1 
ATOM   16580 C C     . SER A 1 3805 ? 191.303 164.521 204.085 1.00 9.80  ? 3805 SER A C     1 
ATOM   16581 O O     . SER A 1 3805 ? 192.044 165.475 204.360 1.00 12.65 ? 3805 SER A O     1 
ATOM   16582 C CB    . SER A 1 3805 ? 192.275 162.492 202.980 1.00 9.79  ? 3805 SER A CB    1 
ATOM   16583 O OG    . SER A 1 3805 ? 192.831 161.211 203.199 1.00 17.47 ? 3805 SER A OG    1 
ATOM   16584 N N     . THR A 1 3806 ? 190.076 164.699 203.591 1.00 11.39 ? 3806 THR A N     1 
ATOM   16585 C CA    . THR A 1 3806 ? 189.572 166.057 203.415 1.00 9.08  ? 3806 THR A CA    1 
ATOM   16586 C C     . THR A 1 3806 ? 189.358 166.738 204.762 1.00 9.18  ? 3806 THR A C     1 
ATOM   16587 O O     . THR A 1 3806 ? 189.607 167.942 204.899 1.00 11.65 ? 3806 THR A O     1 
ATOM   16588 C CB    . THR A 1 3806 ? 188.291 166.059 202.572 1.00 10.19 ? 3806 THR A CB    1 
ATOM   16589 O OG1   . THR A 1 3806 ? 187.960 167.405 202.208 1.00 10.76 ? 3806 THR A OG1   1 
ATOM   16590 C CG2   . THR A 1 3806 ? 187.120 165.446 203.314 1.00 11.43 ? 3806 THR A CG2   1 
ATOM   16591 N N     . ALA A 1 3807 ? 188.937 165.979 205.781 1.00 13.99 ? 3807 ALA A N     1 
ATOM   16592 C CA    . ALA A 1 3807 ? 188.844 166.534 207.125 1.00 7.83  ? 3807 ALA A CA    1 
ATOM   16593 C C     . ALA A 1 3807 ? 190.213 166.948 207.641 1.00 4.98  ? 3807 ALA A C     1 
ATOM   16594 O O     . ALA A 1 3807 ? 190.349 167.995 208.278 1.00 9.62  ? 3807 ALA A O     1 
ATOM   16595 C CB    . ALA A 1 3807 ? 188.198 165.522 208.070 1.00 6.75  ? 3807 ALA A CB    1 
ATOM   16596 N N     . CYS A 1 3808 ? 191.238 166.136 207.380 1.00 3.07  ? 3808 CYS A N     1 
ATOM   16597 C CA    . CYS A 1 3808 ? 192.588 166.478 207.816 1.00 3.04  ? 3808 CYS A CA    1 
ATOM   16598 C C     . CYS A 1 3808 ? 193.073 167.760 207.156 1.00 6.70  ? 3808 CYS A C     1 
ATOM   16599 O O     . CYS A 1 3808 ? 193.649 168.631 207.819 1.00 5.40  ? 3808 CYS A O     1 
ATOM   16600 C CB    . CYS A 1 3808 ? 193.544 165.332 207.496 1.00 2.22  ? 3808 CYS A CB    1 
ATOM   16601 S SG    . CYS A 1 3808 ? 193.371 163.906 208.562 1.00 7.77  ? 3808 CYS A SG    1 
ATOM   16602 N N     . SER A 1 3809 ? 192.856 167.886 205.846 1.00 9.76  ? 3809 SER A N     1 
ATOM   16603 C CA    . SER A 1 3809 ? 193.265 169.099 205.144 1.00 9.22  ? 3809 SER A CA    1 
ATOM   16604 C C     . SER A 1 3809 ? 192.521 170.320 205.672 1.00 8.62  ? 3809 SER A C     1 
ATOM   16605 O O     . SER A 1 3809 ? 193.129 171.371 205.918 1.00 10.46 ? 3809 SER A O     1 
ATOM   16606 C CB    . SER A 1 3809 ? 193.032 168.937 203.643 1.00 12.11 ? 3809 SER A CB    1 
ATOM   16607 O OG    . SER A 1 3809 ? 191.716 169.327 203.289 1.00 14.12 ? 3809 SER A OG    1 
ATOM   16608 N N     . SER A 1 3810 ? 191.204 170.195 205.866 1.00 4.25  ? 3810 SER A N     1 
ATOM   16609 C CA    . SER A 1 3810 ? 190.422 171.310 206.386 1.00 3.44  ? 3810 SER A CA    1 
ATOM   16610 C C     . SER A 1 3810 ? 190.878 171.701 207.785 1.00 9.60  ? 3810 SER A C     1 
ATOM   16611 O O     . SER A 1 3810 ? 190.994 172.891 208.097 1.00 9.61  ? 3810 SER A O     1 
ATOM   16612 C CB    . SER A 1 3810 ? 188.936 170.953 206.387 1.00 9.30  ? 3810 SER A CB    1 
ATOM   16613 O OG    . SER A 1 3810 ? 188.490 170.610 205.087 1.00 16.67 ? 3810 SER A OG    1 
ATOM   16614 N N     . ILE A 1 3811 ? 191.149 170.713 208.641 1.00 9.53  ? 3811 ILE A N     1 
ATOM   16615 C CA    . ILE A 1 3811 ? 191.593 170.997 210.002 1.00 3.72  ? 3811 ILE A CA    1 
ATOM   16616 C C     . ILE A 1 3811 ? 192.936 171.710 209.986 1.00 1.30  ? 3811 ILE A C     1 
ATOM   16617 O O     . ILE A 1 3811 ? 193.126 172.722 210.671 1.00 9.49  ? 3811 ILE A O     1 
ATOM   16618 C CB    . ILE A 1 3811 ? 191.655 169.701 210.830 1.00 2.28  ? 3811 ILE A CB    1 
ATOM   16619 C CG1   . ILE A 1 3811 ? 190.249 169.214 211.178 1.00 2.37  ? 3811 ILE A CG1   1 
ATOM   16620 C CG2   . ILE A 1 3811 ? 192.480 169.906 212.087 1.00 4.18  ? 3811 ILE A CG2   1 
ATOM   16621 C CD1   . ILE A 1 3811 ? 190.226 167.848 211.811 1.00 5.14  ? 3811 ILE A CD1   1 
ATOM   16622 N N     . TYR A 1 3812 ? 193.889 171.198 209.203 1.00 3.85  ? 3812 TYR A N     1 
ATOM   16623 C CA    . TYR A 1 3812 ? 195.207 171.820 209.177 1.00 3.57  ? 3812 TYR A CA    1 
ATOM   16624 C C     . TYR A 1 3812 ? 195.135 173.242 208.646 1.00 5.00  ? 3812 TYR A C     1 
ATOM   16625 O O     . TYR A 1 3812 ? 195.828 174.132 209.147 1.00 6.63  ? 3812 TYR A O     1 
ATOM   16626 C CB    . TYR A 1 3812 ? 196.189 171.014 208.335 1.00 3.85  ? 3812 TYR A CB    1 
ATOM   16627 C CG    . TYR A 1 3812 ? 197.428 171.820 208.024 1.00 8.68  ? 3812 TYR A CG    1 
ATOM   16628 C CD1   . TYR A 1 3812 ? 198.283 172.229 209.040 1.00 12.54 ? 3812 TYR A CD1   1 
ATOM   16629 C CD2   . TYR A 1 3812 ? 197.724 172.208 206.726 1.00 8.45  ? 3812 TYR A CD2   1 
ATOM   16630 C CE1   . TYR A 1 3812 ? 199.407 172.982 208.769 1.00 10.87 ? 3812 TYR A CE1   1 
ATOM   16631 C CE2   . TYR A 1 3812 ? 198.848 172.962 206.446 1.00 6.44  ? 3812 TYR A CE2   1 
ATOM   16632 C CZ    . TYR A 1 3812 ? 199.685 173.345 207.471 1.00 7.64  ? 3812 TYR A CZ    1 
ATOM   16633 O OH    . TYR A 1 3812 ? 200.806 174.093 207.201 1.00 8.85  ? 3812 TYR A OH    1 
ATOM   16634 N N     . PHE A 1 3813 ? 194.321 173.481 207.620 1.00 6.29  ? 3813 PHE A N     1 
ATOM   16635 C CA    . PHE A 1 3813 ? 194.287 174.830 207.074 1.00 4.31  ? 3813 PHE A CA    1 
ATOM   16636 C C     . PHE A 1 3813 ? 193.472 175.783 207.941 1.00 4.82  ? 3813 PHE A C     1 
ATOM   16637 O O     . PHE A 1 3813 ? 193.749 176.986 207.948 1.00 8.27  ? 3813 PHE A O     1 
ATOM   16638 C CB    . PHE A 1 3813 ? 193.792 174.795 205.632 1.00 4.89  ? 3813 PHE A CB    1 
ATOM   16639 C CG    . PHE A 1 3813 ? 194.898 174.575 204.644 1.00 6.30  ? 3813 PHE A CG    1 
ATOM   16640 C CD1   . PHE A 1 3813 ? 195.292 173.296 204.302 1.00 6.90  ? 3813 PHE A CD1   1 
ATOM   16641 C CD2   . PHE A 1 3813 ? 195.581 175.647 204.098 1.00 7.99  ? 3813 PHE A CD2   1 
ATOM   16642 C CE1   . PHE A 1 3813 ? 196.324 173.090 203.414 1.00 6.33  ? 3813 PHE A CE1   1 
ATOM   16643 C CE2   . PHE A 1 3813 ? 196.614 175.445 203.208 1.00 8.01  ? 3813 PHE A CE2   1 
ATOM   16644 C CZ    . PHE A 1 3813 ? 196.986 174.166 202.866 1.00 7.35  ? 3813 PHE A CZ    1 
ATOM   16645 N N     . THR A 1 3814 ? 192.507 175.276 208.711 1.00 3.75  ? 3814 THR A N     1 
ATOM   16646 C CA    . THR A 1 3814 ? 191.896 176.101 209.748 1.00 1.69  ? 3814 THR A CA    1 
ATOM   16647 C C     . THR A 1 3814 ? 192.919 176.484 210.811 1.00 3.24  ? 3814 THR A C     1 
ATOM   16648 O O     . THR A 1 3814 ? 192.972 177.639 211.250 1.00 11.33 ? 3814 THR A O     1 
ATOM   16649 C CB    . THR A 1 3814 ? 190.714 175.365 210.379 1.00 5.20  ? 3814 THR A CB    1 
ATOM   16650 O OG1   . THR A 1 3814 ? 189.762 175.027 209.363 1.00 10.61 ? 3814 THR A OG1   1 
ATOM   16651 C CG2   . THR A 1 3814 ? 190.040 176.238 211.421 1.00 6.33  ? 3814 THR A CG2   1 
ATOM   16652 N N     . MET A 1 3815 ? 193.754 175.527 211.224 1.00 4.68  ? 3815 MET A N     1 
ATOM   16653 C CA    . MET A 1 3815 ? 194.845 175.839 212.143 1.00 0.53  ? 3815 MET A CA    1 
ATOM   16654 C C     . MET A 1 3815 ? 195.784 176.884 211.555 1.00 5.85  ? 3815 MET A C     1 
ATOM   16655 O O     . MET A 1 3815 ? 196.229 177.798 212.257 1.00 9.86  ? 3815 MET A O     1 
ATOM   16656 C CB    . MET A 1 3815 ? 195.618 174.566 212.486 1.00 0.00  ? 3815 MET A CB    1 
ATOM   16657 C CG    . MET A 1 3815 ? 194.789 173.475 213.131 1.00 3.22  ? 3815 MET A CG    1 
ATOM   16658 S SD    . MET A 1 3815 ? 195.632 171.883 213.106 1.00 18.00 ? 3815 MET A SD    1 
ATOM   16659 C CE    . MET A 1 3815 ? 197.008 172.206 214.194 1.00 5.68  ? 3815 MET A CE    1 
ATOM   16660 N N     . GLU A 1 3816 ? 196.106 176.755 210.268 1.00 7.60  ? 3816 GLU A N     1 
ATOM   16661 C CA    . GLU A 1 3816 ? 196.991 177.715 209.618 1.00 4.18  ? 3816 GLU A CA    1 
ATOM   16662 C C     . GLU A 1 3816 ? 196.364 179.104 209.580 1.00 4.74  ? 3816 GLU A C     1 
ATOM   16663 O O     . GLU A 1 3816 ? 197.049 180.109 209.797 1.00 6.97  ? 3816 GLU A O     1 
ATOM   16664 C CB    . GLU A 1 3816 ? 197.328 177.236 208.206 1.00 7.39  ? 3816 GLU A CB    1 
ATOM   16665 C CG    . GLU A 1 3816 ? 198.284 178.136 207.448 1.00 11.01 ? 3816 GLU A CG    1 
ATOM   16666 C CD    . GLU A 1 3816 ? 199.659 178.182 208.082 1.00 18.24 ? 3816 GLU A CD    1 
ATOM   16667 O OE1   . GLU A 1 3816 ? 200.033 177.207 208.768 1.00 14.12 ? 3816 GLU A OE1   1 
ATOM   16668 O OE2   . GLU A 1 3816 ? 200.369 179.192 207.894 1.00 17.46 ? 3816 GLU A OE2   1 
ATOM   16669 N N     . SER A 1 3817 ? 195.062 179.180 209.298 1.00 4.88  ? 3817 SER A N     1 
ATOM   16670 C CA    . SER A 1 3817 ? 194.353 180.453 209.275 1.00 4.07  ? 3817 SER A CA    1 
ATOM   16671 C C     . SER A 1 3817 ? 194.107 181.020 210.666 1.00 7.92  ? 3817 SER A C     1 
ATOM   16672 O O     . SER A 1 3817 ? 193.739 182.193 210.779 1.00 10.32 ? 3817 SER A O     1 
ATOM   16673 C CB    . SER A 1 3817 ? 193.020 180.295 208.542 1.00 8.84  ? 3817 SER A CB    1 
ATOM   16674 O OG    . SER A 1 3817 ? 193.222 180.117 207.152 1.00 9.66  ? 3817 SER A OG    1 
ATOM   16675 N N     . LEU A 1 3818 ? 194.281 180.216 211.718 1.00 10.27 ? 3818 LEU A N     1 
ATOM   16676 C CA    . LEU A 1 3818 ? 194.149 180.717 213.084 1.00 3.46  ? 3818 LEU A CA    1 
ATOM   16677 C C     . LEU A 1 3818 ? 195.112 181.856 213.399 1.00 2.14  ? 3818 LEU A C     1 
ATOM   16678 O O     . LEU A 1 3818 ? 194.978 182.476 214.459 1.00 3.00  ? 3818 LEU A O     1 
ATOM   16679 C CB    . LEU A 1 3818 ? 194.355 179.572 214.079 1.00 3.01  ? 3818 LEU A CB    1 
ATOM   16680 C CG    . LEU A 1 3818 ? 193.116 178.782 214.506 1.00 1.01  ? 3818 LEU A CG    1 
ATOM   16681 C CD1   . LEU A 1 3818 ? 193.438 177.896 215.687 1.00 8.47  ? 3818 LEU A CD1   1 
ATOM   16682 C CD2   . LEU A 1 3818 ? 191.990 179.722 214.871 1.00 1.72  ? 3818 LEU A CD2   1 
ATOM   16683 N N     . LYS A 1 3819 ? 196.074 182.140 212.517 1.00 7.48  ? 3819 LYS A N     1 
ATOM   16684 C CA    . LYS A 1 3819 ? 196.906 183.329 212.665 1.00 4.05  ? 3819 LYS A CA    1 
ATOM   16685 C C     . LYS A 1 3819 ? 196.067 184.597 212.709 1.00 6.82  ? 3819 LYS A C     1 
ATOM   16686 O O     . LYS A 1 3819 ? 196.405 185.543 213.429 1.00 9.09  ? 3819 LYS A O     1 
ATOM   16687 C CB    . LYS A 1 3819 ? 197.897 183.417 211.506 1.00 2.96  ? 3819 LYS A CB    1 
ATOM   16688 C CG    . LYS A 1 3819 ? 199.019 182.409 211.540 1.00 8.25  ? 3819 LYS A CG    1 
ATOM   16689 C CD    . LYS A 1 3819 ? 200.256 182.974 210.870 1.00 8.24  ? 3819 LYS A CD    1 
ATOM   16690 C CE    . LYS A 1 3819 ? 200.067 183.046 209.367 1.00 4.49  ? 3819 LYS A CE    1 
ATOM   16691 N NZ    . LYS A 1 3819 ? 199.676 181.728 208.801 1.00 4.52  ? 3819 LYS A NZ    1 
ATOM   16692 N N     . GLN A 1 3820 ? 194.978 184.637 211.940 1.00 5.70  ? 3820 GLN A N     1 
ATOM   16693 C CA    . GLN A 1 3820 ? 194.169 185.847 211.852 1.00 1.55  ? 3820 GLN A CA    1 
ATOM   16694 C C     . GLN A 1 3820 ? 193.480 186.153 213.175 1.00 4.19  ? 3820 GLN A C     1 
ATOM   16695 O O     . GLN A 1 3820 ? 193.303 187.322 213.535 1.00 13.54 ? 3820 GLN A O     1 
ATOM   16696 C CB    . GLN A 1 3820 ? 193.138 185.704 210.733 1.00 4.03  ? 3820 GLN A CB    1 
ATOM   16697 C CG    . GLN A 1 3820 ? 193.694 185.161 209.422 1.00 6.33  ? 3820 GLN A CG    1 
ATOM   16698 C CD    . GLN A 1 3820 ? 194.985 185.835 208.996 1.00 8.22  ? 3820 GLN A CD    1 
ATOM   16699 O OE1   . GLN A 1 3820 ? 195.972 185.167 208.687 1.00 12.55 ? 3820 GLN A OE1   1 
ATOM   16700 N NE2   . GLN A 1 3820 ? 194.980 187.162 208.962 1.00 8.52  ? 3820 GLN A NE2   1 
ATOM   16701 N N     . ILE A 1 3821 ? 193.071 185.114 213.905 1.00 2.94  ? 3821 ILE A N     1 
ATOM   16702 C CA    . ILE A 1 3821 ? 192.359 185.316 215.165 1.00 1.51  ? 3821 ILE A CA    1 
ATOM   16703 C C     . ILE A 1 3821 ? 193.266 185.982 216.191 1.00 6.73  ? 3821 ILE A C     1 
ATOM   16704 O O     . ILE A 1 3821 ? 192.868 186.929 216.879 1.00 11.04 ? 3821 ILE A O     1 
ATOM   16705 C CB    . ILE A 1 3821 ? 191.808 183.977 215.687 1.00 1.31  ? 3821 ILE A CB    1 
ATOM   16706 C CG1   . ILE A 1 3821 ? 190.799 183.389 214.701 1.00 7.20  ? 3821 ILE A CG1   1 
ATOM   16707 C CG2   . ILE A 1 3821 ? 191.165 184.158 217.048 1.00 5.53  ? 3821 ILE A CG2   1 
ATOM   16708 C CD1   . ILE A 1 3821 ? 189.798 184.389 214.190 1.00 9.26  ? 3821 ILE A CD1   1 
ATOM   16709 N N     . HIS A 1 3822 ? 194.500 185.500 216.306 1.00 6.69  ? 3822 HIS A N     1 
ATOM   16710 C CA    . HIS A 1 3822 ? 195.431 185.993 217.308 1.00 3.47  ? 3822 HIS A CA    1 
ATOM   16711 C C     . HIS A 1 3822 ? 196.848 185.686 216.852 1.00 7.78  ? 3822 HIS A C     1 
ATOM   16712 O O     . HIS A 1 3822 ? 197.112 184.630 216.273 1.00 14.74 ? 3822 HIS A O     1 
ATOM   16713 C CB    . HIS A 1 3822 ? 195.154 185.360 218.675 1.00 2.78  ? 3822 HIS A CB    1 
ATOM   16714 C CG    . HIS A 1 3822 ? 195.811 186.063 219.821 1.00 4.88  ? 3822 HIS A CG    1 
ATOM   16715 N ND1   . HIS A 1 3822 ? 196.907 185.549 220.478 1.00 0.68  ? 3822 HIS A ND1   1 
ATOM   16716 C CD2   . HIS A 1 3822 ? 195.510 187.226 220.444 1.00 7.59  ? 3822 HIS A CD2   1 
ATOM   16717 C CE1   . HIS A 1 3822 ? 197.263 186.372 221.447 1.00 1.26  ? 3822 HIS A CE1   1 
ATOM   16718 N NE2   . HIS A 1 3822 ? 196.431 187.397 221.449 1.00 7.91  ? 3822 HIS A NE2   1 
ATOM   16719 N N     . PHE A 1 3823 ? 197.758 186.624 217.120 1.00 8.29  ? 3823 PHE A N     1 
ATOM   16720 C CA    . PHE A 1 3823 ? 199.145 186.462 216.701 1.00 8.51  ? 3823 PHE A CA    1 
ATOM   16721 C C     . PHE A 1 3823 ? 199.821 185.266 217.356 1.00 4.82  ? 3823 PHE A C     1 
ATOM   16722 O O     . PHE A 1 3823 ? 200.746 184.697 216.770 1.00 8.71  ? 3823 PHE A O     1 
ATOM   16723 C CB    . PHE A 1 3823 ? 199.937 187.734 217.006 1.00 8.04  ? 3823 PHE A CB    1 
ATOM   16724 C CG    . PHE A 1 3823 ? 200.057 188.036 218.473 1.00 6.62  ? 3823 PHE A CG    1 
ATOM   16725 C CD1   . PHE A 1 3823 ? 199.086 188.781 219.120 1.00 4.55  ? 3823 PHE A CD1   1 
ATOM   16726 C CD2   . PHE A 1 3823 ? 201.133 187.569 219.208 1.00 5.69  ? 3823 PHE A CD2   1 
ATOM   16727 C CE1   . PHE A 1 3823 ? 199.189 189.056 220.465 1.00 6.77  ? 3823 PHE A CE1   1 
ATOM   16728 C CE2   . PHE A 1 3823 ? 201.237 187.838 220.554 1.00 6.08  ? 3823 PHE A CE2   1 
ATOM   16729 C CZ    . PHE A 1 3823 ? 200.266 188.586 221.182 1.00 9.08  ? 3823 PHE A CZ    1 
ATOM   16730 N N     . LEU A 1 3824 ? 199.386 184.876 218.554 1.00 0.14  ? 3824 LEU A N     1 
ATOM   16731 C CA    . LEU A 1 3824 ? 200.032 183.784 219.267 1.00 2.93  ? 3824 LEU A CA    1 
ATOM   16732 C C     . LEU A 1 3824 ? 199.664 182.420 218.700 1.00 7.54  ? 3824 LEU A C     1 
ATOM   16733 O O     . LEU A 1 3824 ? 200.397 181.451 218.927 1.00 13.27 ? 3824 LEU A O     1 
ATOM   16734 C CB    . LEU A 1 3824 ? 199.670 183.852 220.754 1.00 6.31  ? 3824 LEU A CB    1 
ATOM   16735 C CG    . LEU A 1 3824 ? 200.294 182.857 221.733 1.00 1.41  ? 3824 LEU A CG    1 
ATOM   16736 C CD1   . LEU A 1 3824 ? 201.799 183.031 221.788 1.00 2.97  ? 3824 LEU A CD1   1 
ATOM   16737 C CD2   . LEU A 1 3824 ? 199.687 183.022 223.111 1.00 2.18  ? 3824 LEU A CD2   1 
ATOM   16738 N N     . TYR A 1 3825 ? 198.565 182.323 217.951 1.00 1.85  ? 3825 TYR A N     1 
ATOM   16739 C CA    . TYR A 1 3825 ? 198.111 181.041 217.415 1.00 0.00  ? 3825 TYR A CA    1 
ATOM   16740 C C     . TYR A 1 3825 ? 198.951 180.715 216.185 1.00 1.38  ? 3825 TYR A C     1 
ATOM   16741 O O     . TYR A 1 3825 ? 198.547 180.916 215.039 1.00 2.02  ? 3825 TYR A O     1 
ATOM   16742 C CB    . TYR A 1 3825 ? 196.625 181.080 217.084 1.00 1.71  ? 3825 TYR A CB    1 
ATOM   16743 C CG    . TYR A 1 3825 ? 195.726 181.490 218.228 1.00 0.00  ? 3825 TYR A CG    1 
ATOM   16744 C CD1   . TYR A 1 3825 ? 196.144 181.383 219.547 1.00 0.00  ? 3825 TYR A CD1   1 
ATOM   16745 C CD2   . TYR A 1 3825 ? 194.443 181.957 217.986 1.00 3.61  ? 3825 TYR A CD2   1 
ATOM   16746 C CE1   . TYR A 1 3825 ? 195.323 181.760 220.587 1.00 1.16  ? 3825 TYR A CE1   1 
ATOM   16747 C CE2   . TYR A 1 3825 ? 193.611 182.323 219.019 1.00 2.05  ? 3825 TYR A CE2   1 
ATOM   16748 C CZ    . TYR A 1 3825 ? 194.055 182.223 220.317 1.00 4.32  ? 3825 TYR A CZ    1 
ATOM   16749 O OH    . TYR A 1 3825 ? 193.224 182.593 221.346 1.00 6.32  ? 3825 TYR A OH    1 
ATOM   16750 N N     . GLN A 1 3826 ? 200.147 180.194 216.438 1.00 4.07  ? 3826 GLN A N     1 
ATOM   16751 C CA    . GLN A 1 3826 ? 201.103 179.865 215.389 1.00 2.77  ? 3826 GLN A CA    1 
ATOM   16752 C C     . GLN A 1 3826 ? 201.360 178.367 215.418 1.00 4.34  ? 3826 GLN A C     1 
ATOM   16753 O O     . GLN A 1 3826 ? 201.934 177.852 216.382 1.00 3.28  ? 3826 GLN A O     1 
ATOM   16754 C CB    . GLN A 1 3826 ? 202.409 180.637 215.579 1.00 5.51  ? 3826 GLN A CB    1 
ATOM   16755 C CG    . GLN A 1 3826 ? 202.265 182.144 215.494 1.00 5.71  ? 3826 GLN A CG    1 
ATOM   16756 C CD    . GLN A 1 3826 ? 201.860 182.617 214.119 1.00 9.38  ? 3826 GLN A CD    1 
ATOM   16757 O OE1   . GLN A 1 3826 ? 202.318 182.087 213.109 1.00 10.39 ? 3826 GLN A OE1   1 
ATOM   16758 N NE2   . GLN A 1 3826 ? 200.997 183.624 214.071 1.00 4.57  ? 3826 GLN A NE2   1 
ATOM   16759 N N     . TYR A 1 3827 ? 200.940 177.673 214.364 1.00 6.43  ? 3827 TYR A N     1 
ATOM   16760 C CA    . TYR A 1 3827 ? 201.103 176.230 214.262 1.00 0.71  ? 3827 TYR A CA    1 
ATOM   16761 C C     . TYR A 1 3827 ? 201.769 175.890 212.940 1.00 2.05  ? 3827 TYR A C     1 
ATOM   16762 O O     . TYR A 1 3827 ? 201.418 176.455 211.900 1.00 9.44  ? 3827 TYR A O     1 
ATOM   16763 C CB    . TYR A 1 3827 ? 199.759 175.509 214.378 1.00 1.07  ? 3827 TYR A CB    1 
ATOM   16764 C CG    . TYR A 1 3827 ? 198.851 176.088 215.434 1.00 5.17  ? 3827 TYR A CG    1 
ATOM   16765 C CD1   . TYR A 1 3827 ? 199.115 175.895 216.781 1.00 4.28  ? 3827 TYR A CD1   1 
ATOM   16766 C CD2   . TYR A 1 3827 ? 197.732 176.827 215.086 1.00 5.39  ? 3827 TYR A CD2   1 
ATOM   16767 C CE1   . TYR A 1 3827 ? 198.291 176.422 217.751 1.00 1.67  ? 3827 TYR A CE1   1 
ATOM   16768 C CE2   . TYR A 1 3827 ? 196.902 177.358 216.049 1.00 0.07  ? 3827 TYR A CE2   1 
ATOM   16769 C CZ    . TYR A 1 3827 ? 197.186 177.152 217.379 1.00 1.60  ? 3827 TYR A CZ    1 
ATOM   16770 O OH    . TYR A 1 3827 ? 196.364 177.677 218.345 1.00 8.68  ? 3827 TYR A OH    1 
ATOM   16771 N N     . SER A 1 3828 ? 202.722 174.969 212.985 1.00 2.42  ? 3828 SER A N     1 
ATOM   16772 C CA    . SER A 1 3828 ? 203.437 174.531 211.800 1.00 3.12  ? 3828 SER A CA    1 
ATOM   16773 C C     . SER A 1 3828 ? 202.817 173.252 211.245 1.00 8.35  ? 3828 SER A C     1 
ATOM   16774 O O     . SER A 1 3828 ? 201.967 172.616 211.872 1.00 9.90  ? 3828 SER A O     1 
ATOM   16775 C CB    . SER A 1 3828 ? 204.916 174.314 212.121 1.00 8.88  ? 3828 SER A CB    1 
ATOM   16776 O OG    . SER A 1 3828 ? 205.104 173.147 212.901 1.00 8.48  ? 3828 SER A OG    1 
ATOM   16777 N N     . LEU A 1 3829 ? 203.250 172.882 210.038 1.00 9.66  ? 3829 LEU A N     1 
ATOM   16778 C CA    . LEU A 1 3829 ? 202.801 171.626 209.449 1.00 5.94  ? 3829 LEU A CA    1 
ATOM   16779 C C     . LEU A 1 3829 ? 203.274 170.429 210.258 1.00 6.68  ? 3829 LEU A C     1 
ATOM   16780 O O     . LEU A 1 3829 ? 202.572 169.417 210.332 1.00 13.01 ? 3829 LEU A O     1 
ATOM   16781 C CB    . LEU A 1 3829 ? 203.287 171.512 208.004 1.00 6.27  ? 3829 LEU A CB    1 
ATOM   16782 C CG    . LEU A 1 3829 ? 202.694 170.373 207.171 1.00 7.06  ? 3829 LEU A CG    1 
ATOM   16783 C CD1   . LEU A 1 3829 ? 201.198 170.241 207.395 1.00 8.73  ? 3829 LEU A CD1   1 
ATOM   16784 C CD2   . LEU A 1 3829 ? 202.997 170.578 205.699 1.00 9.04  ? 3829 LEU A CD2   1 
ATOM   16785 N N     . GLN A 1 3830 ? 204.459 170.522 210.865 1.00 1.68  ? 3830 GLN A N     1 
ATOM   16786 C CA    . GLN A 1 3830 ? 204.967 169.409 211.656 1.00 3.78  ? 3830 GLN A CA    1 
ATOM   16787 C C     . GLN A 1 3830 ? 204.094 169.153 212.878 1.00 9.58  ? 3830 GLN A C     1 
ATOM   16788 O O     . GLN A 1 3830 ? 203.967 168.008 213.319 1.00 9.72  ? 3830 GLN A O     1 
ATOM   16789 C CB    . GLN A 1 3830 ? 206.415 169.683 212.073 1.00 5.43  ? 3830 GLN A CB    1 
ATOM   16790 C CG    . GLN A 1 3830 ? 207.071 168.697 213.065 1.00 6.97  ? 3830 GLN A CG    1 
ATOM   16791 C CD    . GLN A 1 3830 ? 206.808 167.210 212.798 1.00 11.86 ? 3830 GLN A CD    1 
ATOM   16792 O OE1   . GLN A 1 3830 ? 206.305 166.815 211.746 1.00 10.69 ? 3830 GLN A OE1   1 
ATOM   16793 N NE2   . GLN A 1 3830 ? 207.161 166.380 213.771 1.00 7.80  ? 3830 GLN A NE2   1 
ATOM   16794 N N     . PHE A 1 3831 ? 203.473 170.197 213.427 1.00 8.76  ? 3831 PHE A N     1 
ATOM   16795 C CA    . PHE A 1 3831 ? 202.602 170.021 214.587 1.00 5.62  ? 3831 PHE A CA    1 
ATOM   16796 C C     . PHE A 1 3831 ? 201.356 169.219 214.215 1.00 6.31  ? 3831 PHE A C     1 
ATOM   16797 O O     . PHE A 1 3831 ? 200.967 168.279 214.922 1.00 11.30 ? 3831 PHE A O     1 
ATOM   16798 C CB    . PHE A 1 3831 ? 202.247 171.397 215.158 1.00 8.42  ? 3831 PHE A CB    1 
ATOM   16799 C CG    . PHE A 1 3831 ? 201.206 171.373 216.237 1.00 8.06  ? 3831 PHE A CG    1 
ATOM   16800 C CD1   . PHE A 1 3831 ? 201.507 170.885 217.496 1.00 13.00 ? 3831 PHE A CD1   1 
ATOM   16801 C CD2   . PHE A 1 3831 ? 199.941 171.882 216.011 1.00 5.10  ? 3831 PHE A CD2   1 
ATOM   16802 C CE1   . PHE A 1 3831 ? 200.557 170.877 218.497 1.00 13.01 ? 3831 PHE A CE1   1 
ATOM   16803 C CE2   . PHE A 1 3831 ? 198.989 171.876 217.011 1.00 1.72  ? 3831 PHE A CE2   1 
ATOM   16804 C CZ    . PHE A 1 3831 ? 199.297 171.374 218.253 1.00 6.31  ? 3831 PHE A CZ    1 
ATOM   16805 N N     . PHE A 1 3832 ? 200.735 169.554 213.080 1.00 5.51  ? 3832 PHE A N     1 
ATOM   16806 C CA    . PHE A 1 3832 ? 199.619 168.753 212.588 1.00 2.83  ? 3832 PHE A CA    1 
ATOM   16807 C C     . PHE A 1 3832 ? 200.054 167.347 212.197 1.00 5.44  ? 3832 PHE A C     1 
ATOM   16808 O O     . PHE A 1 3832 ? 199.290 166.394 212.376 1.00 11.29 ? 3832 PHE A O     1 
ATOM   16809 C CB    . PHE A 1 3832 ? 198.951 169.427 211.394 1.00 1.66  ? 3832 PHE A CB    1 
ATOM   16810 C CG    . PHE A 1 3832 ? 197.805 168.640 210.832 1.00 2.50  ? 3832 PHE A CG    1 
ATOM   16811 C CD1   . PHE A 1 3832 ? 196.687 168.376 211.599 1.00 7.96  ? 3832 PHE A CD1   1 
ATOM   16812 C CD2   . PHE A 1 3832 ? 197.866 168.125 209.550 1.00 3.91  ? 3832 PHE A CD2   1 
ATOM   16813 C CE1   . PHE A 1 3832 ? 195.639 167.639 211.087 1.00 6.93  ? 3832 PHE A CE1   1 
ATOM   16814 C CE2   . PHE A 1 3832 ? 196.823 167.387 209.035 1.00 5.61  ? 3832 PHE A CE2   1 
ATOM   16815 C CZ    . PHE A 1 3832 ? 195.709 167.144 209.804 1.00 6.91  ? 3832 PHE A CZ    1 
ATOM   16816 N N     . LEU A 1 3833 ? 201.254 167.198 211.637 1.00 8.39  ? 3833 LEU A N     1 
ATOM   16817 C CA    . LEU A 1 3833 ? 201.743 165.865 211.305 1.00 7.19  ? 3833 LEU A CA    1 
ATOM   16818 C C     . LEU A 1 3833 ? 201.925 165.026 212.561 1.00 9.02  ? 3833 LEU A C     1 
ATOM   16819 O O     . LEU A 1 3833 ? 201.636 163.826 212.563 1.00 15.05 ? 3833 LEU A O     1 
ATOM   16820 C CB    . LEU A 1 3833 ? 203.050 165.962 210.521 1.00 6.13  ? 3833 LEU A CB    1 
ATOM   16821 C CG    . LEU A 1 3833 ? 202.937 166.461 209.079 1.00 2.63  ? 3833 LEU A CG    1 
ATOM   16822 C CD1   . LEU A 1 3833 ? 204.159 166.061 208.280 1.00 9.46  ? 3833 LEU A CD1   1 
ATOM   16823 C CD2   . LEU A 1 3833 ? 201.673 165.934 208.424 1.00 7.76  ? 3833 LEU A CD2   1 
ATOM   16824 N N     . ASP A 1 3834 ? 202.403 165.645 213.642 1.00 2.98  ? 3834 ASP A N     1 
ATOM   16825 C CA    . ASP A 1 3834 ? 202.491 164.955 214.923 1.00 9.21  ? 3834 ASP A CA    1 
ATOM   16826 C C     . ASP A 1 3834 ? 201.110 164.562 215.430 1.00 11.50 ? 3834 ASP A C     1 
ATOM   16827 O O     . ASP A 1 3834 ? 200.926 163.457 215.950 1.00 13.49 ? 3834 ASP A O     1 
ATOM   16828 C CB    . ASP A 1 3834 ? 203.208 165.835 215.943 1.00 9.92  ? 3834 ASP A CB    1 
ATOM   16829 C CG    . ASP A 1 3834 ? 204.708 165.852 215.743 1.00 13.99 ? 3834 ASP A CG    1 
ATOM   16830 O OD1   . ASP A 1 3834 ? 205.260 164.824 215.297 1.00 21.27 ? 3834 ASP A OD1   1 
ATOM   16831 O OD2   . ASP A 1 3834 ? 205.338 166.890 216.034 1.00 9.46  ? 3834 ASP A OD2   1 
ATOM   16832 N N     . ILE A 1 3835 ? 200.126 165.451 215.284 1.00 10.44 ? 3835 ILE A N     1 
ATOM   16833 C CA    . ILE A 1 3835 ? 198.761 165.121 215.696 1.00 3.96  ? 3835 ILE A CA    1 
ATOM   16834 C C     . ILE A 1 3835 ? 198.240 163.919 214.914 1.00 8.16  ? 3835 ILE A C     1 
ATOM   16835 O O     . ILE A 1 3835 ? 197.634 162.997 215.480 1.00 16.66 ? 3835 ILE A O     1 
ATOM   16836 C CB    . ILE A 1 3835 ? 197.842 166.343 215.521 1.00 3.70  ? 3835 ILE A CB    1 
ATOM   16837 C CG1   . ILE A 1 3835 ? 198.181 167.422 216.547 1.00 10.08 ? 3835 ILE A CG1   1 
ATOM   16838 C CG2   . ILE A 1 3835 ? 196.382 165.938 215.633 1.00 4.06  ? 3835 ILE A CG2   1 
ATOM   16839 C CD1   . ILE A 1 3835 ? 197.419 168.706 216.347 1.00 7.36  ? 3835 ILE A CD1   1 
ATOM   16840 N N     . TYR A 1 3836 ? 198.463 163.917 213.600 1.00 3.64  ? 3836 TYR A N     1 
ATOM   16841 C CA    . TYR A 1 3836 ? 197.981 162.832 212.751 1.00 3.25  ? 3836 TYR A CA    1 
ATOM   16842 C C     . TYR A 1 3836 ? 198.695 161.522 213.063 1.00 8.74  ? 3836 TYR A C     1 
ATOM   16843 O O     . TYR A 1 3836 ? 198.065 160.460 213.128 1.00 13.60 ? 3836 TYR A O     1 
ATOM   16844 C CB    . TYR A 1 3836 ? 198.156 163.227 211.284 1.00 6.84  ? 3836 TYR A CB    1 
ATOM   16845 C CG    . TYR A 1 3836 ? 197.415 162.362 210.294 1.00 9.74  ? 3836 TYR A CG    1 
ATOM   16846 C CD1   . TYR A 1 3836 ? 196.037 162.227 210.356 1.00 6.08  ? 3836 TYR A CD1   1 
ATOM   16847 C CD2   . TYR A 1 3836 ? 198.089 161.720 209.266 1.00 14.35 ? 3836 TYR A CD2   1 
ATOM   16848 C CE1   . TYR A 1 3836 ? 195.359 161.443 209.450 1.00 7.61  ? 3836 TYR A CE1   1 
ATOM   16849 C CE2   . TYR A 1 3836 ? 197.416 160.943 208.349 1.00 9.96  ? 3836 TYR A CE2   1 
ATOM   16850 C CZ    . TYR A 1 3836 ? 196.051 160.809 208.446 1.00 7.59  ? 3836 TYR A CZ    1 
ATOM   16851 O OH    . TYR A 1 3836 ? 195.373 160.034 207.536 1.00 12.30 ? 3836 TYR A OH    1 
ATOM   16852 N N     . HIS A 1 3837 ? 200.008 161.575 213.281 1.00 7.88  ? 3837 HIS A N     1 
ATOM   16853 C CA    . HIS A 1 3837 ? 200.740 160.364 213.627 1.00 4.96  ? 3837 HIS A CA    1 
ATOM   16854 C C     . HIS A 1 3837 ? 200.316 159.850 214.995 1.00 6.49  ? 3837 HIS A C     1 
ATOM   16855 O O     . HIS A 1 3837 ? 200.320 158.638 215.241 1.00 19.06 ? 3837 HIS A O     1 
ATOM   16856 C CB    . HIS A 1 3837 ? 202.241 160.636 213.589 1.00 8.30  ? 3837 HIS A CB    1 
ATOM   16857 C CG    . HIS A 1 3837 ? 202.777 160.844 212.208 1.00 13.57 ? 3837 HIS A CG    1 
ATOM   16858 N ND1   . HIS A 1 3837 ? 203.743 161.782 211.918 1.00 11.43 ? 3837 HIS A ND1   1 
ATOM   16859 C CD2   . HIS A 1 3837 ? 202.462 160.253 211.031 1.00 11.42 ? 3837 HIS A CD2   1 
ATOM   16860 C CE1   . HIS A 1 3837 ? 204.012 161.749 210.626 1.00 10.63 ? 3837 HIS A CE1   1 
ATOM   16861 N NE2   . HIS A 1 3837 ? 203.247 160.831 210.064 1.00 15.07 ? 3837 HIS A NE2   1 
ATOM   16862 N N     . ASN A 1 3838 ? 199.942 160.758 215.899 1.00 6.16  ? 3838 ASN A N     1 
ATOM   16863 C CA    . ASN A 1 3838 ? 199.433 160.348 217.201 1.00 7.07  ? 3838 ASN A CA    1 
ATOM   16864 C C     . ASN A 1 3838 ? 198.088 159.648 217.075 1.00 5.12  ? 3838 ASN A C     1 
ATOM   16865 O O     . ASN A 1 3838 ? 197.856 158.619 217.718 1.00 11.09 ? 3838 ASN A O     1 
ATOM   16866 C CB    . ASN A 1 3838 ? 199.330 161.562 218.125 1.00 8.71  ? 3838 ASN A CB    1 
ATOM   16867 C CG    . ASN A 1 3838 ? 199.049 161.180 219.565 1.00 10.15 ? 3838 ASN A CG    1 
ATOM   16868 O OD1   . ASN A 1 3838 ? 197.986 160.647 219.884 1.00 12.57 ? 3838 ASN A OD1   1 
ATOM   16869 N ND2   . ASN A 1 3838 ? 200.010 161.441 220.442 1.00 10.92 ? 3838 ASN A ND2   1 
ATOM   16870 N N     . VAL A 1 3839 ? 197.184 160.192 216.258 1.00 5.43  ? 3839 VAL A N     1 
ATOM   16871 C CA    . VAL A 1 3839 ? 195.886 159.547 216.105 1.00 10.63 ? 3839 VAL A CA    1 
ATOM   16872 C C     . VAL A 1 3839 ? 196.002 158.256 215.300 1.00 9.04  ? 3839 VAL A C     1 
ATOM   16873 O O     . VAL A 1 3839 ? 195.112 157.401 215.375 1.00 12.73 ? 3839 VAL A O     1 
ATOM   16874 C CB    . VAL A 1 3839 ? 194.856 160.511 215.478 1.00 10.42 ? 3839 VAL A CB    1 
ATOM   16875 C CG1   . VAL A 1 3839 ? 195.175 160.794 214.027 1.00 8.44  ? 3839 VAL A CG1   1 
ATOM   16876 C CG2   . VAL A 1 3839 ? 193.447 159.961 215.620 1.00 9.30  ? 3839 VAL A CG2   1 
ATOM   16877 N N     . LEU A 1 3840 ? 197.084 158.072 214.543 1.00 7.01  ? 3840 LEU A N     1 
ATOM   16878 C CA    . LEU A 1 3840 ? 197.227 156.841 213.769 1.00 8.31  ? 3840 LEU A CA    1 
ATOM   16879 C C     . LEU A 1 3840 ? 197.960 155.734 214.529 1.00 11.81 ? 3840 LEU A C     1 
ATOM   16880 O O     . LEU A 1 3840 ? 197.401 154.657 214.754 1.00 15.26 ? 3840 LEU A O     1 
ATOM   16881 C CB    . LEU A 1 3840 ? 197.947 157.129 212.448 1.00 8.26  ? 3840 LEU A CB    1 
ATOM   16882 C CG    . LEU A 1 3840 ? 197.188 157.932 211.395 1.00 9.21  ? 3840 LEU A CG    1 
ATOM   16883 C CD1   . LEU A 1 3840 ? 198.020 158.029 210.137 1.00 5.36  ? 3840 LEU A CD1   1 
ATOM   16884 C CD2   . LEU A 1 3840 ? 195.843 157.293 211.101 1.00 12.16 ? 3840 LEU A CD2   1 
ATOM   16885 N N     . TYR A 1 3841 ? 199.206 155.980 214.931 1.00 6.38  ? 3841 TYR A N     1 
ATOM   16886 C CA    . TYR A 1 3841 ? 200.098 154.898 215.333 1.00 7.00  ? 3841 TYR A CA    1 
ATOM   16887 C C     . TYR A 1 3841 ? 200.225 154.706 216.840 1.00 12.15 ? 3841 TYR A C     1 
ATOM   16888 O O     . TYR A 1 3841 ? 200.911 153.771 217.266 1.00 19.82 ? 3841 TYR A O     1 
ATOM   16889 C CB    . TYR A 1 3841 ? 201.487 155.114 214.724 1.00 11.64 ? 3841 TYR A CB    1 
ATOM   16890 C CG    . TYR A 1 3841 ? 201.474 155.195 213.215 1.00 13.98 ? 3841 TYR A CG    1 
ATOM   16891 C CD1   . TYR A 1 3841 ? 201.399 154.044 212.442 1.00 12.44 ? 3841 TYR A CD1   1 
ATOM   16892 C CD2   . TYR A 1 3841 ? 201.531 156.418 212.563 1.00 12.91 ? 3841 TYR A CD2   1 
ATOM   16893 C CE1   . TYR A 1 3841 ? 201.383 154.108 211.065 1.00 10.03 ? 3841 TYR A CE1   1 
ATOM   16894 C CE2   . TYR A 1 3841 ? 201.517 156.491 211.184 1.00 16.48 ? 3841 TYR A CE2   1 
ATOM   16895 C CZ    . TYR A 1 3841 ? 201.442 155.333 210.440 1.00 17.07 ? 3841 TYR A CZ    1 
ATOM   16896 O OH    . TYR A 1 3841 ? 201.428 155.397 209.066 1.00 17.31 ? 3841 TYR A OH    1 
ATOM   16897 N N     . GLU A 1 3842 ? 199.603 155.552 217.661 1.00 9.31  ? 3842 GLU A N     1 
ATOM   16898 C CA    . GLU A 1 3842 ? 199.616 155.303 219.098 1.00 15.56 ? 3842 GLU A CA    1 
ATOM   16899 C C     . GLU A 1 3842 ? 198.293 155.619 219.790 1.00 13.32 ? 3842 GLU A C     1 
ATOM   16900 O O     . GLU A 1 3842 ? 198.303 156.033 220.956 1.00 14.47 ? 3842 GLU A O     1 
ATOM   16901 C CB    . GLU A 1 3842 ? 200.789 156.049 219.771 1.00 14.02 ? 3842 GLU A CB    1 
ATOM   16902 C CG    . GLU A 1 3842 ? 200.665 157.555 219.897 1.00 12.82 ? 3842 GLU A CG    1 
ATOM   16903 C CD    . GLU A 1 3842 ? 201.455 158.279 218.826 1.00 14.97 ? 3842 GLU A CD    1 
ATOM   16904 O OE1   . GLU A 1 3842 ? 201.584 157.734 217.710 1.00 14.06 ? 3842 GLU A OE1   1 
ATOM   16905 O OE2   . GLU A 1 3842 ? 201.954 159.390 219.102 1.00 14.96 ? 3842 GLU A OE2   1 
ATOM   16906 N N     . ASN A 1 3843 ? 197.163 155.405 219.134 1.00 12.26 ? 3843 ASN A N     1 
ATOM   16907 C CA    . ASN A 1 3843 ? 195.876 155.609 219.787 1.00 15.36 ? 3843 ASN A CA    1 
ATOM   16908 C C     . ASN A 1 3843 ? 195.632 154.548 220.853 1.00 21.90 ? 3843 ASN A C     1 
ATOM   16909 O O     . ASN A 1 3843 ? 195.785 153.352 220.578 1.00 24.93 ? 3843 ASN A O     1 
ATOM   16910 C CB    . ASN A 1 3843 ? 194.743 155.564 218.775 1.00 15.99 ? 3843 ASN A CB    1 
ATOM   16911 C CG    . ASN A 1 3843 ? 194.318 156.929 218.328 1.00 17.55 ? 3843 ASN A CG    1 
ATOM   16912 O OD1   . ASN A 1 3843 ? 194.441 157.898 219.072 1.00 24.31 ? 3843 ASN A OD1   1 
ATOM   16913 N ND2   . ASN A 1 3843 ? 193.775 157.015 217.123 1.00 12.90 ? 3843 ASN A ND2   1 
ATOM   16914 N N     . PRO A 1 3844 ? 195.235 154.937 222.069 1.00 21.06 ? 3844 PRO A N     1 
ATOM   16915 C CA    . PRO A 1 3844 ? 194.753 153.939 223.032 1.00 19.99 ? 3844 PRO A CA    1 
ATOM   16916 C C     . PRO A 1 3844 ? 193.417 153.329 222.650 1.00 21.18 ? 3844 PRO A C     1 
ATOM   16917 O O     . PRO A 1 3844 ? 193.064 152.271 223.186 1.00 21.33 ? 3844 PRO A O     1 
ATOM   16918 C CB    . PRO A 1 3844 ? 194.629 154.742 224.333 1.00 23.28 ? 3844 PRO A CB    1 
ATOM   16919 C CG    . PRO A 1 3844 ? 195.581 155.875 224.166 1.00 23.59 ? 3844 PRO A CG    1 
ATOM   16920 C CD    . PRO A 1 3844 ? 195.521 156.230 222.711 1.00 21.64 ? 3844 PRO A CD    1 
ATOM   16921 N N     . ASN A 1 3845 ? 192.666 153.960 221.745 1.00 25.89 ? 3845 ASN A N     1 
ATOM   16922 C CA    . ASN A 1 3845 ? 191.349 153.466 221.367 1.00 24.75 ? 3845 ASN A CA    1 
ATOM   16923 C C     . ASN A 1 3845 ? 191.393 152.475 220.213 1.00 25.21 ? 3845 ASN A C     1 
ATOM   16924 O O     . ASN A 1 3845 ? 190.367 151.857 219.909 1.00 25.93 ? 3845 ASN A O     1 
ATOM   16925 C CB    . ASN A 1 3845 ? 190.438 154.637 220.994 1.00 25.41 ? 3845 ASN A CB    1 
ATOM   16926 C CG    . ASN A 1 3845 ? 190.179 155.569 222.161 1.00 27.80 ? 3845 ASN A CG    1 
ATOM   16927 O OD1   . ASN A 1 3845 ? 190.589 156.729 222.146 1.00 26.01 ? 3845 ASN A OD1   1 
ATOM   16928 N ND2   . ASN A 1 3845 ? 189.485 155.067 223.175 1.00 30.15 ? 3845 ASN A ND2   1 
ATOM   16929 N N     . LEU A 1 3846 ? 192.542 152.317 219.563 1.00 25.41 ? 3846 LEU A N     1 
ATOM   16930 C CA    . LEU A 1 3846 ? 192.676 151.418 218.425 1.00 25.81 ? 3846 LEU A CA    1 
ATOM   16931 C C     . LEU A 1 3846 ? 193.383 150.112 218.767 1.00 28.43 ? 3846 LEU A C     1 
ATOM   16932 O O     . LEU A 1 3846 ? 193.638 149.313 217.860 1.00 25.47 ? 3846 LEU A O     1 
ATOM   16933 C CB    . LEU A 1 3846 ? 193.422 152.115 217.278 1.00 23.11 ? 3846 LEU A CB    1 
ATOM   16934 C CG    . LEU A 1 3846 ? 192.639 153.019 216.319 1.00 22.37 ? 3846 LEU A CG    1 
ATOM   16935 C CD1   . LEU A 1 3846 ? 191.613 152.211 215.556 1.00 21.55 ? 3846 LEU A CD1   1 
ATOM   16936 C CD2   . LEU A 1 3846 ? 191.967 154.180 217.025 1.00 29.13 ? 3846 LEU A CD2   1 
ATOM   16937 N N     . LYS A 1 3847 ? 193.713 149.875 220.039 1.00 27.95 ? 3847 LYS A N     1 
ATOM   16938 C CA    . LYS A 1 3847 ? 194.396 148.635 220.397 1.00 28.58 ? 3847 LYS A CA    1 
ATOM   16939 C C     . LYS A 1 3847 ? 193.502 147.417 220.189 1.00 28.96 ? 3847 LYS A C     1 
ATOM   16940 O O     . LYS A 1 3847 ? 193.970 146.373 219.721 1.00 31.42 ? 3847 LYS A O     1 
ATOM   16941 C CB    . LYS A 1 3847 ? 194.887 148.689 221.844 1.00 26.11 ? 3847 LYS A CB    1 
ATOM   16942 C CG    . LYS A 1 3847 ? 195.375 150.048 222.312 1.00 27.91 ? 3847 LYS A CG    1 
ATOM   16943 C CD    . LYS A 1 3847 ? 196.892 150.132 222.218 1.00 27.98 ? 3847 LYS A CD    1 
ATOM   16944 C CE    . LYS A 1 3847 ? 197.411 151.473 222.710 1.00 28.68 ? 3847 LYS A CE    1 
ATOM   16945 N NZ    . LYS A 1 3847 ? 197.319 151.586 224.194 1.00 26.17 ? 3847 LYS A NZ    1 
ATOM   16946 N N     . GLY A 1 3848 ? 192.221 147.527 220.525 1.00 28.52 ? 3848 GLY A N     1 
ATOM   16947 C CA    . GLY A 1 3848 ? 191.348 146.370 220.492 1.00 31.22 ? 3848 GLY A CA    1 
ATOM   16948 C C     . GLY A 1 3848 ? 190.554 146.200 219.213 1.00 29.79 ? 3848 GLY A C     1 
ATOM   16949 O O     . GLY A 1 3848 ? 190.408 145.081 218.714 1.00 28.88 ? 3848 GLY A O     1 
ATOM   16950 N N     . VAL A 1 3849 ? 190.036 147.302 218.671 1.00 25.58 ? 3849 VAL A N     1 
ATOM   16951 C CA    . VAL A 1 3849 ? 189.137 147.218 217.528 1.00 28.19 ? 3849 VAL A CA    1 
ATOM   16952 C C     . VAL A 1 3849 ? 189.927 146.896 216.266 1.00 29.58 ? 3849 VAL A C     1 
ATOM   16953 O O     . VAL A 1 3849 ? 190.929 147.553 215.949 1.00 30.29 ? 3849 VAL A O     1 
ATOM   16954 C CB    . VAL A 1 3849 ? 188.344 148.528 217.378 1.00 29.59 ? 3849 VAL A CB    1 
ATOM   16955 C CG1   . VAL A 1 3849 ? 187.813 148.676 215.964 1.00 26.69 ? 3849 VAL A CG1   1 
ATOM   16956 C CG2   . VAL A 1 3849 ? 187.206 148.572 218.385 1.00 26.65 ? 3849 VAL A CG2   1 
ATOM   16957 N N     . THR A 1 3850 ? 189.474 145.876 215.534 1.00 29.25 ? 3850 THR A N     1 
ATOM   16958 C CA    . THR A 1 3850 ? 190.120 145.457 214.296 1.00 28.99 ? 3850 THR A CA    1 
ATOM   16959 C C     . THR A 1 3850 ? 189.254 145.614 213.056 1.00 28.58 ? 3850 THR A C     1 
ATOM   16960 O O     . THR A 1 3850 ? 189.803 145.592 211.947 1.00 27.80 ? 3850 THR A O     1 
ATOM   16961 C CB    . THR A 1 3850 ? 190.573 143.991 214.388 1.00 32.20 ? 3850 THR A CB    1 
ATOM   16962 O OG1   . THR A 1 3850 ? 189.424 143.135 214.427 1.00 30.53 ? 3850 THR A OG1   1 
ATOM   16963 C CG2   . THR A 1 3850 ? 191.412 143.765 215.636 1.00 31.58 ? 3850 THR A CG2   1 
ATOM   16964 N N     . ASP A 1 3851 ? 187.937 145.757 213.191 1.00 27.90 ? 3851 ASP A N     1 
ATOM   16965 C CA    . ASP A 1 3851 ? 187.084 145.957 212.026 1.00 27.04 ? 3851 ASP A CA    1 
ATOM   16966 C C     . ASP A 1 3851 ? 187.363 147.320 211.407 1.00 26.55 ? 3851 ASP A C     1 
ATOM   16967 O O     . ASP A 1 3851 ? 187.552 148.311 212.117 1.00 34.03 ? 3851 ASP A O     1 
ATOM   16968 C CB    . ASP A 1 3851 ? 185.612 145.839 212.419 1.00 28.59 ? 3851 ASP A CB    1 
ATOM   16969 C CG    . ASP A 1 3851 ? 184.685 145.826 211.216 1.00 32.38 ? 3851 ASP A CG    1 
ATOM   16970 O OD1   . ASP A 1 3851 ? 185.175 145.938 210.073 1.00 30.82 ? 3851 ASP A OD1   1 
ATOM   16971 O OD2   . ASP A 1 3851 ? 183.459 145.696 211.414 1.00 32.33 ? 3851 ASP A OD2   1 
ATOM   16972 N N     . HIS A 1 3852 ? 187.373 147.369 210.074 1.00 24.56 ? 3852 HIS A N     1 
ATOM   16973 C CA    . HIS A 1 3852 ? 187.846 148.563 209.382 1.00 26.70 ? 3852 HIS A CA    1 
ATOM   16974 C C     . HIS A 1 3852 ? 186.837 149.703 209.462 1.00 26.60 ? 3852 HIS A C     1 
ATOM   16975 O O     . HIS A 1 3852 ? 187.216 150.861 209.676 1.00 27.84 ? 3852 HIS A O     1 
ATOM   16976 C CB    . HIS A 1 3852 ? 188.158 148.229 207.924 1.00 31.02 ? 3852 HIS A CB    1 
ATOM   16977 C CG    . HIS A 1 3852 ? 189.266 147.236 207.758 1.00 30.27 ? 3852 HIS A CG    1 
ATOM   16978 N ND1   . HIS A 1 3852 ? 190.593 147.602 207.705 1.00 27.44 ? 3852 HIS A ND1   1 
ATOM   16979 C CD2   . HIS A 1 3852 ? 189.242 145.889 207.625 1.00 26.41 ? 3852 HIS A CD2   1 
ATOM   16980 C CE1   . HIS A 1 3852 ? 191.340 146.524 207.553 1.00 27.21 ? 3852 HIS A CE1   1 
ATOM   16981 N NE2   . HIS A 1 3852 ? 190.545 145.471 207.501 1.00 25.31 ? 3852 HIS A NE2   1 
ATOM   16982 N N     . THR A 1 3853 ? 185.548 149.402 209.284 1.00 27.50 ? 3853 THR A N     1 
ATOM   16983 C CA    . THR A 1 3853 ? 184.549 150.467 209.253 1.00 27.15 ? 3853 THR A CA    1 
ATOM   16984 C C     . THR A 1 3853 ? 184.386 151.118 210.622 1.00 24.92 ? 3853 THR A C     1 
ATOM   16985 O O     . THR A 1 3853 ? 184.091 152.315 210.713 1.00 25.83 ? 3853 THR A O     1 
ATOM   16986 C CB    . THR A 1 3853 ? 183.212 149.928 208.735 1.00 28.78 ? 3853 THR A CB    1 
ATOM   16987 O OG1   . THR A 1 3853 ? 182.296 151.015 208.550 1.00 27.19 ? 3853 THR A OG1   1 
ATOM   16988 C CG2   . THR A 1 3853 ? 182.611 148.910 209.697 1.00 27.96 ? 3853 THR A CG2   1 
ATOM   16989 N N     . GLN A 1 3854 ? 184.571 150.351 211.698 1.00 20.94 ? 3854 GLN A N     1 
ATOM   16990 C CA    . GLN A 1 3854 ? 184.586 150.942 213.030 1.00 22.84 ? 3854 GLN A CA    1 
ATOM   16991 C C     . GLN A 1 3854 ? 185.905 151.652 213.301 1.00 21.76 ? 3854 GLN A C     1 
ATOM   16992 O O     . GLN A 1 3854 ? 185.928 152.700 213.957 1.00 26.99 ? 3854 GLN A O     1 
ATOM   16993 C CB    . GLN A 1 3854 ? 184.329 149.867 214.086 1.00 23.96 ? 3854 GLN A CB    1 
ATOM   16994 C CG    . GLN A 1 3854 ? 182.867 149.708 214.462 1.00 24.94 ? 3854 GLN A CG    1 
ATOM   16995 C CD    . GLN A 1 3854 ? 182.109 148.833 213.484 1.00 28.86 ? 3854 GLN A CD    1 
ATOM   16996 O OE1   . GLN A 1 3854 ? 182.686 147.955 212.843 1.00 29.75 ? 3854 GLN A OE1   1 
ATOM   16997 N NE2   . GLN A 1 3854 ? 180.809 149.071 213.361 1.00 29.28 ? 3854 GLN A NE2   1 
ATOM   16998 N N     . ARG A 1 3855 ? 187.008 151.092 212.798 1.00 18.86 ? 3855 ARG A N     1 
ATOM   16999 C CA    . ARG A 1 3855 ? 188.315 151.704 213.006 1.00 19.51 ? 3855 ARG A CA    1 
ATOM   17000 C C     . ARG A 1 3855 ? 188.369 153.096 212.394 1.00 16.30 ? 3855 ARG A C     1 
ATOM   17001 O O     . ARG A 1 3855 ? 188.950 154.015 212.979 1.00 16.77 ? 3855 ARG A O     1 
ATOM   17002 C CB    . ARG A 1 3855 ? 189.409 150.815 212.415 1.00 22.22 ? 3855 ARG A CB    1 
ATOM   17003 C CG    . ARG A 1 3855 ? 190.059 149.885 213.423 1.00 20.03 ? 3855 ARG A CG    1 
ATOM   17004 C CD    . ARG A 1 3855 ? 191.156 149.047 212.796 1.00 19.24 ? 3855 ARG A CD    1 
ATOM   17005 N NE    . ARG A 1 3855 ? 192.454 149.703 212.886 1.00 18.66 ? 3855 ARG A NE    1 
ATOM   17006 C CZ    . ARG A 1 3855 ? 193.302 149.545 213.893 1.00 21.39 ? 3855 ARG A CZ    1 
ATOM   17007 N NH1   . ARG A 1 3855 ? 193.014 148.766 214.922 1.00 23.38 ? 3855 ARG A NH1   1 
ATOM   17008 N NH2   . ARG A 1 3855 ? 194.467 150.184 213.867 1.00 20.96 ? 3855 ARG A NH2   1 
ATOM   17009 N N     . LEU A 1 3856 ? 187.770 153.271 211.215 1.00 15.19 ? 3856 LEU A N     1 
ATOM   17010 C CA    . LEU A 1 3856 ? 187.734 154.591 210.593 1.00 15.10 ? 3856 LEU A CA    1 
ATOM   17011 C C     . LEU A 1 3856 ? 186.941 155.587 211.432 1.00 17.70 ? 3856 LEU A C     1 
ATOM   17012 O O     . LEU A 1 3856 ? 187.339 156.750 211.565 1.00 18.41 ? 3856 LEU A O     1 
ATOM   17013 C CB    . LEU A 1 3856 ? 187.152 154.497 209.184 1.00 17.22 ? 3856 LEU A CB    1 
ATOM   17014 C CG    . LEU A 1 3856 ? 187.066 155.832 208.445 1.00 18.14 ? 3856 LEU A CG    1 
ATOM   17015 C CD1   . LEU A 1 3856 ? 188.446 156.307 208.038 1.00 13.67 ? 3856 LEU A CD1   1 
ATOM   17016 C CD2   . LEU A 1 3856 ? 186.160 155.707 207.232 1.00 16.37 ? 3856 LEU A CD2   1 
ATOM   17017 N N     . SER A 1 3857 ? 185.811 155.156 211.996 1.00 17.19 ? 3857 SER A N     1 
ATOM   17018 C CA    . SER A 1 3857 ? 185.035 156.049 212.849 1.00 12.30 ? 3857 SER A CA    1 
ATOM   17019 C C     . SER A 1 3857 ? 185.834 156.465 214.076 1.00 12.63 ? 3857 SER A C     1 
ATOM   17020 O O     . SER A 1 3857 ? 185.845 157.647 214.449 1.00 17.16 ? 3857 SER A O     1 
ATOM   17021 C CB    . SER A 1 3857 ? 183.724 155.381 213.259 1.00 13.99 ? 3857 SER A CB    1 
ATOM   17022 O OG    . SER A 1 3857 ? 182.914 155.111 212.129 1.00 20.54 ? 3857 SER A OG    1 
ATOM   17023 N N     . ILE A 1 3858 ? 186.523 155.510 214.708 1.00 12.47 ? 3858 ILE A N     1 
ATOM   17024 C CA    . ILE A 1 3858 ? 187.350 155.847 215.867 1.00 10.30 ? 3858 ILE A CA    1 
ATOM   17025 C C     . ILE A 1 3858 ? 188.465 156.807 215.476 1.00 9.27  ? 3858 ILE A C     1 
ATOM   17026 O O     . ILE A 1 3858 ? 188.744 157.776 216.192 1.00 20.31 ? 3858 ILE A O     1 
ATOM   17027 C CB    . ILE A 1 3858 ? 187.906 154.580 216.544 1.00 9.14  ? 3858 ILE A CB    1 
ATOM   17028 C CG1   . ILE A 1 3858 ? 186.830 153.502 216.651 1.00 15.53 ? 3858 ILE A CG1   1 
ATOM   17029 C CG2   . ILE A 1 3858 ? 188.472 154.911 217.910 1.00 12.87 ? 3858 ILE A CG2   1 
ATOM   17030 C CD1   . ILE A 1 3858 ? 187.337 152.183 217.180 1.00 16.66 ? 3858 ILE A CD1   1 
ATOM   17031 N N     . ILE A 1 3859 ? 189.120 156.560 214.339 1.00 10.79 ? 3859 ILE A N     1 
ATOM   17032 C CA    . ILE A 1 3859 ? 190.222 157.426 213.927 1.00 9.76  ? 3859 ILE A CA    1 
ATOM   17033 C C     . ILE A 1 3859 ? 189.727 158.839 213.655 1.00 7.27  ? 3859 ILE A C     1 
ATOM   17034 O O     . ILE A 1 3859 ? 190.345 159.813 214.090 1.00 14.83 ? 3859 ILE A O     1 
ATOM   17035 C CB    . ILE A 1 3859 ? 190.958 156.834 212.712 1.00 10.31 ? 3859 ILE A CB    1 
ATOM   17036 C CG1   . ILE A 1 3859 ? 191.622 155.511 213.089 1.00 13.75 ? 3859 ILE A CG1   1 
ATOM   17037 C CG2   . ILE A 1 3859 ? 191.996 157.809 212.184 1.00 12.95 ? 3859 ILE A CG2   1 
ATOM   17038 C CD1   . ILE A 1 3859 ? 192.145 154.742 211.912 1.00 15.38 ? 3859 ILE A CD1   1 
ATOM   17039 N N     . THR A 1 3860 ? 188.601 158.978 212.954 1.00 8.56  ? 3860 THR A N     1 
ATOM   17040 C CA    . THR A 1 3860 ? 188.080 160.311 212.657 1.00 7.44  ? 3860 THR A CA    1 
ATOM   17041 C C     . THR A 1 3860 ? 187.686 161.048 213.935 1.00 8.23  ? 3860 THR A C     1 
ATOM   17042 O O     . THR A 1 3860 ? 188.064 162.213 214.140 1.00 11.43 ? 3860 THR A O     1 
ATOM   17043 C CB    . THR A 1 3860 ? 186.887 160.203 211.705 1.00 8.84  ? 3860 THR A CB    1 
ATOM   17044 O OG1   . THR A 1 3860 ? 187.280 159.497 210.522 1.00 7.13  ? 3860 THR A OG1   1 
ATOM   17045 C CG2   . THR A 1 3860 ? 186.390 161.584 211.313 1.00 7.93  ? 3860 THR A CG2   1 
ATOM   17046 N N     . LYS A 1 3861 ? 186.928 160.378 214.812 1.00 5.40  ? 3861 LYS A N     1 
ATOM   17047 C CA    . LYS A 1 3861 ? 186.506 161.007 216.060 1.00 8.55  ? 3861 LYS A CA    1 
ATOM   17048 C C     . LYS A 1 3861 ? 187.702 161.441 216.898 1.00 8.42  ? 3861 LYS A C     1 
ATOM   17049 O O     . LYS A 1 3861 ? 187.764 162.589 217.362 1.00 8.37  ? 3861 LYS A O     1 
ATOM   17050 C CB    . LYS A 1 3861 ? 185.617 160.046 216.850 1.00 7.07  ? 3861 LYS A CB    1 
ATOM   17051 C CG    . LYS A 1 3861 ? 185.060 160.628 218.138 1.00 9.03  ? 3861 LYS A CG    1 
ATOM   17052 C CD    . LYS A 1 3861 ? 183.743 159.981 218.536 1.00 8.60  ? 3861 LYS A CD    1 
ATOM   17053 C CE    . LYS A 1 3861 ? 182.627 160.367 217.582 1.00 12.88 ? 3861 LYS A CE    1 
ATOM   17054 N NZ    . LYS A 1 3861 ? 181.974 161.636 218.004 1.00 14.17 ? 3861 LYS A NZ    1 
ATOM   17055 N N     . ASP A 1 3862 ? 188.673 160.545 217.088 1.00 8.81  ? 3862 ASP A N     1 
ATOM   17056 C CA    . ASP A 1 3862 ? 189.806 160.880 217.936 1.00 7.26  ? 3862 ASP A CA    1 
ATOM   17057 C C     . ASP A 1 3862 ? 190.711 161.906 217.274 1.00 7.33  ? 3862 ASP A C     1 
ATOM   17058 O O     . ASP A 1 3862 ? 191.376 162.679 217.963 1.00 11.76 ? 3862 ASP A O     1 
ATOM   17059 C CB    . ASP A 1 3862 ? 190.604 159.632 218.295 1.00 7.85  ? 3862 ASP A CB    1 
ATOM   17060 C CG    . ASP A 1 3862 ? 191.707 159.926 219.288 1.00 15.58 ? 3862 ASP A CG    1 
ATOM   17061 O OD1   . ASP A 1 3862 ? 191.401 160.131 220.482 1.00 15.53 ? 3862 ASP A OD1   1 
ATOM   17062 O OD2   . ASP A 1 3862 ? 192.876 160.002 218.865 1.00 18.38 ? 3862 ASP A OD2   1 
ATOM   17063 N N     . LEU A 1 3863 ? 190.766 161.930 215.943 1.00 3.87  ? 3863 LEU A N     1 
ATOM   17064 C CA    . LEU A 1 3863 ? 191.541 162.965 215.271 1.00 5.02  ? 3863 LEU A CA    1 
ATOM   17065 C C     . LEU A 1 3863 ? 190.947 164.334 215.548 1.00 4.54  ? 3863 LEU A C     1 
ATOM   17066 O O     . LEU A 1 3863 ? 191.667 165.283 215.880 1.00 11.78 ? 3863 LEU A O     1 
ATOM   17067 C CB    . LEU A 1 3863 ? 191.595 162.700 213.769 1.00 14.27 ? 3863 LEU A CB    1 
ATOM   17068 C CG    . LEU A 1 3863 ? 191.986 163.926 212.941 1.00 5.13  ? 3863 LEU A CG    1 
ATOM   17069 C CD1   . LEU A 1 3863 ? 193.489 164.174 213.005 1.00 4.00  ? 3863 LEU A CD1   1 
ATOM   17070 C CD2   . LEU A 1 3863 ? 191.512 163.791 211.512 1.00 3.43  ? 3863 LEU A CD2   1 
ATOM   17071 N N     . PHE A 1 3864 ? 189.623 164.447 215.429 1.00 6.39  ? 3864 PHE A N     1 
ATOM   17072 C CA    . PHE A 1 3864 ? 188.956 165.697 215.773 1.00 2.20  ? 3864 PHE A CA    1 
ATOM   17073 C C     . PHE A 1 3864 ? 189.252 166.087 217.218 1.00 5.31  ? 3864 PHE A C     1 
ATOM   17074 O O     . PHE A 1 3864 ? 189.619 167.235 217.509 1.00 9.88  ? 3864 PHE A O     1 
ATOM   17075 C CB    . PHE A 1 3864 ? 187.453 165.545 215.548 1.00 6.21  ? 3864 PHE A CB    1 
ATOM   17076 C CG    . PHE A 1 3864 ? 187.001 165.962 214.181 1.00 7.78  ? 3864 PHE A CG    1 
ATOM   17077 C CD1   . PHE A 1 3864 ? 187.232 167.242 213.716 1.00 6.51  ? 3864 PHE A CD1   1 
ATOM   17078 C CD2   . PHE A 1 3864 ? 186.373 165.055 213.346 1.00 7.59  ? 3864 PHE A CD2   1 
ATOM   17079 C CE1   . PHE A 1 3864 ? 186.819 167.616 212.455 1.00 3.77  ? 3864 PHE A CE1   1 
ATOM   17080 C CE2   . PHE A 1 3864 ? 185.965 165.424 212.083 1.00 10.20 ? 3864 PHE A CE2   1 
ATOM   17081 C CZ    . PHE A 1 3864 ? 186.189 166.705 211.638 1.00 6.57  ? 3864 PHE A CZ    1 
ATOM   17082 N N     . GLN A 1 3865 ? 189.132 165.121 218.135 1.00 9.78  ? 3865 GLN A N     1 
ATOM   17083 C CA    . GLN A 1 3865 ? 189.327 165.407 219.555 1.00 6.17  ? 3865 GLN A CA    1 
ATOM   17084 C C     . GLN A 1 3865 ? 190.759 165.837 219.858 1.00 1.46  ? 3865 GLN A C     1 
ATOM   17085 O O     . GLN A 1 3865 ? 190.979 166.805 220.593 1.00 4.84  ? 3865 GLN A O     1 
ATOM   17086 C CB    . GLN A 1 3865 ? 188.954 164.182 220.387 1.00 8.07  ? 3865 GLN A CB    1 
ATOM   17087 C CG    . GLN A 1 3865 ? 188.990 164.414 221.884 1.00 7.16  ? 3865 GLN A CG    1 
ATOM   17088 C CD    . GLN A 1 3865 ? 187.705 165.016 222.405 1.00 8.51  ? 3865 GLN A CD    1 
ATOM   17089 O OE1   . GLN A 1 3865 ? 187.416 166.187 222.169 1.00 9.47  ? 3865 GLN A OE1   1 
ATOM   17090 N NE2   . GLN A 1 3865 ? 186.921 164.214 223.113 1.00 12.74 ? 3865 GLN A NE2   1 
ATOM   17091 N N     . VAL A 1 3866 ? 191.746 165.126 219.312 1.00 2.79  ? 3866 VAL A N     1 
ATOM   17092 C CA    . VAL A 1 3866 ? 193.144 165.432 219.595 1.00 2.22  ? 3866 VAL A CA    1 
ATOM   17093 C C     . VAL A 1 3866 ? 193.541 166.758 218.963 1.00 3.08  ? 3866 VAL A C     1 
ATOM   17094 O O     . VAL A 1 3866 ? 194.312 167.529 219.547 1.00 6.43  ? 3866 VAL A O     1 
ATOM   17095 C CB    . VAL A 1 3866 ? 194.051 164.280 219.126 1.00 3.37  ? 3866 VAL A CB    1 
ATOM   17096 C CG1   . VAL A 1 3866 ? 195.514 164.647 219.296 1.00 4.96  ? 3866 VAL A CG1   1 
ATOM   17097 C CG2   . VAL A 1 3866 ? 193.743 163.018 219.911 1.00 4.02  ? 3866 VAL A CG2   1 
ATOM   17098 N N     . ALA A 1 3867 ? 193.031 167.048 217.762 1.00 7.14  ? 3867 ALA A N     1 
ATOM   17099 C CA    . ALA A 1 3867 ? 193.281 168.353 217.165 1.00 3.67  ? 3867 ALA A CA    1 
ATOM   17100 C C     . ALA A 1 3867 ? 192.750 169.464 218.055 1.00 3.23  ? 3867 ALA A C     1 
ATOM   17101 O O     . ALA A 1 3867 ? 193.468 170.429 218.352 1.00 2.90  ? 3867 ALA A O     1 
ATOM   17102 C CB    . ALA A 1 3867 ? 192.647 168.427 215.777 1.00 4.32  ? 3867 ALA A CB    1 
ATOM   17103 N N     . PHE A 1 3868 ? 191.503 169.329 218.519 1.00 3.60  ? 3868 PHE A N     1 
ATOM   17104 C CA    . PHE A 1 3868 ? 190.952 170.347 219.406 1.00 0.00  ? 3868 PHE A CA    1 
ATOM   17105 C C     . PHE A 1 3868 ? 191.777 170.478 220.676 1.00 4.05  ? 3868 PHE A C     1 
ATOM   17106 O O     . PHE A 1 3868 ? 192.092 171.590 221.102 1.00 11.10 ? 3868 PHE A O     1 
ATOM   17107 C CB    . PHE A 1 3868 ? 189.507 170.029 219.769 1.00 6.01  ? 3868 PHE A CB    1 
ATOM   17108 C CG    . PHE A 1 3868 ? 188.931 170.972 220.783 1.00 6.85  ? 3868 PHE A CG    1 
ATOM   17109 C CD1   . PHE A 1 3868 ? 188.598 172.267 220.429 1.00 7.37  ? 3868 PHE A CD1   1 
ATOM   17110 C CD2   . PHE A 1 3868 ? 188.753 170.578 222.097 1.00 2.73  ? 3868 PHE A CD2   1 
ATOM   17111 C CE1   . PHE A 1 3868 ? 188.078 173.141 221.356 1.00 0.00  ? 3868 PHE A CE1   1 
ATOM   17112 C CE2   . PHE A 1 3868 ? 188.235 171.451 223.029 1.00 4.72  ? 3868 PHE A CE2   1 
ATOM   17113 C CZ    . PHE A 1 3868 ? 187.899 172.735 222.656 1.00 2.99  ? 3868 PHE A CZ    1 
ATOM   17114 N N     . ASN A 1 3869 ? 192.142 169.353 221.291 1.00 6.25  ? 3869 ASN A N     1 
ATOM   17115 C CA    . ASN A 1 3869 ? 192.877 169.410 222.550 1.00 0.00  ? 3869 ASN A CA    1 
ATOM   17116 C C     . ASN A 1 3869 ? 194.220 170.102 222.373 1.00 0.00  ? 3869 ASN A C     1 
ATOM   17117 O O     . ASN A 1 3869 ? 194.526 171.067 223.085 1.00 3.44  ? 3869 ASN A O     1 
ATOM   17118 C CB    . ASN A 1 3869 ? 193.075 168.000 223.102 1.00 1.06  ? 3869 ASN A CB    1 
ATOM   17119 C CG    . ASN A 1 3869 ? 191.777 167.360 223.540 1.00 7.38  ? 3869 ASN A CG    1 
ATOM   17120 O OD1   . ASN A 1 3869 ? 190.794 168.046 223.811 1.00 8.91  ? 3869 ASN A OD1   1 
ATOM   17121 N ND2   . ASN A 1 3869 ? 191.766 166.035 223.607 1.00 5.76  ? 3869 ASN A ND2   1 
ATOM   17122 N N     . ARG A 1 3870 ? 195.019 169.647 221.407 1.00 0.00  ? 3870 ARG A N     1 
ATOM   17123 C CA    . ARG A 1 3870 ? 196.351 170.200 221.210 1.00 0.70  ? 3870 ARG A CA    1 
ATOM   17124 C C     . ARG A 1 3870 ? 196.320 171.664 220.799 1.00 2.29  ? 3870 ARG A C     1 
ATOM   17125 O O     . ARG A 1 3870 ? 197.157 172.444 221.263 1.00 2.08  ? 3870 ARG A O     1 
ATOM   17126 C CB    . ARG A 1 3870 ? 197.113 169.379 220.171 1.00 0.00  ? 3870 ARG A CB    1 
ATOM   17127 C CG    . ARG A 1 3870 ? 197.630 168.055 220.697 1.00 3.74  ? 3870 ARG A CG    1 
ATOM   17128 C CD    . ARG A 1 3870 ? 198.918 167.657 220.002 1.00 7.08  ? 3870 ARG A CD    1 
ATOM   17129 N NE    . ARG A 1 3870 ? 199.180 166.228 220.110 1.00 8.95  ? 3870 ARG A NE    1 
ATOM   17130 C CZ    . ARG A 1 3870 ? 200.373 165.674 219.949 1.00 13.53 ? 3870 ARG A CZ    1 
ATOM   17131 N NH1   . ARG A 1 3870 ? 201.438 166.402 219.661 1.00 14.13 ? 3870 ARG A NH1   1 
ATOM   17132 N NH2   . ARG A 1 3870 ? 200.500 164.357 220.078 1.00 13.52 ? 3870 ARG A NH2   1 
ATOM   17133 N N     . VAL A 1 3871 ? 195.389 172.063 219.936 1.00 5.88  ? 3871 VAL A N     1 
ATOM   17134 C CA    . VAL A 1 3871 ? 195.326 173.459 219.518 1.00 0.00  ? 3871 VAL A CA    1 
ATOM   17135 C C     . VAL A 1 3871 ? 194.789 174.349 220.630 1.00 1.41  ? 3871 VAL A C     1 
ATOM   17136 O O     . VAL A 1 3871 ? 195.374 175.388 220.943 1.00 5.43  ? 3871 VAL A O     1 
ATOM   17137 C CB    . VAL A 1 3871 ? 194.483 173.586 218.236 1.00 1.61  ? 3871 VAL A CB    1 
ATOM   17138 C CG1   . VAL A 1 3871 ? 194.324 175.041 217.851 1.00 2.20  ? 3871 VAL A CG1   1 
ATOM   17139 C CG2   . VAL A 1 3871 ? 195.126 172.811 217.114 1.00 10.36 ? 3871 VAL A CG2   1 
ATOM   17140 N N     . ALA A 1 3872 ? 193.673 173.957 221.251 1.00 1.63  ? 3872 ALA A N     1 
ATOM   17141 C CA    . ALA A 1 3872 ? 193.047 174.775 222.278 1.00 0.00  ? 3872 ALA A CA    1 
ATOM   17142 C C     . ALA A 1 3872 ? 193.887 174.875 223.541 1.00 1.73  ? 3872 ALA A C     1 
ATOM   17143 O O     . ALA A 1 3872 ? 193.731 175.841 224.292 1.00 11.00 ? 3872 ALA A O     1 
ATOM   17144 C CB    . ALA A 1 3872 ? 191.668 174.211 222.614 1.00 0.13  ? 3872 ALA A CB    1 
ATOM   17145 N N     . ARG A 1 3873 ? 194.777 173.914 223.797 1.00 8.95  ? 3873 ARG A N     1 
ATOM   17146 C CA    . ARG A 1 3873 ? 195.635 174.024 224.970 1.00 1.31  ? 3873 ARG A CA    1 
ATOM   17147 C C     . ARG A 1 3873 ? 196.494 175.282 224.931 1.00 0.64  ? 3873 ARG A C     1 
ATOM   17148 O O     . ARG A 1 3873 ? 196.930 175.756 225.985 1.00 6.76  ? 3873 ARG A O     1 
ATOM   17149 C CB    . ARG A 1 3873 ? 196.517 172.782 225.084 1.00 2.13  ? 3873 ARG A CB    1 
ATOM   17150 C CG    . ARG A 1 3873 ? 197.187 172.614 226.432 1.00 8.65  ? 3873 ARG A CG    1 
ATOM   17151 C CD    . ARG A 1 3873 ? 196.243 172.944 227.577 1.00 12.11 ? 3873 ARG A CD    1 
ATOM   17152 N NE    . ARG A 1 3873 ? 195.353 171.833 227.890 1.00 13.39 ? 3873 ARG A NE    1 
ATOM   17153 C CZ    . ARG A 1 3873 ? 194.309 171.913 228.702 1.00 11.98 ? 3873 ARG A CZ    1 
ATOM   17154 N NH1   . ARG A 1 3873 ? 193.982 173.049 229.297 1.00 10.69 ? 3873 ARG A NH1   1 
ATOM   17155 N NH2   . ARG A 1 3873 ? 193.577 170.827 228.928 1.00 9.97  ? 3873 ARG A NH2   1 
ATOM   17156 N N     . GLY A 1 3874 ? 196.736 175.835 223.746 1.00 3.50  ? 3874 GLY A N     1 
ATOM   17157 C CA    . GLY A 1 3874 ? 197.478 177.070 223.609 1.00 3.27  ? 3874 GLY A CA    1 
ATOM   17158 C C     . GLY A 1 3874 ? 196.630 178.198 223.061 1.00 3.05  ? 3874 GLY A C     1 
ATOM   17159 O O     . GLY A 1 3874 ? 197.086 178.976 222.219 1.00 3.40  ? 3874 GLY A O     1 
ATOM   17160 N N     . MET A 1 3875 ? 195.392 178.299 223.536 1.00 1.03  ? 3875 MET A N     1 
ATOM   17161 C CA    . MET A 1 3875 ? 194.451 179.312 223.084 1.00 0.58  ? 3875 MET A CA    1 
ATOM   17162 C C     . MET A 1 3875 ? 193.773 179.940 224.292 1.00 1.50  ? 3875 MET A C     1 
ATOM   17163 O O     . MET A 1 3875 ? 193.602 179.285 225.324 1.00 4.02  ? 3875 MET A O     1 
ATOM   17164 C CB    . MET A 1 3875 ? 193.404 178.701 222.149 1.00 0.40  ? 3875 MET A CB    1 
ATOM   17165 C CG    . MET A 1 3875 ? 193.807 178.692 220.690 1.00 2.20  ? 3875 MET A CG    1 
ATOM   17166 S SD    . MET A 1 3875 ? 192.781 177.612 219.682 1.00 8.97  ? 3875 MET A SD    1 
ATOM   17167 C CE    . MET A 1 3875 ? 191.320 178.616 219.488 1.00 4.59  ? 3875 MET A CE    1 
ATOM   17168 N N     . LEU A 1 3876 ? 193.390 181.208 224.164 1.00 0.00  ? 3876 LEU A N     1 
ATOM   17169 C CA    . LEU A 1 3876 ? 192.693 181.885 225.249 1.00 2.81  ? 3876 LEU A CA    1 
ATOM   17170 C C     . LEU A 1 3876 ? 191.311 181.275 225.459 1.00 0.00  ? 3876 LEU A C     1 
ATOM   17171 O O     . LEU A 1 3876 ? 190.692 180.741 224.538 1.00 4.12  ? 3876 LEU A O     1 
ATOM   17172 C CB    . LEU A 1 3876 ? 192.565 183.380 224.958 1.00 2.31  ? 3876 LEU A CB    1 
ATOM   17173 C CG    . LEU A 1 3876 ? 193.825 184.125 224.520 1.00 1.86  ? 3876 LEU A CG    1 
ATOM   17174 C CD1   . LEU A 1 3876 ? 193.479 185.541 224.100 1.00 4.09  ? 3876 LEU A CD1   1 
ATOM   17175 C CD2   . LEU A 1 3876 ? 194.849 184.140 225.635 1.00 1.29  ? 3876 LEU A CD2   1 
ATOM   17176 N N     . HIS A 1 3877 ? 190.815 181.373 226.693 1.00 0.00  ? 3877 HIS A N     1 
ATOM   17177 C CA    . HIS A 1 3877 ? 189.521 180.781 227.005 1.00 0.00  ? 3877 HIS A CA    1 
ATOM   17178 C C     . HIS A 1 3877 ? 188.385 181.696 226.568 1.00 9.49  ? 3877 HIS A C     1 
ATOM   17179 O O     . HIS A 1 3877 ? 187.424 181.918 227.312 1.00 21.39 ? 3877 HIS A O     1 
ATOM   17180 C CB    . HIS A 1 3877 ? 189.413 180.466 228.498 1.00 3.08  ? 3877 HIS A CB    1 
ATOM   17181 C CG    . HIS A 1 3877 ? 188.292 179.532 228.838 1.00 3.76  ? 3877 HIS A CG    1 
ATOM   17182 N ND1   . HIS A 1 3877 ? 186.969 179.846 228.616 1.00 1.95  ? 3877 HIS A ND1   1 
ATOM   17183 C CD2   . HIS A 1 3877 ? 188.299 178.287 229.369 1.00 3.31  ? 3877 HIS A CD2   1 
ATOM   17184 C CE1   . HIS A 1 3877 ? 186.208 178.839 229.004 1.00 2.29  ? 3877 HIS A CE1   1 
ATOM   17185 N NE2   . HIS A 1 3877 ? 186.990 177.880 229.464 1.00 5.06  ? 3877 HIS A NE2   1 
ATOM   17186 N N     . GLN A 1 3878 ? 188.495 182.223 225.354 1.00 6.52  ? 3878 GLN A N     1 
ATOM   17187 C CA    . GLN A 1 3878 ? 187.387 182.853 224.655 1.00 0.25  ? 3878 GLN A CA    1 
ATOM   17188 C C     . GLN A 1 3878 ? 187.329 182.413 223.207 1.00 5.40  ? 3878 GLN A C     1 
ATOM   17189 O O     . GLN A 1 3878 ? 186.397 182.800 222.495 1.00 5.68  ? 3878 GLN A O     1 
ATOM   17190 C CB    . GLN A 1 3878 ? 187.500 184.383 224.714 1.00 0.00  ? 3878 GLN A CB    1 
ATOM   17191 C CG    . GLN A 1 3878 ? 188.593 184.949 223.823 1.00 0.00  ? 3878 GLN A CG    1 
ATOM   17192 C CD    . GLN A 1 3878 ? 189.254 186.179 224.406 1.00 5.63  ? 3878 GLN A CD    1 
ATOM   17193 O OE1   . GLN A 1 3878 ? 189.032 186.528 225.564 1.00 10.22 ? 3878 GLN A OE1   1 
ATOM   17194 N NE2   . GLN A 1 3878 ? 190.071 186.847 223.602 1.00 8.65  ? 3878 GLN A NE2   1 
ATOM   17195 N N     . ASP A 1 3879 ? 188.290 181.612 222.755 1.00 8.28  ? 3879 ASP A N     1 
ATOM   17196 C CA    . ASP A 1 3879 ? 188.352 181.094 221.401 1.00 0.00  ? 3879 ASP A CA    1 
ATOM   17197 C C     . ASP A 1 3879 ? 188.158 179.588 221.346 1.00 2.49  ? 3879 ASP A C     1 
ATOM   17198 O O     . ASP A 1 3879 ? 188.146 179.022 220.249 1.00 12.06 ? 3879 ASP A O     1 
ATOM   17199 C CB    . ASP A 1 3879 ? 189.694 181.464 220.764 1.00 0.00  ? 3879 ASP A CB    1 
ATOM   17200 C CG    . ASP A 1 3879 ? 189.979 182.946 220.828 1.00 5.72  ? 3879 ASP A CG    1 
ATOM   17201 O OD1   . ASP A 1 3879 ? 189.015 183.732 220.910 1.00 14.47 ? 3879 ASP A OD1   1 
ATOM   17202 O OD2   . ASP A 1 3879 ? 191.168 183.326 220.808 1.00 8.40  ? 3879 ASP A OD2   1 
ATOM   17203 N N     . HIS A 1 3880 ? 188.018 178.922 222.496 1.00 2.71  ? 3880 HIS A N     1 
ATOM   17204 C CA    . HIS A 1 3880 ? 187.793 177.481 222.483 1.00 0.00  ? 3880 HIS A CA    1 
ATOM   17205 C C     . HIS A 1 3880 ? 186.497 177.140 221.767 1.00 2.48  ? 3880 HIS A C     1 
ATOM   17206 O O     . HIS A 1 3880 ? 186.432 176.158 221.022 1.00 11.61 ? 3880 HIS A O     1 
ATOM   17207 C CB    . HIS A 1 3880 ? 187.767 176.918 223.904 1.00 1.45  ? 3880 HIS A CB    1 
ATOM   17208 C CG    . HIS A 1 3880 ? 189.044 177.107 224.659 1.00 2.79  ? 3880 HIS A CG    1 
ATOM   17209 N ND1   . HIS A 1 3880 ? 190.250 176.607 224.221 1.00 2.46  ? 3880 HIS A ND1   1 
ATOM   17210 C CD2   . HIS A 1 3880 ? 189.293 177.699 225.849 1.00 8.36  ? 3880 HIS A CD2   1 
ATOM   17211 C CE1   . HIS A 1 3880 ? 191.193 176.913 225.093 1.00 0.00  ? 3880 HIS A CE1   1 
ATOM   17212 N NE2   . HIS A 1 3880 ? 190.639 177.575 226.091 1.00 0.66  ? 3880 HIS A NE2   1 
ATOM   17213 N N     . ILE A 1 3881 ? 185.448 177.934 221.988 1.00 5.11  ? 3881 ILE A N     1 
ATOM   17214 C CA    . ILE A 1 3881 ? 184.192 177.696 221.288 1.00 3.15  ? 3881 ILE A CA    1 
ATOM   17215 C C     . ILE A 1 3881 ? 184.354 177.958 219.796 1.00 1.58  ? 3881 ILE A C     1 
ATOM   17216 O O     . ILE A 1 3881 ? 183.773 177.250 218.967 1.00 12.83 ? 3881 ILE A O     1 
ATOM   17217 C CB    . ILE A 1 3881 ? 183.060 178.539 221.904 1.00 5.10  ? 3881 ILE A CB    1 
ATOM   17218 C CG1   . ILE A 1 3881 ? 181.718 178.158 221.278 1.00 4.71  ? 3881 ILE A CG1   1 
ATOM   17219 C CG2   . ILE A 1 3881 ? 183.333 180.028 221.750 1.00 3.21  ? 3881 ILE A CG2   1 
ATOM   17220 C CD1   . ILE A 1 3881 ? 181.391 176.690 221.389 1.00 5.49  ? 3881 ILE A CD1   1 
ATOM   17221 N N     . THR A 1 3882 ? 185.160 178.957 219.427 1.00 0.54  ? 3882 THR A N     1 
ATOM   17222 C CA    . THR A 1 3882 ? 185.352 179.267 218.014 1.00 2.03  ? 3882 THR A CA    1 
ATOM   17223 C C     . THR A 1 3882 ? 185.991 178.097 217.280 1.00 5.08  ? 3882 THR A C     1 
ATOM   17224 O O     . THR A 1 3882 ? 185.464 177.619 216.268 1.00 14.72 ? 3882 THR A O     1 
ATOM   17225 C CB    . THR A 1 3882 ? 186.206 180.526 217.863 1.00 2.86  ? 3882 THR A CB    1 
ATOM   17226 O OG1   . THR A 1 3882 ? 185.613 181.601 218.601 1.00 14.84 ? 3882 THR A OG1   1 
ATOM   17227 C CG2   . THR A 1 3882 ? 186.319 180.922 216.402 1.00 0.00  ? 3882 THR A CG2   1 
ATOM   17228 N N     . PHE A 1 3883 ? 187.121 177.606 217.792 1.00 0.59  ? 3883 PHE A N     1 
ATOM   17229 C CA    . PHE A 1 3883 ? 187.773 176.456 217.176 1.00 0.00  ? 3883 PHE A CA    1 
ATOM   17230 C C     . PHE A 1 3883 ? 186.900 175.213 217.258 1.00 4.28  ? 3883 PHE A C     1 
ATOM   17231 O O     . PHE A 1 3883 ? 186.825 174.437 216.300 1.00 10.51 ? 3883 PHE A O     1 
ATOM   17232 C CB    . PHE A 1 3883 ? 189.122 176.194 217.835 1.00 0.86  ? 3883 PHE A CB    1 
ATOM   17233 C CG    . PHE A 1 3883 ? 190.036 175.345 217.008 1.00 8.33  ? 3883 PHE A CG    1 
ATOM   17234 C CD1   . PHE A 1 3883 ? 190.356 175.709 215.712 1.00 7.04  ? 3883 PHE A CD1   1 
ATOM   17235 C CD2   . PHE A 1 3883 ? 190.552 174.167 217.515 1.00 3.32  ? 3883 PHE A CD2   1 
ATOM   17236 C CE1   . PHE A 1 3883 ? 191.190 174.923 214.946 1.00 4.42  ? 3883 PHE A CE1   1 
ATOM   17237 C CE2   . PHE A 1 3883 ? 191.381 173.376 216.752 1.00 2.68  ? 3883 PHE A CE2   1 
ATOM   17238 C CZ    . PHE A 1 3883 ? 191.704 173.756 215.466 1.00 0.00  ? 3883 PHE A CZ    1 
ATOM   17239 N N     . ALA A 1 3884 ? 186.240 175.001 218.397 1.00 0.09  ? 3884 ALA A N     1 
ATOM   17240 C CA    . ALA A 1 3884 ? 185.425 173.806 218.568 1.00 0.00  ? 3884 ALA A CA    1 
ATOM   17241 C C     . ALA A 1 3884 ? 184.297 173.759 217.551 1.00 0.00  ? 3884 ALA A C     1 
ATOM   17242 O O     . ALA A 1 3884 ? 184.030 172.711 216.956 1.00 11.84 ? 3884 ALA A O     1 
ATOM   17243 C CB    . ALA A 1 3884 ? 184.867 173.751 219.988 1.00 6.81  ? 3884 ALA A CB    1 
ATOM   17244 N N     . MET A 1 3885 ? 183.635 174.887 217.313 1.00 0.00  ? 3885 MET A N     1 
ATOM   17245 C CA    . MET A 1 3885 ? 182.527 174.876 216.373 1.00 3.56  ? 3885 MET A CA    1 
ATOM   17246 C C     . MET A 1 3885 ? 182.979 175.010 214.923 1.00 4.76  ? 3885 MET A C     1 
ATOM   17247 O O     . MET A 1 3885 ? 182.255 174.566 214.029 1.00 11.37 ? 3885 MET A O     1 
ATOM   17248 C CB    . MET A 1 3885 ? 181.515 175.955 216.759 1.00 1.94  ? 3885 MET A CB    1 
ATOM   17249 C CG    . MET A 1 3885 ? 181.829 177.348 216.329 1.00 3.58  ? 3885 MET A CG    1 
ATOM   17250 S SD    . MET A 1 3885 ? 180.447 178.400 216.799 1.00 30.43 ? 3885 MET A SD    1 
ATOM   17251 C CE    . MET A 1 3885 ? 179.059 177.356 216.361 1.00 9.93  ? 3885 MET A CE    1 
ATOM   17252 N N     . LEU A 1 3886 ? 184.177 175.540 214.662 1.00 2.53  ? 3886 LEU A N     1 
ATOM   17253 C CA    . LEU A 1 3886 ? 184.752 175.386 213.328 1.00 0.31  ? 3886 LEU A CA    1 
ATOM   17254 C C     . LEU A 1 3886 ? 185.033 173.917 213.028 1.00 5.39  ? 3886 LEU A C     1 
ATOM   17255 O O     . LEU A 1 3886 ? 184.759 173.430 211.924 1.00 14.35 ? 3886 LEU A O     1 
ATOM   17256 C CB    . LEU A 1 3886 ? 186.027 176.218 213.198 1.00 1.54  ? 3886 LEU A CB    1 
ATOM   17257 C CG    . LEU A 1 3886 ? 185.851 177.728 213.033 1.00 2.93  ? 3886 LEU A CG    1 
ATOM   17258 C CD1   . LEU A 1 3886 ? 187.190 178.430 213.152 1.00 5.20  ? 3886 LEU A CD1   1 
ATOM   17259 C CD2   . LEU A 1 3886 ? 185.192 178.054 211.706 1.00 8.72  ? 3886 LEU A CD2   1 
ATOM   17260 N N     . LEU A 1 3887 ? 185.575 173.190 214.009 1.00 2.46  ? 3887 LEU A N     1 
ATOM   17261 C CA    . LEU A 1 3887 ? 185.753 171.750 213.858 1.00 3.45  ? 3887 LEU A CA    1 
ATOM   17262 C C     . LEU A 1 3887 ? 184.419 171.036 213.700 1.00 6.55  ? 3887 LEU A C     1 
ATOM   17263 O O     . LEU A 1 3887 ? 184.320 170.068 212.941 1.00 14.70 ? 3887 LEU A O     1 
ATOM   17264 C CB    . LEU A 1 3887 ? 186.513 171.179 215.056 1.00 3.46  ? 3887 LEU A CB    1 
ATOM   17265 C CG    . LEU A 1 3887 ? 187.932 171.680 215.321 1.00 0.59  ? 3887 LEU A CG    1 
ATOM   17266 C CD1   . LEU A 1 3887 ? 188.671 170.712 216.221 1.00 0.26  ? 3887 LEU A CD1   1 
ATOM   17267 C CD2   . LEU A 1 3887 ? 188.685 171.877 214.020 1.00 2.89  ? 3887 LEU A CD2   1 
ATOM   17268 N N     . ALA A 1 3888 ? 183.393 171.482 214.426 1.00 6.29  ? 3888 ALA A N     1 
ATOM   17269 C CA    . ALA A 1 3888 ? 182.065 170.898 214.270 1.00 9.42  ? 3888 ALA A CA    1 
ATOM   17270 C C     . ALA A 1 3888 ? 181.531 171.117 212.861 1.00 7.73  ? 3888 ALA A C     1 
ATOM   17271 O O     . ALA A 1 3888 ? 180.910 170.222 212.280 1.00 13.37 ? 3888 ALA A O     1 
ATOM   17272 C CB    . ALA A 1 3888 ? 181.107 171.487 215.305 1.00 8.69  ? 3888 ALA A CB    1 
ATOM   17273 N N     . ARG A 1 3889 ? 181.755 172.306 212.302 1.00 5.03  ? 3889 ARG A N     1 
ATOM   17274 C CA    . ARG A 1 3889 ? 181.361 172.577 210.923 1.00 7.71  ? 3889 ARG A CA    1 
ATOM   17275 C C     . ARG A 1 3889 ? 182.123 171.687 209.946 1.00 9.40  ? 3889 ARG A C     1 
ATOM   17276 O O     . ARG A 1 3889 ? 181.548 171.174 208.975 1.00 14.18 ? 3889 ARG A O     1 
ATOM   17277 C CB    . ARG A 1 3889 ? 181.596 174.053 210.610 1.00 10.19 ? 3889 ARG A CB    1 
ATOM   17278 C CG    . ARG A 1 3889 ? 181.012 174.526 209.301 1.00 14.74 ? 3889 ARG A CG    1 
ATOM   17279 C CD    . ARG A 1 3889 ? 180.796 176.029 209.320 1.00 13.23 ? 3889 ARG A CD    1 
ATOM   17280 N NE    . ARG A 1 3889 ? 180.383 176.545 208.021 1.00 21.21 ? 3889 ARG A NE    1 
ATOM   17281 C CZ    . ARG A 1 3889 ? 180.043 177.806 207.792 1.00 19.43 ? 3889 ARG A CZ    1 
ATOM   17282 N NH1   . ARG A 1 3889 ? 180.057 178.711 208.757 1.00 9.47  ? 3889 ARG A NH1   1 
ATOM   17283 N NH2   . ARG A 1 3889 ? 179.682 178.168 206.565 1.00 15.04 ? 3889 ARG A NH2   1 
ATOM   17284 N N     . ILE A 1 3890 ? 183.421 171.496 210.189 1.00 8.49  ? 3890 ILE A N     1 
ATOM   17285 C CA    . ILE A 1 3890 ? 184.225 170.615 209.345 1.00 8.03  ? 3890 ILE A CA    1 
ATOM   17286 C C     . ILE A 1 3890 ? 183.671 169.195 209.389 1.00 5.71  ? 3890 ILE A C     1 
ATOM   17287 O O     . ILE A 1 3890 ? 183.537 168.526 208.358 1.00 11.11 ? 3890 ILE A O     1 
ATOM   17288 C CB    . ILE A 1 3890 ? 185.700 170.658 209.781 1.00 8.75  ? 3890 ILE A CB    1 
ATOM   17289 C CG1   . ILE A 1 3890 ? 186.399 171.886 209.203 1.00 4.97  ? 3890 ILE A CG1   1 
ATOM   17290 C CG2   . ILE A 1 3890 ? 186.426 169.402 209.341 1.00 10.53 ? 3890 ILE A CG2   1 
ATOM   17291 C CD1   . ILE A 1 3890 ? 187.821 172.048 209.688 1.00 4.22  ? 3890 ILE A CD1   1 
ATOM   17292 N N     . LYS A 1 3891 ? 183.335 168.719 210.588 1.00 3.29  ? 3891 LYS A N     1 
ATOM   17293 C CA    . LYS A 1 3891 ? 182.762 167.384 210.730 1.00 5.75  ? 3891 LYS A CA    1 
ATOM   17294 C C     . LYS A 1 3891 ? 181.403 167.289 210.047 1.00 13.46 ? 3891 LYS A C     1 
ATOM   17295 O O     . LYS A 1 3891 ? 181.075 166.263 209.441 1.00 16.78 ? 3891 LYS A O     1 
ATOM   17296 C CB    . LYS A 1 3891 ? 182.647 167.022 212.210 1.00 6.47  ? 3891 LYS A CB    1 
ATOM   17297 C CG    . LYS A 1 3891 ? 181.985 165.684 212.479 1.00 8.85  ? 3891 LYS A CG    1 
ATOM   17298 C CD    . LYS A 1 3891 ? 182.767 164.880 213.503 1.00 10.22 ? 3891 LYS A CD    1 
ATOM   17299 C CE    . LYS A 1 3891 ? 182.445 163.399 213.408 1.00 13.59 ? 3891 LYS A CE    1 
ATOM   17300 N NZ    . LYS A 1 3891 ? 183.161 162.613 214.448 1.00 20.24 ? 3891 LYS A NZ    1 
ATOM   17301 N N     . LEU A 1 3892 ? 180.596 168.347 210.144 1.00 11.35 ? 3892 LEU A N     1 
ATOM   17302 C CA    . LEU A 1 3892 ? 179.276 168.337 209.523 1.00 10.38 ? 3892 LEU A CA    1 
ATOM   17303 C C     . LEU A 1 3892 ? 179.383 168.249 208.007 1.00 14.45 ? 3892 LEU A C     1 
ATOM   17304 O O     . LEU A 1 3892 ? 178.588 167.560 207.359 1.00 20.82 ? 3892 LEU A O     1 
ATOM   17305 C CB    . LEU A 1 3892 ? 178.494 169.581 209.941 1.00 11.41 ? 3892 LEU A CB    1 
ATOM   17306 C CG    . LEU A 1 3892 ? 177.118 169.754 209.304 1.00 17.25 ? 3892 LEU A CG    1 
ATOM   17307 C CD1   . LEU A 1 3892 ? 176.278 168.521 209.545 1.00 19.02 ? 3892 LEU A CD1   1 
ATOM   17308 C CD2   . LEU A 1 3892 ? 176.432 170.979 209.869 1.00 18.37 ? 3892 LEU A CD2   1 
ATOM   17309 N N     . LYS A 1 3893 ? 180.353 168.951 207.421 1.00 16.04 ? 3893 LYS A N     1 
ATOM   17310 C CA    . LYS A 1 3893 ? 180.639 168.740 206.003 1.00 15.87 ? 3893 LYS A CA    1 
ATOM   17311 C C     . LYS A 1 3893 ? 181.219 167.351 205.755 1.00 15.72 ? 3893 LYS A C     1 
ATOM   17312 O O     . LYS A 1 3893 ? 181.070 166.795 204.661 1.00 17.98 ? 3893 LYS A O     1 
ATOM   17313 C CB    . LYS A 1 3893 ? 181.572 169.830 205.464 1.00 11.09 ? 3893 LYS A CB    1 
ATOM   17314 C CG    . LYS A 1 3893 ? 180.927 171.202 205.182 1.00 16.55 ? 3893 LYS A CG    1 
ATOM   17315 C CD    . LYS A 1 3893 ? 179.939 171.696 206.229 1.00 20.00 ? 3893 LYS A CD    1 
ATOM   17316 C CE    . LYS A 1 3893 ? 179.717 173.195 206.114 1.00 21.00 ? 3893 LYS A CE    1 
ATOM   17317 N NZ    . LYS A 1 3893 ? 178.803 173.709 207.171 1.00 12.10 ? 3893 LYS A NZ    1 
ATOM   17318 N N     . GLY A 1 3894 ? 181.883 166.775 206.758 1.00 20.54 ? 3894 GLY A N     1 
ATOM   17319 C CA    . GLY A 1 3894 ? 182.422 165.434 206.601 1.00 19.81 ? 3894 GLY A CA    1 
ATOM   17320 C C     . GLY A 1 3894 ? 181.349 164.363 206.517 1.00 22.78 ? 3894 GLY A C     1 
ATOM   17321 O O     . GLY A 1 3894 ? 181.460 163.425 205.722 1.00 20.88 ? 3894 GLY A O     1 
ATOM   17322 N N     . THR A 1 3895 ? 180.305 164.480 207.333 1.00 25.70 ? 3895 THR A N     1 
ATOM   17323 C CA    . THR A 1 3895 ? 179.275 163.452 207.385 1.00 27.77 ? 3895 THR A CA    1 
ATOM   17324 C C     . THR A 1 3895 ? 178.305 163.590 206.213 1.00 28.27 ? 3895 THR A C     1 
ATOM   17325 O O     . THR A 1 3895 ? 178.202 164.639 205.572 1.00 23.80 ? 3895 THR A O     1 
ATOM   17326 C CB    . THR A 1 3895 ? 178.511 163.518 208.708 1.00 28.09 ? 3895 THR A CB    1 
ATOM   17327 O OG1   . THR A 1 3895 ? 177.507 162.495 208.735 1.00 31.17 ? 3895 THR A OG1   1 
ATOM   17328 C CG2   . THR A 1 3895 ? 177.851 164.870 208.872 1.00 24.39 ? 3895 THR A CG2   1 
ATOM   17329 N N     . VAL A 1 3896 ? 177.583 162.505 205.943 1.00 31.82 ? 3896 VAL A N     1 
ATOM   17330 C CA    . VAL A 1 3896 ? 176.705 162.436 204.782 1.00 33.62 ? 3896 VAL A CA    1 
ATOM   17331 C C     . VAL A 1 3896 ? 175.242 162.211 205.142 1.00 32.86 ? 3896 VAL A C     1 
ATOM   17332 O O     . VAL A 1 3896 ? 174.387 162.256 204.242 1.00 31.78 ? 3896 VAL A O     1 
ATOM   17333 C CB    . VAL A 1 3896 ? 177.178 161.344 203.800 1.00 31.51 ? 3896 VAL A CB    1 
ATOM   17334 C CG1   . VAL A 1 3896 ? 178.565 161.666 203.276 1.00 29.59 ? 3896 VAL A CG1   1 
ATOM   17335 C CG2   . VAL A 1 3896 ? 177.166 159.984 204.479 1.00 32.18 ? 3896 VAL A CG2   1 
ATOM   17336 N N     . GLY A 1 3897 ? 174.905 161.973 206.411 1.00 32.25 ? 3897 GLY A N     1 
ATOM   17337 C CA    . GLY A 1 3897 ? 173.530 161.673 206.767 1.00 32.70 ? 3897 GLY A CA    1 
ATOM   17338 C C     . GLY A 1 3897 ? 172.588 162.856 206.680 1.00 33.38 ? 3897 GLY A C     1 
ATOM   17339 O O     . GLY A 1 3897 ? 171.375 162.663 206.549 1.00 31.73 ? 3897 GLY A O     1 
ATOM   17340 N N     . GLU A 1 3898 ? 173.113 164.074 206.748 1.00 32.29 ? 3898 GLU A N     1 
ATOM   17341 C CA    . GLU A 1 3898 ? 172.307 165.284 206.749 1.00 33.31 ? 3898 GLU A CA    1 
ATOM   17342 C C     . GLU A 1 3898 ? 172.941 166.321 205.833 1.00 31.84 ? 3898 GLU A C     1 
ATOM   17343 O O     . GLU A 1 3898 ? 174.145 166.251 205.555 1.00 32.01 ? 3898 GLU A O     1 
ATOM   17344 C CB    . GLU A 1 3898 ? 172.152 165.847 208.173 1.00 34.60 ? 3898 GLU A CB    1 
ATOM   17345 C CG    . GLU A 1 3898 ? 173.432 166.369 208.801 1.00 32.31 ? 3898 GLU A CG    1 
ATOM   17346 C CD    . GLU A 1 3898 ? 174.229 165.276 209.489 1.00 33.01 ? 3898 GLU A CD    1 
ATOM   17347 O OE1   . GLU A 1 3898 ? 173.966 164.084 209.225 1.00 33.67 ? 3898 GLU A OE1   1 
ATOM   17348 O OE2   . GLU A 1 3898 ? 175.111 165.607 210.306 1.00 32.96 ? 3898 GLU A OE2   1 
ATOM   17349 N N     . PRO A 1 3899 ? 172.159 167.280 205.338 1.00 30.17 ? 3899 PRO A N     1 
ATOM   17350 C CA    . PRO A 1 3899 ? 172.695 168.260 204.386 1.00 27.74 ? 3899 PRO A CA    1 
ATOM   17351 C C     . PRO A 1 3899 ? 173.771 169.133 205.014 1.00 32.29 ? 3899 PRO A C     1 
ATOM   17352 O O     . PRO A 1 3899 ? 174.011 169.123 206.222 1.00 34.90 ? 3899 PRO A O     1 
ATOM   17353 C CB    . PRO A 1 3899 ? 171.469 169.091 203.995 1.00 26.88 ? 3899 PRO A CB    1 
ATOM   17354 C CG    . PRO A 1 3899 ? 170.302 168.224 204.313 1.00 31.81 ? 3899 PRO A CG    1 
ATOM   17355 C CD    . PRO A 1 3899 ? 170.705 167.437 205.518 1.00 29.51 ? 3899 PRO A CD    1 
ATOM   17356 N N     . THR A 1 3900 ? 174.431 169.908 204.151 1.00 27.36 ? 3900 THR A N     1 
ATOM   17357 C CA    . THR A 1 3900 ? 175.492 170.803 204.593 1.00 28.73 ? 3900 THR A CA    1 
ATOM   17358 C C     . THR A 1 3900 ? 174.968 172.013 205.355 1.00 30.42 ? 3900 THR A C     1 
ATOM   17359 O O     . THR A 1 3900 ? 175.732 172.622 206.113 1.00 32.01 ? 3900 THR A O     1 
ATOM   17360 C CB    . THR A 1 3900 ? 176.318 171.276 203.394 1.00 30.18 ? 3900 THR A CB    1 
ATOM   17361 O OG1   . THR A 1 3900 ? 177.332 172.185 203.838 1.00 29.28 ? 3900 THR A OG1   1 
ATOM   17362 C CG2   . THR A 1 3900 ? 175.429 171.972 202.374 1.00 27.94 ? 3900 THR A CG2   1 
ATOM   17363 N N     . TYR A 1 3901 ? 173.692 172.367 205.177 1.00 29.87 ? 3901 TYR A N     1 
ATOM   17364 C CA    . TYR A 1 3901 ? 173.092 173.533 205.829 1.00 26.17 ? 3901 TYR A CA    1 
ATOM   17365 C C     . TYR A 1 3901 ? 173.893 174.800 205.540 1.00 25.33 ? 3901 TYR A C     1 
ATOM   17366 O O     . TYR A 1 3901 ? 174.100 175.640 206.417 1.00 27.27 ? 3901 TYR A O     1 
ATOM   17367 C CB    . TYR A 1 3901 ? 172.944 173.312 207.336 1.00 20.42 ? 3901 TYR A CB    1 
ATOM   17368 C CG    . TYR A 1 3901 ? 171.953 172.231 207.698 1.00 21.45 ? 3901 TYR A CG    1 
ATOM   17369 C CD1   . TYR A 1 3901 ? 172.347 171.116 208.424 1.00 25.22 ? 3901 TYR A CD1   1 
ATOM   17370 C CD2   . TYR A 1 3901 ? 170.623 172.325 207.313 1.00 25.27 ? 3901 TYR A CD2   1 
ATOM   17371 C CE1   . TYR A 1 3901 ? 171.445 170.125 208.754 1.00 29.07 ? 3901 TYR A CE1   1 
ATOM   17372 C CE2   . TYR A 1 3901 ? 169.713 171.340 207.638 1.00 28.64 ? 3901 TYR A CE2   1 
ATOM   17373 C CZ    . TYR A 1 3901 ? 170.129 170.242 208.359 1.00 31.93 ? 3901 TYR A CZ    1 
ATOM   17374 O OH    . TYR A 1 3901 ? 169.224 169.258 208.684 1.00 32.74 ? 3901 TYR A OH    1 
ATOM   17375 N N     . ASP A 1 3902 ? 174.344 174.938 204.290 1.00 25.01 ? 3902 ASP A N     1 
ATOM   17376 C CA    . ASP A 1 3902 ? 175.186 176.070 203.917 1.00 24.22 ? 3902 ASP A CA    1 
ATOM   17377 C C     . ASP A 1 3902 ? 174.438 177.386 204.098 1.00 26.89 ? 3902 ASP A C     1 
ATOM   17378 O O     . ASP A 1 3902 ? 174.992 178.355 204.631 1.00 30.83 ? 3902 ASP A O     1 
ATOM   17379 C CB    . ASP A 1 3902 ? 175.656 175.889 202.468 1.00 26.28 ? 3902 ASP A CB    1 
ATOM   17380 C CG    . ASP A 1 3902 ? 176.541 177.030 201.964 1.00 27.42 ? 3902 ASP A CG    1 
ATOM   17381 O OD1   . ASP A 1 3902 ? 176.743 178.039 202.668 1.00 24.99 ? 3902 ASP A OD1   1 
ATOM   17382 O OD2   . ASP A 1 3902 ? 177.046 176.906 200.829 1.00 31.71 ? 3902 ASP A OD2   1 
ATOM   17383 N N     . ALA A 1 3903 ? 173.173 177.436 203.676 1.00 30.37 ? 3903 ALA A N     1 
ATOM   17384 C CA    . ALA A 1 3903 ? 172.399 178.668 203.796 1.00 26.42 ? 3903 ALA A CA    1 
ATOM   17385 C C     . ALA A 1 3903 ? 172.198 179.059 205.254 1.00 23.58 ? 3903 ALA A C     1 
ATOM   17386 O O     . ALA A 1 3903 ? 172.272 180.244 205.603 1.00 28.11 ? 3903 ALA A O     1 
ATOM   17387 C CB    . ALA A 1 3903 ? 171.053 178.512 203.090 1.00 26.94 ? 3903 ALA A CB    1 
ATOM   17388 N N     . GLU A 1 3904 ? 171.930 178.078 206.120 1.00 19.30 ? 3904 GLU A N     1 
ATOM   17389 C CA    . GLU A 1 3904 ? 171.738 178.378 207.536 1.00 23.30 ? 3904 GLU A CA    1 
ATOM   17390 C C     . GLU A 1 3904 ? 173.007 178.942 208.162 1.00 23.28 ? 3904 GLU A C     1 
ATOM   17391 O O     . GLU A 1 3904 ? 172.949 179.911 208.926 1.00 24.24 ? 3904 GLU A O     1 
ATOM   17392 C CB    . GLU A 1 3904 ? 171.278 177.127 208.282 1.00 20.23 ? 3904 GLU A CB    1 
ATOM   17393 C CG    . GLU A 1 3904 ? 169.793 176.830 208.138 1.00 19.30 ? 3904 GLU A CG    1 
ATOM   17394 C CD    . GLU A 1 3904 ? 169.491 175.897 206.983 1.00 27.91 ? 3904 GLU A CD    1 
ATOM   17395 O OE1   . GLU A 1 3904 ? 170.382 175.691 206.133 1.00 33.16 ? 3904 GLU A OE1   1 
ATOM   17396 O OE2   . GLU A 1 3904 ? 168.361 175.369 206.925 1.00 28.21 ? 3904 GLU A OE2   1 
ATOM   17397 N N     . PHE A 1 3905 ? 174.165 178.353 207.851 1.00 18.87 ? 3905 PHE A N     1 
ATOM   17398 C CA    . PHE A 1 3905 ? 175.420 178.892 208.366 1.00 15.89 ? 3905 PHE A CA    1 
ATOM   17399 C C     . PHE A 1 3905 ? 175.693 180.284 207.817 1.00 16.68 ? 3905 PHE A C     1 
ATOM   17400 O O     . PHE A 1 3905 ? 176.175 181.159 208.544 1.00 23.02 ? 3905 PHE A O     1 
ATOM   17401 C CB    . PHE A 1 3905 ? 176.584 177.958 208.042 1.00 18.31 ? 3905 PHE A CB    1 
ATOM   17402 C CG    . PHE A 1 3905 ? 176.695 176.780 208.965 1.00 20.36 ? 3905 PHE A CG    1 
ATOM   17403 C CD1   . PHE A 1 3905 ? 177.257 176.925 210.222 1.00 15.07 ? 3905 PHE A CD1   1 
ATOM   17404 C CD2   . PHE A 1 3905 ? 176.259 175.528 208.572 1.00 20.68 ? 3905 PHE A CD2   1 
ATOM   17405 C CE1   . PHE A 1 3905 ? 177.370 175.847 211.075 1.00 18.06 ? 3905 PHE A CE1   1 
ATOM   17406 C CE2   . PHE A 1 3905 ? 176.370 174.445 209.419 1.00 17.64 ? 3905 PHE A CE2   1 
ATOM   17407 C CZ    . PHE A 1 3905 ? 176.925 174.605 210.673 1.00 21.02 ? 3905 PHE A CZ    1 
ATOM   17408 N N     . GLN A 1 3906 ? 175.407 180.507 206.534 1.00 17.07 ? 3906 GLN A N     1 
ATOM   17409 C CA    . GLN A 1 3906 ? 175.639 181.826 205.954 1.00 18.03 ? 3906 GLN A CA    1 
ATOM   17410 C C     . GLN A 1 3906 ? 174.770 182.880 206.628 1.00 16.33 ? 3906 GLN A C     1 
ATOM   17411 O O     . GLN A 1 3906 ? 175.234 183.993 206.911 1.00 16.08 ? 3906 GLN A O     1 
ATOM   17412 C CB    . GLN A 1 3906 ? 175.377 181.793 204.450 1.00 19.30 ? 3906 GLN A CB    1 
ATOM   17413 C CG    . GLN A 1 3906 ? 176.048 182.919 203.695 1.00 19.27 ? 3906 GLN A CG    1 
ATOM   17414 C CD    . GLN A 1 3906 ? 177.552 182.756 203.646 1.00 20.31 ? 3906 GLN A CD    1 
ATOM   17415 O OE1   . GLN A 1 3906 ? 178.281 183.390 204.407 1.00 21.40 ? 3906 GLN A OE1   1 
ATOM   17416 N NE2   . GLN A 1 3906 ? 178.026 181.900 202.749 1.00 20.01 ? 3906 GLN A NE2   1 
ATOM   17417 N N     . HIS A 1 3907 ? 173.505 182.546 206.894 1.00 19.57 ? 3907 HIS A N     1 
ATOM   17418 C CA    . HIS A 1 3907 ? 172.643 183.468 207.623 1.00 17.68 ? 3907 HIS A CA    1 
ATOM   17419 C C     . HIS A 1 3907 ? 173.185 183.710 209.024 1.00 19.47 ? 3907 HIS A C     1 
ATOM   17420 O O     . HIS A 1 3907 ? 173.424 184.857 209.406 1.00 23.85 ? 3907 HIS A O     1 
ATOM   17421 C CB    . HIS A 1 3907 ? 171.212 182.935 207.675 1.00 19.79 ? 3907 HIS A CB    1 
ATOM   17422 C CG    . HIS A 1 3907 ? 170.248 183.861 208.350 1.00 23.85 ? 3907 HIS A CG    1 
ATOM   17423 N ND1   . HIS A 1 3907 ? 169.741 183.624 209.609 1.00 23.03 ? 3907 HIS A ND1   1 
ATOM   17424 C CD2   . HIS A 1 3907 ? 169.700 185.029 207.940 1.00 20.94 ? 3907 HIS A CD2   1 
ATOM   17425 C CE1   . HIS A 1 3907 ? 168.919 184.602 209.944 1.00 18.98 ? 3907 HIS A CE1   1 
ATOM   17426 N NE2   . HIS A 1 3907 ? 168.877 185.469 208.949 1.00 17.55 ? 3907 HIS A NE2   1 
ATOM   17427 N N     . PHE A 1 3908 ? 173.477 182.631 209.755 1.00 16.73 ? 3908 PHE A N     1 
ATOM   17428 C CA    . PHE A 1 3908 ? 174.017 182.730 211.107 1.00 17.79 ? 3908 PHE A CA    1 
ATOM   17429 C C     . PHE A 1 3908 ? 175.263 183.604 211.160 1.00 18.11 ? 3908 PHE A C     1 
ATOM   17430 O O     . PHE A 1 3908 ? 175.490 184.302 212.155 1.00 16.53 ? 3908 PHE A O     1 
ATOM   17431 C CB    . PHE A 1 3908 ? 174.328 181.324 211.619 1.00 14.65 ? 3908 PHE A CB    1 
ATOM   17432 C CG    . PHE A 1 3908 ? 174.973 181.288 212.971 1.00 14.70 ? 3908 PHE A CG    1 
ATOM   17433 C CD1   . PHE A 1 3908 ? 174.285 181.709 214.095 1.00 18.16 ? 3908 PHE A CD1   1 
ATOM   17434 C CD2   . PHE A 1 3908 ? 176.266 180.821 213.120 1.00 10.49 ? 3908 PHE A CD2   1 
ATOM   17435 C CE1   . PHE A 1 3908 ? 174.876 181.666 215.339 1.00 14.52 ? 3908 PHE A CE1   1 
ATOM   17436 C CE2   . PHE A 1 3908 ? 176.861 180.778 214.361 1.00 10.22 ? 3908 PHE A CE2   1 
ATOM   17437 C CZ    . PHE A 1 3908 ? 176.165 181.198 215.472 1.00 14.24 ? 3908 PHE A CZ    1 
ATOM   17438 N N     . LEU A 1 3909 ? 176.079 183.584 210.107 1.00 12.67 ? 3909 LEU A N     1 
ATOM   17439 C CA    . LEU A 1 3909 ? 177.315 184.358 210.115 1.00 6.91  ? 3909 LEU A CA    1 
ATOM   17440 C C     . LEU A 1 3909 ? 177.074 185.822 209.761 1.00 14.86 ? 3909 LEU A C     1 
ATOM   17441 O O     . LEU A 1 3909 ? 177.523 186.721 210.479 1.00 21.31 ? 3909 LEU A O     1 
ATOM   17442 C CB    . LEU A 1 3909 ? 178.335 183.737 209.158 1.00 12.35 ? 3909 LEU A CB    1 
ATOM   17443 C CG    . LEU A 1 3909 ? 178.951 182.404 209.580 1.00 17.22 ? 3909 LEU A CG    1 
ATOM   17444 C CD1   . LEU A 1 3909 ? 180.293 182.209 208.898 1.00 17.62 ? 3909 LEU A CD1   1 
ATOM   17445 C CD2   . LEU A 1 3909 ? 179.103 182.333 211.088 1.00 12.82 ? 3909 LEU A CD2   1 
ATOM   17446 N N     . ARG A 1 3910 ? 176.376 186.092 208.651 1.00 20.17 ? 3910 ARG A N     1 
ATOM   17447 C CA    . ARG A 1 3910 ? 176.303 187.462 208.152 1.00 19.89 ? 3910 ARG A CA    1 
ATOM   17448 C C     . ARG A 1 3910 ? 174.942 187.916 207.643 1.00 20.58 ? 3910 ARG A C     1 
ATOM   17449 O O     . ARG A 1 3910 ? 174.840 189.057 207.180 1.00 21.10 ? 3910 ARG A O     1 
ATOM   17450 C CB    . ARG A 1 3910 ? 177.330 187.672 207.029 1.00 19.51 ? 3910 ARG A CB    1 
ATOM   17451 C CG    . ARG A 1 3910 ? 177.165 186.731 205.853 1.00 18.92 ? 3910 ARG A CG    1 
ATOM   17452 C CD    . ARG A 1 3910 ? 178.473 186.559 205.101 1.00 18.13 ? 3910 ARG A CD    1 
ATOM   17453 N NE    . ARG A 1 3910 ? 179.176 187.824 204.927 1.00 18.13 ? 3910 ARG A NE    1 
ATOM   17454 C CZ    . ARG A 1 3910 ? 180.372 187.943 204.369 1.00 22.19 ? 3910 ARG A CZ    1 
ATOM   17455 N NH1   . ARG A 1 3910 ? 181.031 186.890 203.914 1.00 19.36 ? 3910 ARG A NH1   1 
ATOM   17456 N NH2   . ARG A 1 3910 ? 180.921 189.150 204.262 1.00 22.20 ? 3910 ARG A NH2   1 
ATOM   17457 N N     . GLY A 1 3911 ? 173.901 187.085 207.703 1.00 26.75 ? 3911 GLY A N     1 
ATOM   17458 C CA    . GLY A 1 3911 ? 172.623 187.461 207.127 1.00 31.07 ? 3911 GLY A CA    1 
ATOM   17459 C C     . GLY A 1 3911 ? 171.817 188.413 207.982 1.00 32.56 ? 3911 GLY A C     1 
ATOM   17460 O O     . GLY A 1 3911 ? 170.829 188.976 207.501 1.00 33.56 ? 3911 GLY A O     1 
ATOM   17461 N N     . ASN A 1 3912 ? 172.211 188.601 209.240 1.00 25.52 ? 3912 ASN A N     1 
ATOM   17462 C CA    . ASN A 1 3912 ? 171.560 189.599 210.074 1.00 28.68 ? 3912 ASN A CA    1 
ATOM   17463 C C     . ASN A 1 3912 ? 171.975 191.016 209.705 1.00 29.39 ? 3912 ASN A C     1 
ATOM   17464 O O     . ASN A 1 3912 ? 171.392 191.972 210.226 1.00 32.08 ? 3912 ASN A O     1 
ATOM   17465 C CB    . ASN A 1 3912 ? 171.855 189.318 211.549 1.00 31.11 ? 3912 ASN A CB    1 
ATOM   17466 C CG    . ASN A 1 3912 ? 173.327 189.444 211.884 1.00 36.12 ? 3912 ASN A CG    1 
ATOM   17467 O OD1   . ASN A 1 3912 ? 173.850 190.547 212.027 1.00 30.70 ? 3912 ASN A OD1   1 
ATOM   17468 N ND2   . ASN A 1 3912 ? 174.007 188.309 211.996 1.00 31.24 ? 3912 ASN A ND2   1 
ATOM   17469 N N     . GLU A 1 3913 ? 172.958 191.171 208.821 1.00 28.29 ? 3913 GLU A N     1 
ATOM   17470 C CA    . GLU A 1 3913 ? 173.381 192.475 208.333 1.00 30.44 ? 3913 GLU A CA    1 
ATOM   17471 C C     . GLU A 1 3913 ? 172.561 192.951 207.142 1.00 32.65 ? 3913 GLU A C     1 
ATOM   17472 O O     . GLU A 1 3913 ? 172.827 194.040 206.622 1.00 30.95 ? 3913 GLU A O     1 
ATOM   17473 C CB    . GLU A 1 3913 ? 174.867 192.442 207.951 1.00 29.51 ? 3913 GLU A CB    1 
ATOM   17474 C CG    . GLU A 1 3913 ? 175.777 191.619 208.874 1.00 32.49 ? 3913 GLU A CG    1 
ATOM   17475 C CD    . GLU A 1 3913 ? 175.740 192.023 210.347 1.00 29.91 ? 3913 GLU A CD    1 
ATOM   17476 O OE1   . GLU A 1 3913 ? 176.443 191.366 211.143 1.00 29.00 ? 3913 GLU A OE1   1 
ATOM   17477 O OE2   . GLU A 1 3913 ? 175.054 192.998 210.718 1.00 28.00 ? 3913 GLU A OE2   1 
ATOM   17478 N N     . ILE A 1 3914 ? 171.583 192.161 206.694 1.00 32.84 ? 3914 ILE A N     1 
ATOM   17479 C CA    . ILE A 1 3914 ? 170.718 192.594 205.605 1.00 32.33 ? 3914 ILE A CA    1 
ATOM   17480 C C     . ILE A 1 3914 ? 169.913 193.803 206.055 1.00 34.35 ? 3914 ILE A C     1 
ATOM   17481 O O     . ILE A 1 3914 ? 169.267 193.788 207.111 1.00 36.71 ? 3914 ILE A O     1 
ATOM   17482 C CB    . ILE A 1 3914 ? 169.797 191.447 205.160 1.00 31.72 ? 3914 ILE A CB    1 
ATOM   17483 C CG1   . ILE A 1 3914 ? 170.619 190.284 204.607 1.00 30.96 ? 3914 ILE A CG1   1 
ATOM   17484 C CG2   . ILE A 1 3914 ? 168.799 191.936 204.120 1.00 31.56 ? 3914 ILE A CG2   1 
ATOM   17485 C CD1   . ILE A 1 3914 ? 169.813 189.023 204.389 1.00 30.71 ? 3914 ILE A CD1   1 
ATOM   17486 N N     . VAL A 1 3915 ? 169.948 194.860 205.253 1.00 34.10 ? 3915 VAL A N     1 
ATOM   17487 C CA    . VAL A 1 3915 ? 169.303 196.119 205.604 1.00 32.91 ? 3915 VAL A CA    1 
ATOM   17488 C C     . VAL A 1 3915 ? 167.871 196.117 205.086 1.00 32.50 ? 3915 VAL A C     1 
ATOM   17489 O O     . VAL A 1 3915 ? 167.614 195.765 203.928 1.00 32.38 ? 3915 VAL A O     1 
ATOM   17490 C CB    . VAL A 1 3915 ? 170.097 197.318 205.060 1.00 34.59 ? 3915 VAL A CB    1 
ATOM   17491 C CG1   . VAL A 1 3915 ? 170.268 197.228 203.547 1.00 31.06 ? 3915 VAL A CG1   1 
ATOM   17492 C CG2   . VAL A 1 3915 ? 169.415 198.618 205.451 1.00 33.05 ? 3915 VAL A CG2   1 
ATOM   17493 N N     . LEU A 1 3916 ? 166.937 196.487 205.958 1.00 34.36 ? 3916 LEU A N     1 
ATOM   17494 C CA    . LEU A 1 3916 ? 165.527 196.631 205.624 1.00 37.58 ? 3916 LEU A CA    1 
ATOM   17495 C C     . LEU A 1 3916 ? 164.826 197.277 206.809 1.00 38.32 ? 3916 LEU A C     1 
ATOM   17496 O O     . LEU A 1 3916 ? 165.230 197.087 207.960 1.00 38.29 ? 3916 LEU A O     1 
ATOM   17497 C CB    . LEU A 1 3916 ? 164.874 195.284 205.283 1.00 38.20 ? 3916 LEU A CB    1 
ATOM   17498 C CG    . LEU A 1 3916 ? 164.509 194.324 206.417 1.00 38.16 ? 3916 LEU A CG    1 
ATOM   17499 C CD1   . LEU A 1 3916 ? 163.559 193.261 205.895 1.00 36.78 ? 3916 LEU A CD1   1 
ATOM   17500 C CD2   . LEU A 1 3916 ? 165.746 193.683 207.029 1.00 34.92 ? 3916 LEU A CD2   1 
ATOM   17501 N N     . SER A 1 3917 ? 163.777 198.047 206.514 1.00 41.66 ? 3917 SER A N     1 
ATOM   17502 C CA    . SER A 1 3917 ? 163.032 198.761 207.546 1.00 44.43 ? 3917 SER A CA    1 
ATOM   17503 C C     . SER A 1 3917 ? 161.530 198.527 207.431 1.00 44.55 ? 3917 SER A C     1 
ATOM   17504 O O     . SER A 1 3917 ? 160.743 199.340 207.927 1.00 45.47 ? 3917 SER A O     1 
ATOM   17505 C CB    . SER A 1 3917 ? 163.339 200.260 207.496 1.00 42.40 ? 3917 SER A CB    1 
ATOM   17506 O OG    . SER A 1 3917 ? 162.873 200.837 206.289 1.00 39.23 ? 3917 SER A OG    1 
ATOM   17507 N N     . ALA A 1 3918 ? 161.116 197.438 206.791 1.00 39.39 ? 3918 ALA A N     1 
ATOM   17508 C CA    . ALA A 1 3918 ? 159.703 197.129 206.623 1.00 40.32 ? 3918 ALA A CA    1 
ATOM   17509 C C     . ALA A 1 3918 ? 159.276 196.078 207.638 1.00 41.39 ? 3918 ALA A C     1 
ATOM   17510 O O     . ALA A 1 3918 ? 159.899 195.017 207.745 1.00 42.52 ? 3918 ALA A O     1 
ATOM   17511 C CB    . ALA A 1 3918 ? 159.424 196.639 205.202 1.00 37.25 ? 3918 ALA A CB    1 
ATOM   17512 N N     . GLY A 1 3919 ? 158.211 196.376 208.380 1.00 39.04 ? 3919 GLY A N     1 
ATOM   17513 C CA    . GLY A 1 3919 ? 157.701 195.438 209.359 1.00 36.44 ? 3919 GLY A CA    1 
ATOM   17514 C C     . GLY A 1 3919 ? 158.548 195.288 210.600 1.00 38.97 ? 3919 GLY A C     1 
ATOM   17515 O O     . GLY A 1 3919 ? 158.433 194.277 211.296 1.00 39.12 ? 3919 GLY A O     1 
ATOM   17516 N N     . SER A 1 3920 ? 159.396 196.268 210.902 1.00 41.20 ? 3920 SER A N     1 
ATOM   17517 C CA    . SER A 1 3920 ? 160.260 196.200 212.073 1.00 40.68 ? 3920 SER A CA    1 
ATOM   17518 C C     . SER A 1 3920 ? 159.558 196.629 213.355 1.00 42.93 ? 3920 SER A C     1 
ATOM   17519 O O     . SER A 1 3920 ? 160.165 196.550 214.429 1.00 44.89 ? 3920 SER A O     1 
ATOM   17520 C CB    . SER A 1 3920 ? 161.509 197.059 211.856 1.00 40.54 ? 3920 SER A CB    1 
ATOM   17521 O OG    . SER A 1 3920 ? 161.175 198.304 211.268 1.00 44.46 ? 3920 SER A OG    1 
ATOM   17522 N N     . THR A 1 3921 ? 158.310 197.078 213.272 1.00 46.07 ? 3921 THR A N     1 
ATOM   17523 C CA    . THR A 1 3921 ? 157.565 197.477 214.462 1.00 45.88 ? 3921 THR A CA    1 
ATOM   17524 C C     . THR A 1 3921 ? 157.139 196.242 215.246 1.00 44.58 ? 3921 THR A C     1 
ATOM   17525 O O     . THR A 1 3921 ? 156.553 195.321 214.664 1.00 42.93 ? 3921 THR A O     1 
ATOM   17526 C CB    . THR A 1 3921 ? 156.334 198.291 214.087 1.00 46.62 ? 3921 THR A CB    1 
ATOM   17527 O OG1   . THR A 1 3921 ? 155.425 197.470 213.343 1.00 46.48 ? 3921 THR A OG1   1 
ATOM   17528 C CG2   . THR A 1 3921 ? 156.730 199.495 213.242 1.00 44.71 ? 3921 THR A CG2   1 
ATOM   17529 N N     . PRO A 1 3922 ? 157.425 196.179 216.547 1.00 46.93 ? 3922 PRO A N     1 
ATOM   17530 C CA    . PRO A 1 3922 ? 156.983 195.026 217.342 1.00 46.23 ? 3922 PRO A CA    1 
ATOM   17531 C C     . PRO A 1 3922 ? 155.467 194.907 217.345 1.00 46.16 ? 3922 PRO A C     1 
ATOM   17532 O O     . PRO A 1 3922 ? 154.744 195.906 217.374 1.00 46.23 ? 3922 PRO A O     1 
ATOM   17533 C CB    . PRO A 1 3922 ? 157.530 195.328 218.743 1.00 43.93 ? 3922 PRO A CB    1 
ATOM   17534 C CG    . PRO A 1 3922 ? 158.637 196.315 218.519 1.00 45.27 ? 3922 PRO A CG    1 
ATOM   17535 C CD    . PRO A 1 3922 ? 158.202 197.139 217.347 1.00 44.62 ? 3922 PRO A CD    1 
ATOM   17536 N N     . ARG A 1 3923 ? 154.988 193.665 217.315 1.00 43.60 ? 3923 ARG A N     1 
ATOM   17537 C CA    . ARG A 1 3923 ? 153.558 193.392 217.260 1.00 45.53 ? 3923 ARG A CA    1 
ATOM   17538 C C     . ARG A 1 3923 ? 152.987 192.903 218.582 1.00 46.63 ? 3923 ARG A C     1 
ATOM   17539 O O     . ARG A 1 3923 ? 151.883 193.312 218.954 1.00 44.04 ? 3923 ARG A O     1 
ATOM   17540 C CB    . ARG A 1 3923 ? 153.264 192.355 216.171 1.00 44.74 ? 3923 ARG A CB    1 
ATOM   17541 C CG    . ARG A 1 3923 ? 151.790 192.059 215.971 1.00 44.20 ? 3923 ARG A CG    1 
ATOM   17542 C CD    . ARG A 1 3923 ? 151.598 190.623 215.530 1.00 42.81 ? 3923 ARG A CD    1 
ATOM   17543 N NE    . ARG A 1 3923 ? 152.318 189.705 216.402 1.00 43.71 ? 3923 ARG A NE    1 
ATOM   17544 C CZ    . ARG A 1 3923 ? 152.345 188.389 216.247 1.00 45.60 ? 3923 ARG A CZ    1 
ATOM   17545 N NH1   . ARG A 1 3923 ? 151.696 187.797 215.258 1.00 44.42 ? 3923 ARG A NH1   1 
ATOM   17546 N NH2   . ARG A 1 3923 ? 153.039 187.649 217.106 1.00 45.85 ? 3923 ARG A NH2   1 
ATOM   17547 N N     . ILE A 1 3924 ? 153.709 192.048 219.300 1.00 47.05 ? 3924 ILE A N     1 
ATOM   17548 C CA    . ILE A 1 3924 ? 153.258 191.527 220.583 1.00 46.95 ? 3924 ILE A CA    1 
ATOM   17549 C C     . ILE A 1 3924 ? 153.931 192.328 221.690 1.00 45.98 ? 3924 ILE A C     1 
ATOM   17550 O O     . ILE A 1 3924 ? 155.033 192.862 221.519 1.00 44.95 ? 3924 ILE A O     1 
ATOM   17551 C CB    . ILE A 1 3924 ? 153.553 190.016 220.722 1.00 46.94 ? 3924 ILE A CB    1 
ATOM   17552 C CG1   . ILE A 1 3924 ? 152.839 189.428 221.943 1.00 46.25 ? 3924 ILE A CG1   1 
ATOM   17553 C CG2   . ILE A 1 3924 ? 155.050 189.763 220.800 1.00 45.61 ? 3924 ILE A CG2   1 
ATOM   17554 C CD1   . ILE A 1 3924 ? 152.815 187.915 221.969 1.00 46.47 ? 3924 ILE A CD1   1 
ATOM   17555 N N     . GLN A 1 3925 ? 153.243 192.427 222.832 1.00 51.05 ? 3925 GLN A N     1 
ATOM   17556 C CA    . GLN A 1 3925 ? 153.777 193.186 223.958 1.00 52.84 ? 3925 GLN A CA    1 
ATOM   17557 C C     . GLN A 1 3925 ? 155.047 192.554 224.515 1.00 51.89 ? 3925 GLN A C     1 
ATOM   17558 O O     . GLN A 1 3925 ? 155.874 193.251 225.113 1.00 51.90 ? 3925 GLN A O     1 
ATOM   17559 C CB    . GLN A 1 3925 ? 152.717 193.312 225.053 1.00 52.04 ? 3925 GLN A CB    1 
ATOM   17560 C CG    . GLN A 1 3925 ? 152.056 191.998 225.432 1.00 52.25 ? 3925 GLN A CG    1 
ATOM   17561 C CD    . GLN A 1 3925 ? 150.822 192.194 226.290 1.00 53.28 ? 3925 GLN A CD    1 
ATOM   17562 O OE1   . GLN A 1 3925 ? 150.496 193.315 226.683 1.00 52.24 ? 3925 GLN A OE1   1 
ATOM   17563 N NE2   . GLN A 1 3925 ? 150.126 191.102 226.585 1.00 52.95 ? 3925 GLN A NE2   1 
ATOM   17564 N N     . GLY A 1 3926 ? 155.219 191.248 224.334 1.00 41.97 ? 3926 GLY A N     1 
ATOM   17565 C CA    . GLY A 1 3926 ? 156.417 190.576 224.797 1.00 39.81 ? 3926 GLY A CA    1 
ATOM   17566 C C     . GLY A 1 3926 ? 157.516 190.532 223.756 1.00 40.45 ? 3926 GLY A C     1 
ATOM   17567 O O     . GLY A 1 3926 ? 158.069 189.465 223.473 1.00 43.61 ? 3926 GLY A O     1 
ATOM   17568 N N     . LEU A 1 3927 ? 157.841 191.685 223.176 1.00 35.67 ? 3927 LEU A N     1 
ATOM   17569 C CA    . LEU A 1 3927 ? 158.877 191.765 222.157 1.00 36.20 ? 3927 LEU A CA    1 
ATOM   17570 C C     . LEU A 1 3927 ? 159.414 193.188 222.113 1.00 35.34 ? 3927 LEU A C     1 
ATOM   17571 O O     . LEU A 1 3927 ? 158.708 194.139 222.458 1.00 37.26 ? 3927 LEU A O     1 
ATOM   17572 C CB    . LEU A 1 3927 ? 158.339 191.349 220.783 1.00 36.78 ? 3927 LEU A CB    1 
ATOM   17573 C CG    . LEU A 1 3927 ? 159.362 190.957 219.717 1.00 35.72 ? 3927 LEU A CG    1 
ATOM   17574 C CD1   . LEU A 1 3927 ? 159.949 189.587 220.015 1.00 31.33 ? 3927 LEU A CD1   1 
ATOM   17575 C CD2   . LEU A 1 3927 ? 158.724 190.979 218.338 1.00 36.43 ? 3927 LEU A CD2   1 
ATOM   17576 N N     . THR A 1 3928 ? 160.665 193.322 221.686 1.00 33.12 ? 3928 THR A N     1 
ATOM   17577 C CA    . THR A 1 3928 ? 161.328 194.614 221.563 1.00 34.57 ? 3928 THR A CA    1 
ATOM   17578 C C     . THR A 1 3928 ? 161.726 194.854 220.109 1.00 34.02 ? 3928 THR A C     1 
ATOM   17579 O O     . THR A 1 3928 ? 161.538 194.001 219.239 1.00 31.94 ? 3928 THR A O     1 
ATOM   17580 C CB    . THR A 1 3928 ? 162.545 194.701 222.487 1.00 33.62 ? 3928 THR A CB    1 
ATOM   17581 O OG1   . THR A 1 3928 ? 163.068 196.035 222.467 1.00 35.07 ? 3928 THR A OG1   1 
ATOM   17582 C CG2   . THR A 1 3928 ? 163.625 193.739 222.040 1.00 34.06 ? 3928 THR A CG2   1 
ATOM   17583 N N     . VAL A 1 3929 ? 162.282 196.041 219.853 1.00 33.64 ? 3929 VAL A N     1 
ATOM   17584 C CA    . VAL A 1 3929 ? 162.567 196.450 218.481 1.00 34.52 ? 3929 VAL A CA    1 
ATOM   17585 C C     . VAL A 1 3929 ? 163.719 195.639 217.891 1.00 34.20 ? 3929 VAL A C     1 
ATOM   17586 O O     . VAL A 1 3929 ? 163.654 195.202 216.735 1.00 33.03 ? 3929 VAL A O     1 
ATOM   17587 C CB    . VAL A 1 3929 ? 162.824 197.970 218.418 1.00 34.12 ? 3929 VAL A CB    1 
ATOM   17588 C CG1   . VAL A 1 3929 ? 164.078 198.362 219.190 1.00 34.65 ? 3929 VAL A CG1   1 
ATOM   17589 C CG2   . VAL A 1 3929 ? 162.913 198.433 216.971 1.00 32.18 ? 3929 VAL A CG2   1 
ATOM   17590 N N     . GLU A 1 3930 ? 164.788 195.418 218.664 1.00 35.12 ? 3930 GLU A N     1 
ATOM   17591 C CA    . GLU A 1 3930 ? 165.901 194.624 218.153 1.00 35.50 ? 3930 GLU A CA    1 
ATOM   17592 C C     . GLU A 1 3930 ? 165.488 193.171 217.949 1.00 33.90 ? 3930 GLU A C     1 
ATOM   17593 O O     . GLU A 1 3930 ? 165.865 192.545 216.950 1.00 33.23 ? 3930 GLU A O     1 
ATOM   17594 C CB    . GLU A 1 3930 ? 167.108 194.728 219.090 1.00 37.15 ? 3930 GLU A CB    1 
ATOM   17595 C CG    . GLU A 1 3930 ? 166.920 194.106 220.467 1.00 36.89 ? 3930 GLU A CG    1 
ATOM   17596 C CD    . GLU A 1 3930 ? 168.218 194.011 221.247 1.00 37.54 ? 3930 GLU A CD    1 
ATOM   17597 O OE1   . GLU A 1 3930 ? 168.952 193.017 221.066 1.00 37.07 ? 3930 GLU A OE1   1 
ATOM   17598 O OE2   . GLU A 1 3930 ? 168.503 194.932 222.040 1.00 36.27 ? 3930 GLU A OE2   1 
ATOM   17599 N N     . GLN A 1 3931 ? 164.692 192.627 218.871 1.00 31.13 ? 3931 GLN A N     1 
ATOM   17600 C CA    . GLN A 1 3931 ? 164.183 191.274 218.690 1.00 31.70 ? 3931 GLN A CA    1 
ATOM   17601 C C     . GLN A 1 3931 ? 163.250 191.197 217.490 1.00 34.17 ? 3931 GLN A C     1 
ATOM   17602 O O     . GLN A 1 3931 ? 163.276 190.214 216.748 1.00 31.37 ? 3931 GLN A O     1 
ATOM   17603 C CB    . GLN A 1 3931 ? 163.475 190.800 219.958 1.00 29.08 ? 3931 GLN A CB    1 
ATOM   17604 C CG    . GLN A 1 3931 ? 164.416 190.340 221.060 1.00 31.57 ? 3931 GLN A CG    1 
ATOM   17605 C CD    . GLN A 1 3931 ? 163.677 189.948 222.323 1.00 34.92 ? 3931 GLN A CD    1 
ATOM   17606 O OE1   . GLN A 1 3931 ? 162.447 189.957 222.362 1.00 38.48 ? 3931 GLN A OE1   1 
ATOM   17607 N NE2   . GLN A 1 3931 ? 164.424 189.602 223.364 1.00 30.77 ? 3931 GLN A NE2   1 
ATOM   17608 N N     . ALA A 1 3932 ? 162.423 192.225 217.278 1.00 31.58 ? 3932 ALA A N     1 
ATOM   17609 C CA    . ALA A 1 3932 ? 161.546 192.234 216.111 1.00 29.43 ? 3932 ALA A CA    1 
ATOM   17610 C C     . ALA A 1 3932 ? 162.347 192.256 214.815 1.00 29.78 ? 3932 ALA A C     1 
ATOM   17611 O O     . ALA A 1 3932 ? 162.020 191.542 213.857 1.00 28.56 ? 3932 ALA A O     1 
ATOM   17612 C CB    . ALA A 1 3932 ? 160.598 193.432 216.174 1.00 30.13 ? 3932 ALA A CB    1 
ATOM   17613 N N     . GLU A 1 3933 ? 163.402 193.072 214.764 1.00 27.17 ? 3933 GLU A N     1 
ATOM   17614 C CA    . GLU A 1 3933 ? 164.254 193.100 213.580 1.00 24.39 ? 3933 GLU A CA    1 
ATOM   17615 C C     . GLU A 1 3933 ? 164.929 191.752 213.360 1.00 28.45 ? 3933 GLU A C     1 
ATOM   17616 O O     . GLU A 1 3933 ? 165.046 191.283 212.220 1.00 29.53 ? 3933 GLU A O     1 
ATOM   17617 C CB    . GLU A 1 3933 ? 165.293 194.213 213.709 1.00 24.50 ? 3933 GLU A CB    1 
ATOM   17618 C CG    . GLU A 1 3933 ? 165.925 194.623 212.391 1.00 29.56 ? 3933 GLU A CG    1 
ATOM   17619 C CD    . GLU A 1 3933 ? 167.221 195.386 212.576 1.00 30.82 ? 3933 GLU A CD    1 
ATOM   17620 O OE1   . GLU A 1 3933 ? 167.580 195.681 213.736 1.00 31.76 ? 3933 GLU A OE1   1 
ATOM   17621 O OE2   . GLU A 1 3933 ? 167.880 195.694 211.561 1.00 27.32 ? 3933 GLU A OE2   1 
ATOM   17622 N N     . ALA A 1 3934 ? 165.387 191.116 214.442 1.00 26.53 ? 3934 ALA A N     1 
ATOM   17623 C CA    . ALA A 1 3934 ? 165.968 189.784 214.323 1.00 25.79 ? 3934 ALA A CA    1 
ATOM   17624 C C     . ALA A 1 3934 ? 164.945 188.787 213.798 1.00 26.14 ? 3934 ALA A C     1 
ATOM   17625 O O     . ALA A 1 3934 ? 165.276 187.917 212.985 1.00 27.91 ? 3934 ALA A O     1 
ATOM   17626 C CB    . ALA A 1 3934 ? 166.520 189.329 215.673 1.00 24.69 ? 3934 ALA A CB    1 
ATOM   17627 N N     . VAL A 1 3935 ? 163.696 188.901 214.252 1.00 25.18 ? 3935 VAL A N     1 
ATOM   17628 C CA    . VAL A 1 3935 ? 162.628 188.044 213.745 1.00 25.95 ? 3935 VAL A CA    1 
ATOM   17629 C C     . VAL A 1 3935 ? 162.451 188.243 212.249 1.00 25.91 ? 3935 VAL A C     1 
ATOM   17630 O O     . VAL A 1 3935 ? 162.282 187.277 211.499 1.00 26.65 ? 3935 VAL A O     1 
ATOM   17631 C CB    . VAL A 1 3935 ? 161.315 188.310 214.505 1.00 29.32 ? 3935 VAL A CB    1 
ATOM   17632 C CG1   . VAL A 1 3935 ? 160.186 187.518 213.890 1.00 28.17 ? 3935 VAL A CG1   1 
ATOM   17633 C CG2   . VAL A 1 3935 ? 161.459 187.917 215.950 1.00 30.26 ? 3935 VAL A CG2   1 
ATOM   17634 N N     . VAL A 1 3936 ? 162.475 189.495 211.791 1.00 23.91 ? 3936 VAL A N     1 
ATOM   17635 C CA    . VAL A 1 3936 ? 162.301 189.761 210.362 1.00 26.32 ? 3936 VAL A CA    1 
ATOM   17636 C C     . VAL A 1 3936 ? 163.447 189.152 209.558 1.00 26.79 ? 3936 VAL A C     1 
ATOM   17637 O O     . VAL A 1 3936 ? 163.228 188.473 208.543 1.00 28.25 ? 3936 VAL A O     1 
ATOM   17638 C CB    . VAL A 1 3936 ? 162.170 191.273 210.105 1.00 26.20 ? 3936 VAL A CB    1 
ATOM   17639 C CG1   . VAL A 1 3936 ? 161.976 191.533 208.626 1.00 24.60 ? 3936 VAL A CG1   1 
ATOM   17640 C CG2   . VAL A 1 3936 ? 161.001 191.841 210.889 1.00 27.46 ? 3936 VAL A CG2   1 
ATOM   17641 N N     . ARG A 1 3937 ? 164.688 189.377 210.002 1.00 24.98 ? 3937 ARG A N     1 
ATOM   17642 C CA    . ARG A 1 3937 ? 165.831 188.829 209.273 1.00 25.84 ? 3937 ARG A CA    1 
ATOM   17643 C C     . ARG A 1 3937 ? 165.812 187.306 209.266 1.00 24.43 ? 3937 ARG A C     1 
ATOM   17644 O O     . ARG A 1 3937 ? 166.192 186.679 208.271 1.00 23.56 ? 3937 ARG A O     1 
ATOM   17645 C CB    . ARG A 1 3937 ? 167.152 189.335 209.853 1.00 28.94 ? 3937 ARG A CB    1 
ATOM   17646 C CG    . ARG A 1 3937 ? 167.648 190.651 209.270 1.00 27.05 ? 3937 ARG A CG    1 
ATOM   17647 C CD    . ARG A 1 3937 ? 167.047 191.842 209.974 1.00 28.52 ? 3937 ARG A CD    1 
ATOM   17648 N NE    . ARG A 1 3937 ? 167.328 191.797 211.403 1.00 30.55 ? 3937 ARG A NE    1 
ATOM   17649 C CZ    . ARG A 1 3937 ? 168.465 192.195 211.956 1.00 30.76 ? 3937 ARG A CZ    1 
ATOM   17650 N NH1   . ARG A 1 3937 ? 169.450 192.696 211.228 1.00 32.38 ? 3937 ARG A NH1   1 
ATOM   17651 N NH2   . ARG A 1 3937 ? 168.620 192.086 213.272 1.00 25.93 ? 3937 ARG A NH2   1 
ATOM   17652 N N     . LEU A 1 3938 ? 165.390 186.690 210.371 1.00 25.10 ? 3938 LEU A N     1 
ATOM   17653 C CA    . LEU A 1 3938 ? 165.303 185.236 210.413 1.00 26.33 ? 3938 LEU A CA    1 
ATOM   17654 C C     . LEU A 1 3938 ? 164.156 184.724 209.550 1.00 29.47 ? 3938 LEU A C     1 
ATOM   17655 O O     . LEU A 1 3938 ? 164.243 183.627 208.989 1.00 28.53 ? 3938 LEU A O     1 
ATOM   17656 C CB    . LEU A 1 3938 ? 165.148 184.773 211.859 1.00 20.87 ? 3938 LEU A CB    1 
ATOM   17657 C CG    . LEU A 1 3938 ? 165.124 183.273 212.130 1.00 24.00 ? 3938 LEU A CG    1 
ATOM   17658 C CD1   . LEU A 1 3938 ? 166.441 182.642 211.719 1.00 22.49 ? 3938 LEU A CD1   1 
ATOM   17659 C CD2   . LEU A 1 3938 ? 164.852 183.035 213.596 1.00 26.16 ? 3938 LEU A CD2   1 
ATOM   17660 N N     . SER A 1 3939 ? 163.077 185.501 209.436 1.00 27.01 ? 3939 SER A N     1 
ATOM   17661 C CA    . SER A 1 3939 ? 161.985 185.154 208.538 1.00 25.65 ? 3939 SER A CA    1 
ATOM   17662 C C     . SER A 1 3939 ? 162.401 185.258 207.081 1.00 24.30 ? 3939 SER A C     1 
ATOM   17663 O O     . SER A 1 3939 ? 161.811 184.585 206.229 1.00 23.32 ? 3939 SER A O     1 
ATOM   17664 C CB    . SER A 1 3939 ? 160.779 186.055 208.803 1.00 25.37 ? 3939 SER A CB    1 
ATOM   17665 O OG    . SER A 1 3939 ? 161.006 187.362 208.305 1.00 24.51 ? 3939 SER A OG    1 
ATOM   17666 N N     . CYS A 1 3940 ? 163.394 186.096 206.776 1.00 24.05 ? 3940 CYS A N     1 
ATOM   17667 C CA    . CYS A 1 3940 ? 163.961 186.097 205.430 1.00 22.50 ? 3940 CYS A CA    1 
ATOM   17668 C C     . CYS A 1 3940 ? 164.512 184.725 205.057 1.00 24.09 ? 3940 CYS A C     1 
ATOM   17669 O O     . CYS A 1 3940 ? 164.478 184.342 203.882 1.00 25.39 ? 3940 CYS A O     1 
ATOM   17670 C CB    . CYS A 1 3940 ? 165.053 187.161 205.320 1.00 23.51 ? 3940 CYS A CB    1 
ATOM   17671 S SG    . CYS A 1 3940 ? 166.037 187.083 203.807 1.00 31.78 ? 3940 CYS A SG    1 
ATOM   17672 N N     . LEU A 1 3941 ? 165.018 183.977 206.034 1.00 27.82 ? 3941 LEU A N     1 
ATOM   17673 C CA    . LEU A 1 3941 ? 165.489 182.625 205.776 1.00 27.72 ? 3941 LEU A CA    1 
ATOM   17674 C C     . LEU A 1 3941 ? 164.314 181.726 205.388 1.00 27.91 ? 3941 LEU A C     1 
ATOM   17675 O O     . LEU A 1 3941 ? 163.242 181.811 205.995 1.00 27.53 ? 3941 LEU A O     1 
ATOM   17676 C CB    . LEU A 1 3941 ? 166.198 182.064 207.009 1.00 23.83 ? 3941 LEU A CB    1 
ATOM   17677 C CG    . LEU A 1 3941 ? 167.053 180.806 206.850 1.00 25.52 ? 3941 LEU A CG    1 
ATOM   17678 C CD1   . LEU A 1 3941 ? 168.343 181.124 206.112 1.00 22.48 ? 3941 LEU A CD1   1 
ATOM   17679 C CD2   . LEU A 1 3941 ? 167.347 180.181 208.204 1.00 26.50 ? 3941 LEU A CD2   1 
ATOM   17680 N N     . PRO A 1 3942 ? 164.482 180.863 204.382 1.00 26.34 ? 3942 PRO A N     1 
ATOM   17681 C CA    . PRO A 1 3942 ? 163.353 180.026 203.939 1.00 26.69 ? 3942 PRO A CA    1 
ATOM   17682 C C     . PRO A 1 3942 ? 162.803 179.105 205.014 1.00 25.86 ? 3942 PRO A C     1 
ATOM   17683 O O     . PRO A 1 3942 ? 161.621 178.745 204.959 1.00 25.88 ? 3942 PRO A O     1 
ATOM   17684 C CB    . PRO A 1 3942 ? 163.945 179.234 202.763 1.00 25.74 ? 3942 PRO A CB    1 
ATOM   17685 C CG    . PRO A 1 3942 ? 165.428 179.310 202.948 1.00 26.30 ? 3942 PRO A CG    1 
ATOM   17686 C CD    . PRO A 1 3942 ? 165.682 180.651 203.557 1.00 24.92 ? 3942 PRO A CD    1 
ATOM   17687 N N     . ALA A 1 3943 ? 163.620 178.706 205.990 1.00 22.48 ? 3943 ALA A N     1 
ATOM   17688 C CA    . ALA A 1 3943 ? 163.148 177.787 207.018 1.00 25.11 ? 3943 ALA A CA    1 
ATOM   17689 C C     . ALA A 1 3943 ? 162.199 178.449 208.009 1.00 27.55 ? 3943 ALA A C     1 
ATOM   17690 O O     . ALA A 1 3943 ? 161.531 177.742 208.771 1.00 28.93 ? 3943 ALA A O     1 
ATOM   17691 C CB    . ALA A 1 3943 ? 164.334 177.177 207.765 1.00 22.59 ? 3943 ALA A CB    1 
ATOM   17692 N N     . PHE A 1 3944 ? 162.123 179.778 208.022 1.00 29.74 ? 3944 PHE A N     1 
ATOM   17693 C CA    . PHE A 1 3944 ? 161.300 180.514 208.976 1.00 29.42 ? 3944 PHE A CA    1 
ATOM   17694 C C     . PHE A 1 3944 ? 160.326 181.452 208.268 1.00 30.28 ? 3944 PHE A C     1 
ATOM   17695 O O     . PHE A 1 3944 ? 160.151 182.604 208.669 1.00 28.44 ? 3944 PHE A O     1 
ATOM   17696 C CB    . PHE A 1 3944 ? 162.159 181.304 209.966 1.00 28.27 ? 3944 PHE A CB    1 
ATOM   17697 C CG    . PHE A 1 3944 ? 163.138 180.465 210.752 1.00 25.84 ? 3944 PHE A CG    1 
ATOM   17698 C CD1   . PHE A 1 3944 ? 164.257 179.915 210.149 1.00 26.78 ? 3944 PHE A CD1   1 
ATOM   17699 C CD2   . PHE A 1 3944 ? 162.931 180.228 212.100 1.00 24.52 ? 3944 PHE A CD2   1 
ATOM   17700 C CE1   . PHE A 1 3944 ? 165.146 179.149 210.875 1.00 27.00 ? 3944 PHE A CE1   1 
ATOM   17701 C CE2   . PHE A 1 3944 ? 163.817 179.463 212.829 1.00 22.83 ? 3944 PHE A CE2   1 
ATOM   17702 C CZ    . PHE A 1 3944 ? 164.925 178.923 212.215 1.00 25.56 ? 3944 PHE A CZ    1 
ATOM   17703 N N     . LYS A 1 3945 ? 159.675 180.970 207.205 1.00 29.98 ? 3945 LYS A N     1 
ATOM   17704 C CA    . LYS A 1 3945 ? 158.647 181.768 206.540 1.00 30.14 ? 3945 LYS A CA    1 
ATOM   17705 C C     . LYS A 1 3945 ? 157.538 182.164 207.506 1.00 32.10 ? 3945 LYS A C     1 
ATOM   17706 O O     . LYS A 1 3945 ? 157.166 183.339 207.599 1.00 32.63 ? 3945 LYS A O     1 
ATOM   17707 C CB    . LYS A 1 3945 ? 158.070 180.999 205.348 1.00 31.06 ? 3945 LYS A CB    1 
ATOM   17708 C CG    . LYS A 1 3945 ? 159.064 180.635 204.245 1.00 33.56 ? 3945 LYS A CG    1 
ATOM   17709 C CD    . LYS A 1 3945 ? 159.512 181.864 203.445 1.00 32.27 ? 3945 LYS A CD    1 
ATOM   17710 C CE    . LYS A 1 3945 ? 160.796 182.493 203.960 1.00 31.92 ? 3945 LYS A CE    1 
ATOM   17711 N NZ    . LYS A 1 3945 ? 161.248 183.614 203.090 1.00 29.19 ? 3945 LYS A NZ    1 
ATOM   17712 N N     . ASP A 1 3946 ? 157.002 181.194 208.244 1.00 35.39 ? 3946 ASP A N     1 
ATOM   17713 C CA    . ASP A 1 3946 ? 155.956 181.459 209.229 1.00 35.58 ? 3946 ASP A CA    1 
ATOM   17714 C C     . ASP A 1 3946 ? 156.624 181.591 210.590 1.00 37.18 ? 3946 ASP A C     1 
ATOM   17715 O O     . ASP A 1 3946 ? 156.891 180.604 211.275 1.00 36.49 ? 3946 ASP A O     1 
ATOM   17716 C CB    . ASP A 1 3946 ? 154.906 180.355 209.217 1.00 33.59 ? 3946 ASP A CB    1 
ATOM   17717 C CG    . ASP A 1 3946 ? 154.039 180.386 207.974 1.00 35.02 ? 3946 ASP A CG    1 
ATOM   17718 O OD1   . ASP A 1 3946 ? 153.850 181.482 207.406 1.00 34.88 ? 3946 ASP A OD1   1 
ATOM   17719 O OD2   . ASP A 1 3946 ? 153.547 179.314 207.564 1.00 37.40 ? 3946 ASP A OD2   1 
ATOM   17720 N N     . LEU A 1 3947 ? 156.913 182.825 210.980 1.00 32.97 ? 3947 LEU A N     1 
ATOM   17721 C CA    . LEU A 1 3947 ? 157.514 183.097 212.279 1.00 32.96 ? 3947 LEU A CA    1 
ATOM   17722 C C     . LEU A 1 3947 ? 156.731 184.114 213.090 1.00 33.61 ? 3947 LEU A C     1 
ATOM   17723 O O     . LEU A 1 3947 ? 156.656 183.988 214.313 1.00 32.83 ? 3947 LEU A O     1 
ATOM   17724 C CB    . LEU A 1 3947 ? 158.967 183.564 212.099 1.00 31.69 ? 3947 LEU A CB    1 
ATOM   17725 C CG    . LEU A 1 3947 ? 159.809 183.780 213.358 1.00 35.66 ? 3947 LEU A CG    1 
ATOM   17726 C CD1   . LEU A 1 3947 ? 159.886 182.501 214.166 1.00 32.69 ? 3947 LEU A CD1   1 
ATOM   17727 C CD2   . LEU A 1 3947 ? 161.207 184.226 212.970 1.00 35.15 ? 3947 LEU A CD2   1 
ATOM   17728 N N     . ILE A 1 3948 ? 156.147 185.124 212.441 1.00 35.50 ? 3948 ILE A N     1 
ATOM   17729 C CA    . ILE A 1 3948 ? 155.218 186.020 213.124 1.00 34.84 ? 3948 ILE A CA    1 
ATOM   17730 C C     . ILE A 1 3948 ? 153.933 185.281 213.484 1.00 37.43 ? 3948 ILE A C     1 
ATOM   17731 O O     . ILE A 1 3948 ? 153.423 185.386 214.607 1.00 35.29 ? 3948 ILE A O     1 
ATOM   17732 C CB    . ILE A 1 3948 ? 154.929 187.254 212.250 1.00 35.28 ? 3948 ILE A CB    1 
ATOM   17733 C CG1   . ILE A 1 3948 ? 156.219 188.013 211.942 1.00 34.12 ? 3948 ILE A CG1   1 
ATOM   17734 C CG2   . ILE A 1 3948 ? 153.934 188.175 212.933 1.00 35.73 ? 3948 ILE A CG2   1 
ATOM   17735 C CD1   . ILE A 1 3948 ? 156.911 188.539 213.169 1.00 33.46 ? 3948 ILE A CD1   1 
ATOM   17736 N N     . ALA A 1 3949 ? 153.390 184.522 212.530 1.00 37.95 ? 3949 ALA A N     1 
ATOM   17737 C CA    . ALA A 1 3949 ? 152.137 183.814 212.771 1.00 38.01 ? 3949 ALA A CA    1 
ATOM   17738 C C     . ALA A 1 3949 ? 152.288 182.784 213.882 1.00 38.11 ? 3949 ALA A C     1 
ATOM   17739 O O     . ALA A 1 3949 ? 151.394 182.631 214.722 1.00 40.18 ? 3949 ALA A O     1 
ATOM   17740 C CB    . ALA A 1 3949 ? 151.655 183.149 211.483 1.00 34.86 ? 3949 ALA A CB    1 
ATOM   17741 N N     . LYS A 1 3950 ? 153.414 182.069 213.906 1.00 35.42 ? 3950 LYS A N     1 
ATOM   17742 C CA    . LYS A 1 3950 ? 153.594 181.030 214.914 1.00 34.99 ? 3950 LYS A CA    1 
ATOM   17743 C C     . LYS A 1 3950 ? 153.903 181.626 216.282 1.00 35.51 ? 3950 LYS A C     1 
ATOM   17744 O O     . LYS A 1 3950 ? 153.549 181.040 217.312 1.00 36.56 ? 3950 LYS A O     1 
ATOM   17745 C CB    . LYS A 1 3950 ? 154.688 180.053 214.482 1.00 34.68 ? 3950 LYS A CB    1 
ATOM   17746 C CG    . LYS A 1 3950 ? 154.291 179.187 213.294 1.00 37.09 ? 3950 LYS A CG    1 
ATOM   17747 C CD    . LYS A 1 3950 ? 155.442 178.326 212.803 1.00 36.36 ? 3950 LYS A CD    1 
ATOM   17748 C CE    . LYS A 1 3950 ? 155.767 177.220 213.791 1.00 35.28 ? 3950 LYS A CE    1 
ATOM   17749 N NZ    . LYS A 1 3950 ? 156.814 176.300 213.267 1.00 35.17 ? 3950 LYS A NZ    1 
ATOM   17750 N N     . VAL A 1 3951 ? 154.559 182.791 216.322 1.00 33.71 ? 3951 VAL A N     1 
ATOM   17751 C CA    . VAL A 1 3951 ? 154.805 183.433 217.612 1.00 36.73 ? 3951 VAL A CA    1 
ATOM   17752 C C     . VAL A 1 3951 ? 153.563 184.145 218.122 1.00 37.37 ? 3951 VAL A C     1 
ATOM   17753 O O     . VAL A 1 3951 ? 153.484 184.457 219.318 1.00 34.01 ? 3951 VAL A O     1 
ATOM   17754 C CB    . VAL A 1 3951 ? 155.987 184.424 217.550 1.00 36.07 ? 3951 VAL A CB    1 
ATOM   17755 C CG1   . VAL A 1 3951 ? 155.657 185.628 216.693 1.00 35.46 ? 3951 VAL A CG1   1 
ATOM   17756 C CG2   . VAL A 1 3951 ? 156.444 184.840 218.943 1.00 33.92 ? 3951 VAL A CG2   1 
ATOM   17757 N N     . GLN A 1 3952 ? 152.577 184.392 217.255 1.00 38.35 ? 3952 GLN A N     1 
ATOM   17758 C CA    . GLN A 1 3952 ? 151.307 184.940 217.724 1.00 39.65 ? 3952 GLN A CA    1 
ATOM   17759 C C     . GLN A 1 3952 ? 150.662 184.014 218.749 1.00 40.36 ? 3952 GLN A C     1 
ATOM   17760 O O     . GLN A 1 3952 ? 150.176 184.464 219.793 1.00 38.90 ? 3952 GLN A O     1 
ATOM   17761 C CB    . GLN A 1 3952 ? 150.364 185.172 216.543 1.00 36.63 ? 3952 GLN A CB    1 
ATOM   17762 C CG    . GLN A 1 3952 ? 148.955 185.589 216.945 1.00 37.85 ? 3952 GLN A CG    1 
ATOM   17763 C CD    . GLN A 1 3952 ? 148.943 186.690 217.992 1.00 40.84 ? 3952 GLN A CD    1 
ATOM   17764 O OE1   . GLN A 1 3952 ? 149.632 187.701 217.856 1.00 41.05 ? 3952 GLN A OE1   1 
ATOM   17765 N NE2   . GLN A 1 3952 ? 148.162 186.493 219.047 1.00 38.87 ? 3952 GLN A NE2   1 
ATOM   17766 N N     . ALA A 1 3953 ? 150.653 182.714 218.468 1.00 36.05 ? 3953 ALA A N     1 
ATOM   17767 C CA    . ALA A 1 3953 ? 150.161 181.723 219.414 1.00 37.29 ? 3953 ALA A CA    1 
ATOM   17768 C C     . ALA A 1 3953 ? 151.293 181.335 220.365 1.00 36.75 ? 3953 ALA A C     1 
ATOM   17769 O O     . ALA A 1 3953 ? 152.343 181.983 220.413 1.00 33.80 ? 3953 ALA A O     1 
ATOM   17770 C CB    . ALA A 1 3953 ? 149.591 180.518 218.671 1.00 35.75 ? 3953 ALA A CB    1 
ATOM   17771 N N     . ASP A 1 3954 ? 151.085 180.265 221.136 1.00 42.55 ? 3954 ASP A N     1 
ATOM   17772 C CA    . ASP A 1 3954 ? 152.077 179.744 222.077 1.00 43.57 ? 3954 ASP A CA    1 
ATOM   17773 C C     . ASP A 1 3954 ? 152.462 180.810 223.109 1.00 39.70 ? 3954 ASP A C     1 
ATOM   17774 O O     . ASP A 1 3954 ? 153.582 181.324 223.142 1.00 37.27 ? 3954 ASP A O     1 
ATOM   17775 C CB    . ASP A 1 3954 ? 153.311 179.211 221.337 1.00 41.37 ? 3954 ASP A CB    1 
ATOM   17776 C CG    . ASP A 1 3954 ? 154.276 178.489 222.257 1.00 41.94 ? 3954 ASP A CG    1 
ATOM   17777 O OD1   . ASP A 1 3954 ? 153.976 177.345 222.658 1.00 41.23 ? 3954 ASP A OD1   1 
ATOM   17778 O OD2   . ASP A 1 3954 ? 155.337 179.065 222.578 1.00 42.54 ? 3954 ASP A OD2   1 
ATOM   17779 N N     . GLU A 1 3955 ? 151.474 181.140 223.948 1.00 38.90 ? 3955 GLU A N     1 
ATOM   17780 C CA    . GLU A 1 3955 ? 151.660 182.132 225.004 1.00 39.75 ? 3955 GLU A CA    1 
ATOM   17781 C C     . GLU A 1 3955 ? 152.842 181.818 225.915 1.00 42.28 ? 3955 GLU A C     1 
ATOM   17782 O O     . GLU A 1 3955 ? 153.304 182.704 226.643 1.00 39.03 ? 3955 GLU A O     1 
ATOM   17783 C CB    . GLU A 1 3955 ? 150.376 182.250 225.830 1.00 40.55 ? 3955 GLU A CB    1 
ATOM   17784 C CG    . GLU A 1 3955 ? 149.824 180.919 226.325 1.00 41.42 ? 3955 GLU A CG    1 
ATOM   17785 C CD    . GLU A 1 3955 ? 150.421 180.486 227.650 1.00 41.62 ? 3955 GLU A CD    1 
ATOM   17786 O OE1   . GLU A 1 3955 ? 150.953 181.350 228.378 1.00 39.40 ? 3955 GLU A OE1   1 
ATOM   17787 O OE2   . GLU A 1 3955 ? 150.357 179.278 227.963 1.00 39.50 ? 3955 GLU A OE2   1 
ATOM   17788 N N     . GLN A 1 3956 ? 153.343 180.581 225.892 1.00 42.33 ? 3956 GLN A N     1 
ATOM   17789 C CA    . GLN A 1 3956 ? 154.548 180.219 226.628 1.00 42.17 ? 3956 GLN A CA    1 
ATOM   17790 C C     . GLN A 1 3956 ? 155.798 180.883 226.059 1.00 40.60 ? 3956 GLN A C     1 
ATOM   17791 O O     . GLN A 1 3956 ? 156.861 180.815 226.689 1.00 39.89 ? 3956 GLN A O     1 
ATOM   17792 C CB    . GLN A 1 3956 ? 154.702 178.693 226.631 1.00 39.81 ? 3956 GLN A CB    1 
ATOM   17793 C CG    . GLN A 1 3956 ? 155.711 178.135 227.629 1.00 37.98 ? 3956 GLN A CG    1 
ATOM   17794 C CD    . GLN A 1 3956 ? 157.075 177.891 227.011 1.00 40.02 ? 3956 GLN A CD    1 
ATOM   17795 O OE1   . GLN A 1 3956 ? 157.186 177.571 225.828 1.00 40.11 ? 3956 GLN A OE1   1 
ATOM   17796 N NE2   . GLN A 1 3956 ? 158.123 178.042 227.813 1.00 39.78 ? 3956 GLN A NE2   1 
ATOM   17797 N N     . PHE A 1 3957 ? 155.696 181.514 224.885 1.00 34.11 ? 3957 PHE A N     1 
ATOM   17798 C CA    . PHE A 1 3957 ? 156.865 182.131 224.269 1.00 34.39 ? 3957 PHE A CA    1 
ATOM   17799 C C     . PHE A 1 3957 ? 157.430 183.246 225.138 1.00 34.96 ? 3957 PHE A C     1 
ATOM   17800 O O     . PHE A 1 3957 ? 158.651 183.398 225.240 1.00 36.34 ? 3957 PHE A O     1 
ATOM   17801 C CB    . PHE A 1 3957 ? 156.517 182.666 222.882 1.00 31.79 ? 3957 PHE A CB    1 
ATOM   17802 C CG    . PHE A 1 3957 ? 157.607 183.494 222.268 1.00 31.77 ? 3957 PHE A CG    1 
ATOM   17803 C CD1   . PHE A 1 3957 ? 158.709 182.889 221.688 1.00 30.49 ? 3957 PHE A CD1   1 
ATOM   17804 C CD2   . PHE A 1 3957 ? 157.536 184.876 222.278 1.00 34.10 ? 3957 PHE A CD2   1 
ATOM   17805 C CE1   . PHE A 1 3957 ? 159.715 183.645 221.126 1.00 30.42 ? 3957 PHE A CE1   1 
ATOM   17806 C CE2   . PHE A 1 3957 ? 158.541 185.639 221.717 1.00 34.40 ? 3957 PHE A CE2   1 
ATOM   17807 C CZ    . PHE A 1 3957 ? 159.631 185.022 221.140 1.00 32.54 ? 3957 PHE A CZ    1 
ATOM   17808 N N     . GLY A 1 3958 ? 156.563 184.052 225.752 1.00 32.31 ? 3958 GLY A N     1 
ATOM   17809 C CA    . GLY A 1 3958 ? 157.051 185.104 226.631 1.00 32.40 ? 3958 GLY A CA    1 
ATOM   17810 C C     . GLY A 1 3958 ? 157.790 184.559 227.839 1.00 30.47 ? 3958 GLY A C     1 
ATOM   17811 O O     . GLY A 1 3958 ? 158.844 185.076 228.223 1.00 27.08 ? 3958 GLY A O     1 
ATOM   17812 N N     . ILE A 1 3959 ? 157.250 183.501 228.449 1.00 33.75 ? 3959 ILE A N     1 
ATOM   17813 C CA    . ILE A 1 3959 ? 157.914 182.875 229.587 1.00 34.31 ? 3959 ILE A CA    1 
ATOM   17814 C C     . ILE A 1 3959 ? 159.266 182.321 229.167 1.00 34.98 ? 3959 ILE A C     1 
ATOM   17815 O O     . ILE A 1 3959 ? 160.259 182.443 229.896 1.00 34.44 ? 3959 ILE A O     1 
ATOM   17816 C CB    . ILE A 1 3959 ? 157.020 181.780 230.202 1.00 34.21 ? 3959 ILE A CB    1 
ATOM   17817 C CG1   . ILE A 1 3959 ? 155.722 182.374 230.758 1.00 34.44 ? 3959 ILE A CG1   1 
ATOM   17818 C CG2   . ILE A 1 3959 ? 157.768 181.026 231.290 1.00 32.21 ? 3959 ILE A CG2   1 
ATOM   17819 C CD1   . ILE A 1 3959 ? 154.580 182.433 229.762 1.00 35.72 ? 3959 ILE A CD1   1 
ATOM   17820 N N     . TRP A 1 3960 ? 159.329 181.701 227.987 1.00 29.62 ? 3960 TRP A N     1 
ATOM   17821 C CA    . TRP A 1 3960 ? 160.606 181.191 227.496 1.00 30.04 ? 3960 TRP A CA    1 
ATOM   17822 C C     . TRP A 1 3960 ? 161.589 182.326 227.243 1.00 31.53 ? 3960 TRP A C     1 
ATOM   17823 O O     . TRP A 1 3960 ? 162.785 182.200 227.528 1.00 31.80 ? 3960 TRP A O     1 
ATOM   17824 C CB    . TRP A 1 3960 ? 160.401 180.375 226.221 1.00 28.83 ? 3960 TRP A CB    1 
ATOM   17825 C CG    . TRP A 1 3960 ? 161.692 180.031 225.549 1.00 29.10 ? 3960 TRP A CG    1 
ATOM   17826 C CD1   . TRP A 1 3960 ? 162.514 178.989 225.850 1.00 29.08 ? 3960 TRP A CD1   1 
ATOM   17827 C CD2   . TRP A 1 3960 ? 162.318 180.739 224.474 1.00 25.74 ? 3960 TRP A CD2   1 
ATOM   17828 N NE1   . TRP A 1 3960 ? 163.611 178.997 225.024 1.00 28.31 ? 3960 TRP A NE1   1 
ATOM   17829 C CE2   . TRP A 1 3960 ? 163.516 180.064 224.171 1.00 26.83 ? 3960 TRP A CE2   1 
ATOM   17830 C CE3   . TRP A 1 3960 ? 161.982 181.877 223.736 1.00 29.37 ? 3960 TRP A CE3   1 
ATOM   17831 C CZ2   . TRP A 1 3960 ? 164.377 180.486 223.164 1.00 27.61 ? 3960 TRP A CZ2   1 
ATOM   17832 C CZ3   . TRP A 1 3960 ? 162.838 182.294 222.736 1.00 28.02 ? 3960 TRP A CZ3   1 
ATOM   17833 C CH2   . TRP A 1 3960 ? 164.021 181.600 222.459 1.00 23.20 ? 3960 TRP A CH2   1 
ATOM   17834 N N     . LEU A 1 3961 ? 161.101 183.442 226.701 1.00 28.49 ? 3961 LEU A N     1 
ATOM   17835 C CA    . LEU A 1 3961 ? 161.963 184.586 226.436 1.00 29.27 ? 3961 LEU A CA    1 
ATOM   17836 C C     . LEU A 1 3961 ? 162.515 185.177 227.725 1.00 30.82 ? 3961 LEU A C     1 
ATOM   17837 O O     . LEU A 1 3961 ? 163.664 185.633 227.758 1.00 30.64 ? 3961 LEU A O     1 
ATOM   17838 C CB    . LEU A 1 3961 ? 161.189 185.643 225.648 1.00 28.63 ? 3961 LEU A CB    1 
ATOM   17839 C CG    . LEU A 1 3961 ? 161.993 186.703 224.899 1.00 29.45 ? 3961 LEU A CG    1 
ATOM   17840 C CD1   . LEU A 1 3961 ? 163.201 186.084 224.222 1.00 28.85 ? 3961 LEU A CD1   1 
ATOM   17841 C CD2   . LEU A 1 3961 ? 161.106 187.398 223.882 1.00 27.40 ? 3961 LEU A CD2   1 
ATOM   17842 N N     . ASP A 1 3962 ? 161.722 185.173 228.793 1.00 27.36 ? 3962 ASP A N     1 
ATOM   17843 C CA    . ASP A 1 3962 ? 162.177 185.656 230.089 1.00 26.71 ? 3962 ASP A CA    1 
ATOM   17844 C C     . ASP A 1 3962 ? 162.926 184.598 230.890 1.00 28.25 ? 3962 ASP A C     1 
ATOM   17845 O O     . ASP A 1 3962 ? 163.364 184.886 232.008 1.00 29.72 ? 3962 ASP A O     1 
ATOM   17846 C CB    . ASP A 1 3962 ? 160.991 186.175 230.906 1.00 31.32 ? 3962 ASP A CB    1 
ATOM   17847 C CG    . ASP A 1 3962 ? 160.402 187.447 230.332 1.00 33.14 ? 3962 ASP A CG    1 
ATOM   17848 O OD1   . ASP A 1 3962 ? 161.154 188.219 229.702 1.00 30.48 ? 3962 ASP A OD1   1 
ATOM   17849 O OD2   . ASP A 1 3962 ? 159.187 187.677 230.513 1.00 34.75 ? 3962 ASP A OD2   1 
ATOM   17850 N N     . SER A 1 3963 ? 163.079 183.389 230.354 1.00 27.35 ? 3963 SER A N     1 
ATOM   17851 C CA    . SER A 1 3963 ? 163.795 182.337 231.062 1.00 27.65 ? 3963 SER A CA    1 
ATOM   17852 C C     . SER A 1 3963 ? 165.272 182.686 231.197 1.00 22.64 ? 3963 SER A C     1 
ATOM   17853 O O     . SER A 1 3963 ? 165.864 183.334 230.330 1.00 24.52 ? 3963 SER A O     1 
ATOM   17854 C CB    . SER A 1 3963 ? 163.641 181.000 230.338 1.00 26.71 ? 3963 SER A CB    1 
ATOM   17855 O OG    . SER A 1 3963 ? 164.329 179.969 231.024 1.00 27.72 ? 3963 SER A OG    1 
ATOM   17856 N N     . SER A 1 3964 ? 165.867 182.249 232.311 1.00 21.10 ? 3964 SER A N     1 
ATOM   17857 C CA    . SER A 1 3964 ? 167.267 182.563 232.576 1.00 23.49 ? 3964 SER A CA    1 
ATOM   17858 C C     . SER A 1 3964 ? 168.186 181.933 231.537 1.00 23.03 ? 3964 SER A C     1 
ATOM   17859 O O     . SER A 1 3964 ? 169.108 182.586 231.034 1.00 20.80 ? 3964 SER A O     1 
ATOM   17860 C CB    . SER A 1 3964 ? 167.649 182.098 233.980 1.00 23.50 ? 3964 SER A CB    1 
ATOM   17861 O OG    . SER A 1 3964 ? 167.382 180.716 234.147 1.00 25.76 ? 3964 SER A OG    1 
ATOM   17862 N N     . SER A 1 3965 ? 167.952 180.665 231.204 1.00 26.35 ? 3965 SER A N     1 
ATOM   17863 C CA    . SER A 1 3965 ? 168.731 179.942 230.199 1.00 23.08 ? 3965 SER A CA    1 
ATOM   17864 C C     . SER A 1 3965 ? 167.760 179.297 229.221 1.00 17.96 ? 3965 SER A C     1 
ATOM   17865 O O     . SER A 1 3965 ? 167.431 178.109 229.344 1.00 19.56 ? 3965 SER A O     1 
ATOM   17866 C CB    . SER A 1 3965 ? 169.646 178.901 230.844 1.00 24.22 ? 3965 SER A CB    1 
ATOM   17867 O OG    . SER A 1 3965 ? 168.896 177.918 231.535 1.00 28.70 ? 3965 SER A OG    1 
ATOM   17868 N N     . PRO A 1 3966 ? 167.280 180.050 228.233 1.00 21.18 ? 3966 PRO A N     1 
ATOM   17869 C CA    . PRO A 1 3966 ? 166.294 179.546 227.272 1.00 24.72 ? 3966 PRO A CA    1 
ATOM   17870 C C     . PRO A 1 3966 ? 166.925 178.794 226.104 1.00 27.50 ? 3966 PRO A C     1 
ATOM   17871 O O     . PRO A 1 3966 ? 166.513 178.936 224.952 1.00 26.67 ? 3966 PRO A O     1 
ATOM   17872 C CB    . PRO A 1 3966 ? 165.600 180.834 226.817 1.00 26.59 ? 3966 PRO A CB    1 
ATOM   17873 C CG    . PRO A 1 3966 ? 166.602 181.981 227.296 1.00 24.64 ? 3966 PRO A CG    1 
ATOM   17874 C CD    . PRO A 1 3966 ? 167.858 181.240 227.615 1.00 25.35 ? 3966 PRO A CD    1 
ATOM   17875 N N     . GLU A 1 3967 ? 167.933 177.983 226.408 1.00 28.23 ? 3967 GLU A N     1 
ATOM   17876 C CA    . GLU A 1 3967 ? 168.552 177.108 225.426 1.00 24.20 ? 3967 GLU A CA    1 
ATOM   17877 C C     . GLU A 1 3967 ? 168.414 175.634 225.764 1.00 23.91 ? 3967 GLU A C     1 
ATOM   17878 O O     . GLU A 1 3967 ? 168.564 174.802 224.861 1.00 25.65 ? 3967 GLU A O     1 
ATOM   17879 C CB    . GLU A 1 3967 ? 170.041 177.453 225.261 1.00 20.80 ? 3967 GLU A CB    1 
ATOM   17880 C CG    . GLU A 1 3967 ? 170.912 177.051 226.438 1.00 23.97 ? 3967 GLU A CG    1 
ATOM   17881 C CD    . GLU A 1 3967 ? 171.132 178.178 227.422 1.00 26.40 ? 3967 GLU A CD    1 
ATOM   17882 O OE1   . GLU A 1 3967 ? 170.394 179.180 227.356 1.00 29.27 ? 3967 GLU A OE1   1 
ATOM   17883 O OE2   . GLU A 1 3967 ? 172.041 178.059 228.270 1.00 24.47 ? 3967 GLU A OE2   1 
ATOM   17884 N N     . GLN A 1 3968 ? 168.132 175.281 227.020 1.00 21.19 ? 3968 GLN A N     1 
ATOM   17885 C CA    . GLN A 1 3968 ? 167.816 173.896 227.345 1.00 27.12 ? 3968 GLN A CA    1 
ATOM   17886 C C     . GLN A 1 3968 ? 166.547 173.448 226.632 1.00 29.67 ? 3968 GLN A C     1 
ATOM   17887 O O     . GLN A 1 3968 ? 166.484 172.335 226.097 1.00 30.47 ? 3968 GLN A O     1 
ATOM   17888 C CB    . GLN A 1 3968 ? 167.666 173.733 228.858 1.00 28.73 ? 3968 GLN A CB    1 
ATOM   17889 C CG    . GLN A 1 3968 ? 168.936 174.007 229.649 1.00 29.54 ? 3968 GLN A CG    1 
ATOM   17890 C CD    . GLN A 1 3968 ? 170.180 173.481 228.963 1.00 29.92 ? 3968 GLN A CD    1 
ATOM   17891 O OE1   . GLN A 1 3968 ? 170.302 172.284 228.704 1.00 28.44 ? 3968 GLN A OE1   1 
ATOM   17892 N NE2   . GLN A 1 3968 ? 171.116 174.376 228.669 1.00 29.83 ? 3968 GLN A NE2   1 
ATOM   17893 N N     . THR A 1 3969 ? 165.526 174.301 226.617 1.00 26.40 ? 3969 THR A N     1 
ATOM   17894 C CA    . THR A 1 3969 ? 164.287 174.043 225.897 1.00 26.70 ? 3969 THR A CA    1 
ATOM   17895 C C     . THR A 1 3969 ? 163.979 175.244 225.016 1.00 26.22 ? 3969 THR A C     1 
ATOM   17896 O O     . THR A 1 3969 ? 163.892 176.371 225.511 1.00 28.17 ? 3969 THR A O     1 
ATOM   17897 C CB    . THR A 1 3969 ? 163.122 173.780 226.857 1.00 31.22 ? 3969 THR A CB    1 
ATOM   17898 O OG1   . THR A 1 3969 ? 162.908 174.934 227.680 1.00 28.92 ? 3969 THR A OG1   1 
ATOM   17899 C CG2   . THR A 1 3969 ? 163.418 172.578 227.743 1.00 29.83 ? 3969 THR A CG2   1 
ATOM   17900 N N     . VAL A 1 3970 ? 163.811 175.001 223.721 1.00 23.46 ? 3970 VAL A N     1 
ATOM   17901 C CA    . VAL A 1 3970 ? 163.548 176.066 222.757 1.00 23.77 ? 3970 VAL A CA    1 
ATOM   17902 C C     . VAL A 1 3970 ? 162.264 175.732 222.007 1.00 27.79 ? 3970 VAL A C     1 
ATOM   17903 O O     . VAL A 1 3970 ? 162.097 174.591 221.551 1.00 25.10 ? 3970 VAL A O     1 
ATOM   17904 C CB    . VAL A 1 3970 ? 164.731 176.247 221.792 1.00 23.83 ? 3970 VAL A CB    1 
ATOM   17905 C CG1   . VAL A 1 3970 ? 164.343 177.133 220.622 1.00 22.08 ? 3970 VAL A CG1   1 
ATOM   17906 C CG2   . VAL A 1 3970 ? 165.933 176.819 222.524 1.00 21.57 ? 3970 VAL A CG2   1 
ATOM   17907 N N     . PRO A 1 3971 ? 161.333 176.675 221.863 1.00 30.04 ? 3971 PRO A N     1 
ATOM   17908 C CA    . PRO A 1 3971 ? 160.094 176.379 221.136 1.00 31.37 ? 3971 PRO A CA    1 
ATOM   17909 C C     . PRO A 1 3971 ? 160.364 176.054 219.675 1.00 29.49 ? 3971 PRO A C     1 
ATOM   17910 O O     . PRO A 1 3971 ? 161.318 176.546 219.070 1.00 28.90 ? 3971 PRO A O     1 
ATOM   17911 C CB    . PRO A 1 3971 ? 159.279 177.670 221.281 1.00 30.77 ? 3971 PRO A CB    1 
ATOM   17912 C CG    . PRO A 1 3971 ? 160.292 178.729 221.563 1.00 26.43 ? 3971 PRO A CG    1 
ATOM   17913 C CD    . PRO A 1 3971 ? 161.359 178.057 222.368 1.00 25.42 ? 3971 PRO A CD    1 
ATOM   17914 N N     . TYR A 1 3972 ? 159.508 175.204 219.113 1.00 32.34 ? 3972 TYR A N     1 
ATOM   17915 C CA    . TYR A 1 3972 ? 159.614 174.818 217.711 1.00 31.33 ? 3972 TYR A CA    1 
ATOM   17916 C C     . TYR A 1 3972 ? 158.954 175.893 216.859 1.00 33.13 ? 3972 TYR A C     1 
ATOM   17917 O O     . TYR A 1 3972 ? 157.724 176.001 216.826 1.00 34.32 ? 3972 TYR A O     1 
ATOM   17918 C CB    . TYR A 1 3972 ? 158.965 173.457 217.477 1.00 32.70 ? 3972 TYR A CB    1 
ATOM   17919 C CG    . TYR A 1 3972 ? 159.690 172.300 218.129 1.00 36.29 ? 3972 TYR A CG    1 
ATOM   17920 C CD1   . TYR A 1 3972 ? 160.985 172.446 218.608 1.00 36.35 ? 3972 TYR A CD1   1 
ATOM   17921 C CD2   . TYR A 1 3972 ? 159.079 171.060 218.263 1.00 36.76 ? 3972 TYR A CD2   1 
ATOM   17922 C CE1   . TYR A 1 3972 ? 161.650 171.391 219.204 1.00 35.00 ? 3972 TYR A CE1   1 
ATOM   17923 C CE2   . TYR A 1 3972 ? 159.736 169.999 218.856 1.00 34.87 ? 3972 TYR A CE2   1 
ATOM   17924 C CZ    . TYR A 1 3972 ? 161.021 170.170 219.325 1.00 34.17 ? 3972 TYR A CZ    1 
ATOM   17925 O OH    . TYR A 1 3972 ? 161.680 169.117 219.917 1.00 33.25 ? 3972 TYR A OH    1 
ATOM   17926 N N     . LEU A 1 3973 ? 159.766 176.692 216.171 1.00 31.20 ? 3973 LEU A N     1 
ATOM   17927 C CA    . LEU A 1 3973 ? 159.261 177.779 215.345 1.00 32.43 ? 3973 LEU A CA    1 
ATOM   17928 C C     . LEU A 1 3973 ? 159.612 177.642 213.873 1.00 32.60 ? 3973 LEU A C     1 
ATOM   17929 O O     . LEU A 1 3973 ? 158.998 178.314 213.043 1.00 33.40 ? 3973 LEU A O     1 
ATOM   17930 C CB    . LEU A 1 3973 ? 159.786 179.125 215.860 1.00 32.08 ? 3973 LEU A CB    1 
ATOM   17931 C CG    . LEU A 1 3973 ? 159.280 179.528 217.246 1.00 33.72 ? 3973 LEU A CG    1 
ATOM   17932 C CD1   . LEU A 1 3973 ? 159.963 180.799 217.719 1.00 33.14 ? 3973 LEU A CD1   1 
ATOM   17933 C CD2   . LEU A 1 3973 ? 157.768 179.694 217.244 1.00 31.97 ? 3973 LEU A CD2   1 
ATOM   17934 N N     . TRP A 1 3974 ? 160.579 176.796 213.530 1.00 28.85 ? 3974 TRP A N     1 
ATOM   17935 C CA    . TRP A 1 3974 ? 160.887 176.546 212.129 1.00 30.46 ? 3974 TRP A CA    1 
ATOM   17936 C C     . TRP A 1 3974 ? 159.797 175.695 211.490 1.00 30.68 ? 3974 TRP A C     1 
ATOM   17937 O O     . TRP A 1 3974 ? 159.210 174.821 212.134 1.00 30.83 ? 3974 TRP A O     1 
ATOM   17938 C CB    . TRP A 1 3974 ? 162.243 175.856 211.996 1.00 28.47 ? 3974 TRP A CB    1 
ATOM   17939 C CG    . TRP A 1 3974 ? 162.354 174.584 212.776 1.00 26.08 ? 3974 TRP A CG    1 
ATOM   17940 C CD1   . TRP A 1 3974 ? 162.042 173.328 212.345 1.00 29.20 ? 3974 TRP A CD1   1 
ATOM   17941 C CD2   . TRP A 1 3974 ? 162.825 174.441 214.121 1.00 26.01 ? 3974 TRP A CD2   1 
ATOM   17942 N NE1   . TRP A 1 3974 ? 162.282 172.412 213.340 1.00 32.98 ? 3974 TRP A NE1   1 
ATOM   17943 C CE2   . TRP A 1 3974 ? 162.764 173.070 214.441 1.00 28.09 ? 3974 TRP A CE2   1 
ATOM   17944 C CE3   . TRP A 1 3974 ? 163.288 175.339 215.086 1.00 26.54 ? 3974 TRP A CE3   1 
ATOM   17945 C CZ2   . TRP A 1 3974 ? 163.149 172.577 215.685 1.00 27.45 ? 3974 TRP A CZ2   1 
ATOM   17946 C CZ3   . TRP A 1 3974 ? 163.670 174.846 216.320 1.00 27.04 ? 3974 TRP A CZ3   1 
ATOM   17947 C CH2   . TRP A 1 3974 ? 163.599 173.479 216.608 1.00 27.34 ? 3974 TRP A CH2   1 
ATOM   17948 N N     . SER A 1 3975 ? 159.525 175.958 210.211 1.00 29.90 ? 3975 SER A N     1 
ATOM   17949 C CA    . SER A 1 3975 ? 158.469 175.256 209.481 1.00 30.06 ? 3975 SER A CA    1 
ATOM   17950 C C     . SER A 1 3975 ? 159.092 174.110 208.689 1.00 32.48 ? 3975 SER A C     1 
ATOM   17951 O O     . SER A 1 3975 ? 159.395 174.219 207.499 1.00 30.99 ? 3975 SER A O     1 
ATOM   17952 C CB    . SER A 1 3975 ? 157.711 176.221 208.578 1.00 31.73 ? 3975 SER A CB    1 
ATOM   17953 O OG    . SER A 1 3975 ? 158.590 176.864 207.672 1.00 32.29 ? 3975 SER A OG    1 
ATOM   17954 N N     . GLU A 1 3976 ? 159.286 172.987 209.376 1.00 37.68 ? 3976 GLU A N     1 
ATOM   17955 C CA    . GLU A 1 3976 ? 159.802 171.768 208.771 1.00 39.03 ? 3976 GLU A CA    1 
ATOM   17956 C C     . GLU A 1 3976 ? 158.932 170.589 209.183 1.00 40.34 ? 3976 GLU A C     1 
ATOM   17957 O O     . GLU A 1 3976 ? 158.552 170.465 210.352 1.00 39.29 ? 3976 GLU A O     1 
ATOM   17958 C CB    . GLU A 1 3976 ? 161.257 171.515 209.181 1.00 38.11 ? 3976 GLU A CB    1 
ATOM   17959 C CG    . GLU A 1 3976 ? 162.234 172.581 208.708 1.00 40.23 ? 3976 GLU A CG    1 
ATOM   17960 C CD    . GLU A 1 3976 ? 162.418 172.585 207.204 1.00 37.48 ? 3976 GLU A CD    1 
ATOM   17961 O OE1   . GLU A 1 3976 ? 162.321 171.503 206.588 1.00 37.92 ? 3976 GLU A OE1   1 
ATOM   17962 O OE2   . GLU A 1 3976 ? 162.663 173.670 206.636 1.00 33.47 ? 3976 GLU A OE2   1 
ATOM   17963 N N     . GLU A 1 3977 ? 158.618 169.724 208.218 1.00 45.31 ? 3977 GLU A N     1 
ATOM   17964 C CA    . GLU A 1 3977 ? 157.784 168.552 208.463 1.00 46.15 ? 3977 GLU A CA    1 
ATOM   17965 C C     . GLU A 1 3977 ? 158.613 167.279 208.607 1.00 46.12 ? 3977 GLU A C     1 
ATOM   17966 O O     . GLU A 1 3977 ? 158.553 166.605 209.639 1.00 44.84 ? 3977 GLU A O     1 
ATOM   17967 C CB    . GLU A 1 3977 ? 156.762 168.391 207.328 1.00 44.53 ? 3977 GLU A CB    1 
ATOM   17968 C CG    . GLU A 1 3977 ? 155.736 169.508 207.243 1.00 44.89 ? 3977 GLU A CG    1 
ATOM   17969 C CD    . GLU A 1 3977 ? 154.785 169.336 206.073 1.00 47.13 ? 3977 GLU A CD    1 
ATOM   17970 O OE1   . GLU A 1 3977 ? 154.999 168.409 205.263 1.00 48.67 ? 3977 GLU A OE1   1 
ATOM   17971 O OE2   . GLU A 1 3977 ? 153.827 170.128 205.962 1.00 45.66 ? 3977 GLU A OE2   1 
ATOM   17972 N N     . THR A 1 3978 ? 159.391 166.940 207.583 1.00 41.18 ? 3978 THR A N     1 
ATOM   17973 C CA    . THR A 1 3978 ? 160.162 165.702 207.562 1.00 40.92 ? 3978 THR A CA    1 
ATOM   17974 C C     . THR A 1 3978 ? 161.468 165.751 208.361 1.00 39.79 ? 3978 THR A C     1 
ATOM   17975 O O     . THR A 1 3978 ? 161.775 164.771 209.052 1.00 37.61 ? 3978 THR A O     1 
ATOM   17976 C CB    . THR A 1 3978 ? 160.449 165.281 206.115 1.00 41.42 ? 3978 THR A CB    1 
ATOM   17977 O OG1   . THR A 1 3978 ? 161.218 166.288 205.447 1.00 40.38 ? 3978 THR A OG1   1 
ATOM   17978 C CG2   . THR A 1 3978 ? 159.147 165.060 205.358 1.00 39.55 ? 3978 THR A CG2   1 
ATOM   17979 N N     . PRO A 1 3979 ? 162.269 166.822 208.305 1.00 39.42 ? 3979 PRO A N     1 
ATOM   17980 C CA    . PRO A 1 3979 ? 163.588 166.768 208.958 1.00 37.57 ? 3979 PRO A CA    1 
ATOM   17981 C C     . PRO A 1 3979 ? 163.473 166.591 210.464 1.00 37.88 ? 3979 PRO A C     1 
ATOM   17982 O O     . PRO A 1 3979 ? 162.737 167.313 211.140 1.00 38.50 ? 3979 PRO A O     1 
ATOM   17983 C CB    . PRO A 1 3979 ? 164.219 168.118 208.595 1.00 39.36 ? 3979 PRO A CB    1 
ATOM   17984 C CG    . PRO A 1 3979 ? 163.465 168.588 207.411 1.00 39.87 ? 3979 PRO A CG    1 
ATOM   17985 C CD    . PRO A 1 3979 ? 162.069 168.137 207.668 1.00 39.41 ? 3979 PRO A CD    1 
ATOM   17986 N N     . ALA A 1 3980 ? 164.214 165.610 210.986 1.00 39.96 ? 3980 ALA A N     1 
ATOM   17987 C CA    . ALA A 1 3980 ? 164.277 165.352 212.420 1.00 37.93 ? 3980 ALA A CA    1 
ATOM   17988 C C     . ALA A 1 3980 ? 165.700 165.046 212.876 1.00 36.28 ? 3980 ALA A C     1 
ATOM   17989 O O     . ALA A 1 3980 ? 165.893 164.525 213.979 1.00 34.19 ? 3980 ALA A O     1 
ATOM   17990 C CB    . ALA A 1 3980 ? 163.339 164.206 212.809 1.00 35.25 ? 3980 ALA A CB    1 
ATOM   17991 N N     . THR A 1 3981 ? 166.697 165.348 212.049 1.00 33.64 ? 3981 THR A N     1 
ATOM   17992 C CA    . THR A 1 3981 ? 168.075 165.074 212.424 1.00 32.59 ? 3981 THR A CA    1 
ATOM   17993 C C     . THR A 1 3981 ? 168.510 166.004 213.556 1.00 26.54 ? 3981 THR A C     1 
ATOM   17994 O O     . THR A 1 3981 ? 168.128 167.179 213.580 1.00 24.21 ? 3981 THR A O     1 
ATOM   17995 C CB    . THR A 1 3981 ? 169.007 165.224 211.216 1.00 32.70 ? 3981 THR A CB    1 
ATOM   17996 O OG1   . THR A 1 3981 ? 170.335 164.822 211.576 1.00 28.65 ? 3981 THR A OG1   1 
ATOM   17997 C CG2   . THR A 1 3981 ? 169.027 166.657 210.700 1.00 28.18 ? 3981 THR A CG2   1 
ATOM   17998 N N     . PRO A 1 3982 ? 169.285 165.503 214.522 1.00 25.51 ? 3982 PRO A N     1 
ATOM   17999 C CA    . PRO A 1 3982 ? 169.688 166.361 215.650 1.00 24.93 ? 3982 PRO A CA    1 
ATOM   18000 C C     . PRO A 1 3982 ? 170.467 167.594 215.227 1.00 22.82 ? 3982 PRO A C     1 
ATOM   18001 O O     . PRO A 1 3982 ? 170.319 168.654 215.846 1.00 25.59 ? 3982 PRO A O     1 
ATOM   18002 C CB    . PRO A 1 3982 ? 170.537 165.424 216.521 1.00 25.04 ? 3982 PRO A CB    1 
ATOM   18003 C CG    . PRO A 1 3982 ? 170.156 164.045 216.116 1.00 25.78 ? 3982 PRO A CG    1 
ATOM   18004 C CD    . PRO A 1 3982 ? 169.711 164.104 214.690 1.00 27.04 ? 3982 PRO A CD    1 
ATOM   18005 N N     . ILE A 1 3983 ? 171.295 167.487 214.186 1.00 21.33 ? 3983 ILE A N     1 
ATOM   18006 C CA    . ILE A 1 3983 ? 172.085 168.631 213.740 1.00 20.73 ? 3983 ILE A CA    1 
ATOM   18007 C C     . ILE A 1 3983 ? 171.181 169.732 213.201 1.00 23.86 ? 3983 ILE A C     1 
ATOM   18008 O O     . ILE A 1 3983 ? 171.423 170.923 213.433 1.00 25.54 ? 3983 ILE A O     1 
ATOM   18009 C CB    . ILE A 1 3983 ? 173.120 168.186 212.691 1.00 22.30 ? 3983 ILE A CB    1 
ATOM   18010 C CG1   . ILE A 1 3983 ? 173.892 166.963 213.186 1.00 18.99 ? 3983 ILE A CG1   1 
ATOM   18011 C CG2   . ILE A 1 3983 ? 174.072 169.323 212.368 1.00 21.05 ? 3983 ILE A CG2   1 
ATOM   18012 C CD1   . ILE A 1 3983 ? 174.619 167.184 214.488 1.00 21.57 ? 3983 ILE A CD1   1 
ATOM   18013 N N     . GLY A 1 3984 ? 170.136 169.357 212.461 1.00 26.28 ? 3984 GLY A N     1 
ATOM   18014 C CA    . GLY A 1 3984 ? 169.230 170.357 211.920 1.00 20.19 ? 3984 GLY A CA    1 
ATOM   18015 C C     . GLY A 1 3984 ? 168.485 171.115 213.002 1.00 20.00 ? 3984 GLY A C     1 
ATOM   18016 O O     . GLY A 1 3984 ? 168.386 172.344 212.961 1.00 18.92 ? 3984 GLY A O     1 
ATOM   18017 N N     . GLN A 1 3985 ? 167.947 170.389 213.986 1.00 19.27 ? 3985 GLN A N     1 
ATOM   18018 C CA    . GLN A 1 3985 ? 167.300 171.059 215.109 1.00 16.48 ? 3985 GLN A CA    1 
ATOM   18019 C C     . GLN A 1 3985 ? 168.293 171.916 215.880 1.00 23.54 ? 3985 GLN A C     1 
ATOM   18020 O O     . GLN A 1 3985 ? 167.955 173.019 216.322 1.00 32.48 ? 3985 GLN A O     1 
ATOM   18021 C CB    . GLN A 1 3985 ? 166.628 170.047 216.040 1.00 16.76 ? 3985 GLN A CB    1 
ATOM   18022 C CG    . GLN A 1 3985 ? 165.229 169.612 215.612 1.00 21.47 ? 3985 GLN A CG    1 
ATOM   18023 C CD    . GLN A 1 3985 ? 165.227 168.526 214.559 1.00 28.86 ? 3985 GLN A CD    1 
ATOM   18024 O OE1   . GLN A 1 3985 ? 165.718 167.424 214.791 1.00 28.22 ? 3985 GLN A OE1   1 
ATOM   18025 N NE2   . GLN A 1 3985 ? 164.667 168.830 213.394 1.00 27.22 ? 3985 GLN A NE2   1 
ATOM   18026 N N     . ALA A 1 3986 ? 169.525 171.431 216.048 1.00 18.52 ? 3986 ALA A N     1 
ATOM   18027 C CA    . ALA A 1 3986 ? 170.530 172.204 216.770 1.00 15.38 ? 3986 ALA A CA    1 
ATOM   18028 C C     . ALA A 1 3986 ? 170.816 173.526 216.070 1.00 12.64 ? 3986 ALA A C     1 
ATOM   18029 O O     . ALA A 1 3986 ? 170.856 174.581 216.709 1.00 18.52 ? 3986 ALA A O     1 
ATOM   18030 C CB    . ALA A 1 3986 ? 171.811 171.385 216.923 1.00 17.31 ? 3986 ALA A CB    1 
ATOM   18031 N N     . ILE A 1 3987 ? 171.004 173.492 214.750 1.00 13.37 ? 3987 ILE A N     1 
ATOM   18032 C CA    . ILE A 1 3987 ? 171.326 174.725 214.034 1.00 15.50 ? 3987 ILE A CA    1 
ATOM   18033 C C     . ILE A 1 3987 ? 170.113 175.649 213.952 1.00 18.46 ? 3987 ILE A C     1 
ATOM   18034 O O     . ILE A 1 3987 ? 170.256 176.880 214.010 1.00 19.50 ? 3987 ILE A O     1 
ATOM   18035 C CB    . ILE A 1 3987 ? 171.913 174.410 212.644 1.00 13.39 ? 3987 ILE A CB    1 
ATOM   18036 C CG1   . ILE A 1 3987 ? 172.482 175.678 212.010 1.00 12.84 ? 3987 ILE A CG1   1 
ATOM   18037 C CG2   . ILE A 1 3987 ? 170.880 173.778 211.734 1.00 23.19 ? 3987 ILE A CG2   1 
ATOM   18038 C CD1   . ILE A 1 3987 ? 173.350 175.415 210.812 1.00 16.90 ? 3987 ILE A CD1   1 
ATOM   18039 N N     . HIS A 1 3988 ? 168.904 175.092 213.827 1.00 23.07 ? 3988 HIS A N     1 
ATOM   18040 C CA    . HIS A 1 3988 ? 167.710 175.930 213.846 1.00 21.35 ? 3988 HIS A CA    1 
ATOM   18041 C C     . HIS A 1 3988 ? 167.553 176.627 215.192 1.00 17.37 ? 3988 HIS A C     1 
ATOM   18042 O O     . HIS A 1 3988 ? 167.238 177.823 215.248 1.00 17.25 ? 3988 HIS A O     1 
ATOM   18043 C CB    . HIS A 1 3988 ? 166.476 175.089 213.523 1.00 21.03 ? 3988 HIS A CB    1 
ATOM   18044 C CG    . HIS A 1 3988 ? 166.203 174.955 212.058 1.00 22.52 ? 3988 HIS A CG    1 
ATOM   18045 N ND1   . HIS A 1 3988 ? 165.189 174.167 211.558 1.00 21.14 ? 3988 HIS A ND1   1 
ATOM   18046 C CD2   . HIS A 1 3988 ? 166.815 175.506 210.983 1.00 21.52 ? 3988 HIS A CD2   1 
ATOM   18047 C CE1   . HIS A 1 3988 ? 165.186 174.240 210.239 1.00 23.86 ? 3988 HIS A CE1   1 
ATOM   18048 N NE2   . HIS A 1 3988 ? 166.163 175.046 209.865 1.00 23.72 ? 3988 HIS A NE2   1 
ATOM   18049 N N     . ARG A 1 3989 ? 167.782 175.899 216.288 1.00 13.38 ? 3989 ARG A N     1 
ATOM   18050 C CA    . ARG A 1 3989 ? 167.743 176.507 217.611 1.00 12.53 ? 3989 ARG A CA    1 
ATOM   18051 C C     . ARG A 1 3989 ? 168.858 177.527 217.788 1.00 15.55 ? 3989 ARG A C     1 
ATOM   18052 O O     . ARG A 1 3989 ? 168.674 178.526 218.487 1.00 18.67 ? 3989 ARG A O     1 
ATOM   18053 C CB    . ARG A 1 3989 ? 167.835 175.423 218.684 1.00 16.15 ? 3989 ARG A CB    1 
ATOM   18054 C CG    . ARG A 1 3989 ? 166.607 174.532 218.765 1.00 17.90 ? 3989 ARG A CG    1 
ATOM   18055 C CD    . ARG A 1 3989 ? 166.806 173.402 219.758 1.00 12.44 ? 3989 ARG A CD    1 
ATOM   18056 N NE    . ARG A 1 3989 ? 165.648 172.519 219.815 1.00 19.08 ? 3989 ARG A NE    1 
ATOM   18057 C CZ    . ARG A 1 3989 ? 165.597 171.397 220.520 1.00 23.99 ? 3989 ARG A CZ    1 
ATOM   18058 N NH1   . ARG A 1 3989 ? 166.628 170.985 221.239 1.00 23.07 ? 3989 ARG A NH1   1 
ATOM   18059 N NH2   . ARG A 1 3989 ? 164.485 170.669 220.501 1.00 22.05 ? 3989 ARG A NH2   1 
ATOM   18060 N N     . LEU A 1 3990 ? 170.015 177.293 217.169 1.00 14.70 ? 3990 LEU A N     1 
ATOM   18061 C CA    . LEU A 1 3990 ? 171.096 178.270 217.222 1.00 13.54 ? 3990 LEU A CA    1 
ATOM   18062 C C     . LEU A 1 3990 ? 170.688 179.575 216.551 1.00 14.79 ? 3990 LEU A C     1 
ATOM   18063 O O     . LEU A 1 3990 ? 170.935 180.664 217.085 1.00 18.70 ? 3990 LEU A O     1 
ATOM   18064 C CB    . LEU A 1 3990 ? 172.346 177.689 216.564 1.00 13.22 ? 3990 LEU A CB    1 
ATOM   18065 C CG    . LEU A 1 3990 ? 173.545 178.615 216.386 1.00 14.41 ? 3990 LEU A CG    1 
ATOM   18066 C CD1   . LEU A 1 3990 ? 174.137 178.980 217.734 1.00 15.07 ? 3990 LEU A CD1   1 
ATOM   18067 C CD2   . LEU A 1 3990 ? 174.585 177.961 215.498 1.00 14.06 ? 3990 LEU A CD2   1 
ATOM   18068 N N     . LEU A 1 3991 ? 170.054 179.482 215.382 1.00 19.58 ? 3991 LEU A N     1 
ATOM   18069 C CA    . LEU A 1 3991 ? 169.573 180.686 214.710 1.00 15.73 ? 3991 LEU A CA    1 
ATOM   18070 C C     . LEU A 1 3991 ? 168.479 181.370 215.525 1.00 9.36  ? 3991 LEU A C     1 
ATOM   18071 O O     . LEU A 1 3991 ? 168.431 182.603 215.607 1.00 12.51 ? 3991 LEU A O     1 
ATOM   18072 C CB    . LEU A 1 3991 ? 169.070 180.339 213.311 1.00 18.14 ? 3991 LEU A CB    1 
ATOM   18073 C CG    . LEU A 1 3991 ? 170.170 180.016 212.296 1.00 14.55 ? 3991 LEU A CG    1 
ATOM   18074 C CD1   . LEU A 1 3991 ? 169.680 179.001 211.276 1.00 17.78 ? 3991 LEU A CD1   1 
ATOM   18075 C CD2   . LEU A 1 3991 ? 170.671 181.270 211.616 1.00 15.61 ? 3991 LEU A CD2   1 
ATOM   18076 N N     . LEU A 1 3992 ? 167.594 180.581 216.141 1.00 12.96 ? 3992 LEU A N     1 
ATOM   18077 C CA    . LEU A 1 3992 ? 166.562 181.147 217.006 1.00 13.63 ? 3992 LEU A CA    1 
ATOM   18078 C C     . LEU A 1 3992 ? 167.175 181.902 218.180 1.00 16.46 ? 3992 LEU A C     1 
ATOM   18079 O O     . LEU A 1 3992 ? 166.707 182.987 218.544 1.00 18.75 ? 3992 LEU A O     1 
ATOM   18080 C CB    . LEU A 1 3992 ? 165.640 180.039 217.512 1.00 20.02 ? 3992 LEU A CB    1 
ATOM   18081 C CG    . LEU A 1 3992 ? 164.418 179.662 216.672 1.00 20.82 ? 3992 LEU A CG    1 
ATOM   18082 C CD1   . LEU A 1 3992 ? 163.481 178.781 217.476 1.00 19.92 ? 3992 LEU A CD1   1 
ATOM   18083 C CD2   . LEU A 1 3992 ? 163.692 180.905 216.204 1.00 22.36 ? 3992 LEU A CD2   1 
ATOM   18084 N N     . ILE A 1 3993 ? 168.217 181.336 218.792 1.00 18.45 ? 3993 ILE A N     1 
ATOM   18085 C CA    . ILE A 1 3993 ? 168.883 181.989 219.915 1.00 14.88 ? 3993 ILE A CA    1 
ATOM   18086 C C     . ILE A 1 3993 ? 169.583 183.262 219.457 1.00 17.28 ? 3993 ILE A C     1 
ATOM   18087 O O     . ILE A 1 3993 ? 169.587 184.274 220.168 1.00 24.13 ? 3993 ILE A O     1 
ATOM   18088 C CB    . ILE A 1 3993 ? 169.856 181.010 220.597 1.00 10.38 ? 3993 ILE A CB    1 
ATOM   18089 C CG1   . ILE A 1 3993 ? 169.080 180.002 221.444 1.00 13.87 ? 3993 ILE A CG1   1 
ATOM   18090 C CG2   . ILE A 1 3993 ? 170.865 181.752 221.454 1.00 10.45 ? 3993 ILE A CG2   1 
ATOM   18091 C CD1   . ILE A 1 3993 ? 168.150 180.640 222.445 1.00 21.49 ? 3993 ILE A CD1   1 
ATOM   18092 N N     . GLN A 1 3994 ? 170.189 183.238 218.269 1.00 14.78 ? 3994 GLN A N     1 
ATOM   18093 C CA    . GLN A 1 3994 ? 170.712 184.479 217.709 1.00 10.02 ? 3994 GLN A CA    1 
ATOM   18094 C C     . GLN A 1 3994 ? 169.607 185.513 217.539 1.00 13.04 ? 3994 GLN A C     1 
ATOM   18095 O O     . GLN A 1 3994 ? 169.838 186.711 217.738 1.00 19.14 ? 3994 GLN A O     1 
ATOM   18096 C CB    . GLN A 1 3994 ? 171.407 184.212 216.375 1.00 15.52 ? 3994 GLN A CB    1 
ATOM   18097 C CG    . GLN A 1 3994 ? 171.822 185.472 215.635 1.00 13.98 ? 3994 GLN A CG    1 
ATOM   18098 C CD    . GLN A 1 3994 ? 173.138 185.317 214.913 1.00 14.84 ? 3994 GLN A CD    1 
ATOM   18099 O OE1   . GLN A 1 3994 ? 174.011 184.573 215.348 1.00 13.10 ? 3994 GLN A OE1   1 
ATOM   18100 N NE2   . GLN A 1 3994 ? 173.287 186.018 213.797 1.00 17.83 ? 3994 GLN A NE2   1 
ATOM   18101 N N     . ALA A 1 3995 ? 168.399 185.073 217.184 1.00 19.46 ? 3995 ALA A N     1 
ATOM   18102 C CA    . ALA A 1 3995 ? 167.267 185.991 217.102 1.00 18.38 ? 3995 ALA A CA    1 
ATOM   18103 C C     . ALA A 1 3995 ? 166.754 186.362 218.490 1.00 19.74 ? 3995 ALA A C     1 
ATOM   18104 O O     . ALA A 1 3995 ? 166.779 187.534 218.881 1.00 19.34 ? 3995 ALA A O     1 
ATOM   18105 C CB    . ALA A 1 3995 ? 166.148 185.372 216.261 1.00 18.75 ? 3995 ALA A CB    1 
ATOM   18106 N N     . PHE A 1 3996 ? 166.292 185.374 219.251 1.00 23.40 ? 3996 PHE A N     1 
ATOM   18107 C CA    . PHE A 1 3996 ? 165.761 185.589 220.591 1.00 23.16 ? 3996 PHE A CA    1 
ATOM   18108 C C     . PHE A 1 3996 ? 166.848 185.342 221.628 1.00 23.04 ? 3996 PHE A C     1 
ATOM   18109 O O     . PHE A 1 3996 ? 167.407 184.243 221.693 1.00 25.36 ? 3996 PHE A O     1 
ATOM   18110 C CB    . PHE A 1 3996 ? 164.577 184.663 220.869 1.00 23.62 ? 3996 PHE A CB    1 
ATOM   18111 C CG    . PHE A 1 3996 ? 163.466 184.777 219.874 1.00 22.77 ? 3996 PHE A CG    1 
ATOM   18112 C CD1   . PHE A 1 3996 ? 162.826 185.984 219.668 1.00 23.66 ? 3996 PHE A CD1   1 
ATOM   18113 C CD2   . PHE A 1 3996 ? 163.055 183.672 219.148 1.00 23.48 ? 3996 PHE A CD2   1 
ATOM   18114 C CE1   . PHE A 1 3996 ? 161.800 186.087 218.759 1.00 22.46 ? 3996 PHE A CE1   1 
ATOM   18115 C CE2   . PHE A 1 3996 ? 162.030 183.771 218.234 1.00 23.04 ? 3996 PHE A CE2   1 
ATOM   18116 C CZ    . PHE A 1 3996 ? 161.401 184.981 218.039 1.00 25.72 ? 3996 PHE A CZ    1 
ATOM   18117 N N     . ARG A 1 3997 ? 167.116 186.352 222.455 1.00 19.47 ? 3997 ARG A N     1 
ATOM   18118 C CA    . ARG A 1 3997 ? 168.089 186.259 223.538 1.00 16.35 ? 3997 ARG A CA    1 
ATOM   18119 C C     . ARG A 1 3997 ? 169.480 185.940 223.003 1.00 13.96 ? 3997 ARG A C     1 
ATOM   18120 O O     . ARG A 1 3997 ? 169.987 184.832 223.214 1.00 11.83 ? 3997 ARG A O     1 
ATOM   18121 C CB    . ARG A 1 3997 ? 167.653 185.203 224.556 1.00 15.94 ? 3997 ARG A CB    1 
ATOM   18122 C CG    . ARG A 1 3997 ? 166.704 185.720 225.622 1.00 15.46 ? 3997 ARG A CG    1 
ATOM   18123 C CD    . ARG A 1 3997 ? 167.420 186.676 226.561 1.00 17.66 ? 3997 ARG A CD    1 
ATOM   18124 N NE    . ARG A 1 3997 ? 168.223 185.986 227.565 1.00 19.93 ? 3997 ARG A NE    1 
ATOM   18125 C CZ    . ARG A 1 3997 ? 167.747 185.144 228.473 1.00 20.17 ? 3997 ARG A CZ    1 
ATOM   18126 N NH1   . ARG A 1 3997 ? 166.450 184.911 228.592 1.00 26.64 ? 3997 ARG A NH1   1 
ATOM   18127 N NH2   . ARG A 1 3997 ? 168.593 184.537 229.301 1.00 17.06 ? 3997 ARG A NH2   1 
ATOM   18128 N N     . PRO A 1 3998 ? 170.131 186.882 222.311 1.00 17.01 ? 3998 PRO A N     1 
ATOM   18129 C CA    . PRO A 1 3998 ? 171.481 186.614 221.790 1.00 14.02 ? 3998 PRO A CA    1 
ATOM   18130 C C     . PRO A 1 3998 ? 172.560 186.551 222.858 1.00 14.15 ? 3998 PRO A C     1 
ATOM   18131 O O     . PRO A 1 3998 ? 173.717 186.274 222.518 1.00 16.82 ? 3998 PRO A O     1 
ATOM   18132 C CB    . PRO A 1 3998 ? 171.727 187.784 220.830 1.00 12.05 ? 3998 PRO A CB    1 
ATOM   18133 C CG    . PRO A 1 3998 ? 170.837 188.867 221.305 1.00 12.53 ? 3998 PRO A CG    1 
ATOM   18134 C CD    . PRO A 1 3998 ? 169.648 188.226 221.954 1.00 18.89 ? 3998 PRO A CD    1 
ATOM   18135 N N     . ASP A 1 3999 ? 172.236 186.813 224.126 1.00 14.42 ? 3999 ASP A N     1 
ATOM   18136 C CA    . ASP A 1 3999 ? 173.239 186.682 225.177 1.00 9.85  ? 3999 ASP A CA    1 
ATOM   18137 C C     . ASP A 1 3999 ? 173.580 185.223 225.449 1.00 13.34 ? 3999 ASP A C     1 
ATOM   18138 O O     . ASP A 1 3999 ? 174.687 184.921 225.908 1.00 14.66 ? 3999 ASP A O     1 
ATOM   18139 C CB    . ASP A 1 3999 ? 172.756 187.367 226.456 1.00 14.53 ? 3999 ASP A CB    1 
ATOM   18140 C CG    . ASP A 1 3999 ? 171.342 186.977 226.825 1.00 15.78 ? 3999 ASP A CG    1 
ATOM   18141 O OD1   . ASP A 1 3999 ? 170.480 186.963 225.925 1.00 15.66 ? 3999 ASP A OD1   1 
ATOM   18142 O OD2   . ASP A 1 3999 ? 171.093 186.689 228.014 1.00 12.54 ? 3999 ASP A OD2   1 
ATOM   18143 N N     . ARG A 1 4000 ? 172.651 184.310 225.173 1.00 12.26 ? 4000 ARG A N     1 
ATOM   18144 C CA    . ARG A 1 4000 ? 172.870 182.881 225.338 1.00 10.47 ? 4000 ARG A CA    1 
ATOM   18145 C C     . ARG A 1 4000 ? 173.504 182.244 224.108 1.00 10.26 ? 4000 ARG A C     1 
ATOM   18146 O O     . ARG A 1 4000 ? 173.423 181.021 223.940 1.00 10.91 ? 4000 ARG A O     1 
ATOM   18147 C CB    . ARG A 1 4000 ? 171.547 182.187 225.659 1.00 10.25 ? 4000 ARG A CB    1 
ATOM   18148 C CG    . ARG A 1 4000 ? 170.688 182.944 226.646 1.00 5.48  ? 4000 ARG A CG    1 
ATOM   18149 C CD    . ARG A 1 4000 ? 171.349 183.081 228.005 1.00 18.42 ? 4000 ARG A CD    1 
ATOM   18150 N NE    . ARG A 1 4000 ? 171.654 181.786 228.602 1.00 17.67 ? 4000 ARG A NE    1 
ATOM   18151 C CZ    . ARG A 1 4000 ? 172.824 181.461 229.132 1.00 13.60 ? 4000 ARG A CZ    1 
ATOM   18152 N NH1   . ARG A 1 4000 ? 173.828 182.320 229.169 1.00 13.04 ? 4000 ARG A NH1   1 
ATOM   18153 N NH2   . ARG A 1 4000 ? 172.989 180.244 229.642 1.00 15.14 ? 4000 ARG A NH2   1 
ATOM   18154 N N     . LEU A 1 4001 ? 174.122 183.051 223.241 1.00 7.05  ? 4001 LEU A N     1 
ATOM   18155 C CA    . LEU A 1 4001 ? 174.698 182.523 222.011 1.00 5.07  ? 4001 LEU A CA    1 
ATOM   18156 C C     . LEU A 1 4001 ? 175.864 181.589 222.306 1.00 6.45  ? 4001 LEU A C     1 
ATOM   18157 O O     . LEU A 1 4001 ? 176.038 180.572 221.627 1.00 14.57 ? 4001 LEU A O     1 
ATOM   18158 C CB    . LEU A 1 4001 ? 175.144 183.670 221.106 1.00 12.29 ? 4001 LEU A CB    1 
ATOM   18159 C CG    . LEU A 1 4001 ? 175.696 183.289 219.732 1.00 10.02 ? 4001 LEU A CG    1 
ATOM   18160 C CD1   . LEU A 1 4001 ? 174.686 182.439 218.982 1.00 12.47 ? 4001 LEU A CD1   1 
ATOM   18161 C CD2   . LEU A 1 4001 ? 176.063 184.524 218.929 1.00 10.49 ? 4001 LEU A CD2   1 
ATOM   18162 N N     . LEU A 1 4002 ? 176.677 181.918 223.311 1.00 10.23 ? 4002 LEU A N     1 
ATOM   18163 C CA    . LEU A 1 4002 ? 177.790 181.046 223.672 1.00 3.42  ? 4002 LEU A CA    1 
ATOM   18164 C C     . LEU A 1 4002 ? 177.292 179.693 224.158 1.00 4.30  ? 4002 LEU A C     1 
ATOM   18165 O O     . LEU A 1 4002 ? 177.825 178.649 223.766 1.00 9.70  ? 4002 LEU A O     1 
ATOM   18166 C CB    . LEU A 1 4002 ? 178.657 181.696 224.750 1.00 8.04  ? 4002 LEU A CB    1 
ATOM   18167 C CG    . LEU A 1 4002 ? 179.665 182.782 224.368 1.00 10.96 ? 4002 LEU A CG    1 
ATOM   18168 C CD1   . LEU A 1 4002 ? 180.783 182.211 223.505 1.00 6.40  ? 4002 LEU A CD1   1 
ATOM   18169 C CD2   . LEU A 1 4002 ? 178.996 183.963 223.698 1.00 15.05 ? 4002 LEU A CD2   1 
ATOM   18170 N N     . ALA A 1 4003 ? 176.268 179.691 225.012 1.00 11.16 ? 4003 ALA A N     1 
ATOM   18171 C CA    . ALA A 1 4003 ? 175.722 178.433 225.508 1.00 10.53 ? 4003 ALA A CA    1 
ATOM   18172 C C     . ALA A 1 4003 ? 175.091 177.626 224.383 1.00 9.59  ? 4003 ALA A C     1 
ATOM   18173 O O     . ALA A 1 4003 ? 175.244 176.399 224.321 1.00 15.34 ? 4003 ALA A O     1 
ATOM   18174 C CB    . ALA A 1 4003 ? 174.704 178.706 226.613 1.00 9.43  ? 4003 ALA A CB    1 
ATOM   18175 N N     . MET A 1 4004 ? 174.374 178.298 223.480 1.00 4.60  ? 4004 MET A N     1 
ATOM   18176 C CA    . MET A 1 4004 ? 173.756 177.593 222.366 1.00 5.87  ? 4004 MET A CA    1 
ATOM   18177 C C     . MET A 1 4004 ? 174.813 177.004 221.438 1.00 10.17 ? 4004 MET A C     1 
ATOM   18178 O O     . MET A 1 4004 ? 174.654 175.882 220.951 1.00 22.34 ? 4004 MET A O     1 
ATOM   18179 C CB    . MET A 1 4004 ? 172.840 178.542 221.598 1.00 12.58 ? 4004 MET A CB    1 
ATOM   18180 C CG    . MET A 1 4004 ? 171.895 177.893 220.592 1.00 14.10 ? 4004 MET A CG    1 
ATOM   18181 S SD    . MET A 1 4004 ? 170.788 176.615 221.246 1.00 22.13 ? 4004 MET A SD    1 
ATOM   18182 C CE    . MET A 1 4004 ? 171.695 175.098 220.970 1.00 13.36 ? 4004 MET A CE    1 
ATOM   18183 N N     . ALA A 1 4005 ? 175.902 177.736 221.193 1.00 4.29  ? 4005 ALA A N     1 
ATOM   18184 C CA    . ALA A 1 4005 ? 176.992 177.198 220.388 1.00 5.70  ? 4005 ALA A CA    1 
ATOM   18185 C C     . ALA A 1 4005 ? 177.667 176.025 221.087 1.00 11.42 ? 4005 ALA A C     1 
ATOM   18186 O O     . ALA A 1 4005 ? 178.096 175.068 220.434 1.00 16.31 ? 4005 ALA A O     1 
ATOM   18187 C CB    . ALA A 1 4005 ? 178.006 178.298 220.076 1.00 1.97  ? 4005 ALA A CB    1 
ATOM   18188 N N     . HIS A 1 4006 ? 177.783 176.085 222.415 1.00 5.94  ? 4006 HIS A N     1 
ATOM   18189 C CA    . HIS A 1 4006 ? 178.318 174.948 223.157 1.00 1.50  ? 4006 HIS A CA    1 
ATOM   18190 C C     . HIS A 1 4006 ? 177.438 173.716 222.986 1.00 9.41  ? 4006 HIS A C     1 
ATOM   18191 O O     . HIS A 1 4006 ? 177.946 172.609 222.778 1.00 19.34 ? 4006 HIS A O     1 
ATOM   18192 C CB    . HIS A 1 4006 ? 178.464 175.301 224.635 1.00 8.92  ? 4006 HIS A CB    1 
ATOM   18193 C CG    . HIS A 1 4006 ? 179.751 175.988 224.969 1.00 12.63 ? 4006 HIS A CG    1 
ATOM   18194 N ND1   . HIS A 1 4006 ? 180.960 175.328 224.999 1.00 10.48 ? 4006 HIS A ND1   1 
ATOM   18195 C CD2   . HIS A 1 4006 ? 180.019 177.276 225.288 1.00 9.71  ? 4006 HIS A CD2   1 
ATOM   18196 C CE1   . HIS A 1 4006 ? 181.916 176.178 225.324 1.00 11.33 ? 4006 HIS A CE1   1 
ATOM   18197 N NE2   . HIS A 1 4006 ? 181.372 177.368 225.503 1.00 9.23  ? 4006 HIS A NE2   1 
ATOM   18198 N N     . MET A 1 4007 ? 176.116 173.887 223.058 1.00 10.40 ? 4007 MET A N     1 
ATOM   18199 C CA    . MET A 1 4007 ? 175.228 172.747 222.833 1.00 7.33  ? 4007 MET A CA    1 
ATOM   18200 C C     . MET A 1 4007 ? 175.302 172.257 221.392 1.00 13.08 ? 4007 MET A C     1 
ATOM   18201 O O     . MET A 1 4007 ? 175.169 171.057 221.130 1.00 18.65 ? 4007 MET A O     1 
ATOM   18202 C CB    . MET A 1 4007 ? 173.785 173.092 223.196 1.00 7.08  ? 4007 MET A CB    1 
ATOM   18203 C CG    . MET A 1 4007 ? 173.597 173.736 224.547 1.00 15.48 ? 4007 MET A CG    1 
ATOM   18204 S SD    . MET A 1 4007 ? 171.877 174.198 224.792 1.00 27.17 ? 4007 MET A SD    1 
ATOM   18205 C CE    . MET A 1 4007 ? 171.066 172.616 224.585 1.00 17.01 ? 4007 MET A CE    1 
ATOM   18206 N N     . PHE A 1 4008 ? 175.493 173.172 220.442 1.00 11.77 ? 4008 PHE A N     1 
ATOM   18207 C CA    . PHE A 1 4008 ? 175.637 172.771 219.046 1.00 10.94 ? 4008 PHE A CA    1 
ATOM   18208 C C     . PHE A 1 4008 ? 176.895 171.934 218.842 1.00 9.40  ? 4008 PHE A C     1 
ATOM   18209 O O     . PHE A 1 4008 ? 176.868 170.912 218.144 1.00 18.43 ? 4008 PHE A O     1 
ATOM   18210 C CB    . PHE A 1 4008 ? 175.647 174.013 218.155 1.00 9.09  ? 4008 PHE A CB    1 
ATOM   18211 C CG    . PHE A 1 4008 ? 175.959 173.732 216.715 1.00 11.85 ? 4008 PHE A CG    1 
ATOM   18212 C CD1   . PHE A 1 4008 ? 174.995 173.206 215.874 1.00 10.97 ? 4008 PHE A CD1   1 
ATOM   18213 C CD2   . PHE A 1 4008 ? 177.210 174.021 216.195 1.00 11.03 ? 4008 PHE A CD2   1 
ATOM   18214 C CE1   . PHE A 1 4008 ? 175.276 172.954 214.547 1.00 13.51 ? 4008 PHE A CE1   1 
ATOM   18215 C CE2   . PHE A 1 4008 ? 177.497 173.773 214.868 1.00 15.07 ? 4008 PHE A CE2   1 
ATOM   18216 C CZ    . PHE A 1 4008 ? 176.527 173.239 214.043 1.00 18.50 ? 4008 PHE A CZ    1 
ATOM   18217 N N     . VAL A 1 4009 ? 178.005 172.345 219.455 1.00 5.28  ? 4009 VAL A N     1 
ATOM   18218 C CA    . VAL A 1 4009 ? 179.230 171.553 219.381 1.00 7.71  ? 4009 VAL A CA    1 
ATOM   18219 C C     . VAL A 1 4009 ? 179.038 170.223 220.095 1.00 9.82  ? 4009 VAL A C     1 
ATOM   18220 O O     . VAL A 1 4009 ? 179.587 169.195 219.685 1.00 13.47 ? 4009 VAL A O     1 
ATOM   18221 C CB    . VAL A 1 4009 ? 180.418 172.339 219.961 1.00 4.39  ? 4009 VAL A CB    1 
ATOM   18222 C CG1   . VAL A 1 4009 ? 181.670 171.489 219.946 1.00 4.39  ? 4009 VAL A CG1   1 
ATOM   18223 C CG2   . VAL A 1 4009 ? 180.636 173.608 219.185 1.00 9.26  ? 4009 VAL A CG2   1 
ATOM   18224 N N     . SER A 1 4010 ? 178.261 170.224 221.181 1.00 9.54  ? 4010 SER A N     1 
ATOM   18225 C CA    . SER A 1 4010 ? 177.957 168.980 221.878 1.00 11.21 ? 4010 SER A CA    1 
ATOM   18226 C C     . SER A 1 4010 ? 177.198 168.013 220.979 1.00 11.53 ? 4010 SER A C     1 
ATOM   18227 O O     . SER A 1 4010 ? 177.499 166.816 220.947 1.00 9.66  ? 4010 SER A O     1 
ATOM   18228 C CB    . SER A 1 4010 ? 177.152 169.281 223.141 1.00 10.60 ? 4010 SER A CB    1 
ATOM   18229 O OG    . SER A 1 4010 ? 176.964 168.115 223.917 1.00 14.93 ? 4010 SER A OG    1 
ATOM   18230 N N     . THR A 1 4011 ? 176.208 168.514 220.243 1.00 11.18 ? 4011 THR A N     1 
ATOM   18231 C CA    . THR A 1 4011 ? 175.458 167.657 219.335 1.00 10.23 ? 4011 THR A CA    1 
ATOM   18232 C C     . THR A 1 4011 ? 176.303 167.175 218.163 1.00 10.92 ? 4011 THR A C     1 
ATOM   18233 O O     . THR A 1 4011 ? 176.167 166.018 217.754 1.00 19.65 ? 4011 THR A O     1 
ATOM   18234 C CB    . THR A 1 4011 ? 174.217 168.382 218.810 1.00 11.18 ? 4011 THR A CB    1 
ATOM   18235 O OG1   . THR A 1 4011 ? 174.604 169.606 218.176 1.00 14.58 ? 4011 THR A OG1   1 
ATOM   18236 C CG2   . THR A 1 4011 ? 173.258 168.686 219.948 1.00 11.32 ? 4011 THR A CG2   1 
ATOM   18237 N N     . ASN A 1 4012 ? 177.173 168.026 217.618 1.00 6.93  ? 4012 ASN A N     1 
ATOM   18238 C CA    . ASN A 1 4012 ? 177.970 167.642 216.460 1.00 6.66  ? 4012 ASN A CA    1 
ATOM   18239 C C     . ASN A 1 4012 ? 179.227 166.851 216.801 1.00 10.57 ? 4012 ASN A C     1 
ATOM   18240 O O     . ASN A 1 4012 ? 179.824 166.259 215.895 1.00 13.07 ? 4012 ASN A O     1 
ATOM   18241 C CB    . ASN A 1 4012 ? 178.371 168.883 215.654 1.00 8.30  ? 4012 ASN A CB    1 
ATOM   18242 C CG    . ASN A 1 4012 ? 177.188 169.542 214.976 1.00 13.18 ? 4012 ASN A CG    1 
ATOM   18243 O OD1   . ASN A 1 4012 ? 176.197 169.881 215.619 1.00 13.48 ? 4012 ASN A OD1   1 
ATOM   18244 N ND2   . ASN A 1 4012 ? 177.287 169.723 213.666 1.00 16.74 ? 4012 ASN A ND2   1 
ATOM   18245 N N     . LEU A 1 4013 ? 179.648 166.819 218.069 1.00 11.56 ? 4013 LEU A N     1 
ATOM   18246 C CA    . LEU A 1 4013 ? 180.863 166.099 218.433 1.00 9.35  ? 4013 LEU A CA    1 
ATOM   18247 C C     . LEU A 1 4013 ? 180.753 165.345 219.755 1.00 11.62 ? 4013 LEU A C     1 
ATOM   18248 O O     . LEU A 1 4013 ? 181.788 164.946 220.303 1.00 12.61 ? 4013 LEU A O     1 
ATOM   18249 C CB    . LEU A 1 4013 ? 182.060 167.058 218.496 1.00 6.94  ? 4013 LEU A CB    1 
ATOM   18250 C CG    . LEU A 1 4013 ? 182.533 167.695 217.187 1.00 7.79  ? 4013 LEU A CG    1 
ATOM   18251 C CD1   . LEU A 1 4013 ? 183.006 169.116 217.420 1.00 2.96  ? 4013 LEU A CD1   1 
ATOM   18252 C CD2   . LEU A 1 4013 ? 183.637 166.867 216.558 1.00 12.53 ? 4013 LEU A CD2   1 
ATOM   18253 N N     . GLY A 1 4014 ? 179.555 165.141 220.285 1.00 13.51 ? 4014 GLY A N     1 
ATOM   18254 C CA    . GLY A 1 4014 ? 179.386 164.432 221.536 1.00 16.20 ? 4014 GLY A CA    1 
ATOM   18255 C C     . GLY A 1 4014 ? 179.492 165.350 222.742 1.00 14.13 ? 4014 GLY A C     1 
ATOM   18256 O O     . GLY A 1 4014 ? 180.147 166.390 222.719 1.00 13.31 ? 4014 GLY A O     1 
ATOM   18257 N N     . GLU A 1 4015 ? 178.827 164.948 223.822 1.00 24.27 ? 4015 GLU A N     1 
ATOM   18258 C CA    . GLU A 1 4015 ? 178.828 165.751 225.045 1.00 25.94 ? 4015 GLU A CA    1 
ATOM   18259 C C     . GLU A 1 4015 ? 180.018 165.404 225.935 1.00 29.99 ? 4015 GLU A C     1 
ATOM   18260 O O     . GLU A 1 4015 ? 179.904 165.218 227.146 1.00 31.90 ? 4015 GLU A O     1 
ATOM   18261 C CB    . GLU A 1 4015 ? 177.508 165.561 225.785 1.00 26.66 ? 4015 GLU A CB    1 
ATOM   18262 C CG    . GLU A 1 4015 ? 177.177 166.662 226.782 1.00 29.42 ? 4015 GLU A CG    1 
ATOM   18263 C CD    . GLU A 1 4015 ? 175.888 166.398 227.535 1.00 31.14 ? 4015 GLU A CD    1 
ATOM   18264 O OE1   . GLU A 1 4015 ? 175.082 165.570 227.062 1.00 28.02 ? 4015 GLU A OE1   1 
ATOM   18265 O OE2   . GLU A 1 4015 ? 175.678 167.020 228.598 1.00 31.71 ? 4015 GLU A OE2   1 
ATOM   18266 N N     . SER A 1 4016 ? 181.188 165.308 225.309 1.00 21.60 ? 4016 SER A N     1 
ATOM   18267 C CA    . SER A 1 4016 ? 182.438 165.222 226.053 1.00 20.49 ? 4016 SER A CA    1 
ATOM   18268 C C     . SER A 1 4016 ? 183.556 165.973 225.344 1.00 21.35 ? 4016 SER A C     1 
ATOM   18269 O O     . SER A 1 4016 ? 184.726 165.778 225.698 1.00 21.48 ? 4016 SER A O     1 
ATOM   18270 C CB    . SER A 1 4016 ? 182.839 163.757 226.264 1.00 22.84 ? 4016 SER A CB    1 
ATOM   18271 O OG    . SER A 1 4016 ? 184.078 163.662 226.945 1.00 24.00 ? 4016 SER A OG    1 
ATOM   18272 N N     . PHE A 1 4017 ? 183.242 166.818 224.361 1.00 13.60 ? 4017 PHE A N     1 
ATOM   18273 C CA    . PHE A 1 4017 ? 184.253 167.299 223.428 1.00 9.37  ? 4017 PHE A CA    1 
ATOM   18274 C C     . PHE A 1 4017 ? 185.149 168.358 224.061 1.00 12.74 ? 4017 PHE A C     1 
ATOM   18275 O O     . PHE A 1 4017 ? 186.377 168.291 223.942 1.00 13.48 ? 4017 PHE A O     1 
ATOM   18276 C CB    . PHE A 1 4017 ? 183.571 167.838 222.170 1.00 7.86  ? 4017 PHE A CB    1 
ATOM   18277 C CG    . PHE A 1 4017 ? 184.525 168.282 221.106 1.00 6.19  ? 4017 PHE A CG    1 
ATOM   18278 C CD1   . PHE A 1 4017 ? 185.188 167.350 220.326 1.00 5.26  ? 4017 PHE A CD1   1 
ATOM   18279 C CD2   . PHE A 1 4017 ? 184.755 169.623 220.875 1.00 9.05  ? 4017 PHE A CD2   1 
ATOM   18280 C CE1   . PHE A 1 4017 ? 186.066 167.747 219.346 1.00 4.59  ? 4017 PHE A CE1   1 
ATOM   18281 C CE2   . PHE A 1 4017 ? 185.632 170.026 219.894 1.00 8.73  ? 4017 PHE A CE2   1 
ATOM   18282 C CZ    . PHE A 1 4017 ? 186.286 169.086 219.127 1.00 6.53  ? 4017 PHE A CZ    1 
ATOM   18283 N N     . MET A 1 4018 ? 184.558 169.339 224.740 1.00 14.68 ? 4018 MET A N     1 
ATOM   18284 C CA    . MET A 1 4018 ? 185.329 170.399 225.374 1.00 10.01 ? 4018 MET A CA    1 
ATOM   18285 C C     . MET A 1 4018 ? 185.718 170.073 226.809 1.00 19.88 ? 4018 MET A C     1 
ATOM   18286 O O     . MET A 1 4018 ? 186.485 170.830 227.413 1.00 18.25 ? 4018 MET A O     1 
ATOM   18287 C CB    . MET A 1 4018 ? 184.547 171.716 225.358 1.00 8.02  ? 4018 MET A CB    1 
ATOM   18288 C CG    . MET A 1 4018 ? 184.763 172.555 224.116 1.00 9.77  ? 4018 MET A CG    1 
ATOM   18289 S SD    . MET A 1 4018 ? 183.267 173.439 223.653 1.00 18.75 ? 4018 MET A SD    1 
ATOM   18290 C CE    . MET A 1 4018 ? 182.174 172.065 223.332 1.00 16.73 ? 4018 MET A CE    1 
ATOM   18291 N N     . SER A 1 4019 ? 185.219 168.963 227.363 1.00 22.26 ? 4019 SER A N     1 
ATOM   18292 C CA    . SER A 1 4019 ? 185.414 168.682 228.783 1.00 17.75 ? 4019 SER A CA    1 
ATOM   18293 C C     . SER A 1 4019 ? 186.883 168.489 229.132 1.00 16.02 ? 4019 SER A C     1 
ATOM   18294 O O     . SER A 1 4019 ? 187.257 168.574 230.307 1.00 19.86 ? 4019 SER A O     1 
ATOM   18295 C CB    . SER A 1 4019 ? 184.605 167.450 229.187 1.00 18.71 ? 4019 SER A CB    1 
ATOM   18296 O OG    . SER A 1 4019 ? 185.095 166.286 228.548 1.00 22.66 ? 4019 SER A OG    1 
ATOM   18297 N N     . ILE A 1 4020 ? 187.727 168.222 228.136 1.00 15.81 ? 4020 ILE A N     1 
ATOM   18298 C CA    . ILE A 1 4020 ? 189.154 168.080 228.397 1.00 21.51 ? 4020 ILE A CA    1 
ATOM   18299 C C     . ILE A 1 4020 ? 189.761 169.422 228.791 1.00 20.95 ? 4020 ILE A C     1 
ATOM   18300 O O     . ILE A 1 4020 ? 190.761 169.480 229.515 1.00 20.20 ? 4020 ILE A O     1 
ATOM   18301 C CB    . ILE A 1 4020 ? 189.857 167.469 227.172 1.00 25.97 ? 4020 ILE A CB    1 
ATOM   18302 C CG1   . ILE A 1 4020 ? 189.085 166.244 226.678 1.00 22.80 ? 4020 ILE A CG1   1 
ATOM   18303 C CG2   . ILE A 1 4020 ? 191.289 167.084 227.511 1.00 21.51 ? 4020 ILE A CG2   1 
ATOM   18304 C CD1   . ILE A 1 4020 ? 189.077 165.089 227.655 1.00 19.24 ? 4020 ILE A CD1   1 
ATOM   18305 N N     . MET A 1 4021 ? 189.173 170.523 228.316 1.00 18.38 ? 4021 MET A N     1 
ATOM   18306 C CA    . MET A 1 4021 ? 189.709 171.840 228.642 1.00 17.02 ? 4021 MET A CA    1 
ATOM   18307 C C     . MET A 1 4021 ? 189.383 172.251 230.072 1.00 22.27 ? 4021 MET A C     1 
ATOM   18308 O O     . MET A 1 4021 ? 190.108 173.059 230.663 1.00 24.22 ? 4021 MET A O     1 
ATOM   18309 C CB    . MET A 1 4021 ? 189.177 172.883 227.659 1.00 16.79 ? 4021 MET A CB    1 
ATOM   18310 C CG    . MET A 1 4021 ? 189.638 172.691 226.220 1.00 18.21 ? 4021 MET A CG    1 
ATOM   18311 S SD    . MET A 1 4021 ? 191.426 172.802 226.012 1.00 17.75 ? 4021 MET A SD    1 
ATOM   18312 C CE    . MET A 1 4021 ? 191.873 171.074 225.874 1.00 12.18 ? 4021 MET A CE    1 
ATOM   18313 N N     . GLU A 1 4022 ? 188.299 171.719 230.643 1.00 28.88 ? 4022 GLU A N     1 
ATOM   18314 C CA    . GLU A 1 4022 ? 187.917 172.113 231.997 1.00 22.88 ? 4022 GLU A CA    1 
ATOM   18315 C C     . GLU A 1 4022 ? 188.876 171.543 233.035 1.00 19.91 ? 4022 GLU A C     1 
ATOM   18316 O O     . GLU A 1 4022 ? 189.224 172.227 234.005 1.00 22.46 ? 4022 GLU A O     1 
ATOM   18317 C CB    . GLU A 1 4022 ? 186.487 171.668 232.294 1.00 21.52 ? 4022 GLU A CB    1 
ATOM   18318 C CG    . GLU A 1 4022 ? 185.431 172.406 231.499 1.00 21.14 ? 4022 GLU A CG    1 
ATOM   18319 C CD    . GLU A 1 4022 ? 184.377 171.473 230.945 1.00 27.58 ? 4022 GLU A CD    1 
ATOM   18320 O OE1   . GLU A 1 4022 ? 184.370 170.289 231.341 1.00 28.86 ? 4022 GLU A OE1   1 
ATOM   18321 O OE2   . GLU A 1 4022 ? 183.559 171.920 230.114 1.00 27.57 ? 4022 GLU A OE2   1 
ATOM   18322 N N     . GLN A 1 4023 ? 189.307 170.298 232.855 1.00 26.56 ? 4023 GLN A N     1 
ATOM   18323 C CA    . GLN A 1 4023 ? 190.210 169.682 233.811 1.00 28.64 ? 4023 GLN A CA    1 
ATOM   18324 C C     . GLN A 1 4023 ? 191.565 170.389 233.778 1.00 31.77 ? 4023 GLN A C     1 
ATOM   18325 O O     . GLN A 1 4023 ? 191.959 170.942 232.748 1.00 31.30 ? 4023 GLN A O     1 
ATOM   18326 C CB    . GLN A 1 4023 ? 190.381 168.195 233.503 1.00 25.21 ? 4023 GLN A CB    1 
ATOM   18327 C CG    . GLN A 1 4023 ? 191.058 167.901 232.179 1.00 26.53 ? 4023 GLN A CG    1 
ATOM   18328 C CD    . GLN A 1 4023 ? 191.153 166.418 231.887 1.00 31.31 ? 4023 GLN A CD    1 
ATOM   18329 O OE1   . GLN A 1 4023 ? 190.754 165.586 232.703 1.00 34.98 ? 4023 GLN A OE1   1 
ATOM   18330 N NE2   . GLN A 1 4023 ? 191.688 166.077 230.721 1.00 27.84 ? 4023 GLN A NE2   1 
ATOM   18331 N N     . PRO A 1 4024 ? 192.293 170.401 234.893 1.00 28.96 ? 4024 PRO A N     1 
ATOM   18332 C CA    . PRO A 1 4024 ? 193.590 171.085 234.902 1.00 26.93 ? 4024 PRO A CA    1 
ATOM   18333 C C     . PRO A 1 4024 ? 194.620 170.308 234.097 1.00 28.90 ? 4024 PRO A C     1 
ATOM   18334 O O     . PRO A 1 4024 ? 194.781 169.097 234.262 1.00 28.14 ? 4024 PRO A O     1 
ATOM   18335 C CB    . PRO A 1 4024 ? 193.952 171.154 236.392 1.00 25.71 ? 4024 PRO A CB    1 
ATOM   18336 C CG    . PRO A 1 4024 ? 192.928 170.306 237.120 1.00 25.96 ? 4024 PRO A CG    1 
ATOM   18337 C CD    . PRO A 1 4024 ? 192.106 169.587 236.104 1.00 25.06 ? 4024 PRO A CD    1 
ATOM   18338 N N     . LEU A 1 4025 ? 195.316 171.021 233.216 1.00 24.53 ? 4025 LEU A N     1 
ATOM   18339 C CA    . LEU A 1 4025 ? 196.254 170.385 232.302 1.00 23.53 ? 4025 LEU A CA    1 
ATOM   18340 C C     . LEU A 1 4025 ? 197.420 169.775 233.070 1.00 26.68 ? 4025 LEU A C     1 
ATOM   18341 O O     . LEU A 1 4025 ? 197.901 170.346 234.054 1.00 27.95 ? 4025 LEU A O     1 
ATOM   18342 C CB    . LEU A 1 4025 ? 196.760 171.396 231.272 1.00 21.36 ? 4025 LEU A CB    1 
ATOM   18343 C CG    . LEU A 1 4025 ? 197.799 172.442 231.686 1.00 21.90 ? 4025 LEU A CG    1 
ATOM   18344 C CD1   . LEU A 1 4025 ? 198.422 173.071 230.456 1.00 19.56 ? 4025 LEU A CD1   1 
ATOM   18345 C CD2   . LEU A 1 4025 ? 197.186 173.515 232.572 1.00 19.74 ? 4025 LEU A CD2   1 
ATOM   18346 N N     . ASP A 1 4026 ? 197.860 168.601 232.628 1.00 22.03 ? 4026 ASP A N     1 
ATOM   18347 C CA    . ASP A 1 4026 ? 198.986 167.897 233.237 1.00 21.15 ? 4026 ASP A CA    1 
ATOM   18348 C C     . ASP A 1 4026 ? 200.163 167.960 232.270 1.00 21.70 ? 4026 ASP A C     1 
ATOM   18349 O O     . ASP A 1 4026 ? 200.157 167.317 231.218 1.00 20.23 ? 4026 ASP A O     1 
ATOM   18350 C CB    . ASP A 1 4026 ? 198.606 166.461 233.584 1.00 22.21 ? 4026 ASP A CB    1 
ATOM   18351 C CG    . ASP A 1 4026 ? 197.913 165.744 232.442 1.00 25.19 ? 4026 ASP A CG    1 
ATOM   18352 O OD1   . ASP A 1 4026 ? 197.609 166.395 231.420 1.00 26.69 ? 4026 ASP A OD1   1 
ATOM   18353 O OD2   . ASP A 1 4026 ? 197.672 164.525 232.566 1.00 26.16 ? 4026 ASP A OD2   1 
ATOM   18354 N N     . LEU A 1 4027 ? 201.177 168.745 232.632 1.00 23.70 ? 4027 LEU A N     1 
ATOM   18355 C CA    . LEU A 1 4027 ? 202.334 168.902 231.762 1.00 23.80 ? 4027 LEU A CA    1 
ATOM   18356 C C     . LEU A 1 4027 ? 203.157 167.628 231.643 1.00 28.15 ? 4027 LEU A C     1 
ATOM   18357 O O     . LEU A 1 4027 ? 203.901 167.484 230.671 1.00 24.65 ? 4027 LEU A O     1 
ATOM   18358 C CB    . LEU A 1 4027 ? 203.224 170.042 232.259 1.00 22.37 ? 4027 LEU A CB    1 
ATOM   18359 C CG    . LEU A 1 4027 ? 203.064 171.395 231.566 1.00 22.02 ? 4027 LEU A CG    1 
ATOM   18360 C CD1   . LEU A 1 4027 ? 201.613 171.836 231.567 1.00 19.92 ? 4027 LEU A CD1   1 
ATOM   18361 C CD2   . LEU A 1 4027 ? 203.947 172.441 232.226 1.00 24.36 ? 4027 LEU A CD2   1 
ATOM   18362 N N     . THR A 1 4028 ? 203.051 166.703 232.599 1.00 29.38 ? 4028 THR A N     1 
ATOM   18363 C CA    . THR A 1 4028 ? 203.903 165.518 232.556 1.00 26.43 ? 4028 THR A CA    1 
ATOM   18364 C C     . THR A 1 4028 ? 203.590 164.647 231.344 1.00 26.81 ? 4028 THR A C     1 
ATOM   18365 O O     . THR A 1 4028 ? 204.504 164.223 230.627 1.00 27.72 ? 4028 THR A O     1 
ATOM   18366 C CB    . THR A 1 4028 ? 203.782 164.727 233.866 1.00 27.05 ? 4028 THR A CB    1 
ATOM   18367 O OG1   . THR A 1 4028 ? 204.705 163.629 233.858 1.00 32.36 ? 4028 THR A OG1   1 
ATOM   18368 C CG2   . THR A 1 4028 ? 202.360 164.221 234.111 1.00 25.47 ? 4028 THR A CG2   1 
ATOM   18369 N N     . HIS A 1 4029 ? 202.305 164.407 231.071 1.00 27.23 ? 4029 HIS A N     1 
ATOM   18370 C CA    . HIS A 1 4029 ? 201.935 163.537 229.961 1.00 30.33 ? 4029 HIS A CA    1 
ATOM   18371 C C     . HIS A 1 4029 ? 202.314 164.177 228.630 1.00 29.64 ? 4029 HIS A C     1 
ATOM   18372 O O     . HIS A 1 4029 ? 202.857 163.508 227.743 1.00 24.20 ? 4029 HIS A O     1 
ATOM   18373 C CB    . HIS A 1 4029 ? 200.435 163.234 230.035 1.00 26.64 ? 4029 HIS A CB    1 
ATOM   18374 C CG    . HIS A 1 4029 ? 199.889 162.481 228.858 1.00 28.09 ? 4029 HIS A CG    1 
ATOM   18375 N ND1   . HIS A 1 4029 ? 200.702 161.977 227.866 1.00 31.61 ? 4029 HIS A ND1   1 
ATOM   18376 C CD2   . HIS A 1 4029 ? 198.619 162.202 228.477 1.00 27.30 ? 4029 HIS A CD2   1 
ATOM   18377 C CE1   . HIS A 1 4029 ? 199.960 161.385 226.948 1.00 32.72 ? 4029 HIS A CE1   1 
ATOM   18378 N NE2   . HIS A 1 4029 ? 198.692 161.507 227.295 1.00 32.38 ? 4029 HIS A NE2   1 
ATOM   18379 N N     . ILE A 1 4030 ? 202.064 165.480 228.486 1.00 27.25 ? 4030 ILE A N     1 
ATOM   18380 C CA    . ILE A 1 4030 ? 202.402 166.174 227.247 1.00 24.97 ? 4030 ILE A CA    1 
ATOM   18381 C C     . ILE A 1 4030 ? 203.909 166.192 227.031 1.00 28.34 ? 4030 ILE A C     1 
ATOM   18382 O O     . ILE A 1 4030 ? 204.399 165.843 225.951 1.00 28.89 ? 4030 ILE A O     1 
ATOM   18383 C CB    . ILE A 1 4030 ? 201.820 167.599 227.260 1.00 20.03 ? 4030 ILE A CB    1 
ATOM   18384 C CG1   . ILE A 1 4030 ? 200.407 167.602 227.848 1.00 20.86 ? 4030 ILE A CG1   1 
ATOM   18385 C CG2   . ILE A 1 4030 ? 201.831 168.189 225.864 1.00 24.83 ? 4030 ILE A CG2   1 
ATOM   18386 C CD1   . ILE A 1 4030 ? 199.392 166.870 227.005 1.00 25.85 ? 4030 ILE A CD1   1 
ATOM   18387 N N     . VAL A 1 4031 ? 204.669 166.591 228.055 1.00 22.83 ? 4031 VAL A N     1 
ATOM   18388 C CA    . VAL A 1 4031 ? 206.115 166.761 227.926 1.00 24.40 ? 4031 VAL A CA    1 
ATOM   18389 C C     . VAL A 1 4031 ? 206.873 165.453 227.777 1.00 29.32 ? 4031 VAL A C     1 
ATOM   18390 O O     . VAL A 1 4031 ? 207.814 165.389 226.975 1.00 32.89 ? 4031 VAL A O     1 
ATOM   18391 C CB    . VAL A 1 4031 ? 206.648 167.558 229.132 1.00 22.55 ? 4031 VAL A CB    1 
ATOM   18392 C CG1   . VAL A 1 4031 ? 208.154 167.629 229.104 1.00 23.81 ? 4031 VAL A CG1   1 
ATOM   18393 C CG2   . VAL A 1 4031 ? 206.083 168.968 229.114 1.00 24.00 ? 4031 VAL A CG2   1 
ATOM   18394 N N     . GLY A 1 4032 ? 206.494 164.404 228.502 1.00 26.21 ? 4032 GLY A N     1 
ATOM   18395 C CA    . GLY A 1 4032 ? 207.245 163.168 228.446 1.00 24.21 ? 4032 GLY A CA    1 
ATOM   18396 C C     . GLY A 1 4032 ? 207.172 162.431 227.126 1.00 29.06 ? 4032 GLY A C     1 
ATOM   18397 O O     . GLY A 1 4032 ? 208.134 161.759 226.741 1.00 30.82 ? 4032 GLY A O     1 
ATOM   18398 N N     . THR A 1 4033 ? 206.050 162.543 226.414 1.00 29.65 ? 4033 THR A N     1 
ATOM   18399 C CA    . THR A 1 4033 ? 205.816 161.706 225.242 1.00 29.11 ? 4033 THR A CA    1 
ATOM   18400 C C     . THR A 1 4033 ? 205.798 162.490 223.936 1.00 31.14 ? 4033 THR A C     1 
ATOM   18401 O O     . THR A 1 4033 ? 206.603 162.194 223.047 1.00 32.35 ? 4033 THR A O     1 
ATOM   18402 C CB    . THR A 1 4033 ? 204.510 160.921 225.418 1.00 28.19 ? 4033 THR A CB    1 
ATOM   18403 O OG1   . THR A 1 4033 ? 203.413 161.833 225.541 1.00 27.82 ? 4033 THR A OG1   1 
ATOM   18404 C CG2   . THR A 1 4033 ? 204.578 160.047 226.660 1.00 31.38 ? 4033 THR A CG2   1 
ATOM   18405 N N     . GLU A 1 4034 ? 204.922 163.485 223.781 1.00 27.04 ? 4034 GLU A N     1 
ATOM   18406 C CA    . GLU A 1 4034 ? 204.766 164.148 222.492 1.00 29.57 ? 4034 GLU A CA    1 
ATOM   18407 C C     . GLU A 1 4034 ? 205.385 165.542 222.453 1.00 27.06 ? 4034 GLU A C     1 
ATOM   18408 O O     . GLU A 1 4034 ? 204.956 166.381 221.654 1.00 27.33 ? 4034 GLU A O     1 
ATOM   18409 C CB    . GLU A 1 4034 ? 203.291 164.212 222.083 1.00 24.68 ? 4034 GLU A CB    1 
ATOM   18410 C CG    . GLU A 1 4034 ? 202.399 165.135 222.900 1.00 20.95 ? 4034 GLU A CG    1 
ATOM   18411 C CD    . GLU A 1 4034 ? 201.839 164.472 224.135 1.00 28.62 ? 4034 GLU A CD    1 
ATOM   18412 O OE1   . GLU A 1 4034 ? 202.367 163.416 224.539 1.00 34.39 ? 4034 GLU A OE1   1 
ATOM   18413 O OE2   . GLU A 1 4034 ? 200.850 164.997 224.687 1.00 30.15 ? 4034 GLU A OE2   1 
ATOM   18414 N N     . VAL A 1 4035 ? 206.388 165.805 223.282 1.00 20.75 ? 4035 VAL A N     1 
ATOM   18415 C CA    . VAL A 1 4035 ? 207.180 167.025 223.190 1.00 24.16 ? 4035 VAL A CA    1 
ATOM   18416 C C     . VAL A 1 4035 ? 208.615 166.610 222.900 1.00 24.75 ? 4035 VAL A C     1 
ATOM   18417 O O     . VAL A 1 4035 ? 209.316 166.103 223.784 1.00 24.26 ? 4035 VAL A O     1 
ATOM   18418 C CB    . VAL A 1 4035 ? 207.085 167.875 224.463 1.00 21.49 ? 4035 VAL A CB    1 
ATOM   18419 C CG1   . VAL A 1 4035 ? 208.113 168.991 224.431 1.00 18.31 ? 4035 VAL A CG1   1 
ATOM   18420 C CG2   . VAL A 1 4035 ? 205.690 168.455 224.598 1.00 23.71 ? 4035 VAL A CG2   1 
ATOM   18421 N N     . LYS A 1 4036 ? 209.048 166.805 221.660 1.00 25.20 ? 4036 LYS A N     1 
ATOM   18422 C CA    . LYS A 1 4036 ? 210.418 166.483 221.304 1.00 20.89 ? 4036 LYS A CA    1 
ATOM   18423 C C     . LYS A 1 4036 ? 211.370 167.457 221.993 1.00 24.01 ? 4036 LYS A C     1 
ATOM   18424 O O     . LYS A 1 4036 ? 211.032 168.631 222.174 1.00 21.42 ? 4036 LYS A O     1 
ATOM   18425 C CB    . LYS A 1 4036 ? 210.615 166.542 219.790 1.00 22.28 ? 4036 LYS A CB    1 
ATOM   18426 C CG    . LYS A 1 4036 ? 209.517 165.866 218.988 1.00 23.37 ? 4036 LYS A CG    1 
ATOM   18427 C CD    . LYS A 1 4036 ? 209.320 164.423 219.417 1.00 23.14 ? 4036 LYS A CD    1 
ATOM   18428 C CE    . LYS A 1 4036 ? 208.035 163.852 218.847 1.00 20.31 ? 4036 LYS A CE    1 
ATOM   18429 N NZ    . LYS A 1 4036 ? 207.713 162.523 219.434 1.00 21.99 ? 4036 LYS A NZ    1 
ATOM   18430 N N     . PRO A 1 4037 ? 212.558 167.003 222.394 1.00 28.98 ? 4037 PRO A N     1 
ATOM   18431 C CA    . PRO A 1 4037 ? 213.517 167.924 223.025 1.00 25.73 ? 4037 PRO A CA    1 
ATOM   18432 C C     . PRO A 1 4037 ? 213.932 169.075 222.126 1.00 24.31 ? 4037 PRO A C     1 
ATOM   18433 O O     . PRO A 1 4037 ? 214.369 170.113 222.638 1.00 23.99 ? 4037 PRO A O     1 
ATOM   18434 C CB    . PRO A 1 4037 ? 214.706 167.016 223.372 1.00 29.51 ? 4037 PRO A CB    1 
ATOM   18435 C CG    . PRO A 1 4037 ? 214.501 165.763 222.575 1.00 26.31 ? 4037 PRO A CG    1 
ATOM   18436 C CD    . PRO A 1 4037 ? 213.030 165.610 222.412 1.00 27.43 ? 4037 PRO A CD    1 
ATOM   18437 N N     . ASN A 1 4038 ? 213.820 168.925 220.804 1.00 24.08 ? 4038 ASN A N     1 
ATOM   18438 C CA    . ASN A 1 4038 ? 214.075 170.048 219.909 1.00 26.64 ? 4038 ASN A CA    1 
ATOM   18439 C C     . ASN A 1 4038 ? 213.048 171.156 220.105 1.00 28.97 ? 4038 ASN A C     1 
ATOM   18440 O O     . ASN A 1 4038 ? 213.395 172.343 220.095 1.00 25.95 ? 4038 ASN A O     1 
ATOM   18441 C CB    . ASN A 1 4038 ? 214.074 169.573 218.457 1.00 27.16 ? 4038 ASN A CB    1 
ATOM   18442 C CG    . ASN A 1 4038 ? 215.442 169.126 217.990 1.00 31.15 ? 4038 ASN A CG    1 
ATOM   18443 O OD1   . ASN A 1 4038 ? 216.415 169.871 218.091 1.00 28.48 ? 4038 ASN A OD1   1 
ATOM   18444 N ND2   . ASN A 1 4038 ? 215.524 167.904 217.479 1.00 31.92 ? 4038 ASN A ND2   1 
ATOM   18445 N N     . THR A 1 4039 ? 211.784 170.792 220.280 1.00 24.29 ? 4039 THR A N     1 
ATOM   18446 C CA    . THR A 1 4039 ? 210.729 171.786 220.418 1.00 19.01 ? 4039 THR A CA    1 
ATOM   18447 C C     . THR A 1 4039 ? 210.789 172.424 221.800 1.00 17.23 ? 4039 THR A C     1 
ATOM   18448 O O     . THR A 1 4039 ? 210.758 171.705 222.805 1.00 15.75 ? 4039 THR A O     1 
ATOM   18449 C CB    . THR A 1 4039 ? 209.359 171.156 220.198 1.00 17.43 ? 4039 THR A CB    1 
ATOM   18450 O OG1   . THR A 1 4039 ? 209.148 170.118 221.161 1.00 22.13 ? 4039 THR A OG1   1 
ATOM   18451 C CG2   . THR A 1 4039 ? 209.262 170.572 218.798 1.00 21.47 ? 4039 THR A CG2   1 
ATOM   18452 N N     . PRO A 1 4040 ? 210.880 173.745 221.898 1.00 13.40 ? 4040 PRO A N     1 
ATOM   18453 C CA    . PRO A 1 4040 ? 210.841 174.392 223.213 1.00 14.75 ? 4040 PRO A CA    1 
ATOM   18454 C C     . PRO A 1 4040 ? 209.425 174.644 223.702 1.00 16.22 ? 4040 PRO A C     1 
ATOM   18455 O O     . PRO A 1 4040 ? 208.598 175.198 222.972 1.00 17.71 ? 4040 PRO A O     1 
ATOM   18456 C CB    . PRO A 1 4040 ? 211.595 175.701 222.971 1.00 15.47 ? 4040 PRO A CB    1 
ATOM   18457 C CG    . PRO A 1 4040 ? 211.369 176.010 221.528 1.00 12.65 ? 4040 PRO A CG    1 
ATOM   18458 C CD    . PRO A 1 4040 ? 211.066 174.717 220.808 1.00 15.91 ? 4040 PRO A CD    1 
ATOM   18459 N N     . VAL A 1 4041 ? 209.136 174.249 224.940 1.00 15.19 ? 4041 VAL A N     1 
ATOM   18460 C CA    . VAL A 1 4041 ? 207.813 174.486 225.504 1.00 11.73 ? 4041 VAL A CA    1 
ATOM   18461 C C     . VAL A 1 4041 ? 207.698 175.961 225.860 1.00 12.85 ? 4041 VAL A C     1 
ATOM   18462 O O     . VAL A 1 4041 ? 208.486 176.486 226.655 1.00 16.50 ? 4041 VAL A O     1 
ATOM   18463 C CB    . VAL A 1 4041 ? 207.568 173.596 226.729 1.00 10.69 ? 4041 VAL A CB    1 
ATOM   18464 C CG1   . VAL A 1 4041 ? 206.262 173.976 227.405 1.00 9.63  ? 4041 VAL A CG1   1 
ATOM   18465 C CG2   . VAL A 1 4041 ? 207.568 172.133 226.330 1.00 13.29 ? 4041 VAL A CG2   1 
ATOM   18466 N N     . LEU A 1 4042 ? 206.720 176.636 225.265 1.00 15.83 ? 4042 LEU A N     1 
ATOM   18467 C CA    . LEU A 1 4042 ? 206.488 178.054 225.503 1.00 11.57 ? 4042 LEU A CA    1 
ATOM   18468 C C     . LEU A 1 4042 ? 205.439 178.197 226.598 1.00 13.59 ? 4042 LEU A C     1 
ATOM   18469 O O     . LEU A 1 4042 ? 204.316 177.704 226.456 1.00 17.05 ? 4042 LEU A O     1 
ATOM   18470 C CB    . LEU A 1 4042 ? 206.039 178.748 224.219 1.00 12.85 ? 4042 LEU A CB    1 
ATOM   18471 C CG    . LEU A 1 4042 ? 206.990 178.673 223.020 1.00 14.98 ? 4042 LEU A CG    1 
ATOM   18472 C CD1   . LEU A 1 4042 ? 206.717 179.813 222.063 1.00 18.96 ? 4042 LEU A CD1   1 
ATOM   18473 C CD2   . LEU A 1 4042 ? 208.444 178.692 223.464 1.00 12.36 ? 4042 LEU A CD2   1 
ATOM   18474 N N     . MET A 1 4043 ? 205.811 178.864 227.686 1.00 21.08 ? 4043 MET A N     1 
ATOM   18475 C CA    . MET A 1 4043 ? 205.016 178.889 228.912 1.00 17.99 ? 4043 MET A CA    1 
ATOM   18476 C C     . MET A 1 4043 ? 204.160 180.157 228.943 1.00 16.25 ? 4043 MET A C     1 
ATOM   18477 O O     . MET A 1 4043 ? 204.198 180.947 229.885 1.00 19.75 ? 4043 MET A O     1 
ATOM   18478 C CB    . MET A 1 4043 ? 205.948 178.821 230.121 1.00 17.17 ? 4043 MET A CB    1 
ATOM   18479 C CG    . MET A 1 4043 ? 206.632 177.470 230.367 1.00 18.55 ? 4043 MET A CG    1 
ATOM   18480 S SD    . MET A 1 4043 ? 205.680 175.944 230.406 1.00 36.72 ? 4043 MET A SD    1 
ATOM   18481 C CE    . MET A 1 4043 ? 204.428 176.370 231.607 1.00 20.32 ? 4043 MET A CE    1 
ATOM   18482 N N     . CYS A 1 4044 ? 203.380 180.346 227.878 1.00 12.51 ? 4044 CYS A N     1 
ATOM   18483 C CA    . CYS A 1 4044 ? 202.726 181.627 227.625 1.00 8.07  ? 4044 CYS A CA    1 
ATOM   18484 C C     . CYS A 1 4044 ? 201.729 181.977 228.725 1.00 15.31 ? 4044 CYS A C     1 
ATOM   18485 O O     . CYS A 1 4044 ? 200.923 181.143 229.147 1.00 19.18 ? 4044 CYS A O     1 
ATOM   18486 C CB    . CYS A 1 4044 ? 202.016 181.603 226.271 1.00 12.17 ? 4044 CYS A CB    1 
ATOM   18487 S SG    . CYS A 1 4044 ? 203.063 181.130 224.872 1.00 29.47 ? 4044 CYS A SG    1 
ATOM   18488 N N     . SER A 1 4045 ? 201.787 183.227 229.185 1.00 19.68 ? 4045 SER A N     1 
ATOM   18489 C CA    . SER A 1 4045 ? 200.943 183.700 230.273 1.00 15.24 ? 4045 SER A CA    1 
ATOM   18490 C C     . SER A 1 4045 ? 200.372 185.067 229.927 1.00 15.94 ? 4045 SER A C     1 
ATOM   18491 O O     . SER A 1 4045 ? 201.057 185.903 229.333 1.00 23.34 ? 4045 SER A O     1 
ATOM   18492 C CB    . SER A 1 4045 ? 201.723 183.792 231.589 1.00 14.00 ? 4045 SER A CB    1 
ATOM   18493 O OG    . SER A 1 4045 ? 202.248 182.534 231.965 1.00 21.15 ? 4045 SER A OG    1 
ATOM   18494 N N     . VAL A 1 4046 ? 199.118 185.284 230.311 1.00 15.99 ? 4046 VAL A N     1 
ATOM   18495 C CA    . VAL A 1 4046 ? 198.504 186.607 230.166 1.00 19.75 ? 4046 VAL A CA    1 
ATOM   18496 C C     . VAL A 1 4046 ? 199.203 187.583 231.102 1.00 24.93 ? 4046 VAL A C     1 
ATOM   18497 O O     . VAL A 1 4046 ? 199.560 187.200 232.235 1.00 27.23 ? 4046 VAL A O     1 
ATOM   18498 C CB    . VAL A 1 4046 ? 196.997 186.527 230.467 1.00 18.45 ? 4046 VAL A CB    1 
ATOM   18499 C CG1   . VAL A 1 4046 ? 196.393 187.904 230.660 1.00 17.27 ? 4046 VAL A CG1   1 
ATOM   18500 C CG2   . VAL A 1 4046 ? 196.287 185.799 229.343 1.00 21.87 ? 4046 VAL A CG2   1 
ATOM   18501 N N     . PRO A 1 4047 ? 199.447 188.832 230.696 1.00 27.68 ? 4047 PRO A N     1 
ATOM   18502 C CA    . PRO A 1 4047 ? 200.108 189.784 231.598 1.00 25.11 ? 4047 PRO A CA    1 
ATOM   18503 C C     . PRO A 1 4047 ? 199.348 189.937 232.907 1.00 23.26 ? 4047 PRO A C     1 
ATOM   18504 O O     . PRO A 1 4047 ? 198.118 190.015 232.932 1.00 25.44 ? 4047 PRO A O     1 
ATOM   18505 C CB    . PRO A 1 4047 ? 200.115 191.086 230.792 1.00 24.14 ? 4047 PRO A CB    1 
ATOM   18506 C CG    . PRO A 1 4047 ? 200.104 190.636 229.372 1.00 23.65 ? 4047 PRO A CG    1 
ATOM   18507 C CD    . PRO A 1 4047 ? 199.262 189.392 229.345 1.00 22.65 ? 4047 PRO A CD    1 
ATOM   18508 N N     . GLY A 1 4048 ? 200.101 189.989 234.001 1.00 23.22 ? 4048 GLY A N     1 
ATOM   18509 C CA    . GLY A 1 4048 ? 199.526 189.900 235.324 1.00 27.86 ? 4048 GLY A CA    1 
ATOM   18510 C C     . GLY A 1 4048 ? 199.406 188.495 235.867 1.00 26.00 ? 4048 GLY A C     1 
ATOM   18511 O O     . GLY A 1 4048 ? 198.665 188.284 236.834 1.00 25.33 ? 4048 GLY A O     1 
ATOM   18512 N N     . TYR A 1 4049 ? 200.104 187.529 235.274 1.00 20.51 ? 4049 TYR A N     1 
ATOM   18513 C CA    . TYR A 1 4049 ? 200.049 186.140 235.703 1.00 22.45 ? 4049 TYR A CA    1 
ATOM   18514 C C     . TYR A 1 4049 ? 201.401 185.486 235.469 1.00 24.50 ? 4049 TYR A C     1 
ATOM   18515 O O     . TYR A 1 4049 ? 202.124 185.833 234.532 1.00 25.33 ? 4049 TYR A O     1 
ATOM   18516 C CB    . TYR A 1 4049 ? 198.946 185.372 234.960 1.00 22.94 ? 4049 TYR A CB    1 
ATOM   18517 C CG    . TYR A 1 4049 ? 198.458 184.132 235.672 1.00 20.60 ? 4049 TYR A CG    1 
ATOM   18518 C CD1   . TYR A 1 4049 ? 199.098 182.913 235.499 1.00 19.10 ? 4049 TYR A CD1   1 
ATOM   18519 C CD2   . TYR A 1 4049 ? 197.366 184.182 236.526 1.00 18.08 ? 4049 TYR A CD2   1 
ATOM   18520 C CE1   . TYR A 1 4049 ? 198.656 181.776 236.145 1.00 26.44 ? 4049 TYR A CE1   1 
ATOM   18521 C CE2   . TYR A 1 4049 ? 196.919 183.050 237.180 1.00 17.16 ? 4049 TYR A CE2   1 
ATOM   18522 C CZ    . TYR A 1 4049 ? 197.567 181.851 236.985 1.00 27.09 ? 4049 TYR A CZ    1 
ATOM   18523 O OH    . TYR A 1 4049 ? 197.125 180.722 237.635 1.00 27.55 ? 4049 TYR A OH    1 
ATOM   18524 N N     . ASP A 1 4050 ? 201.734 184.532 236.336 1.00 27.05 ? 4050 ASP A N     1 
ATOM   18525 C CA    . ASP A 1 4050 ? 202.977 183.782 236.251 1.00 27.58 ? 4050 ASP A CA    1 
ATOM   18526 C C     . ASP A 1 4050 ? 202.664 182.295 236.198 1.00 30.76 ? 4050 ASP A C     1 
ATOM   18527 O O     . ASP A 1 4050 ? 201.777 181.814 236.909 1.00 28.62 ? 4050 ASP A O     1 
ATOM   18528 C CB    . ASP A 1 4050 ? 203.896 184.080 237.440 1.00 29.30 ? 4050 ASP A CB    1 
ATOM   18529 C CG    . ASP A 1 4050 ? 205.247 183.407 237.313 1.00 31.34 ? 4050 ASP A CG    1 
ATOM   18530 O OD1   . ASP A 1 4050 ? 205.720 183.238 236.170 1.00 29.63 ? 4050 ASP A OD1   1 
ATOM   18531 O OD2   . ASP A 1 4050 ? 205.832 183.044 238.355 1.00 30.88 ? 4050 ASP A OD2   1 
ATOM   18532 N N     . ALA A 1 4051 ? 203.399 181.571 235.355 1.00 30.53 ? 4051 ALA A N     1 
ATOM   18533 C CA    . ALA A 1 4051 ? 203.173 180.145 235.156 1.00 29.75 ? 4051 ALA A CA    1 
ATOM   18534 C C     . ALA A 1 4051 ? 204.386 179.298 235.515 1.00 28.39 ? 4051 ALA A C     1 
ATOM   18535 O O     . ALA A 1 4051 ? 204.458 178.134 235.103 1.00 28.28 ? 4051 ALA A O     1 
ATOM   18536 C CB    . ALA A 1 4051 ? 202.759 179.870 233.710 1.00 26.81 ? 4051 ALA A CB    1 
ATOM   18537 N N     . SER A 1 4052 ? 205.344 179.847 236.262 1.00 26.72 ? 4052 SER A N     1 
ATOM   18538 C CA    . SER A 1 4052 ? 206.486 179.048 236.688 1.00 28.43 ? 4052 SER A CA    1 
ATOM   18539 C C     . SER A 1 4052 ? 206.081 178.000 237.715 1.00 32.05 ? 4052 SER A C     1 
ATOM   18540 O O     . SER A 1 4052 ? 206.692 176.927 237.777 1.00 31.41 ? 4052 SER A O     1 
ATOM   18541 C CB    . SER A 1 4052 ? 207.579 179.956 237.253 1.00 29.35 ? 4052 SER A CB    1 
ATOM   18542 O OG    . SER A 1 4052 ? 208.158 180.749 236.232 1.00 33.29 ? 4052 SER A OG    1 
ATOM   18543 N N     . GLY A 1 4053 ? 205.052 178.286 238.516 1.00 33.21 ? 4053 GLY A N     1 
ATOM   18544 C CA    . GLY A 1 4053 ? 204.639 177.353 239.550 1.00 32.30 ? 4053 GLY A CA    1 
ATOM   18545 C C     . GLY A 1 4053 ? 204.190 176.011 239.007 1.00 34.15 ? 4053 GLY A C     1 
ATOM   18546 O O     . GLY A 1 4053 ? 204.445 174.972 239.623 1.00 30.63 ? 4053 GLY A O     1 
ATOM   18547 N N     . HIS A 1 4054 ? 203.517 176.010 237.854 1.00 30.54 ? 4054 HIS A N     1 
ATOM   18548 C CA    . HIS A 1 4054 ? 203.064 174.756 237.260 1.00 29.96 ? 4054 HIS A CA    1 
ATOM   18549 C C     . HIS A 1 4054 ? 204.234 173.819 236.980 1.00 31.15 ? 4054 HIS A C     1 
ATOM   18550 O O     . HIS A 1 4054 ? 204.224 172.653 237.392 1.00 34.35 ? 4054 HIS A O     1 
ATOM   18551 C CB    . HIS A 1 4054 ? 202.280 175.036 235.977 1.00 28.90 ? 4054 HIS A CB    1 
ATOM   18552 C CG    . HIS A 1 4054 ? 201.115 175.957 236.168 1.00 28.55 ? 4054 HIS A CG    1 
ATOM   18553 N ND1   . HIS A 1 4054 ? 201.231 177.330 236.114 1.00 28.72 ? 4054 HIS A ND1   1 
ATOM   18554 C CD2   . HIS A 1 4054 ? 199.809 175.699 236.415 1.00 30.78 ? 4054 HIS A CD2   1 
ATOM   18555 C CE1   . HIS A 1 4054 ? 200.046 177.877 236.318 1.00 29.57 ? 4054 HIS A CE1   1 
ATOM   18556 N NE2   . HIS A 1 4054 ? 199.166 176.910 236.504 1.00 34.10 ? 4054 HIS A NE2   1 
ATOM   18557 N N     . VAL A 1 4055 ? 205.272 174.316 236.306 1.00 28.86 ? 4055 VAL A N     1 
ATOM   18558 C CA    . VAL A 1 4055 ? 206.383 173.436 235.961 1.00 31.55 ? 4055 VAL A CA    1 
ATOM   18559 C C     . VAL A 1 4055 ? 207.290 173.202 237.166 1.00 35.50 ? 4055 VAL A C     1 
ATOM   18560 O O     . VAL A 1 4055 ? 207.999 172.191 237.227 1.00 34.79 ? 4055 VAL A O     1 
ATOM   18561 C CB    . VAL A 1 4055 ? 207.159 174.000 234.758 1.00 28.90 ? 4055 VAL A CB    1 
ATOM   18562 C CG1   . VAL A 1 4055 ? 207.875 175.255 235.148 1.00 26.07 ? 4055 VAL A CG1   1 
ATOM   18563 C CG2   . VAL A 1 4055 ? 208.135 172.965 234.211 1.00 33.55 ? 4055 VAL A CG2   1 
ATOM   18564 N N     . GLU A 1 4056 ? 207.279 174.104 238.149 1.00 34.99 ? 4056 GLU A N     1 
ATOM   18565 C CA    . GLU A 1 4056 ? 207.990 173.825 239.393 1.00 31.67 ? 4056 GLU A CA    1 
ATOM   18566 C C     . GLU A 1 4056 ? 207.368 172.634 240.113 1.00 34.28 ? 4056 GLU A C     1 
ATOM   18567 O O     . GLU A 1 4056 ? 208.077 171.739 240.589 1.00 34.25 ? 4056 GLU A O     1 
ATOM   18568 C CB    . GLU A 1 4056 ? 207.999 175.063 240.289 1.00 33.95 ? 4056 GLU A CB    1 
ATOM   18569 C CG    . GLU A 1 4056 ? 208.939 176.164 239.813 1.00 34.76 ? 4056 GLU A CG    1 
ATOM   18570 C CD    . GLU A 1 4056 ? 210.369 175.688 239.623 1.00 37.49 ? 4056 GLU A CD    1 
ATOM   18571 O OE1   . GLU A 1 4056 ? 210.821 174.815 240.393 1.00 37.30 ? 4056 GLU A OE1   1 
ATOM   18572 O OE2   . GLU A 1 4056 ? 211.043 176.190 238.698 1.00 36.57 ? 4056 GLU A OE2   1 
ATOM   18573 N N     . ASP A 1 4057 ? 206.035 172.596 240.188 1.00 34.48 ? 4057 ASP A N     1 
ATOM   18574 C CA    . ASP A 1 4057 ? 205.360 171.426 240.740 1.00 35.54 ? 4057 ASP A CA    1 
ATOM   18575 C C     . ASP A 1 4057 ? 205.574 170.196 239.867 1.00 35.49 ? 4057 ASP A C     1 
ATOM   18576 O O     . ASP A 1 4057 ? 205.670 169.076 240.385 1.00 37.10 ? 4057 ASP A O     1 
ATOM   18577 C CB    . ASP A 1 4057 ? 203.869 171.710 240.912 1.00 36.80 ? 4057 ASP A CB    1 
ATOM   18578 C CG    . ASP A 1 4057 ? 203.595 172.726 242.004 1.00 39.98 ? 4057 ASP A CG    1 
ATOM   18579 O OD1   . ASP A 1 4057 ? 204.396 172.799 242.960 1.00 40.00 ? 4057 ASP A OD1   1 
ATOM   18580 O OD2   . ASP A 1 4057 ? 202.582 173.449 241.908 1.00 38.16 ? 4057 ASP A OD2   1 
ATOM   18581 N N     . LEU A 1 4058 ? 205.645 170.385 238.547 1.00 32.45 ? 4058 LEU A N     1 
ATOM   18582 C CA    . LEU A 1 4058 ? 205.987 169.285 237.650 1.00 31.86 ? 4058 LEU A CA    1 
ATOM   18583 C C     . LEU A 1 4058 ? 207.340 168.678 238.003 1.00 34.02 ? 4058 LEU A C     1 
ATOM   18584 O O     . LEU A 1 4058 ? 207.474 167.453 238.109 1.00 30.78 ? 4058 LEU A O     1 
ATOM   18585 C CB    . LEU A 1 4058 ? 205.993 169.785 236.207 1.00 30.66 ? 4058 LEU A CB    1 
ATOM   18586 C CG    . LEU A 1 4058 ? 206.314 168.748 235.136 1.00 32.98 ? 4058 LEU A CG    1 
ATOM   18587 C CD1   . LEU A 1 4058 ? 205.061 167.986 234.805 1.00 31.18 ? 4058 LEU A CD1   1 
ATOM   18588 C CD2   . LEU A 1 4058 ? 206.891 169.411 233.895 1.00 34.35 ? 4058 LEU A CD2   1 
ATOM   18589 N N     . ALA A 1 4059 ? 208.355 169.522 238.180 1.00 37.50 ? 4059 ALA A N     1 
ATOM   18590 C CA    . ALA A 1 4059 ? 209.679 169.032 238.544 1.00 37.06 ? 4059 ALA A CA    1 
ATOM   18591 C C     . ALA A 1 4059 ? 209.668 168.396 239.927 1.00 34.69 ? 4059 ALA A C     1 
ATOM   18592 O O     . ALA A 1 4059 ? 210.360 167.401 240.166 1.00 32.97 ? 4059 ALA A O     1 
ATOM   18593 C CB    . ALA A 1 4059 ? 210.694 170.171 238.484 1.00 34.47 ? 4059 ALA A CB    1 
ATOM   18594 N N     . ALA A 1 4060 ? 208.893 168.964 240.854 1.00 31.14 ? 4060 ALA A N     1 
ATOM   18595 C CA    . ALA A 1 4060 ? 208.806 168.391 242.193 1.00 34.09 ? 4060 ALA A CA    1 
ATOM   18596 C C     . ALA A 1 4060 ? 208.222 166.984 242.157 1.00 35.28 ? 4060 ALA A C     1 
ATOM   18597 O O     . ALA A 1 4060 ? 208.730 166.077 242.826 1.00 37.51 ? 4060 ALA A O     1 
ATOM   18598 C CB    . ALA A 1 4060 ? 207.971 169.297 243.098 1.00 33.89 ? 4060 ALA A CB    1 
ATOM   18599 N N     . GLU A 1 4061 ? 207.157 166.780 241.376 1.00 34.64 ? 4061 GLU A N     1 
ATOM   18600 C CA    . GLU A 1 4061 ? 206.546 165.455 241.317 1.00 32.97 ? 4061 GLU A CA    1 
ATOM   18601 C C     . GLU A 1 4061 ? 207.385 164.482 240.497 1.00 37.18 ? 4061 GLU A C     1 
ATOM   18602 O O     . GLU A 1 4061 ? 207.359 163.275 240.760 1.00 35.27 ? 4061 GLU A O     1 
ATOM   18603 C CB    . GLU A 1 4061 ? 205.122 165.545 240.758 1.00 33.75 ? 4061 GLU A CB    1 
ATOM   18604 C CG    . GLU A 1 4061 ? 205.005 166.084 239.340 1.00 34.69 ? 4061 GLU A CG    1 
ATOM   18605 C CD    . GLU A 1 4061 ? 205.173 165.008 238.282 1.00 36.88 ? 4061 GLU A CD    1 
ATOM   18606 O OE1   . GLU A 1 4061 ? 205.008 163.816 238.613 1.00 38.47 ? 4061 GLU A OE1   1 
ATOM   18607 O OE2   . GLU A 1 4061 ? 205.472 165.356 237.120 1.00 36.28 ? 4061 GLU A OE2   1 
ATOM   18608 N N     . GLN A 1 4062 ? 208.126 164.976 239.508 1.00 40.42 ? 4062 GLN A N     1 
ATOM   18609 C CA    . GLN A 1 4062 ? 208.957 164.127 238.666 1.00 40.35 ? 4062 GLN A CA    1 
ATOM   18610 C C     . GLN A 1 4062 ? 210.413 164.094 239.129 1.00 41.80 ? 4062 GLN A C     1 
ATOM   18611 O O     . GLN A 1 4062 ? 211.235 163.411 238.508 1.00 35.99 ? 4062 GLN A O     1 
ATOM   18612 C CB    . GLN A 1 4062 ? 208.839 164.599 237.206 1.00 38.61 ? 4062 GLN A CB    1 
ATOM   18613 C CG    . GLN A 1 4062 ? 209.551 163.755 236.156 1.00 39.34 ? 4062 GLN A CG    1 
ATOM   18614 C CD    . GLN A 1 4062 ? 209.302 164.257 234.750 1.00 37.68 ? 4062 GLN A CD    1 
ATOM   18615 O OE1   . GLN A 1 4062 ? 208.616 165.258 234.552 1.00 38.46 ? 4062 GLN A OE1   1 
ATOM   18616 N NE2   . GLN A 1 4062 ? 209.864 163.567 233.765 1.00 36.33 ? 4062 GLN A NE2   1 
ATOM   18617 N N     . ASN A 1 4063 ? 210.730 164.781 240.228 1.00 43.66 ? 4063 ASN A N     1 
ATOM   18618 C CA    . ASN A 1 4063 ? 212.074 164.840 240.818 1.00 43.51 ? 4063 ASN A CA    1 
ATOM   18619 C C     . ASN A 1 4063 ? 213.157 165.019 239.754 1.00 44.32 ? 4063 ASN A C     1 
ATOM   18620 O O     . ASN A 1 4063 ? 214.114 164.247 239.655 1.00 42.08 ? 4063 ASN A O     1 
ATOM   18621 C CB    . ASN A 1 4063 ? 212.351 163.618 241.702 1.00 39.94 ? 4063 ASN A CB    1 
ATOM   18622 C CG    . ASN A 1 4063 ? 212.315 162.308 240.941 1.00 44.22 ? 4063 ASN A CG    1 
ATOM   18623 O OD1   . ASN A 1 4063 ? 211.266 161.677 240.816 1.00 46.35 ? 4063 ASN A OD1   1 
ATOM   18624 N ND2   . ASN A 1 4063 ? 213.464 161.894 240.422 1.00 44.64 ? 4063 ASN A ND2   1 
ATOM   18625 N N     . THR A 1 4064 ? 213.000 166.069 238.952 1.00 39.90 ? 4064 THR A N     1 
ATOM   18626 C CA    . THR A 1 4064 ? 213.984 166.462 237.953 1.00 37.78 ? 4064 THR A CA    1 
ATOM   18627 C C     . THR A 1 4064 ? 214.464 167.871 238.268 1.00 37.90 ? 4064 THR A C     1 
ATOM   18628 O O     . THR A 1 4064 ? 213.647 168.775 238.474 1.00 36.74 ? 4064 THR A O     1 
ATOM   18629 C CB    . THR A 1 4064 ? 213.395 166.402 236.541 1.00 37.55 ? 4064 THR A CB    1 
ATOM   18630 O OG1   . THR A 1 4064 ? 212.919 165.077 236.276 1.00 35.98 ? 4064 THR A OG1   1 
ATOM   18631 C CG2   . THR A 1 4064 ? 214.449 166.769 235.508 1.00 36.86 ? 4064 THR A CG2   1 
ATOM   18632 N N     . GLN A 1 4065 ? 215.781 168.057 238.309 1.00 37.99 ? 4065 GLN A N     1 
ATOM   18633 C CA    . GLN A 1 4065 ? 216.332 169.354 238.676 1.00 39.55 ? 4065 GLN A CA    1 
ATOM   18634 C C     . GLN A 1 4065 ? 216.149 170.354 237.538 1.00 39.35 ? 4065 GLN A C     1 
ATOM   18635 O O     . GLN A 1 4065 ? 216.139 169.994 236.357 1.00 37.18 ? 4065 GLN A O     1 
ATOM   18636 C CB    . GLN A 1 4065 ? 217.813 169.227 239.043 1.00 38.12 ? 4065 GLN A CB    1 
ATOM   18637 C CG    . GLN A 1 4065 ? 218.761 169.056 237.866 1.00 39.24 ? 4065 GLN A CG    1 
ATOM   18638 C CD    . GLN A 1 4065 ? 219.338 170.379 237.393 1.00 40.46 ? 4065 GLN A CD    1 
ATOM   18639 O OE1   . GLN A 1 4065 ? 219.536 171.299 238.186 1.00 39.36 ? 4065 GLN A OE1   1 
ATOM   18640 N NE2   . GLN A 1 4065 ? 219.599 170.484 236.097 1.00 39.40 ? 4065 GLN A NE2   1 
ATOM   18641 N N     . ILE A 1 4066 ? 215.996 171.623 237.906 1.00 37.00 ? 4066 ILE A N     1 
ATOM   18642 C CA    . ILE A 1 4066 ? 215.768 172.706 236.958 1.00 34.45 ? 4066 ILE A CA    1 
ATOM   18643 C C     . ILE A 1 4066 ? 216.860 173.750 237.143 1.00 35.12 ? 4066 ILE A C     1 
ATOM   18644 O O     . ILE A 1 4066 ? 217.132 174.177 238.271 1.00 39.46 ? 4066 ILE A O     1 
ATOM   18645 C CB    . ILE A 1 4066 ? 214.380 173.346 237.144 1.00 33.77 ? 4066 ILE A CB    1 
ATOM   18646 C CG1   . ILE A 1 4066 ? 213.298 172.272 237.252 1.00 35.62 ? 4066 ILE A CG1   1 
ATOM   18647 C CG2   . ILE A 1 4066 ? 214.073 174.287 235.993 1.00 30.71 ? 4066 ILE A CG2   1 
ATOM   18648 C CD1   . ILE A 1 4066 ? 213.165 171.409 236.024 1.00 35.61 ? 4066 ILE A CD1   1 
ATOM   18649 N N     . THR A 1 4067 ? 217.484 174.155 236.039 1.00 26.79 ? 4067 THR A N     1 
ATOM   18650 C CA    . THR A 1 4067 ? 218.435 175.267 236.054 1.00 28.84 ? 4067 THR A CA    1 
ATOM   18651 C C     . THR A 1 4067 ? 217.725 176.550 235.613 1.00 27.74 ? 4067 THR A C     1 
ATOM   18652 O O     . THR A 1 4067 ? 218.012 177.153 234.576 1.00 25.45 ? 4067 THR A O     1 
ATOM   18653 C CB    . THR A 1 4067 ? 219.653 174.941 235.194 1.00 31.24 ? 4067 THR A CB    1 
ATOM   18654 O OG1   . THR A 1 4067 ? 220.547 176.063 235.168 1.00 33.51 ? 4067 THR A OG1   1 
ATOM   18655 C CG2   . THR A 1 4067 ? 219.258 174.535 233.777 1.00 27.92 ? 4067 THR A CG2   1 
ATOM   18656 N N     . SER A 1 4068 ? 216.779 176.969 236.453 1.00 26.68 ? 4068 SER A N     1 
ATOM   18657 C CA    . SER A 1 4068 ? 215.977 178.153 236.172 1.00 26.28 ? 4068 SER A CA    1 
ATOM   18658 C C     . SER A 1 4068 ? 216.860 179.384 236.013 1.00 27.11 ? 4068 SER A C     1 
ATOM   18659 O O     . SER A 1 4068 ? 217.810 179.587 236.774 1.00 33.75 ? 4068 SER A O     1 
ATOM   18660 C CB    . SER A 1 4068 ? 214.963 178.375 237.293 1.00 25.41 ? 4068 SER A CB    1 
ATOM   18661 O OG    . SER A 1 4068 ? 214.276 179.599 237.117 1.00 27.20 ? 4068 SER A OG    1 
ATOM   18662 N N     . ILE A 1 4069 ? 216.544 180.204 235.014 1.00 18.90 ? 4069 ILE A N     1 
ATOM   18663 C CA    . ILE A 1 4069 ? 217.349 181.369 234.667 1.00 21.52 ? 4069 ILE A CA    1 
ATOM   18664 C C     . ILE A 1 4069 ? 216.419 182.551 234.434 1.00 25.98 ? 4069 ILE A C     1 
ATOM   18665 O O     . ILE A 1 4069 ? 215.413 182.425 233.729 1.00 26.60 ? 4069 ILE A O     1 
ATOM   18666 C CB    . ILE A 1 4069 ? 218.212 181.108 233.418 1.00 26.16 ? 4069 ILE A CB    1 
ATOM   18667 C CG1   . ILE A 1 4069 ? 219.347 180.141 233.751 1.00 27.12 ? 4069 ILE A CG1   1 
ATOM   18668 C CG2   . ILE A 1 4069 ? 218.773 182.409 232.864 1.00 25.23 ? 4069 ILE A CG2   1 
ATOM   18669 C CD1   . ILE A 1 4069 ? 219.789 179.308 232.578 1.00 26.43 ? 4069 ILE A CD1   1 
ATOM   18670 N N     . ALA A 1 4070 ? 216.748 183.694 235.029 1.00 28.96 ? 4070 ALA A N     1 
ATOM   18671 C CA    . ALA A 1 4070 ? 216.025 184.926 234.754 1.00 27.63 ? 4070 ALA A CA    1 
ATOM   18672 C C     . ALA A 1 4070 ? 216.638 185.633 233.553 1.00 28.45 ? 4070 ALA A C     1 
ATOM   18673 O O     . ALA A 1 4070 ? 217.857 185.609 233.355 1.00 29.28 ? 4070 ALA A O     1 
ATOM   18674 C CB    . ALA A 1 4070 ? 216.043 185.846 235.974 1.00 26.45 ? 4070 ALA A CB    1 
ATOM   18675 N N     . ILE A 1 4071 ? 215.787 186.264 232.748 1.00 27.80 ? 4071 ILE A N     1 
ATOM   18676 C CA    . ILE A 1 4071 ? 216.195 186.903 231.502 1.00 29.19 ? 4071 ILE A CA    1 
ATOM   18677 C C     . ILE A 1 4071 ? 216.077 188.411 231.668 1.00 30.68 ? 4071 ILE A C     1 
ATOM   18678 O O     . ILE A 1 4071 ? 215.079 188.908 232.204 1.00 32.77 ? 4071 ILE A O     1 
ATOM   18679 C CB    . ILE A 1 4071 ? 215.353 186.407 230.315 1.00 28.81 ? 4071 ILE A CB    1 
ATOM   18680 C CG1   . ILE A 1 4071 ? 215.539 184.901 230.130 1.00 29.92 ? 4071 ILE A CG1   1 
ATOM   18681 C CG2   . ILE A 1 4071 ? 215.728 187.144 229.039 1.00 29.13 ? 4071 ILE A CG2   1 
ATOM   18682 C CD1   . ILE A 1 4071 ? 216.979 184.489 229.916 1.00 30.63 ? 4071 ILE A CD1   1 
ATOM   18683 N N     . GLY A 1 4072 ? 217.095 189.137 231.210 1.00 34.86 ? 4072 GLY A N     1 
ATOM   18684 C CA    . GLY A 1 4072 ? 217.106 190.583 231.313 1.00 36.78 ? 4072 GLY A CA    1 
ATOM   18685 C C     . GLY A 1 4072 ? 218.476 191.153 231.618 1.00 36.40 ? 4072 GLY A C     1 
ATOM   18686 O O     . GLY A 1 4072 ? 218.754 192.315 231.308 1.00 36.51 ? 4072 GLY A O     1 
ATOM   18687 N N     . SER A 1 4073 ? 219.339 190.347 232.228 1.00 37.31 ? 4073 SER A N     1 
ATOM   18688 C CA    . SER A 1 4073 ? 220.694 190.768 232.548 1.00 37.83 ? 4073 SER A CA    1 
ATOM   18689 C C     . SER A 1 4073 ? 221.631 190.501 231.375 1.00 38.63 ? 4073 SER A C     1 
ATOM   18690 O O     . SER A 1 4073 ? 221.446 189.552 230.609 1.00 36.82 ? 4073 SER A O     1 
ATOM   18691 C CB    . SER A 1 4073 ? 221.205 190.044 233.795 1.00 35.61 ? 4073 SER A CB    1 
ATOM   18692 O OG    . SER A 1 4073 ? 222.547 190.398 234.078 1.00 36.08 ? 4073 SER A OG    1 
ATOM   18693 N N     . ALA A 1 4074 ? 222.641 191.363 231.237 1.00 36.91 ? 4074 ALA A N     1 
ATOM   18694 C CA    . ALA A 1 4074 ? 223.643 191.165 230.194 1.00 36.29 ? 4074 ALA A CA    1 
ATOM   18695 C C     . ALA A 1 4074 ? 224.422 189.875 230.419 1.00 36.55 ? 4074 ALA A C     1 
ATOM   18696 O O     . ALA A 1 4074 ? 224.649 189.105 229.478 1.00 34.55 ? 4074 ALA A O     1 
ATOM   18697 C CB    . ALA A 1 4074 ? 224.590 192.363 230.138 1.00 36.16 ? 4074 ALA A CB    1 
ATOM   18698 N N     . GLU A 1 4075 ? 224.839 189.622 231.661 1.00 39.35 ? 4075 GLU A N     1 
ATOM   18699 C CA    . GLU A 1 4075 ? 225.499 188.364 231.987 1.00 41.11 ? 4075 GLU A CA    1 
ATOM   18700 C C     . GLU A 1 4075 ? 224.509 187.208 232.044 1.00 43.17 ? 4075 GLU A C     1 
ATOM   18701 O O     . GLU A 1 4075 ? 224.917 186.045 231.928 1.00 43.59 ? 4075 GLU A O     1 
ATOM   18702 C CB    . GLU A 1 4075 ? 226.245 188.500 233.319 1.00 40.21 ? 4075 GLU A CB    1 
ATOM   18703 C CG    . GLU A 1 4075 ? 227.104 187.302 233.712 1.00 39.70 ? 4075 GLU A CG    1 
ATOM   18704 C CD    . GLU A 1 4075 ? 227.873 186.716 232.541 1.00 42.64 ? 4075 GLU A CD    1 
ATOM   18705 O OE1   . GLU A 1 4075 ? 228.570 187.479 231.839 1.00 41.75 ? 4075 GLU A OE1   1 
ATOM   18706 O OE2   . GLU A 1 4075 ? 227.783 185.489 232.324 1.00 43.14 ? 4075 GLU A OE2   1 
ATOM   18707 N N     . GLY A 1 4076 ? 223.219 187.505 232.214 1.00 37.13 ? 4076 GLY A N     1 
ATOM   18708 C CA    . GLY A 1 4076 ? 222.219 186.452 232.204 1.00 37.14 ? 4076 GLY A CA    1 
ATOM   18709 C C     . GLY A 1 4076 ? 222.157 185.723 230.877 1.00 36.77 ? 4076 GLY A C     1 
ATOM   18710 O O     . GLY A 1 4076 ? 221.907 184.518 230.832 1.00 34.36 ? 4076 GLY A O     1 
ATOM   18711 N N     . PHE A 1 4077 ? 222.389 186.443 229.777 1.00 37.36 ? 4077 PHE A N     1 
ATOM   18712 C CA    . PHE A 1 4077 ? 222.394 185.811 228.462 1.00 35.27 ? 4077 PHE A CA    1 
ATOM   18713 C C     . PHE A 1 4077 ? 223.519 184.791 228.354 1.00 37.46 ? 4077 PHE A C     1 
ATOM   18714 O O     . PHE A 1 4077 ? 223.314 183.665 227.886 1.00 35.25 ? 4077 PHE A O     1 
ATOM   18715 C CB    . PHE A 1 4077 ? 222.538 186.873 227.375 1.00 35.10 ? 4077 PHE A CB    1 
ATOM   18716 C CG    . PHE A 1 4077 ? 221.284 187.642 227.115 1.00 36.73 ? 4077 PHE A CG    1 
ATOM   18717 C CD1   . PHE A 1 4077 ? 221.255 188.635 226.154 1.00 34.81 ? 4077 PHE A CD1   1 
ATOM   18718 C CD2   . PHE A 1 4077 ? 220.136 187.384 227.843 1.00 35.89 ? 4077 PHE A CD2   1 
ATOM   18719 C CE1   . PHE A 1 4077 ? 220.104 189.348 225.920 1.00 33.40 ? 4077 PHE A CE1   1 
ATOM   18720 C CE2   . PHE A 1 4077 ? 218.985 188.095 227.613 1.00 36.22 ? 4077 PHE A CE2   1 
ATOM   18721 C CZ    . PHE A 1 4077 ? 218.972 189.079 226.653 1.00 34.80 ? 4077 PHE A CZ    1 
ATOM   18722 N N     . ASN A 1 4078 ? 224.722 185.177 228.783 1.00 40.37 ? 4078 ASN A N     1 
ATOM   18723 C CA    . ASN A 1 4078 ? 225.854 184.259 228.747 1.00 39.82 ? 4078 ASN A CA    1 
ATOM   18724 C C     . ASN A 1 4078 ? 225.629 183.078 229.681 1.00 38.10 ? 4078 ASN A C     1 
ATOM   18725 O O     . ASN A 1 4078 ? 225.982 181.940 229.352 1.00 36.94 ? 4078 ASN A O     1 
ATOM   18726 C CB    . ASN A 1 4078 ? 227.138 185.002 229.113 1.00 37.12 ? 4078 ASN A CB    1 
ATOM   18727 C CG    . ASN A 1 4078 ? 227.434 186.149 228.166 1.00 40.32 ? 4078 ASN A CG    1 
ATOM   18728 O OD1   . ASN A 1 4078 ? 227.024 186.132 227.005 1.00 39.21 ? 4078 ASN A OD1   1 
ATOM   18729 N ND2   . ASN A 1 4078 ? 228.142 187.157 228.660 1.00 40.28 ? 4078 ASN A ND2   1 
ATOM   18730 N N     . GLN A 1 4079 ? 225.039 183.329 230.852 1.00 32.38 ? 4079 GLN A N     1 
ATOM   18731 C CA    . GLN A 1 4079 ? 224.758 182.240 231.781 1.00 35.59 ? 4079 GLN A CA    1 
ATOM   18732 C C     . GLN A 1 4079 ? 223.745 181.261 231.194 1.00 36.43 ? 4079 GLN A C     1 
ATOM   18733 O O     . GLN A 1 4079 ? 223.906 180.041 231.317 1.00 34.47 ? 4079 GLN A O     1 
ATOM   18734 C CB    . GLN A 1 4079 ? 224.265 182.807 233.112 1.00 34.33 ? 4079 GLN A CB    1 
ATOM   18735 C CG    . GLN A 1 4079 ? 224.130 181.780 234.221 1.00 35.82 ? 4079 GLN A CG    1 
ATOM   18736 C CD    . GLN A 1 4079 ? 222.690 181.388 234.480 1.00 37.00 ? 4079 GLN A CD    1 
ATOM   18737 O OE1   . GLN A 1 4079 ? 221.780 182.206 234.347 1.00 36.63 ? 4079 GLN A OE1   1 
ATOM   18738 N NE2   . GLN A 1 4079 ? 222.476 180.133 234.856 1.00 35.51 ? 4079 GLN A NE2   1 
ATOM   18739 N N     . ALA A 1 4080 ? 222.703 181.779 230.538 1.00 36.80 ? 4080 ALA A N     1 
ATOM   18740 C CA    . ALA A 1 4080 ? 221.719 180.913 229.897 1.00 34.40 ? 4080 ALA A CA    1 
ATOM   18741 C C     . ALA A 1 4080 ? 222.334 180.129 228.746 1.00 35.64 ? 4080 ALA A C     1 
ATOM   18742 O O     . ALA A 1 4080 ? 222.021 178.949 228.557 1.00 33.48 ? 4080 ALA A O     1 
ATOM   18743 C CB    . ALA A 1 4080 ? 220.531 181.740 229.407 1.00 33.94 ? 4080 ALA A CB    1 
ATOM   18744 N N     . ASP A 1 4081 ? 223.206 180.767 227.962 1.00 37.31 ? 4081 ASP A N     1 
ATOM   18745 C CA    . ASP A 1 4081 ? 223.877 180.061 226.874 1.00 37.39 ? 4081 ASP A CA    1 
ATOM   18746 C C     . ASP A 1 4081 ? 224.773 178.949 227.408 1.00 37.22 ? 4081 ASP A C     1 
ATOM   18747 O O     . ASP A 1 4081 ? 224.809 177.847 226.848 1.00 33.24 ? 4081 ASP A O     1 
ATOM   18748 C CB    . ASP A 1 4081 ? 224.686 181.046 226.030 1.00 36.75 ? 4081 ASP A CB    1 
ATOM   18749 C CG    . ASP A 1 4081 ? 225.391 180.376 224.867 1.00 39.28 ? 4081 ASP A CG    1 
ATOM   18750 O OD1   . ASP A 1 4081 ? 226.535 180.770 224.557 1.00 39.22 ? 4081 ASP A OD1   1 
ATOM   18751 O OD2   . ASP A 1 4081 ? 224.802 179.455 224.263 1.00 37.25 ? 4081 ASP A OD2   1 
ATOM   18752 N N     . LYS A 1 4082 ? 225.506 179.221 228.490 1.00 39.74 ? 4082 LYS A N     1 
ATOM   18753 C CA    . LYS A 1 4082 ? 226.344 178.188 229.092 1.00 41.13 ? 4082 LYS A CA    1 
ATOM   18754 C C     . LYS A 1 4082 ? 225.499 177.047 229.644 1.00 40.80 ? 4082 LYS A C     1 
ATOM   18755 O O     . LYS A 1 4082 ? 225.876 175.876 229.529 1.00 40.08 ? 4082 LYS A O     1 
ATOM   18756 C CB    . LYS A 1 4082 ? 227.221 178.793 230.188 1.00 38.07 ? 4082 LYS A CB    1 
ATOM   18757 C CG    . LYS A 1 4082 ? 228.638 179.132 229.737 1.00 40.36 ? 4082 LYS A CG    1 
ATOM   18758 C CD    . LYS A 1 4082 ? 228.647 180.247 228.703 1.00 38.74 ? 4082 LYS A CD    1 
ATOM   18759 C CE    . LYS A 1 4082 ? 230.061 180.710 228.396 1.00 39.62 ? 4082 LYS A CE    1 
ATOM   18760 N NZ    . LYS A 1 4082 ? 230.117 181.533 227.157 1.00 39.31 ? 4082 LYS A NZ    1 
ATOM   18761 N N     . ALA A 1 4083 ? 224.352 177.370 230.249 1.00 38.65 ? 4083 ALA A N     1 
ATOM   18762 C CA    . ALA A 1 4083 ? 223.451 176.325 230.726 1.00 38.07 ? 4083 ALA A CA    1 
ATOM   18763 C C     . ALA A 1 4083 ? 222.915 175.490 229.570 1.00 37.20 ? 4083 ALA A C     1 
ATOM   18764 O O     . ALA A 1 4083 ? 222.779 174.268 229.688 1.00 35.39 ? 4083 ALA A O     1 
ATOM   18765 C CB    . ALA A 1 4083 ? 222.302 176.943 231.520 1.00 35.94 ? 4083 ALA A CB    1 
ATOM   18766 N N     . ILE A 1 4084 ? 222.599 176.136 228.445 1.00 35.06 ? 4084 ILE A N     1 
ATOM   18767 C CA    . ILE A 1 4084 ? 222.157 175.408 227.259 1.00 37.92 ? 4084 ILE A CA    1 
ATOM   18768 C C     . ILE A 1 4084 ? 223.248 174.459 226.784 1.00 38.65 ? 4084 ILE A C     1 
ATOM   18769 O O     . ILE A 1 4084 ? 222.993 173.281 226.504 1.00 35.72 ? 4084 ILE A O     1 
ATOM   18770 C CB    . ILE A 1 4084 ? 221.754 176.397 226.147 1.00 38.22 ? 4084 ILE A CB    1 
ATOM   18771 C CG1   . ILE A 1 4084 ? 220.422 177.070 226.471 1.00 36.76 ? 4084 ILE A CG1   1 
ATOM   18772 C CG2   . ILE A 1 4084 ? 221.657 175.684 224.810 1.00 32.70 ? 4084 ILE A CG2   1 
ATOM   18773 C CD1   . ILE A 1 4084 ? 219.332 176.107 226.833 1.00 34.46 ? 4084 ILE A CD1   1 
ATOM   18774 N N     . ASN A 1 4085 ? 224.484 174.955 226.697 1.00 38.73 ? 4085 ASN A N     1 
ATOM   18775 C CA    . ASN A 1 4085 ? 225.584 174.133 226.200 1.00 38.16 ? 4085 ASN A CA    1 
ATOM   18776 C C     . ASN A 1 4085 ? 225.873 172.961 227.131 1.00 37.03 ? 4085 ASN A C     1 
ATOM   18777 O O     . ASN A 1 4085 ? 226.153 171.849 226.670 1.00 37.34 ? 4085 ASN A O     1 
ATOM   18778 C CB    . ASN A 1 4085 ? 226.834 174.992 226.009 1.00 36.88 ? 4085 ASN A CB    1 
ATOM   18779 C CG    . ASN A 1 4085 ? 226.674 176.011 224.897 1.00 37.33 ? 4085 ASN A CG    1 
ATOM   18780 O OD1   . ASN A 1 4085 ? 225.562 176.433 224.582 1.00 39.69 ? 4085 ASN A OD1   1 
ATOM   18781 N ND2   . ASN A 1 4085 ? 227.789 176.412 224.297 1.00 36.30 ? 4085 ASN A ND2   1 
ATOM   18782 N N     . THR A 1 4086 ? 225.815 173.188 228.444 1.00 34.22 ? 4086 THR A N     1 
ATOM   18783 C CA    . THR A 1 4086 ? 226.131 172.139 229.404 1.00 35.49 ? 4086 THR A CA    1 
ATOM   18784 C C     . THR A 1 4086 ? 224.940 171.251 229.740 1.00 37.21 ? 4086 THR A C     1 
ATOM   18785 O O     . THR A 1 4086 ? 225.115 170.255 230.450 1.00 38.78 ? 4086 THR A O     1 
ATOM   18786 C CB    . THR A 1 4086 ? 226.685 172.750 230.694 1.00 35.96 ? 4086 THR A CB    1 
ATOM   18787 O OG1   . THR A 1 4086 ? 227.368 171.740 231.448 1.00 34.64 ? 4086 THR A OG1   1 
ATOM   18788 C CG2   . THR A 1 4086 ? 225.557 173.323 231.538 1.00 33.48 ? 4086 THR A CG2   1 
ATOM   18789 N N     . ALA A 1 4087 ? 223.743 171.577 229.255 1.00 36.72 ? 4087 ALA A N     1 
ATOM   18790 C CA    . ALA A 1 4087 ? 222.556 170.790 229.562 1.00 38.25 ? 4087 ALA A CA    1 
ATOM   18791 C C     . ALA A 1 4087 ? 222.111 169.893 228.418 1.00 37.25 ? 4087 ALA A C     1 
ATOM   18792 O O     . ALA A 1 4087 ? 221.489 168.856 228.669 1.00 34.09 ? 4087 ALA A O     1 
ATOM   18793 C CB    . ALA A 1 4087 ? 221.397 171.711 229.955 1.00 35.98 ? 4087 ALA A CB    1 
ATOM   18794 N N     . VAL A 1 4088 ? 222.407 170.265 227.170 1.00 36.75 ? 4088 VAL A N     1 
ATOM   18795 C CA    . VAL A 1 4088 ? 222.019 169.423 226.042 1.00 38.53 ? 4088 VAL A CA    1 
ATOM   18796 C C     . VAL A 1 4088 ? 222.767 168.097 226.071 1.00 40.71 ? 4088 VAL A C     1 
ATOM   18797 O O     . VAL A 1 4088 ? 222.214 167.057 225.695 1.00 40.21 ? 4088 VAL A O     1 
ATOM   18798 C CB    . VAL A 1 4088 ? 222.235 170.170 224.711 1.00 40.96 ? 4088 VAL A CB    1 
ATOM   18799 C CG1   . VAL A 1 4088 ? 221.259 171.327 224.592 1.00 37.59 ? 4088 VAL A CG1   1 
ATOM   18800 C CG2   . VAL A 1 4088 ? 223.669 170.671 224.602 1.00 40.53 ? 4088 VAL A CG2   1 
ATOM   18801 N N     . LYS A 1 4089 ? 224.026 168.102 226.512 1.00 39.95 ? 4089 LYS A N     1 
ATOM   18802 C CA    . LYS A 1 4089 ? 224.796 166.871 226.619 1.00 41.02 ? 4089 LYS A CA    1 
ATOM   18803 C C     . LYS A 1 4089 ? 224.419 166.040 227.837 1.00 39.31 ? 4089 LYS A C     1 
ATOM   18804 O O     . LYS A 1 4089 ? 224.846 164.885 227.934 1.00 38.44 ? 4089 LYS A O     1 
ATOM   18805 C CB    . LYS A 1 4089 ? 226.293 167.190 226.657 1.00 38.62 ? 4089 LYS A CB    1 
ATOM   18806 C CG    . LYS A 1 4089 ? 226.820 167.838 225.387 1.00 38.48 ? 4089 LYS A CG    1 
ATOM   18807 C CD    . LYS A 1 4089 ? 228.320 168.067 225.461 1.00 37.55 ? 4089 LYS A CD    1 
ATOM   18808 C CE    . LYS A 1 4089 ? 228.665 169.167 226.451 1.00 36.91 ? 4089 LYS A CE    1 
ATOM   18809 N NZ    . LYS A 1 4089 ? 228.160 170.493 226.001 1.00 39.17 ? 4089 LYS A NZ    1 
ATOM   18810 N N     . SER A 1 4090 ? 223.630 166.592 228.760 1.00 37.35 ? 4090 SER A N     1 
ATOM   18811 C CA    . SER A 1 4090 ? 223.226 165.875 229.959 1.00 37.55 ? 4090 SER A CA    1 
ATOM   18812 C C     . SER A 1 4090 ? 221.717 165.806 230.146 1.00 37.77 ? 4090 SER A C     1 
ATOM   18813 O O     . SER A 1 4090 ? 221.260 165.164 231.098 1.00 35.30 ? 4090 SER A O     1 
ATOM   18814 C CB    . SER A 1 4090 ? 223.863 166.515 231.202 1.00 37.08 ? 4090 SER A CB    1 
ATOM   18815 O OG    . SER A 1 4090 ? 223.715 167.924 231.181 1.00 35.89 ? 4090 SER A OG    1 
ATOM   18816 N N     . GLY A 1 4091 ? 220.935 166.438 229.275 1.00 38.51 ? 4091 GLY A N     1 
ATOM   18817 C CA    . GLY A 1 4091 ? 219.489 166.382 229.369 1.00 36.73 ? 4091 GLY A CA    1 
ATOM   18818 C C     . GLY A 1 4091 ? 218.923 167.027 230.617 1.00 36.67 ? 4091 GLY A C     1 
ATOM   18819 O O     . GLY A 1 4091 ? 218.020 166.476 231.254 1.00 35.94 ? 4091 GLY A O     1 
ATOM   18820 N N     . ARG A 1 4092 ? 219.446 168.195 230.979 1.00 38.17 ? 4092 ARG A N     1 
ATOM   18821 C CA    . ARG A 1 4092 ? 218.984 168.932 232.146 1.00 41.22 ? 4092 ARG A CA    1 
ATOM   18822 C C     . ARG A 1 4092 ? 217.952 169.967 231.721 1.00 40.25 ? 4092 ARG A C     1 
ATOM   18823 O O     . ARG A 1 4092 ? 218.174 170.717 230.765 1.00 38.88 ? 4092 ARG A O     1 
ATOM   18824 C CB    . ARG A 1 4092 ? 220.154 169.602 232.867 1.00 40.10 ? 4092 ARG A CB    1 
ATOM   18825 C CG    . ARG A 1 4092 ? 221.158 168.622 233.462 1.00 38.46 ? 4092 ARG A CG    1 
ATOM   18826 C CD    . ARG A 1 4092 ? 220.537 167.798 234.586 1.00 34.39 ? 4092 ARG A CD    1 
ATOM   18827 N NE    . ARG A 1 4092 ? 219.850 166.607 234.099 1.00 38.93 ? 4092 ARG A NE    1 
ATOM   18828 C CZ    . ARG A 1 4092 ? 219.022 165.869 234.826 1.00 42.91 ? 4092 ARG A CZ    1 
ATOM   18829 N NH1   . ARG A 1 4092 ? 218.749 166.173 236.084 1.00 40.92 ? 4092 ARG A NH1   1 
ATOM   18830 N NH2   . ARG A 1 4092 ? 218.451 164.803 234.275 1.00 40.28 ? 4092 ARG A NH2   1 
ATOM   18831 N N     . TRP A 1 4093 ? 216.830 170.004 232.437 1.00 33.52 ? 4093 TRP A N     1 
ATOM   18832 C CA    . TRP A 1 4093 ? 215.681 170.818 232.048 1.00 28.16 ? 4093 TRP A CA    1 
ATOM   18833 C C     . TRP A 1 4093 ? 216.003 172.281 232.315 1.00 26.80 ? 4093 TRP A C     1 
ATOM   18834 O O     . TRP A 1 4093 ? 215.969 172.741 233.458 1.00 33.73 ? 4093 TRP A O     1 
ATOM   18835 C CB    . TRP A 1 4093 ? 214.435 170.394 232.810 1.00 26.73 ? 4093 TRP A CB    1 
ATOM   18836 C CG    . TRP A 1 4093 ? 213.790 169.169 232.270 1.00 30.15 ? 4093 TRP A CG    1 
ATOM   18837 C CD1   . TRP A 1 4093 ? 214.286 168.333 231.314 1.00 34.24 ? 4093 TRP A CD1   1 
ATOM   18838 C CD2   . TRP A 1 4093 ? 212.508 168.650 232.632 1.00 29.61 ? 4093 TRP A CD2   1 
ATOM   18839 N NE1   . TRP A 1 4093 ? 213.400 167.310 231.075 1.00 32.89 ? 4093 TRP A NE1   1 
ATOM   18840 C CE2   . TRP A 1 4093 ? 212.297 167.486 231.869 1.00 30.99 ? 4093 TRP A CE2   1 
ATOM   18841 C CE3   . TRP A 1 4093 ? 211.521 169.053 233.534 1.00 28.74 ? 4093 TRP A CE3   1 
ATOM   18842 C CZ2   . TRP A 1 4093 ? 211.140 166.723 231.980 1.00 28.63 ? 4093 TRP A CZ2   1 
ATOM   18843 C CZ3   . TRP A 1 4093 ? 210.375 168.296 233.643 1.00 28.20 ? 4093 TRP A CZ3   1 
ATOM   18844 C CH2   . TRP A 1 4093 ? 210.192 167.145 232.869 1.00 26.68 ? 4093 TRP A CH2   1 
ATOM   18845 N N     . VAL A 1 4094 ? 216.305 173.017 231.257 1.00 19.84 ? 4094 VAL A N     1 
ATOM   18846 C CA    . VAL A 1 4094 ? 216.634 174.431 231.360 1.00 24.64 ? 4094 VAL A CA    1 
ATOM   18847 C C     . VAL A 1 4094 ? 215.342 175.237 231.393 1.00 23.96 ? 4094 VAL A C     1 
ATOM   18848 O O     . VAL A 1 4094 ? 214.364 174.892 230.720 1.00 25.35 ? 4094 VAL A O     1 
ATOM   18849 C CB    . VAL A 1 4094 ? 217.541 174.862 230.194 1.00 26.66 ? 4094 VAL A CB    1 
ATOM   18850 C CG1   . VAL A 1 4094 ? 216.805 174.737 228.880 1.00 25.05 ? 4094 VAL A CG1   1 
ATOM   18851 C CG2   . VAL A 1 4094 ? 218.042 176.283 230.394 1.00 25.45 ? 4094 VAL A CG2   1 
ATOM   18852 N N     . MET A 1 4095 ? 215.327 176.303 232.189 1.00 25.21 ? 4095 MET A N     1 
ATOM   18853 C CA    . MET A 1 4095 ? 214.172 177.189 232.289 1.00 22.54 ? 4095 MET A CA    1 
ATOM   18854 C C     . MET A 1 4095 ? 214.632 178.631 232.151 1.00 25.07 ? 4095 MET A C     1 
ATOM   18855 O O     . MET A 1 4095 ? 215.628 179.033 232.761 1.00 33.96 ? 4095 MET A O     1 
ATOM   18856 C CB    . MET A 1 4095 ? 213.425 177.004 233.605 1.00 24.57 ? 4095 MET A CB    1 
ATOM   18857 C CG    . MET A 1 4095 ? 212.123 177.776 233.634 1.00 20.43 ? 4095 MET A CG    1 
ATOM   18858 S SD    . MET A 1 4095 ? 210.823 176.944 234.541 1.00 28.31 ? 4095 MET A SD    1 
ATOM   18859 C CE    . MET A 1 4095 ? 209.640 178.275 234.705 1.00 21.79 ? 4095 MET A CE    1 
ATOM   18860 N N     . LEU A 1 4096 ? 213.909 179.399 231.347 1.00 20.47 ? 4096 LEU A N     1 
ATOM   18861 C CA    . LEU A 1 4096 ? 214.149 180.827 231.223 1.00 22.18 ? 4096 LEU A CA    1 
ATOM   18862 C C     . LEU A 1 4096 ? 212.917 181.598 231.680 1.00 23.55 ? 4096 LEU A C     1 
ATOM   18863 O O     . LEU A 1 4096 ? 211.787 181.268 231.310 1.00 21.26 ? 4096 LEU A O     1 
ATOM   18864 C CB    . LEU A 1 4096 ? 214.516 181.202 229.786 1.00 23.11 ? 4096 LEU A CB    1 
ATOM   18865 C CG    . LEU A 1 4096 ? 215.946 180.953 229.280 1.00 22.07 ? 4096 LEU A CG    1 
ATOM   18866 C CD1   . LEU A 1 4096 ? 216.451 179.525 229.470 1.00 20.34 ? 4096 LEU A CD1   1 
ATOM   18867 C CD2   . LEU A 1 4096 ? 216.064 181.371 227.829 1.00 22.59 ? 4096 LEU A CD2   1 
ATOM   18868 N N     . LYS A 1 4097 ? 213.146 182.617 232.502 1.00 26.24 ? 4097 LYS A N     1 
ATOM   18869 C CA    . LYS A 1 4097 ? 212.086 183.423 233.092 1.00 26.59 ? 4097 LYS A CA    1 
ATOM   18870 C C     . LYS A 1 4097 ? 211.913 184.708 232.296 1.00 26.07 ? 4097 LYS A C     1 
ATOM   18871 O O     . LYS A 1 4097 ? 212.870 185.473 232.138 1.00 23.91 ? 4097 LYS A O     1 
ATOM   18872 C CB    . LYS A 1 4097 ? 212.408 183.763 234.549 1.00 27.72 ? 4097 LYS A CB    1 
ATOM   18873 C CG    . LYS A 1 4097 ? 212.535 182.571 235.477 1.00 24.70 ? 4097 LYS A CG    1 
ATOM   18874 C CD    . LYS A 1 4097 ? 211.201 181.894 235.703 1.00 25.01 ? 4097 LYS A CD    1 
ATOM   18875 C CE    . LYS A 1 4097 ? 211.354 180.712 236.641 1.00 31.54 ? 4097 LYS A CE    1 
ATOM   18876 N NZ    . LYS A 1 4097 ? 211.704 181.145 238.022 1.00 27.86 ? 4097 LYS A NZ    1 
ATOM   18877 N N     . ASN A 1 4098 ? 210.693 184.949 231.817 1.00 22.88 ? 4098 ASN A N     1 
ATOM   18878 C CA    . ASN A 1 4098 ? 210.344 186.185 231.114 1.00 21.92 ? 4098 ASN A CA    1 
ATOM   18879 C C     . ASN A 1 4098 ? 211.316 186.463 229.969 1.00 26.52 ? 4098 ASN A C     1 
ATOM   18880 O O     . ASN A 1 4098 ? 211.884 187.550 229.845 1.00 30.85 ? 4098 ASN A O     1 
ATOM   18881 C CB    . ASN A 1 4098 ? 210.284 187.365 232.083 1.00 24.72 ? 4098 ASN A CB    1 
ATOM   18882 C CG    . ASN A 1 4098 ? 209.350 187.113 233.247 1.00 24.46 ? 4098 ASN A CG    1 
ATOM   18883 O OD1   . ASN A 1 4098 ? 208.352 186.404 233.115 1.00 23.14 ? 4098 ASN A OD1   1 
ATOM   18884 N ND2   . ASN A 1 4098 ? 209.668 187.692 234.398 1.00 24.50 ? 4098 ASN A ND2   1 
ATOM   18885 N N     . VAL A 1 4099 ? 211.512 185.449 229.124 1.00 22.08 ? 4099 VAL A N     1 
ATOM   18886 C CA    . VAL A 1 4099 ? 212.427 185.570 227.995 1.00 21.60 ? 4099 VAL A CA    1 
ATOM   18887 C C     . VAL A 1 4099 ? 211.905 186.517 226.925 1.00 22.94 ? 4099 VAL A C     1 
ATOM   18888 O O     . VAL A 1 4099 ? 212.663 186.914 226.034 1.00 29.00 ? 4099 VAL A O     1 
ATOM   18889 C CB    . VAL A 1 4099 ? 212.706 184.169 227.410 1.00 24.89 ? 4099 VAL A CB    1 
ATOM   18890 C CG1   . VAL A 1 4099 ? 211.473 183.629 226.698 1.00 23.43 ? 4099 VAL A CG1   1 
ATOM   18891 C CG2   . VAL A 1 4099 ? 213.931 184.180 226.503 1.00 24.79 ? 4099 VAL A CG2   1 
ATOM   18892 N N     . HIS A 1 4100 ? 210.632 186.913 227.006 1.00 21.57 ? 4100 HIS A N     1 
ATOM   18893 C CA    . HIS A 1 4100 ? 210.048 187.821 226.026 1.00 23.85 ? 4100 HIS A CA    1 
ATOM   18894 C C     . HIS A 1 4100 ? 210.637 189.223 226.093 1.00 20.75 ? 4100 HIS A C     1 
ATOM   18895 O O     . HIS A 1 4100 ? 210.380 190.026 225.190 1.00 17.20 ? 4100 HIS A O     1 
ATOM   18896 C CB    . HIS A 1 4100 ? 208.533 187.897 226.218 1.00 21.43 ? 4100 HIS A CB    1 
ATOM   18897 C CG    . HIS A 1 4100 ? 208.118 188.536 227.506 1.00 16.23 ? 4100 HIS A CG    1 
ATOM   18898 N ND1   . HIS A 1 4100 ? 208.212 187.892 228.721 1.00 18.33 ? 4100 HIS A ND1   1 
ATOM   18899 C CD2   . HIS A 1 4100 ? 207.597 189.757 227.768 1.00 18.27 ? 4100 HIS A CD2   1 
ATOM   18900 C CE1   . HIS A 1 4100 ? 207.772 188.691 229.676 1.00 18.02 ? 4100 HIS A CE1   1 
ATOM   18901 N NE2   . HIS A 1 4100 ? 207.393 189.829 229.125 1.00 17.84 ? 4100 HIS A NE2   1 
ATOM   18902 N N     . LEU A 1 4101 ? 211.405 189.538 227.138 1.00 18.95 ? 4101 LEU A N     1 
ATOM   18903 C CA    . LEU A 1 4101 ? 212.027 190.854 227.232 1.00 21.10 ? 4101 LEU A CA    1 
ATOM   18904 C C     . LEU A 1 4101 ? 213.015 191.082 226.095 1.00 24.09 ? 4101 LEU A C     1 
ATOM   18905 O O     . LEU A 1 4101 ? 213.119 192.196 225.566 1.00 25.38 ? 4101 LEU A O     1 
ATOM   18906 C CB    . LEU A 1 4101 ? 212.720 191.009 228.586 1.00 20.70 ? 4101 LEU A CB    1 
ATOM   18907 C CG    . LEU A 1 4101 ? 211.843 190.841 229.828 1.00 18.99 ? 4101 LEU A CG    1 
ATOM   18908 C CD1   . LEU A 1 4101 ? 212.679 190.935 231.094 1.00 23.66 ? 4101 LEU A CD1   1 
ATOM   18909 C CD2   . LEU A 1 4101 ? 210.729 191.870 229.845 1.00 14.22 ? 4101 LEU A CD2   1 
ATOM   18910 N N     . ALA A 1 4102 ? 213.748 190.044 225.705 1.00 21.45 ? 4102 ALA A N     1 
ATOM   18911 C CA    . ALA A 1 4102 ? 214.754 190.162 224.657 1.00 24.01 ? 4102 ALA A CA    1 
ATOM   18912 C C     . ALA A 1 4102 ? 214.296 189.451 223.394 1.00 22.99 ? 4102 ALA A C     1 
ATOM   18913 O O     . ALA A 1 4102 ? 214.268 188.211 223.362 1.00 21.67 ? 4102 ALA A O     1 
ATOM   18914 C CB    . ALA A 1 4102 ? 216.086 189.588 225.132 1.00 21.77 ? 4102 ALA A CB    1 
ATOM   18915 N N     . PRO A 1 4103 ? 213.931 190.175 222.342 1.00 25.73 ? 4103 PRO A N     1 
ATOM   18916 C CA    . PRO A 1 4103 ? 213.536 189.515 221.091 1.00 28.57 ? 4103 PRO A CA    1 
ATOM   18917 C C     . PRO A 1 4103 ? 214.718 189.031 220.263 1.00 28.99 ? 4103 PRO A C     1 
ATOM   18918 O O     . PRO A 1 4103 ? 214.642 187.967 219.644 1.00 28.86 ? 4103 PRO A O     1 
ATOM   18919 C CB    . PRO A 1 4103 ? 212.748 190.604 220.350 1.00 27.27 ? 4103 PRO A CB    1 
ATOM   18920 C CG    . PRO A 1 4103 ? 212.561 191.732 221.341 1.00 25.37 ? 4103 PRO A CG    1 
ATOM   18921 C CD    . PRO A 1 4103 ? 213.687 191.624 222.304 1.00 23.82 ? 4103 PRO A CD    1 
ATOM   18922 N N     . GLY A 1 4104 ? 215.808 189.800 220.230 1.00 28.17 ? 4104 GLY A N     1 
ATOM   18923 C CA    . GLY A 1 4104 ? 216.958 189.398 219.434 1.00 29.58 ? 4104 GLY A CA    1 
ATOM   18924 C C     . GLY A 1 4104 ? 217.632 188.145 219.961 1.00 30.27 ? 4104 GLY A C     1 
ATOM   18925 O O     . GLY A 1 4104 ? 217.986 187.244 219.191 1.00 33.07 ? 4104 GLY A O     1 
ATOM   18926 N N     . TRP A 1 4105 ? 217.823 188.069 221.279 1.00 25.62 ? 4105 TRP A N     1 
ATOM   18927 C CA    . TRP A 1 4105 ? 218.393 186.862 221.861 1.00 28.04 ? 4105 TRP A CA    1 
ATOM   18928 C C     . TRP A 1 4105 ? 217.468 185.673 221.648 1.00 31.34 ? 4105 TRP A C     1 
ATOM   18929 O O     . TRP A 1 4105 ? 217.927 184.536 221.497 1.00 33.97 ? 4105 TRP A O     1 
ATOM   18930 C CB    . TRP A 1 4105 ? 218.665 187.066 223.348 1.00 28.24 ? 4105 TRP A CB    1 
ATOM   18931 C CG    . TRP A 1 4105 ? 219.471 185.962 223.940 1.00 30.27 ? 4105 TRP A CG    1 
ATOM   18932 C CD1   . TRP A 1 4105 ? 220.830 185.901 224.043 1.00 32.26 ? 4105 TRP A CD1   1 
ATOM   18933 C CD2   . TRP A 1 4105 ? 218.972 184.734 224.476 1.00 30.82 ? 4105 TRP A CD2   1 
ATOM   18934 N NE1   . TRP A 1 4105 ? 221.207 184.720 224.632 1.00 30.81 ? 4105 TRP A NE1   1 
ATOM   18935 C CE2   . TRP A 1 4105 ? 220.084 183.984 224.905 1.00 32.91 ? 4105 TRP A CE2   1 
ATOM   18936 C CE3   . TRP A 1 4105 ? 217.693 184.201 224.645 1.00 30.40 ? 4105 TRP A CE3   1 
ATOM   18937 C CZ2   . TRP A 1 4105 ? 219.954 182.729 225.490 1.00 34.44 ? 4105 TRP A CZ2   1 
ATOM   18938 C CZ3   . TRP A 1 4105 ? 217.566 182.958 225.222 1.00 32.56 ? 4105 TRP A CZ3   1 
ATOM   18939 C CH2   . TRP A 1 4105 ? 218.689 182.234 225.640 1.00 32.54 ? 4105 TRP A CH2   1 
ATOM   18940 N N     . LEU A 1 4106 ? 216.158 185.919 221.623 1.00 28.83 ? 4106 LEU A N     1 
ATOM   18941 C CA    . LEU A 1 4106 ? 215.209 184.841 221.372 1.00 27.67 ? 4106 LEU A CA    1 
ATOM   18942 C C     . LEU A 1 4106 ? 215.281 184.371 219.922 1.00 27.28 ? 4106 LEU A C     1 
ATOM   18943 O O     . LEU A 1 4106 ? 215.156 183.172 219.646 1.00 31.79 ? 4106 LEU A O     1 
ATOM   18944 C CB    . LEU A 1 4106 ? 213.800 185.302 221.738 1.00 27.34 ? 4106 LEU A CB    1 
ATOM   18945 C CG    . LEU A 1 4106 ? 212.783 184.209 222.049 1.00 29.75 ? 4106 LEU A CG    1 
ATOM   18946 C CD1   . LEU A 1 4106 ? 213.362 183.225 223.047 1.00 27.00 ? 4106 LEU A CD1   1 
ATOM   18947 C CD2   . LEU A 1 4106 ? 211.514 184.831 222.602 1.00 28.14 ? 4106 LEU A CD2   1 
ATOM   18948 N N     . MET A 1 4107 ? 215.490 185.300 218.984 1.00 25.75 ? 4107 MET A N     1 
ATOM   18949 C CA    . MET A 1 4107 ? 215.773 184.917 217.604 1.00 30.84 ? 4107 MET A CA    1 
ATOM   18950 C C     . MET A 1 4107 ? 217.021 184.050 217.526 1.00 30.44 ? 4107 MET A C     1 
ATOM   18951 O O     . MET A 1 4107 ? 217.044 183.034 216.819 1.00 28.01 ? 4107 MET A O     1 
ATOM   18952 C CB    . MET A 1 4107 ? 215.953 186.163 216.735 1.00 28.03 ? 4107 MET A CB    1 
ATOM   18953 C CG    . MET A 1 4107 ? 215.329 186.081 215.349 1.00 30.26 ? 4107 MET A CG    1 
ATOM   18954 S SD    . MET A 1 4107 ? 213.568 185.718 215.329 1.00 38.31 ? 4107 MET A SD    1 
ATOM   18955 C CE    . MET A 1 4107 ? 212.902 187.378 215.435 1.00 29.40 ? 4107 MET A CE    1 
ATOM   18956 N N     . GLN A 1 4108 ? 218.075 184.447 218.241 1.00 31.98 ? 4108 GLN A N     1 
ATOM   18957 C CA    . GLN A 1 4108 ? 219.304 183.660 218.246 1.00 31.42 ? 4108 GLN A CA    1 
ATOM   18958 C C     . GLN A 1 4108 ? 219.063 182.266 218.814 1.00 31.47 ? 4108 GLN A C     1 
ATOM   18959 O O     . GLN A 1 4108 ? 219.578 181.274 218.287 1.00 31.69 ? 4108 GLN A O     1 
ATOM   18960 C CB    . GLN A 1 4108 ? 220.386 184.384 219.045 1.00 29.00 ? 4108 GLN A CB    1 
ATOM   18961 C CG    . GLN A 1 4108 ? 221.734 183.688 219.037 1.00 33.02 ? 4108 GLN A CG    1 
ATOM   18962 C CD    . GLN A 1 4108 ? 222.793 184.465 219.790 1.00 33.05 ? 4108 GLN A CD    1 
ATOM   18963 O OE1   . GLN A 1 4108 ? 222.516 185.521 220.360 1.00 31.26 ? 4108 GLN A OE1   1 
ATOM   18964 N NE2   . GLN A 1 4108 ? 224.015 183.946 219.798 1.00 34.06 ? 4108 GLN A NE2   1 
ATOM   18965 N N     . LEU A 1 4109 ? 218.282 182.175 219.892 1.00 29.30 ? 4109 LEU A N     1 
ATOM   18966 C CA    . LEU A 1 4109 ? 217.973 180.877 220.484 1.00 30.06 ? 4109 LEU A CA    1 
ATOM   18967 C C     . LEU A 1 4109 ? 217.178 180.004 219.522 1.00 30.98 ? 4109 LEU A C     1 
ATOM   18968 O O     . LEU A 1 4109 ? 217.447 178.803 219.395 1.00 32.66 ? 4109 LEU A O     1 
ATOM   18969 C CB    . LEU A 1 4109 ? 217.200 181.065 221.788 1.00 32.48 ? 4109 LEU A CB    1 
ATOM   18970 C CG    . LEU A 1 4109 ? 216.868 179.776 222.541 1.00 32.72 ? 4109 LEU A CG    1 
ATOM   18971 C CD1   . LEU A 1 4109 ? 218.140 179.066 222.979 1.00 30.50 ? 4109 LEU A CD1   1 
ATOM   18972 C CD2   . LEU A 1 4109 ? 215.967 180.061 223.729 1.00 30.99 ? 4109 LEU A CD2   1 
ATOM   18973 N N     . GLU A 1 4110 ? 216.189 180.587 218.842 1.00 28.27 ? 4110 GLU A N     1 
ATOM   18974 C CA    . GLU A 1 4110 ? 215.403 179.822 217.880 1.00 29.53 ? 4110 GLU A CA    1 
ATOM   18975 C C     . GLU A 1 4110 ? 216.278 179.320 216.741 1.00 30.71 ? 4110 GLU A C     1 
ATOM   18976 O O     . GLU A 1 4110 ? 216.135 178.176 216.294 1.00 29.81 ? 4110 GLU A O     1 
ATOM   18977 C CB    . GLU A 1 4110 ? 214.250 180.679 217.350 1.00 28.49 ? 4110 GLU A CB    1 
ATOM   18978 C CG    . GLU A 1 4110 ? 213.185 179.924 216.557 1.00 28.36 ? 4110 GLU A CG    1 
ATOM   18979 C CD    . GLU A 1 4110 ? 213.634 179.541 215.160 1.00 30.43 ? 4110 GLU A CD    1 
ATOM   18980 O OE1   . GLU A 1 4110 ? 213.486 178.358 214.790 1.00 31.91 ? 4110 GLU A OE1   1 
ATOM   18981 O OE2   . GLU A 1 4110 ? 214.139 180.423 214.433 1.00 30.16 ? 4110 GLU A OE2   1 
ATOM   18982 N N     . LYS A 1 4111 ? 217.191 180.165 216.256 1.00 33.75 ? 4111 LYS A N     1 
ATOM   18983 C CA    . LYS A 1 4111 ? 218.092 179.743 215.189 1.00 34.30 ? 4111 LYS A CA    1 
ATOM   18984 C C     . LYS A 1 4111 ? 219.024 178.631 215.656 1.00 35.00 ? 4111 LYS A C     1 
ATOM   18985 O O     . LYS A 1 4111 ? 219.270 177.668 214.920 1.00 33.53 ? 4111 LYS A O     1 
ATOM   18986 C CB    . LYS A 1 4111 ? 218.896 180.938 214.679 1.00 34.31 ? 4111 LYS A CB    1 
ATOM   18987 C CG    . LYS A 1 4111 ? 218.147 181.822 213.695 1.00 33.86 ? 4111 LYS A CG    1 
ATOM   18988 C CD    . LYS A 1 4111 ? 217.446 180.997 212.629 1.00 33.53 ? 4111 LYS A CD    1 
ATOM   18989 C CE    . LYS A 1 4111 ? 216.572 181.869 211.743 1.00 32.96 ? 4111 LYS A CE    1 
ATOM   18990 N NZ    . LYS A 1 4111 ? 215.795 181.061 210.763 1.00 33.67 ? 4111 LYS A NZ    1 
ATOM   18991 N N     . LYS A 1 4112 ? 219.551 178.743 216.878 1.00 33.72 ? 4112 LYS A N     1 
ATOM   18992 C CA    . LYS A 1 4112 ? 220.533 177.770 217.346 1.00 32.07 ? 4112 LYS A CA    1 
ATOM   18993 C C     . LYS A 1 4112 ? 219.883 176.461 217.775 1.00 34.65 ? 4112 LYS A C     1 
ATOM   18994 O O     . LYS A 1 4112 ? 220.561 175.429 217.833 1.00 38.02 ? 4112 LYS A O     1 
ATOM   18995 C CB    . LYS A 1 4112 ? 221.350 178.356 218.498 1.00 29.82 ? 4112 LYS A CB    1 
ATOM   18996 C CG    . LYS A 1 4112 ? 220.701 178.215 219.863 1.00 30.94 ? 4112 LYS A CG    1 
ATOM   18997 C CD    . LYS A 1 4112 ? 221.751 178.161 220.959 1.00 34.19 ? 4112 LYS A CD    1 
ATOM   18998 C CE    . LYS A 1 4112 ? 222.382 176.781 221.048 1.00 35.65 ? 4112 LYS A CE    1 
ATOM   18999 N NZ    . LYS A 1 4112 ? 223.367 176.689 222.161 1.00 33.57 ? 4112 LYS A NZ    1 
ATOM   19000 N N     . LEU A 1 4113 ? 218.584 176.475 218.082 1.00 33.70 ? 4113 LEU A N     1 
ATOM   19001 C CA    . LEU A 1 4113 ? 217.917 175.255 218.520 1.00 33.58 ? 4113 LEU A CA    1 
ATOM   19002 C C     . LEU A 1 4113 ? 217.756 174.229 217.407 1.00 32.80 ? 4113 LEU A C     1 
ATOM   19003 O O     . LEU A 1 4113 ? 217.397 173.083 217.697 1.00 33.22 ? 4113 LEU A O     1 
ATOM   19004 C CB    . LEU A 1 4113 ? 216.548 175.588 219.114 1.00 34.24 ? 4113 LEU A CB    1 
ATOM   19005 C CG    . LEU A 1 4113 ? 216.527 175.843 220.622 1.00 35.16 ? 4113 LEU A CG    1 
ATOM   19006 C CD1   . LEU A 1 4113 ? 215.100 175.853 221.145 1.00 32.62 ? 4113 LEU A CD1   1 
ATOM   19007 C CD2   . LEU A 1 4113 ? 217.367 174.810 221.359 1.00 30.49 ? 4113 LEU A CD2   1 
ATOM   19008 N N     . HIS A 1 4114 ? 218.004 174.606 216.150 1.00 33.62 ? 4114 HIS A N     1 
ATOM   19009 C CA    . HIS A 1 4114 ? 217.922 173.638 215.062 1.00 35.16 ? 4114 HIS A CA    1 
ATOM   19010 C C     . HIS A 1 4114 ? 218.983 172.553 215.195 1.00 36.00 ? 4114 HIS A C     1 
ATOM   19011 O O     . HIS A 1 4114 ? 218.787 171.432 214.712 1.00 35.57 ? 4114 HIS A O     1 
ATOM   19012 C CB    . HIS A 1 4114 ? 218.054 174.350 213.716 1.00 35.12 ? 4114 HIS A CB    1 
ATOM   19013 C CG    . HIS A 1 4114 ? 216.755 174.851 213.167 1.00 36.76 ? 4114 HIS A CG    1 
ATOM   19014 N ND1   . HIS A 1 4114 ? 215.598 174.102 213.191 1.00 34.17 ? 4114 HIS A ND1   1 
ATOM   19015 C CD2   . HIS A 1 4114 ? 216.428 176.028 212.584 1.00 38.13 ? 4114 HIS A CD2   1 
ATOM   19016 C CE1   . HIS A 1 4114 ? 214.616 174.795 212.644 1.00 35.97 ? 4114 HIS A CE1   1 
ATOM   19017 N NE2   . HIS A 1 4114 ? 215.093 175.967 212.268 1.00 38.01 ? 4114 HIS A NE2   1 
ATOM   19018 N N     . SER A 1 4115 ? 220.105 172.864 215.839 1.00 33.02 ? 4115 SER A N     1 
ATOM   19019 C CA    . SER A 1 4115 ? 221.158 171.878 216.032 1.00 34.61 ? 4115 SER A CA    1 
ATOM   19020 C C     . SER A 1 4115 ? 220.674 170.747 216.931 1.00 34.92 ? 4115 SER A C     1 
ATOM   19021 O O     . SER A 1 4115 ? 219.958 170.972 217.910 1.00 35.85 ? 4115 SER A O     1 
ATOM   19022 C CB    . SER A 1 4115 ? 222.398 172.534 216.637 1.00 34.33 ? 4115 SER A CB    1 
ATOM   19023 O OG    . SER A 1 4115 ? 222.194 172.839 218.005 1.00 34.35 ? 4115 SER A OG    1 
ATOM   19024 N N     . LEU A 1 4116 ? 221.072 169.525 216.591 1.00 36.14 ? 4116 LEU A N     1 
ATOM   19025 C CA    . LEU A 1 4116 ? 220.635 168.350 217.328 1.00 38.74 ? 4116 LEU A CA    1 
ATOM   19026 C C     . LEU A 1 4116 ? 221.247 168.318 218.723 1.00 38.43 ? 4116 LEU A C     1 
ATOM   19027 O O     . LEU A 1 4116 ? 222.354 168.809 218.956 1.00 36.46 ? 4116 LEU A O     1 
ATOM   19028 C CB    . LEU A 1 4116 ? 220.998 167.074 216.568 1.00 37.63 ? 4116 LEU A CB    1 
ATOM   19029 C CG    . LEU A 1 4116 ? 220.709 167.089 215.066 1.00 39.85 ? 4116 LEU A CG    1 
ATOM   19030 C CD1   . LEU A 1 4116 ? 221.222 165.820 214.406 1.00 38.41 ? 4116 LEU A CD1   1 
ATOM   19031 C CD2   . LEU A 1 4116 ? 219.220 167.269 214.809 1.00 38.23 ? 4116 LEU A CD2   1 
ATOM   19032 N N     . GLN A 1 4117 ? 220.502 167.733 219.654 1.00 39.69 ? 4117 GLN A N     1 
ATOM   19033 C CA    . GLN A 1 4117 ? 220.862 167.589 221.059 1.00 38.97 ? 4117 GLN A CA    1 
ATOM   19034 C C     . GLN A 1 4117 ? 221.184 166.137 221.380 1.00 39.36 ? 4117 GLN A C     1 
ATOM   19035 O O     . GLN A 1 4117 ? 220.420 165.236 221.002 1.00 38.50 ? 4117 GLN A O     1 
ATOM   19036 C CB    . GLN A 1 4117 ? 219.729 168.099 221.950 1.00 39.90 ? 4117 GLN A CB    1 
ATOM   19037 C CG    . GLN A 1 4117 ? 218.425 167.328 221.825 1.00 38.73 ? 4117 GLN A CG    1 
ATOM   19038 C CD    . GLN A 1 4117 ? 217.612 167.783 220.625 1.00 40.74 ? 4117 GLN A CD    1 
ATOM   19039 O OE1   . GLN A 1 4117 ? 218.119 168.485 219.751 1.00 38.84 ? 4117 GLN A OE1   1 
ATOM   19040 N NE2   . GLN A 1 4117 ? 216.355 167.372 220.569 1.00 40.49 ? 4117 GLN A NE2   1 
ATOM   19041 N N     . PRO A 1 4118 ? 222.322 165.872 222.026 1.00 47.31 ? 4118 PRO A N     1 
ATOM   19042 C CA    . PRO A 1 4118 ? 222.698 164.477 222.307 1.00 45.78 ? 4118 PRO A CA    1 
ATOM   19043 C C     . PRO A 1 4118 ? 221.722 163.741 223.209 1.00 45.32 ? 4118 PRO A C     1 
ATOM   19044 O O     . PRO A 1 4118 ? 221.560 162.523 223.062 1.00 43.79 ? 4118 PRO A O     1 
ATOM   19045 C CB    . PRO A 1 4118 ? 224.076 164.616 222.972 1.00 43.67 ? 4118 PRO A CB    1 
ATOM   19046 C CG    . PRO A 1 4118 ? 224.594 165.940 222.507 1.00 44.33 ? 4118 PRO A CG    1 
ATOM   19047 C CD    . PRO A 1 4118 ? 223.387 166.821 222.390 1.00 44.71 ? 4118 PRO A CD    1 
ATOM   19048 N N     . HIS A 1 4119 ? 221.066 164.436 224.134 1.00 40.43 ? 4119 HIS A N     1 
ATOM   19049 C CA    . HIS A 1 4119 ? 220.262 163.796 225.168 1.00 39.88 ? 4119 HIS A CA    1 
ATOM   19050 C C     . HIS A 1 4119 ? 218.779 163.972 224.870 1.00 38.36 ? 4119 HIS A C     1 
ATOM   19051 O O     . HIS A 1 4119 ? 218.353 165.037 224.411 1.00 35.42 ? 4119 HIS A O     1 
ATOM   19052 C CB    . HIS A 1 4119 ? 220.596 164.370 226.545 1.00 37.29 ? 4119 HIS A CB    1 
ATOM   19053 C CG    . HIS A 1 4119 ? 220.490 163.371 227.655 1.00 39.80 ? 4119 HIS A CG    1 
ATOM   19054 N ND1   . HIS A 1 4119 ? 219.295 163.065 228.270 1.00 39.11 ? 4119 HIS A ND1   1 
ATOM   19055 C CD2   . HIS A 1 4119 ? 221.430 162.607 228.259 1.00 41.01 ? 4119 HIS A CD2   1 
ATOM   19056 C CE1   . HIS A 1 4119 ? 219.504 162.157 229.206 1.00 39.41 ? 4119 HIS A CE1   1 
ATOM   19057 N NE2   . HIS A 1 4119 ? 220.791 161.862 229.220 1.00 39.96 ? 4119 HIS A NE2   1 
ATOM   19058 N N     . ALA A 1 4120 ? 218.000 162.920 225.130 1.00 36.30 ? 4120 ALA A N     1 
ATOM   19059 C CA    . ALA A 1 4120 ? 216.567 162.953 224.861 1.00 35.69 ? 4120 ALA A CA    1 
ATOM   19060 C C     . ALA A 1 4120 ? 215.765 163.479 226.044 1.00 37.26 ? 4120 ALA A C     1 
ATOM   19061 O O     . ALA A 1 4120 ? 214.651 163.980 225.855 1.00 40.71 ? 4120 ALA A O     1 
ATOM   19062 C CB    . ALA A 1 4120 ? 216.073 161.558 224.477 1.00 33.31 ? 4120 ALA A CB    1 
ATOM   19063 N N     . CYS A 1 4121 ? 216.299 163.372 227.263 1.00 32.98 ? 4121 CYS A N     1 
ATOM   19064 C CA    . CYS A 1 4121 ? 215.593 163.871 228.438 1.00 32.96 ? 4121 CYS A CA    1 
ATOM   19065 C C     . CYS A 1 4121 ? 215.524 165.391 228.484 1.00 32.00 ? 4121 CYS A C     1 
ATOM   19066 O O     . CYS A 1 4121 ? 214.785 165.934 229.313 1.00 30.44 ? 4121 CYS A O     1 
ATOM   19067 C CB    . CYS A 1 4121 ? 216.257 163.350 229.714 1.00 34.51 ? 4121 CYS A CB    1 
ATOM   19068 S SG    . CYS A 1 4121 ? 216.151 161.560 229.934 1.00 43.70 ? 4121 CYS A SG    1 
ATOM   19069 N N     . PHE A 1 4122 ? 216.271 166.081 227.626 1.00 30.23 ? 4122 PHE A N     1 
ATOM   19070 C CA    . PHE A 1 4122 ? 216.270 167.536 227.615 1.00 30.54 ? 4122 PHE A CA    1 
ATOM   19071 C C     . PHE A 1 4122 ? 214.876 168.079 227.330 1.00 28.12 ? 4122 PHE A C     1 
ATOM   19072 O O     . PHE A 1 4122 ? 214.180 167.609 226.426 1.00 30.28 ? 4122 PHE A O     1 
ATOM   19073 C CB    . PHE A 1 4122 ? 217.257 168.047 226.566 1.00 31.11 ? 4122 PHE A CB    1 
ATOM   19074 C CG    . PHE A 1 4122 ? 217.339 169.543 226.483 1.00 30.94 ? 4122 PHE A CG    1 
ATOM   19075 C CD1   . PHE A 1 4122 ? 218.022 170.269 227.443 1.00 32.82 ? 4122 PHE A CD1   1 
ATOM   19076 C CD2   . PHE A 1 4122 ? 216.739 170.223 225.437 1.00 28.85 ? 4122 PHE A CD2   1 
ATOM   19077 C CE1   . PHE A 1 4122 ? 218.100 171.644 227.364 1.00 29.93 ? 4122 PHE A CE1   1 
ATOM   19078 C CE2   . PHE A 1 4122 ? 216.815 171.597 225.353 1.00 29.71 ? 4122 PHE A CE2   1 
ATOM   19079 C CZ    . PHE A 1 4122 ? 217.496 172.309 226.318 1.00 28.44 ? 4122 PHE A CZ    1 
ATOM   19080 N N     . ARG A 1 4123 ? 214.467 169.074 228.117 1.00 23.37 ? 4123 ARG A N     1 
ATOM   19081 C CA    . ARG A 1 4123 ? 213.191 169.756 227.902 1.00 26.65 ? 4123 ARG A CA    1 
ATOM   19082 C C     . ARG A 1 4123 ? 213.432 171.233 228.193 1.00 22.41 ? 4123 ARG A C     1 
ATOM   19083 O O     . ARG A 1 4123 ? 213.810 171.592 229.311 1.00 27.90 ? 4123 ARG A O     1 
ATOM   19084 C CB    . ARG A 1 4123 ? 212.092 169.188 228.786 1.00 26.31 ? 4123 ARG A CB    1 
ATOM   19085 C CG    . ARG A 1 4123 ? 211.607 167.809 228.381 1.00 28.05 ? 4123 ARG A CG    1 
ATOM   19086 C CD    . ARG A 1 4123 ? 211.013 167.792 226.987 1.00 23.09 ? 4123 ARG A CD    1 
ATOM   19087 N NE    . ARG A 1 4123 ? 210.438 166.488 226.684 1.00 25.71 ? 4123 ARG A NE    1 
ATOM   19088 C CZ    . ARG A 1 4123 ? 211.102 165.489 226.119 1.00 27.82 ? 4123 ARG A CZ    1 
ATOM   19089 N NH1   . ARG A 1 4123 ? 212.375 165.611 225.779 1.00 25.80 ? 4123 ARG A NH1   1 
ATOM   19090 N NH2   . ARG A 1 4123 ? 210.474 164.340 225.891 1.00 25.66 ? 4123 ARG A NH2   1 
ATOM   19091 N N     . LEU A 1 4124 ? 213.215 172.075 227.191 1.00 19.13 ? 4124 LEU A N     1 
ATOM   19092 C CA    . LEU A 1 4124 ? 213.508 173.493 227.307 1.00 18.78 ? 4124 LEU A CA    1 
ATOM   19093 C C     . LEU A 1 4124 ? 212.212 174.274 227.483 1.00 18.12 ? 4124 LEU A C     1 
ATOM   19094 O O     . LEU A 1 4124 ? 211.297 174.174 226.662 1.00 27.69 ? 4124 LEU A O     1 
ATOM   19095 C CB    . LEU A 1 4124 ? 214.275 173.967 226.070 1.00 19.41 ? 4124 LEU A CB    1 
ATOM   19096 C CG    . LEU A 1 4124 ? 214.871 175.372 225.991 1.00 18.40 ? 4124 LEU A CG    1 
ATOM   19097 C CD1   . LEU A 1 4124 ? 216.065 175.372 225.053 1.00 22.49 ? 4124 LEU A CD1   1 
ATOM   19098 C CD2   . LEU A 1 4124 ? 213.856 176.361 225.513 1.00 17.76 ? 4124 LEU A CD2   1 
ATOM   19099 N N     . PHE A 1 4125 ? 212.140 175.051 228.563 1.00 13.45 ? 4125 PHE A N     1 
ATOM   19100 C CA    . PHE A 1 4125 ? 210.949 175.822 228.911 1.00 11.74 ? 4125 PHE A CA    1 
ATOM   19101 C C     . PHE A 1 4125 ? 211.270 177.306 228.803 1.00 18.24 ? 4125 PHE A C     1 
ATOM   19102 O O     . PHE A 1 4125 ? 212.209 177.789 229.444 1.00 24.14 ? 4125 PHE A O     1 
ATOM   19103 C CB    . PHE A 1 4125 ? 210.461 175.487 230.319 1.00 19.14 ? 4125 PHE A CB    1 
ATOM   19104 C CG    . PHE A 1 4125 ? 210.104 174.044 230.517 1.00 17.08 ? 4125 PHE A CG    1 
ATOM   19105 C CD1   . PHE A 1 4125 ? 208.868 173.563 230.126 1.00 17.38 ? 4125 PHE A CD1   1 
ATOM   19106 C CD2   . PHE A 1 4125 ? 211.002 173.170 231.100 1.00 21.44 ? 4125 PHE A CD2   1 
ATOM   19107 C CE1   . PHE A 1 4125 ? 208.535 172.237 230.312 1.00 20.65 ? 4125 PHE A CE1   1 
ATOM   19108 C CE2   . PHE A 1 4125 ? 210.677 171.843 231.286 1.00 20.09 ? 4125 PHE A CE2   1 
ATOM   19109 C CZ    . PHE A 1 4125 ? 209.442 171.376 230.892 1.00 19.13 ? 4125 PHE A CZ    1 
ATOM   19110 N N     . LEU A 1 4126 ? 210.491 178.027 227.997 1.00 20.26 ? 4126 LEU A N     1 
ATOM   19111 C CA    . LEU A 1 4126 ? 210.579 179.483 227.916 1.00 20.19 ? 4126 LEU A CA    1 
ATOM   19112 C C     . LEU A 1 4126 ? 209.308 180.079 228.512 1.00 18.78 ? 4126 LEU A C     1 
ATOM   19113 O O     . LEU A 1 4126 ? 208.243 180.095 227.897 1.00 21.44 ? 4126 LEU A O     1 
ATOM   19114 C CB    . LEU A 1 4126 ? 210.793 179.939 226.477 1.00 17.57 ? 4126 LEU A CB    1 
ATOM   19115 C CG    . LEU A 1 4126 ? 211.992 179.331 225.765 1.00 15.84 ? 4126 LEU A CG    1 
ATOM   19116 C CD1   . LEU A 1 4126 ? 212.138 179.899 224.373 1.00 18.12 ? 4126 LEU A CD1   1 
ATOM   19117 C CD2   . LEU A 1 4126 ? 213.231 179.624 226.581 1.00 20.98 ? 4126 LEU A CD2   1 
ATOM   19118 N N     . THR A 1 4127 ? 209.433 180.572 229.739 1.00 17.29 ? 4127 THR A N     1 
ATOM   19119 C CA    . THR A 1 4127 ? 208.337 181.306 230.351 1.00 18.61 ? 4127 THR A CA    1 
ATOM   19120 C C     . THR A 1 4127 ? 208.331 182.733 229.826 1.00 22.36 ? 4127 THR A C     1 
ATOM   19121 O O     . THR A 1 4127 ? 209.330 183.449 229.930 1.00 25.63 ? 4127 THR A O     1 
ATOM   19122 C CB    . THR A 1 4127 ? 208.460 181.290 231.872 1.00 24.62 ? 4127 THR A CB    1 
ATOM   19123 O OG1   . THR A 1 4127 ? 208.286 179.951 232.346 1.00 27.07 ? 4127 THR A OG1   1 
ATOM   19124 C CG2   . THR A 1 4127 ? 207.395 182.176 232.495 1.00 24.30 ? 4127 THR A CG2   1 
ATOM   19125 N N     . MET A 1 4128 ? 207.206 183.140 229.249 1.00 17.79 ? 4128 MET A N     1 
ATOM   19126 C CA    . MET A 1 4128 ? 207.124 184.423 228.571 1.00 16.58 ? 4128 MET A CA    1 
ATOM   19127 C C     . MET A 1 4128 ? 205.668 184.847 228.462 1.00 15.98 ? 4128 MET A C     1 
ATOM   19128 O O     . MET A 1 4128 ? 204.776 184.021 228.266 1.00 22.62 ? 4128 MET A O     1 
ATOM   19129 C CB    . MET A 1 4128 ? 207.834 184.360 227.207 1.00 17.87 ? 4128 MET A CB    1 
ATOM   19130 C CG    . MET A 1 4128 ? 207.449 183.194 226.281 1.00 19.29 ? 4128 MET A CG    1 
ATOM   19131 S SD    . MET A 1 4128 ? 205.785 183.079 225.603 1.00 31.74 ? 4128 MET A SD    1 
ATOM   19132 C CE    . MET A 1 4128 ? 205.657 184.633 224.734 1.00 16.05 ? 4128 MET A CE    1 
ATOM   19133 N N     . GLU A 1 4129 ? 205.443 186.143 228.643 1.00 15.81 ? 4129 GLU A N     1 
ATOM   19134 C CA    . GLU A 1 4129 ? 204.108 186.713 228.640 1.00 14.01 ? 4129 GLU A CA    1 
ATOM   19135 C C     . GLU A 1 4129 ? 203.631 186.926 227.208 1.00 16.37 ? 4129 GLU A C     1 
ATOM   19136 O O     . GLU A 1 4129 ? 204.418 186.950 226.261 1.00 24.90 ? 4129 GLU A O     1 
ATOM   19137 C CB    . GLU A 1 4129 ? 204.101 188.028 229.414 1.00 16.12 ? 4129 GLU A CB    1 
ATOM   19138 C CG    . GLU A 1 4129 ? 203.948 187.855 230.913 1.00 22.78 ? 4129 GLU A CG    1 
ATOM   19139 C CD    . GLU A 1 4129 ? 203.436 189.105 231.591 1.00 23.11 ? 4129 GLU A CD    1 
ATOM   19140 O OE1   . GLU A 1 4129 ? 203.218 190.114 230.889 1.00 20.68 ? 4129 GLU A OE1   1 
ATOM   19141 O OE2   . GLU A 1 4129 ? 203.249 189.078 232.825 1.00 23.87 ? 4129 GLU A OE2   1 
ATOM   19142 N N     . ILE A 1 4130 ? 202.325 187.124 227.050 1.00 13.65 ? 4130 ILE A N     1 
ATOM   19143 C CA    . ILE A 1 4130 ? 201.760 187.236 225.711 1.00 11.86 ? 4130 ILE A CA    1 
ATOM   19144 C C     . ILE A 1 4130 ? 202.098 188.618 225.173 1.00 11.20 ? 4130 ILE A C     1 
ATOM   19145 O O     . ILE A 1 4130 ? 201.355 189.584 225.377 1.00 19.57 ? 4130 ILE A O     1 
ATOM   19146 C CB    . ILE A 1 4130 ? 200.241 186.986 225.710 1.00 16.10 ? 4130 ILE A CB    1 
ATOM   19147 C CG1   . ILE A 1 4130 ? 199.923 185.609 226.292 1.00 11.95 ? 4130 ILE A CG1   1 
ATOM   19148 C CG2   . ILE A 1 4130 ? 199.684 187.086 224.302 1.00 13.89 ? 4130 ILE A CG2   1 
ATOM   19149 C CD1   . ILE A 1 4130 ? 198.451 185.262 226.266 1.00 11.36 ? 4130 ILE A CD1   1 
ATOM   19150 N N     . ASN A 1 4131 ? 203.233 188.712 224.483 1.00 12.94 ? 4131 ASN A N     1 
ATOM   19151 C CA    . ASN A 1 4131 ? 203.762 189.952 223.953 1.00 15.49 ? 4131 ASN A CA    1 
ATOM   19152 C C     . ASN A 1 4131 ? 203.886 189.840 222.441 1.00 17.40 ? 4131 ASN A C     1 
ATOM   19153 O O     . ASN A 1 4131 ? 204.535 188.908 221.945 1.00 18.59 ? 4131 ASN A O     1 
ATOM   19154 C CB    . ASN A 1 4131 ? 205.134 190.265 224.573 1.00 12.06 ? 4131 ASN A CB    1 
ATOM   19155 C CG    . ASN A 1 4131 ? 205.601 191.673 224.273 1.00 19.33 ? 4131 ASN A CG    1 
ATOM   19156 O OD1   . ASN A 1 4131 ? 204.828 192.627 224.358 1.00 20.84 ? 4131 ASN A OD1   1 
ATOM   19157 N ND2   . ASN A 1 4131 ? 206.872 191.810 223.916 1.00 23.99 ? 4131 ASN A ND2   1 
ATOM   19158 N N     . PRO A 1 4132 ? 203.289 190.757 221.674 1.00 15.36 ? 4132 PRO A N     1 
ATOM   19159 C CA    . PRO A 1 4132 ? 203.276 190.606 220.211 1.00 15.70 ? 4132 PRO A CA    1 
ATOM   19160 C C     . PRO A 1 4132 ? 204.634 190.759 219.549 1.00 19.93 ? 4132 PRO A C     1 
ATOM   19161 O O     . PRO A 1 4132 ? 204.743 190.496 218.346 1.00 15.93 ? 4132 PRO A O     1 
ATOM   19162 C CB    . PRO A 1 4132 ? 202.313 191.713 219.757 1.00 11.79 ? 4132 PRO A CB    1 
ATOM   19163 C CG    . PRO A 1 4132 ? 202.340 192.713 220.858 1.00 17.33 ? 4132 PRO A CG    1 
ATOM   19164 C CD    . PRO A 1 4132 ? 202.515 191.927 222.118 1.00 16.74 ? 4132 PRO A CD    1 
ATOM   19165 N N     . LYS A 1 4133 ? 205.669 191.165 220.275 1.00 23.03 ? 4133 LYS A N     1 
ATOM   19166 C CA    . LYS A 1 4133 ? 206.981 191.359 219.678 1.00 26.06 ? 4133 LYS A CA    1 
ATOM   19167 C C     . LYS A 1 4133 ? 207.792 190.063 219.704 1.00 22.46 ? 4133 LYS A C     1 
ATOM   19168 O O     . LYS A 1 4133 ? 208.847 189.979 219.065 1.00 24.86 ? 4133 LYS A O     1 
ATOM   19169 C CB    . LYS A 1 4133 ? 207.704 192.502 220.417 1.00 19.68 ? 4133 LYS A CB    1 
ATOM   19170 C CG    . LYS A 1 4133 ? 209.199 192.652 220.184 1.00 20.71 ? 4133 LYS A CG    1 
ATOM   19171 C CD    . LYS A 1 4133 ? 209.428 192.974 218.703 1.00 21.43 ? 4133 LYS A CD    1 
ATOM   19172 C CE    . LYS A 1 4133 ? 210.741 192.439 218.170 1.00 20.86 ? 4133 LYS A CE    1 
ATOM   19173 N NZ    . LYS A 1 4133 ? 210.593 191.089 217.555 1.00 17.58 ? 4133 LYS A NZ    1 
ATOM   19174 N N     . VAL A 1 4134 ? 207.284 189.036 220.376 1.00 14.86 ? 4134 VAL A N     1 
ATOM   19175 C CA    . VAL A 1 4134 ? 207.964 187.738 220.475 1.00 18.51 ? 4134 VAL A CA    1 
ATOM   19176 C C     . VAL A 1 4134 ? 208.112 187.139 219.082 1.00 22.97 ? 4134 VAL A C     1 
ATOM   19177 O O     . VAL A 1 4134 ? 207.181 187.251 218.264 1.00 28.03 ? 4134 VAL A O     1 
ATOM   19178 C CB    . VAL A 1 4134 ? 207.178 186.805 221.402 1.00 18.72 ? 4134 VAL A CB    1 
ATOM   19179 C CG1   . VAL A 1 4134 ? 207.739 185.389 221.376 1.00 18.16 ? 4134 VAL A CG1   1 
ATOM   19180 C CG2   . VAL A 1 4134 ? 207.187 187.349 222.819 1.00 19.07 ? 4134 VAL A CG2   1 
ATOM   19181 N N     . PRO A 1 4135 ? 209.250 186.522 218.757 1.00 20.13 ? 4135 PRO A N     1 
ATOM   19182 C CA    . PRO A 1 4135 ? 209.440 185.980 217.406 1.00 15.60 ? 4135 PRO A CA    1 
ATOM   19183 C C     . PRO A 1 4135 ? 208.371 184.966 217.027 1.00 19.20 ? 4135 PRO A C     1 
ATOM   19184 O O     . PRO A 1 4135 ? 207.971 184.122 217.830 1.00 18.96 ? 4135 PRO A O     1 
ATOM   19185 C CB    . PRO A 1 4135 ? 210.822 185.326 217.484 1.00 18.71 ? 4135 PRO A CB    1 
ATOM   19186 C CG    . PRO A 1 4135 ? 211.527 186.078 218.552 1.00 21.61 ? 4135 PRO A CG    1 
ATOM   19187 C CD    . PRO A 1 4135 ? 210.482 186.440 219.561 1.00 18.68 ? 4135 PRO A CD    1 
ATOM   19188 N N     . VAL A 1 4136 ? 207.914 185.061 215.777 1.00 19.44 ? 4136 VAL A N     1 
ATOM   19189 C CA    . VAL A 1 4136 ? 206.952 184.098 215.252 1.00 13.07 ? 4136 VAL A CA    1 
ATOM   19190 C C     . VAL A 1 4136 ? 207.621 182.754 214.997 1.00 13.70 ? 4136 VAL A C     1 
ATOM   19191 O O     . VAL A 1 4136 ? 206.991 181.700 215.149 1.00 13.41 ? 4136 VAL A O     1 
ATOM   19192 C CB    . VAL A 1 4136 ? 206.291 184.659 213.979 1.00 9.86  ? 4136 VAL A CB    1 
ATOM   19193 C CG1   . VAL A 1 4136 ? 205.355 183.636 213.358 1.00 11.08 ? 4136 VAL A CG1   1 
ATOM   19194 C CG2   . VAL A 1 4136 ? 205.549 185.944 214.292 1.00 11.83 ? 4136 VAL A CG2   1 
ATOM   19195 N N     . ASN A 1 4137 ? 208.899 182.763 214.607 1.00 14.11 ? 4137 ASN A N     1 
ATOM   19196 C CA    . ASN A 1 4137 ? 209.604 181.514 214.331 1.00 12.09 ? 4137 ASN A CA    1 
ATOM   19197 C C     . ASN A 1 4137 ? 209.649 180.621 215.564 1.00 13.02 ? 4137 ASN A C     1 
ATOM   19198 O O     . ASN A 1 4137 ? 209.525 179.396 215.456 1.00 11.45 ? 4137 ASN A O     1 
ATOM   19199 C CB    . ASN A 1 4137 ? 211.019 181.807 213.834 1.00 15.13 ? 4137 ASN A CB    1 
ATOM   19200 C CG    . ASN A 1 4137 ? 211.031 182.498 212.488 1.00 19.27 ? 4137 ASN A CG    1 
ATOM   19201 O OD1   . ASN A 1 4137 ? 210.285 182.131 211.582 1.00 17.04 ? 4137 ASN A OD1   1 
ATOM   19202 N ND2   . ASN A 1 4137 ? 211.885 183.506 212.349 1.00 25.80 ? 4137 ASN A ND2   1 
ATOM   19203 N N     . LEU A 1 4138 ? 209.841 181.216 216.743 1.00 17.38 ? 4138 LEU A N     1 
ATOM   19204 C CA    . LEU A 1 4138 ? 209.794 180.438 217.976 1.00 16.65 ? 4138 LEU A CA    1 
ATOM   19205 C C     . LEU A 1 4138 ? 208.400 179.875 218.215 1.00 17.67 ? 4138 LEU A C     1 
ATOM   19206 O O     . LEU A 1 4138 ? 208.251 178.742 218.688 1.00 18.87 ? 4138 LEU A O     1 
ATOM   19207 C CB    . LEU A 1 4138 ? 210.225 181.300 219.159 1.00 13.53 ? 4138 LEU A CB    1 
ATOM   19208 C CG    . LEU A 1 4138 ? 210.287 180.548 220.488 1.00 13.07 ? 4138 LEU A CG    1 
ATOM   19209 C CD1   . LEU A 1 4138 ? 211.416 179.529 220.473 1.00 16.29 ? 4138 LEU A CD1   1 
ATOM   19210 C CD2   . LEU A 1 4138 ? 210.423 181.505 221.649 1.00 13.02 ? 4138 LEU A CD2   1 
ATOM   19211 N N     . LEU A 1 4139 ? 207.367 180.659 217.905 1.00 15.20 ? 4139 LEU A N     1 
ATOM   19212 C CA    . LEU A 1 4139 ? 205.997 180.203 218.111 1.00 10.02 ? 4139 LEU A CA    1 
ATOM   19213 C C     . LEU A 1 4139 ? 205.672 179.011 217.218 1.00 15.96 ? 4139 LEU A C     1 
ATOM   19214 O O     . LEU A 1 4139 ? 205.006 178.065 217.653 1.00 12.69 ? 4139 LEU A O     1 
ATOM   19215 C CB    . LEU A 1 4139 ? 205.028 181.356 217.855 1.00 10.12 ? 4139 LEU A CB    1 
ATOM   19216 C CG    . LEU A 1 4139 ? 204.509 182.119 219.076 1.00 13.04 ? 4139 LEU A CG    1 
ATOM   19217 C CD1   . LEU A 1 4139 ? 205.659 182.596 219.942 1.00 13.43 ? 4139 LEU A CD1   1 
ATOM   19218 C CD2   . LEU A 1 4139 ? 203.660 183.295 218.639 1.00 6.76  ? 4139 LEU A CD2   1 
ATOM   19219 N N     . ARG A 1 4140 ? 206.126 179.046 215.962 1.00 14.07 ? 4140 ARG A N     1 
ATOM   19220 C CA    . ARG A 1 4140 ? 205.920 177.912 215.063 1.00 6.78  ? 4140 ARG A CA    1 
ATOM   19221 C C     . ARG A 1 4140 ? 206.664 176.670 215.533 1.00 3.69  ? 4140 ARG A C     1 
ATOM   19222 O O     . ARG A 1 4140 ? 206.121 175.562 215.462 1.00 10.09 ? 4140 ARG A O     1 
ATOM   19223 C CB    . ARG A 1 4140 ? 206.360 178.265 213.641 1.00 9.14  ? 4140 ARG A CB    1 
ATOM   19224 C CG    . ARG A 1 4140 ? 205.870 179.604 213.127 1.00 11.83 ? 4140 ARG A CG    1 
ATOM   19225 C CD    . ARG A 1 4140 ? 204.368 179.589 212.883 1.00 7.46  ? 4140 ARG A CD    1 
ATOM   19226 N NE    . ARG A 1 4140 ? 203.924 178.595 211.908 1.00 11.50 ? 4140 ARG A NE    1 
ATOM   19227 C CZ    . ARG A 1 4140 ? 204.427 178.420 210.691 1.00 14.53 ? 4140 ARG A CZ    1 
ATOM   19228 N NH1   . ARG A 1 4140 ? 205.350 179.228 210.193 1.00 14.96 ? 4140 ARG A NH1   1 
ATOM   19229 N NH2   . ARG A 1 4140 ? 203.968 177.424 209.938 1.00 12.57 ? 4140 ARG A NH2   1 
ATOM   19230 N N     . ALA A 1 4141 ? 207.895 176.829 216.012 1.00 5.72  ? 4141 ALA A N     1 
ATOM   19231 C CA    . ALA A 1 4141 ? 208.769 175.705 216.316 1.00 10.76 ? 4141 ALA A CA    1 
ATOM   19232 C C     . ALA A 1 4141 ? 208.622 175.202 217.744 1.00 9.29  ? 4141 ALA A C     1 
ATOM   19233 O O     . ALA A 1 4141 ? 209.328 174.267 218.133 1.00 10.34 ? 4141 ALA A O     1 
ATOM   19234 C CB    . ALA A 1 4141 ? 210.226 176.086 216.050 1.00 14.73 ? 4141 ALA A CB    1 
ATOM   19235 N N     . GLY A 1 4142 ? 207.719 175.787 218.532 1.00 9.72  ? 4142 GLY A N     1 
ATOM   19236 C CA    . GLY A 1 4142 ? 207.583 175.412 219.921 1.00 10.82 ? 4142 GLY A CA    1 
ATOM   19237 C C     . GLY A 1 4142 ? 206.144 175.103 220.277 1.00 8.10  ? 4142 GLY A C     1 
ATOM   19238 O O     . GLY A 1 4142 ? 205.207 175.490 219.576 1.00 15.23 ? 4142 GLY A O     1 
ATOM   19239 N N     . ARG A 1 4143 ? 205.988 174.390 221.388 1.00 7.83  ? 4143 ARG A N     1 
ATOM   19240 C CA    . ARG A 1 4143 ? 204.671 174.048 221.902 1.00 8.95  ? 4143 ARG A CA    1 
ATOM   19241 C C     . ARG A 1 4143 ? 204.172 175.157 222.818 1.00 7.35  ? 4143 ARG A C     1 
ATOM   19242 O O     . ARG A 1 4143 ? 204.819 175.490 223.815 1.00 13.41 ? 4143 ARG A O     1 
ATOM   19243 C CB    . ARG A 1 4143 ? 204.726 172.714 222.646 1.00 9.31  ? 4143 ARG A CB    1 
ATOM   19244 C CG    . ARG A 1 4143 ? 203.375 172.158 223.058 1.00 9.17  ? 4143 ARG A CG    1 
ATOM   19245 C CD    . ARG A 1 4143 ? 202.600 171.606 221.874 1.00 10.63 ? 4143 ARG A CD    1 
ATOM   19246 N NE    . ARG A 1 4143 ? 201.261 171.182 222.265 1.00 10.28 ? 4143 ARG A NE    1 
ATOM   19247 C CZ    . ARG A 1 4143 ? 200.945 169.949 222.637 1.00 10.47 ? 4143 ARG A CZ    1 
ATOM   19248 N NH1   . ARG A 1 4143 ? 201.841 168.976 222.632 1.00 12.47 ? 4143 ARG A NH1   1 
ATOM   19249 N NH2   . ARG A 1 4143 ? 199.700 169.685 223.020 1.00 7.70  ? 4143 ARG A NH2   1 
ATOM   19250 N N     . ILE A 1 4144 ? 203.018 175.725 222.483 1.00 7.70  ? 4144 ILE A N     1 
ATOM   19251 C CA    . ILE A 1 4144 ? 202.488 176.905 223.156 1.00 8.09  ? 4144 ILE A CA    1 
ATOM   19252 C C     . ILE A 1 4144 ? 201.424 176.469 224.151 1.00 9.22  ? 4144 ILE A C     1 
ATOM   19253 O O     . ILE A 1 4144 ? 200.443 175.813 223.780 1.00 14.58 ? 4144 ILE A O     1 
ATOM   19254 C CB    . ILE A 1 4144 ? 201.921 177.920 222.153 1.00 11.92 ? 4144 ILE A CB    1 
ATOM   19255 C CG1   . ILE A 1 4144 ? 203.051 178.552 221.339 1.00 9.98  ? 4144 ILE A CG1   1 
ATOM   19256 C CG2   . ILE A 1 4144 ? 201.094 178.977 222.863 1.00 6.91  ? 4144 ILE A CG2   1 
ATOM   19257 C CD1   . ILE A 1 4144 ? 202.628 179.001 219.964 1.00 8.55  ? 4144 ILE A CD1   1 
ATOM   19258 N N     . PHE A 1 4145 ? 201.622 176.836 225.415 1.00 10.59 ? 4145 PHE A N     1 
ATOM   19259 C CA    . PHE A 1 4145 ? 200.651 176.622 226.478 1.00 5.72  ? 4145 PHE A CA    1 
ATOM   19260 C C     . PHE A 1 4145 ? 200.208 177.981 226.996 1.00 8.35  ? 4145 PHE A C     1 
ATOM   19261 O O     . PHE A 1 4145 ? 201.046 178.798 227.388 1.00 18.65 ? 4145 PHE A O     1 
ATOM   19262 C CB    . PHE A 1 4145 ? 201.254 175.800 227.618 1.00 8.74  ? 4145 PHE A CB    1 
ATOM   19263 C CG    . PHE A 1 4145 ? 201.410 174.344 227.303 1.00 8.66  ? 4145 PHE A CG    1 
ATOM   19264 C CD1   . PHE A 1 4145 ? 200.372 173.456 227.511 1.00 7.69  ? 4145 PHE A CD1   1 
ATOM   19265 C CD2   . PHE A 1 4145 ? 202.603 173.862 226.797 1.00 11.43 ? 4145 PHE A CD2   1 
ATOM   19266 C CE1   . PHE A 1 4145 ? 200.524 172.114 227.221 1.00 10.55 ? 4145 PHE A CE1   1 
ATOM   19267 C CE2   . PHE A 1 4145 ? 202.759 172.525 226.505 1.00 12.20 ? 4145 PHE A CE2   1 
ATOM   19268 C CZ    . PHE A 1 4145 ? 201.719 171.650 226.716 1.00 11.57 ? 4145 PHE A CZ    1 
ATOM   19269 N N     . VAL A 1 4146 ? 198.906 178.220 227.004 1.00 4.88  ? 4146 VAL A N     1 
ATOM   19270 C CA    . VAL A 1 4146 ? 198.343 179.493 227.440 1.00 4.91  ? 4146 VAL A CA    1 
ATOM   19271 C C     . VAL A 1 4146 ? 197.676 179.316 228.794 1.00 10.29 ? 4146 VAL A C     1 
ATOM   19272 O O     . VAL A 1 4146 ? 196.860 178.407 228.987 1.00 7.53  ? 4146 VAL A O     1 
ATOM   19273 C CB    . VAL A 1 4146 ? 197.350 180.045 226.401 1.00 3.32  ? 4146 VAL A CB    1 
ATOM   19274 C CG1   . VAL A 1 4146 ? 196.688 181.307 226.913 1.00 0.50  ? 4146 VAL A CG1   1 
ATOM   19275 C CG2   . VAL A 1 4146 ? 198.075 180.341 225.107 1.00 9.66  ? 4146 VAL A CG2   1 
ATOM   19276 N N     . PHE A 1 4147 ? 198.028 180.189 229.735 1.00 11.77 ? 4147 PHE A N     1 
ATOM   19277 C CA    . PHE A 1 4147 ? 197.446 180.203 231.068 1.00 9.08  ? 4147 PHE A CA    1 
ATOM   19278 C C     . PHE A 1 4147 ? 196.837 181.569 231.330 1.00 9.38  ? 4147 PHE A C     1 
ATOM   19279 O O     . PHE A 1 4147 ? 197.441 182.594 231.000 1.00 9.81  ? 4147 PHE A O     1 
ATOM   19280 C CB    . PHE A 1 4147 ? 198.499 179.876 232.122 1.00 12.19 ? 4147 PHE A CB    1 
ATOM   19281 C CG    . PHE A 1 4147 ? 199.324 178.676 231.785 1.00 11.66 ? 4147 PHE A CG    1 
ATOM   19282 C CD1   . PHE A 1 4147 ? 200.601 178.820 231.299 1.00 8.87  ? 4147 PHE A CD1   1 
ATOM   19283 C CD2   . PHE A 1 4147 ? 198.820 177.398 231.959 1.00 13.84 ? 4147 PHE A CD2   1 
ATOM   19284 C CE1   . PHE A 1 4147 ? 201.358 177.714 230.985 1.00 13.73 ? 4147 PHE A CE1   1 
ATOM   19285 C CE2   . PHE A 1 4147 ? 199.578 176.284 231.651 1.00 15.10 ? 4147 PHE A CE2   1 
ATOM   19286 C CZ    . PHE A 1 4147 ? 200.846 176.442 231.166 1.00 15.40 ? 4147 PHE A CZ    1 
ATOM   19287 N N     . GLU A 1 4148 ? 195.650 181.576 231.922 1.00 5.26  ? 4148 GLU A N     1 
ATOM   19288 C CA    . GLU A 1 4148 ? 194.890 182.776 232.217 1.00 3.83  ? 4148 GLU A CA    1 
ATOM   19289 C C     . GLU A 1 4148 ? 194.499 182.773 233.685 1.00 11.11 ? 4148 GLU A C     1 
ATOM   19290 O O     . GLU A 1 4148 ? 194.289 181.707 234.271 1.00 12.91 ? 4148 GLU A O     1 
ATOM   19291 C CB    . GLU A 1 4148 ? 193.622 182.843 231.353 1.00 6.30  ? 4148 GLU A CB    1 
ATOM   19292 C CG    . GLU A 1 4148 ? 193.841 183.314 229.927 1.00 2.82  ? 4148 GLU A CG    1 
ATOM   19293 C CD    . GLU A 1 4148 ? 192.542 183.490 229.166 1.00 5.86  ? 4148 GLU A CD    1 
ATOM   19294 O OE1   . GLU A 1 4148 ? 191.575 182.761 229.462 1.00 11.43 ? 4148 GLU A OE1   1 
ATOM   19295 O OE2   . GLU A 1 4148 ? 192.485 184.361 228.273 1.00 10.09 ? 4148 GLU A OE2   1 
ATOM   19296 N N     . PRO A 1 4149 ? 194.391 183.943 234.304 1.00 10.86 ? 4149 PRO A N     1 
ATOM   19297 C CA    . PRO A 1 4149 ? 193.873 184.007 235.668 1.00 6.55  ? 4149 PRO A CA    1 
ATOM   19298 C C     . PRO A 1 4149 ? 192.404 183.633 235.697 1.00 3.50  ? 4149 PRO A C     1 
ATOM   19299 O O     . PRO A 1 4149 ? 191.587 184.240 234.988 1.00 1.42  ? 4149 PRO A O     1 
ATOM   19300 C CB    . PRO A 1 4149 ? 194.087 185.477 236.059 1.00 9.71  ? 4149 PRO A CB    1 
ATOM   19301 C CG    . PRO A 1 4149 ? 194.142 186.204 234.771 1.00 8.51  ? 4149 PRO A CG    1 
ATOM   19302 C CD    . PRO A 1 4149 ? 194.776 185.268 233.793 1.00 7.89  ? 4149 PRO A CD    1 
ATOM   19303 N N     . PRO A 1 4150 ? 192.031 182.630 236.487 1.00 2.61  ? 4150 PRO A N     1 
ATOM   19304 C CA    . PRO A 1 4150 ? 190.628 182.212 236.552 1.00 1.91  ? 4150 PRO A CA    1 
ATOM   19305 C C     . PRO A 1 4150 ? 189.737 183.359 236.992 1.00 4.11  ? 4150 PRO A C     1 
ATOM   19306 O O     . PRO A 1 4150 ? 190.040 184.054 237.973 1.00 9.76  ? 4150 PRO A O     1 
ATOM   19307 C CB    . PRO A 1 4150 ? 190.643 181.082 237.593 1.00 2.62  ? 4150 PRO A CB    1 
ATOM   19308 C CG    . PRO A 1 4150 ? 192.061 180.607 237.619 1.00 3.27  ? 4150 PRO A CG    1 
ATOM   19309 C CD    . PRO A 1 4150 ? 192.895 181.817 237.359 1.00 3.01  ? 4150 PRO A CD    1 
ATOM   19310 N N     . PRO A 1 4151 ? 188.633 183.594 236.284 1.00 2.77  ? 4151 PRO A N     1 
ATOM   19311 C CA    . PRO A 1 4151 ? 187.756 184.714 236.638 1.00 3.31  ? 4151 PRO A CA    1 
ATOM   19312 C C     . PRO A 1 4151 ? 187.113 184.516 238.002 1.00 5.71  ? 4151 PRO A C     1 
ATOM   19313 O O     . PRO A 1 4151 ? 186.846 183.392 238.432 1.00 11.10 ? 4151 PRO A O     1 
ATOM   19314 C CB    . PRO A 1 4151 ? 186.704 184.711 235.522 1.00 1.84  ? 4151 PRO A CB    1 
ATOM   19315 C CG    . PRO A 1 4151 ? 187.309 183.914 234.414 1.00 5.03  ? 4151 PRO A CG    1 
ATOM   19316 C CD    . PRO A 1 4151 ? 188.174 182.893 235.075 1.00 5.84  ? 4151 PRO A CD    1 
ATOM   19317 N N     . GLY A 1 4152 ? 186.868 185.628 238.683 1.00 1.12  ? 4152 GLY A N     1 
ATOM   19318 C CA    . GLY A 1 4152 ? 186.171 185.603 239.957 1.00 1.12  ? 4152 GLY A CA    1 
ATOM   19319 C C     . GLY A 1 4152 ? 186.896 186.343 241.062 1.00 6.48  ? 4152 GLY A C     1 
ATOM   19320 O O     . GLY A 1 4152 ? 188.122 186.471 241.061 1.00 2.83  ? 4152 GLY A O     1 
ATOM   19321 N N     . VAL A 1 4153 ? 186.118 186.847 242.022 1.00 7.44  ? 4153 VAL A N     1 
ATOM   19322 C CA    . VAL A 1 4153 ? 186.702 187.516 243.179 1.00 2.14  ? 4153 VAL A CA    1 
ATOM   19323 C C     . VAL A 1 4153 ? 187.422 186.511 244.066 1.00 3.71  ? 4153 VAL A C     1 
ATOM   19324 O O     . VAL A 1 4153 ? 188.489 186.800 244.616 1.00 7.75  ? 4153 VAL A O     1 
ATOM   19325 C CB    . VAL A 1 4153 ? 185.614 188.279 243.956 1.00 0.00  ? 4153 VAL A CB    1 
ATOM   19326 C CG1   . VAL A 1 4153 ? 186.218 189.006 245.144 1.00 0.00  ? 4153 VAL A CG1   1 
ATOM   19327 C CG2   . VAL A 1 4153 ? 184.890 189.251 243.043 1.00 2.96  ? 4153 VAL A CG2   1 
ATOM   19328 N N     . LYS A 1 4154 ? 186.848 185.317 244.221 1.00 5.06  ? 4154 LYS A N     1 
ATOM   19329 C CA    . LYS A 1 4154 ? 187.407 184.321 245.129 1.00 0.00  ? 4154 LYS A CA    1 
ATOM   19330 C C     . LYS A 1 4154 ? 188.784 183.860 244.664 1.00 0.00  ? 4154 LYS A C     1 
ATOM   19331 O O     . LYS A 1 4154 ? 189.730 183.785 245.459 1.00 3.20  ? 4154 LYS A O     1 
ATOM   19332 C CB    . LYS A 1 4154 ? 186.435 183.147 245.240 1.00 2.04  ? 4154 LYS A CB    1 
ATOM   19333 C CG    . LYS A 1 4154 ? 186.961 181.909 245.930 1.00 2.96  ? 4154 LYS A CG    1 
ATOM   19334 C CD    . LYS A 1 4154 ? 185.817 180.940 246.180 1.00 1.22  ? 4154 LYS A CD    1 
ATOM   19335 C CE    . LYS A 1 4154 ? 186.297 179.649 246.809 1.00 7.25  ? 4154 LYS A CE    1 
ATOM   19336 N NZ    . LYS A 1 4154 ? 185.164 178.721 247.069 1.00 8.82  ? 4154 LYS A NZ    1 
ATOM   19337 N N     . ALA A 1 4155 ? 188.918 183.556 243.372 1.00 0.00  ? 4155 ALA A N     1 
ATOM   19338 C CA    . ALA A 1 4155 ? 190.215 183.153 242.838 1.00 0.00  ? 4155 ALA A CA    1 
ATOM   19339 C C     . ALA A 1 4155 ? 191.224 184.288 242.926 1.00 1.34  ? 4155 ALA A C     1 
ATOM   19340 O O     . ALA A 1 4155 ? 192.400 184.062 243.235 1.00 11.00 ? 4155 ALA A O     1 
ATOM   19341 C CB    . ALA A 1 4155 ? 190.063 182.681 241.393 1.00 0.00  ? 4155 ALA A CB    1 
ATOM   19342 N N     . ASN A 1 4156 ? 190.780 185.518 242.660 1.00 1.73  ? 4156 ASN A N     1 
ATOM   19343 C CA    . ASN A 1 4156 ? 191.663 186.674 242.772 1.00 1.23  ? 4156 ASN A CA    1 
ATOM   19344 C C     . ASN A 1 4156 ? 192.185 186.824 244.193 1.00 0.09  ? 4156 ASN A C     1 
ATOM   19345 O O     . ASN A 1 4156 ? 193.374 187.091 244.405 1.00 0.00  ? 4156 ASN A O     1 
ATOM   19346 C CB    . ASN A 1 4156 ? 190.915 187.936 242.340 1.00 1.17  ? 4156 ASN A CB    1 
ATOM   19347 C CG    . ASN A 1 4156 ? 191.843 189.043 241.886 1.00 1.88  ? 4156 ASN A CG    1 
ATOM   19348 O OD1   . ASN A 1 4156 ? 192.984 189.139 242.337 1.00 2.20  ? 4156 ASN A OD1   1 
ATOM   19349 N ND2   . ASN A 1 4156 ? 191.353 189.893 240.994 1.00 0.00  ? 4156 ASN A ND2   1 
ATOM   19350 N N     . MET A 1 4157 ? 191.308 186.649 245.181 1.00 2.17  ? 4157 MET A N     1 
ATOM   19351 C CA    . MET A 1 4157 ? 191.704 186.810 246.573 1.00 0.00  ? 4157 MET A CA    1 
ATOM   19352 C C     . MET A 1 4157 ? 192.635 185.689 247.019 1.00 0.09  ? 4157 MET A C     1 
ATOM   19353 O O     . MET A 1 4157 ? 193.593 185.934 247.760 1.00 2.72  ? 4157 MET A O     1 
ATOM   19354 C CB    . MET A 1 4157 ? 190.462 186.874 247.455 1.00 0.00  ? 4157 MET A CB    1 
ATOM   19355 C CG    . MET A 1 4157 ? 189.802 188.234 247.441 1.00 0.00  ? 4157 MET A CG    1 
ATOM   19356 S SD    . MET A 1 4157 ? 188.411 188.363 248.568 1.00 0.00  ? 4157 MET A SD    1 
ATOM   19357 C CE    . MET A 1 4157 ? 189.219 189.170 249.935 1.00 2.86  ? 4157 MET A CE    1 
ATOM   19358 N N     . LEU A 1 4158 ? 192.374 184.454 246.579 1.00 1.12  ? 4158 LEU A N     1 
ATOM   19359 C CA    . LEU A 1 4158 ? 193.320 183.373 246.844 1.00 0.00  ? 4158 LEU A CA    1 
ATOM   19360 C C     . LEU A 1 4158 ? 194.686 183.677 246.247 1.00 0.64  ? 4158 LEU A C     1 
ATOM   19361 O O     . LEU A 1 4158 ? 195.717 183.453 246.891 1.00 12.22 ? 4158 LEU A O     1 
ATOM   19362 C CB    . LEU A 1 4158 ? 192.790 182.045 246.301 1.00 2.64  ? 4158 LEU A CB    1 
ATOM   19363 C CG    . LEU A 1 4158 ? 191.449 181.509 246.792 1.00 1.75  ? 4158 LEU A CG    1 
ATOM   19364 C CD1   . LEU A 1 4158 ? 191.388 180.015 246.576 1.00 8.60  ? 4158 LEU A CD1   1 
ATOM   19365 C CD2   . LEU A 1 4158 ? 191.322 181.800 248.263 1.00 0.00  ? 4158 LEU A CD2   1 
ATOM   19366 N N     . ARG A 1 4159 ? 194.711 184.192 245.017 1.00 1.23  ? 4159 ARG A N     1 
ATOM   19367 C CA    . ARG A 1 4159 ? 195.977 184.519 244.370 1.00 0.00  ? 4159 ARG A CA    1 
ATOM   19368 C C     . ARG A 1 4159 ? 196.724 185.602 245.140 1.00 3.32  ? 4159 ARG A C     1 
ATOM   19369 O O     . ARG A 1 4159 ? 197.935 185.498 245.371 1.00 5.51  ? 4159 ARG A O     1 
ATOM   19370 C CB    . ARG A 1 4159 ? 195.708 184.954 242.930 1.00 0.63  ? 4159 ARG A CB    1 
ATOM   19371 C CG    . ARG A 1 4159 ? 196.870 184.779 241.983 1.00 6.42  ? 4159 ARG A CG    1 
ATOM   19372 C CD    . ARG A 1 4159 ? 196.390 184.551 240.555 1.00 11.93 ? 4159 ARG A CD    1 
ATOM   19373 N NE    . ARG A 1 4159 ? 195.426 185.550 240.103 1.00 9.13  ? 4159 ARG A NE    1 
ATOM   19374 C CZ    . ARG A 1 4159 ? 194.125 185.333 239.966 1.00 0.02  ? 4159 ARG A CZ    1 
ATOM   19375 N NH1   . ARG A 1 4159 ? 193.586 184.160 240.251 1.00 0.00  ? 4159 ARG A NH1   1 
ATOM   19376 N NH2   . ARG A 1 4159 ? 193.346 186.315 239.524 1.00 0.00  ? 4159 ARG A NH2   1 
ATOM   19377 N N     . THR A 1 4160 ? 196.008 186.649 245.558 1.00 7.27  ? 4160 THR A N     1 
ATOM   19378 C CA    . THR A 1 4160 ? 196.642 187.734 246.301 1.00 3.68  ? 4160 THR A CA    1 
ATOM   19379 C C     . THR A 1 4160 ? 197.172 187.247 247.642 1.00 2.15  ? 4160 THR A C     1 
ATOM   19380 O O     . THR A 1 4160 ? 198.281 187.613 248.049 1.00 2.05  ? 4160 THR A O     1 
ATOM   19381 C CB    . THR A 1 4160 ? 195.657 188.882 246.517 1.00 0.69  ? 4160 THR A CB    1 
ATOM   19382 O OG1   . THR A 1 4160 ? 194.467 188.378 247.129 1.00 8.59  ? 4160 THR A OG1   1 
ATOM   19383 C CG2   . THR A 1 4160 ? 195.291 189.527 245.192 1.00 0.00  ? 4160 THR A CG2   1 
ATOM   19384 N N     . PHE A 1 4161 ? 196.394 186.421 248.345 1.00 4.16  ? 4161 PHE A N     1 
ATOM   19385 C CA    . PHE A 1 4161 ? 196.816 185.946 249.656 1.00 2.28  ? 4161 PHE A CA    1 
ATOM   19386 C C     . PHE A 1 4161 ? 197.997 184.992 249.542 1.00 5.97  ? 4161 PHE A C     1 
ATOM   19387 O O     . PHE A 1 4161 ? 198.863 184.961 250.424 1.00 13.14 ? 4161 PHE A O     1 
ATOM   19388 C CB    . PHE A 1 4161 ? 195.641 185.277 250.365 1.00 0.00  ? 4161 PHE A CB    1 
ATOM   19389 C CG    . PHE A 1 4161 ? 194.879 186.200 251.269 1.00 1.05  ? 4161 PHE A CG    1 
ATOM   19390 C CD1   . PHE A 1 4161 ? 195.425 186.629 252.465 1.00 7.72  ? 4161 PHE A CD1   1 
ATOM   19391 C CD2   . PHE A 1 4161 ? 193.618 186.647 250.917 1.00 0.39  ? 4161 PHE A CD2   1 
ATOM   19392 C CE1   . PHE A 1 4161 ? 194.726 187.483 253.293 1.00 5.45  ? 4161 PHE A CE1   1 
ATOM   19393 C CE2   . PHE A 1 4161 ? 192.916 187.500 251.741 1.00 0.00  ? 4161 PHE A CE2   1 
ATOM   19394 C CZ    . PHE A 1 4161 ? 193.471 187.917 252.931 1.00 4.28  ? 4161 PHE A CZ    1 
ATOM   19395 N N     . SER A 1 4162 ? 198.051 184.203 248.467 1.00 1.94  ? 4162 SER A N     1 
ATOM   19396 C CA    . SER A 1 4162 ? 199.213 183.354 248.240 1.00 1.13  ? 4162 SER A CA    1 
ATOM   19397 C C     . SER A 1 4162 ? 200.444 184.176 247.888 1.00 3.10  ? 4162 SER A C     1 
ATOM   19398 O O     . SER A 1 4162 ? 201.562 183.812 248.269 1.00 6.71  ? 4162 SER A O     1 
ATOM   19399 C CB    . SER A 1 4162 ? 198.918 182.341 247.135 1.00 5.04  ? 4162 SER A CB    1 
ATOM   19400 O OG    . SER A 1 4162 ? 197.853 181.485 247.504 1.00 6.86  ? 4162 SER A OG    1 
ATOM   19401 N N     . SER A 1 4163 ? 200.264 185.277 247.155 1.00 4.18  ? 4163 SER A N     1 
ATOM   19402 C CA    . SER A 1 4163 ? 201.404 186.117 246.800 1.00 5.93  ? 4163 SER A CA    1 
ATOM   19403 C C     . SER A 1 4163 ? 202.012 186.788 248.028 1.00 6.55  ? 4163 SER A C     1 
ATOM   19404 O O     . SER A 1 4163 ? 203.240 186.851 248.162 1.00 7.59  ? 4163 SER A O     1 
ATOM   19405 C CB    . SER A 1 4163 ? 200.981 187.162 245.768 1.00 5.97  ? 4163 SER A CB    1 
ATOM   19406 O OG    . SER A 1 4163 ? 200.050 188.078 246.317 1.00 11.57 ? 4163 SER A OG    1 
ATOM   19407 N N     . ILE A 1 4164 ? 201.179 187.292 248.928 1.00 9.40  ? 4164 ILE A N     1 
ATOM   19408 C CA    . ILE A 1 4164 ? 201.682 188.028 250.096 1.00 5.50  ? 4164 ILE A CA    1 
ATOM   19409 C C     . ILE A 1 4164 ? 202.284 187.042 251.092 1.00 6.48  ? 4164 ILE A C     1 
ATOM   19410 O O     . ILE A 1 4164 ? 201.649 186.020 251.407 1.00 4.43  ? 4164 ILE A O     1 
ATOM   19411 C CB    . ILE A 1 4164 ? 200.557 188.839 250.739 1.00 3.36  ? 4164 ILE A CB    1 
ATOM   19412 C CG1   . ILE A 1 4164 ? 199.990 189.850 249.742 1.00 6.53  ? 4164 ILE A CG1   1 
ATOM   19413 C CG2   . ILE A 1 4164 ? 201.062 189.558 251.979 1.00 5.99  ? 4164 ILE A CG2   1 
ATOM   19414 C CD1   . ILE A 1 4164 ? 198.657 190.428 250.156 1.00 4.53  ? 4164 ILE A CD1   1 
ATOM   19415 N N     . PRO A 1 4165 ? 203.487 187.294 251.606 1.00 8.52  ? 4165 PRO A N     1 
ATOM   19416 C CA    . PRO A 1 4165 ? 204.073 186.381 252.595 1.00 6.23  ? 4165 PRO A CA    1 
ATOM   19417 C C     . PRO A 1 4165 ? 203.251 186.329 253.873 1.00 10.53 ? 4165 PRO A C     1 
ATOM   19418 O O     . PRO A 1 4165 ? 202.586 187.295 254.255 1.00 11.98 ? 4165 PRO A O     1 
ATOM   19419 C CB    . PRO A 1 4165 ? 205.461 186.977 252.851 1.00 9.19  ? 4165 PRO A CB    1 
ATOM   19420 C CG    . PRO A 1 4165 ? 205.747 187.810 251.647 1.00 12.74 ? 4165 PRO A CG    1 
ATOM   19421 C CD    . PRO A 1 4165 ? 204.425 188.358 251.215 1.00 13.25 ? 4165 PRO A CD    1 
ATOM   19422 N N     . VAL A 1 4166 ? 203.298 185.171 254.532 1.00 14.43 ? 4166 VAL A N     1 
ATOM   19423 C CA    . VAL A 1 4166 ? 202.570 184.991 255.784 1.00 15.18 ? 4166 VAL A CA    1 
ATOM   19424 C C     . VAL A 1 4166 ? 203.170 185.858 256.885 1.00 15.43 ? 4166 VAL A C     1 
ATOM   19425 O O     . VAL A 1 4166 ? 202.452 186.376 257.748 1.00 15.97 ? 4166 VAL A O     1 
ATOM   19426 C CB    . VAL A 1 4166 ? 202.553 183.501 256.175 1.00 13.28 ? 4166 VAL A CB    1 
ATOM   19427 C CG1   . VAL A 1 4166 ? 201.890 183.305 257.527 1.00 14.33 ? 4166 VAL A CG1   1 
ATOM   19428 C CG2   . VAL A 1 4166 ? 201.844 182.684 255.108 1.00 11.65 ? 4166 VAL A CG2   1 
ATOM   19429 N N     . SER A 1 4167 ? 204.493 186.027 256.877 1.00 13.02 ? 4167 SER A N     1 
ATOM   19430 C CA    . SER A 1 4167 ? 205.146 186.822 257.912 1.00 7.30  ? 4167 SER A CA    1 
ATOM   19431 C C     . SER A 1 4167 ? 204.716 188.284 257.851 1.00 11.43 ? 4167 SER A C     1 
ATOM   19432 O O     . SER A 1 4167 ? 204.495 188.914 258.891 1.00 20.77 ? 4167 SER A O     1 
ATOM   19433 C CB    . SER A 1 4167 ? 206.663 186.707 257.780 1.00 13.63 ? 4167 SER A CB    1 
ATOM   19434 O OG    . SER A 1 4167 ? 207.096 187.161 256.510 1.00 12.28 ? 4167 SER A OG    1 
ATOM   19435 N N     . ARG A 1 4168 ? 204.593 188.838 256.645 1.00 12.87 ? 4168 ARG A N     1 
ATOM   19436 C CA    . ARG A 1 4168 ? 204.299 190.257 256.479 1.00 10.78 ? 4168 ARG A CA    1 
ATOM   19437 C C     . ARG A 1 4168 ? 202.880 190.625 256.900 1.00 9.82  ? 4168 ARG A C     1 
ATOM   19438 O O     . ARG A 1 4168 ? 202.613 191.803 257.159 1.00 10.00 ? 4168 ARG A O     1 
ATOM   19439 C CB    . ARG A 1 4168 ? 204.549 190.658 255.021 1.00 10.74 ? 4168 ARG A CB    1 
ATOM   19440 C CG    . ARG A 1 4168 ? 204.390 192.138 254.723 1.00 15.46 ? 4168 ARG A CG    1 
ATOM   19441 C CD    . ARG A 1 4168 ? 205.283 192.569 253.575 1.00 14.50 ? 4168 ARG A CD    1 
ATOM   19442 N NE    . ARG A 1 4168 ? 204.614 192.459 252.285 1.00 10.07 ? 4168 ARG A NE    1 
ATOM   19443 C CZ    . ARG A 1 4168 ? 204.076 193.479 251.632 1.00 7.65  ? 4168 ARG A CZ    1 
ATOM   19444 N NH1   . ARG A 1 4168 ? 204.094 194.705 252.129 1.00 3.82  ? 4168 ARG A NH1   1 
ATOM   19445 N NH2   . ARG A 1 4168 ? 203.507 193.265 250.450 1.00 11.97 ? 4168 ARG A NH2   1 
ATOM   19446 N N     . ILE A 1 4169 ? 201.977 189.653 257.004 1.00 10.77 ? 4169 ILE A N     1 
ATOM   19447 C CA    . ILE A 1 4169 ? 200.582 189.919 257.341 1.00 10.12 ? 4169 ILE A CA    1 
ATOM   19448 C C     . ILE A 1 4169 ? 200.266 189.656 258.807 1.00 8.83  ? 4169 ILE A C     1 
ATOM   19449 O O     . ILE A 1 4169 ? 199.300 190.237 259.329 1.00 9.37  ? 4169 ILE A O     1 
ATOM   19450 C CB    . ILE A 1 4169 ? 199.630 189.105 256.438 1.00 12.95 ? 4169 ILE A CB    1 
ATOM   19451 C CG1   . ILE A 1 4169 ? 198.178 189.553 256.599 1.00 9.53  ? 4169 ILE A CG1   1 
ATOM   19452 C CG2   . ILE A 1 4169 ? 199.761 187.630 256.726 1.00 17.18 ? 4169 ILE A CG2   1 
ATOM   19453 C CD1   . ILE A 1 4169 ? 197.269 189.010 255.527 1.00 11.77 ? 4169 ILE A CD1   1 
ATOM   19454 N N     . CYS A 1 4170 ? 201.051 188.833 259.497 1.00 11.19 ? 4170 CYS A N     1 
ATOM   19455 C CA    . CYS A 1 4170 ? 200.747 188.415 260.861 1.00 16.89 ? 4170 CYS A CA    1 
ATOM   19456 C C     . CYS A 1 4170 ? 201.272 189.360 261.929 1.00 18.29 ? 4170 CYS A C     1 
ATOM   19457 O O     . CYS A 1 4170 ? 200.671 189.462 263.000 1.00 19.69 ? 4170 CYS A O     1 
ATOM   19458 C CB    . CYS A 1 4170 ? 201.315 187.016 261.123 1.00 17.56 ? 4170 CYS A CB    1 
ATOM   19459 S SG    . CYS A 1 4170 ? 203.104 186.887 260.918 1.00 22.74 ? 4170 CYS A SG    1 
ATOM   19460 N N     . LYS A 1 4171 ? 202.376 190.056 261.670 1.00 15.04 ? 4171 LYS A N     1 
ATOM   19461 C CA    . LYS A 1 4171 ? 203.033 190.847 262.699 1.00 19.86 ? 4171 LYS A CA    1 
ATOM   19462 C C     . LYS A 1 4171 ? 202.201 192.081 263.045 1.00 16.48 ? 4171 LYS A C     1 
ATOM   19463 O O     . LYS A 1 4171 ? 201.110 192.304 262.514 1.00 17.67 ? 4171 LYS A O     1 
ATOM   19464 C CB    . LYS A 1 4171 ? 204.427 191.261 262.239 1.00 22.76 ? 4171 LYS A CB    1 
ATOM   19465 C CG    . LYS A 1 4171 ? 204.419 192.290 261.126 1.00 10.74 ? 4171 LYS A CG    1 
ATOM   19466 C CD    . LYS A 1 4171 ? 205.827 192.709 260.759 1.00 16.97 ? 4171 LYS A CD    1 
ATOM   19467 C CE    . LYS A 1 4171 ? 205.822 193.710 259.619 1.00 23.26 ? 4171 LYS A CE    1 
ATOM   19468 N NZ    . LYS A 1 4171 ? 205.441 193.082 258.324 1.00 21.60 ? 4171 LYS A NZ    1 
ATOM   19469 N N     . SER A 1 4172 ? 202.733 192.888 263.974 1.00 17.90 ? 4172 SER A N     1 
ATOM   19470 C CA    . SER A 1 4172 ? 202.228 194.221 264.292 1.00 19.90 ? 4172 SER A CA    1 
ATOM   19471 C C     . SER A 1 4172 ? 200.820 194.136 264.880 1.00 18.87 ? 4172 SER A C     1 
ATOM   19472 O O     . SER A 1 4172 ? 200.360 193.030 265.191 1.00 18.79 ? 4172 SER A O     1 
ATOM   19473 C CB    . SER A 1 4172 ? 202.258 195.095 263.037 1.00 17.55 ? 4172 SER A CB    1 
ATOM   19474 O OG    . SER A 1 4172 ? 201.335 194.635 262.068 1.00 27.41 ? 4172 SER A OG    1 
ATOM   19475 N N     . PRO A 1 4173 ? 200.131 195.261 265.102 1.00 15.28 ? 4173 PRO A N     1 
ATOM   19476 C CA    . PRO A 1 4173 ? 198.715 195.194 265.478 1.00 21.26 ? 4173 PRO A CA    1 
ATOM   19477 C C     . PRO A 1 4173 ? 197.930 194.211 264.624 1.00 18.56 ? 4173 PRO A C     1 
ATOM   19478 O O     . PRO A 1 4173 ? 198.153 194.084 263.418 1.00 25.36 ? 4173 PRO A O     1 
ATOM   19479 C CB    . PRO A 1 4173 ? 198.228 196.630 265.263 1.00 20.17 ? 4173 PRO A CB    1 
ATOM   19480 C CG    . PRO A 1 4173 ? 199.450 197.477 265.394 1.00 22.35 ? 4173 PRO A CG    1 
ATOM   19481 C CD    . PRO A 1 4173 ? 200.673 196.600 265.395 1.00 21.96 ? 4173 PRO A CD    1 
ATOM   19482 N N     . ASN A 1 4174 ? 196.999 193.512 265.269 1.00 13.33 ? 4174 ASN A N     1 
ATOM   19483 C CA    . ASN A 1 4174 ? 196.195 192.504 264.596 1.00 17.65 ? 4174 ASN A CA    1 
ATOM   19484 C C     . ASN A 1 4174 ? 195.238 193.105 263.578 1.00 22.91 ? 4174 ASN A C     1 
ATOM   19485 O O     . ASN A 1 4174 ? 194.651 192.359 262.787 1.00 24.42 ? 4174 ASN A O     1 
ATOM   19486 C CB    . ASN A 1 4174 ? 195.421 191.700 265.635 1.00 18.22 ? 4174 ASN A CB    1 
ATOM   19487 C CG    . ASN A 1 4174 ? 196.323 190.827 266.479 1.00 20.86 ? 4174 ASN A CG    1 
ATOM   19488 O OD1   . ASN A 1 4174 ? 197.253 190.201 265.971 1.00 23.59 ? 4174 ASN A OD1   1 
ATOM   19489 N ND2   . ASN A 1 4174 ? 196.056 190.784 267.778 1.00 15.63 ? 4174 ASN A ND2   1 
ATOM   19490 N N     . GLU A 1 4175 ? 195.064 194.427 263.588 1.00 15.13 ? 4175 GLU A N     1 
ATOM   19491 C CA    . GLU A 1 4175 ? 194.224 195.093 262.602 1.00 6.92  ? 4175 GLU A CA    1 
ATOM   19492 C C     . GLU A 1 4175 ? 194.818 195.033 261.202 1.00 7.41  ? 4175 GLU A C     1 
ATOM   19493 O O     . GLU A 1 4175 ? 194.081 195.185 260.220 1.00 16.71 ? 4175 GLU A O     1 
ATOM   19494 C CB    . GLU A 1 4175 ? 194.002 196.543 263.031 1.00 8.76  ? 4175 GLU A CB    1 
ATOM   19495 C CG    . GLU A 1 4175 ? 192.919 196.708 264.084 1.00 11.78 ? 4175 GLU A CG    1 
ATOM   19496 C CD    . GLU A 1 4175 ? 193.315 196.166 265.440 1.00 20.98 ? 4175 GLU A CD    1 
ATOM   19497 O OE1   . GLU A 1 4175 ? 194.524 196.142 265.748 1.00 24.68 ? 4175 GLU A OE1   1 
ATOM   19498 O OE2   . GLU A 1 4175 ? 192.410 195.747 266.190 1.00 20.97 ? 4175 GLU A OE2   1 
ATOM   19499 N N     . ARG A 1 4176 ? 196.130 194.812 261.087 1.00 5.46  ? 4176 ARG A N     1 
ATOM   19500 C CA    . ARG A 1 4176 ? 196.749 194.718 259.770 1.00 6.79  ? 4176 ARG A CA    1 
ATOM   19501 C C     . ARG A 1 4176 ? 196.214 193.537 258.970 1.00 8.78  ? 4176 ARG A C     1 
ATOM   19502 O O     . ARG A 1 4176 ? 196.135 193.612 257.741 1.00 10.32 ? 4176 ARG A O     1 
ATOM   19503 C CB    . ARG A 1 4176 ? 198.273 194.651 259.903 1.00 4.24  ? 4176 ARG A CB    1 
ATOM   19504 C CG    . ARG A 1 4176 ? 198.966 194.119 258.662 1.00 5.84  ? 4176 ARG A CG    1 
ATOM   19505 C CD    . ARG A 1 4176 ? 200.446 193.861 258.865 1.00 6.19  ? 4176 ARG A CD    1 
ATOM   19506 N NE    . ARG A 1 4176 ? 201.037 194.796 259.811 1.00 8.86  ? 4176 ARG A NE    1 
ATOM   19507 C CZ    . ARG A 1 4176 ? 201.728 195.867 259.444 1.00 11.18 ? 4176 ARG A CZ    1 
ATOM   19508 N NH1   . ARG A 1 4176 ? 201.939 196.145 258.170 1.00 16.70 ? 4176 ARG A NH1   1 
ATOM   19509 N NH2   . ARG A 1 4176 ? 202.216 196.679 260.375 1.00 7.72  ? 4176 ARG A NH2   1 
ATOM   19510 N N     . ALA A 1 4177 ? 195.814 192.454 259.639 1.00 9.61  ? 4177 ALA A N     1 
ATOM   19511 C CA    . ALA A 1 4177 ? 195.218 191.331 258.921 1.00 3.17  ? 4177 ALA A CA    1 
ATOM   19512 C C     . ALA A 1 4177 ? 193.924 191.747 258.232 1.00 3.44  ? 4177 ALA A C     1 
ATOM   19513 O O     . ALA A 1 4177 ? 193.700 191.436 257.055 1.00 9.80  ? 4177 ALA A O     1 
ATOM   19514 C CB    . ALA A 1 4177 ? 194.972 190.168 259.880 1.00 9.74  ? 4177 ALA A CB    1 
ATOM   19515 N N     . ARG A 1 4178 ? 193.064 192.473 258.946 1.00 3.17  ? 4178 ARG A N     1 
ATOM   19516 C CA    . ARG A 1 4178 ? 191.805 192.899 258.348 1.00 4.17  ? 4178 ARG A CA    1 
ATOM   19517 C C     . ARG A 1 4178 ? 192.038 193.972 257.296 1.00 3.07  ? 4178 ARG A C     1 
ATOM   19518 O O     . ARG A 1 4178 ? 191.300 194.045 256.309 1.00 2.78  ? 4178 ARG A O     1 
ATOM   19519 C CB    . ARG A 1 4178 ? 190.861 193.410 259.429 1.00 6.27  ? 4178 ARG A CB    1 
ATOM   19520 C CG    . ARG A 1 4178 ? 189.429 193.615 258.982 1.00 2.97  ? 4178 ARG A CG    1 
ATOM   19521 C CD    . ARG A 1 4178 ? 188.624 194.122 260.152 1.00 6.37  ? 4178 ARG A CD    1 
ATOM   19522 N NE    . ARG A 1 4178 ? 188.498 193.119 261.202 1.00 15.87 ? 4178 ARG A NE    1 
ATOM   19523 C CZ    . ARG A 1 4178 ? 187.465 192.304 261.352 1.00 12.11 ? 4178 ARG A CZ    1 
ATOM   19524 N NH1   . ARG A 1 4178 ? 186.409 192.374 260.561 1.00 8.12  ? 4178 ARG A NH1   1 
ATOM   19525 N NH2   . ARG A 1 4178 ? 187.488 191.404 262.331 1.00 10.47 ? 4178 ARG A NH2   1 
ATOM   19526 N N     . LEU A 1 4179 ? 193.062 194.805 257.488 1.00 8.29  ? 4179 LEU A N     1 
ATOM   19527 C CA    . LEU A 1 4179 ? 193.422 195.781 256.467 1.00 1.10  ? 4179 LEU A CA    1 
ATOM   19528 C C     . LEU A 1 4179 ? 193.875 195.094 255.186 1.00 4.39  ? 4179 LEU A C     1 
ATOM   19529 O O     . LEU A 1 4179 ? 193.515 195.520 254.083 1.00 16.08 ? 4179 LEU A O     1 
ATOM   19530 C CB    . LEU A 1 4179 ? 194.514 196.703 256.998 1.00 0.00  ? 4179 LEU A CB    1 
ATOM   19531 C CG    . LEU A 1 4179 ? 194.011 197.685 258.050 1.00 2.90  ? 4179 LEU A CG    1 
ATOM   19532 C CD1   . LEU A 1 4179 ? 195.156 198.499 258.580 1.00 4.77  ? 4179 LEU A CD1   1 
ATOM   19533 C CD2   . LEU A 1 4179 ? 192.945 198.584 257.462 1.00 8.96  ? 4179 LEU A CD2   1 
ATOM   19534 N N     . TYR A 1 4180 ? 194.666 194.028 255.312 1.00 2.54  ? 4180 TYR A N     1 
ATOM   19535 C CA    . TYR A 1 4180 ? 195.078 193.267 254.139 1.00 1.15  ? 4180 TYR A CA    1 
ATOM   19536 C C     . TYR A 1 4180 ? 193.889 192.584 253.482 1.00 3.60  ? 4180 TYR A C     1 
ATOM   19537 O O     . TYR A 1 4180 ? 193.816 192.497 252.253 1.00 6.67  ? 4180 TYR A O     1 
ATOM   19538 C CB    . TYR A 1 4180 ? 196.134 192.235 254.523 1.00 1.84  ? 4180 TYR A CB    1 
ATOM   19539 C CG    . TYR A 1 4180 ? 197.549 192.737 254.414 1.00 2.94  ? 4180 TYR A CG    1 
ATOM   19540 C CD1   . TYR A 1 4180 ? 198.036 193.685 255.297 1.00 6.51  ? 4180 TYR A CD1   1 
ATOM   19541 C CD2   . TYR A 1 4180 ? 198.399 192.264 253.428 1.00 8.29  ? 4180 TYR A CD2   1 
ATOM   19542 C CE1   . TYR A 1 4180 ? 199.331 194.148 255.203 1.00 7.94  ? 4180 TYR A CE1   1 
ATOM   19543 C CE2   . TYR A 1 4180 ? 199.696 192.720 253.326 1.00 6.91  ? 4180 TYR A CE2   1 
ATOM   19544 C CZ    . TYR A 1 4180 ? 200.156 193.663 254.218 1.00 8.57  ? 4180 TYR A CZ    1 
ATOM   19545 O OH    . TYR A 1 4180 ? 201.447 194.123 254.124 1.00 7.06  ? 4180 TYR A OH    1 
ATOM   19546 N N     . PHE A 1 4181 ? 192.950 192.080 254.286 1.00 1.68  ? 4181 PHE A N     1 
ATOM   19547 C CA    . PHE A 1 4181 ? 191.748 191.484 253.714 1.00 0.00  ? 4181 PHE A CA    1 
ATOM   19548 C C     . PHE A 1 4181 ? 190.958 192.517 252.921 1.00 4.54  ? 4181 PHE A C     1 
ATOM   19549 O O     . PHE A 1 4181 ? 190.475 192.233 251.819 1.00 11.15 ? 4181 PHE A O     1 
ATOM   19550 C CB    . PHE A 1 4181 ? 190.867 190.900 254.814 1.00 4.45  ? 4181 PHE A CB    1 
ATOM   19551 C CG    . PHE A 1 4181 ? 189.495 190.525 254.344 1.00 3.61  ? 4181 PHE A CG    1 
ATOM   19552 C CD1   . PHE A 1 4181 ? 189.310 189.427 253.526 1.00 2.82  ? 4181 PHE A CD1   1 
ATOM   19553 C CD2   . PHE A 1 4181 ? 188.401 191.306 254.656 1.00 9.07  ? 4181 PHE A CD2   1 
ATOM   19554 C CE1   . PHE A 1 4181 ? 188.052 189.082 253.083 1.00 3.22  ? 4181 PHE A CE1   1 
ATOM   19555 C CE2   . PHE A 1 4181 ? 187.146 190.969 254.196 1.00 9.10  ? 4181 PHE A CE2   1 
ATOM   19556 C CZ    . PHE A 1 4181 ? 186.973 189.859 253.411 1.00 5.22  ? 4181 PHE A CZ    1 
ATOM   19557 N N     . LEU A 1 4182 ? 190.806 193.720 253.479 1.00 13.24 ? 4182 LEU A N     1 
ATOM   19558 C CA    . LEU A 1 4182 ? 190.092 194.789 252.790 1.00 2.40  ? 4182 LEU A CA    1 
ATOM   19559 C C     . LEU A 1 4182 ? 190.806 195.183 251.506 1.00 0.00  ? 4182 LEU A C     1 
ATOM   19560 O O     . LEU A 1 4182 ? 190.167 195.433 250.478 1.00 8.97  ? 4182 LEU A O     1 
ATOM   19561 C CB    . LEU A 1 4182 ? 189.955 195.998 253.713 1.00 0.23  ? 4182 LEU A CB    1 
ATOM   19562 C CG    . LEU A 1 4182 ? 188.703 196.077 254.583 1.00 1.27  ? 4182 LEU A CG    1 
ATOM   19563 C CD1   . LEU A 1 4182 ? 188.739 197.342 255.419 1.00 3.89  ? 4182 LEU A CD1   1 
ATOM   19564 C CD2   . LEU A 1 4182 ? 187.451 196.022 253.733 1.00 3.68  ? 4182 LEU A CD2   1 
ATOM   19565 N N     . LEU A 1 4183 ? 192.136 195.256 251.554 1.00 0.00  ? 4183 LEU A N     1 
ATOM   19566 C CA    . LEU A 1 4183 ? 192.912 195.577 250.363 1.00 0.00  ? 4183 LEU A CA    1 
ATOM   19567 C C     . LEU A 1 4183 ? 192.735 194.513 249.288 1.00 2.56  ? 4183 LEU A C     1 
ATOM   19568 O O     . LEU A 1 4183 ? 192.592 194.836 248.103 1.00 7.94  ? 4183 LEU A O     1 
ATOM   19569 C CB    . LEU A 1 4183 ? 194.384 195.723 250.740 1.00 3.45  ? 4183 LEU A CB    1 
ATOM   19570 C CG    . LEU A 1 4183 ? 195.367 196.066 249.627 1.00 6.75  ? 4183 LEU A CG    1 
ATOM   19571 C CD1   . LEU A 1 4183 ? 194.849 197.235 248.810 1.00 7.64  ? 4183 LEU A CD1   1 
ATOM   19572 C CD2   . LEU A 1 4183 ? 196.729 196.372 250.220 1.00 7.29  ? 4183 LEU A CD2   1 
ATOM   19573 N N     . ALA A 1 4184 ? 192.743 193.238 249.682 1.00 7.28  ? 4184 ALA A N     1 
ATOM   19574 C CA    . ALA A 1 4184 ? 192.530 192.158 248.725 1.00 4.32  ? 4184 ALA A CA    1 
ATOM   19575 C C     . ALA A 1 4184 ? 191.130 192.217 248.128 1.00 0.00  ? 4184 ALA A C     1 
ATOM   19576 O O     . ALA A 1 4184 ? 190.954 192.005 246.924 1.00 3.79  ? 4184 ALA A O     1 
ATOM   19577 C CB    . ALA A 1 4184 ? 192.774 190.808 249.396 1.00 2.52  ? 4184 ALA A CB    1 
ATOM   19578 N N     . TRP A 1 4185 ? 190.122 192.498 248.955 1.00 0.00  ? 4185 TRP A N     1 
ATOM   19579 C CA    . TRP A 1 4185 ? 188.761 192.647 248.448 1.00 0.00  ? 4185 TRP A CA    1 
ATOM   19580 C C     . TRP A 1 4185 ? 188.672 193.779 247.435 1.00 5.20  ? 4185 TRP A C     1 
ATOM   19581 O O     . TRP A 1 4185 ? 188.070 193.627 246.368 1.00 12.30 ? 4185 TRP A O     1 
ATOM   19582 C CB    . TRP A 1 4185 ? 187.789 192.895 249.600 1.00 1.10  ? 4185 TRP A CB    1 
ATOM   19583 C CG    . TRP A 1 4185 ? 186.377 193.080 249.144 1.00 0.00  ? 4185 TRP A CG    1 
ATOM   19584 C CD1   . TRP A 1 4185 ? 185.714 194.262 249.011 1.00 1.86  ? 4185 TRP A CD1   1 
ATOM   19585 C CD2   . TRP A 1 4185 ? 185.450 192.058 248.764 1.00 0.38  ? 4185 TRP A CD2   1 
ATOM   19586 N NE1   . TRP A 1 4185 ? 184.435 194.043 248.568 1.00 5.57  ? 4185 TRP A NE1   1 
ATOM   19587 C CE2   . TRP A 1 4185 ? 184.246 192.696 248.411 1.00 4.84  ? 4185 TRP A CE2   1 
ATOM   19588 C CE3   . TRP A 1 4185 ? 185.520 190.665 248.689 1.00 1.29  ? 4185 TRP A CE3   1 
ATOM   19589 C CZ2   . TRP A 1 4185 ? 183.123 191.992 247.987 1.00 6.29  ? 4185 TRP A CZ2   1 
ATOM   19590 C CZ3   . TRP A 1 4185 ? 184.404 189.967 248.271 1.00 4.50  ? 4185 TRP A CZ3   1 
ATOM   19591 C CH2   . TRP A 1 4185 ? 183.222 190.630 247.924 1.00 5.13  ? 4185 TRP A CH2   1 
ATOM   19592 N N     . PHE A 1 4186 ? 189.265 194.929 247.758 1.00 1.21  ? 4186 PHE A N     1 
ATOM   19593 C CA    . PHE A 1 4186 ? 189.227 196.073 246.855 1.00 0.00  ? 4186 PHE A CA    1 
ATOM   19594 C C     . PHE A 1 4186 ? 189.944 195.766 245.544 1.00 3.66  ? 4186 PHE A C     1 
ATOM   19595 O O     . PHE A 1 4186 ? 189.435 196.076 244.459 1.00 19.23 ? 4186 PHE A O     1 
ATOM   19596 C CB    . PHE A 1 4186 ? 189.844 197.283 247.558 1.00 4.08  ? 4186 PHE A CB    1 
ATOM   19597 C CG    . PHE A 1 4186 ? 190.284 198.376 246.634 1.00 5.02  ? 4186 PHE A CG    1 
ATOM   19598 C CD1   . PHE A 1 4186 ? 189.362 199.228 246.055 1.00 1.66  ? 4186 PHE A CD1   1 
ATOM   19599 C CD2   . PHE A 1 4186 ? 191.626 198.559 246.354 1.00 0.07  ? 4186 PHE A CD2   1 
ATOM   19600 C CE1   . PHE A 1 4186 ? 189.772 200.236 245.212 1.00 3.64  ? 4186 PHE A CE1   1 
ATOM   19601 C CE2   . PHE A 1 4186 ? 192.038 199.561 245.510 1.00 1.37  ? 4186 PHE A CE2   1 
ATOM   19602 C CZ    . PHE A 1 4186 ? 191.112 200.400 244.940 1.00 3.61  ? 4186 PHE A CZ    1 
ATOM   19603 N N     . HIS A 1 4187 ? 191.119 195.139 245.626 1.00 0.00  ? 4187 HIS A N     1 
ATOM   19604 C CA    . HIS A 1 4187 ? 191.884 194.807 244.429 1.00 0.00  ? 4187 HIS A CA    1 
ATOM   19605 C C     . HIS A 1 4187 ? 191.136 193.809 243.556 1.00 4.23  ? 4187 HIS A C     1 
ATOM   19606 O O     . HIS A 1 4187 ? 191.079 193.964 242.329 1.00 11.56 ? 4187 HIS A O     1 
ATOM   19607 C CB    . HIS A 1 4187 ? 193.250 194.262 244.842 1.00 0.00  ? 4187 HIS A CB    1 
ATOM   19608 C CG    . HIS A 1 4187 ? 194.176 193.989 243.700 1.00 0.00  ? 4187 HIS A CG    1 
ATOM   19609 N ND1   . HIS A 1 4187 ? 194.836 194.991 243.023 1.00 0.00  ? 4187 HIS A ND1   1 
ATOM   19610 C CD2   . HIS A 1 4187 ? 194.587 192.826 243.143 1.00 0.82  ? 4187 HIS A CD2   1 
ATOM   19611 C CE1   . HIS A 1 4187 ? 195.597 194.458 242.085 1.00 0.00  ? 4187 HIS A CE1   1 
ATOM   19612 N NE2   . HIS A 1 4187 ? 195.466 193.146 242.138 1.00 0.10  ? 4187 HIS A NE2   1 
ATOM   19613 N N     . ALA A 1 4188 ? 190.534 192.791 244.174 1.00 5.97  ? 4188 ALA A N     1 
ATOM   19614 C CA    . ALA A 1 4188 ? 189.755 191.820 243.419 1.00 0.00  ? 4188 ALA A CA    1 
ATOM   19615 C C     . ALA A 1 4188 ? 188.536 192.465 242.777 1.00 1.80  ? 4188 ALA A C     1 
ATOM   19616 O O     . ALA A 1 4188 ? 188.208 192.170 241.626 1.00 8.66  ? 4188 ALA A O     1 
ATOM   19617 C CB    . ALA A 1 4188 ? 189.336 190.668 244.328 1.00 1.18  ? 4188 ALA A CB    1 
ATOM   19618 N N     . ILE A 1 4189 ? 187.849 193.347 243.505 1.00 6.82  ? 4189 ILE A N     1 
ATOM   19619 C CA    . ILE A 1 4189 ? 186.657 193.989 242.958 1.00 8.15  ? 4189 ILE A CA    1 
ATOM   19620 C C     . ILE A 1 4189 ? 187.023 194.840 241.749 1.00 1.39  ? 4189 ILE A C     1 
ATOM   19621 O O     . ILE A 1 4189 ? 186.369 194.778 240.701 1.00 6.36  ? 4189 ILE A O     1 
ATOM   19622 C CB    . ILE A 1 4189 ? 185.949 194.819 244.043 1.00 5.94  ? 4189 ILE A CB    1 
ATOM   19623 C CG1   . ILE A 1 4189 ? 185.261 193.899 245.054 1.00 9.46  ? 4189 ILE A CG1   1 
ATOM   19624 C CG2   . ILE A 1 4189 ? 184.949 195.778 243.422 1.00 5.94  ? 4189 ILE A CG2   1 
ATOM   19625 C CD1   . ILE A 1 4189 ? 184.003 193.250 244.546 1.00 9.22  ? 4189 ILE A CD1   1 
ATOM   19626 N N     . ILE A 1 4190 ? 188.094 195.630 241.866 1.00 2.57  ? 4190 ILE A N     1 
ATOM   19627 C CA    . ILE A 1 4190 ? 188.473 196.498 240.754 1.00 3.47  ? 4190 ILE A CA    1 
ATOM   19628 C C     . ILE A 1 4190 ? 189.090 195.742 239.590 1.00 6.90  ? 4190 ILE A C     1 
ATOM   19629 O O     . ILE A 1 4190 ? 189.062 196.248 238.463 1.00 15.84 ? 4190 ILE A O     1 
ATOM   19630 C CB    . ILE A 1 4190 ? 189.432 197.617 241.203 1.00 0.00  ? 4190 ILE A CB    1 
ATOM   19631 C CG1   . ILE A 1 4190 ? 190.781 197.050 241.628 1.00 0.00  ? 4190 ILE A CG1   1 
ATOM   19632 C CG2   . ILE A 1 4190 ? 188.813 198.416 242.332 1.00 0.54  ? 4190 ILE A CG2   1 
ATOM   19633 C CD1   . ILE A 1 4190 ? 191.819 198.108 241.853 1.00 0.00  ? 4190 ILE A CD1   1 
ATOM   19634 N N     . GLN A 1 4191 ? 189.649 194.550 239.815 1.00 5.50  ? 4191 GLN A N     1 
ATOM   19635 C CA    . GLN A 1 4191 ? 190.089 193.753 238.674 1.00 1.76  ? 4191 GLN A CA    1 
ATOM   19636 C C     . GLN A 1 4191 ? 188.957 192.983 238.004 1.00 3.28  ? 4191 GLN A C     1 
ATOM   19637 O O     . GLN A 1 4191 ? 188.974 192.813 236.781 1.00 5.33  ? 4191 GLN A O     1 
ATOM   19638 C CB    . GLN A 1 4191 ? 191.200 192.784 239.077 1.00 1.57  ? 4191 GLN A CB    1 
ATOM   19639 C CG    . GLN A 1 4191 ? 192.562 193.428 239.176 1.00 0.00  ? 4191 GLN A CG    1 
ATOM   19640 C CD    . GLN A 1 4191 ? 193.649 192.425 239.477 1.00 2.40  ? 4191 GLN A CD    1 
ATOM   19641 O OE1   . GLN A 1 4191 ? 193.375 191.261 239.761 1.00 6.31  ? 4191 GLN A OE1   1 
ATOM   19642 N NE2   . GLN A 1 4191 ? 194.895 192.856 239.360 1.00 6.16  ? 4191 GLN A NE2   1 
ATOM   19643 N N     . GLU A 1 4192 ? 187.974 192.500 238.766 1.00 1.69  ? 4192 GLU A N     1 
ATOM   19644 C CA    . GLU A 1 4192 ? 186.855 191.812 238.132 1.00 3.56  ? 4192 GLU A CA    1 
ATOM   19645 C C     . GLU A 1 4192 ? 185.879 192.792 237.500 1.00 5.58  ? 4192 GLU A C     1 
ATOM   19646 O O     . GLU A 1 4192 ? 185.063 192.394 236.662 1.00 9.74  ? 4192 GLU A O     1 
ATOM   19647 C CB    . GLU A 1 4192 ? 186.137 190.903 239.129 1.00 0.00  ? 4192 GLU A CB    1 
ATOM   19648 C CG    . GLU A 1 4192 ? 187.042 189.964 239.923 1.00 4.51  ? 4192 GLU A CG    1 
ATOM   19649 C CD    . GLU A 1 4192 ? 188.092 189.249 239.077 1.00 10.77 ? 4192 GLU A CD    1 
ATOM   19650 O OE1   . GLU A 1 4192 ? 189.186 188.970 239.608 1.00 7.75  ? 4192 GLU A OE1   1 
ATOM   19651 O OE2   . GLU A 1 4192 ? 187.818 188.930 237.900 1.00 12.89 ? 4192 GLU A OE2   1 
ATOM   19652 N N     . ARG A 1 4193 ? 185.937 194.070 237.881 1.00 3.30  ? 4193 ARG A N     1 
ATOM   19653 C CA    . ARG A 1 4193 ? 185.188 195.070 237.131 1.00 0.00  ? 4193 ARG A CA    1 
ATOM   19654 C C     . ARG A 1 4193 ? 185.847 195.403 235.802 1.00 0.00  ? 4193 ARG A C     1 
ATOM   19655 O O     . ARG A 1 4193 ? 185.180 195.938 234.912 1.00 0.44  ? 4193 ARG A O     1 
ATOM   19656 C CB    . ARG A 1 4193 ? 185.015 196.342 237.955 1.00 0.78  ? 4193 ARG A CB    1 
ATOM   19657 C CG    . ARG A 1 4193 ? 183.908 196.270 238.982 1.00 0.00  ? 4193 ARG A CG    1 
ATOM   19658 C CD    . ARG A 1 4193 ? 183.795 197.579 239.726 1.00 0.00  ? 4193 ARG A CD    1 
ATOM   19659 N NE    . ARG A 1 4193 ? 183.096 198.582 238.933 1.00 1.53  ? 4193 ARG A NE    1 
ATOM   19660 C CZ    . ARG A 1 4193 ? 181.846 198.966 239.146 1.00 0.00  ? 4193 ARG A CZ    1 
ATOM   19661 N NH1   . ARG A 1 4193 ? 181.134 198.477 240.146 1.00 0.00  ? 4193 ARG A NH1   1 
ATOM   19662 N NH2   . ARG A 1 4193 ? 181.296 199.862 238.333 1.00 0.00  ? 4193 ARG A NH2   1 
ATOM   19663 N N     . LEU A 1 4194 ? 187.138 195.103 235.647 1.00 0.00  ? 4194 LEU A N     1 
ATOM   19664 C CA    . LEU A 1 4194 ? 187.810 195.356 234.377 1.00 0.00  ? 4194 LEU A CA    1 
ATOM   19665 C C     . LEU A 1 4194 ? 187.273 194.461 233.271 1.00 4.85  ? 4194 LEU A C     1 
ATOM   19666 O O     . LEU A 1 4194 ? 187.366 194.813 232.090 1.00 5.13  ? 4194 LEU A O     1 
ATOM   19667 C CB    . LEU A 1 4194 ? 189.315 195.157 234.529 1.00 0.00  ? 4194 LEU A CB    1 
ATOM   19668 C CG    . LEU A 1 4194 ? 190.100 196.312 235.144 1.00 0.00  ? 4194 LEU A CG    1 
ATOM   19669 C CD1   . LEU A 1 4194 ? 191.561 195.936 235.285 1.00 0.00  ? 4194 LEU A CD1   1 
ATOM   19670 C CD2   . LEU A 1 4194 ? 189.946 197.569 234.310 1.00 2.73  ? 4194 LEU A CD2   1 
ATOM   19671 N N     . ARG A 1 4195 ? 186.721 193.301 233.629 1.00 10.21 ? 4195 ARG A N     1 
ATOM   19672 C CA    . ARG A 1 4195 ? 186.147 192.414 232.625 1.00 1.30  ? 4195 ARG A CA    1 
ATOM   19673 C C     . ARG A 1 4195 ? 184.909 193.034 231.991 1.00 0.00  ? 4195 ARG A C     1 
ATOM   19674 O O     . ARG A 1 4195 ? 184.635 192.820 230.805 1.00 0.67  ? 4195 ARG A O     1 
ATOM   19675 C CB    . ARG A 1 4195 ? 185.817 191.063 233.258 1.00 1.38  ? 4195 ARG A CB    1 
ATOM   19676 C CG    . ARG A 1 4195 ? 187.043 190.310 233.749 1.00 3.04  ? 4195 ARG A CG    1 
ATOM   19677 C CD    . ARG A 1 4195 ? 186.764 188.828 233.955 1.00 7.44  ? 4195 ARG A CD    1 
ATOM   19678 N NE    . ARG A 1 4195 ? 185.779 188.583 235.001 1.00 9.87  ? 4195 ARG A NE    1 
ATOM   19679 C CZ    . ARG A 1 4195 ? 184.541 188.161 234.781 1.00 11.36 ? 4195 ARG A CZ    1 
ATOM   19680 N NH1   . ARG A 1 4195 ? 184.100 187.918 233.558 1.00 6.76  ? 4195 ARG A NH1   1 
ATOM   19681 N NH2   . ARG A 1 4195 ? 183.726 187.977 235.815 1.00 10.81 ? 4195 ARG A NH2   1 
ATOM   19682 N N     . TYR A 1 4196 ? 184.146 193.797 232.769 1.00 0.00  ? 4196 TYR A N     1 
ATOM   19683 C CA    . TYR A 1 4196 ? 182.959 194.489 232.270 1.00 0.00  ? 4196 TYR A CA    1 
ATOM   19684 C C     . TYR A 1 4196 ? 183.319 195.920 231.865 1.00 0.32  ? 4196 TYR A C     1 
ATOM   19685 O O     . TYR A 1 4196 ? 182.693 196.891 232.284 1.00 7.53  ? 4196 TYR A O     1 
ATOM   19686 C CB    . TYR A 1 4196 ? 181.863 194.479 233.329 1.00 0.00  ? 4196 TYR A CB    1 
ATOM   19687 C CG    . TYR A 1 4196 ? 181.495 193.104 233.841 1.00 0.00  ? 4196 TYR A CG    1 
ATOM   19688 C CD1   . TYR A 1 4196 ? 182.267 192.474 234.808 1.00 1.77  ? 4196 TYR A CD1   1 
ATOM   19689 C CD2   . TYR A 1 4196 ? 180.376 192.441 233.366 1.00 5.18  ? 4196 TYR A CD2   1 
ATOM   19690 C CE1   . TYR A 1 4196 ? 181.938 191.224 235.281 1.00 3.48  ? 4196 TYR A CE1   1 
ATOM   19691 C CE2   . TYR A 1 4196 ? 180.037 191.189 233.835 1.00 4.33  ? 4196 TYR A CE2   1 
ATOM   19692 C CZ    . TYR A 1 4196 ? 180.822 190.586 234.793 1.00 4.59  ? 4196 TYR A CZ    1 
ATOM   19693 O OH    . TYR A 1 4196 ? 180.489 189.338 235.263 1.00 9.03  ? 4196 TYR A OH    1 
ATOM   19694 N N     . ALA A 1 4197 ? 184.342 196.029 231.019 1.00 0.59  ? 4197 ALA A N     1 
ATOM   19695 C CA    . ALA A 1 4197 ? 185.001 197.311 230.767 1.00 0.00  ? 4197 ALA A CA    1 
ATOM   19696 C C     . ALA A 1 4197 ? 184.067 198.425 230.304 1.00 4.03  ? 4197 ALA A C     1 
ATOM   19697 O O     . ALA A 1 4197 ? 184.212 199.554 230.798 1.00 19.71 ? 4197 ALA A O     1 
ATOM   19698 C CB    . ALA A 1 4197 ? 186.146 197.105 229.767 1.00 1.73  ? 4197 ALA A CB    1 
ATOM   19699 N N     . PRO A 1 4198 ? 183.123 198.212 229.369 1.00 4.42  ? 4198 PRO A N     1 
ATOM   19700 C CA    . PRO A 1 4198 ? 182.215 199.316 229.015 1.00 1.19  ? 4198 PRO A CA    1 
ATOM   19701 C C     . PRO A 1 4198 ? 181.442 199.840 230.216 1.00 5.41  ? 4198 PRO A C     1 
ATOM   19702 O O     . PRO A 1 4198 ? 181.499 201.033 230.527 1.00 7.62  ? 4198 PRO A O     1 
ATOM   19703 C CB    . PRO A 1 4198 ? 181.266 198.701 227.976 1.00 4.93  ? 4198 PRO A CB    1 
ATOM   19704 C CG    . PRO A 1 4198 ? 181.720 197.320 227.733 1.00 9.26  ? 4198 PRO A CG    1 
ATOM   19705 C CD    . PRO A 1 4198 ? 182.986 197.060 228.461 1.00 7.12  ? 4198 PRO A CD    1 
ATOM   19706 N N     . LEU A 1 4199 ? 180.728 198.952 230.908 1.00 0.59  ? 4199 LEU A N     1 
ATOM   19707 C CA    . LEU A 1 4199 ? 179.857 199.365 232.000 1.00 0.00  ? 4199 LEU A CA    1 
ATOM   19708 C C     . LEU A 1 4199 ? 180.583 199.453 233.337 1.00 2.89  ? 4199 LEU A C     1 
ATOM   19709 O O     . LEU A 1 4199 ? 180.038 200.024 234.287 1.00 7.77  ? 4199 LEU A O     1 
ATOM   19710 C CB    . LEU A 1 4199 ? 178.674 198.399 232.099 1.00 0.43  ? 4199 LEU A CB    1 
ATOM   19711 C CG    . LEU A 1 4199 ? 177.587 198.644 233.143 1.00 3.71  ? 4199 LEU A CG    1 
ATOM   19712 C CD1   . LEU A 1 4199 ? 176.578 199.652 232.624 1.00 8.27  ? 4199 LEU A CD1   1 
ATOM   19713 C CD2   . LEU A 1 4199 ? 176.911 197.341 233.503 1.00 3.21  ? 4199 LEU A CD2   1 
ATOM   19714 N N     . GLY A 1 4200 ? 181.811 198.952 233.422 1.00 0.88  ? 4200 GLY A N     1 
ATOM   19715 C CA    . GLY A 1 4200 ? 182.546 198.977 234.671 1.00 0.00  ? 4200 GLY A CA    1 
ATOM   19716 C C     . GLY A 1 4200 ? 183.400 200.222 234.735 1.00 6.48  ? 4200 GLY A C     1 
ATOM   19717 O O     . GLY A 1 4200 ? 182.877 201.315 234.974 1.00 25.05 ? 4200 GLY A O     1 
ATOM   19718 N N     . TRP A 1 4201 ? 184.706 200.091 234.532 1.00 0.00  ? 4201 TRP A N     1 
ATOM   19719 C CA    . TRP A 1 4201 ? 185.568 201.250 234.353 1.00 2.90  ? 4201 TRP A CA    1 
ATOM   19720 C C     . TRP A 1 4201 ? 185.864 201.442 232.874 1.00 6.55  ? 4201 TRP A C     1 
ATOM   19721 O O     . TRP A 1 4201 ? 186.328 200.515 232.203 1.00 14.40 ? 4201 TRP A O     1 
ATOM   19722 C CB    . TRP A 1 4201 ? 186.852 201.127 235.171 1.00 4.30  ? 4201 TRP A CB    1 
ATOM   19723 C CG    . TRP A 1 4201 ? 186.570 201.236 236.633 1.00 12.90 ? 4201 TRP A CG    1 
ATOM   19724 C CD1   . TRP A 1 4201 ? 185.356 201.467 237.206 1.00 13.70 ? 4201 TRP A CD1   1 
ATOM   19725 C CD2   . TRP A 1 4201 ? 187.515 201.198 237.707 1.00 10.69 ? 4201 TRP A CD2   1 
ATOM   19726 N NE1   . TRP A 1 4201 ? 185.479 201.534 238.567 1.00 9.09  ? 4201 TRP A NE1   1 
ATOM   19727 C CE2   . TRP A 1 4201 ? 186.795 201.377 238.902 1.00 6.62  ? 4201 TRP A CE2   1 
ATOM   19728 C CE3   . TRP A 1 4201 ? 188.895 201.013 237.777 1.00 10.58 ? 4201 TRP A CE3   1 
ATOM   19729 C CZ2   . TRP A 1 4201 ? 187.404 201.376 240.147 1.00 6.97  ? 4201 TRP A CZ2   1 
ATOM   19730 C CZ3   . TRP A 1 4201 ? 189.495 201.016 239.018 1.00 13.55 ? 4201 TRP A CZ3   1 
ATOM   19731 C CH2   . TRP A 1 4201 ? 188.753 201.194 240.183 1.00 10.41 ? 4201 TRP A CH2   1 
ATOM   19732 N N     . SER A 1 4202 ? 185.612 202.661 232.390 1.00 6.44  ? 4202 SER A N     1 
ATOM   19733 C CA    . SER A 1 4202 ? 185.505 203.013 230.977 1.00 8.62  ? 4202 SER A CA    1 
ATOM   19734 C C     . SER A 1 4202 ? 186.538 202.343 230.081 1.00 7.56  ? 4202 SER A C     1 
ATOM   19735 O O     . SER A 1 4202 ? 186.215 201.933 228.962 1.00 18.45 ? 4202 SER A O     1 
ATOM   19736 C CB    . SER A 1 4202 ? 185.607 204.530 230.818 1.00 13.95 ? 4202 SER A CB    1 
ATOM   19737 O OG    . SER A 1 4202 ? 186.959 204.950 230.858 1.00 18.74 ? 4202 SER A OG    1 
ATOM   19738 N N     . LYS A 1 4203 ? 187.774 202.227 230.548 1.00 0.00  ? 4203 LYS A N     1 
ATOM   19739 C CA    . LYS A 1 4203 ? 188.831 201.610 229.767 1.00 0.00  ? 4203 LYS A CA    1 
ATOM   19740 C C     . LYS A 1 4203 ? 189.601 200.615 230.621 1.00 0.65  ? 4203 LYS A C     1 
ATOM   19741 O O     . LYS A 1 4203 ? 189.513 200.627 231.851 1.00 11.07 ? 4203 LYS A O     1 
ATOM   19742 C CB    . LYS A 1 4203 ? 189.775 202.663 229.181 1.00 5.46  ? 4203 LYS A CB    1 
ATOM   19743 C CG    . LYS A 1 4203 ? 190.869 203.131 230.111 1.00 1.72  ? 4203 LYS A CG    1 
ATOM   19744 C CD    . LYS A 1 4203 ? 191.841 204.021 229.361 1.00 1.76  ? 4203 LYS A CD    1 
ATOM   19745 C CE    . LYS A 1 4203 ? 191.427 205.478 229.446 1.00 6.77  ? 4203 LYS A CE    1 
ATOM   19746 N NZ    . LYS A 1 4203 ? 192.453 206.385 228.861 1.00 9.21  ? 4203 LYS A NZ    1 
ATOM   19747 N N     . LYS A 1 4204 ? 190.347 199.743 229.952 1.00 0.00  ? 4204 LYS A N     1 
ATOM   19748 C CA    . LYS A 1 4204 ? 191.033 198.635 230.610 1.00 0.00  ? 4204 LYS A CA    1 
ATOM   19749 C C     . LYS A 1 4204 ? 192.316 199.156 231.241 1.00 0.29  ? 4204 LYS A C     1 
ATOM   19750 O O     . LYS A 1 4204 ? 193.352 199.259 230.580 1.00 0.91  ? 4204 LYS A O     1 
ATOM   19751 C CB    . LYS A 1 4204 ? 191.323 197.522 229.610 1.00 1.52  ? 4204 LYS A CB    1 
ATOM   19752 C CG    . LYS A 1 4204 ? 191.478 196.147 230.230 1.00 10.71 ? 4204 LYS A CG    1 
ATOM   19753 C CD    . LYS A 1 4204 ? 190.126 195.491 230.457 1.00 9.85  ? 4204 LYS A CD    1 
ATOM   19754 C CE    . LYS A 1 4204 ? 189.379 195.305 229.146 1.00 4.13  ? 4204 LYS A CE    1 
ATOM   19755 N NZ    . LYS A 1 4204 ? 188.131 194.510 229.317 1.00 0.00  ? 4204 LYS A NZ    1 
ATOM   19756 N N     . TYR A 1 4205 ? 192.252 199.489 232.525 1.00 1.12  ? 4205 TYR A N     1 
ATOM   19757 C CA    . TYR A 1 4205 ? 193.433 199.912 233.258 1.00 0.00  ? 4205 TYR A CA    1 
ATOM   19758 C C     . TYR A 1 4205 ? 194.296 198.712 233.622 1.00 1.91  ? 4205 TYR A C     1 
ATOM   19759 O O     . TYR A 1 4205 ? 193.810 197.586 233.751 1.00 3.11  ? 4205 TYR A O     1 
ATOM   19760 C CB    . TYR A 1 4205 ? 193.040 200.671 234.524 1.00 0.00  ? 4205 TYR A CB    1 
ATOM   19761 C CG    . TYR A 1 4205 ? 192.163 201.873 234.279 1.00 0.00  ? 4205 TYR A CG    1 
ATOM   19762 C CD1   . TYR A 1 4205 ? 192.639 202.968 233.576 1.00 0.00  ? 4205 TYR A CD1   1 
ATOM   19763 C CD2   . TYR A 1 4205 ? 190.860 201.916 234.752 1.00 0.00  ? 4205 TYR A CD2   1 
ATOM   19764 C CE1   . TYR A 1 4205 ? 191.847 204.069 233.352 1.00 0.00  ? 4205 TYR A CE1   1 
ATOM   19765 C CE2   . TYR A 1 4205 ? 190.059 203.014 234.530 1.00 0.00  ? 4205 TYR A CE2   1 
ATOM   19766 C CZ    . TYR A 1 4205 ? 190.558 204.087 233.827 1.00 0.86  ? 4205 TYR A CZ    1 
ATOM   19767 O OH    . TYR A 1 4205 ? 189.767 205.187 233.602 1.00 0.71  ? 4205 TYR A OH    1 
ATOM   19768 N N     . GLU A 1 4206 ? 195.591 198.962 233.778 1.00 2.22  ? 4206 GLU A N     1 
ATOM   19769 C CA    . GLU A 1 4206 ? 196.539 197.928 234.175 1.00 0.99  ? 4206 GLU A CA    1 
ATOM   19770 C C     . GLU A 1 4206 ? 196.708 197.985 235.687 1.00 1.56  ? 4206 GLU A C     1 
ATOM   19771 O O     . GLU A 1 4206 ? 197.334 198.907 236.215 1.00 2.67  ? 4206 GLU A O     1 
ATOM   19772 C CB    . GLU A 1 4206 ? 197.874 198.111 233.460 1.00 2.51  ? 4206 GLU A CB    1 
ATOM   19773 C CG    . GLU A 1 4206 ? 197.750 198.237 231.954 1.00 4.87  ? 4206 GLU A CG    1 
ATOM   19774 C CD    . GLU A 1 4206 ? 199.092 198.232 231.259 1.00 8.78  ? 4206 GLU A CD    1 
ATOM   19775 O OE1   . GLU A 1 4206 ? 200.124 198.229 231.961 1.00 10.48 ? 4206 GLU A OE1   1 
ATOM   19776 O OE2   . GLU A 1 4206 ? 199.117 198.229 230.011 1.00 12.98 ? 4206 GLU A OE2   1 
ATOM   19777 N N     . PHE A 1 4207 ? 196.168 196.989 236.379 1.00 0.00  ? 4207 PHE A N     1 
ATOM   19778 C CA    . PHE A 1 4207 ? 196.134 196.938 237.836 1.00 0.00  ? 4207 PHE A CA    1 
ATOM   19779 C C     . PHE A 1 4207 ? 196.777 195.656 238.333 1.00 1.52  ? 4207 PHE A C     1 
ATOM   19780 O O     . PHE A 1 4207 ? 196.220 194.921 239.149 1.00 14.53 ? 4207 PHE A O     1 
ATOM   19781 C CB    . PHE A 1 4207 ? 194.701 197.068 238.333 1.00 0.00  ? 4207 PHE A CB    1 
ATOM   19782 C CG    . PHE A 1 4207 ? 194.176 198.466 238.286 1.00 0.00  ? 4207 PHE A CG    1 
ATOM   19783 C CD1   . PHE A 1 4207 ? 192.822 198.708 238.286 1.00 0.46  ? 4207 PHE A CD1   1 
ATOM   19784 C CD2   . PHE A 1 4207 ? 195.042 199.543 238.265 1.00 6.91  ? 4207 PHE A CD2   1 
ATOM   19785 C CE1   . PHE A 1 4207 ? 192.344 199.993 238.241 1.00 0.00  ? 4207 PHE A CE1   1 
ATOM   19786 C CE2   . PHE A 1 4207 ? 194.565 200.832 238.228 1.00 3.49  ? 4207 PHE A CE2   1 
ATOM   19787 C CZ    . PHE A 1 4207 ? 193.212 201.057 238.219 1.00 1.00  ? 4207 PHE A CZ    1 
ATOM   19788 N N     . GLY A 1 4208 ? 197.972 195.368 237.829 1.00 4.87  ? 4208 GLY A N     1 
ATOM   19789 C CA    . GLY A 1 4208 ? 198.659 194.139 238.165 1.00 8.38  ? 4208 GLY A CA    1 
ATOM   19790 C C     . GLY A 1 4208 ? 199.175 194.081 239.586 1.00 1.67  ? 4208 GLY A C     1 
ATOM   19791 O O     . GLY A 1 4208 ? 198.690 194.793 240.467 1.00 0.00  ? 4208 GLY A O     1 
ATOM   19792 N N     . GLU A 1 4209 ? 200.169 193.222 239.816 1.00 5.15  ? 4209 GLU A N     1 
ATOM   19793 C CA    . GLU A 1 4209 ? 200.704 193.041 241.158 1.00 0.00  ? 4209 GLU A CA    1 
ATOM   19794 C C     . GLU A 1 4209 ? 201.448 194.269 241.663 1.00 1.18  ? 4209 GLU A C     1 
ATOM   19795 O O     . GLU A 1 4209 ? 201.633 194.400 242.875 1.00 5.11  ? 4209 GLU A O     1 
ATOM   19796 C CB    . GLU A 1 4209 ? 201.631 191.824 241.195 1.00 3.56  ? 4209 GLU A CB    1 
ATOM   19797 C CG    . GLU A 1 4209 ? 203.039 192.094 240.691 1.00 6.59  ? 4209 GLU A CG    1 
ATOM   19798 C CD    . GLU A 1 4209 ? 203.106 192.224 239.182 1.00 8.88  ? 4209 GLU A CD    1 
ATOM   19799 O OE1   . GLU A 1 4209 ? 203.971 192.975 238.685 1.00 7.76  ? 4209 GLU A OE1   1 
ATOM   19800 O OE2   . GLU A 1 4209 ? 202.296 191.571 238.492 1.00 10.12 ? 4209 GLU A OE2   1 
ATOM   19801 N N     . SER A 1 4210 ? 201.885 195.163 240.772 1.00 7.92  ? 4210 SER A N     1 
ATOM   19802 C CA    . SER A 1 4210 ? 202.647 196.329 241.210 1.00 6.73  ? 4210 SER A CA    1 
ATOM   19803 C C     . SER A 1 4210 ? 201.801 197.252 242.076 1.00 5.15  ? 4210 SER A C     1 
ATOM   19804 O O     . SER A 1 4210 ? 202.265 197.747 243.110 1.00 17.28 ? 4210 SER A O     1 
ATOM   19805 C CB    . SER A 1 4210 ? 203.193 197.084 240.000 1.00 12.07 ? 4210 SER A CB    1 
ATOM   19806 O OG    . SER A 1 4210 ? 202.167 197.326 239.053 1.00 17.95 ? 4210 SER A OG    1 
ATOM   19807 N N     . ASP A 1 4211 ? 200.553 197.494 241.671 1.00 4.98  ? 4211 ASP A N     1 
ATOM   19808 C CA    . ASP A 1 4211 ? 199.673 198.345 242.463 1.00 0.43  ? 4211 ASP A CA    1 
ATOM   19809 C C     . ASP A 1 4211 ? 199.369 197.719 243.816 1.00 0.17  ? 4211 ASP A C     1 
ATOM   19810 O O     . ASP A 1 4211 ? 199.321 198.418 244.833 1.00 6.86  ? 4211 ASP A O     1 
ATOM   19811 C CB    . ASP A 1 4211 ? 198.382 198.622 241.698 1.00 0.72  ? 4211 ASP A CB    1 
ATOM   19812 C CG    . ASP A 1 4211 ? 198.616 199.427 240.443 1.00 4.28  ? 4211 ASP A CG    1 
ATOM   19813 O OD1   . ASP A 1 4211 ? 199.518 200.289 240.451 1.00 11.74 ? 4211 ASP A OD1   1 
ATOM   19814 O OD2   . ASP A 1 4211 ? 197.898 199.204 239.450 1.00 6.67  ? 4211 ASP A OD2   1 
ATOM   19815 N N     . LEU A 1 4212 ? 199.149 196.404 243.847 1.00 0.00  ? 4212 LEU A N     1 
ATOM   19816 C CA    . LEU A 1 4212 ? 198.884 195.733 245.115 1.00 0.00  ? 4212 LEU A CA    1 
ATOM   19817 C C     . LEU A 1 4212 ? 200.105 195.772 246.026 1.00 2.89  ? 4212 LEU A C     1 
ATOM   19818 O O     . LEU A 1 4212 ? 199.972 195.949 247.241 1.00 6.66  ? 4212 LEU A O     1 
ATOM   19819 C CB    . LEU A 1 4212 ? 198.438 194.294 244.862 1.00 1.29  ? 4212 LEU A CB    1 
ATOM   19820 C CG    . LEU A 1 4212 ? 198.003 193.481 246.080 1.00 2.42  ? 4212 LEU A CG    1 
ATOM   19821 C CD1   . LEU A 1 4212 ? 196.703 194.018 246.649 1.00 0.00  ? 4212 LEU A CD1   1 
ATOM   19822 C CD2   . LEU A 1 4212 ? 197.855 192.024 245.703 1.00 3.08  ? 4212 LEU A CD2   1 
ATOM   19823 N N     . ARG A 1 4213 ? 201.302 195.612 245.459 1.00 0.95  ? 4213 ARG A N     1 
ATOM   19824 C CA    . ARG A 1 4213 ? 202.518 195.742 246.255 1.00 1.24  ? 4213 ARG A CA    1 
ATOM   19825 C C     . ARG A 1 4213 ? 202.661 197.149 246.815 1.00 0.00  ? 4213 ARG A C     1 
ATOM   19826 O O     . ARG A 1 4213 ? 203.039 197.325 247.978 1.00 0.55  ? 4213 ARG A O     1 
ATOM   19827 C CB    . ARG A 1 4213 ? 203.745 195.376 245.419 1.00 2.05  ? 4213 ARG A CB    1 
ATOM   19828 C CG    . ARG A 1 4213 ? 203.845 193.912 245.010 1.00 2.43  ? 4213 ARG A CG    1 
ATOM   19829 C CD    . ARG A 1 4213 ? 203.892 192.977 246.212 1.00 4.55  ? 4213 ARG A CD    1 
ATOM   19830 N NE    . ARG A 1 4213 ? 202.567 192.522 246.619 1.00 6.52  ? 4213 ARG A NE    1 
ATOM   19831 C CZ    . ARG A 1 4213 ? 202.059 191.335 246.318 1.00 7.46  ? 4213 ARG A CZ    1 
ATOM   19832 N NH1   . ARG A 1 4213 ? 202.741 190.451 245.607 1.00 5.97  ? 4213 ARG A NH1   1 
ATOM   19833 N NH2   . ARG A 1 4213 ? 200.837 191.027 246.740 1.00 4.74  ? 4213 ARG A NH2   1 
ATOM   19834 N N     . SER A 1 4214 ? 202.372 198.165 246.001 1.00 0.00  ? 4214 SER A N     1 
ATOM   19835 C CA    . SER A 1 4214 ? 202.472 199.540 246.478 1.00 0.00  ? 4214 SER A CA    1 
ATOM   19836 C C     . SER A 1 4214 ? 201.456 199.821 247.578 1.00 0.27  ? 4214 SER A C     1 
ATOM   19837 O O     . SER A 1 4214 ? 201.769 200.498 248.563 1.00 8.95  ? 4214 SER A O     1 
ATOM   19838 C CB    . SER A 1 4214 ? 202.293 200.513 245.315 1.00 4.33  ? 4214 SER A CB    1 
ATOM   19839 O OG    . SER A 1 4214 ? 203.448 200.536 244.497 1.00 7.84  ? 4214 SER A OG    1 
ATOM   19840 N N     . ALA A 1 4215 ? 200.232 199.312 247.428 1.00 0.25  ? 4215 ALA A N     1 
ATOM   19841 C CA    . ALA A 1 4215 ? 199.218 199.494 248.462 1.00 0.00  ? 4215 ALA A CA    1 
ATOM   19842 C C     . ALA A 1 4215 ? 199.602 198.774 249.746 1.00 1.99  ? 4215 ALA A C     1 
ATOM   19843 O O     . ALA A 1 4215 ? 199.388 199.294 250.848 1.00 4.65  ? 4215 ALA A O     1 
ATOM   19844 C CB    . ALA A 1 4215 ? 197.863 199.012 247.954 1.00 0.00  ? 4215 ALA A CB    1 
ATOM   19845 N N     . CYS A 1 4216 ? 200.171 197.573 249.625 1.00 0.00  ? 4216 CYS A N     1 
ATOM   19846 C CA    . CYS A 1 4216 ? 200.633 196.845 250.800 1.00 0.00  ? 4216 CYS A CA    1 
ATOM   19847 C C     . CYS A 1 4216 ? 201.765 197.587 251.497 1.00 0.00  ? 4216 CYS A C     1 
ATOM   19848 O O     . CYS A 1 4216 ? 201.805 197.652 252.729 1.00 1.14  ? 4216 CYS A O     1 
ATOM   19849 C CB    . CYS A 1 4216 ? 201.077 195.441 250.396 1.00 5.27  ? 4216 CYS A CB    1 
ATOM   19850 S SG    . CYS A 1 4216 ? 199.728 194.269 250.140 1.00 17.86 ? 4216 CYS A SG    1 
ATOM   19851 N N     . ASP A 1 4217 ? 202.695 198.152 250.724 1.00 0.74  ? 4217 ASP A N     1 
ATOM   19852 C CA    . ASP A 1 4217 ? 203.768 198.951 251.309 1.00 0.00  ? 4217 ASP A CA    1 
ATOM   19853 C C     . ASP A 1 4217 ? 203.216 200.184 252.011 1.00 0.00  ? 4217 ASP A C     1 
ATOM   19854 O O     . ASP A 1 4217 ? 203.688 200.555 253.092 1.00 9.36  ? 4217 ASP A O     1 
ATOM   19855 C CB    . ASP A 1 4217 ? 204.769 199.360 250.230 1.00 0.00  ? 4217 ASP A CB    1 
ATOM   19856 C CG    . ASP A 1 4217 ? 205.477 198.175 249.612 1.00 3.94  ? 4217 ASP A CG    1 
ATOM   19857 O OD1   . ASP A 1 4217 ? 205.260 197.039 250.081 1.00 10.47 ? 4217 ASP A OD1   1 
ATOM   19858 O OD2   . ASP A 1 4217 ? 206.251 198.377 248.654 1.00 9.05  ? 4217 ASP A OD2   1 
ATOM   19859 N N     . THR A 1 4218 ? 202.229 200.841 251.402 1.00 0.00  ? 4218 THR A N     1 
ATOM   19860 C CA    . THR A 1 4218 ? 201.605 202.001 252.029 1.00 0.00  ? 4218 THR A CA    1 
ATOM   19861 C C     . THR A 1 4218 ? 200.970 201.624 253.360 1.00 1.07  ? 4218 THR A C     1 
ATOM   19862 O O     . THR A 1 4218 ? 201.159 202.311 254.372 1.00 8.09  ? 4218 THR A O     1 
ATOM   19863 C CB    . THR A 1 4218 ? 200.561 202.603 251.087 1.00 0.00  ? 4218 THR A CB    1 
ATOM   19864 O OG1   . THR A 1 4218 ? 201.211 203.139 249.928 1.00 4.53  ? 4218 THR A OG1   1 
ATOM   19865 C CG2   . THR A 1 4218 ? 199.775 203.702 251.780 1.00 0.00  ? 4218 THR A CG2   1 
ATOM   19866 N N     . VAL A 1 4219 ? 200.217 200.521 253.379 1.00 0.00  ? 4219 VAL A N     1 
ATOM   19867 C CA    . VAL A 1 4219 ? 199.580 200.079 254.616 1.00 0.00  ? 4219 VAL A CA    1 
ATOM   19868 C C     . VAL A 1 4219 ? 200.631 199.727 255.661 1.00 1.82  ? 4219 VAL A C     1 
ATOM   19869 O O     . VAL A 1 4219 ? 200.499 200.084 256.837 1.00 9.95  ? 4219 VAL A O     1 
ATOM   19870 C CB    . VAL A 1 4219 ? 198.629 198.900 254.338 1.00 0.00  ? 4219 VAL A CB    1 
ATOM   19871 C CG1   . VAL A 1 4219 ? 198.104 198.319 255.638 1.00 0.96  ? 4219 VAL A CG1   1 
ATOM   19872 C CG2   . VAL A 1 4219 ? 197.473 199.354 253.463 1.00 0.00  ? 4219 VAL A CG2   1 
ATOM   19873 N N     . ASP A 1 4220 ? 201.697 199.035 255.249 1.00 5.39  ? 4220 ASP A N     1 
ATOM   19874 C CA    . ASP A 1 4220 ? 202.765 198.689 256.181 1.00 1.55  ? 4220 ASP A CA    1 
ATOM   19875 C C     . ASP A 1 4220 ? 203.364 199.936 256.813 1.00 1.21  ? 4220 ASP A C     1 
ATOM   19876 O O     . ASP A 1 4220 ? 203.460 200.038 258.041 1.00 5.65  ? 4220 ASP A O     1 
ATOM   19877 C CB    . ASP A 1 4220 ? 203.856 197.889 255.467 1.00 1.25  ? 4220 ASP A CB    1 
ATOM   19878 C CG    . ASP A 1 4220 ? 203.465 196.447 255.230 1.00 9.26  ? 4220 ASP A CG    1 
ATOM   19879 O OD1   . ASP A 1 4220 ? 202.674 195.902 256.025 1.00 11.63 ? 4220 ASP A OD1   1 
ATOM   19880 O OD2   . ASP A 1 4220 ? 203.959 195.854 254.248 1.00 11.39 ? 4220 ASP A OD2   1 
ATOM   19881 N N     . THR A 1 4221 ? 203.765 200.903 255.985 1.00 0.00  ? 4221 THR A N     1 
ATOM   19882 C CA    . THR A 1 4221 ? 204.419 202.098 256.507 1.00 2.76  ? 4221 THR A CA    1 
ATOM   19883 C C     . THR A 1 4221 ? 203.484 202.896 257.405 1.00 1.65  ? 4221 THR A C     1 
ATOM   19884 O O     . THR A 1 4221 ? 203.897 203.383 258.463 1.00 12.63 ? 4221 THR A O     1 
ATOM   19885 C CB    . THR A 1 4221 ? 204.927 202.973 255.361 1.00 2.41  ? 4221 THR A CB    1 
ATOM   19886 O OG1   . THR A 1 4221 ? 203.843 203.289 254.482 1.00 4.40  ? 4221 THR A OG1   1 
ATOM   19887 C CG2   . THR A 1 4221 ? 206.011 202.251 254.581 1.00 1.54  ? 4221 THR A CG2   1 
ATOM   19888 N N     . TRP A 1 4222 ? 202.218 203.034 257.013 1.00 0.00  ? 4222 TRP A N     1 
ATOM   19889 C CA    . TRP A 1 4222 ? 201.324 203.885 257.787 1.00 0.00  ? 4222 TRP A CA    1 
ATOM   19890 C C     . TRP A 1 4222 ? 200.852 203.219 259.073 1.00 0.60  ? 4222 TRP A C     1 
ATOM   19891 O O     . TRP A 1 4222 ? 200.608 203.914 260.064 1.00 8.07  ? 4222 TRP A O     1 
ATOM   19892 C CB    . TRP A 1 4222 ? 200.151 204.325 256.914 1.00 0.00  ? 4222 TRP A CB    1 
ATOM   19893 C CG    . TRP A 1 4222 ? 200.547 205.478 256.053 1.00 0.91  ? 4222 TRP A CG    1 
ATOM   19894 C CD1   . TRP A 1 4222 ? 201.048 205.419 254.788 1.00 0.51  ? 4222 TRP A CD1   1 
ATOM   19895 C CD2   . TRP A 1 4222 ? 200.514 206.864 256.407 1.00 5.63  ? 4222 TRP A CD2   1 
ATOM   19896 N NE1   . TRP A 1 4222 ? 201.323 206.682 254.328 1.00 1.62  ? 4222 TRP A NE1   1 
ATOM   19897 C CE2   . TRP A 1 4222 ? 200.999 207.589 255.303 1.00 3.92  ? 4222 TRP A CE2   1 
ATOM   19898 C CE3   . TRP A 1 4222 ? 200.113 207.564 257.549 1.00 4.27  ? 4222 TRP A CE3   1 
ATOM   19899 C CZ2   . TRP A 1 4222 ? 201.094 208.977 255.305 1.00 4.79  ? 4222 TRP A CZ2   1 
ATOM   19900 C CZ3   . TRP A 1 4222 ? 200.208 208.941 257.549 1.00 4.67  ? 4222 TRP A CZ3   1 
ATOM   19901 C CH2   . TRP A 1 4222 ? 200.695 209.633 256.435 1.00 3.92  ? 4222 TRP A CH2   1 
ATOM   19902 N N     . LEU A 1 4223 ? 200.744 201.888 259.099 1.00 1.88  ? 4223 LEU A N     1 
ATOM   19903 C CA    . LEU A 1 4223 ? 200.457 201.212 260.360 1.00 3.58  ? 4223 LEU A CA    1 
ATOM   19904 C C     . LEU A 1 4223 ? 201.682 201.160 261.261 1.00 9.17  ? 4223 LEU A C     1 
ATOM   19905 O O     . LEU A 1 4223 ? 201.543 201.157 262.488 1.00 10.43 ? 4223 LEU A O     1 
ATOM   19906 C CB    . LEU A 1 4223 ? 199.917 199.805 260.103 1.00 0.00  ? 4223 LEU A CB    1 
ATOM   19907 C CG    . LEU A 1 4223 ? 198.411 199.679 259.862 1.00 3.97  ? 4223 LEU A CG    1 
ATOM   19908 C CD1   . LEU A 1 4223 ? 197.648 200.069 261.115 1.00 8.49  ? 4223 LEU A CD1   1 
ATOM   19909 C CD2   . LEU A 1 4223 ? 197.957 200.535 258.686 1.00 5.74  ? 4223 LEU A CD2   1 
ATOM   19910 N N     . ASP A 1 4224 ? 202.884 201.113 260.683 1.00 7.59  ? 4224 ASP A N     1 
ATOM   19911 C CA    . ASP A 1 4224 ? 204.087 201.238 261.496 1.00 4.61  ? 4224 ASP A CA    1 
ATOM   19912 C C     . ASP A 1 4224 ? 204.178 202.622 262.123 1.00 8.60  ? 4224 ASP A C     1 
ATOM   19913 O O     . ASP A 1 4224 ? 204.526 202.758 263.301 1.00 14.03 ? 4224 ASP A O     1 
ATOM   19914 C CB    . ASP A 1 4224 ? 205.325 200.954 260.646 1.00 5.69  ? 4224 ASP A CB    1 
ATOM   19915 C CG    . ASP A 1 4224 ? 205.438 199.498 260.250 1.00 9.14  ? 4224 ASP A CG    1 
ATOM   19916 O OD1   . ASP A 1 4224 ? 204.598 198.692 260.702 1.00 11.11 ? 4224 ASP A OD1   1 
ATOM   19917 O OD2   . ASP A 1 4224 ? 206.362 199.160 259.482 1.00 5.81  ? 4224 ASP A OD2   1 
ATOM   19918 N N     . ASP A 1 4225 ? 203.865 203.661 261.348 1.00 6.65  ? 4225 ASP A N     1 
ATOM   19919 C CA    . ASP A 1 4225 ? 203.968 205.026 261.853 1.00 6.48  ? 4225 ASP A CA    1 
ATOM   19920 C C     . ASP A 1 4225 ? 202.888 205.316 262.887 1.00 12.32 ? 4225 ASP A C     1 
ATOM   19921 O O     . ASP A 1 4225 ? 203.170 205.879 263.950 1.00 18.97 ? 4225 ASP A O     1 
ATOM   19922 C CB    . ASP A 1 4225 ? 203.887 206.017 260.692 1.00 7.41  ? 4225 ASP A CB    1 
ATOM   19923 C CG    . ASP A 1 4225 ? 205.172 206.081 259.891 1.00 12.26 ? 4225 ASP A CG    1 
ATOM   19924 O OD1   . ASP A 1 4225 ? 206.044 205.208 260.094 1.00 13.56 ? 4225 ASP A OD1   1 
ATOM   19925 O OD2   . ASP A 1 4225 ? 205.311 207.001 259.058 1.00 9.45  ? 4225 ASP A OD2   1 
ATOM   19926 N N     . THR A 1 4226 ? 201.641 204.944 262.592 1.00 11.71 ? 4226 THR A N     1 
ATOM   19927 C CA    . THR A 1 4226 ? 200.551 205.225 263.520 1.00 10.32 ? 4226 THR A CA    1 
ATOM   19928 C C     . THR A 1 4226 ? 200.654 204.359 264.768 1.00 9.75  ? 4226 THR A C     1 
ATOM   19929 O O     . THR A 1 4226 ? 200.511 204.852 265.893 1.00 12.86 ? 4226 THR A O     1 
ATOM   19930 C CB    . THR A 1 4226 ? 199.208 205.013 262.825 1.00 11.00 ? 4226 THR A CB    1 
ATOM   19931 O OG1   . THR A 1 4226 ? 199.032 206.014 261.815 1.00 12.04 ? 4226 THR A OG1   1 
ATOM   19932 C CG2   . THR A 1 4226 ? 198.072 205.107 263.825 1.00 14.57 ? 4226 THR A CG2   1 
ATOM   19933 N N     . ALA A 1 4227 ? 200.913 203.069 264.591 1.00 12.37 ? 4227 ALA A N     1 
ATOM   19934 C CA    . ALA A 1 4227 ? 201.031 202.119 265.693 1.00 20.50 ? 4227 ALA A CA    1 
ATOM   19935 C C     . ALA A 1 4227 ? 202.506 201.755 265.840 1.00 22.48 ? 4227 ALA A C     1 
ATOM   19936 O O     . ALA A 1 4227 ? 202.981 200.775 265.266 1.00 22.71 ? 4227 ALA A O     1 
ATOM   19937 C CB    . ALA A 1 4227 ? 200.176 200.891 265.443 1.00 16.76 ? 4227 ALA A CB    1 
ATOM   19938 N N     . LYS A 1 4228 ? 203.227 202.560 266.621 1.00 21.12 ? 4228 LYS A N     1 
ATOM   19939 C CA    . LYS A 1 4228 ? 204.654 202.326 266.813 1.00 21.09 ? 4228 LYS A CA    1 
ATOM   19940 C C     . LYS A 1 4228 ? 204.906 201.007 267.530 1.00 21.10 ? 4228 LYS A C     1 
ATOM   19941 O O     . LYS A 1 4228 ? 205.840 200.274 267.185 1.00 21.05 ? 4228 LYS A O     1 
ATOM   19942 C CB    . LYS A 1 4228 ? 205.269 203.493 267.583 1.00 23.35 ? 4228 LYS A CB    1 
ATOM   19943 C CG    . LYS A 1 4228 ? 204.980 204.849 266.958 1.00 20.31 ? 4228 LYS A CG    1 
ATOM   19944 C CD    . LYS A 1 4228 ? 203.840 205.558 267.673 1.00 20.34 ? 4228 LYS A CD    1 
ATOM   19945 C CE    . LYS A 1 4228 ? 203.558 206.917 267.056 1.00 21.57 ? 4228 LYS A CE    1 
ATOM   19946 N NZ    . LYS A 1 4228 ? 202.365 207.564 267.669 1.00 23.92 ? 4228 LYS A NZ    1 
ATOM   19947 N N     . GLY A 1 4229 ? 204.084 200.685 268.518 1.00 24.05 ? 4229 GLY A N     1 
ATOM   19948 C CA    . GLY A 1 4229 ? 204.203 199.449 269.263 1.00 27.45 ? 4229 GLY A CA    1 
ATOM   19949 C C     . GLY A 1 4229 ? 203.467 198.302 268.610 1.00 25.52 ? 4229 GLY A C     1 
ATOM   19950 O O     . GLY A 1 4229 ? 203.088 198.358 267.436 1.00 29.08 ? 4229 GLY A O     1 
ATOM   19951 N N     . ARG A 1 4230 ? 203.264 197.239 269.385 1.00 29.56 ? 4230 ARG A N     1 
ATOM   19952 C CA    . ARG A 1 4230 ? 202.585 196.040 268.912 1.00 35.09 ? 4230 ARG A CA    1 
ATOM   19953 C C     . ARG A 1 4230 ? 201.193 195.889 269.511 1.00 35.96 ? 4230 ARG A C     1 
ATOM   19954 O O     . ARG A 1 4230 ? 200.604 194.805 269.421 1.00 32.77 ? 4230 ARG A O     1 
ATOM   19955 C CB    . ARG A 1 4230 ? 203.430 194.801 269.224 1.00 39.70 ? 4230 ARG A CB    1 
ATOM   19956 C CG    . ARG A 1 4230 ? 203.994 194.787 270.637 1.00 38.77 ? 4230 ARG A CG    1 
ATOM   19957 C CD    . ARG A 1 4230 ? 204.760 193.508 270.931 1.00 34.79 ? 4230 ARG A CD    1 
ATOM   19958 N NE    . ARG A 1 4230 ? 205.380 193.545 272.251 1.00 35.89 ? 4230 ARG A NE    1 
ATOM   19959 C CZ    . ARG A 1 4230 ? 206.053 192.540 272.794 1.00 38.09 ? 4230 ARG A CZ    1 
ATOM   19960 N NH1   . ARG A 1 4230 ? 206.209 191.389 272.159 1.00 39.87 ? 4230 ARG A NH1   1 
ATOM   19961 N NH2   . ARG A 1 4230 ? 206.583 192.692 274.004 1.00 36.63 ? 4230 ARG A NH2   1 
ATOM   19962 N N     . GLN A 1 4231 ? 200.655 196.942 270.115 1.00 34.49 ? 4231 GLN A N     1 
ATOM   19963 C CA    . GLN A 1 4231 ? 199.385 196.839 270.811 1.00 36.39 ? 4231 GLN A CA    1 
ATOM   19964 C C     . GLN A 1 4231 ? 198.225 196.767 269.821 1.00 33.10 ? 4231 GLN A C     1 
ATOM   19965 O O     . GLN A 1 4231 ? 198.325 197.183 268.664 1.00 25.31 ? 4231 GLN A O     1 
ATOM   19966 C CB    . GLN A 1 4231 ? 199.191 198.023 271.761 1.00 33.81 ? 4231 GLN A CB    1 
ATOM   19967 C CG    . GLN A 1 4231 ? 199.004 199.373 271.078 1.00 33.85 ? 4231 GLN A CG    1 
ATOM   19968 C CD    . GLN A 1 4231 ? 200.303 199.972 270.576 1.00 31.87 ? 4231 GLN A CD    1 
ATOM   19969 O OE1   . GLN A 1 4231 ? 201.384 199.442 270.828 1.00 33.97 ? 4231 GLN A OE1   1 
ATOM   19970 N NE2   . GLN A 1 4231 ? 200.203 201.090 269.868 1.00 31.02 ? 4231 GLN A NE2   1 
ATOM   19971 N N     . ASN A 1 4232 ? 197.110 196.226 270.301 1.00 34.38 ? 4232 ASN A N     1 
ATOM   19972 C CA    . ASN A 1 4232 ? 195.871 196.167 269.533 1.00 30.20 ? 4232 ASN A CA    1 
ATOM   19973 C C     . ASN A 1 4232 ? 195.307 197.581 269.468 1.00 29.61 ? 4232 ASN A C     1 
ATOM   19974 O O     . ASN A 1 4232 ? 194.633 198.040 270.392 1.00 29.30 ? 4232 ASN A O     1 
ATOM   19975 C CB    . ASN A 1 4232 ? 194.905 195.185 270.194 1.00 29.71 ? 4232 ASN A CB    1 
ATOM   19976 C CG    . ASN A 1 4232 ? 193.468 195.306 269.692 1.00 29.96 ? 4232 ASN A CG    1 
ATOM   19977 O OD1   . ASN A 1 4232 ? 193.171 196.029 268.743 1.00 27.83 ? 4232 ASN A OD1   1 
ATOM   19978 N ND2   . ASN A 1 4232 ? 192.565 194.583 270.343 1.00 30.70 ? 4232 ASN A ND2   1 
ATOM   19979 N N     . ILE A 1 4233 ? 195.588 198.285 268.369 1.00 23.59 ? 4233 ILE A N     1 
ATOM   19980 C CA    . ILE A 1 4233 ? 195.141 199.664 268.231 1.00 26.44 ? 4233 ILE A CA    1 
ATOM   19981 C C     . ILE A 1 4233 ? 193.675 199.695 267.829 1.00 23.87 ? 4233 ILE A C     1 
ATOM   19982 O O     . ILE A 1 4233 ? 193.182 198.803 267.125 1.00 23.72 ? 4233 ILE A O     1 
ATOM   19983 C CB    . ILE A 1 4233 ? 196.009 200.421 267.212 1.00 23.62 ? 4233 ILE A CB    1 
ATOM   19984 C CG1   . ILE A 1 4233 ? 195.885 199.791 265.824 1.00 14.12 ? 4233 ILE A CG1   1 
ATOM   19985 C CG2   . ILE A 1 4233 ? 197.454 200.445 267.670 1.00 26.75 ? 4233 ILE A CG2   1 
ATOM   19986 C CD1   . ILE A 1 4233 ? 196.515 200.614 264.725 1.00 19.37 ? 4233 ILE A CD1   1 
ATOM   19987 N N     . SER A 1 4234 ? 192.969 200.725 268.281 1.00 16.23 ? 4234 SER A N     1 
ATOM   19988 C CA    . SER A 1 4234 ? 191.561 200.861 267.959 1.00 17.70 ? 4234 SER A CA    1 
ATOM   19989 C C     . SER A 1 4234 ? 191.384 201.156 266.471 1.00 19.50 ? 4234 SER A C     1 
ATOM   19990 O O     . SER A 1 4234 ? 192.237 201.796 265.851 1.00 17.75 ? 4234 SER A O     1 
ATOM   19991 C CB    . SER A 1 4234 ? 190.928 201.974 268.789 1.00 15.10 ? 4234 SER A CB    1 
ATOM   19992 O OG    . SER A 1 4234 ? 189.749 202.466 268.176 1.00 16.78 ? 4234 SER A OG    1 
ATOM   19993 N N     . PRO A 1 4235 ? 190.291 200.681 265.869 1.00 17.22 ? 4235 PRO A N     1 
ATOM   19994 C CA    . PRO A 1 4235 ? 190.029 201.022 264.462 1.00 9.03  ? 4235 PRO A CA    1 
ATOM   19995 C C     . PRO A 1 4235 ? 189.902 202.514 264.218 1.00 8.60  ? 4235 PRO A C     1 
ATOM   19996 O O     . PRO A 1 4235 ? 190.214 202.979 263.117 1.00 13.18 ? 4235 PRO A O     1 
ATOM   19997 C CB    . PRO A 1 4235 ? 188.716 200.285 264.163 1.00 9.82  ? 4235 PRO A CB    1 
ATOM   19998 C CG    . PRO A 1 4235 ? 188.656 199.191 265.170 1.00 13.71 ? 4235 PRO A CG    1 
ATOM   19999 C CD    . PRO A 1 4235 ? 189.296 199.738 266.405 1.00 12.43 ? 4235 PRO A CD    1 
ATOM   20000 N N     . ASP A 1 4236 ? 189.445 203.280 265.211 1.00 10.46 ? 4236 ASP A N     1 
ATOM   20001 C CA    . ASP A 1 4236 ? 189.341 204.725 265.042 1.00 12.93 ? 4236 ASP A CA    1 
ATOM   20002 C C     . ASP A 1 4236 ? 190.710 205.354 264.823 1.00 10.65 ? 4236 ASP A C     1 
ATOM   20003 O O     . ASP A 1 4236 ? 190.822 206.404 264.179 1.00 10.94 ? 4236 ASP A O     1 
ATOM   20004 C CB    . ASP A 1 4236 ? 188.654 205.346 266.257 1.00 13.88 ? 4236 ASP A CB    1 
ATOM   20005 C CG    . ASP A 1 4236 ? 187.215 204.903 266.402 1.00 14.86 ? 4236 ASP A CG    1 
ATOM   20006 O OD1   . ASP A 1 4236 ? 186.703 204.234 265.480 1.00 17.98 ? 4236 ASP A OD1   1 
ATOM   20007 O OD2   . ASP A 1 4236 ? 186.595 205.222 267.438 1.00 14.09 ? 4236 ASP A OD2   1 
ATOM   20008 N N     . LYS A 1 4237 ? 191.761 204.730 265.355 1.00 13.53 ? 4237 LYS A N     1 
ATOM   20009 C CA    . LYS A 1 4237 ? 193.116 205.236 265.191 1.00 13.04 ? 4237 LYS A CA    1 
ATOM   20010 C C     . LYS A 1 4237 ? 193.754 204.795 263.882 1.00 10.75 ? 4237 LYS A C     1 
ATOM   20011 O O     . LYS A 1 4237 ? 194.887 205.199 263.601 1.00 12.52 ? 4237 LYS A O     1 
ATOM   20012 C CB    . LYS A 1 4237 ? 193.982 204.785 266.367 1.00 10.19 ? 4237 LYS A CB    1 
ATOM   20013 C CG    . LYS A 1 4237 ? 193.840 205.650 267.608 1.00 10.97 ? 4237 LYS A CG    1 
ATOM   20014 C CD    . LYS A 1 4237 ? 194.899 205.311 268.643 1.00 9.23  ? 4237 LYS A CD    1 
ATOM   20015 C CE    . LYS A 1 4237 ? 196.299 205.469 268.078 1.00 16.12 ? 4237 LYS A CE    1 
ATOM   20016 N NZ    . LYS A 1 4237 ? 197.332 204.935 269.007 1.00 19.57 ? 4237 LYS A NZ    1 
ATOM   20017 N N     . ILE A 1 4238 ? 193.067 203.979 263.088 1.00 5.16  ? 4238 ILE A N     1 
ATOM   20018 C CA    . ILE A 1 4238 ? 193.620 203.542 261.802 1.00 4.71  ? 4238 ILE A CA    1 
ATOM   20019 C C     . ILE A 1 4238 ? 193.742 204.749 260.880 1.00 8.04  ? 4238 ILE A C     1 
ATOM   20020 O O     . ILE A 1 4238 ? 192.772 205.519 260.739 1.00 6.26  ? 4238 ILE A O     1 
ATOM   20021 C CB    . ILE A 1 4238 ? 192.727 202.458 261.173 1.00 6.29  ? 4238 ILE A CB    1 
ATOM   20022 C CG1   . ILE A 1 4238 ? 192.779 201.169 261.996 1.00 4.83  ? 4238 ILE A CG1   1 
ATOM   20023 C CG2   . ILE A 1 4238 ? 193.143 202.183 259.738 1.00 5.70  ? 4238 ILE A CG2   1 
ATOM   20024 C CD1   . ILE A 1 4238 ? 194.021 200.347 261.780 1.00 0.58  ? 4238 ILE A CD1   1 
ATOM   20025 N N     . PRO A 1 4239 ? 194.890 204.972 260.232 1.00 9.07  ? 4239 PRO A N     1 
ATOM   20026 C CA    . PRO A 1 4239 ? 195.016 206.129 259.335 1.00 2.28  ? 4239 PRO A CA    1 
ATOM   20027 C C     . PRO A 1 4239 ? 194.180 205.971 258.076 1.00 3.18  ? 4239 PRO A C     1 
ATOM   20028 O O     . PRO A 1 4239 ? 194.718 205.773 256.984 1.00 8.39  ? 4239 PRO A O     1 
ATOM   20029 C CB    . PRO A 1 4239 ? 196.515 206.163 259.015 1.00 0.15  ? 4239 PRO A CB    1 
ATOM   20030 C CG    . PRO A 1 4239 ? 196.974 204.762 259.221 1.00 5.02  ? 4239 PRO A CG    1 
ATOM   20031 C CD    . PRO A 1 4239 ? 196.150 204.219 260.348 1.00 3.41  ? 4239 PRO A CD    1 
ATOM   20032 N N     . TRP A 1 4240 ? 192.858 206.059 258.228 1.00 5.21  ? 4240 TRP A N     1 
ATOM   20033 C CA    . TRP A 1 4240 ? 191.955 205.825 257.106 1.00 0.00  ? 4240 TRP A CA    1 
ATOM   20034 C C     . TRP A 1 4240 ? 192.177 206.840 255.995 1.00 0.00  ? 4240 TRP A C     1 
ATOM   20035 O O     . TRP A 1 4240 ? 192.217 206.484 254.812 1.00 0.00  ? 4240 TRP A O     1 
ATOM   20036 C CB    . TRP A 1 4240 ? 190.509 205.877 257.595 1.00 2.23  ? 4240 TRP A CB    1 
ATOM   20037 C CG    . TRP A 1 4240 ? 190.118 204.728 258.462 1.00 3.51  ? 4240 TRP A CG    1 
ATOM   20038 C CD1   . TRP A 1 4240 ? 189.573 204.797 259.707 1.00 5.33  ? 4240 TRP A CD1   1 
ATOM   20039 C CD2   . TRP A 1 4240 ? 190.192 203.334 258.133 1.00 3.97  ? 4240 TRP A CD2   1 
ATOM   20040 N NE1   . TRP A 1 4240 ? 189.332 203.536 260.189 1.00 7.40  ? 4240 TRP A NE1   1 
ATOM   20041 C CE2   . TRP A 1 4240 ? 189.696 202.620 259.239 1.00 5.34  ? 4240 TRP A CE2   1 
ATOM   20042 C CE3   . TRP A 1 4240 ? 190.638 202.622 257.016 1.00 4.77  ? 4240 TRP A CE3   1 
ATOM   20043 C CZ2   . TRP A 1 4240 ? 189.635 201.230 259.261 1.00 8.02  ? 4240 TRP A CZ2   1 
ATOM   20044 C CZ3   . TRP A 1 4240 ? 190.575 201.244 257.040 1.00 1.47  ? 4240 TRP A CZ3   1 
ATOM   20045 C CH2   . TRP A 1 4240 ? 190.077 200.563 258.154 1.00 7.84  ? 4240 TRP A CH2   1 
ATOM   20046 N N     . SER A 1 4241 ? 192.314 208.117 256.360 1.00 0.85  ? 4241 SER A N     1 
ATOM   20047 C CA    . SER A 1 4241 ? 192.462 209.164 255.355 1.00 0.00  ? 4241 SER A CA    1 
ATOM   20048 C C     . SER A 1 4241 ? 193.739 208.982 254.550 1.00 0.00  ? 4241 SER A C     1 
ATOM   20049 O O     . SER A 1 4241 ? 193.738 209.157 253.327 1.00 5.15  ? 4241 SER A O     1 
ATOM   20050 C CB    . SER A 1 4241 ? 192.439 210.538 256.022 1.00 7.21  ? 4241 SER A CB    1 
ATOM   20051 O OG    . SER A 1 4241 ? 191.215 210.753 256.702 1.00 13.74 ? 4241 SER A OG    1 
ATOM   20052 N N     . ALA A 1 4242 ? 194.839 208.628 255.216 1.00 2.15  ? 4242 ALA A N     1 
ATOM   20053 C CA    . ALA A 1 4242 ? 196.100 208.437 254.509 1.00 0.00  ? 4242 ALA A CA    1 
ATOM   20054 C C     . ALA A 1 4242 ? 195.986 207.319 253.482 1.00 0.00  ? 4242 ALA A C     1 
ATOM   20055 O O     . ALA A 1 4242 ? 196.382 207.483 252.323 1.00 0.81  ? 4242 ALA A O     1 
ATOM   20056 C CB    . ALA A 1 4242 ? 197.219 208.141 255.506 1.00 2.81  ? 4242 ALA A CB    1 
ATOM   20057 N N     . LEU A 1 4243 ? 195.425 206.178 253.888 1.00 1.15  ? 4243 LEU A N     1 
ATOM   20058 C CA    . LEU A 1 4243 ? 195.289 205.050 252.973 1.00 0.00  ? 4243 LEU A CA    1 
ATOM   20059 C C     . LEU A 1 4243 ? 194.353 205.382 251.819 1.00 0.98  ? 4243 LEU A C     1 
ATOM   20060 O O     . LEU A 1 4243 ? 194.669 205.104 250.656 1.00 6.81  ? 4243 LEU A O     1 
ATOM   20061 C CB    . LEU A 1 4243 ? 194.787 203.819 253.726 1.00 0.00  ? 4243 LEU A CB    1 
ATOM   20062 C CG    . LEU A 1 4243 ? 195.567 203.379 254.964 1.00 0.00  ? 4243 LEU A CG    1 
ATOM   20063 C CD1   . LEU A 1 4243 ? 194.936 202.135 255.561 1.00 0.83  ? 4243 LEU A CD1   1 
ATOM   20064 C CD2   . LEU A 1 4243 ? 197.029 203.139 254.633 1.00 2.85  ? 4243 LEU A CD2   1 
ATOM   20065 N N     . LYS A 1 4244 ? 193.199 205.983 252.116 1.00 1.22  ? 4244 LYS A N     1 
ATOM   20066 C CA    . LYS A 1 4244 ? 192.242 206.301 251.062 1.00 0.00  ? 4244 LYS A CA    1 
ATOM   20067 C C     . LYS A 1 4244 ? 192.828 207.294 250.070 1.00 0.00  ? 4244 LYS A C     1 
ATOM   20068 O O     . LYS A 1 4244 ? 192.705 207.117 248.855 1.00 11.32 ? 4244 LYS A O     1 
ATOM   20069 C CB    . LYS A 1 4244 ? 190.951 206.851 251.664 1.00 0.00  ? 4244 LYS A CB    1 
ATOM   20070 C CG    . LYS A 1 4244 ? 190.115 205.822 252.385 1.00 0.00  ? 4244 LYS A CG    1 
ATOM   20071 C CD    . LYS A 1 4244 ? 188.704 206.325 252.599 1.00 5.65  ? 4244 LYS A CD    1 
ATOM   20072 C CE    . LYS A 1 4244 ? 188.692 207.602 253.417 1.00 1.45  ? 4244 LYS A CE    1 
ATOM   20073 N NZ    . LYS A 1 4244 ? 189.204 207.380 254.795 1.00 4.53  ? 4244 LYS A NZ    1 
ATOM   20074 N N     . THR A 1 4245 ? 193.480 208.345 250.568 1.00 0.00  ? 4245 THR A N     1 
ATOM   20075 C CA    . THR A 1 4245 ? 194.039 209.352 249.677 1.00 0.00  ? 4245 THR A CA    1 
ATOM   20076 C C     . THR A 1 4245 ? 195.192 208.790 248.856 1.00 2.11  ? 4245 THR A C     1 
ATOM   20077 O O     . THR A 1 4245 ? 195.307 209.083 247.661 1.00 2.40  ? 4245 THR A O     1 
ATOM   20078 C CB    . THR A 1 4245 ? 194.489 210.567 250.485 1.00 0.53  ? 4245 THR A CB    1 
ATOM   20079 O OG1   . THR A 1 4245 ? 193.351 211.158 251.124 1.00 2.86  ? 4245 THR A OG1   1 
ATOM   20080 C CG2   . THR A 1 4245 ? 195.144 211.600 249.585 1.00 3.39  ? 4245 THR A CG2   1 
ATOM   20081 N N     . LEU A 1 4246 ? 196.048 207.972 249.468 1.00 5.09  ? 4246 LEU A N     1 
ATOM   20082 C CA    . LEU A 1 4246 ? 197.189 207.437 248.738 1.00 0.00  ? 4246 LEU A CA    1 
ATOM   20083 C C     . LEU A 1 4246 ? 196.759 206.398 247.712 1.00 0.00  ? 4246 LEU A C     1 
ATOM   20084 O O     . LEU A 1 4246 ? 197.404 206.249 246.670 1.00 6.07  ? 4246 LEU A O     1 
ATOM   20085 C CB    . LEU A 1 4246 ? 198.203 206.851 249.717 1.00 0.00  ? 4246 LEU A CB    1 
ATOM   20086 C CG    . LEU A 1 4246 ? 199.067 207.906 250.405 1.00 0.00  ? 4246 LEU A CG    1 
ATOM   20087 C CD1   . LEU A 1 4246 ? 199.570 207.396 251.731 1.00 0.20  ? 4246 LEU A CD1   1 
ATOM   20088 C CD2   . LEU A 1 4246 ? 200.224 208.310 249.518 1.00 2.17  ? 4246 LEU A CD2   1 
ATOM   20089 N N     . MET A 1 4247 ? 195.677 205.670 247.979 1.00 0.00  ? 4247 MET A N     1 
ATOM   20090 C CA    . MET A 1 4247 ? 195.188 204.683 247.029 1.00 1.96  ? 4247 MET A CA    1 
ATOM   20091 C C     . MET A 1 4247 ? 194.174 205.251 246.046 1.00 0.08  ? 4247 MET A C     1 
ATOM   20092 O O     . MET A 1 4247 ? 193.777 204.547 245.116 1.00 3.05  ? 4247 MET A O     1 
ATOM   20093 C CB    . MET A 1 4247 ? 194.578 203.490 247.770 1.00 1.68  ? 4247 MET A CB    1 
ATOM   20094 C CG    . MET A 1 4247 ? 195.599 202.658 248.527 1.00 0.78  ? 4247 MET A CG    1 
ATOM   20095 S SD    . MET A 1 4247 ? 194.863 201.517 249.705 1.00 12.06 ? 4247 MET A SD    1 
ATOM   20096 C CE    . MET A 1 4247 ? 193.603 200.768 248.681 1.00 3.87  ? 4247 MET A CE    1 
ATOM   20097 N N     . ALA A 1 4248 ? 193.730 206.493 246.235 1.00 0.00  ? 4248 ALA A N     1 
ATOM   20098 C CA    . ALA A 1 4248 ? 192.878 207.155 245.262 1.00 0.00  ? 4248 ALA A CA    1 
ATOM   20099 C C     . ALA A 1 4248 ? 193.610 208.178 244.415 1.00 4.32  ? 4248 ALA A C     1 
ATOM   20100 O O     . ALA A 1 4248 ? 193.102 208.552 243.355 1.00 14.25 ? 4248 ALA A O     1 
ATOM   20101 C CB    . ALA A 1 4248 ? 191.707 207.856 245.964 1.00 1.55  ? 4248 ALA A CB    1 
ATOM   20102 N N     . GLN A 1 4249 ? 194.782 208.635 244.850 1.00 6.83  ? 4249 GLN A N     1 
ATOM   20103 C CA    . GLN A 1 4249 ? 195.489 209.704 244.171 1.00 8.52  ? 4249 GLN A CA    1 
ATOM   20104 C C     . GLN A 1 4249 ? 196.875 209.303 243.688 1.00 5.06  ? 4249 GLN A C     1 
ATOM   20105 O O     . GLN A 1 4249 ? 197.436 210.003 242.839 1.00 4.94  ? 4249 GLN A O     1 
ATOM   20106 C CB    . GLN A 1 4249 ? 195.626 210.921 245.103 1.00 9.43  ? 4249 GLN A CB    1 
ATOM   20107 C CG    . GLN A 1 4249 ? 194.318 211.595 245.511 1.00 9.53  ? 4249 GLN A CG    1 
ATOM   20108 C CD    . GLN A 1 4249 ? 193.549 212.180 244.345 1.00 12.70 ? 4249 GLN A CD    1 
ATOM   20109 O OE1   . GLN A 1 4249 ? 193.961 213.178 243.757 1.00 13.51 ? 4249 GLN A OE1   1 
ATOM   20110 N NE2   . GLN A 1 4249 ? 192.411 211.577 244.021 1.00 11.71 ? 4249 GLN A NE2   1 
ATOM   20111 N N     . SER A 1 4250 ? 197.437 208.212 244.186 1.00 4.43  ? 4250 SER A N     1 
ATOM   20112 C CA    . SER A 1 4250 ? 198.861 207.979 243.967 1.00 0.38  ? 4250 SER A CA    1 
ATOM   20113 C C     . SER A 1 4250 ? 199.194 206.624 243.360 1.00 2.51  ? 4250 SER A C     1 
ATOM   20114 O O     . SER A 1 4250 ? 200.121 206.539 242.552 1.00 6.46  ? 4250 SER A O     1 
ATOM   20115 C CB    . SER A 1 4250 ? 199.614 208.144 245.296 1.00 0.08  ? 4250 SER A CB    1 
ATOM   20116 O OG    . SER A 1 4250 ? 200.997 207.893 245.133 1.00 8.21  ? 4250 SER A OG    1 
ATOM   20117 N N     . ILE A 1 4251 ? 198.480 205.562 243.728 1.00 4.96  ? 4251 ILE A N     1 
ATOM   20118 C CA    . ILE A 1 4251 ? 198.910 204.226 243.327 1.00 8.17  ? 4251 ILE A CA    1 
ATOM   20119 C C     . ILE A 1 4251 ? 197.826 203.487 242.551 1.00 1.57  ? 4251 ILE A C     1 
ATOM   20120 O O     . ILE A 1 4251 ? 198.128 202.605 241.742 1.00 5.84  ? 4251 ILE A O     1 
ATOM   20121 C CB    . ILE A 1 4251 ? 199.375 203.413 244.550 1.00 2.74  ? 4251 ILE A CB    1 
ATOM   20122 C CG1   . ILE A 1 4251 ? 198.253 203.277 245.568 1.00 2.95  ? 4251 ILE A CG1   1 
ATOM   20123 C CG2   . ILE A 1 4251 ? 200.597 204.054 245.193 1.00 5.60  ? 4251 ILE A CG2   1 
ATOM   20124 C CD1   . ILE A 1 4251 ? 198.684 202.568 246.809 1.00 3.75  ? 4251 ILE A CD1   1 
ATOM   20125 N N     . TYR A 1 4252 ? 196.564 203.842 242.772 1.00 0.00  ? 4252 TYR A N     1 
ATOM   20126 C CA    . TYR A 1 4252 ? 195.481 203.313 241.954 1.00 1.14  ? 4252 TYR A CA    1 
ATOM   20127 C C     . TYR A 1 4252 ? 194.804 204.373 241.104 1.00 1.54  ? 4252 TYR A C     1 
ATOM   20128 O O     . TYR A 1 4252 ? 194.341 204.064 240.006 1.00 2.65  ? 4252 TYR A O     1 
ATOM   20129 C CB    . TYR A 1 4252 ? 194.429 202.624 242.832 1.00 1.89  ? 4252 TYR A CB    1 
ATOM   20130 C CG    . TYR A 1 4252 ? 194.808 201.228 243.265 1.00 0.00  ? 4252 TYR A CG    1 
ATOM   20131 C CD1   . TYR A 1 4252 ? 194.748 200.165 242.378 1.00 0.33  ? 4252 TYR A CD1   1 
ATOM   20132 C CD2   . TYR A 1 4252 ? 195.240 200.977 244.559 1.00 3.26  ? 4252 TYR A CD2   1 
ATOM   20133 C CE1   . TYR A 1 4252 ? 195.097 198.889 242.771 1.00 1.84  ? 4252 TYR A CE1   1 
ATOM   20134 C CE2   . TYR A 1 4252 ? 195.594 199.707 244.959 1.00 2.43  ? 4252 TYR A CE2   1 
ATOM   20135 C CZ    . TYR A 1 4252 ? 195.520 198.667 244.062 1.00 1.26  ? 4252 TYR A CZ    1 
ATOM   20136 O OH    . TYR A 1 4252 ? 195.870 197.398 244.457 1.00 2.13  ? 4252 TYR A OH    1 
ATOM   20137 N N     . GLY A 1 4253 ? 194.732 205.611 241.589 1.00 1.06  ? 4253 GLY A N     1 
ATOM   20138 C CA    . GLY A 1 4253 ? 194.269 206.719 240.782 1.00 0.00  ? 4253 GLY A CA    1 
ATOM   20139 C C     . GLY A 1 4253 ? 195.324 207.338 239.903 1.00 1.60  ? 4253 GLY A C     1 
ATOM   20140 O O     . GLY A 1 4253 ? 195.010 208.229 239.109 1.00 10.61 ? 4253 GLY A O     1 
ATOM   20141 N N     . GLY A 1 4254 ? 196.571 206.887 240.024 1.00 0.00  ? 4254 GLY A N     1 
ATOM   20142 C CA    . GLY A 1 4254 ? 197.625 207.366 239.154 1.00 0.00  ? 4254 GLY A CA    1 
ATOM   20143 C C     . GLY A 1 4254 ? 197.534 206.859 237.734 1.00 3.16  ? 4254 GLY A C     1 
ATOM   20144 O O     . GLY A 1 4254 ? 198.251 207.366 236.867 1.00 18.24 ? 4254 GLY A O     1 
ATOM   20145 N N     . ARG A 1 4255 ? 196.675 205.876 237.476 1.00 2.99  ? 4255 ARG A N     1 
ATOM   20146 C CA    . ARG A 1 4255 ? 196.457 205.364 236.133 1.00 1.03  ? 4255 ARG A CA    1 
ATOM   20147 C C     . ARG A 1 4255 ? 195.080 205.715 235.595 1.00 0.00  ? 4255 ARG A C     1 
ATOM   20148 O O     . ARG A 1 4255 ? 194.819 205.504 234.407 1.00 0.00  ? 4255 ARG A O     1 
ATOM   20149 C CB    . ARG A 1 4255 ? 196.659 203.846 236.114 1.00 1.37  ? 4255 ARG A CB    1 
ATOM   20150 C CG    . ARG A 1 4255 ? 197.751 203.381 237.059 1.00 5.03  ? 4255 ARG A CG    1 
ATOM   20151 C CD    . ARG A 1 4255 ? 197.805 201.871 237.164 1.00 2.25  ? 4255 ARG A CD    1 
ATOM   20152 N NE    . ARG A 1 4255 ? 198.539 201.294 236.045 1.00 0.83  ? 4255 ARG A NE    1 
ATOM   20153 C CZ    . ARG A 1 4255 ? 199.726 200.712 236.152 1.00 4.79  ? 4255 ARG A CZ    1 
ATOM   20154 N NH1   . ARG A 1 4255 ? 200.327 200.577 237.322 1.00 5.12  ? 4255 ARG A NH1   1 
ATOM   20155 N NH2   . ARG A 1 4255 ? 200.324 200.254 235.057 1.00 6.67  ? 4255 ARG A NH2   1 
ATOM   20156 N N     . VAL A 1 4256 ? 194.199 206.250 236.433 1.00 1.24  ? 4256 VAL A N     1 
ATOM   20157 C CA    . VAL A 1 4256 ? 192.866 206.648 235.999 1.00 2.70  ? 4256 VAL A CA    1 
ATOM   20158 C C     . VAL A 1 4256 ? 192.967 207.962 235.239 1.00 2.86  ? 4256 VAL A C     1 
ATOM   20159 O O     . VAL A 1 4256 ? 193.567 208.928 235.723 1.00 3.53  ? 4256 VAL A O     1 
ATOM   20160 C CB    . VAL A 1 4256 ? 191.917 206.769 237.200 1.00 0.00  ? 4256 VAL A CB    1 
ATOM   20161 C CG1   . VAL A 1 4256 ? 190.660 207.512 236.802 1.00 0.62  ? 4256 VAL A CG1   1 
ATOM   20162 C CG2   . VAL A 1 4256 ? 191.578 205.396 237.746 1.00 0.00  ? 4256 VAL A CG2   1 
ATOM   20163 N N     . ASP A 1 4257 ? 192.375 208.002 234.046 1.00 5.73  ? 4257 ASP A N     1 
ATOM   20164 C CA    . ASP A 1 4257 ? 192.480 209.164 233.173 1.00 1.40  ? 4257 ASP A CA    1 
ATOM   20165 C C     . ASP A 1 4257 ? 191.354 210.168 233.380 1.00 0.91  ? 4257 ASP A C     1 
ATOM   20166 O O     . ASP A 1 4257 ? 191.619 211.364 233.537 1.00 6.05  ? 4257 ASP A O     1 
ATOM   20167 C CB    . ASP A 1 4257 ? 192.497 208.722 231.709 1.00 4.11  ? 4257 ASP A CB    1 
ATOM   20168 C CG    . ASP A 1 4257 ? 193.897 208.513 231.181 1.00 11.41 ? 4257 ASP A CG    1 
ATOM   20169 O OD1   . ASP A 1 4257 ? 194.101 207.562 230.399 1.00 7.25  ? 4257 ASP A OD1   1 
ATOM   20170 O OD2   . ASP A 1 4257 ? 194.794 209.302 231.545 1.00 8.42  ? 4257 ASP A OD2   1 
ATOM   20171 N N     . ASN A 1 4258 ? 190.105 209.719 233.386 1.00 0.00  ? 4258 ASN A N     1 
ATOM   20172 C CA    . ASN A 1 4258 ? 188.972 210.629 233.407 1.00 5.03  ? 4258 ASN A CA    1 
ATOM   20173 C C     . ASN A 1 4258 ? 188.470 210.837 234.829 1.00 3.00  ? 4258 ASN A C     1 
ATOM   20174 O O     . ASN A 1 4258 ? 188.929 210.207 235.784 1.00 5.27  ? 4258 ASN A O     1 
ATOM   20175 C CB    . ASN A 1 4258 ? 187.831 210.133 232.506 1.00 8.03  ? 4258 ASN A CB    1 
ATOM   20176 C CG    . ASN A 1 4258 ? 187.337 208.758 232.885 1.00 1.98  ? 4258 ASN A CG    1 
ATOM   20177 O OD1   . ASN A 1 4258 ? 187.776 208.179 233.873 1.00 5.75  ? 4258 ASN A OD1   1 
ATOM   20178 N ND2   . ASN A 1 4258 ? 186.398 208.236 232.109 1.00 0.63  ? 4258 ASN A ND2   1 
ATOM   20179 N N     . GLU A 1 4259 ? 187.504 211.750 234.945 1.00 5.04  ? 4259 GLU A N     1 
ATOM   20180 C CA    . GLU A 1 4259 ? 186.989 212.147 236.249 1.00 3.84  ? 4259 GLU A CA    1 
ATOM   20181 C C     . GLU A 1 4259 ? 186.105 211.067 236.859 1.00 5.20  ? 4259 GLU A C     1 
ATOM   20182 O O     . GLU A 1 4259 ? 186.092 210.883 238.080 1.00 12.48 ? 4259 GLU A O     1 
ATOM   20183 C CB    . GLU A 1 4259 ? 186.217 213.459 236.112 1.00 14.38 ? 4259 GLU A CB    1 
ATOM   20184 C CG    . GLU A 1 4259 ? 185.260 213.756 237.252 1.00 18.55 ? 4259 GLU A CG    1 
ATOM   20185 C CD    . GLU A 1 4259 ? 184.114 214.653 236.830 1.00 17.85 ? 4259 GLU A CD    1 
ATOM   20186 O OE1   . GLU A 1 4259 ? 183.160 214.807 237.620 1.00 20.58 ? 4259 GLU A OE1   1 
ATOM   20187 O OE2   . GLU A 1 4259 ? 184.167 215.200 235.709 1.00 16.37 ? 4259 GLU A OE2   1 
ATOM   20188 N N     . PHE A 1 4260 ? 185.361 210.339 236.027 1.00 4.97  ? 4260 PHE A N     1 
ATOM   20189 C CA    . PHE A 1 4260 ? 184.297 209.486 236.548 1.00 0.00  ? 4260 PHE A CA    1 
ATOM   20190 C C     . PHE A 1 4260 ? 184.842 208.160 237.068 1.00 1.88  ? 4260 PHE A C     1 
ATOM   20191 O O     . PHE A 1 4260 ? 184.352 207.632 238.075 1.00 15.55 ? 4260 PHE A O     1 
ATOM   20192 C CB    . PHE A 1 4260 ? 183.244 209.279 235.464 1.00 0.00  ? 4260 PHE A CB    1 
ATOM   20193 C CG    . PHE A 1 4260 ? 182.560 210.552 235.061 1.00 5.13  ? 4260 PHE A CG    1 
ATOM   20194 C CD1   . PHE A 1 4260 ? 181.421 210.981 235.715 1.00 5.64  ? 4260 PHE A CD1   1 
ATOM   20195 C CD2   . PHE A 1 4260 ? 183.083 211.341 234.051 1.00 4.88  ? 4260 PHE A CD2   1 
ATOM   20196 C CE1   . PHE A 1 4260 ? 180.805 212.160 235.357 1.00 5.33  ? 4260 PHE A CE1   1 
ATOM   20197 C CE2   . PHE A 1 4260 ? 182.470 212.520 233.691 1.00 3.95  ? 4260 PHE A CE2   1 
ATOM   20198 C CZ    . PHE A 1 4260 ? 181.329 212.930 234.344 1.00 2.14  ? 4260 PHE A CZ    1 
ATOM   20199 N N     . ASP A 1 4261 ? 185.865 207.614 236.411 1.00 0.00  ? 4261 ASP A N     1 
ATOM   20200 C CA    . ASP A 1 4261 ? 186.534 206.439 236.957 1.00 0.00  ? 4261 ASP A CA    1 
ATOM   20201 C C     . ASP A 1 4261 ? 187.225 206.769 238.272 1.00 1.10  ? 4261 ASP A C     1 
ATOM   20202 O O     . ASP A 1 4261 ? 187.234 205.953 239.200 1.00 2.38  ? 4261 ASP A O     1 
ATOM   20203 C CB    . ASP A 1 4261 ? 187.532 205.885 235.944 1.00 0.98  ? 4261 ASP A CB    1 
ATOM   20204 C CG    . ASP A 1 4261 ? 186.853 205.232 234.761 1.00 5.13  ? 4261 ASP A CG    1 
ATOM   20205 O OD1   . ASP A 1 4261 ? 185.628 205.003 234.831 1.00 7.11  ? 4261 ASP A OD1   1 
ATOM   20206 O OD2   . ASP A 1 4261 ? 187.542 204.959 233.757 1.00 6.31  ? 4261 ASP A OD2   1 
ATOM   20207 N N     . GLN A 1 4262 ? 187.810 207.965 238.372 1.00 0.00  ? 4262 GLN A N     1 
ATOM   20208 C CA    . GLN A 1 4262 ? 188.367 208.413 239.644 1.00 0.00  ? 4262 GLN A CA    1 
ATOM   20209 C C     . GLN A 1 4262 ? 187.280 208.561 240.698 1.00 0.00  ? 4262 GLN A C     1 
ATOM   20210 O O     . GLN A 1 4262 ? 187.490 208.225 241.868 1.00 15.72 ? 4262 GLN A O     1 
ATOM   20211 C CB    . GLN A 1 4262 ? 189.114 209.732 239.457 1.00 0.00  ? 4262 GLN A CB    1 
ATOM   20212 C CG    . GLN A 1 4262 ? 189.800 210.241 240.713 1.00 2.44  ? 4262 GLN A CG    1 
ATOM   20213 C CD    . GLN A 1 4262 ? 190.895 209.319 241.203 1.00 0.00  ? 4262 GLN A CD    1 
ATOM   20214 O OE1   . GLN A 1 4262 ? 191.960 209.226 240.597 1.00 1.66  ? 4262 GLN A OE1   1 
ATOM   20215 N NE2   . GLN A 1 4262 ? 190.640 208.637 242.309 1.00 0.00  ? 4262 GLN A NE2   1 
ATOM   20216 N N     . ARG A 1 4263 ? 186.113 209.068 240.305 1.00 0.00  ? 4263 ARG A N     1 
ATOM   20217 C CA    . ARG A 1 4263 ? 185.011 209.199 241.250 1.00 0.00  ? 4263 ARG A CA    1 
ATOM   20218 C C     . ARG A 1 4263 ? 184.577 207.840 241.771 1.00 0.00  ? 4263 ARG A C     1 
ATOM   20219 O O     . ARG A 1 4263 ? 184.278 207.686 242.959 1.00 4.90  ? 4263 ARG A O     1 
ATOM   20220 C CB    . ARG A 1 4263 ? 183.836 209.925 240.593 1.00 0.00  ? 4263 ARG A CB    1 
ATOM   20221 C CG    . ARG A 1 4263 ? 182.600 210.017 241.465 1.00 0.00  ? 4263 ARG A CG    1 
ATOM   20222 C CD    . ARG A 1 4263 ? 181.498 210.812 240.789 1.00 3.17  ? 4263 ARG A CD    1 
ATOM   20223 N NE    . ARG A 1 4263 ? 180.864 210.085 239.697 1.00 6.15  ? 4263 ARG A NE    1 
ATOM   20224 C CZ    . ARG A 1 4263 ? 179.975 210.612 238.867 1.00 1.56  ? 4263 ARG A CZ    1 
ATOM   20225 N NH1   . ARG A 1 4263 ? 179.598 211.875 238.970 1.00 0.00  ? 4263 ARG A NH1   1 
ATOM   20226 N NH2   . ARG A 1 4263 ? 179.445 209.852 237.915 1.00 1.08  ? 4263 ARG A NH2   1 
ATOM   20227 N N     . LEU A 1 4264 ? 184.555 206.832 240.901 1.00 0.00  ? 4264 LEU A N     1 
ATOM   20228 C CA    . LEU A 1 4264 ? 184.139 205.507 241.347 1.00 0.00  ? 4264 LEU A CA    1 
ATOM   20229 C C     . LEU A 1 4264 ? 185.226 204.820 242.171 1.00 0.00  ? 4264 LEU A C     1 
ATOM   20230 O O     . LEU A 1 4264 ? 184.923 204.080 243.116 1.00 8.19  ? 4264 LEU A O     1 
ATOM   20231 C CB    . LEU A 1 4264 ? 183.716 204.667 240.148 1.00 1.43  ? 4264 LEU A CB    1 
ATOM   20232 C CG    . LEU A 1 4264 ? 183.226 203.289 240.551 1.00 4.64  ? 4264 LEU A CG    1 
ATOM   20233 C CD1   . LEU A 1 4264 ? 182.100 203.485 241.513 1.00 7.07  ? 4264 LEU A CD1   1 
ATOM   20234 C CD2   . LEU A 1 4264 ? 182.697 202.609 239.324 1.00 1.61  ? 4264 LEU A CD2   1 
ATOM   20235 N N     . LEU A 1 4265 ? 186.495 205.061 241.843 1.00 2.71  ? 4265 LEU A N     1 
ATOM   20236 C CA    . LEU A 1 4265 ? 187.579 204.610 242.710 1.00 0.00  ? 4265 LEU A CA    1 
ATOM   20237 C C     . LEU A 1 4265 ? 187.441 205.207 244.103 1.00 0.00  ? 4265 LEU A C     1 
ATOM   20238 O O     . LEU A 1 4265 ? 187.586 204.504 245.114 1.00 4.46  ? 4265 LEU A O     1 
ATOM   20239 C CB    . LEU A 1 4265 ? 188.922 204.994 242.091 1.00 0.00  ? 4265 LEU A CB    1 
ATOM   20240 C CG    . LEU A 1 4265 ? 190.198 204.469 242.740 1.00 0.00  ? 4265 LEU A CG    1 
ATOM   20241 C CD1   . LEU A 1 4265 ? 190.204 202.961 242.767 1.00 4.66  ? 4265 LEU A CD1   1 
ATOM   20242 C CD2   . LEU A 1 4265 ? 191.396 204.988 241.984 1.00 1.19  ? 4265 LEU A CD2   1 
ATOM   20243 N N     . ASN A 1 4266 ? 187.139 206.504 244.170 1.00 0.00  ? 4266 ASN A N     1 
ATOM   20244 C CA    . ASN A 1 4266 ? 186.900 207.157 245.450 1.00 0.00  ? 4266 ASN A CA    1 
ATOM   20245 C C     . ASN A 1 4266 ? 185.699 206.549 246.159 1.00 0.07  ? 4266 ASN A C     1 
ATOM   20246 O O     . ASN A 1 4266 ? 185.723 206.361 247.377 1.00 4.15  ? 4266 ASN A O     1 
ATOM   20247 C CB    . ASN A 1 4266 ? 186.689 208.654 245.237 1.00 0.00  ? 4266 ASN A CB    1 
ATOM   20248 C CG    . ASN A 1 4266 ? 187.911 209.338 244.668 1.00 0.36  ? 4266 ASN A CG    1 
ATOM   20249 O OD1   . ASN A 1 4266 ? 188.971 208.731 244.536 1.00 1.43  ? 4266 ASN A OD1   1 
ATOM   20250 N ND2   . ASN A 1 4266 ? 187.766 210.608 244.313 1.00 2.71  ? 4266 ASN A ND2   1 
ATOM   20251 N N     . THR A 1 4267 ? 184.633 206.250 245.416 1.00 0.00  ? 4267 THR A N     1 
ATOM   20252 C CA    . THR A 1 4267 ? 183.446 205.657 246.023 1.00 0.00  ? 4267 THR A CA    1 
ATOM   20253 C C     . THR A 1 4267 ? 183.776 204.324 246.679 1.00 0.00  ? 4267 THR A C     1 
ATOM   20254 O O     . THR A 1 4267 ? 183.389 204.069 247.826 1.00 5.81  ? 4267 THR A O     1 
ATOM   20255 C CB    . THR A 1 4267 ? 182.353 205.480 244.970 1.00 0.59  ? 4267 THR A CB    1 
ATOM   20256 O OG1   . THR A 1 4267 ? 181.956 206.763 244.471 1.00 6.81  ? 4267 THR A OG1   1 
ATOM   20257 C CG2   . THR A 1 4267 ? 181.149 204.781 245.565 1.00 5.30  ? 4267 THR A CG2   1 
ATOM   20258 N N     . PHE A 1 4268 ? 184.510 203.466 245.968 1.00 0.00  ? 4268 PHE A N     1 
ATOM   20259 C CA    . PHE A 1 4268 ? 184.920 202.185 246.540 1.00 0.00  ? 4268 PHE A CA    1 
ATOM   20260 C C     . PHE A 1 4268 ? 185.788 202.378 247.777 1.00 0.00  ? 4268 PHE A C     1 
ATOM   20261 O O     . PHE A 1 4268 ? 185.589 201.709 248.798 1.00 3.70  ? 4268 PHE A O     1 
ATOM   20262 C CB    . PHE A 1 4268 ? 185.660 201.352 245.494 1.00 1.91  ? 4268 PHE A CB    1 
ATOM   20263 C CG    . PHE A 1 4268 ? 184.782 200.835 244.395 1.00 4.57  ? 4268 PHE A CG    1 
ATOM   20264 C CD1   . PHE A 1 4268 ? 183.405 200.829 244.534 1.00 7.27  ? 4268 PHE A CD1   1 
ATOM   20265 C CD2   . PHE A 1 4268 ? 185.332 200.369 243.217 1.00 0.68  ? 4268 PHE A CD2   1 
ATOM   20266 C CE1   . PHE A 1 4268 ? 182.597 200.354 243.526 1.00 2.69  ? 4268 PHE A CE1   1 
ATOM   20267 C CE2   . PHE A 1 4268 ? 184.529 199.897 242.206 1.00 1.91  ? 4268 PHE A CE2   1 
ATOM   20268 C CZ    . PHE A 1 4268 ? 183.158 199.889 242.362 1.00 5.46  ? 4268 PHE A CZ    1 
ATOM   20269 N N     . LEU A 1 4269 ? 186.763 203.287 247.705 1.00 1.07  ? 4269 LEU A N     1 
ATOM   20270 C CA    . LEU A 1 4269 ? 187.670 203.467 248.835 1.00 0.00  ? 4269 LEU A CA    1 
ATOM   20271 C C     . LEU A 1 4269 ? 186.948 204.014 250.062 1.00 2.88  ? 4269 LEU A C     1 
ATOM   20272 O O     . LEU A 1 4269 ? 187.209 203.574 251.186 1.00 4.24  ? 4269 LEU A O     1 
ATOM   20273 C CB    . LEU A 1 4269 ? 188.835 204.366 248.436 1.00 0.00  ? 4269 LEU A CB    1 
ATOM   20274 C CG    . LEU A 1 4269 ? 189.771 203.663 247.459 1.00 0.00  ? 4269 LEU A CG    1 
ATOM   20275 C CD1   . LEU A 1 4269 ? 190.727 204.628 246.826 1.00 0.00  ? 4269 LEU A CD1   1 
ATOM   20276 C CD2   . LEU A 1 4269 ? 190.530 202.572 248.178 1.00 2.12  ? 4269 LEU A CD2   1 
ATOM   20277 N N     . GLU A 1 4270 ? 186.043 204.978 249.874 1.00 0.00  ? 4270 GLU A N     1 
ATOM   20278 C CA    . GLU A 1 4270 ? 185.261 205.471 251.005 1.00 0.00  ? 4270 GLU A CA    1 
ATOM   20279 C C     . GLU A 1 4270 ? 184.348 204.389 251.564 1.00 0.00  ? 4270 GLU A C     1 
ATOM   20280 O O     . GLU A 1 4270 ? 184.199 204.271 252.785 1.00 5.90  ? 4270 GLU A O     1 
ATOM   20281 C CB    . GLU A 1 4270 ? 184.442 206.701 250.611 1.00 0.00  ? 4270 GLU A CB    1 
ATOM   20282 C CG    . GLU A 1 4270 ? 185.220 207.799 249.918 1.00 4.54  ? 4270 GLU A CG    1 
ATOM   20283 C CD    . GLU A 1 4270 ? 184.314 208.807 249.239 1.00 12.43 ? 4270 GLU A CD    1 
ATOM   20284 O OE1   . GLU A 1 4270 ? 183.097 208.544 249.145 1.00 11.97 ? 4270 GLU A OE1   1 
ATOM   20285 O OE2   . GLU A 1 4270 ? 184.818 209.859 248.793 1.00 7.98  ? 4270 GLU A OE2   1 
ATOM   20286 N N     . ARG A 1 4271 ? 183.721 203.595 250.693 1.00 1.23  ? 4271 ARG A N     1 
ATOM   20287 C CA    . ARG A 1 4271 ? 182.807 202.565 251.171 1.00 0.00  ? 4271 ARG A CA    1 
ATOM   20288 C C     . ARG A 1 4271 ? 183.541 201.501 251.976 1.00 2.83  ? 4271 ARG A C     1 
ATOM   20289 O O     . ARG A 1 4271 ? 183.025 201.022 252.992 1.00 12.56 ? 4271 ARG A O     1 
ATOM   20290 C CB    . ARG A 1 4271 ? 182.064 201.937 249.994 1.00 1.00  ? 4271 ARG A CB    1 
ATOM   20291 C CG    . ARG A 1 4271 ? 180.634 201.536 250.313 1.00 3.40  ? 4271 ARG A CG    1 
ATOM   20292 C CD    . ARG A 1 4271 ? 180.096 200.492 249.342 1.00 6.47  ? 4271 ARG A CD    1 
ATOM   20293 N NE    . ARG A 1 4271 ? 180.864 199.253 249.363 1.00 12.34 ? 4271 ARG A NE    1 
ATOM   20294 C CZ    . ARG A 1 4271 ? 181.790 198.927 248.471 1.00 9.70  ? 4271 ARG A CZ    1 
ATOM   20295 N NH1   . ARG A 1 4271 ? 182.089 199.728 247.461 1.00 4.73  ? 4271 ARG A NH1   1 
ATOM   20296 N NH2   . ARG A 1 4271 ? 182.428 197.767 248.593 1.00 4.42  ? 4271 ARG A NH2   1 
ATOM   20297 N N     . LEU A 1 4272 ? 184.745 201.122 251.548 1.00 2.08  ? 4272 LEU A N     1 
ATOM   20298 C CA    . LEU A 1 4272 ? 185.463 200.032 252.204 1.00 0.00  ? 4272 LEU A CA    1 
ATOM   20299 C C     . LEU A 1 4272 ? 186.359 200.522 253.338 1.00 0.00  ? 4272 LEU A C     1 
ATOM   20300 O O     . LEU A 1 4272 ? 186.210 200.090 254.485 1.00 2.84  ? 4272 LEU A O     1 
ATOM   20301 C CB    . LEU A 1 4272 ? 186.292 199.254 251.177 1.00 0.90  ? 4272 LEU A CB    1 
ATOM   20302 C CG    . LEU A 1 4272 ? 185.513 198.442 250.145 1.00 1.19  ? 4272 LEU A CG    1 
ATOM   20303 C CD1   . LEU A 1 4272 ? 186.424 198.040 249.001 1.00 3.99  ? 4272 LEU A CD1   1 
ATOM   20304 C CD2   . LEU A 1 4272 ? 184.888 197.225 250.800 1.00 4.67  ? 4272 LEU A CD2   1 
ATOM   20305 N N     . PHE A 1 4273 ? 187.293 201.419 253.034 1.00 0.87  ? 4273 PHE A N     1 
ATOM   20306 C CA    . PHE A 1 4273 ? 188.331 201.813 253.985 1.00 0.00  ? 4273 PHE A CA    1 
ATOM   20307 C C     . PHE A 1 4273 ? 187.764 202.844 254.950 1.00 1.46  ? 4273 PHE A C     1 
ATOM   20308 O O     . PHE A 1 4273 ? 187.932 204.052 254.783 1.00 0.34  ? 4273 PHE A O     1 
ATOM   20309 C CB    . PHE A 1 4273 ? 189.553 202.340 253.247 1.00 0.00  ? 4273 PHE A CB    1 
ATOM   20310 C CG    . PHE A 1 4273 ? 190.378 201.262 252.617 1.00 0.00  ? 4273 PHE A CG    1 
ATOM   20311 C CD1   . PHE A 1 4273 ? 190.098 200.818 251.337 1.00 0.00  ? 4273 PHE A CD1   1 
ATOM   20312 C CD2   . PHE A 1 4273 ? 191.418 200.674 253.311 1.00 5.84  ? 4273 PHE A CD2   1 
ATOM   20313 C CE1   . PHE A 1 4273 ? 190.847 199.819 250.759 1.00 0.00  ? 4273 PHE A CE1   1 
ATOM   20314 C CE2   . PHE A 1 4273 ? 192.171 199.673 252.737 1.00 4.80  ? 4273 PHE A CE2   1 
ATOM   20315 C CZ    . PHE A 1 4273 ? 191.886 199.247 251.459 1.00 6.33  ? 4273 PHE A CZ    1 
ATOM   20316 N N     . THR A 1 4274 ? 187.084 202.351 255.981 1.00 3.84  ? 4274 THR A N     1 
ATOM   20317 C CA    . THR A 1 4274 ? 186.503 203.197 257.010 1.00 2.90  ? 4274 THR A CA    1 
ATOM   20318 C C     . THR A 1 4274 ? 186.512 202.429 258.322 1.00 3.55  ? 4274 THR A C     1 
ATOM   20319 O O     . THR A 1 4274 ? 186.655 201.205 258.343 1.00 11.10 ? 4274 THR A O     1 
ATOM   20320 C CB    . THR A 1 4274 ? 185.077 203.636 256.649 1.00 4.18  ? 4274 THR A CB    1 
ATOM   20321 O OG1   . THR A 1 4274 ? 184.594 204.561 257.631 1.00 6.83  ? 4274 THR A OG1   1 
ATOM   20322 C CG2   . THR A 1 4274 ? 184.147 202.437 256.591 1.00 7.22  ? 4274 THR A CG2   1 
ATOM   20323 N N     . THR A 1 4275 ? 186.369 203.167 259.425 1.00 3.15  ? 4275 THR A N     1 
ATOM   20324 C CA    . THR A 1 4275 ? 186.340 202.531 260.737 1.00 5.90  ? 4275 THR A CA    1 
ATOM   20325 C C     . THR A 1 4275 ? 185.121 201.635 260.914 1.00 11.60 ? 4275 THR A C     1 
ATOM   20326 O O     . THR A 1 4275 ? 185.139 200.744 261.769 1.00 8.30  ? 4275 THR A O     1 
ATOM   20327 C CB    . THR A 1 4275 ? 186.386 203.592 261.839 1.00 6.74  ? 4275 THR A CB    1 
ATOM   20328 O OG1   . THR A 1 4275 ? 186.467 202.953 263.118 1.00 13.54 ? 4275 THR A OG1   1 
ATOM   20329 C CG2   . THR A 1 4275 ? 185.146 204.471 261.789 1.00 10.96 ? 4275 THR A CG2   1 
ATOM   20330 N N     . ARG A 1 4276 ? 184.069 201.845 260.120 1.00 7.91  ? 4276 ARG A N     1 
ATOM   20331 C CA    . ARG A 1 4276 ? 182.906 200.970 260.165 1.00 5.91  ? 4276 ARG A CA    1 
ATOM   20332 C C     . ARG A 1 4276 ? 183.191 199.593 259.582 1.00 9.51  ? 4276 ARG A C     1 
ATOM   20333 O O     . ARG A 1 4276 ? 182.396 198.672 259.787 1.00 17.46 ? 4276 ARG A O     1 
ATOM   20334 C CB    . ARG A 1 4276 ? 181.735 201.617 259.425 1.00 8.23  ? 4276 ARG A CB    1 
ATOM   20335 C CG    . ARG A 1 4276 ? 181.183 202.874 260.083 1.00 12.85 ? 4276 ARG A CG    1 
ATOM   20336 C CD    . ARG A 1 4276 ? 180.902 202.663 261.568 1.00 16.96 ? 4276 ARG A CD    1 
ATOM   20337 N NE    . ARG A 1 4276 ? 181.941 203.210 262.432 1.00 14.54 ? 4276 ARG A NE    1 
ATOM   20338 C CZ    . ARG A 1 4276 ? 182.398 202.610 263.523 1.00 16.07 ? 4276 ARG A CZ    1 
ATOM   20339 N NH1   . ARG A 1 4276 ? 181.944 201.427 263.903 1.00 9.62  ? 4276 ARG A NH1   1 
ATOM   20340 N NH2   . ARG A 1 4276 ? 183.334 203.212 264.252 1.00 13.92 ? 4276 ARG A NH2   1 
ATOM   20341 N N     . SER A 1 4277 ? 184.302 199.432 258.860 1.00 8.20  ? 4277 SER A N     1 
ATOM   20342 C CA    . SER A 1 4277 ? 184.632 198.138 258.276 1.00 4.33  ? 4277 SER A CA    1 
ATOM   20343 C C     . SER A 1 4277 ? 185.076 197.125 259.320 1.00 10.88 ? 4277 SER A C     1 
ATOM   20344 O O     . SER A 1 4277 ? 185.202 195.939 258.999 1.00 20.83 ? 4277 SER A O     1 
ATOM   20345 C CB    . SER A 1 4277 ? 185.723 198.299 257.220 1.00 4.41  ? 4277 SER A CB    1 
ATOM   20346 O OG    . SER A 1 4277 ? 186.939 198.715 257.813 1.00 2.21  ? 4277 SER A OG    1 
ATOM   20347 N N     . PHE A 1 4278 ? 185.324 197.561 260.551 1.00 10.79 ? 4278 PHE A N     1 
ATOM   20348 C CA    . PHE A 1 4278 ? 185.705 196.673 261.637 1.00 11.85 ? 4278 PHE A CA    1 
ATOM   20349 C C     . PHE A 1 4278 ? 184.518 196.228 262.482 1.00 14.37 ? 4278 PHE A C     1 
ATOM   20350 O O     . PHE A 1 4278 ? 184.713 195.522 263.477 1.00 18.40 ? 4278 PHE A O     1 
ATOM   20351 C CB    . PHE A 1 4278 ? 186.760 197.345 262.516 1.00 6.78  ? 4278 PHE A CB    1 
ATOM   20352 C CG    . PHE A 1 4278 ? 188.146 197.272 261.950 1.00 8.48  ? 4278 PHE A CG    1 
ATOM   20353 C CD1   . PHE A 1 4278 ? 188.495 198.009 260.832 1.00 12.86 ? 4278 PHE A CD1   1 
ATOM   20354 C CD2   . PHE A 1 4278 ? 189.101 196.468 262.538 1.00 7.99  ? 4278 PHE A CD2   1 
ATOM   20355 C CE1   . PHE A 1 4278 ? 189.769 197.934 260.309 1.00 8.75  ? 4278 PHE A CE1   1 
ATOM   20356 C CE2   . PHE A 1 4278 ? 190.372 196.390 262.018 1.00 11.40 ? 4278 PHE A CE2   1 
ATOM   20357 C CZ    . PHE A 1 4278 ? 190.709 197.125 260.905 1.00 10.39 ? 4278 PHE A CZ    1 
ATOM   20358 N N     . ASP A 1 4279 ? 183.302 196.620 262.114 1.00 8.25  ? 4279 ASP A N     1 
ATOM   20359 C CA    . ASP A 1 4279 ? 182.109 196.153 262.805 1.00 11.08 ? 4279 ASP A CA    1 
ATOM   20360 C C     . ASP A 1 4279 ? 181.784 194.731 262.352 1.00 17.03 ? 4279 ASP A C     1 
ATOM   20361 O O     . ASP A 1 4279 ? 182.449 194.160 261.483 1.00 22.26 ? 4279 ASP A O     1 
ATOM   20362 C CB    . ASP A 1 4279 ? 180.941 197.104 262.559 1.00 15.42 ? 4279 ASP A CB    1 
ATOM   20363 C CG    . ASP A 1 4279 ? 181.319 198.554 262.758 1.00 17.82 ? 4279 ASP A CG    1 
ATOM   20364 O OD1   . ASP A 1 4279 ? 180.746 199.417 262.061 1.00 15.43 ? 4279 ASP A OD1   1 
ATOM   20365 O OD2   . ASP A 1 4279 ? 182.188 198.833 263.609 1.00 15.79 ? 4279 ASP A OD2   1 
ATOM   20366 N N     . SER A 1 4280 ? 180.743 194.145 262.936 1.00 15.93 ? 4280 SER A N     1 
ATOM   20367 C CA    . SER A 1 4280 ? 180.323 192.794 262.588 1.00 20.40 ? 4280 SER A CA    1 
ATOM   20368 C C     . SER A 1 4280 ? 179.218 192.761 261.544 1.00 23.30 ? 4280 SER A C     1 
ATOM   20369 O O     . SER A 1 4280 ? 179.050 191.741 260.869 1.00 25.47 ? 4280 SER A O     1 
ATOM   20370 C CB    . SER A 1 4280 ? 179.850 192.049 263.841 1.00 21.95 ? 4280 SER A CB    1 
ATOM   20371 O OG    . SER A 1 4280 ? 179.006 192.869 264.631 1.00 23.42 ? 4280 SER A OG    1 
ATOM   20372 N N     . GLU A 1 4281 ? 178.467 193.849 261.393 1.00 17.93 ? 4281 GLU A N     1 
ATOM   20373 C CA    . GLU A 1 4281 ? 177.367 193.921 260.443 1.00 19.00 ? 4281 GLU A CA    1 
ATOM   20374 C C     . GLU A 1 4281 ? 177.733 194.681 259.174 1.00 19.58 ? 4281 GLU A C     1 
ATOM   20375 O O     . GLU A 1 4281 ? 176.841 195.027 258.394 1.00 22.86 ? 4281 GLU A O     1 
ATOM   20376 C CB    . GLU A 1 4281 ? 176.147 194.566 261.102 1.00 20.04 ? 4281 GLU A CB    1 
ATOM   20377 C CG    . GLU A 1 4281 ? 176.344 196.026 261.486 1.00 20.02 ? 4281 GLU A CG    1 
ATOM   20378 C CD    . GLU A 1 4281 ? 176.900 196.196 262.887 1.00 26.92 ? 4281 GLU A CD    1 
ATOM   20379 O OE1   . GLU A 1 4281 ? 177.353 195.193 263.478 1.00 24.86 ? 4281 GLU A OE1   1 
ATOM   20380 O OE2   . GLU A 1 4281 ? 176.883 197.335 263.400 1.00 24.12 ? 4281 GLU A OE2   1 
ATOM   20381 N N     . PHE A 1 4282 ? 179.017 194.948 258.951 1.00 15.05 ? 4282 PHE A N     1 
ATOM   20382 C CA    . PHE A 1 4282 ? 179.428 195.726 257.790 1.00 10.30 ? 4282 PHE A CA    1 
ATOM   20383 C C     . PHE A 1 4282 ? 179.335 194.873 256.531 1.00 12.57 ? 4282 PHE A C     1 
ATOM   20384 O O     . PHE A 1 4282 ? 179.898 193.776 256.469 1.00 17.55 ? 4282 PHE A O     1 
ATOM   20385 C CB    . PHE A 1 4282 ? 180.851 196.246 257.982 1.00 10.71 ? 4282 PHE A CB    1 
ATOM   20386 C CG    . PHE A 1 4282 ? 181.425 196.913 256.766 1.00 12.13 ? 4282 PHE A CG    1 
ATOM   20387 C CD1   . PHE A 1 4282 ? 182.469 196.335 256.068 1.00 11.70 ? 4282 PHE A CD1   1 
ATOM   20388 C CD2   . PHE A 1 4282 ? 180.928 198.128 256.329 1.00 15.00 ? 4282 PHE A CD2   1 
ATOM   20389 C CE1   . PHE A 1 4282 ? 183.002 196.951 254.954 1.00 9.08  ? 4282 PHE A CE1   1 
ATOM   20390 C CE2   . PHE A 1 4282 ? 181.456 198.747 255.215 1.00 14.07 ? 4282 PHE A CE2   1 
ATOM   20391 C CZ    . PHE A 1 4282 ? 182.494 198.157 254.527 1.00 9.70  ? 4282 PHE A CZ    1 
ATOM   20392 N N     . LYS A 1 4283 ? 178.629 195.382 255.524 1.00 10.67 ? 4283 LYS A N     1 
ATOM   20393 C CA    . LYS A 1 4283 ? 178.391 194.643 254.292 1.00 9.99  ? 4283 LYS A CA    1 
ATOM   20394 C C     . LYS A 1 4283 ? 179.463 194.980 253.265 1.00 11.61 ? 4283 LYS A C     1 
ATOM   20395 O O     . LYS A 1 4283 ? 179.668 196.153 252.937 1.00 15.50 ? 4283 LYS A O     1 
ATOM   20396 C CB    . LYS A 1 4283 ? 177.012 194.974 253.722 1.00 12.03 ? 4283 LYS A CB    1 
ATOM   20397 C CG    . LYS A 1 4283 ? 175.897 195.065 254.746 1.00 13.63 ? 4283 LYS A CG    1 
ATOM   20398 C CD    . LYS A 1 4283 ? 175.637 193.738 255.432 1.00 10.52 ? 4283 LYS A CD    1 
ATOM   20399 C CE    . LYS A 1 4283 ? 174.470 193.857 256.399 1.00 16.80 ? 4283 LYS A CE    1 
ATOM   20400 N NZ    . LYS A 1 4283 ? 174.240 192.608 257.173 1.00 16.86 ? 4283 LYS A NZ    1 
ATOM   20401 N N     . LEU A 1 4284 ? 180.144 193.950 252.756 1.00 9.90  ? 4284 LEU A N     1 
ATOM   20402 C CA    . LEU A 1 4284 ? 181.076 194.167 251.654 1.00 0.35  ? 4284 LEU A CA    1 
ATOM   20403 C C     . LEU A 1 4284 ? 180.336 194.601 250.397 1.00 11.40 ? 4284 LEU A C     1 
ATOM   20404 O O     . LEU A 1 4284 ? 180.820 195.453 249.644 1.00 19.33 ? 4284 LEU A O     1 
ATOM   20405 C CB    . LEU A 1 4284 ? 181.893 192.904 251.378 1.00 0.00  ? 4284 LEU A CB    1 
ATOM   20406 C CG    . LEU A 1 4284 ? 183.146 192.618 252.212 1.00 1.62  ? 4284 LEU A CG    1 
ATOM   20407 C CD1   . LEU A 1 4284 ? 184.157 193.734 252.061 1.00 7.37  ? 4284 LEU A CD1   1 
ATOM   20408 C CD2   . LEU A 1 4284 ? 182.812 192.402 253.666 1.00 15.07 ? 4284 LEU A CD2   1 
ATOM   20409 N N     . ALA A 1 4285 ? 179.163 194.023 250.152 1.00 14.27 ? 4285 ALA A N     1 
ATOM   20410 C CA    . ALA A 1 4285 ? 178.362 194.379 248.984 1.00 14.32 ? 4285 ALA A CA    1 
ATOM   20411 C C     . ALA A 1 4285 ? 176.899 194.141 249.314 1.00 18.64 ? 4285 ALA A C     1 
ATOM   20412 O O     . ALA A 1 4285 ? 176.537 193.049 249.762 1.00 20.77 ? 4285 ALA A O     1 
ATOM   20413 C CB    . ALA A 1 4285 ? 178.781 193.565 247.763 1.00 8.64  ? 4285 ALA A CB    1 
ATOM   20414 N N     . CYS A 1 4286 ? 176.067 195.157 249.106 1.00 22.54 ? 4286 CYS A N     1 
ATOM   20415 C CA    . CYS A 1 4286 ? 174.635 195.026 249.314 1.00 24.66 ? 4286 CYS A CA    1 
ATOM   20416 C C     . CYS A 1 4286 ? 173.930 194.807 247.977 1.00 27.25 ? 4286 CYS A C     1 
ATOM   20417 O O     . CYS A 1 4286 ? 174.541 194.846 246.906 1.00 27.34 ? 4286 CYS A O     1 
ATOM   20418 C CB    . CYS A 1 4286 ? 174.089 196.255 250.036 1.00 27.44 ? 4286 CYS A CB    1 
ATOM   20419 S SG    . CYS A 1 4286 ? 174.495 197.826 249.241 1.00 39.81 ? 4286 CYS A SG    1 
ATOM   20420 N N     . LYS A 1 4287 ? 172.620 194.566 248.043 1.00 29.82 ? 4287 LYS A N     1 
ATOM   20421 C CA    . LYS A 1 4287 ? 171.759 194.329 246.887 1.00 27.79 ? 4287 LYS A CA    1 
ATOM   20422 C C     . LYS A 1 4287 ? 172.225 193.164 246.023 1.00 26.50 ? 4287 LYS A C     1 
ATOM   20423 O O     . LYS A 1 4287 ? 171.781 193.034 244.877 1.00 26.70 ? 4287 LYS A O     1 
ATOM   20424 C CB    . LYS A 1 4287 ? 171.619 195.584 246.013 1.00 24.07 ? 4287 LYS A CB    1 
ATOM   20425 C CG    . LYS A 1 4287 ? 171.589 196.899 246.772 1.00 25.65 ? 4287 LYS A CG    1 
ATOM   20426 C CD    . LYS A 1 4287 ? 171.885 198.064 245.840 1.00 30.02 ? 4287 LYS A CD    1 
ATOM   20427 C CE    . LYS A 1 4287 ? 170.730 198.317 244.886 1.00 30.80 ? 4287 LYS A CE    1 
ATOM   20428 N NZ    . LYS A 1 4287 ? 171.036 199.409 243.921 1.00 23.18 ? 4287 LYS A NZ    1 
ATOM   20429 N N     . VAL A 1 4288 ? 173.110 192.310 246.539 1.00 24.99 ? 4288 VAL A N     1 
ATOM   20430 C CA    . VAL A 1 4288 ? 173.668 191.238 245.728 1.00 24.32 ? 4288 VAL A CA    1 
ATOM   20431 C C     . VAL A 1 4288 ? 172.646 190.122 245.556 1.00 26.97 ? 4288 VAL A C     1 
ATOM   20432 O O     . VAL A 1 4288 ? 172.005 189.681 246.521 1.00 32.49 ? 4288 VAL A O     1 
ATOM   20433 C CB    . VAL A 1 4288 ? 174.980 190.724 246.346 1.00 19.61 ? 4288 VAL A CB    1 
ATOM   20434 C CG1   . VAL A 1 4288 ? 174.747 190.136 247.724 1.00 23.63 ? 4288 VAL A CG1   1 
ATOM   20435 C CG2   . VAL A 1 4288 ? 175.587 189.686 245.450 1.00 18.72 ? 4288 VAL A CG2   1 
ATOM   20436 N N     . ASP A 1 4289 ? 172.477 189.676 244.309 1.00 25.49 ? 4289 ASP A N     1 
ATOM   20437 C CA    . ASP A 1 4289 ? 171.545 188.601 243.966 1.00 27.15 ? 4289 ASP A CA    1 
ATOM   20438 C C     . ASP A 1 4289 ? 170.151 188.879 244.523 1.00 33.19 ? 4289 ASP A C     1 
ATOM   20439 O O     . ASP A 1 4289 ? 169.535 188.035 245.178 1.00 29.97 ? 4289 ASP A O     1 
ATOM   20440 C CB    . ASP A 1 4289 ? 172.072 187.246 244.441 1.00 25.27 ? 4289 ASP A CB    1 
ATOM   20441 N N     . GLY A 1 4290 ? 169.654 190.084 244.257 1.00 35.18 ? 4290 GLY A N     1 
ATOM   20442 C CA    . GLY A 1 4290 ? 168.337 190.500 244.696 1.00 35.14 ? 4290 GLY A CA    1 
ATOM   20443 C C     . GLY A 1 4290 ? 168.303 191.235 246.021 1.00 37.83 ? 4290 GLY A C     1 
ATOM   20444 O O     . GLY A 1 4290 ? 168.149 192.460 246.040 1.00 39.33 ? 4290 GLY A O     1 
ATOM   20445 N N     . HIS A 1 4291 ? 168.449 190.517 247.139 1.00 34.74 ? 4291 HIS A N     1 
ATOM   20446 C CA    . HIS A 1 4291 ? 168.342 191.157 248.443 1.00 36.85 ? 4291 HIS A CA    1 
ATOM   20447 C C     . HIS A 1 4291 ? 169.335 190.658 249.484 1.00 36.46 ? 4291 HIS A C     1 
ATOM   20448 O O     . HIS A 1 4291 ? 169.271 191.116 250.629 1.00 36.21 ? 4291 HIS A O     1 
ATOM   20449 C CB    . HIS A 1 4291 ? 166.918 190.993 248.997 1.00 35.14 ? 4291 HIS A CB    1 
ATOM   20450 C CG    . HIS A 1 4291 ? 166.486 189.568 249.138 1.00 38.28 ? 4291 HIS A CG    1 
ATOM   20451 N ND1   . HIS A 1 4291 ? 166.030 188.818 248.075 1.00 39.08 ? 4291 HIS A ND1   1 
ATOM   20452 C CD2   . HIS A 1 4291 ? 166.444 188.752 250.219 1.00 37.54 ? 4291 HIS A CD2   1 
ATOM   20453 C CE1   . HIS A 1 4291 ? 165.724 187.604 248.494 1.00 37.02 ? 4291 HIS A CE1   1 
ATOM   20454 N NE2   . HIS A 1 4291 ? 165.966 187.537 249.791 1.00 36.54 ? 4291 HIS A NE2   1 
ATOM   20455 N N     . LYS A 1 4292 ? 170.244 189.749 249.141 1.00 31.80 ? 4292 LYS A N     1 
ATOM   20456 C CA    . LYS A 1 4292 ? 171.194 189.251 250.124 1.00 29.76 ? 4292 LYS A CA    1 
ATOM   20457 C C     . LYS A 1 4292 ? 172.378 190.208 250.251 1.00 31.02 ? 4292 LYS A C     1 
ATOM   20458 O O     . LYS A 1 4292 ? 172.425 191.277 249.635 1.00 29.56 ? 4292 LYS A O     1 
ATOM   20459 C CB    . LYS A 1 4292 ? 171.647 187.839 249.762 1.00 28.29 ? 4292 LYS A CB    1 
ATOM   20460 C CG    . LYS A 1 4292 ? 170.541 186.796 249.865 1.00 31.22 ? 4292 LYS A CG    1 
ATOM   20461 C CD    . LYS A 1 4292 ? 170.981 185.444 249.325 1.00 32.12 ? 4292 LYS A CD    1 
ATOM   20462 C CE    . LYS A 1 4292 ? 171.372 185.526 247.859 1.00 31.61 ? 4292 LYS A CE    1 
ATOM   20463 N NZ    . LYS A 1 4292 ? 170.476 186.452 247.113 1.00 30.05 ? 4292 LYS A NZ    1 
ATOM   20464 N N     . ASP A 1 4293 ? 173.348 189.816 251.074 1.00 22.70 ? 4293 ASP A N     1 
ATOM   20465 C CA    . ASP A 1 4293 ? 174.485 190.667 251.388 1.00 19.66 ? 4293 ASP A CA    1 
ATOM   20466 C C     . ASP A 1 4293 ? 175.714 189.791 251.583 1.00 19.59 ? 4293 ASP A C     1 
ATOM   20467 O O     . ASP A 1 4293 ? 175.612 188.580 251.789 1.00 23.51 ? 4293 ASP A O     1 
ATOM   20468 C CB    . ASP A 1 4293 ? 174.226 191.510 252.643 1.00 22.37 ? 4293 ASP A CB    1 
ATOM   20469 C CG    . ASP A 1 4293 ? 173.071 192.479 252.472 1.00 24.22 ? 4293 ASP A CG    1 
ATOM   20470 O OD1   . ASP A 1 4293 ? 173.259 193.522 251.814 1.00 22.74 ? 4293 ASP A OD1   1 
ATOM   20471 O OD2   . ASP A 1 4293 ? 171.978 192.201 253.007 1.00 23.91 ? 4293 ASP A OD2   1 
ATOM   20472 N N     . ILE A 1 4294 ? 176.885 190.420 251.518 1.00 15.86 ? 4294 ILE A N     1 
ATOM   20473 C CA    . ILE A 1 4294 ? 178.156 189.760 251.796 1.00 16.13 ? 4294 ILE A CA    1 
ATOM   20474 C C     . ILE A 1 4294 ? 178.737 190.372 253.063 1.00 11.25 ? 4294 ILE A C     1 
ATOM   20475 O O     . ILE A 1 4294 ? 179.141 191.540 253.064 1.00 13.88 ? 4294 ILE A O     1 
ATOM   20476 C CB    . ILE A 1 4294 ? 179.143 189.895 250.621 1.00 13.64 ? 4294 ILE A CB    1 
ATOM   20477 C CG1   . ILE A 1 4294 ? 178.555 189.282 249.350 1.00 6.60  ? 4294 ILE A CG1   1 
ATOM   20478 C CG2   . ILE A 1 4294 ? 180.467 189.229 250.957 1.00 9.42  ? 4294 ILE A CG2   1 
ATOM   20479 C CD1   . ILE A 1 4294 ? 179.518 189.276 248.187 1.00 7.04  ? 4294 ILE A CD1   1 
ATOM   20480 N N     . GLN A 1 4295 ? 178.795 189.581 254.129 1.00 9.60  ? 4295 GLN A N     1 
ATOM   20481 C CA    . GLN A 1 4295 ? 179.209 190.054 255.442 1.00 8.49  ? 4295 GLN A CA    1 
ATOM   20482 C C     . GLN A 1 4295 ? 180.726 190.054 255.580 1.00 7.75  ? 4295 GLN A C     1 
ATOM   20483 O O     . GLN A 1 4295 ? 181.443 189.333 254.883 1.00 11.95 ? 4295 GLN A O     1 
ATOM   20484 C CB    . GLN A 1 4295 ? 178.599 189.187 256.549 1.00 14.62 ? 4295 GLN A CB    1 
ATOM   20485 C CG    . GLN A 1 4295 ? 177.097 188.999 256.470 1.00 17.81 ? 4295 GLN A CG    1 
ATOM   20486 C CD    . GLN A 1 4295 ? 176.338 190.301 256.598 1.00 16.56 ? 4295 GLN A CD    1 
ATOM   20487 O OE1   . GLN A 1 4295 ? 175.392 190.555 255.855 1.00 17.52 ? 4295 GLN A OE1   1 
ATOM   20488 N NE2   . GLN A 1 4295 ? 176.740 191.129 257.556 1.00 11.99 ? 4295 GLN A NE2   1 
ATOM   20489 N N     . MET A 1 4296 ? 181.201 190.876 256.505 1.00 8.29  ? 4296 MET A N     1 
ATOM   20490 C CA    . MET A 1 4296 ? 182.615 190.893 256.858 1.00 10.62 ? 4296 MET A CA    1 
ATOM   20491 C C     . MET A 1 4296 ? 182.964 189.681 257.713 1.00 9.14  ? 4296 MET A C     1 
ATOM   20492 O O     . MET A 1 4296 ? 182.186 189.310 258.599 1.00 12.06 ? 4296 MET A O     1 
ATOM   20493 C CB    . MET A 1 4296 ? 182.945 192.185 257.604 1.00 14.77 ? 4296 MET A CB    1 
ATOM   20494 C CG    . MET A 1 4296 ? 184.417 192.384 257.942 1.00 15.95 ? 4296 MET A CG    1 
ATOM   20495 S SD    . MET A 1 4296 ? 185.539 192.537 256.545 1.00 12.37 ? 4296 MET A SD    1 
ATOM   20496 C CE    . MET A 1 4296 ? 185.141 194.162 255.927 1.00 4.90  ? 4296 MET A CE    1 
ATOM   20497 N N     . PRO A 1 4297 ? 184.110 189.039 257.485 1.00 6.04  ? 4297 PRO A N     1 
ATOM   20498 C CA    . PRO A 1 4297 ? 184.551 187.966 258.389 1.00 15.26 ? 4297 PRO A CA    1 
ATOM   20499 C C     . PRO A 1 4297 ? 185.111 188.546 259.680 1.00 15.17 ? 4297 PRO A C     1 
ATOM   20500 O O     . PRO A 1 4297 ? 186.085 189.300 259.665 1.00 13.50 ? 4297 PRO A O     1 
ATOM   20501 C CB    . PRO A 1 4297 ? 185.631 187.241 257.579 1.00 13.71 ? 4297 PRO A CB    1 
ATOM   20502 C CG    . PRO A 1 4297 ? 186.123 188.256 256.616 1.00 9.58  ? 4297 PRO A CG    1 
ATOM   20503 C CD    . PRO A 1 4297 ? 184.952 189.128 256.281 1.00 7.47  ? 4297 PRO A CD    1 
ATOM   20504 N N     . ASP A 1 4298 ? 184.495 188.177 260.802 1.00 22.41 ? 4298 ASP A N     1 
ATOM   20505 C CA    . ASP A 1 4298 ? 184.949 188.652 262.103 1.00 18.37 ? 4298 ASP A CA    1 
ATOM   20506 C C     . ASP A 1 4298 ? 186.237 187.943 262.497 1.00 21.79 ? 4298 ASP A C     1 
ATOM   20507 O O     . ASP A 1 4298 ? 186.244 187.117 263.415 1.00 24.08 ? 4298 ASP A O     1 
ATOM   20508 C CB    . ASP A 1 4298 ? 183.871 188.434 263.165 1.00 17.28 ? 4298 ASP A CB    1 
ATOM   20509 C CG    . ASP A 1 4298 ? 184.029 189.363 264.352 1.00 22.34 ? 4298 ASP A CG    1 
ATOM   20510 O OD1   . ASP A 1 4298 ? 184.529 188.910 265.404 1.00 20.58 ? 4298 ASP A OD1   1 
ATOM   20511 O OD2   . ASP A 1 4298 ? 183.657 190.548 264.232 1.00 25.37 ? 4298 ASP A OD2   1 
ATOM   20512 N N     . GLY A 1 4299 ? 187.329 188.264 261.811 1.00 18.90 ? 4299 GLY A N     1 
ATOM   20513 C CA    . GLY A 1 4299 ? 188.581 187.570 262.025 1.00 18.35 ? 4299 GLY A CA    1 
ATOM   20514 C C     . GLY A 1 4299 ? 189.703 188.425 262.573 1.00 16.35 ? 4299 GLY A C     1 
ATOM   20515 O O     . GLY A 1 4299 ? 189.701 189.650 262.428 1.00 14.90 ? 4299 GLY A O     1 
ATOM   20516 N N     . ILE A 1 4300 ? 190.670 187.774 263.212 1.00 16.44 ? 4300 ILE A N     1 
ATOM   20517 C CA    . ILE A 1 4300 ? 191.850 188.452 263.729 1.00 17.12 ? 4300 ILE A CA    1 
ATOM   20518 C C     . ILE A 1 4300 ? 193.136 187.966 263.073 1.00 18.24 ? 4300 ILE A C     1 
ATOM   20519 O O     . ILE A 1 4300 ? 194.100 188.744 262.974 1.00 22.34 ? 4300 ILE A O     1 
ATOM   20520 C CB    . ILE A 1 4300 ? 191.936 188.294 265.264 1.00 18.56 ? 4300 ILE A CB    1 
ATOM   20521 C CG1   . ILE A 1 4300 ? 190.668 188.834 265.926 1.00 19.67 ? 4300 ILE A CG1   1 
ATOM   20522 C CG2   . ILE A 1 4300 ? 193.142 189.015 265.831 1.00 16.49 ? 4300 ILE A CG2   1 
ATOM   20523 C CD1   . ILE A 1 4300 ? 190.421 190.300 265.672 1.00 20.78 ? 4300 ILE A CD1   1 
ATOM   20524 N N     . ARG A 1 4301 ? 193.179 186.730 262.586 1.00 13.40 ? 4301 ARG A N     1 
ATOM   20525 C CA    . ARG A 1 4301 ? 194.349 186.144 261.954 1.00 14.80 ? 4301 ARG A CA    1 
ATOM   20526 C C     . ARG A 1 4301 ? 194.066 185.937 260.470 1.00 17.66 ? 4301 ARG A C     1 
ATOM   20527 O O     . ARG A 1 4301 ? 192.911 185.833 260.049 1.00 17.34 ? 4301 ARG A O     1 
ATOM   20528 C CB    . ARG A 1 4301 ? 194.719 184.813 262.636 1.00 19.95 ? 4301 ARG A CB    1 
ATOM   20529 C CG    . ARG A 1 4301 ? 195.915 184.081 262.047 1.00 21.32 ? 4301 ARG A CG    1 
ATOM   20530 C CD    . ARG A 1 4301 ? 197.223 184.684 262.512 1.00 20.19 ? 4301 ARG A CD    1 
ATOM   20531 N NE    . ARG A 1 4301 ? 198.356 184.102 261.805 1.00 22.56 ? 4301 ARG A NE    1 
ATOM   20532 C CZ    . ARG A 1 4301 ? 198.895 184.619 260.710 1.00 22.34 ? 4301 ARG A CZ    1 
ATOM   20533 N NH1   . ARG A 1 4301 ? 198.431 185.735 260.172 1.00 20.09 ? 4301 ARG A NH1   1 
ATOM   20534 N NH2   . ARG A 1 4301 ? 199.926 184.002 260.140 1.00 18.10 ? 4301 ARG A NH2   1 
ATOM   20535 N N     . ARG A 1 4302 ? 195.139 185.892 259.671 1.00 16.38 ? 4302 ARG A N     1 
ATOM   20536 C CA    . ARG A 1 4302 ? 194.986 185.657 258.238 1.00 11.61 ? 4302 ARG A CA    1 
ATOM   20537 C C     . ARG A 1 4302 ? 194.275 184.341 257.955 1.00 15.54 ? 4302 ARG A C     1 
ATOM   20538 O O     . ARG A 1 4302 ? 193.634 184.198 256.908 1.00 16.71 ? 4302 ARG A O     1 
ATOM   20539 C CB    . ARG A 1 4302 ? 196.349 185.667 257.542 1.00 7.86  ? 4302 ARG A CB    1 
ATOM   20540 C CG    . ARG A 1 4302 ? 197.016 184.299 257.490 1.00 19.53 ? 4302 ARG A CG    1 
ATOM   20541 C CD    . ARG A 1 4302 ? 198.415 184.346 256.907 1.00 18.51 ? 4302 ARG A CD    1 
ATOM   20542 N NE    . ARG A 1 4302 ? 198.431 184.868 255.547 1.00 17.51 ? 4302 ARG A NE    1 
ATOM   20543 C CZ    . ARG A 1 4302 ? 198.425 184.114 254.457 1.00 15.66 ? 4302 ARG A CZ    1 
ATOM   20544 N NH1   . ARG A 1 4302 ? 198.387 182.794 254.530 1.00 17.88 ? 4302 ARG A NH1   1 
ATOM   20545 N NH2   . ARG A 1 4302 ? 198.460 184.699 253.263 1.00 13.49 ? 4302 ARG A NH2   1 
ATOM   20546 N N     . GLU A 1 4303 ? 194.375 183.372 258.868 1.00 17.40 ? 4303 GLU A N     1 
ATOM   20547 C CA    . GLU A 1 4303 ? 193.766 182.068 258.630 1.00 15.43 ? 4303 GLU A CA    1 
ATOM   20548 C C     . GLU A 1 4303 ? 192.254 182.177 258.508 1.00 14.55 ? 4303 GLU A C     1 
ATOM   20549 O O     . GLU A 1 4303 ? 191.650 181.556 257.627 1.00 15.29 ? 4303 GLU A O     1 
ATOM   20550 C CB    . GLU A 1 4303 ? 194.144 181.099 259.749 1.00 14.46 ? 4303 GLU A CB    1 
ATOM   20551 C CG    . GLU A 1 4303 ? 193.960 179.636 259.381 1.00 15.15 ? 4303 GLU A CG    1 
ATOM   20552 C CD    . GLU A 1 4303 ? 194.526 179.301 258.015 1.00 22.20 ? 4303 GLU A CD    1 
ATOM   20553 O OE1   . GLU A 1 4303 ? 195.726 179.561 257.786 1.00 25.27 ? 4303 GLU A OE1   1 
ATOM   20554 O OE2   . GLU A 1 4303 ? 193.770 178.780 257.168 1.00 21.47 ? 4303 GLU A OE2   1 
ATOM   20555 N N     . GLU A 1 4304 ? 191.623 182.969 259.376 1.00 11.75 ? 4304 GLU A N     1 
ATOM   20556 C CA    . GLU A 1 4304 ? 190.169 183.066 259.347 1.00 14.83 ? 4304 GLU A CA    1 
ATOM   20557 C C     . GLU A 1 4304 ? 189.691 183.825 258.115 1.00 14.42 ? 4304 GLU A C     1 
ATOM   20558 O O     . GLU A 1 4304 ? 188.667 183.472 257.521 1.00 14.11 ? 4304 GLU A O     1 
ATOM   20559 C CB    . GLU A 1 4304 ? 189.666 183.715 260.636 1.00 16.64 ? 4304 GLU A CB    1 
ATOM   20560 C CG    . GLU A 1 4304 ? 188.296 183.221 261.070 1.00 17.77 ? 4304 GLU A CG    1 
ATOM   20561 C CD    . GLU A 1 4304 ? 187.971 183.583 262.504 1.00 21.77 ? 4304 GLU A CD    1 
ATOM   20562 O OE1   . GLU A 1 4304 ? 187.217 182.828 263.151 1.00 23.87 ? 4304 GLU A OE1   1 
ATOM   20563 O OE2   . GLU A 1 4304 ? 188.485 184.609 262.992 1.00 18.15 ? 4304 GLU A OE2   1 
ATOM   20564 N N     . PHE A 1 4305 ? 190.432 184.856 257.700 1.00 12.94 ? 4305 PHE A N     1 
ATOM   20565 C CA    . PHE A 1 4305 ? 190.103 185.545 256.454 1.00 14.86 ? 4305 PHE A CA    1 
ATOM   20566 C C     . PHE A 1 4305 ? 190.240 184.617 255.253 1.00 13.91 ? 4305 PHE A C     1 
ATOM   20567 O O     . PHE A 1 4305 ? 189.387 184.618 254.357 1.00 13.88 ? 4305 PHE A O     1 
ATOM   20568 C CB    . PHE A 1 4305 ? 190.989 186.778 256.282 1.00 11.54 ? 4305 PHE A CB    1 
ATOM   20569 C CG    . PHE A 1 4305 ? 190.798 187.811 257.350 1.00 9.40  ? 4305 PHE A CG    1 
ATOM   20570 C CD1   . PHE A 1 4305 ? 189.561 188.400 257.544 1.00 9.63  ? 4305 PHE A CD1   1 
ATOM   20571 C CD2   . PHE A 1 4305 ? 191.847 188.186 258.166 1.00 7.66  ? 4305 PHE A CD2   1 
ATOM   20572 C CE1   . PHE A 1 4305 ? 189.377 189.348 258.524 1.00 5.99  ? 4305 PHE A CE1   1 
ATOM   20573 C CE2   . PHE A 1 4305 ? 191.666 189.132 259.150 1.00 9.52  ? 4305 PHE A CE2   1 
ATOM   20574 C CZ    . PHE A 1 4305 ? 190.430 189.713 259.329 1.00 9.20  ? 4305 PHE A CZ    1 
ATOM   20575 N N     . VAL A 1 4306 ? 191.305 183.813 255.218 1.00 9.75  ? 4306 VAL A N     1 
ATOM   20576 C CA    . VAL A 1 4306 ? 191.477 182.870 254.118 1.00 8.02  ? 4306 VAL A CA    1 
ATOM   20577 C C     . VAL A 1 4306 ? 190.347 181.849 254.106 1.00 9.43  ? 4306 VAL A C     1 
ATOM   20578 O O     . VAL A 1 4306 ? 189.785 181.543 253.049 1.00 8.46  ? 4306 VAL A O     1 
ATOM   20579 C CB    . VAL A 1 4306 ? 192.857 182.194 254.199 1.00 16.09 ? 4306 VAL A CB    1 
ATOM   20580 C CG1   . VAL A 1 4306 ? 192.942 181.048 253.209 1.00 15.93 ? 4306 VAL A CG1   1 
ATOM   20581 C CG2   . VAL A 1 4306 ? 193.953 183.206 253.918 1.00 12.74 ? 4306 VAL A CG2   1 
ATOM   20582 N N     . GLN A 1 4307 ? 189.985 181.313 255.275 1.00 10.90 ? 4307 GLN A N     1 
ATOM   20583 C CA    . GLN A 1 4307 ? 188.898 180.340 255.324 1.00 11.62 ? 4307 GLN A CA    1 
ATOM   20584 C C     . GLN A 1 4307 ? 187.578 180.969 254.900 1.00 7.90  ? 4307 GLN A C     1 
ATOM   20585 O O     . GLN A 1 4307 ? 186.750 180.314 254.258 1.00 11.37 ? 4307 GLN A O     1 
ATOM   20586 C CB    . GLN A 1 4307 ? 188.777 179.729 256.720 1.00 11.95 ? 4307 GLN A CB    1 
ATOM   20587 C CG    . GLN A 1 4307 ? 189.917 178.797 257.100 1.00 7.94  ? 4307 GLN A CG    1 
ATOM   20588 C CD    . GLN A 1 4307 ? 190.208 178.801 258.588 1.00 14.00 ? 4307 GLN A CD    1 
ATOM   20589 O OE1   . GLN A 1 4307 ? 190.201 179.847 259.234 1.00 16.59 ? 4307 GLN A OE1   1 
ATOM   20590 N NE2   . GLN A 1 4307 ? 190.467 177.621 259.141 1.00 10.80 ? 4307 GLN A NE2   1 
ATOM   20591 N N     . TRP A 1 4308 ? 187.358 182.237 255.252 1.00 3.20  ? 4308 TRP A N     1 
ATOM   20592 C CA    . TRP A 1 4308 ? 186.170 182.933 254.772 1.00 8.58  ? 4308 TRP A CA    1 
ATOM   20593 C C     . TRP A 1 4308 ? 186.182 183.061 253.256 1.00 6.60  ? 4308 TRP A C     1 
ATOM   20594 O O     . TRP A 1 4308 ? 185.143 182.908 252.605 1.00 3.38  ? 4308 TRP A O     1 
ATOM   20595 C CB    . TRP A 1 4308 ? 186.069 184.316 255.409 1.00 15.32 ? 4308 TRP A CB    1 
ATOM   20596 C CG    . TRP A 1 4308 ? 184.824 185.047 255.019 1.00 13.26 ? 4308 TRP A CG    1 
ATOM   20597 C CD1   . TRP A 1 4308 ? 183.602 184.959 255.614 1.00 11.42 ? 4308 TRP A CD1   1 
ATOM   20598 C CD2   . TRP A 1 4308 ? 184.672 185.954 253.921 1.00 5.03  ? 4308 TRP A CD2   1 
ATOM   20599 N NE1   . TRP A 1 4308 ? 182.701 185.768 254.967 1.00 8.73  ? 4308 TRP A NE1   1 
ATOM   20600 C CE2   . TRP A 1 4308 ? 183.334 186.389 253.923 1.00 5.92  ? 4308 TRP A CE2   1 
ATOM   20601 C CE3   . TRP A 1 4308 ? 185.540 186.446 252.943 1.00 3.28  ? 4308 TRP A CE3   1 
ATOM   20602 C CZ2   . TRP A 1 4308 ? 182.843 187.291 252.985 1.00 8.70  ? 4308 TRP A CZ2   1 
ATOM   20603 C CZ3   . TRP A 1 4308 ? 185.050 187.340 252.013 1.00 4.47  ? 4308 TRP A CZ3   1 
ATOM   20604 C CH2   . TRP A 1 4308 ? 183.714 187.754 252.041 1.00 8.82  ? 4308 TRP A CH2   1 
ATOM   20605 N N     . VAL A 1 4309 ? 187.347 183.359 252.679 1.00 9.35  ? 4309 VAL A N     1 
ATOM   20606 C CA    . VAL A 1 4309 ? 187.428 183.557 251.235 1.00 3.35  ? 4309 VAL A CA    1 
ATOM   20607 C C     . VAL A 1 4309 ? 187.176 182.242 250.504 1.00 2.13  ? 4309 VAL A C     1 
ATOM   20608 O O     . VAL A 1 4309 ? 186.446 182.197 249.507 1.00 4.71  ? 4309 VAL A O     1 
ATOM   20609 C CB    . VAL A 1 4309 ? 188.784 184.174 250.852 1.00 0.38  ? 4309 VAL A CB    1 
ATOM   20610 C CG1   . VAL A 1 4309 ? 188.992 184.098 249.358 1.00 1.24  ? 4309 VAL A CG1   1 
ATOM   20611 C CG2   . VAL A 1 4309 ? 188.865 185.610 251.326 1.00 5.53  ? 4309 VAL A CG2   1 
ATOM   20612 N N     . GLU A 1 4310 ? 187.769 181.148 250.992 1.00 8.77  ? 4310 GLU A N     1 
ATOM   20613 C CA    . GLU A 1 4310 ? 187.529 179.846 250.373 1.00 7.05  ? 4310 GLU A CA    1 
ATOM   20614 C C     . GLU A 1 4310 ? 186.125 179.319 250.636 1.00 4.70  ? 4310 GLU A C     1 
ATOM   20615 O O     . GLU A 1 4310 ? 185.697 178.379 249.959 1.00 4.20  ? 4310 GLU A O     1 
ATOM   20616 C CB    . GLU A 1 4310 ? 188.558 178.816 250.841 1.00 5.30  ? 4310 GLU A CB    1 
ATOM   20617 C CG    . GLU A 1 4310 ? 189.971 179.343 250.963 1.00 11.69 ? 4310 GLU A CG    1 
ATOM   20618 C CD    . GLU A 1 4310 ? 191.000 178.234 251.049 1.00 14.42 ? 4310 GLU A CD    1 
ATOM   20619 O OE1   . GLU A 1 4310 ? 191.353 177.668 249.993 1.00 9.86  ? 4310 GLU A OE1   1 
ATOM   20620 O OE2   . GLU A 1 4310 ? 191.457 177.929 252.170 1.00 9.60  ? 4310 GLU A OE2   1 
ATOM   20621 N N     . LEU A 1 4311 ? 185.403 179.890 251.595 1.00 3.90  ? 4311 LEU A N     1 
ATOM   20622 C CA    . LEU A 1 4311 ? 184.009 179.527 251.809 1.00 1.97  ? 4311 LEU A CA    1 
ATOM   20623 C C     . LEU A 1 4311 ? 183.049 180.367 250.981 1.00 4.85  ? 4311 LEU A C     1 
ATOM   20624 O O     . LEU A 1 4311 ? 181.832 180.228 251.144 1.00 4.02  ? 4311 LEU A O     1 
ATOM   20625 C CB    . LEU A 1 4311 ? 183.645 179.644 253.291 1.00 7.17  ? 4311 LEU A CB    1 
ATOM   20626 C CG    . LEU A 1 4311 ? 183.621 178.350 254.107 1.00 9.49  ? 4311 LEU A CG    1 
ATOM   20627 C CD1   . LEU A 1 4311 ? 184.993 177.696 254.174 1.00 9.12  ? 4311 LEU A CD1   1 
ATOM   20628 C CD2   . LEU A 1 4311 ? 183.080 178.619 255.502 1.00 7.30  ? 4311 LEU A CD2   1 
ATOM   20629 N N     . LEU A 1 4312 ? 183.560 181.233 250.114 1.00 7.49  ? 4312 LEU A N     1 
ATOM   20630 C CA    . LEU A 1 4312 ? 182.692 182.034 249.267 1.00 8.10  ? 4312 LEU A CA    1 
ATOM   20631 C C     . LEU A 1 4312 ? 181.930 181.128 248.303 1.00 7.56  ? 4312 LEU A C     1 
ATOM   20632 O O     . LEU A 1 4312 ? 182.474 180.121 247.834 1.00 9.94  ? 4312 LEU A O     1 
ATOM   20633 C CB    . LEU A 1 4312 ? 183.507 183.064 248.484 1.00 9.72  ? 4312 LEU A CB    1 
ATOM   20634 C CG    . LEU A 1 4312 ? 183.733 184.428 249.136 1.00 2.60  ? 4312 LEU A CG    1 
ATOM   20635 C CD1   . LEU A 1 4312 ? 184.804 185.197 248.387 1.00 0.00  ? 4312 LEU A CD1   1 
ATOM   20636 C CD2   . LEU A 1 4312 ? 182.442 185.223 249.188 1.00 1.27  ? 4312 LEU A CD2   1 
ATOM   20637 N N     . PRO A 1 4313 ? 180.673 181.443 247.997 1.00 4.70  ? 4313 PRO A N     1 
ATOM   20638 C CA    . PRO A 1 4313 ? 179.920 180.622 247.045 1.00 6.54  ? 4313 PRO A CA    1 
ATOM   20639 C C     . PRO A 1 4313 ? 180.557 180.639 245.664 1.00 9.85  ? 4313 PRO A C     1 
ATOM   20640 O O     . PRO A 1 4313 ? 181.163 181.627 245.245 1.00 10.81 ? 4313 PRO A O     1 
ATOM   20641 C CB    . PRO A 1 4313 ? 178.535 181.278 247.029 1.00 8.17  ? 4313 PRO A CB    1 
ATOM   20642 C CG    . PRO A 1 4313 ? 178.452 182.014 248.326 1.00 11.80 ? 4313 PRO A CG    1 
ATOM   20643 C CD    . PRO A 1 4313 ? 179.841 182.500 248.592 1.00 7.13  ? 4313 PRO A CD    1 
ATOM   20644 N N     . ASP A 1 4314 ? 180.420 179.514 244.959 1.00 14.15 ? 4314 ASP A N     1 
ATOM   20645 C CA    . ASP A 1 4314 ? 180.924 179.432 243.593 1.00 11.91 ? 4314 ASP A CA    1 
ATOM   20646 C C     . ASP A 1 4314 ? 180.186 180.416 242.693 1.00 17.49 ? 4314 ASP A C     1 
ATOM   20647 O O     . ASP A 1 4314 ? 180.801 181.093 241.860 1.00 21.08 ? 4314 ASP A O     1 
ATOM   20648 C CB    . ASP A 1 4314 ? 180.785 177.996 243.079 1.00 16.19 ? 4314 ASP A CB    1 
ATOM   20649 C CG    . ASP A 1 4314 ? 181.180 177.838 241.615 1.00 23.12 ? 4314 ASP A CG    1 
ATOM   20650 O OD1   . ASP A 1 4314 ? 181.797 178.754 241.034 1.00 20.54 ? 4314 ASP A OD1   1 
ATOM   20651 O OD2   . ASP A 1 4314 ? 180.866 176.775 241.037 1.00 25.62 ? 4314 ASP A OD2   1 
ATOM   20652 N N     . THR A 1 4315 ? 178.869 180.522 242.858 1.00 12.49 ? 4315 THR A N     1 
ATOM   20653 C CA    . THR A 1 4315 ? 178.102 181.483 242.079 1.00 11.52 ? 4315 THR A CA    1 
ATOM   20654 C C     . THR A 1 4315 ? 178.514 182.908 242.430 1.00 9.64  ? 4315 THR A C     1 
ATOM   20655 O O     . THR A 1 4315 ? 178.693 183.256 243.600 1.00 14.44 ? 4315 THR A O     1 
ATOM   20656 C CB    . THR A 1 4315 ? 176.600 181.285 242.311 1.00 13.78 ? 4315 THR A CB    1 
ATOM   20657 O OG1   . THR A 1 4315 ? 175.860 182.214 241.508 1.00 10.62 ? 4315 THR A OG1   1 
ATOM   20658 C CG2   . THR A 1 4315 ? 176.232 181.467 243.781 1.00 9.38  ? 4315 THR A CG2   1 
ATOM   20659 N N     . GLN A 1 4316 ? 178.691 183.729 241.397 1.00 4.30  ? 4316 GLN A N     1 
ATOM   20660 C CA    . GLN A 1 4316 ? 179.074 185.131 241.563 1.00 0.00  ? 4316 GLN A CA    1 
ATOM   20661 C C     . GLN A 1 4316 ? 178.397 185.927 240.454 1.00 3.28  ? 4316 GLN A C     1 
ATOM   20662 O O     . GLN A 1 4316 ? 178.786 185.835 239.286 1.00 11.20 ? 4316 GLN A O     1 
ATOM   20663 C CB    . GLN A 1 4316 ? 180.587 185.309 241.528 1.00 0.00  ? 4316 GLN A CB    1 
ATOM   20664 C CG    . GLN A 1 4316 ? 181.028 186.740 241.261 1.00 3.21  ? 4316 GLN A CG    1 
ATOM   20665 C CD    . GLN A 1 4316 ? 182.526 186.873 241.111 1.00 4.17  ? 4316 GLN A CD    1 
ATOM   20666 O OE1   . GLN A 1 4316 ? 183.279 185.958 241.438 1.00 11.26 ? 4316 GLN A OE1   1 
ATOM   20667 N NE2   . GLN A 1 4316 ? 182.966 188.011 240.595 1.00 0.00  ? 4316 GLN A NE2   1 
ATOM   20668 N N     . THR A 1 4317 ? 177.376 186.685 240.820 1.00 2.60  ? 4317 THR A N     1 
ATOM   20669 C CA    . THR A 1 4317 ? 176.760 187.621 239.901 1.00 2.00  ? 4317 THR A CA    1 
ATOM   20670 C C     . THR A 1 4317 ? 177.629 188.867 239.774 1.00 2.88  ? 4317 THR A C     1 
ATOM   20671 O O     . THR A 1 4317 ? 178.484 189.127 240.623 1.00 8.24  ? 4317 THR A O     1 
ATOM   20672 C CB    . THR A 1 4317 ? 175.364 187.995 240.391 1.00 3.08  ? 4317 THR A CB    1 
ATOM   20673 O OG1   . THR A 1 4317 ? 175.451 188.549 241.708 1.00 8.66  ? 4317 THR A OG1   1 
ATOM   20674 C CG2   . THR A 1 4317 ? 174.467 186.770 240.423 1.00 8.91  ? 4317 THR A CG2   1 
ATOM   20675 N N     . PRO A 1 4318 ? 177.444 189.651 238.709 1.00 4.09  ? 4318 PRO A N     1 
ATOM   20676 C CA    . PRO A 1 4318 ? 178.131 190.950 238.640 1.00 1.95  ? 4318 PRO A CA    1 
ATOM   20677 C C     . PRO A 1 4318 ? 177.719 191.905 239.747 1.00 1.97  ? 4318 PRO A C     1 
ATOM   20678 O O     . PRO A 1 4318 ? 178.401 192.913 239.960 1.00 5.74  ? 4318 PRO A O     1 
ATOM   20679 C CB    . PRO A 1 4318 ? 177.740 191.485 237.255 1.00 5.30  ? 4318 PRO A CB    1 
ATOM   20680 C CG    . PRO A 1 4318 ? 176.534 190.699 236.861 1.00 6.09  ? 4318 PRO A CG    1 
ATOM   20681 C CD    . PRO A 1 4318 ? 176.724 189.349 237.462 1.00 8.36  ? 4318 PRO A CD    1 
ATOM   20682 N N     . SER A 1 4319 ? 176.622 191.621 240.454 1.00 4.01  ? 4319 SER A N     1 
ATOM   20683 C CA    . SER A 1 4319 ? 176.215 192.447 241.584 1.00 0.00  ? 4319 SER A CA    1 
ATOM   20684 C C     . SER A 1 4319 ? 177.212 192.392 242.735 1.00 1.99  ? 4319 SER A C     1 
ATOM   20685 O O     . SER A 1 4319 ? 177.166 193.255 243.617 1.00 8.24  ? 4319 SER A O     1 
ATOM   20686 C CB    . SER A 1 4319 ? 174.833 192.018 242.070 1.00 0.97  ? 4319 SER A CB    1 
ATOM   20687 O OG    . SER A 1 4319 ? 174.279 192.986 242.940 1.00 12.06 ? 4319 SER A OG    1 
ATOM   20688 N N     . TRP A 1 4320 ? 178.095 191.389 242.759 1.00 4.61  ? 4320 TRP A N     1 
ATOM   20689 C CA    . TRP A 1 4320 ? 179.201 191.399 243.712 1.00 0.97  ? 4320 TRP A CA    1 
ATOM   20690 C C     . TRP A 1 4320 ? 180.047 192.650 243.541 1.00 6.43  ? 4320 TRP A C     1 
ATOM   20691 O O     . TRP A 1 4320 ? 180.585 193.188 244.515 1.00 14.83 ? 4320 TRP A O     1 
ATOM   20692 C CB    . TRP A 1 4320 ? 180.083 190.164 243.524 1.00 1.04  ? 4320 TRP A CB    1 
ATOM   20693 C CG    . TRP A 1 4320 ? 179.532 188.889 244.060 1.00 0.00  ? 4320 TRP A CG    1 
ATOM   20694 C CD1   . TRP A 1 4320 ? 178.233 188.495 244.063 1.00 0.00  ? 4320 TRP A CD1   1 
ATOM   20695 C CD2   . TRP A 1 4320 ? 180.275 187.828 244.667 1.00 1.40  ? 4320 TRP A CD2   1 
ATOM   20696 N NE1   . TRP A 1 4320 ? 178.113 187.256 244.640 1.00 2.37  ? 4320 TRP A NE1   1 
ATOM   20697 C CE2   . TRP A 1 4320 ? 179.356 186.823 245.019 1.00 3.67  ? 4320 TRP A CE2   1 
ATOM   20698 C CE3   . TRP A 1 4320 ? 181.630 187.631 244.949 1.00 2.80  ? 4320 TRP A CE3   1 
ATOM   20699 C CZ2   . TRP A 1 4320 ? 179.746 185.639 245.636 1.00 2.11  ? 4320 TRP A CZ2   1 
ATOM   20700 C CZ3   . TRP A 1 4320 ? 182.014 186.457 245.561 1.00 8.41  ? 4320 TRP A CZ3   1 
ATOM   20701 C CH2   . TRP A 1 4320 ? 181.076 185.475 245.898 1.00 2.31  ? 4320 TRP A CH2   1 
ATOM   20702 N N     . LEU A 1 4321 ? 180.178 193.118 242.306 1.00 4.37  ? 4321 LEU A N     1 
ATOM   20703 C CA    . LEU A 1 4321 ? 181.076 194.198 241.937 1.00 0.00  ? 4321 LEU A CA    1 
ATOM   20704 C C     . LEU A 1 4321 ? 180.424 195.568 242.036 1.00 0.00  ? 4321 LEU A C     1 
ATOM   20705 O O     . LEU A 1 4321 ? 181.086 196.574 241.766 1.00 8.47  ? 4321 LEU A O     1 
ATOM   20706 C CB    . LEU A 1 4321 ? 181.573 193.972 240.508 1.00 0.77  ? 4321 LEU A CB    1 
ATOM   20707 C CG    . LEU A 1 4321 ? 182.245 192.624 240.240 1.00 0.00  ? 4321 LEU A CG    1 
ATOM   20708 C CD1   . LEU A 1 4321 ? 182.632 192.509 238.784 1.00 1.59  ? 4321 LEU A CD1   1 
ATOM   20709 C CD2   . LEU A 1 4321 ? 183.453 192.434 241.126 1.00 0.22  ? 4321 LEU A CD2   1 
ATOM   20710 N N     . GLY A 1 4322 ? 179.150 195.633 242.413 1.00 0.00  ? 4322 GLY A N     1 
ATOM   20711 C CA    . GLY A 1 4322 ? 178.390 196.858 242.346 1.00 2.98  ? 4322 GLY A CA    1 
ATOM   20712 C C     . GLY A 1 4322 ? 177.696 197.083 241.023 1.00 0.00  ? 4322 GLY A C     1 
ATOM   20713 O O     . GLY A 1 4322 ? 176.877 198.003 240.919 1.00 7.91  ? 4322 GLY A O     1 
ATOM   20714 N N     . LEU A 1 4323 ? 177.992 196.268 240.020 1.00 0.00  ? 4323 LEU A N     1 
ATOM   20715 C CA    . LEU A 1 4323 ? 177.392 196.370 238.704 1.00 0.00  ? 4323 LEU A CA    1 
ATOM   20716 C C     . LEU A 1 4323 ? 176.021 195.703 238.690 1.00 2.27  ? 4323 LEU A C     1 
ATOM   20717 O O     . LEU A 1 4323 ? 175.722 194.862 239.538 1.00 6.11  ? 4323 LEU A O     1 
ATOM   20718 C CB    . LEU A 1 4323 ? 178.307 195.721 237.672 1.00 0.00  ? 4323 LEU A CB    1 
ATOM   20719 C CG    . LEU A 1 4323 ? 179.591 196.478 237.339 1.00 0.00  ? 4323 LEU A CG    1 
ATOM   20720 C CD1   . LEU A 1 4323 ? 180.556 195.587 236.588 1.00 0.00  ? 4323 LEU A CD1   1 
ATOM   20721 C CD2   . LEU A 1 4323 ? 179.271 197.720 236.535 1.00 4.19  ? 4323 LEU A CD2   1 
ATOM   20722 N N     . PRO A 1 4324 ? 175.163 196.068 237.742 1.00 2.39  ? 4324 PRO A N     1 
ATOM   20723 C CA    . PRO A 1 4324 ? 173.869 195.390 237.627 1.00 0.84  ? 4324 PRO A CA    1 
ATOM   20724 C C     . PRO A 1 4324 ? 174.035 193.958 237.144 1.00 5.59  ? 4324 PRO A C     1 
ATOM   20725 O O     . PRO A 1 4324 ? 175.049 193.580 236.555 1.00 5.37  ? 4324 PRO A O     1 
ATOM   20726 C CB    . PRO A 1 4324 ? 173.105 196.238 236.605 1.00 4.04  ? 4324 PRO A CB    1 
ATOM   20727 C CG    . PRO A 1 4324 ? 174.147 196.975 235.856 1.00 3.11  ? 4324 PRO A CG    1 
ATOM   20728 C CD    . PRO A 1 4324 ? 175.297 197.178 236.785 1.00 3.18  ? 4324 PRO A CD    1 
ATOM   20729 N N     . ASN A 1 4325 ? 173.006 193.150 237.413 1.00 10.36 ? 4325 ASN A N     1 
ATOM   20730 C CA    . ASN A 1 4325 ? 173.051 191.736 237.057 1.00 5.25  ? 4325 ASN A CA    1 
ATOM   20731 C C     . ASN A 1 4325 ? 173.106 191.507 235.553 1.00 8.60  ? 4325 ASN A C     1 
ATOM   20732 O O     . ASN A 1 4325 ? 173.625 190.474 235.117 1.00 15.01 ? 4325 ASN A O     1 
ATOM   20733 C CB    . ASN A 1 4325 ? 171.842 191.009 237.645 1.00 5.74  ? 4325 ASN A CB    1 
ATOM   20734 C CG    . ASN A 1 4325 ? 171.914 190.886 239.151 1.00 10.22 ? 4325 ASN A CG    1 
ATOM   20735 O OD1   . ASN A 1 4325 ? 172.971 190.599 239.711 1.00 10.95 ? 4325 ASN A OD1   1 
ATOM   20736 N ND2   . ASN A 1 4325 ? 170.787 191.107 239.817 1.00 11.05 ? 4325 ASN A ND2   1 
ATOM   20737 N N     . ASN A 1 4326 ? 172.596 192.438 234.750 1.00 3.65  ? 4326 ASN A N     1 
ATOM   20738 C CA    . ASN A 1 4326 ? 172.573 192.275 233.303 1.00 0.91  ? 4326 ASN A CA    1 
ATOM   20739 C C     . ASN A 1 4326 ? 173.892 192.652 232.641 1.00 2.78  ? 4326 ASN A C     1 
ATOM   20740 O O     . ASN A 1 4326 ? 174.007 192.557 231.413 1.00 8.27  ? 4326 ASN A O     1 
ATOM   20741 C CB    . ASN A 1 4326 ? 171.421 193.086 232.701 1.00 6.98  ? 4326 ASN A CB    1 
ATOM   20742 C CG    . ASN A 1 4326 ? 171.592 194.578 232.886 1.00 12.15 ? 4326 ASN A CG    1 
ATOM   20743 O OD1   . ASN A 1 4326 ? 172.423 195.032 233.669 1.00 16.97 ? 4326 ASN A OD1   1 
ATOM   20744 N ND2   . ASN A 1 4326 ? 170.791 195.353 232.168 1.00 16.16 ? 4326 ASN A ND2   1 
ATOM   20745 N N     . ALA A 1 4327 ? 174.888 193.077 233.422 1.00 1.04  ? 4327 ALA A N     1 
ATOM   20746 C CA    . ALA A 1 4327 ? 176.231 193.226 232.877 1.00 5.58  ? 4327 ALA A CA    1 
ATOM   20747 C C     . ALA A 1 4327 ? 176.750 191.904 232.333 1.00 9.36  ? 4327 ALA A C     1 
ATOM   20748 O O     . ALA A 1 4327 ? 177.498 191.884 231.349 1.00 8.68  ? 4327 ALA A O     1 
ATOM   20749 C CB    . ALA A 1 4327 ? 177.174 193.772 233.948 1.00 2.27  ? 4327 ALA A CB    1 
ATOM   20750 N N     . GLU A 1 4328 ? 176.354 190.789 232.955 1.00 5.27  ? 4328 GLU A N     1 
ATOM   20751 C CA    . GLU A 1 4328 ? 176.701 189.478 232.420 1.00 0.00  ? 4328 GLU A CA    1 
ATOM   20752 C C     . GLU A 1 4328 ? 176.069 189.256 231.052 1.00 8.09  ? 4328 GLU A C     1 
ATOM   20753 O O     . GLU A 1 4328 ? 176.719 188.731 230.143 1.00 16.85 ? 4328 GLU A O     1 
ATOM   20754 C CB    . GLU A 1 4328 ? 176.274 188.383 233.396 1.00 4.09  ? 4328 GLU A CB    1 
ATOM   20755 C CG    . GLU A 1 4328 ? 177.029 187.080 233.219 1.00 10.40 ? 4328 GLU A CG    1 
ATOM   20756 C CD    . GLU A 1 4328 ? 178.501 187.209 233.550 1.00 7.17  ? 4328 GLU A CD    1 
ATOM   20757 O OE1   . GLU A 1 4328 ? 178.837 187.957 234.491 1.00 9.70  ? 4328 GLU A OE1   1 
ATOM   20758 O OE2   . GLU A 1 4328 ? 179.323 186.567 232.865 1.00 7.90  ? 4328 GLU A OE2   1 
ATOM   20759 N N     . ARG A 1 4329 ? 174.803 189.649 230.885 1.00 12.29 ? 4329 ARG A N     1 
ATOM   20760 C CA    . ARG A 1 4329 ? 174.167 189.529 229.576 1.00 4.00  ? 4329 ARG A CA    1 
ATOM   20761 C C     . ARG A 1 4329 ? 174.872 190.390 228.539 1.00 0.44  ? 4329 ARG A C     1 
ATOM   20762 O O     . ARG A 1 4329 ? 175.062 189.964 227.394 1.00 7.75  ? 4329 ARG A O     1 
ATOM   20763 C CB    . ARG A 1 4329 ? 172.688 189.907 229.659 1.00 5.34  ? 4329 ARG A CB    1 
ATOM   20764 C CG    . ARG A 1 4329 ? 171.829 188.920 230.419 1.00 9.18  ? 4329 ARG A CG    1 
ATOM   20765 C CD    . ARG A 1 4329 ? 170.356 189.189 230.173 1.00 12.47 ? 4329 ARG A CD    1 
ATOM   20766 N NE    . ARG A 1 4329 ? 169.498 188.246 230.880 1.00 15.47 ? 4329 ARG A NE    1 
ATOM   20767 C CZ    . ARG A 1 4329 ? 168.174 188.237 230.802 1.00 13.86 ? 4329 ARG A CZ    1 
ATOM   20768 N NH1   . ARG A 1 4329 ? 167.520 189.108 230.052 1.00 13.13 ? 4329 ARG A NH1   1 
ATOM   20769 N NH2   . ARG A 1 4329 ? 167.491 187.329 231.492 1.00 9.91  ? 4329 ARG A NH2   1 
ATOM   20770 N N     . VAL A 1 4330 ? 175.260 191.608 228.917 1.00 2.74  ? 4330 VAL A N     1 
ATOM   20771 C CA    . VAL A 1 4330 ? 175.959 192.488 227.981 1.00 8.45  ? 4330 VAL A CA    1 
ATOM   20772 C C     . VAL A 1 4330 ? 177.288 191.871 227.560 1.00 6.76  ? 4330 VAL A C     1 
ATOM   20773 O O     . VAL A 1 4330 ? 177.637 191.844 226.371 1.00 3.87  ? 4330 VAL A O     1 
ATOM   20774 C CB    . VAL A 1 4330 ? 176.157 193.884 228.596 1.00 5.73  ? 4330 VAL A CB    1 
ATOM   20775 C CG1   . VAL A 1 4330 ? 176.798 194.815 227.587 1.00 6.34  ? 4330 VAL A CG1   1 
ATOM   20776 C CG2   . VAL A 1 4330 ? 174.831 194.447 229.056 1.00 10.14 ? 4330 VAL A CG2   1 
ATOM   20777 N N     . LEU A 1 4331 ? 178.049 191.365 228.532 1.00 7.98  ? 4331 LEU A N     1 
ATOM   20778 C CA    . LEU A 1 4331 ? 179.337 190.754 228.224 1.00 4.75  ? 4331 LEU A CA    1 
ATOM   20779 C C     . LEU A 1 4331 ? 179.165 189.519 227.349 1.00 8.44  ? 4331 LEU A C     1 
ATOM   20780 O O     . LEU A 1 4331 ? 179.936 189.304 226.406 1.00 8.91  ? 4331 LEU A O     1 
ATOM   20781 C CB    . LEU A 1 4331 ? 180.064 190.402 229.521 1.00 1.21  ? 4331 LEU A CB    1 
ATOM   20782 C CG    . LEU A 1 4331 ? 181.474 189.833 229.389 1.00 6.26  ? 4331 LEU A CG    1 
ATOM   20783 C CD1   . LEU A 1 4331 ? 182.425 190.889 228.859 1.00 6.35  ? 4331 LEU A CD1   1 
ATOM   20784 C CD2   . LEU A 1 4331 ? 181.952 189.301 230.727 1.00 5.47  ? 4331 LEU A CD2   1 
ATOM   20785 N N     . LEU A 1 4332 ? 178.154 188.700 227.642 1.00 8.47  ? 4332 LEU A N     1 
ATOM   20786 C CA    . LEU A 1 4332 ? 177.911 187.501 226.850 1.00 4.55  ? 4332 LEU A CA    1 
ATOM   20787 C C     . LEU A 1 4332 ? 177.511 187.851 225.423 1.00 8.52  ? 4332 LEU A C     1 
ATOM   20788 O O     . LEU A 1 4332 ? 177.944 187.192 224.471 1.00 15.04 ? 4332 LEU A O     1 
ATOM   20789 C CB    . LEU A 1 4332 ? 176.836 186.648 227.520 1.00 5.62  ? 4332 LEU A CB    1 
ATOM   20790 C CG    . LEU A 1 4332 ? 177.302 185.828 228.723 1.00 3.86  ? 4332 LEU A CG    1 
ATOM   20791 C CD1   . LEU A 1 4332 ? 176.202 184.894 229.188 1.00 8.72  ? 4332 LEU A CD1   1 
ATOM   20792 C CD2   . LEU A 1 4332 ? 178.565 185.056 228.387 1.00 8.32  ? 4332 LEU A CD2   1 
ATOM   20793 N N     . THR A 1 4333 ? 176.678 188.880 225.252 1.00 8.75  ? 4333 THR A N     1 
ATOM   20794 C CA    . THR A 1 4333 ? 176.308 189.316 223.910 1.00 10.37 ? 4333 THR A CA    1 
ATOM   20795 C C     . THR A 1 4333 ? 177.527 189.805 223.138 1.00 8.74  ? 4333 THR A C     1 
ATOM   20796 O O     . THR A 1 4333 ? 177.701 189.476 221.957 1.00 11.02 ? 4333 THR A O     1 
ATOM   20797 C CB    . THR A 1 4333 ? 175.252 190.418 223.991 1.00 8.80  ? 4333 THR A CB    1 
ATOM   20798 O OG1   . THR A 1 4333 ? 174.041 189.883 224.537 1.00 9.46  ? 4333 THR A OG1   1 
ATOM   20799 C CG2   . THR A 1 4333 ? 174.970 190.990 222.614 1.00 9.20  ? 4333 THR A CG2   1 
ATOM   20800 N N     . THR A 1 4334 ? 178.387 190.587 223.795 1.00 8.64  ? 4334 THR A N     1 
ATOM   20801 C CA    . THR A 1 4334 ? 179.598 191.061 223.134 1.00 7.63  ? 4334 THR A CA    1 
ATOM   20802 C C     . THR A 1 4334 ? 180.488 189.895 222.723 1.00 10.17 ? 4334 THR A C     1 
ATOM   20803 O O     . THR A 1 4334 ? 181.041 189.884 221.617 1.00 14.98 ? 4334 THR A O     1 
ATOM   20804 C CB    . THR A 1 4334 ? 180.354 192.021 224.052 1.00 7.51  ? 4334 THR A CB    1 
ATOM   20805 O OG1   . THR A 1 4334 ? 179.555 193.187 224.285 1.00 13.35 ? 4334 THR A OG1   1 
ATOM   20806 C CG2   . THR A 1 4334 ? 181.672 192.441 223.423 1.00 6.10  ? 4334 THR A CG2   1 
ATOM   20807 N N     . GLN A 1 4335 ? 180.624 188.894 223.596 1.00 7.34  ? 4335 GLN A N     1 
ATOM   20808 C CA    . GLN A 1 4335 ? 181.451 187.735 223.272 1.00 6.64  ? 4335 GLN A CA    1 
ATOM   20809 C C     . GLN A 1 4335 ? 180.851 186.927 222.126 1.00 11.95 ? 4335 GLN A C     1 
ATOM   20810 O O     . GLN A 1 4335 ? 181.584 186.404 221.279 1.00 17.31 ? 4335 GLN A O     1 
ATOM   20811 C CB    . GLN A 1 4335 ? 181.635 186.869 224.516 1.00 5.49  ? 4335 GLN A CB    1 
ATOM   20812 C CG    . GLN A 1 4335 ? 182.419 187.561 225.617 1.00 10.58 ? 4335 GLN A CG    1 
ATOM   20813 C CD    . GLN A 1 4335 ? 183.215 186.599 226.469 1.00 14.36 ? 4335 GLN A CD    1 
ATOM   20814 O OE1   . GLN A 1 4335 ? 184.277 186.126 226.067 1.00 16.49 ? 4335 GLN A OE1   1 
ATOM   20815 N NE2   . GLN A 1 4335 ? 182.708 186.308 227.660 1.00 11.57 ? 4335 GLN A NE2   1 
ATOM   20816 N N     . GLY A 1 4336 ? 179.523 186.813 222.084 1.00 10.22 ? 4336 GLY A N     1 
ATOM   20817 C CA    . GLY A 1 4336 ? 178.887 186.125 220.971 1.00 5.87  ? 4336 GLY A CA    1 
ATOM   20818 C C     . GLY A 1 4336 ? 179.124 186.825 219.648 1.00 8.57  ? 4336 GLY A C     1 
ATOM   20819 O O     . GLY A 1 4336 ? 179.436 186.186 218.639 1.00 12.60 ? 4336 GLY A O     1 
ATOM   20820 N N     . VAL A 1 4337 ? 178.982 188.152 219.636 1.00 11.33 ? 4337 VAL A N     1 
ATOM   20821 C CA    . VAL A 1 4337 ? 179.269 188.902 218.415 1.00 9.43  ? 4337 VAL A CA    1 
ATOM   20822 C C     . VAL A 1 4337 ? 180.738 188.767 218.029 1.00 11.28 ? 4337 VAL A C     1 
ATOM   20823 O O     . VAL A 1 4337 ? 181.068 188.688 216.839 1.00 10.61 ? 4337 VAL A O     1 
ATOM   20824 C CB    . VAL A 1 4337 ? 178.854 190.375 218.573 1.00 7.10  ? 4337 VAL A CB    1 
ATOM   20825 C CG1   . VAL A 1 4337 ? 179.019 191.110 217.259 1.00 15.05 ? 4337 VAL A CG1   1 
ATOM   20826 C CG2   . VAL A 1 4337 ? 177.412 190.464 219.022 1.00 10.11 ? 4337 VAL A CG2   1 
ATOM   20827 N N     . ASP A 1 4338 ? 181.640 188.736 219.012 1.00 11.53 ? 4338 ASP A N     1 
ATOM   20828 C CA    . ASP A 1 4338 ? 183.055 188.545 218.706 1.00 12.58 ? 4338 ASP A CA    1 
ATOM   20829 C C     . ASP A 1 4338 ? 183.310 187.180 218.076 1.00 14.12 ? 4338 ASP A C     1 
ATOM   20830 O O     . ASP A 1 4338 ? 184.099 187.064 217.131 1.00 21.14 ? 4338 ASP A O     1 
ATOM   20831 C CB    . ASP A 1 4338 ? 183.895 188.717 219.969 1.00 14.57 ? 4338 ASP A CB    1 
ATOM   20832 C CG    . ASP A 1 4338 ? 185.324 189.116 219.666 1.00 18.47 ? 4338 ASP A CG    1 
ATOM   20833 O OD1   . ASP A 1 4338 ? 185.653 189.288 218.473 1.00 13.67 ? 4338 ASP A OD1   1 
ATOM   20834 O OD2   . ASP A 1 4338 ? 186.118 189.259 220.619 1.00 22.75 ? 4338 ASP A OD2   1 
ATOM   20835 N N     . MET A 1 4339 ? 182.660 186.134 218.592 1.00 5.74  ? 4339 MET A N     1 
ATOM   20836 C CA    . MET A 1 4339 ? 182.814 184.808 218.000 1.00 4.61  ? 4339 MET A CA    1 
ATOM   20837 C C     . MET A 1 4339 ? 182.260 184.773 216.581 1.00 15.17 ? 4339 MET A C     1 
ATOM   20838 O O     . MET A 1 4339 ? 182.862 184.167 215.684 1.00 20.66 ? 4339 MET A O     1 
ATOM   20839 C CB    . MET A 1 4339 ? 182.136 183.755 218.877 1.00 8.45  ? 4339 MET A CB    1 
ATOM   20840 C CG    . MET A 1 4339 ? 182.226 182.337 218.334 1.00 8.79  ? 4339 MET A CG    1 
ATOM   20841 S SD    . MET A 1 4339 ? 180.901 181.257 218.909 1.00 16.79 ? 4339 MET A SD    1 
ATOM   20842 C CE    . MET A 1 4339 ? 179.450 182.188 218.437 1.00 9.90  ? 4339 MET A CE    1 
ATOM   20843 N N     . ILE A 1 4340 ? 181.116 185.426 216.356 1.00 16.57 ? 4340 ILE A N     1 
ATOM   20844 C CA    . ILE A 1 4340 ? 180.559 185.506 215.007 1.00 5.08  ? 4340 ILE A CA    1 
ATOM   20845 C C     . ILE A 1 4340 ? 181.531 186.202 214.067 1.00 9.43  ? 4340 ILE A C     1 
ATOM   20846 O O     . ILE A 1 4340 ? 181.745 185.756 212.934 1.00 11.92 ? 4340 ILE A O     1 
ATOM   20847 C CB    . ILE A 1 4340 ? 179.192 186.212 215.025 1.00 6.38  ? 4340 ILE A CB    1 
ATOM   20848 C CG1   . ILE A 1 4340 ? 178.195 185.417 215.859 1.00 5.97  ? 4340 ILE A CG1   1 
ATOM   20849 C CG2   . ILE A 1 4340 ? 178.669 186.395 213.614 1.00 12.47 ? 4340 ILE A CG2   1 
ATOM   20850 C CD1   . ILE A 1 4340 ? 178.219 183.948 215.553 1.00 8.93  ? 4340 ILE A CD1   1 
ATOM   20851 N N     . SER A 1 4341 ? 182.134 187.303 214.519 1.00 9.00  ? 4341 SER A N     1 
ATOM   20852 C CA    . SER A 1 4341 ? 183.086 188.021 213.676 1.00 9.36  ? 4341 SER A CA    1 
ATOM   20853 C C     . SER A 1 4341 ? 184.315 187.171 213.380 1.00 7.05  ? 4341 SER A C     1 
ATOM   20854 O O     . SER A 1 4341 ? 184.838 187.193 212.260 1.00 10.48 ? 4341 SER A O     1 
ATOM   20855 C CB    . SER A 1 4341 ? 183.491 189.335 214.339 1.00 8.19  ? 4341 SER A CB    1 
ATOM   20856 O OG    . SER A 1 4341 ? 184.217 189.098 215.530 1.00 17.58 ? 4341 SER A OG    1 
ATOM   20857 N N     . LYS A 1 4342 ? 184.797 186.424 214.376 1.00 3.65  ? 4342 LYS A N     1 
ATOM   20858 C CA    . LYS A 1 4342 ? 185.959 185.568 214.155 1.00 6.73  ? 4342 LYS A CA    1 
ATOM   20859 C C     . LYS A 1 4342 ? 185.659 184.480 213.130 1.00 11.73 ? 4342 LYS A C     1 
ATOM   20860 O O     . LYS A 1 4342 ? 186.449 184.252 212.203 1.00 14.05 ? 4342 LYS A O     1 
ATOM   20861 C CB    . LYS A 1 4342 ? 186.417 184.955 215.477 1.00 7.02  ? 4342 LYS A CB    1 
ATOM   20862 C CG    . LYS A 1 4342 ? 187.092 185.944 216.412 1.00 11.77 ? 4342 LYS A CG    1 
ATOM   20863 C CD    . LYS A 1 4342 ? 187.585 185.267 217.678 1.00 12.05 ? 4342 LYS A CD    1 
ATOM   20864 C CE    . LYS A 1 4342 ? 188.146 186.276 218.663 1.00 7.29  ? 4342 LYS A CE    1 
ATOM   20865 N NZ    . LYS A 1 4342 ? 189.415 186.878 218.176 1.00 12.97 ? 4342 LYS A NZ    1 
ATOM   20866 N N     . MET A 1 4343 ? 184.510 183.813 213.259 1.00 9.37  ? 4343 MET A N     1 
ATOM   20867 C CA    . MET A 1 4343 ? 184.145 182.823 212.252 1.00 6.21  ? 4343 MET A CA    1 
ATOM   20868 C C     . MET A 1 4343 ? 183.942 183.449 210.880 1.00 13.83 ? 4343 MET A C     1 
ATOM   20869 O O     . MET A 1 4343 ? 184.307 182.839 209.869 1.00 16.38 ? 4343 MET A O     1 
ATOM   20870 C CB    . MET A 1 4343 ? 182.887 182.062 212.661 1.00 6.87  ? 4343 MET A CB    1 
ATOM   20871 C CG    . MET A 1 4343 ? 182.905 181.524 214.066 1.00 5.24  ? 4343 MET A CG    1 
ATOM   20872 S SD    . MET A 1 4343 ? 182.054 179.946 214.123 1.00 11.59 ? 4343 MET A SD    1 
ATOM   20873 C CE    . MET A 1 4343 ? 180.357 180.471 213.928 1.00 16.16 ? 4343 MET A CE    1 
ATOM   20874 N N     . LEU A 1 4344 ? 183.370 184.654 210.819 1.00 11.13 ? 4344 LEU A N     1 
ATOM   20875 C CA    . LEU A 1 4344 ? 183.200 185.322 209.533 1.00 10.45 ? 4344 LEU A CA    1 
ATOM   20876 C C     . LEU A 1 4344 ? 184.546 185.609 208.883 1.00 12.20 ? 4344 LEU A C     1 
ATOM   20877 O O     . LEU A 1 4344 ? 184.709 185.429 207.671 1.00 12.58 ? 4344 LEU A O     1 
ATOM   20878 C CB    . LEU A 1 4344 ? 182.402 186.612 209.711 1.00 11.12 ? 4344 LEU A CB    1 
ATOM   20879 C CG    . LEU A 1 4344 ? 181.699 187.129 208.456 1.00 13.51 ? 4344 LEU A CG    1 
ATOM   20880 C CD1   . LEU A 1 4344 ? 180.885 186.021 207.811 1.00 12.71 ? 4344 LEU A CD1   1 
ATOM   20881 C CD2   . LEU A 1 4344 ? 180.818 188.321 208.787 1.00 13.87 ? 4344 LEU A CD2   1 
ATOM   20882 N N     . LYS A 1 4345 ? 185.526 186.053 209.672 1.00 11.86 ? 4345 LYS A N     1 
ATOM   20883 C CA    . LYS A 1 4345 ? 186.856 186.265 209.117 1.00 10.33 ? 4345 LYS A CA    1 
ATOM   20884 C C     . LYS A 1 4345 ? 187.576 184.957 208.825 1.00 9.89  ? 4345 LYS A C     1 
ATOM   20885 O O     . LYS A 1 4345 ? 188.599 184.976 208.133 1.00 16.30 ? 4345 LYS A O     1 
ATOM   20886 C CB    . LYS A 1 4345 ? 187.706 187.129 210.050 1.00 8.09  ? 4345 LYS A CB    1 
ATOM   20887 C CG    . LYS A 1 4345 ? 188.515 186.355 211.068 1.00 5.58  ? 4345 LYS A CG    1 
ATOM   20888 C CD    . LYS A 1 4345 ? 188.992 187.261 212.189 1.00 8.29  ? 4345 LYS A CD    1 
ATOM   20889 C CE    . LYS A 1 4345 ? 189.743 188.464 211.645 1.00 7.47  ? 4345 LYS A CE    1 
ATOM   20890 N NZ    . LYS A 1 4345 ? 190.215 189.355 212.738 1.00 9.95  ? 4345 LYS A NZ    1 
ATOM   20891 N N     . MET A 1 4346 ? 187.073 183.828 209.330 1.00 6.70  ? 4346 MET A N     1 
ATOM   20892 C CA    . MET A 1 4346 ? 187.583 182.518 208.937 1.00 8.42  ? 4346 MET A CA    1 
ATOM   20893 C C     . MET A 1 4346 ? 186.813 181.903 207.773 1.00 10.94 ? 4346 MET A C     1 
ATOM   20894 O O     . MET A 1 4346 ? 186.707 180.673 207.688 1.00 11.46 ? 4346 MET A O     1 
ATOM   20895 C CB    . MET A 1 4346 ? 187.589 181.563 210.128 1.00 10.47 ? 4346 MET A CB    1 
ATOM   20896 C CG    . MET A 1 4346 ? 188.424 182.045 211.284 1.00 15.77 ? 4346 MET A CG    1 
ATOM   20897 S SD    . MET A 1 4346 ? 190.149 182.120 210.792 1.00 18.07 ? 4346 MET A SD    1 
ATOM   20898 C CE    . MET A 1 4346 ? 190.812 180.811 211.796 1.00 2.71  ? 4346 MET A CE    1 
ATOM   20899 N N     . GLN A 1 4347 ? 186.269 182.721 206.879 1.00 12.03 ? 4347 GLN A N     1 
ATOM   20900 C CA    . GLN A 1 4347 ? 185.627 182.210 205.674 1.00 12.39 ? 4347 GLN A CA    1 
ATOM   20901 C C     . GLN A 1 4347 ? 186.610 182.184 204.511 1.00 11.20 ? 4347 GLN A C     1 
ATOM   20902 O O     . GLN A 1 4347 ? 187.596 182.922 204.494 0.00 12.59 ? 4347 GLN A O     1 
ATOM   20903 C CB    . GLN A 1 4347 ? 184.402 183.053 205.312 1.00 14.86 ? 4347 GLN A CB    1 
ATOM   20904 C CG    . GLN A 1 4347 ? 183.141 182.794 206.144 1.00 18.41 ? 4347 GLN A CG    1 
ATOM   20905 C CD    . GLN A 1 4347 ? 182.805 181.318 206.321 1.00 17.05 ? 4347 GLN A CD    1 
ATOM   20906 O OE1   . GLN A 1 4347 ? 183.493 180.583 207.029 1.00 11.38 ? 4347 GLN A OE1   1 
ATOM   20907 N NE2   . GLN A 1 4347 ? 181.734 180.881 205.669 1.00 17.81 ? 4347 GLN A NE2   1 
ATOM   20908 N N     . ALA A 1 4375 ? 184.298 186.211 190.411 1.00 34.16 ? 4375 ALA A N     1 
ATOM   20909 C CA    . ALA A 1 4375 ? 184.331 185.746 191.792 1.00 35.49 ? 4375 ALA A CA    1 
ATOM   20910 C C     . ALA A 1 4375 ? 183.506 186.659 192.693 1.00 35.08 ? 4375 ALA A C     1 
ATOM   20911 O O     . ALA A 1 4375 ? 182.277 186.663 192.630 1.00 36.70 ? 4375 ALA A O     1 
ATOM   20912 C CB    . ALA A 1 4375 ? 185.766 185.662 192.290 1.00 31.96 ? 4375 ALA A CB    1 
ATOM   20913 N N     . TRP A 1 4376 ? 184.192 187.432 193.529 1.00 32.45 ? 4376 TRP A N     1 
ATOM   20914 C CA    . TRP A 1 4376 ? 183.550 188.371 194.439 1.00 32.44 ? 4376 TRP A CA    1 
ATOM   20915 C C     . TRP A 1 4376 ? 183.369 189.755 193.828 1.00 32.58 ? 4376 TRP A C     1 
ATOM   20916 O O     . TRP A 1 4376 ? 182.873 190.662 194.512 1.00 33.01 ? 4376 TRP A O     1 
ATOM   20917 C CB    . TRP A 1 4376 ? 184.340 188.427 195.756 1.00 33.84 ? 4376 TRP A CB    1 
ATOM   20918 C CG    . TRP A 1 4376 ? 185.790 188.811 195.632 1.00 35.80 ? 4376 TRP A CG    1 
ATOM   20919 C CD1   . TRP A 1 4376 ? 186.861 187.980 195.792 1.00 36.18 ? 4376 TRP A CD1   1 
ATOM   20920 C CD2   . TRP A 1 4376 ? 186.334 190.124 195.437 1.00 33.68 ? 4376 TRP A CD2   1 
ATOM   20921 N NE1   . TRP A 1 4376 ? 188.032 188.677 195.645 1.00 36.82 ? 4376 TRP A NE1   1 
ATOM   20922 C CE2   . TRP A 1 4376 ? 187.738 189.997 195.434 1.00 33.96 ? 4376 TRP A CE2   1 
ATOM   20923 C CE3   . TRP A 1 4376 ? 185.774 191.389 195.242 1.00 35.22 ? 4376 TRP A CE3   1 
ATOM   20924 C CZ2   . TRP A 1 4376 ? 188.586 191.084 195.244 1.00 34.14 ? 4376 TRP A CZ2   1 
ATOM   20925 C CZ3   . TRP A 1 4376 ? 186.618 192.466 195.056 1.00 36.22 ? 4376 TRP A CZ3   1 
ATOM   20926 C CH2   . TRP A 1 4376 ? 188.009 192.307 195.056 1.00 34.44 ? 4376 TRP A CH2   1 
ATOM   20927 N N     . MET A 1 4377 ? 183.738 189.922 192.553 1.00 33.69 ? 4377 MET A N     1 
ATOM   20928 C CA    . MET A 1 4377 ? 183.382 191.128 191.812 1.00 34.98 ? 4377 MET A CA    1 
ATOM   20929 C C     . MET A 1 4377 ? 181.895 191.420 191.945 1.00 36.53 ? 4377 MET A C     1 
ATOM   20930 O O     . MET A 1 4377 ? 181.494 192.549 192.240 1.00 35.29 ? 4377 MET A O     1 
ATOM   20931 C CB    . MET A 1 4377 ? 183.731 190.968 190.329 1.00 38.32 ? 4377 MET A CB    1 
ATOM   20932 C CG    . MET A 1 4377 ? 185.199 190.837 189.948 1.00 37.73 ? 4377 MET A CG    1 
ATOM   20933 S SD    . MET A 1 4377 ? 186.228 192.252 190.367 1.00 39.22 ? 4377 MET A SD    1 
ATOM   20934 C CE    . MET A 1 4377 ? 187.049 191.633 191.822 1.00 34.86 ? 4377 MET A CE    1 
ATOM   20935 N N     . ARG A 1 4378 ? 181.062 190.400 191.731 1.00 37.46 ? 4378 ARG A N     1 
ATOM   20936 C CA    . ARG A 1 4378 ? 179.619 190.606 191.684 1.00 37.29 ? 4378 ARG A CA    1 
ATOM   20937 C C     . ARG A 1 4378 ? 179.059 190.955 193.058 1.00 36.91 ? 4378 ARG A C     1 
ATOM   20938 O O     . ARG A 1 4378 ? 178.186 191.823 193.174 1.00 35.80 ? 4378 ARG A O     1 
ATOM   20939 C CB    . ARG A 1 4378 ? 178.933 189.360 191.118 1.00 36.44 ? 4378 ARG A CB    1 
ATOM   20940 C CG    . ARG A 1 4378 ? 178.981 189.255 189.594 1.00 36.27 ? 4378 ARG A CG    1 
ATOM   20941 C CD    . ARG A 1 4378 ? 180.358 188.817 189.105 1.00 36.76 ? 4378 ARG A CD    1 
ATOM   20942 N NE    . ARG A 1 4378 ? 180.370 188.468 187.690 1.00 38.19 ? 4378 ARG A NE    1 
ATOM   20943 C CZ    . ARG A 1 4378 ? 181.464 188.423 186.941 1.00 39.04 ? 4378 ARG A CZ    1 
ATOM   20944 N NH1   . ARG A 1 4378 ? 182.658 188.695 187.443 1.00 37.77 ? 4378 ARG A NH1   1 
ATOM   20945 N NH2   . ARG A 1 4378 ? 181.358 188.096 185.656 1.00 34.99 ? 4378 ARG A NH2   1 
ATOM   20946 N N     . THR A 1 4379 ? 179.540 190.287 194.110 1.00 33.94 ? 4379 THR A N     1 
ATOM   20947 C CA    . THR A 1 4379 ? 179.071 190.600 195.457 1.00 35.03 ? 4379 THR A CA    1 
ATOM   20948 C C     . THR A 1 4379 ? 179.480 192.008 195.874 1.00 34.34 ? 4379 THR A C     1 
ATOM   20949 O O     . THR A 1 4379 ? 178.673 192.755 196.446 1.00 33.07 ? 4379 THR A O     1 
ATOM   20950 C CB    . THR A 1 4379 ? 179.602 189.570 196.455 1.00 33.76 ? 4379 THR A CB    1 
ATOM   20951 O OG1   . THR A 1 4379 ? 181.025 189.693 196.564 1.00 32.69 ? 4379 THR A OG1   1 
ATOM   20952 C CG2   . THR A 1 4379 ? 179.248 188.159 196.004 1.00 33.29 ? 4379 THR A CG2   1 
ATOM   20953 N N     . LEU A 1 4380 ? 180.729 192.394 195.594 1.00 33.34 ? 4380 LEU A N     1 
ATOM   20954 C CA    . LEU A 1 4380 ? 181.144 193.758 195.906 1.00 33.20 ? 4380 LEU A CA    1 
ATOM   20955 C C     . LEU A 1 4380 ? 180.329 194.764 195.101 1.00 31.46 ? 4380 LEU A C     1 
ATOM   20956 O O     . LEU A 1 4380 ? 179.918 195.804 195.628 1.00 27.67 ? 4380 LEU A O     1 
ATOM   20957 C CB    . LEU A 1 4380 ? 182.640 193.931 195.638 1.00 32.95 ? 4380 LEU A CB    1 
ATOM   20958 C CG    . LEU A 1 4380 ? 183.193 195.356 195.526 1.00 33.40 ? 4380 LEU A CG    1 
ATOM   20959 C CD1   . LEU A 1 4380 ? 182.842 196.196 196.751 1.00 31.77 ? 4380 LEU A CD1   1 
ATOM   20960 C CD2   . LEU A 1 4380 ? 184.692 195.347 195.299 1.00 31.00 ? 4380 LEU A CD2   1 
ATOM   20961 N N     . HIS A 1 4381 ? 180.072 194.460 193.828 1.00 32.61 ? 4381 HIS A N     1 
ATOM   20962 C CA    . HIS A 1 4381 ? 179.274 195.345 192.989 1.00 34.61 ? 4381 HIS A CA    1 
ATOM   20963 C C     . HIS A 1 4381 ? 177.873 195.530 193.553 1.00 34.12 ? 4381 HIS A C     1 
ATOM   20964 O O     . HIS A 1 4381 ? 177.377 196.659 193.640 1.00 33.88 ? 4381 HIS A O     1 
ATOM   20965 C CB    . HIS A 1 4381 ? 179.210 194.781 191.569 1.00 34.98 ? 4381 HIS A CB    1 
ATOM   20966 C CG    . HIS A 1 4381 ? 178.440 195.631 190.609 1.00 35.11 ? 4381 HIS A CG    1 
ATOM   20967 N ND1   . HIS A 1 4381 ? 178.931 196.815 190.102 1.00 34.04 ? 4381 HIS A ND1   1 
ATOM   20968 C CD2   . HIS A 1 4381 ? 177.211 195.469 190.064 1.00 36.64 ? 4381 HIS A CD2   1 
ATOM   20969 C CE1   . HIS A 1 4381 ? 178.039 197.343 189.283 1.00 34.62 ? 4381 HIS A CE1   1 
ATOM   20970 N NE2   . HIS A 1 4381 ? 176.986 196.548 189.244 1.00 39.02 ? 4381 HIS A NE2   1 
ATOM   20971 N N     . THR A 1 4382 ? 177.221 194.436 193.953 1.00 32.96 ? 4382 THR A N     1 
ATOM   20972 C CA    . THR A 1 4382 ? 175.844 194.549 194.422 1.00 34.82 ? 4382 THR A CA    1 
ATOM   20973 C C     . THR A 1 4382 ? 175.775 195.259 195.770 1.00 30.46 ? 4382 THR A C     1 
ATOM   20974 O O     . THR A 1 4382 ? 174.868 196.068 196.001 1.00 28.21 ? 4382 THR A O     1 
ATOM   20975 C CB    . THR A 1 4382 ? 175.168 193.172 194.476 1.00 33.53 ? 4382 THR A CB    1 
ATOM   20976 O OG1   . THR A 1 4382 ? 173.775 193.336 194.771 1.00 34.75 ? 4382 THR A OG1   1 
ATOM   20977 C CG2   . THR A 1 4382 ? 175.793 192.267 195.521 1.00 31.84 ? 4382 THR A CG2   1 
ATOM   20978 N N     . THR A 1 4383 ? 176.738 195.005 196.666 1.00 29.43 ? 4383 THR A N     1 
ATOM   20979 C CA    . THR A 1 4383 ? 176.705 195.715 197.943 1.00 30.30 ? 4383 THR A CA    1 
ATOM   20980 C C     . THR A 1 4383 ? 177.019 197.200 197.768 1.00 30.00 ? 4383 THR A C     1 
ATOM   20981 O O     . THR A 1 4383 ? 176.401 198.042 198.431 1.00 28.97 ? 4383 THR A O     1 
ATOM   20982 C CB    . THR A 1 4383 ? 177.651 195.063 198.959 1.00 29.54 ? 4383 THR A CB    1 
ATOM   20983 O OG1   . THR A 1 4383 ? 177.467 195.675 200.242 1.00 29.01 ? 4383 THR A OG1   1 
ATOM   20984 C CG2   . THR A 1 4383 ? 179.104 195.200 198.552 1.00 28.10 ? 4383 THR A CG2   1 
ATOM   20985 N N     . ALA A 1 4384 ? 177.938 197.547 196.862 1.00 29.19 ? 4384 ALA A N     1 
ATOM   20986 C CA    . ALA A 1 4384 ? 178.222 198.954 196.604 1.00 26.84 ? 4384 ALA A CA    1 
ATOM   20987 C C     . ALA A 1 4384 ? 177.030 199.652 195.959 1.00 26.17 ? 4384 ALA A C     1 
ATOM   20988 O O     . ALA A 1 4384 ? 176.735 200.809 196.278 1.00 27.95 ? 4384 ALA A O     1 
ATOM   20989 C CB    . ALA A 1 4384 ? 179.466 199.083 195.728 1.00 24.59 ? 4384 ALA A CB    1 
ATOM   20990 N N     . SER A 1 4385 ? 176.337 198.968 195.045 1.00 27.83 ? 4385 SER A N     1 
ATOM   20991 C CA    . SER A 1 4385 ? 175.142 199.547 194.441 1.00 28.24 ? 4385 SER A CA    1 
ATOM   20992 C C     . SER A 1 4385 ? 174.037 199.736 195.472 1.00 27.19 ? 4385 SER A C     1 
ATOM   20993 O O     . SER A 1 4385 ? 173.319 200.742 195.443 1.00 30.60 ? 4385 SER A O     1 
ATOM   20994 C CB    . SER A 1 4385 ? 174.658 198.667 193.289 1.00 30.62 ? 4385 SER A CB    1 
ATOM   20995 O OG    . SER A 1 4385 ? 175.590 198.668 192.222 1.00 29.37 ? 4385 SER A OG    1 
ATOM   20996 N N     . ASN A 1 4386 ? 173.881 198.777 196.387 1.00 21.97 ? 4386 ASN A N     1 
ATOM   20997 C CA    . ASN A 1 4386 ? 172.900 198.935 197.455 1.00 24.09 ? 4386 ASN A CA    1 
ATOM   20998 C C     . ASN A 1 4386 ? 173.251 200.119 198.346 1.00 27.30 ? 4386 ASN A C     1 
ATOM   20999 O O     . ASN A 1 4386 ? 172.366 200.874 198.768 1.00 27.63 ? 4386 ASN A O     1 
ATOM   21000 C CB    . ASN A 1 4386 ? 172.806 197.647 198.272 1.00 24.87 ? 4386 ASN A CB    1 
ATOM   21001 C CG    . ASN A 1 4386 ? 172.032 196.560 197.553 1.00 26.87 ? 4386 ASN A CG    1 
ATOM   21002 O OD1   . ASN A 1 4386 ? 171.660 196.714 196.390 1.00 28.41 ? 4386 ASN A OD1   1 
ATOM   21003 N ND2   . ASN A 1 4386 ? 171.788 195.451 198.241 1.00 25.69 ? 4386 ASN A ND2   1 
ATOM   21004 N N     . TRP A 1 4387 ? 174.542 200.297 198.643 1.00 26.62 ? 4387 TRP A N     1 
ATOM   21005 C CA    . TRP A 1 4387 ? 174.970 201.461 199.413 1.00 24.23 ? 4387 TRP A CA    1 
ATOM   21006 C C     . TRP A 1 4387 ? 174.651 202.759 198.680 1.00 23.54 ? 4387 TRP A C     1 
ATOM   21007 O O     . TRP A 1 4387 ? 174.114 203.700 199.276 1.00 25.13 ? 4387 TRP A O     1 
ATOM   21008 C CB    . TRP A 1 4387 ? 176.465 201.375 199.706 1.00 20.38 ? 4387 TRP A CB    1 
ATOM   21009 C CG    . TRP A 1 4387 ? 176.821 200.370 200.745 1.00 21.82 ? 4387 TRP A CG    1 
ATOM   21010 C CD1   . TRP A 1 4387 ? 175.965 199.700 201.565 1.00 24.89 ? 4387 TRP A CD1   1 
ATOM   21011 C CD2   . TRP A 1 4387 ? 178.136 199.911 201.075 1.00 22.35 ? 4387 TRP A CD2   1 
ATOM   21012 N NE1   . TRP A 1 4387 ? 176.664 198.854 202.390 1.00 26.11 ? 4387 TRP A NE1   1 
ATOM   21013 C CE2   . TRP A 1 4387 ? 178.000 198.965 202.108 1.00 23.86 ? 4387 TRP A CE2   1 
ATOM   21014 C CE3   . TRP A 1 4387 ? 179.415 200.210 200.598 1.00 20.29 ? 4387 TRP A CE3   1 
ATOM   21015 C CZ2   . TRP A 1 4387 ? 179.093 198.314 202.671 1.00 23.73 ? 4387 TRP A CZ2   1 
ATOM   21016 C CZ3   . TRP A 1 4387 ? 180.498 199.563 201.158 1.00 22.31 ? 4387 TRP A CZ3   1 
ATOM   21017 C CH2   . TRP A 1 4387 ? 180.331 198.626 202.184 1.00 25.23 ? 4387 TRP A CH2   1 
ATOM   21018 N N     . LEU A 1 4388 ? 174.963 202.823 197.382 1.00 21.56 ? 4388 LEU A N     1 
ATOM   21019 C CA    . LEU A 1 4388 ? 174.663 204.021 196.601 1.00 21.17 ? 4388 LEU A CA    1 
ATOM   21020 C C     . LEU A 1 4388 ? 173.170 204.319 196.593 1.00 22.83 ? 4388 LEU A C     1 
ATOM   21021 O O     . LEU A 1 4388 ? 172.760 205.479 196.717 1.00 20.74 ? 4388 LEU A O     1 
ATOM   21022 C CB    . LEU A 1 4388 ? 175.179 203.866 195.170 1.00 23.02 ? 4388 LEU A CB    1 
ATOM   21023 C CG    . LEU A 1 4388 ? 176.682 203.952 194.920 1.00 22.72 ? 4388 LEU A CG    1 
ATOM   21024 C CD1   . LEU A 1 4388 ? 176.948 204.157 193.444 1.00 25.37 ? 4388 LEU A CD1   1 
ATOM   21025 C CD2   . LEU A 1 4388 ? 177.254 205.112 195.705 1.00 19.94 ? 4388 LEU A CD2   1 
ATOM   21026 N N     . HIS A 1 4389 ? 172.341 203.286 196.440 1.00 26.99 ? 4389 HIS A N     1 
ATOM   21027 C CA    . HIS A 1 4389 ? 170.898 203.494 196.452 1.00 29.71 ? 4389 HIS A CA    1 
ATOM   21028 C C     . HIS A 1 4389 ? 170.422 203.992 197.811 1.00 28.68 ? 4389 HIS A C     1 
ATOM   21029 O O     . HIS A 1 4389 ? 169.581 204.895 197.887 1.00 30.61 ? 4389 HIS A O     1 
ATOM   21030 C CB    . HIS A 1 4389 ? 170.180 202.198 196.075 1.00 31.28 ? 4389 HIS A CB    1 
ATOM   21031 C CG    . HIS A 1 4389 ? 168.690 202.325 196.024 1.00 34.77 ? 4389 HIS A CG    1 
ATOM   21032 N ND1   . HIS A 1 4389 ? 168.033 202.977 195.002 1.00 33.20 ? 4389 HIS A ND1   1 
ATOM   21033 C CD2   . HIS A 1 4389 ? 167.728 201.889 196.871 1.00 32.63 ? 4389 HIS A CD2   1 
ATOM   21034 C CE1   . HIS A 1 4389 ? 166.731 202.934 195.221 1.00 32.61 ? 4389 HIS A CE1   1 
ATOM   21035 N NE2   . HIS A 1 4389 ? 166.519 202.280 196.349 1.00 34.67 ? 4389 HIS A NE2   1 
ATOM   21036 N N     . LEU A 1 4390 ? 170.947 203.417 198.895 1.00 25.94 ? 4390 LEU A N     1 
ATOM   21037 C CA    . LEU A 1 4390 ? 170.470 203.782 200.225 1.00 26.70 ? 4390 LEU A CA    1 
ATOM   21038 C C     . LEU A 1 4390 ? 171.050 205.117 200.685 1.00 25.80 ? 4390 LEU A C     1 
ATOM   21039 O O     . LEU A 1 4390 ? 170.352 205.909 201.330 1.00 24.04 ? 4390 LEU A O     1 
ATOM   21040 C CB    . LEU A 1 4390 ? 170.797 202.660 201.213 1.00 24.76 ? 4390 LEU A CB    1 
ATOM   21041 C CG    . LEU A 1 4390 ? 170.246 202.719 202.640 1.00 25.78 ? 4390 LEU A CG    1 
ATOM   21042 C CD1   . LEU A 1 4390 ? 170.117 201.311 203.177 1.00 27.20 ? 4390 LEU A CD1   1 
ATOM   21043 C CD2   . LEU A 1 4390 ? 171.139 203.531 203.561 1.00 22.85 ? 4390 LEU A CD2   1 
ATOM   21044 N N     . ILE A 1 4391 ? 172.314 205.380 200.376 1.00 23.24 ? 4391 ILE A N     1 
ATOM   21045 C CA    . ILE A 1 4391 ? 172.939 206.642 200.796 1.00 21.87 ? 4391 ILE A CA    1 
ATOM   21046 C C     . ILE A 1 4391 ? 172.263 207.803 200.074 1.00 25.14 ? 4391 ILE A C     1 
ATOM   21047 O O     . ILE A 1 4391 ? 172.087 207.746 198.844 1.00 25.96 ? 4391 ILE A O     1 
ATOM   21048 C CB    . ILE A 1 4391 ? 174.442 206.615 200.511 1.00 18.47 ? 4391 ILE A CB    1 
ATOM   21049 C CG1   . ILE A 1 4391 ? 175.162 205.735 201.534 1.00 20.51 ? 4391 ILE A CG1   1 
ATOM   21050 C CG2   . ILE A 1 4391 ? 175.019 208.022 200.530 1.00 20.71 ? 4391 ILE A CG2   1 
ATOM   21051 C CD1   . ILE A 1 4391 ? 176.667 205.741 201.391 1.00 20.53 ? 4391 ILE A CD1   1 
ATOM   21052 N N     . PRO A 1 4392 ? 171.865 208.860 200.779 1.00 23.48 ? 4392 PRO A N     1 
ATOM   21053 C CA    . PRO A 1 4392 ? 171.176 209.973 200.119 1.00 23.05 ? 4392 PRO A CA    1 
ATOM   21054 C C     . PRO A 1 4392 ? 172.087 210.714 199.153 1.00 23.92 ? 4392 PRO A C     1 
ATOM   21055 O O     . PRO A 1 4392 ? 173.314 210.592 199.180 1.00 21.82 ? 4392 PRO A O     1 
ATOM   21056 C CB    . PRO A 1 4392 ? 170.758 210.874 201.287 1.00 18.54 ? 4392 PRO A CB    1 
ATOM   21057 C CG    . PRO A 1 4392 ? 170.762 209.977 202.484 1.00 20.02 ? 4392 PRO A CG    1 
ATOM   21058 C CD    . PRO A 1 4392 ? 171.878 209.010 202.242 1.00 21.39 ? 4392 PRO A CD    1 
ATOM   21059 N N     . GLN A 1 4393 ? 171.455 211.504 198.291 1.00 27.10 ? 4393 GLN A N     1 
ATOM   21060 C CA    . GLN A 1 4393 ? 172.158 212.250 197.255 1.00 23.09 ? 4393 GLN A CA    1 
ATOM   21061 C C     . GLN A 1 4393 ? 172.889 213.435 197.886 1.00 24.60 ? 4393 GLN A C     1 
ATOM   21062 O O     . GLN A 1 4393 ? 172.987 213.564 199.109 1.00 29.32 ? 4393 GLN A O     1 
ATOM   21063 C CB    . GLN A 1 4393 ? 171.181 212.690 196.170 1.00 22.15 ? 4393 GLN A CB    1 
ATOM   21064 C CG    . GLN A 1 4393 ? 170.258 211.584 195.681 1.00 24.74 ? 4393 GLN A CG    1 
ATOM   21065 C CD    . GLN A 1 4393 ? 171.009 210.442 195.025 1.00 27.16 ? 4393 GLN A CD    1 
ATOM   21066 O OE1   . GLN A 1 4393 ? 170.785 209.274 195.342 1.00 26.84 ? 4393 GLN A OE1   1 
ATOM   21067 N NE2   . GLN A 1 4393 ? 171.906 210.775 194.104 1.00 26.50 ? 4393 GLN A NE2   1 
ATOM   21068 N N     . THR A 1 4394 ? 173.415 214.318 197.038 1.00 21.83 ? 4394 THR A N     1 
ATOM   21069 C CA    . THR A 1 4394 ? 174.255 215.420 197.487 1.00 23.04 ? 4394 THR A CA    1 
ATOM   21070 C C     . THR A 1 4394 ? 173.539 216.285 198.524 1.00 19.04 ? 4394 THR A C     1 
ATOM   21071 O O     . THR A 1 4394 ? 172.309 216.354 198.582 1.00 17.57 ? 4394 THR A O     1 
ATOM   21072 C CB    . THR A 1 4394 ? 174.676 216.287 196.300 1.00 25.00 ? 4394 THR A CB    1 
ATOM   21073 O OG1   . THR A 1 4394 ? 173.542 217.013 195.810 1.00 24.05 ? 4394 THR A OG1   1 
ATOM   21074 C CG2   . THR A 1 4394 ? 175.239 215.421 195.183 1.00 21.28 ? 4394 THR A CG2   1 
ATOM   21075 N N     . LEU A 1 4395 ? 174.341 216.951 199.350 1.00 21.39 ? 4395 LEU A N     1 
ATOM   21076 C CA    . LEU A 1 4395 ? 173.858 217.772 200.451 1.00 23.08 ? 4395 LEU A CA    1 
ATOM   21077 C C     . LEU A 1 4395 ? 174.037 219.246 200.109 1.00 23.62 ? 4395 LEU A C     1 
ATOM   21078 O O     . LEU A 1 4395 ? 175.096 219.656 199.623 1.00 22.18 ? 4395 LEU A O     1 
ATOM   21079 C CB    . LEU A 1 4395 ? 174.602 217.430 201.745 1.00 19.89 ? 4395 LEU A CB    1 
ATOM   21080 C CG    . LEU A 1 4395 ? 174.272 218.218 203.011 1.00 20.30 ? 4395 LEU A CG    1 
ATOM   21081 C CD1   . LEU A 1 4395 ? 172.831 217.983 203.430 1.00 15.99 ? 4395 LEU A CD1   1 
ATOM   21082 C CD2   . LEU A 1 4395 ? 175.226 217.822 204.122 1.00 18.24 ? 4395 LEU A CD2   1 
ATOM   21083 N N     . SER A 1 4396 ? 173.000 220.037 200.366 1.00 24.26 ? 4396 SER A N     1 
ATOM   21084 C CA    . SER A 1 4396 ? 172.958 221.435 199.961 1.00 24.38 ? 4396 SER A CA    1 
ATOM   21085 C C     . SER A 1 4396 ? 173.218 222.356 201.146 1.00 24.92 ? 4396 SER A C     1 
ATOM   21086 O O     . SER A 1 4396 ? 172.716 222.126 202.250 1.00 25.31 ? 4396 SER A O     1 
ATOM   21087 C CB    . SER A 1 4396 ? 171.605 221.773 199.333 1.00 27.55 ? 4396 SER A CB    1 
ATOM   21088 O OG    . SER A 1 4396 ? 170.550 221.548 200.250 1.00 30.43 ? 4396 SER A OG    1 
ATOM   21089 N N     . HIS A 1 4397 ? 174.005 223.401 200.905 1.00 30.20 ? 4397 HIS A N     1 
ATOM   21090 C CA    . HIS A 1 4397 ? 174.311 224.439 201.885 1.00 30.31 ? 4397 HIS A CA    1 
ATOM   21091 C C     . HIS A 1 4397 ? 174.196 225.817 201.245 1.00 35.04 ? 4397 HIS A C     1 
ATOM   21092 O O     . HIS A 1 4397 ? 175.091 226.659 201.348 1.00 36.45 ? 4397 HIS A O     1 
ATOM   21093 C CB    . HIS A 1 4397 ? 175.698 224.236 202.487 1.00 28.27 ? 4397 HIS A CB    1 
ATOM   21094 C CG    . HIS A 1 4397 ? 176.796 224.165 201.473 1.00 29.66 ? 4397 HIS A CG    1 
ATOM   21095 N ND1   . HIS A 1 4397 ? 177.050 223.034 200.728 1.00 28.97 ? 4397 HIS A ND1   1 
ATOM   21096 C CD2   . HIS A 1 4397 ? 177.712 225.084 201.087 1.00 28.75 ? 4397 HIS A CD2   1 
ATOM   21097 C CE1   . HIS A 1 4397 ? 178.075 223.260 199.925 1.00 27.24 ? 4397 HIS A CE1   1 
ATOM   21098 N NE2   . HIS A 1 4397 ? 178.495 224.496 200.123 1.00 25.85 ? 4397 HIS A NE2   1 
ATOM   21099 N N     . LEU A 1 4398 ? 173.068 226.069 200.576 1.00 37.20 ? 4398 LEU A N     1 
ATOM   21100 C CA    . LEU A 1 4398 ? 172.891 227.259 199.751 1.00 35.85 ? 4398 LEU A CA    1 
ATOM   21101 C C     . LEU A 1 4398 ? 172.231 228.412 200.500 1.00 36.91 ? 4398 LEU A C     1 
ATOM   21102 O O     . LEU A 1 4398 ? 171.511 229.212 199.887 1.00 35.55 ? 4398 LEU A O     1 
ATOM   21103 C CB    . LEU A 1 4398 ? 172.086 226.910 198.498 1.00 32.28 ? 4398 LEU A CB    1 
ATOM   21104 C CG    . LEU A 1 4398 ? 172.601 225.712 197.697 1.00 35.33 ? 4398 LEU A CG    1 
ATOM   21105 C CD1   . LEU A 1 4398 ? 171.620 225.334 196.596 1.00 33.54 ? 4398 LEU A CD1   1 
ATOM   21106 C CD2   . LEU A 1 4398 ? 173.981 226.000 197.122 1.00 32.87 ? 4398 LEU A CD2   1 
ATOM   21107 N N     . LYS A 1 4399 ? 172.455 228.522 201.808 1.00 34.01 ? 4399 LYS A N     1 
ATOM   21108 C CA    . LYS A 1 4399 ? 171.889 229.596 202.617 1.00 28.76 ? 4399 LYS A CA    1 
ATOM   21109 C C     . LYS A 1 4399 ? 173.024 230.280 203.364 1.00 28.70 ? 4399 LYS A C     1 
ATOM   21110 O O     . LYS A 1 4399 ? 173.696 229.647 204.183 1.00 34.80 ? 4399 LYS A O     1 
ATOM   21111 C CB    . LYS A 1 4399 ? 170.849 229.055 203.599 1.00 26.95 ? 4399 LYS A CB    1 
ATOM   21112 C CG    . LYS A 1 4399 ? 169.525 228.674 202.967 1.00 29.61 ? 4399 LYS A CG    1 
ATOM   21113 C CD    . LYS A 1 4399 ? 169.566 227.240 202.473 1.00 29.70 ? 4399 LYS A CD    1 
ATOM   21114 C CE    . LYS A 1 4399 ? 169.729 226.273 203.629 1.00 28.46 ? 4399 LYS A CE    1 
ATOM   21115 N NZ    . LYS A 1 4399 ? 169.722 224.857 203.172 1.00 30.62 ? 4399 LYS A NZ    1 
ATOM   21116 N N     . ARG A 1 4400 ? 173.255 231.559 203.068 1.00 29.03 ? 4400 ARG A N     1 
ATOM   21117 C CA    . ARG A 1 4400 ? 174.212 232.357 203.835 1.00 27.15 ? 4400 ARG A CA    1 
ATOM   21118 C C     . ARG A 1 4400 ? 173.839 233.826 203.657 1.00 30.85 ? 4400 ARG A C     1 
ATOM   21119 O O     . ARG A 1 4400 ? 174.111 234.415 202.607 1.00 34.27 ? 4400 ARG A O     1 
ATOM   21120 C CB    . ARG A 1 4400 ? 175.643 232.083 203.395 1.00 29.45 ? 4400 ARG A CB    1 
ATOM   21121 C CG    . ARG A 1 4400 ? 176.688 232.640 204.345 1.00 27.94 ? 4400 ARG A CG    1 
ATOM   21122 C CD    . ARG A 1 4400 ? 178.092 232.397 203.829 1.00 30.10 ? 4400 ARG A CD    1 
ATOM   21123 N NE    . ARG A 1 4400 ? 179.083 233.169 204.568 1.00 32.87 ? 4400 ARG A NE    1 
ATOM   21124 C CZ    . ARG A 1 4400 ? 179.796 232.697 205.582 1.00 31.28 ? 4400 ARG A CZ    1 
ATOM   21125 N NH1   . ARG A 1 4400 ? 179.652 231.453 206.007 1.00 30.52 ? 4400 ARG A NH1   1 
ATOM   21126 N NH2   . ARG A 1 4400 ? 180.676 233.492 206.182 1.00 29.71 ? 4400 ARG A NH2   1 
ATOM   21127 N N     . THR A 1 4401 ? 173.214 234.403 204.678 1.00 29.86 ? 4401 THR A N     1 
ATOM   21128 C CA    . THR A 1 4401 ? 172.840 235.810 204.680 1.00 29.21 ? 4401 THR A CA    1 
ATOM   21129 C C     . THR A 1 4401 ? 173.704 236.549 205.696 1.00 32.57 ? 4401 THR A C     1 
ATOM   21130 O O     . THR A 1 4401 ? 174.273 235.936 206.603 1.00 34.93 ? 4401 THR A O     1 
ATOM   21131 C CB    . THR A 1 4401 ? 171.354 235.973 205.013 1.00 30.40 ? 4401 THR A CB    1 
ATOM   21132 O OG1   . THR A 1 4401 ? 170.590 235.043 204.236 1.00 30.60 ? 4401 THR A OG1   1 
ATOM   21133 C CG2   . THR A 1 4401 ? 170.867 237.380 204.689 1.00 30.00 ? 4401 THR A CG2   1 
ATOM   21134 N N     . VAL A 1 4402 ? 173.815 237.869 205.529 1.00 26.65 ? 4402 VAL A N     1 
ATOM   21135 C CA    . VAL A 1 4402 ? 174.643 238.663 206.431 1.00 25.46 ? 4402 VAL A CA    1 
ATOM   21136 C C     . VAL A 1 4402 ? 174.067 238.655 207.844 1.00 29.06 ? 4402 VAL A C     1 
ATOM   21137 O O     . VAL A 1 4402 ? 174.810 238.648 208.832 1.00 27.55 ? 4402 VAL A O     1 
ATOM   21138 C CB    . VAL A 1 4402 ? 174.806 240.095 205.884 1.00 27.89 ? 4402 VAL A CB    1 
ATOM   21139 C CG1   . VAL A 1 4402 ? 173.449 240.743 205.649 1.00 28.12 ? 4402 VAL A CG1   1 
ATOM   21140 C CG2   . VAL A 1 4402 ? 175.655 240.939 206.825 1.00 27.64 ? 4402 VAL A CG2   1 
ATOM   21141 N N     . GLU A 1 4403 ? 172.737 238.643 207.965 1.00 30.76 ? 4403 GLU A N     1 
ATOM   21142 C CA    . GLU A 1 4403 ? 172.115 238.739 209.281 1.00 28.96 ? 4403 GLU A CA    1 
ATOM   21143 C C     . GLU A 1 4403 ? 172.268 237.465 210.101 1.00 29.44 ? 4403 GLU A C     1 
ATOM   21144 O O     . GLU A 1 4403 ? 172.250 237.536 211.335 1.00 30.19 ? 4403 GLU A O     1 
ATOM   21145 C CB    . GLU A 1 4403 ? 170.631 239.092 209.146 1.00 29.40 ? 4403 GLU A CB    1 
ATOM   21146 C CG    . GLU A 1 4403 ? 169.718 237.906 208.875 1.00 30.59 ? 4403 GLU A CG    1 
ATOM   21147 C CD    . GLU A 1 4403 ? 168.250 238.284 208.896 1.00 32.16 ? 4403 GLU A CD    1 
ATOM   21148 O OE1   . GLU A 1 4403 ? 167.910 239.315 209.514 1.00 28.20 ? 4403 GLU A OE1   1 
ATOM   21149 O OE2   . GLU A 1 4403 ? 167.436 237.549 208.298 1.00 34.20 ? 4403 GLU A OE2   1 
ATOM   21150 N N     . ASN A 1 4404 ? 172.416 236.308 209.459 1.00 25.63 ? 4404 ASN A N     1 
ATOM   21151 C CA    . ASN A 1 4404 ? 172.523 235.053 210.190 1.00 27.19 ? 4404 ASN A CA    1 
ATOM   21152 C C     . ASN A 1 4404 ? 173.960 234.619 210.450 1.00 25.51 ? 4404 ASN A C     1 
ATOM   21153 O O     . ASN A 1 4404 ? 174.167 233.557 211.046 1.00 26.40 ? 4404 ASN A O     1 
ATOM   21154 C CB    . ASN A 1 4404 ? 171.763 233.938 209.454 1.00 27.26 ? 4404 ASN A CB    1 
ATOM   21155 C CG    . ASN A 1 4404 ? 172.310 233.659 208.065 1.00 23.66 ? 4404 ASN A CG    1 
ATOM   21156 O OD1   . ASN A 1 4404 ? 173.518 233.573 207.855 1.00 22.41 ? 4404 ASN A OD1   1 
ATOM   21157 N ND2   . ASN A 1 4404 ? 171.407 233.486 207.109 1.00 22.20 ? 4404 ASN A ND2   1 
ATOM   21158 N N     . ILE A 1 4405 ? 174.953 235.398 210.019 1.00 24.06 ? 4405 ILE A N     1 
ATOM   21159 C CA    . ILE A 1 4405 ? 176.334 235.071 210.359 1.00 22.62 ? 4405 ILE A CA    1 
ATOM   21160 C C     . ILE A 1 4405 ? 176.588 235.313 211.843 1.00 24.13 ? 4405 ILE A C     1 
ATOM   21161 O O     . ILE A 1 4405 ? 177.507 234.732 212.432 1.00 22.26 ? 4405 ILE A O     1 
ATOM   21162 C CB    . ILE A 1 4405 ? 177.314 235.863 209.473 1.00 24.62 ? 4405 ILE A CB    1 
ATOM   21163 C CG1   . ILE A 1 4405 ? 178.623 235.089 209.310 1.00 24.30 ? 4405 ILE A CG1   1 
ATOM   21164 C CG2   . ILE A 1 4405 ? 177.581 237.244 210.048 1.00 27.62 ? 4405 ILE A CG2   1 
ATOM   21165 C CD1   . ILE A 1 4405 ? 179.591 235.729 208.346 1.00 25.09 ? 4405 ILE A CD1   1 
ATOM   21166 N N     . LYS A 1 4406 ? 175.787 236.180 212.468 1.00 20.30 ? 4406 LYS A N     1 
ATOM   21167 C CA    . LYS A 1 4406 ? 175.945 236.433 213.896 1.00 19.88 ? 4406 LYS A CA    1 
ATOM   21168 C C     . LYS A 1 4406 ? 175.456 235.254 214.726 1.00 22.09 ? 4406 LYS A C     1 
ATOM   21169 O O     . LYS A 1 4406 ? 175.932 235.034 215.846 1.00 25.13 ? 4406 LYS A O     1 
ATOM   21170 C CB    . LYS A 1 4406 ? 175.201 237.709 214.293 1.00 26.02 ? 4406 LYS A CB    1 
ATOM   21171 C CG    . LYS A 1 4406 ? 176.066 238.958 214.309 1.00 25.26 ? 4406 LYS A CG    1 
ATOM   21172 C CD    . LYS A 1 4406 ? 176.342 239.464 212.904 1.00 22.38 ? 4406 LYS A CD    1 
ATOM   21173 C CE    . LYS A 1 4406 ? 175.077 240.012 212.266 1.00 22.52 ? 4406 LYS A CE    1 
ATOM   21174 N NZ    . LYS A 1 4406 ? 175.335 240.565 210.909 1.00 26.79 ? 4406 LYS A NZ    1 
ATOM   21175 N N     . ASP A 1 4407 ? 174.504 234.486 214.198 1.00 20.39 ? 4407 ASP A N     1 
ATOM   21176 C CA    . ASP A 1 4407 ? 173.914 233.375 214.933 1.00 17.79 ? 4407 ASP A CA    1 
ATOM   21177 C C     . ASP A 1 4407 ? 174.936 232.260 215.108 1.00 17.31 ? 4407 ASP A C     1 
ATOM   21178 O O     . ASP A 1 4407 ? 175.434 231.714 214.116 1.00 20.26 ? 4407 ASP A O     1 
ATOM   21179 C CB    . ASP A 1 4407 ? 172.674 232.855 214.203 1.00 14.14 ? 4407 ASP A CB    1 
ATOM   21180 C CG    . ASP A 1 4407 ? 171.931 231.796 214.992 1.00 17.66 ? 4407 ASP A CG    1 
ATOM   21181 O OD1   . ASP A 1 4407 ? 172.109 231.733 216.225 1.00 18.72 ? 4407 ASP A OD1   1 
ATOM   21182 O OD2   . ASP A 1 4407 ? 171.163 231.026 214.378 1.00 18.55 ? 4407 ASP A OD2   1 
ATOM   21183 N N     . PRO A 1 4408 ? 175.283 231.902 216.349 1.00 13.67 ? 4408 PRO A N     1 
ATOM   21184 C CA    . PRO A 1 4408 ? 176.222 230.784 216.544 1.00 10.24 ? 4408 PRO A CA    1 
ATOM   21185 C C     . PRO A 1 4408 ? 175.665 229.457 216.071 1.00 9.59  ? 4408 PRO A C     1 
ATOM   21186 O O     . PRO A 1 4408 ? 176.416 228.618 215.554 1.00 11.95 ? 4408 PRO A O     1 
ATOM   21187 C CB    . PRO A 1 4408 ? 176.465 230.792 218.059 1.00 7.97  ? 4408 PRO A CB    1 
ATOM   21188 C CG    . PRO A 1 4408 ? 176.008 232.141 218.524 1.00 9.28  ? 4408 PRO A CG    1 
ATOM   21189 C CD    . PRO A 1 4408 ? 174.877 232.504 217.627 1.00 10.20 ? 4408 PRO A CD    1 
ATOM   21190 N N     . LEU A 1 4409 ? 174.357 229.245 216.235 1.00 10.68 ? 4409 LEU A N     1 
ATOM   21191 C CA    . LEU A 1 4409 ? 173.743 228.019 215.741 1.00 7.68  ? 4409 LEU A CA    1 
ATOM   21192 C C     . LEU A 1 4409 ? 173.904 227.902 214.237 1.00 13.58 ? 4409 LEU A C     1 
ATOM   21193 O O     . LEU A 1 4409 ? 174.216 226.823 213.722 1.00 15.84 ? 4409 LEU A O     1 
ATOM   21194 C CB    . LEU A 1 4409 ? 172.263 227.971 216.116 1.00 9.13  ? 4409 LEU A CB    1 
ATOM   21195 C CG    . LEU A 1 4409 ? 171.902 227.908 217.596 1.00 11.43 ? 4409 LEU A CG    1 
ATOM   21196 C CD1   . LEU A 1 4409 ? 170.430 228.221 217.781 1.00 13.88 ? 4409 LEU A CD1   1 
ATOM   21197 C CD2   . LEU A 1 4409 ? 172.238 226.540 218.155 1.00 9.72  ? 4409 LEU A CD2   1 
ATOM   21198 N N     . PHE A 1 4410 ? 173.697 229.004 213.513 1.00 16.31 ? 4410 PHE A N     1 
ATOM   21199 C CA    . PHE A 1 4410 ? 173.864 228.958 212.067 1.00 13.47 ? 4410 PHE A CA    1 
ATOM   21200 C C     . PHE A 1 4410 ? 175.308 228.671 211.689 1.00 12.02 ? 4410 PHE A C     1 
ATOM   21201 O O     . PHE A 1 4410 ? 175.564 227.924 210.745 1.00 14.94 ? 4410 PHE A O     1 
ATOM   21202 C CB    . PHE A 1 4410 ? 173.412 230.258 211.414 1.00 12.79 ? 4410 PHE A CB    1 
ATOM   21203 C CG    . PHE A 1 4410 ? 173.526 230.230 209.922 1.00 14.76 ? 4410 PHE A CG    1 
ATOM   21204 C CD1   . PHE A 1 4410 ? 172.597 229.544 209.161 1.00 16.33 ? 4410 PHE A CD1   1 
ATOM   21205 C CD2   . PHE A 1 4410 ? 174.601 230.821 209.283 1.00 15.76 ? 4410 PHE A CD2   1 
ATOM   21206 C CE1   . PHE A 1 4410 ? 172.710 229.493 207.790 1.00 13.45 ? 4410 PHE A CE1   1 
ATOM   21207 C CE2   . PHE A 1 4410 ? 174.721 230.766 207.914 1.00 17.54 ? 4410 PHE A CE2   1 
ATOM   21208 C CZ    . PHE A 1 4410 ? 173.773 230.104 207.168 1.00 16.57 ? 4410 PHE A CZ    1 
ATOM   21209 N N     . ARG A 1 4411 ? 176.267 229.273 212.393 1.00 11.61 ? 4411 ARG A N     1 
ATOM   21210 C CA    . ARG A 1 4411 ? 177.671 229.031 212.074 1.00 10.03 ? 4411 ARG A CA    1 
ATOM   21211 C C     . ARG A 1 4411 ? 178.035 227.568 212.291 1.00 9.07  ? 4411 ARG A C     1 
ATOM   21212 O O     . ARG A 1 4411 ? 178.687 226.940 211.444 1.00 10.04 ? 4411 ARG A O     1 
ATOM   21213 C CB    . ARG A 1 4411 ? 178.561 229.941 212.919 1.00 10.52 ? 4411 ARG A CB    1 
ATOM   21214 C CG    . ARG A 1 4411 ? 178.794 231.312 212.314 1.00 14.90 ? 4411 ARG A CG    1 
ATOM   21215 C CD    . ARG A 1 4411 ? 179.609 232.181 213.250 1.00 12.57 ? 4411 ARG A CD    1 
ATOM   21216 N NE    . ARG A 1 4411 ? 178.814 232.671 214.369 1.00 13.56 ? 4411 ARG A NE    1 
ATOM   21217 C CZ    . ARG A 1 4411 ? 179.300 232.924 215.576 1.00 15.42 ? 4411 ARG A CZ    1 
ATOM   21218 N NH1   . ARG A 1 4411 ? 180.575 232.721 215.865 1.00 12.13 ? 4411 ARG A NH1   1 
ATOM   21219 N NH2   . ARG A 1 4411 ? 178.485 233.389 216.519 1.00 14.63 ? 4411 ARG A NH2   1 
ATOM   21220 N N     . PHE A 1 4412 ? 177.605 227.002 213.422 1.00 12.87 ? 4412 PHE A N     1 
ATOM   21221 C CA    . PHE A 1 4412 ? 177.882 225.596 213.693 1.00 6.93  ? 4412 PHE A CA    1 
ATOM   21222 C C     . PHE A 1 4412 ? 177.227 224.697 212.656 1.00 14.23 ? 4412 PHE A C     1 
ATOM   21223 O O     . PHE A 1 4412 ? 177.859 223.774 212.131 1.00 18.35 ? 4412 PHE A O     1 
ATOM   21224 C CB    . PHE A 1 4412 ? 177.397 225.213 215.089 1.00 3.85  ? 4412 PHE A CB    1 
ATOM   21225 C CG    . PHE A 1 4412 ? 177.234 223.736 215.269 1.00 5.81  ? 4412 PHE A CG    1 
ATOM   21226 C CD1   . PHE A 1 4412 ? 178.340 222.904 215.273 1.00 11.58 ? 4412 PHE A CD1   1 
ATOM   21227 C CD2   . PHE A 1 4412 ? 175.978 223.172 215.385 1.00 7.60  ? 4412 PHE A CD2   1 
ATOM   21228 C CE1   . PHE A 1 4412 ? 178.196 221.545 215.417 1.00 7.06  ? 4412 PHE A CE1   1 
ATOM   21229 C CE2   . PHE A 1 4412 ? 175.831 221.813 215.524 1.00 3.22  ? 4412 PHE A CE2   1 
ATOM   21230 C CZ    . PHE A 1 4412 ? 176.943 221.000 215.543 1.00 1.30  ? 4412 PHE A CZ    1 
ATOM   21231 N N     . PHE A 1 4413 ? 175.949 224.943 212.358 1.00 15.27 ? 4413 PHE A N     1 
ATOM   21232 C CA    . PHE A 1 4413 ? 175.239 224.110 211.396 1.00 5.12  ? 4413 PHE A CA    1 
ATOM   21233 C C     . PHE A 1 4413 ? 175.829 224.253 210.002 1.00 7.24  ? 4413 PHE A C     1 
ATOM   21234 O O     . PHE A 1 4413 ? 175.881 223.281 209.247 1.00 13.55 ? 4413 PHE A O     1 
ATOM   21235 C CB    . PHE A 1 4413 ? 173.754 224.464 211.399 1.00 8.82  ? 4413 PHE A CB    1 
ATOM   21236 C CG    . PHE A 1 4413 ? 172.980 223.807 212.502 1.00 7.58  ? 4413 PHE A CG    1 
ATOM   21237 C CD1   . PHE A 1 4413 ? 173.350 222.561 212.977 1.00 4.68  ? 4413 PHE A CD1   1 
ATOM   21238 C CD2   . PHE A 1 4413 ? 171.894 224.442 213.079 1.00 12.38 ? 4413 PHE A CD2   1 
ATOM   21239 C CE1   . PHE A 1 4413 ? 172.644 221.955 213.992 1.00 8.92  ? 4413 PHE A CE1   1 
ATOM   21240 C CE2   . PHE A 1 4413 ? 171.185 223.840 214.098 1.00 7.62  ? 4413 PHE A CE2   1 
ATOM   21241 C CZ    . PHE A 1 4413 ? 171.560 222.595 214.554 1.00 10.93 ? 4413 PHE A CZ    1 
ATOM   21242 N N     . GLU A 1 4414 ? 176.288 225.452 209.645 1.00 3.72  ? 4414 GLU A N     1 
ATOM   21243 C CA    . GLU A 1 4414 ? 176.903 225.662 208.342 1.00 3.80  ? 4414 GLU A CA    1 
ATOM   21244 C C     . GLU A 1 4414 ? 178.204 224.886 208.223 1.00 5.22  ? 4414 GLU A C     1 
ATOM   21245 O O     . GLU A 1 4414 ? 178.448 224.216 207.214 1.00 9.78  ? 4414 GLU A O     1 
ATOM   21246 C CB    . GLU A 1 4414 ? 177.138 227.155 208.115 1.00 12.84 ? 4414 GLU A CB    1 
ATOM   21247 C CG    . GLU A 1 4414 ? 177.750 227.497 206.769 1.00 17.07 ? 4414 GLU A CG    1 
ATOM   21248 C CD    . GLU A 1 4414 ? 179.219 227.854 206.871 1.00 17.21 ? 4414 GLU A CD    1 
ATOM   21249 O OE1   . GLU A 1 4414 ? 179.880 227.964 205.817 1.00 13.42 ? 4414 GLU A OE1   1 
ATOM   21250 O OE2   . GLU A 1 4414 ? 179.712 228.024 208.005 1.00 14.32 ? 4414 GLU A OE2   1 
ATOM   21251 N N     . ARG A 1 4415 ? 179.056 224.960 209.248 1.00 8.89  ? 4415 ARG A N     1 
ATOM   21252 C CA    . ARG A 1 4415 ? 180.298 224.194 209.211 1.00 9.84  ? 4415 ARG A CA    1 
ATOM   21253 C C     . ARG A 1 4415 ? 180.019 222.695 209.190 1.00 13.29 ? 4415 ARG A C     1 
ATOM   21254 O O     . ARG A 1 4415 ? 180.666 221.944 208.446 1.00 15.07 ? 4415 ARG A O     1 
ATOM   21255 C CB    . ARG A 1 4415 ? 181.184 224.572 210.397 1.00 5.78  ? 4415 ARG A CB    1 
ATOM   21256 C CG    . ARG A 1 4415 ? 182.148 223.487 210.838 1.00 6.05  ? 4415 ARG A CG    1 
ATOM   21257 C CD    . ARG A 1 4415 ? 182.617 223.733 212.258 1.00 9.18  ? 4415 ARG A CD    1 
ATOM   21258 N NE    . ARG A 1 4415 ? 183.294 225.019 212.373 1.00 13.35 ? 4415 ARG A NE    1 
ATOM   21259 C CZ    . ARG A 1 4415 ? 183.164 225.849 213.398 1.00 13.91 ? 4415 ARG A CZ    1 
ATOM   21260 N NH1   . ARG A 1 4415 ? 182.392 225.557 214.432 1.00 4.09  ? 4415 ARG A NH1   1 
ATOM   21261 N NH2   . ARG A 1 4415 ? 183.824 227.004 213.385 1.00 9.06  ? 4415 ARG A NH2   1 
ATOM   21262 N N     . GLU A 1 4416 ? 179.041 222.249 209.980 1.00 12.16 ? 4416 GLU A N     1 
ATOM   21263 C CA    . GLU A 1 4416 ? 178.681 220.837 210.014 1.00 6.15  ? 4416 GLU A CA    1 
ATOM   21264 C C     . GLU A 1 4416 ? 178.178 220.364 208.657 1.00 9.61  ? 4416 GLU A C     1 
ATOM   21265 O O     . GLU A 1 4416 ? 178.595 219.312 208.161 1.00 11.97 ? 4416 GLU A O     1 
ATOM   21266 C CB    . GLU A 1 4416 ? 177.620 220.609 211.091 1.00 4.30  ? 4416 GLU A CB    1 
ATOM   21267 C CG    . GLU A 1 4416 ? 177.357 219.158 211.428 1.00 7.64  ? 4416 GLU A CG    1 
ATOM   21268 C CD    . GLU A 1 4416 ? 178.260 218.647 212.529 1.00 14.83 ? 4416 GLU A CD    1 
ATOM   21269 O OE1   . GLU A 1 4416 ? 179.146 219.403 212.980 1.00 11.20 ? 4416 GLU A OE1   1 
ATOM   21270 O OE2   . GLU A 1 4416 ? 178.075 217.489 212.952 1.00 13.93 ? 4416 GLU A OE2   1 
ATOM   21271 N N     . VAL A 1 4417 ? 177.287 221.139 208.036 1.00 11.48 ? 4417 VAL A N     1 
ATOM   21272 C CA    . VAL A 1 4417 ? 176.713 220.757 206.751 1.00 7.99  ? 4417 VAL A CA    1 
ATOM   21273 C C     . VAL A 1 4417 ? 177.777 220.784 205.664 1.00 9.73  ? 4417 VAL A C     1 
ATOM   21274 O O     . VAL A 1 4417 ? 177.800 219.921 204.783 1.00 16.27 ? 4417 VAL A O     1 
ATOM   21275 C CB    . VAL A 1 4417 ? 175.520 221.669 206.406 1.00 8.07  ? 4417 VAL A CB    1 
ATOM   21276 C CG1   . VAL A 1 4417 ? 175.188 221.585 204.929 1.00 10.36 ? 4417 VAL A CG1   1 
ATOM   21277 C CG2   . VAL A 1 4417 ? 174.309 221.297 207.240 1.00 13.61 ? 4417 VAL A CG2   1 
ATOM   21278 N N     . LYS A 1 4418 ? 178.682 221.763 205.712 1.00 7.72  ? 4418 LYS A N     1 
ATOM   21279 C CA    . LYS A 1 4418 ? 179.748 221.830 204.719 1.00 9.72  ? 4418 LYS A CA    1 
ATOM   21280 C C     . LYS A 1 4418 ? 180.675 220.626 204.822 1.00 12.55 ? 4418 LYS A C     1 
ATOM   21281 O O     . LYS A 1 4418 ? 181.006 219.993 203.810 1.00 20.00 ? 4418 LYS A O     1 
ATOM   21282 C CB    . LYS A 1 4418 ? 180.528 223.134 204.884 1.00 11.98 ? 4418 LYS A CB    1 
ATOM   21283 C CG    . LYS A 1 4418 ? 181.868 223.157 204.170 1.00 12.23 ? 4418 LYS A CG    1 
ATOM   21284 C CD    . LYS A 1 4418 ? 182.578 224.479 204.392 1.00 16.26 ? 4418 LYS A CD    1 
ATOM   21285 C CE    . LYS A 1 4418 ? 182.667 224.814 205.872 1.00 18.66 ? 4418 LYS A CE    1 
ATOM   21286 N NZ    . LYS A 1 4418 ? 183.367 223.754 206.648 1.00 14.72 ? 4418 LYS A NZ    1 
ATOM   21287 N N     . MET A 1 4419 ? 181.103 220.288 206.042 1.00 13.72 ? 4419 MET A N     1 
ATOM   21288 C CA    . MET A 1 4419 ? 181.973 219.128 206.212 1.00 13.24 ? 4419 MET A CA    1 
ATOM   21289 C C     . MET A 1 4419 ? 181.257 217.842 205.818 1.00 11.64 ? 4419 MET A C     1 
ATOM   21290 O O     . MET A 1 4419 ? 181.841 216.975 205.153 1.00 15.14 ? 4419 MET A O     1 
ATOM   21291 C CB    . MET A 1 4419 ? 182.469 219.050 207.656 1.00 12.55 ? 4419 MET A CB    1 
ATOM   21292 C CG    . MET A 1 4419 ? 183.217 217.770 207.985 1.00 15.94 ? 4419 MET A CG    1 
ATOM   21293 S SD    . MET A 1 4419 ? 183.163 217.348 209.735 1.00 31.93 ? 4419 MET A SD    1 
ATOM   21294 C CE    . MET A 1 4419 ? 183.487 215.588 209.665 1.00 17.89 ? 4419 MET A CE    1 
ATOM   21295 N N     . GLY A 1 4420 ? 179.987 217.709 206.207 1.00 11.21 ? 4420 GLY A N     1 
ATOM   21296 C CA    . GLY A 1 4420 ? 179.228 216.532 205.831 1.00 11.96 ? 4420 GLY A CA    1 
ATOM   21297 C C     . GLY A 1 4420 ? 179.046 216.409 204.333 1.00 14.23 ? 4420 GLY A C     1 
ATOM   21298 O O     . GLY A 1 4420 ? 179.124 215.314 203.783 1.00 19.77 ? 4420 GLY A O     1 
ATOM   21299 N N     . ALA A 1 4421 ? 178.806 217.532 203.652 1.00 15.68 ? 4421 ALA A N     1 
ATOM   21300 C CA    . ALA A 1 4421 ? 178.646 217.507 202.204 1.00 13.87 ? 4421 ALA A CA    1 
ATOM   21301 C C     . ALA A 1 4421 ? 179.948 217.141 201.509 1.00 12.69 ? 4421 ALA A C     1 
ATOM   21302 O O     . ALA A 1 4421 ? 179.945 216.367 200.547 1.00 15.91 ? 4421 ALA A O     1 
ATOM   21303 C CB    . ALA A 1 4421 ? 178.135 218.858 201.707 1.00 13.13 ? 4421 ALA A CB    1 
ATOM   21304 N N     . LYS A 1 4422 ? 181.073 217.688 201.976 1.00 11.57 ? 4422 LYS A N     1 
ATOM   21305 C CA    . LYS A 1 4422 ? 182.357 217.324 201.385 1.00 15.30 ? 4422 LYS A CA    1 
ATOM   21306 C C     . LYS A 1 4422 ? 182.647 215.840 201.567 1.00 17.62 ? 4422 LYS A C     1 
ATOM   21307 O O     . LYS A 1 4422 ? 183.060 215.155 200.621 1.00 23.87 ? 4422 LYS A O     1 
ATOM   21308 C CB    . LYS A 1 4422 ? 183.477 218.167 201.993 1.00 16.37 ? 4422 LYS A CB    1 
ATOM   21309 C CG    . LYS A 1 4422 ? 184.867 217.737 201.561 1.00 16.36 ? 4422 LYS A CG    1 
ATOM   21310 C CD    . LYS A 1 4422 ? 185.937 218.352 202.446 1.00 16.90 ? 4422 LYS A CD    1 
ATOM   21311 C CE    . LYS A 1 4422 ? 185.662 218.071 203.915 1.00 18.26 ? 4422 LYS A CE    1 
ATOM   21312 N NZ    . LYS A 1 4422 ? 185.567 216.612 204.194 1.00 14.24 ? 4422 LYS A NZ    1 
ATOM   21313 N N     . LEU A 1 4423 ? 182.422 215.318 202.776 1.00 14.77 ? 4423 LEU A N     1 
ATOM   21314 C CA    . LEU A 1 4423 ? 182.685 213.904 203.022 1.00 15.16 ? 4423 LEU A CA    1 
ATOM   21315 C C     . LEU A 1 4423 ? 181.701 213.018 202.264 1.00 15.75 ? 4423 LEU A C     1 
ATOM   21316 O O     . LEU A 1 4423 ? 182.068 211.937 201.792 1.00 17.76 ? 4423 LEU A O     1 
ATOM   21317 C CB    . LEU A 1 4423 ? 182.653 213.627 204.525 1.00 14.58 ? 4423 LEU A CB    1 
ATOM   21318 C CG    . LEU A 1 4423 ? 182.642 212.190 205.034 1.00 15.61 ? 4423 LEU A CG    1 
ATOM   21319 C CD1   . LEU A 1 4423 ? 184.047 211.627 205.035 1.00 17.94 ? 4423 LEU A CD1   1 
ATOM   21320 C CD2   . LEU A 1 4423 ? 182.096 212.187 206.443 1.00 17.08 ? 4423 LEU A CD2   1 
ATOM   21321 N N     . LEU A 1 4424 ? 180.452 213.467 202.121 1.00 14.16 ? 4424 LEU A N     1 
ATOM   21322 C CA    . LEU A 1 4424 ? 179.480 212.735 201.319 1.00 13.29 ? 4424 LEU A CA    1 
ATOM   21323 C C     . LEU A 1 4424 ? 179.904 212.669 199.862 1.00 16.35 ? 4424 LEU A C     1 
ATOM   21324 O O     . LEU A 1 4424 ? 179.809 211.612 199.232 1.00 20.64 ? 4424 LEU A O     1 
ATOM   21325 C CB    . LEU A 1 4424 ? 178.104 213.389 201.437 1.00 14.11 ? 4424 LEU A CB    1 
ATOM   21326 C CG    . LEU A 1 4424 ? 176.999 212.800 200.559 1.00 14.02 ? 4424 LEU A CG    1 
ATOM   21327 C CD1   . LEU A 1 4424 ? 176.853 211.307 200.793 1.00 19.02 ? 4424 LEU A CD1   1 
ATOM   21328 C CD2   . LEU A 1 4424 ? 175.686 213.515 200.813 1.00 15.78 ? 4424 LEU A CD2   1 
ATOM   21329 N N     . GLN A 1 4425 ? 180.360 213.790 199.302 1.00 18.53 ? 4425 GLN A N     1 
ATOM   21330 C CA    . GLN A 1 4425 ? 180.821 213.780 197.920 1.00 15.16 ? 4425 GLN A CA    1 
ATOM   21331 C C     . GLN A 1 4425 ? 182.024 212.864 197.755 1.00 15.18 ? 4425 GLN A C     1 
ATOM   21332 O O     . GLN A 1 4425 ? 182.112 212.115 196.776 1.00 18.36 ? 4425 GLN A O     1 
ATOM   21333 C CB    . GLN A 1 4425 ? 181.153 215.198 197.457 1.00 16.64 ? 4425 GLN A CB    1 
ATOM   21334 C CG    . GLN A 1 4425 ? 179.955 216.133 197.401 1.00 16.85 ? 4425 GLN A CG    1 
ATOM   21335 C CD    . GLN A 1 4425 ? 178.722 215.475 196.809 1.00 20.32 ? 4425 GLN A CD    1 
ATOM   21336 O OE1   . GLN A 1 4425 ? 177.693 215.349 197.473 1.00 21.24 ? 4425 GLN A OE1   1 
ATOM   21337 N NE2   . GLN A 1 4425 ? 178.820 215.055 195.554 1.00 20.88 ? 4425 GLN A NE2   1 
ATOM   21338 N N     . ASP A 1 4426 ? 182.956 212.898 198.711 1.00 19.20 ? 4426 ASP A N     1 
ATOM   21339 C CA    . ASP A 1 4426 ? 184.120 212.020 198.633 1.00 20.11 ? 4426 ASP A CA    1 
ATOM   21340 C C     . ASP A 1 4426 ? 183.710 210.551 198.681 1.00 19.83 ? 4426 ASP A C     1 
ATOM   21341 O O     . ASP A 1 4426 ? 184.202 209.730 197.897 1.00 21.46 ? 4426 ASP A O     1 
ATOM   21342 C CB    . ASP A 1 4426 ? 185.094 212.346 199.764 1.00 15.02 ? 4426 ASP A CB    1 
ATOM   21343 C CG    . ASP A 1 4426 ? 186.516 211.937 199.442 1.00 21.74 ? 4426 ASP A CG    1 
ATOM   21344 O OD1   . ASP A 1 4426 ? 187.360 211.942 200.363 1.00 24.26 ? 4426 ASP A OD1   1 
ATOM   21345 O OD2   . ASP A 1 4426 ? 186.791 211.611 198.269 1.00 22.94 ? 4426 ASP A OD2   1 
ATOM   21346 N N     . VAL A 1 4427 ? 182.803 210.203 199.597 1.00 20.34 ? 4427 VAL A N     1 
ATOM   21347 C CA    . VAL A 1 4427 ? 182.365 208.815 199.731 1.00 16.71 ? 4427 VAL A CA    1 
ATOM   21348 C C     . VAL A 1 4427 ? 181.619 208.364 198.482 1.00 19.21 ? 4427 VAL A C     1 
ATOM   21349 O O     . VAL A 1 4427 ? 181.845 207.260 197.974 1.00 25.14 ? 4427 VAL A O     1 
ATOM   21350 C CB    . VAL A 1 4427 ? 181.507 208.649 200.999 1.00 17.93 ? 4427 VAL A CB    1 
ATOM   21351 C CG1   . VAL A 1 4427 ? 180.661 207.389 200.915 1.00 17.68 ? 4427 VAL A CG1   1 
ATOM   21352 C CG2   . VAL A 1 4427 ? 182.392 208.620 202.233 1.00 19.15 ? 4427 VAL A CG2   1 
ATOM   21353 N N     . ARG A 1 4428 ? 180.717 209.207 197.970 1.00 18.97 ? 4428 ARG A N     1 
ATOM   21354 C CA    . ARG A 1 4428 ? 179.992 208.880 196.746 1.00 19.57 ? 4428 ARG A CA    1 
ATOM   21355 C C     . ARG A 1 4428 ? 180.944 208.676 195.578 1.00 23.50 ? 4428 ARG A C     1 
ATOM   21356 O O     . ARG A 1 4428 ? 180.801 207.714 194.816 1.00 21.95 ? 4428 ARG A O     1 
ATOM   21357 C CB    . ARG A 1 4428 ? 178.985 209.985 196.422 1.00 17.30 ? 4428 ARG A CB    1 
ATOM   21358 C CG    . ARG A 1 4428 ? 177.825 210.109 197.394 1.00 17.59 ? 4428 ARG A CG    1 
ATOM   21359 C CD    . ARG A 1 4428 ? 176.525 210.427 196.669 1.00 18.62 ? 4428 ARG A CD    1 
ATOM   21360 N NE    . ARG A 1 4428 ? 176.136 209.406 195.705 1.00 17.25 ? 4428 ARG A NE    1 
ATOM   21361 C CZ    . ARG A 1 4428 ? 175.352 208.375 195.983 1.00 21.99 ? 4428 ARG A CZ    1 
ATOM   21362 N NH1   . ARG A 1 4428 ? 174.850 208.195 197.193 1.00 20.73 ? 4428 ARG A NH1   1 
ATOM   21363 N NH2   . ARG A 1 4428 ? 175.054 207.508 195.019 1.00 24.10 ? 4428 ARG A NH2   1 
ATOM   21364 N N     . GLN A 1 4429 ? 181.927 209.566 195.421 1.00 21.46 ? 4429 GLN A N     1 
ATOM   21365 C CA    . GLN A 1 4429 ? 182.863 209.437 194.311 1.00 18.88 ? 4429 GLN A CA    1 
ATOM   21366 C C     . GLN A 1 4429 ? 183.691 208.165 194.433 1.00 20.65 ? 4429 GLN A C     1 
ATOM   21367 O O     . GLN A 1 4429 ? 183.850 207.427 193.455 1.00 25.68 ? 4429 GLN A O     1 
ATOM   21368 C CB    . GLN A 1 4429 ? 183.769 210.666 194.244 1.00 19.34 ? 4429 GLN A CB    1 
ATOM   21369 C CG    . GLN A 1 4429 ? 184.703 210.684 193.046 1.00 22.89 ? 4429 GLN A CG    1 
ATOM   21370 C CD    . GLN A 1 4429 ? 186.063 210.093 193.355 1.00 26.89 ? 4429 GLN A CD    1 
ATOM   21371 O OE1   . GLN A 1 4429 ? 186.510 210.102 194.502 1.00 27.86 ? 4429 GLN A OE1   1 
ATOM   21372 N NE2   . GLN A 1 4429 ? 186.727 209.571 192.332 1.00 23.74 ? 4429 GLN A NE2   1 
ATOM   21373 N N     . ASP A 1 4430 ? 184.210 207.881 195.630 1.00 22.25 ? 4430 ASP A N     1 
ATOM   21374 C CA    . ASP A 1 4430 ? 185.021 206.681 195.815 1.00 21.20 ? 4430 ASP A CA    1 
ATOM   21375 C C     . ASP A 1 4430 ? 184.203 205.416 195.591 1.00 20.97 ? 4430 ASP A C     1 
ATOM   21376 O O     . ASP A 1 4430 ? 184.678 204.460 194.967 1.00 20.46 ? 4430 ASP A O     1 
ATOM   21377 C CB    . ASP A 1 4430 ? 185.638 206.677 197.213 1.00 24.24 ? 4430 ASP A CB    1 
ATOM   21378 C CG    . ASP A 1 4430 ? 186.696 207.744 197.383 1.00 26.03 ? 4430 ASP A CG    1 
ATOM   21379 O OD1   . ASP A 1 4430 ? 187.359 208.091 196.383 1.00 19.81 ? 4430 ASP A OD1   1 
ATOM   21380 O OD2   . ASP A 1 4430 ? 186.869 208.237 198.517 1.00 29.33 ? 4430 ASP A OD2   1 
ATOM   21381 N N     . LEU A 1 4431 ? 182.963 205.395 196.078 1.00 27.31 ? 4431 LEU A N     1 
ATOM   21382 C CA    . LEU A 1 4431 ? 182.162 204.184 195.969 1.00 24.85 ? 4431 LEU A CA    1 
ATOM   21383 C C     . LEU A 1 4431 ? 181.662 203.984 194.542 1.00 27.53 ? 4431 LEU A C     1 
ATOM   21384 O O     . LEU A 1 4431 ? 181.573 202.848 194.065 1.00 23.92 ? 4431 LEU A O     1 
ATOM   21385 C CB    . LEU A 1 4431 ? 181.008 204.242 196.969 1.00 19.02 ? 4431 LEU A CB    1 
ATOM   21386 C CG    . LEU A 1 4431 ? 180.114 203.013 197.082 1.00 26.39 ? 4431 LEU A CG    1 
ATOM   21387 C CD1   . LEU A 1 4431 ? 180.952 201.838 197.535 1.00 29.21 ? 4431 LEU A CD1   1 
ATOM   21388 C CD2   . LEU A 1 4431 ? 179.019 203.275 198.090 1.00 25.65 ? 4431 LEU A CD2   1 
ATOM   21389 N N     . ALA A 1 4432 ? 181.357 205.073 193.831 1.00 30.75 ? 4432 ALA A N     1 
ATOM   21390 C CA    . ALA A 1 4432 ? 181.019 204.959 192.416 1.00 27.87 ? 4432 ALA A CA    1 
ATOM   21391 C C     . ALA A 1 4432 ? 182.227 204.526 191.597 1.00 25.83 ? 4432 ALA A C     1 
ATOM   21392 O O     . ALA A 1 4432 ? 182.086 203.790 190.615 1.00 27.62 ? 4432 ALA A O     1 
ATOM   21393 C CB    . ALA A 1 4432 ? 180.461 206.284 191.897 1.00 22.34 ? 4432 ALA A CB    1 
ATOM   21394 N N     . ASP A 1 4433 ? 183.424 204.972 191.984 1.00 25.30 ? 4433 ASP A N     1 
ATOM   21395 C CA    . ASP A 1 4433 ? 184.643 204.477 191.354 1.00 26.57 ? 4433 ASP A CA    1 
ATOM   21396 C C     . ASP A 1 4433 ? 184.803 202.979 191.586 1.00 26.34 ? 4433 ASP A C     1 
ATOM   21397 O O     . ASP A 1 4433 ? 185.184 202.238 190.673 1.00 30.71 ? 4433 ASP A O     1 
ATOM   21398 C CB    . ASP A 1 4433 ? 185.846 205.251 191.897 1.00 30.37 ? 4433 ASP A CB    1 
ATOM   21399 C CG    . ASP A 1 4433 ? 187.131 204.953 191.149 1.00 30.43 ? 4433 ASP A CG    1 
ATOM   21400 O OD1   . ASP A 1 4433 ? 187.122 204.113 190.228 1.00 31.62 ? 4433 ASP A OD1   1 
ATOM   21401 O OD2   . ASP A 1 4433 ? 188.159 205.578 191.480 1.00 29.76 ? 4433 ASP A OD2   1 
ATOM   21402 N N     . VAL A 1 4434 ? 184.513 202.518 192.803 1.00 25.53 ? 4434 VAL A N     1 
ATOM   21403 C CA    . VAL A 1 4434 ? 184.557 201.086 193.091 1.00 26.82 ? 4434 VAL A CA    1 
ATOM   21404 C C     . VAL A 1 4434 ? 183.562 200.337 192.213 1.00 29.77 ? 4434 VAL A C     1 
ATOM   21405 O O     . VAL A 1 4434 ? 183.879 199.288 191.637 1.00 31.10 ? 4434 VAL A O     1 
ATOM   21406 C CB    . VAL A 1 4434 ? 184.290 200.837 194.588 1.00 28.87 ? 4434 VAL A CB    1 
ATOM   21407 C CG1   . VAL A 1 4434 ? 183.843 199.402 194.826 1.00 25.58 ? 4434 VAL A CG1   1 
ATOM   21408 C CG2   . VAL A 1 4434 ? 185.520 201.169 195.408 1.00 27.53 ? 4434 VAL A CG2   1 
ATOM   21409 N N     . VAL A 1 4435 ? 182.344 200.871 192.093 1.00 31.22 ? 4435 VAL A N     1 
ATOM   21410 C CA    . VAL A 1 4435 ? 181.334 200.257 191.233 1.00 28.98 ? 4435 VAL A CA    1 
ATOM   21411 C C     . VAL A 1 4435 ? 181.843 200.164 189.802 1.00 30.25 ? 4435 VAL A C     1 
ATOM   21412 O O     . VAL A 1 4435 ? 181.766 199.109 189.165 1.00 30.65 ? 4435 VAL A O     1 
ATOM   21413 C CB    . VAL A 1 4435 ? 180.013 201.044 191.306 1.00 29.03 ? 4435 VAL A CB    1 
ATOM   21414 C CG1   . VAL A 1 4435 ? 179.004 200.471 190.332 1.00 31.00 ? 4435 VAL A CG1   1 
ATOM   21415 C CG2   . VAL A 1 4435 ? 179.451 201.007 192.711 1.00 32.05 ? 4435 VAL A CG2   1 
ATOM   21416 N N     . GLN A 1 4436 ? 182.397 201.263 189.286 1.00 31.13 ? 4436 GLN A N     1 
ATOM   21417 C CA    . GLN A 1 4436 ? 182.851 201.294 187.900 1.00 29.90 ? 4436 GLN A CA    1 
ATOM   21418 C C     . GLN A 1 4436 ? 183.989 200.307 187.670 1.00 30.98 ? 4436 GLN A C     1 
ATOM   21419 O O     . GLN A 1 4436 ? 184.049 199.655 186.621 1.00 35.82 ? 4436 GLN A O     1 
ATOM   21420 C CB    . GLN A 1 4436 ? 183.279 202.713 187.522 1.00 28.57 ? 4436 GLN A CB    1 
ATOM   21421 C CG    . GLN A 1 4436 ? 183.147 203.054 186.040 1.00 31.51 ? 4436 GLN A CG    1 
ATOM   21422 C CD    . GLN A 1 4436 ? 181.704 203.102 185.550 1.00 34.84 ? 4436 GLN A CD    1 
ATOM   21423 O OE1   . GLN A 1 4436 ? 180.767 202.760 186.273 1.00 33.98 ? 4436 GLN A OE1   1 
ATOM   21424 N NE2   . GLN A 1 4436 ? 181.523 203.535 184.308 1.00 35.17 ? 4436 GLN A NE2   1 
ATOM   21425 N N     . VAL A 1 4437 ? 184.903 200.190 188.634 1.00 27.90 ? 4437 VAL A N     1 
ATOM   21426 C CA    . VAL A 1 4437 ? 185.953 199.181 188.538 1.00 32.29 ? 4437 VAL A CA    1 
ATOM   21427 C C     . VAL A 1 4437 ? 185.356 197.779 188.571 1.00 34.59 ? 4437 VAL A C     1 
ATOM   21428 O O     . VAL A 1 4437 ? 185.903 196.850 187.962 1.00 34.46 ? 4437 VAL A O     1 
ATOM   21429 C CB    . VAL A 1 4437 ? 186.996 199.387 189.654 1.00 31.88 ? 4437 VAL A CB    1 
ATOM   21430 C CG1   . VAL A 1 4437 ? 188.031 198.275 189.644 1.00 30.46 ? 4437 VAL A CG1   1 
ATOM   21431 C CG2   . VAL A 1 4437 ? 187.684 200.731 189.486 1.00 32.13 ? 4437 VAL A CG2   1 
ATOM   21432 N N     . CYS A 1 4438 ? 184.224 197.599 189.259 1.00 37.32 ? 4438 CYS A N     1 
ATOM   21433 C CA    . CYS A 1 4438 ? 183.629 196.268 189.357 1.00 37.95 ? 4438 CYS A CA    1 
ATOM   21434 C C     . CYS A 1 4438 ? 183.238 195.718 187.989 1.00 37.77 ? 4438 CYS A C     1 
ATOM   21435 O O     . CYS A 1 4438 ? 183.505 194.548 187.692 1.00 36.20 ? 4438 CYS A O     1 
ATOM   21436 C CB    . CYS A 1 4438 ? 182.417 196.296 190.287 1.00 38.40 ? 4438 CYS A CB    1 
ATOM   21437 S SG    . CYS A 1 4438 ? 182.816 196.132 192.038 1.00 39.59 ? 4438 CYS A SG    1 
ATOM   21438 N N     . GLU A 1 4439 ? 182.609 196.534 187.137 1.00 35.08 ? 4439 GLU A N     1 
ATOM   21439 C CA    . GLU A 1 4439 ? 182.252 196.025 185.815 1.00 37.92 ? 4439 GLU A CA    1 
ATOM   21440 C C     . GLU A 1 4439 ? 183.461 195.869 184.903 1.00 41.25 ? 4439 GLU A C     1 
ATOM   21441 O O     . GLU A 1 4439 ? 183.392 195.092 183.944 1.00 40.40 ? 4439 GLU A O     1 
ATOM   21442 C CB    . GLU A 1 4439 ? 181.222 196.920 185.118 1.00 35.29 ? 4439 GLU A CB    1 
ATOM   21443 C CG    . GLU A 1 4439 ? 179.907 197.107 185.853 1.00 39.61 ? 4439 GLU A CG    1 
ATOM   21444 C CD    . GLU A 1 4439 ? 179.769 198.496 186.432 1.00 41.21 ? 4439 GLU A CD    1 
ATOM   21445 O OE1   . GLU A 1 4439 ? 180.803 199.100 186.767 1.00 41.34 ? 4439 GLU A OE1   1 
ATOM   21446 O OE2   . GLU A 1 4439 ? 178.625 198.985 186.551 1.00 39.92 ? 4439 GLU A OE2   1 
ATOM   21447 N N     . GLY A 1 4440 ? 184.555 196.578 185.172 1.00 35.71 ? 4440 GLY A N     1 
ATOM   21448 C CA    . GLY A 1 4440 ? 185.751 196.483 184.367 1.00 33.96 ? 4440 GLY A CA    1 
ATOM   21449 C C     . GLY A 1 4440 ? 185.975 197.620 183.394 1.00 36.47 ? 4440 GLY A C     1 
ATOM   21450 O O     . GLY A 1 4440 ? 187.013 197.638 182.720 1.00 36.22 ? 4440 GLY A O     1 
ATOM   21451 N N     . LYS A 1 4441 ? 185.049 198.571 183.296 1.00 37.03 ? 4441 LYS A N     1 
ATOM   21452 C CA    . LYS A 1 4441 ? 185.233 199.732 182.434 1.00 37.39 ? 4441 LYS A CA    1 
ATOM   21453 C C     . LYS A 1 4441 ? 186.179 200.771 183.020 1.00 37.10 ? 4441 LYS A C     1 
ATOM   21454 O O     . LYS A 1 4441 ? 186.451 201.779 182.360 1.00 35.87 ? 4441 LYS A O     1 
ATOM   21455 C CB    . LYS A 1 4441 ? 183.883 200.388 182.110 1.00 36.49 ? 4441 LYS A CB    1 
ATOM   21456 C CG    . LYS A 1 4441 ? 183.206 199.837 180.858 1.00 38.97 ? 4441 LYS A CG    1 
ATOM   21457 C CD    . LYS A 1 4441 ? 182.560 198.478 181.057 1.00 39.39 ? 4441 LYS A CD    1 
ATOM   21458 C CE    . LYS A 1 4441 ? 181.292 198.578 181.884 1.00 39.12 ? 4441 LYS A CE    1 
ATOM   21459 N NZ    . LYS A 1 4441 ? 180.611 197.259 181.987 1.00 40.04 ? 4441 LYS A NZ    1 
ATOM   21460 N N     . LYS A 1 4442 ? 186.687 200.558 184.231 1.00 35.52 ? 4442 LYS A N     1 
ATOM   21461 C CA    . LYS A 1 4442 ? 187.661 201.463 184.820 1.00 36.38 ? 4442 LYS A CA    1 
ATOM   21462 C C     . LYS A 1 4442 ? 188.723 200.648 185.544 1.00 33.38 ? 4442 LYS A C     1 
ATOM   21463 O O     . LYS A 1 4442 ? 188.451 199.569 186.078 1.00 30.74 ? 4442 LYS A O     1 
ATOM   21464 C CB    . LYS A 1 4442 ? 186.991 202.466 185.770 1.00 35.99 ? 4442 LYS A CB    1 
ATOM   21465 C CG    . LYS A 1 4442 ? 187.908 203.573 186.261 1.00 34.60 ? 4442 LYS A CG    1 
ATOM   21466 C CD    . LYS A 1 4442 ? 187.157 204.555 187.137 1.00 31.87 ? 4442 LYS A CD    1 
ATOM   21467 C CE    . LYS A 1 4442 ? 188.045 205.718 187.546 1.00 32.94 ? 4442 LYS A CE    1 
ATOM   21468 N NZ    . LYS A 1 4442 ? 189.154 205.274 188.433 1.00 30.79 ? 4442 LYS A NZ    1 
ATOM   21469 N N     . LYS A 1 4443 ? 189.942 201.178 185.553 1.00 34.65 ? 4443 LYS A N     1 
ATOM   21470 C CA    . LYS A 1 4443 ? 191.097 200.505 186.131 1.00 36.12 ? 4443 LYS A CA    1 
ATOM   21471 C C     . LYS A 1 4443 ? 191.377 201.072 187.515 1.00 37.18 ? 4443 LYS A C     1 
ATOM   21472 O O     . LYS A 1 4443 ? 191.432 202.294 187.690 1.00 36.03 ? 4443 LYS A O     1 
ATOM   21473 C CB    . LYS A 1 4443 ? 192.331 200.663 185.236 1.00 38.49 ? 4443 LYS A CB    1 
ATOM   21474 C CG    . LYS A 1 4443 ? 192.430 199.649 184.102 1.00 34.68 ? 4443 LYS A CG    1 
ATOM   21475 C CD    . LYS A 1 4443 ? 191.446 199.950 182.982 1.00 36.12 ? 4443 LYS A CD    1 
ATOM   21476 C CE    . LYS A 1 4443 ? 191.792 201.251 182.275 1.00 35.50 ? 4443 LYS A CE    1 
ATOM   21477 N NZ    . LYS A 1 4443 ? 190.871 201.532 181.139 1.00 37.33 ? 4443 LYS A NZ    1 
ATOM   21478 N N     . GLN A 1 4444 ? 191.552 200.186 188.490 1.00 44.95 ? 4444 GLN A N     1 
ATOM   21479 C CA    . GLN A 1 4444 ? 191.814 200.601 189.859 1.00 46.86 ? 4444 GLN A CA    1 
ATOM   21480 C C     . GLN A 1 4444 ? 193.261 201.052 190.023 1.00 45.35 ? 4444 GLN A C     1 
ATOM   21481 O O     . GLN A 1 4444 ? 194.152 200.650 189.269 1.00 47.12 ? 4444 GLN A O     1 
ATOM   21482 C CB    . GLN A 1 4444 ? 191.512 199.460 190.832 1.00 43.29 ? 4444 GLN A CB    1 
ATOM   21483 C CG    . GLN A 1 4444 ? 192.488 198.298 190.749 1.00 43.47 ? 4444 GLN A CG    1 
ATOM   21484 C CD    . GLN A 1 4444 ? 192.118 197.156 191.674 1.00 49.65 ? 4444 GLN A CD    1 
ATOM   21485 O OE1   . GLN A 1 4444 ? 191.102 197.209 192.367 1.00 48.12 ? 4444 GLN A OE1   1 
ATOM   21486 N NE2   . GLN A 1 4444 ? 192.944 196.117 191.691 1.00 47.21 ? 4444 GLN A NE2   1 
ATOM   21487 N N     . THR A 1 4445 ? 193.487 201.900 191.019 1.00 37.43 ? 4445 THR A N     1 
ATOM   21488 C CA    . THR A 1 4445 ? 194.813 202.390 191.372 1.00 40.55 ? 4445 THR A CA    1 
ATOM   21489 C C     . THR A 1 4445 ? 195.139 201.980 192.806 1.00 41.17 ? 4445 THR A C     1 
ATOM   21490 O O     . THR A 1 4445 ? 194.383 201.253 193.454 1.00 43.01 ? 4445 THR A O     1 
ATOM   21491 C CB    . THR A 1 4445 ? 194.904 203.909 191.193 1.00 41.33 ? 4445 THR A CB    1 
ATOM   21492 O OG1   . THR A 1 4445 ? 196.262 204.332 191.364 1.00 42.71 ? 4445 THR A OG1   1 
ATOM   21493 C CG2   . THR A 1 4445 ? 194.026 204.622 192.205 1.00 39.07 ? 4445 THR A CG2   1 
ATOM   21494 N N     . ASN A 1 4446 ? 196.284 202.463 193.300 1.00 38.91 ? 4446 ASN A N     1 
ATOM   21495 C CA    . ASN A 1 4446 ? 196.753 202.065 194.625 1.00 37.06 ? 4446 ASN A CA    1 
ATOM   21496 C C     . ASN A 1 4446 ? 195.760 202.454 195.714 1.00 39.73 ? 4446 ASN A C     1 
ATOM   21497 O O     . ASN A 1 4446 ? 195.451 201.647 196.601 1.00 41.50 ? 4446 ASN A O     1 
ATOM   21498 C CB    . ASN A 1 4446 ? 198.125 202.685 194.896 1.00 37.55 ? 4446 ASN A CB    1 
ATOM   21499 C CG    . ASN A 1 4446 ? 198.152 204.179 194.634 1.00 40.96 ? 4446 ASN A CG    1 
ATOM   21500 O OD1   . ASN A 1 4446 ? 197.803 204.981 195.499 1.00 40.30 ? 4446 ASN A OD1   1 
ATOM   21501 N ND2   . ASN A 1 4446 ? 198.571 204.559 193.432 1.00 40.19 ? 4446 ASN A ND2   1 
ATOM   21502 N N     . TYR A 1 4447 ? 195.244 203.685 195.660 1.00 35.91 ? 4447 TYR A N     1 
ATOM   21503 C CA    . TYR A 1 4447 ? 194.209 204.089 196.605 1.00 37.06 ? 4447 TYR A CA    1 
ATOM   21504 C C     . TYR A 1 4447 ? 192.968 203.223 196.444 1.00 34.56 ? 4447 TYR A C     1 
ATOM   21505 O O     . TYR A 1 4447 ? 192.396 202.747 197.431 1.00 32.28 ? 4447 TYR A O     1 
ATOM   21506 C CB    . TYR A 1 4447 ? 193.866 205.565 196.406 1.00 36.19 ? 4447 TYR A CB    1 
ATOM   21507 C CG    . TYR A 1 4447 ? 192.606 206.006 197.113 1.00 37.65 ? 4447 TYR A CG    1 
ATOM   21508 C CD1   . TYR A 1 4447 ? 192.420 205.747 198.465 1.00 36.93 ? 4447 TYR A CD1   1 
ATOM   21509 C CD2   . TYR A 1 4447 ? 191.596 206.669 196.429 1.00 37.08 ? 4447 TYR A CD2   1 
ATOM   21510 C CE1   . TYR A 1 4447 ? 191.271 206.146 199.117 1.00 36.20 ? 4447 TYR A CE1   1 
ATOM   21511 C CE2   . TYR A 1 4447 ? 190.440 207.070 197.074 1.00 37.70 ? 4447 TYR A CE2   1 
ATOM   21512 C CZ    . TYR A 1 4447 ? 190.284 206.805 198.418 1.00 36.65 ? 4447 TYR A CZ    1 
ATOM   21513 O OH    . TYR A 1 4447 ? 189.140 207.200 199.069 1.00 35.11 ? 4447 TYR A OH    1 
ATOM   21514 N N     . LEU A 1 4448 ? 192.552 202.985 195.200 1.00 34.97 ? 4448 LEU A N     1 
ATOM   21515 C CA    . LEU A 1 4448 ? 191.426 202.091 194.968 1.00 34.26 ? 4448 LEU A CA    1 
ATOM   21516 C C     . LEU A 1 4448 ? 191.749 200.664 195.390 1.00 33.88 ? 4448 LEU A C     1 
ATOM   21517 O O     . LEU A 1 4448 ? 190.873 199.968 195.909 1.00 35.01 ? 4448 LEU A O     1 
ATOM   21518 C CB    . LEU A 1 4448 ? 191.000 202.139 193.499 1.00 34.65 ? 4448 LEU A CB    1 
ATOM   21519 C CG    . LEU A 1 4448 ? 190.042 203.256 193.065 1.00 33.04 ? 4448 LEU A CG    1 
ATOM   21520 C CD1   . LEU A 1 4448 ? 188.698 203.111 193.762 1.00 31.20 ? 4448 LEU A CD1   1 
ATOM   21521 C CD2   . LEU A 1 4448 ? 190.618 204.642 193.317 1.00 31.91 ? 4448 LEU A CD2   1 
ATOM   21522 N N     . ARG A 1 4449 ? 192.990 200.212 195.192 1.00 35.14 ? 4449 ARG A N     1 
ATOM   21523 C CA    . ARG A 1 4449 ? 193.346 198.856 195.599 1.00 35.50 ? 4449 ARG A CA    1 
ATOM   21524 C C     . ARG A 1 4449 ? 193.204 198.678 197.106 1.00 32.56 ? 4449 ARG A C     1 
ATOM   21525 O O     . ARG A 1 4449 ? 192.573 197.721 197.572 1.00 31.04 ? 4449 ARG A O     1 
ATOM   21526 C CB    . ARG A 1 4449 ? 194.766 198.515 195.145 1.00 34.84 ? 4449 ARG A CB    1 
ATOM   21527 C CG    . ARG A 1 4449 ? 194.867 198.128 193.678 1.00 36.48 ? 4449 ARG A CG    1 
ATOM   21528 C CD    . ARG A 1 4449 ? 196.199 197.475 193.363 1.00 34.57 ? 4449 ARG A CD    1 
ATOM   21529 N NE    . ARG A 1 4449 ? 197.310 198.398 193.560 1.00 36.72 ? 4449 ARG A NE    1 
ATOM   21530 C CZ    . ARG A 1 4449 ? 197.779 199.216 192.628 1.00 38.74 ? 4449 ARG A CZ    1 
ATOM   21531 N NH1   . ARG A 1 4449 ? 197.250 199.261 191.416 1.00 36.17 ? 4449 ARG A NH1   1 
ATOM   21532 N NH2   . ARG A 1 4449 ? 198.803 200.012 192.921 1.00 38.88 ? 4449 ARG A NH2   1 
ATOM   21533 N N     . THR A 1 4450 ? 193.768 199.603 197.888 1.00 30.75 ? 4450 THR A N     1 
ATOM   21534 C CA    . THR A 1 4450 ? 193.619 199.493 199.336 1.00 34.15 ? 4450 THR A CA    1 
ATOM   21535 C C     . THR A 1 4450 ? 192.172 199.708 199.767 1.00 32.42 ? 4450 THR A C     1 
ATOM   21536 O O     . THR A 1 4450 ? 191.735 199.132 200.770 1.00 28.57 ? 4450 THR A O     1 
ATOM   21537 C CB    . THR A 1 4450 ? 194.557 200.470 200.056 1.00 31.42 ? 4450 THR A CB    1 
ATOM   21538 O OG1   . THR A 1 4450 ? 194.524 200.213 201.466 1.00 28.82 ? 4450 THR A OG1   1 
ATOM   21539 C CG2   . THR A 1 4450 ? 194.159 201.911 199.807 1.00 30.60 ? 4450 THR A CG2   1 
ATOM   21540 N N     . LEU A 1 4451 ? 191.405 200.502 199.013 1.00 31.00 ? 4451 LEU A N     1 
ATOM   21541 C CA    . LEU A 1 4451 ? 189.991 200.667 199.330 1.00 28.05 ? 4451 LEU A CA    1 
ATOM   21542 C C     . LEU A 1 4451 ? 189.227 199.358 199.158 1.00 29.28 ? 4451 LEU A C     1 
ATOM   21543 O O     . LEU A 1 4451 ? 188.399 199.001 200.003 1.00 30.80 ? 4451 LEU A O     1 
ATOM   21544 C CB    . LEU A 1 4451 ? 189.391 201.771 198.460 1.00 29.62 ? 4451 LEU A CB    1 
ATOM   21545 C CG    . LEU A 1 4451 ? 187.949 202.175 198.759 1.00 27.83 ? 4451 LEU A CG    1 
ATOM   21546 C CD1   . LEU A 1 4451 ? 187.867 202.803 200.131 1.00 27.48 ? 4451 LEU A CD1   1 
ATOM   21547 C CD2   . LEU A 1 4451 ? 187.454 203.149 197.712 1.00 28.07 ? 4451 LEU A CD2   1 
ATOM   21548 N N     . ILE A 1 4452 ? 189.492 198.623 198.073 1.00 28.78 ? 4452 ILE A N     1 
ATOM   21549 C CA    . ILE A 1 4452 ? 188.875 197.306 197.912 1.00 28.17 ? 4452 ILE A CA    1 
ATOM   21550 C C     . ILE A 1 4452 ? 189.345 196.351 198.999 1.00 26.92 ? 4452 ILE A C     1 
ATOM   21551 O O     . ILE A 1 4452 ? 188.549 195.582 199.551 1.00 27.11 ? 4452 ILE A O     1 
ATOM   21552 C CB    . ILE A 1 4452 ? 189.133 196.722 196.510 1.00 31.13 ? 4452 ILE A CB    1 
ATOM   21553 C CG1   . ILE A 1 4452 ? 188.963 197.776 195.422 1.00 29.56 ? 4452 ILE A CG1   1 
ATOM   21554 C CG2   . ILE A 1 4452 ? 188.205 195.552 196.251 1.00 29.76 ? 4452 ILE A CG2   1 
ATOM   21555 C CD1   . ILE A 1 4452 ? 187.549 198.271 195.293 1.00 27.70 ? 4452 ILE A CD1   1 
ATOM   21556 N N     . ASN A 1 4453 ? 190.644 196.364 199.312 1.00 27.14 ? 4453 ASN A N     1 
ATOM   21557 C CA    . ASN A 1 4453 ? 191.135 195.482 200.368 1.00 32.19 ? 4453 ASN A CA    1 
ATOM   21558 C C     . ASN A 1 4453 ? 190.451 195.765 201.698 1.00 33.40 ? 4453 ASN A C     1 
ATOM   21559 O O     . ASN A 1 4453 ? 190.212 194.840 202.481 1.00 34.63 ? 4453 ASN A O     1 
ATOM   21560 C CB    . ASN A 1 4453 ? 192.652 195.603 200.514 1.00 32.76 ? 4453 ASN A CB    1 
ATOM   21561 C CG    . ASN A 1 4453 ? 193.399 195.087 199.300 1.00 34.74 ? 4453 ASN A CG    1 
ATOM   21562 O OD1   . ASN A 1 4453 ? 194.110 195.832 198.629 1.00 34.64 ? 4453 ASN A OD1   1 
ATOM   21563 N ND2   . ASN A 1 4453 ? 193.237 193.801 199.012 1.00 33.53 ? 4453 ASN A ND2   1 
ATOM   21564 N N     . GLU A 1 4454 ? 190.127 197.029 201.971 1.00 29.76 ? 4454 GLU A N     1 
ATOM   21565 C CA    . GLU A 1 4454 ? 189.411 197.353 203.199 1.00 26.97 ? 4454 GLU A CA    1 
ATOM   21566 C C     . GLU A 1 4454 ? 187.937 196.964 203.119 1.00 28.20 ? 4454 GLU A C     1 
ATOM   21567 O O     . GLU A 1 4454 ? 187.369 196.480 204.104 1.00 31.60 ? 4454 GLU A O     1 
ATOM   21568 C CB    . GLU A 1 4454 ? 189.560 198.842 203.512 1.00 26.23 ? 4454 GLU A CB    1 
ATOM   21569 C CG    . GLU A 1 4454 ? 190.929 199.206 204.063 1.00 29.61 ? 4454 GLU A CG    1 
ATOM   21570 C CD    . GLU A 1 4454 ? 191.223 200.689 203.980 1.00 30.59 ? 4454 GLU A CD    1 
ATOM   21571 O OE1   . GLU A 1 4454 ? 191.188 201.243 202.862 1.00 31.15 ? 4454 GLU A OE1   1 
ATOM   21572 O OE2   . GLU A 1 4454 ? 191.499 201.299 205.034 1.00 28.32 ? 4454 GLU A OE2   1 
ATOM   21573 N N     . LEU A 1 4455 ? 187.300 197.161 201.961 1.00 21.85 ? 4455 LEU A N     1 
ATOM   21574 C CA    . LEU A 1 4455 ? 185.868 196.893 201.859 1.00 23.06 ? 4455 LEU A CA    1 
ATOM   21575 C C     . LEU A 1 4455 ? 185.554 195.400 201.839 1.00 25.57 ? 4455 LEU A C     1 
ATOM   21576 O O     . LEU A 1 4455 ? 184.503 194.989 202.343 1.00 27.01 ? 4455 LEU A O     1 
ATOM   21577 C CB    . LEU A 1 4455 ? 185.286 197.572 200.620 1.00 26.33 ? 4455 LEU A CB    1 
ATOM   21578 C CG    . LEU A 1 4455 ? 185.290 199.102 200.614 1.00 26.31 ? 4455 LEU A CG    1 
ATOM   21579 C CD1   . LEU A 1 4455 ? 184.816 199.632 199.273 1.00 24.35 ? 4455 LEU A CD1   1 
ATOM   21580 C CD2   . LEU A 1 4455 ? 184.427 199.646 201.740 1.00 26.91 ? 4455 LEU A CD2   1 
ATOM   21581 N N     . VAL A 1 4456 ? 186.431 194.578 201.259 1.00 30.02 ? 4456 VAL A N     1 
ATOM   21582 C CA    . VAL A 1 4456 ? 186.159 193.143 201.202 1.00 31.98 ? 4456 VAL A CA    1 
ATOM   21583 C C     . VAL A 1 4456 ? 186.222 192.527 202.595 1.00 30.38 ? 4456 VAL A C     1 
ATOM   21584 O O     . VAL A 1 4456 ? 185.451 191.615 202.918 1.00 30.01 ? 4456 VAL A O     1 
ATOM   21585 C CB    . VAL A 1 4456 ? 187.117 192.441 200.220 1.00 28.47 ? 4456 VAL A CB    1 
ATOM   21586 C CG1   . VAL A 1 4456 ? 186.902 192.963 198.808 1.00 30.14 ? 4456 VAL A CG1   1 
ATOM   21587 C CG2   . VAL A 1 4456 ? 188.570 192.618 200.647 1.00 25.79 ? 4456 VAL A CG2   1 
ATOM   21588 N N     . LYS A 1 4457 ? 187.131 193.007 203.440 1.00 27.11 ? 4457 LYS A N     1 
ATOM   21589 C CA    . LYS A 1 4457 ? 187.232 192.541 204.815 1.00 29.35 ? 4457 LYS A CA    1 
ATOM   21590 C C     . LYS A 1 4457 ? 186.265 193.255 205.749 1.00 31.26 ? 4457 LYS A C     1 
ATOM   21591 O O     . LYS A 1 4457 ? 186.218 192.927 206.939 1.00 30.74 ? 4457 LYS A O     1 
ATOM   21592 C CB    . LYS A 1 4457 ? 188.664 192.710 205.331 1.00 30.60 ? 4457 LYS A CB    1 
ATOM   21593 C CG    . LYS A 1 4457 ? 189.734 192.239 204.362 1.00 30.35 ? 4457 LYS A CG    1 
ATOM   21594 C CD    . LYS A 1 4457 ? 191.099 192.158 205.033 1.00 32.50 ? 4457 LYS A CD    1 
ATOM   21595 C CE    . LYS A 1 4457 ? 191.565 193.513 205.549 1.00 31.12 ? 4457 LYS A CE    1 
ATOM   21596 N NZ    . LYS A 1 4457 ? 191.214 194.627 204.626 1.00 30.81 ? 4457 LYS A NZ    1 
ATOM   21597 N N     . GLY A 1 4458 ? 185.499 194.214 205.241 1.00 29.00 ? 4458 GLY A N     1 
ATOM   21598 C CA    . GLY A 1 4458 ? 184.530 194.927 206.053 1.00 25.69 ? 4458 GLY A CA    1 
ATOM   21599 C C     . GLY A 1 4458 ? 185.129 195.795 207.137 1.00 24.04 ? 4458 GLY A C     1 
ATOM   21600 O O     . GLY A 1 4458 ? 184.544 195.916 208.220 1.00 29.27 ? 4458 GLY A O     1 
ATOM   21601 N N     . ILE A 1 4459 ? 186.278 196.412 206.873 1.00 21.25 ? 4459 ILE A N     1 
ATOM   21602 C CA    . ILE A 1 4459 ? 186.914 197.329 207.810 1.00 28.19 ? 4459 ILE A CA    1 
ATOM   21603 C C     . ILE A 1 4459 ? 186.801 198.740 207.252 1.00 27.87 ? 4459 ILE A C     1 
ATOM   21604 O O     . ILE A 1 4459 ? 186.940 198.954 206.041 1.00 25.93 ? 4459 ILE A O     1 
ATOM   21605 C CB    . ILE A 1 4459 ? 188.384 196.952 208.089 1.00 28.56 ? 4459 ILE A CB    1 
ATOM   21606 C CG1   . ILE A 1 4459 ? 189.224 197.024 206.815 1.00 27.91 ? 4459 ILE A CG1   1 
ATOM   21607 C CG2   . ILE A 1 4459 ? 188.468 195.563 208.703 1.00 28.75 ? 4459 ILE A CG2   1 
ATOM   21608 C CD1   . ILE A 1 4459 ? 190.709 196.893 207.063 1.00 29.41 ? 4459 ILE A CD1   1 
ATOM   21609 N N     . LEU A 1 4460 ? 186.515 199.692 208.130 1.00 29.73 ? 4460 LEU A N     1 
ATOM   21610 C CA    . LEU A 1 4460 ? 186.256 201.060 207.700 1.00 21.99 ? 4460 LEU A CA    1 
ATOM   21611 C C     . LEU A 1 4460 ? 187.505 201.666 207.069 1.00 24.04 ? 4460 LEU A C     1 
ATOM   21612 O O     . LEU A 1 4460 ? 188.577 201.642 207.684 1.00 28.40 ? 4460 LEU A O     1 
ATOM   21613 C CB    . LEU A 1 4460 ? 185.802 201.906 208.886 1.00 21.15 ? 4460 LEU A CB    1 
ATOM   21614 C CG    . LEU A 1 4460 ? 185.504 203.380 208.613 1.00 23.62 ? 4460 LEU A CG    1 
ATOM   21615 C CD1   . LEU A 1 4460 ? 184.385 203.524 207.597 1.00 25.05 ? 4460 LEU A CD1   1 
ATOM   21616 C CD2   . LEU A 1 4460 ? 185.158 204.098 209.905 1.00 25.97 ? 4460 LEU A CD2   1 
ATOM   21617 N N     . PRO A 1 4461 ? 187.415 202.198 205.852 1.00 25.59 ? 4461 PRO A N     1 
ATOM   21618 C CA    . PRO A 1 4461 ? 188.575 202.869 205.254 1.00 21.34 ? 4461 PRO A CA    1 
ATOM   21619 C C     . PRO A 1 4461 ? 189.010 204.062 206.091 1.00 22.09 ? 4461 PRO A C     1 
ATOM   21620 O O     . PRO A 1 4461 ? 188.186 204.783 206.655 1.00 27.66 ? 4461 PRO A O     1 
ATOM   21621 C CB    . PRO A 1 4461 ? 188.062 203.304 203.878 1.00 20.79 ? 4461 PRO A CB    1 
ATOM   21622 C CG    . PRO A 1 4461 ? 186.925 202.384 203.589 1.00 23.52 ? 4461 PRO A CG    1 
ATOM   21623 C CD    . PRO A 1 4461 ? 186.289 202.089 204.910 1.00 25.50 ? 4461 PRO A CD    1 
ATOM   21624 N N     . ARG A 1 4462 ? 190.327 204.266 206.164 1.00 27.51 ? 4462 ARG A N     1 
ATOM   21625 C CA    . ARG A 1 4462 ? 190.855 205.364 206.966 1.00 27.72 ? 4462 ARG A CA    1 
ATOM   21626 C C     . ARG A 1 4462 ? 190.533 206.719 206.350 1.00 27.04 ? 4462 ARG A C     1 
ATOM   21627 O O     . ARG A 1 4462 ? 190.459 207.722 207.068 1.00 27.18 ? 4462 ARG A O     1 
ATOM   21628 C CB    . ARG A 1 4462 ? 192.364 205.205 207.147 1.00 24.63 ? 4462 ARG A CB    1 
ATOM   21629 C CG    . ARG A 1 4462 ? 192.802 203.992 207.971 1.00 26.26 ? 4462 ARG A CG    1 
ATOM   21630 C CD    . ARG A 1 4462 ? 192.447 204.092 209.459 1.00 28.38 ? 4462 ARG A CD    1 
ATOM   21631 N NE    . ARG A 1 4462 ? 191.019 203.969 209.729 1.00 28.64 ? 4462 ARG A NE    1 
ATOM   21632 C CZ    . ARG A 1 4462 ? 190.475 204.036 210.936 1.00 30.81 ? 4462 ARG A CZ    1 
ATOM   21633 N NH1   . ARG A 1 4462 ? 191.214 204.223 212.018 1.00 30.21 ? 4462 ARG A NH1   1 
ATOM   21634 N NH2   . ARG A 1 4462 ? 189.156 203.913 211.062 1.00 30.26 ? 4462 ARG A NH2   1 
ATOM   21635 N N     . SER A 1 4463 ? 190.343 206.773 205.032 1.00 27.88 ? 4463 SER A N     1 
ATOM   21636 C CA    . SER A 1 4463 ? 190.002 208.023 204.369 1.00 26.67 ? 4463 SER A CA    1 
ATOM   21637 C C     . SER A 1 4463 ? 188.541 208.412 204.551 1.00 25.94 ? 4463 SER A C     1 
ATOM   21638 O O     . SER A 1 4463 ? 188.190 209.566 204.286 1.00 30.94 ? 4463 SER A O     1 
ATOM   21639 C CB    . SER A 1 4463 ? 190.324 207.934 202.876 1.00 26.36 ? 4463 SER A CB    1 
ATOM   21640 O OG    . SER A 1 4463 ? 189.881 209.091 202.191 1.00 30.43 ? 4463 SER A OG    1 
ATOM   21641 N N     . TRP A 1 4464 ? 187.689 207.489 204.987 1.00 23.59 ? 4464 TRP A N     1 
ATOM   21642 C CA    . TRP A 1 4464 ? 186.285 207.783 205.238 1.00 23.00 ? 4464 TRP A CA    1 
ATOM   21643 C C     . TRP A 1 4464 ? 186.015 208.193 206.678 1.00 23.80 ? 4464 TRP A C     1 
ATOM   21644 O O     . TRP A 1 4464 ? 184.876 208.542 207.004 1.00 22.31 ? 4464 TRP A O     1 
ATOM   21645 C CB    . TRP A 1 4464 ? 185.417 206.569 204.888 1.00 21.60 ? 4464 TRP A CB    1 
ATOM   21646 C CG    . TRP A 1 4464 ? 185.386 206.230 203.431 1.00 24.59 ? 4464 TRP A CG    1 
ATOM   21647 C CD1   . TRP A 1 4464 ? 186.169 206.755 202.446 1.00 24.48 ? 4464 TRP A CD1   1 
ATOM   21648 C CD2   . TRP A 1 4464 ? 184.524 205.281 202.794 1.00 21.55 ? 4464 TRP A CD2   1 
ATOM   21649 N NE1   . TRP A 1 4464 ? 185.847 206.194 201.236 1.00 24.23 ? 4464 TRP A NE1   1 
ATOM   21650 C CE2   . TRP A 1 4464 ? 184.840 205.284 201.423 1.00 22.32 ? 4464 TRP A CE2   1 
ATOM   21651 C CE3   . TRP A 1 4464 ? 183.515 204.428 203.251 1.00 23.87 ? 4464 TRP A CE3   1 
ATOM   21652 C CZ2   . TRP A 1 4464 ? 184.184 204.470 200.505 1.00 23.21 ? 4464 TRP A CZ2   1 
ATOM   21653 C CZ3   . TRP A 1 4464 ? 182.865 203.621 202.338 1.00 21.93 ? 4464 TRP A CZ3   1 
ATOM   21654 C CH2   . TRP A 1 4464 ? 183.202 203.648 200.981 1.00 19.94 ? 4464 TRP A CH2   1 
ATOM   21655 N N     . SER A 1 4465 ? 187.026 208.164 207.541 1.00 29.43 ? 4465 SER A N     1 
ATOM   21656 C CA    . SER A 1 4465 ? 186.859 208.448 208.961 1.00 26.78 ? 4465 SER A CA    1 
ATOM   21657 C C     . SER A 1 4465 ? 187.281 209.887 209.230 1.00 26.90 ? 4465 SER A C     1 
ATOM   21658 O O     . SER A 1 4465 ? 188.476 210.197 209.265 1.00 27.57 ? 4465 SER A O     1 
ATOM   21659 C CB    . SER A 1 4465 ? 187.672 207.470 209.806 1.00 22.73 ? 4465 SER A CB    1 
ATOM   21660 O OG    . SER A 1 4465 ? 189.061 207.671 209.623 1.00 24.25 ? 4465 SER A OG    1 
ATOM   21661 N N     . HIS A 1 4466 ? 186.296 210.764 209.422 1.00 23.68 ? 4466 HIS A N     1 
ATOM   21662 C CA    . HIS A 1 4466 ? 186.553 212.144 209.799 1.00 25.32 ? 4466 HIS A CA    1 
ATOM   21663 C C     . HIS A 1 4466 ? 185.739 212.583 211.006 1.00 27.05 ? 4466 HIS A C     1 
ATOM   21664 O O     . HIS A 1 4466 ? 185.853 213.741 211.422 1.00 29.12 ? 4466 HIS A O     1 
ATOM   21665 C CB    . HIS A 1 4466 ? 186.275 213.087 208.619 1.00 24.46 ? 4466 HIS A CB    1 
ATOM   21666 C CG    . HIS A 1 4466 ? 187.298 213.001 207.529 1.00 27.68 ? 4466 HIS A CG    1 
ATOM   21667 N ND1   . HIS A 1 4466 ? 187.131 212.212 206.412 1.00 30.21 ? 4466 HIS A ND1   1 
ATOM   21668 C CD2   . HIS A 1 4466 ? 188.504 213.599 207.391 1.00 25.45 ? 4466 HIS A CD2   1 
ATOM   21669 C CE1   . HIS A 1 4466 ? 188.189 212.330 205.630 1.00 27.73 ? 4466 HIS A CE1   1 
ATOM   21670 N NE2   . HIS A 1 4466 ? 189.037 213.167 206.201 1.00 26.20 ? 4466 HIS A NE2   1 
ATOM   21671 N N     . TYR A 1 4467 ? 184.927 211.697 211.576 1.00 17.17 ? 4467 TYR A N     1 
ATOM   21672 C CA    . TYR A 1 4467 ? 184.210 211.963 212.811 1.00 17.03 ? 4467 TYR A CA    1 
ATOM   21673 C C     . TYR A 1 4467 ? 184.385 210.772 213.740 1.00 20.67 ? 4467 TYR A C     1 
ATOM   21674 O O     . TYR A 1 4467 ? 184.652 209.653 213.292 1.00 19.12 ? 4467 TYR A O     1 
ATOM   21675 C CB    . TYR A 1 4467 ? 182.723 212.246 212.561 1.00 16.36 ? 4467 TYR A CB    1 
ATOM   21676 C CG    . TYR A 1 4467 ? 181.989 211.172 211.790 1.00 15.54 ? 4467 TYR A CG    1 
ATOM   21677 C CD1   . TYR A 1 4467 ? 182.032 211.132 210.403 1.00 15.21 ? 4467 TYR A CD1   1 
ATOM   21678 C CD2   . TYR A 1 4467 ? 181.240 210.208 212.447 1.00 17.39 ? 4467 TYR A CD2   1 
ATOM   21679 C CE1   . TYR A 1 4467 ? 181.355 210.159 209.695 1.00 14.98 ? 4467 TYR A CE1   1 
ATOM   21680 C CE2   . TYR A 1 4467 ? 180.563 209.231 211.747 1.00 16.09 ? 4467 TYR A CE2   1 
ATOM   21681 C CZ    . TYR A 1 4467 ? 180.622 209.211 210.373 1.00 12.45 ? 4467 TYR A CZ    1 
ATOM   21682 O OH    . TYR A 1 4467 ? 179.946 208.237 209.679 1.00 11.40 ? 4467 TYR A OH    1 
ATOM   21683 N N     . THR A 1 4468 ? 184.246 211.025 215.039 1.00 19.15 ? 4468 THR A N     1 
ATOM   21684 C CA    . THR A 1 4468 ? 184.528 210.000 216.035 1.00 10.52 ? 4468 THR A CA    1 
ATOM   21685 C C     . THR A 1 4468 ? 183.573 208.823 215.890 1.00 13.96 ? 4468 THR A C     1 
ATOM   21686 O O     . THR A 1 4468 ? 182.350 208.991 215.874 1.00 15.81 ? 4468 THR A O     1 
ATOM   21687 C CB    . THR A 1 4468 ? 184.433 210.591 217.442 1.00 9.80  ? 4468 THR A CB    1 
ATOM   21688 O OG1   . THR A 1 4468 ? 185.386 211.652 217.578 1.00 14.21 ? 4468 THR A OG1   1 
ATOM   21689 C CG2   . THR A 1 4468 ? 184.723 209.527 218.484 1.00 12.45 ? 4468 THR A CG2   1 
ATOM   21690 N N     . VAL A 1 4469 ? 184.144 207.628 215.787 1.00 14.33 ? 4469 VAL A N     1 
ATOM   21691 C CA    . VAL A 1 4469 ? 183.378 206.395 215.615 1.00 14.53 ? 4469 VAL A CA    1 
ATOM   21692 C C     . VAL A 1 4469 ? 183.923 205.362 216.590 1.00 9.31  ? 4469 VAL A C     1 
ATOM   21693 O O     . VAL A 1 4469 ? 185.073 205.468 217.047 1.00 9.20  ? 4469 VAL A O     1 
ATOM   21694 C CB    . VAL A 1 4469 ? 183.449 205.880 214.158 1.00 20.09 ? 4469 VAL A CB    1 
ATOM   21695 C CG1   . VAL A 1 4469 ? 182.650 206.783 213.236 1.00 14.65 ? 4469 VAL A CG1   1 
ATOM   21696 C CG2   . VAL A 1 4469 ? 184.894 205.786 213.697 1.00 15.63 ? 4469 VAL A CG2   1 
ATOM   21697 N N     . PRO A 1 4470 ? 183.119 204.357 216.944 1.00 9.21  ? 4470 PRO A N     1 
ATOM   21698 C CA    . PRO A 1 4470 ? 183.609 203.320 217.859 1.00 13.66 ? 4470 PRO A CA    1 
ATOM   21699 C C     . PRO A 1 4470 ? 184.831 202.615 217.291 1.00 18.41 ? 4470 PRO A C     1 
ATOM   21700 O O     . PRO A 1 4470 ? 184.991 202.480 216.076 1.00 19.49 ? 4470 PRO A O     1 
ATOM   21701 C CB    . PRO A 1 4470 ? 182.417 202.365 217.988 1.00 12.88 ? 4470 PRO A CB    1 
ATOM   21702 C CG    . PRO A 1 4470 ? 181.233 203.188 217.641 1.00 11.08 ? 4470 PRO A CG    1 
ATOM   21703 C CD    . PRO A 1 4470 ? 181.696 204.171 216.613 1.00 13.68 ? 4470 PRO A CD    1 
ATOM   21704 N N     . ALA A 1 4471 ? 185.703 202.166 218.193 1.00 20.38 ? 4471 ALA A N     1 
ATOM   21705 C CA    . ALA A 1 4471 ? 186.994 201.623 217.792 1.00 21.87 ? 4471 ALA A CA    1 
ATOM   21706 C C     . ALA A 1 4471 ? 186.826 200.268 217.122 1.00 21.32 ? 4471 ALA A C     1 
ATOM   21707 O O     . ALA A 1 4471 ? 186.930 199.224 217.773 1.00 18.54 ? 4471 ALA A O     1 
ATOM   21708 C CB    . ALA A 1 4471 ? 187.925 201.508 219.000 1.00 20.06 ? 4471 ALA A CB    1 
ATOM   21709 N N     . GLY A 1 4472 ? 186.567 200.281 215.818 1.00 19.24 ? 4472 GLY A N     1 
ATOM   21710 C CA    . GLY A 1 4472 ? 186.379 199.061 215.062 1.00 21.27 ? 4472 GLY A CA    1 
ATOM   21711 C C     . GLY A 1 4472 ? 184.918 198.700 214.902 1.00 21.40 ? 4472 GLY A C     1 
ATOM   21712 O O     . GLY A 1 4472 ? 184.285 198.235 215.853 1.00 24.27 ? 4472 GLY A O     1 
ATOM   21713 N N     . MET A 1 4473 ? 184.368 198.909 213.708 1.00 20.79 ? 4473 MET A N     1 
ATOM   21714 C CA    . MET A 1 4473 ? 182.987 198.527 213.458 1.00 24.58 ? 4473 MET A CA    1 
ATOM   21715 C C     . MET A 1 4473 ? 182.822 198.171 211.988 1.00 24.23 ? 4473 MET A C     1 
ATOM   21716 O O     . MET A 1 4473 ? 183.657 198.520 211.149 1.00 14.60 ? 4473 MET A O     1 
ATOM   21717 C CB    . MET A 1 4473 ? 182.001 199.635 213.846 1.00 13.25 ? 4473 MET A CB    1 
ATOM   21718 C CG    . MET A 1 4473 ? 182.098 200.900 213.018 1.00 17.65 ? 4473 MET A CG    1 
ATOM   21719 S SD    . MET A 1 4473 ? 180.927 202.143 213.595 1.00 22.00 ? 4473 MET A SD    1 
ATOM   21720 C CE    . MET A 1 4473 ? 181.275 203.484 212.471 1.00 11.83 ? 4473 MET A CE    1 
ATOM   21721 N N     . THR A 1 4474 ? 181.731 197.472 211.697 1.00 23.10 ? 4474 THR A N     1 
ATOM   21722 C CA    . THR A 1 4474 ? 181.448 197.000 210.351 1.00 17.10 ? 4474 THR A CA    1 
ATOM   21723 C C     . THR A 1 4474 ? 181.101 198.168 209.429 1.00 22.78 ? 4474 THR A C     1 
ATOM   21724 O O     . THR A 1 4474 ? 180.423 199.121 209.823 1.00 19.04 ? 4474 THR A O     1 
ATOM   21725 C CB    . THR A 1 4474 ? 180.306 195.980 210.400 1.00 16.70 ? 4474 THR A CB    1 
ATOM   21726 O OG1   . THR A 1 4474 ? 180.799 194.737 210.914 1.00 23.88 ? 4474 THR A OG1   1 
ATOM   21727 C CG2   . THR A 1 4474 ? 179.710 195.744 209.033 1.00 13.89 ? 4474 THR A CG2   1 
ATOM   21728 N N     . VAL A 1 4475 ? 181.587 198.087 208.185 1.00 27.07 ? 4475 VAL A N     1 
ATOM   21729 C CA    . VAL A 1 4475 ? 181.382 199.163 207.217 1.00 17.70 ? 4475 VAL A CA    1 
ATOM   21730 C C     . VAL A 1 4475 ? 179.905 199.353 206.907 1.00 18.33 ? 4475 VAL A C     1 
ATOM   21731 O O     . VAL A 1 4475 ? 179.474 200.462 206.577 1.00 23.35 ? 4475 VAL A O     1 
ATOM   21732 C CB    . VAL A 1 4475 ? 182.191 198.892 205.933 1.00 15.84 ? 4475 VAL A CB    1 
ATOM   21733 C CG1   . VAL A 1 4475 ? 182.036 200.035 204.946 1.00 20.42 ? 4475 VAL A CG1   1 
ATOM   21734 C CG2   . VAL A 1 4475 ? 183.643 198.693 206.264 1.00 20.92 ? 4475 VAL A CG2   1 
ATOM   21735 N N     . ILE A 1 4476 ? 179.107 198.287 206.981 1.00 21.01 ? 4476 ILE A N     1 
ATOM   21736 C CA    . ILE A 1 4476 ? 177.669 198.430 206.761 1.00 21.73 ? 4476 ILE A CA    1 
ATOM   21737 C C     . ILE A 1 4476 ? 177.043 199.310 207.839 1.00 22.21 ? 4476 ILE A C     1 
ATOM   21738 O O     . ILE A 1 4476 ? 176.187 200.156 207.549 1.00 22.39 ? 4476 ILE A O     1 
ATOM   21739 C CB    . ILE A 1 4476 ? 176.987 197.050 206.670 1.00 22.52 ? 4476 ILE A CB    1 
ATOM   21740 C CG1   . ILE A 1 4476 ? 177.507 196.259 205.461 1.00 21.90 ? 4476 ILE A CG1   1 
ATOM   21741 C CG2   . ILE A 1 4476 ? 175.476 197.201 206.595 1.00 23.43 ? 4476 ILE A CG2   1 
ATOM   21742 C CD1   . ILE A 1 4476 ? 178.728 195.405 205.709 1.00 21.46 ? 4476 ILE A CD1   1 
ATOM   21743 N N     . GLN A 1 4477 ? 177.462 199.137 209.095 1.00 18.91 ? 4477 GLN A N     1 
ATOM   21744 C CA    . GLN A 1 4477 ? 176.977 200.017 210.155 1.00 15.79 ? 4477 GLN A CA    1 
ATOM   21745 C C     . GLN A 1 4477 ? 177.428 201.454 209.927 1.00 19.22 ? 4477 GLN A C     1 
ATOM   21746 O O     . GLN A 1 4477 ? 176.668 202.400 210.175 1.00 17.94 ? 4477 GLN A O     1 
ATOM   21747 C CB    . GLN A 1 4477 ? 177.451 199.520 211.520 1.00 16.12 ? 4477 GLN A CB    1 
ATOM   21748 C CG    . GLN A 1 4477 ? 177.477 198.012 211.667 1.00 21.68 ? 4477 GLN A CG    1 
ATOM   21749 C CD    . GLN A 1 4477 ? 178.303 197.564 212.854 1.00 21.63 ? 4477 GLN A CD    1 
ATOM   21750 O OE1   . GLN A 1 4477 ? 179.366 198.117 213.125 1.00 17.69 ? 4477 GLN A OE1   1 
ATOM   21751 N NE2   . GLN A 1 4477 ? 177.816 196.560 213.572 1.00 20.94 ? 4477 GLN A NE2   1 
ATOM   21752 N N     . TRP A 1 4478 ? 178.668 201.639 209.466 1.00 14.86 ? 4478 TRP A N     1 
ATOM   21753 C CA    . TRP A 1 4478 ? 179.142 202.981 209.148 1.00 13.19 ? 4478 TRP A CA    1 
ATOM   21754 C C     . TRP A 1 4478 ? 178.306 203.614 208.046 1.00 16.12 ? 4478 TRP A C     1 
ATOM   21755 O O     . TRP A 1 4478 ? 177.946 204.789 208.130 1.00 20.50 ? 4478 TRP A O     1 
ATOM   21756 C CB    . TRP A 1 4478 ? 180.613 202.944 208.738 1.00 16.62 ? 4478 TRP A CB    1 
ATOM   21757 C CG    . TRP A 1 4478 ? 181.205 204.308 208.551 1.00 17.96 ? 4478 TRP A CG    1 
ATOM   21758 C CD1   . TRP A 1 4478 ? 181.871 205.047 209.484 1.00 19.52 ? 4478 TRP A CD1   1 
ATOM   21759 C CD2   . TRP A 1 4478 ? 181.181 205.100 207.357 1.00 13.66 ? 4478 TRP A CD2   1 
ATOM   21760 N NE1   . TRP A 1 4478 ? 182.265 206.246 208.946 1.00 13.57 ? 4478 TRP A NE1   1 
ATOM   21761 C CE2   . TRP A 1 4478 ? 181.853 206.303 207.641 1.00 13.26 ? 4478 TRP A CE2   1 
ATOM   21762 C CE3   . TRP A 1 4478 ? 180.656 204.907 206.076 1.00 15.98 ? 4478 TRP A CE3   1 
ATOM   21763 C CZ2   . TRP A 1 4478 ? 182.015 207.309 206.692 1.00 19.96 ? 4478 TRP A CZ2   1 
ATOM   21764 C CZ3   . TRP A 1 4478 ? 180.818 205.906 205.136 1.00 19.03 ? 4478 TRP A CZ3   1 
ATOM   21765 C CH2   . TRP A 1 4478 ? 181.492 207.092 205.448 1.00 21.52 ? 4478 TRP A CH2   1 
ATOM   21766 N N     . VAL A 1 4479 ? 177.987 202.850 207.003 1.00 18.30 ? 4479 VAL A N     1 
ATOM   21767 C CA    . VAL A 1 4479 ? 177.178 203.385 205.915 1.00 14.94 ? 4479 VAL A CA    1 
ATOM   21768 C C     . VAL A 1 4479 ? 175.776 203.718 206.404 1.00 16.20 ? 4479 VAL A C     1 
ATOM   21769 O O     . VAL A 1 4479 ? 175.208 204.747 206.025 1.00 23.44 ? 4479 VAL A O     1 
ATOM   21770 C CB    . VAL A 1 4479 ? 177.159 202.394 204.737 1.00 17.62 ? 4479 VAL A CB    1 
ATOM   21771 C CG1   . VAL A 1 4479 ? 175.975 202.667 203.820 1.00 17.46 ? 4479 VAL A CG1   1 
ATOM   21772 C CG2   . VAL A 1 4479 ? 178.468 202.470 203.967 1.00 17.33 ? 4479 VAL A CG2   1 
ATOM   21773 N N     . SER A 1 4480 ? 175.204 202.877 207.268 1.00 11.91 ? 4480 SER A N     1 
ATOM   21774 C CA    . SER A 1 4480 ? 173.862 203.142 207.777 1.00 14.82 ? 4480 SER A CA    1 
ATOM   21775 C C     . SER A 1 4480 ? 173.828 204.412 208.621 1.00 19.96 ? 4480 SER A C     1 
ATOM   21776 O O     . SER A 1 4480 ? 172.969 205.283 208.421 1.00 23.58 ? 4480 SER A O     1 
ATOM   21777 C CB    . SER A 1 4480 ? 173.365 201.943 208.584 1.00 19.48 ? 4480 SER A CB    1 
ATOM   21778 O OG    . SER A 1 4480 ? 174.184 201.721 209.718 1.00 26.85 ? 4480 SER A OG    1 
ATOM   21779 N N     . ASP A 1 4481 ? 174.759 204.546 209.572 1.00 17.93 ? 4481 ASP A N     1 
ATOM   21780 C CA    . ASP A 1 4481 ? 174.727 205.737 210.416 1.00 16.02 ? 4481 ASP A CA    1 
ATOM   21781 C C     . ASP A 1 4481 ? 175.132 206.980 209.633 1.00 16.50 ? 4481 ASP A C     1 
ATOM   21782 O O     . ASP A 1 4481 ? 174.643 208.075 209.922 1.00 22.37 ? 4481 ASP A O     1 
ATOM   21783 C CB    . ASP A 1 4481 ? 175.579 205.537 211.682 1.00 19.03 ? 4481 ASP A CB    1 
ATOM   21784 C CG    . ASP A 1 4481 ? 177.074 205.790 211.479 1.00 16.46 ? 4481 ASP A CG    1 
ATOM   21785 O OD1   . ASP A 1 4481 ? 177.545 206.011 210.350 1.00 17.52 ? 4481 ASP A OD1   1 
ATOM   21786 O OD2   . ASP A 1 4481 ? 177.799 205.771 212.494 1.00 15.98 ? 4481 ASP A OD2   1 
ATOM   21787 N N     . PHE A 1 4482 ? 175.992 206.826 208.622 1.00 11.12 ? 4482 PHE A N     1 
ATOM   21788 C CA    . PHE A 1 4482 ? 176.282 207.919 207.703 1.00 13.36 ? 4482 PHE A CA    1 
ATOM   21789 C C     . PHE A 1 4482 ? 175.035 208.359 206.950 1.00 15.50 ? 4482 PHE A C     1 
ATOM   21790 O O     . PHE A 1 4482 ? 174.812 209.559 206.762 1.00 17.43 ? 4482 PHE A O     1 
ATOM   21791 C CB    . PHE A 1 4482 ? 177.374 207.489 206.727 1.00 13.29 ? 4482 PHE A CB    1 
ATOM   21792 C CG    . PHE A 1 4482 ? 177.901 208.602 205.880 1.00 13.21 ? 4482 PHE A CG    1 
ATOM   21793 C CD1   . PHE A 1 4482 ? 178.894 209.439 206.347 1.00 14.99 ? 4482 PHE A CD1   1 
ATOM   21794 C CD2   . PHE A 1 4482 ? 177.410 208.800 204.602 1.00 15.01 ? 4482 PHE A CD2   1 
ATOM   21795 C CE1   . PHE A 1 4482 ? 179.374 210.461 205.560 1.00 17.40 ? 4482 PHE A CE1   1 
ATOM   21796 C CE2   . PHE A 1 4482 ? 177.892 209.818 203.811 1.00 17.95 ? 4482 PHE A CE2   1 
ATOM   21797 C CZ    . PHE A 1 4482 ? 178.876 210.651 204.291 1.00 17.23 ? 4482 PHE A CZ    1 
ATOM   21798 N N     . SER A 1 4483 ? 174.221 207.406 206.497 1.00 13.32 ? 4483 SER A N     1 
ATOM   21799 C CA    . SER A 1 4483 ? 172.979 207.762 205.823 1.00 14.22 ? 4483 SER A CA    1 
ATOM   21800 C C     . SER A 1 4483 ? 172.038 208.499 206.765 1.00 15.08 ? 4483 SER A C     1 
ATOM   21801 O O     . SER A 1 4483 ? 171.387 209.470 206.367 1.00 19.62 ? 4483 SER A O     1 
ATOM   21802 C CB    . SER A 1 4483 ? 172.306 206.511 205.259 1.00 18.90 ? 4483 SER A CB    1 
ATOM   21803 O OG    . SER A 1 4483 ? 171.640 205.785 206.277 1.00 22.92 ? 4483 SER A OG    1 
ATOM   21804 N N     . GLU A 1 4484 ? 171.953 208.052 208.021 1.00 13.02 ? 4484 GLU A N     1 
ATOM   21805 C CA    . GLU A 1 4484 ? 171.116 208.759 208.992 1.00 14.60 ? 4484 GLU A CA    1 
ATOM   21806 C C     . GLU A 1 4484 ? 171.625 210.177 209.240 1.00 17.43 ? 4484 GLU A C     1 
ATOM   21807 O O     . GLU A 1 4484 ? 170.834 211.128 209.329 1.00 16.84 ? 4484 GLU A O     1 
ATOM   21808 C CB    . GLU A 1 4484 ? 171.047 207.976 210.302 1.00 16.40 ? 4484 GLU A CB    1 
ATOM   21809 C CG    . GLU A 1 4484 ? 170.709 206.507 210.135 1.00 18.63 ? 4484 GLU A CG    1 
ATOM   21810 C CD    . GLU A 1 4484 ? 169.850 205.973 211.264 1.00 22.70 ? 4484 GLU A CD    1 
ATOM   21811 O OE1   . GLU A 1 4484 ? 169.525 206.752 212.184 1.00 20.38 ? 4484 GLU A OE1   1 
ATOM   21812 O OE2   . GLU A 1 4484 ? 169.502 204.774 211.231 1.00 21.81 ? 4484 GLU A OE2   1 
ATOM   21813 N N     . ARG A 1 4485 ? 172.945 210.336 209.363 1.00 14.34 ? 4485 ARG A N     1 
ATOM   21814 C CA    . ARG A 1 4485 ? 173.525 211.660 209.566 1.00 12.84 ? 4485 ARG A CA    1 
ATOM   21815 C C     . ARG A 1 4485 ? 173.258 212.568 208.373 1.00 17.81 ? 4485 ARG A C     1 
ATOM   21816 O O     . ARG A 1 4485 ? 172.915 213.744 208.540 1.00 19.67 ? 4485 ARG A O     1 
ATOM   21817 C CB    . ARG A 1 4485 ? 175.026 211.537 209.817 1.00 6.50  ? 4485 ARG A CB    1 
ATOM   21818 C CG    . ARG A 1 4485 ? 175.375 210.834 211.110 1.00 8.67  ? 4485 ARG A CG    1 
ATOM   21819 C CD    . ARG A 1 4485 ? 176.870 210.836 211.351 1.00 9.51  ? 4485 ARG A CD    1 
ATOM   21820 N NE    . ARG A 1 4485 ? 177.263 209.833 212.332 1.00 13.48 ? 4485 ARG A NE    1 
ATOM   21821 C CZ    . ARG A 1 4485 ? 177.920 210.101 213.452 1.00 15.37 ? 4485 ARG A CZ    1 
ATOM   21822 N NH1   . ARG A 1 4485 ? 178.270 211.336 213.767 1.00 11.63 ? 4485 ARG A NH1   1 
ATOM   21823 N NH2   . ARG A 1 4485 ? 178.238 209.105 214.273 1.00 16.63 ? 4485 ARG A NH2   1 
ATOM   21824 N N     . ILE A 1 4486 ? 173.407 212.039 207.159 1.00 16.21 ? 4486 ILE A N     1 
ATOM   21825 C CA    . ILE A 1 4486 ? 173.132 212.832 205.969 1.00 10.30 ? 4486 ILE A CA    1 
ATOM   21826 C C     . ILE A 1 4486 ? 171.656 213.199 205.906 1.00 9.75  ? 4486 ILE A C     1 
ATOM   21827 O O     . ILE A 1 4486 ? 171.301 214.309 205.503 1.00 15.89 ? 4486 ILE A O     1 
ATOM   21828 C CB    . ILE A 1 4486 ? 173.591 212.079 204.707 1.00 14.33 ? 4486 ILE A CB    1 
ATOM   21829 C CG1   . ILE A 1 4486 ? 175.117 211.973 204.668 1.00 14.02 ? 4486 ILE A CG1   1 
ATOM   21830 C CG2   . ILE A 1 4486 ? 173.095 212.779 203.455 1.00 20.11 ? 4486 ILE A CG2   1 
ATOM   21831 C CD1   . ILE A 1 4486 ? 175.837 213.226 205.104 1.00 11.25 ? 4486 ILE A CD1   1 
ATOM   21832 N N     . LYS A 1 4487 ? 170.774 212.284 206.312 1.00 11.89 ? 4487 LYS A N     1 
ATOM   21833 C CA    . LYS A 1 4487 ? 169.345 212.581 206.322 1.00 14.96 ? 4487 LYS A CA    1 
ATOM   21834 C C     . LYS A 1 4487 ? 169.025 213.722 207.281 1.00 16.71 ? 4487 LYS A C     1 
ATOM   21835 O O     . LYS A 1 4487 ? 168.267 214.642 206.944 1.00 20.65 ? 4487 LYS A O     1 
ATOM   21836 C CB    . LYS A 1 4487 ? 168.553 211.328 206.697 1.00 15.73 ? 4487 LYS A CB    1 
ATOM   21837 C CG    . LYS A 1 4487 ? 168.164 210.449 205.523 1.00 16.58 ? 4487 LYS A CG    1 
ATOM   21838 C CD    . LYS A 1 4487 ? 167.283 209.298 205.980 1.00 17.13 ? 4487 LYS A CD    1 
ATOM   21839 C CE    . LYS A 1 4487 ? 166.942 208.361 204.833 1.00 18.86 ? 4487 LYS A CE    1 
ATOM   21840 N NZ    . LYS A 1 4487 ? 166.184 209.053 203.754 1.00 17.92 ? 4487 LYS A NZ    1 
ATOM   21841 N N     . GLN A 1 4488 ? 169.599 213.685 208.488 1.00 17.33 ? 4488 GLN A N     1 
ATOM   21842 C CA    . GLN A 1 4488 ? 169.327 214.776 209.419 1.00 15.98 ? 4488 GLN A CA    1 
ATOM   21843 C C     . GLN A 1 4488 ? 169.958 216.077 208.941 1.00 15.93 ? 4488 GLN A C     1 
ATOM   21844 O O     . GLN A 1 4488 ? 169.409 217.155 209.188 1.00 15.43 ? 4488 GLN A O     1 
ATOM   21845 C CB    . GLN A 1 4488 ? 169.813 214.452 210.833 1.00 16.86 ? 4488 GLN A CB    1 
ATOM   21846 C CG    . GLN A 1 4488 ? 171.308 214.574 211.037 1.00 16.38 ? 4488 GLN A CG    1 
ATOM   21847 C CD    . GLN A 1 4488 ? 171.709 214.424 212.486 1.00 21.31 ? 4488 GLN A CD    1 
ATOM   21848 O OE1   . GLN A 1 4488 ? 170.863 214.251 213.361 1.00 24.22 ? 4488 GLN A OE1   1 
ATOM   21849 N NE2   . GLN A 1 4488 ? 173.005 214.508 212.750 1.00 17.15 ? 4488 GLN A NE2   1 
ATOM   21850 N N     . LEU A 1 4489 ? 171.095 216.002 208.245 1.00 13.04 ? 4489 LEU A N     1 
ATOM   21851 C CA    . LEU A 1 4489 ? 171.695 217.215 207.699 1.00 14.29 ? 4489 LEU A CA    1 
ATOM   21852 C C     . LEU A 1 4489 ? 170.834 217.800 206.586 1.00 18.93 ? 4489 LEU A C     1 
ATOM   21853 O O     . LEU A 1 4489 ? 170.721 219.023 206.461 1.00 17.32 ? 4489 LEU A O     1 
ATOM   21854 C CB    . LEU A 1 4489 ? 173.107 216.925 207.196 1.00 13.28 ? 4489 LEU A CB    1 
ATOM   21855 C CG    . LEU A 1 4489 ? 174.178 216.811 208.282 1.00 10.61 ? 4489 LEU A CG    1 
ATOM   21856 C CD1   . LEU A 1 4489 ? 175.494 216.331 207.693 1.00 15.33 ? 4489 LEU A CD1   1 
ATOM   21857 C CD2   . LEU A 1 4489 ? 174.357 218.126 209.016 1.00 9.43  ? 4489 LEU A CD2   1 
ATOM   21858 N N     . GLN A 1 4490 ? 170.225 216.943 205.764 1.00 18.62 ? 4490 GLN A N     1 
ATOM   21859 C CA    . GLN A 1 4490 ? 169.282 217.423 204.758 1.00 13.62 ? 4490 GLN A CA    1 
ATOM   21860 C C     . GLN A 1 4490 ? 168.071 218.073 205.409 1.00 13.94 ? 4490 GLN A C     1 
ATOM   21861 O O     . GLN A 1 4490 ? 167.579 219.100 204.931 1.00 18.11 ? 4490 GLN A O     1 
ATOM   21862 C CB    . GLN A 1 4490 ? 168.841 216.281 203.842 1.00 15.04 ? 4490 GLN A CB    1 
ATOM   21863 C CG    . GLN A 1 4490 ? 169.968 215.580 203.108 1.00 15.65 ? 4490 GLN A CG    1 
ATOM   21864 C CD    . GLN A 1 4490 ? 169.490 214.367 202.337 1.00 18.11 ? 4490 GLN A CD    1 
ATOM   21865 O OE1   . GLN A 1 4490 ? 168.647 213.608 202.813 1.00 19.62 ? 4490 GLN A OE1   1 
ATOM   21866 N NE2   . GLN A 1 4490 ? 170.031 214.177 201.140 1.00 16.18 ? 4490 GLN A NE2   1 
ATOM   21867 N N     . ASN A 1 4491 ? 167.568 217.482 206.494 1.00 11.10 ? 4491 ASN A N     1 
ATOM   21868 C CA    . ASN A 1 4491 ? 166.456 218.103 207.210 1.00 14.35 ? 4491 ASN A CA    1 
ATOM   21869 C C     . ASN A 1 4491 ? 166.857 219.460 207.778 1.00 16.85 ? 4491 ASN A C     1 
ATOM   21870 O O     . ASN A 1 4491 ? 166.081 220.422 207.722 1.00 20.13 ? 4491 ASN A O     1 
ATOM   21871 C CB    . ASN A 1 4491 ? 165.962 217.176 208.319 1.00 18.48 ? 4491 ASN A CB    1 
ATOM   21872 C CG    . ASN A 1 4491 ? 165.431 215.863 207.785 1.00 24.07 ? 4491 ASN A CG    1 
ATOM   21873 O OD1   . ASN A 1 4491 ? 164.731 215.831 206.774 1.00 22.78 ? 4491 ASN A OD1   1 
ATOM   21874 N ND2   . ASN A 1 4491 ? 165.763 214.770 208.461 1.00 22.16 ? 4491 ASN A ND2   1 
ATOM   21875 N N     . ILE A 1 4492 ? 168.072 219.555 208.323 1.00 19.56 ? 4492 ILE A N     1 
ATOM   21876 C CA    . ILE A 1 4492 ? 168.569 220.821 208.856 1.00 21.17 ? 4492 ILE A CA    1 
ATOM   21877 C C     . ILE A 1 4492 ? 168.683 221.859 207.747 1.00 16.63 ? 4492 ILE A C     1 
ATOM   21878 O O     . ILE A 1 4492 ? 168.306 223.024 207.925 1.00 20.07 ? 4492 ILE A O     1 
ATOM   21879 C CB    . ILE A 1 4492 ? 169.918 220.599 209.568 1.00 20.94 ? 4492 ILE A CB    1 
ATOM   21880 C CG1   . ILE A 1 4492 ? 169.697 220.028 210.969 1.00 16.57 ? 4492 ILE A CG1   1 
ATOM   21881 C CG2   . ILE A 1 4492 ? 170.720 221.890 209.636 1.00 14.04 ? 4492 ILE A CG2   1 
ATOM   21882 C CD1   . ILE A 1 4492 ? 170.969 219.582 211.651 1.00 12.91 ? 4492 ILE A CD1   1 
ATOM   21883 N N     . SER A 1 4493 ? 169.207 221.455 206.589 1.00 17.92 ? 4493 SER A N     1 
ATOM   21884 C CA    . SER A 1 4493 ? 169.341 222.376 205.466 1.00 21.56 ? 4493 SER A CA    1 
ATOM   21885 C C     . SER A 1 4493 ? 167.978 222.831 204.958 1.00 23.31 ? 4493 SER A C     1 
ATOM   21886 O O     . SER A 1 4493 ? 167.799 224.000 204.602 1.00 20.97 ? 4493 SER A O     1 
ATOM   21887 C CB    . SER A 1 4493 ? 170.145 221.719 204.345 1.00 19.10 ? 4493 SER A CB    1 
ATOM   21888 O OG    . SER A 1 4493 ? 170.655 222.687 203.447 1.00 16.29 ? 4493 SER A OG    1 
ATOM   21889 N N     . LEU A 1 4494 ? 167.004 221.921 204.912 1.00 21.77 ? 4494 LEU A N     1 
ATOM   21890 C CA    . LEU A 1 4494 ? 165.656 222.304 204.506 1.00 21.38 ? 4494 LEU A CA    1 
ATOM   21891 C C     . LEU A 1 4494 ? 165.048 223.295 205.490 1.00 23.89 ? 4494 LEU A C     1 
ATOM   21892 O O     . LEU A 1 4494 ? 164.408 224.274 205.085 1.00 25.75 ? 4494 LEU A O     1 
ATOM   21893 C CB    . LEU A 1 4494 ? 164.776 221.061 204.375 1.00 19.91 ? 4494 LEU A CB    1 
ATOM   21894 C CG    . LEU A 1 4494 ? 163.283 221.305 204.157 1.00 25.40 ? 4494 LEU A CG    1 
ATOM   21895 C CD1   . LEU A 1 4494 ? 163.047 221.998 202.824 1.00 23.70 ? 4494 LEU A CD1   1 
ATOM   21896 C CD2   . LEU A 1 4494 ? 162.509 219.999 204.230 1.00 24.28 ? 4494 LEU A CD2   1 
ATOM   21897 N N     . ALA A 1 4495 ? 165.240 223.060 206.791 1.00 21.56 ? 4495 ALA A N     1 
ATOM   21898 C CA    . ALA A 1 4495 ? 164.736 223.992 207.793 1.00 21.86 ? 4495 ALA A CA    1 
ATOM   21899 C C     . ALA A 1 4495 ? 165.395 225.359 207.657 1.00 24.08 ? 4495 ALA A C     1 
ATOM   21900 O O     . ALA A 1 4495 ? 164.728 226.393 207.770 1.00 25.83 ? 4495 ALA A O     1 
ATOM   21901 C CB    . ALA A 1 4495 ? 164.955 223.426 209.196 1.00 24.17 ? 4495 ALA A CB    1 
ATOM   21902 N N     . ALA A 1 4496 ? 166.709 225.383 207.418 1.00 22.19 ? 4496 ALA A N     1 
ATOM   21903 C CA    . ALA A 1 4496 ? 167.411 226.645 207.226 1.00 20.56 ? 4496 ALA A CA    1 
ATOM   21904 C C     . ALA A 1 4496 ? 166.973 227.359 205.954 1.00 27.67 ? 4496 ALA A C     1 
ATOM   21905 O O     . ALA A 1 4496 ? 166.966 228.594 205.920 1.00 27.50 ? 4496 ALA A O     1 
ATOM   21906 C CB    . ALA A 1 4496 ? 168.921 226.412 207.200 1.00 16.01 ? 4496 ALA A CB    1 
ATOM   21907 N N     . ALA A 1 4497 ? 166.620 226.613 204.907 1.00 27.28 ? 4497 ALA A N     1 
ATOM   21908 C CA    . ALA A 1 4497 ? 166.059 227.229 203.711 1.00 26.57 ? 4497 ALA A CA    1 
ATOM   21909 C C     . ALA A 1 4497 ? 164.683 227.822 203.989 1.00 25.05 ? 4497 ALA A C     1 
ATOM   21910 O O     . ALA A 1 4497 ? 164.354 228.898 203.477 1.00 23.25 ? 4497 ALA A O     1 
ATOM   21911 C CB    . ALA A 1 4497 ? 165.981 226.206 202.579 1.00 24.17 ? 4497 ALA A CB    1 
ATOM   21912 N N     . SER A 1 4498 ? 163.869 227.131 204.790 1.00 22.63 ? 4498 SER A N     1 
ATOM   21913 C CA    . SER A 1 4498 ? 162.548 227.652 205.130 1.00 23.16 ? 4498 SER A CA    1 
ATOM   21914 C C     . SER A 1 4498 ? 162.654 228.931 205.955 1.00 26.18 ? 4498 SER A C     1 
ATOM   21915 O O     . SER A 1 4498 ? 161.965 229.919 205.676 1.00 29.26 ? 4498 SER A O     1 
ATOM   21916 C CB    . SER A 1 4498 ? 161.745 226.590 205.881 1.00 25.76 ? 4498 SER A CB    1 
ATOM   21917 O OG    . SER A 1 4498 ? 160.544 227.132 206.402 1.00 27.87 ? 4498 SER A OG    1 
ATOM   21918 N N     . GLY A 1 4499 ? 163.513 228.932 206.975 1.00 25.63 ? 4499 GLY A N     1 
ATOM   21919 C CA    . GLY A 1 4499 ? 163.690 230.095 207.813 1.00 27.13 ? 4499 GLY A CA    1 
ATOM   21920 C C     . GLY A 1 4499 ? 165.132 230.228 208.263 1.00 26.47 ? 4499 GLY A C     1 
ATOM   21921 O O     . GLY A 1 4499 ? 165.874 229.251 208.349 1.00 23.95 ? 4499 GLY A O     1 
ATOM   21922 N N     . GLY A 1 4500 ? 165.511 231.464 208.576 1.00 28.62 ? 4500 GLY A N     1 
ATOM   21923 C CA    . GLY A 1 4500 ? 166.894 231.758 208.896 1.00 29.89 ? 4500 GLY A CA    1 
ATOM   21924 C C     . GLY A 1 4500 ? 167.301 231.453 210.323 1.00 26.60 ? 4500 GLY A C     1 
ATOM   21925 O O     . GLY A 1 4500 ? 168.210 230.649 210.553 1.00 21.48 ? 4500 GLY A O     1 
ATOM   21926 N N     . ALA A 1 4501 ? 166.635 232.080 211.296 1.00 30.27 ? 4501 ALA A N     1 
ATOM   21927 C CA    . ALA A 1 4501 ? 167.034 231.927 212.689 1.00 33.26 ? 4501 ALA A CA    1 
ATOM   21928 C C     . ALA A 1 4501 ? 165.911 231.409 213.580 1.00 35.59 ? 4501 ALA A C     1 
ATOM   21929 O O     . ALA A 1 4501 ? 166.136 231.219 214.782 1.00 35.54 ? 4501 ALA A O     1 
ATOM   21930 C CB    . ALA A 1 4501 ? 167.558 233.257 213.245 1.00 32.85 ? 4501 ALA A CB    1 
ATOM   21931 N N     . LYS A 1 4502 ? 164.718 231.173 213.039 1.00 36.88 ? 4502 LYS A N     1 
ATOM   21932 C CA    . LYS A 1 4502 ? 163.601 230.650 213.816 1.00 36.47 ? 4502 LYS A CA    1 
ATOM   21933 C C     . LYS A 1 4502 ? 163.575 229.130 213.861 1.00 33.43 ? 4502 LYS A C     1 
ATOM   21934 O O     . LYS A 1 4502 ? 163.366 228.550 214.930 1.00 33.77 ? 4502 LYS A O     1 
ATOM   21935 C CB    . LYS A 1 4502 ? 162.274 231.163 213.245 1.00 35.80 ? 4502 LYS A CB    1 
ATOM   21936 C CG    . LYS A 1 4502 ? 161.047 230.755 214.048 1.00 35.43 ? 4502 LYS A CG    1 
ATOM   21937 C CD    . LYS A 1 4502 ? 160.674 231.808 215.081 1.00 37.33 ? 4502 LYS A CD    1 
ATOM   21938 C CE    . LYS A 1 4502 ? 160.577 233.189 214.455 1.00 35.73 ? 4502 LYS A CE    1 
ATOM   21939 N NZ    . LYS A 1 4502 ? 160.519 234.264 215.484 1.00 32.39 ? 4502 LYS A NZ    1 
ATOM   21940 N N     . GLU A 1 4503 ? 163.788 228.470 212.721 1.00 29.94 ? 4503 GLU A N     1 
ATOM   21941 C CA    . GLU A 1 4503 ? 163.714 227.015 212.675 1.00 32.44 ? 4503 GLU A CA    1 
ATOM   21942 C C     . GLU A 1 4503 ? 164.949 226.346 213.264 1.00 29.65 ? 4503 GLU A C     1 
ATOM   21943 O O     . GLU A 1 4503 ? 164.847 225.228 213.779 1.00 31.81 ? 4503 GLU A O     1 
ATOM   21944 C CB    . GLU A 1 4503 ? 163.496 226.547 211.236 1.00 33.35 ? 4503 GLU A CB    1 
ATOM   21945 C CG    . GLU A 1 4503 ? 162.396 227.297 210.503 1.00 32.49 ? 4503 GLU A CG    1 
ATOM   21946 C CD    . GLU A 1 4503 ? 161.058 227.213 211.215 1.00 36.87 ? 4503 GLU A CD    1 
ATOM   21947 O OE1   . GLU A 1 4503 ? 160.739 226.137 211.764 1.00 34.96 ? 4503 GLU A OE1   1 
ATOM   21948 O OE2   . GLU A 1 4503 ? 160.325 228.224 211.225 1.00 36.46 ? 4503 GLU A OE2   1 
ATOM   21949 N N     . LEU A 1 4504 ? 166.113 226.998 213.200 1.00 24.57 ? 4504 LEU A N     1 
ATOM   21950 C CA    . LEU A 1 4504 ? 167.332 226.378 213.711 1.00 23.71 ? 4504 LEU A CA    1 
ATOM   21951 C C     . LEU A 1 4504 ? 167.227 226.093 215.203 1.00 22.25 ? 4504 LEU A C     1 
ATOM   21952 O O     . LEU A 1 4504 ? 167.656 225.032 215.671 1.00 26.98 ? 4504 LEU A O     1 
ATOM   21953 C CB    . LEU A 1 4504 ? 168.540 227.268 213.421 1.00 27.03 ? 4504 LEU A CB    1 
ATOM   21954 C CG    . LEU A 1 4504 ? 169.047 227.299 211.978 1.00 22.82 ? 4504 LEU A CG    1 
ATOM   21955 C CD1   . LEU A 1 4504 ? 170.460 227.834 211.931 1.00 18.08 ? 4504 LEU A CD1   1 
ATOM   21956 C CD2   . LEU A 1 4504 ? 168.982 225.921 211.346 1.00 18.00 ? 4504 LEU A CD2   1 
ATOM   21957 N N     . LYS A 1 4505 ? 166.668 227.031 215.969 1.00 19.69 ? 4505 LYS A N     1 
ATOM   21958 C CA    . LYS A 1 4505 ? 166.449 226.786 217.390 1.00 23.70 ? 4505 LYS A CA    1 
ATOM   21959 C C     . LYS A 1 4505 ? 165.433 225.674 217.619 1.00 24.94 ? 4505 LYS A C     1 
ATOM   21960 O O     . LYS A 1 4505 ? 165.617 224.842 218.515 1.00 24.70 ? 4505 LYS A O     1 
ATOM   21961 C CB    . LYS A 1 4505 ? 165.993 228.069 218.082 1.00 21.37 ? 4505 LYS A CB    1 
ATOM   21962 C CG    . LYS A 1 4505 ? 165.493 227.856 219.499 1.00 20.36 ? 4505 LYS A CG    1 
ATOM   21963 C CD    . LYS A 1 4505 ? 164.932 229.133 220.089 1.00 23.85 ? 4505 LYS A CD    1 
ATOM   21964 C CE    . LYS A 1 4505 ? 163.841 228.826 221.098 1.00 25.22 ? 4505 LYS A CE    1 
ATOM   21965 N NZ    . LYS A 1 4505 ? 164.336 227.954 222.197 1.00 21.15 ? 4505 LYS A NZ    1 
ATOM   21966 N N     . ASN A 1 4506 ? 164.368 225.634 216.819 1.00 20.47 ? 4506 ASN A N     1 
ATOM   21967 C CA    . ASN A 1 4506 ? 163.298 224.659 216.980 1.00 19.27 ? 4506 ASN A CA    1 
ATOM   21968 C C     . ASN A 1 4506 ? 163.625 223.311 216.349 1.00 20.65 ? 4506 ASN A C     1 
ATOM   21969 O O     . ASN A 1 4506 ? 162.733 222.466 216.220 1.00 21.73 ? 4506 ASN A O     1 
ATOM   21970 C CB    . ASN A 1 4506 ? 161.996 225.208 216.396 1.00 25.16 ? 4506 ASN A CB    1 
ATOM   21971 C CG    . ASN A 1 4506 ? 161.585 226.523 217.024 1.00 26.39 ? 4506 ASN A CG    1 
ATOM   21972 O OD1   . ASN A 1 4506 ? 162.246 227.021 217.935 1.00 22.78 ? 4506 ASN A OD1   1 
ATOM   21973 N ND2   . ASN A 1 4506 ? 160.490 227.095 216.539 1.00 27.50 ? 4506 ASN A ND2   1 
ATOM   21974 N N     . ILE A 1 4507 ? 164.874 223.091 215.954 1.00 18.66 ? 4507 ILE A N     1 
ATOM   21975 C CA    . ILE A 1 4507 ? 165.302 221.809 215.407 1.00 19.18 ? 4507 ILE A CA    1 
ATOM   21976 C C     . ILE A 1 4507 ? 165.507 220.842 216.564 1.00 20.64 ? 4507 ILE A C     1 
ATOM   21977 O O     . ILE A 1 4507 ? 166.317 221.096 217.462 1.00 23.57 ? 4507 ILE A O     1 
ATOM   21978 C CB    . ILE A 1 4507 ? 166.586 221.953 214.577 1.00 19.95 ? 4507 ILE A CB    1 
ATOM   21979 C CG1   . ILE A 1 4507 ? 166.273 222.503 213.188 1.00 20.73 ? 4507 ILE A CG1   1 
ATOM   21980 C CG2   . ILE A 1 4507 ? 167.295 220.617 214.449 1.00 21.36 ? 4507 ILE A CG2   1 
ATOM   21981 C CD1   . ILE A 1 4507 ? 167.503 222.756 212.351 1.00 19.86 ? 4507 ILE A CD1   1 
ATOM   21982 N N     . HIS A 1 4508 ? 164.767 219.733 216.547 1.00 15.38 ? 4508 HIS A N     1 
ATOM   21983 C CA    . HIS A 1 4508 ? 164.939 218.671 217.535 1.00 13.72 ? 4508 HIS A CA    1 
ATOM   21984 C C     . HIS A 1 4508 ? 166.063 217.753 217.054 1.00 13.70 ? 4508 HIS A C     1 
ATOM   21985 O O     . HIS A 1 4508 ? 165.854 216.633 216.585 1.00 19.90 ? 4508 HIS A O     1 
ATOM   21986 C CB    . HIS A 1 4508 ? 163.634 217.918 217.744 1.00 16.62 ? 4508 HIS A CB    1 
ATOM   21987 C CG    . HIS A 1 4508 ? 162.640 218.656 218.585 1.00 17.16 ? 4508 HIS A CG    1 
ATOM   21988 N ND1   . HIS A 1 4508 ? 161.318 218.281 218.678 1.00 22.39 ? 4508 HIS A ND1   1 
ATOM   21989 C CD2   . HIS A 1 4508 ? 162.774 219.755 219.364 1.00 17.53 ? 4508 HIS A CD2   1 
ATOM   21990 C CE1   . HIS A 1 4508 ? 160.681 219.113 219.481 1.00 22.60 ? 4508 HIS A CE1   1 
ATOM   21991 N NE2   . HIS A 1 4508 ? 161.542 220.017 219.912 1.00 20.60 ? 4508 HIS A NE2   1 
ATOM   21992 N N     . VAL A 1 4509 ? 167.286 218.267 217.171 1.00 15.19 ? 4509 VAL A N     1 
ATOM   21993 C CA    . VAL A 1 4509 ? 168.434 217.620 216.555 1.00 15.03 ? 4509 VAL A CA    1 
ATOM   21994 C C     . VAL A 1 4509 ? 168.797 216.353 217.324 1.00 14.31 ? 4509 VAL A C     1 
ATOM   21995 O O     . VAL A 1 4509 ? 168.547 216.231 218.530 1.00 18.14 ? 4509 VAL A O     1 
ATOM   21996 C CB    . VAL A 1 4509 ? 169.620 218.601 216.489 1.00 13.07 ? 4509 VAL A CB    1 
ATOM   21997 C CG1   . VAL A 1 4509 ? 170.236 218.811 217.865 1.00 9.85  ? 4509 VAL A CG1   1 
ATOM   21998 C CG2   . VAL A 1 4509 ? 170.647 218.143 215.476 1.00 17.12 ? 4509 VAL A CG2   1 
ATOM   21999 N N     . CYS A 1 4510 ? 169.379 215.389 216.613 1.00 12.71 ? 4510 CYS A N     1 
ATOM   22000 C CA    . CYS A 1 4510 ? 169.828 214.132 217.201 1.00 11.64 ? 4510 CYS A CA    1 
ATOM   22001 C C     . CYS A 1 4510 ? 171.314 214.258 217.515 1.00 11.80 ? 4510 CYS A C     1 
ATOM   22002 O O     . CYS A 1 4510 ? 172.148 214.270 216.605 1.00 12.10 ? 4510 CYS A O     1 
ATOM   22003 C CB    . CYS A 1 4510 ? 169.560 212.963 216.257 1.00 11.44 ? 4510 CYS A CB    1 
ATOM   22004 S SG    . CYS A 1 4510 ? 170.437 211.443 216.678 1.00 12.19 ? 4510 CYS A SG    1 
ATOM   22005 N N     . LEU A 1 4511 ? 171.640 214.330 218.808 1.00 9.83  ? 4511 LEU A N     1 
ATOM   22006 C CA    . LEU A 1 4511 ? 173.010 214.616 219.225 1.00 7.17  ? 4511 LEU A CA    1 
ATOM   22007 C C     . LEU A 1 4511 ? 173.987 213.541 218.770 1.00 6.68  ? 4511 LEU A C     1 
ATOM   22008 O O     . LEU A 1 4511 ? 175.161 213.836 218.525 1.00 7.37  ? 4511 LEU A O     1 
ATOM   22009 C CB    . LEU A 1 4511 ? 173.070 214.772 220.743 1.00 8.66  ? 4511 LEU A CB    1 
ATOM   22010 C CG    . LEU A 1 4511 ? 174.276 215.528 221.300 1.00 6.14  ? 4511 LEU A CG    1 
ATOM   22011 C CD1   . LEU A 1 4511 ? 174.235 216.980 220.869 1.00 9.85  ? 4511 LEU A CD1   1 
ATOM   22012 C CD2   . LEU A 1 4511 ? 174.330 215.417 222.813 1.00 8.22  ? 4511 LEU A CD2   1 
ATOM   22013 N N     . GLY A 1 4512 ? 173.530 212.294 218.659 1.00 7.05  ? 4512 GLY A N     1 
ATOM   22014 C CA    . GLY A 1 4512 ? 174.424 211.226 218.241 1.00 9.60  ? 4512 GLY A CA    1 
ATOM   22015 C C     . GLY A 1 4512 ? 174.930 211.401 216.822 1.00 10.99 ? 4512 GLY A C     1 
ATOM   22016 O O     . GLY A 1 4512 ? 176.069 211.045 216.511 1.00 9.48  ? 4512 GLY A O     1 
ATOM   22017 N N     . GLY A 1 4513 ? 174.093 211.950 215.943 1.00 13.80 ? 4513 GLY A N     1 
ATOM   22018 C CA    . GLY A 1 4513 ? 174.451 212.096 214.547 1.00 5.14  ? 4513 GLY A CA    1 
ATOM   22019 C C     . GLY A 1 4513 ? 175.379 213.245 214.223 1.00 9.42  ? 4513 GLY A C     1 
ATOM   22020 O O     . GLY A 1 4513 ? 175.929 213.279 213.119 1.00 14.82 ? 4513 GLY A O     1 
ATOM   22021 N N     . LEU A 1 4514 ? 175.564 214.191 215.138 1.00 15.35 ? 4514 LEU A N     1 
ATOM   22022 C CA    . LEU A 1 4514 ? 176.445 215.316 214.860 1.00 10.74 ? 4514 LEU A CA    1 
ATOM   22023 C C     . LEU A 1 4514 ? 177.892 214.848 214.805 1.00 9.35  ? 4514 LEU A C     1 
ATOM   22024 O O     . LEU A 1 4514 ? 178.292 213.925 215.519 1.00 13.75 ? 4514 LEU A O     1 
ATOM   22025 C CB    . LEU A 1 4514 ? 176.292 216.408 215.919 1.00 7.23  ? 4514 LEU A CB    1 
ATOM   22026 C CG    . LEU A 1 4514 ? 175.162 217.425 215.740 1.00 4.09  ? 4514 LEU A CG    1 
ATOM   22027 C CD1   . LEU A 1 4514 ? 175.319 218.191 214.443 1.00 10.15 ? 4514 LEU A CD1   1 
ATOM   22028 C CD2   . LEU A 1 4514 ? 173.816 216.764 215.800 1.00 7.26  ? 4514 LEU A CD2   1 
ATOM   22029 N N     . PHE A 1 4515 ? 178.681 215.492 213.944 1.00 1.98  ? 4515 PHE A N     1 
ATOM   22030 C CA    . PHE A 1 4515 ? 180.087 215.124 213.821 1.00 8.63  ? 4515 PHE A CA    1 
ATOM   22031 C C     . PHE A 1 4515 ? 180.876 215.584 215.039 1.00 13.54 ? 4515 PHE A C     1 
ATOM   22032 O O     . PHE A 1 4515 ? 181.792 214.889 215.495 1.00 13.13 ? 4515 PHE A O     1 
ATOM   22033 C CB    . PHE A 1 4515 ? 180.667 215.720 212.540 1.00 8.15  ? 4515 PHE A CB    1 
ATOM   22034 C CG    . PHE A 1 4515 ? 180.034 215.185 211.288 1.00 11.48 ? 4515 PHE A CG    1 
ATOM   22035 C CD1   . PHE A 1 4515 ? 180.016 213.827 211.027 1.00 10.99 ? 4515 PHE A CD1   1 
ATOM   22036 C CD2   . PHE A 1 4515 ? 179.443 216.042 210.378 1.00 13.24 ? 4515 PHE A CD2   1 
ATOM   22037 C CE1   . PHE A 1 4515 ? 179.427 213.335 209.878 1.00 10.52 ? 4515 PHE A CE1   1 
ATOM   22038 C CE2   . PHE A 1 4515 ? 178.853 215.556 209.230 1.00 11.05 ? 4515 PHE A CE2   1 
ATOM   22039 C CZ    . PHE A 1 4515 ? 178.845 214.201 208.979 1.00 7.72  ? 4515 PHE A CZ    1 
ATOM   22040 N N     . VAL A 1 4516 ? 180.539 216.755 215.571 1.00 9.01  ? 4516 VAL A N     1 
ATOM   22041 C CA    . VAL A 1 4516 ? 181.126 217.284 216.799 1.00 3.30  ? 4516 VAL A CA    1 
ATOM   22042 C C     . VAL A 1 4516 ? 180.009 217.793 217.706 1.00 6.60  ? 4516 VAL A C     1 
ATOM   22043 O O     . VAL A 1 4516 ? 179.756 219.005 217.763 1.00 15.18 ? 4516 VAL A O     1 
ATOM   22044 C CB    . VAL A 1 4516 ? 182.168 218.372 216.487 1.00 4.14  ? 4516 VAL A CB    1 
ATOM   22045 C CG1   . VAL A 1 4516 ? 183.427 217.740 215.932 1.00 6.01  ? 4516 VAL A CG1   1 
ATOM   22046 C CG2   . VAL A 1 4516 ? 181.627 219.340 215.449 1.00 12.99 ? 4516 VAL A CG2   1 
ATOM   22047 N N     . PRO A 1 4517 ? 179.309 216.909 218.425 1.00 2.62  ? 4517 PRO A N     1 
ATOM   22048 C CA    . PRO A 1 4517 ? 178.186 217.369 219.264 1.00 0.00  ? 4517 PRO A CA    1 
ATOM   22049 C C     . PRO A 1 4517 ? 178.595 218.345 220.353 1.00 2.67  ? 4517 PRO A C     1 
ATOM   22050 O O     . PRO A 1 4517 ? 177.773 219.166 220.783 1.00 8.73  ? 4517 PRO A O     1 
ATOM   22051 C CB    . PRO A 1 4517 ? 177.634 216.064 219.856 1.00 3.64  ? 4517 PRO A CB    1 
ATOM   22052 C CG    . PRO A 1 4517 ? 178.183 214.972 218.996 1.00 6.82  ? 4517 PRO A CG    1 
ATOM   22053 C CD    . PRO A 1 4517 ? 179.506 215.455 218.508 1.00 1.31  ? 4517 PRO A CD    1 
ATOM   22054 N N     . GLU A 1 4518 ? 179.842 218.274 220.822 1.00 2.89  ? 4518 GLU A N     1 
ATOM   22055 C CA    . GLU A 1 4518 ? 180.317 219.246 221.798 1.00 1.23  ? 4518 GLU A CA    1 
ATOM   22056 C C     . GLU A 1 4518 ? 180.304 220.651 221.211 1.00 3.18  ? 4518 GLU A C     1 
ATOM   22057 O O     . GLU A 1 4518 ? 179.987 221.624 221.907 1.00 10.53 ? 4518 GLU A O     1 
ATOM   22058 C CB    . GLU A 1 4518 ? 181.716 218.862 222.276 1.00 3.04  ? 4518 GLU A CB    1 
ATOM   22059 C CG    . GLU A 1 4518 ? 182.399 219.914 223.128 1.00 8.28  ? 4518 GLU A CG    1 
ATOM   22060 C CD    . GLU A 1 4518 ? 183.461 219.324 224.033 1.00 11.14 ? 4518 GLU A CD    1 
ATOM   22061 O OE1   . GLU A 1 4518 ? 183.718 218.106 223.930 1.00 7.08  ? 4518 GLU A OE1   1 
ATOM   22062 O OE2   . GLU A 1 4518 ? 184.038 220.077 224.846 1.00 9.16  ? 4518 GLU A OE2   1 
ATOM   22063 N N     . ALA A 1 4519 ? 180.635 220.776 219.923 1.00 2.34  ? 4519 ALA A N     1 
ATOM   22064 C CA    . ALA A 1 4519 ? 180.496 222.061 219.250 1.00 2.88  ? 4519 ALA A CA    1 
ATOM   22065 C C     . ALA A 1 4519 ? 179.042 222.506 219.194 1.00 2.50  ? 4519 ALA A C     1 
ATOM   22066 O O     . ALA A 1 4519 ? 178.764 223.705 219.268 1.00 6.15  ? 4519 ALA A O     1 
ATOM   22067 C CB    . ALA A 1 4519 ? 181.089 221.992 217.845 1.00 1.31  ? 4519 ALA A CB    1 
ATOM   22068 N N     . TYR A 1 4520 ? 178.100 221.567 219.069 1.00 2.57  ? 4520 TYR A N     1 
ATOM   22069 C CA    . TYR A 1 4520 ? 176.690 221.944 219.125 1.00 3.59  ? 4520 TYR A CA    1 
ATOM   22070 C C     . TYR A 1 4520 ? 176.317 222.483 220.498 1.00 4.15  ? 4520 TYR A C     1 
ATOM   22071 O O     . TYR A 1 4520 ? 175.567 223.460 220.606 1.00 11.46 ? 4520 TYR A O     1 
ATOM   22072 C CB    . TYR A 1 4520 ? 175.793 220.759 218.779 1.00 3.52  ? 4520 TYR A CB    1 
ATOM   22073 C CG    . TYR A 1 4520 ? 174.331 221.055 219.018 1.00 3.82  ? 4520 TYR A CG    1 
ATOM   22074 C CD1   . TYR A 1 4520 ? 173.657 221.983 218.237 1.00 1.21  ? 4520 TYR A CD1   1 
ATOM   22075 C CD2   . TYR A 1 4520 ? 173.631 220.426 220.035 1.00 3.38  ? 4520 TYR A CD2   1 
ATOM   22076 C CE1   . TYR A 1 4520 ? 172.325 222.265 218.454 1.00 1.84  ? 4520 TYR A CE1   1 
ATOM   22077 C CE2   . TYR A 1 4520 ? 172.299 220.702 220.260 1.00 6.30  ? 4520 TYR A CE2   1 
ATOM   22078 C CZ    . TYR A 1 4520 ? 171.652 221.622 219.467 1.00 9.31  ? 4520 TYR A CZ    1 
ATOM   22079 O OH    . TYR A 1 4520 ? 170.324 221.899 219.688 1.00 14.55 ? 4520 TYR A OH    1 
ATOM   22080 N N     . ILE A 1 4521 ? 176.815 221.846 221.559 1.00 3.48  ? 4521 ILE A N     1 
ATOM   22081 C CA    . ILE A 1 4521 ? 176.536 222.327 222.910 1.00 4.40  ? 4521 ILE A CA    1 
ATOM   22082 C C     . ILE A 1 4521 ? 177.114 223.724 223.098 1.00 6.87  ? 4521 ILE A C     1 
ATOM   22083 O O     . ILE A 1 4521 ? 176.462 224.623 223.652 1.00 9.22  ? 4521 ILE A O     1 
ATOM   22084 C CB    . ILE A 1 4521 ? 177.093 221.336 223.950 1.00 4.38  ? 4521 ILE A CB    1 
ATOM   22085 C CG1   . ILE A 1 4521 ? 176.361 219.995 223.860 1.00 3.50  ? 4521 ILE A CG1   1 
ATOM   22086 C CG2   . ILE A 1 4521 ? 176.974 221.908 225.352 1.00 4.33  ? 4521 ILE A CG2   1 
ATOM   22087 C CD1   . ILE A 1 4521 ? 174.864 220.116 223.722 1.00 0.41  ? 4521 ILE A CD1   1 
ATOM   22088 N N     . THR A 1 4522 ? 178.343 223.931 222.619 1.00 4.65  ? 4522 THR A N     1 
ATOM   22089 C CA    . THR A 1 4522 ? 178.974 225.243 222.707 1.00 0.00  ? 4522 THR A CA    1 
ATOM   22090 C C     . THR A 1 4522 ? 178.197 226.289 221.917 1.00 6.47  ? 4522 THR A C     1 
ATOM   22091 O O     . THR A 1 4522 ? 178.034 227.425 222.372 1.00 10.12 ? 4522 THR A O     1 
ATOM   22092 C CB    . THR A 1 4522 ? 180.415 225.161 222.210 1.00 0.00  ? 4522 THR A CB    1 
ATOM   22093 O OG1   . THR A 1 4522 ? 181.153 224.247 223.030 1.00 2.03  ? 4522 THR A OG1   1 
ATOM   22094 C CG2   . THR A 1 4522 ? 181.074 226.523 222.261 1.00 1.83  ? 4522 THR A CG2   1 
ATOM   22095 N N     . ALA A 1 4523 ? 177.714 225.926 220.728 1.00 2.19  ? 4523 ALA A N     1 
ATOM   22096 C CA    . ALA A 1 4523 ? 176.956 226.868 219.912 1.00 0.00  ? 4523 ALA A CA    1 
ATOM   22097 C C     . ALA A 1 4523 ? 175.623 227.214 220.559 1.00 0.00  ? 4523 ALA A C     1 
ATOM   22098 O O     . ALA A 1 4523 ? 175.167 228.357 220.474 1.00 11.20 ? 4523 ALA A O     1 
ATOM   22099 C CB    . ALA A 1 4523 ? 176.743 226.296 218.513 1.00 1.45  ? 4523 ALA A CB    1 
ATOM   22100 N N     . THR A 1 4524 ? 174.977 226.239 221.196 1.00 0.60  ? 4524 THR A N     1 
ATOM   22101 C CA    . THR A 1 4524 ? 173.754 226.524 221.939 1.00 3.94  ? 4524 THR A CA    1 
ATOM   22102 C C     . THR A 1 4524 ? 174.020 227.487 223.090 1.00 6.73  ? 4524 THR A C     1 
ATOM   22103 O O     . THR A 1 4524 ? 173.255 228.437 223.314 1.00 11.17 ? 4524 THR A O     1 
ATOM   22104 C CB    . THR A 1 4524 ? 173.153 225.219 222.458 1.00 9.82  ? 4524 THR A CB    1 
ATOM   22105 O OG1   . THR A 1 4524 ? 172.825 224.369 221.352 1.00 12.79 ? 4524 THR A OG1   1 
ATOM   22106 C CG2   . THR A 1 4524 ? 171.915 225.490 223.270 1.00 9.43  ? 4524 THR A CG2   1 
ATOM   22107 N N     . ARG A 1 4525 ? 175.112 227.260 223.824 1.00 5.44  ? 4525 ARG A N     1 
ATOM   22108 C CA    . ARG A 1 4525 ? 175.490 228.179 224.892 1.00 1.62  ? 4525 ARG A CA    1 
ATOM   22109 C C     . ARG A 1 4525 ? 175.748 229.577 224.345 1.00 7.24  ? 4525 ARG A C     1 
ATOM   22110 O O     . ARG A 1 4525 ? 175.320 230.573 224.937 1.00 11.03 ? 4525 ARG A O     1 
ATOM   22111 C CB    . ARG A 1 4525 ? 176.727 227.651 225.612 1.00 1.59  ? 4525 ARG A CB    1 
ATOM   22112 C CG    . ARG A 1 4525 ? 176.959 228.247 226.980 1.00 2.70  ? 4525 ARG A CG    1 
ATOM   22113 C CD    . ARG A 1 4525 ? 178.192 227.644 227.615 1.00 0.00  ? 4525 ARG A CD    1 
ATOM   22114 N NE    . ARG A 1 4525 ? 178.295 227.979 229.029 1.00 5.70  ? 4525 ARG A NE    1 
ATOM   22115 C CZ    . ARG A 1 4525 ? 179.329 227.670 229.796 1.00 9.18  ? 4525 ARG A CZ    1 
ATOM   22116 N NH1   . ARG A 1 4525 ? 180.374 227.017 229.316 1.00 5.81  ? 4525 ARG A NH1   1 
ATOM   22117 N NH2   . ARG A 1 4525 ? 179.314 228.021 231.078 1.00 13.71 ? 4525 ARG A NH2   1 
ATOM   22118 N N     . GLN A 1 4526 ? 176.446 229.665 223.212 1.00 7.63  ? 4526 GLN A N     1 
ATOM   22119 C CA    . GLN A 1 4526 ? 176.735 230.956 222.596 1.00 2.70  ? 4526 GLN A CA    1 
ATOM   22120 C C     . GLN A 1 4526 ? 175.457 231.659 222.159 1.00 4.15  ? 4526 GLN A C     1 
ATOM   22121 O O     . GLN A 1 4526 ? 175.327 232.881 222.303 1.00 11.11 ? 4526 GLN A O     1 
ATOM   22122 C CB    . GLN A 1 4526 ? 177.661 230.756 221.398 1.00 1.27  ? 4526 GLN A CB    1 
ATOM   22123 C CG    . GLN A 1 4526 ? 179.120 230.585 221.741 1.00 1.77  ? 4526 GLN A CG    1 
ATOM   22124 C CD    . GLN A 1 4526 ? 179.999 230.572 220.511 1.00 5.46  ? 4526 GLN A CD    1 
ATOM   22125 O OE1   . GLN A 1 4526 ? 180.755 229.630 220.284 1.00 4.95  ? 4526 GLN A OE1   1 
ATOM   22126 N NE2   . GLN A 1 4526 ? 179.909 231.625 219.711 1.00 10.70 ? 4526 GLN A NE2   1 
ATOM   22127 N N     . TYR A 1 4527 ? 174.511 230.905 221.597 1.00 4.13  ? 4527 TYR A N     1 
ATOM   22128 C CA    . TYR A 1 4527 ? 173.250 231.492 221.165 1.00 7.51  ? 4527 TYR A CA    1 
ATOM   22129 C C     . TYR A 1 4527 ? 172.482 232.050 222.353 1.00 6.93  ? 4527 TYR A C     1 
ATOM   22130 O O     . TYR A 1 4527 ? 171.911 233.144 222.275 1.00 12.24 ? 4527 TYR A O     1 
ATOM   22131 C CB    . TYR A 1 4527 ? 172.412 230.448 220.425 1.00 9.27  ? 4527 TYR A CB    1 
ATOM   22132 C CG    . TYR A 1 4527 ? 170.967 230.842 220.207 1.00 11.75 ? 4527 TYR A CG    1 
ATOM   22133 C CD1   . TYR A 1 4527 ? 170.596 231.593 219.102 1.00 11.32 ? 4527 TYR A CD1   1 
ATOM   22134 C CD2   . TYR A 1 4527 ? 169.979 230.477 221.108 1.00 9.59  ? 4527 TYR A CD2   1 
ATOM   22135 C CE1   . TYR A 1 4527 ? 169.283 231.957 218.894 1.00 9.98  ? 4527 TYR A CE1   1 
ATOM   22136 C CE2   . TYR A 1 4527 ? 168.664 230.839 220.911 1.00 8.53  ? 4527 TYR A CE2   1 
ATOM   22137 C CZ    . TYR A 1 4527 ? 168.321 231.579 219.803 1.00 11.94 ? 4527 TYR A CZ    1 
ATOM   22138 O OH    . TYR A 1 4527 ? 167.010 231.942 219.601 1.00 13.11 ? 4527 TYR A OH    1 
ATOM   22139 N N     . VAL A 1 4528 ? 172.453 231.310 223.463 1.00 7.25  ? 4528 VAL A N     1 
ATOM   22140 C CA    . VAL A 1 4528 ? 171.766 231.811 224.651 1.00 5.78  ? 4528 VAL A CA    1 
ATOM   22141 C C     . VAL A 1 4528 ? 172.492 233.028 225.214 1.00 6.38  ? 4528 VAL A C     1 
ATOM   22142 O O     . VAL A 1 4528 ? 171.863 233.964 225.722 1.00 9.60  ? 4528 VAL A O     1 
ATOM   22143 C CB    . VAL A 1 4528 ? 171.617 230.694 225.699 1.00 8.76  ? 4528 VAL A CB    1 
ATOM   22144 C CG1   . VAL A 1 4528 ? 171.003 231.242 226.975 1.00 6.01  ? 4528 VAL A CG1   1 
ATOM   22145 C CG2   . VAL A 1 4528 ? 170.760 229.571 225.146 1.00 12.56 ? 4528 VAL A CG2   1 
ATOM   22146 N N     . ALA A 1 4529 ? 173.824 233.040 225.130 1.00 8.50  ? 4529 ALA A N     1 
ATOM   22147 C CA    . ALA A 1 4529 ? 174.584 234.194 225.599 1.00 6.07  ? 4529 ALA A CA    1 
ATOM   22148 C C     . ALA A 1 4529 ? 174.276 235.437 224.774 1.00 8.40  ? 4529 ALA A C     1 
ATOM   22149 O O     . ALA A 1 4529 ? 174.148 236.535 225.325 1.00 19.78 ? 4529 ALA A O     1 
ATOM   22150 C CB    . ALA A 1 4529 ? 176.080 233.885 225.568 1.00 3.84  ? 4529 ALA A CB    1 
ATOM   22151 N N     . GLN A 1 4530 ? 174.161 235.290 223.452 1.00 8.02  ? 4530 GLN A N     1 
ATOM   22152 C CA    . GLN A 1 4530 ? 173.828 236.436 222.610 1.00 7.90  ? 4530 GLN A CA    1 
ATOM   22153 C C     . GLN A 1 4530 ? 172.372 236.858 222.750 1.00 9.62  ? 4530 GLN A C     1 
ATOM   22154 O O     . GLN A 1 4530 ? 172.063 238.044 222.592 1.00 8.85  ? 4530 GLN A O     1 
ATOM   22155 C CB    . GLN A 1 4530 ? 174.116 236.146 221.138 1.00 6.56  ? 4530 GLN A CB    1 
ATOM   22156 C CG    . GLN A 1 4530 ? 175.548 235.799 220.824 1.00 8.65  ? 4530 GLN A CG    1 
ATOM   22157 C CD    . GLN A 1 4530 ? 175.791 235.682 219.334 1.00 13.68 ? 4530 GLN A CD    1 
ATOM   22158 O OE1   . GLN A 1 4530 ? 174.850 235.576 218.548 1.00 13.56 ? 4530 GLN A OE1   1 
ATOM   22159 N NE2   . GLN A 1 4530 ? 177.058 235.701 218.936 1.00 12.57 ? 4530 GLN A NE2   1 
ATOM   22160 N N     . ALA A 1 4531 ? 171.470 235.913 223.025 1.00 10.68 ? 4531 ALA A N     1 
ATOM   22161 C CA    . ALA A 1 4531 ? 170.054 236.252 223.131 1.00 9.56  ? 4531 ALA A CA    1 
ATOM   22162 C C     . ALA A 1 4531 ? 169.814 237.269 224.237 1.00 12.62 ? 4531 ALA A C     1 
ATOM   22163 O O     . ALA A 1 4531 ? 169.013 238.196 224.077 1.00 15.69 ? 4531 ALA A O     1 
ATOM   22164 C CB    . ALA A 1 4531 ? 169.227 234.989 223.370 1.00 9.92  ? 4531 ALA A CB    1 
ATOM   22165 N N     . ASN A 1 4532 ? 170.497 237.111 225.362 1.00 9.07  ? 4532 ASN A N     1 
ATOM   22166 C CA    . ASN A 1 4532 ? 170.435 238.055 226.462 1.00 13.50 ? 4532 ASN A CA    1 
ATOM   22167 C C     . ASN A 1 4532 ? 171.726 238.869 226.494 1.00 13.86 ? 4532 ASN A C     1 
ATOM   22168 O O     . ASN A 1 4532 ? 172.586 238.749 225.619 1.00 14.91 ? 4532 ASN A O     1 
ATOM   22169 C CB    . ASN A 1 4532 ? 170.188 237.306 227.772 1.00 11.92 ? 4532 ASN A CB    1 
ATOM   22170 C CG    . ASN A 1 4532 ? 168.762 236.806 227.896 1.00 14.00 ? 4532 ASN A CG    1 
ATOM   22171 O OD1   . ASN A 1 4532 ? 167.840 237.582 228.146 1.00 16.66 ? 4532 ASN A OD1   1 
ATOM   22172 N ND2   . ASN A 1 4532 ? 168.574 235.505 227.716 1.00 13.64 ? 4532 ASN A ND2   1 
ATOM   22173 N N     . SER A 1 4533 ? 171.867 239.719 227.505 1.00 14.49 ? 4533 SER A N     1 
ATOM   22174 C CA    . SER A 1 4533 ? 173.109 240.448 227.722 1.00 18.92 ? 4533 SER A CA    1 
ATOM   22175 C C     . SER A 1 4533 ? 174.131 239.623 228.488 1.00 20.25 ? 4533 SER A C     1 
ATOM   22176 O O     . SER A 1 4533 ? 175.232 240.115 228.759 1.00 24.69 ? 4533 SER A O     1 
ATOM   22177 C CB    . SER A 1 4533 ? 172.836 241.756 228.473 1.00 23.59 ? 4533 SER A CB    1 
ATOM   22178 O OG    . SER A 1 4533 ? 172.329 241.503 229.771 1.00 24.46 ? 4533 SER A OG    1 
ATOM   22179 N N     . TRP A 1 4534 ? 173.789 238.388 228.837 1.00 15.27 ? 4534 TRP A N     1 
ATOM   22180 C CA    . TRP A 1 4534 ? 174.648 237.533 229.636 1.00 10.76 ? 4534 TRP A CA    1 
ATOM   22181 C C     . TRP A 1 4534 ? 175.891 237.130 228.851 1.00 9.08  ? 4534 TRP A C     1 
ATOM   22182 O O     . TRP A 1 4534 ? 175.912 237.130 227.618 1.00 6.67  ? 4534 TRP A O     1 
ATOM   22183 C CB    . TRP A 1 4534 ? 173.884 236.286 230.078 1.00 11.84 ? 4534 TRP A CB    1 
ATOM   22184 C CG    . TRP A 1 4534 ? 172.550 236.585 230.693 1.00 16.99 ? 4534 TRP A CG    1 
ATOM   22185 C CD1   . TRP A 1 4534 ? 172.157 237.756 231.275 1.00 17.87 ? 4534 TRP A CD1   1 
ATOM   22186 C CD2   . TRP A 1 4534 ? 171.423 235.705 230.764 1.00 14.62 ? 4534 TRP A CD2   1 
ATOM   22187 N NE1   . TRP A 1 4534 ? 170.861 237.653 231.715 1.00 19.26 ? 4534 TRP A NE1   1 
ATOM   22188 C CE2   . TRP A 1 4534 ? 170.387 236.404 231.413 1.00 20.59 ? 4534 TRP A CE2   1 
ATOM   22189 C CE3   . TRP A 1 4534 ? 171.191 234.392 230.347 1.00 9.34  ? 4534 TRP A CE3   1 
ATOM   22190 C CZ2   . TRP A 1 4534 ? 169.141 235.835 231.655 1.00 19.86 ? 4534 TRP A CZ2   1 
ATOM   22191 C CZ3   . TRP A 1 4534 ? 169.954 233.828 230.589 1.00 15.76 ? 4534 TRP A CZ3   1 
ATOM   22192 C CH2   . TRP A 1 4534 ? 168.944 234.549 231.236 1.00 18.43 ? 4534 TRP A CH2   1 
ATOM   22193 N N     . SER A 1 4535 ? 176.942 236.792 229.588 1.00 13.52 ? 4535 SER A N     1 
ATOM   22194 C CA    . SER A 1 4535 ? 178.162 236.282 228.989 1.00 6.69  ? 4535 SER A CA    1 
ATOM   22195 C C     . SER A 1 4535 ? 178.145 234.755 228.981 1.00 8.28  ? 4535 SER A C     1 
ATOM   22196 O O     . SER A 1 4535 ? 177.250 234.112 229.532 1.00 10.78 ? 4535 SER A O     1 
ATOM   22197 C CB    . SER A 1 4535 ? 179.388 236.807 229.732 1.00 9.59  ? 4535 SER A CB    1 
ATOM   22198 O OG    . SER A 1 4535 ? 179.675 236.009 230.863 1.00 12.92 ? 4535 SER A OG    1 
ATOM   22199 N N     . LEU A 1 4536 ? 179.155 234.174 228.334 1.00 8.07  ? 4536 LEU A N     1 
ATOM   22200 C CA    . LEU A 1 4536 ? 179.163 232.730 228.125 1.00 7.75  ? 4536 LEU A CA    1 
ATOM   22201 C C     . LEU A 1 4536 ? 179.420 231.972 229.422 1.00 11.18 ? 4536 LEU A C     1 
ATOM   22202 O O     . LEU A 1 4536 ? 178.727 230.993 229.721 1.00 12.75 ? 4536 LEU A O     1 
ATOM   22203 C CB    . LEU A 1 4536 ? 180.204 232.364 227.069 1.00 3.19  ? 4536 LEU A CB    1 
ATOM   22204 C CG    . LEU A 1 4536 ? 180.202 230.918 226.577 1.00 4.89  ? 4536 LEU A CG    1 
ATOM   22205 C CD1   . LEU A 1 4536 ? 180.369 230.884 225.078 1.00 3.76  ? 4536 LEU A CD1   1 
ATOM   22206 C CD2   . LEU A 1 4536 ? 181.311 230.125 227.247 1.00 6.74  ? 4536 LEU A CD2   1 
ATOM   22207 N N     . GLU A 1 4537 ? 180.405 232.406 230.206 1.00 7.64  ? 4537 GLU A N     1 
ATOM   22208 C CA    . GLU A 1 4537 ? 180.783 231.689 231.418 1.00 5.34  ? 4537 GLU A CA    1 
ATOM   22209 C C     . GLU A 1 4537 ? 179.750 231.814 232.530 1.00 8.73  ? 4537 GLU A C     1 
ATOM   22210 O O     . GLU A 1 4537 ? 179.842 231.086 233.523 1.00 11.26 ? 4537 GLU A O     1 
ATOM   22211 C CB    . GLU A 1 4537 ? 182.143 232.186 231.918 1.00 6.25  ? 4537 GLU A CB    1 
ATOM   22212 C CG    . GLU A 1 4537 ? 182.063 233.317 232.931 1.00 6.90  ? 4537 GLU A CG    1 
ATOM   22213 C CD    . GLU A 1 4537 ? 181.936 234.681 232.287 1.00 5.92  ? 4537 GLU A CD    1 
ATOM   22214 O OE1   . GLU A 1 4537 ? 181.729 234.748 231.059 1.00 4.85  ? 4537 GLU A OE1   1 
ATOM   22215 O OE2   . GLU A 1 4537 ? 182.033 235.690 233.015 1.00 9.69  ? 4537 GLU A OE2   1 
ATOM   22216 N N     . GLU A 1 4538 ? 178.773 232.705 232.387 1.00 7.87  ? 4538 GLU A N     1 
ATOM   22217 C CA    . GLU A 1 4538 ? 177.750 232.930 233.397 1.00 7.78  ? 4538 GLU A CA    1 
ATOM   22218 C C     . GLU A 1 4538 ? 176.542 232.020 233.221 1.00 16.26 ? 4538 GLU A C     1 
ATOM   22219 O O     . GLU A 1 4538 ? 175.483 232.298 233.793 1.00 18.93 ? 4538 GLU A O     1 
ATOM   22220 C CB    . GLU A 1 4538 ? 177.302 234.391 233.370 1.00 8.66  ? 4538 GLU A CB    1 
ATOM   22221 C CG    . GLU A 1 4538 ? 178.367 235.384 233.796 1.00 12.73 ? 4538 GLU A CG    1 
ATOM   22222 C CD    . GLU A 1 4538 ? 177.925 236.822 233.613 1.00 16.82 ? 4538 GLU A CD    1 
ATOM   22223 O OE1   . GLU A 1 4538 ? 177.197 237.101 232.637 1.00 15.45 ? 4538 GLU A OE1   1 
ATOM   22224 O OE2   . GLU A 1 4538 ? 178.310 237.676 234.439 1.00 16.37 ? 4538 GLU A OE2   1 
ATOM   22225 N N     . LEU A 1 4539 ? 176.669 230.949 232.443 1.00 12.37 ? 4539 LEU A N     1 
ATOM   22226 C CA    . LEU A 1 4539 ? 175.557 230.063 232.135 1.00 6.68  ? 4539 LEU A CA    1 
ATOM   22227 C C     . LEU A 1 4539 ? 175.856 228.648 232.604 1.00 9.58  ? 4539 LEU A C     1 
ATOM   22228 O O     . LEU A 1 4539 ? 177.002 228.192 232.548 1.00 7.76  ? 4539 LEU A O     1 
ATOM   22229 C CB    . LEU A 1 4539 ? 175.257 230.055 230.635 1.00 6.69  ? 4539 LEU A CB    1 
ATOM   22230 C CG    . LEU A 1 4539 ? 174.925 231.402 229.999 1.00 6.73  ? 4539 LEU A CG    1 
ATOM   22231 C CD1   . LEU A 1 4539 ? 175.002 231.308 228.490 1.00 8.99  ? 4539 LEU A CD1   1 
ATOM   22232 C CD2   . LEU A 1 4539 ? 173.545 231.843 230.434 1.00 8.93  ? 4539 LEU A CD2   1 
ATOM   22233 N N     . CYS A 1 4540 ? 174.814 227.961 233.068 1.00 16.35 ? 4540 CYS A N     1 
ATOM   22234 C CA    . CYS A 1 4540 ? 174.892 226.562 233.456 1.00 8.87  ? 4540 CYS A CA    1 
ATOM   22235 C C     . CYS A 1 4540 ? 173.743 225.805 232.806 1.00 8.24  ? 4540 CYS A C     1 
ATOM   22236 O O     . CYS A 1 4540 ? 172.664 226.357 232.579 1.00 8.69  ? 4540 CYS A O     1 
ATOM   22237 C CB    . CYS A 1 4540 ? 174.850 226.391 234.981 1.00 10.58 ? 4540 CYS A CB    1 
ATOM   22238 S SG    . CYS A 1 4540 ? 173.241 226.708 235.736 1.00 20.71 ? 4540 CYS A SG    1 
ATOM   22239 N N     . LEU A 1 4541 ? 173.987 224.532 232.510 1.00 10.21 ? 4541 LEU A N     1 
ATOM   22240 C CA    . LEU A 1 4541 ? 173.034 223.735 231.753 1.00 4.94  ? 4541 LEU A CA    1 
ATOM   22241 C C     . LEU A 1 4541 ? 171.997 223.101 232.669 1.00 4.61  ? 4541 LEU A C     1 
ATOM   22242 O O     . LEU A 1 4541 ? 172.335 222.468 233.673 1.00 17.82 ? 4541 LEU A O     1 
ATOM   22243 C CB    . LEU A 1 4541 ? 173.766 222.652 230.961 1.00 6.42  ? 4541 LEU A CB    1 
ATOM   22244 C CG    . LEU A 1 4541 ? 172.931 221.736 230.068 1.00 4.06  ? 4541 LEU A CG    1 
ATOM   22245 C CD1   . LEU A 1 4541 ? 172.060 222.546 229.132 1.00 8.48  ? 4541 LEU A CD1   1 
ATOM   22246 C CD2   . LEU A 1 4541 ? 173.834 220.809 229.280 1.00 7.65  ? 4541 LEU A CD2   1 
ATOM   22247 N N     . GLU A 1 4542 ? 170.729 223.273 232.314 1.00 1.02  ? 4542 GLU A N     1 
ATOM   22248 C CA    . GLU A 1 4542 ? 169.620 222.628 232.999 1.00 8.54  ? 4542 GLU A CA    1 
ATOM   22249 C C     . GLU A 1 4542 ? 168.892 221.743 231.999 1.00 9.13  ? 4542 GLU A C     1 
ATOM   22250 O O     . GLU A 1 4542 ? 168.631 222.159 230.868 1.00 16.51 ? 4542 GLU A O     1 
ATOM   22251 C CB    . GLU A 1 4542 ? 168.659 223.657 233.608 1.00 8.79  ? 4542 GLU A CB    1 
ATOM   22252 C CG    . GLU A 1 4542 ? 167.533 223.051 234.428 1.00 13.55 ? 4542 GLU A CG    1 
ATOM   22253 C CD    . GLU A 1 4542 ? 166.622 224.101 235.034 1.00 14.13 ? 4542 GLU A CD    1 
ATOM   22254 O OE1   . GLU A 1 4542 ? 166.851 225.304 234.789 1.00 9.72  ? 4542 GLU A OE1   1 
ATOM   22255 O OE2   . GLU A 1 4542 ? 165.675 223.724 235.757 1.00 19.63 ? 4542 GLU A OE2   1 
ATOM   22256 N N     . VAL A 1 4543 ? 168.573 220.522 232.413 1.00 10.70 ? 4543 VAL A N     1 
ATOM   22257 C CA    . VAL A 1 4543 ? 168.059 219.510 231.501 1.00 12.80 ? 4543 VAL A CA    1 
ATOM   22258 C C     . VAL A 1 4543 ? 166.685 219.046 231.961 1.00 13.30 ? 4543 VAL A C     1 
ATOM   22259 O O     . VAL A 1 4543 ? 166.478 218.700 233.128 1.00 16.90 ? 4543 VAL A O     1 
ATOM   22260 C CB    . VAL A 1 4543 ? 169.036 218.323 231.385 1.00 14.50 ? 4543 VAL A CB    1 
ATOM   22261 C CG1   . VAL A 1 4543 ? 168.436 217.230 230.536 1.00 14.90 ? 4543 VAL A CG1   1 
ATOM   22262 C CG2   . VAL A 1 4543 ? 170.349 218.796 230.784 1.00 7.91  ? 4543 VAL A CG2   1 
ATOM   22263 N N     . ASN A 1 4544 ? 165.741 219.039 231.021 1.00 7.85  ? 4544 ASN A N     1 
ATOM   22264 C CA    . ASN A 1 4544 ? 164.359 218.650 231.290 1.00 15.59 ? 4544 ASN A CA    1 
ATOM   22265 C C     . ASN A 1 4544 ? 163.978 217.549 230.312 1.00 14.18 ? 4544 ASN A C     1 
ATOM   22266 O O     . ASN A 1 4544 ? 163.965 217.772 229.098 1.00 16.23 ? 4544 ASN A O     1 
ATOM   22267 C CB    . ASN A 1 4544 ? 163.414 219.845 231.160 1.00 17.62 ? 4544 ASN A CB    1 
ATOM   22268 C CG    . ASN A 1 4544 ? 162.008 219.534 231.632 1.00 18.86 ? 4544 ASN A CG    1 
ATOM   22269 O OD1   . ASN A 1 4544 ? 161.711 218.414 232.047 1.00 21.38 ? 4544 ASN A OD1   1 
ATOM   22270 N ND2   . ASN A 1 4544 ? 161.130 220.526 231.561 1.00 19.10 ? 4544 ASN A ND2   1 
ATOM   22271 N N     . VAL A 1 4545 ? 163.670 216.367 230.834 1.00 20.33 ? 4545 VAL A N     1 
ATOM   22272 C CA    . VAL A 1 4545 ? 163.218 215.257 230.004 1.00 16.87 ? 4545 VAL A CA    1 
ATOM   22273 C C     . VAL A 1 4545 ? 161.697 215.222 230.017 1.00 18.75 ? 4545 VAL A C     1 
ATOM   22274 O O     . VAL A 1 4545 ? 161.074 215.185 231.085 1.00 19.22 ? 4545 VAL A O     1 
ATOM   22275 C CB    . VAL A 1 4545 ? 163.809 213.929 230.501 1.00 16.64 ? 4545 VAL A CB    1 
ATOM   22276 C CG1   . VAL A 1 4545 ? 163.057 212.754 229.900 1.00 16.95 ? 4545 VAL A CG1   1 
ATOM   22277 C CG2   . VAL A 1 4545 ? 165.289 213.848 230.172 1.00 18.01 ? 4545 VAL A CG2   1 
ATOM   22278 N N     . THR A 1 4546 ? 161.094 215.236 228.834 1.00 20.78 ? 4546 THR A N     1 
ATOM   22279 C CA    . THR A 1 4546 ? 159.647 215.216 228.685 1.00 24.56 ? 4546 THR A CA    1 
ATOM   22280 C C     . THR A 1 4546 ? 159.203 213.894 228.066 1.00 26.52 ? 4546 THR A C     1 
ATOM   22281 O O     . THR A 1 4546 ? 160.014 213.017 227.759 1.00 25.06 ? 4546 THR A O     1 
ATOM   22282 C CB    . THR A 1 4546 ? 159.173 216.401 227.842 1.00 25.97 ? 4546 THR A CB    1 
ATOM   22283 O OG1   . THR A 1 4546 ? 159.822 216.373 226.565 1.00 23.75 ? 4546 THR A OG1   1 
ATOM   22284 C CG2   . THR A 1 4546 ? 159.488 217.712 228.542 1.00 22.95 ? 4546 THR A CG2   1 
ATOM   22285 N N     . THR A 1 4547 ? 157.891 213.757 227.890 1.00 35.62 ? 4547 THR A N     1 
ATOM   22286 C CA    . THR A 1 4547 ? 157.295 212.551 227.328 1.00 40.07 ? 4547 THR A CA    1 
ATOM   22287 C C     . THR A 1 4547 ? 156.732 212.771 225.933 1.00 37.22 ? 4547 THR A C     1 
ATOM   22288 O O     . THR A 1 4547 ? 157.096 212.052 224.998 1.00 36.99 ? 4547 THR A O     1 
ATOM   22289 C CB    . THR A 1 4547 ? 156.186 212.030 228.255 1.00 39.25 ? 4547 THR A CB    1 
ATOM   22290 O OG1   . THR A 1 4547 ? 155.209 213.058 228.461 1.00 38.08 ? 4547 THR A OG1   1 
ATOM   22291 C CG2   . THR A 1 4547 ? 156.765 211.611 229.598 1.00 34.83 ? 4547 THR A CG2   1 
ATOM   22292 N N     . SER A 1 4548 ? 155.848 213.750 225.768 1.00 37.19 ? 4548 SER A N     1 
ATOM   22293 C CA    . SER A 1 4548 ? 155.286 214.033 224.456 1.00 39.74 ? 4548 SER A CA    1 
ATOM   22294 C C     . SER A 1 4548 ? 156.320 214.713 223.569 1.00 40.04 ? 4548 SER A C     1 
ATOM   22295 O O     . SER A 1 4548 ? 157.119 215.532 224.031 1.00 39.86 ? 4548 SER A O     1 
ATOM   22296 C CB    . SER A 1 4548 ? 154.043 214.912 224.589 1.00 38.79 ? 4548 SER A CB    1 
ATOM   22297 O OG    . SER A 1 4548 ? 154.367 216.168 225.160 1.00 41.50 ? 4548 SER A OG    1 
ATOM   22298 N N     . GLN A 1 4549 ? 156.306 214.360 222.282 1.00 36.66 ? 4549 GLN A N     1 
ATOM   22299 C CA    . GLN A 1 4549 ? 157.218 214.980 221.329 1.00 37.39 ? 4549 GLN A CA    1 
ATOM   22300 C C     . GLN A 1 4549 ? 156.815 216.412 220.998 1.00 37.55 ? 4549 GLN A C     1 
ATOM   22301 O O     . GLN A 1 4549 ? 157.667 217.204 220.583 1.00 35.19 ? 4549 GLN A O     1 
ATOM   22302 C CB    . GLN A 1 4549 ? 157.286 214.137 220.053 1.00 37.01 ? 4549 GLN A CB    1 
ATOM   22303 C CG    . GLN A 1 4549 ? 158.322 214.597 219.035 1.00 37.50 ? 4549 GLN A CG    1 
ATOM   22304 C CD    . GLN A 1 4549 ? 159.745 214.479 219.546 1.00 38.92 ? 4549 GLN A CD    1 
ATOM   22305 O OE1   . GLN A 1 4549 ? 160.029 213.703 220.459 1.00 36.61 ? 4549 GLN A OE1   1 
ATOM   22306 N NE2   . GLN A 1 4549 ? 160.650 215.250 218.954 1.00 35.90 ? 4549 GLN A NE2   1 
ATOM   22307 N N     . GLY A 1 4550 ? 155.548 216.764 221.193 1.00 33.87 ? 4550 GLY A N     1 
ATOM   22308 C CA    . GLY A 1 4550 ? 155.065 218.087 220.851 1.00 32.73 ? 4550 GLY A CA    1 
ATOM   22309 C C     . GLY A 1 4550 ? 155.160 219.078 221.992 1.00 34.25 ? 4550 GLY A C     1 
ATOM   22310 O O     . GLY A 1 4550 ? 154.477 220.107 221.985 1.00 32.98 ? 4550 GLY A O     1 
ATOM   22311 N N     . ALA A 1 4551 ? 155.994 218.771 222.984 1.00 35.70 ? 4551 ALA A N     1 
ATOM   22312 C CA    . ALA A 1 4551 ? 156.177 219.670 224.116 1.00 36.59 ? 4551 ALA A CA    1 
ATOM   22313 C C     . ALA A 1 4551 ? 156.728 221.011 223.649 1.00 36.56 ? 4551 ALA A C     1 
ATOM   22314 O O     . ALA A 1 4551 ? 157.650 221.068 222.830 1.00 35.31 ? 4551 ALA A O     1 
ATOM   22315 C CB    . ALA A 1 4551 ? 157.115 219.039 225.145 1.00 32.82 ? 4551 ALA A CB    1 
ATOM   22316 N N     . THR A 1 4552 ? 156.154 222.091 224.172 1.00 36.12 ? 4552 THR A N     1 
ATOM   22317 C CA    . THR A 1 4552 ? 156.553 223.430 223.762 1.00 38.01 ? 4552 THR A CA    1 
ATOM   22318 C C     . THR A 1 4552 ? 157.964 223.742 224.248 1.00 36.75 ? 4552 THR A C     1 
ATOM   22319 O O     . THR A 1 4552 ? 158.330 223.437 225.386 1.00 33.69 ? 4552 THR A O     1 
ATOM   22320 C CB    . THR A 1 4552 ? 155.568 224.465 224.305 1.00 36.01 ? 4552 THR A CB    1 
ATOM   22321 O OG1   . THR A 1 4552 ? 154.232 224.081 223.958 1.00 38.33 ? 4552 THR A OG1   1 
ATOM   22322 C CG2   . THR A 1 4552 ? 155.857 225.839 223.718 1.00 36.07 ? 4552 THR A CG2   1 
ATOM   22323 N N     . LEU A 1 4553 ? 158.757 224.356 223.374 1.00 31.81 ? 4553 LEU A N     1 
ATOM   22324 C CA    . LEU A 1 4553 ? 160.132 224.709 223.691 1.00 29.59 ? 4553 LEU A CA    1 
ATOM   22325 C C     . LEU A 1 4553 ? 160.211 226.167 224.124 1.00 29.00 ? 4553 LEU A C     1 
ATOM   22326 O O     . LEU A 1 4553 ? 159.637 227.051 223.482 1.00 31.05 ? 4553 LEU A O     1 
ATOM   22327 C CB    . LEU A 1 4553 ? 161.039 224.474 222.482 1.00 32.25 ? 4553 LEU A CB    1 
ATOM   22328 C CG    . LEU A 1 4553 ? 161.837 223.168 222.447 1.00 31.61 ? 4553 LEU A CG    1 
ATOM   22329 C CD1   . LEU A 1 4553 ? 162.742 223.126 221.224 1.00 28.59 ? 4553 LEU A CD1   1 
ATOM   22330 C CD2   . LEU A 1 4553 ? 162.639 222.976 223.719 1.00 29.21 ? 4553 LEU A CD2   1 
ATOM   22331 N N     . ASP A 1 4554 ? 160.930 226.413 225.215 1.00 29.06 ? 4554 ASP A N     1 
ATOM   22332 C CA    . ASP A 1 4554 ? 161.092 227.759 225.740 1.00 27.33 ? 4554 ASP A CA    1 
ATOM   22333 C C     . ASP A 1 4554 ? 162.154 228.503 224.930 1.00 25.46 ? 4554 ASP A C     1 
ATOM   22334 O O     . ASP A 1 4554 ? 162.776 227.948 224.021 1.00 23.92 ? 4554 ASP A O     1 
ATOM   22335 C CB    . ASP A 1 4554 ? 161.437 227.709 227.227 1.00 26.35 ? 4554 ASP A CB    1 
ATOM   22336 C CG    . ASP A 1 4554 ? 160.223 227.903 228.113 1.00 30.96 ? 4554 ASP A CG    1 
ATOM   22337 O OD1   . ASP A 1 4554 ? 159.094 227.928 227.579 1.00 30.38 ? 4554 ASP A OD1   1 
ATOM   22338 O OD2   . ASP A 1 4554 ? 160.398 228.032 229.342 1.00 32.09 ? 4554 ASP A OD2   1 
ATOM   22339 N N     . ALA A 1 4555 ? 162.365 229.781 225.253 1.00 26.93 ? 4555 ALA A N     1 
ATOM   22340 C CA    . ALA A 1 4555 ? 163.313 230.593 224.497 1.00 26.55 ? 4555 ALA A CA    1 
ATOM   22341 C C     . ALA A 1 4555 ? 164.738 230.074 224.644 1.00 23.49 ? 4555 ALA A C     1 
ATOM   22342 O O     . ALA A 1 4555 ? 165.488 230.017 223.663 1.00 26.92 ? 4555 ALA A O     1 
ATOM   22343 C CB    . ALA A 1 4555 ? 163.226 232.051 224.943 1.00 24.22 ? 4555 ALA A CB    1 
ATOM   22344 N N     . CYS A 1 4556 ? 165.132 229.698 225.859 1.00 17.30 ? 4556 CYS A N     1 
ATOM   22345 C CA    . CYS A 1 4556 ? 166.471 229.187 226.112 1.00 18.20 ? 4556 CYS A CA    1 
ATOM   22346 C C     . CYS A 1 4556 ? 166.564 227.670 226.026 1.00 18.38 ? 4556 CYS A C     1 
ATOM   22347 O O     . CYS A 1 4556 ? 167.671 227.129 226.116 1.00 13.86 ? 4556 CYS A O     1 
ATOM   22348 C CB    . CYS A 1 4556 ? 166.959 229.649 227.491 1.00 17.04 ? 4556 CYS A CB    1 
ATOM   22349 S SG    . CYS A 1 4556 ? 166.001 228.997 228.877 1.00 39.01 ? 4556 CYS A SG    1 
ATOM   22350 N N     . SER A 1 4557 ? 165.443 226.977 225.850 1.00 20.51 ? 4557 SER A N     1 
ATOM   22351 C CA    . SER A 1 4557 ? 165.440 225.522 225.836 1.00 13.23 ? 4557 SER A CA    1 
ATOM   22352 C C     . SER A 1 4557 ? 165.787 224.990 224.452 1.00 14.60 ? 4557 SER A C     1 
ATOM   22353 O O     . SER A 1 4557 ? 165.396 225.565 223.432 1.00 23.67 ? 4557 SER A O     1 
ATOM   22354 C CB    . SER A 1 4557 ? 164.076 224.992 226.274 1.00 15.62 ? 4557 SER A CB    1 
ATOM   22355 O OG    . SER A 1 4557 ? 163.741 225.462 227.566 1.00 22.43 ? 4557 SER A OG    1 
ATOM   22356 N N     . PHE A 1 4558 ? 166.529 223.885 224.423 1.00 12.89 ? 4558 PHE A N     1 
ATOM   22357 C CA    . PHE A 1 4558 ? 166.932 223.231 223.184 1.00 12.38 ? 4558 PHE A CA    1 
ATOM   22358 C C     . PHE A 1 4558 ? 166.633 221.745 223.290 1.00 17.95 ? 4558 PHE A C     1 
ATOM   22359 O O     . PHE A 1 4558 ? 167.154 221.069 224.182 1.00 25.37 ? 4558 PHE A O     1 
ATOM   22360 C CB    . PHE A 1 4558 ? 168.417 223.453 222.900 1.00 7.72  ? 4558 PHE A CB    1 
ATOM   22361 C CG    . PHE A 1 4558 ? 168.725 224.795 222.317 1.00 9.65  ? 4558 PHE A CG    1 
ATOM   22362 C CD1   . PHE A 1 4558 ? 168.584 225.945 223.074 1.00 12.96 ? 4558 PHE A CD1   1 
ATOM   22363 C CD2   . PHE A 1 4558 ? 169.175 224.906 221.016 1.00 14.02 ? 4558 PHE A CD2   1 
ATOM   22364 C CE1   . PHE A 1 4558 ? 168.874 227.178 222.538 1.00 17.91 ? 4558 PHE A CE1   1 
ATOM   22365 C CE2   . PHE A 1 4558 ? 169.466 226.135 220.477 1.00 14.00 ? 4558 PHE A CE2   1 
ATOM   22366 C CZ    . PHE A 1 4558 ? 169.315 227.271 221.238 1.00 18.49 ? 4558 PHE A CZ    1 
ATOM   22367 N N     . GLY A 1 4559 ? 165.810 221.237 222.375 1.00 15.29 ? 4559 GLY A N     1 
ATOM   22368 C CA    . GLY A 1 4559 ? 165.443 219.835 222.381 1.00 16.08 ? 4559 GLY A CA    1 
ATOM   22369 C C     . GLY A 1 4559 ? 166.443 218.995 221.612 1.00 11.98 ? 4559 GLY A C     1 
ATOM   22370 O O     . GLY A 1 4559 ? 166.875 219.371 220.520 1.00 14.60 ? 4559 GLY A O     1 
ATOM   22371 N N     . VAL A 1 4560 ? 166.817 217.857 222.196 1.00 12.56 ? 4560 VAL A N     1 
ATOM   22372 C CA    . VAL A 1 4560 ? 167.659 216.873 221.533 1.00 15.46 ? 4560 VAL A CA    1 
ATOM   22373 C C     . VAL A 1 4560 ? 166.969 215.519 221.630 1.00 15.46 ? 4560 VAL A C     1 
ATOM   22374 O O     . VAL A 1 4560 ? 166.143 215.276 222.512 1.00 21.45 ? 4560 VAL A O     1 
ATOM   22375 C CB    . VAL A 1 4560 ? 169.085 216.798 222.126 1.00 14.20 ? 4560 VAL A CB    1 
ATOM   22376 C CG1   . VAL A 1 4560 ? 169.755 218.159 222.083 1.00 16.56 ? 4560 VAL A CG1   1 
ATOM   22377 C CG2   . VAL A 1 4560 ? 169.054 216.258 223.542 1.00 11.59 ? 4560 VAL A CG2   1 
ATOM   22378 N N     . THR A 1 4561 ? 167.312 214.638 220.695 1.00 9.05  ? 4561 THR A N     1 
ATOM   22379 C CA    . THR A 1 4561 ? 166.697 213.323 220.610 1.00 10.44 ? 4561 THR A CA    1 
ATOM   22380 C C     . THR A 1 4561 ? 167.784 212.279 220.403 1.00 14.73 ? 4561 THR A C     1 
ATOM   22381 O O     . THR A 1 4561 ? 168.908 212.589 220.000 1.00 18.46 ? 4561 THR A O     1 
ATOM   22382 C CB    . THR A 1 4561 ? 165.664 213.250 219.478 1.00 13.40 ? 4561 THR A CB    1 
ATOM   22383 O OG1   . THR A 1 4561 ? 166.236 213.764 218.270 1.00 12.60 ? 4561 THR A OG1   1 
ATOM   22384 C CG2   . THR A 1 4561 ? 164.425 214.059 219.830 1.00 17.88 ? 4561 THR A CG2   1 
ATOM   22385 N N     . GLY A 1 4562 ? 167.438 211.028 220.694 1.00 13.48 ? 4562 GLY A N     1 
ATOM   22386 C CA    . GLY A 1 4562 ? 168.358 209.924 220.547 1.00 12.02 ? 4562 GLY A CA    1 
ATOM   22387 C C     . GLY A 1 4562 ? 169.197 209.620 221.766 1.00 11.58 ? 4562 GLY A C     1 
ATOM   22388 O O     . GLY A 1 4562 ? 169.976 208.661 221.735 1.00 16.79 ? 4562 GLY A O     1 
ATOM   22389 N N     . LEU A 1 4563 ? 169.072 210.403 222.833 1.00 7.21  ? 4563 LEU A N     1 
ATOM   22390 C CA    . LEU A 1 4563 ? 169.828 210.138 224.047 1.00 8.47  ? 4563 LEU A CA    1 
ATOM   22391 C C     . LEU A 1 4563 ? 169.282 208.903 224.752 1.00 11.61 ? 4563 LEU A C     1 
ATOM   22392 O O     . LEU A 1 4563 ? 168.067 208.721 224.872 1.00 10.09 ? 4563 LEU A O     1 
ATOM   22393 C CB    . LEU A 1 4563 ? 169.772 211.347 224.980 1.00 11.61 ? 4563 LEU A CB    1 
ATOM   22394 C CG    . LEU A 1 4563 ? 170.602 212.569 224.583 1.00 8.62  ? 4563 LEU A CG    1 
ATOM   22395 C CD1   . LEU A 1 4563 ? 170.730 213.526 225.751 1.00 9.18  ? 4563 LEU A CD1   1 
ATOM   22396 C CD2   . LEU A 1 4563 ? 171.972 212.151 224.082 1.00 6.47  ? 4563 LEU A CD2   1 
ATOM   22397 N N     . LYS A 1 4564 ? 170.189 208.048 225.217 1.00 10.55 ? 4564 LYS A N     1 
ATOM   22398 C CA    . LYS A 1 4564 ? 169.832 206.815 225.904 1.00 8.21  ? 4564 LYS A CA    1 
ATOM   22399 C C     . LYS A 1 4564 ? 170.457 206.815 227.289 1.00 11.08 ? 4564 LYS A C     1 
ATOM   22400 O O     . LYS A 1 4564 ? 171.644 207.124 227.439 1.00 7.98  ? 4564 LYS A O     1 
ATOM   22401 C CB    . LYS A 1 4564 ? 170.290 205.587 225.112 1.00 5.37  ? 4564 LYS A CB    1 
ATOM   22402 C CG    . LYS A 1 4564 ? 169.767 205.539 223.688 1.00 6.37  ? 4564 LYS A CG    1 
ATOM   22403 C CD    . LYS A 1 4564 ? 168.317 205.092 223.653 1.00 9.58  ? 4564 LYS A CD    1 
ATOM   22404 C CE    . LYS A 1 4564 ? 167.798 205.019 222.230 1.00 10.97 ? 4564 LYS A CE    1 
ATOM   22405 N NZ    . LYS A 1 4564 ? 168.150 206.238 221.450 1.00 13.93 ? 4564 LYS A NZ    1 
ATOM   22406 N N     . LEU A 1 4565 ? 169.660 206.467 228.294 1.00 7.07  ? 4565 LEU A N     1 
ATOM   22407 C CA    . LEU A 1 4565 ? 170.100 206.458 229.682 1.00 0.25  ? 4565 LEU A CA    1 
ATOM   22408 C C     . LEU A 1 4565 ? 170.441 205.034 230.099 1.00 6.74  ? 4565 LEU A C     1 
ATOM   22409 O O     . LEU A 1 4565 ? 169.617 204.126 229.958 1.00 16.24 ? 4565 LEU A O     1 
ATOM   22410 C CB    . LEU A 1 4565 ? 169.019 207.042 230.591 1.00 1.83  ? 4565 LEU A CB    1 
ATOM   22411 C CG    . LEU A 1 4565 ? 169.335 207.140 232.080 1.00 5.80  ? 4565 LEU A CG    1 
ATOM   22412 C CD1   . LEU A 1 4565 ? 170.511 208.064 232.319 1.00 3.99  ? 4565 LEU A CD1   1 
ATOM   22413 C CD2   . LEU A 1 4565 ? 168.112 207.631 232.818 1.00 8.34  ? 4565 LEU A CD2   1 
ATOM   22414 N N     . GLN A 1 4566 ? 171.651 204.845 230.617 1.00 4.70  ? 4566 GLN A N     1 
ATOM   22415 C CA    . GLN A 1 4566 ? 172.161 203.518 230.932 1.00 0.00  ? 4566 GLN A CA    1 
ATOM   22416 C C     . GLN A 1 4566 ? 171.915 203.180 232.395 1.00 0.39  ? 4566 GLN A C     1 
ATOM   22417 O O     . GLN A 1 4566 ? 172.359 203.905 233.288 1.00 3.58  ? 4566 GLN A O     1 
ATOM   22418 C CB    . GLN A 1 4566 ? 173.655 203.433 230.625 1.00 0.31  ? 4566 GLN A CB    1 
ATOM   22419 C CG    . GLN A 1 4566 ? 174.035 203.991 229.273 1.00 2.00  ? 4566 GLN A CG    1 
ATOM   22420 C CD    . GLN A 1 4566 ? 173.899 202.968 228.171 1.00 8.23  ? 4566 GLN A CD    1 
ATOM   22421 O OE1   . GLN A 1 4566 ? 173.013 203.065 227.323 1.00 4.22  ? 4566 GLN A OE1   1 
ATOM   22422 N NE2   . GLN A 1 4566 ? 174.780 201.975 228.176 1.00 11.82 ? 4566 GLN A NE2   1 
ATOM   22423 N N     . GLY A 1 4567 ? 171.214 202.076 232.633 1.00 11.92 ? 4567 GLY A N     1 
ATOM   22424 C CA    . GLY A 1 4567 ? 171.031 201.582 233.984 1.00 13.04 ? 4567 GLY A CA    1 
ATOM   22425 C C     . GLY A 1 4567 ? 170.158 202.441 234.864 1.00 3.42  ? 4567 GLY A C     1 
ATOM   22426 O O     . GLY A 1 4567 ? 170.256 202.354 236.090 1.00 0.00  ? 4567 GLY A O     1 
ATOM   22427 N N     . ALA A 1 4568 ? 169.300 203.270 234.276 1.00 9.26  ? 4568 ALA A N     1 
ATOM   22428 C CA    . ALA A 1 4568 ? 168.429 204.134 235.057 1.00 11.50 ? 4568 ALA A CA    1 
ATOM   22429 C C     . ALA A 1 4568 ? 167.257 204.566 234.192 1.00 10.49 ? 4568 ALA A C     1 
ATOM   22430 O O     . ALA A 1 4568 ? 167.268 204.399 232.970 1.00 5.07  ? 4568 ALA A O     1 
ATOM   22431 C CB    . ALA A 1 4568 ? 169.182 205.353 235.599 1.00 8.53  ? 4568 ALA A CB    1 
ATOM   22432 N N     . THR A 1 4569 ? 166.242 205.119 234.848 1.00 9.53  ? 4569 THR A N     1 
ATOM   22433 C CA    . THR A 1 4569 ? 165.067 205.643 234.171 1.00 15.07 ? 4569 THR A CA    1 
ATOM   22434 C C     . THR A 1 4569 ? 164.546 206.843 234.946 1.00 17.61 ? 4569 THR A C     1 
ATOM   22435 O O     . THR A 1 4569 ? 164.829 207.009 236.135 1.00 17.82 ? 4569 THR A O     1 
ATOM   22436 C CB    . THR A 1 4569 ? 163.971 204.577 234.030 1.00 17.70 ? 4569 THR A CB    1 
ATOM   22437 O OG1   . THR A 1 4569 ? 162.842 205.133 233.345 1.00 24.13 ? 4569 THR A OG1   1 
ATOM   22438 C CG2   . THR A 1 4569 ? 163.534 204.074 235.396 1.00 8.28  ? 4569 THR A CG2   1 
ATOM   22439 N N     . CYS A 1 4570 ? 163.782 207.687 234.257 1.00 18.01 ? 4570 CYS A N     1 
ATOM   22440 C CA    . CYS A 1 4570 ? 163.194 208.878 234.852 1.00 23.42 ? 4570 CYS A CA    1 
ATOM   22441 C C     . CYS A 1 4570 ? 161.686 208.874 234.644 1.00 26.08 ? 4570 CYS A C     1 
ATOM   22442 O O     . CYS A 1 4570 ? 161.205 208.663 233.526 1.00 24.69 ? 4570 CYS A O     1 
ATOM   22443 C CB    . CYS A 1 4570 ? 163.808 210.152 234.262 1.00 22.17 ? 4570 CYS A CB    1 
ATOM   22444 S SG    . CYS A 1 4570 ? 163.731 210.269 232.467 1.00 34.39 ? 4570 CYS A SG    1 
ATOM   22445 N N     . ASN A 1 4571 ? 160.943 209.108 235.728 1.00 31.06 ? 4571 ASN A N     1 
ATOM   22446 C CA    . ASN A 1 4571 ? 159.486 209.132 235.643 1.00 33.50 ? 4571 ASN A CA    1 
ATOM   22447 C C     . ASN A 1 4571 ? 158.996 210.435 235.019 1.00 34.90 ? 4571 ASN A C     1 
ATOM   22448 O O     . ASN A 1 4571 ? 158.336 210.425 233.974 1.00 35.91 ? 4571 ASN A O     1 
ATOM   22449 C CB    . ASN A 1 4571 ? 158.872 208.919 237.032 1.00 32.95 ? 4571 ASN A CB    1 
ATOM   22450 C CG    . ASN A 1 4571 ? 159.482 209.820 238.089 1.00 38.30 ? 4571 ASN A CG    1 
ATOM   22451 O OD1   . ASN A 1 4571 ? 160.329 210.662 237.788 1.00 38.73 ? 4571 ASN A OD1   1 
ATOM   22452 N ND2   . ASN A 1 4571 ? 159.049 209.652 239.333 1.00 36.74 ? 4571 ASN A ND2   1 
ATOM   22453 N N     . ASN A 1 4572 ? 159.307 211.566 235.650 1.00 31.12 ? 4572 ASN A N     1 
ATOM   22454 C CA    . ASN A 1 4572 ? 159.072 212.875 235.058 1.00 35.28 ? 4572 ASN A CA    1 
ATOM   22455 C C     . ASN A 1 4572 ? 160.384 213.592 234.771 1.00 35.78 ? 4572 ASN A C     1 
ATOM   22456 O O     . ASN A 1 4572 ? 160.704 213.871 233.612 1.00 35.48 ? 4572 ASN A O     1 
ATOM   22457 C CB    . ASN A 1 4572 ? 158.192 213.724 235.986 1.00 32.22 ? 4572 ASN A CB    1 
ATOM   22458 C CG    . ASN A 1 4572 ? 156.713 213.436 235.816 1.00 35.06 ? 4572 ASN A CG    1 
ATOM   22459 O OD1   . ASN A 1 4572 ? 156.314 212.296 235.583 1.00 35.13 ? 4572 ASN A OD1   1 
ATOM   22460 N ND2   . ASN A 1 4572 ? 155.892 214.472 235.934 1.00 35.58 ? 4572 ASN A ND2   1 
ATOM   22461 N N     . ASN A 1 4573 ? 161.161 213.892 235.811 1.00 24.65 ? 4573 ASN A N     1 
ATOM   22462 C CA    . ASN A 1 4573 ? 162.537 214.327 235.609 1.00 24.20 ? 4573 ASN A CA    1 
ATOM   22463 C C     . ASN A 1 4573 ? 163.436 213.719 236.683 1.00 25.50 ? 4573 ASN A C     1 
ATOM   22464 O O     . ASN A 1 4573 ? 164.616 214.081 236.762 1.00 26.52 ? 4573 ASN A O     1 
ATOM   22465 C CB    . ASN A 1 4573 ? 162.610 215.869 235.610 1.00 24.47 ? 4573 ASN A CB    1 
ATOM   22466 C CG    . ASN A 1 4573 ? 163.946 216.408 235.111 1.00 22.51 ? 4573 ASN A CG    1 
ATOM   22467 O OD1   . ASN A 1 4573 ? 164.851 215.655 234.756 1.00 20.34 ? 4573 ASN A OD1   1 
ATOM   22468 N ND2   . ASN A 1 4573 ? 164.067 217.729 235.082 1.00 23.90 ? 4573 ASN A ND2   1 
ATOM   22469 N N     . LYS A 1 4574 ? 162.924 212.816 237.515 1.00 21.14 ? 4574 LYS A N     1 
ATOM   22470 C CA    . LYS A 1 4574 ? 163.679 212.243 238.620 1.00 18.51 ? 4574 LYS A CA    1 
ATOM   22471 C C     . LYS A 1 4574 ? 164.178 210.855 238.243 1.00 20.20 ? 4574 LYS A C     1 
ATOM   22472 O O     . LYS A 1 4574 ? 163.382 209.981 237.884 1.00 25.37 ? 4574 LYS A O     1 
ATOM   22473 C CB    . LYS A 1 4574 ? 162.822 212.173 239.884 1.00 22.66 ? 4574 LYS A CB    1 
ATOM   22474 C CG    . LYS A 1 4574 ? 162.637 213.511 240.582 1.00 19.64 ? 4574 LYS A CG    1 
ATOM   22475 C CD    . LYS A 1 4574 ? 161.630 213.424 241.719 1.00 19.18 ? 4574 LYS A CD    1 
ATOM   22476 C CE    . LYS A 1 4574 ? 161.628 212.052 242.375 1.00 26.52 ? 4574 LYS A CE    1 
ATOM   22477 N NZ    . LYS A 1 4574 ? 161.425 212.136 243.847 1.00 24.54 ? 4574 LYS A NZ    1 
ATOM   22478 N N     . LEU A 1 4575 ? 165.490 210.656 238.332 1.00 16.20 ? 4575 LEU A N     1 
ATOM   22479 C CA    . LEU A 1 4575 ? 166.075 209.372 237.983 1.00 16.43 ? 4575 LEU A CA    1 
ATOM   22480 C C     . LEU A 1 4575 ? 165.749 208.310 239.026 1.00 17.77 ? 4575 LEU A C     1 
ATOM   22481 O O     . LEU A 1 4575 ? 165.479 208.598 240.194 1.00 25.77 ? 4575 LEU A O     1 
ATOM   22482 C CB    . LEU A 1 4575 ? 167.592 209.480 237.837 1.00 11.28 ? 4575 LEU A CB    1 
ATOM   22483 C CG    . LEU A 1 4575 ? 168.161 210.247 236.648 1.00 6.23  ? 4575 LEU A CG    1 
ATOM   22484 C CD1   . LEU A 1 4575 ? 169.568 209.769 236.381 1.00 7.35  ? 4575 LEU A CD1   1 
ATOM   22485 C CD2   . LEU A 1 4575 ? 167.295 210.061 235.420 1.00 10.52 ? 4575 LEU A CD2   1 
ATOM   22486 N N     . SER A 1 4576 ? 165.780 207.059 238.575 1.00 11.67 ? 4576 SER A N     1 
ATOM   22487 C CA    . SER A 1 4576 ? 165.665 205.900 239.445 1.00 15.18 ? 4576 SER A CA    1 
ATOM   22488 C C     . SER A 1 4576 ? 166.388 204.746 238.769 1.00 12.54 ? 4576 SER A C     1 
ATOM   22489 O O     . SER A 1 4576 ? 166.402 204.656 237.539 1.00 10.96 ? 4576 SER A O     1 
ATOM   22490 C CB    . SER A 1 4576 ? 164.202 205.540 239.722 1.00 13.62 ? 4576 SER A CB    1 
ATOM   22491 O OG    . SER A 1 4576 ? 163.532 205.174 238.531 1.00 18.32 ? 4576 SER A OG    1 
ATOM   22492 N N     . LEU A 1 4577 ? 166.998 203.880 239.571 1.00 11.35 ? 4577 LEU A N     1 
ATOM   22493 C CA    . LEU A 1 4577 ? 167.753 202.764 239.019 1.00 10.10 ? 4577 LEU A CA    1 
ATOM   22494 C C     . LEU A 1 4577 ? 166.829 201.769 238.331 1.00 14.06 ? 4577 LEU A C     1 
ATOM   22495 O O     . LEU A 1 4577 ? 165.708 201.519 238.781 1.00 18.10 ? 4577 LEU A O     1 
ATOM   22496 C CB    . LEU A 1 4577 ? 168.543 202.063 240.118 1.00 10.72 ? 4577 LEU A CB    1 
ATOM   22497 C CG    . LEU A 1 4577 ? 169.781 202.791 240.626 1.00 5.39  ? 4577 LEU A CG    1 
ATOM   22498 C CD1   . LEU A 1 4577 ? 170.447 201.949 241.679 1.00 10.80 ? 4577 LEU A CD1   1 
ATOM   22499 C CD2   . LEU A 1 4577 ? 170.737 203.080 239.487 1.00 7.28  ? 4577 LEU A CD2   1 
ATOM   22500 N N     . SER A 1 4578 ? 167.308 201.203 237.226 1.00 14.00 ? 4578 SER A N     1 
ATOM   22501 C CA    . SER A 1 4578 ? 166.567 200.202 236.476 1.00 15.90 ? 4578 SER A CA    1 
ATOM   22502 C C     . SER A 1 4578 ? 167.513 199.087 236.063 1.00 21.22 ? 4578 SER A C     1 
ATOM   22503 O O     . SER A 1 4578 ? 168.666 199.343 235.706 1.00 23.29 ? 4578 SER A O     1 
ATOM   22504 C CB    . SER A 1 4578 ? 165.895 200.809 235.239 1.00 14.75 ? 4578 SER A CB    1 
ATOM   22505 O OG    . SER A 1 4578 ? 165.099 199.848 234.569 1.00 14.70 ? 4578 SER A OG    1 
ATOM   22506 N N     . ASN A 1 4579 ? 167.022 197.848 236.120 1.00 23.44 ? 4579 ASN A N     1 
ATOM   22507 C CA    . ASN A 1 4579 ? 167.838 196.715 235.700 1.00 20.73 ? 4579 ASN A CA    1 
ATOM   22508 C C     . ASN A 1 4579 ? 167.959 196.641 234.184 1.00 23.41 ? 4579 ASN A C     1 
ATOM   22509 O O     . ASN A 1 4579 ? 168.931 196.079 233.669 1.00 28.03 ? 4579 ASN A O     1 
ATOM   22510 C CB    . ASN A 1 4579 ? 167.260 195.414 236.253 1.00 19.01 ? 4579 ASN A CB    1 
ATOM   22511 C CG    . ASN A 1 4579 ? 167.231 195.389 237.767 1.00 23.50 ? 4579 ASN A CG    1 
ATOM   22512 O OD1   . ASN A 1 4579 ? 168.237 195.095 238.413 1.00 29.16 ? 4579 ASN A OD1   1 
ATOM   22513 N ND2   . ASN A 1 4579 ? 166.075 195.696 238.342 1.00 24.18 ? 4579 ASN A ND2   1 
ATOM   22514 N N     . ALA A 1 4580 ? 166.989 197.192 233.459 1.00 19.98 ? 4580 ALA A N     1 
ATOM   22515 C CA    . ALA A 1 4580 ? 167.038 197.228 232.001 1.00 19.22 ? 4580 ALA A CA    1 
ATOM   22516 C C     . ALA A 1 4580 ? 167.831 198.453 231.565 1.00 18.61 ? 4580 ALA A C     1 
ATOM   22517 O O     . ALA A 1 4580 ? 167.415 199.590 231.808 1.00 22.20 ? 4580 ALA A O     1 
ATOM   22518 C CB    . ALA A 1 4580 ? 165.628 197.249 231.420 1.00 22.25 ? 4580 ALA A CB    1 
ATOM   22519 N N     . ILE A 1 4581 ? 168.972 198.226 230.919 1.00 15.02 ? 4581 ILE A N     1 
ATOM   22520 C CA    . ILE A 1 4581 ? 169.840 199.307 230.465 1.00 15.48 ? 4581 ILE A CA    1 
ATOM   22521 C C     . ILE A 1 4581 ? 169.275 199.955 229.210 1.00 14.37 ? 4581 ILE A C     1 
ATOM   22522 O O     . ILE A 1 4581 ? 168.331 199.440 228.600 1.00 19.14 ? 4581 ILE A O     1 
ATOM   22523 C CB    . ILE A 1 4581 ? 171.270 198.802 230.208 1.00 14.52 ? 4581 ILE A CB    1 
ATOM   22524 C CG1   . ILE A 1 4581 ? 171.256 197.721 229.124 1.00 14.30 ? 4581 ILE A CG1   1 
ATOM   22525 C CG2   . ILE A 1 4581 ? 171.910 198.316 231.501 1.00 18.62 ? 4581 ILE A CG2   1 
ATOM   22526 C CD1   . ILE A 1 4581 ? 172.626 197.297 228.662 1.00 14.68 ? 4581 ILE A CD1   1 
ATOM   22527 N N     . SER A 1 4582 ? 169.853 201.093 228.827 1.00 10.96 ? 4582 SER A N     1 
ATOM   22528 C CA    . SER A 1 4582 ? 169.508 201.804 227.597 1.00 12.25 ? 4582 SER A CA    1 
ATOM   22529 C C     . SER A 1 4582 ? 168.026 202.184 227.573 1.00 10.32 ? 4582 SER A C     1 
ATOM   22530 O O     . SER A 1 4582 ? 167.250 201.737 226.726 1.00 18.50 ? 4582 SER A O     1 
ATOM   22531 C CB    . SER A 1 4582 ? 169.888 200.980 226.363 1.00 14.46 ? 4582 SER A CB    1 
ATOM   22532 O OG    . SER A 1 4582 ? 169.927 201.794 225.204 1.00 13.95 ? 4582 SER A OG    1 
ATOM   22533 N N     . THR A 1 4583 ? 167.646 203.026 228.528 1.00 5.78  ? 4583 THR A N     1 
ATOM   22534 C CA    . THR A 1 4583 ? 166.312 203.604 228.558 1.00 8.17  ? 4583 THR A CA    1 
ATOM   22535 C C     . THR A 1 4583 ? 166.284 204.831 227.657 1.00 8.87  ? 4583 THR A C     1 
ATOM   22536 O O     . THR A 1 4583 ? 167.094 205.748 227.823 1.00 10.35 ? 4583 THR A O     1 
ATOM   22537 C CB    . THR A 1 4583 ? 165.912 203.982 229.984 1.00 9.57  ? 4583 THR A CB    1 
ATOM   22538 O OG1   . THR A 1 4583 ? 165.805 202.797 230.782 1.00 16.89 ? 4583 THR A OG1   1 
ATOM   22539 C CG2   . THR A 1 4583 ? 164.578 204.710 229.988 1.00 9.01  ? 4583 THR A CG2   1 
ATOM   22540 N N     . ALA A 1 4584 ? 165.360 204.839 226.701 1.00 10.55 ? 4584 ALA A N     1 
ATOM   22541 C CA    . ALA A 1 4584 ? 165.268 205.944 225.758 1.00 11.77 ? 4584 ALA A CA    1 
ATOM   22542 C C     . ALA A 1 4584 ? 164.781 207.209 226.452 1.00 13.06 ? 4584 ALA A C     1 
ATOM   22543 O O     . ALA A 1 4584 ? 163.849 207.177 227.260 1.00 12.23 ? 4584 ALA A O     1 
ATOM   22544 C CB    . ALA A 1 4584 ? 164.328 205.585 224.608 1.00 9.23  ? 4584 ALA A CB    1 
ATOM   22545 N N     . LEU A 1 4585 ? 165.418 208.330 226.128 1.00 12.42 ? 4585 LEU A N     1 
ATOM   22546 C CA    . LEU A 1 4585 ? 164.998 209.630 226.635 1.00 13.15 ? 4585 LEU A CA    1 
ATOM   22547 C C     . LEU A 1 4585 ? 164.315 210.399 225.515 1.00 15.61 ? 4585 LEU A C     1 
ATOM   22548 O O     . LEU A 1 4585 ? 164.998 210.882 224.599 1.00 18.81 ? 4585 LEU A O     1 
ATOM   22549 C CB    . LEU A 1 4585 ? 166.195 210.417 227.172 1.00 12.10 ? 4585 LEU A CB    1 
ATOM   22550 C CG    . LEU A 1 4585 ? 167.038 209.757 228.264 1.00 12.00 ? 4585 LEU A CG    1 
ATOM   22551 C CD1   . LEU A 1 4585 ? 168.030 210.752 228.839 1.00 8.47  ? 4585 LEU A CD1   1 
ATOM   22552 C CD2   . LEU A 1 4585 ? 166.150 209.197 229.358 1.00 9.78  ? 4585 LEU A CD2   1 
ATOM   22553 N N     . PRO A 1 4586 ? 162.994 210.543 225.535 1.00 16.26 ? 4586 PRO A N     1 
ATOM   22554 C CA    . PRO A 1 4586 ? 162.316 211.232 224.432 1.00 20.15 ? 4586 PRO A CA    1 
ATOM   22555 C C     . PRO A 1 4586 ? 162.294 212.741 224.611 1.00 24.04 ? 4586 PRO A C     1 
ATOM   22556 O O     . PRO A 1 4586 ? 161.725 213.248 225.583 1.00 23.56 ? 4586 PRO A O     1 
ATOM   22557 C CB    . PRO A 1 4586 ? 160.904 210.638 224.469 1.00 19.71 ? 4586 PRO A CB    1 
ATOM   22558 C CG    . PRO A 1 4586 ? 160.703 210.204 225.895 1.00 20.67 ? 4586 PRO A CG    1 
ATOM   22559 C CD    . PRO A 1 4586 ? 162.051 210.085 226.568 1.00 18.56 ? 4586 PRO A CD    1 
ATOM   22560 N N     . LEU A 1 4587 ? 162.908 213.465 223.674 1.00 19.45 ? 4587 LEU A N     1 
ATOM   22561 C CA    . LEU A 1 4587 ? 162.923 214.928 223.666 1.00 18.25 ? 4587 LEU A CA    1 
ATOM   22562 C C     . LEU A 1 4587 ? 163.537 215.473 224.960 1.00 16.61 ? 4587 LEU A C     1 
ATOM   22563 O O     . LEU A 1 4587 ? 162.873 216.060 225.817 1.00 18.91 ? 4587 LEU A O     1 
ATOM   22564 C CB    . LEU A 1 4587 ? 161.515 215.489 223.423 1.00 21.48 ? 4587 LEU A CB    1 
ATOM   22565 C CG    . LEU A 1 4587 ? 161.398 217.011 223.325 1.00 23.85 ? 4587 LEU A CG    1 
ATOM   22566 C CD1   . LEU A 1 4587 ? 162.195 217.519 222.140 1.00 20.56 ? 4587 LEU A CD1   1 
ATOM   22567 C CD2   . LEU A 1 4587 ? 159.942 217.431 223.219 1.00 27.25 ? 4587 LEU A CD2   1 
ATOM   22568 N N     . THR A 1 4588 ? 164.834 215.219 225.094 1.00 11.45 ? 4588 THR A N     1 
ATOM   22569 C CA    . THR A 1 4588 ? 165.599 215.808 226.182 1.00 15.38 ? 4588 THR A CA    1 
ATOM   22570 C C     . THR A 1 4588 ? 165.870 217.279 225.888 1.00 16.36 ? 4588 THR A C     1 
ATOM   22571 O O     . THR A 1 4588 ? 166.540 217.612 224.907 1.00 16.64 ? 4588 THR A O     1 
ATOM   22572 C CB    . THR A 1 4588 ? 166.912 215.052 226.371 1.00 14.53 ? 4588 THR A CB    1 
ATOM   22573 O OG1   . THR A 1 4588 ? 166.634 213.692 226.726 1.00 20.16 ? 4588 THR A OG1   1 
ATOM   22574 C CG2   . THR A 1 4588 ? 167.745 215.691 227.458 1.00 8.57  ? 4588 THR A CG2   1 
ATOM   22575 N N     . GLN A 1 4589 ? 165.353 218.160 226.739 1.00 15.32 ? 4589 GLN A N     1 
ATOM   22576 C CA    . GLN A 1 4589 ? 165.477 219.599 226.545 1.00 9.29  ? 4589 GLN A CA    1 
ATOM   22577 C C     . GLN A 1 4589 ? 166.690 220.124 227.298 1.00 15.53 ? 4589 GLN A C     1 
ATOM   22578 O O     . GLN A 1 4589 ? 166.877 219.814 228.479 1.00 20.07 ? 4589 GLN A O     1 
ATOM   22579 C CB    . GLN A 1 4589 ? 164.218 220.329 227.012 1.00 13.11 ? 4589 GLN A CB    1 
ATOM   22580 C CG    . GLN A 1 4589 ? 162.965 219.978 226.238 1.00 14.63 ? 4589 GLN A CG    1 
ATOM   22581 C CD    . GLN A 1 4589 ? 161.772 220.802 226.672 1.00 22.30 ? 4589 GLN A CD    1 
ATOM   22582 O OE1   . GLN A 1 4589 ? 161.903 221.982 226.991 1.00 19.87 ? 4589 GLN A OE1   1 
ATOM   22583 N NE2   . GLN A 1 4589 ? 160.598 220.185 226.678 1.00 23.42 ? 4589 GLN A NE2   1 
ATOM   22584 N N     . LEU A 1 4590 ? 167.508 220.917 226.614 1.00 9.79  ? 4590 LEU A N     1 
ATOM   22585 C CA    . LEU A 1 4590 ? 168.678 221.549 227.207 1.00 2.92  ? 4590 LEU A CA    1 
ATOM   22586 C C     . LEU A 1 4590 ? 168.375 223.023 227.438 1.00 7.95  ? 4590 LEU A C     1 
ATOM   22587 O O     . LEU A 1 4590 ? 168.055 223.749 226.492 1.00 20.31 ? 4590 LEU A O     1 
ATOM   22588 C CB    . LEU A 1 4590 ? 169.903 221.392 226.307 1.00 2.56  ? 4590 LEU A CB    1 
ATOM   22589 C CG    . LEU A 1 4590 ? 170.355 219.979 225.934 1.00 10.52 ? 4590 LEU A CG    1 
ATOM   22590 C CD1   . LEU A 1 4590 ? 171.828 219.986 225.595 1.00 6.03  ? 4590 LEU A CD1   1 
ATOM   22591 C CD2   . LEU A 1 4590 ? 170.085 218.998 227.060 1.00 19.62 ? 4590 LEU A CD2   1 
ATOM   22592 N N     . ARG A 1 4591 ? 168.479 223.461 228.688 1.00 11.41 ? 4591 ARG A N     1 
ATOM   22593 C CA    . ARG A 1 4591 ? 168.222 224.844 229.065 1.00 7.55  ? 4591 ARG A CA    1 
ATOM   22594 C C     . ARG A 1 4591 ? 169.496 225.463 229.617 1.00 7.62  ? 4591 ARG A C     1 
ATOM   22595 O O     . ARG A 1 4591 ? 170.212 224.828 230.396 1.00 18.28 ? 4591 ARG A O     1 
ATOM   22596 C CB    . ARG A 1 4591 ? 167.111 224.935 230.111 1.00 11.01 ? 4591 ARG A CB    1 
ATOM   22597 C CG    . ARG A 1 4591 ? 165.824 224.241 229.728 1.00 14.36 ? 4591 ARG A CG    1 
ATOM   22598 C CD    . ARG A 1 4591 ? 164.683 224.747 230.588 1.00 14.46 ? 4591 ARG A CD    1 
ATOM   22599 N NE    . ARG A 1 4591 ? 164.574 226.199 230.526 1.00 11.43 ? 4591 ARG A NE    1 
ATOM   22600 C CZ    . ARG A 1 4591 ? 164.279 226.972 231.562 1.00 17.92 ? 4591 ARG A CZ    1 
ATOM   22601 N NH1   . ARG A 1 4591 ? 164.064 226.464 232.764 1.00 14.86 ? 4591 ARG A NH1   1 
ATOM   22602 N NH2   . ARG A 1 4591 ? 164.200 228.289 231.387 1.00 19.19 ? 4591 ARG A NH2   1 
ATOM   22603 N N     . TRP A 1 4592 ? 169.773 226.697 229.217 1.00 5.03  ? 4592 TRP A N     1 
ATOM   22604 C CA    . TRP A 1 4592 ? 170.881 227.464 229.765 1.00 5.96  ? 4592 TRP A CA    1 
ATOM   22605 C C     . TRP A 1 4592 ? 170.306 228.558 230.653 1.00 10.21 ? 4592 TRP A C     1 
ATOM   22606 O O     . TRP A 1 4592 ? 169.461 229.342 230.209 1.00 15.01 ? 4592 TRP A O     1 
ATOM   22607 C CB    . TRP A 1 4592 ? 171.740 228.053 228.649 1.00 6.43  ? 4592 TRP A CB    1 
ATOM   22608 C CG    . TRP A 1 4592 ? 172.487 227.009 227.891 1.00 3.49  ? 4592 TRP A CG    1 
ATOM   22609 C CD1   . TRP A 1 4592 ? 172.145 226.473 226.688 1.00 8.24  ? 4592 TRP A CD1   1 
ATOM   22610 C CD2   . TRP A 1 4592 ? 173.700 226.363 228.288 1.00 2.19  ? 4592 TRP A CD2   1 
ATOM   22611 N NE1   . TRP A 1 4592 ? 173.070 225.534 226.309 1.00 9.66  ? 4592 TRP A NE1   1 
ATOM   22612 C CE2   . TRP A 1 4592 ? 174.036 225.449 227.275 1.00 5.58  ? 4592 TRP A CE2   1 
ATOM   22613 C CE3   . TRP A 1 4592 ? 174.535 226.470 229.403 1.00 6.49  ? 4592 TRP A CE3   1 
ATOM   22614 C CZ2   . TRP A 1 4592 ? 175.171 224.647 227.340 1.00 6.91  ? 4592 TRP A CZ2   1 
ATOM   22615 C CZ3   . TRP A 1 4592 ? 175.659 225.674 229.466 1.00 5.41  ? 4592 TRP A CZ3   1 
ATOM   22616 C CH2   . TRP A 1 4592 ? 175.967 224.774 228.442 1.00 5.09  ? 4592 TRP A CH2   1 
ATOM   22617 N N     . VAL A 1 4593 ? 170.752 228.601 231.905 1.00 6.33  ? 4593 VAL A N     1 
ATOM   22618 C CA    . VAL A 1 4593 ? 170.203 229.519 232.891 1.00 13.63 ? 4593 VAL A CA    1 
ATOM   22619 C C     . VAL A 1 4593 ? 171.342 230.226 233.607 1.00 14.59 ? 4593 VAL A C     1 
ATOM   22620 O O     . VAL A 1 4593 ? 172.478 229.743 233.641 1.00 12.89 ? 4593 VAL A O     1 
ATOM   22621 C CB    . VAL A 1 4593 ? 169.291 228.795 233.905 1.00 15.29 ? 4593 VAL A CB    1 
ATOM   22622 C CG1   . VAL A 1 4593 ? 167.968 228.422 233.258 1.00 11.60 ? 4593 VAL A CG1   1 
ATOM   22623 C CG2   . VAL A 1 4593 ? 169.985 227.563 234.453 1.00 11.15 ? 4593 VAL A CG2   1 
ATOM   22624 N N     . LYS A 1 4594 ? 171.028 231.386 234.177 1.00 14.89 ? 4594 LYS A N     1 
ATOM   22625 C CA    . LYS A 1 4594 ? 171.997 232.156 234.949 1.00 13.35 ? 4594 LYS A CA    1 
ATOM   22626 C C     . LYS A 1 4594 ? 172.338 231.397 236.225 1.00 16.98 ? 4594 LYS A C     1 
ATOM   22627 O O     . LYS A 1 4594 ? 171.505 231.287 237.131 1.00 22.46 ? 4594 LYS A O     1 
ATOM   22628 C CB    . LYS A 1 4594 ? 171.428 233.534 235.271 1.00 18.83 ? 4594 LYS A CB    1 
ATOM   22629 C CG    . LYS A 1 4594 ? 172.453 234.654 235.301 1.00 20.00 ? 4594 LYS A CG    1 
ATOM   22630 C CD    . LYS A 1 4594 ? 172.928 235.009 233.904 1.00 19.08 ? 4594 LYS A CD    1 
ATOM   22631 C CE    . LYS A 1 4594 ? 174.132 235.932 233.955 1.00 17.99 ? 4594 LYS A CE    1 
ATOM   22632 N NZ    . LYS A 1 4594 ? 173.846 237.178 234.718 1.00 19.59 ? 4594 LYS A NZ    1 
ATOM   22633 N N     . GLN A 1 4595 ? 173.556 230.867 236.301 1.00 16.63 ? 4595 GLN A N     1 
ATOM   22634 C CA    . GLN A 1 4595 ? 173.966 230.123 237.483 1.00 24.89 ? 4595 GLN A CA    1 
ATOM   22635 C C     . GLN A 1 4595 ? 174.113 231.056 238.679 1.00 28.49 ? 4595 GLN A C     1 
ATOM   22636 O O     . GLN A 1 4595 ? 174.596 232.184 238.555 1.00 28.16 ? 4595 GLN A O     1 
ATOM   22637 C CB    . GLN A 1 4595 ? 175.274 229.376 237.220 1.00 23.14 ? 4595 GLN A CB    1 
ATOM   22638 C CG    . GLN A 1 4595 ? 176.486 230.261 237.010 1.00 25.04 ? 4595 GLN A CG    1 
ATOM   22639 C CD    . GLN A 1 4595 ? 177.786 229.495 237.137 1.00 28.04 ? 4595 GLN A CD    1 
ATOM   22640 O OE1   . GLN A 1 4595 ? 177.908 228.590 237.963 1.00 27.65 ? 4595 GLN A OE1   1 
ATOM   22641 N NE2   . GLN A 1 4595 ? 178.765 229.850 236.315 1.00 25.06 ? 4595 GLN A NE2   1 
ATOM   22642 N N     . THR A 1 4596 ? 173.672 230.582 239.841 1.00 32.32 ? 4596 THR A N     1 
ATOM   22643 C CA    . THR A 1 4596 ? 173.698 231.369 241.066 1.00 35.35 ? 4596 THR A CA    1 
ATOM   22644 C C     . THR A 1 4596 ? 174.922 231.090 241.929 1.00 37.45 ? 4596 THR A C     1 
ATOM   22645 O O     . THR A 1 4596 ? 175.014 231.634 243.035 1.00 34.69 ? 4596 THR A O     1 
ATOM   22646 C CB    . THR A 1 4596 ? 172.427 231.116 241.882 1.00 39.18 ? 4596 THR A CB    1 
ATOM   22647 O OG1   . THR A 1 4596 ? 172.360 229.732 242.247 1.00 36.53 ? 4596 THR A OG1   1 
ATOM   22648 C CG2   . THR A 1 4596 ? 171.195 231.478 241.068 1.00 36.27 ? 4596 THR A CG2   1 
ATOM   22649 N N     . ASN A 1 4597 ? 175.854 230.261 241.453 1.00 38.36 ? 4597 ASN A N     1 
ATOM   22650 C CA    . ASN A 1 4597 ? 177.090 229.953 242.174 1.00 39.06 ? 4597 ASN A CA    1 
ATOM   22651 C C     . ASN A 1 4597 ? 176.804 229.392 243.566 1.00 37.38 ? 4597 ASN A C     1 
ATOM   22652 O O     . ASN A 1 4597 ? 177.466 229.741 244.546 1.00 36.98 ? 4597 ASN A O     1 
ATOM   22653 C CB    . ASN A 1 4597 ? 178.001 231.181 242.259 1.00 38.00 ? 4597 ASN A CB    1 
ATOM   22654 C CG    . ASN A 1 4597 ? 178.424 231.688 240.895 1.00 38.97 ? 4597 ASN A CG    1 
ATOM   22655 O OD1   . ASN A 1 4597 ? 179.233 231.061 240.211 1.00 39.75 ? 4597 ASN A OD1   1 
ATOM   22656 N ND2   . ASN A 1 4597 ? 177.874 232.827 240.490 1.00 38.01 ? 4597 ASN A ND2   1 
ATOM   22657 N N     . THR A 1 4598 ? 175.808 228.517 243.655 1.00 38.84 ? 4598 THR A N     1 
ATOM   22658 C CA    . THR A 1 4598 ? 175.455 227.848 244.896 1.00 41.26 ? 4598 THR A CA    1 
ATOM   22659 C C     . THR A 1 4598 ? 175.894 226.391 244.840 1.00 40.91 ? 4598 THR A C     1 
ATOM   22660 O O     . THR A 1 4598 ? 176.082 225.822 243.760 1.00 39.24 ? 4598 THR A O     1 
ATOM   22661 C CB    . THR A 1 4598 ? 173.948 227.931 245.167 1.00 41.29 ? 4598 THR A CB    1 
ATOM   22662 O OG1   . THR A 1 4598 ? 173.661 227.387 246.461 1.00 38.59 ? 4598 THR A OG1   1 
ATOM   22663 C CG2   . THR A 1 4598 ? 173.170 227.157 244.113 1.00 40.99 ? 4598 THR A CG2   1 
ATOM   22664 N N     . GLU A 1 4599 ? 176.070 225.794 246.015 1.00 41.32 ? 4599 GLU A N     1 
ATOM   22665 C CA    . GLU A 1 4599 ? 176.496 224.404 246.087 1.00 42.18 ? 4599 GLU A CA    1 
ATOM   22666 C C     . GLU A 1 4599 ? 175.354 223.473 245.698 1.00 41.57 ? 4599 GLU A C     1 
ATOM   22667 O O     . GLU A 1 4599 ? 174.208 223.656 246.119 1.00 40.21 ? 4599 GLU A O     1 
ATOM   22668 C CB    . GLU A 1 4599 ? 176.991 224.072 247.494 1.00 41.16 ? 4599 GLU A CB    1 
ATOM   22669 C CG    . GLU A 1 4599 ? 177.508 222.651 247.652 1.00 41.53 ? 4599 GLU A CG    1 
ATOM   22670 C CD    . GLU A 1 4599 ? 178.536 222.286 246.598 1.00 42.41 ? 4599 GLU A CD    1 
ATOM   22671 O OE1   . GLU A 1 4599 ? 179.513 223.044 246.430 1.00 41.52 ? 4599 GLU A OE1   1 
ATOM   22672 O OE2   . GLU A 1 4599 ? 178.366 221.240 245.937 1.00 42.24 ? 4599 GLU A OE2   1 
ATOM   22673 N N     . LYS A 1 4600 ? 175.674 222.471 244.884 1.00 38.61 ? 4600 LYS A N     1 
ATOM   22674 C CA    . LYS A 1 4600 ? 174.682 221.489 244.474 1.00 39.47 ? 4600 LYS A CA    1 
ATOM   22675 C C     . LYS A 1 4600 ? 174.275 220.612 245.654 1.00 37.50 ? 4600 LYS A C     1 
ATOM   22676 O O     . LYS A 1 4600 ? 175.077 220.309 246.541 1.00 33.79 ? 4600 LYS A O     1 
ATOM   22677 C CB    . LYS A 1 4600 ? 175.228 220.631 243.331 1.00 33.62 ? 4600 LYS A CB    1 
ATOM   22678 C CG    . LYS A 1 4600 ? 176.459 219.815 243.693 1.00 31.77 ? 4600 LYS A CG    1 
ATOM   22679 C CD    . LYS A 1 4600 ? 177.088 219.178 242.462 1.00 35.91 ? 4600 LYS A CD    1 
ATOM   22680 C CE    . LYS A 1 4600 ? 176.222 218.067 241.896 1.00 37.36 ? 4600 LYS A CE    1 
ATOM   22681 N NZ    . LYS A 1 4600 ? 176.116 216.917 242.836 1.00 39.86 ? 4600 LYS A NZ    1 
ATOM   22682 N N     . LYS A 1 4601 ? 173.006 220.211 245.660 1.00 32.84 ? 4601 LYS A N     1 
ATOM   22683 C CA    . LYS A 1 4601 ? 172.473 219.418 246.755 1.00 29.16 ? 4601 LYS A CA    1 
ATOM   22684 C C     . LYS A 1 4601 ? 173.000 217.985 246.680 1.00 27.57 ? 4601 LYS A C     1 
ATOM   22685 O O     . LYS A 1 4601 ? 173.638 217.572 245.708 1.00 29.04 ? 4601 LYS A O     1 
ATOM   22686 C CB    . LYS A 1 4601 ? 170.947 219.445 246.734 1.00 30.11 ? 4601 LYS A CB    1 
ATOM   22687 C CG    . LYS A 1 4601 ? 170.341 219.353 245.347 1.00 28.12 ? 4601 LYS A CG    1 
ATOM   22688 C CD    . LYS A 1 4601 ? 168.854 219.656 245.379 1.00 28.35 ? 4601 LYS A CD    1 
ATOM   22689 C CE    . LYS A 1 4601 ? 168.144 218.821 246.433 1.00 31.03 ? 4601 LYS A CE    1 
ATOM   22690 N NZ    . LYS A 1 4601 ? 166.663 218.906 246.307 1.00 29.45 ? 4601 LYS A NZ    1 
ATOM   22691 N N     . ALA A 1 4602 ? 172.730 217.219 247.733 1.00 22.86 ? 4602 ALA A N     1 
ATOM   22692 C CA    . ALA A 1 4602 ? 173.163 215.832 247.822 1.00 23.09 ? 4602 ALA A CA    1 
ATOM   22693 C C     . ALA A 1 4602 ? 172.195 214.866 247.155 1.00 28.28 ? 4602 ALA A C     1 
ATOM   22694 O O     . ALA A 1 4602 ? 172.459 213.659 247.140 1.00 23.78 ? 4602 ALA A O     1 
ATOM   22695 C CB    . ALA A 1 4602 ? 173.359 215.433 249.288 1.00 24.37 ? 4602 ALA A CB    1 
ATOM   22696 N N     . SER A 1 4603 ? 171.087 215.364 246.607 1.00 28.43 ? 4603 SER A N     1 
ATOM   22697 C CA    . SER A 1 4603 ? 170.090 214.533 245.949 1.00 20.79 ? 4603 SER A CA    1 
ATOM   22698 C C     . SER A 1 4603 ? 170.213 214.568 244.431 1.00 16.53 ? 4603 SER A C     1 
ATOM   22699 O O     . SER A 1 4603 ? 169.291 214.141 243.731 1.00 19.04 ? 4603 SER A O     1 
ATOM   22700 C CB    . SER A 1 4603 ? 168.685 214.962 246.372 1.00 20.52 ? 4603 SER A CB    1 
ATOM   22701 O OG    . SER A 1 4603 ? 167.699 214.183 245.718 1.00 22.20 ? 4603 SER A OG    1 
ATOM   22702 N N     . VAL A 1 4604 ? 171.328 215.077 243.906 1.00 17.30 ? 4604 VAL A N     1 
ATOM   22703 C CA    . VAL A 1 4604 ? 171.555 215.133 242.470 1.00 15.44 ? 4604 VAL A CA    1 
ATOM   22704 C C     . VAL A 1 4604 ? 172.839 214.386 242.142 1.00 12.15 ? 4604 VAL A C     1 
ATOM   22705 O O     . VAL A 1 4604 ? 173.754 214.277 242.962 1.00 17.12 ? 4604 VAL A O     1 
ATOM   22706 C CB    . VAL A 1 4604 ? 171.625 216.580 241.935 1.00 12.71 ? 4604 VAL A CB    1 
ATOM   22707 C CG1   . VAL A 1 4604 ? 170.309 217.299 242.171 1.00 15.45 ? 4604 VAL A CG1   1 
ATOM   22708 C CG2   . VAL A 1 4604 ? 172.766 217.331 242.584 1.00 17.08 ? 4604 VAL A CG2   1 
ATOM   22709 N N     . VAL A 1 4605 ? 172.895 213.865 240.917 1.00 7.74  ? 4605 VAL A N     1 
ATOM   22710 C CA    . VAL A 1 4605 ? 174.048 213.127 240.426 1.00 3.88  ? 4605 VAL A CA    1 
ATOM   22711 C C     . VAL A 1 4605 ? 174.500 213.745 239.112 1.00 5.49  ? 4605 VAL A C     1 
ATOM   22712 O O     . VAL A 1 4605 ? 173.701 214.278 238.339 1.00 11.73 ? 4605 VAL A O     1 
ATOM   22713 C CB    . VAL A 1 4605 ? 173.744 211.624 240.235 1.00 5.90  ? 4605 VAL A CB    1 
ATOM   22714 C CG1   . VAL A 1 4605 ? 173.476 210.965 241.571 1.00 12.57 ? 4605 VAL A CG1   1 
ATOM   22715 C CG2   . VAL A 1 4605 ? 172.559 211.436 239.301 1.00 3.10  ? 4605 VAL A CG2   1 
ATOM   22716 N N     . THR A 1 4606 ? 175.800 213.666 238.864 1.00 1.51  ? 4606 THR A N     1 
ATOM   22717 C CA    . THR A 1 4606 ? 176.403 214.151 237.628 1.00 0.00  ? 4606 THR A CA    1 
ATOM   22718 C C     . THR A 1 4606 ? 176.723 212.937 236.766 1.00 4.21  ? 4606 THR A C     1 
ATOM   22719 O O     . THR A 1 4606 ? 177.630 212.162 237.079 1.00 9.43  ? 4606 THR A O     1 
ATOM   22720 C CB    . THR A 1 4606 ? 177.651 214.980 237.912 1.00 0.50  ? 4606 THR A CB    1 
ATOM   22721 O OG1   . THR A 1 4606 ? 177.357 215.958 238.916 1.00 7.29  ? 4606 THR A OG1   1 
ATOM   22722 C CG2   . THR A 1 4606 ? 178.122 215.680 236.652 1.00 4.36  ? 4606 THR A CG2   1 
ATOM   22723 N N     . LEU A 1 4607 ? 175.970 212.769 235.693 1.00 0.91  ? 4607 LEU A N     1 
ATOM   22724 C CA    . LEU A 1 4607 ? 176.159 211.641 234.790 1.00 1.32  ? 4607 LEU A CA    1 
ATOM   22725 C C     . LEU A 1 4607 ? 176.994 212.064 233.591 1.00 2.95  ? 4607 LEU A C     1 
ATOM   22726 O O     . LEU A 1 4607 ? 176.716 213.109 232.991 1.00 6.95  ? 4607 LEU A O     1 
ATOM   22727 C CB    . LEU A 1 4607 ? 174.822 211.100 234.307 1.00 0.50  ? 4607 LEU A CB    1 
ATOM   22728 C CG    . LEU A 1 4607 ? 173.818 210.648 235.363 1.00 0.00  ? 4607 LEU A CG    1 
ATOM   22729 C CD1   . LEU A 1 4607 ? 172.745 209.808 234.713 1.00 0.43  ? 4607 LEU A CD1   1 
ATOM   22730 C CD2   . LEU A 1 4607 ? 174.515 209.863 236.459 1.00 1.18  ? 4607 LEU A CD2   1 
ATOM   22731 N N     . PRO A 1 4608 ? 178.015 211.300 233.218 1.00 1.74  ? 4608 PRO A N     1 
ATOM   22732 C CA    . PRO A 1 4608 ? 178.722 211.591 231.970 1.00 0.31  ? 4608 PRO A CA    1 
ATOM   22733 C C     . PRO A 1 4608 ? 177.839 211.296 230.772 1.00 3.90  ? 4608 PRO A C     1 
ATOM   22734 O O     . PRO A 1 4608 ? 176.996 210.397 230.796 1.00 11.64 ? 4608 PRO A O     1 
ATOM   22735 C CB    . PRO A 1 4608 ? 179.931 210.653 232.018 1.00 0.00  ? 4608 PRO A CB    1 
ATOM   22736 C CG    . PRO A 1 4608 ? 179.513 209.534 232.889 1.00 0.00  ? 4608 PRO A CG    1 
ATOM   22737 C CD    . PRO A 1 4608 ? 178.444 210.028 233.822 1.00 0.32  ? 4608 PRO A CD    1 
ATOM   22738 N N     . VAL A 1 4609 ? 178.037 212.068 229.715 1.00 3.46  ? 4609 VAL A N     1 
ATOM   22739 C CA    . VAL A 1 4609 ? 177.288 211.905 228.474 1.00 2.17  ? 4609 VAL A CA    1 
ATOM   22740 C C     . VAL A 1 4609 ? 178.298 211.496 227.410 1.00 2.43  ? 4609 VAL A C     1 
ATOM   22741 O O     . VAL A 1 4609 ? 179.081 212.312 226.915 1.00 8.52  ? 4609 VAL A O     1 
ATOM   22742 C CB    . VAL A 1 4609 ? 176.525 213.169 228.075 1.00 0.18  ? 4609 VAL A CB    1 
ATOM   22743 C CG1   . VAL A 1 4609 ? 175.799 212.952 226.761 1.00 0.00  ? 4609 VAL A CG1   1 
ATOM   22744 C CG2   . VAL A 1 4609 ? 175.545 213.554 229.165 1.00 1.24  ? 4609 VAL A CG2   1 
ATOM   22745 N N     . TYR A 1 4610 ? 178.295 210.215 227.061 1.00 0.00  ? 4610 TYR A N     1 
ATOM   22746 C CA    . TYR A 1 4610 ? 179.172 209.717 226.018 1.00 2.93  ? 4610 TYR A CA    1 
ATOM   22747 C C     . TYR A 1 4610 ? 178.422 209.672 224.691 1.00 6.94  ? 4610 TYR A C     1 
ATOM   22748 O O     . TYR A 1 4610 ? 177.189 209.683 224.645 1.00 6.44  ? 4610 TYR A O     1 
ATOM   22749 C CB    . TYR A 1 4610 ? 179.697 208.328 226.376 1.00 3.78  ? 4610 TYR A CB    1 
ATOM   22750 C CG    . TYR A 1 4610 ? 180.485 208.277 227.663 1.00 0.00  ? 4610 TYR A CG    1 
ATOM   22751 C CD1   . TYR A 1 4610 ? 181.830 208.606 227.692 1.00 2.25  ? 4610 TYR A CD1   1 
ATOM   22752 C CD2   . TYR A 1 4610 ? 179.885 207.879 228.848 1.00 1.96  ? 4610 TYR A CD2   1 
ATOM   22753 C CE1   . TYR A 1 4610 ? 182.553 208.550 228.865 1.00 0.24  ? 4610 TYR A CE1   1 
ATOM   22754 C CE2   . TYR A 1 4610 ? 180.599 207.822 230.025 1.00 2.41  ? 4610 TYR A CE2   1 
ATOM   22755 C CZ    . TYR A 1 4610 ? 181.932 208.161 230.028 1.00 0.00  ? 4610 TYR A CZ    1 
ATOM   22756 O OH    . TYR A 1 4610 ? 182.650 208.103 231.199 1.00 0.00  ? 4610 TYR A OH    1 
ATOM   22757 N N     . LEU A 1 4611 ? 179.182 209.617 223.600 1.00 4.81  ? 4611 LEU A N     1 
ATOM   22758 C CA    . LEU A 1 4611 ? 178.590 209.595 222.268 1.00 7.91  ? 4611 LEU A CA    1 
ATOM   22759 C C     . LEU A 1 4611 ? 178.371 208.180 221.746 1.00 9.11  ? 4611 LEU A C     1 
ATOM   22760 O O     . LEU A 1 4611 ? 177.382 207.928 221.053 1.00 13.47 ? 4611 LEU A O     1 
ATOM   22761 C CB    . LEU A 1 4611 ? 179.453 210.396 221.282 1.00 9.03  ? 4611 LEU A CB    1 
ATOM   22762 C CG    . LEU A 1 4611 ? 180.790 209.840 220.787 1.00 11.89 ? 4611 LEU A CG    1 
ATOM   22763 C CD1   . LEU A 1 4611 ? 181.252 210.616 219.567 1.00 1.81  ? 4611 LEU A CD1   1 
ATOM   22764 C CD2   . LEU A 1 4611 ? 181.844 209.883 221.872 1.00 10.51 ? 4611 LEU A CD2   1 
ATOM   22765 N N     . ASN A 1 4612 ? 179.266 207.251 222.064 1.00 4.62  ? 4612 ASN A N     1 
ATOM   22766 C CA    . ASN A 1 4612 ? 179.153 205.874 221.608 1.00 4.07  ? 4612 ASN A CA    1 
ATOM   22767 C C     . ASN A 1 4612 ? 178.772 204.952 222.760 1.00 6.65  ? 4612 ASN A C     1 
ATOM   22768 O O     . ASN A 1 4612 ? 178.754 205.343 223.929 1.00 12.36 ? 4612 ASN A O     1 
ATOM   22769 C CB    . ASN A 1 4612 ? 180.464 205.395 220.974 1.00 4.72  ? 4612 ASN A CB    1 
ATOM   22770 C CG    . ASN A 1 4612 ? 181.042 206.394 219.999 1.00 10.89 ? 4612 ASN A CG    1 
ATOM   22771 O OD1   . ASN A 1 4612 ? 182.204 206.781 220.106 1.00 6.75  ? 4612 ASN A OD1   1 
ATOM   22772 N ND2   . ASN A 1 4612 ? 180.233 206.816 219.037 1.00 13.05 ? 4612 ASN A ND2   1 
ATOM   22773 N N     . PHE A 1 4613 ? 178.460 203.703 222.405 1.00 11.14 ? 4613 PHE A N     1 
ATOM   22774 C CA    . PHE A 1 4613 ? 178.283 202.669 223.419 1.00 7.61  ? 4613 PHE A CA    1 
ATOM   22775 C C     . PHE A 1 4613 ? 179.561 202.465 224.219 1.00 3.57  ? 4613 PHE A C     1 
ATOM   22776 O O     . PHE A 1 4613 ? 179.505 202.179 225.419 1.00 8.58  ? 4613 PHE A O     1 
ATOM   22777 C CB    . PHE A 1 4613 ? 177.826 201.363 222.764 1.00 6.86  ? 4613 PHE A CB    1 
ATOM   22778 C CG    . PHE A 1 4613 ? 178.836 200.765 221.823 1.00 7.59  ? 4613 PHE A CG    1 
ATOM   22779 C CD1   . PHE A 1 4613 ? 179.827 199.915 222.286 1.00 6.33  ? 4613 PHE A CD1   1 
ATOM   22780 C CD2   . PHE A 1 4613 ? 178.797 201.063 220.473 1.00 9.37  ? 4613 PHE A CD2   1 
ATOM   22781 C CE1   . PHE A 1 4613 ? 180.755 199.375 221.422 1.00 9.56  ? 4613 PHE A CE1   1 
ATOM   22782 C CE2   . PHE A 1 4613 ? 179.723 200.524 219.606 1.00 11.67 ? 4613 PHE A CE2   1 
ATOM   22783 C CZ    . PHE A 1 4613 ? 180.703 199.679 220.081 1.00 11.19 ? 4613 PHE A CZ    1 
ATOM   22784 N N     . THR A 1 4614 ? 180.715 202.600 223.574 1.00 4.36  ? 4614 THR A N     1 
ATOM   22785 C CA    . THR A 1 4614 ? 181.974 202.659 224.295 1.00 4.05  ? 4614 THR A CA    1 
ATOM   22786 C C     . THR A 1 4614 ? 182.130 204.038 224.917 1.00 5.29  ? 4614 THR A C     1 
ATOM   22787 O O     . THR A 1 4614 ? 181.777 205.054 224.313 1.00 13.38 ? 4614 THR A O     1 
ATOM   22788 C CB    . THR A 1 4614 ? 183.152 202.347 223.369 1.00 10.26 ? 4614 THR A CB    1 
ATOM   22789 O OG1   . THR A 1 4614 ? 184.376 202.415 224.111 1.00 18.88 ? 4614 THR A OG1   1 
ATOM   22790 C CG2   . THR A 1 4614 ? 183.211 203.317 222.203 1.00 4.64  ? 4614 THR A CG2   1 
ATOM   22791 N N     . ARG A 1 4615 ? 182.633 204.069 226.143 1.00 1.74  ? 4615 ARG A N     1 
ATOM   22792 C CA    . ARG A 1 4615 ? 182.727 205.308 226.906 1.00 0.52  ? 4615 ARG A CA    1 
ATOM   22793 C C     . ARG A 1 4615 ? 184.161 205.816 226.811 1.00 7.16  ? 4615 ARG A C     1 
ATOM   22794 O O     . ARG A 1 4615 ? 184.970 205.630 227.719 1.00 15.01 ? 4615 ARG A O     1 
ATOM   22795 C CB    . ARG A 1 4615 ? 182.281 205.082 228.344 1.00 1.00  ? 4615 ARG A CB    1 
ATOM   22796 C CG    . ARG A 1 4615 ? 180.941 204.373 228.442 1.00 0.00  ? 4615 ARG A CG    1 
ATOM   22797 C CD    . ARG A 1 4615 ? 180.455 204.308 229.871 1.00 1.93  ? 4615 ARG A CD    1 
ATOM   22798 N NE    . ARG A 1 4615 ? 179.180 203.613 229.986 1.00 0.00  ? 4615 ARG A NE    1 
ATOM   22799 C CZ    . ARG A 1 4615 ? 178.592 203.322 231.137 1.00 2.13  ? 4615 ARG A CZ    1 
ATOM   22800 N NH1   . ARG A 1 4615 ? 179.129 203.670 232.293 1.00 2.33  ? 4615 ARG A NH1   1 
ATOM   22801 N NH2   . ARG A 1 4615 ? 177.429 202.678 231.126 1.00 5.64  ? 4615 ARG A NH2   1 
ATOM   22802 N N     . ALA A 1 4616 ? 184.469 206.475 225.695 1.00 6.70  ? 4616 ALA A N     1 
ATOM   22803 C CA    . ALA A 1 4616 ? 185.818 206.956 225.429 1.00 4.54  ? 4616 ALA A CA    1 
ATOM   22804 C C     . ALA A 1 4616 ? 185.928 208.463 225.264 1.00 4.81  ? 4616 ALA A C     1 
ATOM   22805 O O     . ALA A 1 4616 ? 187.022 209.000 225.475 1.00 5.67  ? 4616 ALA A O     1 
ATOM   22806 C CB    . ALA A 1 4616 ? 186.390 206.283 224.173 1.00 0.00  ? 4616 ALA A CB    1 
ATOM   22807 N N     . ASP A 1 4617 ? 184.857 209.162 224.895 1.00 7.52  ? 4617 ASP A N     1 
ATOM   22808 C CA    . ASP A 1 4617 ? 184.888 210.610 224.736 1.00 6.68  ? 4617 ASP A CA    1 
ATOM   22809 C C     . ASP A 1 4617 ? 183.682 211.225 225.430 1.00 4.76  ? 4617 ASP A C     1 
ATOM   22810 O O     . ASP A 1 4617 ? 182.548 210.784 225.219 1.00 3.50  ? 4617 ASP A O     1 
ATOM   22811 C CB    . ASP A 1 4617 ? 184.905 211.009 223.257 1.00 7.86  ? 4617 ASP A CB    1 
ATOM   22812 C CG    . ASP A 1 4617 ? 186.072 210.406 222.501 1.00 8.54  ? 4617 ASP A CG    1 
ATOM   22813 O OD1   . ASP A 1 4617 ? 185.844 209.485 221.690 1.00 5.40  ? 4617 ASP A OD1   1 
ATOM   22814 O OD2   . ASP A 1 4617 ? 187.217 210.856 222.714 1.00 10.81 ? 4617 ASP A OD2   1 
ATOM   22815 N N     . LEU A 1 4618 ? 183.930 212.248 226.244 1.00 2.31  ? 4618 LEU A N     1 
ATOM   22816 C CA    . LEU A 1 4618 ? 182.882 212.989 226.932 1.00 1.91  ? 4618 LEU A CA    1 
ATOM   22817 C C     . LEU A 1 4618 ? 182.389 214.129 226.054 1.00 5.37  ? 4618 LEU A C     1 
ATOM   22818 O O     . LEU A 1 4618 ? 183.192 214.895 225.511 1.00 14.28 ? 4618 LEU A O     1 
ATOM   22819 C CB    . LEU A 1 4618 ? 183.387 213.547 228.263 1.00 2.80  ? 4618 LEU A CB    1 
ATOM   22820 C CG    . LEU A 1 4618 ? 183.738 212.564 229.373 1.00 5.99  ? 4618 LEU A CG    1 
ATOM   22821 C CD1   . LEU A 1 4618 ? 184.363 213.294 230.545 1.00 6.28  ? 4618 LEU A CD1   1 
ATOM   22822 C CD2   . LEU A 1 4618 ? 182.475 211.866 229.814 1.00 10.06 ? 4618 LEU A CD2   1 
ATOM   22823 N N     . ILE A 1 4619 ? 181.070 214.241 225.920 1.00 0.00  ? 4619 ILE A N     1 
ATOM   22824 C CA    . ILE A 1 4619 ? 180.467 215.390 225.257 1.00 6.25  ? 4619 ILE A CA    1 
ATOM   22825 C C     . ILE A 1 4619 ? 180.257 216.482 226.296 1.00 9.65  ? 4619 ILE A C     1 
ATOM   22826 O O     . ILE A 1 4619 ? 180.821 217.576 226.189 1.00 5.06  ? 4619 ILE A O     1 
ATOM   22827 C CB    . ILE A 1 4619 ? 179.148 215.013 224.561 1.00 0.40  ? 4619 ILE A CB    1 
ATOM   22828 C CG1   . ILE A 1 4619 ? 179.366 213.836 223.613 1.00 4.25  ? 4619 ILE A CG1   1 
ATOM   22829 C CG2   . ILE A 1 4619 ? 178.593 216.198 223.796 1.00 0.32  ? 4619 ILE A CG2   1 
ATOM   22830 C CD1   . ILE A 1 4619 ? 180.451 214.077 222.587 1.00 2.94  ? 4619 ILE A CD1   1 
ATOM   22831 N N     . PHE A 1 4620 ? 179.454 216.186 227.312 1.00 6.48  ? 4620 PHE A N     1 
ATOM   22832 C CA    . PHE A 1 4620 ? 179.209 217.109 228.412 1.00 1.80  ? 4620 PHE A CA    1 
ATOM   22833 C C     . PHE A 1 4620 ? 178.752 216.286 229.612 1.00 0.27  ? 4620 PHE A C     1 
ATOM   22834 O O     . PHE A 1 4620 ? 178.726 215.053 229.562 1.00 8.97  ? 4620 PHE A O     1 
ATOM   22835 C CB    . PHE A 1 4620 ? 178.193 218.187 228.012 1.00 3.27  ? 4620 PHE A CB    1 
ATOM   22836 C CG    . PHE A 1 4620 ? 176.822 217.655 227.692 1.00 2.43  ? 4620 PHE A CG    1 
ATOM   22837 C CD1   . PHE A 1 4620 ? 176.535 217.149 226.438 1.00 0.63  ? 4620 PHE A CD1   1 
ATOM   22838 C CD2   . PHE A 1 4620 ? 175.810 217.703 228.634 1.00 3.30  ? 4620 PHE A CD2   1 
ATOM   22839 C CE1   . PHE A 1 4620 ? 175.274 216.669 226.140 1.00 1.00  ? 4620 PHE A CE1   1 
ATOM   22840 C CE2   . PHE A 1 4620 ? 174.546 217.228 228.339 1.00 3.67  ? 4620 PHE A CE2   1 
ATOM   22841 C CZ    . PHE A 1 4620 ? 174.279 216.710 227.091 1.00 0.00  ? 4620 PHE A CZ    1 
ATOM   22842 N N     . THR A 1 4621 ? 178.404 216.968 230.697 1.00 0.89  ? 4621 THR A N     1 
ATOM   22843 C CA    . THR A 1 4621 ? 177.918 216.324 231.907 1.00 2.18  ? 4621 THR A CA    1 
ATOM   22844 C C     . THR A 1 4621 ? 176.546 216.880 232.253 1.00 2.60  ? 4621 THR A C     1 
ATOM   22845 O O     . THR A 1 4621 ? 176.306 218.085 232.136 1.00 3.27  ? 4621 THR A O     1 
ATOM   22846 C CB    . THR A 1 4621 ? 178.881 216.532 233.081 1.00 7.87  ? 4621 THR A CB    1 
ATOM   22847 O OG1   . THR A 1 4621 ? 179.001 217.931 233.365 1.00 10.49 ? 4621 THR A OG1   1 
ATOM   22848 C CG2   . THR A 1 4621 ? 180.253 215.966 232.752 1.00 2.39  ? 4621 THR A CG2   1 
ATOM   22849 N N     . VAL A 1 4622 ? 175.647 215.998 232.676 1.00 2.55  ? 4622 VAL A N     1 
ATOM   22850 C CA    . VAL A 1 4622 ? 174.269 216.358 232.975 1.00 3.67  ? 4622 VAL A CA    1 
ATOM   22851 C C     . VAL A 1 4622 ? 173.987 216.063 234.441 1.00 0.54  ? 4622 VAL A C     1 
ATOM   22852 O O     . VAL A 1 4622 ? 174.358 215.004 234.958 1.00 6.28  ? 4622 VAL A O     1 
ATOM   22853 C CB    . VAL A 1 4622 ? 173.275 215.619 232.053 1.00 3.68  ? 4622 VAL A CB    1 
ATOM   22854 C CG1   . VAL A 1 4622 ? 173.417 214.111 232.185 1.00 2.60  ? 4622 VAL A CG1   1 
ATOM   22855 C CG2   . VAL A 1 4622 ? 171.857 216.040 232.366 1.00 6.00  ? 4622 VAL A CG2   1 
ATOM   22856 N N     . ASP A 1 4623 ? 173.349 217.015 235.114 1.00 2.80  ? 4623 ASP A N     1 
ATOM   22857 C CA    . ASP A 1 4623 ? 172.942 216.862 236.502 1.00 2.54  ? 4623 ASP A CA    1 
ATOM   22858 C C     . ASP A 1 4623 ? 171.491 216.408 236.546 1.00 6.12  ? 4623 ASP A C     1 
ATOM   22859 O O     . ASP A 1 4623 ? 170.623 217.027 235.922 1.00 16.15 ? 4623 ASP A O     1 
ATOM   22860 C CB    . ASP A 1 4623 ? 173.105 218.172 237.271 1.00 2.54  ? 4623 ASP A CB    1 
ATOM   22861 C CG    . ASP A 1 4623 ? 174.550 218.591 237.403 1.00 5.65  ? 4623 ASP A CG    1 
ATOM   22862 O OD1   . ASP A 1 4623 ? 175.425 217.894 236.851 1.00 5.78  ? 4623 ASP A OD1   1 
ATOM   22863 O OD2   . ASP A 1 4623 ? 174.812 219.619 238.060 1.00 10.09 ? 4623 ASP A OD2   1 
ATOM   22864 N N     . PHE A 1 4624 ? 171.232 215.331 237.278 1.00 0.46  ? 4624 PHE A N     1 
ATOM   22865 C CA    . PHE A 1 4624 ? 169.897 214.764 237.377 1.00 2.00  ? 4624 PHE A CA    1 
ATOM   22866 C C     . PHE A 1 4624 ? 169.490 214.639 238.835 1.00 6.69  ? 4624 PHE A C     1 
ATOM   22867 O O     . PHE A 1 4624 ? 170.298 214.259 239.685 1.00 11.76 ? 4624 PHE A O     1 
ATOM   22868 C CB    . PHE A 1 4624 ? 169.821 213.389 236.712 1.00 9.01  ? 4624 PHE A CB    1 
ATOM   22869 C CG    . PHE A 1 4624 ? 169.383 213.427 235.277 1.00 11.42 ? 4624 PHE A CG    1 
ATOM   22870 C CD1   . PHE A 1 4624 ? 168.057 213.655 234.953 1.00 13.03 ? 4624 PHE A CD1   1 
ATOM   22871 C CD2   . PHE A 1 4624 ? 170.286 213.197 234.256 1.00 7.50  ? 4624 PHE A CD2   1 
ATOM   22872 C CE1   . PHE A 1 4624 ? 167.647 213.681 233.638 1.00 9.52  ? 4624 PHE A CE1   1 
ATOM   22873 C CE2   . PHE A 1 4624 ? 169.880 213.217 232.939 1.00 6.21  ? 4624 PHE A CE2   1 
ATOM   22874 C CZ    . PHE A 1 4624 ? 168.559 213.461 232.629 1.00 6.59  ? 4624 PHE A CZ    1 
ATOM   22875 N N     . GLU A 1 4625 ? 168.231 214.962 239.116 1.00 15.39 ? 4625 GLU A N     1 
ATOM   22876 C CA    . GLU A 1 4625 ? 167.638 214.699 240.420 1.00 11.30 ? 4625 GLU A CA    1 
ATOM   22877 C C     . GLU A 1 4625 ? 167.281 213.222 240.512 1.00 15.40 ? 4625 GLU A C     1 
ATOM   22878 O O     . GLU A 1 4625 ? 166.562 212.701 239.654 1.00 20.93 ? 4625 GLU A O     1 
ATOM   22879 C CB    . GLU A 1 4625 ? 166.395 215.565 240.620 1.00 13.82 ? 4625 GLU A CB    1 
ATOM   22880 C CG    . GLU A 1 4625 ? 166.604 216.821 241.450 1.00 15.52 ? 4625 GLU A CG    1 
ATOM   22881 C CD    . GLU A 1 4625 ? 166.945 216.530 242.899 1.00 22.28 ? 4625 GLU A CD    1 
ATOM   22882 O OE1   . GLU A 1 4625 ? 167.338 217.474 243.613 1.00 23.86 ? 4625 GLU A OE1   1 
ATOM   22883 O OE2   . GLU A 1 4625 ? 166.798 215.369 243.336 1.00 21.03 ? 4625 GLU A OE2   1 
ATOM   22884 N N     . ILE A 1 4626 ? 167.790 212.540 241.535 1.00 13.33 ? 4626 ILE A N     1 
ATOM   22885 C CA    . ILE A 1 4626 ? 167.459 211.134 241.736 1.00 12.92 ? 4626 ILE A CA    1 
ATOM   22886 C C     . ILE A 1 4626 ? 166.206 211.037 242.593 1.00 19.95 ? 4626 ILE A C     1 
ATOM   22887 O O     . ILE A 1 4626 ? 165.779 212.024 243.202 1.00 22.87 ? 4626 ILE A O     1 
ATOM   22888 C CB    . ILE A 1 4626 ? 168.625 210.360 242.371 1.00 16.75 ? 4626 ILE A CB    1 
ATOM   22889 C CG1   . ILE A 1 4626 ? 169.017 210.981 243.707 1.00 18.67 ? 4626 ILE A CG1   1 
ATOM   22890 C CG2   . ILE A 1 4626 ? 169.817 210.352 241.440 1.00 18.10 ? 4626 ILE A CG2   1 
ATOM   22891 C CD1   . ILE A 1 4626 ? 170.152 210.266 244.383 1.00 19.14 ? 4626 ILE A CD1   1 
ATOM   22892 N N     . ALA A 1 4627 ? 165.607 209.850 242.643 1.00 23.55 ? 4627 ALA A N     1 
ATOM   22893 C CA    . ALA A 1 4627 ? 164.422 209.636 243.457 1.00 24.23 ? 4627 ALA A CA    1 
ATOM   22894 C C     . ALA A 1 4627 ? 164.776 209.738 244.942 1.00 30.47 ? 4627 ALA A C     1 
ATOM   22895 O O     . ALA A 1 4627 ? 165.936 209.911 245.329 1.00 27.96 ? 4627 ALA A O     1 
ATOM   22896 C CB    . ALA A 1 4627 ? 163.791 208.286 243.130 1.00 23.69 ? 4627 ALA A CB    1 
ATOM   22897 N N     . THR A 1 4628 ? 163.754 209.618 245.788 1.00 37.06 ? 4628 THR A N     1 
ATOM   22898 C CA    . THR A 1 4628 ? 163.913 209.858 247.216 1.00 39.42 ? 4628 THR A CA    1 
ATOM   22899 C C     . THR A 1 4628 ? 164.558 208.697 247.962 1.00 39.46 ? 4628 THR A C     1 
ATOM   22900 O O     . THR A 1 4628 ? 164.879 208.850 249.145 1.00 39.53 ? 4628 THR A O     1 
ATOM   22901 C CB    . THR A 1 4628 ? 162.554 210.169 247.849 1.00 39.51 ? 4628 THR A CB    1 
ATOM   22902 O OG1   . THR A 1 4628 ? 162.728 210.453 249.242 1.00 36.61 ? 4628 THR A OG1   1 
ATOM   22903 C CG2   . THR A 1 4628 ? 161.612 208.986 247.691 1.00 38.14 ? 4628 THR A CG2   1 
ATOM   22904 N N     . LYS A 1 4629 ? 164.761 207.551 247.314 1.00 33.54 ? 4629 LYS A N     1 
ATOM   22905 C CA    . LYS A 1 4629 ? 165.286 206.366 247.980 1.00 35.95 ? 4629 LYS A CA    1 
ATOM   22906 C C     . LYS A 1 4629 ? 166.720 206.041 247.589 1.00 36.03 ? 4629 LYS A C     1 
ATOM   22907 O O     . LYS A 1 4629 ? 167.539 205.728 248.459 1.00 37.51 ? 4629 LYS A O     1 
ATOM   22908 C CB    . LYS A 1 4629 ? 164.380 205.160 247.692 1.00 38.24 ? 4629 LYS A CB    1 
ATOM   22909 C CG    . LYS A 1 4629 ? 162.921 205.380 248.064 1.00 38.58 ? 4629 LYS A CG    1 
ATOM   22910 C CD    . LYS A 1 4629 ? 161.990 204.566 247.180 1.00 37.52 ? 4629 LYS A CD    1 
ATOM   22911 C CE    . LYS A 1 4629 ? 162.174 204.913 245.711 1.00 35.63 ? 4629 LYS A CE    1 
ATOM   22912 N NZ    . LYS A 1 4629 ? 161.917 206.356 245.442 1.00 36.82 ? 4629 LYS A NZ    1 
ATOM   22913 N N     . GLU A 1 4630 ? 167.049 206.105 246.302 1.00 30.10 ? 4630 GLU A N     1 
ATOM   22914 C CA    . GLU A 1 4630 ? 168.394 205.770 245.860 1.00 25.56 ? 4630 GLU A CA    1 
ATOM   22915 C C     . GLU A 1 4630 ? 169.396 206.825 246.320 1.00 26.78 ? 4630 GLU A C     1 
ATOM   22916 O O     . GLU A 1 4630 ? 169.043 207.962 246.645 1.00 29.95 ? 4630 GLU A O     1 
ATOM   22917 C CB    . GLU A 1 4630 ? 168.445 205.633 244.338 1.00 28.37 ? 4630 GLU A CB    1 
ATOM   22918 C CG    . GLU A 1 4630 ? 167.769 204.385 243.790 1.00 31.35 ? 4630 GLU A CG    1 
ATOM   22919 C CD    . GLU A 1 4630 ? 166.281 204.570 243.569 1.00 32.43 ? 4630 GLU A CD    1 
ATOM   22920 O OE1   . GLU A 1 4630 ? 165.780 205.693 243.786 1.00 37.37 ? 4630 GLU A OE1   1 
ATOM   22921 O OE2   . GLU A 1 4630 ? 165.614 203.593 243.172 1.00 26.86 ? 4630 GLU A OE2   1 
ATOM   22922 N N     . ASP A 1 4631 ? 170.670 206.429 246.346 1.00 17.62 ? 4631 ASP A N     1 
ATOM   22923 C CA    . ASP A 1 4631 ? 171.743 207.325 246.741 1.00 10.05 ? 4631 ASP A CA    1 
ATOM   22924 C C     . ASP A 1 4631 ? 172.742 207.503 245.601 1.00 14.45 ? 4631 ASP A C     1 
ATOM   22925 O O     . ASP A 1 4631 ? 172.866 206.630 244.736 1.00 21.43 ? 4631 ASP A O     1 
ATOM   22926 C CB    . ASP A 1 4631 ? 172.477 206.802 247.982 1.00 15.87 ? 4631 ASP A CB    1 
ATOM   22927 C CG    . ASP A 1 4631 ? 172.905 205.357 247.840 1.00 22.17 ? 4631 ASP A CG    1 
ATOM   22928 O OD1   . ASP A 1 4631 ? 172.150 204.571 247.231 1.00 23.68 ? 4631 ASP A OD1   1 
ATOM   22929 O OD2   . ASP A 1 4631 ? 173.995 205.008 248.338 1.00 16.43 ? 4631 ASP A OD2   1 
ATOM   22930 N N     . PRO A 1 4632 ? 173.454 208.633 245.564 1.00 9.71  ? 4632 PRO A N     1 
ATOM   22931 C CA    . PRO A 1 4632 ? 174.391 208.877 244.454 1.00 8.52  ? 4632 PRO A CA    1 
ATOM   22932 C C     . PRO A 1 4632 ? 175.449 207.801 244.294 1.00 7.04  ? 4632 PRO A C     1 
ATOM   22933 O O     . PRO A 1 4632 ? 175.857 207.508 243.163 1.00 9.38  ? 4632 PRO A O     1 
ATOM   22934 C CB    . PRO A 1 4632 ? 175.035 210.223 244.821 1.00 9.99  ? 4632 PRO A CB    1 
ATOM   22935 C CG    . PRO A 1 4632 ? 174.252 210.776 245.974 1.00 13.62 ? 4632 PRO A CG    1 
ATOM   22936 C CD    . PRO A 1 4632 ? 173.112 209.869 246.284 1.00 14.74 ? 4632 PRO A CD    1 
ATOM   22937 N N     . ARG A 1 4633 ? 175.914 207.212 245.396 1.00 7.99  ? 4633 ARG A N     1 
ATOM   22938 C CA    . ARG A 1 4633 ? 176.995 206.235 245.324 1.00 3.30  ? 4633 ARG A CA    1 
ATOM   22939 C C     . ARG A 1 4633 ? 176.588 205.016 244.507 1.00 2.15  ? 4633 ARG A C     1 
ATOM   22940 O O     . ARG A 1 4633 ? 177.402 204.457 243.761 1.00 6.97  ? 4633 ARG A O     1 
ATOM   22941 C CB    . ARG A 1 4633 ? 177.412 205.826 246.736 1.00 6.89  ? 4633 ARG A CB    1 
ATOM   22942 C CG    . ARG A 1 4633 ? 178.441 206.746 247.371 1.00 4.29  ? 4633 ARG A CG    1 
ATOM   22943 C CD    . ARG A 1 4633 ? 179.166 206.066 248.521 1.00 6.24  ? 4633 ARG A CD    1 
ATOM   22944 N NE    . ARG A 1 4633 ? 178.428 204.925 249.050 1.00 16.81 ? 4633 ARG A NE    1 
ATOM   22945 C CZ    . ARG A 1 4633 ? 177.535 204.999 250.028 1.00 14.37 ? 4633 ARG A CZ    1 
ATOM   22946 N NH1   . ARG A 1 4633 ? 177.242 206.149 250.612 1.00 9.02  ? 4633 ARG A NH1   1 
ATOM   22947 N NH2   . ARG A 1 4633 ? 176.919 203.890 250.430 1.00 10.41 ? 4633 ARG A NH2   1 
ATOM   22948 N N     . SER A 1 4634 ? 175.336 204.579 244.645 1.00 6.22  ? 4634 SER A N     1 
ATOM   22949 C CA    . SER A 1 4634 ? 174.865 203.441 243.865 1.00 4.54  ? 4634 SER A CA    1 
ATOM   22950 C C     . SER A 1 4634 ? 174.832 203.772 242.378 1.00 7.18  ? 4634 SER A C     1 
ATOM   22951 O O     . SER A 1 4634 ? 175.179 202.932 241.539 1.00 12.69 ? 4634 SER A O     1 
ATOM   22952 C CB    . SER A 1 4634 ? 173.489 203.003 244.359 1.00 6.45  ? 4634 SER A CB    1 
ATOM   22953 O OG    . SER A 1 4634 ? 172.927 202.043 243.490 1.00 9.83  ? 4634 SER A OG    1 
ATOM   22954 N N     . PHE A 1 4635 ? 174.422 204.995 242.032 1.00 9.52  ? 4635 PHE A N     1 
ATOM   22955 C CA    . PHE A 1 4635 ? 174.497 205.443 240.645 1.00 7.19  ? 4635 PHE A CA    1 
ATOM   22956 C C     . PHE A 1 4635 ? 175.933 205.435 240.140 1.00 2.70  ? 4635 PHE A C     1 
ATOM   22957 O O     . PHE A 1 4635 ? 176.193 205.068 238.989 1.00 3.21  ? 4635 PHE A O     1 
ATOM   22958 C CB    . PHE A 1 4635 ? 173.906 206.845 240.510 1.00 5.29  ? 4635 PHE A CB    1 
ATOM   22959 C CG    . PHE A 1 4635 ? 172.412 206.875 240.464 1.00 3.35  ? 4635 PHE A CG    1 
ATOM   22960 C CD1   . PHE A 1 4635 ? 171.665 206.697 241.613 1.00 8.92  ? 4635 PHE A CD1   1 
ATOM   22961 C CD2   . PHE A 1 4635 ? 171.753 207.108 239.273 1.00 1.07  ? 4635 PHE A CD2   1 
ATOM   22962 C CE1   . PHE A 1 4635 ? 170.290 206.731 241.570 1.00 12.08 ? 4635 PHE A CE1   1 
ATOM   22963 C CE2   . PHE A 1 4635 ? 170.379 207.145 239.225 1.00 7.49  ? 4635 PHE A CE2   1 
ATOM   22964 C CZ    . PHE A 1 4635 ? 169.646 206.956 240.375 1.00 14.88 ? 4635 PHE A CZ    1 
ATOM   22965 N N     . TYR A 1 4636 ? 176.876 205.860 240.981 1.00 9.22  ? 4636 TYR A N     1 
ATOM   22966 C CA    . TYR A 1 4636 ? 178.268 205.913 240.551 1.00 7.00  ? 4636 TYR A CA    1 
ATOM   22967 C C     . TYR A 1 4636 ? 178.830 204.514 240.329 1.00 9.99  ? 4636 TYR A C     1 
ATOM   22968 O O     . TYR A 1 4636 ? 179.590 204.286 239.381 1.00 7.53  ? 4636 TYR A O     1 
ATOM   22969 C CB    . TYR A 1 4636 ? 179.108 206.675 241.577 1.00 3.58  ? 4636 TYR A CB    1 
ATOM   22970 C CG    . TYR A 1 4636 ? 178.631 208.087 241.827 1.00 5.36  ? 4636 TYR A CG    1 
ATOM   22971 C CD1   . TYR A 1 4636 ? 177.951 208.796 240.847 1.00 3.39  ? 4636 TYR A CD1   1 
ATOM   22972 C CD2   . TYR A 1 4636 ? 178.859 208.711 243.043 1.00 3.59  ? 4636 TYR A CD2   1 
ATOM   22973 C CE1   . TYR A 1 4636 ? 177.508 210.082 241.074 1.00 3.44  ? 4636 TYR A CE1   1 
ATOM   22974 C CE2   . TYR A 1 4636 ? 178.423 209.998 243.278 1.00 4.13  ? 4636 TYR A CE2   1 
ATOM   22975 C CZ    . TYR A 1 4636 ? 177.748 210.679 242.290 1.00 3.68  ? 4636 TYR A CZ    1 
ATOM   22976 O OH    . TYR A 1 4636 ? 177.312 211.963 242.519 1.00 8.02  ? 4636 TYR A OH    1 
ATOM   22977 N N     . GLU A 1 4637 ? 178.472 203.564 241.192 1.00 4.29  ? 4637 GLU A N     1 
ATOM   22978 C CA    . GLU A 1 4637 ? 179.022 202.218 241.090 1.00 1.74  ? 4637 GLU A CA    1 
ATOM   22979 C C     . GLU A 1 4637 ? 178.278 201.332 240.104 1.00 4.24  ? 4637 GLU A C     1 
ATOM   22980 O O     . GLU A 1 4637 ? 178.815 200.293 239.705 1.00 8.07  ? 4637 GLU A O     1 
ATOM   22981 C CB    . GLU A 1 4637 ? 179.055 201.540 242.464 1.00 3.13  ? 4637 GLU A CB    1 
ATOM   22982 C CG    . GLU A 1 4637 ? 177.698 201.267 243.072 1.00 7.33  ? 4637 GLU A CG    1 
ATOM   22983 C CD    . GLU A 1 4637 ? 177.806 200.658 244.455 1.00 16.28 ? 4637 GLU A CD    1 
ATOM   22984 O OE1   . GLU A 1 4637 ? 178.943 200.474 244.935 1.00 14.06 ? 4637 GLU A OE1   1 
ATOM   22985 O OE2   . GLU A 1 4637 ? 176.756 200.361 245.061 1.00 15.03 ? 4637 GLU A OE2   1 
ATOM   22986 N N     . ARG A 1 4638 ? 177.075 201.714 239.690 1.00 3.69  ? 4638 ARG A N     1 
ATOM   22987 C CA    . ARG A 1 4638 ? 176.343 200.952 238.691 1.00 0.66  ? 4638 ARG A CA    1 
ATOM   22988 C C     . ARG A 1 4638 ? 176.684 201.382 237.268 1.00 2.09  ? 4638 ARG A C     1 
ATOM   22989 O O     . ARG A 1 4638 ? 176.157 200.802 236.313 1.00 6.71  ? 4638 ARG A O     1 
ATOM   22990 C CB    . ARG A 1 4638 ? 174.837 201.077 238.959 1.00 1.85  ? 4638 ARG A CB    1 
ATOM   22991 C CG    . ARG A 1 4638 ? 173.964 200.117 238.179 1.00 6.45  ? 4638 ARG A CG    1 
ATOM   22992 C CD    . ARG A 1 4638 ? 172.558 200.071 238.725 1.00 8.87  ? 4638 ARG A CD    1 
ATOM   22993 N NE    . ARG A 1 4638 ? 172.455 199.169 239.864 1.00 0.00  ? 4638 ARG A NE    1 
ATOM   22994 C CZ    . ARG A 1 4638 ? 171.483 198.283 240.026 1.00 5.51  ? 4638 ARG A CZ    1 
ATOM   22995 N NH1   . ARG A 1 4638 ? 170.507 198.160 239.143 1.00 4.98  ? 4638 ARG A NH1   1 
ATOM   22996 N NH2   . ARG A 1 4638 ? 171.490 197.503 241.102 1.00 11.84 ? 4638 ARG A NH2   1 
ATOM   22997 N N     . GLY A 1 4639 ? 177.568 202.362 237.103 1.00 0.52  ? 4639 GLY A N     1 
ATOM   22998 C CA    . GLY A 1 4639 ? 177.981 202.782 235.779 1.00 4.87  ? 4639 GLY A CA    1 
ATOM   22999 C C     . GLY A 1 4639 ? 176.944 203.561 235.006 1.00 6.86  ? 4639 GLY A C     1 
ATOM   23000 O O     . GLY A 1 4639 ? 176.951 203.533 233.773 1.00 10.93 ? 4639 GLY A O     1 
ATOM   23001 N N     . VAL A 1 4640 ? 176.045 204.260 235.699 1.00 0.76  ? 4640 VAL A N     1 
ATOM   23002 C CA    . VAL A 1 4640 ? 174.993 205.006 235.024 1.00 0.00  ? 4640 VAL A CA    1 
ATOM   23003 C C     . VAL A 1 4640 ? 175.597 206.154 234.222 1.00 0.35  ? 4640 VAL A C     1 
ATOM   23004 O O     . VAL A 1 4640 ? 176.459 206.900 234.704 1.00 2.09  ? 4640 VAL A O     1 
ATOM   23005 C CB    . VAL A 1 4640 ? 173.966 205.517 236.050 1.00 0.00  ? 4640 VAL A CB    1 
ATOM   23006 C CG1   . VAL A 1 4640 ? 172.826 206.236 235.355 1.00 2.18  ? 4640 VAL A CG1   1 
ATOM   23007 C CG2   . VAL A 1 4640 ? 173.443 204.364 236.888 1.00 2.52  ? 4640 VAL A CG2   1 
ATOM   23008 N N     . ALA A 1 4641 ? 175.143 206.291 232.980 1.00 2.51  ? 4641 ALA A N     1 
ATOM   23009 C CA    . ALA A 1 4641 ? 175.610 207.344 232.087 1.00 0.00  ? 4641 ALA A CA    1 
ATOM   23010 C C     . ALA A 1 4641 ? 174.544 207.574 231.023 1.00 0.00  ? 4641 ALA A C     1 
ATOM   23011 O O     . ALA A 1 4641 ? 173.575 206.819 230.913 1.00 8.89  ? 4641 ALA A O     1 
ATOM   23012 C CB    . ALA A 1 4641 ? 176.959 206.984 231.461 1.00 0.00  ? 4641 ALA A CB    1 
ATOM   23013 N N     . VAL A 1 4642 ? 174.730 208.632 230.240 1.00 0.93  ? 4642 VAL A N     1 
ATOM   23014 C CA    . VAL A 1 4642 ? 173.853 208.959 229.121 1.00 1.35  ? 4642 VAL A CA    1 
ATOM   23015 C C     . VAL A 1 4642 ? 174.648 208.759 227.841 1.00 4.95  ? 4642 VAL A C     1 
ATOM   23016 O O     . VAL A 1 4642 ? 175.802 209.195 227.746 1.00 5.63  ? 4642 VAL A O     1 
ATOM   23017 C CB    . VAL A 1 4642 ? 173.308 210.392 229.214 1.00 3.48  ? 4642 VAL A CB    1 
ATOM   23018 C CG1   . VAL A 1 4642 ? 172.277 210.636 228.127 1.00 3.01  ? 4642 VAL A CG1   1 
ATOM   23019 C CG2   . VAL A 1 4642 ? 172.705 210.638 230.582 1.00 3.92  ? 4642 VAL A CG2   1 
ATOM   23020 N N     . LEU A 1 4643 ? 174.044 208.086 226.867 1.00 8.83  ? 4643 LEU A N     1 
ATOM   23021 C CA    . LEU A 1 4643 ? 174.700 207.756 225.610 1.00 7.92  ? 4643 LEU A CA    1 
ATOM   23022 C C     . LEU A 1 4643 ? 173.936 208.380 224.451 1.00 9.11  ? 4643 LEU A C     1 
ATOM   23023 O O     . LEU A 1 4643 ? 172.704 208.295 224.396 1.00 9.13  ? 4643 LEU A O     1 
ATOM   23024 C CB    . LEU A 1 4643 ? 174.794 206.240 225.432 1.00 7.95  ? 4643 LEU A CB    1 
ATOM   23025 C CG    . LEU A 1 4643 ? 176.111 205.567 225.819 1.00 0.95  ? 4643 LEU A CG    1 
ATOM   23026 C CD1   . LEU A 1 4643 ? 176.515 205.907 227.238 1.00 0.98  ? 4643 LEU A CD1   1 
ATOM   23027 C CD2   . LEU A 1 4643 ? 175.965 204.072 225.670 1.00 3.98  ? 4643 LEU A CD2   1 
ATOM   23028 N N     . CYS A 1 4644 ? 174.669 209.013 223.533 1.00 9.27  ? 4644 CYS A N     1 
ATOM   23029 C CA    . CYS A 1 4644 ? 174.047 209.594 222.350 1.00 7.18  ? 4644 CYS A CA    1 
ATOM   23030 C C     . CYS A 1 4644 ? 173.674 208.537 221.318 1.00 8.57  ? 4644 CYS A C     1 
ATOM   23031 O O     . CYS A 1 4644 ? 172.638 208.663 220.657 1.00 5.79  ? 4644 CYS A O     1 
ATOM   23032 C CB    . CYS A 1 4644 ? 174.977 210.634 221.721 1.00 6.82  ? 4644 CYS A CB    1 
ATOM   23033 S SG    . CYS A 1 4644 ? 175.681 211.830 222.876 1.00 0.00  ? 4644 CYS A SG    1 
ATOM   23034 N N     . THR A 1 4645 ? 174.494 207.502 221.164 1.00 13.88 ? 4645 THR A N     1 
ATOM   23035 C CA    . THR A 1 4645 ? 174.213 206.433 220.212 1.00 9.75  ? 4645 THR A CA    1 
ATOM   23036 C C     . THR A 1 4645 ? 173.918 205.125 220.937 1.00 7.23  ? 4645 THR A C     1 
ATOM   23037 O O     . THR A 1 4645 ? 174.656 204.719 221.832 0.00 8.46  ? 4645 THR A O     1 
ATOM   23038 C CB    . THR A 1 4645 ? 175.390 206.216 219.243 1.00 9.25  ? 4645 THR A CB    1 
ATOM   23039 O OG1   . THR A 1 4645 ? 175.635 207.420 218.507 1.00 10.42 ? 4645 THR A OG1   1 
ATOM   23040 C CG2   . THR A 1 4645 ? 175.083 205.088 218.272 1.00 11.07 ? 4645 THR A CG2   1 
HETATM 23041 P PB    . ADP B 2 .    ? 204.134 218.648 228.673 1.00 6.63  ? 4701 ADP A PB    1 
HETATM 23042 O O1B   . ADP B 2 .    ? 205.519 218.305 229.160 1.00 3.67  ? 4701 ADP A O1B   1 
HETATM 23043 O O2B   . ADP B 2 .    ? 203.056 217.716 229.157 1.00 3.75  ? 4701 ADP A O2B   1 
HETATM 23044 O O3B   . ADP B 2 .    ? 204.038 218.991 227.209 1.00 7.20  ? 4701 ADP A O3B   1 
HETATM 23045 P PA    . ADP B 2 .    ? 204.894 221.182 229.601 1.00 0.00  ? 4701 ADP A PA    1 
HETATM 23046 O O1A   . ADP B 2 .    ? 205.737 220.858 230.804 1.00 0.00  ? 4701 ADP A O1A   1 
HETATM 23047 O O2A   . ADP B 2 .    ? 205.541 221.424 228.262 1.00 9.23  ? 4701 ADP A O2A   1 
HETATM 23048 O O3A   . ADP B 2 .    ? 203.794 220.025 229.422 1.00 12.68 ? 4701 ADP A O3A   1 
HETATM 23049 O "O5'" . ADP B 2 .    ? 203.959 222.441 229.949 1.00 0.00  ? 4701 ADP A "O5'" 1 
HETATM 23050 C "C5'" . ADP B 2 .    ? 203.817 223.505 229.013 1.00 2.81  ? 4701 ADP A "C5'" 1 
HETATM 23051 C "C4'" . ADP B 2 .    ? 203.584 224.816 229.748 1.00 5.38  ? 4701 ADP A "C4'" 1 
HETATM 23052 O "O4'" . ADP B 2 .    ? 202.502 224.699 230.671 1.00 6.05  ? 4701 ADP A "O4'" 1 
HETATM 23053 C "C3'" . ADP B 2 .    ? 204.810 225.210 230.555 1.00 1.97  ? 4701 ADP A "C3'" 1 
HETATM 23054 O "O3'" . ADP B 2 .    ? 205.423 226.368 229.988 1.00 0.02  ? 4701 ADP A "O3'" 1 
HETATM 23055 C "C2'" . ADP B 2 .    ? 204.307 225.525 231.946 1.00 2.23  ? 4701 ADP A "C2'" 1 
HETATM 23056 O "O2'" . ADP B 2 .    ? 204.738 226.828 232.345 1.00 5.22  ? 4701 ADP A "O2'" 1 
HETATM 23057 C "C1'" . ADP B 2 .    ? 202.794 225.470 231.837 1.00 5.00  ? 4701 ADP A "C1'" 1 
HETATM 23058 N N9    . ADP B 2 .    ? 202.216 224.850 233.054 1.00 3.62  ? 4701 ADP A N9    1 
HETATM 23059 C C8    . ADP B 2 .    ? 201.848 223.566 233.200 1.00 1.28  ? 4701 ADP A C8    1 
HETATM 23060 N N7    . ADP B 2 .    ? 201.354 223.342 234.443 1.00 1.72  ? 4701 ADP A N7    1 
HETATM 23061 C C5    . ADP B 2 .    ? 201.402 224.505 235.116 1.00 2.36  ? 4701 ADP A C5    1 
HETATM 23062 C C6    . ADP B 2 .    ? 201.039 224.977 236.472 1.00 1.14  ? 4701 ADP A C6    1 
HETATM 23063 N N6    . ADP B 2 .    ? 200.508 224.139 237.392 1.00 1.99  ? 4701 ADP A N6    1 
HETATM 23064 N N1    . ADP B 2 .    ? 201.254 226.276 236.762 1.00 3.16  ? 4701 ADP A N1    1 
HETATM 23065 C C2    . ADP B 2 .    ? 201.780 227.127 235.865 1.00 3.60  ? 4701 ADP A C2    1 
HETATM 23066 N N3    . ADP B 2 .    ? 202.132 226.769 234.620 1.00 4.81  ? 4701 ADP A N3    1 
HETATM 23067 C C4    . ADP B 2 .    ? 201.970 225.496 234.193 1.00 4.21  ? 4701 ADP A C4    1 
HETATM 23068 P PG    . ATP C 3 .    ? 204.367 235.480 196.817 1.00 17.90 ? 4702 ATP A PG    1 
HETATM 23069 O O1G   . ATP C 3 .    ? 204.332 234.736 195.529 1.00 5.73  ? 4702 ATP A O1G   1 
HETATM 23070 O O2G   . ATP C 3 .    ? 203.166 236.399 197.034 1.00 13.41 ? 4702 ATP A O2G   1 
HETATM 23071 O O3G   . ATP C 3 .    ? 204.536 234.582 198.039 1.00 7.16  ? 4702 ATP A O3G   1 
HETATM 23072 P PB    . ATP C 3 .    ? 206.130 237.721 197.650 1.00 12.16 ? 4702 ATP A PB    1 
HETATM 23073 O O1B   . ATP C 3 .    ? 207.487 238.091 197.204 1.00 11.02 ? 4702 ATP A O1B   1 
HETATM 23074 O O2B   . ATP C 3 .    ? 205.954 237.425 199.136 1.00 3.71  ? 4702 ATP A O2B   1 
HETATM 23075 O O3B   . ATP C 3 .    ? 205.616 236.452 196.862 1.00 9.70  ? 4702 ATP A O3B   1 
HETATM 23076 P PA    . ATP C 3 .    ? 205.020 240.348 196.862 1.00 0.00  ? 4702 ATP A PA    1 
HETATM 23077 O O1A   . ATP C 3 .    ? 205.106 241.240 198.034 1.00 7.36  ? 4702 ATP A O1A   1 
HETATM 23078 O O2A   . ATP C 3 .    ? 206.111 240.548 195.814 1.00 6.81  ? 4702 ATP A O2A   1 
HETATM 23079 O O3A   . ATP C 3 .    ? 205.034 238.812 197.271 1.00 0.31  ? 4702 ATP A O3A   1 
HETATM 23080 O "O5'" . ATP C 3 .    ? 203.619 240.508 196.157 1.00 0.00  ? 4702 ATP A "O5'" 1 
HETATM 23081 C "C5'" . ATP C 3 .    ? 203.000 241.802 196.011 1.00 1.82  ? 4702 ATP A "C5'" 1 
HETATM 23082 C "C4'" . ATP C 3 .    ? 202.583 241.983 194.573 1.00 2.29  ? 4702 ATP A "C4'" 1 
HETATM 23083 O "O4'" . ATP C 3 .    ? 201.403 242.816 194.516 1.00 1.02  ? 4702 ATP A "O4'" 1 
HETATM 23084 C "C3'" . ATP C 3 .    ? 203.616 242.669 193.683 1.00 1.06  ? 4702 ATP A "C3'" 1 
HETATM 23085 O "O3'" . ATP C 3 .    ? 203.530 242.206 192.341 1.00 3.39  ? 4702 ATP A "O3'" 1 
HETATM 23086 C "C2'" . ATP C 3 .    ? 203.222 244.140 193.798 1.00 0.00  ? 4702 ATP A "C2'" 1 
HETATM 23087 O "O2'" . ATP C 3 .    ? 203.634 244.890 192.662 1.00 3.44  ? 4702 ATP A "O2'" 1 
HETATM 23088 C "C1'" . ATP C 3 .    ? 201.697 244.035 193.858 1.00 0.00  ? 4702 ATP A "C1'" 1 
HETATM 23089 N N9    . ATP C 3 .    ? 201.057 245.128 194.584 1.00 1.67  ? 4702 ATP A N9    1 
HETATM 23090 C C8    . ATP C 3 .    ? 200.172 246.043 194.077 1.00 8.82  ? 4702 ATP A C8    1 
HETATM 23091 N N7    . ATP C 3 .    ? 199.763 246.933 194.947 1.00 2.36  ? 4702 ATP A N7    1 
HETATM 23092 C C5    . ATP C 3 .    ? 200.427 246.581 196.111 1.00 0.53  ? 4702 ATP A C5    1 
HETATM 23093 C C6    . ATP C 3 .    ? 200.424 247.129 197.408 1.00 0.40  ? 4702 ATP A C6    1 
HETATM 23094 N N6    . ATP C 3 .    ? 199.705 248.198 197.762 1.00 0.86  ? 4702 ATP A N6    1 
HETATM 23095 N N1    . ATP C 3 .    ? 201.199 246.538 198.340 1.00 5.88  ? 4702 ATP A N1    1 
HETATM 23096 C C2    . ATP C 3 .    ? 201.921 245.470 197.993 1.00 1.16  ? 4702 ATP A C2    1 
HETATM 23097 N N3    . ATP C 3 .    ? 202.006 244.867 196.807 1.00 0.95  ? 4702 ATP A N3    1 
HETATM 23098 C C4    . ATP C 3 .    ? 201.230 245.472 195.903 1.00 2.22  ? 4702 ATP A C4    1 
HETATM 23099 P PB    . ADP D 2 .    ? 206.143 219.606 171.265 1.00 4.24  ? 4703 ADP A PB    1 
HETATM 23100 O O1B   . ADP D 2 .    ? 206.860 220.928 171.207 1.00 7.38  ? 4703 ADP A O1B   1 
HETATM 23101 O O2B   . ADP D 2 .    ? 204.689 219.715 171.647 1.00 11.77 ? 4703 ADP A O2B   1 
HETATM 23102 O O3B   . ADP D 2 .    ? 206.892 218.523 171.999 1.00 13.27 ? 4703 ADP A O3B   1 
HETATM 23103 P PA    . ADP D 2 .    ? 207.296 219.379 168.697 1.00 8.56  ? 4703 ADP A PA    1 
HETATM 23104 O O1A   . ADP D 2 .    ? 208.494 218.560 169.109 1.00 10.78 ? 4703 ADP A O1A   1 
HETATM 23105 O O2A   . ADP D 2 .    ? 207.441 220.868 168.517 1.00 7.96  ? 4703 ADP A O2A   1 
HETATM 23106 O O3A   . ADP D 2 .    ? 206.102 219.091 169.740 1.00 10.50 ? 4703 ADP A O3A   1 
HETATM 23107 O "O5'" . ADP D 2 .    ? 206.733 218.763 167.323 1.00 11.74 ? 4703 ADP A "O5'" 1 
HETATM 23108 C "C5'" . ADP D 2 .    ? 205.480 219.170 166.779 1.00 5.86  ? 4703 ADP A "C5'" 1 
HETATM 23109 C "C4'" . ADP D 2 .    ? 205.347 218.560 165.391 1.00 7.02  ? 4703 ADP A "C4'" 1 
HETATM 23110 O "O4'" . ADP D 2 .    ? 204.333 219.227 164.638 1.00 5.98  ? 4703 ADP A "O4'" 1 
HETATM 23111 C "C3'" . ADP D 2 .    ? 206.644 218.706 164.612 1.00 7.17  ? 4703 ADP A "C3'" 1 
HETATM 23112 O "O3'" . ADP D 2 .    ? 207.278 217.433 164.462 1.00 5.78  ? 4703 ADP A "O3'" 1 
HETATM 23113 C "C2'" . ADP D 2 .    ? 206.253 219.251 163.255 1.00 8.75  ? 4703 ADP A "C2'" 1 
HETATM 23114 O "O2'" . ADP D 2 .    ? 206.710 218.381 162.217 1.00 16.37 ? 4703 ADP A "O2'" 1 
HETATM 23115 C "C1'" . ADP D 2 .    ? 204.736 219.316 163.270 1.00 8.47  ? 4703 ADP A "C1'" 1 
HETATM 23116 N N9    . ADP D 2 .    ? 204.306 220.592 162.650 1.00 12.43 ? 4703 ADP A N9    1 
HETATM 23117 C C8    . ADP D 2 .    ? 204.866 221.159 161.564 1.00 11.84 ? 4703 ADP A C8    1 
HETATM 23118 N N7    . ADP D 2 .    ? 204.243 222.318 161.239 1.00 8.53  ? 4703 ADP A N7    1 
HETATM 23119 C C5    . ADP D 2 .    ? 203.254 222.502 162.130 1.00 10.49 ? 4703 ADP A C5    1 
HETATM 23120 C C6    . ADP D 2 .    ? 202.216 223.527 162.369 1.00 10.72 ? 4703 ADP A C6    1 
HETATM 23121 N N6    . ADP D 2 .    ? 202.104 224.609 161.563 1.00 9.46  ? 4703 ADP A N6    1 
HETATM 23122 N N1    . ADP D 2 .    ? 201.382 223.343 163.416 1.00 11.37 ? 4703 ADP A N1    1 
HETATM 23123 C C2    . ADP D 2 .    ? 201.479 222.269 164.220 1.00 7.00  ? 4703 ADP A C2    1 
HETATM 23124 N N3    . ADP D 2 .    ? 202.399 221.302 164.064 1.00 3.87  ? 4703 ADP A N3    1 
HETATM 23125 C C4    . ADP D 2 .    ? 203.296 221.360 163.054 1.00 9.02  ? 4703 ADP A C4    1 
HETATM 23126 P PB    . ADP E 2 .    ? 213.394 188.406 174.535 1.00 0.59  ? 4704 ADP A PB    1 
HETATM 23127 O O1B   . ADP E 2 .    ? 214.516 189.313 174.102 1.00 9.08  ? 4704 ADP A O1B   1 
HETATM 23128 O O2B   . ADP E 2 .    ? 212.023 188.895 174.147 1.00 11.43 ? 4704 ADP A O2B   1 
HETATM 23129 O O3B   . ADP E 2 .    ? 213.496 187.916 175.957 1.00 2.12  ? 4704 ADP A O3B   1 
HETATM 23130 P PA    . ADP E 2 .    ? 215.082 186.530 173.341 1.00 0.00  ? 4704 ADP A PA    1 
HETATM 23131 O O1A   . ADP E 2 .    ? 215.548 187.167 172.060 1.00 0.00  ? 4704 ADP A O1A   1 
HETATM 23132 O O2A   . ADP E 2 .    ? 215.912 186.659 174.593 1.00 8.71  ? 4704 ADP A O2A   1 
HETATM 23133 O O3A   . ADP E 2 .    ? 213.603 187.079 173.651 1.00 1.03  ? 4704 ADP A O3A   1 
HETATM 23134 O "O5'" . ADP E 2 .    ? 214.841 184.963 173.065 1.00 8.50  ? 4704 ADP A "O5'" 1 
HETATM 23135 C "C5'" . ADP E 2 .    ? 215.957 184.080 172.967 1.00 11.46 ? 4704 ADP A "C5'" 1 
HETATM 23136 C "C4'" . ADP E 2 .    ? 215.508 182.709 172.481 1.00 7.20  ? 4704 ADP A "C4'" 1 
HETATM 23137 O "O4'" . ADP E 2 .    ? 214.277 182.805 171.765 1.00 4.07  ? 4704 ADP A "O4'" 1 
HETATM 23138 C "C3'" . ADP E 2 .    ? 216.530 182.103 171.534 1.00 8.24  ? 4704 ADP A "C3'" 1 
HETATM 23139 O "O3'" . ADP E 2 .    ? 217.166 180.980 172.149 1.00 10.36 ? 4704 ADP A "O3'" 1 
HETATM 23140 C "C2'" . ADP E 2 .    ? 215.746 181.651 170.320 1.00 3.82  ? 4704 ADP A "C2'" 1 
HETATM 23141 O "O2'" . ADP E 2 .    ? 215.964 180.258 170.078 1.00 7.59  ? 4704 ADP A "O2'" 1 
HETATM 23142 C "C1'" . ADP E 2 .    ? 214.289 181.892 170.668 1.00 6.90  ? 4704 ADP A "C1'" 1 
HETATM 23143 N N9    . ADP E 2 .    ? 213.564 182.456 169.505 1.00 6.67  ? 4704 ADP A N9    1 
HETATM 23144 C C8    . ADP E 2 .    ? 213.223 183.743 169.330 1.00 2.41  ? 4704 ADP A C8    1 
HETATM 23145 N N7    . ADP E 2 .    ? 212.560 183.918 168.159 1.00 2.29  ? 4704 ADP A N7    1 
HETATM 23146 C C5    . ADP E 2 .    ? 212.467 182.716 167.566 1.00 0.46  ? 4704 ADP A C5    1 
HETATM 23147 C C6    . ADP E 2 .    ? 211.893 182.186 166.312 1.00 7.23  ? 4704 ADP A C6    1 
HETATM 23148 N N6    . ADP E 2 .    ? 211.265 182.999 165.431 1.00 10.67 ? 4704 ADP A N6    1 
HETATM 23149 N N1    . ADP E 2 .    ? 212.015 180.864 166.078 1.00 7.75  ? 4704 ADP A N1    1 
HETATM 23150 C C2    . ADP E 2 .    ? 212.635 180.041 166.940 1.00 1.41  ? 4704 ADP A C2    1 
HETATM 23151 N N3    . ADP E 2 .    ? 213.179 180.453 168.095 1.00 2.09  ? 4704 ADP A N3    1 
HETATM 23152 C C4    . ADP E 2 .    ? 213.128 181.755 168.458 1.00 3.91  ? 4704 ADP A C4    1 
# 
